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*** 7MLM completo ***elNémo ID: 240324204016499480Job options:ID = 240324204016499480 JOBID = 7MLM completo USERID = helen PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:
HEADER 7MLM completo
HEADER IMMUNE SYSTEM 28-APR-21 7MLM
TITLE CRYSTAL STRUCTURE OF MOUSE TLR4/MD-2 IN COMPLEX WITH SULFATIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TOLL-LIKE RECEPTOR 4,VARIABLE LYMPHOCYTE RECEPTOR B;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.2.6;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: LYMPHOCYTE ANTIGEN 96;
COMPND 8 CHAIN: C;
COMPND 9 SYNONYM: LY-96,ESOP-1,PROTEIN MD-2;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, EPTATRETUS BURGERI;
SOURCE 3 ORGANISM_COMMON: MOUSE, INSHORE HAGFISH;
SOURCE 4 ORGANISM_TAXID: 10090, 7764;
SOURCE 5 GENE: TLR4, LPS, VLRB;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE (BTI-TN-5B1-4);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 GENE: LY96, ESOP1, MD2;
SOURCE 14 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 16 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE (BTI-TN-5B1-4)
KEYWDS INNATE IMMUNITY, ENDOGENOUS LIGANDS, TOLL-LIKE RECEPTORS, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SU,B.BEUTLER
REVDAT 3 18-OCT-23 7MLM 1 REMARK
REVDAT 2 25-AUG-21 7MLM 1 JRNL
REVDAT 1 28-JUL-21 7MLM 0
JRNL AUTH L.SU,M.ATHAMNA,Y.WANG,J.WANG,M.FREUDENBERG,T.YUE,J.WANG,
JRNL AUTH 2 E.M.Y.MORESCO,H.HE,T.ZOR,B.BEUTLER
JRNL TITL SULFATIDES ARE ENDOGENOUS LIGANDS FOR THE TLR4-MD-2 COMPLEX.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 118 2021
JRNL REFN ESSN 1091-6490
JRNL PMID 34290146
JRNL DOI 10.1073/PNAS.2105316118
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.15.2_3472
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 75.1
REMARK 3 NUMBER OF REFLECTIONS : 46679
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.280
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 46.3960 - 5.0678 0.98 4368 196 0.2145 0.2349
REMARK 3 2 5.0678 - 4.0232 1.00 4302 192 0.1612 0.1809
REMARK 3 3 4.0232 - 3.5149 0.98 4210 188 0.1694 0.2068
REMARK 3 4 3.5149 - 3.1936 1.00 4224 190 0.2137 0.2591
REMARK 3 5 3.1936 - 2.9647 1.00 4222 189 0.2243 0.2612
REMARK 3 6 2.9647 - 2.7899 0.98 4150 186 0.2414 0.3086
REMARK 3 7 2.7899 - 2.6502 0.97 4142 184 0.2450 0.2518
REMARK 3 8 2.6502 - 2.5349 0.93 3941 177 0.2491 0.3074
REMARK 3 9 2.5349 - 2.4373 0.77 3233 145 0.2497 0.2611
REMARK 3 10 2.4373 - 2.3532 0.57 2415 108 0.2536 0.2838
REMARK 3 11 2.3532 - 2.2796 0.43 1813 81 0.2497 0.3046
REMARK 3 12 2.2796 - 2.2145 0.35 1466 66 0.2454 0.2764
REMARK 3 13 2.2145 - 2.1562 0.29 1219 55 0.2364 0.2697
REMARK 3 14 2.1562 - 2.1040 0.23 974 43 0.2403 0.3793
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 27:59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.317 47.573 12.060
REMARK 3 T TENSOR
REMARK 3 T11: 0.2034 T22: 0.5249
REMARK 3 T33: 0.6422 T12: -0.0122
REMARK 3 T13: 0.1045 T23: -0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 0.9034 L22: 0.0628
REMARK 3 L33: 2.4824 L12: 0.0027
REMARK 3 L13: -1.4726 L23: -0.0748
REMARK 3 S TENSOR
REMARK 3 S11: 0.0876 S12: 0.0045 S13: 0.1946
REMARK 3 S21: 0.0123 S22: -0.0021 S23: -0.3738
REMARK 3 S31: -0.1150 S32: 0.6806 S33: -0.0582
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: ( CHAIN A AND RESID 60:260 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.899 46.765 8.321
REMARK 3 T TENSOR
REMARK 3 T11: 0.1599 T22: 0.2153
REMARK 3 T33: 0.2109 T12: 0.0381
REMARK 3 T13: 0.1089 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.7332 L22: 1.1305
REMARK 3 L33: 1.0863 L12: 0.0002
REMARK 3 L13: 0.2367 L23: 0.3294
REMARK 3 S TENSOR
REMARK 3 S11: 0.0414 S12: 0.2357 S13: 0.1193
REMARK 3 S21: -0.0836 S22: -0.0720 S23: 0.1056
REMARK 3 S31: -0.1074 S32: -0.0469 S33: 0.0195
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: ( CHAIN A AND RESID 261:346 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.729 19.655 2.163
REMARK 3 T TENSOR
REMARK 3 T11: 0.3794 T22: 0.3692
REMARK 3 T33: 0.3511 T12: -0.0679
REMARK 3 T13: 0.0959 T23: -0.1411
REMARK 3 L TENSOR
REMARK 3 L11: 0.8566 L22: 0.9934
REMARK 3 L33: 0.7670 L12: -0.3845
REMARK 3 L13: 0.0171 L23: 0.3322
REMARK 3 S TENSOR
REMARK 3 S11: -0.1259 S12: 0.0607 S13: -0.1890
REMARK 3 S21: 0.1461 S22: -0.1229 S23: 0.5100
REMARK 3 S31: 0.5188 S32: -0.4672 S33: 0.1626
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: ( CHAIN A AND RESID 347:433 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.116 9.087 -10.397
REMARK 3 T TENSOR
REMARK 3 T11: 0.5263 T22: 0.1047
REMARK 3 T33: 0.0500 T12: 0.0104
REMARK 3 T13: 0.1279 T23: -0.2605
REMARK 3 L TENSOR
REMARK 3 L11: 0.3459 L22: 0.6458
REMARK 3 L33: 0.7694 L12: -0.2932
REMARK 3 L13: -0.1219 L23: 0.3317
REMARK 3 S TENSOR
REMARK 3 S11: -0.4523 S12: 0.1689 S13: -0.1303
REMARK 3 S21: 0.4127 S22: 0.1330 S23: 0.1743
REMARK 3 S31: 0.4338 S32: -0.4086 S33: 0.0219
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: ( CHAIN A AND RESID 434:466 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.157 3.690 -15.402
REMARK 3 T TENSOR
REMARK 3 T11: 0.3150 T22: 0.1341
REMARK 3 T33: 0.2015 T12: -0.0118
REMARK 3 T13: 0.0421 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 2.2630 L22: 2.2272
REMARK 3 L33: 2.6829 L12: -0.7292
REMARK 3 L13: 0.7051 L23: 0.5456
REMARK 3 S TENSOR
REMARK 3 S11: -0.2274 S12: -0.0204 S13: -0.1440
REMARK 3 S21: 0.3071 S22: 0.0235 S23: -0.2388
REMARK 3 S31: 0.2875 S32: -0.0575 S33: 0.1194
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: ( CHAIN A AND RESID 467:563 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.534 9.819 -14.764
REMARK 3 T TENSOR
REMARK 3 T11: 0.3196 T22: 0.1442
REMARK 3 T33: 0.4281 T12: 0.0197
REMARK 3 T13: -0.1408 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 0.9133 L22: 0.1768
REMARK 3 L33: 0.6235 L12: -0.0105
REMARK 3 L13: -0.1519 L23: -0.1849
REMARK 3 S TENSOR
REMARK 3 S11: -0.2872 S12: -0.0190 S13: -0.0414
REMARK 3 S21: 0.2113 S22: -0.0070 S23: -0.5149
REMARK 3 S31: 0.0472 S32: 0.1846 S33: 0.0856
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: ( CHAIN A AND RESID 564:618 )
REMARK 3 ORIGIN FOR THE GROUP (A): 67.607 18.781 -7.967
REMARK 3 T TENSOR
REMARK 3 T11: 0.3753 T22: 0.2207
REMARK 3 T33: 0.8911 T12: -0.1740
REMARK 3 T13: -0.7706 T23: -0.0821
REMARK 3 L TENSOR
REMARK 3 L11: 0.3207 L22: 0.4426
REMARK 3 L33: 0.4282 L12: -0.2235
REMARK 3 L13: -0.0762 L23: -0.2749
REMARK 3 S TENSOR
REMARK 3 S11: -0.1936 S12: -0.0865 S13: 0.1690
REMARK 3 S21: 0.2053 S22: -0.0145 S23: -0.4679
REMARK 3 S31: -0.1390 S32: 0.2799 S33: -0.0444
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: ( CHAIN C AND RESID 21:44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.079 22.738 31.554
REMARK 3 T TENSOR
REMARK 3 T11: 0.7715 T22: 0.2710
REMARK 3 T33: 0.3023 T12: 0.0808
REMARK 3 T13: -0.2137 T23: -0.2197
REMARK 3 L TENSOR
REMARK 3 L11: 0.7864 L22: 2.8154
REMARK 3 L33: 0.1335 L12: 1.1780
REMARK 3 L13: -0.2937 L23: -0.3575
REMARK 3 S TENSOR
REMARK 3 S11: 0.0223 S12: -0.1871 S13: -0.0800
REMARK 3 S21: 0.2451 S22: 0.1015 S23: -0.2012
REMARK 3 S31: 0.2067 S32: 0.1632 S33: -0.1156
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: ( CHAIN C AND RESID 45:55 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.460 16.034 31.203
REMARK 3 T TENSOR
REMARK 3 T11: 0.4415 T22: 0.1921
REMARK 3 T33: 0.2970 T12: 0.0125
REMARK 3 T13: 0.0609 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 6.7115 L22: 1.8746
REMARK 3 L33: 5.6376 L12: 0.2662
REMARK 3 L13: 0.7956 L23: 3.1375
REMARK 3 S TENSOR
REMARK 3 S11: -0.1542 S12: -0.2881 S13: -0.3120
REMARK 3 S21: 0.5467 S22: 0.1052 S23: 0.5547
REMARK 3 S31: 0.1696 S32: -0.2194 S33: 0.0225
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: ( CHAIN C AND RESID 56:82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.912 24.262 20.001
REMARK 3 T TENSOR
REMARK 3 T11: 0.2646 T22: 0.1727
REMARK 3 T33: 0.2139 T12: 0.0291
REMARK 3 T13: -0.0100 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 0.6929 L22: 1.9883
REMARK 3 L33: 1.1680 L12: -0.0502
REMARK 3 L13: -0.1949 L23: -0.3569
REMARK 3 S TENSOR
REMARK 3 S11: 0.1573 S12: 0.0054 S13: -0.0300
REMARK 3 S21: 0.3761 S22: 0.0627 S23: -0.0546
REMARK 3 S31: 0.1266 S32: 0.0141 S33: -0.1126
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: ( CHAIN C AND RESID 83:102 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.450 17.647 14.220
REMARK 3 T TENSOR
REMARK 3 T11: 0.2656 T22: 0.2299
REMARK 3 T33: 0.2915 T12: 0.0563
REMARK 3 T13: -0.0575 T23: -0.0924
REMARK 3 L TENSOR
REMARK 3 L11: 1.2727 L22: 2.8483
REMARK 3 L33: 0.8741 L12: -1.4165
REMARK 3 L13: 0.1149 L23: -1.1741
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: 0.0238 S13: 0.0453
REMARK 3 S21: 0.2959 S22: -0.0585 S23: -0.1369
REMARK 3 S31: 0.1618 S32: 0.0900 S33: -0.0799
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: ( CHAIN C AND RESID 103:143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.378 21.413 20.784
REMARK 3 T TENSOR
REMARK 3 T11: 0.3501 T22: 0.2045
REMARK 3 T33: 0.2268 T12: 0.0031
REMARK 3 T13: -0.0852 T23: -0.1023
REMARK 3 L TENSOR
REMARK 3 L11: 0.7703 L22: 2.9302
REMARK 3 L33: 0.8237 L12: -0.4752
REMARK 3 L13: -0.2880 L23: -1.0479
REMARK 3 S TENSOR
REMARK 3 S11: 0.1756 S12: 0.0603 S13: 0.0813
REMARK 3 S21: 0.3961 S22: 0.0478 S23: -0.2402
REMARK 3 S31: 0.2590 S32: 0.1399 S33: -0.0395
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: ( CHAIN C AND RESID 144:156 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.291 19.584 26.359
REMARK 3 T TENSOR
REMARK 3 T11: 0.3441 T22: 0.2340
REMARK 3 T33: 0.3064 T12: 0.0062
REMARK 3 T13: -0.1559 T23: -0.1592
REMARK 3 L TENSOR
REMARK 3 L11: 1.6095 L22: 2.2112
REMARK 3 L33: 1.5542 L12: -0.2941
REMARK 3 L13: 0.9736 L23: 1.2680
REMARK 3 S TENSOR
REMARK 3 S11: 0.2032 S12: -0.1335 S13: 0.0156
REMARK 3 S21: 0.3795 S22: 0.0083 S23: -0.0639
REMARK 3 S31: 0.0674 S32: 0.1213 S33: -0.0282
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: ( CHAIN A AND RESID 703:704 ) OR ( CHAIN C AND RESID
REMARK 3 203:203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.242 12.278 17.039
REMARK 3 T TENSOR
REMARK 3 T11: 0.5176 T22: 0.4973
REMARK 3 T33: 0.5096 T12: 0.0244
REMARK 3 T13: -0.0574 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0040
REMARK 3 L33: -0.0006 L12: -0.0077
REMARK 3 L13: 0.0013 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0465 S12: 0.0694 S13: -0.0095
REMARK 3 S21: -0.0802 S22: 0.0822 S23: 0.0676
REMARK 3 S31: 0.0472 S32: -0.0829 S33: 0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7MLM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-APR-21.
REMARK 100 THE DEPOSITION ID IS D_1000256336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-JUL-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58410
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 11.90
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 1.13400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 5IJC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH8.0, 0.8 M SODIUM
REMARK 280 FORMATE, 8% PEG 8000, 8% PEG 1000, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.64800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.64800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 72.54700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 82.14650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 72.54700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 82.14650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.64800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 72.54700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 82.14650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 44.64800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 72.54700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 82.14650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -15
REMARK 465 LEU A -14
REMARK 465 LEU A -13
REMARK 465 VAL A -12
REMARK 465 ASN A -11
REMARK 465 GLN A -10
REMARK 465 SER A -9
REMARK 465 HIS A -8
REMARK 465 GLN A -7
REMARK 465 GLY A -6
REMARK 465 PHE A -5
REMARK 465 ASN A -4
REMARK 465 LYS A -3
REMARK 465 GLU A -2
REMARK 465 HIS A -1
REMARK 465 THR A 0
REMARK 465 SER A 1
REMARK 465 LYS A 2
REMARK 465 MET A 3
REMARK 465 VAL A 4
REMARK 465 SER A 5
REMARK 465 ALA A 6
REMARK 465 ILE A 7
REMARK 465 VAL A 8
REMARK 465 LEU A 9
REMARK 465 TYR A 10
REMARK 465 VAL A 11
REMARK 465 LEU A 12
REMARK 465 LEU A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 ALA A 16
REMARK 465 ALA A 17
REMARK 465 HIS A 18
REMARK 465 SER A 19
REMARK 465 ALA A 20
REMARK 465 PHE A 21
REMARK 465 ALA A 22
REMARK 465 ALA A 23
REMARK 465 ASP A 24
REMARK 465 PRO A 25
REMARK 465 ASN A 26
REMARK 465 GLY A 607
REMARK 465 SER A 608
REMARK 465 THR A 619
REMARK 465 MET C -22
REMARK 465 LEU C -21
REMARK 465 LEU C -20
REMARK 465 VAL C -19
REMARK 465 ASN C -18
REMARK 465 GLN C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 GLN C -14
REMARK 465 GLY C -13
REMARK 465 PHE C -12
REMARK 465 ASN C -11
REMARK 465 LYS C -10
REMARK 465 GLU C -9
REMARK 465 HIS C -8
REMARK 465 THR C -7
REMARK 465 SER C -6
REMARK 465 LYS C -5
REMARK 465 MET C -4
REMARK 465 VAL C -3
REMARK 465 SER C -2
REMARK 465 ALA C -1
REMARK 465 ILE C 0
REMARK 465 VAL C 1
REMARK 465 LEU C 2
REMARK 465 TYR C 3
REMARK 465 VAL C 4
REMARK 465 LEU C 5
REMARK 465 LEU C 6
REMARK 465 ALA C 7
REMARK 465 ALA C 8
REMARK 465 ALA C 9
REMARK 465 ALA C 10
REMARK 465 HIS C 11
REMARK 465 SER C 12
REMARK 465 ALA C 13
REMARK 465 PHE C 14
REMARK 465 ALA C 15
REMARK 465 ALA C 16
REMARK 465 ASP C 17
REMARK 465 PRO C 18
REMARK 465 GLU C 19
REMARK 465 LYS C 20
REMARK 465 ARG C 157
REMARK 465 ASP C 158
REMARK 465 VAL C 159
REMARK 465 ASN C 160
REMARK 465 LEU C 161
REMARK 465 VAL C 162
REMARK 465 PRO C 163
REMARK 465 ARG C 164
REMARK 465 GLY C 165
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 ND2 ASN A 492 O5 NAG A 701 2.07
REMARK 500 O4 NAG D 1 O5 NAG D 2 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 34 15.05 59.68
REMARK 500 ILE A 35 -53.09 -130.21
REMARK 500 LYS A 66 -36.53 71.87
REMARK 500 LEU A 100 55.31 -93.19
REMARK 500 GLN A 114 -73.00 64.21
REMARK 500 ASN A 159 -154.91 -121.77
REMARK 500 ASN A 184 -157.57 -119.50
REMARK 500 ASN A 200 78.58 -118.52
REMARK 500 HIS A 228 -72.30 -72.87
REMARK 500 THR A 290 -167.80 -111.66
REMARK 500 SER A 317 41.79 -78.59
REMARK 500 ASN A 415 53.09 -98.16
REMARK 500 ASP A 460 16.12 -140.28
REMARK 500 LEU A 468 58.19 -90.06
REMARK 500 ASN A 479 -152.77 -103.91
REMARK 500 ASP A 483 16.35 58.79
REMARK 500 ASN A 528 -165.05 -112.19
REMARK 500 ASN A 552 -155.38 -121.68
REMARK 500 CYS A 580 54.81 -99.04
REMARK 500 SER A 614 55.90 -114.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7MLM A 26 544 UNP Q9QUK6 TLR4_MOUSE 26 544
DBREF 7MLM A 545 619 UNP Q4G1L2 Q4G1L2_EPTBU 126 200
DBREF 7MLM C 19 160 UNP Q9JHF9 LY96_MOUSE 19 160
SEQADV 7MLM MET A -15 UNP Q9QUK6 INITIATING METHIONINE
SEQADV 7MLM LEU A -14 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM LEU A -13 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM VAL A -12 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ASN A -11 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM GLN A -10 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM SER A -9 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM HIS A -8 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM GLN A -7 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM GLY A -6 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM PHE A -5 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ASN A -4 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM LYS A -3 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM GLU A -2 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM HIS A -1 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM THR A 0 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM SER A 1 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM LYS A 2 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM MET A 3 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM VAL A 4 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM SER A 5 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 6 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ILE A 7 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM VAL A 8 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM LEU A 9 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM TYR A 10 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM VAL A 11 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM LEU A 12 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM LEU A 13 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 14 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 15 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 16 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 17 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM HIS A 18 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM SER A 19 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 20 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM PHE A 21 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 22 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ALA A 23 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM ASP A 24 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM PRO A 25 UNP Q9QUK6 EXPRESSION TAG
SEQADV 7MLM MET C -22 UNP Q9JHF9 INITIATING METHIONINE
SEQADV 7MLM LEU C -21 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LEU C -20 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM VAL C -19 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ASN C -18 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM GLN C -17 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM SER C -16 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM HIS C -15 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM GLN C -14 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM GLY C -13 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM PHE C -12 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ASN C -11 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LYS C -10 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM GLU C -9 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM HIS C -8 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM THR C -7 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM SER C -6 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LYS C -5 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM MET C -4 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM VAL C -3 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM SER C -2 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C -1 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ILE C 0 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM VAL C 1 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LEU C 2 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM TYR C 3 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM VAL C 4 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LEU C 5 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LEU C 6 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 7 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 8 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 9 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 10 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM HIS C 11 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM SER C 12 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 13 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM PHE C 14 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 15 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ALA C 16 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ASP C 17 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM PRO C 18 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM LEU C 161 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM VAL C 162 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM PRO C 163 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM ARG C 164 UNP Q9JHF9 EXPRESSION TAG
SEQADV 7MLM GLY C 165 UNP Q9JHF9 EXPRESSION TAG
SEQRES 1 A 635 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS
SEQRES 2 A 635 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR
SEQRES 3 A 635 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA ALA
SEQRES 4 A 635 ASP PRO ASN PRO CYS ILE GLU VAL VAL PRO ASN ILE THR
SEQRES 5 A 635 TYR GLN CYS MET ASP GLN LYS LEU SER LYS VAL PRO ASP
SEQRES 6 A 635 ASP ILE PRO SER SER THR LYS ASN ILE ASP LEU SER PHE
SEQRES 7 A 635 ASN PRO LEU LYS ILE LEU LYS SER TYR SER PHE SER ASN
SEQRES 8 A 635 PHE SER GLU LEU GLN TRP LEU ASP LEU SER ARG CYS GLU
SEQRES 9 A 635 ILE GLU THR ILE GLU ASP LYS ALA TRP HIS GLY LEU HIS
SEQRES 10 A 635 HIS LEU SER ASN LEU ILE LEU THR GLY ASN PRO ILE GLN
SEQRES 11 A 635 SER PHE SER PRO GLY SER PHE SER GLY LEU THR SER LEU
SEQRES 12 A 635 GLU ASN LEU VAL ALA VAL GLU THR LYS LEU ALA SER LEU
SEQRES 13 A 635 GLU SER PHE PRO ILE GLY GLN LEU ILE THR LEU LYS LYS
SEQRES 14 A 635 LEU ASN VAL ALA HIS ASN PHE ILE HIS SER CYS LYS LEU
SEQRES 15 A 635 PRO ALA TYR PHE SER ASN LEU THR ASN LEU VAL HIS VAL
SEQRES 16 A 635 ASP LEU SER TYR ASN TYR ILE GLN THR ILE THR VAL ASN
SEQRES 17 A 635 ASP LEU GLN PHE LEU ARG GLU ASN PRO GLN VAL ASN LEU
SEQRES 18 A 635 SER LEU ASP MET SER LEU ASN PRO ILE ASP PHE ILE GLN
SEQRES 19 A 635 ASP GLN ALA PHE GLN GLY ILE LYS LEU HIS GLU LEU THR
SEQRES 20 A 635 LEU ARG GLY ASN PHE ASN SER SER ASN ILE MET LYS THR
SEQRES 21 A 635 CYS LEU GLN ASN LEU ALA GLY LEU HIS VAL HIS ARG LEU
SEQRES 22 A 635 ILE LEU GLY GLU PHE LYS ASP GLU ARG ASN LEU GLU ILE
SEQRES 23 A 635 PHE GLU PRO SER ILE MET GLU GLY LEU CYS ASP VAL THR
SEQRES 24 A 635 ILE ASP GLU PHE ARG LEU THR TYR THR ASN ASP PHE SER
SEQRES 25 A 635 ASP ASP ILE VAL LYS PHE HIS CYS LEU ALA ASN VAL SER
SEQRES 26 A 635 ALA MET SER LEU ALA GLY VAL SER ILE LYS TYR LEU GLU
SEQRES 27 A 635 ASP VAL PRO LYS HIS PHE LYS TRP GLN SER LEU SER ILE
SEQRES 28 A 635 ILE ARG CYS GLN LEU LYS GLN PHE PRO THR LEU ASP LEU
SEQRES 29 A 635 PRO PHE LEU LYS SER LEU THR LEU THR MET ASN LYS GLY
SEQRES 30 A 635 SER ILE SER PHE LYS LYS VAL ALA LEU PRO SER LEU SER
SEQRES 31 A 635 TYR LEU ASP LEU SER ARG ASN ALA LEU SER PHE SER GLY
SEQRES 32 A 635 CYS CYS SER TYR SER ASP LEU GLY THR ASN SER LEU ARG
SEQRES 33 A 635 HIS LEU ASP LEU SER PHE ASN GLY ALA ILE ILE MET SER
SEQRES 34 A 635 ALA ASN PHE MET GLY LEU GLU GLU LEU GLN HIS LEU ASP
SEQRES 35 A 635 PHE GLN HIS SER THR LEU LYS ARG VAL THR GLU PHE SER
SEQRES 36 A 635 ALA PHE LEU SER LEU GLU LYS LEU LEU TYR LEU ASP ILE
SEQRES 37 A 635 SER TYR THR ASN THR LYS ILE ASP PHE ASP GLY ILE PHE
SEQRES 38 A 635 LEU GLY LEU THR SER LEU ASN THR LEU LYS MET ALA GLY
SEQRES 39 A 635 ASN SER PHE LYS ASP ASN THR LEU SER ASN VAL PHE ALA
SEQRES 40 A 635 ASN THR THR ASN LEU THR PHE LEU ASP LEU SER LYS CYS
SEQRES 41 A 635 GLN LEU GLU GLN ILE SER TRP GLY VAL PHE ASP THR LEU
SEQRES 42 A 635 HIS ARG LEU GLN LEU LEU ASN MET SER HIS ASN ASN LEU
SEQRES 43 A 635 LEU PHE LEU ASP SER SER HIS TYR ASN GLN LEU TYR SER
SEQRES 44 A 635 LEU LYS GLU LEU ALA LEU ASP THR ASN GLN LEU LYS SER
SEQRES 45 A 635 VAL PRO ASP GLY ILE PHE ASP ARG LEU THR SER LEU GLN
SEQRES 46 A 635 LYS ILE TRP LEU HIS THR ASN PRO TRP ASP CYS SER CYS
SEQRES 47 A 635 PRO ARG ILE ASP TYR LEU SER ARG TRP LEU ASN LYS ASN
SEQRES 48 A 635 SER GLN LYS GLU GLN GLY SER ALA LYS CYS SER GLY SER
SEQRES 49 A 635 GLY LYS PRO VAL ARG SER ILE ILE CYS PRO THR
SEQRES 1 C 188 MET LEU LEU VAL ASN GLN SER HIS GLN GLY PHE ASN LYS
SEQRES 2 C 188 GLU HIS THR SER LYS MET VAL SER ALA ILE VAL LEU TYR
SEQRES 3 C 188 VAL LEU LEU ALA ALA ALA ALA HIS SER ALA PHE ALA ALA
SEQRES 4 C 188 ASP PRO GLU LYS GLN GLN TRP PHE CYS ASN SER SER ASP
SEQRES 5 C 188 ALA ILE ILE SER TYR SER TYR CYS ASP HIS LEU LYS PHE
SEQRES 6 C 188 PRO ILE SER ILE SER SER GLU PRO CYS ILE ARG LEU ARG
SEQRES 7 C 188 GLY THR ASN GLY PHE VAL HIS VAL GLU PHE ILE PRO ARG
SEQRES 8 C 188 GLY ASN LEU LYS TYR LEU TYR PHE ASN LEU PHE ILE SER
SEQRES 9 C 188 VAL ASN SER ILE GLU LEU PRO LYS ARG LYS GLU VAL LEU
SEQRES 10 C 188 CYS HIS GLY HIS ASP ASP ASP TYR SER PHE CYS ARG ALA
SEQRES 11 C 188 LEU LYS GLY GLU THR VAL ASN THR SER ILE PRO PHE SER
SEQRES 12 C 188 PHE GLU GLY ILE LEU PHE PRO LYS GLY HIS TYR ARG CYS
SEQRES 13 C 188 VAL ALA GLU ALA ILE ALA GLY ASP THR GLU GLU LYS LEU
SEQRES 14 C 188 PHE CYS LEU ASN PHE THR ILE ILE HIS ARG ARG ASP VAL
SEQRES 15 C 188 ASN LEU VAL PRO ARG GLY
HET NAG B 1 14
HET NAG B 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG D 3 14
HET NAG A 701 14
HET NAG A 702 14
HET ZKM A 703 53
HET ZKM A 704 53
HET NAG C 201 14
HET NAG C 202 14
HET ZKM C 203 53
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM ZKM N-[(1S,2R,3E)-2-HYDROXY-1-{[(3-O-SULFO-BETA-D-
HETNAM 2 ZKM GALACTOPYRANOSYL)OXY]METHYL}HEPTADEC-3-EN-1-YL]-
HETNAM 3 ZKM HEXADECANAMIDE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 3 NAG 9(C8 H15 N O6)
FORMUL 7 ZKM 3(C40 H77 N O11 S)
FORMUL 12 HOH *262(H2 O)
HELIX 1 AA1 PRO A 167 ASN A 172 5 6
HELIX 2 AA2 VAL A 191 ASP A 193 5 3
HELIX 3 AA3 LEU A 194 ASN A 200 1 7
HELIX 4 AA4 SER A 238 ASN A 248 1 11
HELIX 5 AA5 GLU A 272 VAL A 282 5 11
HELIX 6 AA6 SER A 296 ALA A 306 5 11
HELIX 7 AA7 SER A 390 GLY A 395 1 6
HELIX 8 AA8 ASP A 534 ASN A 539 5 6
HELIX 9 AA9 ILE A 585 ASN A 595 1 11
HELIX 10 AB1 PRO A 611 ILE A 615 5 5
HELIX 11 AB2 TYR C 102 ALA C 107 5 6
SHEET 1 AA125 ILE A 29 VAL A 32 0
SHEET 2 AA125 THR A 36 GLN A 38 -1 O GLN A 38 N ILE A 29
SHEET 3 AA125 ASN A 57 ASP A 59 1 O ASN A 57 N TYR A 37
SHEET 4 AA125 TRP A 81 ASP A 83 1 O ASP A 83 N ILE A 58
SHEET 5 AA125 ASN A 105 ILE A 107 1 O ILE A 107 N LEU A 82
SHEET 6 AA125 ASN A 129 VAL A 131 1 O VAL A 131 N LEU A 106
SHEET 7 AA125 LYS A 153 ASN A 155 1 O ASN A 155 N LEU A 130
SHEET 8 AA125 HIS A 178 ASP A 180 1 O ASP A 180 N LEU A 154
SHEET 9 AA125 SER A 206 ASP A 208 1 O SER A 206 N VAL A 179
SHEET 10 AA125 LYS A 226 ARG A 233 1 O GLU A 229 N LEU A 207
SHEET 11 AA125 HIS A 253 GLY A 260 1 O ILE A 258 N LEU A 232
SHEET 12 AA125 THR A 283 LEU A 289 1 O ARG A 288 N LEU A 257
SHEET 13 AA125 ALA A 310 ALA A 314 1 O ALA A 310 N PHE A 287
SHEET 14 AA125 SER A 332 ILE A 336 1 O SER A 334 N LEU A 313
SHEET 15 AA125 SER A 353 THR A 357 1 O THR A 355 N ILE A 335
SHEET 16 AA125 TYR A 375 ASP A 377 1 O ASP A 377 N LEU A 356
SHEET 17 AA125 HIS A 401 ASP A 403 1 O ASP A 403 N LEU A 376
SHEET 18 AA125 HIS A 424 ASP A 426 1 O HIS A 424 N LEU A 402
SHEET 19 AA125 TYR A 449 ASP A 451 1 O TYR A 449 N LEU A 425
SHEET 20 AA125 THR A 473 LYS A 475 1 O LYS A 475 N LEU A 450
SHEET 21 AA125 PHE A 498 ASP A 500 1 O PHE A 498 N LEU A 474
SHEET 22 AA125 LEU A 522 ASN A 524 1 O ASN A 524 N LEU A 499
SHEET 23 AA125 GLU A 546 ALA A 548 1 O ALA A 548 N LEU A 523
SHEET 24 AA125 LYS A 570 TRP A 572 1 O TRP A 572 N LEU A 547
SHEET 25 AA125 GLU A 599 GLN A 600 1 O GLN A 600 N ILE A 571
SHEET 1 AA2 2 ILE A 67 LEU A 68 0
SHEET 2 AA2 2 THR A 91 ILE A 92 1 O THR A 91 N LEU A 68
SHEET 1 AA3 2 THR A 188 ILE A 189 0
SHEET 2 AA3 2 PHE A 216 ILE A 217 1 O PHE A 216 N ILE A 189
SHEET 1 AA4 3 PHE A 385 CYS A 388 0
SHEET 2 AA4 3 ALA A 409 MET A 412 1 O ILE A 411 N PHE A 385
SHEET 3 AA4 3 THR A 431 LYS A 433 1 O LYS A 433 N MET A 412
SHEET 1 AA5 2 LYS A 458 ILE A 459 0
SHEET 2 AA5 2 SER A 480 PHE A 481 1 O SER A 480 N ILE A 459
SHEET 1 AA6 2 THR A 485 LEU A 486 0
SHEET 2 AA6 2 GLN A 508 ILE A 509 1 O GLN A 508 N LEU A 486
SHEET 1 AA7 6 TRP C 23 ASN C 26 0
SHEET 2 AA7 6 ALA C 30 TYR C 36 -1 O ILE C 32 N CYS C 25
SHEET 3 AA7 6 GLU C 144 HIS C 155 -1 O THR C 152 N SER C 33
SHEET 4 AA7 6 GLY C 129 ALA C 139 -1 N TYR C 131 O ILE C 153
SHEET 5 AA7 6 LEU C 74 VAL C 82 -1 N ASN C 77 O GLU C 136
SHEET 6 AA7 6 ILE C 85 GLU C 86 -1 O ILE C 85 N VAL C 82
SHEET 1 AA8 6 TRP C 23 ASN C 26 0
SHEET 2 AA8 6 ALA C 30 TYR C 36 -1 O ILE C 32 N CYS C 25
SHEET 3 AA8 6 GLU C 144 HIS C 155 -1 O THR C 152 N SER C 33
SHEET 4 AA8 6 GLY C 129 ALA C 139 -1 N TYR C 131 O ILE C 153
SHEET 5 AA8 6 LEU C 74 VAL C 82 -1 N ASN C 77 O GLU C 136
SHEET 6 AA8 6 ARG C 90 VAL C 93 -1 O ARG C 90 N LEU C 78
SHEET 1 AA9 3 SER C 45 GLU C 49 0
SHEET 2 AA9 3 GLY C 56 PHE C 65 -1 O PHE C 60 N GLU C 49
SHEET 3 AA9 3 VAL C 113 GLU C 122 -1 O THR C 115 N VAL C 63
SSBOND 1 CYS A 28 CYS A 39 1555 1555 2.03
SSBOND 2 CYS A 280 CYS A 304 1555 1555 2.03
SSBOND 3 CYS A 388 CYS A 389 1555 1555 2.02
SSBOND 4 CYS A 580 CYS A 605 1555 1555 2.03
SSBOND 5 CYS A 582 CYS A 617 1555 1555 2.03
SSBOND 6 CYS C 25 CYS C 51 1555 1555 2.03
SSBOND 7 CYS C 37 CYS C 148 1555 1555 2.03
SSBOND 8 CYS C 95 CYS C 105 1555 1555 2.03
LINK ND2 ASN A 204 C1 NAG B 1 1555 1555 1.53
LINK ND2 ASN A 237 C1 NAG D 1 1555 1555 1.48
LINK ND2 ASN A 492 C1 NAG A 701 1555 1555 1.52
LINK ND2 ASN A 524 C1 NAG A 702 1555 1555 1.51
LINK ND2 ASN C 114 C1 NAG C 201 1555 1555 1.48
LINK ND2 ASN C 150 C1 NAG C 202 1555 1555 1.53
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.43
LINK O4 NAG D 2 C1 NAG D 3 1555 1555 1.46
CISPEP 1 CYS A 388 CYS A 389 0 -8.89
CISPEP 2 CYS A 582 PRO A 583 0 3.69
CISPEP 3 GLU C 49 PRO C 50 0 -0.08
CRYST1 145.094 164.293 89.296 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006892 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006087 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011199 0.00000
ATOM 1 N PRO A 27 50.510 47.668 17.698 1.00 64.31 N
ANISOU 1 N PRO A 27 4902 9726 9806 -328 645 -1177 N
ATOM 2 CA PRO A 27 49.730 46.694 18.466 1.00 62.77 C
ANISOU 2 CA PRO A 27 4777 9466 9606 -155 581 -1178 C
ATOM 3 C PRO A 27 48.836 45.843 17.571 1.00 59.58 C
ANISOU 3 C PRO A 27 4508 8893 9237 11 633 -1132 C
ATOM 4 O PRO A 27 48.262 44.857 18.029 1.00 56.85 O
ANISOU 4 O PRO A 27 4236 8490 8874 177 599 -1124 O
ATOM 5 CB PRO A 27 48.892 47.578 19.387 1.00 59.64 C
ANISOU 5 CB PRO A 27 4459 8939 9263 -315 554 -1253 C
ATOM 6 CG PRO A 27 48.677 48.817 18.589 1.00 61.55 C
ANISOU 6 CG PRO A 27 4760 9055 9570 -512 651 -1265 C
ATOM 7 CD PRO A 27 49.948 49.027 17.804 1.00 64.63 C
ANISOU 7 CD PRO A 27 5027 9618 9913 -559 692 -1235 C
ATOM 8 N CYS A 28 48.724 46.237 16.306 1.00 57.73 N
ANISOU 8 N CYS A 28 4315 8581 9039 -40 720 -1101 N
ATOM 9 CA CYS A 28 47.885 45.556 15.330 1.00 53.84 C
ANISOU 9 CA CYS A 28 3953 7942 8561 82 779 -1058 C
ATOM 10 C CYS A 28 48.693 44.492 14.604 1.00 49.95 C
ANISOU 10 C CYS A 28 3410 7566 8005 246 807 -995 C
ATOM 11 O CYS A 28 49.789 44.768 14.112 1.00 55.24 O
ANISOU 11 O CYS A 28 3958 8381 8651 206 827 -966 O
ATOM 12 CB CYS A 28 47.316 46.549 14.319 1.00 52.29 C
ANISOU 12 CB CYS A 28 3832 7614 8423 -50 864 -1045 C
ATOM 13 SG CYS A 28 46.169 47.759 14.991 1.00 62.32 S
ANISOU 13 SG CYS A 28 5249 8690 9739 -211 858 -1073 S
ATOM 14 N ILE A 29 48.142 43.283 14.529 1.00 39.64 N
ANISOU 14 N ILE A 29 2208 6187 6667 425 819 -974 N
ATOM 15 CA ILE A 29 48.776 42.221 13.754 1.00 46.22 C
ANISOU 15 CA ILE A 29 3029 7091 7441 585 873 -912 C
ATOM 16 C ILE A 29 48.744 42.601 12.282 1.00 50.37 C
ANISOU 16 C ILE A 29 3580 7575 7984 519 954 -880 C
ATOM 17 O ILE A 29 47.669 42.760 11.689 1.00 48.41 O
ANISOU 17 O ILE A 29 3461 7173 7759 477 994 -889 O
ATOM 18 CB ILE A 29 48.084 40.873 13.996 1.00 43.60 C
ANISOU 18 CB ILE A 29 2843 6656 7068 771 894 -907 C
ATOM 19 CG1 ILE A 29 48.350 40.382 15.418 1.00 43.15 C
ANISOU 19 CG1 ILE A 29 2749 6671 6975 874 822 -916 C
ATOM 20 CG2 ILE A 29 48.549 39.844 12.974 1.00 42.74 C
ANISOU 20 CG2 ILE A 29 2764 6572 6903 913 987 -846 C
ATOM 21 CD1 ILE A 29 47.995 38.926 15.638 1.00 44.52 C
ANISOU 21 CD1 ILE A 29 3063 6766 7088 1086 867 -891 C
ATOM 22 N GLU A 30 49.922 42.753 11.686 1.00 53.71 N
ANISOU 22 N GLU A 30 3875 8146 8387 510 979 -836 N
ATOM 23 CA GLU A 30 50.016 42.995 10.253 1.00 58.47 C
ANISOU 23 CA GLU A 30 4496 8725 8995 470 1057 -796 C
ATOM 24 C GLU A 30 49.730 41.693 9.512 1.00 64.61 C
ANISOU 24 C GLU A 30 5377 9449 9722 638 1123 -760 C
ATOM 25 O GLU A 30 50.461 40.712 9.669 1.00 73.16 O
ANISOU 25 O GLU A 30 6419 10621 10757 793 1139 -724 O
ATOM 26 CB GLU A 30 51.396 43.537 9.894 1.00 62.06 C
ANISOU 26 CB GLU A 30 4782 9355 9443 408 1064 -763 C
ATOM 27 CG GLU A 30 51.507 44.064 8.473 1.00 66.84 C
ANISOU 27 CG GLU A 30 5398 9934 10062 334 1138 -727 C
ATOM 28 CD GLU A 30 52.485 45.219 8.356 1.00 70.72 C
ANISOU 28 CD GLU A 30 5755 10538 10576 173 1139 -729 C
ATOM 29 OE1 GLU A 30 52.712 45.915 9.368 1.00 73.23 O
ANISOU 29 OE1 GLU A 30 6008 10906 10909 59 1087 -781 O
ATOM 30 OE2 GLU A 30 53.029 45.434 7.254 1.00 71.49 O
ANISOU 30 OE2 GLU A 30 5818 10675 10670 151 1197 -685 O
ATOM 31 N VAL A 31 48.665 41.679 8.716 1.00 60.37 N
ANISOU 31 N VAL A 31 4979 8773 9188 607 1170 -768 N
ATOM 32 CA VAL A 31 48.210 40.483 8.014 1.00 49.44 C
ANISOU 32 CA VAL A 31 3717 7323 7746 729 1242 -756 C
ATOM 33 C VAL A 31 48.650 40.494 6.553 1.00 48.15 C
ANISOU 33 C VAL A 31 3533 7204 7557 719 1315 -709 C
ATOM 34 O VAL A 31 49.294 39.555 6.085 1.00 57.20 O
ANISOU 34 O VAL A 31 4672 8407 8656 842 1372 -676 O
ATOM 35 CB VAL A 31 46.677 40.323 8.136 1.00 41.83 C
ANISOU 35 CB VAL A 31 2920 6196 6776 699 1246 -803 C
ATOM 36 CG1 VAL A 31 46.183 39.235 7.199 1.00 36.54 C
ANISOU 36 CG1 VAL A 31 2377 5470 6035 773 1335 -803 C
ATOM 37 CG2 VAL A 31 46.295 40.006 9.576 1.00 43.86 C
ANISOU 37 CG2 VAL A 31 3214 6405 7045 747 1182 -848 C
ATOM 38 N VAL A 32 48.297 41.547 5.816 1.00 44.68 N
ANISOU 38 N VAL A 32 3092 6738 7146 582 1323 -699 N
ATOM 39 CA VAL A 32 48.814 41.792 4.477 1.00 45.54 C
ANISOU 39 CA VAL A 32 3161 6905 7237 555 1380 -650 C
ATOM 40 C VAL A 32 49.433 43.189 4.506 1.00 51.58 C
ANISOU 40 C VAL A 32 3812 7728 8059 419 1355 -634 C
ATOM 41 O VAL A 32 48.718 44.168 4.740 1.00 55.17 O
ANISOU 41 O VAL A 32 4305 8103 8553 306 1340 -653 O
ATOM 42 CB VAL A 32 47.731 41.702 3.395 1.00 38.84 C
ANISOU 42 CB VAL A 32 2438 5972 6346 527 1434 -645 C
ATOM 43 CG1 VAL A 32 48.352 41.850 2.011 1.00 38.52 C
ANISOU 43 CG1 VAL A 32 2351 6005 6279 516 1491 -592 C
ATOM 44 CG2 VAL A 32 46.963 40.388 3.509 1.00 37.32 C
ANISOU 44 CG2 VAL A 32 2377 5709 6095 623 1466 -684 C
ATOM 45 N PRO A 33 50.740 43.331 4.287 1.00 53.87 N
ANISOU 45 N PRO A 33 3966 8152 8352 422 1361 -601 N
ATOM 46 CA PRO A 33 51.409 44.612 4.567 1.00 51.82 C
ANISOU 46 CA PRO A 33 3593 7953 8142 276 1339 -607 C
ATOM 47 C PRO A 33 50.758 45.801 3.874 1.00 45.86 C
ANISOU 47 C PRO A 33 2901 7104 7419 139 1382 -601 C
ATOM 48 O PRO A 33 50.471 45.767 2.676 1.00 44.09 O
ANISOU 48 O PRO A 33 2732 6854 7168 156 1438 -560 O
ATOM 49 CB PRO A 33 52.836 44.380 4.058 1.00 50.35 C
ANISOU 49 CB PRO A 33 3268 7926 7936 317 1361 -557 C
ATOM 50 CG PRO A 33 53.038 42.916 4.199 1.00 48.35 C
ANISOU 50 CG PRO A 33 3029 7707 7634 509 1369 -534 C
ATOM 51 CD PRO A 33 51.701 42.287 3.892 1.00 51.00 C
ANISOU 51 CD PRO A 33 3542 7892 7942 562 1395 -558 C
ATOM 52 N ASN A 34 50.513 46.858 4.656 1.00 47.33 N
ANISOU 52 N ASN A 34 3082 7241 7659 9 1363 -641 N
ATOM 53 CA ASN A 34 49.934 48.117 4.175 1.00 47.72 C
ANISOU 53 CA ASN A 34 3195 7190 7746 -118 1424 -631 C
ATOM 54 C ASN A 34 48.555 47.922 3.552 1.00 46.26 C
ANISOU 54 C ASN A 34 3156 6886 7534 -61 1456 -601 C
ATOM 55 O ASN A 34 48.051 48.813 2.863 1.00 45.22 O
ANISOU 55 O ASN A 34 3081 6690 7411 -121 1523 -564 O
ATOM 56 CB ASN A 34 50.866 48.818 3.178 1.00 50.74 C
ANISOU 56 CB ASN A 34 3504 7643 8132 -192 1489 -593 C
ATOM 57 CG ASN A 34 52.113 49.372 3.836 1.00 55.86 C
ANISOU 57 CG ASN A 34 4013 8406 8804 -302 1471 -630 C
ATOM 58 OD1 ASN A 34 52.328 49.186 5.033 1.00 59.68 O
ANISOU 58 OD1 ASN A 34 4445 8937 9294 -316 1403 -681 O
ATOM 59 ND2 ASN A 34 52.949 50.048 3.054 1.00 58.01 N
ANISOU 59 ND2 ASN A 34 4222 8738 9081 -386 1531 -605 N
ATOM 60 N ILE A 35 47.922 46.771 3.782 1.00 42.68 N
ANISOU 60 N ILE A 35 2768 6411 7039 55 1416 -614 N
ATOM 61 CA ILE A 35 46.629 46.492 3.167 1.00 44.02 C
ANISOU 61 CA ILE A 35 3066 6500 7159 99 1443 -592 C
ATOM 62 C ILE A 35 45.618 46.015 4.205 1.00 40.06 C
ANISOU 62 C ILE A 35 2648 5916 6658 133 1394 -640 C
ATOM 63 O ILE A 35 44.518 46.568 4.306 1.00 38.98 O
ANISOU 63 O ILE A 35 2593 5695 6521 97 1407 -632 O
ATOM 64 CB ILE A 35 46.770 45.472 2.021 1.00 43.77 C
ANISOU 64 CB ILE A 35 3051 6530 7051 192 1474 -562 C
ATOM 65 CG1 ILE A 35 47.389 46.142 0.789 1.00 45.70 C
ANISOU 65 CG1 ILE A 35 3243 6834 7285 149 1533 -504 C
ATOM 66 CG2 ILE A 35 45.422 44.851 1.686 1.00 36.82 C
ANISOU 66 CG2 ILE A 35 2296 5592 6100 237 1486 -566 C
ATOM 67 CD1 ILE A 35 47.229 45.357 -0.496 1.00 49.39 C
ANISOU 67 CD1 ILE A 35 3748 7349 7670 220 1573 -470 C
ATOM 68 N THR A 36 45.970 44.989 4.977 1.00 37.12 N
ANISOU 68 N THR A 36 2255 5569 6278 213 1344 -682 N
ATOM 69 CA THR A 36 45.034 44.377 5.913 1.00 36.59 C
ANISOU 69 CA THR A 36 2276 5424 6204 259 1302 -730 C
ATOM 70 C THR A 36 45.648 44.322 7.301 1.00 39.53 C
ANISOU 70 C THR A 36 2575 5819 6624 266 1232 -776 C
ATOM 71 O THR A 36 46.750 43.792 7.474 1.00 40.85 O
ANISOU 71 O THR A 36 2650 6090 6783 327 1217 -773 O
ATOM 72 CB THR A 36 44.647 42.965 5.471 1.00 39.96 C
ANISOU 72 CB THR A 36 2785 5846 6552 370 1328 -741 C
ATOM 73 OG1 THR A 36 44.102 43.011 4.148 1.00 44.45 O
ANISOU 73 OG1 THR A 36 3407 6421 7061 351 1389 -703 O
ATOM 74 CG2 THR A 36 43.613 42.390 6.416 1.00 34.20 C
ANISOU 74 CG2 THR A 36 2159 5026 5810 403 1295 -796 C
ATOM 75 N TYR A 37 44.928 44.845 8.290 1.00 38.25 N
ANISOU 75 N TYR A 37 2452 5576 6504 211 1191 -813 N
ATOM 76 CA TYR A 37 45.416 44.876 9.661 1.00 35.62 C
ANISOU 76 CA TYR A 37 2051 5274 6211 205 1118 -861 C
ATOM 77 C TYR A 37 44.368 44.312 10.607 1.00 41.43 C
ANISOU 77 C TYR A 37 2888 5910 6941 260 1072 -905 C
ATOM 78 O TYR A 37 43.174 44.603 10.480 1.00 38.03 O
ANISOU 78 O TYR A 37 2564 5374 6512 227 1090 -906 O
ATOM 79 CB TYR A 37 45.811 46.294 10.062 1.00 36.23 C
ANISOU 79 CB TYR A 37 2052 5359 6355 46 1115 -875 C
ATOM 80 CG TYR A 37 47.125 46.691 9.441 1.00 44.34 C
ANISOU 80 CG TYR A 37 2954 6515 7379 -5 1145 -848 C
ATOM 81 CD1 TYR A 37 47.182 47.185 8.145 1.00 44.84 C
ANISOU 81 CD1 TYR A 37 3032 6568 7436 -44 1224 -796 C
ATOM 82 CD2 TYR A 37 48.314 46.532 10.137 1.00 43.80 C
ANISOU 82 CD2 TYR A 37 2747 6594 7300 -7 1092 -872 C
ATOM 83 CE1 TYR A 37 48.386 47.529 7.569 1.00 48.39 C
ANISOU 83 CE1 TYR A 37 3370 7134 7881 -91 1253 -773 C
ATOM 84 CE2 TYR A 37 49.522 46.876 9.572 1.00 48.32 C
ANISOU 84 CE2 TYR A 37 3200 7301 7860 -57 1119 -847 C
ATOM 85 CZ TYR A 37 49.554 47.376 8.288 1.00 50.97 C
ANISOU 85 CZ TYR A 37 3560 7607 8201 -102 1200 -801 C
ATOM 86 OH TYR A 37 50.759 47.721 7.719 1.00 54.61 O
ANISOU 86 OH TYR A 37 3902 8196 8649 -154 1229 -777 O
ATOM 87 N GLN A 38 44.830 43.490 11.544 1.00 43.82 N
ANISOU 87 N GLN A 38 3158 6261 7230 353 1017 -935 N
ATOM 88 CA GLN A 38 43.983 42.785 12.502 1.00 40.03 C
ANISOU 88 CA GLN A 38 2777 5695 6738 428 974 -978 C
ATOM 89 C GLN A 38 44.275 43.349 13.889 1.00 40.26 C
ANISOU 89 C GLN A 38 2752 5746 6796 374 880 -1007 C
ATOM 90 O GLN A 38 45.232 42.933 14.547 1.00 43.49 O
ANISOU 90 O GLN A 38 3054 6277 7192 441 840 -1016 O
ATOM 91 CB GLN A 38 44.238 41.279 12.435 1.00 42.70 C
ANISOU 91 CB GLN A 38 3166 6054 7005 597 999 -971 C
ATOM 92 CG GLN A 38 43.517 40.461 13.491 1.00 45.37 C
ANISOU 92 CG GLN A 38 3615 6304 7320 686 964 -1014 C
ATOM 93 CD GLN A 38 42.013 40.596 13.403 1.00 57.66 C
ANISOU 93 CD GLN A 38 5332 7717 8860 621 968 -1037 C
ATOM 94 OE1 GLN A 38 41.438 41.567 13.888 1.00 63.26 O
ANISOU 94 OE1 GLN A 38 6061 8375 9601 516 911 -1040 O
ATOM 95 NE2 GLN A 38 41.366 39.620 12.777 1.00 61.09 N
ANISOU 95 NE2 GLN A 38 5885 8093 9233 680 1044 -1053 N
ATOM 96 N CYS A 39 43.455 44.302 14.325 1.00 41.62 N
ANISOU 96 N CYS A 39 3001 5815 6997 257 850 -1018 N
ATOM 97 CA CYS A 39 43.626 44.964 15.610 1.00 43.85 C
ANISOU 97 CA CYS A 39 3255 6104 7304 176 769 -1051 C
ATOM 98 C CYS A 39 42.665 44.445 16.675 1.00 37.21 C
ANISOU 98 C CYS A 39 2544 5158 6436 236 700 -1076 C
ATOM 99 O CYS A 39 42.506 45.092 17.715 1.00 35.66 O
ANISOU 99 O CYS A 39 2359 4931 6259 155 637 -1103 O
ATOM 100 CB CYS A 39 43.448 46.479 15.455 1.00 46.47 C
ANISOU 100 CB CYS A 39 3592 6378 7686 -5 801 -1046 C
ATOM 101 SG CYS A 39 44.399 47.276 14.130 1.00 54.80 S
ANISOU 101 SG CYS A 39 4525 7521 8775 -99 904 -1016 S
ATOM 102 N MET A 40 42.029 43.298 16.442 1.00 33.60 N
ANISOU 102 N MET A 40 2191 4643 5931 365 719 -1072 N
ATOM 103 CA MET A 40 41.010 42.793 17.355 1.00 31.62 C
ANISOU 103 CA MET A 40 2082 4281 5652 413 667 -1099 C
ATOM 104 C MET A 40 41.571 42.551 18.751 1.00 35.33 C
ANISOU 104 C MET A 40 2499 4807 6118 459 579 -1125 C
ATOM 105 O MET A 40 42.678 42.027 18.912 1.00 44.83 O
ANISOU 105 O MET A 40 3582 6147 7304 546 574 -1117 O
ATOM 106 CB MET A 40 40.419 41.490 16.812 1.00 30.79 C
ANISOU 106 CB MET A 40 2091 4122 5485 534 726 -1103 C
ATOM 107 CG MET A 40 39.358 40.859 17.698 1.00 40.62 C
ANISOU 107 CG MET A 40 3491 5252 6692 582 687 -1136 C
ATOM 108 SD MET A 40 38.906 39.209 17.134 1.00 48.77 S
ANISOU 108 SD MET A 40 4659 6232 7641 713 783 -1159 S
ATOM 109 CE MET A 40 38.643 39.527 15.393 1.00 46.67 C
ANISOU 109 CE MET A 40 4375 5996 7361 635 881 -1138 C
ATOM 110 N ASP A 41 40.790 42.938 19.761 1.00 31.22 N
ANISOU 110 N ASP A 41 2064 4192 5605 408 511 -1150 N
ATOM 111 CA ASP A 41 41.027 42.575 21.159 1.00 34.74 C
ANISOU 111 CA ASP A 41 2495 4670 6033 466 424 -1177 C
ATOM 112 C ASP A 41 42.446 42.942 21.594 1.00 37.72 C
ANISOU 112 C ASP A 41 2673 5243 6418 440 388 -1181 C
ATOM 113 O ASP A 41 43.230 42.108 22.051 1.00 42.08 O
ANISOU 113 O ASP A 41 3141 5921 6925 576 368 -1172 O
ATOM 114 CB ASP A 41 40.742 41.086 21.382 1.00 36.21 C
ANISOU 114 CB ASP A 41 2778 4819 6161 651 441 -1176 C
ATOM 115 CG ASP A 41 40.790 40.687 22.849 1.00 39.39 C
ANISOU 115 CG ASP A 41 3193 5235 6540 726 358 -1196 C
ATOM 116 OD1 ASP A 41 40.854 41.581 23.718 1.00 38.21 O
ANISOU 116 OD1 ASP A 41 2991 5109 6416 619 278 -1218 O
ATOM 117 OD2 ASP A 41 40.770 39.471 23.133 1.00 44.30 O
ANISOU 117 OD2 ASP A 41 3882 5840 7110 893 383 -1189 O
ATOM 118 N GLN A 42 42.767 44.227 21.438 1.00 33.23 N
ANISOU 118 N GLN A 42 2027 4705 5894 261 391 -1194 N
ATOM 119 CA GLN A 42 44.066 44.758 21.831 1.00 35.70 C
ANISOU 119 CA GLN A 42 2144 5216 6205 184 362 -1215 C
ATOM 120 C GLN A 42 43.941 45.840 22.898 1.00 34.98 C
ANISOU 120 C GLN A 42 2048 5108 6133 11 305 -1267 C
ATOM 121 O GLN A 42 44.889 46.601 23.120 1.00 45.28 O
ANISOU 121 O GLN A 42 3204 6561 7439 -126 300 -1301 O
ATOM 122 CB GLN A 42 44.818 45.293 20.609 1.00 36.84 C
ANISOU 122 CB GLN A 42 2182 5440 6375 105 444 -1195 C
ATOM 123 CG GLN A 42 45.278 44.211 19.628 1.00 44.95 C
ANISOU 123 CG GLN A 42 3170 6536 7373 273 501 -1149 C
ATOM 124 CD GLN A 42 46.368 43.305 20.193 1.00 54.90 C
ANISOU 124 CD GLN A 42 4284 8004 8571 424 464 -1138 C
ATOM 125 OE1 GLN A 42 46.771 43.436 21.349 1.00 62.86 O
ANISOU 125 OE1 GLN A 42 5208 9126 9550 409 387 -1165 O
ATOM 126 NE2 GLN A 42 46.850 42.382 19.370 1.00 53.65 N
ANISOU 126 NE2 GLN A 42 4094 7907 8384 577 529 -1093 N
ATOM 127 N LYS A 43 42.786 45.917 23.566 1.00 33.75 N
ANISOU 127 N LYS A 43 2054 4781 5988 5 267 -1279 N
ATOM 128 CA LYS A 43 42.515 46.920 24.597 1.00 34.03 C
ANISOU 128 CA LYS A 43 2119 4767 6042 -155 222 -1329 C
ATOM 129 C LYS A 43 42.700 48.340 24.072 1.00 43.70 C
ANISOU 129 C LYS A 43 3333 5955 7316 -368 300 -1343 C
ATOM 130 O LYS A 43 43.069 49.248 24.821 1.00 49.74 O
ANISOU 130 O LYS A 43 4054 6759 8087 -538 287 -1399 O
ATOM 131 CB LYS A 43 43.383 46.698 25.837 1.00 35.84 C
ANISOU 131 CB LYS A 43 2206 5190 6224 -149 132 -1373 C
ATOM 132 CG LYS A 43 42.990 45.474 26.634 1.00 41.65 C
ANISOU 132 CG LYS A 43 2996 5917 6912 52 61 -1358 C
ATOM 133 CD LYS A 43 43.811 45.369 27.906 1.00 52.87 C
ANISOU 133 CD LYS A 43 4268 7545 8275 57 -26 -1395 C
ATOM 134 CE LYS A 43 43.196 44.365 28.864 1.00 58.39 C
ANISOU 134 CE LYS A 43 5063 8188 8935 235 -92 -1383 C
ATOM 135 NZ LYS A 43 43.951 44.278 30.140 1.00 64.91 N
ANISOU 135 NZ LYS A 43 5740 9231 9693 250 -179 -1412 N
ATOM 136 N LEU A 44 42.446 48.541 22.783 1.00 41.09 N
ANISOU 136 N LEU A 44 3049 5548 7014 -366 392 -1295 N
ATOM 137 CA LEU A 44 42.585 49.865 22.197 1.00 39.76 C
ANISOU 137 CA LEU A 44 2891 5326 6889 -549 490 -1296 C
ATOM 138 C LEU A 44 41.459 50.773 22.667 1.00 33.85 C
ANISOU 138 C LEU A 44 2323 4371 6167 -641 515 -1296 C
ATOM 139 O LEU A 44 40.295 50.373 22.704 1.00 34.03 O
ANISOU 139 O LEU A 44 2486 4261 6183 -536 495 -1259 O
ATOM 140 CB LEU A 44 42.595 49.767 20.671 1.00 37.87 C
ANISOU 140 CB LEU A 44 2652 5072 6664 -497 583 -1234 C
ATOM 141 CG LEU A 44 43.724 48.915 20.094 1.00 37.14 C
ANISOU 141 CG LEU A 44 2390 5176 6547 -405 576 -1227 C
ATOM 142 CD1 LEU A 44 43.594 48.790 18.585 1.00 34.97 C
ANISOU 142 CD1 LEU A 44 2134 4868 6285 -351 670 -1166 C
ATOM 143 CD2 LEU A 44 45.077 49.497 20.477 1.00 37.07 C
ANISOU 143 CD2 LEU A 44 2196 5356 6531 -546 572 -1282 C
ATOM 144 N SER A 45 41.820 51.999 23.050 1.00 34.95 N
ANISOU 144 N SER A 45 2460 4489 6331 -843 569 -1340 N
ATOM 145 CA SER A 45 40.834 53.020 23.378 1.00 39.86 C
ANISOU 145 CA SER A 45 3264 4901 6979 -937 630 -1330 C
ATOM 146 C SER A 45 40.400 53.829 22.163 1.00 40.78 C
ANISOU 146 C SER A 45 3480 4890 7125 -965 779 -1256 C
ATOM 147 O SER A 45 39.288 54.373 22.163 1.00 41.56 O
ANISOU 147 O SER A 45 3750 4809 7231 -952 834 -1206 O
ATOM 148 CB SER A 45 41.381 53.967 24.455 1.00 49.16 C
ANISOU 148 CB SER A 45 4420 6098 8160 -1152 637 -1420 C
ATOM 149 OG SER A 45 41.344 53.366 25.739 1.00 64.84 O
ANISOU 149 OG SER A 45 6371 8150 10113 -1115 503 -1473 O
ATOM 150 N LYS A 46 41.240 53.904 21.129 1.00 46.43 N
ANISOU 150 N LYS A 46 4088 5702 7850 -988 847 -1241 N
ATOM 151 CA LYS A 46 40.965 54.675 19.920 1.00 49.40 C
ANISOU 151 CA LYS A 46 4541 5978 8249 -1010 997 -1168 C
ATOM 152 C LYS A 46 41.640 53.987 18.740 1.00 46.87 C
ANISOU 152 C LYS A 46 4088 5798 7923 -923 1006 -1137 C
ATOM 153 O LYS A 46 42.443 53.068 18.917 1.00 49.34 O
ANISOU 153 O LYS A 46 4250 6281 8216 -869 913 -1177 O
ATOM 154 CB LYS A 46 41.454 56.123 20.058 1.00 57.87 C
ANISOU 154 CB LYS A 46 5657 6979 9352 -1235 1132 -1205 C
ATOM 155 CG LYS A 46 40.585 56.964 20.975 1.00 70.74 C
ANISOU 155 CG LYS A 46 7469 8419 10989 -1312 1172 -1212 C
ATOM 156 CD LYS A 46 41.231 58.280 21.367 1.00 79.19 C
ANISOU 156 CD LYS A 46 8577 9431 12080 -1565 1303 -1282 C
ATOM 157 CE LYS A 46 40.279 59.067 22.257 1.00 78.83 C
ANISOU 157 CE LYS A 46 8736 9177 12039 -1623 1355 -1280 C
ATOM 158 NZ LYS A 46 40.819 60.373 22.724 1.00 74.39 N
ANISOU 158 NZ LYS A 46 8249 8530 11486 -1881 1502 -1357 N
ATOM 159 N VAL A 47 41.312 54.443 17.536 1.00 45.66 N
ANISOU 159 N VAL A 47 3994 5576 7780 -899 1127 -1058 N
ATOM 160 CA VAL A 47 41.944 53.855 16.346 1.00 46.12 C
ANISOU 160 CA VAL A 47 3931 5760 7832 -825 1148 -1027 C
ATOM 161 C VAL A 47 43.413 54.266 16.308 1.00 49.04 C
ANISOU 161 C VAL A 47 4146 6264 8222 -974 1180 -1091 C
ATOM 162 O VAL A 47 43.733 55.450 16.530 1.00 54.48 O
ANISOU 162 O VAL A 47 4873 6890 8936 -1158 1278 -1122 O
ATOM 163 CB VAL A 47 41.199 54.277 15.068 1.00 49.59 C
ANISOU 163 CB VAL A 47 4467 6108 8268 -761 1271 -924 C
ATOM 164 CG1 VAL A 47 39.980 55.131 15.402 1.00 50.29 C
ANISOU 164 CG1 VAL A 47 4746 6010 8351 -769 1336 -871 C
ATOM 165 CG2 VAL A 47 42.133 54.968 14.057 1.00 47.39 C
ANISOU 165 CG2 VAL A 47 4115 5874 8016 -854 1397 -907 C
ATOM 166 N PRO A 48 44.336 53.334 16.082 1.00 49.90 N
ANISOU 166 N PRO A 48 4083 6562 8313 -910 1110 -1115 N
ATOM 167 CA PRO A 48 45.759 53.690 16.091 1.00 56.95 C
ANISOU 167 CA PRO A 48 4806 7621 9210 -1052 1133 -1177 C
ATOM 168 C PRO A 48 46.132 54.523 14.875 1.00 63.36 C
ANISOU 168 C PRO A 48 5619 8404 10052 -1139 1285 -1140 C
ATOM 169 O PRO A 48 45.748 54.215 13.744 1.00 65.44 O
ANISOU 169 O PRO A 48 5915 8632 10319 -1018 1332 -1061 O
ATOM 170 CB PRO A 48 46.468 52.329 16.075 1.00 55.06 C
ANISOU 170 CB PRO A 48 4400 7587 8933 -901 1024 -1185 C
ATOM 171 CG PRO A 48 45.426 51.343 16.519 1.00 48.92 C
ANISOU 171 CG PRO A 48 3725 6728 8133 -720 932 -1157 C
ATOM 172 CD PRO A 48 44.135 51.881 15.995 1.00 50.29 C
ANISOU 172 CD PRO A 48 4091 6689 8328 -708 1007 -1096 C
ATOM 173 N ASP A 49 46.888 55.592 15.121 1.00 66.73 N
ANISOU 173 N ASP A 49 6012 8848 10492 -1360 1369 -1203 N
ATOM 174 CA ASP A 49 47.419 56.412 14.042 1.00 72.29 C
ANISOU 174 CA ASP A 49 6721 9534 11210 -1456 1516 -1174 C
ATOM 175 C ASP A 49 48.597 55.758 13.332 1.00 72.06 C
ANISOU 175 C ASP A 49 6522 9722 11134 -1400 1465 -1165 C
ATOM 176 O ASP A 49 49.049 56.282 12.307 1.00 74.49 O
ANISOU 176 O ASP A 49 6834 10025 11443 -1446 1568 -1128 O
ATOM 177 CB ASP A 49 47.828 57.786 14.584 1.00 73.21 C
ANISOU 177 CB ASP A 49 6926 9577 11312 -1701 1613 -1236 C
ATOM 178 CG ASP A 49 46.632 58.665 14.907 1.00 74.81 C
ANISOU 178 CG ASP A 49 7348 9516 11561 -1748 1727 -1210 C
ATOM 179 OD1 ASP A 49 45.511 58.330 14.469 1.00 75.02 O
ANISOU 179 OD1 ASP A 49 7475 9423 11607 -1573 1731 -1116 O
ATOM 180 OD2 ASP A 49 46.809 59.683 15.608 1.00 78.99 O
ANISOU 180 OD2 ASP A 49 7983 9963 12066 -1931 1792 -1268 O
ATOM 181 N ASP A 50 49.100 54.631 13.843 1.00 69.66 N
ANISOU 181 N ASP A 50 6078 9604 10785 -1291 1317 -1188 N
ATOM 182 CA ASP A 50 50.182 53.910 13.182 1.00 70.70 C
ANISOU 182 CA ASP A 50 6057 9940 10866 -1207 1273 -1162 C
ATOM 183 C ASP A 50 49.720 53.157 11.943 1.00 67.05 C
ANISOU 183 C ASP A 50 5621 9434 10421 -1017 1299 -1073 C
ATOM 184 O ASP A 50 50.567 52.729 11.152 1.00 65.42 O
ANISOU 184 O ASP A 50 5319 9360 10179 -959 1297 -1037 O
ATOM 185 CB ASP A 50 50.837 52.922 14.148 1.00 76.89 C
ANISOU 185 CB ASP A 50 6698 10933 11585 -1124 1125 -1196 C
ATOM 186 CG ASP A 50 51.561 53.609 15.287 1.00 86.81 C
ANISOU 186 CG ASP A 50 7893 12300 12791 -1315 1089 -1281 C
ATOM 187 OD1 ASP A 50 51.926 54.792 15.134 1.00 89.74 O
ANISOU 187 OD1 ASP A 50 8306 12629 13163 -1521 1185 -1316 O
ATOM 188 OD2 ASP A 50 51.772 52.960 16.333 1.00 92.07 O
ANISOU 188 OD2 ASP A 50 8479 13098 13407 -1256 972 -1310 O
ATOM 189 N ILE A 51 48.417 52.985 11.763 1.00 60.60 N
ANISOU 189 N ILE A 51 4934 8447 9646 -923 1323 -1035 N
ATOM 190 CA ILE A 51 47.901 52.199 10.636 1.00 51.42 C
ANISOU 190 CA ILE A 51 3809 7256 8473 -745 1338 -956 C
ATOM 191 C ILE A 51 48.218 52.922 9.331 1.00 54.37 C
ANISOU 191 C ILE A 51 4199 7609 8852 -798 1459 -899 C
ATOM 192 O ILE A 51 47.893 54.117 9.192 1.00 60.59 O
ANISOU 192 O ILE A 51 5075 8268 9678 -924 1573 -891 O
ATOM 193 CB ILE A 51 46.396 51.976 10.790 1.00 49.46 C
ANISOU 193 CB ILE A 51 3696 6846 8249 -655 1341 -931 C
ATOM 194 CG1 ILE A 51 46.085 51.419 12.179 1.00 59.28 C
ANISOU 194 CG1 ILE A 51 4956 8091 9479 -620 1218 -986 C
ATOM 195 CG2 ILE A 51 45.888 51.020 9.725 1.00 42.58 C
ANISOU 195 CG2 ILE A 51 2864 5979 7334 -480 1341 -863 C
ATOM 196 CD1 ILE A 51 44.607 51.315 12.471 1.00 62.45 C
ANISOU 196 CD1 ILE A 51 5537 8325 9866 -545 1197 -952 C
ATOM 197 N PRO A 52 48.844 52.260 8.361 1.00 50.31 N
ANISOU 197 N PRO A 52 3615 7206 8296 -702 1450 -854 N
ATOM 198 CA PRO A 52 49.216 52.947 7.119 1.00 42.13 C
ANISOU 198 CA PRO A 52 2587 6160 7262 -752 1560 -801 C
ATOM 199 C PRO A 52 48.008 53.393 6.312 1.00 41.73 C
ANISOU 199 C PRO A 52 2680 5949 7226 -706 1657 -729 C
ATOM 200 O PRO A 52 46.951 52.760 6.321 1.00 45.93 O
ANISOU 200 O PRO A 52 3287 6424 7741 -583 1622 -701 O
ATOM 201 CB PRO A 52 50.037 51.895 6.364 1.00 42.38 C
ANISOU 201 CB PRO A 52 2514 6349 7238 -629 1509 -766 C
ATOM 202 CG PRO A 52 49.624 50.601 6.949 1.00 46.46 C
ANISOU 202 CG PRO A 52 3032 6896 7726 -474 1405 -777 C
ATOM 203 CD PRO A 52 49.322 50.871 8.389 1.00 48.06 C
ANISOU 203 CD PRO A 52 3241 7060 7958 -546 1350 -848 C
ATOM 204 N SER A 53 48.199 54.496 5.583 1.00 47.60 N
ANISOU 204 N SER A 53 3464 6633 7988 -803 1787 -693 N
ATOM 205 CA SER A 53 47.121 55.200 4.896 1.00 45.70 C
ANISOU 205 CA SER A 53 3364 6245 7757 -771 1907 -612 C
ATOM 206 C SER A 53 46.546 54.437 3.709 1.00 44.17 C
ANISOU 206 C SER A 53 3191 6092 7499 -600 1893 -528 C
ATOM 207 O SER A 53 45.460 54.794 3.239 1.00 40.11 O
ANISOU 207 O SER A 53 2785 5490 6964 -537 1963 -454 O
ATOM 208 CB SER A 53 47.624 56.569 4.429 1.00 51.19 C
ANISOU 208 CB SER A 53 4102 6869 8480 -916 2064 -593 C
ATOM 209 OG SER A 53 46.707 57.184 3.543 1.00 60.31 O
ANISOU 209 OG SER A 53 5383 7909 9623 -848 2191 -489 O
ATOM 210 N SER A 54 47.231 53.411 3.212 1.00 46.12 N
ANISOU 210 N SER A 54 3343 6479 7701 -523 1811 -533 N
ATOM 211 CA SER A 54 46.728 52.633 2.087 1.00 45.42 C
ANISOU 211 CA SER A 54 3282 6438 7536 -382 1798 -467 C
ATOM 212 C SER A 54 45.902 51.428 2.520 1.00 49.03 C
ANISOU 212 C SER A 54 3777 6906 7948 -265 1699 -487 C
ATOM 213 O SER A 54 45.476 50.650 1.660 1.00 50.46 O
ANISOU 213 O SER A 54 3985 7137 8051 -162 1684 -449 O
ATOM 214 CB SER A 54 47.891 52.168 1.202 1.00 44.09 C
ANISOU 214 CB SER A 54 3013 6403 7337 -363 1786 -457 C
ATOM 215 OG SER A 54 48.740 51.271 1.898 1.00 40.91 O
ANISOU 215 OG SER A 54 2509 6100 6934 -343 1689 -515 O
ATOM 216 N THR A 55 45.656 51.268 3.819 1.00 38.19 N
ANISOU 216 N THR A 55 2409 5486 6614 -287 1638 -549 N
ATOM 217 CA THR A 55 44.967 50.086 4.322 1.00 37.07 C
ANISOU 217 CA THR A 55 2304 5348 6432 -182 1548 -578 C
ATOM 218 C THR A 55 43.554 49.996 3.762 1.00 36.38 C
ANISOU 218 C THR A 55 2331 5211 6281 -112 1577 -525 C
ATOM 219 O THR A 55 42.819 50.987 3.716 1.00 36.00 O
ANISOU 219 O THR A 55 2349 5083 6247 -147 1647 -480 O
ATOM 220 CB THR A 55 44.915 50.115 5.850 1.00 43.07 C
ANISOU 220 CB THR A 55 3053 6061 7249 -227 1484 -652 C
ATOM 221 OG1 THR A 55 46.248 50.155 6.375 1.00 44.38 O
ANISOU 221 OG1 THR A 55 3096 6318 7448 -292 1448 -701 O
ATOM 222 CG2 THR A 55 44.199 48.886 6.389 1.00 39.33 C
ANISOU 222 CG2 THR A 55 2628 5582 6734 -115 1401 -683 C
ATOM 223 N LYS A 56 43.175 48.787 3.343 1.00 35.43 N
ANISOU 223 N LYS A 56 2236 5146 6078 -14 1532 -528 N
ATOM 224 CA LYS A 56 41.852 48.522 2.802 1.00 36.30 C
ANISOU 224 CA LYS A 56 2440 5254 6100 43 1547 -490 C
ATOM 225 C LYS A 56 40.928 47.806 3.776 1.00 34.22 C
ANISOU 225 C LYS A 56 2241 4942 5818 79 1485 -544 C
ATOM 226 O LYS A 56 39.706 47.928 3.644 1.00 32.98 O
ANISOU 226 O LYS A 56 2159 4772 5599 100 1500 -516 O
ATOM 227 CB LYS A 56 41.969 47.687 1.517 1.00 37.12 C
ANISOU 227 CB LYS A 56 2537 5462 6106 103 1560 -464 C
ATOM 228 CG LYS A 56 42.992 48.227 0.523 1.00 43.35 C
ANISOU 228 CG LYS A 56 3254 6308 6907 77 1613 -417 C
ATOM 229 CD LYS A 56 42.363 48.485 -0.835 1.00 52.52 C
ANISOU 229 CD LYS A 56 4447 7537 7970 105 1669 -343 C
ATOM 230 CE LYS A 56 42.160 47.197 -1.616 1.00 58.90 C
ANISOU 230 CE LYS A 56 5269 8436 8676 167 1651 -355 C
ATOM 231 NZ LYS A 56 43.407 46.748 -2.293 1.00 60.65 N
ANISOU 231 NZ LYS A 56 5418 8717 8908 178 1661 -356 N
ATOM 232 N ASN A 57 41.472 47.076 4.749 1.00 33.54 N
ANISOU 232 N ASN A 57 2126 4842 5777 93 1418 -617 N
ATOM 233 CA ASN A 57 40.673 46.289 5.681 1.00 36.02 C
ANISOU 233 CA ASN A 57 2506 5107 6073 134 1362 -676 C
ATOM 234 C ASN A 57 41.234 46.468 7.082 1.00 35.93 C
ANISOU 234 C ASN A 57 2447 5047 6156 105 1302 -733 C
ATOM 235 O ASN A 57 42.411 46.181 7.319 1.00 37.40 O
ANISOU 235 O ASN A 57 2546 5290 6375 112 1276 -757 O
ATOM 236 CB ASN A 57 40.674 44.807 5.291 1.00 34.27 C
ANISOU 236 CB ASN A 57 2315 4933 5773 213 1353 -709 C
ATOM 237 CG ASN A 57 40.435 44.591 3.811 1.00 36.82 C
ANISOU 237 CG ASN A 57 2656 5333 6003 225 1413 -660 C
ATOM 238 OD1 ASN A 57 39.313 44.721 3.326 1.00 32.19 O
ANISOU 238 OD1 ASN A 57 2131 4763 5338 218 1437 -634 O
ATOM 239 ND2 ASN A 57 41.494 44.246 3.086 1.00 42.52 N
ANISOU 239 ND2 ASN A 57 3316 6118 6723 248 1438 -645 N
ATOM 240 N ILE A 58 40.393 46.933 8.004 1.00 32.20 N
ANISOU 240 N ILE A 58 2027 4489 5717 76 1280 -754 N
ATOM 241 CA ILE A 58 40.760 47.117 9.404 1.00 35.57 C
ANISOU 241 CA ILE A 58 2424 4872 6217 42 1213 -811 C
ATOM 242 C ILE A 58 39.740 46.383 10.263 1.00 33.84 C
ANISOU 242 C ILE A 58 2319 4588 5951 98 1142 -846 C
ATOM 243 O ILE A 58 38.532 46.611 10.128 1.00 31.38 O
ANISOU 243 O ILE A 58 2105 4225 5592 98 1157 -819 O
ATOM 244 CB ILE A 58 40.817 48.602 9.797 1.00 38.53 C
ANISOU 244 CB ILE A 58 2811 5179 6649 -75 1238 -784 C
ATOM 245 CG1 ILE A 58 41.958 49.316 9.074 1.00 41.95 C
ANISOU 245 CG1 ILE A 58 3133 5674 7132 -149 1313 -764 C
ATOM 246 CG2 ILE A 58 40.990 48.750 11.293 1.00 39.85 C
ANISOU 246 CG2 ILE A 58 2993 5300 6850 -121 1147 -839 C
ATOM 247 CD1 ILE A 58 42.048 50.796 9.390 1.00 39.85 C
ANISOU 247 CD1 ILE A 58 2899 5326 6916 -281 1371 -745 C
ATOM 248 N ASP A 59 40.219 45.512 11.147 1.00 32.50 N
ANISOU 248 N ASP A 59 2132 4431 5785 151 1069 -902 N
ATOM 249 CA ASP A 59 39.375 44.842 12.131 1.00 31.57 C
ANISOU 249 CA ASP A 59 2123 4242 5631 199 1001 -941 C
ATOM 250 C ASP A 59 39.719 45.427 13.496 1.00 35.67 C
ANISOU 250 C ASP A 59 2625 4724 6202 148 918 -966 C
ATOM 251 O ASP A 59 40.794 45.157 14.042 1.00 37.99 O
ANISOU 251 O ASP A 59 2822 5090 6521 166 878 -994 O
ATOM 252 CB ASP A 59 39.581 43.329 12.094 1.00 30.46 C
ANISOU 252 CB ASP A 59 2000 4133 5441 314 1003 -981 C
ATOM 253 CG ASP A 59 38.556 42.571 12.924 1.00 32.14 C
ANISOU 253 CG ASP A 59 2349 4261 5602 360 958 -1023 C
ATOM 254 OD1 ASP A 59 37.851 43.196 13.745 1.00 31.35 O
ANISOU 254 OD1 ASP A 59 2309 4090 5515 311 900 -1025 O
ATOM 255 OD2 ASP A 59 38.453 41.340 12.746 1.00 39.12 O
ANISOU 255 OD2 ASP A 59 3291 5144 6430 443 992 -1057 O
ATOM 256 N LEU A 60 38.815 46.249 14.032 1.00 20.69 N
ANISOU 256 N LEU A 60 1816 2957 3086 26 1058 -502 N
ATOM 257 CA LEU A 60 38.996 46.885 15.331 1.00 20.60 C
ANISOU 257 CA LEU A 60 1831 2865 3133 -12 1019 -516 C
ATOM 258 C LEU A 60 38.095 46.279 16.400 1.00 18.41 C
ANISOU 258 C LEU A 60 1661 2501 2833 32 959 -540 C
ATOM 259 O LEU A 60 37.900 46.886 17.457 1.00 27.28 O
ANISOU 259 O LEU A 60 2844 3543 3976 2 922 -535 O
ATOM 260 CB LEU A 60 38.737 48.389 15.231 1.00 30.70 C
ANISOU 260 CB LEU A 60 3131 4102 4432 -93 1059 -446 C
ATOM 261 CG LEU A 60 39.775 49.288 14.560 1.00 36.22 C
ANISOU 261 CG LEU A 60 3736 4856 5170 -167 1108 -416 C
ATOM 262 CD1 LEU A 60 39.237 50.701 14.416 1.00 35.41 C
ANISOU 262 CD1 LEU A 60 3687 4692 5076 -238 1145 -338 C
ATOM 263 CD2 LEU A 60 41.073 49.292 15.351 1.00 37.86 C
ANISOU 263 CD2 LEU A 60 3867 5071 5447 -190 1054 -469 C
ATOM 264 N SER A 61 37.554 45.091 16.151 1.00 24.16 N
ANISOU 264 N SER A 61 2419 3245 3516 97 951 -568 N
ATOM 265 CA SER A 61 36.526 44.547 17.020 1.00 22.71 C
ANISOU 265 CA SER A 61 2344 2982 3302 127 913 -579 C
ATOM 266 C SER A 61 37.094 44.167 18.387 1.00 23.88 C
ANISOU 266 C SER A 61 2527 3073 3473 140 829 -626 C
ATOM 267 O SER A 61 38.294 43.936 18.557 1.00 31.34 O
ANISOU 267 O SER A 61 3403 4050 4453 152 787 -664 O
ATOM 268 CB SER A 61 35.860 43.335 16.366 1.00 27.72 C
ANISOU 268 CB SER A 61 2999 3646 3886 185 924 -598 C
ATOM 269 OG SER A 61 36.806 42.335 16.034 1.00 29.94 O
ANISOU 269 OG SER A 61 3222 3984 4169 235 890 -646 O
ATOM 270 N PHE A 62 36.195 44.124 19.373 1.00 23.19 N
ANISOU 270 N PHE A 62 2547 2901 3361 139 804 -622 N
ATOM 271 CA PHE A 62 36.509 43.703 20.739 1.00 23.94 C
ANISOU 271 CA PHE A 62 2708 2932 3457 154 723 -661 C
ATOM 272 C PHE A 62 37.544 44.611 21.401 1.00 26.22 C
ANISOU 272 C PHE A 62 2960 3207 3797 113 681 -670 C
ATOM 273 O PHE A 62 38.357 44.161 22.212 1.00 37.69 O
ANISOU 273 O PHE A 62 4416 4642 5263 136 601 -713 O
ATOM 274 CB PHE A 62 36.944 42.233 20.770 1.00 19.35 C
ANISOU 274 CB PHE A 62 2126 2368 2859 223 669 -710 C
ATOM 275 CG PHE A 62 35.849 41.282 20.369 1.00 20.73 C
ANISOU 275 CG PHE A 62 2360 2533 2982 256 697 -707 C
ATOM 276 CD1 PHE A 62 34.968 40.786 21.311 1.00 20.28 C
ANISOU 276 CD1 PHE A 62 2422 2398 2885 259 674 -709 C
ATOM 277 CD2 PHE A 62 35.684 40.913 19.041 1.00 16.02 C
ANISOU 277 CD2 PHE A 62 1701 2008 2375 278 749 -703 C
ATOM 278 CE1 PHE A 62 33.949 39.929 20.941 1.00 22.48 C
ANISOU 278 CE1 PHE A 62 2749 2667 3123 278 701 -707 C
ATOM 279 CE2 PHE A 62 34.671 40.052 18.669 1.00 20.99 C
ANISOU 279 CE2 PHE A 62 2384 2628 2962 303 768 -705 C
ATOM 280 CZ PHE A 62 33.800 39.565 19.618 1.00 19.03 C
ANISOU 280 CZ PHE A 62 2247 2300 2683 301 744 -707 C
ATOM 281 N ASN A 63 37.500 45.902 21.073 1.00 23.79 N
ANISOU 281 N ASN A 63 2621 2900 3518 53 730 -629 N
ATOM 282 CA ASN A 63 38.264 46.949 21.731 1.00 19.64 C
ANISOU 282 CA ASN A 63 2077 2345 3042 -2 696 -631 C
ATOM 283 C ASN A 63 37.314 47.939 22.399 1.00 19.97 C
ANISOU 283 C ASN A 63 2214 2301 3071 -42 714 -601 C
ATOM 284 O ASN A 63 36.261 48.257 21.837 1.00 21.03 O
ANISOU 284 O ASN A 63 2379 2429 3183 -46 780 -560 O
ATOM 285 CB ASN A 63 39.165 47.697 20.733 1.00 23.78 C
ANISOU 285 CB ASN A 63 2477 2940 3619 -49 740 -610 C
ATOM 286 CG ASN A 63 40.293 46.832 20.195 1.00 26.46 C
ANISOU 286 CG ASN A 63 2706 3368 3980 -11 720 -653 C
ATOM 287 OD1 ASN A 63 41.214 46.473 20.928 1.00 26.28 O
ANISOU 287 OD1 ASN A 63 2654 3343 3988 6 641 -705 O
ATOM 288 ND2 ASN A 63 40.231 46.503 18.909 1.00 23.19 N
ANISOU 288 ND2 ASN A 63 2229 3033 3549 5 789 -635 N
ATOM 289 N PRO A 64 37.646 48.435 23.592 1.00 24.16 N
ANISOU 289 N PRO A 64 2795 2768 3617 -66 654 -626 N
ATOM 290 CA PRO A 64 36.749 49.376 24.304 1.00 26.06 C
ANISOU 290 CA PRO A 64 3132 2925 3845 -98 670 -608 C
ATOM 291 C PRO A 64 36.830 50.791 23.743 1.00 29.20 C
ANISOU 291 C PRO A 64 3490 3313 4291 -161 716 -565 C
ATOM 292 O PRO A 64 37.343 51.731 24.363 1.00 30.20 O
ANISOU 292 O PRO A 64 3626 3392 4456 -210 682 -575 O
ATOM 293 CB PRO A 64 37.256 49.279 25.747 1.00 24.79 C
ANISOU 293 CB PRO A 64 3036 2707 3676 -98 580 -657 C
ATOM 294 CG PRO A 64 38.703 48.951 25.605 1.00 28.32 C
ANISOU 294 CG PRO A 64 3382 3208 4170 -96 519 -689 C
ATOM 295 CD PRO A 64 38.826 48.073 24.397 1.00 25.20 C
ANISOU 295 CD PRO A 64 2902 2899 3774 -57 560 -678 C
ATOM 296 N LEU A 65 36.291 50.966 22.535 1.00 25.18 N
ANISOU 296 N LEU A 65 2944 2844 3778 -162 791 -516 N
ATOM 297 CA LEU A 65 36.376 52.261 21.865 1.00 25.52 C
ANISOU 297 CA LEU A 65 2955 2878 3862 -220 836 -466 C
ATOM 298 C LEU A 65 35.449 53.285 22.514 1.00 26.23 C
ANISOU 298 C LEU A 65 3142 2872 3953 -238 845 -452 C
ATOM 299 O LEU A 65 35.838 54.442 22.722 1.00 24.06 O
ANISOU 299 O LEU A 65 2870 2547 3723 -295 836 -439 O
ATOM 300 CB LEU A 65 36.060 52.101 20.376 1.00 23.69 C
ANISOU 300 CB LEU A 65 2667 2718 3615 -209 909 -417 C
ATOM 301 CG LEU A 65 37.043 51.260 19.557 1.00 24.77 C
ANISOU 301 CG LEU A 65 2698 2958 3756 -196 914 -430 C
ATOM 302 CD1 LEU A 65 36.668 51.274 18.080 1.00 21.39 C
ANISOU 302 CD1 LEU A 65 2229 2596 3302 -192 990 -378 C
ATOM 303 CD2 LEU A 65 38.468 51.758 19.767 1.00 23.78 C
ANISOU 303 CD2 LEU A 65 2493 2850 3693 -253 883 -448 C
ATOM 304 N LYS A 66 34.211 52.880 22.816 1.00 21.31 N
ANISOU 304 N LYS A 66 2594 2222 3281 -191 864 -457 N
ATOM 305 CA LYS A 66 33.228 53.667 23.565 1.00 20.51 C
ANISOU 305 CA LYS A 66 2585 2034 3173 -192 873 -459 C
ATOM 306 C LYS A 66 32.660 54.840 22.774 1.00 25.18 C
ANISOU 306 C LYS A 66 3176 2598 3792 -212 923 -403 C
ATOM 307 O LYS A 66 31.477 55.167 22.908 1.00 26.72 O
ANISOU 307 O LYS A 66 3430 2752 3972 -184 953 -397 O
ATOM 308 CB LYS A 66 33.823 54.176 24.886 1.00 21.36 C
ANISOU 308 CB LYS A 66 2745 2072 3297 -223 811 -504 C
ATOM 309 CG LYS A 66 34.290 53.076 25.827 1.00 22.33 C
ANISOU 309 CG LYS A 66 2893 2207 3384 -196 749 -559 C
ATOM 310 CD LYS A 66 34.410 53.604 27.251 1.00 35.36 C
ANISOU 310 CD LYS A 66 4632 3777 5028 -214 695 -604 C
ATOM 311 CE LYS A 66 35.336 52.747 28.102 1.00 48.12 C
ANISOU 311 CE LYS A 66 6256 5404 6623 -203 610 -653 C
ATOM 312 NZ LYS A 66 34.845 51.353 28.267 1.00 55.57 N
ANISOU 312 NZ LYS A 66 7236 6377 7502 -147 611 -665 N
ATOM 313 N ILE A 67 33.483 55.487 21.956 1.00 21.93 N
ANISOU 313 N ILE A 67 2701 2208 3423 -261 933 -363 N
ATOM 314 CA ILE A 67 33.024 56.628 21.171 1.00 19.37 C
ANISOU 314 CA ILE A 67 2386 1850 3123 -284 975 -302 C
ATOM 315 C ILE A 67 33.862 56.726 19.905 1.00 18.53 C
ANISOU 315 C ILE A 67 2193 1815 3034 -324 1005 -250 C
ATOM 316 O ILE A 67 35.090 56.602 19.941 1.00 32.09 O
ANISOU 316 O ILE A 67 3845 3568 4779 -368 984 -265 O
ATOM 317 CB ILE A 67 33.071 57.940 21.987 1.00 19.66 C
ANISOU 317 CB ILE A 67 2487 1779 3205 -326 949 -309 C
ATOM 318 CG1 ILE A 67 32.551 59.109 21.147 1.00 24.04 C
ANISOU 318 CG1 ILE A 67 3063 2287 3784 -343 986 -241 C
ATOM 319 CG2 ILE A 67 34.479 58.217 22.511 1.00 22.26 C
ANISOU 319 CG2 ILE A 67 2780 2099 3578 -392 899 -335 C
ATOM 320 CD1 ILE A 67 32.471 60.424 21.896 1.00 19.76 C
ANISOU 320 CD1 ILE A 67 2595 1627 3288 -376 961 -249 C
ATOM 321 N LEU A 68 33.186 56.943 18.781 1.00 22.13 N
ANISOU 321 N LEU A 68 2645 2293 3469 -307 1054 -191 N
ATOM 322 CA LEU A 68 33.851 57.167 17.503 1.00 18.96 C
ANISOU 322 CA LEU A 68 2178 1956 3072 -348 1094 -132 C
ATOM 323 C LEU A 68 34.045 58.669 17.325 1.00 23.06 C
ANISOU 323 C LEU A 68 2729 2396 3637 -416 1103 -77 C
ATOM 324 O LEU A 68 33.099 59.395 16.998 1.00 22.57 O
ANISOU 324 O LEU A 68 2729 2276 3569 -397 1117 -33 O
ATOM 325 CB LEU A 68 33.043 56.565 16.358 1.00 18.55 C
ANISOU 325 CB LEU A 68 2114 1972 2963 -294 1137 -98 C
ATOM 326 CG LEU A 68 33.079 55.036 16.280 1.00 26.40 C
ANISOU 326 CG LEU A 68 3063 3053 3914 -241 1133 -147 C
ATOM 327 CD1 LEU A 68 32.313 54.524 15.069 1.00 24.91 C
ANISOU 327 CD1 LEU A 68 2864 2931 3670 -194 1172 -114 C
ATOM 328 CD2 LEU A 68 34.514 54.540 16.257 1.00 19.46 C
ANISOU 328 CD2 LEU A 68 2100 2240 3053 -275 1124 -175 C
ATOM 329 N LYS A 69 35.272 59.133 17.540 1.00 32.38 N
ANISOU 329 N LYS A 69 3866 3571 4867 -494 1089 -80 N
ATOM 330 CA LYS A 69 35.576 60.554 17.484 1.00 31.95 C
ANISOU 330 CA LYS A 69 3846 3430 4864 -572 1091 -33 C
ATOM 331 C LYS A 69 35.689 61.035 16.042 1.00 24.78 C
ANISOU 331 C LYS A 69 2916 2559 3941 -612 1152 58 C
ATOM 332 O LYS A 69 36.081 60.287 15.141 1.00 24.89 O
ANISOU 332 O LYS A 69 2857 2683 3918 -607 1193 74 O
ATOM 333 CB LYS A 69 36.874 60.849 18.233 1.00 27.49 C
ANISOU 333 CB LYS A 69 3235 2849 4361 -651 1052 -73 C
ATOM 334 CG LYS A 69 36.848 60.417 19.683 1.00 29.11 C
ANISOU 334 CG LYS A 69 3471 3016 4573 -616 984 -161 C
ATOM 335 CD LYS A 69 35.986 61.341 20.517 1.00 21.71 C
ANISOU 335 CD LYS A 69 2648 1950 3650 -604 956 -171 C
ATOM 336 CE LYS A 69 36.464 62.772 20.394 1.00 22.78 C
ANISOU 336 CE LYS A 69 2809 1999 3850 -695 954 -129 C
ATOM 337 NZ LYS A 69 35.697 63.711 21.253 1.00 22.95 N
ANISOU 337 NZ LYS A 69 2943 1888 3890 -679 921 -149 N
ATOM 338 N SER A 70 35.329 62.300 15.834 1.00 22.66 N
ANISOU 338 N SER A 70 2721 2192 3698 -648 1157 119 N
ATOM 339 CA SER A 70 35.401 62.899 14.508 1.00 23.39 C
ANISOU 339 CA SER A 70 2816 2301 3771 -692 1211 216 C
ATOM 340 C SER A 70 36.807 62.788 13.933 1.00 24.72 C
ANISOU 340 C SER A 70 2885 2554 3954 -785 1251 234 C
ATOM 341 O SER A 70 37.800 62.907 14.653 1.00 24.56 O
ANISOU 341 O SER A 70 2814 2525 3993 -849 1226 189 O
ATOM 342 CB SER A 70 34.983 64.369 14.569 1.00 24.17 C
ANISOU 342 CB SER A 70 3016 2258 3909 -728 1197 273 C
ATOM 343 OG SER A 70 33.660 64.500 15.052 1.00 28.28 O
ANISOU 343 OG SER A 70 3619 2706 4418 -635 1164 252 O
ATOM 344 N TYR A 71 36.877 62.548 12.623 1.00 25.48 N
ANISOU 344 N TYR A 71 2950 2737 3995 -791 1314 297 N
ATOM 345 CA TYR A 71 38.105 62.521 11.829 1.00 27.56 C
ANISOU 345 CA TYR A 71 3121 3091 4261 -881 1374 328 C
ATOM 346 C TYR A 71 39.045 61.379 12.192 1.00 29.05 C
ANISOU 346 C TYR A 71 3186 3391 4462 -873 1370 241 C
ATOM 347 O TYR A 71 40.204 61.389 11.759 1.00 26.17 O
ANISOU 347 O TYR A 71 2726 3100 4118 -952 1414 247 O
ATOM 348 CB TYR A 71 38.873 63.845 11.926 1.00 26.64 C
ANISOU 348 CB TYR A 71 3020 2889 4213 -1009 1382 377 C
ATOM 349 CG TYR A 71 38.006 65.067 11.734 1.00 27.27 C
ANISOU 349 CG TYR A 71 3234 2833 4295 -1018 1371 456 C
ATOM 350 CD1 TYR A 71 37.382 65.316 10.518 1.00 28.83 C
ANISOU 350 CD1 TYR A 71 3488 3043 4423 -1000 1415 549 C
ATOM 351 CD2 TYR A 71 37.818 65.976 12.765 1.00 28.61 C
ANISOU 351 CD2 TYR A 71 3476 2860 4534 -1039 1310 436 C
ATOM 352 CE1 TYR A 71 36.588 66.439 10.337 1.00 30.53 C
ANISOU 352 CE1 TYR A 71 3829 3128 4642 -999 1395 622 C
ATOM 353 CE2 TYR A 71 37.027 67.100 12.595 1.00 34.16 C
ANISOU 353 CE2 TYR A 71 4303 3432 5243 -1039 1295 503 C
ATOM 354 CZ TYR A 71 36.416 67.325 11.380 1.00 38.52 C
ANISOU 354 CZ TYR A 71 4910 3997 5731 -1016 1336 598 C
ATOM 355 OH TYR A 71 35.631 68.445 11.209 1.00 44.66 O
ANISOU 355 OH TYR A 71 5813 4638 6517 -1007 1312 665 O
ATOM 356 N SER A 72 38.582 60.383 12.953 1.00 28.11 N
ANISOU 356 N SER A 72 3064 3288 4329 -778 1320 161 N
ATOM 357 CA SER A 72 39.472 59.309 13.384 1.00 29.27 C
ANISOU 357 CA SER A 72 3104 3525 4491 -761 1302 78 C
ATOM 358 C SER A 72 39.954 58.457 12.217 1.00 32.37 C
ANISOU 358 C SER A 72 3406 4061 4832 -749 1368 85 C
ATOM 359 O SER A 72 41.059 57.903 12.273 1.00 29.88 O
ANISOU 359 O SER A 72 2979 3829 4544 -771 1374 34 O
ATOM 360 CB SER A 72 38.772 58.433 14.418 1.00 35.67 C
ANISOU 360 CB SER A 72 3954 4311 5289 -663 1235 1 C
ATOM 361 OG SER A 72 38.857 59.021 15.704 1.00 49.64 O
ANISOU 361 OG SER A 72 5768 5977 7117 -688 1170 -38 O
ATOM 362 N PHE A 73 39.151 58.339 11.158 1.00 32.60 N
ANISOU 362 N PHE A 73 3479 4121 4785 -709 1415 143 N
ATOM 363 CA PHE A 73 39.475 57.503 10.008 1.00 33.86 C
ANISOU 363 CA PHE A 73 3574 4417 4873 -679 1461 146 C
ATOM 364 C PHE A 73 39.771 58.311 8.749 1.00 32.17 C
ANISOU 364 C PHE A 73 3373 4239 4610 -745 1511 241 C
ATOM 365 O PHE A 73 39.800 57.739 7.655 1.00 36.75 O
ANISOU 365 O PHE A 73 3933 4926 5105 -708 1533 257 O
ATOM 366 CB PHE A 73 38.330 56.524 9.727 1.00 30.46 C
ANISOU 366 CB PHE A 73 3190 4014 4370 -565 1445 126 C
ATOM 367 CG PHE A 73 38.006 55.610 10.878 1.00 28.46 C
ANISOU 367 CG PHE A 73 2934 3734 4145 -495 1391 37 C
ATOM 368 CD1 PHE A 73 38.859 54.567 11.215 1.00 32.59 C
ANISOU 368 CD1 PHE A 73 3369 4331 4682 -468 1368 -43 C
ATOM 369 CD2 PHE A 73 36.847 55.784 11.616 1.00 21.02 C
ANISOU 369 CD2 PHE A 73 2088 2694 3204 -447 1340 33 C
ATOM 370 CE1 PHE A 73 38.563 53.722 12.273 1.00 31.93 C
ANISOU 370 CE1 PHE A 73 3301 4218 4613 -402 1304 -118 C
ATOM 371 CE2 PHE A 73 36.547 54.944 12.678 1.00 26.68 C
ANISOU 371 CE2 PHE A 73 2817 3389 3932 -386 1281 -45 C
ATOM 372 CZ PHE A 73 37.404 53.910 13.004 1.00 33.40 C
ANISOU 372 CZ PHE A 73 3589 4307 4793 -365 1261 -116 C
ATOM 373 N SER A 74 40.000 59.622 8.874 1.00 29.62 N
ANISOU 373 N SER A 74 3088 3828 4337 -842 1526 303 N
ATOM 374 CA SER A 74 40.109 60.498 7.711 1.00 36.38 C
ANISOU 374 CA SER A 74 3984 4696 5143 -907 1572 406 C
ATOM 375 C SER A 74 41.374 60.269 6.891 1.00 36.81 C
ANISOU 375 C SER A 74 3935 4885 5164 -959 1607 411 C
ATOM 376 O SER A 74 41.437 60.733 5.746 1.00 42.32 O
ANISOU 376 O SER A 74 4661 5625 5795 -998 1652 492 O
ATOM 377 CB SER A 74 40.039 61.961 8.156 1.00 34.19 C
ANISOU 377 CB SER A 74 3783 4273 4933 -999 1567 468 C
ATOM 378 OG SER A 74 40.901 62.207 9.253 1.00 44.03 O
ANISOU 378 OG SER A 74 4972 5478 6280 -1061 1535 410 O
ATOM 379 N ASN A 75 42.374 59.578 7.436 1.00 34.05 N
ANISOU 379 N ASN A 75 3471 4605 4862 -957 1589 328 N
ATOM 380 CA ASN A 75 43.572 59.255 6.672 1.00 38.92 C
ANISOU 380 CA ASN A 75 3979 5356 5452 -989 1625 326 C
ATOM 381 C ASN A 75 43.411 58.003 5.820 1.00 40.86 C
ANISOU 381 C ASN A 75 4192 5728 5604 -886 1637 298 C
ATOM 382 O ASN A 75 44.201 57.804 4.890 1.00 45.86 O
ANISOU 382 O ASN A 75 4758 6474 6194 -903 1681 319 O
ATOM 383 CB ASN A 75 44.770 59.084 7.612 1.00 39.84 C
ANISOU 383 CB ASN A 75 3979 5490 5667 -1028 1596 249 C
ATOM 384 CG ASN A 75 45.315 60.411 8.108 1.00 41.08 C
ANISOU 384 CG ASN A 75 4143 5557 5910 -1157 1595 288 C
ATOM 385 OD1 ASN A 75 45.271 61.414 7.396 1.00 40.53 O
ANISOU 385 OD1 ASN A 75 4129 5457 5814 -1235 1634 384 O
ATOM 386 ND2 ASN A 75 45.830 60.424 9.333 1.00 42.95 N
ANISOU 386 ND2 ASN A 75 4328 5745 6247 -1181 1544 213 N
ATOM 387 N PHE A 76 42.408 57.168 6.102 1.00 40.59 N
ANISOU 387 N PHE A 76 4207 5676 5541 -782 1599 253 N
ATOM 388 CA PHE A 76 42.228 55.896 5.400 1.00 38.18 C
ANISOU 388 CA PHE A 76 3875 5479 5153 -680 1595 215 C
ATOM 389 C PHE A 76 41.318 56.106 4.189 1.00 42.26 C
ANISOU 389 C PHE A 76 4477 6017 5565 -663 1629 290 C
ATOM 390 O PHE A 76 40.146 55.724 4.160 1.00 45.35 O
ANISOU 390 O PHE A 76 4941 6374 5915 -592 1602 282 O
ATOM 391 CB PHE A 76 41.676 54.842 6.352 1.00 32.04 C
ANISOU 391 CB PHE A 76 3104 4670 4399 -582 1531 125 C
ATOM 392 CG PHE A 76 42.462 54.716 7.625 1.00 34.03 C
ANISOU 392 CG PHE A 76 3288 4888 4755 -602 1494 52 C
ATOM 393 CD1 PHE A 76 43.807 54.389 7.588 1.00 37.99 C
ANISOU 393 CD1 PHE A 76 3672 5472 5290 -622 1501 13 C
ATOM 394 CD2 PHE A 76 41.862 54.930 8.854 1.00 36.79 C
ANISOU 394 CD2 PHE A 76 3688 5122 5169 -598 1454 21 C
ATOM 395 CE1 PHE A 76 44.541 54.276 8.754 1.00 35.59 C
ANISOU 395 CE1 PHE A 76 3300 5140 5083 -640 1460 -60 C
ATOM 396 CE2 PHE A 76 42.591 54.819 10.025 1.00 39.31 C
ANISOU 396 CE2 PHE A 76 3943 5411 5580 -619 1418 -50 C
ATOM 397 CZ PHE A 76 43.933 54.493 9.973 1.00 38.06 C
ANISOU 397 CZ PHE A 76 3666 5340 5456 -641 1417 -92 C
ATOM 398 N SER A 77 41.901 56.729 3.162 1.00 41.12 N
ANISOU 398 N SER A 77 4317 5930 5375 -733 1689 363 N
ATOM 399 CA SER A 77 41.151 57.059 1.957 1.00 41.45 C
ANISOU 399 CA SER A 77 4442 5993 5313 -733 1725 442 C
ATOM 400 C SER A 77 40.842 55.837 1.103 1.00 33.73 C
ANISOU 400 C SER A 77 3448 5129 4240 -633 1724 405 C
ATOM 401 O SER A 77 39.910 55.886 0.294 1.00 40.35 O
ANISOU 401 O SER A 77 4367 5972 4992 -608 1733 444 O
ATOM 402 CB SER A 77 41.920 58.090 1.128 1.00 48.68 C
ANISOU 402 CB SER A 77 5351 6938 6207 -843 1792 537 C
ATOM 403 OG SER A 77 43.271 57.701 0.953 1.00 58.90 O
ANISOU 403 OG SER A 77 6520 8335 7525 -861 1824 509 O
ATOM 404 N GLU A 78 41.594 54.750 1.256 1.00 32.56 N
ANISOU 404 N GLU A 78 3202 5061 4107 -571 1711 330 N
ATOM 405 CA GLU A 78 41.363 53.546 0.472 1.00 40.35 C
ANISOU 405 CA GLU A 78 4176 6140 5014 -466 1709 295 C
ATOM 406 C GLU A 78 40.650 52.459 1.266 1.00 40.76 C
ANISOU 406 C GLU A 78 4243 6157 5086 -367 1632 207 C
ATOM 407 O GLU A 78 40.542 51.326 0.787 1.00 47.60 O
ANISOU 407 O GLU A 78 5097 7081 5906 -272 1621 168 O
ATOM 408 CB GLU A 78 42.683 53.013 -0.081 1.00 50.55 C
ANISOU 408 CB GLU A 78 5367 7525 6313 -448 1762 283 C
ATOM 409 CG GLU A 78 42.613 52.679 -1.558 1.00 62.67 C
ANISOU 409 CG GLU A 78 6924 9139 7748 -404 1826 327 C
ATOM 410 CD GLU A 78 43.830 51.930 -2.041 1.00 65.36 C
ANISOU 410 CD GLU A 78 7181 9538 8115 -364 1888 288 C
ATOM 411 OE1 GLU A 78 44.543 51.345 -1.199 1.00 65.90 O
ANISOU 411 OE1 GLU A 78 7172 9601 8265 -342 1853 209 O
ATOM 412 OE2 GLU A 78 44.073 51.921 -3.265 1.00 64.12 O
ANISOU 412 OE2 GLU A 78 7045 9423 7896 -360 1964 322 O
ATOM 413 N LEU A 79 40.152 52.783 2.458 1.00 33.39 N
ANISOU 413 N LEU A 79 3345 5115 4225 -382 1584 182 N
ATOM 414 CA LEU A 79 39.521 51.792 3.321 1.00 27.01 C
ANISOU 414 CA LEU A 79 2554 4265 3443 -296 1514 103 C
ATOM 415 C LEU A 79 38.187 51.334 2.738 1.00 26.09 C
ANISOU 415 C LEU A 79 2514 4150 3247 -232 1492 105 C
ATOM 416 O LEU A 79 37.331 52.155 2.393 1.00 33.71 O
ANISOU 416 O LEU A 79 3555 5068 4186 -265 1510 162 O
ATOM 417 CB LEU A 79 39.315 52.377 4.720 1.00 26.19 C
ANISOU 417 CB LEU A 79 2475 4041 3437 -333 1482 86 C
ATOM 418 CG LEU A 79 38.965 51.408 5.856 1.00 24.71 C
ANISOU 418 CG LEU A 79 2291 3806 3293 -260 1414 2 C
ATOM 419 CD1 LEU A 79 40.134 50.480 6.128 1.00 23.01 C
ANISOU 419 CD1 LEU A 79 1983 3653 3108 -228 1397 -64 C
ATOM 420 CD2 LEU A 79 38.542 52.132 7.137 1.00 22.14 C
ANISOU 420 CD2 LEU A 79 2008 3353 3050 -296 1395 -2 C
ATOM 421 N GLN A 80 38.008 50.015 2.646 1.00 24.99 N
ANISOU 421 N GLN A 80 2361 4056 3079 -138 1452 44 N
ATOM 422 CA GLN A 80 36.804 49.411 2.086 1.00 26.17 C
ANISOU 422 CA GLN A 80 2570 4217 3155 -76 1423 31 C
ATOM 423 C GLN A 80 35.988 48.617 3.094 1.00 23.54 C
ANISOU 423 C GLN A 80 2271 3813 2862 -15 1350 -31 C
ATOM 424 O GLN A 80 34.768 48.524 2.947 1.00 29.52 O
ANISOU 424 O GLN A 80 3088 4539 3589 9 1326 -34 O
ATOM 425 CB GLN A 80 37.169 48.481 0.922 1.00 30.15 C
ANISOU 425 CB GLN A 80 3052 4816 3588 -9 1441 26 C
ATOM 426 CG GLN A 80 37.854 49.165 -0.253 1.00 35.62 C
ANISOU 426 CG GLN A 80 3729 5575 4230 -59 1516 92 C
ATOM 427 CD GLN A 80 38.517 48.177 -1.195 1.00 46.67 C
ANISOU 427 CD GLN A 80 5127 6982 5623 20 1570 82 C
ATOM 428 OE1 GLN A 80 38.407 46.965 -1.019 1.00 45.05 O
ANISOU 428 OE1 GLN A 80 4938 6734 5447 93 1547 11 O
ATOM 429 NE2 GLN A 80 39.214 48.691 -2.199 1.00 61.76 N
ANISOU 429 NE2 GLN A 80 7031 8930 7505 -20 1658 132 N
ATOM 430 N TRP A 81 36.631 48.041 4.106 1.00 21.35 N
ANISOU 430 N TRP A 81 1956 3504 2651 8 1318 -81 N
ATOM 431 CA TRP A 81 35.978 47.128 5.036 1.00 20.13 C
ANISOU 431 CA TRP A 81 1836 3290 2524 66 1250 -140 C
ATOM 432 C TRP A 81 36.445 47.484 6.438 1.00 25.61 C
ANISOU 432 C TRP A 81 2516 3906 3309 30 1234 -166 C
ATOM 433 O TRP A 81 37.648 47.453 6.714 1.00 30.68 O
ANISOU 433 O TRP A 81 3092 4572 3993 11 1247 -186 O
ATOM 434 CB TRP A 81 36.320 45.674 4.687 1.00 20.16 C
ANISOU 434 CB TRP A 81 1823 3336 2501 151 1228 -185 C
ATOM 435 CG TRP A 81 35.698 44.621 5.557 1.00 28.94 C
ANISOU 435 CG TRP A 81 2976 4385 3634 205 1162 -241 C
ATOM 436 CD1 TRP A 81 34.496 44.005 5.363 1.00 29.46 C
ANISOU 436 CD1 TRP A 81 3102 4431 3661 248 1127 -250 C
ATOM 437 CD2 TRP A 81 36.268 44.023 6.732 1.00 30.17 C
ANISOU 437 CD2 TRP A 81 3118 4493 3853 217 1124 -299 C
ATOM 438 NE1 TRP A 81 34.272 43.079 6.352 1.00 28.07 N
ANISOU 438 NE1 TRP A 81 2954 4194 3519 281 1074 -303 N
ATOM 439 CE2 TRP A 81 35.345 43.070 7.205 1.00 23.56 C
ANISOU 439 CE2 TRP A 81 2341 3605 3007 264 1071 -334 C
ATOM 440 CE3 TRP A 81 37.462 44.214 7.438 1.00 34.34 C
ANISOU 440 CE3 TRP A 81 3584 5019 4444 190 1131 -327 C
ATOM 441 CZ2 TRP A 81 35.577 42.310 8.352 1.00 31.19 C
ANISOU 441 CZ2 TRP A 81 3317 4516 4018 285 1026 -391 C
ATOM 442 CZ3 TRP A 81 37.691 43.454 8.578 1.00 34.28 C
ANISOU 442 CZ3 TRP A 81 3579 4960 4484 217 1081 -392 C
ATOM 443 CH2 TRP A 81 36.753 42.513 9.021 1.00 32.64 C
ANISOU 443 CH2 TRP A 81 3443 4700 4260 264 1031 -422 C
ATOM 444 N LEU A 82 35.504 47.835 7.314 1.00 20.41 N
ANISOU 444 N LEU A 82 1917 3153 2683 21 1209 -168 N
ATOM 445 CA LEU A 82 35.816 48.300 8.661 1.00 20.63 C
ANISOU 445 CA LEU A 82 1944 3098 2795 -15 1201 -189 C
ATOM 446 C LEU A 82 34.916 47.585 9.657 1.00 27.82 C
ANISOU 446 C LEU A 82 2912 3939 3719 32 1147 -234 C
ATOM 447 O LEU A 82 33.690 47.730 9.607 1.00 26.80 O
ANISOU 447 O LEU A 82 2845 3769 3568 46 1136 -214 O
ATOM 448 CB LEU A 82 35.643 49.817 8.776 1.00 19.14 C
ANISOU 448 CB LEU A 82 1778 2849 2643 -89 1247 -127 C
ATOM 449 CG LEU A 82 35.774 50.429 10.174 1.00 21.45 C
ANISOU 449 CG LEU A 82 2083 3044 3024 -127 1244 -146 C
ATOM 450 CD1 LEU A 82 37.144 50.140 10.777 1.00 19.33 C
ANISOU 450 CD1 LEU A 82 1733 2800 2810 -149 1237 -198 C
ATOM 451 CD2 LEU A 82 35.515 51.926 10.130 1.00 19.28 C
ANISOU 451 CD2 LEU A 82 1842 2703 2782 -196 1292 -76 C
ATOM 452 N ASP A 83 35.525 46.832 10.568 1.00 23.12 N
ANISOU 452 N ASP A 83 2295 3328 3161 53 1114 -296 N
ATOM 453 CA ASP A 83 34.802 46.012 11.533 1.00 17.77 C
ANISOU 453 CA ASP A 83 1673 2588 2490 94 1065 -340 C
ATOM 454 C ASP A 83 34.977 46.624 12.915 1.00 22.70 C
ANISOU 454 C ASP A 83 2311 3128 3187 57 1069 -363 C
ATOM 455 O ASP A 83 36.090 46.655 13.452 1.00 25.25 O
ANISOU 455 O ASP A 83 2575 3457 3561 39 1072 -401 O
ATOM 456 CB ASP A 83 35.297 44.569 11.507 1.00 23.58 C
ANISOU 456 CB ASP A 83 2389 3363 3207 154 1025 -396 C
ATOM 457 CG ASP A 83 34.379 43.624 12.262 1.00 33.37 C
ANISOU 457 CG ASP A 83 3700 4543 4435 193 977 -431 C
ATOM 458 OD1 ASP A 83 33.622 44.087 13.139 1.00 28.18 O
ANISOU 458 OD1 ASP A 83 3096 3811 3799 171 974 -425 O
ATOM 459 OD2 ASP A 83 34.411 42.412 11.974 1.00 37.60 O
ANISOU 459 OD2 ASP A 83 4241 5103 4940 245 946 -462 O
ATOM 460 N LEU A 84 33.875 47.096 13.491 1.00 17.39 N
ANISOU 460 N LEU A 84 1709 2380 2520 49 1070 -346 N
ATOM 461 CA LEU A 84 33.866 47.669 14.830 1.00 16.22 C
ANISOU 461 CA LEU A 84 1588 2144 2431 21 1079 -370 C
ATOM 462 C LEU A 84 32.950 46.882 15.759 1.00 21.16 C
ANISOU 462 C LEU A 84 2290 2713 3038 58 1039 -406 C
ATOM 463 O LEU A 84 32.364 47.439 16.688 1.00 16.79 O
ANISOU 463 O LEU A 84 1791 2082 2505 43 1048 -409 O
ATOM 464 CB LEU A 84 33.451 49.137 14.782 1.00 20.40 C
ANISOU 464 CB LEU A 84 2140 2625 2989 -30 1126 -315 C
ATOM 465 CG LEU A 84 34.342 50.027 13.916 1.00 23.25 C
ANISOU 465 CG LEU A 84 2438 3029 3367 -84 1167 -267 C
ATOM 466 CD1 LEU A 84 33.601 51.282 13.472 1.00 22.96 C
ANISOU 466 CD1 LEU A 84 2447 2948 3329 -115 1199 -194 C
ATOM 467 CD2 LEU A 84 35.619 50.388 14.662 1.00 27.78 C
ANISOU 467 CD2 LEU A 84 2967 3589 3998 -131 1139 -291 C
ATOM 468 N SER A 85 32.816 45.581 15.503 1.00 27.08 N
ANISOU 468 N SER A 85 3047 3498 3744 106 997 -431 N
ATOM 469 CA SER A 85 31.953 44.735 16.313 1.00 23.02 C
ANISOU 469 CA SER A 85 2605 2933 3207 132 960 -458 C
ATOM 470 C SER A 85 32.424 44.735 17.761 1.00 23.45 C
ANISOU 470 C SER A 85 2690 2919 3301 125 955 -510 C
ATOM 471 O SER A 85 33.626 44.740 18.038 1.00 16.63 O
ANISOU 471 O SER A 85 1781 2069 2469 121 932 -537 O
ATOM 472 CB SER A 85 31.948 43.308 15.765 1.00 18.48 C
ANISOU 472 CB SER A 85 2027 2405 2589 179 920 -481 C
ATOM 473 OG SER A 85 31.588 43.286 14.392 1.00 26.38 O
ANISOU 473 OG SER A 85 3000 3472 3549 190 925 -442 O
ATOM 474 N ARG A 86 31.461 44.753 18.682 1.00 18.54 N
ANISOU 474 N ARG A 86 2150 2228 2666 119 948 -513 N
ATOM 475 CA ARG A 86 31.725 44.655 20.118 1.00 19.10 C
ANISOU 475 CA ARG A 86 2284 2229 2745 113 910 -548 C
ATOM 476 C ARG A 86 32.758 45.679 20.577 1.00 19.70 C
ANISOU 476 C ARG A 86 2333 2289 2863 77 885 -543 C
ATOM 477 O ARG A 86 33.753 45.346 21.224 1.00 22.69 O
ANISOU 477 O ARG A 86 2706 2661 3256 83 827 -576 O
ATOM 478 CB ARG A 86 32.177 43.243 20.490 1.00 20.92 C
ANISOU 478 CB ARG A 86 2536 2460 2953 153 857 -593 C
ATOM 479 CG ARG A 86 31.738 42.804 21.868 1.00 18.76 C
ANISOU 479 CG ARG A 86 2369 2108 2651 151 821 -615 C
ATOM 480 CD ARG A 86 30.282 42.406 21.834 1.00 29.90 C
ANISOU 480 CD ARG A 86 3835 3500 4024 148 857 -600 C
ATOM 481 NE ARG A 86 29.516 42.923 22.957 1.00 23.83 N
ANISOU 481 NE ARG A 86 3149 2668 3239 117 866 -593 N
ATOM 482 CZ ARG A 86 28.203 42.767 23.089 1.00 30.16 C
ANISOU 482 CZ ARG A 86 3986 3464 4011 99 875 -562 C
ATOM 483 NH1 ARG A 86 27.510 42.109 22.168 1.00 25.35 N
ANISOU 483 NH1 ARG A 86 3344 2901 3388 108 873 -540 N
ATOM 484 NH2 ARG A 86 27.579 43.266 24.144 1.00 22.10 N
ANISOU 484 NH2 ARG A 86 3031 2393 2975 72 886 -559 N
ATOM 485 N CYS A 87 32.521 46.941 20.234 1.00 25.46 N
ANISOU 485 N CYS A 87 3046 3011 3617 40 925 -502 N
ATOM 486 CA CYS A 87 33.444 48.004 20.601 1.00 24.88 C
ANISOU 486 CA CYS A 87 2947 2916 3589 -5 905 -495 C
ATOM 487 C CYS A 87 32.874 48.943 21.653 1.00 23.27 C
ANISOU 487 C CYS A 87 2823 2625 3393 -33 899 -492 C
ATOM 488 O CYS A 87 33.454 50.007 21.896 1.00 21.92 O
ANISOU 488 O CYS A 87 2641 2426 3263 -76 888 -481 O
ATOM 489 CB CYS A 87 33.874 48.788 19.361 1.00 44.11 C
ANISOU 489 CB CYS A 87 5301 5406 6053 -35 951 -449 C
ATOM 490 SG CYS A 87 35.076 47.899 18.347 1.00 47.64 S
ANISOU 490 SG CYS A 87 5638 5961 6503 -14 952 -468 S
ATOM 491 N GLU A 88 31.765 48.567 22.296 1.00 20.16 N
ANISOU 491 N GLU A 88 2510 2188 2961 -11 907 -505 N
ATOM 492 CA GLU A 88 31.153 49.338 23.378 1.00 23.86 C
ANISOU 492 CA GLU A 88 3061 2578 3428 -30 907 -514 C
ATOM 493 C GLU A 88 30.806 50.761 22.952 1.00 22.09 C
ANISOU 493 C GLU A 88 2826 2326 3240 -57 944 -475 C
ATOM 494 O GLU A 88 30.703 51.659 23.792 1.00 20.09 O
ANISOU 494 O GLU A 88 2626 2005 3002 -80 933 -486 O
ATOM 495 CB GLU A 88 32.060 49.350 24.618 1.00 31.15 C
ANISOU 495 CB GLU A 88 4025 3457 4353 -45 838 -554 C
ATOM 496 CG GLU A 88 32.240 47.975 25.253 1.00 35.62 C
ANISOU 496 CG GLU A 88 4633 4028 4874 -13 792 -591 C
ATOM 497 CD GLU A 88 33.502 47.869 26.090 1.00 45.73 C
ANISOU 497 CD GLU A 88 5918 5291 6165 -19 707 -626 C
ATOM 498 OE1 GLU A 88 34.365 47.026 25.766 1.00 51.63 O
ANISOU 498 OE1 GLU A 88 6612 6085 6920 6 666 -642 O
ATOM 499 OE2 GLU A 88 33.634 48.627 27.073 1.00 49.02 O
ANISOU 499 OE2 GLU A 88 6391 5649 6584 -46 678 -643 O
ATOM 500 N ILE A 89 30.621 50.981 21.652 1.00 24.71 N
ANISOU 500 N ILE A 89 3098 2708 3584 -54 985 -431 N
ATOM 501 CA ILE A 89 30.387 52.325 21.138 1.00 15.77 C
ANISOU 501 CA ILE A 89 1958 1546 2486 -79 1014 -386 C
ATOM 502 C ILE A 89 28.996 52.784 21.555 1.00 19.67 C
ANISOU 502 C ILE A 89 2518 1986 2972 -56 1041 -388 C
ATOM 503 O ILE A 89 27.995 52.110 21.282 1.00 19.76 O
ANISOU 503 O ILE A 89 2532 2023 2951 -19 1068 -393 O
ATOM 504 CB ILE A 89 30.550 52.364 19.613 1.00 16.89 C
ANISOU 504 CB ILE A 89 2029 1759 2630 -80 1048 -335 C
ATOM 505 CG1 ILE A 89 31.949 51.890 19.210 1.00 17.16 C
ANISOU 505 CG1 ILE A 89 1988 1857 2675 -101 1030 -341 C
ATOM 506 CG2 ILE A 89 30.285 53.768 19.083 1.00 21.11 C
ANISOU 506 CG2 ILE A 89 2572 2254 3196 -106 1073 -280 C
ATOM 507 CD1 ILE A 89 32.114 51.663 17.728 1.00 16.21 C
ANISOU 507 CD1 ILE A 89 1799 1820 2538 -95 1071 -301 C
ATOM 508 N GLU A 90 28.930 53.932 22.228 1.00 17.63 N
ANISOU 508 N GLU A 90 2306 1650 2743 -79 1033 -391 N
ATOM 509 CA GLU A 90 27.663 54.576 22.533 1.00 22.05 C
ANISOU 509 CA GLU A 90 2917 2156 3304 -53 1062 -394 C
ATOM 510 C GLU A 90 27.412 55.814 21.686 1.00 25.32 C
ANISOU 510 C GLU A 90 3321 2542 3759 -58 1080 -340 C
ATOM 511 O GLU A 90 26.253 56.206 21.516 1.00 19.23 O
ANISOU 511 O GLU A 90 2569 1748 2990 -20 1107 -334 O
ATOM 512 CB GLU A 90 27.602 54.970 24.013 1.00 27.67 C
ANISOU 512 CB GLU A 90 3707 2792 4014 -63 1042 -446 C
ATOM 513 CG GLU A 90 27.299 53.823 24.961 1.00 33.44 C
ANISOU 513 CG GLU A 90 4480 3535 4692 -45 1038 -497 C
ATOM 514 CD GLU A 90 26.703 54.298 26.276 1.00 42.90 C
ANISOU 514 CD GLU A 90 5765 4661 5873 -42 1043 -544 C
ATOM 515 OE1 GLU A 90 27.345 55.125 26.959 1.00 51.58 O
ANISOU 515 OE1 GLU A 90 6903 5702 6992 -69 1008 -561 O
ATOM 516 OE2 GLU A 90 25.590 53.849 26.624 1.00 51.06 O
ANISOU 516 OE2 GLU A 90 6821 5710 6868 -17 1072 -557 O
ATOM 517 N THR A 91 28.457 56.423 21.137 1.00 23.55 N
ANISOU 517 N THR A 91 3064 2318 3565 -104 1066 -301 N
ATOM 518 CA THR A 91 28.333 57.720 20.490 1.00 21.94 C
ANISOU 518 CA THR A 91 2871 2066 3400 -121 1077 -246 C
ATOM 519 C THR A 91 29.100 57.700 19.182 1.00 18.78 C
ANISOU 519 C THR A 91 2405 1729 3000 -152 1090 -184 C
ATOM 520 O THR A 91 30.278 57.333 19.159 1.00 21.38 O
ANISOU 520 O THR A 91 2688 2100 3335 -195 1078 -190 O
ATOM 521 CB THR A 91 28.858 58.832 21.402 1.00 18.00 C
ANISOU 521 CB THR A 91 2424 1470 2946 -165 1046 -263 C
ATOM 522 OG1 THR A 91 28.156 58.791 22.653 1.00 25.22 O
ANISOU 522 OG1 THR A 91 3403 2332 3848 -133 1038 -327 O
ATOM 523 CG2 THR A 91 28.655 60.192 20.756 1.00 18.67 C
ANISOU 523 CG2 THR A 91 2533 1489 3072 -181 1054 -205 C
ATOM 524 N ILE A 92 28.425 58.074 18.103 1.00 20.99 N
ANISOU 524 N ILE A 92 2682 2022 3272 -129 1116 -128 N
ATOM 525 CA ILE A 92 29.057 58.340 16.817 1.00 18.15 C
ANISOU 525 CA ILE A 92 2279 1708 2907 -163 1136 -58 C
ATOM 526 C ILE A 92 29.075 59.854 16.655 1.00 19.73 C
ANISOU 526 C ILE A 92 2530 1816 3151 -199 1132 -4 C
ATOM 527 O ILE A 92 28.022 60.482 16.503 1.00 20.28 O
ANISOU 527 O ILE A 92 2649 1830 3227 -154 1131 16 O
ATOM 528 CB ILE A 92 28.311 57.658 15.662 1.00 19.66 C
ANISOU 528 CB ILE A 92 2443 1979 3049 -112 1161 -30 C
ATOM 529 CG1 ILE A 92 28.182 56.155 15.920 1.00 25.05 C
ANISOU 529 CG1 ILE A 92 3087 2737 3692 -75 1161 -90 C
ATOM 530 CG2 ILE A 92 29.023 57.909 14.346 1.00 18.36 C
ANISOU 530 CG2 ILE A 92 2242 1869 2866 -151 1187 42 C
ATOM 531 CD1 ILE A 92 27.287 55.442 14.939 1.00 22.82 C
ANISOU 531 CD1 ILE A 92 2784 2523 3363 -21 1177 -77 C
ATOM 532 N GLU A 93 30.263 60.450 16.720 1.00 22.28 N
ANISOU 532 N GLU A 93 2841 2115 3509 -278 1127 16 N
ATOM 533 CA GLU A 93 30.358 61.896 16.605 1.00 21.55 C
ANISOU 533 CA GLU A 93 2804 1923 3462 -323 1120 67 C
ATOM 534 C GLU A 93 29.991 62.336 15.191 1.00 22.56 C
ANISOU 534 C GLU A 93 2940 2067 3564 -317 1149 158 C
ATOM 535 O GLU A 93 30.013 61.550 14.239 1.00 26.33 O
ANISOU 535 O GLU A 93 3367 2647 3990 -300 1177 183 O
ATOM 536 CB GLU A 93 31.756 62.378 16.990 1.00 21.11 C
ANISOU 536 CB GLU A 93 2725 1843 3453 -421 1108 65 C
ATOM 537 CG GLU A 93 31.990 62.357 18.497 1.00 20.95 C
ANISOU 537 CG GLU A 93 2729 1767 3465 -426 1062 -19 C
ATOM 538 CD GLU A 93 33.200 63.162 18.917 1.00 23.91 C
ANISOU 538 CD GLU A 93 3098 2089 3900 -524 1037 -20 C
ATOM 539 OE1 GLU A 93 34.096 63.367 18.078 1.00 26.11 O
ANISOU 539 OE1 GLU A 93 3321 2408 4192 -595 1063 33 O
ATOM 540 OE2 GLU A 93 33.248 63.601 20.090 1.00 32.04 O
ANISOU 540 OE2 GLU A 93 4177 3035 4961 -533 994 -76 O
ATOM 541 N ASP A 94 29.657 63.623 15.064 1.00 26.67 N
ANISOU 541 N ASP A 94 3533 2481 4118 -330 1137 208 N
ATOM 542 CA ASP A 94 28.964 64.104 13.873 1.00 23.90 C
ANISOU 542 CA ASP A 94 3218 2123 3739 -299 1149 290 C
ATOM 543 C ASP A 94 29.814 64.033 12.610 1.00 29.55 C
ANISOU 543 C ASP A 94 3896 2916 4417 -362 1189 369 C
ATOM 544 O ASP A 94 29.267 64.165 11.509 1.00 32.19 O
ANISOU 544 O ASP A 94 4253 3272 4705 -331 1201 436 O
ATOM 545 CB ASP A 94 28.467 65.537 14.090 1.00 24.24 C
ANISOU 545 CB ASP A 94 3357 2021 3832 -295 1119 325 C
ATOM 546 CG ASP A 94 29.594 66.531 14.304 1.00 36.64 C
ANISOU 546 CG ASP A 94 4956 3512 5455 -405 1116 357 C
ATOM 547 OD1 ASP A 94 30.692 66.121 14.734 1.00 43.46 O
ANISOU 547 OD1 ASP A 94 5759 4421 6333 -475 1126 323 O
ATOM 548 OD2 ASP A 94 29.365 67.735 14.046 1.00 50.15 O
ANISOU 548 OD2 ASP A 94 6748 5111 7197 -419 1099 416 O
ATOM 549 N LYS A 95 31.124 63.836 12.734 1.00 22.86 N
ANISOU 549 N LYS A 95 2990 2112 3585 -449 1210 360 N
ATOM 550 CA LYS A 95 32.007 63.628 11.592 1.00 26.44 C
ANISOU 550 CA LYS A 95 3390 2657 3999 -512 1261 421 C
ATOM 551 C LYS A 95 32.915 62.434 11.840 1.00 31.30 C
ANISOU 551 C LYS A 95 3900 3387 4604 -528 1279 355 C
ATOM 552 O LYS A 95 34.104 62.447 11.504 1.00 29.52 O
ANISOU 552 O LYS A 95 3613 3214 4388 -611 1313 371 O
ATOM 553 CB LYS A 95 32.826 64.880 11.292 1.00 27.51 C
ANISOU 553 CB LYS A 95 3560 2718 4173 -621 1277 496 C
ATOM 554 CG LYS A 95 32.000 66.042 10.770 1.00 33.46 C
ANISOU 554 CG LYS A 95 4425 3362 4925 -605 1261 580 C
ATOM 555 CD LYS A 95 32.900 67.205 10.422 1.00 48.86 C
ANISOU 555 CD LYS A 95 6412 5240 6911 -727 1282 659 C
ATOM 556 CE LYS A 95 32.119 68.409 9.935 1.00 57.94 C
ANISOU 556 CE LYS A 95 7687 6264 8063 -711 1258 746 C
ATOM 557 NZ LYS A 95 33.018 69.535 9.557 1.00 65.70 N
ANISOU 557 NZ LYS A 95 8714 7170 9077 -841 1282 832 N
ATOM 558 N ALA A 96 32.359 61.374 12.431 1.00 27.60 N
ANISOU 558 N ALA A 96 3409 2960 4119 -448 1256 277 N
ATOM 559 CA ALA A 96 33.177 60.224 12.800 1.00 21.28 C
ANISOU 559 CA ALA A 96 2520 2253 3314 -453 1259 208 C
ATOM 560 C ALA A 96 33.750 59.524 11.577 1.00 21.49 C
ANISOU 560 C ALA A 96 2474 2406 3284 -464 1312 236 C
ATOM 561 O ALA A 96 34.844 58.952 11.646 1.00 26.84 O
ANISOU 561 O ALA A 96 3068 3157 3973 -501 1326 200 O
ATOM 562 CB ALA A 96 32.359 59.245 13.641 1.00 20.20 C
ANISOU 562 CB ALA A 96 2391 2123 3163 -366 1225 128 C
ATOM 563 N TRP A 97 33.036 59.568 10.451 1.00 21.61 N
ANISOU 563 N TRP A 97 2520 2452 3239 -430 1338 296 N
ATOM 564 CA TRP A 97 33.427 58.863 9.238 1.00 26.78 C
ANISOU 564 CA TRP A 97 3118 3230 3825 -429 1389 319 C
ATOM 565 C TRP A 97 33.876 59.808 8.128 1.00 28.73 C
ANISOU 565 C TRP A 97 3387 3482 4047 -503 1440 421 C
ATOM 566 O TRP A 97 33.812 59.451 6.947 1.00 26.50 O
ANISOU 566 O TRP A 97 3094 3285 3687 -489 1481 460 O
ATOM 567 CB TRP A 97 32.285 57.957 8.773 1.00 31.76 C
ANISOU 567 CB TRP A 97 3764 3911 4391 -329 1377 300 C
ATOM 568 CG TRP A 97 32.139 56.777 9.680 1.00 33.53 C
ANISOU 568 CG TRP A 97 3951 4161 4629 -274 1344 202 C
ATOM 569 CD1 TRP A 97 33.113 55.888 10.010 1.00 38.32 C
ANISOU 569 CD1 TRP A 97 4480 4835 5245 -286 1349 140 C
ATOM 570 CD2 TRP A 97 30.969 56.375 10.395 1.00 26.85 C
ANISOU 570 CD2 TRP A 97 3144 3270 3787 -201 1302 155 C
ATOM 571 NE1 TRP A 97 32.623 54.947 10.880 1.00 33.91 N
