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*** IMMUNE SYSTEM 28-APR-21 7MLM ***elNémo ID: 2403091708342514661Job options:ID = 2403091708342514661 JOBID = IMMUNE SYSTEM 28-APR-21 7MLM USERID = unknown 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 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
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 SOFTWARE USED: UCSF CHIMERA 1.17.3_b42480.
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 -0.994277 -0.104095 0.024030 22.56642
REMARK 350 BIOMT2 2 -0.104095 0.893382 -0.437072 -1.93445
REMARK 350 BIOMT3 2 0.024030 -0.437072 -0.899105 -13.75449
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 1 ALA A 168 SER A 171 1 4
HELIX 2 2 ASN A 192 GLU A 199 1 8
HELIX 3 3 SER A 239 LEU A 249 1 11
HELIX 4 4 PRO A 273 ASP A 281 1 9
HELIX 5 5 ASP A 297 LYS A 301 1 5
HELIX 6 6 HIS A 303 LEU A 305 1 3
HELIX 7 7 TYR A 391 LEU A 394 1 4
HELIX 8 8 LYS A 482 ASN A 484 1 3
HELIX 9 9 SER A 535 TYR A 538 1 4
HELIX 10 10 ASP A 586 LYS A 594 1 9
HELIX 11 11 VAL A 612 SER A 614 1 3
SHEET 1 1 1 ILE A 29 VAL A 32 0
SHEET 2 2 1 THR A 36 GLN A 38 0
SHEET 3 3 1 ASN A 57 ASP A 59 0
SHEET 4 4 1 TRP A 81 ASP A 83 0
SHEET 5 5 1 ASN A 105 ILE A 107 0
SHEET 6 6 1 ASN A 129 VAL A 131 0
SHEET 7 7 1 LYS A 153 ASN A 155 0
SHEET 8 8 1 HIS A 178 ASP A 180 0
SHEET 9 9 1 SER A 206 ASP A 208 0
SHEET 10 10 1 GLU A 229 ARG A 233 0
SHEET 11 11 1 ARG A 256 GLY A 260 0
SHEET 12 12 1 GLU A 286 LEU A 289 0
SHEET 13 13 1 ALA A 310 ALA A 314 0
SHEET 14 14 1 SER A 332 ILE A 336 0
SHEET 15 15 1 SER A 353 THR A 357 0
SHEET 16 16 1 TYR A 375 ASP A 377 0
SHEET 17 17 1 PHE A 385 CYS A 388 0
SHEET 18 18 1 HIS A 401 ASP A 403 0
SHEET 19 19 1 ALA A 409 MET A 412 0
SHEET 20 20 1 HIS A 424 ASP A 426 0
SHEET 21 21 1 THR A 431 LYS A 433 0
SHEET 22 22 1 TYR A 449 ASP A 451 0
SHEET 23 23 1 THR A 473 LYS A 475 0
SHEET 24 24 1 PHE A 498 ASP A 500 0
SHEET 25 25 1 LEU A 522 ASN A 524 0
SHEET 26 26 1 GLU A 546 ALA A 548 0
SHEET 27 27 1 LYS A 570 TRP A 572 0
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 2.324 1.504 -58.951 1.00 64.31 N
ANISOU 1 N PRO A 27 4902 9726 9806 -328 645 -1177 N
ATOM 2 CA PRO A 27 1.426 0.877 -57.977 1.00 62.77 C
ANISOU 2 CA PRO A 27 4777 9466 9606 -155 581 -1178 C
ATOM 3 C PRO A 27 2.187 0.271 -56.803 1.00 59.58 C
ANISOU 3 C PRO A 27 4508 8893 9237 11 633 -1132 C
ATOM 4 O PRO A 27 1.579 -0.123 -55.810 1.00 56.85 O
ANISOU 4 O PRO A 27 4236 8490 8874 177 599 -1124 O
ATOM 5 CB PRO A 27 0.738 -0.211 -58.798 1.00 59.64 C
ANISOU 5 CB PRO A 27 4459 8939 9263 -315 554 -1253 C
ATOM 6 CG PRO A 27 1.770 -0.606 -59.797 1.00 61.55 C
ANISOU 6 CG PRO A 27 4760 9055 9570 -512 651 -1265 C
ATOM 7 CD PRO A 27 2.511 0.661 -60.146 1.00 64.63 C
ANISOU 7 CD PRO A 27 5027 9618 9913 -559 692 -1235 C
ATOM 8 N CYS A 28 3.508 0.199 -56.933 1.00 57.73 N
ANISOU 8 N CYS A 28 4315 8581 9039 -40 720 -1101 N
ATOM 9 CA CYS A 28 4.379 -0.382 -55.921 1.00 53.84 C
ANISOU 9 CA CYS A 28 3953 7942 8561 82 779 -1058 C
ATOM 10 C CYS A 28 4.842 0.697 -54.955 1.00 49.95 C
ANISOU 10 C CYS A 28 3410 7566 8005 246 807 -995 C
ATOM 11 O CYS A 28 5.319 1.752 -55.379 1.00 55.24 O
ANISOU 11 O CYS A 28 3958 8381 8651 206 827 -966 O
ATOM 12 CB CYS A 28 5.591 -1.049 -56.567 1.00 52.29 C
ANISOU 12 CB CYS A 28 3832 7614 8423 -50 864 -1045 C
ATOM 13 SG CYS A 28 5.226 -2.484 -57.587 1.00 62.32 S
ANISOU 13 SG CYS A 28 5249 8690 9739 -211 858 -1073 S
ATOM 14 N ILE A 29 4.713 0.423 -53.659 1.00 39.64 N
ANISOU 14 N ILE A 29 2208 6187 6667 425 819 -974 N
ATOM 15 CA ILE A 29 5.234 1.337 -52.647 1.00 46.22 C
ANISOU 15 CA ILE A 29 3029 7091 7441 585 873 -912 C
ATOM 16 C ILE A 29 6.751 1.364 -52.746 1.00 50.37 C
ANISOU 16 C ILE A 29 3580 7575 7984 519 954 -880 C
ATOM 17 O ILE A 29 7.421 0.341 -52.552 1.00 48.41 O
ANISOU 17 O ILE A 29 3461 7173 7759 477 994 -889 O
ATOM 18 CB ILE A 29 4.775 0.925 -51.242 1.00 43.60 C
ANISOU 18 CB ILE A 29 2843 6656 7068 771 894 -907 C
ATOM 19 CG1 ILE A 29 3.273 1.152 -51.081 1.00 43.15 C
ANISOU 19 CG1 ILE A 29 2749 6671 6975 874 822 -916 C
ATOM 20 CG2 ILE A 29 5.554 1.690 -50.181 1.00 42.74 C
ANISOU 20 CG2 ILE A 29 2764 6572 6903 913 987 -846 C
ATOM 21 CD1 ILE A 29 2.797 1.093 -49.645 1.00 44.52 C
ANISOU 21 CD1 ILE A 29 3063 6766 7088 1086 867 -891 C
ATOM 22 N GLU A 30 7.302 2.535 -53.051 1.00 53.71 N
ANISOU 22 N GLU A 30 3875 8146 8387 510 979 -836 N
ATOM 23 CA GLU A 30 8.747 2.711 -53.052 1.00 58.47 C
ANISOU 23 CA GLU A 30 4496 8725 8995 470 1057 -796 C
ATOM 24 C GLU A 30 9.238 2.777 -51.610 1.00 64.61 C
ANISOU 24 C GLU A 30 5377 9449 9722 638 1123 -760 C
ATOM 25 O GLU A 30 8.857 3.680 -50.861 1.00 73.16 O
ANISOU 25 O GLU A 30 6419 10621 10757 793 1139 -724 O
ATOM 26 CB GLU A 30 9.129 3.973 -53.819 1.00 62.06 C
ANISOU 26 CB GLU A 30 4782 9355 9443 408 1064 -763 C
ATOM 27 CG GLU A 30 10.617 4.104 -54.099 1.00 66.84 C
ANISOU 27 CG GLU A 30 5398 9934 10062 334 1138 -727 C
ATOM 28 CD GLU A 30 10.902 4.824 -55.405 1.00 70.72 C
ANISOU 28 CD GLU A 30 5755 10538 10576 173 1139 -729 C
ATOM 29 OE1 GLU A 30 10.032 4.802 -56.301 1.00 73.23 O
ANISOU 29 OE1 GLU A 30 6008 10906 10909 59 1087 -781 O
ATOM 30 OE2 GLU A 30 11.994 5.412 -55.540 1.00 71.49 O
ANISOU 30 OE2 GLU A 30 5818 10675 10670 151 1197 -685 O
ATOM 31 N VAL A 31 10.073 1.819 -51.217 1.00 60.37 N
ANISOU 31 N VAL A 31 4979 8773 9188 607 1170 -768 N
ATOM 32 CA VAL A 31 10.555 1.694 -49.845 1.00 49.44 C
ANISOU 32 CA VAL A 31 3717 7323 7746 729 1242 -756 C
ATOM 33 C VAL A 31 11.965 2.258 -49.698 1.00 48.15 C
ANISOU 33 C VAL A 31 3533 7204 7557 719 1315 -709 C
ATOM 34 O VAL A 31 12.209 3.127 -48.860 1.00 57.20 O
ANISOU 34 O VAL A 31 4672 8407 8656 842 1372 -676 O
ATOM 35 CB VAL A 31 10.487 0.225 -49.369 1.00 41.83 C
ANISOU 35 CB VAL A 31 2920 6196 6776 699 1246 -803 C
ATOM 36 CG1 VAL A 31 11.222 0.062 -48.051 1.00 36.54 C
ANISOU 36 CG1 VAL A 31 2377 5470 6035 773 1335 -803 C
ATOM 37 CG2 VAL A 31 9.035 -0.216 -49.233 1.00 43.86 C
ANISOU 37 CG2 VAL A 31 3214 6405 7045 747 1182 -848 C
ATOM 38 N VAL A 32 12.909 1.762 -50.498 1.00 44.68 N
ANISOU 38 N VAL A 32 3092 6738 7146 582 1323 -699 N
ATOM 39 CA VAL A 32 14.240 2.340 -50.614 1.00 45.54 C
ANISOU 39 CA VAL A 32 3161 6905 7237 555 1380 -650 C
ATOM 40 C VAL A 32 14.447 2.645 -52.097 1.00 51.58 C
ANISOU 40 C VAL A 32 3812 7728 8059 419 1355 -634 C
ATOM 41 O VAL A 32 14.444 1.721 -52.916 1.00 55.17 O
ANISOU 41 O VAL A 32 4305 8103 8553 306 1340 -653 O
ATOM 42 CB VAL A 32 15.341 1.408 -50.094 1.00 38.84 C
ANISOU 42 CB VAL A 32 2438 5972 6346 527 1434 -645 C
ATOM 43 CG1 VAL A 32 16.693 2.111 -50.133 1.00 38.52 C
ANISOU 43 CG1 VAL A 32 2351 6005 6279 516 1491 -592 C
ATOM 44 CG2 VAL A 32 15.018 0.926 -48.683 1.00 37.32 C
ANISOU 44 CG2 VAL A 32 2377 5709 6095 623 1466 -684 C
ATOM 45 N PRO A 33 14.619 3.908 -52.488 1.00 53.87 N
ANISOU 45 N PRO A 33 3966 8152 8352 422 1361 -601 N
ATOM 46 CA PRO A 33 14.555 4.262 -53.916 1.00 51.82 C
ANISOU 46 CA PRO A 33 3593 7953 8142 276 1339 -607 C
ATOM 47 C PRO A 33 15.498 3.444 -54.787 1.00 45.86 C
ANISOU 47 C PRO A 33 2901 7104 7419 139 1382 -601 C
ATOM 48 O PRO A 33 16.680 3.285 -54.480 1.00 44.09 O
ANISOU 48 O PRO A 33 2732 6854 7168 156 1438 -560 O
ATOM 49 CB PRO A 33 14.933 5.748 -53.924 1.00 50.35 C
ANISOU 49 CB PRO A 33 3268 7926 7936 317 1361 -557 C
ATOM 50 CG PRO A 33 14.503 6.239 -52.591 1.00 48.35 C
ANISOU 50 CG PRO A 33 3029 7707 7634 509 1369 -534 C
ATOM 51 CD PRO A 33 14.754 5.100 -51.634 1.00 51.00 C
ANISOU 51 CD PRO A 33 3542 7892 7942 562 1395 -558 C
ATOM 52 N ASN A 34 14.948 2.909 -55.883 1.00 47.33 N
ANISOU 52 N ASN A 34 3082 7241 7659 9 1363 -641 N
ATOM 53 CA ASN A 34 15.692 2.126 -56.875 1.00 47.72 C
ANISOU 53 CA ASN A 34 3195 7190 7746 -118 1424 -631 C
ATOM 54 C ASN A 34 16.339 0.884 -56.269 1.00 46.26 C
ANISOU 54 C ASN A 34 3156 6886 7534 -61 1456 -601 C
ATOM 55 O ASN A 34 17.212 0.271 -56.888 1.00 45.22 O
ANISOU 55 O ASN A 34 3081 6690 7411 -121 1523 -564 O
ATOM 56 CB ASN A 34 16.754 2.979 -57.581 1.00 50.74 C
ANISOU 56 CB ASN A 34 3504 7643 8132 -192 1489 -593 C
ATOM 57 CG ASN A 34 16.149 4.014 -58.508 1.00 55.86 C
ANISOU 57 CG ASN A 34 4013 8406 8804 -302 1471 -630 C
ATOM 58 OD1 ASN A 34 14.929 4.149 -58.588 1.00 59.68 O
ANISOU 58 OD1 ASN A 34 4445 8937 9294 -316 1403 -681 O
ATOM 59 ND2 ASN A 34 17.000 4.758 -59.206 1.00 58.01 N
ANISOU 59 ND2 ASN A 34 4222 8738 9081 -386 1531 -605 N
ATOM 60 N ILE A 35 15.926 0.489 -55.064 1.00 42.68 N
ANISOU 60 N ILE A 35 2768 6411 7039 55 1416 -614 N
ATOM 61 CA ILE A 35 16.544 -0.652 -54.398 1.00 44.02 C
ANISOU 61 CA ILE A 35 3066 6500 7159 99 1443 -592 C
ATOM 62 C ILE A 35 15.489 -1.634 -53.896 1.00 40.06 C
ANISOU 62 C ILE A 35 2648 5916 6658 133 1394 -640 C
ATOM 63 O ILE A 35 15.556 -2.830 -54.197 1.00 38.98 O
ANISOU 63 O ILE A 35 2593 5695 6521 97 1407 -632 O
ATOM 64 CB ILE A 35 17.464 -0.192 -53.251 1.00 43.77 C
ANISOU 64 CB ILE A 35 3051 6530 7051 192 1474 -562 C
ATOM 65 CG1 ILE A 35 18.766 0.386 -53.815 1.00 45.70 C
ANISOU 65 CG1 ILE A 35 3243 6834 7285 149 1533 -504 C
ATOM 66 CG2 ILE A 35 17.745 -1.341 -52.294 1.00 36.82 C
ANISOU 66 CG2 ILE A 35 2296 5592 6100 237 1486 -566 C
ATOM 67 CD1 ILE A 35 19.883 0.517 -52.801 1.00 49.39 C
ANISOU 67 CD1 ILE A 35 3748 7349 7670 220 1573 -470 C
ATOM 68 N THR A 36 14.517 -1.148 -53.127 1.00 37.12 N
ANISOU 68 N THR A 36 2255 5569 6278 213 1344 -682 N
ATOM 69 CA THR A 36 13.532 -2.018 -52.495 1.00 36.59 C
ANISOU 69 CA THR A 36 2276 5424 6204 259 1302 -730 C
ATOM 70 C THR A 36 12.129 -1.540 -52.824 1.00 39.53 C
ANISOU 70 C THR A 36 2575 5819 6624 266 1232 -776 C
ATOM 71 O THR A 36 11.798 -0.372 -52.594 1.00 40.85 O
ANISOU 71 O THR A 36 2650 6090 6783 327 1217 -773 O
ATOM 72 CB THR A 36 13.715 -2.055 -50.977 1.00 39.96 C
ANISOU 72 CB THR A 36 2785 5846 6552 370 1328 -741 C
ATOM 73 OG1 THR A 36 15.049 -2.470 -50.666 1.00 44.45 O
ANISOU 73 OG1 THR A 36 3407 6421 7061 351 1389 -703 O
ATOM 74 CG2 THR A 36 12.733 -3.029 -50.360 1.00 34.20 C
ANISOU 74 CG2 THR A 36 2159 5026 5810 403 1295 -796 C
ATOM 75 N TYR A 37 11.299 -2.444 -53.338 1.00 38.25 N
ANISOU 75 N TYR A 37 2452 5576 6504 211 1191 -813 N
ATOM 76 CA TYR A 37 9.935 -2.105 -53.718 1.00 35.62 C
ANISOU 76 CA TYR A 37 2051 5274 6211 205 1118 -861 C
ATOM 77 C TYR A 37 8.956 -3.096 -53.108 1.00 41.43 C
ANISOU 77 C TYR A 37 2888 5910 6941 260 1072 -905 C
ATOM 78 O TYR A 37 9.200 -4.307 -53.097 1.00 38.03 O
ANISOU 78 O TYR A 37 2564 5374 6512 227 1090 -906 O
ATOM 79 CB TYR A 37 9.794 -2.058 -55.236 1.00 36.23 C
ANISOU 79 CB TYR A 37 2052 5359 6355 46 1115 -875 C
ATOM 80 CG TYR A 37 10.408 -0.804 -55.803 1.00 44.34 C
ANISOU 80 CG TYR A 37 2954 6515 7379 -5 1145 -848 C
ATOM 81 CD1 TYR A 37 11.770 -0.730 -56.061 1.00 44.84 C
ANISOU 81 CD1 TYR A 37 3032 6568 7436 -44 1224 -796 C
ATOM 82 CD2 TYR A 37 9.632 0.320 -56.040 1.00 43.80 C
ANISOU 82 CD2 TYR A 37 2747 6594 7300 -7 1092 -872 C
ATOM 83 CE1 TYR A 37 12.336 0.423 -56.560 1.00 48.39 C
ANISOU 83 CE1 TYR A 37 3370 7134 7881 -91 1253 -773 C
ATOM 84 CE2 TYR A 37 10.187 1.477 -56.541 1.00 48.32 C
ANISOU 84 CE2 TYR A 37 3200 7301 7860 -57 1119 -847 C
ATOM 85 CZ TYR A 37 11.540 1.524 -56.802 1.00 50.97 C
ANISOU 85 CZ TYR A 37 3560 7607 8201 -102 1200 -801 C
ATOM 86 OH TYR A 37 12.099 2.677 -57.304 1.00 54.61 O
ANISOU 86 OH TYR A 37 3902 8196 8649 -154 1229 -777 O
ATOM 87 N GLN A 38 7.855 -2.561 -52.589 1.00 43.82 N
ANISOU 87 N GLN A 38 3158 6261 7230 353 1017 -935 N
ATOM 88 CA GLN A 38 6.826 -3.327 -51.891 1.00 40.03 C
ANISOU 88 CA GLN A 38 2777 5695 6738 428 974 -978 C
ATOM 89 C GLN A 38 5.560 -3.293 -52.741 1.00 40.26 C
ANISOU 89 C GLN A 38 2752 5746 6796 374 880 -1007 C
ATOM 90 O GLN A 38 4.784 -2.336 -52.673 1.00 43.49 O
ANISOU 90 O GLN A 38 3054 6277 7192 441 840 -1016 O
ATOM 91 CB GLN A 38 6.588 -2.756 -50.493 1.00 42.70 C
ANISOU 91 CB GLN A 38 3166 6054 7005 597 999 -971 C
ATOM 92 CG GLN A 38 5.435 -3.385 -49.733 1.00 45.37 C
ANISOU 92 CG GLN A 38 3615 6304 7320 686 964 -1014 C
ATOM 93 CD GLN A 38 5.628 -4.868 -49.509 1.00 57.66 C
ANISOU 93 CD GLN A 38 5332 7717 8860 621 968 -1037 C
ATOM 94 OE1 GLN A 38 5.370 -5.678 -50.396 1.00 63.26 O
ANISOU 94 OE1 GLN A 38 6061 8375 9601 516 911 -1040 O
ATOM 95 NE2 GLN A 38 6.088 -5.233 -48.318 1.00 61.09 N
ANISOU 95 NE2 GLN A 38 5885 8093 9233 680 1044 -1053 N
ATOM 96 N CYS A 39 5.359 -4.333 -53.547 1.00 41.62 N
ANISOU 96 N CYS A 39 3001 5815 6997 257 850 -1018 N
ATOM 97 CA CYS A 39 4.218 -4.427 -54.446 1.00 43.85 C
ANISOU 97 CA CYS A 39 3255 6104 7304 176 769 -1051 C
ATOM 98 C CYS A 39 3.126 -5.354 -53.920 1.00 37.21 C
ANISOU 98 C CYS A 39 2544 5158 6436 236 700 -1076 C
ATOM 99 O CYS A 39 2.240 -5.743 -54.687 1.00 35.66 O
ANISOU 99 O CYS A 39 2359 4931 6259 155 637 -1103 O
ATOM 100 CB CYS A 39 4.671 -4.905 -55.831 1.00 46.47 C
ANISOU 100 CB CYS A 39 3592 6378 7686 -5 801 -1046 C
ATOM 101 SG CYS A 39 6.072 -4.023 -56.575 1.00 54.80 S
ANISOU 101 SG CYS A 39 4525 7521 8775 -99 904 -1016 S
ATOM 102 N MET A 40 3.168 -5.709 -52.637 1.00 33.60 N
ANISOU 102 N MET A 40 2191 4643 5931 365 719 -1072 N
ATOM 103 CA MET A 40 2.231 -6.680 -52.084 1.00 31.62 C
ANISOU 103 CA MET A 40 2082 4281 5652 413 667 -1099 C
ATOM 104 C MET A 40 0.787 -6.215 -52.223 1.00 35.33 C
ANISOU 104 C MET A 40 2499 4807 6118 459 579 -1125 C
ATOM 105 O MET A 40 0.469 -5.043 -51.998 1.00 44.83 O
ANISOU 105 O MET A 40 3582 6147 7304 546 574 -1117 O
ATOM 106 CB MET A 40 2.544 -6.929 -50.607 1.00 30.79 C
ANISOU 106 CB MET A 40 2091 4122 5485 534 726 -1103 C
ATOM 107 CG MET A 40 1.612 -7.912 -49.920 1.00 40.62 C
ANISOU 107 CG MET A 40 3491 5252 6692 582 687 -1136 C
ATOM 108 SD MET A 40 1.871 -7.951 -48.138 1.00 48.77 S
ANISOU 108 SD MET A 40 4659 6232 7641 713 783 -1159 S
ATOM 109 CE MET A 40 3.652 -8.110 -48.077 1.00 46.67 C
ANISOU 109 CE MET A 40 4375 5996 7361 635 881 -1138 C
ATOM 110 N ASP A 41 -0.087 -7.152 -52.597 1.00 31.22 N
ANISOU 110 N ASP A 41 2064 4192 5605 408 511 -1150 N
ATOM 111 CA ASP A 41 -1.539 -6.977 -52.548 1.00 34.74 C
ANISOU 111 CA ASP A 41 2495 4670 6033 466 424 -1177 C
ATOM 112 C ASP A 41 -1.971 -5.715 -53.294 1.00 37.72 C
ANISOU 112 C ASP A 41 2673 5243 6418 440 388 -1181 C
ATOM 113 O ASP A 41 -2.621 -4.819 -52.751 1.00 42.08 O
ANISOU 113 O ASP A 41 3141 5921 6925 576 368 -1172 O
ATOM 114 CB ASP A 41 -2.029 -6.962 -51.096 1.00 36.21 C
ANISOU 114 CB ASP A 41 2778 4819 6161 651 441 -1176 C
ATOM 115 CG ASP A 41 -3.546 -6.969 -50.982 1.00 39.39 C
ANISOU 115 CG ASP A 41 3193 5235 6540 726 358 -1196 C
ATOM 116 OD1 ASP A 41 -4.229 -7.177 -52.006 1.00 38.21 O
ANISOU 116 OD1 ASP A 41 2991 5109 6416 619 278 -1218 O
ATOM 117 OD2 ASP A 41 -4.056 -6.759 -49.862 1.00 44.30 O
ANISOU 117 OD2 ASP A 41 3882 5840 7110 893 383 -1189 O
ATOM 118 N GLN A 42 -1.588 -5.658 -54.571 1.00 33.23 N
ANISOU 118 N GLN A 42 2027 4705 5894 261 391 -1194 N
ATOM 119 CA GLN A 42 -1.941 -4.543 -55.441 1.00 35.70 C
ANISOU 119 CA GLN A 42 2144 5216 6205 184 362 -1215 C
ATOM 120 C GLN A 42 -2.772 -4.994 -56.637 1.00 34.98 C
ANISOU 120 C GLN A 42 2048 5108 6133 11 305 -1267 C
ATOM 121 O GLN A 42 -2.894 -4.253 -57.618 1.00 45.28 O
ANISOU 121 O GLN A 42 3204 6561 7439 -126 300 -1301 O
ATOM 122 CB GLN A 42 -0.681 -3.809 -55.907 1.00 36.84 C
ANISOU 122 CB GLN A 42 2182 5440 6375 105 444 -1195 C
ATOM 123 CG GLN A 42 0.048 -3.041 -54.801 1.00 44.95 C
ANISOU 123 CG GLN A 42 3170 6536 7373 273 501 -1149 C
ATOM 124 CD GLN A 42 -0.738 -1.843 -54.277 1.00 54.90 C
ANISOU 124 CD GLN A 42 4284 8004 8571 424 464 -1138 C
ATOM 125 OE1 GLN A 42 -1.867 -1.587 -54.696 1.00 62.86 O
ANISOU 125 OE1 GLN A 42 5208 9126 9550 409 387 -1165 O
ATOM 126 NE2 GLN A 42 -0.135 -1.102 -53.356 1.00 53.65 N
ANISOU 126 NE2 GLN A 42 4094 7907 8384 577 529 -1093 N
ATOM 127 N LYS A 43 -3.350 -6.197 -56.569 1.00 33.75 N
ANISOU 127 N LYS A 43 2054 4781 5988 5 267 -1279 N
ATOM 128 CA LYS A 43 -4.153 -6.769 -57.651 1.00 34.03 C
ANISOU 128 CA LYS A 43 2119 4767 6042 -155 222 -1329 C
ATOM 129 C LYS A 43 -3.375 -6.839 -58.961 1.00 43.70 C
ANISOU 129 C LYS A 43 3333 5955 7316 -368 300 -1343 C
ATOM 130 O LYS A 43 -3.954 -6.742 -60.046 1.00 49.74 O
ANISOU 130 O LYS A 43 4054 6759 8087 -538 287 -1399 O
ATOM 131 CB LYS A 43 -5.457 -5.995 -57.851 1.00 35.84 C
ANISOU 131 CB LYS A 43 2206 5190 6224 -149 132 -1373 C
ATOM 132 CG LYS A 43 -6.452 -6.195 -56.729 1.00 41.65 C
ANISOU 132 CG LYS A 43 2996 5917 6912 52 61 -1358 C
ATOM 133 CD LYS A 43 -7.762 -5.494 -57.037 1.00 52.87 C
ANISOU 133 CD LYS A 43 4268 7545 8275 57 -26 -1395 C
ATOM 134 CE LYS A 43 -8.861 -5.971 -56.105 1.00 58.39 C
ANISOU 134 CE LYS A 43 5063 8188 8935 235 -92 -1383 C
ATOM 135 NZ LYS A 43 -10.169 -5.339 -56.415 1.00 64.91 N
ANISOU 135 NZ LYS A 43 5740 9231 9693 250 -179 -1412 N
ATOM 136 N LEU A 44 -2.060 -7.007 -58.870 1.00 41.09 N
ANISOU 136 N LEU A 44 3049 5548 7014 -366 392 -1295 N
ATOM 137 CA LEU A 44 -1.238 -7.095 -60.067 1.00 39.76 C
ANISOU 137 CA LEU A 44 2891 5326 6889 -549 490 -1296 C
ATOM 138 C LEU A 44 -1.464 -8.426 -60.767 1.00 33.85 C
ANISOU 138 C LEU A 44 2323 4371 6167 -641 515 -1296 C
ATOM 139 O LEU A 44 -1.515 -9.478 -60.129 1.00 34.03 O
ANISOU 139 O LEU A 44 2486 4261 6183 -536 495 -1259 O
ATOM 140 CB LEU A 44 0.237 -6.920 -59.707 1.00 37.87 C
ANISOU 140 CB LEU A 44 2652 5072 6664 -497 583 -1234 C
ATOM 141 CG LEU A 44 0.579 -5.588 -59.043 1.00 37.14 C
ANISOU 141 CG LEU A 44 2390 5176 6547 -405 576 -1227 C
ATOM 142 CD1 LEU A 44 2.040 -5.546 -58.629 1.00 34.97 C
ANISOU 142 CD1 LEU A 44 2134 4868 6285 -351 670 -1166 C
ATOM 143 CD2 LEU A 44 0.243 -4.430 -59.972 1.00 37.07 C
ANISOU 143 CD2 LEU A 44 2196 5356 6531 -546 572 -1282 C
ATOM 144 N SER A 45 -1.623 -8.369 -62.091 1.00 34.95 N
ANISOU 144 N SER A 45 2460 4489 6331 -843 569 -1340 N
ATOM 145 CA SER A 45 -1.696 -9.575 -62.905 1.00 39.86 C
ANISOU 145 CA SER A 45 3264 4901 6979 -937 630 -1330 C
ATOM 146 C SER A 45 -0.326 -10.053 -63.370 1.00 40.78 C
ANISOU 146 C SER A 45 3480 4890 7125 -965 779 -1256 C
ATOM 147 O SER A 45 -0.162 -11.249 -63.641 1.00 41.56 O
ANISOU 147 O SER A 45 3750 4809 7231 -952 834 -1206 O
ATOM 148 CB SER A 45 -2.598 -9.344 -64.125 1.00 49.16 C
ANISOU 148 CB SER A 45 4420 6098 8160 -1152 637 -1420 C
ATOM 149 OG SER A 45 -3.970 -9.375 -63.767 1.00 64.84 O
ANISOU 149 OG SER A 45 6371 8150 10113 -1115 503 -1473 O
ATOM 150 N LYS A 46 0.656 -9.154 -63.449 1.00 46.43 N
ANISOU 150 N LYS A 46 4088 5702 7850 -988 847 -1241 N
ATOM 151 CA LYS A 46 2.004 -9.470 -63.913 1.00 49.40 C
ANISOU 151 CA LYS A 46 4541 5978 8249 -1010 997 -1168 C
ATOM 152 C LYS A 46 2.992 -8.556 -63.198 1.00 46.87 C
ANISOU 152 C LYS A 46 4088 5798 7923 -923 1006 -1137 C
ATOM 153 O LYS A 46 2.599 -7.598 -62.529 1.00 49.34 O
ANISOU 153 O LYS A 46 4250 6281 8216 -869 913 -1177 O
ATOM 154 CB LYS A 46 2.121 -9.312 -65.435 1.00 57.87 C
ANISOU 154 CB LYS A 46 5657 6979 9352 -1235 1132 -1205 C
ATOM 155 CG LYS A 46 1.431 -10.421 -66.207 1.00 70.74 C
ANISOU 155 CG LYS A 46 7469 8419 10989 -1312 1172 -1212 C
ATOM 156 CD LYS A 46 1.265 -10.107 -67.683 1.00 79.19 C
ANISOU 156 CD LYS A 46 8577 9431 12080 -1565 1303 -1282 C
ATOM 157 CE LYS A 46 0.595 -11.283 -68.380 1.00 78.83 C
ANISOU 157 CE LYS A 46 8736 9177 12039 -1623 1355 -1280 C
ATOM 158 NZ LYS A 46 0.359 -11.077 -69.835 1.00 74.39 N
ANISOU 158 NZ LYS A 46 8249 8530 11486 -1881 1502 -1357 N
ATOM 159 N VAL A 47 4.277 -8.858 -63.350 1.00 45.66 N
ANISOU 159 N VAL A 47 3994 5576 7780 -899 1127 -1058 N
ATOM 160 CA VAL A 47 5.296 -8.007 -62.719 1.00 46.12 C
ANISOU 160 CA VAL A 47 3931 5760 7832 -825 1148 -1027 C
ATOM 161 C VAL A 47 5.334 -6.660 -63.436 1.00 49.04 C
ANISOU 161 C VAL A 47 4146 6264 8222 -974 1180 -1091 C
ATOM 162 O VAL A 47 5.327 -6.619 -64.682 1.00 54.48 O
ANISOU 162 O VAL A 47 4873 6890 8936 -1158 1278 -1122 O
ATOM 163 CB VAL A 47 6.669 -8.700 -62.732 1.00 49.59 C
ANISOU 163 CB VAL A 47 4467 6108 8268 -761 1271 -924 C
ATOM 164 CG1 VAL A 47 6.571 -10.097 -63.335 1.00 50.29 C
ANISOU 164 CG1 VAL A 47 4746 6010 8351 -769 1336 -871 C
ATOM 165 CG2 VAL A 47 7.743 -7.841 -63.426 1.00 47.39 C
ANISOU 165 CG2 VAL A 47 4115 5874 8016 -854 1397 -907 C
ATOM 166 N PRO A 48 5.327 -5.545 -62.711 1.00 49.90 N
ANISOU 166 N PRO A 48 4083 6562 8313 -910 1110 -1115 N
ATOM 167 CA PRO A 48 5.310 -4.236 -63.373 1.00 56.95 C
ANISOU 167 CA PRO A 48 4806 7621 9210 -1052 1133 -1177 C
ATOM 168 C PRO A 48 6.642 -3.934 -64.041 1.00 63.36 C
ANISOU 168 C PRO A 48 5619 8404 10052 -1139 1285 -1140 C
ATOM 169 O PRO A 48 7.712 -4.136 -63.461 1.00 65.44 O
ANISOU 169 O PRO A 48 5915 8632 10319 -1018 1332 -1061 O
ATOM 170 CB PRO A 48 5.026 -3.258 -62.225 1.00 55.06 C
ANISOU 170 CB PRO A 48 4400 7587 8933 -901 1024 -1185 C
ATOM 171 CG PRO A 48 4.457 -4.106 -61.124 1.00 48.92 C
ANISOU 171 CG PRO A 48 3725 6728 8133 -720 932 -1157 C
ATOM 172 CD PRO A 48 5.143 -5.426 -61.258 1.00 50.29 C
ANISOU 172 CD PRO A 48 4091 6689 8328 -708 1007 -1096 C
ATOM 173 N ASP A 49 6.566 -3.447 -65.279 1.00 66.73 N
ANISOU 173 N ASP A 49 6012 8848 10492 -1360 1369 -1203 N
ATOM 174 CA ASP A 49 7.752 -3.001 -65.995 1.00 72.29 C
ANISOU 174 CA ASP A 49 6721 9534 11210 -1456 1516 -1174 C
ATOM 175 C ASP A 49 8.259 -1.650 -65.508 1.00 72.06 C
ANISOU 175 C ASP A 49 6522 9722 11134 -1400 1465 -1165 C
ATOM 176 O ASP A 49 9.340 -1.224 -65.931 1.00 74.49 O
ANISOU 176 O ASP A 49 6834 10025 11443 -1446 1568 -1128 O
ATOM 177 CB ASP A 49 7.464 -2.943 -67.499 1.00 73.21 C
ANISOU 177 CB ASP A 49 6926 9577 11312 -1701 1613 -1236 C
ATOM 178 CG ASP A 49 7.380 -4.323 -68.129 1.00 74.81 C
ANISOU 178 CG ASP A 49 7348 9516 11561 -1748 1727 -1210 C
ATOM 179 OD1 ASP A 49 7.805 -5.302 -67.480 1.00 75.02 O
ANISOU 179 OD1 ASP A 49 7475 9423 11607 -1573 1731 -1116 O
ATOM 180 OD2 ASP A 49 6.879 -4.431 -69.268 1.00 78.99 O
ANISOU 180 OD2 ASP A 49 7983 9963 12066 -1931 1792 -1268 O
ATOM 181 N ASP A 50 7.515 -0.971 -64.630 1.00 69.66 N
ANISOU 181 N ASP A 50 6078 9604 10785 -1291 1317 -1188 N
ATOM 182 CA ASP A 50 7.966 0.296 -64.066 1.00 70.70 C
ANISOU 182 CA ASP A 50 6057 9940 10866 -1207 1273 -1162 C
ATOM 183 C ASP A 50 9.060 0.122 -63.023 1.00 67.05 C
ANISOU 183 C ASP A 50 5621 9434 10421 -1017 1299 -1073 C
ATOM 184 O ASP A 50 9.708 1.111 -62.664 1.00 65.42 O
ANISOU 184 O ASP A 50 5319 9360 10179 -959 1297 -1037 O
ATOM 185 CB ASP A 50 6.795 1.050 -63.436 1.00 76.89 C
ANISOU 185 CB ASP A 50 6698 10933 11585 -1124 1125 -1196 C
ATOM 186 CG ASP A 50 5.772 1.502 -64.457 1.00 86.81 C
ANISOU 186 CG ASP A 50 7893 12300 12791 -1315 1089 -1281 C
ATOM 187 OD1 ASP A 50 6.130 1.623 -65.646 1.00 89.74 O
ANISOU 187 OD1 ASP A 50 8306 12629 13163 -1521 1185 -1316 O
ATOM 188 OD2 ASP A 50 4.611 1.746 -64.066 1.00 92.07 O
ANISOU 188 OD2 ASP A 50 8479 13098 13407 -1256 972 -1310 O
ATOM 189 N ILE A 51 9.273 -1.092 -62.534 1.00 60.60 N
ANISOU 189 N ILE A 51 4934 8447 9646 -923 1323 -1035 N
ATOM 190 CA ILE A 51 10.254 -1.322 -61.466 1.00 51.42 C
ANISOU 190 CA ILE A 51 3809 7256 8473 -745 1338 -956 C
ATOM 191 C ILE A 51 11.655 -1.043 -62.001 1.00 54.37 C
ANISOU 191 C ILE A 51 4199 7609 8852 -798 1459 -899 C
ATOM 192 O ILE A 51 12.038 -1.598 -63.049 1.00 60.59 O
ANISOU 192 O ILE A 51 5075 8268 9678 -924 1573 -891 O
ATOM 193 CB ILE A 51 10.141 -2.754 -60.942 1.00 49.46 C
ANISOU 193 CB ILE A 51 3696 6846 8249 -655 1341 -931 C
ATOM 194 CG1 ILE A 51 8.690 -3.071 -60.582 1.00 59.28 C
ANISOU 194 CG1 ILE A 51 4956 8091 9479 -620 1218 -986 C
ATOM 195 CG2 ILE A 51 11.028 -2.947 -59.724 1.00 42.58 C
ANISOU 195 CG2 ILE A 51 2864 5979 7334 -480 1341 -863 C
ATOM 196 CD1 ILE A 51 8.463 -4.515 -60.202 1.00 62.45 C
ANISOU 196 CD1 ILE A 51 5537 8325 9866 -545 1197 -952 C
ATOM 197 N PRO A 52 12.445 -0.203 -61.337 1.00 50.31 N
ANISOU 197 N PRO A 52 3615 7206 8296 -702 1450 -854 N
ATOM 198 CA PRO A 52 13.774 0.132 -61.860 1.00 42.13 C
ANISOU 198 CA PRO A 52 2587 6160 7262 -752 1560 -801 C
ATOM 199 C PRO A 52 14.715 -1.062 -61.875 1.00 41.73 C
ANISOU 199 C PRO A 52 2680 5949 7226 -706 1657 -729 C
ATOM 200 O PRO A 52 14.641 -1.957 -61.032 1.00 45.93 O
ANISOU 200 O PRO A 52 3287 6424 7741 -583 1622 -701 O
ATOM 201 CB PRO A 52 14.268 1.223 -60.904 1.00 42.38 C
ANISOU 201 CB PRO A 52 2514 6349 7238 -629 1509 -766 C
ATOM 202 CG PRO A 52 13.468 1.039 -59.674 1.00 46.46 C
ANISOU 202 CG PRO A 52 3032 6896 7726 -474 1405 -777 C
ATOM 203 CD PRO A 52 12.125 0.552 -60.118 1.00 48.06 C
ANISOU 203 CD PRO A 52 3241 7060 7958 -546 1350 -848 C
ATOM 204 N SER A 53 15.631 -1.039 -62.847 1.00 47.60 N
ANISOU 204 N SER A 53 3464 6633 7988 -803 1787 -693 N
ATOM 205 CA SER A 53 16.498 -2.172 -63.159 1.00 45.70 C
ANISOU 205 CA SER A 53 3364 6245 7757 -771 1907 -612 C
ATOM 206 C SER A 53 17.545 -2.458 -62.090 1.00 44.17 C
ANISOU 206 C SER A 53 3191 6092 7499 -600 1893 -528 C
ATOM 207 O SER A 53 18.132 -3.546 -62.105 1.00 40.11 O
ANISOU 207 O SER A 53 2785 5490 6964 -537 1963 -454 O
ATOM 208 CB SER A 53 17.191 -1.926 -64.502 1.00 51.19 C
ANISOU 208 CB SER A 53 4102 6869 8480 -916 2064 -593 C
ATOM 209 OG SER A 53 18.227 -2.865 -64.729 1.00 60.31 O
ANISOU 209 OG SER A 53 5383 7909 9623 -848 2191 -489 O
ATOM 210 N SER A 54 17.798 -1.529 -61.173 1.00 46.12 N
ANISOU 210 N SER A 54 3343 6479 7701 -523 1811 -533 N
ATOM 211 CA SER A 54 18.778 -1.748 -60.116 1.00 45.42 C
ANISOU 211 CA SER A 54 3282 6438 7536 -382 1798 -467 C
ATOM 212 C SER A 54 18.166 -2.338 -58.852 1.00 49.03 C
ANISOU 212 C SER A 54 3777 6906 7948 -265 1699 -487 C
ATOM 213 O SER A 54 18.882 -2.508 -57.859 1.00 50.46 O
ANISOU 213 O SER A 54 3985 7137 8051 -162 1684 -449 O
ATOM 214 CB SER A 54 19.493 -0.435 -59.776 1.00 44.09 C
ANISOU 214 CB SER A 54 3013 6403 7337 -363 1786 -457 C
ATOM 215 OG SER A 54 18.593 0.515 -59.230 1.00 40.91 O
ANISOU 215 OG SER A 54 2509 6100 6934 -343 1689 -515 O
ATOM 216 N THR A 55 16.875 -2.667 -58.872 1.00 38.19 N
ANISOU 216 N THR A 55 2409 5486 6614 -287 1638 -549 N
ATOM 217 CA THR A 55 16.192 -3.136 -57.672 1.00 37.07 C
ANISOU 217 CA THR A 55 2304 5348 6432 -182 1548 -578 C
ATOM 218 C THR A 55 16.799 -4.439 -57.170 1.00 36.38 C
ANISOU 218 C THR A 55 2331 5211 6281 -112 1577 -525 C
ATOM 219 O THR A 55 17.074 -5.358 -57.947 1.00 36.00 O
ANISOU 219 O THR A 55 2349 5083 6247 -147 1647 -480 O
ATOM 220 CB THR A 55 14.703 -3.337 -57.957 1.00 43.07 C
ANISOU 220 CB THR A 55 3053 6061 7249 -227 1484 -652 C
ATOM 221 OG1 THR A 55 14.125 -2.098 -58.387 1.00 44.38 O
ANISOU 221 OG1 THR A 55 3096 6318 7448 -292 1448 -701 O
ATOM 222 CG2 THR A 55 13.977 -3.825 -56.713 1.00 39.33 C
ANISOU 222 CG2 THR A 55 2628 5582 6734 -115 1401 -683 C
ATOM 223 N LYS A 56 16.998 -4.513 -55.853 1.00 35.43 N
ANISOU 223 N LYS A 56 2236 5146 6078 -14 1532 -528 N
ATOM 224 CA LYS A 56 17.548 -5.693 -55.207 1.00 36.30 C
ANISOU 224 CA LYS A 56 2440 5254 6100 43 1547 -490 C
ATOM 225 C LYS A 56 16.505 -6.534 -54.484 1.00 34.22 C
ANISOU 225 C LYS A 56 2241 4942 5818 79 1485 -544 C
ATOM 226 O LYS A 56 16.723 -7.736 -54.303 1.00 32.98 O
ANISOU 226 O LYS A 56 2159 4772 5599 100 1500 -516 O
ATOM 227 CB LYS A 56 18.640 -5.282 -54.207 1.00 37.12 C
ANISOU 227 CB LYS A 56 2537 5462 6106 103 1560 -464 C
ATOM 228 CG LYS A 56 19.663 -4.307 -54.779 1.00 43.35 C
ANISOU 228 CG LYS A 56 3254 6308 6907 77 1613 -417 C
ATOM 229 CD LYS A 56 21.077 -4.845 -54.647 1.00 52.52 C
ANISOU 229 CD LYS A 56 4447 7537 7970 105 1669 -343 C
ATOM 230 CE LYS A 56 21.606 -4.697 -53.229 1.00 58.90 C
ANISOU 230 CE LYS A 56 5269 8436 8676 167 1651 -355 C
ATOM 231 NZ LYS A 56 22.116 -3.326 -52.960 1.00 60.65 N
ANISOU 231 NZ LYS A 56 5418 8717 8908 178 1661 -356 N
ATOM 232 N ASN A 57 15.382 -5.942 -54.077 1.00 33.54 N
ANISOU 232 N ASN A 57 2126 4842 5777 93 1418 -617 N
ATOM 233 CA ASN A 57 14.360 -6.642 -53.307 1.00 36.02 C
ANISOU 233 CA ASN A 57 2506 5107 6073 134 1362 -676 C
ATOM 234 C ASN A 57 12.992 -6.266 -53.851 1.00 35.93 C
ANISOU 234 C ASN A 57 2447 5047 6156 105 1302 -733 C
ATOM 235 O ASN A 57 12.642 -5.083 -53.882 1.00 37.40 O
ANISOU 235 O ASN A 57 2546 5290 6375 112 1276 -757 O
ATOM 236 CB ASN A 57 14.458 -6.292 -51.819 1.00 34.27 C
ANISOU 236 CB ASN A 57 2315 4933 5773 213 1353 -709 C
ATOM 237 CG ASN A 57 15.879 -6.339 -51.298 1.00 36.82 C
ANISOU 237 CG ASN A 57 2656 5333 6003 225 1413 -660 C
ATOM 238 OD1 ASN A 57 16.439 -7.413 -51.085 1.00 32.19 O
ANISOU 238 OD1 ASN A 57 2131 4763 5338 218 1437 -634 O
ATOM 239 ND2 ASN A 57 16.467 -5.168 -51.078 1.00 42.52 N
ANISOU 239 ND2 ASN A 57 3316 6118 6723 248 1438 -645 N
ATOM 240 N ILE A 58 12.223 -7.270 -54.270 1.00 32.20 N
ANISOU 240 N ILE A 58 2027 4489 5717 76 1280 -754 N
ATOM 241 CA ILE A 58 10.867 -7.083 -54.775 1.00 35.57 C
ANISOU 241 CA ILE A 58 2424 4872 6217 42 1213 -811 C
ATOM 242 C ILE A 58 9.938 -8.002 -53.993 1.00 33.84 C
ANISOU 242 C ILE A 58 2319 4588 5951 98 1142 -846 C
ATOM 243 O ILE A 58 10.179 -9.213 -53.917 1.00 31.38 O
ANISOU 243 O ILE A 58 2105 4225 5592 98 1157 -819 O
ATOM 244 CB ILE A 58 10.764 -7.378 -56.280 1.00 38.53 C
ANISOU 244 CB ILE A 58 2811 5179 6649 -75 1238 -784 C
ATOM 245 CG1 ILE A 58 11.549 -6.350 -57.094 1.00 41.95 C
ANISOU 245 CG1 ILE A 58 3133 5674 7132 -149 1313 -764 C
ATOM 246 CG2 ILE A 58 9.317 -7.382 -56.724 1.00 39.85 C
ANISOU 246 CG2 ILE A 58 2993 5300 6850 -121 1147 -839 C
ATOM 247 CD1 ILE A 58 11.519 -6.604 -58.588 1.00 39.85 C
ANISOU 247 CD1 ILE A 58 2899 5326 6916 -281 1371 -745 C
ATOM 248 N ASP A 59 8.879 -7.436 -53.421 1.00 32.50 N
ANISOU 248 N ASP A 59 2132 4431 5785 151 1069 -902 N
ATOM 249 CA ASP A 59 7.831 -8.209 -52.763 1.00 31.57 C
ANISOU 249 CA ASP A 59 2123 4242 5631 199 1001 -941 C
ATOM 250 C ASP A 59 6.588 -8.127 -53.640 1.00 35.67 C
ANISOU 250 C ASP A 59 2625 4724 6202 148 918 -966 C
ATOM 251 O ASP A 59 5.943 -7.075 -53.719 1.00 37.99 O
ANISOU 251 O ASP A 59 2822 5090 6521 166 878 -994 O
ATOM 252 CB ASP A 59 7.566 -7.687 -51.352 1.00 30.46 C
ANISOU 252 CB ASP A 59 2000 4133 5441 314 1003 -981 C
ATOM 253 CG ASP A 59 6.662 -8.603 -50.541 1.00 32.14 C
ANISOU 253 CG ASP A 59 2349 4261 5602 360 958 -1023 C
ATOM 254 OD1 ASP A 59 6.015 -9.498 -51.126 1.00 31.35 O
ANISOU 254 OD1 ASP A 59 2309 4090 5515 311 900 -1025 O
ATOM 255 OD2 ASP A 59 6.605 -8.427 -49.307 1.00 39.12 O
ANISOU 255 OD2 ASP A 59 3291 5144 6430 443 992 -1057 O
ATOM 256 N LEU A 60 6.269 -9.230 -54.320 1.00 20.69 N
ANISOU 256 N LEU A 60 1816 2957 3086 26 1058 -502 N
ATOM 257 CA LEU A 60 5.109 -9.311 -55.198 1.00 20.60 C
ANISOU 257 CA LEU A 60 1831 2865 3133 -12 1019 -516 C
ATOM 258 C LEU A 60 3.993 -10.161 -54.603 1.00 18.41 C
ANISOU 258 C LEU A 60 1661 2501 2833 32 959 -540 C
ATOM 259 O LEU A 60 3.084 -10.578 -55.327 1.00 27.28 O
ANISOU 259 O LEU A 60 2844 3543 3976 2 922 -535 O
ATOM 260 CB LEU A 60 5.510 -9.870 -56.564 1.00 30.70 C
ANISOU 260 CB LEU A 60 3131 4102 4432 -93 1059 -446 C
ATOM 261 CG LEU A 60 6.284 -8.986 -57.541 1.00 36.22 C
ANISOU 261 CG LEU A 60 3736 4856 5170 -167 1108 -416 C
ATOM 262 CD1 LEU A 60 6.726 -9.794 -58.749 1.00 35.41 C
ANISOU 262 CD1 LEU A 60 3687 4692 5076 -238 1145 -338 C
ATOM 263 CD2 LEU A 60 5.441 -7.799 -57.975 1.00 37.86 C
ANISOU 263 CD2 LEU A 60 3867 5071 5447 -190 1054 -469 C
ATOM 264 N SER A 61 4.037 -10.413 -53.299 1.00 24.16 N
ANISOU 264 N SER A 61 2419 3245 3516 97 951 -568 N
ATOM 265 CA SER A 61 3.136 -11.381 -52.699 1.00 22.71 C
ANISOU 265 CA SER A 61 2344 2982 3302 127 913 -579 C
ATOM 266 C SER A 61 1.693 -10.877 -52.703 1.00 23.88 C
ANISOU 266 C SER A 61 2527 3073 3473 140 829 -626 C
ATOM 267 O SER A 61 1.418 -9.677 -52.781 1.00 31.34 O
ANISOU 267 O SER A 61 3403 4050 4453 152 787 -664 O
ATOM 268 CB SER A 61 3.580 -11.712 -51.273 1.00 27.72 C
ANISOU 268 CB SER A 61 2999 3646 3886 185 924 -598 C
ATOM 269 OG SER A 61 3.662 -10.549 -50.469 1.00 29.94 O
ANISOU 269 OG SER A 61 3222 3984 4169 235 890 -646 O
ATOM 270 N PHE A 62 0.767 -11.836 -52.633 1.00 23.19 N
ANISOU 270 N PHE A 62 2547 2901 3361 139 804 -622 N
ATOM 271 CA PHE A 62 -0.669 -11.571 -52.540 1.00 23.94 C
ANISOU 271 CA PHE A 62 2708 2932 3457 154 723 -661 C
ATOM 272 C PHE A 62 -1.199 -10.818 -53.759 1.00 26.22 C
ANISOU 272 C PHE A 62 2960 3207 3797 113 681 -670 C
ATOM 273 O PHE A 62 -2.123 -10.008 -53.653 1.00 37.69 O
ANISOU 273 O PHE A 62 4416 4642 5263 136 601 -713 O
ATOM 274 CB PHE A 62 -1.005 -10.841 -51.234 1.00 19.35 C
ANISOU 274 CB PHE A 62 2126 2368 2859 223 669 -710 C
ATOM 275 CG PHE A 62 -0.737 -11.668 -50.006 1.00 20.73 C
ANISOU 275 CG PHE A 62 2360 2533 2982 256 697 -707 C
ATOM 276 CD1 PHE A 62 -1.708 -12.510 -49.499 1.00 20.28 C
ANISOU 276 CD1 PHE A 62 2422 2398 2885 259 674 -709 C
ATOM 277 CD2 PHE A 62 0.502 -11.625 -49.382 1.00 16.02 C
ANISOU 277 CD2 PHE A 62 1701 2008 2375 278 749 -703 C
ATOM 278 CE1 PHE A 62 -1.456 -13.286 -48.383 1.00 22.48 C
ANISOU 278 CE1 PHE A 62 2749 2667 3123 278 701 -707 C
ATOM 279 CE2 PHE A 62 0.756 -12.394 -48.264 1.00 20.99 C
ANISOU 279 CE2 PHE A 62 2384 2628 2962 303 768 -705 C
ATOM 280 CZ PHE A 62 -0.221 -13.229 -47.768 1.00 19.03 C
ANISOU 280 CZ PHE A 62 2247 2300 2683 301 744 -707 C
ATOM 281 N ASN A 63 -0.627 -11.101 -54.929 1.00 23.79 N
ANISOU 281 N ASN A 63 2621 2900 3518 53 730 -629 N
ATOM 282 CA ASN A 63 -1.111 -10.641 -56.220 1.00 19.64 C
ANISOU 282 CA ASN A 63 2077 2345 3042 -2 696 -631 C
ATOM 283 C ASN A 63 -1.525 -11.837 -57.073 1.00 19.97 C
ANISOU 283 C ASN A 63 2214 2301 3071 -42 714 -601 C
ATOM 284 O ASN A 63 -0.857 -12.875 -57.042 1.00 21.03 O
ANISOU 284 O ASN A 63 2379 2429 3183 -46 780 -560 O
ATOM 285 CB ASN A 63 -0.038 -9.828 -56.964 1.00 23.78 C
ANISOU 285 CB ASN A 63 2477 2940 3619 -49 740 -610 C
ATOM 286 CG ASN A 63 0.263 -8.497 -56.293 1.00 26.46 C
ANISOU 286 CG ASN A 63 2706 3368 3980 -11 720 -653 C
ATOM 287 OD1 ASN A 63 -0.574 -7.594 -56.285 1.00 26.28 O
ANISOU 287 OD1 ASN A 63 2654 3343 3988 6 641 -705 O
ATOM 288 ND2 ASN A 63 1.463 -8.366 -55.738 1.00 23.19 N
ANISOU 288 ND2 ASN A 63 2229 3033 3549 5 789 -635 N
ATOM 289 N PRO A 64 -2.616 -11.731 -57.832 1.00 24.16 N
ANISOU 289 N PRO A 64 2795 2768 3617 -66 654 -626 N
ATOM 290 CA PRO A 64 -3.085 -12.869 -58.658 1.00 26.06 C
ANISOU 290 CA PRO A 64 3132 2925 3845 -98 670 -608 C
ATOM 291 C PRO A 64 -2.268 -13.036 -59.934 1.00 29.20 C
ANISOU 291 C PRO A 64 3490 3313 4291 -161 716 -565 C
ATOM 292 O PRO A 64 -2.722 -12.793 -61.059 1.00 30.20 O
ANISOU 292 O PRO A 64 3626 3392 4456 -210 682 -575 O
ATOM 293 CB PRO A 64 -4.545 -12.492 -58.932 1.00 24.79 C
ANISOU 293 CB PRO A 64 3036 2707 3676 -98 580 -657 C
ATOM 294 CG PRO A 64 -4.546 -11.001 -58.918 1.00 28.32 C
ANISOU 294 CG PRO A 64 3382 3208 4170 -96 519 -689 C
ATOM 295 CD PRO A 64 -3.538 -10.583 -57.892 1.00 25.20 C
ANISOU 295 CD PRO A 64 2902 2899 3774 -57 560 -678 C
ATOM 296 N LEU A 65 -1.021 -13.483 -59.768 1.00 25.18 N
ANISOU 296 N LEU A 65 2944 2844 3778 -162 791 -516 N
ATOM 297 CA LEU A 65 -0.120 -13.610 -60.911 1.00 25.52 C
ANISOU 297 CA LEU A 65 2955 2878 3862 -220 836 -466 C
ATOM 298 C LEU A 65 -0.510 -14.789 -61.798 1.00 26.23 C
ANISOU 298 C LEU A 65 3142 2872 3953 -238 845 -452 C
ATOM 299 O LEU A 65 -0.512 -14.674 -63.031 1.00 24.06 O
ANISOU 299 O LEU A 65 2870 2547 3723 -295 836 -439 O
ATOM 300 CB LEU A 65 1.325 -13.743 -60.425 1.00 23.69 C
ANISOU 300 CB LEU A 65 2667 2718 3615 -209 909 -417 C
ATOM 301 CG LEU A 65 1.913 -12.532 -59.695 1.00 24.77 C
ANISOU 301 CG LEU A 65 2698 2958 3756 -196 914 -430 C
ATOM 302 CD1 LEU A 65 3.383 -12.760 -59.365 1.00 21.39 C
ANISOU 302 CD1 LEU A 65 2229 2596 3302 -192 990 -378 C
ATOM 303 CD2 LEU A 65 1.727 -11.270 -60.530 1.00 23.78 C
ANISOU 303 CD2 LEU A 65 2493 2850 3693 -253 883 -448 C
ATOM 304 N LYS A 66 -0.818 -15.936 -61.185 1.00 21.31 N
ANISOU 304 N LYS A 66 2594 2222 3281 -191 864 -457 N
ATOM 305 CA LYS A 66 -1.348 -17.129 -61.850 1.00 20.51 C
ANISOU 305 CA LYS A 66 2585 2034 3173 -192 873 -459 C
ATOM 306 C LYS A 66 -0.317 -17.854 -62.708 1.00 25.18 C
ANISOU 306 C LYS A 66 3176 2598 3792 -212 923 -403 C
ATOM 307 O LYS A 66 -0.322 -19.087 -62.779 1.00 26.72 O
ANISOU 307 O LYS A 66 3430 2752 3972 -184 953 -397 O
ATOM 308 CB LYS A 66 -2.576 -16.782 -62.704 1.00 21.36 C
ANISOU 308 CB LYS A 66 2745 2072 3297 -223 811 -504 C
ATOM 309 CG LYS A 66 -3.735 -16.185 -61.920 1.00 22.33 C
ANISOU 309 CG LYS A 66 2893 2207 3384 -196 749 -559 C
ATOM 310 CD LYS A 66 -5.035 -16.314 -62.703 1.00 35.36 C
ANISOU 310 CD LYS A 66 4632 3777 5028 -214 695 -604 C
ATOM 311 CE LYS A 66 -6.083 -15.313 -62.239 1.00 48.12 C
ANISOU 311 CE LYS A 66 6256 5404 6623 -203 610 -653 C
ATOM 312 NZ LYS A 66 -6.486 -15.513 -60.822 1.00 55.57 N
ANISOU 312 NZ LYS A 66 7236 6377 7502 -147 611 -665 N
ATOM 313 N ILE A 67 0.565 -17.113 -63.369 1.00 21.93 N
ANISOU 313 N ILE A 67 2701 2208 3423 -261 933 -363 N
ATOM 314 CA ILE A 67 1.578 -17.726 -64.221 1.00 19.37 C
ANISOU 314 CA ILE A 67 2386 1850 3123 -284 975 -302 C
ATOM 315 C ILE A 67 2.793 -16.811 -64.281 1.00 18.53 C
ANISOU 315 C ILE A 67 2193 1815 3034 -324 1005 -250 C
ATOM 316 O ILE A 67 2.668 -15.594 -64.444 1.00 32.09 O
ANISOU 316 O ILE A 67 3845 3568 4779 -368 984 -265 O
ATOM 317 CB ILE A 67 1.028 -18.033 -65.633 1.00 19.66 C
ANISOU 317 CB ILE A 67 2487 1779 3205 -326 949 -309 C
ATOM 318 CG1 ILE A 67 2.104 -18.706 -66.489 1.00 24.04 C
ANISOU 318 CG1 ILE A 67 3063 2287 3784 -343 986 -241 C
ATOM 319 CG2 ILE A 67 0.493 -16.771 -66.307 1.00 22.26 C
ANISOU 319 CG2 ILE A 67 2780 2099 3578 -392 899 -335 C
ATOM 320 CD1 ILE A 67 1.627 -19.132 -67.863 1.00 19.76 C
ANISOU 320 CD1 ILE A 67 2595 1627 3288 -376 961 -249 C
ATOM 321 N LEU A 68 3.972 -17.409 -64.140 1.00 22.13 N
ANISOU 321 N LEU A 68 2645 2293 3469 -307 1054 -191 N
ATOM 322 CA LEU A 68 5.232 -16.688 -64.279 1.00 18.96 C
ANISOU 322 CA LEU A 68 2178 1956 3072 -348 1094 -132 C
ATOM 323 C LEU A 68 5.685 -16.799 -65.731 1.00 23.06 C
ANISOU 323 C LEU A 68 2729 2396 3637 -416 1103 -77 C
ATOM 324 O LEU A 68 6.195 -17.841 -66.157 1.00 22.57 O
ANISOU 324 O LEU A 68 2729 2276 3569 -397 1117 -33 O
ATOM 325 CB LEU A 68 6.281 -17.239 -63.319 1.00 18.55 C
ANISOU 325 CB LEU A 68 2114 1972 2963 -294 1137 -98 C
ATOM 326 CG LEU A 68 6.062 -16.875 -61.848 1.00 26.40 C
ANISOU 326 CG LEU A 68 3063 3053 3914 -241 1133 -147 C
ATOM 327 CD1 LEU A 68 7.191 -17.398 -60.973 1.00 24.91 C
ANISOU 327 CD1 LEU A 68 2864 2931 3670 -194 1172 -114 C
ATOM 328 CD2 LEU A 68 5.912 -15.372 -61.691 1.00 19.46 C
ANISOU 328 CD2 LEU A 68 2100 2240 3053 -275 1124 -175 C
ATOM 329 N LYS A 69 5.498 -15.723 -66.489 1.00 32.38 N
ANISOU 329 N LYS A 69 3866 3571 4867 -494 1089 -80 N
ATOM 330 CA LYS A 69 5.809 -15.721 -67.910 1.00 31.95 C
ANISOU 330 CA LYS A 69 3846 3430 4864 -572 1091 -33 C
ATOM 331 C LYS A 69 7.309 -15.577 -68.143 1.00 24.78 C
ANISOU 331 C LYS A 69 2916 2559 3941 -612 1152 58 C
ATOM 332 O LYS A 69 8.027 -14.953 -67.355 1.00 24.89 O
ANISOU 332 O LYS A 69 2857 2683 3918 -607 1193 74 O
ATOM 333 CB LYS A 69 5.063 -14.591 -68.616 1.00 27.49 C
ANISOU 333 CB LYS A 69 3235 2849 4361 -651 1052 -73 C
ATOM 334 CG LYS A 69 3.560 -14.663 -68.450 1.00 29.11 C
ANISOU 334 CG LYS A 69 3471 3016 4573 -616 984 -161 C
ATOM 335 CD LYS A 69 2.967 -15.775 -69.289 1.00 21.71 C
ANISOU 335 CD LYS A 69 2648 1950 3650 -604 956 -171 C
ATOM 336 CE LYS A 69 3.337 -15.600 -70.746 1.00 22.78 C
ANISOU 336 CE LYS A 69 2809 1999 3850 -695 954 -129 C
ATOM 337 NZ LYS A 69 2.716 -16.625 -71.625 1.00 22.95 N
ANISOU 337 NZ LYS A 69 2943 1888 3890 -679 921 -149 N
ATOM 338 N SER A 70 7.775 -16.174 -69.238 1.00 22.66 N
ANISOU 338 N SER A 70 2721 2192 3698 -648 1157 119 N
ATOM 339 CA SER A 70 9.186 -16.105 -69.595 1.00 23.39 C
ANISOU 339 CA SER A 70 2816 2301 3771 -692 1211 216 C
ATOM 340 C SER A 70 9.652 -14.659 -69.703 1.00 24.72 C
ANISOU 340 C SER A 70 2885 2554 3954 -785 1251 234 C
ATOM 341 O SER A 70 8.917 -13.786 -70.167 1.00 24.56 O
ANISOU 341 O SER A 70 2814 2525 3993 -849 1226 189 O
ATOM 342 CB SER A 70 9.431 -16.827 -70.921 1.00 24.17 C
ANISOU 342 CB SER A 70 3016 2258 3909 -728 1197 273 C
ATOM 343 OG SER A 70 9.053 -18.187 -70.834 1.00 28.28 O
ANISOU 343 OG SER A 70 3619 2706 4418 -635 1164 252 O
ATOM 344 N TYR A 71 10.886 -14.417 -69.259 1.00 25.48 N
ANISOU 344 N TYR A 71 2950 2737 3995 -791 1314 297 N
ATOM 345 CA TYR A 71 11.593 -13.141 -69.369 1.00 27.56 C
ANISOU 345 CA TYR A 71 3121 3091 4261 -881 1374 328 C
ATOM 346 C TYR A 71 10.968 -12.020 -68.549 1.00 29.05 C
ANISOU 346 C TYR A 71 3186 3391 4462 -873 1370 241 C
ATOM 347 O TYR A 71 11.332 -10.854 -68.743 1.00 26.17 O
ANISOU 347 O TYR A 71 2726 3100 4118 -952 1414 247 O
ATOM 348 CB TYR A 71 11.712 -12.682 -70.828 1.00 26.64 C
ANISOU 348 CB TYR A 71 3020 2889 4213 -1009 1382 377 C
ATOM 349 CG TYR A 71 12.181 -13.765 -71.770 1.00 27.27 C
ANISOU 349 CG TYR A 71 3234 2833 4295 -1018 1371 456 C
ATOM 350 CD1 TYR A 71 13.454 -14.310 -71.655 1.00 28.83 C
ANISOU 350 CD1 TYR A 71 3488 3043 4423 -1000 1415 549 C
ATOM 351 CD2 TYR A 71 11.356 -14.237 -72.781 1.00 28.61 C
ANISOU 351 CD2 TYR A 71 3476 2860 4534 -1039 1310 436 C
ATOM 352 CE1 TYR A 71 13.890 -15.302 -72.521 1.00 30.53 C
ANISOU 352 CE1 TYR A 71 3829 3128 4642 -999 1395 622 C
ATOM 353 CE2 TYR A 71 11.781 -15.227 -73.650 1.00 34.16 C
ANISOU 353 CE2 TYR A 71 4303 3432 5243 -1039 1295 503 C
ATOM 354 CZ TYR A 71 13.047 -15.754 -73.515 1.00 38.52 C
ANISOU 354 CZ TYR A 71 4910 3997 5731 -1016 1336 598 C
ATOM 355 OH TYR A 71 13.472 -16.738 -74.382 1.00 44.66 O
ANISOU 355 OH TYR A 71 5813 4638 6517 -1007 1312 665 O
ATOM 356 N SER A 72 10.056 -12.333 -67.625 1.00 28.11 N
ANISOU 356 N SER A 72 3064 3288 4329 -778 1320 161 N
ATOM 357 CA SER A 72 9.379 -11.281 -66.871 1.00 29.27 C
ANISOU 357 CA SER A 72 3104 3525 4491 -761 1302 78 C
ATOM 358 C SER A 72 10.333 -10.523 -65.957 1.00 32.37 C
ANISOU 358 C SER A 72 3406 4061 4832 -749 1368 85 C
ATOM 359 O SER A 72 10.113 -9.336 -65.684 1.00 29.88 O
ANISOU 359 O SER A 72 2979 3829 4544 -771 1374 34 O
ATOM 360 CB SER A 72 8.235 -11.875 -66.056 1.00 35.67 C
ANISOU 360 CB SER A 72 3954 4311 5289 -663 1235 1 C
ATOM 361 OG SER A 72 7.083 -12.038 -66.864 1.00 49.64 O
ANISOU 361 OG SER A 72 5768 5977 7117 -688 1170 -38 O
ATOM 362 N PHE A 73 11.391 -11.179 -65.478 1.00 32.60 N
ANISOU 362 N PHE A 73 3479 4121 4785 -709 1415 143 N
ATOM 363 CA PHE A 73 12.340 -10.579 -64.547 1.00 33.86 C
ANISOU 363 CA PHE A 73 3574 4417 4873 -679 1461 146 C
ATOM 364 C PHE A 73 13.713 -10.342 -65.167 1.00 32.17 C
ANISOU 364 C PHE A 73 3373 4239 4610 -745 1511 241 C
ATOM 365 O PHE A 73 14.674 -10.090 -64.433 1.00 36.75 O
ANISOU 365 O PHE A 73 3933 4926 5105 -708 1533 257 O
ATOM 366 CB PHE A 73 12.488 -11.460 -63.302 1.00 30.46 C
ANISOU 366 CB PHE A 73 3190 4014 4370 -565 1445 126 C
ATOM 367 CG PHE A 73 11.202 -11.692 -62.556 1.00 28.46 C
ANISOU 367 CG PHE A 73 2934 3734 4145 -495 1391 37 C
ATOM 368 CD1 PHE A 73 10.626 -10.674 -61.807 1.00 32.59 C
ANISOU 368 CD1 PHE A 73 3369 4331 4682 -468 1368 -43 C
ATOM 369 CD2 PHE A 73 10.574 -12.926 -62.592 1.00 21.02 C
ANISOU 369 CD2 PHE A 73 2088 2694 3204 -447 1340 33 C
ATOM 370 CE1 PHE A 73 9.443 -10.884 -61.116 1.00 31.93 C
ANISOU 370 CE1 PHE A 73 3301 4218 4613 -402 1304 -118 C
ATOM 371 CE2 PHE A 73 9.388 -13.141 -61.906 1.00 26.68 C
ANISOU 371 CE2 PHE A 73 2817 3389 3932 -386 1281 -45 C
ATOM 372 CZ PHE A 73 8.824 -12.120 -61.165 1.00 33.40 C
ANISOU 372 CZ PHE A 73 3589 4307 4793 -365 1261 -116 C
ATOM 373 N SER A 74 13.830 -10.407 -66.497 1.00 29.62 N
ANISOU 373 N SER A 74 3088 3828 4337 -842 1526 303 N
ATOM 374 CA SER A 74 15.133 -10.376 -67.156 1.00 36.38 C
ANISOU 374 CA SER A 74 3984 4696 5143 -907 1572 406 C
ATOM 375 C SER A 74 15.824 -9.020 -67.077 1.00 36.81 C
ANISOU 375 C SER A 74 3935 4885 5164 -959 1607 411 C
ATOM 376 O SER A 74 17.032 -8.948 -67.335 1.00 42.32 O
ANISOU 376 O SER A 74 4661 5625 5795 -998 1652 492 O
ATOM 377 CB SER A 74 14.981 -10.795 -68.621 1.00 34.19 C
ANISOU 377 CB SER A 74 3783 4273 4933 -999 1567 468 C
ATOM 378 OG SER A 74 13.908 -10.111 -69.243 1.00 44.03 O
ANISOU 378 OG SER A 74 4972 5478 6280 -1061 1535 410 O
ATOM 379 N ASN A 75 15.104 -7.953 -66.735 1.00 34.05 N
ANISOU 379 N ASN A 75 3471 4605 4862 -957 1589 328 N
ATOM 380 CA ASN A 75 15.727 -6.647 -66.560 1.00 38.92 C
ANISOU 380 CA ASN A 75 3979 5356 5452 -989 1625 326 C
ATOM 381 C ASN A 75 16.329 -6.459 -65.174 1.00 40.86 C
ANISOU 381 C ASN A 75 4192 5728 5604 -886 1637 298 C
ATOM 382 O ASN A 75 17.160 -5.561 -64.998 1.00 45.86 O
ANISOU 382 O ASN A 75 4758 6474 6194 -903 1681 319 O
ATOM 383 CB ASN A 75 14.708 -5.534 -66.831 1.00 39.84 C
ANISOU 383 CB ASN A 75 3979 5490 5667 -1028 1596 249 C
ATOM 384 CG ASN A 75 14.448 -5.330 -68.312 1.00 41.08 C
ANISOU 384 CG ASN A 75 4143 5557 5910 -1157 1595 288 C
ATOM 385 OD1 ASN A 75 15.341 -5.517 -69.138 1.00 40.53 O
ANISOU 385 OD1 ASN A 75 4129 5457 5814 -1235 1634 384 O
ATOM 386 ND2 ASN A 75 13.223 -4.947 -68.656 1.00 42.95 N
ANISOU 386 ND2 ASN A 75 4328 5745 6247 -1181 1544 213 N
ATOM 387 N PHE A 76 15.946 -7.286 -64.198 1.00 40.59 N
ANISOU 387 N PHE A 76 4207 5676 5541 -782 1599 253 N
ATOM 388 CA PHE A 76 16.399 -7.127 -62.815 1.00 38.18 C
ANISOU 388 CA PHE A 76 3875 5479 5153 -680 1595 215 C
ATOM 389 C PHE A 76 17.675 -7.942 -62.599 1.00 42.26 C
ANISOU 389 C PHE A 76 4477 6017 5565 -663 1629 290 C
ATOM 390 O PHE A 76 17.693 -8.999 -61.965 1.00 45.35 O
ANISOU 390 O PHE A 76 4941 6374 5915 -592 1602 282 O
ATOM 391 CB PHE A 76 15.293 -7.532 -61.848 1.00 32.04 C
ANISOU 391 CB PHE A 76 3104 4670 4399 -582 1531 125 C
ATOM 392 CG PHE A 76 13.980 -6.860 -62.128 1.00 34.03 C
ANISOU 392 CG PHE A 76 3288 4888 4755 -602 1494 52 C
ATOM 393 CD1 PHE A 76 13.881 -5.479 -62.110 1.00 37.99 C
ANISOU 393 CD1 PHE A 76 3672 5472 5290 -622 1501 13 C
ATOM 394 CD2 PHE A 76 12.849 -7.605 -62.414 1.00 36.79 C
ANISOU 394 CD2 PHE A 76 3688 5122 5169 -598 1454 21 C
ATOM 395 CE1 PHE A 76 12.677 -4.852 -62.372 1.00 35.59 C
ANISOU 395 CE1 PHE A 76 3300 5140 5083 -640 1460 -60 C
ATOM 396 CE2 PHE A 76 11.641 -6.983 -62.677 1.00 39.31 C
ANISOU 396 CE2 PHE A 76 3943 5411 5580 -619 1418 -50 C
ATOM 397 CZ PHE A 76 11.557 -5.604 -62.657 1.00 38.06 C
ANISOU 397 CZ PHE A 76 3666 5340 5456 -641 1417 -92 C
ATOM 398 N SER A 77 18.770 -7.409 -63.147 1.00 41.12 N
ANISOU 398 N SER A 77 4317 5930 5375 -733 1689 363 N
ATOM 399 CA SER A 77 20.054 -8.094 -63.083 1.00 41.45 C
ANISOU 399 CA SER A 77 4442 5993 5313 -733 1725 442 C
ATOM 400 C SER A 77 20.673 -8.057 -61.692 1.00 33.73 C
ANISOU 400 C SER A 77 3448 5129 4240 -633 1724 405 C
ATOM 401 O SER A 77 21.525 -8.898 -61.388 1.00 40.35 O
ANISOU 401 O SER A 77 4367 5972 4992 -608 1733 444 O
ATOM 402 CB SER A 77 21.023 -7.485 -64.098 1.00 48.68 C
ANISOU 402 CB SER A 77 5351 6938 6207 -843 1792 537 C
ATOM 403 OG SER A 77 21.048 -6.072 -63.998 1.00 58.90 O
ANISOU 403 OG SER A 77 6520 8335 7525 -861 1824 509 O
ATOM 404 N GLU A 78 20.273 -7.111 -60.846 1.00 32.56 N
ANISOU 404 N GLU A 78 3202 5061 4107 -571 1711 330 N
ATOM 405 CA GLU A 78 20.823 -7.008 -59.503 1.00 40.35 C
ANISOU 405 CA GLU A 78 4176 6140 5014 -466 1709 295 C
ATOM 406 C GLU A 78 19.874 -7.547 -58.440 1.00 40.76 C
ANISOU 406 C GLU A 78 4243 6157 5086 -367 1632 207 C
ATOM 407 O GLU A 78 20.131 -7.369 -57.246 1.00 47.60 O
ANISOU 407 O GLU A 78 5097 7081 5906 -272 1621 168 O
ATOM 408 CB GLU A 78 21.191 -5.559 -59.191 1.00 50.55 C
ANISOU 408 CB GLU A 78 5367 7525 6313 -448 1762 283 C
ATOM 409 CG GLU A 78 22.578 -5.417 -58.596 1.00 62.67 C
ANISOU 409 CG GLU A 78 6924 9139 7748 -404 1826 327 C
ATOM 410 CD GLU A 78 22.843 -4.030 -58.066 1.00 65.36 C
ANISOU 410 CD GLU A 78 7181 9538 8115 -364 1888 288 C
ATOM 411 OE1 GLU A 78 21.867 -3.292 -57.813 1.00 65.90 O
ANISOU 411 OE1 GLU A 78 7172 9601 8265 -342 1853 209 O
ATOM 412 OE2 GLU A 78 24.027 -3.676 -57.897 1.00 64.12 O
ANISOU 412 OE2 GLU A 78 7045 9423 7896 -360 1964 322 O
ATOM 413 N LEU A 79 18.795 -8.213 -58.848 1.00 33.39 N
ANISOU 413 N LEU A 79 3345 5115 4225 -382 1584 182 N
ATOM 414 CA LEU A 79 17.792 -8.699 -57.908 1.00 27.01 C
ANISOU 414 CA LEU A 79 2554 4265 3443 -296 1514 103 C
ATOM 415 C LEU A 79 18.347 -9.846 -57.067 1.00 26.09 C
ANISOU 415 C LEU A 79 2514 4150 3247 -232 1492 105 C
ATOM 416 O LEU A 79 18.889 -10.819 -57.601 1.00 33.71 O
ANISOU 416 O LEU A 79 3555 5068 4186 -265 1510 162 O
ATOM 417 CB LEU A 79 16.545 -9.155 -58.669 1.00 26.19 C
ANISOU 417 CB LEU A 79 2475 4041 3437 -333 1482 86 C
ATOM 418 CG LEU A 79 15.264 -9.399 -57.861 1.00 24.71 C
ANISOU 418 CG LEU A 79 2291 3806 3293 -260 1414 2 C
ATOM 419 CD1 LEU A 79 14.757 -8.092 -57.282 1.00 23.01 C
ANISOU 419 CD1 LEU A 79 1983 3653 3108 -228 1397 -64 C
ATOM 420 CD2 LEU A 79 14.171 -10.084 -58.685 1.00 22.14 C
ANISOU 420 CD2 LEU A 79 2008 3353 3050 -296 1395 -2 C
ATOM 421 N GLN A 80 18.193 -9.733 -55.747 1.00 24.99 N
ANISOU 421 N GLN A 80 2361 4056 3079 -138 1452 44 N
ATOM 422 CA GLN A 80 18.690 -10.725 -54.799 1.00 26.17 C
ANISOU 422 CA GLN A 80 2570 4217 3155 -76 1423 31 C
ATOM 423 C GLN A 80 17.593 -11.447 -54.032 1.00 23.54 C
ANISOU 423 C GLN A 80 2271 3813 2862 -15 1350 -31 C
ATOM 424 O GLN A 80 17.785 -12.600 -53.643 1.00 29.52 O
ANISOU 424 O GLN A 80 3088 4539 3589 9 1326 -34 O
ATOM 425 CB GLN A 80 19.632 -10.064 -53.785 1.00 30.15 C
ANISOU 425 CB GLN A 80 3052 4816 3588 -9 1441 26 C
ATOM 426 CG GLN A 80 20.879 -9.430 -54.388 1.00 35.62 C
ANISOU 426 CG GLN A 80 3729 5575 4230 -59 1516 92 C
ATOM 427 CD GLN A 80 21.576 -8.488 -53.424 1.00 46.67 C
ANISOU 427 CD GLN A 80 5127 6982 5623 20 1570 82 C
ATOM 428 OE1 GLN A 80 21.177 -8.356 -52.269 1.00 45.05 O
ANISOU 428 OE1 GLN A 80 4938 6734 5447 93 1547 11 O
ATOM 429 NE2 GLN A 80 22.622 -7.823 -53.897 1.00 61.76 N
ANISOU 429 NE2 GLN A 80 7031 8930 7505 -20 1658 132 N
ATOM 430 N TRP A 81 16.457 -10.795 -53.802 1.00 21.35 N
ANISOU 430 N TRP A 81 1956 3504 2651 8 1318 -81 N
ATOM 431 CA TRP A 81 15.405 -11.326 -52.944 1.00 20.13 C
ANISOU 431 CA TRP A 81 1836 3290 2524 66 1250 -140 C
ATOM 432 C TRP A 81 14.074 -11.079 -53.636 1.00 25.61 C
ANISOU 432 C TRP A 81 2516 3906 3309 30 1234 -166 C
ATOM 433 O TRP A 81 13.734 -9.928 -53.925 1.00 30.68 O
ANISOU 433 O TRP A 81 3092 4572 3993 11 1247 -186 O
ATOM 434 CB TRP A 81 15.449 -10.654 -51.566 1.00 20.16 C
ANISOU 434 CB TRP A 81 1823 3336 2501 151 1228 -185 C
ATOM 435 CG TRP A 81 14.427 -11.119 -50.570 1.00 28.94 C
ANISOU 435 CG TRP A 81 2976 4385 3634 205 1162 -241 C
ATOM 436 CD1 TRP A 81 14.563 -12.141 -49.675 1.00 29.46 C
ANISOU 436 CD1 TRP A 81 3102 4431 3661 248 1127 -250 C
ATOM 437 CD2 TRP A 81 13.131 -10.550 -50.331 1.00 30.17 C
ANISOU 437 CD2 TRP A 81 3118 4493 3853 217 1124 -299 C
ATOM 438 NE1 TRP A 81 13.428 -12.257 -48.911 1.00 28.07 N
ANISOU 438 NE1 TRP A 81 2954 4194 3519 281 1074 -303 N
ATOM 439 CE2 TRP A 81 12.533 -11.292 -49.293 1.00 23.56 C
ANISOU 439 CE2 TRP A 81 2341 3605 3007 264 1071 -334 C
ATOM 440 CE3 TRP A 81 12.412 -9.495 -50.906 1.00 34.34 C
ANISOU 440 CE3 TRP A 81 3584 5019 4444 190 1131 -327 C
ATOM 441 CZ2 TRP A 81 11.251 -11.014 -48.819 1.00 31.19 C
ANISOU 441 CZ2 TRP A 81 3317 4516 4018 285 1026 -391 C
ATOM 442 CZ3 TRP A 81 11.136 -9.220 -50.430 1.00 34.28 C
ANISOU 442 CZ3 TRP A 81 3579 4960 4484 217 1081 -392 C
ATOM 443 CH2 TRP A 81 10.571 -9.976 -49.395 1.00 32.64 C
ANISOU 443 CH2 TRP A 81 3443 4700 4260 264 1031 -422 C
ATOM 444 N LEU A 82 13.334 -12.151 -53.915 1.00 20.41 N
ANISOU 444 N LEU A 82 1917 3153 2683 21 1209 -168 N
ATOM 445 CA LEU A 82 12.087 -12.073 -54.668 1.00 20.63 C
ANISOU 445 CA LEU A 82 1944 3098 2795 -15 1201 -189 C
ATOM 446 C LEU A 82 11.021 -12.892 -53.955 1.00 27.82 C
ANISOU 446 C LEU A 82 2912 3939 3719 32 1147 -234 C
ATOM 447 O LEU A 82 11.164 -14.111 -53.810 1.00 26.80 O
ANISOU 447 O LEU A 82 2845 3769 3568 46 1136 -214 O
ATOM 448 CB LEU A 82 12.275 -12.572 -56.103 1.00 19.14 C
ANISOU 448 CB LEU A 82 1778 2849 2643 -89 1247 -127 C
ATOM 449 CG LEU A 82 11.016 -12.705 -56.965 1.00 21.45 C
ANISOU 449 CG LEU A 82 2083 3044 3024 -127 1244 -146 C
ATOM 450 CD1 LEU A 82 10.296 -11.368 -57.102 1.00 19.33 C
ANISOU 450 CD1 LEU A 82 1733 2800 2810 -149 1237 -198 C
ATOM 451 CD2 LEU A 82 11.360 -13.268 -58.334 1.00 19.28 C
ANISOU 451 CD2 LEU A 82 1842 2703 2782 -196 1292 -76 C
ATOM 452 N ASP A 83 9.951 -12.227 -53.531 1.00 23.12 N
ANISOU 452 N ASP A 83 2295 3328 3161 53 1114 -296 N
ATOM 453 CA ASP A 83 8.887 -12.849 -52.752 1.00 17.77 C
ANISOU 453 CA ASP A 83 1673 2588 2490 94 1065 -340 C
ATOM 454 C ASP A 83 7.641 -12.938 -53.621 1.00 22.70 C
ANISOU 454 C ASP A 83 2311 3128 3187 57 1069 -363 C
ATOM 455 O ASP A 83 7.061 -11.912 -53.995 1.00 25.25 O
ANISOU 455 O ASP A 83 2575 3457 3561 39 1072 -401 O
ATOM 456 CB ASP A 83 8.608 -12.061 -51.475 1.00 23.58 C
ANISOU 456 CB ASP A 83 2389 3363 3207 154 1025 -396 C
ATOM 457 CG ASP A 83 7.736 -12.826 -50.496 1.00 33.37 C
ANISOU 457 CG ASP A 83 3700 4543 4435 193 977 -431 C
ATOM 458 OD1 ASP A 83 7.006 -13.743 -50.924 1.00 28.18 O
ANISOU 458 OD1 ASP A 83 3096 3811 3799 171 974 -425 O
ATOM 459 OD2 ASP A 83 7.784 -12.512 -49.291 1.00 37.60 O
ANISOU 459 OD2 ASP A 83 4241 5103 4940 245 946 -462 O
ATOM 460 N LEU A 84 7.226 -14.164 -53.927 1.00 17.39 N
ANISOU 460 N LEU A 84 1709 2380 2520 49 1070 -346 N
ATOM 461 CA LEU A 84 6.025 -14.420 -54.709 1.00 16.22 C
ANISOU 461 CA LEU A 84 1588 2144 2431 21 1079 -370 C
ATOM 462 C LEU A 84 5.012 -15.233 -53.912 1.00 21.16 C
ANISOU 462 C LEU A 84 2290 2713 3038 58 1039 -406 C
ATOM 463 O LEU A 84 4.240 -16.008 -54.478 1.00 16.79 O
ANISOU 463 O LEU A 84 1791 2082 2505 43 1048 -409 O
ATOM 464 CB LEU A 84 6.376 -15.128 -56.015 1.00 20.40 C
ANISOU 464 CB LEU A 84 2140 2625 2989 -30 1126 -315 C
ATOM 465 CG LEU A 84 7.348 -14.367 -56.916 1.00 23.25 C
ANISOU 465 CG LEU A 84 2438 3029 3367 -84 1167 -267 C
ATOM 466 CD1 LEU A 84 8.064 -15.311 -57.874 1.00 22.96 C
ANISOU 466 CD1 LEU A 84 2447 2948 3329 -115 1199 -194 C
ATOM 467 CD2 LEU A 84 6.618 -13.271 -57.680 1.00 27.78 C
ANISOU 467 CD2 LEU A 84 2967 3589 3998 -131 1139 -291 C
ATOM 468 N SER A 85 5.020 -15.065 -52.590 1.00 27.08 N
ANISOU 468 N SER A 85 3047 3498 3744 106 997 -431 N
ATOM 469 CA SER A 85 4.110 -15.803 -51.728 1.00 23.02 C
ANISOU 469 CA SER A 85 2605 2933 3207 132 960 -458 C
ATOM 470 C SER A 85 2.666 -15.482 -52.088 1.00 23.45 C
ANISOU 470 C SER A 85 2690 2919 3301 125 955 -510 C
ATOM 471 O SER A 85 2.331 -14.339 -52.412 1.00 16.63 O
ANISOU 471 O SER A 85 1781 2069 2469 121 932 -537 O
ATOM 472 CB SER A 85 4.373 -15.456 -50.263 1.00 18.48 C
ANISOU 472 CB SER A 85 2027 2405 2589 179 920 -481 C
ATOM 473 OG SER A 85 5.733 -15.672 -49.920 1.00 26.38 O
ANISOU 473 OG SER A 85 3000 3472 3549 190 925 -442 O
ATOM 474 N ARG A 86 1.818 -16.509 -52.051 1.00 18.54 N
ANISOU 474 N ARG A 86 2150 2228 2666 119 948 -513 N
ATOM 475 CA ARG A 86 0.378 -16.367 -52.269 1.00 19.10 C
ANISOU 475 CA ARG A 86 2284 2229 2745 113 910 -548 C
ATOM 476 C ARG A 86 0.070 -15.621 -53.563 1.00 19.70 C
ANISOU 476 C ARG A 86 2333 2289 2863 77 885 -543 C
ATOM 477 O ARG A 86 -0.681 -14.644 -53.581 1.00 22.69 O
ANISOU 477 O ARG A 86 2706 2661 3256 83 827 -576 O
ATOM 478 CB ARG A 86 -0.282 -15.665 -51.082 1.00 20.92 C
ANISOU 478 CB ARG A 86 2536 2460 2953 153 857 -593 C
ATOM 479 CG ARG A 86 -1.693 -16.130 -50.805 1.00 18.76 C
ANISOU 479 CG ARG A 86 2369 2108 2651 151 821 -615 C
ATOM 480 CD ARG A 86 -1.658 -17.460 -50.091 1.00 29.90 C
ANISOU 480 CD ARG A 86 3835 3500 4024 148 857 -600 C
ATOM 481 NE ARG A 86 -2.618 -18.420 -50.612 1.00 23.83 N
ANISOU 481 NE ARG A 86 3149 2668 3239 117 866 -593 N
ATOM 482 CZ ARG A 86 -2.708 -19.677 -50.190 1.00 30.16 C
ANISOU 482 CZ ARG A 86 3986 3464 4011 99 875 -562 C
ATOM 483 NH1 ARG A 86 -1.894 -20.126 -49.242 1.00 25.35 N
ANISOU 483 NH1 ARG A 86 3344 2901 3388 108 873 -540 N
ATOM 484 NH2 ARG A 86 -3.612 -20.489 -50.714 1.00 22.10 N
ANISOU 484 NH2 ARG A 86 3031 2393 2975 72 886 -559 N
ATOM 485 N CYS A 87 0.661 -16.086 -54.659 1.00 25.46 N
ANISOU 485 N CYS A 87 3046 3011 3617 40 925 -502 N
ATOM 486 CA CYS A 87 0.457 -15.446 -55.950 1.00 24.88 C
ANISOU 486 CA CYS A 87 2947 2916 3589 -5 905 -495 C
ATOM 487 C CYS A 87 -0.363 -16.298 -56.907 1.00 23.27 C
ANISOU 487 C CYS A 87 2823 2625 3393 -33 899 -492 C
ATOM 488 O CYS A 87 -0.428 -15.981 -58.099 1.00 21.92 O
ANISOU 488 O CYS A 87 2641 2426 3263 -76 888 -481 O
ATOM 489 CB CYS A 87 1.799 -15.076 -56.580 1.00 44.11 C
ANISOU 489 CB CYS A 87 5301 5406 6053 -35 951 -449 C
ATOM 490 SG CYS A 87 2.558 -13.623 -55.820 1.00 47.64 S
ANISOU 490 SG CYS A 87 5638 5961 6503 -14 952 -468 S
ATOM 491 N GLU A 88 -1.006 -17.358 -56.410 1.00 20.16 N
ANISOU 491 N GLU A 88 2510 2188 2961 -11 907 -505 N
ATOM 492 CA GLU A 88 -1.885 -18.219 -57.202 1.00 23.86 C
ANISOU 492 CA GLU A 88 3061 2578 3428 -30 907 -514 C
ATOM 493 C GLU A 88 -1.176 -18.816 -58.413 1.00 22.09 C
ANISOU 493 C GLU A 88 2826 2326 3240 -57 944 -475 C
ATOM 494 O GLU A 88 -1.821 -19.185 -59.398 1.00 20.09 O
ANISOU 494 O GLU A 88 2626 2005 3002 -80 933 -486 O
ATOM 495 CB GLU A 88 -3.147 -17.456 -57.635 1.00 31.15 C
ANISOU 495 CB GLU A 88 4025 3457 4353 -45 838 -554 C
ATOM 496 CG GLU A 88 -4.043 -17.051 -56.469 1.00 35.62 C
ANISOU 496 CG GLU A 88 4633 4028 4874 -13 792 -591 C
ATOM 497 CD GLU A 88 -4.951 -15.880 -56.798 1.00 45.73 C
ANISOU 497 CD GLU A 88 5918 5291 6165 -19 707 -626 C
ATOM 498 OE1 GLU A 88 -4.842 -14.832 -56.127 1.00 51.63 O
ANISOU 498 OE1 GLU A 88 6612 6085 6920 6 666 -642 O
ATOM 499 OE2 GLU A 88 -5.776 -16.004 -57.727 1.00 49.02 O
ANISOU 499 OE2 GLU A 88 6391 5649 6584 -46 678 -643 O
ATOM 500 N ILE A 89 0.150 -18.919 -58.354 1.00 24.71 N
ANISOU 500 N ILE A 89 3098 2708 3584 -54 985 -431 N
ATOM 501 CA ILE A 89 0.925 -19.382 -59.499 1.00 15.77 C
ANISOU 501 CA ILE A 89 1958 1546 2486 -79 1014 -386 C
ATOM 502 C ILE A 89 0.679 -20.871 -59.700 1.00 19.67 C
ANISOU 502 C ILE A 89 2518 1986 2972 -56 1041 -388 C
ATOM 503 O ILE A 89 0.870 -21.677 -58.781 1.00 19.76 O
ANISOU 503 O ILE A 89 2532 2023 2951 -19 1068 -393 O
ATOM 504 CB ILE A 89 2.418 -19.087 -59.305 1.00 16.89 C
ANISOU 504 CB ILE A 89 2029 1759 2630 -80 1048 -335 C
ATOM 505 CG1 ILE A 89 2.647 -17.588 -59.094 1.00 17.16 C
ANISOU 505 CG1 ILE A 89 1988 1857 2675 -101 1030 -341 C
ATOM 506 CG2 ILE A 89 3.221 -19.591 -60.498 1.00 21.11 C
ANISOU 506 CG2 ILE A 89 2572 2254 3196 -106 1073 -280 C
ATOM 507 CD1 ILE A 89 4.046 -17.240 -58.653 1.00 16.21 C
ANISOU 507 CD1 ILE A 89 1799 1820 2538 -95 1071 -301 C
ATOM 508 N GLU A 90 0.243 -21.241 -60.904 1.00 17.63 N
ANISOU 508 N GLU A 90 2306 1650 2743 -79 1033 -391 N
ATOM 509 CA GLU A 90 0.136 -22.638 -61.290 1.00 22.05 C
ANISOU 509 CA GLU A 90 2917 2156 3304 -53 1062 -394 C
ATOM 510 C GLU A 90 1.217 -23.063 -62.271 1.00 25.32 C
ANISOU 510 C GLU A 90 3321 2542 3759 -58 1080 -340 C
ATOM 511 O GLU A 90 1.521 -24.257 -62.357 1.00 19.23 O
ANISOU 511 O GLU A 90 2569 1748 2990 -20 1107 -334 O
ATOM 512 CB GLU A 90 -1.235 -22.920 -61.914 1.00 27.67 C
ANISOU 512 CB GLU A 90 3707 2792 4014 -63 1042 -446 C
ATOM 513 CG GLU A 90 -2.368 -23.063 -60.913 1.00 33.44 C
ANISOU 513 CG GLU A 90 4480 3535 4692 -45 1038 -497 C
ATOM 514 CD GLU A 90 -3.534 -23.867 -61.466 1.00 42.90 C
ANISOU 514 CD GLU A 90 5765 4661 5873 -42 1043 -544 C
ATOM 515 OE1 GLU A 90 -4.078 -23.481 -62.523 1.00 51.58 O
ANISOU 515 OE1 GLU A 90 6903 5702 6992 -69 1008 -561 O
ATOM 516 OE2 GLU A 90 -3.902 -24.888 -60.847 1.00 51.06 O
ANISOU 516 OE2 GLU A 90 6821 5710 6868 -17 1072 -557 O
ATOM 517 N THR A 91 1.817 -22.123 -62.993 1.00 23.55 N
ANISOU 517 N THR A 91 3064 2318 3565 -104 1066 -301 N
ATOM 518 CA THR A 91 2.706 -22.456 -64.095 1.00 21.94 C
ANISOU 518 CA THR A 91 2871 2066 3400 -121 1077 -246 C
ATOM 519 C THR A 91 3.943 -21.582 -64.018 1.00 18.78 C
ANISOU 519 C THR A 91 2405 1729 3000 -152 1090 -184 C
ATOM 520 O THR A 91 3.832 -20.356 -63.927 1.00 21.38 O
ANISOU 520 O THR A 91 2688 2100 3335 -195 1078 -190 O
ATOM 521 CB THR A 91 1.998 -22.265 -65.439 1.00 18.00 C
ANISOU 521 CB THR A 91 2424 1470 2946 -165 1046 -263 C
ATOM 522 OG1 THR A 91 0.802 -23.058 -65.462 1.00 25.22 O
ANISOU 522 OG1 THR A 91 3403 2332 3848 -133 1038 -327 O
ATOM 523 CG2 THR A 91 2.904 -22.688 -66.583 1.00 18.67 C
ANISOU 523 CG2 THR A 91 2533 1489 3072 -181 1054 -205 C
ATOM 524 N ILE A 92 5.109 -22.215 -64.035 1.00 20.99 N
ANISOU 524 N ILE A 92 2682 2022 3272 -129 1116 -128 N
ATOM 525 CA ILE A 92 6.386 -21.535 -64.206 1.00 18.15 C
ANISOU 525 CA ILE A 92 2279 1708 2907 -163 1136 -58 C
ATOM 526 C ILE A 92 6.835 -21.821 -65.633 1.00 19.73 C
ANISOU 526 C ILE A 92 2530 1816 3151 -199 1132 -4 C
ATOM 527 O ILE A 92 7.161 -22.964 -65.972 1.00 20.28 O
ANISOU 527 O ILE A 92 2649 1830 3227 -154 1131 16 O
ATOM 528 CB ILE A 92 7.427 -22.008 -63.182 1.00 19.66 C
ANISOU 528 CB ILE A 92 2443 1979 3049 -112 1161 -30 C
ATOM 529 CG1 ILE A 92 6.892 -21.841 -61.758 1.00 25.05 C
ANISOU 529 CG1 ILE A 92 3087 2737 3692 -75 1161 -90 C
ATOM 530 CG2 ILE A 92 8.726 -21.244 -63.351 1.00 18.36 C
ANISOU 530 CG2 ILE A 92 2242 1869 2866 -151 1187 42 C
ATOM 531 CD1 ILE A 92 7.764 -22.469 -60.701 1.00 22.82 C
ANISOU 531 CD1 ILE A 92 2784 2523 3363 -21 1177 -77 C
ATOM 532 N GLU A 93 6.822 -20.797 -66.482 1.00 22.28 N
ANISOU 532 N GLU A 93 2841 2115 3509 -278 1127 16 N
ATOM 533 CA GLU A 93 7.208 -20.998 -67.869 1.00 21.55 C
ANISOU 533 CA GLU A 93 2804 1923 3462 -323 1120 67 C
ATOM 534 C GLU A 93 8.698 -21.314 -67.960 1.00 22.56 C
ANISOU 534 C GLU A 93 2940 2067 3564 -317 1149 158 C
ATOM 535 O GLU A 93 9.478 -21.038 -67.044 1.00 26.33 O
ANISOU 535 O GLU A 93 3367 2647 3990 -300 1177 183 O
ATOM 536 CB GLU A 93 6.848 -19.776 -68.713 1.00 21.11 C
ANISOU 536 CB GLU A 93 2725 1843 3453 -421 1108 65 C
ATOM 537 CG GLU A 93 5.355 -19.686 -69.010 1.00 20.95 C
ANISOU 537 CG GLU A 93 2729 1767 3465 -426 1062 -19 C
ATOM 538 CD GLU A 93 5.034 -18.718 -70.128 1.00 23.91 C
ANISOU 538 CD GLU A 93 3098 2089 3900 -524 1037 -20 C
ATOM 539 OE1 GLU A 93 5.847 -17.810 -70.378 1.00 26.11 O
ANISOU 539 OE1 GLU A 93 3321 2408 4192 -595 1063 33 O
ATOM 540 OE2 GLU A 93 3.966 -18.875 -70.765 1.00 32.04 O
ANISOU 540 OE2 GLU A 93 4177 3035 4961 -533 994 -76 O
ATOM 541 N ASP A 94 9.087 -21.899 -69.096 1.00 26.67 N
ANISOU 541 N ASP A 94 3533 2481 4118 -330 1137 208 N
ATOM 542 CA ASP A 94 10.384 -22.562 -69.192 1.00 23.90 C
ANISOU 542 CA ASP A 94 3218 2123 3739 -299 1149 290 C
ATOM 543 C ASP A 94 11.562 -21.600 -69.093 1.00 29.55 C
ANISOU 543 C ASP A 94 3896 2916 4417 -362 1189 369 C
ATOM 544 O ASP A 94 12.696 -22.057 -68.903 1.00 32.19 O
ANISOU 544 O ASP A 94 4253 3272 4705 -331 1201 436 O
ATOM 545 CB ASP A 94 10.473 -23.368 -70.492 1.00 24.24 C
ANISOU 545 CB ASP A 94 3357 2021 3832 -295 1119 325 C
ATOM 546 CG ASP A 94 10.394 -22.501 -71.736 1.00 36.64 C
ANISOU 546 CG ASP A 94 4956 3512 5455 -405 1116 357 C
ATOM 547 OD1 ASP A 94 9.835 -21.387 -71.665 1.00 43.46 O
ANISOU 547 OD1 ASP A 94 5759 4421 6333 -475 1126 323 O
ATOM 548 OD2 ASP A 94 10.891 -22.953 -72.793 1.00 50.15 O
ANISOU 548 OD2 ASP A 94 6748 5111 7197 -419 1099 416 O
ATOM 549 N LYS A 95 11.333 -20.296 -69.221 1.00 22.86 N
ANISOU 549 N LYS A 95 2990 2112 3585 -449 1210 360 N
ATOM 550 CA LYS A 95 12.365 -19.285 -69.019 1.00 26.44 C
ANISOU 550 CA LYS A 95 3390 2657 3999 -512 1261 421 C
ATOM 551 C LYS A 95 11.844 -18.174 -68.122 1.00 31.30 C
ANISOU 551 C LYS A 95 3900 3387 4604 -528 1279 355 C
ATOM 552 O LYS A 95 12.112 -16.988 -68.342 1.00 29.52 O
ANISOU 552 O LYS A 95 3613 3214 4388 -611 1313 371 O
ATOM 553 CB LYS A 95 12.855 -18.724 -70.350 1.00 27.51 C
ANISOU 553 CB LYS A 95 3560 2718 4173 -621 1277 496 C
ATOM 554 CG LYS A 95 13.635 -19.723 -71.186 1.00 33.46 C
ANISOU 554 CG LYS A 95 4425 3362 4925 -605 1261 580 C
ATOM 555 CD LYS A 95 14.151 -19.059 -72.442 1.00 48.86 C
ANISOU 555 CD LYS A 95 6412 5240 6911 -727 1282 659 C
ATOM 556 CE LYS A 95 14.901 -20.027 -73.335 1.00 57.94 C
ANISOU 556 CE LYS A 95 7687 6264 8063 -711 1258 746 C
ATOM 557 NZ LYS A 95 15.440 -19.354 -74.550 1.00 65.70 N
ANISOU 557 NZ LYS A 95 8714 7170 9077 -841 1282 832 N
ATOM 558 N ALA A 96 11.090 -18.547 -67.085 1.00 27.60 N
ANISOU 558 N ALA A 96 3409 2960 4119 -448 1256 277 N
ATOM 559 CA ALA A 96 10.464 -17.544 -66.231 1.00 21.28 C
ANISOU 559 CA ALA A 96 2520 2253 3314 -453 1259 208 C
ATOM 560 C ALA A 96 11.497 -16.723 -65.474 1.00 21.49 C
ANISOU 560 C ALA A 96 2474 2406 3284 -464 1312 236 C
ATOM 561 O ALA A 96 11.261 -15.545 -65.184 1.00 26.84 O
ANISOU 561 O ALA A 96 3068 3157 3973 -501 1326 200 O
ATOM 562 CB ALA A 96 9.496 -18.213 -65.257 1.00 20.20 C
ANISOU 562 CB ALA A 96 2391 2123 3163 -366 1225 128 C
ATOM 563 N TRP A 97 12.647 -17.321 -65.158 1.00 21.61 N
ANISOU 563 N TRP A 97 2520 2452 3239 -430 1338 296 N
ATOM 564 CA TRP A 97 13.679 -16.677 -64.357 1.00 26.78 C
ANISOU 564 CA TRP A 97 3118 3230 3825 -429 1389 319 C
ATOM 565 C TRP A 97 14.925 -16.335 -65.168 1.00 28.73 C
ANISOU 565 C TRP A 97 3387 3482 4047 -503 1440 421 C
ATOM 566 O TRP A 97 16.017 -16.210 -64.604 1.00 26.50 O
ANISOU 566 O TRP A 97 3094 3285 3687 -489 1481 460 O
ATOM 567 CB TRP A 97 14.022 -17.554 -63.150 1.00 31.76 C
ANISOU 567 CB TRP A 97 3764 3911 4391 -329 1377 300 C
ATOM 568 CG TRP A 97 12.914 -17.533 -62.146 1.00 33.53 C
ANISOU 568 CG TRP A 97 3951 4161 4629 -274 1344 202 C
ATOM 569 CD1 TRP A 97 12.368 -16.429 -61.571 1.00 38.32 C
ANISOU 569 CD1 TRP A 97 4480 4835 5245 -286 1349 140 C
ATOM 570 CD2 TRP A 97 12.199 -18.654 -61.624 1.00 26.85 C
ANISOU 570 CD2 TRP A 97 3144 3270 3787 -201 1302 155 C
ATOM 571 NE1 TRP A 97 11.361 -16.790 -60.712 1.00 33.91 N
ANISOU 571 NE1 TRP A 97 3923 4269 4692 -225 1309 64 N
ATOM 572 CE2 TRP A 97 11.238 -18.153 -60.726 1.00 34.26 C
ANISOU 572 CE2 TRP A 97 4037 4247 4733 -177 1284 72 C
ATOM 573 CE3 TRP A 97 12.282 -20.030 -61.823 1.00 27.48 C
ANISOU 573 CE3 TRP A 97 3291 3282 3867 -153 1277 174 C
ATOM 574 CZ2 TRP A 97 10.370 -18.981 -60.033 1.00 30.17 C
ANISOU 574 CZ2 TRP A 97 3545 3701 4216 -118 1250 14 C
ATOM 575 CZ3 TRP A 97 11.422 -20.846 -61.134 1.00 42.16 C
ANISOU 575 CZ3 TRP A 97 5163 5122 5734 -92 1247 109 C
ATOM 576 CH2 TRP A 97 10.480 -20.323 -60.250 1.00 42.76 C
ANISOU 576 CH2 TRP A 97 5200 5237 5812 -80 1237 33 C
ATOM 577 N HIS A 98 14.773 -16.154 -66.477 1.00 27.71 N
ANISOU 577 N HIS A 98 3290 3260 3977 -585 1438 462 N
ATOM 578 CA HIS A 98 15.874 -15.683 -67.306 1.00 29.66 C
ANISOU 578 CA HIS A 98 3558 3506 4205 -675 1492 561 C
ATOM 579 C HIS A 98 16.354 -14.321 -66.826 1.00 34.02 C
ANISOU 579 C HIS A 98 4004 4195 4726 -730 1562 553 C
ATOM 580 O HIS A 98 15.550 -13.414 -66.599 1.00 34.38 O
ANISOU 580 O HIS A 98 3957 4286 4818 -751 1559 477 O
ATOM 581 CB HIS A 98 15.421 -15.605 -68.765 1.00 28.39 C
ANISOU 581 CB HIS A 98 3443 3216 4130 -763 1472 590 C
ATOM 582 CG HIS A 98 16.415 -14.961 -69.682 1.00 32.41 C
ANISOU 582 CG HIS A 98 3966 3717 4630 -879 1532 689 C
ATOM 583 ND1 HIS A 98 16.443 -13.602 -69.915 1.00 33.14 N
ANISOU 583 ND1 HIS A 98 3963 3882 4746 -979 1578 680 N
ATOM 584 CD2 HIS A 98 17.398 -15.492 -70.446 1.00 34.22 C
ANISOU 584 CD2 HIS A 98 4298 3874 4831 -910 1545 797 C
ATOM 585 CE1 HIS A 98 17.408 -13.323 -70.773 1.00 35.23 C
ANISOU 585 CE1 HIS A 98 4269 4131 4984 -1065 1602 772 C
ATOM 586 NE2 HIS A 98 18.003 -14.453 -71.111 1.00 37.68 N
ANISOU 586 NE2 HIS A 98 4705 4344 5267 -1033 1597 853 N
ATOM 587 N GLY A 99 17.668 -14.181 -66.657 1.00 35.27 N
ANISOU 587 N GLY A 99 4177 4425 4798 -743 1610 623 N
ATOM 588 CA GLY A 99 18.259 -12.918 -66.265 1.00 30.40 C
ANISOU 588 CA GLY A 99 3470 3952 4129 -780 1637 608 C
ATOM 589 C GLY A 99 18.500 -12.737 -64.781 1.00 32.40 C
ANISOU 589 C GLY A 99 3667 4337 4305 -688 1631 544 C
ATOM 590 O GLY A 99 19.088 -11.721 -64.389 1.00 41.72 O
ANISOU 590 O GLY A 99 4775 5641 5434 -708 1656 532 O
ATOM 591 N LEU A 100 18.074 -13.682 -63.947 1.00 35.49 N
ANISOU 591 N LEU A 100 4089 4705 4690 -588 1598 501 N
ATOM 592 CA LEU A 100 18.229 -13.565 -62.498 1.00 34.18 C
ANISOU 592 CA LEU A 100 3878 4651 4457 -500 1579 432 C
ATOM 593 C LEU A 100 19.512 -14.230 -62.008 1.00 35.96 C
ANISOU 593 C LEU A 100 4164 4921 4578 -458 1600 488 C
ATOM 594 O LEU A 100 19.485 -15.084 -61.123 1.00 33.38 O
ANISOU 594 O LEU A 100 3865 4597 4220 -371 1572 458 O
ATOM 595 CB LEU A 100 17.012 -14.156 -61.799 1.00 23.09 C
ANISOU 595 CB LEU A 100 2469 3203 3101 -421 1526 347 C
ATOM 596 CG LEU A 100 15.681 -13.466 -62.092 1.00 30.13 C
ANISOU 596 CG LEU A 100 3302 4061 4085 -450 1500 280 C
ATOM 597 CD1 LEU A 100 14.588 -14.026 -61.206 1.00 22.08 C
