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*** TRANSFERASE 27-AUG-14 4UXX ***elNémo ID: 240124020217199678Job options:ID = 240124020217199678 JOBID = TRANSFERASE 27-AUG-14 4UXX 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 TRANSFERASE 27-AUG-14 4UXX TITLE STRUCTURE OF DELTA4-DGKA WITH AMPPCP IN 9.9 MAG COMPND MOL_ID: 1; COMPND 2 MOLECULE: DIACYLGLYCEROL KINASE; COMPND 3 CHAIN: A, B, C; COMPND 4 SYNONYM: DAGK, DIGLYCERIDE KINASE, DGK; COMPND 5 EC: 2.7.1.107; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12; SOURCE 3 ORGANISM_TAXID: 83333; SOURCE 4 ATCC: 29425; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: WH1061; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PTRCHISB; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCHISB-DGKA-DELTA4 KEYWDS TRANSFERASE, ATP ANALOGUE, DGKA, DIACYLGLYEROL KINASE, IN MESO KEYWDS 2 CRYSTALLIZATION, LIPID CUBIC PHASE, LIPIDIC CUBIC PHASE, LIPID KEYWDS 3 MESOPHASE, LIPIDIC MESOPHASE, MEMBRANE PROTEIN, 9.9 MAG, KEYWDS 4 MONOACYLGLYCEROL, NON- HYDROLYZABLE ATP ANALOGUE, NUCLEOTIDE KEYWDS 5 ANALOGUE EXPDTA X-RAY DIFFRACTION AUTHOR D.LI,L.VOGELEY,M.CAFFREY REVDAT 4 03-APR-19 4UXX 1 REMARK REVDAT 3 06-MAR-19 4UXX 1 REMARK ATOM REVDAT 2 13-JAN-16 4UXX 1 JRNL REVDAT 1 30-SEP-15 4UXX 0 JRNL AUTH D.LI,P.J.STANSFELD,M.S.P.SANSOM,A.KEOGH,L.VOGELEY,N.HOWE, JRNL AUTH 2 J.A.LYONS,D.ARAGAO,P.FROMME,R.FROMME,S.BASU,I.GROTJOHANN, JRNL AUTH 3 C.KUPITZ,K.RENDEK,U.WEIERSTALL,N.A.ZATSEPIN,V.CHEREZOV, JRNL AUTH 4 W.LIU,S.BANDARU,N.J.ENGLISH,C.GATI,A.BARTY,O.YEFANOV, JRNL AUTH 5 H.N.CHAPMAN,K.DIEDERICHS,M.MESSERSCHMIDT,S.BOUTET, JRNL AUTH 6 G.J.WILLIAMS,M.MARVIN SEIBERT,M.CAFFREY JRNL TITL TERNARY STRUCTURE REVEALS MECHANISM OF A MEMBRANE JRNL TITL 2 DIACYLGLYCEROL KINASE. JRNL REF NAT.COMMUN. V. 6 10140 2015 JRNL REFN ESSN 2041-1723 JRNL PMID 26673816 JRNL DOI 10.1038/NCOMMS10140 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE) 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.08 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 17165 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.219 REMARK 3 FREE R VALUE : 0.258 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900 REMARK 3 FREE R VALUE TEST SET COUNT : 850 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 53.0852 - 4.9067 0.99 2879 136 0.2256 0.2865 REMARK 3 2 4.9067 - 3.8950 1.00 2755 155 0.1862 0.2021 REMARK 3 3 3.8950 - 3.4027 1.00 2712 155 0.2141 0.2569 REMARK 3 4 3.4027 - 3.0917 1.00 2667 151 0.2416 0.2552 REMARK 3 5 3.0917 - 2.8701 1.00 2682 126 0.2524 0.3027 REMARK 3 6 2.8701 - 2.7009 0.97 2620 127 0.2780 0.3403 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.620 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 68.67 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.91 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 : 0.012 2843 REMARK 3 ANGLE : 0.749 3810 REMARK 3 CHIRALITY : 0.036 454 REMARK 3 PLANARITY : 0.003 460 REMARK 3 DIHEDRAL : 13.027 1044 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 10 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.0327 -15.3396 24.6987 REMARK 3 T TENSOR REMARK 3 T11: 0.6597 T22: 0.6592 REMARK 3 T33: 0.5546 T12: 0.1736 REMARK 3 T13: -0.0937 T23: -0.1208 REMARK 3 L TENSOR REMARK 3 L11: 4.0517 L22: 5.0842 REMARK 3 L33: 3.9087 L12: -0.5384 REMARK 3 L13: -3.0252 L23: 1.4467 REMARK 3 S TENSOR REMARK 3 S11: 0.3108 S12: 0.1325 S13: 0.3732 REMARK 3 S21: -0.2604 S22: 0.2931 S23: -0.1111 REMARK 3 S31: 0.0270 S32: 0.5119 S33: -0.5863 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 52 THROUGH 91 ) REMARK 3 ORIGIN FOR THE GROUP (A): 48.5967 -16.7510 16.3047 REMARK 3 T TENSOR REMARK 3 T11: 0.7951 T22: 0.5098 REMARK 3 T33: 0.4593 T12: 0.1557 REMARK 3 T13: -0.0043 T23: -0.0053 REMARK 3 L TENSOR REMARK 3 L11: 4.5710 L22: 4.3060 REMARK 3 L33: 1.8698 L12: -0.7840 REMARK 3 L13: -2.1405 L23: 1.7335 REMARK 3 S TENSOR REMARK 3 S11: -0.1287 S12: 0.7102 S13: 0.1641 REMARK 3 S21: -0.3118 S22: 0.1710 S23: 0.0672 REMARK 3 S31: -1.2650 S32: -0.1693 S33: 0.1049 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 92 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 41.3466 -14.3266 29.4790 REMARK 3 T TENSOR REMARK 3 T11: 0.7137 T22: 0.4931 REMARK 3 T33: 0.5915 T12: 0.2592 REMARK 3 T13: 0.0035 T23: -0.0437 REMARK 3 L TENSOR REMARK 3 L11: 3.0171 L22: 3.3243 REMARK 3 L33: 8.2956 L12: -1.1638 REMARK 3 L13: -0.8684 L23: 0.3023 REMARK 3 S TENSOR REMARK 3 S11: -0.0243 S12: -0.0081 S13: -0.0032 REMARK 3 S21: 0.0345 S22: -0.2767 S23: 0.1411 REMARK 3 S31: -0.2178 S32: -0.2189 S33: 0.3795 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 27 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.8532 -38.9715 13.0505 REMARK 3 T TENSOR REMARK 3 T11: 1.1099 T22: 0.9255 REMARK 3 T33: 0.2815 T12: 0.0607 REMARK 3 T13: -0.0789 T23: -0.0410 REMARK 3 L TENSOR REMARK 3 L11: 4.8016 L22: 3.2199 REMARK 3 L33: 5.3797 L12: 1.9331 REMARK 3 L13: -3.5906 L23: -0.3313 REMARK 3 S TENSOR REMARK 3 S11: -0.4170 S12: 1.4691 S13: 0.5888 REMARK 3 S21: -0.8560 S22: 0.1671 S23: -0.0995 REMARK 3 S31: 1.0242 S32: -0.8178 S33: 0.1090 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 28 THROUGH 83 ) REMARK 3 ORIGIN FOR THE GROUP (A): 51.7071 -33.0517 24.1616 REMARK 3 T TENSOR REMARK 3 T11: 0.9193 T22: 0.5659 REMARK 3 T33: 0.4553 T12: 0.3242 REMARK 3 T13: 0.0673 T23: -0.0190 REMARK 3 L TENSOR REMARK 3 L11: 2.4553 L22: 3.4661 REMARK 3 L33: 1.1231 L12: -0.7262 REMARK 3 L13: 1.5008 L23: -1.2709 REMARK 3 S TENSOR REMARK 3 S11: -0.2339 S12: -0.0404 S13: -0.0453 REMARK 3 S21: 0.1700 S22: 0.0174 S23: -0.0666 REMARK 3 S31: 0.8049 S32: 0.0340 S33: 0.3396 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 84 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 57.0297 -24.5143 22.2502 REMARK 3 T TENSOR REMARK 3 T11: 0.4423 T22: 0.4246 REMARK 3 T33: 0.5358 T12: 0.2202 REMARK 3 T13: 0.0128 T23: -0.0525 REMARK 3 L TENSOR REMARK 3 L11: 5.1560 L22: 3.4155 REMARK 3 L33: 5.9900 L12: -0.5581 REMARK 3 L13: -0.4239 L23: 1.9975 REMARK 3 S TENSOR REMARK 3 S11: 0.0663 S12: -0.1310 S13: -0.0024 REMARK 3 S21: 0.4531 S22: 0.1744 S23: -0.2363 REMARK 3 S31: 0.2439 S32: 0.6955 S33: -0.1690 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 16 THROUGH 28 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.8101 -15.2448 14.6023 REMARK 3 T TENSOR REMARK 3 T11: 1.1288 T22: 1.1618 REMARK 3 T33: 0.8215 T12: 0.3044 REMARK 3 T13: 0.0601 T23: -0.0909 REMARK 3 L TENSOR REMARK 3 L11: 4.1450 L22: 6.9092 REMARK 3 L33: 5.0481 L12: 4.9559 REMARK 3 L13: -4.0480 L23: -5.8716 REMARK 3 S TENSOR REMARK 3 S11: -0.3254 S12: 0.7815 S13: -0.3064 REMARK 3 S21: -0.9127 S22: 1.2007 S23: 0.4934 REMARK 3 S31: -1.0937 S32: -1.5862 S33: -1.2145 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 29 THROUGH 51 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.1360 -24.2619 31.7308 REMARK 3 T TENSOR REMARK 3 T11: 1.1468 T22: 1.1857 REMARK 3 T33: 0.8372 T12: 0.4538 REMARK 3 T13: 0.1805 T23: 0.0810 REMARK 3 L TENSOR REMARK 3 L11: 2.9057 L22: 3.4274 REMARK 3 L33: 4.6922 L12: -0.0232 REMARK 3 L13: 2.3754 L23: -1.3938 REMARK 3 S TENSOR REMARK 3 S11: -0.2885 S12: -0.7511 S13: -0.0880 REMARK 3 S21: 0.7818 S22: 0.9884 S23: 0.2534 REMARK 3 S31: -0.5368 S32: -1.5314 S33: -0.4401 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 52 THROUGH 82 ) REMARK 3 ORIGIN FOR THE GROUP (A): 39.5808 -23.4238 21.0060 REMARK 3 T TENSOR REMARK 3 T11: 0.5948 T22: 0.6228 REMARK 3 T33: 0.5002 T12: 0.2553 REMARK 3 T13: 0.0041 T23: 0.0158 REMARK 3 L TENSOR REMARK 3 L11: 2.3988 L22: 2.0497 REMARK 3 L33: 2.0005 L12: -0.1049 REMARK 3 L13: -0.9633 L23: 1.6754 REMARK 3 S TENSOR REMARK 3 S11: 0.1146 S12: 0.2820 S13: 0.0577 REMARK 3 S21: 0.1452 S22: -0.0731 S23: 0.3141 REMARK 3 S31: -0.3687 S32: -1.7800 S33: -0.0535 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 83 THROUGH 120 ) REMARK 3 ORIGIN FOR THE GROUP (A): 40.5818 -33.1005 20.6706 REMARK 3 T TENSOR REMARK 3 T11: 0.6972 T22: 0.5265 REMARK 3 T33: 0.6736 T12: 0.0408 REMARK 3 T13: 0.0668 T23: -0.0712 REMARK 3 L TENSOR REMARK 3 L11: 4.6521 L22: 4.7524 REMARK 3 L33: 8.9088 L12: -0.2365 REMARK 3 L13: -1.7116 L23: 1.2798 REMARK 3 S TENSOR REMARK 3 S11: -0.2561 S12: 0.3340 S13: -0.1078 REMARK 3 S21: 0.5521 S22: 0.0636 S23: 0.3845 REMARK 3 S31: 0.5730 S32: -1.3542 S33: 0.2364 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 1 REMARK 3 NCS GROUP : 1 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THERE ARE THREE NCS-RELATED MOLECULES REMARK 3 IN THE ASYMMETRIC UNIT BUT NCS GLOBAL RESTRAINTS WERE NOT USED REMARK 3 IN THE REFINEMENT. REMARK 4 REMARK 4 4UXX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-AUG-14. REMARK 100 THE DEPOSITION ID IS D_1290061583. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-DEC-12 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.6 REMARK 200 NUMBER OF CRYSTALS USED : 5 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320, 1.28238 REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL CRYO REMARK 200 -COOLED REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17218 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 REMARK 200 RESOLUTION RANGE LOW (A) : 53.070 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 9.100 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.77 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1 REMARK 200 DATA REDUNDANCY IN SHELL : 5.30 REMARK 200 R MERGE FOR SHELL (I) : 0.86000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 3ZE5 REMARK 200 REMARK 200 REMARK: FOUR CRYSTALS WERE USED FOR THE NATIVE DATA SET. A SINGLE REMARK 200 CRYSTAL WAS USED FOR THE ZN-ANOMALOUS DATA SET. REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 63.85 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 7-10 %(V/V) 2-METHYL-2, 4-PENTANEDIOL REMARK 280 (MPD), 0.1 M SODIUM CHLORIDE, 0.1 M LITHIUM NITRATE, 0.1 M REMARK 280 SODIUM CITRATE/HCL PH 5.6. CRYSTALLIZED USING THE IN MESO (LIPID REMARK 280 CUBIC PHASE) METHOD AT 4 DEGREES CELCIUS WITH THE 9.9 REMARK 280 MONOACYLGLYCEROL (MONOOLEIN, 9.9 MAG) AS THE HOSTING REMARK 280 LIPID.CRYSTALS WERE SOAKED WITH 5-10 MM AMPPCP, 60 MM ZINC REMARK 280 ACETATE BEFORE HARVESTING., LIPIDIC CUBIC PHASE, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z+2/3 REMARK 290 6555 -X,-X+Y,-Z+1/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.25333 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 130.50667 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 130.50667 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.25333 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10560 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19570 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -83.7 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 NA NA C1126 LIES ON A SPECIAL POSITION. 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 GLY A -8 REMARK 465 HIS A -7 REMARK 465 HIS A -6 REMARK 465 HIS A -5 REMARK 465 HIS A -4 REMARK 465 HIS A -3 REMARK 465 HIS A -2 REMARK 465 GLU A -1 REMARK 465 LEU A 0 REMARK 465 ALA A 1 REMARK 465 ASN A 2 REMARK 465 ASN A 3 REMARK 465 THR A 4 REMARK 465 THR A 5 REMARK 465 GLY A 6 REMARK 465 GLY B -8 REMARK 465 HIS B -7 REMARK 465 HIS B -6 REMARK 465 HIS B -5 REMARK 465 HIS B -4 REMARK 465 HIS B -3 REMARK 465 HIS B -2 REMARK 465 GLU B -1 REMARK 465 LEU B 0 REMARK 465 ALA B 1 REMARK 465 ASN B 2 REMARK 465 ASN B 3 REMARK 465 THR B 4 REMARK 465 THR B 5 REMARK 465 GLY C -8 REMARK 465 HIS C -7 REMARK 465 HIS C -6 REMARK 465 HIS C -5 REMARK 465 HIS C -4 REMARK 465 HIS C -3 REMARK 465 HIS C -2 REMARK 465 GLU C -1 REMARK 465 LEU C 0 REMARK 465 ALA C 1 REMARK 465 ASN C 2 REMARK 465 ASN C 3 REMARK 465 THR C 4 REMARK 465 THR C 5 REMARK 465 GLY C 6 REMARK 465 PHE C 7 REMARK 465 THR C 8 REMARK 465 ARG C 9 REMARK 465 ILE C 10 REMARK 465 ILE C 11 REMARK 465 LYS C 12 REMARK 465 ALA C 13 REMARK 465 ALA C 14 REMARK 465 GLY C 15 REMARK 465 GLY C 121 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLY A 121 CA C O REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1122 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 76 OE1 REMARK 620 2 ACT A1123 O 106.0 REMARK 620 3 GLU A 28 OE1 145.2 101.9 REMARK 620 4 ACT A1123 OXT 94.9 47.8 88.7 REMARK 620 5 GLU A 28 OE2 155.2 66.4 57.4 95.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA B1126 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU B 28 OE1 REMARK 620 2 ACT B1125 OXT 130.9 REMARK 620 3 ACT B1125 O 163.0 50.7 REMARK 620 4 GLU B 76 OE2 117.5 80.4 79.2 REMARK 620 5 GLU B 76 OE1 82.9 72.2 111.2 53.8 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN C1121 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ACP C1123 O1B REMARK 620 2 ACP C1123 O3G 87.9 REMARK 620 3 GLU C 28 OE2 118.2 112.4 REMARK 620 4 GLU C 76 OE1 100.4 114.7 118.8 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN C1122 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 76 OE2 REMARK 620 2 ACP C1123 O1A 120.7 REMARK 620 3 ACP C1123 O1G 80.9 130.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA C1126 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU C 88 OE1 REMARK 620 2 GLU C 88 OE1 78.8 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1121 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1122 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1121 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP C 1123 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 1122 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1122 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1123 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC C 1124 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 1123 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC B 1124 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1124 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC A 1125 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OLC C 1125 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 1125 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1126 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 1126 REMARK 800 REMARK 800 SITE_IDENTIFIER: BC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1126 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 4UXW RELATED DB: PDB REMARK 900 STRUCTURE OF DELTA4-DGKA-APO IN 9.9 MAG REMARK 900 RELATED ID: 4UXZ RELATED DB: PDB REMARK 900 STRUCTURE OF DELTA7-DGKA-SYN IN 7.9 MAG TO 2.18 ANGSTROM RESOLUTION REMARK 999 REMARK 999 SEQUENCE REMARK 999 THE PROTEIN CONTAINS AN N-TERMINAL HIS TAG 'GHHHHHHEL'. REMARK 999 COMPARED TO THE WILDTYPE FORM, THE PROTEIN HAS FOUR REMARK 999 MUTATIONS. THEY ARE I53V, I70L, M96L AND V107D. DBREF 4UXX A 1 121 UNP P0ABN1 KDGL_ECOLI 2 122 DBREF 4UXX B 1 121 UNP P0ABN1 KDGL_ECOLI 2 122 DBREF 4UXX C 1 121 UNP P0ABN1 KDGL_ECOLI 2 122 SEQADV 4UXX GLY A -8 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS A -7 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS A -6 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS A -5 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS A -4 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS A -3 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS A -2 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX GLU A -1 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX LEU A 0 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX CYS A 53 UNP P0ABN1 ILE 54 ENGINEERED MUTATION SEQADV 4UXX LEU A 70 UNP P0ABN1 ILE 71 ENGINEERED MUTATION SEQADV 4UXX LEU A 96 UNP P0ABN1 MET 97 ENGINEERED MUTATION SEQADV 4UXX ASP A 107 UNP P0ABN1 VAL 108 ENGINEERED MUTATION SEQADV 4UXX GLY B -8 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS B -7 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS B -6 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS B -5 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS B -4 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS B -3 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS B -2 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX GLU B -1 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX LEU B 0 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX CYS B 53 UNP P0ABN1 ILE 54 ENGINEERED MUTATION SEQADV 4UXX