ANISOU 571 NE1 TRP A 97 3923 4269 4692 -225 1309 64 N
ATOM 572 CE2 TRP A 97 31.306 55.225 11.132 1.00 34.26 C
ANISOU 572 CE2 TRP A 97 4037 4247 4733 -177 1284 72 C
ATOM 573 CE3 TRP A 97 29.671 56.872 10.479 1.00 27.48 C
ANISOU 573 CE3 TRP A 97 3291 3282 3867 -153 1277 174 C
ATOM 574 CZ2 TRP A 97 30.392 54.568 11.939 1.00 30.17 C
ANISOU 574 CZ2 TRP A 97 3545 3701 4216 -118 1250 14 C
ATOM 575 CZ3 TRP A 97 28.768 56.218 11.277 1.00 42.16 C
ANISOU 575 CZ3 TRP A 97 5163 5122 5734 -92 1247 109 C
ATOM 576 CH2 TRP A 97 29.129 55.080 11.996 1.00 42.76 C
ANISOU 576 CH2 TRP A 97 5200 5237 5812 -80 1237 33 C
ATOM 577 N HIS A 98 34.354 60.995 8.490 1.00 27.71 N
ANISOU 577 N HIS A 98 3290 3260 3977 -585 1438 462 N
ATOM 578 CA HIS A 98 34.939 61.902 7.512 1.00 29.66 C
ANISOU 578 CA HIS A 98 3558 3506 4205 -675 1492 561 C
ATOM 579 C HIS A 98 36.131 61.247 6.829 1.00 34.02 C
ANISOU 579 C HIS A 98 4004 4195 4726 -730 1562 553 C
ATOM 580 O HIS A 98 37.006 60.684 7.491 1.00 34.38 O
ANISOU 580 O HIS A 98 3957 4286 4818 -751 1559 477 O
ATOM 581 CB HIS A 98 35.367 63.197 8.205 1.00 28.39 C
ANISOU 581 CB HIS A 98 3443 3216 4130 -763 1472 590 C
ATOM 582 CG HIS A 98 36.147 64.131 7.331 1.00 32.41 C
ANISOU 582 CG HIS A 98 3966 3717 4630 -879 1532 689 C
ATOM 583 ND1 HIS A 98 37.520 64.074 7.216 1.00 33.14 N
ANISOU 583 ND1 HIS A 98 3963 3882 4746 -979 1578 680 N
ATOM 584 CD2 HIS A 98 35.749 65.164 6.552 1.00 34.22 C
ANISOU 584 CD2 HIS A 98 4298 3874 4831 -910 1545 797 C
ATOM 585 CE1 HIS A 98 37.932 65.023 6.395 1.00 35.23 C
ANISOU 585 CE1 HIS A 98 4269 4131 4984 -1065 1602 772 C
ATOM 586 NE2 HIS A 98 36.877 65.699 5.978 1.00 37.68 N
ANISOU 586 NE2 HIS A 98 4705 4344 5267 -1033 1597 853 N
ATOM 587 N GLY A 99 36.159 61.308 5.498 1.00 35.27 N
ANISOU 587 N GLY A 99 4177 4425 4798 -743 1610 623 N
ATOM 588 CA GLY A 99 37.268 60.780 4.731 1.00 30.40 C
ANISOU 588 CA GLY A 99 3470 3952 4129 -780 1637 608 C
ATOM 589 C GLY A 99 37.098 59.366 4.217 1.00 32.40 C
ANISOU 589 C GLY A 99 3667 4337 4305 -688 1631 544 C
ATOM 590 O GLY A 99 37.967 58.889 3.476 1.00 41.72 O
ANISOU 590 O GLY A 99 4775 5641 5434 -708 1656 532 O
ATOM 591 N LEU A 100 36.014 58.684 4.577 1.00 35.49 N
ANISOU 591 N LEU A 100 4089 4705 4690 -588 1598 501 N
ATOM 592 CA LEU A 100 35.794 57.300 4.159 1.00 34.18 C
ANISOU 592 CA LEU A 100 3878 4651 4457 -500 1579 432 C
ATOM 593 C LEU A 100 34.969 57.217 2.879 1.00 35.96 C
ANISOU 593 C LEU A 100 4164 4921 4578 -458 1600 488 C
ATOM 594 O LEU A 100 33.940 56.544 2.830 1.00 33.38 O
ANISOU 594 O LEU A 100 3865 4597 4220 -371 1572 458 O
ATOM 595 CB LEU A 100 35.128 56.521 5.285 1.00 23.09 C
ANISOU 595 CB LEU A 100 2469 3203 3101 -421 1526 347 C
ATOM 596 CG LEU A 100 35.936 56.400 6.575 1.00 30.13 C
ANISOU 596 CG LEU A 100 3302 4061 4085 -450 1500 280 C
ATOM 597 CD1 LEU A 100 35.250 55.459 7.544 1.00 22.08 C
ANISOU 597 CD1 LEU A 100 2286 3015 3089 -367 1448 197 C
ATOM 598 CD2 LEU A 100 37.341 55.923 6.255 1.00 32.64 C
ANISOU 598 CD2 LEU A 100 3518 4489 4393 -486 1510 247 C
ATOM 599 N HIS A 101 35.424 57.890 1.817 1.00 37.78 N
ANISOU 599 N HIS A 101 4417 5188 4748 -524 1648 569 N
ATOM 600 CA HIS A 101 34.621 57.937 0.598 1.00 39.20 C
ANISOU 600 CA HIS A 101 4671 5399 4823 -489 1668 633 C
ATOM 601 C HIS A 101 34.510 56.570 -0.067 1.00 37.14 C
ANISOU 601 C HIS A 101 4363 5268 4481 -415 1654 559 C
ATOM 602 O HIS A 101 33.564 56.331 -0.824 1.00 41.32 O
ANISOU 602 O HIS A 101 4951 5814 4934 -355 1652 583 O
ATOM 603 CB HIS A 101 35.187 58.955 -0.399 1.00 48.40 C
ANISOU 603 CB HIS A 101 5880 6576 5933 -583 1721 740 C
ATOM 604 CG HIS A 101 36.440 59.635 0.054 1.00 63.29 C
ANISOU 604 CG HIS A 101 7711 8448 7887 -692 1742 750 C
ATOM 605 ND1 HIS A 101 37.697 59.153 -0.243 1.00 66.72 N
ANISOU 605 ND1 HIS A 101 8038 9006 8306 -736 1768 709 N
ATOM 606 CD2 HIS A 101 36.631 60.774 0.761 1.00 65.98 C
ANISOU 606 CD2 HIS A 101 8089 8665 8314 -765 1739 799 C
ATOM 607 CE1 HIS A 101 38.607 59.960 0.270 1.00 67.49 C
ANISOU 607 CE1 HIS A 101 8102 9061 8479 -832 1782 733 C
ATOM 608 NE2 HIS A 101 37.987 60.951 0.886 1.00 67.64 N
ANISOU 608 NE2 HIS A 101 8211 8929 8560 -856 1762 785 N
ATOM 609 N HIS A 102 35.442 55.659 0.209 1.00 39.92 N
ANISOU 609 N HIS A 102 4611 5708 4849 -413 1642 470 N
ATOM 610 CA HIS A 102 35.483 54.362 -0.455 1.00 39.32 C
ANISOU 610 CA HIS A 102 4489 5753 4698 -349 1628 396 C
ATOM 611 C HIS A 102 35.021 53.208 0.426 1.00 35.42 C
ANISOU 611 C HIS A 102 3964 5248 4248 -263 1559 295 C
ATOM 612 O HIS A 102 35.084 52.053 -0.011 1.00 36.99 O
ANISOU 612 O HIS A 102 4123 5537 4394 -208 1538 226 O
ATOM 613 CB HIS A 102 36.896 54.074 -0.957 1.00 47.17 C
ANISOU 613 CB HIS A 102 5388 6869 5665 -394 1664 378 C
ATOM 614 CG HIS A 102 37.306 54.925 -2.115 1.00 58.47 C
ANISOU 614 CG HIS A 102 6849 8347 7019 -473 1733 469 C
ATOM 615 ND1 HIS A 102 38.544 55.523 -2.196 1.00 62.11 N
ANISOU 615 ND1 HIS A 102 7248 8847 7505 -556 1779 512 N
ATOM 616 CD2 HIS A 102 36.646 55.270 -3.245 1.00 60.67 C
ANISOU 616 CD2 HIS A 102 7219 8638 7196 -481 1764 531 C
ATOM 617 CE1 HIS A 102 38.628 56.204 -3.325 1.00 64.41 C
ANISOU 617 CE1 HIS A 102 7589 9175 7708 -617 1836 598 C
ATOM 618 NE2 HIS A 102 37.490 56.067 -3.980 1.00 63.53 N
ANISOU 618 NE2 HIS A 102 7577 9047 7515 -574 1827 610 N
ATOM 619 N LEU A 103 34.561 53.478 1.644 1.00 30.28 N
ANISOU 619 N LEU A 103 3333 4487 3686 -251 1525 284 N
ATOM 620 CA LEU A 103 34.141 52.397 2.527 1.00 33.46 C
ANISOU 620 CA LEU A 103 3714 4875 4126 -177 1459 193 C
ATOM 621 C LEU A 103 32.866 51.758 1.993 1.00 33.07 C
ANISOU 621 C LEU A 103 3713 4835 4016 -103 1432 176 C
ATOM 622 O LEU A 103 31.846 52.434 1.824 1.00 29.63 O
ANISOU 622 O LEU A 103 3348 4336 3575 -91 1444 234 O
ATOM 623 CB LEU A 103 33.925 52.911 3.946 1.00 25.42 C
ANISOU 623 CB LEU A 103 2713 3736 3209 -189 1437 185 C
ATOM 624 CG LEU A 103 33.746 51.764 4.944 1.00 26.05 C
ANISOU 624 CG LEU A 103 2768 3805 3324 -127 1371 92 C
ATOM 625 CD1 LEU A 103 35.089 51.108 5.239 1.00 20.76 C
ANISOU 625 CD1 LEU A 103 2015 3200 2675 -136 1361 39 C
ATOM 626 CD2 LEU A 103 33.053 52.220 6.220 1.00 19.82 C
ANISOU 626 CD2 LEU A 103 2023 2894 2612 -124 1350 85 C
ATOM 627 N SER A 104 32.927 50.454 1.729 1.00 32.63 N
ANISOU 627 N SER A 104 3619 4858 3921 -50 1395 98 N
ATOM 628 CA SER A 104 31.777 49.708 1.238 1.00 28.63 C
ANISOU 628 CA SER A 104 3149 4364 3364 13 1364 65 C
ATOM 629 C SER A 104 31.134 48.823 2.295 1.00 24.74 C
ANISOU 629 C SER A 104 2656 3823 2923 68 1292 -5 C
ATOM 630 O SER A 104 29.945 48.509 2.172 1.00 22.03 O
ANISOU 630 O SER A 104 2351 3455 2564 111 1267 -18 O
ATOM 631 CB SER A 104 32.181 48.834 0.046 1.00 33.81 C
ANISOU 631 CB SER A 104 3777 5136 3932 25 1376 20 C
ATOM 632 OG SER A 104 32.959 47.726 0.469 1.00 34.25 O
ANISOU 632 OG SER A 104 3766 5244 4005 57 1333 -57 O
ATOM 633 N ASN A 105 31.884 48.406 3.312 1.00 23.07 N
ANISOU 633 N ASN A 105 2402 3595 2767 68 1262 -46 N
ATOM 634 CA ASN A 105 31.377 47.530 4.360 1.00 19.76 C
ANISOU 634 CA ASN A 105 1992 3125 2388 114 1197 -105 C
ATOM 635 C ASN A 105 31.648 48.154 5.720 1.00 26.61 C
ANISOU 635 C ASN A 105 2867 3900 3342 82 1194 -99 C
ATOM 636 O ASN A 105 32.793 48.494 6.033 1.00 36.67 O
ANISOU 636 O ASN A 105 4101 5181 4649 44 1216 -94 O
ATOM 637 CB ASN A 105 32.019 46.138 4.272 1.00 22.96 C
ANISOU 637 CB ASN A 105 2358 3597 2769 167 1161 -163 C
ATOM 638 CG ASN A 105 31.457 45.305 3.134 1.00 30.47 C
ANISOU 638 CG ASN A 105 3316 4618 3641 215 1149 -184 C
ATOM 639 OD1 ASN A 105 30.506 44.547 3.319 1.00 33.74 O
ANISOU 639 OD1 ASN A 105 3764 5002 4053 255 1102 -217 O
ATOM 640 ND2 ASN A 105 32.042 45.444 1.950 1.00 32.08 N
ANISOU 640 ND2 ASN A 105 3502 4898 3790 201 1185 -166 N
ATOM 641 N LEU A 106 30.593 48.308 6.520 1.00 19.98 N
ANISOU 641 N LEU A 106 2076 2976 2539 96 1168 -105 N
ATOM 642 CA LEU A 106 30.682 48.840 7.877 1.00 19.18 C
ANISOU 642 CA LEU A 106 1991 2781 2514 70 1164 -111 C
ATOM 643 C LEU A 106 29.908 47.922 8.811 1.00 23.01 C
ANISOU 643 C LEU A 106 2507 3224 3013 110 1106 -165 C
ATOM 644 O LEU A 106 28.714 47.683 8.598 1.00 21.61 O
ANISOU 644 O LEU A 106 2360 3037 2815 140 1086 -168 O
ATOM 645 CB LEU A 106 30.134 50.269 7.956 1.00 17.41 C
ANISOU 645 CB LEU A 106 1807 2485 2324 38 1210 -48 C
ATOM 646 CG LEU A 106 30.108 50.874 9.360 1.00 17.10 C
ANISOU 646 CG LEU A 106 1791 2345 2363 15 1212 -59 C
ATOM 647 CD1 LEU A 106 31.514 50.954 9.930 1.00 17.39 C
ANISOU 647 CD1 LEU A 106 1782 2385 2439 -31 1221 -78 C
ATOM 648 CD2 LEU A 106 29.453 52.247 9.359 1.00 17.39 C
ANISOU 648 CD2 LEU A 106 1872 2305 2432 -5 1260 4 C
ATOM 649 N ILE A 107 30.582 47.415 9.841 1.00 17.12 N
ANISOU 649 N ILE A 107 1750 2451 2302 108 1082 -208 N
ATOM 650 CA ILE A 107 30.015 46.425 10.750 1.00 20.48 C
ANISOU 650 CA ILE A 107 2210 2839 2734 138 1032 -257 C
ATOM 651 C ILE A 107 30.031 47.012 12.155 1.00 22.17 C
ANISOU 651 C ILE A 107 2453 2961 3008 110 1038 -268 C
ATOM 652 O ILE A 107 31.105 47.251 12.724 1.00 18.65 O
ANISOU 652 O ILE A 107 1981 2504 2602 85 1053 -284 O
ATOM 653 CB ILE A 107 30.782 45.093 10.688 1.00 26.38 C
ANISOU 653 CB ILE A 107 2930 3634 3460 172 1000 -303 C
ATOM 654 CG1 ILE A 107 30.853 44.595 9.240 1.00 26.91 C
ANISOU 654 CG1 ILE A 107 2967 3793 3464 202 1003 -293 C
ATOM 655 CG2 ILE A 107 30.130 44.049 11.586 1.00 23.69 C
ANISOU 655 CG2 ILE A 107 2635 3244 3121 198 953 -346 C
ATOM 656 CD1 ILE A 107 31.501 43.233 9.069 1.00 33.25 C
ANISOU 656 CD1 ILE A 107 3752 4636 4244 249 976 -337 C
ATOM 657 N LEU A 108 28.838 47.253 12.707 1.00 19.69 N
ANISOU 657 N LEU A 108 2189 2588 2704 115 1029 -266 N
ATOM 658 CA LEU A 108 28.683 47.842 14.032 1.00 14.77 C
ANISOU 658 CA LEU A 108 1604 1878 2129 93 1039 -279 C
ATOM 659 C LEU A 108 28.050 46.884 15.033 1.00 17.14 C
ANISOU 659 C LEU A 108 1949 2144 2421 110 998 -322 C
ATOM 660 O LEU A 108 27.494 47.341 16.039 1.00 20.70 O
ANISOU 660 O LEU A 108 2443 2527 2896 98 1006 -331 O
ATOM 661 CB LEU A 108 27.841 49.119 13.947 1.00 15.23 C
ANISOU 661 CB LEU A 108 1687 1889 2212 83 1076 -239 C
ATOM 662 CG LEU A 108 28.354 50.211 13.006 1.00 17.08 C
ANISOU 662 CG LEU A 108 1893 2141 2457 58 1128 -184 C
ATOM 663 CD1 LEU A 108 27.369 51.364 12.916 1.00 17.35 C
ANISOU 663 CD1 LEU A 108 1961 2118 2515 62 1166 -144 C
ATOM 664 CD2 LEU A 108 29.713 50.705 13.469 1.00 18.10 C
ANISOU 664 CD2 LEU A 108 1992 2254 2629 11 1159 -186 C
ATOM 665 N THR A 109 28.134 45.574 14.798 1.00 20.88 N
ANISOU 665 N THR A 109 2415 2658 2859 136 961 -348 N
ATOM 666 CA THR A 109 27.426 44.596 15.619 1.00 18.74 C
ANISOU 666 CA THR A 109 2191 2354 2575 146 928 -380 C
ATOM 667 C THR A 109 27.770 44.738 17.098 1.00 13.75 C
ANISOU 667 C THR A 109 1602 1651 1972 127 934 -408 C
ATOM 668 O THR A 109 28.936 44.903 17.468 1.00 20.75 O
ANISOU 668 O THR A 109 2470 2530 2882 121 944 -429 O
ATOM 669 CB THR A 109 27.766 43.184 15.137 1.00 19.70 C
ANISOU 669 CB THR A 109 2299 2522 2664 177 896 -407 C
ATOM 670 OG1 THR A 109 27.395 43.049 13.760 1.00 15.74 O
ANISOU 670 OG1 THR A 109 1765 2086 2128 197 893 -386 O
ATOM 671 CG2 THR A 109 27.049 42.127 15.974 1.00 13.53 C
ANISOU 671 CG2 THR A 109 1571 1699 1871 180 870 -436 C
ATOM 672 N GLY A 110 26.739 44.686 17.941 1.00 14.05 N
ANISOU 672 N GLY A 110 1692 1641 2006 117 929 -414 N
ATOM 673 CA GLY A 110 26.918 44.608 19.372 1.00 13.56 C
ANISOU 673 CA GLY A 110 1685 1514 1951 102 930 -444 C
ATOM 674 C GLY A 110 27.200 45.913 20.085 1.00 21.27 C
ANISOU 674 C GLY A 110 2680 2439 2964 79 963 -444 C
ATOM 675 O GLY A 110 27.375 45.901 21.311 1.00 18.61 O
ANISOU 675 O GLY A 110 2398 2047 2626 68 961 -475 O
ATOM 676 N ASN A 111 27.246 47.038 19.376 1.00 20.96 N
ANISOU 676 N ASN A 111 2604 2409 2953 72 993 -413 N
ATOM 677 CA ASN A 111 27.524 48.321 20.013 1.00 15.68 C
ANISOU 677 CA ASN A 111 1953 1680 2325 51 1032 -417 C
ATOM 678 C ASN A 111 26.227 48.967 20.477 1.00 16.18 C
ANISOU 678 C ASN A 111 2059 1700 2388 50 1042 -407 C
ATOM 679 O ASN A 111 25.326 49.173 19.655 1.00 18.56 O
ANISOU 679 O ASN A 111 2339 2028 2685 65 1043 -376 O
ATOM 680 CB ASN A 111 28.249 49.256 19.064 1.00 14.61 C
ANISOU 680 CB ASN A 111 1758 1567 2225 38 1071 -387 C
ATOM 681 CG ASN A 111 29.637 48.769 18.713 1.00 21.81 C
ANISOU 681 CG ASN A 111 2615 2528 3144 31 1056 -397 C
ATOM 682 OD1 ASN A 111 30.540 48.800 19.544 1.00 17.20 O
ANISOU 682 OD1 ASN A 111 2039 1918 2577 12 1018 -422 O
ATOM 683 ND2 ASN A 111 29.818 48.329 17.472 1.00 22.32 N
ANISOU 683 ND2 ASN A 111 2625 2669 3187 45 1057 -373 N
ATOM 684 N PRO A 112 26.099 49.331 21.756 1.00 18.47 N
ANISOU 684 N PRO A 112 2410 1926 2683 37 1048 -437 N
ATOM 685 CA PRO A 112 24.837 49.897 22.271 1.00 17.89 C
ANISOU 685 CA PRO A 112 2371 1819 2607 39 1056 -433 C
ATOM 686 C PRO A 112 24.648 51.358 21.868 1.00 20.22 C
ANISOU 686 C PRO A 112 2657 2076 2949 45 1096 -415 C
ATOM 687 O PRO A 112 24.575 52.268 22.704 1.00 17.64 O
ANISOU 687 O PRO A 112 2376 1683 2645 39 1113 -436 O
ATOM 688 CB PRO A 112 24.998 49.724 23.787 1.00 15.50 C
ANISOU 688 CB PRO A 112 2140 1466 2282 22 1045 -473 C
ATOM 689 CG PRO A 112 26.479 49.857 24.006 1.00 21.31 C
ANISOU 689 CG PRO A 112 2882 2177 3038 12 1043 -500 C
ATOM 690 CD PRO A 112 27.138 49.247 22.795 1.00 16.06 C
ANISOU 690 CD PRO A 112 2144 1578 2382 23 1041 -482 C
ATOM 691 N ILE A 113 24.553 51.596 20.560 1.00 18.40 N
ANISOU 691 N ILE A 113 2373 1885 2733 60 1109 -376 N
ATOM 692 CA ILE A 113 24.361 52.953 20.056 1.00 19.08 C
ANISOU 692 CA ILE A 113 2454 1930 2865 72 1154 -352 C
ATOM 693 C ILE A 113 22.951 53.437 20.356 1.00 22.46 C
ANISOU 693 C ILE A 113 2904 2331 3298 99 1151 -356 C
ATOM 694 O ILE A 113 22.755 54.587 20.767 1.00 23.74 O
ANISOU 694 O ILE A 113 3099 2420 3500 109 1179 -365 O
ATOM 695 CB ILE A 113 24.677 53.006 18.551 1.00 18.99 C
ANISOU 695 CB ILE A 113 2385 1976 2853 78 1163 -299 C
ATOM 696 CG1 ILE A 113 26.147 52.666 18.313 1.00 20.23 C
ANISOU 696 CG1 ILE A 113 2512 2168 3005 41 1144 -288 C
ATOM 697 CG2 ILE A 113 24.330 54.380 17.984 1.00 16.16 C
ANISOU 697 CG2 ILE A 113 2035 1576 2528 85 1168 -249 C
ATOM 698 CD1 ILE A 113 26.427 52.097 16.946 1.00 27.20 C
ANISOU 698 CD1 ILE A 113 3337 3136 3862 50 1154 -256 C
ATOM 699 N GLN A 114 21.950 52.578 20.146 1.00 16.47 N
ANISOU 699 N GLN A 114 2125 1629 2505 113 1118 -355 N
ATOM 700 CA GLN A 114 20.570 52.885 20.508 1.00 18.29 C
ANISOU 700 CA GLN A 114 2361 1849 2739 136 1116 -368 C
ATOM 701 C GLN A 114 20.033 54.060 19.699 1.00 24.52 C
ANISOU 701 C GLN A 114 3133 2611 3573 178 1143 -345 C
ATOM 702 O GLN A 114 19.209 53.874 18.797 1.00 22.67 O
ANISOU 702 O GLN A 114 2857 2422 3334 210 1133 -329 O
ATOM 703 CB GLN A 114 20.464 53.167 22.009 1.00 21.69 C
ANISOU 703 CB GLN A 114 2848 2228 3167 118 1121 -406 C
ATOM 704 CG GLN A 114 19.094 53.627 22.464 1.00 39.13 C
ANISOU 704 CG GLN A 114 5056 4429 5384 143 1126 -425 C
ATOM 705 CD GLN A 114 19.168 54.630 23.592 1.00 50.99 C
ANISOU 705 CD GLN A 114 6613 5859 6901 141 1143 -454 C
ATOM 706 OE1 GLN A 114 18.997 55.826 23.379 1.00 47.04 O
ANISOU 706 OE1 GLN A 114 6119 5307 6445 171 1160 -453 O
ATOM 707 NE2 GLN A 114 19.416 54.147 24.805 1.00 62.97 N
ANISOU 707 NE2 GLN A 114 8176 7370 8380 109 1137 -482 N
ATOM 708 N SER A 115 20.492 55.269 20.010 1.00 22.90 N
ANISOU 708 N SER A 115 2964 2325 3413 183 1177 -346 N
ATOM 709 CA SER A 115 20.049 56.466 19.309 1.00 24.08 C
ANISOU 709 CA SER A 115 3112 2424 3614 231 1205 -322 C
ATOM 710 C SER A 115 21.064 56.833 18.229 1.00 21.70 C
ANISOU 710 C SER A 115 2800 2133 3312 206 1187 -251 C
ATOM 711 O SER A 115 22.224 57.140 18.528 1.00 24.04 O
ANISOU 711 O SER A 115 3120 2401 3614 155 1175 -237 O
ATOM 712 CB SER A 115 19.848 57.626 20.283 1.00 32.45 C
ANISOU 712 CB SER A 115 4229 3385 4715 243 1213 -351 C
ATOM 713 OG SER A 115 21.077 58.240 20.624 1.00 66.08 O
ANISOU 713 OG SER A 115 8531 7591 8986 192 1190 -332 O
ATOM 714 N PHE A 116 20.620 56.791 16.976 1.00 20.77 N
ANISOU 714 N PHE A 116 2646 2062 3184 236 1180 -206 N
ATOM 715 CA PHE A 116 21.401 57.242 15.827 1.00 21.66 C
ANISOU 715 CA PHE A 116 2754 2189 3285 214 1165 -130 C
ATOM 716 C PHE A 116 20.876 58.625 15.456 1.00 17.96 C
ANISOU 716 C PHE A 116 2324 1647 2855 246 1147 -86 C
ATOM 717 O PHE A 116 19.840 58.748 14.796 1.00 26.75 O
ANISOU 717 O PHE A 116 3421 2775 3968 306 1135 -73 O
ATOM 718 CB PHE A 116 21.271 56.266 14.661 1.00 16.79 C
ANISOU 718 CB PHE A 116 2086 1673 2621 229 1166 -110 C
ATOM 719 CG PHE A 116 21.918 54.928 14.901 1.00 17.04 C
ANISOU 719 CG PHE A 116 2086 1770 2617 199 1178 -148 C
ATOM 720 CD1 PHE A 116 21.308 53.969 15.696 1.00 18.83 C
ANISOU 720 CD1 PHE A 116 2305 2013 2836 210 1182 -213 C
ATOM 721 CD2 PHE A 116 23.130 54.620 14.302 1.00 23.04 C
ANISOU 721 CD2 PHE A 116 2828 2577 3351 158 1179 -116 C
ATOM 722 CE1 PHE A 116 21.905 52.738 15.905 1.00 16.31 C
ANISOU 722 CE1 PHE A 116 1976 1748 2472 176 1141 -233 C
ATOM 723 CE2 PHE A 116 23.729 53.391 14.503 1.00 20.28 C
ANISOU 723 CE2 PHE A 116 2450 2283 2973 141 1183 -155 C
ATOM 724 CZ PHE A 116 23.115 52.449 15.307 1.00 20.16 C
ANISOU 724 CZ PHE A 116 2442 2275 2942 151 1148 -210 C
ATOM 725 N SER A 117 21.585 59.667 15.890 1.00 18.28 N
ANISOU 725 N SER A 117 2414 1602 2929 208 1138 -64 N
ATOM 726 CA SER A 117 21.153 61.037 15.657 1.00 25.93 C
ANISOU 726 CA SER A 117 3433 2480 3938 237 1116 -24 C
ATOM 727 C SER A 117 21.256 61.385 14.169 1.00 31.32 C
ANISOU 727 C SER A 117 4116 3188 4596 241 1100 67 C
ATOM 728 O SER A 117 21.938 60.693 13.411 1.00 29.66 O
ANISOU 728 O SER A 117 3870 3059 4338 204 1113 99 O
ATOM 729 CB SER A 117 21.991 61.999 16.499 1.00 24.29 C
ANISOU 729 CB SER A 117 3284 2174 3773 184 1108 -26 C
ATOM 730 OG SER A 117 23.366 61.897 16.179 1.00 35.78 O
ANISOU 730 OG SER A 117 4730 3653 5213 102 1112 15 O
ATOM 731 N PRO A 118 20.562 62.438 13.723 1.00 34.30 N
ANISOU 731 N PRO A 118 4536 3497 5000 289 1072 108 N
ATOM 732 CA PRO A 118 20.607 62.803 12.300 1.00 28.10 C
ANISOU 732 CA PRO A 118 3766 2730 4181 295 1053 201 C
ATOM 733 C PRO A 118 22.026 63.010 11.783 1.00 27.19 C
ANISOU 733 C PRO A 118 3668 2623 4041 201 1071 270 C
ATOM 734 O PRO A 118 22.895 63.551 12.473 1.00 29.12 O
ANISOU 734 O PRO A 118 3941 2803 4321 136 1079 267 O
ATOM 735 CB PRO A 118 19.801 64.104 12.248 1.00 29.70 C
ANISOU 735 CB PRO A 118 4032 2821 4431 357 1012 228 C
ATOM 736 CG PRO A 118 18.836 63.987 13.373 1.00 29.71 C
ANISOU 736 CG PRO A 118 4013 2796 4478 418 1014 131 C
ATOM 737 CD PRO A 118 19.574 63.249 14.462 1.00 28.71 C
ANISOU 737 CD PRO A 118 3862 2698 4349 355 1054 65 C
ATOM 738 N GLY A 119 22.252 62.579 10.544 1.00 22.03 N
ANISOU 738 N GLY A 119 2994 2051 3323 192 1078 328 N
ATOM 739 CA GLY A 119 23.564 62.686 9.943 1.00 21.61 C
ANISOU 739 CA GLY A 119 2944 2026 3239 102 1107 392 C
ATOM 740 C GLY A 119 24.611 61.776 10.540 1.00 24.66 C
ANISOU 740 C GLY A 119 3270 2477 3623 39 1143 339 C
ATOM 741 O GLY A 119 25.804 62.009 10.334 1.00 30.74 O
ANISOU 741 O GLY A 119 4036 3254 4389 -43 1168 376 O
ATOM 742 N SER A 120 24.203 60.736 11.276 1.00 22.37 N
ANISOU 742 N SER A 120 2932 2234 3334 75 1145 252 N
ATOM 743 CA SER A 120 25.172 59.857 11.923 1.00 19.71 C
ANISOU 743 CA SER A 120 2547 1949 2995 25 1167 198 C
ATOM 744 C SER A 120 26.036 59.109 10.917 1.00 23.18 C
ANISOU 744 C SER A 120 2934 2495 3376 -10 1196 228 C
ATOM 745 O SER A 120 27.165 58.734 11.248 1.00 27.17 O
ANISOU 745 O SER A 120 3403 3032 3888 -68 1215 207 O
ATOM 746 CB SER A 120 24.458 58.858 12.841 1.00 18.50 C
ANISOU 746 CB SER A 120 2365 1819 2845 74 1162 107 C
ATOM 747 OG SER A 120 23.977 59.503 14.007 1.00 23.64 O
ANISOU 747 OG SER A 120 3058 2375 3549 89 1148 66 O
ATOM 748 N PHE A 121 25.546 58.909 9.694 1.00 19.57 N
ANISOU 748 N PHE A 121 2475 2097 2863 25 1199 273 N
ATOM 749 CA PHE A 121 26.279 58.192 8.659 1.00 22.61 C
ANISOU 749 CA PHE A 121 2816 2590 3183 -1 1231 297 C
ATOM 750 C PHE A 121 26.761 59.104 7.538 1.00 22.76 C
ANISOU 750 C PHE A 121 2872 2607 3169 -45 1250 398 C
ATOM 751 O PHE A 121 27.058 58.619 6.441 1.00 24.37 O
ANISOU 751 O PHE A 121 3054 2902 3302 -49 1277 429 O
ATOM 752 CB PHE A 121 25.411 57.070 8.094 1.00 19.16 C
ANISOU 752 CB PHE A 121 2348 2238 2692 69 1220 262 C
ATOM 753 CG PHE A 121 25.111 55.991 9.085 1.00 21.95 C
ANISOU 753 CG PHE A 121 2663 2609 3068 96 1212 167 C
ATOM 754 CD1 PHE A 121 26.108 55.129 9.499 1.00 17.82 C
ANISOU 754 CD1 PHE A 121 2094 2134 2543 62 1231 121 C
ATOM 755 CD2 PHE A 121 23.837 55.836 9.603 1.00 19.68 C
ANISOU 755 CD2 PHE A 121 2385 2289 2802 156 1184 124 C
ATOM 756 CE1 PHE A 121 25.848 54.134 10.411 1.00 18.61 C
ANISOU 756 CE1 PHE A 121 2173 2240 2656 85 1219 40 C
ATOM 757 CE2 PHE A 121 23.567 54.837 10.519 1.00 18.66 C
ANISOU 757 CE2 PHE A 121 2229 2173 2687 171 1183 43 C
ATOM 758 CZ PHE A 121 24.574 53.985 10.923 1.00 16.72 C
ANISOU 758 CZ PHE A 121 1952 1967 2433 135 1198 5 C
ATOM 759 N SER A 122 26.839 60.408 7.791 1.00 23.72 N
ANISOU 759 N SER A 122 3055 2620 3336 -78 1239 450 N
ATOM 760 CA SER A 122 27.390 61.345 6.823 1.00 22.47 C
ANISOU 760 CA SER A 122 2944 2444 3151 -136 1261 553 C
ATOM 761 C SER A 122 28.808 60.946 6.433 1.00 25.34 C
ANISOU 761 C SER A 122 3248 2892 3487 -222 1321 564 C
ATOM 762 O SER A 122 29.598 60.502 7.270 1.00 27.72 O
ANISOU 762 O SER A 122 3491 3210 3831 -260 1333 501 O
ATOM 763 CB SER A 122 27.382 62.755 7.410 1.00 23.14 C
ANISOU 763 CB SER A 122 3103 2385 3306 -169 1238 592 C
ATOM 764 OG SER A 122 27.793 62.731 8.765 1.00 25.29 O
ANISOU 764 OG SER A 122 3350 2608 3650 -196 1231 519 O
ATOM 765 N GLY A 123 29.124 61.104 5.147 1.00 28.64 N
ANISOU 765 N GLY A 123 3682 3368 3832 -251 1357 642 N
ATOM 766 CA GLY A 123 30.452 60.827 4.642 1.00 24.15 C
ANISOU 766 CA GLY A 123 3056 2887 3234 -335 1424 659 C
ATOM 767 C GLY A 123 30.668 59.429 4.099 1.00 28.79 C
ANISOU 767 C GLY A 123 3566 3619 3755 -299 1453 604 C
ATOM 768 O GLY A 123 31.711 59.178 3.479 1.00 26.50 O
ANISOU 768 O GLY A 123 3227 3415 3427 -359 1515 619 O
ATOM 769 N LEU A 124 29.725 58.510 4.306 1.00 31.27 N
ANISOU 769 N LEU A 124 3866 3960 4055 -207 1412 538 N
ATOM 770 CA LEU A 124 29.865 57.128 3.840 1.00 28.87 C
ANISOU 770 CA LEU A 124 3496 3782 3692 -168 1432 477 C
ATOM 771 C LEU A 124 29.218 56.984 2.460 1.00 29.67 C
ANISOU 771 C LEU A 124 3636 3946 3691 -124 1434 528 C
ATOM 772 O LEU A 124 28.199 56.317 2.271 1.00 33.93 O
ANISOU 772 O LEU A 124 4182 4510 4201 -44 1393 491 O
ATOM 773 CB LEU A 124 29.259 56.170 4.857 1.00 24.99 C
ANISOU 773 CB LEU A 124 2971 3282 3243 -103 1387 377 C
ATOM 774 CG LEU A 124 29.959 56.139 6.214 1.00 24.62 C
ANISOU 774 CG LEU A 124 2887 3187 3281 -141 1381 319 C
ATOM 775 CD1 LEU A 124 29.086 55.458 7.253 1.00 21.09 C
ANISOU 775 CD1 LEU A 124 2440 2703 2869 -77 1333 240 C
ATOM 776 CD2 LEU A 124 31.300 55.433 6.084 1.00 26.29 C
ANISOU 776 CD2 LEU A 124 3016 3489 3484 -184 1425 284 C
ATOM 777 N THR A 125 29.859 57.618 1.475 1.00 26.94 N
ANISOU 777 N THR A 125 3319 3629 3288 -185 1484 613 N
ATOM 778 CA THR A 125 29.251 57.831 0.166 1.00 34.92 C
ANISOU 778 CA THR A 125 4395 4675 4197 -154 1481 685 C
ATOM 779 C THR A 125 29.328 56.622 -0.761 1.00 32.96 C
ANISOU 779 C THR A 125 4106 4567 3852 -115 1507 643 C
ATOM 780 O THR A 125 28.726 56.662 -1.841 1.00 30.89 O
ANISOU 780 O THR A 125 3900 4341 3497 -78 1493 691 O
ATOM 781 CB THR A 125 29.904 59.032 -0.522 1.00 40.83 C
ANISOU 781 CB THR A 125 5206 5393 4914 -241 1528 802 C
ATOM 782 OG1 THR A 125 31.328 58.865 -0.521 1.00 40.32 O
ANISOU 782 OG1 THR A 125 5070 5394 4856 -331 1610 791 O
ATOM 783 CG2 THR A 125 29.534 60.318 0.206 1.00 40.60 C
ANISOU 783 CG2 THR A 125 5247 5210 4969 -262 1485 852 C
ATOM 784 N SER A 126 30.048 55.564 -0.384 1.00 38.59 N
ANISOU 784 N SER A 126 4727 5354 4582 -118 1537 555 N
ATOM 785 CA SER A 126 30.113 54.345 -1.183 1.00 30.18 C
ANISOU 785 CA SER A 126 3622 4412 3433 -75 1547 496 C
ATOM 786 C SER A 126 29.596 53.133 -0.425 1.00 27.87 C
ANISOU 786 C SER A 126 3280 4126 3183 -6 1486 381 C
ATOM 787 O SER A 126 29.805 52.000 -0.875 1.00 30.18 O
ANISOU 787 O SER A 126 3532 4507 3429 19 1463 304 O
ATOM 788 CB SER A 126 31.546 54.086 -1.652 1.00 32.06 C
ANISOU 788 CB SER A 126 3798 4742 3641 -147 1576 468 C
ATOM 789 OG SER A 126 32.075 55.221 -2.311 1.00 43.48 O
ANISOU 789 OG SER A 126 5289 6180 5051 -225 1632 573 O
ATOM 790 N LEU A 127 28.924 53.340 0.705 1.00 29.03 N
ANISOU 790 N LEU A 127 3436 4177 3417 18 1452 363 N
ATOM 791 CA LEU A 127 28.543 52.227 1.562 1.00 26.92 C
ANISOU 791 CA LEU A 127 3126 3908 3195 66 1398 257 C
ATOM 792 C LEU A 127 27.573 51.302 0.841 1.00 25.79 C
ANISOU 792 C LEU A 127 2992 3822 2985 139 1367 220 C
ATOM 793 O LEU A 127 26.561 51.746 0.288 1.00 20.76 O
ANISOU 793 O LEU A 127 2407 3168 2314 177 1341 267 O
ATOM 794 CB LEU A 127 27.921 52.740 2.861 1.00 27.10 C
ANISOU 794 CB LEU A 127 3168 3816 3313 73 1368 248 C
ATOM 795 CG LEU A 127 27.986 51.747 4.027 1.00 23.51 C
ANISOU 795 CG LEU A 127 2670 3348 2916 89 1322 147 C
ATOM 796 CD1 LEU A 127 29.436 51.447 4.382 1.00 20.27 C
ANISOU 796 CD1 LEU A 127 2206 2972 2522 37 1318 113 C
ATOM 797 CD2 LEU A 127 27.227 52.255 5.247 1.00 20.09 C
ANISOU 797 CD2 LEU A 127 2263 2807 2563 101 1307 138 C
ATOM 798 N GLU A 128 27.901 50.011 0.838 1.00 23.00 N
ANISOU 798 N GLU A 128 2590 3530 2618 151 1324 124 N
ATOM 799 CA GLU A 128 27.071 48.981 0.231 1.00 24.68 C
ANISOU 799 CA GLU A 128 2807 3792 2779 210 1288 71 C
ATOM 800 C GLU A 128 26.446 48.035 1.241 1.00 24.90 C
ANISOU 800 C GLU A 128 2814 3780 2867 239 1223 -16 C
ATOM 801 O GLU A 128 25.390 47.464 0.964 1.00 25.41 O
ANISOU 801 O GLU A 128 2891 3853 2912 287 1194 -46 O
ATOM 802 CB GLU A 128 27.891 48.147 -0.763 1.00 23.83 C
ANISOU 802 CB GLU A 128 2674 3781 2599 197 1297 26 C
ATOM 803 CG GLU A 128 28.322 48.885 -2.020 1.00 34.05 C
ANISOU 803 CG GLU A 128 4000 5133 3803 173 1359 107 C
ATOM 804 CD GLU A 128 29.143 48.009 -2.947 1.00 45.49 C
ANISOU 804 CD GLU A 128 5427 6667 5191 158 1377 47 C
ATOM 805 OE1 GLU A 128 28.954 46.773 -2.918 1.00 50.23 O
ANISOU 805 OE1 GLU A 128 6012 7271 5803 192 1339 -46 O
ATOM 806 OE2 GLU A 128 29.981 48.552 -3.697 1.00 50.97 O
ANISOU 806 OE2 GLU A 128 6126 7408 5834 109 1434 93 O
ATOM 807 N ASN A 129 27.070 47.859 2.403 1.00 25.94 N
ANISOU 807 N ASN A 129 2917 3872 3066 211 1198 -53 N
ATOM 808 CA ASN A 129 26.651 46.851 3.371 1.00 22.49 C
ANISOU 808 CA ASN A 129 2468 3407 2670 234 1133 -128 C
ATOM 809 C ASN A 129 26.741 47.466 4.758 1.00 25.91 C
ANISOU 809 C ASN A 129 2911 3750 3183 211 1125 -115 C
ATOM 810 O ASN A 129 27.842 47.732 5.248 1.00 30.03 O
ANISOU 810 O ASN A 129 3414 4264 3731 177 1138 -108 O
ATOM 811 CB ASN A 129 27.524 45.600 3.271 1.00 21.37 C
ANISOU 811 CB ASN A 129 2286 3332 2502 242 1101 -193 C
ATOM 812 CG ASN A 129 27.166 44.558 4.309 1.00 30.54 C
ANISOU 812 CG ASN A 129 3451 4456 3697 275 1037 -243 C
ATOM 813 OD1 ASN A 129 25.996 44.390 4.650 1.00 29.93 O
ANISOU 813 OD1 ASN A 129 3399 4335 3637 291 1012 -256 O
ATOM 814 ND2 ASN A 129 28.171 43.858 4.825 1.00 29.37 N
ANISOU 814 ND2 ASN A 129 3286 4315 3560 289 1018 -263 N
ATOM 815 N LEU A 130 25.592 47.690 5.388 1.00 21.19 N
ANISOU 815 N LEU A 130 2341 3086 2624 230 1109 -117 N
ATOM 816 CA LEU A 130 25.528 48.253 6.730 1.00 18.64 C
ANISOU 816 CA LEU A 130 2036 2674 2374 210 1104 -116 C
ATOM 817 C LEU A 130 24.995 47.191 7.681 1.00 23.44 C
ANISOU 817 C LEU A 130 2649 3259 3000 225 1043 -179 C
ATOM 818 O LEU A 130 23.856 46.734 7.531 1.00 19.06 O
ANISOU 818 O LEU A 130 2100 2708 2436 253 1020 -201 O
ATOM 819 CB LEU A 130 24.644 49.498 6.759 1.00 16.52 C
ANISOU 819 CB LEU A 130 1798 2342 2137 220 1143 -63 C
ATOM 820 CG LEU A 130 24.442 50.152 8.126 1.00 16.63 C
ANISOU 820 CG LEU A 130 1834 2260 2225 204 1145 -69 C
ATOM 821 CD1 LEU A 130 25.771 50.463 8.795 1.00 16.23 C
ANISOU 821 CD1 LEU A 130 1778 2186 2204 155 1160 -65 C
ATOM 822 CD2 LEU A 130 23.616 51.414 7.976 1.00 16.75 C
ANISOU 822 CD2 LEU A 130 1876 2217 2271 227 1192 -15 C
ATOM 823 N VAL A 131 25.814 46.802 8.655 1.00 20.14 N
ANISOU 823 N VAL A 131 2230 2815 2607 206 1023 -204 N
ATOM 824 CA VAL A 131 25.445 45.809 9.658 1.00 18.33 C
ANISOU 824 CA VAL A 131 2019 2553 2391 215 976 -252 C
ATOM 825 C VAL A 131 25.255 46.535 10.981 1.00 15.41 C
ANISOU 825 C VAL A 131 1681 2096 2077 190 984 -249 C
ATOM 826 O VAL A 131 26.232 46.901 11.646 1.00 17.50 O
ANISOU 826 O VAL A 131 1946 2331 2371 165 999 -248 O
ATOM 827 CB VAL A 131 26.497 44.700 9.786 1.00 19.58 C
ANISOU 827 CB VAL A 131 2163 2744 2532 223 951 -285 C
ATOM 828 CG1 VAL A 131 26.073 43.696 10.844 1.00 22.31 C
ANISOU 828 CG1 VAL A 131 2542 3044 2893 229 912 -326 C
ATOM 829 CG2 VAL A 131 26.711 44.007 8.453 1.00 15.06 C
ANISOU 829 CG2 VAL A 131 1562 2260 1902 253 948 -291 C
ATOM 830 N ALA A 132 24.000 46.739 11.371 1.00 15.48 N
ANISOU 830 N ALA A 132 1712 2067 2103 199 978 -254 N
ATOM 831 CA ALA A 132 23.655 47.380 12.634 1.00 14.24 C
ANISOU 831 CA ALA A 132 1588 1831 1993 181 987 -258 C
ATOM 832 C ALA A 132 23.009 46.386 13.594 1.00 19.98 C
ANISOU 832 C ALA A 132 2340 2535 2717 178 951 -299 C
ATOM 833 O ALA A 132 22.046 46.708 14.294 1.00 20.15 O
ANISOU 833 O ALA A 132 2382 2515 2761 175 954 -307 O
ATOM 834 CB ALA A 132 22.740 48.577 12.395 1.00 16.16 C
ANISOU 834 CB ALA A 132 1836 2042 2263 194 1020 -230 C
ATOM 835 N VAL A 133 23.544 45.163 13.635 1.00 22.97 N
ANISOU 835 N VAL A 133 2718 2940 3070 180 923 -324 N
ATOM 836 CA VAL A 133 22.972 44.108 14.461 1.00 15.60 C
ANISOU 836 CA VAL A 133 1813 1981 2131 174 899 -357 C
ATOM 837 C VAL A 133 23.245 44.392 15.930 1.00 13.34 C
ANISOU 837 C VAL A 133 1571 1627 1872 147 909 -369 C
ATOM 838 O VAL A 133 24.368 44.738 16.318 1.00 20.10 O
ANISOU 838 O VAL A 133 2431 2466 2742 138 919 -370 O
ATOM 839 CB VAL A 133 23.541 42.739 14.052 1.00 16.42 C
ANISOU 839 CB VAL A 133 1912 2123 2205 189 873 -381 C
ATOM 840 CG1 VAL A 133 23.125 41.656 15.049 1.00 14.66 C
ANISOU 840 CG1 VAL A 133 1731 1858 1982 175 859 -414 C
ATOM 841 CG2 VAL A 133 23.092 42.382 12.649 1.00 13.57 C
ANISOU 841 CG2 VAL A 133 1516 1828 1811 217 865 -377 C
ATOM 842 N GLU A 134 22.210 44.244 16.753 1.00 13.44 N
ANISOU 842 N GLU A 134 1612 1604 1892 133 911 -382 N
ATOM 843 CA GLU A 134 22.298 44.405 18.204 1.00 16.86 C
ANISOU 843 CA GLU A 134 2093 1974 2337 107 923 -397 C
ATOM 844 C GLU A 134 22.908 45.756 18.577 1.00 19.38 C
ANISOU 844 C GLU A 134 2420 2258 2687 100 949 -384 C
ATOM 845 O GLU A 134 23.899 45.852 19.301 1.00 19.93 O
ANISOU 845 O GLU A 134 2513 2296 2763 88 955 -398 O
ATOM 846 CB GLU A 134 23.078 43.251 18.839 1.00 17.06 C
ANISOU 846 CB GLU A 134 2152 1984 2344 100 908 -424 C
ATOM 847 CG GLU A 134 22.805 43.092 20.330 1.00 23.77 C
ANISOU 847 CG GLU A 134 3065 2774 3190 72 920 -443 C
ATOM 848 CD GLU A 134 23.648 42.006 20.968 1.00 35.54 C
ANISOU 848 CD GLU A 134 4600 4244 4660 72 905 -470 C
ATOM 849 OE1 GLU A 134 24.445 41.375 20.245 1.00 37.40 O
ANISOU 849 OE1 GLU A 134 4810 4511 4890 97 883 -479 O
ATOM 850 OE2 GLU A 134 23.510 41.784 22.193 1.00 38.72 O
ANISOU 850 OE2 GLU A 134 5067 4597 5049 50 915 -485 O
ATOM 851 N THR A 135 22.288 46.815 18.061 1.00 21.09 N
ANISOU 851 N THR A 135 2615 2475 2923 111 967 -362 N
ATOM 852 CA THR A 135 22.639 48.180 18.426 1.00 14.03 C
ANISOU 852 CA THR A 135 1733 1533 2065 105 1001 -352 C
ATOM 853 C THR A 135 21.508 48.876 19.172 1.00 19.44 C
ANISOU 853 C THR A 135 2443 2176 2769 106 1018 -361 C
ATOM 854 O THR A 135 21.499 50.108 19.267 1.00 20.41 O
ANISOU 854 O THR A 135 2572 2256 2925 113 1048 -352 O
ATOM 855 CB THR A 135 23.037 48.981 17.186 1.00 15.13 C
ANISOU 855 CB THR A 135 1833 1697 2219 120 1022 -316 C
ATOM 856 OG1 THR A 135 21.955 48.971 16.249 1.00 16.20 O
ANISOU 856 OG1 THR A 135 1941 1871 2343 148 1015 -301 O
ATOM 857 CG2 THR A 135 24.277 48.380 16.533 1.00 13.96 C
ANISOU 857 CG2 THR A 135 1656 1596 2051 116 1012 -310 C
ATOM 858 N LYS A 136 20.558 48.103 19.707 1.00 20.32 N
ANISOU 858 N LYS A 136 2566 2295 2861 100 1004 -380 N
ATOM 859 CA LYS A 136 19.418 48.642 20.449 1.00 14.86 C
ANISOU 859 CA LYS A 136 1887 1575 2183 101 1022 -395 C
ATOM 860 C LYS A 136 18.606 49.611 19.595 1.00 15.79 C
ANISOU 860 C LYS A 136 1965 1703 2330 137 1034 -380 C
ATOM 861 O LYS A 136 17.970 50.531 20.109 1.00 24.67 O
ANISOU 861 O LYS A 136 3100 2793 3481 150 1056 -391 O
ATOM 862 CB LYS A 136 19.876 49.295 21.758 1.00 17.91 C
ANISOU 862 CB LYS A 136 2329 1899 2577 82 1043 -412 C
ATOM 863 CG LYS A 136 20.601 48.308 22.677 1.00 21.69 C
ANISOU 863 CG LYS A 136 2853 2366 3022 52 1032 -431 C
ATOM 864 CD LYS A 136 21.099 48.954 23.959 1.00 24.00 C
ANISOU 864 CD LYS A 136 3206 2599 3314 36 1049 -452 C
ATOM 865 CE LYS A 136 21.780 47.925 24.850 1.00 37.25 C
ANISOU 865 CE LYS A 136 4936 4266 4952 13 1034 -471 C
ATOM 866 NZ LYS A 136 22.327 48.524 26.097 1.00 47.37 N
ANISOU 866 NZ LYS A 136 6284 5493 6223 0 1042 -496 N
ATOM 867 N LEU A 137 18.645 49.400 18.281 1.00 14.37 N
ANISOU 867 N LEU A 137 1744 1572 2145 159 1021 -359 N
ATOM 868 CA LEU A 137 17.862 50.199 17.350 1.00 23.35 C
ANISOU 868 CA LEU A 137 2844 2722 3306 200 1032 -344 C
ATOM 869 C LEU A 137 16.381 49.898 17.530 1.00 24.45 C
ANISOU 869 C LEU A 137 2957 2884 3448 215 1025 -371 C
ATOM 870 O LEU A 137 15.979 48.733 17.591 1.00 22.93 O
ANISOU 870 O LEU A 137 2754 2729 3230 197 1006 -388 O
ATOM 871 CB LEU A 137 18.299 49.907 15.915 1.00 14.67 C
ANISOU 871 CB LEU A 137 1710 1675 2187 217 1023 -316 C
ATOM 872 CG LEU A 137 17.543 50.587 14.776 1.00 17.83 C
ANISOU 872 CG LEU A 137 2074 2097 2605 266 1036 -297 C
ATOM 873 CD1 LEU A 137 17.697 52.096 14.846 1.00 15.52 C
ANISOU 873 CD1 LEU A 137 1800 1737 2361 290 1078 -272 C
ATOM 874 CD2 LEU A 137 18.014 50.045 13.426 1.00 15.05 C
ANISOU 874 CD2 LEU A 137 1694 1808 2216 277 1027 -273 C
ATOM 875 N ALA A 138 15.568 50.951 17.608 1.00 27.17 N
ANISOU 875 N ALA A 138 3289 3204 3831 249 1045 -378 N
ATOM 876 CA ALA A 138 14.160 50.813 17.943 1.00 15.77 C
ANISOU 876 CA ALA A 138 1814 1780 2398 264 1045 -411 C
ATOM 877 C ALA A 138 13.229 50.912 16.743 1.00 21.66 C
ANISOU 877 C ALA A 138 2496 2573 3160 315 1035 -411 C
ATOM 878 O ALA A 138 12.117 50.373 16.804 1.00 25.90 O
ANISOU 878 O ALA A 138 2993 3147 3700 320 1030 -441 O
ATOM 879 CB ALA A 138 13.757 51.873 18.977 1.00 16.20 C
ANISOU 879 CB ALA A 138 1892 1780 2485 276 1071 -432 C
ATOM 880 N SER A 139 13.637 51.582 15.666 1.00 21.88 N
ANISOU 880 N SER A 139 2514 2597 3203 354 1038 -378 N
ATOM 881 CA SER A 139 12.784 51.685 14.491 1.00 29.98 C
ANISOU 881 CA SER A 139 3481 3664 4244 411 1029 -378 C
ATOM 882 C SER A 139 13.603 52.155 13.297 1.00 26.03 C
ANISOU 882 C SER A 139 2989 3162 3741 439 1041 -328 C
ATOM 883 O SER A 139 14.629 52.826 13.449 1.00 24.33 O
ANISOU 883 O SER A 139 2819 2894 3532 427 1067 -293 O
ATOM 884 CB SER A 139 11.608 52.641 14.725 1.00 34.65 C
ANISOU 884 CB SER A 139 4043 4232 4890 468 1035 -403 C
ATOM 885 OG SER A 139 12.007 53.992 14.589 1.00 33.29 O
ANISOU 885 OG SER A 139 3900 3988 4759 512 1056 -373 O
ATOM 886 N LEU A 140 13.122 51.799 12.102 1.00 26.71 N
ANISOU 886 N LEU A 140 3029 3304 3818 478 1028 -324 N
ATOM 887 CA LEU A 140 13.791 52.197 10.868 1.00 21.06 C
ANISOU 887 CA LEU A 140 2320 2593 3090 513 1050 -268 C
ATOM 888 C LEU A 140 13.444 53.622 10.465 1.00 28.70 C
ANISOU 888 C LEU A 140 3301 3505 4098 580 1044 -223 C
ATOM 889 O LEU A 140 14.264 54.300 9.835 1.00 30.17 O
ANISOU 889 O LEU A 140 3537 3672 4256 574 1028 -151 O
ATOM 890 CB LEU A 140 13.424 51.233 9.741 1.00 19.27 C
ANISOU 890 CB LEU A 140 2048 2450 2824 531 1028 -278 C
ATOM 891 CG LEU A 140 13.992 49.820 9.827 1.00 27.29 C
ANISOU 891 CG LEU A 140 3068 3519 3779 465 1004 -303 C
ATOM 892 CD1 LEU A 140 13.626 49.020 8.588 1.00 21.32 C
ANISOU 892 CD1 LEU A 140 2272 2839 2989 493 990 -315 C
ATOM 893 CD2 LEU A 140 15.494 49.869 10.004 1.00 27.19 C
ANISOU 893 CD2 LEU A 140 3107 3488 3736 420 1020 -267 C
ATOM 894 N GLU A 141 12.234 54.079 10.798 1.00 34.71 N
ANISOU 894 N GLU A 141 4027 4246 4917 634 1033 -261 N
ATOM 895 CA GLU A 141 11.815 55.436 10.460 1.00 38.72 C
ANISOU 895 CA GLU A 141 4557 4696 5458 698 993 -219 C
ATOM 896 C GLU A 141 12.816 56.474 10.955 1.00 34.98 C
ANISOU 896 C GLU A 141 4164 4134 4994 672 1010 -171 C
ATOM 897 O GLU A 141 13.109 57.451 10.254 1.00 33.63 O
ANISOU 897 O GLU A 141 4043 3920 4815 695 973 -99 O
ATOM 898 CB GLU A 141 10.428 55.709 11.043 1.00 48.55 C
ANISOU 898 CB GLU A 141 5743 5928 6775 758 992 -287 C
ATOM 899 CG GLU A 141 9.308 54.860 10.450 1.00 66.68 C
ANISOU 899 CG GLU A 141 7950 8310 9075 790 964 -334 C
ATOM 900 CD GLU A 141 8.764 55.434 9.154 1.00 79.61 C
ANISOU 900 CD GLU A 141 9579 9965 10705 866 879 -287 C
ATOM 901 OE1 GLU A 141 9.326 56.433 8.660 1.00 86.66 O
ANISOU 901 OE1 GLU A 141 10544 10803 11580 888 847 -210 O
ATOM 902 OE2 GLU A 141 7.769 54.893 8.630 1.00 82.21 O
ANISOU 902 OE2 GLU A 141 9831 10360 11045 902 842 -327 O
ATOM 903 N SER A 142 13.357 56.278 12.154 1.00 36.09 N
ANISOU 903 N SER A 142 4323 4241 5149 620 1062 -209 N
ATOM 904 CA SER A 142 14.305 57.212 12.746 1.00 39.79 C
ANISOU 904 CA SER A 142 4864 4624 5632 588 1076 -176 C
ATOM 905 C SER A 142 15.755 56.894 12.400 1.00 37.57 C
ANISOU 905 C SER A 142 4617 4361 5298 516 1086 -125 C
ATOM 906 O SER A 142 16.659 57.596 12.866 1.00 34.06 O
ANISOU 906 O SER A 142 4226 3851 4866 477 1096 -98 O
ATOM 907 CB SER A 142 14.135 57.234 14.266 1.00 41.32 C
ANISOU 907 CB SER A 142 5064 4770 5864 572 1121 -248 C
ATOM 908 OG SER A 142 15.145 58.014 14.875 1.00 57.83 O
ANISOU 908 OG SER A 142 7225 6783 7965 532 1130 -224 O
ATOM 909 N PHE A 143 15.995 55.870 11.584 1.00 26.66 N
ANISOU 909 N PHE A 143 3203 3067 3862 499 1082 -116 N
ATOM 910 CA PHE A 143 17.345 55.434 11.258 1.00 23.45 C
ANISOU 910 CA PHE A 143 2813 2690 3407 437 1097 -81 C
ATOM 911 C PHE A 143 17.876 56.268 10.095 1.00 25.64 C
ANISOU 911 C PHE A 143 3126 2962 3654 437 1074 10 C
ATOM 912 O PHE A 143 17.353 56.150 8.976 1.00 27.34 O
ANISOU 912 O PHE A 143 3328 3226 3833 476 1043 39 O
ATOM 913 CB PHE A 143 17.337 53.955 10.902 1.00 22.45 C
ANISOU 913 CB PHE A 143 2639 2657 3235 424 1105 -119 C
ATOM 914 CG PHE A 143 18.651 53.265 11.109 1.00 20.07 C
ANISOU 914 CG PHE A 143 2344 2380 2901 364 1130 -121 C
ATOM 915 CD1 PHE A 143 19.464 53.595 12.181 1.00 23.73 C
ANISOU 915 CD1 PHE A 143 2838 2786 3392 321 1152 -131 C
ATOM 916 CD2 PHE A 143 19.059 52.262 10.243 1.00 18.95 C
ANISOU 916 CD2 PHE A 143 2176 2321 2703 355 1128 -119 C
ATOM 917 CE1 PHE A 143 20.672 52.947 12.376 1.00 24.15 C
ANISOU 917 CE1 PHE A 143 2890 2865 3421 271 1164 -137 C
ATOM 918 CE2 PHE A 143 20.267 51.610 10.431 1.00 16.74 C
ANISOU 918 CE2 PHE A 143 1899 2067 2394 303 1128 -126 C
ATOM 919 CZ PHE A 143 21.073 51.953 11.500 1.00 19.63 C
ANISOU 919 CZ PHE A 143 2290 2377 2790 262 1138 -134 C
ATOM 920 N PRO A 144 18.905 57.103 10.295 1.00 27.49 N
ANISOU 920 N PRO A 144 3409 3137 3898 390 1086 57 N
ATOM 921 CA PRO A 144 19.334 58.062 9.246 1.00 25.56 C
ANISOU 921 CA PRO A 144 3210 2871 3629 383 1067 151 C
ATOM 922 C PRO A 144 20.173 57.426 8.142 1.00 25.47 C
ANISOU 922 C PRO A 144 3185 2949 3542 347 1082 194 C
ATOM 923 O PRO A 144 21.376 57.669 7.978 1.00 29.30 O
ANISOU 923 O PRO A 144 3688 3435 4011 282 1110 236 O
ATOM 924 CB PRO A 144 20.112 59.102 10.059 1.00 25.34 C
ANISOU 924 CB PRO A 144 3234 2744 3650 335 1080 172 C
ATOM 925 CG PRO A 144 20.718 58.297 11.180 1.00 22.67 C
ANISOU 925 CG PRO A 144 2866 2421 3326 290 1113 101 C
ATOM 926 CD PRO A 144 19.703 57.233 11.527 1.00 25.79 C
ANISOU 926 CD PRO A 144 3212 2869 3718 337 1114 26 C
ATOM 927 N ILE A 145 19.529 56.589 7.332 1.00 21.81 N
ANISOU 927 N ILE A 145 2687 2570 3031 388 1065 179 N
ATOM 928 CA ILE A 145 20.181 55.942 6.202 1.00 20.38 C
ANISOU 928 CA ILE A 145 2495 2481 2770 367 1077 210 C
ATOM 929 C ILE A 145 19.571 56.378 4.877 1.00 19.97 C
ANISOU 929 C ILE A 145 2473 2453 2664 413 1037 274 C
ATOM 930 O ILE A 145 19.886 55.799 3.833 1.00 25.29 O
ANISOU 930 O ILE A 145 3140 3211 3258 409 1042 294 O
ATOM 931 CB ILE A 145 20.149 54.410 6.339 1.00 22.18 C
ANISOU 931 CB ILE A 145 2662 2793 2974 368 1090 131 C
ATOM 932 CG1 ILE A 145 18.704 53.914 6.417 1.00 19.99 C
ANISOU 932 CG1 ILE A 145 2352 2529 2714 431 1053 76 C
ATOM 933 CG2 ILE A 145 20.925 53.968 7.569 1.00 22.49 C
ANISOU 933 CG2 ILE A 145 2684 2809 3053 319 1125 79 C
ATOM 934 CD1 ILE A 145 18.551 52.405 6.355 1.00 20.43 C
ANISOU 934 CD1 ILE A 145 2357 2664 2741 432 1058 6 C
ATOM 935 N GLY A 146 18.707 57.394 4.891 1.00 28.63 N
ANISOU 935 N GLY A 146 3606 3475 3798 463 994 304 N
ATOM 936 CA GLY A 146 17.988 57.846 3.714 1.00 28.35 C
ANISOU 936 CA GLY A 146 3604 3452 3715 520 940 362 C
ATOM 937 C GLY A 146 18.836 58.430 2.604 1.00 31.68 C
ANISOU 937 C GLY A 146 4093 3885 4061 482 950 466 C
ATOM 938 O GLY A 146 18.309 58.667 1.512 1.00 27.49 O
ANISOU 938 O GLY A 146 3598 3378 3470 528 904 517 O
ATOM 939 N GLN A 147 20.126 58.673 2.842 1.00 27.54 N
ANISOU 939 N GLN A 147 3586 3346 3534 398 1009 498 N
ATOM 940 CA GLN A 147 21.009 59.230 1.824 1.00 26.82 C
ANISOU 940 CA GLN A 147 3554 3268 3370 346 1034 597 C
ATOM 941 C GLN A 147 22.160 58.294 1.474 1.00 32.82 C
ANISOU 941 C GLN A 147 4268 4131 4069 282 1100 581 C
ATOM 942 O GLN A 147 23.039 58.672 0.689 1.00 36.95 O
ANISOU 942 O GLN A 147 4828 4679 4531 225 1139 655 O
ATOM 943 CB GLN A 147 21.547 60.589 2.276 1.00 30.87 C
ANISOU 943 CB GLN A 147 4132 3661 3936 296 1045 664 C
ATOM 944 CG GLN A 147 20.465 61.651 2.457 1.00 44.89 C
ANISOU 944 CG GLN A 147 5967 5326 5764 366 976 690 C
ATOM 945 CD GLN A 147 20.868 62.743 3.430 1.00 60.65 C
ANISOU 945 CD GLN A 147 8007 7192 7847 325 985 706 C
ATOM 946 OE1 GLN A 147 21.465 62.470 4.472 1.00 69.77 O
ANISOU 946 OE1 GLN A 147 9118 8336 9056 276 1025 647 O
ATOM 947 NE2 GLN A 147 20.544 63.986 3.096 1.00 66.24 N
ANISOU 947 NE2 GLN A 147 8805 7795 8567 346 942 785 N
ATOM 948 N LEU A 148 22.182 57.084 2.037 1.00 26.49 N
ANISOU 948 N LEU A 148 3390 3390 3284 289 1115 484 N
ATOM 949 CA LEU A 148 23.126 56.046 1.624 1.00 28.07 C
ANISOU 949 CA LEU A 148 3543 3696 3426 251 1166 455 C
ATOM 950 C LEU A 148 22.586 55.386 0.352 1.00 29.79 C
ANISOU 950 C LEU A 148 3765 4008 3544 300 1142 459 C
ATOM 951 O LEU A 148 22.182 54.222 0.325 1.00 34.13 O
ANISOU 951 O LEU A 148 4265 4623 4078 337 1127 382 O
ATOM 952 CB LEU A 148 23.340 55.042 2.750 1.00 28.68 C
ANISOU 952 CB LEU A 148 3550 3785 3560 244 1181 354 C
ATOM 953 CG LEU A 148 23.839 55.605 4.081 1.00 24.49 C
ANISOU 953 CG LEU A 148 3018 3166 3122 199 1197 339 C
ATOM 954 CD1 LEU A 148 23.804 54.523 5.143 1.00 21.51 C
ANISOU 954 CD1 LEU A 148 2585 2802 2788 208 1198 238 C
ATOM 955 CD2 LEU A 148 25.244 56.168 3.929 1.00 25.09 C
ANISOU 955 CD2 LEU A 148 3101 3241 3192 116 1249 392 C
ATOM 956 N ILE A 149 22.579 56.175 -0.726 1.00 28.35 N
ANISOU 956 N ILE A 149 3651 3827 3292 299 1134 553 N
ATOM 957 CA ILE A 149 21.959 55.770 -1.981 1.00 26.52 C
ANISOU 957 CA ILE A 149 3444 3673 2959 352 1097 569 C
ATOM 958 C ILE A 149 22.651 54.577 -2.626 1.00 28.38 C
ANISOU 958 C ILE A 149 3637 4033 3113 335 1143 524 C
ATOM 959 O ILE A 149 22.097 53.970 -3.548 1.00 28.40 O
ANISOU 959 O ILE A 149 3647 4109 3035 384 1109 508 O
ATOM 960 CB ILE A 149 21.923 56.964 -2.960 1.00 27.32 C
ANISOU 960 CB ILE A 149 3645 3740 2995 348 1081 691 C
ATOM 961 CG1 ILE A 149 23.326 57.261 -3.493 1.00 40.85 C
ANISOU 961 CG1 ILE A 149 5384 5491 4647 256 1168 757 C
ATOM 962 CG2 ILE A 149 21.346 58.188 -2.270 1.00 24.99 C
ANISOU 962 CG2 ILE A 149 3397 3310 2790 365 1036 733 C
ATOM 963 CD1 ILE A 149 23.426 58.537 -4.295 1.00 44.97 C
ANISOU 963 CD1 ILE A 149 6015 5960 5112 231 1164 888 C
ATOM 964 N THR A 150 23.846 54.223 -2.159 1.00 24.84 N
ANISOU 964 N THR A 150 3143 3610 2686 272 1215 497 N
ATOM 965 CA THR A 150 24.572 53.066 -2.660 1.00 24.00 C
ANISOU 965 CA THR A 150 2988 3617 2514 262 1261 442 C
ATOM 966 C THR A 150 24.258 51.786 -1.894 1.00 28.70 C
ANISOU 966 C THR A 150 3512 4231 3161 297 1240 324 C
ATOM 967 O THR A 150 24.681 50.708 -2.327 1.00 32.41 O
ANISOU 967 O THR A 150 3946 4790 3578 305 1263 266 O
ATOM 968 CB THR A 150 26.082 53.332 -2.599 1.00 26.27 C
ANISOU 968 CB THR A 150 3254 3927 2801 178 1349 470 C
ATOM 969 OG1 THR A 150 26.446 53.690 -1.258 1.00 27.45 O
ANISOU 969 OG1 THR A 150 3371 3992 3067 141 1356 449 O
ATOM 970 CG2 THR A 150 26.475 54.464 -3.548 1.00 24.45 C
ANISOU 970 CG2 THR A 150 3098 3694 2499 131 1383 589 C
ATOM 971 N LEU A 151 23.521 51.876 -0.787 1.00 27.38 N
ANISOU 971 N LEU A 151 3330 3983 3090 317 1199 288 N
ATOM 972 CA LEU A 151 23.332 50.731 0.096 1.00 27.91 C
ANISOU 972 CA LEU A 151 3339 4055 3212 334 1188 185 C
ATOM 973 C LEU A 151 22.611 49.599 -0.624 1.00 26.45 C
ANISOU 973 C LEU A 151 3138 3944 2967 388 1150 125 C
ATOM 974 O LEU A 151 21.551 49.795 -1.228 1.00 24.55 O
ANISOU 974 O LEU A 151 2924 3707 2697 433 1096 142 O
ATOM 975 CB LEU A 151 22.550 51.147 1.342 1.00 23.30 C
ANISOU 975 CB LEU A 151 2752 3370 2730 345 1154 164 C
ATOM 976 CG LEU A 151 22.507 50.156 2.508 1.00 21.42 C
ANISOU 976 CG LEU A 151 2466 3117 2555 344 1155 71 C
ATOM 977 CD1 LEU A 151 23.886 49.997 3.129 1.00 23.41 C
ANISOU 977 CD1 LEU A 151 2694 3368 2831 290 1205 58 C
ATOM 978 CD2 LEU A 151 21.479 50.590 3.553 1.00 18.06 C
ANISOU 978 CD2 LEU A 151 2044 2604 2213 364 1122 53 C
ATOM 979 N LYS A 152 23.203 48.409 -0.563 1.00 22.50 N
ANISOU 979 N LYS A 152 2596 3500 2451 384 1174 52 N
ATOM 980 CA LYS A 152 22.637 47.198 -1.139 1.00 24.38 C
ANISOU 980 CA LYS A 152 2819 3804 2641 428 1140 -18 C
ATOM 981 C LYS A 152 22.054 46.265 -0.090 1.00 28.44 C
ANISOU 981 C LYS A 152 3297 4278 3231 440 1111 -105 C
ATOM 982 O LYS A 152 21.003 45.661 -0.322 1.00 31.14 O
ANISOU 982 O LYS A 152 3634 4633 3567 476 1061 -149 O
ATOM 983 CB LYS A 152 23.702 46.449 -1.944 1.00 23.92 C
ANISOU 983 CB LYS A 152 2749 3830 2508 413 1175 -47 C
ATOM 984 CG LYS A 152 24.315 47.249 -3.080 1.00 28.60 C
ANISOU 984 CG LYS A 152 3378 4487 3003 402 1228 39 C
ATOM 985 CD LYS A 152 25.274 46.390 -3.892 1.00 32.84 C
ANISOU 985 CD LYS A 152 3904 5089 3485 375 1237 -14 C
ATOM 986 CE LYS A 152 25.878 47.162 -5.053 1.00 41.56 C
ANISOU 986 CE LYS A 152 5047 6259 4485 353 1293 69 C
ATOM 987 NZ LYS A 152 26.790 46.301 -5.854 1.00 46.57 N
ANISOU 987 NZ LYS A 152 5671 6953 5072 331 1310 9 N
ATOM 988 N LYS A 153 22.713 46.135 1.059 1.00 21.77 N
ANISOU 988 N LYS A 153 2434 3374 2463 388 1109 -137 N
ATOM 989 CA LYS A 153 22.290 45.226 2.115 1.00 20.69 C
ANISOU 989 CA LYS A 153 2276 3193 2391 376 1059 -217 C
ATOM 990 C LYS A 153 22.168 45.983 3.428 1.00 22.42 C
ANISOU 990 C LYS A 153 2500 3331 2688 356 1056 -195 C
ATOM 991 O LYS A 153 23.043 46.781 3.775 1.00 21.60 O
ANISOU 991 O LYS A 153 2404 3201 2603 324 1084 -151 O
ATOM 992 CB LYS A 153 23.277 44.066 2.284 1.00 20.06 C
ANISOU 992 CB LYS A 153 2174 3141 2306 346 1034 -286 C
ATOM 993 CG LYS A 153 23.374 43.146 1.083 1.00 35.04 C
ANISOU 993 CG LYS A 153 4088 5073 4154 359 1050 -321 C
ATOM 994 CD LYS A 153 24.302 41.982 1.378 1.00 41.82 C
ANISOU 994 CD LYS A 153 4963 5880 5048 345 1044 -358 C
ATOM 995 CE LYS A 153 24.243 40.922 0.292 1.00 52.54 C
ANISOU 995 CE LYS A 153 6338 7281 6342 391 1043 -384 C
ATOM 996 NZ LYS A 153 24.952 39.685 0.721 1.00 58.44 N
ANISOU 996 NZ LYS A 153 7101 7990 7114 411 1026 -411 N
ATOM 997 N LEU A 154 21.080 45.725 4.156 1.00 19.31 N
ANISOU 997 N LEU A 154 2102 2895 2341 369 1024 -229 N
ATOM 998 CA LEU A 154 20.848 46.308 5.473 1.00 16.05 C
ANISOU 998 CA LEU A 154 1700 2401 1999 350 1017 -221 C
ATOM 999 C LEU A 154 20.517 45.186 6.443 1.00 22.61 C
ANISOU 999 C LEU A 154 2528 3214 2850 338 964 -280 C
ATOM 1000 O LEU A 154 19.512 44.489 6.268 1.00 23.07 O
ANISOU 1000 O LEU A 154 2573 3288 2904 359 942 -316 O
ATOM 1001 CB LEU A 154 19.713 47.335 5.442 1.00 16.35 C
ANISOU 1001 CB LEU A 154 1742 2398 2072 385 1043 -189 C
ATOM 1002 CG LEU A 154 19.362 47.932 6.810 1.00 20.94 C
ANISOU 1002 CG LEU A 154 2335 2896 2727 367 1037 -194 C
ATOM 1003 CD1 LEU A 154 20.532 48.734 7.359 1.00 17.94 C
ANISOU 1003 CD1 LEU A 154 1980 2471 2366 330 1066 -154 C
ATOM 1004 CD2 LEU A 154 18.101 48.780 6.748 1.00 24.89 C
ANISOU 1004 CD2 LEU A 154 2826 3362 3268 417 1054 -179 C
ATOM 1005 N ASN A 155 21.359 45.011 7.460 1.00 15.10 N
ANISOU 1005 N ASN A 155 1593 2225 1919 307 950 -282 N
ATOM 1006 CA ASN A 155 21.150 44.013 8.504 1.00 16.44 C
ANISOU 1006 CA ASN A 155 1780 2361 2107 296 912 -319 C
ATOM 1007 C ASN A 155 20.871 44.753 9.806 1.00 19.73 C
ANISOU 1007 C ASN A 155 2219 2700 2577 270 918 -310 C
ATOM 1008 O ASN A 155 21.752 45.435 10.341 1.00 15.14 O
ANISOU 1008 O ASN A 155 1652 2086 2015 249 935 -290 O
ATOM 1009 CB ASN A 155 22.366 43.095 8.638 1.00 15.59 C
ANISOU 1009 CB ASN A 155 1678 2269 1977 291 894 -335 C
ATOM 1010 CG ASN A 155 22.079 41.854 9.469 1.00 17.51 C
ANISOU 1010 CG ASN A 155 1947 2477 2229 286 863 -372 C
ATOM 1011 OD1 ASN A 155 21.045 41.767 10.133 1.00 21.12 O
ANISOU 1011 OD1 ASN A 155 2417 2893 2712 273 858 -384 O
ATOM 1012 ND2 ASN A 155 22.998 40.893 9.443 1.00 20.50 N
ANISOU 1012 ND2 ASN A 155 2332 2867 2589 296 848 -393 N
ATOM 1013 N VAL A 156 19.642 44.628 10.303 1.00 15.79 N
ANISOU 1013 N VAL A 156 1723 2175 2101 272 909 -330 N
ATOM 1014 CA VAL A 156 19.254 45.212 11.582 1.00 14.70 C
ANISOU 1014 CA VAL A 156 1609 1970 2007 250 916 -330 C
ATOM 1015 C VAL A 156 18.651 44.117 12.449 1.00 21.43 C
ANISOU 1015 C VAL A 156 2478 2802 2863 230 896 -365 C
ATOM 1016 O VAL A 156 17.694 44.349 13.197 1.00 15.13 O
ANISOU 1016 O VAL A 156 1684 1971 2092 219 904 -377 O
ATOM 1017 CB VAL A 156 18.279 46.385 11.390 1.00 18.81 C
ANISOU 1017 CB VAL A 156 2112 2474 2560 273 941 -316 C
ATOM 1018 CG1 VAL A 156 19.011 47.570 10.771 1.00 14.82 C
ANISOU 1018 CG1 VAL A 156 1608 1962 2060 284 976 -271 C
ATOM 1019 CG2 VAL A 156 17.105 45.954 10.526 1.00 17.90 C
ANISOU 1019 CG2 VAL A 156 1959 2408 2436 305 932 -336 C
ATOM 1020 N ALA A 157 19.213 42.917 12.359 1.00 21.37 N
ANISOU 1020 N ALA A 157 2481 2809 2828 224 877 -384 N
ATOM 1021 CA ALA A 157 18.757 41.824 13.199 1.00 18.14 C
ANISOU 1021 CA ALA A 157 2098 2370 2425 198 869 -415 C
ATOM 1022 C ALA A 157 19.129 42.079 14.659 1.00 15.53 C
ANISOU 1022 C ALA A 157 1809 1975 2115 166 879 -415 C
ATOM 1023 O ALA A 157 20.059 42.829 14.968 1.00 18.82 O
ANISOU 1023 O ALA A 157 2237 2374 2538 164 884 -396 O
ATOM 1024 CB ALA A 157 19.352 40.500 12.726 1.00 13.64 C
ANISOU 1024 CB ALA A 157 1536 1822 1826 205 850 -438 C
ATOM 1025 N HIS A 158 18.369 41.453 15.561 1.00 18.03 N
ANISOU 1025 N HIS A 158 2151 2257 2443 136 888 -438 N
ATOM 1026 CA HIS A 158 18.674 41.432 16.995 1.00 17.64 C
ANISOU 1026 CA HIS A 158 2152 2148 2401 103 902 -444 C
ATOM 1027 C HIS A 158 18.611 42.833 17.610 1.00 14.81 C
ANISOU 1027 C HIS A 158 1799 1762 2066 102 920 -426 C
ATOM 1028 O HIS A 158 19.486 43.241 18.375 1.00 19.50 O
ANISOU 1028 O HIS A 158 2427 2321 2663 92 926 -422 O
ATOM 1029 CB HIS A 158 20.037 40.776 17.251 1.00 15.16 C
ANISOU 1029 CB HIS A 158 1870 1820 2070 104 887 -451 C
ATOM 1030 CG HIS A 158 20.235 40.301 18.658 1.00 15.91 C
ANISOU 1030 CG HIS A 158 2027 1855 2163 72 901 -468 C
ATOM 1031 ND1 HIS A 158 21.128 39.304 18.987 1.00 18.10 N
ANISOU 1031 ND1 HIS A 158 2343 2113 2423 73 888 -488 N
ATOM 1032 CD2 HIS A 158 19.658 40.687 19.820 1.00 19.93 C
ANISOU 1032 CD2 HIS A 158 2571 2321 2680 41 928 -470 C
ATOM 1033 CE1 HIS A 158 21.091 39.095 20.290 1.00 18.61 C
ANISOU 1033 CE1 HIS A 158 2469 2121 2480 44 907 -498 C
ATOM 1034 NE2 HIS A 158 20.208 39.922 20.820 1.00 21.60 N
ANISOU 1034 NE2 HIS A 158 2846 2487 2873 21 933 -487 N
ATOM 1035 N ASN A 159 17.555 43.576 17.275 1.00 15.92 N
ANISOU 1035 N ASN A 159 1906 1918 2226 115 931 -422 N
ATOM 1036 CA ASN A 159 17.346 44.899 17.859 1.00 15.43 C
ANISOU 1036 CA ASN A 159 1850 1824 2189 119 952 -412 C
ATOM 1037 C ASN A 159 16.000 44.960 18.574 1.00 19.62 C
ANISOU 1037 C ASN A 159 2376 2342 2736 106 975 -434 C
ATOM 1038 O ASN A 159 15.480 43.929 19.015 1.00 17.66 O
ANISOU 1038 O ASN A 159 2139 2093 2480 77 982 -455 O
ATOM 1039 CB ASN A 159 17.439 45.988 16.788 1.00 16.78 C
ANISOU 1039 CB ASN A 159 1984 2019 2374 157 953 -387 C
ATOM 1040 CG ASN A 159 18.868 46.256 16.354 1.00 19.25 C
ANISOU 1040 CG ASN A 159 2305 2333 2677 160 948 -364 C
ATOM 1041 OD1 ASN A 159 19.723 46.588 17.176 1.00 17.40 O
ANISOU 1041 OD1 ASN A 159 2104 2056 2450 141 958 -363 O
ATOM 1042 ND2 ASN A 159 19.137 46.106 15.061 1.00 19.85 N
ANISOU 1042 ND2 ASN A 159 2347 2461 2735 183 938 -348 N
ATOM 1043 N PHE A 160 15.431 46.160 18.705 1.00 14.45 N
ANISOU 1043 N PHE A 160 1705 1676 2109 127 992 -431 N
ATOM 1044 CA PHE A 160 14.142 46.354 19.358 1.00 19.83 C
ANISOU 1044 CA PHE A 160 2372 2352 2809 122 1017 -457 C
ATOM 1045 C PHE A 160 13.071 46.819 18.376 1.00 20.49 C
ANISOU 1045 C PHE A 160 2389 2479 2919 166 1014 -462 C
ATOM 1046 O PHE A 160 12.101 47.469 18.773 1.00 23.68 O
ANISOU 1046 O PHE A 160 2769 2878 3349 182 1035 -481 O
ATOM 1047 CB PHE A 160 14.264 47.352 20.510 1.00 17.30 C
ANISOU 1047 CB PHE A 160 2089 1981 2502 117 1042 -462 C
ATOM 1048 CG PHE A 160 15.276 46.964 21.550 1.00 20.93 C
ANISOU 1048 CG PHE A 160 2616 2398 2937 79 1047 -462 C
ATOM 1049 CD1 PHE A 160 15.417 45.645 21.947 1.00 26.08 C
ANISOU 1049 CD1 PHE A 160 3295 3051 3561 42 1046 -471 C
ATOM 1050 CD2 PHE A 160 16.090 47.924 22.129 1.00 28.68 C
ANISOU 1050 CD2 PHE A 160 3637 3335 3926 81 1056 -455 C
ATOM 1051 CE1 PHE A 160 16.350 45.289 22.908 1.00 25.42 C
ANISOU 1051 CE1 PHE A 160 3277 2928 3454 13 1050 -473 C
ATOM 1052 CE2 PHE A 160 17.028 47.575 23.086 1.00 30.96 C
ANISOU 1052 CE2 PHE A 160 3985 3587 4190 50 1058 -460 C
ATOM 1053 CZ PHE A 160 17.157 46.256 23.478 1.00 31.20 C
ANISOU 1053 CZ PHE A 160 4043 3622 4189 19 1054 -468 C
ATOM 1054 N ILE A 161 13.241 46.508 17.091 1.00 22.14 N
ANISOU 1054 N ILE A 161 2565 2730 3118 190 990 -449 N
ATOM 1055 CA ILE A 161 12.252 46.898 16.096 1.00 19.21 C
ANISOU 1055 CA ILE A 161 2130 2401 2768 237 987 -456 C
ATOM 1056 C ILE A 161 10.963 46.124 16.331 1.00 22.58 C
ANISOU 1056 C ILE A 161 2517 2853 3208 220 998 -493 C
ATOM 1057 O ILE A 161 10.964 44.888 16.408 1.00 20.85 O
ANISOU 1057 O ILE A 161 2307 2643 2971 180 996 -506 O
ATOM 1058 CB ILE A 161 12.794 46.669 14.678 1.00 15.45 C
ANISOU 1058 CB ILE A 161 1633 1966 2271 264 964 -435 C
ATOM 1059 CG1 ILE A 161 14.037 47.528 14.438 1.00 17.02 C
ANISOU 1059 CG1 ILE A 161 1865 2139 2464 275 967 -398 C
ATOM 1060 CG2 ILE A 161 11.732 46.994 13.647 1.00 15.99 C
ANISOU 1060 CG2 ILE A 161 1635 2079 2363 316 961 -447 C
ATOM 1061 CD1 ILE A 161 14.775 47.189 13.170 1.00 15.10 C
ANISOU 1061 CD1 ILE A 161 1610 1939 2189 290 954 -376 C
ATOM 1062 N HIS A 162 9.850 46.855 16.443 1.00 21.40 N
ANISOU 1062 N HIS A 162 2321 2711 3097 251 1013 -514 N
ATOM 1063 CA HIS A 162 8.541 46.267 16.685 1.00 26.13 C
ANISOU 1063 CA HIS A 162 2870 3338 3719 235 1032 -554 C
ATOM 1064 C HIS A 162 7.543 46.548 15.568 1.00 26.25 C
ANISOU 1064 C HIS A 162 2801 3404 3769 291 1018 -571 C
ATOM 1065 O HIS A 162 6.398 46.082 15.647 1.00 23.64 O
ANISOU 1065 O HIS A 162 2412 3101 3467 279 1032 -609 O
ATOM 1066 CB HIS A 162 7.976 46.769 18.025 1.00 23.43 C
ANISOU 1066 CB HIS A 162 2541 2966 3396 218 1069 -575 C
ATOM 1067 CG HIS A 162 7.868 48.261 18.116 1.00 35.92 C
ANISOU 1067 CG HIS A 162 4116 4528 5005 277 1072 -571 C
ATOM 1068 ND1 HIS A 162 8.913 49.062 18.521 1.00 40.75 N
ANISOU 1068 ND1 HIS A 162 4789 5089 5606 282 1070 -546 N
ATOM 1069 CD2 HIS A 162 6.834 49.096 17.854 1.00 37.94 C
ANISOU 1069 CD2 HIS A 162 4309 4802 5304 336 1076 -594 C
ATOM 1070 CE1 HIS A 162 8.529 50.326 18.503 1.00 37.48 C
ANISOU 1070 CE1 HIS A 162 4356 4657 5227 339 1076 -553 C
ATOM 1071 NE2 HIS A 162 7.272 50.374 18.103 1.00 40.71 N
ANISOU 1071 NE2 HIS A 162 4690 5108 5669 376 1077 -582 N
ATOM 1072 N SER A 163 7.940 47.274 14.528 1.00 28.08 N
ANISOU 1072 N SER A 163 3020 3646 4002 350 994 -546 N
ATOM 1073 CA SER A 163 7.067 47.591 13.409 1.00 25.34 C
ANISOU 1073 CA SER A 163 2594 3345 3690 415 976 -562 C
ATOM 1074 C SER A 163 7.664 47.032 12.129 1.00 25.91 C
ANISOU 1074 C SER A 163 2662 3451 3731 427 951 -545 C
ATOM 1075 O SER A 163 8.886 47.030 11.954 1.00 26.62 O
ANISOU 1075 O SER A 163 2810 3524 3780 415 948 -510 O
ATOM 1076 CB SER A 163 6.868 49.106 13.273 1.00 23.27 C
ANISOU 1076 CB SER A 163 2318 3058 3467 490 975 -553 C
ATOM 1077 OG SER A 163 6.221 49.425 12.055 1.00 29.12 O
ANISOU 1077 OG SER A 163 2986 3836 4241 564 948 -562 O
ATOM 1078 N CYS A 164 6.796 46.554 11.241 1.00 28.58 N
ANISOU 1078 N CYS A 164 2927 3841 4092 451 934 -576 N
ATOM 1079 CA CYS A 164 7.184 46.049 9.932 1.00 22.07 C
ANISOU 1079 CA CYS A 164 2087 3057 3240 472 910 -573 C
ATOM 1080 C CYS A 164 7.159 47.131 8.860 1.00 23.31 C
ANISOU 1080 C CYS A 164 2209 3228 3417 562 893 -558 C
ATOM 1081 O CYS A 164 7.274 46.818 7.669 1.00 23.10 O
ANISOU 1081 O CYS A 164 2154 3248 3374 593 870 -567 O
ATOM 1082 CB CYS A 164 6.260 44.897 9.534 1.00 29.65 C
ANISOU 1082 CB CYS A 164 2982 4063 4219 444 896 -629 C
ATOM 1083 SG CYS A 164 6.900 43.805 8.270 1.00 38.34 S
ANISOU 1083 SG CYS A 164 4088 5211 5269 437 870 -643 S
ATOM 1084 N LYS A 165 7.019 48.391 9.259 1.00 26.63 N
ANISOU 1084 N LYS A 165 2634 3607 3875 608 901 -540 N
ATOM 1085 CA LYS A 165 6.875 49.486 8.310 1.00 23.66 C
ANISOU 1085 CA LYS A 165 2225 3226 3539 704 884 -525 C
ATOM 1086 C LYS A 165 8.176 49.708 7.548 1.00 21.26 C
ANISOU 1086 C LYS A 165 1999 2911 3167 703 877 -453 C
ATOM 1087 O LYS A 165 9.205 50.041 8.145 1.00 23.54 O
ANISOU 1087 O LYS A 165 2355 3149 3442 669 923 -418 O
ATOM 1088 CB LYS A 165 6.469 50.758 9.047 1.00 26.43 C
ANISOU 1088 CB LYS A 165 2581 3517 3946 748 891 -518 C
ATOM 1089 CG LYS A 165 6.478 52.004 8.182 1.00 30.10 C
ANISOU 1089 CG LYS A 165 3060 3949 4428 840 844 -465 C
ATOM 1090 CD LYS A 165 5.432 51.928 7.078 1.00 40.39 C
ANISOU 1090 CD LYS A 165 4295 5314 5738 905 756 -479 C
ATOM 1091 CE LYS A 165 5.016 53.322 6.641 1.00 44.12 C
ANISOU 1091 CE LYS A 165 4782 5741 6239 1003 692 -435 C
ATOM 1092 NZ LYS A 165 4.026 53.305 5.535 1.00 40.77 N
ANISOU 1092 NZ LYS A 165 4297 5375 5819 1075 592 -445 N
ATOM 1093 N LEU A 166 8.128 49.520 6.236 1.00 20.61 N
ANISOU 1093 N LEU A 166 1917 2883 3032 733 810 -427 N
ATOM 1094 CA LEU A 166 9.237 49.906 5.378 1.00 23.59 C
ANISOU 1094 CA LEU A 166 2374 3259 3331 736 792 -345 C
ATOM 1095 C LEU A 166 9.182 51.408 5.149 1.00 22.80 C
ANISOU 1095 C LEU A 166 2313 3103 3246 796 760 -278 C
ATOM 1096 O LEU A 166 8.234 51.893 4.521 1.00 28.23 O
ANISOU 1096 O LEU A 166 2970 3804 3952 866 692 -275 O
ATOM 1097 CB LEU A 166 9.177 49.167 4.050 1.00 20.02 C
ANISOU 1097 CB LEU A 166 1916 2885 2805 748 734 -343 C
ATOM 1098 CG LEU A 166 9.050 47.647 4.130 1.00 28.69 C
ANISOU 1098 CG LEU A 166 2972 4035 3891 697 748 -417 C
ATOM 1099 CD1 LEU A 166 8.834 47.075 2.741 1.00 25.84 C
ANISOU 1099 CD1 LEU A 166 2606 3750 3461 722 677 -420 C
ATOM 1100 CD2 LEU A 166 10.268 47.019 4.790 1.00 25.00 C
ANISOU 1100 CD2 LEU A 166 2554 3547 3399 629 818 -417 C
ATOM 1101 N PRO A 167 10.154 52.174 5.633 1.00 21.28 N
ANISOU 1101 N PRO A 167 2190 2844 3051 772 801 -224 N
ATOM 1102 CA PRO A 167 10.049 53.635 5.579 1.00 20.67 C
ANISOU 1102 CA PRO A 167 2156 2696 3002 825 774 -166 C
ATOM 1103 C PRO A 167 10.006 54.166 4.154 1.00 22.85 C
ANISOU 1103 C PRO A 167 2472 2994 3217 876 699 -92 C
ATOM 1104 O PRO A 167 10.415 53.506 3.197 1.00 22.86 O
ANISOU 1104 O PRO A 167 2488 3062 3137 858 682 -71 O
ATOM 1105 CB PRO A 167 11.312 54.106 6.307 1.00 22.21 C
ANISOU 1105 CB PRO A 167 2420 2825 3193 767 836 -125 C
ATOM 1106 CG PRO A 167 12.256 52.939 6.220 1.00 22.77 C
ANISOU 1106 CG PRO A 167 2495 2952 3205 696 876 -137 C
ATOM 1107 CD PRO A 167 11.394 51.728 6.289 1.00 19.14 C
ANISOU 1107 CD PRO A 167 1960 2557 2756 696 870 -219 C
ATOM 1108 N ALA A 168 9.511 55.402 4.035 1.00 30.79 N
ANISOU 1108 N ALA A 168 3503 3936 4258 943 653 -52 N
ATOM 1109 CA ALA A 168 9.335 56.018 2.723 1.00 27.99 C
ANISOU 1109 CA ALA A 168 3198 3591 3848 1001 571 23 C
ATOM 1110 C ALA A 168 10.665 56.343 2.058 1.00 25.56 C
ANISOU 1110 C ALA A 168 2990 3272 3450 950 594 120 C
ATOM 1111 O ALA A 168 10.744 56.372 0.824 1.00 34.87 O
ANISOU 1111 O ALA A 168 4211 4494 4545 971 544 177 O
ATOM 1112 CB ALA A 168 8.490 57.285 2.843 1.00 24.29 C
ANISOU 1112 CB ALA A 168 2738 3043 3446 1089 513 41 C
ATOM 1113 N TYR A 169 11.716 56.593 2.844 1.00 22.64 N
ANISOU 1113 N TYR A 169 2658 2849 3094 882 669 140 N
ATOM 1114 CA TYR A 169 13.001 56.936 2.249 1.00 23.67 C
ANISOU 1114 CA TYR A 169 2872 2973 3148 826 697 229 C
ATOM 1115 C TYR A 169 13.631 55.772 1.497 1.00 27.65 C
ANISOU 1115 C TYR A 169 3363 3582 3561 782 720 221 C
ATOM 1116 O TYR A 169 14.666 55.965 0.850 1.00 37.41 O
ANISOU 1116 O TYR A 169 4659 4832 4723 737 747 292 O
ATOM 1117 CB TYR A 169 13.969 57.463 3.318 1.00 26.32 C
ANISOU 1117 CB TYR A 169 3240 3230 3530 761 767 242 C
ATOM 1118 CG TYR A 169 14.355 56.488 4.417 1.00 24.06 C
ANISOU 1118 CG TYR A 169 2897 2966 3278 705 833 159 C
ATOM 1119 CD1 TYR A 169 15.186 55.407 4.162 1.00 24.36 C
ANISOU 1119 CD1 TYR A 169 2918 3081 3256 648 872 144 C
ATOM 1120 CD2 TYR A 169 13.919 56.676 5.720 1.00 21.42 C
ANISOU 1120 CD2 TYR A 169 2535 2573 3031 710 855 98 C
ATOM 1121 CE1 TYR A 169 15.545 54.528 5.163 1.00 23.09 C
ANISOU 1121 CE1 TYR A 169 2716 2932 3124 601 923 73 C
ATOM 1122 CE2 TYR A 169 14.280 55.800 6.729 1.00 21.96 C
ANISOU 1122 CE2 TYR A 169 2566 2658 3121 658 912 29 C
ATOM 1123 CZ TYR A 169 15.093 54.729 6.444 1.00 25.93 C
ANISOU 1123 CZ TYR A 169 3056 3231 3565 604 942 20 C
ATOM 1124 OH TYR A 169 15.455 53.854 7.442 1.00 25.83 O
ANISOU 1124 OH TYR A 169 3016 3228 3572 557 989 -44 O
ATOM 1125 N PHE A 170 13.039 54.576 1.568 1.00 23.55 N
ANISOU 1125 N PHE A 170 2768 3135 3046 790 713 136 N
ATOM 1126 CA PHE A 170 13.507 53.456 0.759 1.00 28.74 C
ANISOU 1126 CA PHE A 170 3415 3889 3615 762 721 120 C
ATOM 1127 C PHE A 170 13.462 53.764 -0.732 1.00 29.60 C
ANISOU 1127 C PHE A 170 3580 4044 3625 798 665 190 C
ATOM 1128 O PHE A 170 14.147 53.094 -1.513 1.00 27.83 O
ANISOU 1128 O PHE A 170 3373 3892 3308 768 685 200 O
ATOM 1129 CB PHE A 170 12.675 52.208 1.057 1.00 34.12 C
ANISOU 1129 CB PHE A 170 4011 4626 4326 771 708 16 C
ATOM 1130 CG PHE A 170 13.211 51.372 2.186 1.00 32.39 C
ANISOU 1130 CG PHE A 170 3758 4400 4147 708 780 -47 C
ATOM 1131 CD1 PHE A 170 14.134 51.891 3.077 1.00 32.92 C
ANISOU 1131 CD1 PHE A 170 3857 4403 4246 661 840 -21 C
ATOM 1132 CD2 PHE A 170 12.804 50.058 2.337 1.00 28.64 C
ANISOU 1132 CD2 PHE A 170 3226 3980 3678 693 780 -131 C
ATOM 1133 CE1 PHE A 170 14.631 51.116 4.108 1.00 31.21 C
ANISOU 1133 CE1 PHE A 170 3618 4180 4062 609 896 -78 C
ATOM 1134 CE2 PHE A 170 13.297 49.279 3.363 1.00 28.32 C
ANISOU 1134 CE2 PHE A 170 3166 3926 3668 638 840 -183 C
ATOM 1135 CZ PHE A 170 14.212 49.807 4.250 1.00 28.26 C
ANISOU 1135 CZ PHE A 170 3193 3857 3688 599 896 -156 C
ATOM 1136 N SER A 171 12.668 54.755 -1.146 1.00 30.30 N
ANISOU 1136 N SER A 171 3698 4089 3724 865 594 237 N
ATOM 1137 CA SER A 171 12.658 55.160 -2.547 1.00 33.95 C
ANISOU 1137 CA SER A 171 4232 4584 4083 900 536 316 C
ATOM 1138 C SER A 171 13.957 55.854 -2.935 1.00 32.47 C
ANISOU 1138 C SER A 171 4139 4370 3827 841 592 419 C
ATOM 1139 O SER A 171 14.330 55.851 -4.113 1.00 33.18 O
ANISOU 1139 O SER A 171 4290 4513 3803 838 579 479 O
ATOM 1140 CB SER A 171 11.460 56.070 -2.820 1.00 38.84 C
ANISOU 1140 CB SER A 171 4864 5155 4739 993 437 340 C
ATOM 1141 OG SER A 171 11.503 57.227 -2.004 1.00 45.90 O
ANISOU 1141 OG SER A 171 5788 5935 5715 1000 451 377 O
ATOM 1142 N ASN A 172 14.653 56.454 -1.966 1.00 33.85 N
ANISOU 1142 N ASN A 172 4328 4466 4069 790 655 438 N
ATOM 1143 CA ASN A 172 15.976 57.005 -2.237 1.00 37.01 C
ANISOU 1143 CA ASN A 172 4800 4846 4415 717 720 524 C
ATOM 1144 C ASN A 172 17.017 55.905 -2.380 1.00 34.81 C
ANISOU 1144 C ASN A 172 4488 4660 4079 649 795 489 C
ATOM 1145 O ASN A 172 18.027 56.092 -3.068 1.00 37.70 O
ANISOU 1145 O ASN A 172 4905 5056 4363 598 841 555 O
ATOM 1146 CB ASN A 172 16.388 57.970 -1.125 1.00 44.05 C
ANISOU 1146 CB ASN A 172 5712 5623 5402 682 757 546 C
ATOM 1147 CG ASN A 172 15.722 59.322 -1.250 1.00 44.42 C
ANISOU 1147 CG ASN A 172 5829 5568 5482 738 691 615 C
ATOM 1148 OD1 ASN A 172 15.170 59.657 -2.295 1.00 49.48 O
ANISOU 1148 OD1 ASN A 172 6520 6221 6059 794 622 669 O
ATOM 1149 ND2 ASN A 172 15.783 60.113 -0.185 1.00 34.83 N
ANISOU 1149 ND2 ASN A 172 4622 4246 4364 727 707 611 N
ATOM 1150 N LEU A 173 16.783 54.757 -1.744 1.00 30.01 N
ANISOU 1150 N LEU A 173 3795 4095 3511 649 808 384 N
ATOM 1151 CA LEU A 173 17.743 53.654 -1.708 1.00 25.56 C
ANISOU 1151 CA LEU A 173 3195 3606 2911 594 874 337 C
ATOM 1152 C LEU A 173 17.437 52.676 -2.844 1.00 30.31 C
ANISOU 1152 C LEU A 173 3787 4315 3415 625 841 307 C
ATOM 1153 O LEU A 173 17.000 51.542 -2.641 1.00 30.48 O
ANISOU 1153 O LEU A 173 3749 4383 3451 640 828 216 O
ATOM 1154 CB LEU A 173 17.701 52.964 -0.350 1.00 22.26 C
ANISOU 1154 CB LEU A 173 2707 3163 2589 574 903 245 C
ATOM 1155 CG LEU A 173 17.770 53.868 0.881 1.00 28.33 C
ANISOU 1155 CG LEU A 173 3481 3825 3458 554 922 256 C
ATOM 1156 CD1 LEU A 173 17.759 53.041 2.157 1.00 27.73 C
ANISOU 1156 CD1 LEU A 173 3345 3738 3455 533 952 164 C
ATOM 1157 CD2 LEU A 173 19.003 54.753 0.827 1.00 27.17 C
ANISOU 1157 CD2 LEU A 173 3388 3640 3294 493 973 337 C
ATOM 1158 N THR A 174 17.691 53.145 -4.068 1.00 30.67 N
ANISOU 1158 N THR A 174 3903 4397 3355 632 829 386 N
ATOM 1159 CA THR A 174 17.306 52.392 -5.258 1.00 33.96 C
ANISOU 1159 CA THR A 174 4327 4910 3666 670 786 365 C
ATOM 1160 C THR A 174 18.081 51.090 -5.414 1.00 38.00 C
ANISOU 1160 C THR A 174 4798 5510 4130 636 842 294 C
ATOM 1161 O THR A 174 17.678 50.237 -6.212 1.00 40.05 O
ANISOU 1161 O THR A 174 5050 5848 4318 670 803 248 O
ATOM 1162 CB THR A 174 17.508 53.246 -6.510 1.00 34.87 C
ANISOU 1162 CB THR A 174 4541 5040 3665 679 769 475 C
ATOM 1163 OG1 THR A 174 18.910 53.391 -6.765 1.00 38.34 O
ANISOU 1163 OG1 THR A 174 5014 5508 4046 605 865 526 O
ATOM 1164 CG2 THR A 174 16.897 54.618 -6.313 1.00 34.70 C
ANISOU 1164 CG2 THR A 174 4573 4915 3695 711 716 554 C
ATOM 1165 N ASN A 175 19.181 50.918 -4.684 1.00 28.69 N
ANISOU 1165 N ASN A 175 3592 4320 2989 575 926 281 N
ATOM 1166 CA ASN A 175 20.009 49.727 -4.803 1.00 27.62 C
ANISOU 1166 CA ASN A 175 3418 4262 2814 549 978 214 C
ATOM 1167 C ASN A 175 19.794 48.732 -3.671 1.00 32.09 C
ANISOU 1167 C ASN A 175 3910 4807 3475 546 978 110 C
ATOM 1168 O ASN A 175 20.405 47.660 -3.684 1.00 30.95 O
ANISOU 1168 O ASN A 175 3734 4717 3308 533 1011 45 O
ATOM 1169 CB ASN A 175 21.488 50.120 -4.866 1.00 25.70 C
ANISOU 1169 CB ASN A 175 3190 4034 2541 483 1071 265 C
ATOM 1170 CG ASN A 175 21.804 51.001 -6.058 1.00 29.89 C
ANISOU 1170 CG ASN A 175 3800 4594 2963 472 1085 370 C
ATOM 1171 OD1 ASN A 175 21.941 50.516 -7.179 1.00 31.26 O
ANISOU 1171 OD1 ASN A 175 3999 4860 3021 487 1090 368 O
ATOM 1172 ND2 ASN A 175 21.923 52.304 -5.822 1.00 29.52 N
ANISOU 1172 ND2 ASN A 175 3801 4467 2950 443 1093 463 N
ATOM 1173 N LEU A 176 18.949 49.056 -2.696 1.00 28.61 N
ANISOU 1173 N LEU A 176 3447 4289 3136 560 943 93 N
ATOM 1174 CA LEU A 176 18.715 48.172 -1.558 1.00 27.80 C
ANISOU 1174 CA LEU A 176 3285 4159 3119 550 948 3 C
ATOM 1175 C LEU A 176 17.947 46.939 -2.019 1.00 29.98 C
ANISOU 1175 C LEU A 176 3530 4493 3366 584 901 -79 C
ATOM 1176 O LEU A 176 16.792 47.044 -2.444 1.00 33.28 O
ANISOU 1176 O LEU A 176 3945 4919 3782 628 833 -85 O
ATOM 1177 CB LEU A 176 17.958 48.920 -0.464 1.00 23.77 C
ANISOU 1177 CB LEU A 176 2762 3555 2714 556 930 9 C
ATOM 1178 CG LEU A 176 17.691 48.186 0.854 1.00 23.22 C
ANISOU 1178 CG LEU A 176 2643 3446 2733 539 943 -72 C
ATOM 1179 CD1 LEU A 176 18.985 47.786 1.543 1.00 20.37 C
ANISOU 1179 CD1 LEU A 176 2278 3077 2385 487 1007 -88 C
ATOM 1180 CD2 LEU A 176 16.844 49.051 1.771 1.00 24.01 C
ANISOU 1180 CD2 LEU A 176 2735 3463 2923 553 927 -64 C
ATOM 1181 N VAL A 177 18.584 45.771 -1.940 1.00 21.42 N
ANISOU 1181 N VAL A 177 2424 3451 2264 565 930 -145 N
ATOM 1182 CA VAL A 177 17.946 44.522 -2.337 1.00 24.80 C
ANISOU 1182 CA VAL A 177 2829 3927 2668 589 887 -229 C
ATOM 1183 C VAL A 177 17.675 43.582 -1.166 1.00 29.25 C
ANISOU 1183 C VAL A 177 3350 4446 3319 568 891 -310 C
ATOM 1184 O VAL A 177 16.859 42.658 -1.319 1.00 28.33 O
ANISOU 1184 O VAL A 177 3210 4348 3206 582 846 -379 O
ATOM 1185 CB VAL A 177 18.765 43.789 -3.422 1.00 28.49 C
ANISOU 1185 CB VAL A 177 3316 4482 3028 596 905 -249 C
ATOM 1186 CG1 VAL A 177 18.667 44.524 -4.752 1.00 30.00 C
ANISOU 1186 CG1 VAL A 177 3557 4728 3115 623 884 -179 C
ATOM 1187 CG2 VAL A 177 20.219 43.635 -2.984 1.00 27.01 C
ANISOU 1187 CG2 VAL A 177 3122 4296 2843 559 984 -247 C
ATOM 1188 N HIS A 178 18.322 43.770 -0.014 1.00 24.19 N
ANISOU 1188 N HIS A 178 2702 3746 2743 532 940 -305 N
ATOM 1189 CA HIS A 178 18.127 42.860 1.109 1.00 19.06 C
ANISOU 1189 CA HIS A 178 2027 3052 2164 509 945 -376 C
ATOM 1190 C HIS A 178 18.024 43.639 2.413 1.00 25.74 C
ANISOU 1190 C HIS A 178 2870 3813 3097 480 967 -351 C
ATOM 1191 O HIS A 178 18.828 44.541 2.677 1.00 27.12 O
ANISOU 1191 O HIS A 178 3064 3962 3280 460 996 -295 O
ATOM 1192 CB HIS A 178 19.260 41.829 1.204 1.00 18.98 C
ANISOU 1192 CB HIS A 178 2044 3015 2154 464 951 -405 C
ATOM 1193 CG HIS A 178 18.931 40.653 2.072 1.00 34.51 C
ANISOU 1193 CG HIS A 178 4022 4918 4173 450 925 -448 C
ATOM 1194 ND1 HIS A 178 19.192 40.630 3.425 1.00 36.69 N
ANISOU 1194 ND1 HIS A 178 4311 5135 4495 438 916 -421 N
ATOM 1195 CD2 HIS A 178 18.343 39.468 1.784 1.00 35.67 C
ANISOU 1195 CD2 HIS A 178 4165 5080 4306 457 884 -509 C
ATOM 1196 CE1 HIS A 178 18.789 39.479 3.932 1.00 29.71 C
ANISOU 1196 CE1 HIS A 178 3436 4223 3631 424 881 -468 C
ATOM 1197 NE2 HIS A 178 18.270 38.755 2.957 1.00 35.55 N
ANISOU 1197 NE2 HIS A 178 4167 4999 4343 433 868 -521 N
ATOM 1198 N VAL A 179 17.021 43.289 3.216 1.00 22.89 N
ANISOU 1198 N VAL A 179 2486 3411 2801 473 950 -397 N
ATOM 1199 CA VAL A 179 16.848 43.819 4.562 1.00 18.88 C
ANISOU 1199 CA VAL A 179 1982 2833 2357 445 939 -379 C
ATOM 1200 C VAL A 179 16.667 42.636 5.505 1.00 15.88 C
ANISOU 1200 C VAL A 179 1617 2420 1998 415 903 -412 C
ATOM 1201 O VAL A 179 15.783 41.798 5.288 1.00 19.31 O
ANISOU 1201 O VAL A 179 2035 2859 2442 419 889 -455 O
ATOM 1202 CB VAL A 179 15.652 44.780 4.655 1.00 22.42 C
ANISOU 1202 CB VAL A 179 2403 3253 2861 477 955 -369 C
ATOM 1203 CG1 VAL A 179 15.418 45.177 6.097 1.00 23.09 C
ANISOU 1203 CG1 VAL A 179 2498 3269 3008 443 943 -367 C
ATOM 1204 CG2 VAL A 179 15.893 46.009 3.787 1.00 19.47 C
ANISOU 1204 CG2 VAL A 179 2054 2890 2452 508 944 -289 C
ATOM 1205 N ASP A 180 17.509 42.557 6.535 1.00 15.58 N
ANISOU 1205 N ASP A 180 1609 2339 1972 378 893 -398 N
ATOM 1206 CA ASP A 180 17.432 41.495 7.533 1.00 15.02 C
ANISOU 1206 CA ASP A 180 1563 2223 1920 346 869 -425 C
ATOM 1207 C ASP A 180 16.735 42.053 8.767 1.00 17.76 C
ANISOU 1207 C ASP A 180 1915 2514 2321 318 873 -423 C
ATOM 1208 O ASP A 180 17.300 42.882 9.486 1.00 18.86 O
ANISOU 1208 O ASP A 180 2072 2618 2477 302 881 -396 O
ATOM 1209 CB ASP A 180 18.819 40.960 7.883 1.00 16.33 C
ANISOU 1209 CB ASP A 180 1760 2379 2064 332 858 -420 C
ATOM 1210 CG ASP A 180 18.765 39.676 8.696 1.00 25.34 C
ANISOU 1210 CG ASP A 180 2931 3477 3219 306 839 -456 C
ATOM 1211 OD1 ASP A 180 17.667 39.304 9.161 1.00 23.30 O
ANISOU 1211 OD1 ASP A 180 2671 3192 2990 284 840 -482 O
ATOM 1212 OD2 ASP A 180 19.821 39.031 8.862 1.00 25.08 O
ANISOU 1212 OD2 ASP A 180 2921 3439 3170 306 828 -463 O
ATOM 1213 N LEU A 181 15.505 41.604 9.007 1.00 17.84 N
ANISOU 1213 N LEU A 181 1906 2513 2359 309 871 -455 N
ATOM 1214 CA LEU A 181 14.759 41.971 10.204 1.00 16.18 C
ANISOU 1214 CA LEU A 181 1698 2254 2194 281 880 -459 C
ATOM 1215 C LEU A 181 14.708 40.847 11.229 1.00 23.75 C
ANISOU 1215 C LEU A 181 2689 3171 3162 231 879 -487 C
ATOM 1216 O LEU A 181 13.866 40.891 12.131 1.00 21.34 O
ANISOU 1216 O LEU A 181 2382 2836 2891 202 894 -502 O
ATOM 1217 CB LEU A 181 13.338 42.402 9.834 1.00 15.45 C
ANISOU 1217 CB LEU A 181 1551 2184 2137 304 889 -479 C
ATOM 1218 CG LEU A 181 13.204 43.708 9.047 1.00 21.28 C
ANISOU 1218 CG LEU A 181 2257 2946 2882 358 899 -454 C
ATOM 1219 CD1 LEU A 181 11.784 43.922 8.554 1.00 26.76 C
ANISOU 1219 CD1 LEU A 181 2884 3667 3615 392 899 -485 C
ATOM 1220 CD2 LEU A 181 13.647 44.891 9.888 1.00 22.84 C
ANISOU 1220 CD2 LEU A 181 2483 3095 3101 352 913 -420 C
ATOM 1221 N SER A 182 15.582 39.846 11.115 1.00 21.18 N
ANISOU 1221 N SER A 182 2395 2844 2808 221 865 -498 N
ATOM 1222 CA SER A 182 15.492 38.670 11.971 1.00 18.35 C
ANISOU 1222 CA SER A 182 2070 2442 2459 176 869 -531 C
ATOM 1223 C SER A 182 15.647 39.050 13.436 1.00 14.23 C
ANISOU 1223 C SER A 182 1587 1863 1958 141 885 -517 C
ATOM 1224 O SER A 182 16.298 40.041 13.775 1.00 17.55 O
ANISOU 1224 O SER A 182 2018 2273 2376 153 883 -484 O
ATOM 1225 CB SER A 182 16.558 37.637 11.595 1.00 15.60 C
ANISOU 1225 CB SER A 182 1752 2097 2078 185 851 -546 C
ATOM 1226 OG SER A 182 16.620 37.444 10.192 1.00 43.22 O
ANISOU 1226 OG SER A 182 5222 5653 5548 224 838 -555 O
ATOM 1227 N TYR A 183 15.012 38.261 14.304 1.00 14.37 N
ANISOU 1227 N TYR A 183 1626 1842 1994 93 907 -547 N
ATOM 1228 CA TYR A 183 15.210 38.350 15.750 1.00 15.03 C
ANISOU 1228 CA TYR A 183 1758 1867 2085 55 928 -541 C
ATOM 1229 C TYR A 183 14.896 39.752 16.279 1.00 14.26 C
ANISOU 1229 C TYR A 183 1649 1764 2006 64 939 -515 C
ATOM 1230 O TYR A 183 15.687 40.360 17.003 1.00 19.49 O
ANISOU 1230 O TYR A 183 2346 2395 2663 64 938 -494 O
ATOM 1231 CB TYR A 183 16.636 37.926 16.114 1.00 15.33 C
ANISOU 1231 CB TYR A 183 1849 1878 2098 60 911 -533 C
ATOM 1232 CG TYR A 183 16.870 37.618 17.576 1.00 25.36 C
ANISOU 1232 CG TYR A 183 3184 3084 3368 18 935 -539 C
ATOM 1233 CD1 TYR A 183 15.820 37.607 18.489 1.00 35.51 C
ANISOU 1233 CD1 TYR A 183 4482 4339 4671 -28 976 -551 C
ATOM 1234 CD2 TYR A 183 18.151 37.348 18.046 1.00 30.19 C
ANISOU 1234 CD2 TYR A 183 3843 3668 3961 27 920 -534 C
ATOM 1235 CE1 TYR A 183 16.038 37.333 19.826 1.00 37.63 C
ANISOU 1235 CE1 TYR A 183 4819 4550 4929 -66 1004 -554 C
ATOM 1236 CE2 TYR A 183 18.379 37.072 19.378 1.00 32.10 C
ANISOU 1236 CE2 TYR A 183 4153 3850 4195 -6 942 -540 C
ATOM 1237 CZ TYR A 183 17.321 37.064 20.263 1.00 37.09 C
ANISOU 1237 CZ TYR A 183 4807 4452 4835 -54 986 -547 C
ATOM 1238 OH TYR A 183 17.554 36.789 21.591 1.00 45.39 O
ANISOU 1238 OH TYR A 183 5935 5443 5866 -89 1012 -551 O
ATOM 1239 N ASN A 184 13.729 40.273 15.901 1.00 18.06 N
ANISOU 1239 N ASN A 184 2077 2273 2511 75 950 -522 N
ATOM 1240 CA ASN A 184 13.231 41.516 16.482 1.00 18.61 C
ANISOU 1240 CA ASN A 184 2135 2332 2603 85 965 -509 C
ATOM 1241 C ASN A 184 11.900 41.253 17.173 1.00 21.15 C
ANISOU 1241 C ASN A 184 2437 2646 2954 50 1002 -542 C
ATOM 1242 O ASN A 184 11.607 40.108 17.530 1.00 26.51 O
ANISOU 1242 O ASN A 184 3132 3309 3632 2 1022 -570 O
ATOM 1243 CB ASN A 184 13.093 42.611 15.419 1.00 16.76 C
ANISOU 1243 CB ASN A 184 1852 2138 2376 142 949 -489 C
ATOM 1244 CG ASN A 184 14.409 43.299 15.116 1.00 20.33 C
ANISOU 1244 CG ASN A 184 2330 2586 2808 166 932 -453 C
ATOM 1245 OD1 ASN A 184 14.838 44.189 15.852 1.00 19.66 O
ANISOU 1245 OD1 ASN A 184 2272 2463 2733 163 943 -437 O
ATOM 1246 ND2 ASN A 184 15.057 42.888 14.037 1.00 16.39 N
ANISOU 1246 ND2 ASN A 184 1821 2124 2282 187 911 -444 N
ATOM 1247 N TYR A 185 11.082 42.288 17.357 1.00 18.90 N
ANISOU 1247 N TYR A 185 2116 2370 2696 72 1016 -543 N
ATOM 1248 CA TYR A 185 9.847 42.171 18.123 1.00 16.85 C
ANISOU 1248 CA TYR A 185 1832 2106 2464 40 1056 -576 C
ATOM 1249 C TYR A 185 8.616 42.441 17.265 1.00 25.48 C
ANISOU 1249 C TYR A 185 2837 3251 3594 71 1056 -600 C
ATOM 1250 O TYR A 185 7.580 42.873 17.771 1.00 25.05 O
ANISOU 1250 O TYR A 185 2744 3203 3571 70 1085 -623 O
ATOM 1251 CB TYR A 185 9.877 43.104 19.334 1.00 16.25 C
ANISOU 1251 CB TYR A 185 1790 1993 2392 37 1081 -569 C
ATOM 1252 CG TYR A 185 10.925 42.728 20.361 1.00 25.12 C
ANISOU 1252 CG TYR A 185 2998 3063 3483 -2 1090 -556 C
ATOM 1253 CD1 TYR A 185 12.257 43.069 20.176 1.00 25.75 C
ANISOU 1253 CD1 TYR A 185 3116 3125 3541 19 1057 -525 C
ATOM 1254 CD2 TYR A 185 10.582 42.028 21.510 1.00 24.53 C
ANISOU 1254 CD2 TYR A 185 2964 2956 3401 -60 1134 -578 C
ATOM 1255 CE1 TYR A 185 13.221 42.724 21.106 1.00 20.17 C
ANISOU 1255 CE1 TYR A 185 2482 2373 2809 -11 1063 -518 C
ATOM 1256 CE2 TYR A 185 11.541 41.678 22.446 1.00 27.11 C
ANISOU 1256 CE2 TYR A 185 3373 3233 3695 -91 1142 -567 C
ATOM 1257 CZ TYR A 185 12.859 42.028 22.238 1.00 27.36 C
ANISOU 1257 CZ TYR A 185 3437 3250 3709 -63 1103 -538 C
ATOM 1258 OH TYR A 185 13.813 41.683 23.167 1.00 36.87 O
ANISOU 1258 OH TYR A 185 4720 4408 4883 -89 1110 -532 O
ATOM 1259 N ILE A 186 8.709 42.174 15.964 1.00 16.71 N
ANISOU 1259 N ILE A 186 1690 2180 2480 102 1024 -598 N
ATOM 1260 CA ILE A 186 7.580 42.405 15.069 1.00 20.83 C
ANISOU 1260 CA ILE A 186 2124 2753 3038 137 1018 -624 C
ATOM 1261 C ILE A 186 6.509 41.356 15.338 1.00 24.18 C
ANISOU 1261 C ILE A 186 2505 3189 3493 79 1048 -678 C
ATOM 1262 O ILE A 186 6.745 40.151 15.190 1.00 28.02 O
ANISOU 1262 O ILE A 186 3011 3669 3967 32 1050 -697 O
ATOM 1263 CB ILE A 186 8.025 42.384 13.601 1.00 24.73 C
ANISOU 1263 CB ILE A 186 2595 3286 3514 186 979 -612 C
ATOM 1264 CG1 ILE A 186 9.021 43.513 13.328 1.00 25.54 C
ANISOU 1264 CG1 ILE A 186 2733 3379 3592 237 962 -562 C
ATOM 1265 CG2 ILE A 186 6.819 42.503 12.671 1.00 17.82 C
ANISOU 1265 CG2 ILE A 186 1624 2466 2682 221 969 -648 C
ATOM 1266 CD1 ILE A 186 9.588 43.496 11.930 1.00 16.60 C
ANISOU 1266 CD1 ILE A 186 1589 2286 2434 281 934 -547 C
ATOM 1267 N GLN A 187 5.322 41.817 15.741 1.00 21.49 N
ANISOU 1267 N GLN A 187 2105 2865 3197 81 1073 -706 N
ATOM 1268 CA GLN A 187 4.169 40.960 15.972 1.00 24.07 C
ANISOU 1268 CA GLN A 187 2372 3209 3562 23 1107 -762 C
ATOM 1269 C GLN A 187 3.083 41.105 14.916 1.00 24.91 C
ANISOU 1269 C GLN A 187 2366 3379 3720 60 1085 -801 C
ATOM 1270 O GLN A 187 2.232 40.217 14.805 1.00 26.51 O
ANISOU 1270 O GLN A 187 2510 3606 3959 8 1101 -855 O
ATOM 1271 CB GLN A 187 3.552 41.255 17.351 1.00 22.56 C
ANISOU 1271 CB GLN A 187 2190 2995 3386 -13 1162 -775 C
ATOM 1272 CG GLN A 187 4.526 41.180 18.525 1.00 34.04 C
ANISOU 1272 CG GLN A 187 3752 4387 4794 -49 1185 -744 C
ATOM 1273 CD GLN A 187 3.868 41.494 19.864 1.00 36.08 C
ANISOU 1273 CD GLN A 187 4017 4627 5062 -81 1243 -762 C
ATOM 1274 OE1 GLN A 187 3.029 40.733 20.353 1.00 41.60 O
ANISOU 1274 OE1 GLN A 187 4692 5332 5782 -146 1292 -802 O
ATOM 1275 NE2 GLN A 187 4.250 42.617 20.462 1.00 40.99 N
ANISOU 1275 NE2 GLN A 187 4674 5229 5670 -40 1241 -737 N
ATOM 1276 N THR A 188 3.094 42.188 14.142 1.00 23.48 N
ANISOU 1276 N THR A 188 2152 3223 3547 147 1047 -779 N
ATOM 1277 CA THR A 188 2.025 42.506 13.208 1.00 31.33 C
ANISOU 1277 CA THR A 188 3034 4275 4595 196 1019 -817 C
ATOM 1278 C THR A 188 2.612 42.922 11.867 1.00 27.87 C
ANISOU 1278 C THR A 188 2590 3862 4138 270 964 -793 C
ATOM 1279 O THR A 188 3.691 43.516 11.800 1.00 24.58 O
ANISOU 1279 O THR A 188 2247 3417 3677 304 956 -738 O
ATOM 1280 CB THR A 188 1.127 43.629 13.765 1.00 36.71 C
ANISOU 1280 CB THR A 188 3664 4962 5321 240 1035 -826 C
ATOM 1281 OG1 THR A 188 0.599 43.229 15.036 1.00 39.98 O
ANISOU 1281 OG1 THR A 188 4086 5358 5746 169 1094 -851 O
ATOM 1282 CG2 THR A 188 -0.032 43.937 12.831 1.00 42.31 C
ANISOU 1282 CG2 THR A 188 4249 5732 6095 296 998 -870 C
ATOM 1283 N ILE A 189 1.898 42.579 10.798 1.00 27.16 N
ANISOU 1283 N ILE A 189 2409 3828 4081 292 926 -839 N
ATOM 1284 CA ILE A 189 2.163 43.090 9.458 1.00 24.57 C
ANISOU 1284 CA ILE A 189 2054 3538 3746 375 870 -829 C
ATOM 1285 C ILE A 189 0.856 43.662 8.931 1.00 24.93 C
ANISOU 1285 C ILE A 189 1978 3633 3862 436 830 -873 C
ATOM 1286 O ILE A 189 -0.119 42.923 8.751 1.00 24.18 O
ANISOU 1286 O ILE A 189 1796 3582 3810 400 816 -939 O
ATOM 1287 CB ILE A 189 2.699 42.003 8.511 1.00 30.97 C
ANISOU 1287 CB ILE A 189 2872 4378 4516 353 842 -853 C
ATOM 1288 CG1 ILE A 189 3.945 41.346 9.103 1.00 27.63 C
ANISOU 1288 CG1 ILE A 189 2565 3903 4030 294 877 -814 C
ATOM 1289 CG2 ILE A 189 3.010 42.599 7.144 1.00 24.06 C
ANISOU 1289 CG2 ILE A 189 1974 3549 3621 444 785 -844 C
ATOM 1290 CD1 ILE A 189 4.447 40.172 8.299 1.00 22.66 C
ANISOU 1290 CD1 ILE A 189 1948 3298 3363 268 857 -847 C
ATOM 1291 N THR A 190 0.830 44.968 8.694 1.00 24.33 N
ANISOU 1291 N THR A 190 1893 3549 3801 527 808 -842 N
ATOM 1292 CA THR A 190 -0.376 45.655 8.258 1.00 28.86 C
ANISOU 1292 CA THR A 190 2358 4162 4446 600 761 -879 C
ATOM 1293 C THR A 190 -0.292 45.984 6.775 1.00 30.92 C
ANISOU 1293 C THR A 190 2577 4470 4701 693 674 -884 C
ATOM 1294 O THR A 190 0.762 45.868 6.142 1.00 28.02 O
ANISOU 1294 O THR A 190 2272 4103 4271 706 664 -853 O
ATOM 1295 CB THR A 190 -0.599 46.941 9.060 1.00 29.46 C
ANISOU 1295 CB THR A 190 2449 4194 4552 651 787 -850 C
ATOM 1296 OG1 THR A 190 0.424 47.891 8.730 1.00 29.94 O
ANISOU 1296 OG1 THR A 190 2585 4213 4578 716 778 -790 O
ATOM 1297 CG2 THR A 190 -0.563 46.659 10.548 1.00 23.62 C
ANISOU 1297 CG2 THR A 190 1762 3415 3799 566 866 -846 C
ATOM 1298 N VAL A 191 -1.439 46.396 6.228 1.00 27.44 N
ANISOU 1298 N VAL A 191 2028 4076 4323 761 606 -926 N
ATOM 1299 CA VAL A 191 -1.493 46.850 4.840 1.00 29.56 C
ANISOU 1299 CA VAL A 191 2255 4394 4582 871 500 -930 C
ATOM 1300 C VAL A 191 -0.542 48.021 4.641 1.00 30.80 C
ANISOU 1300 C VAL A 191 2500 4501 4702 951 496 -856 C
ATOM 1301 O VAL A 191 0.231 48.067 3.677 1.00 27.02 O
ANISOU 1301 O VAL A 191 2112 4024 4131 969 441 -788 O
ATOM 1302 CB VAL A 191 -2.935 47.235 4.457 1.00 32.98 C
ANISOU 1302 CB VAL A 191 2564 4873 5094 938 418 -981 C
ATOM 1303 CG1 VAL A 191 -2.978 47.826 3.056 1.00 30.13 C
ANISOU 1303 CG1 VAL A 191 2184 4555 4708 1065 287 -967 C
ATOM 1304 CG2 VAL A 191 -3.867 46.043 4.571 1.00 28.80 C
ANISOU 1304 CG2 VAL A 191 1943 4397 4603 851 419 -1059 C
ATOM 1305 N ASN A 192 -0.580 48.982 5.568 1.00 28.82 N
ANISOU 1305 N ASN A 192 2277 4182 4491 968 547 -827 N
ATOM 1306 CA ASN A 192 0.228 50.188 5.430 1.00 35.35 C
ANISOU 1306 CA ASN A 192 3189 4948 5295 1042 539 -756 C
ATOM 1307 C ASN A 192 1.712 49.900 5.611 1.00 36.95 C
ANISOU 1307 C ASN A 192 3520 5110 5411 969 599 -691 C
ATOM 1308 O ASN A 192 2.551 50.634 5.074 1.00 37.26 O
ANISOU 1308 O ASN A 192 3657 5110 5388 1002 570 -605 O
ATOM 1309 CB ASN A 192 -0.234 51.243 6.435 1.00 41.89 C
ANISOU 1309 CB ASN A 192 4012 5713 6193 1076 578 -755 C
ATOM 1310 CG ASN A 192 0.595 52.508 6.369 1.00 46.59 C
ANISOU 1310 CG ASN A 192 4699 6230 6774 1145 571 -686 C
ATOM 1311 OD1 ASN A 192 0.559 53.235 5.377 1.00 49.01 O
ANISOU 1311 OD1 ASN A 192 5041 6526 7054 1226 475 -629 O
ATOM 1312 ND2 ASN A 192 1.344 52.782 7.431 1.00 45.01 N
ANISOU 1312 ND2 ASN A 192 4569 5963 6569 1095 663 -666 N
ATOM 1313 N ASP A 193 2.059 48.843 6.353 1.00 33.91 N
ANISOU 1313 N ASP A 193 3139 4731 5015 869 680 -725 N
ATOM 1314 CA ASP A 193 3.466 48.523 6.575 1.00 23.37 C
ANISOU 1314 CA ASP A 193 1911 3361 3608 807 735 -676 C
ATOM 1315 C ASP A 193 4.189 48.264 5.262 1.00 24.47 C
ANISOU 1315 C ASP A 193 2114 3532 3650 817 668 -619 C
ATOM 1316 O ASP A 193 5.372 48.593 5.118 1.00 23.14 O
ANISOU 1316 O ASP A 193 2044 3330 3420 806 687 -549 O
ATOM 1317 CB ASP A 193 3.594 47.304 7.487 1.00 27.19 C
ANISOU 1317 CB ASP A 193 2426 3839 4066 689 789 -691 C
ATOM 1318 CG ASP A 193 3.423 47.649 8.949 1.00 38.39 C
ANISOU 1318 CG ASP A 193 3882 5203 5502 647 841 -679 C
ATOM 1319 OD1 ASP A 193 3.430 48.850 9.285 1.00 33.84 O
ANISOU 1319 OD1 ASP A 193 3321 4587 4951 703 847 -656 O
ATOM 1320 OD2 ASP A 193 3.278 46.715 9.764 1.00 36.76 O
ANISOU 1320 OD2 ASP A 193 3691 4995 5283 561 873 -697 O
ATOM 1321 N LEU A 194 3.491 47.674 4.294 1.00 25.20 N
ANISOU 1321 N LEU A 194 2151 3694 3730 837 592 -652 N
ATOM 1322 CA LEU A 194 4.060 47.334 3.000 1.00 24.37 C
ANISOU 1322 CA LEU A 194 2103 3631 3527 848 528 -611 C
ATOM 1323 C LEU A 194 3.698 48.348 1.927 1.00 26.89 C
ANISOU 1323 C LEU A 194 2435 3960 3820 945 429 -558 C
ATOM 1324 O LEU A 194 3.874 48.067 0.736 1.00 28.98 O
ANISOU 1324 O LEU A 194 2734 4274 4003 964 361 -534 O
ATOM 1325 CB LEU A 194 3.601 45.936 2.586 1.00 25.17 C
ANISOU 1325 CB LEU A 194 2150 3799 3616 802 502 -684 C
ATOM 1326 CG LEU A 194 3.897 44.882 3.655 1.00 26.82 C
ANISOU 1326 CG LEU A 194 2352 3988 3849 705 594 -734 C
ATOM 1327 CD1 LEU A 194 3.433 43.493 3.237 1.00 30.62 C
ANISOU 1327 CD1 LEU A 194 2787 4524 4323 655 564 -807 C
ATOM 1328 CD2 LEU A 194 5.382 44.887 3.989 1.00 26.48 C
ANISOU 1328 CD2 LEU A 194 2418 3900 3743 668 657 -676 C
ATOM 1329 N GLN A 195 3.196 49.520 2.329 1.00 26.23 N
ANISOU 1329 N GLN A 195 2334 3830 3802 1008 419 -540 N
ATOM 1330 CA GLN A 195 2.810 50.545 1.365 1.00 28.63 C
ANISOU 1330 CA GLN A 195 2660 4132 4089 1107 318 -487 C
ATOM 1331 C GLN A 195 3.920 50.815 0.357 1.00 31.07 C
ANISOU 1331 C GLN A 195 3092 4436 4275 1109 293 -389 C
ATOM 1332 O GLN A 195 3.667 50.857 -0.850 1.00 30.11 O
ANISOU 1332 O GLN A 195 2991 4361 4090 1159 199 -363 O
ATOM 1333 CB GLN A 195 2.430 51.828 2.100 1.00 37.24 C
ANISOU 1333 CB GLN A 195 3741 5147 5262 1168 329 -471 C
ATOM 1334 CG GLN A 195 1.878 52.920 1.205 1.00 52.17 C
ANISOU 1334 CG GLN A 195 5649 7023 7149 1281 216 -422 C
ATOM 1335 CD GLN A 195 1.591 54.184 1.977 1.00 69.99 C
ANISOU 1335 CD GLN A 195 7909 9194 9490 1343 230 -410 C
ATOM 1336 OE1 GLN A 195 2.241 54.466 2.982 1.00 75.54 O
ANISOU 1336 OE1 GLN A 195 8651 9834 10215 1296 324 -400 O
ATOM 1337 NE2 GLN A 195 0.613 54.951 1.520 1.00 71.86 N
ANISOU 1337 NE2 GLN A 195 8104 9425 9773 1452 131 -415 N
ATOM 1338 N PHE A 196 5.160 50.973 0.833 1.00 27.68 N
ANISOU 1338 N PHE A 196 2748 3960 3811 1053 377 -336 N
ATOM 1339 CA PHE A 196 6.262 51.328 -0.059 1.00 26.75 C
ANISOU 1339 CA PHE A 196 2743 3838 3583 1048 369 -241 C
ATOM 1340 C PHE A 196 6.408 50.337 -1.208 1.00 27.82 C
ANISOU 1340 C PHE A 196 2890 4062 3620 1035 324 -253 C
ATOM 1341 O PHE A 196 6.650 50.736 -2.353 1.00 28.04 O
ANISOU 1341 O PHE A 196 2986 4112 3557 1073 265 -186 O
ATOM 1342 CB PHE A 196 7.577 51.414 0.714 1.00 26.40 C
ANISOU 1342 CB PHE A 196 2763 3743 3525 975 472 -204 C
ATOM 1343 CG PHE A 196 8.794 51.298 -0.165 1.00 28.05 C
ANISOU 1343 CG PHE A 196 3062 3976 3618 943 485 -133 C
ATOM 1344 CD1 PHE A 196 9.183 52.354 -0.974 1.00 28.31 C
ANISOU 1344 CD1 PHE A 196 3181 3984 3591 979 450 -34 C
ATOM 1345 CD2 PHE A 196 9.540 50.131 -0.191 1.00 26.92 C
ANISOU 1345 CD2 PHE A 196 2920 3883 3426 877 534 -166 C
ATOM 1346 CE1 PHE A 196 10.298 52.250 -1.789 1.00 30.18 C
ANISOU 1346 CE1 PHE A 196 3497 4253 3719 943 473 30 C
ATOM 1347 CE2 PHE A 196 10.656 50.021 -1.005 1.00 32.22 C
ANISOU 1347 CE2 PHE A 196 3665 4586 3993 852 553 -109 C
ATOM 1348 CZ PHE A 196 11.035 51.082 -1.804 1.00 32.51 C
ANISOU 1348 CZ PHE A 196 3781 4605 3968 881 527 -12 C
ATOM 1349 N LEU A 197 6.287 49.039 -0.922 1.00 30.32 N
ANISOU 1349 N LEU A 197 3147 4425 3948 980 353 -335 N
ATOM 1350 CA LEU A 197 6.442 48.040 -1.974 1.00 30.53 C
ANISOU 1350 CA LEU A 197 3186 4531 3883 967 312 -357 C
ATOM 1351 C LEU A 197 5.232 48.017 -2.897 1.00 32.16 C
ANISOU 1351 C LEU A 197 3342 4792 4086 1035 193 -389 C
ATOM 1352 O LEU A 197 5.373 47.801 -4.107 1.00 26.71 O
ANISOU 1352 O LEU A 197 2698 4157 3294 1060 129 -367 O
ATOM 1353 CB LEU A 197 6.679 46.661 -1.361 1.00 26.62 C
ANISOU 1353 CB LEU A 197 2652 4056 3406 888 373 -437 C
ATOM 1354 CG LEU A 197 8.139 46.411 -0.984 1.00 31.02 C
ANISOU 1354 CG LEU A 197 3282 4589 3916 827 465 -402 C
ATOM 1355 CD1 LEU A 197 8.305 45.038 -0.382 1.00 32.73 C
ANISOU 1355 CD1 LEU A 197 3466 4817 4153 759 512 -482 C
ATOM 1356 CD2 LEU A 197 9.019 46.566 -2.213 1.00 30.30 C
ANISOU 1356 CD2 LEU A 197 3275 4537 3698 844 444 -336 C
ATOM 1357 N ARG A 198 4.040 48.239 -2.337 1.00 33.96 N
ANISOU 1357 N ARG A 198 3471 5009 4424 1068 162 -444 N
ATOM 1358 CA ARG A 198 2.841 48.372 -3.156 1.00 31.06 C
ANISOU 1358 CA ARG A 198 3044 4690 4069 1143 39 -474 C
ATOM 1359 C ARG A 198 2.981 49.528 -4.139 1.00 36.05 C
ANISOU 1359 C ARG A 198 3764 5306 4627 1228 -41 -376 C
ATOM 1360 O ARG A 198 2.603 49.408 -5.310 1.00 40.31 O
ANISOU 1360 O ARG A 198 4320 5903 5094 1276 -145 -371 O
ATOM 1361 CB ARG A 198 1.622 48.568 -2.251 1.00 33.33 C
ANISOU 1361 CB ARG A 198 3203 4962 4499 1166 35 -548 C
ATOM 1362 CG ARG A 198 0.272 48.460 -2.948 1.00 28.36 C
ANISOU 1362 CG ARG A 198 2476 4393 3906 1232 -89 -608 C
ATOM 1363 CD ARG A 198 -0.886 48.458 -1.947 1.00 28.67 C
ANISOU 1363 CD ARG A 198 2369 4430 4094 1236 -70 -697 C
ATOM 1364 NE ARG A 198 -0.914 47.259 -1.108 1.00 34.39 N
ANISOU 1364 NE ARG A 198 3030 5172 4864 1129 21 -778 N
ATOM 1365 CZ ARG A 198 -0.565 47.235 0.176 1.00 35.67 C
ANISOU 1365 CZ ARG A 198 3189 5282 5082 1069 143 -788 C
ATOM 1366 NH1 ARG A 198 -0.162 48.346 0.777 1.00 32.92 N
ANISOU 1366 NH1 ARG A 198 2891 4864 4755 1104 189 -729 N
ATOM 1367 NH2 ARG A 198 -0.624 46.102 0.864 1.00 34.67 N
ANISOU 1367 NH2 ARG A 198 3015 5170 4987 972 216 -856 N
ATOM 1368 N GLU A 199 3.539 50.653 -3.682 1.00 39.41 N
ANISOU 1368 N GLU A 199 4256 5652 5066 1243 5 -296 N
ATOM 1369 CA GLU A 199 3.720 51.802 -4.564 1.00 46.93 C
ANISOU 1369 CA GLU A 199 5307 6575 5948 1316 -66 -193 C
ATOM 1370 C GLU A 199 4.764 51.515 -5.635 1.00 42.24 C
ANISOU 1370 C GLU A 199 4827 6022 5201 1285 -62 -125 C
ATOM 1371 O GLU A 199 4.635 51.977 -6.775 1.00 47.37 O
ANISOU 1371 O GLU A 199 5546 6692 5760 1344 -152 -65 O
ATOM 1372 CB GLU A 199 4.128 53.037 -3.756 1.00 55.24 C
ANISOU 1372 CB GLU A 199 6409 7523 7057 1327 -11 -127 C
ATOM 1373 CG GLU A 199 3.307 53.307 -2.510 1.00 58.45 C
ANISOU 1373 CG GLU A 199 6712 7885 7612 1346 17 -197 C
ATOM 1374 CD GLU A 199 2.179 54.285 -2.739 1.00 64.08 C
ANISOU 1374 CD GLU A 199 7389 8570 8390 1461 -89 -195 C
ATOM 1375 OE1 GLU A 199 1.935 54.654 -3.907 1.00 68.04 O
ANISOU 1375 OE1 GLU A 199 7942 9092 8819 1530 -199 -144 O
ATOM 1376 OE2 GLU A 199 1.541 54.690 -1.744 1.00 66.44 O
ANISOU 1376 OE2 GLU A 199 7610 8827 8808 1488 -63 -247 O
ATOM 1377 N ASN A 200 5.800 50.748 -5.289 1.00 39.74 N
ANISOU 1377 N ASN A 200 4532 5719 4849 1195 42 -136 N
ATOM 1378 CA ASN A 200 6.984 50.567 -6.125 1.00 40.69 C
ANISOU 1378 CA ASN A 200 4758 5872 4831 1158 75 -71 C
ATOM 1379 C ASN A 200 7.116 49.096 -6.500 1.00 43.69 C
ANISOU 1379 C ASN A 200 5105 6336 5159 1114 83 -152 C
ATOM 1380 O ASN A 200 7.933 48.367 -5.915 1.00 39.01 O
ANISOU 1380 O ASN A 200 4506 5744 4571 1041 177 -182 O
ATOM 1381 CB ASN A 200 8.235 51.060 -5.401 1.00 35.66 C
ANISOU 1381 CB ASN A 200 4180 5171 4200 1096 191 -9 C
ATOM 1382 CG ASN A 200 8.130 52.511 -4.982 1.00 36.35 C
ANISOU 1382 CG ASN A 200 4306 5162 4343 1135 184 67 C
ATOM 1383 OD1 ASN A 200 8.643 53.399 -5.657 1.00 36.95 O
ANISOU 1383 OD1 ASN A 200 4484 5212 4344 1151 169 169 O
ATOM 1384 ND2 ASN A 200 7.462 52.759 -3.860 1.00 30.02 N
ANISOU 1384 ND2 ASN A 200 3428 4307 3672 1148 196 16 N
ATOM 1385 N PRO A 201 6.338 48.622 -7.479 1.00 47.87 N
ANISOU 1385 N PRO A 201 5616 6935 5637 1158 -21 -192 N
ATOM 1386 CA PRO A 201 6.449 47.214 -7.890 1.00 44.65 C
ANISOU 1386 CA PRO A 201 5184 6602 5177 1118 -21 -274 C
ATOM 1387 C PRO A 201 7.748 46.880 -8.607 1.00 43.17 C
ANISOU 1387 C PRO A 201 5097 6453 4852 1082 36 -230 C
ATOM 1388 O PRO A 201 8.049 45.692 -8.779 1.00 46.61 O
ANISOU 1388 O PRO A 201 5518 6939 5251 1042 57 -301 O
ATOM 1389 CB PRO A 201 5.243 47.026 -8.817 1.00 40.60 C
ANISOU 1389 CB PRO A 201 4634 6148 4644 1185 -162 -318 C
ATOM 1390 CG PRO A 201 4.990 48.389 -9.367 1.00 41.92 C
ANISOU 1390 CG PRO A 201 4864 6285 4777 1264 -232 -220 C
ATOM 1391 CD PRO A 201 5.325 49.350 -8.264 1.00 41.53 C
ANISOU 1391 CD PRO A 201 4817 6142 4822 1252 -151 -166 C
ATOM 1392 N GLN A 202 8.525 47.878 -9.027 1.00 33.17 N
ANISOU 1392 N GLN A 202 3929 5165 3509 1093 63 -119 N
ATOM 1393 CA GLN A 202 9.785 47.636 -9.719 1.00 32.66 C
ANISOU 1393 CA GLN A 202 3953 5144 3313 1056 127 -76 C
ATOM 1394 C GLN A 202 10.929 47.296 -8.774 1.00 38.04 C
ANISOU 1394 C GLN A 202 4623 5795 4036 979 258 -84 C
ATOM 1395 O GLN A 202 11.963 46.801 -9.233 1.00 41.36 O
ANISOU 1395 O GLN A 202 5088 6262 4364 944 319 -79 O
ATOM 1396 CB GLN A 202 10.169 48.860 -10.558 1.00 32.85 C
ANISOU 1396 CB GLN A 202 4089 5156 3237 1088 110 52 C