ANISOU 597 CD1 LEU A 100 2286 3015 3089 -367 1448 197 C
ATOM 598 CD2 LEU A 100 15.828 -11.968 -61.894 1.00 32.64 C
ANISOU 598 CD2 LEU A 100 3518 4489 4393 -486 1510 247 C
ATOM 599 N HIS A 101 20.657 -13.828 -62.569 1.00 37.78 N
ANISOU 599 N HIS A 101 4417 5188 4748 -524 1648 569 N
ATOM 600 CA HIS A 101 21.904 -14.505 -62.219 1.00 39.20 C
ANISOU 600 CA HIS A 101 4671 5399 4823 -489 1668 633 C
ATOM 601 C HIS A 101 22.299 -14.262 -60.767 1.00 37.14 C
ANISOU 601 C HIS A 101 4363 5268 4481 -415 1654 559 C
ATOM 602 O HIS A 101 23.045 -15.060 -60.192 1.00 41.32 O
ANISOU 602 O HIS A 101 4951 5814 4934 -355 1652 583 O
ATOM 603 CB HIS A 101 23.046 -14.074 -63.147 1.00 48.40 C
ANISOU 603 CB HIS A 101 5880 6576 5933 -583 1721 740 C
ATOM 604 CG HIS A 101 22.666 -13.041 -64.159 1.00 63.29 C
ANISOU 604 CG HIS A 101 7711 8448 7887 -692 1742 750 C
ATOM 605 ND1 HIS A 101 22.797 -11.688 -63.928 1.00 66.72 N
ANISOU 605 ND1 HIS A 101 8038 9006 8306 -736 1768 709 N
ATOM 606 CD2 HIS A 101 22.182 -13.162 -65.418 1.00 65.98 C
ANISOU 606 CD2 HIS A 101 8089 8665 8314 -765 1739 799 C
ATOM 607 CE1 HIS A 101 22.401 -11.021 -64.996 1.00 67.49 C
ANISOU 607 CE1 HIS A 101 8102 9061 8479 -832 1782 733 C
ATOM 608 NE2 HIS A 101 22.021 -11.892 -65.914 1.00 67.64 N
ANISOU 608 NE2 HIS A 101 8211 8929 8560 -856 1762 785 N
ATOM 609 N HIS A 102 21.803 -13.189 -60.152 1.00 39.92 N
ANISOU 609 N HIS A 102 4611 5708 4849 -413 1642 470 N
ATOM 610 CA HIS A 102 22.202 -12.813 -58.801 1.00 39.32 C
ANISOU 610 CA HIS A 102 4489 5753 4698 -349 1628 396 C
ATOM 611 C HIS A 102 21.142 -13.103 -57.746 1.00 35.42 C
ANISOU 611 C HIS A 102 3964 5248 4248 -263 1559 295 C
ATOM 612 O HIS A 102 21.345 -12.757 -56.576 1.00 36.99 O
ANISOU 612 O HIS A 102 4123 5537 4394 -208 1538 226 O
ATOM 613 CB HIS A 102 22.563 -11.330 -58.754 1.00 47.17 C
ANISOU 613 CB HIS A 102 5388 6869 5665 -394 1664 378 C
ATOM 614 CG HIS A 102 23.840 -11.001 -59.458 1.00 58.47 C
ANISOU 614 CG HIS A 102 6849 8347 7019 -473 1733 469 C
ATOM 615 ND1 HIS A 102 23.968 -9.915 -60.295 1.00 62.11 N
ANISOU 615 ND1 HIS A 102 7248 8847 7505 -556 1779 512 N
ATOM 616 CD2 HIS A 102 25.049 -11.609 -59.442 1.00 60.67 C
ANISOU 616 CD2 HIS A 102 7219 8638 7196 -481 1764 531 C
ATOM 617 CE1 HIS A 102 25.201 -9.870 -60.768 1.00 64.41 C
ANISOU 617 CE1 HIS A 102 7589 9175 7708 -617 1836 598 C
ATOM 618 NE2 HIS A 102 25.877 -10.887 -60.266 1.00 63.53 N
ANISOU 618 NE2 HIS A 102 7577 9047 7515 -574 1827 610 N
ATOM 619 N LEU A 103 20.025 -13.722 -58.116 1.00 30.28 N
ANISOU 619 N LEU A 103 3333 4487 3686 -251 1525 284 N
ATOM 620 CA LEU A 103 18.974 -13.987 -57.140 1.00 33.46 C
ANISOU 620 CA LEU A 103 3714 4875 4126 -177 1459 193 C
ATOM 621 C LEU A 103 19.443 -15.042 -56.148 1.00 33.07 C
ANISOU 621 C LEU A 103 3713 4835 4016 -103 1432 176 C
ATOM 622 O LEU A 103 19.793 -16.161 -56.537 1.00 29.63 O
ANISOU 622 O LEU A 103 3348 4336 3575 -91 1444 234 O
ATOM 623 CB LEU A 103 17.694 -14.439 -57.834 1.00 25.42 C
ANISOU 623 CB LEU A 103 2713 3736 3209 -189 1437 185 C
ATOM 624 CG LEU A 103 16.505 -14.466 -56.870 1.00 26.05 C
ANISOU 624 CG LEU A 103 2768 3805 3324 -127 1371 92 C
ATOM 625 CD1 LEU A 103 16.018 -13.049 -56.594 1.00 20.76 C
ANISOU 625 CD1 LEU A 103 2015 3200 2675 -136 1361 39 C
ATOM 626 CD2 LEU A 103 15.380 -15.357 -57.375 1.00 19.82 C
ANISOU 626 CD2 LEU A 103 2023 2894 2612 -124 1350 85 C
ATOM 627 N SER A 104 19.448 -14.683 -54.865 1.00 32.63 N
ANISOU 627 N SER A 104 3619 4858 3921 -50 1395 98 N
ATOM 628 CA SER A 104 19.847 -15.598 -53.805 1.00 28.63 C
ANISOU 628 CA SER A 104 3149 4364 3364 13 1364 65 C
ATOM 629 C SER A 104 18.676 -16.137 -52.999 1.00 24.74 C
ANISOU 629 C SER A 104 2656 3823 2923 68 1292 -5 C
ATOM 630 O SER A 104 18.799 -17.216 -52.409 1.00 22.03 O
ANISOU 630 O SER A 104 2351 3455 2564 111 1267 -18 O
ATOM 631 CB SER A 104 20.826 -14.909 -52.849 1.00 33.81 C
ANISOU 631 CB SER A 104 3777 5136 3932 25 1376 20 C
ATOM 632 OG SER A 104 20.156 -13.958 -52.036 1.00 34.25 O
ANISOU 632 OG SER A 104 3766 5244 4005 57 1333 -57 O
ATOM 633 N ASN A 105 17.559 -15.416 -52.946 1.00 23.07 N
ANISOU 633 N ASN A 105 2402 3595 2767 68 1262 -46 N
ATOM 634 CA ASN A 105 16.391 -15.824 -52.177 1.00 19.76 C
ANISOU 634 CA ASN A 105 1992 3125 2388 114 1197 -105 C
ATOM 635 C ASN A 105 15.163 -15.820 -53.075 1.00 26.61 C
ANISOU 635 C ASN A 105 2867 3900 3342 82 1194 -99 C
ATOM 636 O ASN A 105 14.861 -14.807 -53.713 1.00 36.67 O
ANISOU 636 O ASN A 105 4101 5181 4649 44 1216 -94 O
ATOM 637 CB ASN A 105 16.175 -14.897 -50.971 1.00 22.96 C
ANISOU 637 CB ASN A 105 2358 3597 2769 167 1161 -163 C
ATOM 638 CG ASN A 105 17.160 -15.161 -49.847 1.00 30.47 C
ANISOU 638 CG ASN A 105 3316 4618 3641 215 1149 -184 C
ATOM 639 OD1 ASN A 105 16.884 -15.944 -48.939 1.00 33.74 O
ANISOU 639 OD1 ASN A 105 3764 5002 4053 255 1102 -217 O
ATOM 640 ND2 ASN A 105 18.316 -14.509 -49.903 1.00 32.08 N
ANISOU 640 ND2 ASN A 105 3502 4898 3790 201 1185 -166 N
ATOM 641 N LEU A 106 14.466 -16.954 -53.126 1.00 19.98 N
ANISOU 641 N LEU A 106 2076 2976 2539 96 1168 -105 N
ATOM 642 CA LEU A 106 13.233 -17.108 -53.894 1.00 19.18 C
ANISOU 642 CA LEU A 106 1991 2781 2514 70 1164 -111 C
ATOM 643 C LEU A 106 12.183 -17.756 -53.005 1.00 23.01 C
ANISOU 643 C LEU A 106 2507 3224 3013 110 1106 -165 C
ATOM 644 O LEU A 106 12.410 -18.847 -52.470 1.00 21.61 O
ANISOU 644 O LEU A 106 2360 3037 2815 140 1086 -168 O
ATOM 645 CB LEU A 106 13.460 -17.950 -55.155 1.00 17.41 C
ANISOU 645 CB LEU A 106 1807 2485 2324 38 1210 -48 C
ATOM 646 CG LEU A 106 12.202 -18.235 -55.976 1.00 17.10 C
ANISOU 646 CG LEU A 106 1791 2345 2363 15 1212 -59 C
ATOM 647 CD1 LEU A 106 11.583 -16.938 -56.468 1.00 17.39 C
ANISOU 647 CD1 LEU A 106 1782 2385 2439 -31 1221 -78 C
ATOM 648 CD2 LEU A 106 12.502 -19.162 -57.144 1.00 17.39 C
ANISOU 648 CD2 LEU A 106 1872 2305 2432 -5 1260 4 C
ATOM 649 N ILE A 107 11.040 -17.090 -52.851 1.00 17.12 N
ANISOU 649 N ILE A 107 1750 2451 2302 108 1082 -208 N
ATOM 650 CA ILE A 107 9.990 -17.519 -51.935 1.00 20.48 C
ANISOU 650 CA ILE A 107 2210 2839 2734 138 1032 -257 C
ATOM 651 C ILE A 107 8.725 -17.760 -52.748 1.00 22.17 C
ANISOU 651 C ILE A 107 2453 2961 3008 110 1038 -268 C
ATOM 652 O ILE A 107 8.156 -16.819 -53.318 1.00 18.65 O
ANISOU 652 O ILE A 107 1981 2504 2602 85 1053 -284 O
ATOM 653 CB ILE A 107 9.753 -16.487 -50.820 1.00 26.38 C
ANISOU 653 CB ILE A 107 2930 3634 3460 172 1000 -303 C
ATOM 654 CG1 ILE A 107 11.073 -16.176 -50.104 1.00 26.91 C
ANISOU 654 CG1 ILE A 107 2967 3793 3464 202 1003 -293 C
ATOM 655 CG2 ILE A 107 8.707 -16.986 -49.830 1.00 23.69 C
ANISOU 655 CG2 ILE A 107 2635 3244 3121 198 953 -346 C
ATOM 656 CD1 ILE A 107 10.944 -15.242 -48.914 1.00 33.25 C
ANISOU 656 CD1 ILE A 107 3752 4636 4244 249 976 -337 C
ATOM 657 N LEU A 108 8.294 -19.024 -52.808 1.00 19.69 N
ANISOU 657 N LEU A 108 2189 2588 2704 115 1029 -266 N
ATOM 658 CA LEU A 108 7.117 -19.424 -53.571 1.00 14.77 C
ANISOU 658 CA LEU A 108 1604 1878 2129 93 1039 -279 C
ATOM 659 C LEU A 108 5.986 -19.933 -52.686 1.00 17.14 C
ANISOU 659 C LEU A 108 1949 2144 2421 110 998 -322 C
ATOM 660 O LEU A 108 5.118 -20.665 -53.176 1.00 20.70 O
ANISOU 660 O LEU A 108 2443 2527 2896 98 1006 -331 O
ATOM 661 CB LEU A 108 7.491 -20.504 -54.591 1.00 15.23 C
ANISOU 661 CB LEU A 108 1687 1889 2212 83 1076 -239 C
ATOM 662 CG LEU A 108 8.595 -20.146 -55.587 1.00 17.08 C
ANISOU 662 CG LEU A 108 1893 2141 2457 58 1128 -184 C
ATOM 663 CD1 LEU A 108 8.958 -21.339 -56.455 1.00 17.35 C
ANISOU 663 CD1 LEU A 108 1961 2118 2515 62 1166 -144 C
ATOM 664 CD2 LEU A 108 8.164 -18.972 -56.447 1.00 18.10 C
ANISOU 664 CD2 LEU A 108 1992 2254 2629 11 1159 -186 C
ATOM 665 N THR A 109 5.960 -19.553 -51.408 1.00 20.88 N
ANISOU 665 N THR A 109 2415 2658 2859 136 961 -348 N
ATOM 666 CA THR A 109 5.005 -20.113 -50.456 1.00 18.74 C
ANISOU 666 CA THR A 109 2191 2354 2575 146 928 -380 C
ATOM 667 C THR A 109 3.565 -19.948 -50.929 1.00 13.75 C
ANISOU 667 C THR A 109 1602 1651 1972 127 934 -408 C
ATOM 668 O THR A 109 3.172 -18.883 -51.414 1.00 20.75 O
ANISOU 668 O THR A 109 2470 2530 2882 121 944 -429 O
ATOM 669 CB THR A 109 5.188 -19.439 -49.094 1.00 19.70 C
ANISOU 669 CB THR A 109 2299 2522 2664 177 896 -407 C
ATOM 670 OG1 THR A 109 6.531 -19.642 -48.640 1.00 15.74 O
ANISOU 670 OG1 THR A 109 1765 2086 2128 197 893 -386 O
ATOM 671 CG2 THR A 109 4.203 -19.993 -48.067 1.00 13.53 C
ANISOU 671 CG2 THR A 109 1571 1699 1871 180 870 -436 C
ATOM 672 N GLY A 110 2.784 -21.020 -50.796 1.00 14.05 N
ANISOU 672 N GLY A 110 1692 1641 2006 117 929 -414 N
ATOM 673 CA GLY A 110 1.357 -20.964 -51.013 1.00 13.56 C
ANISOU 673 CA GLY A 110 1685 1514 1951 102 930 -444 C
ATOM 674 C GLY A 110 0.894 -21.032 -52.453 1.00 21.27 C
ANISOU 674 C GLY A 110 2680 2439 2964 79 963 -444 C
ATOM 675 O GLY A 110 -0.319 -20.975 -52.696 1.00 18.61 O
ANISOU 675 O GLY A 110 2398 2047 2626 68 961 -475 O
ATOM 676 N ASN A 111 1.803 -21.157 -53.417 1.00 20.96 N
ANISOU 676 N ASN A 111 2604 2409 2953 72 993 -413 N
ATOM 677 CA ASN A 111 1.410 -21.217 -54.821 1.00 15.68 C
ANISOU 677 CA ASN A 111 1953 1680 2325 51 1032 -417 C
ATOM 678 C ASN A 111 1.149 -22.659 -55.230 1.00 16.18 C
ANISOU 678 C ASN A 111 2059 1700 2388 50 1042 -407 C
ATOM 679 O ASN A 111 2.043 -23.502 -55.081 1.00 18.56 O
ANISOU 679 O ASN A 111 2339 2028 2685 65 1043 -376 O
ATOM 680 CB ASN A 111 2.481 -20.619 -55.713 1.00 14.61 C
ANISOU 680 CB ASN A 111 1758 1567 2225 38 1071 -387 C
ATOM 681 CG ASN A 111 2.657 -19.133 -55.496 1.00 21.81 C
ANISOU 681 CG ASN A 111 2615 2528 3144 31 1056 -397 C
ATOM 682 OD1 ASN A 111 1.801 -18.340 -55.875 1.00 17.20 O
ANISOU 682 OD1 ASN A 111 2039 1918 2577 12 1018 -422 O
ATOM 683 ND2 ASN A 111 3.779 -18.747 -54.897 1.00 22.32 N
ANISOU 683 ND2 ASN A 111 2625 2669 3187 45 1057 -373 N
ATOM 684 N PRO A 112 -0.027 -22.981 -55.775 1.00 18.47 N
ANISOU 684 N PRO A 112 2410 1926 2683 37 1048 -437 N
ATOM 685 CA PRO A 112 -0.355 -24.377 -56.125 1.00 17.89 C
ANISOU 685 CA PRO A 112 2371 1819 2607 39 1056 -433 C
ATOM 686 C PRO A 112 0.330 -24.831 -57.412 1.00 20.22 C
ANISOU 686 C PRO A 112 2657 2076 2949 45 1096 -415 C
ATOM 687 O PRO A 112 -0.310 -25.172 -58.414 1.00 17.64 O
ANISOU 687 O PRO A 112 2376 1683 2645 39 1113 -436 O
ATOM 688 CB PRO A 112 -1.883 -24.327 -56.261 1.00 15.50 C
ANISOU 688 CB PRO A 112 2140 1466 2282 22 1045 -473 C
ATOM 689 CG PRO A 112 -2.151 -22.935 -56.760 1.00 21.31 C
ANISOU 689 CG PRO A 112 2882 2177 3038 12 1043 -500 C
ATOM 690 CD PRO A 112 -1.117 -22.051 -56.110 1.00 16.06 C
ANISOU 690 CD PRO A 112 2144 1578 2382 23 1041 -482 C
ATOM 691 N ILE A 113 1.663 -24.850 -57.388 1.00 18.40 N
ANISOU 691 N ILE A 113 2373 1885 2733 60 1109 -376 N
ATOM 692 CA ILE A 113 2.428 -25.275 -58.557 1.00 19.08 C
ANISOU 692 CA ILE A 113 2454 1930 2865 72 1154 -352 C
ATOM 693 C ILE A 113 2.302 -26.777 -58.757 1.00 22.46 C
ANISOU 693 C ILE A 113 2904 2331 3298 99 1151 -356 C
ATOM 694 O ILE A 113 2.131 -27.249 -59.888 1.00 23.74 O
ANISOU 694 O ILE A 113 3099 2420 3500 109 1179 -365 O
ATOM 695 CB ILE A 113 3.896 -24.837 -58.415 1.00 18.99 C
ANISOU 695 CB ILE A 113 2385 1976 2853 78 1163 -299 C
ATOM 696 CG1 ILE A 113 3.985 -23.312 -58.377 1.00 20.23 C
ANISOU 696 CG1 ILE A 113 2512 2168 3005 41 1144 -288 C
ATOM 697 CG2 ILE A 113 4.734 -25.410 -59.554 1.00 16.16 C
ANISOU 697 CG2 ILE A 113 2035 1576 2528 85 1168 -249 C
ATOM 698 CD1 ILE A 113 5.200 -22.791 -57.654 1.00 27.20 C
ANISOU 698 CD1 ILE A 113 3337 3136 3862 50 1154 -256 C
ATOM 699 N GLN A 114 2.397 -27.550 -57.672 1.00 16.47 N
ANISOU 699 N GLN A 114 2125 1629 2505 113 1118 -355 N
ATOM 700 CA GLN A 114 2.175 -28.992 -57.720 1.00 18.29 C
ANISOU 700 CA GLN A 114 2361 1849 2739 136 1116 -368 C
ATOM 701 C GLN A 114 3.222 -29.686 -58.584 1.00 24.52 C
ANISOU 701 C GLN A 114 3133 2611 3573 178 1143 -345 C
ATOM 702 O GLN A 114 4.114 -30.363 -58.062 1.00 22.67 O
ANISOU 702 O GLN A 114 2857 2422 3334 210 1133 -329 O
ATOM 703 CB GLN A 114 0.764 -29.296 -58.230 1.00 21.69 C
ANISOU 703 CB GLN A 114 2848 2228 3167 118 1121 -406 C
ATOM 704 CG GLN A 114 0.480 -30.769 -58.444 1.00 39.13 C
ANISOU 704 CG GLN A 114 5056 4429 5384 143 1126 -425 C
ATOM 705 CD GLN A 114 -0.437 -31.015 -59.620 1.00 50.99 C
ANISOU 705 CD GLN A 114 6613 5859 6901 141 1143 -454 C
ATOM 706 OE1 GLN A 114 0.011 -31.413 -60.690 1.00 47.04 O
ANISOU 706 OE1 GLN A 114 6119 5307 6445 171 1160 -453 O
ATOM 707 NE2 GLN A 114 -1.732 -30.786 -59.426 1.00 62.97 N
ANISOU 707 NE2 GLN A 114 8176 7370 8380 109 1137 -482 N
ATOM 708 N SER A 115 3.125 -29.523 -59.900 1.00 22.90 N
ANISOU 708 N SER A 115 2964 2325 3413 183 1177 -346 N
ATOM 709 CA SER A 115 4.066 -30.140 -60.825 1.00 24.08 C
ANISOU 709 CA SER A 115 3112 2424 3614 231 1205 -322 C
ATOM 710 C SER A 115 5.140 -29.128 -61.215 1.00 21.70 C
ANISOU 710 C SER A 115 2800 2133 3312 206 1187 -251 C
ATOM 711 O SER A 115 4.844 -28.092 -61.822 1.00 24.04 O
ANISOU 711 O SER A 115 3120 2401 3614 155 1175 -237 O
ATOM 712 CB SER A 115 3.345 -30.672 -62.063 1.00 32.45 C
ANISOU 712 CB SER A 115 4229 3385 4715 243 1213 -351 C
ATOM 713 OG SER A 115 3.063 -29.638 -62.987 1.00 66.08 O
ANISOU 713 OG SER A 115 8531 7591 8986 192 1190 -332 O
ATOM 714 N PHE A 116 6.384 -29.433 -60.854 1.00 20.77 N
ANISOU 714 N PHE A 116 2646 2062 3184 236 1180 -206 N
ATOM 715 CA PHE A 116 7.555 -28.659 -61.260 1.00 21.66 C
ANISOU 715 CA PHE A 116 2754 2189 3285 214 1165 -130 C
ATOM 716 C PHE A 116 8.212 -29.426 -62.403 1.00 17.96 C
ANISOU 716 C PHE A 116 2324 1647 2855 246 1147 -86 C
ATOM 717 O PHE A 116 8.938 -30.398 -62.172 1.00 26.75 O
ANISOU 717 O PHE A 116 3421 2775 3968 306 1135 -73 O
ATOM 718 CB PHE A 116 8.517 -28.470 -60.091 1.00 16.79 C
ANISOU 718 CB PHE A 116 2086 1673 2621 229 1166 -110 C
ATOM 719 CG PHE A 116 7.990 -27.581 -58.996 1.00 17.04 C
ANISOU 719 CG PHE A 116 2086 1770 2617 199 1178 -148 C
ATOM 720 CD1 PHE A 116 7.059 -28.048 -58.079 1.00 18.83 C
ANISOU 720 CD1 PHE A 116 2305 2013 2836 210 1182 -213 C
ATOM 721 CD2 PHE A 116 8.452 -26.280 -58.867 1.00 23.04 C
ANISOU 721 CD2 PHE A 116 2828 2577 3351 158 1179 -116 C
ATOM 722 CE1 PHE A 116 6.585 -27.227 -57.070 1.00 16.31 C
ANISOU 722 CE1 PHE A 116 1976 1748 2472 176 1141 -233 C
ATOM 723 CE2 PHE A 116 7.987 -25.458 -57.859 1.00 20.28 C
ANISOU 723 CE2 PHE A 116 2450 2283 2973 141 1183 -155 C
ATOM 724 CZ PHE A 116 7.051 -25.933 -56.960 1.00 20.16 C
ANISOU 724 CZ PHE A 116 2442 2275 2942 151 1148 -210 C
ATOM 725 N SER A 117 7.949 -28.997 -63.637 1.00 18.28 N
ANISOU 725 N SER A 117 2414 1602 2929 208 1138 -64 N
ATOM 726 CA SER A 117 8.464 -29.684 -64.812 1.00 25.93 C
ANISOU 726 CA SER A 117 3433 2480 3938 237 1116 -24 C
ATOM 727 C SER A 117 9.983 -29.517 -64.907 1.00 31.32 C
ANISOU 727 C SER A 117 4116 3188 4596 241 1100 67 C
ATOM 728 O SER A 117 10.557 -28.636 -64.264 1.00 29.66 O
ANISOU 728 O SER A 117 3870 3059 4338 204 1113 99 O
ATOM 729 CB SER A 117 7.779 -29.151 -66.070 1.00 24.29 C
ANISOU 729 CB SER A 117 3284 2174 3773 184 1108 -26 C
ATOM 730 OG SER A 117 7.999 -27.761 -66.225 1.00 35.78 O
ANISOU 730 OG SER A 117 4730 3653 5213 102 1112 15 O
ATOM 731 N PRO A 118 10.660 -30.372 -65.682 1.00 34.30 N
ANISOU 731 N PRO A 118 4536 3497 5000 289 1072 108 N
ATOM 732 CA PRO A 118 12.122 -30.270 -65.792 1.00 28.10 C
ANISOU 732 CA PRO A 118 3766 2730 4181 295 1053 201 C
ATOM 733 C PRO A 118 12.593 -28.884 -66.218 1.00 27.19 C
ANISOU 733 C PRO A 118 3668 2623 4041 201 1071 270 C
ATOM 734 O PRO A 118 11.974 -28.218 -67.053 1.00 29.12 O
ANISOU 734 O PRO A 118 3941 2803 4321 136 1079 267 O
ATOM 735 CB PRO A 118 12.466 -31.324 -66.849 1.00 29.70 C
ANISOU 735 CB PRO A 118 4032 2821 4431 357 1012 228 C
ATOM 736 CG PRO A 118 11.393 -32.344 -66.718 1.00 29.71 C
ANISOU 736 CG PRO A 118 4013 2796 4478 418 1014 131 C
ATOM 737 CD PRO A 118 10.145 -31.574 -66.367 1.00 28.71 C
ANISOU 737 CD PRO A 118 3862 2698 4349 355 1054 65 C
ATOM 738 N GLY A 119 13.712 -28.457 -65.638 1.00 22.03 N
ANISOU 738 N GLY A 119 2994 2051 3323 192 1078 328 N
ATOM 739 CA GLY A 119 14.251 -27.146 -65.930 1.00 21.61 C
ANISOU 739 CA GLY A 119 2944 2026 3239 102 1107 392 C
ATOM 740 C GLY A 119 13.435 -25.992 -65.398 1.00 24.66 C
ANISOU 740 C GLY A 119 3270 2477 3623 39 1143 339 C
ATOM 741 O GLY A 119 13.618 -24.861 -65.853 1.00 30.74 O
ANISOU 741 O GLY A 119 4036 3254 4389 -43 1168 376 O
ATOM 742 N SER A 120 12.536 -26.239 -64.439 1.00 22.37 N
ANISOU 742 N SER A 120 2932 2234 3334 75 1145 252 N
ATOM 743 CA SER A 120 11.681 -25.172 -63.927 1.00 19.71 C
ANISOU 743 CA SER A 120 2547 1949 2995 25 1167 198 C
ATOM 744 C SER A 120 12.477 -24.079 -63.228 1.00 23.18 C
ANISOU 744 C SER A 120 2934 2495 3376 -10 1196 228 C
ATOM 745 O SER A 120 12.020 -22.933 -63.180 1.00 27.17 O
ANISOU 745 O SER A 120 3403 3032 3888 -68 1215 207 O
ATOM 746 CB SER A 120 10.628 -25.743 -62.971 1.00 18.50 C
ANISOU 746 CB SER A 120 2365 1819 2845 74 1162 107 C
ATOM 747 OG SER A 120 9.635 -26.457 -63.686 1.00 23.64 O
ANISOU 747 OG SER A 120 3058 2375 3549 89 1148 66 O
ATOM 748 N PHE A 121 13.663 -24.398 -62.711 1.00 19.57 N
ANISOU 748 N PHE A 121 2475 2097 2863 25 1199 273 N
ATOM 749 CA PHE A 121 14.500 -23.436 -62.007 1.00 22.61 C
ANISOU 749 CA PHE A 121 2816 2590 3183 -1 1231 297 C
ATOM 750 C PHE A 121 15.748 -23.053 -62.792 1.00 22.76 C
ANISOU 750 C PHE A 121 2872 2607 3169 -45 1250 398 C
ATOM 751 O PHE A 121 16.714 -22.559 -62.201 1.00 24.37 O
ANISOU 751 O PHE A 121 3054 2902 3302 -49 1277 429 O
ATOM 752 CB PHE A 121 14.885 -23.991 -60.637 1.00 19.16 C
ANISOU 752 CB PHE A 121 2348 2238 2692 69 1220 262 C
ATOM 753 CG PHE A 121 13.722 -24.149 -59.709 1.00 21.95 C
ANISOU 753 CG PHE A 121 2663 2609 3068 96 1212 167 C
ATOM 754 CD1 PHE A 121 13.097 -23.037 -59.180 1.00 17.82 C
ANISOU 754 CD1 PHE A 121 2094 2134 2543 62 1231 121 C
ATOM 755 CD2 PHE A 121 13.253 -25.405 -59.366 1.00 19.68 C
ANISOU 755 CD2 PHE A 121 2385 2289 2802 156 1184 124 C
ATOM 756 CE1 PHE A 121 12.026 -23.166 -58.328 1.00 18.61 C
ANISOU 756 CE1 PHE A 121 2173 2240 2656 85 1219 40 C
ATOM 757 CE2 PHE A 121 12.178 -25.544 -58.509 1.00 18.66 C
ANISOU 757 CE2 PHE A 121 2229 2173 2687 171 1183 43 C
ATOM 758 CZ PHE A 121 11.564 -24.423 -57.989 1.00 16.72 C
ANISOU 758 CZ PHE A 121 1952 1967 2433 135 1198 5 C
ATOM 759 N SER A 122 15.747 -23.276 -64.104 1.00 23.72 N
ANISOU 759 N SER A 122 3055 2620 3336 -78 1239 450 N
ATOM 760 CA SER A 122 16.846 -22.846 -64.955 1.00 22.47 C
ANISOU 760 CA SER A 122 2944 2444 3151 -136 1261 553 C
ATOM 761 C SER A 122 17.076 -21.346 -64.823 1.00 25.34 C
ANISOU 761 C SER A 122 3248 2892 3487 -222 1321 564 C
ATOM 762 O SER A 122 16.128 -20.562 -64.722 1.00 27.72 O
ANISOU 762 O SER A 122 3491 3210 3831 -260 1333 501 O
ATOM 763 CB SER A 122 16.542 -23.206 -66.408 1.00 23.14 C
ANISOU 763 CB SER A 122 3103 2385 3306 -169 1238 592 C
ATOM 764 OG SER A 122 15.188 -22.929 -66.716 1.00 25.29 O
ANISOU 764 OG SER A 122 3350 2608 3650 -196 1231 519 O
ATOM 765 N GLY A 123 18.349 -20.950 -64.819 1.00 28.64 N
ANISOU 765 N GLY A 123 3682 3368 3832 -251 1357 642 N
ATOM 766 CA GLY A 123 18.720 -19.552 -64.763 1.00 24.15 C
ANISOU 766 CA GLY A 123 3056 2887 3234 -335 1424 659 C
ATOM 767 C GLY A 123 18.971 -18.996 -63.377 1.00 28.79 C
ANISOU 767 C GLY A 123 3566 3619 3755 -299 1453 604 C
ATOM 768 O GLY A 123 19.475 -17.869 -63.261 1.00 26.50 O
ANISOU 768 O GLY A 123 3227 3415 3427 -359 1515 619 O
ATOM 769 N LEU A 124 18.642 -19.739 -62.320 1.00 31.27 N
ANISOU 769 N LEU A 124 3866 3960 4055 -207 1412 538 N
ATOM 770 CA LEU A 124 18.826 -19.268 -60.945 1.00 28.87 C
ANISOU 770 CA LEU A 124 3496 3782 3692 -168 1432 477 C
ATOM 771 C LEU A 124 20.185 -19.737 -60.419 1.00 29.67 C
ANISOU 771 C LEU A 124 3636 3946 3691 -124 1434 528 C
ATOM 772 O LEU A 124 20.297 -20.570 -59.518 1.00 33.93 O
ANISOU 772 O LEU A 124 4182 4510 4201 -44 1393 491 O
ATOM 773 CB LEU A 124 17.678 -19.752 -60.070 1.00 24.99 C
ANISOU 773 CB LEU A 124 2971 3282 3243 -103 1387 377 C
ATOM 774 CG LEU A 124 16.305 -19.192 -60.436 1.00 24.62 C
ANISOU 774 CG LEU A 124 2887 3187 3281 -141 1381 319 C
ATOM 775 CD1 LEU A 124 15.202 -19.996 -59.769 1.00 21.09 C
ANISOU 775 CD1 LEU A 124 2440 2703 2869 -77 1333 240 C
ATOM 776 CD2 LEU A 124 16.224 -17.726 -60.037 1.00 26.29 C
ANISOU 776 CD2 LEU A 124 3016 3489 3484 -184 1425 284 C
ATOM 777 N THR A 125 21.238 -19.153 -60.998 1.00 26.94 N
ANISOU 777 N THR A 125 3319 3629 3288 -185 1484 613 N
ATOM 778 CA THR A 125 22.594 -19.666 -60.835 1.00 34.92 C
ANISOU 778 CA THR A 125 4395 4675 4197 -154 1481 685 C
ATOM 779 C THR A 125 23.266 -19.249 -59.531 1.00 32.96 C
ANISOU 779 C THR A 125 4106 4567 3852 -115 1507 643 C
ATOM 780 O THR A 125 24.364 -19.741 -59.244 1.00 30.89 O
ANISOU 780 O THR A 125 3900 4341 3497 -78 1493 691 O
ATOM 781 CB THR A 125 23.464 -19.219 -62.012 1.00 40.83 C
ANISOU 781 CB THR A 125 5206 5393 4914 -241 1528 802 C
ATOM 782 OG1 THR A 125 23.355 -17.798 -62.172 1.00 40.32 O
ANISOU 782 OG1 THR A 125 5070 5394 4856 -331 1610 791 O
ATOM 783 CG2 THR A 125 23.018 -19.919 -63.290 1.00 40.60 C
ANISOU 783 CG2 THR A 125 5247 5210 4969 -262 1485 852 C
ATOM 784 N SER A 126 22.655 -18.361 -58.745 1.00 38.59 N
ANISOU 784 N SER A 126 4727 5354 4582 -118 1537 555 N
ATOM 785 CA SER A 126 23.200 -17.966 -57.451 1.00 30.18 C
ANISOU 785 CA SER A 126 3622 4412 3433 -75 1547 496 C
ATOM 786 C SER A 126 22.252 -18.285 -56.306 1.00 27.87 C
ANISOU 786 C SER A 126 3280 4126 3183 -6 1486 381 C
ATOM 787 O SER A 126 22.464 -17.800 -55.188 1.00 30.18 O
ANISOU 787 O SER A 126 3532 4507 3429 19 1463 304 O
ATOM 788 CB SER A 126 23.533 -16.473 -57.442 1.00 32.06 C
ANISOU 788 CB SER A 126 3798 4742 3641 -147 1576 468 C
ATOM 789 OG SER A 126 24.368 -16.135 -58.533 1.00 43.48 O
ANISOU 789 OG SER A 126 5289 6180 5051 -225 1632 573 O
ATOM 790 N LEU A 127 21.220 -19.089 -56.552 1.00 29.03 N
ANISOU 790 N LEU A 127 3436 4177 3417 18 1452 363 N
ATOM 791 CA LEU A 127 20.187 -19.306 -55.550 1.00 26.92 C
ANISOU 791 CA LEU A 127 3126 3908 3195 66 1398 257 C
ATOM 792 C LEU A 127 20.767 -19.987 -54.319 1.00 25.79 C
ANISOU 792 C LEU A 127 2992 3822 2985 139 1367 220 C
ATOM 793 O LEU A 127 21.449 -21.013 -54.420 1.00 20.76 O
ANISOU 793 O LEU A 127 2407 3168 2314 177 1341 267 O
ATOM 794 CB LEU A 127 19.046 -20.142 -56.131 1.00 27.10 C
ANISOU 794 CB LEU A 127 3168 3816 3313 73 1368 248 C
ATOM 795 CG LEU A 127 17.709 -19.980 -55.399 1.00 23.51 C
ANISOU 795 CG LEU A 127 2670 3348 2916 89 1322 147 C
ATOM 796 CD1 LEU A 127 17.226 -18.539 -55.499 1.00 20.27 C
ANISOU 796 CD1 LEU A 127 2206 2972 2522 37 1318 113 C
ATOM 797 CD2 LEU A 127 16.652 -20.941 -55.929 1.00 20.09 C
ANISOU 797 CD2 LEU A 127 2263 2807 2563 101 1307 138 C
ATOM 798 N GLU A 128 20.505 -19.396 -53.155 1.00 23.00 N
ANISOU 798 N GLU A 128 2590 3530 2618 151 1324 124 N
ATOM 799 CA GLU A 128 20.946 -19.929 -51.875 1.00 24.68 C
ANISOU 799 CA GLU A 128 2807 3792 2779 210 1288 71 C
ATOM 800 C GLU A 128 19.808 -20.433 -51.005 1.00 24.90 C
ANISOU 800 C GLU A 128 2814 3780 2867 239 1223 -16 C
ATOM 801 O GLU A 128 20.026 -21.314 -50.172 1.00 25.41 O
ANISOU 801 O GLU A 128 2891 3853 2912 287 1194 -46 O
ATOM 802 CB GLU A 128 21.716 -18.862 -51.085 1.00 23.83 C
ANISOU 802 CB GLU A 128 2674 3781 2599 197 1297 26 C
ATOM 803 CG GLU A 128 23.066 -18.479 -51.668 1.00 34.05 C
ANISOU 803 CG GLU A 128 4000 5133 3803 173 1359 107 C
ATOM 804 CD GLU A 128 23.762 -17.408 -50.850 1.00 45.49 C
ANISOU 804 CD GLU A 128 5427 6667 5191 158 1377 47 C
ATOM 805 OE1 GLU A 128 23.506 -17.334 -49.628 1.00 50.23 O
ANISOU 805 OE1 GLU A 128 6012 7271 5803 192 1339 -46 O
ATOM 806 OE2 GLU A 128 24.557 -16.636 -51.427 1.00 50.97 O
ANISOU 806 OE2 GLU A 128 6126 7408 5834 109 1434 93 O
ATOM 807 N ASN A 129 18.602 -19.899 -51.181 1.00 25.94 N
ANISOU 807 N ASN A 129 2917 3872 3066 211 1198 -53 N
ATOM 808 CA ASN A 129 17.482 -20.185 -50.291 1.00 22.49 C
ANISOU 808 CA ASN A 129 2468 3407 2670 234 1133 -128 C
ATOM 809 C ASN A 129 16.236 -20.358 -51.144 1.00 25.91 C
ANISOU 809 C ASN A 129 2911 3750 3183 211 1125 -115 C
ATOM 810 O ASN A 129 15.748 -19.389 -51.733 1.00 30.03 O
ANISOU 810 O ASN A 129 3414 4264 3731 177 1138 -108 O
ATOM 811 CB ASN A 129 17.293 -19.063 -49.270 1.00 21.37 C
ANISOU 811 CB ASN A 129 2286 3332 2502 242 1101 -193 C
ATOM 812 CG ASN A 129 16.095 -19.290 -48.373 1.00 30.54 C
ANISOU 812 CG ASN A 129 3451 4456 3697 275 1037 -243 C
ATOM 813 OD1 ASN A 129 15.791 -20.425 -48.010 1.00 29.93 O
ANISOU 813 OD1 ASN A 129 3399 4335 3637 291 1012 -256 O
ATOM 814 ND2 ASN A 129 15.401 -18.213 -48.019 1.00 29.37 N
ANISOU 814 ND2 ASN A 129 3286 4315 3560 289 1018 -263 N
ATOM 815 N LEU A 130 15.723 -21.583 -51.211 1.00 21.19 N
ANISOU 815 N LEU A 130 2341 3086 2624 230 1109 -117 N
ATOM 816 CA LEU A 130 14.520 -21.891 -51.973 1.00 18.64 C
ANISOU 816 CA LEU A 130 2036 2674 2374 210 1104 -116 C
ATOM 817 C LEU A 130 13.413 -22.275 -51.002 1.00 23.44 C
ANISOU 817 C LEU A 130 2649 3259 3000 225 1043 -179 C
ATOM 818 O LEU A 130 13.533 -23.273 -50.282 1.00 19.06 O
ANISOU 818 O LEU A 130 2100 2708 2436 253 1020 -201 O
ATOM 819 CB LEU A 130 14.778 -23.016 -52.972 1.00 16.52 C
ANISOU 819 CB LEU A 130 1798 2342 2137 220 1143 -63 C
ATOM 820 CG LEU A 130 13.575 -23.479 -53.794 1.00 16.63 C
ANISOU 820 CG LEU A 130 1834 2260 2225 204 1145 -69 C
ATOM 821 CD1 LEU A 130 12.908 -22.315 -54.508 1.00 16.23 C
ANISOU 821 CD1 LEU A 130 1778 2186 2204 155 1160 -65 C
ATOM 822 CD2 LEU A 130 14.009 -24.535 -54.792 1.00 16.75 C
ANISOU 822 CD2 LEU A 130 1876 2217 2271 227 1192 -15 C
ATOM 823 N VAL A 131 12.340 -21.489 -50.984 1.00 20.14 N
ANISOU 823 N VAL A 131 2230 2815 2607 206 1023 -204 N
ATOM 824 CA VAL A 131 11.186 -21.733 -50.126 1.00 18.33 C
ANISOU 824 CA VAL A 131 2019 2553 2391 215 976 -252 C
ATOM 825 C VAL A 131 10.039 -22.196 -51.012 1.00 15.41 C
ANISOU 825 C VAL A 131 1681 2096 2077 190 984 -249 C
ATOM 826 O VAL A 131 9.405 -21.385 -51.699 1.00 17.50 O
ANISOU 826 O VAL A 131 1946 2331 2371 165 999 -248 O
ATOM 827 CB VAL A 131 10.791 -20.488 -49.322 1.00 19.58 C
ANISOU 827 CB VAL A 131 2163 2744 2532 223 951 -285 C
ATOM 828 CG1 VAL A 131 9.584 -20.789 -48.450 1.00 22.31 C
ANISOU 828 CG1 VAL A 131 2542 3044 2893 229 912 -326 C
ATOM 829 CG2 VAL A 131 11.952 -20.008 -48.471 1.00 15.06 C
ANISOU 829 CG2 VAL A 131 1562 2260 1902 253 948 -291 C
ATOM 830 N ALA A 132 9.763 -23.497 -50.994 1.00 15.48 N
ANISOU 830 N ALA A 132 1712 2067 2103 199 978 -254 N
ATOM 831 CA ALA A 132 8.667 -24.087 -51.753 1.00 14.24 C
ANISOU 831 CA ALA A 132 1588 1831 1993 181 987 -258 C
ATOM 832 C ALA A 132 7.570 -24.597 -50.824 1.00 19.98 C
ANISOU 832 C ALA A 132 2340 2535 2717 178 951 -299 C
ATOM 833 O ALA A 132 6.997 -25.667 -51.039 1.00 20.15 O
ANISOU 833 O ALA A 132 2382 2515 2761 175 954 -307 O
ATOM 834 CB ALA A 132 9.180 -25.207 -52.653 1.00 16.16 C
ANISOU 834 CB ALA A 132 1836 2042 2263 194 1020 -230 C
ATOM 835 N VAL A 133 7.266 -23.822 -49.779 1.00 22.97 N
ANISOU 835 N VAL A 133 2718 2940 3070 180 923 -324 N
ATOM 836 CA VAL A 133 6.285 -24.234 -48.784 1.00 15.60 C
ANISOU 836 CA VAL A 133 1813 1981 2131 174 899 -357 C
ATOM 837 C VAL A 133 4.885 -24.167 -49.376 1.00 13.34 C
ANISOU 837 C VAL A 133 1571 1627 1872 147 909 -369 C
ATOM 838 O VAL A 133 4.511 -23.184 -50.028 1.00 20.10 O
ANISOU 838 O VAL A 133 2431 2466 2742 138 919 -370 O
ATOM 839 CB VAL A 133 6.392 -23.354 -47.528 1.00 16.42 C
ANISOU 839 CB VAL A 133 1912 2123 2205 189 873 -381 C
ATOM 840 CG1 VAL A 133 5.229 -23.625 -46.572 1.00 14.66 C
ANISOU 840 CG1 VAL A 133 1731 1858 1982 175 859 -414 C
ATOM 841 CG2 VAL A 133 7.722 -23.583 -46.839 1.00 13.57 C
ANISOU 841 CG2 VAL A 133 1516 1828 1811 217 865 -377 C
ATOM 842 N GLU A 134 4.106 -25.221 -49.146 1.00 13.44 N
ANISOU 842 N GLU A 134 1612 1604 1892 133 911 -382 N
ATOM 843 CA GLU A 134 2.710 -25.306 -49.576 1.00 16.86 C
ANISOU 843 CA GLU A 134 2093 1974 2337 107 923 -397 C
ATOM 844 C GLU A 134 2.571 -25.033 -51.073 1.00 19.38 C
ANISOU 844 C GLU A 134 2420 2258 2687 100 949 -384 C
ATOM 845 O GLU A 134 1.827 -24.157 -51.515 1.00 19.93 O
ANISOU 845 O GLU A 134 2513 2296 2763 88 955 -398 O
ATOM 846 CB GLU A 134 1.824 -24.364 -48.756 1.00 17.06 C
ANISOU 846 CB GLU A 134 2152 1984 2344 100 908 -424 C
ATOM 847 CG GLU A 134 0.347 -24.737 -48.805 1.00 23.77 C
ANISOU 847 CG GLU A 134 3065 2774 3190 72 920 -443 C
ATOM 848 CD GLU A 134 -0.532 -23.748 -48.065 1.00 35.54 C
ANISOU 848 CD GLU A 134 4600 4244 4660 72 905 -470 C
ATOM 849 OE1 GLU A 134 0.013 -22.772 -47.512 1.00 37.40 O
ANISOU 849 OE1 GLU A 134 4810 4511 4890 97 883 -479 O
ATOM 850 OE2 GLU A 134 -1.767 -23.952 -48.037 1.00 38.72 O
ANISOU 850 OE2 GLU A 134 5067 4597 5049 50 915 -485 O
ATOM 851 N THR A 135 3.314 -25.810 -51.858 1.00 21.09 N
ANISOU 851 N THR A 135 2615 2475 2923 111 967 -362 N
ATOM 852 CA THR A 135 3.200 -25.791 -53.309 1.00 14.03 C
ANISOU 852 CA THR A 135 1733 1533 2065 105 1001 -352 C
ATOM 853 C THR A 135 2.663 -27.108 -53.854 1.00 19.44 C
ANISOU 853 C THR A 135 2443 2176 2769 106 1018 -361 C
ATOM 854 O THR A 135 2.807 -27.386 -55.049 1.00 20.41 O
ANISOU 854 O THR A 135 2572 2256 2925 113 1048 -352 O
ATOM 855 CB THR A 135 4.548 -25.455 -53.949 1.00 15.13 C
ANISOU 855 CB THR A 135 1833 1697 2219 120 1022 -316 C
ATOM 856 OG1 THR A 135 5.522 -26.417 -53.531 1.00 16.20 O
ANISOU 856 OG1 THR A 135 1941 1871 2343 148 1015 -301 O
ATOM 857 CG2 THR A 135 5.006 -24.060 -53.536 1.00 13.96 C
ANISOU 857 CG2 THR A 135 1656 1596 2051 116 1012 -310 C
ATOM 858 N LYS A 136 2.041 -27.920 -52.993 1.00 20.32 N
ANISOU 858 N LYS A 136 2566 2295 2861 100 1004 -380 N
ATOM 859 CA LYS A 136 1.479 -29.213 -53.384 1.00 14.86 C
ANISOU 859 CA LYS A 136 1887 1575 2183 101 1022 -395 C
ATOM 860 C LYS A 136 2.545 -30.127 -53.981 1.00 15.79 C
ANISOU 860 C LYS A 136 1965 1703 2330 137 1034 -380 C
ATOM 861 O LYS A 136 2.252 -30.988 -54.810 1.00 24.67 O
ANISOU 861 O LYS A 136 3100 2793 3481 150 1056 -391 O
ATOM 862 CB LYS A 136 0.297 -29.029 -54.343 1.00 17.91 C
ANISOU 862 CB LYS A 136 2329 1899 2577 82 1043 -412 C
ATOM 863 CG LYS A 136 -0.832 -28.202 -53.721 1.00 21.69 C
ANISOU 863 CG LYS A 136 2853 2366 3022 52 1032 -431 C
ATOM 864 CD LYS A 136 -1.991 -27.975 -54.678 1.00 24.00 C
ANISOU 864 CD LYS A 136 3206 2599 3314 36 1049 -452 C
ATOM 865 CE LYS A 136 -3.098 -27.180 -54.001 1.00 37.25 C
ANISOU 865 CE LYS A 136 4936 4266 4952 13 1034 -471 C
ATOM 866 NZ LYS A 136 -4.234 -26.891 -54.917 1.00 47.37 N
ANISOU 866 NZ LYS A 136 6284 5493 6223 0 1042 -496 N
ATOM 867 N LEU A 137 3.790 -29.920 -53.556 1.00 14.37 N
ANISOU 867 N LEU A 137 1744 1572 2145 159 1021 -359 N
ATOM 868 CA LEU A 137 4.898 -30.763 -53.982 1.00 23.35 C
ANISOU 868 CA LEU A 137 2844 2722 3306 200 1032 -344 C
ATOM 869 C LEU A 137 4.743 -32.157 -53.393 1.00 24.45 C
ANISOU 869 C LEU A 137 2957 2884 3448 215 1025 -371 C
ATOM 870 O LEU A 137 4.481 -32.309 -52.197 1.00 22.93 O
ANISOU 870 O LEU A 137 2754 2729 3230 197 1006 -388 O
ATOM 871 CB LEU A 137 6.224 -30.140 -53.549 1.00 14.67 C
ANISOU 871 CB LEU A 137 1710 1675 2187 217 1023 -316 C
ATOM 872 CG LEU A 137 7.512 -30.912 -53.830 1.00 17.83 C
ANISOU 872 CG LEU A 137 2074 2097 2605 266 1036 -297 C
ATOM 873 CD1 LEU A 137 7.725 -31.086 -55.324 1.00 15.52 C
ANISOU 873 CD1 LEU A 137 1800 1737 2361 290 1078 -272 C
ATOM 874 CD2 LEU A 137 8.705 -30.212 -53.179 1.00 15.05 C
ANISOU 874 CD2 LEU A 137 1694 1808 2216 277 1027 -273 C
ATOM 875 N ALA A 138 4.912 -33.177 -54.233 1.00 27.17 N
ANISOU 875 N ALA A 138 3289 3204 3831 249 1045 -378 N
ATOM 876 CA ALA A 138 4.633 -34.550 -53.844 1.00 15.77 C
ANISOU 876 CA ALA A 138 1814 1780 2398 264 1045 -411 C
ATOM 877 C ALA A 138 5.877 -35.363 -53.519 1.00 21.66 C
ANISOU 877 C ALA A 138 2496 2573 3160 315 1035 -411 C
ATOM 878 O ALA A 138 5.774 -36.337 -52.763 1.00 25.90 O
ANISOU 878 O ALA A 138 2993 3147 3700 320 1030 -441 O
ATOM 879 CB ALA A 138 3.845 -35.263 -54.951 1.00 16.20 C
ANISOU 879 CB ALA A 138 1892 1780 2485 276 1071 -432 C
ATOM 880 N SER A 139 7.040 -35.006 -54.063 1.00 21.88 N
ANISOU 880 N SER A 139 2514 2597 3203 354 1038 -378 N
ATOM 881 CA SER A 139 8.257 -35.746 -53.764 1.00 29.98 C
ANISOU 881 CA SER A 139 3481 3664 4244 411 1029 -378 C
ATOM 882 C SER A 139 9.473 -34.936 -54.188 1.00 26.03 C
ANISOU 882 C SER A 139 2989 3162 3741 439 1041 -328 C
ATOM 883 O SER A 139 9.398 -34.093 -55.089 1.00 24.33 O
ANISOU 883 O SER A 139 2819 2894 3532 427 1067 -293 O
ATOM 884 CB SER A 139 8.274 -37.114 -54.457 1.00 34.65 C
ANISOU 884 CB SER A 139 4043 4232 4890 468 1035 -403 C
ATOM 885 OG SER A 139 8.646 -36.998 -55.818 1.00 33.29 O
ANISOU 885 OG SER A 139 3900 3988 4759 512 1056 -373 O
ATOM 886 N LEU A 140 10.601 -35.216 -53.529 1.00 26.71 N
ANISOU 886 N LEU A 140 3029 3304 3818 478 1028 -324 N
ATOM 887 CA LEU A 140 11.851 -34.532 -53.844 1.00 21.06 C
ANISOU 887 CA LEU A 140 2320 2593 3090 513 1050 -268 C
ATOM 888 C LEU A 140 12.539 -35.132 -55.061 1.00 28.70 C
ANISOU 888 C LEU A 140 3301 3505 4098 580 1044 -223 C
ATOM 889 O LEU A 140 13.242 -34.418 -55.784 1.00 30.17 O
ANISOU 889 O LEU A 140 3537 3672 4256 574 1028 -151 O
ATOM 890 CB LEU A 140 12.790 -34.580 -52.639 1.00 19.27 C
ANISOU 890 CB LEU A 140 2048 2450 2824 531 1028 -278 C
ATOM 891 CG LEU A 140 12.404 -33.738 -51.428 1.00 27.29 C
ANISOU 891 CG LEU A 140 3068 3519 3779 465 1004 -303 C
ATOM 892 CD1 LEU A 140 13.484 -33.808 -50.361 1.00 21.32 C
ANISOU 892 CD1 LEU A 140 2272 2839 2989 493 990 -315 C
ATOM 893 CD2 LEU A 140 12.159 -32.303 -51.843 1.00 27.19 C
ANISOU 893 CD2 LEU A 140 3107 3488 3736 420 1020 -267 C
ATOM 894 N GLU A 141 12.365 -36.437 -55.286 1.00 34.71 N
ANISOU 894 N GLU A 141 4027 4246 4917 634 1033 -261 N
ATOM 895 CA GLU A 141 12.979 -37.099 -56.433 1.00 38.72 C
ANISOU 895 CA GLU A 141 4557 4696 5458 698 993 -219 C
ATOM 896 C GLU A 141 12.640 -36.390 -57.740 1.00 34.98 C
ANISOU 896 C GLU A 141 4164 4134 4994 672 1010 -171 C
ATOM 897 O GLU A 141 13.499 -36.245 -58.619 1.00 33.63 O
ANISOU 897 O GLU A 141 4043 3920 4815 695 973 -99 O
ATOM 898 CB GLU A 141 12.535 -38.561 -56.485 1.00 48.55 C
ANISOU 898 CB GLU A 141 5743 5928 6775 758 992 -287 C
ATOM 899 CG GLU A 141 13.013 -39.416 -55.316 1.00 66.68 C
ANISOU 899 CG GLU A 141 7950 8310 9075 790 964 -334 C
ATOM 900 CD GLU A 141 14.422 -39.944 -55.516 1.00 79.61 C
ANISOU 900 CD GLU A 141 9579 9965 10705 866 879 -287 C
ATOM 901 OE1 GLU A 141 15.068 -39.561 -56.513 1.00 86.66 O
ANISOU 901 OE1 GLU A 141 10544 10803 11580 888 847 -210 O
ATOM 902 OE2 GLU A 141 14.885 -40.748 -54.682 1.00 82.21 O
ANISOU 902 OE2 GLU A 141 9831 10360 11045 902 842 -327 O
ATOM 903 N SER A 142 11.399 -35.936 -57.884 1.00 36.09 N
ANISOU 903 N SER A 142 4323 4241 5149 620 1062 -209 N
ATOM 904 CA SER A 142 10.948 -35.266 -59.096 1.00 39.79 C
ANISOU 904 CA SER A 142 4864 4624 5632 588 1076 -176 C
ATOM 905 C SER A 142 11.148 -33.756 -59.056 1.00 37.57 C
ANISOU 905 C SER A 142 4617 4361 5298 516 1086 -125 C
ATOM 906 O SER A 142 10.778 -33.068 -60.014 1.00 34.06 O
ANISOU 906 O SER A 142 4226 3851 4866 477 1096 -98 O
ATOM 907 CB SER A 142 9.471 -35.580 -59.346 1.00 41.32 C
ANISOU 907 CB SER A 142 5064 4770 5864 572 1121 -248 C
ATOM 908 OG SER A 142 8.971 -34.819 -60.428 1.00 57.83 O
ANISOU 908 OG SER A 142 7225 6783 7965 532 1130 -224 O
ATOM 909 N PHE A 143 11.738 -33.229 -57.985 1.00 26.66 N
ANISOU 909 N PHE A 143 3203 3067 3862 499 1082 -116 N
ATOM 910 CA PHE A 143 11.901 -31.793 -57.813 1.00 23.45 C
ANISOU 910 CA PHE A 143 2813 2690 3407 437 1097 -81 C
ATOM 911 C PHE A 143 13.173 -31.342 -58.527 1.00 25.64 C
ANISOU 911 C PHE A 143 3126 2962 3654 437 1074 10 C
ATOM 912 O PHE A 143 14.275 -31.721 -58.100 1.00 27.34 O
ANISOU 912 O PHE A 143 3328 3226 3833 476 1043 39 O
ATOM 913 CB PHE A 143 11.966 -31.456 -56.331 1.00 22.45 C
ANISOU 913 CB PHE A 143 2639 2657 3235 424 1105 -119 C
ATOM 914 CG PHE A 143 11.560 -30.051 -56.001 1.00 20.07 C
ANISOU 914 CG PHE A 143 2344 2380 2901 364 1130 -121 C
ATOM 915 CD1 PHE A 143 10.530 -29.431 -56.689 1.00 23.73 C
ANISOU 915 CD1 PHE A 143 2838 2786 3392 321 1152 -131 C
ATOM 916 CD2 PHE A 143 12.194 -29.361 -54.980 1.00 18.95 C
ANISOU 916 CD2 PHE A 143 2176 2321 2703 355 1128 -119 C
ATOM 917 CE1 PHE A 143 10.150 -28.138 -56.373 1.00 24.15 C
ANISOU 917 CE1 PHE A 143 2890 2865 3421 271 1164 -137 C
ATOM 918 CE2 PHE A 143 11.820 -28.066 -54.659 1.00 16.74 C
ANISOU 918 CE2 PHE A 143 1899 2067 2394 303 1128 -126 C
ATOM 919 CZ PHE A 143 10.796 -27.455 -55.357 1.00 19.63 C
ANISOU 919 CZ PHE A 143 2290 2377 2790 262 1138 -134 C
ATOM 920 N PRO A 144 13.082 -30.536 -59.594 1.00 27.49 N
ANISOU 920 N PRO A 144 3409 3137 3898 390 1086 57 N
ATOM 921 CA PRO A 144 14.272 -30.222 -60.425 1.00 25.56 C
ANISOU 921 CA PRO A 144 3210 2871 3629 383 1067 151 C
ATOM 922 C PRO A 144 15.186 -29.167 -59.810 1.00 25.47 C
ANISOU 922 C PRO A 144 3185 2949 3542 347 1082 194 C
ATOM 923 O PRO A 144 15.329 -28.032 -60.284 1.00 29.30 O
ANISOU 923 O PRO A 144 3688 3435 4011 282 1110 236 O
ATOM 924 CB PRO A 144 13.633 -29.760 -61.740 1.00 25.34 C
ANISOU 924 CB PRO A 144 3234 2744 3650 335 1080 172 C
ATOM 925 CG PRO A 144 12.348 -29.107 -61.301 1.00 22.67 C
ANISOU 925 CG PRO A 144 2866 2421 3326 290 1113 101 C
ATOM 926 CD PRO A 144 11.857 -29.903 -60.114 1.00 25.79 C
ANISOU 926 CD PRO A 144 3212 2869 3718 337 1114 26 C
ATOM 927 N ILE A 145 15.853 -29.541 -58.721 1.00 21.81 N
ANISOU 927 N ILE A 145 2687 2570 3031 388 1065 179 N
ATOM 928 CA ILE A 145 16.801 -28.663 -58.049 1.00 20.38 C
ANISOU 928 CA ILE A 145 2495 2481 2770 367 1077 210 C
ATOM 929 C ILE A 145 18.216 -29.224 -58.097 1.00 19.97 C
ANISOU 929 C ILE A 145 2473 2453 2664 413 1037 274 C
ATOM 930 O ILE A 145 19.111 -28.696 -57.429 1.00 25.29 O
ANISOU 930 O ILE A 145 3140 3211 3258 409 1042 294 O
ATOM 931 CB ILE A 145 16.374 -28.385 -56.597 1.00 22.18 C
ANISOU 931 CB ILE A 145 2662 2793 2974 368 1090 131 C
ATOM 932 CG1 ILE A 145 16.280 -29.693 -55.811 1.00 19.99 C
ANISOU 932 CG1 ILE A 145 2352 2529 2714 431 1053 76 C
ATOM 933 CG2 ILE A 145 15.043 -27.653 -56.564 1.00 22.49 C
ANISOU 933 CG2 ILE A 145 2684 2809 3053 319 1125 79 C
ATOM 934 CD1 ILE A 145 16.059 -29.519 -54.319 1.00 20.43 C
ANISOU 934 CD1 ILE A 145 2357 2664 2741 432 1058 6 C
ATOM 935 N GLY A 146 18.444 -30.280 -58.879 1.00 28.63 N
ANISOU 935 N GLY A 146 3606 3475 3798 463 994 304 N
ATOM 936 CA GLY A 146 19.723 -30.963 -58.944 1.00 28.35 C
ANISOU 936 CA GLY A 146 3604 3452 3715 520 940 362 C
ATOM 937 C GLY A 146 20.877 -30.156 -59.499 1.00 31.68 C
ANISOU 937 C GLY A 146 4093 3885 4061 482 950 466 C
ATOM 938 O GLY A 146 22.021 -30.616 -59.416 1.00 27.49 O
ANISOU 938 O GLY A 146 3598 3378 3470 528 904 517 O
ATOM 939 N GLN A 147 20.622 -28.975 -60.063 1.00 27.54 N
ANISOU 939 N GLN A 147 3586 3346 3534 398 1009 498 N
ATOM 940 CA GLN A 147 21.679 -28.137 -60.616 1.00 26.82 C
ANISOU 940 CA GLN A 147 3554 3268 3370 346 1034 597 C
ATOM 941 C GLN A 147 21.781 -26.787 -59.916 1.00 32.82 C
ANISOU 941 C GLN A 147 4268 4131 4069 282 1100 581 C
ATOM 942 O GLN A 147 22.576 -25.937 -60.338 1.00 36.95 O
ANISOU 942 O GLN A 147 4828 4679 4531 225 1139 655 O
ATOM 943 CB GLN A 147 21.469 -27.942 -62.119 1.00 30.87 C
ANISOU 943 CB GLN A 147 4132 3661 3936 296 1045 664 C
ATOM 944 CG GLN A 147 21.553 -29.236 -62.926 1.00 44.89 C
ANISOU 944 CG GLN A 147 5967 5326 5764 366 976 690 C
ATOM 945 CD GLN A 147 20.788 -29.166 -64.234 1.00 60.65 C
ANISOU 945 CD GLN A 147 8007 7192 7847 325 985 706 C
ATOM 946 OE1 GLN A 147 19.683 -28.626 -64.290 1.00 69.77 O
ANISOU 946 OE1 GLN A 147 9118 8336 9056 276 1025 647 O
ATOM 947 NE2 GLN A 147 21.372 -29.712 -65.294 1.00 66.24 N
ANISOU 947 NE2 GLN A 147 8805 7795 8567 346 942 785 N
ATOM 948 N LEU A 148 20.995 -26.564 -58.860 1.00 26.49 N
ANISOU 948 N LEU A 148 3390 3390 3284 289 1115 484 N
ATOM 949 CA LEU A 148 21.150 -25.387 -58.005 1.00 28.07 C
ANISOU 949 CA LEU A 148 3543 3696 3426 251 1166 455 C
ATOM 950 C LEU A 148 22.298 -25.654 -57.028 1.00 29.79 C
ANISOU 950 C LEU A 148 3765 4008 3544 300 1142 459 C
ATOM 951 O LEU A 148 22.123 -25.799 -55.816 1.00 34.13 O
ANISOU 951 O LEU A 148 4265 4623 4078 337 1127 382 O
ATOM 952 CB LEU A 148 19.842 -25.074 -57.289 1.00 28.68 C
ANISOU 952 CB LEU A 148 3550 3785 3560 244 1181 354 C
ATOM 953 CG LEU A 148 18.619 -24.833 -58.174 1.00 24.49 C
ANISOU 953 CG LEU A 148 3018 3166 3122 199 1197 339 C
ATOM 954 CD1 LEU A 148 17.373 -24.739 -57.316 1.00 21.51 C
ANISOU 954 CD1 LEU A 148 2585 2802 2788 208 1198 238 C
ATOM 955 CD2 LEU A 148 18.801 -23.570 -59.003 1.00 25.09 C
ANISOU 955 CD2 LEU A 148 3101 3241 3192 116 1249 392 C
ATOM 956 N ILE A 149 23.507 -25.725 -57.593 1.00 28.35 N
ANISOU 956 N ILE A 149 3651 3827 3292 299 1134 553 N
ATOM 957 CA ILE A 149 24.692 -26.124 -56.845 1.00 26.52 C
ANISOU 957 CA ILE A 149 3444 3673 2959 352 1097 569 C
ATOM 958 C ILE A 149 25.057 -25.139 -55.743 1.00 28.38 C
ANISOU 958 C ILE A 149 3637 4033 3113 335 1143 524 C
ATOM 959 O ILE A 149 25.874 -25.463 -54.875 1.00 28.40 O
ANISOU 959 O ILE A 149 3647 4109 3035 384 1109 508 O
ATOM 960 CB ILE A 149 25.883 -26.318 -57.809 1.00 27.32 C
ANISOU 960 CB ILE A 149 3645 3740 2995 348 1081 691 C
ATOM 961 CG1 ILE A 149 26.387 -24.966 -58.315 1.00 40.85 C
ANISOU 961 CG1 ILE A 149 5384 5491 4647 256 1168 757 C
ATOM 962 CG2 ILE A 149 25.473 -27.203 -58.974 1.00 24.99 C
ANISOU 962 CG2 ILE A 149 3397 3310 2790 365 1036 733 C
ATOM 963 CD1 ILE A 149 27.413 -25.061 -59.420 1.00 44.97 C
ANISOU 963 CD1 ILE A 149 6015 5960 5112 231 1164 888 C
ATOM 964 N THR A 150 24.468 -23.946 -55.755 1.00 24.84 N
ANISOU 964 N THR A 150 3143 3610 2686 272 1215 497 N
ATOM 965 CA THR A 150 24.698 -22.948 -54.721 1.00 24.00 C
ANISOU 965 CA THR A 150 2988 3617 2514 262 1261 442 C
ATOM 966 C THR A 150 23.718 -23.056 -53.558 1.00 28.70 C
ANISOU 966 C THR A 150 3512 4231 3161 297 1240 324 C
ATOM 967 O THR A 150 23.912 -22.377 -52.544 1.00 32.41 O
ANISOU 967 O THR A 150 3946 4790 3578 305 1263 266 O
ATOM 968 CB THR A 150 24.608 -21.541 -55.325 1.00 26.27 C
ANISOU 968 CB THR A 150 3254 3927 2801 178 1349 470 C
ATOM 969 OG1 THR A 150 23.343 -21.389 -55.986 1.00 27.45 O
ANISOU 969 OG1 THR A 150 3371 3992 3067 141 1356 449 O
ATOM 970 CG2 THR A 150 25.735 -21.307 -56.332 1.00 24.45 C
ANISOU 970 CG2 THR A 150 3098 3694 2499 131 1383 589 C
ATOM 971 N LEU A 151 22.690 -23.897 -53.673 1.00 27.38 N
ANISOU 971 N LEU A 151 3330 3983 3090 317 1199 288 N
ATOM 972 CA LEU A 151 21.615 -23.923 -52.688 1.00 27.91 C
ANISOU 972 CA LEU A 151 3339 4055 3212 334 1188 185 C
ATOM 973 C LEU A 151 22.141 -24.318 -51.315 1.00 26.45 C
ANISOU 973 C LEU A 151 3138 3944 2967 388 1150 125 C
ATOM 974 O LEU A 151 22.827 -25.334 -51.159 1.00 24.55 O
ANISOU 974 O LEU A 151 2924 3707 2697 433 1096 142 O
ATOM 975 CB LEU A 151 20.515 -24.889 -53.131 1.00 23.30 C
ANISOU 975 CB LEU A 151 2752 3370 2730 345 1154 164 C
ATOM 976 CG LEU A 151 19.185 -24.832 -52.376 1.00 21.42 C
ANISOU 976 CG LEU A 151 2466 3117 2555 344 1155 71 C
ATOM 977 CD1 LEU A 151 18.472 -23.516 -52.642 1.00 23.41 C
ANISOU 977 CD1 LEU A 151 2694 3368 2831 290 1205 58 C
ATOM 978 CD2 LEU A 151 18.299 -26.023 -52.745 1.00 18.06 C
ANISOU 978 CD2 LEU A 151 2044 2604 2213 364 1122 53 C
ATOM 979 N LYS A 152 21.821 -23.497 -50.318 1.00 22.50 N
ANISOU 979 N LYS A 152 2596 3500 2451 384 1174 52 N
ATOM 980 CA LYS A 152 22.183 -23.738 -48.929 1.00 24.38 C
ANISOU 980 CA LYS A 152 2819 3804 2641 428 1140 -18 C
ATOM 981 C LYS A 152 21.007 -24.208 -48.088 1.00 28.44 C
ANISOU 981 C LYS A 152 3297 4278 3231 440 1111 -105 C
ATOM 982 O LYS A 152 21.174 -25.081 -47.232 1.00 31.14 O
ANISOU 982 O LYS A 152 3634 4633 3567 476 1061 -149 O
ATOM 983 CB LYS A 152 22.771 -22.468 -48.309 1.00 23.92 C
ANISOU 983 CB LYS A 152 2749 3830 2508 413 1175 -47 C
ATOM 984 CG LYS A 152 24.005 -21.933 -49.014 1.00 28.60 C
ANISOU 984 CG LYS A 152 3378 4487 3003 402 1228 39 C
ATOM 985 CD LYS A 152 24.584 -20.742 -48.263 1.00 32.84 C
ANISOU 985 CD LYS A 152 3904 5089 3485 375 1237 -14 C
ATOM 986 CE LYS A 152 25.838 -20.207 -48.935 1.00 41.56 C
ANISOU 986 CE LYS A 152 5047 6259 4485 353 1293 69 C
ATOM 987 NZ LYS A 152 26.408 -19.063 -48.173 1.00 46.57 N
ANISOU 987 NZ LYS A 152 5671 6953 5072 331 1310 9 N
ATOM 988 N LYS A 153 19.821 -23.648 -48.314 1.00 21.77 N
ANISOU 988 N LYS A 153 2434 3374 2463 388 1109 -137 N
ATOM 989 CA LYS A 153 18.634 -23.968 -47.533 1.00 20.69 C
ANISOU 989 CA LYS A 153 2276 3193 2391 376 1059 -217 C
ATOM 990 C LYS A 153 17.499 -24.370 -48.462 1.00 22.42 C
ANISOU 990 C LYS A 153 2500 3331 2688 356 1056 -195 C
ATOM 991 O LYS A 153 17.266 -23.719 -49.484 1.00 21.60 O
ANISOU 991 O LYS A 153 2404 3201 2603 324 1084 -151 O
ATOM 992 CB LYS A 153 18.192 -22.779 -46.672 1.00 20.06 C
ANISOU 992 CB LYS A 153 2174 3141 2306 346 1034 -286 C
ATOM 993 CG LYS A 153 19.187 -22.377 -45.601 1.00 35.04 C
ANISOU 993 CG LYS A 153 4088 5073 4154 359 1050 -321 C
ATOM 994 CD LYS A 153 18.625 -21.257 -44.746 1.00 41.82 C
ANISOU 994 CD LYS A 153 4963 5880 5048 345 1044 -358 C
ATOM 995 CE LYS A 153 19.488 -20.988 -43.526 1.00 52.54 C
ANISOU 995 CE LYS A 153 6338 7281 6342 391 1043 -384 C
ATOM 996 NZ LYS A 153 18.792 -20.078 -42.575 1.00 58.44 N
ANISOU 996 NZ LYS A 153 7101 7990 7114 411 1026 -411 N
ATOM 997 N LEU A 154 16.794 -25.443 -48.098 1.00 19.31 N
ANISOU 997 N LEU A 154 2102 2895 2341 369 1024 -229 N
ATOM 998 CA LEU A 154 15.628 -25.916 -48.836 1.00 16.05 C
ANISOU 998 CA LEU A 154 1700 2401 1999 350 1017 -221 C
ATOM 999 C LEU A 154 14.480 -26.093 -47.857 1.00 22.61 C
ANISOU 999 C LEU A 154 2528 3214 2850 338 964 -280 C
ATOM 1000 O LEU A 154 14.571 -26.907 -46.933 1.00 23.07 O
ANISOU 1000 O LEU A 154 2573 3288 2904 359 942 -316 O
ATOM 1001 CB LEU A 154 15.917 -27.234 -49.560 1.00 16.35 C
ANISOU 1001 CB LEU A 154 1742 2398 2072 385 1043 -189 C
ATOM 1002 CG LEU A 154 14.710 -27.830 -50.294 1.00 20.94 C
ANISOU 1002 CG LEU A 154 2335 2896 2727 367 1037 -194 C
ATOM 1003 CD1 LEU A 154 14.263 -26.912 -51.422 1.00 17.94 C
ANISOU 1003 CD1 LEU A 154 1980 2471 2366 330 1066 -154 C
ATOM 1004 CD2 LEU A 154 15.001 -29.230 -50.813 1.00 24.89 C
ANISOU 1004 CD2 LEU A 154 2826 3362 3268 417 1054 -179 C
ATOM 1005 N ASN A 155 13.405 -25.333 -48.057 1.00 15.10 N
ANISOU 1005 N ASN A 155 1593 2225 1919 307 950 -282 N
ATOM 1006 CA ASN A 155 12.201 -25.425 -47.237 1.00 16.44 C
ANISOU 1006 CA ASN A 155 1780 2361 2107 296 912 -319 C
ATOM 1007 C ASN A 155 11.082 -25.975 -48.113 1.00 19.73 C
ANISOU 1007 C ASN A 155 2219 2700 2577 270 918 -310 C
ATOM 1008 O ASN A 155 10.642 -25.312 -49.058 1.00 15.14 O
ANISOU 1008 O ASN A 155 1652 2086 2015 249 935 -290 O
ATOM 1009 CB ASN A 155 11.828 -24.061 -46.654 1.00 15.59 C
ANISOU 1009 CB ASN A 155 1678 2269 1977 291 894 -335 C
ATOM 1010 CG ASN A 155 10.791 -24.157 -45.546 1.00 17.51 C
ANISOU 1010 CG ASN A 155 1947 2477 2229 286 863 -372 C
ATOM 1011 OD1 ASN A 155 10.179 -25.207 -45.347 1.00 21.12 O
ANISOU 1011 OD1 ASN A 155 2417 2893 2712 273 858 -384 O
ATOM 1012 ND2 ASN A 155 10.582 -23.058 -44.827 1.00 20.50 N
ANISOU 1012 ND2 ASN A 155 2332 2867 2589 296 848 -393 N
ATOM 1013 N VAL A 156 10.637 -27.191 -47.804 1.00 15.79 N
ANISOU 1013 N VAL A 156 1723 2175 2101 272 909 -330 N
ATOM 1014 CA VAL A 156 9.517 -27.813 -48.501 1.00 14.70 C
ANISOU 1014 CA VAL A 156 1609 1970 2007 250 916 -330 C
ATOM 1015 C VAL A 156 8.489 -28.251 -47.469 1.00 21.43 C
ANISOU 1015 C VAL A 156 2478 2802 2863 230 896 -365 C
ATOM 1016 O VAL A 156 7.852 -29.301 -47.608 1.00 15.13 O
ANISOU 1016 O VAL A 156 1684 1971 2092 219 904 -377 O
ATOM 1017 CB VAL A 156 9.983 -28.990 -49.373 1.00 18.81 C
ANISOU 1017 CB VAL A 156 2112 2474 2560 273 941 -316 C
ATOM 1018 CG1 VAL A 156 10.778 -28.469 -50.564 1.00 14.82 C
ANISOU 1018 CG1 VAL A 156 1608 1962 2060 284 976 -271 C
ATOM 1019 CG2 VAL A 156 10.809 -29.960 -48.544 1.00 17.90 C
ANISOU 1019 CG2 VAL A 156 1959 2408 2436 305 932 -336 C
ATOM 1020 N ALA A 157 8.316 -27.442 -46.429 1.00 21.37 N
ANISOU 1020 N ALA A 157 2481 2809 2828 224 877 -384 N
ATOM 1021 CA ALA A 157 7.308 -27.735 -45.427 1.00 18.14 C
ANISOU 1021 CA ALA A 157 2098 2370 2425 198 869 -415 C
ATOM 1022 C ALA A 157 5.906 -27.565 -46.011 1.00 15.53 C
ANISOU 1022 C ALA A 157 1809 1975 2115 166 879 -415 C
ATOM 1023 O ALA A 157 5.698 -26.847 -46.993 1.00 18.82 O
ANISOU 1023 O ALA A 157 2237 2374 2538 164 884 -396 O
ATOM 1024 CB ALA A 157 7.485 -26.833 -44.208 1.00 13.64 C
ANISOU 1024 CB ALA A 157 1536 1822 1826 205 850 -438 C
ATOM 1025 N HIS A 158 4.943 -28.258 -45.399 1.00 18.03 N
ANISOU 1025 N HIS A 158 2151 2257 2443 136 888 -438 N
ATOM 1026 CA HIS A 158 3.517 -28.092 -45.700 1.00 17.64 C
ANISOU 1026 CA HIS A 158 2152 2148 2401 103 902 -444 C
ATOM 1027 C HIS A 158 3.187 -28.506 -47.136 1.00 14.81 C
ANISOU 1027 C HIS A 158 1799 1762 2066 102 920 -426 C
ATOM 1028 O HIS A 158 2.469 -27.813 -47.858 1.00 19.50 O
ANISOU 1028 O HIS A 158 2427 2321 2663 92 926 -422 O
ATOM 1029 CB HIS A 158 3.067 -26.652 -45.422 1.00 15.16 C
ANISOU 1029 CB HIS A 158 1870 1820 2070 104 887 -451 C
ATOM 1030 CG HIS A 158 1.587 -26.492 -45.258 1.00 15.91 C
ANISOU 1030 CG HIS A 158 2027 1855 2163 72 901 -468 C
ATOM 1031 ND1 HIS A 158 1.025 -25.444 -44.561 1.00 18.10 N
ANISOU 1031 ND1 HIS A 158 2343 2113 2423 73 888 -488 N
ATOM 1032 CD2 HIS A 158 0.553 -27.244 -45.703 1.00 19.93 C
ANISOU 1032 CD2 HIS A 158 2571 2321 2680 41 928 -470 C
ATOM 1033 CE1 HIS A 158 -0.290 -25.559 -44.582 1.00 18.61 C
ANISOU 1033 CE1 HIS A 158 2469 2121 2480 44 907 -498 C
ATOM 1034 NE2 HIS A 158 -0.603 -26.642 -45.269 1.00 21.60 N
ANISOU 1034 NE2 HIS A 158 2846 2487 2873 21 933 -487 N
ATOM 1035 N ASN A 159 3.715 -29.659 -47.552 1.00 15.92 N
ANISOU 1035 N ASN A 159 1906 1918 2226 115 931 -422 N
ATOM 1036 CA ASN A 159 3.408 -30.196 -48.876 1.00 15.43 C
ANISOU 1036 CA ASN A 159 1850 1824 2189 119 952 -412 C
ATOM 1037 C ASN A 159 2.791 -31.586 -48.758 1.00 19.62 C
ANISOU 1037 C ASN A 159 2376 2342 2736 106 975 -434 C
ATOM 1038 O ASN A 159 2.188 -31.916 -47.730 1.00 17.66 O
ANISOU 1038 O ASN A 159 2139 2093 2480 77 982 -455 O
ATOM 1039 CB ASN A 159 4.662 -30.234 -49.753 1.00 16.78 C
ANISOU 1039 CB ASN A 159 1984 2019 2374 157 953 -387 C
ATOM 1040 CG ASN A 159 5.062 -28.859 -50.254 1.00 19.25 C
ANISOU 1040 CG ASN A 159 2305 2333 2677 160 948 -364 C
ATOM 1041 OD1 ASN A 159 4.275 -28.175 -50.909 1.00 17.40 O
ANISOU 1041 OD1 ASN A 159 2104 2056 2450 141 958 -363 O
ATOM 1042 ND2 ASN A 159 6.286 -28.443 -49.944 1.00 19.85 N
ANISOU 1042 ND2 ASN A 159 2347 2461 2735 183 938 -348 N
ATOM 1043 N PHE A 160 2.924 -32.405 -49.803 1.00 14.45 N
ANISOU 1043 N PHE A 160 1705 1676 2109 127 992 -431 N
ATOM 1044 CA PHE A 160 2.390 -33.762 -49.815 1.00 19.83 C
ANISOU 1044 CA PHE A 160 2372 2352 2809 122 1017 -457 C
ATOM 1045 C PHE A 160 3.499 -34.809 -49.847 1.00 20.49 C
ANISOU 1045 C PHE A 160 2389 2479 2919 166 1014 -462 C
ATOM 1046 O PHE A 160 3.287 -35.927 -50.322 1.00 23.68 O
ANISOU 1046 O PHE A 160 2769 2878 3349 182 1035 -481 O
ATOM 1047 CB PHE A 160 1.447 -33.962 -51.001 1.00 17.30 C
ANISOU 1047 CB PHE A 160 2089 1981 2502 117 1042 -462 C
ATOM 1048 CG PHE A 160 0.299 -32.994 -51.039 1.00 20.93 C
ANISOU 1048 CG PHE A 160 2616 2398 2937 79 1047 -462 C
ATOM 1049 CD1 PHE A 160 -0.351 -32.616 -49.876 1.00 26.08 C
ANISOU 1049 CD1 PHE A 160 3295 3051 3561 42 1046 -471 C
ATOM 1050 CD2 PHE A 160 -0.128 -32.459 -52.244 1.00 28.68 C
ANISOU 1050 CD2 PHE A 160 3637 3335 3926 81 1056 -455 C
ATOM 1051 CE1 PHE A 160 -1.411 -31.724 -49.914 1.00 25.42 C
ANISOU 1051 CE1 PHE A 160 3277 2928 3454 13 1050 -473 C
ATOM 1052 CE2 PHE A 160 -1.183 -31.563 -52.288 1.00 30.96 C
ANISOU 1052 CE2 PHE A 160 3985 3587 4190 50 1058 -460 C
ATOM 1053 CZ PHE A 160 -1.827 -31.197 -51.122 1.00 31.20 C
ANISOU 1053 CZ PHE A 160 4043 3622 4189 19 1054 -468 C
ATOM 1054 N ILE A 161 4.689 -34.457 -49.361 1.00 22.14 N
ANISOU 1054 N ILE A 161 2565 2730 3118 190 990 -449 N
ATOM 1055 CA ILE A 161 5.792 -35.407 -49.338 1.00 19.21 C
ANISOU 1055 CA ILE A 161 2130 2401 2768 237 987 -456 C
ATOM 1056 C ILE A 161 5.482 -36.520 -48.348 1.00 22.58 C
ANISOU 1056 C ILE A 161 2517 2853 3208 220 998 -493 C
ATOM 1057 O ILE A 161 5.169 -36.266 -47.177 1.00 20.85 O
ANISOU 1057 O ILE A 161 2307 2643 2971 180 996 -506 O
ATOM 1058 CB ILE A 161 7.109 -34.698 -48.991 1.00 15.45 C
ANISOU 1058 CB ILE A 161 1633 1966 2271 264 964 -435 C
ATOM 1059 CG1 ILE A 161 7.442 -33.646 -50.051 1.00 17.02 C
ANISOU 1059 CG1 ILE A 161 1865 2139 2464 275 967 -398 C
ATOM 1060 CG2 ILE A 161 8.238 -35.702 -48.883 1.00 15.99 C
ANISOU 1060 CG2 ILE A 161 1635 2079 2363 316 961 -447 C
ATOM 1061 CD1 ILE A 161 8.580 -32.737 -49.669 1.00 15.10 C
ANISOU 1061 CD1 ILE A 161 1610 1939 2189 290 954 -376 C
ATOM 1062 N HIS A 162 5.572 -37.768 -48.818 1.00 21.40 N
ANISOU 1062 N HIS A 162 2321 2711 3097 251 1013 -514 N
ATOM 1063 CA HIS A 162 5.292 -38.940 -48.003 1.00 26.13 C
ANISOU 1063 CA HIS A 162 2870 3338 3719 235 1032 -554 C
ATOM 1064 C HIS A 162 6.494 -39.865 -47.852 1.00 26.25 C
ANISOU 1064 C HIS A 162 2801 3404 3769 291 1018 -571 C
ATOM 1065 O HIS A 162 6.388 -40.889 -47.162 1.00 23.64 O
ANISOU 1065 O HIS A 162 2412 3101 3467 279 1032 -609 O
ATOM 1066 CB HIS A 162 4.106 -39.723 -48.593 1.00 23.43 C
ANISOU 1066 CB HIS A 162 2541 2966 3396 218 1069 -575 C
ATOM 1067 CG HIS A 162 4.309 -40.151 -50.015 1.00 35.92 C
ANISOU 1067 CG HIS A 162 4116 4528 5005 277 1072 -571 C
ATOM 1068 ND1 HIS A 162 4.010 -39.341 -51.089 1.00 40.75 N
ANISOU 1068 ND1 HIS A 162 4789 5089 5606 282 1070 -546 N
ATOM 1069 CD2 HIS A 162 4.782 -41.308 -50.537 1.00 37.94 C
ANISOU 1069 CD2 HIS A 162 4309 4802 5304 336 1076 -594 C
ATOM 1070 CE1 HIS A 162 4.292 -39.979 -52.211 1.00 37.48 C
ANISOU 1070 CE1 HIS A 162 4356 4657 5227 339 1076 -553 C
ATOM 1071 NE2 HIS A 162 4.760 -41.174 -51.904 1.00 40.71 N
ANISOU 1071 NE2 HIS A 162 4690 5108 5669 376 1077 -582 N
ATOM 1072 N SER A 163 7.632 -39.534 -48.454 1.00 28.08 N
ANISOU 1072 N SER A 163 3020 3646 4002 350 994 -546 N
ATOM 1073 CA SER A 163 8.836 -40.344 -48.366 1.00 25.34 C
ANISOU 1073 CA SER A 163 2594 3345 3690 415 976 -562 C
ATOM 1074 C SER A 163 9.951 -39.525 -47.739 1.00 25.91 C
ANISOU 1074 C SER A 163 2662 3451 3731 427 951 -545 C
ATOM 1075 O SER A 163 10.056 -38.319 -47.981 1.00 26.62 O
ANISOU 1075 O SER A 163 2810 3524 3780 415 948 -510 O
ATOM 1076 CB SER A 163 9.271 -40.844 -49.749 1.00 23.27 C
ANISOU 1076 CB SER A 163 2318 3058 3467 490 975 -553 C
ATOM 1077 OG SER A 163 10.560 -41.426 -49.695 1.00 29.12 O
ANISOU 1077 OG SER A 163 2986 3836 4241 564 948 -562 O
ATOM 1078 N CYS A 164 10.775 -40.185 -46.930 1.00 28.58 N
ANISOU 1078 N CYS A 164 2927 3841 4092 451 934 -576 N
ATOM 1079 CA CYS A 164 11.940 -39.577 -46.303 1.00 22.07 C
ANISOU 1079 CA CYS A 164 2087 3057 3240 472 910 -573 C
ATOM 1080 C CYS A 164 13.200 -39.728 -47.146 1.00 23.31 C
ANISOU 1080 C CYS A 164 2209 3228 3417 562 893 -558 C
ATOM 1081 O CYS A 164 14.301 -39.438 -46.662 1.00 23.10 O
ANISOU 1081 O CYS A 164 2154 3248 3374 593 870 -567 O
ATOM 1082 CB CYS A 164 12.158 -40.196 -44.921 1.00 29.65 C
ANISOU 1082 CB CYS A 164 2982 4063 4219 444 896 -629 C
ATOM 1083 SG CYS A 164 13.153 -39.224 -43.796 1.00 38.34 S
ANISOU 1083 SG CYS A 164 4088 5211 5269 437 870 -643 S
ATOM 1084 N LYS A 165 13.059 -40.168 -48.392 1.00 26.63 N
ANISOU 1084 N LYS A 165 2634 3607 3875 608 901 -540 N
ATOM 1085 CA LYS A 165 14.207 -40.449 -49.243 1.00 23.66 C
ANISOU 1085 CA LYS A 165 2225 3226 3539 704 884 -525 C
ATOM 1086 C LYS A 165 14.926 -39.158 -49.614 1.00 21.26 C
ANISOU 1086 C LYS A 165 1999 2911 3167 703 877 -453 C
ATOM 1087 O LYS A 165 14.350 -38.283 -50.269 1.00 23.54 O
ANISOU 1087 O LYS A 165 2355 3149 3442 669 923 -418 O
ATOM 1088 CB LYS A 165 13.751 -41.181 -50.500 1.00 26.43 C
ANISOU 1088 CB LYS A 165 2581 3517 3946 748 891 -518 C
ATOM 1089 CG LYS A 165 14.837 -41.353 -51.544 1.00 30.10 C
ANISOU 1089 CG LYS A 165 3060 3949 4428 840 844 -465 C
ATOM 1090 CD LYS A 165 15.961 -42.251 -51.042 1.00 40.39 C
ANISOU 1090 CD LYS A 165 4295 5314 5738 905 756 -479 C
ATOM 1091 CE LYS A 165 16.679 -42.908 -52.208 1.00 44.12 C
ANISOU 1091 CE LYS A 165 4782 5741 6239 1003 692 -435 C
ATOM 1092 NZ LYS A 165 17.812 -43.763 -51.775 1.00 40.77 N
ANISOU 1092 NZ LYS A 165 4297 5375 5819 1075 592 -445 N
ATOM 1093 N LEU A 166 16.178 -39.041 -49.192 1.00 20.61 N
ANISOU 1093 N LEU A 166 1917 2883 3032 733 810 -427 N
ATOM 1094 CA LEU A 166 17.034 -37.962 -49.660 1.00 23.59 C
ANISOU 1094 CA LEU A 166 2374 3259 3331 736 792 -345 C
ATOM 1095 C LEU A 166 17.550 -38.310 -51.047 1.00 22.80 C
ANISOU 1095 C LEU A 166 2313 3103 3246 796 760 -278 C
ATOM 1096 O LEU A 166 18.309 -39.276 -51.189 1.00 28.23 O
ANISOU 1096 O LEU A 166 2970 3804 3952 866 692 -275 O
ATOM 1097 CB LEU A 166 18.197 -37.739 -48.705 1.00 20.02 C
ANISOU 1097 CB LEU A 166 1916 2885 2805 748 734 -343 C
ATOM 1098 CG LEU A 166 17.833 -37.550 -47.234 1.00 28.69 C
ANISOU 1098 CG LEU A 166 2972 4035 3891 697 748 -417 C
ATOM 1099 CD1 LEU A 166 19.095 -37.509 -46.393 1.00 25.84 C
ANISOU 1099 CD1 LEU A 166 2606 3750 3461 722 677 -420 C
ATOM 1100 CD2 LEU A 166 17.000 -36.295 -47.021 1.00 25.00 C
ANISOU 1100 CD2 LEU A 166 2554 3547 3399 629 818 -417 C
ATOM 1101 N PRO A 167 17.171 -37.572 -52.085 1.00 21.28 N
ANISOU 1101 N PRO A 167 2190 2844 3051 772 801 -224 N
ATOM 1102 CA PRO A 167 17.511 -37.977 -53.452 1.00 20.67 C
ANISOU 1102 CA PRO A 167 2156 2696 3002 825 774 -166 C
ATOM 1103 C PRO A 167 19.011 -37.996 -53.701 1.00 22.85 C
ANISOU 1103 C PRO A 167 2472 2994 3217 876 699 -92 C
ATOM 1104 O PRO A 167 19.800 -37.368 -52.992 1.00 22.86 O
ANISOU 1104 O PRO A 167 2488 3062 3137 858 682 -71 O
ATOM 1105 CB PRO A 167 16.820 -36.916 -54.315 1.00 22.21 C
ANISOU 1105 CB PRO A 167 2420 2825 3193 767 836 -125 C
ATOM 1106 CG PRO A 167 16.631 -35.743 -53.393 1.00 22.77 C
ANISOU 1106 CG PRO A 167 2495 2952 3205 696 876 -137 C
ATOM 1107 CD PRO A 167 16.376 -36.333 -52.051 1.00 19.14 C
ANISOU 1107 CD PRO A 167 1960 2557 2756 696 870 -219 C
ATOM 1108 N ALA A 168 19.392 -38.727 -54.754 1.00 30.79 N
ANISOU 1108 N ALA A 168 3503 3936 4258 943 653 -52 N
ATOM 1109 CA ALA A 168 20.805 -38.904 -55.074 1.00 27.99 C
ANISOU 1109 CA ALA A 168 3198 3591 3848 1001 571 23 C
ATOM 1110 C ALA A 168 21.448 -37.615 -55.567 1.00 25.56 C
ANISOU 1110 C ALA A 168 2990 3272 3450 950 594 120 C
ATOM 1111 O ALA A 168 22.659 -37.428 -55.396 1.00 34.87 O
ANISOU 1111 O ALA A 168 4211 4494 4545 971 544 177 O
ATOM 1112 CB ALA A 168 20.976 -40.004 -56.120 1.00 24.29 C
ANISOU 1112 CB ALA A 168 2738 3043 3446 1089 513 41 C
ATOM 1113 N TYR A 169 20.670 -36.720 -56.181 1.00 22.64 N
ANISOU 1113 N TYR A 169 2658 2849 3094 882 669 140 N
ATOM 1114 CA TYR A 169 21.250 -35.485 -56.694 1.00 23.67 C
ANISOU 1114 CA TYR A 169 2872 2973 3148 826 697 229 C
ATOM 1115 C TYR A 169 21.730 -34.556 -55.587 1.00 27.65 C
ANISOU 1115 C TYR A 169 3363 3582 3561 782 720 221 C
ATOM 1116 O TYR A 169 22.345 -33.529 -55.891 1.00 37.41 O
ANISOU 1116 O TYR A 169 4659 4832 4723 737 747 292 O
ATOM 1117 CB TYR A 169 20.252 -34.756 -57.604 1.00 26.32 C
ANISOU 1117 CB TYR A 169 3240 3230 3530 761 767 242 C
ATOM 1118 CG TYR A 169 18.967 -34.278 -56.950 1.00 24.06 C
ANISOU 1118 CG TYR A 169 2897 2966 3278 705 833 159 C
ATOM 1119 CD1 TYR A 169 18.965 -33.218 -56.055 1.00 24.36 C
ANISOU 1119 CD1 TYR A 169 2918 3081 3256 648 872 144 C
ATOM 1120 CD2 TYR A 169 17.750 -34.865 -57.261 1.00 21.42 C
ANISOU 1120 CD2 TYR A 169 2535 2573 3031 710 855 98 C
ATOM 1121 CE1 TYR A 169 17.796 -32.778 -55.469 1.00 23.09 C
ANISOU 1121 CE1 TYR A 169 2716 2932 3124 601 923 73 C
ATOM 1122 CE2 TYR A 169 16.573 -34.425 -56.680 1.00 21.96 C
ANISOU 1122 CE2 TYR A 169 2566 2658 3121 658 912 29 C
ATOM 1123 CZ TYR A 169 16.603 -33.381 -55.786 1.00 25.93 C
ANISOU 1123 CZ TYR A 169 3056 3231 3565 604 942 20 C
ATOM 1124 OH TYR A 169 15.438 -32.939 -55.204 1.00 25.83 O
ANISOU 1124 OH TYR A 169 3016 3228 3572 557 989 -44 O
ATOM 1125 N PHE A 170 21.462 -34.887 -54.321 1.00 23.55 N
ANISOU 1125 N PHE A 170 2768 3135 3046 790 713 136 N
ATOM 1126 CA PHE A 170 22.014 -34.119 -53.210 1.00 28.74 C
ANISOU 1126 CA PHE A 170 3415 3889 3615 762 721 120 C
ATOM 1127 C PHE A 170 23.537 -34.087 -53.233 1.00 29.60 C
ANISOU 1127 C PHE A 170 3580 4044 3625 798 665 190 C
ATOM 1128 O PHE A 170 24.137 -33.206 -52.608 1.00 27.83 O
ANISOU 1128 O PHE A 170 3373 3892 3308 768 685 200 O
ATOM 1129 CB PHE A 170 21.527 -34.694 -51.879 1.00 34.12 C
ANISOU 1129 CB PHE A 170 4011 4626 4326 771 708 16 C
ATOM 1130 CG PHE A 170 20.231 -34.103 -51.397 1.00 32.39 C
ANISOU 1130 CG PHE A 170 3758 4400 4147 708 780 -47 C
ATOM 1131 CD1 PHE A 170 19.408 -33.398 -52.258 1.00 32.92 C
ANISOU 1131 CD1 PHE A 170 3857 4403 4246 661 840 -21 C
ATOM 1132 CD2 PHE A 170 19.852 -34.236 -50.073 1.00 28.64 C
ANISOU 1132 CD2 PHE A 170 3226 3980 3678 693 780 -131 C
ATOM 1133 CE1 PHE A 170 18.223 -32.849 -51.808 1.00 31.21 C
ANISOU 1133 CE1 PHE A 170 3618 4180 4062 609 896 -78 C
ATOM 1134 CE2 PHE A 170 18.671 -33.689 -49.617 1.00 28.32 C
ANISOU 1134 CE2 PHE A 170 3166 3926 3668 638 840 -183 C
ATOM 1135 CZ PHE A 170 17.854 -32.994 -50.485 1.00 28.26 C
ANISOU 1135 CZ PHE A 170 3193 3857 3688 599 896 -156 C
ATOM 1136 N SER A 171 24.175 -35.029 -53.932 1.00 30.30 N
ANISOU 1136 N SER A 171 3698 4089 3724 865 594 237 N
ATOM 1137 CA SER A 171 25.627 -34.992 -54.072 1.00 33.95 C
ANISOU 1137 CA SER A 171 4232 4584 4083 900 536 316 C
ATOM 1138 C SER A 171 26.071 -33.838 -54.960 1.00 32.47 C
ANISOU 1138 C SER A 171 4139 4370 3827 841 592 419 C
ATOM 1139 O SER A 171 27.205 -33.363 -54.834 1.00 33.18 O
ANISOU 1139 O SER A 171 4290 4513 3803 838 579 479 O
ATOM 1140 CB SER A 171 26.133 -36.324 -54.627 1.00 38.84 C
ANISOU 1140 CB SER A 171 4864 5155 4739 993 437 340 C
ATOM 1141 OG SER A 171 25.554 -36.603 -55.889 1.00 45.90 O
ANISOU 1141 OG SER A 171 5788 5935 5715 1000 451 377 O
ATOM 1142 N ASN A 172 25.199 -33.378 -55.862 1.00 33.85 N
ANISOU 1142 N ASN A 172 4328 4466 4069 790 655 438 N
ATOM 1143 CA ASN A 172 25.500 -32.182 -56.640 1.00 37.01 C
ANISOU 1143 CA ASN A 172 4800 4846 4415 717 720 524 C
ATOM 1144 C ASN A 172 25.373 -30.924 -55.794 1.00 34.81 C
ANISOU 1144 C ASN A 172 4488 4660 4079 649 795 489 C
ATOM 1145 O ASN A 172 26.029 -29.915 -56.079 1.00 37.70 O
ANISOU 1145 O ASN A 172 4905 5056 4363 598 841 555 O
ATOM 1146 CB ASN A 172 24.574 -32.089 -57.853 1.00 44.05 C
ANISOU 1146 CB ASN A 172 5712 5623 5402 682 757 546 C
ATOM 1147 CG ASN A 172 24.992 -33.010 -58.977 1.00 44.42 C
ANISOU 1147 CG ASN A 172 5829 5568 5482 738 691 615 C
ATOM 1148 OD1 ASN A 172 26.110 -33.519 -58.990 1.00 49.48 O
ANISOU 1148 OD1 ASN A 172 6520 6221 6059 794 622 669 O
ATOM 1149 ND2 ASN A 172 24.097 -33.218 -59.936 1.00 34.83 N
ANISOU 1149 ND2 ASN A 172 4622 4246 4364 727 707 611 N
ATOM 1150 N LEU A 173 24.542 -30.969 -54.753 1.00 30.01 N
ANISOU 1150 N LEU A 173 3795 4095 3511 649 808 384 N
ATOM 1151 CA LEU A 173 24.243 -29.806 -53.918 1.00 25.56 C
ANISOU 1151 CA LEU A 173 3195 3606 2911 594 874 337 C
ATOM 1152 C LEU A 173 25.185 -29.791 -52.712 1.00 30.31 C
ANISOU 1152 C LEU A 173 3787 4315 3415 625 841 307 C
ATOM 1153 O LEU A 173 24.791 -29.996 -51.563 1.00 30.48 O
ANISOU 1153 O LEU A 173 3749 4383 3451 640 828 216 O
ATOM 1154 CB LEU A 173 22.782 -29.830 -53.486 1.00 22.26 C
ANISOU 1154 CB LEU A 173 2707 3163 2589 574 903 245 C
ATOM 1155 CG LEU A 173 21.746 -30.070 -54.584 1.00 28.33 C
ANISOU 1155 CG LEU A 173 3481 3825 3458 554 922 256 C
ATOM 1156 CD1 LEU A 173 20.337 -30.027 -54.013 1.00 27.73 C
ANISOU 1156 CD1 LEU A 173 3345 3738 3455 533 952 164 C
ATOM 1157 CD2 LEU A 173 21.903 -29.051 -55.700 1.00 27.17 C
ANISOU 1157 CD2 LEU A 173 3388 3640 3294 493 973 337 C
ATOM 1158 N THR A 174 26.461 -29.527 -53.003 1.00 30.67 N
ANISOU 1158 N THR A 174 3903 4397 3355 632 829 386 N
ATOM 1159 CA THR A 174 27.502 -29.630 -51.986 1.00 33.96 C
ANISOU 1159 CA THR A 174 4327 4910 3666 670 786 365 C
ATOM 1160 C THR A 174 27.364 -28.587 -50.885 1.00 38.00 C
ANISOU 1160 C THR A 174 4798 5510 4130 636 842 294 C
ATOM 1161 O THR A 174 28.003 -28.724 -49.836 1.00 40.05 O
ANISOU 1161 O THR A 174 5050 5848 4318 670 803 248 O
ATOM 1162 CB THR A 174 28.883 -29.495 -52.630 1.00 34.87 C
ANISOU 1162 CB THR A 174 4541 5040 3665 679 769 475 C
ATOM 1163 OG1 THR A 174 29.085 -28.138 -53.039 1.00 38.34 O
ANISOU 1163 OG1 THR A 174 5014 5508 4046 605 865 526 O
ATOM 1164 CG2 THR A 174 28.986 -30.398 -53.842 1.00 34.70 C
ANISOU 1164 CG2 THR A 174 4573 4915 3695 711 716 554 C
ATOM 1165 N ASN A 175 26.556 -27.550 -51.095 1.00 28.69 N
ANISOU 1165 N ASN A 175 3592 4320 2989 575 926 281 N
ATOM 1166 CA ASN A 175 26.400 -26.482 -50.119 1.00 27.62 C
ANISOU 1166 CA ASN A 175 3418 4262 2814 549 978 214 C
ATOM 1167 C ASN A 175 25.111 -26.588 -49.316 1.00 32.09 C
ANISOU 1167 C ASN A 175 3910 4807 3475 546 978 110 C
ATOM 1168 O ASN A 175 24.885 -25.767 -48.423 1.00 30.95 O
ANISOU 1168 O ASN A 175 3734 4717 3308 533 1011 45 O
ATOM 1169 CB ASN A 175 26.458 -25.120 -50.817 1.00 25.70 C
ANISOU 1169 CB ASN A 175 3190 4034 2541 483 1071 265 C
ATOM 1170 CG ASN A 175 27.778 -24.885 -51.522 1.00 29.89 C
ANISOU 1170 CG ASN A 175 3800 4594 2963 472 1085 370 C
ATOM 1171 OD1 ASN A 175 28.776 -24.544 -50.891 1.00 31.26 O
ANISOU 1171 OD1 ASN A 175 3999 4860 3021 487 1090 368 O
ATOM 1172 ND2 ASN A 175 27.791 -25.066 -52.840 1.00 29.52 N
ANISOU 1172 ND2 ASN A 175 3801 4467 2950 443 1093 463 N
ATOM 1173 N LEU A 176 24.263 -27.571 -49.608 1.00 28.61 N
ANISOU 1173 N LEU A 176 3447 4289 3136 560 943 93 N
ATOM 1174 CA LEU A 176 22.990 -27.720 -48.908 1.00 27.80 C
ANISOU 1174 CA LEU A 176 3285 4159 3119 550 948 3 C
ATOM 1175 C LEU A 176 23.246 -28.164 -47.473 1.00 29.98 C
ANISOU 1175 C LEU A 176 3530 4493 3366 584 901 -79 C
ATOM 1176 O LEU A 176 23.745 -29.269 -47.239 1.00 33.28 O
ANISOU 1176 O LEU A 176 3945 4919 3782 628 833 -85 O
ATOM 1177 CB LEU A 176 22.103 -28.717 -49.647 1.00 23.77 C
ANISOU 1177 CB LEU A 176 2762 3555 2714 556 930 9 C
ATOM 1178 CG LEU A 176 20.684 -28.947 -49.115 1.00 23.22 C
ANISOU 1178 CG LEU A 176 2643 3446 2733 539 943 -72 C
ATOM 1179 CD1 LEU A 176 19.863 -27.669 -49.144 1.00 20.37 C
ANISOU 1179 CD1 LEU A 176 2278 3077 2385 487 1007 -88 C
ATOM 1180 CD2 LEU A 176 19.997 -30.040 -49.915 1.00 24.01 C
ANISOU 1180 CD2 LEU A 176 2735 3463 2923 553 927 -64 C
ATOM 1181 N VAL A 177 22.910 -27.305 -46.510 1.00 21.42 N
ANISOU 1181 N VAL A 177 2424 3451 2264 565 930 -145 N
ATOM 1182 CA VAL A 177 23.093 -27.625 -45.100 1.00 24.80 C
ANISOU 1182 CA VAL A 177 2829 3927 2668 589 887 -229 C
ATOM 1183 C VAL A 177 21.780 -27.802 -44.344 1.00 29.25 C
ANISOU 1183 C VAL A 177 3350 4446 3319 568 891 -310 C
ATOM 1184 O VAL A 177 21.796 -28.386 -43.248 1.00 28.33 O
ANISOU 1184 O VAL A 177 3210 4348 3206 582 846 -379 O
ATOM 1185 CB VAL A 177 23.972 -26.572 -44.391 1.00 28.49 C
ANISOU 1185 CB VAL A 177 3316 4482 3028 596 905 -249 C
ATOM 1186 CG1 VAL A 177 25.421 -26.696 -44.839 1.00 30.00 C
ANISOU 1186 CG1 VAL A 177 3557 4728 3115 623 884 -179 C
ATOM 1187 CG2 VAL A 177 23.435 -25.166 -44.647 1.00 27.01 C
ANISOU 1187 CG2 VAL A 177 3122 4296 2843 559 984 -247 C
ATOM 1188 N HIS A 178 20.652 -27.321 -44.872 1.00 24.19 N
ANISOU 1188 N HIS A 178 2702 3746 2743 532 940 -305 N
ATOM 1189 CA HIS A 178 19.387 -27.425 -44.153 1.00 19.06 C
ANISOU 1189 CA HIS A 178 2027 3052 2164 509 945 -376 C
ATOM 1190 C HIS A 178 18.265 -27.812 -45.106 1.00 25.74 C
ANISOU 1190 C HIS A 178 2870 3813 3097 480 967 -351 C
ATOM 1191 O HIS A 178 18.137 -27.245 -46.198 1.00 27.12 O
ANISOU 1191 O HIS A 178 3064 3962 3280 460 996 -295 O
ATOM 1192 CB HIS A 178 19.035 -26.114 -43.436 1.00 18.98 C
ANISOU 1192 CB HIS A 178 2044 3015 2154 464 951 -405 C
ATOM 1193 CG HIS A 178 17.976 -26.268 -42.388 1.00 34.51 C
ANISOU 1193 CG HIS A 178 4022 4918 4173 450 925 -448 C
ATOM 1194 ND1 HIS A 178 16.632 -26.137 -42.662 1.00 36.69 N
ANISOU 1194 ND1 HIS A 178 4311 5135 4495 438 916 -421 N
ATOM 1195 CD2 HIS A 178 18.062 -26.564 -41.069 1.00 35.67 C
ANISOU 1195 CD2 HIS A 178 4165 5080 4306 457 884 -509 C
ATOM 1196 CE1 HIS A 178 15.936 -26.335 -41.558 1.00 29.71 C
ANISOU 1196 CE1 HIS A 178 3436 4223 3631 424 881 -468 C
ATOM 1197 NE2 HIS A 178 16.780 -26.595 -40.576 1.00 35.55 N
ANISOU 1197 NE2 HIS A 178 4167 4999 4343 433 868 -521 N