LEU B 70 UNP P0ABN1 ILE 71 ENGINEERED MUTATION SEQADV 4UXX LEU B 96 UNP P0ABN1 MET 97 ENGINEERED MUTATION SEQADV 4UXX ASP B 107 UNP P0ABN1 VAL 108 ENGINEERED MUTATION SEQADV 4UXX GLY C -8 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS C -7 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS C -6 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS C -5 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS C -4 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS C -3 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX HIS C -2 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX GLU C -1 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX LEU C 0 UNP P0ABN1 EXPRESSION TAG SEQADV 4UXX CYS C 53 UNP P0ABN1 ILE 54 ENGINEERED MUTATION SEQADV 4UXX LEU C 70 UNP P0ABN1 ILE 71 ENGINEERED MUTATION SEQADV 4UXX LEU C 96 UNP P0ABN1 MET 97 ENGINEERED MUTATION SEQADV 4UXX ASP C 107 UNP P0ABN1 VAL 108 ENGINEERED MUTATION SEQRES 1 A 130 GLY HIS HIS HIS HIS HIS HIS GLU LEU ALA ASN ASN THR SEQRES 2 A 130 THR GLY PHE THR ARG ILE ILE LYS ALA ALA GLY TYR SER SEQRES 3 A 130 TRP LYS GLY LEU ARG ALA ALA TRP ILE ASN GLU ALA ALA SEQRES 4 A 130 PHE ARG GLN GLU GLY VAL ALA VAL LEU LEU ALA VAL VAL SEQRES 5 A 130 ILE ALA CYS TRP LEU ASP VAL ASP ALA CYS THR ARG VAL SEQRES 6 A 130 LEU LEU ILE SER SER VAL MET LEU VAL MET ILE VAL GLU SEQRES 7 A 130 LEU LEU ASN SER ALA ILE GLU ALA VAL VAL ASP ARG ILE SEQRES 8 A 130 GLY SER GLU TYR HIS GLU LEU SER GLY ARG ALA LYS ASP SEQRES 9 A 130 LEU GLY SER ALA ALA VAL LEU ILE ALA ILE ILE ASP ALA SEQRES 10 A 130 VAL ILE THR TRP CYS ILE LEU LEU TRP SER HIS PHE GLY SEQRES 1 B 130 GLY HIS HIS HIS HIS HIS HIS GLU LEU ALA ASN ASN THR SEQRES 2 B 130 THR GLY PHE THR ARG ILE ILE LYS ALA ALA GLY TYR SER SEQRES 3 B 130 TRP LYS GLY LEU ARG ALA ALA TRP ILE ASN GLU ALA ALA SEQRES 4 B 130 PHE ARG GLN GLU GLY VAL ALA VAL LEU LEU ALA VAL VAL SEQRES 5 B 130 ILE ALA CYS TRP LEU ASP VAL ASP ALA CYS THR ARG VAL SEQRES 6 B 130 LEU LEU ILE SER SER VAL MET LEU VAL MET ILE VAL GLU SEQRES 7 B 130 LEU LEU ASN SER ALA ILE GLU ALA VAL VAL ASP ARG ILE SEQRES 8 B 130 GLY SER GLU TYR HIS GLU LEU SER GLY ARG ALA LYS ASP SEQRES 9 B 130 LEU GLY SER ALA ALA VAL LEU ILE ALA ILE ILE ASP ALA SEQRES 10 B 130 VAL ILE THR TRP CYS ILE LEU LEU TRP SER HIS PHE GLY SEQRES 1 C 130 GLY HIS HIS HIS HIS HIS HIS GLU LEU ALA ASN ASN THR SEQRES 2 C 130 THR GLY PHE THR ARG ILE ILE LYS ALA ALA GLY TYR SER SEQRES 3 C 130 TRP LYS GLY LEU ARG ALA ALA TRP ILE ASN GLU ALA ALA SEQRES 4 C 130 PHE ARG GLN GLU GLY VAL ALA VAL LEU LEU ALA VAL VAL SEQRES 5 C 130 ILE ALA CYS TRP LEU ASP VAL ASP ALA CYS THR ARG VAL SEQRES 6 C 130 LEU LEU ILE SER SER VAL MET LEU VAL MET ILE VAL GLU SEQRES 7 C 130 LEU LEU ASN SER ALA ILE GLU ALA VAL VAL ASP ARG ILE SEQRES 8 C 130 GLY SER GLU TYR HIS GLU LEU SER GLY ARG ALA LYS ASP SEQRES 9 C 130 LEU GLY SER ALA ALA VAL LEU ILE ALA ILE ILE ASP ALA SEQRES 10 C 130 VAL ILE THR TRP CYS ILE LEU LEU TRP SER HIS PHE GLY HET CL A1121 1 HET NA A1122 1 HET ACT A1123 4 HET OLC A1124 25 HET OLC A1125 25 HET ACT A1126 4 HET MPD B1122 8 HET OLC B1123 25 HET OLC B1124 25 HET ACT B1125 4 HET NA B1126 1 HET ZN C1121 1 HET ZN C1122 1 HET ACP C1123 31 HET OLC C1124 25 HET OLC C1125 25 HET NA C1126 1 HETNAM CL CHLORIDE ION HETNAM NA SODIUM ION HETNAM ACT ACETATE ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL HETNAM ZN ZINC ION HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE FORMUL 4 CL CL 1- FORMUL 5 NA 3(NA 1+) FORMUL 6 ACT 3(C2 H3 O2 1-) FORMUL 7 OLC 6(C21 H40 O4) FORMUL 10 MPD C6 H14 O2 FORMUL 15 ZN 2(ZN 2+) FORMUL 17 ACP C11 H18 N5 O12 P3 FORMUL 21 HOH *13(H2 O) HELIX 1 1 PHE A 7 ASN A 27 1 21 HELIX 2 2 GLU A 28 LEU A 48 1 21 HELIX 3 3 ASP A 51 HIS A 87 1 37 HELIX 4 4 GLY A 91 PHE A 120 1 30 HELIX 5 5 PHE B 7 ASN B 27 1 21 HELIX 6 6 GLU B 28 LEU B 48 1 21 HELIX 7 7 ASP B 51 TYR B 86 1 36 HELIX 8 8 GLY B 91 PHE B 120 1 30 HELIX 9 9 TYR C 16 ASN C 27 1 12 HELIX 10 10 GLU C 28 LEU C 48 1 21 HELIX 11 11 ASP C 51 GLY C 83 1 33 HELIX 12 12 LEU C 89 PHE C 120 1 32 LINK NA NA C1126 OE1 GLU C 88 1555 4645 2.43 LINK ZN ZN C1121 O1B ADP C1123 1555 1555 2.14 LINK ZN ZN C1121 OE1 GLU C 76 1555 1555 1.99 LINK ZN ZN C1121 O3G ADP C1123 1555 1555 2.11 LINK ZN ZN C1122 OE2 GLU C 76 1555 1555 1.97 LINK ZN ZN C1122 O1A ADP C1123 1555 1555 2.09 LINK ZN ZN C1122 O1G ADP C1123 1555 1555 2.22 LINK ZN ZN C1121 OE2 GLU C 28 1555 1555 2.09 SITE 1 AC1 3 GLU C 28 GLU C 76 ACP C1123 SITE 1 AC2 2 GLU C 76 ACP C1123 SITE 1 AC3 3 ASN A 27 ALA A 29 ARG A 32 SITE 1 AC4 17 ARG B 9 TYR B 16 HOH B2001 GLU C 28 SITE 2 AC4 17 ASN C 72 GLU C 76 GLU C 85 TYR C 86 SITE 3 AC4 17 HIS C 87 SER C 90 GLY C 91 LYS C 94 SITE 4 AC4 17 ASP C 95 ZN C1121 ZN C1122 OLC C1125 SITE 5 AC4 17 HOH C2004 SITE 1 AC5 5 ARG A 81 GLU B 88 LEU B 89 SER B 90 SITE 2 AC5 5 ARG B 92 SITE 1 AC6 3 GLU A 28 GLU A 76 ACT A1123 SITE 1 AC7 3 GLU A 28 GLU A 76 NA A1122 SITE 1 AC8 7 ARG B 9 ILE B 10 ALA C 30 GLN C 33 SITE 2 AC8 7 GLU C 34 CYS C 113 OLC C1125 SITE 1 AC9 10 SER A 17 CYS A 113 TRP A 117 GLU B 34 SITE 2 AC9 10 ALA B 37 ILE B 44 GLU B 69 ASN B 72 SITE 3 AC9 10 LEU B 102 OLC B1124 SITE 1 BC1 7 ILE A 10 TRP A 117 GLN B 33 GLU B 34 SITE 2 BC1 7 TRP B 112 TRP B 117 OLC B1123 SITE 1 BC2 3 TRP A 18 TRP A 25 ILE A 26 SITE 1 BC3 12 GLN A 33 GLU A 34 ALA A 37 ILE A 44 SITE 2 BC3 12 VAL A 62 ALA A 108 VAL A 109 TRP A 112 SITE 3 BC3 12 LEU A 116 LEU B 39 LEU B 40 TRP B 47 SITE 1 BC4 10 ALA B 13 SER B 17 GLU C 69 ASN C 72 SITE 2 BC4 10 SER C 98 LEU C 102 ILE C 106 VAL C 109 SITE 3 BC4 10 ACP C1123 OLC C1124 SITE 1 BC5 8 GLU B 76 GLY B 83 SER B 84 GLU B 85 SITE 2 BC5 8 TYR B 86 HIS B 87 LYS B 94 NA B1126 SITE 1 BC6 3 GLU B 28 GLU B 76 ACT B1125 SITE 1 BC7 1 GLU C 88 SITE 1 BC8 1 HIS A 119 CRYST1 72.940 72.940 195.760 90.00 90.00 120.00 P 31 2 1 18 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 0.013710 0.007915 0.000000 0.00000 SCALE2 0.000000 0.015831 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005108 0.00000 ATOM 1 N PHE A 7 70.822 -34.884 18.150 1.00140.53 N ANISOU 1 N PHE A 7 18996 17298 17103 4851 96 -3022 N ATOM 2 CA PHE A 7 70.774 -33.532 18.696 1.00137.27 C ANISOU 2 CA PHE A 7 18317 17221 16617 4720 -171 -2948 C ATOM 3 C PHE A 7 70.898 -32.471 17.608 1.00126.11 C ANISOU 3 C PHE A 7 16811 15991 15115 4356 -83 -3109 C ATOM 4 O PHE A 7 70.610 -31.297 17.843 1.00120.54 O ANISOU 4 O PHE A 7 15971 15496 14334 4156 -244 -3052 O ATOM 5 CB PHE A 7 71.874 -33.337 19.744 1.00145.29 C ANISOU 5 CB PHE A 7 18946 18487 17771 5109 -325 -2905 C ATOM 6 CG PHE A 7 71.765 -34.268 20.920 1.00147.16 C ANISOU 6 CG PHE A 7 19296 18582 18037 5520 -440 -2691 C ATOM 7 CD1 PHE A 7 70.987 -33.928 22.015 1.00146.15 C ANISOU 7 CD1 PHE A 7 19248 18497 17783 5518 -690 -2480 C ATOM 8 CD2 PHE A 7 72.441 -35.477 20.934 1.00142.98 C ANISOU 8 CD2 PHE A 7 18817 17854 17654 5927 -265 -2685 C ATOM 9 CE1 PHE A 7 70.882 -34.777 23.101 1.00146.91 C ANISOU 9 CE1 PHE A 7 19502 18450 17868 5910 -762 -2257 C ATOM 10 CE2 PHE A 7 72.339 -36.332 22.018 1.00142.19 C ANISOU 10 CE2 PHE A 7 18862 17605 17560 6293 -341 -2425 C ATOM 11 CZ PHE A 7 71.559 -35.980 23.102 1.00146.62 C ANISOU 11 CZ PHE A 7 19531 18217 17960 6297 -589 -2212 C ATOM 12 N THR A 8 71.338 -32.883 16.423 1.00116.74 N ANISOU 12 N THR A 8 15720 14705 13933 4282 206 -3304 N ATOM 13 CA THR A 8 71.537 -31.949 15.320 1.00119.20 C ANISOU 13 CA THR A 8 15998 15163 14130 3972 349 -3445 C ATOM 14 C THR A 8 70.243 -31.262 14.883 1.00123.85 C ANISOU 14 C THR A 8 16833 15767 14457 3599 218 -3350 C ATOM 15 O THR A 8 70.239 -30.065 14.595 1.00128.34 O ANISOU 15 O THR A 8 17301 16525 14937 3397 198 -3328 O ATOM 16 CB THR A 8 72.157 -32.650 14.095 1.00120.84 C ANISOU 16 CB THR A 8 16341 15227 14347 3961 716 -3675 C ATOM 17 OG1 THR A 8 71.399 -33.826 13.780 1.00123.04 O ANISOU 17 OG1 THR A 8 16995 15205 14549 3941 787 -3698 O ATOM 18 CG2 THR A 8 73.597 -33.045 14.378 1.00128.41 C ANISOU 18 CG2 THR A 8 16961 16229 15601 4317 879 -3793 C ATOM 19 N ARG A 9 69.149 -32.016 14.829 1.00111.49 N ANISOU 19 N ARG A 9 15579 13995 12788 3515 147 -3299 N ATOM 20 CA ARG A 9 67.866 -31.446 14.429 1.00104.74 C ANISOU 20 CA ARG A 9 14917 13174 11704 3191 -11 -3220 C ATOM 21 C ARG A 9 67.308 -30.500 15.494 1.00108.97 C ANISOU 21 C ARG A 9 15287 13845 12269 3168 -287 -2998 C ATOM 22 O ARG A 9 66.653 -29.509 15.168 1.00116.17 O ANISOU 22 O ARG A 9 16220 14884 13034 2937 -391 -2917 O ATOM 23 CB ARG A 9 66.855 -32.554 14.122 1.00117.30 C ANISOU 23 CB ARG A 9 16830 14516 13223 3087 -5 -3282 C ATOM 24 CG ARG A 9 65.517 -32.040 13.608 1.00134.08 C ANISOU 24 CG ARG A 9 19113 16714 15117 2760 -191 -3243 C ATOM 25 CD ARG A 9 64.617 -33.172 13.141 1.00154.58 C ANISOU 25 CD ARG A 9 21989 19089 17655 2612 -153 -3400 C ATOM 26 NE ARG A 9 63.385 -32.669 12.540 1.00167.17 N ANISOU 26 NE ARG A 9 23682 20815 19018 2307 -361 -3401 N ATOM 27 CZ ARG A 9 62.494 -33.429 11.911 1.00172.13 C ANISOU 27 CZ ARG A 9 24517 21345 19540 2094 -374 -3594 C ATOM 28 NH1 ARG A 9 62.697 -34.734 11.792 1.00170.41 N ANISOU 28 NH1 ARG A 9 24464 20847 19437 2130 -142 -3806 N ATOM 29 NH2 ARG A 9 61.400 -32.883 11.396 1.00174.82 N ANISOU 29 NH2 ARG A 9 24887 21868 19669 1851 -614 -3589 N ATOM 30 N ILE A 10 67.563 -30.815 16.763 1.00100.00 N ANISOU 30 N ILE A 10 14008 12679 11310 3428 -394 -2894 N ATOM 31 CA ILE A 10 67.106 -29.981 17.874 1.00100.78 C ANISOU 31 CA ILE A 10 13961 12899 11432 3423 -631 -2707 C ATOM 32 C ILE A 10 67.650 -28.561 17.776 1.00 95.99 C ANISOU 32 C ILE A 10 13096 12556 10820 3308 -640 -2721 C ATOM 33 O ILE A 10 66.927 -27.592 18.014 1.00 79.57 O ANISOU 33 O ILE A 10 11000 10555 8679 3126 -765 -2600 O ATOM 34 CB ILE A 10 67.508 -30.587 19.238 1.00110.10 C ANISOU 34 CB ILE A 10 15041 14037 12754 3771 -727 -2609 C ATOM 35 CG1 ILE A 10 66.748 -31.890 19.479 1.00114.90 C ANISOU 35 CG1 ILE A 10 15956 14321 13380 3858 -684 -2545 C ATOM 36 CG2 ILE A 10 67.183 -29.630 20.373 1.00103.58 C ANISOU 36 CG2 ILE A 10 14057 13375 11923 3756 -951 -2457 C ATOM 37 CD1 ILE A 10 65.244 -31.701 19.566 1.00110.97 C ANISOU 37 CD1 ILE A 10 15650 13713 12801 3581 -792 -2442 C ATOM 38 N ILE A 11 68.920 -28.441 17.401 1.00 97.11 N ANISOU 38 N ILE A 11 13033 12810 11053 3406 -466 -2883 N ATOM 39 CA ILE A 11 69.525 -27.133 17.191 1.00103.33 C ANISOU 39 CA ILE A 11 13579 13809 11872 3265 -387 -2943 C ATOM 40 C ILE A 11 68.876 -26.438 16.001 1.00 97.81 C ANISOU 40 C ILE A 11 13105 13088 10970 2958 -272 -2911 C ATOM 41 O ILE A 11 68.683 -25.222 16.000 1.00100.57 O ANISOU 41 O ILE A 11 13381 13538 11291 2788 -269 -2836 O ATOM 42 CB ILE A 11 71.044 -27.249 16.955 1.00107.19 C ANISOU 42 CB ILE A 11 13782 14404 12541 3422 -177 -3163 C ATOM 43 CG1 ILE A 11 71.688 -28.115 18.039 1.00101.49 C ANISOU 43 CG1 ILE A 11 12856 13715 11990 3799 -315 -3179 C ATOM 44 CG2 ILE A 11 71.689 -25.871 16.905 1.00107.13 C ANISOU 44 CG2 ILE A 11 13487 14597 12621 3256 -64 -3254 C ATOM 45 CD1 ILE A 11 71.623 -27.508 19.422 1.00 88.86 C ANISOU 45 CD1 ILE A 11 11027 12300 10436 3884 -592 -3087 C ATOM 46 N LYS A 12 68.534 -27.227 14.989 1.00 99.80 N ANISOU 46 N LYS A 12 13647 13207 11067 2902 -171 -2968 N ATOM 47 CA LYS A 12 67.885 -26.710 13.792 1.00 92.82 C ANISOU 47 CA LYS A 12 13016 12332 9919 2652 -99 -2937 C ATOM 48 C LYS A 12 66.433 -26.311 14.069 1.00 87.93 C ANISOU 48 C LYS A 12 12526 11707 9175 2514 -368 -2732 C ATOM 49 O LYS A 12 65.950 -25.312 13.538 1.00 83.93 O ANISOU 49 O LYS A 12 12094 11284 8513 2353 -373 -2617 O ATOM 50 CB LYS A 12 67.999 -27.731 12.657 1.00 96.80 C ANISOU 50 CB LYS A 12 13784 12724 10272 2632 78 -3109 C ATOM 51 CG LYS A 12 67.809 -27.145 11.268 1.00104.13 C ANISOU 51 CG LYS A 12 14953 13721 10890 2422 231 -3129 C ATOM 52 CD LYS A 12 67.579 -28.234 10.239 1.00112.16 C ANISOU 52 CD LYS A 12 16284 14637 11696 2365 328 -3307 C ATOM 53 CE LYS A 12 68.857 -29.052 10.092 1.00127.74 C ANISOU 53 CE LYS A 12 18175 16504 13857 2528 636 -3533 C ATOM 54 NZ LYS A 12 68.756 -30.191 9.143 1.00140.27 N ANISOU 54 NZ LYS A 12 20066 17951 15278 2477 795 -3750 N ATOM 55 N ALA A 13 65.742 -27.088 14.899 1.00 85.05 N ANISOU 55 N ALA A 13 12191 11230 8894 2592 -564 -2677 N ATOM 56 CA ALA A 13 64.359 -26.777 15.253 1.00 74.34 C ANISOU 56 CA ALA A 13 10913 9855 7479 2466 -799 -2506 C ATOM 57 C ALA A 13 64.300 -25.566 16.182 1.00 76.85 C ANISOU 57 C ALA A 13 11016 10274 7909 2460 -887 -2342 C ATOM 58 O ALA A 13 63.356 -24.776 16.128 1.00 73.37 O ANISOU 58 O ALA A 13 10610 9868 7399 2323 -999 -2189 O ATOM 59 CB ALA A 13 63.690 -27.978 15.906 1.00 63.48 C ANISOU 59 CB ALA A 13 9635 8289 6194 2537 -908 -2514 C ATOM 60 N ALA A 14 65.314 -25.428 17.031 1.00 68.73 N ANISOU 60 N ALA A 14 9754 9301 7059 2616 -836 -2391 N ATOM 61 CA ALA A 14 65.403 -24.298 17.952 1.00 59.94 C ANISOU 61 CA ALA A 14 8423 8295 6058 2595 -893 -2302 C ATOM 62 C ALA A 14 65.660 -22.994 17.205 1.00 66.83 C ANISOU 62 C ALA A 14 9250 9262 6881 2423 -721 -2287 C ATOM 63 O ALA A 14 65.057 -21.965 17.513 1.00 71.41 O ANISOU 63 O ALA A 14 9800 9857 7474 2309 -761 -2145 O ATOM 64 CB ALA A 14 66.492 -24.538 18.983 1.00 72.80 C ANISOU 64 CB ALA A 14 9794 10009 7858 2809 -905 -2408 C ATOM 65 N GLY A 15 66.562 -23.045 16.228 1.00 77.71 N ANISOU 65 N GLY A 15 10640 10672 8212 2412 -489 -2430 N ATOM 66 CA GLY A 15 66.876 -21.886 15.410 1.00 75.07 C ANISOU 66 CA GLY A 15 10320 10385 7817 2258 -249 -2411 C ATOM 67 C GLY A 15 65.654 -21.399 14.659 1.00 73.57 C ANISOU 67 C GLY A 15 10405 10157 7390 2129 -318 -2196 C ATOM 68 O GLY A 15 65.448 -20.195 14.502 1.00 65.20 O ANISOU 68 O GLY A 15 9352 9106 6316 2028 -211 -2059 O ATOM 69 N TYR A 16 64.848 -22.347 14.193 1.00 63.74 N ANISOU 69 N TYR A 16 9379 8871 5970 2140 -490 -2178 N ATOM 70 CA TYR A 16 63.570 -22.052 13.555 1.00 62.80 C ANISOU 70 CA TYR A 16 9474 8764 5622 2045 -645 -1998 C ATOM 71 C TYR A 16 62.713 -21.259 14.533 1.00 75.68 C ANISOU 71 C TYR A 16 10977 10379 7400 2023 -810 -1799 C ATOM 72 O TYR A 16 62.288 -20.141 14.237 1.00 70.51 O ANISOU 72 O TYR A 16 10359 9746 6683 1965 -764 -1614 O ATOM 73 CB TYR A 16 62.877 -23.340 13.106 1.00 63.56 C ANISOU 73 CB TYR A 16 9752 8828 5571 2040 -823 -2093 C ATOM 74 CG TYR A 16 63.468 -23.929 11.840 1.00 66.34 C ANISOU 74 CG TYR A 16 10313 9203 5689 2019 -644 -2269 C ATOM 75 CD1 TYR A 16 64.106 -23.120 10.909 1.00 68.14 C ANISOU 75 CD1 TYR A 16 10644 9500 5745 1982 -390 -2243 C ATOM 76 CD2 TYR A 16 63.402 -25.294 11.583 1.00 67.49 C ANISOU 76 CD2 TYR A 16 10576 9274 5795 2030 -679 -2469 C ATOM 77 CE1 TYR A 16 64.650 -23.648 9.752 1.00 70.96 C ANISOU 77 CE1 TYR A 16 11222 9873 5869 1958 -191 -2410 C ATOM 78 CE2 TYR A 16 63.944 -25.832 10.427 1.00 70.30 C ANISOU 78 CE2 TYR A 16 11139 9639 5933 1999 -485 -2655 C ATOM 79 CZ TYR A 16 64.567 -25.004 9.516 1.00 77.79 C ANISOU 79 CZ TYR A 16 12191 10678 6687 1964 -248 -2625 C ATOM 80 OH TYR A 16 65.109 -25.534 8.365 1.00 87.06 O ANISOU 80 OH TYR A 16 13598 11855 7624 1929 -23 -2816 O ATOM 81 N SER A 17 62.442 -21.870 15.683 1.00 67.41 N ANISOU 81 N SER A 17 9803 9271 6538 2083 -976 -1828 N ATOM 82 CA SER A 17 61.638 -21.257 16.736 1.00 73.22 C ANISOU 82 CA SER A 17 10424 9970 7426 2063 -1110 -1670 C ATOM 83 C SER A 17 62.140 -19.856 17.082 1.00 73.10 C ANISOU 83 C SER A 17 10263 9987 7526 2018 -933 -1602 C ATOM 84 O SER A 17 61.352 -18.916 17.183 1.00 75.52 O ANISOU 84 O SER A 17 10575 10265 7855 1956 -950 -1415 O ATOM 85 CB SER A 17 61.640 -22.136 17.985 1.00 55.80 C ANISOU 85 CB SER A 17 8125 7691 5387 2163 -1230 -1737 C ATOM 86 OG SER A 17 61.325 -23.478 17.659 1.00 76.72 O ANISOU 86 OG SER A 17 10922 10261 7969 2200 -1312 -1828 O ATOM 87 N TRP A 18 63.451 -19.724 17.267 1.00 63.39 N ANISOU 87 N TRP A 18 8883 8806 6394 2047 -745 -1773 N ATOM 88 CA TRP A 18 64.055 -18.426 17.560 1.00 72.27 C ANISOU 88 CA TRP A 18 9848 9952 7660 1964 -525 -1782 C ATOM 89 C TRP A 18 63.870 -17.433 16.420 1.00 70.21 C ANISOU 89 C TRP A 18 9755 9651 7269 1868 -304 -1633 C ATOM 90 O TRP A 18 63.648 -16.244 16.653 1.00 67.47 O ANISOU 90 O TRP A 18 9372 9244 7020 1788 -164 -1512 O ATOM 91 CB TRP A 18 65.546 -18.581 17.860 1.00 78.07 C ANISOU 91 CB TRP A 18 10348 10778 8538 2005 -369 -2050 C ATOM 92 CG TRP A 18 66.263 -17.268 17.995 1.00 80.54 C ANISOU 92 CG TRP A 18 10480 11107 9014 1870 -84 -2130 C