ATOM 1397 CG GLN A 202 10.582 50.086 -9.742 1.00 39.35 C
ANISOU 1397 CG GLN A 202 4938 5881 4134 1072 167 138 C
ATOM 1398 CD GLN A 202 9.413 50.756 -9.046 1.00 48.21 C
ANISOU 1398 CD GLN A 202 5999 6934 5386 1126 99 126 C
ATOM 1399 OE1 GLN A 202 8.266 50.342 -9.201 1.00 53.04 O
ANISOU 1399 OE1 GLN A 202 6543 7575 6035 1175 6 56 O
ATOM 1400 NE2 GLN A 202 9.700 51.798 -8.275 1.00 46.16 N
ANISOU 1400 NE2 GLN A 202 5760 6582 5197 1117 144 189 N
ATOM 1401 N VAL A 203 10.771 47.550 -7.477 1.00 37.85 N
ANISOU 1401 N VAL A 203 4539 5696 4145 956 301 -100 N
ATOM 1402 CA VAL A 203 11.847 47.319 -6.522 1.00 32.54 C
ANISOU 1402 CA VAL A 203 3860 4988 3514 888 415 -103 C
ATOM 1403 C VAL A 203 12.026 45.824 -6.302 1.00 28.92 C
ANISOU 1403 C VAL A 203 3355 4573 3061 850 441 -207 C
ATOM 1404 O VAL A 203 11.064 45.103 -6.007 1.00 31.08 O
ANISOU 1404 O VAL A 203 3560 4853 3396 857 394 -290 O
ATOM 1405 CB VAL A 203 11.549 48.036 -5.197 1.00 31.38 C
ANISOU 1405 CB VAL A 203 3673 4750 3502 878 444 -94 C
ATOM 1406 CG1 VAL A 203 12.561 47.640 -4.126 1.00 28.41 C
ANISOU 1406 CG1 VAL A 203 3283 4339 3172 808 549 -114 C
ATOM 1407 CG2 VAL A 203 11.529 49.540 -5.399 1.00 28.28 C
ANISOU 1407 CG2 VAL A 203 3340 4301 3103 913 424 11 C
ATOM 1408 N ASN A 204 13.263 45.351 -6.444 1.00 31.93 N
ANISOU 1408 N ASN A 204 3771 4981 3378 810 515 -203 N
ATOM 1409 CA ASN A 204 13.630 43.991 -6.060 1.00 34.41 C
ANISOU 1409 CA ASN A 204 4049 5317 3708 774 551 -296 C
ATOM 1410 C ASN A 204 14.110 44.027 -4.613 1.00 35.13 C
ANISOU 1410 C ASN A 204 4108 5334 3906 726 626 -303 C
ATOM 1411 O ASN A 204 15.170 44.588 -4.320 1.00 40.74 O
ANISOU 1411 O ASN A 204 4849 6022 4608 699 695 -246 O
ATOM 1412 CB ASN A 204 14.707 43.430 -6.988 1.00 30.33 C
ANISOU 1412 CB ASN A 204 3582 4872 3068 767 588 -298 C
ATOM 1413 CG ASN A 204 14.996 41.958 -6.728 1.00 49.68 C
ANISOU 1413 CG ASN A 204 6003 7343 5530 743 607 -402 C
ATOM 1414 OD1 ASN A 204 14.178 41.258 -6.132 1.00 56.67 O
ANISOU 1414 OD1 ASN A 204 6837 8200 6495 735 571 -475 O
ATOM 1415 ND2 ASN A 204 16.159 41.483 -7.175 1.00 53.21 N
ANISOU 1415 ND2 ASN A 204 6481 7837 5899 732 664 -411 N
ATOM 1416 N LEU A 205 13.328 43.439 -3.708 1.00 29.68 N
ANISOU 1416 N LEU A 205 3356 4607 3313 711 612 -374 N
ATOM 1417 CA LEU A 205 13.651 43.461 -2.289 1.00 27.52 C
ANISOU 1417 CA LEU A 205 3058 4262 3135 667 676 -383 C
ATOM 1418 C LEU A 205 13.419 42.093 -1.670 1.00 27.09 C
ANISOU 1418 C LEU A 205 2966 4202 3126 634 681 -480 C
ATOM 1419 O LEU A 205 12.429 41.422 -1.971 1.00 31.59 O
ANISOU 1419 O LEU A 205 3500 4796 3708 643 624 -541 O
ATOM 1420 CB LEU A 205 12.814 44.508 -1.537 1.00 24.59 C
ANISOU 1420 CB LEU A 205 2660 3829 2854 681 664 -352 C
ATOM 1421 CG LEU A 205 13.211 44.718 -0.076 1.00 30.00 C
ANISOU 1421 CG LEU A 205 3334 4439 3627 638 733 -353 C
ATOM 1422 CD1 LEU A 205 14.587 45.364 0.009 1.00 32.62 C
ANISOU 1422 CD1 LEU A 205 3720 4752 3925 617 793 -284 C
ATOM 1423 CD2 LEU A 205 12.171 45.549 0.661 1.00 31.78 C
ANISOU 1423 CD2 LEU A 205 3522 4610 3943 657 716 -348 C
ATOM 1424 N SER A 206 14.340 41.692 -0.802 1.00 22.13 N
ANISOU 1424 N SER A 206 2348 3537 2524 593 747 -491 N
ATOM 1425 CA SER A 206 14.220 40.475 -0.014 1.00 22.18 C
ANISOU 1425 CA SER A 206 2332 3516 2579 555 759 -571 C
ATOM 1426 C SER A 206 14.089 40.841 1.457 1.00 27.62 C
ANISOU 1426 C SER A 206 3005 4127 3363 520 803 -564 C
ATOM 1427 O SER A 206 14.758 41.763 1.933 1.00 32.63 O
ANISOU 1427 O SER A 206 3660 4728 4010 516 844 -505 O
ATOM 1428 CB SER A 206 15.431 39.562 -0.223 1.00 18.64 C
ANISOU 1428 CB SER A 206 1917 3088 2076 544 789 -599 C
ATOM 1429 OG SER A 206 15.462 39.067 -1.547 1.00 26.83 O
ANISOU 1429 OG SER A 206 2970 4200 3024 576 750 -623 O
ATOM 1430 N LEU A 207 13.223 40.123 2.171 1.00 20.86 N
ANISOU 1430 N LEU A 207 2114 3241 2569 491 795 -626 N
ATOM 1431 CA LEU A 207 12.967 40.384 3.582 1.00 18.52 C
ANISOU 1431 CA LEU A 207 1816 2865 2355 452 828 -612 C
ATOM 1432 C LEU A 207 13.218 39.112 4.382 1.00 21.14 C
ANISOU 1432 C LEU A 207 2187 3144 2702 396 825 -636 C
ATOM 1433 O LEU A 207 12.655 38.057 4.070 1.00 20.70 O
ANISOU 1433 O LEU A 207 2111 3109 2646 381 800 -705 O
ATOM 1434 CB LEU A 207 11.526 40.875 3.806 1.00 18.64 C
ANISOU 1434 CB LEU A 207 1760 2886 2435 465 815 -641 C
ATOM 1435 CG LEU A 207 11.163 42.303 3.365 1.00 27.27 C
ANISOU 1435 CG LEU A 207 2842 3988 3532 519 791 -580 C
ATOM 1436 CD1 LEU A 207 9.656 42.546 3.420 1.00 21.02 C
ANISOU 1436 CD1 LEU A 207 1977 3205 2805 538 753 -614 C
ATOM 1437 CD2 LEU A 207 11.900 43.340 4.203 1.00 29.06 C
ANISOU 1437 CD2 LEU A 207 3104 4156 3782 514 846 -521 C
ATOM 1438 N ASP A 208 14.064 39.207 5.407 1.00 16.36 N
ANISOU 1438 N ASP A 208 1633 2478 2104 370 842 -588 N
ATOM 1439 CA ASP A 208 14.272 38.111 6.348 1.00 20.46 C
ANISOU 1439 CA ASP A 208 2189 2947 2639 322 835 -611 C
ATOM 1440 C ASP A 208 13.526 38.460 7.630 1.00 25.33 C
ANISOU 1440 C ASP A 208 2799 3514 3311 285 848 -604 C
ATOM 1441 O ASP A 208 13.932 39.365 8.367 1.00 28.40 O
ANISOU 1441 O ASP A 208 3207 3875 3708 285 858 -555 O
ATOM 1442 CB ASP A 208 15.756 37.873 6.616 1.00 17.95 C
ANISOU 1442 CB ASP A 208 1926 2608 2285 324 832 -578 C
ATOM 1443 CG ASP A 208 16.022 36.533 7.286 1.00 26.90 C
ANISOU 1443 CG ASP A 208 3096 3699 3425 288 820 -618 C
ATOM 1444 OD1 ASP A 208 15.119 36.009 7.974 1.00 25.89 O
ANISOU 1444 OD1 ASP A 208 2963 3538 3337 246 826 -654 O
ATOM 1445 OD2 ASP A 208 17.137 36.000 7.128 1.00 31.71 O
ANISOU 1445 OD2 ASP A 208 3738 4307 4002 303 810 -616 O
ATOM 1446 N MET A 209 12.434 37.744 7.887 1.00 22.90 N
ANISOU 1446 N MET A 209 2461 3199 3042 249 850 -659 N
ATOM 1447 CA MET A 209 11.568 37.997 9.030 1.00 18.35 C
ANISOU 1447 CA MET A 209 1870 2584 2517 209 871 -661 C
ATOM 1448 C MET A 209 11.737 36.966 10.136 1.00 21.56 C
ANISOU 1448 C MET A 209 2324 2933 2934 145 887 -683 C
ATOM 1449 O MET A 209 10.940 36.954 11.080 1.00 26.73 O
ANISOU 1449 O MET A 209 2969 3559 3629 101 914 -696 O
ATOM 1450 CB MET A 209 10.104 38.028 8.589 1.00 25.39 C
ANISOU 1450 CB MET A 209 2678 3514 3455 208 872 -712 C
ATOM 1451 CG MET A 209 9.775 39.073 7.543 1.00 30.45 C
ANISOU 1451 CG MET A 209 3265 4210 4094 277 855 -700 C
ATOM 1452 SD MET A 209 9.961 40.762 8.136 1.00 37.63 S
ANISOU 1452 SD MET A 209 4187 5093 5018 314 872 -627 S
ATOM 1453 CE MET A 209 9.149 41.658 6.818 1.00 50.48 C
ANISOU 1453 CE MET A 209 5729 6787 6663 392 851 -645 C
ATOM 1454 N SER A 210 12.753 36.110 10.047 1.00 17.23 N
ANISOU 1454 N SER A 210 1828 2368 2351 142 875 -689 N
ATOM 1455 CA SER A 210 12.885 34.988 10.968 1.00 20.61 C
ANISOU 1455 CA SER A 210 2303 2739 2788 85 891 -720 C
ATOM 1456 C SER A 210 12.938 35.461 12.418 1.00 19.05 C
ANISOU 1456 C SER A 210 2141 2488 2608 51 918 -686 C
ATOM 1457 O SER A 210 13.377 36.573 12.718 1.00 21.92 O
ANISOU 1457 O SER A 210 2511 2852 2965 78 911 -634 O
ATOM 1458 CB SER A 210 14.139 34.179 10.634 1.00 18.17 C
ANISOU 1458 CB SER A 210 2046 2420 2437 107 867 -726 C
ATOM 1459 OG SER A 210 14.141 33.787 9.271 1.00 17.81 O
ANISOU 1459 OG SER A 210 1973 2427 2366 143 842 -760 O
ATOM 1460 N LEU A 211 12.453 34.605 13.319 1.00 17.20 N
ANISOU 1460 N LEU A 211 1933 2205 2396 -14 953 -721 N
ATOM 1461 CA LEU A 211 12.542 34.825 14.765 1.00 18.39 C
ANISOU 1461 CA LEU A 211 2134 2300 2555 -54 984 -698 C
ATOM 1462 C LEU A 211 11.860 36.126 15.193 1.00 20.65 C
ANISOU 1462 C LEU A 211 2382 2601 2864 -44 997 -668 C
ATOM 1463 O LEU A 211 12.307 36.807 16.120 1.00 22.23 O
ANISOU 1463 O LEU A 211 2619 2770 3056 -44 1003 -634 O
ATOM 1464 CB LEU A 211 13.997 34.791 15.234 1.00 15.06 C
ANISOU 1464 CB LEU A 211 1781 1845 2098 -32 963 -666 C
ATOM 1465 CG LEU A 211 14.699 33.452 14.998 1.00 19.15 C
ANISOU 1465 CG LEU A 211 2347 2336 2593 -36 950 -700 C
ATOM 1466 CD1 LEU A 211 16.202 33.619 15.095 1.00 22.91 C
ANISOU 1466 CD1 LEU A 211 2863 2805 3038 10 915 -669 C
ATOM 1467 CD2 LEU A 211 14.207 32.409 15.990 1.00 17.61 C
ANISOU 1467 CD2 LEU A 211 2209 2074 2409 -109 998 -737 C
ATOM 1468 N ASN A 212 10.762 36.475 14.508 1.00 15.99 N
ANISOU 1468 N ASN A 212 1715 2058 2303 -33 998 -689 N
ATOM 1469 CA ASN A 212 9.881 37.540 14.967 1.00 18.27 C
ANISOU 1469 CA ASN A 212 1963 2357 2622 -27 1016 -676 C
ATOM 1470 C ASN A 212 8.562 36.944 15.449 1.00 23.62 C
ANISOU 1470 C ASN A 212 2600 3031 3341 -90 1062 -728 C
ATOM 1471 O ASN A 212 8.001 36.063 14.785 1.00 21.88 O
ANISOU 1471 O ASN A 212 2338 2834 3140 -115 1066 -779 O
ATOM 1472 CB ASN A 212 9.599 38.571 13.869 1.00 16.33 C
ANISOU 1472 CB ASN A 212 1654 2169 2383 43 984 -660 C
ATOM 1473 CG ASN A 212 10.716 39.594 13.727 1.00 21.82 C
ANISOU 1473 CG ASN A 212 2384 2861 3045 96 958 -603 C
ATOM 1474 OD1 ASN A 212 10.774 40.575 14.469 1.00 19.52 O
ANISOU 1474 OD1 ASN A 212 2108 2548 2762 104 967 -576 O
ATOM 1475 ND2 ASN A 212 11.602 39.373 12.764 1.00 15.54 N
ANISOU 1475 ND2 ASN A 212 1600 2089 2215 128 929 -590 N
ATOM 1476 N PRO A 213 8.051 37.389 16.603 1.00 17.17 N
ANISOU 1476 N PRO A 213 1794 2189 2541 -119 1101 -723 N
ATOM 1477 CA PRO A 213 6.821 36.808 17.176 1.00 19.59 C
ANISOU 1477 CA PRO A 213 2064 2493 2885 -188 1156 -773 C
ATOM 1478 C PRO A 213 5.557 37.273 16.459 1.00 19.36 C
ANISOU 1478 C PRO A 213 1924 2527 2906 -164 1150 -805 C
ATOM 1479 O PRO A 213 4.655 37.869 17.051 1.00 26.96 O
ANISOU 1479 O PRO A 213 2845 3500 3898 -169 1179 -815 O
ATOM 1480 CB PRO A 213 6.889 37.283 18.633 1.00 19.60 C
ANISOU 1480 CB PRO A 213 2123 2450 2874 -213 1196 -750 C
ATOM 1481 CG PRO A 213 7.604 38.590 18.557 1.00 19.75 C
ANISOU 1481 CG PRO A 213 2155 2474 2875 -138 1154 -700 C
ATOM 1482 CD PRO A 213 8.608 38.464 17.443 1.00 16.82 C
ANISOU 1482 CD PRO A 213 1795 2119 2479 -92 1099 -677 C
ATOM 1483 N ILE A 214 5.483 36.978 15.163 1.00 18.63 N
ANISOU 1483 N ILE A 214 1778 2478 2822 -135 1112 -827 N
ATOM 1484 CA ILE A 214 4.352 37.405 14.346 1.00 23.76 C
ANISOU 1484 CA ILE A 214 2316 3192 3520 -104 1095 -861 C
ATOM 1485 C ILE A 214 3.112 36.609 14.734 1.00 23.84 C
ANISOU 1485 C ILE A 214 2263 3213 3583 -184 1141 -928 C
ATOM 1486 O ILE A 214 3.117 35.372 14.710 1.00 24.92 O
ANISOU 1486 O ILE A 214 2412 3333 3722 -255 1164 -970 O
ATOM 1487 CB ILE A 214 4.670 37.243 12.854 1.00 21.63 C
ANISOU 1487 CB ILE A 214 2012 2968 3239 -53 1039 -873 C
ATOM 1488 CG1 ILE A 214 5.757 38.236 12.430 1.00 22.51 C
ANISOU 1488 CG1 ILE A 214 2173 3078 3303 28 1001 -805 C
ATOM 1489 CG2 ILE A 214 3.415 37.409 12.014 1.00 20.01 C
ANISOU 1489 CG2 ILE A 214 1683 2831 3091 -32 1019 -927 C
ATOM 1490 CD1 ILE A 214 6.328 37.971 11.056 1.00 23.74 C
ANISOU 1490 CD1 ILE A 214 2321 3272 3429 73 956 -810 C
ATOM 1491 N ASP A 215 2.036 37.318 15.088 1.00 20.90 N
ANISOU 1491 N ASP A 215 1818 2868 3253 -174 1159 -942 N
ATOM 1492 CA ASP A 215 0.757 36.682 15.363 1.00 28.45 C
ANISOU 1492 CA ASP A 215 2695 3849 4267 -246 1201 -1007 C
ATOM 1493 C ASP A 215 -0.421 37.323 14.639 1.00 25.37 C
ANISOU 1493 C ASP A 215 2171 3530 3937 -197 1171 -1044 C
ATOM 1494 O ASP A 215 -1.558 36.878 14.837 1.00 30.14 O
ANISOU 1494 O ASP A 215 2693 4162 4595 -253 1201 -1102 O
ATOM 1495 CB ASP A 215 0.473 36.668 16.876 1.00 31.35 C
ANISOU 1495 CB ASP A 215 3110 4173 4629 -307 1274 -1001 C
ATOM 1496 CG ASP A 215 0.516 38.053 17.502 1.00 43.03 C
ANISOU 1496 CG ASP A 215 4604 5649 6097 -240 1274 -957 C
ATOM 1497 OD1 ASP A 215 -0.146 38.974 16.982 1.00 49.09 O
ANISOU 1497 OD1 ASP A 215 5287 6464 6900 -171 1246 -964 O
ATOM 1498 OD2 ASP A 215 1.195 38.213 18.538 1.00 45.53 O
ANISOU 1498 OD2 ASP A 215 5016 5912 6369 -256 1303 -920 O
ATOM 1499 N PHE A 216 -0.197 38.347 13.815 1.00 27.94 N
ANISOU 1499 N PHE A 216 2473 3885 4259 -96 1112 -1015 N
ATOM 1500 CA PHE A 216 -1.298 38.995 13.105 1.00 27.56 C
ANISOU 1500 CA PHE A 216 2299 3902 4271 -39 1075 -1050 C
ATOM 1501 C PHE A 216 -0.792 39.592 11.801 1.00 31.81 C
ANISOU 1501 C PHE A 216 2824 4471 4792 57 1000 -1028 C
ATOM 1502 O PHE A 216 0.141 40.401 11.803 1.00 27.05 O
ANISOU 1502 O PHE A 216 2297 3839 4143 116 989 -963 O
ATOM 1503 CB PHE A 216 -1.951 40.081 13.967 1.00 23.91 C
ANISOU 1503 CB PHE A 216 1813 3438 3834 -5 1106 -1037 C
ATOM 1504 CG PHE A 216 -3.111 40.767 13.300 1.00 29.79 C
ANISOU 1504 CG PHE A 216 2426 4246 4646 60 1067 -1077 C
ATOM 1505 CD1 PHE A 216 -4.241 40.048 12.938 1.00 32.65 C
ANISOU 1505 CD1 PHE A 216 2673 4660 5071 14 1061 -1151 C
ATOM 1506 CD2 PHE A 216 -3.079 42.127 13.045 1.00 30.88 C
ANISOU 1506 CD2 PHE A 216 2554 4389 4789 165 1035 -1043 C
ATOM 1507 CE1 PHE A 216 -5.308 40.673 12.327 1.00 32.04 C
ANISOU 1507 CE1 PHE A 216 2470 4644 5060 79 1015 -1191 C
ATOM 1508 CE2 PHE A 216 -4.146 42.758 12.434 1.00 30.18 C
ANISOU 1508 CE2 PHE A 216 2346 4354 4767 233 992 -1081 C
ATOM 1509 CZ PHE A 216 -5.260 42.031 12.075 1.00 30.86 C
ANISOU 1509 CZ PHE A 216 2315 4497 4915 192 979 -1155 C
ATOM 1510 N ILE A 217 -1.412 39.194 10.695 1.00 31.66 N
ANISOU 1510 N ILE A 217 2706 4513 4809 71 949 -1085 N
ATOM 1511 CA ILE A 217 -1.198 39.815 9.394 1.00 27.87 C
ANISOU 1511 CA ILE A 217 2191 4076 4321 170 872 -1077 C
ATOM 1512 C ILE A 217 -2.538 40.374 8.938 1.00 32.00 C
ANISOU 1512 C ILE A 217 2579 4660 4919 220 827 -1125 C
ATOM 1513 O ILE A 217 -3.525 39.633 8.855 1.00 25.75 O
ANISOU 1513 O ILE A 217 1693 3909 4182 166 821 -1197 O
ATOM 1514 CB ILE A 217 -0.633 38.816 8.367 1.00 30.42 C
ANISOU 1514 CB ILE A 217 2521 4426 4609 155 832 -1110 C
ATOM 1515 CG1 ILE A 217 0.719 38.265 8.831 1.00 31.40 C
ANISOU 1515 CG1 ILE A 217 2781 4488 4661 113 873 -1063 C
ATOM 1516 CG2 ILE A 217 -0.495 39.469 7.001 1.00 29.47 C
ANISOU 1516 CG2 ILE A 217 2361 4363 4474 262 748 -1108 C
ATOM 1517 CD1 ILE A 217 1.388 37.343 7.833 1.00 38.28 C
ANISOU 1517 CD1 ILE A 217 3670 5384 5490 110 838 -1096 C
ATOM 1518 N GLN A 218 -2.574 41.674 8.657 1.00 33.23 N
ANISOU 1518 N GLN A 218 2724 4821 5082 322 793 -1087 N
ATOM 1519 CA GLN A 218 -3.832 42.328 8.324 1.00 31.21 C
ANISOU 1519 CA GLN A 218 2345 4615 4900 383 747 -1128 C
ATOM 1520 C GLN A 218 -4.424 41.747 7.043 1.00 34.45 C
ANISOU 1520 C GLN A 218 2650 5102 5338 403 656 -1195 C
ATOM 1521 O GLN A 218 -3.709 41.257 6.163 1.00 32.06 O
ANISOU 1521 O GLN A 218 2377 4818 4987 413 613 -1197 O
ATOM 1522 CB GLN A 218 -3.625 43.837 8.168 1.00 31.47 C
ANISOU 1522 CB GLN A 218 2398 4628 4932 499 720 -1074 C
ATOM 1523 CG GLN A 218 -4.926 44.626 8.038 1.00 31.24 C
ANISOU 1523 CG GLN A 218 2252 4637 4982 568 678 -1111 C
ATOM 1524 CD GLN A 218 -4.714 46.125 7.988 1.00 33.42 C
ANISOU 1524 CD GLN A 218 2557 4879 5262 682 656 -1060 C
ATOM 1525 OE1 GLN A 218 -3.598 46.602 7.788 1.00 35.58 O
ANISOU 1525 OE1 GLN A 218 2927 5112 5480 718 658 -998 O
ATOM 1526 NE2 GLN A 218 -5.791 46.880 8.173 1.00 38.13 N
ANISOU 1526 NE2 GLN A 218 3069 5492 5927 740 637 -1088 N
ATOM 1527 N ASP A 219 -5.752 41.800 6.954 1.00 40.08 N
ANISOU 1527 N ASP A 219 3236 5862 6128 410 623 -1256 N
ATOM 1528 CA ASP A 219 -6.460 41.353 5.762 1.00 42.06 C
ANISOU 1528 CA ASP A 219 3375 6192 6413 435 520 -1325 C
ATOM 1529 C ASP A 219 -5.968 42.122 4.543 1.00 45.03 C
ANISOU 1529 C ASP A 219 3764 6596 6750 563 418 -1294 C
ATOM 1530 O ASP A 219 -6.014 43.356 4.519 1.00 41.90 O
ANISOU 1530 O ASP A 219 3377 6182 6363 660 395 -1250 O
ATOM 1531 CB ASP A 219 -7.964 41.549 5.958 1.00 48.21 C
ANISOU 1531 CB ASP A 219 4020 7013 7286 438 500 -1384 C
ATOM 1532 CG ASP A 219 -8.799 40.643 5.073 1.00 61.67 C
ANISOU 1532 CG ASP A 219 5607 8792 9033 408 417 -1472 C
ATOM 1533 OD1 ASP A 219 -8.843 39.424 5.339 1.00 69.34 O
ANISOU 1533 OD1 ASP A 219 6572 9764 10009 290 460 -1516 O
ATOM 1534 OD2 ASP A 219 -9.425 41.150 4.119 1.00 67.40 O
ANISOU 1534 OD2 ASP A 219 6248 9574 9788 501 303 -1498 O
ATOM 1535 N GLN A 220 -5.468 41.385 3.548 1.00 47.96 N
ANISOU 1535 N GLN A 220 4142 7008 7073 563 357 -1319 N
ATOM 1536 CA GLN A 220 -4.996 41.916 2.270 1.00 45.39 C
ANISOU 1536 CA GLN A 220 3829 6726 6693 681 251 -1298 C
ATOM 1537 C GLN A 220 -3.719 42.739 2.390 1.00 40.79 C
ANISOU 1537 C GLN A 220 3392 6079 6028 728 290 -1195 C
ATOM 1538 O GLN A 220 -3.438 43.568 1.519 1.00 37.83 O
ANISOU 1538 O GLN A 220 3070 5705 5597 825 207 -1134 O
ATOM 1539 CB GLN A 220 -6.072 42.754 1.571 1.00 44.14 C
ANISOU 1539 CB GLN A 220 3568 6616 6586 789 133 -1319 C
ATOM 1540 CG GLN A 220 -7.205 41.944 0.989 1.00 55.12 C
ANISOU 1540 CG GLN A 220 4832 8081 8031 758 48 -1412 C
ATOM 1541 CD GLN A 220 -7.675 42.503 -0.336 1.00 68.43 C
ANISOU 1541 CD GLN A 220 6470 9830 9702 885 -118 -1419 C
ATOM 1542 OE1 GLN A 220 -7.462 43.679 -0.635 1.00 76.26 O
ANISOU 1542 OE1 GLN A 220 7511 10799 10667 997 -163 -1351 O
ATOM 1543 NE2 GLN A 220 -8.300 41.660 -1.145 1.00 71.61 N
ANISOU 1543 NE2 GLN A 220 6804 10296 10107 859 -216 -1488 N
ATOM 1544 N ALA A 221 -2.926 42.523 3.443 1.00 26.72 N
ANISOU 1544 N ALA A 221 1689 4233 4230 655 411 -1164 N
ATOM 1545 CA ALA A 221 -1.687 43.278 3.593 1.00 29.25 C
ANISOU 1545 CA ALA A 221 2137 4495 4481 692 450 -1074 C
ATOM 1546 C ALA A 221 -0.724 43.017 2.443 1.00 33.74 C
ANISOU 1546 C ALA A 221 2816 5073 4931 710 384 -1018 C
ATOM 1547 O ALA A 221 0.100 43.880 2.116 1.00 33.67 O
ANISOU 1547 O ALA A 221 2900 5034 4859 768 374 -935 O
ATOM 1548 CB ALA A 221 -1.017 42.936 4.924 1.00 27.28 C
ANISOU 1548 CB ALA A 221 1976 4168 4219 593 571 -1041 C
ATOM 1549 N PHE A 222 -0.816 41.845 1.815 1.00 29.95 N
ANISOU 1549 N PHE A 222 2328 4635 4417 661 342 -1065 N
ATOM 1550 CA PHE A 222 0.108 41.435 0.768 1.00 29.08 C
ANISOU 1550 CA PHE A 222 2322 4539 4190 670 292 -1026 C
ATOM 1551 C PHE A 222 -0.493 41.506 -0.628 1.00 32.38 C
ANISOU 1551 C PHE A 222 2709 5024 4569 739 156 -1040 C
ATOM 1552 O PHE A 222 0.057 40.904 -1.555 1.00 31.52 O
ANISOU 1552 O PHE A 222 2669 4942 4364 735 109 -1034 O
ATOM 1553 CB PHE A 222 0.617 40.021 1.044 1.00 24.60 C
ANISOU 1553 CB PHE A 222 1792 3959 3595 570 341 -1067 C
ATOM 1554 CG PHE A 222 1.680 39.965 2.094 1.00 25.89 C
ANISOU 1554 CG PHE A 222 2039 4054 3745 519 454 -1026 C
ATOM 1555 CD1 PHE A 222 3.013 40.089 1.748 1.00 30.24 C
ANISOU 1555 CD1 PHE A 222 2706 4583 4200 536 468 -959 C
ATOM 1556 CD2 PHE A 222 1.348 39.810 3.432 1.00 28.82 C
ANISOU 1556 CD2 PHE A 222 2370 4385 4197 456 546 -1054 C
ATOM 1557 CE1 PHE A 222 4.004 40.048 2.712 1.00 25.20 C
ANISOU 1557 CE1 PHE A 222 2138 3884 3553 494 563 -925 C
ATOM 1558 CE2 PHE A 222 2.336 39.770 4.406 1.00 29.86 C
ANISOU 1558 CE2 PHE A 222 2585 4452 4310 414 640 -1017 C
ATOM 1559 CZ PHE A 222 3.667 39.888 4.043 1.00 23.65 C
ANISOU 1559 CZ PHE A 222 1909 3644 3434 434 644 -953 C
ATOM 1560 N GLN A 223 -1.603 42.217 -0.801 1.00 41.91 N
ANISOU 1560 N GLN A 223 3816 6261 5845 805 89 -1063 N
ATOM 1561 CA GLN A 223 -2.110 42.475 -2.141 1.00 45.24 C
ANISOU 1561 CA GLN A 223 4225 6742 6222 886 -52 -1063 C
ATOM 1562 C GLN A 223 -1.201 43.470 -2.851 1.00 42.79 C
ANISOU 1562 C GLN A 223 4042 6411 5805 965 -82 -954 C
ATOM 1563 O GLN A 223 -0.843 44.512 -2.292 1.00 39.15 O
ANISOU 1563 O GLN A 223 3617 5896 5364 1001 -31 -889 O
ATOM 1564 CB GLN A 223 -3.540 43.006 -2.084 1.00 48.09 C
ANISOU 1564 CB GLN A 223 4439 7137 6694 943 -121 -1118 C
ATOM 1565 CG GLN A 223 -4.575 41.949 -1.726 1.00 57.84 C
ANISOU 1565 CG GLN A 223 5536 8416 8026 865 -119 -1234 C
ATOM 1566 CD GLN A 223 -4.544 40.751 -2.662 1.00 62.91 C
ANISOU 1566 CD GLN A 223 6196 9104 8602 818 -192 -1282 C
ATOM 1567 OE1 GLN A 223 -4.313 40.890 -3.863 1.00 67.20 O
ANISOU 1567 OE1 GLN A 223 6804 9681 9048 882 -297 -1252 O
ATOM 1568 NE2 GLN A 223 -4.779 39.566 -2.112 1.00 62.05 N
ANISOU 1568 NE2 GLN A 223 6038 8995 8542 705 -136 -1357 N
ATOM 1569 N GLY A 224 -0.819 43.141 -4.083 1.00 39.75 N
ANISOU 1569 N GLY A 224 3729 6069 5305 988 -161 -935 N
ATOM 1570 CA GLY A 224 0.064 44.004 -4.842 1.00 33.21 C
ANISOU 1570 CA GLY A 224 3027 5227 4363 1052 -184 -830 C
ATOM 1571 C GLY A 224 1.489 44.048 -4.343 1.00 37.73 C
ANISOU 1571 C GLY A 224 3709 5748 4880 1003 -66 -763 C
ATOM 1572 O GLY A 224 2.214 44.997 -4.654 1.00 41.63 O
ANISOU 1572 O GLY A 224 4295 6214 5308 1046 -58 -668 O
ATOM 1573 N ILE A 225 1.920 43.041 -3.587 1.00 32.98 N
ANISOU 1573 N ILE A 225 3100 5129 4302 911 23 -810 N
ATOM 1574 CA ILE A 225 3.248 43.011 -2.987 1.00 27.87 C
ANISOU 1574 CA ILE A 225 2542 4432 3616 863 134 -758 C
ATOM 1575 C ILE A 225 4.085 41.967 -3.711 1.00 28.79 C
ANISOU 1575 C ILE A 225 2728 4583 3627 828 134 -773 C
ATOM 1576 O ILE A 225 3.650 40.822 -3.889 1.00 32.13 O
ANISOU 1576 O ILE A 225 3110 5038 4058 788 105 -856 O
ATOM 1577 CB ILE A 225 3.177 42.715 -1.480 1.00 28.63 C
ANISOU 1577 CB ILE A 225 2588 4473 3816 794 237 -795 C
ATOM 1578 CG1 ILE A 225 2.313 43.766 -0.783 1.00 27.98 C
ANISOU 1578 CG1 ILE A 225 2433 4362 3836 836 239 -790 C
ATOM 1579 CG2 ILE A 225 4.572 42.687 -0.874 1.00 23.14 C
ANISOU 1579 CG2 ILE A 225 1985 3727 3079 749 338 -744 C
ATOM 1580 CD1 ILE A 225 2.725 45.192 -1.081 1.00 28.57 C
ANISOU 1580 CD1 ILE A 225 2574 4405 3878 913 222 -694 C
ATOM 1581 N LYS A 226 5.281 42.365 -4.128 1.00 24.47 N
ANISOU 1581 N LYS A 226 2285 4030 2982 841 168 -696 N
ATOM 1582 CA LYS A 226 6.231 41.472 -4.768 1.00 29.38 C
ANISOU 1582 CA LYS A 226 2976 4684 3501 814 183 -707 C
ATOM 1583 C LYS A 226 7.507 41.436 -3.940 1.00 32.19 C
ANISOU 1583 C LYS A 226 3386 4990 3854 766 297 -670 C
ATOM 1584 O LYS A 226 7.975 42.473 -3.459 1.00 27.66 O
ANISOU 1584 O LYS A 226 2840 4373 3298 778 345 -596 O
ATOM 1585 CB LYS A 226 6.543 41.930 -6.195 1.00 39.45 C
ANISOU 1585 CB LYS A 226 4327 6016 4646 876 117 -653 C
ATOM 1586 CG LYS A 226 6.484 40.833 -7.236 1.00 53.33 C
ANISOU 1586 CG LYS A 226 6102 7842 6318 875 55 -718 C
ATOM 1587 CD LYS A 226 7.051 41.323 -8.553 1.00 63.31 C
ANISOU 1587 CD LYS A 226 7461 9160 7434 928 17 -653 C
ATOM 1588 CE LYS A 226 8.417 41.958 -8.357 1.00 68.48 C
ANISOU 1588 CE LYS A 226 8196 9788 8037 915 118 -563 C
ATOM 1589 NZ LYS A 226 9.066 42.315 -9.648 1.00 70.43 N
ANISOU 1589 NZ LYS A 226 8539 10092 8128 952 99 -502 N
ATOM 1590 N LEU A 227 8.059 40.239 -3.761 1.00 25.95 N
ANISOU 1590 N LEU A 227 2611 4201 3047 715 334 -726 N
ATOM 1591 CA LEU A 227 9.290 40.057 -3.008 1.00 23.18 C
ANISOU 1591 CA LEU A 227 2306 3807 2693 673 431 -703 C
ATOM 1592 C LEU A 227 10.147 39.023 -3.719 1.00 27.40 C
ANISOU 1592 C LEU A 227 2893 4382 3137 663 435 -738 C
ATOM 1593 O LEU A 227 9.633 38.076 -4.318 1.00 29.39 O
ANISOU 1593 O LEU A 227 3131 4670 3365 661 377 -810 O
ATOM 1594 CB LEU A 227 9.023 39.609 -1.562 1.00 20.98 C
ANISOU 1594 CB LEU A 227 1982 3463 2524 613 488 -745 C
ATOM 1595 CG LEU A 227 8.502 40.659 -0.577 1.00 24.48 C
ANISOU 1595 CG LEU A 227 2386 3857 3058 616 519 -709 C
ATOM 1596 CD1 LEU A 227 8.155 40.029 0.766 1.00 20.26 C
ANISOU 1596 CD1 LEU A 227 1811 3269 2616 551 574 -762 C
ATOM 1597 CD2 LEU A 227 9.526 41.757 -0.391 1.00 29.01 C
ANISOU 1597 CD2 LEU A 227 3019 4400 3604 635 569 -618 C
ATOM 1598 N HIS A 228 11.463 39.223 -3.663 1.00 25.79 N
ANISOU 1598 N HIS A 228 2747 4171 2882 659 502 -690 N
ATOM 1599 CA HIS A 228 12.388 38.223 -4.180 1.00 24.30 C
ANISOU 1599 CA HIS A 228 2601 4015 2617 652 519 -731 C
ATOM 1600 C HIS A 228 12.421 37.030 -3.236 1.00 22.98 C
ANISOU 1600 C HIS A 228 2416 3797 2519 601 545 -807 C
ATOM 1601 O HIS A 228 11.888 35.960 -3.546 1.00 25.85 O
ANISOU 1601 O HIS A 228 2768 4173 2880 589 497 -887 O
ATOM 1602 CB HIS A 228 13.795 38.800 -4.349 1.00 21.92 C
ANISOU 1602 CB HIS A 228 2352 3724 2251 660 588 -662 C
ATOM 1603 CG HIS A 228 14.774 37.837 -4.947 1.00 25.12 C
ANISOU 1603 CG HIS A 228 2795 4173 2576 663 609 -707 C
ATOM 1604 ND1 HIS A 228 14.671 37.381 -6.244 1.00 30.90 N
ANISOU 1604 ND1 HIS A 228 3555 4980 3206 698 560 -740 N
ATOM 1605 CD2 HIS A 228 15.868 37.235 -4.424 1.00 27.52 C
ANISOU 1605 CD2 HIS A 228 3112 4457 2887 643 671 -730 C
ATOM 1606 CE1 HIS A 228 15.659 36.541 -6.495 1.00 27.70 C
ANISOU 1606 CE1 HIS A 228 3178 4600 2749 699 597 -785 C
ATOM 1607 NE2 HIS A 228 16.399 36.434 -5.407 1.00 25.45 N
ANISOU 1607 NE2 HIS A 228 2881 4257 2532 668 662 -780 N
ATOM 1608 N GLU A 229 13.039 37.215 -2.076 1.00 24.57 N
ANISOU 1608 N GLU A 229 2621 3937 2778 568 615 -781 N
ATOM 1609 CA GLU A 229 13.187 36.163 -1.084 1.00 22.75 C
ANISOU 1609 CA GLU A 229 2390 3648 2606 520 643 -840 C
ATOM 1610 C GLU A 229 12.501 36.585 0.204 1.00 23.56 C
ANISOU 1610 C GLU A 229 2454 3686 2813 481 671 -827 C
ATOM 1611 O GLU A 229 12.778 37.667 0.732 1.00 25.51 O
ANISOU 1611 O GLU A 229 2701 3909 3083 487 710 -761 O
ATOM 1612 CB GLU A 229 14.663 35.866 -0.819 1.00 22.26 C
ANISOU 1612 CB GLU A 229 2373 3572 2511 518 700 -829 C
ATOM 1613 CG GLU A 229 14.902 34.555 -0.109 1.00 32.56 C
ANISOU 1613 CG GLU A 229 3709 4804 3859 472 695 -874 C
ATOM 1614 CD GLU A 229 16.370 34.273 0.093 1.00 44.97 C
ANISOU 1614 CD GLU A 229 5340 6334 5412 468 718 -830 C
ATOM 1615 OE1 GLU A 229 16.978 34.905 0.978 1.00 47.09 O
ANISOU 1615 OE1 GLU A 229 5624 6548 5720 450 754 -762 O
ATOM 1616 OE2 GLU A 229 16.920 33.427 -0.641 1.00 48.36 O
ANISOU 1616 OE2 GLU A 229 5797 6788 5791 487 699 -870 O
ATOM 1617 N LEU A 230 11.612 35.733 0.708 1.00 19.70 N
ANISOU 1617 N LEU A 230 1934 3167 2383 438 653 -891 N
ATOM 1618 CA LEU A 230 10.955 35.937 1.992 1.00 19.94 C
ANISOU 1618 CA LEU A 230 1931 3138 2507 392 690 -891 C
ATOM 1619 C LEU A 230 11.277 34.751 2.886 1.00 22.15 C
ANISOU 1619 C LEU A 230 2244 3357 2815 334 721 -938 C
ATOM 1620 O LEU A 230 10.944 33.610 2.551 1.00 26.88 O
ANISOU 1620 O LEU A 230 2848 3957 3410 310 685 -1004 O
ATOM 1621 CB LEU A 230 9.442 36.088 1.828 1.00 19.28 C
ANISOU 1621 CB LEU A 230 1771 3077 2477 387 645 -923 C
ATOM 1622 CG LEU A 230 8.657 36.233 3.135 1.00 24.87 C
ANISOU 1622 CG LEU A 230 2434 3733 3282 336 691 -934 C
ATOM 1623 CD1 LEU A 230 9.012 37.529 3.850 1.00 23.90 C
ANISOU 1623 CD1 LEU A 230 2317 3581 3181 358 743 -864 C
ATOM 1624 CD2 LEU A 230 7.156 36.141 2.881 1.00 19.92 C
ANISOU 1624 CD2 LEU A 230 1718 3140 2712 326 644 -985 C
ATOM 1625 N THR A 231 11.921 35.014 4.015 1.00 23.56 N
ANISOU 1625 N THR A 231 2472 3461 3019 305 759 -873 N
ATOM 1626 CA THR A 231 12.262 33.980 4.982 1.00 21.01 C
ANISOU 1626 CA THR A 231 2200 3065 2717 251 773 -889 C
ATOM 1627 C THR A 231 11.371 34.138 6.204 1.00 18.58 C
ANISOU 1627 C THR A 231 1870 2708 2481 194 805 -887 C
ATOM 1628 O THR A 231 11.347 35.208 6.818 1.00 22.44 O
ANISOU 1628 O THR A 231 2356 3179 2989 201 824 -822 O
ATOM 1629 CB THR A 231 13.736 34.064 5.379 1.00 19.15 C
ANISOU 1629 CB THR A 231 2039 2791 2447 266 781 -824 C
ATOM 1630 OG1 THR A 231 14.544 34.099 4.199 1.00 20.59 O
ANISOU 1630 OG1 THR A 231 2233 3027 2564 318 762 -818 O
ATOM 1631 CG2 THR A 231 14.133 32.860 6.210 1.00 18.15 C
ANISOU 1631 CG2 THR A 231 1965 2598 2332 224 782 -855 C
ATOM 1632 N LEU A 232 10.637 33.070 6.550 1.00 17.65 N
ANISOU 1632 N LEU A 232 1738 2568 2401 136 814 -961 N
ATOM 1633 CA LEU A 232 9.788 33.014 7.744 1.00 24.72 C
ANISOU 1633 CA LEU A 232 2617 3417 3361 68 856 -968 C
ATOM 1634 C LEU A 232 10.172 31.749 8.510 1.00 26.50 C
ANISOU 1634 C LEU A 232 2911 3570 3586 8 879 -1002 C
ATOM 1635 O LEU A 232 9.524 30.705 8.382 1.00 32.74 O
ANISOU 1635 O LEU A 232 3685 4353 4402 -41 888 -1089 O
ATOM 1636 CB LEU A 232 8.296 33.024 7.384 1.00 24.27 C
ANISOU 1636 CB LEU A 232 2453 3408 3359 47 858 -1036 C
ATOM 1637 CG LEU A 232 7.670 34.294 6.806 1.00 30.75 C
ANISOU 1637 CG LEU A 232 3197 4292 4195 105 836 -1009 C
ATOM 1638 CD1 LEU A 232 6.243 34.005 6.350 1.00 25.17 C
ANISOU 1638 CD1 LEU A 232 2384 3635 3543 83 811 -1084 C
ATOM 1639 CD2 LEU A 232 7.705 35.425 7.822 1.00 26.64 C
ANISOU 1639 CD2 LEU A 232 2696 3731 3694 108 865 -926 C
ATOM 1640 N ARG A 233 11.238 31.842 9.301 1.00 19.33 N
ANISOU 1640 N ARG A 233 2083 2608 2653 13 886 -941 N
ATOM 1641 CA ARG A 233 11.729 30.728 10.102 1.00 22.76 C
ANISOU 1641 CA ARG A 233 2595 2967 3084 -33 903 -965 C
ATOM 1642 C ARG A 233 11.603 31.052 11.584 1.00 21.86 C
ANISOU 1642 C ARG A 233 2516 2795 2995 -83 951 -923 C
ATOM 1643 O ARG A 233 11.944 32.155 12.023 1.00 19.21 O
ANISOU 1643 O ARG A 233 2180 2466 2652 -55 949 -853 O
ATOM 1644 CB ARG A 233 13.188 30.392 9.768 1.00 16.74 C
ANISOU 1644 CB ARG A 233 1899 2193 2268 23 862 -941 C
ATOM 1645 CG ARG A 233 13.405 29.856 8.359 1.00 17.05 C
ANISOU 1645 CG ARG A 233 1924 2283 2273 69 816 -991 C
ATOM 1646 CD ARG A 233 14.774 29.212 8.214 1.00 18.98 C
ANISOU 1646 CD ARG A 233 2237 2502 2472 112 783 -984 C
ATOM 1647 NE ARG A 233 14.890 28.005 9.025 1.00 19.33 N
ANISOU 1647 NE ARG A 233 2354 2459 2532 68 787 -1025 N
ATOM 1648 CZ ARG A 233 16.031 27.360 9.232 1.00 23.12 C
ANISOU 1648 CZ ARG A 233 2902 2896 2985 101 758 -1020 C
ATOM 1649 NH1 ARG A 233 17.150 27.815 8.688 1.00 19.82 N
ANISOU 1649 NH1 ARG A 233 2477 2523 2529 174 731 -980 N
ATOM 1650 NH2 ARG A 233 16.055 26.267 9.984 1.00 17.35 N
ANISOU 1650 NH2 ARG A 233 2248 2075 2268 61 755 -1056 N
ATOM 1651 N GLY A 234 11.111 30.084 12.349 1.00 17.30 N
ANISOU 1651 N GLY A 234 1974 2158 2440 -161 995 -971 N
ATOM 1652 CA GLY A 234 11.003 30.249 13.787 1.00 20.20 C
ANISOU 1652 CA GLY A 234 2388 2468 2819 -215 1048 -938 C
ATOM 1653 C GLY A 234 10.106 31.383 14.229 1.00 21.55 C
ANISOU 1653 C GLY A 234 2492 2672 3023 -226 1076 -905 C
ATOM 1654 O GLY A 234 10.353 31.982 15.281 1.00 25.34 O
ANISOU 1654 O GLY A 234 3012 3121 3497 -234 1096 -855 O
ATOM 1655 N ASN A 235 9.058 31.693 13.461 1.00 19.87 N
ANISOU 1655 N ASN A 235 2180 2522 2847 -222 1072 -938 N
ATOM 1656 CA ASN A 235 8.151 32.772 13.838 1.00 19.69 C
ANISOU 1656 CA ASN A 235 2092 2529 2859 -222 1088 -913 C
ATOM 1657 C ASN A 235 7.016 32.314 14.740 1.00 28.54 C
ANISOU 1657 C ASN A 235 3191 3627 4024 -315 1159 -953 C
ATOM 1658 O ASN A 235 6.500 33.119 15.524 1.00 23.13 O
ANISOU 1658 O ASN A 235 2491 2942 3356 -321 1182 -923 O
ATOM 1659 CB ASN A 235 7.543 33.433 12.596 1.00 18.08 C
ANISOU 1659 CB ASN A 235 1790 2406 2675 -163 1045 -926 C
ATOM 1660 CG ASN A 235 8.585 34.054 11.695 1.00 19.00 C
ANISOU 1660 CG ASN A 235 1926 2550 2742 -74 988 -879 C
ATOM 1661 OD1 ASN A 235 9.205 33.360 10.893 1.00 29.30 O
ANISOU 1661 OD1 ASN A 235 3251 3865 4015 -55 959 -904 O
ATOM 1662 ND2 ASN A 235 8.783 35.363 11.818 1.00 20.42 N
ANISOU 1662 ND2 ASN A 235 2102 2742 2914 -22 973 -815 N
ATOM 1663 N PHE A 236 6.618 31.048 14.664 1.00 25.21 N
ANISOU 1663 N PHE A 236 2772 3187 3621 -390 1197 -1023 N
ATOM 1664 CA PHE A 236 5.343 30.615 15.211 1.00 27.39 C
ANISOU 1664 CA PHE A 236 2995 3464 3949 -486 1265 -1071 C
ATOM 1665 C PHE A 236 5.531 29.588 16.316 1.00 31.69 C
ANISOU 1665 C PHE A 236 3641 3925 4473 -585 1343 -1082 C
ATOM 1666 O PHE A 236 6.365 28.684 16.209 1.00 29.09 O
ANISOU 1666 O PHE A 236 3408 3538 4105 -591 1319 -1085 O
ATOM 1667 CB PHE A 236 4.465 30.055 14.093 1.00 25.03 C
ANISOU 1667 CB PHE A 236 2586 3226 3699 -508 1252 -1154 C
ATOM 1668 CG PHE A 236 4.257 31.024 12.967 1.00 29.69 C
ANISOU 1668 CG PHE A 236 3084 3897 4300 -410 1176 -1146 C
ATOM 1669 CD1 PHE A 236 3.487 32.161 13.159 1.00 25.92 C
ANISOU 1669 CD1 PHE A 236 2537 3459 3854 -377 1166 -1115 C
ATOM 1670 CD2 PHE A 236 4.851 30.822 11.731 1.00 29.10 C
ANISOU 1670 CD2 PHE A 236 3007 3855 4195 -345 1110 -1166 C
ATOM 1671 CE1 PHE A 236 3.295 33.075 12.133 1.00 24.43 C
ANISOU 1671 CE1 PHE A 236 2274 3338 3671 -285 1101 -1106 C
ATOM 1672 CE2 PHE A 236 4.662 31.734 10.695 1.00 23.83 C
ANISOU 1672 CE2 PHE A 236 2262 3262 3530 -257 1050 -1158 C
ATOM 1673 CZ PHE A 236 3.882 32.862 10.899 1.00 22.57 C
ANISOU 1673 CZ PHE A 236 2033 3136 3405 -228 1044 -1125 C
ATOM 1674 N ASN A 237 4.752 29.760 17.387 1.00 41.58 N
ANISOU 1674 N ASN A 237 4891 5162 5745 -653 1404 -1070 N
ATOM 1675 CA ASN A 237 4.686 28.818 18.493 1.00 37.91 C
ANISOU 1675 CA ASN A 237 4521 4622 5261 -765 1489 -1077 C
ATOM 1676 C ASN A 237 3.486 27.885 18.423 1.00 31.43 C
ANISOU 1676 C ASN A 237 3638 3811 4494 -887 1546 -1137 C
ATOM 1677 O ASN A 237 3.510 26.826 19.057 1.00 27.65 O
ANISOU 1677 O ASN A 237 3261 3252 3991 -984 1572 -1130 O
ATOM 1678 CB ASN A 237 4.640 29.575 19.832 1.00 40.74 C
ANISOU 1678 CB ASN A 237 4934 4953 5594 -766 1519 -1021 C
ATOM 1679 CG ASN A 237 5.891 29.369 20.666 1.00 56.54 C
ANISOU 1679 CG ASN A 237 7085 6874 7524 -759 1528 -975 C
ATOM 1680 OD1 ASN A 237 6.505 28.304 20.626 1.00 70.08 O
ANISOU 1680 OD1 ASN A 237 8890 8531 9205 -798 1550 -992 O
ATOM 1681 ND2 ASN A 237 6.271 30.387 21.428 1.00 64.73 N
ANISOU 1681 ND2 ASN A 237 8153 7906 8537 -707 1510 -921 N
ATOM 1682 N SER A 238 2.448 28.247 17.677 1.00 30.74 N
ANISOU 1682 N SER A 238 3406 3803 4470 -875 1516 -1177 N
ATOM 1683 CA SER A 238 1.188 27.524 17.666 1.00 31.82 C
ANISOU 1683 CA SER A 238 3465 3957 4667 -988 1553 -1230 C
ATOM 1684 C SER A 238 0.768 27.277 16.228 1.00 32.44 C
ANISOU 1684 C SER A 238 3429 4099 4798 -966 1475 -1289 C
ATOM 1685 O SER A 238 0.963 28.135 15.363 1.00 23.90 O
ANISOU 1685 O SER A 238 2277 3082 3720 -852 1413 -1290 O
ATOM 1686 CB SER A 238 0.096 28.312 18.394 1.00 39.77 C
ANISOU 1686 CB SER A 238 4412 5002 5699 -987 1577 -1221 C
ATOM 1687 OG SER A 238 0.659 29.347 19.183 1.00 55.72 O
ANISOU 1687 OG SER A 238 6497 7005 7671 -909 1577 -1159 O
ATOM 1688 N SER A 239 0.182 26.105 15.979 1.00 30.31 N
ANISOU 1688 N SER A 239 3155 3801 4559 -1069 1459 -1330 N
ATOM 1689 CA SER A 239 -0.248 25.767 14.627 1.00 32.16 C
ANISOU 1689 CA SER A 239 3300 4086 4833 -1047 1359 -1386 C
ATOM 1690 C SER A 239 -1.318 26.734 14.135 1.00 29.06 C
ANISOU 1690 C SER A 239 2718 3809 4513 -1008 1360 -1428 C
ATOM 1691 O SER A 239 -1.270 27.208 12.993 1.00 36.00 O
ANISOU 1691 O SER A 239 3529 4752 5397 -909 1267 -1445 O
ATOM 1692 CB SER A 239 -0.768 24.332 14.590 1.00 35.58 C
ANISOU 1692 CB SER A 239 3765 4459 5294 -1181 1350 -1427 C
ATOM 1693 OG SER A 239 0.063 23.461 15.337 1.00 47.37 O
ANISOU 1693 OG SER A 239 5438 5833 6727 -1233 1370 -1385 O
ATOM 1694 N ASN A 240 -2.292 27.041 14.997 1.00 28.21 N
ANISOU 1694 N ASN A 240 2551 3723 4446 -1065 1439 -1433 N
ATOM 1695 CA ASN A 240 -3.407 27.897 14.603 1.00 36.90 C
ANISOU 1695 CA ASN A 240 3507 4914 5601 -1007 1402 -1460 C
ATOM 1696 C ASN A 240 -2.935 29.301 14.242 1.00 31.03 C
ANISOU 1696 C ASN A 240 2748 4212 4829 -852 1350 -1416 C
ATOM 1697 O ASN A 240 -3.477 29.927 13.325 1.00 33.31 O
ANISOU 1697 O ASN A 240 2920 4577 5157 -778 1281 -1443 O
ATOM 1698 CB ASN A 240 -4.441 27.950 15.731 1.00 45.75 C
ANISOU 1698 CB ASN A 240 4614 6029 6740 -1074 1475 -1454 C
ATOM 1699 CG ASN A 240 -5.806 28.420 15.259 1.00 62.87 C
ANISOU 1699 CG ASN A 240 6616 8287 8984 -1054 1443 -1504 C
ATOM 1700 OD1 ASN A 240 -5.944 29.491 14.670 1.00 66.08 O
ANISOU 1700 OD1 ASN A 240 6945 8755 9406 -938 1384 -1501 O
ATOM 1701 ND2 ASN A 240 -6.827 27.610 15.516 1.00 71.67 N
ANISOU 1701 ND2 ASN A 240 7678 9408 10146 -1167 1479 -1548 N
ATOM 1702 N ILE A 241 -1.933 29.819 14.955 1.00 28.79 N
ANISOU 1702 N ILE A 241 2586 3875 4478 -803 1376 -1344 N
ATOM 1703 CA ILE A 241 -1.422 31.149 14.635 1.00 31.03 C
ANISOU 1703 CA ILE A 241 2872 4186 4732 -665 1320 -1291 C
ATOM 1704 C ILE A 241 -0.667 31.129 13.311 1.00 34.20 C
ANISOU 1704 C ILE A 241 3262 4619 5116 -590 1243 -1302 C
ATOM 1705 O ILE A 241 -0.767 32.067 12.510 1.00 28.17 O
ANISOU 1705 O ILE A 241 2436 3912 4358 -488 1176 -1291 O
ATOM 1706 CB ILE A 241 -0.548 31.675 15.788 1.00 27.13 C
ANISOU 1706 CB ILE A 241 2511 3625 4174 -642 1359 -1213 C
ATOM 1707 CG1 ILE A 241 -1.398 31.871 17.046 1.00 26.05 C
ANISOU 1707 CG1 ILE A 241 2372 3474 4050 -699 1430 -1209 C
ATOM 1708 CG2 ILE A 241 0.135 32.977 15.399 1.00 23.09 C
ANISOU 1708 CG2 ILE A 241 2012 3131 3628 -512 1296 -1153 C
ATOM 1709 CD1 ILE A 241 -0.651 32.493 18.204 1.00 24.14 C
ANISOU 1709 CD1 ILE A 241 2246 3177 3748 -673 1460 -1141 C
ATOM 1710 N MET A 242 0.095 30.062 13.053 1.00 34.82 N
ANISOU 1710 N MET A 242 3402 4659 5168 -637 1254 -1326 N
ATOM 1711 CA MET A 242 0.792 29.965 11.774 1.00 29.86 C
ANISOU 1711 CA MET A 242 2785 4055 4504 -556 1159 -1332 C
ATOM 1712 C MET A 242 -0.193 29.820 10.622 1.00 27.46 C
ANISOU 1712 C MET A 242 2356 3827 4252 -548 1079 -1395 C
ATOM 1713 O MET A 242 -0.040 30.467 9.580 1.00 23.98 O
ANISOU 1713 O MET A 242 1876 3444 3793 -446 999 -1390 O
ATOM 1714 CB MET A 242 1.775 28.797 11.779 1.00 22.97 C
ANISOU 1714 CB MET A 242 2058 3099 3571 -592 1133 -1319 C
ATOM 1715 CG MET A 242 2.431 28.587 10.425 1.00 27.31 C
ANISOU 1715 CG MET A 242 2631 3672 4074 -510 1024 -1327 C
ATOM 1716 SD MET A 242 3.803 27.415 10.444 1.00 36.01 S
ANISOU 1716 SD MET A 242 3905 4676 5100 -517 993 -1310 S
ATOM 1717 CE MET A 242 4.448 27.647 8.793 1.00 30.07 C
ANISOU 1717 CE MET A 242 3142 3988 4294 -397 882 -1319 C
ATOM 1718 N LYS A 243 -1.209 28.971 10.789 1.00 32.78 N
ANISOU 1718 N LYS A 243 2966 4501 4986 -659 1097 -1455 N
ATOM 1719 CA LYS A 243 -2.202 28.804 9.735 1.00 38.58 C
ANISOU 1719 CA LYS A 243 3571 5310 5776 -659 1015 -1523 C
ATOM 1720 C LYS A 243 -2.957 30.102 9.476 1.00 35.67 C
ANISOU 1720 C LYS A 243 3059 5033 5459 -575 1006 -1532 C
ATOM 1721 O LYS A 243 -3.203 30.463 8.319 1.00 30.15 O
ANISOU 1721 O LYS A 243 2295 4400 4763 -495 904 -1553 O
ATOM 1722 CB LYS A 243 -3.172 27.681 10.102 1.00 40.70 C
ANISOU 1722 CB LYS A 243 3793 5559 6111 -808 1048 -1585 C
ATOM 1723 CG LYS A 243 -4.261 27.458 9.066 1.00 41.39 C
ANISOU 1723 CG LYS A 243 3737 5724 6265 -819 960 -1665 C
ATOM 1724 CD LYS A 243 -5.103 26.236 9.394 1.00 41.06 C
ANISOU 1724 CD LYS A 243 3662 5651 6287 -980 989 -1726 C
ATOM 1725 CE LYS A 243 -6.178 26.011 8.343 1.00 46.95 C
ANISOU 1725 CE LYS A 243 4258 6476 7103 -992 891 -1812 C
ATOM 1726 NZ LYS A 243 -6.256 24.589 7.918 1.00 50.83 N
ANISOU 1726 NZ LYS A 243 4802 6912 7597 -1096 837 -1862 N
ATOM 1727 N THR A 244 -3.327 30.822 10.541 1.00 36.34 N
ANISOU 1727 N THR A 244 3141 5106 5562 -579 1082 -1495 N
ATOM 1728 CA THR A 244 -4.073 32.067 10.370 1.00 34.49 C
ANISOU 1728 CA THR A 244 2824 4926 5356 -488 1042 -1478 C
ATOM 1729 C THR A 244 -3.232 33.126 9.666 1.00 35.31 C
ANISOU 1729 C THR A 244 2963 5048 5406 -349 980 -1423 C
ATOM 1730 O THR A 244 -3.750 33.896 8.848 1.00 38.32 O
ANISOU 1730 O THR A 244 3254 5493 5811 -263 907 -1435 O
ATOM 1731 CB THR A 244 -4.556 32.591 11.725 1.00 30.75 C
ANISOU 1731 CB THR A 244 2377 4417 4889 -515 1122 -1437 C
ATOM 1732 OG1 THR A 244 -5.446 31.640 12.324 1.00 36.74 O
ANISOU 1732 OG1 THR A 244 3097 5166 5695 -642 1180 -1488 O
ATOM 1733 CG2 THR A 244 -5.292 33.910 11.555 1.00 27.68 C
ANISOU 1733 CG2 THR A 244 1903 4081 4532 -415 1083 -1423 C
ATOM 1734 N CYS A 245 -1.932 33.179 9.966 1.00 26.43 N
ANISOU 1734 N CYS A 245 1972 3865 4206 -326 1005 -1361 N
ATOM 1735 CA CYS A 245 -1.080 34.202 9.365 1.00 30.59 C
ANISOU 1735 CA CYS A 245 2546 4401 4677 -205 953 -1299 C
ATOM 1736 C CYS A 245 -0.739 33.876 7.915 1.00 33.72 C
ANISOU 1736 C CYS A 245 2905 4856 5053 -151 875 -1343 C
ATOM 1737 O CYS A 245 -0.647 34.782 7.079 1.00 33.91 O
ANISOU 1737 O CYS A 245 2900 4926 5058 -47 810 -1321 O
ATOM 1738 CB CYS A 245 0.198 34.371 10.184 1.00 28.66 C
ANISOU 1738 CB CYS A 245 2453 4077 4360 -201 999 -1218 C
ATOM 1739 SG CYS A 245 -0.035 35.224 11.753 1.00 27.37 S
ANISOU 1739 SG CYS A 245 2339 3860 4200 -216 1065 -1153 S
ATOM 1740 N LEU A 246 -0.541 32.591 7.599 1.00 28.14 N
ANISOU 1740 N LEU A 246 2240 4127 4324 -219 851 -1380 N
ATOM 1741 CA LEU A 246 -0.197 32.207 6.231 1.00 28.60 C
ANISOU 1741 CA LEU A 246 2324 4215 4326 -169 740 -1392 C
ATOM 1742 C LEU A 246 -1.321 32.534 5.258 1.00 32.37 C
ANISOU 1742 C LEU A 246 2670 4778 4850 -129 651 -1443 C
ATOM 1743 O LEU A 246 -1.069 32.824 4.081 1.00 37.13 O
ANISOU 1743 O LEU A 246 3283 5424 5398 -45 556 -1433 O
ATOM 1744 CB LEU A 246 0.135 30.718 6.168 1.00 32.79 C
ANISOU 1744 CB LEU A 246 2933 4694 4832 -255 728 -1428 C
ATOM 1745 CG LEU A 246 1.465 30.285 6.778 1.00 31.84 C
ANISOU 1745 CG LEU A 246 2962 4491 4645 -268 778 -1379 C
ATOM 1746 CD1 LEU A 246 1.745 28.844 6.414 1.00 29.99 C
ANISOU 1746 CD1 LEU A 246 2799 4212 4385 -327 737 -1422 C
ATOM 1747 CD2 LEU A 246 2.600 31.185 6.323 1.00 22.39 C
ANISOU 1747 CD2 LEU A 246 1827 3307 3372 -156 758 -1312 C
ATOM 1748 N GLN A 247 -2.570 32.479 5.728 1.00 31.95 N
ANISOU 1748 N GLN A 247 2491 4754 4895 -189 679 -1499 N
ATOM 1749 CA GLN A 247 -3.709 32.771 4.863 1.00 29.05 C
ANISOU 1749 CA GLN A 247 1983 4471 4585 -151 588 -1555 C
ATOM 1750 C GLN A 247 -3.667 34.205 4.350 1.00 30.16 C
ANISOU 1750 C GLN A 247 2093 4657 4709 -13 540 -1509 C
ATOM 1751 O GLN A 247 -4.033 34.471 3.198 1.00 40.22 O
ANISOU 1751 O GLN A 247 3321 5991 5969 59 426 -1527 O
ATOM 1752 CB GLN A 247 -5.014 32.509 5.613 1.00 36.00 C
ANISOU 1752 CB GLN A 247 2723 5374 5581 -243 645 -1624 C
ATOM 1753 CG GLN A 247 -5.628 31.150 5.320 1.00 49.26 C
ANISOU 1753 CG GLN A 247 4365 7055 7297 -357 610 -1702 C
ATOM 1754 CD GLN A 247 -6.384 30.587 6.502 1.00 55.26 C
ANISOU 1754 CD GLN A 247 5062 7793 8144 -495 724 -1743 C
ATOM 1755 OE1 GLN A 247 -6.729 31.310 7.435 1.00 51.68 O
ANISOU 1755 OE1 GLN A 247 4604 7324 7709 -485 799 -1703 O
ATOM 1756 NE2 GLN A 247 -6.637 29.286 6.474 1.00 60.68 N
ANISOU 1756 NE2 GLN A 247 5761 8447 8847 -616 718 -1793 N
ATOM 1757 N ASN A 248 -3.227 35.141 5.187 1.00 27.22 N
ANISOU 1757 N ASN A 248 1755 4253 4335 24 622 -1449 N
ATOM 1758 CA ASN A 248 -3.200 36.554 4.835 1.00 34.83 C
ANISOU 1758 CA ASN A 248 2698 5244 5293 148 585 -1402 C
ATOM 1759 C ASN A 248 -1.927 36.955 4.097 1.00 33.41 C
ANISOU 1759 C ASN A 248 2650 5044 4999 226 540 -1323 C
ATOM 1760 O ASN A 248 -1.690 38.151 3.896 1.00 35.63 O
ANISOU 1760 O ASN A 248 2945 5329 5263 321 522 -1268 O
ATOM 1761 CB ASN A 248 -3.388 37.410 6.089 1.00 38.68 C
ANISOU 1761 CB ASN A 248 3219 5674 5805 142 665 -1341 C
ATOM 1762 CG ASN A 248 -4.853 37.611 6.437 1.00 44.11 C
ANISOU 1762 CG ASN A 248 3786 6392 6582 122 661 -1387 C
ATOM 1763 OD1 ASN A 248 -5.699 37.734 5.551 1.00 46.76 O
ANISOU 1763 OD1 ASN A 248 4007 6798 6962 169 572 -1440 O
ATOM 1764 ND2 ASN A 248 -5.160 37.647 7.728 1.00 46.96 N
ANISOU 1764 ND2 ASN A 248 4173 6704 6965 57 752 -1369 N
ATOM 1765 N LEU A 249 -1.099 35.986 3.694 1.00 29.77 N
ANISOU 1765 N LEU A 249 2288 4560 4464 187 525 -1319 N
ATOM 1766 CA LEU A 249 -0.098 36.233 2.663 1.00 27.34 C
ANISOU 1766 CA LEU A 249 2078 4261 4049 262 462 -1265 C
ATOM 1767 C LEU A 249 -0.722 36.322 1.275 1.00 28.46 C
ANISOU 1767 C LEU A 249 2167 4477 4169 325 332 -1294 C
ATOM 1768 O LEU A 249 0.008 36.466 0.291 1.00 30.29 O
ANISOU 1768 O LEU A 249 2478 4726 4303 385 274 -1256 O
ATOM 1769 CB LEU A 249 0.972 35.134 2.676 1.00 30.01 C
ANISOU 1769 CB LEU A 249 2531 4554 4316 206 487 -1262 C
ATOM 1770 CG LEU A 249 1.844 34.950 3.924 1.00 31.31 C
ANISOU 1770 CG LEU A 249 2777 4641 4477 153 598 -1226 C
ATOM 1771 CD1 LEU A 249 2.890 33.859 3.711 1.00 31.83 C
ANISOU 1771 CD1 LEU A 249 2953 4670 4471 119 596 -1229 C
ATOM 1772 CD2 LEU A 249 2.508 36.257 4.314 1.00 28.69 C
ANISOU 1772 CD2 LEU A 249 2483 4291 4127 220 641 -1146 C
ATOM 1773 N ALA A 250 -2.051 36.249 1.190 1.00 32.82 N
ANISOU 1773 N ALA A 250 2587 5075 4808 313 287 -1363 N
ATOM 1774 CA ALA A 250 -2.753 36.182 -0.086 1.00 29.78 C
ANISOU 1774 CA ALA A 250 2144 4762 4410 363 153 -1405 C
ATOM 1775 C ALA A 250 -2.453 37.398 -0.952 1.00 30.08 C
ANISOU 1775 C ALA A 250 2219 4828 4381 490 81 -1335 C
ATOM 1776 O ALA A 250 -2.431 38.535 -0.469 1.00 32.61 O
ANISOU 1776 O ALA A 250 2531 5130 4730 546 118 -1281 O
ATOM 1777 CB ALA A 250 -4.258 36.070 0.158 1.00 28.94 C
ANISOU 1777 CB ALA A 250 1868 4699 4426 331 127 -1489 C
ATOM 1778 N GLY A 251 -2.236 37.152 -2.244 1.00 28.22 N
ANISOU 1778 N GLY A 251 2033 4635 4053 535 -23 -1336 N
ATOM 1779 CA GLY A 251 -1.866 38.177 -3.189 1.00 30.21 C
ANISOU 1779 CA GLY A 251 2345 4914 4221 647 -94 -1264 C
ATOM 1780 C GLY A 251 -0.373 38.346 -3.363 1.00 29.37 C
ANISOU 1780 C GLY A 251 2389 4772 3998 662 -41 -1180 C
ATOM 1781 O GLY A 251 0.058 39.013 -4.311 1.00 32.75 O
ANISOU 1781 O GLY A 251 2886 5226 4332 741 -100 -1120 O
ATOM 1782 N LEU A 252 0.421 37.740 -2.488 1.00 28.52 N
ANISOU 1782 N LEU A 252 2333 4609 3893 586 66 -1176 N
ATOM 1783 CA LEU A 252 1.865 37.908 -2.527 1.00 26.88 C
ANISOU 1783 CA LEU A 252 2254 4369 3590 597 125 -1102 C
ATOM 1784 C LEU A 252 2.479 37.123 -3.684 1.00 31.38 C
ANISOU 1784 C LEU A 252 2901 4976 4044 606 69 -1119 C
ATOM 1785 O LEU A 252 2.013 36.035 -4.040 1.00 30.00 O
ANISOU 1785 O LEU A 252 2699 4824 3875 564 21 -1201 O
ATOM 1786 CB LEU A 252 2.449 37.453 -1.194 1.00 25.31 C
ANISOU 1786 CB LEU A 252 2079 4100 3438 518 246 -1101 C
ATOM 1787 CG LEU A 252 3.942 37.233 -1.012 1.00 26.97 C
ANISOU 1787 CG LEU A 252 2406 4271 3571 504 314 -1052 C
ATOM 1788 CD1 LEU A 252 4.687 38.553 -1.130 1.00 22.87 C
ANISOU 1788 CD1 LEU A 252 1941 3743 3006 571 336 -954 C
ATOM 1789 CD2 LEU A 252 4.216 36.559 0.329 1.00 37.66 C
ANISOU 1789 CD2 LEU A 252 3768 5556 4984 418 411 -1074 C
ATOM 1790 N HIS A 253 3.532 37.688 -4.276 1.00 35.87 N
ANISOU 1790 N HIS A 253 3568 5553 4508 658 78 -1043 N
ATOM 1791 CA HIS A 253 4.290 37.063 -5.357 1.00 34.27 C
ANISOU 1791 CA HIS A 253 3450 5389 4181 673 43 -1051 C
ATOM 1792 C HIS A 253 5.751 37.024 -4.925 1.00 32.75 C
ANISOU 1792 C HIS A 253 3347 5158 3940 654 145 -999 C
ATOM 1793 O HIS A 253 6.423 38.061 -4.900 1.00 31.45 O
ANISOU 1793 O HIS A 253 3227 4983 3740 691 184 -911 O
ATOM 1794 CB HIS A 253 4.114 37.836 -6.665 1.00 34.72 C
ANISOU 1794 CB HIS A 253 3536 5510 4144 759 -51 -1009 C
ATOM 1795 CG HIS A 253 4.692 37.152 -7.868 1.00 48.06 C
ANISOU 1795 CG HIS A 253 5306 7254 5702 777 -96 -1032 C
ATOM 1796 ND1 HIS A 253 3.998 37.026 -9.052 1.00 51.81 N
ANISOU 1796 ND1 HIS A 253 5775 7796 6114 822 -217 -1068 N
ATOM 1797 CD2 HIS A 253 5.899 36.573 -8.077 1.00 51.54 C
ANISOU 1797 CD2 HIS A 253 5832 7694 6057 760 -38 -1028 C
ATOM 1798 CE1 HIS A 253 4.749 36.391 -9.935 1.00 51.96 C
ANISOU 1798 CE1 HIS A 253 5879 7853 6011 830 -227 -1086 C
ATOM 1799 NE2 HIS A 253 5.907 36.106 -9.368 1.00 48.96 N
ANISOU 1799 NE2 HIS A 253 5551 7434 5617 794 -117 -1064 N
ATOM 1800 N VAL A 254 6.237 35.841 -4.560 1.00 30.71 N
ANISOU 1800 N VAL A 254 3113 4872 3683 596 185 -1055 N
ATOM 1801 CA VAL A 254 7.605 35.671 -4.087 1.00 28.92 C
ANISOU 1801 CA VAL A 254 2960 4607 3421 578 275 -1020 C
ATOM 1802 C VAL A 254 8.339 34.741 -5.039 1.00 23.32 C
ANISOU 1802 C VAL A 254 2318 3935 2609 590 252 -1061 C
ATOM 1803 O VAL A 254 7.780 33.734 -5.488 1.00 33.61 O
ANISOU 1803 O VAL A 254 3607 5254 3908 571 191 -1145 O
ATOM 1804 CB VAL A 254 7.660 35.121 -2.649 1.00 36.36 C
ANISOU 1804 CB VAL A 254 3883 5471 4460 505 350 -1044 C
ATOM 1805 CG1 VAL A 254 9.077 34.860 -2.255 1.00 46.56 C
ANISOU 1805 CG1 VAL A 254 5250 6728 5711 495 425 -1017 C
ATOM 1806 CG2 VAL A 254 7.114 36.114 -1.690 1.00 56.33 C
ANISOU 1806 CG2 VAL A 254 6358 7966 7078 499 388 -1001 C
ATOM 1807 N HIS A 255 9.592 35.082 -5.343 1.00 23.61 N
ANISOU 1807 N HIS A 255 2424 3985 2562 619 302 -1007 N
ATOM 1808 CA HIS A 255 10.454 34.148 -6.055 1.00 26.86 C
ANISOU 1808 CA HIS A 255 2897 4426 2882 629 302 -1052 C
ATOM 1809 C HIS A 255 10.825 32.964 -5.168 1.00 23.94 C
ANISOU 1809 C HIS A 255 2536 3991 2571 574 343 -1115 C
ATOM 1810 O HIS A 255 10.791 31.810 -5.610 1.00 22.97 O
ANISOU 1810 O HIS A 255 2435 3873 2422 565 304 -1198 O
ATOM 1811 CB HIS A 255 11.713 34.860 -6.546 1.00 25.41 C
ANISOU 1811 CB HIS A 255 2774 4278 2603 670 357 -977 C
ATOM 1812 CG HIS A 255 12.607 33.989 -7.373 1.00 27.17 C
ANISOU 1812 CG HIS A 255 3054 4544 2724 690 362 -1027 C
ATOM 1813 ND1 HIS A 255 12.251 33.540 -8.626 1.00 24.29 N
ANISOU 1813 ND1 HIS A 255 2715 4248 2267 724 288 -1077 N
ATOM 1814 CD2 HIS A 255 13.835 33.471 -7.121 1.00 22.96 C
ANISOU 1814 CD2 HIS A 255 2557 3998 2169 686 430 -1040 C
ATOM 1815 CE1 HIS A 255 13.223 32.789 -9.113 1.00 28.34 C
ANISOU 1815 CE1 HIS A 255 3278 4788 2702 740 317 -1121 C
ATOM 1816 NE2 HIS A 255 14.195 32.730 -8.220 1.00 27.00 N
ANISOU 1816 NE2 HIS A 255 3111 4570 2576 719 403 -1100 N
ATOM 1817 N ARG A 256 11.183 33.228 -3.912 1.00 22.38 N
ANISOU 1817 N ARG A 256 2329 3726 2449 539 416 -1078 N
ATOM 1818 CA ARG A 256 11.696 32.193 -3.019 1.00 22.71 C
ANISOU 1818 CA ARG A 256 2395 3698 2536 493 457 -1123 C
ATOM 1819 C ARG A 256 11.126 32.373 -1.619 1.00 25.76 C
ANISOU 1819 C ARG A 256 2742 4011 3034 435 496 -1108 C
ATOM 1820 O ARG A 256 11.435 33.360 -0.945 1.00 21.83 O
ANISOU 1820 O ARG A 256 2237 3494 2564 439 549 -1037 O
ATOM 1821 CB ARG A 256 13.226 32.227 -2.977 1.00 20.67 C
ANISOU 1821 CB ARG A 256 2192 3440 2223 520 519 -1092 C
ATOM 1822 CG ARG A 256 13.827 31.115 -2.144 1.00 26.12 C
ANISOU 1822 CG ARG A 256 2916 4058 2952 486 548 -1141 C
ATOM 1823 CD ARG A 256 15.343 31.054 -2.250 1.00 26.24 C
ANISOU 1823 CD ARG A 256 2987 4062 2922 510 582 -1095 C
ATOM 1824 NE ARG A 256 15.826 31.114 -3.627 1.00 39.26 N
ANISOU 1824 NE ARG A 256 4655 5794 4467 563 564 -1101 N
ATOM 1825 CZ ARG A 256 16.544 32.121 -4.117 1.00 38.33 C
ANISOU 1825 CZ ARG A 256 4545 5724 4297 591 598 -1024 C
ATOM 1826 NH1 ARG A 256 16.864 33.146 -3.339 1.00 30.82 N
ANISOU 1826 NH1 ARG A 256 3580 4738 3391 572 647 -939 N
ATOM 1827 NH2 ARG A 256 16.952 32.101 -5.379 1.00 40.53 N
ANISOU 1827 NH2 ARG A 256 4846 6079 4473 633 587 -1033 N
ATOM 1828 N LEU A 257 10.317 31.413 -1.177 1.00 22.82 N
ANISOU 1828 N LEU A 257 2349 3597 2724 378 473 -1175 N
ATOM 1829 CA LEU A 257 9.736 31.401 0.160 1.00 23.27 C
ANISOU 1829 CA LEU A 257 2375 3586 2882 312 517 -1171 C
ATOM 1830 C LEU A 257 10.426 30.334 0.999 1.00 23.52 C
ANISOU 1830 C LEU A 257 2468 3538 2930 267 554 -1199 C
ATOM 1831 O LEU A 257 10.493 29.170 0.592 1.00 22.68 O
ANISOU 1831 O LEU A 257 2396 3417 2804 253 516 -1266 O
ATOM 1832 CB LEU A 257 8.230 31.132 0.096 1.00 21.19 C
ANISOU 1832 CB LEU A 257 2036 3333 2682 269 468 -1223 C
ATOM 1833 CG LEU A 257 7.479 31.054 1.426 1.00 23.52 C
ANISOU 1833 CG LEU A 257 2289 3568 3080 193 519 -1228 C
ATOM 1834 CD1 LEU A 257 7.523 32.399 2.129 1.00 21.17 C
ANISOU 1834 CD1 LEU A 257 1964 3268 2811 216 576 -1153 C
ATOM 1835 CD2 LEU A 257 6.042 30.597 1.215 1.00 21.94 C
ANISOU 1835 CD2 LEU A 257 2008 3388 2941 145 468 -1295 C
ATOM 1836 N ILE A 258 10.935 30.727 2.165 1.00 19.36 N
ANISOU 1836 N ILE A 258 1960 2956 2439 247 622 -1151 N
ATOM 1837 CA ILE A 258 11.649 29.822 3.061 1.00 19.01 C
ANISOU 1837 CA ILE A 258 1983 2831 2409 210 655 -1167 C
ATOM 1838 C ILE A 258 10.856 29.720 4.357 1.00 20.53 C
ANISOU 1838 C ILE A 258 2160 2958 2684 131 696 -1165 C
ATOM 1839 O ILE A 258 10.561 30.741 4.991 1.00 23.00 O
ANISOU 1839 O ILE A 258 2435 3274 3031 127 739 -1116 O
ATOM 1840 CB ILE A 258 13.086 30.297 3.325 1.00 19.73 C
ANISOU 1840 CB ILE A 258 2127 2909 2462 253 686 -1098 C
ATOM 1841 CG1 ILE A 258 13.825 30.496 2.001 1.00 21.28 C
ANISOU 1841 CG1 ILE A 258 2333 3178 2576 324 655 -1089 C
ATOM 1842 CG2 ILE A 258 13.827 29.291 4.191 1.00 18.12 C
ANISOU 1842 CG2 ILE A 258 1999 2617 2270 224 692 -1103 C
ATOM 1843 CD1 ILE A 258 15.247 31.008 2.162 1.00 29.36 C
ANISOU 1843 CD1 ILE A 258 3403 4186 3567 355 676 -1000 C
ATOM 1844 N LEU A 259 10.513 28.492 4.748 1.00 22.97 N
ANISOU 1844 N LEU A 259 2502 3205 3020 67 685 -1219 N
ATOM 1845 CA LEU A 259 9.664 28.229 5.901 1.00 19.42 C
ANISOU 1845 CA LEU A 259 2041 2695 2641 -21 726 -1224 C
ATOM 1846 C LEU A 259 10.303 27.144 6.760 1.00 31.53 C
ANISOU 1846 C LEU A 259 3674 4129 4175 -66 743 -1235 C
ATOM 1847 O LEU A 259 11.043 26.296 6.256 1.00 20.45 O
ANISOU 1847 O LEU A 259 2333 2705 2733 -37 702 -1268 O
ATOM 1848 CB LEU A 259 8.257 27.792 5.453 1.00 23.52 C
ANISOU 1848 CB LEU A 259 2489 3241 3207 -75 688 -1282 C
ATOM 1849 CG LEU A 259 7.008 28.423 6.076 1.00 38.27 C
ANISOU 1849 CG LEU A 259 4266 5126 5148 -127 728 -1276 C
ATOM 1850 CD1 LEU A 259 7.073 29.931 5.988 1.00 41.81 C
ANISOU 1850 CD1 LEU A 259 4661 5634 5592 -57 748 -1218 C
ATOM 1851 CD2 LEU A 259 5.741 27.900 5.396 1.00 38.67 C
ANISOU 1851 CD2 LEU A 259 4238 5214 5240 -171 673 -1345 C
ATOM 1852 N GLY A 260 10.020 27.173 8.056 1.00 19.19 N
ANISOU 1852 N GLY A 260 2132 2506 2655 -131 803 -1210 N
ATOM 1853 CA GLY A 260 10.482 26.128 8.946 1.00 24.92 C
ANISOU 1853 CA GLY A 260 2959 3129 3380 -182 816 -1217 C
ATOM 1854 C GLY A 260 10.734 26.662 10.343 1.00 20.96 C
ANISOU 1854 C GLY A 260 2494 2579 2891 -210 887 -1160 C
ATOM 1855 O GLY A 260 10.382 27.791 10.672 1.00 21.63 O
ANISOU 1855 O GLY A 260 2518 2707 2994 -202 931 -1124 O
ATOM 1856 N GLU A 261 11.361 25.811 11.156 1.00 24.10 N
ANISOU 1856 N GLU A 261 3359 3148 2649 235 1121 -1008 N
ATOM 1857 CA GLU A 261 11.632 26.109 12.556 1.00 25.97 C
ANISOU 1857 CA GLU A 261 3667 3373 2828 318 1185 -983 C
ATOM 1858 C GLU A 261 13.105 25.889 12.865 1.00 27.70 C
ANISOU 1858 C GLU A 261 4064 3501 2962 439 1147 -912 C
ATOM 1859 O GLU A 261 13.902 25.620 11.961 1.00 23.52 O
ANISOU 1859 O GLU A 261 3583 2926 2428 462 1068 -884 O
ATOM 1860 CB GLU A 261 10.772 25.227 13.468 1.00 27.23 C
ANISOU 1860 CB GLU A 261 3892 3507 2949 205 1361 -995 C
ATOM 1861 CG GLU A 261 9.371 24.971 12.944 1.00 33.51 C
ANISOU 1861 CG GLU A 261 4541 4363 3829 45 1416 -1065 C
ATOM 1862 CD GLU A 261 8.524 24.165 13.906 1.00 41.22 C
ANISOU 1862 CD GLU A 261 5573 5314 4775 -68 1601 -1074 C
ATOM 1863 OE1 GLU A 261 8.449 22.930 13.746 1.00 37.42 O
ANISOU 1863 OE1 GLU A 261 5209 4744 4266 -179 1690 -1056 O
ATOM 1864 OE2 GLU A 261 7.934 24.770 14.827 1.00 43.44 O
ANISOU 1864 OE2 GLU A 261 5782 5663 5062 -45 1663 -1098 O
ATOM 1865 N PHE A 262 13.469 25.992 14.143 1.00 24.31 N
ANISOU 1865 N PHE A 262 3724 3050 2464 518 1192 -881 N
ATOM 1866 CA PHE A 262 14.809 25.683 14.618 1.00 22.96 C
ANISOU 1866 CA PHE A 262 3678 2809 2238 602 1109 -793 C
ATOM 1867 C PHE A 262 14.717 24.680 15.758 1.00 30.69 C
ANISOU 1867 C PHE A 262 4805 3723 3132 561 1221 -745 C
ATOM 1868 O PHE A 262 13.765 24.695 16.543 1.00 25.06 O
ANISOU 1868 O PHE A 262 4071 3047 2405 515 1332 -772 O
ATOM 1869 CB PHE A 262 15.550 26.942 15.096 1.00 22.05 C
ANISOU 1869 CB PHE A 262 3478 2741 2161 724 975 -779 C
ATOM 1870 CG PHE A 262 15.695 27.996 14.043 1.00 26.13 C
ANISOU 1870 CG PHE A 262 3854 3307 2769 767 863 -810 C
ATOM 1871 CD1 PHE A 262 16.715 27.924 13.109 1.00 20.11 C
ANISOU 1871 CD1 PHE A 262 3113 2501 2028 792 763 -764 C
ATOM 1872 CD2 PHE A 262 14.813 29.060 13.986 1.00 23.80 C
ANISOU 1872 CD2 PHE A 262 3402 3099 2540 783 860 -876 C
ATOM 1873 CE1 PHE A 262 16.848 28.893 12.138 1.00 19.30 C
ANISOU 1873 CE1 PHE A 262 2887 2439 2006 829 663 -775 C
ATOM 1874 CE2 PHE A 262 14.943 30.032 13.018 1.00 25.04 C
ANISOU 1874 CE2 PHE A 262 3433 3294 2785 825 746 -882 C
ATOM 1875 CZ PHE A 262 15.964 29.949 12.094 1.00 19.39 C
ANISOU 1875 CZ PHE A 262 2750 2533 2084 846 649 -828 C
ATOM 1876 N LYS A 263 15.722 23.805 15.842 1.00 23.92 N
ANISOU 1876 N LYS A 263 4095 2769 2223 579 1194 -670 N
ATOM 1877 CA LYS A 263 15.755 22.818 16.918 1.00 27.93 C
ANISOU 1877 CA LYS A 263 4763 3201 2650 555 1294 -613 C
ATOM 1878 C LYS A 263 15.864 23.474 18.287 1.00 27.29 C
ANISOU 1878 C LYS A 263 4671 3161 2537 638 1282 -596 C
ATOM 1879 O LYS A 263 15.329 22.949 19.271 1.00 29.64 O
ANISOU 1879 O LYS A 263 5051 3436 2775 603 1400 -578 O
ATOM 1880 CB LYS A 263 16.921 21.852 16.715 1.00 24.72 C
ANISOU 1880 CB LYS A 263 4508 2683 2201 581 1249 -536 C
ATOM 1881 CG LYS A 263 16.704 20.802 15.641 1.00 25.51 C
ANISOU 1881 CG LYS A 263 4675 2713 2305 478 1305 -546 C
ATOM 1882 CD LYS A 263 17.976 19.994 15.438 1.00 24.62 C
ANISOU 1882 CD LYS A 263 4695 2501 2159 526 1239 -470 C
ATOM 1883 CE LYS A 263 17.714 18.705 14.677 1.00 33.50 C
ANISOU 1883 CE LYS A 263 5931 3531 3267 417 1323 -474 C
ATOM 1884 NZ LYS A 263 18.765 17.684 14.956 1.00 46.10 N
ANISOU 1884 NZ LYS A 263 7698 5009 4808 460 1308 -390 N
ATOM 1885 N ASP A 264 16.560 24.608 18.377 1.00 30.55 N
ANISOU 1885 N ASP A 264 4986 3628 2991 741 1143 -602 N
ATOM 1886 CA ASP A 264 16.812 25.273 19.650 1.00 29.92 C
ANISOU 1886 CA ASP A 264 4899 3581 2887 822 1113 -590 C
ATOM 1887 C ASP A 264 15.802 26.380 19.942 1.00 31.32 C
ANISOU 1887 C ASP A 264 4921 3869 3110 822 1134 -670 C
ATOM 1888 O ASP A 264 16.123 27.342 20.649 1.00 31.16 O
ANISOU 1888 O ASP A 264 4842 3890 3109 898 1061 -680 O
ATOM 1889 CB ASP A 264 18.236 25.828 19.686 1.00 31.56 C
ANISOU 1889 CB ASP A 264 5103 3769 3121 922 957 -545 C
ATOM 1890 CG ASP A 264 18.481 26.878 18.620 1.00 36.43 C
ANISOU 1890 CG ASP A 264 5565 4437 3841 938 843 -581 C
ATOM 1891 OD1 ASP A 264 18.047 26.672 17.468 1.00 37.48 O
ANISOU 1891 OD1 ASP A 264 5655 4577 4010 880 860 -612 O
ATOM 1892 OD2 ASP A 264 19.102 27.914 18.933 1.00 39.36 O
ANISOU 1892 OD2 ASP A 264 5863 4835 4257 1006 739 -576 O
ATOM 1893 N GLU A 265 14.586 26.263 19.413 1.00 32.86 N
ANISOU 1893 N GLU A 265 5047 4110 3329 735 1233 -728 N
ATOM 1894 CA GLU A 265 13.505 27.191 19.711 1.00 34.45 C
ANISOU 1894 CA GLU A 265 5099 4419 3571 730 1271 -806 C
ATOM 1895 C GLU A 265 12.223 26.399 19.931 1.00 44.03 C
ANISOU 1895 C GLU A 265 6335 5639 4754 612 1454 -823 C
ATOM 1896 O GLU A 265 12.066 25.293 19.404 1.00 48.63 O
ANISOU 1896 O GLU A 265 7009 6149 5321 513 1537 -799 O
ATOM 1897 CB GLU A 265 13.295 28.212 18.578 1.00 33.42 C
ANISOU 1897 CB GLU A 265 4796 4354 3548 747 1182 -871 C
ATOM 1898 CG GLU A 265 14.471 29.141 18.308 1.00 31.86 C
ANISOU 1898 CG GLU A 265 4555 4139 3412 836 1012 -849 C
ATOM 1899 CD GLU A 265 14.582 30.268 19.317 1.00 38.64 C
ANISOU 1899 CD GLU A 265 5350 5031 4301 903 961 -861 C
ATOM 1900 OE1 GLU A 265 15.699 30.793 19.501 1.00 42.62 O
ANISOU 1900 OE1 GLU A 265 5872 5493 4827 969 843 -810 O
ATOM 1901 OE2 GLU A 265 13.553 30.637 19.923 1.00 38.88 O
ANISOU 1901 OE2 GLU A 265 5311 5129 4334 887 1040 -920 O
ATOM 1902 N ARG A 266 11.309 26.966 20.719 1.00 47.59 N
ANISOU 1902 N ARG A 266 6698 6175 5208 612 1520 -868 N
ATOM 1903 CA ARG A 266 10.024 26.315 20.953 1.00 49.30 C
ANISOU 1903 CA ARG A 266 6906 6405 5419 482 1700 -887 C
ATOM 1904 C ARG A 266 9.292 26.121 19.631 1.00 43.78 C
ANISOU 1904 C ARG A 266 6101 5717 4814 360 1738 -945 C
ATOM 1905 O ARG A 266 9.167 27.054 18.835 1.00 35.38 O
ANISOU 1905 O ARG A 266 4883 4721 3838 393 1644 -1005 O
ATOM 1906 CB ARG A 266 9.176 27.142 21.919 1.00 54.14 C
ANISOU 1906 CB ARG A 266 7410 7126 6036 514 1744 -932 C
ATOM 1907 CG ARG A 266 9.883 27.551 23.206 1.00 63.72 C
ANISOU 1907 CG ARG A 266 8694 8347 7168 636 1687 -902 C
ATOM 1908 CD ARG A 266 9.412 26.746 24.410 1.00 71.26 C
ANISOU 1908 CD ARG A 266 9767 9279 8030 589 1839 -857 C
ATOM 1909 NE ARG A 266 9.689 27.443 25.664 1.00 74.23 N
ANISOU 1909 NE ARG A 266 10149 9705 8351 696 1797 -863 N
ATOM 1910 CZ ARG A 266 9.687 26.864 26.859 1.00 78.24 C
ANISOU 1910 CZ ARG A 266 10787 10182 8757 701 1886 -811 C
ATOM 1911 NH1 ARG A 266 9.435 25.566 26.971 1.00 79.96 N
ANISOU 1911 NH1 ARG A 266 11145 10313 8923 606 2023 -744 N
ATOM 1912 NH2 ARG A 266 9.947 27.579 27.944 1.00 77.74 N
ANISOU 1912 NH2 ARG A 266 10720 10167 8651 798 1840 -828 N
ATOM 1913 N ASN A 267 8.804 24.907 19.400 1.00 36.91 N
ANISOU 1913 N ASN A 267 5310 4780 3935 212 1872 -934 N
ATOM 1914 CA ASN A 267 8.338 24.501 18.084 1.00 39.83 C
ANISOU 1914 CA ASN A 267 5606 5142 4384 84 1894 -992 C
ATOM 1915 C ASN A 267 6.833 24.264 18.065 1.00 40.07 C
ANISOU 1915 C ASN A 267 5504 5234 4487 -80 2039 -1066 C
ATOM 1916 O ASN A 267 6.176 24.152 19.105 1.00 41.69 O
ANISOU 1916 O ASN A 267 5714 5461 4665 -110 2148 -1053 O
ATOM 1917 CB ASN A 267 9.065 23.235 17.622 1.00 39.25 C
ANISOU 1917 CB ASN A 267 5722 4934 4256 35 1914 -933 C
ATOM 1918 CG ASN A 267 10.533 23.477 17.337 1.00 37.98 C
ANISOU 1918 CG ASN A 267 5651 4724 4055 182 1751 -873 C
ATOM 1919 OD1 ASN A 267 10.904 24.496 16.755 1.00 44.67 O
ANISOU 1919 OD1 ASN A 267 6386 5632 4953 272 1617 -904 O
ATOM 1920 ND2 ASN A 267 11.380 22.539 17.748 1.00 31.22 N
ANISOU 1920 ND2 ASN A 267 4991 3756 3116 206 1758 -787 N
ATOM 1921 N LEU A 268 6.298 24.191 16.846 1.00 37.06 N
ANISOU 1921 N LEU A 268 4986 4883 4210 -181 1984 -1123 N
ATOM 1922 CA LEU A 268 4.884 23.907 16.648 1.00 37.96 C
ANISOU 1922 CA LEU A 268 4950 5056 4416 -347 2082 -1194 C
ATOM 1923 C LEU A 268 4.519 22.549 17.235 1.00 51.17 C
ANISOU 1923 C LEU A 268 6771 6633 6037 -485 2279 -1159 C
ATOM 1924 O LEU A 268 5.263 21.572 17.104 1.00 48.99 O
ANISOU 1924 O LEU A 268 6688 6233 5695 -501 2299 -1095 O
ATOM 1925 CB LEU A 268 4.537 23.938 15.155 1.00 36.49 C
ANISOU 1925 CB LEU A 268 4620 4905 4342 -421 1962 -1251 C
ATOM 1926 CG LEU A 268 3.806 25.162 14.589 1.00 34.61 C
ANISOU 1926 CG LEU A 268 4125 4808 4216 -393 1849 -1335 C
ATOM 1927 CD1 LEU A 268 4.643 26.415 14.771 1.00 31.63 C
ANISOU 1927 CD1 LEU A 268 3729 4472 3816 -201 1712 -1311 C
ATOM 1928 CD2 LEU A 268 3.442 24.969 13.119 1.00 37.49 C
ANISOU 1928 CD2 LEU A 268 4376 5195 4674 -479 1745 -1388 C
ATOM 1929 N GLU A 269 3.357 22.497 17.886 1.00 60.88 N
ANISOU 1929 N GLU A 269 7908 7920 7303 -584 2427 -1202 N
ATOM 1930 CA GLU A 269 2.861 21.241 18.436 1.00 68.19 C
ANISOU 1930 CA GLU A 269 8954 8759 8196 -733 2629 -1172 C
ATOM 1931 C GLU A 269 2.680 20.198 17.340 1.00 66.33 C
ANISOU 1931 C GLU A 269 8732 8444 8027 -885 2623 -1189 C
ATOM 1932 O GLU A 269 3.218 19.088 17.426 1.00 66.85 O
ANISOU 1932 O GLU A 269 9003 8373 8026 -929 2691 -1123 O
ATOM 1933 CB GLU A 269 1.548 21.494 19.179 1.00 78.83 C
ANISOU 1933 CB GLU A 269 10154 10195 9602 -811 2742 -1213 C
ATOM 1934 CG GLU A 269 0.874 20.258 19.745 1.00 89.37 C
ANISOU 1934 CG GLU A 269 11582 11443 10930 -973 2934 -1178 C
ATOM 1935 CD GLU A 269 -0.423 20.597 20.449 1.00 95.85 C
ANISOU 1935 CD GLU A 269 12243 12360 11814 -1038 3029 -1221 C
ATOM 1936 OE1 GLU A 269 -0.834 21.774 20.391 1.00 96.79 O
ANISOU 1936 OE1 GLU A 269 12170 12614 11990 -964 2941 -1286 O
ATOM 1937 OE2 GLU A 269 -1.031 19.695 21.059 1.00 98.59 O
ANISOU 1937 OE2 GLU A 269 12658 12645 12157 -1159 3188 -1188 O
ATOM 1938 N ILE A 270 1.929 20.540 16.294 1.00 65.31 N
ANISOU 1938 N ILE A 270 8387 8400 8030 -961 2535 -1282 N
ATOM 1939 CA ILE A 270 1.698 19.657 15.158 1.00 63.71 C
ANISOU 1939 CA ILE A 270 8171 8138 7899 -1100 2506 -1318 C
ATOM 1940 C ILE A 270 1.858 20.474 13.883 1.00 58.63 C
ANISOU 1940 C ILE A 270 7370 7578 7327 -1035 2290 -1376 C
ATOM 1941 O ILE A 270 1.569 21.674 13.854 1.00 61.53 O
ANISOU 1941 O ILE A 270 7569 8071 7740 -948 2202 -1420 O
ATOM 1942 CB ILE A 270 0.300 18.989 15.221 1.00 67.14 C
ANISOU 1942 CB ILE A 270 8490 8586 8432 -1310 2663 -1388 C
ATOM 1943 CG1 ILE A 270 0.106 18.262 16.553 1.00 68.61 C
ANISOU 1943 CG1 ILE A 270 8830 8696 8544 -1370 2891 -1323 C
ATOM 1944 CG2 ILE A 270 0.103 18.006 14.073 1.00 66.08 C
ANISOU 1944 CG2 ILE A 270 8356 8380 8371 -1454 2632 -1431 C
ATOM 1945 CD1 ILE A 270 -1.264 17.640 16.722 1.00 73.34 C
ANISOU 1945 CD1 ILE A 270 9313 9308 9244 -1578 3065 -1386 C
ATOM 1946 N PHE A 271 2.341 19.819 12.825 1.00 49.37 N
ANISOU 1946 N PHE A 271 6265 6332 6162 -1071 2206 -1373 N
ATOM 1947 CA PHE A 271 2.518 20.442 11.512 1.00 47.58 C
ANISOU 1947 CA PHE A 271 5911 6173 5993 -1019 2007 -1422 C
ATOM 1948 C PHE A 271 1.797 19.575 10.482 1.00 55.35 C
ANISOU 1948 C PHE A 271 6829 7137 7066 -1188 2007 -1498 C
ATOM 1949 O PHE A 271 2.373 18.632 9.931 1.00 53.26 O
ANISOU 1949 O PHE A 271 6707 6762 6766 -1228 1995 -1472 O
ATOM 1950 CB PHE A 271 4.002 20.613 11.175 1.00 47.62 C
ANISOU 1950 CB PHE A 271 6069 6116 5907 -864 1881 -1343 C
ATOM 1951 CG PHE A 271 4.278 21.641 10.101 1.00 56.48 C
ANISOU 1951 CG PHE A 271 7055 7331 7073 -763 1681 -1373 C
ATOM 1952 CD1 PHE A 271 3.316 21.970 9.156 1.00 59.04 C
ANISOU 1952 CD1 PHE A 271 7172 7753 7506 -835 1606 -1468 C
ATOM 1953 CD2 PHE A 271 5.505 22.278 10.042 1.00 59.32 C
ANISOU 1953 CD2 PHE A 271 7496 7677 7367 -593 1568 -1306 C
ATOM 1954 CE1 PHE A 271 3.574 22.910 8.173 1.00 58.30 C
ANISOU 1954 CE1 PHE A 271 6966 7741 7446 -737 1425 -1488 C
ATOM 1955 CE2 PHE A 271 5.768 23.220 9.061 1.00 60.07 C
ANISOU 1955 CE2 PHE A 271 7472 7849 7502 -503 1394 -1325 C
ATOM 1956 CZ PHE A 271 4.801 23.536 8.126 1.00 58.98 C
ANISOU 1956 CZ PHE A 271 7139 7806 7463 -573 1324 -1412 C
ATOM 1957 N GLU A 272 0.541 19.906 10.219 1.00 59.80 N
ANISOU 1957 N GLU A 272 7169 7808 7744 -1283 2014 -1598 N
ATOM 1958 CA GLU A 272 -0.232 19.257 9.176 1.00 59.83 C
ANISOU 1958 CA GLU A 272 7070 7816 7846 -1435 1988 -1691 C
ATOM 1959 C GLU A 272 -0.161 20.067 7.889 1.00 54.69 C
ANISOU 1959 C GLU A 272 6276 7264 7240 -1356 1774 -1746 C
ATOM 1960 O GLU A 272 0.170 21.257 7.907 1.00 54.43 O
ANISOU 1960 O GLU A 272 6173 7317 7191 -1206 1667 -1726 O
ATOM 1961 CB GLU A 272 -1.684 19.098 9.621 1.00 65.58 C
ANISOU 1961 CB GLU A 272 7629 8606 8682 -1591 2122 -1777 C
ATOM 1962 CG GLU A 272 -1.884 18.113 10.765 1.00 80.40 C
ANISOU 1962 CG GLU A 272 9648 10376 10525 -1703 2351 -1728 C
ATOM 1963 CD GLU A 272 -3.336 17.994 11.175 1.00 92.88 C
ANISOU 1963 CD GLU A 272 11046 12024 12221 -1861 2490 -1816 C
ATOM 1964 OE1 GLU A 272 -4.138 18.853 10.755 1.00 96.74 O
ANISOU 1964 OE1 GLU A 272 11294 12656 12805 -1854 2405 -1910 O
ATOM 1965 OE2 GLU A 272 -3.678 17.045 11.912 1.00 96.96 O
ANISOU 1965 OE2 GLU A 272 11657 12448 12734 -1992 2684 -1790 O
ATOM 1966 N PRO A 273 -0.439 19.441 6.743 1.00 48.65 N
ANISOU 1966 N PRO A 273 5474 6484 6528 -1451 1705 -1813 N
ATOM 1967 CA PRO A 273 -0.442 20.205 5.483 1.00 48.12 C
ANISOU 1967 CA PRO A 273 5269 6518 6497 -1376 1502 -1866 C
ATOM 1968 C PRO A 273 -1.438 21.353 5.470 1.00 46.91 C
ANISOU 1968 C PRO A 273 4863 6525 6436 -1350 1445 -1943 C
ATOM 1969 O PRO A 273 -1.167 22.394 4.858 1.00 47.58 O
ANISOU 1969 O PRO A 273 4864 6696 6520 -1218 1285 -1942 O
ATOM 1970 CB PRO A 273 -0.788 19.138 4.437 1.00 49.17 C
ANISOU 1970 CB PRO A 273 5405 6602 6676 -1515 1477 -1941 C
ATOM 1971 CG PRO A 273 -0.297 17.869 5.026 1.00 51.45 C
ANISOU 1971 CG PRO A 273 5917 6726 6906 -1597 1625 -1880 C
ATOM 1972 CD PRO A 273 -0.525 17.989 6.506 1.00 48.98 C
ANISOU 1972 CD PRO A 273 5635 6399 6576 -1607 1796 -1828 C
ATOM 1973 N SER A 274 -2.587 21.194 6.135 1.00 44.01 N
ANISOU 1973 N SER A 274 4372 6198 6151 -1471 1576 -2009 N
ATOM 1974 CA SER A 274 -3.614 22.232 6.130 1.00 45.42 C
ANISOU 1974 CA SER A 274 4300 6532 6427 -1452 1527 -2094 C
ATOM 1975 C SER A 274 -3.159 23.507 6.827 1.00 43.93 C
ANISOU 1975 C SER A 274 4095 6406 6192 -1275 1489 -2032 C
ATOM 1976 O SER A 274 -3.794 24.553 6.654 1.00 47.44 O
ANISOU 1976 O SER A 274 4341 6978 6704 -1217 1405 -2092 O
ATOM 1977 CB SER A 274 -4.893 21.710 6.786 1.00 45.04 C
ANISOU 1977 CB SER A 274 4132 6507 6475 -1625 1697 -2174 C
ATOM 1978 OG SER A 274 -4.858 21.904 8.189 1.00 49.00 O
ANISOU 1978 OG SER A 274 4691 6994 6933 -1600 1854 -2113 O
ATOM 1979 N ILE A 275 -2.085 23.443 7.618 1.00 42.41 N
ANISOU 1979 N ILE A 275 4105 6123 5887 -1187 1546 -1918 N
ATOM 1980 CA ILE A 275 -1.490 24.658 8.165 1.00 44.52 C
ANISOU 1980 CA ILE A 275 4370 6437 6107 -1007 1485 -1860 C
ATOM 1981 C ILE A 275 -1.077 25.598 7.040 1.00 41.69 C
ANISOU 1981 C ILE A 275 3933 6144 5762 -881 1270 -1865 C
ATOM 1982 O ILE A 275 -1.164 26.825 7.177 1.00 47.54 O
ANISOU 1982 O ILE A 275 4558 6975 6529 -762 1189 -1871 O
ATOM 1983 CB ILE A 275 -0.303 24.291 9.082 1.00 46.65 C
ANISOU 1983 CB ILE A 275 4888 6588 6250 -936 1568 -1740 C
ATOM 1984 CG1 ILE A 275 -0.815 23.716 10.406 1.00 53.10 C
ANISOU 1984 CG1 ILE A 275 5758 7369 7050 -1026 1783 -1730 C
ATOM 1985 CG2 ILE A 275 0.606 25.486 9.326 1.00 42.49 C
ANISOU 1985 CG2 ILE A 275 4384 6091 5671 -737 1459 -1677 C
ATOM 1986 CD1 ILE A 275 0.287 23.323 11.360 1.00 52.64 C
ANISOU 1986 CD1 ILE A 275 5945 7196 6860 -954 1867 -1616 C
ATOM 1987 N MET A 276 -0.665 25.045 5.898 1.00 35.62 N
ANISOU 1987 N MET A 276 3224 5333 4979 -906 1177 -1864 N
ATOM 1988 CA MET A 276 -0.216 25.829 4.756 1.00 36.48 C
ANISOU 1988 CA MET A 276 3278 5494 5087 -791 981 -1859 C
ATOM 1989 C MET A 276 -1.302 26.019 3.701 1.00 36.65 C
ANISOU 1989 C MET A 276 3094 5623 5209 -854 880 -1973 C
ATOM 1990 O MET A 276 -0.979 26.255 2.532 1.00 38.91 O
ANISOU 1990 O MET A 276 3365 5933 5485 -798 729 -1976 O
ATOM 1991 CB MET A 276 1.010 25.179 4.117 1.00 43.71 C
ANISOU 1991 CB MET A 276 4393 6303 5911 -757 931 -1784 C
ATOM 1992 CG MET A 276 2.122 24.833 5.086 1.00 49.88 C
ANISOU 1992 CG MET A 276 5390 6970 6592 -701 1025 -1677 C
ATOM 1993 SD MET A 276 3.542 24.133 4.227 1.00 57.32 S
ANISOU 1993 SD MET A 276 6543 7799 7437 -652 952 -1600 S
ATOM 1994 CE MET A 276 2.722 23.014 3.093 1.00 59.68 C
ANISOU 1994 CE MET A 276 6797 8092 7788 -822 943 -1698 C
ATOM 1995 N GLU A 277 -2.578 25.914 4.084 1.00 40.73 N
ANISOU 1995 N GLU A 277 3450 6206 5819 -965 962 -2069 N
ATOM 1996 CA GLU A 277 -3.659 26.154 3.131 1.00 45.72 C
ANISOU 1996 CA GLU A 277 3869 6950 6553 -1017 860 -2187 C
ATOM 1997 C GLU A 277 -3.592 27.560 2.550 1.00 39.51 C
ANISOU 1997 C GLU A 277 2960 6268 5784 -854 681 -2186 C
ATOM 1998 O GLU A 277 -3.998 27.778 1.402 1.00 37.09 O
ANISOU 1998 O GLU A 277 2542 6033 5518 -847 540 -2249 O
ATOM 1999 CB GLU A 277 -5.015 25.926 3.803 1.00 50.47 C
ANISOU 1999 CB GLU A 277 4306 7610 7259 -1152 988 -2288 C
ATOM 2000 CG GLU A 277 -5.768 24.710 3.292 1.00 61.52 C
ANISOU 2000 CG GLU A 277 5670 8982 8721 -1343 1042 -2380 C
ATOM 2001 CD GLU A 277 -6.110 24.816 1.819 1.00 71.60 C
ANISOU 2001 CD GLU A 277 6834 10330 10042 -1340 858 -2464 C
ATOM 2002 OE1 GLU A 277 -6.531 25.908 1.382 1.00 77.06 O
ANISOU 2002 OE1 GLU A 277 7357 11143 10779 -1241 724 -2506 O
ATOM 2003 OE2 GLU A 277 -5.947 23.812 1.095 1.00 71.58 O
ANISOU 2003 OE2 GLU A 277 6914 10259 10024 -1430 843 -2487 O
ATOM 2004 N GLY A 278 -3.083 28.521 3.321 1.00 35.03 N
ANISOU 2004 N GLY A 278 2414 5709 5185 -721 683 -2115 N
ATOM 2005 CA GLY A 278 -2.989 29.884 2.829 1.00 34.25 C
ANISOU 2005 CA GLY A 278 2207 5697 5108 -565 520 -2107 C
ATOM 2006 C GLY A 278 -2.055 30.037 1.645 1.00 39.53 C
ANISOU 2006 C GLY A 278 2965 6338 5716 -476 366 -2047 C
ATOM 2007 O GLY A 278 -2.244 30.930 0.815 1.00 43.72 O
ANISOU 2007 O GLY A 278 3383 6949 6278 -386 213 -2065 O
ATOM 2008 N LEU A 279 -1.042 29.170 1.543 1.00 34.94 N
ANISOU 2008 N LEU A 279 2590 5642 5044 -497 407 -1972 N
ATOM 2009 CA LEU A 279 -0.057 29.268 0.470 1.00 31.27 C
ANISOU 2009 CA LEU A 279 2224 5146 4512 -410 277 -1908 C
ATOM 2010 C LEU A 279 -0.666 29.103 -0.914 1.00 35.75 C
ANISOU 2010 C LEU A 279 2690 5782 5111 -449 152 -1987 C
ATOM 2011 O LEU A 279 0.018 29.379 -1.907 1.00 35.78 O
ANISOU 2011 O LEU A 279 2746 5785 5063 -362 28 -1940 O
ATOM 2012 CB LEU A 279 1.042 28.225 0.662 1.00 30.59 C
ANISOU 2012 CB LEU A 279 2370 4924 4329 -441 358 -1830 C
ATOM 2013 CG LEU A 279 1.867 28.364 1.937 1.00 31.19 C
ANISOU 2013 CG LEU A 279 2576 4923 4352 -379 462 -1740 C
ATOM 2014 CD1 LEU A 279 3.029 27.391 1.909 1.00 28.99 C
ANISOU 2014 CD1 LEU A 279 2524 4516 3975 -388 509 -1663 C
ATOM 2015 CD2 LEU A 279 2.356 29.792 2.101 1.00 28.58 C
ANISOU 2015 CD2 LEU A 279 2196 4637 4027 -212 367 -1685 C
ATOM 2016 N CYS A 280 -1.921 28.655 -1.008 1.00 37.09 N
ANISOU 2016 N CYS A 280 2718 6012 5363 -577 183 -2106 N
ATOM 2017 CA CYS A 280 -2.572 28.538 -2.308 1.00 35.69 C
ANISOU 2017 CA CYS A 280 2431 5911 5220 -608 53 -2195 C
ATOM 2018 C CYS A 280 -2.871 29.901 -2.916 1.00 38.91 C
ANISOU 2018 C CYS A 280 2688 6433 5662 -470 -110 -2204 C
ATOM 2019 O CYS A 280 -2.944 30.026 -4.143 1.00 41.35 O
ANISOU 2019 O CYS A 280 2978 6784 5951 -429 -249 -2221 O
ATOM 2020 CB CYS A 280 -3.856 27.723 -2.178 1.00 39.12 C
ANISOU 2020 CB CYS A 280 2739 6379 5746 -783 131 -2328 C
ATOM 2021 SG CYS A 280 -3.694 25.976 -2.615 1.00 59.04 S
ANISOU 2021 SG CYS A 280 5406 8792 8234 -951 207 -2363 S
ATOM 2022 N ASP A 281 -3.052 30.929 -2.088 1.00 41.34 N
ANISOU 2022 N ASP A 281 2933 6771 6005 -385 -91 -2172 N
ATOM 2023 CA ASP A 281 -3.281 32.279 -2.578 1.00 42.57 C
ANISOU 2023 CA ASP A 281 3076 6949 6148 -227 -221 -2107 C
ATOM 2024 C ASP A 281 -1.984 33.059 -2.760 1.00 41.45 C
ANISOU 2024 C ASP A 281 3042 6767 5940 -80 -294 -1984 C
ATOM 2025 O ASP A 281 -2.016 34.292 -2.849 1.00 39.14 O
ANISOU 2025 O ASP A 281 2764 6466 5640 46 -367 -1908 O
ATOM 2026 CB ASP A 281 -4.228 33.029 -1.639 1.00 46.54 C
ANISOU 2026 CB ASP A 281 3500 7472 6709 -209 -169 -2120 C
ATOM 2027 CG ASP A 281 -5.589 32.364 -1.526 1.00 60.23 C
ANISOU 2027 CG ASP A 281 5122 9250 8514 -343 -105 -2237 C
ATOM 2028 OD1 ASP A 281 -6.022 31.718 -2.502 1.00 63.41 O
ANISOU 2028 OD1 ASP A 281 5496 9674 8924 -407 -157 -2297 O
ATOM 2029 OD2 ASP A 281 -6.230 32.489 -0.461 1.00 65.61 O
ANISOU 2029 OD2 ASP A 281 5745 9940 9242 -382 -2 -2267 O
ATOM 2030 N VAL A 282 -0.849 32.366 -2.811 1.00 38.33 N
ANISOU 2030 N VAL A 282 2727 6337 5497 -98 -270 -1962 N
ATOM 2031 CA VAL A 282 0.455 32.971 -3.047 1.00 30.13 C
ANISOU 2031 CA VAL A 282 1818 5244 4388 38 -331 -1835 C
ATOM 2032 C VAL A 282 1.071 32.310 -4.273 1.00 29.41 C
ANISOU 2032 C VAL A 282 1838 5122 4216 31 -399 -1808 C
ATOM 2033 O VAL A 282 0.989 31.087 -4.434 1.00 33.85 O
ANISOU 2033 O VAL A 282 2471 5641 4749 -89 -335 -1850 O
ATOM 2034 CB VAL A 282 1.383 32.821 -1.821 1.00 30.92 C
ANISOU 2034 CB VAL A 282 2061 5240 4446 54 -203 -1752 C
ATOM 2035 CG1 VAL A 282 2.723 33.505 -2.067 1.00 27.88 C
ANISOU 2035 CG1 VAL A 282 1790 4800 4002 196 -271 -1629 C
ATOM 2036 CG2 VAL A 282 0.714 33.379 -0.571 1.00 33.41 C
ANISOU 2036 CG2 VAL A 282 2271 5590 4833 54 -124 -1790 C
ATOM 2037 N THR A 283 1.671 33.117 -5.145 1.00 31.92 N
ANISOU 2037 N THR A 283 2171 5460 4498 159 -528 -1739 N
ATOM 2038 CA THR A 283 2.428 32.606 -6.282 1.00 38.18 C
ANISOU 2038 CA THR A 283 3085 6221 5200 176 -590 -1695 C
ATOM 2039 C THR A 283 3.881 32.461 -5.850 1.00 36.21 C
ANISOU 2039 C THR A 283 3021 5858 4878 229 -525 -1575 C
ATOM 2040 O THR A 283 4.538 33.456 -5.525 1.00 31.59 O
ANISOU 2040 O THR A 283 2447 5257 4299 345 -551 -1490 O
ATOM 2041 CB THR A 283 2.316 33.523 -7.502 1.00 42.88 C
ANISOU 2041 CB THR A 283 3649 6867 5775 286 -736 -1653 C
ATOM 2042 OG1 THR A 283 3.298 34.558 -7.417 1.00 60.64 O
ANISOU 2042 OG1 THR A 283 5986 9058 7996 417 -756 -1513 O
ATOM 2043 CG2 THR A 283 0.945 34.162 -7.574 1.00 29.76 C
ANISOU 2043 CG2 THR A 283 1890 5242 4175 279 -756 -1688 C
ATOM 2044 N ILE A 284 4.377 31.227 -5.846 1.00 39.54 N
ANISOU 2044 N ILE A 284 3585 6200 5237 145 -444 -1573 N
ATOM 2045 CA ILE A 284 5.698 30.897 -5.326 1.00 31.60 C
ANISOU 2045 CA ILE A 284 2758 5083 4166 180 -368 -1474 C
ATOM 2046 C ILE A 284 6.497 30.243 -6.445 1.00 37.14 C
ANISOU 2046 C ILE A 284 3585 5749 4776 191 -412 -1439 C
ATOM 2047 O ILE A 284 6.077 29.217 -6.993 1.00 36.83 O
ANISOU 2047 O ILE A 284 3570 5709 4714 92 -403 -1512 O
ATOM 2048 CB ILE A 284 5.605 29.967 -4.105 1.00 26.79 C
ANISOU 2048 CB ILE A 284 2220 4398 3563 73 -211 -1499 C
ATOM 2049 CG1 ILE A 284 4.658 30.555 -3.055 1.00 26.38 C
ANISOU 2049 CG1 ILE A 284 2029 4395 3599 52 -162 -1548 C
ATOM 2050 CG2 ILE A 284 6.979 29.719 -3.513 1.00 24.69 C
ANISOU 2050 CG2 ILE A 284 2131 4020 3229 127 -144 -1397 C
ATOM 2051 CD1 ILE A 284 4.308 29.595 -1.935 1.00 29.11 C
ANISOU 2051 CD1 ILE A 284 2425 4683 3954 -69 -3 -1586 C
ATOM 2052 N ASP A 285 7.642 30.836 -6.790 1.00 36.85 N
ANISOU 2052 N ASP A 285 3627 5683 4690 312 -459 -1333 N
ATOM 2053 CA ASP A 285 8.522 30.211 -7.772 1.00 35.11 C
ANISOU 2053 CA ASP A 285 3538 5425 4377 331 -486 -1293 C
ATOM 2054 C ASP A 285 9.371 29.122 -7.134 1.00 33.70 C
ANISOU 2054 C ASP A 285 3529 5130 4147 281 -369 -1265 C
ATOM 2055 O ASP A 285 9.498 28.024 -7.687 1.00 28.52 O
ANISOU 2055 O ASP A 285 2964 4439 3435 215 -349 -1299 O
ATOM 2056 CB ASP A 285 9.418 31.259 -8.433 1.00 31.30 C
ANISOU 2056 CB ASP A 285 3070 4957 3865 476 -575 -1188 C
ATOM 2057 CG ASP A 285 8.630 32.375 -9.082 1.00 40.59 C
ANISOU 2057 CG ASP A 285 4093 6242 5089 537 -695 -1204 C
ATOM 2058 OD1 ASP A 285 7.441 32.162 -9.389 1.00 47.17 O
ANISOU 2058 OD1 ASP A 285 4818 7149 5954 469 -732 -1305 O
ATOM 2059 OD2 ASP A 285 9.200 33.466 -9.291 1.00 46.27 O
ANISOU 2059 OD2 ASP A 285 4796 6969 5815 655 -754 -1116 O
ATOM 2060 N GLU A 286 9.954 29.406 -5.972 1.00 31.41 N
ANISOU 2060 N GLU A 286 3284 4776 3874 318 -295 -1207 N
ATOM 2061 CA GLU A 286 10.803 28.454 -5.271 1.00 31.66 C
ANISOU 2061 CA GLU A 286 3479 4695 3855 288 -187 -1174 C
ATOM 2062 C GLU A 286 10.346 28.350 -3.825 1.00 34.18 C
ANISOU 2062 C GLU A 286 3783 4983 4222 234 -82 -1198 C
ATOM 2063 O GLU A 286 10.141 29.370 -3.160 1.00 30.08 O
ANISOU 2063 O GLU A 286 3172 4499 3758 291 -93 -1182 O
ATOM 2064 CB GLU A 286 12.275 28.872 -5.337 1.00 36.24 C
ANISOU 2064 CB GLU A 286 4162 5220 4387 410 -205 -1064 C
ATOM 2065 CG GLU A 286 12.768 29.161 -6.745 1.00 48.31 C
ANISOU 2065 CG GLU A 286 5698 6788 5869 479 -305 -1027 C
ATOM 2066 CD GLU A 286 14.262 29.359 -6.804 1.00 57.11 C
ANISOU 2066 CD GLU A 286 6924 7838 6937 581 -302 -924 C
ATOM 2067 OE1 GLU A 286 14.882 29.510 -5.734 1.00 56.17 O
ANISOU 2067 OE1 GLU A 286 6853 7655 6834 615 -242 -882 O
ATOM 2068 OE2 GLU A 286 14.819 29.359 -7.919 1.00 59.20 O
ANISOU 2068 OE2 GLU A 286 7227 8119 7146 630 -358 -889 O
ATOM 2069 N PHE A 287 10.192 27.119 -3.343 1.00 28.54 N
ANISOU 2069 N PHE A 287 3163 4198 3483 126 23 -1236 N
ATOM 2070 CA PHE A 287 9.760 26.852 -1.977 1.00 26.48 C
ANISOU 2070 CA PHE A 287 2908 3899 3252 65 141 -1255 C
ATOM 2071 C PHE A 287 10.844 26.067 -1.250 1.00 26.42 C
ANISOU 2071 C PHE A 287 3092 3769 3175 79 232 -1193 C
ATOM 2072 O PHE A 287 11.256 24.997 -1.711 1.00 27.14 O
ANISOU 2072 O PHE A 287 3307 3793 3212 32 258 -1195 O
ATOM 2073 CB PHE A 287 8.437 26.078 -1.959 1.00 24.77 C
ANISOU 2073 CB PHE A 287 2622 3710 3081 -89 196 -1361 C
ATOM 2074 CG PHE A 287 7.885 25.845 -0.577 1.00 25.27 C
ANISOU 2074 CG PHE A 287 2679 3745 3177 -156 327 -1381 C
ATOM 2075 CD1 PHE A 287 7.174 26.840 0.073 1.00 25.90 C
ANISOU 2075 CD1 PHE A 287 2614 3903 3326 -130 325 -1402 C
ATOM 2076 CD2 PHE A 287 8.071 24.631 0.070 1.00 32.80 C
ANISOU 2076 CD2 PHE A 287 3779 4594 4092 -244 453 -1377 C
ATOM 2077 CE1 PHE A 287 6.663 26.635 1.343 1.00 28.79 C
ANISOU 2077 CE1 PHE A 287 2976 4248 3714 -188 451 -1421 C
ATOM 2078 CE2 PHE A 287 7.562 24.418 1.345 1.00 31.34 C
ANISOU 2078 CE2 PHE A 287 3597 4383 3929 -304 581 -1388 C
ATOM 2079 CZ PHE A 287 6.857 25.423 1.980 1.00 33.90 C
ANISOU 2079 CZ PHE A 287 3772 4793 4316 -276 582 -1411 C
ATOM 2080 N ARG A 288 11.303 26.601 -0.119 1.00 23.71 N
ANISOU 2080 N ARG A 288 2775 3397 2835 149 276 -1141 N
ATOM 2081 CA ARG A 288 12.277 25.933 0.736 1.00 23.03 C
ANISOU 2081 CA ARG A 288 2866 3200 2685 172 363 -1085 C
ATOM 2082 C ARG A 288 11.636 25.608 2.078 1.00 28.28 C
ANISOU 2082 C ARG A 288 3542 3840 3363 105 486 -1110 C
ATOM 2083 O ARG A 288 11.129 26.503 2.763 1.00 33.14 O
ANISOU 2083 O ARG A 288 4049 4515 4028 136 488 -1122 O
ATOM 2084 CB ARG A 288 13.528 26.793 0.952 1.00 29.80 C
ANISOU 2084 CB ARG A 288 3763 4038 3522 325 307 -1000 C
ATOM 2085 CG ARG A 288 14.415 26.942 -0.273 1.00 31.31 C
ANISOU 2085 CG ARG A 288 3983 4230 3683 395 212 -958 C
ATOM 2086 CD ARG A 288 15.885 26.740 0.071 1.00 30.12 C
ANISOU 2086 CD ARG A 288 3980 3991 3475 488 227 -882 C
ATOM 2087 NE ARG A 288 16.700 27.829 -0.454 1.00 37.30 N
ANISOU 2087 NE ARG A 288 4839 4932 4403 610 130 -823 N
ATOM 2088 CZ ARG A 288 17.393 28.680 0.296 1.00 40.85 C
ANISOU 2088 CZ ARG A 288 5280 5366 4876 712 115 -775 C
ATOM 2089 NH1 ARG A 288 17.394 28.559 1.615 1.00 40.11 N
ANISOU 2089 NH1 ARG A 288 5232 5230 4777 715 186 -779 N
ATOM 2090 NH2 ARG A 288 18.098 29.645 -0.278 1.00 54.94 N
ANISOU 2090 NH2 ARG A 288 7013 7175 6687 811 29 -723 N
ATOM 2091 N LEU A 289 11.655 24.332 2.448 1.00 23.01 N
ANISOU 2091 N LEU A 289 3010 3082 2650 16 591 -1117 N
ATOM 2092 CA LEU A 289 11.234 23.892 3.769 1.00 24.61 C
ANISOU 2092 CA LEU A 289 3263 3241 2846 -41 725 -1122 C
ATOM 2093 C LEU A 289 12.457 23.438 4.551 1.00 23.19 C
ANISOU 2093 C LEU A 289 3277 2951 2581 36 776 -1044 C
ATOM 2094 O LEU A 289 13.278 22.671 4.040 1.00 24.26 O
ANISOU 2094 O LEU A 289 3546 3010 2663 46 766 -1014 O
ATOM 2095 CB LEU A 289 10.214 22.752 3.685 1.00 29.21 C
ANISOU 2095 CB LEU A 289 3853 3798 3449 -212 819 -1189 C
ATOM 2096 CG LEU A 289 9.702 22.206 5.020 1.00 31.27 C
ANISOU 2096 CG LEU A 289 4171 4008 3701 -287 975 -1191 C
ATOM 2097 CD1 LEU A 289 8.948 23.287 5.787 1.00 26.82 C
ANISOU 2097 CD1 LEU A 289 3454 3543 3193 -260 988 -1215 C
ATOM 2098 CD2 LEU A 289 8.824 20.989 4.803 1.00 37.55 C
ANISOU 2098 CD2 LEU A 289 4986 4760 4522 -462 1067 -1252 C
ATOM 2099 N THR A 290 12.582 23.921 5.780 1.00 24.96 N
ANISOU 2099 N THR A 290 3517 3172 2793 96 827 -1015 N
ATOM 2100 CA THR A 290 13.690 23.553 6.649 1.00 23.00 C
ANISOU 2100 CA THR A 290 3447 2827 2464 178 873 -947 C
ATOM 2101 C THR A 290 13.154 22.712 7.806 1.00 24.82 C
ANISOU 2101 C THR A 290 3773 2999 2658 95 1027 -950 C
ATOM 2102 O THR A 290 12.009 22.248 7.780 1.00 24.65 O
ANISOU 2102 O THR A 290 3692 2998 2677 -41 1101 -1005 O
ATOM 2103 CB THR A 290 14.429 24.797 7.143 1.00 23.60 C
ANISOU 2103 CB THR A 290 3481 2940 2545 333 798 -907 C
ATOM 2104 OG1 THR A 290 13.632 25.471 8.125 1.00 21.81 O
ANISOU 2104 OG1 THR A 290 3161 2774 2351 332 845 -935 O
ATOM 2105 CG2 THR A 290 14.712 25.740 5.979 1.00 20.53 C
ANISOU 2105 CG2 THR A 290 2970 2622 2210 397 656 -907 C
ATOM 2106 N TYR A 291 13.999 22.510 8.820 1.00 23.30 N
ANISOU 2106 N TYR A 291 3731 2732 2389 178 1074 -892 N
ATOM 2107 CA TYR A 291 13.635 21.673 9.957 1.00 24.36 C
ANISOU 2107 CA TYR A 291 3987 2799 2471 115 1224 -879 C
ATOM 2108 C TYR A 291 12.292 22.090 10.539 1.00 26.08 C
ANISOU 2108 C TYR A 291 4066 3099 2744 33 1300 -931 C
ATOM 2109 O TYR A 291 12.008 23.278 10.710 1.00 28.05 O
ANISOU 2109 O TYR A 291 4168 3449 3042 96 1242 -954 O
ATOM 2110 CB TYR A 291 14.703 21.746 11.055 1.00 23.91 C
ANISOU 2110 CB TYR A 291 4080 2680 2324 250 1241 -813 C
ATOM 2111 CG TYR A 291 14.246 21.145 12.377 1.00 30.06 C
ANISOU 2111 CG TYR A 291 4959 3413 3048 204 1386 -790 C
ATOM 2112 CD1 TYR A 291 14.382 19.785 12.625 1.00 29.24 C
ANISOU 2112 CD1 TYR A 291 5028 3194 2889 133 1475 -748 C
ATOM 2113 CD2 TYR A 291 13.675 21.936 13.372 1.00 26.13 C
ANISOU 2113 CD2 TYR A 291 4379 2990 2559 233 1423 -803 C
ATOM 2114 CE1 TYR A 291 13.961 19.227 13.823 1.00 33.07 C
ANISOU 2114 CE1 TYR A 291 5605 3634 3325 90 1603 -714 C
ATOM 2115 CE2 TYR A 291 13.250 21.386 14.571 1.00 26.51 C
ANISOU 2115 CE2 TYR A 291 4513 3004 2557 192 1547 -772 C
ATOM 2116 CZ TYR A 291 13.396 20.032 14.790 1.00 32.26 C
ANISOU 2116 CZ TYR A 291 5417 3613 3228 120 1639 -724 C
ATOM 2117 OH TYR A 291 12.978 19.483 15.983 1.00 39.96 O
ANISOU 2117 OH TYR A 291 6485 4547 4151 80 1768 -686 O
ATOM 2118 N THR A 292 11.466 21.089 10.838 1.00 26.63 N
ANISOU 2118 N THR A 292 4184 3125 2811 -110 1435 -951 N
ATOM 2119 CA THR A 292 10.270 21.249 11.650 1.00 31.02 C
ANISOU 2119 CA THR A 292 4649 3737 3402 -193 1548 -990 C
ATOM 2120 C THR A 292 10.250 20.123 12.673 1.00 28.90 C
ANISOU 2120 C THR A 292 4570 3359 3054 -253 1715 -946 C
ATOM 2121 O THR A 292 10.597 18.985 12.350 1.00 31.28 O
ANISOU 2121 O THR A 292 5017 3549 3320 -313 1754 -921 O
ATOM 2122 CB THR A 292 8.989 21.216 10.798 1.00 35.09 C
ANISOU 2122 CB THR A 292 4981 4326 4025 -339 1547 -1077 C
ATOM 2123 OG1 THR A 292 8.835 19.917 10.215 1.00 40.97 O
ANISOU 2123 OG1 THR A 292 5817 4981 4770 -469 1601 -1088 O
ATOM 2124 CG2 THR A 292 9.057 22.244 9.680 1.00 31.34 C
ANISOU 2124 CG2 THR A 292 4339 3951 3618 -275 1375 -1113 C
ATOM 2125 N ASN A 293 9.869 20.446 13.911 1.00 37.59 N
ANISOU 2125 N ASN A 293 5674 4487 4122 -231 1813 -934 N
ATOM 2126 CA ASN A 293 9.776 19.424 14.951 1.00 42.18 C
ANISOU 2126 CA ASN A 293 6436 4969 4622 -287 1984 -886 C
ATOM 2127 C ASN A 293 8.851 18.294 14.519 1.00 46.15 C
ANISOU 2127 C ASN A 293 6941 5418 5177 -486 2095 -919 C
ATOM 2128 O ASN A 293 9.238 17.119 14.513 1.00 45.24 O
ANISOU 2128 O ASN A 293 7008 5171 5010 -538 2162 -875 O
ATOM 2129 CB ASN A 293 9.287 20.059 16.255 1.00 44.18 C
ANISOU 2129 CB ASN A 293 6655 5288 4843 -244 2075 -884 C
ATOM 2130 CG ASN A 293 9.240 19.079 17.409 1.00 52.66 C
ANISOU 2130 CG ASN A 293 7913 6264 5830 -283 2225 -811 C
ATOM 2131 OD1 ASN A 293 8.185 18.531 17.728 1.00 62.99 O
ANISOU 2131 OD1 ASN A 293 9202 7568 7163 -428 2386 -835 O
ATOM 2132 ND2 ASN A 293 10.378 18.878 18.062 1.00 50.21 N
ANISOU 2132 ND2 ASN A 293 7765 5880 5433 -152 2156 -714 N
ATOM 2133 N ASP A 294 7.625 18.636 14.146 1.00 48.32 N
ANISOU 2133 N ASP A 294 7011 5790 5560 -599 2113 -1000 N
ATOM 2134 CA ASP A 294 6.681 17.683 13.592 1.00 49.92 C
ANISOU 2134 CA ASP A 294 7174 5957 5837 -794 2197 -1051 C
ATOM 2135 C ASP A 294 6.729 17.751 12.072 1.00 49.82 C
ANISOU 2135 C ASP A 294 7055 5973 5900 -820 2045 -1109 C
ATOM 2136 O ASP A 294 7.000 18.804 11.491 1.00 55.63 O
ANISOU 2136 O ASP A 294 7667 6806 6665 -716 1894 -1131 O
ATOM 2137 CB ASP A 294 5.265 17.971 14.099 1.00 51.90 C
ANISOU 2137 CB ASP A 294 7255 6299 6165 -907 2311 -1114 C
ATOM 2138 CG ASP A 294 4.235 16.992 13.560 1.00 60.41 C
ANISOU 2138 CG ASP A 294 8277 7341 7335 -1118 2402 -1176 C
ATOM 2139 OD1 ASP A 294 3.846 17.113 12.378 1.00 65.29 O
ANISOU 2139 OD1 ASP A 294 8749 8012 8046 -1175 2294 -1253 O
ATOM 2140 OD2 ASP A 294 3.822 16.089 14.314 1.00 62.81 O
ANISOU 2140 OD2 ASP A 294 8686 7561 7617 -1227 2581 -1147 O
ATOM 2141 N PHE A 295 6.480 16.610 11.432 1.00 41.79 N
ANISOU 2141 N PHE A 295 6097 4870 4913 -957 2086 -1132 N
ATOM 2142 CA PHE A 295 6.417 16.559 9.978 1.00 45.12 C
ANISOU 2142 CA PHE A 295 6422 5318 5402 -996 1953 -1197 C
ATOM 2143 C PHE A 295 5.635 15.325 9.551 1.00 51.71 C
ANISOU 2143 C PHE A 295 7273 6077 6298 -1192 2046 -1251 C
ATOM 2144 O PHE A 295 5.585 14.320 10.264 1.00 54.75 O
ANISOU 2144 O PHE A 295 7813 6342 6648 -1274 2197 -1210 O
ATOM 2145 CB PHE A 295 7.815 16.549 9.344 1.00 42.58 C
ANISOU 2145 CB PHE A 295 6228 4943 5008 -860 1823 -1144 C
ATOM 2146 CG PHE A 295 7.793 16.589 7.839 1.00 39.49 C
ANISOU 2146 CG PHE A 295 5739 4592 4672 -883 1682 -1207 C
ATOM 2147 CD1 PHE A 295 7.611 17.789 7.172 1.00 40.96 C
ANISOU 2147 CD1 PHE A 295 5735 4916 4910 -812 1543 -1248 C
ATOM 2148 CD2 PHE A 295 7.939 15.430 7.093 1.00 41.85 C
ANISOU 2148 CD2 PHE A 295 6141 4791 4971 -972 1688 -1226 C
ATOM 2149 CE1 PHE A 295 7.579 17.835 5.793 1.00 41.71 C
ANISOU 2149 CE1 PHE A 295 5748 5053 5046 -825 1414 -1302 C
ATOM 2150 CE2 PHE A 295 7.906 15.470 5.710 1.00 45.56 C
ANISOU 2150 CE2 PHE A 295 6524 5304 5483 -986 1558 -1289 C
ATOM 2151 CZ PHE A 295 7.729 16.676 5.060 1.00 43.50 C
ANISOU 2151 CZ PHE A 295 6077 5186 5264 -911 1421 -1324 C
ATOM 2152 N SER A 296 5.026 15.418 8.370 1.00 53.96 N
ANISOU 2152 N SER A 296 7397 6429 6676 -1266 1950 -1345 N
ATOM 2153 CA SER A 296 4.304 14.312 7.757 1.00 52.23 C
ANISOU 2153 CA SER A 296 7170 6146 6528 -1449 2004 -1415 C
ATOM 2154 C SER A 296 4.612 14.304 6.267 1.00 49.52 C
ANISOU 2154 C SER A 296 6780 5827 6208 -1429 1833 -1471 C
ATOM 2155 O SER A 296 4.675 15.365 5.639 1.00 49.15 O
ANISOU 2155 O SER A 296 6591 5905 6179 -1332 1689 -1497 O
ATOM 2156 CB SER A 296 2.792 14.425 7.992 1.00 49.26 C
ANISOU 2156 CB SER A 296 6595 5851 6269 -1601 2093 -1504 C
ATOM 2157 OG SER A 296 2.245 15.529 7.291 1.00 51.04 O
ANISOU 2157 OG SER A 296 6585 6241 6569 -1561 1957 -1582 O
ATOM 2158 N ASP A 297 4.805 13.104 5.707 1.00 47.24 N
ANISOU 2158 N ASP A 297 6615 5417 5916 -1518 1853 -1488 N
ATOM 2159 CA ASP A 297 5.245 12.986 4.317 1.00 47.46 C
ANISOU 2159 CA ASP A 297 6634 5455 5943 -1486 1698 -1533 C
ATOM 2160 C ASP A 297 4.288 13.670 3.351 1.00 46.97 C
ANISOU 2160 C ASP A 297 6323 5543 5979 -1529 1583 -1646 C
ATOM 2161 O ASP A 297 4.699 14.094 2.264 1.00 49.21 O
ANISOU 2161 O ASP A 297 6562 5889 6248 -1447 1426 -1670 O
ATOM 2162 CB ASP A 297 5.405 11.512 3.935 1.00 47.95 C
ANISOU 2162 CB ASP A 297 6858 5361 6002 -1598 1753 -1551 C
ATOM 2163 CG ASP A 297 6.465 10.804 4.758 1.00 45.36 C
ANISOU 2163 CG ASP A 297 6791 4877 5568 -1537 1845 -1438 C
ATOM 2164 OD1 ASP A 297 7.361 11.490 5.292 1.00 46.30 O
ANISOU 2164 OD1 ASP A 297 6973 5017 5601 -1375 1814 -1350 O
ATOM 2165 OD2 ASP A 297 6.407 9.562 4.867 1.00 45.46 O
ANISOU 2165 OD2 ASP A 297 6944 4744 5584 -1648 1944 -1440 O
ATOM 2166 N ASP A 298 3.012 13.787 3.725 1.00 48.20 N
ANISOU 2166 N ASP A 298 6317 5763 6235 -1654 1661 -1716 N
ATOM 2167 CA ASP A 298 2.030 14.428 2.859 1.00 51.76 C
ANISOU 2167 CA ASP A 298 6523 6360 6785 -1694 1553 -1830 C
ATOM 2168 C ASP A 298 2.332 15.905 2.630 1.00 45.72 C
ANISOU 2168 C ASP A 298 5638 5736 5996 -1523 1413 -1806 C
ATOM 2169 O ASP A 298 1.878 16.467 1.627 1.00 46.40 O
ANISOU 2169 O ASP A 298 5562 5935 6134 -1509 1276 -1884 O
ATOM 2170 CB ASP A 298 0.628 14.282 3.453 1.00 63.05 C
ANISOU 2170 CB ASP A 298 7800 7827 8328 -1856 1679 -1906 C
ATOM 2171 CG ASP A 298 0.259 12.840 3.742 1.00 74.34 C
ANISOU 2171 CG ASP A 298 9341 9111 9795 -2039 1833 -1927 C
ATOM 2172 OD1 ASP A 298 0.336 12.001 2.820 1.00 77.74 O
ANISOU 2172 OD1 ASP A 298 9822 9474 10243 -2109 1781 -1983 O
ATOM 2173 OD2 ASP A 298 -0.115 12.546 4.896 1.00 77.98 O
ANISOU 2173 OD2 ASP A 298 9842 9521 10267 -2112 2009 -1888 O
ATOM 2174 N ILE A 299 3.086 16.540 3.533 1.00 43.49 N
ANISOU 2174 N ILE A 299 5436 5448 5640 -1391 1441 -1702 N
ATOM 2175 CA ILE A 299 3.338 17.978 3.435 1.00 47.22 C
ANISOU 2175 CA ILE A 299 5793 6047 6102 -1234 1321 -1678 C
ATOM 2176 C ILE A 299 4.012 18.324 2.111 1.00 52.99 C
ANISOU 2176 C ILE A 299 6518 6814 6801 -1136 1140 -1682 C
ATOM 2177 O ILE A 299 3.725 19.364 1.505 1.00 48.95 O
ANISOU 2177 O ILE A 299 5845 6428 6325 -1065 1014 -1715 O
ATOM 2178 CB ILE A 299 4.170 18.456 4.641 1.00 46.23 C
ANISOU 2178 CB ILE A 299 5784 5886 5895 -1110 1383 -1567 C
ATOM 2179 CG1 ILE A 299 3.346 18.347 5.926 1.00 50.93 C
ANISOU 2179 CG1 ILE A 299 6348 6480 6523 -1194 1553 -1572 C
ATOM 2180 CG2 ILE A 299 4.656 19.885 4.443 1.00 42.30 C
ANISOU 2180 CG2 ILE A 299 5196 5494 5383 -937 1245 -1535 C
ATOM 2181 CD1 ILE A 299 4.006 18.950 7.143 1.00 52.99 C
ANISOU 2181 CD1 ILE A 299 6696 6731 6707 -1067 1606 -1478 C
ATOM 2182 N VAL A 300 4.906 17.456 1.634 1.00 60.04 N
ANISOU 2182 N VAL A 300 7590 7598 7625 -1127 1128 -1647 N
ATOM 2183 CA VAL A 300 5.591 17.724 0.374 1.00 61.06 C
ANISOU 2183 CA VAL A 300 7726 7760 7715 -1033 969 -1647 C
ATOM 2184 C VAL A 300 4.692 17.495 -0.835 1.00 63.11 C
ANISOU 2184 C VAL A 300 7849 8088 8042 -1127 882 -1766 C
ATOM 2185 O VAL A 300 4.993 18.000 -1.924 1.00 68.95 O
ANISOU 2185 O VAL A 300 8541 8898 8760 -1043 736 -1779 O
ATOM 2186 CB VAL A 300 6.860 16.865 0.253 1.00 61.84 C
ANISOU 2186 CB VAL A 300 8058 7724 7716 -986 984 -1576 C
ATOM 2187 CG1 VAL A 300 7.702 17.003 1.506 1.00 63.96 C
ANISOU 2187 CG1 VAL A 300 8463 7921 7918 -898 1072 -1467 C
ATOM 2188 CG2 VAL A 300 6.502 15.411 -0.002 1.00 62.22 C
ANISOU 2188 CG2 VAL A 300 8198 7662 7781 -1141 1061 -1635 C
ATOM 2189 N LYS A 301 3.600 16.748 -0.678 1.00 56.91 N
ANISOU 2189 N LYS A 301 7001 7284 7338 -1298 968 -1855 N
ATOM 2190 CA LYS A 301 2.645 16.511 -1.751 1.00 49.68 C
ANISOU 2190 CA LYS A 301 5941 6436 6498 -1397 887 -1984 C
ATOM 2191 C LYS A 301 1.471 17.480 -1.708 1.00 44.04 C
ANISOU 2191 C LYS A 301 4979 5873 5881 -1415 847 -2057 C
ATOM 2192 O LYS A 301 0.457 17.240 -2.372 1.00 43.79 O
ANISOU 2192 O LYS A 301 4805 5900 5933 -1520 803 -2177 O
ATOM 2193 CB LYS A 301 2.135 15.069 -1.689 1.00 51.79 C
ANISOU 2193 CB LYS A 301 6278 6588 6811 -1582 998 -2051 C
ATOM 2194 CG LYS A 301 3.122 14.041 -2.214 1.00 54.94 C
ANISOU 2194 CG LYS A 301 6890 6855 7130 -1573 989 -2021 C
ATOM 2195 CD LYS A 301 2.740 12.631 -1.803 1.00 57.34 C
ANISOU 2195 CD LYS A 301 7297 7014 7476 -1748 1133 -2059 C
ATOM 2196 CE LYS A 301 2.887 12.437 -0.305 1.00 60.68 C
ANISOU 2196 CE LYS A 301 7825 7349 7884 -1769 1310 -1965 C
ATOM 2197 NZ LYS A 301 3.157 11.013 0.045 1.00 67.30 N
ANISOU 2197 NZ LYS A 301 8862 8002 8706 -1875 1437 -1947 N
ATOM 2198 N PHE A 302 1.587 18.567 -0.948 1.00 46.87 N
ANISOU 2198 N PHE A 302 5280 6294 6232 -1310 855 -1992 N
ATOM 2199 CA PHE A 302 0.474 19.491 -0.772 1.00 44.12 C
ANISOU 2199 CA PHE A 302 4701 6083 5978 -1322 830 -2059 C
ATOM 2200 C PHE A 302 0.156 20.189 -2.088 1.00 42.99 C
ANISOU 2200 C PHE A 302 4410 6065 5859 -1260 640 -2127 C
ATOM 2201 O PHE A 302 1.059 20.632 -2.804 1.00 45.53 O
ANISOU 2201 O PHE A 302 4798 6398 6104 -1129 522 -2068 O
ATOM 2202 CB PHE A 302 0.807 20.513 0.313 1.00 46.55 C
ANISOU 2202 CB PHE A 302 5001 6422 6262 -1206 872 -1971 C
ATOM 2203 CG PHE A 302 -0.395 21.229 0.863 1.00 48.39 C
ANISOU 2203 CG PHE A 302 5023 6768 6596 -1245 905 -2038 C
ATOM 2204 CD1 PHE A 302 -1.490 20.517 1.321 1.00 47.81 C
ANISOU 2204 CD1 PHE A 302 4872 6685 6608 -1417 1032 -2121 C