ATOM 1198 N VAL A 179 17.464 -28.790 -44.686 1.00 22.89 N
ANISOU 1198 N VAL A 179 2486 3411 2801 473 950 -397 N
ATOM 1199 CA VAL A 179 16.257 -29.197 -45.392 1.00 18.88 C
ANISOU 1199 CA VAL A 179 1982 2833 2357 445 939 -379 C
ATOM 1200 C VAL A 179 15.115 -29.213 -44.383 1.00 15.88 C
ANISOU 1200 C VAL A 179 1617 2420 1998 415 903 -412 C
ATOM 1201 O VAL A 179 15.214 -29.876 -43.343 1.00 19.31 O
ANISOU 1201 O VAL A 179 2035 2859 2442 419 889 -455 O
ATOM 1202 CB VAL A 179 16.414 -30.572 -46.061 1.00 22.42 C
ANISOU 1202 CB VAL A 179 2403 3253 2861 477 955 -369 C
ATOM 1203 CG1 VAL A 179 15.090 -31.020 -46.642 1.00 23.09 C
ANISOU 1203 CG1 VAL A 179 2498 3269 3008 443 943 -367 C
ATOM 1204 CG2 VAL A 179 17.488 -30.515 -47.140 1.00 19.47 C
ANISOU 1204 CG2 VAL A 179 2054 2890 2452 508 944 -289 C
ATOM 1205 N ASP A 180 14.045 -28.475 -44.678 1.00 15.58 N
ANISOU 1205 N ASP A 180 1609 2339 1972 378 893 -398 N
ATOM 1206 CA ASP A 180 12.867 -28.420 -43.818 1.00 15.02 C
ANISOU 1206 CA ASP A 180 1563 2223 1920 346 869 -425 C
ATOM 1207 C ASP A 180 11.803 -29.332 -44.413 1.00 17.76 C
ANISOU 1207 C ASP A 180 1915 2514 2321 318 873 -423 C
ATOM 1208 O ASP A 180 11.227 -29.025 -45.461 1.00 18.86 O
ANISOU 1208 O ASP A 180 2072 2618 2477 302 881 -396 O
ATOM 1209 CB ASP A 180 12.347 -26.991 -43.678 1.00 16.33 C
ANISOU 1209 CB ASP A 180 1760 2379 2064 332 858 -420 C
ATOM 1210 CG ASP A 180 11.307 -26.850 -42.578 1.00 25.34 C
ANISOU 1210 CG ASP A 180 2931 3477 3219 306 839 -456 C
ATOM 1211 OD1 ASP A 180 10.838 -27.883 -42.057 1.00 23.30 O
ANISOU 1211 OD1 ASP A 180 2671 3192 2990 284 840 -482 O
ATOM 1212 OD2 ASP A 180 10.964 -25.702 -42.226 1.00 25.08 O
ANISOU 1212 OD2 ASP A 180 2921 3439 3170 306 828 -463 O
ATOM 1213 N LEU A 181 11.547 -30.457 -43.749 1.00 17.84 N
ANISOU 1213 N LEU A 181 1906 2513 2359 309 871 -455 N
ATOM 1214 CA LEU A 181 10.485 -31.373 -44.143 1.00 16.18 C
ANISOU 1214 CA LEU A 181 1698 2254 2194 281 880 -459 C
ATOM 1215 C LEU A 181 9.267 -31.283 -43.235 1.00 23.75 C
ANISOU 1215 C LEU A 181 2689 3171 3162 231 879 -487 C
ATOM 1216 O LEU A 181 8.436 -32.197 -43.246 1.00 21.34 O
ANISOU 1216 O LEU A 181 2382 2836 2891 202 894 -502 O
ATOM 1217 CB LEU A 181 11.006 -32.812 -44.172 1.00 15.45 C
ANISOU 1217 CB LEU A 181 1551 2184 2137 304 889 -479 C
ATOM 1218 CG LEU A 181 12.035 -33.143 -45.256 1.00 21.28 C
ANISOU 1218 CG LEU A 181 2257 2946 2882 358 899 -454 C
ATOM 1219 CD1 LEU A 181 12.635 -34.523 -45.055 1.00 26.76 C
ANISOU 1219 CD1 LEU A 181 2884 3667 3615 392 899 -485 C
ATOM 1220 CD2 LEU A 181 11.415 -33.041 -46.637 1.00 22.84 C
ANISOU 1220 CD2 LEU A 181 2483 3095 3101 352 913 -420 C
ATOM 1221 N SER A 182 9.139 -30.211 -42.452 1.00 21.18 N
ANISOU 1221 N SER A 182 2395 2844 2808 221 865 -498 N
ATOM 1222 CA SER A 182 8.079 -30.131 -41.455 1.00 18.35 C
ANISOU 1222 CA SER A 182 2070 2442 2459 176 869 -531 C
ATOM 1223 C SER A 182 6.709 -30.199 -42.111 1.00 14.23 C
ANISOU 1223 C SER A 182 1587 1863 1958 141 885 -517 C
ATOM 1224 O SER A 182 6.532 -29.806 -43.267 1.00 17.55 O
ANISOU 1224 O SER A 182 2018 2273 2376 153 883 -484 O
ATOM 1225 CB SER A 182 8.192 -28.841 -40.638 1.00 15.60 C
ANISOU 1225 CB SER A 182 1752 2097 2078 185 851 -546 C
ATOM 1226 OG SER A 182 9.527 -28.608 -40.220 1.00 43.22 O
ANISOU 1226 OG SER A 182 5222 5653 5548 224 838 -555 O
ATOM 1227 N TYR A 183 5.740 -30.733 -41.365 1.00 14.37 N
ANISOU 1227 N TYR A 183 1626 1842 1994 93 907 -547 N
ATOM 1228 CA TYR A 183 4.330 -30.695 -41.749 1.00 15.03 C
ANISOU 1228 CA TYR A 183 1758 1867 2085 55 928 -541 C
ATOM 1229 C TYR A 183 4.098 -31.346 -43.115 1.00 14.26 C
ANISOU 1229 C TYR A 183 1649 1764 2006 64 939 -515 C
ATOM 1230 O TYR A 183 3.463 -30.773 -44.003 1.00 19.49 O
ANISOU 1230 O TYR A 183 2346 2395 2663 64 938 -494 O
ATOM 1231 CB TYR A 183 3.815 -29.253 -41.727 1.00 15.33 C
ANISOU 1231 CB TYR A 183 1849 1878 2098 60 911 -533 C
ATOM 1232 CG TYR A 183 2.311 -29.098 -41.741 1.00 25.36 C
ANISOU 1232 CG TYR A 183 3184 3084 3368 18 935 -539 C
ATOM 1233 CD1 TYR A 183 1.470 -30.204 -41.655 1.00 35.51 C
ANISOU 1233 CD1 TYR A 183 4482 4339 4671 -28 976 -551 C
ATOM 1234 CD2 TYR A 183 1.730 -27.840 -41.852 1.00 30.19 C
ANISOU 1234 CD2 TYR A 183 3843 3668 3961 27 920 -534 C
ATOM 1235 CE1 TYR A 183 0.096 -30.060 -41.676 1.00 37.63 C
ANISOU 1235 CE1 TYR A 183 4819 4550 4929 -66 1004 -554 C
ATOM 1236 CE2 TYR A 183 0.360 -27.685 -41.873 1.00 32.10 C
ANISOU 1236 CE2 TYR A 183 4153 3850 4195 -6 942 -540 C
ATOM 1237 CZ TYR A 183 -0.452 -28.797 -41.783 1.00 37.09 C
ANISOU 1237 CZ TYR A 183 4807 4452 4835 -54 986 -547 C
ATOM 1238 OH TYR A 183 -1.819 -28.637 -41.806 1.00 45.39 O
ANISOU 1238 OH TYR A 183 5935 5443 5866 -89 1012 -551 O
ATOM 1239 N ASN A 184 4.631 -32.556 -43.286 1.00 18.06 N
ANISOU 1239 N ASN A 184 2077 2273 2511 75 950 -522 N
ATOM 1240 CA ASN A 184 4.327 -33.357 -44.467 1.00 18.61 C
ANISOU 1240 CA ASN A 184 2135 2332 2603 85 965 -509 C
ATOM 1241 C ASN A 184 3.671 -34.662 -44.038 1.00 21.15 C
ANISOU 1241 C ASN A 184 2437 2646 2954 50 1002 -542 C
ATOM 1242 O ASN A 184 3.116 -34.739 -42.937 1.00 26.51 O
ANISOU 1242 O ASN A 184 3132 3309 3632 2 1022 -570 O
ATOM 1243 CB ASN A 184 5.587 -33.622 -45.299 1.00 16.76 C
ANISOU 1243 CB ASN A 184 1852 2138 2376 142 949 -489 C
ATOM 1244 CG ASN A 184 5.945 -32.458 -46.201 1.00 20.33 C
ANISOU 1244 CG ASN A 184 2330 2586 2808 166 932 -453 C
ATOM 1245 OD1 ASN A 184 5.372 -32.297 -47.280 1.00 19.66 O
ANISOU 1245 OD1 ASN A 184 2272 2463 2733 163 943 -437 O
ATOM 1246 ND2 ASN A 184 6.889 -31.639 -45.763 1.00 16.39 N
ANISOU 1246 ND2 ASN A 184 1821 2124 2282 187 911 -444 N
ATOM 1247 N TYR A 185 3.733 -35.693 -44.878 1.00 18.90 N
ANISOU 1247 N TYR A 185 2116 2370 2696 72 1016 -543 N
ATOM 1248 CA TYR A 185 3.026 -36.943 -44.624 1.00 16.85 C
ANISOU 1248 CA TYR A 185 1832 2106 2464 40 1056 -576 C
ATOM 1249 C TYR A 185 3.984 -38.116 -44.455 1.00 25.48 C
ANISOU 1249 C TYR A 185 2837 3251 3594 71 1056 -600 C
ATOM 1250 O TYR A 185 3.627 -39.263 -44.725 1.00 25.05 O
ANISOU 1250 O TYR A 185 2744 3203 3571 70 1085 -623 O
ATOM 1251 CB TYR A 185 2.017 -37.224 -45.737 1.00 16.25 C
ANISOU 1251 CB TYR A 185 1790 1993 2392 37 1081 -569 C
ATOM 1252 CG TYR A 185 0.882 -36.222 -45.793 1.00 25.12 C
ANISOU 1252 CG TYR A 185 2998 3063 3483 -2 1090 -556 C
ATOM 1253 CD1 TYR A 185 1.058 -34.981 -46.386 1.00 25.75 C
ANISOU 1253 CD1 TYR A 185 3116 3125 3541 19 1057 -525 C
ATOM 1254 CD2 TYR A 185 -0.360 -36.517 -45.247 1.00 24.53 C
ANISOU 1254 CD2 TYR A 185 2964 2956 3401 -60 1134 -578 C
ATOM 1255 CE1 TYR A 185 0.029 -34.058 -46.436 1.00 20.17 C
ANISOU 1255 CE1 TYR A 185 2482 2373 2809 -11 1063 -518 C
ATOM 1256 CE2 TYR A 185 -1.396 -35.599 -45.291 1.00 27.11 C
ANISOU 1256 CE2 TYR A 185 3373 3233 3695 -91 1142 -567 C
ATOM 1257 CZ TYR A 185 -1.195 -34.370 -45.886 1.00 27.36 C
ANISOU 1257 CZ TYR A 185 3437 3250 3709 -63 1103 -538 C
ATOM 1258 OH TYR A 185 -2.223 -33.457 -45.933 1.00 36.87 O
ANISOU 1258 OH TYR A 185 4720 4408 4883 -89 1110 -532 O
ATOM 1259 N ILE A 186 5.203 -37.847 -43.991 1.00 16.71 N
ANISOU 1259 N ILE A 186 1690 2180 2480 102 1024 -598 N
ATOM 1260 CA ILE A 186 6.185 -38.909 -43.802 1.00 20.83 C
ANISOU 1260 CA ILE A 186 2124 2753 3038 137 1018 -624 C
ATOM 1261 C ILE A 186 5.777 -39.756 -42.603 1.00 24.18 C
ANISOU 1261 C ILE A 186 2505 3189 3493 79 1048 -678 C
ATOM 1262 O ILE A 186 5.678 -39.258 -41.475 1.00 28.02 O
ANISOU 1262 O ILE A 186 3011 3669 3967 32 1050 -697 O
ATOM 1263 CB ILE A 186 7.595 -38.333 -43.624 1.00 24.73 C
ANISOU 1263 CB ILE A 186 2595 3286 3514 186 979 -612 C
ATOM 1264 CG1 ILE A 186 8.027 -37.576 -44.882 1.00 25.54 C
ANISOU 1264 CG1 ILE A 186 2733 3379 3592 237 962 -562 C
ATOM 1265 CG2 ILE A 186 8.594 -39.444 -43.303 1.00 17.82 C
ANISOU 1265 CG2 ILE A 186 1624 2466 2682 221 969 -648 C
ATOM 1266 CD1 ILE A 186 9.363 -36.889 -44.747 1.00 16.60 C
ANISOU 1266 CD1 ILE A 186 1589 2286 2434 281 934 -547 C
ATOM 1267 N GLN A 187 5.534 -41.046 -42.849 1.00 21.49 N
ANISOU 1267 N GLN A 187 2105 2865 3197 81 1073 -706 N
ATOM 1268 CA GLN A 187 5.205 -42.009 -41.809 1.00 24.07 C
ANISOU 1268 CA GLN A 187 2372 3209 3562 23 1107 -762 C
ATOM 1269 C GLN A 187 6.325 -42.996 -41.519 1.00 24.91 C
ANISOU 1269 C GLN A 187 2366 3379 3720 60 1085 -801 C
ATOM 1270 O GLN A 187 6.309 -43.627 -40.457 1.00 26.51 O
ANISOU 1270 O GLN A 187 2510 3606 3959 8 1101 -855 O
ATOM 1271 CB GLN A 187 3.943 -42.802 -42.196 1.00 22.56 C
ANISOU 1271 CB GLN A 187 2190 2995 3386 -13 1162 -775 C
ATOM 1272 CG GLN A 187 2.726 -41.949 -42.549 1.00 34.04 C
ANISOU 1272 CG GLN A 187 3752 4387 4794 -49 1185 -744 C
ATOM 1273 CD GLN A 187 1.510 -42.782 -42.938 1.00 36.08 C
ANISOU 1273 CD GLN A 187 4017 4627 5062 -81 1243 -762 C
ATOM 1274 OE1 GLN A 187 0.929 -43.484 -42.106 1.00 41.60 O
ANISOU 1274 OE1 GLN A 187 4692 5332 5782 -146 1292 -802 O
ATOM 1275 NE2 GLN A 187 1.119 -42.703 -44.205 1.00 40.99 N
ANISOU 1275 NE2 GLN A 187 4674 5229 5670 -40 1241 -737 N
ATOM 1276 N THR A 188 7.291 -43.141 -42.423 1.00 23.48 N
ANISOU 1276 N THR A 188 2152 3223 3547 147 1047 -779 N
ATOM 1277 CA THR A 188 8.325 -44.160 -42.324 1.00 31.33 C
ANISOU 1277 CA THR A 188 3034 4275 4595 196 1019 -817 C
ATOM 1278 C THR A 188 9.688 -43.549 -42.619 1.00 27.87 C
ANISOU 1278 C THR A 188 2590 3862 4138 270 964 -793 C
ATOM 1279 O THR A 188 9.810 -42.618 -43.419 1.00 24.58 O
ANISOU 1279 O THR A 188 2247 3417 3677 304 956 -738 O
ATOM 1280 CB THR A 188 8.043 -45.323 -43.296 1.00 36.71 C
ANISOU 1280 CB THR A 188 3664 4962 5321 240 1035 -826 C
ATOM 1281 OG1 THR A 188 6.749 -45.872 -43.018 1.00 39.98 O
ANISOU 1281 OG1 THR A 188 4086 5358 5746 169 1094 -851 O
ATOM 1282 CG2 THR A 188 9.079 -46.427 -43.167 1.00 42.31 C
ANISOU 1282 CG2 THR A 188 4249 5732 6095 296 998 -870 C
ATOM 1283 N ILE A 189 10.707 -44.071 -41.942 1.00 27.16 N
ANISOU 1283 N ILE A 189 2409 3828 4081 292 926 -839 N
ATOM 1284 CA ILE A 189 12.104 -43.794 -42.256 1.00 24.57 C
ANISOU 1284 CA ILE A 189 2054 3538 3746 375 870 -829 C
ATOM 1285 C ILE A 189 12.801 -45.137 -42.418 1.00 24.93 C
ANISOU 1285 C ILE A 189 1978 3633 3862 436 830 -873 C
ATOM 1286 O ILE A 189 12.887 -45.913 -41.459 1.00 24.18 O
ANISOU 1286 O ILE A 189 1796 3582 3810 400 816 -939 O
ATOM 1287 CB ILE A 189 12.795 -42.954 -41.168 1.00 30.97 C
ANISOU 1287 CB ILE A 189 2872 4378 4516 353 842 -853 C
ATOM 1288 CG1 ILE A 189 12.022 -41.659 -40.922 1.00 27.63 C
ANISOU 1288 CG1 ILE A 189 2565 3903 4030 294 877 -814 C
ATOM 1289 CG2 ILE A 189 14.232 -42.648 -41.569 1.00 24.06 C
ANISOU 1289 CG2 ILE A 189 1974 3549 3621 444 785 -844 C
ATOM 1290 CD1 ILE A 189 12.557 -40.848 -39.768 1.00 22.66 C
ANISOU 1290 CD1 ILE A 189 1948 3298 3363 268 857 -847 C
ATOM 1291 N THR A 190 13.285 -45.415 -43.622 1.00 24.33 N
ANISOU 1291 N THR A 190 1893 3549 3801 527 808 -842 N
ATOM 1292 CA THR A 190 13.909 -46.692 -43.933 1.00 28.86 C
ANISOU 1292 CA THR A 190 2358 4162 4446 600 761 -879 C
ATOM 1293 C THR A 190 15.421 -46.539 -44.006 1.00 30.92 C
ANISOU 1293 C THR A 190 2577 4470 4701 693 674 -884 C
ATOM 1294 O THR A 190 15.963 -45.429 -44.021 1.00 28.02 O
ANISOU 1294 O THR A 190 2272 4103 4271 706 664 -853 O
ATOM 1295 CB THR A 190 13.382 -47.255 -45.256 1.00 29.46 C
ANISOU 1295 CB THR A 190 2449 4194 4552 651 787 -850 C
ATOM 1296 OG1 THR A 190 13.834 -46.429 -46.339 1.00 29.94 O
ANISOU 1296 OG1 THR A 190 2585 4213 4578 716 778 -790 O
ATOM 1297 CG2 THR A 190 11.868 -47.301 -45.256 1.00 23.62 C
ANISOU 1297 CG2 THR A 190 1762 3415 3799 566 866 -846 C
ATOM 1298 N VAL A 191 16.098 -47.690 -44.048 1.00 27.44 N
ANISOU 1298 N VAL A 191 2028 4076 4323 761 606 -926 N
ATOM 1299 CA VAL A 191 17.548 -47.707 -44.227 1.00 29.56 C
ANISOU 1299 CA VAL A 191 2255 4394 4582 871 500 -930 C
ATOM 1300 C VAL A 191 17.917 -47.010 -45.528 1.00 30.80 C
ANISOU 1300 C VAL A 191 2500 4501 4702 951 496 -856 C
ATOM 1301 O VAL A 191 18.829 -46.177 -45.576 1.00 27.02 O
ANISOU 1301 O VAL A 191 2112 4024 4131 969 441 -788 O
ATOM 1302 CB VAL A 191 18.074 -49.155 -44.204 1.00 32.98 C
ANISOU 1302 CB VAL A 191 2564 4873 5094 938 418 -981 C
ATOM 1303 CG1 VAL A 191 19.563 -49.190 -44.515 1.00 30.13 C
ANISOU 1303 CG1 VAL A 191 2184 4555 4708 1065 287 -967 C
ATOM 1304 CG2 VAL A 191 17.783 -49.822 -42.873 1.00 28.80 C
ANISOU 1304 CG2 VAL A 191 1943 4397 4603 851 419 -1059 C
ATOM 1305 N ASN A 192 17.195 -47.337 -46.603 1.00 28.82 N
ANISOU 1305 N ASN A 192 2277 4182 4491 968 547 -827 N
ATOM 1306 CA ASN A 192 17.519 -46.792 -47.916 1.00 35.35 C
ANISOU 1306 CA ASN A 192 3189 4948 5295 1042 539 -756 C
ATOM 1307 C ASN A 192 17.207 -45.305 -48.005 1.00 36.95 C
ANISOU 1307 C ASN A 192 3520 5110 5411 969 599 -691 C
ATOM 1308 O ASN A 192 17.830 -44.592 -48.803 1.00 37.26 O
ANISOU 1308 O ASN A 192 3657 5110 5388 1002 570 -605 O
ATOM 1309 CB ASN A 192 16.762 -47.559 -49.000 1.00 41.89 C
ANISOU 1309 CB ASN A 192 4012 5713 6193 1076 578 -755 C
ATOM 1310 CG ASN A 192 17.025 -47.012 -50.387 1.00 46.59 C
ANISOU 1310 CG ASN A 192 4699 6230 6774 1145 571 -686 C
ATOM 1311 OD1 ASN A 192 18.139 -47.107 -50.902 1.00 49.01 O
ANISOU 1311 OD1 ASN A 192 5041 6526 7054 1226 475 -629 O
ATOM 1312 ND2 ASN A 192 15.997 -46.442 -51.005 1.00 45.01 N
ANISOU 1312 ND2 ASN A 192 4569 5963 6569 1095 663 -666 N
ATOM 1313 N ASP A 193 16.258 -44.814 -47.201 1.00 33.91 N
ANISOU 1313 N ASP A 193 3139 4731 5015 869 680 -725 N
ATOM 1314 CA ASP A 193 15.904 -43.399 -47.249 1.00 23.37 C
ANISOU 1314 CA ASP A 193 1911 3361 3608 807 735 -676 C
ATOM 1315 C ASP A 193 17.102 -42.517 -46.932 1.00 24.47 C
ANISOU 1315 C ASP A 193 2114 3532 3650 817 668 -619 C
ATOM 1316 O ASP A 193 17.243 -41.421 -47.488 1.00 23.14 O
ANISOU 1316 O ASP A 193 2044 3330 3420 806 687 -549 O
ATOM 1317 CB ASP A 193 14.769 -43.104 -46.270 1.00 27.19 C
ANISOU 1317 CB ASP A 193 2426 3839 4066 689 789 -691 C
ATOM 1318 CG ASP A 193 13.412 -43.481 -46.819 1.00 38.39 C
ANISOU 1318 CG ASP A 193 3882 5203 5502 647 841 -679 C
ATOM 1319 OD1 ASP A 193 13.313 -43.759 -48.031 1.00 33.84 O
ANISOU 1319 OD1 ASP A 193 3321 4587 4951 703 847 -656 O
ATOM 1320 OD2 ASP A 193 12.442 -43.502 -46.034 1.00 36.76 O
ANISOU 1320 OD2 ASP A 193 3691 4995 5283 561 873 -697 O
ATOM 1321 N LEU A 194 17.975 -42.980 -46.040 1.00 25.20 N
ANISOU 1321 N LEU A 194 2151 3694 3730 837 592 -652 N
ATOM 1322 CA LEU A 194 19.147 -42.233 -45.614 1.00 24.37 C
ANISOU 1322 CA LEU A 194 2103 3631 3527 848 528 -611 C
ATOM 1323 C LEU A 194 20.413 -42.697 -46.316 1.00 26.89 C
ANISOU 1323 C LEU A 194 2435 3960 3820 945 429 -558 C
ATOM 1324 O LEU A 194 21.516 -42.354 -45.877 1.00 28.98 O
ANISOU 1324 O LEU A 194 2734 4274 4003 964 361 -534 O
ATOM 1325 CB LEU A 194 19.308 -42.346 -44.099 1.00 25.17 C
ANISOU 1325 CB LEU A 194 2150 3799 3616 802 502 -684 C
ATOM 1326 CG LEU A 194 18.042 -41.937 -43.343 1.00 26.82 C
ANISOU 1326 CG LEU A 194 2352 3988 3849 705 594 -734 C
ATOM 1327 CD1 LEU A 194 18.210 -42.056 -41.834 1.00 30.62 C
ANISOU 1327 CD1 LEU A 194 2787 4524 4323 655 564 -807 C
ATOM 1328 CD2 LEU A 194 17.637 -40.524 -43.740 1.00 26.48 C
ANISOU 1328 CD2 LEU A 194 2418 3900 3743 668 657 -676 C
ATOM 1329 N GLN A 195 20.271 -43.471 -47.398 1.00 26.23 N
ANISOU 1329 N GLN A 195 2334 3830 3802 1008 419 -540 N
ATOM 1330 CA GLN A 195 21.433 -43.971 -48.124 1.00 28.63 C
ANISOU 1330 CA GLN A 195 2660 4132 4089 1107 318 -487 C
ATOM 1331 C GLN A 195 22.413 -42.853 -48.455 1.00 31.07 C
ANISOU 1331 C GLN A 195 3092 4436 4275 1109 293 -389 C
ATOM 1332 O GLN A 195 23.618 -42.994 -48.226 1.00 30.11 O
ANISOU 1332 O GLN A 195 2991 4361 4090 1159 199 -363 O
ATOM 1333 CB GLN A 195 20.980 -44.681 -49.397 1.00 37.24 C
ANISOU 1333 CB GLN A 195 3741 5147 5262 1168 329 -471 C
ATOM 1334 CG GLN A 195 22.096 -45.363 -50.163 1.00 52.17 C
ANISOU 1334 CG GLN A 195 5649 7023 7149 1281 216 -422 C
ATOM 1335 CD GLN A 195 21.598 -45.982 -51.446 1.00 69.99 C
ANISOU 1335 CD GLN A 195 7909 9194 9490 1343 230 -410 C
ATOM 1336 OE1 GLN A 195 20.633 -45.503 -52.038 1.00 75.54 O
ANISOU 1336 OE1 GLN A 195 8651 9834 10215 1296 324 -400 O
ATOM 1337 NE2 GLN A 195 22.246 -47.052 -51.881 1.00 71.86 N
ANISOU 1337 NE2 GLN A 195 8104 9425 9773 1452 131 -415 N
ATOM 1338 N PHE A 196 21.911 -41.724 -48.968 1.00 27.68 N
ANISOU 1338 N PHE A 196 2748 3960 3811 1053 377 -336 N
ATOM 1339 CA PHE A 196 22.794 -40.643 -49.399 1.00 26.75 C
ANISOU 1339 CA PHE A 196 2743 3838 3583 1048 369 -241 C
ATOM 1340 C PHE A 196 23.722 -40.183 -48.280 1.00 27.82 C
ANISOU 1340 C PHE A 196 2890 4062 3620 1035 324 -253 C
ATOM 1341 O PHE A 196 24.908 -39.924 -48.516 1.00 28.04 O
ANISOU 1341 O PHE A 196 2986 4112 3557 1073 265 -186 O
ATOM 1342 CB PHE A 196 21.983 -39.454 -49.913 1.00 26.40 C
ANISOU 1342 CB PHE A 196 2763 3743 3525 975 472 -204 C
ATOM 1343 CG PHE A 196 22.757 -38.163 -49.921 1.00 28.05 C
ANISOU 1343 CG PHE A 196 3062 3976 3618 943 485 -133 C
ATOM 1344 CD1 PHE A 196 23.732 -37.930 -50.878 1.00 28.31 C
ANISOU 1344 CD1 PHE A 196 3181 3984 3591 979 450 -34 C
ATOM 1345 CD2 PHE A 196 22.518 -37.189 -48.965 1.00 26.92 C
ANISOU 1345 CD2 PHE A 196 2920 3883 3426 877 534 -166 C
ATOM 1346 CE1 PHE A 196 24.451 -36.747 -50.886 1.00 30.18 C
ANISOU 1346 CE1 PHE A 196 3497 4253 3719 943 473 30 C
ATOM 1347 CE2 PHE A 196 23.235 -36.003 -48.967 1.00 32.22 C
ANISOU 1347 CE2 PHE A 196 3665 4586 3993 852 553 -109 C
ATOM 1348 CZ PHE A 196 24.202 -35.782 -49.929 1.00 32.51 C
ANISOU 1348 CZ PHE A 196 3781 4605 3968 881 527 -12 C
ATOM 1349 N LEU A 197 23.199 -40.055 -47.059 1.00 30.32 N
ANISOU 1349 N LEU A 197 3147 4425 3948 980 353 -335 N
ATOM 1350 CA LEU A 197 24.029 -39.594 -45.952 1.00 30.53 C
ANISOU 1350 CA LEU A 197 3186 4531 3883 967 312 -357 C
ATOM 1351 C LEU A 197 24.994 -40.679 -45.496 1.00 32.16 C
ANISOU 1351 C LEU A 197 3342 4792 4086 1035 193 -389 C
ATOM 1352 O LEU A 197 26.130 -40.382 -45.108 1.00 26.71 O
ANISOU 1352 O LEU A 197 2698 4157 3294 1060 129 -367 O
ATOM 1353 CB LEU A 197 23.151 -39.131 -44.791 1.00 26.62 C
ANISOU 1353 CB LEU A 197 2652 4056 3406 888 373 -437 C
ATOM 1354 CG LEU A 197 22.655 -37.693 -44.946 1.00 31.02 C
ANISOU 1354 CG LEU A 197 3282 4589 3916 827 465 -402 C
ATOM 1355 CD1 LEU A 197 21.792 -37.299 -43.773 1.00 32.73 C
ANISOU 1355 CD1 LEU A 197 3466 4817 4153 759 512 -482 C
ATOM 1356 CD2 LEU A 197 23.842 -36.754 -45.076 1.00 30.30 C
ANISOU 1356 CD2 LEU A 197 3275 4537 3698 844 444 -336 C
ATOM 1357 N ARG A 198 24.552 -41.939 -45.539 1.00 33.96 N
ANISOU 1357 N ARG A 198 3471 5009 4424 1068 162 -444 N
ATOM 1358 CA ARG A 198 25.444 -43.056 -45.254 1.00 31.06 C
ANISOU 1358 CA ARG A 198 3044 4690 4069 1143 39 -474 C
ATOM 1359 C ARG A 198 26.622 -43.071 -46.220 1.00 36.05 C
ANISOU 1359 C ARG A 198 3764 5306 4627 1228 -41 -376 C
ATOM 1360 O ARG A 198 27.766 -43.302 -45.814 1.00 40.31 O
ANISOU 1360 O ARG A 198 4320 5903 5094 1276 -145 -371 O
ATOM 1361 CB ARG A 198 24.660 -44.369 -45.327 1.00 33.33 C
ANISOU 1361 CB ARG A 198 3203 4962 4499 1166 35 -548 C
ATOM 1362 CG ARG A 198 25.394 -45.594 -44.797 1.00 28.36 C
ANISOU 1362 CG ARG A 198 2476 4393 3906 1232 -89 -608 C
ATOM 1363 CD ARG A 198 24.475 -46.815 -44.711 1.00 28.67 C
ANISOU 1363 CD ARG A 198 2369 4430 4094 1236 -70 -697 C
ATOM 1364 NE ARG A 198 23.424 -46.669 -43.703 1.00 34.39 N
ANISOU 1364 NE ARG A 198 3030 5172 4864 1129 21 -778 N
ATOM 1365 CZ ARG A 198 22.142 -46.445 -43.984 1.00 35.67 C
ANISOU 1365 CZ ARG A 198 3189 5282 5082 1069 143 -788 C
ATOM 1366 NH1 ARG A 198 21.746 -46.344 -45.245 1.00 32.92 N
ANISOU 1366 NH1 ARG A 198 2891 4864 4755 1104 189 -729 N
ATOM 1367 NH2 ARG A 198 21.254 -46.329 -43.006 1.00 34.67 N
ANISOU 1367 NH2 ARG A 198 3015 5170 4987 972 216 -856 N
ATOM 1368 N GLU A 199 26.360 -42.808 -47.504 1.00 39.41 N
ANISOU 1368 N GLU A 199 4256 5652 5066 1243 5 -296 N
ATOM 1369 CA GLU A 199 27.436 -42.791 -48.491 1.00 46.93 C
ANISOU 1369 CA GLU A 199 5307 6575 5948 1316 -66 -193 C
ATOM 1370 C GLU A 199 28.374 -41.613 -48.262 1.00 42.24 C
ANISOU 1370 C GLU A 199 4827 6022 5201 1285 -62 -125 C
ATOM 1371 O GLU A 199 29.587 -41.728 -48.476 1.00 47.37 O
ANISOU 1371 O GLU A 199 5546 6692 5760 1344 -152 -65 O
ATOM 1372 CB GLU A 199 26.860 -42.730 -49.908 1.00 55.24 C
ANISOU 1372 CB GLU A 199 6409 7523 7057 1327 -11 -127 C
ATOM 1373 CG GLU A 199 25.734 -43.703 -50.202 1.00 58.45 C
ANISOU 1373 CG GLU A 199 6712 7885 7612 1346 17 -197 C
ATOM 1374 CD GLU A 199 26.207 -44.985 -50.846 1.00 64.08 C
ANISOU 1374 CD GLU A 199 7389 8570 8390 1461 -89 -195 C
ATOM 1375 OE1 GLU A 199 27.436 -45.190 -50.939 1.00 68.04 O
ANISOU 1375 OE1 GLU A 199 7942 9092 8819 1530 -199 -144 O
ATOM 1376 OE2 GLU A 199 25.344 -45.785 -51.265 1.00 66.44 O
ANISOU 1376 OE2 GLU A 199 7610 8827 8808 1488 -63 -247 O
ATOM 1377 N ASN A 200 27.832 -40.476 -47.821 1.00 39.74 N
ANISOU 1377 N ASN A 200 4532 5719 4849 1195 42 -136 N
ATOM 1378 CA ASN A 200 28.553 -39.207 -47.766 1.00 40.69 C
ANISOU 1378 CA ASN A 200 4758 5872 4831 1158 75 -71 C
ATOM 1379 C ASN A 200 28.631 -38.733 -46.320 1.00 43.69 C
ANISOU 1379 C ASN A 200 5105 6336 5159 1114 83 -152 C
ATOM 1380 O ASN A 200 27.874 -37.840 -45.908 1.00 39.01 O
ANISOU 1380 O ASN A 200 4506 5744 4571 1041 177 -182 O
ATOM 1381 CB ASN A 200 27.872 -38.162 -48.647 1.00 35.66 C
ANISOU 1381 CB ASN A 200 4180 5171 4200 1096 191 -9 C
ATOM 1382 CG ASN A 200 27.746 -38.610 -50.088 1.00 36.35 C
ANISOU 1382 CG ASN A 200 4306 5162 4343 1135 184 67 C
ATOM 1383 OD1 ASN A 200 28.550 -38.234 -50.935 1.00 36.95 O
ANISOU 1383 OD1 ASN A 200 4484 5212 4344 1151 169 169 O
ATOM 1384 ND2 ASN A 200 26.730 -39.418 -50.373 1.00 30.02 N
ANISOU 1384 ND2 ASN A 200 3428 4307 3672 1148 196 16 N
ATOM 1385 N PRO A 201 29.541 -39.298 -45.519 1.00 47.87 N
ANISOU 1385 N PRO A 201 5616 6935 5637 1158 -21 -192 N
ATOM 1386 CA PRO A 201 29.667 -38.854 -44.122 1.00 44.65 C
ANISOU 1386 CA PRO A 201 5184 6602 5177 1118 -21 -274 C
ATOM 1387 C PRO A 201 30.236 -37.453 -43.968 1.00 43.17 C
ANISOU 1387 C PRO A 201 5097 6453 4852 1082 36 -230 C
ATOM 1388 O PRO A 201 30.160 -36.893 -42.866 1.00 46.61 O
ANISOU 1388 O PRO A 201 5518 6939 5251 1042 57 -301 O
ATOM 1389 CB PRO A 201 30.604 -39.901 -43.508 1.00 40.60 C
ANISOU 1389 CB PRO A 201 4634 6148 4644 1185 -162 -318 C
ATOM 1390 CG PRO A 201 31.418 -40.382 -44.661 1.00 41.92 C
ANISOU 1390 CG PRO A 201 4864 6285 4777 1264 -232 -220 C
ATOM 1391 CD PRO A 201 30.504 -40.363 -45.851 1.00 41.53 C
ANISOU 1391 CD PRO A 201 4817 6142 4822 1252 -151 -166 C
ATOM 1392 N GLN A 202 30.798 -36.867 -45.025 1.00 33.17 N
ANISOU 1392 N GLN A 202 3929 5165 3509 1093 63 -119 N
ATOM 1393 CA GLN A 202 31.362 -35.525 -44.954 1.00 32.66 C
ANISOU 1393 CA GLN A 202 3953 5144 3313 1056 127 -76 C
ATOM 1394 C GLN A 202 30.309 -34.429 -45.051 1.00 38.04 C
ANISOU 1394 C GLN A 202 4623 5795 4036 979 258 -84 C
ATOM 1395 O GLN A 202 30.609 -33.276 -44.729 1.00 41.36 O
ANISOU 1395 O GLN A 202 5088 6262 4364 944 319 -79 O
ATOM 1396 CB GLN A 202 32.399 -35.330 -46.066 1.00 32.85 C
ANISOU 1396 CB GLN A 202 4089 5156 3237 1088 110 52 C
ATOM 1397 CG GLN A 202 31.813 -35.263 -47.478 1.00 39.35 C
ANISOU 1397 CG GLN A 202 4938 5881 4134 1072 167 138 C
ATOM 1398 CD GLN A 202 31.322 -36.608 -47.979 1.00 48.21 C
ANISOU 1398 CD GLN A 202 5999 6934 5386 1126 99 126 C
ATOM 1399 OE1 GLN A 202 31.456 -37.622 -47.298 1.00 53.04 O
ANISOU 1399 OE1 GLN A 202 6543 7575 6035 1175 6 56 O
ATOM 1400 NE2 GLN A 202 30.752 -36.621 -49.178 1.00 46.16 N
ANISOU 1400 NE2 GLN A 202 5760 6582 5197 1117 144 189 N
ATOM 1401 N VAL A 203 29.096 -34.759 -45.487 1.00 37.85 N
ANISOU 1401 N VAL A 203 4539 5696 4145 956 301 -100 N
ATOM 1402 CA VAL A 203 28.058 -33.754 -45.675 1.00 32.54 C
ANISOU 1402 CA VAL A 203 3860 4988 3514 888 415 -103 C
ATOM 1403 C VAL A 203 27.545 -33.285 -44.321 1.00 28.92 C
ANISOU 1403 C VAL A 203 3355 4573 3061 850 441 -207 C
ATOM 1404 O VAL A 203 27.169 -34.097 -43.466 1.00 31.08 O
ANISOU 1404 O VAL A 203 3560 4853 3396 857 394 -290 O
ATOM 1405 CB VAL A 203 26.913 -34.320 -46.529 1.00 31.38 C
ANISOU 1405 CB VAL A 203 3673 4750 3502 878 444 -94 C
ATOM 1406 CG1 VAL A 203 25.734 -33.353 -46.565 1.00 28.41 C
ANISOU 1406 CG1 VAL A 203 3283 4339 3172 808 549 -114 C
ATOM 1407 CG2 VAL A 203 27.401 -34.637 -47.930 1.00 28.28 C
ANISOU 1407 CG2 VAL A 203 3340 4301 3103 913 424 11 C
ATOM 1408 N ASN A 204 27.527 -31.969 -44.121 1.00 31.93 N
ANISOU 1408 N ASN A 204 3771 4981 3378 810 515 -203 N
ATOM 1409 CA ASN A 204 26.870 -31.361 -42.967 1.00 34.41 C
ANISOU 1409 CA ASN A 204 4049 5317 3708 774 551 -296 C
ATOM 1410 C ASN A 204 25.434 -31.039 -43.364 1.00 35.13 C
ANISOU 1410 C ASN A 204 4108 5334 3906 726 626 -303 C
ATOM 1411 O ASN A 204 25.198 -30.153 -44.191 1.00 40.74 O
ANISOU 1411 O ASN A 204 4849 6022 4608 699 695 -246 O
ATOM 1412 CB ASN A 204 27.614 -30.108 -42.508 1.00 30.33 C
ANISOU 1412 CB ASN A 204 3582 4872 3068 767 588 -298 C
ATOM 1413 CG ASN A 204 27.061 -29.541 -41.208 1.00 49.68 C
ANISOU 1413 CG ASN A 204 6003 7343 5530 743 607 -402 C
ATOM 1414 OD1 ASN A 204 26.386 -30.246 -40.458 1.00 56.67 O
ANISOU 1414 OD1 ASN A 204 6837 8200 6495 735 571 -475 O
ATOM 1415 ND2 ASN A 204 27.345 -28.267 -40.936 1.00 53.21 N
ANISOU 1415 ND2 ASN A 204 6481 7837 5899 732 664 -411 N
ATOM 1416 N LEU A 205 24.476 -31.761 -42.784 1.00 29.68 N
ANISOU 1416 N LEU A 205 3356 4607 3313 711 612 -374 N
ATOM 1417 CA LEU A 205 23.072 -31.585 -43.127 1.00 27.52 C
ANISOU 1417 CA LEU A 205 3058 4262 3135 667 676 -383 C
ATOM 1418 C LEU A 205 22.215 -31.581 -41.872 1.00 27.09 C
ANISOU 1418 C LEU A 205 2966 4202 3126 634 681 -480 C
ATOM 1419 O LEU A 205 22.434 -32.375 -40.954 1.00 31.59 O
ANISOU 1419 O LEU A 205 3500 4796 3708 643 624 -541 O
ATOM 1420 CB LEU A 205 22.581 -32.691 -44.075 1.00 24.59 C
ANISOU 1420 CB LEU A 205 2660 3829 2854 681 664 -352 C
ATOM 1421 CG LEU A 205 21.169 -32.487 -44.622 1.00 30.00 C
ANISOU 1421 CG LEU A 205 3334 4439 3627 638 733 -353 C
ATOM 1422 CD1 LEU A 205 21.136 -31.293 -45.565 1.00 32.62 C
ANISOU 1422 CD1 LEU A 205 3720 4752 3925 617 793 -284 C
ATOM 1423 CD2 LEU A 205 20.662 -33.744 -45.314 1.00 31.78 C
ANISOU 1423 CD2 LEU A 205 3522 4610 3943 657 716 -348 C
ATOM 1424 N SER A 206 21.238 -30.683 -41.847 1.00 22.13 N
ANISOU 1424 N SER A 206 2348 3537 2524 593 747 -491 N
ATOM 1425 CA SER A 206 20.238 -30.617 -40.793 1.00 22.18 C
ANISOU 1425 CA SER A 206 2332 3516 2579 555 759 -571 C
ATOM 1426 C SER A 206 18.874 -30.961 -41.372 1.00 27.62 C
ANISOU 1426 C SER A 206 3005 4127 3363 520 803 -564 C
ATOM 1427 O SER A 206 18.549 -30.549 -42.490 1.00 32.63 O
ANISOU 1427 O SER A 206 3660 4728 4010 516 844 -505 O
ATOM 1428 CB SER A 206 20.203 -29.227 -40.153 1.00 18.64 C
ANISOU 1428 CB SER A 206 1917 3088 2076 544 789 -599 C
ATOM 1429 OG SER A 206 21.403 -28.968 -39.453 1.00 26.83 O
ANISOU 1429 OG SER A 206 2970 4200 3024 576 750 -623 O
ATOM 1430 N LEU A 207 18.083 -31.720 -40.615 1.00 20.86 N
ANISOU 1430 N LEU A 207 2114 3241 2569 491 795 -626 N
ATOM 1431 CA LEU A 207 16.764 -32.157 -41.056 1.00 18.52 C
ANISOU 1431 CA LEU A 207 1816 2865 2355 452 828 -612 C
ATOM 1432 C LEU A 207 15.722 -31.720 -40.034 1.00 21.14 C
ANISOU 1432 C LEU A 207 2187 3144 2702 396 825 -636 C
ATOM 1433 O LEU A 207 15.855 -32.016 -38.841 1.00 20.70 O
ANISOU 1433 O LEU A 207 2111 3109 2646 381 800 -705 O
ATOM 1434 CB LEU A 207 16.716 -33.684 -41.242 1.00 18.64 C
ANISOU 1434 CB LEU A 207 1760 2886 2435 465 815 -641 C
ATOM 1435 CG LEU A 207 17.442 -34.296 -42.452 1.00 27.27 C
ANISOU 1435 CG LEU A 207 2842 3988 3532 519 791 -580 C
ATOM 1436 CD1 LEU A 207 17.516 -35.819 -42.356 1.00 21.02 C
ANISOU 1436 CD1 LEU A 207 1977 3205 2805 538 753 -614 C
ATOM 1437 CD2 LEU A 207 16.781 -33.877 -43.759 1.00 29.06 C
ANISOU 1437 CD2 LEU A 207 3104 4156 3782 514 846 -521 C
ATOM 1438 N ASP A 208 14.691 -31.014 -40.495 1.00 16.36 N
ANISOU 1438 N ASP A 208 1633 2478 2104 370 842 -588 N
ATOM 1439 CA ASP A 208 13.547 -30.670 -39.657 1.00 20.46 C
ANISOU 1439 CA ASP A 208 2189 2947 2639 322 835 -611 C
ATOM 1440 C ASP A 208 12.398 -31.590 -40.049 1.00 25.33 C
ANISOU 1440 C ASP A 208 2799 3514 3311 285 848 -604 C
ATOM 1441 O ASP A 208 11.828 -31.455 -41.137 1.00 28.40 O
ANISOU 1441 O ASP A 208 3207 3875 3708 285 858 -555 O
ATOM 1442 CB ASP A 208 13.159 -29.201 -39.809 1.00 17.95 C
ANISOU 1442 CB ASP A 208 1926 2608 2285 324 832 -578 C
ATOM 1443 CG ASP A 208 12.231 -28.723 -38.702 1.00 26.90 C
ANISOU 1443 CG ASP A 208 3096 3699 3425 288 820 -618 C
ATOM 1444 OD1 ASP A 208 11.504 -29.556 -38.118 1.00 25.89 O
ANISOU 1444 OD1 ASP A 208 2963 3538 3337 246 826 -654 O
ATOM 1445 OD2 ASP A 208 12.224 -27.511 -38.414 1.00 31.71 O
ANISOU 1445 OD2 ASP A 208 3738 4307 4002 303 810 -616 O
ATOM 1446 N MET A 209 12.067 -32.526 -39.162 1.00 22.90 N
ANISOU 1446 N MET A 209 2461 3199 3042 249 850 -659 N
ATOM 1447 CA MET A 209 11.042 -33.530 -39.411 1.00 18.35 C
ANISOU 1447 CA MET A 209 1870 2584 2517 209 871 -661 C
ATOM 1448 C MET A 209 9.751 -33.253 -38.655 1.00 21.56 C
ANISOU 1448 C MET A 209 2324 2933 2934 145 887 -683 C
ATOM 1449 O MET A 209 8.866 -34.115 -38.631 1.00 26.73 O
ANISOU 1449 O MET A 209 2969 3559 3629 101 914 -696 O
ATOM 1450 CB MET A 209 11.558 -34.919 -39.035 1.00 25.39 C
ANISOU 1450 CB MET A 209 2678 3514 3455 208 872 -712 C
ATOM 1451 CG MET A 209 12.802 -35.361 -39.779 1.00 30.45 C
ANISOU 1451 CG MET A 209 3265 4210 4094 277 855 -700 C
ATOM 1452 SD MET A 209 12.535 -35.592 -41.543 1.00 37.63 S
ANISOU 1452 SD MET A 209 4187 5093 5018 314 872 -627 S
ATOM 1453 CE MET A 209 14.042 -36.446 -41.988 1.00 50.48 C
ANISOU 1453 CE MET A 209 5729 6787 6663 392 851 -645 C
ATOM 1454 N SER A 210 9.619 -32.075 -38.048 1.00 17.23 N
ANISOU 1454 N SER A 210 1828 2368 2351 142 875 -689 N
ATOM 1455 CA SER A 210 8.494 -31.798 -37.164 1.00 20.61 C
ANISOU 1455 CA SER A 210 2303 2739 2788 85 891 -720 C
ATOM 1456 C SER A 210 7.161 -31.983 -37.884 1.00 19.05 C
ANISOU 1456 C SER A 210 2141 2488 2608 51 918 -686 C
ATOM 1457 O SER A 210 7.057 -31.818 -39.101 1.00 21.92 O
ANISOU 1457 O SER A 210 2511 2852 2965 78 911 -634 O
ATOM 1458 CB SER A 210 8.599 -30.375 -36.611 1.00 18.17 C
ANISOU 1458 CB SER A 210 2046 2420 2437 107 867 -726 C
ATOM 1459 OG SER A 210 9.859 -30.162 -35.996 1.00 17.81 O
ANISOU 1459 OG SER A 210 1973 2427 2366 143 842 -760 O
ATOM 1460 N LEU A 211 6.140 -32.359 -37.113 1.00 17.20 N
ANISOU 1460 N LEU A 211 1933 2205 2396 -14 953 -721 N
ATOM 1461 CA LEU A 211 4.760 -32.456 -37.598 1.00 18.39 C
ANISOU 1461 CA LEU A 211 2134 2300 2555 -54 984 -698 C
ATOM 1462 C LEU A 211 4.627 -33.434 -38.767 1.00 20.65 C
ANISOU 1462 C LEU A 211 2382 2601 2864 -44 997 -668 C
ATOM 1463 O LEU A 211 3.826 -33.230 -39.683 1.00 22.23 O
ANISOU 1463 O LEU A 211 2619 2770 3056 -44 1003 -634 O
ATOM 1464 CB LEU A 211 4.216 -31.077 -37.974 1.00 15.06 C
ANISOU 1464 CB LEU A 211 1781 1845 2098 -32 963 -666 C
ATOM 1465 CG LEU A 211 4.153 -30.090 -36.807 1.00 19.15 C
ANISOU 1465 CG LEU A 211 2347 2336 2593 -36 950 -700 C
ATOM 1466 CD1 LEU A 211 4.009 -28.672 -37.322 1.00 22.91 C
ANISOU 1466 CD1 LEU A 211 2863 2805 3038 10 915 -669 C
ATOM 1467 CD2 LEU A 211 3.006 -30.442 -35.871 1.00 17.61 C
ANISOU 1467 CD2 LEU A 211 2209 2074 2409 -109 998 -737 C
ATOM 1468 N ASN A 212 5.424 -34.511 -38.734 1.00 15.99 N
ANISOU 1468 N ASN A 212 1715 2058 2303 -33 998 -689 N
ATOM 1469 CA ASN A 212 5.226 -35.636 -39.638 1.00 18.27 C
ANISOU 1469 CA ASN A 212 1963 2357 2622 -27 1016 -676 C
ATOM 1470 C ASN A 212 4.710 -36.839 -38.855 1.00 23.62 C
ANISOU 1470 C ASN A 212 2600 3031 3341 -90 1062 -728 C
ATOM 1471 O ASN A 212 5.221 -37.137 -37.768 1.00 21.88 O
ANISOU 1471 O ASN A 212 2338 2834 3140 -115 1066 -779 O
ATOM 1472 CB ASN A 212 6.516 -36.024 -40.370 1.00 16.33 C
ANISOU 1472 CB ASN A 212 1654 2169 2383 43 984 -660 C
ATOM 1473 CG ASN A 212 6.792 -35.139 -41.576 1.00 21.82 C
ANISOU 1473 CG ASN A 212 2384 2861 3045 96 958 -603 C
ATOM 1474 OD1 ASN A 212 6.250 -35.359 -42.660 1.00 19.52 O
ANISOU 1474 OD1 ASN A 212 2108 2548 2762 104 967 -576 O
ATOM 1475 ND2 ASN A 212 7.645 -34.139 -41.394 1.00 15.54 N
ANISOU 1475 ND2 ASN A 212 1600 2089 2215 128 929 -590 N
ATOM 1476 N PRO A 213 3.692 -37.539 -39.370 1.00 17.17 N
ANISOU 1476 N PRO A 213 1794 2189 2541 -119 1101 -723 N
ATOM 1477 CA PRO A 213 3.085 -38.667 -38.637 1.00 19.59 C
ANISOU 1477 CA PRO A 213 2064 2493 2885 -188 1156 -773 C
ATOM 1478 C PRO A 213 3.944 -39.928 -38.673 1.00 19.36 C
ANISOU 1478 C PRO A 213 1924 2527 2906 -164 1150 -805 C
ATOM 1479 O PRO A 213 3.527 -40.987 -39.146 1.00 26.96 O
ANISOU 1479 O PRO A 213 2845 3500 3898 -169 1179 -815 O
ATOM 1480 CB PRO A 213 1.745 -38.839 -39.364 1.00 19.60 C
ANISOU 1480 CB PRO A 213 2123 2450 2874 -213 1196 -750 C
ATOM 1481 CG PRO A 213 2.032 -38.412 -40.764 1.00 19.75 C
ANISOU 1481 CG PRO A 213 2155 2474 2875 -138 1154 -700 C
ATOM 1482 CD PRO A 213 3.046 -37.303 -40.673 1.00 16.82 C
ANISOU 1482 CD PRO A 213 1795 2119 2479 -92 1099 -677 C
ATOM 1483 N ILE A 214 5.162 -39.815 -38.146 1.00 18.63 N
ANISOU 1483 N ILE A 214 1778 2478 2822 -135 1112 -827 N
ATOM 1484 CA ILE A 214 6.105 -40.928 -38.157 1.00 23.76 C
ANISOU 1484 CA ILE A 214 2316 3192 3520 -104 1095 -861 C
ATOM 1485 C ILE A 214 5.638 -42.004 -37.184 1.00 23.84 C
ANISOU 1485 C ILE A 214 2263 3213 3583 -184 1141 -928 C
ATOM 1486 O ILE A 214 5.423 -41.736 -35.995 1.00 24.92 O
ANISOU 1486 O ILE A 214 2412 3333 3722 -255 1164 -970 O
ATOM 1487 CB ILE A 214 7.519 -40.444 -37.811 1.00 21.63 C
ANISOU 1487 CB ILE A 214 2012 2968 3239 -53 1039 -873 C
ATOM 1488 CG1 ILE A 214 8.067 -39.555 -38.933 1.00 22.51 C
ANISOU 1488 CG1 ILE A 214 2173 3078 3303 28 1001 -805 C
ATOM 1489 CG2 ILE A 214 8.441 -41.621 -37.541 1.00 20.01 C
ANISOU 1489 CG2 ILE A 214 1683 2831 3091 -32 1019 -927 C
ATOM 1490 CD1 ILE A 214 9.332 -38.814 -38.566 1.00 23.74 C
ANISOU 1490 CD1 ILE A 214 2321 3272 3429 73 956 -810 C
ATOM 1491 N ASP A 215 5.485 -43.233 -37.684 1.00 20.90 N
ANISOU 1491 N ASP A 215 1818 2868 3253 -174 1159 -942 N
ATOM 1492 CA ASP A 215 5.162 -44.370 -36.836 1.00 28.45 C
ANISOU 1492 CA ASP A 215 2695 3849 4267 -246 1201 -1007 C
ATOM 1493 C ASP A 215 6.057 -45.583 -37.058 1.00 25.37 C
ANISOU 1493 C ASP A 215 2171 3530 3937 -197 1171 -1044 C
ATOM 1494 O ASP A 215 5.839 -46.614 -36.411 1.00 30.14 O
ANISOU 1494 O ASP A 215 2693 4162 4595 -253 1201 -1102 O
ATOM 1495 CB ASP A 215 3.692 -44.786 -37.024 1.00 31.35 C
ANISOU 1495 CB ASP A 215 3110 4173 4629 -307 1274 -1001 C
ATOM 1496 CG ASP A 215 3.342 -45.095 -38.472 1.00 43.03 C
ANISOU 1496 CG ASP A 215 4604 5649 6097 -240 1274 -957 C
ATOM 1497 OD1 ASP A 215 4.064 -45.884 -39.114 1.00 49.09 O
ANISOU 1497 OD1 ASP A 215 5287 6464 6900 -171 1246 -964 O
ATOM 1498 OD2 ASP A 215 2.321 -44.566 -38.960 1.00 45.53 O
ANISOU 1498 OD2 ASP A 215 5016 5912 6369 -256 1303 -920 O
ATOM 1499 N PHE A 216 7.050 -45.503 -37.945 1.00 27.94 N
ANISOU 1499 N PHE A 216 2473 3885 4259 -96 1112 -1015 N
ATOM 1500 CA PHE A 216 7.929 -46.643 -38.194 1.00 27.56 C
ANISOU 1500 CA PHE A 216 2299 3902 4271 -39 1075 -1050 C
ATOM 1501 C PHE A 216 9.294 -46.154 -38.651 1.00 31.81 C
ANISOU 1501 C PHE A 216 2824 4471 4792 57 1000 -1028 C
ATOM 1502 O PHE A 216 9.398 -45.417 -39.636 1.00 27.05 O
ANISOU 1502 O PHE A 216 2297 3839 4143 116 989 -963 O
ATOM 1503 CB PHE A 216 7.328 -47.589 -39.240 1.00 23.91 C
ANISOU 1503 CB PHE A 216 1813 3438 3834 -5 1106 -1037 C
ATOM 1504 CG PHE A 216 8.175 -48.799 -39.520 1.00 29.79 C
ANISOU 1504 CG PHE A 216 2426 4246 4646 60 1067 -1077 C
ATOM 1505 CD1 PHE A 216 8.452 -49.713 -38.513 1.00 32.65 C
ANISOU 1505 CD1 PHE A 216 2673 4660 5071 14 1061 -1151 C
ATOM 1506 CD2 PHE A 216 8.685 -49.030 -40.786 1.00 30.88 C
ANISOU 1506 CD2 PHE A 216 2554 4389 4789 165 1035 -1043 C
ATOM 1507 CE1 PHE A 216 9.228 -50.825 -38.765 1.00 32.04 C
ANISOU 1507 CE1 PHE A 216 2470 4644 5060 79 1015 -1191 C
ATOM 1508 CE2 PHE A 216 9.462 -50.144 -41.043 1.00 30.18 C
ANISOU 1508 CE2 PHE A 216 2346 4354 4767 233 992 -1081 C
ATOM 1509 CZ PHE A 216 9.734 -51.041 -40.033 1.00 30.86 C
ANISOU 1509 CZ PHE A 216 2315 4497 4915 192 979 -1155 C
ATOM 1510 N ILE A 217 10.335 -46.569 -37.936 1.00 31.66 N
ANISOU 1510 N ILE A 217 2706 4513 4809 71 949 -1085 N
ATOM 1511 CA ILE A 217 11.717 -46.368 -38.350 1.00 27.87 C
ANISOU 1511 CA ILE A 217 2191 4076 4321 170 872 -1077 C
ATOM 1512 C ILE A 217 12.343 -47.747 -38.505 1.00 32.00 C
ANISOU 1512 C ILE A 217 2579 4660 4919 220 827 -1125 C
ATOM 1513 O ILE A 217 12.335 -48.543 -37.559 1.00 25.75 O
ANISOU 1513 O ILE A 217 1693 3909 4182 166 821 -1197 O
ATOM 1514 CB ILE A 217 12.501 -45.511 -37.339 1.00 30.42 C
ANISOU 1514 CB ILE A 217 2521 4426 4609 155 832 -1110 C
ATOM 1515 CG1 ILE A 217 11.869 -44.123 -37.196 1.00 31.40 C
ANISOU 1515 CG1 ILE A 217 2781 4488 4661 113 873 -1063 C
ATOM 1516 CG2 ILE A 217 13.958 -45.385 -37.756 1.00 29.47 C
ANISOU 1516 CG2 ILE A 217 2361 4363 4474 262 748 -1108 C
ATOM 1517 CD1 ILE A 217 12.634 -43.184 -36.288 1.00 38.28 C
ANISOU 1517 CD1 ILE A 217 3670 5384 5490 110 838 -1096 C
ATOM 1518 N GLN A 218 12.871 -48.029 -39.694 1.00 33.23 N
ANISOU 1518 N GLN A 218 2724 4821 5082 322 793 -1087 N
ATOM 1519 CA GLN A 218 13.390 -49.360 -39.979 1.00 31.21 C
ANISOU 1519 CA GLN A 218 2345 4615 4900 383 747 -1128 C
ATOM 1520 C GLN A 218 14.565 -49.692 -39.064 1.00 34.45 C
ANISOU 1520 C GLN A 218 2650 5102 5338 403 656 -1195 C
ATOM 1521 O GLN A 218 15.295 -48.810 -38.601 1.00 32.06 O
ANISOU 1521 O GLN A 218 2377 4818 4987 413 613 -1197 O
ATOM 1522 CB GLN A 218 13.822 -49.461 -41.445 1.00 31.47 C
ANISOU 1522 CB GLN A 218 2398 4628 4932 499 720 -1074 C
ATOM 1523 CG GLN A 218 14.170 -50.881 -41.886 1.00 31.24 C
ANISOU 1523 CG GLN A 218 2252 4637 4982 568 678 -1111 C
ATOM 1524 CD GLN A 218 14.496 -50.986 -43.362 1.00 33.42 C
ANISOU 1524 CD GLN A 218 2557 4879 5262 682 656 -1060 C
ATOM 1525 OE1 GLN A 218 14.724 -49.982 -44.034 1.00 35.58 O
ANISOU 1525 OE1 GLN A 218 2927 5112 5480 718 658 -998 O
ATOM 1526 NE2 GLN A 218 14.518 -52.210 -43.876 1.00 38.13 N
ANISOU 1526 NE2 GLN A 218 3069 5492 5927 740 637 -1088 N
ATOM 1527 N ASP A 219 14.733 -50.987 -38.801 1.00 40.08 N
ANISOU 1527 N ASP A 219 3236 5862 6128 410 623 -1256 N
ATOM 1528 CA ASP A 219 15.853 -51.469 -38.004 1.00 42.06 C
ANISOU 1528 CA ASP A 219 3375 6192 6413 435 520 -1325 C
ATOM 1529 C ASP A 219 17.169 -51.037 -38.638 1.00 45.03 C
ANISOU 1529 C ASP A 219 3764 6596 6750 563 418 -1294 C
ATOM 1530 O ASP A 219 17.433 -51.340 -39.806 1.00 41.90 O
ANISOU 1530 O ASP A 219 3377 6182 6363 660 395 -1250 O
ATOM 1531 CB ASP A 219 15.780 -52.992 -37.889 1.00 48.21 C
ANISOU 1531 CB ASP A 219 4020 7013 7286 438 500 -1384 C
ATOM 1532 CG ASP A 219 16.517 -53.530 -36.677 1.00 61.67 C
ANISOU 1532 CG ASP A 219 5607 8792 9033 408 417 -1472 C
ATOM 1533 OD1 ASP A 219 16.025 -53.341 -35.546 1.00 69.34 O
ANISOU 1533 OD1 ASP A 219 6572 9764 10009 290 460 -1516 O
ATOM 1534 OD2 ASP A 219 17.583 -54.156 -36.855 1.00 67.40 O
ANISOU 1534 OD2 ASP A 219 6248 9574 9788 501 303 -1498 O
ATOM 1535 N GLN A 220 17.976 -50.302 -37.869 1.00 47.96 N
ANISOU 1535 N GLN A 220 4142 7008 7073 563 357 -1319 N
ATOM 1536 CA GLN A 220 19.305 -49.834 -38.259 1.00 45.39 C
ANISOU 1536 CA GLN A 220 3829 6726 6693 681 251 -1298 C
ATOM 1537 C GLN A 220 19.277 -48.776 -39.356 1.00 40.79 C
ANISOU 1537 C GLN A 220 3392 6079 6028 728 290 -1195 C
ATOM 1538 O GLN A 220 20.275 -48.595 -40.060 1.00 37.83 O
ANISOU 1538 O GLN A 220 3070 5705 5597 825 207 -1134 O
ATOM 1539 CB GLN A 220 20.209 -50.991 -38.698 1.00 44.14 C
ANISOU 1539 CB GLN A 220 3568 6616 6586 789 133 -1319 C
ATOM 1540 CG GLN A 220 20.684 -51.868 -37.565 1.00 55.12 C
ANISOU 1540 CG GLN A 220 4832 8081 8031 758 48 -1412 C
ATOM 1541 CD GLN A 220 22.115 -52.318 -37.762 1.00 68.43 C
ANISOU 1541 CD GLN A 220 6470 9830 9702 885 -118 -1419 C
ATOM 1542 OE1 GLN A 220 22.623 -52.330 -38.884 1.00 76.26 O
ANISOU 1542 OE1 GLN A 220 7511 10799 10667 997 -163 -1351 O
ATOM 1543 NE2 GLN A 220 22.779 -52.672 -36.671 1.00 71.61 N
ANISOU 1543 NE2 GLN A 220 6804 10296 10107 859 -216 -1488 N
ATOM 1544 N ALA A 221 18.162 -48.058 -39.512 1.00 26.72 N
ANISOU 1544 N ALA A 221 1689 4233 4230 655 411 -1164 N
ATOM 1545 CA ALA A 221 18.094 -47.026 -40.540 1.00 29.25 C
ANISOU 1545 CA ALA A 221 2137 4495 4481 692 450 -1074 C
ATOM 1546 C ALA A 221 19.119 -45.925 -40.304 1.00 33.74 C
ANISOU 1546 C ALA A 221 2816 5073 4931 710 384 -1018 C
ATOM 1547 O ALA A 221 19.561 -45.275 -41.259 1.00 33.67 O
ANISOU 1547 O ALA A 221 2900 5034 4859 768 374 -935 O
ATOM 1548 CB ALA A 221 16.688 -46.428 -40.597 1.00 27.28 C
ANISOU 1548 CB ALA A 221 1976 4168 4219 593 571 -1041 C
ATOM 1549 N PHE A 222 19.514 -45.709 -39.050 1.00 29.95 N
ANISOU 1549 N PHE A 222 2328 4635 4417 661 342 -1065 N
ATOM 1550 CA PHE A 222 20.411 -44.624 -38.680 1.00 29.08 C
ANISOU 1550 CA PHE A 222 2322 4539 4190 670 292 -1026 C
ATOM 1551 C PHE A 222 21.825 -45.092 -38.368 1.00 32.38 C
ANISOU 1551 C PHE A 222 2709 5024 4569 739 156 -1040 C
ATOM 1552 O PHE A 222 22.588 -44.343 -37.752 1.00 31.52 O
ANISOU 1552 O PHE A 222 2669 4942 4364 735 109 -1034 O
ATOM 1553 CB PHE A 222 19.842 -43.857 -37.488 1.00 24.60 C
ANISOU 1553 CB PHE A 222 1792 3959 3595 570 341 -1067 C
ATOM 1554 CG PHE A 222 18.745 -42.910 -37.858 1.00 25.89 C
ANISOU 1554 CG PHE A 222 2039 4054 3745 519 454 -1026 C
ATOM 1555 CD1 PHE A 222 19.037 -41.607 -38.215 1.00 30.24 C
ANISOU 1555 CD1 PHE A 222 2706 4583 4200 536 468 -959 C
ATOM 1556 CD2 PHE A 222 17.422 -43.327 -37.870 1.00 28.82 C
ANISOU 1556 CD2 PHE A 222 2370 4385 4197 456 546 -1054 C
ATOM 1557 CE1 PHE A 222 18.032 -40.725 -38.568 1.00 25.20 C
ANISOU 1557 CE1 PHE A 222 2138 3884 3553 494 563 -925 C
ATOM 1558 CE2 PHE A 222 16.407 -42.449 -38.224 1.00 29.86 C
ANISOU 1558 CE2 PHE A 222 2585 4452 4310 414 640 -1017 C
ATOM 1559 CZ PHE A 222 16.715 -41.145 -38.573 1.00 23.65 C
ANISOU 1559 CZ PHE A 222 1909 3644 3434 434 644 -953 C
ATOM 1560 N GLN A 223 22.191 -46.306 -38.770 1.00 41.91 N
ANISOU 1560 N GLN A 223 3816 6261 5845 805 89 -1063 N
ATOM 1561 CA GLN A 223 23.581 -46.727 -38.668 1.00 45.24 C
ANISOU 1561 CA GLN A 223 4225 6742 6222 886 -52 -1063 C
ATOM 1562 C GLN A 223 24.419 -45.985 -39.701 1.00 42.79 C
ANISOU 1562 C GLN A 223 4042 6411 5805 965 -82 -954 C
ATOM 1563 O GLN A 223 24.052 -45.909 -40.878 1.00 39.15 O
ANISOU 1563 O GLN A 223 3617 5896 5364 1001 -31 -889 O
ATOM 1564 CB GLN A 223 23.703 -48.235 -38.866 1.00 48.09 C
ANISOU 1564 CB GLN A 223 4439 7137 6694 943 -121 -1118 C
ATOM 1565 CG GLN A 223 23.205 -49.054 -37.683 1.00 57.84 C
ANISOU 1565 CG GLN A 223 5536 8416 8026 865 -119 -1234 C
ATOM 1566 CD GLN A 223 23.890 -48.683 -36.377 1.00 62.91 C
ANISOU 1566 CD GLN A 223 6196 9104 8602 818 -192 -1282 C
ATOM 1567 OE1 GLN A 223 25.081 -48.374 -36.351 1.00 67.20 O
ANISOU 1567 OE1 GLN A 223 6804 9681 9048 882 -297 -1252 O
ATOM 1568 NE2 GLN A 223 23.136 -48.713 -35.285 1.00 62.05 N
ANISOU 1568 NE2 GLN A 223 6038 8995 8542 705 -136 -1357 N
ATOM 1569 N GLY A 224 25.542 -45.428 -39.255 1.00 39.75 N
ANISOU 1569 N GLY A 224 3729 6069 5305 988 -161 -935 N
ATOM 1570 CA GLY A 224 26.405 -44.679 -40.147 1.00 33.21 C
ANISOU 1570 CA GLY A 224 3027 5227 4363 1052 -184 -830 C
ATOM 1571 C GLY A 224 25.848 -43.348 -40.597 1.00 37.73 C
ANISOU 1571 C GLY A 224 3709 5748 4880 1003 -66 -763 C
ATOM 1572 O GLY A 224 26.296 -42.814 -41.615 1.00 41.63 O
ANISOU 1572 O GLY A 224 4295 6214 5308 1046 -58 -668 O
ATOM 1573 N ILE A 225 24.891 -42.788 -39.861 1.00 32.98 N
ANISOU 1573 N ILE A 225 3100 5129 4302 911 23 -810 N
ATOM 1574 CA ILE A 225 24.226 -41.547 -40.236 1.00 27.87 C
ANISOU 1574 CA ILE A 225 2542 4432 3616 863 134 -758 C
ATOM 1575 C ILE A 225 24.690 -40.444 -39.296 1.00 28.79 C
ANISOU 1575 C ILE A 225 2728 4583 3627 828 134 -773 C
ATOM 1576 O ILE A 225 24.668 -40.609 -38.070 1.00 32.13 O
ANISOU 1576 O ILE A 225 3110 5038 4058 788 105 -856 O
ATOM 1577 CB ILE A 225 22.696 -41.696 -40.202 1.00 28.63 C
ANISOU 1577 CB ILE A 225 2588 4473 3816 794 237 -795 C
ATOM 1578 CG1 ILE A 225 22.261 -42.824 -41.137 1.00 27.98 C
ANISOU 1578 CG1 ILE A 225 2433 4362 3836 836 239 -790 C
ATOM 1579 CG2 ILE A 225 22.022 -40.390 -40.595 1.00 23.14 C
ANISOU 1579 CG2 ILE A 225 1985 3727 3079 749 338 -744 C
ATOM 1580 CD1 ILE A 225 22.805 -42.695 -42.544 1.00 28.57 C
ANISOU 1580 CD1 ILE A 225 2574 4405 3878 913 222 -694 C
ATOM 1581 N LYS A 226 25.111 -39.325 -39.873 1.00 24.47 N
ANISOU 1581 N LYS A 226 2285 4030 2982 841 168 -696 N
ATOM 1582 CA LYS A 226 25.516 -38.152 -39.118 1.00 29.38 C
ANISOU 1582 CA LYS A 226 2976 4684 3501 814 183 -707 C
ATOM 1583 C LYS A 226 24.629 -36.981 -39.516 1.00 32.19 C
ANISOU 1583 C LYS A 226 3386 4990 3854 766 297 -670 C
ATOM 1584 O LYS A 226 24.332 -36.789 -40.699 1.00 27.66 O
ANISOU 1584 O LYS A 226 2840 4373 3298 778 345 -596 O
ATOM 1585 CB LYS A 226 26.985 -37.810 -39.376 1.00 39.45 C
ANISOU 1585 CB LYS A 226 4327 6016 4646 876 117 -653 C
ATOM 1586 CG LYS A 226 27.798 -37.538 -38.129 1.00 53.33 C
ANISOU 1586 CG LYS A 226 6102 7842 6318 875 55 -718 C
ATOM 1587 CD LYS A 226 29.152 -36.965 -38.494 1.00 63.31 C
ANISOU 1587 CD LYS A 226 7461 9160 7434 928 17 -653 C
ATOM 1588 CE LYS A 226 29.009 -35.788 -39.444 1.00 68.48 C
ANISOU 1588 CE LYS A 226 8196 9788 8037 915 118 -563 C
ATOM 1589 NZ LYS A 226 30.308 -35.110 -39.705 1.00 70.43 N
ANISOU 1589 NZ LYS A 226 8539 10092 8128 952 99 -502 N
ATOM 1590 N LEU A 227 24.194 -36.208 -38.524 1.00 25.95 N
ANISOU 1590 N LEU A 227 2611 4201 3047 715 334 -726 N
ATOM 1591 CA LEU A 227 23.356 -35.043 -38.758 1.00 23.18 C
ANISOU 1591 CA LEU A 227 2306 3807 2693 673 431 -703 C
ATOM 1592 C LEU A 227 23.808 -33.925 -37.835 1.00 27.40 C
ANISOU 1592 C LEU A 227 2893 4382 3137 663 435 -738 C
ATOM 1593 O LEU A 227 24.240 -34.169 -36.706 1.00 29.39 O
ANISOU 1593 O LEU A 227 3131 4670 3365 661 377 -810 O
ATOM 1594 CB LEU A 227 21.867 -35.345 -38.523 1.00 20.98 C
ANISOU 1594 CB LEU A 227 1982 3463 2524 613 488 -745 C
ATOM 1595 CG LEU A 227 21.131 -36.167 -39.586 1.00 24.48 C
ANISOU 1595 CG LEU A 227 2386 3857 3058 616 519 -709 C
ATOM 1596 CD1 LEU A 227 19.713 -36.498 -39.140 1.00 20.26 C
ANISOU 1596 CD1 LEU A 227 1811 3269 2616 551 574 -762 C
ATOM 1597 CD2 LEU A 227 21.105 -35.419 -40.901 1.00 29.01 C
ANISOU 1597 CD2 LEU A 227 3019 4400 3604 635 569 -618 C
ATOM 1598 N HIS A 228 23.721 -32.692 -38.332 1.00 25.79 N
ANISOU 1598 N HIS A 228 2747 4171 2882 659 502 -690 N
ATOM 1599 CA HIS A 228 23.986 -31.532 -37.490 1.00 24.30 C
ANISOU 1599 CA HIS A 228 2601 4015 2617 652 519 -731 C
ATOM 1600 C HIS A 228 22.830 -31.338 -36.520 1.00 22.98 C
ANISOU 1600 C HIS A 228 2416 3797 2519 601 545 -807 C
ATOM 1601 O HIS A 228 22.956 -31.602 -35.320 1.00 25.85 O
ANISOU 1601 O HIS A 228 2768 4173 2880 589 497 -887 O
ATOM 1602 CB HIS A 228 24.187 -30.269 -38.330 1.00 21.92 C
ANISOU 1602 CB HIS A 228 2352 3724 2251 660 588 -662 C
ATOM 1603 CG HIS A 228 24.535 -29.057 -37.522 1.00 25.12 C
ANISOU 1603 CG HIS A 228 2795 4173 2576 663 609 -707 C
ATOM 1604 ND1 HIS A 228 25.724 -28.938 -36.833 1.00 30.90 N
ANISOU 1604 ND1 HIS A 228 3555 4980 3206 698 560 -740 N
ATOM 1605 CD2 HIS A 228 23.849 -27.915 -37.282 1.00 27.52 C
ANISOU 1605 CD2 HIS A 228 3112 4457 2887 643 671 -730 C
ATOM 1606 CE1 HIS A 228 25.756 -27.776 -36.206 1.00 27.70 C
ANISOU 1606 CE1 HIS A 228 3178 4600 2749 699 597 -785 C
ATOM 1607 NE2 HIS A 228 24.630 -27.137 -36.461 1.00 25.45 N
ANISOU 1607 NE2 HIS A 228 2881 4257 2532 668 662 -780 N
ATOM 1608 N GLU A 229 21.695 -30.885 -37.040 1.00 24.57 N
ANISOU 1608 N GLU A 229 2621 3937 2778 568 615 -781 N
ATOM 1609 CA GLU A 229 20.513 -30.613 -36.240 1.00 22.75 C
ANISOU 1609 CA GLU A 229 2390 3648 2606 520 643 -840 C
ATOM 1610 C GLU A 229 19.369 -31.491 -36.716 1.00 23.56 C
ANISOU 1610 C GLU A 229 2454 3686 2813 481 671 -827 C
ATOM 1611 O GLU A 229 19.045 -31.499 -37.908 1.00 25.51 O
ANISOU 1611 O GLU A 229 2701 3909 3083 487 710 -761 O
ATOM 1612 CB GLU A 229 20.118 -29.139 -36.333 1.00 22.26 C
ANISOU 1612 CB GLU A 229 2373 3572 2511 518 700 -829 C
ATOM 1613 CG GLU A 229 19.157 -28.698 -35.255 1.00 32.56 C
ANISOU 1613 CG GLU A 229 3709 4804 3859 472 695 -874 C
ATOM 1614 CD GLU A 229 18.826 -27.229 -35.350 1.00 44.97 C
ANISOU 1614 CD GLU A 229 5340 6334 5412 468 718 -830 C
ATOM 1615 OE1 GLU A 229 18.048 -26.854 -36.248 1.00 47.09 O
ANISOU 1615 OE1 GLU A 229 5624 6548 5720 450 754 -762 O
ATOM 1616 OE2 GLU A 229 19.354 -26.446 -34.533 1.00 48.36 O
ANISOU 1616 OE2 GLU A 229 5797 6788 5791 487 699 -870 O
ATOM 1617 N LEU A 230 18.759 -32.224 -35.789 1.00 19.70 N
ANISOU 1617 N LEU A 230 1934 3167 2383 438 653 -891 N
ATOM 1618 CA LEU A 230 17.575 -33.028 -36.062 1.00 19.94 C
ANISOU 1618 CA LEU A 230 1931 3138 2507 392 690 -891 C
ATOM 1619 C LEU A 230 16.454 -32.549 -35.155 1.00 22.15 C
ANISOU 1619 C LEU A 230 2244 3357 2815 334 721 -938 C
ATOM 1620 O LEU A 230 16.581 -32.601 -33.928 1.00 26.88 O
ANISOU 1620 O LEU A 230 2848 3957 3410 310 685 -1004 O
ATOM 1621 CB LEU A 230 17.846 -34.516 -35.838 1.00 19.28 C
ANISOU 1621 CB LEU A 230 1771 3077 2477 387 645 -923 C
ATOM 1622 CG LEU A 230 16.635 -35.434 -36.031 1.00 24.87 C
ANISOU 1622 CG LEU A 230 2434 3733 3282 336 691 -934 C
ATOM 1623 CD1 LEU A 230 16.164 -35.429 -37.478 1.00 23.90 C
ANISOU 1623 CD1 LEU A 230 2317 3581 3181 358 743 -864 C
ATOM 1624 CD2 LEU A 230 16.946 -36.851 -35.561 1.00 19.92 C
ANISOU 1624 CD2 LEU A 230 1718 3140 2712 326 644 -985 C
ATOM 1625 N THR A 231 15.364 -32.084 -35.750 1.00 23.56 N
ANISOU 1625 N THR A 231 2472 3461 3019 305 759 -873 N
ATOM 1626 CA THR A 231 14.199 -31.626 -35.006 1.00 21.01 C
ANISOU 1626 CA THR A 231 2200 3065 2717 251 773 -889 C
ATOM 1627 C THR A 231 13.080 -32.642 -35.172 1.00 18.58 C
ANISOU 1627 C THR A 231 1870 2708 2481 194 805 -887 C
ATOM 1628 O THR A 231 12.685 -32.948 -36.300 1.00 22.44 O
ANISOU 1628 O THR A 231 2356 3179 2989 201 824 -822 O
ATOM 1629 CB THR A 231 13.747 -30.247 -35.487 1.00 19.15 C
ANISOU 1629 CB THR A 231 2039 2791 2447 266 781 -824 C
ATOM 1630 OG1 THR A 231 14.867 -29.357 -35.495 1.00 20.59 O
ANISOU 1630 OG1 THR A 231 2233 3027 2564 318 762 -818 O
ATOM 1631 CG2 THR A 231 12.680 -29.686 -34.568 1.00 18.15 C
ANISOU 1631 CG2 THR A 231 1965 2598 2332 224 782 -855 C
ATOM 1632 N LEU A 232 12.575 -33.163 -34.044 1.00 17.65 N
ANISOU 1632 N LEU A 232 1738 2568 2401 136 814 -961 N
ATOM 1633 CA LEU A 232 11.439 -34.091 -34.009 1.00 24.72 C
ANISOU 1633 CA LEU A 232 2617 3417 3361 68 856 -968 C
ATOM 1634 C LEU A 232 10.425 -33.523 -33.018 1.00 26.50 C
ANISOU 1634 C LEU A 232 2911 3570 3586 8 879 -1002 C
ATOM 1635 O LEU A 232 10.384 -33.921 -31.849 1.00 32.74 O
ANISOU 1635 O LEU A 232 3685 4353 4402 -41 888 -1089 O
ATOM 1636 CB LEU A 232 11.874 -35.510 -33.621 1.00 24.27 C
ANISOU 1636 CB LEU A 232 2453 3408 3359 47 858 -1036 C
ATOM 1637 CG LEU A 232 12.718 -36.332 -34.596 1.00 30.75 C
ANISOU 1637 CG LEU A 232 3197 4292 4195 105 836 -1009 C
ATOM 1638 CD1 LEU A 232 13.185 -37.617 -33.918 1.00 25.17 C
ANISOU 1638 CD1 LEU A 232 2384 3635 3543 83 811 -1084 C
ATOM 1639 CD2 LEU A 232 11.938 -36.633 -35.866 1.00 26.64 C
ANISOU 1639 CD2 LEU A 232 2696 3731 3694 108 865 -926 C
ATOM 1640 N ARG A 233 9.611 -32.580 -33.485 1.00 19.33 N
ANISOU 1640 N ARG A 233 2083 2608 2653 13 886 -941 N
ATOM 1641 CA ARG A 233 8.585 -31.943 -32.669 1.00 22.76 C
ANISOU 1641 CA ARG A 233 2595 2967 3084 -33 903 -965 C
ATOM 1642 C ARG A 233 7.202 -32.274 -33.211 1.00 21.86 C
ANISOU 1642 C ARG A 233 2516 2795 2995 -83 951 -923 C
ATOM 1643 O ARG A 233 6.966 -32.216 -34.422 1.00 19.21 O
ANISOU 1643 O ARG A 233 2180 2466 2652 -55 949 -853 O
ATOM 1644 CB ARG A 233 8.770 -30.421 -32.616 1.00 16.74 C
ANISOU 1644 CB ARG A 233 1899 2193 2268 23 862 -941 C
ATOM 1645 CG ARG A 233 10.036 -29.964 -31.903 1.00 17.05 C
ANISOU 1645 CG ARG A 233 1924 2283 2273 69 816 -991 C
ATOM 1646 CD ARG A 233 9.981 -28.483 -31.568 1.00 18.98 C
ANISOU 1646 CD ARG A 233 2237 2502 2472 112 783 -984 C
ATOM 1647 NE ARG A 233 8.948 -28.192 -30.580 1.00 19.33 N
ANISOU 1647 NE ARG A 233 2354 2459 2532 68 787 -1025 N
ATOM 1648 CZ ARG A 233 8.560 -26.965 -30.254 1.00 23.12 C
ANISOU 1648 CZ ARG A 233 2902 2896 2985 101 758 -1020 C
ATOM 1649 NH1 ARG A 233 9.121 -25.921 -30.846 1.00 19.82 N
ANISOU 1649 NH1 ARG A 233 2477 2523 2529 174 731 -980 N
ATOM 1650 NH2 ARG A 233 7.612 -26.783 -29.344 1.00 17.35 N
ANISOU 1650 NH2 ARG A 233 2248 2075 2268 61 755 -1056 N
ATOM 1651 N GLY A 234 6.293 -32.621 -32.308 1.00 17.30 N
ANISOU 1651 N GLY A 234 1974 2158 2440 -161 995 -971 N
ATOM 1652 CA GLY A 234 4.921 -32.897 -32.694 1.00 20.20 C
ANISOU 1652 CA GLY A 234 2388 2468 2819 -215 1048 -938 C
ATOM 1653 C GLY A 234 4.754 -34.050 -33.657 1.00 21.55 C
ANISOU 1653 C GLY A 234 2492 2672 3023 -226 1076 -905 C
ATOM 1654 O GLY A 234 3.825 -34.035 -34.472 1.00 25.34 O
ANISOU 1654 O GLY A 234 3012 3121 3497 -234 1096 -855 O
ATOM 1655 N ASN A 235 5.622 -35.062 -33.584 1.00 19.87 N
ANISOU 1655 N ASN A 235 2180 2522 2847 -222 1072 -938 N
ATOM 1656 CA ASN A 235 5.509 -36.208 -34.481 1.00 19.69 C
ANISOU 1656 CA ASN A 235 2092 2529 2859 -222 1088 -913 C
ATOM 1657 C ASN A 235 4.598 -37.301 -33.945 1.00 28.54 C
ANISOU 1657 C ASN A 235 3191 3627 4024 -315 1159 -953 C
ATOM 1658 O ASN A 235 4.012 -38.047 -34.739 1.00 23.13 O
ANISOU 1658 O ASN A 235 2491 2942 3356 -321 1182 -923 O
ATOM 1659 CB ASN A 235 6.885 -36.821 -34.760 1.00 18.08 C
ANISOU 1659 CB ASN A 235 1790 2406 2675 -163 1045 -926 C
ATOM 1660 CG ASN A 235 7.832 -35.853 -35.430 1.00 19.00 C
ANISOU 1660 CG ASN A 235 1926 2550 2742 -74 988 -879 C
ATOM 1661 OD1 ASN A 235 8.451 -35.028 -34.764 1.00 29.30 O
ANISOU 1661 OD1 ASN A 235 3251 3865 4015 -55 959 -904 O
ATOM 1662 ND2 ASN A 235 7.952 -35.948 -36.751 1.00 20.42 N
ANISOU 1662 ND2 ASN A 235 2102 2742 2914 -22 973 -815 N
ATOM 1663 N PHE A 236 4.450 -37.414 -32.629 1.00 25.21 N
ANISOU 1663 N PHE A 236 2772 3187 3621 -390 1197 -1023 N
ATOM 1664 CA PHE A 236 3.899 -38.615 -32.024 1.00 27.39 C
ANISOU 1664 CA PHE A 236 2995 3464 3949 -486 1265 -1071 C
ATOM 1665 C PHE A 236 2.609 -38.320 -31.276 1.00 31.69 C
ANISOU 1665 C PHE A 236 3641 3925 4473 -585 1343 -1082 C
ATOM 1666 O PHE A 236 2.495 -37.308 -30.578 1.00 29.09 O
ANISOU 1666 O PHE A 236 3408 3538 4105 -591 1319 -1085 O
ATOM 1667 CB PHE A 236 4.934 -39.246 -31.094 1.00 25.03 C
ANISOU 1667 CB PHE A 236 2586 3226 3699 -508 1252 -1154 C
ATOM 1668 CG PHE A 236 6.235 -39.546 -31.778 1.00 29.69 C
ANISOU 1668 CG PHE A 236 3084 3897 4300 -410 1176 -1146 C
ATOM 1669 CD1 PHE A 236 6.306 -40.553 -32.728 1.00 25.92 C
ANISOU 1669 CD1 PHE A 236 2537 3459 3854 -377 1166 -1115 C
ATOM 1670 CD2 PHE A 236 7.375 -38.809 -31.500 1.00 29.10 C
ANISOU 1670 CD2 PHE A 236 3007 3855 4195 -345 1110 -1166 C
ATOM 1671 CE1 PHE A 236 7.498 -40.835 -33.381 1.00 24.43 C
ANISOU 1671 CE1 PHE A 236 2274 3338 3671 -285 1101 -1106 C
ATOM 1672 CE2 PHE A 236 8.576 -39.087 -32.150 1.00 23.83 C
ANISOU 1672 CE2 PHE A 236 2262 3262 3530 -257 1050 -1158 C
ATOM 1673 CZ PHE A 236 8.634 -40.103 -33.092 1.00 22.57 C
ANISOU 1673 CZ PHE A 236 2033 3136 3405 -228 1044 -1125 C
ATOM 1674 N ASN A 237 1.634 -39.216 -31.454 1.00 41.58 N
ANISOU 1674 N ASN A 237 4891 5162 5745 -653 1404 -1070 N
ATOM 1675 CA ASN A 237 0.373 -39.186 -30.731 1.00 37.91 C
ANISOU 1675 CA ASN A 237 4521 4622 5261 -765 1489 -1077 C
ATOM 1676 C ASN A 237 0.326 -40.150 -29.555 1.00 31.43 C
ANISOU 1676 C ASN A 237 3638 3811 4494 -887 1546 -1137 C
ATOM 1677 O ASN A 237 -0.500 -39.964 -28.657 1.00 27.65 O
ANISOU 1677 O ASN A 237 3261 3252 3991 -984 1572 -1130 O
ATOM 1678 CB ASN A 237 -0.791 -39.516 -31.682 1.00 40.74 C
ANISOU 1678 CB ASN A 237 4934 4953 5594 -766 1519 -1021 C
ATOM 1679 CG ASN A 237 -1.715 -38.335 -31.912 1.00 56.54 C
ANISOU 1679 CG ASN A 237 7085 6874 7524 -759 1528 -975 C
ATOM 1680 OD1 ASN A 237 -1.913 -37.509 -31.022 1.00 70.08 O
ANISOU 1680 OD1 ASN A 237 8890 8531 9205 -798 1550 -992 O
ATOM 1681 ND2 ASN A 237 -2.286 -38.251 -33.107 1.00 64.73 N
ANISOU 1681 ND2 ASN A 237 8153 7906 8537 -707 1510 -921 N
ATOM 1682 N SER A 238 1.182 -41.166 -29.538 1.00 30.74 N
ANISOU 1682 N SER A 238 3406 3803 4470 -875 1516 -1177 N
ATOM 1683 CA SER A 238 1.122 -42.239 -28.560 1.00 31.82 C
ANISOU 1683 CA SER A 238 3465 3957 4667 -988 1553 -1230 C
ATOM 1684 C SER A 238 2.506 -42.459 -27.976 1.00 32.44 C
ANISOU 1684 C SER A 238 3429 4099 4798 -966 1475 -1289 C
ATOM 1685 O SER A 238 3.508 -42.369 -28.690 1.00 23.90 O
ANISOU 1685 O SER A 238 2277 3082 3720 -852 1413 -1290 O
ATOM 1686 CB SER A 238 0.618 -43.536 -29.198 1.00 39.77 C
ANISOU 1686 CB SER A 238 4412 5002 5699 -987 1577 -1221 C
ATOM 1687 OG SER A 238 0.014 -43.281 -30.455 1.00 55.72 O
ANISOU 1687 OG SER A 238 6497 7005 7671 -909 1577 -1159 O
ATOM 1688 N SER A 239 2.556 -42.759 -26.677 1.00 30.31 N
ANISOU 1688 N SER A 239 3155 3801 4559 -1069 1459 -1330 N
ATOM 1689 CA SER A 239 3.839 -42.979 -26.019 1.00 32.16 C
ANISOU 1689 CA SER A 239 3300 4086 4833 -1047 1359 -1386 C
ATOM 1690 C SER A 239 4.564 -44.177 -26.619 1.00 29.06 C
ANISOU 1690 C SER A 239 2718 3809 4513 -1008 1360 -1428 C
ATOM 1691 O SER A 239 5.771 -44.122 -26.883 1.00 36.00 O
ANISOU 1691 O SER A 239 3529 4752 5397 -909 1267 -1445 O
ATOM 1692 CB SER A 239 3.627 -43.179 -24.520 1.00 35.58 C
ANISOU 1692 CB SER A 239 3765 4459 5294 -1181 1350 -1427 C
ATOM 1693 OG SER A 239 2.683 -42.257 -24.003 1.00 47.37 O
ANISOU 1693 OG SER A 239 5438 5833 6727 -1233 1370 -1385 O
ATOM 1694 N ASN A 240 3.830 -45.271 -26.846 1.00 28.21 N
ANISOU 1694 N ASN A 240 2551 3723 4446 -1065 1439 -1433 N
ATOM 1695 CA ASN A 240 4.440 -46.499 -27.347 1.00 36.90 C
ANISOU 1695 CA ASN A 240 3507 4914 5601 -1007 1402 -1460 C
ATOM 1696 C ASN A 240 5.039 -46.301 -28.735 1.00 31.03 C
ANISOU 1696 C ASN A 240 2748 4212 4829 -852 1350 -1416 C
ATOM 1697 O ASN A 240 6.087 -46.874 -29.052 1.00 33.31 O
ANISOU 1697 O ASN A 240 2920 4577 5157 -778 1281 -1443 O
ATOM 1698 CB ASN A 240 3.401 -47.622 -27.364 1.00 45.75 C
ANISOU 1698 CB ASN A 240 4614 6029 6740 -1074 1475 -1454 C
ATOM 1699 CG ASN A 240 4.026 -49.005 -27.425 1.00 62.87 C
ANISOU 1699 CG ASN A 240 6616 8287 8984 -1054 1443 -1504 C
ATOM 1700 OD1 ASN A 240 4.817 -49.309 -28.317 1.00 66.08 O
ANISOU 1700 OD1 ASN A 240 6945 8755 9406 -938 1384 -1501 O
ATOM 1701 ND2 ASN A 240 3.674 -49.852 -26.464 1.00 71.67 N
ANISOU 1701 ND2 ASN A 240 7678 9408 10146 -1167 1479 -1548 N
ATOM 1702 N ILE A 241 4.386 -45.503 -29.582 1.00 28.79 N
ANISOU 1702 N ILE A 241 2586 3875 4478 -803 1376 -1344 N
ATOM 1703 CA ILE A 241 4.928 -45.255 -30.915 1.00 31.03 C
ANISOU 1703 CA ILE A 241 2872 4186 4732 -665 1320 -1291 C
ATOM 1704 C ILE A 241 6.181 -44.392 -30.833 1.00 34.20 C
ANISOU 1704 C ILE A 241 3262 4619 5116 -590 1243 -1302 C
ATOM 1705 O ILE A 241 7.152 -44.611 -31.569 1.00 28.17 O
ANISOU 1705 O ILE A 241 2436 3912 4358 -488 1176 -1291 O
ATOM 1706 CB ILE A 241 3.853 -44.625 -31.818 1.00 27.13 C
ANISOU 1706 CB ILE A 241 2511 3625 4174 -642 1359 -1213 C
ATOM 1707 CG1 ILE A 241 2.703 -45.612 -32.036 1.00 26.05 C
ANISOU 1707 CG1 ILE A 241 2372 3474 4050 -699 1430 -1209 C
ATOM 1708 CG2 ILE A 241 4.447 -44.198 -33.151 1.00 23.09 C
ANISOU 1708 CG2 ILE A 241 2012 3131 3628 -512 1296 -1153 C
ATOM 1709 CD1 ILE A 241 1.648 -45.126 -33.004 1.00 24.14 C
ANISOU 1709 CD1 ILE A 241 2246 3177 3748 -673 1460 -1141 C
ATOM 1710 N MET A 242 6.188 -43.401 -29.936 1.00 34.82 N
ANISOU 1710 N MET A 242 3402 4659 5168 -637 1254 -1326 N
ATOM 1711 CA MET A 242 7.385 -42.582 -29.775 1.00 29.86 C
ANISOU 1711 CA MET A 242 2785 4055 4504 -556 1159 -1332 C
ATOM 1712 C MET A 242 8.539 -43.401 -29.212 1.00 27.46 C
ANISOU 1712 C MET A 242 2356 3827 4252 -548 1079 -1395 C
ATOM 1713 O MET A 242 9.676 -43.290 -29.683 1.00 23.98 O
ANISOU 1713 O MET A 242 1876 3444 3793 -446 999 -1390 O
ATOM 1714 CB MET A 242 7.103 -41.380 -28.877 1.00 22.97 C
ANISOU 1714 CB MET A 242 2058 3099 3571 -592 1133 -1319 C
ATOM 1715 CG MET A 242 8.355 -40.569 -28.585 1.00 27.31 C
ANISOU 1715 CG MET A 242 2631 3672 4074 -510 1024 -1327 C
ATOM 1716 SD MET A 242 8.037 -38.989 -27.773 1.00 36.01 S
ANISOU 1716 SD MET A 242 3905 4676 5100 -517 993 -1310 S
ATOM 1717 CE MET A 242 9.665 -38.255 -27.850 1.00 30.07 C
ANISOU 1717 CE MET A 242 3142 3988 4294 -397 882 -1319 C
ATOM 1718 N LYS A 243 8.267 -44.226 -28.200 1.00 32.78 N
ANISOU 1718 N LYS A 243 2966 4501 4986 -659 1097 -1455 N
ATOM 1719 CA LYS A 243 9.320 -45.058 -27.631 1.00 38.58 C
ANISOU 1719 CA LYS A 243 3571 5310 5776 -659 1015 -1523 C
ATOM 1720 C LYS A 243 9.864 -46.041 -28.660 1.00 35.67 C
ANISOU 1720 C LYS A 243 3059 5033 5459 -575 1006 -1532 C
ATOM 1721 O LYS A 243 11.080 -46.247 -28.748 1.00 30.15 O
ANISOU 1721 O LYS A 243 2295 4400 4763 -495 904 -1553 O
ATOM 1722 CB LYS A 243 8.797 -45.799 -26.401 1.00 40.70 C
ANISOU 1722 CB LYS A 243 3793 5559 6111 -808 1048 -1585 C
ATOM 1723 CG LYS A 243 9.827 -46.714 -25.761 1.00 41.39 C
ANISOU 1723 CG LYS A 243 3737 5724 6265 -819 960 -1665 C
ATOM 1724 CD LYS A 243 9.316 -47.307 -24.458 1.00 41.06 C
ANISOU 1724 CD LYS A 243 3662 5651 6287 -980 989 -1726 C
ATOM 1725 CE LYS A 243 10.360 -48.206 -23.817 1.00 46.95 C
ANISOU 1725 CE LYS A 243 4258 6476 7103 -992 891 -1812 C
ATOM 1726 NZ LYS A 243 10.508 -47.942 -22.361 1.00 50.83 N
ANISOU 1726 NZ LYS A 243 4802 6912 7597 -1096 837 -1862 N
ATOM 1727 N THR A 244 8.979 -46.653 -29.454 1.00 36.34 N
ANISOU 1727 N THR A 244 3141 5106 5562 -579 1082 -1495 N
ATOM 1728 CA THR A 244 9.425 -47.625 -30.450 1.00 34.49 C
ANISOU 1728 CA THR A 244 2824 4926 5356 -488 1042 -1478 C
ATOM 1729 C THR A 244 10.274 -46.964 -31.530 1.00 35.31 C
ANISOU 1729 C THR A 244 2963 5048 5406 -349 980 -1423 C
ATOM 1730 O THR A 244 11.251 -47.553 -32.008 1.00 38.32 O
ANISOU 1730 O THR A 244 3254 5493 5811 -263 907 -1435 O
ATOM 1731 CB THR A 244 8.224 -48.334 -31.082 1.00 30.75 C
ANISOU 1731 CB THR A 244 2377 4417 4889 -515 1122 -1437 C
ATOM 1732 OG1 THR A 244 7.502 -49.056 -30.076 1.00 36.74 O
ANISOU 1732 OG1 THR A 244 3097 5166 5695 -642 1180 -1488 O
ATOM 1733 CG2 THR A 244 8.684 -49.312 -32.151 1.00 27.68 C
ANISOU 1733 CG2 THR A 244 1903 4081 4532 -415 1083 -1423 C
ATOM 1734 N CYS A 245 9.921 -45.738 -31.926 1.00 26.43 N
ANISOU 1734 N CYS A 245 1972 3865 4206 -326 1005 -1361 N
ATOM 1735 CA CYS A 245 10.661 -45.068 -32.992 1.00 30.59 C
ANISOU 1735 CA CYS A 245 2546 4401 4677 -205 953 -1299 C
ATOM 1736 C CYS A 245 12.001 -44.531 -32.501 1.00 33.72 C
ANISOU 1736 C CYS A 245 2905 4856 5053 -151 875 -1343 C
ATOM 1737 O CYS A 245 12.989 -44.553 -33.243 1.00 33.91 O
ANISOU 1737 O CYS A 245 2900 4926 5058 -47 810 -1321 O
ATOM 1738 CB CYS A 245 9.822 -43.938 -33.585 1.00 28.66 C
ANISOU 1738 CB CYS A 245 2453 4077 4360 -201 999 -1218 C
ATOM 1739 SG CYS A 245 8.461 -44.492 -34.626 1.00 27.37 S
ANISOU 1739 SG CYS A 245 2339 3860 4200 -216 1065 -1153 S
ATOM 1740 N LEU A 246 12.053 -44.038 -31.259 1.00 28.14 N
ANISOU 1740 N LEU A 246 2240 4127 4324 -219 851 -1380 N
ATOM 1741 CA LEU A 246 13.301 -43.493 -30.727 1.00 28.60 C
ANISOU 1741 CA LEU A 246 2324 4215 4326 -169 740 -1392 C
ATOM 1742 C LEU A 246 14.377 -44.563 -30.617 1.00 32.37 C
ANISOU 1742 C LEU A 246 2670 4778 4850 -129 651 -1443 C
ATOM 1743 O LEU A 246 15.573 -44.268 -30.745 1.00 37.13 O
ANISOU 1743 O LEU A 246 3283 5424 5398 -45 556 -1433 O
ATOM 1744 CB LEU A 246 13.059 -42.850 -29.364 1.00 32.79 C
ANISOU 1744 CB LEU A 246 2933 4694 4832 -255 728 -1428 C
ATOM 1745 CG LEU A 246 12.306 -41.522 -29.355 1.00 31.84 C
ANISOU 1745 CG LEU A 246 2962 4491 4645 -268 778 -1379 C
ATOM 1746 CD1 LEU A 246 12.371 -40.912 -27.972 1.00 29.99 C
ANISOU 1746 CD1 LEU A 246 2799 4212 4385 -327 737 -1422 C
ATOM 1747 CD2 LEU A 246 12.865 -40.565 -30.392 1.00 22.39 C
ANISOU 1747 CD2 LEU A 246 1827 3307 3372 -156 758 -1312 C
ATOM 1748 N GLN A 247 13.973 -45.811 -30.367 1.00 31.95 N
ANISOU 1748 N GLN A 247 2491 4754 4895 -189 679 -1499 N
ATOM 1749 CA GLN A 247 14.938 -46.900 -30.239 1.00 29.05 C
ANISOU 1749 CA GLN A 247 1983 4471 4585 -151 588 -1555 C
ATOM 1750 C GLN A 247 15.714 -47.112 -31.532 1.00 30.16 C
ANISOU 1750 C GLN A 247 2093 4657 4709 -13 540 -1509 C
ATOM 1751 O GLN A 247 16.913 -47.416 -31.503 1.00 40.22 O
ANISOU 1751 O GLN A 247 3321 5991 5969 59 426 -1527 O
ATOM 1752 CB GLN A 247 14.222 -48.185 -29.826 1.00 36.00 C
ANISOU 1752 CB GLN A 247 2723 5374 5581 -243 645 -1624 C
ATOM 1753 CG GLN A 247 14.281 -48.468 -28.334 1.00 49.26 C
ANISOU 1753 CG GLN A 247 4365 7055 7297 -357 610 -1702 C
ATOM 1754 CD GLN A 247 13.055 -49.197 -27.833 1.00 55.26 C
ANISOU 1754 CD GLN A 247 5062 7793 8144 -495 724 -1743 C
ATOM 1755 OE1 GLN A 247 12.298 -49.773 -28.612 1.00 51.68 O
ANISOU 1755 OE1 GLN A 247 4604 7324 7709 -485 799 -1703 O
ATOM 1756 NE2 GLN A 247 12.846 -49.166 -26.524 1.00 60.68 N
ANISOU 1756 NE2 GLN A 247 5761 8447 8847 -616 718 -1793 N
ATOM 1757 N ASN A 248 15.050 -46.960 -32.675 1.00 27.22 N
ANISOU 1757 N ASN A 248 1755 4253 4335 24 622 -1449 N
ATOM 1758 CA ASN A 248 15.665 -47.199 -33.974 1.00 34.83 C
ANISOU 1758 CA ASN A 248 2698 5244 5293 148 585 -1402 C
ATOM 1759 C ASN A 248 16.397 -45.975 -34.515 1.00 33.41 C
ANISOU 1759 C ASN A 248 2650 5044 4999 226 540 -1323 C
ATOM 1760 O ASN A 248 16.811 -45.977 -35.679 1.00 35.63 O
ANISOU 1760 O ASN A 248 2945 5329 5263 321 522 -1268 O
ATOM 1761 CB ASN A 248 14.611 -47.680 -34.973 1.00 38.68 C
ANISOU 1761 CB ASN A 248 3219 5674 5805 142 665 -1341 C
ATOM 1762 CG ASN A 248 14.387 -49.181 -34.897 1.00 44.11 C
ANISOU 1762 CG ASN A 248 3786 6392 6582 122 661 -1387 C
ATOM 1763 OD1 ASN A 248 15.324 -49.946 -34.670 1.00 46.76 O
ANISOU 1763 OD1 ASN A 248 4007 6798 6962 169 572 -1440 O
ATOM 1764 ND2 ASN A 248 13.145 -49.609 -35.090 1.00 46.96 N
ANISOU 1764 ND2 ASN A 248 4173 6704 6965 57 752 -1369 N
ATOM 1765 N LEU A 249 16.561 -44.927 -33.701 1.00 29.77 N
ANISOU 1765 N LEU A 249 2288 4560 4464 187 525 -1319 N
ATOM 1766 CA LEU A 249 17.566 -43.908 -33.981 1.00 27.34 C
ANISOU 1766 CA LEU A 249 2078 4261 4049 262 462 -1265 C
ATOM 1767 C LEU A 249 18.976 -44.403 -33.682 1.00 28.46 C
ANISOU 1767 C LEU A 249 2167 4477 4169 325 332 -1294 C
ATOM 1768 O LEU A 249 19.929 -43.630 -33.812 1.00 30.29 O
ANISOU 1768 O LEU A 249 2478 4726 4303 385 274 -1256 O
ATOM 1769 CB LEU A 249 17.284 -42.636 -33.171 1.00 30.01 C
ANISOU 1769 CB LEU A 249 2531 4554 4316 206 487 -1262 C
ATOM 1770 CG LEU A 249 15.980 -41.867 -33.409 1.00 31.31 C
ANISOU 1770 CG LEU A 249 2777 4641 4477 153 598 -1226 C
ATOM 1771 CD1 LEU A 249 15.923 -40.599 -32.561 1.00 31.83 C
ANISOU 1771 CD1 LEU A 249 2953 4670 4471 119 596 -1229 C
ATOM 1772 CD2 LEU A 249 15.813 -41.533 -34.880 1.00 28.69 C
ANISOU 1772 CD2 LEU A 249 2483 4291 4127 220 641 -1146 C
ATOM 1773 N ALA A 250 19.117 -45.672 -33.299 1.00 32.82 N
ANISOU 1773 N ALA A 250 2587 5075 4808 313 287 -1363 N
ATOM 1774 CA ALA A 250 20.392 -46.221 -32.853 1.00 29.78 C
ANISOU 1774 CA ALA A 250 2144 4762 4410 363 153 -1405 C
ATOM 1775 C ALA A 250 21.458 -46.103 -33.934 1.00 30.08 C
ANISOU 1775 C ALA A 250 2219 4828 4381 490 81 -1335 C
ATOM 1776 O ALA A 250 21.202 -46.367 -35.113 1.00 32.61 O
ANISOU 1776 O ALA A 250 2531 5130 4730 546 118 -1281 O
ATOM 1777 CB ALA A 250 20.212 -47.684 -32.450 1.00 28.94 C
ANISOU 1777 CB ALA A 250 1868 4699 4426 331 127 -1489 C
ATOM 1778 N GLY A 251 22.665 -45.718 -33.519 1.00 28.22 N
ANISOU 1778 N GLY A 251 2033 4635 4053 535 -23 -1336 N
ATOM 1779 CA GLY A 251 23.768 -45.485 -34.419 1.00 30.21 C
ANISOU 1779 CA GLY A 251 2345 4914 4221 647 -94 -1264 C
ATOM 1780 C GLY A 251 23.891 -44.051 -34.886 1.00 29.37 C
ANISOU 1780 C GLY A 251 2389 4772 3998 662 -41 -1180 C
ATOM 1781 O GLY A 251 24.925 -43.683 -35.455 1.00 32.75 O
ANISOU 1781 O GLY A 251 2886 5226 4332 741 -100 -1120 O
ATOM 1782 N LEU A 252 22.875 -43.234 -34.637 1.00 28.52 N
ANISOU 1782 N LEU A 252 2333 4609 3893 586 66 -1176 N
ATOM 1783 CA LEU A 252 22.868 -41.860 -35.115 1.00 26.88 C
ANISOU 1783 CA LEU A 252 2254 4369 3590 597 125 -1102 C
ATOM 1784 C LEU A 252 23.818 -40.988 -34.298 1.00 31.38 C
ANISOU 1784 C LEU A 252 2901 4976 4044 606 69 -1119 C
ATOM 1785 O LEU A 252 23.983 -41.179 -33.088 1.00 30.00 O
ANISOU 1785 O LEU A 252 2699 4824 3875 564 21 -1201 O
ATOM 1786 CB LEU A 252 21.443 -41.322 -35.045 1.00 25.31 C
ANISOU 1786 CB LEU A 252 2079 4100 3438 518 246 -1101 C
ATOM 1787 CG LEU A 252 21.143 -39.840 -35.201 1.00 26.97 C