ATOM 93 CD1 TRP A 18 67.193 -16.753 17.139 1.00 96.56 C ANISOU 93 CD1 TRP A 18 12486 13134 11070 1784 260 -2244 C ATOM 94 CD2 TRP A 18 66.096 -16.296 19.036 1.00 85.16 C ANISOU 94 CD2 TRP A 18 10898 11686 9774 1779 -70 -2126 C ATOM 95 NE1 TRP A 18 67.623 -15.528 17.587 1.00 97.67 N ANISOU 95 NE1 TRP A 18 12440 13256 11415 1636 498 -2321 N ATOM 96 CE2 TRP A 18 66.965 -15.224 18.749 1.00 93.15 C ANISOU 96 CE2 TRP A 18 11776 12686 10931 1627 293 -2260 C ATOM 97 CE3 TRP A 18 65.301 -16.230 20.185 1.00 94.38 C ANISOU 97 CE3 TRP A 18 12027 12840 10994 1797 -293 -2041 C ATOM 98 CZ2 TRP A 18 67.062 -14.101 19.568 1.00 97.19 C ANISOU 98 CZ2 TRP A 18 12110 13173 11645 1480 431 -2332 C ATOM 99 CZ3 TRP A 18 65.399 -15.113 20.997 1.00101.10 C ANISOU 99 CZ3 TRP A 18 12715 13681 12018 1666 -167 -2101 C ATOM 100 CH2 TRP A 18 66.273 -14.065 20.684 1.00 99.43 C ANISOU 100 CH2 TRP A 18 12364 13459 11955 1504 187 -2256 C ATOM 101 N LYS A 19 63.964 -17.921 15.189 1.00 64.06 N ANISOU 101 N LYS A 19 9189 8894 6257 1886 -250 -1636 N ATOM 102 CA LYS A 19 63.751 -17.069 14.030 1.00 76.53 C ANISOU 102 CA LYS A 19 10996 10447 7635 1837 -51 -1460 C ATOM 103 C LYS A 19 62.300 -16.608 13.997 1.00 81.50 C ANISOU 103 C LYS A 19 11744 11056 8168 1855 -268 -1171 C ATOM 104 O LYS A 19 62.008 -15.463 13.652 1.00 82.21 O ANISOU 104 O LYS A 19 11925 11085 8225 1842 -102 -956 O ATOM 105 CB LYS A 19 64.118 -17.804 12.740 1.00 65.21 C ANISOU 105 CB LYS A 19 9795 9066 5917 1861 27 -1545 C ATOM 106 CG LYS A 19 64.215 -16.902 11.522 1.00 71.76 C ANISOU 106 CG LYS A 19 10888 9873 6504 1831 315 -1383 C ATOM 107 CD LYS A 19 64.685 -17.675 10.298 1.00 81.78 C ANISOU 107 CD LYS A 19 12401 11200 7472 1844 424 -1510 C ATOM 108 CE LYS A 19 64.563 -16.838 9.034 1.00 83.42 C ANISOU 108 CE LYS A 19 12955 11401 7339 1847 666 -1294 C ATOM 109 NZ LYS A 19 64.288 -17.667 7.827 1.00101.04 N ANISOU 109 NZ LYS A 19 15509 13749 9131 1880 562 -1334 N ATOM 110 N GLY A 20 61.392 -17.510 14.357 1.00 63.00 N ANISOU 110 N GLY A 20 9390 8747 5800 1895 -614 -1168 N ATOM 111 CA GLY A 20 59.979 -17.184 14.422 1.00 62.78 C ANISOU 111 CA GLY A 20 9402 8716 5737 1913 -846 -935 C ATOM 112 C GLY A 20 59.666 -16.214 15.542 1.00 72.67 C ANISOU 112 C GLY A 20 10476 9863 7271 1890 -789 -817 C ATOM 113 O GLY A 20 58.838 -15.313 15.386 1.00 72.88 O ANISOU 113 O GLY A 20 10545 9849 7299 1914 -789 -570 O ATOM 114 N LEU A 21 60.319 -16.398 16.684 1.00 66.81 N ANISOU 114 N LEU A 21 9538 9084 6762 1859 -742 -994 N ATOM 115 CA LEU A 21 60.127 -15.501 17.820 1.00 78.08 C ANISOU 115 CA LEU A 21 10803 10421 8441 1813 -666 -940 C ATOM 116 C LEU A 21 60.627 -14.095 17.525 1.00 75.59 C ANISOU 116 C LEU A 21 10495 10027 8198 1747 -312 -862 C ATOM 117 O LEU A 21 59.954 -13.111 17.828 1.00 76.65 O ANISOU 117 O LEU A 21 10624 10049 8451 1728 -228 -676 O ATOM 118 CB LEU A 21 60.838 -16.039 19.058 1.00 79.84 C ANISOU 118 CB LEU A 21 10834 10673 8830 1810 -707 -1174 C ATOM 119 CG LEU A 21 60.195 -17.224 19.775 1.00 77.98 C ANISOU 119 CG LEU A 21 10596 10434 8600 1880 -993 -1204 C ATOM 120 CD1 LEU A 21 61.119 -17.782 20.849 1.00 74.65 C ANISOU 120 CD1 LEU A 21 10026 10068 8271 1939 -1016 -1416 C ATOM 121 CD2 LEU A 21 58.864 -16.815 20.378 1.00 67.32 C ANISOU 121 CD2 LEU A 21 9241 8985 7354 1852 -1097 -1017 C ATOM 122 N ARG A 22 61.813 -14.003 16.937 1.00 70.21 N ANISOU 122 N ARG A 22 9827 9377 7473 1708 -63 -1012 N ATOM 123 CA ARG A 22 62.377 -12.713 16.569 1.00 65.56 C ANISOU 123 CA ARG A 22 9268 8676 6967 1623 350 -963 C ATOM 124 C ARG A 22 61.495 -12.039 15.516 1.00 74.91 C ANISOU 124 C ARG A 22 10730 9779 7953 1702 416 -610 C ATOM 125 O ARG A 22 61.257 -10.838 15.582 1.00 73.90 O ANISOU 125 O ARG A 22 10642 9491 7946 1678 672 -433 O ATOM 126 CB ARG A 22 63.809 -12.876 16.058 1.00 68.77 C ANISOU 126 CB ARG A 22 9628 9131 7372 1561 623 -1215 C ATOM 127 CG ARG A 22 64.513 -11.570 15.705 1.00 94.88 C ANISOU 127 CG ARG A 22 12953 12288 10810 1435 1129 -1216 C ATOM 128 CD ARG A 22 65.946 -11.814 15.232 1.00120.95 C ANISOU 128 CD ARG A 22 16161 15641 14153 1358 1414 -1508 C ATOM 129 NE ARG A 22 66.619 -10.565 14.881 1.00141.29 N ANISOU 129 NE ARG A 22 18757 18039 16888 1206 1960 -1533 N ATOM 130 CZ ARG A 22 67.916 -10.466 14.608 1.00153.28 C ANISOU 130 CZ ARG A 22 20130 19559 18551 1083 2319 -1822 C ATOM 131 NH1 ARG A 22 68.686 -11.543 14.659 1.00156.43 N ANISOU 131 NH1 ARG A 22 20338 20145 18952 1126 2160 -2097 N ATOM 132 NH2 ARG A 22 68.446 -9.290 14.299 1.00156.83 N ANISOU 132 NH2 ARG A 22 20613 19803 19172 919 2866 -1843 N ATOM 133 N ALA A 23 61.004 -12.814 14.553 1.00 87.36 N ANISOU 133 N ALA A 23 12503 11473 9217 1808 185 -511 N ATOM 134 CA ALA A 23 60.129 -12.283 13.505 1.00 85.41 C ANISOU 134 CA ALA A 23 12519 11221 8712 1929 165 -174 C ATOM 135 C ALA A 23 58.835 -11.707 14.085 1.00 80.42 C ANISOU 135 C ALA A 23 11814 10522 8218 2001 -11 77 C ATOM 136 O ALA A 23 58.384 -10.632 13.686 1.00 76.19 O ANISOU 136 O ALA A 23 11411 9877 7662 2091 163 374 O ATOM 137 CB ALA A 23 59.804 -13.366 12.485 1.00 82.31 C ANISOU 137 CB ALA A 23 12309 11021 7946 2008 -122 -191 C ATOM 138 N ALA A 24 58.243 -12.432 15.030 1.00 76.72 N ANISOU 138 N ALA A 24 11147 10102 7902 1975 -326 -34 N ATOM 139 CA ALA A 24 57.015 -11.998 15.691 1.00 74.77 C ANISOU 139 CA ALA A 24 10791 9784 7833 2026 -480 158 C ATOM 140 C ALA A 24 57.212 -10.697 16.463 1.00 81.25 C ANISOU 140 C ALA A 24 11531 10386 8955 1968 -127 232 C ATOM 141 O ALA A 24 56.330 -9.838 16.489 1.00 67.13 O ANISOU 141 O ALA A 24 9761 8483 7262 2058 -79 503 O ATOM 142 CB ALA A 24 56.504 -13.087 16.622 1.00 68.53 C ANISOU 142 CB ALA A 24 9822 9052 7165 1980 -801 -19 C ATOM 143 N TRP A 25 58.372 -10.563 17.096 1.00 90.77 N ANISOU 143 N TRP A 25 12631 11537 10321 1818 121 -32 N ATOM 144 CA TRP A 25 58.674 -9.395 17.914 1.00 81.30 C ANISOU 144 CA TRP A 25 11330 10139 9420 1707 472 -59 C ATOM 145 C TRP A 25 58.734 -8.121 17.066 1.00 84.03 C ANISOU 145 C TRP A 25 11874 10297 9755 1752 876 199 C ATOM 146 O TRP A 25 58.135 -7.107 17.422 1.00 93.08 O ANISOU 146 O TRP A 25 13026 11242 11098 1774 1066 390 O ATOM 147 CB TRP A 25 59.991 -9.597 18.665 1.00 82.01 C ANISOU 147 CB TRP A 25 11234 10277 9651 1534 614 -450 C ATOM 148 CG TRP A 25 60.333 -8.479 19.601 1.00 93.65 C ANISOU 148 CG TRP A 25 12571 11582 11430 1374 949 -568 C ATOM 149 CD1 TRP A 25 61.132 -7.405 19.345 1.00102.19 C ANISOU 149 CD1 TRP A 25 13669 12506 12653 1244 1426 -635 C ATOM 150 CD2 TRP A 25 59.893 -8.337 20.958 1.00 95.53 C ANISOU 150 CD2 TRP A 25 12644 11782 11869 1304 864 -667 C ATOM 151 NE1 TRP A 25 61.212 -6.598 20.455 1.00 98.57 N ANISOU 151 NE1 TRP A 25 13050 11920 12482 1082 1632 -794 N ATOM 152 CE2 TRP A 25 60.460 -7.149 21.459 1.00 92.54 C ANISOU 152 CE2 TRP A 25 12183 11239 11739 1123 1283 -812 C ATOM 153 CE3 TRP A 25 59.071 -9.098 21.795 1.00 98.49 C ANISOU 153 CE3 TRP A 25 12953 12232 12238 1365 509 -659 C ATOM 154 CZ2 TRP A 25 60.232 -6.704 22.759 1.00 88.20 C ANISOU 154 CZ2 TRP A 25 11491 10621 11399 1003 1330 -961 C ATOM 155 CZ3 TRP A 25 58.847 -8.655 23.086 1.00 93.54 C ANISOU 155 CZ3 TRP A 25 12202 11526 11812 1262 572 -775 C ATOM 156 CH2 TRP A 25 59.424 -7.469 23.555 1.00 92.43 C ANISOU 156 CH2 TRP A 25 11987 11248 11886 1084 966 -930 C ATOM 157 N ILE A 26 59.454 -8.175 15.948 1.00 89.06 N ANISOU 157 N ILE A 26 12698 10975 10165 1776 1042 213 N ATOM 158 CA ILE A 26 59.621 -7.004 15.086 1.00 93.44 C ANISOU 158 CA ILE A 26 13501 11326 10677 1830 1487 471 C ATOM 159 C ILE A 26 58.338 -6.586 14.360 1.00 88.28 C ANISOU 159 C ILE A 26 13062 10646 9834 2096 1346 936 C ATOM 160 O ILE A 26 58.017 -5.397 14.303 1.00109.45 O ANISOU 160 O ILE A 26 15856 13078 12650 2171 1678 1205 O ATOM 161 CB ILE A 26 60.733 -7.237 14.033 1.00 96.06 C ANISOU 161 CB ILE A 26 14010 11708 10782 1792 1729 365 C ATOM 162 CG1 ILE A 26 62.108 -6.991 14.653 1.00104.15 C ANISOU 162 CG1 ILE A 26 14820 12652 12100 1532 2102 -35 C ATOM 163 CG2 ILE A 26 60.593 -6.272 12.871 1.00103.47 C ANISOU 163 CG2 ILE A 26 15316 12472 11525 1937 2092 741 C ATOM 164 CD1 ILE A 26 62.763 -8.211 15.233 1.00108.02 C ANISOU 164 CD1 ILE A 26 15043 13383 12615 1442 1797 -426 C ATOM 165 N ASN A 27 57.587 -7.548 13.834 1.00 77.48 N ANISOU 165 N ASN A 27 11732 9532 8173 2243 857 1020 N ATOM 166 CA ASN A 27 56.433 -7.213 13.001 1.00 88.46 C ANISOU 166 CA ASN A 27 13305 10976 9332 2519 669 1437 C ATOM 167 C ASN A 27 55.147 -6.947 13.778 1.00 97.53 C ANISOU 167 C ASN A 27 14248 12080 10728 2617 436 1602 C ATOM 168 O ASN A 27 54.403 -6.020 13.450 1.00113.18 O ANISOU 168 O ASN A 27 16333 13945 12726 2833 534 1977 O ATOM 169 CB ASN A 27 56.177 -8.323 11.975 1.00 90.69 C ANISOU 169 CB ASN A 27 13714 11581 9163 2622 249 1421 C ATOM 170 CG ASN A 27 57.183 -8.315 10.839 1.00 98.31 C ANISOU 170 CG ASN A 27 14994 12569 9791 2622 529 1411 C ATOM 171 OD1 ASN A 27 56.946 -7.715 9.788 1.00117.87 O ANISOU 171 OD1 ASN A 27 17784 15045 11957 2829 645 1746 O ATOM 172 ND2 ASN A 27 58.313 -8.980 11.043 1.00 91.31 N ANISOU 172 ND2 ASN A 27 14033 11703 8957 2410 653 1037 N ATOM 173 N GLU A 28 54.869 -7.750 14.796 1.00100.63 N ANISOU 173 N GLU A 28 14362 12553 11318 2480 153 1339 N ATOM 174 CA GLU A 28 53.628 -7.569 15.533 1.00110.42 C ANISOU 174 CA GLU A 28 15402 13745 12805 2557 -44 1471 C ATOM 175 C GLU A 28 53.864 -6.848 16.857 1.00109.93 C ANISOU 175 C GLU A 28 15186 13414 13170 2393 288 1351 C ATOM 176 O GLU A 28 54.670 -7.286 17.676 1.00115.15 O ANISOU 176 O GLU A 28 15733 14076 13944 2173 347 1007 O ATOM 177 CB GLU A 28 52.951 -8.917 15.761 1.00117.47 C ANISOU 177 CB GLU A 28 16117 14881 13634 2525 -555 1291 C ATOM 178 CG GLU A 28 52.507 -9.539 14.449 1.00133.77 C ANISOU 178 CG GLU A 28 18314 17224 15287 2684 -904 1401 C ATOM 179 CD GLU A 28 51.556 -8.662 13.665 1.00159.69 C ANISOU 179 CD GLU A 28 21683 20535 18458 2975 -963 1824 C ATOM 180 OE1 GLU A 28 50.655 -8.049 14.275 1.00167.58 O ANISOU 180 OE1 GLU A 28 22506 21408 19758 3068 -959 2000 O ATOM 181 OE2 GLU A 28 51.744 -8.565 12.435 1.00166.91 O ANISOU 181 OE2 GLU A 28 22855 21592 18972 3128 -992 1989 O ATOM 182 N ALA A 29 53.159 -5.739 17.059 1.00110.64 N ANISOU 182 N ALA A 29 15275 13280 13482 2515 503 1631 N ATOM 183 CA ALA A 29 53.284 -4.967 18.288 1.00100.94 C ANISOU 183 CA ALA A 29 13921 11777 12654 2354 849 1514 C ATOM 184 C ALA A 29 52.569 -5.690 19.422 1.00101.74 C ANISOU 184 C ALA A 29 13770 11947 12939 2267 550 1334 C ATOM 185 O ALA A 29 52.983 -5.616 20.579 1.00 99.09 O ANISOU 185 O ALA A 29 13323 11508 12820 2059 712 1067 O ATOM 186 CB ALA A 29 52.724 -3.563 18.105 1.00 98.26 C ANISOU 186 CB ALA A 29 13686 11138 12511 2529 1218 1881 C ATOM 187 N ALA A 30 51.491 -6.389 19.078 1.00 98.81 N ANISOU 187 N ALA A 30 13314 11757 12471 2424 125 1469 N ATOM 188 CA ALA A 30 50.723 -7.152 20.055 1.00 85.51 C ANISOU 188 CA ALA A 30 11408 10120 10962 2345 -135 1314 C ATOM 189 C ALA A 30 51.577 -8.219 20.733 1.00 93.04 C ANISOU 189 C ALA A 30 12328 11185 11838 2125 -241 927 C ATOM 190 O ALA A 30 51.410 -8.495 21.920 1.00102.48 O ANISOU 190 O ALA A 30 13404 12310 13223 1999 -232 750 O ATOM 191 CB ALA A 30 49.514 -7.792 19.393 1.00 91.24 C ANISOU 191 CB ALA A 30 12032 11050 11587 2526 -570 1477 C ATOM 192 N PHE A 31 52.485 -8.824 19.973 1.00 93.28 N ANISOU 192 N PHE A 31 12477 11386 11578 2102 -328 809 N ATOM 193 CA PHE A 31 53.374 -9.837 20.530 1.00 76.53 C ANISOU 193 CA PHE A 31 10325 9373 9379 1945 -421 467 C ATOM 194 C PHE A 31 54.365 -9.215 21.512 1.00 85.79 C ANISOU 194 C PHE A 31 11458 10417 10722 1779 -89 256 C ATOM 195 O PHE A 31 54.739 -9.839 22.501 1.00 88.71 O ANISOU 195 O PHE A 31 11741 10834 11132 1673 -163 5 O ATOM 196 CB PHE A 31 54.126 -10.582 19.424 1.00 66.96 C ANISOU 196 CB PHE A 31 9243 8356 7841 1973 -552 390 C ATOM 197 CG PHE A 31 55.013 -11.688 19.937 1.00 59.64 C ANISOU 197 CG PHE A 31 8275 7536 6849 1862 -654 63 C ATOM 198 CD1 PHE A 31 54.481 -12.932 20.242 1.00 59.81 C ANISOU 198 CD1 PHE A 31 8245 7645 6834 1864 -965 -41 C ATOM 199 CD2 PHE A 31 56.375 -11.487 20.114 1.00 65.75 C ANISOU 199 CD2 PHE A 31 9050 8312 7618 1766 -422 -143 C ATOM 200 CE1 PHE A 31 55.285 -13.950 20.719 1.00 60.59 C ANISOU 200 CE1 PHE A 31 8332 7813 6875 1811 -1036 -300 C ATOM 201 CE2 PHE A 31 57.184 -12.504 20.590 1.00 62.31 C ANISOU 201 CE2 PHE A 31 8555 7992 7129 1717 -536 -421 C ATOM 202 CZ PHE A 31 56.638 -13.737 20.892 1.00 61.19 C ANISOU 202 CZ PHE A 31 8400 7918 6933 1759 -841 -477 C ATOM 203 N ARG A 32 54.792 -7.987 21.231 1.00 93.54 N ANISOU 203 N ARG A 32 12508 11239 11793 1760 286 351 N ATOM 204 CA ARG A 32 55.729 -7.289 22.103 1.00 96.24 C ANISOU 204 CA ARG A 32 12787 11462 12317 1567 630 105 C ATOM 205 C ARG A 32 55.058 -7.000 23.436 1.00 92.02 C ANISOU 205 C ARG A 32 12136 10798 12029 1492 672 47 C ATOM 206 O ARG A 32 55.680 -7.084 24.498 1.00 83.19 O ANISOU 206 O ARG A 32 10924 9709 10975 1331 731 -254 O ATOM 207 CB ARG A 32 56.198 -5.976 21.482 1.00 93.05 C ANISOU 207 CB ARG A 32 12499 10854 12003 1547 1090 228 C ATOM 208 CG ARG A 32 57.163 -6.118 20.320 1.00 79.64 C ANISOU 208 CG ARG A 32 10932 9248 10080 1562 1182 212 C ATOM 209 CD ARG A 32 57.766 -4.769 19.978 1.00 88.52 C ANISOU 209 CD ARG A 32 12165 10112 11357 1482 1744 265 C ATOM 210 NE ARG A 32 56.896 -3.988 19.111 1.00 92.31 N ANISOU 210 NE ARG A 32 12858 10411 11806 1706 1886 720 N ATOM 211 CZ ARG A 32 56.928 -4.020 17.790 1.00112.15 C ANISOU 211 CZ ARG A 32 15600 12973 14038 1883 1887 975 C ATOM 212 NH1 ARG A 32 57.800 -4.800 17.170 1.00117.99 N ANISOU 212 NH1 ARG A 32 16388 13914 14528 1831 1788 797 N ATOM 213 NH2 ARG A 32 56.095 -3.255 17.101 1.00125.16 N ANISOU 213 NH2 ARG A 32 17438 14468 15648 2127 2000 1412 N ATOM 214 N GLN A 33 53.780 -6.648 23.366 1.00 77.73 N ANISOU 214 N GLN A 33 10328 8857 10347 1623 643 333 N ATOM 215 CA GLN A 33 53.005 -6.336 24.557 1.00 85.28 C ANISOU 215 CA GLN A 33 11188 9656 11556 1565 726 308 C ATOM 216 C GLN A 33 52.799 -7.598 25.385 1.00 94.19 C ANISOU 216 C GLN A 33 12243 10943 12603 1520 399 117 C ATOM 217 O GLN A 33 52.890 -7.569 26.613 1.00 94.71 O ANISOU 217 O GLN A 33 12266 10955 12764 1392 491 -82 O ATOM 218 CB GLN A 33 51.657 -5.717 24.179 1.00 87.98 C ANISOU 218 CB GLN A 33 11517 9832 12078 1751 763 673 C ATOM 219 CG GLN A 33 51.741 -4.256 23.778 1.00103.76 C ANISOU 219 CG GLN A 33 13610 11567 14249 1801 1207 876 C ATOM 220 CD GLN A 33 50.568 -3.816 22.927 1.00108.35 C ANISOU 220 CD GLN A 33 14204 12074 14892 2093 1147 1310 C ATOM 221 OE1 GLN A 33 49.529 -4.474 22.889 1.00110.60 O ANISOU 221 OE1 GLN A 33 14360 12482 15181 2218 799 1417 O ATOM 222 NE2 GLN A 33 50.726 -2.688 22.244 1.00118.45 N ANISOU 222 NE2 GLN A 33 15630 13149 16227 2211 1500 1559 N ATOM 223 N GLU A 34 52.523 -8.706 24.706 1.00 92.09 N ANISOU 223 N GLU A 34 11986 10861 12144 1626 42 175 N ATOM 224 CA GLU A 34 52.371 -9.994 25.374 1.00 88.02 C ANISOU 224 CA GLU A 34 11439 10459 11544 1596 -230 10 C ATOM 225 C GLU A 34 53.699 -10.445 25.968 1.00 84.84 C ANISOU 225 C GLU A 34 11058 10181 10994 1496 -222 -293 C ATOM 226 O GLU A 34 53.736 -11.050 27.040 1.00 89.11 O ANISOU 226 O GLU A 34 11593 10744 11520 1453 -294 -450 O ATOM 227 CB GLU A 34 51.831 -11.047 24.406 1.00 87.87 C ANISOU 227 CB GLU A 34 11429 10590 11369 1708 -571 106 C ATOM 228 CG GLU A 34 50.395 -10.794 23.989 1.00105.80 C ANISOU 228 CG GLU A 34 13609 12797 13792 1816 -663 359 C ATOM 229 CD GLU A 34 50.003 -11.532 22.726 1.00118.66 C ANISOU 229 CD GLU A 34 15243 14620 15223 1923 -983 443 C ATOM 230 OE1 GLU A 34 50.814 -12.343 22.233 1.00122.59 O ANISOU 230 OE1 GLU A 34 15837 15268 15472 1898 -1112 296 O ATOM 231 OE2 GLU A 34 48.881 -11.299 22.226 1.00118.63 O ANISOU 231 OE2 GLU A 34 15133 14629 15313 2036 -1108 642 O ATOM 232 N GLY A 35 54.786 -10.159 25.256 1.00 78.14 N ANISOU 232 N GLY A 35 10236 9422 10033 1477 -132 -368 N ATOM 233 CA GLY A 35 56.119 -10.457 25.745 1.00 81.14 C ANISOU 233 CA GLY A 35 10574 9944 10310 1393 -115 -671 C ATOM 234 C GLY A 35 56.373 -9.716 27.043 1.00 82.00 C ANISOU 234 C GLY A 35 10613 9982 10562 1252 95 -860 C ATOM 235 O GLY A 35 56.955 -10.260 27.981 1.00 81.61 O ANISOU 235 O GLY A 35 10519 10069 10419 1222 -15 -1095 O ATOM 236 N VAL A 36 55.930 -8.464 27.089 1.00 84.71 N ANISOU 236 N VAL A 36 10956 10110 11118 1179 403 -755 N ATOM 237 CA VAL A 36 56.023 -7.650 28.295 1.00 80.61 C ANISOU 237 CA VAL A 36 10388 9486 10754 1018 649 -943 C ATOM 238 C VAL A 36 55.131 -8.216 29.397 1.00 77.70 C ANISOU 238 C VAL A 36 10048 9088 10388 1044 506 -932 C ATOM 239 O VAL A 36 55.542 -8.322 30.554 1.00 85.16 O ANISOU 239 O VAL A 36 10978 10113 11265 954 506 -1182 O ATOM 240 CB VAL A 36 55.632 -6.184 28.016 1.00 74.42 C ANISOU 240 CB VAL A 36 9628 8414 10235 951 1066 -800 C ATOM 241 CG1 VAL A 36 55.468 -5.413 29.315 1.00 73.81 C ANISOU 241 CG1 VAL A 36 9520 8189 10334 779 1328 -989 C ATOM 242 CG2 VAL A 36 56.668 -5.519 27.120 1.00 81.82 C ANISOU 242 CG2 VAL A 36 10564 9341 11184 882 1312 -863 C ATOM 243 N ALA A 37 53.912 -8.588 29.020 1.00 75.97 N ANISOU 243 N ALA A 37 9867 8763 10233 1171 387 -652 N ATOM 244 CA ALA A 37 52.935 -9.138 29.956 1.00 74.57 C ANISOU 244 CA ALA A 37 9718 8511 10102 1191 304 -617 C ATOM 245 C ALA A 37 53.413 -10.438 30.597 1.00 73.94 C ANISOU 245 C ALA A 37 9698 8622 9774 1226 41 -787 C ATOM 246 O ALA A 37 53.147 -10.688 31.772 1.00 80.25 O ANISOU 246 O ALA A 37 10561 9384 10546 1192 70 -878 O ATOM 247 CB ALA A 37 51.605 -9.359 29.252 1.00 76.54 C ANISOU 247 CB ALA A 37 9939 8649 10492 1315 205 -317 C ATOM 248 N VAL A 38 54.115 -11.261 29.825 1.00 74.85 N ANISOU 248 N VAL A 38 9814 8924 9701 1311 -188 -816 N ATOM 249 CA VAL A 38 54.652 -12.518 30.336 1.00 75.61 C ANISOU 249 CA VAL A 38 9975 9184 9568 1390 -420 -950 C ATOM 250 C VAL A 38 55.699 -12.217 31.400 1.00 79.74 C ANISOU 250 C VAL A 38 10475 9851 9971 1327 -365 -1225 C ATOM 251 O VAL A 38 55.711 -12.831 32.469 1.00 77.22 O ANISOU 251 O VAL A 38 10248 9583 9508 1377 -449 -1306 O ATOM 252 CB VAL A 38 55.269 -13.379 29.212 1.00 72.36 C ANISOU 252 CB VAL A 38 9560 8926 9006 1494 -631 -943 C ATOM 253 CG1 VAL A 38 56.151 -14.475 29.795 1.00 73.02 C ANISOU 253 CG1 VAL A 38 9691 9183 8870 1596 -813 -1113 C ATOM 254 CG2 VAL A 38 54.175 -13.986 28.349 1.00 79.50 C ANISOU 254 CG2 VAL A 38 10503 9739 9966 1557 -758 -729 C ATOM 255 N LEU A 39 56.572 -11.260 31.101 1.00 82.95 N ANISOU 255 N LEU A 39 10762 10326 10430 1217 -212 -1376 N ATOM 256 CA LEU A 39 57.607 -10.842 32.037 1.00 83.30 C ANISOU 256 CA LEU A 39 10722 10544 10386 1119 -160 -1699 C ATOM 257 C LEU A 39 57.001 -10.288 33.323 1.00 87.46 C ANISOU 257 C LEU A 39 11321 10957 10953 1014 -1 -1767 C ATOM 258 O LEU A 39 57.467 -10.593 34.419 1.00 83.98 O ANISOU 258 O LEU A 39 10909 10692 10310 1026 -104 -1973 O ATOM 259 CB LEU A 39 58.509 -9.786 31.393 1.00 90.55 C ANISOU 259 CB LEU A 39 11480 11490 11434 967 60 -1861 C ATOM 260 CG LEU A 39 59.599 -9.168 32.270 1.00106.10 C ANISOU 260 CG LEU A 39 13294 13647 13371 804 150 -2264 C ATOM 261 CD1 LEU A 39 60.621 -10.214 32.687 1.00118.56 C ANISOU 261 CD1 LEU A 39 14783 15578 14685 947 -187 -2471 C ATOM 262 CD2 LEU A 39 60.269 -7.998 31.561 1.00106.09 C ANISOU 262 CD2 LEU A 39 13151 13571 13588 607 481 -2405 C ATOM 263 N LEU A 40 55.949 -9.488 33.181 1.00 86.40 N ANISOU 263 N LEU A 40 11224 10536 11067 932 252 -1588 N ATOM 264 CA LEU A 40 55.244 -8.938 34.333 1.00 82.38 C ANISOU 264 CA LEU A 40 10797 9867 10635 828 461 -1635 C ATOM 265 C LEU A 40 54.533 -10.023 35.130 1.00 90.54 C ANISOU 265 C LEU A 40 11998 10890 11514 953 296 -1536 C ATOM 266 O LEU A 40 54.559 -10.014 36.359 1.00 95.03 O ANISOU 266 O LEU A 40 12673 11498 11938 907 346 -1693 O ATOM 267 CB LEU A 40 54.239 -7.870 33.896 1.00 90.79 C ANISOU 267 CB LEU A 40 11847 10602 12047 755 786 -1430 C ATOM 268 CG LEU A 40 54.690 -6.410 33.999 1.00 93.33 C ANISOU 268 CG LEU A 40 12096 10805 12561 549 1164 -1612 C ATOM 269 CD1 LEU A 40 55.963 -6.161 33.204 1.00 92.27 C ANISOU 269 CD1 LEU A 40 11838 10839 12380 495 1152 -1772 C ATOM 270 CD2 LEU A 40 53.578 -5.474 33.548 1.00 90.05 C ANISOU 270 CD2 LEU A 40 11691 10028 12494 553 1482 -1336 C ATOM 271 N ALA A 41 53.909 -10.962 34.426 1.00 82.11 N ANISOU 271 N ALA A 41 10968 9766 10464 1101 120 -1291 N ATOM 272 CA ALA A 41 53.172 -12.037 35.079 1.00 78.48 C ANISOU 272 CA ALA A 41 10674 9237 9906 1204 23 -1186 C ATOM 273 C ALA A 41 54.094 -12.890 35.940 1.00 80.26 C ANISOU 273 C ALA A 41 11024 9702 9771 1312 -172 -1355 C ATOM 274 O ALA A 41 53.754 -13.231 37.070 1.00 87.53 O ANISOU 274 O ALA A 41 12130 10577 10550 1340 -120 -1373 O ATOM 275 CB ALA A 41 52.466 -12.900 34.048 1.00 67.51 C ANISOU 275 CB ALA A 41 9268 7767 8617 1311 -130 -955 C ATOM 276 N VAL A 42 55.259 -13.230 35.400 1.00 77.30 N ANISOU 276 N VAL A 42 10550 9579 9241 1393 -385 -1467 N ATOM 277 CA VAL A 42 56.231 -14.027 36.135 1.00 84.42 C ANISOU 277 CA VAL A 42 11525 10746 9805 1549 -606 -1617 C ATOM 278 C VAL A 42 56.725 -13.277 37.367 1.00 85.07 C ANISOU 278 C VAL A 42 11614 10981 9726 1452 -530 -1878 C ATOM 279 O VAL A 42 56.758 -13.830 38.466 1.00 90.53 O ANISOU 279 O VAL A 42 12498 11759 10138 1570 -610 -1910 O ATOM 280 CB VAL A 42 57.432 -14.408 35.252 1.00 84.67 C ANISOU 280 CB VAL A 42 11389 11022 9761 1648 -819 -1714 C ATOM 281 CG1 VAL A 42 58.538 -15.027 36.094 1.00 83.02 C ANISOU 281 CG1 VAL A 42 11191 11130 9224 1827 -1049 -1900 C ATOM 282 CG2 VAL A 42 56.994 -15.360 34.150 1.00 80.65 C ANISOU 282 CG2 VAL A 42 10925 10389 9330 1762 -918 -1490 C ATOM 283 N VAL A 43 57.099 -12.015 37.175 1.00 79.62 N ANISOU 283 N VAL A 43 10735 10316 9203 1234 -357 -2070 N ATOM 284 CA VAL A 43 57.568 -11.174 38.271 1.00 80.59 C ANISOU 284 CA VAL A 43 10832 10582 9205 1081 -254 -2385 C ATOM 285 C VAL A 43 56.494 -11.021 39.342 1.00 89.85 C ANISOU 285 C VAL A 43 12252 11540 10345 1028 -52 -2311 C ATOM 286 O VAL A 43 56.763 -11.202 40.528 1.00 76.19 O ANISOU 286 O VAL A 43 10667 9986 8297 1068 -121 -2473 O ATOM 287 CB VAL A 43 57.996 -9.776 37.774 1.00 71.38 C ANISOU 287 CB VAL A 43 9433 9376 8311 812 1 -2596 C ATOM 288 CG1 VAL A 43 58.198 -8.825 38.946 1.00 73.21 C ANISOU 288 CG1 VAL A 43 9667 9674 8474 596 188 -2934 C ATOM 289 CG2 VAL A 43 59.264 -9.876 36.944 1.00 70.81 C ANISOU 289 CG2 VAL A 43 9112 9562 8231 838 -165 -2757 C ATOM 290 N ILE A 44 55.277 -10.699 38.916 1.00 92.01 N ANISOU 290 N ILE A 44 12573 11449 10939 955 198 -2067 N ATOM 291 CA ILE A 44 54.168 -10.529 39.845 1.00 87.51 C ANISOU 291 CA ILE A 44 12213 10628 10410 895 448 -1989 C ATOM 292 C ILE A 44 53.865 -11.827 40.586 1.00 90.45 C ANISOU 292 C ILE A 44 12858 11027 10483 1103 294 -1857 C ATOM 293 O ILE A 44 53.670 -11.821 41.801 1.00 98.22 O ANISOU 293 O ILE A 44 14065 12013 11241 1089 402 -1946 O ATOM 294 CB ILE A 44 52.905 -10.036 39.117 1.00 77.56 C ANISOU 294 CB ILE A 44 10889 8986 9593 822 710 -1730 C ATOM 295 CG1 ILE A 44 53.086 -8.579 38.694 1.00 73.23 C ANISOU 295 CG1 ILE A 44 10158 8339 9328 622 978 -1849 C ATOM 296 CG2 ILE A 44 51.681 -10.168 40.006 1.00 62.36 C ANISOU 296 CG2 ILE A 44 9166 6791 7736 803 949 -1615 C ATOM 297 CD1 ILE A 44 51.887 -8.001 38.002 1.00 71.84 C ANISOU 297 CD1 ILE A 44 9910 7809 9577 601 1229 -1577 C ATOM 298 N ALA A 45 53.839 -12.940 39.860 1.00 93.25 N ANISOU 298 N ALA A 45 13221 11386 10821 1293 74 -1651 N ATOM 299 CA ALA A 45 53.573 -14.234 40.480 1.00 95.25 C ANISOU 299 CA ALA A 45 13756 11613 10821 1502 -24 -1505 C ATOM 300 C ALA A 45 54.684 -14.611 41.457 1.00 96.56 C ANISOU 300 C ALA A 45 14057 12129 10502 1663 -244 -1687 C ATOM 301 O ALA A 45 54.432 -15.242 42.484 1.00107.91 O ANISOU 301 O ALA A 45 15809 13541 11652 1798 -213 -1620 O ATOM 302 CB ALA A 45 53.411 -15.313 39.419 1.00 94.39 C ANISOU 302 CB ALA A 45 13611 11432 10820 1650 -194 -1293 C ATOM 303 N CYS A 46 55.911 -14.217 41.132 1.00 87.12 N ANISOU 303 N CYS A 46 12617 11267 9215 1659 -458 -1918 N ATOM 304 CA CYS A 46 57.062 -14.505 41.983 1.00 93.24 C ANISOU 304 CA CYS A 46 13431 12450 9546 1825 -726 -2130 C ATOM 305 C CYS A 46 57.222 -13.510 43.129 1.00 99.60 C ANISOU 305 C CYS A 46 14277 13401 10164 1646 -607 -2428 C ATOM 306 O CYS A 46 57.899 -13.803 44.114 1.00105.50 O ANISOU 306 O CYS A 46 15143 14475 10467 1800 -814 -2581 O ATOM 307 CB CYS A 46 58.345 -14.542 41.153 1.00100.99 C ANISOU 307 CB CYS A 46 14082 13750 10539 1890 -1003 -2294 C ATOM 308 SG CYS A 46 58.482 -15.988 40.077 1.00124.47 S ANISOU 308 SG CYS A 46 17071 16659 13561 2182 -1211 -2006 S ATOM 309 N TRP A 47 56.603 -12.339 43.007 1.00 98.50 N ANISOU 309 N TRP A 47 14048 13027 10350 1334 -274 -2515 N ATOM 310 CA TRP A 47 56.748 -11.321 44.042 1.00 86.46 C ANISOU 310 CA TRP A 47 12558 11609 8685 1118 -109 -2842 C ATOM 311 C TRP A 47 55.608 -11.417 45.048 1.00 86.03 C ANISOU 311 C TRP A 47 12879 11280 8527 1103 170 -2705 C ATOM 312 O TRP A 47 55.729 -10.954 46.183 1.00 79.87 O ANISOU 312 O TRP A 47 12257 10634 7455 1011 254 -2949 O ATOM 313 CB TRP A 47 56.800 -9.921 43.420 1.00 93.78 C ANISOU 313 CB TRP A 47 13194 12408 10031 783 162 -3046 C ATOM 314 CG TRP A 47 56.719 -8.806 44.420 1.00115.89 C ANISOU 314 CG TRP A 47 16052 15202 12779 510 440 -3379 C ATOM 315 CD1 TRP A 47 57.689 -8.410 45.295 1.00123.91 C ANISOU 315 CD1 TRP A 47 17012 16615 13454 416 304 -3817 C ATOM 316 CD2 TRP A 47 55.599 -7.943 44.645 1.00124.42 C ANISOU 316 CD2 TRP A 47 17244 15861 14167 291 912 -3325 C ATOM 317 NE1 TRP A 47 57.240 -7.354 46.053 1.00130.93 N ANISOU 317 NE1 TRP A 47 17999 17343 14405 126 680 -4057 N ATOM 318 CE2 TRP A 47 55.960 -7.048 45.672 1.00130.96 C ANISOU 318 CE2 TRP A 47 18112 16827 14819 54 1074 -3748 C ATOM 319 CE3 TRP A 47 54.325 -7.840 44.077 1.00120.70 C ANISOU 319 CE3 TRP A 47 16823 14924 14114 279 1208 -2976 C ATOM 320 CZ2 TRP A 47 55.092 -6.062 46.142 1.00134.81 C ANISOU 320 CZ2 TRP A 47 18715 16960 15546 -194 1563 -3821 C ATOM 321 CZ3 TRP A 47 53.466 -6.862 44.545 1.00124.17 C ANISOU 321 CZ3 TRP A 47 17344 15030 14803 62 1668 -3030 C ATOM 322 CH2 TRP A 47 53.853 -5.986 45.567 1.00132.65 C ANISOU 322 CH2 TRP A 47 18485 16210 15707 -173 1863 -3443 C ATOM 323 N LEU A 48 54.508 -12.039 44.639 1.00 99.66 N ANISOU 323 N LEU A 48 14745 12633 10487 1184 321 -2339 N ATOM 324 CA LEU A 48 53.423 -12.301 45.572 1.00101.53 C ANISOU 324 CA LEU A 48 15343 12591 10642 1191 607 -2191 C ATOM 325 C LEU A 48 53.752 -13.567 46.344 1.00 86.59 C ANISOU 325 C LEU A 48 13790 10877 8233 1508 381 -2073 C ATOM 326 O LEU A 48 54.401 -14.471 45.818 1.00 99.71 O ANISOU 326 O LEU A 48 15393 12714 9776 1750 55 -1962 O ATOM 327 CB LEU A 48 52.079 -12.440 44.856 1.00110.51 C ANISOU 327 CB LEU A 48 16452 13260 12276 1132 882 -1884 C ATOM 328 CG LEU A 48 51.567 -11.228 44.079 1.00103.17 C ANISOU 328 CG LEU A 48 15223 12104 11873 883 1134 -1915 C ATOM 329 CD1 LEU A 48 50.187 -11.515 43.518 1.00 95.06 C ANISOU 329 CD1 LEU A 48 14171 10671 11278 881 1352 -1609 C ATOM 330 CD2 LEU A 48 51.532 -10.010 44.983 1.00114.51 C ANISOU 330 CD2 LEU A 48 16711 13508 13290 646 1444 -2196 C ATOM 331 N ASP A 49 53.312 -13.629 47.593 1.00 92.96 N ANISOU 331 N ASP A 49 14975 11623 8725 1523 580 -2086 N ATOM 332 CA ASP A 49 53.469 -14.837 48.387 1.00110.82 C ANISOU 332 CA ASP A 49 17642 13981 10483 1855 442 -1909 C ATOM 333 C ASP A 49 52.255 -15.736 48.168 1.00107.74 C ANISOU 333 C ASP A 49 17480 13106 10351 1923 728 -1536 C ATOM 334 O ASP A 49 51.316 -15.724 48.963 1.00116.05 O ANISOU 334 O ASP A 49 18847 13865 11380 1850 1110 -1456 O ATOM 335 CB ASP A 49 53.650 -14.503 49.868 1.00132.13 C ANISOU 335 CB ASP A 49 20685 16882 12638 1860 514 -2109 C ATOM 336 CG ASP A 49 54.046 -15.714 50.693 1.00150.03 C ANISOU 336 CG ASP A 49 23382 19336 14288 2270 305 -1923 C ATOM 337 OD1 ASP A 49 54.669 -16.639 50.128 1.00150.50 O ANISOU 337 OD1 ASP A 49 23364 19538 14281 2561 -23 -1757 O ATOM 338 OD2 ASP A 49 53.748 -15.737 51.906 1.00157.10 O ANISOU 338 OD2 ASP A 49 24711 20229 14752 2318 487 -1935 O ATOM 339 N VAL A 50 52.276 -16.513 47.091 1.00 88.36 N ANISOU 339 N VAL A 50 14857 10563 8152 2043 568 -1337 N ATOM 340 CA VAL A 50 51.150 -17.375 46.743 1.00 87.43 C ANISOU 340 CA VAL A 50 14882 9997 8339 2066 826 -1039 C ATOM 341 C VAL A 50 51.636 -18.805 46.551 1.00 84.17 C ANISOU 341 C VAL A 50 14656 9632 7693 2407 600 -831 C ATOM 342 O VAL A 50 52.831 -19.034 46.367 1.00 89.74 O ANISOU 342 O VAL A 50 15260 10715 8121 2613 210 -906 O ATOM 343 CB VAL A 50 50.448 -16.901 45.458 1.00 93.63 C ANISOU 343 CB VAL A 50 15256 10552 9768 1831 915 -1008 C ATOM 344 CG1 VAL A 50 49.803 -15.541 45.673 1.00 94.69 C ANISOU 344 CG1 VAL A 50 15243 10547 10187 1531 1218 -1156 C ATOM 345 CG2 VAL A 50 51.441 -16.846 44.306 1.00 81.96 C ANISOU 345 CG2 VAL A 50 13417 9362 8360 1885 522 -1082 C ATOM 346 N ASP A 51 50.719 -19.768 46.590 1.00 70.31 N ANISOU 346 N ASP A 51 13159 7477 6080 2464 874 -583 N ATOM 347 CA ASP A 51 51.111 -21.167 46.441 1.00 81.26 C ANISOU 347 CA ASP A 51 14771 8831 7275 2786 742 -374 C ATOM 348 C ASP A 51 51.455 -21.503 44.997 1.00 81.55 C ANISOU 348 C ASP A 51 14428 8915 7642 2783 484 -373 C ATOM 349 O ASP A 51 51.239 -20.701 44.088 1.00 84.95 O ANISOU 349 O ASP A 51 14451 9365 8462 2529 436 -496 O ATOM 350 CB ASP A 51 50.012 -22.112 46.939 1.00 95.13 C ANISOU 350 CB ASP A 51 16942 10095 9108 2817 1186 -134 C ATOM 351 CG ASP A 51 48.693 -21.907 46.225 1.00120.70 C ANISOU 351 CG ASP A 51 19933 12932 12994 2481 1503 -130 C ATOM 352 OD1 ASP A 51 48.320 -20.743 45.974 1.00132.34 O ANISOU 352 OD1 ASP A 51 21084 14445 14753 2211 1543 -288 O ATOM 353 OD2 ASP A 51 48.030 -22.920 45.912 1.00130.91 O ANISOU 353 OD2 ASP A 51 21345 13872 14523 2494 1717 23 O ATOM 354 N ALA A 52 51.993 -22.702 44.802 1.00 89.29 N ANISOU 354 N ALA A 52 16092 11731 6101 5745 -162 448 N ATOM 355 CA ALA A 52 52.511 -23.128 43.509 1.00 83.71 C ANISOU 355 CA ALA A 52 15003 10961 5842 5530 -263 475 C ATOM 356 C ALA A 52 51.447 -23.181 42.415 1.00 81.11 C ANISOU 356 C ALA A 52 14513 10258 6045 5323 113 533 C ATOM 357 O ALA A 52 51.660 -22.666 41.318 1.00 84.86 O ANISOU 357 O ALA A 52 14742 10637 6863 4981 -12 329 O ATOM 358 CB ALA A 52 53.180 -24.483 43.644 1.00 77.30 C ANISOU 358 CB ALA A 52 14014 10289 5068 5768 -290 796 C ATOM 359 N CYS A 53 50.313 -23.809 42.716 1.00 84.01 N ANISOU 359 N CYS A 53 15017 10424 6478 5540 579 803 N ATOM 360 CA CYS A 53 49.245 -23.985 41.734 1.00 84.06 C ANISOU 360 CA CYS A 53 14836 10101 7000 5387 940 848 C ATOM 361 C CYS A 53 48.740 -22.656 41.177 1.00 74.67 C ANISOU 361 C CYS A 53 13685 8768 5917 5110 873 539 C ATOM 362 O CYS A 53 48.507 -22.527 39.975 1.00 84.64 O ANISOU 362 O CYS A 53 14678 9880 7602 4859 892 462 O ATOM 363 CB CYS A 53 48.080 -24.765 42.350 1.00 88.38 C ANISOU 363 CB CYS A 53 15544 10461 7574 5662 1471 1130 C ATOM 364 SG CYS A 53 48.512 -26.416 42.952 1.00152.23 S ANISOU 364 SG CYS A 53 23495 18699 15646 5842 1679 1467 S ATOM 365 N THR A 54 48.580 -21.669 42.051 1.00 84.68 N ANISOU 365 N THR A 54 15293 10087 6795 5168 799 364 N ATOM 366 CA THR A 54 48.137 -20.348 41.627 1.00 80.36 C ANISOU 366 CA THR A 54 14809 9381 6344 4931 747 77 C ATOM 367 C THR A 54 49.220 -19.666 40.796 1.00 72.16 C ANISOU 367 C THR A 54 13562 8436 5419 4603 339 -172 C ATOM 368 O THR A 54 48.930 -19.044 39.773 1.00 77.61 O ANISOU 368 O THR A 54 14115 8939 6433 4355 342 -287 O ATOM 369 CB THR A 54 47.763 -19.471 42.828 1.00 69.90 C ANISOU 369 CB THR A 54 13895 8083 4580 5068 787 -80 C ATOM 370 OG1 THR A 54 46.690 -20.091 43.549 1.00 84.99 O ANISOU 370 OG1 THR A 54 15957 9865 6470 5314 1201 179 O ATOM 371 CG2 THR A 54 47.322 -18.093 42.366 1.00 68.84 C ANISOU 371 CG2 THR A 54 13796 7746 4616 4814 748 -363 C ATOM 372 N ARG A 55 50.469 -19.796 41.236 1.00 67.15 N ANISOU 372 N ARG A 55 12901 8090 4523 4616 -3 -250 N ATOM 373 CA ARG A 55 51.600 -19.216 40.517 1.00 79.17 C ANISOU 373 CA ARG A 55 14205 9704 6172 4302 -369 -506 C ATOM 374 C ARG A 55 51.752 -19.824 39.129 1.00 78.75 C ANISOU 374 C ARG A 55 13778 9544 6600 4100 -324 -390 C ATOM 375 O ARG A 55 52.062 -19.117 38.169 1.00 77.67 O ANISOU 375 O ARG A 55 13501 9311 6698 3791 -439 -572 O ATOM 376 CB ARG A 55 52.898 -19.360 41.323 1.00 81.11 C ANISOU 376 CB ARG A 55 14451 10302 6063 4391 -746 -626 C ATOM 377 CG ARG A 55 54.102 -18.733 40.626 1.00 90.82 C ANISOU 377 CG ARG A 55 15433 11612 7464 4051 -1101 -938 C ATOM 378 CD ARG A 55 55.369 -18.715 41.473 1.00 94.67 C ANISOU 378 CD ARG A 55 15896 12461 7612 4131 -1512 -1144 C ATOM 379 NE ARG A 55 55.152 -18.067 42.765 1.00103.58 N ANISOU 379 NE ARG A 55 17381 13736 8240 4319 -1582 -1318 N ATOM 380 CZ ARG A 55 55.284 -18.654 43.948 1.00104.52 C ANISOU 380 CZ ARG A 55 17686 14140 7888 4687 -1668 -1191 C