ATOM 2205 CD2 PHE A 302 -0.419 22.610 0.942 1.00 47.73 C
ANISOU 2205 CD2 PHE A 302 4818 6795 6524 -1109 814 -2019 C
ATOM 2206 CE1 PHE A 302 -2.592 21.167 1.834 1.00 50.92 C
ANISOU 2206 CE1 PHE A 302 5065 7187 7096 -1450 1068 -2186 C
ATOM 2207 CE2 PHE A 302 -1.519 23.267 1.456 1.00 48.61 C
ANISOU 2207 CE2 PHE A 302 4733 7009 6726 -1137 844 -2085 C
ATOM 2208 CZ PHE A 302 -2.607 22.545 1.901 1.00 51.39 C
ANISOU 2208 CZ PHE A 302 5005 7360 7162 -1307 972 -2170 C
ATOM 2209 N HIS A 303 -1.139 20.287 -2.399 1.00 40.37 N
ANISOU 2209 N HIS A 303 3876 5829 5634 -1355 613 -2250 N
ATOM 2210 CA HIS A 303 -1.578 20.778 -3.701 1.00 39.73 C
ANISOU 2210 CA HIS A 303 3654 5863 5578 -1314 433 -2331 C
ATOM 2211 C HIS A 303 -1.209 22.236 -3.942 1.00 40.86 C
ANISOU 2211 C HIS A 303 3727 6109 5689 -1129 304 -2269 C
ATOM 2212 O HIS A 303 -1.106 22.650 -5.101 1.00 43.62 O
ANISOU 2212 O HIS A 303 4033 6528 6012 -1051 146 -2290 O
ATOM 2213 CB HIS A 303 -3.090 20.599 -3.836 1.00 44.95 C
ANISOU 2213 CB HIS A 303 4102 6607 6370 -1454 439 -2481 C
ATOM 2214 CG HIS A 303 -3.882 21.408 -2.857 1.00 46.58 C
ANISOU 2214 CG HIS A 303 4147 6893 6657 -1455 507 -2494 C
ATOM 2215 ND1 HIS A 303 -4.603 22.522 -3.226 1.00 46.99 N
ANISOU 2215 ND1 HIS A 303 3990 7094 6769 -1382 387 -2551 N
ATOM 2216 CD2 HIS A 303 -4.055 21.272 -1.521 1.00 47.86 C
ANISOU 2216 CD2 HIS A 303 4332 7007 6844 -1512 682 -2456 C
ATOM 2217 CE1 HIS A 303 -5.195 23.033 -2.160 1.00 46.65 C
ANISOU 2217 CE1 HIS A 303 3842 7093 6790 -1396 486 -2554 C
ATOM 2218 NE2 HIS A 303 -4.876 22.295 -1.113 1.00 46.50 N
ANISOU 2218 NE2 HIS A 303 3961 6959 6748 -1475 667 -2497 N
ATOM 2219 N CYS A 304 -1.014 23.026 -2.884 1.00 41.46 N
ANISOU 2219 N CYS A 304 3792 6194 5765 -1056 368 -2195 N
ATOM 2220 CA CYS A 304 -0.621 24.420 -3.057 1.00 44.33 C
ANISOU 2220 CA CYS A 304 4096 6640 6106 -882 252 -2133 C
ATOM 2221 C CYS A 304 0.829 24.574 -3.497 1.00 42.71 C
ANISOU 2221 C CYS A 304 4068 6373 5787 -751 188 -2016 C
ATOM 2222 O CYS A 304 1.248 25.694 -3.811 1.00 45.35 O
ANISOU 2222 O CYS A 304 4364 6766 6100 -606 81 -1960 O
ATOM 2223 CB CYS A 304 -0.856 25.206 -1.763 1.00 46.08 C
ANISOU 2223 CB CYS A 304 4254 6887 6368 -843 339 -2098 C
ATOM 2224 SG CYS A 304 -2.560 25.149 -1.147 1.00 61.14 S
ANISOU 2224 SG CYS A 304 5938 8880 8414 -986 427 -2232 S
ATOM 2225 N LEU A 305 1.598 23.487 -3.526 1.00 34.32 N
ANISOU 2225 N LEU A 305 3194 5189 4655 -798 254 -1979 N
ATOM 2226 CA LEU A 305 2.965 23.490 -4.026 1.00 38.01 C
ANISOU 2226 CA LEU A 305 3828 5596 5016 -685 198 -1880 C
ATOM 2227 C LEU A 305 3.058 23.026 -5.476 1.00 38.50 C
ANISOU 2227 C LEU A 305 3911 5678 5041 -691 83 -1928 C
ATOM 2228 O LEU A 305 4.166 22.820 -5.979 1.00 38.27 O
ANISOU 2228 O LEU A 305 4028 5591 4921 -616 49 -1857 O
ATOM 2229 CB LEU A 305 3.855 22.604 -3.149 1.00 32.35 C
ANISOU 2229 CB LEU A 305 3317 4734 4239 -713 336 -1805 C
ATOM 2230 CG LEU A 305 3.918 22.891 -1.645 1.00 33.02 C
ANISOU 2230 CG LEU A 305 3425 4783 4337 -702 463 -1750 C
ATOM 2231 CD1 LEU A 305 4.777 21.858 -0.918 1.00 32.75 C
ANISOU 2231 CD1 LEU A 305 3609 4601 4232 -733 590 -1683 C
ATOM 2232 CD2 LEU A 305 4.431 24.299 -1.392 1.00 31.49 C
ANISOU 2232 CD2 LEU A 305 3181 4650 4133 -539 390 -1675 C
ATOM 2233 N ALA A 306 1.920 22.871 -6.160 1.00 38.59 N
ANISOU 2233 N ALA A 306 3775 5770 5118 -775 22 -2050 N
ATOM 2234 CA ALA A 306 1.910 22.218 -7.467 1.00 41.60 C
ANISOU 2234 CA ALA A 306 4184 6160 5462 -803 -73 -2115 C
ATOM 2235 C ALA A 306 2.573 23.062 -8.551 1.00 44.31 C
ANISOU 2235 C ALA A 306 4534 6571 5729 -644 -229 -2060 C
ATOM 2236 O ALA A 306 3.177 22.509 -9.477 1.00 45.92 O
ANISOU 2236 O ALA A 306 4847 6745 5854 -624 -283 -2057 O
ATOM 2237 CB ALA A 306 0.474 21.877 -7.867 1.00 42.91 C
ANISOU 2237 CB ALA A 306 4177 6402 5727 -932 -105 -2270 C
ATOM 2238 N ASN A 307 2.471 24.387 -8.465 1.00 43.80 N
ANISOU 2238 N ASN A 307 4359 6597 5687 -531 -299 -2016 N
ATOM 2239 CA ASN A 307 2.995 25.274 -9.497 1.00 42.80 C
ANISOU 2239 CA ASN A 307 4226 6539 5498 -382 -444 -1961 C
ATOM 2240 C ASN A 307 4.388 25.802 -9.182 1.00 39.08 C
ANISOU 2240 C ASN A 307 3890 6005 4954 -253 -423 -1812 C
ATOM 2241 O ASN A 307 4.938 26.576 -9.971 1.00 42.84 O
ANISOU 2241 O ASN A 307 4373 6527 5379 -126 -529 -1748 O
ATOM 2242 CB ASN A 307 2.031 26.442 -9.723 1.00 44.13 C
ANISOU 2242 CB ASN A 307 4188 6842 5737 -328 -549 -2004 C
ATOM 2243 CG ASN A 307 0.661 25.981 -10.178 1.00 53.89 C
ANISOU 2243 CG ASN A 307 5274 8154 7046 -443 -593 -2161 C
ATOM 2244 OD1 ASN A 307 0.526 24.932 -10.807 1.00 55.30 O
ANISOU 2244 OD1 ASN A 307 5504 8307 7201 -531 -599 -2235 O
ATOM 2245 ND2 ASN A 307 -0.365 26.759 -9.856 1.00 53.96 N
ANISOU 2245 ND2 ASN A 307 5093 8258 7150 -442 -624 -2217 N
ATOM 2246 N VAL A 308 4.961 25.408 -8.044 1.00 33.75 N
ANISOU 2246 N VAL A 308 3322 5226 4276 -281 -290 -1755 N
ATOM 2247 CA VAL A 308 6.350 25.724 -7.746 1.00 30.14 C
ANISOU 2247 CA VAL A 308 3005 4697 3750 -169 -266 -1624 C
ATOM 2248 C VAL A 308 7.265 25.076 -8.785 1.00 32.70 C
ANISOU 2248 C VAL A 308 3472 4979 3974 -137 -308 -1596 C
ATOM 2249 O VAL A 308 7.006 23.966 -9.268 1.00 38.25 O
ANISOU 2249 O VAL A 308 4227 5652 4656 -233 -293 -1671 O
ATOM 2250 CB VAL A 308 6.691 25.253 -6.320 1.00 31.49 C
ANISOU 2250 CB VAL A 308 3268 4764 3932 -217 -114 -1587 C
ATOM 2251 CG1 VAL A 308 8.187 25.153 -6.108 1.00 35.15 C
ANISOU 2251 CG1 VAL A 308 3908 5134 4314 -126 -83 -1473 C
ATOM 2252 CG2 VAL A 308 6.076 26.186 -5.293 1.00 30.56 C
ANISOU 2252 CG2 VAL A 308 3022 4695 3894 -200 -83 -1586 C
ATOM 2253 N SER A 309 8.341 25.789 -9.147 1.00 26.31 N
ANISOU 2253 N SER A 309 2722 4168 3106 1 -360 -1490 N
ATOM 2254 CA SER A 309 9.337 25.280 -10.081 1.00 29.39 C
ANISOU 2254 CA SER A 309 3250 4521 3397 50 -392 -1450 C
ATOM 2255 C SER A 309 10.614 24.779 -9.414 1.00 30.67 C
ANISOU 2255 C SER A 309 3584 4561 3509 79 -296 -1365 C
ATOM 2256 O SER A 309 11.349 24.006 -10.037 1.00 27.48 O
ANISOU 2256 O SER A 309 3307 4106 3027 87 -293 -1355 O
ATOM 2257 CB SER A 309 9.710 26.360 -11.109 1.00 25.58 C
ANISOU 2257 CB SER A 309 2721 4122 2876 184 -516 -1390 C
ATOM 2258 OG SER A 309 10.104 27.563 -10.473 1.00 42.79 O
ANISOU 2258 OG SER A 309 4853 6310 5095 282 -520 -1299 O
ATOM 2259 N ALA A 310 10.905 25.198 -8.180 1.00 25.47 N
ANISOU 2259 N ALA A 310 2931 3857 2889 103 -222 -1309 N
ATOM 2260 CA ALA A 310 12.036 24.672 -7.421 1.00 23.42 C
ANISOU 2260 CA ALA A 310 2831 3480 2586 128 -130 -1238 C
ATOM 2261 C ALA A 310 11.562 24.319 -6.020 1.00 27.49 C
ANISOU 2261 C ALA A 310 3351 3942 3153 47 -15 -1260 C
ATOM 2262 O ALA A 310 11.208 25.208 -5.238 1.00 26.23 O
ANISOU 2262 O ALA A 310 3096 3820 3052 76 -8 -1244 O
ATOM 2263 CB ALA A 310 13.192 25.671 -7.356 1.00 22.14 C
ANISOU 2263 CB ALA A 310 2693 3315 2403 275 -165 -1125 C
ATOM 2264 N MET A 311 11.562 23.027 -5.707 1.00 31.16 N
ANISOU 2264 N MET A 311 3932 4315 3593 -51 75 -1296 N
ATOM 2265 CA MET A 311 11.167 22.517 -4.402 1.00 29.03 C
ANISOU 2265 CA MET A 311 3694 3979 3356 -134 200 -1310 C
ATOM 2266 C MET A 311 12.406 22.061 -3.644 1.00 28.00 C
ANISOU 2266 C MET A 311 3743 3732 3165 -78 275 -1227 C
ATOM 2267 O MET A 311 13.299 21.435 -4.225 1.00 24.03 O
ANISOU 2267 O MET A 311 3367 3170 2595 -45 263 -1201 O
ATOM 2268 CB MET A 311 10.181 21.354 -4.549 1.00 26.52 C
ANISOU 2268 CB MET A 311 3376 3634 3064 -296 255 -1412 C
ATOM 2269 CG MET A 311 9.754 20.704 -3.244 1.00 34.06 C
ANISOU 2269 CG MET A 311 4379 4513 4051 -395 399 -1423 C
ATOM 2270 SD MET A 311 8.773 21.804 -2.207 1.00 39.30 S
ANISOU 2270 SD MET A 311 4867 5265 4801 -400 430 -1436 S
ATOM 2271 CE MET A 311 7.501 22.300 -3.364 1.00 43.88 C
ANISOU 2271 CE MET A 311 5232 5987 5455 -449 312 -1543 C
ATOM 2272 N SER A 312 12.456 22.365 -2.346 1.00 24.02 N
ANISOU 2272 N SER A 312 3249 3197 2680 -61 351 -1189 N
ATOM 2273 CA SER A 312 13.645 22.068 -1.557 1.00 23.37 C
ANISOU 2273 CA SER A 312 3327 3013 2540 11 411 -1110 C
ATOM 2274 C SER A 312 13.277 21.640 -0.140 1.00 27.59 C
ANISOU 2274 C SER A 312 3914 3486 3084 -49 538 -1110 C
ATOM 2275 O SER A 312 12.414 22.246 0.502 1.00 25.23 O
ANISOU 2275 O SER A 312 3497 3247 2843 -78 563 -1136 O
ATOM 2276 CB SER A 312 14.579 23.279 -1.506 1.00 21.41 C
ANISOU 2276 CB SER A 312 3049 2800 2287 166 337 -1031 C
ATOM 2277 OG SER A 312 15.776 22.946 -0.834 1.00 44.01 O
ANISOU 2277 OG SER A 312 6063 5567 5094 240 383 -963 O
ATOM 2278 N LEU A 313 13.955 20.597 0.344 1.00 27.60 N
ANISOU 2278 N LEU A 313 4096 3366 3024 -61 619 -1078 N
ATOM 2279 CA LEU A 313 13.822 20.118 1.714 1.00 25.21 C
ANISOU 2279 CA LEU A 313 3882 2989 2709 -99 745 -1059 C
ATOM 2280 C LEU A 313 15.217 19.986 2.311 1.00 30.12 C
ANISOU 2280 C LEU A 313 4666 3523 3256 21 759 -975 C
ATOM 2281 O LEU A 313 16.094 19.359 1.707 1.00 34.71 O
ANISOU 2281 O LEU A 313 5362 4040 3785 56 733 -953 O
ATOM 2282 CB LEU A 313 13.086 18.769 1.774 1.00 25.07 C
ANISOU 2282 CB LEU A 313 3936 2895 2694 -257 847 -1113 C
ATOM 2283 CG LEU A 313 11.756 18.595 1.032 1.00 31.05 C
ANISOU 2283 CG LEU A 313 4551 3720 3525 -395 833 -1213 C
ATOM 2284 CD1 LEU A 313 11.262 17.169 1.182 1.00 40.45 C
ANISOU 2284 CD1 LEU A 313 5845 4807 4718 -544 943 -1256 C
ATOM 2285 CD2 LEU A 313 10.699 19.574 1.523 1.00 28.66 C
ANISOU 2285 CD2 LEU A 313 4062 3529 3299 -418 837 -1247 C
ATOM 2286 N ALA A 314 15.423 20.587 3.483 1.00 22.44 N
ANISOU 2286 N ALA A 314 3697 2551 2278 90 795 -933 N
ATOM 2287 CA ALA A 314 16.703 20.538 4.182 1.00 21.71 C
ANISOU 2287 CA ALA A 314 3747 2383 2120 211 803 -860 C
ATOM 2288 C ALA A 314 16.455 20.248 5.654 1.00 25.29 C
ANISOU 2288 C ALA A 314 4280 2784 2545 194 919 -841 C
ATOM 2289 O ALA A 314 15.721 20.986 6.318 1.00 25.32 O
ANISOU 2289 O ALA A 314 4175 2857 2589 185 942 -859 O
ATOM 2290 CB ALA A 314 17.482 21.847 4.020 1.00 21.68 C
ANISOU 2290 CB ALA A 314 3659 2446 2134 356 694 -821 C
ATOM 2291 N GLY A 315 17.070 19.181 6.158 1.00 29.32 N
ANISOU 2291 N GLY A 315 4984 3174 2982 197 992 -806 N
ATOM 2292 CA GLY A 315 16.931 18.815 7.552 1.00 23.25 C
ANISOU 2292 CA GLY A 315 4301 2353 2179 188 1092 -767 C
ATOM 2293 C GLY A 315 15.547 18.372 7.961 1.00 29.27 C
ANISOU 2293 C GLY A 315 5039 3117 2967 35 1221 -822 C
ATOM 2294 O GLY A 315 15.204 18.456 9.143 1.00 30.72 O
ANISOU 2294 O GLY A 315 5251 3294 3128 34 1311 -805 O
ATOM 2295 N VAL A 316 14.748 17.877 7.021 1.00 28.26 N
ANISOU 2295 N VAL A 316 4844 3003 2892 -95 1223 -882 N
ATOM 2296 CA VAL A 316 13.344 17.559 7.257 1.00 32.32 C
ANISOU 2296 CA VAL A 316 5277 3541 3463 -253 1320 -939 C
ATOM 2297 C VAL A 316 13.195 16.067 7.522 1.00 39.90 C
ANISOU 2297 C VAL A 316 6408 4364 4388 -366 1445 -933 C
ATOM 2298 O VAL A 316 13.874 15.236 6.903 1.00 42.46 O
ANISOU 2298 O VAL A 316 6858 4600 4677 -362 1421 -922 O
ATOM 2299 CB VAL A 316 12.481 18.008 6.062 1.00 34.17 C
ANISOU 2299 CB VAL A 316 5313 3882 3788 -327 1236 -1020 C
ATOM 2300 CG1 VAL A 316 11.041 17.576 6.241 1.00 31.39 C
ANISOU 2300 CG1 VAL A 316 4872 3550 3504 -498 1335 -1089 C
ATOM 2301 CG2 VAL A 316 12.567 19.522 5.898 1.00 33.13 C
ANISOU 2301 CG2 VAL A 316 5016 3878 3693 -214 1122 -1019 C
ATOM 2302 N SER A 317 12.299 15.724 8.445 1.00 28.98 N
ANISOU 2302 N SER A 317 5031 2963 3018 -467 1582 -940 N
ATOM 2303 CA SER A 317 12.053 14.337 8.832 1.00 32.85 C
ANISOU 2303 CA SER A 317 5683 3317 3483 -585 1720 -928 C
ATOM 2304 C SER A 317 11.182 13.579 7.842 1.00 31.42 C
ANISOU 2304 C SER A 317 5437 3119 3381 -754 1732 -1010 C
ATOM 2305 O SER A 317 10.299 12.823 8.251 1.00 37.75 O
ANISOU 2305 O SER A 317 6259 3867 4217 -902 1863 -1033 O
ATOM 2306 CB SER A 317 11.427 14.314 10.223 1.00 40.32 C
ANISOU 2306 CB SER A 317 6657 4252 4410 -625 1870 -899 C
ATOM 2307 OG SER A 317 12.317 14.857 11.177 1.00 52.29 O
ANISOU 2307 OG SER A 317 8264 5765 5838 -464 1860 -825 O
ATOM 2308 N ILE A 318 11.403 13.758 6.540 1.00 34.47 N
ANISOU 2308 N ILE A 318 5747 3551 3798 -737 1598 -1057 N
ATOM 2309 CA ILE A 318 10.625 13.021 5.552 1.00 36.26 C
ANISOU 2309 CA ILE A 318 5918 3764 4095 -889 1595 -1144 C
ATOM 2310 C ILE A 318 11.160 11.599 5.459 1.00 38.03 C
ANISOU 2310 C ILE A 318 6359 3818 4272 -936 1657 -1122 C
ATOM 2311 O ILE A 318 12.373 11.379 5.343 1.00 37.34 O
ANISOU 2311 O ILE A 318 6419 3663 4105 -817 1608 -1065 O
ATOM 2312 CB ILE A 318 10.657 13.730 4.187 1.00 34.39 C
ANISOU 2312 CB ILE A 318 5528 3642 3897 -845 1429 -1202 C
ATOM 2313 CG1 ILE A 318 9.954 12.876 3.129 1.00 32.05 C
ANISOU 2313 CG1 ILE A 318 5194 3323 3662 -992 1415 -1298 C
ATOM 2314 CG2 ILE A 318 12.092 14.065 3.771 1.00 29.40 C
ANISOU 2314 CG2 ILE A 318 4987 2997 3185 -672 1319 -1139 C
ATOM 2315 CD1 ILE A 318 9.497 13.644 1.915 1.00 31.69 C
ANISOU 2315 CD1 ILE A 318 4951 3417 3672 -985 1272 -1375 C
ATOM 2316 N LYS A 319 10.256 10.625 5.537 1.00 43.67 N
ANISOU 2316 N LYS A 319 7093 4458 5041 -1111 1768 -1169 N
ATOM 2317 CA LYS A 319 10.626 9.221 5.430 1.00 44.25 C
ANISOU 2317 CA LYS A 319 7368 4360 5085 -1175 1833 -1158 C
ATOM 2318 C LYS A 319 10.352 8.640 4.054 1.00 41.10 C
ANISOU 2318 C LYS A 319 6924 3952 4743 -1263 1755 -1255 C
ATOM 2319 O LYS A 319 11.123 7.793 3.590 1.00 40.99 O
ANISOU 2319 O LYS A 319 7068 3825 4682 -1238 1732 -1245 O
ATOM 2320 CB LYS A 319 9.879 8.396 6.481 1.00 46.36 C
ANISOU 2320 CB LYS A 319 7718 4523 5374 -1315 2022 -1138 C
ATOM 2321 CG LYS A 319 10.108 8.884 7.896 1.00 47.13 C
ANISOU 2321 CG LYS A 319 7878 4626 5404 -1230 2112 -1043 C
ATOM 2322 CD LYS A 319 11.576 8.798 8.278 1.00 50.25 C
ANISOU 2322 CD LYS A 319 8474 4944 5676 -1051 2073 -946 C
ATOM 2323 CE LYS A 319 11.856 9.636 9.508 1.00 57.73 C
ANISOU 2323 CE LYS A 319 9433 5945 6558 -932 2110 -870 C
ATOM 2324 NZ LYS A 319 10.808 9.418 10.539 1.00 60.26 N
ANISOU 2324 NZ LYS A 319 9741 6251 6903 -1053 2280 -861 N
ATOM 2325 N TYR A 320 9.285 9.079 3.389 1.00 39.59 N
ANISOU 2325 N TYR A 320 6518 3876 4647 -1359 1707 -1353 N
ATOM 2326 CA TYR A 320 8.924 8.549 2.083 1.00 40.73 C
ANISOU 2326 CA TYR A 320 6607 4023 4847 -1446 1627 -1458 C
ATOM 2327 C TYR A 320 8.480 9.682 1.172 1.00 42.24 C
ANISOU 2327 C TYR A 320 6569 4399 5083 -1406 1482 -1526 C
ATOM 2328 O TYR A 320 7.614 10.484 1.538 1.00 38.25 O
ANISOU 2328 O TYR A 320 5889 4006 4639 -1439 1496 -1551 O
ATOM 2329 CB TYR A 320 7.822 7.493 2.200 1.00 38.69 C
ANISOU 2329 CB TYR A 320 6344 3676 4680 -1660 1747 -1531 C
ATOM 2330 CG TYR A 320 8.236 6.310 3.042 1.00 50.99 C
ANISOU 2330 CG TYR A 320 8141 5038 6195 -1704 1893 -1461 C
ATOM 2331 CD1 TYR A 320 9.187 5.410 2.585 1.00 52.25 C
ANISOU 2331 CD1 TYR A 320 8496 5065 6293 -1659 1864 -1441 C
ATOM 2332 CD2 TYR A 320 7.694 6.105 4.302 1.00 45.23 C
ANISOU 2332 CD2 TYR A 320 7448 4255 5482 -1783 2061 -1410 C
ATOM 2333 CE1 TYR A 320 9.579 4.334 3.353 1.00 49.05 C
ANISOU 2333 CE1 TYR A 320 8315 4474 5846 -1691 1993 -1374 C
ATOM 2334 CE2 TYR A 320 8.079 5.030 5.078 1.00 50.49 C
ANISOU 2334 CE2 TYR A 320 8344 4737 6102 -1818 2196 -1337 C
ATOM 2335 CZ TYR A 320 9.022 4.148 4.599 1.00 53.47 C
ANISOU 2335 CZ TYR A 320 8914 4981 6422 -1770 2159 -1319 C
ATOM 2336 OH TYR A 320 9.412 3.075 5.363 1.00 57.91 O
ANISOU 2336 OH TYR A 320 9711 5354 6937 -1797 2288 -1244 O
ATOM 2337 N LEU A 321 9.086 9.745 -0.009 1.00 38.98 N
ANISOU 2337 N LEU A 321 6160 4016 4636 -1330 1344 -1555 N
ATOM 2338 CA LEU A 321 8.716 10.686 -1.063 1.00 40.54 C
ANISOU 2338 CA LEU A 321 6161 4376 4866 -1292 1196 -1621 C
ATOM 2339 C LEU A 321 8.202 9.849 -2.228 1.00 45.06 C
ANISOU 2339 C LEU A 321 6710 4927 5483 -1405 1143 -1739 C
ATOM 2340 O LEU A 321 8.992 9.335 -3.025 1.00 49.81 O
ANISOU 2340 O LEU A 321 7425 5476 6024 -1351 1078 -1744 O
ATOM 2341 CB LEU A 321 9.903 11.557 -1.465 1.00 41.13 C
ANISOU 2341 CB LEU A 321 6261 4513 4855 -1094 1078 -1548 C
ATOM 2342 CG LEU A 321 9.671 12.608 -2.553 1.00 44.84 C
ANISOU 2342 CG LEU A 321 6548 5146 5342 -1030 923 -1596 C
ATOM 2343 CD1 LEU A 321 8.401 13.387 -2.277 1.00 45.59 C
ANISOU 2343 CD1 LEU A 321 6429 5362 5531 -1100 927 -1650 C
ATOM 2344 CD2 LEU A 321 10.856 13.548 -2.635 1.00 45.57 C
ANISOU 2344 CD2 LEU A 321 6671 5287 5358 -839 841 -1501 C
ATOM 2345 N GLU A 322 6.881 9.702 -2.319 1.00 46.05 N
ANISOU 2345 N GLU A 322 6685 5095 5715 -1560 1172 -1840 N
ATOM 2346 CA GLU A 322 6.261 8.824 -3.300 1.00 51.45 C
ANISOU 2346 CA GLU A 322 7341 5750 6457 -1689 1135 -1966 C
ATOM 2347 C GLU A 322 4.974 9.448 -3.820 1.00 55.96 C
ANISOU 2347 C GLU A 322 7660 6473 7131 -1768 1066 -2080 C
ATOM 2348 O GLU A 322 4.299 10.197 -3.110 1.00 52.93 O
ANISOU 2348 O GLU A 322 7140 6172 6801 -1786 1110 -2069 O
ATOM 2349 CB GLU A 322 5.959 7.438 -2.703 1.00 56.77 C
ANISOU 2349 CB GLU A 322 8150 6245 7174 -1849 1288 -1983 C
ATOM 2350 CG GLU A 322 7.191 6.624 -2.334 1.00 63.07 C
ANISOU 2350 CG GLU A 322 9212 6877 7876 -1780 1347 -1888 C
ATOM 2351 CD GLU A 322 6.872 5.463 -1.414 1.00 72.78 C
ANISOU 2351 CD GLU A 322 10577 7931 9145 -1924 1523 -1871 C
ATOM 2352 OE1 GLU A 322 5.692 5.296 -1.044 1.00 77.38 O
ANISOU 2352 OE1 GLU A 322 11044 8523 9835 -2083 1609 -1931 O
ATOM 2353 OE2 GLU A 322 7.807 4.717 -1.055 1.00 75.71 O
ANISOU 2353 OE2 GLU A 322 11170 8155 9442 -1875 1579 -1795 O
ATOM 2354 N ASP A 323 4.644 9.125 -5.072 1.00 62.95 N
ANISOU 2354 N ASP A 323 8484 7394 8039 -1809 952 -2194 N
ATOM 2355 CA ASP A 323 3.370 9.504 -5.687 1.00 63.27 C
ANISOU 2355 CA ASP A 323 8292 7565 8181 -1898 878 -2325 C
ATOM 2356 C ASP A 323 3.182 11.021 -5.710 1.00 56.16 C
ANISOU 2356 C ASP A 323 7218 6845 7277 -1778 787 -2295 C
ATOM 2357 O ASP A 323 2.185 11.559 -5.222 1.00 53.35 O
ANISOU 2357 O ASP A 323 6689 6572 7010 -1842 820 -2333 O
ATOM 2358 CB ASP A 323 2.200 8.814 -4.982 1.00 67.18 C
ANISOU 2358 CB ASP A 323 8719 8000 8805 -2104 1017 -2396 C
ATOM 2359 CG ASP A 323 2.377 7.312 -4.900 1.00 78.12 C
ANISOU 2359 CG ASP A 323 10285 9194 10203 -2227 1116 -2419 C
ATOM 2360 OD1 ASP A 323 3.148 6.757 -5.713 1.00 81.97 O
ANISOU 2360 OD1 ASP A 323 10905 9620 10620 -2173 1041 -2430 O
ATOM 2361 OD2 ASP A 323 1.749 6.688 -4.022 1.00 83.24 O
ANISOU 2361 OD2 ASP A 323 10945 9750 10932 -2376 1273 -2425 O
ATOM 2362 N VAL A 324 4.159 11.713 -6.285 1.00 50.57 N
ANISOU 2362 N VAL A 324 6555 6193 6467 -1603 673 -2227 N
ATOM 2363 CA VAL A 324 4.033 13.141 -6.555 1.00 44.64 C
ANISOU 2363 CA VAL A 324 5644 5608 5709 -1481 561 -2206 C
ATOM 2364 C VAL A 324 3.222 13.287 -7.837 1.00 45.94 C
ANISOU 2364 C VAL A 324 5651 5889 5914 -1513 416 -2339 C
ATOM 2365 O VAL A 324 3.611 12.728 -8.873 1.00 51.92 O
ANISOU 2365 O VAL A 324 6485 6624 6618 -1497 334 -2384 O
ATOM 2366 CB VAL A 324 5.409 13.813 -6.674 1.00 45.70 C
ANISOU 2366 CB VAL A 324 5890 5750 5725 -1287 503 -2078 C
ATOM 2367 CG1 VAL A 324 5.257 15.310 -6.886 1.00 41.73 C
ANISOU 2367 CG1 VAL A 324 5225 5407 5225 -1167 397 -2050 C
ATOM 2368 CG2 VAL A 324 6.248 13.522 -5.438 1.00 50.00 C
ANISOU 2368 CG2 VAL A 324 6604 6169 6225 -1257 640 -1959 C
ATOM 2369 N PRO A 325 2.091 13.993 -7.815 1.00 47.18 N
ANISOU 2369 N PRO A 325 5592 6172 6163 -1555 379 -2409 N
ATOM 2370 CA PRO A 325 1.243 14.063 -9.013 1.00 50.47 C
ANISOU 2370 CA PRO A 325 5856 6698 6623 -1590 238 -2548 C
ATOM 2371 C PRO A 325 1.998 14.601 -10.221 1.00 55.57 C
ANISOU 2371 C PRO A 325 6536 7420 7160 -1430 73 -2523 C
ATOM 2372 O PRO A 325 2.795 15.536 -10.117 1.00 58.49 O
ANISOU 2372 O PRO A 325 6937 7831 7457 -1275 38 -2406 O
ATOM 2373 CB PRO A 325 0.113 15.007 -8.587 1.00 47.30 C
ANISOU 2373 CB PRO A 325 5222 6426 6324 -1615 229 -2592 C
ATOM 2374 CG PRO A 325 0.037 14.840 -7.105 1.00 43.60 C
ANISOU 2374 CG PRO A 325 4793 5874 5901 -1685 413 -2524 C
ATOM 2375 CD PRO A 325 1.459 14.641 -6.653 1.00 41.64 C
ANISOU 2375 CD PRO A 325 4776 5510 5536 -1585 473 -2380 C
ATOM 2376 N LYS A 326 1.735 13.992 -11.381 1.00 55.62 N
ANISOU 2376 N LYS A 326 6536 7443 7156 -1469 -26 -2636 N
ATOM 2377 CA LYS A 326 2.479 14.328 -12.590 1.00 53.41 C
ANISOU 2377 CA LYS A 326 6311 7224 6759 -1325 -172 -2617 C
ATOM 2378 C LYS A 326 2.204 15.742 -13.081 1.00 52.43 C
ANISOU 2378 C LYS A 326 6029 7271 6622 -1196 -305 -2598 C
ATOM 2379 O LYS A 326 3.006 16.281 -13.852 1.00 52.96 O
ANISOU 2379 O LYS A 326 6153 7387 6581 -1048 -402 -2533 O
ATOM 2380 CB LYS A 326 2.163 13.326 -13.700 1.00 53.26 C
ANISOU 2380 CB LYS A 326 6316 7189 6733 -1401 -249 -2757 C
ATOM 2381 CG LYS A 326 2.961 12.038 -13.611 1.00 55.94 C
ANISOU 2381 CG LYS A 326 6872 7357 7026 -1451 -160 -2744 C
ATOM 2382 CD LYS A 326 2.504 11.046 -14.668 1.00 62.96 C
ANISOU 2382 CD LYS A 326 7770 8226 7927 -1518 -234 -2862 C
ATOM 2383 CE LYS A 326 3.320 9.766 -14.633 1.00 65.16 C
ANISOU 2383 CE LYS A 326 8268 8331 8159 -1552 -155 -2840 C
ATOM 2384 NZ LYS A 326 4.729 10.001 -15.046 1.00 64.10 N
ANISOU 2384 NZ LYS A 326 8294 8185 7875 -1392 -191 -2747 N
ATOM 2385 N HIS A 327 1.097 16.356 -12.665 1.00 51.19 N
ANISOU 2385 N HIS A 327 5676 7203 6571 -1248 -309 -2651 N
ATOM 2386 CA HIS A 327 0.837 17.739 -13.040 1.00 49.82 C
ANISOU 2386 CA HIS A 327 5356 7183 6391 -1120 -431 -2626 C
ATOM 2387 C HIS A 327 1.631 18.732 -12.202 1.00 49.10 C
ANISOU 2387 C HIS A 327 5307 7086 6264 -996 -379 -2465 C
ATOM 2388 O HIS A 327 1.544 19.938 -12.455 1.00 53.81 O
ANISOU 2388 O HIS A 327 5798 7794 6851 -878 -474 -2425 O
ATOM 2389 CB HIS A 327 -0.663 18.046 -12.952 1.00 49.24 C
ANISOU 2389 CB HIS A 327 5048 7214 6448 -1213 -466 -2753 C
ATOM 2390 CG HIS A 327 -1.179 18.180 -11.554 1.00 52.49 C
ANISOU 2390 CG HIS A 327 5387 7592 6964 -1299 -319 -2732 C
ATOM 2391 ND1 HIS A 327 -1.547 17.096 -10.787 1.00 54.81 N
ANISOU 2391 ND1 HIS A 327 5720 7773 7332 -1470 -169 -2780 N
ATOM 2392 CD2 HIS A 327 -1.411 19.275 -10.792 1.00 52.90 C
ANISOU 2392 CD2 HIS A 327 5332 7710 7057 -1236 -297 -2671 C
ATOM 2393 CE1 HIS A 327 -1.974 17.515 -9.610 1.00 54.00 C
ANISOU 2393 CE1 HIS A 327 5540 7674 7305 -1508 -56 -2745 C
ATOM 2394 NE2 HIS A 327 -1.900 18.834 -9.586 1.00 52.80 N
ANISOU 2394 NE2 HIS A 327 5297 7631 7134 -1366 -133 -2683 N
ATOM 2395 N PHE A 328 2.402 18.260 -11.223 1.00 43.03 N
ANISOU 2395 N PHE A 328 4688 6186 5475 -1017 -236 -2373 N
ATOM 2396 CA PHE A 328 3.334 19.137 -10.529 1.00 38.81 C
ANISOU 2396 CA PHE A 328 4216 5638 4893 -886 -199 -2222 C
ATOM 2397 C PHE A 328 4.400 19.633 -11.499 1.00 45.05 C
ANISOU 2397 C PHE A 328 5091 6459 5565 -725 -309 -2143 C
ATOM 2398 O PHE A 328 4.916 18.876 -12.326 1.00 45.33 O
ANISOU 2398 O PHE A 328 5243 6454 5528 -722 -342 -2165 O
ATOM 2399 CB PHE A 328 3.991 18.414 -9.353 1.00 36.42 C
ANISOU 2399 CB PHE A 328 4072 5185 4581 -936 -32 -2148 C
ATOM 2400 CG PHE A 328 3.171 18.425 -8.092 1.00 46.10 C
ANISOU 2400 CG PHE A 328 5214 6395 5908 -1040 92 -2166 C
ATOM 2401 CD1 PHE A 328 1.787 18.458 -8.140 1.00 49.21 C
ANISOU 2401 CD1 PHE A 328 5420 6868 6410 -1150 79 -2288 C
ATOM 2402 CD2 PHE A 328 3.790 18.412 -6.855 1.00 49.03 C
ANISOU 2402 CD2 PHE A 328 5692 6676 6263 -1022 222 -2063 C
ATOM 2403 CE1 PHE A 328 1.039 18.468 -6.975 1.00 49.59 C
ANISOU 2403 CE1 PHE A 328 5387 6904 6549 -1245 204 -2304 C
ATOM 2404 CE2 PHE A 328 3.050 18.420 -5.688 1.00 49.42 C
ANISOU 2404 CE2 PHE A 328 5670 6713 6392 -1111 343 -2077 C
ATOM 2405 CZ PHE A 328 1.672 18.450 -5.747 1.00 49.16 C
ANISOU 2405 CZ PHE A 328 5450 6760 6469 -1225 339 -2195 C
ATOM 2406 N LYS A 329 4.730 20.919 -11.387 1.00 44.27 N
ANISOU 2406 N LYS A 329 4936 6432 5452 -591 -360 -2051 N
ATOM 2407 CA LYS A 329 5.601 21.600 -12.334 1.00 43.21 C
ANISOU 2407 CA LYS A 329 4849 6347 5221 -435 -469 -1974 C
ATOM 2408 C LYS A 329 7.022 21.775 -11.813 1.00 38.99 C
ANISOU 2408 C LYS A 329 4471 5726 4619 -337 -403 -1830 C
ATOM 2409 O LYS A 329 7.777 22.585 -12.363 1.00 38.90 O
ANISOU 2409 O LYS A 329 4480 5756 4545 -200 -475 -1744 O
ATOM 2410 CB LYS A 329 4.998 22.957 -12.698 1.00 43.03 C
ANISOU 2410 CB LYS A 329 4654 6465 5232 -347 -585 -1971 C
ATOM 2411 CG LYS A 329 3.588 22.840 -13.257 1.00 45.44 C
ANISOU 2411 CG LYS A 329 4793 6868 5606 -431 -666 -2119 C
ATOM 2412 CD LYS A 329 2.908 24.186 -13.433 1.00 48.71 C
ANISOU 2412 CD LYS A 329 5028 7413 6066 -346 -770 -2118 C
ATOM 2413 CE LYS A 329 1.504 23.989 -13.986 1.00 54.83 C
ANISOU 2413 CE LYS A 329 5636 8286 6912 -431 -854 -2277 C
ATOM 2414 NZ LYS A 329 0.757 25.261 -14.180 1.00 58.46 N
ANISOU 2414 NZ LYS A 329 5914 8876 7422 -347 -963 -2288 N
ATOM 2415 N TRP A 330 7.399 21.032 -10.774 1.00 37.47 N
ANISOU 2415 N TRP A 330 4387 5412 4439 -403 -267 -1803 N
ATOM 2416 CA TRP A 330 8.744 21.113 -10.214 1.00 36.96 C
ANISOU 2416 CA TRP A 330 4471 5260 4314 -313 -203 -1677 C
ATOM 2417 C TRP A 330 9.794 20.875 -11.289 1.00 31.37 C
ANISOU 2417 C TRP A 330 3883 4538 3498 -223 -265 -1637 C
ATOM 2418 O TRP A 330 9.823 19.809 -11.911 1.00 32.64 O
ANISOU 2418 O TRP A 330 4129 4656 3619 -283 -265 -1702 O
ATOM 2419 CB TRP A 330 8.913 20.081 -9.101 1.00 36.57 C
ANISOU 2419 CB TRP A 330 4539 5076 4281 -409 -55 -1674 C
ATOM 2420 CG TRP A 330 7.954 20.183 -7.964 1.00 36.89 C
ANISOU 2420 CG TRP A 330 4482 5117 4416 -504 31 -1708 C
ATOM 2421 CD1 TRP A 330 6.992 21.133 -7.772 1.00 32.04 C
ANISOU 2421 CD1 TRP A 330 3683 4611 3879 -506 -9 -1742 C
ATOM 2422 CD2 TRP A 330 7.869 19.294 -6.846 1.00 33.67 C
ANISOU 2422 CD2 TRP A 330 4163 4597 4035 -607 177 -1710 C
ATOM 2423 NE1 TRP A 330 6.311 20.885 -6.604 1.00 31.24 N
ANISOU 2423 NE1 TRP A 330 3544 4475 3850 -606 108 -1768 N
ATOM 2424 CE2 TRP A 330 6.832 19.762 -6.016 1.00 30.44 C
ANISOU 2424 CE2 TRP A 330 3612 4238 3717 -670 226 -1745 C
ATOM 2425 CE3 TRP A 330 8.572 18.146 -6.466 1.00 31.78 C
ANISOU 2425 CE3 TRP A 330 4113 4216 3747 -647 273 -1683 C
ATOM 2426 CZ2 TRP A 330 6.481 19.123 -4.828 1.00 31.20 C
ANISOU 2426 CZ2 TRP A 330 3752 4251 3853 -775 373 -1750 C
ATOM 2427 CZ3 TRP A 330 8.219 17.510 -5.289 1.00 30.11 C
ANISOU 2427 CZ3 TRP A 330 3949 3916 3576 -749 414 -1685 C
ATOM 2428 CH2 TRP A 330 7.184 17.999 -4.484 1.00 30.63 C
ANISOU 2428 CH2 TRP A 330 3872 4038 3728 -813 466 -1716 C
ATOM 2429 N GLN A 331 10.666 21.862 -11.498 1.00 34.49 N
ANISOU 2429 N GLN A 331 4287 4967 3849 -79 -313 -1530 N
ATOM 2430 CA GLN A 331 11.793 21.715 -12.409 1.00 35.52 C
ANISOU 2430 CA GLN A 331 4536 5082 3877 17 -354 -1475 C
ATOM 2431 C GLN A 331 13.099 21.394 -11.692 1.00 31.78 C
ANISOU 2431 C GLN A 331 4217 4494 3365 68 -262 -1380 C
ATOM 2432 O GLN A 331 14.079 21.037 -12.356 1.00 32.41 O
ANISOU 2432 O GLN A 331 4410 4542 3361 133 -274 -1343 O
ATOM 2433 CB GLN A 331 11.969 22.983 -13.254 1.00 35.30 C
ANISOU 2433 CB GLN A 331 4424 5166 3823 145 -467 -1416 C
ATOM 2434 CG GLN A 331 10.821 23.247 -14.216 1.00 44.70 C
ANISOU 2434 CG GLN A 331 5482 6476 5025 119 -580 -1509 C
ATOM 2435 CD GLN A 331 11.101 24.400 -15.161 1.00 56.64 C
ANISOU 2435 CD GLN A 331 6942 8089 6492 255 -691 -1441 C
ATOM 2436 OE1 GLN A 331 12.162 24.465 -15.783 1.00 61.12 O
ANISOU 2436 OE1 GLN A 331 7609 8642 6972 347 -704 -1365 O
ATOM 2437 NE2 GLN A 331 10.150 25.320 -15.269 1.00 63.61 N
ANISOU 2437 NE2 GLN A 331 7666 9070 7433 269 -769 -1467 N
ATOM 2438 N SER A 332 13.136 21.510 -10.365 1.00 25.38 N
ANISOU 2438 N SER A 332 3412 3623 2610 46 -173 -1343 N
ATOM 2439 CA SER A 332 14.283 21.084 -9.575 1.00 24.36 C
ANISOU 2439 CA SER A 332 3431 3379 2447 85 -85 -1267 C
ATOM 2440 C SER A 332 13.804 20.661 -8.193 1.00 24.26 C
ANISOU 2440 C SER A 332 3431 3294 2492 -5 25 -1284 C
ATOM 2441 O SER A 332 12.944 21.315 -7.597 1.00 24.40 O
ANISOU 2441 O SER A 332 3323 3366 2583 -38 30 -1302 O
ATOM 2442 CB SER A 332 15.334 22.189 -9.449 1.00 22.76 C
ANISOU 2442 CB SER A 332 3225 3194 2227 232 -113 -1151 C
ATOM 2443 OG SER A 332 15.314 22.752 -8.148 1.00 35.71 O
ANISOU 2443 OG SER A 332 4832 4810 3927 244 -57 -1108 O
ATOM 2444 N LEU A 333 14.370 19.565 -7.691 1.00 32.37 N
ANISOU 2444 N LEU A 333 4617 4199 3485 -41 115 -1276 N
ATOM 2445 CA LEU A 333 14.040 19.026 -6.378 1.00 24.63 C
ANISOU 2445 CA LEU A 333 3683 3133 2541 -123 232 -1281 C
ATOM 2446 C LEU A 333 15.320 18.855 -5.572 1.00 23.70 C
ANISOU 2446 C LEU A 333 3714 2915 2374 -36 294 -1188 C
ATOM 2447 O LEU A 333 16.322 18.349 -6.087 1.00 23.40 O
ANISOU 2447 O LEU A 333 3798 2823 2269 23 281 -1160 O
ATOM 2448 CB LEU A 333 13.295 17.687 -6.507 1.00 26.00 C
ANISOU 2448 CB LEU A 333 3910 3242 2728 -274 289 -1377 C
ATOM 2449 CG LEU A 333 12.939 16.905 -5.241 1.00 28.20 C
ANISOU 2449 CG LEU A 333 4261 3414 3038 -376 425 -1382 C
ATOM 2450 CD1 LEU A 333 12.174 17.771 -4.257 1.00 26.50 C
ANISOU 2450 CD1 LEU A 333 3916 3260 2894 -394 461 -1373 C
ATOM 2451 CD2 LEU A 333 12.132 15.667 -5.608 1.00 28.09 C
ANISOU 2451 CD2 LEU A 333 4277 3345 3050 -531 464 -1485 C
ATOM 2452 N SER A 334 15.289 19.283 -4.310 1.00 27.38 N
ANISOU 2452 N SER A 334 4170 3361 2873 -22 357 -1145 N
ATOM 2453 CA SER A 334 16.484 19.277 -3.472 1.00 28.44 C
ANISOU 2453 CA SER A 334 4429 3413 2964 75 402 -1058 C
ATOM 2454 C SER A 334 16.144 18.693 -2.110 1.00 26.22 C
ANISOU 2454 C SER A 334 4220 3048 2695 6 523 -1057 C
ATOM 2455 O SER A 334 15.352 19.277 -1.363 1.00 28.76 O
ANISOU 2455 O SER A 334 4439 3417 3070 -27 552 -1068 O
ATOM 2456 CB SER A 334 17.057 20.691 -3.324 1.00 35.16 C
ANISOU 2456 CB SER A 334 5192 4335 3832 208 336 -989 C
ATOM 2457 OG SER A 334 18.470 20.660 -3.206 1.00 42.16 O
ANISOU 2457 OG SER A 334 6194 5161 4666 322 333 -915 O
ATOM 2458 N ILE A 335 16.757 17.558 -1.780 1.00 25.73 N
ANISOU 2458 N ILE A 335 4336 2861 2579 -8 594 -1041 N
ATOM 2459 CA ILE A 335 16.533 16.864 -0.517 1.00 28.74 C
ANISOU 2459 CA ILE A 335 4818 3146 2956 -69 716 -1029 C
ATOM 2460 C ILE A 335 17.883 16.730 0.172 1.00 28.30 C
ANISOU 2460 C ILE A 335 4915 3005 2834 55 738 -946 C
ATOM 2461 O ILE A 335 18.715 15.908 -0.233 1.00 28.33 O
ANISOU 2461 O ILE A 335 5039 2933 2791 85 729 -924 O
ATOM 2462 CB ILE A 335 15.878 15.494 -0.731 1.00 28.47 C
ANISOU 2462 CB ILE A 335 4865 3028 2925 -216 788 -1095 C
ATOM 2463 CG1 ILE A 335 14.606 15.651 -1.563 1.00 27.77 C
ANISOU 2463 CG1 ILE A 335 4612 3033 2906 -330 745 -1188 C
ATOM 2464 CG2 ILE A 335 15.556 14.838 0.598 1.00 32.12 C
ANISOU 2464 CG2 ILE A 335 5425 3392 3386 -285 924 -1075 C
ATOM 2465 CD1 ILE A 335 14.272 14.440 -2.387 1.00 33.81 C
ANISOU 2465 CD1 ILE A 335 5441 3736 3668 -439 755 -1264 C
ATOM 2466 N ILE A 336 18.103 17.529 1.213 1.00 25.50 N
ANISOU 2466 N ILE A 336 4533 2670 2484 129 754 -896 N
ATOM 2467 CA ILE A 336 19.406 17.653 1.855 1.00 26.84 C
ANISOU 2467 CA ILE A 336 4765 2804 2629 257 724 -794 C
ATOM 2468 C ILE A 336 19.256 17.366 3.342 1.00 30.15 C
ANISOU 2468 C ILE A 336 5250 3168 3039 242 813 -753 C
ATOM 2469 O ILE A 336 18.351 17.901 3.994 1.00 30.53 O
ANISOU 2469 O ILE A 336 5245 3250 3103 203 873 -793 O
ATOM 2470 CB ILE A 336 20.009 19.053 1.624 1.00 28.96 C
ANISOU 2470 CB ILE A 336 4912 3167 2924 379 624 -758 C
ATOM 2471 CG1 ILE A 336 20.278 19.268 0.132 1.00 29.90 C
ANISOU 2471 CG1 ILE A 336 4987 3335 3039 404 540 -783 C
ATOM 2472 CG2 ILE A 336 21.278 19.245 2.435 1.00 29.25 C
ANISOU 2472 CG2 ILE A 336 4965 3181 2967 480 585 -650 C
ATOM 2473 CD1 ILE A 336 20.893 20.605 -0.198 1.00 36.01 C
ANISOU 2473 CD1 ILE A 336 5649 4191 3843 519 448 -740 C
ATOM 2474 N ARG A 337 20.146 16.522 3.873 1.00 25.01 N
ANISOU 2474 N ARG A 337 4714 2431 2356 276 823 -674 N
ATOM 2475 CA ARG A 337 20.188 16.200 5.304 1.00 22.86 C
ANISOU 2475 CA ARG A 337 4527 2100 2060 281 897 -619 C
ATOM 2476 C ARG A 337 18.827 15.748 5.819 1.00 25.59 C
ANISOU 2476 C ARG A 337 4914 2408 2400 149 1035 -684 C
ATOM 2477 O ARG A 337 18.424 16.077 6.935 1.00 36.31 O
ANISOU 2477 O ARG A 337 6272 3773 3751 150 1100 -670 O
ATOM 2478 CB ARG A 337 20.702 17.387 6.125 1.00 22.10 C
ANISOU 2478 CB ARG A 337 4345 2072 1981 392 839 -568 C
ATOM 2479 CG ARG A 337 22.051 17.910 5.681 1.00 25.80 C
ANISOU 2479 CG ARG A 337 4760 2576 2467 503 716 -507 C
ATOM 2480 CD ARG A 337 22.628 18.881 6.690 1.00 29.09 C
ANISOU 2480 CD ARG A 337 5117 3034 2900 595 670 -453 C
ATOM 2481 NE ARG A 337 21.587 19.686 7.316 1.00 45.65 N
ANISOU 2481 NE ARG A 337 7143 5186 5017 574 712 -502 N
ATOM 2482 CZ ARG A 337 21.158 20.849 6.841 1.00 47.37 C
ANISOU 2482 CZ ARG A 337 7222 5494 5284 593 667 -548 C
ATOM 2483 NH1 ARG A 337 20.205 21.509 7.480 1.00 37.90 N
ANISOU 2483 NH1 ARG A 337 5959 4342 4099 577 713 -593 N
ATOM 2484 NH2 ARG A 337 21.685 21.356 5.734 1.00 52.59 N
ANISOU 2484 NH2 ARG A 337 7808 6196 5976 631 579 -546 N
ATOM 2485 N CYS A 338 18.112 14.995 4.996 1.00 26.76 N
ANISOU 2485 N CYS A 338 5091 2520 2556 28 1082 -762 N
ATOM 2486 CA CYS A 338 16.805 14.478 5.357 1.00 25.87 C
ANISOU 2486 CA CYS A 338 5007 2367 2454 -128 1223 -839 C
ATOM 2487 C CYS A 338 16.942 13.026 5.829 1.00 33.11 C
ANISOU 2487 C CYS A 338 6110 3136 3332 -193 1320 -802 C
ATOM 2488 O CYS A 338 18.055 12.542 6.075 1.00 28.59 O
ANISOU 2488 O CYS A 338 5639 2504 2720 -100 1277 -708 O
ATOM 2489 CB CYS A 338 15.853 14.646 4.173 1.00 26.18 C
ANISOU 2489 CB CYS A 338 4894 2488 2565 -235 1178 -932 C
ATOM 2490 SG CYS A 338 15.430 16.367 3.814 1.00 38.43 S
ANISOU 2490 SG CYS A 338 6196 4224 4183 -174 1066 -954 S
ATOM 2491 N GLN A 339 15.817 12.325 5.976 1.00 33.11 N
ANISOU 2491 N GLN A 339 6144 3082 3356 -357 1448 -871 N
ATOM 2492 CA GLN A 339 15.821 11.013 6.619 1.00 31.29 C
ANISOU 2492 CA GLN A 339 6111 2693 3084 -428 1575 -841 C
ATOM 2493 C GLN A 339 15.035 10.000 5.802 1.00 39.65 C
ANISOU 2493 C GLN A 339 7170 3694 4201 -598 1612 -916 C
ATOM 2494 O GLN A 339 14.229 9.235 6.342 1.00 45.90 O
ANISOU 2494 O GLN A 339 8012 4409 5018 -734 1741 -926 O
ATOM 2495 CB GLN A 339 15.260 11.097 8.037 1.00 32.52 C
ANISOU 2495 CB GLN A 339 6297 2835 3224 -459 1705 -801 C
ATOM 2496 CG GLN A 339 15.868 12.205 8.868 1.00 34.33 C
ANISOU 2496 CG GLN A 339 6480 3146 3416 -300 1650 -731 C
ATOM 2497 CD GLN A 339 15.256 12.284 10.238 1.00 41.08 C
ANISOU 2497 CD GLN A 339 7374 3990 4243 -330 1788 -705 C
ATOM 2498 OE1 GLN A 339 14.394 11.481 10.588 1.00 39.23 O
ANISOU 2498 OE1 GLN A 339 7192 3689 4024 -474 1926 -721 O
ATOM 2499 NE2 GLN A 339 15.697 13.253 11.030 1.00 39.15 N
ANISOU 2499 NE2 GLN A 339 7068 3824 3982 -199 1725 -643 N
ATOM 2500 N LEU A 340 15.273 9.965 4.494 1.00 33.10 N
ANISOU 2500 N LEU A 340 6287 2897 3392 -591 1502 -970 N
ATOM 2501 CA LEU A 340 14.583 9.005 3.645 1.00 38.82 C
ANISOU 2501 CA LEU A 340 7012 3568 4171 -744 1521 -1052 C
ATOM 2502 C LEU A 340 15.004 7.584 3.995 1.00 41.28 C
ANISOU 2502 C LEU A 340 7559 3689 4438 -782 1615 -1022 C
ATOM 2503 O LEU A 340 16.191 7.245 3.960 1.00 43.72 O
ANISOU 2503 O LEU A 340 7958 3964 4688 -653 1549 -928 O
ATOM 2504 CB LEU A 340 14.866 9.292 2.171 1.00 30.94 C
ANISOU 2504 CB LEU A 340 5922 2647 3186 -705 1375 -1113 C
ATOM 2505 CG LEU A 340 14.211 10.561 1.629 1.00 35.90 C
ANISOU 2505 CG LEU A 340 6310 3458 3874 -699 1282 -1159 C
ATOM 2506 CD1 LEU A 340 14.383 10.657 0.125 1.00 37.48 C
ANISOU 2506 CD1 LEU A 340 6439 3722 4081 -679 1151 -1222 C
ATOM 2507 CD2 LEU A 340 12.740 10.603 2.014 1.00 33.65 C
ANISOU 2507 CD2 LEU A 340 5893 3216 3679 -858 1360 -1217 C
ATOM 2508 N LYS A 341 14.019 6.756 4.350 1.00 39.02 N
ANISOU 2508 N LYS A 341 7299 3322 4204 -953 1737 -1054 N
ATOM 2509 CA LYS A 341 14.252 5.336 4.582 1.00 48.91 C
ANISOU 2509 CA LYS A 341 8767 4384 5432 -1015 1831 -1034 C
ATOM 2510 C LYS A 341 14.423 4.550 3.290 1.00 53.15 C
ANISOU 2510 C LYS A 341 9295 4901 5997 -1048 1739 -1084 C
ATOM 2511 O LYS A 341 14.933 3.424 3.325 1.00 58.86 O
ANISOU 2511 O LYS A 341 10162 5512 6690 -1041 1761 -1032 O
ATOM 2512 CB LYS A 341 13.085 4.726 5.362 1.00 57.61 C
ANISOU 2512 CB LYS A 341 9880 5414 6595 -1196 1995 -1045 C
ATOM 2513 CG LYS A 341 13.065 5.039 6.843 1.00 62.50 C
ANISOU 2513 CG LYS A 341 10561 6022 7165 -1156 2110 -949 C
ATOM 2514 CD LYS A 341 11.878 4.368 7.518 1.00 68.42 C
ANISOU 2514 CD LYS A 341 11318 6700 7980 -1347 2282 -960 C
ATOM 2515 CE LYS A 341 12.077 4.297 9.020 1.00 73.84 C
ANISOU 2515 CE LYS A 341 12150 7321 8585 -1298 2416 -848 C
ATOM 2516 NZ LYS A 341 12.265 5.644 9.614 1.00 72.70 N
ANISOU 2516 NZ LYS A 341 11894 7329 8399 -1165 2368 -811 N
ATOM 2517 N GLN A 342 14.014 5.119 2.159 1.00 47.59 N
ANISOU 2517 N GLN A 342 8428 4311 5344 -1075 1634 -1185 N
ATOM 2518 CA GLN A 342 13.838 4.367 0.924 1.00 43.61 C
ANISOU 2518 CA GLN A 342 7898 3792 4880 -1142 1564 -1263 C
ATOM 2519 C GLN A 342 13.927 5.347 -0.235 1.00 39.94 C
ANISOU 2519 C GLN A 342 7271 3485 4420 -1072 1411 -1326 C
ATOM 2520 O GLN A 342 13.344 6.434 -0.167 1.00 38.31 O
ANISOU 2520 O GLN A 342 6914 3398 4244 -1082 1392 -1364 O
ATOM 2521 CB GLN A 342 12.487 3.635 0.953 1.00 46.80 C
ANISOU 2521 CB GLN A 342 8272 4124 5384 -1368 1669 -1362 C
ATOM 2522 CG GLN A 342 12.000 3.053 -0.355 1.00 54.16 C
ANISOU 2522 CG GLN A 342 9127 5073 6380 -1459 1588 -1474 C
ATOM 2523 CD GLN A 342 10.803 2.138 -0.153 1.00 61.01 C
ANISOU 2523 CD GLN A 342 9981 5849 7349 -1675 1702 -1545 C
ATOM 2524 OE1 GLN A 342 10.743 1.387 0.821 1.00 63.19 O
ANISOU 2524 OE1 GLN A 342 10389 5996 7625 -1731 1840 -1478 O
ATOM 2525 NE2 GLN A 342 9.841 2.206 -1.065 1.00 66.04 N
ANISOU 2525 NE2 GLN A 342 10454 6561 8078 -1792 1643 -1678 N
ATOM 2526 N PHE A 343 14.672 4.974 -1.275 1.00 38.12 N
ANISOU 2526 N PHE A 343 7058 3267 4158 -990 1298 -1324 N
ATOM 2527 CA PHE A 343 14.921 5.895 -2.375 1.00 34.43 C
ANISOU 2527 CA PHE A 343 6460 2945 3678 -901 1155 -1365 C
ATOM 2528 C PHE A 343 13.598 6.337 -2.996 1.00 36.13 C
ANISOU 2528 C PHE A 343 6513 3246 3969 -1041 1134 -1507 C
ATOM 2529 O PHE A 343 12.675 5.527 -3.131 1.00 43.75 O
ANISOU 2529 O PHE A 343 7471 4150 5004 -1204 1188 -1591 O
ATOM 2530 CB PHE A 343 15.817 5.251 -3.435 1.00 35.17 C
ANISOU 2530 CB PHE A 343 6606 3027 3732 -815 1055 -1354 C
ATOM 2531 CG PHE A 343 16.450 6.240 -4.373 1.00 32.96 C
ANISOU 2531 CG PHE A 343 6226 2885 3413 -678 920 -1350 C
ATOM 2532 CD1 PHE A 343 17.581 6.946 -3.993 1.00 31.24 C
ANISOU 2532 CD1 PHE A 343 6016 2710 3143 -512 883 -1237 C
ATOM 2533 CD2 PHE A 343 15.907 6.478 -5.625 1.00 32.47 C
ANISOU 2533 CD2 PHE A 343 6057 2911 3368 -716 830 -1460 C
ATOM 2534 CE1 PHE A 343 18.164 7.862 -4.845 1.00 29.59 C
ANISOU 2534 CE1 PHE A 343 5714 2623 2906 -394 770 -1228 C
ATOM 2535 CE2 PHE A 343 16.487 7.395 -6.484 1.00 32.49 C
ANISOU 2535 CE2 PHE A 343 5981 3039 3327 -589 715 -1450 C
ATOM 2536 CZ PHE A 343 17.619 8.087 -6.093 1.00 33.51 C
ANISOU 2536 CZ PHE A 343 6121 3202 3410 -430 691 -1332 C
ATOM 2537 N PRO A 344 13.461 7.612 -3.355 1.00 37.61 N
ANISOU 2537 N PRO A 344 6545 3589 4157 -977 1050 -1522 N
ATOM 2538 CA PRO A 344 12.171 8.099 -3.850 1.00 33.87 C
ANISOU 2538 CA PRO A 344 5861 3238 3771 -1083 1007 -1616 C
ATOM 2539 C PRO A 344 11.772 7.435 -5.156 1.00 46.50 C
ANISOU 2539 C PRO A 344 7435 4841 5393 -1160 930 -1737 C
ATOM 2540 O PRO A 344 12.612 7.069 -5.982 1.00 51.07 O
ANISOU 2540 O PRO A 344 8111 5391 5904 -1081 862 -1744 O
ATOM 2541 CB PRO A 344 12.411 9.600 -4.056 1.00 32.37 C
ANISOU 2541 CB PRO A 344 5524 3216 3561 -949 905 -1573 C
ATOM 2542 CG PRO A 344 13.637 9.923 -3.291 1.00 38.67 C
ANISOU 2542 CG PRO A 344 6443 3968 4280 -801 931 -1450 C
ATOM 2543 CD PRO A 344 14.469 8.683 -3.287 1.00 35.17 C
ANISOU 2543 CD PRO A 344 6219 3363 3780 -793 979 -1433 C
ATOM 2544 N THR A 345 10.463 7.280 -5.329 1.00 52.86 N
ANISOU 2544 N THR A 345 8105 5683 6296 -1316 943 -1839 N
ATOM 2545 CA THR A 345 9.874 6.923 -6.611 1.00 60.78 C
ANISOU 2545 CA THR A 345 9028 6733 7333 -1387 846 -1972 C
ATOM 2546 C THR A 345 9.334 8.201 -7.239 1.00 59.18 C
ANISOU 2546 C THR A 345 8606 6729 7150 -1336 724 -2005 C
ATOM 2547 O THR A 345 8.405 8.817 -6.704 1.00 54.28 O
ANISOU 2547 O THR A 345 7832 6186 6606 -1398 753 -2019 O
ATOM 2548 CB THR A 345 8.766 5.882 -6.452 1.00 65.59 C
ANISOU 2548 CB THR A 345 9623 7250 8047 -1595 930 -2075 C
ATOM 2549 OG1 THR A 345 7.822 6.330 -5.471 1.00 67.27 O
ANISOU 2549 OG1 THR A 345 9713 7501 8344 -1685 1021 -2062 O
ATOM 2550 CG2 THR A 345 9.347 4.542 -6.020 1.00 62.01 C
ANISOU 2550 CG2 THR A 345 9391 6599 7572 -1629 1030 -2030 C
ATOM 2551 N LEU A 346 9.933 8.607 -8.358 1.00 54.62 N
ANISOU 2551 N LEU A 346 8019 6234 6500 -1217 592 -2014 N
ATOM 2552 CA LEU A 346 9.647 9.893 -8.978 1.00 51.85 C
ANISOU 2552 CA LEU A 346 7488 6066 6146 -1134 470 -2021 C
ATOM 2553 C LEU A 346 9.515 9.702 -10.480 1.00 54.58 C
ANISOU 2553 C LEU A 346 7797 6481 6462 -1123 337 -2124 C
ATOM 2554 O LEU A 346 10.356 9.043 -11.098 1.00 56.22 O
ANISOU 2554 O LEU A 346 8148 6622 6592 -1070 312 -2125 O
ATOM 2555 CB LEU A 346 10.760 10.908 -8.686 1.00 47.16 C
ANISOU 2555 CB LEU A 346 6926 5519 5473 -952 445 -1885 C
ATOM 2556 CG LEU A 346 11.170 11.189 -7.239 1.00 45.52 C
ANISOU 2556 CG LEU A 346 6778 5249 5268 -920 559 -1771 C
ATOM 2557 CD1 LEU A 346 12.586 11.747 -7.202 1.00 39.37 C
ANISOU 2557 CD1 LEU A 346 6093 4471 4396 -739 527 -1654 C
ATOM 2558 CD2 LEU A 346 10.204 12.155 -6.578 1.00 46.08 C
ANISOU 2558 CD2 LEU A 346 6667 5421 5419 -957 575 -1771 C
ATOM 2559 N ASP A 347 8.466 10.282 -11.066 1.00 52.36 N
ANISOU 2559 N ASP A 347 7359 6733 5805 -664 1186 -1705 N
ATOM 2560 CA ASP A 347 8.301 10.292 -12.515 1.00 54.09 C
ANISOU 2560 CA ASP A 347 7446 7047 6059 -771 1163 -1746 C
ATOM 2561 C ASP A 347 7.953 11.686 -13.024 1.00 54.49 C
ANISOU 2561 C ASP A 347 7396 7210 6097 -690 1036 -1758 C
ATOM 2562 O ASP A 347 7.304 11.824 -14.062 1.00 65.42 O
ANISOU 2562 O ASP A 347 8641 8709 7508 -784 1031 -1816 O
ATOM 2563 CB ASP A 347 7.247 9.277 -12.963 1.00 59.98 C
ANISOU 2563 CB ASP A 347 8110 7837 6843 -967 1301 -1831 C
ATOM 2564 CG ASP A 347 5.929 9.418 -12.218 1.00 71.47 C
ANISOU 2564 CG ASP A 347 9533 9336 8288 -986 1369 -1894 C
ATOM 2565 OD1 ASP A 347 5.489 10.558 -11.958 1.00 75.01 O
ANISOU 2565 OD1 ASP A 347 9940 9854 8708 -879 1286 -1899 O
ATOM 2566 OD2 ASP A 347 5.314 8.376 -11.919 1.00 77.45 O
ANISOU 2566 OD2 ASP A 347 10305 10056 9066 -1113 1509 -1940 O
ATOM 2567 N LEU A 348 8.378 12.728 -12.301 1.00 46.16 N
ANISOU 2567 N LEU A 348 6412 6126 5002 -516 933 -1704 N
ATOM 2568 CA LEU A 348 8.098 14.106 -12.683 1.00 39.76 C
ANISOU 2568 CA LEU A 348 5530 5402 4176 -432 814 -1704 C
ATOM 2569 C LEU A 348 8.701 14.396 -14.053 1.00 46.60 C
ANISOU 2569 C LEU A 348 6317 6319 5071 -467 735 -1690 C
ATOM 2570 O LEU A 348 9.927 14.373 -14.216 1.00 48.94 O
ANISOU 2570 O LEU A 348 6685 6542 5367 -412 679 -1627 O
ATOM 2571 CB LEU A 348 8.633 15.078 -11.630 1.00 35.69 C
ANISOU 2571 CB LEU A 348 5132 4817 3612 -240 722 -1639 C
ATOM 2572 CG LEU A 348 7.999 14.921 -10.243 1.00 40.13 C
ANISOU 2572 CG LEU A 348 5766 5342 4140 -185 791 -1651 C
ATOM 2573 CD1 LEU A 348 8.511 15.980 -9.278 1.00 32.66 C
ANISOU 2573 CD1 LEU A 348 4926 4340 3142 12 687 -1591 C
ATOM 2574 CD2 LEU A 348 6.481 14.962 -10.336 1.00 44.19 C
ANISOU 2574 CD2 LEU A 348 6170 5959 4661 -275 866 -1733 C
ATOM 2575 N PRO A 349 7.869 14.657 -15.068 1.00 47.05 N
ANISOU 2575 N PRO A 349 6217 6507 5151 -557 730 -1752 N
ATOM 2576 CA PRO A 349 8.394 14.790 -16.436 1.00 42.45 C
ANISOU 2576 CA PRO A 349 5550 5981 4597 -602 671 -1744 C
ATOM 2577 C PRO A 349 9.101 16.104 -16.713 1.00 37.18 C
ANISOU 2577 C PRO A 349 4896 5315 3916 -474 528 -1682 C
ATOM 2578 O PRO A 349 9.820 16.189 -17.716 1.00 38.25 O
ANISOU 2578 O PRO A 349 4996 5466 4071 -490 478 -1656 O
ATOM 2579 CB PRO A 349 7.136 14.657 -17.313 1.00 45.35 C
ANISOU 2579 CB PRO A 349 5739 6501 4990 -731 715 -1839 C
ATOM 2580 CG PRO A 349 6.055 14.139 -16.393 1.00 45.63 C
ANISOU 2580 CG PRO A 349 5780 6539 5020 -782 820 -1900 C
ATOM 2581 CD PRO A 349 6.399 14.666 -15.041 1.00 47.70 C
ANISOU 2581 CD PRO A 349 6186 6698 5240 -634 790 -1840 C
ATOM 2582 N PHE A 350 8.915 17.128 -15.881 1.00 35.05 N
ANISOU 2582 N PHE A 350 4676 5028 3615 -354 465 -1656 N
ATOM 2583 CA PHE A 350 9.558 18.419 -16.085 1.00 36.85 C
ANISOU 2583 CA PHE A 350 4921 5247 3834 -245 337 -1595 C
ATOM 2584 C PHE A 350 10.746 18.633 -15.156 1.00 31.24 C
ANISOU 2584 C PHE A 350 4389 4383 3096 -128 294 -1509 C
ATOM 2585 O PHE A 350 11.312 19.732 -15.134 1.00 35.53 O
ANISOU 2585 O PHE A 350 4965 4900 3635 -49 200 -1453 O
ATOM 2586 CB PHE A 350 8.548 19.553 -15.900 1.00 42.23 C
ANISOU 2586 CB PHE A 350 5520 6021 4504 -200 289 -1625 C
ATOM 2587 CG PHE A 350 7.352 19.460 -16.805 1.00 51.37 C
ANISOU 2587 CG PHE A 350 6492 7341 5685 -299 317 -1713 C
ATOM 2588 CD1 PHE A 350 7.489 19.053 -18.123 1.00 48.73 C
ANISOU 2588 CD1 PHE A 350 6054 7079 5381 -389 320 -1736 C
ATOM 2589 CD2 PHE A 350 6.088 19.776 -16.335 1.00 60.65 C
ANISOU 2589 CD2 PHE A 350 7597 8599 6847 -300 342 -1775 C
ATOM 2590 CE1 PHE A 350 6.386 18.966 -18.954 1.00 48.26 C
ANISOU 2590 CE1 PHE A 350 5826 7172 5339 -477 347 -1819 C
ATOM 2591 CE2 PHE A 350 4.982 19.690 -17.159 1.00 60.77 C
ANISOU 2591 CE2 PHE A 350 7437 8770 6882 -390 366 -1861 C
ATOM 2592 CZ PHE A 350 5.131 19.285 -18.471 1.00 54.43 C
ANISOU 2592 CZ PHE A 350 6533 8038 6108 -478 367 -1884 C
ATOM 2593 N LEU A 351 11.139 17.612 -14.398 1.00 26.12 N
ANISOU 2593 N LEU A 351 3850 3641 2435 -122 364 -1499 N
ATOM 2594 CA LEU A 351 12.221 17.745 -13.432 1.00 32.57 C
ANISOU 2594 CA LEU A 351 4834 4322 3219 3 321 -1425 C
ATOM 2595 C LEU A 351 13.565 17.714 -14.152 1.00 30.14 C
ANISOU 2595 C LEU A 351 4557 3965 2931 14 258 -1371 C
ATOM 2596 O LEU A 351 13.898 16.727 -14.817 1.00 32.32 O
ANISOU 2596 O LEU A 351 4788 4256 3238 -67 303 -1390 O
ATOM 2597 CB LEU A 351 12.135 16.630 -12.393 1.00 26.89 C
ANISOU 2597 CB LEU A 351 4183 3548 2486 15 410 -1445 C
ATOM 2598 CG LEU A 351 13.018 16.799 -11.156 1.00 27.44 C
ANISOU 2598 CG LEU A 351 4386 3518 2521 178 353 -1395 C
ATOM 2599 CD1 LEU A 351 12.452 17.868 -10.237 1.00 30.64 C
ANISOU 2599 CD1 LEU A 351 4850 3902 2890 270 322 -1361 C
ATOM 2600 CD2 LEU A 351 13.185 15.482 -10.414 1.00 24.43 C
ANISOU 2600 CD2 LEU A 351 4014 3110 2159 141 449 -1425 C
ATOM 2601 N LYS A 352 14.335 18.792 -14.018 1.00 25.68 N
ANISOU 2601 N LYS A 352 4070 3336 2352 82 176 -1299 N
ATOM 2602 CA LYS A 352 15.636 18.907 -14.664 1.00 26.69 C
ANISOU 2602 CA LYS A 352 4231 3413 2498 79 124 -1242 C
ATOM 2603 C LYS A 352 16.802 18.644 -13.725 1.00 28.34 C
ANISOU 2603 C LYS A 352 4560 3490 2717 129 128 -1142 C
ATOM 2604 O LYS A 352 17.835 18.132 -14.172 1.00 33.40 O
ANISOU 2604 O LYS A 352 5206 4103 3381 152 91 -1111 O
ATOM 2605 CB LYS A 352 15.790 20.300 -15.291 1.00 23.27 C
ANISOU 2605 CB LYS A 352 3703 3040 2098 49 58 -1218 C
ATOM 2606 CG LYS A 352 14.785 20.591 -16.403 1.00 32.93 C
ANISOU 2606 CG LYS A 352 4751 4414 3348 10 30 -1277 C
ATOM 2607 CD LYS A 352 14.503 22.084 -16.533 1.00 44.17 C
ANISOU 2607 CD LYS A 352 6075 5913 4794 54 -53 -1266 C
ATOM 2608 CE LYS A 352 15.365 22.758 -17.598 1.00 50.25 C
ANISOU 2608 CE LYS A 352 6776 6713 5603 64 -132 -1227 C
ATOM 2609 NZ LYS A 352 14.955 22.396 -18.986 1.00 55.32 N
ANISOU 2609 NZ LYS A 352 7312 7450 6256 0 -127 -1268 N
ATOM 2610 N SER A 353 16.662 18.964 -12.440 1.00 24.76 N
ANISOU 2610 N SER A 353 4164 2978 2266 81 218 -1112 N
ATOM 2611 CA SER A 353 17.733 18.789 -11.470 1.00 26.93 C
ANISOU 2611 CA SER A 353 4167 3375 2689 -17 293 -1235 C
ATOM 2612 C SER A 353 17.198 18.040 -10.258 1.00 27.83 C
ANISOU 2612 C SER A 353 4172 3573 2831 110 262 -1342 C
ATOM 2613 O SER A 353 16.097 18.331 -9.781 1.00 21.91 O
ANISOU 2613 O SER A 353 3390 2867 2069 99 295 -1379 O
ATOM 2614 CB SER A 353 18.316 20.148 -11.054 1.00 25.77 C
ANISOU 2614 CB SER A 353 4078 3194 2519 128 164 -1191 C
ATOM 2615 OG SER A 353 18.778 20.867 -12.186 1.00 43.07 O
ANISOU 2615 OG SER A 353 6241 5406 4719 146 69 -1136 O
ATOM 2616 N LEU A 354 17.968 17.067 -9.774 1.00 24.13 N
ANISOU 2616 N LEU A 354 3802 3027 2339 195 247 -1330 N
ATOM 2617 CA LEU A 354 17.615 16.308 -8.579 1.00 23.22 C
ANISOU 2617 CA LEU A 354 3801 2845 2175 245 306 -1347 C
ATOM 2618 C LEU A 354 18.834 16.217 -7.676 1.00 25.13 C
ANISOU 2618 C LEU A 354 4182 2946 2419 271 319 -1235 C
ATOM 2619 O LEU A 354 19.883 15.718 -8.097 1.00 21.68 O
ANISOU 2619 O LEU A 354 3786 2457 1993 264 305 -1184 O
ATOM 2620 CB LEU A 354 17.111 14.903 -8.929 1.00 23.07 C
ANISOU 2620 CB LEU A 354 3870 2793 2102 233 367 -1352 C
ATOM 2621 CG LEU A 354 16.805 14.001 -7.727 1.00 28.26 C
ANISOU 2621 CG LEU A 354 4646 3357 2734 210 485 -1324 C
ATOM 2622 CD1 LEU A 354 15.774 14.645 -6.810 1.00 31.93 C
ANISOU 2622 CD1 LEU A 354 5090 3864 3177 259 493 -1365 C
ATOM 2623 CD2 LEU A 354 16.341 12.616 -8.166 1.00 24.83 C
ANISOU 2623 CD2 LEU A 354 4277 2876 2279 100 611 -1321 C
ATOM 2624 N THR A 355 18.694 16.696 -6.441 1.00 28.30 N
ANISOU 2624 N THR A 355 4667 3287 2799 335 320 -1180 N
ATOM 2625 CA THR A 355 19.741 16.599 -5.432 1.00 25.79 C
ANISOU 2625 CA THR A 355 4499 2843 2457 424 289 -1054 C
ATOM 2626 C THR A 355 19.185 15.845 -4.231 1.00 30.50 C
ANISOU 2626 C THR A 355 5198 3380 3012 446 374 -1050 C
ATOM 2627 O THR A 355 18.233 16.304 -3.587 1.00 33.12 O
ANISOU 2627 O THR A 355 5517 3739 3329 467 394 -1083 O
ATOM 2628 CB THR A 355 20.255 17.982 -5.013 1.00 23.34 C
ANISOU 2628 CB THR A 355 4216 2511 2142 534 164 -959 C
ATOM 2629 OG1 THR A 355 20.948 18.594 -6.105 1.00 29.63 O
ANISOU 2629 OG1 THR A 355 4945 3341 2971 526 82 -937 O
ATOM 2630 CG2 THR A 355 21.214 17.856 -3.846 1.00 24.57 C
ANISOU 2630 CG2 THR A 355 4518 2563 2254 648 115 -840 C
ATOM 2631 N LEU A 356 19.763 14.680 -3.951 1.00 28.00 N
ANISOU 2631 N LEU A 356 4988 2979 2673 435 432 -1007 N
ATOM 2632 CA LEU A 356 19.479 13.913 -2.743 1.00 25.94 C
ANISOU 2632 CA LEU A 356 4861 2631 2364 460 518 -971 C
ATOM 2633 C LEU A 356 20.825 13.625 -2.095 1.00 30.63 C
ANISOU 2633 C LEU A 356 5597 3118 2924 537 480 -849 C
ATOM 2634 O LEU A 356 21.581 12.777 -2.583 1.00 31.13 O
ANISOU 2634 O LEU A 356 5696 3144 2989 499 504 -828 O
ATOM 2635 CB LEU A 356 18.722 12.623 -3.065 1.00 30.50 C
ANISOU 2635 CB LEU A 356 5447 3207 2936 358 648 -1034 C
ATOM 2636 CG LEU A 356 18.535 11.606 -1.935 1.00 35.25 C
ANISOU 2636 CG LEU A 356 6207 3698 3489 360 764 -986 C
ATOM 2637 CD1 LEU A 356 17.860 12.240 -0.733 1.00 42.40 C
ANISOU 2637 CD1 LEU A 356 7151 4594 4366 434 767 -977 C
ATOM 2638 CD2 LEU A 356 17.729 10.420 -2.425 1.00 37.33 C
ANISOU 2638 CD2 LEU A 356 6471 3959 3753 240 896 -1043 C
ATOM 2639 N THR A 357 21.138 14.338 -1.013 1.00 28.47 N
ANISOU 2639 N THR A 357 5403 2802 2611 652 412 -769 N
ATOM 2640 CA THR A 357 22.488 14.308 -0.473 1.00 26.50 C
ANISOU 2640 CA THR A 357 5269 2482 2319 746 335 -655 C
ATOM 2641 C THR A 357 22.461 14.354 1.049 1.00 31.52 C
ANISOU 2641 C THR A 357 6045 3049 2880 850 336 -581 C
ATOM 2642 O THR A 357 21.532 14.894 1.662 1.00 27.06 O
ANISOU 2642 O THR A 357 5471 2504 2308 876 348 -603 O
ATOM 2643 CB THR A 357 23.326 15.469 -1.025 1.00 26.72 C
ANISOU 2643 CB THR A 357 5226 2558 2368 807 181 -616 C
ATOM 2644 OG1 THR A 357 24.714 15.247 -0.748 1.00 30.59 O
ANISOU 2644 OG1 THR A 357 5807 2998 2816 878 111 -524 O
ATOM 2645 CG2 THR A 357 22.894 16.780 -0.402 1.00 28.82 C
ANISOU 2645 CG2 THR A 357 5472 2859 2621 898 89 -593 C
ATOM 2646 N MET A 358 23.499 13.769 1.649 1.00 29.40 N
ANISOU 2646 N MET A 358 5910 2707 2552 910 321 -494 N
ATOM 2647 CA MET A 358 23.676 13.755 3.101 1.00 25.81 C
ANISOU 2647 CA MET A 358 5606 2190 2011 1020 310 -412 C
ATOM 2648 C MET A 358 22.460 13.158 3.807 1.00 26.88 C
ANISOU 2648 C MET A 358 5796 2283 2133 980 453 -448 C
ATOM 2649 O MET A 358 22.115 13.554 4.922 1.00 32.09 O
ANISOU 2649 O MET A 358 6532 2921 2741 1063 442 -410 O
ATOM 2650 CB MET A 358 23.986 15.158 3.629 1.00 25.25 C
ANISOU 2650 CB MET A 358 5522 2163 1910 1143 152 -360 C
ATOM 2651 CG MET A 358 25.191 15.808 2.956 1.00 35.48 C
ANISOU 2651 CG MET A 358 6762 3504 3215 1184 4 -323 C
ATOM 2652 SD MET A 358 25.529 17.485 3.526 1.00 37.63 S
ANISOU 2652 SD MET A 358 7013 3839 3446 1323 -192 -266 S
ATOM 2653 CE MET A 358 26.063 17.181 5.208 1.00 44.91 C
ANISOU 2653 CE MET A 358 8128 4703 4231 1448 -217 -176 C
ATOM 2654 N ASN A 359 21.801 12.202 3.155 1.00 27.30 N
ANISOU 2654 N ASN A 359 5812 2331 2230 853 585 -523 N
ATOM 2655 CA ASN A 359 20.637 11.551 3.739 1.00 28.79 C
ANISOU 2655 CA ASN A 359 6049 2483 2406 803 728 -564 C
ATOM 2656 C ASN A 359 21.042 10.719 4.951 1.00 32.92 C
ANISOU 2656 C ASN A 359 6772 2891 2846 864 792 -472 C
ATOM 2657 O ASN A 359 22.104 10.090 4.978 1.00 35.10 O
ANISOU 2657 O ASN A 359 7140 3112 3084 888 779 -406 O
ATOM 2658 CB ASN A 359 19.940 10.667 2.699 1.00 28.65 C
ANISOU 2658 CB ASN A 359 5950 2491 2444 651 844 -659 C
ATOM 2659 CG ASN A 359 18.553 10.229 3.135 1.00 34.13 C
ANISOU 2659 CG ASN A 359 6653 3180 3137 590 978 -721 C
ATOM 2660 OD1 ASN A 359 17.617 11.027 3.165 1.00 29.63 O
ANISOU 2660 OD1 ASN A 359 5984 2686 2587 592 961 -787 O
ATOM 2661 ND2 ASN A 359 18.413 8.951 3.464 1.00 30.72 N
ANISOU 2661 ND2 ASN A 359 6338 2655 2677 532 1116 -701 N
ATOM 2662 N LYS A 360 20.184 10.733 5.969 1.00 35.38 N
ANISOU 2662 N LYS A 360 7151 3169 3123 893 861 -469 N
ATOM 2663 CA LYS A 360 20.420 9.994 7.205 1.00 42.32 C
ANISOU 2663 CA LYS A 360 8227 3938 3916 955 931 -383 C
ATOM 2664 C LYS A 360 20.023 8.540 6.989 1.00 53.95 C
ANISOU 2664 C LYS A 360 9765 5337 5397 839 1103 -407 C
ATOM 2665 O LYS A 360 18.841 8.233 6.797 1.00 64.85 O
ANISOU 2665 O LYS A 360 11092 6731 6818 742 1216 -486 O
ATOM 2666 CB LYS A 360 19.633 10.601 8.361 1.00 46.62 C
ANISOU 2666 CB LYS A 360 8818 4473 4421 1032 940 -370 C
ATOM 2667 CG LYS A 360 20.433 11.538 9.232 1.00 55.62 C
ANISOU 2667 CG LYS A 360 10026 5619 5488 1191 793 -278 C
ATOM 2668 CD LYS A 360 20.010 12.976 9.039 1.00 63.33 C
ANISOU 2668 CD LYS A 360 10865 6694 6502 1231 677 -318 C
ATOM 2669 CE LYS A 360 20.588 13.836 10.143 1.00 62.82 C
ANISOU 2669 CE LYS A 360 10893 6628 6349 1390 550 -225 C
ATOM 2670 NZ LYS A 360 20.043 15.213 10.091 1.00 62.76 N
ANISOU 2670 NZ LYS A 360 10769 6707 6371 1432 450 -258 N
ATOM 2671 N GLY A 361 21.009 7.647 7.035 1.00 42.76 N
ANISOU 2671 N GLY A 361 8465 3847 3937 848 1123 -338 N
ATOM 2672 CA GLY A 361 20.772 6.244 6.771 1.00 44.53 C
ANISOU 2672 CA GLY A 361 8760 3994 4167 737 1280 -350 C
ATOM 2673 C GLY A 361 21.515 5.748 5.546 1.00 43.21 C
ANISOU 2673 C GLY A 361 8528 3849 4040 664 1259 -370 C
ATOM 2674 O GLY A 361 22.431 6.413 5.052 1.00 44.76 O
ANISOU 2674 O GLY A 361 8656 4105 4247 718 1120 -354 O
ATOM 2675 N SER A 362 21.140 4.568 5.059 1.00 37.99 N
ANISOU 2675 N SER A 362 7894 3139 3402 539 1400 -401 N
ATOM 2676 CA SER A 362 21.613 4.057 3.781 1.00 38.87 C
ANISOU 2676 CA SER A 362 7928 3279 3561 447 1398 -436 C
ATOM 2677 C SER A 362 20.410 3.593 2.977 1.00 44.03 C
ANISOU 2677 C SER A 362 8484 3964 4282 290 1514 -537 C
ATOM 2678 O SER A 362 19.630 2.757 3.444 1.00 53.81 O
ANISOU 2678 O SER A 362 9809 5128 5507 222 1664 -544 O
ATOM 2679 CB SER A 362 22.608 2.903 3.952 1.00 52.17 C
ANISOU 2679 CB SER A 362 9768 4864 5191 456 1450 -358 C
ATOM 2680 OG SER A 362 21.989 1.770 4.535 1.00 70.06 O
ANISOU 2680 OG SER A 362 12171 7022 7427 393 1622 -341 O
ATOM 2681 N ILE A 363 20.253 4.147 1.782 1.00 39.40 N
ANISOU 2681 N ILE A 363 7719 3489 3762 233 1445 -615 N
ATOM 2682 CA ILE A 363 19.200 3.741 0.868 1.00 42.66 C
ANISOU 2682 CA ILE A 363 8026 3952 4232 84 1536 -713 C
ATOM 2683 C ILE A 363 19.845 3.043 -0.320 1.00 43.77 C
ANISOU 2683 C ILE A 363 8131 4099 4402 0 1542 -723 C
ATOM 2684 O ILE A 363 21.023 3.239 -0.631 1.00 43.62 O
ANISOU 2684 O ILE A 363 8112 4085 4375 63 1442 -677 O
ATOM 2685 CB ILE A 363 18.341 4.936 0.408 1.00 43.39 C
ANISOU 2685 CB ILE A 363 7939 4179 4369 84 1457 -802 C
ATOM 2686 CG1 ILE A 363 19.241 6.072 -0.081 1.00 45.47 C
ANISOU 2686 CG1 ILE A 363 8104 4523 4649 176 1278 -791 C
ATOM 2687 CG2 ILE A 363 17.427 5.405 1.531 1.00 38.59 C
ANISOU 2687 CG2 ILE A 363 7365 3563 3735 136 1491 -809 C
ATOM 2688 CD1 ILE A 363 18.503 7.347 -0.421 1.00 43.02 C
ANISOU 2688 CD1 ILE A 363 7631 4340 4373 198 1188 -867 C
ATOM 2689 N SER A 364 19.065 2.195 -0.974 1.00 40.78 N
ANISOU 2689 N SER A 364 7723 3716 4056 -148 1665 -782 N
ATOM 2690 CA SER A 364 19.470 1.588 -2.230 1.00 46.50 C
ANISOU 2690 CA SER A 364 8389 4463 4815 -245 1676 -807 C
ATOM 2691 C SER A 364 18.817 2.340 -3.380 1.00 44.89 C
ANISOU 2691 C SER A 364 7987 4400 4668 -305 1612 -902 C
ATOM 2692 O SER A 364 17.665 2.770 -3.283 1.00 42.03 O
ANISOU 2692 O SER A 364 7552 4097 4322 -338 1638 -966 O
ATOM 2693 CB SER A 364 19.082 0.109 -2.281 1.00 54.58 C
ANISOU 2693 CB SER A 364 9513 5389 5837 -380 1856 -807 C
ATOM 2694 OG SER A 364 17.676 -0.049 -2.208 1.00 62.07 O
ANISOU 2694 OG SER A 364 10419 6354 6811 -482 1963 -879 O
ATOM 2695 N PHE A 365 19.567 2.509 -4.466 1.00 41.82 N
ANISOU 2695 N PHE A 365 7515 4069 4306 -314 1528 -909 N
ATOM 2696 CA PHE A 365 19.023 3.187 -5.634 1.00 33.06 C
ANISOU 2696 CA PHE A 365 6227 3092 3244 -367 1465 -991 C
ATOM 2697 C PHE A 365 17.861 2.399 -6.224 1.00 35.26 C
ANISOU 2697 C PHE A 365 6461 3385 3549 -534 1599 -1062 C
ATOM 2698 O PHE A 365 17.902 1.169 -6.317 1.00 40.19 O
ANISOU 2698 O PHE A 365 7169 3926 4174 -634 1724 -1048 O
ATOM 2699 CB PHE A 365 20.112 3.394 -6.691 1.00 36.97 C
ANISOU 2699 CB PHE A 365 6657 3631 3759 -350 1362 -978 C
ATOM 2700 CG PHE A 365 19.617 4.029 -7.963 1.00 39.10 C
ANISOU 2700 CG PHE A 365 6754 4030 4071 -405 1301 -1053 C
ATOM 2701 CD1 PHE A 365 19.456 5.401 -8.056 1.00 45.26 C
ANISOU 2701 CD1 PHE A 365 7428 4909 4860 -316 1170 -1081 C
ATOM 2702 CD2 PHE A 365 19.321 3.248 -9.070 1.00 32.99 C
ANISOU 2702 CD2 PHE A 365 5930 3279 3325 -546 1375 -1094 C
ATOM 2703 CE1 PHE A 365 19.002 5.984 -9.226 1.00 41.34 C
ANISOU 2703 CE1 PHE A 365 6785 4528 4394 -359 1114 -1143 C
ATOM 2704 CE2 PHE A 365 18.867 3.824 -10.238 1.00 33.43 C
ANISOU 2704 CE2 PHE A 365 5835 3453 3414 -595 1320 -1156 C
ATOM 2705 CZ PHE A 365 18.708 5.193 -10.316 1.00 37.40 C
ANISOU 2705 CZ PHE A 365 6241 4050 3919 -498 1189 -1177 C
ATOM 2706 N LYS A 366 16.811 3.121 -6.604 1.00 40.39 N
ANISOU 2706 N LYS A 366 6981 4143 4222 -564 1574 -1138 N
ATOM 2707 CA LYS A 366 15.695 2.565 -7.351 1.00 42.39 C
ANISOU 2707 CA LYS A 366 7156 4441 4509 -726 1678 -1217 C
ATOM 2708 C LYS A 366 15.570 3.335 -8.654 1.00 39.87 C
ANISOU 2708 C LYS A 366 6669 4260 4220 -746 1575 -1271 C
ATOM 2709 O LYS A 366 15.777 4.552 -8.682 1.00 42.03 O
ANISOU 2709 O LYS A 366 6874 4609 4487 -629 1437 -1270 O
ATOM 2710 CB LYS A 366 14.380 2.649 -6.569 1.00 53.19 C
ANISOU 2710 CB LYS A 366 8525 5815 5871 -755 1761 -1264 C
ATOM 2711 CG LYS A 366 14.355 1.851 -5.281 1.00 58.08 C
ANISOU 2711 CG LYS A 366 9315 6294 6460 -747 1881 -1214 C
ATOM 2712 CD LYS A 366 12.961 1.842 -4.683 1.00 62.08 C
ANISOU 2712 CD LYS A 366 9807 6813 6968 -802 1979 -1273 C
ATOM 2713 CE LYS A 366 12.952 1.217 -3.303 1.00 67.94 C
ANISOU 2713 CE LYS A 366 10725 7416 7674 -770 2087 -1216 C
ATOM 2714 NZ LYS A 366 13.385 -0.204 -3.328 1.00 70.29 N
ANISOU 2714 NZ LYS A 366 11152 7582 7973 -868 2217 -1176 N
ATOM 2715 N LYS A 367 15.230 2.621 -9.726 1.00 40.21 N
ANISOU 2715 N LYS A 367 6649 4333 4298 -896 1645 -1317 N
ATOM 2716 CA LYS A 367 15.115 3.242 -11.039 1.00 41.23 C
ANISOU 2716 CA LYS A 367 6623 4589 4454 -928 1559 -1363 C
ATOM 2717 C LYS A 367 14.063 4.342 -11.020 1.00 42.13 C
ANISOU 2717 C LYS A 367 6625 4816 4567 -895 1501 -1422 C
ATOM 2718 O LYS A 367 13.016 4.211 -10.384 1.00 49.12 O
ANISOU 2718 O LYS A 367 7515 5699 5449 -935 1582 -1462 O
ATOM 2719 CB LYS A 367 14.756 2.190 -12.092 1.00 41.64 C
ANISOU 2719 CB LYS A 367 6627 4653 4542 -1111 1666 -1410 C
ATOM 2720 CG LYS A 367 15.657 0.964 -12.085 1.00 49.32 C
ANISOU 2720 CG LYS A 367 7719 5508 5512 -1158 1747 -1357 C
ATOM 2721 CD LYS A 367 15.339 0.028 -13.244 1.00 55.90 C
ANISOU 2721 CD LYS A 367 8490 6369 6383 -1335 1837 -1408 C
ATOM 2722 CE LYS A 367 16.154 -1.256 -13.171 1.00 57.85 C
ANISOU 2722 CE LYS A 367 8867 6492 6622 -1383 1930 -1358 C
ATOM 2723 NZ LYS A 367 17.619 -1.006 -13.252 1.00 61.45 N
ANISOU 2723 NZ LYS A 367 9376 6918 7055 -1258 1826 -1280 N
ATOM 2724 N VAL A 368 14.352 5.437 -11.717 1.00 36.13 N
ANISOU 2724 N VAL A 368 5766 4152 3809 -818 1360 -1425 N
ATOM 2725 CA VAL A 368 13.422 6.548 -11.846 1.00 33.71 C
ANISOU 2725 CA VAL A 368 5350 3960 3498 -779 1292 -1477 C
ATOM 2726 C VAL A 368 13.125 6.756 -13.328 1.00 38.93 C
ANISOU 2726 C VAL A 368 5869 4734 4190 -870 1259 -1524 C
ATOM 2727 O VAL A 368 13.764 6.168 -14.201 1.00 39.74 O
ANISOU 2727 O VAL A 368 5960 4826 4313 -938 1272 -1512 O
ATOM 2728 CB VAL A 368 13.956 7.841 -11.196 1.00 34.76 C
ANISOU 2728 CB VAL A 368 5503 4105 3601 -586 1146 -1435 C
ATOM 2729 CG1 VAL A 368 14.151 7.636 -9.704 1.00 33.45 C
ANISOU 2729 CG1 VAL A 368 5465 3840 3406 -505 1184 -1394 C
ATOM 2730 CG2 VAL A 368 15.258 8.275 -11.847 1.00 31.65 C
ANISOU 2730 CG2 VAL A 368 5101 3713 3213 -512 1027 -1386 C
ATOM 2731 N ALA A 369 12.124 7.593 -13.603 1.00 36.89 N
ANISOU 2731 N ALA A 369 5500 4587 3931 -869 1220 -1580 N
ATOM 2732 CA ALA A 369 11.712 7.926 -14.970 1.00 37.11 C
ANISOU 2732 CA ALA A 369 5380 4737 3985 -948 1183 -1628 C
ATOM 2733 C ALA A 369 11.585 9.447 -15.046 1.00 38.38 C
ANISOU 2733 C ALA A 369 5480 4979 4124 -817 1041 -1622 C
ATOM 2734 O ALA A 369 10.499 10.003 -14.863 1.00 44.77 O
ANISOU 2734 O ALA A 369 6220 5865 4926 -819 1041 -1672 O
ATOM 2735 CB ALA A 369 10.411 7.217 -15.346 1.00 39.04 C
ANISOU 2735 CB ALA A 369 5533 5043 4257 -1122 1304 -1718 C
ATOM 2736 N LEU A 370 12.705 10.120 -15.308 1.00 40.14 N
ANISOU 2736 N LEU A 370 5731 5183 4338 -704 922 -1560 N
ATOM 2737 CA LEU A 370 12.776 11.581 -15.321 1.00 34.05 C
ANISOU 2737 CA LEU A 370 4930 4462 3544 -568 783 -1540 C
ATOM 2738 C LEU A 370 13.287 12.024 -16.685 1.00 33.49 C
ANISOU 2738 C LEU A 370 4776 4455 3494 -587 705 -1529 C
ATOM 2739 O LEU A 370 14.486 12.282 -16.862 1.00 30.38 O
ANISOU 2739 O LEU A 370 4435 4010 3099 -508 628 -1470 O
ATOM 2740 CB LEU A 370 13.670 12.098 -14.194 1.00 36.98 C
ANISOU 2740 CB LEU A 370 5425 4742 3884 -397 706 -1475 C
ATOM 2741 CG LEU A 370 13.285 11.617 -12.791 1.00 39.40 C
ANISOU 2741 CG LEU A 370 5820 4982 4169 -370 785 -1479 C
ATOM 2742 CD1 LEU A 370 14.324 12.023 -11.761 1.00 37.47 C
ANISOU 2742 CD1 LEU A 370 5675 4658 3901 -211 705 -1421 C
ATOM 2743 CD2 LEU A 370 11.918 12.147 -12.404 1.00 35.28 C
ANISOU 2743 CD2 LEU A 370 5247 4529 3629 -372 808 -1532 C
ATOM 2744 N PRO A 371 12.396 12.147 -17.674 1.00 32.77 N
ANISOU 2744 N PRO A 371 4546 4481 3422 -687 722 -1589 N
ATOM 2745 CA PRO A 371 12.858 12.392 -19.050 1.00 27.10 C
ANISOU 2745 CA PRO A 371 3742 3828 2725 -721 667 -1582 C
ATOM 2746 C PRO A 371 13.526 13.742 -19.256 1.00 29.00 C
ANISOU 2746 C PRO A 371 3992 4074 2952 -586 524 -1527 C
ATOM 2747 O PRO A 371 14.244 13.905 -20.250 1.00 29.29 O
ANISOU 2747 O PRO A 371 3995 4130 3004 -591 476 -1501 O
ATOM 2748 CB PRO A 371 11.572 12.276 -19.879 1.00 27.76 C
ANISOU 2748 CB PRO A 371 3670 4049 2828 -846 718 -1667 C
ATOM 2749 CG PRO A 371 10.476 12.598 -18.919 1.00 31.71 C
ANISOU 2749 CG PRO A 371 4166 4571 3312 -825 743 -1708 C
ATOM 2750 CD PRO A 371 10.927 12.069 -17.586 1.00 28.39 C
ANISOU 2750 CD PRO A 371 3900 4014 2872 -771 790 -1668 C
ATOM 2751 N SER A 372 13.314 14.710 -18.371 1.00 34.88 N
ANISOU 2751 N SER A 372 4785 4800 3670 -469 459 -1508 N
ATOM 2752 CA SER A 372 13.953 16.013 -18.494 1.00 29.09 C
ANISOU 2752 CA SER A 372 4074 4055 2924 -349 329 -1451 C
ATOM 2753 C SER A 372 15.211 16.138 -17.646 1.00 31.80 C
ANISOU 2753 C SER A 372 4570 4264 3247 -228 275 -1377 C
ATOM 2754 O SER A 372 15.828 17.208 -17.634 1.00 33.77 O
ANISOU 2754 O SER A 372 4863 4482 3486 -137 176 -1324 O
ATOM 2755 CB SER A 372 12.966 17.121 -18.116 1.00 26.99 C
ANISOU 2755 CB SER A 372 3763 3851 2640 -298 285 -1472 C
ATOM 2756 OG SER A 372 11.794 17.046 -18.909 1.00 35.18 O
ANISOU 2756 OG SER A 372 4644 5026 3695 -399 324 -1547 O
ATOM 2757 N LEU A 373 15.618 15.071 -16.963 1.00 30.09 N
ANISOU 2757 N LEU A 373 4433 3973 3029 -234 342 -1374 N
ATOM 2758 CA LEU A 373 16.709 15.141 -15.998 1.00 21.74 C
ANISOU 2758 CA LEU A 373 3500 2808 1953 -104 288 -1320 C
ATOM 2759 C LEU A 373 18.042 15.400 -16.696 1.00 22.65 C
ANISOU 2759 C LEU A 373 3632 2890 2083 -64 206 -1269 C
ATOM 2760 O LEU A 373 18.450 14.636 -17.579 1.00 21.13 O
ANISOU 2760 O LEU A 373 3397 2713 1920 -155 250 -1275 O
ATOM 2761 CB LEU A 373 16.774 13.845 -15.198 1.00 23.51 C
ANISOU 2761 CB LEU A 373 3773 2979 2182 -144 393 -1337 C
ATOM 2762 CG LEU A 373 17.765 13.838 -14.034 1.00 26.42 C
ANISOU 2762 CG LEU A 373 4225 3270 2544 -18 347 -1304 C
ATOM 2763 CD1 LEU A 373 17.289 14.763 -12.930 1.00 22.13 C
ANISOU 2763 CD1 LEU A 373 3698 2737 1972 107 287 -1315 C
ATOM 2764 CD2 LEU A 373 17.997 12.428 -13.503 1.00 29.92 C
ANISOU 2764 CD2 LEU A 373 4724 3645 2998 -100 472 -1301 C
ATOM 2765 N SER A 374 18.730 16.468 -16.279 1.00 25.70 N
ANISOU 2765 N SER A 374 4097 3219 2447 65 96 -1215 N
ATOM 2766 CA SER A 374 20.056 16.794 -16.780 1.00 21.37 C
ANISOU 2766 CA SER A 374 3560 2630 1931 96 26 -1137 C
ATOM 2767 C SER A 374 21.099 16.947 -15.683 1.00 20.93 C
ANISOU 2767 C SER A 374 3441 2572 1940 237 -57 -1112 C
ATOM 2768 O SER A 374 22.294 17.012 -15.997 1.00 22.64 O
ANISOU 2768 O SER A 374 3383 2925 2296 82 23 -1205 O
ATOM 2769 CB SER A 374 20.014 18.089 -17.607 1.00 18.81 C
ANISOU 2769 CB SER A 374 3230 2316 1600 27 0 -1092 C
ATOM 2770 OG SER A 374 19.979 19.223 -16.761 1.00 26.96 O
ANISOU 2770 OG SER A 374 4268 3335 2639 -16 32 -1057 O
ATOM 2771 N TYR A 375 20.687 17.023 -14.417 1.00 21.19 N
ANISOU 2771 N TYR A 375 3268 2730 2055 175 27 -1236 N
ATOM 2772 CA TYR A 375 21.600 17.183 -13.292 1.00 19.10 C
ANISOU 2772 CA TYR A 375 3108 2354 1793 65 150 -1201 C
ATOM 2773 C TYR A 375 21.178 16.238 -12.174 1.00 25.02 C
ANISOU 2773 C TYR A 375 3928 3066 2512 138 173 -1237 C
ATOM 2774 O TYR A 375 20.017 16.252 -11.749 1.00 27.14 O
ANISOU 2774 O TYR A 375 4179 3376 2758 166 179 -1275 O
ATOM 2775 CB TYR A 375 21.607 18.638 -12.798 1.00 18.59 C
ANISOU 2775 CB TYR A 375 3137 2234 1694 102 109 -1134 C
ATOM 2776 CG TYR A 375 22.508 18.899 -11.610 1.00 24.38 C
ANISOU 2776 CG TYR A 375 3966 2871 2429 251 24 -1027 C
ATOM 2777 CD1 TYR A 375 22.055 18.689 -10.315 1.00 29.49 C
ANISOU 2777 CD1 TYR A 375 4675 3478 3053 304 49 -1023 C
ATOM 2778 CD2 TYR A 375 23.801 19.378 -11.781 1.00 21.93 C
ANISOU 2778 CD2 TYR A 375 3685 2511 2134 337 -82 -928 C
ATOM 2779 CE1 TYR A 375 22.864 18.929 -9.223 1.00 18.81 C
ANISOU 2779 CE1 TYR A 375 3425 2038 1684 431 -27 -918 C
ATOM 2780 CE2 TYR A 375 24.621 19.623 -10.692 1.00 19.84 C
ANISOU 2780 CE2 TYR A 375 3509 2170 1859 466 -164 -833 C
ATOM 2781 CZ TYR A 375 24.148 19.398 -9.416 1.00 22.70 C
ANISOU 2781 CZ TYR A 375 3944 2493 2188 511 -136 -825 C
ATOM 2782 OH TYR A 375 24.968 19.645 -8.335 1.00 31.45 O
ANISOU 2782 OH TYR A 375 5148 3533 3270 637 -220 -727 O
ATOM 2783 N LEU A 376 22.117 15.426 -11.690 1.00 19.99 N
ANISOU 2783 N LEU A 376 3407 2327 1862 160 197 -1189 N
ATOM 2784 CA LEU A 376 21.815 14.425 -10.672 1.00 20.82 C
ANISOU 2784 CA LEU A 376 3627 2355 1929 177 267 -1169 C
ATOM 2785 C LEU A 376 22.949 14.383 -9.659 1.00 26.93 C
ANISOU 2785 C LEU A 376 4530 3009 2693 233 260 -1059 C
ATOM 2786 O LEU A 376 24.081 14.031 -10.004 1.00 27.87 O
ANISOU 2786 O LEU A 376 4688 3084 2819 237 239 -1006 O
ATOM 2787 CB LEU A 376 21.607 13.046 -11.303 1.00 21.42 C
ANISOU 2787 CB LEU A 376 3747 2409 1981 118 335 -1180 C
ATOM 2788 CG LEU A 376 21.203 11.899 -10.374 1.00 26.34 C
ANISOU 2788 CG LEU A 376 4495 2944 2569 84 454 -1157 C
ATOM 2789 CD1 LEU A 376 19.968 12.278 -9.564 1.00 22.94 C
ANISOU 2789 CD1 LEU A 376 4058 2542 2116 106 481 -1196 C
ATOM 2790 CD2 LEU A 376 20.967 10.623 -11.175 1.00 22.96 C
ANISOU 2790 CD2 LEU A 376 4098 2494 2132 -28 553 -1164 C
ATOM 2791 N ASP A 377 22.641 14.739 -8.413 1.00 27.09 N
ANISOU 2791 N ASP A 377 4623 2982 2686 294 263 -1020 N
ATOM 2792 CA ASP A 377 23.591 14.710 -7.306 1.00 28.93 C
ANISOU 2792 CA ASP A 377 4997 3110 2887 387 231 -908 C
ATOM 2793 C ASP A 377 23.033 13.762 -6.255 1.00 30.45 C
ANISOU 2793 C ASP A 377 5295 3239 3037 387 328 -906 C
ATOM 2794 O ASP A 377 22.080 14.105 -5.547 1.00 27.42 O
ANISOU 2794 O ASP A 377 4913 2868 2637 406 351 -931 O
ATOM 2795 CB ASP A 377 23.813 16.109 -6.729 1.00 26.59 C
ANISOU 2795 CB ASP A 377 4709 2811 2583 491 119 -839 C
ATOM 2796 CG ASP A 377 24.781 16.121 -5.545 1.00 32.05 C
ANISOU 2796 CG ASP A 377 5539 3413 3224 610 58 -724 C
ATOM 2797 OD1 ASP A 377 25.250 15.048 -5.113 1.00 28.60 O
ANISOU 2797 OD1 ASP A 377 5201 2911 2757 606 117 -697 O
ATOM 2798 OD2 ASP A 377 25.086 17.221 -5.040 1.00 33.24 O
ANISOU 2798 OD2 ASP A 377 5704 3566 3361 714 -56 -659 O
ATOM 2799 N LEU A 378 23.624 12.573 -6.155 1.00 33.55 N
ANISOU 2799 N LEU A 378 5782 3559 3407 365 388 -872 N
ATOM 2800 CA LEU A 378 23.232 11.575 -5.167 1.00 23.48 C
ANISOU 2800 CA LEU A 378 4632 2204 2086 361 492 -851 C
ATOM 2801 C LEU A 378 24.354 11.298 -4.171 1.00 26.28 C
ANISOU 2801 C LEU A 378 5139 2458 2390 453 467 -740 C
ATOM 2802 O LEU A 378 24.456 10.195 -3.627 1.00 29.14 O
ANISOU 2802 O LEU A 378 5620 2739 2712 438 556 -708 O
ATOM 2803 CB LEU A 378 22.798 10.284 -5.858 1.00 24.10 C
ANISOU 2803 CB LEU A 378 4711 2276 2168 247 606 -901 C
ATOM 2804 CG LEU A 378 21.567 10.409 -6.757 1.00 26.41 C
ANISOU 2804 CG LEU A 378 4875 2670 2490 164 635 -1004 C
ATOM 2805 CD1 LEU A 378 21.266 9.091 -7.452 1.00 25.53 C
ANISOU 2805 CD1 LEU A 378 4787 2536 2376 48 747 -1028 C
ATOM 2806 CD2 LEU A 378 20.367 10.891 -5.950 1.00 24.66 C
ANISOU 2806 CD2 LEU A 378 4642 2476 2252 186 660 -1042 C
ATOM 2807 N SER A 379 25.181 12.301 -3.899 1.00 22.95 N
ANISOU 2807 N SER A 379 4719 2041 1960 552 341 -676 N
ATOM 2808 CA SER A 379 26.382 12.086 -3.110 1.00 26.74 C
ANISOU 2808 CA SER A 379 5328 2449 2383 647 291 -574 C
ATOM 2809 C SER A 379 26.070 12.033 -1.616 1.00 31.58 C
ANISOU 2809 C SER A 379 6071 3001 2928 728 313 -520 C
ATOM 2810 O SER A 379 25.051 12.552 -1.149 1.00 31.70 O
ANISOU 2810 O SER A 379 6062 3037 2945 735 330 -550 O
ATOM 2811 CB SER A 379 27.398 13.196 -3.384 1.00 23.59 C
ANISOU 2811 CB SER A 379 4882 2089 1993 728 136 -525 C
ATOM 2812 OG SER A 379 26.915 14.461 -2.963 1.00 32.57 O
ANISOU 2812 OG SER A 379 5978 3266 3131 794 53 -516 O
ATOM 2813 N ARG A 380 26.959 11.363 -0.875 1.00 32.53 N
ANISOU 2813 N ARG A 380 6332 3048 2981 789 314 -443 N
ATOM 2814 CA AARG A 380 26.940 11.354 0.588 0.50 29.83 C
ANISOU 2814 CA AARG A 380 6130 2649 2557 888 313 -374 C
ATOM 2815 CA BARG A 380 26.936 11.365 0.589 0.50 29.82 C
ANISOU 2815 CA BARG A 380 6128 2648 2555 888 313 -375 C
ATOM 2816 C ARG A 380 25.659 10.733 1.141 1.00 30.47 C
ANISOU 2816 C ARG A 380 6258 2688 2631 833 456 -412 C
ATOM 2817 O ARG A 380 25.057 11.245 2.082 1.00 29.07 O
ANISOU 2817 O ARG A 380 6120 2504 2421 892 450 -396 O
ATOM 2818 CB AARG A 380 27.147 12.765 1.141 0.50 27.87 C
ANISOU 2818 CB AARG A 380 5858 2446 2284 1002 166 -333 C
ATOM 2819 CB BARG A 380 27.115 12.782 1.137 0.50 27.83 C
ANISOU 2819 CB BARG A 380 5851 2442 2280 1001 167 -335 C
ATOM 2820 CG AARG A 380 28.412 13.422 0.626 0.50 28.33 C
ANISOU 2820 CG AARG A 380 5870 2549 2345 1057 19 -296 C
ATOM 2821 CG BARG A 380 28.406 13.448 0.706 0.50 28.19 C
ANISOU 2821 CG BARG A 380 5859 2531 2323 1064 17 -293 C
ATOM 2822 CD AARG A 380 28.413 14.917 0.861 0.50 27.79 C
ANISOU 2822 CD AARG A 380 5742 2544 2274 1142 -125 -275 C
ATOM 2823 CD BARG A 380 28.316 14.957 0.834 0.50 27.94 C
ANISOU 2823 CD BARG A 380 5753 2565 2297 1138 -121 -280 C
ATOM 2824 NE AARG A 380 29.560 15.550 0.217 0.50 25.04 N
ANISOU 2824 NE AARG A 380 5332 2243 1938 1179 -260 -250 N
ATOM 2825 NE BARG A 380 29.562 15.609 0.440 0.50 26.31 N
ANISOU 2825 NE BARG A 380 5511 2403 2085 1197 -269 -241 N
ATOM 2826 CZ AARG A 380 30.749 15.698 0.793 0.50 26.06 C
ANISOU 2826 CZ AARG A 380 5535 2375 1993 1275 -369 -186 C
ATOM 2827 CZ BARG A 380 29.881 15.921 -0.812 0.50 21.36 C
ANISOU 2827 CZ BARG A 380 4763 1820 1531 1141 -304 -274 C
ATOM 2828 NH1AARG A 380 30.952 15.262 2.030 0.50 28.16 N
ANISOU 2828 NH1AARG A 380 5942 2596 2160 1349 -360 -138 N
ATOM 2829 NH1BARG A 380 29.045 15.639 -1.800 0.50 21.20 N
ANISOU 2829 NH1BARG A 380 4649 1814 1591 1025 -205 -349 N
ATOM 2830 NH2AARG A 380 31.740 16.284 0.136 0.50 21.41 N
ANISOU 2830 NH2AARG A 380 4871 1836 1426 1294 -486 -178 N
ATOM 2831 NH2BARG A 380 31.039 16.513 -1.075 0.50 20.77 N
ANISOU 2831 NH2BARG A 380 4664 1783 1447 1199 -439 -236 N
ATOM 2832 N ASN A 381 25.246 9.607 0.564 1.00 26.43 N
ANISOU 2832 N ASN A 381 5746 2149 2146 718 585 -461 N
ATOM 2833 CA ASN A 381 24.047 8.917 1.025 1.00 27.42 C
ANISOU 2833 CA ASN A 381 5919 2235 2266 654 729 -498 C
ATOM 2834 C ASN A 381 24.338 7.511 1.533 1.00 33.58 C
ANISOU 2834 C ASN A 381 6860 2908 2991 634 846 -448 C
ATOM 2835 O ASN A 381 23.401 6.790 1.895 1.00 35.63 O
ANISOU 2835 O ASN A 381 7174 3120 3244 570 980 -472 O
ATOM 2836 CB ASN A 381 23.000 8.861 -0.093 1.00 27.26 C
ANISOU 2836 CB ASN A 381 5749 2288 2321 524 789 -611 C
ATOM 2837 CG ASN A 381 22.487 10.235 -0.478 1.00 28.11 C
ANISOU 2837 CG ASN A 381 5706 2500 2474 544 691 -666 C
ATOM 2838 OD1 ASN A 381 22.187 11.063 0.383 1.00 29.63 O
ANISOU 2838 OD1 ASN A 381 5918 2698 2644 627 644 -643 O
ATOM 2839 ND2 ASN A 381 22.395 10.489 -1.780 1.00 25.75 N
ANISOU 2839 ND2 ASN A 381 5262 2285 2236 472 661 -737 N
ATOM 2840 N ALA A 382 25.610 7.107 1.588 1.00 31.71 N
ANISOU 2840 N ALA A 382 6705 2632 2712 687 800 -379 N
ATOM 2841 CA ALA A 382 25.980 5.698 1.756 1.00 38.30 C
ANISOU 2841 CA ALA A 382 7675 3373 3503 651 910 -342 C
ATOM 2842 C ALA A 382 25.176 4.815 0.803 1.00 38.37 C
ANISOU 2842 C ALA A 382 7625 3381 3573 494 1041 -419 C
ATOM 2843 O ALA A 382 24.832 3.672 1.121 1.00 39.97 O
ANISOU 2843 O ALA A 382 7940 3500 3748 436 1179 -405 O
ATOM 2844 CB ALA A 382 25.804 5.239 3.204 1.00 40.11 C
ANISOU 2844 CB ALA A 382 8086 3509 3645 722 978 -271 C
ATOM 2845 N LEU A 383 24.885 5.360 -0.378 1.00 30.89 N
ANISOU 2845 N LEU A 383 6505 2529 2702 425 996 -497 N
ATOM 2846 CA LEU A 383 23.999 4.748 -1.357 1.00 28.94 C
ANISOU 2846 CA LEU A 383 6176 2309 2510 278 1098 -581 C
ATOM 2847 C LEU A 383 24.624 3.482 -1.933 1.00 33.68 C
ANISOU 2847 C LEU A 383 6841 2853 3105 207 1174 -562 C
ATOM 2848 O LEU A 383 25.839 3.393 -2.128 1.00 28.89 O
ANISOU 2848 O LEU A 383 6263 2235 2479 262 1104 -514 O
ATOM 2849 CB LEU A 383 23.716 5.765 -2.470 1.00 39.21 C
ANISOU 2849 CB LEU A 383 7281 3736 3881 248 1003 -659 C
ATOM 2850 CG LEU A 383 22.607 5.720 -3.534 1.00 43.07 C
ANISOU 2850 CG LEU A 383 7633 4306 4428 122 1055 -763 C
ATOM 2851 CD1 LEU A 383 23.022 4.927 -4.776 1.00 50.18 C
ANISOU 2851 CD1 LEU A 383 8493 5217 5357 24 1087 -785 C
ATOM 2852 CD2 LEU A 383 21.297 5.203 -2.972 1.00 47.12 C
ANISOU 2852 CD2 LEU A 383 8187 4789 4930 55 1188 -798 C
ATOM 2853 N SER A 384 23.778 2.489 -2.198 1.00 37.48 N
ANISOU 2853 N SER A 384 7344 3297 3599 83 1319 -601 N
ATOM 2854 CA SER A 384 24.193 1.268 -2.877 1.00 40.69 C
ANISOU 2854 CA SER A 384 7798 3655 4008 -6 1404 -595 C
ATOM 2855 C SER A 384 23.463 1.206 -4.208 1.00 43.91 C
ANISOU 2855 C SER A 384 8056 4145 4484 -142 1434 -688 C
ATOM 2856 O SER A 384 22.227 1.191 -4.244 1.00 41.62 O
ANISOU 2856 O SER A 384 7718 3878 4218 -224 1510 -748 O
ATOM 2857 CB SER A 384 23.901 0.021 -2.038 1.00 50.87 C
ANISOU 2857 CB SER A 384 9265 4817 5247 -44 1562 -551 C
ATOM 2858 OG SER A 384 22.510 -0.213 -1.927 1.00 55.56 O
ANISOU 2858 OG SER A 384 9838 5405 5866 -145 1678 -609 O
ATOM 2859 N PHE A 385 24.229 1.178 -5.294 1.00 42.88 N
ANISOU 2859 N PHE A 385 7851 4060 4380 -164 1374 -699 N
ATOM 2860 CA PHE A 385 23.710 1.245 -6.655 1.00 31.64 C
ANISOU 2860 CA PHE A 385 6278 2728 3016 -276 1377 -779 C
ATOM 2861 C PHE A 385 24.068 -0.059 -7.359 1.00 40.56 C
ANISOU 2861 C PHE A 385 7458 3805 4148 -380 1475 -773 C
ATOM 2862 O PHE A 385 25.244 -0.319 -7.634 1.00 39.63 O
ANISOU 2862 O PHE A 385 7375 3667 4016 -335 1428 -730 O
ATOM 2863 CB PHE A 385 24.297 2.456 -7.382 1.00 27.82 C
ANISOU 2863 CB PHE A 385 5657 2349 2564 -207 1214 -798 C
ATOM 2864 CG PHE A 385 23.552 2.860 -8.628 1.00 34.57 C
ANISOU 2864 CG PHE A 385 6349 3314 3472 -298 1197 -881 C
ATOM 2865 CD1 PHE A 385 23.003 1.913 -9.477 1.00 33.04 C
ANISOU 2865 CD1 PHE A 385 6134 3123 3299 -443 1306 -923 C
ATOM 2866 CD2 PHE A 385 23.419 4.200 -8.958 1.00 39.75 C
ANISOU 2866 CD2 PHE A 385 6878 4073 4153 -237 1071 -916 C
ATOM 2867 CE1 PHE A 385 22.336 2.289 -10.616 1.00 29.15 C
ANISOU 2867 CE1 PHE A 385 5496 2734 2846 -523 1287 -994 C
ATOM 2868 CE2 PHE A 385 22.749 4.583 -10.099 1.00 37.05 C
ANISOU 2868 CE2 PHE A 385 6395 3832 3848 -310 1051 -986 C
ATOM 2869 CZ PHE A 385 22.206 3.625 -10.929 1.00 31.37 C
ANISOU 2869 CZ PHE A 385 5658 3117 3146 -452 1158 -1023 C
ATOM 2870 N SER A 386 23.059 -0.865 -7.668 1.00 38.09 N
ANISOU 2870 N SER A 386 7143 3475 3853 -520 1610 -820 N
ATOM 2871 CA SER A 386 23.254 -2.124 -8.377 1.00 41.13 C
ANISOU 2871 CA SER A 386 7569 3814 4245 -636 1715 -822 C
ATOM 2872 C SER A 386 22.841 -1.942 -9.833 1.00 37.74 C
ANISOU 2872 C SER A 386 6976 3492 3872 -744 1696 -899 C
ATOM 2873 O SER A 386 21.656 -1.763 -10.132 1.00 48.13 O
ANISOU 2873 O SER A 386 8205 4865 5219 -834 1741 -966 O
ATOM 2874 CB SER A 386 22.455 -3.246 -7.724 1.00 41.81 C
ANISOU 2874 CB SER A 386 7776 3796 4314 -731 1891 -820 C
ATOM 2875 OG SER A 386 22.672 -4.464 -8.412 1.00 56.34 O
ANISOU 2875 OG SER A 386 9657 5588 6160 -844 1993 -822 O
ATOM 2876 N GLY A 387 23.811 -1.993 -10.735 1.00 36.10 N
ANISOU 2876 N GLY A 387 6728 3315 3674 -733 1632 -888 N
ATOM 2877 CA GLY A 387 23.543 -1.891 -12.149 1.00 40.25 C
ANISOU 2877 CA GLY A 387 7111 3937 4245 -831 1616 -950 C
ATOM 2878 C GLY A 387 23.894 -0.569 -12.793 1.00 38.86 C
ANISOU 2878 C GLY A 387 6799 3874 4092 -751 1456 -968 C
ATOM 2879 O GLY A 387 23.253 -0.194 -13.780 1.00 42.77 O
ANISOU 2879 O GLY A 387 7163 4466 4624 -826 1440 -1029 O
ATOM 2880 N CYS A 388 24.883 0.149 -12.267 1.00 33.69 N
ANISOU 2880 N CYS A 388 6172 3210 3418 -605 1340 -917 N
ATOM 2881 CA CYS A 388 25.318 1.402 -12.869 1.00 34.41 C
ANISOU 2881 CA CYS A 388 6142 3398 3533 -528 1190 -931 C
ATOM 2882 C CYS A 388 26.093 1.133 -14.155 1.00 35.77 C
ANISOU 2882 C CYS A 388 6256 3608 3728 -570 1162 -938 C
ATOM 2883 O CYS A 388 26.913 0.212 -14.214 1.00 31.83 O
ANISOU 2883 O CYS A 388 5840 3041 3211 -581 1207 -901 O
ATOM 2884 CB CYS A 388 26.195 2.172 -11.877 1.00 31.01 C
ANISOU 2884 CB CYS A 388 5764 2940 3078 -370 1083 -875 C
ATOM 2885 SG CYS A 388 26.861 3.731 -12.488 1.00 39.22 S
ANISOU 2885 SG CYS A 388 6668 4084 4151 -270 901 -887 S
ATOM 2886 N CYS A 389 25.818 1.909 -15.208 1.00 37.14 N
ANISOU 2886 N CYS A 389 6290 3887 3934 -594 1093 -983 N
ATOM 2887 CA CYS A 389 24.722 2.875 -15.314 1.00 31.09 C
ANISOU 2887 CA CYS A 389 5421 3207 3185 -599 1055 -1034 C
ATOM 2888 C CYS A 389 24.258 2.887 -16.767 1.00 29.96 C
ANISOU 2888 C CYS A 389 5156 3155 3072 -706 1063 -1086 C
ATOM 2889 O CYS A 389 25.080 2.695 -17.658 1.00 30.95 O
ANISOU 2889 O CYS A 389 5256 3294 3208 -718 1036 -1074 O
ATOM 2890 CB CYS A 389 25.164 4.288 -14.924 1.00 34.04 C
ANISOU 2890 CB CYS A 389 5752 3623 3561 -455 906 -1019 C
ATOM 2891 SG CYS A 389 25.205 4.677 -13.163 1.00 47.11 S
ANISOU 2891 SG CYS A 389 7509 5208 5185 -335 886 -977 S
ATOM 2892 N SER A 390 22.975 3.140 -17.024 1.00 26.89 N
ANISOU 2892 N SER A 390 4687 2833 2696 -780 1097 -1143 N
ATOM 2893 CA SER A 390 22.497 3.244 -18.400 1.00 26.51 C
ANISOU 2893 CA SER A 390 4515 2883 2674 -878 1098 -1192 C
ATOM 2894 C SER A 390 21.179 4.009 -18.413 1.00 31.88 C
ANISOU 2894 C SER A 390 5101 3649 3361 -902 1086 -1247 C
ATOM 2895 O SER A 390 20.727 4.530 -17.391 1.00 30.18 O
ANISOU 2895 O SER A 390 4917 3419 3131 -831 1066 -1246 O
ATOM 2896 CB SER A 390 22.344 1.865 -19.051 1.00 25.81 C
ANISOU 2896 CB SER A 390 4441 2769 2596 -1030 1230 -1212 C
ATOM 2897 OG SER A 390 21.116 1.252 -18.695 1.00 28.97 O
ANISOU 2897 OG SER A 390 4845 3162 3001 -1140 1348 -1258 O
ATOM 2898 N TYR A 391 20.554 4.051 -19.593 1.00 33.64 N
ANISOU 2898 N TYR A 391 5207 3969 3607 -1003 1101 -1298 N
ATOM 2899 CA TYR A 391 19.360 4.871 -19.779 1.00 32.42 C
ANISOU 2899 CA TYR A 391 4945 3914 3458 -1021 1075 -1352 C
ATOM 2900 C TYR A 391 18.195 4.378 -18.930 1.00 37.90 C
ANISOU 2900 C TYR A 391 5665 4586 4150 -1089 1179 -1393 C
ATOM 2901 O TYR A 391 17.412 5.184 -18.414 1.00 40.28 O
ANISOU 2901 O TYR A 391 5932 4930 4443 -1041 1143 -1417 O
ATOM 2902 CB TYR A 391 18.970 4.898 -21.258 1.00 31.83 C
ANISOU 2902 CB TYR A 391 4738 3951 3406 -1123 1078 -1398 C
ATOM 2903 CG TYR A 391 17.605 5.502 -21.525 1.00 31.46 C
ANISOU 2903 CG TYR A 391 4572 4015 3367 -1171 1076 -1465 C
ATOM 2904 CD1 TYR A 391 17.422 6.881 -21.536 1.00 34.31 C
ANISOU 2904 CD1 TYR A 391 4875 4441 3718 -1066 958 -1461 C
ATOM 2905 CD2 TYR A 391 16.499 4.693 -21.766 1.00 29.69 C
ANISOU 2905 CD2 TYR A 391 4292 3829 3158 -1322 1194 -1534 C
ATOM 2906 CE1 TYR A 391 16.173 7.436 -21.782 1.00 36.33 C
ANISOU 2906 CE1 TYR A 391 5022 4804 3979 -1106 955 -1522 C
ATOM 2907 CE2 TYR A 391 15.248 5.239 -22.009 1.00 36.77 C
ANISOU 2907 CE2 TYR A 391 5071 4836 4062 -1365 1191 -1600 C
ATOM 2908 CZ TYR A 391 15.092 6.609 -22.016 1.00 40.58 C
ANISOU 2908 CZ TYR A 391 5498 5387 4532 -1254 1070 -1593 C
ATOM 2909 OH TYR A 391 13.851 7.152 -22.260 1.00 45.47 O
ANISOU 2909 OH TYR A 391 5999 6121 5157 -1293 1066 -1659 O
ATOM 2910 N SER A 392 18.057 3.058 -18.781 1.00 36.23 N
ANISOU 2910 N SER A 392 5516 4306 3945 -1201 1313 -1402 N
ATOM 2911 CA SER A 392 16.908 2.499 -18.075 1.00 43.92 C
ANISOU 2911 CA SER A 392 6510 5256 4921 -1287 1428 -1448 C
ATOM 2912 C SER A 392 16.911 2.820 -16.586 1.00 41.83 C
ANISOU 2912 C SER A 392 6353 4912 4629 -1175 1418 -1411 C
ATOM 2913 O SER A 392 15.852 2.756 -15.952 1.00 46.64 O
ANISOU 2913 O SER A 392 6961 5523 5238 -1215 1483 -1452 O
ATOM 2914 CB SER A 392 16.853 0.984 -18.284 1.00 48.44 C
ANISOU 2914 CB SER A 392 7137 5762 5508 -1434 1577 -1462 C
ATOM 2915 OG SER A 392 18.142 0.407 -18.164 1.00 53.60 O
ANISOU 2915 OG SER A 392 7902 6318 6146 -1385 1576 -1392 O
ATOM 2916 N ASP A 393 18.069 3.155 -16.012 1.00 38.99 N
ANISOU 2916 N ASP A 393 6082 4486 4245 -1036 1338 -1338 N
ATOM 2917 CA ASP A 393 18.105 3.541 -14.606 1.00 43.40 C
ANISOU 2917 CA ASP A 393 6735 4980 4776 -919 1317 -1303 C
ATOM 2918 C ASP A 393 17.434 4.888 -14.376 1.00 41.07 C
ANISOU 2918 C ASP A 393 6359 4773 4474 -833 1220 -1332 C
ATOM 2919 O ASP A 393 16.835 5.111 -13.317 1.00 39.03 O
ANISOU 2919 O ASP A 393 6143 4490 4197 -789 1242 -1337 O
ATOM 2920 CB ASP A 393 19.550 3.593 -14.106 1.00 44.44 C
ANISOU 2920 CB ASP A 393 6968 5032 4887 -794 1249 -1224 C
ATOM 2921 CG ASP A 393 20.249 2.253 -14.199 1.00 41.51 C
ANISOU 2921 CG ASP A 393 6694 4565 4512 -863 1345 -1188 C
ATOM 2922 OD1 ASP A 393 19.593 1.220 -13.950 1.00 40.30 O
ANISOU 2922 OD1 ASP A 393 6594 4357 4361 -975 1485 -1208 O
ATOM 2923 OD2 ASP A 393 21.455 2.235 -14.523 1.00 41.57 O
ANISOU 2923 OD2 ASP A 393 6728 4551 4516 -805 1283 -1143 O
ATOM 2924 N LEU A 394 17.513 5.789 -15.355 1.00 37.87 N
ANISOU 2924 N LEU A 394 5841 4468 4080 -807 1115 -1349 N
ATOM 2925 CA LEU A 394 17.130 7.179 -15.165 1.00 34.94 C
ANISOU 2925 CA LEU A 394 5408 4171 3698 -698 1000 -1361 C
ATOM 2926 C LEU A 394 16.061 7.673 -16.127 1.00 33.01 C
ANISOU 2926 C LEU A 394 5023 4052 3470 -775 991 -1427 C
ATOM 2927 O LEU A 394 15.366 8.640 -15.796 1.00 34.40 O
ANISOU 2927 O LEU A 394 5155 4284 3631 -711 934 -1449 O
ATOM 2928 CB LEU A 394 18.365 8.085 -15.286 1.00 31.99 C
ANISOU 2928 CB LEU A 394 5043 3794 3318 -556 854 -1308 C
ATOM 2929 CG LEU A 394 19.506 7.726 -14.332 1.00 35.78 C
ANISOU 2929 CG LEU A 394 5645 4165 3784 -470 845 -1245 C
ATOM 2930 CD1 LEU A 394 20.773 8.491 -14.685 1.00 28.50 C
ANISOU 2930 CD1 LEU A 394 4708 3252 2870 -361 712 -1205 C
ATOM 2931 CD2 LEU A 394 19.081 7.989 -12.894 1.00 36.36 C
ANISOU 2931 CD2 LEU A 394 5786 4197 3833 -391 856 -1239 C
ATOM 2932 N GLY A 395 15.906 7.052 -17.292 1.00 33.99 N
ANISOU 2932 N GLY A 395 5071 4223 3620 -908 1044 -1459 N
ATOM 2933 CA GLY A 395 14.871 7.473 -18.221 1.00 30.65 C
ANISOU 2933 CA GLY A 395 4502 3928 3213 -988 1039 -1525 C
ATOM 2934 C GLY A 395 15.114 8.826 -18.849 1.00 31.92 C
ANISOU 2934 C GLY A 395 4588 4171 3369 -890 896 -1511 C
ATOM 2935 O GLY A 395 14.155 9.531 -19.177 1.00 38.40 O
ANISOU 2935 O GLY A 395 5307 5094 4191 -903 868 -1557 O
ATOM 2936 N THR A 396 16.377 9.210 -19.028 1.00 29.60 N
ANISOU 2936 N THR A 396 4343 3834 3070 -793 807 -1447 N
ATOM 2937 CA THR A 396 16.721 10.492 -19.622 1.00 23.54 C
ANISOU 2937 CA THR A 396 3520 3125 2298 -699 674 -1426 C
ATOM 2938 C THR A 396 17.883 10.317 -20.586 1.00 33.43 C
ANISOU 2938 C THR A 396 4770 4366 3566 -704 638 -1388 C
ATOM 2939 O THR A 396 18.760 9.472 -20.385 1.00 31.22 O
ANISOU 2939 O THR A 396 4569 4004 3289 -712 678 -1356 O
ATOM 2940 CB THR A 396 17.099 11.540 -18.563 1.00 22.93 C
ANISOU 2940 CB THR A 396 3520 2998 2193 -530 571 -1383 C
ATOM 2941 OG1 THR A 396 17.522 12.744 -19.215 1.00 22.08 O
ANISOU 2941 OG1 THR A 396 3371 2933 2085 -450 447 -1356 O
ATOM 2942 CG2 THR A 396 18.222 11.024 -17.674 1.00 22.73 C
ANISOU 2942 CG2 THR A 396 3618 2857 2160 -456 571 -1331 C
ATOM 2943 N ASN A 397 17.873 11.123 -21.644 1.00 33.98 N
ANISOU 2943 N ASN A 397 4747 4521 3643 -698 566 -1392 N
ATOM 2944 CA ASN A 397 18.974 11.205 -22.591 1.00 30.89 C
ANISOU 2944 CA ASN A 397 4348 4126 3263 -685 516 -1353 C
ATOM 2945 C ASN A 397 19.783 12.481 -22.426 1.00 27.42 C
ANISOU 2945 C ASN A 397 3945 3660 2814 -538 381 -1299 C
ATOM 2946 O ASN A 397 20.704 12.725 -23.212 1.00 30.84 O
ANISOU 2946 O ASN A 397 4370 4092 3257 -517 329 -1267 O
ATOM 2947 CB ASN A 397 18.450 11.123 -24.030 1.00 29.28 C
ANISOU 2947 CB ASN A 397 4013 4036 3075 -792 542 -1396 C
ATOM 2948 CG ASN A 397 17.756 9.812 -24.330 1.00 39.48 C
ANISOU 2948 CG ASN A 397 5267 5354 4380 -946 676 -1451 C
ATOM 2949 OD1 ASN A 397 18.369 8.747 -24.272 1.00 36.07 O
ANISOU 2949 OD1 ASN A 397 4900 4851 3953 -996 745 -1436 O
ATOM 2950 ND2 ASN A 397 16.480 9.883 -24.686 1.00 40.65 N
ANISOU 2950 ND2 ASN A 397 5308 5606 4532 -1024 714 -1518 N
ATOM 2951 N SER A 398 19.463 13.298 -21.423 1.00 27.95 N
ANISOU 2951 N SER A 398 4056 3703 2861 -438 325 -1289 N
ATOM 2952 CA SER A 398 20.016 14.640 -21.301 1.00 29.79 C
ANISOU 2952 CA SER A 398 4320 3916 3084 -312 198 -1243 C
ATOM 2953 C SER A 398 20.895 14.809 -20.070 1.00 27.33 C
ANISOU 2953 C SER A 398 4133 3497 2756 -181 143 -1199 C
ATOM 2954 O SER A 398 21.184 15.944 -19.681 1.00 24.53 O
ANISOU 2954 O SER A 398 3830 3108 2382 -77 47 -1160 O
ATOM 2955 CB SER A 398 18.887 15.669 -21.277 1.00 30.12 C
ANISOU 2955 CB SER A 398 4300 4031 3114 -300 164 -1266 C
ATOM 2956 OG SER A 398 18.048 15.517 -22.401 1.00 35.88 O
ANISOU 2956 OG SER A 398 4895 4877 3859 -409 207 -1317 O
ATOM 2957 N LEU A 399 21.325 13.714 -19.450 1.00 21.45 N
ANISOU 2957 N LEU A 399 3437 2697 2015 -193 207 -1203 N
ATOM 2958 CA LEU A 399 22.126 13.804 -18.235 1.00 23.31 C
ANISOU 2958 CA LEU A 399 3748 2863 2248 -69 157 -1182 C
ATOM 2959 C LEU A 399 23.503 14.375 -18.557 1.00 26.28 C
ANISOU 2959 C LEU A 399 4118 3221 2646 18 52 -1149 C
ATOM 2960 O LEU A 399 24.214 13.850 -19.421 1.00 20.93 O
ANISOU 2960 O LEU A 399 3430 2539 1986 -39 74 -1133 O
ATOM 2961 CB LEU A 399 22.260 12.429 -17.588 1.00 21.73 C
ANISOU 2961 CB LEU A 399 3594 2610 2052 -133 271 -1189 C
ATOM 2962 CG LEU A 399 22.865 12.424 -16.180 1.00 28.84 C
ANISOU 2962 CG LEU A 399 4547 3454 2956 -41 255 -1176 C
ATOM 2963 CD1 LEU A 399 21.852 12.909 -15.146 1.00 20.97 C
ANISOU 2963 CD1 LEU A 399 3556 2473 1940 6 257 -1204 C
ATOM 2964 CD2 LEU A 399 23.402 11.047 -15.822 1.00 29.15 C
ANISOU 2964 CD2 LEU A 399 4669 3411 2995 -108 361 -1150 C
ATOM 2965 N ARG A 400 23.878 15.449 -17.858 1.00 27.25 N
ANISOU 2965 N ARG A 400 4174 3366 2815 120 -36 -1119 N
ATOM 2966 CA ARG A 400 25.191 16.058 -18.014 1.00 21.93 C
ANISOU 2966 CA ARG A 400 3332 2760 2241 59 -20 -1133 C
ATOM 2967 C ARG A 400 26.047 15.981 -16.761 1.00 19.54 C
ANISOU 2967 C ARG A 400 3147 2352 1925 23 54 -1100 C
ATOM 2968 O ARG A 400 27.276 16.061 -16.867 1.00 20.49 O
ANISOU 2968 O ARG A 400 3326 2411 2046 39 32 -1047 O
ATOM 2969 CB ARG A 400 25.058 17.534 -18.419 1.00 26.86 C
ANISOU 2969 CB ARG A 400 4045 3341 2818 -139 84 -1040 C
ATOM 2970 CG ARG A 400 24.281 17.765 -19.702 1.00 40.70 C
ANISOU 2970 CG ARG A 400 6025 4985 4456 -66 -33 -927 C
ATOM 2971 CD ARG A 400 24.643 19.098 -20.340 1.00 52.76 C
ANISOU 2971 CD ARG A 400 7412 6610 6024 -114 -59 -955 C
ATOM 2972 NE ARG A 400 23.962 19.284 -21.617 1.00 65.32 N
ANISOU 2972 NE ARG A 400 8983 8245 7589 -99 -125 -973 N
ATOM 2973 CZ ARG A 400 24.356 18.727 -22.759 1.00 68.60 C
ANISOU 2973 CZ ARG A 400 9380 8674 8010 -105 -147 -984 C
ATOM 2974 NH1 ARG A 400 25.427 17.944 -22.789 1.00 66.26 N
ANISOU 2974 NH1 ARG A 400 9128 8318 7730 -87 -140 -951 N
ATOM 2975 NH2 ARG A 400 23.677 18.950 -23.875 1.00 68.49 N
ANISOU 2975 NH2 ARG A 400 9246 8764 8013 -136 -160 -1022 N
ATOM 2976 N HIS A 401 25.435 15.826 -15.589 1.00 18.43 N
ANISOU 2976 N HIS A 401 3064 2178 1759 59 77 -1116 N
ATOM 2977 CA HIS A 401 26.141 15.852 -14.317 1.00 18.62 C
ANISOU 2977 CA HIS A 401 3221 2090 1765 131 65 -1024 C
ATOM 2978 C HIS A 401 25.637 14.704 -13.458 1.00 22.76 C
ANISOU 2978 C HIS A 401 3811 2574 2261 140 129 -1049 C
ATOM 2979 O HIS A 401 24.427 14.574 -13.240 1.00 22.94 O
ANISOU 2979 O HIS A 401 3804 2644 2271 127 161 -1113 O
ATOM 2980 CB HIS A 401 25.924 17.190 -13.607 1.00 20.70 C
ANISOU 2980 CB HIS A 401 3515 2333 2017 205 -4 -956 C
ATOM 2981 CG HIS A 401 26.670 17.327 -12.315 1.00 28.08 C
ANISOU 2981 CG HIS A 401 4563 3175 2931 328 -66 -856 C
ATOM 2982 ND1 HIS A 401 27.761 18.156 -12.174 1.00 25.15 N
ANISOU 2982 ND1 HIS A 401 4221 2769 2566 433 -187 -759 N
ATOM 2983 CD2 HIS A 401 26.472 16.755 -11.102 1.00 26.76 C
ANISOU 2983 CD2 HIS A 401 4485 2951 2731 367 -30 -841 C
ATOM 2984 CE1 HIS A 401 28.207 18.083 -10.932 1.00 20.38 C
ANISOU 2984 CE1 HIS A 401 3715 2101 1929 528 -227 -692 C
ATOM 2985 NE2 HIS A 401 27.443 17.239 -10.261 1.00 23.99 N
ANISOU 2985 NE2 HIS A 401 4218 2538 2359 489 -128 -735 N
ATOM 2986 N LEU A 402 26.562 13.876 -12.974 1.00 18.88 N
ANISOU 2986 N LEU A 402 3426 1993 1754 166 148 -986 N
ATOM 2987 CA LEU A 402 26.220 12.719 -12.153 1.00 19.73 C
ANISOU 2987 CA LEU A 402 3635 2037 1824 160 228 -980 C
ATOM 2988 C LEU A 402 27.220 12.615 -11.013 1.00 22.15 C
ANISOU 2988 C LEU A 402 4074 2241 2102 241 208 -881 C
ATOM 2989 O LEU A 402 28.406 12.356 -11.244 1.00 22.13 O
ANISOU 2989 O LEU A 402 4107 2201 2099 262 179 -830 O
ATOM 2990 CB LEU A 402 26.211 11.431 -12.984 1.00 21.04 C
ANISOU 2990 CB LEU A 402 3814 2198 1983 85 296 -1007 C
ATOM 2991 CG LEU A 402 25.915 10.119 -12.248 1.00 24.00 C
ANISOU 2991 CG LEU A 402 4313 2489 2318 51 407 -986 C
ATOM 2992 CD1 LEU A 402 24.598 10.204 -11.494 1.00 21.71 C
ANISOU 2992 CD1 LEU A 402 4035 2208 2008 45 456 -1019 C
ATOM 2993 CD2 LEU A 402 25.888 8.951 -13.220 1.00 21.50 C
ANISOU 2993 CD2 LEU A 402 4006 2165 1999 -48 485 -1001 C
ATOM 2994 N ASP A 403 26.738 12.807 -9.786 1.00 20.18 N
ANISOU 2994 N ASP A 403 3896 1952 1820 294 218 -853 N
ATOM 2995 CA ASP A 403 27.566 12.742 -8.585 1.00 24.98 C
ANISOU 2995 CA ASP A 403 4637 2471 2383 391 186 -755 C
ATOM 2996 C ASP A 403 27.101 11.551 -7.758 1.00 25.78 C
ANISOU 2996 C ASP A 403 4849 2504 2441 371 295 -753 C
ATOM 2997 O ASP A 403 25.980 11.548 -7.239 1.00 24.35 O
ANISOU 2997 O ASP A 403 4672 2331 2250 354 350 -790 O
ATOM 2998 CB ASP A 403 27.475 14.038 -7.778 1.00 27.94 C
ANISOU 2998 CB ASP A 403 5019 2851 2744 491 91 -706 C
ATOM 2999 CG ASP A 403 28.548 14.135 -6.699 1.00 37.07 C
ANISOU 2999 CG ASP A 403 6299 3940 3846 611 16 -600 C
ATOM 3000 OD1 ASP A 403 29.138 13.097 -6.336 1.00 37.43 O
ANISOU 3000 OD1 ASP A 403 6441 3925 3856 614 63 -570 O
ATOM 3001 OD2 ASP A 403 28.798 15.256 -6.206 1.00 37.63 O
ANISOU 3001 OD2 ASP A 403 6370 4024 3904 707 -97 -547 O
ATOM 3002 N LEU A 404 27.966 10.546 -7.630 1.00 26.71 N
ANISOU 3002 N LEU A 404 5063 2556 2531 373 330 -708 N
ATOM 3003 CA LEU A 404 27.684 9.360 -6.831 1.00 27.36 C
ANISOU 3003 CA LEU A 404 5274 2557 2565 356 439 -688 C
ATOM 3004 C LEU A 404 28.769 9.138 -5.786 1.00 22.96 C
ANISOU 3004 C LEU A 404 4857 1920 1946 459 402 -590 C
ATOM 3005 O LEU A 404 29.020 8.002 -5.378 1.00 27.21 O
ANISOU 3005 O LEU A 404 5512 2385 2443 448 482 -560 O
ATOM 3006 CB LEU A 404 27.530 8.127 -7.722 1.00 23.13 C
ANISOU 3006 CB LEU A 404 4733 2013 2043 244 541 -730 C
ATOM 3007 CG LEU A 404 26.281 8.130 -8.601 1.00 25.58 C
ANISOU 3007 CG LEU A 404 4930 2399 2391 142 591 -823 C
ATOM 3008 CD1 LEU A 404 26.432 7.204 -9.800 1.00 23.28 C
ANISOU 3008 CD1 LEU A 404 4608 2120 2119 41 647 -853 C