ANISOU 1787 CG LEU A 252 2406 4271 3571 504 314 -1052 C
ATOM 1788 CD1 LEU A 252 21.472 -39.383 -36.613 1.00 22.87 C
ANISOU 1788 CD1 LEU A 252 1941 3743 3006 571 336 -954 C
ATOM 1789 CD2 LEU A 252 19.685 -39.559 -34.852 1.00 37.66 C
ANISOU 1789 CD2 LEU A 252 3768 5556 4984 418 411 -1074 C
ATOM 1790 N HIS A 253 24.451 -40.027 -34.972 1.00 35.87 N
ANISOU 1790 N HIS A 253 3568 5553 4508 658 78 -1043 N
ATOM 1791 CA HIS A 253 25.349 -39.056 -34.353 1.00 34.27 C
ANISOU 1791 CA HIS A 253 3450 5389 4181 673 43 -1051 C
ATOM 1792 C HIS A 253 24.840 -37.667 -34.720 1.00 32.75 C
ANISOU 1792 C HIS A 253 3347 5158 3940 654 145 -999 C
ATOM 1793 O HIS A 253 24.979 -37.234 -35.869 1.00 31.45 O
ANISOU 1793 O HIS A 253 3227 4983 3740 691 184 -911 O
ATOM 1794 CB HIS A 253 26.789 -39.266 -34.824 1.00 34.72 C
ANISOU 1794 CB HIS A 253 3536 5510 4144 759 -51 -1009 C
ATOM 1795 CG HIS A 253 27.805 -38.446 -34.087 1.00 48.06 C
ANISOU 1795 CG HIS A 253 5306 7254 5702 777 -96 -1032 C
ATOM 1796 ND1 HIS A 253 28.978 -38.983 -33.602 1.00 51.81 N
ANISOU 1796 ND1 HIS A 253 5775 7796 6114 822 -217 -1068 N
ATOM 1797 CD2 HIS A 253 27.834 -37.130 -33.767 1.00 51.54 C
ANISOU 1797 CD2 HIS A 253 5832 7694 6057 760 -38 -1028 C
ATOM 1798 CE1 HIS A 253 29.681 -38.035 -33.007 1.00 51.96 C
ANISOU 1798 CE1 HIS A 253 5879 7853 6011 830 -227 -1086 C
ATOM 1799 NE2 HIS A 253 29.009 -36.902 -33.094 1.00 48.96 N
ANISOU 1799 NE2 HIS A 253 5551 7434 5617 794 -117 -1064 N
ATOM 1800 N VAL A 254 24.229 -36.979 -33.759 1.00 30.71 N
ANISOU 1800 N VAL A 254 3113 4872 3683 596 185 -1055 N
ATOM 1801 CA VAL A 254 23.660 -35.657 -33.986 1.00 28.92 C
ANISOU 1801 CA VAL A 254 2960 4607 3421 578 275 -1020 C
ATOM 1802 C VAL A 254 24.375 -34.657 -33.093 1.00 23.32 C
ANISOU 1802 C VAL A 254 2318 3935 2609 590 252 -1061 C
ATOM 1803 O VAL A 254 24.651 -34.946 -31.923 1.00 33.61 O
ANISOU 1803 O VAL A 254 3607 5254 3908 571 191 -1145 O
ATOM 1804 CB VAL A 254 22.142 -35.623 -33.724 1.00 36.36 C
ANISOU 1804 CB VAL A 254 3883 5471 4460 505 350 -1044 C
ATOM 1805 CG1 VAL A 254 21.630 -34.227 -33.862 1.00 46.56 C
ANISOU 1805 CG1 VAL A 254 5250 6728 5711 495 425 -1017 C
ATOM 1806 CG2 VAL A 254 21.422 -36.454 -34.722 1.00 56.33 C
ANISOU 1806 CG2 VAL A 254 6358 7966 7078 499 388 -1001 C
ATOM 1807 N HIS A 255 24.671 -33.481 -33.647 1.00 23.61 N
ANISOU 1807 N HIS A 255 2424 3985 2562 619 302 -1007 N
ATOM 1808 CA HIS A 255 25.143 -32.378 -32.821 1.00 26.86 C
ANISOU 1808 CA HIS A 255 2897 4426 2882 629 302 -1052 C
ATOM 1809 C HIS A 255 24.027 -31.852 -31.925 1.00 23.94 C
ANISOU 1809 C HIS A 255 2536 3991 2571 574 343 -1115 C
ATOM 1810 O HIS A 255 24.240 -31.600 -30.734 1.00 22.97 O
ANISOU 1810 O HIS A 255 2435 3873 2422 565 304 -1198 O
ATOM 1811 CB HIS A 255 25.694 -31.257 -33.700 1.00 25.41 C
ANISOU 1811 CB HIS A 255 2774 4278 2603 670 357 -977 C
ATOM 1812 CG HIS A 255 26.289 -30.125 -32.920 1.00 27.17 C
ANISOU 1812 CG HIS A 255 3054 4544 2724 690 362 -1027 C
ATOM 1813 ND1 HIS A 255 27.449 -30.259 -32.190 1.00 24.29 N
ANISOU 1813 ND1 HIS A 255 2715 4248 2267 724 288 -1077 N
ATOM 1814 CD2 HIS A 255 25.877 -28.845 -32.744 1.00 22.96 C
ANISOU 1814 CD2 HIS A 255 2557 3998 2169 686 430 -1040 C
ATOM 1815 CE1 HIS A 255 27.730 -29.109 -31.603 1.00 28.34 C
ANISOU 1815 CE1 HIS A 255 3278 4788 2702 740 317 -1121 C
ATOM 1816 NE2 HIS A 255 26.792 -28.235 -31.921 1.00 27.00 N
ANISOU 1816 NE2 HIS A 255 3111 4570 2576 719 403 -1100 N
ATOM 1817 N ARG A 256 22.827 -31.677 -32.479 1.00 22.38 N
ANISOU 1817 N ARG A 256 2329 3726 2449 539 416 -1078 N
ATOM 1818 CA ARG A 256 21.726 -31.045 -31.759 1.00 22.71 C
ANISOU 1818 CA ARG A 256 2395 3698 2536 493 457 -1123 C
ATOM 1819 C ARG A 256 20.419 -31.769 -32.050 1.00 25.76 C
ANISOU 1819 C ARG A 256 2742 4011 3034 435 496 -1108 C
ATOM 1820 O ARG A 256 19.932 -31.740 -33.184 1.00 21.83 O
ANISOU 1820 O ARG A 256 2237 3494 2564 439 549 -1037 O
ATOM 1821 CB ARG A 256 21.610 -29.567 -32.143 1.00 20.67 C
ANISOU 1821 CB ARG A 256 2192 3440 2223 520 519 -1092 C
ATOM 1822 CG ARG A 256 20.547 -28.827 -31.359 1.00 26.12 C
ANISOU 1822 CG ARG A 256 2916 4058 2952 486 548 -1141 C
ATOM 1823 CD ARG A 256 20.558 -27.329 -31.622 1.00 26.24 C
ANISOU 1823 CD ARG A 256 2987 4062 2922 510 582 -1095 C
ATOM 1824 NE ARG A 256 21.893 -26.741 -31.546 1.00 39.26 N
ANISOU 1824 NE ARG A 256 4655 5794 4467 563 564 -1101 N
ATOM 1825 CZ ARG A 256 22.529 -26.209 -32.586 1.00 38.33 C
ANISOU 1825 CZ ARG A 256 4545 5724 4297 591 598 -1024 C
ATOM 1826 NH1 ARG A 256 21.946 -26.187 -33.777 1.00 30.82 N
ANISOU 1826 NH1 ARG A 256 3580 4738 3391 572 647 -939 N
ATOM 1827 NH2 ARG A 256 23.740 -25.688 -32.437 1.00 40.53 N
ANISOU 1827 NH2 ARG A 256 4846 6079 4473 633 587 -1033 N
ATOM 1828 N LEU A 257 19.845 -32.396 -31.026 1.00 22.82 N
ANISOU 1828 N LEU A 257 2349 3597 2724 378 473 -1175 N
ATOM 1829 CA LEU A 257 18.564 -33.085 -31.119 1.00 23.27 C
ANISOU 1829 CA LEU A 257 2375 3586 2882 312 517 -1171 C
ATOM 1830 C LEU A 257 17.499 -32.268 -30.399 1.00 23.52 C
ANISOU 1830 C LEU A 257 2468 3538 2930 267 554 -1199 C
ATOM 1831 O LEU A 257 17.671 -31.919 -29.226 1.00 22.68 O
ANISOU 1831 O LEU A 257 2396 3417 2804 253 516 -1266 O
ATOM 1832 CB LEU A 257 18.655 -34.488 -30.511 1.00 21.19 C
ANISOU 1832 CB LEU A 257 2036 3333 2682 269 468 -1223 C
ATOM 1833 CG LEU A 257 17.377 -35.327 -30.502 1.00 23.52 C
ANISOU 1833 CG LEU A 257 2289 3568 3080 193 519 -1228 C
ATOM 1834 CD1 LEU A 257 16.944 -35.634 -31.924 1.00 21.17 C
ANISOU 1834 CD1 LEU A 257 1964 3268 2811 216 576 -1153 C
ATOM 1835 CD2 LEU A 257 17.573 -36.609 -29.704 1.00 21.94 C
ANISOU 1835 CD2 LEU A 257 2008 3388 2941 145 468 -1295 C
ATOM 1836 N ILE A 258 16.405 -31.966 -31.094 1.00 19.36 N
ANISOU 1836 N ILE A 258 1960 2956 2439 247 622 -1151 N
ATOM 1837 CA ILE A 258 15.315 -31.165 -30.545 1.00 19.01 C
ANISOU 1837 CA ILE A 258 1983 2831 2409 210 655 -1167 C
ATOM 1838 C ILE A 258 14.068 -32.037 -30.497 1.00 20.53 C
ANISOU 1838 C ILE A 258 2160 2958 2684 131 696 -1165 C
ATOM 1839 O ILE A 258 13.659 -32.599 -31.521 1.00 23.00 O
ANISOU 1839 O ILE A 258 2435 3274 3031 127 739 -1116 O
ATOM 1840 CB ILE A 258 15.071 -29.892 -31.369 1.00 19.73 C
ANISOU 1840 CB ILE A 258 2127 2909 2462 253 686 -1098 C
ATOM 1841 CG1 ILE A 258 16.367 -29.090 -31.493 1.00 21.28 C
ANISOU 1841 CG1 ILE A 258 2333 3178 2576 324 655 -1089 C
ATOM 1842 CG2 ILE A 258 13.989 -29.041 -30.724 1.00 18.12 C
ANISOU 1842 CG2 ILE A 258 1999 2617 2270 224 692 -1103 C
ATOM 1843 CD1 ILE A 258 16.231 -27.829 -32.332 1.00 29.36 C
ANISOU 1843 CD1 ILE A 258 3403 4186 3567 355 676 -1000 C
ATOM 1844 N LEU A 259 13.467 -32.149 -29.312 1.00 22.97 N
ANISOU 1844 N LEU A 259 2502 3205 3020 67 685 -1219 N
ATOM 1845 CA LEU A 259 12.332 -33.029 -29.071 1.00 19.42 C
ANISOU 1845 CA LEU A 259 2041 2695 2641 -21 726 -1224 C
ATOM 1846 C LEU A 259 11.248 -32.260 -28.326 1.00 31.53 C
ANISOU 1846 C LEU A 259 3674 4129 4175 -66 743 -1235 C
ATOM 1847 O LEU A 259 11.539 -31.313 -27.591 1.00 20.45 O
ANISOU 1847 O LEU A 259 2333 2705 2733 -37 702 -1268 O
ATOM 1848 CB LEU A 259 12.762 -34.264 -28.258 1.00 23.52 C
ANISOU 1848 CB LEU A 259 2489 3241 3207 -75 688 -1282 C
ATOM 1849 CG LEU A 259 12.340 -35.671 -28.692 1.00 38.27 C
ANISOU 1849 CG LEU A 259 4266 5126 5148 -127 728 -1276 C
ATOM 1850 CD1 LEU A 259 12.713 -35.917 -30.136 1.00 41.81 C
ANISOU 1850 CD1 LEU A 259 4661 5634 5592 -57 748 -1218 C
ATOM 1851 CD2 LEU A 259 12.974 -36.729 -27.786 1.00 38.67 C
ANISOU 1851 CD2 LEU A 259 4238 5214 5240 -171 673 -1345 C
ATOM 1852 N GLY A 260 9.998 -32.664 -28.518 1.00 19.19 N
ANISOU 1852 N GLY A 260 2132 2506 2655 -131 803 -1210 N
ATOM 1853 CA GLY A 260 8.901 -32.078 -27.777 1.00 24.92 C
ANISOU 1853 CA GLY A 260 2959 3129 3380 -182 816 -1217 C
ATOM 1854 C GLY A 260 7.621 -32.077 -28.590 1.00 20.96 C
ANISOU 1854 C GLY A 260 2494 2579 2891 -210 887 -1160 C
ATOM 1855 O GLY A 260 7.534 -32.689 -29.651 1.00 21.63 O
ANISOU 1855 O GLY A 260 2518 2707 2994 -202 931 -1124 O
ATOM 1856 N GLU A 261 6.627 -31.365 -28.059 1.00 24.10 N
ANISOU 1856 N GLU A 261 3359 3148 2649 235 1121 -1008 N
ATOM 1857 CA GLU A 261 5.298 -31.296 -28.651 1.00 25.97 C
ANISOU 1857 CA GLU A 261 3667 3373 2828 318 1185 -983 C
ATOM 1858 C GLU A 261 4.874 -29.846 -28.825 1.00 27.70 C
ANISOU 1858 C GLU A 261 4064 3501 2962 439 1147 -912 C
ATOM 1859 O GLU A 261 5.666 -28.928 -28.588 1.00 23.52 O
ANISOU 1859 O GLU A 261 3583 2926 2428 462 1068 -884 O
ATOM 1860 CB GLU A 261 4.281 -32.033 -27.773 1.00 27.23 C
ANISOU 1860 CB GLU A 261 3892 3507 2949 205 1361 -995 C
ATOM 1861 CG GLU A 261 4.820 -33.293 -27.121 1.00 33.51 C
ANISOU 1861 CG GLU A 261 4541 4363 3829 45 1416 -1065 C
ATOM 1862 CD GLU A 261 3.768 -34.038 -26.327 1.00 41.22 C
ANISOU 1862 CD GLU A 261 5573 5314 4775 -68 1601 -1074 C
ATOM 1863 OE1 GLU A 261 3.691 -33.836 -25.098 1.00 37.42 O
ANISOU 1863 OE1 GLU A 261 5209 4744 4266 -179 1690 -1056 O
ATOM 1864 OE2 GLU A 261 3.013 -34.826 -26.936 1.00 43.44 O
ANISOU 1864 OE2 GLU A 261 5782 5663 5062 -45 1663 -1098 O
ATOM 1865 N PHE A 262 3.622 -29.634 -29.230 1.00 24.31 N
ANISOU 1865 N PHE A 262 3724 3050 2464 518 1192 -881 N
ATOM 1866 CA PHE A 262 3.026 -28.310 -29.319 1.00 22.96 C
ANISOU 1866 CA PHE A 262 3678 2809 2238 602 1109 -793 C
ATOM 1867 C PHE A 262 1.721 -28.296 -28.537 1.00 30.69 C
ANISOU 1867 C PHE A 262 4805 3723 3132 561 1221 -745 C
ATOM 1868 O PHE A 262 1.005 -29.299 -28.476 1.00 25.06 O
ANISOU 1868 O PHE A 262 4071 3047 2405 515 1332 -772 O
ATOM 1869 CB PHE A 262 2.760 -27.899 -30.776 1.00 22.05 C
ANISOU 1869 CB PHE A 262 3478 2741 2161 724 975 -779 C
ATOM 1870 CG PHE A 262 3.986 -27.881 -31.634 1.00 26.13 C
ANISOU 1870 CG PHE A 262 3854 3307 2769 767 863 -810 C
ATOM 1871 CD1 PHE A 262 4.833 -26.785 -31.630 1.00 20.11 C
ANISOU 1871 CD1 PHE A 262 3113 2501 2028 792 763 -764 C
ATOM 1872 CD2 PHE A 262 4.294 -28.958 -32.445 1.00 23.80 C
ANISOU 1872 CD2 PHE A 262 3402 3099 2540 783 860 -876 C
ATOM 1873 CE1 PHE A 262 5.964 -26.768 -32.418 1.00 19.30 C
ANISOU 1873 CE1 PHE A 262 2887 2439 2006 829 663 -775 C
ATOM 1874 CE2 PHE A 262 5.422 -28.945 -33.236 1.00 25.04 C
ANISOU 1874 CE2 PHE A 262 3433 3294 2785 825 746 -882 C
ATOM 1875 CZ PHE A 262 6.257 -27.846 -33.223 1.00 19.39 C
ANISOU 1875 CZ PHE A 262 2750 2533 2084 846 649 -828 C
ATOM 1876 N LYS A 263 1.417 -27.141 -27.939 1.00 23.92 N
ANISOU 1876 N LYS A 263 4095 2769 2223 579 1194 -670 N
ATOM 1877 CA LYS A 263 0.171 -27.003 -27.189 1.00 27.93 C
ANISOU 1877 CA LYS A 263 4763 3201 2650 555 1294 -613 C
ATOM 1878 C LYS A 263 -1.051 -27.164 -28.083 1.00 27.29 C
ANISOU 1878 C LYS A 263 4671 3161 2537 638 1282 -596 C
ATOM 1879 O LYS A 263 -2.087 -27.667 -27.633 1.00 29.64 O
ANISOU 1879 O LYS A 263 5051 3436 2775 603 1400 -578 O
ATOM 1880 CB LYS A 263 0.122 -25.646 -26.490 1.00 24.72 C
ANISOU 1880 CB LYS A 263 4508 2683 2201 581 1249 -536 C
ATOM 1881 CG LYS A 263 0.984 -25.534 -25.246 1.00 25.51 C
ANISOU 1881 CG LYS A 263 4675 2713 2305 478 1305 -546 C
ATOM 1882 CD LYS A 263 0.959 -24.107 -24.721 1.00 24.62 C
ANISOU 1882 CD LYS A 263 4695 2501 2159 526 1239 -470 C
ATOM 1883 CE LYS A 263 1.471 -24.019 -23.293 1.00 33.50 C
ANISOU 1883 CE LYS A 263 5931 3531 3267 417 1323 -474 C
ATOM 1884 NZ LYS A 263 0.945 -22.807 -22.600 1.00 46.10 N
ANISOU 1884 NZ LYS A 263 7698 5009 4808 460 1308 -390 N
ATOM 1885 N ASP A 264 -0.958 -26.735 -29.342 1.00 30.55 N
ANISOU 1885 N ASP A 264 4986 3628 2991 741 1143 -602 N
ATOM 1886 CA ASP A 264 -2.091 -26.750 -30.260 1.00 29.92 C
ANISOU 1886 CA ASP A 264 4899 3581 2887 822 1113 -590 C
ATOM 1887 C ASP A 264 -2.110 -27.993 -31.146 1.00 31.32 C
ANISOU 1887 C ASP A 264 4921 3869 3110 822 1134 -670 C
ATOM 1888 O ASP A 264 -2.635 -27.950 -32.264 1.00 31.16 O
ANISOU 1888 O ASP A 264 4842 3890 3109 898 1061 -680 O
ATOM 1889 CB ASP A 264 -2.096 -25.485 -31.118 1.00 31.56 C
ANISOU 1889 CB ASP A 264 5103 3769 3121 922 957 -545 C
ATOM 1890 CG ASP A 264 -0.863 -25.367 -31.992 1.00 36.43 C
ANISOU 1890 CG ASP A 264 5565 4437 3841 938 843 -581 C
ATOM 1891 OD1 ASP A 264 0.250 -25.637 -31.495 1.00 37.48 O
ANISOU 1891 OD1 ASP A 264 5655 4577 4010 880 860 -612 O
ATOM 1892 OD2 ASP A 264 -1.003 -25.010 -33.180 1.00 39.36 O
ANISOU 1892 OD2 ASP A 264 5863 4835 4257 1006 739 -576 O
ATOM 1893 N GLU A 265 -1.549 -29.102 -30.667 1.00 32.86 N
ANISOU 1893 N GLU A 265 5047 4110 3329 735 1233 -728 N
ATOM 1894 CA GLU A 265 -1.605 -30.377 -31.366 1.00 34.45 C
ANISOU 1894 CA GLU A 265 5099 4419 3571 730 1271 -806 C
ATOM 1895 C GLU A 265 -1.904 -31.479 -30.358 1.00 44.03 C
ANISOU 1895 C GLU A 265 6335 5639 4754 612 1454 -823 C
ATOM 1896 O GLU A 265 -1.592 -31.349 -29.170 1.00 48.63 O
ANISOU 1896 O GLU A 265 7009 6149 5321 513 1537 -799 O
ATOM 1897 CB GLU A 265 -0.288 -30.690 -32.099 1.00 33.42 C
ANISOU 1897 CB GLU A 265 4796 4354 3548 747 1182 -871 C
ATOM 1898 CG GLU A 265 0.093 -29.716 -33.206 1.00 31.86 C
ANISOU 1898 CG GLU A 265 4555 4139 3412 836 1012 -849 C
ATOM 1899 CD GLU A 265 -0.685 -29.940 -34.488 1.00 38.64 C
ANISOU 1899 CD GLU A 265 5350 5031 4301 903 961 -861 C
ATOM 1900 OE1 GLU A 265 -0.824 -28.982 -35.275 1.00 42.62 O
ANISOU 1900 OE1 GLU A 265 5872 5493 4827 969 843 -810 O
ATOM 1901 OE2 GLU A 265 -1.153 -31.077 -34.717 1.00 38.88 O
ANISOU 1901 OE2 GLU A 265 5311 5129 4334 887 1040 -920 O
ATOM 1902 N ARG A 266 -2.519 -32.562 -30.835 1.00 47.59 N
ANISOU 1902 N ARG A 266 6698 6175 5208 612 1520 -868 N
ATOM 1903 CA ARG A 266 -2.804 -33.697 -29.963 1.00 49.30 C
ANISOU 1903 CA ARG A 266 6906 6405 5419 482 1700 -887 C
ATOM 1904 C ARG A 266 -1.507 -34.243 -29.380 1.00 43.78 C
ANISOU 1904 C ARG A 266 6101 5717 4814 360 1738 -945 C
ATOM 1905 O ARG A 266 -0.541 -34.487 -30.107 1.00 35.38 O
ANISOU 1905 O ARG A 266 4883 4721 3838 393 1644 -1005 O
ATOM 1906 CB ARG A 266 -3.547 -34.788 -30.735 1.00 54.14 C
ANISOU 1906 CB ARG A 266 7410 7126 6036 514 1744 -932 C
ATOM 1907 CG ARG A 266 -4.767 -34.307 -31.512 1.00 63.72 C
ANISOU 1907 CG ARG A 266 8694 8347 7168 636 1687 -902 C
ATOM 1908 CD ARG A 266 -6.076 -34.710 -30.846 1.00 71.26 C
ANISOU 1908 CD ARG A 266 9767 9279 8030 589 1839 -857 C
ATOM 1909 NE ARG A 266 -7.186 -34.706 -31.797 1.00 74.23 N
ANISOU 1909 NE ARG A 266 10149 9705 8351 696 1797 -863 N
ATOM 1910 CZ ARG A 266 -8.468 -34.698 -31.452 1.00 78.24 C
ANISOU 1910 CZ ARG A 266 10787 10182 8757 701 1886 -811 C
ATOM 1911 NH1 ARG A 266 -8.814 -34.681 -30.171 1.00 79.96 N
ANISOU 1911 NH1 ARG A 266 11145 10313 8923 606 2023 -744 N
ATOM 1912 NH2 ARG A 266 -9.408 -34.698 -32.386 1.00 77.74 N
ANISOU 1912 NH2 ARG A 266 10720 10167 8651 798 1840 -828 N
ATOM 1913 N ASN A 267 -1.488 -34.441 -28.067 1.00 36.91 N
ANISOU 1913 N ASN A 267 5310 4780 3935 212 1872 -934 N
ATOM 1914 CA ASN A 267 -0.252 -34.684 -27.342 1.00 39.83 C
ANISOU 1914 CA ASN A 267 5606 5142 4384 84 1894 -992 C
ATOM 1915 C ASN A 267 -0.198 -36.097 -26.773 1.00 40.07 C
ANISOU 1915 C ASN A 267 5504 5234 4487 -80 2039 -1066 C
ATOM 1916 O ASN A 267 -1.204 -36.811 -26.701 1.00 41.69 O
ANISOU 1916 O ASN A 267 5714 5461 4665 -110 2148 -1053 O
ATOM 1917 CB ASN A 267 -0.081 -33.667 -26.210 1.00 39.25 C
ANISOU 1917 CB ASN A 267 5722 4934 4256 35 1914 -933 C
ATOM 1918 CG ASN A 267 0.166 -32.262 -26.722 1.00 37.98 C
ANISOU 1918 CG ASN A 267 5651 4724 4055 182 1751 -873 C
ATOM 1919 OD1 ASN A 267 0.912 -32.061 -27.680 1.00 44.67 O
ANISOU 1919 OD1 ASN A 267 6386 5632 4953 272 1617 -904 O
ATOM 1920 ND2 ASN A 267 -0.462 -31.279 -26.085 1.00 31.22 N
ANISOU 1920 ND2 ASN A 267 4991 3756 3116 206 1758 -787 N
ATOM 1921 N LEU A 268 1.011 -36.487 -26.369 1.00 37.06 N
ANISOU 1921 N LEU A 268 4986 4883 4210 -181 1984 -1123 N
ATOM 1922 CA LEU A 268 1.226 -37.784 -25.744 1.00 37.96 C
ANISOU 1922 CA LEU A 268 4950 5056 4416 -347 2082 -1194 C
ATOM 1923 C LEU A 268 0.409 -37.909 -24.464 1.00 51.17 C
ANISOU 1923 C LEU A 268 6771 6633 6037 -485 2279 -1159 C
ATOM 1924 O LEU A 268 0.310 -36.967 -23.671 1.00 48.99 O
ANISOU 1924 O LEU A 268 6688 6233 5695 -501 2299 -1095 O
ATOM 1925 CB LEU A 268 2.714 -37.987 -25.433 1.00 36.49 C
ANISOU 1925 CB LEU A 268 4620 4905 4342 -421 1962 -1251 C
ATOM 1926 CG LEU A 268 3.543 -38.903 -26.343 1.00 34.61 C
ANISOU 1926 CG LEU A 268 4125 4808 4216 -393 1849 -1335 C
ATOM 1927 CD1 LEU A 268 3.560 -38.370 -27.764 1.00 31.63 C
ANISOU 1927 CD1 LEU A 268 3729 4472 3816 -201 1712 -1311 C
ATOM 1928 CD2 LEU A 268 4.965 -39.078 -25.818 1.00 37.49 C
ANISOU 1928 CD2 LEU A 268 4376 5195 4674 -479 1745 -1388 C
ATOM 1929 N GLU A 269 -0.176 -39.090 -24.267 1.00 60.88 N
ANISOU 1929 N GLU A 269 7908 7920 7303 -584 2427 -1202 N
ATOM 1930 CA GLU A 269 -0.930 -39.360 -23.049 1.00 68.19 C
ANISOU 1930 CA GLU A 269 8954 8759 8196 -733 2629 -1172 C
ATOM 1931 C GLU A 269 -0.047 -39.213 -21.816 1.00 66.33 C
ANISOU 1931 C GLU A 269 8732 8444 8027 -885 2623 -1189 C
ATOM 1932 O GLU A 269 -0.373 -38.463 -20.888 1.00 66.85 O
ANISOU 1932 O GLU A 269 9003 8373 8026 -929 2691 -1123 O
ATOM 1933 CB GLU A 269 -1.539 -40.761 -23.127 1.00 78.83 C
ANISOU 1933 CB GLU A 269 10154 10195 9602 -811 2742 -1213 C
ATOM 1934 CG GLU A 269 -2.296 -41.210 -21.890 1.00 89.37 C
ANISOU 1934 CG GLU A 269 11582 11443 10930 -973 2934 -1178 C
ATOM 1935 CD GLU A 269 -2.851 -42.609 -22.048 1.00 95.85 C
ANISOU 1935 CD GLU A 269 12243 12360 11814 -1038 3029 -1221 C
ATOM 1936 OE1 GLU A 269 -2.546 -43.252 -23.073 1.00 96.79 O
ANISOU 1936 OE1 GLU A 269 12170 12614 11990 -964 2941 -1286 O
ATOM 1937 OE2 GLU A 269 -3.589 -43.069 -21.154 1.00 98.59 O
ANISOU 1937 OE2 GLU A 269 12658 12645 12157 -1159 3188 -1188 O
ATOM 1938 N ILE A 270 1.084 -39.917 -21.791 1.00 65.31 N
ANISOU 1938 N ILE A 270 8387 8400 8030 -961 2535 -1282 N
ATOM 1939 CA ILE A 270 2.040 -39.848 -20.693 1.00 63.71 C
ANISOU 1939 CA ILE A 270 8171 8138 7899 -1100 2506 -1318 C
ATOM 1940 C ILE A 270 3.437 -39.744 -21.288 1.00 58.63 C
ANISOU 1940 C ILE A 270 7370 7578 7327 -1035 2290 -1376 C
ATOM 1941 O ILE A 270 3.712 -40.275 -22.368 1.00 61.53 O
ANISOU 1941 O ILE A 270 7569 8071 7740 -948 2202 -1420 O
ATOM 1942 CB ILE A 270 1.924 -41.073 -19.750 1.00 67.14 C
ANISOU 1942 CB ILE A 270 8490 8586 8432 -1310 2663 -1388 C
ATOM 1943 CG1 ILE A 270 0.490 -41.235 -19.244 1.00 68.61 C
ANISOU 1943 CG1 ILE A 270 8830 8696 8544 -1370 2891 -1323 C
ATOM 1944 CG2 ILE A 270 2.871 -40.950 -18.562 1.00 66.08 C
ANISOU 1944 CG2 ILE A 270 8356 8380 8371 -1454 2632 -1431 C
ATOM 1945 CD1 ILE A 270 0.278 -42.453 -18.370 1.00 73.34 C
ANISOU 1945 CD1 ILE A 270 9313 9308 9244 -1578 3065 -1386 C
ATOM 1946 N PHE A 271 4.322 -39.036 -20.583 1.00 49.37 N
ANISOU 1946 N PHE A 271 6265 6332 6162 -1071 2206 -1373 N
ATOM 1947 CA PHE A 271 5.719 -38.871 -20.989 1.00 47.58 C
ANISOU 1947 CA PHE A 271 5911 6173 5993 -1019 2007 -1422 C
ATOM 1948 C PHE A 271 6.601 -39.293 -19.815 1.00 55.35 C
ANISOU 1948 C PHE A 271 6829 7137 7066 -1188 2007 -1498 C
ATOM 1949 O PHE A 271 6.928 -38.482 -18.944 1.00 53.26 O
ANISOU 1949 O PHE A 271 6707 6762 6766 -1228 1995 -1472 O
ATOM 1950 CB PHE A 271 6.003 -37.431 -21.427 1.00 47.62 C
ANISOU 1950 CB PHE A 271 6069 6116 5907 -864 1881 -1343 C
ATOM 1951 CG PHE A 271 7.238 -37.278 -22.285 1.00 56.48 C
ANISOU 1951 CG PHE A 271 7055 7331 7073 -763 1681 -1373 C
ATOM 1952 CD1 PHE A 271 8.279 -38.194 -22.219 1.00 59.04 C
ANISOU 1952 CD1 PHE A 271 7172 7753 7506 -835 1606 -1468 C
ATOM 1953 CD2 PHE A 271 7.353 -36.213 -23.161 1.00 59.32 C
ANISOU 1953 CD2 PHE A 271 7496 7677 7367 -593 1568 -1306 C
ATOM 1954 CE1 PHE A 271 9.409 -38.048 -23.005 1.00 58.30 C
ANISOU 1954 CE1 PHE A 271 6966 7741 7446 -737 1425 -1488 C
ATOM 1955 CE2 PHE A 271 8.481 -36.063 -23.951 1.00 60.07 C
ANISOU 1955 CE2 PHE A 271 7472 7849 7502 -503 1394 -1325 C
ATOM 1956 CZ PHE A 271 9.510 -36.982 -23.872 1.00 58.98 C
ANISOU 1956 CZ PHE A 271 7139 7806 7463 -573 1324 -1412 C
ATOM 1957 N GLU A 272 6.989 -40.560 -19.804 1.00 59.80 N
ANISOU 1957 N GLU A 272 7169 7808 7744 -1283 2014 -1598 N
ATOM 1958 CA GLU A 272 7.928 -41.077 -18.825 1.00 59.83 C
ANISOU 1958 CA GLU A 272 7070 7816 7846 -1435 1988 -1691 C
ATOM 1959 C GLU A 272 9.341 -41.057 -19.391 1.00 54.69 C
ANISOU 1959 C GLU A 272 6276 7264 7240 -1356 1774 -1746 C
ATOM 1960 O GLU A 272 9.534 -40.987 -20.609 1.00 54.43 O
ANISOU 1960 O GLU A 272 6173 7317 7191 -1206 1667 -1726 O
ATOM 1961 CB GLU A 272 7.539 -42.498 -18.425 1.00 65.58 C
ANISOU 1961 CB GLU A 272 7629 8606 8682 -1591 2122 -1777 C
ATOM 1962 CG GLU A 272 6.239 -42.593 -17.637 1.00 80.40 C
ANISOU 1962 CG GLU A 272 9648 10376 10525 -1703 2351 -1728 C
ATOM 1963 CD GLU A 272 5.892 -44.019 -17.269 1.00 92.88 C
ANISOU 1963 CD GLU A 272 11046 12024 12221 -1861 2490 -1816 C
ATOM 1964 OE1 GLU A 272 6.512 -44.941 -17.838 1.00 96.74 O
ANISOU 1964 OE1 GLU A 272 11294 12656 12805 -1854 2405 -1910 O
ATOM 1965 OE2 GLU A 272 5.006 -44.222 -16.412 1.00 96.96 O
ANISOU 1965 OE2 GLU A 272 11657 12448 12734 -1992 2684 -1790 O
ATOM 1966 N PRO A 273 10.358 -41.087 -18.527 1.00 48.65 N
ANISOU 1966 N PRO A 273 5474 6484 6528 -1451 1705 -1813 N
ATOM 1967 CA PRO A 273 11.740 -41.132 -19.037 1.00 48.12 C
ANISOU 1967 CA PRO A 273 5269 6518 6497 -1376 1502 -1866 C
ATOM 1968 C PRO A 273 12.027 -42.342 -19.912 1.00 46.91 C
ANISOU 1968 C PRO A 273 4863 6525 6436 -1350 1445 -1943 C
ATOM 1969 O PRO A 273 12.812 -42.239 -20.863 1.00 47.58 O
ANISOU 1969 O PRO A 273 4864 6696 6520 -1218 1285 -1942 O
ATOM 1970 CB PRO A 273 12.578 -41.145 -17.753 1.00 49.17 C
ANISOU 1970 CB PRO A 273 5405 6602 6676 -1515 1477 -1941 C
ATOM 1971 CG PRO A 273 11.731 -40.455 -16.751 1.00 51.45 C
ANISOU 1971 CG PRO A 273 5917 6726 6906 -1597 1625 -1880 C
ATOM 1972 CD PRO A 273 10.316 -40.842 -17.074 1.00 48.98 C
ANISOU 1972 CD PRO A 273 5635 6399 6576 -1607 1796 -1828 C
ATOM 1973 N SER A 274 11.406 -43.489 -19.618 1.00 44.01 N
ANISOU 1973 N SER A 274 4372 6198 6151 -1471 1576 -2009 N
ATOM 1974 CA SER A 274 11.665 -44.706 -20.381 1.00 45.42 C
ANISOU 1974 CA SER A 274 4300 6532 6427 -1452 1527 -2094 C
ATOM 1975 C SER A 274 11.203 -44.598 -21.828 1.00 43.93 C
ANISOU 1975 C SER A 274 4095 6406 6192 -1275 1489 -2032 C
ATOM 1976 O SER A 274 11.608 -45.420 -22.658 1.00 47.44 O
ANISOU 1976 O SER A 274 4341 6978 6704 -1217 1405 -2092 O
ATOM 1977 CB SER A 274 10.990 -45.903 -19.709 1.00 45.04 C
ANISOU 1977 CB SER A 274 4132 6507 6475 -1625 1697 -2174 C
ATOM 1978 OG SER A 274 9.651 -46.042 -20.149 1.00 49.00 O
ANISOU 1978 OG SER A 274 4691 6994 6933 -1600 1854 -2113 O
ATOM 1979 N ILE A 275 10.358 -43.614 -22.147 1.00 42.41 N
ANISOU 1979 N ILE A 275 4105 6123 5887 -1187 1546 -1918 N
ATOM 1980 CA ILE A 275 10.024 -43.343 -23.541 1.00 44.52 C
ANISOU 1980 CA ILE A 275 4370 6437 6107 -1007 1485 -1860 C
ATOM 1981 C ILE A 275 11.285 -43.033 -24.337 1.00 41.69 C
ANISOU 1981 C ILE A 275 3933 6144 5762 -881 1270 -1865 C
ATOM 1982 O ILE A 275 11.391 -43.389 -25.518 1.00 47.54 O
ANISOU 1982 O ILE A 275 4558 6975 6529 -762 1189 -1871 O
ATOM 1983 CB ILE A 275 8.991 -42.197 -23.617 1.00 46.65 C
ANISOU 1983 CB ILE A 275 4888 6588 6250 -936 1568 -1740 C
ATOM 1984 CG1 ILE A 275 7.611 -42.699 -23.184 1.00 53.10 C
ANISOU 1984 CG1 ILE A 275 5758 7369 7050 -1026 1783 -1730 C
ATOM 1985 CG2 ILE A 275 8.933 -41.588 -25.010 1.00 42.49 C
ANISOU 1985 CG2 ILE A 275 4384 6091 5671 -737 1459 -1677 C
ATOM 1986 CD1 ILE A 275 6.541 -41.635 -23.222 1.00 52.64 C
ANISOU 1986 CD1 ILE A 275 5945 7196 6860 -954 1867 -1616 C
ATOM 1987 N MET A 276 12.276 -42.408 -23.699 1.00 35.62 N
ANISOU 1987 N MET A 276 3224 5333 4979 -906 1177 -1864 N
ATOM 1988 CA MET A 276 13.521 -42.028 -24.351 1.00 36.48 C
ANISOU 1988 CA MET A 276 3278 5494 5087 -791 981 -1859 C
ATOM 1989 C MET A 276 14.650 -43.025 -24.103 1.00 36.65 C
ANISOU 1989 C MET A 276 3094 5623 5209 -854 880 -1973 C
ATOM 1990 O MET A 276 15.823 -42.650 -24.197 1.00 38.91 O
ANISOU 1990 O MET A 276 3365 5933 5485 -798 729 -1976 O
ATOM 1991 CB MET A 276 13.957 -40.638 -23.891 1.00 43.71 C
ANISOU 1991 CB MET A 276 4393 6303 5911 -757 931 -1784 C
ATOM 1992 CG MET A 276 12.881 -39.575 -23.979 1.00 49.88 C
ANISOU 1992 CG MET A 276 5390 6970 6592 -701 1025 -1677 C
ATOM 1993 SD MET A 276 13.513 -37.964 -23.476 1.00 57.32 S
ANISOU 1993 SD MET A 276 6543 7799 7437 -652 952 -1600 S
ATOM 1994 CE MET A 276 14.453 -38.419 -22.020 1.00 59.68 C
ANISOU 1994 CE MET A 276 6797 8092 7788 -822 943 -1698 C
ATOM 1995 N GLU A 277 14.322 -44.281 -23.784 1.00 40.73 N
ANISOU 1995 N GLU A 277 3450 6206 5819 -965 962 -2069 N
ATOM 1996 CA GLU A 277 15.360 -45.293 -23.603 1.00 45.72 C
ANISOU 1996 CA GLU A 277 3869 6950 6553 -1017 860 -2187 C
ATOM 1997 C GLU A 277 16.196 -45.469 -24.864 1.00 39.51 C
ANISOU 1997 C GLU A 277 2960 6268 5784 -854 681 -2186 C
ATOM 1998 O GLU A 277 17.385 -45.802 -24.780 1.00 37.09 O
ANISOU 1998 O GLU A 277 2542 6033 5518 -847 540 -2249 O
ATOM 1999 CB GLU A 277 14.730 -46.628 -23.198 1.00 50.47 C
ANISOU 1999 CB GLU A 277 4306 7610 7259 -1152 988 -2288 C
ATOM 2000 CG GLU A 277 15.038 -47.056 -21.774 1.00 61.52 C
ANISOU 2000 CG GLU A 277 5670 8982 8721 -1343 1042 -2380 C
ATOM 2001 CD GLU A 277 16.520 -47.272 -21.540 1.00 71.60 C
ANISOU 2001 CD GLU A 277 6834 10330 10042 -1340 858 -2464 C
ATOM 2002 OE1 GLU A 277 17.180 -47.871 -22.415 1.00 77.06 O
ANISOU 2002 OE1 GLU A 277 7357 11143 10779 -1241 724 -2506 O
ATOM 2003 OE2 GLU A 277 17.027 -46.834 -20.487 1.00 71.58 O
ANISOU 2003 OE2 GLU A 277 6914 10259 10024 -1430 843 -2487 O
ATOM 2004 N GLY A 278 15.598 -45.249 -26.035 1.00 35.03 N
ANISOU 2004 N GLY A 278 2414 5709 5185 -721 683 -2115 N
ATOM 2005 CA GLY A 278 16.337 -45.399 -27.276 1.00 34.25 C
ANISOU 2005 CA GLY A 278 2207 5697 5108 -565 520 -2107 C
ATOM 2006 C GLY A 278 17.477 -44.410 -27.424 1.00 39.53 C
ANISOU 2006 C GLY A 278 2965 6338 5716 -476 366 -2047 C
ATOM 2007 O GLY A 278 18.472 -44.704 -28.092 1.00 43.72 O
ANISOU 2007 O GLY A 278 3383 6949 6278 -386 213 -2065 O
ATOM 2008 N LEU A 279 17.356 -43.232 -26.803 1.00 34.94 N
ANISOU 2008 N LEU A 279 2590 5642 5044 -497 407 -1972 N
ATOM 2009 CA LEU A 279 18.374 -42.193 -26.929 1.00 31.27 C
ANISOU 2009 CA LEU A 279 2224 5146 4512 -410 277 -1908 C
ATOM 2010 C LEU A 279 19.731 -42.620 -26.391 1.00 35.75 C
ANISOU 2010 C LEU A 279 2690 5782 5111 -449 152 -1987 C
ATOM 2011 O LEU A 279 20.720 -41.919 -26.635 1.00 35.78 O
ANISOU 2011 O LEU A 279 2746 5785 5063 -362 28 -1940 O
ATOM 2012 CB LEU A 279 17.926 -40.922 -26.210 1.00 30.59 C
ANISOU 2012 CB LEU A 279 2370 4924 4329 -441 358 -1830 C
ATOM 2013 CG LEU A 279 16.659 -40.269 -26.753 1.00 31.19 C
ANISOU 2013 CG LEU A 279 2576 4923 4352 -379 462 -1740 C
ATOM 2014 CD1 LEU A 279 16.438 -38.931 -26.076 1.00 28.99 C
ANISOU 2014 CD1 LEU A 279 2524 4516 3975 -388 509 -1663 C
ATOM 2015 CD2 LEU A 279 16.747 -40.110 -28.260 1.00 28.58 C
ANISOU 2015 CD2 LEU A 279 2196 4637 4027 -212 367 -1685 C
ATOM 2016 N CYS A 280 19.804 -43.738 -25.663 1.00 37.09 N
ANISOU 2016 N CYS A 280 2718 6012 5363 -577 183 -2106 N
ATOM 2017 CA CYS A 280 21.090 -44.224 -25.177 1.00 35.69 C
ANISOU 2017 CA CYS A 280 2431 5911 5220 -608 53 -2195 C
ATOM 2018 C CYS A 280 21.964 -44.745 -26.309 1.00 38.91 C
ANISOU 2018 C CYS A 280 2688 6433 5662 -470 -110 -2204 C
ATOM 2019 O CYS A 280 23.194 -44.726 -26.197 1.00 41.35 O
ANISOU 2019 O CYS A 280 2978 6784 5951 -429 -249 -2221 O
ATOM 2020 CB CYS A 280 20.875 -45.314 -24.130 1.00 39.12 C
ANISOU 2020 CB CYS A 280 2739 6379 5746 -783 131 -2328 C
ATOM 2021 SG CYS A 280 20.958 -44.747 -22.415 1.00 59.04 S
ANISOU 2021 SG CYS A 280 5406 8792 8234 -951 207 -2363 S
ATOM 2022 N ASP A 281 21.360 -45.216 -27.399 1.00 41.34 N
ANISOU 2022 N ASP A 281 2933 6771 6005 -385 -91 -2172 N
ATOM 2023 CA ASP A 281 22.112 -45.677 -28.555 1.00 42.57 C
ANISOU 2023 CA ASP A 281 3076 6949 6148 -227 -221 -2107 C
ATOM 2024 C ASP A 281 22.370 -44.562 -29.562 1.00 41.45 C
ANISOU 2024 C ASP A 281 3042 6767 5940 -80 -294 -1984 C
ATOM 2025 O ASP A 281 22.696 -44.844 -30.721 1.00 39.14 O
ANISOU 2025 O ASP A 281 2764 6466 5640 46 -367 -1908 O
ATOM 2026 CB ASP A 281 21.386 -46.845 -29.227 1.00 46.54 C
ANISOU 2026 CB ASP A 281 3500 7472 6709 -209 -169 -2120 C
ATOM 2027 CG ASP A 281 21.220 -48.040 -28.303 1.00 60.23 C
ANISOU 2027 CG ASP A 281 5122 9250 8514 -343 -105 -2237 C
ATOM 2028 OD1 ASP A 281 22.076 -48.233 -27.415 1.00 63.41 O
ANISOU 2028 OD1 ASP A 281 5496 9674 8924 -407 -157 -2297 O
ATOM 2029 OD2 ASP A 281 20.235 -48.790 -28.466 1.00 65.61 O
ANISOU 2029 OD2 ASP A 281 5745 9940 9242 -382 -2 -2267 O
ATOM 2030 N VAL A 282 22.226 -43.307 -29.144 1.00 38.33 N
ANISOU 2030 N VAL A 282 2727 6337 5497 -98 -270 -1962 N
ATOM 2031 CA VAL A 282 22.504 -42.143 -29.975 1.00 30.13 C
ANISOU 2031 CA VAL A 282 1818 5244 4388 38 -331 -1835 C
ATOM 2032 C VAL A 282 23.546 -41.289 -29.265 1.00 29.41 C
ANISOU 2032 C VAL A 282 1838 5122 4216 31 -399 -1808 C
ATOM 2033 O VAL A 282 23.473 -41.096 -28.046 1.00 33.85 O
ANISOU 2033 O VAL A 282 2471 5641 4749 -89 -335 -1850 O
ATOM 2034 CB VAL A 282 21.224 -41.324 -30.256 1.00 30.92 C
ANISOU 2034 CB VAL A 282 2061 5240 4446 54 -203 -1752 C
ATOM 2035 CG1 VAL A 282 21.525 -40.141 -31.169 1.00 27.88 C
ANISOU 2035 CG1 VAL A 282 1790 4800 4002 196 -271 -1629 C
ATOM 2036 CG2 VAL A 282 20.143 -42.211 -30.860 1.00 33.41 C
ANISOU 2036 CG2 VAL A 282 2271 5590 4833 54 -124 -1790 C
ATOM 2037 N THR A 283 24.523 -40.793 -30.020 1.00 31.92 N
ANISOU 2037 N THR A 283 2171 5460 4498 159 -528 -1739 N
ATOM 2038 CA THR A 283 25.499 -39.841 -29.500 1.00 38.18 C
ANISOU 2038 CA THR A 283 3085 6221 5200 176 -590 -1695 C
ATOM 2039 C THR A 283 24.970 -38.438 -29.763 1.00 36.21 C
ANISOU 2039 C THR A 283 3021 5858 4878 229 -525 -1575 C
ATOM 2040 O THR A 283 24.807 -38.039 -30.922 1.00 31.59 O
ANISOU 2040 O THR A 283 2447 5257 4299 345 -551 -1490 O
ATOM 2041 CB THR A 283 26.876 -40.028 -30.139 1.00 42.88 C
ANISOU 2041 CB THR A 283 3649 6867 5775 286 -736 -1653 C
ATOM 2042 OG1 THR A 283 26.939 -39.299 -31.367 1.00 60.64 O
ANISOU 2042 OG1 THR A 283 5986 9058 7996 417 -756 -1513 O
ATOM 2043 CG2 THR A 283 27.143 -41.490 -30.431 1.00 29.76 C
ANISOU 2043 CG2 THR A 283 1890 5242 4175 279 -756 -1688 C
ATOM 2044 N ILE A 284 24.702 -37.695 -28.693 1.00 39.54 N
ANISOU 2044 N ILE A 284 3585 6200 5237 145 -444 -1573 N
ATOM 2045 CA ILE A 284 24.058 -36.390 -28.765 1.00 31.60 C
ANISOU 2045 CA ILE A 284 2758 5083 4166 180 -368 -1474 C
ATOM 2046 C ILE A 284 24.986 -35.369 -28.121 1.00 37.14 C
ANISOU 2046 C ILE A 284 3585 5749 4776 191 -412 -1439 C
ATOM 2047 O ILE A 284 25.349 -35.509 -26.947 1.00 36.83 O
ANISOU 2047 O ILE A 284 3570 5709 4714 92 -403 -1512 O
ATOM 2048 CB ILE A 284 22.688 -36.399 -28.067 1.00 26.79 C
ANISOU 2048 CB ILE A 284 2220 4398 3563 73 -211 -1499 C
ATOM 2049 CG1 ILE A 284 21.823 -37.544 -28.602 1.00 26.38 C
ANISOU 2049 CG1 ILE A 284 2029 4395 3599 52 -162 -1548 C
ATOM 2050 CG2 ILE A 284 21.987 -35.066 -28.242 1.00 24.69 C
ANISOU 2050 CG2 ILE A 284 2131 4020 3229 127 -144 -1397 C
ATOM 2051 CD1 ILE A 284 20.560 -37.788 -27.800 1.00 29.11 C
ANISOU 2051 CD1 ILE A 284 2425 4683 3954 -69 -3 -1586 C
ATOM 2052 N ASP A 285 25.377 -34.347 -28.885 1.00 36.85 N
ANISOU 2052 N ASP A 285 3627 5683 4690 312 -459 -1333 N
ATOM 2053 CA ASP A 285 26.172 -33.266 -28.311 1.00 35.11 C
ANISOU 2053 CA ASP A 285 3538 5425 4377 331 -486 -1293 C
ATOM 2054 C ASP A 285 25.292 -32.271 -27.571 1.00 33.70 C
ANISOU 2054 C ASP A 285 3529 5130 4147 281 -369 -1265 C
ATOM 2055 O ASP A 285 25.616 -31.864 -26.449 1.00 28.52 O
ANISOU 2055 O ASP A 285 2964 4439 3435 215 -349 -1299 O
ATOM 2056 CB ASP A 285 26.973 -32.553 -29.401 1.00 31.30 C
ANISOU 2056 CB ASP A 285 3070 4957 3865 476 -575 -1188 C
ATOM 2057 CG ASP A 285 27.866 -33.493 -30.180 1.00 40.59 C
ANISOU 2057 CG ASP A 285 4093 6242 5089 537 -695 -1204 C
ATOM 2058 OD1 ASP A 285 28.190 -34.576 -29.654 1.00 47.17 O
ANISOU 2058 OD1 ASP A 285 4818 7149 5954 469 -732 -1305 O
ATOM 2059 OD2 ASP A 285 28.250 -33.149 -31.317 1.00 46.27 O
ANISOU 2059 OD2 ASP A 285 4796 6969 5815 655 -754 -1116 O
ATOM 2060 N GLU A 286 24.177 -31.873 -28.178 1.00 31.41 N
ANISOU 2060 N GLU A 286 3284 4776 3874 318 -295 -1207 N
ATOM 2061 CA GLU A 286 23.262 -30.913 -27.579 1.00 31.66 C
ANISOU 2061 CA GLU A 286 3479 4695 3855 288 -187 -1174 C
ATOM 2062 C GLU A 286 21.849 -31.472 -27.631 1.00 34.18 C
ANISOU 2062 C GLU A 286 3783 4983 4222 234 -82 -1198 C
ATOM 2063 O GLU A 286 21.405 -31.949 -28.680 1.00 30.08 O
ANISOU 2063 O GLU A 286 3172 4499 3758 291 -93 -1182 O
ATOM 2064 CB GLU A 286 23.328 -29.563 -28.299 1.00 36.24 C
ANISOU 2064 CB GLU A 286 4162 5220 4387 410 -205 -1064 C
ATOM 2065 CG GLU A 286 24.737 -29.011 -28.439 1.00 48.31 C
ANISOU 2065 CG GLU A 286 5698 6788 5869 479 -305 -1027 C
ATOM 2066 CD GLU A 286 24.753 -27.593 -28.954 1.00 57.11 C
ANISOU 2066 CD GLU A 286 6924 7838 6937 581 -302 -924 C
ATOM 2067 OE1 GLU A 286 23.700 -27.123 -29.426 1.00 56.17 O
ANISOU 2067 OE1 GLU A 286 6853 7655 6834 615 -242 -882 O
ATOM 2068 OE2 GLU A 286 25.816 -26.946 -28.883 1.00 59.20 O
ANISOU 2068 OE2 GLU A 286 7227 8119 7146 630 -358 -889 O
ATOM 2069 N PHE A 287 21.149 -31.408 -26.501 1.00 28.54 N
ANISOU 2069 N PHE A 287 3163 4198 3483 126 23 -1236 N
ATOM 2070 CA PHE A 287 19.782 -31.901 -26.389 1.00 26.48 C
ANISOU 2070 CA PHE A 287 2908 3899 3252 65 141 -1255 C
ATOM 2071 C PHE A 287 18.861 -30.750 -26.007 1.00 26.42 C
ANISOU 2071 C PHE A 287 3092 3769 3175 79 232 -1193 C
ATOM 2072 O PHE A 287 19.085 -30.080 -24.993 1.00 27.14 O
ANISOU 2072 O PHE A 287 3307 3793 3212 32 258 -1195 O
ATOM 2073 CB PHE A 287 19.686 -33.027 -25.353 1.00 24.77 C
ANISOU 2073 CB PHE A 287 2622 3710 3081 -89 196 -1361 C
ATOM 2074 CG PHE A 287 18.317 -33.646 -25.248 1.00 25.27 C
ANISOU 2074 CG PHE A 287 2679 3745 3177 -156 327 -1381 C
ATOM 2075 CD1 PHE A 287 17.909 -34.609 -26.157 1.00 25.90 C
ANISOU 2075 CD1 PHE A 287 2614 3903 3326 -130 325 -1402 C
ATOM 2076 CD2 PHE A 287 17.439 -33.270 -24.240 1.00 32.80 C
ANISOU 2076 CD2 PHE A 287 3779 4594 4092 -244 453 -1377 C
ATOM 2077 CE1 PHE A 287 16.653 -35.183 -26.068 1.00 28.79 C
ANISOU 2077 CE1 PHE A 287 2976 4248 3714 -188 451 -1421 C
ATOM 2078 CE2 PHE A 287 16.176 -33.841 -24.146 1.00 31.34 C
ANISOU 2078 CE2 PHE A 287 3597 4383 3929 -304 581 -1388 C
ATOM 2079 CZ PHE A 287 15.785 -34.799 -25.062 1.00 33.90 C
ANISOU 2079 CZ PHE A 287 3772 4793 4316 -276 582 -1411 C
ATOM 2080 N ARG A 288 17.830 -30.523 -26.821 1.00 23.71 N
ANISOU 2080 N ARG A 288 2775 3397 2835 149 276 -1141 N
ATOM 2081 CA ARG A 288 16.812 -29.515 -26.550 1.00 23.03 C
ANISOU 2081 CA ARG A 288 2866 3200 2685 172 363 -1085 C
ATOM 2082 C ARG A 288 15.469 -30.197 -26.330 1.00 28.28 C
ANISOU 2082 C ARG A 288 3542 3840 3363 105 486 -1110 C
ATOM 2083 O ARG A 288 14.997 -30.944 -27.195 1.00 33.14 O
ANISOU 2083 O ARG A 288 4049 4515 4028 136 488 -1122 O
ATOM 2084 CB ARG A 288 16.699 -28.499 -27.693 1.00 29.80 C
ANISOU 2084 CB ARG A 288 3763 4038 3522 325 307 -1000 C
ATOM 2085 CG ARG A 288 17.880 -27.552 -27.820 1.00 31.31 C
ANISOU 2085 CG ARG A 288 3983 4230 3683 395 212 -958 C
ATOM 2086 CD ARG A 288 17.426 -26.112 -28.017 1.00 30.12 C
ANISOU 2086 CD ARG A 288 3980 3991 3475 488 227 -882 C
ATOM 2087 NE ARG A 288 18.106 -25.499 -29.151 1.00 37.30 N
ANISOU 2087 NE ARG A 288 4839 4932 4403 610 130 -823 N
ATOM 2088 CZ ARG A 288 17.498 -25.074 -30.255 1.00 40.85 C
ANISOU 2088 CZ ARG A 288 5280 5366 4876 712 115 -775 C
ATOM 2089 NH1 ARG A 288 16.182 -25.173 -30.371 1.00 40.11 N
ANISOU 2089 NH1 ARG A 288 5232 5230 4777 715 186 -779 N
ATOM 2090 NH2 ARG A 288 18.208 -24.538 -31.237 1.00 54.94 N
ANISOU 2090 NH2 ARG A 288 7013 7175 6687 811 29 -723 N
ATOM 2091 N LEU A 289 14.860 -29.945 -25.177 1.00 23.01 N
ANISOU 2091 N LEU A 289 3010 3082 2650 16 591 -1117 N
ATOM 2092 CA LEU A 289 13.504 -30.386 -24.892 1.00 24.61 C
ANISOU 2092 CA LEU A 289 3263 3241 2846 -41 725 -1122 C
ATOM 2093 C LEU A 289 12.585 -29.175 -24.869 1.00 23.19 C
ANISOU 2093 C LEU A 289 3277 2951 2581 36 776 -1044 C
ATOM 2094 O LEU A 289 12.894 -28.166 -24.229 1.00 24.26 O
ANISOU 2094 O LEU A 289 3546 3010 2663 46 766 -1014 O
ATOM 2095 CB LEU A 289 13.421 -31.131 -23.556 1.00 29.21 C
ANISOU 2095 CB LEU A 289 3853 3798 3449 -212 819 -1189 C
ATOM 2096 CG LEU A 289 12.036 -31.640 -23.152 1.00 31.27 C
ANISOU 2096 CG LEU A 289 4171 4008 3701 -287 975 -1191 C
ATOM 2097 CD1 LEU A 289 11.532 -32.674 -24.154 1.00 26.82 C
ANISOU 2097 CD1 LEU A 289 3454 3543 3193 -260 988 -1215 C
ATOM 2098 CD2 LEU A 289 12.061 -32.217 -21.750 1.00 37.55 C
ANISOU 2098 CD2 LEU A 289 4986 4760 4522 -462 1067 -1252 C
ATOM 2099 N THR A 290 11.466 -29.271 -25.576 1.00 24.96 N
ANISOU 2099 N THR A 290 3517 3172 2793 96 827 -1015 N
ATOM 2100 CA THR A 290 10.485 -28.197 -25.625 1.00 23.00 C
ANISOU 2100 CA THR A 290 3447 2827 2464 178 873 -947 C
ATOM 2101 C THR A 290 9.218 -28.651 -24.902 1.00 24.82 C
ANISOU 2101 C THR A 290 3773 2999 2658 95 1027 -950 C
ATOM 2102 O THR A 290 9.216 -29.665 -24.196 1.00 24.65 O
ANISOU 2102 O THR A 290 3692 2998 2677 -41 1101 -1005 O
ATOM 2103 CB THR A 290 10.200 -27.787 -27.070 1.00 23.60 C
ANISOU 2103 CB THR A 290 3481 2940 2545 333 798 -907 C
ATOM 2104 OG1 THR A 290 9.410 -28.797 -27.710 1.00 21.81 O
ANISOU 2104 OG1 THR A 290 3161 2774 2351 332 845 -935 O
ATOM 2105 CG2 THR A 290 11.507 -27.600 -27.833 1.00 20.53 C
ANISOU 2105 CG2 THR A 290 2970 2622 2210 397 656 -907 C
ATOM 2106 N TYR A 291 8.141 -27.882 -25.077 1.00 23.30 N
ANISOU 2106 N TYR A 291 3731 2732 2389 178 1074 -892 N
ATOM 2107 CA TYR A 291 6.885 -28.167 -24.392 1.00 24.36 C
ANISOU 2107 CA TYR A 291 3987 2799 2471 115 1224 -879 C
ATOM 2108 C TYR A 291 6.467 -29.617 -24.593 1.00 26.08 C
ANISOU 2108 C TYR A 291 4066 3099 2744 33 1300 -931 C
ATOM 2109 O TYR A 291 6.543 -30.159 -25.698 1.00 28.05 O
ANISOU 2109 O TYR A 291 4168 3449 3042 96 1242 -954 O
ATOM 2110 CB TYR A 291 5.766 -27.247 -24.895 1.00 23.91 C
ANISOU 2110 CB TYR A 291 4080 2680 2324 250 1241 -813 C
ATOM 2111 CG TYR A 291 4.380 -27.690 -24.449 1.00 30.06 C
ANISOU 2111 CG TYR A 291 4959 3413 3048 204 1386 -790 C
ATOM 2112 CD1 TYR A 291 3.868 -27.294 -23.220 1.00 29.24 C
ANISOU 2112 CD1 TYR A 291 5028 3194 2889 133 1475 -748 C
ATOM 2113 CD2 TYR A 291 3.587 -28.506 -25.254 1.00 26.13 C
ANISOU 2113 CD2 TYR A 291 4379 2990 2559 233 1423 -803 C
ATOM 2114 CE1 TYR A 291 2.609 -27.700 -22.801 1.00 33.07 C
ANISOU 2114 CE1 TYR A 291 5605 3634 3325 90 1603 -714 C
ATOM 2115 CE2 TYR A 291 2.329 -28.917 -24.842 1.00 26.51 C
ANISOU 2115 CE2 TYR A 291 4513 3004 2557 192 1547 -772 C
ATOM 2116 CZ TYR A 291 1.847 -28.510 -23.615 1.00 32.26 C
ANISOU 2116 CZ TYR A 291 5417 3613 3228 120 1639 -724 C
ATOM 2117 OH TYR A 291 0.594 -28.914 -23.205 1.00 39.96 O
ANISOU 2117 OH TYR A 291 6485 4547 4151 80 1768 -686 O
ATOM 2118 N THR A 292 6.026 -30.238 -23.500 1.00 26.63 N
ANISOU 2118 N THR A 292 4184 3125 2811 -110 1435 -951 N
ATOM 2119 CA THR A 292 5.325 -31.512 -23.528 1.00 31.02 C
ANISOU 2119 CA THR A 292 4649 3737 3402 -193 1548 -990 C
ATOM 2120 C THR A 292 4.107 -31.391 -22.624 1.00 28.90 C
ANISOU 2120 C THR A 292 4570 3359 3054 -253 1715 -946 C
ATOM 2121 O THR A 292 4.186 -30.783 -21.554 1.00 31.28 O
ANISOU 2121 O THR A 292 5017 3549 3320 -313 1754 -921 O
ATOM 2122 CB THR A 292 6.222 -32.671 -23.059 1.00 35.09 C
ANISOU 2122 CB THR A 292 4981 4326 4025 -339 1547 -1077 C
ATOM 2123 OG1 THR A 292 6.551 -32.492 -21.677 1.00 40.97 O
ANISOU 2123 OG1 THR A 292 5817 4981 4770 -469 1601 -1088 O
ATOM 2124 CG2 THR A 292 7.511 -32.715 -23.863 1.00 31.34 C
ANISOU 2124 CG2 THR A 292 4339 3951 3618 -275 1375 -1113 C
ATOM 2125 N ASN A 293 2.976 -31.946 -23.065 1.00 37.59 N
ANISOU 2125 N ASN A 293 5674 4487 4122 -231 1813 -934 N
ATOM 2126 CA ASN A 293 1.766 -31.920 -22.248 1.00 42.18 C
ANISOU 2126 CA ASN A 293 6436 4969 4622 -287 1984 -886 C
ATOM 2127 C ASN A 293 2.021 -32.541 -20.881 1.00 46.15 C
ANISOU 2127 C ASN A 293 6941 5418 5177 -486 2095 -919 C
ATOM 2128 O ASN A 293 1.780 -31.916 -19.841 1.00 45.24 O
ANISOU 2128 O ASN A 293 7008 5171 5010 -538 2162 -875 O
ATOM 2129 CB ASN A 293 0.636 -32.652 -22.976 1.00 44.18 C
ANISOU 2129 CB ASN A 293 6655 5288 4843 -244 2075 -884 C
ATOM 2130 CG ASN A 293 -0.681 -32.601 -22.229 1.00 52.66 C
ANISOU 2130 CG ASN A 293 7913 6264 5830 -283 2225 -811 C
ATOM 2131 OD1 ASN A 293 -1.042 -33.542 -21.523 1.00 62.99 O
ANISOU 2131 OD1 ASN A 293 9202 7568 7163 -428 2386 -835 O
ATOM 2132 ND2 ASN A 293 -1.420 -31.513 -22.406 1.00 50.21 N
ANISOU 2132 ND2 ASN A 293 7765 5880 5433 -152 2156 -714 N
ATOM 2133 N ASP A 294 2.518 -33.770 -20.868 1.00 48.32 N
ANISOU 2133 N ASP A 294 7011 5790 5560 -599 2113 -1000 N
ATOM 2134 CA ASP A 294 2.928 -34.436 -19.645 1.00 49.92 C
ANISOU 2134 CA ASP A 294 7174 5957 5837 -794 2197 -1051 C
ATOM 2135 C ASP A 294 4.428 -34.260 -19.454 1.00 49.82 C
ANISOU 2135 C ASP A 294 7055 5973 5900 -820 2045 -1109 C
ATOM 2136 O ASP A 294 5.185 -34.163 -20.422 1.00 55.63 O
ANISOU 2136 O ASP A 294 7667 6806 6665 -716 1894 -1131 O
ATOM 2137 CB ASP A 294 2.562 -35.922 -19.692 1.00 51.90 C
ANISOU 2137 CB ASP A 294 7255 6299 6165 -907 2311 -1114 C
ATOM 2138 CG ASP A 294 2.958 -36.667 -18.428 1.00 60.41 C
ANISOU 2138 CG ASP A 294 8277 7341 7335 -1118 2402 -1176 C
ATOM 2139 OD1 ASP A 294 4.160 -36.959 -18.249 1.00 65.29 O
ANISOU 2139 OD1 ASP A 294 8749 8012 8046 -1175 2294 -1253 O
ATOM 2140 OD2 ASP A 294 2.067 -36.950 -17.602 1.00 62.81 O
ANISOU 2140 OD2 ASP A 294 8686 7561 7617 -1227 2581 -1147 O
ATOM 2141 N PHE A 295 4.849 -34.201 -18.192 1.00 41.79 N
ANISOU 2141 N PHE A 295 6097 4870 4913 -957 2086 -1132 N
ATOM 2142 CA PHE A 295 6.268 -34.115 -17.873 1.00 45.12 C
ANISOU 2142 CA PHE A 295 6422 5318 5402 -996 1953 -1197 C
ATOM 2143 C PHE A 295 6.491 -34.575 -16.440 1.00 51.71 C
ANISOU 2143 C PHE A 295 7273 6077 6298 -1192 2046 -1251 C
ATOM 2144 O PHE A 295 5.601 -34.479 -15.591 1.00 54.75 O
ANISOU 2144 O PHE A 295 7813 6342 6648 -1274 2197 -1210 O
ATOM 2145 CB PHE A 295 6.812 -32.692 -18.066 1.00 42.58 C
ANISOU 2145 CB PHE A 295 6228 4943 5008 -860 1823 -1144 C
ATOM 2146 CG PHE A 295 8.296 -32.580 -17.835 1.00 39.49 C
ANISOU 2146 CG PHE A 295 5739 4592 4672 -883 1682 -1207 C
ATOM 2147 CD1 PHE A 295 9.190 -32.947 -18.827 1.00 40.96 C
ANISOU 2147 CD1 PHE A 295 5735 4916 4910 -812 1543 -1248 C
ATOM 2148 CD2 PHE A 295 8.796 -32.123 -16.626 1.00 41.85 C
ANISOU 2148 CD2 PHE A 295 6141 4791 4971 -972 1688 -1226 C
ATOM 2149 CE1 PHE A 295 10.552 -32.858 -18.622 1.00 41.71 C
ANISOU 2149 CE1 PHE A 295 5748 5053 5046 -825 1414 -1302 C
ATOM 2150 CE2 PHE A 295 10.161 -32.033 -16.414 1.00 45.56 C
ANISOU 2150 CE2 PHE A 295 6524 5304 5483 -986 1558 -1289 C
ATOM 2151 CZ PHE A 295 11.039 -32.398 -17.416 1.00 43.50 C
ANISOU 2151 CZ PHE A 295 6077 5186 5264 -911 1421 -1324 C
ATOM 2152 N SER A 296 7.698 -35.076 -16.185 1.00 53.96 N
ANISOU 2152 N SER A 296 7397 6429 6676 -1266 1950 -1345 N
ATOM 2153 CA SER A 296 8.125 -35.487 -14.855 1.00 52.23 C
ANISOU 2153 CA SER A 296 7170 6146 6528 -1449 2004 -1415 C
ATOM 2154 C SER A 296 9.567 -35.045 -14.654 1.00 49.52 C
ANISOU 2154 C SER A 296 6780 5827 6208 -1429 1833 -1471 C
ATOM 2155 O SER A 296 10.383 -35.148 -15.575 1.00 49.15 O
ANISOU 2155 O SER A 296 6591 5905 6179 -1332 1689 -1497 O
ATOM 2156 CB SER A 296 7.997 -37.004 -14.665 1.00 49.26 C
ANISOU 2156 CB SER A 296 6595 5851 6269 -1601 2093 -1504 C
ATOM 2157 OG SER A 296 8.926 -37.703 -15.477 1.00 51.04 O
ANISOU 2157 OG SER A 296 6585 6241 6569 -1561 1957 -1582 O
ATOM 2158 N ASP A 297 9.875 -34.552 -13.449 1.00 47.24 N
ANISOU 2158 N ASP A 297 6615 5417 5916 -1518 1853 -1488 N
ATOM 2159 CA ASP A 297 11.191 -33.967 -13.191 1.00 47.46 C
ANISOU 2159 CA ASP A 297 6634 5455 5943 -1486 1698 -1533 C
ATOM 2160 C ASP A 297 12.320 -34.951 -13.461 1.00 46.97 C
ANISOU 2160 C ASP A 297 6323 5543 5979 -1529 1583 -1646 C
ATOM 2161 O ASP A 297 13.445 -34.538 -13.769 1.00 49.21 O
ANISOU 2161 O ASP A 297 6562 5889 6248 -1447 1426 -1670 O
ATOM 2162 CB ASP A 297 11.273 -33.465 -11.747 1.00 47.95 C
ANISOU 2162 CB ASP A 297 6858 5361 6002 -1598 1753 -1551 C
ATOM 2163 CG ASP A 297 10.274 -32.362 -11.451 1.00 45.36 C
ANISOU 2163 CG ASP A 297 6791 4877 5568 -1537 1845 -1438 C
ATOM 2164 OD1 ASP A 297 9.834 -31.686 -12.403 1.00 46.30 O
ANISOU 2164 OD1 ASP A 297 6973 5017 5601 -1375 1814 -1350 O
ATOM 2165 OD2 ASP A 297 9.931 -32.167 -10.266 1.00 45.46 O
ANISOU 2165 OD2 ASP A 297 6944 4744 5584 -1648 1944 -1440 O
ATOM 2166 N ASP A 298 12.044 -36.253 -13.353 1.00 48.20 N
ANISOU 2166 N ASP A 298 6317 5763 6235 -1654 1661 -1716 N
ATOM 2167 CA ASP A 298 13.068 -37.262 -13.594 1.00 51.76 C
ANISOU 2167 CA ASP A 298 6523 6360 6785 -1694 1553 -1830 C
ATOM 2168 C ASP A 298 13.561 -37.257 -15.038 1.00 45.72 C
ANISOU 2168 C ASP A 298 5638 5736 5996 -1523 1413 -1806 C
ATOM 2169 O ASP A 298 14.676 -37.723 -15.298 1.00 46.40 O
ANISOU 2169 O ASP A 298 5562 5935 6134 -1509 1276 -1884 O
ATOM 2170 CB ASP A 298 12.533 -38.651 -13.244 1.00 63.05 C
ANISOU 2170 CB ASP A 298 7800 7827 8328 -1856 1679 -1906 C
ATOM 2171 CG ASP A 298 11.993 -38.734 -11.830 1.00 74.34 C
ANISOU 2171 CG ASP A 298 9341 9111 9795 -2039 1833 -1927 C
ATOM 2172 OD1 ASP A 298 12.731 -38.395 -10.881 1.00 77.74 O
ANISOU 2172 OD1 ASP A 298 9822 9474 10243 -2109 1781 -1983 O
ATOM 2173 OD2 ASP A 298 10.825 -39.145 -11.667 1.00 77.98 O
ANISOU 2173 OD2 ASP A 298 9842 9521 10267 -2112 2009 -1888 O
ATOM 2174 N ILE A 299 12.757 -36.743 -15.974 1.00 43.49 N
ANISOU 2174 N ILE A 299 5436 5448 5640 -1391 1441 -1702 N
ATOM 2175 CA ILE A 299 13.116 -36.791 -17.392 1.00 47.22 C
ANISOU 2175 CA ILE A 299 5793 6047 6102 -1234 1321 -1678 C
ATOM 2176 C ILE A 299 14.444 -36.083 -17.642 1.00 52.99 C
ANISOU 2176 C ILE A 299 6518 6814 6801 -1136 1140 -1682 C
ATOM 2177 O ILE A 299 15.253 -36.525 -18.468 1.00 48.95 O
ANISOU 2177 O ILE A 299 5845 6428 6325 -1065 1014 -1715 O
ATOM 2178 CB ILE A 299 11.982 -36.196 -18.249 1.00 46.23 C
ANISOU 2178 CB ILE A 299 5784 5886 5895 -1110 1383 -1567 C
ATOM 2179 CG1 ILE A 299 10.746 -37.097 -18.185 1.00 50.93 C
ANISOU 2179 CG1 ILE A 299 6348 6480 6523 -1194 1553 -1572 C
ATOM 2180 CG2 ILE A 299 12.425 -36.006 -19.693 1.00 42.30 C
ANISOU 2180 CG2 ILE A 299 5196 5494 5383 -937 1245 -1535 C
ATOM 2181 CD1 ILE A 299 9.634 -36.696 -19.125 1.00 52.99 C
ANISOU 2181 CD1 ILE A 299 6696 6731 6707 -1067 1606 -1478 C
ATOM 2182 N VAL A 300 14.697 -34.986 -16.927 1.00 60.04 N
ANISOU 2182 N VAL A 300 7590 7598 7625 -1127 1128 -1647 N
ATOM 2183 CA VAL A 300 15.947 -34.257 -17.116 1.00 61.06 C
ANISOU 2183 CA VAL A 300 7726 7760 7715 -1033 969 -1647 C
ATOM 2184 C VAL A 300 17.135 -34.969 -16.483 1.00 63.11 C
ANISOU 2184 C VAL A 300 7849 8088 8042 -1127 882 -1766 C
ATOM 2185 O VAL A 300 18.283 -34.680 -16.843 1.00 68.95 O
ANISOU 2185 O VAL A 300 8541 8898 8760 -1043 736 -1779 O
ATOM 2186 CB VAL A 300 15.832 -32.830 -16.557 1.00 61.84 C
ANISOU 2186 CB VAL A 300 8058 7724 7716 -986 984 -1576 C
ATOM 2187 CG1 VAL A 300 14.586 -32.158 -17.098 1.00 63.96 C
ANISOU 2187 CG1 VAL A 300 8463 7921 7918 -898 1072 -1467 C
ATOM 2188 CG2 VAL A 300 15.822 -32.847 -15.038 1.00 62.22 C
ANISOU 2188 CG2 VAL A 300 8198 7662 7781 -1141 1061 -1635 C
ATOM 2189 N LYS A 301 16.896 -35.889 -15.549 1.00 56.91 N
ANISOU 2189 N LYS A 301 7001 7284 7338 -1298 968 -1855 N
ATOM 2190 CA LYS A 301 17.953 -36.667 -14.919 1.00 49.68 C
ANISOU 2190 CA LYS A 301 5941 6436 6498 -1397 887 -1984 C
ATOM 2191 C LYS A 301 18.160 -38.017 -15.591 1.00 44.04 C
ANISOU 2191 C LYS A 301 4979 5873 5881 -1415 847 -2057 C
ATOM 2192 O LYS A 301 18.819 -38.891 -15.017 1.00 43.79 O
ANISOU 2192 O LYS A 301 4805 5900 5933 -1520 803 -2177 O
ATOM 2193 CB LYS A 301 17.643 -36.865 -13.433 1.00 51.79 C
ANISOU 2193 CB LYS A 301 6278 6588 6811 -1582 998 -2051 C
ATOM 2194 CG LYS A 301 17.907 -35.639 -12.577 1.00 54.94 C
ANISOU 2194 CG LYS A 301 6890 6855 7130 -1573 989 -2021 C
ATOM 2195 CD LYS A 301 17.253 -35.752 -11.212 1.00 57.34 C
ANISOU 2195 CD LYS A 301 7297 7014 7476 -1748 1133 -2059 C
ATOM 2196 CE LYS A 301 15.740 -35.710 -11.322 1.00 60.68 C
ANISOU 2196 CE LYS A 301 7825 7349 7884 -1769 1310 -1965 C
ATOM 2197 NZ LYS A 301 15.109 -35.180 -10.080 1.00 67.30 N
ANISOU 2197 NZ LYS A 301 8862 8002 8706 -1875 1437 -1947 N
ATOM 2198 N PHE A 302 17.618 -38.205 -16.793 1.00 46.87 N
ANISOU 2198 N PHE A 302 5280 6294 6232 -1310 855 -1992 N
ATOM 2199 CA PHE A 302 17.683 -39.499 -17.459 1.00 44.12 C
ANISOU 2199 CA PHE A 302 4701 6083 5978 -1322 830 -2059 C
ATOM 2200 C PHE A 302 19.124 -39.832 -17.826 1.00 42.99 C
ANISOU 2200 C PHE A 302 4410 6065 5859 -1260 640 -2127 C
ATOM 2201 O PHE A 302 19.862 -38.979 -18.327 1.00 45.53 O
ANISOU 2201 O PHE A 302 4798 6398 6104 -1129 522 -2068 O
ATOM 2202 CB PHE A 302 16.798 -39.493 -18.704 1.00 46.55 C
ANISOU 2202 CB PHE A 302 5001 6422 6262 -1206 872 -1971 C
ATOM 2203 CG PHE A 302 16.461 -40.866 -19.217 1.00 48.39 C
ANISOU 2203 CG PHE A 302 5023 6768 6596 -1245 905 -2038 C
ATOM 2204 CD1 PHE A 302 15.934 -41.824 -18.369 1.00 47.81 C
ANISOU 2204 CD1 PHE A 302 4872 6685 6608 -1417 1032 -2121 C
ATOM 2205 CD2 PHE A 302 16.651 -41.187 -20.549 1.00 47.73 C
ANISOU 2205 CD2 PHE A 302 4818 6795 6524 -1109 814 -2019 C
ATOM 2206 CE1 PHE A 302 15.615 -43.082 -18.835 1.00 50.92 C
ANISOU 2206 CE1 PHE A 302 5065 7187 7096 -1450 1068 -2186 C
ATOM 2207 CE2 PHE A 302 16.332 -42.445 -21.022 1.00 48.61 C
ANISOU 2207 CE2 PHE A 302 4733 7009 6726 -1137 844 -2085 C
ATOM 2208 CZ PHE A 302 15.815 -43.393 -20.164 1.00 51.39 C
ANISOU 2208 CZ PHE A 302 5005 7360 7162 -1307 972 -2170 C
ATOM 2209 N HIS A 303 19.516 -41.083 -17.574 1.00 40.37 N
ANISOU 2209 N HIS A 303 3876 5829 5634 -1355 613 -2250 N
ATOM 2210 CA HIS A 303 20.910 -41.491 -17.717 1.00 39.73 C
ANISOU 2210 CA HIS A 303 3654 5863 5578 -1314 433 -2331 C
ATOM 2211 C HIS A 303 21.407 -41.416 -19.155 1.00 40.86 C
ANISOU 2211 C HIS A 303 3727 6109 5689 -1129 304 -2269 C
ATOM 2212 O HIS A 303 22.617 -41.293 -19.371 1.00 43.62 O
ANISOU 2212 O HIS A 303 4033 6528 6012 -1051 146 -2290 O
ATOM 2213 CB HIS A 303 21.089 -42.911 -17.182 1.00 44.95 C
ANISOU 2213 CB HIS A 303 4102 6607 6370 -1454 439 -2481 C
ATOM 2214 CG HIS A 303 20.327 -43.945 -17.952 1.00 46.58 C
ANISOU 2214 CG HIS A 303 4147 6893 6657 -1455 507 -2494 C
ATOM 2215 ND1 HIS A 303 20.942 -44.846 -18.793 1.00 46.99 N
ANISOU 2215 ND1 HIS A 303 3990 7094 6769 -1382 387 -2551 N
ATOM 2216 CD2 HIS A 303 19.001 -44.211 -18.018 1.00 47.86 C
ANISOU 2216 CD2 HIS A 303 4332 7007 6844 -1512 682 -2456 C
ATOM 2217 CE1 HIS A 303 20.027 -45.630 -19.337 1.00 46.65 C
ANISOU 2217 CE1 HIS A 303 3842 7093 6790 -1396 486 -2554 C
ATOM 2218 NE2 HIS A 303 18.842 -45.263 -18.885 1.00 46.50 N
ANISOU 2218 NE2 HIS A 303 3961 6959 6748 -1475 667 -2497 N
ATOM 2219 N CYS A 304 20.512 -41.493 -20.142 1.00 41.46 N
ANISOU 2219 N CYS A 304 3792 6194 5765 -1056 368 -2195 N
ATOM 2220 CA CYS A 304 20.928 -41.388 -21.536 1.00 44.33 C
ANISOU 2220 CA CYS A 304 4096 6640 6106 -882 252 -2133 C
ATOM 2221 C CYS A 304 21.311 -39.968 -21.932 1.00 42.71 C
ANISOU 2221 C CYS A 304 4068 6373 5787 -751 188 -2016 C
ATOM 2222 O CYS A 304 21.812 -39.766 -23.044 1.00 45.35 O
ANISOU 2222 O CYS A 304 4364 6766 6100 -606 81 -1960 O
ATOM 2223 CB CYS A 304 19.824 -41.904 -22.464 1.00 46.08 C
ANISOU 2223 CB CYS A 304 4254 6887 6368 -843 339 -2098 C
ATOM 2224 SG CYS A 304 19.300 -43.608 -22.135 1.00 61.14 S
ANISOU 2224 SG CYS A 304 5938 8880 8414 -986 427 -2232 S
ATOM 2225 N LEU A 305 21.090 -38.988 -21.058 1.00 34.32 N
ANISOU 2225 N LEU A 305 3194 5189 4655 -798 254 -1979 N
ATOM 2226 CA LEU A 305 21.507 -37.611 -21.280 1.00 38.01 C
ANISOU 2226 CA LEU A 305 3828 5596 5016 -685 198 -1880 C
ATOM 2227 C LEU A 305 22.834 -37.286 -20.601 1.00 38.50 C
ANISOU 2227 C LEU A 305 3911 5678 5041 -691 83 -1928 C
ATOM 2228 O LEU A 305 23.228 -36.117 -20.564 1.00 38.27 O
ANISOU 2228 O LEU A 305 4028 5591 4921 -616 49 -1857 O
ATOM 2229 CB LEU A 305 20.430 -36.641 -20.785 1.00 32.35 C
ANISOU 2229 CB LEU A 305 3317 4734 4239 -713 336 -1805 C
ATOM 2230 CG LEU A 305 19.008 -36.782 -21.338 1.00 33.02 C
ANISOU 2230 CG LEU A 305 3425 4783 4337 -702 463 -1750 C
ATOM 2231 CD1 LEU A 305 18.051 -35.798 -20.669 1.00 32.75 C
ANISOU 2231 CD1 LEU A 305 3609 4601 4232 -733 590 -1683 C
ATOM 2232 CD2 LEU A 305 19.003 -36.604 -22.847 1.00 31.49 C
ANISOU 2232 CD2 LEU A 305 3181 4650 4133 -539 390 -1675 C
ATOM 2233 N ALA A 306 23.535 -38.296 -20.077 1.00 38.59 N
ANISOU 2233 N ALA A 306 3775 5770 5118 -775 22 -2050 N
ATOM 2234 CA ALA A 306 24.691 -38.044 -19.219 1.00 41.60 C
ANISOU 2234 CA ALA A 306 4184 6160 5462 -803 -73 -2115 C
ATOM 2235 C ALA A 306 25.880 -37.475 -19.986 1.00 44.31 C
ANISOU 2235 C ALA A 306 4534 6571 5729 -644 -229 -2060 C
ATOM 2236 O ALA A 306 26.648 -36.683 -19.429 1.00 45.92 O
ANISOU 2236 O ALA A 306 4847 6745 5854 -624 -283 -2057 O
ATOM 2237 CB ALA A 306 25.094 -39.332 -18.499 1.00 42.91 C
ANISOU 2237 CB ALA A 306 4177 6402 5727 -932 -105 -2270 C
ATOM 2238 N ASN A 307 26.055 -37.861 -21.248 1.00 43.80 N
ANISOU 2238 N ASN A 307 4359 6597 5687 -531 -299 -2016 N
ATOM 2239 CA ASN A 307 27.209 -37.441 -22.035 1.00 42.80 C
ANISOU 2239 CA ASN A 307 4226 6539 5498 -382 -444 -1961 C
ATOM 2240 C ASN A 307 26.928 -36.227 -22.909 1.00 39.08 C
ANISOU 2240 C ASN A 307 3890 6005 4954 -253 -423 -1812 C
ATOM 2241 O ASN A 307 27.820 -35.780 -23.636 1.00 42.84 O
ANISOU 2241 O ASN A 307 4373 6527 5379 -126 -529 -1748 O
ATOM 2242 CB ASN A 307 27.707 -38.604 -22.898 1.00 44.13 C
ANISOU 2242 CB ASN A 307 4188 6842 5737 -328 -549 -2004 C
ATOM 2243 CG ASN A 307 28.137 -39.796 -22.069 1.00 53.89 C
ANISOU 2243 CG ASN A 307 5274 8154 7046 -443 -593 -2161 C
ATOM 2244 OD1 ASN A 307 28.559 -39.647 -20.922 1.00 55.30 O
ANISOU 2244 OD1 ASN A 307 5504 8307 7201 -531 -599 -2235 O
ATOM 2245 ND2 ASN A 307 28.026 -40.989 -22.641 1.00 53.96 N
ANISOU 2245 ND2 ASN A 307 5093 8258 7150 -442 -624 -2217 N
ATOM 2246 N VAL A 308 25.706 -35.694 -22.860 1.00 33.75 N
ANISOU 2246 N VAL A 308 3322 5226 4276 -281 -290 -1755 N
ATOM 2247 CA VAL A 308 25.400 -34.437 -23.528 1.00 30.14 C
ANISOU 2247 CA VAL A 308 3005 4697 3750 -169 -266 -1624 C
ATOM 2248 C VAL A 308 26.245 -33.312 -22.929 1.00 32.70 C
ANISOU 2248 C VAL A 308 3472 4979 3974 -137 -308 -1596 C
ATOM 2249 O VAL A 308 26.519 -33.284 -21.722 1.00 38.25 O
ANISOU 2249 O VAL A 308 4227 5652 4656 -233 -293 -1671 O
ATOM 2250 CB VAL A 308 23.894 -34.140 -23.403 1.00 31.49 C
ANISOU 2250 CB VAL A 308 3268 4764 3932 -217 -114 -1587 C
ATOM 2251 CG1 VAL A 308 23.587 -32.684 -23.681 1.00 35.15 C
ANISOU 2251 CG1 VAL A 308 3908 5134 4314 -126 -83 -1473 C
ATOM 2252 CG2 VAL A 308 23.100 -35.032 -24.340 1.00 30.56 C
ANISOU 2252 CG2 VAL A 308 3022 4695 3894 -200 -83 -1586 C
ATOM 2253 N SER A 309 26.679 -32.381 -23.791 1.00 26.31 N
ANISOU 2253 N SER A 309 2722 4168 3106 1 -360 -1490 N
ATOM 2254 CA SER A 309 27.443 -31.216 -23.363 1.00 29.39 C
ANISOU 2254 CA SER A 309 3250 4521 3397 50 -392 -1450 C
ATOM 2255 C SER A 309 26.625 -29.931 -23.286 1.00 30.67 C
ANISOU 2255 C SER A 309 3584 4561 3509 79 -296 -1365 C
ATOM 2256 O SER A 309 27.048 -28.994 -22.601 1.00 27.48 O
ANISOU 2256 O SER A 309 3307 4106 3027 87 -293 -1355 O
ATOM 2257 CB SER A 309 28.638 -30.984 -24.301 1.00 25.58 C
ANISOU 2257 CB SER A 309 2721 4122 2876 184 -516 -1390 C
ATOM 2258 OG SER A 309 28.225 -30.914 -25.654 1.00 42.79 O
ANISOU 2258 OG SER A 309 4853 6310 5095 282 -520 -1299 O
ATOM 2259 N ALA A 310 25.481 -29.853 -23.970 1.00 25.47 N
ANISOU 2259 N ALA A 310 2931 3857 2889 103 -222 -1309 N
ATOM 2260 CA ALA A 310 24.576 -28.713 -23.853 1.00 23.42 C
ANISOU 2260 CA ALA A 310 2831 3480 2586 128 -130 -1238 C
ATOM 2261 C ALA A 310 23.160 -29.233 -23.655 1.00 27.49 C
ANISOU 2261 C ALA A 310 3351 3942 3153 47 -15 -1260 C
ATOM 2262 O ALA A 310 22.584 -29.838 -24.565 1.00 26.23 O
ANISOU 2262 O ALA A 310 3096 3820 3052 76 -8 -1244 O
ATOM 2263 CB ALA A 310 24.642 -27.805 -25.082 1.00 22.14 C
ANISOU 2263 CB ALA A 310 2693 3315 2403 275 -165 -1125 C
ATOM 2264 N MET A 311 22.605 -28.990 -22.472 1.00 31.16 N
ANISOU 2264 N MET A 311 3932 4315 3593 -51 75 -1296 N
ATOM 2265 CA MET A 311 21.250 -29.390 -22.123 1.00 29.03 C
ANISOU 2265 CA MET A 311 3694 3979 3356 -134 200 -1310 C
ATOM 2266 C MET A 311 20.353 -28.160 -22.098 1.00 28.00 C
ANISOU 2266 C MET A 311 3743 3732 3165 -78 275 -1227 C
ATOM 2267 O MET A 311 20.754 -27.104 -21.596 1.00 24.03 O
ANISOU 2267 O MET A 311 3367 3170 2595 -45 263 -1201 O
ATOM 2268 CB MET A 311 21.223 -30.091 -20.761 1.00 26.52 C
ANISOU 2268 CB MET A 311 3376 3634 3064 -296 255 -1412 C
ATOM 2269 CG MET A 311 19.842 -30.492 -20.272 1.00 34.06 C
ANISOU 2269 CG MET A 311 4379 4513 4051 -395 399 -1423 C
ATOM 2270 SD MET A 311 19.090 -31.776 -21.288 1.00 39.30 S
ANISOU 2270 SD MET A 311 4867 5265 4801 -400 430 -1436 S
ATOM 2271 CE MET A 311 20.387 -33.009 -21.274 1.00 43.88 C
ANISOU 2271 CE MET A 311 5232 5987 5455 -449 312 -1543 C
ATOM 2272 N SER A 312 19.137 -28.298 -22.629 1.00 24.02 N
ANISOU 2272 N SER A 312 3249 3197 2680 -61 351 -1189 N
ATOM 2273 CA SER A 312 18.243 -27.153 -22.750 1.00 23.37 C
ANISOU 2273 CA SER A 312 3327 3013 2540 11 411 -1110 C
ATOM 2274 C SER A 312 16.792 -27.555 -22.506 1.00 27.59 C
ANISOU 2274 C SER A 312 3914 3486 3084 -49 538 -1110 C
ATOM 2275 O SER A 312 16.325 -28.583 -23.006 1.00 25.23 O
ANISOU 2275 O SER A 312 3497 3247 2843 -78 563 -1136 O
ATOM 2276 CB SER A 312 18.376 -26.504 -24.129 1.00 21.41 C
ANISOU 2276 CB SER A 312 3049 2800 2287 166 337 -1031 C
ATOM 2277 OG SER A 312 17.589 -25.333 -24.197 1.00 44.01 O
ANISOU 2277 OG SER A 312 6063 5567 5094 240 383 -963 O
ATOM 2278 N LEU A 313 16.081 -26.721 -21.743 1.00 27.60 N
ANISOU 2278 N LEU A 313 4096 3366 3024 -61 619 -1078 N
ATOM 2279 CA LEU A 313 14.653 -26.879 -21.495 1.00 25.21 C
ANISOU 2279 CA LEU A 313 3882 2989 2709 -99 745 -1059 C
ATOM 2280 C LEU A 313 13.968 -25.550 -21.787 1.00 30.12 C
ANISOU 2280 C LEU A 313 4666 3523 3256 21 759 -975 C
ATOM 2281 O LEU A 313 14.393 -24.508 -21.277 1.00 34.71 O
ANISOU 2281 O LEU A 313 5362 4040 3785 56 733 -953 O
ATOM 2282 CB LEU A 313 14.375 -27.317 -20.048 1.00 25.07 C
ANISOU 2282 CB LEU A 313 3936 2895 2694 -257 847 -1113 C
ATOM 2283 CG LEU A 313 15.139 -28.504 -19.452 1.00 31.05 C
ANISOU 2283 CG LEU A 313 4551 3720 3525 -395 833 -1213 C
ATOM 2284 CD1 LEU A 313 14.745 -28.698 -18.000 1.00 40.45 C
ANISOU 2284 CD1 LEU A 313 5845 4807 4718 -544 943 -1256 C
ATOM 2285 CD2 LEU A 313 14.903 -29.785 -20.239 1.00 28.66 C
ANISOU 2285 CD2 LEU A 313 4062 3529 3299 -418 837 -1247 C
ATOM 2286 N ALA A 314 12.924 -25.587 -22.615 1.00 22.44 N
ANISOU 2286 N ALA A 314 3697 2551 2278 90 795 -933 N
ATOM 2287 CA ALA A 314 12.162 -24.397 -22.979 1.00 21.71 C
ANISOU 2287 CA ALA A 314 3747 2383 2120 211 803 -860 C
ATOM 2288 C ALA A 314 10.677 -24.717 -22.904 1.00 25.29 C
ANISOU 2288 C ALA A 314 4280 2784 2545 194 919 -841 C
ATOM 2289 O ALA A 314 10.207 -25.649 -23.563 1.00 25.32 O
ANISOU 2289 O ALA A 314 4175 2857 2589 185 942 -859 O
ATOM 2290 CB ALA A 314 12.530 -23.900 -24.380 1.00 21.68 C
ANISOU 2290 CB ALA A 314 3659 2446 2134 356 694 -821 C
ATOM 2291 N GLY A 315 9.945 -23.941 -22.108 1.00 29.32 N
ANISOU 2291 N GLY A 315 4984 3174 2982 197 992 -806 N
ATOM 2292 CA GLY A 315 8.516 -24.131 -21.971 1.00 23.25 C
ANISOU 2292 CA GLY A 315 4301 2353 2179 188 1092 -767 C
ATOM 2293 C GLY A 315 8.104 -25.423 -21.307 1.00 29.27 C
ANISOU 2293 C GLY A 315 5039 3117 2967 35 1221 -822 C
ATOM 2294 O GLY A 315 6.980 -25.886 -21.518 1.00 30.72 O
ANISOU 2294 O GLY A 315 5251 3294 3128 34 1311 -805 O
ATOM 2295 N VAL A 316 8.973 -26.007 -20.488 1.00 28.26 N
ANISOU 2295 N VAL A 316 4844 3003 2892 -95 1223 -882 N
ATOM 2296 CA VAL A 316 8.756 -27.328 -19.909 1.00 32.32 C
ANISOU 2296 CA VAL A 316 5277 3541 3463 -253 1320 -939 C
ATOM 2297 C VAL A 316 8.217 -27.184 -18.492 1.00 39.90 C
ANISOU 2297 C VAL A 316 6408 4364 4388 -366 1445 -933 C
ATOM 2298 O VAL A 316 8.628 -26.290 -17.740 1.00 42.46 O
ANISOU 2298 O VAL A 316 6858 4600 4677 -362 1421 -922 O
ATOM 2299 CB VAL A 316 10.059 -28.150 -19.936 1.00 34.17 C
ANISOU 2299 CB VAL A 316 5313 3882 3788 -327 1236 -1020 C
ATOM 2300 CG1 VAL A 316 9.878 -29.477 -19.230 1.00 31.39 C
ANISOU 2300 CG1 VAL A 316 4872 3550 3504 -498 1335 -1089 C
ATOM 2301 CG2 VAL A 316 10.506 -28.370 -21.377 1.00 33.13 C
ANISOU 2301 CG2 VAL A 316 5016 3878 3693 -214 1122 -1019 C
ATOM 2302 N SER A 317 7.295 -28.071 -18.125 1.00 28.98 N
ANISOU 2302 N SER A 317 5031 2963 3018 -467 1582 -940 N
ATOM 2303 CA SER A 317 6.662 -28.054 -16.808 1.00 32.85 C
ANISOU 2303 CA SER A 317 5683 3317 3483 -585 1720 -928 C
ATOM 2304 C SER A 317 7.533 -28.649 -15.712 1.00 31.42 C
ANISOU 2304 C SER A 317 5437 3119 3381 -754 1732 -1010 C
ATOM 2305 O SER A 317 7.034 -29.387 -14.861 1.00 37.75 O
ANISOU 2305 O SER A 317 6259 3867 4217 -902 1863 -1033 O
ATOM 2306 CB SER A 317 5.328 -28.790 -16.890 1.00 40.32 C
ANISOU 2306 CB SER A 317 6657 4252 4410 -625 1870 -899 C
ATOM 2307 OG SER A 317 4.450 -28.129 -17.778 1.00 52.29 O
ANISOU 2307 OG SER A 317 8264 5765 5838 -464 1860 -825 O
ATOM 2308 N ILE A 318 8.831 -28.348 -15.704 1.00 34.47 N
ANISOU 2308 N ILE A 318 5747 3551 3798 -737 1598 -1057 N
ATOM 2309 CA ILE A 318 9.699 -28.857 -14.649 1.00 36.26 C
ANISOU 2309 CA ILE A 318 5918 3764 4095 -889 1595 -1144 C
ATOM 2310 C ILE A 318 9.489 -28.028 -13.390 1.00 38.03 C
ANISOU 2310 C ILE A 318 6359 3818 4272 -936 1657 -1122 C
ATOM 2311 O ILE A 318 9.495 -26.790 -13.432 1.00 37.34 O
ANISOU 2311 O ILE A 318 6419 3663 4105 -817 1608 -1065 O
ATOM 2312 CB ILE A 318 11.172 -28.846 -15.096 1.00 34.39 C
ANISOU 2312 CB ILE A 318 5528 3642 3897 -845 1429 -1202 C
ATOM 2313 CG1 ILE A 318 12.082 -29.250 -13.934 1.00 32.05 C
ANISOU 2313 CG1 ILE A 318 5194 3323 3662 -992 1415 -1298 C
ATOM 2314 CG2 ILE A 318 11.567 -27.481 -15.667 1.00 29.40 C
ANISOU 2314 CG2 ILE A 318 4987 2997 3185 -672 1319 -1139 C
ATOM 2315 CD1 ILE A 318 13.443 -29.742 -14.354 1.00 31.69 C
ANISOU 2315 CD1 ILE A 318 4951 3417 3672 -985 1272 -1375 C
ATOM 2316 N LYS A 319 9.273 -28.710 -12.267 1.00 43.67 N
ANISOU 2316 N LYS A 319 7093 4458 5041 -1111 1768 -1169 N
ATOM 2317 CA LYS A 319 9.088 -28.044 -10.986 1.00 44.25 C
ANISOU 2317 CA LYS A 319 7368 4360 5085 -1175 1833 -1158 C
ATOM 2318 C LYS A 319 10.340 -28.058 -10.126 1.00 41.10 C
ANISOU 2318 C LYS A 319 6924 3952 4743 -1263 1755 -1255 C
ATOM 2319 O LYS A 319 10.590 -27.086 -9.406 1.00 40.99 O
ANISOU 2319 O LYS A 319 7068 3825 4682 -1238 1732 -1245 O
ATOM 2320 CB LYS A 319 7.940 -28.696 -10.212 1.00 46.36 C
ANISOU 2320 CB LYS A 319 7718 4523 5374 -1315 2022 -1138 C
ATOM 2321 CG LYS A 319 6.635 -28.710 -10.980 1.00 47.13 C
ANISOU 2321 CG LYS A 319 7878 4626 5404 -1230 2112 -1043 C
ATOM 2322 CD LYS A 319 6.166 -27.299 -11.295 1.00 50.25 C
ANISOU 2322 CD LYS A 319 8474 4944 5676 -1051 2073 -946 C
ATOM 2323 CE LYS A 319 5.106 -27.320 -12.377 1.00 57.73 C
ANISOU 2323 CE LYS A 319 9433 5945 6558 -932 2110 -870 C
ATOM 2324 NZ LYS A 319 4.110 -28.391 -12.114 1.00 60.26 N
ANISOU 2324 NZ LYS A 319 9741 6251 6903 -1053 2280 -861 N
ATOM 2325 N TYR A 320 11.133 -29.126 -10.190 1.00 39.59 N
ANISOU 2325 N TYR A 320 6518 3876 4647 -1359 1707 -1353 N
ATOM 2326 CA TYR A 320 12.330 -29.242 -9.371 1.00 40.73 C
ANISOU 2326 CA TYR A 320 6607 4023 4847 -1446 1627 -1458 C
ATOM 2327 C TYR A 320 13.464 -29.827 -10.198 1.00 42.24 C
ANISOU 2327 C TYR A 320 6569 4399 5083 -1406 1482 -1526 C
ATOM 2328 O TYR A 320 13.306 -30.873 -10.836 1.00 38.25 O
ANISOU 2328 O TYR A 320 5889 4006 4639 -1439 1496 -1551 O
ATOM 2329 CB TYR A 320 12.071 -30.103 -8.132 1.00 38.69 C
ANISOU 2329 CB TYR A 320 6344 3676 4680 -1660 1747 -1531 C
ATOM 2330 CG TYR A 320 10.997 -29.530 -7.239 1.00 50.99 C
ANISOU 2330 CG TYR A 320 8141 5038 6195 -1704 1893 -1461 C
ATOM 2331 CD1 TYR A 320 11.221 -28.372 -6.510 1.00 52.25 C
ANISOU 2331 CD1 TYR A 320 8496 5065 6293 -1659 1864 -1441 C
ATOM 2332 CD2 TYR A 320 9.752 -30.133 -7.143 1.00 45.23 C
ANISOU 2332 CD2 TYR A 320 7448 4255 5482 -1783 2061 -1410 C
ATOM 2333 CE1 TYR A 320 10.240 -27.837 -5.702 1.00 49.05 C
ANISOU 2333 CE1 TYR A 320 8315 4474 5846 -1691 1993 -1374 C
ATOM 2334 CE2 TYR A 320 8.764 -29.606 -6.335 1.00 50.49 C
ANISOU 2334 CE2 TYR A 320 8344 4737 6102 -1818 2196 -1337 C
ATOM 2335 CZ TYR A 320 9.013 -28.457 -5.617 1.00 53.47 C
ANISOU 2335 CZ TYR A 320 8914 4981 6422 -1770 2159 -1319 C
ATOM 2336 OH TYR A 320 8.038 -27.924 -4.811 1.00 57.91 O
ANISOU 2336 OH TYR A 320 9711 5354 6937 -1797 2288 -1244 O
ATOM 2337 N LEU A 321 14.601 -29.139 -10.187 1.00 38.98 N
ANISOU 2337 N LEU A 321 6160 4016 4636 -1330 1344 -1555 N
ATOM 2338 CA LEU A 321 15.835 -29.598 -10.820 1.00 40.54 C
ANISOU 2338 CA LEU A 321 6161 4376 4866 -1292 1196 -1621 C
ATOM 2339 C LEU A 321 16.843 -29.811 -9.698 1.00 45.06 C
ANISOU 2339 C LEU A 321 6710 4927 5483 -1405 1143 -1739 C
ATOM 2340 O LEU A 321 17.483 -28.859 -9.242 1.00 49.81 O
ANISOU 2340 O LEU A 321 7425 5476 6024 -1351 1078 -1744 O
ATOM 2341 CB LEU A 321 16.333 -28.588 -11.851 1.00 41.13 C
ANISOU 2341 CB LEU A 321 6261 4513 4855 -1094 1078 -1548 C
ATOM 2342 CG LEU A 321 17.613 -28.933 -12.615 1.00 44.84 C
ANISOU 2342 CG LEU A 321 6548 5146 5342 -1030 923 -1596 C
ATOM 2343 CD1 LEU A 321 17.560 -30.358 -13.125 1.00 45.59 C
ANISOU 2343 CD1 LEU A 321 6429 5362 5531 -1100 927 -1650 C
ATOM 2344 CD2 LEU A 321 17.811 -27.970 -13.768 1.00 45.57 C
ANISOU 2344 CD2 LEU A 321 6671 5287 5358 -839 841 -1501 C
ATOM 2345 N GLU A 322 16.974 -31.057 -9.244 1.00 46.05 N
ANISOU 2345 N GLU A 322 6685 5095 5715 -1560 1172 -1840 N
ATOM 2346 CA GLU A 322 17.800 -31.383 -8.091 1.00 51.45 C
ANISOU 2346 CA GLU A 322 7341 5750 6457 -1689 1135 -1966 C
ATOM 2347 C GLU A 322 18.498 -32.717 -8.308 1.00 55.96 C
ANISOU 2347 C GLU A 322 7660 6473 7131 -1768 1066 -2080 C
ATOM 2348 O GLU A 322 17.983 -33.599 -9.000 1.00 52.93 O
ANISOU 2348 O GLU A 322 7140 6172 6801 -1786 1110 -2069 O
ATOM 2349 CB GLU A 322 16.965 -31.441 -6.799 1.00 56.77 C
ANISOU 2349 CB GLU A 322 8150 6245 7174 -1849 1288 -1983 C
ATOM 2350 CG GLU A 322 16.381 -30.105 -6.361 1.00 63.07 C
ANISOU 2350 CG GLU A 322 9212 6877 7876 -1780 1347 -1888 C
ATOM 2351 CD GLU A 322 15.273 -30.258 -5.338 1.00 72.78 C
ANISOU 2351 CD GLU A 322 10577 7931 9145 -1924 1523 -1871 C
ATOM 2352 OE1 GLU A 322 14.942 -31.406 -4.978 1.00 77.38 O
ANISOU 2352 OE1 GLU A 322 11044 8523 9835 -2083 1609 -1931 O
ATOM 2353 OE2 GLU A 322 14.728 -29.225 -4.896 1.00 75.71 O
ANISOU 2353 OE2 GLU A 322 11170 8155 9442 -1875 1579 -1795 O
ATOM 2354 N ASP A 323 19.681 -32.852 -7.705 1.00 62.95 N
ANISOU 2354 N ASP A 323 8484 7394 8039 -1809 952 -2194 N
ATOM 2355 CA ASP A 323 20.424 -34.113 -7.674 1.00 63.27 C
ANISOU 2355 CA ASP A 323 8292 7565 8181 -1898 878 -2325 C
ATOM 2356 C ASP A 323 20.749 -34.614 -9.081 1.00 56.16 C
ANISOU 2356 C ASP A 323 7218 6845 7277 -1778 787 -2295 C
ATOM 2357 O ASP A 323 20.427 -35.743 -9.459 1.00 53.35 O
ANISOU 2357 O ASP A 323 6689 6572 7010 -1842 820 -2333 O
ATOM 2358 CB ASP A 323 19.664 -35.173 -6.874 1.00 67.18 C
ANISOU 2358 CB ASP A 323 8719 8000 8805 -2104 1017 -2396 C
ATOM 2359 CG ASP A 323 19.285 -34.692 -5.488 1.00 78.12 C
ANISOU 2359 CG ASP A 323 10285 9194 10203 -2227 1116 -2419 C
ATOM 2360 OD1 ASP A 323 19.934 -33.748 -4.986 1.00 81.97 O
ANISOU 2360 OD1 ASP A 323 10905 9620 10620 -2173 1041 -2430 O
ATOM 2361 OD2 ASP A 323 18.338 -35.255 -4.903 1.00 83.24 O
ANISOU 2361 OD2 ASP A 323 10945 9750 10932 -2376 1273 -2425 O
ATOM 2362 N VAL A 324 21.393 -33.755 -9.863 1.00 50.57 N
ANISOU 2362 N VAL A 324 6555 6193 6467 -1603 673 -2227 N
ATOM 2363 CA VAL A 324 21.939 -34.153 -11.156 1.00 44.64 C
ANISOU 2363 CA VAL A 324 5644 5608 5709 -1481 561 -2206 C
ATOM 2364 C VAL A 324 23.266 -34.851 -10.889 1.00 45.94 C
ANISOU 2364 C VAL A 324 5651 5889 5914 -1513 416 -2339 C
ATOM 2365 O VAL A 324 24.153 -34.257 -10.258 1.00 51.92 O
ANISOU 2365 O VAL A 324 6485 6624 6618 -1497 334 -2384 O
ATOM 2366 CB VAL A 324 22.111 -32.944 -12.088 1.00 45.70 C
ANISOU 2366 CB VAL A 324 5890 5750 5725 -1287 503 -2078 C
ATOM 2367 CG1 VAL A 324 22.614 -33.387 -13.452 1.00 41.73 C
ANISOU 2367 CG1 VAL A 324 5225 5407 5225 -1167 397 -2050 C
ATOM 2368 CG2 VAL A 324 20.799 -32.183 -12.215 1.00 50.00 C
ANISOU 2368 CG2 VAL A 324 6604 6169 6225 -1257 640 -1959 C