ATOM 381 NH1 ARG A 55 55.636 -19.929 44.030 1.00109.16 N ANISOU 381 NH1 ARG A 55 18137 14875 8465 4927 -1688 -858 N ATOM 382 NH2 ARG A 55 55.063 -17.957 45.055 1.00106.39 N ANISOU 382 NH2 ARG A 55 18135 14456 7834 4740 -1680 -1358 N ATOM 383 N VAL A 56 51.540 -21.131 39.022 1.00 67.77 N ANISOU 383 N VAL A 56 12235 8161 5354 4273 -132 -92 N ATOM 384 CA VAL A 56 51.583 -21.788 37.723 1.00 72.13 C ANISOU 384 CA VAL A 56 12428 8615 6364 4091 -48 -1 C ATOM 385 C VAL A 56 50.477 -21.236 36.826 1.00 68.78 C ANISOU 385 C VAL A 56 11988 7927 6218 3940 168 -41 C ATOM 386 O VAL A 56 50.714 -20.904 35.665 1.00 63.59 O ANISOU 386 O VAL A 56 11132 7210 5820 3665 83 -146 O ATOM 387 CB VAL A 56 51.428 -23.315 37.852 1.00 59.73 C ANISOU 387 CB VAL A 56 10702 7060 4933 4324 184 313 C ATOM 388 CG1 VAL A 56 51.178 -23.943 36.487 1.00 55.06 C ANISOU 388 CG1 VAL A 56 9749 6331 4840 4130 346 364 C ATOM 389 CG2 VAL A 56 52.658 -23.921 38.511 1.00 74.74 C ANISOU 389 CG2 VAL A 56 12549 9228 6619 4467 -74 375 C ATOM 390 N LEU A 57 49.275 -21.123 37.383 1.00 64.66 N ANISOU 390 N LEU A 57 11683 7254 5631 4134 449 42 N ATOM 391 CA LEU A 57 48.117 -20.636 36.639 1.00 63.67 C ANISOU 391 CA LEU A 57 11535 6886 5773 4052 653 11 C ATOM 392 C LEU A 57 48.240 -19.168 36.225 1.00 63.98 C ANISOU 392 C LEU A 57 11690 6841 5778 3825 459 -229 C ATOM 393 O LEU A 57 47.759 -18.783 35.160 1.00 73.66 O ANISOU 393 O LEU A 57 12793 7922 7271 3674 498 -257 O ATOM 394 CB LEU A 57 46.842 -20.838 37.458 1.00 66.35 C ANISOU 394 CB LEU A 57 11993 7148 6070 4185 975 155 C ATOM 395 CG LEU A 57 46.308 -22.269 37.543 1.00 69.78 C ANISOU 395 CG LEU A 57 12173 7632 6707 4188 1256 410 C ATOM 396 CD1 LEU A 57 45.180 -22.360 38.557 1.00 72.76 C ANISOU 396 CD1 LEU A 57 12718 7943 6984 4293 1554 532 C ATOM 397 CD2 LEU A 57 45.837 -22.735 36.175 1.00 57.89 C ANISOU 397 CD2 LEU A 57 10222 6096 5678 3871 1311 410 C ATOM 398 N LEU A 58 48.872 -18.351 37.064 1.00 66.40 N ANISOU 398 N LEU A 58 12232 7239 5758 3813 259 -405 N ATOM 399 CA LEU A 58 49.064 -16.938 36.740 1.00 68.13 C ANISOU 399 CA LEU A 58 12564 7346 5976 3590 109 -649 C ATOM 400 C LEU A 58 49.981 -16.783 35.533 1.00 75.56 C ANISOU 400 C LEU A 58 13258 8313 7141 3284 -89 -724 C ATOM 401 O LEU A 58 49.763 -15.925 34.678 1.00 85.70 O ANISOU 401 O LEU A 58 14544 9418 8601 3099 -84 -796 O ATOM 402 CB LEU A 58 49.640 -16.173 37.937 1.00 60.65 C ANISOU 402 CB LEU A 58 11884 6514 4648 3627 -61 -877 C ATOM 403 CG LEU A 58 48.731 -15.931 39.144 1.00 83.91 C ANISOU 403 CG LEU A 58 15152 9407 7323 3885 140 -879 C ATOM 404 CD1 LEU A 58 49.509 -15.261 40.268 1.00 66.49 C ANISOU 404 CD1 LEU A 58 13168 7389 4705 3899 -85 -1151 C ATOM 405 CD2 LEU A 58 47.525 -15.092 38.755 1.00 76.11 C ANISOU 405 CD2 LEU A 58 14267 8099 6551 3860 373 -906 C ATOM 406 N ILE A 59 51.005 -17.626 35.473 1.00 76.53 N ANISOU 406 N ILE A 59 13173 8649 7257 3244 -245 -694 N ATOM 407 CA ILE A 59 51.973 -17.580 34.386 1.00 72.08 C ANISOU 407 CA ILE A 59 12360 8122 6904 2949 -409 -778 C ATOM 408 C ILE A 59 51.437 -18.260 33.125 1.00 74.06 C ANISOU 408 C ILE A 59 12369 8292 7480 2882 -242 -603 C ATOM 409 O ILE A 59 51.475 -17.678 32.045 1.00 81.64 O ANISOU 409 O ILE A 59 13267 9143 8610 2658 -255 -657 O ATOM 410 CB ILE A 59 53.304 -18.236 34.796 1.00 73.72 C ANISOU 410 CB ILE A 59 12403 8590 7018 2936 -646 -839 C ATOM 411 CG1 ILE A 59 53.905 -17.506 35.998 1.00 76.01 C ANISOU 411 CG1 ILE A 59 12904 9009 6967 2990 -864 -1073 C ATOM 412 CG2 ILE A 59 54.281 -18.238 33.630 1.00 61.27 C ANISOU 412 CG2 ILE A 59 10546 7030 5704 2617 -768 -937 C ATOM 413 CD1 ILE A 59 55.165 -18.143 36.529 1.00 76.92 C ANISOU 413 CD1 ILE A 59 12856 9416 6955 3037 -1138 -1143 C ATOM 414 N SER A 60 50.930 -19.482 33.273 1.00 63.14 N ANISOU 414 N SER A 60 10856 6959 6176 3083 -69 -401 N ATOM 415 CA SER A 60 50.476 -20.281 32.134 1.00 60.76 C ANISOU 415 CA SER A 60 10275 6618 6193 3023 88 -282 C ATOM 416 C SER A 60 49.351 -19.610 31.342 1.00 69.66 C ANISOU 416 C SER A 60 11453 7559 7457 2985 214 -284 C ATOM 417 O SER A 60 49.313 -19.697 30.114 1.00 70.70 O ANISOU 417 O SER A 60 11391 7683 7789 2819 216 -286 O ATOM 418 CB SER A 60 50.013 -21.659 32.612 1.00 48.11 C ANISOU 418 CB SER A 60 8549 5056 4676 3270 308 -87 C ATOM 419 OG SER A 60 51.096 -22.412 33.131 1.00 88.16 O ANISOU 419 OG SER A 60 13522 10305 9671 3317 186 -45 O ATOM 420 N SER A 61 48.437 -18.947 32.047 1.00 67.27 N ANISOU 420 N SER A 61 11406 7118 7035 3152 315 -285 N ATOM 421 CA SER A 61 47.312 -18.278 31.398 1.00 68.12 C ANISOU 421 CA SER A 61 11560 7042 7281 3165 423 -281 C ATOM 422 C SER A 61 47.806 -17.187 30.452 1.00 72.32 C ANISOU 422 C SER A 61 12140 7512 7829 2915 251 -376 C ATOM 423 O SER A 61 47.239 -16.976 29.379 1.00 64.21 O ANISOU 423 O SER A 61 11023 6417 6959 2865 282 -333 O ATOM 424 CB SER A 61 46.361 -17.686 32.440 1.00 53.03 C ANISOU 424 CB SER A 61 9828 5068 5254 3254 539 -262 C ATOM 425 OG SER A 61 47.001 -16.677 33.201 1.00 70.79 O ANISOU 425 OG SER A 61 12433 7225 7241 3309 414 -428 O ATOM 426 N VAL A 62 48.872 -16.504 30.855 1.00 68.10 N ANISOU 426 N VAL A 62 11743 7002 7130 2767 79 -510 N ATOM 427 CA VAL A 62 49.454 -15.440 30.046 1.00 54.45 C ANISOU 427 CA VAL A 62 10078 5176 5435 2514 -35 -606 C ATOM 428 C VAL A 62 50.310 -16.038 28.930 1.00 61.92 C ANISOU 428 C VAL A 62 10759 6254 6514 2289 -107 -590 C ATOM 429 O VAL A 62 50.336 -15.524 27.809 1.00 73.66 O ANISOU 429 O VAL A 62 12234 7662 8091 2128 -107 -569 O ATOM 430 CB VAL A 62 50.305 -14.480 30.904 1.00 60.54 C ANISOU 430 CB VAL A 62 11060 5908 6032 2413 -165 -815 C ATOM 431 CG1 VAL A 62 50.955 -13.414 30.034 1.00 67.87 C ANISOU 431 CG1 VAL A 62 12041 6693 7053 2130 -223 -916 C ATOM 432 CG2 VAL A 62 49.445 -13.830 31.974 1.00 59.97 C ANISOU 432 CG2 VAL A 62 11263 5701 5822 2619 -72 -860 C ATOM 433 N MET A 63 50.994 -17.136 29.239 1.00 57.33 N ANISOU 433 N MET A 63 9974 5869 5940 2293 -153 -590 N ATOM 434 CA MET A 63 51.822 -17.824 28.257 1.00 45.48 C ANISOU 434 CA MET A 63 8192 4495 4592 2086 -197 -594 C ATOM 435 C MET A 63 50.970 -18.411 27.136 1.00 68.72 C ANISOU 435 C MET A 63 10956 7446 7708 2106 -58 -472 C ATOM 436 O MET A 63 51.413 -18.497 25.991 1.00 65.63 O ANISOU 436 O MET A 63 10418 7103 7416 1896 -73 -491 O ATOM 437 CB MET A 63 52.634 -18.938 28.926 1.00 52.71 C ANISOU 437 CB MET A 63 8917 5603 5508 2141 -260 -602 C ATOM 438 CG MET A 63 53.685 -18.452 29.912 1.00 77.36 C ANISOU 438 CG MET A 63 12148 8792 8454 2103 -460 -766 C ATOM 439 SD MET A 63 55.307 -18.185 29.175 1.00109.13 S ANISOU 439 SD MET A 63 15976 12880 12607 1733 -631 -973 S ATOM 440 CE MET A 63 55.904 -19.869 29.060 1.00 72.45 C ANISOU 440 CE MET A 63 10953 8447 8128 1788 -633 -879 C ATOM 441 N LEU A 64 49.743 -18.806 27.469 1.00 62.90 N ANISOU 441 N LEU A 64 10225 6668 7008 2355 84 -373 N ATOM 442 CA LEU A 64 48.820 -19.350 26.477 1.00 68.47 C ANISOU 442 CA LEU A 64 10730 7393 7890 2397 202 -309 C ATOM 443 C LEU A 64 48.457 -18.306 25.427 1.00 69.36 C ANISOU 443 C LEU A 64 10959 7419 7974 2302 148 -303 C ATOM 444 O LEU A 64 48.312 -18.623 24.248 1.00 59.17 O ANISOU 444 O LEU A 64 9490 6221 6771 2212 154 -293 O ATOM 445 CB LEU A 64 47.551 -19.878 27.149 1.00 53.79 C ANISOU 445 CB LEU A 64 8853 5474 6112 2686 386 -240 C ATOM 446 CG LEU A 64 46.493 -20.464 26.212 1.00 50.40 C ANISOU 446 CG LEU A 64 8174 5073 5904 2749 508 -231 C ATOM 447 CD1 LEU A 64 47.028 -21.702 25.514 1.00 49.70 C ANISOU 447 CD1 LEU A 64 7735 5153 5996 2618 554 -266 C ATOM 448 CD2 LEU A 64 45.219 -20.787 26.972 1.00 42.83 C ANISOU 448 CD2 LEU A 64 7100 4115 5056 2807 662 -175 C ATOM 449 N VAL A 65 48.315 -17.059 25.868 1.00 59.55 N ANISOU 449 N VAL A 65 10023 6000 6602 2333 102 -308 N ATOM 450 CA VAL A 65 48.008 -15.952 24.970 1.00 63.31 C ANISOU 450 CA VAL A 65 10659 6348 7047 2273 67 -263 C ATOM 451 C VAL A 65 49.104 -15.779 23.924 1.00 67.56 C ANISOU 451 C VAL A 65 11151 6951 7567 1980 0 -287 C ATOM 452 O VAL A 65 48.825 -15.539 22.749 1.00 69.41 O ANISOU 452 O VAL A 65 11373 7202 7797 1934 0 -210 O ATOM 453 CB VAL A 65 47.825 -14.633 25.748 1.00 65.42 C ANISOU 453 CB VAL A 65 11265 6375 7217 2337 63 -286 C ATOM 454 CG1 VAL A 65 47.632 -13.466 24.791 1.00 65.01 C ANISOU 454 CG1 VAL A 65 11391 6155 7153 2276 49 -206 C ATOM 455 CG2 VAL A 65 46.646 -14.742 26.700 1.00 66.74 C ANISOU 455 CG2 VAL A 65 11491 6463 7406 2628 165 -266 C ATOM 456 N MET A 66 50.352 -15.924 24.354 1.00 71.63 N ANISOU 456 N MET A 66 11635 7514 8067 1792 -54 -399 N ATOM 457 CA MET A 66 51.489 -15.794 23.452 1.00 72.04 C ANISOU 457 CA MET A 66 11623 7608 8140 1491 -83 -454 C ATOM 458 C MET A 66 51.532 -16.946 22.451 1.00 67.33 C ANISOU 458 C MET A 66 10719 7226 7638 1421 -44 -431 C ATOM 459 O MET A 66 51.874 -16.754 21.285 1.00 66.42 O ANISOU 459 O MET A 66 10585 7141 7509 1239 -20 -414 O ATOM 460 CB MET A 66 52.793 -15.733 24.246 1.00 70.68 C ANISOU 460 CB MET A 66 11437 7447 7972 1325 -164 -624 C ATOM 461 CG MET A 66 53.653 -14.527 23.916 1.00 97.08 C ANISOU 461 CG MET A 66 14963 10616 11309 1071 -165 -719 C ATOM 462 SD MET A 66 55.222 -14.533 24.799 1.00110.00 S ANISOU 462 SD MET A 66 16497 12305 12995 867 -289 -992 S ATOM 463 CE MET A 66 55.942 -16.048 24.180 1.00 64.89 C ANISOU 463 CE MET A 66 10381 6856 7419 756 -303 -999 C ATOM 464 N ILE A 67 51.192 -18.142 22.919 1.00 64.63 N ANISOU 464 N ILE A 67 10142 7020 7394 1564 -12 -437 N ATOM 465 CA ILE A 67 51.172 -19.326 22.068 1.00 48.56 C ANISOU 465 CA ILE A 67 7780 5174 5496 1506 53 -454 C ATOM 466 C ILE A 67 50.127 -19.195 20.964 1.00 52.85 C ANISOU 466 C ILE A 67 8305 5762 6014 1575 85 -393 C ATOM 467 O ILE A 67 50.409 -19.449 19.792 1.00 67.72 O ANISOU 467 O ILE A 67 10059 7776 7896 1411 99 -424 O ATOM 468 CB ILE A 67 50.884 -20.601 22.884 1.00 61.51 C ANISOU 468 CB ILE A 67 9189 6895 7286 1680 130 -457 C ATOM 469 CG1 ILE A 67 52.009 -20.861 23.887 1.00 64.24 C ANISOU 469 CG1 ILE A 67 9523 7253 7631 1636 65 -505 C ATOM 470 CG2 ILE A 67 50.712 -21.797 21.964 1.00 59.93 C ANISOU 470 CG2 ILE A 67 8635 6859 7278 1623 236 -504 C ATOM 471 CD1 ILE A 67 51.740 -22.028 24.808 1.00 76.13 C ANISOU 471 CD1 ILE A 67 10869 8808 9248 1852 158 -451 C ATOM 472 N VAL A 68 48.920 -18.790 21.348 1.00 61.88 N ANISOU 472 N VAL A 68 9573 6810 7130 1829 92 -319 N ATOM 473 CA VAL A 68 47.821 -18.632 20.403 1.00 65.80 C ANISOU 473 CA VAL A 68 10035 7362 7606 1952 82 -273 C ATOM 474 C VAL A 68 48.126 -17.519 19.404 1.00 73.70 C ANISOU 474 C VAL A 68 11272 8316 8416 1829 10 -186 C ATOM 475 O VAL A 68 47.795 -17.626 18.222 1.00 63.91 O ANISOU 475 O VAL A 68 9948 7227 7107 1816 -18 -168 O ATOM 476 CB VAL A 68 46.496 -18.339 21.135 1.00 59.29 C ANISOU 476 CB VAL A 68 9291 6408 6826 2259 109 -224 C ATOM 477 CG1 VAL A 68 45.373 -18.097 20.142 1.00 76.34 C ANISOU 477 CG1 VAL A 68 11395 8638 8972 2408 57 -192 C ATOM 478 CG2 VAL A 68 46.145 -19.495 22.055 1.00 49.31 C ANISOU 478 CG2 VAL A 68 7804 5175 5757 2387 240 -289 C ATOM 479 N GLU A 69 48.764 -16.455 19.882 1.00 55.21 N ANISOU 479 N GLU A 69 9227 5766 5986 1742 -6 -142 N ATOM 480 CA GLU A 69 49.157 -15.347 19.018 1.00 47.26 C ANISOU 480 CA GLU A 69 8477 4650 4829 1613 -14 -41 C ATOM 481 C GLU A 69 50.148 -15.791 17.945 1.00 64.42 C ANISOU 481 C GLU A 69 10523 6987 6966 1329 23 -89 C ATOM 482 O GLU A 69 50.038 -15.397 16.783 1.00 75.83 O ANISOU 482 O GLU A 69 12067 8482 8263 1292 33 13 O ATOM 483 CB GLU A 69 49.764 -14.215 19.848 1.00 51.11 C ANISOU 483 CB GLU A 69 9261 4857 5302 1536 6 -45 C ATOM 484 CG GLU A 69 50.299 -13.052 19.026 1.00 85.26 C ANISOU 484 CG GLU A 69 13860 9006 9527 1373 64 57 C ATOM 485 CD GLU A 69 49.231 -12.375 18.190 1.00110.56 C ANISOU 485 CD GLU A 69 17242 12156 12610 1590 52 274 C ATOM 486 OE1 GLU A 69 48.234 -11.899 18.771 1.00118.02 O ANISOU 486 OE1 GLU A 69 18295 12964 13583 1851 21 338 O ATOM 487 OE2 GLU A 69 49.393 -12.315 16.953 1.00112.33 O ANISOU 487 OE2 GLU A 69 17500 12480 12701 1511 75 381 O ATOM 488 N LEU A 70 51.116 -16.611 18.344 1.00 53.67 N ANISOU 488 N LEU A 70 8949 5711 5734 1144 50 -240 N ATOM 489 CA LEU A 70 52.113 -17.135 17.415 1.00 50.12 C ANISOU 489 CA LEU A 70 8336 5408 5301 861 111 -323 C ATOM 490 C LEU A 70 51.472 -18.022 16.354 1.00 68.07 C ANISOU 490 C LEU A 70 10374 7945 7546 909 123 -338 C ATOM 491 O LEU A 70 51.837 -17.964 15.180 1.00 62.63 O ANISOU 491 O LEU A 70 9697 7364 6735 744 172 -332 O ATOM 492 CB LEU A 70 53.193 -17.908 18.172 1.00 48.16 C ANISOU 492 CB LEU A 70 7864 5195 5240 703 120 -488 C ATOM 493 CG LEU A 70 54.183 -17.035 18.946 1.00 55.57 C ANISOU 493 CG LEU A 70 8987 5929 6198 562 97 -551 C ATOM 494 CD1 LEU A 70 54.992 -17.867 19.931 1.00 49.27 C ANISOU 494 CD1 LEU A 70 7951 5205 5564 522 41 -702 C ATOM 495 CD2 LEU A 70 55.097 -16.285 17.989 1.00 46.75 C ANISOU 495 CD2 LEU A 70 8003 4719 5039 266 196 -566 C ATOM 496 N LEU A 71 50.518 -18.846 16.774 1.00 60.40 N ANISOU 496 N LEU A 71 9184 7075 6689 1130 97 -380 N ATOM 497 CA LEU A 71 49.780 -19.697 15.849 1.00 59.12 C ANISOU 497 CA LEU A 71 8758 7165 6539 1193 103 -451 C ATOM 498 C LEU A 71 48.923 -18.847 14.917 1.00 72.53 C ANISOU 498 C LEU A 71 10660 8909 7989 1337 14 -321 C ATOM 499 O LEU A 71 48.793 -19.144 13.730 1.00 61.37 O ANISOU 499 O LEU A 71 9145 7727 6445 1284 1 -365 O ATOM 500 CB LEU A 71 48.910 -20.697 16.613 1.00 48.60 C ANISOU 500 CB LEU A 71 7148 5876 5442 1403 134 -538 C ATOM 501 CG LEU A 71 49.658 -21.822 17.329 1.00 61.63 C ANISOU 501 CG LEU A 71 8535 7537 7345 1299 241 -652 C ATOM 502 CD1 LEU A 71 48.708 -22.654 18.174 1.00 55.76 C ANISOU 502 CD1 LEU A 71 7592 6770 6825 1541 322 -685 C ATOM 503 CD2 LEU A 71 50.380 -22.698 16.319 1.00 52.22 C ANISOU 503 CD2 LEU A 71 7064 6546 6232 1049 319 -804 C ATOM 504 N ASN A 72 48.337 -17.790 15.471 1.00 74.78 N ANISOU 504 N ASN A 72 11234 8978 8202 1535 -47 -163 N ATOM 505 CA ASN A 72 47.545 -16.845 14.693 1.00 48.35 C ANISOU 505 CA ASN A 72 8117 5624 4628 1715 -139 8 C ATOM 506 C ASN A 72 48.374 -16.118 13.640 1.00 64.72 C ANISOU 506 C ASN A 72 10447 7692 6453 1517 -97 133 C ATOM 507 O ASN A 72 47.944 -15.959 12.497 1.00 68.36 O ANISOU 507 O ASN A 72 10958 8334 6683 1595 -159 216 O ATOM 508 CB ASN A 72 46.881 -15.826 15.618 1.00 61.28 C ANISOU 508 CB ASN A 72 10016 6973 6294 1947 -175 146 C ATOM 509 CG ASN A 72 46.194 -14.710 14.858 1.00 51.78 C ANISOU 509 CG ASN A 72 9092 5706 4877 2142 -258 365 C ATOM 510 OD1 ASN A 72 45.454 -14.956 13.908 1.00 71.29 O ANISOU 510 OD1 ASN A 72 11448 8417 7222 2292 -366 381 O ATOM 511 ND2 ASN A 72 46.444 -13.472 15.270 1.00 76.54 N ANISOU 511 ND2 ASN A 72 12589 8518 7974 2151 -210 527 N ATOM 512 N SER A 73 49.567 -15.682 14.033 1.00 61.26 N ANISOU 512 N SER A 73 10166 7049 6061 1266 15 136 N ATOM 513 CA SER A 73 50.473 -14.992 13.123 1.00 61.07 C ANISOU 513 CA SER A 73 10386 6962 5857 1038 125 238 C ATOM 514 C SER A 73 50.913 -15.913 11.991 1.00 70.02 C ANISOU 514 C SER A 73 11297 8410 6897 849 175 121 C ATOM 515 O SER A 73 51.122 -15.470 10.861 1.00 73.21 O ANISOU 515 O SER A 73 11893 8880 7042 778 236 243 O ATOM 516 CB SER A 73 51.690 -14.459 13.878 1.00 56.94 C ANISOU 516 CB SER A 73 9993 6156 5485 785 246 184 C ATOM 517 OG SER A 73 51.310 -13.477 14.825 1.00 88.54 O ANISOU 517 OG SER A 73 14236 9862 9543 942 219 274 O ATOM 518 N ALA A 74 51.062 -17.196 12.306 1.00 68.36 N ANISOU 518 N ALA A 74 10693 8383 6898 771 172 -112 N ATOM 519 CA ALA A 74 51.429 -18.194 11.310 1.00 68.07 C ANISOU 519 CA ALA A 74 10389 8646 6828 589 235 -277 C ATOM 520 C ALA A 74 50.318 -18.337 10.278 1.00 63.57 C ANISOU 520 C ALA A 74 9782 8363 6008 800 119 -247 C ATOM 521 O ALA A 74 50.577 -18.450 9.080 1.00 68.03 O ANISOU 521 O ALA A 74 10369 9145 6335 680 165 -266 O ATOM 522 CB ALA A 74 51.719 -19.531 11.974 1.00 60.62 C ANISOU 522 CB ALA A 74 9023 7792 6220 503 271 -520 C ATOM 523 N ILE A 75 49.077 -18.332 10.755 1.00 60.90 N ANISOU 523 N ILE A 75 9379 8038 5722 1120 -31 -220 N ATOM 524 CA ILE A 75 47.920 -18.409 9.875 1.00 63.51 C ANISOU 524 CA ILE A 75 9643 8646 5843 1367 -189 -218 C ATOM 525 C ILE A 75 47.829 -17.147 9.016 1.00 68.31 C ANISOU 525 C ILE A 75 10688 9217 6051 1469 -242 76 C ATOM 526 O ILE A 75 47.531 -17.219 7.824 1.00 68.73 O ANISOU 526 O ILE A 75 10751 9571 5793 1525 -317 85 O ATOM 527 CB ILE A 75 46.617 -18.600 10.677 1.00 67.14 C ANISOU 527 CB ILE