ATOM 3009 CD2 LEU A 404 25.057 7.755 -7.783 1.00 29.87 C
ANISOU 3009 CD2 LEU A 404 5527 2914 2910 113 687 -844 C
ATOM 3010 N SER A 405 29.412 10.218 -5.346 1.00 22.39 N
ANISOU 3010 N SER A 405 4781 1864 1861 564 277 -538 N
ATOM 3011 CA SER A 405 30.552 10.140 -4.449 1.00 22.55 C
ANISOU 3011 CA SER A 405 4921 1834 1815 673 212 -449 C
ATOM 3012 C SER A 405 30.104 9.968 -3.001 1.00 27.43 C
ANISOU 3012 C SER A 405 5667 2393 2361 740 245 -403 C
ATOM 3013 O SER A 405 28.962 10.254 -2.636 1.00 31.06 O
ANISOU 3013 O SER A 405 6111 2861 2831 720 291 -435 O
ATOM 3014 CB SER A 405 31.425 11.390 -4.576 1.00 32.08 C
ANISOU 3014 CB SER A 405 6069 3092 3029 760 53 -411 C
ATOM 3015 OG SER A 405 30.687 12.563 -4.280 1.00 34.94 O
ANISOU 3015 OG SER A 405 6374 3496 3405 795 -5 -418 O
ATOM 3016 N PHE A 406 31.034 9.490 -2.174 1.00 23.83 N
ANISOU 3016 N PHE A 406 5344 1882 1829 822 222 -331 N
ATOM 3017 CA PHE A 406 30.801 9.269 -0.745 1.00 24.69 C
ANISOU 3017 CA PHE A 406 5595 1931 1853 899 248 -276 C
ATOM 3018 C PHE A 406 29.586 8.374 -0.510 1.00 32.49 C
ANISOU 3018 C PHE A 406 6632 2866 2845 814 411 -311 C
ATOM 3019 O PHE A 406 28.700 8.678 0.292 1.00 34.79 O
ANISOU 3019 O PHE A 406 6955 3144 3117 836 441 -310 O
ATOM 3020 CB PHE A 406 30.643 10.597 -0.001 1.00 27.86 C
ANISOU 3020 CB PHE A 406 5981 2375 2230 999 132 -247 C
ATOM 3021 CG PHE A 406 31.845 11.494 -0.094 1.00 28.15 C
ANISOU 3021 CG PHE A 406 5983 2464 2249 1088 -35 -208 C
ATOM 3022 CD1 PHE A 406 32.923 11.327 0.765 1.00 29.50 C
ANISOU 3022 CD1 PHE A 406 6269 2616 2325 1194 -109 -142 C
ATOM 3023 CD2 PHE A 406 31.892 12.508 -1.030 1.00 22.61 C
ANISOU 3023 CD2 PHE A 406 5135 1836 1619 1068 -121 -240 C
ATOM 3024 CE1 PHE A 406 34.027 12.155 0.677 1.00 27.60 C
ANISOU 3024 CE1 PHE A 406 5989 2434 2065 1270 -267 -117 C
ATOM 3025 CE2 PHE A 406 32.989 13.337 -1.123 1.00 33.41 C
ANISOU 3025 CE2 PHE A 406 6470 3252 2971 1146 -274 -205 C
ATOM 3026 CZ PHE A 406 34.059 13.162 -0.268 1.00 29.00 C
ANISOU 3026 CZ PHE A 406 6019 2680 2320 1244 -349 -148 C
ATOM 3027 N ASN A 407 29.551 7.254 -1.218 1.00 28.49 N
ANISOU 3027 N ASN A 407 6131 2329 2363 715 516 -343 N
ATOM 3028 CA ASN A 407 28.470 6.284 -1.110 1.00 30.19 C
ANISOU 3028 CA ASN A 407 6393 2493 2583 621 675 -377 C
ATOM 3029 C ASN A 407 29.054 4.901 -0.828 1.00 27.66 C
ANISOU 3029 C ASN A 407 6221 2083 2206 611 765 -330 C
ATOM 3030 O ASN A 407 30.252 4.747 -0.579 1.00 34.72 O
ANISOU 3030 O ASN A 407 7185 2956 3050 691 699 -272 O
ATOM 3031 CB ASN A 407 27.614 6.297 -2.380 1.00 26.39 C
ANISOU 3031 CB ASN A 407 5761 2076 2189 489 723 -475 C
ATOM 3032 CG ASN A 407 26.666 7.478 -2.430 1.00 31.62 C
ANISOU 3032 CG ASN A 407 6305 2816 2894 491 674 -528 C
ATOM 3033 OD1 ASN A 407 26.041 7.828 -1.427 1.00 32.58 O
ANISOU 3033 OD1 ASN A 407 6477 2917 2984 541 687 -512 O
ATOM 3034 ND2 ASN A 407 26.546 8.094 -3.597 1.00 27.27 N
ANISOU 3034 ND2 ASN A 407 5597 2353 2410 440 621 -592 N
ATOM 3035 N GLY A 408 28.190 3.893 -0.867 1.00 28.51 N
ANISOU 3035 N GLY A 408 6377 2137 2320 511 916 -358 N
ATOM 3036 CA GLY A 408 28.620 2.538 -0.607 1.00 34.24 C
ANISOU 3036 CA GLY A 408 7249 2768 2992 491 1018 -313 C
ATOM 3037 C GLY A 408 29.019 1.776 -1.853 1.00 37.34 C
ANISOU 3037 C GLY A 408 7588 3171 3427 394 1056 -349 C
ATOM 3038 O GLY A 408 29.931 2.184 -2.578 1.00 37.74 O
ANISOU 3038 O GLY A 408 7559 3278 3504 420 953 -354 O
ATOM 3039 N ALA A 409 28.335 0.666 -2.112 1.00 35.22 N
ANISOU 3039 N ALA A 409 7365 2848 3168 279 1206 -374 N
ATOM 3040 CA ALA A 409 28.686 -0.229 -3.208 1.00 30.77 C
ANISOU 3040 CA ALA A 409 6776 2281 2633 182 1259 -400 C
ATOM 3041 C ALA A 409 28.037 0.252 -4.499 1.00 32.24 C
ANISOU 3041 C ALA A 409 6776 2566 2908 78 1242 -491 C
ATOM 3042 O ALA A 409 26.807 0.262 -4.615 1.00 31.13 O
ANISOU 3042 O ALA A 409 6586 2443 2800 -9 1317 -545 O
ATOM 3043 CB ALA A 409 28.251 -1.660 -2.892 1.00 31.41 C
ANISOU 3043 CB ALA A 409 6999 2255 2680 102 1432 -381 C
ATOM 3044 N ILE A 410 28.862 0.638 -5.467 1.00 31.06 N
ANISOU 3044 N ILE A 410 6525 2482 2793 88 1145 -508 N
ATOM 3045 CA ILE A 410 28.411 1.008 -6.804 1.00 32.37 C
ANISOU 3045 CA ILE A 410 6524 2742 3033 -6 1125 -587 C
ATOM 3046 C ILE A 410 28.922 -0.058 -7.767 1.00 33.83 C
ANISOU 3046 C ILE A 410 6719 2907 3227 -90 1186 -595 C
ATOM 3047 O ILE A 410 30.113 -0.090 -8.104 1.00 36.00 O
ANISOU 3047 O ILE A 410 6997 3186 3494 -37 1116 -567 O
ATOM 3048 CB ILE A 410 28.895 2.407 -7.205 1.00 32.41 C
ANISOU 3048 CB ILE A 410 6397 2843 3074 70 965 -603 C
ATOM 3049 CG1 ILE A 410 28.288 3.466 -6.279 1.00 32.65 C
ANISOU 3049 CG1 ILE A 410 6415 2894 3096 144 911 -598 C
ATOM 3050 CG2 ILE A 410 28.543 2.696 -8.655 1.00 30.55 C
ANISOU 3050 CG2 ILE A 410 6001 2701 2904 -23 946 -678 C
ATOM 3051 CD1 ILE A 410 28.768 4.872 -6.568 1.00 36.04 C
ANISOU 3051 CD1 ILE A 410 6728 3407 3557 221 758 -605 C
ATOM 3052 N ILE A 411 28.025 -0.937 -8.208 1.00 30.94 N
ANISOU 3052 N ILE A 411 6357 2520 2877 -223 1317 -635 N
ATOM 3053 CA ILE A 411 28.383 -2.086 -9.032 1.00 29.05 C
ANISOU 3053 CA ILE A 411 6146 2250 2643 -315 1398 -640 C
ATOM 3054 C ILE A 411 28.253 -1.673 -10.490 1.00 33.52 C
ANISOU 3054 C ILE A 411 6544 2921 3271 -390 1350 -706 C
ATOM 3055 O ILE A 411 27.144 -1.428 -10.982 1.00 35.55 O
ANISOU 3055 O ILE A 411 6706 3235 3565 -480 1384 -768 O
ATOM 3056 CB ILE A 411 27.508 -3.309 -8.721 1.00 33.65 C
ANISOU 3056 CB ILE A 411 6831 2746 3208 -427 1574 -644 C
ATOM 3057 CG1 ILE A 411 27.935 -3.964 -7.404 1.00 32.85 C
ANISOU 3057 CG1 ILE A 411 6923 2526 3033 -349 1628 -564 C
ATOM 3058 CG2 ILE A 411 27.553 -4.322 -9.873 1.00 30.63 C
ANISOU 3058 CG2 ILE A 411 6426 2362 2851 -557 1657 -676 C
ATOM 3059 CD1 ILE A 411 27.316 -3.340 -6.177 1.00 33.68 C
ANISOU 3059 CD1 ILE A 411 7075 2609 3112 -278 1621 -543 C
ATOM 3060 N MET A 412 29.388 -1.600 -11.183 1.00 27.61 N
ANISOU 3060 N MET A 412 5762 2200 2530 -352 1272 -694 N
ATOM 3061 CA MET A 412 29.403 -1.260 -12.600 1.00 28.78 C
ANISOU 3061 CA MET A 412 5763 2441 2730 -416 1227 -748 C
ATOM 3062 C MET A 412 28.988 -2.477 -13.420 1.00 33.65 C
ANISOU 3062 C MET A 412 6392 3037 3358 -562 1357 -778 C
ATOM 3063 O MET A 412 29.615 -3.540 -13.333 1.00 41.56 O
ANISOU 3063 O MET A 412 7499 3961 4329 -575 1423 -743 O
ATOM 3064 CB MET A 412 30.788 -0.766 -13.019 1.00 26.05 C
ANISOU 3064 CB MET A 412 5381 2126 2389 -324 1104 -724 C
ATOM 3065 CG MET A 412 31.232 0.516 -12.324 1.00 29.69 C
ANISOU 3065 CG MET A 412 5814 2619 2849 -190 970 -700 C
ATOM 3066 SD MET A 412 29.994 1.826 -12.391 1.00 40.02 S
ANISOU 3066 SD MET A 412 6991 4018 4197 -198 918 -755 S
ATOM 3067 CE MET A 412 29.740 1.986 -14.158 1.00 28.29 C
ANISOU 3067 CE MET A 412 5351 2633 2765 -301 905 -822 C
ATOM 3068 N SER A 413 27.923 -2.321 -14.210 1.00 32.31 N
ANISOU 3068 N SER A 413 6113 2937 3228 -673 1393 -842 N
ATOM 3069 CA SER A 413 27.440 -3.400 -15.057 1.00 33.25 C
ANISOU 3069 CA SER A 413 6225 3048 3362 -825 1514 -878 C
ATOM 3070 C SER A 413 27.092 -2.956 -16.471 1.00 31.09 C
ANISOU 3070 C SER A 413 5791 2889 3135 -903 1477 -938 C
ATOM 3071 O SER A 413 26.850 -3.816 -17.322 1.00 34.17 O
ANISOU 3071 O SER A 413 6162 3283 3539 -1027 1564 -968 O
ATOM 3072 CB SER A 413 26.212 -4.074 -14.420 1.00 44.03 C
ANISOU 3072 CB SER A 413 7651 4358 4720 -921 1655 -897 C
ATOM 3073 OG SER A 413 25.037 -3.304 -14.593 1.00 52.51 O
ANISOU 3073 OG SER A 413 8611 5514 5826 -966 1642 -956 O
ATOM 3074 N ALA A 414 27.069 -1.655 -16.751 1.00 32.12 N
ANISOU 3074 N ALA A 414 5809 3110 3286 -836 1352 -956 N
ATOM 3075 CA ALA A 414 26.773 -1.137 -18.078 1.00 30.72 C
ANISOU 3075 CA ALA A 414 5484 3043 3146 -897 1308 -1006 C
ATOM 3076 C ALA A 414 27.570 0.145 -18.270 1.00 29.86 C
ANISOU 3076 C ALA A 414 5307 2994 3046 -769 1149 -990 C
ATOM 3077 O ALA A 414 27.718 0.933 -17.330 1.00 36.66 O
ANISOU 3077 O ALA A 414 6192 3841 3895 -657 1076 -965 O
ATOM 3078 CB ALA A 414 25.277 -0.867 -18.258 1.00 26.53 C
ANISOU 3078 CB ALA A 414 4868 2577 2636 -990 1355 -1068 C
ATOM 3079 N ASN A 415 28.077 0.354 -19.480 1.00 27.64 N
ANISOU 3079 N ASN A 415 4941 2775 2786 -789 1100 -1003 N
ATOM 3080 CA ASN A 415 28.943 1.503 -19.755 1.00 23.42 C
ANISOU 3080 CA ASN A 415 4346 2290 2263 -676 957 -987 C
ATOM 3081 C ASN A 415 28.176 2.656 -20.391 1.00 23.33 C
ANISOU 3081 C ASN A 415 4205 2383 2275 -681 888 -1027 C
ATOM 3082 O ASN A 415 28.543 3.163 -21.447 1.00 27.82 O
ANISOU 3082 O ASN A 415 4690 3017 2862 -682 826 -1037 O
ATOM 3083 CB ASN A 415 30.124 1.086 -20.619 1.00 26.89 C
ANISOU 3083 CB ASN A 415 4785 2725 2708 -676 938 -970 C
ATOM 3084 CG ASN A 415 29.713 0.258 -21.813 1.00 28.69 C
ANISOU 3084 CG ASN A 415 4967 2985 2947 -817 1027 -1005 C
ATOM 3085 OD1 ASN A 415 28.530 0.118 -22.116 1.00 30.16 O
ANISOU 3085 OD1 ASN A 415 5102 3213 3143 -918 1092 -1048 O
ATOM 3086 ND2 ASN A 415 30.699 -0.300 -22.506 1.00 23.55 N
ANISOU 3086 ND2 ASN A 415 4330 2320 2297 -826 1030 -991 N
ATOM 3087 N PHE A 416 27.085 3.061 -19.739 1.00 24.68 N
ANISOU 3087 N PHE A 416 4364 2569 2442 -684 902 -1050 N
ATOM 3088 CA PHE A 416 26.425 4.349 -19.944 1.00 24.79 C
ANISOU 3088 CA PHE A 416 4278 2670 2469 -645 815 -1078 C
ATOM 3089 C PHE A 416 25.783 4.510 -21.316 1.00 26.96 C
ANISOU 3089 C PHE A 416 4436 3043 2764 -744 826 -1123 C
ATOM 3090 O PHE A 416 25.686 5.635 -21.819 1.00 23.61 O
ANISOU 3090 O PHE A 416 3929 2693 2350 -696 731 -1133 O
ATOM 3091 CB PHE A 416 27.397 5.507 -19.695 1.00 21.58 C
ANISOU 3091 CB PHE A 416 3859 2273 2067 -499 673 -1047 C
ATOM 3092 CG PHE A 416 27.866 5.604 -18.274 1.00 23.42 C
ANISOU 3092 CG PHE A 416 4183 2431 2283 -396 649 -1010 C
ATOM 3093 CD1 PHE A 416 28.944 4.854 -17.834 1.00 21.78 C
ANISOU 3093 CD1 PHE A 416 4070 2144 2062 -367 671 -966 C
ATOM 3094 CD2 PHE A 416 27.234 6.449 -17.378 1.00 21.51 C
ANISOU 3094 CD2 PHE A 416 3934 2203 2036 -329 606 -1019 C
ATOM 3095 CE1 PHE A 416 29.383 4.944 -16.529 1.00 21.88 C
ANISOU 3095 CE1 PHE A 416 4169 2089 2054 -275 651 -926 C
ATOM 3096 CE2 PHE A 416 27.667 6.543 -16.069 1.00 27.65 C
ANISOU 3096 CE2 PHE A 416 4795 2914 2797 -241 589 -981 C
ATOM 3097 CZ PHE A 416 28.745 5.790 -15.645 1.00 26.60 C
ANISOU 3097 CZ PHE A 416 4758 2701 2648 -215 612 -931 C
ATOM 3098 N MET A 417 25.328 3.423 -21.934 1.00 26.41 N
ANISOU 3098 N MET A 417 4357 2977 2700 -882 940 -1151 N
ATOM 3099 CA MET A 417 24.504 3.550 -23.128 1.00 23.35 C
ANISOU 3099 CA MET A 417 3849 2693 2330 -985 962 -1203 C
ATOM 3100 C MET A 417 23.260 4.373 -22.814 1.00 26.93 C
ANISOU 3100 C MET A 417 4235 3210 2785 -983 941 -1242 C
ATOM 3101 O MET A 417 22.633 4.201 -21.764 1.00 28.38 O
ANISOU 3101 O MET A 417 4473 3353 2959 -979 985 -1249 O
ATOM 3102 CB MET A 417 24.108 2.169 -23.647 1.00 27.59 C
ANISOU 3102 CB MET A 417 4392 3218 2873 -1138 1099 -1234 C
ATOM 3103 CG MET A 417 25.133 1.508 -24.554 1.00 45.07 C
ANISOU 3103 CG MET A 417 6618 5418 5090 -1168 1112 -1215 C
ATOM 3104 SD MET A 417 24.411 0.069 -25.368 1.00 61.18 S
ANISOU 3104 SD MET A 417 8633 7474 7140 -1359 1267 -1268 S
ATOM 3105 CE MET A 417 22.902 0.773 -26.037 1.00 61.00 C
ANISOU 3105 CE MET A 417 8453 7590 7134 -1437 1264 -1342 C
ATOM 3106 N GLY A 418 22.911 5.284 -23.721 1.00 24.38 N
ANISOU 3106 N GLY A 418 3800 2991 2472 -982 873 -1265 N
ATOM 3107 CA GLY A 418 21.797 6.181 -23.501 1.00 25.26 C
ANISOU 3107 CA GLY A 418 3843 3173 2583 -967 839 -1300 C
ATOM 3108 C GLY A 418 22.138 7.454 -22.757 1.00 30.45 C
ANISOU 3108 C GLY A 418 4527 3815 3228 -811 715 -1265 C
ATOM 3109 O GLY A 418 21.279 8.340 -22.661 1.00 31.69 O
ANISOU 3109 O GLY A 418 4626 4035 3382 -786 672 -1291 O
ATOM 3110 N LEU A 419 23.362 7.585 -22.244 1.00 32.32 N
ANISOU 3110 N LEU A 419 4846 3975 3459 -706 655 -1211 N
ATOM 3111 CA LEU A 419 23.767 8.710 -21.410 1.00 28.73 C
ANISOU 3111 CA LEU A 419 4425 3497 2994 -554 541 -1181 C
ATOM 3112 C LEU A 419 25.044 9.364 -21.936 1.00 28.39 C
ANISOU 3112 C LEU A 419 4375 3449 2961 -468 436 -1142 C
ATOM 3113 O LEU A 419 25.898 9.804 -21.161 1.00 25.63 O
ANISOU 3113 O LEU A 419 4078 3049 2610 -352 362 -1111 O
ATOM 3114 CB LEU A 419 23.972 8.265 -19.963 1.00 24.11 C
ANISOU 3114 CB LEU A 419 3947 2820 2394 -497 571 -1160 C
ATOM 3115 CG LEU A 419 22.892 7.470 -19.220 1.00 26.48 C
ANISOU 3115 CG LEU A 419 4284 3094 2682 -575 688 -1189 C
ATOM 3116 CD1 LEU A 419 23.419 7.005 -17.868 1.00 32.74 C
ANISOU 3116 CD1 LEU A 419 5198 3784 3458 -509 712 -1152 C
ATOM 3117 CD2 LEU A 419 21.636 8.304 -19.050 1.00 25.33 C
ANISOU 3117 CD2 LEU A 419 4074 3019 2532 -570 666 -1231 C
ATOM 3118 N GLU A 420 25.198 9.454 -23.258 1.00 25.16 N
ANISOU 3118 N GLU A 420 3896 3100 2565 -525 428 -1148 N
ATOM 3119 CA GLU A 420 26.444 9.972 -23.819 1.00 31.77 C
ANISOU 3119 CA GLU A 420 4731 3927 3413 -457 342 -1112 C
ATOM 3120 C GLU A 420 26.566 11.489 -23.741 1.00 24.95 C
ANISOU 3120 C GLU A 420 3844 3085 2549 -342 214 -1096 C
ATOM 3121 O GLU A 420 27.583 12.026 -24.188 1.00 28.57 O
ANISOU 3121 O GLU A 420 4301 3535 3021 -283 138 -1068 O
ATOM 3122 CB GLU A 420 26.615 9.523 -25.275 1.00 33.27 C
ANISOU 3122 CB GLU A 420 4857 4170 3614 -557 383 -1122 C
ATOM 3123 CG GLU A 420 25.324 9.205 -26.003 1.00 40.52 C
ANISOU 3123 CG GLU A 420 5691 5174 4533 -682 460 -1172 C
ATOM 3124 CD GLU A 420 24.843 7.785 -25.755 1.00 43.25 C
ANISOU 3124 CD GLU A 420 6066 5492 4877 -794 592 -1200 C
ATOM 3125 OE1 GLU A 420 25.667 6.844 -25.803 1.00 45.14 O
ANISOU 3125 OE1 GLU A 420 6364 5671 5117 -819 639 -1180 O
ATOM 3126 OE2 GLU A 420 23.635 7.615 -25.502 1.00 44.18 O
ANISOU 3126 OE2 GLU A 420 6150 5645 4992 -858 649 -1243 O
ATOM 3127 N GLU A 421 25.570 12.191 -23.201 1.00 18.57 N
ANISOU 3127 N GLU A 421 3024 2303 1730 -313 189 -1113 N
ATOM 3128 CA GLU A 421 25.700 13.621 -22.947 1.00 17.94 C
ANISOU 3128 CA GLU A 421 2950 2222 1644 -197 69 -1091 C
ATOM 3129 C GLU A 421 26.416 13.919 -21.636 1.00 21.63 C
ANISOU 3129 C GLU A 421 3474 2627 2115 -63 1 -1079 C
ATOM 3130 O GLU A 421 26.617 15.094 -21.309 1.00 23.32 O
ANISOU 3130 O GLU A 421 3670 2842 2347 30 -92 -1038 O
ATOM 3131 CB GLU A 421 24.319 14.287 -22.942 1.00 18.99 C
ANISOU 3131 CB GLU A 421 3041 2414 1761 -222 71 -1115 C
ATOM 3132 CG GLU A 421 23.573 14.192 -24.267 1.00 28.80 C
ANISOU 3132 CG GLU A 421 4173 3757 3013 -340 120 -1147 C
ATOM 3133 CD GLU A 421 24.316 14.875 -25.401 1.00 45.27 C
ANISOU 3133 CD GLU A 421 6222 5867 5111 -329 57 -1117 C
ATOM 3134 OE1 GLU A 421 24.449 16.116 -25.368 1.00 50.07 O
ANISOU 3134 OE1 GLU A 421 6843 6468 5713 -258 -31 -1085 O
ATOM 3135 OE2 GLU A 421 24.779 14.168 -26.323 1.00 53.57 O
ANISOU 3135 OE2 GLU A 421 7239 6941 6175 -398 102 -1123 O
ATOM 3136 N LEU A 422 26.812 12.888 -20.892 1.00 21.77 N
ANISOU 3136 N LEU A 422 3524 2606 2143 -79 68 -1087 N
ATOM 3137 CA LEU A 422 27.392 13.077 -19.569 1.00 23.41 C
ANISOU 3137 CA LEU A 422 3732 2787 2374 -1 46 -1095 C
ATOM 3138 C LEU A 422 28.725 13.811 -19.662 1.00 23.21 C
ANISOU 3138 C LEU A 422 3632 2780 2408 21 1 -1075 C
ATOM 3139 O LEU A 422 29.640 13.370 -20.364 1.00 20.63 O
ANISOU 3139 O LEU A 422 3318 2435 2087 7 -2 -1062 O
ATOM 3140 CB LEU A 422 27.573 11.723 -18.882 1.00 20.11 C
ANISOU 3140 CB LEU A 422 3406 2295 1940 -54 151 -1075 C
ATOM 3141 CG LEU A 422 27.835 11.710 -17.373 1.00 24.47 C
ANISOU 3141 CG LEU A 422 4013 2791 2494 -7 170 -1056 C
ATOM 3142 CD1 LEU A 422 26.776 12.510 -16.634 1.00 18.71 C
ANISOU 3142 CD1 LEU A 422 3253 2097 1759 27 151 -1087 C
ATOM 3143 CD2 LEU A 422 27.891 10.282 -16.836 1.00 24.47 C
ANISOU 3143 CD2 LEU A 422 4128 2706 2463 -55 275 -1028 C
ATOM 3144 N GLN A 423 28.831 14.930 -18.942 1.00 26.29 N
ANISOU 3144 N GLN A 423 3993 3176 2821 5 11 -1055 N
ATOM 3145 CA GLN A 423 30.043 15.740 -18.912 1.00 25.92 C
ANISOU 3145 CA GLN A 423 4001 3072 2777 19 -22 -973 C
ATOM 3146 C GLN A 423 30.833 15.613 -17.619 1.00 23.79 C
ANISOU 3146 C GLN A 423 3846 2699 2492 115 -58 -886 C
ATOM 3147 O GLN A 423 32.057 15.770 -17.641 1.00 15.74 O
ANISOU 3147 O GLN A 423 2865 1635 1479 170 -115 -818 O
ATOM 3148 CB GLN A 423 29.702 17.220 -19.123 1.00 21.67 C
ANISOU 3148 CB GLN A 423 3450 2551 2232 36 -80 -925 C
ATOM 3149 CG GLN A 423 29.173 17.561 -20.503 1.00 28.96 C
ANISOU 3149 CG GLN A 423 4307 3550 3147 -65 -52 -958 C
ATOM 3150 CD GLN A 423 28.829 19.027 -20.625 1.00 40.43 C
ANISOU 3150 CD GLN A 423 5758 5009 4595 -3 -145 -904 C
ATOM 3151 OE1 GLN A 423 28.313 19.628 -19.685 1.00 44.44 O
ANISOU 3151 OE1 GLN A 423 6275 5502 5105 75 -189 -883 O
ATOM 3152 NE2 GLN A 423 29.124 19.616 -21.779 1.00 39.63 N
ANISOU 3152 NE2 GLN A 423 5622 4936 4499 -17 -185 -883 N
ATOM 3153 N HIS A 424 30.169 15.328 -16.498 1.00 19.23 N
ANISOU 3153 N HIS A 424 3322 2091 1892 143 -33 -889 N
ATOM 3154 CA HIS A 424 30.792 15.331 -15.179 1.00 21.21 C
ANISOU 3154 CA HIS A 424 3685 2257 2118 244 -76 -804 C
ATOM 3155 C HIS A 424 30.399 14.052 -14.450 1.00 22.90 C
ANISOU 3155 C HIS A 424 3968 2430 2302 223 10 -831 C
ATOM 3156 O HIS A 424 29.207 13.747 -14.323 1.00 21.01 O
ANISOU 3156 O HIS A 424 3703 2222 2057 177 70 -896 O
ATOM 3157 CB HIS A 424 30.354 16.569 -14.384 1.00 21.74 C
ANISOU 3157 CB HIS A 424 3763 2320 2176 330 -155 -756 C
ATOM 3158 CG HIS A 424 31.012 16.708 -13.045 1.00 22.57 C
ANISOU 3158 CG HIS A 424 3971 2356 2249 449 -224 -671 C
ATOM 3159 ND1 HIS A 424 32.063 17.570 -12.815 1.00 25.27 N
ANISOU 3159 ND1 HIS A 424 4327 2682 2593 556 -352 -590 N
ATOM 3160 CD2 HIS A 424 30.757 16.105 -11.860 1.00 27.44 C
ANISOU 3160 CD2 HIS A 424 4680 2923 2825 481 -187 -656 C
ATOM 3161 CE1 HIS A 424 32.428 17.493 -11.548 1.00 27.68 C
ANISOU 3161 CE1 HIS A 424 4725 2939 2853 646 -396 -533 C
ATOM 3162 NE2 HIS A 424 31.650 16.611 -10.946 1.00 28.81 N
ANISOU 3162 NE2 HIS A 424 4923 3057 2968 603 -293 -568 N
ATOM 3163 N LEU A 425 31.398 13.302 -13.980 1.00 19.28 N
ANISOU 3163 N LEU A 425 3602 1901 1821 261 12 -779 N
ATOM 3164 CA LEU A 425 31.176 12.017 -13.319 1.00 24.45 C
ANISOU 3164 CA LEU A 425 4348 2500 2440 243 97 -784 C
ATOM 3165 C LEU A 425 32.102 11.909 -12.115 1.00 26.30 C
ANISOU 3165 C LEU A 425 4707 2654 2630 343 56 -694 C
ATOM 3166 O LEU A 425 33.326 11.984 -12.262 1.00 26.50 O
ANISOU 3166 O LEU A 425 4753 2662 2654 390 -5 -647 O
ATOM 3167 CB LEU A 425 31.407 10.855 -14.294 1.00 18.72 C
ANISOU 3167 CB LEU A 425 3608 1780 1723 164 163 -824 C
ATOM 3168 CG LEU A 425 31.135 9.441 -13.782 1.00 19.62 C
ANISOU 3168 CG LEU A 425 3827 1829 1797 131 263 -820 C
ATOM 3169 CD1 LEU A 425 29.717 9.334 -13.249 1.00 20.16 C
ANISOU 3169 CD1 LEU A 425 3904 1906 1850 101 323 -857 C
ATOM 3170 CD2 LEU A 425 31.376 8.423 -14.886 1.00 19.81 C
ANISOU 3170 CD2 LEU A 425 3838 1861 1829 51 319 -848 C
ATOM 3171 N ASP A 426 31.521 11.722 -10.929 1.00 25.85 N
ANISOU 3171 N ASP A 426 4736 2555 2533 381 85 -673 N
ATOM 3172 CA ASP A 426 32.260 11.742 -9.670 1.00 25.71 C
ANISOU 3172 CA ASP A 426 4837 2471 2458 489 34 -588 C
ATOM 3173 C ASP A 426 31.902 10.503 -8.863 1.00 22.51 C
ANISOU 3173 C ASP A 426 4550 1998 2004 473 139 -582 C
ATOM 3174 O ASP A 426 30.744 10.331 -8.468 1.00 23.45 O
ANISOU 3174 O ASP A 426 4678 2113 2118 437 209 -616 O
ATOM 3175 CB ASP A 426 31.947 13.015 -8.872 1.00 19.86 C
ANISOU 3175 CB ASP A 426 4094 1748 1705 578 -58 -550 C
ATOM 3176 CG ASP A 426 32.915 13.244 -7.721 1.00 28.75 C
ANISOU 3176 CG ASP A 426 5325 2831 2767 704 -150 -461 C
ATOM 3177 OD1 ASP A 426 33.606 12.291 -7.314 1.00 27.12 O
ANISOU 3177 OD1 ASP A 426 5213 2573 2517 722 -118 -433 O
ATOM 3178 OD2 ASP A 426 32.987 14.386 -7.221 1.00 28.20 O
ANISOU 3178 OD2 ASP A 426 5244 2786 2686 790 -259 -421 O
ATOM 3179 N PHE A 427 32.894 9.645 -8.612 1.00 23.30 N
ANISOU 3179 N PHE A 427 4742 2042 2066 500 151 -539 N
ATOM 3180 CA PHE A 427 32.716 8.469 -7.765 1.00 24.78 C
ANISOU 3180 CA PHE A 427 5066 2153 2197 499 246 -515 C
ATOM 3181 C PHE A 427 33.507 8.544 -6.465 1.00 24.67 C
ANISOU 3181 C PHE A 427 5179 2087 2106 623 184 -431 C
ATOM 3182 O PHE A 427 33.581 7.541 -5.746 1.00 29.21 O
ANISOU 3182 O PHE A 427 5882 2593 2624 635 257 -400 O
ATOM 3183 CB PHE A 427 33.116 7.197 -8.514 1.00 22.10 C
ANISOU 3183 CB PHE A 427 4749 1786 1863 423 329 -535 C
ATOM 3184 CG PHE A 427 32.191 6.833 -9.633 1.00 22.79 C
ANISOU 3184 CG PHE A 427 4741 1916 2002 297 409 -615 C
ATOM 3185 CD1 PHE A 427 30.850 6.592 -9.388 1.00 24.46 C
ANISOU 3185 CD1 PHE A 427 4955 2127 2213 237 494 -654 C
ATOM 3186 CD2 PHE A 427 32.666 6.707 -10.927 1.00 27.06 C
ANISOU 3186 CD2 PHE A 427 5193 2501 2585 240 397 -651 C
ATOM 3187 CE1 PHE A 427 29.996 6.247 -10.416 1.00 29.33 C
ANISOU 3187 CE1 PHE A 427 5486 2791 2866 125 559 -726 C
ATOM 3188 CE2 PHE A 427 31.818 6.362 -11.961 1.00 28.00 C
ANISOU 3188 CE2 PHE A 427 5232 2667 2740 131 461 -719 C
ATOM 3189 CZ PHE A 427 30.482 6.132 -11.705 1.00 27.51 C
ANISOU 3189 CZ PHE A 427 5172 2607 2672 74 539 -756 C
ATOM 3190 N GLN A 428 34.096 9.697 -6.152 1.00 22.68 N
ANISOU 3190 N GLN A 428 4899 1871 1846 717 50 -393 N
ATOM 3191 CA GLN A 428 35.034 9.854 -5.043 1.00 21.76 C
ANISOU 3191 CA GLN A 428 4889 1728 1650 842 -37 -318 C
ATOM 3192 C GLN A 428 34.546 9.175 -3.765 1.00 30.39 C
ANISOU 3192 C GLN A 428 6127 2753 2666 879 35 -283 C
ATOM 3193 O GLN A 428 33.417 9.396 -3.318 1.00 33.93 O
ANISOU 3193 O GLN A 428 6579 3194 3117 861 84 -298 O
ATOM 3194 CB GLN A 428 35.258 11.348 -4.796 1.00 34.91 C
ANISOU 3194 CB GLN A 428 6494 3453 3319 926 -185 -293 C
ATOM 3195 CG GLN A 428 36.200 11.677 -3.662 1.00 44.19 C
ANISOU 3195 CG GLN A 428 7762 4623 4404 1057 -299 -226 C
ATOM 3196 CD GLN A 428 36.548 13.154 -3.606 1.00 41.71 C
ANISOU 3196 CD GLN A 428 7374 4378 4097 1130 -458 -208 C
ATOM 3197 OE1 GLN A 428 35.665 14.014 -3.605 1.00 40.20 O
ANISOU 3197 OE1 GLN A 428 7123 4215 3935 1124 -476 -220 O
ATOM 3198 NE2 GLN A 428 37.840 13.456 -3.565 1.00 42.47 N
ANISOU 3198 NE2 GLN A 428 7446 4507 4182 1184 -563 -195 N
ATOM 3199 N HIS A 429 35.402 8.324 -3.197 1.00 29.36 N
ANISOU 3199 N HIS A 429 6119 2571 2465 930 44 -239 N
ATOM 3200 CA HIS A 429 35.236 7.642 -1.914 1.00 29.13 C
ANISOU 3200 CA HIS A 429 6252 2473 2344 986 99 -191 C
ATOM 3201 C HIS A 429 34.093 6.632 -1.886 1.00 30.23 C
ANISOU 3201 C HIS A 429 6441 2551 2494 890 269 -217 C
ATOM 3202 O HIS A 429 33.846 6.041 -0.829 1.00 38.72 O
ANISOU 3202 O HIS A 429 7657 3561 3495 929 331 -176 O
ATOM 3203 CB HIS A 429 35.054 8.630 -0.749 1.00 24.46 C
ANISOU 3203 CB HIS A 429 5701 1900 1694 1093 8 -149 C
ATOM 3204 CG HIS A 429 36.337 9.212 -0.238 1.00 30.27 C
ANISOU 3204 CG HIS A 429 6467 2672 2363 1214 -147 -105 C
ATOM 3205 ND1 HIS A 429 36.848 10.407 -0.699 1.00 30.29 N
ANISOU 3205 ND1 HIS A 429 6355 2753 2402 1246 -287 -114 N
ATOM 3206 CD2 HIS A 429 37.210 8.764 0.695 1.00 32.44 C
ANISOU 3206 CD2 HIS A 429 6872 2920 2533 1310 -187 -56 C
ATOM 3207 CE1 HIS A 429 37.982 10.668 -0.073 1.00 34.46 C
ANISOU 3207 CE1 HIS A 429 6860 3319 2914 1312 -382 -115 C
ATOM 3208 NE2 HIS A 429 38.224 9.687 0.778 1.00 34.69 N
ANISOU 3208 NE2 HIS A 429 7018 3292 2870 1347 -323 -91 N
ATOM 3209 N SER A 430 33.383 6.418 -2.989 1.00 28.00 N
ANISOU 3209 N SER A 430 6053 2289 2295 767 345 -286 N
ATOM 3210 CA SER A 430 32.477 5.284 -3.047 1.00 25.66 C
ANISOU 3210 CA SER A 430 5812 1937 2003 669 505 -313 C
ATOM 3211 C SER A 430 33.279 4.013 -3.303 1.00 33.60 C
ANISOU 3211 C SER A 430 6904 2886 2978 647 566 -292 C
ATOM 3212 O SER A 430 34.448 4.056 -3.689 1.00 40.94 O
ANISOU 3212 O SER A 430 7817 3836 3903 689 486 -276 O
ATOM 3213 CB SER A 430 31.424 5.477 -4.136 1.00 31.82 C
ANISOU 3213 CB SER A 430 6448 2771 2872 545 557 -399 C
ATOM 3214 OG SER A 430 30.631 6.622 -3.890 1.00 35.23 O
ANISOU 3214 OG SER A 430 6802 3253 3329 566 506 -422 O
ATOM 3215 N THR A 431 32.645 2.865 -3.086 1.00 36.81 N
ANISOU 3215 N THR A 431 7404 3220 3362 579 710 -293 N
ATOM 3216 CA THR A 431 33.290 1.574 -3.331 1.00 36.87 C
ANISOU 3216 CA THR A 431 7503 3167 3338 549 784 -274 C
ATOM 3217 C THR A 431 32.891 1.125 -4.734 1.00 34.12 C
ANISOU 3217 C THR A 431 7046 2850 3068 410 850 -345 C
ATOM 3218 O THR A 431 31.869 0.468 -4.933 1.00 36.34 O
ANISOU 3218 O THR A 431 7338 3103 3368 305 975 -378 O
ATOM 3219 CB THR A 431 32.905 0.550 -2.268 1.00 37.61 C
ANISOU 3219 CB THR A 431 7779 3157 3354 558 905 -225 C
ATOM 3220 OG1 THR A 431 33.232 1.065 -0.972 1.00 44.77 O
ANISOU 3220 OG1 THR A 431 8783 4046 4183 693 834 -161 O
ATOM 3221 CG2 THR A 431 33.648 -0.774 -2.484 1.00 42.64 C
ANISOU 3221 CG2 THR A 431 8522 3728 3952 538 976 -200 C
ATOM 3222 N LEU A 432 33.707 1.503 -5.716 1.00 35.93 N
ANISOU 3222 N LEU A 432 7169 3142 3342 410 764 -368 N
ATOM 3223 CA LEU A 432 33.511 1.069 -7.093 1.00 33.53 C
ANISOU 3223 CA LEU A 432 6765 2872 3102 290 814 -430 C
ATOM 3224 C LEU A 432 33.832 -0.414 -7.226 1.00 35.06 C
ANISOU 3224 C LEU A 432 7071 2989 3260 239 925 -412 C
ATOM 3225 O LEU A 432 34.916 -0.861 -6.833 1.00 41.81 O
ANISOU 3225 O LEU A 432 8021 3802 4063 316 897 -362 O
ATOM 3226 CB LEU A 432 34.393 1.881 -8.045 1.00 33.56 C
ANISOU 3226 CB LEU A 432 6637 2957 3156 314 691 -453 C
ATOM 3227 CG LEU A 432 33.740 3.026 -8.826 1.00 32.04 C
ANISOU 3227 CG LEU A 432 6277 2860 3037 273 633 -513 C
ATOM 3228 CD1 LEU A 432 34.688 3.594 -9.873 1.00 30.54 C
ANISOU 3228 CD1 LEU A 432 5975 2736 2894 283 536 -532 C
ATOM 3229 CD2 LEU A 432 32.457 2.551 -9.479 1.00 32.78 C
ANISOU 3229 CD2 LEU A 432 6321 2968 3166 142 743 -575 C
ATOM 3230 N LYS A 433 32.896 -1.174 -7.790 1.00 27.76 N
ANISOU 3230 N LYS A 433 6136 2049 2363 110 1049 -454 N
ATOM 3231 CA LYS A 433 33.056 -2.610 -7.971 1.00 38.30 C
ANISOU 3231 CA LYS A 433 7577 3307 3668 45 1170 -440 C
ATOM 3232 C LYS A 433 32.926 -2.968 -9.445 1.00 43.00 C
ANISOU 3232 C LYS A 433 8063 3952 4324 -76 1203 -501 C
ATOM 3233 O LYS A 433 31.994 -2.516 -10.121 1.00 40.43 O
ANISOU 3233 O LYS A 433 7617 3690 4054 -160 1214 -560 O
ATOM 3234 CB LYS A 433 32.030 -3.390 -7.144 1.00 38.80 C
ANISOU 3234 CB LYS A 433 7762 3285 3695 -7 1312 -423 C
ATOM 3235 CG LYS A 433 32.648 -4.219 -6.025 1.00 40.36 C
ANISOU 3235 CG LYS A 433 8155 3376 3801 74 1357 -345 C
ATOM 3236 CD LYS A 433 32.174 -3.767 -4.647 1.00 37.32 C
ANISOU 3236 CD LYS A 433 7857 2954 3367 155 1355 -302 C
ATOM 3237 CE LYS A 433 32.859 -4.567 -3.550 1.00 44.63 C
ANISOU 3237 CE LYS A 433 8984 3781 4192 247 1391 -219 C
ATOM 3238 NZ LYS A 433 32.189 -4.410 -2.235 1.00 52.30 N
ANISOU 3238 NZ LYS A 433 10063 4698 5109 300 1432 -178 N
ATOM 3239 N ARG A 434 33.872 -3.774 -9.932 1.00 40.73 N
ANISOU 3239 N ARG A 434 7177 3716 4581 -370 1065 -51 N
ATOM 3240 CA ARG A 434 33.886 -4.348 -11.276 1.00 35.02 C
ANISOU 3240 CA ARG A 434 6377 2923 4006 -453 1100 -141 C
ATOM 3241 C ARG A 434 34.077 -3.312 -12.377 1.00 35.09 C
ANISOU 3241 C ARG A 434 6179 3075 4078 -427 1028 -266 C
ATOM 3242 O ARG A 434 33.725 -3.567 -13.533 1.00 32.66 O
ANISOU 3242 O ARG A 434 5781 2775 3851 -517 1075 -361 O
ATOM 3243 CB ARG A 434 32.617 -5.164 -11.544 1.00 43.37 C
ANISOU 3243 CB ARG A 434 7449 3948 5082 -664 1263 -155 C
ATOM 3244 CG ARG A 434 32.381 -6.234 -10.499 1.00 52.92 C
ANISOU 3244 CG ARG A 434 8875 4999 6234 -720 1354 -8 C
ATOM 3245 CD ARG A 434 31.356 -7.261 -10.932 1.00 71.39 C
ANISOU 3245 CD ARG A 434 11235 7243 8649 -946 1503 -23 C
ATOM 3246 NE ARG A 434 31.356 -8.408 -10.027 1.00 84.30 N
ANISOU 3246 NE ARG A 434 13050 8732 10247 -963 1542 123 N
ATOM 3247 CZ ARG A 434 32.128 -9.480 -10.180 1.00 92.97 C
ANISOU 3247 CZ ARG A 434 14245 9653 11424 -884 1464 154 C
ATOM 3248 NH1 ARG A 434 32.962 -9.560 -11.207 1.00 94.26 N
ANISOU 3248 NH1 ARG A 434 14331 9783 11700 -781 1356 47 N
ATOM 3249 NH2 ARG A 434 32.064 -10.476 -9.307 1.00 97.29 N
ANISOU 3249 NH2 ARG A 434 14962 10070 11935 -903 1494 295 N
ATOM 3250 N VAL A 435 34.647 -2.149 -12.051 1.00 31.60 N
ANISOU 3250 N VAL A 435 5672 2737 3599 -307 907 -267 N
ATOM 3251 CA VAL A 435 34.895 -1.126 -13.061 1.00 24.35 C
ANISOU 3251 CA VAL A 435 4577 1934 2740 -287 837 -358 C
ATOM 3252 C VAL A 435 36.054 -1.502 -13.977 1.00 30.86 C
ANISOU 3252 C VAL A 435 5361 2683 3683 -224 790 -383 C
ATOM 3253 O VAL A 435 36.218 -0.900 -15.046 1.00 24.33 O
ANISOU 3253 O VAL A 435 4397 1942 2908 -235 770 -452 O
ATOM 3254 CB VAL A 435 35.156 0.231 -12.379 1.00 25.78 C
ANISOU 3254 CB VAL A 435 4713 2222 2860 -190 713 -348 C
ATOM 3255 CG1 VAL A 435 36.550 0.263 -11.765 1.00 26.89 C
ANISOU 3255 CG1 VAL A 435 4908 2281 3027 -42 581 -288 C
ATOM 3256 CG2 VAL A 435 34.967 1.375 -13.355 1.00 23.29 C
ANISOU 3256 CG2 VAL A 435 4233 2031 2585 -211 665 -431 C
ATOM 3257 N THR A 436 36.865 -2.483 -13.591 1.00 33.81 N
ANISOU 3257 N THR A 436 5852 2903 4090 -148 776 -327 N
ATOM 3258 CA THR A 436 38.051 -2.855 -14.348 1.00 30.88 C
ANISOU 3258 CA THR A 436 5433 2474 3826 -56 729 -358 C
ATOM 3259 C THR A 436 37.843 -4.119 -15.177 1.00 33.70 C
ANISOU 3259 C THR A 436 5843 2714 4246 -112 826 -413 C
ATOM 3260 O THR A 436 38.792 -4.604 -15.802 1.00 45.00 O
ANISOU 3260 O THR A 436 7245 4094 5758 -20 799 -450 O
ATOM 3261 CB THR A 436 39.247 -3.026 -13.402 1.00 35.63 C
ANISOU 3261 CB THR A 436 6110 2991 4437 109 613 -282 C
ATOM 3262 OG1 THR A 436 40.465 -2.817 -14.123 1.00 40.52 O
ANISOU 3262 OG1 THR A 436 6597 3639 5161 207 543 -324 O
ATOM 3263 CG2 THR A 436 39.259 -4.418 -12.781 1.00 35.89 C
ANISOU 3263 CG2 THR A 436 6351 2830 4458 139 650 -216 C
ATOM 3264 N GLU A 437 36.619 -4.643 -15.222 1.00 25.68 N
ANISOU 3264 N GLU A 437 4878 1679 3199 -259 927 -427 N
ATOM 3265 CA GLU A 437 36.316 -5.875 -15.937 1.00 24.32 C
ANISOU 3265 CA GLU A 437 4719 1436 3087 -322 980 -469 C
ATOM 3266 C GLU A 437 35.735 -5.625 -17.324 1.00 27.47 C
ANISOU 3266 C GLU A 437 4962 1967 3510 -406 1014 -592 C
ATOM 3267 O GLU A 437 35.360 -6.580 -18.011 1.00 27.40 O
ANISOU 3267 O GLU A 437 4956 1910 3546 -464 1046 -650 O
ATOM 3268 CB GLU A 437 35.368 -6.734 -15.101 1.00 28.32 C
ANISOU 3268 CB GLU A 437 5373 1831 3556 -440 1060 -398 C
ATOM 3269 CG GLU A 437 35.904 -7.010 -13.701 1.00 40.65 C
ANISOU 3269 CG GLU A 437 7116 3267 5061 -347 1025 -258 C
ATOM 3270 CD GLU A 437 34.906 -7.728 -12.824 1.00 48.88 C
ANISOU 3270 CD GLU A 437 8308 4220 6044 -480 1128 -164 C
ATOM 3271 OE1 GLU A 437 33.855 -8.144 -13.348 1.00 48.40 O
ANISOU 3271 OE1 GLU A 437 8197 4179 6015 -650 1221 -220 O
ATOM 3272 OE2 GLU A 437 35.169 -7.877 -11.612 1.00 50.59 O
ANISOU 3272 OE2 GLU A 437 8687 4357 6177 -415 1113 -33 O
ATOM 3273 N PHE A 438 35.657 -4.367 -17.744 1.00 22.62 N
ANISOU 3273 N PHE A 438 4221 1511 2864 -405 993 -631 N
ATOM 3274 CA PHE A 438 35.272 -3.977 -19.099 1.00 24.34 C
ANISOU 3274 CA PHE A 438 4294 1870 3084 -450 1002 -732 C
ATOM 3275 C PHE A 438 35.584 -2.492 -19.239 1.00 27.64 C
ANISOU 3275 C PHE A 438 4613 2422 3467 -406 952 -728 C
ATOM 3276 O PHE A 438 36.073 -1.851 -18.302 1.00 26.76 O
ANISOU 3276 O PHE A 438 4540 2287 3340 -346 904 -662 O
ATOM 3277 CB PHE A 438 33.798 -4.281 -19.418 1.00 31.03 C
ANISOU 3277 CB PHE A 438 5111 2768 3912 -603 1063 -790 C
ATOM 3278 CG PHE A 438 32.797 -3.546 -18.547 1.00 33.38 C
ANISOU 3278 CG PHE A 438 5409 3129 4143 -689 1097 -767 C
ATOM 3279 CD1 PHE A 438 32.944 -3.489 -17.169 1.00 32.78 C
ANISOU 3279 CD1 PHE A 438 5462 2963 4030 -673 1113 -676 C
ATOM 3280 CD2 PHE A 438 31.694 -2.926 -19.117 1.00 34.21 C
ANISOU 3280 CD2 PHE A 438 5393 3389 4216 -774 1108 -844 C
ATOM 3281 CE1 PHE A 438 32.027 -2.822 -16.377 1.00 35.71 C
ANISOU 3281 CE1 PHE A 438 5819 3426 4323 -732 1143 -657 C
ATOM 3282 CE2 PHE A 438 30.769 -2.256 -18.327 1.00 36.18 C
ANISOU 3282 CE2 PHE A 438 5634 3711 4403 -839 1143 -848 C
ATOM 3283 CZ PHE A 438 30.938 -2.206 -16.955 1.00 34.54 C
ANISOU 3283 CZ PHE A 438 5536 3438 4150 -816 1164 -751 C
ATOM 3284 N SER A 439 35.321 -1.954 -20.426 1.00 29.58 N
ANISOU 3284 N SER A 439 4741 2802 3696 -429 951 -796 N
ATOM 3285 CA SER A 439 35.481 -0.523 -20.673 1.00 26.76 C
ANISOU 3285 CA SER A 439 4300 2565 3303 -406 905 -791 C
ATOM 3286 C SER A 439 34.242 0.164 -20.125 1.00 22.90 C
ANISOU 3286 C SER A 439 3792 2155 2753 -478 889 -787 C
ATOM 3287 O SER A 439 33.265 0.394 -20.837 1.00 27.08 O
ANISOU 3287 O SER A 439 4243 2796 3251 -536 891 -841 O
ATOM 3288 CB SER A 439 35.671 -0.245 -22.156 1.00 20.95 C
ANISOU 3288 CB SER A 439 3470 1936 2552 -397 917 -853 C
ATOM 3289 OG SER A 439 36.907 -0.763 -22.597 1.00 22.79 O
ANISOU 3289 OG SER A 439 3706 2119 2834 -313 946 -863 O
ATOM 3290 N ALA A 440 34.288 0.490 -18.832 1.00 22.43 N
ANISOU 3290 N ALA A 440 3799 2049 2673 -453 861 -724 N
ATOM 3291 CA ALA A 440 33.095 0.945 -18.129 1.00 26.74 C
ANISOU 3291 CA ALA A 440 4343 2665 3151 -509 870 -734 C
ATOM 3292 C ALA A 440 32.637 2.328 -18.567 1.00 26.01 C
ANISOU 3292 C ALA A 440 4149 2717 3018 -492 798 -767 C
ATOM 3293 O ALA A 440 31.520 2.729 -18.223 1.00 31.41 O
ANISOU 3293 O ALA A 440 4799 3488 3647 -527 804 -804 O
ATOM 3294 CB ALA A 440 33.341 0.947 -16.620 1.00 28.95 C
ANISOU 3294 CB ALA A 440 4719 2883 3397 -458 845 -644 C
ATOM 3295 N PHE A 441 33.463 3.073 -19.304 1.00 23.49 N
ANISOU 3295 N PHE A 441 3774 2424 2726 -436 728 -746 N
ATOM 3296 CA PHE A 441 33.126 4.439 -19.693 1.00 25.59 C
ANISOU 3296 CA PHE A 441 3972 2794 2959 -413 643 -755 C
ATOM 3297 C PHE A 441 33.149 4.632 -21.206 1.00 18.21 C
ANISOU 3297 C PHE A 441 2972 1929 2018 -431 653 -792 C
ATOM 3298 O PHE A 441 33.269 5.769 -21.676 1.00 24.11 O
ANISOU 3298 O PHE A 441 3681 2731 2750 -401 575 -762 O
ATOM 3299 CB PHE A 441 34.076 5.436 -19.023 1.00 27.69 C
ANISOU 3299 CB PHE A 441 4245 3021 3256 -336 529 -670 C
ATOM 3300 CG PHE A 441 34.311 5.169 -17.562 1.00 24.17 C
ANISOU 3300 CG PHE A 441 3878 2503 2803 -293 506 -631 C
ATOM 3301 CD1 PHE A 441 33.376 5.547 -16.610 1.00 24.88 C
ANISOU 3301 CD1 PHE A 441 4000 2637 2817 -279 489 -657 C
ATOM 3302 CD2 PHE A 441 35.472 4.540 -17.139 1.00 21.89 C
ANISOU 3302 CD2 PHE A 441 3631 2116 2572 -250 499 -571 C
ATOM 3303 CE1 PHE A 441 33.594 5.298 -15.261 1.00 22.24 C
ANISOU 3303 CE1 PHE A 441 3754 2250 2446 -228 473 -616 C
ATOM 3304 CE2 PHE A 441 35.696 4.289 -15.795 1.00 22.13 C
ANISOU 3304 CE2 PHE A 441 3750 2082 2575 -195 465 -531 C
ATOM 3305 CZ PHE A 441 34.756 4.669 -14.855 1.00 18.90 C
ANISOU 3305 CZ PHE A 441 3389 1719 2072 -186 455 -548 C
ATOM 3306 N LEU A 442 33.010 3.547 -21.976 1.00 16.44 N
ANISOU 3306 N LEU A 442 2742 1703 1800 -474 736 -847 N
ATOM 3307 CA LEU A 442 33.209 3.618 -23.423 1.00 16.65 C
ANISOU 3307 CA LEU A 442 2724 1802 1801 -470 749 -881 C
ATOM 3308 C LEU A 442 32.229 4.569 -24.102 1.00 19.50 C
ANISOU 3308 C LEU A 442 3028 2289 2093 -470 683 -911 C
ATOM 3309 O LEU A 442 32.572 5.183 -25.119 1.00 26.91 O
ANISOU 3309 O LEU A 442 3958 3288 2978 -450 673 -910 O
ATOM 3310 CB LEU A 442 33.093 2.221 -24.033 1.00 17.41 C
ANISOU 3310 CB LEU A 442 2815 1877 1924 -495 810 -930 C
ATOM 3311 CG LEU A 442 33.465 2.064 -25.508 1.00 18.91 C
ANISOU 3311 CG LEU A 442 2974 2137 2075 -468 832 -973 C
ATOM 3312 CD1 LEU A 442 34.929 2.398 -25.742 1.00 24.86 C
ANISOU 3312 CD1 LEU A 442 3745 2871 2832 -415 883 -938 C
ATOM 3313 CD2 LEU A 442 33.163 0.656 -25.972 1.00 21.12 C
ANISOU 3313 CD2 LEU A 442 3261 2379 2383 -489 866 -1044 C
ATOM 3314 N SER A 443 31.012 4.705 -23.570 1.00 19.36 N
ANISOU 3314 N SER A 443 2974 2316 2064 -486 644 -938 N
ATOM 3315 CA SER A 443 30.022 5.564 -24.213 1.00 20.25 C
ANISOU 3315 CA SER A 443 3031 2547 2117 -462 569 -981 C
ATOM 3316 C SER A 443 30.280 7.048 -23.982 1.00 16.96 C
ANISOU 3316 C SER A 443 2647 2137 1659 -407 484 -950 C
ATOM 3317 O SER A 443 29.752 7.875 -24.734 1.00 21.97 O
ANISOU 3317 O SER A 443 3266 2853 2229 -373 415 -979 O
ATOM 3318 CB SER A 443 28.619 5.230 -23.711 1.00 18.13 C
ANISOU 3318 CB SER A 443 2698 2336 1856 -494 566 -1040 C
ATOM 3319 OG SER A 443 28.311 3.867 -23.931 1.00 25.13 O
ANISOU 3319 OG SER A 443 3567 3198 2785 -575 645 -1086 O
ATOM 3320 N LEU A 444 31.081 7.400 -22.973 1.00 17.00 N
ANISOU 3320 N LEU A 444 2701 2049 1708 -390 466 -881 N
ATOM 3321 CA LEU A 444 31.148 8.770 -22.458 1.00 15.70 C
ANISOU 3321 CA LEU A 444 2551 1868 1546 -324 341 -825 C
ATOM 3322 C LEU A 444 32.176 9.593 -23.237 1.00 19.73 C
ANISOU 3322 C LEU A 444 3072 2343 2081 -310 284 -714 C
ATOM 3323 O LEU A 444 33.217 10.018 -22.727 1.00 25.59 O
ANISOU 3323 O LEU A 444 3831 2997 2896 -302 241 -622 O
ATOM 3324 CB LEU A 444 31.456 8.747 -20.968 1.00 15.45 C
ANISOU 3324 CB LEU A 444 2558 1759 1555 -301 322 -797 C
ATOM 3325 CG LEU A 444 30.370 8.026 -20.165 1.00 18.23 C
ANISOU 3325 CG LEU A 444 2902 2159 1864 -324 394 -885 C
ATOM 3326 CD1 LEU A 444 30.609 8.176 -18.672 1.00 17.46 C
ANISOU 3326 CD1 LEU A 444 2860 2006 1768 -277 366 -853 C
ATOM 3327 CD2 LEU A 444 29.004 8.563 -20.551 1.00 17.51 C
ANISOU 3327 CD2 LEU A 444 2735 2195 1722 -294 349 -963 C
ATOM 3328 N GLU A 445 31.837 9.850 -24.500 1.00 18.73 N
ANISOU 3328 N GLU A 445 2933 2296 1889 -310 282 -724 N
ATOM 3329 CA GLU A 445 32.736 10.570 -25.392 1.00 18.89 C
ANISOU 3329 CA GLU A 445 2966 2302 1910 -312 257 -604 C
ATOM 3330 C GLU A 445 32.678 12.083 -25.216 1.00 23.17 C
ANISOU 3330 C GLU A 445 3548 2790 2465 -271 109 -529 C
ATOM 3331 O GLU A 445 33.438 12.791 -25.884 1.00 25.19 O
ANISOU 3331 O GLU A 445 3823 3015 2733 -292 85 -405 O
ATOM 3332 CB GLU A 445 32.425 10.208 -26.845 1.00 31.26 C
ANISOU 3332 CB GLU A 445 4525 3980 3373 -319 317 -637 C
ATOM 3333 CG GLU A 445 32.427 8.716 -27.128 1.00 49.46 C
ANISOU 3333 CG GLU A 445 6801 6323 5667 -353 446 -734 C
ATOM 3334 CD GLU A 445 32.796 8.397 -28.563 1.00 59.98 C
ANISOU 3334 CD GLU A 445 8135 7744 6912 -351 516 -728 C
ATOM 3335 OE1 GLU A 445 33.998 8.465 -28.892 1.00 64.03 O
ANISOU 3335 OE1 GLU A 445 8638 8240 7449 -360 573 -622 O
ATOM 3336 OE2 GLU A 445 31.890 8.087 -29.363 1.00 62.77 O
ANISOU 3336 OE2 GLU A 445 8489 8195 7167 -337 512 -836 O
ATOM 3337 N LYS A 446 31.804 12.593 -24.350 1.00 21.94 N
ANISOU 3337 N LYS A 446 3409 2621 2307 -213 13 -600 N
ATOM 3338 CA LYS A 446 31.762 14.012 -24.021 1.00 23.67 C
ANISOU 3338 CA LYS A 446 3681 2759 2552 -156 -147 -549 C
ATOM 3339 C LYS A 446 32.166 14.277 -22.579 1.00 16.86 C
ANISOU 3339 C LYS A 446 2836 1795 1774 -134 -212 -553 C
ATOM 3340 O LYS A 446 32.055 15.417 -22.111 1.00 17.31 O
ANISOU 3340 O LYS A 446 2944 1772 1859 -74 -361 -544 O
ATOM 3341 CB LYS A 446 30.367 14.578 -24.289 1.00 24.92 C
ANISOU 3341 CB LYS A 446 3850 2996 2623 -67 -236 -646 C
ATOM 3342 CG LYS A 446 30.035 14.709 -25.761 1.00 34.69 C
ANISOU 3342 CG LYS A 446 5099 4314 3766 -61 -233 -621 C
ATOM 3343 CD LYS A 446 28.559 14.470 -26.019 1.00 42.06 C
ANISOU 3343 CD LYS A 446 5985 5387 4608 7 -256 -779 C
ATOM 3344 CE LYS A 446 28.358 13.415 -27.092 1.00 50.31 C
ANISOU 3344 CE LYS A 446 6985 6554 5577 -44 -143 -830 C
ATOM 3345 NZ LYS A 446 26.916 13.126 -27.301 1.00 48.81 N
ANISOU 3345 NZ LYS A 446 6723 6506 5318 7 -174 -1001 N
ATOM 3346 N LEU A 447 32.627 13.251 -21.866 1.00 16.27 N
ANISOU 3346 N LEU A 447 2733 1716 1734 -170 -116 -573 N
ATOM 3347 CA LEU A 447 32.969 13.394 -20.458 1.00 19.92 C
ANISOU 3347 CA LEU A 447 3221 2099 2247 -134 -179 -586 C
ATOM 3348 C LEU A 447 34.210 14.263 -20.297 1.00 22.49 C
ANISOU 3348 C LEU A 447 3567 2295 2684 -154 -288 -478 C
ATOM 3349 O LEU A 447 35.245 14.004 -20.917 1.00 19.87 O
ANISOU 3349 O LEU A 447 3194 1941 2414 -228 -229 -383 O
ATOM 3350 CB LEU A 447 33.206 12.020 -19.829 1.00 15.64 C
ANISOU 3350 CB LEU A 447 2662 1576 1705 -164 -50 -614 C
ATOM 3351 CG LEU A 447 33.330 11.967 -18.306 1.00 18.27 C
ANISOU 3351 CG LEU A 447 3037 1860 2044 -110 -98 -642 C
ATOM 3352 CD1 LEU A 447 32.014 12.368 -17.668 1.00 21.30 C
ANISOU 3352 CD1 LEU A 447 3439 2317 2338 -35 -133 -747 C
ATOM 3353 CD2 LEU A 447 33.750 10.581 -17.842 1.00 15.42 C
ANISOU 3353 CD2 LEU A 447 2681 1492 1687 -144 27 -633 C
ATOM 3354 N LEU A 448 34.108 15.293 -19.455 1.00 16.95 N
ANISOU 3354 N LEU A 448 2919 1510 2012 -87 -447 -501 N
ATOM 3355 CA LEU A 448 35.213 16.207 -19.184 1.00 17.62 C
ANISOU 3355 CA LEU A 448 3023 1451 2222 -115 -581 -417 C
ATOM 3356 C LEU A 448 35.913 15.928 -17.865 1.00 18.13 C
ANISOU 3356 C LEU A 448 3091 1458 2340 -87 -632 -446 C
ATOM 3357 O LEU A 448 37.108 16.218 -17.732 1.00 20.99 O
ANISOU 3357 O LEU A 448 3424 1727 2825 -142 -696 -372 O
ATOM 3358 CB LEU A 448 34.714 17.655 -19.150 1.00 21.99 C
ANISOU 3358 CB LEU A 448 3654 1914 2787 -52 -764 -431 C
ATOM 3359 CG LEU A 448 33.605 18.071 -20.116 1.00 29.05 C
ANISOU 3359 CG LEU A 448 4576 2872 3589 -10 -767 -450 C
ATOM 3360 CD1 LEU A 448 33.018 19.406 -19.692 1.00 30.10 C
ANISOU 3360 CD1 LEU A 448 4801 2905 3731 101 -971 -504 C
ATOM 3361 CD2 LEU A 448 34.138 18.155 -21.526 1.00 32.33 C
ANISOU 3361 CD2 LEU A 448 4976 3287 4022 -112 -701 -307 C
ATOM 3362 N TYR A 449 35.193 15.384 -16.888 1.00 17.22 N
ANISOU 3362 N TYR A 449 3007 1404 2131 -4 -605 -551 N
ATOM 3363 CA TYR A 449 35.658 15.310 -15.509 1.00 17.48 C
ANISOU 3363 CA TYR A 449 3080 1388 2175 58 -686 -592 C
ATOM 3364 C TYR A 449 35.303 13.941 -14.949 1.00 21.01 C
ANISOU 3364 C TYR A 449 3530 1930 2524 76 -532 -628 C
ATOM 3365 O TYR A 449 34.124 13.574 -14.906 1.00 19.18 O
ANISOU 3365 O TYR A 449 3307 1801 2180 104 -441 -696 O
ATOM 3366 CB TYR A 449 35.013 16.430 -14.688 1.00 18.63 C
ANISOU 3366 CB TYR A 449 3304 1494 2282 175 -857 -688 C
ATOM 3367 CG TYR A 449 35.461 16.540 -13.252 1.00 21.58 C
ANISOU 3367 CG TYR A 449 3716 1838 2647 259 -956 -728 C
ATOM 3368 CD1 TYR A 449 35.013 15.643 -12.292 1.00 21.33 C
ANISOU 3368 CD1 TYR A 449 3710 1908 2489 324 -859 -777 C
ATOM 3369 CD2 TYR A 449 36.300 17.568 -12.845 1.00 19.73 C
ANISOU 3369 CD2 TYR A 449 3482 1490 2523 271 -1138 -700 C
ATOM 3370 CE1 TYR A 449 35.408 15.750 -10.973 1.00 28.45 C
ANISOU 3370 CE1 TYR A 449 4652 2799 3359 414 -948 -799 C
ATOM 3371 CE2 TYR A 449 36.703 17.682 -11.527 1.00 25.79 C
ANISOU 3371 CE2 TYR A 449 4276 2254 3271 360 -1234 -736 C
ATOM 3372 CZ TYR A 449 36.253 16.770 -10.597 1.00 27.37 C
ANISOU 3372 CZ TYR A 449 4515 2557 3328 439 -1142 -787 C
ATOM 3373 OH TYR A 449 36.646 16.877 -9.280 1.00 26.08 O
ANISOU 3373 OH TYR A 449 4398 2389 3123 540 -1246 -822 O
ATOM 3374 N LEU A 450 36.315 13.192 -14.517 1.00 19.90 N
ANISOU 3374 N LEU A 450 3378 1751 2431 58 -507 -580 N
ATOM 3375 CA LEU A 450 36.116 11.893 -13.889 1.00 20.51 C
ANISOU 3375 CA LEU A 450 3488 1880 2425 77 -379 -594 C
ATOM 3376 C LEU A 450 36.932 11.829 -12.608 1.00 21.53 C
ANISOU 3376 C LEU A 450 3674 1946 2559 155 -488 -593 C
ATOM 3377 O LEU A 450 38.137 12.104 -12.619 1.00 19.53 O
ANISOU 3377 O LEU A 450 3379 1613 2427 142 -590 -548 O
ATOM 3378 CB LEU A 450 36.513 10.748 -14.828 1.00 16.31 C
ANISOU 3378 CB LEU A 450 2899 1366 1933 -9 -221 -536 C
ATOM 3379 CG LEU A 450 36.442 9.350 -14.209 1.00 16.36 C
ANISOU 3379 CG LEU A 450 2959 1382 1878 4 -101 -534 C
ATOM 3380 CD1 LEU A 450 35.025 9.022 -13.753 1.00 17.42 C
ANISOU 3380 CD1 LEU A 450 3144 1598 1877 13 -10 -597 C
ATOM 3381 CD2 LEU A 450 36.953 8.300 -15.182 1.00 16.16 C
ANISOU 3381 CD2 LEU A 450 2881 1348 1909 -63 27 -494 C
ATOM 3382 N ASP A 451 36.272 11.478 -11.509 1.00 23.29 N
ANISOU 3382 N ASP A 451 3986 2215 2646 235 -466 -643 N
ATOM 3383 CA ASP A 451 36.927 11.304 -10.218 1.00 27.59 C
ANISOU 3383 CA ASP A 451 4613 2720 3152 331 -563 -645 C
ATOM 3384 C ASP A 451 36.567 9.923 -9.688 1.00 26.15 C
ANISOU 3384 C ASP A 451 4502 2581 2852 339 -400 -611 C
ATOM 3385 O ASP A 451 35.411 9.672 -9.326 1.00 25.86 O
ANISOU 3385 O ASP A 451 4512 2634 2680 348 -292 -646 O
ATOM 3386 CB ASP A 451 36.514 12.398 -9.234 1.00 24.24 C
ANISOU 3386 CB ASP A 451 4260 2304 2648 446 -722 -738 C
ATOM 3387 CG ASP A 451 37.371 12.409 -7.986 1.00 32.47 C
ANISOU 3387 CG ASP A 451 5381 3295 3660 553 -870 -751 C
ATOM 3388 OD1 ASP A 451 38.245 11.527 -7.861 1.00 34.67 O
ANISOU 3388 OD1 ASP A 451 5659 3536 3977 543 -846 -681 O
ATOM 3389 OD2 ASP A 451 37.180 13.298 -7.131 1.00 32.46 O
ANISOU 3389 OD2 ASP A 451 5423 3307 3602 655 -1010 -819 O
ATOM 3390 N ILE A 452 37.555 9.031 -9.655 1.00 23.43 N
ANISOU 3390 N ILE A 452 4164 2172 2566 333 -383 -542 N
ATOM 3391 CA ILE A 452 37.392 7.712 -9.057 1.00 20.87 C
ANISOU 3391 CA ILE A 452 3940 1847 2142 351 -259 -492 C
ATOM 3392 C ILE A 452 38.392 7.574 -7.915 1.00 25.78 C
ANISOU 3392 C ILE A 452 4649 2409 2738 474 -401 -467 C
ATOM 3393 O ILE A 452 38.843 6.467 -7.592 1.00 26.04 O
ANISOU 3393 O ILE A 452 4753 2390 2750 502 -350 -401 O
ATOM 3394 CB ILE A 452 37.588 6.595 -10.095 1.00 20.86 C
ANISOU 3394 CB ILE A 452 3891 1811 2225 254 -108 -440 C
ATOM 3395 CG1 ILE A 452 38.969 6.710 -10.738 1.00 18.75 C
ANISOU 3395 CG1 ILE A 452 3522 1479 2124 255 -197 -414 C
ATOM 3396 CG2 ILE A 452 36.487 6.654 -11.150 1.00 18.03 C
ANISOU 3396 CG2 ILE A 452 3461 1525 1865 143 26 -478 C
ATOM 3397 CD1 ILE A 452 39.458 5.435 -11.364 1.00 24.87 C
ANISOU 3397 CD1 ILE A 452 4284 2204 2959 226 -80 -369 C
ATOM 3398 N SER A 453 38.747 8.698 -7.295 1.00 21.19 N
ANISOU 3398 N SER A 453 4070 1824 2159 556 -597 -527 N
ATOM 3399 CA SER A 453 39.737 8.676 -6.229 1.00 26.80 C
ANISOU 3399 CA SER A 453 4851 2484 2850 682 -769 -525 C
ATOM 3400 C SER A 453 39.200 7.945 -5.007 1.00 29.56 C
ANISOU 3400 C SER A 453 5382 2873 2975 782 -709 -497 C
ATOM 3401 O SER A 453 38.022 8.068 -4.658 1.00 32.94 O
ANISOU 3401 O SER A 453 5875 3391 3250 782 -605 -524 O
ATOM 3402 CB SER A 453 40.146 10.096 -5.843 1.00 32.36 C
ANISOU 3402 CB SER A 453 5520 3166 3608 740 -1006 -615 C
ATOM 3403 OG SER A 453 40.889 10.718 -6.877 1.00 33.77 O
ANISOU 3403 OG SER A 453 5538 3287 4006 642 -1075 -611 O
ATOM 3404 N TYR A 454 40.080 7.178 -4.362 1.00 24.17 N
ANISOU 3404 N TYR A 454 4782 2133 2271 871 -772 -440 N
ATOM 3405 CA TYR A 454 39.772 6.492 -3.106 1.00 27.61 C
ANISOU 3405 CA TYR A 454 5418 2592 2481 983 -742 -391 C
ATOM 3406 C TYR A 454 38.539 5.606 -3.244 1.00 26.15 C
ANISOU 3406 C TYR A 454 5307 2453 2175 888 -473 -321 C
ATOM 3407 O TYR A 454 37.691 5.540 -2.353 1.00 31.48 O
ANISOU 3407 O TYR A 454 6109 3213 2640 932 -397 -310 O
ATOM 3408 CB TYR A 454 39.602 7.491 -1.956 1.00 26.68 C
ANISOU 3408 CB TYR A 454 5385 2542 2209 1122 -908 -481 C
ATOM 3409 CG TYR A 454 40.717 8.504 -1.880 1.00 35.10 C
ANISOU 3409 CG TYR A 454 6361 3554 3423 1187 -1188 -573 C
ATOM 3410 CD1 TYR A 454 41.961 8.157 -1.369 1.00 32.65 C
ANISOU 3410 CD1 TYR A 454 6073 3177 3157 1291 -1361 -554 C
ATOM 3411 CD2 TYR A 454 40.530 9.804 -2.327 1.00 39.71 C
ANISOU 3411 CD2 TYR A 454 6833 4144 4111 1141 -1288 -678 C
ATOM 3412 CE1 TYR A 454 42.991 9.076 -1.309 1.00 30.21 C
ANISOU 3412 CE1 TYR A 454 5654 2821 3003 1330 -1621 -644 C
ATOM 3413 CE2 TYR A 454 41.549 10.732 -2.271 1.00 34.82 C
ANISOU 3413 CE2 TYR A 454 6128 3454 3647 1173 -1543 -755 C
ATOM 3414 CZ TYR A 454 42.778 10.364 -1.758 1.00 32.22 C
ANISOU 3414 CZ TYR A 454 5800 3071 3369 1258 -1707 -741 C
ATOM 3415 OH TYR A 454 43.799 11.287 -1.701 1.00 39.23 O
ANISOU 3415 OH TYR A 454 6580 3894 4433 1271 -1966 -826 O
ATOM 3416 N THR A 455 38.435 4.927 -4.383 1.00 24.40 N
ANISOU 3416 N THR A 455 4998 2184 2088 750 -326 -279 N
ATOM 3417 CA THR A 455 37.385 3.946 -4.612 1.00 31.70 C
ANISOU 3417 CA THR A 455 5981 3125 2941 637 -83 -214 C
ATOM 3418 C THR A 455 37.859 2.517 -4.384 1.00 32.73 C
ANISOU 3418 C THR A 455 6245 3132 3061 649 -15 -95 C
ATOM 3419 O THR A 455 37.097 1.577 -4.637 1.00 38.68 O
ANISOU 3419 O THR A 455 7052 3859 3786 536 180 -33 O
ATOM 3420 CB THR A 455 36.830 4.083 -6.033 1.00 24.09 C
ANISOU 3420 CB THR A 455 4849 2184 2119 479 31 -263 C
ATOM 3421 OG1 THR A 455 37.908 4.005 -6.973 1.00 30.45 O
ANISOU 3421 OG1 THR A 455 5547 2904 3119 464 -43 -266 O
ATOM 3422 CG2 THR A 455 36.115 5.419 -6.199 1.00 22.19 C
ANISOU 3422 CG2 THR A 455 4509 2062 1861 471 -16 -369 C
ATOM 3423 N ASN A 456 39.090 2.336 -3.899 1.00 35.41 N
ANISOU 3423 N ASN A 456 6640 3388 3428 788 -184 -67 N
ATOM 3424 CA ASN A 456 39.698 1.015 -3.739 1.00 39.72 C
ANISOU 3424 CA ASN A 456 7312 3795 3983 833 -158 39 C
ATOM 3425 C ASN A 456 39.649 0.228 -5.046 1.00 36.46 C
ANISOU 3425 C ASN A 456 6810 3303 3742 700 -19 45 C
ATOM 3426 O ASN A 456 39.333 -0.963 -5.071 1.00 35.81 O
ANISOU 3426 O ASN A 456 6854 3118 3635 651 115 129 O
ATOM 3427 CB ASN A 456 39.047 0.241 -2.591 1.00 43.82 C
ANISOU 3427 CB ASN A 456 8076 4300 4272 866 -57 157 C
ATOM 3428 CG ASN A 456 39.179 0.961 -1.266 1.00 59.77 C
ANISOU 3428 CG ASN A 456 10204 6410 6096 1029 -204 145 C
ATOM 3429 OD1 ASN A 456 40.283 1.139 -0.757 1.00 61.20 O
ANISOU 3429 OD1 ASN A 456 10415 6552 6287 1192 -420 131 O
ATOM 3430 ND2 ASN A 456 38.054 1.379 -0.699 1.00 67.45 N
ANISOU 3430 ND2 ASN A 456 11228 7515 6886 994 -95 138 N
ATOM 3431 N THR A 457 39.958 0.914 -6.142 1.00 31.13 N
ANISOU 3431 N THR A 457 5925 2669 3234 642 -54 -47 N
ATOM 3432 CA THR A 457 40.025 0.303 -7.461 1.00 25.63 C
ANISOU 3432 CA THR A 457 5127 1919 2691 539 56 -65 C
ATOM 3433 C THR A 457 41.445 -0.183 -7.716 1.00 27.35 C
ANISOU 3433 C THR A 457 5305 2046 3042 653 -55 -60 C
ATOM 3434 O THR A 457 42.409 0.564 -7.521 1.00 29.57 O
ANISOU 3434 O THR A 457 5487 2363 3387 747 -228 -96 O
ATOM 3435 CB THR A 457 39.602 1.302 -8.541 1.00 25.47 C
ANISOU 3435 CB THR A 457 4911 2008 2759 426 84 -156 C
ATOM 3436 OG1 THR A 457 38.227 1.655 -8.357 1.00 30.07 O
ANISOU 3436 OG1 THR A 457 5519 2681 3225 333 192 -174 O
ATOM 3437 CG2 THR A 457 39.783 0.713 -9.930 1.00 28.47 C
ANISOU 3437 CG2 THR A 457 5188 2352 3280 343 183 -185 C
ATOM 3438 N LYS A 458 41.574 -1.437 -8.130 1.00 27.63 N
ANISOU 3438 N LYS A 458 5412 1961 3125 646 38 -23 N
ATOM 3439 CA LYS A 458 42.858 -2.008 -8.521 1.00 32.26 C
ANISOU 3439 CA LYS A 458 5945 2468 3846 764 -45 -35 C
ATOM 3440 C LYS A 458 42.849 -2.120 -10.041 1.00 28.49 C
ANISOU 3440 C LYS A 458 5302 2017 3507 662 65 -111 C
ATOM 3441 O LYS A 458 42.243 -3.036 -10.603 1.00 30.34 O
ANISOU 3441 O LYS A 458 5607 2173 3747 582 207 -111 O
ATOM 3442 CB LYS A 458 43.089 -3.354 -7.843 1.00 28.06 C
ANISOU 3442 CB LYS A 458 5637 1765 3259 868 -44 54 C
ATOM 3443 CG LYS A 458 44.499 -3.902 -8.012 1.00 38.62 C
ANISOU 3443 CG LYS A 458 6927 3026 4719 1044 -169 33 C
ATOM 3444 CD LYS A 458 44.765 -5.036 -7.031 1.00 41.22 C
ANISOU 3444 CD LYS A 458 7491 3209 4964 1176 -220 135 C
ATOM 3445 CE LYS A 458 46.119 -5.683 -7.273 1.00 46.58 C
ANISOU 3445 CE LYS A 458 8075 3851 5773 1340 -335 98 C
ATOM 3446 NZ LYS A 458 46.414 -6.730 -6.261 1.00 52.72 N
ANISOU 3446 NZ LYS A 458 9043 4528 6459 1456 -403 194 N
ATOM 3447 N ILE A 459 43.511 -1.174 -10.704 1.00 24.35 N
ANISOU 3447 N ILE A 459 4560 1601 3089 660 -3 -174 N
ATOM 3448 CA ILE A 459 43.515 -1.138 -12.161 1.00 27.94 C
ANISOU 3448 CA ILE A 459 4856 2112 3647 569 103 -240 C
ATOM 3449 C ILE A 459 44.249 -2.362 -12.692 1.00 28.44 C
ANISOU 3449 C ILE A 459 4933 2079 3795 660 140 -260 C
ATOM 3450 O ILE A 459 45.416 -2.603 -12.357 1.00 27.21 O
ANISOU 3450 O ILE A 459 4740 1893 3707 813 26 -257 O
ATOM 3451 CB ILE A 459 44.156 0.165 -12.664 1.00 30.05 C
ANISOU 3451 CB ILE A 459 4902 2511 4005 547 21 -276 C
ATOM 3452 CG1 ILE A 459 43.641 1.366 -11.864 1.00 25.98 C
ANISOU 3452 CG1 ILE A 459 4404 2053 3413 510 -73 -263 C
ATOM 3453 CG2 ILE A 459 43.893 0.352 -14.150 1.00 23.91 C
ANISOU 3453 CG2 ILE A 459 3988 1814 3283 433 150 -326 C
ATOM 3454 CD1 ILE A 459 42.273 1.843 -12.265 1.00 35.11 C
ANISOU 3454 CD1 ILE A 459 5580 3269 4489 371 36 -280 C
ATOM 3455 N ASP A 460 43.556 -3.154 -13.520 1.00 31.23 N
ANISOU 3455 N ASP A 460 5337 2382 4147 575 288 -294 N
ATOM 3456 CA ASP A 460 44.120 -4.374 -14.087 1.00 36.06 C
ANISOU 3456 CA ASP A 460 5984 2885 4834 663 329 -335 C
ATOM 3457 C ASP A 460 43.702 -4.545 -15.545 1.00 30.42 C
ANISOU 3457 C ASP A 460 5175 2227 4157 563 465 -429 C
ATOM 3458 O ASP A 460 43.818 -5.647 -16.095 1.00 29.50 O
ANISOU 3458 O ASP A 460 5122 2004 4081 608 522 -484 O
ATOM 3459 CB ASP A 460 43.694 -5.595 -13.256 1.00 41.91 C
ANISOU 3459 CB ASP A 460 6987 3420 5515 698 343 -270 C
ATOM 3460 CG ASP A 460 44.725 -6.711 -13.267 1.00 66.11 C
ANISOU 3460 CG ASP A 460 10106 6353 8660 878 284 -284 C
ATOM 3461 OD1 ASP A 460 45.232 -7.055 -14.354 1.00 71.61 O
ANISOU 3461 OD1 ASP A 460 10695 7063 9450 925 328 -384 O
ATOM 3462 OD2 ASP A 460 45.024 -7.255 -12.183 1.00 76.26 O
ANISOU 3462 OD2 ASP A 460 11522 7551 9904 973 189 -197 O
ATOM 3463 N PHE A 461 43.209 -3.487 -16.181 1.00 25.59 N
ANISOU 3463 N PHE A 461 4426 1771 3524 440 506 -453 N
ATOM 3464 CA PHE A 461 42.761 -3.549 -17.567 1.00 24.91 C
ANISOU 3464 CA PHE A 461 4258 1761 3447 351 623 -540 C
ATOM 3465 C PHE A 461 43.217 -2.281 -18.267 1.00 26.04 C
ANISOU 3465 C PHE A 461 4191 2090 3614 322 608 -546 C
ATOM 3466 O PHE A 461 42.804 -1.182 -17.888 1.00 22.58 O
ANISOU 3466 O PHE A 461 3718 1724 3139 249 560 -499 O
ATOM 3467 CB PHE A 461 41.237 -3.700 -17.645 1.00 24.41 C
ANISOU 3467 CB PHE A 461 4297 1674 3303 192 710 -555 C
ATOM 3468 CG PHE A 461 40.693 -3.739 -19.048 1.00 22.32 C
ANISOU 3468 CG PHE A 461 3955 1494 3032 106 808 -657 C
ATOM 3469 CD1 PHE A 461 41.320 -4.486 -20.036 1.00 23.26 C
ANISOU 3469 CD1 PHE A 461 4039 1597 3200 181 853 -744 C
ATOM 3470 CD2 PHE A 461 39.538 -3.046 -19.373 1.00 21.27 C
ANISOU 3470 CD2 PHE A 461 3789 1461 2832 -32 847 -676 C
ATOM 3471 CE1 PHE A 461 40.810 -4.527 -21.327 1.00 27.39 C
ANISOU 3471 CE1 PHE A 461 4505 2208 3693 115 935 -846 C
ATOM 3472 CE2 PHE A 461 39.024 -3.083 -20.658 1.00 28.08 C
ANISOU 3472 CE2 PHE A 461 4588 2406 3673 -98 918 -773 C
ATOM 3473 CZ PHE A 461 39.661 -3.823 -21.636 1.00 30.08 C
ANISOU 3473 CZ PHE A 461 4819 2647 3964 -26 962 -858 C
ATOM 3474 N ASP A 462 44.074 -2.436 -19.279 1.00 23.05 N
ANISOU 3474 N ASP A 462 3678 1785 3295 384 651 -600 N
ATOM 3475 CA ASP A 462 44.586 -1.282 -20.010 1.00 24.22 C
ANISOU 3475 CA ASP A 462 3627 2106 3468 344 656 -585 C
ATOM 3476 C ASP A 462 43.486 -0.514 -20.734 1.00 29.12 C
ANISOU 3476 C ASP A 462 4238 2820 4005 197 718 -590 C
ATOM 3477 O ASP A 462 43.652 0.682 -20.996 1.00 30.55 O
ANISOU 3477 O ASP A 462 4305 3110 4192 138 690 -540 O
ATOM 3478 CB ASP A 462 45.660 -1.721 -21.008 1.00 26.13 C
ANISOU 3478 CB ASP A 462 3729 2429 3770 441 723 -644 C
ATOM 3479 CG ASP A 462 46.990 -2.024 -20.341 1.00 35.97 C
ANISOU 3479 CG ASP A 462 4901 3645 5122 595 633 -630 C
ATOM 3480 OD1 ASP A 462 47.039 -2.020 -19.095 1.00 36.29 O
ANISOU 3480 OD1 ASP A 462 5031 3581 5177 635 512 -577 O
ATOM 3481 OD2 ASP A 462 47.986 -2.259 -21.061 1.00 37.18 O
ANISOU 3481 OD2 ASP A 462 4900 3892 5336 686 682 -677 O
ATOM 3482 N GLY A 463 42.374 -1.165 -21.061 1.00 23.58 N
ANISOU 3482 N GLY A 463 3654 2072 3234 135 789 -652 N
ATOM 3483 CA GLY A 463 41.267 -0.509 -21.721 1.00 20.64 C
ANISOU 3483 CA GLY A 463 3272 1790 2780 13 831 -672 C
ATOM 3484 C GLY A 463 40.253 0.136 -20.800 1.00 20.97 C
ANISOU 3484 C GLY A 463 3383 1810 2773 -67 773 -628 C
ATOM 3485 O GLY A 463 39.132 0.419 -21.238 1.00 25.40 O
ANISOU 3485 O GLY A 463 3958 2427 3266 -157 807 -667 O
ATOM 3486 N ILE A 464 40.615 0.396 -19.540 1.00 21.48 N
ANISOU 3486 N ILE A 464 3487 1811 2865 -22 681 -557 N
ATOM 3487 CA ILE A 464 39.635 0.878 -18.569 1.00 19.27 C
ANISOU 3487 CA ILE A 464 3287 1514 2520 -75 637 -528 C
ATOM 3488 C ILE A 464 39.086 2.245 -18.961 1.00 19.77 C
ANISOU 3488 C ILE A 464 3270 1696 2547 -141 601 -523 C
ATOM 3489 O ILE A 464 37.943 2.582 -18.627 1.00 21.12 O
ANISOU 3489 O ILE A 464 3486 1892 2647 -197 602 -542 O
ATOM 3490 CB ILE A 464 40.256 0.902 -17.159 1.00 23.56 C
ANISOU 3490 CB ILE A 464 3895 1976 3080 11 533 -460 C
ATOM 3491 CG1 ILE A 464 39.202 1.309 -16.124 1.00 29.50 C
ANISOU 3491 CG1 ILE A 464 4743 2727 3739 -29 507 -439 C
ATOM 3492 CG2 ILE A 464 41.454 1.846 -17.105 1.00 24.63 C
ANISOU 3492 CG2 ILE A 464 3903 2159 3294 70 423 -421 C
ATOM 3493 CD1 ILE A 464 39.697 1.304 -14.696 1.00 24.22 C
ANISOU 3493 CD1 ILE A 464 4166 1989 3048 66 404 -377 C
ATOM 3494 N PHE A 465 39.872 3.044 -19.686 1.00 19.98 N
ANISOU 3494 N PHE A 465 3175 1794 2621 -134 572 -497 N
ATOM 3495 CA PHE A 465 39.504 4.408 -20.045 1.00 19.62 C
ANISOU 3495 CA PHE A 465 3070 1830 2552 -188 518 -471 C
ATOM 3496 C PHE A 465 39.244 4.576 -21.541 1.00 23.93 C
ANISOU 3496 C PHE A 465 3554 2478 3059 -238 599 -496 C
ATOM 3497 O PHE A 465 39.260 5.705 -22.047 1.00 21.52 O
ANISOU 3497 O PHE A 465 3195 2235 2748 -272 557 -450 O
ATOM 3498 CB PHE A 465 40.589 5.380 -19.582 1.00 18.62 C
ANISOU 3498 CB PHE A 465 2869 1693 2513 -160 401 -397 C
ATOM 3499 CG PHE A 465 40.769 5.430 -18.091 1.00 17.40 C
ANISOU 3499 CG PHE A 465 2783 1454 2373 -99 289 -382 C
ATOM 3500 CD1 PHE A 465 39.678 5.383 -17.242 1.00 16.93 C
ANISOU 3500 CD1 PHE A 465 2839 1373 2222 -97 275 -410 C
ATOM 3501 CD2 PHE A 465 42.036 5.533 -17.540 1.00 18.06 C
ANISOU 3501 CD2 PHE A 465 2807 1499 2554 -38 197 -344 C
ATOM 3502 CE1 PHE A 465 39.844 5.438 -15.874 1.00 18.47 C
ANISOU 3502 CE1 PHE A 465 3110 1507 2400 -28 177 -394 C
ATOM 3503 CE2 PHE A 465 42.209 5.586 -16.174 1.00 18.32 C
ANISOU 3503 CE2 PHE A 465 2915 1464 2582 34 78 -338 C
ATOM 3504 CZ PHE A 465 41.111 5.539 -15.339 1.00 19.58 C
ANISOU 3504 CZ PHE A 465 3211 1601 2626 43 70 -360 C
ATOM 3505 N LEU A 466 39.006 3.480 -22.261 1.00 21.61 N
ANISOU 3505 N LEU A 466 3282 2194 2734 -238 706 -569 N
ATOM 3506 CA LEU A 466 38.630 3.579 -23.666 1.00 24.12 C
ANISOU 3506 CA LEU A 466 3562 2620 2984 -272 775 -612 C
ATOM 3507 C LEU A 466 37.381 4.444 -23.814 1.00 24.54 C
ANISOU 3507 C LEU A 466 3635 2730 2958 -329 729 -626 C
ATOM 3508 O LEU A 466 36.429 4.329 -23.037 1.00 21.40 O
ANISOU 3508 O LEU A 466 3295 2296 2539 -351 702 -665 O
ATOM 3509 CB LEU A 466 38.373 2.186 -24.262 1.00 18.21 C
ANISOU 3509 CB LEU A 466 2858 1853 2210 -260 874 -721 C
ATOM 3510 CG LEU A 466 39.480 1.176 -24.616 1.00 33.29 C
ANISOU 3510 CG LEU A 466 4746 3731 4171 -180 940 -751 C
ATOM 3511 CD1 LEU A 466 38.888 -0.194 -24.936 1.00 38.87 C
ANISOU 3511 CD1 LEU A 466 5543 4369 4858 -179 1004 -877 C
ATOM 3512 CD2 LEU A 466 40.324 1.634 -25.791 1.00 37.23 C
ANISOU 3512 CD2 LEU A 466 5133 4366 4646 -151 995 -726 C
ATOM 3513 N GLY A 467 37.395 5.328 -24.815 1.00 19.19 N
ANISOU 3513 N GLY A 467 3189 1775 2326 -507 397 -583 N
ATOM 3514 CA GLY A 467 36.270 6.181 -25.123 1.00 15.30 C
ANISOU 3514 CA GLY A 467 2724 1390 1700 -547 373 -603 C
ATOM 3515 C GLY A 467 36.330 7.567 -24.511 1.00 20.44 C
ANISOU 3515 C GLY A 467 3388 2031 2347 -506 190 -547 C
ATOM 3516 O GLY A 467 35.549 8.440 -24.914 1.00 26.29 O
ANISOU 3516 O GLY A 467 4132 2862 2997 -539 165 -552 O
ATOM 3517 N LEU A 468 37.240 7.799 -23.568 1.00 22.93 N
ANISOU 3517 N LEU A 468 3710 2243 2761 -435 64 -494 N
ATOM 3518 CA LEU A 468 37.289 9.058 -22.824 1.00 14.66 C
ANISOU 3518 CA LEU A 468 2688 1173 1710 -390 -117 -450 C
ATOM 3519 C LEU A 468 38.189 10.075 -23.530 1.00 23.42 C
ANISOU 3519 C LEU A 468 3692 2289 2918 -418 -183 -396 C
ATOM 3520 O LEU A 468 39.158 10.600 -22.980 1.00 24.21 O
ANISOU 3520 O LEU A 468 3765 2313 3120 -377 -308 -342 O
ATOM 3521 CB LEU A 468 37.748 8.797 -21.396 1.00 17.25 C
ANISOU 3521 CB LEU A 468 3078 1395 2080 -302 -224 -425 C
ATOM 3522 CG LEU A 468 36.744 7.969 -20.593 1.00 18.61 C
ANISOU 3522 CG LEU A 468 3361 1567 2143 -270 -179 -469 C
ATOM 3523 CD1 LEU A 468 37.307 7.615 -19.227 1.00 14.85 C
ANISOU 3523 CD1 LEU A 468 2933 991 1716 -181 -275 -437 C
ATOM 3524 CD2 LEU A 468 35.441 8.742 -20.465 1.00 17.52 C
ANISOU 3524 CD2 LEU A 468 3222 1556 1880 -261 -204 -465 C
ATOM 3525 N THR A 469 37.826 10.364 -24.779 1.00 27.19 N
ANISOU 3525 N THR A 469 4108 2866 3357 -493 -95 -408 N
ATOM 3526 CA THR A 469 38.634 11.225 -25.630 1.00 26.05 C
ANISOU 3526 CA THR A 469 3853 2742 3302 -531 -130 -355 C
ATOM 3527 C THR A 469 38.418 12.709 -25.350 1.00 24.48 C
ANISOU 3527 C THR A 469 3666 2548 3087 -519 -282 -314 C
ATOM 3528 O THR A 469 39.234 13.533 -25.777 1.00 30.88 O
ANISOU 3528 O THR A 469 4394 3347 3993 -537 -348 -257 O
ATOM 3529 CB THR A 469 38.332 10.908 -27.096 1.00 26.60 C
ANISOU 3529 CB THR A 469 3849 2925 3335 -616 29 -384 C
ATOM 3530 OG1 THR A 469 36.989 11.301 -27.397 1.00 38.58 O
ANISOU 3530 OG1 THR A 469 5412 4545 4703 -650 59 -418 O
ATOM 3531 CG2 THR A 469 38.465 9.405 -27.352 1.00 24.67 C
ANISOU 3531 CG2 THR A 469 3602 2669 3101 -629 186 -438 C
ATOM 3532 N SER A 470 37.357 13.066 -24.633 1.00 21.99 N
ANISOU 3532 N SER A 470 3452 2247 2657 -488 -338 -340 N
ATOM 3533 CA SER A 470 37.114 14.446 -24.239 1.00 21.34 C
ANISOU 3533 CA SER A 470 3393 2156 2558 -466 -484 -307 C
ATOM 3534 C SER A 470 37.553 14.727 -22.807 1.00 25.78 C
ANISOU 3534 C SER A 470 4023 2607 3166 -386 -642 -293 C
ATOM 3535 O SER A 470 37.399 15.857 -22.331 1.00 23.45 O
ANISOU 3535 O SER A 470 3753 2293 2864 -357 -769 -270 O
ATOM 3536 CB SER A 470 35.629 14.783 -24.405 1.00 26.79 C
ANISOU 3536 CB SER A 470 4147 2943 3089 -481 -449 -344 C
ATOM 3537 OG SER A 470 35.419 16.179 -24.520 1.00 32.18 O
ANISOU 3537 OG SER A 470 4820 3641 3767 -481 -553 -306 O
ATOM 3538 N LEU A 471 38.107 13.732 -22.120 1.00 17.94 N
ANISOU 3538 N LEU A 471 3051 1545 2219 -345 -629 -302 N
ATOM 3539 CA LEU A 471 38.427 13.868 -20.707 1.00 14.73 C
ANISOU 3539 CA LEU A 471 2714 1048 1836 -267 -769 -292 C
ATOM 3540 C LEU A 471 39.578 14.847 -20.499 1.00 20.58 C
ANISOU 3540 C LEU A 471 3394 1720 2707 -256 -916 -234 C
ATOM 3541 O LEU A 471 40.655 14.690 -21.085 1.00 19.05 O
ANISOU 3541 O LEU A 471 3101 1504 2634 -284 -892 -194 O
ATOM 3542 CB LEU A 471 38.779 12.499 -20.131 1.00 14.97 C
ANISOU 3542 CB LEU A 471 2769 1028 1889 -229 -705 -307 C
ATOM 3543 CG LEU A 471 38.836 12.378 -18.609 1.00 20.45 C
ANISOU 3543 CG LEU A 471 3530 1674 2567 -139 -807 -295 C
ATOM 3544 CD1 LEU A 471 37.508 12.771 -17.984 1.00 18.46 C
ANISOU 3544 CD1 LEU A 471 3328 1514 2171 -98 -804 -301 C
ATOM 3545 CD2 LEU A 471 39.199 10.962 -18.224 1.00 15.44 C
ANISOU 3545 CD2 LEU A 471 2924 976 1966 -113 -735 -309 C
ATOM 3546 N ASN A 472 39.345 15.860 -19.661 1.00 17.98 N
ANISOU 3546 N ASN A 472 3088 1400 2345 -198 -1027 -208 N
ATOM 3547 CA ASN A 472 40.364 16.833 -19.286 1.00 19.44 C
ANISOU 3547 CA ASN A 472 3224 1525 2637 -178 -1170 -155 C
ATOM 3548 C ASN A 472 40.882 16.648 -17.870 1.00 19.84 C
ANISOU 3548 C ASN A 472 3312 1520 2707 -99 -1273 -143 C
ATOM 3549 O ASN A 472 42.069 16.878 -17.624 1.00 18.27 O
ANISOU 3549 O ASN A 472 3059 1256 2625 -95 -1369 -107 O
ATOM 3550 CB ASN A 472 39.816 18.261 -19.425 1.00 19.67 C
ANISOU 3550 CB ASN A 472 3250 1594 2630 -173 -1221 -129 C
ATOM 3551 CG ASN A 472 39.322 18.556 -20.824 1.00 20.51 C
ANISOU 3551 CG ASN A 472 3314 1764 2715 -254 -1136 -134 C
ATOM 3552 OD1 ASN A 472 38.242 19.116 -21.017 1.00 22.23 O
ANISOU 3552 OD1 ASN A 472 3562 2048 2838 -249 -1099 -141 O
ATOM 3553 ND2 ASN A 472 40.112 18.167 -21.814 1.00 19.42 N
ANISOU 3553 ND2 ASN A 472 3099 1608 2673 -330 -1097 -124 N
ATOM 3554 N THR A 473 40.023 16.229 -16.943 1.00 22.24 N
ANISOU 3554 N THR A 473 3697 1852 2899 -38 -1255 -167 N
ATOM 3555 CA THR A 473 40.371 16.093 -15.535 1.00 25.67 C
ANISOU 3555 CA THR A 473 4174 2245 3333 38 -1358 -156 C
ATOM 3556 C THR A 473 40.151 14.650 -15.106 1.00 22.75 C
ANISOU 3556 C THR A 473 3853 1872 2919 60 -1281 -187 C
ATOM 3557 O THR A 473 39.024 14.142 -15.171 1.00 23.64 O
ANISOU 3557 O THR A 473 4013 2044 2923 62 -1173 -214 O
ATOM 3558 CB THR A 473 39.542 17.044 -14.672 1.00 28.81 C
ANISOU 3558 CB THR A 473 4626 2661 3660 102 -1403 -140 C
ATOM 3559 OG1 THR A 473 39.735 18.388 -15.128 1.00 31.27 O
ANISOU 3559 OG1 THR A 473 4898 2957 4026 82 -1452 -113 O
ATOM 3560 CG2 THR A 473 39.970 16.948 -13.219 1.00 20.49 C
ANISOU 3560 CG2 THR A 473 3617 1548 2620 179 -1505 -129 C
ATOM 3561 N LEU A 474 41.224 13.994 -14.668 1.00 19.02 N
ANISOU 3561 N LEU A 474 3361 1329 2537 76 -1326 -175 N
ATOM 3562 CA LEU A 474 41.154 12.629 -14.162 1.00 16.97 C
ANISOU 3562 CA LEU A 474 3145 1047 2256 109 -1253 -190 C
ATOM 3563 C LEU A 474 41.755 12.604 -12.763 1.00 24.11 C
ANISOU 3563 C LEU A 474 4070 1917 3174 177 -1384 -171 C
ATOM 3564 O LEU A 474 42.972 12.750 -12.599 1.00 19.39 O
ANISOU 3564 O LEU A 474 3407 1266 2692 179 -1461 -137 O
ATOM 3565 CB LEU A 474 41.877 11.657 -15.090 1.00 18.14 C
ANISOU 3565 CB LEU A 474 3239 1140 2515 70 -1138 -181 C
ATOM 3566 CG LEU A 474 41.802 10.186 -14.673 1.00 25.15 C
ANISOU 3566 CG LEU A 474 4167 1996 3391 108 -1039 -189 C
ATOM 3567 CD1 LEU A 474 40.384 9.812 -14.291 1.00 21.91 C
ANISOU 3567 CD1 LEU A 474 3847 1656 2823 122 -971 -233 C
ATOM 3568 CD2 LEU A 474 42.302 9.283 -15.787 1.00 21.82 C
ANISOU 3568 CD2 LEU A 474 3685 1542 3061 64 -893 -186 C
ATOM 3569 N LYS A 475 40.901 12.423 -11.760 1.00 21.59 N
ANISOU 3569 N LYS A 475 3833 1637 2733 229 -1405 -191 N
ATOM 3570 CA LYS A 475 41.323 12.247 -10.377 1.00 25.74 C
ANISOU 3570 CA LYS A 475 4390 2143 3246 285 -1515 -193 C
ATOM 3571 C LYS A 475 41.141 10.781 -10.004 1.00 28.05 C
ANISOU 3571 C LYS A 475 4720 2420 3517 319 -1407 -189 C
ATOM 3572 O LYS A 475 40.009 10.286 -9.952 1.00 32.48 O
ANISOU 3572 O LYS A 475 5349 3024 3969 330 -1324 -210 O
ATOM 3573 CB LYS A 475 40.519 13.152 -9.443 1.00 19.73 C
ANISOU 3573 CB LYS A 475 3661 1434 2401 315 -1540 -208 C
ATOM 3574 CG LYS A 475 40.685 14.634 -9.735 1.00 19.18 C
ANISOU 3574 CG LYS A 475 3541 1344 2403 298 -1556 -186 C
ATOM 3575 CD LYS A 475 39.776 15.481 -8.863 1.00 21.55 C
ANISOU 3575 CD LYS A 475 3876 1650 2663 327 -1514 -209 C
ATOM 3576 CE LYS A 475 40.059 16.954 -9.087 1.00 19.93 C
ANISOU 3576 CE LYS A 475 3630 1425 2517 304 -1556 -202 C
ATOM 3577 NZ LYS A 475 39.142 17.839 -8.325 1.00 30.24 N
ANISOU 3577 NZ LYS A 475 4965 2746 3779 336 -1527 -219 N
ATOM 3578 N MET A 476 42.255 10.088 -9.747 1.00 26.23 N
ANISOU 3578 N MET A 476 4437 2135 3395 340 -1404 -150 N
ATOM 3579 CA MET A 476 42.219 8.671 -9.402 1.00 35.32 C
ANISOU 3579 CA MET A 476 5612 3263 4546 380 -1299 -130 C
ATOM 3580 C MET A 476 43.214 8.350 -8.289 1.00 33.14 C
ANISOU 3580 C MET A 476 5303 2963 4326 432 -1376 -87 C
ATOM 3581 O MET A 476 43.806 7.264 -8.269 1.00 25.60 O
ANISOU 3581 O MET A 476 4317 1967 3444 461 -1299 -41 O
ATOM 3582 CB MET A 476 42.481 7.804 -10.633 1.00 32.89 C
ANISOU 3582 CB MET A 476 5262 2910 4327 344 -1143 -116 C
ATOM 3583 CG MET A 476 43.705 8.212 -11.426 1.00 29.96 C
ANISOU 3583 CG MET A 476 4787 2494 4103 312 -1169 -80 C
ATOM 3584 SD MET A 476 43.854 7.275 -12.958 1.00 30.57 S
ANISOU 3584 SD MET A 476 4824 2522 4269 260 -979 -85 S
ATOM 3585 CE MET A 476 43.824 5.598 -12.332 1.00 22.15 C
ANISOU 3585 CE MET A 476 3797 1415 3206 321 -863 -68 C
ATOM 3586 N ALA A 477 43.395 9.276 -7.352 1.00 32.51 N
ANISOU 3586 N ALA A 477 5230 2910 4213 441 -1517 -109 N
ATOM 3587 CA ALA A 477 44.306 9.060 -6.241 1.00 27.73 C
ANISOU 3587 CA ALA A 477 4593 2294 3651 481 -1585 -76 C
ATOM 3588 C ALA A 477 43.764 7.989 -5.298 1.00 23.94 C
ANISOU 3588 C ALA A 477 4173 1830 3094 540 -1530 -67 C
ATOM 3589 O ALA A 477 42.572 7.671 -5.288 1.00 24.97 O
ANISOU 3589 O ALA A 477 4383 1987 3116 546 -1469 -102 O
ATOM 3590 CB ALA A 477 44.532 10.363 -5.478 1.00 25.26 C
ANISOU 3590 CB ALA A 477 4282 1992 3323 462 -1723 -122 C
ATOM 3591 N GLY A 478 44.664 7.428 -4.496 1.00 24.82 N
ANISOU 3591 N GLY A 478 4242 1929 3262 584 -1551 -13 N
ATOM 3592 CA GLY A 478 44.265 6.472 -3.483 1.00 31.59 C
ANISOU 3592 CA GLY A 478 5145 2803 4053 642 -1511 6 C
ATOM 3593 C GLY A 478 43.898 5.094 -3.982 1.00 35.20 C
ANISOU 3593 C GLY A 478 5622 3229 4524 666 -1361 44 C
ATOM 3594 O GLY A 478 43.345 4.301 -3.212 1.00 41.41 O
ANISOU 3594 O GLY A 478 6461 4031 5245 709 -1318 56 O
ATOM 3595 N ASN A 479 44.188 4.776 -5.242 1.00 32.57 N
ANISOU 3595 N ASN A 479 5250 2846 4281 635 -1270 59 N
ATOM 3596 CA ASN A 479 43.908 3.451 -5.779 1.00 25.07 C
ANISOU 3596 CA ASN A 479 4316 1848 3361 647 -1107 82 C
ATOM 3597 C ASN A 479 45.195 2.639 -5.880 1.00 29.74 C
ANISOU 3597 C ASN A 479 4824 2378 4099 681 -1060 159 C
ATOM 3598 O ASN A 479 46.135 2.869 -5.111 1.00 32.09 O
ANISOU 3598 O ASN A 479 5067 2687 4439 715 -1157 206 O
ATOM 3599 CB ASN A 479 43.216 3.572 -7.137 1.00 22.89 C
ANISOU 3599 CB ASN A 479 4062 1559 3076 583 -1010 30 C
ATOM 3600 CG ASN A 479 41.880 4.297 -7.047 1.00 29.10 C
ANISOU 3600 CG ASN A 479 4933 2411 3711 556 -1044 -39 C
ATOM 3601 OD1 ASN A 479 40.980 3.876 -6.318 1.00 27.87 O
ANISOU 3601 OD1 ASN A 479 4854 2288 3448 584 -1027 -53 O
ATOM 3602 ND2 ASN A 479 41.755 5.403 -7.773 1.00 27.51 N
ANISOU 3602 ND2 ASN A 479 4717 2233 3502 504 -1095 -77 N
ATOM 3603 N SER A 480 45.250 1.687 -6.808 1.00 27.88 N
ANISOU 3603 N SER A 480 4575 2078 3939 670 -909 169 N
ATOM 3604 CA SER A 480 46.458 0.898 -7.017 1.00 28.02 C
ANISOU 3604 CA SER A 480 4514 2031 4103 704 -851 239 C
ATOM 3605 C SER A 480 46.374 0.224 -8.381 1.00 28.79 C
ANISOU 3605 C SER A 480 4602 2062 4276 664 -688 214 C
ATOM 3606 O SER A 480 45.333 0.240 -9.043 1.00 25.03 O
ANISOU 3606 O SER A 480 4186 1595 3729 611 -612 144 O
ATOM 3607 CB SER A 480 46.659 -0.132 -5.899 1.00 34.96 C
ANISOU 3607 CB SER A 480 5401 2899 4984 781 -827 305 C
ATOM 3608 OG SER A 480 45.560 -1.022 -5.816 1.00 33.41 O
ANISOU 3608 OG SER A 480 5285 2690 4720 783 -712 281 O
ATOM 3609 N PHE A 481 47.493 -0.374 -8.789 1.00 29.69 N
ANISOU 3609 N PHE A 481 4638 2112 4530 688 -631 267 N
ATOM 3610 CA PHE A 481 47.626 -1.020 -10.087 1.00 26.92 C
ANISOU 3610 CA PHE A 481 4265 1693 4272 652 -479 242 C
ATOM 3611 C PHE A 481 48.170 -2.432 -9.907 1.00 27.46 C
ANISOU 3611 C PHE A 481 4315 1685 4432 713 -356 298 C
ATOM 3612 O PHE A 481 48.839 -2.742 -8.918 1.00 25.43 O
ANISOU 3612 O PHE A 481 4030 1430 4200 785 -410 376 O
ATOM 3613 CB PHE A 481 48.548 -0.215 -11.018 1.00 23.85 C
ANISOU 3613 CB PHE A 481 3781 1297 3982 611 -528 247 C
ATOM 3614 CG PHE A 481 47.917 1.025 -11.582 1.00 26.74 C
ANISOU 3614 CG PHE A 481 4166 1717 4276 537 -600 183 C
ATOM 3615 CD1 PHE A 481 47.737 2.149 -10.799 1.00 23.30 C
ANISOU 3615 CD1 PHE A 481 3748 1351 3755 538 -763 182 C
ATOM 3616 CD2 PHE A 481 47.525 1.071 -12.911 1.00 27.27 C
ANISOU 3616 CD2 PHE A 481 4219 1794 4349 458 -486 121 C
ATOM 3617 CE1 PHE A 481 47.164 3.287 -11.320 1.00 25.60 C
ANISOU 3617 CE1 PHE A 481 4055 1686 3984 474 -823 128 C
ATOM 3618 CE2 PHE A 481 46.951 2.204 -13.435 1.00 22.74 C
ANISOU 3618 CE2 PHE A 481 3654 1284 3703 390 -541 71 C
ATOM 3619 CZ PHE A 481 46.772 3.313 -12.641 1.00 25.30 C
ANISOU 3619 CZ PHE A 481 4014 1636 3964 405 -720 77 C
ATOM 3620 N LYS A 482 47.871 -3.290 -10.883 1.00 28.89 N
ANISOU 3620 N LYS A 482 4513 1801 4661 683 -187 255 N
ATOM 3621 CA LYS A 482 48.415 -4.642 -10.877 1.00 25.45 C
ANISOU 3621 CA LYS A 482 4065 1295 4309 733 -65 294 C
ATOM 3622 C LYS A 482 49.938 -4.595 -10.921 1.00 38.13 C
ANISOU 3622 C LYS A 482 5554 2893 6040 774 -108 370 C
ATOM 3623 O LYS A 482 50.527 -3.855 -11.717 1.00 35.49 O
ANISOU 3623 O LYS A 482 5136 2573 5775 731 -139 363 O
ATOM 3624 CB LYS A 482 47.885 -5.441 -12.065 1.00 28.08 C
ANISOU 3624 CB LYS A 482 4393 1624 4653 657 121 212 C
ATOM 3625 CG LYS A 482 48.533 -6.808 -12.187 1.00 35.69 C
ANISOU 3625 CG LYS A 482 5311 2548 5702 689 242 241 C
ATOM 3626 CD LYS A 482 48.156 -7.487 -13.481 1.00 48.15 C
ANISOU 3626 CD LYS A 482 6872 4131 7291 611 428 159 C
ATOM 3627 CE LYS A 482 48.743 -8.881 -13.559 1.00 56.93 C
ANISOU 3627 CE LYS A 482 7946 5198 8487 646 552 185 C
ATOM 3628 NZ LYS A 482 48.120 -9.676 -14.653 1.00 58.62 N
ANISOU 3628 NZ LYS A 482 8164 5423 8684 568 734 96 N
ATOM 3629 N ASP A 483 50.574 -5.379 -10.049 1.00 31.03 N
ANISOU 3629 N ASP A 483 4646 1974 5169 856 -116 446 N
ATOM 3630 CA ASP A 483 52.028 -5.433 -9.919 1.00 29.83 C
ANISOU 3630 CA ASP A 483 4386 1821 5127 905 -160 526 C
ATOM 3631 C ASP A 483 52.627 -4.074 -9.576 1.00 32.80 C
ANISOU 3631 C ASP A 483 4699 2259 5504 900 -336 560 C
ATOM 3632 O ASP A 483 53.839 -3.872 -9.717 1.00 35.53 O
ANISOU 3632 O ASP A 483 4940 2611 5947 917 -383 614 O
ATOM 3633 CB ASP A 483 52.678 -5.993 -11.187 1.00 35.88 C
ANISOU 3633 CB ASP A 483 5065 2549 6017 872 -23 507 C
ATOM 3634 CG ASP A 483 52.221 -7.401 -11.496 1.00 45.82 C
ANISOU 3634 CG ASP A 483 6362 3766 7281 868 151 472 C
ATOM 3635 OD1 ASP A 483 52.157 -8.219 -10.555 1.00 42.99 O
ANISOU 3635 OD1 ASP A 483 6045 3390 6898 928 149 514 O
ATOM 3636 OD2 ASP A 483 51.919 -7.685 -12.673 1.00 47.28 O
ANISOU 3636 OD2 ASP A 483 6531 3942 7491 801 289 400 O
ATOM 3637 N ASN A 484 51.788 -3.141 -9.118 1.00 35.17 N
ANISOU 3637 N ASN A 484 5057 2614 5693 868 -440 523 N
ATOM 3638 CA ASN A 484 52.204 -1.781 -8.776 1.00 34.77 C
ANISOU 3638 CA ASN A 484 4958 2634 5619 845 -621 531 C
ATOM 3639 C ASN A 484 52.918 -1.094 -9.937 1.00 31.01 C
ANISOU 3639 C ASN A 484 4389 2151 5242 788 -637 519 C
ATOM 3640 O ASN A 484 53.813 -0.271 -9.734 1.00 32.69 O
ANISOU 3640 O ASN A 484 4524 2402 5496 784 -766 557 O
ATOM 3641 CB ASN A 484 53.073 -1.775 -7.516 1.00 35.03 C
ANISOU 3641 CB ASN A 484 4950 2706 5654 916 -730 614 C
ATOM 3642 CG ASN A 484 52.324 -2.283 -6.299 1.00 35.77 C
ANISOU 3642 CG ASN A 484 5126 2822 5643 967 -732 630 C
ATOM 3643 OD1 ASN A 484 51.164 -1.930 -6.082 1.00 30.41 O
ANISOU 3643 OD1 ASN A 484 4527 2174 4854 934 -750 571 O
ATOM 3644 ND2 ASN A 484 52.974 -3.135 -5.511 1.00 32.01 N
ANISOU 3644 ND2 ASN A 484 4628 2335 5200 1048 -710 711 N
ATOM 3645 N THR A 485 52.525 -1.424 -11.161 1.00 35.42 N
ANISOU 3645 N THR A 485 4949 2665 5844 737 -504 465 N
ATOM 3646 CA THR A 485 53.088 -0.828 -12.362 1.00 34.55 C
ANISOU 3646 CA THR A 485 4746 2549 5831 676 -496 452 C
ATOM 3647 C THR A 485 52.024 0.030 -13.023 1.00 34.56 C
ANISOU 3647 C THR A 485 4802 2581 5749 592 -510 367 C
ATOM 3648 O THR A 485 50.914 -0.445 -13.279 1.00 35.37 O
ANISOU 3648 O THR A 485 4989 2687 5764 564 -399 299 O
ATOM 3649 CB THR A 485 53.570 -1.899 -13.341 1.00 35.39 C
ANISOU 3649 CB THR A 485 4793 2597 6058 679 -311 456 C
ATOM 3650 OG1 THR A 485 54.639 -2.651 -12.755 1.00 37.49 O
ANISOU 3650 OG1 THR A 485 5003 2845 6398 758 -305 539 O
ATOM 3651 CG2 THR A 485 54.044 -1.262 -14.642 1.00 26.89 C
ANISOU 3651 CG2 THR A 485 3619 1545 5054 605 -284 433 C
ATOM 3652 N LEU A 486 52.358 1.289 -13.287 1.00 31.34 N
ANISOU 3652 N LEU A 486 4343 2219 5347 546 -635 367 N
ATOM 3653 CA LEU A 486 51.467 2.171 -14.031 1.00 25.70 C
ANISOU 3653 CA LEU A 486 3660 1561 4543 458 -635 290 C
ATOM 3654 C LEU A 486 51.426 1.714 -15.483 1.00 24.11 C
ANISOU 3654 C LEU A 486 3408 1371 4383 394 -455 247 C
ATOM 3655 O LEU A 486 52.423 1.824 -16.202 1.00 28.97 O
ANISOU 3655 O LEU A 486 3911 1986 5109 376 -435 281 O
ATOM 3656 CB LEU A 486 51.939 3.617 -13.916 1.00 24.24 C
ANISOU 3656 CB LEU A 486 3428 1412 4371 429 -817 312 C
ATOM 3657 CG LEU A 486 51.150 4.681 -14.689 1.00 27.13 C
ANISOU 3657 CG LEU A 486 3814 1835 4659 342 -834 247 C
ATOM 3658 CD1 LEU A 486 49.676 4.649 -14.314 1.00 23.32 C
ANISOU 3658 CD1 LEU A 486 3462 1376 4021 336 -813 177 C
ATOM 3659 CD2 LEU A 486 51.731 6.066 -14.443 1.00 23.51 C
ANISOU 3659 CD2 LEU A 486 3307 1394 4230 322 -1021 278 C
ATOM 3660 N SER A 487 50.277 1.208 -15.922 1.00 23.48 N
ANISOU 3660 N SER A 487 3405 1305 4210 356 -325 171 N
ATOM 3661 CA SER A 487 50.143 0.613 -17.241 1.00 30.52 C
ANISOU 3661 CA SER A 487 4259 2210 5128 297 -140 119 C
ATOM 3662 C SER A 487 49.618 1.631 -18.255 1.00 29.35 C
ANISOU 3662 C SER A 487 4090 2142 4918 202 -144 66 C
ATOM 3663 O SER A 487 49.351 2.793 -17.941 1.00 28.63 O
ANISOU 3663 O SER A 487 4018 2089 4770 184 -288 69 O
ATOM 3664 CB SER A 487 49.244 -0.626 -17.177 1.00 34.78 C
ANISOU 3664 CB SER A 487 4887 2717 5610 307 16 67 C
ATOM 3665 OG SER A 487 48.077 -0.385 -16.413 1.00 34.00 O
ANISOU 3665 OG SER A 487 4904 2640 5374 310 -42 34 O
ATOM 3666 N ASN A 488 49.471 1.170 -19.499 1.00 23.28 N
ANISOU 3666 N ASN A 488 3282 1400 4162 142 19 15 N
ATOM 3667 CA ASN A 488 49.147 2.035 -20.636 1.00 23.76 C
ANISOU 3667 CA ASN A 488 3299 1544 4183 51 36 -25 C
ATOM 3668 C ASN A 488 47.633 2.247 -20.721 1.00 26.80 C
ANISOU 3668 C ASN A 488 3786 1985 4410 3 65 -103 C
ATOM 3669 O ASN A 488 46.945 1.778 -21.630 1.00 27.60 O
ANISOU 3669 O ASN A 488 3898 2129 4458 -57 213 -172 O
ATOM 3670 CB ASN A 488 49.707 1.434 -21.920 1.00 35.78 C
ANISOU 3670 CB ASN A 488 4727 3081 5787 11 197 -44 C
ATOM 3671 CG ASN A 488 49.442 2.295 -23.135 1.00 45.37 C
ANISOU 3671 CG ASN A 488 5884 4390 6963 -81 219 -76 C
ATOM 3672 OD1 ASN A 488 49.060 1.798 -24.196 1.00 48.59 O
ANISOU 3672 OD1 ASN A 488 6274 4843 7346 -138 376 -139 O
ATOM 3673 ND2 ASN A 488 49.636 3.595 -22.986 1.00 47.01 N
ANISOU 3673 ND2 ASN A 488 6063 4631 7167 -98 63 -35 N
ATOM 3674 N VAL A 489 47.112 2.990 -19.738 1.00 20.64 N
ANISOU 3674 N VAL A 489 3082 1210 3553 29 -83 -91 N
ATOM 3675 CA VAL A 489 45.674 3.255 -19.673 1.00 23.15 C
ANISOU 3675 CA VAL A 489 3498 1580 3716 -7 -72 -156 C
ATOM 3676 C VAL A 489 45.280 4.611 -20.241 1.00 26.45 C
ANISOU 3676 C VAL A 489 3896 2077 4077 -69 -151 -169 C
ATOM 3677 O VAL A 489 44.079 4.920 -20.301 1.00 29.67 O
ANISOU 3677 O VAL A 489 4376 2541 4355 -102 -140 -221 O
ATOM 3678 CB VAL A 489 45.155 3.170 -18.223 1.00 19.68 C
ANISOU 3678 CB VAL A 489 3167 1104 3206 64 -172 -145 C
ATOM 3679 CG1 VAL A 489 45.269 1.751 -17.691 1.00 25.34 C
ANISOU 3679 CG1 VAL A 489 3920 1751 3957 120 -73 -137 C
ATOM 3680 CG2 VAL A 489 45.922 4.138 -17.335 1.00 19.97 C
ANISOU 3680 CG2 VAL A 489 3181 1116 3290 112 -372 -78 C
ATOM 3681 N PHE A 490 46.244 5.428 -20.664 1.00 24.57 N
ANISOU 3681 N PHE A 490 3559 1846 3932 -86 -228 -119 N
ATOM 3682 CA PHE A 490 45.982 6.796 -21.092 1.00 19.07 C
ANISOU 3682 CA PHE A 490 2839 1210 3197 -137 -321 -117 C
ATOM 3683 C PHE A 490 46.099 6.979 -22.603 1.00 24.90 C
ANISOU 3683 C PHE A 490 3484 2018 3957 -219 -212 -131 C
ATOM 3684 O PHE A 490 46.303 8.105 -23.069 1.00 25.75 O
ANISOU 3684 O PHE A 490 3536 2165 4081 -259 -291 -103 O
ATOM 3685 CB PHE A 490 46.927 7.762 -20.374 1.00 19.49 C
ANISOU 3685 CB PHE A 490 2854 1220 3332 -101 -510 -46 C
ATOM 3686 CG PHE A 490 46.903 7.641 -18.873 1.00 21.56 C
ANISOU 3686 CG PHE A 490 3198 1422 3573 -20 -627 -29 C
ATOM 3687 CD1 PHE A 490 45.776 8.005 -18.152 1.00 24.87 C
ANISOU 3687 CD1 PHE A 490 3730 1859 3862 -4 -688 -69 C
ATOM 3688 CD2 PHE A 490 48.014 7.185 -18.181 1.00 22.72 C
ANISOU 3688 CD2 PHE A 490 3305 1502 3826 42 -679 30 C
ATOM 3689 CE1 PHE A 490 45.757 7.904 -16.772 1.00 25.31 C
ANISOU 3689 CE1 PHE A 490 3858 1868 3891 71 -796 -53 C
ATOM 3690 CE2 PHE A 490 48.000 7.084 -16.800 1.00 25.89 C
ANISOU 3690 CE2 PHE A 490 3776 1859 4201 117 -789 49 C
ATOM 3691 CZ PHE A 490 46.869 7.442 -16.097 1.00 26.64 C
ANISOU 3691 CZ PHE A 490 3984 1974 4163 131 -847 6 C
ATOM 3692 N ALA A 491 45.964 5.899 -23.377 1.00 27.59 N
ANISOU 3692 N ALA A 491 3807 2377 4299 -246 -33 -175 N
ATOM 3693 CA ALA A 491 46.192 5.986 -24.817 1.00 27.84 C
ANISOU 3693 CA ALA A 491 3741 2481 4358 -320 76 -188 C
ATOM 3694 C ALA A 491 45.116 6.815 -25.509 1.00 34.95 C
ANISOU 3694 C ALA A 491 4659 3483 5137 -391 84 -226 C
ATOM 3695 O ALA A 491 45.409 7.557 -26.455 1.00 44.73 O
ANISOU 3695 O ALA A 491 5809 4785 6401 -446 83 -204 O
ATOM 3696 CB ALA A 491 46.257 4.586 -25.424 1.00 28.59 C
ANISOU 3696 CB ALA A 491 3820 2568 4476 -330 269 -237 C
ATOM 3697 N ASN A 492 43.866 6.703 -25.062 1.00 31.64 N
ANISOU 3697 N ASN A 492 4349 3086 4587 -391 94 -279 N
ATOM 3698 CA ASN A 492 42.772 7.442 -25.678 1.00 34.99 C
ANISOU 3698 CA ASN A 492 4794 3612 4889 -453 106 -314 C
ATOM 3699 C ASN A 492 42.530 8.806 -25.047 1.00 25.73 C
ANISOU 3699 C ASN A 492 3654 2438 3684 -434 -73 -274 C
ATOM 3700 O ASN A 492 41.875 9.647 -25.671 1.00 30.32 O
ANISOU 3700 O ASN A 492 4225 3102 4193 -485 -81 -281 O
ATOM 3701 CB ASN A 492 41.474 6.631 -25.621 1.00 49.46 C
ANISOU 3701 CB ASN A 492 6722 5482 6588 -469 218 -394 C
ATOM 3702 CG ASN A 492 41.514 5.408 -26.506 1.00 71.81 C
ANISOU 3702 CG ASN A 492 9518 8334 9432 -511 412 -449 C
ATOM 3703 OD1 ASN A 492 41.705 4.295 -26.026 1.00 88.57 O
ANISOU 3703 OD1 ASN A 492 11678 10384 11591 -472 477 -468 O
ATOM 3704 ND2 ASN A 492 41.348 5.610 -27.811 1.00 74.31 N
ANISOU 3704 ND2 ASN A 492 9761 8752 9721 -589 506 -474 N
ATOM 3705 N THR A 493 43.036 9.053 -23.840 1.00 26.39 N
ANISOU 3705 N THR A 493 3776 2434 3819 -363 -215 -234 N
ATOM 3706 CA THR A 493 42.763 10.307 -23.138 1.00 24.94 C
ANISOU 3706 CA THR A 493 3635 2241 3600 -341 -386 -208 C
ATOM 3707 C THR A 493 43.745 11.395 -23.577 1.00 23.02 C
ANISOU 3707 C THR A 493 3290 1992 3465 -365 -484 -142 C
ATOM 3708 O THR A 493 44.491 11.979 -22.790 1.00 27.71 O
ANISOU 3708 O THR A 493 3877 2517 4135 -325 -631 -94 O
ATOM 3709 CB THR A 493 42.797 10.085 -21.632 1.00 26.28 C
ANISOU 3709 CB THR A 493 3894 2328 3763 -258 -493 -202 C
ATOM 3710 OG1 THR A 493 44.076 9.566 -21.246 1.00 27.51 O
ANISOU 3710 OG1 THR A 493 3995 2406 4051 -216 -518 -155 O
ATOM 3711 CG2 THR A 493 41.709 9.097 -21.230 1.00 22.74 C
ANISOU 3711 CG2 THR A 493 3547 1893 3198 -240 -396 -263 C
ATOM 3712 N THR A 494 43.699 11.672 -24.881 1.00 17.10 N
ANISOU 3712 N THR A 494 2460 1322 2717 -437 -398 -140 N
ATOM 3713 CA THR A 494 44.631 12.573 -25.549 1.00 17.52 C
ANISOU 3713 CA THR A 494 2399 1383 2874 -473 -456 -74 C
ATOM 3714 C THR A 494 44.479 14.026 -25.111 1.00 18.65 C
ANISOU 3714 C THR A 494 2563 1511 3012 -470 -624 -38 C
ATOM 3715 O THR A 494 45.400 14.819 -25.332 1.00 25.70 O
ANISOU 3715 O THR A 494 3372 2380 4011 -486 -710 25 O
ATOM 3716 CB THR A 494 44.440 12.437 -27.068 1.00 29.97 C
ANISOU 3716 CB THR A 494 3892 3066 4430 -552 -307 -87 C
ATOM 3717 OG1 THR A 494 44.359 11.044 -27.406 1.00 41.91 O
ANISOU 3717 OG1 THR A 494 5407 4592 5926 -555 -143 -140 O
ATOM 3718 CG2 THR A 494 45.596 13.036 -27.838 1.00 46.10 C
ANISOU 3718 CG2 THR A 494 5801 5118 6599 -587 -334 -15 C
ATOM 3719 N ASN A 495 43.365 14.393 -24.480 1.00 21.83 N
ANISOU 3719 N ASN A 495 3074 1922 3297 -448 -674 -77 N
ATOM 3720 CA ASN A 495 43.121 15.776 -24.087 1.00 16.91 C
ANISOU 3720 CA ASN A 495 2479 1282 2662 -443 -825 -51 C
ATOM 3721 C ASN A 495 43.164 15.986 -22.579 1.00 18.13 C
ANISOU 3721 C ASN A 495 2726 1349 2815 -368 -974 -59 C
ATOM 3722 O ASN A 495 42.696 17.024 -22.096 1.00 19.18 O
ANISOU 3722 O ASN A 495 2913 1468 2909 -354 -1090 -59 O
ATOM 3723 CB ASN A 495 41.780 16.256 -24.645 1.00 20.41 C
ANISOU 3723 CB ASN A 495 2965 1818 2972 -478 -774 -84 C
ATOM 3724 CG ASN A 495 41.789 16.365 -26.155 1.00 21.90 C
ANISOU 3724 CG ASN A 495 3050 2103 3167 -556 -656 -65 C
ATOM 3725 OD1 ASN A 495 42.637 17.046 -26.734 1.00 27.95 O
ANISOU 3725 OD1 ASN A 495 3718 2864 4036 -589 -697 -3 O
ATOM 3726 ND2 ASN A 495 40.857 15.677 -26.805 1.00 20.81 N
ANISOU 3726 ND2 ASN A 495 2931 2059 2918 -589 -509 -117 N
ATOM 3727 N LEU A 496 43.709 15.031 -21.826 1.00 17.19 N
ANISOU 3727 N LEU A 496 2626 1171 2734 -318 -971 -64 N
ATOM 3728 CA LEU A 496 43.934 15.227 -20.399 1.00 19.89 C
ANISOU 3728 CA LEU A 496 3039 1434 3084 -247 -1118 -61 C
ATOM 3729 C LEU A 496 44.784 16.466 -20.161 1.00 18.53 C
ANISOU 3729 C LEU A 496 2816 1210 3013 -253 -1284 -9 C
ATOM 3730 O LEU A 496 45.806 16.667 -20.820 1.00 19.56 O
ANISOU 3730 O LEU A 496 2836 1332 3262 -290 -1283 44 O
ATOM 3731 CB LEU A 496 44.631 14.005 -19.795 1.00 19.06 C
ANISOU 3731 CB LEU A 496 2932 1278 3033 -198 -1083 -55 C
ATOM 3732 CG LEU A 496 43.835 12.757 -19.420 1.00 23.09 C
ANISOU 3732 CG LEU A 496 3525 1801 3446 -164 -970 -106 C
ATOM 3733 CD1 LEU A 496 44.755 11.708 -18.803 1.00 28.94 C
ANISOU 3733 CD1 LEU A 496 4247 2477 4270 -111 -956 -80 C
ATOM 3734 CD2 LEU A 496 42.697 13.095 -18.473 1.00 20.18 C
ANISOU 3734 CD2 LEU A 496 3283 1440 2946 -124 -1040 -150 C
ATOM 3735 N THR A 497 44.353 17.297 -19.211 1.00 20.16 N
ANISOU 3735 N THR A 497 3090 1417 3155 -205 -1401 -19 N
ATOM 3736 CA THR A 497 45.145 18.421 -18.738 1.00 18.54 C
ANISOU 3736 CA THR A 497 2842 1182 3022 -188 -1548 28 C
ATOM 3737 C THR A 497 45.498 18.312 -17.264 1.00 18.96 C
ANISOU 3737 C THR A 497 2943 1196 3066 -113 -1665 23 C
ATOM 3738 O THR A 497 46.379 19.046 -16.797 1.00 20.06 O
ANISOU 3738 O THR A 497 3040 1299 3285 -101 -1793 60 O
ATOM 3739 CB THR A 497 44.404 19.748 -18.974 1.00 26.69 C
ANISOU 3739 CB THR A 497 3892 2257 3991 -191 -1579 36 C
ATOM 3740 OG1 THR A 497 43.141 19.728 -18.290 1.00 30.54 O
ANISOU 3740 OG1 THR A 497 4488 2782 4333 -136 -1556 -8 O
ATOM 3741 CG2 THR A 497 44.177 19.970 -20.466 1.00 18.43 C
ANISOU 3741 CG2 THR A 497 2782 1257 2963 -274 -1481 49 C
ATOM 3742 N PHE A 498 44.847 17.414 -16.530 1.00 18.64 N
ANISOU 3742 N PHE A 498 2987 1166 2930 -65 -1625 -21 N
ATOM 3743 CA PHE A 498 45.031 17.265 -15.093 1.00 28.05 C
ANISOU 3743 CA PHE A 498 4231 2337 4091 3 -1732 -33 C
ATOM 3744 C PHE A 498 44.959 15.780 -14.771 1.00 29.03 C
ANISOU 3744 C PHE A 498 4391 2447 4193 31 -1639 -53 C
ATOM 3745 O PHE A 498 43.924 15.144 -15.006 1.00 22.80 O
ANISOU 3745 O PHE A 498 3664 1694 3305 36 -1523 -88 O
ATOM 3746 CB PHE A 498 43.953 18.043 -14.329 1.00 20.96 C
ANISOU 3746 CB PHE A 498 3420 1476 3067 58 -1763 -51 C
ATOM 3747 CG PHE A 498 44.111 18.009 -12.834 1.00 24.54 C
ANISOU 3747 CG PHE A 498 3914 1919 3491 107 -1790 -78 C
ATOM 3748 CD1 PHE A 498 43.689 16.911 -12.100 1.00 26.38 C
ANISOU 3748 CD1 PHE A 498 4207 2172 3645 142 -1766 -114 C
ATOM 3749 CD2 PHE A 498 44.660 19.087 -12.160 1.00 28.52 C
ANISOU 3749 CD2 PHE A 498 4414 2364 4058 106 -1834 -80 C
ATOM 3750 CE1 PHE A 498 43.829 16.881 -10.727 1.00 32.04 C
ANISOU 3750 CE1 PHE A 498 4972 2850 4350 165 -1784 -163 C
ATOM 3751 CE2 PHE A 498 44.799 19.064 -10.785 1.00 28.66 C
ANISOU 3751 CE2 PHE A 498 4481 2353 4057 135 -1867 -123 C
ATOM 3752 CZ PHE A 498 44.379 17.957 -10.068 1.00 27.33 C
ANISOU 3752 CZ PHE A 498 4367 2204 3814 169 -1842 -158 C
ATOM 3753 N LEU A 499 46.043 15.228 -14.227 1.00 26.14 N
ANISOU 3753 N LEU A 499 3983 2031 3917 55 -1681 -24 N
ATOM 3754 CA LEU A 499 46.123 13.808 -13.902 1.00 21.69 C
ANISOU 3754 CA LEU A 499 3442 1448 3352 97 -1586 -21 C
ATOM 3755 C LEU A 499 46.690 13.649 -12.498 1.00 27.24 C
ANISOU 3755 C LEU A 499 4158 2140 4052 152 -1689 -15 C
ATOM 3756 O LEU A 499 47.842 14.016 -12.246 1.00 28.01 O
ANISOU 3756 O LEU A 499 4181 2210 4251 144 -1777 21 O
ATOM 3757 CB LEU A 499 46.988 13.063 -14.923 1.00 19.94 C
ANISOU 3757 CB LEU A 499 3133 1180 3263 69 -1485 24 C
ATOM 3758 CG LEU A 499 47.096 11.545 -14.772 1.00 25.04 C
ANISOU 3758 CG LEU A 499 3795 1796 3924 112 -1366 31 C
ATOM 3759 CD1 LEU A 499 45.721 10.902 -14.778 1.00 19.32 C
ANISOU 3759 CD1 LEU A 499 3173 1103 3063 118 -1255 -29 C
ATOM 3760 CD2 LEU A 499 47.972 10.954 -15.868 1.00 23.62 C
ANISOU 3760 CD2 LEU A 499 3507 1599 3869 77 -1255 69 C
ATOM 3761 N ASP A 500 45.888 13.093 -11.592 1.00 28.07 N
ANISOU 3761 N ASP A 500 4353 2271 4042 200 -1671 -51 N
ATOM 3762 CA ASP A 500 46.267 12.917 -10.194 1.00 26.51 C
ANISOU 3762 CA ASP A 500 4178 2073 3823 246 -1751 -57 C
ATOM 3763 C ASP A 500 46.413 11.425 -9.921 1.00 29.64 C
ANISOU 3763 C ASP A 500 4580 2454 4227 300 -1648 -23 C
ATOM 3764 O ASP A 500 45.413 10.706 -9.824 1.00 20.74 O
ANISOU 3764 O ASP A 500 3529 1346 3006 324 -1559 -48 O
ATOM 3765 CB ASP A 500 45.231 13.549 -9.265 1.00 32.92 C
ANISOU 3765 CB ASP A 500 5091 2917 4500 256 -1813 -131 C
ATOM 3766 CG ASP A 500 45.706 13.622 -7.821 1.00 36.70 C
ANISOU 3766 CG ASP A 500 5591 3379 4975 288 -1888 -148 C
ATOM 3767 OD1 ASP A 500 46.765 13.048 -7.499 1.00 31.30 O
ANISOU 3767 OD1 ASP A 500 4844 2679 4370 311 -1900 -93 O
ATOM 3768 OD2 ASP A 500 45.019 14.270 -7.003 1.00 32.95 O
ANISOU 3768 OD2 ASP A 500 5197 2896 4427 295 -1920 -212 O
ATOM 3769 N LEU A 501 47.658 10.965 -9.789 1.00 29.08 N
ANISOU 3769 N LEU A 501 4430 2349 4272 317 -1658 36 N
ATOM 3770 CA LEU A 501 47.953 9.566 -9.509 1.00 25.52 C
ANISOU 3770 CA LEU A 501 3974 1875 3848 372 -1562 77 C
ATOM 3771 C LEU A 501 48.594 9.371 -8.137 1.00 29.60 C
ANISOU 3771 C LEU A 501 4484 2402 4361 423 -1644 102 C
ATOM 3772 O LEU A 501 49.308 8.386 -7.925 1.00 29.09 O
ANISOU 3772 O LEU A 501 4378 2313 4363 467 -1593 160 O
ATOM 3773 CB LEU A 501 48.855 8.988 -10.599 1.00 27.75 C
ANISOU 3773 CB LEU A 501 4164 2105 4273 358 -1474 131 C
ATOM 3774 CG LEU A 501 48.215 8.697 -11.959 1.00 25.96 C
ANISOU 3774 CG LEU A 501 3949 1859 4054 313 -1338 105 C
ATOM 3775 CD1 LEU A 501 49.277 8.639 -13.054 1.00 26.72 C
ANISOU 3775 CD1 LEU A 501 3934 1911 4306 279 -1298 152 C
ATOM 3776 CD2 LEU A 501 47.423 7.398 -11.914 1.00 21.39 C
ANISOU 3776 CD2 LEU A 501 3443 1267 3417 344 -1192 84 C
ATOM 3777 N SER A 502 48.347 10.283 -7.200 1.00 28.39 N
ANISOU 3777 N SER A 502 4371 2281 4134 416 -1761 57 N
ATOM 3778 CA SER A 502 48.981 10.211 -5.891 1.00 28.86 C
ANISOU 3778 CA SER A 502 4424 2352 4191 455 -1836 74 C
ATOM 3779 C SER A 502 48.403 9.068 -5.066 1.00 30.28 C
ANISOU 3779 C SER A 502 4664 2551 4290 521 -1767 85 C
ATOM 3780 O SER A 502 47.253 8.661 -5.246 1.00 30.46 O
ANISOU 3780 O SER A 502 4762 2587 4224 529 -1691 52 O
ATOM 3781 CB SER A 502 48.807 11.532 -5.139 1.00 33.11 C
ANISOU 3781 CB SER A 502 5001 2903 4678 424 -1957 9 C
ATOM 3782 OG SER A 502 47.444 11.789 -4.848 1.00 29.37 O
ANISOU 3782 OG SER A 502 4630 2453 4077 425 -1937 -63 O
ATOM 3783 N LYS A 503 49.225 8.553 -4.150 1.00 28.63 N
ANISOU 3783 N LYS A 503 4418 2345 4113 568 -1794 136 N
ATOM 3784 CA LYS A 503 48.819 7.507 -3.208 1.00 30.43 C
ANISOU 3784 CA LYS A 503 4693 2593 4274 635 -1742 159 C
ATOM 3785 C LYS A 503 48.280 6.272 -3.929 1.00 29.06 C
ANISOU 3785 C LYS A 503 4542 2390 4107 659 -1590 187 C
ATOM 3786 O LYS A 503 47.313 5.648 -3.492 1.00 32.73 O
ANISOU 3786 O LYS A 503 5083 2872 4480 688 -1531 170 O
ATOM 3787 CB LYS A 503 47.794 8.035 -2.201 1.00 27.17 C
ANISOU 3787 CB LYS A 503 4374 2227 3725 638 -1793 88 C
ATOM 3788 CG LYS A 503 48.187 9.342 -1.529 1.00 36.21 C
ANISOU 3788 CG LYS A 503 5512 3383 4865 608 -1921 43 C
ATOM 3789 CD LYS A 503 47.192 9.716 -0.441 1.00 43.47 C
ANISOU 3789 CD LYS A 503 6521 4336 5659 625 -1945 -23 C
ATOM 3790 CE LYS A 503 47.345 11.170 -0.026 1.00 54.71 C
ANISOU 3790 CE LYS A 503 7955 5746 7086 587 -2042 -85 C
ATOM 3791 NZ LYS A 503 46.420 11.527 1.083 1.00 63.63 N
ANISOU 3791 NZ LYS A 503 9166 6900 8111 614 -2047 -143 N
ATOM 3792 N CYS A 504 48.916 5.907 -5.043 1.00 24.89 N
ANISOU 3792 N CYS A 504 3949 1813 3695 644 -1520 225 N
ATOM 3793 CA CYS A 504 48.511 4.742 -5.820 1.00 27.61 C
ANISOU 3793 CA CYS A 504 4311 2111 4067 658 -1359 242 C
ATOM 3794 C CYS A 504 49.468 3.566 -5.654 1.00 30.96 C
ANISOU 3794 C CYS A 504 4677 2492 4594 716 -1286 327 C
ATOM 3795 O CYS A 504 49.392 2.600 -6.421 1.00 34.68 O
ANISOU 3795 O CYS A 504 5147 2907 5122 724 -1143 342 O
ATOM 3796 CB CYS A 504 48.367 5.109 -7.297 1.00 25.19 C
ANISOU 3796 CB CYS A 504 3984 1774 3811 595 -1301 212 C
ATOM 3797 SG CYS A 504 46.849 6.004 -7.691 1.00 35.94 S
ANISOU 3797 SG CYS A 504 5440 3180 5037 539 -1314 117 S
ATOM 3798 N GLN A 505 50.368 3.631 -4.667 1.00 29.90 N
ANISOU 3798 N GLN A 505 4496 2382 4484 757 -1375 378 N
ATOM 3799 CA GLN A 505 51.282 2.527 -4.360 1.00 30.80 C
ANISOU 3799 CA GLN A 505 4553 2463 4685 822 -1313 467 C
ATOM 3800 C GLN A 505 52.088 2.105 -5.588 1.00 29.31 C
ANISOU 3800 C GLN A 505 4289 2210 4638 811 -1223 500 C
ATOM 3801 O GLN A 505 52.512 0.952 -5.710 1.00 34.03 O
ANISOU 3801 O GLN A 505 4862 2759 5308 861 -1112 557 O
ATOM 3802 CB GLN A 505 50.524 1.337 -3.766 1.00 39.20 C
ANISOU 3802 CB GLN A 505 5686 3516 5691 878 -1210 486 C
ATOM 3803 CG GLN A 505 49.765 1.669 -2.486 1.00 41.59 C
ANISOU 3803 CG GLN A 505 6057 3888 5856 895 -1295 460 C
ATOM 3804 CD GLN A 505 49.053 0.464 -1.901 1.00 35.86 C
ANISOU 3804 CD GLN A 505 5391 3152 5083 948 -1195 490 C
ATOM 3805 OE1 GLN A 505 47.829 0.462 -1.755 1.00 38.47 O
ANISOU 3805 OE1 GLN A 505 5807 3503 5306 932 -1172 435 O
ATOM 3806 NE2 GLN A 505 49.817 -0.564 -1.555 1.00 32.10 N
ANISOU 3806 NE2 GLN A 505 4867 2643 4686 1013 -1134 580 N
ATOM 3807 N LEU A 506 52.300 3.044 -6.508 1.00 26.61 N
ANISOU 3807 N LEU A 506 3907 1866 4338 745 -1267 466 N
ATOM 3808 CA LEU A 506 53.067 2.766 -7.713 1.00 27.48 C
ANISOU 3808 CA LEU A 506 3936 1923 4584 726 -1189 493 C
ATOM 3809 C LEU A 506 54.541 2.580 -7.381 1.00 34.10 C
ANISOU 3809 C LEU A 506 4669 2759 5529 765 -1235 576 C
ATOM 3810 O LEU A 506 55.106 3.306 -6.559 1.00 36.66 O
ANISOU 3810 O LEU A 506 4962 3133 5836 767 -1373 594 O
ATOM 3811 CB LEU A 506 52.903 3.905 -8.718 1.00 26.12 C
ANISOU 3811 CB LEU A 506 3742 1757 4425 642 -1236 441 C
ATOM 3812 CG LEU A 506 51.520 4.095 -9.334 1.00 25.66 C
ANISOU 3812 CG LEU A 506 3774 1699 4275 596 -1174 361 C
ATOM 3813 CD1 LEU A 506 51.520 5.293 -10.269 1.00 28.58 C
ANISOU 3813 CD1 LEU A 506 4109 2081 4669 518 -1233 326 C
ATOM 3814 CD2 LEU A 506 51.114 2.836 -10.070 1.00 28.07 C
ANISOU 3814 CD2 LEU A 506 4106 1945 4615 607 -987 354 C
ATOM 3815 N GLU A 507 55.166 1.599 -8.033 1.00 31.64 N
ANISOU 3815 N GLU A 507 4301 2391 5328 795 -1113 624 N