ATOM 2369 N PRO A 325 23.441 -36.103 -11.315 1.00 47.18 N
ANISOU 2369 N PRO A 325 5592 6172 6163 -1555 379 -2409 N
ATOM 2370 CA PRO A 325 24.674 -36.829 -10.981 1.00 50.47 C
ANISOU 2370 CA PRO A 325 5856 6698 6623 -1590 238 -2548 C
ATOM 2371 C PRO A 325 25.920 -36.094 -11.454 1.00 55.57 C
ANISOU 2371 C PRO A 325 6536 7420 7160 -1430 73 -2523 C
ATOM 2372 O PRO A 325 25.956 -35.525 -12.547 1.00 58.49 O
ANISOU 2372 O PRO A 325 6937 7831 7457 -1275 38 -2406 O
ATOM 2373 CB PRO A 325 24.498 -38.168 -11.707 1.00 47.30 C
ANISOU 2373 CB PRO A 325 5222 6426 6324 -1615 229 -2592 C
ATOM 2374 CG PRO A 325 23.018 -38.347 -11.790 1.00 43.60 C
ANISOU 2374 CG PRO A 325 4793 5874 5901 -1685 413 -2524 C
ATOM 2375 CD PRO A 325 22.461 -36.964 -11.998 1.00 41.64 C
ANISOU 2375 CD PRO A 325 4776 5510 5536 -1585 473 -2380 C
ATOM 2376 N LYS A 326 26.954 -36.112 -10.607 1.00 55.62 N
ANISOU 2376 N LYS A 326 6536 7443 7156 -1469 -26 -2636 N
ATOM 2377 CA LYS A 326 28.164 -35.345 -10.884 1.00 53.41 C
ANISOU 2377 CA LYS A 326 6311 7224 6759 -1325 -172 -2617 C
ATOM 2378 C LYS A 326 28.931 -35.864 -12.091 1.00 52.43 C
ANISOU 2378 C LYS A 326 6029 7271 6622 -1196 -305 -2598 C
ATOM 2379 O LYS A 326 29.747 -35.124 -12.652 1.00 52.96 O
ANISOU 2379 O LYS A 326 6153 7387 6581 -1048 -402 -2533 O
ATOM 2380 CB LYS A 326 29.076 -35.336 -9.658 1.00 53.26 C
ANISOU 2380 CB LYS A 326 6316 7189 6733 -1401 -249 -2757 C
ATOM 2381 CG LYS A 326 28.698 -34.297 -8.618 1.00 55.94 C
ANISOU 2381 CG LYS A 326 6872 7357 7026 -1451 -160 -2744 C
ATOM 2382 CD LYS A 326 29.568 -34.433 -7.379 1.00 62.96 C
ANISOU 2382 CD LYS A 326 7770 8226 7927 -1518 -234 -2862 C
ATOM 2383 CE LYS A 326 29.244 -33.372 -6.341 1.00 65.16 C
ANISOU 2383 CE LYS A 326 8268 8331 8159 -1552 -155 -2840 C
ATOM 2384 NZ LYS A 326 29.618 -32.012 -6.810 1.00 64.10 N
ANISOU 2384 NZ LYS A 326 8294 8185 7875 -1392 -191 -2747 N
ATOM 2385 N HIS A 327 28.701 -37.110 -12.504 1.00 51.19 N
ANISOU 2385 N HIS A 327 5676 7203 6571 -1248 -309 -2651 N
ATOM 2386 CA HIS A 327 29.348 -37.618 -13.705 1.00 49.82 C
ANISOU 2386 CA HIS A 327 5356 7183 6391 -1120 -431 -2626 C
ATOM 2387 C HIS A 327 28.675 -37.134 -14.983 1.00 49.10 C
ANISOU 2387 C HIS A 327 5307 7086 6264 -996 -379 -2465 C
ATOM 2388 O HIS A 327 29.160 -37.449 -16.075 1.00 53.81 O
ANISOU 2388 O HIS A 327 5798 7794 6851 -878 -474 -2425 O
ATOM 2389 CB HIS A 327 29.401 -39.151 -13.678 1.00 49.24 C
ANISOU 2389 CB HIS A 327 5048 7214 6448 -1213 -466 -2753 C
ATOM 2390 CG HIS A 327 28.085 -39.813 -13.937 1.00 52.49 C
ANISOU 2390 CG HIS A 327 5387 7592 6964 -1299 -319 -2732 C
ATOM 2391 ND1 HIS A 327 27.144 -40.015 -12.950 1.00 54.81 N
ANISOU 2391 ND1 HIS A 327 5720 7773 7332 -1470 -169 -2780 N
ATOM 2392 CD2 HIS A 327 27.561 -40.342 -15.068 1.00 52.90 C
ANISOU 2392 CD2 HIS A 327 5332 7710 7057 -1236 -297 -2671 C
ATOM 2393 CE1 HIS A 327 26.094 -40.630 -13.462 1.00 54.00 C
ANISOU 2393 CE1 HIS A 327 5540 7674 7305 -1508 -56 -2745 C
ATOM 2394 NE2 HIS A 327 26.320 -40.838 -14.747 1.00 52.80 N
ANISOU 2394 NE2 HIS A 327 5297 7631 7134 -1366 -133 -2683 N
ATOM 2395 N PHE A 328 27.584 -36.377 -14.876 1.00 43.03 N
ANISOU 2395 N PHE A 328 4688 6186 5475 -1017 -236 -2373 N
ATOM 2396 CA PHE A 328 27.023 -35.721 -16.048 1.00 38.81 C
ANISOU 2396 CA PHE A 328 4216 5638 4893 -886 -199 -2222 C
ATOM 2397 C PHE A 328 28.011 -34.696 -16.592 1.00 45.05 C
ANISOU 2397 C PHE A 328 5091 6459 5565 -725 -309 -2143 C
ATOM 2398 O PHE A 328 28.649 -33.957 -15.837 1.00 45.33 O
ANISOU 2398 O PHE A 328 5243 6454 5528 -722 -342 -2165 O
ATOM 2399 CB PHE A 328 25.696 -35.040 -15.709 1.00 36.42 C
ANISOU 2399 CB PHE A 328 4072 5185 4581 -936 -32 -2148 C
ATOM 2400 CG PHE A 328 24.507 -35.959 -15.757 1.00 46.10 C
ANISOU 2400 CG PHE A 328 5214 6395 5908 -1040 92 -2166 C
ATOM 2401 CD1 PHE A 328 24.634 -37.308 -15.469 1.00 49.21 C
ANISOU 2401 CD1 PHE A 328 5420 6868 6410 -1150 79 -2288 C
ATOM 2402 CD2 PHE A 328 23.259 -35.471 -16.101 1.00 49.03 C
ANISOU 2402 CD2 PHE A 328 5692 6676 6263 -1022 222 -2063 C
ATOM 2403 CE1 PHE A 328 23.534 -38.148 -15.516 1.00 49.59 C
ANISOU 2403 CE1 PHE A 328 5387 6904 6549 -1245 204 -2304 C
ATOM 2404 CE2 PHE A 328 22.156 -36.303 -16.147 1.00 49.42 C
ANISOU 2404 CE2 PHE A 328 5670 6713 6392 -1111 343 -2077 C
ATOM 2405 CZ PHE A 328 22.294 -37.645 -15.856 1.00 49.16 C
ANISOU 2405 CZ PHE A 328 5450 6760 6469 -1225 339 -2195 C
ATOM 2406 N LYS A 329 28.131 -34.657 -17.918 1.00 44.27 N
ANISOU 2406 N LYS A 329 4936 6432 5452 -591 -360 -2051 N
ATOM 2407 CA LYS A 329 29.144 -33.863 -18.600 1.00 43.21 C
ANISOU 2407 CA LYS A 329 4849 6347 5221 -435 -469 -1974 C
ATOM 2408 C LYS A 329 28.591 -32.567 -19.179 1.00 38.99 C
ANISOU 2408 C LYS A 329 4471 5726 4619 -337 -403 -1830 C
ATOM 2409 O LYS A 329 29.245 -31.951 -20.028 1.00 38.90 O
ANISOU 2409 O LYS A 329 4480 5756 4545 -200 -475 -1744 O
ATOM 2410 CB LYS A 329 29.793 -34.702 -19.701 1.00 43.03 C
ANISOU 2410 CB LYS A 329 4654 6465 5232 -347 -585 -1971 C
ATOM 2411 CG LYS A 329 30.394 -35.996 -19.174 1.00 45.44 C
ANISOU 2411 CG LYS A 329 4793 6868 5606 -431 -666 -2119 C
ATOM 2412 CD LYS A 329 30.862 -36.925 -20.281 1.00 48.71 C
ANISOU 2412 CD LYS A 329 5028 7413 6066 -346 -770 -2118 C
ATOM 2413 CE LYS A 329 31.441 -38.197 -19.679 1.00 54.83 C
ANISOU 2413 CE LYS A 329 5636 8286 6912 -431 -854 -2277 C
ATOM 2414 NZ LYS A 329 31.915 -39.173 -20.697 1.00 58.46 N
ANISOU 2414 NZ LYS A 329 5914 8876 7422 -347 -963 -2288 N
ATOM 2415 N TRP A 330 27.410 -32.142 -18.734 1.00 37.47 N
ANISOU 2415 N TRP A 330 4387 5412 4439 -403 -267 -1803 N
ATOM 2416 CA TRP A 330 26.804 -30.903 -19.212 1.00 36.96 C
ANISOU 2416 CA TRP A 330 4471 5260 4314 -313 -203 -1677 C
ATOM 2417 C TRP A 330 27.756 -29.730 -19.031 1.00 31.37 C
ANISOU 2417 C TRP A 330 3883 4538 3498 -223 -265 -1637 C
ATOM 2418 O TRP A 330 28.159 -29.418 -17.906 1.00 32.64 O
ANISOU 2418 O TRP A 330 4129 4656 3619 -283 -265 -1702 O
ATOM 2419 CB TRP A 330 25.506 -30.626 -18.456 1.00 36.57 C
ANISOU 2419 CB TRP A 330 4539 5076 4281 -409 -55 -1674 C
ATOM 2420 CG TRP A 330 24.463 -31.688 -18.539 1.00 36.89 C
ANISOU 2420 CG TRP A 330 4482 5117 4416 -504 31 -1708 C
ATOM 2421 CD1 TRP A 330 24.509 -32.842 -19.267 1.00 32.04 C
ANISOU 2421 CD1 TRP A 330 3683 4611 3879 -506 -9 -1742 C
ATOM 2422 CD2 TRP A 330 23.201 -31.689 -17.864 1.00 33.67 C
ANISOU 2422 CD2 TRP A 330 4163 4597 4035 -607 177 -1710 C
ATOM 2423 NE1 TRP A 330 23.353 -33.563 -19.081 1.00 31.24 N
ANISOU 2423 NE1 TRP A 330 3544 4475 3850 -606 108 -1768 N
ATOM 2424 CE2 TRP A 330 22.533 -32.875 -18.225 1.00 30.44 C
ANISOU 2424 CE2 TRP A 330 3612 4238 3717 -670 226 -1745 C
ATOM 2425 CE3 TRP A 330 22.571 -30.799 -16.988 1.00 31.78 C
ANISOU 2425 CE3 TRP A 330 4113 4216 3747 -647 273 -1683 C
ATOM 2426 CZ2 TRP A 330 21.265 -33.194 -17.743 1.00 31.20 C
ANISOU 2426 CZ2 TRP A 330 3752 4251 3853 -775 373 -1750 C
ATOM 2427 CZ3 TRP A 330 21.314 -31.120 -16.506 1.00 30.11 C
ANISOU 2427 CZ3 TRP A 330 3949 3916 3576 -749 414 -1685 C
ATOM 2428 CH2 TRP A 330 20.675 -32.306 -16.884 1.00 30.63 C
ANISOU 2428 CH2 TRP A 330 3872 4038 3728 -813 466 -1716 C
ATOM 2429 N GLN A 331 28.104 -29.069 -20.136 1.00 34.49 N
ANISOU 2429 N GLN A 331 4287 4967 3849 -79 -313 -1530 N
ATOM 2430 CA GLN A 331 28.908 -27.856 -20.088 1.00 35.52 C
ANISOU 2430 CA GLN A 331 4536 5082 3877 17 -354 -1475 C
ATOM 2431 C GLN A 331 28.074 -26.585 -20.200 1.00 31.78 C
ANISOU 2431 C GLN A 331 4217 4494 3365 68 -262 -1380 C
ATOM 2432 O GLN A 331 28.603 -25.494 -19.961 1.00 32.41 O
ANISOU 2432 O GLN A 331 4410 4542 3361 133 -274 -1343 O
ATOM 2433 CB GLN A 331 29.970 -27.872 -21.194 1.00 35.30 C
ANISOU 2433 CB GLN A 331 4424 5166 3823 145 -467 -1416 C
ATOM 2434 CG GLN A 331 31.025 -28.954 -21.021 1.00 44.70 C
ANISOU 2434 CG GLN A 331 5482 6476 5025 119 -580 -1509 C
ATOM 2435 CD GLN A 331 32.158 -28.835 -22.022 1.00 56.64 C
ANISOU 2435 CD GLN A 331 6942 8089 6492 255 -691 -1441 C
ATOM 2436 OE1 GLN A 331 32.723 -27.757 -22.214 1.00 61.12 O
ANISOU 2436 OE1 GLN A 331 7609 8642 6972 347 -704 -1365 O
ATOM 2437 NE2 GLN A 331 32.491 -29.944 -22.672 1.00 63.61 N
ANISOU 2437 NE2 GLN A 331 7666 9070 7433 269 -769 -1467 N
ATOM 2438 N SER A 332 26.794 -26.699 -20.552 1.00 25.38 N
ANISOU 2438 N SER A 332 3412 3623 2610 46 -173 -1343 N
ATOM 2439 CA SER A 332 25.876 -25.568 -20.541 1.00 24.36 C
ANISOU 2439 CA SER A 332 3431 3379 2447 85 -85 -1267 C
ATOM 2440 C SER A 332 24.467 -26.075 -20.270 1.00 24.26 C
ANISOU 2440 C SER A 332 3431 3294 2492 -5 25 -1284 C
ATOM 2441 O SER A 332 24.054 -27.106 -20.809 1.00 24.40 O
ANISOU 2441 O SER A 332 3323 3366 2583 -38 30 -1302 O
ATOM 2442 CB SER A 332 25.909 -24.790 -21.858 1.00 22.76 C
ANISOU 2442 CB SER A 332 3225 3194 2227 232 -113 -1151 C
ATOM 2443 OG SER A 332 24.744 -25.051 -22.622 1.00 35.71 O
ANISOU 2443 OG SER A 332 4832 4810 3927 244 -57 -1108 O
ATOM 2444 N LEU A 333 23.734 -25.341 -19.435 1.00 32.37 N
ANISOU 2444 N LEU A 333 4617 4199 3485 -41 115 -1276 N
ATOM 2445 CA LEU A 333 22.361 -25.673 -19.075 1.00 24.63 C
ANISOU 2445 CA LEU A 333 3683 3133 2541 -123 232 -1281 C
ATOM 2446 C LEU A 333 21.470 -24.467 -19.341 1.00 23.70 C
ANISOU 2446 C LEU A 333 3714 2915 2374 -36 294 -1188 C
ATOM 2447 O LEU A 333 21.824 -23.337 -18.990 1.00 23.40 O
ANISOU 2447 O LEU A 333 3798 2823 2269 23 281 -1160 O
ATOM 2448 CB LEU A 333 22.270 -26.103 -17.602 1.00 26.00 C
ANISOU 2448 CB LEU A 333 3910 3242 2728 -274 289 -1377 C
ATOM 2449 CG LEU A 333 20.898 -26.404 -16.995 1.00 28.20 C
ANISOU 2449 CG LEU A 333 4261 3414 3038 -376 425 -1382 C
ATOM 2450 CD1 LEU A 333 20.141 -27.424 -17.826 1.00 26.50 C
ANISOU 2450 CD1 LEU A 333 3916 3260 2894 -394 461 -1373 C
ATOM 2451 CD2 LEU A 333 21.063 -26.894 -15.563 1.00 28.09 C
ANISOU 2451 CD2 LEU A 333 4277 3345 3050 -531 464 -1485 C
ATOM 2452 N SER A 334 20.317 -24.707 -19.966 1.00 27.38 N
ANISOU 2452 N SER A 334 4170 3361 2873 -22 357 -1145 N
ATOM 2453 CA SER A 334 19.431 -23.622 -20.376 1.00 28.44 C
ANISOU 2453 CA SER A 334 4429 3413 2964 75 402 -1058 C
ATOM 2454 C SER A 334 18.002 -23.958 -19.979 1.00 26.22 C
ANISOU 2454 C SER A 334 4220 3048 2695 6 523 -1057 C
ATOM 2455 O SER A 334 17.425 -24.923 -20.492 1.00 28.76 O
ANISOU 2455 O SER A 334 4439 3417 3070 -27 552 -1068 O
ATOM 2456 CB SER A 334 19.527 -23.376 -21.886 1.00 35.16 C
ANISOU 2456 CB SER A 334 5192 4335 3832 208 336 -989 C
ATOM 2457 OG SER A 334 19.330 -22.006 -22.194 1.00 42.16 O
ANISOU 2457 OG SER A 334 6194 5161 4666 322 333 -915 O
ATOM 2458 N ILE A 335 17.428 -23.154 -19.087 1.00 25.73 N
ANISOU 2458 N ILE A 335 4336 2861 2579 -8 594 -1041 N
ATOM 2459 CA ILE A 335 16.069 -23.345 -18.593 1.00 28.74 C
ANISOU 2459 CA ILE A 335 4818 3146 2956 -69 716 -1029 C
ATOM 2460 C ILE A 335 15.296 -22.068 -18.889 1.00 28.30 C
ANISOU 2460 C ILE A 335 4915 3005 2834 55 738 -946 C
ATOM 2461 O ILE A 335 15.490 -21.047 -18.217 1.00 28.33 O
ANISOU 2461 O ILE A 335 5039 2933 2791 85 729 -924 O
ATOM 2462 CB ILE A 335 16.050 -23.673 -17.095 1.00 28.47 C
ANISOU 2462 CB ILE A 335 4865 3028 2925 -216 788 -1095 C
ATOM 2463 CG1 ILE A 335 16.964 -24.866 -16.814 1.00 27.77 C
ANISOU 2463 CG1 ILE A 335 4612 3033 2906 -330 745 -1188 C
ATOM 2464 CG2 ILE A 335 14.639 -23.974 -16.628 1.00 32.12 C
ANISOU 2464 CG2 ILE A 335 5425 3392 3386 -285 924 -1075 C
ATOM 2465 CD1 ILE A 335 17.556 -24.858 -15.433 1.00 33.81 C
ANISOU 2465 CD1 ILE A 335 5441 3736 3668 -439 755 -1264 C
ATOM 2466 N ILE A 336 14.418 -22.121 -19.887 1.00 25.50 N
ANISOU 2466 N ILE A 336 4533 2670 2484 129 754 -896 N
ATOM 2467 CA ILE A 336 13.743 -20.940 -20.412 1.00 26.84 C
ANISOU 2467 CA ILE A 336 4765 2804 2629 257 724 -794 C
ATOM 2468 C ILE A 336 12.238 -21.166 -20.364 1.00 30.15 C
ANISOU 2468 C ILE A 336 5250 3168 3039 242 813 -753 C
ATOM 2469 O ILE A 336 11.751 -22.221 -20.788 1.00 30.53 O
ANISOU 2469 O ILE A 336 5245 3250 3103 203 873 -793 O
ATOM 2470 CB ILE A 336 14.206 -20.626 -21.848 1.00 28.96 C
ANISOU 2470 CB ILE A 336 4912 3167 2924 379 624 -758 C
ATOM 2471 CG1 ILE A 336 15.695 -20.269 -21.853 1.00 29.90 C
ANISOU 2471 CG1 ILE A 336 4987 3335 3039 404 540 -783 C
ATOM 2472 CG2 ILE A 336 13.380 -19.509 -22.460 1.00 29.25 C
ANISOU 2472 CG2 ILE A 336 4965 3181 2967 480 585 -650 C
ATOM 2473 CD1 ILE A 336 16.242 -19.921 -23.214 1.00 36.01 C
ANISOU 2473 CD1 ILE A 336 5649 4191 3843 519 448 -740 C
ATOM 2474 N ARG A 337 11.508 -20.172 -19.848 1.00 25.01 N
ANISOU 2474 N ARG A 337 4714 2431 2356 276 823 -674 N
ATOM 2475 CA ARG A 337 10.042 -20.199 -19.801 1.00 22.86 C
ANISOU 2475 CA ARG A 337 4527 2100 2060 281 897 -619 C
ATOM 2476 C ARG A 337 9.523 -21.476 -19.152 1.00 25.59 C
ANISOU 2476 C ARG A 337 4914 2408 2400 149 1035 -684 C
ATOM 2477 O ARG A 337 8.514 -22.043 -19.573 1.00 36.31 O
ANISOU 2477 O ARG A 337 6272 3773 3751 150 1100 -670 O
ATOM 2478 CB ARG A 337 9.438 -20.026 -21.198 1.00 22.10 C
ANISOU 2478 CB ARG A 337 4345 2072 1981 392 839 -568 C
ATOM 2479 CG ARG A 337 9.902 -18.782 -21.924 1.00 25.80 C
ANISOU 2479 CG ARG A 337 4760 2576 2467 503 716 -507 C
ATOM 2480 CD ARG A 337 9.069 -18.520 -23.162 1.00 29.09 C
ANISOU 2480 CD ARG A 337 5117 3034 2900 595 670 -453 C
ATOM 2481 NE ARG A 337 8.666 -19.762 -23.810 1.00 45.65 N
ANISOU 2481 NE ARG A 337 7143 5186 5017 574 712 -502 N
ATOM 2482 CZ ARG A 337 9.378 -20.379 -24.745 1.00 47.37 C
ANISOU 2482 CZ ARG A 337 7222 5494 5284 593 667 -548 C
ATOM 2483 NH1 ARG A 337 8.929 -21.506 -25.276 1.00 37.90 N
ANISOU 2483 NH1 ARG A 337 5959 4342 4099 577 713 -593 N
ATOM 2484 NH2 ARG A 337 10.532 -19.869 -25.154 1.00 52.59 N
ANISOU 2484 NH2 ARG A 337 7808 6196 5976 631 579 -546 N
ATOM 2485 N CYS A 338 10.223 -21.936 -18.125 1.00 26.76 N
ANISOU 2485 N CYS A 338 5091 2520 2556 28 1082 -762 N
ATOM 2486 CA CYS A 338 9.840 -23.132 -17.400 1.00 25.87 C
ANISOU 2486 CA CYS A 338 5007 2367 2454 -128 1223 -839 C
ATOM 2487 C CYS A 338 9.091 -22.738 -16.122 1.00 33.11 C
ANISOU 2487 C CYS A 338 6110 3136 3332 -193 1320 -802 C
ATOM 2488 O CYS A 338 8.697 -21.576 -15.951 1.00 28.59 O
ANISOU 2488 O CYS A 338 5639 2504 2720 -100 1277 -708 O
ATOM 2489 CB CYS A 338 11.083 -23.982 -17.139 1.00 26.18 C
ANISOU 2489 CB CYS A 338 4894 2488 2565 -235 1178 -932 C
ATOM 2490 SG CYS A 338 11.789 -24.722 -18.630 1.00 38.43 S
ANISOU 2490 SG CYS A 338 6196 4224 4183 -174 1066 -954 S
ATOM 2491 N GLN A 339 8.872 -23.699 -15.223 1.00 33.11 N
ANISOU 2491 N GLN A 339 6144 3082 3356 -357 1448 -871 N
ATOM 2492 CA GLN A 339 7.990 -23.479 -14.079 1.00 31.29 C
ANISOU 2492 CA GLN A 339 6111 2693 3084 -428 1575 -841 C
ATOM 2493 C GLN A 339 8.638 -23.953 -12.788 1.00 39.65 C
ANISOU 2493 C GLN A 339 7170 3694 4201 -598 1612 -916 C
ATOM 2494 O GLN A 339 8.005 -24.627 -11.969 1.00 45.90 O
ANISOU 2494 O GLN A 339 8012 4409 5018 -734 1741 -926 O
ATOM 2495 CB GLN A 339 6.647 -24.176 -14.283 1.00 32.52 C
ANISOU 2495 CB GLN A 339 6297 2835 3224 -459 1705 -801 C
ATOM 2496 CG GLN A 339 6.013 -23.897 -15.628 1.00 34.33 C
ANISOU 2496 CG GLN A 339 6480 3146 3416 -300 1650 -731 C
ATOM 2497 CD GLN A 339 4.718 -24.638 -15.807 1.00 41.08 C
ANISOU 2497 CD GLN A 339 7374 3990 4243 -330 1788 -705 C
ATOM 2498 OE1 GLN A 339 4.267 -25.341 -14.905 1.00 39.23 O
ANISOU 2498 OE1 GLN A 339 7192 3689 4024 -474 1926 -721 O
ATOM 2499 NE2 GLN A 339 4.105 -24.488 -16.974 1.00 39.15 N
ANISOU 2499 NE2 GLN A 339 7068 3824 3982 -199 1725 -643 N
ATOM 2500 N LEU A 340 9.900 -23.591 -12.578 1.00 33.10 N
ANISOU 2500 N LEU A 340 6287 2897 3392 -591 1502 -970 N
ATOM 2501 CA LEU A 340 10.584 -23.980 -11.354 1.00 38.82 C
ANISOU 2501 CA LEU A 340 7012 3568 4171 -744 1521 -1052 C
ATOM 2502 C LEU A 340 9.946 -23.304 -10.148 1.00 41.28 C
ANISOU 2502 C LEU A 340 7559 3689 4438 -782 1615 -1022 C
ATOM 2503 O LEU A 340 9.851 -22.074 -10.084 1.00 43.72 O
ANISOU 2503 O LEU A 340 7958 3964 4688 -653 1549 -928 O
ATOM 2504 CB LEU A 340 12.069 -23.625 -11.434 1.00 30.94 C
ANISOU 2504 CB LEU A 340 5922 2647 3186 -705 1375 -1113 C
ATOM 2505 CG LEU A 340 12.879 -24.479 -12.408 1.00 35.90 C
ANISOU 2505 CG LEU A 340 6310 3458 3874 -699 1282 -1159 C
ATOM 2506 CD1 LEU A 340 14.362 -24.190 -12.274 1.00 37.48 C
ANISOU 2506 CD1 LEU A 340 6439 3722 4081 -679 1151 -1222 C
ATOM 2507 CD2 LEU A 340 12.588 -25.955 -12.185 1.00 33.65 C
ANISOU 2507 CD2 LEU A 340 5893 3216 3679 -858 1360 -1217 C
ATOM 2508 N LYS A 341 9.491 -24.121 -9.196 1.00 39.02 N
ANISOU 2508 N LYS A 341 7299 3322 4204 -953 1737 -1054 N
ATOM 2509 CA LYS A 341 8.979 -23.617 -7.928 1.00 48.91 C
ANISOU 2509 CA LYS A 341 8767 4384 5432 -1015 1831 -1034 C
ATOM 2510 C LYS A 341 10.084 -23.163 -6.986 1.00 53.15 C
ANISOU 2510 C LYS A 341 9295 4901 5997 -1048 1739 -1084 C
ATOM 2511 O LYS A 341 9.806 -22.433 -6.027 1.00 58.86 O
ANISOU 2511 O LYS A 341 10162 5512 6690 -1041 1761 -1032 O
ATOM 2512 CB LYS A 341 8.160 -24.698 -7.218 1.00 57.61 C
ANISOU 2512 CB LYS A 341 9880 5414 6595 -1196 1995 -1045 C
ATOM 2513 CG LYS A 341 6.770 -24.923 -7.774 1.00 62.50 C
ANISOU 2513 CG LYS A 341 10561 6022 7165 -1156 2110 -949 C
ATOM 2514 CD LYS A 341 6.043 -26.000 -6.983 1.00 68.42 C
ANISOU 2514 CD LYS A 341 11318 6700 7980 -1347 2282 -960 C
ATOM 2515 CE LYS A 341 4.547 -25.934 -7.223 1.00 73.84 C
ANISOU 2515 CE LYS A 341 12150 7321 8585 -1298 2416 -848 C
ATOM 2516 NZ LYS A 341 4.213 -26.091 -8.661 1.00 72.70 N
ANISOU 2516 NZ LYS A 341 11894 7329 8399 -1165 2368 -811 N
ATOM 2517 N GLN A 342 11.324 -23.574 -7.241 1.00 47.59 N
ANISOU 2517 N GLN A 342 8428 4311 5344 -1075 1634 -1185 N
ATOM 2518 CA GLN A 342 12.399 -23.470 -6.263 1.00 43.61 C
ANISOU 2518 CA GLN A 342 7898 3792 4880 -1142 1564 -1263 C
ATOM 2519 C GLN A 342 13.718 -23.481 -7.019 1.00 39.94 C
ANISOU 2519 C GLN A 342 7271 3485 4420 -1072 1411 -1326 C
ATOM 2520 O GLN A 342 13.892 -24.283 -7.942 1.00 38.31 O
ANISOU 2520 O GLN A 342 6914 3398 4244 -1082 1392 -1364 O
ATOM 2521 CB GLN A 342 12.302 -24.633 -5.263 1.00 46.80 C
ANISOU 2521 CB GLN A 342 8272 4124 5384 -1368 1669 -1362 C
ATOM 2522 CG GLN A 342 13.498 -24.861 -4.366 1.00 54.16 C
ANISOU 2522 CG GLN A 342 9127 5073 6380 -1459 1588 -1474 C
ATOM 2523 CD GLN A 342 13.188 -25.852 -3.256 1.00 61.01 C
ANISOU 2523 CD GLN A 342 9981 5849 7349 -1675 1702 -1545 C
ATOM 2524 OE1 GLN A 342 12.093 -25.844 -2.694 1.00 63.19 O
ANISOU 2524 OE1 GLN A 342 10389 5996 7625 -1731 1840 -1478 O
ATOM 2525 NE2 GLN A 342 14.146 -26.716 -2.945 1.00 66.04 N
ANISOU 2525 NE2 GLN A 342 10454 6561 8078 -1792 1643 -1678 N
ATOM 2526 N PHE A 343 14.626 -22.579 -6.646 1.00 38.12 N
ANISOU 2526 N PHE A 343 7058 3267 4158 -990 1298 -1324 N
ATOM 2527 CA PHE A 343 15.867 -22.427 -7.391 1.00 34.43 C
ANISOU 2527 CA PHE A 343 6460 2945 3678 -901 1155 -1365 C
ATOM 2528 C PHE A 343 16.632 -23.749 -7.408 1.00 36.13 C
ANISOU 2528 C PHE A 343 6513 3246 3969 -1041 1134 -1507 C
ATOM 2529 O PHE A 343 16.658 -24.463 -6.401 1.00 43.75 O
ANISOU 2529 O PHE A 343 7471 4150 5004 -1204 1188 -1591 O
ATOM 2530 CB PHE A 343 16.734 -21.319 -6.789 1.00 35.17 C
ANISOU 2530 CB PHE A 343 6606 3027 3732 -815 1055 -1354 C
ATOM 2531 CG PHE A 343 17.810 -20.823 -7.714 1.00 32.96 C
ANISOU 2531 CG PHE A 343 6226 2885 3413 -678 920 -1350 C
ATOM 2532 CD1 PHE A 343 17.513 -19.907 -8.712 1.00 31.24 C
ANISOU 2532 CD1 PHE A 343 6016 2710 3143 -512 883 -1237 C
ATOM 2533 CD2 PHE A 343 19.111 -21.283 -7.600 1.00 32.47 C
ANISOU 2533 CD2 PHE A 343 6057 2911 3368 -716 830 -1460 C
ATOM 2534 CE1 PHE A 343 18.492 -19.453 -9.571 1.00 29.59 C
ANISOU 2534 CE1 PHE A 343 5714 2623 2906 -394 770 -1228 C
ATOM 2535 CE2 PHE A 343 20.098 -20.831 -8.458 1.00 32.49 C
ANISOU 2535 CE2 PHE A 343 5981 3039 3327 -589 715 -1450 C
ATOM 2536 CZ PHE A 343 19.788 -19.912 -9.445 1.00 33.51 C
ANISOU 2536 CZ PHE A 343 6121 3202 3410 -430 691 -1332 C
ATOM 2537 N PRO A 344 17.236 -24.117 -8.537 1.00 37.61 N
ANISOU 2537 N PRO A 344 6545 3589 4157 -977 1050 -1522 N
ATOM 2538 CA PRO A 344 17.884 -25.428 -8.627 1.00 33.87 C
ANISOU 2538 CA PRO A 344 5861 3238 3771 -1083 1007 -1616 C
ATOM 2539 C PRO A 344 19.057 -25.553 -7.671 1.00 46.50 C
ANISOU 2539 C PRO A 344 7435 4841 5393 -1160 930 -1737 C
ATOM 2540 O PRO A 344 19.751 -24.580 -7.364 1.00 51.07 O
ANISOU 2540 O PRO A 344 8111 5391 5904 -1081 862 -1744 O
ATOM 2541 CB PRO A 344 18.361 -25.491 -10.083 1.00 32.37 C
ANISOU 2541 CB PRO A 344 5524 3216 3561 -949 905 -1573 C
ATOM 2542 CG PRO A 344 17.608 -24.438 -10.802 1.00 38.67 C
ANISOU 2542 CG PRO A 344 6443 3968 4280 -801 931 -1450 C
ATOM 2543 CD PRO A 344 17.321 -23.368 -9.802 1.00 35.17 C
ANISOU 2543 CD PRO A 344 6219 3363 3780 -793 979 -1433 C
ATOM 2544 N THR A 345 19.267 -26.777 -7.198 1.00 52.86 N
ANISOU 2544 N THR A 345 8105 5683 6296 -1316 943 -1839 N
ATOM 2545 CA THR A 345 20.486 -27.154 -6.498 1.00 60.78 C
ANISOU 2545 CA THR A 345 9028 6733 7333 -1387 846 -1972 C
ATOM 2546 C THR A 345 21.376 -27.889 -7.492 1.00 59.18 C
ANISOU 2546 C THR A 345 8606 6729 7150 -1336 724 -2005 C
ATOM 2547 O THR A 345 21.020 -28.974 -7.967 1.00 54.28 O
ANISOU 2547 O THR A 345 7832 6186 6606 -1398 753 -2019 O
ATOM 2548 CB THR A 345 20.189 -28.028 -5.280 1.00 65.59 C
ANISOU 2548 CB THR A 345 9623 7250 8047 -1595 930 -2075 C
ATOM 2549 OG1 THR A 345 19.365 -29.133 -5.669 1.00 67.27 O
ANISOU 2549 OG1 THR A 345 9713 7501 8344 -1685 1021 -2062 O
ATOM 2550 CG2 THR A 345 19.477 -27.221 -4.202 1.00 62.01 C
ANISOU 2550 CG2 THR A 345 9391 6599 7572 -1629 1030 -2030 C
ATOM 2551 N LEU A 346 22.518 -27.286 -7.819 1.00 54.62 N
ANISOU 2551 N LEU A 346 8019 6234 6500 -1217 592 -2014 N
ATOM 2552 CA LEU A 346 23.388 -27.777 -8.878 1.00 51.85 C
ANISOU 2552 CA LEU A 346 7488 6066 6146 -1134 470 -2021 C
ATOM 2553 C LEU A 346 24.830 -27.723 -8.401 1.00 54.58 C
ANISOU 2553 C LEU A 346 7797 6481 6462 -1123 337 -2124 C
ATOM 2554 O LEU A 346 25.264 -26.708 -7.850 1.00 56.22 O
ANISOU 2554 O LEU A 346 8148 6622 6592 -1070 312 -2125 O
ATOM 2555 CB LEU A 346 23.238 -26.936 -10.152 1.00 47.16 C
ANISOU 2555 CB LEU A 346 6926 5519 5473 -952 445 -1885 C
ATOM 2556 CG LEU A 346 21.852 -26.733 -10.768 1.00 45.52 C
ANISOU 2556 CG LEU A 346 6778 5249 5268 -920 559 -1771 C
ATOM 2557 CD1 LEU A 346 21.847 -25.476 -11.627 1.00 39.37 C
ANISOU 2557 CD1 LEU A 346 6093 4471 4396 -739 527 -1654 C
ATOM 2558 CD2 LEU A 346 21.442 -27.938 -11.593 1.00 46.08 C
ANISOU 2558 CD2 LEU A 346 6667 5421 5419 -957 575 -1771 C
ATOM 2559 N ASP A 347 25.572 -28.811 -8.619 1.00 52.36 N
ANISOU 2559 N ASP A 347 7359 6733 5805 -664 1186 -1705 N
ATOM 2560 CA ASP A 347 27.003 -28.837 -8.336 1.00 54.09 C
ANISOU 2560 CA ASP A 347 7446 7047 6059 -771 1163 -1746 C
ATOM 2561 C ASP A 347 27.788 -29.421 -9.505 1.00 54.49 C
ANISOU 2561 C ASP A 347 7396 7210 6097 -690 1036 -1758 C
ATOM 2562 O ASP A 347 28.867 -29.983 -9.309 1.00 65.42 O
ANISOU 2562 O ASP A 347 8641 8709 7508 -784 1031 -1816 O
ATOM 2563 CB ASP A 347 27.303 -29.606 -7.048 1.00 59.98 C
ANISOU 2563 CB ASP A 347 8110 7837 6843 -967 1301 -1831 C
ATOM 2564 CG ASP A 347 26.671 -30.989 -7.018 1.00 71.47 C
ANISOU 2564 CG ASP A 347 9533 9336 8288 -986 1369 -1894 C
ATOM 2565 OD1 ASP A 347 26.659 -31.681 -8.058 1.00 75.01 O
ANISOU 2565 OD1 ASP A 347 9940 9854 8708 -879 1286 -1899 O
ATOM 2566 OD2 ASP A 347 26.210 -31.396 -5.934 1.00 77.45 O
ANISOU 2566 OD2 ASP A 347 10305 10056 9066 -1113 1509 -1940 O
ATOM 2567 N LEU A 348 27.257 -29.295 -10.726 1.00 46.16 N
ANISOU 2567 N LEU A 348 6412 6126 5002 -516 933 -1704 N
ATOM 2568 CA LEU A 348 27.911 -29.822 -11.917 1.00 39.76 C
ANISOU 2568 CA LEU A 348 5530 5402 4176 -432 814 -1704 C
ATOM 2569 C LEU A 348 29.277 -29.167 -12.090 1.00 46.60 C
ANISOU 2569 C LEU A 348 6317 6319 5071 -467 735 -1690 C
ATOM 2570 O LEU A 348 29.367 -27.954 -12.314 1.00 48.94 O
ANISOU 2570 O LEU A 348 6685 6542 5367 -412 679 -1627 O
ATOM 2571 CB LEU A 348 27.038 -29.606 -13.154 1.00 35.69 C
ANISOU 2571 CB LEU A 348 5132 4817 3612 -240 722 -1639 C
ATOM 2572 CG LEU A 348 25.682 -30.320 -13.105 1.00 40.13 C
ANISOU 2572 CG LEU A 348 5766 5342 4140 -185 791 -1651 C
ATOM 2573 CD1 LEU A 348 24.913 -30.137 -14.404 1.00 32.66 C
ANISOU 2573 CD1 LEU A 348 4926 4340 3142 12 687 -1591 C
ATOM 2574 CD2 LEU A 348 25.863 -31.797 -12.787 1.00 44.19 C
ANISOU 2574 CD2 LEU A 348 6170 5959 4661 -275 866 -1733 C
ATOM 2575 N PRO A 349 30.367 -29.936 -11.974 1.00 47.05 N
ANISOU 2575 N PRO A 349 6217 6507 5151 -557 730 -1752 N
ATOM 2576 CA PRO A 349 31.705 -29.324 -11.979 1.00 42.45 C
ANISOU 2576 CA PRO A 349 5550 5981 4597 -602 671 -1744 C
ATOM 2577 C PRO A 349 32.191 -28.886 -13.349 1.00 37.18 C
ANISOU 2577 C PRO A 349 4896 5315 3916 -474 528 -1682 C
ATOM 2578 O PRO A 349 33.152 -28.110 -13.416 1.00 38.25 O
ANISOU 2578 O PRO A 349 4996 5466 4071 -490 478 -1656 O
ATOM 2579 CB PRO A 349 32.606 -30.437 -11.415 1.00 45.35 C
ANISOU 2579 CB PRO A 349 5739 6501 4990 -731 715 -1839 C
ATOM 2580 CG PRO A 349 31.663 -31.466 -10.838 1.00 45.63 C
ANISOU 2580 CG PRO A 349 5780 6539 5020 -782 820 -1900 C
ATOM 2581 CD PRO A 349 30.421 -31.370 -11.658 1.00 47.70 C
ANISOU 2581 CD PRO A 349 6186 6698 5240 -634 790 -1840 C
ATOM 2582 N PHE A 350 31.582 -29.362 -14.435 1.00 35.05 N
ANISOU 2582 N PHE A 350 4676 5028 3615 -354 465 -1656 N
ATOM 2583 CA PHE A 350 31.996 -28.989 -15.781 1.00 36.85 C
ANISOU 2583 CA PHE A 350 4921 5247 3834 -245 337 -1595 C
ATOM 2584 C PHE A 350 31.063 -27.966 -16.416 1.00 31.24 C
ANISOU 2584 C PHE A 350 4389 4383 3096 -128 294 -1509 C
ATOM 2585 O PHE A 350 31.223 -27.649 -17.600 1.00 35.53 O
ANISOU 2585 O PHE A 350 4965 4900 3635 -49 200 -1453 O
ATOM 2586 CB PHE A 350 32.087 -30.228 -16.673 1.00 42.23 C
ANISOU 2586 CB PHE A 350 5520 6021 4504 -200 289 -1625 C
ATOM 2587 CG PHE A 350 33.020 -31.287 -16.157 1.00 51.37 C
ANISOU 2587 CG PHE A 350 6492 7341 5685 -299 317 -1713 C
ATOM 2588 CD1 PHE A 350 34.226 -30.943 -15.566 1.00 48.73 C
ANISOU 2588 CD1 PHE A 350 6054 7079 5381 -389 320 -1736 C
ATOM 2589 CD2 PHE A 350 32.687 -32.627 -16.258 1.00 60.65 C
ANISOU 2589 CD2 PHE A 350 7597 8599 6847 -300 342 -1775 C
ATOM 2590 CE1 PHE A 350 35.082 -31.919 -15.088 1.00 48.26 C
ANISOU 2590 CE1 PHE A 350 5826 7172 5339 -477 347 -1819 C
ATOM 2591 CE2 PHE A 350 33.538 -33.607 -15.783 1.00 60.77 C
ANISOU 2591 CE2 PHE A 350 7437 8770 6882 -390 366 -1861 C
ATOM 2592 CZ PHE A 350 34.737 -33.253 -15.197 1.00 54.43 C
ANISOU 2592 CZ PHE A 350 6533 8038 6108 -478 367 -1884 C
ATOM 2593 N LEU A 351 30.103 -27.440 -15.659 1.00 26.12 N
ANISOU 2593 N LEU A 351 3850 3641 2435 -122 364 -1499 N
ATOM 2594 CA LEU A 351 29.124 -26.506 -16.199 1.00 32.57 C
ANISOU 2594 CA LEU A 351 4834 4322 3219 3 321 -1425 C
ATOM 2595 C LEU A 351 29.752 -25.124 -16.345 1.00 30.14 C
ANISOU 2595 C LEU A 351 4557 3965 2931 14 258 -1371 C
ATOM 2596 O LEU A 351 30.196 -24.529 -15.357 1.00 32.32 O
ANISOU 2596 O LEU A 351 4788 4256 3238 -67 303 -1390 O
ATOM 2597 CB LEU A 351 27.897 -26.453 -15.294 1.00 26.89 C
ANISOU 2597 CB LEU A 351 4183 3548 2486 15 410 -1445 C
ATOM 2598 CG LEU A 351 26.670 -25.746 -15.872 1.00 27.44 C
ANISOU 2598 CG LEU A 351 4386 3518 2521 178 353 -1395 C
ATOM 2599 CD1 LEU A 351 26.005 -26.609 -16.931 1.00 30.64 C
ANISOU 2599 CD1 LEU A 351 4850 3902 2890 270 322 -1361 C
ATOM 2600 CD2 LEU A 351 25.680 -25.377 -14.777 1.00 24.43 C
ANISOU 2600 CD2 LEU A 351 4014 3110 2159 141 449 -1425 C
ATOM 2601 N LYS A 352 29.787 -24.615 -17.575 1.00 25.68 N
ANISOU 2601 N LYS A 352 4070 3336 2352 82 176 -1299 N
ATOM 2602 CA LYS A 352 30.372 -23.312 -17.863 1.00 26.69 C
ANISOU 2602 CA LYS A 352 4231 3413 2498 79 124 -1242 C
ATOM 2603 C LYS A 352 29.339 -22.211 -18.038 1.00 28.34 C
ANISOU 2603 C LYS A 352 4560 3490 2717 129 128 -1142 C
ATOM 2604 O LYS A 352 29.624 -21.056 -17.701 1.00 33.40 O
ANISOU 2604 O LYS A 352 5206 4103 3381 152 91 -1111 O
ATOM 2605 CB LYS A 352 31.246 -23.396 -19.123 1.00 23.27 C
ANISOU 2605 CB LYS A 352 3703 3040 2098 49 58 -1218 C
ATOM 2606 CG LYS A 352 32.446 -24.331 -18.981 1.00 32.93 C
ANISOU 2606 CG LYS A 352 4751 4414 3348 10 30 -1277 C
ATOM 2607 CD LYS A 352 32.875 -24.907 -20.326 1.00 44.17 C
ANISOU 2607 CD LYS A 352 6075 5913 4794 54 -53 -1266 C
ATOM 2608 CE LYS A 352 34.002 -24.110 -20.978 1.00 50.25 C
ANISOU 2608 CE LYS A 352 6776 6713 5603 64 -132 -1227 C
ATOM 2609 NZ LYS A 352 35.314 -24.302 -20.295 1.00 55.32 N
ANISOU 2609 NZ LYS A 352 7312 7450 6256 0 -127 -1268 N
ATOM 2610 N SER A 353 28.149 -22.536 -18.539 1.00 24.76 N
ANISOU 2610 N SER A 353 4164 2978 2266 81 218 -1112 N
ATOM 2611 CA SER A 353 27.108 -21.548 -18.783 1.00 26.93 C
ANISOU 2611 CA SER A 353 4167 3375 2689 -17 293 -1235 C
ATOM 2612 C SER A 353 25.805 -22.026 -18.158 1.00 27.83 C
ANISOU 2612 C SER A 353 4172 3573 2831 110 262 -1342 C
ATOM 2613 O SER A 353 25.452 -23.203 -18.273 1.00 21.91 O
ANISOU 2613 O SER A 353 3390 2867 2069 99 295 -1379 O
ATOM 2614 CB SER A 353 26.930 -21.307 -20.289 1.00 25.77 C
ANISOU 2614 CB SER A 353 4078 3194 2519 128 164 -1191 C
ATOM 2615 OG SER A 353 28.153 -20.902 -20.883 1.00 43.07 O
ANISOU 2615 OG SER A 353 6241 5406 4719 146 69 -1136 O
ATOM 2616 N LEU A 354 25.102 -21.117 -17.483 1.00 24.13 N
ANISOU 2616 N LEU A 354 3802 3027 2339 195 247 -1330 N
ATOM 2617 CA LEU A 354 23.804 -21.414 -16.886 1.00 23.22 C
ANISOU 2617 CA LEU A 354 3801 2845 2175 245 306 -1347 C
ATOM 2618 C LEU A 354 22.837 -20.294 -17.232 1.00 25.13 C
ANISOU 2618 C LEU A 354 4182 2946 2419 271 319 -1235 C
ATOM 2619 O LEU A 354 23.097 -19.128 -16.915 1.00 21.68 O
ANISOU 2619 O LEU A 354 3786 2457 1993 264 305 -1184 O
ATOM 2620 CB LEU A 354 23.904 -21.575 -15.365 1.00 23.07 C
ANISOU 2620 CB LEU A 354 3870 2793 2102 233 367 -1352 C
ATOM 2621 CG LEU A 354 22.569 -21.796 -14.643 1.00 28.26 C
ANISOU 2621 CG LEU A 354 4646 3357 2734 210 485 -1324 C
ATOM 2622 CD1 LEU A 354 21.850 -23.022 -15.190 1.00 31.93 C
ANISOU 2622 CD1 LEU A 354 5090 3864 3177 259 493 -1365 C
ATOM 2623 CD2 LEU A 354 22.758 -21.914 -13.134 1.00 24.83 C
ANISOU 2623 CD2 LEU A 354 4277 2876 2279 100 611 -1321 C
ATOM 2624 N THR A 355 21.726 -20.647 -17.876 1.00 28.30 N
ANISOU 2624 N THR A 355 4667 3287 2799 335 320 -1180 N
ATOM 2625 CA THR A 355 20.663 -19.704 -18.196 1.00 25.79 C
ANISOU 2625 CA THR A 355 4499 2843 2457 424 289 -1054 C
ATOM 2626 C THR A 355 19.371 -20.199 -17.559 1.00 30.50 C
ANISOU 2626 C THR A 355 5198 3380 3012 446 374 -1050 C
ATOM 2627 O THR A 355 18.879 -21.283 -17.899 1.00 33.12 O
ANISOU 2627 O THR A 355 5517 3739 3329 467 394 -1083 O
ATOM 2628 CB THR A 355 20.490 -19.534 -19.711 1.00 23.34 C
ANISOU 2628 CB THR A 355 4216 2511 2142 534 164 -959 C
ATOM 2629 OG1 THR A 355 21.641 -18.886 -20.261 1.00 29.63 O
ANISOU 2629 OG1 THR A 355 4945 3341 2971 526 82 -937 O
ATOM 2630 CG2 THR A 355 19.271 -18.685 -20.010 1.00 24.57 C
ANISOU 2630 CG2 THR A 355 4518 2563 2254 648 115 -840 C
ATOM 2631 N LEU A 356 18.841 -19.418 -16.622 1.00 28.00 N
ANISOU 2631 N LEU A 356 4988 2979 2673 435 432 -1007 N
ATOM 2632 CA LEU A 356 17.525 -19.647 -16.035 1.00 25.94 C
ANISOU 2632 CA LEU A 356 4861 2631 2364 460 518 -971 C
ATOM 2633 C LEU A 356 16.763 -18.337 -16.175 1.00 30.63 C
ANISOU 2633 C LEU A 356 5597 3118 2924 537 480 -849 C
ATOM 2634 O LEU A 356 17.038 -17.377 -15.447 1.00 31.13 O
ANISOU 2634 O LEU A 356 5696 3144 2989 499 504 -828 O
ATOM 2635 CB LEU A 356 17.633 -20.081 -14.572 1.00 30.50 C
ANISOU 2635 CB LEU A 356 5447 3207 2936 358 648 -1034 C
ATOM 2636 CG LEU A 356 16.341 -20.155 -13.754 1.00 35.25 C
ANISOU 2636 CG LEU A 356 6207 3698 3489 360 764 -986 C
ATOM 2637 CD1 LEU A 356 15.321 -21.059 -14.421 1.00 42.40 C
ANISOU 2637 CD1 LEU A 356 7151 4594 4366 434 767 -977 C
ATOM 2638 CD2 LEU A 356 16.636 -20.643 -12.350 1.00 37.33 C
ANISOU 2638 CD2 LEU A 356 6471 3959 3753 240 896 -1043 C
ATOM 2639 N THR A 357 15.823 -18.285 -17.119 1.00 28.47 N
ANISOU 2639 N THR A 357 5403 2802 2611 652 412 -769 N
ATOM 2640 CA THR A 357 15.216 -17.016 -17.489 1.00 26.50 C
ANISOU 2640 CA THR A 357 5269 2482 2319 746 335 -655 C
ATOM 2641 C THR A 357 13.735 -17.196 -17.794 1.00 31.52 C
ANISOU 2641 C THR A 357 6045 3049 2880 850 336 -581 C
ATOM 2642 O THR A 357 13.288 -18.272 -18.211 1.00 27.06 O
ANISOU 2642 O THR A 357 5471 2504 2308 876 348 -603 O
ATOM 2643 CB THR A 357 15.935 -16.394 -18.693 1.00 26.72 C
ANISOU 2643 CB THR A 357 5226 2558 2368 807 181 -616 C
ATOM 2644 OG1 THR A 357 15.547 -15.022 -18.840 1.00 30.59 O
ANISOU 2644 OG1 THR A 357 5807 2998 2816 878 111 -524 O
ATOM 2645 CG2 THR A 357 15.600 -17.149 -19.962 1.00 28.82 C
ANISOU 2645 CG2 THR A 357 5472 2859 2621 898 89 -593 C
ATOM 2646 N MET A 358 12.979 -16.120 -17.572 1.00 29.40 N
ANISOU 2646 N MET A 358 5910 2707 2552 910 321 -494 N
ATOM 2647 CA MET A 358 11.544 -16.082 -17.854 1.00 25.81 C
ANISOU 2647 CA MET A 358 5606 2190 2011 1020 310 -412 C
ATOM 2648 C MET A 358 10.803 -17.206 -17.132 1.00 26.88 C
ANISOU 2648 C MET A 358 5796 2283 2133 980 453 -448 C
ATOM 2649 O MET A 358 9.805 -17.730 -17.630 1.00 32.09 O
ANISOU 2649 O MET A 358 6532 2921 2741 1063 442 -410 O
ATOM 2650 CB MET A 358 11.280 -16.125 -19.361 1.00 25.25 C
ANISOU 2650 CB MET A 358 5522 2163 1910 1143 152 -360 C
ATOM 2651 CG MET A 358 12.000 -15.026 -20.136 1.00 35.48 C
ANISOU 2651 CG MET A 358 6762 3504 3215 1184 4 -323 C
ATOM 2652 SD MET A 358 11.745 -15.105 -21.920 1.00 37.63 S
ANISOU 2652 SD MET A 358 7013 3839 3446 1323 -192 -266 S
ATOM 2653 CE MET A 358 10.010 -14.680 -22.044 1.00 44.91 C
ANISOU 2653 CE MET A 358 8128 4703 4231 1448 -217 -176 C
ATOM 2654 N ASN A 359 11.293 -17.584 -15.953 1.00 27.30 N
ANISOU 2654 N ASN A 359 5812 2331 2230 853 585 -523 N
ATOM 2655 CA ASN A 359 10.658 -18.634 -15.171 1.00 28.79 C
ANISOU 2655 CA ASN A 359 6049 2483 2406 803 728 -564 C
ATOM 2656 C ASN A 359 9.289 -18.180 -14.677 1.00 32.92 C
ANISOU 2656 C ASN A 359 6772 2891 2846 864 792 -472 C
ATOM 2657 O ASN A 359 9.084 -17.016 -14.318 1.00 35.10 O
ANISOU 2657 O ASN A 359 7140 3112 3084 888 779 -406 O
ATOM 2658 CB ASN A 359 11.544 -19.028 -13.984 1.00 28.65 C
ANISOU 2658 CB ASN A 359 5950 2491 2444 651 844 -659 C
ATOM 2659 CG ASN A 359 11.107 -20.327 -13.329 1.00 34.13 C
ANISOU 2659 CG ASN A 359 6653 3180 3137 590 978 -721 C
ATOM 2660 OD1 ASN A 359 11.281 -21.408 -13.889 1.00 29.63 O
ANISOU 2660 OD1 ASN A 359 5984 2686 2587 592 961 -787 O
ATOM 2661 ND2 ASN A 359 10.546 -20.225 -12.131 1.00 30.72 N
ANISOU 2661 ND2 ASN A 359 6338 2655 2677 532 1116 -701 N
ATOM 2662 N LYS A 360 8.340 -19.113 -14.677 1.00 35.38 N
ANISOU 2662 N LYS A 360 7151 3169 3123 893 861 -469 N
ATOM 2663 CA LYS A 360 6.974 -18.845 -14.239 1.00 42.32 C
ANISOU 2663 CA LYS A 360 8227 3938 3916 955 931 -383 C
ATOM 2664 C LYS A 360 6.927 -18.904 -12.718 1.00 53.95 C
ANISOU 2664 C LYS A 360 9765 5337 5397 839 1103 -407 C
ATOM 2665 O LYS A 360 7.120 -19.972 -12.125 1.00 64.85 O
ANISOU 2665 O LYS A 360 11092 6731 6818 742 1216 -486 O
ATOM 2666 CB LYS A 360 6.000 -19.848 -14.847 1.00 46.62 C
ANISOU 2666 CB LYS A 360 8818 4473 4421 1032 940 -370 C
ATOM 2667 CG LYS A 360 5.284 -19.349 -16.078 1.00 55.62 C
ANISOU 2667 CG LYS A 360 10026 5619 5488 1191 793 -278 C
ATOM 2668 CD LYS A 360 5.772 -20.045 -17.327 1.00 63.33 C
ANISOU 2668 CD LYS A 360 10865 6694 6502 1231 677 -318 C
ATOM 2669 CE LYS A 360 4.824 -19.768 -18.475 1.00 62.82 C
ANISOU 2669 CE LYS A 360 10893 6628 6349 1390 550 -225 C
ATOM 2670 NZ LYS A 360 5.169 -20.584 -19.664 1.00 62.76 N
ANISOU 2670 NZ LYS A 360 10769 6707 6371 1432 450 -258 N
ATOM 2671 N GLY A 361 6.658 -17.761 -12.092 1.00 42.76 N
ANISOU 2671 N GLY A 361 8465 3847 3937 848 1123 -338 N
ATOM 2672 CA GLY A 361 6.659 -17.671 -10.647 1.00 44.53 C
ANISOU 2672 CA GLY A 361 8760 3994 4167 737 1280 -350 C
ATOM 2673 C GLY A 361 7.725 -16.728 -10.123 1.00 43.21 C
ANISOU 2673 C GLY A 361 8528 3849 4040 664 1259 -370 C
ATOM 2674 O GLY A 361 8.288 -15.930 -10.880 1.00 44.76 O
ANISOU 2674 O GLY A 361 8656 4105 4247 718 1120 -354 O
ATOM 2675 N SER A 362 7.995 -16.798 -8.823 1.00 37.99 N
ANISOU 2675 N SER A 362 7894 3139 3402 539 1400 -401 N
ATOM 2676 CA SER A 362 9.124 -16.110 -8.214 1.00 38.87 C
ANISOU 2676 CA SER A 362 7928 3279 3561 447 1398 -436 C
ATOM 2677 C SER A 362 9.887 -17.107 -7.358 1.00 44.03 C
ANISOU 2677 C SER A 362 8484 3964 4282 290 1514 -537 C
ATOM 2678 O SER A 362 9.310 -17.734 -6.464 1.00 53.81 O
ANISOU 2678 O SER A 362 9809 5128 5507 222 1664 -544 O
ATOM 2679 CB SER A 362 8.681 -14.915 -7.362 1.00 52.17 C
ANISOU 2679 CB SER A 362 9768 4864 5191 456 1450 -358 C
ATOM 2680 OG SER A 362 7.925 -15.333 -6.239 1.00 70.06 O
ANISOU 2680 OG SER A 362 12171 7022 7427 393 1622 -341 O
ATOM 2681 N ILE A 363 11.173 -17.263 -7.644 1.00 39.40 N
ANISOU 2681 N ILE A 363 7719 3489 3762 233 1445 -615 N
ATOM 2682 CA ILE A 363 12.047 -18.116 -6.858 1.00 42.66 C
ANISOU 2682 CA ILE A 363 8026 3952 4232 84 1536 -713 C
ATOM 2683 C ILE A 363 13.042 -17.229 -6.125 1.00 43.77 C
ANISOU 2683 C ILE A 363 8131 4099 4402 0 1542 -723 C
ATOM 2684 O ILE A 363 13.322 -16.095 -6.522 1.00 43.62 O
ANISOU 2684 O ILE A 363 8112 4085 4375 63 1442 -677 O
ATOM 2685 CB ILE A 363 12.773 -19.160 -7.729 1.00 43.39 C
ANISOU 2685 CB ILE A 363 7939 4179 4369 84 1457 -802 C
ATOM 2686 CG1 ILE A 363 13.423 -18.478 -8.934 1.00 45.47 C
ANISOU 2686 CG1 ILE A 363 8104 4523 4649 176 1278 -791 C
ATOM 2687 CG2 ILE A 363 11.812 -20.254 -8.171 1.00 38.59 C
ANISOU 2687 CG2 ILE A 363 7365 3563 3735 136 1491 -809 C
ATOM 2688 CD1 ILE A 363 14.040 -19.432 -9.931 1.00 43.02 C
ANISOU 2688 CD1 ILE A 363 7631 4340 4373 198 1188 -867 C
ATOM 2689 N SER A 364 13.562 -17.748 -5.022 1.00 40.78 N
ANISOU 2689 N SER A 364 7723 3716 4056 -148 1665 -782 N
ATOM 2690 CA SER A 364 14.654 -17.107 -4.310 1.00 46.50 C
ANISOU 2690 CA SER A 364 8389 4463 4815 -245 1676 -807 C
ATOM 2691 C SER A 364 15.960 -17.792 -4.682 1.00 44.89 C
ANISOU 2691 C SER A 364 7987 4400 4668 -305 1612 -902 C
ATOM 2692 O SER A 364 16.010 -19.013 -4.853 1.00 42.03 O
ANISOU 2692 O SER A 364 7552 4097 4322 -338 1638 -966 O
ATOM 2693 CB SER A 364 14.441 -17.168 -2.797 1.00 54.58 C
ANISOU 2693 CB SER A 364 9513 5389 5837 -380 1856 -807 C
ATOM 2694 OG SER A 364 14.414 -18.510 -2.342 1.00 62.07 O
ANISOU 2694 OG SER A 364 10419 6354 6811 -482 1963 -879 O
ATOM 2695 N PHE A 365 17.017 -16.996 -4.822 1.00 41.82 N
ANISOU 2695 N PHE A 365 7515 4069 4306 -314 1528 -909 N
ATOM 2696 CA PHE A 365 18.321 -17.557 -5.144 1.00 33.06 C
ANISOU 2696 CA PHE A 365 6227 3092 3244 -367 1465 -991 C
ATOM 2697 C PHE A 365 18.810 -18.466 -4.024 1.00 35.26 C
ANISOU 2697 C PHE A 365 6461 3385 3549 -534 1599 -1062 C
ATOM 2698 O PHE A 365 18.662 -18.158 -2.838 1.00 40.19 O
ANISOU 2698 O PHE A 365 7169 3926 4174 -634 1724 -1048 O
ATOM 2699 CB PHE A 365 19.338 -16.442 -5.401 1.00 36.97 C
ANISOU 2699 CB PHE A 365 6657 3631 3759 -350 1362 -978 C
ATOM 2700 CG PHE A 365 20.733 -16.937 -5.675 1.00 39.10 C
ANISOU 2700 CG PHE A 365 6754 4030 4071 -405 1301 -1053 C
ATOM 2701 CD1 PHE A 365 21.097 -17.374 -6.938 1.00 45.26 C
ANISOU 2701 CD1 PHE A 365 7428 4909 4860 -316 1170 -1081 C
ATOM 2702 CD2 PHE A 365 21.684 -16.956 -4.666 1.00 32.99 C
ANISOU 2702 CD2 PHE A 365 5930 3279 3325 -546 1375 -1094 C
ATOM 2703 CE1 PHE A 365 22.380 -17.828 -7.189 1.00 41.34 C
ANISOU 2703 CE1 PHE A 365 6785 4528 4394 -359 1114 -1143 C
ATOM 2704 CE2 PHE A 365 22.963 -17.409 -4.910 1.00 33.43 C
ANISOU 2704 CE2 PHE A 365 5835 3453 3414 -595 1320 -1156 C
ATOM 2705 CZ PHE A 365 23.311 -17.844 -6.173 1.00 37.40 C
ANISOU 2705 CZ PHE A 365 6241 4050 3919 -498 1189 -1177 C
ATOM 2706 N LYS A 366 19.377 -19.604 -4.414 1.00 40.39 N
ANISOU 2706 N LYS A 366 6981 4143 4222 -564 1574 -1138 N
ATOM 2707 CA LYS A 366 20.062 -20.502 -3.499 1.00 42.39 C
ANISOU 2707 CA LYS A 366 7156 4441 4509 -726 1678 -1217 C
ATOM 2708 C LYS A 366 21.493 -20.663 -3.980 1.00 39.87 C
ANISOU 2708 C LYS A 366 6669 4260 4220 -746 1575 -1271 C
ATOM 2709 O LYS A 366 21.744 -20.715 -5.188 1.00 42.03 O
ANISOU 2709 O LYS A 366 6874 4609 4487 -629 1437 -1270 O
ATOM 2710 CB LYS A 366 19.382 -21.873 -3.421 1.00 53.19 C
ANISOU 2710 CB LYS A 366 8525 5815 5871 -755 1761 -1264 C
ATOM 2711 CG LYS A 366 17.968 -21.851 -2.877 1.00 58.08 C
ANISOU 2711 CG LYS A 366 9315 6294 6460 -747 1881 -1214 C
ATOM 2712 CD LYS A 366 17.455 -23.262 -2.661 1.00 62.08 C
ANISOU 2712 CD LYS A 366 9807 6813 6968 -802 1979 -1273 C
ATOM 2713 CE LYS A 366 15.983 -23.269 -2.302 1.00 67.94 C
ANISOU 2713 CE LYS A 366 10725 7416 7674 -770 2087 -1216 C
ATOM 2714 NZ LYS A 366 15.711 -22.546 -1.033 1.00 70.29 N
ANISOU 2714 NZ LYS A 366 11152 7582 7973 -868 2217 -1176 N
ATOM 2715 N LYS A 367 22.425 -20.742 -3.031 1.00 40.21 N
ANISOU 2715 N LYS A 367 6649 4333 4298 -896 1645 -1317 N
ATOM 2716 CA LYS A 367 23.837 -20.861 -3.369 1.00 41.23 C
ANISOU 2716 CA LYS A 367 6623 4589 4454 -928 1559 -1363 C
ATOM 2717 C LYS A 367 24.086 -22.118 -4.191 1.00 42.13 C
ANISOU 2717 C LYS A 367 6625 4816 4567 -895 1501 -1422 C
ATOM 2718 O LYS A 367 23.494 -23.169 -3.942 1.00 49.12 O
ANISOU 2718 O LYS A 367 7515 5699 5449 -935 1582 -1462 O
ATOM 2719 CB LYS A 367 24.686 -20.889 -2.095 1.00 41.64 C
ANISOU 2719 CB LYS A 367 6627 4653 4542 -1111 1666 -1410 C
ATOM 2720 CG LYS A 367 24.395 -19.755 -1.124 1.00 49.32 C
ANISOU 2720 CG LYS A 367 7719 5508 5512 -1158 1747 -1357 C
ATOM 2721 CD LYS A 367 25.368 -19.758 0.049 1.00 55.90 C
ANISOU 2721 CD LYS A 367 8490 6369 6383 -1335 1837 -1408 C
ATOM 2722 CE LYS A 367 25.006 -18.701 1.083 1.00 57.85 C
ANISOU 2722 CE LYS A 367 8867 6492 6622 -1383 1930 -1358 C
ATOM 2723 NZ LYS A 367 25.055 -17.321 0.529 1.00 61.45 N
ANISOU 2723 NZ LYS A 367 9376 6918 7055 -1258 1826 -1280 N
ATOM 2724 N VAL A 368 24.964 -22.002 -5.182 1.00 36.13 N
ANISOU 2724 N VAL A 368 5766 4152 3809 -818 1360 -1425 N
ATOM 2725 CA VAL A 368 25.354 -23.128 -6.016 1.00 33.71 C
ANISOU 2725 CA VAL A 368 5350 3960 3498 -779 1292 -1477 C
ATOM 2726 C VAL A 368 26.862 -23.321 -5.888 1.00 38.93 C
ANISOU 2726 C VAL A 368 5869 4734 4190 -870 1259 -1524 C
ATOM 2727 O VAL A 368 27.570 -22.493 -5.314 1.00 39.74 O
ANISOU 2727 O VAL A 368 5960 4826 4313 -938 1272 -1512 O
ATOM 2728 CB VAL A 368 24.937 -22.943 -7.489 1.00 34.76 C
ANISOU 2728 CB VAL A 368 5503 4105 3601 -586 1146 -1435 C
ATOM 2729 CG1 VAL A 368 23.425 -22.851 -7.599 1.00 33.45 C
ANISOU 2729 CG1 VAL A 368 5465 3840 3406 -505 1184 -1394 C
ATOM 2730 CG2 VAL A 368 25.588 -21.706 -8.083 1.00 31.65 C
ANISOU 2730 CG2 VAL A 368 5101 3713 3213 -512 1027 -1386 C
ATOM 2731 N ALA A 369 27.346 -24.446 -6.417 1.00 36.89 N
ANISOU 2731 N ALA A 369 5500 4587 3931 -869 1220 -1580 N
ATOM 2732 CA ALA A 369 28.771 -24.788 -6.403 1.00 37.11 C
ANISOU 2732 CA ALA A 369 5380 4737 3985 -948 1183 -1628 C
ATOM 2733 C ALA A 369 29.145 -25.224 -7.819 1.00 38.38 C
ANISOU 2733 C ALA A 369 5480 4979 4124 -817 1041 -1622 C
ATOM 2734 O ALA A 369 29.131 -26.415 -8.141 1.00 44.77 O
ANISOU 2734 O ALA A 369 6220 5865 4926 -819 1041 -1672 O
ATOM 2735 CB ALA A 369 29.073 -25.869 -5.366 1.00 39.04 C
ANISOU 2735 CB ALA A 369 5533 5043 4257 -1122 1304 -1718 C
ATOM 2736 N LEU A 370 29.471 -24.252 -8.670 1.00 40.14 N
ANISOU 2736 N LEU A 370 5731 5183 4338 -704 922 -1560 N
ATOM 2737 CA LEU A 370 29.761 -24.489 -10.084 1.00 34.05 C
ANISOU 2737 CA LEU A 370 4930 4462 3544 -568 783 -1540 C
ATOM 2738 C LEU A 370 31.155 -23.957 -10.384 1.00 33.49 C
ANISOU 2738 C LEU A 370 4776 4455 3494 -587 705 -1529 C
ATOM 2739 O LEU A 370 31.314 -22.828 -10.869 1.00 30.38 O
ANISOU 2739 O LEU A 370 4435 4010 3099 -508 628 -1470 O
ATOM 2740 CB LEU A 370 28.708 -23.835 -10.978 1.00 36.98 C
ANISOU 2740 CB LEU A 370 5425 4742 3884 -397 706 -1475 C
ATOM 2741 CG LEU A 370 27.261 -24.240 -10.677 1.00 39.40 C
ANISOU 2741 CG LEU A 370 5820 4982 4169 -370 785 -1479 C
ATOM 2742 CD1 LEU A 370 26.275 -23.412 -11.481 1.00 37.47 C
ANISOU 2742 CD1 LEU A 370 5675 4658 3901 -211 705 -1421 C
ATOM 2743 CD2 LEU A 370 27.057 -25.719 -10.946 1.00 35.28 C
ANISOU 2743 CD2 LEU A 370 5247 4529 3629 -372 808 -1532 C
ATOM 2744 N PRO A 371 32.196 -24.756 -10.127 1.00 32.77 N
ANISOU 2744 N PRO A 371 4546 4481 3422 -687 722 -1589 N
ATOM 2745 CA PRO A 371 33.566 -24.228 -10.224 1.00 27.10 C
ANISOU 2745 CA PRO A 371 3742 3828 2725 -721 667 -1582 C
ATOM 2746 C PRO A 371 33.992 -23.843 -11.632 1.00 29.00 C
ANISOU 2746 C PRO A 371 3992 4074 2952 -586 524 -1527 C
ATOM 2747 O PRO A 371 34.959 -23.085 -11.775 1.00 29.29 O
ANISOU 2747 O PRO A 371 3995 4130 3004 -591 476 -1501 O
ATOM 2748 CB PRO A 371 34.425 -25.377 -9.679 1.00 27.76 C
ANISOU 2748 CB PRO A 371 3670 4049 2828 -846 718 -1667 C
ATOM 2749 CG PRO A 371 33.605 -26.602 -9.910 1.00 31.71 C
ANISOU 2749 CG PRO A 371 4166 4571 3312 -825 743 -1708 C
ATOM 2750 CD PRO A 371 32.173 -26.177 -9.738 1.00 28.39 C
ANISOU 2750 CD PRO A 371 3900 4014 2872 -771 790 -1668 C
ATOM 2751 N SER A 372 33.322 -24.337 -12.668 1.00 34.88 N
ANISOU 2751 N SER A 372 4785 4800 3670 -469 459 -1508 N
ATOM 2752 CA SER A 372 33.659 -23.978 -14.039 1.00 29.09 C
ANISOU 2752 CA SER A 372 4074 4055 2924 -349 329 -1451 C
ATOM 2753 C SER A 372 32.785 -22.861 -14.590 1.00 31.80 C
ANISOU 2753 C SER A 372 4570 4264 3247 -228 275 -1377 C
ATOM 2754 O SER A 372 32.946 -22.487 -15.756 1.00 33.77 O
ANISOU 2754 O SER A 372 4863 4482 3486 -137 176 -1324 O
ATOM 2755 CB SER A 372 33.554 -25.208 -14.945 1.00 26.99 C
ANISOU 2755 CB SER A 372 3763 3851 2640 -298 285 -1472 C
ATOM 2756 OG SER A 372 34.380 -26.257 -14.471 1.00 35.18 O
ANISOU 2756 OG SER A 372 4644 5026 3695 -399 324 -1547 O
ATOM 2757 N LEU A 373 31.889 -22.304 -13.779 1.00 30.09 N
ANISOU 2757 N LEU A 373 4433 3973 3029 -234 342 -1374 N
ATOM 2758 CA LEU A 373 30.898 -21.349 -14.260 1.00 21.74 C
ANISOU 2758 CA LEU A 373 3500 2808 1953 -104 288 -1320 C
ATOM 2759 C LEU A 373 31.561 -20.040 -14.685 1.00 22.65 C
ANISOU 2759 C LEU A 373 3632 2890 2083 -64 206 -1269 C
ATOM 2760 O LEU A 373 32.257 -19.399 -13.890 1.00 21.13 O
ANISOU 2760 O LEU A 373 3397 2713 1920 -155 250 -1275 O
ATOM 2761 CB LEU A 373 29.862 -21.088 -13.173 1.00 23.51 C
ANISOU 2761 CB LEU A 373 3773 2979 2182 -144 393 -1337 C
ATOM 2762 CG LEU A 373 28.667 -20.232 -13.594 1.00 26.42 C
ANISOU 2762 CG LEU A 373 4225 3270 2544 -18 347 -1304 C
ATOM 2763 CD1 LEU A 373 27.788 -20.994 -14.568 1.00 22.13 C
ANISOU 2763 CD1 LEU A 373 3698 2737 1972 107 287 -1315 C
ATOM 2764 CD2 LEU A 373 27.863 -19.759 -12.388 1.00 29.92 C
ANISOU 2764 CD2 LEU A 373 4724 3645 2998 -100 472 -1301 C
ATOM 2765 N SER A 374 31.320 -19.635 -15.937 1.00 25.70 N
ANISOU 2765 N SER A 374 4097 3219 2447 65 96 -1215 N
ATOM 2766 CA SER A 374 31.803 -18.366 -16.459 1.00 21.37 C
ANISOU 2766 CA SER A 374 3560 2630 1931 96 26 -1137 C
ATOM 2767 C SER A 374 30.702 -17.487 -17.033 1.00 20.93 C
ANISOU 2767 C SER A 374 3441 2572 1940 237 -57 -1112 C
ATOM 2768 O SER A 374 30.958 -16.309 -17.308 1.00 22.64 O
ANISOU 2768 O SER A 374 3383 2925 2296 82 23 -1205 O
ATOM 2769 CB SER A 374 32.865 -18.602 -17.546 1.00 18.81 C
ANISOU 2769 CB SER A 374 3230 2316 1600 27 0 -1092 C
ATOM 2770 OG SER A 374 32.256 -18.955 -18.773 1.00 26.96 O
ANISOU 2770 OG SER A 374 4268 3335 2639 -16 32 -1057 O
ATOM 2771 N TYR A 375 29.498 -18.024 -17.236 1.00 21.19 N
ANISOU 2771 N TYR A 375 3268 2730 2055 175 27 -1236 N
ATOM 2772 CA TYR A 375 28.377 -17.276 -17.792 1.00 19.10 C
ANISOU 2772 CA TYR A 375 3108 2354 1793 65 150 -1201 C
ATOM 2773 C TYR A 375 27.123 -17.593 -16.988 1.00 25.02 C
ANISOU 2773 C TYR A 375 3928 3066 2512 138 173 -1237 C
ATOM 2774 O TYR A 375 26.771 -18.765 -16.815 1.00 27.14 O
ANISOU 2774 O TYR A 375 4179 3376 2758 166 179 -1275 O
ATOM 2775 CB TYR A 375 28.173 -17.622 -19.275 1.00 18.59 C
ANISOU 2775 CB TYR A 375 3137 2234 1694 102 109 -1134 C
ATOM 2776 CG TYR A 375 27.011 -16.912 -19.936 1.00 24.38 C
ANISOU 2776 CG TYR A 375 3966 2871 2429 251 24 -1027 C
ATOM 2777 CD1 TYR A 375 25.725 -17.431 -19.861 1.00 29.49 C
ANISOU 2777 CD1 TYR A 375 4675 3478 3053 304 49 -1023 C
ATOM 2778 CD2 TYR A 375 27.201 -15.739 -20.656 1.00 21.93 C
ANISOU 2778 CD2 TYR A 375 3685 2511 2134 337 -82 -928 C
ATOM 2779 CE1 TYR A 375 24.658 -16.798 -20.464 1.00 18.81 C
ANISOU 2779 CE1 TYR A 375 3425 2038 1684 431 -27 -918 C
ATOM 2780 CE2 TYR A 375 26.137 -15.096 -21.266 1.00 19.84 C
ANISOU 2780 CE2 TYR A 375 3509 2170 1859 466 -164 -833 C
ATOM 2781 CZ TYR A 375 24.869 -15.629 -21.168 1.00 22.70 C
ANISOU 2781 CZ TYR A 375 3944 2493 2188 511 -136 -825 C
ATOM 2782 OH TYR A 375 23.813 -14.985 -21.779 1.00 31.45 O
ANISOU 2782 OH TYR A 375 5148 3533 3270 637 -220 -727 O
ATOM 2783 N LEU A 376 26.442 -16.554 -16.505 1.00 19.99 N
ANISOU 2783 N LEU A 376 3407 2327 1862 160 197 -1189 N
ATOM 2784 CA LEU A 376 25.268 -16.733 -15.657 1.00 20.82 C
ANISOU 2784 CA LEU A 376 3627 2355 1929 177 267 -1169 C
ATOM 2785 C LEU A 376 24.207 -15.716 -16.050 1.00 26.93 C
ANISOU 2785 C LEU A 376 4530 3009 2693 233 260 -1059 C
ATOM 2786 O LEU A 376 24.417 -14.508 -15.906 1.00 27.87 O
ANISOU 2786 O LEU A 376 4688 3084 2819 237 239 -1006 O
ATOM 2787 CB LEU A 376 25.633 -16.585 -14.178 1.00 21.42 C
ANISOU 2787 CB LEU A 376 3747 2409 1981 118 335 -1180 C
ATOM 2788 CG LEU A 376 24.524 -16.824 -13.151 1.00 26.34 C
ANISOU 2788 CG LEU A 376 4495 2944 2569 84 454 -1157 C
ATOM 2789 CD1 LEU A 376 23.869 -18.182 -13.379 1.00 22.94 C
ANISOU 2789 CD1 LEU A 376 4058 2542 2116 106 481 -1196 C
ATOM 2790 CD2 LEU A 376 25.076 -16.709 -11.734 1.00 22.96 C
ANISOU 2790 CD2 LEU A 376 4098 2494 2132 -28 553 -1164 C
ATOM 2791 N ASP A 377 23.071 -16.209 -16.541 1.00 27.09 N
ANISOU 2791 N ASP A 377 4623 2982 2686 294 263 -1020 N
ATOM 2792 CA ASP A 377 21.930 -15.383 -16.921 1.00 28.93 C
ANISOU 2792 CA ASP A 377 4997 3110 2887 387 231 -908 C
ATOM 2793 C ASP A 377 20.748 -15.825 -16.071 1.00 30.45 C
ANISOU 2793 C ASP A 377 5295 3239 3037 387 328 -906 C
ATOM 2794 O ASP A 377 20.171 -16.891 -16.311 1.00 27.42 O
ANISOU 2794 O ASP A 377 4913 2868 2637 406 351 -931 O
ATOM 2795 CB ASP A 377 21.622 -15.516 -18.413 1.00 26.59 C
ANISOU 2795 CB ASP A 377 4709 2811 2583 491 119 -839 C
ATOM 2796 CG ASP A 377 20.412 -14.688 -18.850 1.00 32.05 C
ANISOU 2796 CG ASP A 377 5539 3413 3224 610 58 -724 C
ATOM 2797 OD1 ASP A 377 19.757 -14.047 -18.003 1.00 28.60 O
ANISOU 2797 OD1 ASP A 377 5201 2911 2757 606 117 -697 O
ATOM 2798 OD2 ASP A 377 20.112 -14.671 -20.061 1.00 33.24 O
ANISOU 2798 OD2 ASP A 377 5704 3566 3361 714 -56 -659 O
ATOM 2799 N LEU A 378 20.390 -15.009 -15.082 1.00 33.55 N
ANISOU 2799 N LEU A 378 5782 3559 3407 365 388 -872 N
ATOM 2800 CA LEU A 378 19.251 -15.273 -14.211 1.00 23.48 C
ANISOU 2800 CA LEU A 378 4632 2204 2086 361 492 -851 C
ATOM 2801 C LEU A 378 18.161 -14.217 -14.373 1.00 26.28 C
ANISOU 2801 C LEU A 378 5139 2458 2390 453 467 -740 C
ATOM 2802 O LEU A 378 17.411 -13.937 -13.434 1.00 29.14 O
ANISOU 2802 O LEU A 378 5620 2739 2712 438 556 -708 O
ATOM 2803 CB LEU A 378 19.703 -15.358 -12.755 1.00 24.10 C
ANISOU 2803 CB LEU A 378 4711 2276 2168 247 606 -901 C
ATOM 2804 CG LEU A 378 20.674 -16.498 -12.440 1.00 26.41 C
ANISOU 2804 CG LEU A 378 4875 2670 2490 164 635 -1004 C
ATOM 2805 CD1 LEU A 378 21.117 -16.447 -10.987 1.00 25.53 C
ANISOU 2805 CD1 LEU A 378 4787 2536 2376 48 747 -1028 C
ATOM 2806 CD2 LEU A 378 20.040 -17.843 -12.775 1.00 24.66 C
ANISOU 2806 CD2 LEU A 378 4642 2476 2252 186 660 -1042 C
ATOM 2807 N SER A 379 18.043 -13.650 -15.568 1.00 22.95 N
ANISOU 2807 N SER A 379 4719 2041 1960 552 341 -676 N
ATOM 2808 CA SER A 379 17.165 -12.511 -15.770 1.00 26.74 C
ANISOU 2808 CA SER A 379 5328 2449 2383 647 291 -574 C
ATOM 2809 C SER A 379 15.707 -12.944 -15.912 1.00 31.58 C
ANISOU 2809 C SER A 379 6071 3001 2928 728 313 -520 C
ATOM 2810 O SER A 379 15.404 -14.089 -16.262 1.00 31.70 O
ANISOU 2810 O SER A 379 6062 3037 2945 735 330 -550 O
ATOM 2811 CB SER A 379 17.592 -11.730 -17.014 1.00 23.59 C
ANISOU 2811 CB SER A 379 4882 2089 1993 728 136 -525 C
ATOM 2812 OG SER A 379 17.449 -12.506 -18.192 1.00 32.57 O
ANISOU 2812 OG SER A 379 5978 3266 3131 794 53 -516 O
ATOM 2813 N ARG A 380 14.805 -12.008 -15.599 1.00 32.53 N
ANISOU 2813 N ARG A 380 6332 3048 2981 789 314 -443 N
ATOM 2814 CA AARG A 380 13.370 -12.163 -15.844 0.50 29.83 C
ANISOU 2814 CA AARG A 380 6130 2649 2557 888 313 -374 C
ATOM 2815 CA BARG A 380 13.372 -12.169 -15.854 0.50 29.82 C
ANISOU 2815 CA BARG A 380 6128 2648 2555 888 313 -375 C
ATOM 2816 C ARG A 380 12.778 -13.330 -15.058 1.00 30.47 C
ANISOU 2816 C ARG A 380 6258 2688 2631 833 456 -412 C
ATOM 2817 O ARG A 380 11.986 -14.113 -15.579 1.00 29.07 O
ANISOU 2817 O ARG A 380 6120 2504 2421 892 450 -396 O
ATOM 2818 CB AARG A 380 13.089 -12.311 -17.340 0.50 27.87 C
ANISOU 2818 CB AARG A 380 5858 2446 2284 1002 166 -333 C
ATOM 2819 CB BARG A 380 13.098 -12.345 -17.348 0.50 27.83 C
ANISOU 2819 CB BARG A 380 5851 2442 2280 1001 167 -335 C
ATOM 2820 CG AARG A 380 13.652 -11.170 -18.163 0.50 28.33 C
ANISOU 2820 CG AARG A 380 5870 2549 2345 1057 19 -296 C
ATOM 2821 CG BARG A 380 13.579 -11.189 -18.201 0.50 28.19 C
ANISOU 2821 CG BARG A 380 5859 2531 2323 1064 17 -293 C
ATOM 2822 CD AARG A 380 13.709 -11.506 -19.638 0.50 27.79 C
ANISOU 2822 CD AARG A 380 5742 2544 2274 1142 -125 -275 C
ATOM 2823 CD BARG A 380 13.748 -11.606 -19.649 0.50 27.94 C
ANISOU 2823 CD BARG A 380 5753 2565 2297 1138 -121 -280 C
ATOM 2824 NE AARG A 380 14.400 -10.462 -20.389 0.50 25.04 N
ANISOU 2824 NE AARG A 380 5332 2243 1938 1179 -260 -250 N
ATOM 2825 NE BARG A 380 14.193 -10.494 -20.485 0.50 26.31 N
ANISOU 2825 NE BARG A 380 5511 2403 2085 1197 -269 -241 N
ATOM 2826 CZ AARG A 380 13.801 -9.391 -20.899 0.50 26.06 C
ANISOU 2826 CZ AARG A 380 5535 2375 1993 1275 -369 -186 C
ATOM 2827 CZ BARG A 380 15.463 -10.131 -20.636 0.50 21.36 C
ANISOU 2827 CZ BARG A 380 4763 1820 1531 1141 -304 -274 C
ATOM 2828 NH1AARG A 380 12.494 -9.219 -20.744 0.50 28.16 N
ANISOU 2828 NH1AARG A 380 5942 2596 2160 1349 -360 -138 N
ATOM 2829 NH1BARG A 380 16.421 -10.792 -20.004 0.50 21.20 N
ANISOU 2829 NH1BARG A 380 4649 1814 1591 1025 -205 -349 N
ATOM 2830 NH2AARG A 380 14.504 -8.488 -21.568 0.50 21.41 N
ANISOU 2830 NH2AARG A 380 4871 1836 1426 1294 -486 -178 N
ATOM 2831 NH2BARG A 380 15.772 -9.104 -21.417 0.50 20.77 N
ANISOU 2831 NH2BARG A 380 4664 1783 1447 1199 -439 -236 N
ATOM 2832 N ASN A 381 13.149 -13.441 -13.785 1.00 26.43 N
ANISOU 2832 N ASN A 381 5746 2149 2146 718 585 -461 N
ATOM 2833 CA ASN A 381 12.629 -14.505 -12.935 1.00 27.42 C
ANISOU 2833 CA ASN A 381 5919 2235 2266 654 729 -498 C
ATOM 2834 C ASN A 381 11.845 -13.974 -11.742 1.00 33.58 C
ANISOU 2834 C ASN A 381 6860 2908 2991 634 846 -448 C
ATOM 2835 O ASN A 381 11.402 -14.768 -10.904 1.00 35.63 O
ANISOU 2835 O ASN A 381 7174 3120 3244 570 980 -472 O
ATOM 2836 CB ASN A 381 13.769 -15.407 -12.450 1.00 27.26 C
ANISOU 2836 CB ASN A 381 5749 2288 2321 524 789 -611 C
ATOM 2837 CG ASN A 381 14.438 -16.159 -13.584 1.00 28.11 C
ANISOU 2837 CG ASN A 381 5706 2500 2474 544 691 -666 C
ATOM 2838 OD1 ASN A 381 13.770 -16.707 -14.461 1.00 29.63 O
ANISOU 2838 OD1 ASN A 381 5918 2698 2644 627 644 -643 O
ATOM 2839 ND2 ASN A 381 15.768 -16.179 -13.578 1.00 25.75 N
ANISOU 2839 ND2 ASN A 381 5262 2285 2236 472 661 -737 N
ATOM 2840 N ALA A 382 11.645 -12.656 -11.650 1.00 31.71 N
ANISOU 2840 N ALA A 382 6705 2632 2712 687 800 -379 N
ATOM 2841 CA ALA A 382 11.190 -12.015 -10.412 1.00 38.30 C
ANISOU 2841 CA ALA A 382 7675 3373 3503 651 910 -342 C
ATOM 2842 C ALA A 382 11.997 -12.522 -9.218 1.00 38.37 C
ANISOU 2842 C ALA A 382 7625 3381 3573 494 1041 -419 C
ATOM 2843 O ALA A 382 11.484 -12.645 -8.101 1.00 39.97 O
ANISOU 2843 O ALA A 382 7940 3500 3748 436 1179 -405 O
ATOM 2844 CB ALA A 382 9.692 -12.227 -10.187 1.00 40.11 C
ANISOU 2844 CB ALA A 382 8086 3509 3645 722 978 -271 C
ATOM 2845 N LEU A 383 13.275 -12.808 -9.467 1.00 30.89 N
ANISOU 2845 N LEU A 383 6505 2529 2702 425 996 -497 N
ATOM 2846 CA LEU A 383 14.164 -13.449 -8.510 1.00 28.94 C
ANISOU 2846 CA LEU A 383 6176 2309 2510 278 1098 -581 C
ATOM 2847 C LEU A 383 14.451 -12.519 -7.335 1.00 33.68 C
ANISOU 2847 C LEU A 383 6841 2853 3105 207 1174 -562 C
ATOM 2848 O LEU A 383 14.560 -11.300 -7.489 1.00 28.89 O
ANISOU 2848 O LEU A 383 6263 2235 2479 262 1104 -514 O
ATOM 2849 CB LEU A 383 15.465 -13.833 -9.225 1.00 39.21 C
ANISOU 2849 CB LEU A 383 7281 3736 3881 248 1003 -659 C
ATOM 2850 CG LEU A 383 16.558 -14.802 -8.746 1.00 43.07 C
ANISOU 2850 CG LEU A 383 7633 4306 4428 122 1055 -763 C
ATOM 2851 CD1 LEU A 383 17.601 -14.114 -7.861 1.00 50.18 C
ANISOU 2851 CD1 LEU A 383 8493 5217 5357 24 1087 -785 C
ATOM 2852 CD2 LEU A 383 15.978 -16.021 -8.055 1.00 47.12 C
ANISOU 2852 CD2 LEU A 383 8187 4789 4930 55 1188 -798 C
ATOM 2853 N SER A 384 14.566 -13.108 -6.147 1.00 37.48 N
ANISOU 2853 N SER A 384 7344 3297 3599 83 1319 -601 N
ATOM 2854 CA SER A 384 14.974 -12.383 -4.951 1.00 40.69 C
ANISOU 2854 CA SER A 384 7798 3655 4008 -6 1404 -595 C
ATOM 2855 C SER A 384 16.305 -12.955 -4.493 1.00 43.91 C
ANISOU 2855 C SER A 384 8056 4145 4484 -142 1434 -688 C
ATOM 2856 O SER A 384 16.404 -14.151 -4.195 1.00 41.62 O
ANISOU 2856 O SER A 384 7718 3878 4218 -224 1510 -748 O
ATOM 2857 CB SER A 384 13.928 -12.484 -3.837 1.00 50.87 C
ANISOU 2857 CB SER A 384 9265 4817 5247 -44 1562 -551 C
ATOM 2858 OG SER A 384 13.848 -13.798 -3.320 1.00 55.56 O
ANISOU 2858 OG SER A 384 9838 5405 5866 -145 1678 -609 O
ATOM 2859 N PHE A 385 17.323 -12.101 -4.448 1.00 42.88 N
ANISOU 2859 N PHE A 385 7851 4060 4380 -164 1374 -699 N
ATOM 2860 CA PHE A 385 18.697 -12.491 -4.156 1.00 31.64 C
ANISOU 2860 CA PHE A 385 6278 2728 3016 -276 1377 -779 C
ATOM 2861 C PHE A 385 19.117 -11.802 -2.863 1.00 40.56 C
ANISOU 2861 C PHE A 385 7458 3805 4148 -380 1475 -773 C
ATOM 2862 O PHE A 385 19.274 -10.577 -2.830 1.00 39.63 O
ANISOU 2862 O PHE A 385 7375 3667 4016 -335 1428 -730 O
ATOM 2863 CB PHE A 385 19.611 -12.107 -5.321 1.00 27.82 C
ANISOU 2863 CB PHE A 385 5657 2349 2564 -207 1214 -798 C
ATOM 2864 CG PHE A 385 20.950 -12.799 -5.322 1.00 34.57 C
ANISOU 2864 CG PHE A 385 6349 3314 3472 -298 1197 -881 C
ATOM 2865 CD1 PHE A 385 21.629 -13.054 -4.142 1.00 33.04 C
ANISOU 2865 CD1 PHE A 385 6134 3123 3299 -443 1306 -923 C
ATOM 2866 CD2 PHE A 385 21.538 -13.180 -6.518 1.00 39.75 C
ANISOU 2866 CD2 PHE A 385 6878 4073 4153 -237 1071 -916 C
ATOM 2867 CE1 PHE A 385 22.853 -13.674 -4.152 1.00 29.15 C
ANISOU 2867 CE1 PHE A 385 5496 2734 2846 -523 1287 -994 C
ATOM 2868 CE2 PHE A 385 22.765 -13.804 -6.534 1.00 37.05 C
ANISOU 2868 CE2 PHE A 385 6395 3832 3848 -310 1051 -986 C
ATOM 2869 CZ PHE A 385 23.423 -14.053 -5.348 1.00 31.37 C
ANISOU 2869 CZ PHE A 385 5658 3117 3146 -452 1158 -1023 C
ATOM 2870 N SER A 386 19.319 -12.585 -1.809 1.00 38.09 N
ANISOU 2870 N SER A 386 7143 3475 3853 -520 1610 -820 N
ATOM 2871 CA SER A 386 19.762 -12.063 -0.522 1.00 41.13 C
ANISOU 2871 CA SER A 386 7569 3814 4245 -636 1715 -822 C
ATOM 2872 C SER A 386 21.245 -12.365 -0.348 1.00 37.74 C
ANISOU 2872 C SER A 386 6976 3492 3872 -744 1696 -899 C
ATOM 2873 O SER A 386 21.636 -13.528 -0.201 1.00 48.13 O
ANISOU 2873 O SER A 386 8205 4865 5219 -834 1741 -966 O
ATOM 2874 CB SER A 386 18.949 -12.665 0.618 1.00 41.81 C
ANISOU 2874 CB SER A 386 7776 3796 4314 -731 1891 -820 C
ATOM 2875 OG SER A 386 19.377 -12.133 1.858 1.00 56.34 O
ANISOU 2875 OG SER A 386 9657 5588 6160 -844 1993 -822 O
ATOM 2876 N GLY A 387 22.068 -11.326 -0.358 1.00 36.10 N
ANISOU 2876 N GLY A 387 6728 3315 3674 -733 1632 -888 N
ATOM 2877 CA GLY A 387 23.487 -11.474 -0.147 1.00 40.25 C
ANISOU 2877 CA GLY A 387 7111 3937 4245 -831 1616 -950 C
ATOM 2878 C GLY A 387 24.353 -11.351 -1.380 1.00 38.86 C
ANISOU 2878 C GLY A 387 6799 3874 4092 -751 1456 -968 C
ATOM 2879 O GLY A 387 25.427 -11.960 -1.422 1.00 42.77 O
ANISOU 2879 O GLY A 387 7163 4466 4624 -826 1440 -1029 O
ATOM 2880 N CYS A 388 23.923 -10.589 -2.383 1.00 33.69 N
ANISOU 2880 N CYS A 388 6172 3210 3418 -605 1340 -917 N
ATOM 2881 CA CYS A 388 24.731 -10.373 -3.576 1.00 34.41 C
ANISOU 2881 CA CYS A 388 6142 3398 3533 -528 1190 -931 C
ATOM 2882 C CYS A 388 25.898 -9.441 -3.266 1.00 35.77 C
ANISOU 2882 C CYS A 388 6256 3608 3728 -570 1162 -938 C
ATOM 2883 O CYS A 388 25.735 -8.443 -2.557 1.00 31.83 O
ANISOU 2883 O CYS A 388 5840 3041 3211 -581 1207 -901 O
ATOM 2884 CB CYS A 388 23.860 -9.776 -4.685 1.00 31.01 C
ANISOU 2884 CB CYS A 388 5764 2940 3078 -370 1083 -875 C
ATOM 2885 SG CYS A 388 24.722 -9.398 -6.221 1.00 39.22 S
ANISOU 2885 SG CYS A 388 6668 4084 4151 -270 901 -887 S
ATOM 2886 N CYS A 389 27.093 -9.773 -3.763 1.00 37.14 N
ANISOU 2886 N CYS A 389 6290 3887 3934 -594 1093 -983 N
ATOM 2887 CA CYS A 389 27.442 -11.032 -4.424 1.00 31.09 C
ANISOU 2887 CA CYS A 389 5421 3207 3185 -599 1055 -1034 C
ATOM 2888 C CYS A 389 28.892 -11.349 -4.076 1.00 29.96 C
ANISOU 2888 C CYS A 389 5156 3155 3072 -706 1063 -1086 C
ATOM 2889 O CYS A 389 29.685 -10.425 -3.920 1.00 30.95 O
ANISOU 2889 O CYS A 389 5256 3294 3208 -718 1036 -1074 O
ATOM 2890 CB CYS A 389 27.307 -10.937 -5.946 1.00 34.04 C
ANISOU 2890 CB CYS A 389 5752 3623 3561 -455 906 -1019 C
ATOM 2891 SG CYS A 389 25.654 -11.145 -6.638 1.00 47.11 S
ANISOU 2891 SG CYS A 389 7509 5208 5185 -335 886 -977 S
ATOM 2892 N SER A 390 29.262 -12.627 -3.985 1.00 26.89 N
ANISOU 2892 N SER A 390 4687 2833 2696 -780 1097 -1143 N
ATOM 2893 CA SER A 390 30.655 -12.984 -3.735 1.00 26.51 C
ANISOU 2893 CA SER A 390 4515 2883 2674 -878 1098 -1192 C
ATOM 2894 C SER A 390 30.886 -14.426 -4.170 1.00 31.88 C
ANISOU 2894 C SER A 390 5101 3649 3361 -902 1086 -1247 C
ATOM 2895 O SER A 390 30.009 -15.072 -4.748 1.00 30.18 O
ANISOU 2895 O SER A 390 4917 3419 3131 -831 1066 -1246 O
ATOM 2896 CB SER A 390 31.036 -12.780 -2.265 1.00 25.81 C
ANISOU 2896 CB SER A 390 4441 2769 2596 -1030 1230 -1212 C
ATOM 2897 OG SER A 390 30.635 -13.880 -1.464 1.00 28.97 O
ANISOU 2897 OG SER A 390 4845 3162 3001 -1140 1348 -1258 O
ATOM 2898 N TYR A 391 32.083 -14.931 -3.863 1.00 33.64 N
ANISOU 2898 N TYR A 391 5207 3969 3607 -1003 1101 -1298 N
ATOM 2899 CA TYR A 391 32.487 -16.248 -4.348 1.00 32.42 C
ANISOU 2899 CA TYR A 391 4945 3914 3458 -1021 1075 -1352 C
ATOM 2900 C TYR A 391 31.623 -17.358 -3.763 1.00 37.90 C
ANISOU 2900 C TYR A 391 5665 4586 4150 -1089 1179 -1393 C
ATOM 2901 O TYR A 391 31.314 -18.339 -4.450 1.00 40.28 O
ANISOU 2901 O TYR A 391 5932 4930 4443 -1041 1143 -1417 O
ATOM 2902 CB TYR A 391 33.963 -16.494 -4.026 1.00 31.83 C
ANISOU 2902 CB TYR A 391 4738 3951 3406 -1123 1078 -1398 C
ATOM 2903 CG TYR A 391 34.413 -17.924 -4.252 1.00 31.46 C
ANISOU 2903 CG TYR A 391 4572 4015 3367 -1171 1076 -1465 C
ATOM 2904 CD1 TYR A 391 34.699 -18.392 -5.530 1.00 34.31 C
ANISOU 2904 CD1 TYR A 391 4875 4441 3718 -1066 958 -1461 C
ATOM 2905 CD2 TYR A 391 34.553 -18.807 -3.185 1.00 29.69 C
ANISOU 2905 CD2 TYR A 391 4292 3829 3158 -1322 1194 -1534 C
ATOM 2906 CE1 TYR A 391 35.113 -19.700 -5.738 1.00 36.33 C
ANISOU 2906 CE1 TYR A 391 5022 4804 3979 -1106 955 -1522 C
ATOM 2907 CE2 TYR A 391 34.963 -20.116 -3.385 1.00 36.77 C
ANISOU 2907 CE2 TYR A 391 5071 4836 4062 -1365 1191 -1600 C
ATOM 2908 CZ TYR A 391 35.242 -20.556 -4.662 1.00 40.58 C
ANISOU 2908 CZ TYR A 391 5498 5387 4532 -1254 1070 -1593 C
ATOM 2909 OH TYR A 391 35.651 -21.855 -4.861 1.00 45.47 O
ANISOU 2909 OH TYR A 391 5999 6121 5157 -1293 1066 -1659 O
ATOM 2910 N SER A 392 31.231 -17.228 -2.493 1.00 36.23 N
ANISOU 2910 N SER A 392 5516 4306 3945 -1201 1313 -1402 N
ATOM 2911 CA SER A 392 30.493 -18.295 -1.823 1.00 43.92 C
ANISOU 2911 CA SER A 392 6510 5256 4921 -1287 1428 -1448 C
ATOM 2912 C SER A 392 29.095 -18.501 -2.393 1.00 41.83 C
ANISOU 2912 C SER A 392 6353 4912 4629 -1175 1418 -1411 C
ATOM 2913 O SER A 392 28.518 -19.577 -2.205 1.00 46.64 O
ANISOU 2913 O SER A 392 6961 5523 5238 -1215 1483 -1452 O
ATOM 2914 CB SER A 392 30.409 -18.010 -0.322 1.00 48.44 C
ANISOU 2914 CB SER A 392 7137 5762 5508 -1434 1577 -1462 C
ATOM 2915 OG SER A 392 30.112 -16.645 -0.080 1.00 53.60 O
ANISOU 2915 OG SER A 392 7902 6318 6146 -1385 1576 -1392 O
ATOM 2916 N ASP A 393 28.535 -17.499 -3.075 1.00 38.99 N
ANISOU 2916 N ASP A 393 6082 4486 4245 -1036 1338 -1338 N
ATOM 2917 CA ASP A 393 27.230 -17.678 -3.700 1.00 43.40 C
ANISOU 2917 CA ASP A 393 6735 4980 4776 -919 1317 -1303 C
ATOM 2918 C ASP A 393 27.299 -18.636 -4.881 1.00 41.07 C
ANISOU 2918 C ASP A 393 6359 4773 4474 -833 1220 -1332 C
ATOM 2919 O ASP A 393 26.336 -19.366 -5.146 1.00 39.03 O
ANISOU 2919 O ASP A 393 6143 4490 4197 -789 1242 -1337 O
ATOM 2920 CB ASP A 393 26.672 -16.330 -4.163 1.00 44.44 C
ANISOU 2920 CB ASP A 393 6968 5032 4887 -794 1249 -1224 C
ATOM 2921 CG ASP A 393 26.469 -15.359 -3.019 1.00 41.51 C
ANISOU 2921 CG ASP A 393 6694 4565 4512 -863 1345 -1188 C
ATOM 2922 OD1 ASP A 393 26.061 -15.803 -1.925 1.00 40.30 O
ANISOU 2922 OD1 ASP A 393 6594 4357 4361 -975 1485 -1208 O
ATOM 2923 OD2 ASP A 393 26.718 -14.151 -3.216 1.00 41.57 O
ANISOU 2923 OD2 ASP A 393 6728 4551 4516 -805 1283 -1143 O
ATOM 2924 N LEU A 394 28.427 -18.657 -5.590 1.00 37.87 N
ANISOU 2924 N LEU A 394 5841 4468 4080 -807 1115 -1349 N
ATOM 2925 CA LEU A 394 28.529 -19.340 -6.870 1.00 34.94 C
ANISOU 2925 CA LEU A 394 5408 4171 3698 -698 1000 -1361 C
ATOM 2926 C LEU A 394 29.624 -20.393 -6.934 1.00 33.01 C
ANISOU 2926 C LEU A 394 5023 4052 3470 -775 991 -1427 C
ATOM 2927 O LEU A 394 29.522 -21.305 -7.763 1.00 34.40 O
ANISOU 2927 O LEU A 394 5155 4284 3631 -711 934 -1449 O
ATOM 2928 CB LEU A 394 28.756 -18.318 -7.995 1.00 31.99 C
ANISOU 2928 CB LEU A 394 5043 3794 3318 -556 854 -1308 C
ATOM 2929 CG LEU A 394 27.691 -17.222 -8.074 1.00 35.78 C
ANISOU 2929 CG LEU A 394 5645 4165 3784 -470 845 -1245 C
ATOM 2930 CD1 LEU A 394 28.116 -16.117 -9.030 1.00 28.50 C
ANISOU 2930 CD1 LEU A 394 4708 3252 2870 -361 712 -1205 C
ATOM 2931 CD2 LEU A 394 26.355 -17.827 -8.484 1.00 36.36 C
ANISOU 2931 CD2 LEU A 394 5786 4197 3833 -391 856 -1239 C
ATOM 2932 N GLY A 395 30.654 -20.303 -6.100 1.00 33.99 N
ANISOU 2932 N GLY A 395 5071 4223 3620 -908 1044 -1459 N
ATOM 2933 CA GLY A 395 31.701 -21.311 -6.107 1.00 30.65 C
ANISOU 2933 CA GLY A 395 4502 3928 3213 -988 1039 -1525 C
ATOM 2934 C GLY A 395 32.563 -21.301 -7.348 1.00 31.92 C
ANISOU 2934 C GLY A 395 4588 4171 3369 -890 896 -1511 C
ATOM 2935 O GLY A 395 33.071 -22.351 -7.751 1.00 38.40 O
ANISOU 2935 O GLY A 395 5307 5094 4191 -903 868 -1557 O
ATOM 2936 N THR A 396 32.745 -20.136 -7.969 1.00 29.60 N
ANISOU 2936 N THR A 396 4343 3834 3070 -793 807 -1447 N
ATOM 2937 CA THR A 396 33.555 -20.015 -9.170 1.00 23.54 C
ANISOU 2937 CA THR A 396 3520 3125 2298 -699 674 -1426 C
ATOM 2938 C THR A 396 34.404 -18.757 -9.094 1.00 33.43 C
ANISOU 2938 C THR A 396 4770 4366 3566 -704 638 -1388 C
ATOM 2939 O THR A 396 33.998 -17.744 -8.517 1.00 31.22 O
ANISOU 2939 O THR A 396 4569 4004 3289 -712 678 -1356 O
ATOM 2940 CB THR A 396 32.699 -19.968 -10.446 1.00 22.93 C
ANISOU 2940 CB THR A 396 3520 2998 2193 -530 571 -1383 C
ATOM 2941 OG1 THR A 396 33.546 -19.749 -11.580 1.00 22.08 O
ANISOU 2941 OG1 THR A 396 3371 2933 2085 -450 447 -1356 O
ATOM 2942 CG2 THR A 396 31.668 -18.851 -10.360 1.00 22.73 C
ANISOU 2942 CG2 THR A 396 3618 2857 2160 -456 571 -1331 C
ATOM 2943 N ASN A 397 35.596 -18.836 -9.678 1.00 33.98 N
ANISOU 2943 N ASN A 397 4747 4521 3643 -698 566 -1392 N
ATOM 2944 CA ASN A 397 36.481 -17.693 -9.838 1.00 30.89 C
ANISOU 2944 CA ASN A 397 4348 4126 3263 -685 516 -1353 C
ATOM 2945 C ASN A 397 36.521 -17.190 -11.272 1.00 27.42 C
ANISOU 2945 C ASN A 397 3945 3660 2814 -538 381 -1299 C
ATOM 2946 O ASN A 397 37.289 -16.271 -11.574 1.00 30.84 O
ANISOU 2946 O ASN A 397 4370 4092 3257 -517 329 -1267 O
ATOM 2947 CB ASN A 397 37.903 -18.050 -9.389 1.00 29.28 C
ANISOU 2947 CB ASN A 397 4013 4036 3075 -792 542 -1396 C
ATOM 2948 CG ASN A 397 37.982 -18.420 -7.924 1.00 39.48 C
ANISOU 2948 CG ASN A 397 5267 5354 4380 -946 676 -1451 C
ATOM 2949 OD1 ASN A 397 37.688 -17.605 -7.051 1.00 36.07 O
ANISOU 2949 OD1 ASN A 397 4900 4851 3953 -996 745 -1436 O
ATOM 2950 ND2 ASN A 397 38.413 -19.643 -7.642 1.00 40.65 N
ANISOU 2950 ND2 ASN A 397 5308 5606 4532 -1024 714 -1518 N
ATOM 2951 N SER A 398 35.712 -17.768 -12.159 1.00 27.95 N
ANISOU 2951 N SER A 398 4056 3703 2861 -438 325 -1289 N
ATOM 2952 CA SER A 398 35.821 -17.525 -13.591 1.00 29.79 C
ANISOU 2952 CA SER A 398 4320 3916 3084 -312 198 -1243 C
ATOM 2953 C SER A 398 34.601 -16.821 -14.167 1.00 27.33 C
ANISOU 2953 C SER A 398 4133 3497 2756 -181 143 -1199 C
ATOM 2954 O SER A 398 34.422 -16.816 -15.388 1.00 24.53 O