A 75 9928 9075 6507 1691 -318 -264 C ATOM 528 CG1 ILE A 75 46.621 -19.957 11.381 1.00 74.54 C ANISOU 528 CG1 ILE A 75 10427 10068 7826 1611 -224 -541 C ATOM 529 CG2 ILE A 75 45.400 -18.486 9.774 1.00 58.28 C ANISOU 529 CG2 ILE A 75 8749 8227 5168 1976 -519 -260 C ATOM 530 CD1 ILE A 75 45.428 -20.173 12.277 1.00 85.28 C ANISOU 530 CD1 ILE A 75 11625 11346 9431 1899 -277 -590 C ATOM 531 N GLU A 76 48.106 -15.995 9.624 1.00 57.27 N ANISOU 531 N GLU A 76 9654 7449 4657 1497 -188 314 N ATOM 532 CA GLU A 76 48.109 -14.725 8.900 1.00 63.74 C ANISOU 532 CA GLU A 76 10925 8147 5148 1590 -177 634 C ATOM 533 C GLU A 76 49.158 -14.709 7.790 1.00 75.65 C ANISOU 533 C GLU A 76 12577 9764 6403 1303 -5 667 C ATOM 534 O GLU A 76 48.927 -14.153 6.715 1.00 88.12 O ANISOU 534 O GLU A 76 14417 11463 7601 1420 -27 879 O ATOM 535 CB GLU A 76 48.354 -13.554 9.858 1.00 63.89 C ANISOU 535 CB GLU A 76 11271 7696 5307 1614 -88 825 C ATOM 536 CG GLU A 76 47.170 -13.203 10.747 1.00 98.35 C ANISOU 536 CG GLU A 76 15623 11921 9823 1959 -241 877 C ATOM 537 CD GLU A 76 47.473 -12.069 11.716 1.00116.55 C ANISOU 537 CD GLU A 76 18241 13765 12279 1951 -129 1015 C ATOM 538 OE1 GLU A 76 48.617 -11.561 11.718 1.00127.34 O ANISOU 538 OE1 GLU A 76 19812 14915 13655 1670 61 1052 O ATOM 539 OE2 GLU A 76 46.560 -11.683 12.477 1.00113.46 O ANISOU 539 OE2 GLU A 76 17872 13220 12017 2217 -218 1057 O ATOM 540 N ALA A 77 50.308 -15.321 8.055 1.00 72.10 N ANISOU 540 N ALA A 77 11959 9273 6164 940 172 463 N ATOM 541 CA ALA A 77 51.399 -15.367 7.084 1.00 62.35 C ANISOU 541 CA ALA A 77 10827 8110 4755 624 383 451 C ATOM 542 C ALA A 77 51.019 -16.202 5.868 1.00 68.72 C ANISOU 542 C ALA A 77 11444 9386 5279 649 313 324 C ATOM 543 O ALA A 77 51.347 -15.853 4.732 1.00 70.18 O ANISOU 543 O ALA A 77 11874 9693 5098 576 418 452 O ATOM 544 CB ALA A 77 52.661 -15.917 7.729 1.00 59.83 C ANISOU 544 CB ALA A 77 10296 7647 4788 254 562 218 C ATOM 545 N VAL A 78 50.323 -17.306 6.116 1.00 61.67 N ANISOU 545 N VAL A 78 10118 8755 4560 750 154 59 N ATOM 546 CA VAL A 78 49.852 -18.179 5.050 1.00 67.53 C ANISOU 546 CA VAL A 78 10610 9964 5084 782 66 -141 C ATOM 547 C VAL A 78 48.844 -17.463 4.156 1.00 71.34 C ANISOU 547 C VAL A 78 11351 10657 5099 1127 -140 85 C ATOM 548 O VAL A 78 48.931 -17.528 2.928 1.00 77.50 O ANISOU 548 O VAL A 78 12225 11750 5471 1098 -133 88 O ATOM 549 CB VAL A 78 49.212 -19.459 5.619 1.00 67.54 C ANISOU 549 CB VAL A 78 10075 10140 5446 841 -38 -484 C ATOM 550 CG1 VAL A 78 48.534 -20.248 4.519 1.00 75.29 C ANISOU 550 CG1 VAL A 78 10788 11609 6208 917 -159 -724 C ATOM 551 CG2 VAL A 78 50.258 -20.304 6.329 1.00 65.31 C ANISOU 551 CG2 VAL A 78 9521 9709 5585 516 168 -700 C ATOM 552 N VAL A 79 47.894 -16.776 4.783 1.00 70.94 N ANISOU 552 N VAL A 79 11416 10437 5100 1466 -322 274 N ATOM 553 CA VAL A 79 46.872 -16.023 4.065 1.00 71.05 C ANISOU 553 CA VAL A 79 11666 10612 4716 1853 -550 518 C ATOM 554 C VAL A 79 47.506 -14.975 3.155 1.00 74.99 C ANISOU 554 C VAL A 79 12699 11024 4771 1814 -405 881 C ATOM 555 O VAL A 79 47.104 -14.811 2.001 1.00 87.69 O ANISOU 555 O VAL A 79 14455 12965 5899 1994 -526 995 O ATOM 556 CB VAL A 79 45.897 -15.333 5.043 1.00 74.95 C ANISOU 556 CB VAL A 79 12224 10831 5421 2195 -711 682 C ATOM 557 CG1 VAL A 79 44.955 -14.401 4.297 1.00 83.10 C ANISOU 557 CG1 VAL A 79 13547 11975 6054 2610 -933 992 C ATOM 558 CG2 VAL A 79 45.114 -16.372 5.831 1.00 67.28 C ANISOU 558 CG2 VAL A 79 10740 9972 4851 2277 -836 336 C ATOM 559 N ASP A 80 48.509 -14.279 3.681 1.00 74.11 N ANISOU 559 N ASP A 80 12871 10466 4821 1580 -134 1051 N ATOM 560 CA ASP A 80 49.220 -13.256 2.925 1.00 84.87 C ANISOU 560 CA ASP A 80 14747 11650 5850 1499 94 1395 C ATOM 561 C ASP A 80 49.956 -13.841 1.720 1.00 79.87 C ANISOU 561 C ASP A 80 14110 11347 4889 1237 254 1277 C ATOM 562 O ASP A 80 50.034 -13.206 0.668 1.00 89.75 O ANISOU 562 O ASP A 80 15754 12685 5661 1324 335 1562 O ATOM 563 CB ASP A 80 50.207 -12.518 3.832 1.00 86.88 C ANISOU 563 CB ASP A 80 15212 11349 6449 1245 377 1494 C ATOM 564 CG ASP A 80 49.515 -11.723 4.924 1.00105.31 C ANISOU 564 CG ASP A 80 17648 13329 9036 1508 261 1649 C ATOM 565 OD1 ASP A 80 48.280 -11.850 5.065 1.00102.05 O ANISOU 565 OD1 ASP A 80 17094 13089 8589 1872 -32 1656 O ATOM 566 OD2 ASP A 80 50.206 -10.973 5.644 1.00121.75 O ANISOU 566 OD2 ASP A 80 19933 14958 11369 1344 472 1733 O ATOM 567 N ARG A 81 50.497 -15.047 1.874 1.00 76.74 N ANISOU 567 N ARG A 81 13282 11126 4749 927 320 868 N ATOM 568 CA ARG A 81 51.178 -15.707 0.768 1.00 78.50 C ANISOU 568 CA ARG A 81 13446 11673 4708 660 486 694 C ATOM 569 C ARG A 81 50.170 -16.053 -0.320 1.00 95.37 C ANISOU 569 C ARG A 81 15528 14357 6350 952 217 655 C ATOM 570 O ARG A 81 50.437 -15.891 -1.510 1.00 88.23 O ANISOU 570 O ARG A 81 14880 13699 4943 920 315 758 O ATOM 571 CB ARG A 81 51.892 -16.973 1.243 1.00 74.45 C ANISOU 571 CB ARG A 81 12433 11211 4643 297 603 247 C ATOM 572 CG ARG A 81 52.589 -17.728 0.128 1.00 76.23 C ANISOU 572 CG ARG A 81 12551 11765 4647 3 794 16 C ATOM 573 CD ARG A 81 53.793 -16.938 -0.348 1.00 84.56 C ANISOU 573 CD ARG A 81 14028 12549 5554 -277 1170 234 C ATOM 574 NE ARG A 81 54.564 -17.645 -1.364 1.00 85.30 N ANISOU 574 NE ARG A 81 14026 12915 5470 -595 1411 -2 N ATOM 575 CZ ARG A 81 54.434 -17.442 -2.669 1.00 95.18 C ANISOU 575 CZ ARG A 81 15562 14485 6116 -532 1466 116 C ATOM 576 NH1 ARG A 81 53.566 -16.544 -3.116 1.00111.18 N ANISOU 576 NH1 ARG A 81 17987 16595 7660 -139 1278 493 N ATOM 577 NH2 ARG A 81 55.174 -18.129 -3.528 1.00107.55 N ANISOU 577 NH2 ARG A 81 17023 16289 7551 -850 1714 -139 N ATOM 578 N ILE A 82 49.009 -16.534 0.111 1.00 95.67 N ANISOU 578 N ILE A 82 15223 14591 6536 1239 -117 486 N ATOM 579 CA ILE A 82 47.902 -16.826 -0.789 1.00 93.55 C ANISOU 579 CA ILE A 82 14841 14847 5856 1566 -438 404 C ATOM 580 C ILE A 82 47.345 -15.541 -1.381 1.00 92.11 C ANISOU 580 C ILE A 82 15185 14647 5164 1956 -574 897 C ATOM 581 O ILE A 82 47.051 -15.464 -2.574 1.00 96.12 O ANISOU 581 O ILE A 82 15858 15570 5092 2124 -692 973 O ATOM 582 CB ILE A 82 46.782 -17.583 -0.061 1.00 98.80 C ANISOU 582 CB ILE A 82 14989 15650 6900 1776 -730 92 C ATOM 583 CG1 ILE A 82 47.287 -18.945 0.407 1.00101.32 C ANISOU 583 CG1 ILE A 82 14784 16015 7699 1419 -577 -385 C ATOM 584 CG2 ILE A 82 45.557 -17.729 -0.954 1.00103.30 C ANISOU 584 CG2 ILE A 82 15439 16748 7065 2158 -1102 4 C ATOM 585 CD1 ILE A 82 46.264 -19.723 1.177 1.00105.20 C ANISOU 585 CD1 ILE A 82 14775 16577 8618 1593 -778 -686 C ATOM 586 N GLY A 83 47.213 -14.527 -0.531 1.00 95.77 N ANISOU 586 N GLY A 83 15918 14627 5844 2109 -549 1232 N ATOM 587 CA GLY A 83 46.680 -13.242 -0.944 1.00100.15 C ANISOU 587 CA GLY A 83 16973 15066 6011 2500 -647 1735 C ATOM 588 C GLY A 83 47.554 -12.554 -1.968 1.00118.07 C ANISOU 588 C GLY A 83 19759 17283 7821 2365 -352 2067 C ATOM 589 O GLY A 83 47.085 -11.691 -2.714 1.00136.43 O ANISOU 589 O GLY A 83 22317 19619 9902 2593 -438 2404 O ATOM 590 N SER A 84 48.829 -12.926 -2.003 1.00119.79 N ANISOU 590 N SER A 84 19989 17373 8153 1891 20 1916 N ATOM 591 CA SER A 84 49.755 -12.369 -2.980 1.00137.86 C ANISOU 591 CA SER A 84 22738 19597 10047 1704 372 2182 C ATOM 592 C SER A 84 49.588 -13.050 -4.330 1.00138.55 C ANISOU 592 C SER A 84 22686 20296 9661 1687 262 2008 C ATOM 593 O SER A 84 49.877 -12.464 -5.374 1.00136.95 O ANISOU 593 O SER A 84 22788 20146 9103 1661 408 2277 O ATOM 594 CB SER A 84 51.200 -12.526 -2.485 1.00142.74 C ANISOU 594 CB SER A 84 23338 19825 11070 1164 821 2026 C ATOM 595 OG SER A 84 51.516 -13.892 -2.275 1.00144.82 O ANISOU 595 OG SER A 84 23044 20353 11627 862 791 1494 O ATOM 596 N GLU A 85 49.125 -14.297 -4.294 1.00132.38 N ANISOU 596 N GLU A 85 21429 19974 8896 1696 15 1535 N ATOM 597 CA GLU A 85 48.865 -15.082 -5.508 1.00147.70 C ANISOU 597 CA GLU A 85 23156 22521 10443 1662 -128 1262 C ATOM 598 C GLU A 85 47.482 -14.874 -6.145 1.00152.78 C ANISOU 598 C GLU A 85 23706 23504 10841 2085 -594 1338 C ATOM 599 O GLU A 85 47.397 -14.641 -7.347 1.00146.63 O ANISOU 599 O GLU A 85 23122 22986 9603 2124 -630 1468 O ATOM 600 CB GLU A 85 49.086 -16.564 -5.209 1.00140.46 C ANISOU 600 CB GLU A 85 21679 21902 9787 1404 -123 647 C ATOM 601 CG GLU A 85 50.497 -16.882 -4.726 1.00131.02 C ANISOU 601 CG GLU A 85 20415 20319 9048 862 332 502 C ATOM 602 CD GLU A 85 51.569 -16.693 -5.785 1.00146.53 C ANISOU 602 CD GLU A 85 22744 22337 10594 573 724 603 C ATOM 603 OE1 GLU A 85 51.295 -16.926 -6.987 1.00163.76 O ANISOU 603 OE1 GLU A 85 25028 25035 12159 678 646 550 O ATOM 604 OE2 GLU A 85 52.690 -16.291 -5.418 1.00140.24 O ANISOU 604 OE2 GLU A 85 22137 21070 10078 242 1120 724 O ATOM 605 N TYR A 86 46.409 -14.966 -5.351 1.00160.12 N ANISOU 605 N TYR A 86 24338 24426 12075 2402 -938 1245 N ATOM 606 CA TYR A 86 45.034 -14.917 -5.877 1.00168.24 C ANISOU 606 CA TYR A 86 25180 25794 12948 2807 -1391 1221 C ATOM 607 C TYR A 86 44.407 -13.527 -5.907 1.00174.57 C ANISOU 607 C TYR A 86 26348 26307 13672 3180 -1514 1763 C ATOM 608 O TYR A 86 43.451 -13.283 -6.648 1.00177.33 O ANISOU 608 O TYR A 86 26669 26941 13767 3503 -1831 1838 O ATOM 609 CB TYR A 86 44.095 -15.819 -5.059 1.00161.61 C ANISOU 609 CB TYR A 86 23749 25133 12521 2965 -1692 775 C ATOM 610 CG TYR A 86 44.243 -17.313 -5.242 1.00158.92 C ANISOU 610 CG TYR A 86 22884 25213 12286 2703 -1693 148 C ATOM 611 CD1 TYR A 86 44.627 -17.858 -6.464 1.00172.44 C ANISOU 611 CD1 TYR A 86 24581 27308 13630 2494 -1628 -54 C ATOM 612 CD2 TYR A 86 43.940 -18.182 -4.207 1.00144.51 C ANISOU 612 CD2 TYR A 86 20557 23392 10957 2673 -1752 -256 C ATOM 613 CE1 TYR A 86 44.730 -19.230 -6.627 1.00173.04 C ANISOU 613 CE1 TYR A 86 24136 27726 13886 2243 -1603 -656 C ATOM 614 CE2 TYR A 86 44.039 -19.545 -4.359 1.00142.80 C ANISOU 614 CE2 TYR A 86 19811 23520 10927 2420 -1719 -844 C ATOM 615 CZ TYR A 86 44.435 -20.066 -5.571 1.00160.55 C ANISOU 615 CZ TYR A 86 22032 26115 12857 2200 -1640 -1048 C ATOM 616 OH TYR A 86 44.538 -21.429 -5.731 1.00161.60 O ANISOU 616 OH TYR A 86 21616 26536 13250 1929 -1571 -1646 O ATOM 617 N HIS A 87 44.941 -12.648 -5.065 1.00174.34 N ANISOU 617 N HIS A 87 26631 25706 13904 3132 -1254 2104 N ATOM 618 CA HIS A 87 44.479 -11.277 -4.886 1.00182.69 C ANISOU 618 CA HIS A 87 28024 26372 15017 3438 -1283 2601 C ATOM 619 C HIS A 87 43.100 -11.291 -4.221 1.00190.10 C ANISOU 619 C HIS A 87 28635 27351 16246 3838 -1682 2495 C ATOM 620 O HIS A 87 42.183 -10.608 -4.671 1.00197.28 O ANISOU 620 O HIS A 87 29617 28321 17021 4200 -1922 2725 O ATOM 621 CB HIS A 87 44.395 -10.534 -6.224 1.00186.38 C ANISOU 621 CB HIS A 87 28841 26999 14977 3578 -1293 2957 C ATOM 622 CG HIS A 87 45.673 -10.518 -6.999 1.00188.80 C ANISOU 622 CG HIS A 87 29463 27304 14970 3203 -893 3057 C ATOM 623 ND1 HIS A 87 45.807 -9.829 -8.184 1.00196.07 N ANISOU 623 ND1 HIS A 87 30754 28322 15422 3277 -812 3406 N ATOM 624 CD2 HIS A 87 46.867 -11.117 -6.775 1.00186.17 C ANISOU 624 CD2 HIS A 87 29118 26890 14728 2755 -536 2844 C ATOM 625 CE1 HIS A 87 47.028 -10.005 -8.657 1.00195.25 C ANISOU 625 CE1 HIS A 87 30850 28196 15142 2882 -409 3398 C ATOM 626 NE2 HIS A 87 47.692 -10.781 -7.820 1.00189.25 N ANISOU 626 NE2 HIS A 87 29854 27326 14728 2556 -233 3052 N ATOM 627 N GLU A 88 42.957 -12.073 -3.155 1.00186.52 N ANISOU 627 N GLU A 88 27814 26861 16193 3774 -1738 2141 N ATOM 628 CA GLU A 88 41.679 -12.217 -2.456 1.00189.14 C ANISOU 628 CA GLU A 88 27785 27234 16847 4119 -2077 1978 C ATOM 629 C GLU A 88 41.745 -11.581 -1.065 1.00184.81 C ANISOU 629 C GLU A 88 27357 26096 16765 4151 -1931 2150 C ATOM 630 O GLU A 88 42.689 -11.840 -0.323 1.00182.08 O ANISOU 630 O GLU A 88 27080 25491 16612 3848 -1660 2080 O ATOM 631 CB GLU A 88 41.289 -13.692 -2.365 1.00190.46 C ANISOU 631 CB GLU A 88 27368 27869 17128 4056 -2275 1383 C ATOM 632 CG GLU A 88 39.838 -13.977 -2.721 1.00194.87 C ANISOU 632 CG GLU A 88 27531 28811 17701 4431 -2701 1159 C ATOM 633 CD GLU A 88 39.295 -15.222 -2.042 1.00192.23 C ANISOU 633 CD GLU A 88 26578 28710 17749 4416 -2848 588 C ATOM 634 OE1 GLU A 88 39.898 -16.300 -2.215 1.00194.51 O ANISOU 634 OE1 GLU A 88 26616 29264 18026 4102 -2735 203 O ATOM 635 OE2 GLU A 88 38.260 -15.130 -1.346 1.00188.64 O ANISOU 635 OE2 GLU A 88 25871 28166 17638 4708 -3051 507 O ATOM 636 N LEU A 89 40.755 -10.769 -0.693 1.00189.45 N ANISOU 636 N LEU A 89 27963 26472 17547 4504 -2103 2350 N ATOM 637 CA LEU A 89 40.774 -10.154 0.637 1.00189.73 C ANISOU 637 CA LEU A 89 28102 25944 18040 4524 -1956 2480 C ATOM 638 C LEU A 89 39.721 -10.669 1.630 1.00191.51 C ANISOU 638 C LEU A 89 27896 26189 18678 4744 -2191 2181 C ATOM 639 O LEU A 89 39.308 -9.916 2.515 1.00196.39 O ANISOU 639 O LEU A 89 28597 26385 19637 4888 -2149 2335 O ATOM 640 CB LEU A 89 40.574 -8.641 0.502 1.00191.68 C ANISOU 640 CB LEU A 89 28747 25792 18290 4712 -1864 2960 C ATOM 641 CG LEU A 89 41.688 -7.698 0.065 1.00189.30 C ANISOU 641 CG LEU A 89 28956 25157 17812 4495 -1497 3347 C ATOM 642 CD1 LEU A 89 41.163 -6.282 0.141 1.00190.48 C ANISOU 642 CD1 LEU A 89 29369 24920 18086 4759 -1463 3743 C ATOM 643 CD2 LEU A 89 42.898 -7.853 0.968 1.00176.84 C ANISOU 643 CD2 LEU A 89 27502 23204 16484 4101 -1143 3268 C ATOM 644 N SER A 90 39.306 -11.930 1.535 1.00189.16 N ANISOU 644 N SER A 90 27128 26352 18393 4752 -2402 1733 N ATOM 645 CA SER A 90 38.355 -12.459 2.514 1.00178.96 C ANISOU 645 CA SER A 90 25407 25051 17537 4943 -2577 1430 C ATOM 646 C SER A 90 39.055 -12.628 3.860 1.00167.46 C ANISOU 646 C SER A 90 23984 23159 16484 4690 -2302 1376 C ATOM 647 O SER A 90 40.221 -13.014 3.918 1.00175.60 O ANISOU 647 O SER A 90 25085 24109 17525 4263 -2025 1307 O ATOM 648 CB SER A 90 37.722 -13.761 2.027 1.00175.43 C ANISOU 648 CB SER A 90 24397 25199 17060 4994 -2842 920 C ATOM 649 OG SER A 90 36.906 -13.492 0.900 1.00181.55 O ANISOU 649 OG SER A 90 25113 26316 17552 5241 -3104 954 O ATOM 650 N GLY A 91 38.341 -12.347 4.939 1.00147.48 N ANISOU 650 N GLY A 91 21336 20309 14390 4864 -2322 1358 N ATOM 651 CA GLY A 91 38.949 -12.278 6.257 1.00117.97 C ANISOU 651 CA GLY A 91 17653 16080 11090 4585 -2015 1332 C ATOM 652 C GLY A 91 38.738 -13.350 7.309 1.00101.23 C ANISOU 652 C GLY A 91 15061 13927 9474 4415 -1928 913 C ATOM 653 O GLY A 91 39.332 -13.266 8.390 1.00106.66 O ANISOU 653 O GLY A 91 15839 14231 10457 4192 -1679 917 O ATOM 654 N ARG A 92 37.900 -14.341 7.034 1.00 93.96 N ANISOU 654 N ARG A 92 14319 12823 8558 5566 -1281 -1086 N ATOM 655 CA ARG A 92 37.536 -15.335 8.050 1.00112.26 C ANISOU 655 CA ARG A 92 16354 15096 11203 5191 -1310 -1344 C ATOM 656 C ARG A 92 38.717 -16.070 8.688 1.00 94.02 C ANISOU 656 C ARG A 92 14107 12475 9142 4912 -1032 -1257 C ATOM 657 O ARG A 92 38.700 -16.302 9.897 1.00109.98 O ANISOU 657 O ARG A 92 15955 14346 11485 4652 -966 -1272 O ATOM 658 CB ARG A 92 36.562 -16.356 7.460 1.00121.12 C ANISOU 658 CB ARG A 92 17335 16511 12176 5118 -1569 -1760 C ATOM 659 CG ARG A 92 35.992 -17.321 8.494 1.00136.40 C ANISOU 659 CG ARG A 92 18988 18408 14429 4699 -1602 -2029 C ATOM 660 CD ARG A 92 34.950 -18.239 7.896 1.00149.85 C ANISOU 660 CD ARG A 92 20541 20416 15979 4559 -1870 -2458 C ATOM 661 NE ARG A 92 33.720 -17.495 7.654 1.00161.45 N ANISOU 661 NE ARG A 92 21729 22325 17291 4771 -2159 -2557 N ATOM 662 CZ ARG A 92 32.633 -18.001 7.089 1.00178.24 C ANISOU 662 CZ ARG A 92 23624 24861 19238 4699 -2458 -2926 C ATOM 663 NH1 ARG A 92 32.610 -19.264 6.683 1.00180.12 N ANISOU 663 NH1 ARG A 92 23936 25070 19431 4378 -2505 -3249 N ATOM 664 NH2 ARG A 92 31.564 -17.233 6.928 1.00180.60 N ANISOU 664 NH2 ARG A 92 23624 25610 19385 4960 -2714 -2980 N ATOM 665 N ALA A 93 39.719 -16.457 7.906 1.00 84.92 N ANISOU 665 N ALA A 93 13189 11255 7821 4996 -869 -1169 N ATOM 666 CA ALA A 93 40.885 -17.128 8.485 1.00 77.29 C ANISOU 666 CA ALA A 93 12260 10049 7059 4810 -605 -1070 C ATOM 667 C ALA A 93 41.564 -16.225 9.519 1.00 81.67 C ANISOU 667 C ALA A 93 12737 10426 7866 4709 -432 -756 C ATOM 668 O ALA A 93 41.952 -16.668 10.605 1.00 82.92 O ANISOU 668 O ALA A 93 12771 10428 8306 4482 -329 -746 O ATOM 669 CB ALA A 93 41.872 -17.518 7.396 1.00 70.87 C ANISOU 669 CB ALA A 93 11695 9256 5977 4997 -438 -994 C ATOM 670 N LYS A 94 41.701 -14.944 9.174 1.00 67.14 N ANISOU 670 N LYS A 94 11008 8601 5901 4877 -403 -501 N ATOM 671 CA LYS A 94 42.273 -13.961 10.081 1.00 85.03 C ANISOU 