ATOM 3816 CA GLU A 507 56.595 1.363 -7.893 1.00 35.73 C
ANISOU 3816 CA GLU A 507 4711 2908 5958 832 -1140 705 C
ATOM 3817 C GLU A 507 57.374 1.602 -9.175 1.00 33.72 C
ANISOU 3817 C GLU A 507 4353 2623 5836 788 -1106 718 C
ATOM 3818 O GLU A 507 58.582 1.848 -9.107 1.00 31.31 O
ANISOU 3818 O GLU A 507 3945 2334 5617 796 -1171 778 O
ATOM 3819 CB GLU A 507 56.858 -0.073 -7.412 1.00 30.27 C
ANISOU 3819 CB GLU A 507 4026 2181 5292 921 -1029 766 C
ATOM 3820 CG GLU A 507 56.425 -0.338 -5.978 1.00 37.35 C
ANISOU 3820 CG GLU A 507 4995 3119 6080 977 -1078 784 C
ATOM 3821 CD GLU A 507 56.512 -1.805 -5.599 1.00 38.85 C
ANISOU 3821 CD GLU A 507 5206 3265 6290 1063 -951 841 C
ATOM 3822 OE1 GLU A 507 57.088 -2.593 -6.379 1.00 44.07 O
ANISOU 3822 OE1 GLU A 507 5819 3867 7058 1080 -838 868 O
ATOM 3823 OE2 GLU A 507 56.001 -2.173 -4.521 1.00 41.94 O
ANISOU 3823 OE2 GLU A 507 5661 3681 6592 1110 -964 858 O
ATOM 3824 N GLN A 508 56.718 1.538 -10.329 1.00 33.86 N
ANISOU 3824 N GLN A 508 4391 2602 5872 740 -1003 664 N
ATOM 3825 CA GLN A 508 57.383 1.753 -11.606 1.00 38.51 C
ANISOU 3825 CA GLN A 508 4878 3165 6587 694 -958 675 C
ATOM 3826 C GLN A 508 56.324 2.052 -12.657 1.00 39.05 C
ANISOU 3826 C GLN A 508 4998 3214 6625 625 -884 595 C
ATOM 3827 O GLN A 508 55.128 1.826 -12.448 1.00 39.55 O
ANISOU 3827 O GLN A 508 5175 3275 6579 620 -840 535 O
ATOM 3828 CB GLN A 508 58.232 0.542 -12.002 1.00 37.81 C
ANISOU 3828 CB GLN A 508 4717 3029 6620 748 -821 732 C
ATOM 3829 CG GLN A 508 57.445 -0.748 -12.130 1.00 45.01 C
ANISOU 3829 CG GLN A 508 5709 3887 7504 781 -647 699 C
ATOM 3830 CD GLN A 508 58.328 -1.972 -12.040 1.00 59.68 C
ANISOU 3830 CD GLN A 508 7512 5709 9453 854 -541 764 C
ATOM 3831 OE1 GLN A 508 59.552 -1.867 -11.978 1.00 63.78 O
ANISOU 3831 OE1 GLN A 508 7925 6245 10065 879 -592 834 O
ATOM 3832 NE2 GLN A 508 57.709 -3.145 -12.023 1.00 69.40 N
ANISOU 3832 NE2 GLN A 508 8817 6893 10658 885 -395 738 N
ATOM 3833 N ILE A 509 56.784 2.553 -13.803 1.00 35.93 N
ANISOU 3833 N ILE A 509 4515 2810 6328 569 -868 597 N
ATOM 3834 CA ILE A 509 55.917 3.022 -14.876 1.00 32.25 C
ANISOU 3834 CA ILE A 509 4076 2369 5808 482 -798 518 C
ATOM 3835 C ILE A 509 56.286 2.284 -16.155 1.00 31.71 C
ANISOU 3835 C ILE A 509 3932 2296 5821 454 -612 507 C
ATOM 3836 O ILE A 509 57.469 2.189 -16.503 1.00 33.70 O
ANISOU 3836 O ILE A 509 4067 2542 6197 469 -607 570 O
ATOM 3837 CB ILE A 509 56.041 4.546 -15.061 1.00 29.81 C
ANISOU 3837 CB ILE A 509 3733 2107 5488 416 -952 514 C
ATOM 3838 CG1 ILE A 509 55.714 5.268 -13.753 1.00 27.18 C
ANISOU 3838 CG1 ILE A 509 3475 1788 5065 443 -1131 513 C
ATOM 3839 CG2 ILE A 509 55.140 5.035 -16.189 1.00 33.26 C
ANISOU 3839 CG2 ILE A 509 4194 2588 5857 326 -871 436 C
ATOM 3840 CD1 ILE A 509 56.001 6.746 -13.783 1.00 30.77 C
ANISOU 3840 CD1 ILE A 509 3890 2283 5519 384 -1289 514 C
ATOM 3841 N SER A 510 55.278 1.769 -16.855 1.00 30.61 N
ANISOU 3841 N SER A 510 3857 2164 5611 414 -459 427 N
ATOM 3842 CA SER A 510 55.521 1.080 -18.112 1.00 32.85 C
ANISOU 3842 CA SER A 510 4075 2450 5958 381 -276 401 C
ATOM 3843 C SER A 510 56.000 2.064 -19.177 1.00 36.47 C
ANISOU 3843 C SER A 510 4431 2969 6458 304 -302 404 C
ATOM 3844 O SER A 510 55.907 3.285 -19.030 1.00 37.68 O
ANISOU 3844 O SER A 510 4581 3160 6575 264 -447 411 O
ATOM 3845 CB SER A 510 54.261 0.358 -18.588 1.00 33.04 C
ANISOU 3845 CB SER A 510 4195 2475 5884 348 -115 306 C
ATOM 3846 OG SER A 510 54.128 -0.897 -17.945 1.00 46.72 O
ANISOU 3846 OG SER A 510 5986 4138 7628 420 -29 314 O
ATOM 3847 N TRP A 511 56.518 1.510 -20.268 1.00 33.53 N
ANISOU 3847 N TRP A 511 3973 2604 6162 283 -156 398 N
ATOM 3848 CA TRP A 511 57.068 2.334 -21.334 1.00 35.88 C
ANISOU 3848 CA TRP A 511 4161 2964 6510 214 -165 410 C
ATOM 3849 C TRP A 511 55.947 2.966 -22.155 1.00 31.83 C
ANISOU 3849 C TRP A 511 3694 2518 5883 121 -127 329 C
ATOM 3850 O TRP A 511 54.975 2.298 -22.520 1.00 29.55 O
ANISOU 3850 O TRP A 511 3479 2235 5513 101 7 250 O
ATOM 3851 CB TRP A 511 57.978 1.494 -22.229 1.00 43.50 C
ANISOU 3851 CB TRP A 511 5018 3921 7589 227 -15 429 C
ATOM 3852 CG TRP A 511 58.682 2.291 -23.280 1.00 51.85 C
ANISOU 3852 CG TRP A 511 5948 5044 8707 164 -27 456 C
ATOM 3853 CD1 TRP A 511 59.918 2.858 -23.185 1.00 51.47 C
ANISOU 3853 CD1 TRP A 511 5784 5004 8768 178 -134 547 C
ATOM 3854 CD2 TRP A 511 58.190 2.614 -24.585 1.00 52.50 C
ANISOU 3854 CD2 TRP A 511 6003 5202 8743 75 72 395 C
ATOM 3855 NE1 TRP A 511 60.228 3.515 -24.353 1.00 46.93 N
ANISOU 3855 NE1 TRP A 511 5112 4501 8220 103 -107 549 N
ATOM 3856 CE2 TRP A 511 59.182 3.380 -25.228 1.00 49.68 C
ANISOU 3856 CE2 TRP A 511 5511 4893 8472 40 19 458 C
ATOM 3857 CE3 TRP A 511 57.008 2.329 -25.272 1.00 51.49 C
ANISOU 3857 CE3 TRP A 511 5947 5111 8506 19 199 297 C
ATOM 3858 CZ2 TRP A 511 59.026 3.865 -26.525 1.00 51.37 C
ANISOU 3858 CZ2 TRP A 511 5662 5191 8667 -44 91 428 C
ATOM 3859 CZ3 TRP A 511 56.855 2.810 -26.557 1.00 52.21 C
ANISOU 3859 CZ3 TRP A 511 5973 5288 8574 -66 269 265 C
ATOM 3860 CH2 TRP A 511 57.858 3.568 -27.172 1.00 52.41 C
ANISOU 3860 CH2 TRP A 511 5866 5362 8687 -95 215 332 C
ATOM 3861 N GLY A 512 56.082 4.261 -22.438 1.00 32.32 N
ANISOU 3861 N GLY A 512 3709 2631 5939 65 -246 351 N
ATOM 3862 CA GLY A 512 55.174 4.962 -23.327 1.00 29.18 C
ANISOU 3862 CA GLY A 512 3330 2307 5449 -23 -214 291 C
ATOM 3863 C GLY A 512 53.857 5.392 -22.723 1.00 30.18 C
ANISOU 3863 C GLY A 512 3590 2442 5435 -36 -275 236 C
ATOM 3864 O GLY A 512 52.941 5.751 -23.474 1.00 33.68 O
ANISOU 3864 O GLY A 512 4061 2948 5787 -103 -218 177 O
ATOM 3865 N VAL A 513 53.736 5.389 -21.394 1.00 28.55 N
ANISOU 3865 N VAL A 513 3462 2182 5204 28 -391 255 N
ATOM 3866 CA VAL A 513 52.446 5.656 -20.761 1.00 24.66 C
ANISOU 3866 CA VAL A 513 3101 1696 4572 26 -436 199 C
ATOM 3867 C VAL A 513 51.989 7.093 -21.001 1.00 22.52 C
ANISOU 3867 C VAL A 513 2835 1478 4243 -36 -550 190 C
ATOM 3868 O VAL A 513 50.784 7.364 -21.065 1.00 27.22 O
ANISOU 3868 O VAL A 513 3517 2109 4716 -67 -534 130 O
ATOM 3869 CB VAL A 513 52.530 5.320 -19.258 1.00 27.15 C
ANISOU 3869 CB VAL A 513 3489 1947 4880 113 -539 229 C
ATOM 3870 CG1 VAL A 513 51.289 5.785 -18.521 1.00 28.47 C
ANISOU 3870 CG1 VAL A 513 3784 2127 4905 114 -613 180 C
ATOM 3871 CG2 VAL A 513 52.709 3.826 -19.078 1.00 31.70 C
ANISOU 3871 CG2 VAL A 513 4079 2471 5494 172 -402 230 C
ATOM 3872 N PHE A 514 52.928 8.028 -21.172 1.00 27.20 N
ANISOU 3872 N PHE A 514 3332 2076 4925 -57 -662 252 N
ATOM 3873 CA PHE A 514 52.613 9.450 -21.291 1.00 22.79 C
ANISOU 3873 CA PHE A 514 2776 1552 4330 -109 -787 255 C
ATOM 3874 C PHE A 514 52.845 10.018 -22.688 1.00 22.98 C
ANISOU 3874 C PHE A 514 2698 1641 4392 -190 -726 266 C
ATOM 3875 O PHE A 514 52.681 11.228 -22.881 1.00 29.43 O
ANISOU 3875 O PHE A 514 3504 2483 5196 -236 -825 279 O
ATOM 3876 CB PHE A 514 53.434 10.271 -20.290 1.00 23.10 C
ANISOU 3876 CB PHE A 514 2795 1546 4437 -76 -988 316 C
ATOM 3877 CG PHE A 514 53.291 9.829 -18.865 1.00 27.17 C
ANISOU 3877 CG PHE A 514 3400 2007 4915 5 -1067 314 C
ATOM 3878 CD1 PHE A 514 52.060 9.868 -18.231 1.00 27.80 C
ANISOU 3878 CD1 PHE A 514 3611 2090 4861 22 -1085 253 C
ATOM 3879 CD2 PHE A 514 54.396 9.407 -18.148 1.00 31.92 C
ANISOU 3879 CD2 PHE A 514 3951 2562 5614 65 -1127 377 C
ATOM 3880 CE1 PHE A 514 51.930 9.472 -16.912 1.00 22.71 C
ANISOU 3880 CE1 PHE A 514 3047 1404 4178 97 -1158 255 C
ATOM 3881 CE2 PHE A 514 54.274 9.009 -16.828 1.00 35.54 C
ANISOU 3881 CE2 PHE A 514 4488 2981 6034 141 -1201 380 C
ATOM 3882 CZ PHE A 514 53.038 9.040 -16.209 1.00 28.93 C
ANISOU 3882 CZ PHE A 514 3782 2148 5061 156 -1217 319 C
ATOM 3883 N ASP A 515 53.227 9.192 -23.663 1.00 23.34 N
ANISOU 3883 N ASP A 515 2670 1713 4486 -208 -566 262 N
ATOM 3884 CA ASP A 515 53.582 9.713 -24.980 1.00 31.30 C
ANISOU 3884 CA ASP A 515 3567 2790 5536 -281 -512 283 C
ATOM 3885 C ASP A 515 52.406 10.338 -25.724 1.00 31.98 C
ANISOU 3885 C ASP A 515 3693 2952 5506 -351 -471 231 C
ATOM 3886 O ASP A 515 52.627 11.004 -26.743 1.00 33.83 O
ANISOU 3886 O ASP A 515 3838 3248 5766 -415 -453 257 O
ATOM 3887 CB ASP A 515 54.200 8.607 -25.834 1.00 32.96 C
ANISOU 3887 CB ASP A 515 3694 3016 5814 -280 -340 281 C
ATOM 3888 CG ASP A 515 55.578 8.199 -25.350 1.00 41.49 C
ANISOU 3888 CG ASP A 515 4696 4037 7033 -220 -384 353 C
ATOM 3889 OD1 ASP A 515 56.231 9.000 -24.646 1.00 48.86 O
ANISOU 3889 OD1 ASP A 515 5602 4938 8025 -204 -552 417 O
ATOM 3890 OD2 ASP A 515 56.010 7.076 -25.678 1.00 50.11 O
ANISOU 3890 OD2 ASP A 515 5751 5115 8174 -190 -249 345 O
ATOM 3891 N THR A 516 51.178 10.161 -25.238 1.00 28.92 N
ANISOU 3891 N THR A 516 3432 2566 4992 -339 -458 166 N
ATOM 3892 CA THR A 516 49.996 10.713 -25.887 1.00 25.19 C
ANISOU 3892 CA THR A 516 3000 2170 4400 -400 -419 118 C
ATOM 3893 C THR A 516 49.549 12.046 -25.288 1.00 30.11 C
ANISOU 3893 C THR A 516 3676 2785 4981 -405 -588 135 C
ATOM 3894 O THR A 516 48.889 12.835 -25.981 1.00 30.97 O
ANISOU 3894 O THR A 516 3780 2960 5028 -461 -582 126 O
ATOM 3895 CB THR A 516 48.870 9.664 -25.832 1.00 30.67 C
ANISOU 3895 CB THR A 516 3795 2882 4977 -390 -285 32 C
ATOM 3896 OG1 THR A 516 48.834 8.939 -27.066 1.00 37.59 O
ANISOU 3896 OG1 THR A 516 4609 3823 5849 -439 -103 -3 O
ATOM 3897 CG2 THR A 516 47.505 10.280 -25.567 1.00 38.61 C
ANISOU 3897 CG2 THR A 516 4904 3925 5839 -408 -326 -13 C
ATOM 3898 N LEU A 517 49.958 12.352 -24.055 1.00 22.70 N
ANISOU 3898 N LEU A 517 2778 1767 4079 -348 -740 164 N
ATOM 3899 CA LEU A 517 49.389 13.461 -23.286 1.00 20.19 C
ANISOU 3899 CA LEU A 517 2537 1429 3704 -340 -896 160 C
ATOM 3900 C LEU A 517 50.129 14.775 -23.564 1.00 24.30 C
ANISOU 3900 C LEU A 517 2973 1944 4317 -379 -1023 226 C
ATOM 3901 O LEU A 517 50.727 15.395 -22.683 1.00 22.63 O
ANISOU 3901 O LEU A 517 2764 1669 4164 -351 -1182 261 O
ATOM 3902 CB LEU A 517 49.407 13.116 -21.802 1.00 20.32 C
ANISOU 3902 CB LEU A 517 2644 1371 3706 -260 -995 151 C
ATOM 3903 CG LEU A 517 48.923 11.698 -21.488 1.00 28.58 C
ANISOU 3903 CG LEU A 517 3757 2409 4692 -216 -868 103 C
ATOM 3904 CD1 LEU A 517 48.954 11.423 -19.995 1.00 25.71 C
ANISOU 3904 CD1 LEU A 517 3478 1979 4312 -135 -974 104 C
ATOM 3905 CD2 LEU A 517 47.529 11.481 -22.049 1.00 25.74 C
ANISOU 3905 CD2 LEU A 517 3468 2117 4195 -251 -751 32 C
ATOM 3906 N HIS A 518 50.049 15.213 -24.824 1.00 21.97 N
ANISOU 3906 N HIS A 518 2602 1720 4028 -449 -950 242 N
ATOM 3907 CA HIS A 518 50.732 16.435 -25.239 1.00 22.03 C
ANISOU 3907 CA HIS A 518 2519 1727 4125 -496 -1052 310 C
ATOM 3908 C HIS A 518 50.165 17.685 -24.574 1.00 24.86 C
ANISOU 3908 C HIS A 518 2952 2052 4443 -494 -1208 307 C
ATOM 3909 O HIS A 518 50.851 18.712 -24.526 1.00 21.21 O
ANISOU 3909 O HIS A 518 2433 1555 4070 -518 -1332 364 O
ATOM 3910 CB HIS A 518 50.651 16.602 -26.758 1.00 21.95 C
ANISOU 3910 CB HIS A 518 2414 1810 4114 -570 -930 328 C
ATOM 3911 CG HIS A 518 51.230 15.458 -27.530 1.00 32.30 C
ANISOU 3911 CG HIS A 518 3643 3160 5468 -576 -773 328 C
ATOM 3912 ND1 HIS A 518 51.036 15.308 -28.887 1.00 33.68 N
ANISOU 3912 ND1 HIS A 518 3743 3433 5619 -637 -631 324 N
ATOM 3913 CD2 HIS A 518 51.999 14.412 -27.143 1.00 34.56 C
ANISOU 3913 CD2 HIS A 518 3909 3402 5820 -528 -732 330 C
ATOM 3914 CE1 HIS A 518 51.657 14.218 -29.302 1.00 35.73 C
ANISOU 3914 CE1 HIS A 518 3943 3704 5927 -626 -509 317 C
ATOM 3915 NE2 HIS A 518 52.247 13.655 -28.263 1.00 34.50 N
ANISOU 3915 NE2 HIS A 518 3819 3460 5829 -559 -566 322 N
ATOM 3916 N ARG A 519 48.931 17.633 -24.077 1.00 22.00 N
ANISOU 3916 N ARG A 519 2714 1698 3948 -469 -1203 242 N
ATOM 3917 CA ARG A 519 48.294 18.792 -23.467 1.00 23.86 C
ANISOU 3917 CA ARG A 519 3027 1905 4135 -462 -1339 231 C
ATOM 3918 C ARG A 519 48.207 18.705 -21.952 1.00 21.77 C
ANISOU 3918 C ARG A 519 2865 1564 3842 -390 -1461 199 C
ATOM 3919 O ARG A 519 47.612 19.591 -21.328 1.00 21.34 O
ANISOU 3919 O ARG A 519 2880 1518 3709 -354 -1545 183 O
ATOM 3920 CB ARG A 519 46.891 18.991 -24.046 1.00 19.00 C
ANISOU 3920 CB ARG A 519 2470 1366 3382 -488 -1254 186 C
ATOM 3921 CG ARG A 519 46.875 19.740 -25.364 1.00 20.20 C
ANISOU 3921 CG ARG A 519 2530 1587 3559 -562 -1205 231 C
ATOM 3922 CD ARG A 519 45.688 19.331 -26.206 1.00 23.65 C
ANISOU 3922 CD ARG A 519 2993 2129 3864 -591 -1053 186 C
ATOM 3923 NE ARG A 519 45.738 17.910 -26.533 1.00 30.04 N
ANISOU 3923 NE ARG A 519 3789 2976 4649 -587 -899 148 N
ATOM 3924 CZ ARG A 519 46.427 17.397 -27.547 1.00 22.45 C
ANISOU 3924 CZ ARG A 519 2716 2062 3751 -628 -789 174 C
ATOM 3925 NH1 ARG A 519 47.129 18.188 -28.346 1.00 19.49 N
ANISOU 3925 NH1 ARG A 519 2229 1709 3465 -678 -815 244 N
ATOM 3926 NH2 ARG A 519 46.412 16.091 -27.765 1.00 22.67 N
ANISOU 3926 NH2 ARG A 519 2745 2114 3754 -620 -651 130 N
ATOM 3927 N LEU A 520 48.772 17.666 -21.345 1.00 20.16 N
ANISOU 3927 N LEU A 520 2663 1327 3668 -341 -1441 196 N
ATOM 3928 CA LEU A 520 48.749 17.547 -19.895 1.00 23.37 C
ANISOU 3928 CA LEU A 520 3161 1671 4049 -270 -1557 173 C
ATOM 3929 C LEU A 520 49.512 18.700 -19.257 1.00 25.68 C
ANISOU 3929 C LEU A 520 3419 1934 4403 -258 -1728 212 C
ATOM 3930 O LEU A 520 50.658 18.979 -19.621 1.00 22.46 O
ANISOU 3930 O LEU A 520 2905 1502 4128 -290 -1770 274 O
ATOM 3931 CB LEU A 520 49.354 16.209 -19.477 1.00 21.23 C
ANISOU 3931 CB LEU A 520 2876 1379 3812 -221 -1492 179 C
ATOM 3932 CG LEU A 520 49.250 15.817 -18.004 1.00 20.76 C
ANISOU 3932 CG LEU A 520 2910 1269 3708 -141 -1582 156 C
ATOM 3933 CD1 LEU A 520 47.798 15.574 -17.620 1.00 22.73 C
ANISOU 3933 CD1 LEU A 520 3290 1548 3799 -115 -1536 85 C
ATOM 3934 CD2 LEU A 520 50.109 14.593 -17.709 1.00 21.27 C
ANISOU 3934 CD2 LEU A 520 2932 1308 3842 -96 -1525 186 C
ATOM 3935 N GLN A 521 48.866 19.376 -18.308 1.00 20.96 N
ANISOU 3935 N GLN A 521 2909 1347 3707 -209 -1820 180 N
ATOM 3936 CA GLN A 521 49.477 20.489 -17.595 1.00 21.50 C
ANISOU 3936 CA GLN A 521 2966 1382 3821 -183 -1974 214 C
ATOM 3937 C GLN A 521 49.895 20.136 -16.174 1.00 26.13 C
ANISOU 3937 C GLN A 521 3596 1941 4390 -141 -2038 177 C
ATOM 3938 O GLN A 521 50.845 20.733 -15.656 1.00 22.78 O
ANISOU 3938 O GLN A 521 3155 1452 4046 -153 -2088 196 O
ATOM 3939 CB GLN A 521 48.519 21.685 -17.563 1.00 21.16 C
ANISOU 3939 CB GLN A 521 2996 1359 3686 -166 -1970 200 C
ATOM 3940 CG GLN A 521 48.111 22.169 -18.949 1.00 24.74 C
ANISOU 3940 CG GLN A 521 3400 1860 4142 -227 -1887 223 C
ATOM 3941 CD GLN A 521 47.390 23.504 -18.925 1.00 39.06 C
ANISOU 3941 CD GLN A 521 5268 3672 5902 -211 -1911 228 C
ATOM 3942 OE1 GLN A 521 46.853 23.917 -17.897 1.00 42.59 O
ANISOU 3942 OE1 GLN A 521 5805 4104 6273 -160 -1935 187 O
ATOM 3943 NE2 GLN A 521 47.377 24.188 -20.062 1.00 38.69 N
ANISOU 3943 NE2 GLN A 521 5157 3654 5889 -269 -1869 265 N
ATOM 3944 N LEU A 522 49.220 19.186 -15.531 1.00 22.31 N
ANISOU 3944 N LEU A 522 3189 1473 3815 -104 -2019 121 N
ATOM 3945 CA LEU A 522 49.598 18.742 -14.199 1.00 24.85 C
ANISOU 3945 CA LEU A 522 3557 1761 4124 -76 -2068 81 C
ATOM 3946 C LEU A 522 49.694 17.223 -14.176 1.00 23.16 C
ANISOU 3946 C LEU A 522 3340 1549 3912 -32 -1990 98 C
ATOM 3947 O LEU A 522 48.861 16.527 -14.766 1.00 21.20 O
ANISOU 3947 O LEU A 522 3130 1325 3602 -18 -1866 88 O
ATOM 3948 CB LEU A 522 48.598 19.226 -13.139 1.00 27.48 C
ANISOU 3948 CB LEU A 522 4013 2109 4319 -33 -2047 17 C
ATOM 3949 CG LEU A 522 48.944 18.847 -11.696 1.00 32.24 C
ANISOU 3949 CG LEU A 522 4669 2673 4906 5 -2104 -18 C
ATOM 3950 CD1 LEU A 522 48.705 20.005 -10.745 1.00 35.32 C
ANISOU 3950 CD1 LEU A 522 5124 3039 5257 30 -2126 -44 C
ATOM 3951 CD2 LEU A 522 48.146 17.638 -11.251 1.00 32.69 C
ANISOU 3951 CD2 LEU A 522 4795 2764 4861 50 -2064 -57 C
ATOM 3952 N LEU A 523 50.721 16.719 -13.493 1.00 24.10 N
ANISOU 3952 N LEU A 523 3418 1640 4099 -8 -2023 125 N
ATOM 3953 CA LEU A 523 50.912 15.285 -13.288 1.00 27.33 C
ANISOU 3953 CA LEU A 523 3826 2048 4510 51 -1928 150 C
ATOM 3954 C LEU A 523 51.370 15.078 -11.850 1.00 31.29 C
ANISOU 3954 C LEU A 523 4354 2547 4986 94 -2003 139 C
ATOM 3955 O LEU A 523 52.514 15.397 -11.509 1.00 34.84 O
ANISOU 3955 O LEU A 523 4736 2974 5528 80 -2079 174 O
ATOM 3956 CB LEU A 523 51.929 14.715 -14.279 1.00 23.09 C
ANISOU 3956 CB LEU A 523 3175 1482 4118 37 -1859 226 C
ATOM 3957 CG LEU A 523 52.320 13.241 -14.123 1.00 23.35 C
ANISOU 3957 CG LEU A 523 3192 1496 4183 96 -1755 257 C
ATOM 3958 CD1 LEU A 523 51.098 12.340 -14.169 1.00 22.57 C
ANISOU 3958 CD1 LEU A 523 3195 1405 3974 127 -1629 209 C
ATOM 3959 CD2 LEU A 523 53.326 12.825 -15.186 1.00 25.55 C
ANISOU 3959 CD2 LEU A 523 3352 1741 4616 76 -1686 327 C
ATOM 3960 N ASN A 524 50.481 14.554 -11.003 1.00 30.39 N
ANISOU 3960 N ASN A 524 4341 2457 4749 143 -1976 92 N
ATOM 3961 CA ASN A 524 50.780 14.319 -9.592 1.00 31.08 C
ANISOU 3961 CA ASN A 524 4464 2547 4800 187 -2033 79 C
ATOM 3962 C ASN A 524 50.989 12.823 -9.372 1.00 30.21 C
ANISOU 3962 C ASN A 524 4343 2442 4695 253 -1939 125 C
ATOM 3963 O ASN A 524 50.039 12.035 -9.448 1.00 23.16 O
ANISOU 3963 O ASN A 524 3517 1563 3721 285 -1842 106 O
ATOM 3964 CB ASN A 524 49.662 14.856 -8.699 1.00 30.08 C
ANISOU 3964 CB ASN A 524 4455 2437 4538 196 -2068 -3 C
ATOM 3965 CG ASN A 524 50.059 14.914 -7.228 1.00 40.56 C
ANISOU 3965 CG ASN A 524 5814 3758 5840 231 -2136 -19 C
ATOM 3966 OD1 ASN A 524 51.055 14.317 -6.815 1.00 28.24 O
ANISOU 3966 OD1 ASN A 524 4192 2197 4340 259 -2150 36 O
ATOM 3967 ND2 ASN A 524 49.281 15.638 -6.432 1.00 54.39 N
ANISOU 3967 ND2 ASN A 524 7659 5502 7506 235 -2170 -89 N
ATOM 3968 N MET A 525 52.238 12.438 -9.107 1.00 24.67 N
ANISOU 3968 N MET A 525 3559 1723 4092 271 -1961 187 N
ATOM 3969 CA MET A 525 52.594 11.077 -8.726 1.00 26.62 C
ANISOU 3969 CA MET A 525 3791 1966 4356 340 -1883 236 C
ATOM 3970 C MET A 525 53.294 11.059 -7.371 1.00 35.08 C
ANISOU 3970 C MET A 525 4857 3054 5420 376 -1969 254 C
ATOM 3971 O MET A 525 54.142 10.203 -7.105 1.00 39.15 O
ANISOU 3971 O MET A 525 5314 3562 5997 422 -1940 319 O
ATOM 3972 CB MET A 525 53.471 10.419 -9.789 1.00 28.13 C
ANISOU 3972 CB MET A 525 3881 2123 4685 339 -1799 306 C
ATOM 3973 CG MET A 525 52.735 10.074 -11.072 1.00 33.08 C
ANISOU 3973 CG MET A 525 4524 2729 5318 316 -1673 290 C
ATOM 3974 SD MET A 525 53.734 9.079 -12.193 1.00 48.11 S
ANISOU 3974 SD MET A 525 6316 4581 7384 324 -1546 363 S
ATOM 3975 CE MET A 525 55.096 10.193 -12.531 1.00 38.03 C
ANISOU 3975 CE MET A 525 4907 3307 6236 271 -1673 416 C
ATOM 3976 N SER A 526 52.945 12.005 -6.505 1.00 28.07 N
ANISOU 3976 N SER A 526 4027 2182 4455 357 -2069 195 N
ATOM 3977 CA SER A 526 53.513 12.051 -5.170 1.00 32.30 C
ANISOU 3977 CA SER A 526 4566 2735 4972 390 -2146 203 C
ATOM 3978 C SER A 526 52.898 10.968 -4.289 1.00 31.85 C
ANISOU 3978 C SER A 526 4573 2708 4821 464 -2085 207 C
ATOM 3979 O SER A 526 51.817 10.440 -4.567 1.00 31.54 O
ANISOU 3979 O SER A 526 4600 2676 4707 481 -2001 180 O
ATOM 3980 CB SER A 526 53.291 13.423 -4.537 1.00 34.23 C
ANISOU 3980 CB SER A 526 4862 2971 5172 347 -2253 132 C
ATOM 3981 OG SER A 526 51.927 13.615 -4.201 1.00 36.09 O
ANISOU 3981 OG SER A 526 5208 3221 5283 356 -2229 58 O
ATOM 3982 N HIS A 527 53.610 10.646 -3.209 1.00 31.13 N
ANISOU 3982 N HIS A 527 4458 2637 4733 508 -2129 245 N
ATOM 3983 CA HIS A 527 53.150 9.675 -2.215 1.00 29.69 C
ANISOU 3983 CA HIS A 527 4327 2488 4466 580 -2085 260 C
ATOM 3984 C HIS A 527 52.908 8.300 -2.835 1.00 28.47 C
ANISOU 3984 C HIS A 527 4166 2317 4334 626 -1947 312 C
ATOM 3985 O HIS A 527 51.946 7.607 -2.499 1.00 27.15 O
ANISOU 3985 O HIS A 527 4073 2163 4080 663 -1878 298 O
ATOM 3986 CB HIS A 527 51.904 10.182 -1.484 1.00 31.57 C
ANISOU 3986 CB HIS A 527 4677 2752 4568 577 -2107 174 C
ATOM 3987 CG HIS A 527 52.137 11.440 -0.707 1.00 35.39 C
ANISOU 3987 CG HIS A 527 5176 3238 5033 546 -2223 122 C
ATOM 3988 ND1 HIS A 527 52.648 11.439 0.573 1.00 38.62 N
ANISOU 3988 ND1 HIS A 527 5579 3679 5417 583 -2285 139 N
ATOM 3989 CD2 HIS A 527 51.934 12.739 -1.030 1.00 33.76 C
ANISOU 3989 CD2 HIS A 527 4993 3001 4834 485 -2282 58 C
ATOM 3990 CE1 HIS A 527 52.746 12.683 1.006 1.00 36.79 C
ANISOU 3990 CE1 HIS A 527 5368 3432 5178 545 -2374 83 C
ATOM 3991 NE2 HIS A 527 52.320 13.491 0.053 1.00 36.04 N
ANISOU 3991 NE2 HIS A 527 5293 3293 5107 487 -2371 34 N
ATOM 3992 N ASN A 528 53.787 7.909 -3.751 1.00 27.85 N
ANISOU 3992 N ASN A 528 4000 2203 4378 622 -1901 373 N
ATOM 3993 CA ASN A 528 53.876 6.539 -4.242 1.00 29.22 C
ANISOU 3993 CA ASN A 528 4153 2345 4603 674 -1764 433 C
ATOM 3994 C ASN A 528 55.201 5.930 -3.768 1.00 32.00 C
ANISOU 3994 C ASN A 528 4417 2697 5044 725 -1774 524 C
ATOM 3995 O ASN A 528 55.868 6.459 -2.874 1.00 38.37 O
ANISOU 3995 O ASN A 528 5195 3541 5845 728 -1885 537 O
ATOM 3996 CB ASN A 528 53.726 6.491 -5.765 1.00 29.71 C
ANISOU 3996 CB ASN A 528 4190 2361 4737 631 -1677 424 C
ATOM 3997 CG ASN A 528 52.302 6.772 -6.219 1.00 32.21 C
ANISOU 3997 CG ASN A 528 4602 2681 4956 597 -1635 346 C
ATOM 3998 OD1 ASN A 528 51.409 5.949 -6.034 1.00 29.29 O
ANISOU 3998 OD1 ASN A 528 4305 2308 4514 631 -1544 333 O
ATOM 3999 ND2 ASN A 528 52.088 7.937 -6.822 1.00 31.84 N
ANISOU 3999 ND2 ASN A 528 4553 2641 4905 528 -1699 297 N
ATOM 4000 N ASN A 529 55.583 4.808 -4.374 1.00 29.27 N
ANISOU 4000 N ASN A 529 4030 2309 4782 766 -1653 585 N
ATOM 4001 CA ASN A 529 56.795 4.079 -4.014 1.00 31.86 C
ANISOU 4001 CA ASN A 529 4274 2633 5196 826 -1640 677 C
ATOM 4002 C ASN A 529 57.714 3.912 -5.219 1.00 36.53 C
ANISOU 4002 C ASN A 529 4767 3180 5933 807 -1585 718 C
ATOM 4003 O ASN A 529 58.305 2.851 -5.429 1.00 41.41 O
ANISOU 4003 O ASN A 529 5339 3766 6630 862 -1488 784 O
ATOM 4004 CB ASN A 529 56.456 2.715 -3.415 1.00 31.47 C
ANISOU 4004 CB ASN A 529 4269 2573 5114 911 -1533 723 C
ATOM 4005 CG ASN A 529 55.697 2.820 -2.108 1.00 33.89 C
ANISOU 4005 CG ASN A 529 4656 2934 5286 936 -1591 699 C
ATOM 4006 OD1 ASN A 529 56.030 3.631 -1.245 1.00 39.19 O
ANISOU 4006 OD1 ASN A 529 5315 3659 5915 924 -1720 688 O
ATOM 4007 ND2 ASN A 529 54.672 1.992 -1.954 1.00 30.18 N
ANISOU 4007 ND2 ASN A 529 4267 2448 4752 969 -1491 689 N
ATOM 4008 N LEU A 530 57.829 4.959 -6.034 1.00 33.62 N
ANISOU 4008 N LEU A 530 4363 2808 5602 728 -1643 680 N
ATOM 4009 CA LEU A 530 58.661 4.899 -7.230 1.00 31.09 C
ANISOU 4009 CA LEU A 530 3941 2451 5420 702 -1594 718 C
ATOM 4010 C LEU A 530 60.121 4.663 -6.863 1.00 31.70 C
ANISOU 4010 C LEU A 530 3910 2543 5592 737 -1634 804 C
ATOM 4011 O LEU A 530 60.699 5.392 -6.051 1.00 34.65 O
ANISOU 4011 O LEU A 530 4257 2962 5948 724 -1766 813 O
ATOM 4012 CB LEU A 530 58.521 6.192 -8.036 1.00 29.85 C
ANISOU 4012 CB LEU A 530 3765 2297 5279 609 -1667 668 C
ATOM 4013 CG LEU A 530 57.120 6.457 -8.593 1.00 34.96 C
ANISOU 4013 CG LEU A 530 4509 2932 5842 571 -1619 587 C
ATOM 4014 CD1 LEU A 530 57.030 7.839 -9.227 1.00 28.17 C
ANISOU 4014 CD1 LEU A 530 3629 2082 4992 483 -1709 545 C
ATOM 4015 CD2 LEU A 530 56.732 5.375 -9.587 1.00 29.33 C
ANISOU 4015 CD2 LEU A 530 3803 2166 5174 590 -1444 592 C
ATOM 4016 N LEU A 531 60.714 3.631 -7.463 1.00 32.15 N
ANISOU 4016 N LEU A 531 3904 2561 5750 781 -1515 863 N
ATOM 4017 CA LEU A 531 62.102 3.263 -7.209 1.00 36.17 C
ANISOU 4017 CA LEU A 531 4305 3083 6354 822 -1533 951 C
ATOM 4018 C LEU A 531 63.065 3.828 -8.240 1.00 36.08 C
ANISOU 4018 C LEU A 531 4172 3066 6472 767 -1553 979 C
ATOM 4019 O LEU A 531 64.207 4.152 -7.897 1.00 40.40 O
ANISOU 4019 O LEU A 531 4628 3646 7074 767 -1636 1035 O
ATOM 4020 CB LEU A 531 62.241 1.737 -7.176 1.00 35.27 C
ANISOU 4020 CB LEU A 531 4193 2931 6278 912 -1385 1004 C
ATOM 4021 CG LEU A 531 61.294 1.012 -6.220 1.00 38.00 C
ANISOU 4021 CG LEU A 531 4656 3277 6507 972 -1343 988 C
ATOM 4022 CD1 LEU A 531 61.292 -0.486 -6.504 1.00 33.99 C
ANISOU 4022 CD1 LEU A 531 4158 2709 6049 1044 -1172 1027 C
ATOM 4023 CD2 LEU A 531 61.679 1.304 -4.776 1.00 34.41 C
ANISOU 4023 CD2 LEU A 531 4204 2890 5982 1008 -1470 1021 C
ATOM 4024 N PHE A 532 62.628 3.938 -9.490 1.00 34.72 N
ANISOU 4024 N PHE A 532 3992 2854 6346 719 -1474 944 N
ATOM 4025 CA PHE A 532 63.398 4.584 -10.540 1.00 33.06 C
ANISOU 4025 CA PHE A 532 3669 2642 6252 658 -1493 968 C
ATOM 4026 C PHE A 532 62.432 5.273 -11.487 1.00 34.08 C
ANISOU 4026 C PHE A 532 3841 2751 6356 585 -1477 897 C
ATOM 4027 O PHE A 532 61.246 4.938 -11.549 1.00 36.26 O
ANISOU 4027 O PHE A 532 4223 3004 6549 591 -1406 837 O
ATOM 4028 CB PHE A 532 64.265 3.590 -11.326 1.00 46.65 C
ANISOU 4028 CB PHE A 532 5286 4331 8107 701 -1362 1035 C
ATOM 4029 CG PHE A 532 65.451 3.076 -10.565 1.00 60.34 C
ANISOU 4029 CG PHE A 532 6948 6092 9888 764 -1389 1118 C
ATOM 4030 CD1 PHE A 532 66.630 3.804 -10.516 1.00 60.02 C
ANISOU 4030 CD1 PHE A 532 6796 6093 9915 731 -1497 1171 C
ATOM 4031 CD2 PHE A 532 65.396 1.855 -9.912 1.00 64.72 C
ANISOU 4031 CD2 PHE A 532 7545 6630 10417 855 -1304 1147 C
ATOM 4032 CE1 PHE A 532 67.729 3.331 -9.817 1.00 56.53 C
ANISOU 4032 CE1 PHE A 532 6286 5681 9512 789 -1521 1249 C
ATOM 4033 CE2 PHE A 532 66.490 1.374 -9.213 1.00 61.13 C
ANISOU 4033 CE2 PHE A 532 7021 6202 10002 917 -1328 1228 C
ATOM 4034 CZ PHE A 532 67.659 2.114 -9.167 1.00 59.23 C
ANISOU 4034 CZ PHE A 532 6670 6010 9827 885 -1437 1279 C
ATOM 4035 N LEU A 533 62.953 6.242 -12.226 1.00 35.99 N
ANISOU 4035 N LEU A 533 3998 3004 6671 513 -1541 907 N
ATOM 4036 CA LEU A 533 62.245 6.828 -13.350 1.00 31.70 C
ANISOU 4036 CA LEU A 533 3466 2442 6137 446 -1508 861 C
ATOM 4037 C LEU A 533 62.965 6.459 -14.639 1.00 33.46 C
ANISOU 4037 C LEU A 533 3564 2642 6507 437 -1402 912 C
ATOM 4038 O LEU A 533 64.150 6.113 -14.638 1.00 37.19 O
ANISOU 4038 O LEU A 533 3929 3124 7077 465 -1397 985 O
ATOM 4039 CB LEU A 533 62.147 8.351 -13.217 1.00 30.83 C
ANISOU 4039 CB LEU A 533 3363 2364 5988 364 -1665 828 C
ATOM 4040 CG LEU A 533 61.342 8.911 -12.043 1.00 36.76 C
ANISOU 4040 CG LEU A 533 4236 3138 6592 361 -1768 763 C
ATOM 4041 CD1 LEU A 533 61.361 10.434 -12.057 1.00 30.30 C
ANISOU 4041 CD1 LEU A 533 3414 2338 5761 275 -1907 731 C
ATOM 4042 CD2 LEU A 533 59.913 8.391 -12.058 1.00 35.33 C
ANISOU 4042 CD2 LEU A 533 4182 2940 6302 386 -1679 696 C
ATOM 4043 N ASP A 534 62.230 6.520 -15.743 1.00 37.03 N
ANISOU 4043 N ASP A 534 4032 3066 6973 398 -1312 873 N
ATOM 4044 CA ASP A 534 62.800 6.347 -17.070 1.00 46.46 C
ANISOU 4044 CA ASP A 534 5115 4278 8261 358 -1189 892 C
ATOM 4045 C ASP A 534 62.735 7.675 -17.812 1.00 43.53 C
ANISOU 4045 C ASP A 534 4702 3949 7887 257 -1262 876 C
ATOM 4046 O ASP A 534 61.761 8.424 -17.682 1.00 44.27 O
ANISOU 4046 O ASP A 534 4889 4051 7882 213 -1322 815 O
ATOM 4047 CB ASP A 534 62.067 5.254 -17.857 1.00 47.35 C
ANISOU 4047 CB ASP A 534 5275 4379 8336 364 -969 830 C
ATOM 4048 CG ASP A 534 62.839 4.797 -19.088 1.00 61.69 C
ANISOU 4048 CG ASP A 534 6967 6215 10255 346 -825 855 C
ATOM 4049 OD1 ASP A 534 63.889 5.398 -19.398 1.00 69.50 O
ANISOU 4049 OD1 ASP A 534 7833 7233 11340 323 -896 922 O
ATOM 4050 OD2 ASP A 534 62.394 3.830 -19.745 1.00 68.26 O
ANISOU 4050 OD2 ASP A 534 7826 7037 11072 354 -641 806 O
ATOM 4051 N SER A 535 63.782 7.965 -18.587 1.00 43.95 N
ANISOU 4051 N SER A 535 4614 4030 8053 223 -1255 936 N
ATOM 4052 CA SER A 535 63.872 9.248 -19.272 1.00 48.66 C
ANISOU 4052 CA SER A 535 5157 4666 8667 129 -1332 938 C
ATOM 4053 C SER A 535 62.888 9.364 -20.431 1.00 47.36 C
ANISOU 4053 C SER A 535 5030 4535 8430 62 -1200 865 C
ATOM 4054 O SER A 535 62.603 10.481 -20.875 1.00 48.76 O
ANISOU 4054 O SER A 535 5201 4740 8587 -15 -1267 853 O
ATOM 4055 CB SER A 535 65.301 9.468 -19.771 1.00 56.84 C
ANISOU 4055 CB SER A 535 6024 5728 9845 113 -1356 1030 C
ATOM 4056 OG SER A 535 65.475 10.785 -20.262 1.00 64.92 O
ANISOU 4056 OG SER A 535 6992 6782 10892 23 -1457 1046 O
ATOM 4057 N SER A 536 62.352 8.244 -20.918 1.00 48.59 N
ANISOU 4057 N SER A 536 5226 4689 8548 88 -1015 817 N
ATOM 4058 CA SER A 536 61.492 8.265 -22.095 1.00 50.62 C
ANISOU 4058 CA SER A 536 5505 4989 8740 22 -878 748 C
ATOM 4059 C SER A 536 60.070 8.719 -21.789 1.00 44.50 C
ANISOU 4059 C SER A 536 4871 4214 7822 -5 -909 668 C
ATOM 4060 O SER A 536 59.378 9.196 -22.695 1.00 48.53 O
ANISOU 4060 O SER A 536 5390 4773 8275 -76 -853 624 O
ATOM 4061 CB SER A 536 61.459 6.878 -22.742 1.00 58.93 C
ANISOU 4061 CB SER A 536 6546 6040 9805 56 -665 719 C
ATOM 4062 OG SER A 536 60.809 5.933 -21.908 1.00 68.02 O
ANISOU 4062 OG SER A 536 7812 7137 10893 124 -621 678 O
ATOM 4063 N HIS A 537 59.625 8.592 -20.537 1.00 40.17 N
ANISOU 4063 N HIS A 537 4429 3621 7214 50 -999 652 N
ATOM 4064 CA HIS A 537 58.242 8.885 -20.176 1.00 46.54 C
ANISOU 4064 CA HIS A 537 5375 4429 7880 36 -1017 575 C
ATOM 4065 C HIS A 537 57.897 10.367 -20.252 1.00 50.46 C
ANISOU 4065 C HIS A 537 5882 4949 8340 -31 -1154 568 C
ATOM 4066 O HIS A 537 56.708 10.706 -20.238 1.00 57.74 O
ANISOU 4066 O HIS A 537 6905 5886 9146 -56 -1149 502 O
ATOM 4067 CB HIS A 537 57.954 8.371 -18.764 1.00 47.37 C
ANISOU 4067 CB HIS A 537 5581 4482 7934 118 -1084 569 C
ATOM 4068 CG HIS A 537 58.155 6.897 -18.599 1.00 49.81 C
ANISOU 4068 CG HIS A 537 5896 4758 8271 189 -949 576 C
ATOM 4069 ND1 HIS A 537 58.529 6.329 -17.400 1.00 51.75 N
ANISOU 4069 ND1 HIS A 537 6170 4958 8535 275 -1012 616 N
ATOM 4070 CD2 HIS A 537 58.024 5.872 -19.475 1.00 51.67 C
ANISOU 4070 CD2 HIS A 537 6114 4998 8521 187 -754 547 C
ATOM 4071 CE1 HIS A 537 58.627 5.020 -17.546 1.00 53.49 C
ANISOU 4071 CE1 HIS A 537 6389 5150 8784 325 -860 617 C
ATOM 4072 NE2 HIS A 537 58.325 4.717 -18.796 1.00 52.91 N
ANISOU 4072 NE2 HIS A 537 6290 5102 8710 272 -701 571 N
ATOM 4073 N TYR A 538 58.888 11.253 -20.344 1.00 49.12 N
ANISOU 4073 N TYR A 538 5611 4784 8269 -62 -1271 634 N
ATOM 4074 CA TYR A 538 58.655 12.687 -20.222 1.00 40.48 C
ANISOU 4074 CA TYR A 538 4531 3695 7155 -118 -1422 634 C
ATOM 4075 C TYR A 538 59.085 13.467 -21.459 1.00 36.40 C
ANISOU 4075 C TYR A 538 3902 3223 6705 -202 -1401 670 C
ATOM 4076 O TYR A 538 59.182 14.698 -21.398 1.00 45.44 O
ANISOU 4076 O TYR A 538 5031 4364 7869 -250 -1534 690 O
ATOM 4077 CB TYR A 538 59.371 13.222 -18.977 1.00 43.73 C
ANISOU 4077 CB TYR A 538 4939 4061 7614 -83 -1618 677 C
ATOM 4078 CG TYR A 538 59.064 12.419 -17.731 1.00 47.14 C
ANISOU 4078 CG TYR A 538 5469 4456 7985 4 -1642 655 C
ATOM 4079 CD1 TYR A 538 59.807 11.291 -17.407 1.00 56.96 C
ANISOU 4079 CD1 TYR A 538 6669 5684 9290 73 -1582 698 C
ATOM 4080 CD2 TYR A 538 58.023 12.779 -16.888 1.00 49.17 C
ANISOU 4080 CD2 TYR A 538 5860 4698 8124 22 -1718 594 C
ATOM 4081 CE1 TYR A 538 59.526 10.545 -16.272 1.00 64.53 C
ANISOU 4081 CE1 TYR A 538 7713 6612 10195 154 -1601 686 C
ATOM 4082 CE2 TYR A 538 57.734 12.040 -15.749 1.00 56.24 C
ANISOU 4082 CE2 TYR A 538 6841 5579 8948 97 -1728 572 C
ATOM 4083 CZ TYR A 538 58.489 10.924 -15.446 1.00 66.22 C
ANISOU 4083 CZ TYR A 538 8058 6831 10272 160 -1667 618 C
ATOM 4084 OH TYR A 538 58.207 10.187 -14.316 1.00 69.68 O
ANISOU 4084 OH TYR A 538 8577 7275 10625 227 -1660 596 O
ATOM 4085 N ASN A 539 59.322 12.789 -22.581 1.00 34.57 N
ANISOU 4085 N ASN A 539 3593 3036 6508 -221 -1235 677 N
ATOM 4086 CA ASN A 539 59.797 13.442 -23.793 1.00 39.17 C
ANISOU 4086 CA ASN A 539 4057 3671 7155 -297 -1204 718 C
ATOM 4087 C ASN A 539 58.685 14.080 -24.619 1.00 36.06 C
ANISOU 4087 C ASN A 539 3708 3329 6667 -365 -1154 669 C
ATOM 4088 O ASN A 539 58.987 14.774 -25.597 1.00 38.46 O
ANISOU 4088 O ASN A 539 3917 3680 7014 -432 -1142 708 O
ATOM 4089 CB ASN A 539 60.559 12.436 -24.659 1.00 45.90 C
ANISOU 4089 CB ASN A 539 4801 4557 8082 -285 -1045 746 C
ATOM 4090 CG ASN A 539 61.775 11.859 -23.956 1.00 53.84 C
ANISOU 4090 CG ASN A 539 5742 5520 9196 -219 -1092 810 C
ATOM 4091 OD1 ASN A 539 62.119 10.693 -24.145 1.00 66.89 O
ANISOU 4091 OD1 ASN A 539 7366 7170 10880 -170 -963 810 O
ATOM 4092 ND2 ASN A 539 62.434 12.677 -23.142 1.00 52.89 N
ANISOU 4092 ND2 ASN A 539 5594 5367 9133 -217 -1277 865 N
ATOM 4093 N GLN A 540 57.413 13.865 -24.263 1.00 35.14 N
ANISOU 4093 N GLN A 540 3726 3208 6419 -348 -1122 590 N
ATOM 4094 CA GLN A 540 56.294 14.395 -25.037 1.00 32.83 C
ANISOU 4094 CA GLN A 540 3477 2971 6028 -408 -1065 543 C
ATOM 4095 C GLN A 540 55.270 15.102 -24.156 1.00 33.48 C
ANISOU 4095 C GLN A 540 3691 3022 6009 -397 -1181 498 C
ATOM 4096 O GLN A 540 54.126 15.304 -24.581 1.00 31.81 O
ANISOU 4096 O GLN A 540 3545 2853 5688 -426 -1122 445 O
ATOM 4097 CB GLN A 540 55.615 13.289 -25.848 1.00 26.73 C
ANISOU 4097 CB GLN A 540 2723 2252 5180 -411 -858 482 C
ATOM 4098 CG GLN A 540 56.525 12.637 -26.870 1.00 34.10 C
ANISOU 4098 CG GLN A 540 3526 3227 6203 -426 -729 516 C
ATOM 4099 CD GLN A 540 55.759 11.962 -27.989 1.00 38.58 C
ANISOU 4099 CD GLN A 540 4098 3871 6690 -462 -534 453 C
ATOM 4100 OE1 GLN A 540 54.901 12.570 -28.629 1.00 47.21 O
ANISOU 4100 OE1 GLN A 540 5211 5026 7699 -520 -510 426 O
ATOM 4101 NE2 GLN A 540 56.070 10.694 -28.233 1.00 31.37 N
ANISOU 4101 NE2 GLN A 540 3163 2954 5802 -428 -392 429 N
ATOM 4102 N LEU A 541 55.656 15.492 -22.942 1.00 31.88 N
ANISOU 4102 N LEU A 541 3525 2751 5836 -356 -1344 517 N
ATOM 4103 CA LEU A 541 54.798 16.303 -22.080 1.00 29.82 C
ANISOU 4103 CA LEU A 541 3381 2459 5491 -346 -1470 476 C
ATOM 4104 C LEU A 541 55.044 17.780 -22.406 1.00 28.41 C
ANISOU 4104 C LEU A 541 3152 2277 5365 -410 -1591 518 C
ATOM 4105 O LEU A 541 55.579 18.559 -21.613 1.00 24.46 O
ANISOU 4105 O LEU A 541 2650 1722 4921 -404 -1758 545 O
ATOM 4106 CB LEU A 541 55.049 15.969 -20.615 1.00 28.27 C
ANISOU 4106 CB LEU A 541 3252 2198 5293 -270 -1581 470 C
ATOM 4107 CG LEU A 541 54.689 14.523 -20.247 1.00 31.04 C
ANISOU 4107 CG LEU A 541 3663 2547 5585 -205 -1460 431 C
ATOM 4108 CD1 LEU A 541 54.951 14.212 -18.783 1.00 33.38 C
ANISOU 4108 CD1 LEU A 541 4020 2786 5877 -127 -1573 434 C
ATOM 4109 CD2 LEU A 541 53.235 14.226 -20.594 1.00 22.79 C
ANISOU 4109 CD2 LEU A 541 2719 1541 4398 -215 -1347 354 C
ATOM 4110 N TYR A 542 54.630 18.156 -23.621 1.00 25.96 N
ANISOU 4110 N TYR A 542 2798 2029 5035 -473 -1501 522 N
ATOM 4111 CA TYR A 542 54.933 19.486 -24.144 1.00 32.33 C
ANISOU 4111 CA TYR A 542 3541 2846 5896 -532 -1582 575 C
ATOM 4112 C TYR A 542 54.296 20.588 -23.305 1.00 34.06 C
ANISOU 4112 C TYR A 542 3871 3042 6029 -495 -1703 548 C
ATOM 4113 O TYR A 542 54.851 21.688 -23.199 1.00 32.23 O
ANISOU 4113 O TYR A 542 3618 2792 5835 -492 -1790 597 O
ATOM 4114 CB TYR A 542 54.467 19.595 -25.598 1.00 31.56 C
ANISOU 4114 CB TYR A 542 3389 2841 5760 -589 -1438 581 C
ATOM 4115 CG TYR A 542 55.067 18.577 -26.553 1.00 32.68 C
ANISOU 4115 CG TYR A 542 3421 3034 5963 -614 -1288 604 C
ATOM 4116 CD1 TYR A 542 56.381 18.689 -26.989 1.00 37.23 C
ANISOU 4116 CD1 TYR A 542 3861 3614 6670 -634 -1302 683 C
ATOM 4117 CD2 TYR A 542 54.306 17.523 -27.044 1.00 28.49 C
ANISOU 4117 CD2 TYR A 542 2930 2560 5336 -602 -1117 541 C
ATOM 4118 CE1 TYR A 542 56.927 17.768 -27.872 1.00 38.69 C
ANISOU 4118 CE1 TYR A 542 3947 3854 6898 -644 -1155 699 C
ATOM 4119 CE2 TYR A 542 54.843 16.597 -27.924 1.00 32.33 C
ANISOU 4119 CE2 TYR A 542 3324 3098 5860 -612 -967 552 C
ATOM 4120 CZ TYR A 542 56.153 16.724 -28.335 1.00 39.62 C
ANISOU 4120 CZ TYR A 542 4111 4023 6918 -630 -985 631 C
ATOM 4121 OH TYR A 542 56.692 15.809 -29.212 1.00 47.84 O
ANISOU 4121 OH TYR A 542 5060 5118 7998 -635 -833 638 O
ATOM 4122 N SER A 543 53.143 20.317 -22.703 1.00 31.22 N
ANISOU 4122 N SER A 543 3636 2675 5551 -463 -1699 474 N
ATOM 4123 CA SER A 543 52.391 21.324 -21.973 1.00 27.52 C
ANISOU 4123 CA SER A 543 3273 2196 4988 -424 -1790 444 C
ATOM 4124 C SER A 543 52.604 21.250 -20.468 1.00 26.85 C
ANISOU 4124 C SER A 543 3262 2043 4895 -356 -1920 421 C
ATOM 4125 O SER A 543 52.055 22.083 -19.739 1.00 26.21 O
ANISOU 4125 O SER A 543 3274 1943 4742 -315 -1994 399 O
ATOM 4126 CB SER A 543 50.897 21.191 -22.293 1.00 24.71 C
ANISOU 4126 CB SER A 543 3006 1892 4490 -428 -1699 380 C
ATOM 4127 OG SER A 543 50.670 21.232 -23.692 1.00 24.46 O
ANISOU 4127 OG SER A 543 2904 1929 4461 -494 -1578 401 O
ATOM 4128 N LEU A 544 53.403 20.296 -19.988 1.00 25.61 N
ANISOU 4128 N LEU A 544 3067 1846 4816 -343 -1945 431 N
ATOM 4129 CA LEU A 544 53.473 20.027 -18.557 1.00 25.84 C
ANISOU 4129 CA LEU A 544 3171 1824 4821 -280 -2058 400 C
ATOM 4130 C LEU A 544 54.031 21.225 -17.807 1.00 24.45 C
ANISOU 4130 C LEU A 544 3031 1601 4658 -277 -2138 409 C
ATOM 4131 O LEU A 544 55.168 21.643 -18.041 1.00 26.97 O
ANISOU 4131 O LEU A 544 3268 1883 5095 -310 -2174 470 O
ATOM 4132 CB LEU A 544 54.330 18.793 -18.288 1.00 26.25 C
ANISOU 4132 CB LEU A 544 3174 1841 4960 -262 -2032 423 C
ATOM 4133 CG LEU A 544 54.151 18.236 -16.876 1.00 30.78 C
ANISOU 4133 CG LEU A 544 3836 2413 5446 -195 -2071 368 C
ATOM 4134 CD1 LEU A 544 52.731 17.711 -16.687 1.00 23.31 C
ANISOU 4134 CD1 LEU A 544 3013 1495 4347 -154 -1988 300 C
ATOM 4135 CD2 LEU A 544 55.176 17.154 -16.590 1.00 24.88 C
ANISOU 4135 CD2 LEU A 544 3024 1653 4775 -151 -2035 416 C
ATOM 4136 N LYS A 545 53.223 21.768 -16.898 1.00 24.22 N
ANISOU 4136 N LYS A 545 3122 1570 4509 -243 -2158 342 N
ATOM 4137 CA LYS A 545 53.627 22.880 -16.048 1.00 25.49 C
ANISOU 4137 CA LYS A 545 3325 1683 4676 -241 -2230 332 C
ATOM 4138 C LYS A 545 54.015 22.455 -14.642 1.00 30.49 C
ANISOU 4138 C LYS A 545 4010 2275 5299 -218 -2295 285 C
ATOM 4139 O LYS A 545 54.885 23.089 -14.037 1.00 29.80 O
ANISOU 4139 O LYS A 545 3913 2134 5276 -228 -2373 301 O
ATOM 4140 CB LYS A 545 52.500 23.914 -15.948 1.00 24.47 C
ANISOU 4140 CB LYS A 545 3283 1576 4437 -218 -2213 295 C
ATOM 4141 CG LYS A 545 52.040 24.495 -17.270 1.00 28.25 C
ANISOU 4141 CG LYS A 545 3718 2096 4921 -245 -2166 339 C
ATOM 4142 CD LYS A 545 50.941 25.521 -17.039 1.00 26.34 C
ANISOU 4142 CD LYS A 545 3561 1868 4577 -222 -2157 300 C
ATOM 4143 CE LYS A 545 50.375 26.061 -18.341 1.00 32.69 C
ANISOU 4143 CE LYS A 545 4329 2713 5380 -254 -2111 340 C
ATOM 4144 NZ LYS A 545 49.252 27.001 -18.081 1.00 35.43 N
ANISOU 4144 NZ LYS A 545 4760 3073 5629 -230 -2101 301 N
ATOM 4145 N GLU A 546 53.389 21.412 -14.102 1.00 24.91 N
ANISOU 4145 N GLU A 546 3358 1594 4512 -185 -2271 230 N
ATOM 4146 CA GLU A 546 53.583 21.030 -12.708 1.00 28.93 C
ANISOU 4146 CA GLU A 546 3930 2071 4993 -151 -2333 185 C
ATOM 4147 C GLU A 546 53.757 19.521 -12.618 1.00 31.18 C
ANISOU 4147 C GLU A 546 4180 2384 5282 -130 -2311 188 C
ATOM 4148 O GLU A 546 52.921 18.763 -13.119 1.00 31.79 O
ANISOU 4148 O GLU A 546 4272 2513 5292 -108 -2234 174 O
ATOM 4149 CB GLU A 546 52.409 21.503 -11.843 1.00 24.92 C
ANISOU 4149 CB GLU A 546 3547 1581 4340 -102 -2316 114 C
ATOM 4150 CG GLU A 546 52.256 23.025 -11.813 1.00 35.46 C
ANISOU 4150 CG GLU A 546 4908 2896 5668 -104 -2335 119 C
ATOM 4151 CD GLU A 546 51.060 23.484 -11.005 1.00 47.41 C
ANISOU 4151 CD GLU A 546 6532 4430 7052 -52 -2310 57 C
ATOM 4152 OE1 GLU A 546 50.599 22.710 -10.144 1.00 54.85 O
ANISOU 4152 OE1 GLU A 546 7537 5385 7917 -13 -2300 9 O
ATOM 4153 OE2 GLU A 546 50.577 24.615 -11.235 1.00 57.46 O
ANISOU 4153 OE2 GLU A 546 7824 5705 8301 -49 -2301 60 O
ATOM 4154 N LEU A 547 54.846 19.096 -11.978 1.00 30.96 N
ANISOU 4154 N LEU A 547 4098 2353 5313 -110 -2349 223 N
ATOM 4155 CA LEU A 547 55.212 17.688 -11.861 1.00 29.99 C
ANISOU 4155 CA LEU A 547 3926 2273 5194 -56 -2292 259 C
ATOM 4156 C LEU A 547 55.535 17.399 -10.401 1.00 31.43 C
ANISOU 4156 C LEU A 547 4156 2458 5331 -7 -2343 239 C
ATOM 4157 O LEU A 547 56.549 17.877 -9.879 1.00 31.84 O
ANISOU 4157 O LEU A 547 4166 2484 5448 -22 -2419 265 O
ATOM 4158 CB LEU A 547 56.400 17.361 -12.767 1.00 26.67 C
ANISOU 4158 CB LEU A 547 3364 1850 4918 -78 -2268 348 C
ATOM 4159 CG LEU A 547 57.005 15.957 -12.704 1.00 26.98 C
ANISOU 4159 CG LEU A 547 3344 1910 4997 -14 -2196 403 C
ATOM 4160 CD1 LEU A 547 55.957 14.902 -13.003 1.00 26.10 C
ANISOU 4160 CD1 LEU A 547 3294 1816 4806 39 -2075 381 C
ATOM 4161 CD2 LEU A 547 58.170 15.843 -13.673 1.00 27.63 C
ANISOU 4161 CD2 LEU A 547 3283 1984 5232 -43 -2173 489 C
ATOM 4162 N ALA A 548 54.678 16.620 -9.745 1.00 30.56 N
ANISOU 4162 N ALA A 548 4128 2379 5105 53 -2298 199 N
ATOM 4163 CA ALA A 548 54.851 16.262 -8.343 1.00 29.72 C
ANISOU 4163 CA ALA A 548 4068 2284 4941 106 -2336 184 C
ATOM 4164 C ALA A 548 55.442 14.858 -8.254 1.00 33.89 C
ANISOU 4164 C ALA A 548 4537 2839 5502 167 -2272 249 C
ATOM 4165 O ALA A 548 54.794 13.878 -8.642 1.00 30.32 O
ANISOU 4165 O ALA A 548 4107 2404 5008 206 -2169 255 O
ATOM 4166 CB ALA A 548 53.519 16.341 -7.596 1.00 26.23 C
ANISOU 4166 CB ALA A 548 3756 1856 4353 137 -2323 103 C
ATOM 4167 N LEU A 549 56.676 14.765 -7.753 1.00 36.33 N
ANISOU 4167 N LEU A 549 4772 3145 5886 176 -2324 302 N
ATOM 4168 CA LEU A 549 57.353 13.487 -7.577 1.00 28.72 C
ANISOU 4168 CA LEU A 549 3749 2201 4963 240 -2266 372 C
ATOM 4169 C LEU A 549 57.848 13.293 -6.149 1.00 29.61 C
ANISOU 4169 C LEU A 549 3877 2336 5037 286 -2329 381 C
ATOM 4170 O LEU A 549 58.586 12.336 -5.886 1.00 30.24 O
ANISOU 4170 O LEU A 549 3898 2432 5159 340 -2295 449 O
ATOM 4171 CB LEU A 549 58.523 13.353 -8.562 1.00 31.88 C
ANISOU 4171 CB LEU A 549 4015 2585 5512 214 -2246 452 C
ATOM 4172 CG LEU A 549 58.167 13.116 -10.032 1.00 33.62 C
ANISOU 4172 CG LEU A 549 4198 2789 5785 190 -2149 467 C
ATOM 4173 CD1 LEU A 549 59.397 13.281 -10.910 1.00 29.77 C
ANISOU 4173 CD1 LEU A 549 3574 2288 5450 152 -2152 541 C
ATOM 4174 CD2 LEU A 549 57.558 11.733 -10.207 1.00 35.21 C
ANISOU 4174 CD2 LEU A 549 4437 2992 5950 260 -2012 476 C
ATOM 4175 N ASP A 550 57.449 14.160 -5.221 1.00 30.84 N
ANISOU 4175 N ASP A 550 4110 2493 5115 271 -2412 316 N
ATOM 4176 CA ASP A 550 57.900 14.054 -3.842 1.00 32.54 C
ANISOU 4176 CA ASP A 550 4338 2735 5289 314 -2475 322 C
ATOM 4177 C ASP A 550 57.368 12.783 -3.186 1.00 33.89 C
ANISOU 4177 C ASP A 550 4553 2946 5376 397 -2401 338 C
ATOM 4178 O ASP A 550 56.440 12.135 -3.678 1.00 34.55 O
ANISOU 4178 O ASP A 550 4683 3030 5413 418 -2307 323 O
ATOM 4179 CB ASP A 550 57.447 15.271 -3.036 1.00 35.58 C
ANISOU 4179 CB ASP A 550 4807 3105 5607 285 -2563 243 C
ATOM 4180 CG ASP A 550 55.936 15.401 -2.981 1.00 41.00 C
ANISOU 4180 CG ASP A 550 5610 3790 6178 293 -2517 163 C
ATOM 4181 OD1 ASP A 550 55.334 15.862 -3.974 1.00 40.05 O
ANISOU 4181 OD1 ASP A 550 5508 3640 6068 249 -2486 134 O
ATOM 4182 OD2 ASP A 550 55.347 15.024 -1.948 1.00 41.14 O
ANISOU 4182 OD2 ASP A 550 5697 3841 6094 345 -2510 135 O
ATOM 4183 N THR A 551 57.980 12.433 -2.053 1.00 35.11 N
ANISOU 4183 N THR A 551 4691 3136 5513 446 -2443 371 N
ATOM 4184 CA THR A 551 57.490 11.369 -1.177 1.00 39.04 C
ANISOU 4184 CA THR A 551 5236 3674 5922 526 -2389 387 C
ATOM 4185 C THR A 551 57.385 10.038 -1.920 1.00 32.77 C
ANISOU 4185 C THR A 551 4414 2871 5165 573 -2261 448 C
ATOM 4186 O THR A 551 56.345 9.376 -1.923 1.00 35.14 O
ANISOU 4186 O THR A 551 4787 3175 5390 607 -2178 427 O
ATOM 4187 CB THR A 551 56.151 11.755 -0.543 1.00 39.80 C
ANISOU 4187 CB THR A 551 5455 3783 5886 528 -2393 299 C
ATOM 4188 OG1 THR A 551 56.178 13.143 -0.187 1.00 44.79 O
ANISOU 4188 OG1 THR A 551 6116 4397 6507 475 -2494 234 O
ATOM 4189 CG2 THR A 551 55.899 10.943 0.719 1.00 40.64 C
ANISOU 4189 CG2 THR A 551 5598 3942 5903 605 -2378 319 C
ATOM 4190 N ASN A 552 58.480 9.657 -2.575 1.00 34.63 N
ANISOU 4190 N ASN A 552 4545 3091 5522 575 -2238 523 N
ATOM 4191 CA ASN A 552 58.595 8.330 -3.164 1.00 39.31 C
ANISOU 4191 CA ASN A 552 5103 3666 6167 632 -2110 590 C
ATOM 4192 C ASN A 552 59.805 7.620 -2.571 1.00 36.55 C
ANISOU 4192 C ASN A 552 4670 3339 5879 692 -2116 683 C
ATOM 4193 O ASN A 552 60.233 7.933 -1.455 1.00 39.08 O
ANISOU 4193 O ASN A 552 4986 3702 6159 708 -2207 690 O
ATOM 4194 CB ASN A 552 58.707 8.412 -4.689 1.00 38.93 C
ANISOU 4194 CB ASN A 552 5003 3573 6217 585 -2047 596 C
ATOM 4195 CG ASN A 552 57.380 8.723 -5.359 1.00 40.79 C
ANISOU 4195 CG ASN A 552 5324 3790 6386 547 -2001 519 C
ATOM 4196 OD1 ASN A 552 56.587 7.825 -5.634 1.00 36.73 O
ANISOU 4196 OD1 ASN A 552 4862 3262 5833 584 -1887 515 O
ATOM 4197 ND2 ASN A 552 57.141 9.997 -5.636 1.00 37.16 N
ANISOU 4197 ND2 ASN A 552 4879 3327 5912 472 -2085 460 N
ATOM 4198 N GLN A 553 60.361 6.658 -3.302 1.00 34.68 N
ANISOU 4198 N GLN A 553 4366 3073 5738 729 -2015 753 N
ATOM 4199 CA GLN A 553 61.576 5.967 -2.894 1.00 38.65 C
ANISOU 4199 CA GLN A 553 4780 3594 6312 788 -2010 848 C
ATOM 4200 C GLN A 553 62.723 6.254 -3.858 1.00 37.71 C
ANISOU 4200 C GLN A 553 4540 3455 6334 748 -2019 893 C
ATOM 4201 O GLN A 553 63.664 5.464 -3.970 1.00 41.33 O
ANISOU 4201 O GLN A 553 4916 3911 6877 799 -1969 975 O
ATOM 4202 CB GLN A 553 61.326 4.463 -2.788 1.00 41.22 C
ANISOU 4202 CB GLN A 553 5127 3899 6634 880 -1873 901 C
ATOM 4203 CG GLN A 553 60.070 4.083 -2.009 1.00 52.12 C
ANISOU 4203 CG GLN A 553 6627 5293 7882 916 -1842 860 C
ATOM 4204 CD GLN A 553 60.231 4.252 -0.512 1.00 60.61 C
ANISOU 4204 CD GLN A 553 7720 6437 8872 952 -1937 874 C
ATOM 4205 OE1 GLN A 553 61.343 4.210 0.011 1.00 67.37 O
ANISOU 4205 OE1 GLN A 553 8498 7327 9773 981 -1993 938 O
ATOM 4206 NE2 GLN A 553 59.117 4.443 0.187 1.00 61.00 N
ANISOU 4206 NE2 GLN A 553 7868 6510 8797 952 -1955 815 N
ATOM 4207 N LEU A 554 62.650 7.382 -4.562 1.00 34.14 N
ANISOU 4207 N LEU A 554 4076 2988 5909 658 -2080 843 N
ATOM 4208 CA LEU A 554 63.623 7.695 -5.600 1.00 34.48 C
ANISOU 4208 CA LEU A 554 4004 3010 6085 612 -2080 885 C
ATOM 4209 C LEU A 554 64.986 8.012 -5.001 1.00 40.00 C
ANISOU 4209 C LEU A 554 4610 3748 6841 612 -2176 945 C
ATOM 4210 O LEU A 554 65.093 8.713 -3.991 1.00 40.53 O
ANISOU 4210 O LEU A 554 4705 3850 6844 596 -2291 919 O
ATOM 4211 CB LEU A 554 63.142 8.879 -6.435 1.00 33.66 C
ANISOU 4211 CB LEU A 554 3916 2884 5988 515 -2125 818 C
ATOM 4212 CG LEU A 554 61.961 8.646 -7.372 1.00 33.84 C
ANISOU 4212 CG LEU A 554 4003 2871 5983 502 -2024 769 C
ATOM 4213 CD1 LEU A 554 61.439 9.980 -7.871 1.00 33.86 C
ANISOU 4213 CD1 LEU A 554 4035 2865 5965 410 -2097 700 C
ATOM 4214 CD2 LEU A 554 62.372 7.753 -8.536 1.00 32.40 C
ANISOU 4214 CD2 LEU A 554 3742 2655 5914 524 -1892 825 C
ATOM 4215 N LYS A 555 66.033 7.497 -5.647 1.00 37.80 N
ANISOU 4215 N LYS A 555 4216 3462 6683 629 -2125 1024 N
ATOM 4216 CA LYS A 555 67.409 7.762 -5.261 1.00 39.00 C
ANISOU 4216 CA LYS A 555 4264 3652 6903 625 -2205 1090 C
ATOM 4217 C LYS A 555 68.230 8.408 -6.367 1.00 37.95 C
ANISOU 4217 C LYS A 555 4023 3504 6894 551 -2221 1118 C
ATOM 4218 O LYS A 555 69.324 8.914 -6.087 1.00 39.96 O
ANISOU 4218 O LYS A 555 4194 3789 7199 525 -2306 1160 O
ATOM 4219 CB LYS A 555 68.104 6.463 -4.823 1.00 46.79 C
ANISOU 4219 CB LYS A 555 5199 4658 7920 727 -2133 1179 C
ATOM 4220 CG LYS A 555 67.386 5.720 -3.710 1.00 50.12 C
ANISOU 4220 CG LYS A 555 5718 5098 8227 808 -2109 1169 C
ATOM 4221 CD LYS A 555 68.168 4.491 -3.277 1.00 52.43 C
ANISOU 4221 CD LYS A 555 5955 5410 8558 909 -2042 1265 C
ATOM 4222 CE LYS A 555 67.478 3.780 -2.122 1.00 57.94 C
ANISOU 4222 CE LYS A 555 6746 6130 9139 990 -2022 1263 C
ATOM 4223 NZ LYS A 555 68.253 2.608 -1.634 1.00 63.37 N
ANISOU 4223 NZ LYS A 555 7382 6836 9861 1092 -1962 1360 N
ATOM 4224 N SER A 556 67.741 8.408 -7.604 1.00 37.87 N
ANISOU 4224 N SER A 556 4007 3451 6932 516 -2139 1097 N
ATOM 4225 CA SER A 556 68.458 8.976 -8.737 1.00 37.22 C
ANISOU 4225 CA SER A 556 3817 3357 6968 447 -2141 1128 C
ATOM 4226 C SER A 556 67.480 9.130 -9.890 1.00 45.41 C
ANISOU 4226 C SER A 556 4890 4352 8011 407 -2065 1078 C
ATOM 4227 O SER A 556 66.383 8.562 -9.876 1.00 42.15 O
ANISOU 4227 O SER A 556 4572 3918 7524 444 -1990 1032 O
ATOM 4228 CB SER A 556 69.643 8.098 -9.155 1.00 39.44 C
ANISOU 4228 CB SER A 556 3971 3649 7366 497 -2066 1227 C
ATOM 4229 OG SER A 556 69.197 6.935 -9.830 1.00 40.23 O
ANISOU 4229 OG SER A 556 4077 3713 7494 558 -1908 1239 O
ATOM 4230 N VAL A 557 67.886 9.916 -10.882 1.00 35.94 N
ANISOU 4230 N VAL A 557 3614 3146 6897 329 -2085 1091 N
ATOM 4231 CA VAL A 557 67.134 10.051 -12.127 1.00 37.66 C
ANISOU 4231 CA VAL A 557 3837 3332 7139 290 -2007 1060 C
ATOM 4232 C VAL A 557 68.093 9.808 -13.286 1.00 38.25 C
ANISOU 4232 C VAL A 557 3767 3410 7358 276 -1934 1136 C
ATOM 4233 O VAL A 557 69.305 10.022 -13.138 1.00 37.47 O
ANISOU 4233 O VAL A 557 3569 3337 7330 264 -1986 1199 O
ATOM 4234 CB VAL A 557 66.464 11.431 -12.239 1.00 37.06 C
ANISOU 4234 CB VAL A 557 3823 3249 7010 199 -2104 991 C
ATOM 4235 CG1 VAL A 557 65.511 11.659 -11.073 1.00 36.19 C
ANISOU 4235 CG1 VAL A 557 3855 3140 6757 217 -2168 913 C
ATOM 4236 CG2 VAL A 557 67.515 12.534 -12.308 1.00 40.65 C
ANISOU 4236 CG2 VAL A 557 4194 3714 7536 122 -2211 1026 C
ATOM 4237 N PRO A 558 67.613 9.343 -14.435 1.00 40.11 N
ANISOU 4237 N PRO A 558 3981 3620 7639 280 -1810 1133 N
ATOM 4238 CA PRO A 558 68.487 9.260 -15.609 1.00 38.23 C
ANISOU 4238 CA PRO A 558 3597 3390 7538 259 -1743 1201 C
ATOM 4239 C PRO A 558 68.895 10.652 -16.056 1.00 41.01 C
ANISOU 4239 C PRO A 558 3894 3764 7926 154 -1848 1209 C
ATOM 4240 O PRO A 558 68.179 11.632 -15.839 1.00 46.82 O
ANISOU 4240 O PRO A 558 4712 4491 8587 95 -1936 1148 O
ATOM 4241 CB PRO A 558 67.613 8.569 -16.664 1.00 40.60 C
ANISOU 4241 CB PRO A 558 3915 3655 7857 282 -1588 1174 C
ATOM 4242 CG PRO A 558 66.486 7.940 -15.895 1.00 42.36 C
ANISOU 4242 CG PRO A 558 4288 3846 7960 337 -1554 1108 C
ATOM 4243 CD PRO A 558 66.265 8.815 -14.704 1.00 40.03 C
ANISOU 4243 CD PRO A 558 4078 3575 7558 308 -1714 1069 C
ATOM 4244 N ASP A 559 70.072 10.735 -16.671 1.00 42.65 N
ANISOU 4244 N ASP A 559 3962 3998 8246 131 -1834 1285 N
ATOM 4245 CA ASP A 559 70.554 12.015 -17.172 1.00 45.29 C
ANISOU 4245 CA ASP A 559 4239 4349 8620 29 -1917 1303 C
ATOM 4246 C ASP A 559 69.607 12.563 -18.235 1.00 43.95 C
ANISOU 4246 C ASP A 559 4088 4169 8443 -29 -1878 1263 C
ATOM 4247 O ASP A 559 69.161 11.833 -19.126 1.00 46.88 O
ANISOU 4247 O ASP A 559 4425 4538 8848 4 -1750 1264 O
ATOM 4248 CB ASP A 559 71.966 11.861 -17.741 1.00 46.25 C
ANISOU 4248 CB ASP A 559 4206 4506 8861 22 -1884 1396 C
ATOM 4249 CG ASP A 559 73.020 11.680 -16.659 1.00 52.16 C
ANISOU 4249 CG ASP A 559 4929 5274 9615 57 -1958 1441 C
ATOM 4250 OD1 ASP A 559 72.670 11.744 -15.460 1.00 56.14 O
ANISOU 4250 OD1 ASP A 559 5533 5768 10030 81 -2040 1398 O
ATOM 4251 OD2 ASP A 559 74.202 11.477 -17.010 1.00 55.78 O
ANISOU 4251 OD2 ASP A 559 5266 5765 10163 61 -1932 1520 O
ATOM 4252 N GLY A 560 69.284 13.850 -18.123 1.00 42.33 N
ANISOU 4252 N GLY A 560 3939 3955 8191 -111 -1983 1226 N
ATOM 4253 CA GLY A 560 68.471 14.530 -19.111 1.00 37.50 C
ANISOU 4253 CA GLY A 560 3341 3340 7569 -174 -1957 1196 C
ATOM 4254 C GLY A 560 66.988 14.240 -19.063 1.00 39.18 C
ANISOU 4254 C GLY A 560 3666 3530 7688 -145 -1922 1118 C
ATOM 4255 O GLY A 560 66.286 14.558 -20.029 1.00 45.69 O
ANISOU 4255 O GLY A 560 4484 4365 8512 -185 -1874 1101 O
ATOM 4256 N ILE A 561 66.483 13.656 -17.973 1.00 36.44 N
ANISOU 4256 N ILE A 561 3427 3162 7256 -79 -1941 1072 N
ATOM 4257 CA ILE A 561 65.079 13.255 -17.937 1.00 37.07 C
ANISOU 4257 CA ILE A 561 3625 3220 7241 -43 -1888 1001 C
ATOM 4258 C ILE A 561 64.160 14.470 -18.002 1.00 38.82 C
ANISOU 4258 C ILE A 561 3931 3435 7385 -114 -1966 939 C
ATOM 4259 O ILE A 561 63.059 14.399 -18.563 1.00 40.64 O
ANISOU 4259 O ILE A 561 4217 3658 7566 -114 -1908 899 O
ATOM 4260 CB ILE A 561 64.802 12.395 -16.685 1.00 37.91 C
ANISOU 4260 CB ILE A 561 3830 3311 7261 40 -1887 968 C
ATOM 4261 CG1 ILE A 561 63.343 11.929 -16.662 1.00 37.97 C
ANISOU 4261 CG1 ILE A 561 3969 3295 7162 75 -1816 894 C
ATOM 4262 CG2 ILE A 561 65.159 13.153 -15.410 1.00 32.32 C
ANISOU 4262 CG2 ILE A 561 3174 2612 6495 20 -2033 946 C
ATOM 4263 CD1 ILE A 561 63.061 10.854 -15.642 1.00 38.08 C
ANISOU 4263 CD1 ILE A 561 4068 3298 7102 162 -1774 872 C
ATOM 4264 N PHE A 562 64.598 15.603 -17.455 1.00 35.94 N
ANISOU 4264 N PHE A 562 3582 3064 7009 -175 -2089 933 N
ATOM 4265 CA PHE A 562 63.815 16.830 -17.418 1.00 37.14 C
ANISOU 4265 CA PHE A 562 3824 3196 7093 -238 -2160 876 C
ATOM 4266 C PHE A 562 64.103 17.753 -18.598 1.00 34.88 C
ANISOU 4266 C PHE A 562 3461 2914 6877 -318 -2148 919 C
ATOM 4267 O PHE A 562 63.581 18.871 -18.631 1.00 33.43 O
ANISOU 4267 O PHE A 562 3350 2706 6647 -367 -2199 887 O
ATOM 4268 CB PHE A 562 64.081 17.581 -16.109 1.00 38.36 C
ANISOU 4268 CB PHE A 562 4059 3322 7196 -249 -2285 841 C
ATOM 4269 CG PHE A 562 63.778 16.778 -14.870 1.00 35.13 C
ANISOU 4269 CG PHE A 562 3729 2919 6699 -172 -2299 798 C
ATOM 4270 CD1 PHE A 562 62.701 15.904 -14.837 1.00 31.05 C
ANISOU 4270 CD1 PHE A 562 3285 2412 6100 -114 -2222 753 C
ATOM 4271 CD2 PHE A 562 64.575 16.892 -13.741 1.00 32.48 C
ANISOU 4271 CD2 PHE A 562 3398 2583 6362 -157 -2382 806 C
ATOM 4272 CE1 PHE A 562 62.421 15.160 -13.697 1.00 35.26 C
ANISOU 4272 CE1 PHE A 562 3896 2954 6548 -41 -2225 721 C
ATOM 4273 CE2 PHE A 562 64.303 16.151 -12.598 1.00 38.02 C
ANISOU 4273 CE2 PHE A 562 4169 3298 6979 -84 -2390 774 C
ATOM 4274 CZ PHE A 562 63.223 15.285 -12.576 1.00 35.85 C
ANISOU 4274 CZ PHE A 562 3968 3033 6620 -27 -2310 733 C
ATOM 4275 N ASP A 563 64.915 17.311 -19.565 1.00 41.40 N
ANISOU 4275 N ASP A 563 4148 3775 7808 -326 -2071 994 N
ATOM 4276 CA ASP A 563 65.429 18.223 -20.585 1.00 39.30 C
ANISOU 4276 CA ASP A 563 3809 3524 7601 -399 -2056 1045 C
ATOM 4277 C ASP A 563 64.335 18.735 -21.514 1.00 38.81 C
ANISOU 4277 C ASP A 563 3783 3480 7483 -437 -2001 1013 C
ATOM 4278 O ASP A 563 64.382 19.896 -21.939 1.00 42.92 O
ANISOU 4278 O ASP A 563 4321 3996 7991 -486 -2024 1030 O
ATOM 4279 CB ASP A 563 66.532 17.536 -21.387 1.00 44.47 C
ANISOU 4279 CB ASP A 563 4307 4225 8367 -393 -1969 1126 C
ATOM 4280 CG ASP A 563 67.861 17.550 -20.663 1.00 50.87 C
ANISOU 4280 CG ASP A 563 5069 5024 9236 -383 -2037 1178 C
ATOM 4281 OD1 ASP A 563 67.934 18.173 -19.584 1.00 50.92 O
ANISOU 4281 OD1 ASP A 563 5159 4990 9198 -390 -2151 1149 O
ATOM 4282 OD2 ASP A 563 68.830 16.948 -21.169 1.00 54.20 O
ANISOU 4282 OD2 ASP A 563 5367 5481 9745 -369 -1973 1246 O
ATOM 4283 N ARG A 564 63.348 17.902 -21.837 1.00 51.23 N
ANISOU 4283 N ARG A 564 6376 4013 9078 -248 -3508 335 N
ATOM 4284 CA ARG A 564 62.316 18.259 -22.802 1.00 50.45 C
ANISOU 4284 CA ARG A 564 6296 3941 8933 -244 -3469 335 C
ATOM 4285 C ARG A 564 61.047 18.797 -22.153 1.00 49.34 C
ANISOU 4285 C ARG A 564 6216 3801 8731 -218 -3468 315 C
ATOM 4286 O ARG A 564 60.058 19.030 -22.857 1.00 53.48 O
ANISOU 4286 O ARG A 564 6759 4356 9205 -214 -3429 310 O
ATOM 4287 CB ARG A 564 61.988 17.053 -23.683 1.00 49.48 C
ANISOU 4287 CB ARG A 564 6160 3866 8775 -240 -3403 323 C
ATOM 4288 CG ARG A 564 63.069 16.736 -24.699 1.00 53.50 C
ANISOU 4288 CG ARG A 564 6603 4402 9323 -277 -3381 339 C
ATOM 4289 CD ARG A 564 62.730 15.497 -25.508 1.00 64.78 C
ANISOU 4289 CD ARG A 564 8023 5877 10714 -271 -3318 322 C
ATOM 4290 NE ARG A 564 63.816 14.523 -25.468 1.00 78.73 N
ANISOU 4290 NE ARG A 564 9744 7652 12518 -284 -3310 322 N
ATOM 4291 CZ ARG A 564 63.840 13.393 -26.167 1.00 88.23 C
ANISOU 4291 CZ ARG A 564 10928 8893 13703 -285 -3260 310 C
ATOM 4292 NH1 ARG A 564 62.836 13.083 -26.976 1.00 89.64 N
ANISOU 4292 NH1 ARG A 564 11129 9106 13825 -276 -3215 295 N
ATOM 4293 NH2 ARG A 564 64.875 12.573 -26.061 1.00 90.82 N
ANISOU 4293 NH2 ARG A 564 11213 9226 14069 -297 -3257 312 N
ATOM 4294 N LEU A 565 61.053 19.000 -20.834 1.00 45.19 N
ANISOU 4294 N LEU A 565 5717 3253 8199 -205 -3501 299 N
ATOM 4295 CA LEU A 565 59.925 19.602 -20.123 1.00 42.45 C
ANISOU 4295 CA LEU A 565 5422 2917 7789 -186 -3495 276 C
ATOM 4296 C LEU A 565 59.966 21.128 -20.261 1.00 42.86 C
ANISOU 4296 C LEU A 565 5480 2942 7864 -201 -3539 296 C
ATOM 4297 O LEU A 565 60.135 21.874 -19.297 1.00 40.07 O
ANISOU 4297 O LEU A 565 5146 2555 7523 -198 -3590 292 O
ATOM 4298 CB LEU A 565 59.941 19.175 -18.661 1.00 41.76 C
ANISOU 4298 CB LEU A 565 5361 2817 7689 -165 -3514 249 C
ATOM 4299 CG LEU A 565 59.743 17.684 -18.396 1.00 38.74 C
ANISOU 4299 CG LEU A 565 4979 2464 7276 -147 -3469 226 C
ATOM 4300 CD1 LEU A 565 59.778 17.391 -16.906 1.00 38.96 C
ANISOU 4300 CD1 LEU A 565 5033 2476 7292 -128 -3493 202 C
ATOM 4301 CD2 LEU A 565 58.434 17.220 -19.002 1.00 37.92 C
ANISOU 4301 CD2 LEU A 565 4897 2411 7098 -134 -3399 211 C
ATOM 4302 N THR A 566 59.789 21.583 -21.505 1.00 47.19 N
ANISOU 4302 N THR A 566 6011 3504 8415 -217 -3520 317 N
ATOM 4303 CA THR A 566 59.995 22.982 -21.869 1.00 51.08 C
ANISOU 4303 CA THR A 566 6498 3970 8941 -237 -3561 342 C
ATOM 4304 C THR A 566 58.961 23.927 -21.267 1.00 48.01 C
ANISOU 4304 C THR A 566 6159 3584 8499 -223 -3566 325 C
ATOM 4305 O THR A 566 59.177 25.143 -21.288 1.00 51.31 O
ANISOU 4305 O THR A 566 6578 3973 8946 -237 -3611 343 O
ATOM 4306 CB THR A 566 59.983 23.127 -23.392 1.00 56.82 C
ANISOU 4306 CB THR A 566 7195 4715 9678 -256 -3532 367 C
ATOM 4307 OG1 THR A 566 58.839 22.446 -23.922 1.00 63.18 O
ANISOU 4307 OG1 THR A 566 8022 5571 10412 -241 -3464 346 O
ATOM 4308 CG2 THR A 566 61.244 22.528 -23.998 1.00 51.17 C
ANISOU 4308 CG2 THR A 566 6420 3996 9026 -280 -3535 388 C
ATOM 4309 N SER A 567 57.852 23.412 -20.746 1.00 43.91 N
ANISOU 4309 N SER A 567 5680 3098 7907 -198 -3522 294 N
ATOM 4310 CA SER A 567 56.816 24.247 -20.159 1.00 41.24 C
ANISOU 4310 CA SER A 567 5389 2765 7517 -183 -3522 278 C
ATOM 4311 C SER A 567 56.823 24.211 -18.639 1.00 40.58 C
ANISOU 4311 C SER A 567 5337 2660 7423 -164 -3554 254 C
ATOM 4312 O SER A 567 55.946 24.816 -18.016 1.00 39.45 O
ANISOU 4312 O SER A 567 5234 2520 7234 -149 -3554 237 O
ATOM 4313 CB SER A 567 55.438 23.818 -20.672 1.00 38.26 C
ANISOU 4313 CB SER A 567 5035 2440 7064 -170 -3451 262 C
ATOM 4314 OG SER A 567 55.347 23.940 -22.081 1.00 38.01 O
ANISOU 4314 OG SER A 567 4979 2426 7037 -187 -3424 282 O
ATOM 4315 N LEU A 568 57.790 23.527 -18.033 1.00 39.75 N
ANISOU 4315 N LEU A 568 5213 2532 7360 -163 -3583 251 N
ATOM 4316 CA LEU A 568 57.745 23.280 -16.599 1.00 39.96 C
ANISOU 4316 CA LEU A 568 5270 2542 7371 -142 -3607 225 C
ATOM 4317 C LEU A 568 57.871 24.575 -15.807 1.00 43.71 C
ANISOU 4317 C LEU A 568 5771 2974 7862 -143 -3674 226 C
ATOM 4318 O LEU A 568 58.704 25.434 -16.108 1.00 41.59 O
ANISOU 4318 O LEU A 568 5480 2667 7655 -165 -3730 253 O
ATOM 4319 CB LEU A 568 58.860 22.315 -16.195 1.00 42.39 C
ANISOU 4319 CB LEU A 568 5549 2831 7728 -145 -3629 226 C
ATOM 4320 CG LEU A 568 58.677 21.624 -14.841 1.00 43.57 C
ANISOU 4320 CG LEU A 568 5727 2978 7849 -119 -3632 194 C
ATOM 4321 CD1 LEU A 568 57.543 20.610 -14.907 1.00 44.00 C
ANISOU 4321 CD1 LEU A 568 5800 3088 7830 -97 -3553 170 C
ATOM 4322 CD2 LEU A 568 59.968 20.971 -14.363 1.00 40.76 C
ANISOU 4322 CD2 LEU A 568 5341 2589 7556 -126 -3675 200 C
ATOM 4323 N GLN A 569 57.038 24.700 -14.777 1.00 40.51 N
ANISOU 4323 N GLN A 569 5413 2575 7404 -118 -3670 198 N
ATOM 4324 CA GLN A 569 57.063 25.834 -13.865 1.00 41.14 C
ANISOU 4324 CA GLN A 569 5526 2615 7492 -114 -3734 192 C
ATOM 4325 C GLN A 569 57.213 25.437 -12.404 1.00 43.86 C
ANISOU 4325 C GLN A 569 5898 2937 7828 -92 -3766 165 C
ATOM 4326 O GLN A 569 57.745 26.224 -11.618 1.00 46.95 O
ANISOU 4326 O GLN A 569 6305 3280 8253 -93 -3841 165 O
ATOM 4327 CB GLN A 569 55.786 26.675 -14.029 1.00 40.77 C
ANISOU 4327 CB GLN A 569 5515 2591 7384 -104 -3705 185 C
ATOM 4328 CG GLN A 569 55.665 27.350 -15.391 1.00 48.54 C
ANISOU 4328 CG GLN A 569 6476 3587 8380 -127 -3688 213 C
ATOM 4329 CD GLN A 569 54.262 27.842 -15.680 1.00 51.26 C
ANISOU 4329 CD GLN A 569 6853 3968 8655 -117 -3640 204 C
ATOM 4330 OE1 GLN A 569 53.366 27.726 -14.846 1.00 49.06 O
ANISOU 4330 OE1 GLN A 569 6614 3705 8322 -92 -3619 178 O
ATOM 4331 NE2 GLN A 569 54.062 28.390 -16.872 1.00 46.69 N
ANISOU 4331 NE2 GLN A 569 6257 3403 8081 -135 -3622 226 N
ATOM 4332 N LYS A 570 56.761 24.245 -12.017 1.00 40.88 N
ANISOU 4332 N LYS A 570 5529 2595 7410 -72 -3714 142 N
ATOM 4333 CA LYS A 570 56.880 23.774 -10.644 1.00 41.12 C
ANISOU 4333 CA LYS A 570 5585 2608 7431 -50 -3740 116 C
ATOM 4334 C LYS A 570 57.210 22.291 -10.641 1.00 40.76 C
ANISOU 4334 C LYS A 570 5514 2584 7387 -45 -3702 108 C
ATOM 4335 O LYS A 570 56.637 21.524 -11.420 1.00 41.97 O
ANISOU 4335 O LYS A 570 5654 2785 7508 -44 -3631 109 O
ATOM 4336 CB LYS A 570 55.591 24.013 -9.852 1.00 40.77 C
ANISOU 4336 CB LYS A 570 5594 2585 7312 -22 -3713 88 C
ATOM 4337 CG LYS A 570 55.291 25.472 -9.571 1.00 41.22 C
ANISOU 4337 CG LYS A 570 5683 2615 7366 -22 -3760 89 C
ATOM 4338 CD LYS A 570 53.983 25.626 -8.815 1.00 42.75 C
ANISOU 4338 CD LYS A 570 5926 2832 7484 6 -3727 62 C
ATOM 4339 CE LYS A 570 53.653 27.092 -8.587 1.00 48.38 C
ANISOU 4339 CE LYS A 570 6673 3519 8192 6 -3772 64 C
ATOM 4340 NZ LYS A 570 52.356 27.268 -7.878 1.00 53.55 N
ANISOU 4340 NZ LYS A 570 7375 4197 8774 33 -3738 39 N
ATOM 4341 N ILE A 571 58.121 21.891 -9.756 1.00 41.30 N
ANISOU 4341 N ILE A 571 5578 2618 7495 -41 -3752 100 N
ATOM 4342 CA ILE A 571 58.460 20.485 -9.563 1.00 41.02 C
ANISOU 4342 CA ILE A 571 5523 2599 7462 -34 -3723 90 C
ATOM 4343 C ILE A 571 58.672 20.224 -8.076 1.00 41.42 C
ANISOU 4343 C ILE A 571 5604 2624 7510 -13 -3765 63 C
ATOM 4344 O ILE A 571 59.302 21.021 -7.372 1.00 42.23 O
ANISOU 4344 O ILE A 571 5720 2675 7651 -16 -3844 64 O
ATOM 4345 CB ILE A 571 59.700 20.074 -10.391 1.00 41.28 C
ANISOU 4345 CB ILE A 571 5501 2617 7567 -61 -3740 118 C
ATOM 4346 CG1 ILE A 571 59.920 18.563 -10.309 1.00 40.88 C
ANISOU 4346 CG1 ILE A 571 5431 2591 7512 -53 -3699 107 C
ATOM 4347 CG2 ILE A 571 60.946 20.832 -9.939 1.00 45.33 C
ANISOU 4347 CG2 ILE A 571 6000 3064 8158 -78 -3836 135 C
ATOM 4348 CD1 ILE A 571 60.875 18.032 -11.348 1.00 40.92 C
ANISOU 4348 CD1 ILE A 571 5380 2595 7574 -77 -3693 135 C
ATOM 4349 N TRP A 572 58.117 19.114 -7.594 1.00 40.87 N
ANISOU 4349 N TRP A 572 5547 2588 7395 8 -3714 39 N
ATOM 4350 CA TRP A 572 58.281 18.660 -6.218 1.00 41.17 C
ANISOU 4350 CA TRP A 572 5610 2606 7425 30 -3745 12 C
ATOM 4351 C TRP A 572 59.171 17.426 -6.237 1.00 41.17 C
ANISOU 4351 C TRP A 572 5575 2606 7463 25 -3741 14 C
ATOM 4352 O TRP A 572 58.838 16.434 -6.894 1.00 40.49 O
ANISOU 4352 O TRP A 572 5467 2563 7353 25 -3672 15 O
ATOM 4353 CB TRP A 572 56.932 18.328 -5.575 1.00 40.55 C
ANISOU 4353 CB TRP A 572 5575 2567 7266 59 -3690 -17 C
ATOM 4354 CG TRP A 572 56.006 19.492 -5.361 1.00 42.51 C
ANISOU 4354 CG TRP A 572 5864 2816 7474 68 -3695 -22 C
ATOM 4355 CD1 TRP A 572 55.695 20.086 -4.169 1.00 49.65 C
ANISOU 4355 CD1 TRP A 572 6814 3695 8356 89 -3736 -45 C
ATOM 4356 CD2 TRP A 572 55.252 20.190 -6.364 1.00 41.72 C
ANISOU 4356 CD2 TRP A 572 5761 2740 7349 58 -3657 -6 C
ATOM 4357 NE1 TRP A 572 54.803 21.112 -4.370 1.00 50.13 N
ANISOU 4357 NE1 TRP A 572 6902 3765 8382 92 -3726 -43 N
ATOM 4358 CE2 TRP A 572 54.516 21.196 -5.707 1.00 47.09 C
ANISOU 4358 CE2 TRP A 572 6487 3410 7995 72 -3678 -19 C
ATOM 4359 CE3 TRP A 572 55.131 20.064 -7.753 1.00 39.71 C
ANISOU 4359 CE3 TRP A 572 5473 2516 7099 38 -3611 18 C
ATOM 4360 CZ2 TRP A 572 53.672 22.069 -6.390 1.00 40.06 C
ANISOU 4360 CZ2 TRP A 572 5608 2539 7075 67 -3652 -8 C
ATOM 4361 CZ3 TRP A 572 54.292 20.935 -8.429 1.00 44.97 C
ANISOU 4361 CZ3 TRP A 572 6150 3199 7736 33 -3587 28 C
ATOM 4362 CH2 TRP A 572 53.575 21.924 -7.746 1.00 42.35 C
ANISOU 4362 CH2 TRP A 572 5862 2857 7370 47 -3607 15 C
ATOM 4363 N LEU A 573 60.298 17.487 -5.528 1.00 41.97 N
ANISOU 4363 N LEU A 573 5669 2657 7623 19 -3818 14 N
ATOM 4364 CA LEU A 573 61.221 16.363 -5.471 1.00 42.07 C
ANISOU 4364 CA LEU A 573 5645 2662 7676 13 -3822 17 C
ATOM 4365 C LEU A 573 61.658 16.006 -4.057 1.00 45.94 C
ANISOU 4365 C LEU A 573 6158 3120 8177 31 -3876 -8 C
ATOM 4366 O LEU A 573 62.443 15.066 -3.891 1.00 46.18 O
ANISOU 4366 O LEU A 573 6162 3142 8243 27 -3885 -8 O
ATOM 4367 CB LEU A 573 62.463 16.645 -6.334 1.00 42.58 C
ANISOU 4367 CB LEU A 573 5659 2696 7825 -20 -3864 54 C
ATOM 4368 CG LEU A 573 62.246 16.593 -7.850 1.00 42.03 C
ANISOU 4368 CG LEU A 573 5554 2661 7752 -39 -3804 79 C
ATOM 4369 CD1 LEU A 573 63.503 17.001 -8.601 1.00 44.08 C
ANISOU 4369 CD1 LEU A 573 5764 2884 8099 -73 -3854 117 C
ATOM 4370 CD2 LEU A 573 61.799 15.201 -8.277 1.00 41.19 C
ANISOU 4370 CD2 LEU A 573 5434 2608 7608 -29 -3722 69 C
ATOM 4371 N HIS A 574 61.159 16.707 -3.039 1.00 46.32 N
ANISOU 4371 N HIS A 574 6257 3150 8195 51 -3911 -31 N
ATOM 4372 CA HIS A 574 61.578 16.484 -1.661 1.00 43.46 C
ANISOU 4372 CA HIS A 574 5920 2750 7842 69 -3971 -56 C
ATOM 4373 C HIS A 574 61.092 15.122 -1.165 1.00 46.20 C
ANISOU 4373 C HIS A 574 6275 3137 8143 92 -3912 -82 C
ATOM 4374 O HIS A 574 60.393 14.383 -1.864 1.00 51.04 O
ANISOU 4374 O HIS A 574 6873 3804 8715 94 -3825 -80 O
ATOM 4375 CB HIS A 574 61.060 17.606 -0.760 1.00 43.90 C
ANISOU 4375 CB HIS A 574 6031 2779 7870 87 -4020 -75 C
ATOM 4376 CG HIS A 574 59.566 17.662 -0.655 1.00 44.56 C
ANISOU 4376 CG HIS A 574 6152 2911 7866 111 -3948 -94 C
ATOM 4377 ND1 HIS A 574 58.834 16.740 0.062 1.00 42.62 N
ANISOU 4377 ND1 HIS A 574 5931 2699 7565 138 -3900 -123 N
ATOM 4378 CD2 HIS A 574 58.667 18.529 -1.178 1.00 42.81 C
ANISOU 4378 CD2 HIS A 574 5948 2711 7608 110 -3918 -87 C
ATOM 4379 CE1 HIS A 574 57.549 17.034 -0.025 1.00 42.03 C
ANISOU 4379 CE1 HIS A 574 5884 2662 7423 152 -3842 -132 C
ATOM 4380 NE2 HIS A 574 57.421 18.116 -0.771 1.00 45.08 N
ANISOU 4380 NE2 HIS A 574 6268 3042 7820 136 -3852 -111 N
ATOM 4381 N THR A 575 61.480 14.792 0.068 1.00 43.32 N
ANISOU 4381 N THR A 575 5932 2742 7786 110 -3962 -107 N
ATOM 4382 CA THR A 575 61.075 13.554 0.736 1.00 42.86 C
ANISOU 4382 CA THR A 575 5884 2714 7686 133 -3918 -134 C
ATOM 4383 C THR A 575 61.395 12.332 -0.124 1.00 42.31 C
ANISOU 4383 C THR A 575 5765 2678 7631 119 -3859 -120 C
ATOM 4384 O THR A 575 60.573 11.432 -0.311 1.00 41.49 O
ANISOU 4384 O THR A 575 5663 2627 7475 132 -3779 -130 O
ATOM 4385 CB THR A 575 59.590 13.597 1.114 1.00 42.20 C
ANISOU 4385 CB THR A 575 5845 2673 7516 160 -3856 -158 C
ATOM 4386 OG1 THR A 575 59.266 14.908 1.593 1.00 42.67 O
ANISOU 4386 OG1 THR A 575 5945 2703 7563 168 -3905 -164 O
ATOM 4387 CG2 THR A 575 59.293 12.599 2.227 1.00 42.04 C
ANISOU 4387 CG2 THR A 575 5849 2665 7460 189 -3843 -191 C
ATOM 4388 N ASN A 576 62.612 12.318 -0.662 1.00 47.29 N
ANISOU 4388 N ASN A 576 6352 3278 8338 93 -3902 -94 N
ATOM 4389 CA ASN A 576 63.156 11.181 -1.385 1.00 45.41 C
ANISOU 4389 CA ASN A 576 6065 3062 8128 79 -3863 -79 C
ATOM 4390 C ASN A 576 64.579 10.920 -0.910 1.00 47.50 C
ANISOU 4390 C ASN A 576 6302 3273 8471 66 -3943 -72 C
ATOM 4391 O ASN A 576 65.328 11.866 -0.633 1.00 45.05 O
ANISOU 4391 O ASN A 576 5992 2908 8215 53 -4028 -60 O
ATOM 4392 CB ASN A 576 63.144 11.416 -2.903 1.00 47.19 C
ANISOU 4392 CB ASN A 576 6253 3311 8367 53 -3819 -46 C
ATOM 4393 CG ASN A 576 61.777 11.183 -3.520 1.00 45.73 C
ANISOU 4393 CG ASN A 576 6083 3187 8104 65 -3725 -53 C
ATOM 4394 OD1 ASN A 576 61.388 10.044 -3.777 1.00 40.43 O
ANISOU 4394 OD1 ASN A 576 5402 2558 7403 73 -3660 -61 O
ATOM 4395 ND2 ASN A 576 61.042 12.262 -3.762 1.00 41.07 N
ANISOU 4395 ND2 ASN A 576 5517 2601 7484 66 -3720 -49 N
ATOM 4396 N PRO A 577 64.974 9.655 -0.784 1.00 46.86 N
ANISOU 4396 N PRO A 577 6198 3205 8401 69 -3921 -79 N
ATOM 4397 CA PRO A 577 66.338 9.330 -0.316 1.00 44.99 C
ANISOU 4397 CA PRO A 577 5932 2918 8243 56 -3999 -70 C
ATOM 4398 C PRO A 577 67.372 9.458 -1.430 1.00 46.36 C
ANISOU 4398 C PRO A 577 6043 3082 8490 18 -4011 -28 C
ATOM 4399 O PRO A 577 67.873 8.481 -1.993 1.00 43.94 O
ANISOU 4399 O PRO A 577 5687 2810 8197 2 -3969 -19 O
ATOM 4400 CB PRO A 577 66.175 7.891 0.182 1.00 43.66 C
ANISOU 4400 CB PRO A 577 5764 2779 8047 75 -3957 -95 C
ATOM 4401 CG PRO A 577 65.100 7.325 -0.694 1.00 43.81 C
ANISOU 4401 CG PRO A 577 5781 2866 8000 81 -3848 -96 C
ATOM 4402 CD PRO A 577 64.138 8.453 -0.950 1.00 42.15 C
ANISOU 4402 CD PRO A 577 5604 2668 7744 86 -3830 -96 C
ATOM 4403 N TRP A 578 67.719 10.701 -1.756 1.00 47.64 N
ANISOU 4403 N TRP A 578 6196 3226 8679 -6 -4054 -8 N
ATOM 4404 CA TRP A 578 68.602 10.967 -2.886 1.00 47.61 C
ANISOU 4404 CA TRP A 578 6124 3245 8722 -51 -4046 29 C
ATOM 4405 C TRP A 578 70.036 10.546 -2.587 1.00 48.96 C
ANISOU 4405 C TRP A 578 6229 3436 8937 -86 -4080 37 C
ATOM 4406 O TRP A 578 70.570 10.837 -1.515 1.00 46.61 O
ANISOU 4406 O TRP A 578 5937 3123 8650 -89 -4147 22 O
ATOM 4407 CB TRP A 578 68.553 12.451 -3.249 1.00 45.41 C
ANISOU 4407 CB TRP A 578 5855 2940 8460 -67 -4085 49 C
ATOM 4408 CG TRP A 578 67.212 12.898 -3.751 1.00 48.65 C
ANISOU 4408 CG TRP A 578 6317 3339 8829 -38 -4047 49 C
ATOM 4409 CD1 TRP A 578 66.325 13.715 -3.111 1.00 48.55 C
ANISOU 4409 CD1 TRP A 578 6360 3323 8765 -16 -4058 27 C
ATOM 4410 CD2 TRP A 578 66.602 12.541 -4.998 1.00 45.47 C
ANISOU 4410 CD2 TRP A 578 5895 2988 8393 -42 -3959 61 C
ATOM 4411 NE1 TRP A 578 65.204 13.895 -3.886 1.00 47.08 N
ANISOU 4411 NE1 TRP A 578 6187 3188 8514 -10 -3979 25 N
ATOM 4412 CE2 TRP A 578 65.348 13.183 -5.048 1.00 45.96 C
ANISOU 4412 CE2 TRP A 578 6001 3080 8382 -25 -3919 45 C
ATOM 4413 CE3 TRP A 578 66.996 11.745 -6.077 1.00 43.75 C
ANISOU 4413 CE3 TRP A 578 5628 2796 8199 -59 -3911 83 C
ATOM 4414 CZ2 TRP A 578 64.485 13.053 -6.136 1.00 42.43 C
ANISOU 4414 CZ2 TRP A 578 5548 2686 7887 -26 -3836 51 C
ATOM 4415 CZ3 TRP A 578 66.137 11.615 -7.156 1.00 42.87 C
ANISOU 4415 CZ3 TRP A 578 5514 2737 8038 -58 -3828 86 C
ATOM 4416 CH2 TRP A 578 64.897 12.266 -7.177 1.00 42.08 C
ANISOU 4416 CH2 TRP A 578 5457 2665 7867 -42 -3793 71 C
ATOM 4417 N ASP A 579 70.658 9.866 -3.549 1.00 50.50 N
ANISOU 4417 N ASP A 579 6360 3668 9157 -112 -4035 61 N
ATOM 4418 CA ASP A 579 72.058 9.453 -3.455 1.00 50.95 C
ANISOU 4418 CA ASP A 579 6344 3753 9262 -149 -4061 76 C
ATOM 4419 C ASP A 579 72.912 10.579 -4.018 1.00 51.25 C
ANISOU 4419 C ASP A 579 6335 3784 9352 -193 -4104 112 C
ATOM 4420 O ASP A 579 72.978 10.780 -5.233 1.00 52.44 O
ANISOU 4420 O ASP A 579 6454 3950 9521 -213 -4066 140 O
ATOM 4421 CB ASP A 579 72.285 8.140 -4.199 1.00 47.27 C
ANISOU 4421 CB ASP A 579 5833 3331 8797 -154 -3991 85 C
ATOM 4422 CG ASP A 579 73.750 7.722 -4.236 1.00 47.37 C
ANISOU 4422 CG ASP A 579 5761 3378 8860 -193 -4012 107 C
ATOM 4423 OD1 ASP A 579 74.568 8.272 -3.468 1.00 50.81 O
ANISOU 4423 OD1 ASP A 579 6176 3806 9325 -212 -4084 111 O
ATOM 4424 OD2 ASP A 579 74.084 6.832 -5.046 1.00 51.11 O
ANISOU 4424 OD2 ASP A 579 6187 3889 9344 -204 -3958 123 O
ATOM 4425 N CYS A 580 73.577 11.309 -3.132 1.00 50.48 N
ANISOU 4425 N CYS A 580 6234 3668 9280 -209 -4185 109 N
ATOM 4426 CA CYS A 580 74.372 12.474 -3.517 1.00 56.90 C
ANISOU 4426 CA CYS A 580 7007 4468 10144 -251 -4237 142 C
ATOM 4427 C CYS A 580 75.856 12.134 -3.618 1.00 55.87 C
ANISOU 4427 C CYS A 580 6785 4371 10070 -295 -4262 170 C
ATOM 4428 O CYS A 580 76.708 12.762 -2.987 1.00 60.65 O
ANISOU 4428 O CYS A 580 7365 4967 10712 -321 -4338 178 O
ATOM 4429 CB CYS A 580 74.124 13.608 -2.531 1.00 61.55 C
ANISOU 4429 CB CYS A 580 7649 5011 10726 -241 -4316 123 C
ATOM 4430 SG CYS A 580 72.426 14.235 -2.573 1.00 64.68 S
ANISOU 4430 SG CYS A 580 8143 5369 11063 -193 -4289 101 S
ATOM 4431 N SER A 581 76.185 11.123 -4.418 1.00 54.48 N
ANISOU 4431 N SER A 581 6558 4238 9904 -305 -4198 187 N
ATOM 4432 CA SER A 581 77.567 10.768 -4.705 1.00 51.62 C
ANISOU 4432 CA SER A 581 6102 3915 9598 -347 -4210 221 C
ATOM 4433 C SER A 581 77.898 11.158 -6.139 1.00 58.32 C
ANISOU 4433 C SER A 581 6899 4776 10483 -380 -4175 263 C
ATOM 4434 O SER A 581 77.045 11.076 -7.030 1.00 59.30 O
ANISOU 4434 O SER A 581 7052 4900 10580 -364 -4112 261 O
ATOM 4435 CB SER A 581 77.821 9.270 -4.491 1.00 49.77 C
ANISOU 4435 CB SER A 581 5839 3724 9349 -334 -4168 210 C
ATOM 4436 OG SER A 581 77.274 8.493 -5.542 1.00 57.97 O
ANISOU 4436 OG SER A 581 6876 4783 10366 -321 -4081 214 O
ATOM 4437 N CYS A 582 79.132 11.605 -6.354 1.00 56.06 N
ANISOU 4437 N CYS A 582 6535 4504 10260 -426 -4216 302 N
ATOM 4438 CA CYS A 582 79.489 12.019 -7.706 1.00 60.19 C
ANISOU 4438 CA CYS A 582 7007 5040 10822 -459 -4184 344 C
ATOM 4439 C CYS A 582 80.123 10.859 -8.466 1.00 58.01 C
ANISOU 4439 C CYS A 582 6659 4818 10564 -471 -4123 367 C
ATOM 4440 O CYS A 582 80.824 10.039 -7.868 1.00 60.83 O
ANISOU 4440 O CYS A 582 6975 5206 10932 -473 -4134 367 O
ATOM 4441 CB CYS A 582 80.456 13.198 -7.670 1.00 63.09 C
ANISOU 4441 CB CYS A 582 7326 5392 11253 -505 -4258 379 C
ATOM 4442 SG CYS A 582 79.748 14.702 -6.968 1.00 72.16 S
ANISOU 4442 SG CYS A 582 8555 6476 12386 -495 -4331 356 S
ATOM 4443 N PRO A 583 79.920 10.767 -9.791 1.00 56.37 N
ANISOU 4443 N PRO A 583 6431 4626 10360 -478 -4058 388 N
ATOM 4444 CA PRO A 583 79.198 11.714 -10.650 1.00 61.11 C
ANISOU 4444 CA PRO A 583 7066 5201 10951 -478 -4041 394 C
ATOM 4445 C PRO A 583 77.706 11.425 -10.805 1.00 57.01 C
ANISOU 4445 C PRO A 583 6632 4667 10360 -431 -3988 356 C
ATOM 4446 O PRO A 583 77.103 11.892 -11.768 1.00 59.77 O
ANISOU 4446 O PRO A 583 7000 5014 10698 -430 -3952 364 O
ATOM 4447 CB PRO A 583 79.902 11.541 -11.992 1.00 59.60 C
ANISOU 4447 CB PRO A 583 6796 5047 10803 -511 -3995 439 C
ATOM 4448 CG PRO A 583 80.227 10.079 -12.015 1.00 55.43 C
ANISOU 4448 CG PRO A 583 6233 4563 10266 -500 -3947 434 C
ATOM 4449 CD PRO A 583 80.555 9.699 -10.586 1.00 52.95 C
ANISOU 4449 CD PRO A 583 5926 4245 9946 -490 -4000 412 C
ATOM 4450 N ARG A 584 77.120 10.675 -9.872 1.00 48.07 N
ANISOU 4450 N ARG A 584 5551 3530 9183 -394 -3984 317 N
ATOM 4451 CA ARG A 584 75.739 10.234 -10.043 1.00 46.93 C
ANISOU 4451 CA ARG A 584 5480 3379 8973 -350 -3928 284 C
ATOM 4452 C ARG A 584 74.757 11.392 -9.893 1.00 50.96 C
ANISOU 4452 C ARG A 584 6060 3847 9456 -332 -3952 272 C
ATOM 4453 O ARG A 584 73.835 11.547 -10.704 1.00 50.75 O
ANISOU 4453 O ARG A 584 6065 3820 9397 -316 -3905 270 O
ATOM 4454 CB ARG A 584 75.423 9.123 -9.044 1.00 46.61 C
ANISOU 4454 CB ARG A 584 5471 3343 8895 -316 -3920 248 C
ATOM 4455 CG ARG A 584 74.029 8.540 -9.172 1.00 45.47 C
ANISOU 4455 CG ARG A 584 5396 3194 8686 -271 -3862 216 C
ATOM 4456 CD ARG A 584 73.819 7.418 -8.170 1.00 49.44 C
ANISOU 4456 CD ARG A 584 5924 3703 9159 -241 -3855 183 C
ATOM 4457 NE ARG A 584 72.540 6.738 -8.354 1.00 54.47 N
ANISOU 4457 NE ARG A 584 6619 4338 9739 -200 -3796 157 N
ATOM 4458 CZ ARG A 584 72.131 5.711 -7.618 1.00 58.40 C
ANISOU 4458 CZ ARG A 584 7145 4840 10203 -170 -3778 127 C
ATOM 4459 NH1 ARG A 584 72.899 5.242 -6.645 1.00 59.84 N
ANISOU 4459 NH1 ARG A 584 7304 5030 10401 -175 -3815 118 N
ATOM 4460 NH2 ARG A 584 70.952 5.150 -7.852 1.00 53.84 N
ANISOU 4460 NH2 ARG A 584 6617 4261 9577 -135 -3725 107 N
ATOM 4461 N ILE A 585 74.941 12.222 -8.868 1.00 53.26 N
ANISOU 4461 N ILE A 585 6374 4104 9759 -335 -4027 264 N
ATOM 4462 CA ILE A 585 73.993 13.286 -8.548 1.00 49.72 C
ANISOU 4462 CA ILE A 585 5995 3614 9281 -313 -4055 249 C
ATOM 4463 C ILE A 585 74.300 14.521 -9.390 1.00 47.87 C
ANISOU 4463 C ILE A 585 5735 3370 9085 -347 -4076 283 C
ATOM 4464 O ILE A 585 73.719 15.593 -9.182 1.00 48.00 O
ANISOU 4464 O ILE A 585 5797 3351 9088 -338 -4110 278 O
ATOM 4465 CB ILE A 585 74.028 13.604 -7.040 1.00 48.08 C
ANISOU 4465 CB ILE A 585 5828 3373 9066 -299 -4128 222 C
ATOM 4466 CG1 ILE A 585 72.734 14.286 -6.585 1.00 47.66 C
ANISOU 4466 CG1 ILE A 585 5863 3282 8963 -259 -4138 195 C
ATOM 4467 CG2 ILE A 585 75.256 14.437 -6.686 1.00 49.36 C
ANISOU 4467 CG2 ILE A 585 5940 3524 9289 -343 -4208 245 C
ATOM 4468 CD1 ILE A 585 71.536 13.359 -6.537 1.00 50.66 C
ANISOU 4468 CD1 ILE A 585 6297 3671 9281 -212 -4073 167 C
ATOM 4469 N ASP A 586 75.193 14.366 -10.371 1.00 48.09 N
ANISOU 4469 N ASP A 586 5687 3429 9158 -385 -4053 319 N
ATOM 4470 CA ASP A 586 75.701 15.520 -11.109 1.00 49.12 C
ANISOU 4470 CA ASP A 586 5779 3550 9334 -423 -4080 356 C
ATOM 4471 C ASP A 586 74.600 16.206 -11.910 1.00 47.98 C
ANISOU 4471 C ASP A 586 5680 3396 9155 -406 -4046 355 C
ATOM 4472 O ASP A 586 74.412 17.423 -11.801 1.00 48.39 O
ANISOU 4472 O ASP A 586 5755 3416 9215 -414 -4091 362 O
ATOM 4473 CB ASP A 586 76.847 15.095 -12.027 1.00 53.23 C
ANISOU 4473 CB ASP A 586 6206 4110 9909 -465 -4054 396 C
ATOM 4474 CG ASP A 586 77.533 16.277 -12.688 1.00 61.01 C
ANISOU 4474 CG ASP A 586 7143 5085 10951 -509 -4089 438 C
ATOM 4475 OD1 ASP A 586 77.339 17.420 -12.222 1.00 65.14 O
ANISOU 4475 OD1 ASP A 586 7700 5570 11481 -512 -4147 435 O
ATOM 4476 OD2 ASP A 586 78.266 16.064 -13.677 1.00 66.85 O
ANISOU 4476 OD2 ASP A 586 7812 5857 11731 -539 -4057 473 O
ATOM 4477 N TYR A 587 73.874 15.449 -12.738 1.00 48.62 N
ANISOU 4477 N TYR A 587 5774 3505 9196 -385 -3968 348 N
ATOM 4478 CA TYR A 587 72.825 16.056 -13.554 1.00 46.31 C
ANISOU 4478 CA TYR A 587 5519 3209 8867 -370 -3933 348 C
ATOM 4479 C TYR A 587 71.766 16.716 -12.681 1.00 46.16 C
ANISOU 4479 C TYR A 587 5582 3152 8804 -334 -3966 321 C
ATOM 4480 O TYR A 587 71.356 17.852 -12.934 1.00 49.26 O
ANISOU 4480 O TYR A 587 5998 3526 9195 -337 -3987 330 O
ATOM 4481 CB TYR A 587 72.176 15.015 -14.469 1.00 45.26 C
ANISOU 4481 CB TYR A 587 5389 3115 8692 -350 -3847 340 C
ATOM 4482 CG TYR A 587 70.886 15.512 -15.098 1.00 52.45 C
ANISOU 4482 CG TYR A 587 6352 4025 9553 -325 -3813 333 C
ATOM 4483 CD1 TYR A 587 70.911 16.374 -16.188 1.00 59.33 C
ANISOU 4483 CD1 TYR A 587 7199 4904 10439 -349 -3803 360 C
ATOM 4484 CD2 TYR A 587 69.647 15.131 -14.592 1.00 51.49 C
ANISOU 4484 CD2 TYR A 587 6300 3897 9369 -279 -3791 300 C
ATOM 4485 CE1 TYR A 587 69.740 16.840 -16.761 1.00 56.88 C
ANISOU 4485 CE1 TYR A 587 6933 4596 10081 -328 -3773 353 C
ATOM 4486 CE2 TYR A 587 68.470 15.592 -15.159 1.00 48.31 C
ANISOU 4486 CE2 TYR A 587 5939 3496 8919 -258 -3761 296 C
ATOM 4487 CZ TYR A 587 68.524 16.446 -16.243 1.00 47.38 C
ANISOU 4487 CZ TYR A 587 5798 3389 8816 -283 -3752 322 C
ATOM 4488 OH TYR A 587 67.356 16.905 -16.810 1.00 42.60 O
ANISOU 4488 OH TYR A 587 5233 2789 8164 -264 -3723 318 O
ATOM 4489 N LEU A 588 71.313 16.015 -11.641 1.00 45.90 N
ANISOU 4489 N LEU A 588 5594 3110 8736 -299 -3969 287 N
ATOM 4490 CA LEU A 588 70.204 16.511 -10.832 1.00 45.65 C
ANISOU 4490 CA LEU A 588 5642 3046 8658 -260 -3991 260 C
ATOM 4491 C LEU A 588 70.598 17.764 -10.059 1.00 46.62 C
ANISOU 4491 C LEU A 588 5777 3126 8810 -275 -4077 263 C
ATOM 4492 O LEU A 588 69.835 18.735 -10.006 1.00 46.56 O
ANISOU 4492 O LEU A 588 5816 3094 8781 -261 -4096 260 O
ATOM 4493 CB LEU A 588 69.723 15.413 -9.880 1.00 48.95 C
ANISOU 4493 CB LEU A 588 6099 3463 9036 -222 -3976 225 C
ATOM 4494 CG LEU A 588 68.489 15.710 -9.032 1.00 48.43 C
ANISOU 4494 CG LEU A 588 6116 3368 8918 -176 -3987 195 C
ATOM 4495 CD1 LEU A 588 67.381 16.290 -9.898 1.00 44.81 C
ANISOU 4495 CD1 LEU A 588 5688 2914 8423 -161 -3949 203 C
ATOM 4496 CD2 LEU A 588 68.013 14.450 -8.316 1.00 46.39 C
ANISOU 4496 CD2 LEU A 588 5887 3118 8622 -140 -3957 164 C
ATOM 4497 N SER A 589 71.787 17.760 -9.451 1.00 48.80 N
ANISOU 4497 N SER A 589 6011 3396 9135 -304 -4131 270 N
ATOM 4498 CA SER A 589 72.227 18.908 -8.663 1.00 48.57 C
ANISOU 4498 CA SER A 589 5993 3327 9136 -320 -4219 272 C
ATOM 4499 C SER A 589 72.398 20.145 -9.535 1.00 48.93 C
ANISOU 4499 C SER A 589 6016 3363 9213 -352 -4236 305 C
ATOM 4500 O SER A 589 71.948 21.240 -9.176 1.00 49.23 O
ANISOU 4500 O SER A 589 6097 3365 9243 -344 -4282 299 O
ATOM 4501 CB SER A 589 73.529 18.571 -7.936 1.00 53.91 C
ANISOU 4501 CB SER A 589 6618 4004 9860 -350 -4272 276 C
ATOM 4502 OG SER A 589 74.476 18.007 -8.825 1.00 54.09 O
ANISOU 4502 OG SER A 589 6559 4065 9925 -386 -4238 308 O
ATOM 4503 N ARG A 590 73.052 19.991 -10.690 1.00 54.00 N
ANISOU 4503 N ARG A 590 6590 4036 9892 -386 -4200 338 N
ATOM 4504 CA ARG A 590 73.207 21.120 -11.602 1.00 54.94 C
ANISOU 4504 CA ARG A 590 6684 4148 10041 -416 -4211 371 C
ATOM 4505 C ARG A 590 71.861 21.575 -12.150 1.00 56.05 C
ANISOU 4505 C ARG A 590 6881 4287 10128 -385 -4171 362 C
ATOM 4506 O ARG A 590 71.627 22.778 -12.321 1.00 55.11 O
ANISOU 4506 O ARG A 590 6778 4143 10016 -394 -4204 373 O
ATOM 4507 CB ARG A 590 74.148 20.754 -12.750 1.00 55.64 C
ANISOU 4507 CB ARG A 590 6687 4274 10178 -457 -4173 408 C
ATOM 4508 CG ARG A 590 75.595 20.552 -12.342 1.00 53.14 C
ANISOU 4508 CG ARG A 590 6301 3962 9927 -497 -4220 429 C
ATOM 4509 CD ARG A 590 76.476 20.342 -13.566 1.00 57.86 C
ANISOU 4509 CD ARG A 590 6813 4596 10575 -537 -4182 472 C
ATOM 4510 NE ARG A 590 77.823 19.916 -13.203 1.00 67.22 N
ANISOU 4510 NE ARG A 590 7928 5795 11820 -572 -4215 492 N
ATOM 4511 CZ ARG A 590 78.809 20.745 -12.880 1.00 65.32 C
ANISOU 4511 CZ ARG A 590 7643 5534 11641 -613 -4288 519 C
ATOM 4512 NH1 ARG A 590 78.605 22.056 -12.870 1.00 54.28 N
ANISOU 4512 NH1 ARG A 590 6267 4100 10256 -625 -4337 526 N
ATOM 4513 NH2 ARG A 590 80.002 20.262 -12.562 1.00 66.40 N
ANISOU 4513 NH2 ARG A 590 7711 5689 11829 -643 -4314 539 N
ATOM 4514 N TRP A 591 70.963 20.629 -12.433 1.00 51.01 N
ANISOU 4514 N TRP A 591 6272 3674 9434 -350 -4100 342 N
ATOM 4515 CA TRP A 591 69.650 20.995 -12.954 1.00 47.61 C
ANISOU 4515 CA TRP A 591 5894 3246 8950 -320 -4060 335 C
ATOM 4516 C TRP A 591 68.819 21.704 -11.893 1.00 46.59 C
ANISOU 4516 C TRP A 591 5838 3075 8787 -287 -4107 310 C
ATOM 4517 O TRP A 591 68.172 22.720 -12.172 1.00 46.53 O
ANISOU 4517 O TRP A 591 5861 3053 8764 -282 -4118 316 O
ATOM 4518 CB TRP A 591 68.914 19.759 -13.465 1.00 45.41 C
ANISOU 4518 CB TRP A 591 5626 3005 8622 -291 -3977 320 C
ATOM 4519 CG TRP A 591 67.649 20.096 -14.184 1.00 44.60 C
ANISOU 4519 CG TRP A 591 5564 2914 8469 -268 -3933 318 C
ATOM 4520 CD1 TRP A 591 67.488 20.229 -15.530 1.00 44.21 C
ANISOU 4520 CD1 TRP A 591 5485 2896 8416 -284 -3884 338 C
ATOM 4521 CD2 TRP A 591 66.367 20.361 -13.598 1.00 44.13 C
ANISOU 4521 CD2 TRP A 591 5578 2836 8353 -225 -3933 294 C
ATOM 4522 NE1 TRP A 591 66.187 20.554 -15.822 1.00 43.52 N
ANISOU 4522 NE1 TRP A 591 5450 2813 8274 -255 -3855 329 N
ATOM 4523 CE2 TRP A 591 65.478 20.641 -14.654 1.00 43.46 C
ANISOU 4523 CE2 TRP A 591 5504 2775 8234 -219 -3884 303 C
ATOM 4524 CE3 TRP A 591 65.884 20.385 -12.286 1.00 44.22 C
ANISOU 4524 CE3 TRP A 591 5646 2814 8340 -192 -3971 267 C
ATOM 4525 CZ2 TRP A 591 64.137 20.944 -14.440 1.00 42.89 C
ANISOU 4525 CZ2 TRP A 591 5485 2730 8081 -193 -3847 276 C
ATOM 4526 CZ3 TRP A 591 64.550 20.686 -12.075 1.00 43.64 C
ANISOU 4526 CZ3 TRP A 591 5625 2774 8182 -167 -3929 238 C
ATOM 4527 CH2 TRP A 591 63.692 20.960 -13.147 1.00 42.99 C
ANISOU 4527 CH2 TRP A 591 5544 2733 8056 -169 -3867 244 C
ATOM 4528 N LEU A 592 68.807 21.165 -10.670 1.00 46.72 N
ANISOU 4528 N LEU A 592 5887 3075 8790 -264 -4135 281 N
ATOM 4529 CA LEU A 592 68.051 21.798 -9.594 1.00 46.85 C
ANISOU 4529 CA LEU A 592 5975 3052 8774 -231 -4181 256 C
ATOM 4530 C LEU A 592 68.610 23.170 -9.247 1.00 50.58 C
ANISOU 4530 C LEU A 592 6445 3486 9287 -258 -4264 269 C
ATOM 4531 O LEU A 592 67.861 24.050 -8.811 1.00 47.94 O
ANISOU 4531 O LEU A 592 6167 3122 8927 -237 -4296 258 O
ATOM 4532 CB LEU A 592 68.037 20.896 -8.359 1.00 46.85 C
ANISOU 4532 CB LEU A 592 6004 3043 8756 -203 -4195 223 C
ATOM 4533 CG LEU A 592 67.001 19.772 -8.351 1.00 55.48 C
ANISOU 4533 CG LEU A 592 7132 4157 9790 -160 -4125 201 C
ATOM 4534 CD1 LEU A 592 67.048 19.005 -7.038 1.00 49.11 C
ANISOU 4534 CD1 LEU A 592 6354 3336 8968 -134 -4147 168 C
ATOM 4535 CD2 LEU A 592 65.612 20.341 -8.593 1.00 54.19 C
ANISOU 4535 CD2 LEU A 592 7019 4014 9558 -135 -4083 188 C
ATOM 4536 N ASN A 593 69.917 23.373 -9.429 1.00 50.41 N
ANISOU 4536 N ASN A 593 6358 3466 9329 -305 -4301 292 N
ATOM 4537 CA ASN A 593 70.502 24.686 -9.177 1.00 52.51 C
ANISOU 4537 CA ASN A 593 6617 3697 9639 -336 -4381 307 C
ATOM 4538 C ASN A 593 70.102 25.679 -10.262 1.00 52.30 C
ANISOU 4538 C ASN A 593 6585 3672 9615 -350 -4364 333 C
ATOM 4539 O ASN A 593 69.661 26.796 -9.963 1.00 49.95 O
ANISOU 4539 O ASN A 593 6328 3342 9310 -344 -4410 329 O
ATOM 4540 CB ASN A 593 72.024 24.571 -9.078 1.00 52.84 C
ANISOU 4540 CB ASN A 593 6585 3742 9751 -385 -4424 328 C
ATOM 4541 CG ASN A 593 72.674 25.838 -8.556 1.00 52.59 C
ANISOU 4541 CG ASN A 593 6548 3670 9765 -416 -4519 337 C
ATOM 4542 OD1 ASN A 593 72.638 26.116 -7.357 1.00 52.57 O
ANISOU 4542 OD1 ASN A 593 6589 3634 9753 -401 -4583 311 O
ATOM 4543 ND2 ASN A 593 73.279 26.609 -9.452 1.00 52.51 N
ANISOU 4543 ND2 ASN A 593 6484 3661 9804 -459 -4530 375 N
ATOM 4544 N LYS A 594 70.238 25.285 -11.531 1.00 56.37 N
ANISOU 4544 N LYS A 594 7050 4226 10140 -368 -4298 357 N
ATOM 4545 CA LYS A 594 69.891 26.185 -12.627 1.00 56.12 C
ANISOU 4545 CA LYS A 594 7010 4202 10112 -382 -4279 382 C
ATOM 4546 C LYS A 594 68.401 26.502 -12.647 1.00 60.42 C
ANISOU 4546 C LYS A 594 7626 4742 10588 -338 -4251 363 C
ATOM 4547 O LYS A 594 68.004 27.596 -13.066 1.00 60.15 O
ANISOU 4547 O LYS A 594 7606 4695 10552 -345 -4266 376 O
ATOM 4548 CB LYS A 594 70.323 25.577 -13.963 1.00 54.16 C
ANISOU 4548 CB LYS A 594 6696 4000 9883 -408 -4211 410 C
ATOM 4549 CG LYS A 594 70.282 26.554 -15.127 1.00 61.27 C
ANISOU 4549 CG LYS A 594 7570 4907 10802 -434 -4200 441 C
ATOM 4550 CD LYS A 594 70.915 25.970 -16.383 1.00 69.85 C
ANISOU 4550 CD LYS A 594 8586 6038 11918 -464 -4142 469 C
ATOM 4551 CE LYS A 594 69.925 25.161 -17.202 1.00 75.30 C
ANISOU 4551 CE LYS A 594 9296 6769 12548 -434 -4054 457 C
ATOM 4552 NZ LYS A 594 70.520 24.750 -18.505 1.00 74.91 N
ANISOU 4552 NZ LYS A 594 9178 6760 12525 -465 -4001 485 N
ATOM 4553 N ASN A 595 67.565 25.570 -12.194 1.00 61.54 N
ANISOU 4553 N ASN A 595 7812 4894 10674 -295 -4210 335 N
ATOM 4554 CA ASN A 595 66.114 25.729 -12.181 1.00 55.80 C
ANISOU 4554 CA ASN A 595 7152 4168 9883 -252 -4179 318 C
ATOM 4555 C ASN A 595 65.571 25.817 -10.757 1.00 49.06 C
ANISOU 4555 C ASN A 595 6365 3276 8998 -213 -4224 285 C
ATOM 4556 O ASN A 595 64.499 25.291 -10.451 1.00 45.91 O
ANISOU 4556 O ASN A 595 6006 2919 8519 -182 -4163 252 O
ATOM 4557 CB ASN A 595 65.444 24.583 -12.935 1.00 45.44 C
ANISOU 4557 CB ASN A 595 5836 2902 8528 -231 -4089 313 C
ATOM 4558 CG ASN A 595 65.840 24.534 -14.398 1.00 45.24 C
ANISOU 4558 CG ASN A 595 5751 2915 8525 -265 -4041 342 C
ATOM 4559 OD1 ASN A 595 65.236 25.199 -15.239 1.00 50.85 O
ANISOU 4559 OD1 ASN A 595 6467 3636 9218 -267 -4018 356 O
ATOM 4560 ND2 ASN A 595 66.858 23.738 -14.710 1.00 45.43 N
ANISOU 4560 ND2 ASN A 595 5716 2960 8587 -291 -4025 353 N
ATOM 4561 N SER A 596 66.305 26.495 -9.870 1.00 47.70 N
ANISOU 4561 N SER A 596 6196 3065 8862 -229 -4306 281 N
ATOM 4562 CA SER A 596 65.919 26.558 -8.465 1.00 48.12 C
ANISOU 4562 CA SER A 596 6311 3082 8890 -195 -4355 249 C
ATOM 4563 C SER A 596 64.624 27.326 -8.235 1.00 47.58 C
ANISOU 4563 C SER A 596 6304 3023 8750 -168 -4338 227 C
ATOM 4564 O SER A 596 64.004 27.158 -7.180 1.00 47.46 O
ANISOU 4564 O SER A 596 6339 3011 8681 -137 -4338 189 O
ATOM 4565 CB SER A 596 67.041 27.186 -7.637 1.00 50.25 C
ANISOU 4565 CB SER A 596 6565 3315 9211 -225 -4448 248 C
ATOM 4566 OG SER A 596 67.436 28.432 -8.181 1.00 53.03 O
ANISOU 4566 OG SER A 596 6895 3652 9602 -260 -4489 274 O
ATOM 4567 N GLN A 597 64.201 28.170 -9.179 1.00 47.37 N
ANISOU 4567 N GLN A 597 6271 3010 8715 -181 -4317 247 N
ATOM 4568 CA GLN A 597 62.933 28.865 -8.988 1.00 52.79 C
ANISOU 4568 CA GLN A 597 7011 3721 9326 -159 -4288 223 C
ATOM 4569 C GLN A 597 61.753 27.918 -9.152 1.00 51.76 C
ANISOU 4569 C GLN A 597 6897 3662 9106 -133 -4181 196 C
ATOM 4570 O GLN A 597 60.660 28.198 -8.647 1.00 50.78 O
ANISOU 4570 O GLN A 597 6822 3559 8912 -107 -4155 168 O
ATOM 4571 CB GLN A 597 62.803 30.036 -9.963 1.00 55.40 C
ANISOU 4571 CB GLN A 597 7330 4046 9674 -182 -4297 252 C
ATOM 4572 CG GLN A 597 62.108 29.697 -11.278 1.00 67.75 C
ANISOU 4572 CG GLN A 597 8870 5673 11198 -186 -4199 263 C
ATOM 4573 CD GLN A 597 63.084 29.355 -12.385 1.00 75.53 C
ANISOU 4573 CD GLN A 597 9789 6657 12253 -218 -4194 302 C
ATOM 4574 OE1 GLN A 597 64.236 29.010 -12.125 1.00 78.52 O
ANISOU 4574 OE1 GLN A 597 10136 6998 12702 -234 -4246 318 O
ATOM 4575 NE2 GLN A 597 62.630 29.460 -13.628 1.00 75.00 N
ANISOU 4575 NE2 GLN A 597 9701 6629 12168 -229 -4133 319 N
ATOM 4576 N LYS A 598 61.955 26.793 -9.843 1.00 51.07 N
ANISOU 4576 N LYS A 598 6770 3611 9023 -138 -4120 203 N
ATOM 4577 CA LYS A 598 60.860 25.870 -10.112 1.00 45.15 C
ANISOU 4577 CA LYS A 598 6033 2928 8194 -116 -4020 181 C
ATOM 4578 C LYS A 598 60.673 24.860 -8.988 1.00 46.33 C
ANISOU 4578 C LYS A 598 6207 3087 8310 -89 -4007 147 C
ATOM 4579 O LYS A 598 59.547 24.412 -8.747 1.00 45.04 O
ANISOU 4579 O LYS A 598 6074 2968 8071 -64 -3943 121 O
ATOM 4580 CB LYS A 598 61.104 25.152 -11.442 1.00 43.63 C
ANISOU 4580 CB LYS A 598 5789 2772 8019 -135 -3960 205 C
ATOM 4581 CG LYS A 598 61.287 26.112 -12.619 1.00 52.46 C
ANISOU 4581 CG LYS A 598 6879 3883 9170 -163 -3969 240 C
ATOM 4582 CD LYS A 598 61.712 25.402 -13.900 1.00 50.49 C
ANISOU 4582 CD LYS A 598 6576 3660 8947 -182 -3922 265 C
ATOM 4583 CE LYS A 598 61.822 26.389 -15.057 1.00 48.95 C
ANISOU 4583 CE LYS A 598 6357 3460 8782 -208 -3929 299 C
ATOM 4584 NZ LYS A 598 62.349 25.772 -16.310 1.00 52.09 N
ANISOU 4584 NZ LYS A 598 6700 3877 9213 -229 -3891 326 N
ATOM 4585 N GLU A 599 61.743 24.497 -8.285 1.00 49.19 N
ANISOU 4585 N GLU A 599 6555 3407 8728 -93 -4069 148 N
ATOM 4586 CA GLU A 599 61.627 23.488 -7.243 1.00 48.00 C
ANISOU 4586 CA GLU A 599 6425 3264 8548 -67 -4058 116 C
ATOM 4587 C GLU A 599 60.788 24.002 -6.080 1.00 46.68 C
ANISOU 4587 C GLU A 599 6321 3090 8325 -38 -4076 82 C
ATOM 4588 O GLU A 599 61.012 25.105 -5.574 1.00 45.95 O
ANISOU 4588 O GLU A 599 6254 2951 8256 -41 -4151 84 O
ATOM 4589 CB GLU A 599 63.005 23.065 -6.746 1.00 45.26 C
ANISOU 4589 CB GLU A 599 6050 2869 8278 -80 -4128 125 C
ATOM 4590 CG GLU A 599 62.939 22.137 -5.549 1.00 47.08 C
ANISOU 4590 CG GLU A 599 6306 3101 8483 -53 -4129 91 C
ATOM 4591 CD GLU A 599 64.267 21.491 -5.253 1.00 51.84 C
ANISOU 4591 CD GLU A 599 6873 3666 9160 -68 -4182 102 C
ATOM 4592 OE1 GLU A 599 64.273 20.324 -4.811 1.00 54.32 O
ANISOU 4592 OE1 GLU A 599 7184 3999 9456 -52 -4151 83 O
ATOM 4593 OE2 GLU A 599 65.305 22.148 -5.473 1.00 56.69 O
ANISOU 4593 OE2 GLU A 599 7457 4228 9852 -96 -4257 133 O
ATOM 4594 N GLN A 600 59.821 23.191 -5.659 1.00 47.07 N
ANISOU 4594 N GLN A 600 6396 3185 8303 -10 -4009 53 N
ATOM 4595 CA GLN A 600 58.986 23.475 -4.500 1.00 45.40 C
ANISOU 4595 CA GLN A 600 6242 2971 8035 21 -4017 20 C
ATOM 4596 C GLN A 600 59.445 22.583 -3.353 1.00 45.23 C
ANISOU 4596 C GLN A 600 6233 2934 8021 39 -4044 -5 C
ATOM 4597 O GLN A 600 59.508 21.359 -3.503 1.00 43.63 O
ANISOU 4597 O GLN A 600 6005 2762 7809 42 -3992 -9 O
ATOM 4598 CB GLN A 600 57.511 23.233 -4.821 1.00 45.68 C
ANISOU 4598 CB GLN A 600 6299 3070 7987 38 -3922 7 C
ATOM 4599 CG GLN A 600 57.057 23.799 -6.163 1.00 42.45 C
ANISOU 4599 CG GLN A 600 5870 2689 7571 19 -3880 32 C
ATOM 4600 CD GLN A 600 57.077 25.315 -6.200 1.00 43.04 C
ANISOU 4600 CD GLN A 600 5964 2727 7662 9 -3939 44 C
ATOM 4601 OE1 GLN A 600 56.470 25.978 -5.358 1.00 43.24 O
ANISOU 4601 OE1 GLN A 600 6037 2740 7652 29 -3962 24 O
ATOM 4602 NE2 GLN A 600 57.783 25.873 -7.178 1.00 43.35 N
ANISOU 4602 NE2 GLN A 600 5966 2747 7756 -21 -3964 76 N
ATOM 4603 N GLY A 601 59.765 23.190 -2.217 1.00 44.93 N
ANISOU 4603 N GLY A 601 6231 2844 7996 51 -4126 -22 N
ATOM 4604 CA GLY A 601 60.396 22.439 -1.155 1.00 45.34 C
ANISOU 4604 CA GLY A 601 6290 2870 8067 65 -4167 -42 C
ATOM 4605 C GLY A 601 61.871 22.232 -1.450 1.00 49.19 C
ANISOU 4605 C GLY A 601 6730 3316 8645 36 -4228 -16 C
ATOM 4606 O GLY A 601 62.471 22.906 -2.294 1.00 51.96 O
ANISOU 4606 O GLY A 601 7048 3645 9050 6 -4258 17 O
ATOM 4607 N SER A 602 62.459 21.266 -0.749 1.00 50.74 N
ANISOU 4607 N SER A 602 6919 3500 8860 44 -4246 -31 N
ATOM 4608 CA SER A 602 63.896 21.028 -0.836 1.00 54.71 C
ANISOU 4608 CA SER A 602 7378 3957 9452 19 -4313 -8 C
ATOM 4609 C SER A 602 64.163 19.532 -0.877 1.00 56.84 C
ANISOU 4609 C SER A 602 7617 4257 9722 23 -4263 -14 C
ATOM 4610 O SER A 602 63.955 18.834 0.121 1.00 61.55 O
ANISOU 4610 O SER A 602 8240 4858 10288 49 -4261 -46 O
ATOM 4611 CB SER A 602 64.629 21.672 0.339 1.00 49.81 C
ANISOU 4611 CB SER A 602 6787 3264 8876 23 -4432 -19 C
ATOM 4612 OG SER A 602 64.563 23.084 0.260 1.00 53.58 O
ANISOU 4612 OG SER A 602 7286 3706 9367 14 -4488 -8 O
ATOM 4613 N ALA A 603 64.629 19.045 -2.025 1.00 55.98 N
ANISOU 4613 N ALA A 603 7452 4169 9648 -3 -4223 17 N
ATOM 4614 CA ALA A 603 65.206 17.710 -2.107 1.00 58.85 C
ANISOU 4614 CA ALA A 603 7778 4548 10034 -6 -4196 18 C
ATOM 4615 C ALA A 603 66.540 17.718 -1.371 1.00 61.59 C
ANISOU 4615 C ALA A 603 8110 4828 10463 -19 -4299 25 C
ATOM 4616 O ALA A 603 67.484 18.400 -1.787 1.00 59.30 O
ANISOU 4616 O ALA A 603 7776 4531 10225 -59 -4342 51 O
ATOM 4617 CB ALA A 603 65.381 17.294 -3.564 1.00 45.32 C
ANISOU 4617 CB ALA A 603 6011 2870 8340 -31 -4133 50 C
ATOM 4618 N LYS A 604 66.620 16.985 -0.266 1.00 60.71 N