ANISOU 2954 O SER A 398 3830 3108 2382 -77 47 -1160 O
ATOM 2955 CB SER A 398 36.056 -18.842 -14.328 1.00 30.12 C
ANISOU 2955 CB SER A 398 4300 4031 3114 -300 164 -1266 C
ATOM 2956 OG SER A 398 37.173 -19.520 -13.796 1.00 35.88 O
ANISOU 2956 OG SER A 398 4895 4877 3859 -409 207 -1317 O
ATOM 2957 N LEU A 399 33.760 -16.231 -13.323 1.00 21.45 N
ANISOU 2957 N LEU A 399 3437 2697 2015 -193 207 -1203 N
ATOM 2958 CA LEU A 399 32.543 -15.585 -13.802 1.00 23.31 C
ANISOU 2958 CA LEU A 399 3748 2863 2248 -69 157 -1182 C
ATOM 2959 C LEU A 399 32.895 -14.335 -14.602 1.00 26.28 C
ANISOU 2959 C LEU A 399 4118 3221 2646 18 52 -1149 C
ATOM 2960 O LEU A 399 33.603 -13.451 -14.107 1.00 20.93 O
ANISOU 2960 O LEU A 399 3430 2539 1986 -39 74 -1133 O
ATOM 2961 CB LEU A 399 31.638 -15.226 -12.628 1.00 21.73 C
ANISOU 2961 CB LEU A 399 3594 2610 2052 -133 271 -1189 C
ATOM 2962 CG LEU A 399 30.225 -14.769 -13.007 1.00 28.84 C
ANISOU 2962 CG LEU A 399 4547 3454 2956 -41 255 -1176 C
ATOM 2963 CD1 LEU A 399 29.359 -15.955 -13.426 1.00 20.97 C
ANISOU 2963 CD1 LEU A 399 3556 2473 1940 6 257 -1204 C
ATOM 2964 CD2 LEU A 399 29.581 -13.991 -11.871 1.00 29.15 C
ANISOU 2964 CD2 LEU A 399 4669 3411 2995 -108 361 -1150 C
ATOM 2965 N ARG A 400 32.396 -14.263 -15.839 1.00 27.25 N
ANISOU 2965 N ARG A 400 4174 3366 2815 120 -36 -1119 N
ATOM 2966 CA ARG A 400 32.596 -13.099 -16.690 1.00 21.93 C
ANISOU 2966 CA ARG A 400 3332 2760 2241 59 -20 -1133 C
ATOM 2967 C ARG A 400 31.308 -12.368 -17.029 1.00 19.54 C
ANISOU 2967 C ARG A 400 3147 2352 1925 23 54 -1100 C
ATOM 2968 O ARG A 400 31.361 -11.179 -17.363 1.00 20.49 O
ANISOU 2968 O ARG A 400 3326 2411 2046 39 32 -1047 O
ATOM 2969 CB ARG A 400 33.284 -13.501 -18.004 1.00 26.86 C
ANISOU 2969 CB ARG A 400 4045 3341 2818 -139 84 -1040 C
ATOM 2970 CG ARG A 400 34.627 -14.184 -17.825 1.00 40.70 C
ANISOU 2970 CG ARG A 400 6025 4985 4456 -66 -33 -927 C
ATOM 2971 CD ARG A 400 35.489 -14.053 -19.072 1.00 52.76 C
ANISOU 2971 CD ARG A 400 7412 6610 6024 -114 -59 -955 C
ATOM 2972 NE ARG A 400 36.813 -14.634 -18.873 1.00 65.32 N
ANISOU 2972 NE ARG A 400 8983 8245 7589 -99 -125 -973 N
ATOM 2973 CZ ARG A 400 37.803 -14.025 -18.227 1.00 68.60 C
ANISOU 2973 CZ ARG A 400 9380 8674 8010 -105 -147 -984 C
ATOM 2974 NH1 ARG A 400 37.625 -12.815 -17.712 1.00 66.26 N
ANISOU 2974 NH1 ARG A 400 9128 8318 7730 -87 -140 -951 N
ATOM 2975 NH2 ARG A 400 38.976 -14.627 -18.092 1.00 68.49 N
ANISOU 2975 NH2 ARG A 400 9246 8764 8013 -136 -160 -1022 N
ATOM 2976 N HIS A 401 30.162 -13.041 -16.949 1.00 18.43 N
ANISOU 2976 N HIS A 401 3064 2178 1759 59 77 -1116 N
ATOM 2977 CA HIS A 401 28.883 -12.480 -17.356 1.00 18.62 C
ANISOU 2977 CA HIS A 401 3221 2090 1765 131 65 -1024 C
ATOM 2978 C HIS A 401 27.848 -12.810 -16.293 1.00 22.76 C
ANISOU 2978 C HIS A 401 3811 2574 2261 140 129 -1049 C
ATOM 2979 O HIS A 401 27.674 -13.980 -15.935 1.00 22.94 O
ANISOU 2979 O HIS A 401 3804 2644 2271 127 161 -1113 O
ATOM 2980 CB HIS A 401 28.456 -13.040 -18.714 1.00 20.70 C
ANISOU 2980 CB HIS A 401 3515 2333 2017 205 -4 -956 C
ATOM 2981 CG HIS A 401 27.177 -12.465 -19.240 1.00 28.08 C
ANISOU 2981 CG HIS A 401 4563 3175 2931 328 -66 -856 C
ATOM 2982 ND1 HIS A 401 27.139 -11.592 -20.305 1.00 25.15 N
ANISOU 2982 ND1 HIS A 401 4221 2769 2566 433 -187 -759 N
ATOM 2983 CD2 HIS A 401 25.889 -12.652 -18.861 1.00 26.76 C
ANISOU 2983 CD2 HIS A 401 4485 2951 2731 367 -30 -841 C
ATOM 2984 CE1 HIS A 401 25.884 -11.260 -20.553 1.00 20.38 C
ANISOU 2984 CE1 HIS A 401 3715 2101 1929 528 -227 -692 C
ATOM 2985 NE2 HIS A 401 25.106 -11.888 -19.691 1.00 23.99 N
ANISOU 2985 NE2 HIS A 401 4218 2538 2359 489 -128 -735 N
ATOM 2986 N LEU A 402 27.165 -11.781 -15.792 1.00 18.88 N
ANISOU 2986 N LEU A 402 3426 1993 1754 166 148 -986 N
ATOM 2987 CA LEU A 402 26.156 -11.947 -14.751 1.00 19.73 C
ANISOU 2987 CA LEU A 402 3635 2037 1824 160 228 -980 C
ATOM 2988 C LEU A 402 24.966 -11.060 -15.076 1.00 22.15 C
ANISOU 2988 C LEU A 402 4074 2241 2102 241 208 -881 C
ATOM 2989 O LEU A 402 25.079 -9.830 -15.054 1.00 22.13 O
ANISOU 2989 O LEU A 402 4107 2201 2099 262 179 -830 O
ATOM 2990 CB LEU A 402 26.723 -11.606 -13.368 1.00 21.04 C
ANISOU 2990 CB LEU A 402 3814 2198 1983 85 296 -1007 C
ATOM 2991 CG LEU A 402 25.766 -11.687 -12.174 1.00 24.00 C
ANISOU 2991 CG LEU A 402 4313 2489 2318 51 407 -986 C
ATOM 2992 CD1 LEU A 402 25.114 -13.058 -12.092 1.00 21.71 C
ANISOU 2992 CD1 LEU A 402 4035 2208 2008 45 456 -1019 C
ATOM 2993 CD2 LEU A 402 26.495 -11.376 -10.877 1.00 21.50 C
ANISOU 2993 CD2 LEU A 402 4006 2165 1999 -48 485 -1001 C
ATOM 2994 N ASP A 403 23.826 -11.686 -15.368 1.00 20.18 N
ANISOU 2994 N ASP A 403 3896 1952 1820 294 218 -853 N
ATOM 2995 CA ASP A 403 22.592 -10.980 -15.702 1.00 24.98 C
ANISOU 2995 CA ASP A 403 4637 2471 2383 391 186 -755 C
ATOM 2996 C ASP A 403 21.578 -11.259 -14.602 1.00 25.78 C
ANISOU 2996 C ASP A 403 4849 2504 2441 371 295 -753 C
ATOM 2997 O ASP A 403 21.129 -12.398 -14.438 1.00 24.35 O
ANISOU 2997 O ASP A 403 4672 2331 2250 354 350 -790 O
ATOM 2998 CB ASP A 403 22.055 -11.417 -17.066 1.00 27.94 C
ANISOU 2998 CB ASP A 403 5019 2851 2744 491 91 -706 C
ATOM 2999 CG ASP A 403 20.959 -10.496 -17.590 1.00 37.07 C
ANISOU 2999 CG ASP A 403 6299 3940 3846 611 16 -600 C
ATOM 3000 OD1 ASP A 403 20.373 -9.737 -16.791 1.00 37.43 O
ANISOU 3000 OD1 ASP A 403 6441 3925 3856 614 63 -570 O
ATOM 3001 OD2 ASP A 403 20.678 -10.535 -18.807 1.00 37.63 O
ANISOU 3001 OD2 ASP A 403 6370 4024 3904 707 -97 -547 O
ATOM 3002 N LEU A 404 21.213 -10.218 -13.855 1.00 26.71 N
ANISOU 3002 N LEU A 404 5063 2556 2531 373 330 -708 N
ATOM 3003 CA LEU A 404 20.217 -10.318 -12.796 1.00 27.36 C
ANISOU 3003 CA LEU A 404 5274 2557 2565 356 439 -688 C
ATOM 3004 C LEU A 404 19.092 -9.314 -13.010 1.00 22.96 C
ANISOU 3004 C LEU A 404 4857 1920 1946 459 402 -590 C
ATOM 3005 O LEU A 404 18.461 -8.869 -12.050 1.00 27.21 O
ANISOU 3005 O LEU A 404 5512 2385 2443 448 482 -560 O
ATOM 3006 CB LEU A 404 20.861 -10.124 -11.423 1.00 23.13 C
ANISOU 3006 CB LEU A 404 4733 2013 2043 244 541 -730 C
ATOM 3007 CG LEU A 404 21.790 -11.257 -10.991 1.00 25.58 C
ANISOU 3007 CG LEU A 404 4930 2399 2391 142 591 -823 C
ATOM 3008 CD1 LEU A 404 22.779 -10.801 -9.926 1.00 23.28 C
ANISOU 3008 CD1 LEU A 404 4608 2120 2119 41 647 -853 C
ATOM 3009 CD2 LEU A 404 20.982 -12.446 -10.500 1.00 29.87 C
ANISOU 3009 CD2 LEU A 404 5527 2914 2910 113 687 -844 C
ATOM 3010 N SER A 405 18.835 -8.958 -14.267 1.00 22.39 N
ANISOU 3010 N SER A 405 4781 1864 1861 564 277 -538 N
ATOM 3011 CA SER A 405 17.880 -7.917 -14.606 1.00 22.55 C
ANISOU 3011 CA SER A 405 4921 1834 1815 673 212 -449 C
ATOM 3012 C SER A 405 16.452 -8.453 -14.595 1.00 27.43 C
ANISOU 3012 C SER A 405 5667 2393 2361 740 245 -403 C
ATOM 3013 O SER A 405 16.210 -9.659 -14.677 1.00 31.06 O
ANISOU 3013 O SER A 405 6111 2861 2831 720 291 -435 O
ATOM 3014 CB SER A 405 18.198 -7.319 -15.978 1.00 32.08 C
ANISOU 3014 CB SER A 405 6069 3092 3029 760 53 -411 C
ATOM 3015 OG SER A 405 18.172 -8.312 -16.989 1.00 34.94 O
ANISOU 3015 OG SER A 405 6374 3496 3405 795 -5 -418 O
ATOM 3016 N PHE A 406 15.500 -7.526 -14.491 1.00 23.83 N
ANISOU 3016 N PHE A 406 5344 1882 1829 822 222 -331 N
ATOM 3017 CA PHE A 406 14.069 -7.841 -14.478 1.00 24.69 C
ANISOU 3017 CA PHE A 406 5595 1931 1853 899 248 -276 C
ATOM 3018 C PHE A 406 13.732 -8.857 -13.389 1.00 32.49 C
ANISOU 3018 C PHE A 406 6632 2866 2845 814 411 -311 C
ATOM 3019 O PHE A 406 13.052 -9.858 -13.622 1.00 34.79 O
ANISOU 3019 O PHE A 406 6955 3144 3117 836 441 -310 O
ATOM 3020 CB PHE A 406 13.604 -8.345 -15.846 1.00 27.86 C
ANISOU 3020 CB PHE A 406 5981 2375 2230 999 132 -247 C
ATOM 3021 CG PHE A 406 13.803 -7.355 -16.960 1.00 28.15 C
ANISOU 3021 CG PHE A 406 5983 2464 2249 1088 -35 -208 C
ATOM 3022 CD1 PHE A 406 12.872 -6.352 -17.193 1.00 29.50 C
ANISOU 3022 CD1 PHE A 406 6269 2616 2325 1194 -109 -142 C
ATOM 3023 CD2 PHE A 406 14.913 -7.435 -17.778 1.00 22.61 C
ANISOU 3023 CD2 PHE A 406 5135 1836 1619 1068 -121 -240 C
ATOM 3024 CE1 PHE A 406 13.058 -5.444 -18.219 1.00 27.60 C
ANISOU 3024 CE1 PHE A 406 5989 2434 2065 1270 -267 -117 C
ATOM 3025 CE2 PHE A 406 15.105 -6.533 -18.802 1.00 33.41 C
ANISOU 3025 CE2 PHE A 406 6470 3252 2971 1146 -274 -205 C
ATOM 3026 CZ PHE A 406 14.176 -5.536 -19.025 1.00 29.00 C
ANISOU 3026 CZ PHE A 406 6019 2680 2320 1244 -349 -148 C
ATOM 3027 N ASN A 407 14.212 -8.588 -12.183 1.00 28.49 N
ANISOU 3027 N ASN A 407 6131 2329 2363 715 516 -343 N
ATOM 3028 CA ASN A 407 13.978 -9.445 -11.029 1.00 30.19 C
ANISOU 3028 CA ASN A 407 6393 2493 2583 621 675 -377 C
ATOM 3029 C ASN A 407 13.404 -8.612 -9.885 1.00 27.66 C
ANISOU 3029 C ASN A 407 6221 2083 2206 611 765 -330 C
ATOM 3030 O ASN A 407 13.067 -7.438 -10.050 1.00 34.72 O
ANISOU 3030 O ASN A 407 7185 2956 3050 691 699 -272 O
ATOM 3031 CB ASN A 407 15.271 -10.161 -10.626 1.00 26.39 C
ANISOU 3031 CB ASN A 407 5761 2076 2189 489 723 -475 C
ATOM 3032 CG ASN A 407 15.597 -11.328 -11.537 1.00 31.62 C
ANISOU 3032 CG ASN A 407 6305 2816 2894 491 674 -528 C
ATOM 3033 OD1 ASN A 407 14.715 -12.104 -11.908 1.00 32.58 O
ANISOU 3033 OD1 ASN A 407 6477 2917 2984 541 687 -512 O
ATOM 3034 ND2 ASN A 407 16.866 -11.464 -11.895 1.00 27.27 N
ANISOU 3034 ND2 ASN A 407 5597 2353 2410 440 621 -592 N
ATOM 3035 N GLY A 408 13.295 -9.237 -8.718 1.00 28.51 N
ANISOU 3035 N GLY A 408 6377 2137 2320 511 916 -358 N
ATOM 3036 CA GLY A 408 12.757 -8.558 -7.561 1.00 34.24 C
ANISOU 3036 CA GLY A 408 7249 2768 2992 491 1018 -313 C
ATOM 3037 C GLY A 408 13.810 -7.891 -6.701 1.00 37.34 C
ANISOU 3037 C GLY A 408 7588 3171 3427 394 1056 -349 C
ATOM 3038 O GLY A 408 14.550 -7.021 -7.170 1.00 37.74 O
ANISOU 3038 O GLY A 408 7559 3278 3504 420 953 -354 O
ATOM 3039 N ALA A 409 13.887 -8.298 -5.438 1.00 35.22 N
ANISOU 3039 N ALA A 409 7365 2848 3168 279 1206 -374 N
ATOM 3040 CA ALA A 409 14.770 -7.665 -4.467 1.00 30.77 C
ANISOU 3040 CA ALA A 409 6776 2281 2633 182 1259 -400 C
ATOM 3041 C ALA A 409 16.162 -8.276 -4.555 1.00 32.24 C
ANISOU 3041 C ALA A 409 6776 2566 2908 78 1242 -491 C
ATOM 3042 O ALA A 409 16.344 -9.464 -4.268 1.00 31.13 O
ANISOU 3042 O ALA A 409 6586 2443 2800 -9 1317 -545 O
ATOM 3043 CB ALA A 409 14.209 -7.816 -3.053 1.00 31.41 C
ANISOU 3043 CB ALA A 409 6999 2255 2680 102 1432 -381 C
ATOM 3044 N ILE A 410 17.141 -7.463 -4.940 1.00 31.06 N
ANISOU 3044 N ILE A 410 6525 2482 2793 88 1145 -508 N
ATOM 3045 CA ILE A 410 18.546 -7.853 -4.959 1.00 32.37 C
ANISOU 3045 CA ILE A 410 6524 2742 3033 -6 1125 -587 C
ATOM 3046 C ILE A 410 19.258 -7.041 -3.882 1.00 33.83 C
ANISOU 3046 C ILE A 410 6719 2907 3227 -90 1186 -595 C
ATOM 3047 O ILE A 410 19.518 -5.843 -4.060 1.00 36.00 O
ANISOU 3047 O ILE A 410 6997 3186 3494 -37 1116 -567 O
ATOM 3048 CB ILE A 410 19.182 -7.639 -6.338 1.00 32.41 C
ANISOU 3048 CB ILE A 410 6397 2843 3074 70 965 -603 C
ATOM 3049 CG1 ILE A 410 18.511 -8.541 -7.379 1.00 32.65 C
ANISOU 3049 CG1 ILE A 410 6415 2894 3096 144 911 -598 C
ATOM 3050 CG2 ILE A 410 20.678 -7.906 -6.281 1.00 30.55 C
ANISOU 3050 CG2 ILE A 410 6001 2701 2904 -23 946 -678 C
ATOM 3051 CD1 ILE A 410 19.039 -8.342 -8.784 1.00 36.04 C
ANISOU 3051 CD1 ILE A 410 6728 3407 3557 221 758 -605 C
ATOM 3052 N ILE A 411 19.569 -7.687 -2.761 1.00 30.94 N
ANISOU 3052 N ILE A 411 6357 2520 2877 -223 1317 -635 N
ATOM 3053 CA ILE A 411 20.136 -7.018 -1.595 1.00 29.05 C
ANISOU 3053 CA ILE A 411 6146 2250 2643 -315 1398 -640 C
ATOM 3054 C ILE A 411 21.651 -7.094 -1.706 1.00 33.52 C
ANISOU 3054 C ILE A 411 6544 2921 3271 -390 1350 -706 C
ATOM 3055 O ILE A 411 22.240 -8.178 -1.605 1.00 35.55 O
ANISOU 3055 O ILE A 411 6706 3235 3565 -480 1384 -768 O
ATOM 3056 CB ILE A 411 19.643 -7.641 -0.281 1.00 33.65 C
ANISOU 3056 CB ILE A 411 6831 2746 3208 -427 1574 -644 C
ATOM 3057 CG1 ILE A 411 18.204 -7.212 0.019 1.00 32.85 C
ANISOU 3057 CG1 ILE A 411 6923 2526 3033 -349 1628 -564 C
ATOM 3058 CG2 ILE A 411 20.575 -7.275 0.882 1.00 30.63 C
ANISOU 3058 CG2 ILE A 411 6426 2362 2851 -557 1657 -676 C
ATOM 3059 CD1 ILE A 411 17.155 -8.062 -0.655 1.00 33.68 C
ANISOU 3059 CD1 ILE A 411 7075 2609 3112 -278 1621 -543 C
ATOM 3060 N MET A 412 22.284 -5.940 -1.909 1.00 27.61 N
ANISOU 3060 N MET A 412 5762 2200 2530 -352 1272 -694 N
ATOM 3061 CA MET A 412 23.737 -5.863 -1.989 1.00 28.78 C
ANISOU 3061 CA MET A 412 5763 2441 2730 -416 1227 -748 C
ATOM 3062 C MET A 412 24.329 -5.933 -0.585 1.00 33.65 C
ANISOU 3062 C MET A 412 6392 3037 3358 -562 1357 -778 C
ATOM 3063 O MET A 412 24.006 -5.107 0.278 1.00 41.56 O
ANISOU 3063 O MET A 412 7499 3961 4329 -575 1423 -743 O
ATOM 3064 CB MET A 412 24.168 -4.580 -2.700 1.00 26.05 C
ANISOU 3064 CB MET A 412 5381 2126 2389 -324 1104 -724 C
ATOM 3065 CG MET A 412 23.710 -4.484 -4.150 1.00 29.69 C
ANISOU 3065 CG MET A 412 5814 2619 2849 -190 970 -700 C
ATOM 3066 SD MET A 412 24.094 -5.958 -5.116 1.00 40.02 S
ANISOU 3066 SD MET A 412 6991 4018 4197 -198 918 -755 S
ATOM 3067 CE MET A 412 25.869 -6.072 -4.902 1.00 28.29 C
ANISOU 3067 CE MET A 412 5351 2633 2765 -301 905 -822 C
ATOM 3068 N SER A 413 25.190 -6.927 -0.357 1.00 32.31 N
ANISOU 3068 N SER A 413 6113 2937 3228 -673 1393 -842 N
ATOM 3069 CA SER A 413 25.838 -7.090 0.935 1.00 33.25 C
ANISOU 3069 CA SER A 413 6225 3048 3362 -825 1514 -878 C
ATOM 3070 C SER A 413 27.328 -7.389 0.836 1.00 31.09 C
ANISOU 3070 C SER A 413 5791 2889 3135 -903 1477 -938 C
ATOM 3071 O SER A 413 28.009 -7.363 1.864 1.00 34.17 O
ANISOU 3071 O SER A 413 6162 3283 3539 -1027 1564 -968 O
ATOM 3072 CB SER A 413 25.150 -8.203 1.745 1.00 44.03 C
ANISOU 3072 CB SER A 413 7651 4358 4720 -921 1655 -897 C
ATOM 3073 OG SER A 413 25.530 -9.492 1.301 1.00 52.51 O
ANISOU 3073 OG SER A 413 8611 5514 5826 -966 1642 -956 O
ATOM 3074 N ALA A 414 27.853 -7.659 -0.357 1.00 32.12 N
ANISOU 3074 N ALA A 414 5809 3110 3286 -836 1352 -956 N
ATOM 3075 CA ALA A 414 29.269 -7.931 -0.553 1.00 30.72 C
ANISOU 3075 CA ALA A 414 5484 3043 3146 -897 1308 -1006 C
ATOM 3076 C ALA A 414 29.661 -7.407 -1.927 1.00 29.86 C
ANISOU 3076 C ALA A 414 5307 2994 3046 -769 1149 -990 C
ATOM 3077 O ALA A 414 28.883 -7.518 -2.881 1.00 36.66 O
ANISOU 3077 O ALA A 414 6192 3841 3895 -657 1076 -965 O
ATOM 3078 CB ALA A 414 29.577 -9.426 -0.444 1.00 26.53 C
ANISOU 3078 CB ALA A 414 4868 2577 2636 -990 1355 -1068 C
ATOM 3079 N ASN A 415 30.860 -6.843 -2.029 1.00 27.64 N
ANISOU 3079 N ASN A 415 4941 2775 2786 -789 1100 -1003 N
ATOM 3080 CA ASN A 415 31.304 -6.217 -3.276 1.00 23.42 C
ANISOU 3080 CA ASN A 415 4346 2290 2263 -676 957 -987 C
ATOM 3081 C ASN A 415 32.190 -7.146 -4.097 1.00 23.33 C
ANISOU 3081 C ASN A 415 4205 2383 2275 -681 888 -1027 C
ATOM 3082 O ASN A 415 33.302 -6.796 -4.480 1.00 27.82 O
ANISOU 3082 O ASN A 415 4690 3017 2862 -682 826 -1037 O
ATOM 3083 CB ASN A 415 32.007 -4.898 -2.990 1.00 26.89 C
ANISOU 3083 CB ASN A 415 4785 2725 2708 -676 938 -970 C
ATOM 3084 CG ASN A 415 33.040 -5.011 -1.894 1.00 28.69 C
ANISOU 3084 CG ASN A 415 4967 2985 2947 -817 1027 -1005 C
ATOM 3085 OD1 ASN A 415 33.373 -6.104 -1.441 1.00 30.16 O
ANISOU 3085 OD1 ASN A 415 5102 3213 3143 -918 1092 -1048 O
ATOM 3086 ND2 ASN A 415 33.559 -3.869 -1.459 1.00 23.55 N
ANISOU 3086 ND2 ASN A 415 4330 2320 2297 -826 1030 -991 N
ATOM 3087 N PHE A 416 31.687 -8.355 -4.355 1.00 24.68 N
ANISOU 3087 N PHE A 416 4364 2569 2442 -684 902 -1050 N
ATOM 3088 CA PHE A 416 32.171 -9.249 -5.405 1.00 24.79 C
ANISOU 3088 CA PHE A 416 4278 2670 2469 -645 815 -1078 C
ATOM 3089 C PHE A 416 33.580 -9.778 -5.174 1.00 26.96 C
ANISOU 3089 C PHE A 416 4436 3043 2764 -744 826 -1123 C
ATOM 3090 O PHE A 416 34.295 -10.062 -6.142 1.00 23.61 O
ANISOU 3090 O PHE A 416 3929 2693 2350 -696 731 -1133 O
ATOM 3091 CB PHE A 416 32.097 -8.570 -6.777 1.00 21.58 C
ANISOU 3091 CB PHE A 416 3859 2273 2067 -499 673 -1047 C
ATOM 3092 CG PHE A 416 30.698 -8.269 -7.225 1.00 23.42 C
ANISOU 3092 CG PHE A 416 4183 2431 2283 -396 649 -1010 C
ATOM 3093 CD1 PHE A 416 30.065 -7.103 -6.826 1.00 21.78 C
ANISOU 3093 CD1 PHE A 416 4070 2144 2062 -367 671 -966 C
ATOM 3094 CD2 PHE A 416 30.017 -9.146 -8.051 1.00 21.51 C
ANISOU 3094 CD2 PHE A 416 3934 2203 2036 -329 606 -1019 C
ATOM 3095 CE1 PHE A 416 28.780 -6.819 -7.240 1.00 21.88 C
ANISOU 3095 CE1 PHE A 416 4169 2089 2054 -275 651 -926 C
ATOM 3096 CE2 PHE A 416 28.729 -8.868 -8.468 1.00 27.65 C
ANISOU 3096 CE2 PHE A 416 4795 2914 2797 -241 589 -981 C
ATOM 3097 CZ PHE A 416 28.111 -7.701 -8.063 1.00 26.60 C
ANISOU 3097 CZ PHE A 416 4758 2701 2648 -215 612 -931 C
ATOM 3098 N MET A 417 34.001 -9.933 -3.922 1.00 26.41 N
ANISOU 3098 N MET A 417 4357 2977 2700 -882 940 -1151 N
ATOM 3099 CA MET A 417 35.240 -10.649 -3.648 1.00 23.35 C
ANISOU 3099 CA MET A 417 3849 2693 2330 -985 962 -1203 C
ATOM 3100 C MET A 417 35.157 -12.062 -4.213 1.00 26.93 C
ANISOU 3100 C MET A 417 4235 3210 2785 -983 941 -1242 C
ATOM 3101 O MET A 417 34.128 -12.735 -4.092 1.00 28.38 O
ANISOU 3101 O MET A 417 4473 3353 2959 -979 985 -1249 O
ATOM 3102 CB MET A 417 35.504 -10.694 -2.145 1.00 27.59 C
ANISOU 3102 CB MET A 417 4392 3218 2873 -1138 1099 -1234 C
ATOM 3103 CG MET A 417 36.211 -9.472 -1.582 1.00 45.07 C
ANISOU 3103 CG MET A 417 6618 5418 5090 -1168 1112 -1215 C
ATOM 3104 SD MET A 417 36.771 -9.794 0.103 1.00 61.18 S
ANISOU 3104 SD MET A 417 8633 7474 7140 -1359 1267 -1268 S
ATOM 3105 CE MET A 417 37.642 -11.348 -0.116 1.00 61.00 C
ANISOU 3105 CE MET A 417 8453 7590 7134 -1437 1264 -1342 C
ATOM 3106 N GLY A 418 36.239 -12.508 -4.848 1.00 24.38 N
ANISOU 3106 N GLY A 418 3800 2991 2472 -982 873 -1265 N
ATOM 3107 CA GLY A 418 36.256 -13.802 -5.497 1.00 25.26 C
ANISOU 3107 CA GLY A 418 3843 3173 2583 -967 839 -1300 C
ATOM 3108 C GLY A 418 35.753 -13.808 -6.924 1.00 30.45 C
ANISOU 3108 C GLY A 418 4527 3815 3228 -811 715 -1265 C
ATOM 3109 O GLY A 418 35.875 -14.840 -7.597 1.00 31.69 O
ANISOU 3109 O GLY A 418 4626 4035 3382 -786 672 -1291 O
ATOM 3110 N LEU A 419 35.210 -12.693 -7.415 1.00 32.32 N
ANISOU 3110 N LEU A 419 4846 3975 3459 -706 655 -1211 N
ATOM 3111 CA LEU A 419 34.588 -12.615 -8.731 1.00 28.73 C
ANISOU 3111 CA LEU A 419 4425 3497 2994 -554 541 -1181 C
ATOM 3112 C LEU A 419 35.160 -11.461 -9.552 1.00 28.39 C
ANISOU 3112 C LEU A 419 4375 3449 2961 -468 436 -1142 C
ATOM 3113 O LEU A 419 34.440 -10.796 -10.302 1.00 25.63 O
ANISOU 3113 O LEU A 419 4078 3049 2610 -352 362 -1111 O
ATOM 3114 CB LEU A 419 33.073 -12.459 -8.604 1.00 24.11 C
ANISOU 3114 CB LEU A 419 3947 2820 2394 -497 571 -1160 C
ATOM 3115 CG LEU A 419 32.250 -13.412 -7.730 1.00 26.48 C
ANISOU 3115 CG LEU A 419 4284 3094 2682 -575 688 -1189 C
ATOM 3116 CD1 LEU A 419 30.808 -12.929 -7.641 1.00 32.74 C
ANISOU 3116 CD1 LEU A 419 5198 3784 3458 -509 712 -1152 C
ATOM 3117 CD2 LEU A 419 32.311 -14.826 -8.278 1.00 25.33 C
ANISOU 3117 CD2 LEU A 419 4074 3019 2532 -570 666 -1231 C
ATOM 3118 N GLU A 420 36.465 -11.205 -9.440 1.00 25.16 N
ANISOU 3118 N GLU A 420 3896 3100 2565 -525 428 -1148 N
ATOM 3119 CA GLU A 420 37.048 -10.049 -10.118 1.00 31.77 C
ANISOU 3119 CA GLU A 420 4731 3927 3413 -457 342 -1112 C
ATOM 3120 C GLU A 420 37.256 -10.257 -11.613 1.00 24.95 C
ANISOU 3120 C GLU A 420 3844 3085 2549 -342 214 -1096 C
ATOM 3121 O GLU A 420 37.743 -9.339 -12.278 1.00 28.57 O
ANISOU 3121 O GLU A 420 4301 3535 3021 -283 138 -1068 O
ATOM 3122 CB GLU A 420 38.379 -9.650 -9.470 1.00 33.27 C
ANISOU 3122 CB GLU A 420 4857 4170 3614 -557 383 -1122 C
ATOM 3123 CG GLU A 420 39.100 -10.771 -8.748 1.00 40.52 C
ANISOU 3123 CG GLU A 420 5691 5174 4533 -682 460 -1172 C
ATOM 3124 CD GLU A 420 38.610 -10.963 -7.322 1.00 43.25 C
ANISOU 3124 CD GLU A 420 6066 5492 4877 -794 592 -1200 C
ATOM 3125 OE1 GLU A 420 38.432 -9.959 -6.597 1.00 45.14 O
ANISOU 3125 OE1 GLU A 420 6364 5671 5117 -819 639 -1180 O
ATOM 3126 OE2 GLU A 420 38.394 -12.126 -6.932 1.00 44.18 O
ANISOU 3126 OE2 GLU A 420 6150 5645 4992 -858 649 -1243 O
ATOM 3127 N GLU A 421 36.915 -11.425 -12.157 1.00 18.57 N
ANISOU 3127 N GLU A 421 3024 2303 1730 -313 189 -1113 N
ATOM 3128 CA GLU A 421 36.934 -11.624 -13.602 1.00 17.94 C
ANISOU 3128 CA GLU A 421 2950 2222 1644 -197 69 -1091 C
ATOM 3129 C GLU A 421 35.669 -11.114 -14.279 1.00 21.63 C
ANISOU 3129 C GLU A 421 3474 2627 2115 -63 1 -1079 C
ATOM 3130 O GLU A 421 35.563 -11.197 -15.507 1.00 23.32 O
ANISOU 3130 O GLU A 421 3670 2842 2347 30 -92 -1038 O
ATOM 3131 CB GLU A 421 37.131 -13.108 -13.931 1.00 18.99 C
ANISOU 3131 CB GLU A 421 3041 2414 1761 -222 71 -1115 C
ATOM 3132 CG GLU A 421 38.451 -13.689 -13.439 1.00 28.80 C
ANISOU 3132 CG GLU A 421 4173 3757 3013 -340 120 -1147 C
ATOM 3133 CD GLU A 421 39.654 -13.003 -14.061 1.00 45.27 C
ANISOU 3133 CD GLU A 421 6222 5867 5111 -329 57 -1117 C
ATOM 3134 OE1 GLU A 421 39.853 -13.138 -15.287 1.00 50.07 O
ANISOU 3134 OE1 GLU A 421 6843 6468 5713 -258 -31 -1085 O
ATOM 3135 OE2 GLU A 421 40.397 -12.316 -13.326 1.00 53.57 O
ANISOU 3135 OE2 GLU A 421 7239 6941 6175 -398 102 -1123 O
ATOM 3136 N LEU A 422 34.720 -10.582 -13.510 1.00 21.77 N
ANISOU 3136 N LEU A 422 3524 2606 2143 -79 68 -1087 N
ATOM 3137 CA LEU A 422 33.429 -10.182 -14.054 1.00 23.41 C
ANISOU 3137 CA LEU A 422 3732 2787 2374 -1 46 -1095 C
ATOM 3138 C LEU A 422 33.590 -9.031 -15.041 1.00 23.21 C
ANISOU 3138 C LEU A 422 3632 2780 2408 21 1 -1075 C
ATOM 3139 O LEU A 422 34.144 -7.982 -14.700 1.00 20.63 O
ANISOU 3139 O LEU A 422 3318 2435 2087 7 -2 -1062 O
ATOM 3140 CB LEU A 422 32.486 -9.786 -12.918 1.00 20.11 C
ANISOU 3140 CB LEU A 422 3406 2295 1940 -54 151 -1075 C
ATOM 3141 CG LEU A 422 30.991 -9.670 -13.229 1.00 24.47 C
ANISOU 3141 CG LEU A 422 4013 2791 2494 -7 170 -1056 C
ATOM 3142 CD1 LEU A 422 30.477 -10.939 -13.888 1.00 18.71 C
ANISOU 3142 CD1 LEU A 422 3253 2097 1759 27 151 -1087 C
ATOM 3143 CD2 LEU A 422 30.187 -9.366 -11.967 1.00 24.47 C
ANISOU 3143 CD2 LEU A 422 4128 2706 2463 -55 275 -1028 C
ATOM 3144 N GLN A 423 33.094 -9.232 -16.263 1.00 26.29 N
ANISOU 3144 N GLN A 423 3993 3176 2821 5 11 -1055 N
ATOM 3145 CA GLN A 423 33.155 -8.226 -17.317 1.00 25.92 C
ANISOU 3145 CA GLN A 423 4001 3072 2777 19 -22 -973 C
ATOM 3146 C GLN A 423 31.822 -7.553 -17.600 1.00 23.79 C
ANISOU 3146 C GLN A 423 3846 2699 2492 115 -58 -886 C
ATOM 3147 O GLN A 423 31.808 -6.393 -18.022 1.00 15.74 O
ANISOU 3147 O GLN A 423 2865 1635 1479 170 -115 -818 O
ATOM 3148 CB GLN A 423 33.665 -8.850 -18.622 1.00 21.67 C
ANISOU 3148 CB GLN A 423 3450 2551 2232 36 -80 -925 C
ATOM 3149 CG GLN A 423 35.111 -9.306 -18.588 1.00 28.96 C
ANISOU 3149 CG GLN A 423 4307 3550 3147 -65 -52 -958 C
ATOM 3150 CD GLN A 423 35.531 -9.938 -19.894 1.00 40.43 C
ANISOU 3150 CD GLN A 423 5758 5009 4595 -3 -145 -904 C
ATOM 3151 OE1 GLN A 423 34.753 -10.655 -20.519 1.00 44.44 O
ANISOU 3151 OE1 GLN A 423 6275 5502 5105 75 -189 -883 O
ATOM 3152 NE2 GLN A 423 36.759 -9.666 -20.322 1.00 39.63 N
ANISOU 3152 NE2 GLN A 423 5622 4936 4499 -17 -185 -883 N
ATOM 3153 N HIS A 424 30.704 -8.244 -17.375 1.00 19.23 N
ANISOU 3153 N HIS A 424 3322 2091 1892 143 -33 -889 N
ATOM 3154 CA HIS A 424 29.379 -7.763 -17.750 1.00 21.21 C
ANISOU 3154 CA HIS A 424 3685 2257 2118 244 -76 -804 C
ATOM 3155 C HIS A 424 28.440 -7.945 -16.564 1.00 22.90 C
ANISOU 3155 C HIS A 424 3968 2430 2302 223 10 -831 C
ATOM 3156 O HIS A 424 28.320 -9.053 -16.026 1.00 21.01 O
ANISOU 3156 O HIS A 424 3703 2222 2057 177 70 -896 O
ATOM 3157 CB HIS A 424 28.861 -8.526 -18.978 1.00 21.74 C
ANISOU 3157 CB HIS A 424 3763 2320 2176 330 -155 -756 C
ATOM 3158 CG HIS A 424 27.541 -8.041 -19.494 1.00 22.57 C
ANISOU 3158 CG HIS A 424 3971 2356 2249 449 -224 -671 C
ATOM 3159 ND1 HIS A 424 27.425 -7.222 -20.597 1.00 25.27 N
ANISOU 3159 ND1 HIS A 424 4327 2682 2593 556 -352 -590 N
ATOM 3160 CD2 HIS A 424 26.277 -8.274 -19.067 1.00 27.44 C
ANISOU 3160 CD2 HIS A 424 4680 2923 2825 481 -187 -656 C
ATOM 3161 CE1 HIS A 424 26.149 -6.970 -20.827 1.00 27.68 C
ANISOU 3161 CE1 HIS A 424 4725 2939 2853 646 -396 -533 C
ATOM 3162 NE2 HIS A 424 25.431 -7.598 -19.913 1.00 28.81 N
ANISOU 3162 NE2 HIS A 424 4923 3057 2968 603 -293 -568 N
ATOM 3163 N LEU A 425 27.781 -6.860 -16.152 1.00 19.28 N
ANISOU 3163 N LEU A 425 3602 1901 1821 261 12 -779 N
ATOM 3164 CA LEU A 425 26.899 -6.867 -14.986 1.00 24.45 C
ANISOU 3164 CA LEU A 425 4348 2500 2440 243 97 -784 C
ATOM 3165 C LEU A 425 25.649 -6.057 -15.302 1.00 26.30 C
ANISOU 3165 C LEU A 425 4707 2654 2630 343 56 -694 C
ATOM 3166 O LEU A 425 25.742 -4.868 -15.623 1.00 26.50 O
ANISOU 3166 O LEU A 425 4753 2662 2654 390 -5 -647 O
ATOM 3167 CB LEU A 425 27.618 -6.306 -13.753 1.00 18.72 C
ANISOU 3167 CB LEU A 425 3608 1780 1723 164 163 -824 C
ATOM 3168 CG LEU A 425 26.859 -6.321 -12.427 1.00 19.62 C
ANISOU 3168 CG LEU A 425 3827 1829 1797 131 263 -820 C
ATOM 3169 CD1 LEU A 425 26.392 -7.728 -12.099 1.00 20.16 C
ANISOU 3169 CD1 LEU A 425 3904 1906 1850 101 323 -857 C
ATOM 3170 CD2 LEU A 425 27.733 -5.768 -11.311 1.00 19.81 C
ANISOU 3170 CD2 LEU A 425 3838 1861 1829 51 319 -848 C
ATOM 3171 N ASP A 426 24.482 -6.695 -15.201 1.00 25.85 N
ANISOU 3171 N ASP A 426 4736 2555 2533 381 85 -673 N
ATOM 3172 CA ASP A 426 23.212 -6.099 -15.608 1.00 25.71 C
ANISOU 3172 CA ASP A 426 4837 2471 2458 489 34 -588 C
ATOM 3173 C ASP A 426 22.202 -6.263 -14.481 1.00 22.51 C
ANISOU 3173 C ASP A 426 4550 1998 2004 473 139 -582 C
ATOM 3174 O ASP A 426 21.844 -7.391 -14.126 1.00 23.45 O
ANISOU 3174 O ASP A 426 4678 2113 2118 437 209 -616 O
ATOM 3175 CB ASP A 426 22.692 -6.747 -16.898 1.00 19.86 C
ANISOU 3175 CB ASP A 426 4094 1748 1705 578 -58 -550 C
ATOM 3176 CG ASP A 426 21.556 -5.963 -17.537 1.00 28.75 C
ANISOU 3176 CG ASP A 426 5325 2831 2767 704 -150 -461 C
ATOM 3177 OD1 ASP A 426 20.937 -5.128 -16.850 1.00 27.12 O
ANISOU 3177 OD1 ASP A 426 5213 2573 2517 722 -118 -433 O
ATOM 3178 OD2 ASP A 426 21.282 -6.180 -18.736 1.00 28.20 O
ANISOU 3178 OD2 ASP A 426 5244 2786 2686 790 -259 -421 O
ATOM 3179 N PHE A 427 21.738 -5.141 -13.926 1.00 23.30 N
ANISOU 3179 N PHE A 427 4742 2042 2066 500 151 -539 N
ATOM 3180 CA PHE A 427 20.692 -5.146 -12.908 1.00 24.78 C
ANISOU 3180 CA PHE A 427 5066 2153 2197 499 246 -515 C
ATOM 3181 C PHE A 427 19.390 -4.515 -13.386 1.00 24.67 C
ANISOU 3181 C PHE A 427 5179 2087 2106 623 184 -431 C
ATOM 3182 O PHE A 427 18.489 -4.299 -12.567 1.00 29.21 O
ANISOU 3182 O PHE A 427 5882 2593 2624 635 257 -400 O
ATOM 3183 CB PHE A 427 21.160 -4.418 -11.647 1.00 22.10 C
ANISOU 3183 CB PHE A 427 4749 1786 1863 423 329 -535 C
ATOM 3184 CG PHE A 427 22.236 -5.136 -10.893 1.00 22.79 C
ANISOU 3184 CG PHE A 427 4741 1916 2002 297 409 -615 C
ATOM 3185 CD1 PHE A 427 22.021 -6.413 -10.404 1.00 24.46 C
ANISOU 3185 CD1 PHE A 427 4955 2127 2213 237 494 -654 C
ATOM 3186 CD2 PHE A 427 23.454 -4.525 -10.652 1.00 27.06 C
ANISOU 3186 CD2 PHE A 427 5193 2501 2585 240 397 -651 C
ATOM 3187 CE1 PHE A 427 23.008 -7.074 -9.701 1.00 29.33 C
ANISOU 3187 CE1 PHE A 427 5486 2791 2866 125 559 -726 C
ATOM 3188 CE2 PHE A 427 24.447 -5.179 -9.949 1.00 28.00 C
ANISOU 3188 CE2 PHE A 427 5232 2667 2740 131 461 -719 C
ATOM 3189 CZ PHE A 427 24.223 -6.455 -9.474 1.00 27.51 C
ANISOU 3189 CZ PHE A 427 5172 2607 2672 74 539 -756 C
ATOM 3190 N GLN A 428 19.274 -4.214 -14.678 1.00 22.68 N
ANISOU 3190 N GLN A 428 4899 1871 1846 717 50 -393 N
ATOM 3191 CA GLN A 428 18.167 -3.439 -15.234 1.00 21.76 C
ANISOU 3191 CA GLN A 428 4889 1728 1650 842 -37 -318 C
ATOM 3192 C GLN A 428 16.810 -3.892 -14.698 1.00 30.39 C
ANISOU 3192 C GLN A 428 6127 2753 2666 879 35 -283 C
ATOM 3193 O GLN A 428 16.475 -5.079 -14.735 1.00 33.93 O
ANISOU 3193 O GLN A 428 6579 3194 3117 861 84 -298 O
ATOM 3194 CB GLN A 428 18.200 -3.560 -16.760 1.00 34.91 C
ANISOU 3194 CB GLN A 428 6494 3453 3319 926 -185 -293 C
ATOM 3195 CG GLN A 428 17.102 -2.819 -17.486 1.00 44.19 C
ANISOU 3195 CG GLN A 428 7762 4623 4404 1057 -299 -226 C
ATOM 3196 CD GLN A 428 17.312 -2.797 -18.990 1.00 41.71 C
ANISOU 3196 CD GLN A 428 7374 4378 4097 1130 -458 -208 C
ATOM 3197 OE1 GLN A 428 17.524 -3.838 -19.616 1.00 40.20 O
ANISOU 3197 OE1 GLN A 428 7123 4215 3935 1124 -476 -220 O
ATOM 3198 NE2 GLN A 428 17.261 -1.608 -19.577 1.00 42.47 N
ANISOU 3198 NE2 GLN A 428 7446 4507 4182 1184 -563 -195 N
ATOM 3199 N HIS A 429 16.044 -2.933 -14.175 1.00 29.36 N
ANISOU 3199 N HIS A 429 6119 2571 2465 930 44 -239 N
ATOM 3200 CA HIS A 429 14.665 -3.072 -13.709 1.00 29.13 C
ANISOU 3200 CA HIS A 429 6252 2473 2344 986 99 -191 C
ATOM 3201 C HIS A 429 14.504 -3.974 -12.490 1.00 30.23 C
ANISOU 3201 C HIS A 429 6441 2551 2494 890 269 -217 C
ATOM 3202 O HIS A 429 13.368 -4.190 -12.053 1.00 38.72 O
ANISOU 3202 O HIS A 429 7657 3561 3495 929 331 -176 O
ATOM 3203 CB HIS A 429 13.723 -3.568 -14.820 1.00 24.46 C
ANISOU 3203 CB HIS A 429 5701 1900 1694 1093 8 -149 C
ATOM 3204 CG HIS A 429 13.265 -2.490 -15.756 1.00 30.27 C
ANISOU 3204 CG HIS A 429 6467 2672 2363 1214 -147 -105 C
ATOM 3205 ND1 HIS A 429 13.919 -2.201 -16.935 1.00 30.29 N
ANISOU 3205 ND1 HIS A 429 6355 2753 2402 1246 -287 -114 N
ATOM 3206 CD2 HIS A 429 12.218 -1.635 -15.687 1.00 32.44 C
ANISOU 3206 CD2 HIS A 429 6872 2920 2533 1310 -187 -56 C
ATOM 3207 CE1 HIS A 429 13.296 -1.212 -17.550 1.00 34.46 C
ANISOU 3207 CE1 HIS A 429 6860 3319 2914 1312 -382 -115 C
ATOM 3208 NE2 HIS A 429 12.260 -0.850 -16.814 1.00 34.69 N
ANISOU 3208 NE2 HIS A 429 7018 3292 2870 1347 -323 -91 N
ATOM 3209 N SER A 430 15.582 -4.516 -11.931 1.00 28.00 N
ANISOU 3209 N SER A 430 6053 2289 2295 767 345 -286 N
ATOM 3210 CA SER A 430 15.469 -5.153 -10.631 1.00 25.66 C
ANISOU 3210 CA SER A 430 5812 1937 2003 669 505 -313 C
ATOM 3211 C SER A 430 15.433 -4.081 -9.547 1.00 33.60 C
ANISOU 3211 C SER A 430 6904 2886 2978 647 566 -292 C
ATOM 3212 O SER A 430 15.757 -2.916 -9.783 1.00 40.94 O
ANISOU 3212 O SER A 430 7817 3836 3903 689 486 -276 O
ATOM 3213 CB SER A 430 16.630 -6.115 -10.388 1.00 31.82 C
ANISOU 3213 CB SER A 430 6448 2771 2872 545 557 -399 C
ATOM 3214 OG SER A 430 16.651 -7.151 -11.350 1.00 35.23 O
ANISOU 3214 OG SER A 430 6802 3253 3329 566 506 -422 O
ATOM 3215 N THR A 431 15.034 -4.476 -8.343 1.00 36.81 N
ANISOU 3215 N THR A 431 7404 3220 3362 579 710 -293 N
ATOM 3216 CA THR A 431 14.991 -3.554 -7.207 1.00 36.87 C
ANISOU 3216 CA THR A 431 7503 3167 3338 549 784 -274 C
ATOM 3217 C THR A 431 16.301 -3.715 -6.441 1.00 34.12 C
ANISOU 3217 C THR A 431 7046 2850 3068 410 850 -345 C
ATOM 3218 O THR A 431 16.424 -4.552 -5.547 1.00 36.34 O
ANISOU 3218 O THR A 431 7338 3103 3368 305 975 -378 O
ATOM 3219 CB THR A 431 13.773 -3.813 -6.326 1.00 37.61 C
ANISOU 3219 CB THR A 431 7779 3157 3354 558 905 -225 C
ATOM 3220 OG1 THR A 431 12.585 -3.726 -7.121 1.00 44.77 O
ANISOU 3220 OG1 THR A 431 8783 4046 4183 693 834 -161 O
ATOM 3221 CG2 THR A 431 13.691 -2.791 -5.186 1.00 42.64 C
ANISOU 3221 CG2 THR A 431 8522 3728 3952 538 976 -200 C
ATOM 3222 N LEU A 432 17.292 -2.908 -6.814 1.00 35.93 N
ANISOU 3222 N LEU A 432 7169 3142 3342 410 764 -368 N
ATOM 3223 CA LEU A 432 18.569 -2.877 -6.112 1.00 33.53 C
ANISOU 3223 CA LEU A 432 6765 2872 3102 290 814 -430 C
ATOM 3224 C LEU A 432 18.397 -2.239 -4.739 1.00 35.06 C
ANISOU 3224 C LEU A 432 7071 2989 3260 239 925 -412 C
ATOM 3225 O LEU A 432 17.868 -1.128 -4.623 1.00 41.81 O
ANISOU 3225 O LEU A 432 8021 3802 4063 316 897 -362 O
ATOM 3226 CB LEU A 432 19.610 -2.100 -6.921 1.00 33.56 C
ANISOU 3226 CB LEU A 432 6637 2957 3156 314 691 -453 C
ATOM 3227 CG LEU A 432 20.631 -2.903 -7.734 1.00 32.04 C
ANISOU 3227 CG LEU A 432 6277 2860 3037 273 633 -513 C
ATOM 3228 CD1 LEU A 432 21.715 -2.001 -8.308 1.00 30.54 C
ANISOU 3228 CD1 LEU A 432 5975 2736 2894 283 536 -532 C
ATOM 3229 CD2 LEU A 432 21.248 -3.989 -6.876 1.00 32.78 C
ANISOU 3229 CD2 LEU A 432 6321 2968 3166 142 743 -575 C
ATOM 3230 N LYS A 433 18.853 -2.937 -3.701 1.00 27.76 N
ANISOU 3230 N LYS A 433 6136 2049 2363 110 1049 -454 N
ATOM 3231 CA LYS A 433 18.746 -2.461 -2.329 1.00 38.30 C
ANISOU 3231 CA LYS A 433 7577 3307 3668 45 1170 -440 C
ATOM 3232 C LYS A 433 20.129 -2.373 -1.698 1.00 43.00 C
ANISOU 3232 C LYS A 433 8063 3952 4324 -76 1203 -501 C
ATOM 3233 O LYS A 433 20.928 -3.312 -1.803 1.00 40.43 O
ANISOU 3233 O LYS A 433 7617 3690 4054 -160 1214 -560 O
ATOM 3234 CB LYS A 433 17.841 -3.374 -1.496 1.00 38.80 C
ANISOU 3234 CB LYS A 433 7762 3285 3695 -7 1312 -423 C
ATOM 3235 CG LYS A 433 16.552 -2.703 -1.037 1.00 40.36 C
ANISOU 3235 CG LYS A 433 8155 3376 3801 74 1357 -345 C
ATOM 3236 CD LYS A 433 15.314 -3.390 -1.606 1.00 37.32 C
ANISOU 3236 CD LYS A 433 7857 2954 3367 155 1355 -302 C
ATOM 3237 CE LYS A 433 14.048 -2.658 -1.186 1.00 44.63 C
ANISOU 3237 CE LYS A 433 8984 3781 4192 247 1391 -219 C
ATOM 3238 NZ LYS A 433 12.826 -3.468 -1.417 1.00 52.30 N
ANISOU 3238 NZ LYS A 433 10063 4698 5109 300 1432 -178 N
ATOM 3239 N ARG A 434 20.400 -1.237 -1.052 1.00 40.73 N
ANISOU 3239 N ARG A 434 7177 3716 4581 -370 1065 -51 N
ATOM 3240 CA ARG A 434 21.606 -0.976 -0.269 1.00 35.02 C
ANISOU 3240 CA ARG A 434 6377 2923 4006 -453 1100 -141 C
ATOM 3241 C ARG A 434 22.874 -0.904 -1.111 1.00 35.09 C
ANISOU 3241 C ARG A 434 6179 3075 4078 -427 1028 -266 C
ATOM 3242 O ARG A 434 23.976 -1.084 -0.585 1.00 32.66 O
ANISOU 3242 O ARG A 434 5781 2775 3851 -517 1075 -361 O
ATOM 3243 CB ARG A 434 21.780 -2.013 0.845 1.00 43.37 C
ANISOU 3243 CB ARG A 434 7449 3948 5082 -664 1263 -155 C
ATOM 3244 CG ARG A 434 20.563 -2.116 1.740 1.00 52.92 C
ANISOU 3244 CG ARG A 434 8875 4999 6234 -720 1354 -8 C
ATOM 3245 CD ARG A 434 20.844 -2.856 3.031 1.00 71.39 C
ANISOU 3245 CD ARG A 434 11235 7243 8649 -946 1503 -23 C
ATOM 3246 NE ARG A 434 19.737 -2.700 3.971 1.00 84.30 N
ANISOU 3246 NE ARG A 434 13050 8732 10247 -963 1542 123 N
ATOM 3247 CZ ARG A 434 19.640 -1.708 4.852 1.00 92.97 C
ANISOU 3247 CZ ARG A 434 14245 9653 11424 -884 1464 154 C
ATOM 3248 NH1 ARG A 434 20.586 -0.783 4.922 1.00 94.26 N
ANISOU 3248 NH1 ARG A 434 14331 9783 11700 -781 1356 47 N
ATOM 3249 NH2 ARG A 434 18.596 -1.643 5.668 1.00 97.29 N
ANISOU 3249 NH2 ARG A 434 14962 10070 11935 -903 1494 295 N
ATOM 3250 N VAL A 435 22.747 -0.625 -2.411 1.00 31.60 N
ANISOU 3250 N VAL A 435 5672 2737 3599 -307 907 -267 N
ATOM 3251 CA VAL A 435 23.921 -0.504 -3.270 1.00 24.35 C
ANISOU 3251 CA VAL A 435 4577 1934 2740 -287 837 -358 C
ATOM 3252 C VAL A 435 24.684 0.789 -3.009 1.00 30.86 C
ANISOU 3252 C VAL A 435 5361 2683 3683 -224 790 -383 C
ATOM 3253 O VAL A 435 25.838 0.923 -3.435 1.00 24.33 O
ANISOU 3253 O VAL A 435 4397 1942 2908 -235 770 -452 O
ATOM 3254 CB VAL A 435 23.499 -0.600 -4.749 1.00 25.78 C
ANISOU 3254 CB VAL A 435 4713 2222 2860 -190 713 -348 C
ATOM 3255 CG1 VAL A 435 22.829 0.691 -5.201 1.00 26.89 C
ANISOU 3255 CG1 VAL A 435 4908 2281 3027 -42 581 -288 C
ATOM 3256 CG2 VAL A 435 24.686 -0.933 -5.632 1.00 23.29 C
ANISOU 3256 CG2 VAL A 435 4233 2031 2585 -211 665 -431 C
ATOM 3257 N THR A 436 24.074 1.749 -2.319 1.00 33.81 N
ANISOU 3257 N THR A 436 5852 2903 4090 -148 776 -327 N
ATOM 3258 CA THR A 436 24.681 3.052 -2.095 1.00 30.88 C
ANISOU 3258 CA THR A 436 5433 2474 3826 -56 729 -358 C
ATOM 3259 C THR A 436 25.261 3.195 -0.691 1.00 33.70 C
ANISOU 3259 C THR A 436 5843 2714 4246 -112 826 -413 C
ATOM 3260 O THR A 436 25.729 4.279 -0.330 1.00 45.00 O
ANISOU 3260 O THR A 436 7245 4094 5758 -20 799 -450 O
ATOM 3261 CB THR A 436 23.657 4.163 -2.366 1.00 35.63 C
ANISOU 3261 CB THR A 436 6110 2991 4437 109 613 -282 C
ATOM 3262 OG1 THR A 436 24.338 5.372 -2.713 1.00 40.52 O
ANISOU 3262 OG1 THR A 436 6597 3639 5161 207 543 -324 O
ATOM 3263 CG2 THR A 436 22.780 4.409 -1.144 1.00 35.89 C
ANISOU 3263 CG2 THR A 436 6351 2830 4458 139 650 -216 C
ATOM 3264 N GLU A 437 25.270 2.118 0.094 1.00 25.68 N
ANISOU 3264 N GLU A 437 4878 1679 3199 -259 927 -427 N
ATOM 3265 CA GLU A 437 25.750 2.151 1.468 1.00 24.32 C
ANISOU 3265 CA GLU A 437 4719 1436 3087 -322 980 -469 C
ATOM 3266 C GLU A 437 27.188 1.664 1.603 1.00 27.47 C
ANISOU 3266 C GLU A 437 4962 1967 3510 -406 1014 -592 C
ATOM 3267 O GLU A 437 27.698 1.565 2.723 1.00 27.40 O
ANISOU 3267 O GLU A 437 4956 1910 3546 -464 1046 -650 O
ATOM 3268 CB GLU A 437 24.816 1.330 2.358 1.00 28.32 C
ANISOU 3268 CB GLU A 437 5373 1831 3556 -440 1060 -398 C
ATOM 3269 CG GLU A 437 23.363 1.778 2.256 1.00 40.65 C
ANISOU 3269 CG GLU A 437 7116 3267 5061 -347 1025 -258 C
ATOM 3270 CD GLU A 437 22.419 0.875 3.014 1.00 48.88 C
ANISOU 3270 CD GLU A 437 8308 4220 6044 -480 1128 -164 C
ATOM 3271 OE1 GLU A 437 22.908 -0.010 3.741 1.00 48.40 O
ANISOU 3271 OE1 GLU A 437 8197 4179 6015 -650 1221 -220 O
ATOM 3272 OE2 GLU A 437 21.188 1.048 2.885 1.00 50.59 O
ANISOU 3272 OE2 GLU A 437 8687 4357 6177 -415 1113 -33 O
ATOM 3273 N PHE A 438 27.846 1.362 0.488 1.00 22.62 N
ANISOU 3273 N PHE A 438 4221 1511 2864 -405 993 -631 N
ATOM 3274 CA PHE A 438 29.269 1.034 0.439 1.00 24.34 C
ANISOU 3274 CA PHE A 438 4294 1870 3084 -450 1002 -732 C
ATOM 3275 C PHE A 438 29.675 1.038 -1.030 1.00 27.64 C
ANISOU 3275 C PHE A 438 4613 2422 3467 -406 952 -728 C
ATOM 3276 O PHE A 438 28.854 1.290 -1.918 1.00 26.76 O
ANISOU 3276 O PHE A 438 4540 2287 3340 -346 904 -662 O
ATOM 3277 CB PHE A 438 29.602 -0.306 1.118 1.00 31.03 C
ANISOU 3277 CB PHE A 438 5111 2768 3912 -603 1063 -790 C
ATOM 3278 CG PHE A 438 28.943 -1.517 0.485 1.00 33.38 C
ANISOU 3278 CG PHE A 438 5409 3129 4143 -689 1097 -767 C
ATOM 3279 CD1 PHE A 438 27.596 -1.517 0.155 1.00 32.78 C
ANISOU 3279 CD1 PHE A 438 5462 2963 4030 -673 1113 -676 C
ATOM 3280 CD2 PHE A 438 29.680 -2.667 0.239 1.00 34.21 C
ANISOU 3280 CD2 PHE A 438 5393 3389 4216 -774 1108 -844 C
ATOM 3281 CE1 PHE A 438 26.997 -2.624 -0.417 1.00 35.71 C
ANISOU 3281 CE1 PHE A 438 5819 3426 4323 -732 1143 -657 C
ATOM 3282 CE2 PHE A 438 29.084 -3.783 -0.335 1.00 36.18 C
ANISOU 3282 CE2 PHE A 438 5634 3711 4403 -839 1143 -848 C
ATOM 3283 CZ PHE A 438 27.740 -3.759 -0.662 1.00 34.54 C
ANISOU 3283 CZ PHE A 438 5536 3438 4150 -816 1164 -751 C
ATOM 3284 N SER A 439 30.956 0.780 -1.278 1.00 29.58 N
ANISOU 3284 N SER A 439 4741 2802 3696 -429 951 -796 N
ATOM 3285 CA SER A 439 31.464 0.658 -2.642 1.00 26.76 C
ANISOU 3285 CA SER A 439 4300 2565 3303 -406 905 -791 C
ATOM 3286 C SER A 439 31.125 -0.744 -3.118 1.00 22.90 C
ANISOU 3286 C SER A 439 3792 2155 2753 -478 889 -787 C
ATOM 3287 O SER A 439 31.920 -1.676 -2.994 1.00 27.08 O
ANISOU 3287 O SER A 439 4243 2796 3251 -536 891 -841 O
ATOM 3288 CB SER A 439 32.961 0.924 -2.690 1.00 20.95 C
ANISOU 3288 CB SER A 439 3470 1936 2552 -397 917 -853 C
ATOM 3289 OG SER A 439 33.227 2.278 -2.394 1.00 22.79 O
ANISOU 3289 OG SER A 439 3706 2119 2834 -313 946 -863 O
ATOM 3290 N ALA A 440 29.919 -0.890 -3.668 1.00 22.43 N
ANISOU 3290 N ALA A 440 3799 2049 2673 -453 861 -724 N
ATOM 3291 CA ALA A 440 29.381 -2.213 -3.960 1.00 26.74 C
ANISOU 3291 CA ALA A 440 4343 2665 3151 -509 870 -734 C
ATOM 3292 C ALA A 440 30.101 -2.909 -5.106 1.00 26.01 C
ANISOU 3292 C ALA A 440 4149 2717 3018 -492 798 -767 C
ATOM 3293 O ALA A 440 29.900 -4.113 -5.299 1.00 31.41 O
ANISOU 3293 O ALA A 440 4799 3488 3647 -527 804 -804 O
ATOM 3294 CB ALA A 440 27.890 -2.117 -4.282 1.00 28.95 C
ANISOU 3294 CB ALA A 440 4719 2883 3397 -458 845 -644 C
ATOM 3295 N PHE A 441 30.922 -2.192 -5.876 1.00 23.49 N
ANISOU 3295 N PHE A 441 3774 2424 2726 -436 728 -746 N
ATOM 3296 CA PHE A 441 31.584 -2.771 -7.041 1.00 25.59 C
ANISOU 3296 CA PHE A 441 3972 2794 2959 -413 643 -755 C
ATOM 3297 C PHE A 441 33.102 -2.647 -6.965 1.00 18.21 C
ANISOU 3297 C PHE A 441 2972 1929 2018 -431 653 -792 C
ATOM 3298 O PHE A 441 33.775 -2.725 -7.999 1.00 24.11 O
ANISOU 3298 O PHE A 441 3681 2731 2750 -401 575 -762 O
ATOM 3299 CB PHE A 441 31.068 -2.120 -8.328 1.00 27.69 C
ANISOU 3299 CB PHE A 441 4245 3021 3256 -336 529 -670 C
ATOM 3300 CG PHE A 441 29.572 -1.974 -8.381 1.00 24.17 C
ANISOU 3300 CG PHE A 441 3878 2503 2803 -293 506 -631 C
ATOM 3301 CD1 PHE A 441 28.762 -3.053 -8.701 1.00 24.88 C
ANISOU 3301 CD1 PHE A 441 4000 2637 2817 -279 489 -657 C
ATOM 3302 CD2 PHE A 441 28.975 -0.751 -8.113 1.00 21.89 C
ANISOU 3302 CD2 PHE A 441 3631 2116 2572 -250 499 -571 C
ATOM 3303 CE1 PHE A 441 27.381 -2.916 -8.748 1.00 22.24 C
ANISOU 3303 CE1 PHE A 441 3754 2250 2446 -228 473 -616 C
ATOM 3304 CE2 PHE A 441 27.598 -0.607 -8.159 1.00 22.13 C
ANISOU 3304 CE2 PHE A 441 3750 2082 2575 -195 465 -531 C
ATOM 3305 CZ PHE A 441 26.800 -1.691 -8.478 1.00 18.90 C
ANISOU 3305 CZ PHE A 441 3389 1719 2072 -186 455 -548 C
ATOM 3306 N LEU A 442 33.655 -2.481 -5.759 1.00 16.44 N
ANISOU 3306 N LEU A 442 2742 1703 1800 -474 736 -847 N
ATOM 3307 CA LEU A 442 35.076 -2.165 -5.617 1.00 16.65 C
ANISOU 3307 CA LEU A 442 2724 1802 1801 -470 749 -881 C
ATOM 3308 C LEU A 442 35.977 -3.255 -6.189 1.00 19.50 C
ANISOU 3308 C LEU A 442 3028 2289 2093 -470 683 -911 C
ATOM 3309 O LEU A 442 37.073 -2.955 -6.676 1.00 26.91 O
ANISOU 3309 O LEU A 442 3958 3288 2978 -450 673 -910 O
ATOM 3310 CB LEU A 442 35.412 -1.926 -4.145 1.00 17.41 C
ANISOU 3310 CB LEU A 442 2815 1877 1924 -495 810 -930 C
ATOM 3311 CG LEU A 442 36.807 -1.392 -3.819 1.00 18.91 C
ANISOU 3311 CG LEU A 442 2974 2137 2075 -468 832 -973 C
ATOM 3312 CD1 LEU A 442 37.022 -0.016 -4.426 1.00 24.86 C
ANISOU 3312 CD1 LEU A 442 3745 2871 2832 -415 883 -938 C
ATOM 3313 CD2 LEU A 442 37.007 -1.345 -2.320 1.00 21.12 C
ANISOU 3313 CD2 LEU A 442 3261 2379 2383 -489 866 -1044 C
ATOM 3314 N SER A 443 35.547 -4.518 -6.140 1.00 19.36 N
ANISOU 3314 N SER A 443 2974 2316 2064 -486 644 -938 N
ATOM 3315 CA SER A 443 36.395 -5.602 -6.628 1.00 20.25 C
ANISOU 3315 CA SER A 443 3031 2547 2117 -462 569 -981 C
ATOM 3316 C SER A 443 36.440 -5.685 -8.148 1.00 16.96 C
ANISOU 3316 C SER A 443 2647 2137 1659 -407 484 -950 C
ATOM 3317 O SER A 443 37.364 -6.302 -8.690 1.00 21.97 O
ANISOU 3317 O SER A 443 3266 2853 2229 -373 415 -979 O
ATOM 3318 CB SER A 443 35.914 -6.944 -6.080 1.00 18.13 C
ANISOU 3318 CB SER A 443 2698 2336 1856 -494 566 -1040 C
ATOM 3319 OG SER A 443 35.884 -6.936 -4.666 1.00 25.13 O
ANISOU 3319 OG SER A 443 3567 3198 2785 -575 645 -1086 O
ATOM 3320 N LEU A 444 35.476 -5.075 -8.843 1.00 17.00 N
ANISOU 3320 N LEU A 444 2701 2049 1708 -390 466 -881 N
ATOM 3321 CA LEU A 444 35.231 -5.347 -10.262 1.00 15.70 C
ANISOU 3321 CA LEU A 444 2551 1868 1546 -324 341 -825 C
ATOM 3322 C LEU A 444 36.098 -4.447 -11.145 1.00 19.73 C
ANISOU 3322 C LEU A 444 3072 2343 2081 -310 284 -714 C
ATOM 3323 O LEU A 444 35.624 -3.572 -11.875 1.00 25.59 O
ANISOU 3323 O LEU A 444 3831 2997 2896 -302 241 -622 O
ATOM 3324 CB LEU A 444 33.750 -5.184 -10.571 1.00 15.45 C
ANISOU 3324 CB LEU A 444 2558 1759 1555 -301 322 -797 C
ATOM 3325 CG LEU A 444 32.883 -6.164 -9.777 1.00 18.23 C
ANISOU 3325 CG LEU A 444 2902 2159 1864 -324 394 -885 C
ATOM 3326 CD1 LEU A 444 31.436 -6.104 -10.237 1.00 17.46 C
ANISOU 3326 CD1 LEU A 444 2860 2006 1768 -277 366 -853 C
ATOM 3327 CD2 LEU A 444 33.437 -7.570 -9.917 1.00 17.51 C
ANISOU 3327 CD2 LEU A 444 2735 2195 1722 -294 349 -963 C
ATOM 3328 N GLU A 445 37.403 -4.712 -11.093 1.00 18.73 N
ANISOU 3328 N GLU A 445 2933 2296 1889 -310 282 -724 N
ATOM 3329 CA GLU A 445 38.367 -3.904 -11.828 1.00 18.89 C
ANISOU 3329 CA GLU A 445 2966 2302 1910 -312 257 -604 C
ATOM 3330 C GLU A 445 38.489 -4.296 -13.296 1.00 23.17 C
ANISOU 3330 C GLU A 445 3548 2790 2465 -271 109 -529 C
ATOM 3331 O GLU A 445 39.239 -3.643 -14.028 1.00 25.19 O
ANISOU 3331 O GLU A 445 3823 3015 2733 -292 85 -405 O
ATOM 3332 CB GLU A 445 39.738 -3.993 -11.156 1.00 31.26 C
ANISOU 3332 CB GLU A 445 4525 3980 3373 -319 317 -637 C
ATOM 3333 CG GLU A 445 39.729 -3.650 -9.676 1.00 49.46 C
ANISOU 3333 CG GLU A 445 6801 6323 5667 -353 446 -734 C
ATOM 3334 CD GLU A 445 41.054 -3.089 -9.201 1.00 59.98 C
ANISOU 3334 CD GLU A 445 8135 7744 6912 -351 516 -728 C
ATOM 3335 OE1 GLU A 445 41.325 -1.902 -9.479 1.00 64.03 O
ANISOU 3335 OE1 GLU A 445 8638 8240 7449 -360 573 -622 O
ATOM 3336 OE2 GLU A 445 41.826 -3.829 -8.560 1.00 62.77 O
ANISOU 3336 OE2 GLU A 445 8489 8195 7167 -337 512 -836 O
ATOM 3337 N LYS A 446 37.785 -5.336 -13.741 1.00 21.94 N
ANISOU 3337 N LYS A 446 3409 2621 2307 -213 13 -600 N
ATOM 3338 CA LYS A 446 37.738 -5.707 -15.149 1.00 23.67 C
ANISOU 3338 CA LYS A 446 3681 2759 2552 -156 -147 -549 C
ATOM 3339 C LYS A 446 36.354 -5.506 -15.747 1.00 16.86 C
ANISOU 3339 C LYS A 446 2836 1795 1774 -134 -212 -553 C
ATOM 3340 O LYS A 446 36.120 -5.898 -16.897 1.00 17.31 O
ANISOU 3340 O LYS A 446 2944 1772 1859 -74 -361 -544 O
ATOM 3341 CB LYS A 446 38.184 -7.158 -15.331 1.00 24.92 C
ANISOU 3341 CB LYS A 446 3850 2996 2623 -67 -236 -646 C
ATOM 3342 CG LYS A 446 39.669 -7.370 -15.124 1.00 34.69 C
ANISOU 3342 CG LYS A 446 5099 4314 3766 -61 -233 -621 C
ATOM 3343 CD LYS A 446 39.955 -8.731 -14.518 1.00 42.06 C
ANISOU 3343 CD LYS A 446 5985 5387 4608 7 -256 -779 C
ATOM 3344 CE LYS A 446 40.814 -8.603 -13.273 1.00 50.31 C
ANISOU 3344 CE LYS A 446 6985 6554 5577 -44 -143 -830 C
ATOM 3345 NZ LYS A 446 41.041 -9.925 -12.635 1.00 48.81 N
ANISOU 3345 NZ LYS A 446 6723 6506 5318 7 -174 -1001 N
ATOM 3346 N LEU A 447 35.433 -4.908 -14.993 1.00 16.27 N
ANISOU 3346 N LEU A 447 2733 1716 1734 -170 -116 -573 N
ATOM 3347 CA LEU A 447 34.063 -4.739 -15.454 1.00 19.92 C
ANISOU 3347 CA LEU A 447 3221 2099 2247 -134 -179 -586 C
ATOM 3348 C LEU A 447 34.006 -3.729 -16.594 1.00 22.49 C
ANISOU 3348 C LEU A 447 3567 2295 2684 -154 -288 -478 C
ATOM 3349 O LEU A 447 34.508 -2.609 -16.469 1.00 19.87 O
ANISOU 3349 O LEU A 447 3194 1941 2414 -228 -229 -383 O
ATOM 3350 CB LEU A 447 33.170 -4.278 -14.301 1.00 15.64 C
ANISOU 3350 CB LEU A 447 2662 1576 1705 -164 -50 -614 C
ATOM 3351 CG LEU A 447 31.661 -4.290 -14.546 1.00 18.27 C
ANISOU 3351 CG LEU A 447 3037 1860 2044 -110 -98 -642 C
ATOM 3352 CD1 LEU A 447 31.183 -5.715 -14.747 1.00 21.30 C
ANISOU 3352 CD1 LEU A 447 3439 2317 2338 -35 -133 -747 C
ATOM 3353 CD2 LEU A 447 30.917 -3.633 -13.393 1.00 15.42 C
ANISOU 3353 CD2 LEU A 447 2681 1492 1687 -144 27 -633 C
ATOM 3354 N LEU A 448 33.384 -4.125 -17.706 1.00 16.95 N
ANISOU 3354 N LEU A 448 2919 1510 2012 -87 -447 -501 N
ATOM 3355 CA LEU A 448 33.235 -3.268 -18.878 1.00 17.62 C
ANISOU 3355 CA LEU A 448 3023 1451 2222 -115 -581 -417 C
ATOM 3356 C LEU A 448 31.852 -2.653 -19.000 1.00 18.13 C
ANISOU 3356 C LEU A 448 3091 1458 2340 -87 -632 -446 C
ATOM 3357 O LEU A 448 31.713 -1.564 -19.570 1.00 20.99 O
ANISOU 3357 O LEU A 448 3424 1727 2825 -142 -696 -372 O
ATOM 3358 CB LEU A 448 33.507 -4.062 -20.160 1.00 21.99 C
ANISOU 3358 CB LEU A 448 3654 1914 2787 -52 -764 -431 C
ATOM 3359 CG LEU A 448 34.593 -5.138 -20.140 1.00 29.05 C
ANISOU 3359 CG LEU A 448 4576 2872 3589 -10 -767 -450 C
ATOM 3360 CD1 LEU A 448 34.465 -6.030 -21.362 1.00 30.10 C
ANISOU 3360 CD1 LEU A 448 4801 2905 3731 101 -971 -504 C
ATOM 3361 CD2 LEU A 448 35.962 -4.503 -20.092 1.00 32.33 C
ANISOU 3361 CD2 LEU A 448 4976 3287 4022 -112 -701 -307 C
ATOM 3362 N TYR A 449 30.828 -3.331 -18.489 1.00 17.22 N
ANISOU 3362 N TYR A 449 3007 1404 2131 -4 -605 -551 N
ATOM 3363 CA TYR A 449 29.438 -2.993 -18.764 1.00 17.48 C
ANISOU 3363 CA TYR A 449 3080 1388 2175 58 -686 -592 C
ATOM 3364 C TYR A 449 28.645 -3.103 -17.471 1.00 21.01 C
ANISOU 3364 C TYR A 449 3530 1930 2524 76 -532 -628 C
ATOM 3365 O TYR A 449 28.595 -4.177 -16.862 1.00 19.18 O
ANISOU 3365 O TYR A 449 3307 1801 2180 104 -441 -696 O
ATOM 3366 CB TYR A 449 28.883 -3.934 -19.837 1.00 18.63 C
ANISOU 3366 CB TYR A 449 3304 1494 2282 175 -857 -688 C
ATOM 3367 CG TYR A 449 27.473 -3.657 -20.296 1.00 21.58 C
ANISOU 3367 CG TYR A 449 3716 1838 2647 259 -956 -728 C
ATOM 3368 CD1 TYR A 449 26.384 -3.995 -19.504 1.00 21.33 C
ANISOU 3368 CD1 TYR A 449 3710 1908 2489 324 -859 -777 C
ATOM 3369 CD2 TYR A 449 27.227 -3.096 -21.541 1.00 19.73 C
ANISOU 3369 CD2 TYR A 449 3482 1490 2523 271 -1138 -700 C
ATOM 3370 CE1 TYR A 449 25.091 -3.758 -19.927 1.00 28.45 C
ANISOU 3370 CE1 TYR A 449 4652 2799 3359 414 -948 -799 C
ATOM 3371 CE2 TYR A 449 25.936 -2.852 -21.972 1.00 25.79 C
ANISOU 3371 CE2 TYR A 449 4276 2254 3271 360 -1234 -736 C
ATOM 3372 CZ TYR A 449 24.873 -3.186 -21.161 1.00 27.37 C
ANISOU 3372 CZ TYR A 449 4515 2557 3328 439 -1142 -787 C
ATOM 3373 OH TYR A 449 23.582 -2.951 -21.583 1.00 26.08 O
ANISOU 3373 OH TYR A 449 4398 2389 3123 540 -1246 -822 O
ATOM 3374 N LEU A 450 28.024 -2.002 -17.056 1.00 19.90 N
ANISOU 3374 N LEU A 450 3378 1751 2431 58 -507 -580 N
ATOM 3375 CA LEU A 450 27.169 -1.981 -15.877 1.00 20.51 C
ANISOU 3375 CA LEU A 450 3488 1880 2425 77 -379 -594 C
ATOM 3376 C LEU A 450 25.858 -1.294 -16.224 1.00 21.53 C
ANISOU 3376 C LEU A 450 3674 1946 2559 155 -488 -593 C
ATOM 3377 O LEU A 450 25.857 -0.179 -16.756 1.00 19.53 O
ANISOU 3377 O LEU A 450 3379 1613 2427 142 -590 -548 O
ATOM 3378 CB LEU A 450 27.848 -1.265 -14.704 1.00 16.31 C
ANISOU 3378 CB LEU A 450 2899 1366 1933 -9 -221 -536 C
ATOM 3379 CG LEU A 450 26.976 -1.098 -13.456 1.00 16.36 C
ANISOU 3379 CG LEU A 450 2959 1382 1878 4 -101 -534 C
ATOM 3380 CD1 LEU A 450 26.542 -2.450 -12.904 1.00 17.42 C
ANISOU 3380 CD1 LEU A 450 3144 1598 1877 13 -10 -597 C
ATOM 3381 CD2 LEU A 450 27.701 -0.287 -12.394 1.00 16.16 C
ANISOU 3381 CD2 LEU A 450 2881 1348 1909 -63 27 -494 C
ATOM 3382 N ASP A 451 24.749 -1.966 -15.932 1.00 23.29 N
ANISOU 3382 N ASP A 451 3986 2215 2646 235 -466 -643 N
ATOM 3383 CA ASP A 451 23.415 -1.414 -16.140 1.00 27.59 C
ANISOU 3383 CA ASP A 451 4613 2720 3152 331 -563 -645 C
ATOM 3384 C ASP A 451 22.650 -1.524 -14.828 1.00 26.15 C
ANISOU 3384 C ASP A 451 4502 2581 2852 339 -400 -611 C
ATOM 3385 O ASP A 451 22.309 -2.630 -14.392 1.00 25.86 O
ANISOU 3385 O ASP A 451 4512 2634 2680 348 -292 -646 O
ATOM 3386 CB ASP A 451 22.683 -2.140 -17.268 1.00 24.24 C
ANISOU 3386 CB ASP A 451 4260 2304 2648 446 -722 -738 C
ATOM 3387 CG ASP A 451 21.417 -1.426 -17.691 1.00 32.47 C
ANISOU 3387 CG ASP A 451 5381 3295 3660 553 -870 -751 C
ATOM 3388 OD1 ASP A 451 21.078 -0.402 -17.064 1.00 34.67 O
ANISOU 3388 OD1 ASP A 451 5659 3536 3977 543 -846 -681 O
ATOM 3389 OD2 ASP A 451 20.760 -1.880 -18.650 1.00 32.46 O
ANISOU 3389 OD2 ASP A 451 5423 3307 3602 655 -1010 -819 O
ATOM 3390 N ILE A 452 22.393 -0.378 -14.201 1.00 23.43 N
ANISOU 3390 N ILE A 452 4164 2172 2566 333 -383 -542 N
ATOM 3391 CA ILE A 452 21.562 -0.315 -13.005 1.00 20.87 C
ANISOU 3391 CA ILE A 452 3940 1847 2142 351 -259 -492 C
ATOM 3392 C ILE A 452 20.363 0.579 -13.298 1.00 25.78 C
ANISOU 3392 C ILE A 452 4649 2409 2738 474 -401 -467 C
ATOM 3393 O ILE A 452 19.810 1.221 -12.395 1.00 26.04 O
ANISOU 3393 O ILE A 452 4753 2390 2750 502 -350 -401 O
ATOM 3394 CB ILE A 452 22.354 0.209 -11.796 1.00 20.86 C
ANISOU 3394 CB ILE A 452 3891 1811 2225 254 -108 -440 C
ATOM 3395 CG1 ILE A 452 22.933 1.589 -12.104 1.00 18.75 C
ANISOU 3395 CG1 ILE A 452 3522 1479 2124 255 -197 -414 C
ATOM 3396 CG2 ILE A 452 23.458 -0.775 -11.420 1.00 18.03 C
ANISOU 3396 CG2 ILE A 452 3461 1525 1865 143 26 -478 C
ATOM 3397 CD1 ILE A 452 23.275 2.393 -10.882 1.00 24.87 C
ANISOU 3397 CD1 ILE A 452 4284 2204 2959 226 -80 -369 C
ATOM 3398 N SER A 453 19.953 0.629 -14.564 1.00 21.19 N
ANISOU 3398 N SER A 453 4070 1824 2159 556 -597 -527 N
ATOM 3399 CA SER A 453 18.851 1.497 -14.953 1.00 26.80 C
ANISOU 3399 CA SER A 453 4851 2484 2850 682 -769 -525 C
ATOM 3400 C SER A 453 17.542 1.013 -14.347 1.00 29.56 C
ANISOU 3400 C SER A 453 5382 2873 2975 782 -709 -497 C
ATOM 3401 O SER A 453 17.286 -0.192 -14.261 1.00 32.94 O
ANISOU 3401 O SER A 453 5875 3391 3250 782 -605 -524 O
ATOM 3402 CB SER A 453 18.724 1.559 -16.474 1.00 32.36 C
ANISOU 3402 CB SER A 453 5520 3166 3608 740 -1006 -615 C
ATOM 3403 OG SER A 453 19.817 2.249 -17.055 1.00 33.77 O
ANISOU 3403 OG SER A 453 5538 3287 4006 642 -1075 -611 O
ATOM 3404 N TYR A 454 16.715 1.970 -13.922 1.00 24.17 N
ANISOU 3404 N TYR A 454 4782 2133 2271 871 -772 -440 N
ATOM 3405 CA TYR A 454 15.369 1.696 -13.417 1.00 27.61 C
ANISOU 3405 CA TYR A 454 5418 2592 2481 983 -742 -391 C
ATOM 3406 C TYR A 454 15.400 0.696 -12.266 1.00 26.15 C
ANISOU 3406 C TYR A 454 5307 2453 2175 888 -473 -321 C
ATOM 3407 O TYR A 454 14.560 -0.199 -12.169 1.00 31.48 O
ANISOU 3407 O TYR A 454 6109 3213 2640 932 -397 -310 O
ATOM 3408 CB TYR A 454 14.443 1.211 -14.538 1.00 26.68 C
ANISOU 3408 CB TYR A 454 5385 2542 2209 1122 -908 -481 C
ATOM 3409 CG TYR A 454 14.504 2.076 -15.773 1.00 35.10 C
ANISOU 3409 CG TYR A 454 6361 3554 3423 1187 -1188 -573 C
ATOM 3410 CD1 TYR A 454 13.870 3.311 -15.809 1.00 32.65 C
ANISOU 3410 CD1 TYR A 454 6073 3177 3157 1291 -1361 -554 C
ATOM 3411 CD2 TYR A 454 15.202 1.662 -16.898 1.00 39.71 C
ANISOU 3411 CD2 TYR A 454 6833 4144 4111 1141 -1288 -678 C
ATOM 3412 CE1 TYR A 454 13.933 4.114 -16.932 1.00 30.21 C
ANISOU 3412 CE1 TYR A 454 5654 2821 3003 1330 -1621 -644 C
ATOM 3413 CE2 TYR A 454 15.271 2.453 -18.026 1.00 34.82 C
ANISOU 3413 CE2 TYR A 454 6128 3454 3647 1173 -1543 -755 C
ATOM 3414 CZ TYR A 454 14.632 3.678 -18.040 1.00 32.22 C
ANISOU 3414 CZ TYR A 454 5800 3071 3369 1258 -1707 -741 C
ATOM 3415 OH TYR A 454 14.699 4.471 -19.164 1.00 39.23 O
ANISOU 3415 OH TYR A 454 6580 3894 4433 1271 -1966 -826 O
ATOM 3416 N THR A 455 16.391 0.845 -11.392 1.00 24.40 N
ANISOU 3416 N THR A 455 4998 2184 2088 750 -326 -279 N
ATOM 3417 CA THR A 455 16.483 0.052 -10.175 1.00 31.70 C
ANISOU 3417 CA THR A 455 5981 3125 2941 637 -83 -214 C
ATOM 3418 C THR A 455 15.960 0.793 -8.952 1.00 32.73 C
ANISOU 3418 C THR A 455 6245 3132 3061 649 -15 -95 C
ATOM 3419 O THR A 455 16.068 0.273 -7.836 1.00 38.68 O
ANISOU 3419 O THR A 455 7052 3859 3786 536 180 -33 O
ATOM 3420 CB THR A 455 17.932 -0.383 -9.932 1.00 24.09 C
ANISOU 3420 CB THR A 455 4849 2184 2119 479 31 -263 C
ATOM 3421 OG1 THR A 455 18.780 0.771 -9.935 1.00 30.45 O
ANISOU 3421 OG1 THR A 455 5547 2904 3119 464 -43 -266 O
ATOM 3422 CG2 THR A 455 18.389 -1.344 -11.023 1.00 22.19 C
ANISOU 3422 CG2 THR A 455 4509 2062 1861 471 -16 -369 C
ATOM 3423 N ASN A 456 15.384 1.983 -9.141 1.00 35.41 N
ANISOU 3423 N ASN A 456 6640 3388 3428 788 -184 -67 N
ATOM 3424 CA ASN A 456 14.941 2.838 -8.039 1.00 39.72 C
ANISOU 3424 CA ASN A 456 7312 3795 3983 833 -158 39 C
ATOM 3425 C ASN A 456 16.073 3.079 -7.044 1.00 36.46 C
ANISOU 3425 C ASN A 456 6810 3303 3742 700 -19 45 C
ATOM 3426 O ASN A 456 15.885 3.025 -5.827 1.00 35.81 O
ANISOU 3426 O ASN A 456 6854 3118 3635 651 115 129 O
ATOM 3427 CB ASN A 456 13.702 2.259 -7.353 1.00 43.82 C
ANISOU 3427 CB ASN A 456 8076 4300 4272 866 -57 157 C
ATOM 3428 CG ASN A 456 12.535 2.110 -8.305 1.00 59.77 C
ANISOU 3428 CG ASN A 456 10204 6410 6096 1029 -204 145 C
ATOM 3429 OD1 ASN A 456 12.011 3.099 -8.813 1.00 61.20 O
ANISOU 3429 OD1 ASN A 456 10415 6552 6287 1192 -420 131 O
ATOM 3430 ND2 ASN A 456 12.120 0.874 -8.553 1.00 67.45 N
ANISOU 3430 ND2 ASN A 456 11228 7515 6886 994 -95 138 N
ATOM 3431 N THR A 457 17.262 3.339 -7.578 1.00 31.13 N
ANISOU 3431 N THR A 457 5925 2669 3234 642 -54 -47 N
ATOM 3432 CA THR A 457 18.433 3.657 -6.776 1.00 25.63 C
ANISOU 3432 CA THR A 457 5127 1919 2691 539 56 -65 C
ATOM 3433 C THR A 457 18.514 5.165 -6.584 1.00 27.35 C
ANISOU 3433 C THR A 457 5305 2046 3042 653 -55 -60 C
ATOM 3434 O THR A 457 18.415 5.928 -7.551 1.00 29.57 O
ANISOU 3434 O THR A 457 5487 2363 3387 747 -228 -96 O
ATOM 3435 CB THR A 457 19.706 3.137 -7.449 1.00 25.47 C
ANISOU 3435 CB THR A 457 4911 2008 2759 426 84 -156 C
ATOM 3436 OG1 THR A 457 19.667 1.708 -7.511 1.00 30.07 O
ANISOU 3436 OG1 THR A 457 5519 2681 3225 333 192 -174 O
ATOM 3437 CG2 THR A 457 20.945 3.569 -6.681 1.00 28.47 C
ANISOU 3437 CG2 THR A 457 5188 2352 3280 343 183 -185 C
ATOM 3438 N LYS A 458 18.672 5.594 -5.339 1.00 27.63 N
ANISOU 3438 N LYS A 458 5412 1961 3125 646 38 -23 N
ATOM 3439 CA LYS A 458 18.876 7.001 -5.011 1.00 32.26 C
ANISOU 3439 CA LYS A 458 5945 2468 3846 764 -45 -35 C
ATOM 3440 C LYS A 458 20.345 7.159 -4.634 1.00 28.49 C
ANISOU 3440 C LYS A 458 5302 2017 3507 662 65 -111 C
ATOM 3441 O LYS A 458 20.752 6.816 -3.522 1.00 30.34 O
ANISOU 3441 O LYS A 458 5607 2173 3747 582 207 -111 O
ATOM 3442 CB LYS A 458 17.941 7.445 -3.892 1.00 28.06 C
ANISOU 3442 CB LYS A 458 5637 1765 3259 868 -44 54 C
ATOM 3443 CG LYS A 458 17.926 8.948 -3.654 1.00 38.62 C
ANISOU 3443 CG LYS A 458 6927 3026 4719 1044 -169 33 C
ATOM 3444 CD LYS A 458 16.732 9.354 -2.799 1.00 41.22 C
ANISOU 3444 CD LYS A 458 7491 3209 4964 1176 -220 135 C
ATOM 3445 CE LYS A 458 16.773 10.830 -2.440 1.00 46.58 C
ANISOU 3445 CE LYS A 458 8075 3851 5773 1340 -335 98 C
ATOM 3446 NZ LYS A 458 15.564 11.242 -1.681 1.00 52.72 N
ANISOU 3446 NZ LYS A 458 9043 4528 6459 1456 -403 194 N
ATOM 3447 N ILE A 459 21.141 7.667 -5.573 1.00 24.35 N
ANISOU 3447 N ILE A 459 4560 1601 3089 660 -3 -174 N
ATOM 3448 CA ILE A 459 22.575 7.801 -5.353 1.00 27.94 C
ANISOU 3448 CA ILE A 459 4856 2112 3647 569 103 -240 C
ATOM 3449 C ILE A 459 22.821 8.823 -4.251 1.00 28.44 C
ANISOU 3449 C ILE A 459 4933 2079 3795 660 140 -260 C
ATOM 3450 O ILE A 459 22.384 9.977 -4.341 1.00 27.21 O
ANISOU 3450 O ILE A 459 4740 1893 3707 813 26 -257 O
ATOM 3451 CB ILE A 459 23.284 8.197 -6.657 1.00 30.05 C
ANISOU 3451 CB ILE A 459 4902 2511 4005 547 21 -276 C
ATOM 3452 CG1 ILE A 459 22.759 7.368 -7.833 1.00 25.98 C
ANISOU 3452 CG1 ILE A 459 4404 2053 3413 510 -73 -263 C
ATOM 3453 CG2 ILE A 459 24.790 8.042 -6.516 1.00 23.91 C
ANISOU 3453 CG2 ILE A 459 3988 1814 3283 433 150 -326 C
ATOM 3454 CD1 ILE A 459 23.317 5.974 -7.913 1.00 35.11 C
ANISOU 3454 CD1 ILE A 459 5580 3269 4489 371 36 -280 C
ATOM 3455 N ASP A 460 23.517 8.394 -3.191 1.00 31.23 N
ANISOU 3455 N ASP A 460 5337 2382 4147 575 288 -294 N
ATOM 3456 CA ASP A 460 23.808 9.253 -2.048 1.00 36.06 C
ANISOU 3456 CA ASP A 460 5984 2885 4834 663 329 -335 C
ATOM 3457 C ASP A 460 25.226 9.020 -1.534 1.00 30.42 C
ANISOU 3457 C ASP A 460 5175 2227 4157 563 465 -429 C
ATOM 3458 O ASP A 460 25.547 9.417 -0.408 1.00 29.50 O
ANISOU 3458 O ASP A 460 5122 2004 4081 608 522 -484 O
ATOM 3459 CB ASP A 460 22.782 9.017 -0.928 1.00 41.91 C
ANISOU 3459 CB ASP A 460 6987 3420 5515 698 343 -270 C
ATOM 3460 CG ASP A 460 22.523 10.256 -0.088 1.00 66.11 C
ANISOU 3460 CG ASP A 460 10106 6353 8660 878 284 -284 C
ATOM 3461 OD1 ASP A 460 23.495 10.925 0.318 1.00 71.61 O
ANISOU 3461 OD1 ASP A 460 10695 7063 9450 925 328 -384 O
ATOM 3462 OD2 ASP A 460 21.340 10.560 0.175 1.00 76.26 O
ANISOU 3462 OD2 ASP A 460 11522 7551 9904 973 189 -197 O
ATOM 3463 N PHE A 461 26.079 8.377 -2.326 1.00 25.59 N
ANISOU 3463 N PHE A 461 4426 1771 3524 440 506 -453 N
ATOM 3464 CA PHE A 461 27.449 8.085 -1.922 1.00 24.91 C
ANISOU 3464 CA PHE A 461 4258 1761 3447 351 623 -540 C
ATOM 3465 C PHE A 461 28.355 8.328 -3.117 1.00 26.04 C
ANISOU 3465 C PHE A 461 4191 2090 3614 322 608 -546 C
ATOM 3466 O PHE A 461 28.217 7.659 -4.144 1.00 22.58 O
ANISOU 3466 O PHE A 461 3718 1724 3139 249 560 -499 O
ATOM 3467 CB PHE A 461 27.578 6.642 -1.422 1.00 24.41 C
ANISOU 3467 CB PHE A 461 4297 1674 3303 192 710 -555 C
ATOM 3468 CG PHE A 461 28.975 6.253 -1.015 1.00 22.32 C
ANISOU 3468 CG PHE A 461 3955 1494 3032 106 808 -657 C
ATOM 3469 CD1 PHE A 461 29.766 7.114 -0.267 1.00 23.26 C
ANISOU 3469 CD1 PHE A 461 4039 1597 3200 181 853 -744 C
ATOM 3470 CD2 PHE A 461 29.488 5.014 -1.363 1.00 21.27 C
ANISOU 3470 CD2 PHE A 461 3789 1461 2832 -32 847 -676 C
ATOM 3471 CE1 PHE A 461 31.050 6.748 0.114 1.00 27.39 C
ANISOU 3471 CE1 PHE A 461 4505 2208 3693 115 935 -846 C
ATOM 3472 CE2 PHE A 461 30.768 4.643 -0.986 1.00 28.08 C
ANISOU 3472 CE2 PHE A 461 4588 2406 3673 -98 918 -773 C
ATOM 3473 CZ PHE A 461 31.550 5.511 -0.248 1.00 30.08 C
ANISOU 3473 CZ PHE A 461 4819 2647 3964 -26 962 -858 C
ATOM 3474 N ASP A 462 29.271 9.290 -2.983 1.00 23.05 N
ANISOU 3474 N ASP A 462 3678 1785 3295 384 651 -600 N
ATOM 3475 CA ASP A 462 30.181 9.614 -4.076 1.00 24.22 C
ANISOU 3475 CA ASP A 462 3627 2106 3468 344 656 -585 C
ATOM 3476 C ASP A 462 31.097 8.451 -4.437 1.00 29.12 C
ANISOU 3476 C ASP A 462 4238 2820 4005 197 718 -590 C
ATOM 3477 O ASP A 462 31.575 8.385 -5.575 1.00 30.55 O
ANISOU 3477 O ASP A 462 4305 3110 4192 138 690 -540 O
ATOM 3478 CB ASP A 462 31.018 10.846 -3.721 1.00 26.13 C
ANISOU 3478 CB ASP A 462 3729 2429 3770 441 723 -644 C
ATOM 3479 CG ASP A 462 30.235 12.141 -3.846 1.00 35.97 C
ANISOU 3479 CG ASP A 462 4901 3645 5122 595 633 -630 C
ATOM 3480 OD1 ASP A 462 29.012 12.070 -4.080 1.00 36.29 O
ANISOU 3480 OD1 ASP A 462 5031 3581 5177 635 512 -577 O
ATOM 3481 OD2 ASP A 462 30.842 13.227 -3.718 1.00 37.18 O
ANISOU 3481 OD2 ASP A 462 4900 3892 5336 686 682 -677 O
ATOM 3482 N GLY A 463 31.352 7.537 -3.506 1.00 23.58 N
ANISOU 3482 N GLY A 463 3654 2072 3234 135 789 -652 N
ATOM 3483 CA GLY A 463 32.184 6.384 -3.770 1.00 20.64 C
ANISOU 3483 CA GLY A 463 3272 1790 2780 13 831 -672 C
ATOM 3484 C GLY A 463 31.460 5.174 -4.323 1.00 20.97 C
ANISOU 3484 C GLY A 463 3383 1810 2773 -67 773 -628 C
ATOM 3485 O GLY A 463 32.003 4.065 -4.265 1.00 25.40 O
ANISOU 3485 O GLY A 463 3958 2427 3266 -157 807 -667 O
ATOM 3486 N ILE A 464 30.256 5.353 -4.875 1.00 21.48 N
ANISOU 3486 N ILE A 464 3487 1811 2865 -22 681 -557 N
ATOM 3487 CA ILE A 464 29.449 4.206 -5.287 1.00 19.27 C
ANISOU 3487 CA ILE A 464 3287 1514 2520 -75 637 -528 C
ATOM 3488 C ILE A 464 30.126 3.421 -6.405 1.00 19.77 C
ANISOU 3488 C ILE A 464 3270 1696 2547 -141 601 -523 C
ATOM 3489 O ILE A 464 29.924 2.206 -6.530 1.00 21.12 O
ANISOU 3489 O ILE A 464 3486 1892 2647 -197 602 -542 O
ATOM 3490 CB ILE A 464 28.039 4.672 -5.698 1.00 23.56 C
ANISOU 3490 CB ILE A 464 3895 1976 3080 11 533 -460 C
ATOM 3491 CG1 ILE A 464 27.160 3.463 -6.033 1.00 29.50 C
ANISOU 3491 CG1 ILE A 464 4743 2727 3739 -29 507 -439 C
ATOM 3492 CG2 ILE A 464 28.104 5.633 -6.881 1.00 24.63 C
ANISOU 3492 CG2 ILE A 464 3903 2159 3294 70 423 -421 C
ATOM 3493 CD1 ILE A 464 25.733 3.811 -6.390 1.00 24.22 C
ANISOU 3493 CD1 ILE A 464 4166 1989 3048 66 404 -377 C
ATOM 3494 N PHE A 465 30.948 4.086 -7.220 1.00 19.98 N
ANISOU 3494 N PHE A 465 3175 1794 2621 -134 572 -497 N
ATOM 3495 CA PHE A 465 31.581 3.474 -8.382 1.00 19.62 C
ANISOU 3495 CA PHE A 465 3070 1830 2552 -188 518 -471 C
ATOM 3496 C PHE A 465 33.093 3.327 -8.221 1.00 23.93 C
ANISOU 3496 C PHE A 465 3554 2478 3059 -238 599 -496 C
ATOM 3497 O PHE A 465 33.805 3.152 -9.218 1.00 21.52 O
ANISOU 3497 O PHE A 465 3195 2235 2748 -272 557 -450 O
ATOM 3498 CB PHE A 465 31.256 4.281 -9.638 1.00 18.62 C
ANISOU 3498 CB PHE A 465 2869 1693 2513 -160 401 -397 C
ATOM 3499 CG PHE A 465 29.795 4.305 -9.989 1.00 17.40 C
ANISOU 3499 CG PHE A 465 2783 1454 2373 -99 289 -382 C
ATOM 3500 CD1 PHE A 465 29.013 3.173 -9.848 1.00 16.93 C
ANISOU 3500 CD1 PHE A 465 2839 1373 2222 -97 275 -410 C
ATOM 3501 CD2 PHE A 465 29.207 5.464 -10.469 1.00 18.06 C
ANISOU 3501 CD2 PHE A 465 2807 1499 2554 -38 197 -344 C
ATOM 3502 CE1 PHE A 465 27.674 3.194 -10.178 1.00 18.47 C
ANISOU 3502 CE1 PHE A 465 3110 1507 2400 -28 177 -394 C
ATOM 3503 CE2 PHE A 465 27.870 5.492 -10.799 1.00 18.32 C
ANISOU 3503 CE2 PHE A 465 2915 1464 2582 34 78 -338 C
ATOM 3504 CZ PHE A 465 27.101 4.355 -10.654 1.00 19.58 C
ANISOU 3504 CZ PHE A 465 3211 1601 2626 43 70 -360 C
ATOM 3505 N LEU A 466 33.601 3.394 -6.991 1.00 21.61 N
ANISOU 3505 N LEU A 466 3282 2194 2734 -238 706 -569 N
ATOM 3506 CA LEU A 466 35.017 3.140 -6.754 1.00 24.12 C
ANISOU 3506 CA LEU A 466 3562 2620 2984 -272 775 -612 C
ATOM 3507 C LEU A 466 35.395 1.757 -7.277 1.00 24.54 C
ANISOU 3507 C LEU A 466 3635 2730 2958 -329 729 -626 C
ATOM 3508 O LEU A 466 34.662 0.781 -7.090 1.00 21.40 O
ANISOU 3508 O LEU A 466 3295 2296 2539 -351 702 -665 O
ATOM 3509 CB LEU A 466 35.347 3.240 -5.257 1.00 18.21 C
ANISOU 3509 CB LEU A 466 2858 1853 2210 -260 874 -721 C
ATOM 3510 CG LEU A 466 35.440 4.563 -4.475 1.00 33.29 C
ANISOU 3510 CG LEU A 466 4746 3731 4171 -180 940 -751 C
ATOM 3511 CD1 LEU A 466 35.522 4.306 -2.973 1.00 38.87 C
ANISOU 3511 CD1 LEU A 466 5543 4369 4858 -179 1004 -877 C
ATOM 3512 CD2 LEU A 466 36.635 5.399 -4.897 1.00 37.23 C
ANISOU 3512 CD2 LEU A 466 5133 4366 4646 -151 995 -726 C
ATOM 3513 N GLY A 467 36.545 1.679 -7.952 1.00 19.19 N
ANISOU 3513 N GLY A 467 3189 1775 2326 -507 397 -583 N
ATOM 3514 CA GLY A 467 37.071 0.433 -8.462 1.00 15.30 C
ANISOU 3514 CA GLY A 467 2724 1390 1700 -547 373 -603 C
ATOM 3515 C GLY A 467 36.735 0.142 -9.912 1.00 20.44 C
ANISOU 3515 C GLY A 467 3388 2031 2347 -506 190 -547 C
ATOM 3516 O GLY A 467 37.339 -0.764 -10.502 1.00 26.29 O
ANISOU 3516 O GLY A 467 4132 2862 2997 -539 165 -552 O
ATOM 3517 N LEU A 468 35.806 0.889 -10.504 1.00 22.93 N
ANISOU 3517 N LEU A 468 3710 2243 2761 -435 64 -494 N
ATOM 3518 CA LEU A 468 35.317 0.602 -11.853 1.00 14.66 C
ANISOU 3518 CA LEU A 468 2688 1173 1710 -390 -117 -450 C
ATOM 3519 C LEU A 468 36.156 1.330 -12.906 1.00 23.42 C
ANISOU 3519 C LEU A 468 3692 2289 2918 -418 -183 -396 C
ATOM 3520 O LEU A 468 35.666 2.110 -13.723 1.00 24.21 O
ANISOU 3520 O LEU A 468 3765 2313 3120 -377 -308 -342 O
ATOM 3521 CB LEU A 468 33.843 0.968 -11.957 1.00 17.25 C
ANISOU 3521 CB LEU A 468 3078 1395 2080 -302 -224 -425 C
ATOM 3522 CG LEU A 468 32.950 0.090 -11.079 1.00 18.61 C
ANISOU 3522 CG LEU A 468 3361 1567 2143 -270 -179 -469 C
ATOM 3523 CD1 LEU A 468 31.514 0.583 -11.106 1.00 14.85 C
ANISOU 3523 CD1 LEU A 468 2933 991 1716 -181 -275 -437 C
ATOM 3524 CD2 LEU A 468 33.043 -1.353 -11.549 1.00 17.52 C
ANISOU 3524 CD2 LEU A 468 3222 1556 1880 -261 -204 -465 C
ATOM 3525 N THR A 469 37.455 1.034 -12.882 1.00 27.19 N
ANISOU 3525 N THR A 469 4108 2866 3357 -493 -95 -408 N
ATOM 3526 CA THR A 469 38.411 1.719 -13.739 1.00 26.05 C
ANISOU 3526 CA THR A 469 3853 2742 3302 -531 -130 -355 C
ATOM 3527 C THR A 469 38.433 1.169 -15.162 1.00 24.48 C
ANISOU 3527 C THR A 469 3666 2548 3087 -519 -282 -314 C
ATOM 3528 O THR A 469 38.966 1.830 -16.060 1.00 30.88 O
ANISOU 3528 O THR A 469 4394 3347 3993 -537 -348 -257 O
ATOM 3529 CB THR A 469 39.803 1.630 -13.109 1.00 26.60 C
ANISOU 3529 CB THR A 469 3849 2925 3335 -616 29 -384 C
ATOM 3530 OG1 THR A 469 40.245 0.269 -13.131 1.00 38.58 O
ANISOU 3530 OG1 THR A 469 5412 4545 4703 -650 59 -418 O
ATOM 3531 CG2 THR A 469 39.757 2.100 -11.654 1.00 24.67 C
ANISOU 3531 CG2 THR A 469 3602 2669 3101 -629 186 -438 C
ATOM 3532 N SER A 470 37.856 -0.006 -15.392 1.00 21.99 N
ANISOU 3532 N SER A 470 3452 2247 2657 -488 -338 -340 N
ATOM 3533 CA SER A 470 37.748 -0.570 -16.729 1.00 21.34 C
ANISOU 3533 CA SER A 470 3393 2156 2558 -466 -484 -307 C
ATOM 3534 C SER A 470 36.376 -0.337 -17.349 1.00 25.78 C
ANISOU 3534 C SER A 470 4023 2607 3166 -386 -642 -293 C
ATOM 3535 O SER A 470 36.135 -0.770 -18.481 1.00 23.45 O
ANISOU 3535 O SER A 470 3753 2293 2864 -357 -769 -270 O
ATOM 3536 CB SER A 470 38.055 -2.070 -16.689 1.00 26.79 C
ANISOU 3536 CB SER A 470 4147 2943 3089 -481 -449 -344 C
ATOM 3537 OG SER A 470 38.447 -2.558 -17.960 1.00 32.18 O
ANISOU 3537 OG SER A 470 4820 3641 3767 -481 -553 -306 O
ATOM 3538 N LEU A 471 35.482 0.346 -16.640 1.00 17.94 N
ANISOU 3538 N LEU A 471 3051 1545 2219 -345 -629 -302 N
ATOM 3539 CA LEU A 471 34.106 0.496 -17.091 1.00 14.73 C
ANISOU 3539 CA LEU A 471 2714 1048 1836 -267 -769 -292 C
ATOM 3540 C LEU A 471 34.029 1.390 -18.324 1.00 20.58 C
ANISOU 3540 C LEU A 471 3394 1720 2707 -256 -916 -234 C
ATOM 3541 O LEU A 471 34.515 2.526 -18.312 1.00 19.05 O
ANISOU 3541 O LEU A 471 3101 1504 2634 -284 -892 -194 O
ATOM 3542 CB LEU A 471 33.260 1.072 -15.959 1.00 14.97 C
ANISOU 3542 CB LEU A 471 2769 1028 1889 -229 -705 -307 C
ATOM 3543 CG LEU A 471 31.742 1.009 -16.123 1.00 20.45 C
ANISOU 3543 CG LEU A 471 3530 1674 2567 -139 -807 -295 C
ATOM 3544 CD1 LEU A 471 31.276 -0.425 -16.311 1.00 18.46 C
ANISOU 3544 CD1 LEU A 471 3328 1514 2171 -98 -804 -301 C
ATOM 3545 CD2 LEU A 471 31.073 1.624 -14.915 1.00 15.44 C
ANISOU 3545 CD2 LEU A 471 2924 976 1966 -113 -735 -309 C
ATOM 3546 N ASN A 472 33.415 0.870 -19.390 1.00 17.98 N
ANISOU 3546 N ASN A 472 3088 1400 2345 -198 -1027 -208 N
ATOM 3547 CA ASN A 472 33.180 1.621 -20.617 1.00 19.44 C
ANISOU 3547 CA ASN A 472 3224 1525 2637 -178 -1170 -155 C
ATOM 3548 C ASN A 472 31.729 2.031 -20.805 1.00 19.84 C
ANISOU 3548 C ASN A 472 3312 1520 2707 -99 -1273 -143 C
ATOM 3549 O ASN A 472 31.469 3.114 -21.335 1.00 18.27 O
ANISOU 3549 O ASN A 472 3059 1256 2625 -95 -1369 -107 O
ATOM 3550 CB ASN A 472 33.620 0.800 -21.838 1.00 19.67 C