671 CA LYS A 94 13251 10682 8373 4753 -262 -228 C ATOM 672 C LYS A 94 41.295 -13.598 11.204 1.00 86.85 C ANISOU 672 C LYS A 94 13302 10866 8830 4648 -417 -335 C ATOM 673 O LYS A 94 41.712 -13.328 12.331 1.00 79.22 O ANISOU 673 O LYS A 94 12249 9735 8117 4444 -319 -233 O ATOM 674 CB LYS A 94 42.701 -12.705 9.320 1.00 67.30 C ANISOU 674 CB LYS A 94 11260 8407 5905 4937 -161 75 C ATOM 675 CG LYS A 94 43.999 -12.875 8.552 1.00 84.76 C ANISOU 675 CG LYS A 94 13602 10641 7963 4953 100 276 C ATOM 676 CD LYS A 94 44.477 -11.566 7.955 1.00 96.01 C ANISOU 676 CD LYS A 94 15291 11990 9198 5046 250 615 C ATOM 677 CE LYS A 94 45.882 -11.714 7.395 1.00 99.18 C ANISOU 677 CE LYS A 94 15741 12447 9496 4982 563 839 C ATOM 678 NZ LYS A 94 46.322 -10.498 6.659 1.00 98.90 N ANISOU 678 NZ LYS A 94 16004 12342 9231 5046 741 1178 N ATOM 679 N ASP A 95 39.998 -13.588 10.897 1.00 78.29 N ANISOU 679 N ASP A 95 12142 9970 7634 4798 -661 -546 N ATOM 680 CA ASP A 95 38.978 -13.306 11.909 1.00 68.10 C ANISOU 680 CA ASP A 95 10637 8709 6527 4736 -799 -669 C ATOM 681 C ASP A 95 38.930 -14.394 12.978 1.00 71.56 C ANISOU 681 C ASP A 95 10848 9089 7253 4403 -761 -848 C ATOM 682 O ASP A 95 38.908 -14.105 14.175 1.00 80.43 O ANISOU 682 O ASP A 95 11864 10089 8606 4254 -706 -797 O ATOM 683 CB ASP A 95 37.594 -13.161 11.266 1.00 86.23 C ANISOU 683 CB ASP A 95 12830 11322 8613 4987 -1075 -876 C ATOM 684 CG ASP A 95 37.457 -11.889 10.452 1.00 96.56 C ANISOU 684 CG ASP A 95 14386 12666 9635 5385 -1127 -669 C ATOM 685 OD1 ASP A 95 38.204 -10.926 10.720 1.00106.98 O ANISOU 685 OD1 ASP A 95 15941 13711 10994 5408 -952 -373 O ATOM 686 OD2 ASP A 95 36.599 -11.852 9.544 1.00 84.56 O ANISOU 686 OD2 ASP A 95 12844 11449 7836 5668 -1346 -802 O ATOM 687 N LEU A 96 38.908 -15.645 12.532 1.00 70.80 N ANISOU 687 N LEU A 96 10726 9059 7117 4297 -783 -1057 N ATOM 688 CA LEU A 96 38.874 -16.784 13.440 1.00 75.65 C ANISOU 688 CA LEU A 96 11208 9569 7965 3989 -726 -1217 C ATOM 689 C LEU A 96 40.131 -16.875 14.297 1.00 82.33 C ANISOU 689 C LEU A 96 12117 10163 9003 3863 -491 -995 C ATOM 690 O LEU A 96 40.057 -17.203 15.480 1.00 77.65 O ANISOU 690 O LEU A 96 11404 9463 8636 3659 -439 -1017 O ATOM 691 CB LEU A 96 38.679 -18.083 12.661 1.00 63.64 C ANISOU 691 CB LEU A 96 9754 8104 6323 3914 -782 -1483 C ATOM 692 CG LEU A 96 37.305 -18.253 12.017 1.00 66.58 C ANISOU 692 CG LEU A 96 9980 8779 6538 3928 -1050 -1786 C ATOM 693 CD1 LEU A 96 37.325 -19.422 11.057 1.00 81.61 C ANISOU 693 CD1 LEU A 96 12044 10702 8262 3867 -1101 -2040 C ATOM 694 CD2 LEU A 96 36.230 -18.436 13.076 1.00 66.45 C ANISOU 694 CD2 LEU A 96 9655 8854 6741 3673 -1130 -1953 C ATOM 695 N GLY A 97 41.283 -16.594 13.695 1.00 69.97 N ANISOU 695 N GLY A 97 10718 8543 7325 3989 -348 -782 N ATOM 696 CA GLY A 97 42.539 -16.597 14.423 1.00 68.11 C ANISOU 696 CA GLY A 97 10484 8159 7238 3888 -142 -567 C ATOM 697 C GLY A 97 42.572 -15.532 15.503 1.00 72.97 C ANISOU 697 C GLY A 97 11011 8690 8024 3784 -132 -412 C ATOM 698 O GLY A 97 43.061 -15.769 16.608 1.00 67.48 O ANISOU 698 O GLY A 97 10223 7898 7518 3619 -50 -358 O ATOM 699 N SER A 98 42.051 -14.354 15.178 1.00 61.19 N ANISOU 699 N SER A 98 9585 7227 6437 3909 -219 -343 N ATOM 700 CA SER A 98 41.961 -13.261 16.138 1.00 76.51 C ANISOU 700 CA SER A 98 11516 9049 8504 3841 -221 -227 C ATOM 701 C SER A 98 40.967 -13.597 17.244 1.00 76.31 C ANISOU 701 C SER A 98 11304 9042 8650 3739 -320 -417 C ATOM 702 O SER A 98 41.148 -13.200 18.395 1.00 66.50 O ANISOU 702 O SER A 98 10018 7685 7563 3607 -276 -358 O ATOM 703 CB SER A 98 41.560 -11.963 15.440 1.00 72.78 C ANISOU 703 CB SER A 98 11239 8564 7850 4064 -283 -113 C ATOM 704 OG SER A 98 42.665 -11.378 14.773 1.00 89.62 O ANISOU 704 OG SER A 98 13571 10614 9868 4067 -126 139 O ATOM 705 N ALA A 99 39.914 -14.325 16.887 1.00 75.53 N ANISOU 705 N ALA A 99 11088 9106 8503 3780 -449 -655 N ATOM 706 CA ALA A 99 38.904 -14.736 17.854 1.00 70.61 C ANISOU 706 CA ALA A 99 10252 8549 8026 3649 -517 -842 C ATOM 707 C ALA A 99 39.504 -15.698 18.869 1.00 74.58 C ANISOU 707 C ALA A 99 10708 8908 8719 3392 -380 -840 C ATOM 708 O ALA A 99 39.173 -15.654 20.054 1.00 69.22 O ANISOU 708 O ALA A 99 9922 8192 8186 3267 -353 -860 O ATOM 709 CB ALA A 99 37.718 -15.376 17.151 1.00 57.53 C ANISOU 709 CB ALA A 99 8452 7139 6265 3682 -680 -1108 C ATOM 710 N ALA A 100 40.385 -16.571 18.393 1.00 68.53 N ANISOU 710 N ALA A 100 10047 8070 7923 3356 -286 -810 N ATOM 711 CA ALA A 100 41.057 -17.531 19.257 1.00 68.34 C ANISOU 711 CA ALA A 100 10028 7902 8034 3194 -151 -782 C ATOM 712 C ALA A 100 41.924 -16.818 20.290 1.00 71.94 C ANISOU 712 C ALA A 100 10464 8274 8596 3150 -66 -569 C ATOM 713 O ALA A 100 41.993 -17.230 21.447 1.00 76.77 O ANISOU 713 O ALA A 100 11023 8814 9334 3020 -11 -564 O ATOM 714 CB ALA A 100 41.896 -18.492 18.432 1.00 67.31 C ANISOU 714 CB ALA A 100 10045 7722 7806 3262 -62 -778 C ATOM 715 N VAL A 101 42.585 -15.747 19.861 1.00 65.15 N ANISOU 715 N VAL A 101 9665 7423 7666 3240 -53 -396 N ATOM 716 CA VAL A 101 43.437 -14.967 20.750 1.00 65.11 C ANISOU 716 CA VAL A 101 9646 7351 7742 3145 8 -218 C ATOM 717 C VAL A 101 42.600 -14.245 21.801 1.00 68.64 C ANISOU 717 C VAL A 101 10056 7750 8276 3085 -67 -277 C ATOM 718 O VAL A 101 42.987 -14.165 22.969 1.00 67.46 O ANISOU 718 O VAL A 101 9862 7547 8222 2959 -32 -232 O ATOM 719 CB VAL A 101 44.280 -13.941 19.967 1.00 59.45 C ANISOU 719 CB VAL A 101 9032 6634 6920 3190 58 -26 C ATOM 720 CG1 VAL A 101 45.142 -13.120 20.916 1.00 59.16 C ANISOU 720 CG1 VAL A 101 8975 6533 6969 3013 106 124 C ATOM 721 CG2 VAL A 101 45.146 -14.644 18.934 1.00 66.94 C ANISOU 721 CG2 VAL A 101 9999 7676 7757 3279 163 41 C ATOM 722 N LEU A 102 41.446 -13.734 21.380 1.00 64.16 N ANISOU 722 N LEU A 102 9500 7232 7646 3211 -173 -386 N ATOM 723 CA LEU A 102 40.539 -13.025 22.278 1.00 63.29 C ANISOU 723 CA LEU A 102 9351 7112 7584 3230 -234 -457 C ATOM 724 C LEU A 102 40.086 -13.914 23.431 1.00 63.62 C ANISOU 724 C LEU A 102 9235 7187 7750 3078 -198 -573 C ATOM 725 O LEU A 102 40.138 -13.511 24.593 1.00 62.34 O ANISOU 725 O LEU A 102 9071 6962 7652 3010 -169 -546 O ATOM 726 CB LEU A 102 39.318 -12.508 21.516 1.00 55.25 C ANISOU 726 CB LEU A 102 8322 6225 6448 3460 -359 -567 C ATOM 727 CG LEU A 102 38.290 -11.774 22.382 1.00 66.15 C ANISOU 727 CG LEU A 102 9641 7645 7849 3562 -412 -652 C ATOM 728 CD1 LEU A 102 38.901 -10.523 22.997 1.00 60.89 C ANISOU 728 CD1 LEU A 102 9209 6744 7182 3579 -369 -503 C ATOM 729 CD2 LEU A 102 37.028 -11.439 21.599 1.00 58.19 C ANISOU 729 CD2 LEU A 102 8545 6862 6703 3840 -551 -777 C ATOM 730 N ILE A 103 39.647 -15.125 23.098 1.00 62.88 N ANISOU 730 N ILE A 103 9046 7175 7672 3014 -192 -703 N ATOM 731 CA ILE A 103 39.189 -16.083 24.097 1.00 70.70 C ANISOU 731 CA ILE A 103 9932 8165 8764 2836 -124 -798 C ATOM 732 C ILE A 103 40.311 -16.425 25.075 1.00 63.10 C ANISOU 732 C ILE A 103 9049 7060 7868 2739 -14 -649 C ATOM 733 O ILE A 103 40.074 -16.589 26.272 1.00 64.88 O ANISOU 733 O ILE A 103 9235 7264 8152 2643 41 -655 O ATOM 734 CB ILE A 103 38.668 -17.377 23.434 1.00 61.21 C ANISOU 734 CB ILE A 103 8692 7009 7554 2733 -122 -962 C ATOM 735 CG1 ILE A 103 37.538 -17.054 22.456 1.00 59.74 C ANISOU 735 CG1 ILE A 103 8378 7044 7275 2828 -270 -1133 C ATOM 736 CG2 ILE A 103 38.182 -18.366 24.479 1.00 61.19 C ANISOU 736 CG2 ILE A 103 8634 6961 7653 2505 -17 -1038 C ATOM 737 CD1 ILE A 103 36.368 -16.341 23.096 1.00 65.36 C ANISOU 737 CD1 ILE A 103 8883 7946 8006 2872 -325 -1220 C ATOM 738 N ALA A 104 41.534 -16.513 24.562 1.00 64.00 N ANISOU 738 N ALA A 104 9254 7117 7946 2785 20 -513 N ATOM 739 CA ALA A 104 42.702 -16.774 25.396 1.00 64.16 C ANISOU 739 CA ALA A 104 9300 7082 7997 2738 98 -365 C ATOM 740 C ALA A 104 42.944 -15.625 26.367 1.00 65.09 C ANISOU 740 C ALA A 104 9403 7196 8133 2690 61 -293 C ATOM 741 O ALA A 104 43.292 -15.841 27.528 1.00 72.43 O ANISOU 741 O ALA A 104 10318 8115 9087 2623 92 -250 O ATOM 742 CB ALA A 104 43.933 -17.004 24.534 1.00 47.90 C ANISOU 742 CB ALA A 104 7279 5045 5875 2824 145 -240 C ATOM 743 N ILE A 105 42.761 -14.403 25.880 1.00 57.97 N ANISOU 743 N ILE A 105 8548 6284 7194 2737 -7 -283 N ATOM 744 CA ILE A 105 42.939 -13.222 26.711 1.00 56.32 C ANISOU 744 CA ILE A 105 8403 6013 6985 2682 -45 -243 C ATOM 745 C ILE A 105 41.850 -13.144 27.775 1.00 66.87 C ANISOU 745 C ILE A 105 9712 7352 8345 2693 -57 -370 C ATOM 746 O ILE A 105 42.134 -12.873 28.941 1.00 62.75 O ANISOU 746 O ILE A 105 9216 6802 7825 2615 -52 -355 O ATOM 747 CB ILE A 105 42.935 -11.937 25.867 1.00 57.49 C ANISOU 747 CB ILE A 105 8696 6081 7067 2750 -92 -195 C ATOM 748 CG1 ILE A 105 44.178 -11.889 24.977 1.00 58.45 C ANISOU 748 CG1 ILE A 105 8839 6218 7152 2690 -41 -38 C ATOM 749 CG2 ILE A 105 42.881 -10.709 26.760 1.00 57.30 C ANISOU 749 CG2 ILE A 105 8816 5924 7032 2700 -130 -201 C ATOM 750 CD1 ILE A 105 44.221 -10.692 24.058 1.00 68.63 C ANISOU 750 CD1 ILE A 105 10323 7399 8355 2738 -50 45 C ATOM 751 N ILE A 106 40.606 -13.387 27.370 1.00 64.75 N ANISOU 751 N ILE A 106 9369 7159 8073 2789 -73 -501 N ATOM 752 CA ILE A 106 39.484 -13.426 28.304 1.00 67.96 C ANISOU 752 CA ILE A 106 9687 7641 8495 2801 -52 -624 C ATOM 753 C ILE A 106 39.707 -14.475 29.389 1.00 72.64 C ANISOU 753 C ILE A 106 10234 8233 9133 2647 50 -606 C ATOM 754 O ILE A 106 39.455 -14.227 30.569 1.00 68.93 O ANISOU 754 O ILE A 106 9773 7772 8646 2626 88 -624 O ATOM 755 CB ILE A 106 38.155 -13.723 27.581 1.00 62.97 C ANISOU 755 CB ILE A 106 8895 7178 7851 2890 -85 -776 C ATOM 756 CG1 ILE A 106 37.802 -12.584 26.625 1.00 61.74 C ANISOU 756 CG1 ILE A 106 8809 7045 7604 3126 -196 -784 C ATOM 757 CG2 ILE A 106 37.027 -13.926 28.583 1.00 58.07 C ANISOU 757 CG2 ILE A 106 8114 6702 7249 2862 -23 -897 C ATOM 758 CD1 ILE A 106 36.547 -12.837 25.825 1.00 64.31 C ANISOU 758 CD1 ILE A 106 8938 7615 7882 3251 -270 -940 C ATOM 759 N ASP A 107 40.186 -15.644 28.977 1.00 62.90 N ANISOU 759 N ASP A 107 8994 6975 7931 2569 102 -566 N ATOM 760 CA ASP A 107 40.490 -16.730 29.903 1.00 62.92 C ANISOU 760 CA ASP A 107 9025 6931 7950 2465 211 -516 C ATOM 761 C ASP A 107 41.557 -16.328 30.917 1.00 72.64 C ANISOU 761 C ASP A 107 10326 8137 9137 2470 200 -386 C ATOM 762 O ASP A 107 41.459 -16.655 32.100 1.00 75.30 O ANISOU 762 O ASP A 107 10692 8477 9443 2431 264 -366 O ATOM 763 CB ASP A 107 40.944 -17.974 29.138 1.00 65.47 C ANISOU 763 CB ASP A 107 9406 7181 8288 2443 267 -489 C ATOM 764 CG ASP A 107 41.477 -19.057 30.055 1.00 94.29 C ANISOU 764 CG ASP A 107 13167 10735 11924 2405 384 -391 C ATOM 765 OD1 ASP A 107 40.669 -19.660 30.791 1.00103.77 O ANISOU 765 OD1 ASP A 107 14389 11902 13138 2289 486 -440 O ATOM 766 OD2 ASP A 107 42.701 -19.307 30.040 1.00104.55 O ANISOU 766 OD2 ASP A 107 14531 12012 13182 2505 385 -254 O ATOM 767 N ALA A 108 42.578 -15.622 30.443 1.00 62.92 N ANISOU 767 N ALA A 108 9116 6904 7886 2501 120 -301 N ATOM 768 CA ALA A 108 43.667 -15.175 31.303 1.00 60.94 C ANISOU 768 CA ALA A 108 8886 6684 7585 2461 77 -202 C ATOM 769 C ALA A 108 43.184 -14.127 32.308 1.00 70.63 C ANISOU 769 C ALA A 108 10175 7892 8769 2428 28 -279 C ATOM 770 O ALA A 108 43.657 -14.084 33.443 1.00 65.92 O ANISOU 770 O ALA A 108 9607 7338 8104 2386 9 -250 O ATOM 771 CB ALA A 108 44.813 -14.634 30.466 1.00 47.37 C ANISOU 771 CB ALA A 108 7139 4999 5859 2439 21 -105 C ATOM 772 N VAL A 109 42.244 -13.285 31.884 1.00 72.21 N ANISOU 772 N VAL A 109 10414 8041 8982 2484 3 -381 N ATOM 773 CA VAL A 109 41.665 -12.271 32.764 1.00 68.17 C ANISOU 773 CA VAL A 109 10003 7490 8408 2518 -26 -474 C ATOM 774 C VAL A 109 40.858 -12.937 33.873 1.00 67.89 C ANISOU 774 C VAL A 109 9916 7540 8340 2538 72 -533 C ATOM 775 O VAL A 109 40.965 -12.567 35.044 1.00 62.36 O ANISOU 775 O VAL A 109 9302 6843 7547 2527 69 -556 O ATOM 776 CB VAL A 109 40.756 -11.290 31.989 1.00 58.45 C ANISOU 776 CB VAL A 109 8837 6198 7172 2666 -61 -560 C ATOM 777 CG1 VAL A 109 40.000 -10.383 32.950 1.00 50.65 C ANISOU 777 CG1 VAL A 109 7969 5175 6101 2777 -60 -674 C ATOM 778 CG2 VAL A 109 41.574 -10.467 31.011 1.00 50.60 C ANISOU 778 CG2 VAL A 109 7973 5077 6177 2634 -132 -477 C ATOM 779 N ILE A 110 40.054 -13.925 33.492 1.00 62.32 N ANISOU 779 N ILE A 110 9081 6904 7693 2541 165 -563 N ATOM 780 CA ILE A 110 39.260 -14.693 34.444 1.00 65.84 C ANISOU 780 CA ILE A 110 9471 7431 8114 2502 303 -597 C ATOM 781 C ILE A 110 40.161 -15.404 35.450 1.00 69.07 C ANISOU 781 C ILE A 110 9976 7811 8455 2437 349 -473 C ATOM 782 O ILE A 110 39.906 -15.376 36.655 1.00 68.03 O ANISOU 782 O ILE A 110 9900 7725 8222 2445 416 -477 O ATOM 783 CB ILE A 110 38.373 -15.730 33.726 1.00 67.92 C ANISOU 783 CB ILE A 110 9588 7755 8463 2427 395 -653 C ATOM 784 CG1 ILE A 110 37.290 -15.027 32.905 1.00 68.04 C ANISOU 784 CG1 ILE A 110 9456 7895 8501 2532 337 -795 C ATOM 785 CG2 ILE A 110 37.744 -16.687 34.726 1.00 52.78 C ANISOU 785 CG2 ILE A 110 7646 5885 6521 2306 578 -648 C ATOM 786 CD1 ILE A 110 36.387 -15.975 32.144 1.00 70.03 C ANISOU 786 CD1 ILE A 110 9522 8263 8822 2418 388 -891 C ATOM 787 N THR A 111 41.214 -16.038 34.940 1.00 68.10 N ANISOU 787 N THR A 111 9876 7637 8362 2415 316 -358 N ATOM 788 CA THR A 111 42.183 -16.742 35.773 1.00 59.86 C ANISOU 788 CA THR A 111 8913 6602 7230 2427 336 -220 C ATOM 789 C THR A 111 42.794 -15.816 36.821 1.00 60.26 C ANISOU 789 C THR A 111 9016 6727 7153 2441 227 -219 C ATOM 790 O THR A 111 42.820 -16.141 38.007 1.00 63.08 O ANISOU 790 O THR A 111 9453 7134 7380 2469 273 -179 O ATOM 791 CB THR A 111 43.316 -17.356 34.924 1.00 50.12 C ANISOU 791 CB THR A 111 7663 5351 6031 2471 298 -106 C ATOM 792 OG1 THR A 111 42.795 -18.425 34.126 1.00 63.49 O ANISOU 792 OG1 THR A 111 9380 6940 7802 2459 412 -118 O ATOM 793 CG2 THR A 111 44.425 -17.893 35.814 1.00 50.11 C ANISOU 793 CG2 THR A 111 7712 5425 5902 2557 281 40 C ATOM 794 N TRP A 112 43.272 -14.658 36.380 1.00 56.02 N ANISOU 794 N TRP A 112 8465 6185 6635 2405 85 -267 N ATOM 795 CA TRP A 112 43.886 -13.700 37.291 1.00 64.82 C ANISOU 795 CA TRP A 112 9655 7345 7627 2357 -39 -303 C ATOM 796 C TRP A 112 42.875 -13.123 38.276 1.00 82.53 C ANISOU 796 C TRP A 112 12020 9565 9773 2405 6 -432 C ATOM 797 O TRP A 112 43.202 -12.894 39.437 1.00 80.56 O ANISOU 797 O TRP A 112 11864 9382 9363 2401 -42 -454 O ATOM 798 CB TRP A 112 44.562 -12.574 36.508 1.00 55.27 C ANISOU 798 CB TRP A 112 8452 6081 6469 2248 -170 -330 C ATOM 799 CG TRP A 112 45.960 -12.903 36.091 1.00 51.23 C ANISOU 799 CG TRP A 112 7802 5698 5967 2172 -242 -202 C ATOM 800 CD1 TRP A 112 46.345 -13.837 35.174 1.00 56.12 C ANISOU 800 CD1 TRP A 112 8295 6367 6663 2242 -178 -87 C ATOM 801 CD2 TRP A 112 47.164 -12.296 36.575 1.00 60.15 C ANISOU 801 CD2 TRP A 112 8884 6962 7010 2016 -388 -191 C ATOM 802 NE1 TRP A 112 47.715 -13.852 35.060 1.00 56.43 N ANISOU 802 NE1 TRP A 112 8187 6589 6664 2182 -259 11 N ATOM 803 CE2 TRP A 112 48.241 -12.914 35.909 1.00 58.13 C ANISOU 803 CE2 TRP A 112 8419 6882 6787 2018 -395 -51 C ATOM 804 CE3 TRP A 112 47.435 -11.290 37.508 1.00 58.97 C ANISOU 804 CE3 TRP A 112 8846 6817 6743 1865 -517 -304 C ATOM 805 CZ2 TRP A 112 49.567 -12.559 36.145 1.00 65.95 C ANISOU 805 CZ2 TRP A 112 9242 8110 7706 1863 -526 -11 C ATOM 806 CZ3 TRP A 112 48.752 -10.939 37.742 1.00 68.78 C ANISOU 806 CZ3 TRP A 112 9957 8259 7918 1666 -664 -282 C ATOM 807 CH2 TRP A 112 49.802 -11.572 37.063 1.00 74.69 C ANISOU 807 CH2 TRP A 112 10430 9237 8711 1661 -667 -131 C ATOM 808 N CYS A 113 41.650 -12.888 37.815 1.00 68.66 N ANISOU 808 N CYS A 113 10248 7753 8089 2474 94 -525 N ATOM 809 CA CYS A 113 40.609 -12.364 38.693 1.00 63.45 C ANISOU 809 CA CYS A 113 9666 7116 7325 2573 168 -648 C ATOM 810 C CYS A 113 40.232 -13.358 39.782 1.00 75.15 C ANISOU 810 C CYS A 113 11137 8713 8704 2584 323 -595 C ATOM 811 O CYS A 113 40.283 -13.032 40.964 1.00 78.62 O ANISOU 811 O CYS A 113 11706 9202 8965 2628 325 -631 O ATOM 812 CB CYS A 113 39.366 -11.980 37.891 1.00 62.02 C ANISOU 812 CB CYS A 113 9401 6932 7232 2687 230 -750 C ATOM 813 SG CYS A 113 39.478 -10.368 37.097 1.00 77.61 S ANISOU 813 SG CYS A 113 11544 8728 9216 2779 81 -838 S ATOM 814 N ILE A 114 39.873 -14.573 39.380 1.00 66.53 N ANISOU 814 N ILE A 114 9929 7643 7706 2534 459 -509 N ATOM 815 CA ILE A 114 39.445 -15.601 40.325 1.00 68.50 C ANISOU 815 CA ILE A 114 10212 