ANISOU 4618 N LYS A 604 8021 4708 10338 4 -4319 -5 N
ATOM 4619 CA LYS A 604 67.805 16.974 0.577 1.00 59.75 C
ANISOU 4619 CA LYS A 604 7872 4578 10251 -19 -4389 -15 C
ATOM 4620 C LYS A 604 68.447 15.596 0.550 1.00 59.98 C
ANISOU 4620 C LYS A 604 7852 4647 10290 -29 -4352 -17 C
ATOM 4621 O LYS A 604 67.758 14.576 0.434 1.00 63.18 O
ANISOU 4621 O LYS A 604 8273 5072 10662 -1 -4286 -29 O
ATOM 4622 CB LYS A 604 67.464 17.369 2.016 1.00 58.19 C
ANISOU 4622 CB LYS A 604 7741 4344 10026 14 -4453 -53 C
ATOM 4623 CG LYS A 604 66.658 18.657 2.131 1.00 61.46 C
ANISOU 4623 CG LYS A 604 8213 4718 10420 33 -4486 -54 C
ATOM 4624 CD LYS A 604 66.519 19.077 3.585 1.00 63.99 C
ANISOU 4624 CD LYS A 604 8595 5001 10718 62 -4559 -92 C
ATOM 4625 CE LYS A 604 65.072 19.065 4.056 1.00 60.54 C
ANISOU 4625 CE LYS A 604 8221 4589 10192 105 -4504 -125 C
ATOM 4626 NZ LYS A 604 64.439 20.412 3.972 1.00 56.47 N
ANISOU 4626 NZ LYS A 604 7743 4064 9652 108 -4521 -124 N
ATOM 4627 N CYS A 605 69.770 15.576 0.670 1.00 61.36 N
ANISOU 4627 N CYS A 605 7967 4834 10513 -69 -4396 -5 N
ATOM 4628 CA CYS A 605 70.518 14.335 0.549 1.00 62.34 C
ANISOU 4628 CA CYS A 605 8034 5000 10654 -85 -4364 -2 C
ATOM 4629 C CYS A 605 70.301 13.444 1.762 1.00 60.83 C
ANISOU 4629 C CYS A 605 7876 4811 10426 -51 -4371 -41 C
ATOM 4630 O CYS A 605 70.172 13.923 2.892 1.00 61.20 O
ANISOU 4630 O CYS A 605 7968 4828 10455 -31 -4433 -69 O
ATOM 4631 CB CYS A 605 72.001 14.638 0.385 1.00 65.30 C
ANISOU 4631 CB CYS A 605 8332 5388 11090 -138 -4415 25 C
ATOM 4632 SG CYS A 605 72.327 15.607 -1.080 1.00 72.38 S
ANISOU 4632 SG CYS A 605 9183 6286 12033 -181 -4404 74 S
ATOM 4633 N SER A 606 70.261 12.139 1.516 1.00 58.86 N
ANISOU 4633 N SER A 606 7603 4596 10164 -43 -4308 -45 N
ATOM 4634 CA SER A 606 70.200 11.156 2.589 1.00 58.70 C
ANISOU 4634 CA SER A 606 7602 4587 10114 -16 -4310 -80 C
ATOM 4635 C SER A 606 71.455 11.236 3.448 1.00 61.57 C
ANISOU 4635 C SER A 606 7926 4960 10508 -40 -4387 -84 C
ATOM 4636 O SER A 606 72.567 11.301 2.926 1.00 65.93 O
ANISOU 4636 O SER A 606 8406 5536 11109 -85 -4403 -53 O
ATOM 4637 CB SER A 606 70.037 9.746 2.019 1.00 60.66 C
ANISOU 4637 CB SER A 606 7823 4875 10350 -9 -4227 -77 C
ATOM 4638 OG SER A 606 71.002 9.486 1.013 1.00 63.96 O
ANISOU 4638 OG SER A 606 8161 5326 10813 -52 -4206 -41 O
ATOM 4639 N GLY A 609 71.207 16.088 4.406 1.00 57.40 N
ANISOU 4639 N GLY A 609 7514 4285 10012 -57 -4622 -83 N
ATOM 4640 CA GLY A 609 70.367 17.226 4.734 1.00 52.20 C
ANISOU 4640 CA GLY A 609 6927 3579 9329 -32 -4657 -96 C
ATOM 4641 C GLY A 609 70.619 18.431 3.851 1.00 58.49 C
ANISOU 4641 C GLY A 609 7701 4358 10164 -68 -4680 -60 C
ATOM 4642 O GLY A 609 69.782 19.330 3.754 1.00 68.09 O
ANISOU 4642 O GLY A 609 8970 5542 11360 -48 -4687 -62 O
ATOM 4643 N LYS A 610 71.781 18.456 3.213 1.00 58.34 N
ANISOU 4643 N LYS A 610 7603 4362 10202 -120 -4692 -27 N
ATOM 4644 CA LYS A 610 72.082 19.526 2.273 1.00 68.33 C
ANISOU 4644 CA LYS A 610 8839 5616 11509 -157 -4708 9 C
ATOM 4645 C LYS A 610 71.159 19.410 1.065 1.00 68.15 C
ANISOU 4645 C LYS A 610 8824 5605 11466 -144 -4618 29 C
ATOM 4646 O LYS A 610 70.946 18.299 0.561 1.00 67.30 O
ANISOU 4646 O LYS A 610 8695 5533 11344 -135 -4542 32 O
ATOM 4647 CB LYS A 610 73.541 19.458 1.830 1.00 73.46 C
ANISOU 4647 CB LYS A 610 9396 6292 12225 -216 -4734 43 C
ATOM 4648 CG LYS A 610 73.975 20.635 0.975 1.00 81.93 C
ANISOU 4648 CG LYS A 610 10435 7349 13345 -259 -4762 80 C
ATOM 4649 CD LYS A 610 75.139 21.373 1.606 1.00 85.76 C
ANISOU 4649 CD LYS A 610 10886 7818 13879 -300 -4865 87 C
ATOM 4650 CE LYS A 610 75.435 22.663 0.863 1.00 83.15 C
ANISOU 4650 CE LYS A 610 10534 7465 13594 -339 -4899 120 C
ATOM 4651 NZ LYS A 610 76.857 23.077 1.013 1.00 82.09 N
ANISOU 4651 NZ LYS A 610 10329 7333 13527 -396 -4976 144 N
ATOM 4652 N PRO A 611 70.578 20.512 0.590 1.00 68.47 N
ANISOU 4652 N PRO A 611 8893 5619 11503 -143 -4626 41 N
ATOM 4653 CA PRO A 611 69.753 20.441 -0.621 1.00 66.45 C
ANISOU 4653 CA PRO A 611 8638 5380 11229 -134 -4544 62 C
ATOM 4654 C PRO A 611 70.557 19.885 -1.785 1.00 64.84 C
ANISOU 4654 C PRO A 611 8351 5218 11067 -175 -4497 98 C
ATOM 4655 O PRO A 611 71.736 20.205 -1.955 1.00 67.94 O
ANISOU 4655 O PRO A 611 8683 5615 11515 -221 -4540 120 O
ATOM 4656 CB PRO A 611 69.347 21.900 -0.862 1.00 67.30 C
ANISOU 4656 CB PRO A 611 8777 5454 11340 -138 -4583 74 C
ATOM 4657 CG PRO A 611 69.496 22.567 0.466 1.00 69.96 C
ANISOU 4657 CG PRO A 611 9159 5749 11672 -127 -4675 45 C
ATOM 4658 CD PRO A 611 70.633 21.872 1.150 1.00 69.92 C
ANISOU 4658 CD PRO A 611 9112 5758 11697 -148 -4712 36 C
ATOM 4659 N VAL A 612 69.914 19.021 -2.578 1.00 57.41 N
ANISOU 4659 N VAL A 612 7406 4308 10099 -157 -4408 102 N
ATOM 4660 CA VAL A 612 70.568 18.489 -3.772 1.00 56.62 C
ANISOU 4660 CA VAL A 612 7232 4248 10033 -192 -4356 135 C
ATOM 4661 C VAL A 612 71.003 19.628 -4.682 1.00 54.81 C
ANISOU 4661 C VAL A 612 6968 4012 9846 -232 -4377 171 C
ATOM 4662 O VAL A 612 72.035 19.545 -5.358 1.00 49.84 O
ANISOU 4662 O VAL A 612 6265 3405 9267 -275 -4376 202 O
ATOM 4663 CB VAL A 612 69.644 17.500 -4.509 1.00 51.58 C
ANISOU 4663 CB VAL A 612 6606 3641 9352 -164 -4260 132 C
ATOM 4664 CG1 VAL A 612 70.346 16.920 -5.730 1.00 50.87 C
ANISOU 4664 CG1 VAL A 612 6440 3592 9295 -198 -4208 163 C
ATOM 4665 CG2 VAL A 612 69.191 16.394 -3.577 1.00 47.27 C
ANISOU 4665 CG2 VAL A 612 6096 3099 8766 -125 -4241 96 C
ATOM 4666 N ARG A 613 70.241 20.724 -4.690 1.00 51.86 N
ANISOU 4666 N ARG A 613 6643 3608 9453 -218 -4399 170 N
ATOM 4667 CA ARG A 613 70.600 21.893 -5.483 1.00 58.08 C
ANISOU 4667 CA ARG A 613 7402 4386 10279 -254 -4425 202 C
ATOM 4668 C ARG A 613 71.900 22.551 -5.034 1.00 63.98 C
ANISOU 4668 C ARG A 613 8106 5115 11089 -299 -4511 216 C
ATOM 4669 O ARG A 613 72.400 23.428 -5.746 1.00 69.44 O
ANISOU 4669 O ARG A 613 8759 5802 11822 -337 -4532 248 O
ATOM 4670 CB ARG A 613 69.473 22.928 -5.445 1.00 57.82 C
ANISOU 4670 CB ARG A 613 7436 4324 10209 -226 -4436 195 C
ATOM 4671 CG ARG A 613 69.256 23.586 -4.089 1.00 58.71 C
ANISOU 4671 CG ARG A 613 7610 4390 10306 -204 -4514 165 C
ATOM 4672 CD ARG A 613 68.790 25.028 -4.263 1.00 65.26 C
ANISOU 4672 CD ARG A 613 8474 5189 11135 -206 -4554 174 C
ATOM 4673 NE ARG A 613 68.145 25.564 -3.068 1.00 74.68 N
ANISOU 4673 NE ARG A 613 9743 6341 12293 -170 -4608 141 N
ATOM 4674 CZ ARG A 613 67.768 26.832 -2.930 1.00 85.02 C
ANISOU 4674 CZ ARG A 613 11091 7615 13598 -167 -4657 142 C
ATOM 4675 NH1 ARG A 613 67.981 27.702 -3.910 1.00 81.78 N
ANISOU 4675 NH1 ARG A 613 10648 7207 13218 -201 -4659 175 N
ATOM 4676 NH2 ARG A 613 67.184 27.234 -1.809 1.00 91.48 N
ANISOU 4676 NH2 ARG A 613 11980 8397 14381 -131 -4705 110 N
ATOM 4677 N SER A 614 72.454 22.168 -3.883 1.00 70.52 N
ANISOU 4677 N SER A 614 8937 5933 11923 -297 -4562 194 N
ATOM 4678 CA SER A 614 73.693 22.773 -3.408 1.00 75.69 C
ANISOU 4678 CA SER A 614 9549 6573 12637 -341 -4648 206 C
ATOM 4679 C SER A 614 74.832 21.761 -3.377 1.00 69.99 C
ANISOU 4679 C SER A 614 8754 5887 11952 -370 -4642 218 C
ATOM 4680 O SER A 614 75.463 21.555 -2.335 1.00 63.98 O
ANISOU 4680 O SER A 614 7988 5121 11202 -375 -4701 201 O
ATOM 4681 CB SER A 614 73.487 23.394 -2.026 1.00 84.41 C
ANISOU 4681 CB SER A 614 10717 7634 13722 -320 -4732 171 C
ATOM 4682 OG SER A 614 72.713 24.576 -2.109 1.00 93.68 O
ANISOU 4682 OG SER A 614 11945 8773 14879 -307 -4755 169 O
ATOM 4683 N ILE A 615 75.108 21.129 -4.516 1.00 69.19 N
ANISOU 4683 N ILE A 615 8595 5825 11868 -388 -4572 247 N
ATOM 4684 CA ILE A 615 76.149 20.112 -4.615 1.00 64.23 C
ANISOU 4684 CA ILE A 615 7894 5237 11274 -413 -4556 261 C
ATOM 4685 C ILE A 615 76.884 20.300 -5.930 1.00 69.82 C
ANISOU 4685 C ILE A 615 8523 5970 12036 -459 -4527 310 C
ATOM 4686 O ILE A 615 76.277 20.204 -7.002 1.00 68.71 O
ANISOU 4686 O ILE A 615 8385 5845 11877 -450 -4457 322 O
ATOM 4687 CB ILE A 615 75.583 18.687 -4.532 1.00 61.54 C
ANISOU 4687 CB ILE A 615 7571 4927 10885 -375 -4482 237 C
ATOM 4688 CG1 ILE A 615 75.054 18.410 -3.132 1.00 67.20 C
ANISOU 4688 CG1 ILE A 615 8355 5622 11556 -334 -4516 191 C
ATOM 4689 CG2 ILE A 615 76.645 17.664 -4.915 1.00 54.41 C
ANISOU 4689 CG2 ILE A 615 6585 4070 10019 -404 -4454 260 C
ATOM 4690 CD1 ILE A 615 74.685 16.998 -2.947 1.00 66.16 C
ANISOU 4690 CD1 ILE A 615 8232 5520 11386 -302 -4453 169 C
ATOM 4691 N ILE A 616 78.184 20.544 -5.855 1.00 78.09 N
ANISOU 4691 N ILE A 616 9498 7024 13148 -507 -4580 339 N
ATOM 4692 CA ILE A 616 79.010 20.758 -7.033 1.00 76.86 C
ANISOU 4692 CA ILE A 616 9260 6892 13051 -554 -4560 389 C
ATOM 4693 C ILE A 616 80.008 19.610 -7.099 1.00 72.47 C
ANISOU 4693 C ILE A 616 8628 6382 12525 -574 -4538 406 C
ATOM 4694 O ILE A 616 80.979 19.569 -6.336 1.00 75.43 O
ANISOU 4694 O ILE A 616 8962 6760 12936 -599 -4601 412 O
ATOM 4695 CB ILE A 616 79.716 22.118 -7.002 1.00 73.41 C
ANISOU 4695 CB ILE A 616 8795 6424 12673 -599 -4642 416 C
ATOM 4696 CG1 ILE A 616 78.743 23.221 -6.580 1.00 68.88 C
ANISOU 4696 CG1 ILE A 616 8306 5801 12065 -574 -4681 390 C
ATOM 4697 CG2 ILE A 616 80.313 22.432 -8.365 1.00 72.68 C
ANISOU 4697 CG2 ILE A 616 8628 6352 12634 -641 -4610 468 C
ATOM 4698 CD1 ILE A 616 77.627 23.473 -7.573 1.00 65.06 C
ANISOU 4698 CD1 ILE A 616 7861 5318 11542 -549 -4611 392 C
ATOM 4699 N CYS A 617 79.767 18.669 -8.013 1.00 68.56 N
ANISOU 4699 N CYS A 617 8113 5925 12013 -563 -4448 414 N
ATOM 4700 CA CYS A 617 80.741 17.635 -8.301 1.00 71.67 C
ANISOU 4700 CA CYS A 617 8426 6367 12440 -584 -4420 438 C
ATOM 4701 C CYS A 617 81.999 18.276 -8.888 1.00 80.43 C
ANISOU 4701 C CYS A 617 9443 7486 13631 -643 -4455 493 C
ATOM 4702 O CYS A 617 81.963 19.423 -9.340 1.00 92.25 O
ANISOU 4702 O CYS A 617 10941 8955 15153 -664 -4482 512 O
ATOM 4703 CB CYS A 617 80.148 16.607 -9.268 1.00 67.65 C
ANISOU 4703 CB CYS A 617 7917 5892 11894 -560 -4317 436 C
ATOM 4704 SG CYS A 617 78.834 15.614 -8.534 1.00 66.46 S
ANISOU 4704 SG CYS A 617 7858 5738 11655 -495 -4273 376 S
ATOM 4705 N PRO A 618 83.140 17.564 -8.859 1.00 73.82 N
ANISOU 4705 N PRO A 618 8523 6689 12838 -670 -4459 520 N
ATOM 4706 CA PRO A 618 84.388 18.103 -9.416 1.00 76.82 C
ANISOU 4706 CA PRO A 618 8806 7081 13299 -726 -4490 577 C
ATOM 4707 C PRO A 618 84.233 18.681 -10.823 1.00 88.12 C
ANISOU 4707 C PRO A 618 10215 8512 14752 -744 -4443 612 C
ATOM 4708 O PRO A 618 84.609 18.028 -11.797 1.00 92.90 O
ANISOU 4708 O PRO A 618 10761 9159 15377 -754 -4379 642 O
ATOM 4709 CB PRO A 618 85.310 16.885 -9.437 1.00 67.95 C
ANISOU 4709 CB PRO A 618 7604 6014 12199 -736 -4462 598 C
ATOM 4710 CG PRO A 618 84.833 16.049 -8.316 1.00 65.19 C
ANISOU 4710 CG PRO A 618 7310 5668 11793 -696 -4467 548 C
ATOM 4711 CD PRO A 618 83.346 16.237 -8.249 1.00 65.88 C
ANISOU 4711 CD PRO A 618 7505 5718 11808 -649 -4437 501 C
TER 4712 PRO A 618
ATOM 4713 N GLN C 21 36.980 23.143 36.936 1.00 51.81 N
ANISOU 4713 N GLN C 21 9057 5298 5332 687 -1826 -1427 N
ATOM 4714 CA GLN C 21 37.597 24.466 36.971 1.00 52.63 C
ANISOU 4714 CA GLN C 21 9082 5458 5459 652 -1801 -1475 C
ATOM 4715 C GLN C 21 36.617 25.524 36.493 1.00 48.34 C
ANISOU 4715 C GLN C 21 8466 4963 4937 586 -1645 -1485 C
ATOM 4716 O GLN C 21 36.217 26.401 37.252 1.00 51.41 O
ANISOU 4716 O GLN C 21 8878 5376 5279 526 -1589 -1505 O
ATOM 4717 CB GLN C 21 38.864 24.509 36.111 1.00 53.68 C
ANISOU 4717 CB GLN C 21 9121 5591 5685 705 -1862 -1516 C
ATOM 4718 CG GLN C 21 39.714 25.766 36.319 1.00 54.68 C
ANISOU 4718 CG GLN C 21 9183 5763 5832 679 -1870 -1566 C
ATOM 4719 CD GLN C 21 40.534 26.142 35.096 1.00 59.65 C
ANISOU 4719 CD GLN C 21 9688 6407 6570 706 -1848 -1611 C
ATOM 4720 OE1 GLN C 21 40.014 26.722 34.143 1.00 67.35 O
ANISOU 4720 OE1 GLN C 21 10585 7422 7583 667 -1719 -1614 O
ATOM 4721 NE2 GLN C 21 41.819 25.812 35.117 1.00 53.97 N
ANISOU 4721 NE2 GLN C 21 8956 5644 5907 770 -1979 -1649 N
ATOM 4722 N GLN C 22 36.238 25.444 35.219 1.00 45.52 N
ANISOU 4722 N GLN C 22 8029 4613 4654 591 -1580 -1476 N
ATOM 4723 CA GLN C 22 35.295 26.413 34.676 1.00 43.21 C
ANISOU 4723 CA GLN C 22 7672 4351 4396 530 -1459 -1481 C
ATOM 4724 C GLN C 22 33.852 26.018 34.981 1.00 39.02 C
ANISOU 4724 C GLN C 22 7211 3780 3833 506 -1408 -1444 C
ATOM 4725 O GLN C 22 32.993 26.890 35.160 1.00 36.71 O
ANISOU 4725 O GLN C 22 6908 3490 3550 453 -1324 -1459 O
ATOM 4726 CB GLN C 22 35.514 26.555 33.172 1.00 47.35 C
ANISOU 4726 CB GLN C 22 8096 4891 5004 531 -1425 -1484 C
ATOM 4727 CG GLN C 22 35.080 27.881 32.600 1.00 48.03 C
ANISOU 4727 CG GLN C 22 8100 5013 5138 471 -1334 -1504 C
ATOM 4728 CD GLN C 22 35.820 29.051 33.214 1.00 47.18 C
ANISOU 4728 CD GLN C 22 7953 4949 5025 450 -1324 -1555 C
ATOM 4729 OE1 GLN C 22 37.047 29.125 33.159 1.00 46.14 O
ANISOU 4729 OE1 GLN C 22 7789 4836 4906 479 -1376 -1584 O
ATOM 4730 NE2 GLN C 22 35.072 29.978 33.797 1.00 42.17 N
ANISOU 4730 NE2 GLN C 22 7323 4321 4377 399 -1256 -1573 N
ATOM 4731 N TRP C 23 33.575 24.717 35.040 1.00 36.26 N
ANISOU 4731 N TRP C 23 6937 3384 3455 545 -1458 -1400 N
ATOM 4732 CA TRP C 23 32.265 24.169 35.376 1.00 37.30 C
ANISOU 4732 CA TRP C 23 7151 3467 3556 529 -1421 -1363 C
ATOM 4733 C TRP C 23 32.429 22.668 35.569 1.00 41.84 C
ANISOU 4733 C TRP C 23 7812 3996 4090 584 -1504 -1321 C
ATOM 4734 O TRP C 23 33.376 22.065 35.054 1.00 42.75 O
ANISOU 4734 O TRP C 23 7902 4112 4230 633 -1574 -1323 O
ATOM 4735 CB TRP C 23 31.227 24.468 34.284 1.00 38.29 C
ANISOU 4735 CB TRP C 23 7217 3578 3753 497 -1353 -1346 C
ATOM 4736 CG TRP C 23 29.835 24.005 34.600 1.00 40.07 C
ANISOU 4736 CG TRP C 23 7523 3738 3964 479 -1317 -1314 C
ATOM 4737 CD1 TRP C 23 28.946 24.608 35.438 1.00 41.91 C
ANISOU 4737 CD1 TRP C 23 7805 3936 4182 436 -1245 -1336 C
ATOM 4738 CD2 TRP C 23 29.164 22.852 34.068 1.00 42.71 C
ANISOU 4738 CD2 TRP C 23 7902 4021 4303 498 -1344 -1260 C
ATOM 4739 NE1 TRP C 23 27.769 23.901 35.471 1.00 42.81 N
ANISOU 4739 NE1 TRP C 23 7991 3976 4299 432 -1226 -1300 N
ATOM 4740 CE2 TRP C 23 27.877 22.818 34.637 1.00 41.41 C
ANISOU 4740 CE2 TRP C 23 7811 3792 4130 469 -1293 -1249 C
ATOM 4741 CE3 TRP C 23 29.529 21.844 33.169 1.00 37.73 C
ANISOU 4741 CE3 TRP C 23 7262 3387 3685 532 -1399 -1226 C
ATOM 4742 CZ2 TRP C 23 26.952 21.817 34.338 1.00 40.05 C
ANISOU 4742 CZ2 TRP C 23 7700 3555 3962 476 -1307 -1198 C
ATOM 4743 CZ3 TRP C 23 28.608 20.849 32.872 1.00 41.44 C
ANISOU 4743 CZ3 TRP C 23 7796 3799 4152 535 -1410 -1177 C
ATOM 4744 CH2 TRP C 23 27.336 20.845 33.454 1.00 43.07 C
ANISOU 4744 CH2 TRP C 23 8071 3945 4350 509 -1371 -1160 C
ATOM 4745 N PHE C 24 31.514 22.074 36.333 1.00 38.35 N
ANISOU 4745 N PHE C 24 7479 3505 3587 574 -1492 -1291 N
ATOM 4746 CA PHE C 24 31.476 20.622 36.460 1.00 43.28 C
ANISOU 4746 CA PHE C 24 8192 4078 4176 623 -1562 -1246 C
ATOM 4747 C PHE C 24 30.112 20.195 36.984 1.00 43.21 C
ANISOU 4747 C PHE C 24 8281 4014 4124 595 -1508 -1214 C
ATOM 4748 O PHE C 24 29.354 21.006 37.519 1.00 37.72 O
ANISOU 4748 O PHE C 24 7606 3311 3415 541 -1423 -1236 O
ATOM 4749 CB PHE C 24 32.604 20.086 37.359 1.00 43.90 C
ANISOU 4749 CB PHE C 24 8345 4143 4193 664 -1679 -1250 C
ATOM 4750 CG PHE C 24 32.672 20.717 38.723 1.00 53.18 C
ANISOU 4750 CG PHE C 24 9605 5323 5279 617 -1680 -1268 C
ATOM 4751 CD1 PHE C 24 33.411 21.873 38.932 1.00 60.89 C
ANISOU 4751 CD1 PHE C 24 10521 6352 6263 589 -1676 -1316 C
ATOM 4752 CD2 PHE C 24 32.030 20.134 39.806 1.00 57.90 C
ANISOU 4752 CD2 PHE C 24 10353 5870 5778 594 -1681 -1239 C
ATOM 4753 CE1 PHE C 24 33.488 22.448 40.186 1.00 64.47 C
ANISOU 4753 CE1 PHE C 24 11064 6809 6623 531 -1675 -1335 C
ATOM 4754 CE2 PHE C 24 32.104 20.705 41.063 1.00 64.47 C
ANISOU 4754 CE2 PHE C 24 11282 6701 6512 532 -1673 -1258 C
ATOM 4755 CZ PHE C 24 32.832 21.863 41.252 1.00 65.11 C
ANISOU 4755 CZ PHE C 24 11303 6837 6598 499 -1671 -1307 C
ATOM 4756 N CYS C 25 29.809 18.906 36.815 1.00 42.76 N
ANISOU 4756 N CYS C 25 8288 3908 4052 632 -1551 -1168 N
ATOM 4757 CA CYS C 25 28.542 18.343 37.264 1.00 45.95 C
ANISOU 4757 CA CYS C 25 8791 4249 4418 612 -1505 -1134 C
ATOM 4758 C CYS C 25 28.735 16.864 37.576 1.00 46.59 C
ANISOU 4758 C CYS C 25 8975 4281 4445 663 -1588 -1091 C
ATOM 4759 O CYS C 25 29.719 16.245 37.161 1.00 38.43 O
ANISOU 4759 O CYS C 25 7917 3254 3430 717 -1675 -1088 O
ATOM 4760 CB CYS C 25 27.429 18.540 36.225 1.00 52.96 C
ANISOU 4760 CB CYS C 25 9617 5117 5387 583 -1440 -1120 C
ATOM 4761 SG CYS C 25 27.620 17.645 34.653 1.00 63.42 S
ANISOU 4761 SG CYS C 25 10877 6443 6776 616 -1492 -1083 S
ATOM 4762 N ASN C 26 27.787 16.303 38.327 1.00 51.92 N
ANISOU 4762 N ASN C 26 9772 4896 5059 645 -1557 -1062 N
ATOM 4763 CA ASN C 26 27.828 14.904 38.743 1.00 48.01 C
ANISOU 4763 CA ASN C 26 9393 4343 4503 687 -1630 -1018 C
ATOM 4764 C ASN C 26 26.664 14.160 38.109 1.00 45.19 C
ANISOU 4764 C ASN C 26 9051 3939 4180 686 -1587 -979 C
ATOM 4765 O ASN C 26 25.506 14.556 38.276 1.00 50.10 O
ANISOU 4765 O ASN C 26 9696 4529 4810 637 -1493 -980 O
ATOM 4766 CB ASN C 26 27.769 14.770 40.270 1.00 52.55 C
ANISOU 4766 CB ASN C 26 10130 4880 4958 658 -1638 -1012 C
ATOM 4767 CG ASN C 26 29.141 14.800 40.915 1.00 61.54 C
ANISOU 4767 CG ASN C 26 11300 6035 6046 678 -1757 -1023 C
ATOM 4768 OD1 ASN C 26 30.150 14.561 40.253 1.00 60.96 O
ANISOU 4768 OD1 ASN C 26 11147 5983 6033 736 -1849 -1030 O
ATOM 4769 ND2 ASN C 26 29.185 15.089 42.212 1.00 70.14 N
ANISOU 4769 ND2 ASN C 26 12519 7107 7026 623 -1758 -1026 N
ATOM 4770 N SER C 27 26.972 13.089 37.389 1.00 40.13 N
ANISOU 4770 N SER C 27 8400 3283 3565 736 -1653 -950 N
ATOM 4771 CA SER C 27 25.980 12.148 36.896 1.00 43.80 C
ANISOU 4771 CA SER C 27 8903 3695 4044 737 -1634 -908 C
ATOM 4772 C SER C 27 26.031 10.873 37.729 1.00 41.23 C
ANISOU 4772 C SER C 27 8721 3308 3638 775 -1694 -872 C
ATOM 4773 O SER C 27 26.911 10.689 38.574 1.00 42.60 O
ANISOU 4773 O SER C 27 8961 3475 3751 803 -1767 -878 O
ATOM 4774 CB SER C 27 26.212 11.826 35.418 1.00 47.16 C
ANISOU 4774 CB SER C 27 9229 4142 4549 749 -1653 -902 C
ATOM 4775 OG SER C 27 25.219 10.937 34.940 1.00 57.04 O
ANISOU 4775 OG SER C 27 10523 5340 5808 738 -1640 -859 O
ATOM 4776 N SER C 28 25.069 9.980 37.482 1.00 39.22 N
ANISOU 4776 N SER C 28 8519 2999 3382 773 -1672 -832 N
ATOM 4777 CA SER C 28 25.081 8.699 38.179 1.00 44.47 C
ANISOU 4777 CA SER C 28 9322 3601 3973 811 -1729 -796 C
ATOM 4778 C SER C 28 26.230 7.813 37.717 1.00 47.54 C
ANISOU 4778 C SER C 28 9695 3987 4381 879 -1836 -795 C
ATOM 4779 O SER C 28 26.636 6.910 38.456 1.00 50.67 O
ANISOU 4779 O SER C 28 10206 4329 4716 920 -1918 -775 O
ATOM 4780 CB SER C 28 23.747 7.976 37.992 1.00 47.67 C
ANISOU 4780 CB SER C 28 9783 3948 4380 789 -1674 -756 C
ATOM 4781 OG SER C 28 23.525 7.651 36.634 1.00 45.04 O
ANISOU 4781 OG SER C 28 9357 3627 4128 788 -1676 -746 O
ATOM 4782 N ASP C 29 26.776 8.064 36.523 1.00 48.76 N
ANISOU 4782 N ASP C 29 9720 4188 4618 888 -1837 -822 N
ATOM 4783 CA ASP C 29 27.903 7.293 36.015 1.00 47.78 C
ANISOU 4783 CA ASP C 29 9576 4051 4526 948 -1918 -840 C
ATOM 4784 C ASP C 29 29.000 8.163 35.411 1.00 41.65 C
ANISOU 4784 C ASP C 29 8678 3334 3814 954 -1928 -896 C
ATOM 4785 O ASP C 29 29.897 7.628 34.751 1.00 40.08 O
ANISOU 4785 O ASP C 29 8444 3122 3665 993 -1969 -926 O
ATOM 4786 CB ASP C 29 27.428 6.262 34.978 1.00 48.92 C
ANISOU 4786 CB ASP C 29 9715 4168 4706 946 -1893 -820 C
ATOM 4787 CG ASP C 29 26.751 6.898 33.768 1.00 55.05 C
ANISOU 4787 CG ASP C 29 10388 4986 5540 878 -1805 -821 C
ATOM 4788 OD1 ASP C 29 26.794 8.137 33.611 1.00 57.48 O
ANISOU 4788 OD1 ASP C 29 10615 5349 5876 843 -1768 -845 O
ATOM 4789 OD2 ASP C 29 26.167 6.143 32.963 1.00 58.11 O
ANISOU 4789 OD2 ASP C 29 10787 5347 5943 854 -1782 -798 O
ATOM 4790 N ALA C 30 28.962 9.478 35.609 1.00 41.05 N
ANISOU 4790 N ALA C 30 8539 3315 3744 914 -1883 -917 N
ATOM 4791 CA ALA C 30 29.930 10.344 34.953 1.00 38.85 C
ANISOU 4791 CA ALA C 30 8139 3093 3528 913 -1881 -969 C
ATOM 4792 C ALA C 30 30.183 11.588 35.788 1.00 41.59 C
ANISOU 4792 C ALA C 30 8468 3484 3850 890 -1877 -992 C
ATOM 4793 O ALA C 30 29.267 12.132 36.409 1.00 38.89 O
ANISOU 4793 O ALA C 30 8162 3148 3465 843 -1817 -975 O
ATOM 4794 CB ALA C 30 29.455 10.745 33.550 1.00 37.92 C
ANISOU 4794 CB ALA C 30 7918 3014 3477 861 -1791 -975 C
ATOM 4795 N ILE C 31 31.440 12.022 35.802 1.00 39.30 N
ANISOU 4795 N ILE C 31 8125 3217 3588 920 -1938 -1037 N
ATOM 4796 CA ILE C 31 31.845 13.300 36.373 1.00 41.08 C
ANISOU 4796 CA ILE C 31 8311 3494 3802 892 -1931 -1068 C
ATOM 4797 C ILE C 31 32.467 14.110 35.245 1.00 49.20 C
ANISOU 4797 C ILE C 31 9194 4581 4919 882 -1888 -1115 C
ATOM 4798 O ILE C 31 33.481 13.700 34.666 1.00 48.54 O
ANISOU 4798 O ILE C 31 9073 4482 4890 927 -1942 -1149 O
ATOM 4799 CB ILE C 31 32.829 13.128 37.541 1.00 45.15 C
ANISOU 4799 CB ILE C 31 8914 3975 4265 928 -2065 -1075 C
ATOM 4800 CG1 ILE C 31 32.231 12.229 38.625 1.00 44.00 C
ANISOU 4800 CG1 ILE C 31 8933 3762 4022 927 -2110 -1023 C
ATOM 4801 CG2 ILE C 31 33.199 14.477 38.126 1.00 44.82 C
ANISOU 4801 CG2 ILE C 31 8835 3990 4203 883 -2050 -1107 C
ATOM 4802 CD1 ILE C 31 33.080 12.156 39.882 1.00 51.68 C
ANISOU 4802 CD1 ILE C 31 10016 4696 4926 934 -2251 -1018 C
ATOM 4803 N ILE C 32 31.857 15.249 34.929 1.00 45.10 N
ANISOU 4803 N ILE C 32 8600 4118 4418 820 -1790 -1123 N
ATOM 4804 CA ILE C 32 32.180 16.025 33.739 1.00 41.09 C
ANISOU 4804 CA ILE C 32 7964 3661 3986 793 -1732 -1157 C
ATOM 4805 C ILE C 32 32.612 17.418 34.166 1.00 44.87 C
ANISOU 4805 C ILE C 32 8381 4197 4469 766 -1713 -1195 C
ATOM 4806 O ILE C 32 31.922 18.068 34.958 1.00 44.87 O
ANISOU 4806 O ILE C 32 8412 4209 4427 728 -1674 -1187 O
ATOM 4807 CB ILE C 32 30.977 16.093 32.781 1.00 36.44 C
ANISOU 4807 CB ILE C 32 7347 3074 3425 737 -1647 -1126 C
ATOM 4808 CG1 ILE C 32 30.593 14.685 32.322 1.00 39.91 C
ANISOU 4808 CG1 ILE C 32 7851 3458 3857 757 -1667 -1090 C
ATOM 4809 CG2 ILE C 32 31.276 16.992 31.594 1.00 35.82 C
ANISOU 4809 CG2 ILE C 32 7154 3044 3412 695 -1593 -1157 C
ATOM 4810 CD1 ILE C 32 29.283 14.622 31.599 1.00 40.15 C
ANISOU 4810 CD1 ILE C 32 7886 3470 3899 700 -1612 -1048 C
ATOM 4811 N SER C 33 33.744 17.875 33.637 1.00 41.35 N
ANISOU 4811 N SER C 33 7853 3782 4076 782 -1732 -1243 N
ATOM 4812 CA SER C 33 34.254 19.207 33.928 1.00 39.00 C
ANISOU 4812 CA SER C 33 7488 3540 3789 756 -1714 -1283 C
ATOM 4813 C SER C 33 35.035 19.695 32.719 1.00 36.78 C
ANISOU 4813 C SER C 33 7095 3291 3589 750 -1681 -1327 C
ATOM 4814 O SER C 33 35.507 18.898 31.905 1.00 40.71 O
ANISOU 4814 O SER C 33 7584 3758 4126 777 -1694 -1340 O
ATOM 4815 CB SER C 33 35.143 19.213 35.179 1.00 42.10 C
ANISOU 4815 CB SER C 33 7943 3917 4134 791 -1822 -1300 C
ATOM 4816 OG SER C 33 36.346 18.496 34.963 1.00 42.54 O
ANISOU 4816 OG SER C 33 8000 3932 4233 860 -1931 -1328 O
ATOM 4817 N TYR C 34 35.163 21.016 32.602 1.00 38.19 N
ANISOU 4817 N TYR C 34 7195 3527 3790 707 -1628 -1356 N
ATOM 4818 CA TYR C 34 35.975 21.587 31.541 1.00 36.04 C
ANISOU 4818 CA TYR C 34 6823 3284 3586 695 -1593 -1402 C
ATOM 4819 C TYR C 34 36.656 22.859 32.020 1.00 36.14 C
ANISOU 4819 C TYR C 34 6777 3345 3609 682 -1595 -1444 C
ATOM 4820 O TYR C 34 36.196 23.526 32.950 1.00 38.43 O
ANISOU 4820 O TYR C 34 7090 3657 3853 657 -1586 -1436 O
ATOM 4821 CB TYR C 34 35.159 21.887 30.274 1.00 35.20 C
ANISOU 4821 CB TYR C 34 6669 3193 3511 630 -1496 -1384 C
ATOM 4822 CG TYR C 34 34.249 23.096 30.345 1.00 36.48 C
ANISOU 4822 CG TYR C 34 6794 3393 3674 570 -1435 -1371 C
ATOM 4823 CD1 TYR C 34 34.690 24.352 29.944 1.00 37.76 C
ANISOU 4823 CD1 TYR C 34 6870 3603 3875 534 -1391 -1408 C
ATOM 4824 CD2 TYR C 34 32.939 22.973 30.780 1.00 34.45 C
ANISOU 4824 CD2 TYR C 34 6591 3111 3388 549 -1420 -1326 C
ATOM 4825 CE1 TYR C 34 33.854 25.455 29.997 1.00 39.68 C
ANISOU 4825 CE1 TYR C 34 7081 3867 4129 482 -1339 -1402 C
ATOM 4826 CE2 TYR C 34 32.097 24.067 30.833 1.00 38.70 C
ANISOU 4826 CE2 TYR C 34 7098 3661 3943 498 -1367 -1325 C
ATOM 4827 CZ TYR C 34 32.556 25.306 30.442 1.00 39.46 C
ANISOU 4827 CZ TYR C 34 7109 3804 4081 466 -1329 -1364 C
ATOM 4828 OH TYR C 34 31.713 26.393 30.498 1.00 39.59 O
ANISOU 4828 OH TYR C 34 7098 3819 4124 418 -1280 -1368 O
ATOM 4829 N SER C 35 37.767 23.172 31.372 1.00 36.26 N
ANISOU 4829 N SER C 35 6723 3369 3683 696 -1599 -1496 N
ATOM 4830 CA SER C 35 38.475 24.434 31.486 1.00 36.24 C
ANISOU 4830 CA SER C 35 6648 3414 3708 677 -1587 -1541 C
ATOM 4831 C SER C 35 38.662 24.994 30.083 1.00 36.08 C
ANISOU 4831 C SER C 35 6541 3418 3749 632 -1492 -1568 C
ATOM 4832 O SER C 35 38.285 24.368 29.091 1.00 35.34 O
ANISOU 4832 O SER C 35 6455 3302 3670 610 -1444 -1554 O
ATOM 4833 CB SER C 35 39.823 24.246 32.186 1.00 37.28 C
ANISOU 4833 CB SER C 35 6792 3516 3857 744 -1712 -1586 C
ATOM 4834 OG SER C 35 40.668 23.391 31.434 1.00 38.37 O
ANISOU 4834 OG SER C 35 6916 3597 4065 795 -1747 -1623 O
ATOM 4835 N TYR C 36 39.245 26.181 29.998 1.00 35.50 N
ANISOU 4835 N TYR C 36 6395 3388 3705 608 -1464 -1608 N
ATOM 4836 CA TYR C 36 39.667 26.684 28.703 1.00 37.14 C
ANISOU 4836 CA TYR C 36 6533 3609 3970 566 -1383 -1642 C
ATOM 4837 C TYR C 36 40.972 26.012 28.301 1.00 36.20 C
ANISOU 4837 C TYR C 36 6405 3438 3910 617 -1419 -1702 C
ATOM 4838 O TYR C 36 41.762 25.591 29.149 1.00 36.73 O
ANISOU 4838 O TYR C 36 6494 3471 3992 691 -1530 -1728 O
ATOM 4839 CB TYR C 36 39.839 28.204 28.733 1.00 36.56 C
ANISOU 4839 CB TYR C 36 6388 3592 3911 521 -1336 -1665 C
ATOM 4840 CG TYR C 36 38.551 28.964 28.942 1.00 35.99 C
ANISOU 4840 CG TYR C 36 6314 3553 3807 465 -1284 -1622 C
ATOM 4841 CD1 TYR C 36 37.400 28.626 28.239 1.00 33.66 C
ANISOU 4841 CD1 TYR C 36 6042 3242 3505 426 -1243 -1576 C
ATOM 4842 CD2 TYR C 36 38.483 30.012 29.846 1.00 40.06 C
ANISOU 4842 CD2 TYR C 36 6811 4104 4306 450 -1280 -1635 C
ATOM 4843 CE1 TYR C 36 36.220 29.316 28.432 1.00 33.47 C
ANISOU 4843 CE1 TYR C 36 6017 3226 3474 384 -1210 -1546 C
ATOM 4844 CE2 TYR C 36 37.308 30.706 30.045 1.00 37.38 C
ANISOU 4844 CE2 TYR C 36 6473 3777 3955 400 -1226 -1611 C
ATOM 4845 CZ TYR C 36 36.180 30.356 29.337 1.00 34.61 C
ANISOU 4845 CZ TYR C 36 6139 3399 3612 373 -1196 -1568 C
ATOM 4846 OH TYR C 36 35.012 31.052 29.542 1.00 32.92 O
ANISOU 4846 OH TYR C 36 5928 3176 3406 332 -1156 -1553 O
ATOM 4847 N CYS C 37 41.185 25.895 26.996 1.00 35.77 N
ANISOU 4847 N CYS C 37 6328 3368 3896 572 -1329 -1731 N
ATOM 4848 CA CYS C 37 42.445 25.349 26.516 1.00 36.62 C
ANISOU 4848 CA CYS C 37 6422 3411 4082 610 -1330 -1806 C
ATOM 4849 C CYS C 37 43.595 26.276 26.895 1.00 48.41 C
ANISOU 4849 C CYS C 37 7848 4914 5634 643 -1370 -1866 C
ATOM 4850 O CYS C 37 43.417 27.484 27.081 1.00 46.39 O
ANISOU 4850 O CYS C 37 7548 4723 5354 604 -1347 -1854 O
ATOM 4851 CB CYS C 37 42.396 25.145 25.004 1.00 40.62 C
ANISOU 4851 CB CYS C 37 6930 3895 4610 530 -1192 -1833 C
ATOM 4852 SG CYS C 37 41.167 23.930 24.488 1.00 56.98 S
ANISOU 4852 SG CYS C 37 9085 5942 6622 493 -1163 -1772 S
ATOM 4853 N ASP C 38 44.786 25.692 27.031 1.00 54.84 N
ANISOU 4853 N ASP C 38 8649 5648 6538 717 -1438 -1934 N
ATOM 4854 CA ASP C 38 45.962 26.465 27.407 1.00 60.87 C
ANISOU 4854 CA ASP C 38 9343 6403 7381 760 -1502 -1998 C
ATOM 4855 C ASP C 38 46.364 27.467 26.335 1.00 58.01 C
ANISOU 4855 C ASP C 38 8919 6065 7058 688 -1360 -2041 C
ATOM 4856 O ASP C 38 47.068 28.433 26.643 1.00 55.72 O
ANISOU 4856 O ASP C 38 8566 5796 6807 702 -1395 -2076 O
ATOM 4857 CB ASP C 38 47.144 25.537 27.695 1.00 67.23 C
ANISOU 4857 CB ASP C 38 10136 7091 8318 861 -1617 -2070 C
ATOM 4858 CG ASP C 38 46.831 24.498 28.752 1.00 76.45 C
ANISOU 4858 CG ASP C 38 11378 8218 9451 933 -1778 -2029 C
ATOM 4859 OD1 ASP C 38 45.912 24.720 29.568 1.00 80.49 O
ANISOU 4859 OD1 ASP C 38 11947 8800 9836 914 -1823 -1953 O
ATOM 4860 OD2 ASP C 38 47.514 23.453 28.763 1.00 78.38 O
ANISOU 4860 OD2 ASP C 38 11625 8348 9810 1005 -1850 -2074 O
ATOM 4861 N HIS C 39 45.935 27.265 25.090 1.00 56.64 N
ANISOU 4861 N HIS C 39 8770 5884 6868 604 -1205 -2038 N
ATOM 4862 CA HIS C 39 46.342 28.129 23.993 1.00 55.49 C
ANISOU 4862 CA HIS C 39 8587 5745 6752 523 -1064 -2081 C
ATOM 4863 C HIS C 39 45.253 29.091 23.535 1.00 53.20 C
ANISOU 4863 C HIS C 39 8299 5547 6369 421 -990 -2019 C
ATOM 4864 O HIS C 39 45.532 29.957 22.700 1.00 57.77 O
ANISOU 4864 O HIS C 39 8852 6138 6961 349 -889 -2048 O
ATOM 4865 CB HIS C 39 46.800 27.281 22.800 1.00 54.56 C
ANISOU 4865 CB HIS C 39 8505 5531 6695 481 -927 -2142 C
ATOM 4866 CG HIS C 39 45.705 26.472 22.177 1.00 59.01 C
ANISOU 4866 CG HIS C 39 9142 6099 7181 414 -863 -2097 C
ATOM 4867 ND1 HIS C 39 45.116 25.401 22.814 1.00 57.62 N
ANISOU 4867 ND1 HIS C 39 9011 5907 6973 471 -954 -2051 N
ATOM 4868 CD2 HIS C 39 45.092 26.579 20.974 1.00 58.97 C
ANISOU 4868 CD2 HIS C 39 9168 6109 7128 294 -733 -2095 C
ATOM 4869 CE1 HIS C 39 44.188 24.883 22.029 1.00 58.39 C
ANISOU 4869 CE1 HIS C 39 9164 6012 7009 392 -878 -2019 C
ATOM 4870 NE2 HIS C 39 44.154 25.579 20.907 1.00 56.32 N
ANISOU 4870 NE2 HIS C 39 8891 5770 6739 286 -754 -2047 N
ATOM 4871 N LEU C 40 44.032 28.971 24.054 1.00 46.62 N
ANISOU 4871 N LEU C 40 7494 4764 5455 415 -1039 -1939 N
ATOM 4872 CA LEU C 40 42.935 29.836 23.632 1.00 40.57 C
ANISOU 4872 CA LEU C 40 6720 4064 4631 330 -985 -1884 C
ATOM 4873 C LEU C 40 41.951 29.965 24.783 1.00 43.06 C
ANISOU 4873 C LEU C 40 7045 4422 4893 363 -1068 -1814 C
ATOM 4874 O LEU C 40 41.441 28.956 25.280 1.00 45.19 O
ANISOU 4874 O LEU C 40 7368 4669 5134 404 -1124 -1779 O
ATOM 4875 CB LEU C 40 42.242 29.279 22.383 1.00 36.96 C
ANISOU 4875 CB LEU C 40 6308 3586 4149 248 -902 -1872 C
ATOM 4876 CG LEU C 40 41.290 30.216 21.640 1.00 34.80 C
ANISOU 4876 CG LEU C 40 6022 3360 3842 157 -858 -1833 C
ATOM 4877 CD1 LEU C 40 42.008 31.493 21.228 1.00 35.66 C
ANISOU 4877 CD1 LEU C 40 6083 3487 3979 124 -809 -1880 C
ATOM 4878 CD2 LEU C 40 40.700 29.511 20.426 1.00 34.58 C
ANISOU 4878 CD2 LEU C 40 6055 3297 3787 91 -817 -1828 C
ATOM 4879 N LYS C 41 41.685 31.204 25.203 1.00 41.96 N
ANISOU 4879 N LYS C 41 6862 4336 4744 341 -1065 -1800 N
ATOM 4880 CA LYS C 41 40.868 31.467 26.381 1.00 38.18 C
ANISOU 4880 CA LYS C 41 6395 3887 4224 362 -1119 -1754 C
ATOM 4881 C LYS C 41 39.656 32.339 26.069 1.00 36.60 C
ANISOU 4881 C LYS C 41 6181 3716 4009 294 -1066 -1713 C
ATOM 4882 O LYS C 41 39.152 33.031 26.959 1.00 33.65 O
ANISOU 4882 O LYS C 41 5799 3365 3620 294 -1077 -1700 O
ATOM 4883 CB LYS C 41 41.713 32.118 27.477 1.00 40.50 C
ANISOU 4883 CB LYS C 41 6660 4202 4526 407 -1177 -1789 C
ATOM 4884 CG LYS C 41 43.017 31.397 27.778 1.00 43.28 C
ANISOU 4884 CG LYS C 41 7017 4511 4918 484 -1260 -1840 C
ATOM 4885 CD LYS C 41 42.989 30.734 29.149 1.00 47.92 C
ANISOU 4885 CD LYS C 41 7661 5082 5466 551 -1382 -1823 C
ATOM 4886 CE LYS C 41 44.323 30.073 29.460 1.00 57.37 C
ANISOU 4886 CE LYS C 41 8856 6219 6722 636 -1500 -1880 C
ATOM 4887 NZ LYS C 41 44.309 29.375 30.769 1.00 64.81 N
ANISOU 4887 NZ LYS C 41 9870 7134 7620 695 -1641 -1860 N
ATOM 4888 N PHE C 42 39.180 32.331 24.828 1.00 39.98 N
ANISOU 4888 N PHE C 42 6613 4133 4446 234 -1016 -1699 N
ATOM 4889 CA PHE C 42 37.990 33.100 24.491 1.00 32.25 C
ANISOU 4889 CA PHE C 42 5632 3157 3465 184 -1004 -1660 C
ATOM 4890 C PHE C 42 36.802 32.579 25.294 1.00 32.80 C
ANISOU 4890 C PHE C 42 5742 3209 3510 204 -1042 -1608 C
ATOM 4891 O PHE C 42 36.511 31.375 25.252 1.00 32.95 O
ANISOU 4891 O PHE C 42 5818 3197 3506 228 -1074 -1581 O
ATOM 4892 CB PHE C 42 37.703 33.023 22.992 1.00 32.55 C
ANISOU 4892 CB PHE C 42 5691 3170 3505 120 -977 -1651 C
ATOM 4893 CG PHE C 42 38.690 33.782 22.147 1.00 45.21 C
ANISOU 4893 CG PHE C 42 7262 4784 5130 84 -927 -1706 C
ATOM 4894 CD1 PHE C 42 39.506 34.750 22.712 1.00 46.00 C
ANISOU 4894 CD1 PHE C 42 7308 4915 5255 105 -913 -1746 C
ATOM 4895 CD2 PHE C 42 38.801 33.530 20.788 1.00 52.15 C
ANISOU 4895 CD2 PHE C 42 8173 5638 6002 22 -891 -1722 C
ATOM 4896 CE1 PHE C 42 40.416 35.448 21.939 1.00 47.54 C
ANISOU 4896 CE1 PHE C 42 7476 5113 5472 70 -861 -1797 C
ATOM 4897 CE2 PHE C 42 39.705 34.227 20.009 1.00 49.83 C
ANISOU 4897 CE2 PHE C 42 7857 5349 5728 -19 -832 -1782 C
ATOM 4898 CZ PHE C 42 40.516 35.186 20.586 1.00 50.53 C
ANISOU 4898 CZ PHE C 42 7887 5465 5845 7 -815 -1818 C
ATOM 4899 N PRO C 43 36.101 33.435 26.030 1.00 31.90 N
ANISOU 4899 N PRO C 43 5614 3102 3405 197 -1040 -1600 N
ATOM 4900 CA PRO C 43 35.157 32.945 27.038 1.00 32.01 C
ANISOU 4900 CA PRO C 43 5680 3089 3395 225 -1070 -1571 C
ATOM 4901 C PRO C 43 33.850 32.436 26.452 1.00 35.32 C
ANISOU 4901 C PRO C 43 6147 3452 3822 202 -1093 -1515 C
ATOM 4902 O PRO C 43 33.397 32.867 25.389 1.00 31.65 O
ANISOU 4902 O PRO C 43 5671 2966 3388 152 -1093 -1496 O
ATOM 4903 CB PRO C 43 34.917 34.177 27.919 1.00 33.42 C
ANISOU 4903 CB PRO C 43 5829 3282 3589 209 -1037 -1601 C
ATOM 4904 CG PRO C 43 35.142 35.326 27.013 1.00 31.72 C
ANISOU 4904 CG PRO C 43 5549 3082 3419 161 -999 -1619 C
ATOM 4905 CD PRO C 43 36.222 34.904 26.053 1.00 32.80 C
ANISOU 4905 CD PRO C 43 5669 3243 3552 161 -999 -1629 C
ATOM 4906 N ILE C 44 33.242 31.505 27.185 1.00 38.38 N
ANISOU 4906 N ILE C 44 6598 3807 4179 237 -1125 -1488 N
ATOM 4907 CA ILE C 44 31.965 30.908 26.811 1.00 32.01 C
ANISOU 4907 CA ILE C 44 5850 2935 3379 220 -1157 -1432 C
ATOM 4908 C ILE C 44 31.435 30.137 28.011 1.00 36.53 C
ANISOU 4908 C ILE C 44 6487 3478 3915 262 -1173 -1419 C
ATOM 4909 O ILE C 44 32.189 29.461 28.717 1.00 38.71 O
ANISOU 4909 O ILE C 44 6784 3782 4143 309 -1185 -1433 O
ATOM 4910 CB ILE C 44 32.108 29.996 25.570 1.00 35.24 C
ANISOU 4910 CB ILE C 44 6288 3328 3773 203 -1183 -1399 C
ATOM 4911 CG1 ILE C 44 30.812 29.218 25.329 1.00 34.92 C
ANISOU 4911 CG1 ILE C 44 6324 3214 3730 188 -1233 -1334 C
ATOM 4912 CG2 ILE C 44 33.291 29.056 25.730 1.00 32.22 C
ANISOU 4912 CG2 ILE C 44 5911 2977 3353 249 -1179 -1426 C
ATOM 4913 CD1 ILE C 44 30.800 28.457 24.043 1.00 34.51 C
ANISOU 4913 CD1 ILE C 44 6314 3139 3660 149 -1257 -1299 C
ATOM 4914 N SER C 45 30.130 30.255 28.245 1.00 36.44 N
ANISOU 4914 N SER C 45 7207 2124 4515 -906 -363 -509 N
ATOM 4915 CA SER C 45 29.449 29.528 29.309 1.00 34.41 C
ANISOU 4915 CA SER C 45 6784 1994 4297 -583 -282 -700 C
ATOM 4916 C SER C 45 28.685 28.372 28.676 1.00 32.16 C
ANISOU 4916 C SER C 45 6449 1832 3938 -470 -312 -552 C
ATOM 4917 O SER C 45 27.725 28.592 27.931 1.00 34.12 O
ANISOU 4917 O SER C 45 6728 1922 4315 -360 -428 -350 O
ATOM 4918 CB SER C 45 28.504 30.445 30.083 1.00 36.63 C
ANISOU 4918 CB SER C 45 7036 2010 4872 -316 -303 -803 C
ATOM 4919 OG SER C 45 29.223 31.418 30.816 1.00 51.18 O
ANISOU 4919 OG SER C 45 8881 3754 6809 -411 -261 -1016 O
ATOM 4920 N ILE C 46 29.118 27.146 28.960 1.00 29.58 N
ANISOU 4920 N ILE C 46 5954 1864 3422 -467 -212 -645 N
ATOM 4921 CA ILE C 46 28.424 25.944 28.517 1.00 32.00 C
ANISOU 4921 CA ILE C 46 6096 2360 3701 -347 -204 -540 C
ATOM 4922 C ILE C 46 28.051 25.126 29.742 1.00 33.24 C
ANISOU 4922 C ILE C 46 6137 2643 3849 -132 -67 -686 C
ATOM 4923 O ILE C 46 28.823 25.039 30.703 1.00 29.85 O
ANISOU 4923 O ILE C 46 5716 2329 3297 -131 12 -857 O
ATOM 4924 CB ILE C 46 29.272 25.098 27.542 1.00 34.46 C
ANISOU 4924 CB ILE C 46 6321 2961 3812 -560 -235 -491 C
ATOM 4925 CG1 ILE C 46 29.659 25.918 26.315 1.00 51.95 C
ANISOU 4925 CG1 ILE C 46 8649 5121 5970 -826 -351 -318 C
ATOM 4926 CG2 ILE C 46 28.512 23.842 27.110 1.00 36.22 C
ANISOU 4926 CG2 ILE C 46 6361 3340 4060 -434 -228 -433 C
ATOM 4927 CD1 ILE C 46 30.122 25.093 25.138 1.00 63.12 C
ANISOU 4927 CD1 ILE C 46 9917 6873 7191 -1007 -397 -265 C
ATOM 4928 N SER C 47 26.858 24.538 29.705 1.00 28.96 N
ANISOU 4928 N SER C 47 5482 2107 3416 36 -37 -618 N
ATOM 4929 CA SER C 47 26.431 23.570 30.700 1.00 30.57 C
ANISOU 4929 CA SER C 47 5578 2453 3583 175 112 -687 C
ATOM 4930 C SER C 47 25.383 22.673 30.059 1.00 37.24 C
ANISOU 4930 C SER C 47 6277 3345 4528 220 126 -581 C
ATOM 4931 O SER C 47 24.875 22.955 28.971 1.00 34.02 O
ANISOU 4931 O SER C 47 5830 2879 4217 201 12 -491 O
ATOM 4932 CB SER C 47 25.874 24.252 31.957 1.00 30.26 C
ANISOU 4932 CB SER C 47 5543 2355 3601 341 202 -840 C
ATOM 4933 OG SER C 47 24.695 24.980 31.664 1.00 40.06 O
ANISOU 4933 OG SER C 47 6742 3426 5055 470 142 -844 O
ATOM 4934 N SER C 48 25.073 21.575 30.737 1.00 34.37 N
ANISOU 4934 N SER C 48 5833 3097 4130 266 266 -590 N
ATOM 4935 CA SER C 48 24.014 20.679 30.306 1.00 37.48 C
ANISOU 4935 CA SER C 48 6069 3528 4642 277 322 -537 C
ATOM 4936 C SER C 48 23.020 20.492 31.442 1.00 40.86 C
ANISOU 4936 C SER C 48 6425 4001 5099 373 504 -592 C
ATOM 4937 O SER C 48 23.378 20.556 32.623 1.00 34.38 O
ANISOU 4937 O SER C 48 5681 3238 4143 413 607 -632 O
ATOM 4938 CB SER C 48 24.563 19.317 29.856 1.00 33.16 C
ANISOU 4938 CB SER C 48 5486 3058 4055 173 326 -486 C
ATOM 4939 OG SER C 48 24.869 18.488 30.961 1.00 35.18 O
ANISOU 4939 OG SER C 48 5809 3340 4216 200 454 -465 O
ATOM 4940 N GLU C 49 21.763 20.279 31.074 1.00 36.74 N
ANISOU 4940 N GLU C 49 5727 3506 4727 400 547 -617 N
ATOM 4941 CA GLU C 49 20.685 20.062 32.035 1.00 34.35 C
ANISOU 4941 CA GLU C 49 5297 3311 4443 444 743 -702 C
ATOM 4942 C GLU C 49 19.848 18.889 31.551 1.00 38.23 C
ANISOU 4942 C GLU C 49 5616 3867 5043 326 846 -674 C
ATOM 4943 O GLU C 49 19.131 19.024 30.538 1.00 38.89 O
ANISOU 4943 O GLU C 49 5532 3969 5274 354 751 -738 O
ATOM 4944 CB GLU C 49 19.827 21.313 32.194 1.00 42.97 C
ANISOU 4944 CB GLU C 49 6289 4399 5637 623 689 -878 C
ATOM 4945 CG GLU C 49 18.622 21.132 33.100 1.00 52.92 C
ANISOU 4945 CG GLU C 49 7344 5858 6906 659 892 -1038 C
ATOM 4946 CD GLU C 49 17.643 22.282 32.991 1.00 65.55 C
ANISOU 4946 CD GLU C 49 8781 7465 8661 882 788 -1273 C
ATOM 4947 OE1 GLU C 49 17.820 23.133 32.095 1.00 67.13 O
ANISOU 4947 OE1 GLU C 49 9058 7465 8985 1008 543 -1250 O
ATOM 4948 OE2 GLU C 49 16.695 22.338 33.799 1.00 71.63 O
ANISOU 4948 OE2 GLU C 49 9345 8448 9423 936 942 -1483 O
ATOM 4949 N PRO C 50 19.903 17.729 32.221 1.00 37.40 N
ANISOU 4949 N PRO C 50 5548 3789 4874 192 1029 -579 N
ATOM 4950 CA PRO C 50 20.723 17.481 33.413 1.00 33.25 C
ANISOU 4950 CA PRO C 50 5221 3277 4135 187 1121 -472 C
ATOM 4951 C PRO C 50 22.184 17.202 33.070 1.00 35.57 C
ANISOU 4951 C PRO C 50 5705 3465 4346 194 962 -376 C
ATOM 4952 O PRO C 50 22.567 17.323 31.907 1.00 33.95 O
ANISOU 4952 O PRO C 50 5467 3195 4235 181 793 -405 O
ATOM 4953 CB PRO C 50 20.071 16.239 34.017 1.00 31.52 C
ANISOU 4953 CB PRO C 50 4974 3092 3910 22 1355 -359 C
ATOM 4954 CG PRO C 50 19.577 15.487 32.818 1.00 33.70 C
ANISOU 4954 CG PRO C 50 5107 3272 4427 -93 1320 -384 C
ATOM 4955 CD PRO C 50 19.128 16.535 31.830 1.00 35.16 C
ANISOU 4955 CD PRO C 50 5115 3514 4729 29 1154 -563 C
ATOM 4956 N CYS C 51 22.984 16.840 34.069 1.00 36.30 N
ANISOU 4956 N CYS C 51 5969 3589 4236 221 1012 -282 N
ATOM 4957 CA CYS C 51 24.331 16.359 33.801 1.00 35.33 C
ANISOU 4957 CA CYS C 51 5986 3403 4033 245 863 -229 C
ATOM 4958 C CYS C 51 24.258 15.098 32.946 1.00 38.65 C
ANISOU 4958 C CYS C 51 6371 3681 4633 149 830 -160 C
ATOM 4959 O CYS C 51 23.327 14.297 33.058 1.00 37.16 O
ANISOU 4959 O CYS C 51 6130 3422 4569 44 979 -81 O
ATOM 4960 CB CYS C 51 25.062 16.081 35.115 1.00 46.04 C
ANISOU 4960 CB CYS C 51 7517 4850 5124 331 915 -138 C
ATOM 4961 SG CYS C 51 26.844 15.800 35.001 1.00 53.07 S
ANISOU 4961 SG CYS C 51 8545 5760 5860 440 699 -172 S
ATOM 4962 N ILE C 52 25.246 14.928 32.071 1.00 32.47 N
ANISOU 4962 N ILE C 52 5593 2874 3871 163 641 -230 N
ATOM 4963 CA ILE C 52 25.176 13.867 31.071 1.00 30.89 C
ANISOU 4963 CA ILE C 52 5297 2566 3873 83 579 -257 C
ATOM 4964 C ILE C 52 25.411 12.513 31.728 1.00 36.20 C
ANISOU 4964 C ILE C 52 6116 3062 4576 99 627 -120 C
ATOM 4965 O ILE C 52 26.453 12.274 32.349 1.00 35.98 O
ANISOU 4965 O ILE C 52 6255 3033 4383 231 540 -72 O
ATOM 4966 CB ILE C 52 26.177 14.113 29.938 1.00 32.80 C
ANISOU 4966 CB ILE C 52 5462 2905 4093 85 364 -414 C
ATOM 4967 CG1 ILE C 52 25.591 15.099 28.932 1.00 32.93 C
ANISOU 4967 CG1 ILE C 52 5322 3027 4161 14 318 -485 C
ATOM 4968 CG2 ILE C 52 26.538 12.809 29.249 1.00 24.26 C
ANISOU 4968 CG2 ILE C 52 4313 1737 3167 63 275 -492 C
ATOM 4969 CD1 ILE C 52 26.600 16.066 28.406 1.00 33.78 C
ANISOU 4969 CD1 ILE C 52 5455 3272 4107 -2 167 -559 C
ATOM 4970 N ARG C 53 24.440 11.618 31.580 1.00 32.84 N
ANISOU 4970 N ARG C 53 5631 2478 4368 -34 756 -60 N
ATOM 4971 CA ARG C 53 24.584 10.217 31.944 1.00 35.71 C
ANISOU 4971 CA ARG C 53 6145 2574 4850 -59 782 81 C
ATOM 4972 C ARG C 53 24.999 9.452 30.694 1.00 37.66 C
ANISOU 4972 C ARG C 53 6257 2708 5344 -68 607 -120 C
ATOM 4973 O ARG C 53 24.237 9.389 29.722 1.00 35.78 O
ANISOU 4973 O ARG C 53 5780 2505 5309 -204 635 -280 O
ATOM 4974 CB ARG C 53 23.274 9.668 32.509 1.00 44.80 C
ANISOU 4974 CB ARG C 53 7302 3606 6113 -261 1050 239 C
ATOM 4975 CG ARG C 53 23.427 8.471 33.429 1.00 53.54 C
ANISOU 4975 CG ARG C 53 8690 4425 7227 -296 1127 525 C
ATOM 4976 CD ARG C 53 22.066 7.990 33.911 1.00 62.57 C
ANISOU 4976 CD ARG C 53 9812 5491 8469 -583 1431 670 C
ATOM 4977 NE ARG C 53 21.441 7.066 32.969 1.00 71.15 N
ANISOU 4977 NE ARG C 53 10748 6339 9947 -785 1467 537 N
ATOM 4978 CZ ARG C 53 20.141 7.046 32.694 1.00 76.63 C
ANISOU 4978 CZ ARG C 53 11204 7115 10797 -1042 1685 423 C
ATOM 4979 NH1 ARG C 53 19.324 7.914 33.276 1.00 80.94 N
ANISOU 4979 NH1 ARG C 53 11632 7977 11142 -1107 1873 419 N
ATOM 4980 NH2 ARG C 53 19.657 6.169 31.826 1.00 74.36 N
ANISOU 4980 NH2 ARG C 53 10760 6622 10871 -1225 1706 257 N
ATOM 4981 N LEU C 54 26.212 8.889 30.709 1.00 32.76 N
ANISOU 4981 N LEU C 54 5756 2000 4692 96 412 -155 N
ATOM 4982 CA LEU C 54 26.730 8.203 29.529 1.00 35.71 C
ANISOU 4982 CA LEU C 54 5961 2326 5279 115 222 -420 C
ATOM 4983 C LEU C 54 25.891 6.987 29.144 1.00 43.45 C
ANISOU 4983 C LEU C 54 6882 2991 6635 -37 303 -443 C
ATOM 4984 O LEU C 54 25.949 6.553 27.988 1.00 47.52 O
ANISOU 4984 O LEU C 54 7160 3533 7364 -78 191 -733 O
ATOM 4985 CB LEU C 54 28.188 7.796 29.756 1.00 36.33 C
ANISOU 4985 CB LEU C 54 6165 2386 5251 357 -13 -494 C
ATOM 4986 CG LEU C 54 29.183 8.951 29.915 1.00 41.30 C
ANISOU 4986 CG LEU C 54 6785 3376 5534 472 -115 -584 C
ATOM 4987 CD1 LEU C 54 30.605 8.436 30.058 1.00 42.67 C
ANISOU 4987 CD1 LEU C 54 7015 3581 5616 718 -358 -736 C
ATOM 4988 CD2 LEU C 54 29.080 9.923 28.746 1.00 36.03 C
ANISOU 4988 CD2 LEU C 54 5848 3017 4824 324 -137 -798 C
ATOM 4989 N ARG C 55 25.115 6.431 30.080 1.00 49.41 N
ANISOU 4989 N ARG C 55 7833 3474 7466 -149 507 -163 N
ATOM 4990 CA ARG C 55 24.151 5.396 29.718 1.00 52.96 C
ANISOU 4990 CA ARG C 55 8206 3630 8287 -375 639 -196 C
ATOM 4991 C ARG C 55 23.101 5.924 28.750 1.00 43.96 C
ANISOU 4991 C ARG C 55 6698 2754 7249 -563 744 -438 C
ATOM 4992 O ARG C 55 22.623 5.181 27.886 1.00 49.22 O
ANISOU 4992 O ARG C 55 7144 3358 8199 -691 728 -658 O
ATOM 4993 CB ARG C 55 23.466 4.842 30.968 1.00 65.63 C
ANISOU 4993 CB ARG C 55 10067 5000 9870 -520 857 185 C
ATOM 4994 CG ARG C 55 24.256 3.797 31.733 1.00 76.44 C
ANISOU 4994 CG ARG C 55 11738 6054 11253 -373 695 433 C
ATOM 4995 CD ARG C 55 23.406 3.180 32.835 1.00 88.03 C
ANISOU 4995 CD ARG C 55 13403 7346 12699 -595 915 816 C
ATOM 4996 NE ARG C 55 22.970 4.170 33.817 1.00 93.76 N
ANISOU 4996 NE ARG C 55 14226 8343 13058 -652 1165 1030 N
ATOM 4997 CZ ARG C 55 23.387 4.208 35.079 1.00 99.06 C
ANISOU 4997 CZ ARG C 55 15184 9045 13410 -544 1184 1373 C
ATOM 4998 NH1 ARG C 55 24.249 3.304 35.526 1.00102.25 N
ANISOU 4998 NH1 ARG C 55 15812 9205 13835 -362 963 1570 N
ATOM 4999 NH2 ARG C 55 22.937 5.145 35.901 1.00 99.04 N
ANISOU 4999 NH2 ARG C 55 15224 9343 13066 -605 1414 1501 N
ATOM 5000 N GLY C 56 22.727 7.194 28.882 1.00 32.05 N
ANISOU 5000 N GLY C 56 6194 2393 3590 -238 -387 85 N
ATOM 5001 CA GLY C 56 21.713 7.795 28.039 1.00 28.52 C
ANISOU 5001 CA GLY C 56 5562 2034 3241 -303 -289 100 C
ATOM 5002 C GLY C 56 21.144 9.044 28.676 1.00 33.23 C
ANISOU 5002 C GLY C 56 6129 2689 3806 -311 -136 145 C
ATOM 5003 O GLY C 56 20.950 9.089 29.894 1.00 33.76 O
ANISOU 5003 O GLY C 56 6345 2696 3786 -317 -56 204 O
ATOM 5004 N THR C 57 20.870 10.069 27.873 1.00 26.94 N
ANISOU 5004 N THR C 57 5156 2005 3075 -307 -88 120 N
ATOM 5005 CA THR C 57 20.422 11.342 28.414 1.00 28.21 C
ANISOU 5005 CA THR C 57 5288 2220 3209 -300 58 154 C
ATOM 5006 C THR C 57 19.541 12.062 27.405 1.00 30.47 C
ANISOU 5006 C THR C 57 5360 2607 3611 -335 137 170 C
ATOM 5007 O THR C 57 19.860 12.109 26.214 1.00 41.26 O
ANISOU 5007 O THR C 57 6599 4038 5041 -320 45 110 O
ATOM 5008 CB THR C 57 21.608 12.241 28.782 1.00 27.29 C
ANISOU 5008 CB THR C 57 5227 2136 3005 -209 5 81 C
ATOM 5009 OG1 THR C 57 22.479 11.546 29.684 1.00 28.44 O
ANISOU 5009 OG1 THR C 57 5566 2193 3047 -173 -93 67 O
ATOM 5010 CG2 THR C 57 21.124 13.524 29.439 1.00 26.17 C
ANISOU 5010 CG2 THR C 57 5089 2031 2824 -205 164 114 C
ATOM 5011 N ASN C 58 18.434 12.612 27.893 1.00 29.82 N
ANISOU 5011 N ASN C 58 5243 2535 3554 -378 309 255 N
ATOM 5012 CA ASN C 58 17.672 13.640 27.199 1.00 35.04 C
ANISOU 5012 CA ASN C 58 5713 3295 4307 -386 407 279 C
ATOM 5013 C ASN C 58 17.814 14.933 27.989 1.00 31.52 C
ANISOU 5013 C ASN C 58 5317 2870 3788 -328 530 281 C
ATOM 5014 O ASN C 58 17.526 14.961 29.190 1.00 41.24 O
ANISOU 5014 O ASN C 58 6692 4034 4943 -334 642 334 O
ATOM 5015 CB ASN C 58 16.196 13.258 27.074 1.00 43.82 C
ANISOU 5015 CB ASN C 58 6720 4401 5529 -480 516 384 C
ATOM 5016 CG ASN C 58 15.976 12.070 26.165 1.00 51.82 C
ANISOU 5016 CG ASN C 58 7669 5396 6623 -550 389 377 C
ATOM 5017 OD1 ASN C 58 16.918 11.536 25.582 1.00 53.97 O
ANISOU 5017 OD1 ASN C 58 7978 5660 6867 -520 229 292 O
ATOM 5018 ND2 ASN C 58 14.723 11.642 26.043 1.00 58.26 N
ANISOU 5018 ND2 ASN C 58 8390 6202 7546 -645 462 468 N
ATOM 5019 N GLY C 59 18.266 15.989 27.330 1.00 29.69 N
ANISOU 5019 N GLY C 59 4984 2724 3573 -273 512 223 N
ATOM 5020 CA GLY C 59 18.445 17.241 28.028 1.00 30.13 C
ANISOU 5020 CA GLY C 59 5095 2792 3561 -221 622 216 C
ATOM 5021 C GLY C 59 18.700 18.400 27.095 1.00 28.05 C
ANISOU 5021 C GLY C 59 4682 2627 3350 -175 620 169 C
ATOM 5022 O GLY C 59 18.388 18.347 25.904 1.00 32.60 O
ANISOU 5022 O GLY C 59 5088 3271 4027 -189 575 169 O
ATOM 5023 N PHE C 60 19.278 19.453 27.666 1.00 24.35 N
ANISOU 5023 N PHE C 60 4290 2157 2803 -121 666 130 N
ATOM 5024 CA PHE C 60 19.590 20.681 26.955 1.00 29.03 C
ANISOU 5024 CA PHE C 60 4769 2827 3432 -74 682 87 C
ATOM 5025 C PHE C 60 21.035 21.070 27.212 1.00 27.21 C
ANISOU 5025 C PHE C 60 4638 2587 3114 -26 571 -13 C
ATOM 5026 O PHE C 60 21.536 20.922 28.330 1.00 30.40 O
ANISOU 5026 O PHE C 60 5222 2920 3408 -20 554 -30 O
ATOM 5027 CB PHE C 60 18.678 21.831 27.392 1.00 31.22 C
ANISOU 5027 CB PHE C 60 5025 3112 3724 -61 887 149 C
ATOM 5028 CG PHE C 60 17.262 21.691 26.927 1.00 30.61 C
ANISOU 5028 CG PHE C 60 4794 3068 3768 -99 997 251 C
ATOM 5029 CD1 PHE C 60 16.337 20.989 27.682 1.00 28.65 C
ANISOU 5029 CD1 PHE C 60 4598 2761 3526 -149 1096 337 C
ATOM 5030 CD2 PHE C 60 16.856 22.264 25.737 1.00 28.80 C
ANISOU 5030 CD2 PHE C 60 4365 2928 3649 -87 1000 265 C
ATOM 5031 CE1 PHE C 60 15.028 20.862 27.252 1.00 29.80 C
ANISOU 5031 CE1 PHE C 60 4582 2940 3801 -189 1194 435 C
ATOM 5032 CE2 PHE C 60 15.552 22.140 25.299 1.00 24.55 C
ANISOU 5032 CE2 PHE C 60 3672 2424 3231 -123 1085 363 C
ATOM 5033 CZ PHE C 60 14.636 21.439 26.057 1.00 27.03 C
ANISOU 5033 CZ PHE C 60 4022 2682 3565 -177 1180 448 C
ATOM 5034 N VAL C 61 21.693 21.570 26.174 1.00 26.73 N
ANISOU 5034 N VAL C 61 4456 2596 3103 6 494 -75 N
ATOM 5035 CA VAL C 61 22.984 22.232 26.297 1.00 26.39 C
ANISOU 5035 CA VAL C 61 4463 2558 3006 50 415 -163 C
ATOM 5036 C VAL C 61 22.713 23.729 26.272 1.00 21.83 C
ANISOU 5036 C VAL C 61 3842 2011 2440 73 548 -157 C
ATOM 5037 O VAL C 61 22.265 24.275 25.258 1.00 24.08 O
ANISOU 5037 O VAL C 61 3969 2365 2814 83 597 -139 O
ATOM 5038 CB VAL C 61 23.946 21.815 25.177 1.00 24.66 C
ANISOU 5038 CB VAL C 61 4143 2388 2838 73 258 -232 C
ATOM 5039 CG1 VAL C 61 25.314 22.441 25.390 1.00 25.79 C
ANISOU 5039 CG1 VAL C 61 4330 2532 2939 112 175 -317 C
ATOM 5040 CG2 VAL C 61 24.047 20.297 25.103 1.00 20.55 C
ANISOU 5040 CG2 VAL C 61 3661 1831 2318 53 144 -230 C
ATOM 5041 N HIS C 62 22.948 24.396 27.395 1.00 21.45 N
ANISOU 5041 N HIS C 62 3944 1906 2299 82 609 -171 N
ATOM 5042 CA HIS C 62 22.764 25.836 27.476 1.00 21.43 C
ANISOU 5042 CA HIS C 62 3931 1914 2298 105 738 -174 C
ATOM 5043 C HIS C 62 24.072 26.516 27.102 1.00 33.03 C
ANISOU 5043 C HIS C 62 5380 3407 3761 129 630 -268 C
ATOM 5044 O HIS C 62 25.125 26.205 27.670 1.00 27.54 O
ANISOU 5044 O HIS C 62 4792 2675 2995 127 502 -330 O
ATOM 5045 CB HIS C 62 22.323 26.254 28.877 1.00 24.80 C
ANISOU 5045 CB HIS C 62 4546 2257 2619 100 869 -146 C
ATOM 5046 CG HIS C 62 21.075 25.570 29.342 1.00 29.41 C
ANISOU 5046 CG HIS C 62 5155 2809 3209 75 989 -48 C
ATOM 5047 ND1 HIS C 62 19.832 25.852 28.819 1.00 31.37 N
ANISOU 5047 ND1 HIS C 62 5260 3098 3563 76 1138 36 N
ATOM 5048 CD2 HIS C 62 20.879 24.617 30.283 1.00 31.77 C
ANISOU 5048 CD2 HIS C 62 5601 3039 3430 47 984 -16 C
ATOM 5049 CE1 HIS C 62 18.923 25.101 29.417 1.00 33.15 C
ANISOU 5049 CE1 HIS C 62 5533 3281 3782 45 1223 115 C
ATOM 5050 NE2 HIS C 62 19.533 24.344 30.310 1.00 29.58 N
ANISOU 5050 NE2 HIS C 62 5263 2760 3215 26 1138 85 N
ATOM 5051 N VAL C 63 24.009 27.422 26.129 1.00 24.58 N
ANISOU 5051 N VAL C 63 4168 2399 2772 152 680 -273 N
ATOM 5052 CA VAL C 63 25.183 28.133 25.639 1.00 26.84 C
ANISOU 5052 CA VAL C 63 4412 2713 3074 170 599 -353 C
ATOM 5053 C VAL C 63 24.901 29.626 25.704 1.00 34.34 C
ANISOU 5053 C VAL C 63 5362 3654 4031 186 743 -348 C
ATOM 5054 O VAL C 63 23.867 30.091 25.210 1.00 34.92 O
ANISOU 5054 O VAL C 63 5344 3758 4166 203 876 -281 O
ATOM 5055 CB VAL C 63 25.557 27.717 24.202 1.00 27.12 C
ANISOU 5055 CB VAL C 63 4272 2828 3202 184 506 -371 C
ATOM 5056 CG1 VAL C 63 26.777 28.497 23.725 1.00 25.58 C
ANISOU 5056 CG1 VAL C 63 4032 2657 3030 203 443 -448 C
ATOM 5057 CG2 VAL C 63 25.830 26.225 24.127 1.00 26.22 C
ANISOU 5057 CG2 VAL C 63 4171 2710 3083 172 370 -380 C
ATOM 5058 N GLU C 64 25.815 30.373 26.323 1.00 30.56 N
ANISOU 5058 N GLU C 64 4988 3131 3493 181 712 -416 N
ATOM 5059 CA GLU C 64 25.752 31.829 26.335 1.00 24.37 C
ANISOU 5059 CA GLU C 64 4214 2330 2716 194 832 -427 C
ATOM 5060 C GLU C 64 27.161 32.369 26.159 1.00 24.86 C
ANISOU 5060 C GLU C 64 4271 2392 2783 183 714 -519 C
ATOM 5061 O GLU C 64 28.023 32.147 27.016 1.00 30.02 O
ANISOU 5061 O GLU C 64 5049 2997 3360 156 602 -578 O
ATOM 5062 CB GLU C 64 25.128 32.366 27.626 1.00 26.06 C
ANISOU 5062 CB GLU C 64 4614 2455 2833 189 968 -406 C
ATOM 5063 CG GLU C 64 24.988 33.883 27.635 1.00 46.39 C
ANISOU 5063 CG GLU C 64 7211 4999 5418 207 1107 -416 C
ATOM 5064 CD GLU C 64 24.188 34.395 28.813 1.00 59.21 C
ANISOU 5064 CD GLU C 64 9013 6532 6950 214 1275 -385 C
ATOM 5065 OE1 GLU C 64 24.095 33.680 29.828 1.00 62.88 O
ANISOU 5065 OE1 GLU C 64 9631 6946 7315 194 1253 -383 O
ATOM 5066 OE2 GLU C 64 23.646 35.516 28.722 1.00 61.59 O
ANISOU 5066 OE2 GLU C 64 9312 6809 7279 245 1437 -362 O
ATOM 5067 N PHE C 65 27.397 33.067 25.052 1.00 21.48 N
ANISOU 5067 N PHE C 65 3698 2017 2445 201 737 -526 N
ATOM 5068 CA PHE C 65 28.700 33.669 24.797 1.00 24.78 C
ANISOU 5068 CA PHE C 65 4090 2437 2888 186 647 -605 C
ATOM 5069 C PHE C 65 28.558 34.683 23.673 1.00 24.79 C
ANISOU 5069 C PHE C 65 3957 2481 2979 210 745 -587 C
ATOM 5070 O PHE C 65 27.510 34.791 23.029 1.00 23.77 O
ANISOU 5070 O PHE C 65 3747 2391 2894 242 855 -513 O
ATOM 5071 CB PHE C 65 29.762 32.616 24.449 1.00 22.84 C
ANISOU 5071 CB PHE C 65 3781 2230 2667 180 459 -652 C
ATOM 5072 CG PHE C 65 29.687 32.105 23.034 1.00 19.72 C
ANISOU 5072 CG PHE C 65 3206 1922 2365 211 442 -627 C
ATOM 5073 CD1 PHE C 65 28.494 31.648 22.500 1.00 17.92 C
ANISOU 5073 CD1 PHE C 65 2920 1732 2159 231 518 -553 C
ATOM 5074 CD2 PHE C 65 30.823 32.075 22.242 1.00 20.51 C
ANISOU 5074 CD2 PHE C 65 3199 2062 2530 218 347 -679 C
ATOM 5075 CE1 PHE C 65 28.435 31.178 21.206 1.00 18.73 C
ANISOU 5075 CE1 PHE C 65 2877 1908 2331 255 490 -536 C
ATOM 5076 CE2 PHE C 65 30.771 31.607 20.947 1.00 21.02 C
ANISOU 5076 CE2 PHE C 65 3123 2200 2663 249 338 -661 C
ATOM 5077 CZ PHE C 65 29.576 31.156 20.428 1.00 17.98 C
ANISOU 5077 CZ PHE C 65 2697 1849 2284 266 403 -592 C
ATOM 5078 N ILE C 66 29.638 35.427 23.446 1.00 26.30 N
ANISOU 5078 N ILE C 66 4126 2665 3201 192 698 -650 N
ATOM 5079 CA ILE C 66 29.760 36.399 22.374 1.00 22.44 C
ANISOU 5079 CA ILE C 66 3519 2211 2797 209 774 -641 C
ATOM 5080 C ILE C 66 30.846 35.891 21.419 1.00 18.20 C
ANISOU 5080 C ILE C 66 2847 1738 2329 210 649 -681 C
ATOM 5081 O ILE C 66 32.037 35.977 21.744 1.00 27.60 O
ANISOU 5081 O ILE C 66 4053 2906 3527 176 544 -751 O
ATOM 5082 CB ILE C 66 30.098 37.795 22.915 1.00 21.89 C
ANISOU 5082 CB ILE C 66 3542 2064 2711 182 848 -679 C
ATOM 5083 CG1 ILE C 66 28.977 38.295 23.832 1.00 19.93 C
ANISOU 5083 CG1 ILE C 66 3435 1745 2391 194 994 -638 C
ATOM 5084 CG2 ILE C 66 30.344 38.771 21.776 1.00 21.65 C
ANISOU 5084 CG2 ILE C 66 3391 2063 2772 198 920 -669 C
ATOM 5085 CD1 ILE C 66 29.346 39.526 24.635 1.00 20.82 C
ANISOU 5085 CD1 ILE C 66 3693 1759 2460 159 1051 -690 C
ATOM 5086 N PRO C 67 30.483 35.349 20.258 1.00 19.59 N
ANISOU 5086 N PRO C 67 2894 1992 2558 248 655 -639 N
ATOM 5087 CA PRO C 67 31.488 34.733 19.382 1.00 21.22 C
ANISOU 5087 CA PRO C 67 2989 2253 2819 257 546 -677 C
ATOM 5088 C PRO C 67 32.464 35.739 18.792 1.00 24.37 C
ANISOU 5088 C PRO C 67 3319 2656 3286 247 567 -715 C
ATOM 5089 O PRO C 67 32.138 36.904 18.553 1.00 21.86 O
ANISOU 5089 O PRO C 67 3000 2320 2986 248 687 -691 O
ATOM 5090 CB PRO C 67 30.642 34.077 18.281 1.00 19.44 C
ANISOU 5090 CB PRO C 67 2669 2099 2617 298 575 -616 C
ATOM 5091 CG PRO C 67 29.317 34.787 18.338 1.00 19.70 C
ANISOU 5091 CG PRO C 67 2723 2123 2639 312 717 -541 C
ATOM 5092 CD PRO C 67 29.116 35.080 19.791 1.00 22.72 C
ANISOU 5092 CD PRO C 67 3251 2425 2957 282 745 -554 C
ATOM 5093 N ARG C 68 33.682 35.257 18.554 1.00 29.18 N
ANISOU 5093 N ARG C 68 3865 3284 3936 239 453 -771 N
ATOM 5094 CA ARG C 68 34.742 36.040 17.936 1.00 28.98 C
ANISOU 5094 CA ARG C 68 3753 3267 3991 226 463 -806 C
ATOM 5095 C ARG C 68 34.720 35.957 16.416 1.00 24.49 C
ANISOU 5095 C ARG C 68 3056 2771 3478 273 520 -775 C
ATOM 5096 O ARG C 68 35.659 36.432 15.768 1.00 29.19 O
ANISOU 5096 O ARG C 68 3566 3380 4145 269 532 -800 O
ATOM 5097 CB ARG C 68 36.105 35.582 18.469 1.00 30.71 C
ANISOU 5097 CB ARG C 68 3956 3470 4242 197 314 -878 C
ATOM 5098 CG ARG C 68 36.243 35.673 19.988 1.00 36.37 C
ANISOU 5098 CG ARG C 68 4815 4113 4892 146 236 -914 C
ATOM 5099 CD ARG C 68 35.654 36.974 20.490 1.00 38.09 C
ANISOU 5099 CD ARG C 68 5132 4269 5072 112 354 -903 C
ATOM 5100 NE ARG C 68 36.289 37.494 21.698 1.00 48.93 N
ANISOU 5100 NE ARG C 68 6618 5564 6408 47 280 -961 N
ATOM 5101 CZ ARG C 68 35.699 37.570 22.888 1.00 49.82 C
ANISOU 5101 CZ ARG C 68 6905 5611 6414 25 284 -964 C
ATOM 5102 NH1 ARG C 68 34.447 37.158 23.048 1.00 39.77 N
ANISOU 5102 NH1 ARG C 68 5698 4341 5072 64 368 -906 N
ATOM 5103 NH2 ARG C 68 36.363 38.066 23.921 1.00 56.15 N
ANISOU 5103 NH2 ARG C 68 7817 6340 7177 -39 203 -1023 N
ATOM 5104 N GLY C 69 33.680 35.359 15.843 1.00 24.47 N
ANISOU 5104 N GLY C 69 3043 2813 3444 314 553 -720 N
ATOM 5105 CA GLY C 69 33.496 35.297 14.406 1.00 16.30 C
ANISOU 5105 CA GLY C 69 1912 1844 2439 358 605 -685 C
ATOM 5106 C GLY C 69 32.070 34.888 14.122 1.00 17.15 C
ANISOU 5106 C GLY C 69 2036 1980 2499 384 643 -615 C
ATOM 5107 O GLY C 69 31.327 34.477 15.017 1.00 19.28 O
ANISOU 5107 O GLY C 69 2379 2223 2724 370 624 -597 O
ATOM 5108 N ASN C 70 31.690 35.014 12.854 1.00 15.71 N
ANISOU 5108 N ASN C 70 1786 1854 2329 421 696 -572 N
ATOM 5109 CA ASN C 70 30.386 34.534 12.428 1.00 18.43 C
ANISOU 5109 CA ASN C 70 2125 2235 2640 443 709 -504 C
ATOM 5110 C ASN C 70 30.303 33.021 12.613 1.00 27.15 C
ANISOU 5110 C ASN C 70 3248 3352 3715 438 591 -528 C
ATOM 5111 O ASN C 70 31.302 32.300 12.506 1.00 26.33 O
ANISOU 5111 O ASN C 70 3134 3249 3621 442 508 -589 O
ATOM 5112 CB ASN C 70 30.128 34.908 10.969 1.00 15.44 C
ANISOU 5112 CB ASN C 70 1678 1916 2272 482 764 -459 C
ATOM 5113 CG ASN C 70 30.285 36.397 10.711 1.00 24.48 C
ANISOU 5113 CG ASN C 70 2813 3047 3444 486 871 -428 C
ATOM 5114 OD1 ASN C 70 30.080 37.218 11.606 1.00 25.87 O
ANISOU 5114 OD1 ASN C 70 3037 3171 3623 462 920 -415 O
ATOM 5115 ND2 ASN C 70 30.648 36.752 9.483 1.00 27.35 N
ANISOU 5115 ND2 ASN C 70 3134 3457 3799 503 874 -402 N
ATOM 5116 N LEU C 71 29.098 32.543 12.917 1.00 19.94 N
ANISOU 5116 N LEU C 71 2361 2442 2774 430 589 -474 N
ATOM 5117 CA LEU C 71 28.849 31.126 13.142 1.00 18.33 C
ANISOU 5117 CA LEU C 71 2184 2239 2543 417 486 -486 C
ATOM 5118 C LEU C 71 28.214 30.445 11.936 1.00 16.93 C
ANISOU 5118 C LEU C 71 1956 2119 2358 434 455 -453 C
ATOM 5119 O LEU C 71 27.715 29.323 12.065 1.00 20.70 O
ANISOU 5119 O LEU C 71 2456 2593 2815 415 381 -447 O
ATOM 5120 CB LEU C 71 27.955 30.932 14.369 1.00 18.87 C
ANISOU 5120 CB LEU C 71 2321 2263 2586 386 501 -450 C
ATOM 5121 CG LEU C 71 28.429 31.527 15.696 1.00 20.74 C
ANISOU 5121 CG LEU C 71 2642 2433 2806 364 526 -482 C
ATOM 5122 CD1 LEU C 71 27.473 31.169 16.831 1.00 15.88 C
ANISOU 5122 CD1 LEU C 71 2108 1773 2152 339 549 -441 C
ATOM 5123 CD2 LEU C 71 29.840 31.060 15.999 1.00 15.67 C
ANISOU 5123 CD2 LEU C 71 2022 1769 2164 359 421 -566 C
ATOM 5124 N LYS C 72 28.235 31.092 10.766 1.00 17.01 N
ANISOU 5124 N LYS C 72 1908 2176 2378 464 504 -432 N
ATOM 5125 CA LYS C 72 27.543 30.565 9.592 1.00 15.29 C
ANISOU 5125 CA LYS C 72 1656 2013 2141 477 470 -395 C
ATOM 5126 C LYS C 72 28.059 29.187 9.196 1.00 21.42 C
ANISOU 5126 C LYS C 72 2456 2790 2890 477 360 -455 C
ATOM 5127 O LYS C 72 27.296 28.368 8.672 1.00 21.91 O
ANISOU 5127 O LYS C 72 2521 2875 2928 464 300 -432 O
ATOM 5128 CB LYS C 72 27.699 31.544 8.427 1.00 15.39 C
ANISOU 5128 CB LYS C 72 1622 2069 2158 515 542 -369 C
ATOM 5129 CG LYS C 72 26.787 31.296 7.231 1.00 29.60 C
ANISOU 5129 CG LYS C 72 3392 3928 3928 529 515 -312 C
ATOM 5130 CD LYS C 72 27.125 32.272 6.104 1.00 32.75 C
ANISOU 5130 CD LYS C 72 3764 4362 4318 572 588 -290 C
ATOM 5131 CE LYS C 72 25.907 32.634 5.256 1.00 40.77 C
ANISOU 5131 CE LYS C 72 4745 5429 5318 587 594 -196 C
ATOM 5132 NZ LYS C 72 25.494 31.540 4.334 1.00 45.25 N
ANISOU 5132 NZ LYS C 72 5327 6037 5831 579 483 -200 N
ATOM 5133 N TYR C 73 29.341 28.913 9.433 1.00 21.54 N
ANISOU 5133 N TYR C 73 2489 2778 2916 491 331 -531 N
ATOM 5134 CA TYR C 73 29.965 27.642 9.089 1.00 15.46 C
ANISOU 5134 CA TYR C 73 1746 1999 2129 504 239 -592 C
ATOM 5135 C TYR C 73 30.645 27.030 10.308 1.00 22.80 C
ANISOU 5135 C TYR C 73 2719 2871 3074 491 176 -640 C
ATOM 5136 O TYR C 73 31.739 26.470 10.216 1.00 31.23 O
ANISOU 5136 O TYR C 73 3788 3922 4157 520 129 -703 O
ATOM 5137 CB TYR C 73 30.974 27.813 7.956 1.00 19.32 C
ANISOU 5137 CB TYR C 73 2204 2516 2622 553 266 -634 C
ATOM 5138 CG TYR C 73 30.404 28.380 6.674 1.00 19.52 C
ANISOU 5138 CG TYR C 73 2204 2596 2616 572 322 -587 C
ATOM 5139 CD1 TYR C 73 29.846 27.548 5.710 1.00 20.69 C
ANISOU 5139 CD1 TYR C 73 2382 2770 2711 576 265 -582 C
ATOM 5140 CD2 TYR C 73 30.436 29.748 6.421 1.00 26.72 C
ANISOU 5140 CD2 TYR C 73 3075 3529 3550 583 426 -548 C
ATOM 5141 CE1 TYR C 73 29.329 28.059 4.539 1.00 20.32 C
ANISOU 5141 CE1 TYR C 73 2324 2774 2624 594 301 -537 C
ATOM 5142 CE2 TYR C 73 29.923 30.270 5.251 1.00 26.82 C
ANISOU 5142 CE2 TYR C 73 3073 3590 3528 606 472 -498 C
ATOM 5143 CZ TYR C 73 29.373 29.418 4.315 1.00 23.78 C
ANISOU 5143 CZ TYR C 73 2718 3235 3082 612 405 -492 C
ATOM 5144 OH TYR C 73 28.858 29.932 3.147 1.00 34.79 O
ANISOU 5144 OH TYR C 73 4109 4678 4432 634 436 -440 O
ATOM 5145 N LEU C 74 30.005 27.140 11.469 1.00 20.04 N
ANISOU 5145 N LEU C 74 2407 2488 2720 453 178 -608 N
ATOM 5146 CA LEU C 74 30.585 26.612 12.698 1.00 21.91 C
ANISOU 5146 CA LEU C 74 2702 2666 2956 439 114 -646 C
ATOM 5147 C LEU C 74 30.719 25.094 12.631 1.00 24.80 C
ANISOU 5147 C LEU C 74 3112 3008 3304 445 9 -676 C
ATOM 5148 O LEU C 74 29.762 24.386 12.303 1.00 24.88 O
ANISOU 5148 O LEU C 74 3142 3023 3290 423 -15 -644 O
ATOM 5149 CB LEU C 74 29.723 27.018 13.896 1.00 22.62 C
ANISOU 5149 CB LEU C 74 2844 2723 3028 397 153 -597 C
ATOM 5150 CG LEU C 74 30.021 26.369 15.250 1.00 24.40 C
ANISOU 5150 CG LEU C 74 3160 2884 3229 376 84 -620 C
ATOM 5151 CD1 LEU C 74 31.349 26.850 15.811 1.00 20.12 C
ANISOU 5151 CD1 LEU C 74 2624 2316 2704 388 54 -679 C
ATOM 5152 CD2 LEU C 74 28.883 26.620 16.236 1.00 22.29 C
ANISOU 5152 CD2 LEU C 74 2952 2586 2931 337 143 -559 C
ATOM 5153 N TYR C 75 31.922 24.599 12.925 1.00 18.81 N
ANISOU 5153 N TYR C 75 2365 2218 2564 474 -56 -738 N
ATOM 5154 CA TYR C 75 32.151 23.176 13.121 1.00 24.28 C
ANISOU 5154 CA TYR C 75 3115 2868 3243 485 -157 -767 C
ATOM 5155 C TYR C 75 33.138 22.994 14.267 1.00 24.35 C
ANISOU 5155 C TYR C 75 3158 2827 3268 495 -224 -802 C
ATOM 5156 O TYR C 75 33.798 23.940 14.707 1.00 20.83 O
ANISOU 5156 O TYR C 75 2680 2386 2849 495 -200 -816 O
ATOM 5157 CB TYR C 75 32.646 22.482 11.841 1.00 22.88 C
ANISOU 5157 CB TYR C 75 2912 2709 3073 534 -179 -808 C
ATOM 5158 CG TYR C 75 34.078 22.764 11.418 1.00 27.74 C
ANISOU 5158 CG TYR C 75 3464 3336 3739 593 -167 -864 C
ATOM 5159 CD1 TYR C 75 35.145 22.054 11.963 1.00 28.27 C
ANISOU 5159 CD1 TYR C 75 3542 3359 3841 631 -245 -910 C
ATOM 5160 CD2 TYR C 75 34.357 23.705 10.435 1.00 28.49 C
ANISOU 5160 CD2 TYR C 75 3486 3485 3854 614 -77 -865 C
ATOM 5161 CE1 TYR C 75 36.449 22.298 11.565 1.00 27.06 C
ANISOU 5161 CE1 TYR C 75 3312 3218 3753 686 -230 -954 C
ATOM 5162 CE2 TYR C 75 35.654 23.953 10.030 1.00 28.14 C
ANISOU 5162 CE2 TYR C 75 3375 3449 3867 665 -54 -910 C
ATOM 5163 CZ TYR C 75 36.696 23.247 10.595 1.00 26.14 C
ANISOU 5163 CZ TYR C 75 3117 3154 3659 700 -129 -954 C
ATOM 5164 OH TYR C 75 37.987 23.498 10.186 1.00 27.13 O
ANISOU 5164 OH TYR C 75 3157 3291 3859 752 -101 -993 O
ATOM 5165 N PHE C 76 33.241 21.759 14.748 1.00 26.76 N
ANISOU 5165 N PHE C 76 3534 3079 3556 503 -316 -815 N
ATOM 5166 CA PHE C 76 34.081 21.428 15.889 1.00 25.64 C
ANISOU 5166 CA PHE C 76 3440 2885 3419 514 -401 -839 C
ATOM 5167 C PHE C 76 35.138 20.409 15.490 1.00 25.52 C
ANISOU 5167 C PHE C 76 3410 2846 3442 580 -483 -889 C
ATOM 5168 O PHE C 76 34.857 19.467 14.743 1.00 18.12 O
ANISOU 5168 O PHE C 76 2493 1897 2494 601 -497 -898 O
ATOM 5169 CB PHE C 76 33.254 20.860 17.043 1.00 25.91 C
ANISOU 5169 CB PHE C 76 3589 2861 3392 469 -437 -797 C
ATOM 5170 CG PHE C 76 32.551 21.899 17.860 1.00 27.01 C
ANISOU 5170 CG PHE C 76 3760 3004 3498 417 -365 -755 C
ATOM 5171 CD1 PHE C 76 31.278 22.324 17.522 1.00 27.85 C
ANISOU 5171 CD1 PHE C 76 3853 3140 3590 378 -269 -701 C
ATOM 5172 CD2 PHE C 76 33.162 22.449 18.978 1.00 32.82 C
ANISOU 5172 CD2 PHE C 76 4543 3710 4218 408 -395 -769 C
ATOM 5173 CE1 PHE C 76 30.625 23.281 18.285 1.00 27.92 C
ANISOU 5173 CE1 PHE C 76 3892 3144 3571 341 -186 -660 C
ATOM 5174 CE2 PHE C 76 32.515 23.406 19.744 1.00 32.34 C
ANISOU 5174 CE2 PHE C 76 4531 3641 4117 363 -318 -735 C
ATOM 5175 CZ PHE C 76 31.245 23.822 19.395 1.00 32.69 C
ANISOU 5175 CZ PHE C 76 4559 3711 4150 334 -205 -680 C
ATOM 5176 N ASN C 77 36.352 20.611 15.989 1.00 21.95 N
ANISOU 5176 N ASN C 77 2922 2382 3037 614 -537 -923 N
ATOM 5177 CA ASN C 77 37.371 19.574 16.014 1.00 18.99 C
ANISOU 5177 CA ASN C 77 2545 1968 2703 681 -632 -960 C
ATOM 5178 C ASN C 77 37.414 19.003 17.422 1.00 24.57 C
ANISOU 5178 C ASN C 77 3356 2608 3372 667 -739 -943 C
ATOM 5179 O ASN C 77 37.576 19.752 18.392 1.00 19.55 O
ANISOU 5179 O ASN C 77 2738 1968 2721 630 -761 -933 O
ATOM 5180 CB ASN C 77 38.745 20.122 15.629 1.00 24.08 C
ANISOU 5180 CB ASN C 77 3064 2645 3442 733 -629 -1001 C
ATOM 5181 CG ASN C 77 38.848 20.450 14.160 1.00 29.85 C
ANISOU 5181 CG ASN C 77 3707 3429 4206 764 -523 -1020 C
ATOM 5182 OD1 ASN C 77 38.142 19.869 13.337 1.00 29.13 O
ANISOU 5182 OD1 ASN C 77 3656 3339 4071 771 -487 -1016 O
ATOM 5183 ND2 ASN C 77 39.736 21.374 13.818 1.00 31.63 N
ANISOU 5183 ND2 ASN C 77 3818 3695 4506 780 -475 -1039 N
ATOM 5184 N LEU C 78 37.254 17.689 17.534 1.00 23.84 N
ANISOU 5184 N LEU C 78 3345 2457 3257 693 -806 -938 N
ATOM 5185 CA LEU C 78 37.257 17.004 18.820 1.00 23.87 C
ANISOU 5185 CA LEU C 78 3465 2390 3216 685 -908 -915 C
ATOM 5186 C LEU C 78 38.471 16.089 18.885 1.00 24.68 C
ANISOU 5186 C LEU C 78 3552 2450 3378 773 -1017 -945 C
ATOM 5187 O LEU C 78 38.619 15.184 18.055 1.00 25.15 O
ANISOU 5187 O LEU C 78 3602 2487 3465 828 -1016 -967 O
ATOM 5188 CB LEU C 78 35.970 16.208 19.016 1.00 22.22 C
ANISOU 5188 CB LEU C 78 3376 2134 2933 636 -892 -872 C
ATOM 5189 CG LEU C 78 34.690 17.001 18.764 1.00 27.00 C
ANISOU 5189 CG LEU C 78 3975 2785 3499 560 -776 -835 C
ATOM 5190 CD1 LEU C 78 33.495 16.085 18.851 1.00 32.64 C
ANISOU 5190 CD1 LEU C 78 4785 3453 4165 513 -767 -791 C
ATOM 5191 CD2 LEU C 78 34.562 18.150 19.752 1.00 22.16 C
ANISOU 5191 CD2 LEU C 78 3379 2186 2853 514 -745 -812 C
ATOM 5192 N PHE C 79 39.340 16.331 19.862 1.00 31.34 N
ANISOU 5192 N PHE C 79 4393 3277 4238 788 -1113 -947 N
ATOM 5193 CA PHE C 79 40.502 15.489 20.121 1.00 28.59 C
ANISOU 5193 CA PHE C 79 4026 2885 3951 874 -1235 -964 C
ATOM 5194 C PHE C 79 40.222 14.731 21.411 1.00 30.37 C
ANISOU 5194 C PHE C 79 4414 3031 4097 861 -1343 -923 C
ATOM 5195 O PHE C 79 40.311 15.302 22.502 1.00 34.58 O
ANISOU 5195 O PHE C 79 5000 3558 4582 819 -1401 -905 O
ATOM 5196 CB PHE C 79 41.775 16.328 20.218 1.00 29.02 C
ANISOU 5196 CB PHE C 79 3942 2985 4101 902 -1279 -992 C
ATOM 5197 CG PHE C 79 41.978 17.252 19.048 1.00 30.93 C
ANISOU 5197 CG PHE C 79 4036 3305 4412 900 -1155 -1024 C
ATOM 5198 CD1 PHE C 79 41.484 18.549 19.072 1.00 31.79 C
ANISOU 5198 CD1 PHE C 79 4122 3464 4492 820 -1071 -1019 C
ATOM 5199 CD2 PHE C 79 42.655 16.819 17.922 1.00 29.41 C
ANISOU 5199 CD2 PHE C 79 3738 3128 4310 983 -1112 -1055 C
ATOM 5200 CE1 PHE C 79 41.665 19.399 17.988 1.00 31.09 C
ANISOU 5200 CE1 PHE C 79 3907 3441 4464 820 -954 -1041 C
ATOM 5201 CE2 PHE C 79 42.841 17.662 16.838 1.00 30.00 C
ANISOU 5201 CE2 PHE C 79 3689 3270 4439 982 -990 -1079 C
ATOM 5202 CZ PHE C 79 42.346 18.954 16.870 1.00 24.02 C
ANISOU 5202 CZ PHE C 79 2911 2564 3653 899 -914 -1070 C
ATOM 5203 N ILE C 80 39.868 13.456 21.279 1.00 26.24 N
ANISOU 5203 N ILE C 80 3980 2439 3550 894 -1366 -909 N
ATOM 5204 CA ILE C 80 39.394 12.636 22.386 1.00 25.00 C
ANISOU 5204 CA ILE C 80 3997 2197 3307 875 -1443 -861 C
ATOM 5205 C ILE C 80 40.458 11.602 22.727 1.00 27.83 C
ANISOU 5205 C ILE C 80 4373 2489 3713 975 -1580 -862 C
ATOM 5206 O ILE C 80 41.160 11.103 21.839 1.00 29.62 O
ANISOU 5206 O ILE C 80 4507 2716 4033 1060 -1580 -897 O
ATOM 5207 CB ILE C 80 38.053 11.961 22.027 1.00 24.73 C
ANISOU 5207 CB ILE C 80 4062 2125 3211 821 -1361 -834 C
ATOM 5208 CG1 ILE C 80 37.068 13.006 21.494 1.00 22.83 C
ANISOU 5208 CG1 ILE C 80 3767 1959 2946 737 -1224 -831 C
ATOM 5209 CG2 ILE C 80 37.463 11.237 23.226 1.00 27.06 C
ANISOU 5209 CG2 ILE C 80 4539 2331 3412 787 -1417 -776 C
ATOM 5210 CD1 ILE C 80 35.810 12.428 20.896 1.00 29.71 C
ANISOU 5210 CD1 ILE C 80 4692 2812 3786 685 -1146 -810 C
ATOM 5211 N SER C 81 40.585 11.295 24.019 1.00 26.80 N
ANISOU 5211 N SER C 81 4367 2300 3518 971 -1694 -821 N
ATOM 5212 CA SER C 81 41.465 10.241 24.499 1.00 29.84 C
ANISOU 5212 CA SER C 81 4795 2609 3934 1067 -1836 -806 C
ATOM 5213 C SER C 81 40.783 9.499 25.640 1.00 28.38 C
ANISOU 5213 C SER C 81 4826 2330 3628 1033 -1894 -744 C
ATOM 5214 O SER C 81 40.061 10.093 26.444 1.00 28.07 O
ANISOU 5214 O SER C 81 4885 2297 3485 945 -1867 -713 O
ATOM 5215 CB SER C 81 42.815 10.789 24.974 1.00 34.88 C
ANISOU 5215 CB SER C 81 5325 3283 4645 1119 -1963 -820 C
ATOM 5216 OG SER C 81 42.737 11.234 26.317 1.00 42.98 O
ANISOU 5216 OG SER C 81 6466 4292 5572 1063 -2055 -786 O
ATOM 5217 N VAL C 82 41.015 8.190 25.693 1.00 29.29 N
ANISOU 5217 N VAL C 82 5020 2353 3756 1107 -1963 -723 N
ATOM 5218 CA VAL C 82 40.529 7.327 26.765 1.00 31.86 C
ANISOU 5218 CA VAL C 82 5554 2573 3976 1092 -2028 -657 C
ATOM 5219 C VAL C 82 41.747 6.699 27.420 1.00 31.76 C
ANISOU 5219 C VAL C 82 5560 2507 4001 1203 -2207 -637 C
ATOM 5220 O VAL C 82 42.492 5.959 26.763 1.00 33.56 O
ANISOU 5220 O VAL C 82 5711 2705 4334 1309 -2242 -658 O
ATOM 5221 CB VAL C 82 39.578 6.237 26.246 1.00 44.05 C
ANISOU 5221 CB VAL C 82 7199 4039 5500 1073 -1947 -641 C
ATOM 5222 CG1 VAL C 82 38.736 5.677 27.383 1.00 53.05 C
ANISOU 5222 CG1 VAL C 82 8557 5086 6513 1012 -1963 -566 C
ATOM 5223 CG2 VAL C 82 38.704 6.771 25.125 1.00 53.55 C
ANISOU 5223 CG2 VAL C 82 8312 5312 6724 999 -1788 -679 C
ATOM 5224 N ASN C 83 41.950 6.991 28.704 1.00 34.11 N
ANISOU 5224 N ASN C 83 5772 3509 3679 1101 -2213 -850 N
ATOM 5225 CA ASN C 83 43.087 6.465 29.458 1.00 35.52 C
ANISOU 5225 CA ASN C 83 5990 3675 3831 1163 -2401 -828 C
ATOM 5226 C ASN C 83 44.388 6.663 28.686 1.00 37.30 C
ANISOU 5226 C ASN C 83 5984 3924 4266 1126 -2531 -806 C
ATOM 5227 O ASN C 83 45.188 5.741 28.510 1.00 42.08 O
ANISOU 5227 O ASN C 83 6511 4543 4933 1169 -2570 -740 O
ATOM 5228 CB ASN C 83 42.867 4.994 29.808 1.00 38.16 C
ANISOU 5228 CB ASN C 83 6417 4005 4077 1240 -2311 -757 C
ATOM 5229 CG ASN C 83 41.612 4.775 30.626 1.00 44.68 C
ANISOU 5229 CG ASN C 83 7458 4798 4721 1290 -2169 -746 C
ATOM 5230 OD1 ASN C 83 41.299 5.561 31.518 1.00 46.66 O
ANISOU 5230 OD1 ASN C 83 7873 5022 4833 1322 -2216 -791 O
ATOM 5231 ND2 ASN C 83 40.882 3.709 30.323 1.00 43.28 N
ANISOU 5231 ND2 ASN C 83 7282 4611 4550 1304 -1991 -680 N
ATOM 5232 N SER C 84 44.577 7.889 28.197 1.00 37.35 N
ANISOU 5232 N SER C 84 5869 3928 4392 1054 -2583 -847 N
ATOM 5233 CA SER C 84 45.722 8.342 27.412 1.00 44.70 C
ANISOU 5233 CA SER C 84 6556 4873 5556 1016 -2685 -809 C
ATOM 5234 C SER C 84 45.819 7.679 26.040 1.00 43.89 C
ANISOU 5234 C SER C 84 6272 4823 5583 1027 -2514 -735 C
ATOM 5235 O SER C 84 46.812 7.899 25.336 1.00 49.59 O
ANISOU 5235 O SER C 84 6785 5557 6498 1025 -2563 -671 O
ATOM 5236 CB SER C 84 47.052 8.142 28.154 1.00 46.48 C
ANISOU 5236 CB SER C 84 6756 5068 5838 1050 -2937 -775 C
ATOM 5237 OG SER C 84 47.013 8.791 29.413 1.00 55.31 O
ANISOU 5237 OG SER C 84 8058 6123 6836 1044 -3079 -849 O
ATOM 5238 N ILE C 85 44.835 6.884 25.631 1.00 33.28 N
ANISOU 5238 N ILE C 85 5002 3500 4145 1048 -2320 -733 N
ATOM 5239 CA ILE C 85 44.815 6.303 24.292 1.00 32.95 C
ANISOU 5239 CA ILE C 85 4826 3494 4198 1069 -2169 -685 C
ATOM 5240 C ILE C 85 44.000 7.224 23.392 1.00 33.09 C
ANISOU 5240 C ILE C 85 4778 3533 4259 1011 -2045 -725 C
ATOM 5241 O ILE C 85 42.805 7.438 23.628 1.00 30.45 O
ANISOU 5241 O ILE C 85 4563 3189 3818 974 -1958 -778 O
ATOM 5242 CB ILE C 85 44.235 4.880 24.302 1.00 36.23 C
ANISOU 5242 CB ILE C 85 5358 3900 4509 1122 -2059 -665 C
ATOM 5243 CG1 ILE C 85 45.124 3.930 25.109 1.00 33.14 C
ANISOU 5243 CG1 ILE C 85 5017 3491 4084 1191 -2171 -611 C
ATOM 5244 CG2 ILE C 85 44.064 4.361 22.882 1.00 31.02 C
ANISOU 5244 CG2 ILE C 85 4599 3261 3926 1149 -1916 -640 C
ATOM 5245 CD1 ILE C 85 44.609 2.504 25.147 1.00 39.28 C
ANISOU 5245 CD1 ILE C 85 5903 4245 4776 1245 -2065 -583 C
ATOM 5246 N GLU C 86 44.642 7.762 22.358 1.00 30.94 N
ANISOU 5246 N GLU C 86 4314 3291 4152 1013 -2026 -685 N
ATOM 5247 CA GLU C 86 44.031 8.783 21.518 1.00 30.02 C
ANISOU 5247 CA GLU C 86 4119 3197 4092 966 -1925 -714 C
ATOM 5248 C GLU C 86 43.267 8.172 20.351 1.00 29.85 C
ANISOU 5248 C GLU C 86 4094 3206 4043 1002 -1746 -711 C
ATOM 5249 O GLU C 86 43.748 7.253 19.681 1.00 29.02 O
ANISOU 5249 O GLU C 86 3948 3111 3966 1082 -1704 -659 O
ATOM 5250 CB GLU C 86 45.091 9.754 20.988 1.00 37.36 C
ANISOU 5250 CB GLU C 86 4837 4134 5223 960 -1986 -657 C
ATOM 5251 CG GLU C 86 45.515 10.826 21.989 1.00 54.76 C
ANISOU 5251 CG GLU C 86 7041 6290 7477 889 -2171 -692 C
ATOM 5252 CD GLU C 86 45.717 12.185 21.341 1.00 70.67 C
ANISOU 5252 CD GLU C 86 8887 8301 9665 840 -2161 -677 C
ATOM 5253 OE1 GLU C 86 46.864 12.513 20.976 1.00 75.77 O
ANISOU 5253 OE1 GLU C 86 9333 8934 10521 854 -2232 -586 O
ATOM 5254 OE2 GLU C 86 44.724 12.928 21.189 1.00 73.28 O
ANISOU 5254 OE2 GLU C 86 9273 8636 9934 790 -2073 -743 O
ATOM 5255 N LEU C 87 42.088 8.695 20.115 1.00 28.00 N
ANISOU 5255 N LEU C 87 3908 2977 3752 949 -1652 -767 N
ATOM 5256 CA LEU C 87 41.204 8.494 18.982 1.00 30.44 C
ANISOU 5256 CA LEU C 87 4207 3309 4050 962 -1509 -782 C
ATOM 5257 C LEU C 87 41.586 9.454 17.861 1.00 29.49 C
ANISOU 5257 C LEU C 87 3922 3233 4051 981 -1454 -754 C
ATOM 5258 O LEU C 87 42.137 10.527 18.120 1.00 30.96 O
ANISOU 5258 O LEU C 87 4013 3420 4328 943 -1512 -740 O
ATOM 5259 CB LEU C 87 39.751 8.739 19.385 1.00 31.79 C
ANISOU 5259 CB LEU C 87 4493 3461 4125 891 -1445 -839 C
ATOM 5260 CG LEU C 87 39.007 7.797 20.334 1.00 36.72 C
ANISOU 5260 CG LEU C 87 5282 4036 4635 880 -1442 -847 C
ATOM 5261 CD1 LEU C 87 39.505 7.905 21.768 1.00 36.97 C
ANISOU 5261 CD1 LEU C 87 5407 4041 4600 878 -1551 -846 C
ATOM 5262 CD2 LEU C 87 37.524 8.102 20.269 1.00 34.96 C
ANISOU 5262 CD2 LEU C 87 5112 3799 4372 823 -1336 -872 C
ATOM 5263 N PRO C 88 41.316 9.110 16.605 1.00 26.29 N
ANISOU 5263 N PRO C 88 3482 2854 3652 1046 -1348 -743 N
ATOM 5264 CA PRO C 88 41.559 10.071 15.525 1.00 29.63 C
ANISOU 5264 CA PRO C 88 3763 3322 4173 1081 -1270 -707 C
ATOM 5265 C PRO C 88 40.703 11.313 15.710 1.00 28.07 C
ANISOU 5265 C PRO C 88 3554 3132 3977 983 -1243 -756 C
ATOM 5266 O PRO C 88 39.606 11.258 16.271 1.00 24.98 O
ANISOU 5266 O PRO C 88 3280 2720 3489 911 -1235 -818 O
ATOM 5267 CB PRO C 88 41.152 9.302 14.262 1.00 27.79 C
ANISOU 5267 CB PRO C 88 3567 3106 3886 1181 -1171 -710 C
ATOM 5268 CG PRO C 88 41.162 7.862 14.665 1.00 30.55 C
ANISOU 5268 CG PRO C 88 4041 3410 4155 1212 -1218 -725 C
ATOM 5269 CD PRO C 88 40.779 7.836 16.104 1.00 32.49 C
ANISOU 5269 CD PRO C 88 4370 3620 4354 1101 -1301 -762 C
ATOM 5270 N LYS C 89 41.221 12.446 15.237 1.00 25.64 N
ANISOU 5270 N LYS C 89 3098 2849 3794 986 -1218 -712 N
ATOM 5271 CA LYS C 89 40.436 13.671 15.239 1.00 25.08 C
ANISOU 5271 CA LYS C 89 3008 2786 3735 908 -1173 -751 C
ATOM 5272 C LYS C 89 39.111 13.434 14.529 1.00 24.14 C
ANISOU 5272 C LYS C 89 2965 2692 3514 912 -1064 -797 C
ATOM 5273 O LYS C 89 39.059 12.787 13.480 1.00 25.94 O
ANISOU 5273 O LYS C 89 3190 2947 3719 1004 -1001 -780 O
ATOM 5274 CB LYS C 89 41.205 14.803 14.548 1.00 27.69 C
ANISOU 5274 CB LYS C 89 3149 3137 4236 934 -1135 -678 C
ATOM 5275 CG LYS C 89 40.433 16.117 14.492 1.00 34.25 C
ANISOU 5275 CG LYS C 89 3953 3971 5089 859 -1082 -712 C
ATOM 5276 CD LYS C 89 41.087 17.145 13.576 1.00 33.59 C
ANISOU 5276 CD LYS C 89 3672 3908 5180 904 -1009 -624 C
ATOM 5277 CE LYS C 89 40.735 16.898 12.118 1.00 40.44 C
ANISOU 5277 CE LYS C 89 4508 4844 6013 1023 -849 -583 C
ATOM 5278 NZ LYS C 89 41.367 17.905 11.224 1.00 44.63 N
ANISOU 5278 NZ LYS C 89 4849 5397 6712 1087 -752 -476 N
ATOM 5279 N ARG C 90 38.029 13.930 15.121 1.00 26.11 N
ANISOU 5279 N ARG C 90 3292 2926 3702 821 -1050 -853 N
ATOM 5280 CA ARG C 90 36.740 13.908 14.454 1.00 33.79 C
ANISOU 5280 CA ARG C 90 4305 3919 4617 811 -955 -882 C
ATOM 5281 C ARG C 90 36.236 15.332 14.278 1.00 22.49 C
ANISOU 5281 C ARG C 90 2806 2510 3231 761 -886 -886 C
ATOM 5282 O ARG C 90 36.469 16.206 15.118 1.00 28.27 O
ANISOU 5282 O ARG C 90 3532 3215 3994 701 -925 -895 O
ATOM 5283 CB ARG C 90 35.709 13.039 15.204 1.00 33.89 C
ANISOU 5283 CB ARG C 90 4463 3886 4528 760 -970 -919 C
ATOM 5284 CG ARG C 90 35.396 13.425 16.648 1.00 32.91 C
ANISOU 5284 CG ARG C 90 4429 3719 4356 684 -1003 -936 C
ATOM 5285 CD ARG C 90 34.467 12.382 17.256 1.00 37.01 C
ANISOU 5285 CD ARG C 90 5076 4192 4795 664 -992 -939 C
ATOM 5286 NE ARG C 90 33.263 12.192 16.445 1.00 30.25 N
ANISOU 5286 NE ARG C 90 4205 3338 3949 648 -913 -937 N
ATOM 5287 CZ ARG C 90 32.730 11.007 16.154 1.00 38.58 C
ANISOU 5287 CZ ARG C 90 5304 4356 4998 658 -923 -933 C
ATOM 5288 NH1 ARG C 90 33.302 9.895 16.592 1.00 38.33 N
ANISOU 5288 NH1 ARG C 90 5337 4286 4940 691 -988 -927 N
ATOM 5289 NH2 ARG C 90 31.628 10.926 15.417 1.00 37.70 N
ANISOU 5289 NH2 ARG C 90 5170 4236 4918 636 -879 -932 N
ATOM 5290 N LYS C 91 35.568 15.554 13.154 1.00 22.00 N
ANISOU 5290 N LYS C 91 2702 2490 3168 796 -794 -881 N
ATOM 5291 CA LYS C 91 35.031 16.853 12.778 1.00 22.34 C
ANISOU 5291 CA LYS C 91 2672 2561 3254 765 -709 -875 C
ATOM 5292 C LYS C 91 33.514 16.758 12.815 1.00 24.89 C
ANISOU 5292 C LYS C 91 3072 2879 3506 711 -660 -907 C
ATOM 5293 O LYS C 91 32.932 15.884 12.165 1.00 20.97 O
ANISOU 5293 O LYS C 91 2614 2387 2966 746 -659 -918 O
ATOM 5294 CB LYS C 91 35.521 17.255 11.388 1.00 21.66 C
ANISOU 5294 CB LYS C 91 2464 2534 3234 869 -633 -824 C
ATOM 5295 CG LYS C 91 34.965 18.569 10.872 1.00 28.15 C
ANISOU 5295 CG LYS C 91 3203 3390 4103 852 -533 -807 C
ATOM 5296 CD LYS C 91 35.359 18.759 9.417 1.00 27.81 C
ANISOU 5296 CD LYS C 91 3064 3407 4095 986 -444 -747 C
ATOM 5297 CE LYS C 91 34.896 20.096 8.873 1.00 29.18 C
ANISOU 5297 CE LYS C 91 3144 3616 4326 981 -336 -717 C
ATOM 5298 NZ LYS C 91 35.548 20.418 7.573 1.00 30.69 N
ANISOU 5298 NZ LYS C 91 3228 3862 4571 1131 -236 -632 N
ATOM 5299 N GLU C 92 32.882 17.636 13.591 1.00 22.29 N
ANISOU 5299 N GLU C 92 2767 2529 3172 632 -626 -916 N
ATOM 5300 CA GLU C 92 31.431 17.660 13.738 1.00 21.83 C
ANISOU 5300 CA GLU C 92 2764 2460 3070 581 -562 -920 C
ATOM 5301 C GLU C 92 30.930 19.016 13.262 1.00 20.86 C
ANISOU 5301 C GLU C 92 2561 2372 2992 566 -463 -904 C
ATOM 5302 O GLU C 92 31.171 20.038 13.914 1.00 25.06 O
ANISOU 5302 O GLU C 92 3091 2884 3547 531 -448 -907 O
ATOM 5303 CB GLU C 92 31.017 17.390 15.185 1.00 25.00 C
ANISOU 5303 CB GLU C 92 3293 2798 3409 525 -582 -926 C
ATOM 5304 CG GLU C 92 31.507 16.052 15.716 1.00 33.80 C
ANISOU 5304 CG GLU C 92 4487 3875 4479 544 -673 -934 C
ATOM 5305 CD GLU C 92 30.960 14.873 14.931 1.00 40.91 C
ANISOU 5305 CD GLU C 92 5389 4773 5383 566 -681 -928 C
ATOM 5306 OE1 GLU C 92 29.877 15.003 14.323 1.00 40.23 O
ANISOU 5306 OE1 GLU C 92 5271 4694 5320 546 -624 -914 O
ATOM 5307 OE2 GLU C 92 31.616 13.809 14.923 1.00 45.04 O
ANISOU 5307 OE2 GLU C 92 5946 5277 5890 605 -757 -937 O
ATOM 5308 N VAL C 93 30.258 19.024 12.118 1.00 21.75 N
ANISOU 5308 N VAL C 93 2617 2531 3118 599 -408 -889 N
ATOM 5309 CA VAL C 93 29.694 20.249 11.565 1.00 20.80 C
ANISOU 5309 CA VAL C 93 2417 2450 3037 594 -306 -865 C
ATOM 5310 C VAL C 93 28.348 20.508 12.224 1.00 26.79 C
ANISOU 5310 C VAL C 93 3227 3179 3774 521 -244 -850 C
ATOM 5311 O VAL C 93 27.495 19.616 12.289 1.00 25.21 O
ANISOU 5311 O VAL C 93 3073 2954 3552 500 -263 -841 O
ATOM 5312 CB VAL C 93 29.555 20.141 10.038 1.00 23.07 C
ANISOU 5312 CB VAL C 93 2632 2801 3333 680 -279 -851 C
ATOM 5313 CG1 VAL C 93 28.995 21.429 9.453 1.00 22.67 C
ANISOU 5313 CG1 VAL C 93 2495 2796 3323 684 -167 -818 C
ATOM 5314 CG2 VAL C 93 30.888 19.805 9.407 1.00 19.79 C
ANISOU 5314 CG2 VAL C 93 2176 2410 2932 780 -314 -844 C
ATOM 5315 N LEU C 94 28.161 21.726 12.727 1.00 26.14 N
ANISOU 5315 N LEU C 94 3136 3087 3709 487 -169 -838 N
ATOM 5316 CA LEU C 94 26.892 22.161 13.299 1.00 24.06 C
ANISOU 5316 CA LEU C 94 2917 2798 3429 440 -76 -805 C
ATOM 5317 C LEU C 94 26.110 23.075 12.367 1.00 29.97 C
ANISOU 5317 C LEU C 94 3564 3598 4226 449 29 -766 C
ATOM 5318 O LEU C 94 24.880 22.984 12.310 1.00 33.20 O
ANISOU 5318 O LEU C 94 3968 4005 4643 425 89 -719 O
ATOM 5319 CB LEU C 94 27.121 22.879 14.634 1.00 23.47 C
ANISOU 5319 CB LEU C 94 2943 2661 3313 412 -59 -820 C
ATOM 5320 CG LEU C 94 27.119 22.032 15.907 1.00 32.22 C
ANISOU 5320 CG LEU C 94 4200 3703 4338 402 -111 -829 C
ATOM 5321 CD1 LEU C 94 27.391 22.889 17.129 1.00 35.92 C
ANISOU 5321 CD1 LEU C 94 4793 4109 4746 400 -107 -857 C
ATOM 5322 CD2 LEU C 94 25.791 21.306 16.050 1.00 36.19 C
ANISOU 5322 CD2 LEU C 94 4730 4190 4832 388 -39 -762 C
ATOM 5323 N CYS C 95 26.797 23.954 11.639 1.00 21.26 N
ANISOU 5323 N CYS C 95 2369 2538 3169 486 55 -770 N
ATOM 5324 CA CYS C 95 26.175 24.846 10.667 1.00 21.33 C
ANISOU 5324 CA CYS C 95 2278 2604 3222 511 156 -729 C
ATOM 5325 C CYS C 95 26.846 24.632 9.318 1.00 19.29 C
ANISOU 5325 C CYS C 95 1932 2412 2984 600 129 -728 C
ATOM 5326 O CYS C 95 28.050 24.874 9.173 1.00 20.92 O
ANISOU 5326 O CYS C 95 2097 2623 3228 640 109 -733 O
ATOM 5327 CB CYS C 95 26.290 26.310 11.101 1.00 32.09 C
ANISOU 5327 CB CYS C 95 3621 3946 4627 490 248 -717 C
ATOM 5328 SG CYS C 95 25.655 26.664 12.761 1.00 36.95 S
ANISOU 5328 SG CYS C 95 4385 4469 5184 425 288 -723 S
ATOM 5329 N HIS C 96 26.070 24.180 8.336 1.00 26.52 N
ANISOU 5329 N HIS C 96 2823 3373 3879 641 126 -713 N
ATOM 5330 CA HIS C 96 26.584 23.890 7.004 1.00 23.29 C
ANISOU 5330 CA HIS C 96 2370 3025 3454 757 101 -714 C
ATOM 5331 C HIS C 96 26.592 25.105 6.084 1.00 27.74 C
ANISOU 5331 C HIS C 96 2830 3653 4055 827 219 -662 C
ATOM 5332 O HIS C 96 27.224 25.056 5.023 1.00 30.01 O
ANISOU 5332 O HIS C 96 3081 3992 4329 951 230 -645 O
ATOM 5333 CB HIS C 96 25.761 22.766 6.365 1.00 20.47 C
ANISOU 5333 CB HIS C 96 2063 2670 3045 781 7 -737 C
ATOM 5334 CG HIS C 96 25.770 21.489 7.150 1.00 24.31 C
ANISOU 5334 CG HIS C 96 2642 3086 3508 723 -106 -777 C
ATOM 5335 ND1 HIS C 96 24.976 21.289 8.260 1.00 34.30 N
ANISOU 5335 ND1 HIS C 96 3946 4290 4797 613 -103 -763 N
ATOM 5336 CD2 HIS C 96 26.484 20.349 6.989 1.00 19.43 C
ANISOU 5336 CD2 HIS C 96 2090 2447 2847 772 -211 -821 C
ATOM 5337 CE1 HIS C 96 25.196 20.078 8.742 1.00 30.08 C
ANISOU 5337 CE1 HIS C 96 3489 3699 4240 593 -204 -794 C
ATOM 5338 NE2 HIS C 96 26.107 19.488 7.990 1.00 29.23 N
ANISOU 5338 NE2 HIS C 96 3400 3614 4092 683 -276 -835 N
ATOM 5339 N GLY C 97 25.915 26.189 6.461 1.00 26.32 N
ANISOU 5339 N GLY C 97 2609 3469 3920 767 319 -628 N
ATOM 5340 CA GLY C 97 25.840 27.385 5.649 1.00 27.47 C
ANISOU 5340 CA GLY C 97 2657 3671 4110 827 442 -570 C
ATOM 5341 C GLY C 97 24.591 27.512 4.805 1.00 34.55 C
ANISOU 5341 C GLY C 97 3544 4616 4967 847 471 -523 C
ATOM 5342 O GLY C 97 24.489 28.465 4.022 1.00 39.19 O
ANISOU 5342 O GLY C 97 4117 5238 5535 873 557 -408 O
ATOM 5343 N HIS C 98 23.637 26.592 4.946 1.00 31.39 N
ANISOU 5343 N HIS C 98 3183 4200 4543 812 385 -563 N
ATOM 5344 CA HIS C 98 22.449 26.581 4.097 1.00 28.92 C
ANISOU 5344 CA HIS C 98 2838 3927 4222 839 374 -532 C
ATOM 5345 C HIS C 98 21.316 25.912 4.862 1.00 21.65 C
ANISOU 5345 C HIS C 98 1950 2944 3333 726 313 -525 C
ATOM 5346 O HIS C 98 21.384 24.711 5.138 1.00 29.12 O
ANISOU 5346 O HIS C 98 2964 3839 4259 698 185 -569 O
ATOM 5347 CB HIS C 98 22.731 25.860 2.783 1.00 28.65 C
ANISOU 5347 CB HIS C 98 2833 3940 4111 974 273 -565 C
ATOM 5348 CG HIS C 98 21.500 25.488 2.019 1.00 35.21 C
ANISOU 5348 CG HIS C 98 3665 4785 4928 990 184 -560 C
ATOM 5349 ND1 HIS C 98 20.743 26.412 1.333 1.00 34.76 N
ANISOU 5349 ND1 HIS C 98 3532 4787 4888 1030 261 -500 N
ATOM 5350 CD2 HIS C 98 20.894 24.291 1.835 1.00 38.40 C
ANISOU 5350 CD2 HIS C 98 4131 5140 5318 968 7 -605 C
ATOM 5351 CE1 HIS C 98 19.722 25.799 0.760 1.00 39.03 C
ANISOU 5351 CE1 HIS C 98 4086 5318 5426 1032 124 -509 C
ATOM 5352 NE2 HIS C 98 19.791 24.511 1.048 1.00 39.60 N
ANISOU 5352 NE2 HIS C 98 4241 5318 5486 991 -36 -574 N
ATOM 5353 N ASP C 99 20.284 26.687 5.198 1.00 22.40 N
ANISOU 5353 N ASP C 99 1988 3035 3486 669 415 -454 N
ATOM 5354 CA ASP C 99 19.073 26.176 5.847 1.00 26.81 C
ANISOU 5354 CA ASP C 99 2548 3534 4105 575 391 -406 C
ATOM 5355 C ASP C 99 19.404 25.323 7.072 1.00 25.94 C
ANISOU 5355 C ASP C 99 2529 3341 3986 505 347 -434 C
ATOM 5356 O ASP C 99 18.924 24.199 7.230 1.00 25.31 O
ANISOU 5356 O ASP C 99 2472 3207 3936 464 236 -432 O
ATOM 5357 CB ASP C 99 18.216 25.386 4.856 1.00 28.35 C
ANISOU 5357 CB ASP C 99 2709 3736 4328 595 247 -400 C
ATOM 5358 CG ASP C 99 17.541 26.270 3.825 1.00 30.96 C
ANISOU 5358 CG ASP C 99 2948 4140 4676 654 297 -347 C
ATOM 5359 OD1 ASP C 99 17.587 27.513 3.965 1.00 27.92 O
ANISOU 5359 OD1 ASP C 99 2514 3795 4299 668 467 -298 O
ATOM 5360 OD2 ASP C 99 16.963 25.713 2.869 1.00 31.23 O
ANISOU 5360 OD2 ASP C 99 2965 4183 4716 691 154 -357 O
ATOM 5361 N ASP C 100 20.220 25.879 7.960 1.00 21.76 N
ANISOU 5361 N ASP C 100 2052 2793 3423 493 427 -456 N
ATOM 5362 CA ASP C 100 20.705 25.110 9.092 1.00 20.99 C
ANISOU 5362 CA ASP C 100 2057 2624 3294 448 377 -491 C
ATOM 5363 C ASP C 100 19.636 24.976 10.175 1.00 21.04 C
ANISOU 5363 C ASP C 100 2096 2562 3336 383 450 -411 C
ATOM 5364 O ASP C 100 18.694 25.769 10.272 1.00 19.66 O
ANISOU 5364 O ASP C 100 1871 2390 3207 372 575 -328 O
ATOM 5365 CB ASP C 100 21.970 25.741 9.664 1.00 22.28 C
ANISOU 5365 CB ASP C 100 2272 2781 3414 462 406 -545 C
ATOM 5366 CG ASP C 100 23.204 25.401 8.849 1.00 27.68 C
ANISOU 5366 CG ASP C 100 2936 3507 4075 528 315 -607 C
ATOM 5367 OD1 ASP C 100 23.469 24.197 8.647 1.00 28.18 O
ANISOU 5367 OD1 ASP C 100 3039 3559 4110 541 195 -645 O
ATOM 5368 OD2 ASP C 100 23.902 26.333 8.397 1.00 26.98 O
ANISOU 5368 OD2 ASP C 100 2791 3456 4006 574 371 -608 O
ATOM 5369 N ASP C 101 19.808 23.947 11.005 1.00 19.76 N
ANISOU 5369 N ASP C 101 2019 2335 3155 353 384 -425 N
ATOM 5370 CA ASP C 101 18.797 23.562 11.979 1.00 20.43 C
ANISOU 5370 CA ASP C 101 2133 2346 3282 310 452 -329 C
ATOM 5371 C ASP C 101 18.745 24.475 13.192 1.00 20.90 C
ANISOU 5371 C ASP C 101 2285 2371 3286 322 609 -292 C
ATOM 5372 O ASP C 101 17.738 24.467 13.908 1.00 21.29 O
ANISOU 5372 O ASP C 101 2348 2369 3372 314 723 -179 O
ATOM 5373 CB ASP C 101 19.051 22.131 12.449 1.00 21.62 C
ANISOU 5373 CB ASP C 101 2348 2435 3429 288 336 -349 C
ATOM 5374 CG ASP C 101 18.994 21.136 11.321 1.00 25.62 C
ANISOU 5374 CG ASP C 101 2791 2951 3991 283 169 -387 C
ATOM 5375 OD1 ASP C 101 18.380 21.456 10.283 1.00 26.40 O
ANISOU 5375 OD1 ASP C 101 2791 3091 4150 289 149 -367 O
ATOM 5376 OD2 ASP C 101 19.552 20.034 11.476 1.00 23.42 O
ANISOU 5376 OD2 ASP C 101 2573 2633 3691 280 52 -438 O
ATOM 5377 N TYR C 102 19.791 25.255 13.442 1.00 23.09 N
ANISOU 5377 N TYR C 102 2629 2663 3482 348 616 -376 N
ATOM 5378 CA TYR C 102 19.937 25.961 14.705 1.00 24.21 C
ANISOU 5378 CA TYR C 102 2907 2747 3544 367 714 -374 C
ATOM 5379 C TYR C 102 19.905 27.469 14.494 1.00 22.76 C
ANISOU 5379 C TYR C 102 2699 2584 3363 388 823 -374 C
ATOM 5380 O TYR C 102 20.487 27.992 13.537 1.00 19.87 O
ANISOU 5380 O TYR C 102 2240 2277 3033 391 785 -423 O
ATOM 5381 CB TYR C 102 21.236 25.560 15.401 1.00 20.85 C
ANISOU 5381 CB TYR C 102 2604 2288 3030 375 595 -477 C
ATOM 5382 CG TYR C 102 21.336 24.082 15.710 1.00 28.60 C
ANISOU 5382 CG TYR C 102 3625 3241 4000 362 495 -476 C
ATOM 5383 CD1 TYR C 102 20.585 23.510 16.730 1.00 28.81 C
ANISOU 5383 CD1 TYR C 102 3742 3201 4002 372 566 -392 C
ATOM 5384 CD2 TYR C 102 22.188 23.261 14.989 1.00 22.83 C
ANISOU 5384 CD2 TYR C 102 2845 2544 3285 353 344 -547 C
ATOM 5385 CE1 TYR C 102 20.677 22.159 17.015 1.00 32.05 C
ANISOU 5385 CE1 TYR C 102 4182 3578 4418 361 482 -382 C
ATOM 5386 CE2 TYR C 102 22.288 21.912 15.265 1.00 23.82 C
ANISOU 5386 CE2 TYR C 102 3011 2635 3404 344 253 -548 C
ATOM 5387 CZ TYR C 102 21.532 21.366 16.279 1.00 30.20 C
ANISOU 5387 CZ TYR C 102 3899 3375 4200 342 319 -467 C
ATOM 5388 OH TYR C 102 21.633 20.020 16.554 1.00 37.76 O
ANISOU 5388 OH TYR C 102 4891 4291 5166 333 234 -458 O
ATOM 5389 N SER C 103 19.235 28.163 15.415 1.00 20.33 N
ANISOU 5389 N SER C 103 2594 2389 2742 -401 369 -1 N
ATOM 5390 CA SER C 103 19.056 29.603 15.283 1.00 20.93 C
ANISOU 5390 CA SER C 103 2554 2497 2902 -398 549 68 C
ATOM 5391 C SER C 103 20.361 30.374 15.437 1.00 18.31 C
ANISOU 5391 C SER C 103 2214 2184 2559 -344 586 -53 C
ATOM 5392 O SER C 103 20.457 31.502 14.943 1.00 21.12 O
ANISOU 5392 O SER C 103 2452 2590 2983 -327 709 -16 O
ATOM 5393 CB SER C 103 18.037 30.097 16.311 1.00 18.44 C
ANISOU 5393 CB SER C 103 2264 2091 2651 -445 708 183 C
ATOM 5394 OG SER C 103 18.519 29.911 17.630 1.00 19.39 O
ANISOU 5394 OG SER C 103 2547 2112 2706 -437 713 96 O
ATOM 5395 N PHE C 104 21.368 29.798 16.097 1.00 20.33 N
ANISOU 5395 N PHE C 104 2583 2397 2745 -316 480 -188 N
ATOM 5396 CA PHE C 104 22.623 30.511 16.298 1.00 20.03 C
ANISOU 5396 CA PHE C 104 2524 2363 2723 -274 494 -292 C
ATOM 5397 C PHE C 104 23.540 30.490 15.082 1.00 17.21 C
ANISOU 5397 C PHE C 104 2058 2100 2381 -208 442 -342 C
ATOM 5398 O PHE C 104 24.532 31.226 15.070 1.00 24.88 O
ANISOU 5398 O PHE C 104 2966 3080 3406 -173 476 -401 O
ATOM 5399 CB PHE C 104 23.377 29.954 17.508 1.00 18.90 C
ANISOU 5399 CB PHE C 104 2537 2131 2513 -270 387 -405 C
ATOM 5400 CG PHE C 104 23.587 28.460 17.480 1.00 25.47 C
ANISOU 5400 CG PHE C 104 3460 2955 3261 -251 214 -458 C
ATOM 5401 CD1 PHE C 104 24.630 27.892 16.760 1.00 21.76 C
ANISOU 5401 CD1 PHE C 104 2953 2537 2776 -189 98 -540 C
ATOM 5402 CD2 PHE C 104 22.766 27.627 18.220 1.00 28.38 C
ANISOU 5402 CD2 PHE C 104 3959 3251 3572 -290 182 -420 C
ATOM 5403 CE1 PHE C 104 24.829 26.511 16.763 1.00 24.51 C
ANISOU 5403 CE1 PHE C 104 3399 2866 3047 -168 -51 -589 C
ATOM 5404 CE2 PHE C 104 22.960 26.253 18.230 1.00 24.32 C
ANISOU 5404 CE2 PHE C 104 3535 2719 2987 -274 27 -468 C
ATOM 5405 CZ PHE C 104 23.993 25.694 17.501 1.00 24.33 C
ANISOU 5405 CZ PHE C 104 3505 2772 2966 -214 -92 -556 C
ATOM 5406 N CYS C 105 23.248 29.673 14.067 1.00 22.86 N
ANISOU 5406 N CYS C 105 2760 2874 3053 -188 362 -316 N
ATOM 5407 CA CYS C 105 24.025 29.733 12.833 1.00 27.84 C
ANISOU 5407 CA CYS C 105 3305 3586 3686 -111 349 -345 C
ATOM 5408 C CYS C 105 23.935 31.107 12.178 1.00 27.93 C
ANISOU 5408 C CYS C 105 3167 3658 3788 -96 513 -272 C
ATOM 5409 O CYS C 105 24.818 31.485 11.400 1.00 26.71 O
ANISOU 5409 O CYS C 105 2931 3554 3664 -22 548 -301 O
ATOM 5410 CB CYS C 105 23.555 28.655 11.859 1.00 27.46 C
ANISOU 5410 CB CYS C 105 3305 3574 3553 -98 239 -323 C
ATOM 5411 SG CYS C 105 23.666 26.964 12.477 1.00 35.81 S
ANISOU 5411 SG CYS C 105 4539 4558 4509 -109 49 -405 S
ATOM 5412 N ARG C 106 22.882 31.864 12.477 1.00 25.35 N
ANISOU 5412 N ARG C 106 2799 3321 3513 -158 629 -168 N
ATOM 5413 CA ARG C 106 22.737 33.219 11.964 1.00 23.02 C
ANISOU 5413 CA ARG C 106 2363 3072 3311 -147 799 -90 C
ATOM 5414 C ARG C 106 23.615 34.228 12.701 1.00 17.02 C
ANISOU 5414 C ARG C 106 1572 2265 2630 -140 891 -154 C
ATOM 5415 O ARG C 106 23.879 35.312 12.167 1.00 16.92 O
ANISOU 5415 O ARG C 106 1436 2291 2704 -111 1021 -118 O
ATOM 5416 CB ARG C 106 21.266 33.636 12.060 1.00 28.22 C
ANISOU 5416 CB ARG C 106 2987 3724 4010 -213 896 58 C
ATOM 5417 CG ARG C 106 20.949 34.985 11.456 1.00 50.19 C
ANISOU 5417 CG ARG C 106 5648 6558 6863 -194 1031 156 C
ATOM 5418 CD ARG C 106 19.767 35.647 12.142 1.00 56.32 C
ANISOU 5418 CD ARG C 106 6475 7287 7637 -236 1040 247 C
ATOM 5419 NE ARG C 106 19.977 35.810 13.578 1.00 50.00 N
ANISOU 5419 NE ARG C 106 5767 6376 6852 -261 1097 195 N
ATOM 5420 CZ ARG C 106 20.794 36.706 14.127 1.00 39.08 C
ANISOU 5420 CZ ARG C 106 4411 4948 5488 -239 1134 124 C
ATOM 5421 NH1 ARG C 106 20.903 36.775 15.447 1.00 34.73 N
ANISOU 5421 NH1 ARG C 106 3965 4284 4948 -274 1204 74 N
ATOM 5422 NH2 ARG C 106 21.508 37.527 13.367 1.00 29.07 N
ANISOU 5422 NH2 ARG C 106 3077 3739 4227 -189 1108 104 N
ATOM 5423 N ALA C 107 24.081 33.891 13.902 1.00 22.07 N
ANISOU 5423 N ALA C 107 2326 2816 3243 -166 818 -247 N
ATOM 5424 CA ALA C 107 24.751 34.867 14.752 1.00 21.64 C
ANISOU 5424 CA ALA C 107 2271 2693 3257 -181 883 -304 C
ATOM 5425 C ALA C 107 26.041 35.372 14.117 1.00 19.97 C
ANISOU 5425 C ALA C 107 1935 2520 3134 -120 886 -361 C
ATOM 5426 O ALA C 107 26.767 34.623 13.458 1.00 23.06 O
ANISOU 5426 O ALA C 107 2301 2956 3504 -58 788 -405 O
ATOM 5427 CB ALA C 107 25.047 34.256 16.117 1.00 20.08 C
ANISOU 5427 CB ALA C 107 2247 2392 2990 -215 765 -397 C
ATOM 5428 N LEU C 108 26.322 36.655 14.327 1.00 18.82 N
ANISOU 5428 N LEU C 108 1713 2344 3095 -134 1010 -353 N
ATOM 5429 CA LEU C 108 27.503 37.313 13.793 1.00 17.91 C
ANISOU 5429 CA LEU C 108 1458 2247 3101 -85 1038 -388 C
ATOM 5430 C LEU C 108 28.556 37.479 14.880 1.00 18.52 C
ANISOU 5430 C LEU C 108 1585 2221 3229 -115 933 -502 C
ATOM 5431 O LEU C 108 28.277 37.356 16.076 1.00 19.17 O
ANISOU 5431 O LEU C 108 1825 2214 3245 -177 872 -548 O
ATOM 5432 CB LEU C 108 27.157 38.688 13.214 1.00 19.26 C
ANISOU 5432 CB LEU C 108 1625 2439 3254 -72 1074 -257 C
ATOM 5433 CG LEU C 108 26.063 38.772 12.155 1.00 17.48 C
ANISOU 5433 CG LEU C 108 1417 2312 2913 -43 1058 -126 C
ATOM 5434 CD1 LEU C 108 25.963 40.199 11.656 1.00 20.02 C
ANISOU 5434 CD1 LEU C 108 1728 2654 3223 -30 1065 -54 C
ATOM 5435 CD2 LEU C 108 26.347 37.817 11.010 1.00 17.43 C
ANISOU 5435 CD2 LEU C 108 1362 2399 2861 22 1015 -125 C