ANISOU 3550 CB ASN A 472 3250 1594 2630 -173 -1221 -129 C
ATOM 3551 CG ASN A 472 35.074 0.390 -21.764 1.00 20.51 C
ANISOU 3551 CG ASN A 472 3314 1764 2715 -254 -1136 -134 C
ATOM 3552 OD1 ASN A 472 35.428 -0.761 -22.025 1.00 22.23 O
ANISOU 3552 OD1 ASN A 472 3562 2048 2838 -249 -1099 -141 O
ATOM 3553 ND2 ASN A 472 35.927 1.334 -21.395 1.00 19.42 N
ANISOU 3553 ND2 ASN A 472 3099 1608 2673 -330 -1097 -124 N
ATOM 3554 N THR A 473 30.786 1.196 -20.374 1.00 22.24 N
ANISOU 3554 N THR A 473 3697 1852 2899 -38 -1255 -167 N
ATOM 3555 CA THR A 473 29.362 1.430 -20.569 1.00 25.67 C
ANISOU 3555 CA THR A 473 4174 2245 3333 38 -1358 -156 C
ATOM 3556 C THR A 473 28.676 1.479 -19.212 1.00 22.75 C
ANISOU 3556 C THR A 473 3853 1872 2919 60 -1281 -187 C
ATOM 3557 O THR A 473 28.702 0.496 -18.460 1.00 23.64 O
ANISOU 3557 O THR A 473 4013 2044 2923 62 -1173 -214 O
ATOM 3558 CB THR A 473 28.743 0.341 -21.446 1.00 28.81 C
ANISOU 3558 CB THR A 473 4626 2661 3660 102 -1403 -140 C
ATOM 3559 OG1 THR A 473 29.438 0.289 -22.697 1.00 31.27 O
ANISOU 3559 OG1 THR A 473 4898 2957 4026 82 -1452 -113 O
ATOM 3560 CG2 THR A 473 27.278 0.641 -21.705 1.00 20.49 C
ANISOU 3560 CG2 THR A 473 3617 1548 2620 179 -1505 -129 C
ATOM 3561 N LEU A 474 28.063 2.620 -18.901 1.00 19.02 N
ANISOU 3561 N LEU A 474 3361 1329 2537 76 -1326 -175 N
ATOM 3562 CA LEU A 474 27.309 2.792 -17.666 1.00 16.97 C
ANISOU 3562 CA LEU A 474 3145 1047 2256 109 -1253 -190 C
ATOM 3563 C LEU A 474 25.901 3.250 -18.023 1.00 24.11 C
ANISOU 3563 C LEU A 474 4070 1917 3174 177 -1384 -171 C
ATOM 3564 O LEU A 474 25.703 4.388 -18.465 1.00 19.39 O
ANISOU 3564 O LEU A 474 3407 1266 2692 179 -1461 -137 O
ATOM 3565 CB LEU A 474 27.992 3.788 -16.734 1.00 18.14 C
ANISOU 3565 CB LEU A 474 3239 1140 2515 70 -1138 -181 C
ATOM 3566 CG LEU A 474 27.305 3.985 -15.380 1.00 25.15 C
ANISOU 3566 CG LEU A 474 4167 1996 3391 108 -1039 -189 C
ATOM 3567 CD1 LEU A 474 26.935 2.648 -14.770 1.00 21.91 C
ANISOU 3567 CD1 LEU A 474 3847 1656 2823 122 -971 -233 C
ATOM 3568 CD2 LEU A 474 28.196 4.767 -14.431 1.00 21.82 C
ANISOU 3568 CD2 LEU A 474 3685 1542 3061 64 -893 -186 C
ATOM 3569 N LYS A 475 24.929 2.362 -17.834 1.00 21.59 N
ANISOU 3569 N LYS A 475 3833 1637 2733 229 -1405 -191 N
ATOM 3570 CA LYS A 475 23.517 2.679 -18.003 1.00 25.74 C
ANISOU 3570 CA LYS A 475 4390 2143 3246 285 -1515 -193 C
ATOM 3571 C LYS A 475 22.880 2.776 -16.623 1.00 28.05 C
ANISOU 3571 C LYS A 475 4720 2420 3517 319 -1407 -189 C
ATOM 3572 O LYS A 475 22.794 1.774 -15.903 1.00 32.48 O
ANISOU 3572 O LYS A 475 5349 3024 3969 330 -1324 -210 O
ATOM 3573 CB LYS A 475 22.819 1.618 -18.854 1.00 19.73 C
ANISOU 3573 CB LYS A 475 3661 1434 2401 315 -1540 -208 C
ATOM 3574 CG LYS A 475 23.381 1.495 -20.260 1.00 19.18 C
ANISOU 3574 CG LYS A 475 3541 1344 2403 298 -1556 -186 C
ATOM 3575 CD LYS A 475 22.738 0.350 -21.021 1.00 21.55 C
ANISOU 3575 CD LYS A 475 3876 1650 2663 327 -1514 -209 C
ATOM 3576 CE LYS A 475 23.226 0.336 -22.457 1.00 19.93 C
ANISOU 3576 CE LYS A 475 3630 1425 2517 304 -1556 -202 C
ATOM 3577 NZ LYS A 475 22.698 -0.815 -23.234 1.00 30.24 N
ANISOU 3577 NZ LYS A 475 4965 2746 3779 336 -1527 -219 N
ATOM 3578 N MET A 476 22.435 3.981 -16.254 1.00 26.23 N
ANISOU 3578 N MET A 476 4437 2135 3395 340 -1404 -150 N
ATOM 3579 CA MET A 476 21.827 4.212 -14.948 1.00 35.32 C
ANISOU 3579 CA MET A 476 5612 3263 4546 380 -1299 -130 C
ATOM 3580 C MET A 476 20.621 5.143 -15.060 1.00 33.14 C
ANISOU 3580 C MET A 476 5303 2963 4326 432 -1376 -87 C
ATOM 3581 O MET A 476 20.361 5.946 -14.155 1.00 25.60 O
ANISOU 3581 O MET A 476 4317 1967 3444 461 -1299 -41 O
ATOM 3582 CB MET A 476 22.852 4.766 -13.960 1.00 32.89 C
ANISOU 3582 CB MET A 476 5262 2910 4327 344 -1143 -116 C
ATOM 3583 CG MET A 476 23.642 5.946 -14.486 1.00 29.96 C
ANISOU 3583 CG MET A 476 4787 2494 4103 312 -1169 -80 C
ATOM 3584 SD MET A 476 24.955 6.433 -13.352 1.00 30.57 S
ANISOU 3584 SD MET A 476 4824 2522 4269 260 -979 -85 S
ATOM 3585 CE MET A 476 24.021 6.698 -11.848 1.00 22.15 C
ANISOU 3585 CE MET A 476 3797 1415 3206 321 -863 -68 C
ATOM 3586 N ALA A 477 19.871 5.035 -16.152 1.00 32.51 N
ANISOU 3586 N ALA A 477 5230 2910 4213 441 -1517 -109 N
ATOM 3587 CA ALA A 477 18.692 5.862 -16.345 1.00 27.73 C
ANISOU 3587 CA ALA A 477 4593 2294 3651 481 -1585 -76 C
ATOM 3588 C ALA A 477 17.591 5.472 -15.363 1.00 23.94 C
ANISOU 3588 C ALA A 477 4173 1830 3094 540 -1530 -67 C
ATOM 3589 O ALA A 477 17.584 4.378 -14.792 1.00 24.97 O
ANISOU 3589 O ALA A 477 4383 1987 3116 546 -1469 -102 O
ATOM 3590 CB ALA A 477 18.183 5.736 -17.779 1.00 25.26 C
ANISOU 3590 CB ALA A 477 4282 1992 3323 462 -1723 -122 C
ATOM 3591 N GLY A 478 16.649 6.390 -15.168 1.00 24.82 N
ANISOU 3591 N GLY A 478 4242 1929 3262 584 -1551 -13 N
ATOM 3592 CA GLY A 478 15.494 6.107 -14.340 1.00 31.59 C
ANISOU 3592 CA GLY A 478 5145 2803 4053 642 -1511 6 C
ATOM 3593 C GLY A 478 15.738 6.088 -12.849 1.00 35.20 C
ANISOU 3593 C GLY A 478 5622 3229 4524 666 -1361 44 C
ATOM 3594 O GLY A 478 14.861 5.644 -12.100 1.00 41.41 O
ANISOU 3594 O GLY A 478 6461 4031 5245 709 -1318 56 O
ATOM 3595 N ASN A 479 16.896 6.556 -12.388 1.00 32.57 N
ANISOU 3595 N ASN A 479 5250 2846 4281 635 -1270 59 N
ATOM 3596 CA ASN A 479 17.183 6.613 -10.961 1.00 25.07 C
ANISOU 3596 CA ASN A 479 4316 1848 3361 647 -1107 82 C
ATOM 3597 C ASN A 479 17.057 8.046 -10.454 1.00 29.74 C
ANISOU 3597 C ASN A 479 4824 2378 4099 681 -1060 159 C
ATOM 3598 O ASN A 479 16.297 8.840 -11.021 1.00 32.09 O
ANISOU 3598 O ASN A 479 5067 2687 4439 715 -1157 206 O
ATOM 3599 CB ASN A 479 18.574 6.043 -10.683 1.00 22.89 C
ANISOU 3599 CB ASN A 479 4062 1559 3076 583 -1010 30 C
ATOM 3600 CG ASN A 479 18.696 4.582 -11.093 1.00 29.10 C
ANISOU 3600 CG ASN A 479 4933 2411 3711 556 -1044 -39 C
ATOM 3601 OD1 ASN A 479 17.949 3.726 -10.616 1.00 27.87 O
ANISOU 3601 OD1 ASN A 479 4854 2288 3448 584 -1027 -53 O
ATOM 3602 ND2 ASN A 479 19.627 4.296 -11.998 1.00 27.51 N
ANISOU 3602 ND2 ASN A 479 4717 2233 3502 504 -1095 -77 N
ATOM 3603 N SER A 480 17.780 8.388 -9.391 1.00 27.88 N
ANISOU 3603 N SER A 480 4575 2078 3939 670 -909 169 N
ATOM 3604 CA SER A 480 17.769 9.749 -8.869 1.00 28.02 C
ANISOU 3604 CA SER A 480 4514 2031 4103 704 -851 239 C
ATOM 3605 C SER A 480 18.980 9.938 -7.965 1.00 28.79 C
ANISOU 3605 C SER A 480 4602 2062 4276 664 -688 214 C
ATOM 3606 O SER A 480 19.688 8.985 -7.630 1.00 25.03 O
ANISOU 3606 O SER A 480 4186 1595 3729 611 -612 144 O
ATOM 3607 CB SER A 480 16.464 10.056 -8.124 1.00 34.96 C
ANISOU 3607 CB SER A 480 5401 2899 4984 781 -827 305 C
ATOM 3608 OG SER A 480 16.271 9.167 -7.038 1.00 33.41 O
ANISOU 3608 OG SER A 480 5285 2690 4720 783 -712 281 O
ATOM 3609 N PHE A 481 19.205 11.192 -7.571 1.00 29.69 N
ANISOU 3609 N PHE A 481 4638 2112 4530 688 -631 267 N
ATOM 3610 CA PHE A 481 20.346 11.580 -6.754 1.00 26.92 C
ANISOU 3610 CA PHE A 481 4265 1693 4272 652 -479 242 C
ATOM 3611 C PHE A 481 19.869 12.389 -5.554 1.00 27.46 C
ANISOU 3611 C PHE A 481 4315 1685 4432 713 -356 298 C
ATOM 3612 O PHE A 481 18.804 13.012 -5.581 1.00 25.43 O
ANISOU 3612 O PHE A 481 4030 1430 4200 785 -410 376 O
ATOM 3613 CB PHE A 481 21.363 12.395 -7.569 1.00 23.85 C
ANISOU 3613 CB PHE A 481 3781 1297 3982 611 -528 247 C
ATOM 3614 CG PHE A 481 22.188 11.573 -8.516 1.00 26.74 C
ANISOU 3614 CG PHE A 481 4166 1717 4276 537 -600 183 C
ATOM 3615 CD1 PHE A 481 21.647 11.087 -9.691 1.00 23.30 C
ANISOU 3615 CD1 PHE A 481 3748 1351 3755 538 -763 182 C
ATOM 3616 CD2 PHE A 481 23.520 11.308 -8.239 1.00 27.27 C
ANISOU 3616 CD2 PHE A 481 4219 1794 4349 458 -486 121 C
ATOM 3617 CE1 PHE A 481 22.407 10.339 -10.561 1.00 25.60 C
ANISOU 3617 CE1 PHE A 481 4055 1686 3984 474 -823 128 C
ATOM 3618 CE2 PHE A 481 24.282 10.560 -9.104 1.00 22.74 C
ANISOU 3618 CE2 PHE A 481 3654 1284 3703 390 -541 71 C
ATOM 3619 CZ PHE A 481 23.727 10.077 -10.266 1.00 25.30 C
ANISOU 3619 CZ PHE A 481 4014 1636 3964 405 -720 77 C
ATOM 3620 N LYS A 482 20.676 12.372 -4.493 1.00 28.89 N
ANISOU 3620 N LYS A 482 4513 1801 4661 683 -187 255 N
ATOM 3621 CA LYS A 482 20.381 13.185 -3.320 1.00 25.45 C
ANISOU 3621 CA LYS A 482 4065 1295 4309 733 -65 294 C
ATOM 3622 C LYS A 482 20.352 14.661 -3.700 1.00 38.13 C
ANISOU 3622 C LYS A 482 5554 2893 6040 774 -108 370 C
ATOM 3623 O LYS A 482 21.243 15.154 -4.401 1.00 35.49 O
ANISOU 3623 O LYS A 482 5136 2573 5775 731 -139 363 O
ATOM 3624 CB LYS A 482 21.420 12.950 -2.227 1.00 28.08 C
ANISOU 3624 CB LYS A 482 4393 1624 4653 657 121 212 C
ATOM 3625 CG LYS A 482 21.242 13.880 -1.041 1.00 35.69 C
ANISOU 3625 CG LYS A 482 5311 2548 5702 689 242 241 C
ATOM 3626 CD LYS A 482 22.400 13.778 -0.078 1.00 48.15 C
ANISOU 3626 CD LYS A 482 6872 4131 7291 611 428 159 C
ATOM 3627 CE LYS A 482 22.177 14.651 1.140 1.00 56.93 C
ANISOU 3627 CE LYS A 482 7946 5198 8487 646 552 185 C
ATOM 3628 NZ LYS A 482 23.130 14.315 2.234 1.00 58.62 N
ANISOU 3628 NZ LYS A 482 8164 5423 8684 568 734 96 N
ATOM 3629 N ASP A 483 19.313 15.363 -3.244 1.00 31.03 N
ANISOU 3629 N ASP A 483 4646 1974 5169 856 -116 446 N
ATOM 3630 CA ASP A 483 19.097 16.777 -3.542 1.00 29.83 C
ANISOU 3630 CA ASP A 483 4386 1821 5127 905 -160 526 C
ATOM 3631 C ASP A 483 18.990 17.041 -5.039 1.00 32.80 C
ANISOU 3631 C ASP A 483 4699 2259 5504 900 -336 560 C
ATOM 3632 O ASP A 483 19.103 18.191 -5.481 1.00 35.53 O
ANISOU 3632 O ASP A 483 4940 2611 5947 917 -383 614 O
ATOM 3633 CB ASP A 483 20.197 17.647 -2.929 1.00 35.88 C
ANISOU 3633 CB ASP A 483 5065 2549 6017 872 -23 507 C
ATOM 3634 CG ASP A 483 20.254 17.528 -1.422 1.00 45.82 C
ANISOU 3634 CG ASP A 483 6362 3766 7281 868 151 472 C
ATOM 3635 OD1 ASP A 483 19.178 17.549 -0.789 1.00 42.99 O
ANISOU 3635 OD1 ASP A 483 6045 3390 6898 928 149 514 O
ATOM 3636 OD2 ASP A 483 21.369 17.405 -0.875 1.00 47.28 O
ANISOU 3636 OD2 ASP A 483 6531 3942 7491 801 289 400 O
ATOM 3637 N ASN A 484 18.766 15.985 -5.826 1.00 35.17 N
ANISOU 3637 N ASN A 484 5057 2614 5693 868 -440 523 N
ATOM 3638 CA ASN A 484 18.670 16.071 -7.283 1.00 34.77 C
ANISOU 3638 CA ASN A 484 4958 2634 5619 845 -621 531 C
ATOM 3639 C ASN A 484 19.901 16.730 -7.898 1.00 31.01 C
ANISOU 3639 C ASN A 484 4389 2151 5242 788 -637 519 C
ATOM 3640 O ASN A 484 19.813 17.408 -8.923 1.00 32.69 O
ANISOU 3640 O ASN A 484 4524 2402 5496 784 -766 557 O
ATOM 3641 CB ASN A 484 17.390 16.796 -7.705 1.00 35.03 C
ANISOU 3641 CB ASN A 484 4950 2706 5654 916 -730 614 C
ATOM 3642 CG ASN A 484 16.140 16.059 -7.264 1.00 35.77 C
ANISOU 3642 CG ASN A 484 5126 2822 5643 967 -732 630 C
ATOM 3643 OD1 ASN A 484 16.057 14.836 -7.380 1.00 30.41 O
ANISOU 3643 OD1 ASN A 484 4527 2174 4854 934 -750 571 O
ATOM 3644 ND2 ASN A 484 15.169 16.797 -6.732 1.00 32.01 N
ANISOU 3644 ND2 ASN A 484 4628 2335 5200 1048 -710 711 N
ATOM 3645 N THR A 485 21.058 16.533 -7.278 1.00 35.42 N
ANISOU 3645 N THR A 485 4949 2665 5844 737 -504 465 N
ATOM 3646 CA THR A 485 22.320 17.069 -7.765 1.00 34.55 C
ANISOU 3646 CA THR A 485 4746 2549 5831 676 -496 452 C
ATOM 3647 C THR A 485 23.189 15.915 -8.232 1.00 34.56 C
ANISOU 3647 C THR A 485 4802 2581 5749 592 -510 367 C
ATOM 3648 O THR A 485 23.408 14.959 -7.482 1.00 35.37 O
ANISOU 3648 O THR A 485 4989 2687 5764 564 -399 299 O
ATOM 3649 CB THR A 485 23.047 17.856 -6.674 1.00 35.39 C
ANISOU 3649 CB THR A 485 4793 2597 6058 679 -311 456 C
ATOM 3650 OG1 THR A 485 22.271 18.999 -6.297 1.00 37.49 O
ANISOU 3650 OG1 THR A 485 5003 2845 6398 758 -305 539 O
ATOM 3651 CG2 THR A 485 24.419 18.305 -7.163 1.00 26.89 C
ANISOU 3651 CG2 THR A 485 3619 1545 5054 605 -284 433 C
ATOM 3652 N LEU A 486 23.672 16.000 -9.467 1.00 31.34 N
ANISOU 3652 N LEU A 486 4343 2219 5347 546 -635 367 N
ATOM 3653 CA LEU A 486 24.618 15.017 -9.982 1.00 25.70 C
ANISOU 3653 CA LEU A 486 3660 1561 4543 458 -635 290 C
ATOM 3654 C LEU A 486 25.955 15.211 -9.279 1.00 24.11 C
ANISOU 3654 C LEU A 486 3408 1371 4383 394 -455 247 C
ATOM 3655 O LEU A 486 26.628 16.225 -9.482 1.00 28.97 O
ANISOU 3655 O LEU A 486 3911 1986 5109 376 -435 281 O
ATOM 3656 CB LEU A 486 24.758 15.161 -11.494 1.00 24.24 C
ANISOU 3656 CB LEU A 486 3428 1412 4371 429 -817 312 C
ATOM 3657 CG LEU A 486 25.763 14.242 -12.201 1.00 27.13 C
ANISOU 3657 CG LEU A 486 3814 1835 4659 342 -834 247 C
ATOM 3658 CD1 LEU A 486 25.468 12.779 -11.905 1.00 23.32 C
ANISOU 3658 CD1 LEU A 486 3462 1376 4021 336 -813 177 C
ATOM 3659 CD2 LEU A 486 25.757 14.492 -13.702 1.00 23.51 C
ANISOU 3659 CD2 LEU A 486 3307 1394 4230 322 -1021 278 C
ATOM 3660 N SER A 487 26.350 14.241 -8.459 1.00 23.48 N
ANISOU 3660 N SER A 487 3405 1305 4210 356 -325 171 N
ATOM 3661 CA SER A 487 27.535 14.360 -7.627 1.00 30.52 C
ANISOU 3661 CA SER A 487 4259 2210 5128 297 -140 119 C
ATOM 3662 C SER A 487 28.752 13.731 -8.306 1.00 29.35 C
ANISOU 3662 C SER A 487 4090 2142 4918 202 -144 66 C
ATOM 3663 O SER A 487 28.682 13.197 -9.415 1.00 28.63 O
ANISOU 3663 O SER A 487 4018 2089 4770 184 -288 69 O
ATOM 3664 CB SER A 487 27.282 13.741 -6.249 1.00 34.78 C
ANISOU 3664 CB SER A 487 4887 2717 5610 307 16 67 C
ATOM 3665 OG SER A 487 26.642 12.482 -6.352 1.00 34.00 O
ANISOU 3665 OG SER A 487 4904 2640 5374 310 -42 34 O
ATOM 3666 N ASN A 488 29.891 13.802 -7.613 1.00 23.28 N
ANISOU 3666 N ASN A 488 3282 1400 4162 142 19 15 N
ATOM 3667 CA ASN A 488 31.188 13.412 -8.169 1.00 23.76 C
ANISOU 3667 CA ASN A 488 3299 1544 4183 51 36 -25 C
ATOM 3668 C ASN A 488 31.393 11.903 -8.018 1.00 26.80 C
ANISOU 3668 C ASN A 488 3786 1985 4410 3 65 -103 C
ATOM 3669 O ASN A 488 32.231 11.418 -7.254 1.00 27.60 O
ANISOU 3669 O ASN A 488 3898 2129 4458 -57 213 -172 O
ATOM 3670 CB ASN A 488 32.301 14.205 -7.493 1.00 35.78 C
ANISOU 3670 CB ASN A 488 4727 3081 5787 11 197 -44 C
ATOM 3671 CG ASN A 488 33.671 13.881 -8.046 1.00 45.37 C
ANISOU 3671 CG ASN A 488 5884 4390 6963 -81 219 -76 C
ATOM 3672 OD1 ASN A 488 34.636 13.714 -7.297 1.00 48.59 O
ANISOU 3672 OD1 ASN A 488 6274 4843 7346 -138 376 -139 O
ATOM 3673 ND2 ASN A 488 33.765 13.781 -9.361 1.00 47.01 N
ANISOU 3673 ND2 ASN A 488 6063 4631 7167 -98 63 -35 N
ATOM 3674 N VAL A 489 30.601 11.146 -8.785 1.00 20.64 N
ANISOU 3674 N VAL A 489 3082 1210 3553 29 -83 -91 N
ATOM 3675 CA VAL A 489 30.665 9.685 -8.728 1.00 23.15 C
ANISOU 3675 CA VAL A 489 3498 1580 3716 -7 -72 -156 C
ATOM 3676 C VAL A 489 31.503 9.070 -9.839 1.00 26.45 C
ANISOU 3676 C VAL A 489 3896 2077 4077 -69 -151 -169 C
ATOM 3677 O VAL A 489 31.686 7.842 -9.855 1.00 29.67 O
ANISOU 3677 O VAL A 489 4376 2541 4355 -102 -140 -221 O
ATOM 3678 CB VAL A 489 29.256 9.061 -8.785 1.00 19.68 C
ANISOU 3678 CB VAL A 489 3167 1104 3206 64 -172 -145 C
ATOM 3679 CG1 VAL A 489 28.456 9.421 -7.544 1.00 25.34 C
ANISOU 3679 CG1 VAL A 489 3920 1751 3957 120 -73 -137 C
ATOM 3680 CG2 VAL A 489 28.531 9.520 -10.041 1.00 19.97 C
ANISOU 3680 CG2 VAL A 489 3181 1116 3290 112 -372 -78 C
ATOM 3681 N PHE A 490 32.023 9.875 -10.764 1.00 24.57 N
ANISOU 3681 N PHE A 490 3559 1846 3932 -86 -228 -119 N
ATOM 3682 CA PHE A 490 32.720 9.373 -11.942 1.00 19.07 C
ANISOU 3682 CA PHE A 490 2839 1210 3197 -137 -321 -117 C
ATOM 3683 C PHE A 490 34.229 9.591 -11.878 1.00 24.90 C
ANISOU 3683 C PHE A 490 3484 2018 3957 -219 -212 -131 C
ATOM 3684 O PHE A 490 34.891 9.596 -12.921 1.00 25.75 O
ANISOU 3684 O PHE A 490 3536 2165 4081 -259 -291 -103 O
ATOM 3685 CB PHE A 490 32.151 10.021 -13.206 1.00 19.49 C
ANISOU 3685 CB PHE A 490 2854 1220 3332 -101 -510 -46 C
ATOM 3686 CG PHE A 490 30.659 9.881 -13.348 1.00 21.56 C
ANISOU 3686 CG PHE A 490 3198 1422 3573 -20 -627 -29 C
ATOM 3687 CD1 PHE A 490 30.082 8.640 -13.571 1.00 24.87 C
ANISOU 3687 CD1 PHE A 490 3730 1859 3862 -4 -688 -69 C
ATOM 3688 CD2 PHE A 490 29.833 10.993 -13.282 1.00 22.72 C
ANISOU 3688 CD2 PHE A 490 3305 1502 3826 42 -679 30 C
ATOM 3689 CE1 PHE A 490 28.712 8.512 -13.712 1.00 25.31 C
ANISOU 3689 CE1 PHE A 490 3858 1868 3891 71 -796 -53 C
ATOM 3690 CE2 PHE A 490 28.461 10.870 -13.425 1.00 25.89 C
ANISOU 3690 CE2 PHE A 490 3776 1859 4201 117 -789 49 C
ATOM 3691 CZ PHE A 490 27.902 9.628 -13.638 1.00 26.64 C
ANISOU 3691 CZ PHE A 490 3984 1974 4163 131 -847 6 C
ATOM 3692 N ALA A 491 34.787 9.760 -10.676 1.00 27.59 N
ANISOU 3692 N ALA A 491 3807 2377 4299 -246 -33 -175 N
ATOM 3693 CA ALA A 491 36.203 10.100 -10.558 1.00 27.84 C
ANISOU 3693 CA ALA A 491 3741 2481 4358 -320 76 -188 C
ATOM 3694 C ALA A 491 37.098 8.943 -10.989 1.00 34.95 C
ANISOU 3694 C ALA A 491 4659 3483 5137 -391 84 -226 C
ATOM 3695 O ALA A 491 38.152 9.161 -11.600 1.00 44.73 O
ANISOU 3695 O ALA A 491 5809 4785 6401 -446 83 -204 O
ATOM 3696 CB ALA A 491 36.525 10.515 -9.124 1.00 28.59 C
ANISOU 3696 CB ALA A 491 3820 2568 4476 -330 269 -237 C
ATOM 3697 N ASN A 492 36.705 7.708 -10.679 1.00 31.64 N
ANISOU 3697 N ASN A 492 4349 3086 4587 -391 94 -279 N
ATOM 3698 CA ASN A 492 37.509 6.547 -11.034 1.00 34.99 C
ANISOU 3698 CA ASN A 492 4794 3612 4889 -453 106 -314 C
ATOM 3699 C ASN A 492 37.166 5.964 -12.398 1.00 25.73 C
ANISOU 3699 C ASN A 492 3654 2438 3684 -434 -73 -274 C
ATOM 3700 O ASN A 492 37.974 5.209 -12.947 1.00 30.32 O
ANISOU 3700 O ASN A 492 4225 3102 4193 -485 -81 -281 O
ATOM 3701 CB ASN A 492 37.367 5.449 -9.975 1.00 49.46 C
ANISOU 3701 CB ASN A 492 6722 5482 6588 -469 218 -394 C
ATOM 3702 CG ASN A 492 37.997 5.829 -8.656 1.00 71.81 C
ANISOU 3702 CG ASN A 492 9518 8334 9432 -511 412 -449 C
ATOM 3703 OD1 ASN A 492 37.303 6.204 -7.717 1.00 88.57 O
ANISOU 3703 OD1 ASN A 492 11678 10384 11591 -472 477 -468 O
ATOM 3704 ND2 ASN A 492 39.324 5.748 -8.583 1.00 74.31 N
ANISOU 3704 ND2 ASN A 492 9761 8752 9721 -589 506 -474 N
ATOM 3705 N THR A 493 36.004 6.290 -12.960 1.00 26.39 N
ANISOU 3705 N THR A 493 3776 2434 3819 -363 -215 -234 N
ATOM 3706 CA THR A 493 35.572 5.694 -14.224 1.00 24.94 C
ANISOU 3706 CA THR A 493 3635 2241 3600 -341 -386 -208 C
ATOM 3707 C THR A 493 36.158 6.462 -15.410 1.00 23.02 C
ANISOU 3707 C THR A 493 3290 1992 3465 -365 -484 -142 C
ATOM 3708 O THR A 493 35.460 6.990 -16.276 1.00 27.71 O
ANISOU 3708 O THR A 493 3877 2517 4135 -325 -631 -94 O
ATOM 3709 CB THR A 493 34.051 5.632 -14.284 1.00 26.28 C
ANISOU 3709 CB THR A 493 3894 2328 3763 -258 -493 -202 C
ATOM 3710 OG1 THR A 493 33.505 6.949 -14.141 1.00 27.51 O
ANISOU 3710 OG1 THR A 493 3995 2406 4051 -216 -518 -155 O
ATOM 3711 CG2 THR A 493 33.526 4.743 -13.163 1.00 22.74 C
ANISOU 3711 CG2 THR A 493 3547 1893 3198 -240 -396 -263 C
ATOM 3712 N THR A 494 37.492 6.482 -15.436 1.00 17.10 N
ANISOU 3712 N THR A 494 2460 1322 2717 -437 -398 -140 N
ATOM 3713 CA THR A 494 38.270 7.262 -16.392 1.00 17.52 C
ANISOU 3713 CA THR A 494 2399 1383 2874 -473 -456 -74 C
ATOM 3714 C THR A 494 38.128 6.767 -17.827 1.00 18.65 C
ANISOU 3714 C THR A 494 2563 1511 3012 -470 -624 -38 C
ATOM 3715 O THR A 494 38.448 7.517 -18.755 1.00 25.70 O
ANISOU 3715 O THR A 494 3372 2380 4011 -486 -710 25 O
ATOM 3716 CB THR A 494 39.742 7.248 -15.952 1.00 29.97 C
ANISOU 3716 CB THR A 494 3892 3066 4430 -552 -307 -87 C
ATOM 3717 OG1 THR A 494 39.810 7.495 -14.539 1.00 41.91 O
ANISOU 3717 OG1 THR A 494 5407 4592 5926 -555 -143 -140 O
ATOM 3718 CG2 THR A 494 40.550 8.320 -16.650 1.00 46.10 C
ANISOU 3718 CG2 THR A 494 5801 5118 6599 -587 -334 -15 C
ATOM 3719 N ASN A 495 37.640 5.546 -18.040 1.00 21.83 N
ANISOU 3719 N ASN A 495 3074 1922 3297 -448 -674 -77 N
ATOM 3720 CA ASN A 495 37.534 4.980 -19.380 1.00 16.91 C
ANISOU 3720 CA ASN A 495 2479 1282 2662 -443 -825 -51 C
ATOM 3721 C ASN A 495 36.094 4.835 -19.856 1.00 18.13 C
ANISOU 3721 C ASN A 495 2726 1349 2815 -368 -974 -59 C
ATOM 3722 O ASN A 495 35.845 4.115 -20.830 1.00 19.18 O
ANISOU 3722 O ASN A 495 2913 1468 2909 -354 -1090 -59 O
ATOM 3723 CB ASN A 495 38.244 3.627 -19.440 1.00 20.41 C
ANISOU 3723 CB ASN A 495 2965 1818 2972 -478 -774 -84 C
ATOM 3724 CG ASN A 495 39.745 3.755 -19.282 1.00 21.90 C
ANISOU 3724 CG ASN A 495 3050 2103 3167 -556 -656 -65 C
ATOM 3725 OD1 ASN A 495 40.397 4.491 -20.023 1.00 27.95 O
ANISOU 3725 OD1 ASN A 495 3718 2864 4036 -589 -697 -3 O
ATOM 3726 ND2 ASN A 495 40.299 3.055 -18.299 1.00 20.81 N
ANISOU 3726 ND2 ASN A 495 2931 2059 2918 -589 -509 -117 N
ATOM 3727 N LEU A 496 35.144 5.495 -19.195 1.00 17.19 N
ANISOU 3727 N LEU A 496 2626 1171 2734 -318 -971 -64 N
ATOM 3728 CA LEU A 496 33.771 5.538 -19.684 1.00 19.89 C
ANISOU 3728 CA LEU A 496 3039 1434 3084 -247 -1118 -61 C
ATOM 3729 C LEU A 496 33.730 6.082 -21.105 1.00 18.53 C
ANISOU 3729 C LEU A 496 2816 1210 3013 -253 -1284 -9 C
ATOM 3730 O LEU A 496 34.360 7.096 -21.411 1.00 19.56 O
ANISOU 3730 O LEU A 496 2836 1332 3262 -290 -1283 44 O
ATOM 3731 CB LEU A 496 32.907 6.417 -18.776 1.00 19.06 C
ANISOU 3731 CB LEU A 496 2932 1278 3033 -198 -1083 -55 C
ATOM 3732 CG LEU A 496 32.342 5.870 -17.467 1.00 23.09 C
ANISOU 3732 CG LEU A 496 3525 1801 3446 -164 -970 -106 C
ATOM 3733 CD1 LEU A 496 31.487 6.928 -16.776 1.00 28.94 C
ANISOU 3733 CD1 LEU A 496 4247 2477 4270 -111 -956 -80 C
ATOM 3734 CD2 LEU A 496 31.540 4.602 -17.701 1.00 20.18 C
ANISOU 3734 CD2 LEU A 496 3283 1440 2946 -124 -1040 -150 C
ATOM 3735 N THR A 497 32.982 5.398 -21.971 1.00 20.16 N
ANISOU 3735 N THR A 497 3090 1417 3155 -205 -1401 -19 N
ATOM 3736 CA THR A 497 32.692 5.887 -23.310 1.00 18.54 C
ANISOU 3736 CA THR A 497 2842 1182 3022 -188 -1548 28 C
ATOM 3737 C THR A 497 31.208 6.114 -23.543 1.00 18.96 C
ANISOU 3737 C THR A 497 2943 1196 3066 -113 -1665 23 C
ATOM 3738 O THR A 497 30.845 6.772 -24.527 1.00 20.06 O
ANISOU 3738 O THR A 497 3040 1299 3285 -101 -1793 60 O
ATOM 3739 CB THR A 497 33.218 4.909 -24.373 1.00 26.69 C
ANISOU 3739 CB THR A 497 3892 2257 3991 -191 -1579 36 C
ATOM 3740 OG1 THR A 497 32.612 3.619 -24.191 1.00 30.54 O
ANISOU 3740 OG1 THR A 497 4488 2782 4333 -136 -1556 -8 O
ATOM 3741 CG2 THR A 497 34.735 4.782 -24.273 1.00 18.43 C
ANISOU 3741 CG2 THR A 497 2782 1257 2963 -274 -1481 49 C
ATOM 3742 N PHE A 498 30.351 5.600 -22.665 1.00 18.64 N
ANISOU 3742 N PHE A 498 2987 1166 2930 -65 -1625 -21 N
ATOM 3743 CA PHE A 498 28.905 5.675 -22.817 1.00 28.05 C
ANISOU 3743 CA PHE A 498 4231 2337 4091 3 -1732 -33 C
ATOM 3744 C PHE A 498 28.307 5.888 -21.434 1.00 29.03 C
ANISOU 3744 C PHE A 498 4391 2447 4193 31 -1639 -53 C
ATOM 3745 O PHE A 498 28.471 5.037 -20.550 1.00 22.80 O
ANISOU 3745 O PHE A 498 3664 1694 3305 36 -1523 -88 O
ATOM 3746 CB PHE A 498 28.363 4.390 -23.454 1.00 20.96 C
ANISOU 3746 CB PHE A 498 3420 1476 3067 58 -1763 -51 C
ATOM 3747 CG PHE A 498 26.883 4.410 -23.720 1.00 24.54 C
ANISOU 3747 CG PHE A 498 3914 1919 3491 107 -1790 -78 C
ATOM 3748 CD1 PHE A 498 25.976 4.161 -22.702 1.00 26.38 C
ANISOU 3748 CD1 PHE A 498 4207 2172 3645 142 -1766 -114 C
ATOM 3749 CD2 PHE A 498 26.401 4.653 -24.995 1.00 28.52 C
ANISOU 3749 CD2 PHE A 498 4414 2364 4058 106 -1834 -80 C
ATOM 3750 CE1 PHE A 498 24.617 4.174 -22.946 1.00 32.04 C
ANISOU 3750 CE1 PHE A 498 4972 2850 4350 165 -1784 -163 C
ATOM 3751 CE2 PHE A 498 25.041 4.664 -25.246 1.00 28.66 C
ANISOU 3751 CE2 PHE A 498 4481 2353 4057 135 -1867 -123 C
ATOM 3752 CZ PHE A 498 24.149 4.420 -24.217 1.00 27.33 C
ANISOU 3752 CZ PHE A 498 4367 2204 3814 169 -1842 -158 C
ATOM 3753 N LEU A 499 27.610 7.007 -21.244 1.00 26.14 N
ANISOU 3753 N LEU A 499 3983 2031 3917 55 -1681 -24 N
ATOM 3754 CA LEU A 499 27.015 7.354 -19.958 1.00 21.69 C
ANISOU 3754 CA LEU A 499 3442 1448 3352 97 -1586 -21 C
ATOM 3755 C LEU A 499 25.578 7.806 -20.179 1.00 27.24 C
ANISOU 3755 C LEU A 499 4158 2140 4052 152 -1689 -15 C
ATOM 3756 O LEU A 499 25.340 8.826 -20.834 1.00 28.01 O
ANISOU 3756 O LEU A 499 4181 2210 4251 144 -1777 21 O
ATOM 3757 CB LEU A 499 27.826 8.449 -19.258 1.00 19.94 C
ANISOU 3757 CB LEU A 499 3133 1180 3263 69 -1485 24 C
ATOM 3758 CG LEU A 499 27.380 8.859 -17.854 1.00 25.04 C
ANISOU 3758 CG LEU A 499 3795 1796 3924 112 -1366 31 C
ATOM 3759 CD1 LEU A 499 27.336 7.657 -16.928 1.00 19.32 C
ANISOU 3759 CD1 LEU A 499 3173 1103 3063 118 -1255 -29 C
ATOM 3760 CD2 LEU A 499 28.294 9.940 -17.292 1.00 23.62 C
ANISOU 3760 CD2 LEU A 499 3507 1599 3869 77 -1255 69 C
ATOM 3761 N ASP A 500 24.626 7.057 -19.626 1.00 28.07 N
ANISOU 3761 N ASP A 500 4353 2271 4042 200 -1671 -51 N
ATOM 3762 CA ASP A 500 23.202 7.331 -19.788 1.00 26.51 C
ANISOU 3762 CA ASP A 500 4178 2073 3823 246 -1751 -57 C
ATOM 3763 C ASP A 500 22.640 7.762 -18.438 1.00 29.64 C
ANISOU 3763 C ASP A 500 4580 2454 4227 300 -1648 -23 C
ATOM 3764 O ASP A 500 22.460 6.931 -17.542 1.00 20.74 O
ANISOU 3764 O ASP A 500 3529 1346 3006 324 -1559 -48 O
ATOM 3765 CB ASP A 500 22.469 6.102 -20.324 1.00 32.92 C
ANISOU 3765 CB ASP A 500 5091 2917 4500 256 -1813 -131 C
ATOM 3766 CG ASP A 500 21.042 6.413 -20.755 1.00 36.70 C
ANISOU 3766 CG ASP A 500 5591 3379 4975 288 -1888 -148 C
ATOM 3767 OD1 ASP A 500 20.560 7.534 -20.499 1.00 31.30 O
ANISOU 3767 OD1 ASP A 500 4844 2679 4370 311 -1900 -93 O
ATOM 3768 OD2 ASP A 500 20.402 5.530 -21.365 1.00 32.95 O
ANISOU 3768 OD2 ASP A 500 5197 2896 4427 295 -1920 -212 O
ATOM 3769 N LEU A 501 22.356 9.058 -18.300 1.00 29.08 N
ANISOU 3769 N LEU A 501 4430 2349 4272 317 -1658 36 N
ATOM 3770 CA LEU A 501 21.797 9.613 -17.075 1.00 25.52 C
ANISOU 3770 CA LEU A 501 3974 1875 3848 372 -1562 77 C
ATOM 3771 C LEU A 501 20.380 10.148 -17.273 1.00 29.60 C
ANISOU 3771 C LEU A 501 4484 2402 4361 423 -1644 102 C
ATOM 3772 O LEU A 501 19.945 11.030 -16.527 1.00 29.09 O
ANISOU 3772 O LEU A 501 4378 2313 4363 467 -1593 160 O
ATOM 3773 CB LEU A 501 22.705 10.715 -16.532 1.00 27.75 C
ANISOU 3773 CB LEU A 501 4164 2105 4273 358 -1474 131 C
ATOM 3774 CG LEU A 501 24.016 10.282 -15.870 1.00 25.96 C
ANISOU 3774 CG LEU A 501 3949 1859 4054 313 -1338 105 C
ATOM 3775 CD1 LEU A 501 25.021 11.431 -15.861 1.00 26.72 C
ANISOU 3775 CD1 LEU A 501 3934 1911 4306 279 -1298 152 C
ATOM 3776 CD2 LEU A 501 23.765 9.781 -14.455 1.00 21.39 C
ANISOU 3776 CD2 LEU A 501 3443 1267 3417 344 -1192 84 C
ATOM 3777 N SER A 502 19.651 9.627 -18.257 1.00 28.39 N
ANISOU 3777 N SER A 502 4371 2281 4134 416 -1761 57 N
ATOM 3778 CA SER A 502 18.320 10.136 -18.560 1.00 28.86 C
ANISOU 3778 CA SER A 502 4424 2352 4191 455 -1836 74 C
ATOM 3779 C SER A 502 17.323 9.736 -17.480 1.00 30.28 C
ANISOU 3779 C SER A 502 4664 2551 4290 521 -1767 85 C
ATOM 3780 O SER A 502 17.483 8.720 -16.800 1.00 30.46 O
ANISOU 3780 O SER A 502 4762 2587 4224 529 -1691 52 O
ATOM 3781 CB SER A 502 17.847 9.617 -19.919 1.00 33.11 C
ANISOU 3781 CB SER A 502 5001 2903 4678 424 -1957 9 C
ATOM 3782 OG SER A 502 17.684 8.209 -19.911 1.00 29.37 O
ANISOU 3782 OG SER A 502 4630 2453 4077 425 -1937 -63 O
ATOM 3783 N LYS A 503 16.283 10.558 -17.332 1.00 28.63 N
ANISOU 3783 N LYS A 503 4418 2345 4113 568 -1794 136 N
ATOM 3784 CA LYS A 503 15.180 10.294 -16.403 1.00 30.43 C
ANISOU 3784 CA LYS A 503 4693 2593 4274 635 -1742 159 C
ATOM 3785 C LYS A 503 15.678 10.098 -14.972 1.00 29.06 C
ANISOU 3785 C LYS A 503 4542 2390 4107 659 -1590 187 C
ATOM 3786 O LYS A 503 15.182 9.247 -14.233 1.00 32.73 O
ANISOU 3786 O LYS A 503 5083 2872 4480 688 -1531 170 O
ATOM 3787 CB LYS A 503 14.350 9.091 -16.856 1.00 27.17 C
ANISOU 3787 CB LYS A 503 4374 2227 3725 638 -1793 88 C
ATOM 3788 CG LYS A 503 13.922 9.134 -18.315 1.00 36.21 C
ANISOU 3788 CG LYS A 503 5512 3383 4865 608 -1921 43 C
ATOM 3789 CD LYS A 503 12.981 7.984 -18.642 1.00 43.47 C
ANISOU 3789 CD LYS A 503 6521 4336 5659 625 -1945 -23 C
ATOM 3790 CE LYS A 503 12.845 7.788 -20.142 1.00 54.71 C
ANISOU 3790 CE LYS A 503 7955 5746 7086 587 -2042 -85 C
ATOM 3791 NZ LYS A 503 11.877 6.708 -20.472 1.00 63.63 N
ANISOU 3791 NZ LYS A 503 9166 6900 8111 614 -2047 -143 N
ATOM 3792 N CYS A 504 16.666 10.899 -14.569 1.00 24.89 N
ANISOU 3792 N CYS A 504 3949 1813 3695 644 -1520 225 N
ATOM 3793 CA CYS A 504 17.225 10.824 -13.225 1.00 27.61 C
ANISOU 3793 CA CYS A 504 4311 2111 4067 658 -1359 242 C
ATOM 3794 C CYS A 504 16.785 11.987 -12.342 1.00 30.96 C
ANISOU 3794 C CYS A 504 4677 2492 4594 716 -1286 327 C
ATOM 3795 O CYS A 504 17.355 12.189 -11.264 1.00 34.68 O
ANISOU 3795 O CYS A 504 5147 2907 5122 724 -1143 342 O
ATOM 3796 CB CYS A 504 18.750 10.746 -13.285 1.00 25.19 C
ANISOU 3796 CB CYS A 504 3984 1774 3811 595 -1301 212 C
ATOM 3797 SG CYS A 504 19.390 9.118 -13.732 1.00 35.94 S
ANISOU 3797 SG CYS A 504 5440 3180 5037 539 -1314 117 S
ATOM 3798 N GLN A 505 15.782 12.756 -12.780 1.00 29.90 N
ANISOU 3798 N GLN A 505 4496 2382 4484 757 -1375 378 N
ATOM 3799 CA GLN A 505 15.220 13.849 -11.981 1.00 30.80 C
ANISOU 3799 CA GLN A 505 4553 2463 4685 822 -1313 467 C
ATOM 3800 C GLN A 505 16.299 14.838 -11.542 1.00 29.31 C
ANISOU 3800 C GLN A 505 4289 2210 4638 811 -1223 500 C
ATOM 3801 O GLN A 505 16.174 15.505 -10.510 1.00 34.03 O
ANISOU 3801 O GLN A 505 4862 2759 5308 861 -1112 557 O
ATOM 3802 CB GLN A 505 14.450 13.306 -10.775 1.00 39.20 C
ANISOU 3802 CB GLN A 505 5686 3516 5691 878 -1210 486 C
ATOM 3803 CG GLN A 505 13.300 12.376 -11.147 1.00 41.59 C
ANISOU 3803 CG GLN A 505 6057 3888 5856 895 -1295 460 C
ATOM 3804 CD GLN A 505 12.533 11.882 -9.935 1.00 35.86 C
ANISOU 3804 CD GLN A 505 5391 3152 5083 948 -1195 490 C
ATOM 3805 OE1 GLN A 505 12.455 10.678 -9.684 1.00 38.47 O
ANISOU 3805 OE1 GLN A 505 5807 3503 5306 932 -1172 435 O
ATOM 3806 NE2 GLN A 505 11.956 12.810 -9.182 1.00 32.10 N
ANISOU 3806 NE2 GLN A 505 4867 2643 4686 1013 -1134 580 N
ATOM 3807 N LEU A 506 17.370 14.933 -12.328 1.00 26.61 N
ANISOU 3807 N LEU A 506 3907 1866 4338 745 -1267 466 N
ATOM 3808 CA LEU A 506 18.456 15.852 -12.022 1.00 27.48 C
ANISOU 3808 CA LEU A 506 3936 1923 4584 726 -1189 493 C
ATOM 3809 C LEU A 506 18.016 17.294 -12.233 1.00 34.10 C
ANISOU 3809 C LEU A 506 4669 2759 5529 765 -1235 576 C
ATOM 3810 O LEU A 506 17.320 17.613 -13.200 1.00 36.66 O
ANISOU 3810 O LEU A 506 4962 3133 5836 767 -1373 594 O
ATOM 3811 CB LEU A 506 19.669 15.547 -12.900 1.00 26.12 C
ANISOU 3811 CB LEU A 506 3742 1757 4425 642 -1236 441 C
ATOM 3812 CG LEU A 506 20.383 14.220 -12.663 1.00 25.66 C
ANISOU 3812 CG LEU A 506 3774 1699 4275 596 -1174 361 C
ATOM 3813 CD1 LEU A 506 21.529 14.056 -13.647 1.00 28.58 C
ANISOU 3813 CD1 LEU A 506 4109 2081 4669 518 -1233 326 C
ATOM 3814 CD2 LEU A 506 20.884 14.159 -11.236 1.00 28.07 C
ANISOU 3814 CD2 LEU A 506 4106 1945 4615 607 -987 354 C
ATOM 3815 N GLU A 507 18.433 18.170 -11.318 1.00 31.64 N
ANISOU 3815 N GLU A 507 4301 2391 5328 795 -1113 624 N
ATOM 3816 CA GLU A 507 18.174 19.597 -11.438 1.00 35.73 C
ANISOU 3816 CA GLU A 507 4711 2908 5958 832 -1140 705 C
ATOM 3817 C GLU A 507 19.435 20.426 -11.616 1.00 33.72 C
ANISOU 3817 C GLU A 507 4353 2623 5836 788 -1106 718 C
ATOM 3818 O GLU A 507 19.351 21.543 -12.136 1.00 31.31 O
ANISOU 3818 O GLU A 507 3945 2334 5617 796 -1171 778 O
ATOM 3819 CB GLU A 507 17.413 20.110 -10.205 1.00 30.27 C
ANISOU 3819 CB GLU A 507 4026 2181 5292 921 -1029 766 C
ATOM 3820 CG GLU A 507 15.980 19.609 -10.106 1.00 37.35 C
ANISOU 3820 CG GLU A 507 4995 3119 6080 977 -1078 784 C
ATOM 3821 CD GLU A 507 15.322 19.967 -8.786 1.00 38.85 C
ANISOU 3821 CD GLU A 507 5206 3265 6290 1063 -951 841 C
ATOM 3822 OE1 GLU A 507 15.904 20.767 -8.023 1.00 44.07 O
ANISOU 3822 OE1 GLU A 507 5819 3867 7058 1080 -838 868 O
ATOM 3823 OE2 GLU A 507 14.222 19.446 -8.508 1.00 41.94 O
ANISOU 3823 OE2 GLU A 507 5661 3681 6592 1110 -964 858 O
ATOM 3824 N GLN A 508 20.588 19.910 -11.205 1.00 33.86 N
ANISOU 3824 N GLN A 508 4391 2602 5872 740 -1003 664 N
ATOM 3825 CA GLN A 508 21.845 20.632 -11.336 1.00 38.51 C
ANISOU 3825 CA GLN A 508 4878 3165 6587 694 -958 675 C
ATOM 3826 C GLN A 508 22.989 19.638 -11.200 1.00 39.05 C
ANISOU 3826 C GLN A 508 4998 3214 6625 625 -884 595 C
ATOM 3827 O GLN A 508 22.805 18.502 -10.751 1.00 39.55 O
ANISOU 3827 O GLN A 508 5175 3275 6579 620 -840 535 O
ATOM 3828 CB GLN A 508 21.955 21.751 -10.296 1.00 37.81 C
ANISOU 3828 CB GLN A 508 4717 3029 6620 748 -821 732 C
ATOM 3829 CG GLN A 508 21.875 21.269 -8.861 1.00 45.01 C
ANISOU 3829 CG GLN A 508 5709 3887 7504 781 -647 699 C
ATOM 3830 CD GLN A 508 21.504 22.378 -7.902 1.00 59.68 C
ANISOU 3830 CD GLN A 508 7512 5709 9453 854 -541 764 C
ATOM 3831 OE1 GLN A 508 21.398 23.541 -8.288 1.00 63.78 O
ANISOU 3831 OE1 GLN A 508 7925 6245 10065 879 -592 834 O
ATOM 3832 NE2 GLN A 508 21.295 22.021 -6.641 1.00 69.40 N
ANISOU 3832 NE2 GLN A 508 8817 6893 10658 885 -395 738 N
ATOM 3833 N ILE A 509 24.184 20.088 -11.582 1.00 35.93 N
ANISOU 3833 N ILE A 509 4515 2810 6328 569 -868 597 N
ATOM 3834 CA ILE A 509 25.372 19.247 -11.648 1.00 32.25 C
ANISOU 3834 CA ILE A 509 4076 2369 5808 482 -798 518 C
ATOM 3835 C ILE A 509 26.464 19.883 -10.799 1.00 31.71 C
ANISOU 3835 C ILE A 509 3932 2296 5821 454 -612 507 C
ATOM 3836 O ILE A 509 26.723 21.087 -10.912 1.00 33.70 O
ANISOU 3836 O ILE A 509 4067 2542 6197 469 -607 570 O
ATOM 3837 CB ILE A 509 25.839 19.064 -13.104 1.00 29.81 C
ANISOU 3837 CB ILE A 509 3733 2107 5488 416 -952 514 C
ATOM 3838 CG1 ILE A 509 24.714 18.471 -13.953 1.00 27.18 C
ANISOU 3838 CG1 ILE A 509 3475 1788 5065 443 -1131 513 C
ATOM 3839 CG2 ILE A 509 27.087 18.191 -13.172 1.00 33.26 C
ANISOU 3839 CG2 ILE A 509 4194 2588 5857 326 -871 436 C
ATOM 3840 CD1 ILE A 509 25.012 18.441 -15.429 1.00 30.77 C
ANISOU 3840 CD1 ILE A 509 3890 2283 5519 384 -1289 514 C
ATOM 3841 N SER A 510 27.104 19.077 -9.956 1.00 30.61 N
ANISOU 3841 N SER A 510 3857 2164 5611 414 -459 427 N
ATOM 3842 CA SER A 510 28.191 19.577 -9.129 1.00 32.85 C
ANISOU 3842 CA SER A 510 4075 2450 5958 381 -276 401 C
ATOM 3843 C SER A 510 29.398 19.936 -9.993 1.00 36.47 C
ANISOU 3843 C SER A 510 4431 2969 6458 304 -302 404 C
ATOM 3844 O SER A 510 29.493 19.575 -11.168 1.00 37.68 O
ANISOU 3844 O SER A 510 4581 3160 6575 264 -447 411 O
ATOM 3845 CB SER A 510 28.586 18.548 -8.071 1.00 33.04 C
ANISOU 3845 CB SER A 510 4195 2475 5884 348 -115 306 C
ATOM 3846 OG SER A 510 27.722 18.622 -6.951 1.00 46.72 O
ANISOU 3846 OG SER A 510 5986 4138 7628 420 -29 314 O
ATOM 3847 N TRP A 511 30.333 20.660 -9.386 1.00 33.53 N
ANISOU 3847 N TRP A 511 3973 2604 6162 283 -156 398 N
ATOM 3848 CA TRP A 511 31.506 21.122 -10.112 1.00 35.88 C
ANISOU 3848 CA TRP A 511 4161 2964 6510 214 -165 410 C
ATOM 3849 C TRP A 511 32.492 19.976 -10.322 1.00 31.83 C
ANISOU 3849 C TRP A 511 3694 2518 5883 121 -127 329 C
ATOM 3850 O TRP A 511 32.773 19.205 -9.399 1.00 29.55 O
ANISOU 3850 O TRP A 511 3479 2235 5513 101 7 250 O
ATOM 3851 CB TRP A 511 32.173 22.269 -9.354 1.00 43.50 C
ANISOU 3851 CB TRP A 511 5018 3921 7589 227 -15 429 C
ATOM 3852 CG TRP A 511 33.318 22.885 -10.092 1.00 51.85 C
ANISOU 3852 CG TRP A 511 5948 5044 8707 164 -27 456 C
ATOM 3853 CD1 TRP A 511 33.268 23.960 -10.929 1.00 51.47 C
ANISOU 3853 CD1 TRP A 511 5784 5004 8768 178 -134 547 C
ATOM 3854 CD2 TRP A 511 34.686 22.462 -10.061 1.00 52.50 C
ANISOU 3854 CD2 TRP A 511 6003 5202 8743 75 72 395 C
ATOM 3855 NE1 TRP A 511 34.522 24.233 -11.423 1.00 46.93 N
ANISOU 3855 NE1 TRP A 511 5112 4501 8220 103 -107 549 N
ATOM 3856 CE2 TRP A 511 35.410 23.326 -10.905 1.00 49.68 C
ANISOU 3856 CE2 TRP A 511 5511 4893 8472 40 19 458 C
ATOM 3857 CE3 TRP A 511 35.367 21.437 -9.402 1.00 51.49 C
ANISOU 3857 CE3 TRP A 511 5947 5111 8506 19 199 297 C
ATOM 3858 CZ2 TRP A 511 36.782 23.195 -11.107 1.00 51.37 C
ANISOU 3858 CZ2 TRP A 511 5662 5191 8667 -44 91 428 C
ATOM 3859 CZ3 TRP A 511 36.727 21.308 -9.603 1.00 52.21 C
ANISOU 3859 CZ3 TRP A 511 5973 5288 8574 -66 269 265 C
ATOM 3860 CH2 TRP A 511 37.422 22.182 -10.446 1.00 52.41 C
ANISOU 3860 CH2 TRP A 511 5866 5362 8687 -95 215 332 C
ATOM 3861 N GLY A 512 33.011 19.861 -11.544 1.00 32.32 N
ANISOU 3861 N GLY A 512 3709 2631 5939 65 -246 351 N
ATOM 3862 CA GLY A 512 34.066 18.914 -11.855 1.00 29.18 C
ANISOU 3862 CA GLY A 512 3330 2307 5449 -23 -214 291 C
ATOM 3863 C GLY A 512 33.627 17.485 -12.078 1.00 30.18 C
ANISOU 3863 C GLY A 512 3590 2442 5435 -36 -275 236 C
ATOM 3864 O GLY A 512 34.481 16.589 -12.084 1.00 33.68 O
ANISOU 3864 O GLY A 512 4061 2948 5787 -103 -218 177 O
ATOM 3865 N VAL A 513 32.330 17.242 -12.282 1.00 28.55 N
ANISOU 3865 N VAL A 513 3462 2182 5204 28 -391 255 N
ATOM 3866 CA VAL A 513 31.831 15.871 -12.359 1.00 24.66 C
ANISOU 3866 CA VAL A 513 3101 1696 4572 26 -436 199 C
ATOM 3867 C VAL A 513 32.366 15.146 -13.591 1.00 22.52 C
ANISOU 3867 C VAL A 513 2835 1478 4243 -36 -550 190 C
ATOM 3868 O VAL A 513 32.546 13.923 -13.569 1.00 27.22 O
ANISOU 3868 O VAL A 513 3517 2109 4716 -67 -534 130 O
ATOM 3869 CB VAL A 513 30.289 15.882 -12.320 1.00 27.15 C
ANISOU 3869 CB VAL A 513 3489 1947 4880 113 -539 229 C
ATOM 3870 CG1 VAL A 513 29.722 14.507 -12.616 1.00 28.47 C
ANISOU 3870 CG1 VAL A 513 3784 2127 4905 114 -613 180 C
ATOM 3871 CG2 VAL A 513 29.816 16.354 -10.960 1.00 31.70 C
ANISOU 3871 CG2 VAL A 513 4079 2471 5494 172 -402 230 C
ATOM 3872 N PHE A 514 32.663 15.879 -14.668 1.00 27.20 N
ANISOU 3872 N PHE A 514 3332 2076 4925 -57 -662 252 N
ATOM 3873 CA PHE A 514 33.070 15.284 -15.940 1.00 22.79 C
ANISOU 3873 CA PHE A 514 2776 1552 4330 -109 -787 255 C
ATOM 3874 C PHE A 514 34.536 15.522 -16.291 1.00 22.98 C
ANISOU 3874 C PHE A 514 2698 1641 4392 -190 -726 266 C
ATOM 3875 O PHE A 514 34.966 15.126 -17.380 1.00 29.43 O
ANISOU 3875 O PHE A 514 3504 2483 5196 -236 -825 279 O
ATOM 3876 CB PHE A 514 32.203 15.816 -17.087 1.00 23.10 C
ANISOU 3876 CB PHE A 514 2795 1546 4437 -76 -988 316 C
ATOM 3877 CG PHE A 514 30.730 15.635 -16.882 1.00 27.17 C
ANISOU 3877 CG PHE A 514 3400 2007 4915 5 -1067 314 C
ATOM 3878 CD1 PHE A 514 30.182 14.369 -16.754 1.00 27.80 C
ANISOU 3878 CD1 PHE A 514 3611 2090 4861 22 -1085 253 C
ATOM 3879 CD2 PHE A 514 29.887 16.731 -16.851 1.00 31.92 C
ANISOU 3879 CD2 PHE A 514 3951 2562 5614 65 -1127 377 C
ATOM 3880 CE1 PHE A 514 28.820 14.201 -16.577 1.00 22.71 C
ANISOU 3880 CE1 PHE A 514 3047 1404 4178 97 -1158 255 C
ATOM 3881 CE2 PHE A 514 28.523 16.572 -16.675 1.00 35.54 C
ANISOU 3881 CE2 PHE A 514 4488 2981 6034 141 -1201 380 C
ATOM 3882 CZ PHE A 514 27.989 15.304 -16.535 1.00 28.93 C
ANISOU 3882 CZ PHE A 514 3782 2148 5061 156 -1217 319 C
ATOM 3883 N ASP A 515 35.312 16.160 -15.413 1.00 23.34 N
ANISOU 3883 N ASP A 515 2670 1713 4486 -208 -566 262 N
ATOM 3884 CA ASP A 515 36.684 16.520 -15.761 1.00 31.30 C
ANISOU 3884 CA ASP A 515 3567 2790 5536 -281 -512 283 C
ATOM 3885 C ASP A 515 37.596 15.314 -15.965 1.00 31.98 C
ANISOU 3885 C ASP A 515 3693 2952 5506 -351 -471 231 C
ATOM 3886 O ASP A 515 38.711 15.485 -16.474 1.00 33.83 O
ANISOU 3886 O ASP A 515 3838 3248 5766 -415 -453 257 O
ATOM 3887 CB ASP A 515 37.275 17.435 -14.690 1.00 32.96 C
ANISOU 3887 CB ASP A 515 3694 3016 5814 -280 -340 281 C
ATOM 3888 CG ASP A 515 36.649 18.816 -14.693 1.00 41.49 C
ANISOU 3888 CG ASP A 515 4696 4037 7033 -220 -384 353 C
ATOM 3889 OD1 ASP A 515 36.078 19.216 -15.731 1.00 48.86 O
ANISOU 3889 OD1 ASP A 515 5602 4938 8025 -204 -552 417 O
ATOM 3890 OD2 ASP A 515 36.731 19.504 -13.656 1.00 50.11 O
ANISOU 3890 OD2 ASP A 515 5751 5115 8174 -190 -249 345 O
ATOM 3891 N THR A 516 37.151 14.111 -15.605 1.00 28.92 N
ANISOU 3891 N THR A 516 3432 2566 4992 -339 -458 166 N
ATOM 3892 CA THR A 516 37.957 12.906 -15.755 1.00 25.19 C
ANISOU 3892 CA THR A 516 3000 2170 4400 -400 -419 118 C
ATOM 3893 C THR A 516 37.650 12.134 -17.037 1.00 30.11 C
ANISOU 3893 C THR A 516 3676 2785 4981 -405 -588 135 C
ATOM 3894 O THR A 516 38.516 11.391 -17.523 1.00 30.97 O
ANISOU 3894 O THR A 516 3780 2960 5028 -461 -582 126 O
ATOM 3895 CB THR A 516 37.761 12.026 -14.506 1.00 30.67 C
ANISOU 3895 CB THR A 516 3795 2882 4977 -390 -285 32 C
ATOM 3896 OG1 THR A 516 38.833 12.260 -13.586 1.00 37.59 O
ANISOU 3896 OG1 THR A 516 4609 3823 5849 -439 -103 -3 O
ATOM 3897 CG2 THR A 516 37.693 10.543 -14.836 1.00 38.61 C
ANISOU 3897 CG2 THR A 516 4904 3925 5839 -408 -326 -13 C
ATOM 3898 N LEU A 517 36.478 12.351 -17.639 1.00 22.70 N
ANISOU 3898 N LEU A 517 2778 1767 4079 -348 -740 164 N
ATOM 3899 CA LEU A 517 35.969 11.491 -18.709 1.00 20.19 C
ANISOU 3899 CA LEU A 517 2537 1429 3704 -340 -896 160 C
ATOM 3900 C LEU A 517 36.454 11.960 -20.086 1.00 24.30 C
ANISOU 3900 C LEU A 517 2973 1944 4317 -379 -1023 226 C
ATOM 3901 O LEU A 517 35.678 12.328 -20.970 1.00 22.63 O
ANISOU 3901 O LEU A 517 2764 1669 4164 -351 -1182 261 O
ATOM 3902 CB LEU A 517 34.447 11.441 -18.644 1.00 20.32 C
ANISOU 3902 CB LEU A 517 2644 1371 3706 -260 -995 151 C
ATOM 3903 CG LEU A 517 33.893 11.239 -17.231 1.00 28.58 C
ANISOU 3903 CG LEU A 517 3757 2409 4692 -216 -868 103 C
ATOM 3904 CD1 LEU A 517 32.375 11.186 -17.237 1.00 25.71 C
ANISOU 3904 CD1 LEU A 517 3478 1979 4312 -135 -974 104 C
ATOM 3905 CD2 LEU A 517 34.475 9.981 -16.611 1.00 25.74 C
ANISOU 3905 CD2 LEU A 517 3468 2117 4195 -251 -751 32 C
ATOM 3906 N HIS A 518 37.777 11.909 -20.267 1.00 21.97 N
ANISOU 3906 N HIS A 518 2602 1720 4028 -449 -950 242 N
ATOM 3907 CA HIS A 518 38.382 12.355 -21.518 1.00 22.03 C
ANISOU 3907 CA HIS A 518 2519 1727 4125 -496 -1052 310 C
ATOM 3908 C HIS A 518 38.001 11.477 -22.706 1.00 24.86 C
ANISOU 3908 C HIS A 518 2952 2052 4443 -494 -1208 307 C
ATOM 3909 O HIS A 518 38.115 11.924 -23.853 1.00 21.21 O
ANISOU 3909 O HIS A 518 2433 1555 4070 -518 -1332 364 O
ATOM 3910 CB HIS A 518 39.907 12.385 -21.393 1.00 21.95 C
ANISOU 3910 CB HIS A 518 2414 1810 4114 -570 -930 328 C
ATOM 3911 CG HIS A 518 40.413 13.262 -20.291 1.00 32.30 C
ANISOU 3911 CG HIS A 518 3643 3160 5468 -576 -773 328 C
ATOM 3912 ND1 HIS A 518 41.724 13.233 -19.865 1.00 33.68 N
ANISOU 3912 ND1 HIS A 518 3743 3433 5619 -637 -631 324 N
ATOM 3913 CD2 HIS A 518 39.791 14.194 -19.529 1.00 34.56 C
ANISOU 3913 CD2 HIS A 518 3909 3402 5820 -528 -732 330 C
ATOM 3914 CE1 HIS A 518 41.888 14.106 -18.887 1.00 35.73 C
ANISOU 3914 CE1 HIS A 518 3943 3704 5927 -626 -509 317 C
ATOM 3915 NE2 HIS A 518 40.730 14.701 -18.663 1.00 34.50 N
ANISOU 3915 NE2 HIS A 518 3819 3460 5829 -559 -566 322 N
ATOM 3916 N ARG A 519 37.570 10.241 -22.466 1.00 22.00 N
ANISOU 3916 N ARG A 519 2714 1698 3948 -469 -1203 242 N
ATOM 3917 CA ARG A 519 37.229 9.319 -23.541 1.00 23.86 C
ANISOU 3917 CA ARG A 519 3027 1905 4135 -462 -1339 231 C
ATOM 3918 C ARG A 519 35.733 9.110 -23.705 1.00 21.77 C
ANISOU 3918 C ARG A 519 2865 1564 3842 -390 -1461 199 C
ATOM 3919 O ARG A 519 35.323 8.285 -24.530 1.00 21.34 O
ANISOU 3919 O ARG A 519 2880 1518 3709 -354 -1545 183 O
ATOM 3920 CB ARG A 519 37.910 7.967 -23.315 1.00 19.00 C
ANISOU 3920 CB ARG A 519 2470 1366 3382 -488 -1254 186 C
ATOM 3921 CG ARG A 519 39.346 7.918 -23.798 1.00 20.20 C
ANISOU 3921 CG ARG A 519 2530 1587 3559 -562 -1205 231 C
ATOM 3922 CD ARG A 519 40.156 6.929 -22.991 1.00 23.65 C
ANISOU 3922 CD ARG A 519 2993 2129 3864 -591 -1053 186 C
ATOM 3923 NE ARG A 519 40.201 7.308 -21.583 1.00 30.04 N
ANISOU 3923 NE ARG A 519 3789 2976 4649 -587 -899 148 N
ATOM 3924 CZ ARG A 519 41.059 8.182 -21.068 1.00 22.45 C
ANISOU 3924 CZ ARG A 519 2716 2062 3751 -628 -789 174 C
ATOM 3925 NH1 ARG A 519 41.956 8.774 -21.843 1.00 19.49 N
ANISOU 3925 NH1 ARG A 519 2229 1709 3465 -678 -815 244 N
ATOM 3926 NH2 ARG A 519 41.022 8.463 -19.774 1.00 22.67 N
ANISOU 3926 NH2 ARG A 519 2745 2114 3754 -620 -651 130 N
ATOM 3927 N LEU A 520 34.908 9.821 -22.942 1.00 20.16 N
ANISOU 3927 N LEU A 520 2663 1327 3668 -341 -1441 196 N
ATOM 3928 CA LEU A 520 33.465 9.687 -23.078 1.00 23.37 C
ANISOU 3928 CA LEU A 520 3161 1671 4049 -270 -1557 173 C
ATOM 3929 C LEU A 520 33.021 10.126 -24.467 1.00 25.68 C
ANISOU 3929 C LEU A 520 3419 1934 4403 -258 -1728 212 C
ATOM 3930 O LEU A 520 33.370 11.217 -24.927 1.00 22.46 O
ANISOU 3930 O LEU A 520 2905 1502 4128 -290 -1770 274 O
ATOM 3931 CB LEU A 520 32.766 10.518 -22.005 1.00 21.23 C
ANISOU 3931 CB LEU A 520 2876 1379 3812 -221 -1492 179 C
ATOM 3932 CG LEU A 520 31.253 10.360 -21.865 1.00 20.76 C
ANISOU 3932 CG LEU A 520 2910 1269 3708 -141 -1582 156 C
ATOM 3933 CD1 LEU A 520 30.908 8.962 -21.373 1.00 22.73 C
ANISOU 3933 CD1 LEU A 520 3290 1548 3799 -115 -1536 85 C
ATOM 3934 CD2 LEU A 520 30.683 11.426 -20.936 1.00 21.27 C
ANISOU 3934 CD2 LEU A 520 2932 1308 3842 -96 -1525 186 C
ATOM 3935 N GLN A 521 32.256 9.265 -25.136 1.00 20.96 N
ANISOU 3935 N GLN A 521 2909 1347 3707 -209 -1820 180 N
ATOM 3936 CA GLN A 521 31.738 9.558 -26.465 1.00 21.50 C
ANISOU 3936 CA GLN A 521 2966 1382 3821 -183 -1974 214 C
ATOM 3937 C GLN A 521 30.256 9.905 -26.471 1.00 26.13 C
ANISOU 3937 C GLN A 521 3596 1941 4390 -141 -2038 177 C
ATOM 3938 O GLN A 521 29.812 10.655 -27.347 1.00 22.78 O
ANISOU 3938 O GLN A 521 3155 1452 4046 -153 -2088 196 O
ATOM 3939 CB GLN A 521 31.988 8.371 -27.402 1.00 21.16 C
ANISOU 3939 CB GLN A 521 2996 1359 3686 -166 -1970 200 C
ATOM 3940 CG GLN A 521 33.461 8.003 -27.531 1.00 24.74 C
ANISOU 3940 CG GLN A 521 3400 1860 4142 -227 -1887 223 C
ATOM 3941 CD GLN A 521 33.733 7.018 -28.653 1.00 39.06 C
ANISOU 3941 CD GLN A 521 5268 3672 5902 -211 -1911 228 C
ATOM 3942 OE1 GLN A 521 32.833 6.311 -29.109 1.00 42.59 O
ANISOU 3942 OE1 GLN A 521 5805 4104 6273 -160 -1935 187 O
ATOM 3943 NE2 GLN A 521 34.979 6.969 -29.106 1.00 38.69 N
ANISOU 3943 NE2 GLN A 521 5157 3654 5889 -269 -1869 265 N
ATOM 3944 N LEU A 522 29.479 9.388 -25.522 1.00 22.31 N
ANISOU 3944 N LEU A 522 3189 1473 3815 -104 -2019 121 N
ATOM 3945 CA LEU A 522 28.068 9.723 -25.415 1.00 24.85 C
ANISOU 3945 CA LEU A 522 3557 1761 4124 -76 -2068 81 C
ATOM 3946 C LEU A 522 27.749 10.134 -23.985 1.00 23.16 C
ANISOU 3946 C LEU A 522 3340 1549 3912 -32 -1990 98 C
ATOM 3947 O LEU A 522 28.237 9.526 -23.027 1.00 21.20 O
ANISOU 3947 O LEU A 522 3130 1325 3602 -18 -1866 88 O
ATOM 3948 CB LEU A 522 27.176 8.548 -25.841 1.00 27.48 C
ANISOU 3948 CB LEU A 522 4013 2109 4319 -33 -2047 17 C
ATOM 3949 CG LEU A 522 25.671 8.828 -25.809 1.00 32.24 C
ANISOU 3949 CG LEU A 522 4669 2673 4906 5 -2104 -18 C
ATOM 3950 CD1 LEU A 522 24.974 8.262 -27.032 1.00 35.32 C
ANISOU 3950 CD1 LEU A 522 5124 3039 5257 30 -2126 -44 C
ATOM 3951 CD2 LEU A 522 25.045 8.265 -24.549 1.00 32.69 C
ANISOU 3951 CD2 LEU A 522 4795 2764 4861 50 -2064 -57 C
ATOM 3952 N LEU A 523 26.927 11.175 -23.852 1.00 24.10 N
ANISOU 3952 N LEU A 523 3418 1640 4099 -8 -2023 125 N
ATOM 3953 CA LEU A 523 26.441 11.644 -22.557 1.00 27.33 C
ANISOU 3953 CA LEU A 523 3826 2048 4510 51 -1928 150 C
ATOM 3954 C LEU A 523 24.967 11.997 -22.714 1.00 31.29 C
ANISOU 3954 C LEU A 523 4354 2547 4986 94 -2003 139 C
ATOM 3955 O LEU A 523 24.633 13.011 -23.337 1.00 34.84 O
ANISOU 3955 O LEU A 523 4736 2974 5528 80 -2079 174 O
ATOM 3956 CB LEU A 523 27.248 12.847 -22.065 1.00 23.09 C
ANISOU 3956 CB LEU A 523 3175 1482 4118 37 -1859 226 C
ATOM 3957 CG LEU A 523 26.791 13.523 -20.767 1.00 23.35 C
ANISOU 3957 CG LEU A 523 3192 1496 4183 96 -1755 257 C
ATOM 3958 CD1 LEU A 523 26.728 12.529 -19.621 1.00 22.57 C
ANISOU 3958 CD1 LEU A 523 3195 1405 3974 127 -1629 209 C
ATOM 3959 CD2 LEU A 523 27.699 14.690 -20.408 1.00 25.55 C
ANISOU 3959 CD2 LEU A 523 3352 1741 4616 76 -1686 327 C
ATOM 3960 N ASN A 524 24.084 11.163 -22.161 1.00 30.39 N
ANISOU 3960 N ASN A 524 4341 2457 4749 143 -1976 92 N
ATOM 3961 CA ASN A 524 22.640 11.370 -22.251 1.00 31.08 C
ANISOU 3961 CA ASN A 524 4464 2547 4800 187 -2033 79 C
ATOM 3962 C ASN A 524 22.126 11.868 -20.903 1.00 30.21 C
ANISOU 3962 C ASN A 524 4343 2442 4695 253 -1939 125 C
ATOM 3963 O ASN A 524 22.100 11.117 -19.921 1.00 23.16 O
ANISOU 3963 O ASN A 524 3517 1563 3721 285 -1842 106 O
ATOM 3964 CB ASN A 524 21.928 10.085 -22.672 1.00 30.08 C
ANISOU 3964 CB ASN A 524 4455 2437 4538 196 -2068 -3 C
ATOM 3965 CG ASN A 524 20.477 10.320 -23.075 1.00 40.56 C
ANISOU 3965 CG ASN A 524 5814 3758 5840 231 -2136 -19 C
ATOM 3966 OD1 ASN A 524 19.904 11.376 -22.799 1.00 28.24 O
ANISOU 3966 OD1 ASN A 524 4192 2197 4340 259 -2150 36 O
ATOM 3967 ND2 ASN A 524 19.878 9.335 -23.734 1.00 54.39 N
ANISOU 3967 ND2 ASN A 524 7659 5502 7506 235 -2170 -89 N
ATOM 3968 N MET A 525 21.726 13.139 -20.861 1.00 24.67 N
ANISOU 3968 N MET A 525 3559 1723 4092 271 -1961 187 N
ATOM 3969 CA MET A 525 21.072 13.736 -19.703 1.00 26.62 C
ANISOU 3969 CA MET A 525 3791 1966 4356 340 -1883 236 C
ATOM 3970 C MET A 525 19.703 14.293 -20.081 1.00 35.08 C
ANISOU 3970 C MET A 525 4857 3054 5420 376 -1969 254 C
ATOM 3971 O MET A 525 19.232 15.273 -19.498 1.00 39.15 O
ANISOU 3971 O MET A 525 5314 3562 5997 422 -1940 319 O
ATOM 3972 CB MET A 525 21.940 14.829 -19.083 1.00 28.13 C
ANISOU 3972 CB MET A 525 3881 2123 4685 339 -1799 306 C
ATOM 3973 CG MET A 525 23.170 14.306 -18.361 1.00 33.08 C
ANISOU 3973 CG MET A 525 4524 2729 5318 316 -1673 290 C
ATOM 3974 SD MET A 525 24.024 15.594 -17.435 1.00 48.11 S
ANISOU 3974 SD MET A 525 6316 4581 7384 324 -1546 363 S
ATOM 3975 CE MET A 525 24.496 16.716 -18.749 1.00 38.03 C
ANISOU 3975 CE MET A 525 4907 3307 6236 271 -1673 416 C
ATOM 3976 N SER A 526 19.055 13.672 -21.062 1.00 28.07 N
ANISOU 3976 N SER A 526 4027 2182 4455 357 -2069 195 N
ATOM 3977 CA SER A 526 17.725 14.089 -21.468 1.00 32.30 C
ANISOU 3977 CA SER A 526 4566 2735 4972 390 -2146 203 C
ATOM 3978 C SER A 526 16.687 13.636 -20.447 1.00 31.85 C
ANISOU 3978 C SER A 526 4573 2708 4821 464 -2085 207 C
ATOM 3979 O SER A 526 16.915 12.722 -19.649 1.00 31.54 O
ANISOU 3979 O SER A 526 4600 2676 4707 481 -2001 180 O
ATOM 3980 CB SER A 526 17.380 13.525 -22.845 1.00 34.23 C
ANISOU 3980 CB SER A 526 4862 2971 5172 347 -2253 132 C
ATOM 3981 OG SER A 526 17.161 12.125 -22.781 1.00 36.09 O
ANISOU 3981 OG SER A 526 5208 3221 5283 356 -2229 58 O
ATOM 3982 N HIS A 527 15.528 14.295 -20.488 1.00 31.13 N
ANISOU 3982 N HIS A 527 4458 2637 4733 508 -2129 245 N
ATOM 3983 CA HIS A 527 14.392 13.958 -19.629 1.00 29.69 C
ANISOU 3983 CA HIS A 527 4327 2488 4466 580 -2085 260 C
ATOM 3984 C HIS A 527 14.748 14.070 -18.147 1.00 28.47 C
ANISOU 3984 C HIS A 527 4166 2317 4334 626 -1947 312 C
ATOM 3985 O HIS A 527 14.337 13.249 -17.326 1.00 27.15 O
ANISOU 3985 O HIS A 527 4073 2163 4080 663 -1878 298 O
ATOM 3986 CB HIS A 527 13.840 12.569 -19.963 1.00 31.57 C
ANISOU 3986 CB HIS A 527 4677 2752 4568 577 -2107 174 C
ATOM 3987 CG HIS A 527 13.308 12.458 -21.358 1.00 35.39 C
ANISOU 3987 CG HIS A 527 5176 3238 5033 546 -2223 122 C
ATOM 3988 ND1 HIS A 527 12.026 12.834 -21.697 1.00 38.62 N
ANISOU 3988 ND1 HIS A 527 5579 3679 5417 583 -2285 139 N
ATOM 3989 CD2 HIS A 527 13.885 12.017 -22.501 1.00 33.76 C
ANISOU 3989 CD2 HIS A 527 4993 3001 4834 485 -2282 58 C
ATOM 3990 CE1 HIS A 527 11.836 12.627 -22.987 1.00 36.79 C
ANISOU 3990 CE1 HIS A 527 5368 3432 5178 545 -2374 83 C
ATOM 3991 NE2 HIS A 527 12.948 12.132 -23.498 1.00 36.04 N
ANISOU 3991 NE2 HIS A 527 5293 3293 5107 487 -2371 34 N
ATOM 3992 N ASN A 528 15.524 15.095 -17.809 1.00 27.85 N
ANISOU 3992 N ASN A 528 4000 2203 4378 622 -1901 373 N
ATOM 3993 CA ASN A 528 15.737 15.516 -16.430 1.00 29.22 C
ANISOU 3993 CA ASN A 528 4153 2345 4603 674 -1764 433 C
ATOM 3994 C ASN A 528 15.084 16.889 -16.227 1.00 32.00 C
ANISOU 3994 C ASN A 528 4417 2697 5044 725 -1774 524 C
ATOM 3995 O ASN A 528 14.274 17.342 -17.041 1.00 38.37 O
ANISOU 3995 O ASN A 528 5195 3541 5845 728 -1885 537 O
ATOM 3996 CB ASN A 528 17.228 15.524 -16.082 1.00 29.71 C
ANISOU 3996 CB ASN A 528 4190 2361 4737 631 -1677 424 C
ATOM 3997 CG ASN A 528 17.803 14.122 -15.952 1.00 32.21 C
ANISOU 3997 CG ASN A 528 4602 2681 4956 597 -1635 346 C
ATOM 3998 OD1 ASN A 528 17.511 13.409 -14.995 1.00 29.29 O
ANISOU 3998 OD1 ASN A 528 4305 2308 4514 631 -1544 333 O
ATOM 3999 ND2 ASN A 528 18.629 13.726 -16.915 1.00 31.84 N
ANISOU 3999 ND2 ASN A 528 4553 2641 4905 528 -1699 297 N
ATOM 4000 N ASN A 529 15.442 17.554 -15.131 1.00 29.27 N
ANISOU 4000 N ASN A 529 4030 2309 4782 766 -1653 585 N
ATOM 4001 CA ASN A 529 14.884 18.853 -14.768 1.00 31.86 C
ANISOU 4001 CA ASN A 529 4274 2633 5196 826 -1640 677 C
ATOM 4002 C ASN A 529 15.984 19.896 -14.602 1.00 36.53 C
ANISOU 4002 C ASN A 529 4767 3180 5933 807 -1585 718 C
ATOM 4003 O ASN A 529 15.954 20.715 -13.681 1.00 41.41 O
ANISOU 4003 O ASN A 529 5339 3766 6630 862 -1488 784 O
ATOM 4004 CB ASN A 529 14.053 18.754 -13.489 1.00 31.47 C
ANISOU 4004 CB ASN A 529 4269 2573 5114 911 -1533 723 C
ATOM 4005 CG ASN A 529 12.834 17.870 -13.649 1.00 33.89 C
ANISOU 4005 CG ASN A 529 4656 2934 5286 936 -1591 699 C
ATOM 4006 OD1 ASN A 529 12.126 17.942 -14.653 1.00 39.19 O
ANISOU 4006 OD1 ASN A 529 5315 3659 5915 924 -1720 688 O
ATOM 4007 ND2 ASN A 529 12.578 17.033 -12.652 1.00 30.18 N
ANISOU 4007 ND2 ASN A 529 4267 2448 4752 969 -1491 689 N
ATOM 4008 N LEU A 530 16.978 19.865 -15.488 1.00 33.62 N
ANISOU 4008 N LEU A 530 4363 2808 5602 728 -1643 680 N
ATOM 4009 CA LEU A 530 18.094 20.800 -15.407 1.00 31.09 C
ANISOU 4009 CA LEU A 530 3941 2451 5420 702 -1594 718 C
ATOM 4010 C LEU A 530 17.611 22.235 -15.574 1.00 31.70 C
ANISOU 4010 C LEU A 530 3910 2543 5592 737 -1634 804 C
ATOM 4011 O LEU A 530 16.924 22.567 -16.545 1.00 34.65 O
ANISOU 4011 O LEU A 530 4257 2962 5948 724 -1766 813 O
ATOM 4012 CB LEU A 530 19.139 20.467 -16.474 1.00 29.85 C
ANISOU 4012 CB LEU A 530 3765 2297 5279 609 -1667 668 C
ATOM 4013 CG LEU A 530 19.811 19.101 -16.315 1.00 34.96 C
ANISOU 4013 CG LEU A 530 4509 2932 5842 571 -1619 587 C
ATOM 4014 CD1 LEU A 530 20.703 18.782 -17.508 1.00 28.17 C
ANISOU 4014 CD1 LEU A 530 3629 2082 4992 483 -1709 545 C
ATOM 4015 CD2 LEU A 530 20.598 19.045 -15.016 1.00 29.33 C
ANISOU 4015 CD2 LEU A 530 3803 2166 5174 590 -1444 592 C
ATOM 4016 N LEU A 531 17.968 23.086 -14.612 1.00 32.15 N
ANISOU 4016 N LEU A 531 3904 2561 5750 781 -1515 863 N
ATOM 4017 CA LEU A 531 17.574 24.490 -14.616 1.00 36.17 C
ANISOU 4017 CA LEU A 531 4305 3083 6354 822 -1533 951 C
ATOM 4018 C LEU A 531 18.642 25.406 -15.193 1.00 36.08 C
ANISOU 4018 C LEU A 531 4172 3066 6472 767 -1553 979 C
ATOM 4019 O LEU A 531 18.307 26.416 -15.820 1.00 40.40 O
ANISOU 4019 O LEU A 531 4628 3646 7074 767 -1636 1035 O
ATOM 4020 CB LEU A 531 17.241 24.944 -13.190 1.00 35.27 C
ANISOU 4020 CB LEU A 531 4193 2931 6278 912 -1385 1004 C
ATOM 4021 CG LEU A 531 16.216 24.085 -12.451 1.00 38.00 C
ANISOU 4021 CG LEU A 531 4656 3277 6507 972 -1343 988 C
ATOM 4022 CD1 LEU A 531 16.206 24.426 -10.965 1.00 33.99 C
ANISOU 4022 CD1 LEU A 531 4158 2709 6049 1044 -1172 1027 C
ATOM 4023 CD2 LEU A 531 14.836 24.262 -13.071 1.00 34.41 C
ANISOU 4023 CD2 LEU A 531 4204 2890 5982 1008 -1470 1021 C
ATOM 4024 N PHE A 532 19.911 25.075 -14.980 1.00 34.72 N
ANISOU 4024 N PHE A 532 3992 2854 6346 719 -1474 944 N
ATOM 4025 CA PHE A 532 21.023 25.788 -15.588 1.00 33.06 C
ANISOU 4025 CA PHE A 532 3669 2642 6252 658 -1493 968 C
ATOM 4026 C PHE A 532 22.135 24.792 -15.865 1.00 34.08 C
ANISOU 4026 C PHE A 532 3841 2751 6356 585 -1477 897 C
ATOM 4027 O PHE A 532 22.195 23.715 -15.266 1.00 36.26 O
ANISOU 4027 O PHE A 532 4223 3004 6549 591 -1406 837 O
ATOM 4028 CB PHE A 532 21.556 26.915 -14.692 1.00 46.65 C
ANISOU 4028 CB PHE A 532 5286 4331 8107 701 -1362 1035 C
ATOM 4029 CG PHE A 532 20.648 28.105 -14.599 1.00 60.34 C
ANISOU 4029 CG PHE A 532 6948 6092 9888 764 -1389 1118 C
ATOM 4030 CD1 PHE A 532 20.677 29.094 -15.570 1.00 60.02 C
ANISOU 4030 CD1 PHE A 532 6796 6093 9915 731 -1497 1171 C
ATOM 4031 CD2 PHE A 532 19.776 28.247 -13.531 1.00 64.72 C
ANISOU 4031 CD2 PHE A 532 7545 6630 10417 855 -1304 1147 C
ATOM 4032 CE1 PHE A 532 19.842 30.197 -15.487 1.00 56.53 C
ANISOU 4032 CE1 PHE A 532 6286 5681 9512 789 -1521 1249 C
ATOM 4033 CE2 PHE A 532 18.940 29.347 -13.439 1.00 61.13 C
ANISOU 4033 CE2 PHE A 532 7021 6202 10002 917 -1328 1228 C
ATOM 4034 CZ PHE A 532 18.975 30.324 -14.419 1.00 59.23 C
ANISOU 4034 CZ PHE A 532 6670 6010 9827 885 -1437 1279 C
ATOM 4035 N LEU A 533 23.018 25.165 -16.781 1.00 35.99 N
ANISOU 4035 N LEU A 533 3998 3004 6671 513 -1541 907 N
ATOM 4036 CA LEU A 533 24.270 24.458 -16.986 1.00 31.70 C
ANISOU 4036 CA LEU A 533 3466 2442 6137 446 -1508 861 C
ATOM 4037 C LEU A 533 25.423 25.358 -16.567 1.00 33.46 C
ANISOU 4037 C LEU A 533 3564 2642 6507 437 -1402 912 C
ATOM 4038 O LEU A 533 25.292 26.584 -16.502 1.00 37.19 O
ANISOU 4038 O LEU A 533 3929 3124 7077 465 -1397 985 O
ATOM 4039 CB LEU A 533 24.437 24.030 -18.447 1.00 30.83 C
ANISOU 4039 CB LEU A 533 3363 2364 5988 364 -1665 828 C
ATOM 4040 CG LEU A 533 23.438 23.018 -19.009 1.00 36.76 C
ANISOU 4040 CG LEU A 533 4236 3138 6592 361 -1768 763 C
ATOM 4041 CD1 LEU A 533 23.743 22.716 -20.471 1.00 30.30 C
ANISOU 4041 CD1 LEU A 533 3414 2338 5761 275 -1907 731 C
ATOM 4042 CD2 LEU A 533 23.429 21.738 -18.187 1.00 35.33 C
ANISOU 4042 CD2 LEU A 533 4182 2940 6302 386 -1679 696 C
ATOM 4043 N ASP A 534 26.556 24.735 -16.267 1.00 37.03 N
ANISOU 4043 N ASP A 534 4032 3066 6973 398 -1312 873 N
ATOM 4044 CA ASP A 534 27.793 25.451 -15.996 1.00 46.46 C
ANISOU 4044 CA ASP A 534 5115 4278 8261 358 -1189 892 C
ATOM 4045 C ASP A 534 28.778 25.178 -17.123 1.00 43.53 C
ANISOU 4045 C ASP A 534 4702 3949 7887 257 -1262 876 C
ATOM 4046 O ASP A 534 28.847 24.060 -17.645 1.00 44.27 O
ANISOU 4046 O ASP A 534 4889 4051 7882 213 -1322 815 O
ATOM 4047 CB ASP A 534 28.393 25.042 -14.645 1.00 47.35 C
ANISOU 4047 CB ASP A 534 5275 4379 8336 364 -969 830 C
ATOM 4048 CG ASP A 534 29.470 26.006 -14.164 1.00 61.69 C
ANISOU 4048 CG ASP A 534 6967 6215 10255 346 -825 855 C
ATOM 4049 OD1 ASP A 534 29.833 26.930 -14.921 1.00 69.50 O
ANISOU 4049 OD1 ASP A 534 7833 7233 11340 323 -896 922 O
ATOM 4050 OD2 ASP A 534 29.952 25.839 -13.022 1.00 68.26 O
ANISOU 4050 OD2 ASP A 534 7826 7037 11072 354 -641 806 O
ATOM 4051 N SER A 535 29.538 26.209 -17.500 1.00 43.95 N
ANISOU 4051 N SER A 535 4614 4030 8053 223 -1255 936 N
ATOM 4052 CA SER A 535 30.451 26.091 -18.630 1.00 48.66 C
ANISOU 4052 CA SER A 535 5157 4666 8667 129 -1332 938 C
ATOM 4053 C SER A 535 31.661 25.218 -18.316 1.00 47.36 C
ANISOU 4053 C SER A 535 5030 4535 8430 62 -1200 865 C
ATOM 4054 O SER A 535 32.326 24.748 -19.245 1.00 48.76 O
ANISOU 4054 O SER A 535 5201 4740 8587 -15 -1267 853 O
ATOM 4055 CB SER A 535 30.905 27.482 -19.074 1.00 56.84 C
ANISOU 4055 CB SER A 535 6024 5728 9845 113 -1356 1030 C
ATOM 4056 OG SER A 535 31.630 27.420 -20.289 1.00 64.92 O
ANISOU 4056 OG SER A 535 6992 6782 10892 23 -1457 1046 O
ATOM 4057 N SER A 536 31.952 24.979 -17.037 1.00 48.59 N
ANISOU 4057 N SER A 536 5226 4689 8548 88 -1015 817 N
ATOM 4058 CA SER A 536 33.155 24.249 -16.657 1.00 50.62 C
ANISOU 4058 CA SER A 536 5505 4989 8740 22 -878 748 C
ATOM 4059 C SER A 536 33.019 22.741 -16.826 1.00 44.50 C
ANISOU 4059 C SER A 536 4871 4214 7822 -5 -909 668 C
ATOM 4060 O SER A 536 34.035 22.053 -16.969 1.00 48.53 O
ANISOU 4060 O SER A 536 5390 4773 8275 -76 -853 624 O
ATOM 4061 CB SER A 536 33.524 24.570 -15.206 1.00 58.93 C
ANISOU 4061 CB SER A 536 6546 6040 9805 56 -665 719 C
ATOM 4062 OG SER A 536 32.560 24.058 -14.301 1.00 68.02 O
ANISOU 4062 OG SER A 536 7812 7137 10893 124 -621 678 O
ATOM 4063 N HIS A 537 31.791 22.216 -16.825 1.00 40.17 N
ANISOU 4063 N HIS A 537 4429 3621 7214 50 -999 652 N
ATOM 4064 CA HIS A 537 31.568 20.775 -16.858 1.00 46.54 C
ANISOU 4064 CA HIS A 537 5375 4429 7880 36 -1017 575 C
ATOM 4065 C HIS A 537 31.946 20.134 -18.188 1.00 50.46 C
ANISOU 4065 C HIS A 537 5882 4949 8340 -31 -1154 568 C
ATOM 4066 O HIS A 537 32.061 18.905 -18.248 1.00 57.74 O
ANISOU 4066 O HIS A 537 6905 5886 9146 -56 -1149 502 O
ATOM 4067 CB HIS A 537 30.101 20.470 -16.549 1.00 47.37 C
ANISOU 4067 CB HIS A 537 5581 4482 7934 118 -1084 569 C
ATOM 4068 CG HIS A 537 29.645 20.960 -15.211 1.00 49.81 C
ANISOU 4068 CG HIS A 537 5896 4758 8271 189 -949 576 C
ATOM 4069 ND1 HIS A 537 28.341 21.330 -14.961 1.00 51.75 N
ANISOU 4069 ND1 HIS A 537 6170 4958 8535 275 -1012 616 N
ATOM 4070 CD2 HIS A 537 30.313 21.131 -14.045 1.00 51.67 C
ANISOU 4070 CD2 HIS A 537 6114 4998 8521 187 -754 547 C
ATOM 4071 CE1 HIS A 537 28.227 21.715 -13.703 1.00 53.49 C
ANISOU 4071 CE1 HIS A 537 6389 5150 8784 325 -860 617 C
ATOM 4072 NE2 HIS A 537 29.410 21.603 -13.125 1.00 52.91 N
ANISOU 4072 NE2 HIS A 537 6290 5102 8710 272 -701 571 N
ATOM 4073 N TYR A 538 32.153 20.920 -19.244 1.00 49.12 N
ANISOU 4073 N TYR A 538 5611 4784 8269 -62 -1271 634 N
ATOM 4074 CA TYR A 538 32.322 20.380 -20.587 1.00 40.48 C
ANISOU 4074 CA TYR A 538 4531 3695 7155 -118 -1422 634 C
ATOM 4075 C TYR A 538 33.661 20.751 -21.214 1.00 36.40 C
ANISOU 4075 C TYR A 538 3902 3223 6705 -202 -1401 670 C
ATOM 4076 O TYR A 538 33.832 20.580 -22.426 1.00 45.44 O
ANISOU 4076 O TYR A 538 5031 4364 7869 -250 -1534 690 O
ATOM 4077 CB TYR A 538 31.166 20.846 -21.480 1.00 43.73 C
ANISOU 4077 CB TYR A 538 4939 4061 7614 -83 -1618 677 C
ATOM 4078 CG TYR A 538 29.807 20.599 -20.860 1.00 47.14 C
ANISOU 4078 CG TYR A 538 5469 4456 7985 4 -1642 655 C
ATOM 4079 CD1 TYR A 538 29.233 21.529 -20.003 1.00 56.96 C
ANISOU 4079 CD1 TYR A 538 6669 5684 9290 73 -1582 698 C
ATOM 4080 CD2 TYR A 538 29.106 19.431 -21.119 1.00 49.17 C
ANISOU 4080 CD2 TYR A 538 5860 4698 8124 22 -1718 594 C
ATOM 4081 CE1 TYR A 538 27.993 21.306 -19.424 1.00 64.53 C
ANISOU 4081 CE1 TYR A 538 7713 6612 10195 154 -1601 686 C
ATOM 4082 CE2 TYR A 538 27.864 19.198 -20.546 1.00 56.24 C
ANISOU 4082 CE2 TYR A 538 6841 5579 8948 97 -1728 572 C
ATOM 4083 CZ TYR A 538 27.312 20.139 -19.700 1.00 66.22 C
ANISOU 4083 CZ TYR A 538 8058 6831 10272 160 -1667 618 C
ATOM 4084 OH TYR A 538 26.078 19.913 -19.128 1.00 69.68 O
ANISOU 4084 OH TYR A 538 8577 7275 10625 227 -1660 596 O
ATOM 4085 N ASN A 539 34.617 21.230 -20.420 1.00 34.57 N
ANISOU 4085 N ASN A 539 3593 3036 6508 -221 -1235 677 N
ATOM 4086 CA ASN A 539 35.905 21.669 -20.940 1.00 39.17 C
ANISOU 4086 CA ASN A 539 4057 3671 7155 -297 -1204 718 C
ATOM 4087 C ASN A 539 36.896 20.531 -21.156 1.00 36.06 C
ANISOU 4087 C ASN A 539 3708 3329 6667 -365 -1154 669 C
ATOM 4088 O ASN A 539 37.972 20.771 -21.717 1.00 38.46 O
ANISOU 4088 O ASN A 539 3917 3680 7014 -432 -1142 708 O
ATOM 4089 CB ASN A 539 36.519 22.705 -19.994 1.00 45.90 C
ANISOU 4089 CB ASN A 539 4801 4557 8082 -285 -1045 746 C
ATOM 4090 CG ASN A 539 35.655 23.943 -19.838 1.00 53.84 C
ANISOU 4090 CG ASN A 539 5742 5520 9196 -219 -1092 810 C
ATOM 4091 OD1 ASN A 539 35.597 24.541 -18.765 1.00 66.89 O
ANISOU 4091 OD1 ASN A 539 7366 7170 10880 -170 -963 810 O
ATOM 4092 ND2 ASN A 539 34.979 24.335 -20.913 1.00 52.89 N
ANISOU 4092 ND2 ASN A 539 5594 5367 9133 -217 -1277 865 N
ATOM 4093 N GLN A 540 36.574 19.305 -20.727 1.00 35.14 N
ANISOU 4093 N GLN A 540 3726 3208 6419 -348 -1122 590 N
ATOM 4094 CA GLN A 540 37.494 18.178 -20.848 1.00 32.83 C
ANISOU 4094 CA GLN A 540 3477 2971 6028 -408 -1065 543 C
ATOM 4095 C GLN A 540 36.822 16.949 -21.450 1.00 33.48 C
ANISOU 4095 C GLN A 540 3691 3022 6009 -397 -1181 498 C
ATOM 4096 O GLN A 540 37.338 15.834 -21.312 1.00 31.81 O
ANISOU 4096 O GLN A 540 3545 2853 5688 -426 -1122 445 O
ATOM 4097 CB GLN A 540 38.113 17.827 -19.493 1.00 26.73 C
ANISOU 4097 CB GLN A 540 2723 2252 5180 -411 -858 482 C
ATOM 4098 CG GLN A 540 38.940 18.946 -18.892 1.00 34.10 C
ANISOU 4098 CG GLN A 540 3526 3227 6203 -426 -729 516 C
ATOM 4099 CD GLN A 540 39.948 18.449 -17.877 1.00 38.58 C
ANISOU 4099 CD GLN A 540 4098 3871 6690 -462 -534 453 C
ATOM 4100 OE1 GLN A 540 40.738 17.546 -18.154 1.00 47.21 O
ANISOU 4100 OE1 GLN A 540 5211 5026 7699 -520 -510 426 O
ATOM 4101 NE2 GLN A 540 39.927 19.041 -16.688 1.00 31.37 N
ANISOU 4101 NE2 GLN A 540 3163 2954 5802 -428 -392 429 N
ATOM 4102 N LEU A 541 35.687 17.128 -22.124 1.00 31.88 N
ANISOU 4102 N LEU A 541 3525 2751 5836 -356 -1344 517 N
ATOM 4103 CA LEU A 541 35.044 16.041 -22.860 1.00 29.82 C
ANISOU 4103 CA LEU A 541 3381 2459 5491 -346 -1470 476 C
ATOM 4104 C LEU A 541 35.634 16.000 -24.274 1.00 28.41 C
ANISOU 4104 C LEU A 541 3152 2277 5365 -410 -1591 518 C
ATOM 4105 O LEU A 541 34.978 16.281 -25.280 1.00 24.46 O
ANISOU 4105 O LEU A 541 2650 1722 4921 -404 -1758 545 O
ATOM 4106 CB LEU A 541 33.531 16.217 -22.854 1.00 28.27 C
ANISOU 4106 CB LEU A 541 3252 2198 5293 -270 -1581 470 C
ATOM 4107 CG LEU A 541 32.911 16.137 -21.452 1.00 31.04 C
ANISOU 4107 CG LEU A 541 3663 2547 5585 -205 -1460 431 C
ATOM 4108 CD1 LEU A 541 31.403 16.319 -21.470 1.00 33.38 C
ANISOU 4108 CD1 LEU A 541 4020 2786 5877 -127 -1573 434 C
ATOM 4109 CD2 LEU A 541 33.272 14.817 -20.780 1.00 22.79 C
ANISOU 4109 CD2 LEU A 541 2719 1541 4398 -215 -1347 354 C
ATOM 4110 N TYR A 542 36.919 15.633 -24.328 1.00 25.96 N
ANISOU 4110 N TYR A 542 2798 2029 5035 -473 -1501 522 N
ATOM 4111 CA TYR A 542 37.671 15.697 -25.579 1.00 32.33 C
ANISOU 4111 CA TYR A 542 3541 2846 5896 -532 -1582 575 C
ATOM 4112 C TYR A 542 37.095 14.765 -26.639 1.00 34.06 C
ANISOU 4112 C TYR A 542 3871 3042 6029 -495 -1703 548 C
ATOM 4113 O TYR A 542 37.172 15.064 -27.837 1.00 32.23 O
ANISOU 4113 O TYR A 542 3618 2792 5835 -492 -1790 597 O
ATOM 4114 CB TYR A 542 39.141 15.357 -25.323 1.00 31.56 C
ANISOU 4114 CB TYR A 542 3389 2841 5760 -589 -1438 581 C
ATOM 4115 CG TYR A 542 39.849 16.246 -24.314 1.00 32.68 C
ANISOU 4115 CG TYR A 542 3421 3034 5963 -614 -1288 604 C
ATOM 4116 CD1 TYR A 542 40.228 17.542 -24.640 1.00 37.23 C
ANISOU 4116 CD1 TYR A 542 3861 3614 6670 -634 -1302 683 C
ATOM 4117 CD2 TYR A 542 40.169 15.774 -23.047 1.00 28.49 C
ANISOU 4117 CD2 TYR A 542 2930 2560 5336 -602 -1117 541 C
ATOM 4118 CE1 TYR A 542 40.887 18.351 -23.725 1.00 38.69 C
ANISOU 4118 CE1 TYR A 542 3947 3854 6898 -644 -1155 699 C
ATOM 4119 CE2 TYR A 542 40.824 16.575 -22.125 1.00 32.33 C
ANISOU 4119 CE2 TYR A 542 3324 3098 5860 -612 -967 552 C
ATOM 4120 CZ TYR A 542 41.181 17.861 -22.469 1.00 39.62 C
ANISOU 4120 CZ TYR A 542 4111 4023 6918 -630 -985 631 C
ATOM 4121 OH TYR A 542 41.836 18.661 -21.559 1.00 47.84 O
ANISOU 4121 OH TYR A 542 5060 5118 7998 -635 -833 638 O
ATOM 4122 N SER A 543 36.514 13.644 -26.226 1.00 31.22 N
ANISOU 4122 N SER A 543 3636 2675 5551 -463 -1699 474 N
ATOM 4123 CA SER A 543 36.033 12.631 -27.151 1.00 27.52 C
ANISOU 4123 CA SER A 543 3273 2196 4988 -424 -1790 444 C
ATOM 4124 C SER A 543 34.532 12.712 -27.392 1.00 26.85 C
ANISOU 4124 C SER A 543 3262 2043 4895 -356 -1920 421 C
ATOM 4125 O SER A 543 34.008 11.933 -28.196 1.00 26.21 O
ANISOU 4125 O SER A 543 3274 1943 4742 -315 -1994 399 O
ATOM 4126 CB SER A 543 36.401 11.236 -26.632 1.00 24.71 C
ANISOU 4126 CB SER A 543 3006 1892 4490 -428 -1699 380 C
ATOM 4127 OG SER A 543 37.792 11.138 -26.374 1.00 24.46 O
ANISOU 4127 OG SER A 543 2904 1929 4461 -494 -1578 401 O
ATOM 4128 N LEU A 544 33.836 13.645 -26.742 1.00 25.61 N
ANISOU 4128 N LEU A 544 3067 1846 4816 -343 -1945 431 N
ATOM 4129 CA LEU A 544 32.378 13.634 -26.751 1.00 25.84 C
ANISOU 4129 CA LEU A 544 3171 1824 4821 -280 -2058 400 C
ATOM 4130 C LEU A 544 31.844 13.854 -28.157 1.00 24.45 C
ANISOU 4130 C LEU A 544 3031 1601 4658 -277 -2138 409 C
ATOM 4131 O LEU A 544 32.093 14.894 -28.771 1.00 26.97 O
ANISOU 4131 O LEU A 544 3268 1883 5095 -310 -2174 470 O
ATOM 4132 CB LEU A 544 31.832 14.703 -25.808 1.00 26.25 C
ANISOU 4132 CB LEU A 544 3174 1841 4960 -262 -2032 423 C
ATOM 4133 CG LEU A 544 30.351 14.513 -25.482 1.00 30.78 C
ANISOU 4133 CG LEU A 544 3836 2413 5446 -195 -2071 368 C
ATOM 4134 CD1 LEU A 544 30.140 13.224 -24.693 1.00 23.31 C
ANISOU 4134 CD1 LEU A 544 3013 1495 4347 -154 -1988 300 C
ATOM 4135 CD2 LEU A 544 29.807 15.711 -24.726 1.00 24.88 C
ANISOU 4135 CD2 LEU A 544 3024 1653 4775 -151 -2035 416 C
ATOM 4136 N LYS A 545 31.101 12.868 -28.655 1.00 24.22 N
ANISOU 4136 N LYS A 545 3122 1570 4509 -243 -2158 342 N
ATOM 4137 CA LYS A 545 30.460 12.946 -29.961 1.00 25.49 C
ANISOU 4137 CA LYS A 545 3325 1683 4676 -241 -2230 332 C
ATOM 4138 C LYS A 545 28.980 13.280 -29.888 1.00 30.49 C
ANISOU 4138 C LYS A 545 4010 2275 5299 -218 -2295 285 C
ATOM 4139 O LYS A 545 28.462 13.936 -30.798 1.00 29.80 O
ANISOU 4139 O LYS A 545 3913 2134 5276 -228 -2373 301 O
ATOM 4140 CB LYS A 545 30.621 11.622 -30.717 1.00 24.47 C
ANISOU 4140 CB LYS A 545 3283 1576 4437 -218 -2213 295 C
ATOM 4141 CG LYS A 545 32.053 11.177 -30.938 1.00 28.25 C
ANISOU 4141 CG LYS A 545 3718 2096 4921 -245 -2166 339 C
ATOM 4142 CD LYS A 545 32.082 9.870 -31.715 1.00 26.34 C
ANISOU 4142 CD LYS A 545 3561 1868 4577 -222 -2157 300 C
ATOM 4143 CE LYS A 545 33.492 9.328 -31.877 1.00 32.69 C
ANISOU 4143 CE LYS A 545 4329 2713 5380 -254 -2111 340 C
ATOM 4144 NZ LYS A 545 33.478 8.013 -32.571 1.00 35.43 N
ANISOU 4144 NZ LYS A 545 4760 3073 5629 -230 -2101 301 N
ATOM 4145 N GLU A 546 28.284 12.840 -28.843 1.00 24.91 N
ANISOU 4145 N GLU A 546 3358 1594 4512 -185 -2271 230 N