ATOM 5436 N LYS C 109 29.781 37.765 14.438 1.00 18.99 N
ANISOU 5436 N LYS C 109 1513 2288 3414 -67 911 -538 N
ATOM 5437 CA LYS C 109 30.852 38.122 15.357 1.00 19.81 C
ANISOU 5437 CA LYS C 109 1624 2291 3612 -103 806 -630 C
ATOM 5438 C LYS C 109 30.435 39.307 16.217 1.00 22.17 C
ANISOU 5438 C LYS C 109 1982 2498 3944 -186 894 -634 C
ATOM 5439 O LYS C 109 29.937 40.318 15.711 1.00 20.82 O
ANISOU 5439 O LYS C 109 1720 2351 3840 -188 1082 -558 O
ATOM 5440 CB LYS C 109 32.128 38.459 14.585 1.00 20.41 C
ANISOU 5440 CB LYS C 109 1500 2389 3868 -37 815 -630 C
ATOM 5441 CG LYS C 109 33.091 39.334 15.374 1.00 21.44 C
ANISOU 5441 CG LYS C 109 1581 2408 4158 -93 754 -691 C
ATOM 5442 CD LYS C 109 34.536 39.213 14.901 1.00 28.82 C
ANISOU 5442 CD LYS C 109 2336 3337 5275 -31 684 -702 C
ATOM 5443 CE LYS C 109 34.741 39.759 13.501 1.00 29.15 C
ANISOU 5443 CE LYS C 109 2300 3455 5320 48 814 -566 C
ATOM 5444 NZ LYS C 109 36.070 40.414 13.352 1.00 26.75 N
ANISOU 5444 NZ LYS C 109 1878 3091 5194 59 779 -544 N
ATOM 5445 N GLY C 110 30.635 39.173 17.525 1.00 23.99 N
ANISOU 5445 N GLY C 110 2382 2617 4117 -250 760 -722 N
ATOM 5446 CA GLY C 110 30.282 40.224 18.452 1.00 28.34 C
ANISOU 5446 CA GLY C 110 3041 3056 4672 -325 831 -741 C
ATOM 5447 C GLY C 110 28.842 40.227 18.916 1.00 20.70 C
ANISOU 5447 C GLY C 110 2237 2068 3562 -353 957 -682 C
ATOM 5448 O GLY C 110 28.484 41.067 19.749 1.00 21.25 O
ANISOU 5448 O GLY C 110 2430 2029 3614 -406 1037 -695 O
ATOM 5449 N GLU C 111 28.006 39.321 18.418 1.00 19.87 N
ANISOU 5449 N GLU C 111 2139 2051 3360 -319 981 -614 N
ATOM 5450 CA GLU C 111 26.604 39.283 18.805 1.00 20.31 C
ANISOU 5450 CA GLU C 111 2318 2085 3314 -343 1107 -532 C
ATOM 5451 C GLU C 111 26.400 38.335 19.974 1.00 25.22 C
ANISOU 5451 C GLU C 111 3175 2624 3784 -367 976 -591 C
ATOM 5452 O GLU C 111 26.978 37.249 20.016 1.00 28.47 O
ANISOU 5452 O GLU C 111 3616 3059 4143 -346 791 -654 O
ATOM 5453 CB GLU C 111 25.725 38.853 17.631 1.00 18.70 C
ANISOU 5453 CB GLU C 111 1989 2010 3106 -304 1194 -411 C
ATOM 5454 CG GLU C 111 24.282 38.531 18.012 1.00 25.16 C
ANISOU 5454 CG GLU C 111 2915 2806 3838 -329 1286 -312 C
ATOM 5455 CD GLU C 111 23.446 38.166 16.808 1.00 27.58 C
ANISOU 5455 CD GLU C 111 3098 3233 4147 -295 1309 -186 C
ATOM 5456 OE1 GLU C 111 22.236 37.891 16.964 1.00 29.64 O
ANISOU 5456 OE1 GLU C 111 3423 3486 4352 -301 1317 -83 O
ATOM 5457 OE2 GLU C 111 24.012 38.153 15.694 1.00 25.26 O
ANISOU 5457 OE2 GLU C 111 2682 3038 3879 -241 1231 -182 O
ATOM 5458 N THR C 112 25.567 38.754 20.920 1.00 20.26 N
ANISOU 5458 N THR C 112 2722 1891 3085 -402 1089 -562 N
ATOM 5459 CA THR C 112 25.225 37.900 22.047 1.00 21.97 C
ANISOU 5459 CA THR C 112 3181 2019 3148 -415 1003 -597 C
ATOM 5460 C THR C 112 24.453 36.675 21.573 1.00 22.34 C
ANISOU 5460 C THR C 112 3201 2147 3138 -390 979 -520 C
ATOM 5461 O THR C 112 23.421 36.794 20.902 1.00 19.43 O
ANISOU 5461 O THR C 112 2732 1839 2812 -386 1129 -391 O
ATOM 5462 CB THR C 112 24.411 38.688 23.072 1.00 26.33 C
ANISOU 5462 CB THR C 112 3929 2434 3640 -442 1178 -561 C
ATOM 5463 OG1 THR C 112 25.230 39.725 23.622 1.00 34.69 O
ANISOU 5463 OG1 THR C 112 5054 3395 4732 -472 1157 -658 O
ATOM 5464 CG2 THR C 112 23.952 37.787 24.204 1.00 25.66 C
ANISOU 5464 CG2 THR C 112 4105 2253 3390 -440 1123 -575 C
ATOM 5465 N VAL C 113 24.968 35.499 21.918 1.00 27.13 N
ANISOU 5465 N VAL C 113 3898 2751 3661 -378 780 -596 N
ATOM 5466 CA VAL C 113 24.310 34.226 21.658 1.00 21.66 C
ANISOU 5466 CA VAL C 113 3222 2105 2902 -362 728 -542 C
ATOM 5467 C VAL C 113 23.835 33.661 22.988 1.00 25.43 C
ANISOU 5467 C VAL C 113 3955 2459 3246 -375 710 -551 C
ATOM 5468 O VAL C 113 24.615 33.560 23.943 1.00 21.32 O
ANISOU 5468 O VAL C 113 3598 1854 2650 -377 583 -660 O
ATOM 5469 CB VAL C 113 25.251 33.242 20.943 1.00 23.99 C
ANISOU 5469 CB VAL C 113 3424 2488 3204 -325 532 -612 C
ATOM 5470 CG1 VAL C 113 24.634 31.850 20.893 1.00 18.95 C
ANISOU 5470 CG1 VAL C 113 2853 1866 2480 -316 454 -577 C
ATOM 5471 CG2 VAL C 113 25.569 33.742 19.545 1.00 27.29 C
ANISOU 5471 CG2 VAL C 113 3604 3025 3741 -296 585 -579 C
ATOM 5472 N ASN C 114 22.555 33.305 23.054 1.00 20.07 N
ANISOU 5472 N ASN C 114 3313 1765 2546 -381 834 -428 N
ATOM 5473 CA ASN C 114 21.971 32.696 24.245 1.00 29.48 C
ANISOU 5473 CA ASN C 114 4742 2837 3621 -382 851 -409 C
ATOM 5474 C ASN C 114 20.949 31.675 23.766 1.00 25.79 C
ANISOU 5474 C ASN C 114 4213 2414 3173 -384 868 -291 C
ATOM 5475 O ASN C 114 19.894 32.049 23.242 1.00 30.96 O
ANISOU 5475 O ASN C 114 4750 3095 3917 -399 1032 -149 O
ATOM 5476 CB ASN C 114 21.334 33.753 25.148 1.00 27.56 C
ANISOU 5476 CB ASN C 114 4647 2468 3355 -390 1066 -356 C
ATOM 5477 CG ASN C 114 20.978 33.217 26.517 1.00 48.71 C
ANISOU 5477 CG ASN C 114 7620 5002 5887 -374 1080 -360 C
ATOM 5478 OD1 ASN C 114 21.287 32.073 26.850 1.00 49.04 O
ANISOU 5478 OD1 ASN C 114 7752 5036 5844 -360 914 -410 O
ATOM 5479 ND2 ASN C 114 20.330 34.047 27.324 1.00 66.16 N
ANISOU 5479 ND2 ASN C 114 9992 7086 8061 -367 1292 -301 N
ATOM 5480 N THR C 115 21.264 30.390 23.920 1.00 21.99 N
ANISOU 5480 N THR C 115 3802 1935 2618 -371 692 -344 N
ATOM 5481 CA THR C 115 20.418 29.346 23.362 1.00 20.55 C
ANISOU 5481 CA THR C 115 3551 1792 2464 -381 670 -248 C
ATOM 5482 C THR C 115 20.473 28.106 24.242 1.00 26.16 C
ANISOU 5482 C THR C 115 4453 2422 3064 -367 555 -285 C
ATOM 5483 O THR C 115 21.425 27.891 24.999 1.00 24.64 O
ANISOU 5483 O THR C 115 4409 2182 2772 -342 433 -407 O
ATOM 5484 CB THR C 115 20.833 28.987 21.928 1.00 28.38 C
ANISOU 5484 CB THR C 115 4338 2925 3519 -378 549 -271 C
ATOM 5485 OG1 THR C 115 19.761 28.292 21.285 1.00 42.32 O
ANISOU 5485 OG1 THR C 115 6023 4721 5334 -404 561 -150 O
ATOM 5486 CG2 THR C 115 22.065 28.093 21.931 1.00 28.37 C
ANISOU 5486 CG2 THR C 115 4388 2945 3445 -343 329 -415 C
ATOM 5487 N SER C 116 19.423 27.295 24.133 1.00 20.71 N
ANISOU 5487 N SER C 116 3752 1712 2404 -385 591 -168 N
ATOM 5488 CA SER C 116 19.356 25.977 24.751 1.00 28.49 C
ANISOU 5488 CA SER C 116 4885 2631 3311 -373 485 -181 C
ATOM 5489 C SER C 116 19.135 24.956 23.646 1.00 26.17 C
ANISOU 5489 C SER C 116 4449 2419 3075 -394 356 -156 C
ATOM 5490 O SER C 116 18.142 25.040 22.912 1.00 30.95 O
ANISOU 5490 O SER C 116 4911 3058 3790 -434 432 -28 O
ATOM 5491 CB SER C 116 18.231 25.904 25.785 1.00 28.65 C
ANISOU 5491 CB SER C 116 5050 2514 3319 -374 664 -51 C
ATOM 5492 OG SER C 116 18.430 26.846 26.822 1.00 36.18 O
ANISOU 5492 OG SER C 116 6176 3376 4194 -347 788 -80 O
ATOM 5493 N ILE C 117 20.046 23.999 23.533 1.00 22.80 N
ANISOU 5493 N ILE C 117 4071 2016 2576 -368 159 -273 N
ATOM 5494 CA ILE C 117 20.057 23.036 22.436 1.00 20.14 C
ANISOU 5494 CA ILE C 117 3631 1752 2271 -378 20 -282 C
ATOM 5495 C ILE C 117 19.592 21.691 22.972 1.00 25.98 C
ANISOU 5495 C ILE C 117 4495 2405 2973 -385 -49 -250 C
ATOM 5496 O ILE C 117 20.256 21.112 23.842 1.00 28.26 O
ANISOU 5496 O ILE C 117 4944 2631 3161 -345 -129 -332 O
ATOM 5497 CB ILE C 117 21.452 22.925 21.801 1.00 21.07 C
ANISOU 5497 CB ILE C 117 3701 1954 2350 -331 -132 -427 C
ATOM 5498 CG1 ILE C 117 21.950 24.309 21.381 1.00 22.82 C
ANISOU 5498 CG1 ILE C 117 3802 2246 2622 -321 -49 -452 C
ATOM 5499 CG2 ILE C 117 21.423 21.970 20.612 1.00 24.27 C
ANISOU 5499 CG2 ILE C 117 4029 2423 2771 -331 -254 -434 C
ATOM 5500 CD1 ILE C 117 23.430 24.367 21.133 1.00 26.80 C
ANISOU 5500 CD1 ILE C 117 4278 2799 3105 -268 -169 -586 C
ATOM 5501 N PRO C 118 18.473 21.154 22.494 1.00 22.14 N
ANISOU 5501 N PRO C 118 3938 1903 2570 -436 -30 -129 N
ATOM 5502 CA PRO C 118 18.049 19.821 22.925 1.00 23.17 C
ANISOU 5502 CA PRO C 118 4175 1945 2685 -448 -104 -97 C
ATOM 5503 C PRO C 118 18.947 18.739 22.351 1.00 27.06 C
ANISOU 5503 C PRO C 118 4696 2476 3110 -420 -314 -223 C
ATOM 5504 O PRO C 118 19.444 18.840 21.227 1.00 26.26 O
ANISOU 5504 O PRO C 118 4489 2474 3016 -414 -398 -285 O
ATOM 5505 CB PRO C 118 16.623 19.707 22.374 1.00 21.94 C
ANISOU 5505 CB PRO C 118 3891 1770 2676 -523 -38 76 C
ATOM 5506 CG PRO C 118 16.619 20.606 21.195 1.00 23.94 C
ANISOU 5506 CG PRO C 118 3963 2144 2991 -543 -29 86 C
ATOM 5507 CD PRO C 118 17.525 21.755 21.539 1.00 20.98 C
ANISOU 5507 CD PRO C 118 3607 1814 2552 -490 52 -5 C
ATOM 5508 N PHE C 119 19.147 17.688 23.145 1.00 27.49 N
ANISOU 5508 N PHE C 119 4907 2443 3097 -396 -384 -255 N
ATOM 5509 CA PHE C 119 19.902 16.529 22.695 1.00 25.41 C
ANISOU 5509 CA PHE C 119 4688 2192 2775 -365 -569 -359 C
ATOM 5510 C PHE C 119 19.311 15.278 23.329 1.00 28.45 C
ANISOU 5510 C PHE C 119 5195 2459 3157 -381 -603 -304 C
ATOM 5511 O PHE C 119 18.624 15.338 24.352 1.00 32.96 O
ANISOU 5511 O PHE C 119 5849 2935 3740 -390 -484 -210 O
ATOM 5512 CB PHE C 119 21.402 16.658 23.019 1.00 24.57 C
ANISOU 5512 CB PHE C 119 4646 2121 2568 -285 -652 -507 C
ATOM 5513 CG PHE C 119 21.726 16.587 24.489 1.00 26.54 C
ANISOU 5513 CG PHE C 119 5074 2280 2732 -246 -633 -527 C
ATOM 5514 CD1 PHE C 119 21.598 17.703 25.299 1.00 25.80 C
ANISOU 5514 CD1 PHE C 119 5023 2160 2619 -247 -504 -500 C
ATOM 5515 CD2 PHE C 119 22.183 15.405 25.054 1.00 30.00 C
ANISOU 5515 CD2 PHE C 119 5647 2655 3097 -203 -745 -571 C
ATOM 5516 CE1 PHE C 119 21.903 17.638 26.648 1.00 30.77 C
ANISOU 5516 CE1 PHE C 119 5850 2696 3144 -207 -498 -523 C
ATOM 5517 CE2 PHE C 119 22.489 15.336 26.399 1.00 32.11 C
ANISOU 5517 CE2 PHE C 119 6046 2868 3286 -156 -722 -562 C
ATOM 5518 CZ PHE C 119 22.349 16.453 27.197 1.00 34.04 C
ANISOU 5518 CZ PHE C 119 6370 3073 3492 -160 -612 -549 C
ATOM 5519 N SER C 120 19.582 14.140 22.697 1.00 33.10 N
ANISOU 5519 N SER C 120 5802 3045 3730 -378 -755 -359 N
ATOM 5520 CA SER C 120 19.031 12.861 23.134 1.00 30.86 C
ANISOU 5520 CA SER C 120 5620 2646 3458 -399 -803 -310 C
ATOM 5521 C SER C 120 19.909 11.762 22.563 1.00 33.42 C
ANISOU 5521 C SER C 120 6003 2979 3715 -357 -979 -431 C
ATOM 5522 O SER C 120 20.057 11.673 21.341 1.00 37.41 O
ANISOU 5522 O SER C 120 6428 3551 4235 -371 -1062 -474 O
ATOM 5523 CB SER C 120 17.581 12.706 22.659 1.00 34.99 C
ANISOU 5523 CB SER C 120 6042 3125 4127 -499 -762 -158 C
ATOM 5524 OG SER C 120 17.049 11.447 23.030 1.00 42.07 O
ANISOU 5524 OG SER C 120 7025 3901 5059 -526 -813 -106 O
ATOM 5525 N PHE C 121 20.500 10.942 23.429 1.00 34.34 N
ANISOU 5525 N PHE C 121 6263 3031 3755 -295 -1025 -477 N
ATOM 5526 CA PHE C 121 21.307 9.820 22.971 1.00 35.37 C
ANISOU 5526 CA PHE C 121 6361 3220 3856 -225 -1119 -525 C
ATOM 5527 C PHE C 121 21.154 8.669 23.957 1.00 42.06 C
ANISOU 5527 C PHE C 121 7353 3953 4673 -205 -1142 -493 C
ATOM 5528 O PHE C 121 20.641 8.839 25.066 1.00 38.73 O
ANISOU 5528 O PHE C 121 7054 3425 4235 -221 -1073 -442 O
ATOM 5529 CB PHE C 121 22.777 10.223 22.781 1.00 34.91 C
ANISOU 5529 CB PHE C 121 6205 3297 3763 -123 -1118 -597 C
ATOM 5530 CG PHE C 121 23.552 10.356 24.063 1.00 32.32 C
ANISOU 5530 CG PHE C 121 5941 2959 3381 -57 -1098 -607 C
ATOM 5531 CD1 PHE C 121 24.239 9.269 24.577 1.00 35.94 C
ANISOU 5531 CD1 PHE C 121 6462 3388 3804 10 -1158 -615 C
ATOM 5532 CD2 PHE C 121 23.620 11.566 24.736 1.00 26.13 C
ANISOU 5532 CD2 PHE C 121 5162 2189 2577 -63 -1028 -607 C
ATOM 5533 CE1 PHE C 121 24.959 9.376 25.741 1.00 34.52 C
ANISOU 5533 CE1 PHE C 121 6349 3195 3573 67 -1165 -618 C
ATOM 5534 CE2 PHE C 121 24.343 11.679 25.907 1.00 26.93 C
ANISOU 5534 CE2 PHE C 121 5333 2277 2621 -6 -1032 -614 C
ATOM 5535 CZ PHE C 121 25.015 10.580 26.408 1.00 28.13 C
ANISOU 5535 CZ PHE C 121 5546 2401 2740 57 -1108 -618 C
ATOM 5536 N GLU C 122 21.625 7.491 23.548 1.00 44.80 N
ANISOU 5536 N GLU C 122 7701 4311 5011 -162 -1223 -519 N
ATOM 5537 CA GLU C 122 21.250 6.259 24.229 1.00 49.23 C
ANISOU 5537 CA GLU C 122 8395 4748 5563 -164 -1258 -482 C
ATOM 5538 C GLU C 122 22.047 5.103 23.646 1.00 57.63 C
ANISOU 5538 C GLU C 122 9444 5843 6608 -98 -1339 -527 C
ATOM 5539 O GLU C 122 22.449 5.141 22.480 1.00 61.28 O
ANISOU 5539 O GLU C 122 9807 6389 7088 -85 -1365 -568 O
ATOM 5540 CB GLU C 122 19.743 5.999 24.070 1.00 52.97 C
ANISOU 5540 CB GLU C 122 8904 5087 6136 -288 -1255 -399 C
ATOM 5541 CG GLU C 122 19.162 4.855 24.878 1.00 63.59 C
ANISOU 5541 CG GLU C 122 10376 6279 7508 -304 -1256 -332 C
ATOM 5542 CD GLU C 122 17.649 4.811 24.779 1.00 72.82 C
ANISOU 5542 CD GLU C 122 11517 7315 8837 -431 -1215 -199 C
ATOM 5543 OE1 GLU C 122 17.126 4.460 23.700 1.00 78.45 O
ANISOU 5543 OE1 GLU C 122 12141 8032 9636 -511 -1307 -188 O
ATOM 5544 OE2 GLU C 122 16.981 5.156 25.774 1.00 77.30 O
ANISOU 5544 OE2 GLU C 122 12131 7787 9452 -443 -1076 -84 O
ATOM 5545 N GLY C 123 22.290 4.094 24.476 1.00 61.82 N
ANISOU 5545 N GLY C 123 10092 6297 7100 -52 -1366 -516 N
ATOM 5546 CA GLY C 123 22.694 2.781 24.002 1.00 60.40 C
ANISOU 5546 CA GLY C 123 9942 6093 6916 -14 -1439 -541 C
ATOM 5547 C GLY C 123 24.037 2.642 23.311 1.00 56.14 C
ANISOU 5547 C GLY C 123 9326 5649 6355 81 -1461 -606 C
ATOM 5548 O GLY C 123 24.149 1.873 22.346 1.00 56.19 O
ANISOU 5548 O GLY C 123 9327 5650 6373 88 -1503 -631 O
ATOM 5549 N ILE C 124 25.062 3.355 23.775 1.00 42.93 N
ANISOU 5549 N ILE C 124 7605 4048 4656 152 -1436 -632 N
ATOM 5550 CA ILE C 124 26.446 3.049 23.425 1.00 38.42 C
ANISOU 5550 CA ILE C 124 6995 3526 4075 251 -1467 -683 C
ATOM 5551 C ILE C 124 27.183 2.686 24.703 1.00 38.60 C
ANISOU 5551 C ILE C 124 7106 3506 4055 323 -1504 -675 C
ATOM 5552 O ILE C 124 27.146 3.439 25.683 1.00 43.21 O
ANISOU 5552 O ILE C 124 7709 4094 4614 317 -1483 -653 O
ATOM 5553 CB ILE C 124 27.160 4.215 22.715 1.00 40.87 C
ANISOU 5553 CB ILE C 124 7164 3950 4414 272 -1429 -724 C
ATOM 5554 CG1 ILE C 124 26.776 4.280 21.240 1.00 47.02 C
ANISOU 5554 CG1 ILE C 124 7881 4768 5218 237 -1413 -745 C
ATOM 5555 CG2 ILE C 124 28.679 4.057 22.837 1.00 33.05 C
ANISOU 5555 CG2 ILE C 124 6159 2982 3418 381 -1471 -768 C
ATOM 5556 CD1 ILE C 124 27.854 4.909 20.365 1.00 56.65 C
ANISOU 5556 CD1 ILE C 124 9005 6072 6448 301 -1393 -799 C
ATOM 5557 N LEU C 125 27.853 1.539 24.689 1.00 39.93 N
ANISOU 5557 N LEU C 125 7343 3626 4205 395 -1564 -692 N
ATOM 5558 CA LEU C 125 28.694 1.148 25.808 1.00 35.65 C
ANISOU 5558 CA LEU C 125 6886 3041 3620 477 -1623 -687 C
ATOM 5559 C LEU C 125 30.027 1.884 25.733 1.00 34.81 C
ANISOU 5559 C LEU C 125 6685 3005 3535 549 -1654 -732 C
ATOM 5560 O LEU C 125 30.764 1.761 24.748 1.00 35.94 O
ANISOU 5560 O LEU C 125 6763 3183 3711 598 -1667 -779 O
ATOM 5561 CB LEU C 125 28.916 -0.363 25.805 1.00 32.44 C
ANISOU 5561 CB LEU C 125 6592 2544 3188 530 -1681 -690 C
ATOM 5562 CG LEU C 125 29.660 -0.943 27.008 1.00 31.57 C
ANISOU 5562 CG LEU C 125 6601 2370 3025 617 -1755 -678 C
ATOM 5563 CD1 LEU C 125 28.949 -0.588 28.305 1.00 31.96 C
ANISOU 5563 CD1 LEU C 125 6750 2374 3018 580 -1736 -622 C
ATOM 5564 CD2 LEU C 125 29.794 -2.450 26.864 1.00 33.43 C
ANISOU 5564 CD2 LEU C 125 6947 2517 3240 664 -1801 -682 C
ATOM 5565 N PHE C 126 30.325 2.662 26.771 1.00 33.46 N
ANISOU 5565 N PHE C 126 6523 2845 3344 557 -1670 -718 N
ATOM 5566 CA PHE C 126 31.583 3.374 26.899 1.00 30.24 C
ANISOU 5566 CA PHE C 126 6039 2486 2966 619 -1728 -757 C
ATOM 5567 C PHE C 126 32.500 2.645 27.871 1.00 32.21 C
ANISOU 5567 C PHE C 126 6398 2661 3180 712 -1849 -757 C
ATOM 5568 O PHE C 126 32.057 2.234 28.951 1.00 34.38 O
ANISOU 5568 O PHE C 126 6811 2866 3388 709 -1866 -712 O
ATOM 5569 CB PHE C 126 31.371 4.808 27.396 1.00 29.08 C
ANISOU 5569 CB PHE C 126 5832 2395 2823 561 -1684 -747 C
ATOM 5570 CG PHE C 126 30.708 5.701 26.392 1.00 32.12 C
ANISOU 5570 CG PHE C 126 6094 2860 3252 486 -1582 -757 C
ATOM 5571 CD1 PHE C 126 31.459 6.369 25.439 1.00 33.86 C
ANISOU 5571 CD1 PHE C 126 6179 3155 3533 507 -1580 -806 C
ATOM 5572 CD2 PHE C 126 29.333 5.877 26.398 1.00 36.94 C
ANISOU 5572 CD2 PHE C 126 6735 3459 3842 399 -1498 -716 C
ATOM 5573 CE1 PHE C 126 30.854 7.198 24.510 1.00 37.76 C
ANISOU 5573 CE1 PHE C 126 6571 3718 4058 443 -1490 -813 C
ATOM 5574 CE2 PHE C 126 28.719 6.706 25.472 1.00 34.81 C
ANISOU 5574 CE2 PHE C 126 6357 3255 3613 333 -1420 -724 C
ATOM 5575 CZ PHE C 126 29.483 7.366 24.526 1.00 35.90 C
ANISOU 5575 CZ PHE C 126 6363 3476 3803 355 -1414 -772 C
ATOM 5576 N PRO C 127 33.769 2.461 27.522 1.00 35.74 N
ANISOU 5576 N PRO C 127 6802 3109 3669 803 -1941 -806 N
ATOM 5577 CA PRO C 127 34.716 1.903 28.489 1.00 40.08 C
ANISOU 5577 CA PRO C 127 7450 3584 4195 896 -2083 -808 C
ATOM 5578 C PRO C 127 34.882 2.817 29.690 1.00 39.19 C
ANISOU 5578 C PRO C 127 7361 3471 4060 872 -2130 -787 C
ATOM 5579 O PRO C 127 34.839 4.045 29.582 1.00 39.54 O
ANISOU 5579 O PRO C 127 7300 3585 4137 815 -2087 -797 O
ATOM 5580 CB PRO C 127 36.019 1.792 27.688 1.00 44.22 C
ANISOU 5580 CB PRO C 127 7892 4115 4792 996 -2173 -876 C
ATOM 5581 CG PRO C 127 35.840 2.719 26.522 1.00 44.81 C
ANISOU 5581 CG PRO C 127 7817 4285 4925 946 -2073 -908 C
ATOM 5582 CD PRO C 127 34.383 2.659 26.201 1.00 34.35 C
ANISOU 5582 CD PRO C 127 6507 2986 3558 839 -1929 -863 C
ATOM 5583 N LYS C 128 35.054 2.194 30.851 1.00 35.51 N
ANISOU 5583 N LYS C 128 7049 2916 3527 918 -2218 -757 N
ATOM 5584 CA LYS C 128 35.302 2.933 32.076 1.00 36.91 C
ANISOU 5584 CA LYS C 128 7288 3071 3666 907 -2280 -738 C
ATOM 5585 C LYS C 128 36.674 3.594 32.027 1.00 37.64 C
ANISOU 5585 C LYS C 128 7268 3189 3846 949 -2419 -788 C
ATOM 5586 O LYS C 128 37.594 3.134 31.345 1.00 43.79 O
ANISOU 5586 O LYS C 128 7976 3964 4700 1025 -2510 -833 O
ATOM 5587 CB LYS C 128 35.224 2.008 33.291 1.00 39.35 C
ANISOU 5587 CB LYS C 128 7812 3265 3876 960 -2351 -697 C
ATOM 5588 CG LYS C 128 33.847 1.871 33.931 1.00 44.23 C
ANISOU 5588 CG LYS C 128 8579 3840 4388 904 -2230 -634 C
ATOM 5589 CD LYS C 128 32.718 1.704 32.919 1.00 51.75 C
ANISOU 5589 CD LYS C 128 9462 4838 5362 832 -2082 -623 C
ATOM 5590 CE LYS C 128 31.386 1.386 33.607 1.00 56.61 C
ANISOU 5590 CE LYS C 128 10249 5383 5878 790 -1987 -558 C
ATOM 5591 NZ LYS C 128 30.935 2.456 34.542 1.00 60.57 N
ANISOU 5591 NZ LYS C 128 10828 5874 6311 751 -1937 -529 N
ATOM 5592 N GLY C 129 36.802 4.698 32.760 1.00 37.99 N
ANISOU 5592 N GLY C 129 7304 3249 3882 901 -2441 -783 N
ATOM 5593 CA GLY C 129 38.095 5.318 32.915 1.00 36.76 C
ANISOU 5593 CA GLY C 129 7055 3099 3812 928 -2598 -822 C
ATOM 5594 C GLY C 129 38.050 6.810 32.669 1.00 35.70 C
ANISOU 5594 C GLY C 129 6793 3045 3728 847 -2544 -839 C
ATOM 5595 O GLY C 129 37.027 7.474 32.874 1.00 36.20 O
ANISOU 5595 O GLY C 129 6891 3139 3724 770 -2405 -813 O
ATOM 5596 N HIS C 130 39.188 7.325 32.227 1.00 35.90 N
ANISOU 5596 N HIS C 130 6668 3094 3877 870 -2664 -883 N
ATOM 5597 CA HIS C 130 39.490 8.749 32.239 1.00 37.21 C
ANISOU 5597 CA HIS C 130 6723 3309 4105 804 -2675 -902 C
ATOM 5598 C HIS C 130 39.537 9.262 30.803 1.00 35.91 C
ANISOU 5598 C HIS C 130 6369 3230 4046 796 -2594 -943 C
ATOM 5599 O HIS C 130 40.434 8.898 30.034 1.00 37.78 O
ANISOU 5599 O HIS C 130 6492 3466 4395 869 -2690 -981 O
ATOM 5600 CB HIS C 130 40.813 8.976 32.960 1.00 44.94 C
ANISOU 5600 CB HIS C 130 7677 4234 5165 830 -2902 -912 C
ATOM 5601 CG HIS C 130 41.166 10.413 33.150 1.00 57.71 C
ANISOU 5601 CG HIS C 130 9204 5879 6844 757 -2938 -926 C
ATOM 5602 ND1 HIS C 130 42.303 10.807 33.820 1.00 63.32 N
ANISOU 5602 ND1 HIS C 130 9879 6540 7640 755 -3143 -928 N
ATOM 5603 CD2 HIS C 130 40.543 11.551 32.762 1.00 60.03 C
ANISOU 5603 CD2 HIS C 130 9436 6241 7133 680 -2800 -938 C
ATOM 5604 CE1 HIS C 130 42.367 12.126 33.836 1.00 62.66 C
ANISOU 5604 CE1 HIS C 130 9722 6487 7599 679 -3133 -943 C
ATOM 5605 NE2 HIS C 130 41.311 12.602 33.200 1.00 61.17 N
ANISOU 5605 NE2 HIS C 130 9518 6370 7354 636 -2923 -952 N
ATOM 5606 N TYR C 131 38.580 10.115 30.449 1.00 33.34 N
ANISOU 5606 N TYR C 131 6012 2972 3684 714 -2424 -937 N
ATOM 5607 CA TYR C 131 38.488 10.677 29.109 1.00 33.69 C
ANISOU 5607 CA TYR C 131 5895 3095 3810 699 -2330 -975 C
ATOM 5608 C TYR C 131 38.978 12.117 29.100 1.00 34.85 C
ANISOU 5608 C TYR C 131 5920 3276 4044 647 -2364 -1001 C
ATOM 5609 O TYR C 131 38.704 12.882 30.029 1.00 34.42 O
ANISOU 5609 O TYR C 131 5934 3210 3933 581 -2357 -979 O
ATOM 5610 CB TYR C 131 37.050 10.633 28.582 1.00 30.71 C
ANISOU 5610 CB TYR C 131 5549 2768 3350 639 -2118 -947 C
ATOM 5611 CG TYR C 131 36.496 9.251 28.319 1.00 30.51 C
ANISOU 5611 CG TYR C 131 5615 2713 3264 678 -2072 -924 C
ATOM 5612 CD1 TYR C 131 36.129 8.418 29.366 1.00 32.17 C
ANISOU 5612 CD1 TYR C 131 5989 2852 3383 690 -2100 -879 C
ATOM 5613 CD2 TYR C 131 36.312 8.790 27.022 1.00 31.60 C
ANISOU 5613 CD2 TYR C 131 5689 2885 3434 704 -2001 -947 C
ATOM 5614 CE1 TYR C 131 35.610 7.157 29.132 1.00 35.23 C
ANISOU 5614 CE1 TYR C 131 6460 3202 3722 721 -2064 -857 C
ATOM 5615 CE2 TYR C 131 35.786 7.529 26.779 1.00 35.85 C
ANISOU 5615 CE2 TYR C 131 6318 3387 3917 730 -1964 -926 C
ATOM 5616 CZ TYR C 131 35.441 6.716 27.838 1.00 34.46 C
ANISOU 5616 CZ TYR C 131 6291 3140 3663 736 -1998 -881 C
ATOM 5617 OH TYR C 131 34.923 5.464 27.603 1.00 31.54 O
ANISOU 5617 OH TYR C 131 6011 2724 3248 759 -1968 -861 O
ATOM 5618 N ARG C 132 39.699 12.481 28.041 1.00 32.21 N
ANISOU 5618 N ARG C 132 5414 2976 3848 682 -2403 -1050 N
ATOM 5619 CA ARG C 132 40.015 13.870 27.736 1.00 32.07 C
ANISOU 5619 CA ARG C 132 5255 2998 3932 628 -2403 -1078 C
ATOM 5620 C ARG C 132 39.464 14.209 26.359 1.00 36.44 C
ANISOU 5620 C ARG C 132 5709 3625 4513 624 -2248 -1111 C
ATOM 5621 O ARG C 132 39.536 13.395 25.432 1.00 32.40 O
ANISOU 5621 O ARG C 132 5175 3120 4017 700 -2229 -1138 O
ATOM 5622 CB ARG C 132 41.526 14.143 27.781 1.00 36.97 C
ANISOU 5622 CB ARG C 132 5726 3581 4741 673 -2622 -1103 C
ATOM 5623 CG ARG C 132 41.931 15.482 27.158 1.00 40.58 C
ANISOU 5623 CG ARG C 132 5989 4078 5353 631 -2621 -1135 C
ATOM 5624 CD ARG C 132 43.128 16.109 27.859 1.00 55.29 C
ANISOU 5624 CD ARG C 132 7747 5888 7374 610 -2822 -1119 C
ATOM 5625 NE ARG C 132 42.863 16.346 29.276 1.00 65.42 N
ANISOU 5625 NE ARG C 132 9217 7121 8518 543 -2858 -1087 N
ATOM 5626 CZ ARG C 132 43.454 15.685 30.266 1.00 68.25 C
ANISOU 5626 CZ ARG C 132 9668 7406 8856 569 -3019 -1057 C
ATOM 5627 NH1 ARG C 132 44.359 14.753 29.998 1.00 70.49 N
ANISOU 5627 NH1 ARG C 132 9861 7661 9261 657 -3155 -1045 N
ATOM 5628 NH2 ARG C 132 43.148 15.963 31.525 1.00 61.00 N
ANISOU 5628 NH2 ARG C 132 8935 6443 7801 515 -3046 -1036 N
ATOM 5629 N CYS C 133 38.900 15.408 26.231 1.00 29.88 N
ANISOU 5629 N CYS C 133 4833 2841 3677 541 -2138 -1111 N
ATOM 5630 CA CYS C 133 38.327 15.863 24.969 1.00 28.62 C
ANISOU 5630 CA CYS C 133 4585 2749 3539 529 -1990 -1139 C
ATOM 5631 C CYS C 133 38.489 17.373 24.901 1.00 37.80 C
ANISOU 5631 C CYS C 133 5635 3938 4792 465 -1975 -1162 C
ATOM 5632 O CYS C 133 37.774 18.113 25.586 1.00 39.90 O
ANISOU 5632 O CYS C 133 5974 4211 4977 378 -1896 -1131 O
ATOM 5633 CB CYS C 133 36.857 15.465 24.848 1.00 28.37 C
ANISOU 5633 CB CYS C 133 4668 2752 3361 479 -1807 -1089 C
ATOM 5634 SG CYS C 133 36.008 16.122 23.387 1.00 30.75 S
ANISOU 5634 SG CYS C 133 4877 3133 3674 449 -1630 -1108 S
ATOM 5635 N VAL C 134 39.438 17.828 24.093 1.00 37.37 N
ANISOU 5635 N VAL C 134 5397 3887 4915 512 -2054 -1221 N
ATOM 5636 CA VAL C 134 39.558 19.239 23.755 1.00 38.61 C
ANISOU 5636 CA VAL C 134 5413 4069 5188 456 -2018 -1248 C
ATOM 5637 C VAL C 134 38.668 19.504 22.546 1.00 35.83 C
ANISOU 5637 C VAL C 134 5015 3796 4803 458 -1783 -1232 C
ATOM 5638 O VAL C 134 38.771 18.825 21.516 1.00 30.88 O
ANISOU 5638 O VAL C 134 4329 3206 4198 544 -1688 -1207 O
ATOM 5639 CB VAL C 134 41.031 19.624 23.503 1.00 36.03 C
ANISOU 5639 CB VAL C 134 4842 3731 5115 507 -2103 -1214 C
ATOM 5640 CG1 VAL C 134 41.925 18.399 23.572 1.00 41.62 C
ANISOU 5640 CG1 VAL C 134 5528 4404 5883 612 -2218 -1183 C
ATOM 5641 CG2 VAL C 134 41.233 20.361 22.176 1.00 35.34 C
ANISOU 5641 CG2 VAL C 134 4531 3712 5185 544 -1908 -1175 C
ATOM 5642 N ALA C 135 37.751 20.455 22.689 1.00 30.78 N
ANISOU 5642 N ALA C 135 4423 3175 4097 367 -1691 -1244 N
ATOM 5643 CA ALA C 135 36.750 20.747 21.670 1.00 25.17 C
ANISOU 5643 CA ALA C 135 3688 2536 3340 354 -1487 -1221 C
ATOM 5644 C ALA C 135 37.042 22.117 21.073 1.00 30.47 C
ANISOU 5644 C ALA C 135 4167 3251 4159 333 -1382 -1203 C
ATOM 5645 O ALA C 135 36.953 23.134 21.766 1.00 29.65 O
ANISOU 5645 O ALA C 135 4073 3119 4075 253 -1405 -1220 O
ATOM 5646 CB ALA C 135 35.343 20.687 22.257 1.00 24.35 C
ANISOU 5646 CB ALA C 135 3762 2433 3059 271 -1399 -1186 C
ATOM 5647 N GLU C 136 37.353 22.140 19.782 1.00 29.30 N
ANISOU 5647 N GLU C 136 3863 3164 4105 409 -1257 -1167 N
ATOM 5648 CA GLU C 136 37.884 23.317 19.105 1.00 28.66 C
ANISOU 5648 CA GLU C 136 3571 3119 4198 419 -1154 -1136 C
ATOM 5649 C GLU C 136 36.856 23.821 18.099 1.00 28.01 C
ANISOU 5649 C GLU C 136 3474 3113 4054 405 -953 -1106 C
ATOM 5650 O GLU C 136 36.661 23.204 17.048 1.00 24.87 O
ANISOU 5650 O GLU C 136 3077 2761 3613 480 -861 -1083 O
ATOM 5651 CB GLU C 136 39.202 22.966 18.418 1.00 32.55 C
ANISOU 5651 CB GLU C 136 3888 3611 4869 537 -1158 -1101 C
ATOM 5652 CG GLU C 136 40.033 24.141 17.953 1.00 41.93 C
ANISOU 5652 CG GLU C 136 4837 4809 6287 551 -1086 -1059 C
ATOM 5653 CD GLU C 136 41.269 23.683 17.208 1.00 52.76 C
ANISOU 5653 CD GLU C 136 6035 6169 7841 687 -1057 -1003 C
ATOM 5654 OE1 GLU C 136 41.134 22.857 16.282 1.00 51.53 O
ANISOU 5654 OE1 GLU C 136 5922 6045 7612 789 -946 -982 O
ATOM 5655 OE2 GLU C 136 42.378 24.130 17.561 1.00 55.21 O
ANISOU 5655 OE2 GLU C 136 6174 6431 8373 692 -1147 -974 O
ATOM 5656 N ALA C 137 36.215 24.945 18.412 1.00 30.40 N
ANISOU 5656 N ALA C 137 3774 3423 4351 314 -889 -1104 N
ATOM 5657 CA ALA C 137 35.197 25.526 17.546 1.00 27.03 C
ANISOU 5657 CA ALA C 137 3326 3067 3878 293 -707 -1063 C
ATOM 5658 C ALA C 137 35.854 26.391 16.480 1.00 27.14 C
ANISOU 5658 C ALA C 137 3125 3130 4058 352 -574 -1020 C
ATOM 5659 O ALA C 137 36.675 27.258 16.796 1.00 32.29 O
ANISOU 5659 O ALA C 137 3646 3751 4871 337 -596 -1021 O
ATOM 5660 CB ALA C 137 34.202 26.354 18.357 1.00 24.09 C
ANISOU 5660 CB ALA C 137 3045 2672 3436 179 -673 -1066 C
ATOM 5661 N ILE C 138 35.483 26.164 15.223 1.00 26.04 N
ANISOU 5661 N ILE C 138 2959 3059 3878 419 -442 -978 N
ATOM 5662 CA ILE C 138 36.124 26.806 14.083 1.00 29.00 C
ANISOU 5662 CA ILE C 138 3152 3478 4389 504 -297 -927 C
ATOM 5663 C ILE C 138 35.056 27.484 13.236 1.00 31.37 C
ANISOU 5663 C ILE C 138 3447 3850 4621 481 -135 -878 C
ATOM 5664 O ILE C 138 33.988 26.909 13.002 1.00 31.03 O
ANISOU 5664 O ILE C 138 3541 3836 4415 455 -134 -875 O
ATOM 5665 CB ILE C 138 36.916 25.793 13.233 1.00 26.78 C
ANISOU 5665 CB ILE C 138 2856 3197 4122 644 -285 -914 C
ATOM 5666 CG1 ILE C 138 37.787 24.899 14.119 1.00 27.10 C
ANISOU 5666 CG1 ILE C 138 2929 3165 4203 665 -461 -954 C
ATOM 5667 CG2 ILE C 138 37.779 26.510 12.211 1.00 28.11 C
ANISOU 5667 CG2 ILE C 138 2828 3390 4464 745 -127 -850 C
ATOM 5668 CD1 ILE C 138 38.922 25.631 14.789 1.00 27.20 C
ANISOU 5668 CD1 ILE C 138 2771 3126 4436 649 -533 -947 C
ATOM 5669 N ALA C 139 35.342 28.706 12.788 1.00 25.90 N
ANISOU 5669 N ALA C 139 2591 3184 4068 488 -4 -834 N
ATOM 5670 CA ALA C 139 34.518 29.384 11.792 1.00 23.95 C
ANISOU 5670 CA ALA C 139 2310 3010 3779 494 165 -771 C
ATOM 5671 C ALA C 139 34.987 28.931 10.416 1.00 30.78 C
ANISOU 5671 C ALA C 139 3141 3916 4638 636 265 -731 C
ATOM 5672 O ALA C 139 36.069 29.318 9.963 1.00 43.09 O
ANISOU 5672 O ALA C 139 4551 5464 6358 725 345 -701 O
ATOM 5673 CB ALA C 139 34.617 30.899 11.946 1.00 24.08 C
ANISOU 5673 CB ALA C 139 2177 3026 3946 443 271 -738 C
ATOM 5674 N GLY C 140 34.172 28.110 9.750 1.00 23.42 N
ANISOU 5674 N GLY C 140 2356 3021 3523 660 261 -727 N
ATOM 5675 CA GLY C 140 34.620 27.366 8.585 1.00 23.13 C
ANISOU 5675 CA GLY C 140 2363 2997 3429 800 318 -712 C
ATOM 5676 C GLY C 140 34.888 28.200 7.350 1.00 37.23 C
ANISOU 5676 C GLY C 140 4038 4831 5275 898 516 -636 C
ATOM 5677 O GLY C 140 35.549 27.717 6.425 1.00 41.75 O
ANISOU 5677 O GLY C 140 4632 5397 5835 1040 594 -617 O
ATOM 5678 N ASP C 141 34.382 29.433 7.301 1.00 37.44 N
ANISOU 5678 N ASP C 141 3961 4900 5363 835 612 -588 N
ATOM 5679 CA ASP C 141 34.655 30.284 6.147 1.00 44.93 C
ANISOU 5679 CA ASP C 141 4802 5893 6377 933 811 -507 C
ATOM 5680 C ASP C 141 36.023 30.945 6.256 1.00 49.90 C
ANISOU 5680 C ASP C 141 5278 6496 7186 970 852 -456 C
ATOM 5681 O ASP C 141 36.729 31.092 5.250 1.00 53.43 O
ANISOU 5681 O ASP C 141 5719 6975 7608 1055 919 -398 O
ATOM 5682 CB ASP C 141 33.556 31.336 6.001 1.00 47.30 C
ANISOU 5682 CB ASP C 141 5066 6253 6652 846 887 -453 C
ATOM 5683 CG ASP C 141 33.310 32.102 7.285 1.00 55.21 C
ANISOU 5683 CG ASP C 141 5991 7225 7761 703 835 -477 C
ATOM 5684 OD1 ASP C 141 33.588 31.549 8.370 1.00 61.65 O
ANISOU 5684 OD1 ASP C 141 6854 7982 8588 644 685 -549 O
ATOM 5685 OD2 ASP C 141 32.836 33.255 7.209 1.00 60.51 O
ANISOU 5685 OD2 ASP C 141 6630 7935 8426 633 887 -393 O
ATOM 5686 N THR C 142 36.413 31.338 7.467 1.00 47.46 N
ANISOU 5686 N THR C 142 4873 6130 7030 876 768 -493 N
ATOM 5687 CA THR C 142 37.700 31.965 7.720 1.00 40.53 C
ANISOU 5687 CA THR C 142 3872 5215 6313 872 758 -441 C
ATOM 5688 C THR C 142 38.723 31.007 8.317 1.00 37.00 C
ANISOU 5688 C THR C 142 3377 4687 5994 929 656 -497 C
ATOM 5689 O THR C 142 39.907 31.357 8.382 1.00 40.35 O
ANISOU 5689 O THR C 142 3692 5076 6561 944 652 -441 O
ATOM 5690 CB THR C 142 37.524 33.164 8.660 1.00 39.85 C
ANISOU 5690 CB THR C 142 3708 5099 6333 729 725 -445 C
ATOM 5691 OG1 THR C 142 37.103 32.700 9.951 1.00 42.18 O
ANISOU 5691 OG1 THR C 142 4002 5334 6690 659 598 -579 O
ATOM 5692 CG2 THR C 142 36.474 34.115 8.110 1.00 32.33 C
ANISOU 5692 CG2 THR C 142 2812 4221 5251 675 815 -381 C
ATOM 5693 N GLU C 143 38.297 29.819 8.752 1.00 30.54 N
ANISOU 5693 N GLU C 143 2658 3841 5105 950 548 -605 N
ATOM 5694 CA GLU C 143 39.153 28.831 9.409 1.00 35.72 C
ANISOU 5694 CA GLU C 143 3332 4430 5811 980 396 -645 C
ATOM 5695 C GLU C 143 39.739 29.344 10.720 1.00 36.09 C
ANISOU 5695 C GLU C 143 3270 4412 6031 874 244 -678 C
ATOM 5696 O GLU C 143 40.702 28.769 11.239 1.00 47.72 O
ANISOU 5696 O GLU C 143 4693 5821 7616 906 125 -688 O
ATOM 5697 CB GLU C 143 40.279 28.353 8.485 1.00 39.11 C
ANISOU 5697 CB GLU C 143 3689 4836 6336 1154 510 -577 C
ATOM 5698 CG GLU C 143 39.844 27.288 7.501 1.00 53.72 C
ANISOU 5698 CG GLU C 143 5724 6708 7977 1271 578 -588 C
ATOM 5699 CD GLU C 143 39.376 26.017 8.186 1.00 61.56 C
ANISOU 5699 CD GLU C 143 6921 7679 8791 1219 385 -671 C
ATOM 5700 OE1 GLU C 143 39.991 25.617 9.196 1.00 63.59 O
ANISOU 5700 OE1 GLU C 143 7139 7878 9143 1185 234 -703 O
ATOM 5701 OE2 GLU C 143 38.390 25.414 7.716 1.00 63.84 O
ANISOU 5701 OE2 GLU C 143 7407 8002 8849 1211 377 -701 O
ATOM 5702 N GLU C 144 39.167 30.406 11.281 1.00 36.13 N
ANISOU 5702 N GLU C 144 5252 3887 4589 -215 -587 -1015 N
ATOM 5703 CA GLU C 144 39.669 30.959 12.528 1.00 32.70 C
ANISOU 5703 CA GLU C 144 4751 3401 4274 -326 -585 -1066 C
ATOM 5704 C GLU C 144 39.030 30.258 13.719 1.00 30.85 C
ANISOU 5704 C GLU C 144 4444 3162 4115 -230 -698 -1162 C
ATOM 5705 O GLU C 144 37.883 29.807 13.663 1.00 36.06 O
ANISOU 5705 O GLU C 144 5151 3787 4763 -99 -778 -1164 O
ATOM 5706 CB GLU C 144 39.411 32.465 12.590 1.00 40.32 C
ANISOU 5706 CB GLU C 144 5866 4180 5274 -417 -569 -985 C
ATOM 5707 CG GLU C 144 39.954 33.226 11.387 1.00 55.87 C
ANISOU 5707 CG GLU C 144 7947 6127 7154 -527 -454 -863 C
ATOM 5708 CD GLU C 144 40.131 34.704 11.657 1.00 72.04 C
ANISOU 5708 CD GLU C 144 10107 7995 9269 -671 -430 -796 C
ATOM 5709 OE1 GLU C 144 40.495 35.059 12.795 1.00 76.12 O
ANISOU 5709 OE1 GLU C 144 10537 8472 9914 -740 -453 -872 O
ATOM 5710 OE2 GLU C 144 39.906 35.514 10.733 1.00 77.99 O
ANISOU 5710 OE2 GLU C 144 11046 8640 9947 -711 -398 -668 O
ATOM 5711 N LYS C 145 39.790 30.165 14.804 1.00 33.77 N
ANISOU 5711 N LYS C 145 4701 3568 4563 -302 -703 -1244 N
ATOM 5712 CA LYS C 145 39.352 29.416 15.975 1.00 32.10 C
ANISOU 5712 CA LYS C 145 4428 3369 4398 -228 -799 -1328 C
ATOM 5713 C LYS C 145 38.492 30.306 16.864 1.00 34.86 C
ANISOU 5713 C LYS C 145 4865 3576 4806 -229 -841 -1332 C
ATOM 5714 O LYS C 145 38.945 31.361 17.321 1.00 35.65 O
ANISOU 5714 O LYS C 145 4986 3598 4961 -331 -816 -1335 O
ATOM 5715 CB LYS C 145 40.560 28.878 16.737 1.00 32.32 C
ANISOU 5715 CB LYS C 145 4313 3498 4469 -285 -808 -1424 C
ATOM 5716 CG LYS C 145 41.482 28.047 15.864 1.00 41.61 C
ANISOU 5716 CG LYS C 145 5383 4825 5601 -282 -770 -1450 C
ATOM 5717 CD LYS C 145 42.503 27.286 16.683 1.00 49.18 C
ANISOU 5717 CD LYS C 145 6195 5880 6611 -294 -825 -1572 C
ATOM 5718 CE LYS C 145 43.488 26.569 15.782 1.00 54.58 C
ANISOU 5718 CE LYS C 145 6754 6720 7263 -292 -784 -1623 C
ATOM 5719 NZ LYS C 145 42.782 25.777 14.744 1.00 51.21 N
ANISOU 5719 NZ LYS C 145 6365 6344 6748 -171 -797 -1577 N
ATOM 5720 N LEU C 146 37.254 29.873 17.110 1.00 30.62 N
ANISOU 5720 N LEU C 146 4366 3006 4264 -116 -906 -1344 N
ATOM 5721 CA LEU C 146 36.308 30.674 17.879 1.00 29.64 C
ANISOU 5721 CA LEU C 146 4312 2761 4190 -100 -942 -1367 C
ATOM 5722 C LEU C 146 36.544 30.539 19.379 1.00 26.52 C
ANISOU 5722 C LEU C 146 3846 2409 3820 -132 -944 -1419 C
ATOM 5723 O LEU C 146 36.529 31.541 20.103 1.00 28.87 O
ANISOU 5723 O LEU C 146 4173 2642 4155 -180 -931 -1428 O
ATOM 5724 CB LEU C 146 34.880 30.272 17.515 1.00 27.17 C
ANISOU 5724 CB LEU C 146 4043 2416 3864 30 -989 -1362 C
ATOM 5725 CG LEU C 146 34.513 30.592 16.066 1.00 30.90 C
ANISOU 5725 CG LEU C 146 4610 2839 4293 81 -987 -1284 C
ATOM 5726 CD1 LEU C 146 33.237 29.884 15.654 1.00 31.03 C
ANISOU 5726 CD1 LEU C 146 4633 2851 4305 223 -1050 -1304 C
ATOM 5727 CD2 LEU C 146 34.366 32.089 15.906 1.00 36.14 C
ANISOU 5727 CD2 LEU C 146 5395 3353 4985 33 -985 -1244 C
ATOM 5728 N PHE C 147 36.762 29.318 19.855 1.00 26.67 N
ANISOU 5728 N PHE C 147 3781 2552 3802 -100 -947 -1420 N
ATOM 5729 CA PHE C 147 37.126 29.050 21.243 1.00 24.74 C
ANISOU 5729 CA PHE C 147 3488 2368 3546 -125 -939 -1431 C
ATOM 5730 C PHE C 147 37.614 27.607 21.320 1.00 26.89 C
ANISOU 5730 C PHE C 147 3688 2751 3779 -90 -964 -1424 C
ATOM 5731 O PHE C 147 37.576 26.864 20.334 1.00 25.34 O
ANISOU 5731 O PHE C 147 3468 2591 3570 -41 -984 -1415 O
ATOM 5732 CB PHE C 147 35.956 29.310 22.198 1.00 24.52 C
ANISOU 5732 CB PHE C 147 3495 2315 3505 -89 -920 -1417 C
ATOM 5733 CG PHE C 147 34.734 28.479 21.912 1.00 25.66 C
ANISOU 5733 CG PHE C 147 3637 2482 3630 -6 -920 -1384 C
ATOM 5734 CD1 PHE C 147 34.615 27.198 22.428 1.00 23.25 C
ANISOU 5734 CD1 PHE C 147 3294 2255 3287 20 -930 -1368 C
ATOM 5735 CD2 PHE C 147 33.701 28.981 21.132 1.00 23.88 C
ANISOU 5735 CD2 PHE C 147 3451 2191 3432 47 -919 -1372 C
ATOM 5736 CE1 PHE C 147 33.496 26.430 22.170 1.00 25.95 C
ANISOU 5736 CE1 PHE C 147 3624 2606 3629 82 -932 -1346 C
ATOM 5737 CE2 PHE C 147 32.577 28.217 20.871 1.00 23.37 C
ANISOU 5737 CE2 PHE C 147 3366 2149 3366 123 -923 -1354 C
ATOM 5738 CZ PHE C 147 32.477 26.939 21.391 1.00 25.61 C
ANISOU 5738 CZ PHE C 147 3599 2508 3622 134 -925 -1343 C
ATOM 5739 N CYS C 148 38.067 27.211 22.507 1.00 30.44 N
ANISOU 5739 N CYS C 148 4112 3248 4206 -104 -975 -1431 N
ATOM 5740 CA CYS C 148 38.626 25.876 22.707 1.00 29.70 C
ANISOU 5740 CA CYS C 148 3965 3239 4082 -69 -1016 -1421 C
ATOM 5741 C CYS C 148 38.369 25.473 24.149 1.00 32.42 C
ANISOU 5741 C CYS C 148 4343 3593 4381 -65 -1029 -1407 C
ATOM 5742 O CYS C 148 38.794 26.178 25.071 1.00 31.84 O
ANISOU 5742 O CYS C 148 4289 3504 4306 -109 -1026 -1438 O
ATOM 5743 CB CYS C 148 40.123 25.864 22.390 1.00 38.56 C
ANISOU 5743 CB CYS C 148 5010 4410 5232 -109 -1036 -1475 C
ATOM 5744 SG CYS C 148 40.940 24.250 22.501 1.00 51.59 S
ANISOU 5744 SG CYS C 148 6585 6157 6860 -45 -1101 -1474 S
ATOM 5745 N LEU C 149 37.679 24.356 24.354 1.00 24.83 N
ANISOU 5745 N LEU C 149 3397 2652 3385 -17 -1050 -1367 N
ATOM 5746 CA LEU C 149 37.384 23.857 25.689 1.00 25.83 C
ANISOU 5746 CA LEU C 149 3577 2782 3455 -25 -1066 -1359 C
ATOM 5747 C LEU C 149 38.122 22.550 25.930 1.00 28.47 C
ANISOU 5747 C LEU C 149 3895 3157 3765 5 -1138 -1340 C
ATOM 5748 O LEU C 149 38.197 21.699 25.040 1.00 28.73 O
ANISOU 5748 O LEU C 149 3883 3211 3822 53 -1167 -1316 O
ATOM 5749 CB LEU C 149 35.879 23.648 25.879 1.00 26.43 C
ANISOU 5749 CB LEU C 149 3699 2831 3514 -14 -1032 -1341 C
ATOM 5750 CG LEU C 149 35.054 24.920 25.702 1.00 28.89 C
ANISOU 5750 CG LEU C 149 4025 3096 3857 -26 -968 -1367 C
ATOM 5751 CD1 LEU C 149 33.580 24.645 25.924 1.00 29.04 C
ANISOU 5751 CD1 LEU C 149 4068 3096 3869 -10 -934 -1371 C
ATOM 5752 CD2 LEU C 149 35.553 26.005 26.640 1.00 29.80 C
ANISOU 5752 CD2 LEU C 149 4170 3197 3957 -72 -953 -1413 C
ATOM 5753 N ASN C 150 38.671 22.400 27.135 1.00 30.18 N
ANISOU 5753 N ASN C 150 4153 3379 3934 -13 -1177 -1356 N
ATOM 5754 CA ASN C 150 39.400 21.197 27.541 1.00 29.10 C
ANISOU 5754 CA ASN C 150 4021 3263 3774 24 -1262 -1342 C
ATOM 5755 C ASN C 150 38.504 20.425 28.504 1.00 31.43 C
ANISOU 5755 C ASN C 150 4421 3530 3992 15 -1287 -1310 C
ATOM 5756 O ASN C 150 38.389 20.792 29.676 1.00 25.47 O
ANISOU 5756 O ASN C 150 3745 2764 3169 -21 -1287 -1335 O
ATOM 5757 CB ASN C 150 40.737 21.555 28.192 1.00 34.72 C
ANISOU 5757 CB ASN C 150 4710 3991 4489 17 -1306 -1393 C
ATOM 5758 CG ASN C 150 41.661 20.349 28.352 1.00 39.41 C
ANISOU 5758 CG ASN C 150 5287 4602 5085 76 -1405 -1390 C
ATOM 5759 OD1 ASN C 150 41.204 19.227 28.576 1.00 35.98 O
ANISOU 5759 OD1 ASN C 150 4910 4147 4614 108 -1455 -1343 O
ATOM 5760 ND2 ASN C 150 42.963 20.577 28.225 1.00 56.05 N
ANISOU 5760 ND2 ASN C 150 7313 6737 7244 91 -1437 -1449 N
ATOM 5761 N PHE C 151 37.882 19.355 28.017 1.00 28.82 N
ANISOU 5761 N PHE C 151 4096 3186 3669 44 -1314 -1264 N
ATOM 5762 CA PHE C 151 36.924 18.597 28.812 1.00 30.71 C
ANISOU 5762 CA PHE C 151 4440 3387 3840 16 -1337 -1239 C
ATOM 5763 C PHE C 151 37.587 17.424 29.523 1.00 33.20 C
ANISOU 5763 C PHE C 151 4823 3682 4108 41 -1453 -1212 C
ATOM 5764 O PHE C 151 38.570 16.851 29.047 1.00 37.37 O
ANISOU 5764 O PHE C 151 5292 4222 4686 103 -1518 -1204 O
ATOM 5765 CB PHE C 151 35.773 18.074 27.945 1.00 24.95 C
ANISOU 5765 CB PHE C 151 3687 2636 3158 27 -1312 -1209 C
ATOM 5766 CG PHE C 151 34.679 19.076 27.709 1.00 31.92 C
ANISOU 5766 CG PHE C 151 4555 3511 4061 -5 -1209 -1242 C
ATOM 5767 CD1 PHE C 151 33.663 19.241 28.636 1.00 28.81 C
ANISOU 5767 CD1 PHE C 151 4243 3093 3609 -66 -1166 -1274 C
ATOM 5768 CD2 PHE C 151 34.657 19.842 26.555 1.00 35.85 C
ANISOU 5768 CD2 PHE C 151 4964 4023 4633 30 -1160 -1249 C
ATOM 5769 CE1 PHE C 151 32.653 20.161 28.423 1.00 28.99 C
ANISOU 5769 CE1 PHE C 151 4240 3108 3666 -81 -1073 -1320 C
ATOM 5770 CE2 PHE C 151 33.648 20.762 26.336 1.00 37.28 C
ANISOU 5770 CE2 PHE C 151 5137 4185 4841 17 -1081 -1279 C
ATOM 5771 CZ PHE C 151 32.645 20.921 27.271 1.00 34.20 C
ANISOU 5771 CZ PHE C 151 4809 3773 4411 -33 -1036 -1317 C
ATOM 5772 N THR C 152 37.025 17.069 30.676 1.00 27.36 N
ANISOU 5772 N THR C 152 4221 2906 3268 -7 -1481 -1203 N
ATOM 5773 CA THR C 152 37.419 15.883 31.425 1.00 31.36 C
ANISOU 5773 CA THR C 152 4840 3365 3712 10 -1607 -1163 C
ATOM 5774 C THR C 152 36.155 15.127 31.796 1.00 34.27 C
ANISOU 5774 C THR C 152 5335 3671 4013 -55 -1620 -1124 C
ATOM 5775 O THR C 152 35.264 15.689 32.441 1.00 40.27 O
ANISOU 5775 O THR C 152 6176 4432 4693 -132 -1546 -1154 O
ATOM 5776 CB THR C 152 38.213 16.247 32.683 1.00 35.90 C
ANISOU 5776 CB THR C 152 5501 3944 4195 8 -1655 -1194 C
ATOM 5777 OG1 THR C 152 39.510 16.738 32.315 1.00 38.41 O
ANISOU 5777 OG1 THR C 152 5698 4304 4594 66 -1668 -1235 O
ATOM 5778 CG2 THR C 152 38.365 15.035 33.588 1.00 39.57 C
ANISOU 5778 CG2 THR C 152 6133 4336 4565 17 -1793 -1143 C
ATOM 5779 N ILE C 153 36.071 13.867 31.380 1.00 28.09 N
ANISOU 5779 N ILE C 153 4573 2832 3269 -28 -1712 -1065 N
ATOM 5780 CA ILE C 153 34.952 12.997 31.719 1.00 29.91 C
ANISOU 5780 CA ILE C 153 4940 2980 3446 -107 -1747 -1019 C
ATOM 5781 C ILE C 153 35.507 11.746 32.387 1.00 37.60 C
ANISOU 5781 C ILE C 153 6066 3864 4355 -91 -1914 -948 C
ATOM 5782 O ILE C 153 36.379 11.072 31.827 1.00 37.16 O
ANISOU 5782 O ILE C 153 5936 3794 4389 9 -2004 -930 O
ATOM 5783 CB ILE C 153 34.110 12.622 30.482 1.00 36.38 C
ANISOU 5783 CB ILE C 153 5642 3785 4394 -97 -1712 -1010 C
ATOM 5784 CG1 ILE C 153 33.536 13.872 29.805 1.00 38.91 C
ANISOU 5784 CG1 ILE C 153 5829 4177 4778 -100 -1561 -1076 C
ATOM 5785 CG2 ILE C 153 32.980 11.688 30.873 1.00 35.85 C
ANISOU 5785 CG2 ILE C 153 5716 3615 4290 -201 -1755 -967 C
ATOM 5786 CD1 ILE C 153 34.362 14.383 28.645 1.00 38.11 C
ANISOU 5786 CD1 ILE C 153 5558 4145 4776 2 -1533 -1089 C
ATOM 5787 N ILE C 154 35.006 11.440 33.581 1.00 37.30 N
ANISOU 5787 N ILE C 154 6260 3760 4154 -193 -1953 -911 N
ATOM 5788 CA ILE C 154 35.394 10.246 34.322 1.00 37.83 C
ANISOU 5788 CA ILE C 154 6529 3714 4132 -198 -2124 -825 C
ATOM 5789 C ILE C 154 34.177 9.334 34.383 1.00 41.17 C
ANISOU 5789 C ILE C 154 7108 4025 4508 -334 -2153 -752 C
ATOM 5790 O ILE C 154 33.214 9.608 35.111 1.00 43.18 O
ANISOU 5790 O ILE C 154 7531 4263 4613 -492 -2069 -746 O
ATOM 5791 CB ILE C 154 35.918 10.583 35.724 1.00 40.94 C
ANISOU 5791 CB ILE C 154 7111 4105 4340 -215 -2160 -823 C
ATOM 5792 CG1 ILE C 154 37.117 11.530 35.619 1.00 34.81 C
ANISOU 5792 CG1 ILE C 154 6156 3429 3642 -97 -2130 -909 C
ATOM 5793 CG2 ILE C 154 36.285 9.306 36.476 1.00 42.60 C
ANISOU 5793 CG2 ILE C 154 7561 4176 4450 -219 -2352 -722 C
ATOM 5794 CD1 ILE C 154 37.892 11.699 36.907 1.00 44.31 C
ANISOU 5794 CD1 ILE C 154 7511 4617 4706 -72 -2207 -915 C
ATOM 5795 N HIS C 155 34.220 8.256 33.606 1.00 43.13 N
ANISOU 5795 N HIS C 155 7302 4197 4887 -285 -2261 -703 N
ATOM 5796 CA HIS C 155 33.123 7.305 33.508 1.00 45.30 C
ANISOU 5796 CA HIS C 155 7694 4348 5169 -418 -2304 -634 C
ATOM 5797 C HIS C 155 33.243 6.278 34.627 1.00 48.29 C
ANISOU 5797 C HIS C 155 8395 4576 5376 -511 -2469 -519 C
ATOM 5798 O HIS C 155 34.325 5.720 34.840 1.00 45.15 O
ANISOU 5798 O HIS C 155 8041 4134 4982 -386 -2624 -486 O
ATOM 5799 CB HIS C 155 33.145 6.623 32.141 1.00 39.26 C
ANISOU 5799 CB HIS C 155 6719 3571 4629 -306 -2354 -638 C
ATOM 5800 CG HIS C 155 31.972 5.731 31.887 1.00 37.57 C
ANISOU 5800 CG HIS C 155 6565 3231 4479 -435 -2384 -583 C
ATOM 5801 ND1 HIS C 155 30.797 5.823 32.601 1.00 37.16 N
ANISOU 5801 ND1 HIS C 155 6626 3147 4345 -633 -2222 -519 N
ATOM 5802 CD2 HIS C 155 31.794 4.728 30.995 1.00 35.02 C
ANISOU 5802 CD2 HIS C 155 6149 2838 4320 -376 -2477 -553 C
ATOM 5803 CE1 HIS C 155 29.946 4.914 32.159 1.00 38.76 C
ANISOU 5803 CE1 HIS C 155 6797 3255 4675 -704 -2220 -452 C
ATOM 5804 NE2 HIS C 155 30.526 4.237 31.184 1.00 38.18 N
ANISOU 5804 NE2 HIS C 155 6644 3115 4747 -570 -2444 -505 N
ATOM 5805 N ARG C 156 32.125 6.026 35.316 1.00 55.29 N
ANISOU 5805 N ARG C 156 9434 5417 6155 -704 -2331 -412 N
ATOM 5806 CA ARG C 156 32.046 5.272 36.579 1.00 60.38 C
ANISOU 5806 CA ARG C 156 10398 5955 6589 -828 -2377 -257 C
ATOM 5807 C ARG C 156 32.459 6.169 37.742 1.00 64.86 C
ANISOU 5807 C ARG C 156 11111 6613 6920 -834 -2307 -280 C
ATOM 5808 O ARG C 156 31.738 7.103 38.097 1.00 70.61 O
ANISOU 5808 O ARG C 156 11772 7470 7585 -913 -2043 -304 O
ATOM 5809 CB ARG C 156 32.904 3.997 36.555 1.00 67.85 C
ANISOU 5809 CB ARG C 156 11516 6720 7546 -756 -2718 -205 C
ATOM 5810 CG ARG C 156 32.849 3.161 37.823 1.00 79.83 C
ANISOU 5810 CG ARG C 156 13398 8097 8836 -881 -2794 -29 C
ATOM 5811 CD ARG C 156 31.429 2.735 38.132 1.00 86.89 C
ANISOU 5811 CD ARG C 156 14352 8958 9706 -1112 -2550 130 C
ATOM 5812 NE ARG C 156 31.348 1.913 39.335 1.00 93.25 N
ANISOU 5812 NE ARG C 156 15528 9625 10277 -1253 -2606 320 N
ATOM 5813 CZ ARG C 156 30.207 1.577 39.928 1.00 97.54 C
ANISOU 5813 CZ ARG C 156 16187 10144 10727 -1487 -2374 477 C
ATOM 5814 NH1 ARG C 156 29.053 1.999 39.432 1.00 96.54 N
ANISOU 5814 NH1 ARG C 156 15814 10126 10740 -1592 -2080 446 N
ATOM 5815 NH2 ARG C 156 30.216 0.826 41.019 1.00101.36 N
ANISOU 5815 NH2 ARG C 156 17037 10497 10979 -1617 -2435 661 N
TER 5816 ARG C 156
HETATM 5817 C1 NAG B 1 17.110 40.288 -7.308 1.00 44.43 C
HETATM 5818 C2 NAG B 1 17.714 39.706 -8.557 1.00 55.08 C
HETATM 5819 C3 NAG B 1 18.369 38.388 -8.209 1.00 56.33 C
HETATM 5820 C4 NAG B 1 19.485 38.644 -7.205 1.00 55.46 C
HETATM 5821 C5 NAG B 1 19.017 39.489 -6.004 1.00 48.70 C
HETATM 5822 C6 NAG B 1 20.174 40.152 -5.291 1.00 54.89 C
HETATM 5823 C7 NAG B 1 16.804 40.275 -10.758 1.00 75.57 C
HETATM 5824 C8 NAG B 1 17.935 41.264 -10.851 1.00 79.78 C
HETATM 5825 N2 NAG B 1 16.743 39.556 -9.628 1.00 66.07 N
HETATM 5826 O3 NAG B 1 18.885 37.765 -9.380 1.00 58.97 O
HETATM 5827 O4 NAG B 1 20.012 37.403 -6.746 1.00 57.47 O
HETATM 5828 O5 NAG B 1 18.136 40.571 -6.375 1.00 44.02 O
HETATM 5829 O6 NAG B 1 20.931 39.243 -4.506 1.00 70.26 O
HETATM 5830 O7 NAG B 1 15.988 40.139 -11.661 1.00 75.47 O
HETATM 5831 C1 NAG B 2 21.006 36.419 -7.039 1.00 67.34 C
HETATM 5832 C2 NAG B 2 21.269 35.365 -5.977 1.00 66.73 C
HETATM 5833 C3 NAG B 2 22.705 34.868 -6.087 1.00 77.32 C
HETATM 5834 C4 NAG B 2 22.972 34.350 -7.494 1.00 82.17 C
HETATM 5835 C5 NAG B 2 22.603 35.404 -8.538 1.00 80.58 C
HETATM 5836 C6 NAG B 2 22.648 34.867 -9.949 1.00 79.94 C
HETATM 5837 C7 NAG B 2 19.814 35.762 -4.042 1.00 43.81 C
HETATM 5838 C8 NAG B 2 19.712 36.350 -2.667 1.00 40.14 C
HETATM 5839 N2 NAG B 2 21.002 35.881 -4.644 1.00 50.11 N
HETATM 5840 O3 NAG B 2 22.930 33.834 -5.135 1.00 82.71 O
HETATM 5841 O4 NAG B 2 24.347 34.009 -7.630 1.00 83.60 O
HETATM 5842 O5 NAG B 2 21.259 35.869 -8.331 1.00 75.54 O
HETATM 5843 O6 NAG B 2 21.350 34.495 -10.391 1.00 77.35 O
HETATM 5844 O7 NAG B 2 18.864 35.205 -4.583 1.00 44.36 O
HETATM 5845 C1 NAG D 1 5.858 31.708 21.959 1.00 49.00 C
HETATM 5846 C2 NAG D 1 5.993 31.332 23.399 1.00 53.61 C
HETATM 5847 C3 NAG D 1 5.812 32.572 24.244 1.00 55.82 C
HETATM 5848 C4 NAG D 1 6.888 33.588 23.882 1.00 59.82 C
HETATM 5849 C5 NAG D 1 7.056 33.789 22.361 1.00 55.87 C
HETATM 5850 C6 NAG D 1 8.429 34.329 22.017 1.00 55.51 C
HETATM 5851 C7 NAG D 1 5.509 29.093 24.245 1.00 53.46 C
HETATM 5852 C8 NAG D 1 4.450 28.109 24.636 1.00 52.28 C
HETATM 5853 N2 NAG D 1 5.077 30.279 23.798 1.00 55.89 N
HETATM 5854 O3 NAG D 1 5.886 32.221 25.622 1.00 55.90 O
HETATM 5855 O4 NAG D 1 6.583 34.843 24.482 1.00 66.80 O
HETATM 5856 O5 NAG D 1 6.916 32.570 21.599 1.00 49.41 O
HETATM 5857 O6 NAG D 1 8.434 35.102 20.825 1.00 54.82 O
HETATM 5858 O7 NAG D 1 6.706 28.828 24.323 1.00 50.14 O
HETATM 5859 C1 NAG D 2 7.527 35.808 24.962 1.00 58.94 C
HETATM 5860 C2 NAG D 2 7.067 37.229 25.293 1.00 56.34 C
HETATM 5861 C3 NAG D 2 8.167 37.986 26.033 1.00 57.28 C
HETATM 5862 C4 NAG D 2 8.608 37.194 27.255 1.00 59.82 C
HETATM 5863 C5 NAG D 2 9.058 35.807 26.816 1.00 60.16 C
HETATM 5864 C6 NAG D 2 9.468 34.920 27.968 1.00 56.19 C
HETATM 5865 C7 NAG D 2 5.441 37.908 23.585 1.00 53.16 C
HETATM 5866 C8 NAG D 2 5.218 38.695 22.331 1.00 48.67 C
HETATM 5867 N2 NAG D 2 6.681 37.940 24.085 1.00 54.25 N
HETATM 5868 O3 NAG D 2 7.691 39.268 26.428 1.00 60.59 O
HETATM 5869 O4 NAG D 2 9.649 37.865 27.958 1.00 66.80 O
HETATM 5870 O5 NAG D 2 7.965 35.150 26.158 1.00 61.34 O
HETATM 5871 O6 NAG D 2 9.723 33.593 27.530 1.00 49.79 O
HETATM 5872 O7 NAG D 2 4.540 37.271 24.123 1.00 60.08 O
HETATM 5873 C1 NAG D 3 9.591 38.739 29.128 1.00 66.74 C
HETATM 5874 C2 NAG D 3 10.498 39.044 30.327 1.00 70.04 C
HETATM 5875 C3 NAG D 3 9.693 39.705 31.444 1.00 68.55 C
HETATM 5876 C4 NAG D 3 8.982 40.939 30.912 1.00 65.28 C
HETATM 5877 C5 NAG D 3 8.106 40.551 29.725 1.00 58.97 C
HETATM 5878 C6 NAG D 3 7.406 41.730 29.089 1.00 55.51 C
HETATM 5879 C7 NAG D 3 12.109 37.838 31.745 1.00 69.09 C
HETATM 5880 C8 NAG D 3 12.666 36.499 32.114 1.00 64.32 C
HETATM 5881 N2 NAG D 3 11.153 37.837 30.808 1.00 71.15 N
HETATM 5882 O3 NAG D 3 10.556 40.071 32.514 1.00 75.03 O
HETATM 5883 O4 NAG D 3 8.195 41.521 31.945 1.00 69.65 O
HETATM 5884 O5 NAG D 3 8.919 39.947 28.707 1.00 64.92 O
HETATM 5885 O6 NAG D 3 6.221 41.325 28.417 1.00 52.47 O
HETATM 5886 O7 NAG D 3 12.504 38.876 32.276 1.00 72.21 O
HETATM 5887 C1 NAG A 701 41.137 5.503 -29.314 1.00 61.23 C
HETATM 5888 C2 NAG A 701 41.685 6.283 -30.504 1.00 66.19 C
HETATM 5889 C3 NAG A 701 41.482 5.488 -31.783 1.00 66.11 C
HETATM 5890 C4 NAG A 701 42.132 4.117 -31.658 1.00 71.30 C
HETATM 5891 C5 NAG A 701 41.606 3.383 -30.424 1.00 65.31 C
HETATM 5892 C6 NAG A 701 42.321 2.073 -30.164 1.00 64.94 C
HETATM 5893 C7 NAG A 701 41.300 8.596 -29.762 1.00 78.77 C
HETATM 5894 C8 NAG A 701 40.609 9.893 -30.059 1.00 79.68 C
HETATM 5895 N2 NAG A 701 41.072 7.601 -30.624 1.00 72.77 N
HETATM 5896 O3 NAG A 701 42.024 6.198 -32.890 1.00 56.80 O
HETATM 5897 O4 NAG A 701 41.831 3.360 -32.823 1.00 77.39 O
HETATM 5898 O5 NAG A 701 41.782 4.197 -29.253 1.00 60.46 O
HETATM 5899 O6 NAG A 701 41.431 0.965 -30.115 1.00 65.93 O
HETATM 5900 O7 NAG A 701 42.029 8.458 -28.786 1.00 81.86 O
HETATM 5901 C1 NAG A 702 49.602 15.838 -4.968 1.00 43.59 C
HETATM 5902 C2 NAG A 702 49.124 17.287 -4.816 1.00 51.68 C
HETATM 5903 C3 NAG A 702 49.116 17.706 -3.342 1.00 49.05 C
HETATM 5904 C4 NAG A 702 48.402 16.677 -2.475 1.00 45.61 C
HETATM 5905 C5 NAG A 702 48.983 15.294 -2.733 1.00 47.00 C
HETATM 5906 C6 NAG A 702 48.298 14.195 -1.954 1.00 51.62 C
HETATM 5907 C7 NAG A 702 49.507 19.096 -6.442 1.00 57.92 C
HETATM 5908 C8 NAG A 702 48.017 19.173 -6.580 1.00 56.11 C
HETATM 5909 N2 NAG A 702 49.974 18.180 -5.588 1.00 55.63 N
HETATM 5910 O3 NAG A 702 48.467 18.967 -3.223 1.00 52.31 O
HETATM 5911 O4 NAG A 702 48.561 17.005 -1.099 1.00 47.48 O
HETATM 5912 O5 NAG A 702 48.832 14.983 -4.123 1.00 45.21 O
HETATM 5913 O6 NAG A 702 46.900 14.422 -1.834 1.00 60.03 O
HETATM 5914 O7 NAG A 702 50.257 19.832 -7.075 1.00 56.01 O
HETATM 5915 C02 ZKM A 703 26.604 12.026 7.664 1.00125.94 C
ANISOU 5915 C02 ZKM A 703 16170 15888 15792 196 -673 205 C
HETATM 5916 C03 ZKM A 703 26.994 13.403 7.266 1.00135.69 C
ANISOU 5916 C03 ZKM A 703 17403 17131 17022 216 -630 207 C
HETATM 5917 C09 ZKM A 703 25.937 14.337 7.680 1.00133.29 C
ANISOU 5917 C09 ZKM A 703 17067 16842 16735 224 -611 258 C
HETATM 5918 C11 ZKM A 703 25.855 14.356 9.204 1.00127.71 C
ANISOU 5918 C11 ZKM A 703 16342 16126 16055 232 -594 263 C
HETATM 5919 C12 ZKM A 703 24.674 15.149 9.638 1.00122.76 C
ANISOU 5919 C12 ZKM A 703 15682 15515 15446 236 -581 317 C
HETATM 5920 C15 ZKM A 703 26.617 11.967 9.193 1.00122.14 C
ANISOU 5920 C15 ZKM A 703 15674 15396 15337 204 -656 206 C
HETATM 5921 C17 ZKM A 703 25.182 10.668 10.519 1.00110.78 C
ANISOU 5921 C17 ZKM A 703 14209 13957 13927 181 -701 245 C
HETATM 5922 C18 ZKM A 703 25.794 10.708 11.920 1.00105.90 C
ANISOU 5922 C18 ZKM A 703 13585 13322 13329 195 -675 226 C
HETATM 5923 C20 ZKM A 703 27.301 8.690 12.134 1.00 98.92 C
ANISOU 5923 C20 ZKM A 703 12746 12407 12433 180 -713 146 C
HETATM 5924 C21 ZKM A 703 27.527 7.291 12.723 1.00 95.68 C
ANISOU 5924 C21 ZKM A 703 12347 11981 12027 165 -746 122 C
HETATM 5925 C22 ZKM A 703 27.171 7.357 14.219 1.00 91.02 C
ANISOU 5925 C22 ZKM A 703 11734 11385 11466 172 -731 138 C
HETATM 5926 C23 ZKM A 703 28.211 8.140 15.024 1.00 82.53 C
ANISOU 5926 C23 ZKM A 703 10661 10297 10400 197 -683 111 C
HETATM 5927 C24 ZKM A 703 29.231 7.203 15.705 1.00 74.33 C
ANISOU 5927 C24 ZKM A 703 9643 9236 9364 196 -689 63 C
HETATM 5928 C25 ZKM A 703 29.867 7.871 16.946 1.00 68.61 C
ANISOU 5928 C25 ZKM A 703 8909 8500 8660 218 -645 50 C
HETATM 5929 C26 ZKM A 703 30.256 6.835 18.029 1.00 65.38 C
ANISOU 5929 C26 ZKM A 703 8506 8073 8264 213 -658 24 C
HETATM 5930 C27 ZKM A 703 30.506 7.496 19.399 1.00 69.39 C
ANISOU 5930 C27 ZKM A 703 8996 8572 8795 234 -618 25 C
HETATM 5931 C28 ZKM A 703 31.221 8.844 19.278 1.00 73.19 C
ANISOU 5931 C28 ZKM A 703 9479 9055 9275 258 -569 15 C
HETATM 5932 C29 ZKM A 703 31.692 9.368 20.637 1.00 75.07 C
ANISOU 5932 C29 ZKM A 703 9706 9282 9536 278 -530 6 C
HETATM 5933 C30 ZKM A 703 33.210 9.183 20.808 1.00 76.89 C
ANISOU 5933 C30 ZKM A 703 9962 9492 9759 289 -513 -52 C
HETATM 5934 C31 ZKM A 703 33.561 8.468 22.126 1.00 79.45 C
ANISOU 5934 C31 ZKM A 703 10287 9799 10102 290 -514 -72 C
HETATM 5935 C32 ZKM A 703 34.484 7.263 21.895 1.00 78.00 C
ANISOU 5935 C32 ZKM A 703 10134 9599 9904 279 -541 -121 C
HETATM 5936 C33 ZKM A 703 35.004 6.646 23.192 1.00 78.72 C
ANISOU 5936 C33 ZKM A 703 10227 9671 10013 283 -537 -146 C
HETATM 5937 C34 ZKM A 703 36.066 5.584 22.924 1.00 79.79 C
ANISOU 5937 C34 ZKM A 703 10394 9788 10133 274 -558 -198 C
HETATM 5938 C35 ZKM A 703 35.513 4.166 23.049 1.00 74.82 C
ANISOU 5938 C35 ZKM A 703 9768 9156 9504 250 -607 -195 C
HETATM 5939 C37 ZKM A 703 24.871 11.440 12.883 1.00103.41 C
ANISOU 5939 C37 ZKM A 703 13237 13016 13039 204 -654 270 C
HETATM 5940 C39 ZKM A 703 25.740 12.187 13.911 1.00100.35 C
ANISOU 5940 C39 ZKM A 703 12847 12617 12667 228 -606 249 C
HETATM 5941 C40 ZKM A 703 26.725 11.546 14.561 1.00 94.85 C
ANISOU 5941 C40 ZKM A 703 12167 11900 11973 231 -605 206 C
HETATM 5942 C41 ZKM A 703 27.592 12.306 15.588 1.00 87.55 C
ANISOU 5942 C41 ZKM A 703 11238 10963 11063 255 -557 185 C
HETATM 5943 C42 ZKM A 703 27.493 11.616 16.966 1.00 79.45 C
ANISOU 5943 C42 ZKM A 703 10203 9924 10059 253 -563 183 C
HETATM 5944 C43 ZKM A 703 28.818 11.687 17.764 1.00 72.26 C
ANISOU 5944 C43 ZKM A 703 9307 8994 9156 270 -533 136 C
HETATM 5945 C44 ZKM A 703 29.072 13.088 18.374 1.00 66.09 C
ANISOU 5945 C44 ZKM A 703 8509 8215 8388 296 -480 145 C
HETATM 5946 C45 ZKM A 703 30.142 13.047 19.487 1.00 63.63 C
ANISOU 5946 C45 ZKM A 703 8205 7882 8089 311 -453 106 C
HETATM 5947 C46 ZKM A 703 29.991 14.170 20.532 1.00 63.33 C
ANISOU 5947 C46 ZKM A 703 8142 7846 8074 333 -409 127 C
HETATM 5948 C47 ZKM A 703 31.333 14.518 21.190 1.00 60.75 C
ANISOU 5948 C47 ZKM A 703 7828 7501 7751 354 -371 83 C
HETATM 5949 C48 ZKM A 703 31.399 14.095 22.667 1.00 60.13 C
ANISOU 5949 C48 ZKM A 703 7739 7409 7697 358 -366 77 C
HETATM 5950 C49 ZKM A 703 32.734 13.408 23.018 1.00 59.16 C
ANISOU 5950 C49 ZKM A 703 7644 7265 7571 361 -364 20 C
HETATM 5951 C50 ZKM A 703 32.520 12.129 23.844 1.00 52.93 C
ANISOU 5951 C50 ZKM A 703 6855 6464 6792 346 -397 14 C
HETATM 5952 C51 ZKM A 703 33.561 11.958 24.956 1.00 45.31 C
ANISOU 5952 C51 ZKM A 703 5898 5479 5840 360 -374 -25 C
HETATM 5953 C52 ZKM A 703 32.920 11.470 26.246 1.00 41.85 C
ANISOU 5953 C52 ZKM A 703 5440 5035 5426 356 -383 -5 C
HETATM 5954 C53 ZKM A 703 33.087 9.970 26.443 1.00 40.33 C
ANISOU 5954 C53 ZKM A 703 5263 4830 5230 337 -424 -29 C
HETATM 5955 N19 ZKM A 703 26.035 9.367 12.438 1.00102.54 N
ANISOU 5955 N19 ZKM A 703 13172 12882 12907 181 -706 202 N
HETATM 5956 O01 ZKM A 703 27.531 11.079 7.119 1.00121.48 O
ANISOU 5956 O01 ZKM A 703 15637 15311 15209 186 -695 159 O
HETATM 5957 O04 ZKM A 703 27.256 13.476 5.830 1.00146.14 O
ANISOU 5957 O04 ZKM A 703 18746 18462 18320 211 -641 196 O
HETATM 5958 O06 ZKM A 703 29.133 15.156 5.248 1.00153.27 O1-
ANISOU 5958 O06 ZKM A 703 19672 19358 19207 248 -569 147 O1-
HETATM 5959 O07 ZKM A 703 29.279 12.858 4.295 1.00151.67 O
ANISOU 5959 O07 ZKM A 703 19504 19145 18979 210 -649 112 O
HETATM 5960 O08 ZKM A 703 29.730 13.131 6.566 1.00153.72 O
ANISOU 5960 O08 ZKM A 703 19744 19386 19276 231 -608 102 O
HETATM 5961 O10 ZKM A 703 24.673 13.857 7.158 1.00135.32 O
ANISOU 5961 O10 ZKM A 703 17312 17114 16989 203 -650 297 O
HETATM 5962 O13 ZKM A 703 24.265 15.962 8.592 1.00118.26 O
ANISOU 5962 O13 ZKM A 703 15109 14962 14863 239 -574 340 O
HETATM 5963 O14 ZKM A 703 25.725 12.978 9.783 1.00126.74 O
ANISOU 5963 O14 ZKM A 703 16224 15992 15939 215 -631 252 O
HETATM 5964 O16 ZKM A 703 26.245 10.699 9.602 1.00115.48 O
ANISOU 5964 O16 ZKM A 703 14832 14546 14499 185 -696 205 O
HETATM 5965 O36 ZKM A 703 28.130 9.217 11.472 1.00 98.70 O
ANISOU 5965 O36 ZKM A 703 12734 12377 12390 190 -693 121 O
HETATM 5966 O38 ZKM A 703 24.088 12.346 12.170 1.00101.82 O
ANISOU 5966 O38 ZKM A 703 13020 12834 12833 206 -645 309 O
HETATM 5967 S05 ZKM A 703 28.852 13.693 5.472 1.00152.14 S
ANISOU 5967 S05 ZKM A 703 19535 19207 19064 225 -615 140 S
HETATM 5968 C02 ZKM A 704 18.152 9.862 17.141 1.00131.84 C
ANISOU 5968 C02 ZKM A 704 16690 16653 16750 152 -745 505 C
HETATM 5969 C03 ZKM A 704 17.040 9.146 16.452 1.00136.09 C
ANISOU 5969 C03 ZKM A 704 17222 17203 17281 128 -791 536 C
HETATM 5970 C09 ZKM A 704 16.126 10.068 15.753 1.00130.78 C
ANISOU 5970 C09 ZKM A 704 16533 16553 16606 130 -784 579 C
HETATM 5971 C11 ZKM A 704 16.870 10.995 14.795 1.00125.91 C
ANISOU 5971 C11 ZKM A 704 15930 15940 15969 143 -757 562 C
HETATM 5972 C12 ZKM A 704 15.919 12.002 14.257 1.00117.33 C
ANISOU 5972 C12 ZKM A 704 14823 14874 14883 147 -746 608 C
HETATM 5973 C15 ZKM A 704 18.889 10.834 16.213 1.00128.26 C
ANISOU 5973 C15 ZKM A 704 16249 16204 16279 166 -717 488 C
HETATM 5974 C17 ZKM A 704 20.436 12.539 16.183 1.00116.01 C
ANISOU 5974 C17 ZKM A 704 14709 14647 14723 203 -643 452 C
HETATM 5975 C18 ZKM A 704 20.123 13.965 16.657 1.00108.45 C
ANISOU 5975 C18 ZKM A 704 13727 13699 13780 224 -598 482 C
HETATM 5976 C20 ZKM A 704 21.774 15.224 15.005 1.00106.14 C
ANISOU 5976 C20 ZKM A 704 13469 13408 13453 246 -556 433 C
HETATM 5977 C21 ZKM A 704 23.051 14.415 15.317 1.00102.61 C
ANISOU 5977 C21 ZKM A 704 13049 12939 13001 247 -559 377 C
HETATM 5978 C22 ZKM A 704 24.327 15.257 15.153 1.00 98.41 C
ANISOU 5978 C22 ZKM A 704 12532 12398 12461 268 -518 340 C
HETATM 5979 C23 ZKM A 704 24.806 15.845 16.482 1.00 90.85 C
ANISOU 5979 C23 ZKM A 704 11563 11430 11525 289 -477 332 C
HETATM 5980 C24 ZKM A 704 26.332 15.683 16.630 1.00 81.47 C
ANISOU 5980 C24 ZKM A 704 10402 10222 10330 300 -459 274 C
HETATM 5981 C25 ZKM A 704 27.094 16.925 16.108 1.00 75.37 C
ANISOU 5981 C25 ZKM A 704 9636 9453 9549 321 -417 260 C
HETATM 5982 C26 ZKM A 704 27.607 17.819 17.263 1.00 73.92 C
ANISOU 5982 C26 ZKM A 704 9440 9262 9385 346 -369 254 C
HETATM 5983 C27 ZKM A 704 27.865 17.018 18.556 1.00 74.85 C
ANISOU 5983 C27 ZKM A 704 9557 9362 9521 344 -374 237 C
HETATM 5984 C28 ZKM A 704 28.574 17.844 19.632 1.00 73.26 C
ANISOU 5984 C28 ZKM A 704 9348 9151 9337 369 -327 223 C
HETATM 5985 C29 ZKM A 704 29.217 19.115 19.066 1.00 70.02 C
ANISOU 5985 C29 ZKM A 704 8942 8745 8917 389 -286 213 C
HETATM 5986 C30 ZKM A 704 30.588 19.415 19.695 1.00 68.07 C
ANISOU 5986 C30 ZKM A 704 8710 8480 8675 409 -250 167 C
HETATM 5987 C31 ZKM A 704 30.740 18.810 21.103 1.00 69.03 C
ANISOU 5987 C31 ZKM A 704 8825 8587 8818 410 -250 157 C
HETATM 5988 C32 ZKM A 704 31.307 19.828 22.101 1.00 71.06 C
ANISOU 5988 C32 ZKM A 704 9071 8837 9093 436 -200 149 C
HETATM 5989 C33 ZKM A 704 30.225 20.468 22.970 1.00 76.19 C
ANISOU 5989 C33 ZKM A 704 9687 9498 9766 442 -185 199 C
HETATM 5990 C34 ZKM A 704 30.794 21.515 23.926 1.00 78.35 C
ANISOU 5990 C34 ZKM A 704 9948 9764 10056 468 -134 192 C
HETATM 5991 C35 ZKM A 704 31.882 22.371 23.278 1.00 75.83 C
ANISOU 5991 C35 ZKM A 704 9646 9442 9722 486 -101 161 C
HETATM 5992 C37 ZKM A 704 20.805 14.249 17.992 1.00 99.25 C
ANISOU 5992 C37 ZKM A 704 12556 12519 12634 242 -564 462 C
HETATM 5993 C39 ZKM A 704 20.878 15.769 18.220 1.00 84.66 C
ANISOU 5993 C39 ZKM A 704 10693 10678 10795 266 -514 478 C
HETATM 5994 C40 ZKM A 704 21.837 16.271 19.008 1.00 69.05 C
ANISOU 5994 C40 ZKM A 704 8720 8689 8828 287 -476 451 C
HETATM 5995 C41 ZKM A 704 21.931 17.791 19.247 1.00 55.25 C
ANISOU 5995 C41 ZKM A 704 6956 6949 7088 311 -426 466 C
HETATM 5996 C42 ZKM A 704 23.286 18.089 19.922 1.00 47.28 C
ANISOU 5996 C42 ZKM A 704 5959 5921 6083 331 -390 421 C
HETATM 5997 C43 ZKM A 704 24.262 18.812 18.967 1.00 51.88 C
ANISOU 5997 C43 ZKM A 704 6562 6503 6646 343 -365 392 C
HETATM 5998 C44 ZKM A 704 24.867 20.087 19.601 1.00 48.77 C
ANISOU 5998 C44 ZKM A 704 6160 6107 6265 371 -311 386 C
HETATM 5999 C45 ZKM A 704 24.971 19.999 21.137 1.00 42.67 C
ANISOU 5999 C45 ZKM A 704 5373 5322 5517 380 -294 384 C
HETATM 6000 C46 ZKM A 704 26.134 20.866 21.655 1.00 39.35 C
ANISOU 6000 C46 ZKM A 704 4959 4890 5102 406 -246 352 C
HETATM 6001 C47 ZKM A 704 26.242 22.176 20.867 1.00 39.07 C
ANISOU 6001 C47 ZKM A 704 4921 4868 5057 420 -213 363 C
HETATM 6002 C48 ZKM A 704 27.631 22.826 20.944 1.00 44.67 C
ANISOU 6002 C48 ZKM A 704 5647 5564 5761 442 -173 320 C
HETATM 6003 C49 ZKM A 704 27.762 23.780 22.143 1.00 45.03 C
ANISOU 6003 C49 ZKM A 704 5672 5606 5830 464 -129 328 C
HETATM 6004 C50 ZKM A 704 28.460 25.094 21.754 1.00 42.09 C
ANISOU 6004 C50 ZKM A 704 5302 5237 5451 487 -83 318 C
HETATM 6005 C51 ZKM A 704 27.884 25.671 20.457 1.00 41.03 C
ANISOU 6005 C51 ZKM A 704 5166 5122 5300 482 -89 344 C
HETATM 6006 C52 ZKM A 704 28.373 27.083 20.176 1.00 43.12 C
ANISOU 6006 C52 ZKM A 704 5428 5392 5562 505 -42 343 C
HETATM 6007 C53 ZKM A 704 27.384 27.867 19.323 1.00 38.70 C
ANISOU 6007 C53 ZKM A 704 4854 4856 4996 502 -42 387 C
HETATM 6008 N19 ZKM A 704 20.458 14.980 15.642 1.00107.38 N
ANISOU 6008 N19 ZKM A 704 13598 13573 13627 235 -575 480 N
HETATM 6009 O01 ZKM A 704 19.087 8.890 17.626 1.00131.08 O
ANISOU 6009 O01 ZKM A 704 16615 16537 16654 148 -756 460 O
HETATM 6010 O04 ZKM A 704 16.274 8.415 17.460 1.00144.05 O
ANISOU 6010 O04 ZKM A 704 18214 18209 18310 117 -812 557 O
HETATM 6011 O06 ZKM A 704 15.592 6.005 18.111 1.00147.28 O1-
ANISOU 6011 O06 ZKM A 704 18627 18605 18727 81 -887 554 O1-
HETATM 6012 O07 ZKM A 704 16.280 6.440 15.760 1.00150.38 O
ANISOU 6012 O07 ZKM A 704 19053 19009 19076 78 -893 530 O
HETATM 6013 O08 ZKM A 704 14.191 7.221 16.442 1.00150.30 O
ANISOU 6013 O08 ZKM A 704 18992 19023 19094 77 -890 617 O
HETATM 6014 O10 ZKM A 704 15.435 10.869 16.745 1.00130.37 O
ANISOU 6014 O10 ZKM A 704 16450 16506 16577 141 -757 616 O
HETATM 6015 O13 ZKM A 704 16.582 13.217 14.172 1.00110.92 O
ANISOU 6015 O13 ZKM A 704 14011 14063 14068 169 -700 598 O
HETATM 6016 O14 ZKM A 704 17.988 11.720 15.471 1.00128.34 O
ANISOU 6016 O14 ZKM A 704 16243 16235 16284 167 -711 531 O
HETATM 6017 O16 ZKM A 704 19.714 11.636 16.973 1.00122.78 O
ANISOU 6017 O16 ZKM A 704 15555 15501 15596 189 -671 469 O
HETATM 6018 O36 ZKM A 704 21.853 16.092 14.204 1.00107.26 O
ANISOU 6018 O36 ZKM A 704 13612 13560 13583 254 -538 440 O
HETATM 6019 O38 ZKM A 704 20.069 13.657 19.017 1.00 99.17 O
ANISOU 6019 O38 ZKM A 704 12528 12506 12645 234 -581 484 O
HETATM 6020 S05 ZKM A 704 15.586 6.996 16.976 1.00149.53 S
ANISOU 6020 S05 ZKM A 704 18915 18904 18996 88 -871 564 S
HETATM 6021 C1 NAG C 201 20.070 33.531 28.685 1.00 56.80 C
HETATM 6022 C2 NAG C 201 19.599 34.680 29.567 1.00 65.20 C
HETATM 6023 C3 NAG C 201 18.715 34.158 30.703 1.00 68.08 C
HETATM 6024 C4 NAG C 201 19.194 32.800 31.207 1.00 67.55 C
HETATM 6025 C5 NAG C 201 19.279 31.780 30.072 1.00 68.23 C
HETATM 6026 C6 NAG C 201 18.169 30.756 30.120 1.00 68.08 C
HETATM 6027 C7 NAG C 201 20.896 36.743 29.876 1.00 67.98 C
HETATM 6028 C8 NAG C 201 19.846 37.412 29.039 1.00 61.17 C
HETATM 6029 N2 NAG C 201 20.724 35.434 30.096 1.00 67.99 N
HETATM 6030 O3 NAG C 201 17.376 34.051 30.236 1.00 69.11 O
HETATM 6031 O4 NAG C 201 20.470 32.936 31.822 1.00 66.05 O
HETATM 6032 O5 NAG C 201 19.175 32.443 28.805 1.00 65.08 O
HETATM 6033 O6 NAG C 201 18.653 29.448 29.845 1.00 66.48 O
HETATM 6034 O7 NAG C 201 21.854 37.360 30.329 1.00 74.73 O
HETATM 6035 C1 NAG C 202 44.194 19.723 28.540 1.00 42.40 C
HETATM 6036 C2 NAG C 202 45.479 20.284 27.900 1.00 43.66 C
HETATM 6037 C3 NAG C 202 46.702 19.469 28.328 1.00 44.68 C
HETATM 6038 C4 NAG C 202 46.751 19.304 29.841 1.00 46.99 C
HETATM 6039 C5 NAG C 202 45.429 18.731 30.334 1.00 48.75 C
HETATM 6040 C6 NAG C 202 45.367 18.548 31.835 1.00 54.70 C
HETATM 6041 C7 NAG C 202 45.187 21.408 25.727 1.00 57.92 C
HETATM 6042 C8 NAG C 202 45.069 22.680 26.500 1.00 57.20 C
HETATM 6043 N2 NAG C 202 45.372 20.296 26.449 1.00 52.35 N
HETATM 6044 O3 NAG C 202 47.883 20.118 27.870 1.00 50.84 O
HETATM 6045 O4 NAG C 202 47.809 18.422 30.201 1.00 51.35 O
HETATM 6046 O5 NAG C 202 44.365 19.617 29.964 1.00 42.08 O
HETATM 6047 O6 NAG C 202 45.309 19.788 32.526 1.00 59.25 O
HETATM 6048 O7 NAG C 202 45.110 21.383 24.503 1.00 56.01 O
HETATM 6049 C02 ZKM C 203 20.809 6.627 13.723 1.00116.96 C
ANISOU 6049 C02 ZKM C 203 14920 14740 14779 106 -848 362 C
HETATM 6050 C03 ZKM C 203 20.575 5.758 12.543 1.00126.14 C
ANISOU 6050 C03 ZKM C 203 16099 15908 15920 84 -892 358 C
HETATM 6051 C09 ZKM C 203 21.683 5.871 11.585 1.00120.35 C
ANISOU 6051 C09 ZKM C 203 15395 15169 15164 89 -885 317 C
HETATM 6052 C11 ZKM C 203 23.055 5.617 12.222 1.00117.04 C
ANISOU 6052 C11 ZKM C 203 14995 14728 14746 101 -866 265 C
HETATM 6053 C12 ZKM C 203 24.026 6.602 11.670 1.00115.92 C
ANISOU 6053 C12 ZKM C 203 14867 14586 14591 120 -828 240 C
HETATM 6054 C15 ZKM C 203 22.023 6.166 14.537 1.00111.02 C
ANISOU 6054 C15 ZKM C 203 14185 13965 14032 114 -836 314 C
HETATM 6055 C17 ZKM C 203 21.856 7.434 16.547 1.00 97.78 C
ANISOU 6055 C17 ZKM C 203 12471 12285 12395 144 -775 339 C
HETATM 6056 C18 ZKM C 203 22.954 7.705 17.579 1.00 89.57 C
ANISOU 6056 C18 ZKM C 203 11438 11228 11368 163 -739 303 C
HETATM 6057 C20 ZKM C 203 24.842 6.267 18.326 1.00 90.31 C
ANISOU 6057 C20 ZKM C 203 11570 11285 11457 162 -748 218 C
HETATM 6058 C21 ZKM C 203 25.804 7.401 17.909 1.00 87.87 C
ANISOU 6058 C21 ZKM C 203 11271 10976 11139 184 -705 195 C
HETATM 6059 C22 ZKM C 203 26.719 7.962 19.024 1.00 80.73 C
ANISOU 6059 C22 ZKM C 203 10366 10057 10250 207 -661 170 C
HETATM 6060 C23 ZKM C 203 26.016 8.309 20.344 1.00 69.74 C
ANISOU 6060 C23 ZKM C 203 8945 8667 8887 214 -645 203 C
HETATM 6061 C24 ZKM C 203 26.444 9.687 20.909 1.00 61.99 C
ANISOU 6061 C24 ZKM C 203 7951 7685 7917 241 -590 204 C
HETATM 6062 C25 ZKM C 203 26.980 9.625 22.366 1.00 53.65 C
ANISOU 6062 C25 ZKM C 203 6889 6612 6882 254 -567 186 C
HETATM 6063 C26 ZKM C 203 27.695 10.944 22.769 1.00 52.82 C
ANISOU 6063 C26 ZKM C 203 6780 6505 6785 282 -513 176 C
HETATM 6064 C27 ZKM C 203 28.047 11.061 24.269 1.00 51.43 C
ANISOU 6064 C27 ZKM C 203 6593 6315 6633 296 -486 167 C
HETATM 6065 C28 ZKM C 203 28.410 12.503 24.646 1.00 50.27 C
ANISOU 6065 C28 ZKM C 203 6434 6172 6495 323 -433 172 C
HETATM 6066 C29 ZKM C 203 29.069 12.630 26.025 1.00 51.06 C
ANISOU 6066 C29 ZKM C 203 6530 6256 6616 339 -404 151 C
HETATM 6067 C30 ZKM C 203 28.996 14.067 26.575 1.00 50.62 C
ANISOU 6067 C30 ZKM C 203 6453 6206 6575 363 -355 172 C
HETATM 6068 C31 ZKM C 203 30.219 14.435 27.435 1.00 49.66 C
ANISOU 6068 C31 ZKM C 203 6340 6067 6462 384 -317 133 C
HETATM 6069 C32 ZKM C 203 30.589 15.921 27.322 1.00 51.92 C
ANISOU 6069 C32 ZKM C 203 6619 6360 6750 408 -268 137 C
HETATM 6070 C33 ZKM C 203 31.075 16.274 25.918 1.00 55.29 C
ANISOU 6070 C33 ZKM C 203 7065 6792 7150 408 -267 121 C
HETATM 6071 C34 ZKM C 203 32.379 17.065 25.933 1.00 59.19 C
ANISOU 6071 C34 ZKM C 203 7574 7277 7640 430 -224 82 C
HETATM 6072 C35 ZKM C 203 32.686 17.685 24.573 1.00 67.95 C
ANISOU 6072 C35 ZKM C 203 8696 8395 8725 433 -217 76 C
HETATM 6073 C37 ZKM C 203 22.493 8.533 18.777 1.00 81.25 C
ANISOU 6073 C37 ZKM C 203 10354 10176 10340 179 -706 332 C
HETATM 6074 C39 ZKM C 203 22.531 10.037 18.446 1.00 75.20 C
ANISOU 6074 C39 ZKM C 203 9578 9423 9573 199 -663 349 C
HETATM 6075 C40 ZKM C 203 23.722 10.655 18.385 1.00 65.63 C
ANISOU 6075 C40 ZKM C 203 8381 8201 8354 217 -629 312 C
HETATM 6076 C41 ZKM C 203 23.804 12.162 18.061 1.00 54.48 C
ANISOU 6076 C41 ZKM C 203 6959 6800 6941 237 -585 327 C
HETATM 6077 C42 ZKM C 203 24.739 12.861 19.070 1.00 46.40 C
ANISOU 6077 C42 ZKM C 203 5935 5764 5932 262 -539 303 C
HETATM 6078 C43 ZKM C 203 24.031 13.140 20.415 1.00 43.37 C
ANISOU 6078 C43 ZKM C 203 5521 5380 5576 268 -525 334 C
HETATM 6079 C44 ZKM C 203 24.522 14.446 21.083 1.00 46.97 C
ANISOU 6079 C44 ZKM C 203 5966 5835 6045 296 -470 333 C
HETATM 6080 C45 ZKM C 203 25.533 14.173 22.215 1.00 47.81 C
ANISOU 6080 C45 ZKM C 203 6081 5921 6165 307 -451 294 C
HETATM 6081 C46 ZKM C 203 25.596 15.309 23.252 1.00 48.19 C
ANISOU 6081 C46 ZKM C 203 6107 5968 6233 331 -403 308 C
HETATM 6082 C47 ZKM C 203 26.499 16.453 22.781 1.00 51.68 C
ANISOU 6082 C47 ZKM C 203 6559 6411 6666 352 -361 287 C
HETATM 6083 C48 ZKM C 203 27.450 16.926 23.889 1.00 52.95 C
ANISOU 6083 C48 ZKM C 203 6720 6556 6842 374 -321 260 C
HETATM 6084 C49 ZKM C 203 26.991 18.227 24.570 1.00 51.18 C
ANISOU 6084 C49 ZKM C 203 6467 6341 6636 394 -280 293 C
HETATM 6085 C50 ZKM C 203 27.577 18.311 25.987 1.00 47.42 C
ANISOU 6085 C50 ZKM C 203 5986 5849 6182 409 -253 275 C
HETATM 6086 C51 ZKM C 203 27.815 19.738 26.482 1.00 42.90 C
ANISOU 6086 C51 ZKM C 203 5398 5280 5621 435 -200 284 C
HETATM 6087 C52 ZKM C 203 28.588 19.726 27.789 1.00 37.80 C
ANISOU 6087 C52 ZKM C 203 4752 4616 4994 450 -175 258 C
HETATM 6088 C53 ZKM C 203 27.846 20.452 28.899 1.00 37.71 C
ANISOU 6088 C53 ZKM C 203 4709 4611 5009 462 -150 296 C
HETATM 6089 N19 ZKM C 203 23.402 6.440 18.133 1.00 90.11 N
ANISOU 6089 N19 ZKM C 203 11521 11279 11439 152 -765 273 N
HETATM 6090 O01 ZKM C 203 19.639 6.566 14.548 1.00111.87 O
ANISOU 6090 O01 ZKM C 203 14246 14102 14156 101 -857 406 O
HETATM 6091 O04 ZKM C 203 19.340 6.188 11.887 1.00136.84 O
ANISOU 6091 O04 ZKM C 203 17436 17284 17274 77 -904 408 O
HETATM 6092 O06 ZKM C 203 18.763 3.663 11.941 1.00143.53 O1-
ANISOU 6092 O06 ZKM C 203 18296 18120 18117 36 -989 398 O1-
HETATM 6093 O07 ZKM C 203 18.172 4.967 9.907 1.00144.00 O
ANISOU 6093 O07 ZKM C 203 18355 18209 18149 38 -982 432 O
HETATM 6094 O08 ZKM C 203 16.883 5.299 11.821 1.00142.75 O
ANISOU 6094 O08 ZKM C 203 18150 18054 18034 43 -967 487 O
HETATM 6095 O10 ZKM C 203 21.651 7.202 11.009 1.00117.87 O
ANISOU 6095 O10 ZKM C 203 15073 14868 14844 105 -851 334 O
HETATM 6096 O13 ZKM C 203 23.848 7.814 12.318 1.00115.57 O
ANISOU 6096 O13 ZKM C 203 14801 14548 14564 140 -786 263 O
HETATM 6097 O14 ZKM C 203 23.137 5.631 13.731 1.00114.14 O
ANISOU 6097 O14 ZKM C 203 14613 14350 14404 111 -846 265 O
HETATM 6098 O16 ZKM C 203 22.494 7.222 15.307 1.00103.97 O
ANISOU 6098 O16 ZKM C 203 13282 13069 13153 138 -787 310 O
HETATM 6099 O36 ZKM C 203 25.224 5.249 18.777 1.00 92.56 O
ANISOU 6099 O36 ZKM C 203 11868 11557 11745 154 -768 192 O
HETATM 6100 O38 ZKM C 203 21.224 8.128 19.200 1.00 79.63 O
ANISOU 6100 O38 ZKM C 203 10127 9981 10149 165 -731 375 O
HETATM 6101 S05 ZKM C 203 18.304 4.995 11.407 1.00142.55 S
ANISOU 6101 S05 ZKM C 203 18158 18015 17992 48 -961 430 S
HETATM 6102 O HOH A 801 62.780 12.773 -20.814 1.00 66.89 O
HETATM 6103 O HOH A 802 11.744 29.846 21.185 1.00 41.75 O
HETATM 6104 O HOH A 803 6.522 10.045 -7.401 1.00 46.02 O
HETATM 6105 O HOH A 804 41.811 20.019 -16.363 1.00 49.42 O
HETATM 6106 O HOH A 805 13.974 4.167 -15.727 1.00 46.96 O
HETATM 6107 O HOH A 806 4.195 33.952 16.294 1.00 26.24 O
HETATM 6108 O HOH A 807 10.594 43.024 -4.930 1.00 25.10 O
HETATM 6109 O HOH A 808 6.933 20.918 14.277 1.00 38.38 O
HETATM 6110 O HOH A 809 39.522 39.838 11.218 1.00 46.46 O
HETATM 6111 O HOH A 810 83.173 20.292 -5.683 1.00 46.23 O
HETATM 6112 O HOH A 811 42.337 2.684 -20.816 1.00 16.59 O
HETATM 6113 O HOH A 812 42.933 15.397 -7.393 1.00 40.37 O
HETATM 6114 O HOH A 813 45.730 -9.804 -14.386 1.00 45.85 O
HETATM 6115 O HOH A 814 -5.576 38.633 3.320 1.00 35.48 O
HETATM 6116 O HOH A 815 43.091 53.394 3.597 1.00 45.81 O
HETATM 6117 O HOH A 816 45.214 2.875 -22.928 1.00 48.10 O
HETATM 6118 O HOH A 817 43.505 -0.376 -4.683 1.00 36.90 O
HETATM 6119 O HOH A 818 29.227 58.471 24.825 1.00 33.36 O
HETATM 6120 O HOH A 819 16.887 53.703 17.974 1.00 33.25 O
HETATM 6121 O HOH A 820 51.962 -1.702 -2.020 1.00 50.35 O
HETATM 6122 O HOH A 821 3.289 37.278 19.469 1.00 28.90 O
HETATM 6123 O HOH A 822 15.455 22.927 -5.683 1.00 29.65 O
HETATM 6124 O HOH A 823 13.733 51.934 -3.670 1.00 43.22 O
HETATM 6125 O HOH A 824 -3.222 35.630 13.459 1.00 34.19 O
HETATM 6126 O HOH A 825 33.911 3.729 0.121 1.00 41.08 O
HETATM 6127 O HOH A 826 33.161 19.377 -14.150 1.00 31.18 O
HETATM 6128 O HOH A 827 4.360 44.649 15.862 1.00 41.99 O
HETATM 6129 O HOH A 828 65.806 6.824 -11.587 1.00 37.93 O
HETATM 6130 O HOH A 829 35.354 15.212 -7.389 1.00 20.78 O
HETATM 6131 O HOH A 830 -2.620 28.543 5.800 1.00 34.27 O
HETATM 6132 O HOH A 831 31.726 54.953 1.912 1.00 28.52 O
HETATM 6133 O HOH A 832 52.051 -2.322 -18.116 1.00 33.32 O
HETATM 6134 O HOH A 833 17.768 30.615 20.950 1.00 44.02 O
HETATM 6135 O HOH A 834 42.998 58.221 14.160 1.00 37.77 O
HETATM 6136 O HOH A 835 62.534 15.656 -20.704 1.00 36.68 O
HETATM 6137 O HOH A 836 52.045 17.903 -21.472 1.00 16.93 O
HETATM 6138 O HOH A 837 21.597 58.911 4.918 1.00 36.08 O
HETATM 6139 O HOH A 838 26.061 61.440 15.168 1.00 34.15 O
HETATM 6140 O HOH A 839 77.412 18.545 -9.923 1.00 41.57 O
HETATM 6141 O HOH A 840 11.655 16.090 13.334 1.00 31.29 O
HETATM 6142 O HOH A 841 21.785 38.647 10.483 1.00 23.23 O
HETATM 6143 O HOH A 842 61.306 19.507 -3.789 1.00 37.51 O
HETATM 6144 O HOH A 843 23.348 65.223 14.419 1.00 30.65 O
HETATM 6145 O HOH A 844 48.613 13.052 -28.569 1.00 36.10 O
HETATM 6146 O HOH A 845 29.733 16.796 -4.315 1.00 26.03 O
HETATM 6147 O HOH A 846 16.249 41.478 19.489 1.00 25.21 O
HETATM 6148 O HOH A 847 31.206 16.148 -7.977 1.00 27.81 O
HETATM 6149 O HOH A 848 8.155 45.812 -5.362 1.00 35.48 O
HETATM 6150 O HOH A 849 5.679 50.864 3.833 1.00 30.38 O
HETATM 6151 O HOH A 850 28.359 61.034 11.684 1.00 20.19 O
HETATM 6152 O HOH A 851 32.471 14.487 -4.442 1.00 25.38 O
HETATM 6153 O HOH A 852 36.830 59.942 10.220 1.00 33.07 O
HETATM 6154 O HOH A 853 20.454 51.928 -2.327 1.00 34.24 O
HETATM 6155 O HOH A 854 36.751 16.647 -26.749 1.00 26.97 O
HETATM 6156 O HOH A 855 12.504 14.638 -15.633 1.00 33.49 O
HETATM 6157 O HOH A 856 56.037 11.538 -22.654 1.00 26.64 O
HETATM 6158 O HOH A 857 23.605 61.788 5.863 1.00 38.76 O
HETATM 6159 O HOH A 858 29.592 11.617 -22.514 1.00 18.19 O
HETATM 6160 O HOH A 859 -8.572 38.143 7.643 1.00 39.45 O
HETATM 6161 O HOH A 860 2.345 26.215 -6.204 1.00 42.30 O
HETATM 6162 O HOH A 861 41.156 13.218 -23.273 1.00 20.18 O
HETATM 6163 O HOH A 862 23.943 19.582 -5.692 1.00 25.36 O
HETATM 6164 O HOH A 863 26.120 55.896 0.280 1.00 32.54 O
HETATM 6165 O HOH A 864 -2.888 49.202 7.496 1.00 29.87 O
HETATM 6166 O HOH A 865 23.696 46.673 21.880 1.00 21.03 O
HETATM 6167 O HOH A 866 25.033 42.080 5.705 1.00 33.20 O
HETATM 6168 O HOH A 867 54.049 -0.480 -3.683 1.00 32.58 O
HETATM 6169 O HOH A 868 53.155 17.466 -4.233 1.00 55.16 O
HETATM 6170 O HOH A 869 30.365 10.329 -29.587 1.00 50.61 O
HETATM 6171 O HOH A 870 7.151 11.866 7.980 1.00 55.45 O
HETATM 6172 O HOH A 871 49.819 0.116 -7.458 1.00 26.46 O
HETATM 6173 O HOH A 872 34.892 45.262 23.757 1.00 41.08 O
HETATM 6174 O HOH A 873 11.329 17.882 9.965 1.00 36.24 O
HETATM 6175 O HOH A 874 44.088 4.918 -27.980 1.00 47.10 O
HETATM 6176 O HOH A 875 36.994 -0.921 -8.606 1.00 47.48 O
HETATM 6177 O HOH A 876 29.177 16.764 7.464 1.00 35.86 O
HETATM 6178 O HOH A 877 16.144 40.992 -3.372 1.00 43.12 O
HETATM 6179 O HOH A 878 50.500 -1.536 -20.226 1.00 36.09 O
HETATM 6180 O HOH A 879 40.212 59.043 18.103 1.00 32.37 O
HETATM 6181 O HOH A 880 21.111 57.592 23.450 1.00 30.30 O
HETATM 6182 O HOH A 881 42.855 5.725 -22.688 1.00 32.95 O
HETATM 6183 O HOH A 882 24.805 43.222 24.266 1.00 30.91 O
HETATM 6184 O HOH A 883 25.651 59.973 22.395 1.00 22.94 O
HETATM 6185 O HOH A 884 27.477 17.429 -7.342 1.00 28.61 O
HETATM 6186 O HOH A 885 25.585 58.477 -0.425 1.00 57.29 O
HETATM 6187 O HOH A 886 30.858 61.168 9.769 1.00 20.67 O
HETATM 6188 O HOH A 887 20.641 7.086 3.020 1.00 46.32 O
HETATM 6189 O HOH A 888 25.995 63.324 12.792 1.00 20.92 O
HETATM 6190 O HOH A 889 14.923 33.472 19.720 1.00 35.85 O
HETATM 6191 O HOH A 890 16.026 51.315 21.967 1.00 28.61 O
HETATM 6192 O HOH A 891 9.125 29.840 19.154 1.00 49.67 O
HETATM 6193 O HOH A 892 22.454 10.827 -24.312 1.00 51.47 O
HETATM 6194 O HOH A 893 37.650 56.452 21.224 1.00 33.23 O
HETATM 6195 O HOH A 894 5.813 45.107 -4.819 1.00 41.55 O
HETATM 6196 O HOH A 895 75.115 12.810 -13.548 1.00 45.24 O
HETATM 6197 O HOH A 896 13.418 25.481 -3.459 1.00 40.78 O
HETATM 6198 O HOH A 897 15.213 49.913 -7.557 1.00 50.00 O
HETATM 6199 O HOH A 898 37.254 20.735 -18.920 1.00 29.86 O
HETATM 6200 O HOH A 899 32.227 17.009 -3.595 1.00 35.99 O
HETATM 6201 O HOH A 900 1.296 46.679 -6.738 1.00 44.49 O
HETATM 6202 O HOH A 901 46.717 3.036 -2.156 1.00 41.33 O
HETATM 6203 O HOH A 902 35.943 2.766 -20.645 1.00 20.09 O
HETATM 6204 O HOH A 903 16.431 -1.641 -0.215 1.00 51.60 O
HETATM 6205 O HOH A 904 35.587 11.784 -22.820 1.00 20.77 O
HETATM 6206 O HOH A 905 46.705 16.469 -7.666 1.00 26.96 O
HETATM 6207 O HOH A 906 -1.617 40.899 -5.654 1.00 37.04 O
HETATM 6208 O HOH A 907 67.632 20.697 -3.523 1.00 45.41 O
HETATM 6209 O HOH A 908 17.255 15.152 9.456 1.00 33.32 O
HETATM 6210 O HOH A 909 35.447 48.825 29.465 1.00 37.23 O
HETATM 6211 O HOH A 910 24.884 48.058 27.295 1.00 40.18 O
HETATM 6212 O HOH A 911 15.479 58.654 9.182 1.00 45.68 O
HETATM 6213 O HOH A 912 37.682 64.493 17.044 1.00 51.10 O
HETATM 6214 O HOH A 913 -1.619 15.599 -3.504 1.00 54.55 O
HETATM 6215 O HOH A 914 9.766 49.515 15.342 1.00 23.30 O
HETATM 6216 O HOH A 915 12.163 37.266 18.962 1.00 29.93 O
HETATM 6217 O HOH A 916 43.025 58.502 10.240 1.00 34.19 O
HETATM 6218 O HOH A 917 16.413 40.674 22.397 1.00 38.80 O
HETATM 6219 O HOH A 918 49.313 -2.625 -14.309 1.00 32.97 O
HETATM 6220 O HOH A 919 57.004 20.624 -20.035 1.00 32.54 O
HETATM 6221 O HOH A 920 8.099 30.587 10.959 1.00 40.35 O
HETATM 6222 O HOH A 921 48.708 27.176 -20.923 1.00 29.93 O
HETATM 6223 O HOH A 922 29.907 46.382 22.778 1.00 15.93 O
HETATM 6224 O HOH A 923 18.049 60.359 13.161 1.00 38.63 O
HETATM 6225 O HOH A 924 21.931 39.112 6.857 1.00 33.77 O
HETATM 6226 O HOH A 925 23.276 59.915 8.166 1.00 21.94 O
HETATM 6227 O HOH A 926 37.246 19.042 -16.501 1.00 24.36 O
HETATM 6228 O HOH A 927 19.955 45.363 20.505 1.00 17.26 O
HETATM 6229 O HOH A 928 13.293 20.543 18.697 1.00 40.11 O
HETATM 6230 O HOH A 929 15.414 49.340 -3.733 1.00 52.89 O
HETATM 6231 O HOH A 930 -2.131 27.086 -7.542 1.00 28.52 O
HETATM 6232 O HOH A 931 28.598 20.247 -14.050 1.00 43.00 O
HETATM 6233 O HOH A 932 30.376 51.785 26.708 1.00 32.22 O
HETATM 6234 O HOH A 933 11.772 27.549 15.966 1.00 36.59 O
HETATM 6235 O HOH A 934 15.225 36.639 2.881 1.00 29.01 O
HETATM 6236 O HOH A 935 15.963 15.840 12.976 1.00 47.16 O
HETATM 6237 O HOH A 936 18.542 19.835 -7.360 1.00 39.70 O
HETATM 6238 O HOH A 937 2.556 28.964 -6.441 1.00 33.93 O
HETATM 6239 O HOH A 938 15.766 47.134 -5.725 1.00 41.93 O
HETATM 6240 O HOH A 939 34.085 67.388 15.606 1.00 40.54 O
HETATM 6241 O HOH A 940 7.920 17.843 -13.081 1.00 43.61 O
HETATM 6242 O HOH A 941 39.418 -3.476 -7.823 1.00 45.99 O
HETATM 6243 O HOH A 942 18.635 13.754 2.330 1.00 28.73 O
HETATM 6244 O HOH A 943 24.786 59.509 4.692 1.00 42.96 O
HETATM 6245 O HOH A 944 37.472 55.162 2.369 1.00 36.60 O
HETATM 6246 O HOH A 945 -0.125 23.911 18.307 1.00 41.19 O
HETATM 6247 O HOH A 946 39.255 14.004 -0.958 1.00 47.87 O
HETATM 6248 O HOH A 947 19.798 39.496 23.779 1.00 43.72 O
HETATM 6249 O HOH A 948 25.554 40.588 7.842 1.00 25.80 O
HETATM 6250 O HOH A 949 49.019 -4.225 -18.439 1.00 51.25 O
HETATM 6251 O HOH A 950 32.434 17.656 -24.125 1.00 37.35 O
HETATM 6252 O HOH A 951 -11.807 40.014 5.629 1.00 47.77 O
HETATM 6253 O HOH A 952 49.254 -6.770 -7.335 1.00 43.91 O
HETATM 6254 O HOH A 953 19.991 61.071 6.729 1.00 43.67 O
HETATM 6255 O HOH A 954 54.921 14.411 -31.251 1.00 43.31 O
HETATM 6256 O HOH A 955 37.602 57.191 17.799 1.00 36.20 O
HETATM 6257 O HOH A 956 29.132 41.526 6.570 1.00 35.91 O
HETATM 6258 O HOH A 957 70.426 11.486 -10.165 1.00 42.03 O
HETATM 6259 O HOH A 958 9.376 22.656 21.414 1.00 43.69 O
HETATM 6260 O HOH A 959 48.175 -1.399 -24.008 1.00 39.14 O
HETATM 6261 O HOH A 960 17.324 23.226 -13.545 1.00 52.35 O
HETATM 6262 O HOH A 961 74.058 24.644 -11.906 1.00 45.77 O
HETATM 6263 O HOH A 962 7.750 28.946 12.692 1.00 38.31 O
HETATM 6264 O HOH A 963 33.090 40.345 10.082 1.00 35.08 O
HETATM 6265 O HOH A 964 16.812 32.233 9.016 1.00 41.38 O
HETATM 6266 O HOH A 965 57.611 -1.385 -20.473 1.00 34.15 O
HETATM 6267 O HOH A 966 6.806 32.293 18.498 1.00 47.61 O
HETATM 6268 O HOH A 967 17.390 32.860 4.379 1.00 40.19 O
HETATM 6269 O HOH A 968 19.692 62.374 8.790 1.00 23.45 O
HETATM 6270 O HOH A 969 35.583 -5.169 -7.729 1.00 39.41 O
HETATM 6271 O HOH A 970 8.474 29.937 -11.679 1.00 47.22 O
HETATM 6272 O HOH A 971 17.414 59.559 6.741 1.00 42.00 O
HETATM 6273 O HOH A 972 27.013 62.167 3.098 1.00 48.12 O
HETATM 6274 O HOH A 973 71.983 9.210 -11.740 1.00 46.79 O
HETATM 6275 O HOH A 974 22.065 46.329 -6.002 1.00 42.76 O
HETATM 6276 O HOH A 975 15.551 7.190 8.343 1.00 42.35 O
HETATM 6277 O HOH A 976 39.570 1.860 -34.440 1.00 40.15 O
HETATM 6278 O HOH A 977 -3.390 36.719 10.907 1.00 28.51 O
HETATM 6279 O HOH A 978 -7.768 42.607 9.289 1.00 40.29 O
HETATM 6280 O HOH A 979 44.203 1.178 -2.742 1.00 36.03 O
HETATM 6281 O HOH A 980 10.529 38.846 20.403 1.00 39.57 O
HETATM 6282 O HOH A 981 41.916 2.685 -36.088 1.00 47.12 O
HETATM 6283 O HOH A 982 17.820 33.152 18.469 1.00 39.33 O
HETATM 6284 O HOH A 983 -2.194 25.439 18.248 1.00 34.57 O
HETATM 6285 O HOH A 984 47.221 -3.641 -15.920 1.00 50.15 O
HETATM 6286 O HOH A 985 -6.218 37.462 11.017 1.00 39.48 O
HETATM 6287 O HOH A 986 2.640 32.208 20.135 1.00 35.17 O
HETATM 6288 O HOH A 987 3.433 47.924 14.261 1.00 45.88 O
HETATM 6289 O HOH A 988 21.597 44.930 23.415 1.00 30.84 O
HETATM 6290 O HOH A 989 45.282 3.028 -34.586 1.00 49.62 O
HETATM 6291 O HOH A 990 36.392 17.375 -5.425 1.00 42.55 O
HETATM 6292 O HOH A 991 38.056 41.165 4.472 1.00 38.77 O
HETATM 6293 O HOH A 992 11.058 15.154 -22.480 1.00 41.50 O
HETATM 6294 O HOH A 993 50.838 -4.084 -15.784 1.00 47.47 O
HETATM 6295 O HOH A 994 22.811 41.121 5.308 1.00 48.26 O
HETATM 6296 O HOH A 995 22.066 30.466 -1.443 1.00 39.29 O
HETATM 6297 O HOH A 996 21.398 35.123 8.136 1.00 35.43 O
HETATM 6298 O HOH A 997 35.381 42.320 24.678 1.00 44.82 O
HETATM 6299 O HOH A 998 20.434 65.138 -1.054 1.00 51.61 O
HETATM 6300 O HOH A 999 12.113 13.682 -24.082 1.00 44.80 O
HETATM 6301 O HOH A1000 25.066 21.541 -4.159 1.00 46.55 O
HETATM 6302 O HOH A1001 18.619 66.638 0.133 1.00 49.60 O
HETATM 6303 O HOH A1002 36.022 56.967 26.357 1.00 29.67 O
HETATM 6304 O HOH A1003 35.653 20.562 -15.175 1.00 39.88 O
HETATM 6305 O HOH A1004 33.117 57.991 26.626 1.00 40.41 O
HETATM 6306 O HOH A1005 11.133 37.528 23.955 1.00 38.54 O
HETATM 6307 O HOH A1006 13.415 50.644 22.624 1.00 45.46 O
HETATM 6308 O HOH A1007 46.218 0.273 -33.782 1.00 47.84 O
HETATM 6309 O HOH A1008 9.086 38.852 22.583 1.00 34.37 O
HETATM 6310 O HOH A1009 39.239 40.339 6.772 1.00 55.85 O
HETATM 6311 O HOH C 301 35.409 9.409 17.579 1.00 31.56 O
HETATM 6312 O HOH C 302 24.285 28.682 8.359 1.00 30.08 O
HETATM 6313 O HOH C 303 29.975 41.335 13.455 1.00 18.96 O
HETATM 6314 O HOH C 304 17.120 22.994 8.799 1.00 25.13 O
HETATM 6315 O HOH C 305 42.719 10.232 28.602 1.00 26.69 O
HETATM 6316 O HOH C 306 38.998 19.646 31.836 1.00 44.33 O
HETATM 6317 O HOH C 307 19.201 19.525 18.775 1.00 41.35 O
HETATM 6318 O HOH C 308 45.713 18.083 25.100 1.00 35.35 O
HETATM 6319 O HOH C 309 15.303 23.779 2.259 1.00 39.24 O
HETATM 6320 O HOH C 310 22.270 35.900 18.681 1.00 22.56 O
HETATM 6321 O HOH C 311 45.354 5.131 19.416 1.00 27.76 O
HETATM 6322 O HOH C 312 31.354 30.444 10.329 1.00 35.87 O
HETATM 6323 O HOH C 313 43.162 23.449 30.032 1.00 33.60 O
HETATM 6324 O HOH C 314 25.415 -0.375 21.516 1.00 30.57 O
HETATM 6325 O HOH C 315 30.096 39.904 11.143 1.00 18.73 O
HETATM 6326 O HOH C 316 34.273 33.029 20.487 1.00 16.52 O
HETATM 6327 O HOH C 317 26.596 33.805 10.856 1.00 18.83 O
HETATM 6328 O HOH C 318 38.971 12.411 18.678 1.00 23.16 O
HETATM 6329 O HOH C 319 45.295 22.463 31.879 1.00 42.26 O
HETATM 6330 O HOH C 320 38.360 29.490 24.439 1.00 29.41 O
HETATM 6331 O HOH C 321 24.566 5.532 25.451 1.00 52.24 O
HETATM 6332 O HOH C 322 39.311 30.948 4.186 1.00 43.67 O
HETATM 6333 O HOH C 323 35.961 32.481 34.713 1.00 51.95 O
HETATM 6334 O HOH C 324 20.007 34.232 16.246 1.00 33.12 O
HETATM 6335 O HOH C 325 42.907 13.149 18.852 1.00 37.33 O
HETATM 6336 O HOH C 326 20.942 28.597 7.636 1.00 30.04 O
HETATM 6337 O HOH C 327 31.627 35.367 25.466 1.00 28.23 O
HETATM 6338 O HOH C 328 46.321 3.084 28.458 1.00 36.74 O
HETATM 6339 O HOH C 329 23.371 36.412 9.537 1.00 24.28 O
HETATM 6340 O HOH C 330 35.523 13.242 11.406 1.00 35.29 O
HETATM 6341 O HOH C 331 42.727 14.500 23.920 1.00 42.48 O
HETATM 6342 O HOH C 332 33.706 35.555 10.814 1.00 44.73 O
HETATM 6343 O HOH C 333 21.922 29.528 28.143 1.00 46.50 O
HETATM 6344 O HOH C 334 17.564 17.894 11.046 1.00 33.48 O
HETATM 6345 O HOH C 335 22.336 22.273 10.600 1.00 34.02 O
HETATM 6346 O HOH C 336 34.191 34.096 22.741 1.00 22.17 O
HETATM 6347 O HOH C 337 43.373 33.524 24.196 1.00 38.30 O
HETATM 6348 O HOH C 338 36.769 38.193 11.337 1.00 42.55 O
HETATM 6349 O HOH C 339 35.968 33.251 31.493 1.00 38.32 O
HETATM 6350 O HOH C 340 20.626 31.377 19.433 1.00 41.49 O
HETATM 6351 O HOH C 341 23.527 20.099 12.110 1.00 44.59 O
HETATM 6352 O HOH C 342 22.123 10.733 36.494 1.00 39.96 O
HETATM 6353 O HOH C 343 38.552 37.842 8.729 1.00 54.34 O
HETATM 6354 O HOH C 344 16.463 31.965 22.739 1.00 46.53 O
HETATM 6355 O HOH C 345 28.514 38.515 7.094 1.00 57.01 O
HETATM 6356 O HOH C 346 21.724 33.455 17.925 1.00 34.52 O
HETATM 6357 O HOH C 347 30.694 37.750 5.650 1.00 46.10 O
HETATM 6358 O HOH C 348 44.585 13.696 17.262 1.00 44.58 O
HETATM 6359 O HOH C 349 44.889 19.088 20.993 1.00 42.05 O
HETATM 6360 O HOH C 350 28.469 40.358 8.820 1.00 30.37 O
HETATM 6361 O HOH C 351 44.658 21.298 19.894 1.00 50.00 O
HETATM 6362 O HOH C 352 33.009 40.729 25.311 1.00 42.63 O
HETATM 6363 O HOH C 353 26.449 35.383 8.305 1.00 32.90 O
CONECT 13 101
CONECT 101 13
CONECT 1415 5817
CONECT 1681 5845
CONECT 2021 2224
CONECT 2224 2021
CONECT 2885 2891
CONECT 2891 2885
CONECT 3704 5887
CONECT 3967 5901
CONECT 4430 4632
CONECT 4442 4704
CONECT 4632 4430
CONECT 4704 4442
CONECT 4761 4961
CONECT 4852 5744
CONECT 4961 4761
CONECT 5328 5411
CONECT 5411 5328
CONECT 5479 6021
CONECT 5744 4852
CONECT 5760 6035
CONECT 5817 1415 5818 5828
CONECT 5818 5817 5819 5825
CONECT 5819 5818 5820 5826
CONECT 5820 5819 5821 5827
CONECT 5821 5820 5822 5828
CONECT 5822 5821 5829
CONECT 5823 5824 5825 5830
CONECT 5824 5823
CONECT 5825 5818 5823
CONECT 5826 5819
CONECT 5827 5820 5831
CONECT 5828 5817 5821
CONECT 5829 5822
CONECT 5830 5823
CONECT 5831 5827 5832 5842
CONECT 5832 5831 5833 5839
CONECT 5833 5832 5834 5840
CONECT 5834 5833 5835 5841
CONECT 5835 5834 5836 5842
CONECT 5836 5835 5843
CONECT 5837 5838 5839 5844
CONECT 5838 5837
CONECT 5839 5832 5837
CONECT 5840 5833
CONECT 5841 5834
CONECT 5842 5831 5835
CONECT 5843 5836
CONECT 5844 5837
CONECT 5845 1681 5846 5856
CONECT 5846 5845 5847 5853
CONECT 5847 5846 5848 5854
CONECT 5848 5847 5849 5855
CONECT 5849 5848 5850 5856
CONECT 5850 5849 5857
CONECT 5851 5852 5853 5858
CONECT 5852 5851
CONECT 5853 5846 5851
CONECT 5854 5847
CONECT 5855 5848 5859
CONECT 5856 5845 5849
CONECT 5857 5850
CONECT 5858 5851
CONECT 5859 5855 5860 5870
CONECT 5860 5859 5861 5867
CONECT 5861 5860 5862 5868
CONECT 5862 5861 5863 5869
CONECT 5863 5862 5864 5870
CONECT 5864 5863 5871
CONECT 5865 5866 5867 5872
CONECT 5866 5865
CONECT 5867 5860 5865
CONECT 5868 5861
CONECT 5869 5862 5873
CONECT 5870 5859 5863
CONECT 5871 5864
CONECT 5872 5865
CONECT 5873 5869 5874 5884
CONECT 5874 5873 5875 5881
CONECT 5875 5874 5876 5882
CONECT 5876 5875 5877 5883
CONECT 5877 5876 5878 5884
CONECT 5878 5877 5885
CONECT 5879 5880 5881 5886
CONECT 5880 5879
CONECT 5881 5874 5879
CONECT 5882 5875
CONECT 5883 5876
CONECT 5884 5873 5877
CONECT 5885 5878
CONECT 5886 5879
CONECT 5887 3704 5888 5898
CONECT 5888 5887 5889 5895
CONECT 5889 5888 5890 5896
CONECT 5890 5889 5891 5897
CONECT 5891 5890 5892 5898
CONECT 5892 5891 5899
CONECT 5893 5894 5895 5900
CONECT 5894 5893
CONECT 5895 5888 5893
CONECT 5896 5889
CONECT 5897 5890
CONECT 5898 5887 5891
CONECT 5899 5892
CONECT 5900 5893
CONECT 5901 3967 5902 5912
CONECT 5902 5901 5903 5909
CONECT 5903 5902 5904 5910
CONECT 5904 5903 5905 5911
CONECT 5905 5904 5906 5912
CONECT 5906 5905 5913
CONECT 5907 5908 5909 5914
CONECT 5908 5907
CONECT 5909 5902 5907
CONECT 5910 5903
CONECT 5911 5904
CONECT 5912 5901 5905
CONECT 5913 5906
CONECT 5914 5907
CONECT 5915 5916 5920 5956
CONECT 5916 5915 5917 5957
CONECT 5917 5916 5918 5961
CONECT 5918 5917 5919 5963
CONECT 5919 5918 5962
CONECT 5920 5915 5963 5964
CONECT 5921 5922 5964
CONECT 5922 5921 5939 5955
CONECT 5923 5924 5955 5965
CONECT 5924 5923 5925
CONECT 5925 5924 5926
CONECT 5926 5925 5927
CONECT 5927 5926 5928
CONECT 5928 5927 5929
CONECT 5929 5928 5930
CONECT 5930 5929 5931
CONECT 5931 5930 5932
CONECT 5932 5931 5933
CONECT 5933 5932 5934
CONECT 5934 5933 5935
CONECT 5935 5934 5936
CONECT 5936 5935 5937
CONECT 5937 5936 5938
CONECT 5938 5937
CONECT 5939 5922 5940 5966
CONECT 5940 5939 5941
CONECT 5941 5940 5942
CONECT 5942 5941 5943
CONECT 5943 5942 5944
CONECT 5944 5943 5945
CONECT 5945 5944 5946
CONECT 5946 5945 5947
CONECT 5947 5946 5948
CONECT 5948 5947 5949
CONECT 5949 5948 5950
CONECT 5950 5949 5951
CONECT 5951 5950 5952
CONECT 5952 5951 5953
CONECT 5953 5952 5954
CONECT 5954 5953
CONECT 5955 5922 5923
CONECT 5956 5915
CONECT 5957 5916 5967
CONECT 5958 5967
CONECT 5959 5967
CONECT 5960 5967
CONECT 5961 5917
CONECT 5962 5919
CONECT 5963 5918 5920
CONECT 5964 5920 5921
CONECT 5965 5923
CONECT 5966 5939
CONECT 5967 5957 5958 5959 5960
CONECT 5968 5969 5973 6009
CONECT 5969 5968 5970 6010
CONECT 5970 5969 5971 6014
CONECT 5971 5970 5972 6016
CONECT 5972 5971 6015
CONECT 5973 5968 6016 6017
CONECT 5974 5975 6017
CONECT 5975 5974 5992 6008
CONECT 5976 5977 6008 6018
CONECT 5977 5976 5978
CONECT 5978 5977 5979
CONECT 5979 5978 5980
CONECT 5980 5979 5981
CONECT 5981 5980 5982
CONECT 5982 5981 5983
CONECT 5983 5982 5984
CONECT 5984 5983 5985
CONECT 5985 5984 5986
CONECT 5986 5985 5987
CONECT 5987 5986 5988
CONECT 5988 5987 5989
CONECT 5989 5988 5990
CONECT 5990 5989 5991
CONECT 5991 5990
CONECT 5992 5975 5993 6019
CONECT 5993 5992 5994
CONECT 5994 5993 5995
CONECT 5995 5994 5996
CONECT 5996 5995 5997
CONECT 5997 5996 5998
CONECT 5998 5997 5999
CONECT 5999 5998 6000
CONECT 6000 5999 6001
CONECT 6001 6000 6002
CONECT 6002 6001 6003
CONECT 6003 6002 6004
CONECT 6004 6003 6005
CONECT 6005 6004 6006
CONECT 6006 6005 6007
CONECT 6007 6006
CONECT 6008 5975 5976
CONECT 6009 5968
CONECT 6010 5969 6020
CONECT 6011 6020
CONECT 6012 6020
CONECT 6013 6020
CONECT 6014 5970
CONECT 6015 5972
CONECT 6016 5971 5973
CONECT 6017 5973 5974
CONECT 6018 5976
CONECT 6019 5992
CONECT 6020 6010 6011 6012 6013
CONECT 6021 5479 6022 6032
CONECT 6022 6021 6023 6029
CONECT 6023 6022 6024 6030
CONECT 6024 6023 6025 6031
CONECT 6025 6024 6026 6032
CONECT 6026 6025 6033
CONECT 6027 6028 6029 6034
CONECT 6028 6027
CONECT 6029 6022 6027
CONECT 6030 6023
CONECT 6031 6024
CONECT 6032 6021 6025
CONECT 6033 6026
CONECT 6034 6027
CONECT 6035 5760 6036 6046
CONECT 6036 6035 6037 6043
CONECT 6037 6036 6038 6044
CONECT 6038 6037 6039 6045
CONECT 6039 6038 6040 6046
CONECT 6040 6039 6047
CONECT 6041 6042 6043 6048
CONECT 6042 6041
CONECT 6043 6036 6041
CONECT 6044 6037
CONECT 6045 6038
CONECT 6046 6035 6039
CONECT 6047 6040
CONECT 6048 6041
CONECT 6049 6050 6054 6090
CONECT 6050 6049 6051 6091
CONECT 6051 6050 6052 6095
CONECT 6052 6051 6053 6097
CONECT 6053 6052 6096
CONECT 6054 6049 6097 6098
CONECT 6055 6056 6098
CONECT 6056 6055 6073 6089
CONECT 6057 6058 6089 6099
CONECT 6058 6057 6059
CONECT 6059 6058 6060
CONECT 6060 6059 6061
CONECT 6061 6060 6062
CONECT 6062 6061 6063
CONECT 6063 6062 6064
CONECT 6064 6063 6065
CONECT 6065 6064 6066
CONECT 6066 6065 6067
CONECT 6067 6066 6068
CONECT 6068 6067 6069
CONECT 6069 6068 6070
CONECT 6070 6069 6071
CONECT 6071 6070 6072
CONECT 6072 6071
CONECT 6073 6056 6074 6100
CONECT 6074 6073 6075
CONECT 6075 6074 6076
CONECT 6076 6075 6077
CONECT 6077 6076 6078
CONECT 6078 6077 6079
CONECT 6079 6078 6080
CONECT 6080 6079 6081
CONECT 6081 6080 6082
CONECT 6082 6081 6083
CONECT 6083 6082 6084
CONECT 6084 6083 6085
CONECT 6085 6084 6086
CONECT 6086 6085 6087
CONECT 6087 6086 6088
CONECT 6088 6087
CONECT 6089 6056 6057
CONECT 6090 6049
CONECT 6091 6050 6101
CONECT 6092 6101
CONECT 6093 6101
CONECT 6094 6101
CONECT 6095 6051
CONECT 6096 6053
CONECT 6097 6052 6054
CONECT 6098 6054 6055
CONECT 6099 6057
CONECT 6100 6073
CONECT 6101 6091 6092 6093 6094
MASTER 600 0 12 11 51 0 0 6 6353 2 307 64
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