ATOM 4146 CA GLU A 546 26.834 12.978 -28.765 1.00 28.93 C
ANISOU 4146 CA GLU A 546 3930 2071 4993 -151 -2333 185 C
ATOM 4147 C GLU A 546 26.446 13.456 -27.374 1.00 31.18 C
ANISOU 4147 C GLU A 546 4180 2384 5282 -130 -2311 188 C
ATOM 4148 O GLU A 546 26.836 12.850 -26.371 1.00 31.79 O
ANISOU 4148 O GLU A 546 4272 2513 5292 -108 -2234 174 O
ATOM 4149 CB GLU A 546 26.140 11.654 -29.107 1.00 24.92 C
ANISOU 4149 CB GLU A 546 3547 1581 4340 -102 -2316 114 C
ATOM 4150 CG GLU A 546 26.411 11.182 -30.537 1.00 35.46 C
ANISOU 4150 CG GLU A 546 4908 2896 5668 -104 -2335 119 C
ATOM 4151 CD GLU A 546 25.772 9.845 -30.850 1.00 47.41 C
ANISOU 4151 CD GLU A 546 6532 4430 7052 -52 -2310 57 C
ATOM 4152 OE1 GLU A 546 24.804 9.478 -30.156 1.00 54.85 O
ANISOU 4152 OE1 GLU A 546 7537 5385 7917 -13 -2300 9 O
ATOM 4153 OE2 GLU A 546 26.240 9.158 -31.785 1.00 57.46 O
ANISOU 4153 OE2 GLU A 546 7824 5705 8301 -49 -2301 60 O
ATOM 4154 N LEU A 547 25.679 14.545 -27.323 1.00 30.96 N
ANISOU 4154 N LEU A 547 4098 2353 5313 -110 -2349 223 N
ATOM 4155 CA LEU A 547 25.274 15.187 -26.077 1.00 29.99 C
ANISOU 4155 CA LEU A 547 3926 2273 5194 -56 -2292 259 C
ATOM 4156 C LEU A 547 23.771 15.424 -26.129 1.00 31.43 C
ANISOU 4156 C LEU A 547 4156 2458 5331 -7 -2343 239 C
ATOM 4157 O LEU A 547 23.297 16.261 -26.907 1.00 31.84 O
ANISOU 4157 O LEU A 547 4166 2484 5448 -22 -2419 265 O
ATOM 4158 CB LEU A 547 26.036 16.497 -25.871 1.00 26.67 C
ANISOU 4158 CB LEU A 547 3364 1850 4918 -78 -2268 348 C
ATOM 4159 CG LEU A 547 25.672 17.376 -24.672 1.00 26.98 C
ANISOU 4159 CG LEU A 547 3344 1910 4997 -14 -2196 403 C
ATOM 4160 CD1 LEU A 547 25.818 16.606 -23.373 1.00 26.10 C
ANISOU 4160 CD1 LEU A 547 3294 1816 4806 39 -2075 381 C
ATOM 4161 CD2 LEU A 547 26.537 18.625 -24.654 1.00 27.63 C
ANISOU 4161 CD2 LEU A 547 3283 1984 5232 -43 -2173 489 C
ATOM 4162 N ALA A 548 23.024 14.692 -25.305 1.00 30.56 N
ANISOU 4162 N ALA A 548 4128 2379 5105 53 -2298 199 N
ATOM 4163 CA ALA A 548 21.572 14.804 -25.247 1.00 29.72 C
ANISOU 4163 CA ALA A 548 4068 2284 4941 106 -2336 184 C
ATOM 4164 C ALA A 548 21.184 15.666 -24.050 1.00 33.89 C
ANISOU 4164 C ALA A 548 4537 2839 5502 167 -2272 249 C
ATOM 4165 O ALA A 548 21.410 15.279 -22.897 1.00 30.32 O
ANISOU 4165 O ALA A 548 4107 2404 5008 206 -2169 255 O
ATOM 4166 CB ALA A 548 20.927 13.420 -25.155 1.00 26.23 C
ANISOU 4166 CB ALA A 548 3756 1856 4353 137 -2323 103 C
ATOM 4167 N LEU A 549 20.609 16.839 -24.326 1.00 36.33 N
ANISOU 4167 N LEU A 549 4772 3145 5886 176 -2324 302 N
ATOM 4168 CA LEU A 549 20.154 17.750 -23.284 1.00 28.72 C
ANISOU 4168 CA LEU A 549 3749 2201 4963 240 -2266 372 C
ATOM 4169 C LEU A 549 18.691 18.138 -23.460 1.00 29.61 C
ANISOU 4169 C LEU A 549 3877 2336 5037 286 -2329 381 C
ATOM 4170 O LEU A 549 18.210 19.033 -22.755 1.00 30.24 O
ANISOU 4170 O LEU A 549 3898 2432 5159 340 -2295 449 O
ATOM 4171 CB LEU A 549 21.031 19.010 -23.245 1.00 31.88 C
ANISOU 4171 CB LEU A 549 4015 2585 5512 214 -2246 452 C
ATOM 4172 CG LEU A 549 22.445 18.852 -22.680 1.00 33.62 C
ANISOU 4172 CG LEU A 549 4198 2789 5785 190 -2149 467 C
ATOM 4173 CD1 LEU A 549 23.271 20.097 -22.960 1.00 29.77 C
ANISOU 4173 CD1 LEU A 549 3574 2288 5450 152 -2152 541 C
ATOM 4174 CD2 LEU A 549 22.383 18.568 -21.187 1.00 35.21 C
ANISOU 4174 CD2 LEU A 549 4437 2992 5950 260 -2012 476 C
ATOM 4175 N ASP A 550 17.970 17.479 -24.365 1.00 30.84 N
ANISOU 4175 N ASP A 550 4110 2493 5115 271 -2412 316 N
ATOM 4176 CA ASP A 550 16.574 17.810 -24.607 1.00 32.54 C
ANISOU 4176 CA ASP A 550 4338 2735 5289 314 -2475 322 C
ATOM 4177 C ASP A 550 15.716 17.499 -23.384 1.00 33.89 C
ANISOU 4177 C ASP A 550 4553 2946 5376 397 -2401 338 C
ATOM 4178 O ASP A 550 16.123 16.779 -22.468 1.00 34.55 O
ANISOU 4178 O ASP A 550 4683 3030 5413 418 -2307 323 O
ATOM 4179 CB ASP A 550 16.043 17.037 -25.813 1.00 35.58 C
ANISOU 4179 CB ASP A 550 4807 3105 5607 285 -2563 243 C
ATOM 4180 CG ASP A 550 16.094 15.534 -25.608 1.00 41.00 C
ANISOU 4180 CG ASP A 550 5610 3790 6178 293 -2517 163 C
ATOM 4181 OD1 ASP A 550 17.188 14.945 -25.740 1.00 40.05 O
ANISOU 4181 OD1 ASP A 550 5508 3640 6068 249 -2486 134 O
ATOM 4182 OD2 ASP A 550 15.041 14.943 -25.296 1.00 41.14 O
ANISOU 4182 OD2 ASP A 550 5697 3841 6094 345 -2510 135 O
ATOM 4183 N THR A 551 14.505 18.061 -23.385 1.00 35.11 N
ANISOU 4183 N THR A 551 4691 3136 5513 446 -2443 371 N
ATOM 4184 CA THR A 551 13.469 17.725 -22.410 1.00 39.04 C
ANISOU 4184 CA THR A 551 5236 3674 5922 526 -2389 387 C
ATOM 4185 C THR A 551 13.946 17.974 -20.980 1.00 32.77 C
ANISOU 4185 C THR A 551 4414 2871 5165 573 -2261 448 C
ATOM 4186 O THR A 551 13.878 17.102 -20.111 1.00 35.14 O
ANISOU 4186 O THR A 551 4787 3175 5390 607 -2178 427 O
ATOM 4187 CB THR A 551 12.993 16.281 -22.590 1.00 39.80 C
ANISOU 4187 CB THR A 551 5455 3783 5886 528 -2393 299 C
ATOM 4188 OG1 THR A 551 12.910 15.982 -23.989 1.00 44.79 O
ANISOU 4188 OG1 THR A 551 6116 4397 6507 475 -2494 234 O
ATOM 4189 CG2 THR A 551 11.614 16.088 -21.977 1.00 40.64 C
ANISOU 4189 CG2 THR A 551 5598 3942 5903 605 -2378 319 C
ATOM 4190 N ASN A 552 14.456 19.181 -20.745 1.00 34.63 N
ANISOU 4190 N ASN A 552 4545 3091 5522 575 -2238 523 N
ATOM 4191 CA ASN A 552 14.772 19.629 -19.396 1.00 39.31 C
ANISOU 4191 CA ASN A 552 5103 3666 6167 632 -2110 590 C
ATOM 4192 C ASN A 552 13.990 20.899 -19.091 1.00 36.55 C
ANISOU 4192 C ASN A 552 4670 3339 5879 692 -2116 683 C
ATOM 4193 O ASN A 552 12.934 21.145 -19.683 1.00 39.08 O
ANISOU 4193 O ASN A 552 4986 3702 6159 708 -2207 690 O
ATOM 4194 CB ASN A 552 16.276 19.864 -19.231 1.00 38.93 C
ANISOU 4194 CB ASN A 552 5003 3573 6217 585 -2047 596 C
ATOM 4195 CG ASN A 552 17.064 18.571 -19.114 1.00 40.79 C
ANISOU 4195 CG ASN A 552 5324 3790 6386 547 -2001 519 C
ATOM 4196 OD1 ASN A 552 17.203 18.014 -18.027 1.00 36.73 O
ANISOU 4196 OD1 ASN A 552 4862 3262 5833 584 -1887 515 O
ATOM 4197 ND2 ASN A 552 17.593 18.096 -20.232 1.00 37.16 N
ANISOU 4197 ND2 ASN A 552 4879 3327 5912 472 -2085 460 N
ATOM 4198 N GLN A 553 14.492 21.712 -18.166 1.00 34.68 N
ANISOU 4198 N GLN A 553 4366 3073 5738 729 -2015 753 N
ATOM 4199 CA GLN A 553 13.894 23.001 -17.848 1.00 38.65 C
ANISOU 4199 CA GLN A 553 4780 3594 6312 788 -2010 848 C
ATOM 4200 C GLN A 553 14.833 24.148 -18.211 1.00 37.71 C
ANISOU 4200 C GLN A 553 4540 3455 6334 748 -2019 893 C
ATOM 4201 O GLN A 553 14.740 25.241 -17.646 1.00 41.33 O
ANISOU 4201 O GLN A 553 4916 3911 6877 799 -1969 975 O
ATOM 4202 CB GLN A 553 13.515 23.065 -16.369 1.00 41.22 C
ANISOU 4202 CB GLN A 553 5127 3899 6634 880 -1873 901 C
ATOM 4203 CG GLN A 553 12.745 21.849 -15.859 1.00 52.12 C
ANISOU 4203 CG GLN A 553 6627 5293 7882 916 -1842 860 C
ATOM 4204 CD GLN A 553 11.302 21.829 -16.321 1.00 60.61 C
ANISOU 4204 CD GLN A 553 7720 6437 8872 952 -1937 874 C
ATOM 4205 OE1 GLN A 553 10.722 22.870 -16.622 1.00 67.37 O
ANISOU 4205 OE1 GLN A 553 8498 7327 9773 981 -1993 938 O
ATOM 4206 NE2 GLN A 553 10.714 20.639 -16.376 1.00 61.00 N
ANISOU 4206 NE2 GLN A 553 7868 6510 8797 952 -1955 815 N
ATOM 4207 N LEU A 554 15.743 23.906 -19.152 1.00 34.14 N
ANISOU 4207 N LEU A 554 4076 2988 5909 658 -2080 843 N
ATOM 4208 CA LEU A 554 16.768 24.885 -19.488 1.00 34.48 C
ANISOU 4208 CA LEU A 554 4004 3010 6085 612 -2080 885 C
ATOM 4209 C LEU A 554 16.169 26.087 -20.204 1.00 40.00 C
ANISOU 4209 C LEU A 554 4610 3748 6841 612 -2176 945 C
ATOM 4210 O LEU A 554 15.309 25.948 -21.077 1.00 40.53 O
ANISOU 4210 O LEU A 554 4705 3850 6844 596 -2291 919 O
ATOM 4211 CB LEU A 554 17.840 24.246 -20.368 1.00 33.66 C
ANISOU 4211 CB LEU A 554 3916 2884 5988 515 -2125 818 C
ATOM 4212 CG LEU A 554 18.776 23.234 -19.715 1.00 33.84 C
ANISOU 4212 CG LEU A 554 4003 2871 5983 502 -2024 769 C
ATOM 4213 CD1 LEU A 554 19.550 22.493 -20.789 1.00 33.86 C
ANISOU 4213 CD1 LEU A 554 4035 2865 5965 410 -2097 700 C
ATOM 4214 CD2 LEU A 554 19.723 23.932 -18.747 1.00 32.40 C
ANISOU 4214 CD2 LEU A 554 3742 2655 5914 524 -1892 825 C
ATOM 4215 N LYS A 555 16.647 27.276 -19.832 1.00 37.80 N
ANISOU 4215 N LYS A 555 4216 3462 6683 629 -2125 1024 N
ATOM 4216 CA LYS A 555 16.247 28.522 -20.462 1.00 39.00 C
ANISOU 4216 CA LYS A 555 4264 3652 6903 625 -2205 1090 C
ATOM 4217 C LYS A 555 17.411 29.289 -21.072 1.00 37.95 C
ANISOU 4217 C LYS A 555 4023 3504 6894 551 -2221 1118 C
ATOM 4218 O LYS A 555 17.175 30.221 -21.852 1.00 39.96 O
ANISOU 4218 O LYS A 555 4194 3789 7199 525 -2306 1160 O
ATOM 4219 CB LYS A 555 15.530 29.431 -19.450 1.00 46.79 C
ANISOU 4219 CB LYS A 555 5199 4658 7920 727 -2133 1179 C
ATOM 4220 CG LYS A 555 14.335 28.783 -18.773 1.00 50.12 C
ANISOU 4220 CG LYS A 555 5718 5098 8227 808 -2109 1169 C
ATOM 4221 CD LYS A 555 13.633 29.762 -17.846 1.00 52.43 C
ANISOU 4221 CD LYS A 555 5955 5410 8558 909 -2042 1265 C
ATOM 4222 CE LYS A 555 12.402 29.132 -17.213 1.00 57.94 C
ANISOU 4222 CE LYS A 555 6746 6130 9139 990 -2022 1263 C
ATOM 4223 NZ LYS A 555 11.657 30.087 -16.350 1.00 63.37 N
ANISOU 4223 NZ LYS A 555 7382 6836 9861 1092 -1962 1360 N
ATOM 4224 N SER A 556 18.649 28.930 -20.744 1.00 37.87 N
ANISOU 4224 N SER A 556 4007 3451 6932 516 -2139 1097 N
ATOM 4225 CA SER A 556 19.830 29.615 -21.251 1.00 37.22 C
ANISOU 4225 CA SER A 556 3817 3357 6968 447 -2141 1128 C
ATOM 4226 C SER A 556 21.042 28.740 -20.976 1.00 45.41 C
ANISOU 4226 C SER A 556 4890 4352 8011 407 -2065 1078 C
ATOM 4227 O SER A 556 20.977 27.791 -20.188 1.00 42.15 O
ANISOU 4227 O SER A 556 4572 3918 7524 444 -1990 1032 O
ATOM 4228 CB SER A 556 20.007 30.993 -20.602 1.00 39.44 C
ANISOU 4228 CB SER A 556 3971 3649 7366 497 -2066 1227 C
ATOM 4229 OG SER A 556 20.469 30.868 -19.268 1.00 40.23 O
ANISOU 4229 OG SER A 556 4077 3713 7494 558 -1908 1239 O
ATOM 4230 N VAL A 557 22.143 29.063 -21.646 1.00 35.94 N
ANISOU 4230 N VAL A 557 3614 3146 6897 329 -2085 1091 N
ATOM 4231 CA VAL A 557 23.429 28.421 -21.388 1.00 37.66 C
ANISOU 4231 CA VAL A 557 3837 3332 7139 290 -2007 1060 C
ATOM 4232 C VAL A 557 24.467 29.515 -21.167 1.00 38.25 C
ANISOU 4232 C VAL A 557 3767 3410 7358 276 -1934 1136 C
ATOM 4233 O VAL A 557 24.298 30.635 -21.670 1.00 37.47 O
ANISOU 4233 O VAL A 557 3569 3337 7330 264 -1986 1199 O
ATOM 4234 CB VAL A 557 23.840 27.489 -22.540 1.00 37.06 C
ANISOU 4234 CB VAL A 557 3823 3249 7010 199 -2104 991 C
ATOM 4235 CG1 VAL A 557 22.792 26.403 -22.750 1.00 36.19 C
ANISOU 4235 CG1 VAL A 557 3855 3140 6757 217 -2168 913 C
ATOM 4236 CG2 VAL A 557 24.063 28.285 -23.822 1.00 40.65 C
ANISOU 4236 CG2 VAL A 557 4194 3714 7536 122 -2211 1026 C
ATOM 4237 N PRO A 558 25.529 29.254 -20.411 1.00 40.11 N
ANISOU 4237 N PRO A 558 3981 3620 7639 280 -1810 1133 N
ATOM 4238 CA PRO A 558 26.617 30.233 -20.322 1.00 38.23 C
ANISOU 4238 CA PRO A 558 3597 3390 7538 259 -1743 1201 C
ATOM 4239 C PRO A 558 27.301 30.379 -21.669 1.00 41.01 C
ANISOU 4239 C PRO A 558 3894 3764 7926 154 -1848 1209 C
ATOM 4240 O PRO A 558 27.315 29.455 -22.486 1.00 46.82 O
ANISOU 4240 O PRO A 558 4712 4491 8587 95 -1936 1148 O
ATOM 4241 CB PRO A 558 27.564 29.628 -19.278 1.00 40.60 C
ANISOU 4241 CB PRO A 558 3915 3655 7857 282 -1588 1174 C
ATOM 4242 CG PRO A 558 26.750 28.591 -18.557 1.00 42.36 C
ANISOU 4242 CG PRO A 558 4288 3846 7960 337 -1554 1108 C
ATOM 4243 CD PRO A 558 25.763 28.079 -19.555 1.00 40.03 C
ANISOU 4243 CD PRO A 558 4078 3575 7558 308 -1714 1069 C
ATOM 4244 N ASP A 559 27.856 31.564 -21.905 1.00 42.65 N
ANISOU 4244 N ASP A 559 3962 3998 8246 131 -1834 1285 N
ATOM 4245 CA ASP A 559 28.567 31.811 -23.152 1.00 45.29 C
ANISOU 4245 CA ASP A 559 4239 4349 8620 29 -1917 1303 C
ATOM 4246 C ASP A 559 29.765 30.875 -23.277 1.00 43.95 C
ANISOU 4246 C ASP A 559 4088 4169 8443 -29 -1878 1263 C
ATOM 4247 O ASP A 559 30.522 30.679 -22.321 1.00 46.88 O
ANISOU 4247 O ASP A 559 4425 4538 8848 4 -1750 1264 O
ATOM 4248 CB ASP A 559 29.020 33.271 -23.221 1.00 46.25 C
ANISOU 4248 CB ASP A 559 4206 4506 8861 22 -1884 1396 C
ATOM 4249 CG ASP A 559 27.868 34.233 -23.475 1.00 52.16 C
ANISOU 4249 CG ASP A 559 4929 5274 9615 57 -1958 1441 C
ATOM 4250 OD1 ASP A 559 26.724 33.765 -23.668 1.00 56.14 O
ANISOU 4250 OD1 ASP A 559 5533 5768 10030 81 -2040 1398 O
ATOM 4251 OD2 ASP A 559 28.110 35.459 -23.484 1.00 55.78 O
ANISOU 4251 OD2 ASP A 559 5266 5765 10163 61 -1932 1520 O
ATOM 4252 N GLY A 560 29.920 30.279 -24.458 1.00 42.33 N
ANISOU 4252 N GLY A 560 3939 3955 8191 -111 -1983 1226 N
ATOM 4253 CA GLY A 560 31.062 29.438 -24.754 1.00 37.50 C
ANISOU 4253 CA GLY A 560 3341 3340 7569 -174 -1957 1196 C
ATOM 4254 C GLY A 560 31.039 28.051 -24.151 1.00 39.18 C
ANISOU 4254 C GLY A 560 3666 3530 7688 -145 -1922 1118 C
ATOM 4255 O GLY A 560 32.084 27.392 -24.128 1.00 45.69 O
ANISOU 4255 O GLY A 560 4484 4365 8512 -185 -1874 1101 O
ATOM 4256 N ILE A 561 29.885 27.580 -23.669 1.00 36.44 N
ANISOU 4256 N ILE A 561 3427 3162 7256 -79 -1941 1072 N
ATOM 4257 CA ILE A 561 29.848 26.295 -22.976 1.00 37.07 C
ANISOU 4257 CA ILE A 561 3625 3220 7241 -43 -1888 1001 C
ATOM 4258 C ILE A 561 30.195 25.151 -23.923 1.00 38.82 C
ANISOU 4258 C ILE A 561 3931 3435 7385 -114 -1966 939 C
ATOM 4259 O ILE A 561 30.790 24.148 -23.509 1.00 40.64 O
ANISOU 4259 O ILE A 561 4217 3658 7566 -114 -1908 899 O
ATOM 4260 CB ILE A 561 28.471 26.088 -22.310 1.00 37.91 C
ANISOU 4260 CB ILE A 561 3830 3311 7261 40 -1887 968 C
ATOM 4261 CG1 ILE A 561 28.437 24.765 -21.539 1.00 37.97 C
ANISOU 4261 CG1 ILE A 561 3969 3295 7162 75 -1816 894 C
ATOM 4262 CG2 ILE A 561 27.348 26.156 -23.340 1.00 32.32 C
ANISOU 4262 CG2 ILE A 561 3174 2612 6495 20 -2033 946 C
ATOM 4263 CD1 ILE A 561 27.246 24.621 -20.625 1.00 38.08 C
ANISOU 4263 CD1 ILE A 561 4068 3298 7102 162 -1774 872 C
ATOM 4264 N PHE A 562 29.853 25.287 -25.203 1.00 35.94 N
ANISOU 4264 N PHE A 562 3582 3064 7009 -175 -2089 933 N
ATOM 4265 CA PHE A 562 30.094 24.263 -26.210 1.00 37.14 C
ANISOU 4265 CA PHE A 562 3824 3196 7093 -238 -2160 876 C
ATOM 4266 C PHE A 562 31.413 24.460 -26.952 1.00 34.88 C
ANISOU 4266 C PHE A 562 3461 2914 6877 -318 -2148 919 C
ATOM 4267 O PHE A 562 31.688 23.720 -27.900 1.00 33.43 O
ANISOU 4267 O PHE A 562 3350 2706 6647 -367 -2199 887 O
ATOM 4268 CB PHE A 562 28.942 24.240 -27.220 1.00 38.36 C
ANISOU 4268 CB PHE A 562 4059 3322 7196 -249 -2285 841 C
ATOM 4269 CG PHE A 562 27.590 23.997 -26.600 1.00 35.13 C
ANISOU 4269 CG PHE A 562 3729 2919 6699 -172 -2299 798 C
ATOM 4270 CD1 PHE A 562 27.447 23.130 -25.526 1.00 31.05 C
ANISOU 4270 CD1 PHE A 562 3285 2412 6100 -114 -2222 753 C
ATOM 4271 CD2 PHE A 562 26.463 24.642 -27.086 1.00 32.48 C
ANISOU 4271 CD2 PHE A 562 3398 2583 6362 -157 -2382 806 C
ATOM 4272 CE1 PHE A 562 26.202 22.907 -24.950 1.00 35.26 C
ANISOU 4272 CE1 PHE A 562 3896 2954 6548 -41 -2225 721 C
ATOM 4273 CE2 PHE A 562 25.215 24.426 -26.516 1.00 38.02 C
ANISOU 4273 CE2 PHE A 562 4169 3298 6979 -84 -2390 774 C
ATOM 4274 CZ PHE A 562 25.084 23.555 -25.447 1.00 35.85 C
ANISOU 4274 CZ PHE A 562 3968 3033 6620 -27 -2310 733 C
ATOM 4275 N ASP A 563 32.232 25.435 -26.541 1.00 41.40 N
ANISOU 4275 N ASP A 563 4148 3775 7808 -326 -2071 994 N
ATOM 4276 CA ASP A 563 33.379 25.839 -27.351 1.00 39.30 C
ANISOU 4276 CA ASP A 563 3809 3524 7601 -399 -2056 1045 C
ATOM 4277 C ASP A 563 34.446 24.754 -27.433 1.00 38.81 C
ANISOU 4277 C ASP A 563 3783 3480 7483 -437 -2001 1013 C
ATOM 4278 O ASP A 563 35.084 24.596 -28.481 1.00 42.92 O
ANISOU 4278 O ASP A 563 4321 3996 7991 -486 -2024 1030 O
ATOM 4279 CB ASP A 563 33.974 27.133 -26.799 1.00 44.47 C
ANISOU 4279 CB ASP A 563 4307 4225 8367 -393 -1969 1126 C
ATOM 4280 CG ASP A 563 33.196 28.354 -27.238 1.00 50.87 C
ANISOU 4280 CG ASP A 563 5069 5024 9236 -383 -2037 1178 C
ATOM 4281 OD1 ASP A 563 32.255 28.192 -28.042 1.00 50.92 O
ANISOU 4281 OD1 ASP A 563 5159 4990 9198 -390 -2151 1149 O
ATOM 4282 OD2 ASP A 563 33.524 29.472 -26.790 1.00 54.20 O
ANISOU 4282 OD2 ASP A 563 5367 5481 9745 -369 -1973 1246 O
ATOM 4283 N ARG A 564 34.656 24.000 -26.356 1.00 51.23 N
ANISOU 4283 N ARG A 564 6376 4013 9078 -248 -3508 335 N
ATOM 4284 CA ARG A 564 35.725 23.012 -26.297 1.00 50.45 C
ANISOU 4284 CA ARG A 564 6296 3941 8933 -244 -3469 335 C
ATOM 4285 C ARG A 564 35.260 21.602 -26.641 1.00 49.34 C
ANISOU 4285 C ARG A 564 6216 3801 8731 -218 -3468 315 C
ATOM 4286 O ARG A 564 36.048 20.658 -26.519 1.00 53.48 O
ANISOU 4286 O ARG A 564 6759 4356 9205 -214 -3429 310 O
ATOM 4287 CB ARG A 564 36.374 23.030 -24.912 1.00 49.48 C
ANISOU 4287 CB ARG A 564 6160 3866 8775 -240 -3403 323 C
ATOM 4288 CG ARG A 564 37.251 24.245 -24.673 1.00 53.50 C
ANISOU 4288 CG ARG A 564 6603 4402 9323 -277 -3381 339 C
ATOM 4289 CD ARG A 564 37.824 24.252 -23.267 1.00 64.78 C
ANISOU 4289 CD ARG A 564 8023 5877 10714 -271 -3318 322 C
ATOM 4290 NE ARG A 564 37.539 25.510 -22.584 1.00 78.73 N
ANISOU 4290 NE ARG A 564 9744 7652 12518 -284 -3310 322 N
ATOM 4291 CZ ARG A 564 38.005 25.838 -21.384 1.00 88.23 C
ANISOU 4291 CZ ARG A 564 10928 8893 13703 -285 -3260 310 C
ATOM 4292 NH1 ARG A 564 38.792 25.002 -20.719 1.00 89.64 N
ANISOU 4292 NH1 ARG A 564 11129 9106 13825 -276 -3215 295 N
ATOM 4293 NH2 ARG A 564 37.689 27.007 -20.849 1.00 90.82 N
ANISOU 4293 NH2 ARG A 564 11213 9226 14069 -297 -3257 312 N
ATOM 4294 N LEU A 565 34.007 21.441 -27.069 1.00 45.19 N
ANISOU 4294 N LEU A 565 5717 3253 8199 -205 -3501 299 N
ATOM 4295 CA LEU A 565 33.486 20.149 -27.518 1.00 42.45 C
ANISOU 4295 CA LEU A 565 5422 2917 7789 -186 -3495 276 C
ATOM 4296 C LEU A 565 33.912 19.881 -28.965 1.00 42.86 C
ANISOU 4296 C LEU A 565 5480 2942 7864 -201 -3539 296 C
ATOM 4297 O LEU A 565 33.102 19.797 -29.888 1.00 40.07 O
ANISOU 4297 O LEU A 565 5146 2555 7523 -198 -3590 292 O
ATOM 4298 CB LEU A 565 31.970 20.117 -27.369 1.00 41.76 C
ANISOU 4298 CB LEU A 565 5361 2817 7689 -165 -3514 249 C
ATOM 4299 CG LEU A 565 31.435 20.213 -25.942 1.00 38.74 C
ANISOU 4299 CG LEU A 565 4979 2464 7276 -147 -3469 226 C
ATOM 4300 CD1 LEU A 565 29.916 20.168 -25.931 1.00 38.96 C
ANISOU 4300 CD1 LEU A 565 5033 2476 7292 -128 -3493 202 C
ATOM 4301 CD2 LEU A 565 32.009 19.095 -25.097 1.00 37.92 C
ANISOU 4301 CD2 LEU A 565 4897 2411 7098 -134 -3399 211 C
ATOM 4302 N THR A 566 35.228 19.730 -29.143 1.00 47.19 N
ANISOU 4302 N THR A 566 6011 3504 8415 -217 -3520 317 N
ATOM 4303 CA THR A 566 35.843 19.670 -30.466 1.00 51.08 C
ANISOU 4303 CA THR A 566 6498 3970 8941 -237 -3561 342 C
ATOM 4304 C THR A 566 35.490 18.408 -31.245 1.00 48.01 C
ANISOU 4304 C THR A 566 6159 3584 8499 -223 -3566 325 C
ATOM 4305 O THR A 566 35.733 18.364 -32.456 1.00 51.31 O
ANISOU 4305 O THR A 566 6578 3973 8946 -237 -3611 343 O
ATOM 4306 CB THR A 566 37.364 19.772 -30.335 1.00 56.82 C
ANISOU 4306 CB THR A 566 7195 4715 9678 -256 -3532 367 C
ATOM 4307 OG1 THR A 566 37.813 18.852 -29.332 1.00 63.18 O
ANISOU 4307 OG1 THR A 566 8022 5571 10412 -241 -3464 346 O
ATOM 4308 CG2 THR A 566 37.775 21.182 -29.937 1.00 51.17 C
ANISOU 4308 CG2 THR A 566 6420 3996 9026 -280 -3535 388 C
ATOM 4309 N SER A 567 34.940 17.389 -30.594 1.00 43.91 N
ANISOU 4309 N SER A 567 5680 3098 7907 -198 -3522 294 N
ATOM 4310 CA SER A 567 34.580 16.149 -31.265 1.00 41.24 C
ANISOU 4310 CA SER A 567 5389 2765 7517 -183 -3522 278 C
ATOM 4311 C SER A 567 33.084 16.020 -31.499 1.00 40.58 C
ANISOU 4311 C SER A 567 5337 2660 7423 -164 -3554 254 C
ATOM 4312 O SER A 567 32.636 14.980 -31.992 1.00 39.45 O
ANISOU 4312 O SER A 567 5234 2520 7234 -149 -3554 237 O
ATOM 4313 CB SER A 567 35.074 14.947 -30.454 1.00 38.26 C
ANISOU 4313 CB SER A 567 5035 2440 7064 -170 -3451 262 C
ATOM 4314 OG SER A 567 36.483 14.966 -30.303 1.00 38.01 O
ANISOU 4314 OG SER A 567 4979 2426 7037 -187 -3424 282 O
ATOM 4315 N LEU A 568 32.307 17.048 -31.167 1.00 39.75 N
ANISOU 4315 N LEU A 568 5213 2532 7360 -163 -3583 251 N
ATOM 4316 CA LEU A 568 30.856 16.921 -31.173 1.00 39.96 C
ANISOU 4316 CA LEU A 568 5270 2542 7371 -142 -3607 225 C
ATOM 4317 C LEU A 568 30.322 16.696 -32.581 1.00 43.71 C
ANISOU 4317 C LEU A 568 5771 2974 7862 -143 -3674 226 C
ATOM 4318 O LEU A 568 30.738 17.354 -33.539 1.00 41.59 O
ANISOU 4318 O LEU A 568 5480 2667 7655 -165 -3730 253 O
ATOM 4319 CB LEU A 568 30.215 18.171 -30.569 1.00 42.39 C
ANISOU 4319 CB LEU A 568 5549 2831 7728 -145 -3629 226 C
ATOM 4320 CG LEU A 568 28.766 18.010 -30.104 1.00 43.57 C
ANISOU 4320 CG LEU A 568 5727 2978 7849 -119 -3632 194 C
ATOM 4321 CD1 LEU A 568 28.696 17.127 -28.866 1.00 44.00 C
ANISOU 4321 CD1 LEU A 568 5800 3088 7830 -97 -3553 170 C
ATOM 4322 CD2 LEU A 568 28.103 19.359 -29.852 1.00 40.76 C
ANISOU 4322 CD2 LEU A 568 5341 2589 7556 -126 -3675 200 C
ATOM 4323 N GLN A 569 29.382 15.761 -32.695 1.00 40.51 N
ANISOU 4323 N GLN A 569 5413 2575 7404 -118 -3670 198 N
ATOM 4324 CA GLN A 569 28.705 15.461 -33.948 1.00 41.14 C
ANISOU 4324 CA GLN A 569 5526 2615 7492 -114 -3734 192 C
ATOM 4325 C GLN A 569 27.189 15.552 -33.858 1.00 43.86 C
ANISOU 4325 C GLN A 569 5898 2937 7828 -92 -3766 165 C
ATOM 4326 O GLN A 569 26.541 15.830 -34.870 1.00 46.95 O
ANISOU 4326 O GLN A 569 6305 3280 8253 -93 -3841 165 O
ATOM 4327 CB GLN A 569 29.095 14.057 -34.438 1.00 40.77 C
ANISOU 4327 CB GLN A 569 5515 2591 7384 -104 -3705 185 C
ATOM 4328 CG GLN A 569 30.566 13.925 -34.819 1.00 48.54 C
ANISOU 4328 CG GLN A 569 6476 3587 8380 -127 -3688 213 C
ATOM 4329 CD GLN A 569 31.019 12.484 -34.924 1.00 51.26 C
ANISOU 4329 CD GLN A 569 6853 3968 8655 -117 -3640 204 C
ATOM 4330 OE1 GLN A 569 30.227 11.558 -34.759 1.00 49.06 O
ANISOU 4330 OE1 GLN A 569 6614 3705 8322 -92 -3619 178 O
ATOM 4331 NE2 GLN A 569 32.303 12.286 -35.195 1.00 46.69 N
ANISOU 4331 NE2 GLN A 569 6257 3403 8081 -135 -3622 226 N
ATOM 4332 N LYS A 570 26.605 15.327 -32.682 1.00 40.88 N
ANISOU 4332 N LYS A 570 5529 2595 7410 -72 -3714 142 N
ATOM 4333 CA LYS A 570 25.162 15.412 -32.498 1.00 41.12 C
ANISOU 4333 CA LYS A 570 5585 2608 7431 -50 -3740 116 C
ATOM 4334 C LYS A 570 24.857 16.046 -31.152 1.00 40.76 C
ANISOU 4334 C LYS A 570 5514 2584 7387 -45 -3702 108 C
ATOM 4335 O LYS A 570 25.503 15.723 -30.151 1.00 41.97 O
ANISOU 4335 O LYS A 570 5654 2785 7508 -44 -3631 109 O
ATOM 4336 CB LYS A 570 24.501 14.033 -32.577 1.00 40.77 C
ANISOU 4336 CB LYS A 570 5594 2585 7312 -22 -3713 88 C
ATOM 4337 CG LYS A 570 24.522 13.407 -33.958 1.00 41.22 C
ANISOU 4337 CG LYS A 570 5683 2615 7366 -22 -3760 89 C
ATOM 4338 CD LYS A 570 23.881 12.031 -33.944 1.00 42.75 C
ANISOU 4338 CD LYS A 570 5926 2832 7484 6 -3727 62 C
ATOM 4339 CE LYS A 570 23.957 11.379 -35.315 1.00 48.38 C
ANISOU 4339 CE LYS A 570 6673 3519 8192 6 -3772 64 C
ATOM 4340 NZ LYS A 570 23.366 10.013 -35.317 1.00 53.55 N
ANISOU 4340 NZ LYS A 570 7375 4197 8774 33 -3738 39 N
ATOM 4341 N ILE A 571 23.864 16.933 -31.128 1.00 41.30 N
ANISOU 4341 N ILE A 571 5578 2618 7495 -41 -3752 100 N
ATOM 4342 CA ILE A 571 23.386 17.541 -29.891 1.00 41.02 C
ANISOU 4342 CA ILE A 571 5523 2599 7462 -34 -3723 90 C
ATOM 4343 C ILE A 571 21.868 17.661 -29.950 1.00 41.42 C
ANISOU 4343 C ILE A 571 5604 2624 7510 -13 -3765 63 C
ATOM 4344 O ILE A 571 21.297 18.040 -30.979 1.00 42.23 O
ANISOU 4344 O ILE A 571 5720 2675 7651 -16 -3844 64 O
ATOM 4345 CB ILE A 571 24.052 18.912 -29.630 1.00 41.28 C
ANISOU 4345 CB ILE A 571 5501 2617 7567 -61 -3740 118 C
ATOM 4346 CG1 ILE A 571 23.670 19.437 -28.246 1.00 40.88 C
ANISOU 4346 CG1 ILE A 571 5431 2591 7512 -53 -3699 107 C
ATOM 4347 CG2 ILE A 571 23.689 19.922 -30.716 1.00 45.33 C
ANISOU 4347 CG2 ILE A 571 6000 3064 8158 -78 -3836 135 C
ATOM 4348 CD1 ILE A 571 24.535 20.576 -27.769 1.00 40.92 C
ANISOU 4348 CD1 ILE A 571 5380 2595 7574 -77 -3693 135 C
ATOM 4349 N TRP A 572 21.212 17.310 -28.846 1.00 40.87 N
ANISOU 4349 N TRP A 572 5547 2588 7395 8 -3714 39 N
ATOM 4350 CA TRP A 572 19.767 17.435 -28.689 1.00 41.17 C
ANISOU 4350 CA TRP A 572 5610 2606 7425 30 -3745 12 C
ATOM 4351 C TRP A 572 19.501 18.563 -27.703 1.00 41.17 C
ANISOU 4351 C TRP A 572 5575 2606 7463 25 -3741 14 C
ATOM 4352 O TRP A 572 19.972 18.510 -26.562 1.00 40.49 O
ANISOU 4352 O TRP A 572 5467 2563 7353 25 -3672 15 O
ATOM 4353 CB TRP A 572 19.146 16.132 -28.181 1.00 40.55 C
ANISOU 4353 CB TRP A 572 5575 2567 7266 59 -3690 -17 C
ATOM 4354 CG TRP A 572 19.209 14.965 -29.127 1.00 42.51 C
ANISOU 4354 CG TRP A 572 5864 2816 7474 68 -3695 -22 C
ATOM 4355 CD1 TRP A 572 18.172 14.425 -29.836 1.00 49.65 C
ANISOU 4355 CD1 TRP A 572 6814 3695 8356 89 -3736 -45 C
ATOM 4356 CD2 TRP A 572 20.367 14.179 -29.450 1.00 41.72 C
ANISOU 4356 CD2 TRP A 572 5761 2740 7349 58 -3657 -6 C
ATOM 4357 NE1 TRP A 572 18.614 13.360 -30.583 1.00 50.13 N
ANISOU 4357 NE1 TRP A 572 6902 3765 8382 92 -3726 -43 N
ATOM 4358 CE2 TRP A 572 19.956 13.189 -30.364 1.00 47.09 C
ANISOU 4358 CE2 TRP A 572 6487 3410 7995 72 -3678 -19 C
ATOM 4359 CE3 TRP A 572 21.710 14.219 -29.058 1.00 39.71 C
ANISOU 4359 CE3 TRP A 572 5473 2516 7099 38 -3611 18 C
ATOM 4360 CZ2 TRP A 572 20.838 12.249 -30.891 1.00 40.06 C
ANISOU 4360 CZ2 TRP A 572 5608 2539 7075 67 -3652 -8 C
ATOM 4361 CZ3 TRP A 572 22.585 13.283 -29.585 1.00 44.97 C
ANISOU 4361 CZ3 TRP A 572 6150 3199 7736 33 -3587 28 C
ATOM 4362 CH2 TRP A 572 22.144 12.313 -30.492 1.00 42.35 C
ANISOU 4362 CH2 TRP A 572 5862 2857 7370 47 -3607 15 C
ATOM 4363 N LEU A 573 18.758 19.580 -28.139 1.00 41.97 N
ANISOU 4363 N LEU A 573 5669 2657 7623 19 -3818 14 N
ATOM 4364 CA LEU A 573 18.437 20.709 -27.279 1.00 42.07 C
ANISOU 4364 CA LEU A 573 5645 2662 7676 13 -3822 17 C
ATOM 4365 C LEU A 573 16.959 21.076 -27.284 1.00 45.94 C
ANISOU 4365 C LEU A 573 6158 3120 8177 31 -3876 -8 C
ATOM 4366 O LEU A 573 16.574 22.022 -26.588 1.00 46.18 O
ANISOU 4366 O LEU A 573 6162 3142 8243 27 -3885 -8 O
ATOM 4367 CB LEU A 573 19.270 21.940 -27.677 1.00 42.58 C
ANISOU 4367 CB LEU A 573 5659 2696 7825 -20 -3864 54 C
ATOM 4368 CG LEU A 573 20.757 21.883 -27.312 1.00 42.03 C
ANISOU 4368 CG LEU A 573 5554 2661 7752 -39 -3804 79 C
ATOM 4369 CD1 LEU A 573 21.504 23.091 -27.853 1.00 44.08 C
ANISOU 4369 CD1 LEU A 573 5764 2884 8099 -73 -3854 117 C
ATOM 4370 CD2 LEU A 573 20.932 21.781 -25.802 1.00 41.19 C
ANISOU 4370 CD2 LEU A 573 5434 2608 7608 -29 -3722 69 C
ATOM 4371 N HIS A 574 16.123 20.347 -28.023 1.00 46.32 N
ANISOU 4371 N HIS A 574 6257 3150 8195 51 -3911 -31 N
ATOM 4372 CA HIS A 574 14.707 20.671 -28.145 1.00 43.46 C
ANISOU 4372 CA HIS A 574 5920 2750 7842 69 -3971 -56 C
ATOM 4373 C HIS A 574 13.986 20.438 -26.818 1.00 46.20 C
ANISOU 4373 C HIS A 574 6275 3137 8143 92 -3912 -82 C
ATOM 4374 O HIS A 574 14.566 19.980 -25.830 1.00 51.04 O
ANISOU 4374 O HIS A 574 6873 3804 8715 94 -3825 -80 O
ATOM 4375 CB HIS A 574 14.068 19.846 -29.263 1.00 43.90 C
ANISOU 4375 CB HIS A 574 6031 2779 7870 87 -4020 -75 C
ATOM 4376 CG HIS A 574 14.056 18.370 -28.999 1.00 44.56 C
ANISOU 4376 CG HIS A 574 6152 2911 7866 111 -3948 -94 C
ATOM 4377 ND1 HIS A 574 13.215 17.785 -28.077 1.00 42.62 N
ANISOU 4377 ND1 HIS A 574 5931 2699 7565 138 -3900 -123 N
ATOM 4378 CD2 HIS A 574 14.783 17.362 -29.536 1.00 42.81 C
ANISOU 4378 CD2 HIS A 574 5948 2711 7608 110 -3918 -87 C
ATOM 4379 CE1 HIS A 574 13.426 16.481 -28.055 1.00 42.03 C
ANISOU 4379 CE1 HIS A 574 5884 2662 7423 152 -3842 -132 C
ATOM 4380 NE2 HIS A 574 14.371 16.198 -28.932 1.00 45.08 N
ANISOU 4380 NE2 HIS A 574 6268 3042 7820 136 -3852 -111 N
ATOM 4381 N THR A 575 12.693 20.769 -26.805 1.00 43.32 N
ANISOU 4381 N THR A 575 5932 2742 7786 110 -3962 -107 N
ATOM 4382 CA THR A 575 11.822 20.573 -25.645 1.00 42.86 C
ANISOU 4382 CA THR A 575 5884 2714 7686 133 -3918 -134 C
ATOM 4383 C THR A 575 12.413 21.223 -24.395 1.00 42.31 C
ANISOU 4383 C THR A 575 5765 2678 7631 119 -3859 -120 C
ATOM 4384 O THR A 575 12.467 20.630 -23.315 1.00 41.49 O
ANISOU 4384 O THR A 575 5663 2627 7475 132 -3779 -130 O
ATOM 4385 CB THR A 575 11.540 19.083 -25.419 1.00 42.20 C
ANISOU 4385 CB THR A 575 5845 2673 7516 160 -3856 -158 C
ATOM 4386 OG1 THR A 575 11.340 18.446 -26.687 1.00 42.67 O
ANISOU 4386 OG1 THR A 575 5945 2703 7563 168 -3905 -164 O
ATOM 4387 CG2 THR A 575 10.273 18.899 -24.592 1.00 42.04 C
ANISOU 4387 CG2 THR A 575 5849 2665 7460 189 -3843 -191 C
ATOM 4388 N ASN A 576 12.872 22.461 -24.560 1.00 47.29 N
ANISOU 4388 N ASN A 576 6352 3278 8338 93 -3902 -94 N
ATOM 4389 CA ASN A 576 13.333 23.298 -23.465 1.00 45.41 C
ANISOU 4389 CA ASN A 576 6065 3062 8128 79 -3863 -79 C
ATOM 4390 C ASN A 576 12.741 24.692 -23.618 1.00 47.50 C
ANISOU 4390 C ASN A 576 6302 3273 8471 66 -3943 -72 C
ATOM 4391 O ASN A 576 12.612 25.196 -24.742 1.00 45.05 O
ANISOU 4391 O ASN A 576 5992 2908 8215 53 -4028 -60 O
ATOM 4392 CB ASN A 576 14.866 23.380 -23.421 1.00 47.19 C
ANISOU 4392 CB ASN A 576 6253 3311 8367 53 -3819 -46 C
ATOM 4393 CG ASN A 576 15.499 22.157 -22.782 1.00 45.73 C
ANISOU 4393 CG ASN A 576 6083 3187 8104 65 -3725 -53 C
ATOM 4394 OD1 ASN A 576 15.553 22.043 -21.558 1.00 40.43 O
ANISOU 4394 OD1 ASN A 576 5402 2558 7403 73 -3660 -61 O
ATOM 4395 ND2 ASN A 576 15.983 21.238 -23.609 1.00 41.07 N
ANISOU 4395 ND2 ASN A 576 5517 2601 7484 66 -3720 -49 N
ATOM 4396 N PRO A 577 12.354 25.331 -22.517 1.00 46.86 N
ANISOU 4396 N PRO A 577 6198 3205 8401 69 -3921 -79 N
ATOM 4397 CA PRO A 577 11.760 26.683 -22.594 1.00 44.99 C
ANISOU 4397 CA PRO A 577 5932 2918 8243 56 -3999 -70 C
ATOM 4398 C PRO A 577 12.821 27.767 -22.753 1.00 46.36 C
ANISOU 4398 C PRO A 577 6043 3082 8490 18 -4011 -28 C
ATOM 4399 O PRO A 577 13.158 28.513 -21.830 1.00 43.94 O
ANISOU 4399 O PRO A 577 5687 2810 8197 2 -3969 -19 O
ATOM 4400 CB PRO A 577 11.004 26.780 -21.266 1.00 43.66 C
ANISOU 4400 CB PRO A 577 5764 2779 8047 75 -3957 -95 C
ATOM 4401 CG PRO A 577 11.811 25.936 -20.328 1.00 43.81 C
ANISOU 4401 CG PRO A 577 5781 2866 8000 81 -3848 -96 C
ATOM 4402 CD PRO A 577 12.330 24.787 -21.148 1.00 42.15 C
ANISOU 4402 CD PRO A 577 5604 2668 7744 86 -3830 -96 C
ATOM 4403 N TRP A 578 13.360 27.874 -23.965 1.00 47.64 N
ANISOU 4403 N TRP A 578 6196 3226 8679 -6 -4054 -8 N
ATOM 4404 CA TRP A 578 14.472 28.783 -24.220 1.00 47.61 C
ANISOU 4404 CA TRP A 578 6124 3245 8722 -51 -4046 29 C
ATOM 4405 C TRP A 578 14.021 30.239 -24.191 1.00 48.96 C
ANISOU 4405 C TRP A 578 6229 3436 8937 -86 -4080 37 C
ATOM 4406 O TRP A 578 12.998 30.596 -24.778 1.00 46.61 O
ANISOU 4406 O TRP A 578 5937 3123 8650 -89 -4147 22 O
ATOM 4407 CB TRP A 578 15.115 28.457 -25.567 1.00 45.41 C
ANISOU 4407 CB TRP A 578 5855 2940 8460 -67 -4085 49 C
ATOM 4408 CG TRP A 578 15.765 27.106 -25.606 1.00 48.65 C
ANISOU 4408 CG TRP A 578 6317 3339 8829 -38 -4047 49 C
ATOM 4409 CD1 TRP A 578 15.342 26.010 -26.303 1.00 48.55 C
ANISOU 4409 CD1 TRP A 578 6360 3323 8765 -16 -4058 27 C
ATOM 4410 CD2 TRP A 578 16.951 26.705 -24.908 1.00 45.47 C
ANISOU 4410 CD2 TRP A 578 5895 2988 8393 -42 -3959 61 C
ATOM 4411 NE1 TRP A 578 16.196 24.955 -26.087 1.00 47.08 N
ANISOU 4411 NE1 TRP A 578 6187 3188 8514 -10 -3979 25 N
ATOM 4412 CE2 TRP A 578 17.190 25.355 -25.233 1.00 45.96 C
ANISOU 4412 CE2 TRP A 578 6001 3080 8382 -25 -3919 45 C
ATOM 4413 CE3 TRP A 578 17.834 27.358 -24.044 1.00 43.75 C
ANISOU 4413 CE3 TRP A 578 5628 2796 8199 -59 -3911 83 C
ATOM 4414 CZ2 TRP A 578 18.277 24.645 -24.723 1.00 42.43 C
ANISOU 4414 CZ2 TRP A 578 5548 2686 7887 -26 -3836 51 C
ATOM 4415 CZ3 TRP A 578 18.912 26.652 -23.537 1.00 42.87 C
ANISOU 4415 CZ3 TRP A 578 5514 2737 8038 -58 -3828 86 C
ATOM 4416 CH2 TRP A 578 19.124 25.310 -23.878 1.00 42.08 C
ANISOU 4416 CH2 TRP A 578 5457 2665 7867 -42 -3793 71 C
ATOM 4417 N ASP A 579 14.800 31.078 -23.510 1.00 50.50 N
ANISOU 4417 N ASP A 579 6360 3668 9157 -112 -4035 61 N
ATOM 4418 CA ASP A 579 14.553 32.519 -23.445 1.00 50.95 C
ANISOU 4418 CA ASP A 579 6344 3753 9262 -149 -4061 76 C
ATOM 4419 C ASP A 579 15.276 33.166 -24.617 1.00 51.25 C
ANISOU 4419 C ASP A 579 6335 3784 9352 -193 -4104 112 C
ATOM 4420 O ASP A 579 16.501 33.302 -24.611 1.00 52.44 O
ANISOU 4420 O ASP A 579 6454 3950 9521 -213 -4066 140 O
ATOM 4421 CB ASP A 579 15.018 33.086 -22.107 1.00 47.27 C
ANISOU 4421 CB ASP A 579 5833 3331 8797 -154 -3991 85 C
ATOM 4422 CG ASP A 579 14.895 34.603 -22.028 1.00 47.37 C
ANISOU 4422 CG ASP A 579 5761 3378 8860 -193 -4012 107 C
ATOM 4423 OD1 ASP A 579 14.205 35.211 -22.874 1.00 50.81 O
ANISOU 4423 OD1 ASP A 579 6176 3806 9325 -212 -4084 111 O
ATOM 4424 OD2 ASP A 579 15.500 35.192 -21.108 1.00 51.11 O
ANISOU 4424 OD2 ASP A 579 6187 3889 9344 -204 -3958 123 O
ATOM 4425 N CYS A 580 14.512 33.575 -25.622 1.00 50.48 N
ANISOU 4425 N CYS A 580 6234 3668 9280 -209 -4185 109 N
ATOM 4426 CA CYS A 580 15.071 34.140 -26.849 1.00 56.90 C
ANISOU 4426 CA CYS A 580 7007 4468 10144 -251 -4237 142 C
ATOM 4427 C CYS A 580 15.025 35.665 -26.839 1.00 55.87 C
ANISOU 4427 C CYS A 580 6785 4371 10070 -295 -4262 170 C
ATOM 4428 O CYS A 580 14.482 36.302 -27.743 1.00 60.65 O
ANISOU 4428 O CYS A 580 7365 4967 10712 -321 -4338 178 O
ATOM 4429 CB CYS A 580 14.336 33.566 -28.054 1.00 61.55 C
ANISOU 4429 CB CYS A 580 7649 5011 10726 -241 -4316 123 C
ATOM 4430 SG CYS A 580 14.588 31.786 -28.266 1.00 64.68 S
ANISOU 4430 SG CYS A 580 8143 5369 11063 -193 -4289 101 S
ATOM 4431 N SER A 581 15.597 36.273 -25.803 1.00 54.48 N
ANISOU 4431 N SER A 581 6558 4238 9904 -305 -4198 187 N
ATOM 4432 CA SER A 581 15.736 37.720 -25.723 1.00 51.62 C
ANISOU 4432 CA SER A 581 6102 3915 9598 -347 -4210 221 C
ATOM 4433 C SER A 581 17.199 38.095 -25.919 1.00 58.32 C
ANISOU 4433 C SER A 581 6899 4776 10483 -380 -4175 263 C
ATOM 4434 O SER A 581 18.102 37.367 -25.492 1.00 59.30 O
ANISOU 4434 O SER A 581 7052 4900 10580 -364 -4112 261 O
ATOM 4435 CB SER A 581 15.225 38.262 -24.382 1.00 49.77 C
ANISOU 4435 CB SER A 581 5839 3724 9349 -334 -4168 210 C
ATOM 4436 OG SER A 581 16.135 37.993 -23.329 1.00 57.97 O
ANISOU 4436 OG SER A 581 6876 4783 10366 -321 -4081 214 O
ATOM 4437 N CYS A 582 17.429 39.222 -26.587 1.00 56.06 N
ANISOU 4437 N CYS A 582 6535 4504 10260 -426 -4216 302 N
ATOM 4438 CA CYS A 582 18.814 39.610 -26.826 1.00 60.19 C
ANISOU 4438 CA CYS A 582 7007 5040 10822 -459 -4184 344 C
ATOM 4439 C CYS A 582 19.302 40.543 -25.723 1.00 58.01 C
ANISOU 4439 C CYS A 582 6659 4818 10564 -471 -4123 367 C
ATOM 4440 O CYS A 582 18.521 41.341 -25.200 1.00 60.83 O
ANISOU 4440 O CYS A 582 6975 5206 10932 -473 -4134 367 O
ATOM 4441 CB CYS A 582 18.954 40.299 -28.180 1.00 63.09 C
ANISOU 4441 CB CYS A 582 7326 5392 11253 -505 -4258 379 C
ATOM 4442 SG CYS A 582 18.593 39.227 -29.586 1.00 72.16 S
ANISOU 4442 SG CYS A 582 8555 6476 12386 -495 -4331 356 S
ATOM 4443 N PRO A 583 20.594 40.490 -25.356 1.00 56.37 N
ANISOU 4443 N PRO A 583 6431 4626 10360 -478 -4058 388 N
ATOM 4444 CA PRO A 583 21.656 39.669 -25.951 1.00 61.11 C
ANISOU 4444 CA PRO A 583 7066 5201 10951 -478 -4041 394 C
ATOM 4445 C PRO A 583 21.832 38.293 -25.312 1.00 57.01 C
ANISOU 4445 C PRO A 583 6632 4667 10360 -431 -3988 356 C
ATOM 4446 O PRO A 583 22.898 37.699 -25.455 1.00 59.77 O
ANISOU 4446 O PRO A 583 7000 5014 10698 -430 -3952 364 O
ATOM 4447 CB PRO A 583 22.900 40.517 -25.707 1.00 59.60 C
ANISOU 4447 CB PRO A 583 6796 5047 10803 -511 -3995 439 C
ATOM 4448 CG PRO A 583 22.624 41.144 -24.375 1.00 55.43 C
ANISOU 4448 CG PRO A 583 6233 4563 10266 -500 -3947 434 C
ATOM 4449 CD PRO A 583 21.134 41.408 -24.336 1.00 52.95 C
ANISOU 4449 CD PRO A 583 5926 4245 9946 -490 -4000 412 C
ATOM 4450 N ARG A 584 20.805 37.793 -24.625 1.00 48.07 N
ANISOU 4450 N ARG A 584 5551 3530 9183 -394 -3984 317 N
ATOM 4451 CA ARG A 584 20.962 36.558 -23.862 1.00 46.93 C
ANISOU 4451 CA ARG A 584 5480 3379 8973 -350 -3928 284 C
ATOM 4452 C ARG A 584 21.090 35.344 -24.778 1.00 50.96 C
ANISOU 4452 C ARG A 584 6060 3847 9456 -332 -3952 272 C
ATOM 4453 O ARG A 584 21.964 34.491 -24.577 1.00 50.75 O
ANISOU 4453 O ARG A 584 6065 3820 9397 -316 -3905 270 O
ATOM 4454 CB ARG A 584 19.786 36.390 -22.902 1.00 46.61 C
ANISOU 4454 CB ARG A 584 5471 3343 8895 -316 -3920 248 C
ATOM 4455 CG ARG A 584 19.874 35.169 -22.008 1.00 45.47 C
ANISOU 4455 CG ARG A 584 5396 3194 8686 -271 -3862 216 C
ATOM 4456 CD ARG A 584 18.688 35.106 -21.061 1.00 49.44 C
ANISOU 4456 CD ARG A 584 5924 3703 9159 -241 -3855 183 C
ATOM 4457 NE ARG A 584 18.806 34.022 -20.090 1.00 54.47 N
ANISOU 4457 NE ARG A 584 6619 4338 9739 -200 -3796 157 N
ATOM 4458 CZ ARG A 584 17.909 33.771 -19.143 1.00 58.40 C
ANISOU 4458 CZ ARG A 584 7145 4840 10203 -170 -3778 127 C
ATOM 4459 NH1 ARG A 584 16.825 34.525 -19.037 1.00 59.84 N
ANISOU 4459 NH1 ARG A 584 7304 5030 10401 -175 -3815 118 N
ATOM 4460 NH2 ARG A 584 18.094 32.764 -18.299 1.00 53.84 N
ANISOU 4460 NH2 ARG A 584 6617 4261 9577 -135 -3725 107 N
ATOM 4461 N ILE A 585 20.235 35.252 -25.795 1.00 53.26 N
ANISOU 4461 N ILE A 585 6374 4104 9759 -335 -4027 264 N
ATOM 4462 CA ILE A 585 20.177 34.075 -26.658 1.00 49.72 C
ANISOU 4462 CA ILE A 585 5995 3614 9281 -313 -4055 249 C
ATOM 4463 C ILE A 585 21.223 34.193 -27.763 1.00 47.87 C
ANISOU 4463 C ILE A 585 5735 3370 9085 -347 -4076 283 C
ATOM 4464 O ILE A 585 21.256 33.382 -28.696 1.00 48.00 O
ANISOU 4464 O ILE A 585 5797 3351 9088 -338 -4110 278 O
ATOM 4465 CB ILE A 585 18.759 33.899 -27.236 1.00 48.08 C
ANISOU 4465 CB ILE A 585 5828 3373 9066 -299 -4128 222 C
ATOM 4466 CG1 ILE A 585 18.513 32.454 -27.679 1.00 47.66 C
ANISOU 4466 CG1 ILE A 585 5863 3282 8963 -259 -4138 195 C
ATOM 4467 CG2 ILE A 585 18.506 34.885 -28.372 1.00 49.36 C
ANISOU 4467 CG2 ILE A 585 5940 3524 9289 -343 -4208 245 C
ATOM 4468 CD1 ILE A 585 18.352 31.479 -26.530 1.00 50.66 C
ANISOU 4468 CD1 ILE A 585 6297 3671 9281 -212 -4073 167 C
ATOM 4469 N ASP A 586 22.107 35.187 -27.642 1.00 48.09 N
ANISOU 4469 N ASP A 586 5687 3429 9158 -385 -4053 319 N
ATOM 4470 CA ASP A 586 23.025 35.508 -28.733 1.00 49.12 C
ANISOU 4470 CA ASP A 586 5779 3550 9334 -423 -4080 356 C
ATOM 4471 C ASP A 586 24.000 34.368 -29.002 1.00 47.98 C
ANISOU 4471 C ASP A 586 5680 3396 9155 -406 -4046 355 C
ATOM 4472 O ASP A 586 24.137 33.918 -30.146 1.00 48.39 O
ANISOU 4472 O ASP A 586 5755 3416 9215 -414 -4091 362 O
ATOM 4473 CB ASP A 586 23.781 36.799 -28.422 1.00 53.23 C
ANISOU 4473 CB ASP A 586 6206 4110 9909 -465 -4054 396 C
ATOM 4474 CG ASP A 586 24.619 37.280 -29.592 1.00 61.01 C
ANISOU 4474 CG ASP A 586 7143 5085 10951 -509 -4089 438 C
ATOM 4475 OD1 ASP A 586 24.393 36.806 -30.726 1.00 65.14 O
ANISOU 4475 OD1 ASP A 586 7700 5570 11481 -512 -4147 435 O
ATOM 4476 OD2 ASP A 586 25.508 38.132 -29.379 1.00 66.85 O
ANISOU 4476 OD2 ASP A 586 7812 5857 11731 -539 -4057 473 O
ATOM 4477 N TYR A 587 24.705 33.899 -27.968 1.00 48.62 N
ANISOU 4477 N TYR A 587 5774 3505 9196 -385 -3968 348 N
ATOM 4478 CA TYR A 587 25.677 32.828 -28.171 1.00 46.31 C
ANISOU 4478 CA TYR A 587 5519 3209 8867 -370 -3933 348 C
ATOM 4479 C TYR A 587 25.005 31.576 -28.719 1.00 46.16 C
ANISOU 4479 C TYR A 587 5582 3152 8804 -334 -3966 321 C
ATOM 4480 O TYR A 587 25.494 30.961 -29.671 1.00 49.26 O
ANISOU 4480 O TYR A 587 5998 3526 9195 -337 -3987 330 O
ATOM 4481 CB TYR A 587 26.409 32.502 -26.867 1.00 45.26 C
ANISOU 4481 CB TYR A 587 5389 3115 8692 -350 -3847 340 C
ATOM 4482 CG TYR A 587 27.189 31.201 -26.943 1.00 52.45 C
ANISOU 4482 CG TYR A 587 6352 4025 9553 -325 -3813 333 C
ATOM 4483 CD1 TYR A 587 28.422 31.147 -27.583 1.00 59.33 C
ANISOU 4483 CD1 TYR A 587 7199 4904 10439 -349 -3803 360 C
ATOM 4484 CD2 TYR A 587 26.687 30.028 -26.388 1.00 51.49 C
ANISOU 4484 CD2 TYR A 587 6300 3897 9369 -279 -3791 300 C
ATOM 4485 CE1 TYR A 587 29.136 29.964 -27.666 1.00 56.88 C
ANISOU 4485 CE1 TYR A 587 6933 4596 10081 -328 -3773 353 C
ATOM 4486 CE2 TYR A 587 27.394 28.840 -26.466 1.00 48.31 C
ANISOU 4486 CE2 TYR A 587 5939 3496 8919 -258 -3761 296 C
ATOM 4487 CZ TYR A 587 28.617 28.815 -27.106 1.00 47.38 C
ANISOU 4487 CZ TYR A 587 5798 3389 8816 -283 -3752 322 C
ATOM 4488 OH TYR A 587 29.324 27.635 -27.184 1.00 42.60 O
ANISOU 4488 OH TYR A 587 5233 2789 8164 -264 -3723 318 O
ATOM 4489 N LEU A 588 23.876 31.184 -28.128 1.00 45.90 N
ANISOU 4489 N LEU A 588 5594 3110 8736 -299 -3969 287 N
ATOM 4490 CA LEU A 588 23.238 29.924 -28.497 1.00 45.65 C
ANISOU 4490 CA LEU A 588 5642 3046 8658 -260 -3991 260 C
ATOM 4491 C LEU A 588 22.700 29.971 -29.922 1.00 46.62 C
ANISOU 4491 C LEU A 588 5777 3126 8810 -275 -4077 263 C
ATOM 4492 O LEU A 588 22.876 29.019 -30.691 1.00 46.56 O
ANISOU 4492 O LEU A 588 5816 3094 8781 -261 -4096 260 O
ATOM 4493 CB LEU A 588 22.120 29.598 -27.504 1.00 48.95 C
ANISOU 4493 CB LEU A 588 6099 3463 9036 -222 -3976 225 C
ATOM 4494 CG LEU A 588 21.412 28.255 -27.660 1.00 48.43 C
ANISOU 4494 CG LEU A 588 6116 3368 8918 -176 -3987 195 C
ATOM 4495 CD1 LEU A 588 22.431 27.136 -27.815 1.00 44.81 C
ANISOU 4495 CD1 LEU A 588 5688 2914 8423 -161 -3949 203 C
ATOM 4496 CD2 LEU A 588 20.493 27.989 -26.471 1.00 46.39 C
ANISOU 4496 CD2 LEU A 588 5887 3118 8622 -140 -3957 164 C
ATOM 4497 N SER A 589 22.040 31.071 -30.292 1.00 48.80 N
ANISOU 4497 N SER A 589 6011 3396 9135 -304 -4131 270 N
ATOM 4498 CA SER A 589 21.465 31.183 -31.630 1.00 48.57 C
ANISOU 4498 CA SER A 589 5993 3327 9136 -320 -4219 272 C
ATOM 4499 C SER A 589 22.548 31.171 -32.701 1.00 48.93 C
ANISOU 4499 C SER A 589 6016 3363 9213 -352 -4236 305 C
ATOM 4500 O SER A 589 22.431 30.469 -33.712 1.00 49.23 O
ANISOU 4500 O SER A 589 6097 3365 9243 -344 -4282 299 O
ATOM 4501 CB SER A 589 20.618 32.452 -31.727 1.00 53.91 C
ANISOU 4501 CB SER A 589 6618 4004 9860 -350 -4272 276 C
ATOM 4502 OG SER A 589 21.330 33.576 -31.243 1.00 54.09 O
ANISOU 4502 OG SER A 589 6559 4065 9925 -386 -4238 308 O
ATOM 4503 N ARG A 590 23.615 31.949 -32.497 1.00 54.00 N
ANISOU 4503 N ARG A 590 6590 4036 9892 -386 -4200 338 N
ATOM 4504 CA ARG A 590 24.718 31.948 -33.453 1.00 54.94 C
ANISOU 4504 CA ARG A 590 6684 4148 10041 -416 -4211 371 C
ATOM 4505 C ARG A 590 25.414 30.594 -33.491 1.00 56.05 C
ANISOU 4505 C ARG A 590 6881 4287 10128 -385 -4171 362 C
ATOM 4506 O ARG A 590 25.825 30.129 -34.561 1.00 55.11 O
ANISOU 4506 O ARG A 590 6778 4143 10016 -394 -4204 373 O
ATOM 4507 CB ARG A 590 25.722 33.049 -33.112 1.00 55.64 C
ANISOU 4507 CB ARG A 590 6687 4274 10178 -457 -4173 408 C
ATOM 4508 CG ARG A 590 25.206 34.461 -33.315 1.00 53.14 C
ANISOU 4508 CG ARG A 590 6301 3962 9927 -497 -4220 429 C
ATOM 4509 CD ARG A 590 26.318 35.478 -33.097 1.00 57.86 C
ANISOU 4509 CD ARG A 590 6813 4596 10575 -537 -4182 472 C
ATOM 4510 NE ARG A 590 25.808 36.844 -33.055 1.00 67.22 N
ANISOU 4510 NE ARG A 590 7928 5795 11820 -572 -4215 492 N
ATOM 4511 CZ ARG A 590 25.598 37.598 -34.128 1.00 65.32 C
ANISOU 4511 CZ ARG A 590 7643 5534 11641 -613 -4288 519 C
ATOM 4512 NH1 ARG A 590 25.851 37.123 -35.340 1.00 54.28 N
ANISOU 4512 NH1 ARG A 590 6267 4100 10256 -625 -4337 526 N
ATOM 4513 NH2 ARG A 590 25.130 38.831 -33.989 1.00 66.40 N
ANISOU 4513 NH2 ARG A 590 7711 5689 11829 -643 -4314 539 N
ATOM 4514 N TRP A 591 25.558 29.947 -32.333 1.00 51.01 N
ANISOU 4514 N TRP A 591 6272 3674 9434 -350 -4100 342 N
ATOM 4515 CA TRP A 591 26.209 28.641 -32.297 1.00 47.61 C
ANISOU 4515 CA TRP A 591 5894 3246 8950 -320 -4060 335 C
ATOM 4516 C TRP A 591 25.350 27.583 -32.976 1.00 46.59 C
ANISOU 4516 C TRP A 591 5838 3075 8787 -287 -4107 310 C
ATOM 4517 O TRP A 591 25.853 26.766 -33.756 1.00 46.53 O
ANISOU 4517 O TRP A 591 5861 3053 8764 -282 -4118 316 O
ATOM 4518 CB TRP A 591 26.511 28.234 -30.857 1.00 45.41 C
ANISOU 4518 CB TRP A 591 5626 3005 8622 -291 -3977 320 C
ATOM 4519 CG TRP A 591 27.348 27.000 -30.770 1.00 44.60 C
ANISOU 4519 CG TRP A 591 5564 2914 8469 -268 -3933 318 C
ATOM 4520 CD1 TRP A 591 28.701 26.942 -30.625 1.00 44.21 C
ANISOU 4520 CD1 TRP A 591 5485 2896 8416 -284 -3884 338 C
ATOM 4521 CD2 TRP A 591 26.893 25.641 -30.839 1.00 44.13 C
ANISOU 4521 CD2 TRP A 591 5578 2836 8353 -225 -3933 294 C
ATOM 4522 NE1 TRP A 591 29.119 25.635 -30.593 1.00 43.52 N
ANISOU 4522 NE1 TRP A 591 5450 2813 8274 -255 -3855 329 N
ATOM 4523 CE2 TRP A 591 28.030 24.817 -30.722 1.00 43.46 C
ANISOU 4523 CE2 TRP A 591 5504 2775 8234 -219 -3884 303 C
ATOM 4524 CE3 TRP A 591 25.638 25.042 -30.984 1.00 44.22 C
ANISOU 4524 CE3 TRP A 591 5646 2814 8340 -192 -3971 267 C
ATOM 4525 CZ2 TRP A 591 27.950 23.428 -30.749 1.00 42.89 C
ANISOU 4525 CZ2 TRP A 591 5485 2730 8081 -193 -3847 276 C
ATOM 4526 CZ3 TRP A 591 25.561 23.661 -31.010 1.00 43.64 C
ANISOU 4526 CZ3 TRP A 591 5625 2774 8182 -167 -3929 238 C
ATOM 4527 CH2 TRP A 591 26.710 22.870 -30.891 1.00 42.99 C
ANISOU 4527 CH2 TRP A 591 5544 2733 8056 -169 -3867 244 C
ATOM 4528 N LEU A 592 24.048 27.569 -32.672 1.00 46.72 N
ANISOU 4528 N LEU A 592 5887 3075 8790 -264 -4135 281 N
ATOM 4529 CA LEU A 592 23.156 26.599 -33.298 1.00 46.85 C
ANISOU 4529 CA LEU A 592 5975 3052 8774 -231 -4181 256 C
ATOM 4530 C LEU A 592 23.050 26.821 -34.800 1.00 50.58 C
ANISOU 4530 C LEU A 592 6445 3486 9287 -258 -4264 269 C
ATOM 4531 O LEU A 592 22.832 25.866 -35.552 1.00 47.94 O
ANISOU 4531 O LEU A 592 6167 3122 8927 -237 -4296 258 O
ATOM 4532 CB LEU A 592 21.773 26.659 -32.648 1.00 46.85 C
ANISOU 4532 CB LEU A 592 6004 3043 8756 -203 -4195 223 C
ATOM 4533 CG LEU A 592 21.605 25.887 -31.339 1.00 55.48 C
ANISOU 4533 CG LEU A 592 7132 4157 9790 -160 -4125 201 C
ATOM 4534 CD1 LEU A 592 20.168 25.970 -30.845 1.00 49.11 C
ANISOU 4534 CD1 LEU A 592 6354 3336 8968 -134 -4147 168 C
ATOM 4535 CD2 LEU A 592 22.026 24.438 -31.530 1.00 54.19 C
ANISOU 4535 CD2 LEU A 592 7019 4014 9558 -135 -4083 188 C
ATOM 4536 N ASN A 593 23.197 28.067 -35.256 1.00 50.41 N
ANISOU 4536 N ASN A 593 6358 3466 9329 -305 -4301 292 N
ATOM 4537 CA ASN A 593 23.171 28.336 -36.690 1.00 52.51 C
ANISOU 4537 CA ASN A 593 6617 3697 9639 -336 -4381 307 C
ATOM 4538 C ASN A 593 24.447 27.840 -37.361 1.00 52.30 C
ANISOU 4538 C ASN A 593 6585 3672 9615 -350 -4364 333 C
ATOM 4539 O ASN A 593 24.392 27.147 -38.385 1.00 49.95 O
ANISOU 4539 O ASN A 593 6328 3342 9310 -344 -4410 329 O
ATOM 4540 CB ASN A 593 22.971 29.831 -36.939 1.00 52.84 C
ANISOU 4540 CB ASN A 593 6585 3742 9751 -385 -4424 328 C
ATOM 4541 CG ASN A 593 22.668 30.148 -38.391 1.00 52.59 C
ANISOU 4541 CG ASN A 593 6548 3670 9765 -416 -4519 337 C
ATOM 4542 OD1 ASN A 593 21.549 29.941 -38.860 1.00 52.57 O
ANISOU 4542 OD1 ASN A 593 6589 3634 9753 -401 -4583 311 O
ATOM 4543 ND2 ASN A 593 23.662 30.659 -39.109 1.00 52.51 N
ANISOU 4543 ND2 ASN A 593 6484 3661 9804 -459 -4530 375 N
ATOM 4544 N LYS A 594 25.607 28.175 -36.791 1.00 56.37 N
ANISOU 4544 N LYS A 594 7050 4226 10140 -368 -4298 357 N
ATOM 4545 CA LYS A 594 26.873 27.751 -37.383 1.00 56.12 C
ANISOU 4545 CA LYS A 594 7010 4202 10112 -382 -4279 382 C
ATOM 4546 C LYS A 594 27.033 26.237 -37.349 1.00 60.42 C
ANISOU 4546 C LYS A 594 7626 4742 10588 -338 -4251 363 C
ATOM 4547 O LYS A 594 27.675 25.659 -38.235 1.00 60.15 O
ANISOU 4547 O LYS A 594 7606 4695 10552 -345 -4266 376 O
ATOM 4548 CB LYS A 594 28.042 28.426 -36.663 1.00 54.16 C
ANISOU 4548 CB LYS A 594 6696 4000 9883 -408 -4211 410 C
ATOM 4549 CG LYS A 594 29.373 28.290 -37.385 1.00 61.27 C
ANISOU 4549 CG LYS A 594 7570 4907 10802 -434 -4200 441 C
ATOM 4550 CD LYS A 594 30.457 29.148 -36.747 1.00 69.85 C
ANISOU 4550 CD LYS A 594 8586 6038 11918 -464 -4142 469 C
ATOM 4551 CE LYS A 594 31.157 28.432 -35.605 1.00 75.30 C
ANISOU 4551 CE LYS A 594 9296 6769 12548 -434 -4054 457 C
ATOM 4552 NZ LYS A 594 32.323 29.221 -35.116 1.00 74.91 N
ANISOU 4552 NZ LYS A 594 9178 6760 12525 -465 -4001 485 N
ATOM 4553 N ASN A 595 26.455 25.577 -36.347 1.00 61.54 N
ANISOU 4553 N ASN A 595 7812 4894 10674 -295 -4210 335 N
ATOM 4554 CA ASN A 595 26.550 24.130 -36.176 1.00 55.80 C
ANISOU 4554 CA ASN A 595 7152 4168 9883 -252 -4179 318 C
ATOM 4555 C ASN A 595 25.201 23.449 -36.389 1.00 49.06 C
ANISOU 4555 C ASN A 595 6365 3276 8998 -213 -4224 285 C
ATOM 4556 O ASN A 595 24.857 22.488 -35.698 1.00 45.91 O
ANISOU 4556 O ASN A 595 6006 2919 8519 -182 -4163 252 O
ATOM 4557 CB ASN A 595 27.105 23.791 -34.795 1.00 45.44 C
ANISOU 4557 CB ASN A 595 5836 2902 8528 -231 -4089 313 C
ATOM 4558 CG ASN A 595 28.508 24.325 -34.580 1.00 45.24 C
ANISOU 4558 CG ASN A 595 5751 2915 8525 -265 -4041 342 C
ATOM 4559 OD1 ASN A 595 29.492 23.676 -34.934 1.00 50.85 O
ANISOU 4559 OD1 ASN A 595 6467 3636 9218 -267 -4018 356 O
ATOM 4560 ND2 ASN A 595 28.606 25.512 -33.990 1.00 45.43 N
ANISOU 4560 ND2 ASN A 595 5716 2960 8587 -291 -4025 353 N
ATOM 4561 N SER A 596 24.423 23.936 -37.359 1.00 47.70 N
ANISOU 4561 N SER A 596 6196 3065 8862 -229 -4306 281 N
ATOM 4562 CA SER A 596 23.079 23.415 -37.580 1.00 48.12 C
ANISOU 4562 CA SER A 596 6311 3082 8890 -195 -4355 249 C
ATOM 4563 C SER A 596 23.070 21.971 -38.066 1.00 47.58 C
ANISOU 4563 C SER A 596 6304 3023 8750 -168 -4338 227 C
ATOM 4564 O SER A 596 22.037 21.304 -37.951 1.00 47.46 O
ANISOU 4564 O SER A 596 6339 3011 8681 -137 -4338 189 O
ATOM 4565 CB SER A 596 22.328 24.296 -38.579 1.00 50.25 C
ANISOU 4565 CB SER A 596 6565 3315 9211 -225 -4448 248 C
ATOM 4566 OG SER A 596 23.080 24.469 -39.767 1.00 53.03 O
ANISOU 4566 OG SER A 596 6895 3652 9602 -260 -4489 274 O
ATOM 4567 N GLN A 597 24.180 21.471 -38.614 1.00 47.37 N
ANISOU 4567 N GLN A 597 6271 3010 8715 -181 -4317 247 N
ATOM 4568 CA GLN A 597 24.194 20.073 -39.029 1.00 52.79 C
ANISOU 4568 CA GLN A 597 7011 3721 9326 -159 -4288 223 C
ATOM 4569 C GLN A 597 24.236 19.140 -37.827 1.00 51.76 C
ANISOU 4569 C GLN A 597 6897 3662 9106 -133 -4181 196 C
ATOM 4570 O GLN A 597 23.854 17.970 -37.939 1.00 50.78 O
ANISOU 4570 O GLN A 597 6822 3559 8912 -107 -4155 168 O
ATOM 4571 CB GLN A 597 25.382 19.792 -39.950 1.00 55.40 C
ANISOU 4571 CB GLN A 597 7330 4046 9674 -182 -4297 252 C
ATOM 4572 CG GLN A 597 26.642 19.311 -39.238 1.00 67.75 C
ANISOU 4572 CG GLN A 597 8870 5673 11198 -186 -4199 263 C
ATOM 4573 CD GLN A 597 27.609 20.437 -38.935 1.00 75.53 C
ANISOU 4573 CD GLN A 597 9789 6657 12253 -218 -4194 302 C
ATOM 4574 OE1 GLN A 597 27.227 21.606 -38.909 1.00 78.52 O
ANISOU 4574 OE1 GLN A 597 10136 6998 12702 -234 -4246 318 O
ATOM 4575 NE2 GLN A 597 28.872 20.091 -38.715 1.00 75.00 N
ANISOU 4575 NE2 GLN A 597 9701 6629 12168 -229 -4133 319 N
ATOM 4576 N LYS A 598 24.686 19.639 -36.673 1.00 51.07 N
ANISOU 4576 N LYS A 598 6770 3611 9023 -138 -4120 203 N
ATOM 4577 CA LYS A 598 24.831 18.793 -35.495 1.00 45.15 C
ANISOU 4577 CA LYS A 598 6033 2928 8194 -116 -4020 181 C
ATOM 4578 C LYS A 598 23.545 18.718 -34.682 1.00 46.33 C
ANISOU 4578 C LYS A 598 6207 3087 8310 -89 -4007 147 C
ATOM 4579 O LYS A 598 23.283 17.694 -34.042 1.00 45.04 O
ANISOU 4579 O LYS A 598 6074 2968 8071 -64 -3943 121 O
ATOM 4580 CB LYS A 598 25.983 19.307 -34.628 1.00 43.63 C
ANISOU 4580 CB LYS A 598 5789 2772 8019 -135 -3960 205 C
ATOM 4581 CG LYS A 598 27.311 19.394 -35.382 1.00 52.46 C
ANISOU 4581 CG LYS A 598 6879 3883 9170 -163 -3969 240 C
ATOM 4582 CD LYS A 598 28.407 20.078 -34.572 1.00 50.49 C
ANISOU 4582 CD LYS A 598 6576 3660 8947 -182 -3922 265 C
ATOM 4583 CE LYS A 598 29.725 20.087 -35.339 1.00 48.95 C
ANISOU 4583 CE LYS A 598 6357 3460 8782 -208 -3929 299 C
ATOM 4584 NZ LYS A 598 30.806 20.848 -34.646 1.00 52.09 N
ANISOU 4584 NZ LYS A 598 6700 3877 9213 -229 -3891 326 N
ATOM 4585 N GLU A 599 22.730 19.769 -34.698 1.00 49.19 N
ANISOU 4585 N GLU A 599 6555 3407 8728 -93 -4069 148 N
ATOM 4586 CA GLU A 599 21.521 19.770 -33.888 1.00 48.00 C
ANISOU 4586 CA GLU A 599 6425 3264 8548 -67 -4058 116 C
ATOM 4587 C GLU A 599 20.525 18.736 -34.397 1.00 46.68 C
ANISOU 4587 C GLU A 599 6321 3090 8325 -38 -4076 82 C
ATOM 4588 O GLU A 599 20.229 18.674 -35.593 1.00 45.95 O
ANISOU 4588 O GLU A 599 6254 2951 8256 -41 -4151 84 O
ATOM 4589 CB GLU A 599 20.879 21.153 -33.880 1.00 45.26 C
ANISOU 4589 CB GLU A 599 6050 2869 8278 -80 -4128 125 C
ATOM 4590 CG GLU A 599 19.531 21.171 -33.186 1.00 47.08 C
ANISOU 4590 CG GLU A 599 6306 3101 8483 -53 -4129 91 C
ATOM 4591 CD GLU A 599 19.046 22.572 -32.917 1.00 51.84 C
ANISOU 4591 CD GLU A 599 6873 3666 9160 -68 -4182 102 C
ATOM 4592 OE1 GLU A 599 18.388 22.782 -31.877 1.00 54.32 O
ANISOU 4592 OE1 GLU A 599 7184 3999 9456 -52 -4151 83 O
ATOM 4593 OE2 GLU A 599 19.332 23.464 -33.741 1.00 56.69 O
ANISOU 4593 OE2 GLU A 599 7457 4228 9852 -96 -4257 133 O
ATOM 4594 N GLN A 600 20.008 17.926 -33.476 1.00 47.07 N
ANISOU 4594 N GLN A 600 6396 3185 8303 -10 -4009 53 N
ATOM 4595 CA GLN A 600 18.972 16.944 -33.765 1.00 45.40 C
ANISOU 4595 CA GLN A 600 6242 2971 8035 21 -4017 20 C
ATOM 4596 C GLN A 600 17.652 17.471 -33.214 1.00 45.23 C
ANISOU 4596 C GLN A 600 6233 2934 8021 39 -4044 -5 C
ATOM 4597 O GLN A 600 17.560 17.804 -32.029 1.00 43.63 O
ANISOU 4597 O GLN A 600 6005 2762 7809 42 -3992 -9 O
ATOM 4598 CB GLN A 600 19.319 15.590 -33.145 1.00 45.68 C
ANISOU 4598 CB GLN A 600 6299 3070 7987 38 -3922 7 C
ATOM 4599 CG GLN A 600 20.767 15.156 -33.350 1.00 42.45 C
ANISOU 4599 CG GLN A 600 5870 2689 7571 19 -3880 32 C
ATOM 4600 CD GLN A 600 21.093 14.860 -34.801 1.00 43.04 C
ANISOU 4600 CD GLN A 600 5964 2727 7662 9 -3939 44 C
ATOM 4601 OE1 GLN A 600 20.428 14.050 -35.448 1.00 43.24 O
ANISOU 4601 OE1 GLN A 600 6037 2740 7652 29 -3962 24 O
ATOM 4602 NE2 GLN A 600 22.121 15.522 -35.322 1.00 43.35 N
ANISOU 4602 NE2 GLN A 600 5966 2747 7756 -21 -3964 76 N
ATOM 4603 N GLY A 601 16.638 17.547 -34.068 1.00 44.93 N
ANISOU 4603 N GLY A 601 6231 2844 7996 51 -4126 -22 N
ATOM 4604 CA GLY A 601 15.419 18.219 -33.676 1.00 45.34 C
ANISOU 4604 CA GLY A 601 6290 2870 8067 65 -4167 -42 C
ATOM 4605 C GLY A 601 15.590 19.725 -33.757 1.00 49.19 C
ANISOU 4605 C GLY A 601 6730 3316 8645 36 -4228 -16 C
ATOM 4606 O GLY A 601 16.514 20.247 -34.390 1.00 51.96 O
ANISOU 4606 O GLY A 601 7048 3645 9050 6 -4258 17 O
ATOM 4607 N SER A 602 14.686 20.435 -33.087 1.00 50.74 N
ANISOU 4607 N SER A 602 6919 3500 8860 44 -4246 -31 N
ATOM 4608 CA SER A 602 14.648 21.891 -33.166 1.00 54.71 C
ANISOU 4608 CA SER A 602 7378 3957 9452 19 -4313 -8 C
ATOM 4609 C SER A 602 14.387 22.470 -31.785 1.00 56.84 C
ANISOU 4609 C SER A 602 7617 4257 9722 23 -4263 -14 C
ATOM 4610 O SER A 602 13.286 22.320 -31.245 1.00 61.55 O
ANISOU 4610 O SER A 602 8240 4858 10288 49 -4261 -46 O
ATOM 4611 CB SER A 602 13.582 22.358 -34.155 1.00 49.81 C
ANISOU 4611 CB SER A 602 6787 3264 8876 23 -4432 -19 C
ATOM 4612 OG SER A 602 13.934 22.003 -35.479 1.00 53.58 O
ANISOU 4612 OG SER A 602 7286 3706 9367 14 -4488 -8 O
ATOM 4613 N ALA A 603 15.393 23.134 -31.221 1.00 55.98 N
ANISOU 4613 N ALA A 603 7452 4169 9648 -3 -4223 17 N
ATOM 4614 CA ALA A 603 15.186 23.985 -30.057 1.00 58.85 C
ANISOU 4614 CA ALA A 603 7778 4548 10034 -6 -4196 18 C
ATOM 4615 C ALA A 603 14.395 25.212 -30.493 1.00 61.59 C
ANISOU 4615 C ALA A 603 8110 4828 10463 -19 -4299 25 C
ATOM 4616 O ALA A 603 14.883 26.026 -31.286 1.00 59.30 O
ANISOU 4616 O ALA A 603 7776 4531 10225 -59 -4342 51 O
ATOM 4617 CB ALA A 603 16.524 24.380 -29.441 1.00 45.32 C
ANISOU 4617 CB ALA A 603 6011 2870 8340 -31 -4133 50 C
ATOM 4618 N LYS A 604 13.167 25.340 -30.003 1.00 60.71 N
ANISOU 4618 N LYS A 604 8021 4708 10338 4 -4319 -5 N
ATOM 4619 CA LYS A 604 12.275 26.415 -30.407 1.00 59.75 C
ANISOU 4619 CA LYS A 604 7872 4578 10251 -19 -4389 -15 C
ATOM 4620 C LYS A 604 12.003 27.333 -29.226 1.00 59.98 C
ANISOU 4620 C LYS A 604 7852 4647 10290 -29 -4352 -17 C
ATOM 4621 O LYS A 604 11.957 26.888 -28.073 1.00 63.18 O
ANISOU 4621 O LYS A 604 8273 5072 10662 -1 -4286 -29 O
ATOM 4622 CB LYS A 604 10.960 25.864 -30.962 1.00 58.19 C
ANISOU 4622 CB LYS A 604 7741 4344 10026 14 -4453 -53 C
ATOM 4623 CG LYS A 604 11.138 24.798 -32.035 1.00 61.46 C
ANISOU 4623 CG LYS A 604 8213 4718 10420 33 -4486 -54 C
ATOM 4624 CD LYS A 604 9.801 24.437 -32.662 1.00 63.99 C
ANISOU 4624 CD LYS A 604 8595 5001 10718 62 -4559 -92 C
ATOM 4625 CE LYS A 604 9.415 22.987 -32.409 1.00 60.54 C
ANISOU 4625 CE LYS A 604 8221 4589 10192 105 -4504 -125 C
ATOM 4626 NZ LYS A 604 9.790 22.095 -33.543 1.00 56.47 N
ANISOU 4626 NZ LYS A 604 7743 4064 9652 108 -4521 -124 N
ATOM 4627 N CYS A 605 11.811 28.613 -29.525 1.00 61.36 N
ANISOU 4627 N CYS A 605 7967 4834 10513 -69 -4396 -5 N
ATOM 4628 CA CYS A 605 11.651 29.614 -28.482 1.00 62.34 C
ANISOU 4628 CA CYS A 605 8034 5000 10654 -85 -4364 -2 C
ATOM 4629 C CYS A 605 10.302 29.476 -27.792 1.00 60.83 C
ANISOU 4629 C CYS A 605 7876 4811 10426 -51 -4371 -41 C
ATOM 4630 O CYS A 605 9.294 29.142 -28.421 1.00 61.20 O
ANISOU 4630 O CYS A 605 7968 4828 10455 -31 -4433 -69 O
ATOM 4631 CB CYS A 605 11.790 31.008 -29.077 1.00 65.30 C
ANISOU 4631 CB CYS A 605 8332 5388 11090 -138 -4415 25 C
ATOM 4632 SG CYS A 605 13.394 31.260 -29.821 1.00 72.38 S
ANISOU 4632 SG CYS A 605 9183 6286 12033 -181 -4404 74 S
ATOM 4633 N SER A 606 10.295 29.735 -26.489 1.00 58.86 N
ANISOU 4633 N SER A 606 7603 4596 10164 -43 -4308 -45 N
ATOM 4634 CA SER A 606 9.057 29.781 -25.722 1.00 58.70 C
ANISOU 4634 CA SER A 606 7602 4587 10114 -16 -4310 -80 C
ATOM 4635 C SER A 606 8.164 30.904 -26.232 1.00 61.57 C
ANISOU 4635 C SER A 606 7926 4960 10508 -40 -4387 -84 C
ATOM 4636 O SER A 606 8.629 32.022 -26.452 1.00 65.93 O
ANISOU 4636 O SER A 606 8406 5536 11109 -85 -4403 -53 O
ATOM 4637 CB SER A 606 9.354 29.974 -24.234 1.00 60.66 C
ANISOU 4637 CB SER A 606 7823 4875 10350 -9 -4227 -77 C
ATOM 4638 OG SER A 606 10.238 31.062 -24.025 1.00 63.96 O
ANISOU 4638 OG SER A 606 8161 5326 10813 -52 -4206 -41 O
ATOM 4639 N GLY A 609 8.171 29.550 -30.995 1.00 57.40 N
ANISOU 4639 N GLY A 609 7514 4285 10012 -57 -4622 -83 N
ATOM 4640 CA GLY A 609 8.113 28.462 -31.954 1.00 52.20 C
ANISOU 4640 CA GLY A 609 6927 3579 9329 -32 -4657 -96 C
ATOM 4641 C GLY A 609 9.197 28.537 -33.011 1.00 58.49 C
ANISOU 4641 C GLY A 609 7701 4358 10164 -68 -4680 -60 C
ATOM 4642 O GLY A 609 9.509 27.542 -33.667 1.00 68.09 O
ANISOU 4642 O GLY A 609 8970 5542 11360 -48 -4687 -62 O
ATOM 4643 N LYS A 610 9.765 29.723 -33.184 1.00 58.34 N
ANISOU 4643 N LYS A 610 7603 4362 10202 -120 -4692 -27 N
ATOM 4644 CA LYS A 610 10.875 29.879 -34.112 1.00 68.33 C
ANISOU 4644 CA LYS A 610 8839 5616 11509 -157 -4708 9 C
ATOM 4645 C LYS A 610 12.086 29.119 -33.581 1.00 68.15 C
ANISOU 4645 C LYS A 610 8824 5605 11466 -144 -4618 29 C
ATOM 4646 O LYS A 610 12.378 29.194 -32.379 1.00 67.30 O
ANISOU 4646 O LYS A 610 8695 5533 11344 -135 -4542 32 O
ATOM 4647 CB LYS A 610 11.218 31.355 -34.296 1.00 73.46 C
ANISOU 4647 CB LYS A 610 9396 6292 12225 -216 -4734 43 C
ATOM 4648 CG LYS A 610 12.259 31.610 -35.372 1.00 81.93 C
ANISOU 4648 CG LYS A 610 10435 7349 13345 -259 -4762 80 C
ATOM 4649 CD LYS A 610 11.720 32.527 -36.451 1.00 85.76 C
ANISOU 4649 CD LYS A 610 10886 7818 13879 -300 -4865 87 C
ATOM 4650 CE LYS A 610 12.681 32.613 -37.624 1.00 83.15 C
ANISOU 4650 CE LYS A 610 10534 7465 13594 -339 -4899 120 C
ATOM 4651 NZ LYS A 610 12.537 33.896 -38.366 1.00 82.09 N
ANISOU 4651 NZ LYS A 610 10329 7333 13527 -396 -4976 144 N
ATOM 4652 N PRO A 611 12.794 28.367 -34.423 1.00 68.47 N
ANISOU 4652 N PRO A 611 8893 5619 11503 -143 -4626 41 N
ATOM 4653 CA PRO A 611 14.012 27.693 -33.957 1.00 66.45 C
ANISOU 4653 CA PRO A 611 8638 5380 11229 -134 -4544 62 C
ATOM 4654 C PRO A 611 15.002 28.703 -33.400 1.00 64.84 C
ANISOU 4654 C PRO A 611 8351 5218 11067 -175 -4497 98 C
ATOM 4655 O PRO A 611 15.167 29.798 -33.942 1.00 67.94 O
ANISOU 4655 O PRO A 611 8683 5615 11515 -221 -4540 120 O
ATOM 4656 CB PRO A 611 14.550 27.014 -35.222 1.00 67.30 C
ANISOU 4656 CB PRO A 611 8777 5454 11340 -138 -4583 74 C
ATOM 4657 CG PRO A 611 13.369 26.893 -36.128 1.00 69.96 C
ANISOU 4657 CG PRO A 611 9159 5749 11672 -127 -4675 45 C
ATOM 4658 CD PRO A 611 12.504 28.081 -35.837 1.00 69.92 C
ANISOU 4658 CD PRO A 611 9112 5758 11697 -148 -4712 36 C
ATOM 4659 N VAL A 612 15.648 28.334 -32.288 1.00 57.41 N
ANISOU 4659 N VAL A 612 7406 4308 10099 -157 -4408 102 N
ATOM 4660 CA VAL A 612 16.680 29.195 -31.715 1.00 56.62 C
ANISOU 4660 CA VAL A 612 7232 4248 10033 -192 -4356 135 C
ATOM 4661 C VAL A 612 17.768 29.464 -32.745 1.00 54.81 C
ANISOU 4661 C VAL A 612 6968 4012 9846 -232 -4377 171 C
ATOM 4662 O VAL A 612 18.359 30.550 -32.778 1.00 49.84 O
ANISOU 4662 O VAL A 612 6265 3405 9267 -275 -4376 202 O
ATOM 4663 CB VAL A 612 17.262 28.574 -30.430 1.00 51.58 C
ANISOU 4663 CB VAL A 612 6606 3641 9352 -164 -4260 132 C
ATOM 4664 CG1 VAL A 612 18.309 29.495 -29.817 1.00 50.87 C
ANISOU 4664 CG1 VAL A 612 6440 3592 9295 -198 -4208 163 C
ATOM 4665 CG2 VAL A 612 16.160 28.278 -29.432 1.00 47.27 C
ANISOU 4665 CG2 VAL A 612 6096 3099 8766 -125 -4241 96 C
ATOM 4666 N ARG A 613 18.027 28.493 -33.623 1.00 51.86 N
ANISOU 4666 N ARG A 613 6643 3608 9453 -218 -4399 170 N
ATOM 4667 CA ARG A 613 19.010 28.671 -34.684 1.00 58.08 C
ANISOU 4667 CA ARG A 613 7402 4386 10279 -254 -4425 202 C
ATOM 4668 C ARG A 613 18.627 29.754 -35.686 1.00 63.98 C
ANISOU 4668 C ARG A 613 8106 5115 11089 -299 -4511 216 C
ATOM 4669 O ARG A 613 19.466 30.123 -36.514 1.00 69.44 O
ANISOU 4669 O ARG A 613 8759 5802 11822 -337 -4532 248 O
ATOM 4670 CB ARG A 613 19.232 27.352 -35.430 1.00 57.82 C
ANISOU 4670 CB ARG A 613 7436 4324 10209 -226 -4436 195 C
ATOM 4671 CG ARG A 613 18.041 26.875 -36.250 1.00 58.71 C
ANISOU 4671 CG ARG A 613 7610 4390 10306 -204 -4514 165 C
ATOM 4672 CD ARG A 613 18.514 26.134 -37.497 1.00 65.26 C
ANISOU 4672 CD ARG A 613 8474 5189 11135 -206 -4554 174 C
ATOM 4673 NE ARG A 613 17.480 25.280 -38.076 1.00 74.68 N
ANISOU 4673 NE ARG A 613 9743 6341 12293 -170 -4608 141 N
ATOM 4674 CZ ARG A 613 17.609 24.633 -39.231 1.00 85.02 C
ANISOU 4674 CZ ARG A 613 11091 7615 13598 -167 -4657 142 C
ATOM 4675 NH1 ARG A 613 18.725 24.750 -39.940 1.00 81.78 N
ANISOU 4675 NH1 ARG A 613 10648 7207 13218 -201 -4659 175 N
ATOM 4676 NH2 ARG A 613 16.619 23.875 -39.682 1.00 91.48 N
ANISOU 4676 NH2 ARG A 613 11980 8397 14381 -131 -4705 110 N
ATOM 4677 N SER A 614 17.395 30.266 -35.645 1.00 70.52 N
ANISOU 4677 N SER A 614 8937 5933 11923 -297 -4562 194 N
ATOM 4678 CA SER A 614 16.980 31.299 -36.587 1.00 75.69 C
ANISOU 4678 CA SER A 614 9549 6573 12637 -341 -4648 206 C
ATOM 4679 C SER A 614 16.694 32.617 -35.878 1.00 69.99 C
ANISOU 4679 C SER A 614 8754 5887 11952 -370 -4642 218 C
ATOM 4680 O SER A 614 15.600 33.176 -36.006 1.00 63.98 O
ANISOU 4680 O SER A 614 7988 5121 11202 -375 -4701 201 O
ATOM 4681 CB SER A 614 15.756 30.837 -37.379 1.00 84.41 C
ANISOU 4681 CB SER A 614 10717 7634 13722 -320 -4732 171 C
ATOM 4682 OG SER A 614 16.106 29.843 -38.323 1.00 93.68 O
ANISOU 4682 OG SER A 614 11945 8773 14879 -307 -4755 169 O
ATOM 4683 N ILE A 615 17.674 33.126 -35.134 1.00 69.19 N
ANISOU 4683 N ILE A 615 8595 5825 11868 -388 -4572 247 N
ATOM 4684 CA ILE A 615 17.520 34.363 -34.376 1.00 64.23 C
ANISOU 4684 CA ILE A 615 7894 5237 11274 -413 -4556 261 C
ATOM 4685 C ILE A 615 18.805 35.163 -34.490 1.00 69.82 C
ANISOU 4685 C ILE A 615 8523 5970 12036 -459 -4527 310 C
ATOM 4686 O ILE A 615 19.870 34.694 -34.074 1.00 68.71 O
ANISOU 4686 O ILE A 615 8385 5845 11877 -450 -4457 322 O
ATOM 4687 CB ILE A 615 17.195 34.105 -32.898 1.00 61.54 C
ANISOU 4687 CB ILE A 615 7571 4927 10885 -375 -4482 237 C
ATOM 4688 CG1 ILE A 615 15.798 33.516 -32.759 1.00 67.20 C
ANISOU 4688 CG1 ILE A 615 8355 5622 11556 -334 -4516 191 C
ATOM 4689 CG2 ILE A 615 17.317 35.390 -32.088 1.00 54.41 C
ANISOU 4689 CG2 ILE A 615 6585 4070 10019 -404 -4454 260 C
ATOM 4690 CD1 ILE A 615 15.365 33.437 -31.356 1.00 66.16 C
ANISOU 4690 CD1 ILE A 615 8232 5520 11386 -302 -4453 169 C
ATOM 4691 N ILE A 616 18.709 36.369 -35.029 1.00 78.09 N
ANISOU 4691 N ILE A 616 9498 7024 13148 -507 -4580 339 N
ATOM 4692 CA ILE A 616 19.860 37.239 -35.213 1.00 76.86 C
ANISOU 4692 CA ILE A 616 9260 6892 13051 -554 -4560 389 C
ATOM 4693 C ILE A 616 19.651 38.458 -34.325 1.00 72.47 C
ANISOU 4693 C ILE A 616 8628 6382 12525 -574 -4538 406 C
ATOM 4694 O ILE A 616 18.844 39.339 -34.638 1.00 75.43 O
ANISOU 4694 O ILE A 616 8962 6760 12936 -599 -4601 412 O
ATOM 4695 CB ILE A 616 20.054 37.636 -36.680 1.00 73.41 C
ANISOU 4695 CB ILE A 616 8795 6424 12673 -599 -4642 416 C
ATOM 4696 CG1 ILE A 616 19.904 36.417 -37.593 1.00 68.88 C
ANISOU 4696 CG1 ILE A 616 8306 5801 12065 -574 -4681 390 C
ATOM 4697 CG2 ILE A 616 21.418 38.280 -36.876 1.00 72.68 C
ANISOU 4697 CG2 ILE A 616 8628 6352 12634 -641 -4610 468 C
ATOM 4698 CD1 ILE A 616 20.985 35.372 -37.410 1.00 65.06 C
ANISOU 4698 CD1 ILE A 616 7861 5318 11542 -549 -4611 392 C
ATOM 4699 N CYS A 617 20.379 38.508 -33.208 1.00 68.56 N
ANISOU 4699 N CYS A 617 8113 5925 12013 -563 -4448 414 N
ATOM 4700 CA CYS A 617 20.410 39.701 -32.386 1.00 71.67 C
ANISOU 4700 CA CYS A 617 8426 6367 12440 -584 -4420 438 C
ATOM 4701 C CYS A 617 21.041 40.845 -33.179 1.00 80.43 C
ANISOU 4701 C CYS A 617 9443 7486 13631 -643 -4455 493 C
ATOM 4702 O CYS A 617 21.706 40.611 -34.191 1.00 92.25 O
ANISOU 4702 O CYS A 617 10941 8955 15153 -664 -4482 512 O
ATOM 4703 CB CYS A 617 21.192 39.432 -31.097 1.00 67.65 C
ANISOU 4703 CB CYS A 617 7917 5892 11894 -560 -4317 436 C
ATOM 4704 SG CYS A 617 20.352 38.293 -29.979 1.00 66.46 S
ANISOU 4704 SG CYS A 617 7858 5738 11655 -495 -4273 376 S
ATOM 4705 N PRO A 618 20.815 42.103 -32.758 1.00 73.82 N
ANISOU 4705 N PRO A 618 8523 6689 12838 -670 -4459 520 N
ATOM 4706 CA PRO A 618 21.397 43.256 -33.457 1.00 76.82 C
ANISOU 4706 CA PRO A 618 8806 7081 13299 -726 -4490 577 C
ATOM 4707 C PRO A 618 22.896 43.116 -33.729 1.00 88.12 C
ANISOU 4707 C PRO A 618 10215 8512 14752 -744 -4443 612 C
ATOM 4708 O PRO A 618 23.704 43.712 -33.017 1.00 92.90 O
ANISOU 4708 O PRO A 618 10761 9159 15377 -754 -4379 642 O
ATOM 4709 CB PRO A 618 21.135 44.412 -32.493 1.00 67.95 C
ANISOU 4709 CB PRO A 618 7604 6014 12199 -736 -4462 598 C
ATOM 4710 CG PRO A 618 19.901 44.018 -31.782 1.00 65.19 C
ANISOU 4710 CG PRO A 618 7310 5668 11793 -696 -4467 548 C
ATOM 4711 CD PRO A 618 19.951 42.525 -31.640 1.00 65.88 C
ANISOU 4711 CD PRO A 618 7505 5718 11808 -649 -4437 501 C
TER 4712 PRO A 618
HETATM 4713 C1 NAG A 701 40.787 5.708 -8.169 1.00 61.23 C
HETATM 4714 C2 NAG A 701 42.074 6.189 -8.831 1.00 66.19 C
HETATM 4715 C3 NAG A 701 43.185 6.280 -7.798 1.00 66.11 C
HETATM 4716 C4 NAG A 701 42.764 7.189 -6.652 1.00 71.30 C
HETATM 4717 C5 NAG A 701 41.442 6.715 -6.047 1.00 65.31 C
HETATM 4718 C6 NAG A 701 40.897 7.663 -4.998 1.00 64.94 C
HETATM 4719 C7 NAG A 701 41.812 5.257 -11.091 1.00 78.77 C
HETATM 4720 C8 NAG A 701 42.389 4.339 -12.127 1.00 79.68 C
HETATM 4721 N2 NAG A 701 42.477 5.326 -9.935 1.00 72.77 N
HETATM 4722 O3 NAG A 701 44.377 6.762 -8.406 1.00 56.80 O
HETATM 4723 O4 NAG A 701 43.776 7.166 -5.654 1.00 77.39 O
HETATM 4724 O5 NAG A 701 40.442 6.605 -7.073 1.00 60.46 O
HETATM 4725 O6 NAG A 701 40.684 7.025 -3.745 1.00 65.93 O
HETATM 4726 O7 NAG A 701 40.790 5.903 -11.294 1.00 81.86 O
HETATM 4727 C1 NAG A 702 18.464 9.467 -24.255 1.00 43.59 C
HETATM 4728 C2 NAG A 702 18.620 8.682 -25.563 1.00 51.68 C
HETATM 4729 C3 NAG A 702 17.256 8.447 -26.222 1.00 49.05 C
HETATM 4730 C4 NAG A 702 16.247 7.887 -25.228 1.00 45.61 C
HETATM 4731 C5 NAG A 702 16.203 8.768 -23.987 1.00 47.00 C
HETATM 4732 C6 NAG A 702 15.265 8.260 -22.917 1.00 51.62 C
HETATM 4733 C7 NAG A 702 20.540 8.827 -27.097 1.00 57.92 C
HETATM 4734 C8 NAG A 702 20.770 7.375 -26.812 1.00 56.11 C
HETATM 4735 N2 NAG A 702 19.502 9.394 -26.474 1.00 55.63 N
HETATM 4736 O3 NAG A 702 17.417 7.539 -27.306 1.00 52.31 O
HETATM 4737 O4 NAG A 702 14.953 7.843 -25.820 1.00 47.48 O
HETATM 4738 O5 NAG A 702 17.513 8.818 -23.411 1.00 45.21 O
HETATM 4739 O6 NAG A 702 15.266 6.840 -22.842 1.00 60.03 O
HETATM 4740 O7 NAG A 702 21.262 9.462 -27.860 1.00 56.01 O
CONECT 13 101 12
CONECT 101 100 13
CONECT 2021 2020 2224
CONECT 2224 2021 2223
CONECT 2885 2884 2891
CONECT 2891 2885 2890
CONECT 3704 3702 4713
CONECT 3967 3965 4727
CONECT 4430 4429 4632
CONECT 4442 4441 4704
CONECT 4632 4430 4631
CONECT 4704 4442 4703
CONECT 4713 3704 4724 4714
CONECT 4714 4713 4715 4721
CONECT 4715 4722 4714 4716
CONECT 4716 4717 4715 4723
CONECT 4717 4718 4724 4716
CONECT 4718 4717 4725
CONECT 4719 4720 4726 4721
CONECT 4720 4719
CONECT 4721 4719 4714
CONECT 4722 4715
CONECT 4723 4716
CONECT 4724 4713 4717
CONECT 4725 4718
CONECT 4726 4719
CONECT 4727 3967 4728 4738
CONECT 4728 4727 4735 4729
CONECT 4729 4736 4730 4728
CONECT 4730 4731 4729 4737
CONECT 4731 4730 4738 4732
CONECT 4732 4731 4739
CONECT 4733 4735 4740 4734
CONECT 4734 4733
CONECT 4735 4733 4728
CONECT 4736 4729
CONECT 4737 4730
CONECT 4738 4727 4731
CONECT 4739 4732
CONECT 4740 4733
END
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