7954 7862 2511 650 -431 C ATOM 816 C ILE A 114 40.521 -15.919 41.360 1.00 73.78 C ANISOU 816 C ILE A 114 11041 8643 8350 2547 597 -307 C ATOM 817 O ILE A 114 40.240 -15.994 42.557 1.00 83.37 O ANISOU 817 O ILE A 114 12365 9933 9377 2598 691 -294 O ATOM 818 CB ILE A 114 39.052 -16.902 39.596 1.00 65.67 C ANISOU 818 CB ILE A 114 9770 7540 7641 2396 794 -358 C ATOM 819 CG1 ILE A 114 37.762 -16.697 38.803 1.00 62.25 C ANISOU 819 CG1 ILE A 114 9134 7179 7337 2348 860 -503 C ATOM 820 CG2 ILE A 114 38.868 -18.045 40.583 1.00 55.93 C ANISOU 820 CG2 ILE A 114 8662 6294 6296 2343 1005 -229 C ATOM 821 CD1 ILE A 114 37.293 -17.944 38.096 1.00 69.24 C ANISOU 821 CD1 ILE A 114 9945 8016 8348 2171 989 -480 C ATOM 822 N LEU A 115 41.753 -16.091 40.896 1.00 68.67 N ANISOU 822 N LEU A 115 10388 7970 7733 2544 446 -217 N ATOM 823 CA LEU A 115 42.854 -16.451 41.781 1.00 62.80 C ANISOU 823 CA LEU A 115 9739 7317 6805 2615 363 -95 C ATOM 824 C LEU A 115 43.230 -15.329 42.744 1.00 69.05 C ANISOU 824 C LEU A 115 10607 8218 7409 2628 202 -203 C ATOM 825 O LEU A 115 43.434 -15.568 43.934 1.00 84.87 O ANISOU 825 O LEU A 115 12734 10331 9182 2710 209 -156 O ATOM 826 CB LEU A 115 44.078 -16.853 40.961 1.00 57.59 C ANISOU 826 CB LEU A 115 8986 6674 6221 2633 241 15 C ATOM 827 CG LEU A 115 43.959 -18.165 40.187 1.00 62.90 C ANISOU 827 CG LEU A 115 9669 7221 7009 2669 393 136 C ATOM 828 CD1 LEU A 115 45.215 -18.390 39.376 1.00 58.15 C ANISOU 828 CD1 LEU A 115 8963 6677 6453 2740 270 225 C ATOM 829 CD2 LEU A 115 43.707 -19.333 41.127 1.00 56.15 C ANISOU 829 CD2 LEU A 115 9012 6317 6007 2757 576 279 C ATOM 830 N LEU A 116 43.322 -14.108 42.230 1.00 68.74 N ANISOU 830 N LEU A 116 10539 8131 7449 2545 60 -351 N ATOM 831 CA LEU A 116 43.743 -12.981 43.051 1.00 69.57 C ANISOU 831 CA LEU A 116 10768 8284 7381 2508 -108 -487 C ATOM 832 C LEU A 116 42.626 -12.517 43.990 1.00 71.82 C ANISOU 832 C LEU A 116 11220 8552 7516 2609 12 -618 C ATOM 833 O LEU A 116 42.898 -12.007 45.077 1.00 63.32 O ANISOU 833 O LEU A 116 10304 7551 6205 2633 -78 -706 O ATOM 834 CB LEU A 116 44.215 -11.827 42.166 1.00 71.90 C ANISOU 834 CB LEU A 116 11049 8467 7802 2359 -270 -592 C ATOM 835 CG LEU A 116 45.601 -12.036 41.545 1.00 67.46 C ANISOU 835 CG LEU A 116 10316 8010 7307 2230 -419 -484 C ATOM 836 CD1 LEU A 116 46.079 -10.782 40.832 1.00 60.13 C ANISOU 836 CD1 LEU A 116 9419 6963 6466 2023 -553 -584 C ATOM 837 CD2 LEU A 116 46.614 -12.493 42.584 1.00 59.11 C ANISOU 837 CD2 LEU A 116 9214 7210 6034 2249 -545 -418 C ATOM 838 N TRP A 117 41.373 -12.690 43.571 1.00 60.99 N ANISOU 838 N TRP A 117 9792 7120 6261 2675 210 -643 N ATOM 839 CA TRP A 117 40.229 -12.349 44.418 1.00 67.09 C ANISOU 839 CA TRP A 117 10660 7941 6889 2806 370 -752 C ATOM 840 C TRP A 117 40.152 -13.292 45.617 1.00 79.69 C ANISOU 840 C TRP A 117 12328 9680 8272 2859 518 -634 C ATOM 841 O TRP A 117 39.611 -12.944 46.666 1.00100.77 O ANISOU 841 O TRP A 117 15135 12435 10720 2971 611 -714 O ATOM 842 CB TRP A 117 38.917 -12.407 43.630 1.00 75.54 C ANISOU 842 CB TRP A 117 11564 9004 8133 2859 546 -798 C ATOM 843 CG TRP A 117 38.650 -11.207 42.766 1.00 77.03 C ANISOU 843 CG TRP A 117 11771 9071 8427 2924 435 -945 C ATOM 844 CD1 TRP A 117 39.260 -9.987 42.837 1.00 59.74 C ANISOU 844 CD1 TRP A 117 9804 6730 6166 2931 248 -1061 C ATOM 845 CD2 TRP A 117 37.697 -11.117 41.699 1.00 72.26 C ANISOU 845 CD2 TRP A 117 10986 8474 7994 2996 505 -987 C ATOM 846 NE1 TRP A 117 38.745 -9.144 41.881 1.00 76.80 N ANISOU 846 NE1 TRP A 117 11980 8760 8439 3029 219 -1147 N ATOM 847 CE2 TRP A 117 37.784 -9.814 41.169 1.00 75.60 C ANISOU 847 CE2 TRP A 117 11563 8733 8428 3098 362 -1103 C ATOM 848 CE3 TRP A 117 36.779 -12.012 41.141 1.00 71.20 C ANISOU 848 CE3 TRP A 117 10585 8477 7992 2969 666 -945 C ATOM 849 CZ2 TRP A 117 36.988 -9.384 40.108 1.00 72.91 C ANISOU 849 CZ2 TRP A 117 11119 8381 8202 3241 370 -1157 C ATOM 850 CZ3 TRP A 117 35.990 -11.584 40.088 1.00 77.25 C ANISOU 850 CZ3 TRP A 117 11197 9276 8878 3074 651 -1029 C ATOM 851 CH2 TRP A 117 36.100 -10.283 39.583 1.00 82.49 C ANISOU 851 CH2 TRP A 117 12020 9795 9529 3242 501 -1123 C ATOM 852 N SER A 118 40.712 -14.484 45.443 1.00 83.67 N ANISOU 852 N SER A 118 12775 10195 8823 2805 552 -434 N ATOM 853 CA SER A 118 40.708 -15.529 46.462 1.00 74.61 C ANISOU 853 CA SER A 118 11746 9132 7471 2869 712 -267 C ATOM 854 C SER A 118 41.862 -15.324 47.429 1.00 84.47 C ANISOU 854 C SER A 118 13145 10506 8445 2955 502 -241 C ATOM 855 O SER A 118 41.740 -15.572 48.629 1.00 85.25 O ANISOU 855 O SER A 118 13418 10717 8257 3068 587 -192 O ATOM 856 CB SER A 118 40.794 -16.913 45.822 1.00 84.99 C ANISOU 856 CB SER A 118 13005 10350 8936 2809 848 -64 C ATOM 857 OG SER A 118 40.841 -17.924 46.814 1.00105.36 O ANISOU 857 OG SER A 118 15777 12960 11297 2886 1015 125 O ATOM 858 N HIS A 119 42.980 -14.854 46.888 1.00 82.26 N ANISOU 858 N HIS A 119 12779 10238 8238 2890 228 -279 N ATOM 859 CA HIS A 119 44.190 -14.623 47.661 1.00 80.68 C ANISOU 859 CA HIS A 119 12637 10224 7795 2927 -23 -279 C ATOM 860 C HIS A 119 43.958 -13.429 48.571 1.00 81.23 C ANISOU 860 C HIS A 119 12882 10338 7645 2920 -123 -512 C ATOM 861 O HIS A 119 44.171 -13.507 49.780 1.00102.38 O ANISOU 861 O HIS A 119 15722 13183 9996 3033 -164 -512 O ATOM 862 CB HIS A 119 45.385 -14.374 46.734 1.00 64.29 C ANISOU 862 CB HIS A 119 10358 8188 5880 2803 -265 -275 C ATOM 863 CG HIS A 119 46.690 -14.210 47.451 1.00 76.11 C ANISOU 863 CG HIS A 119 11820 9962 7136 2814 -540 -277 C ATOM 864 ND1 HIS A 119 47.219 -15.185 48.270 1.00 85.64 N ANISOU 864 ND1 HIS A 119 13067 11380 8091 3032 -552 -95 N ATOM 865 CD2 HIS A 119 47.572 -13.183 47.472 1.00 70.69 C ANISOU 865 CD2 HIS A 119 11058 9397 6405 2623 -822 -442 C ATOM 866 CE1 HIS A 119 48.371 -14.765 48.764 1.00 86.28 C ANISOU 866 CE1 HIS A 119 13050 11757 7976 3002 -852 -158 C ATOM 867 NE2 HIS A 119 48.608 -13.553 48.295 1.00 78.00 N ANISOU 867 NE2 HIS A 119 11918 10660 7058 2717 -1018 -378 N ATOM 868 N PHE A 120 43.525 -12.322 47.980 1.00 83.44 N ANISOU 868 N PHE A 120 13170 10453 8079 2813 -161 -710 N ATOM 869 CA PHE A 120 43.287 -11.099 48.729 1.00 74.36 C ANISOU 869 CA PHE A 120 12252 9272 6730 2819 -251 -959 C ATOM 870 C PHE A 120 41.865 -11.068 49.286 1.00 74.57 C ANISOU 870 C PHE A 120 12405 9273 6657 3011 31 -1013 C ATOM 871 O PHE A 120 41.084 -11.996 49.075 1.00 83.61 O ANISOU 871 O PHE A 120 13424 10442 7903 3079 291 -856 O ATOM 872 CB PHE A 120 43.540 -9.892 47.834 1.00 71.62 C ANISOU 872 CB PHE A 120 11925 8717 6571 2640 -413 -1134 C ATOM 873 CG PHE A 120 44.948 -9.815 47.330 1.00 78.65 C ANISOU 873 CG PHE A 120 12664 9678 7542 2407 -671 -1094 C ATOM 874 CD1 PHE A 120 46.007 -9.693 48.212 1.00 70.44 C ANISOU 874 CD1 PHE A 120 11651 8863 6251 2316 -910 -1148 C ATOM 875 CD2 PHE A 120 45.214 -9.896 45.972 1.00 78.40 C ANISOU 875 CD2 PHE A 120 12432 9540 7816 2285 -671 -1002 C ATOM 876 CE1 PHE A 120 47.306 -9.637 47.752 1.00 70.90 C ANISOU 876 CE1 PHE A 120 11493 9069 6376 2091 -1140 -1113 C ATOM 877 CE2 PHE A 120 46.512 -9.839 45.504 1.00 65.74 C ANISOU 877 CE2 PHE A 120 10648 8054 6275 2072 -875 -955 C ATOM 878 CZ PHE A 120 47.560 -9.709 46.395 1.00 80.54 C ANISOU 878 CZ PHE A 120 12505 10185 7914 1967 -1107 -1010 C ATOM 879 N GLY A 121 41.464 -10.124 49.966 1.00 73.47 N ANISOU 879 N GLY A 121 12492 9101 6321 3096 18 -1221 N TER 880 GLY A 121 ATOM 881 N GLY B 6 21.566 -35.654 15.456 1.00162.11 N ANISOU 881 N GLY B 6 18543 26940 16113 -1026 -3289 554 N ATOM 882 CA GLY B 6 22.439 -36.459 14.623 1.00164.98 C ANISOU 882 CA GLY B 6 19465 27233 15987 -1268 -3232 377 C ATOM 883 C GLY B 6 23.741 -36.813 15.313 1.00166.08 C ANISOU 883 C GLY B 6 20247 26662 16193 -1207 -3006 34 C ATOM 884 O GLY B 6 24.797 -36.274 14.978 1.00171.40 O ANISOU 884 O GLY B 6 21074 27047 17004 -887 -2950 292 O ATOM 885 N PHE B 7 23.666 -37.731 16.273 1.00162.33 N ANISOU 885 N PHE B 7 20170 25766 15744 -1476 -2796 -532 N ATOM 886 CA PHE B 7 24.841 -38.192 17.009 1.00154.81 C ANISOU 886 CA PHE B 7 19836 24086 14897 -1411 -2545 -864 C ATOM 887 C PHE B 7 25.801 -38.927 16.080 1.00151.53 C ANISOU 887 C PHE B 7 19900 23416 14259 -1442 -2391 -906 C ATOM 888 O PHE B 7 26.967 -39.141 16.409 1.00144.87 O ANISOU 888 O PHE B 7 19484 22056 13504 -1278 -2218 -1030 O ATOM 889 CB PHE B 7 24.430 -39.116 18.157 1.00155.01 C ANISOU 889 CB PHE B 7 20175 23666 15057 -1651 -2315 -1375 C ATOM 890 CG PHE B 7 23.487 -38.486 19.144 1.00158.86 C ANISOU 890 CG PHE B 7 20231 24305 15822 -1648 -2391 -1422 C ATOM 891 CD1 PHE B 7 22.118 -38.531 18.934 1.00166.12 C ANISOU 891 CD1 PHE B 7 20678 25825 16616 -1899 -2544 -1408 C ATOM 892 CD2 PHE B 7 23.965 -37.866 20.286 1.00153.83 C ANISOU 892 CD2 PHE B 7 19658 23034 15758 -1329 -2211 -1447 C ATOM 893 CE1 PHE B 7 21.244 -37.961 19.838 1.00169.90 C ANISOU 893 CE1 PHE B 7 20752 26233 17570 -1794 -2496 -1406 C ATOM 894 CE2 PHE B 7 23.094 -37.294 21.196 1.00155.57 C ANISOU 894 CE2 PHE B 7 19512 23171 16427 -1260 -2151 -1472 C ATOM 895 CZ PHE B 7 21.731 -37.342 20.971 1.00164.51 C ANISOU 895 CZ PHE B 7 20174 24865 17468 -1474 -2281 -1448 C ATOM 896 N THR B 8 25.287 -39.306 14.915 1.00153.32 N ANISOU 896 N THR B 8 20007 24049 14196 -1653 -2453 -809 N ATOM 897 CA THR B 8 26.034 -40.065 13.922 1.00154.41 C ANISOU 897 CA THR B 8 20530 24045 14094 -1733 -2301 -885 C ATOM 898 C THR B 8 27.268 -39.306 13.443 1.00156.21 C ANISOU 898 C THR B 8 20847 24169 14336 -1405 -2330 -579 C ATOM 899 O THR B 8 28.318 -39.902 13.197 1.00157.18 O ANISOU 899 O THR B 8 21409 23907 14403 -1348 -2121 -739 O ATOM 900 CB THR B 8 25.145 -40.409 12.711 1.00156.26 C ANISOU 900 CB THR B 8 20517 24869 13988 -2057 -2400 -801 C ATOM 901 OG1 THR B 8 23.844 -40.801 13.167 1.00163.46 O ANISOU 901 OG1 THR B 8 21182 26031 14896 -2349 -2431 -984 O ATOM 902 CG2 THR B 8 25.757 -41.536 11.896 1.00150.06 C ANISOU 902 CG2 THR B 8 20178 23876 12963 -2246 -2165 -1043 C ATOM 903 N ARG B 9 27.134 -37.991 13.307 1.00148.35 N ANISOU 903 N ARG B 9 19386 23530 13450 -1147 -2570 -100 N ATOM 904 CA ARG B 9 28.232 -37.142 12.853 1.00134.16 C ANISOU 904 CA ARG B 9 17603 21658 11712 -806 -2589 273 C ATOM 905 C ARG B 9 29.387 -37.075 13.852 1.00116.59 C ANISOU 905 C ARG B 9 15718 18873 9708 -588 -2422 96 C ATOM 906 O ARG B 9 30.538 -36.883 13.466 1.00111.92 O ANISOU 906 O ARG B 9 15342 18079 9103 -405 -2321 213 O ATOM 907 CB ARG B 9 27.738 -35.725 12.557 1.00140.86 C ANISOU 907 CB ARG B 9 17818 22947 12753 -477 -2840 916 C ATOM 908 CG ARG B 9 28.841 -34.828 12.024 1.00153.16 C ANISOU 908 CG ARG B 9 19391 24358 14446 -98 -2801 1349 C ATOM 909 CD ARG B 9 28.354 -33.472 11.575 1.00166.92 C ANISOU 909 CD ARG B 9 20559 26349 16515 282 -2941 2029 C ATOM 910 NE ARG B 9 29.453 -32.706 10.995 1.00171.25 N ANISOU 910 NE ARG B 9 21203 26650 17215 595 -2827 2393 N ATOM 911 CZ ARG B 9 29.315 -31.533 10.389 1.00174.33 C ANISOU 911 CZ ARG B 9 21205 27199 17834 945 -2891 3043 C ATOM 912 NH1 ARG B 9 28.118 -30.975 10.282 1.00179.10 N ANISOU 912 NH1 ARG B 9 21280 28171 18598 1062 -3055 3404 N ATOM 913 NH2 ARG B 9 30.379 -30.914 9.897 1.00172.03 N ANISOU 913 NH2 ARG B 9 21063 26638 17664 1183 -2743 3316 N ATOM 914 N ILE B 10 29.080 -37.203 15.138 1.00111.26 N ANISOU 914 N ILE B 10 15072 17861 9340 -585 -2345 -188 N ATOM 915 CA ILE B 10 30.114 -37.162 16.164 1.00105.30 C ANISOU 915 CA ILE B 10 14622 16411 8975 -357 -2125 -379 C ATOM 916 C ILE B 10 31.160 -38.235 15.853 1.00103.62 C ANISOU 916 C ILE B 10 14980 16011 8381 -495 -1959 -662 C ATOM 917 O ILE B 10 32.362 -38.022 16.021 1.00107.28 O ANISOU 917 O ILE B 10 15630 16083 9049 -237 -1819 -618 O ATOM 918 CB ILE B 10 29.528 -37.378 17.569 1.00105.49 C ANISOU 918 CB ILE B 10 14661 16135 9286 -432 -2051 -707 C ATOM 919 CG1 ILE B 10 28.467 -36.316 17.876 1.00116.70 C ANISOU 919 CG1 ILE B 10 15502 17718 11121 -283 -2161 -439 C ATOM 920 CG2 ILE B 10 30.635 -37.412 18.615 1.00 92.27 C ANISOU 920 CG2 ILE B 10 13309 13825 7923 -241 -1849 -901 C ATOM 921 CD1 ILE B 10 28.997 -34.903 17.894 1.00116.67 C ANISOU 921 CD1 ILE B 10 15207 17463 11661 164 -2112 -17 C ATOM 922 N ILE B 11 30.684 -39.384 15.381 1.00108.93 N ANISOU 922 N ILE B 11 15832 16698 8857 -732 -1854 -917 N ATOM 923 CA ILE B 11 31.549 -40.465 14.918 1.00116.16 C ANISOU 923 CA ILE B 11 17093 17362 9679 -704 -1587 -1131 C ATOM 924 C ILE B 11 32.332 -40.047 13.668 1.00118.29 C ANISOU 924 C ILE B 11 17395 17824 9725 -619 -1609 -856 C ATOM 925 O ILE B 11 33.475 -40.466 13.477 1.00123.01 O ANISOU 925 O ILE B 11 18199 18220 10320 -487 -1390 -940 O ATOM 926 CB ILE B 11 30.739 -41.744 14.614 1.00122.32 C ANISOU 926 CB ILE B 11 17962 18179 10335 -992 -1467 -1406 C ATOM 927 CG1 ILE B 11 29.834 -42.093 15.796 1.00112.28 C ANISOU 927 CG1 ILE B 11 16632 16751 9278 -1097 -1454 -1624 C ATOM 928 CG2 ILE B 11 31.665 -42.910 14.292 1.00128.23 C ANISOU 928 CG2 ILE B 11 18998 18672 11053 -965 -1164 -1611 C ATOM 929 CD1 ILE B 11 30.589 -42.480 17.047 1.00111.23 C ANISOU 929 CD1 ILE B 11 16639 16153 9470 -890 -1252 -1809 C ATOM 930 N LYS B 12 31.723 -39.208 12.832 1.00122.57 N ANISOU 930 N LYS B 12 17627 18827 10115 -694 -1851 -494 N ATOM 931 CA LYS B 12 32.378 -38.732 11.612 1.00124.08 C ANISOU 931 CA LYS B 12 17800 19230 10115 -616 -1873 -179 C ATOM 932 C LYS B 12 33.563 -37.850 11.959 1.00126.65 C ANISOU 932 C LYS B 12 18152 19348 10621 -291 -1844 60 C ATOM 933 O LYS B 12 34.618 -37.925 11.332 1.00131.70 O ANISOU 933 O LYS B 12 19012 19877 11150 -203 -1696 109 O ATOM 934 CB LYS B 12 31.419 -37.907 10.751 1.00117.05 C ANISOU 934 CB LYS B 12 16434 18932 9109 -682 -2145 243 C ATOM 935 CG LYS B 12 31.824 -37.766 9.297 1.00127.50 C ANISOU 935 CG LYS B 12 17773 20515 10154 -719 -2139 483 C ATOM 936 CD LYS B 12 31.256 -36.477 8.715 1.00140.44 C ANISOU 936 CD LYS B 12 18881 22629 11851 -554 -2401 1082 C ATOM 937 CE LYS B 12 29.746 -36.443 8.655 1.00142.71 C ANISOU 937 CE LYS B 12 18743 23394 12088 -734 -2620 1163 C ATOM 938 NZ LYS B 12 29.304 -35.114 8.142 1.00147.26 N ANISOU 938 NZ LYS B 12 18782 24361 12811 -451 -2836 1820 N ATOM 939 N ALA B 13 33.372 -37.011 12.971 1.00121.24 N ANISOU 939 N ALA B 13 17193 18554 10319 -70 -1936 194 N ATOM 940 CA ALA B 13 34.404 -36.092 13.425 1.00118.17 C ANISOU 940 CA ALA B 13 16739 17704 10456 329 -1812 385 C ATOM 941 C ALA B 13 35.511 -36.831 14.162 1.00109.96 C ANISOU 941 C ALA B 13 16119 16171 9491 374 -1586 19 C ATOM 942 O ALA B 13 36.671 -36.423 14.131 1.00107.96 O ANISOU 942 O ALA B 13 15921 15649 9450 612 -1451 125 O ATOM 943 CB ALA B 13 33.800 -35.019 14.311 1.00116.83 C ANISOU 943 CB ALA B 13 16165 17367 10861 554 -1876 567 C ATOM 944 N ALA B 14 35.141 -37.915 14.836 1.00 95.69 N ANISOU 944 N ALA B 14 14590 14259 7510 148 -1536 -391 N ATOM 945 CA ALA B 14 36.102 -38.723 15.577 1.00 86.99 C ANISOU 945 CA ALA B 14 13841 12711 6500 200 -1307 -693 C ATOM 946 C ALA B 14 37.081 -39.435 14.644 1.00 91.86 C ANISOU 946 C ALA B 14 14626 13325 6950 148 -1071 -723 C ATOM 947 O ALA B 14 38.281 -39.480 14.914 1.00 99.41 O ANISOU 947 O ALA B 14 15749 13953 8068 378 -921 -733 O ATOM 948 CB ALA B 14 35.377 -39.732 16.449 1.00 89.80 C ANISOU 948 CB ALA B 14 14189 12968 6962 -54 -1193 -1035 C ATOM 949 N GLY B 15 36.560 -39.987 13.551 1.00 93.79 N ANISOU 949 N GLY B 15 14805 13970 6862 -112 -1044 -755 N ATOM 950 CA GLY B 15 37.380 -40.658 12.556 1.00 95.48 C ANISOU 950 CA GLY B 15 15178 14214 6886 -154 -822 -811 C ATOM 951 C GLY B 15 38.398 -39.714 11.946 1.00 99.89 C ANISOU 951 C GLY B 15 15796 14751 7408 61 -836 -493 C ATOM 952 O GLY B 15 39.522 -40.103 11.629 1.00114.83 O ANISOU 952 O GLY B 15 17889 16433 9310 155 -605 -549 O ATOM 953 N TYR B 16 37.976 -38.466 11.779 1.00 93.21 N ANISOU 953 N TYR B 16 14763 14109 6542 201 -1104 -135 N ATOM 954 CA TYR B 16 38.818 -37.385 11.283 1.00 79.84 C ANISOU 954 CA TYR B 16 12952 12386 4998 506 -1103 235 C ATOM 955 C TYR B 16 40.042 -37.271 12.181 1.00 92.17 C ANISOU 955 C TYR B 16 14587 13439 6995 802 -920 136 C ATOM 956 O TYR B 16 41.170 -37.502 11.750 1.00100.07 O ANISOU 956 O TYR B 16 15765 14316 7943 901 -714 118 O ATOM 957 CB TYR B 16 38.040 -36.074 11.249 1.00 79.47 C ANISOU 957 CB TYR B 16 12427 12535 5231 634 -1332 648 C ATOM 958 CG TYR B 16 36.974 -36.061 10.182 1.00 95.33 C ANISOU 958 CG TYR B 16 14285 15152 6784 387 -1538 860 C ATOM 959 CD1 TYR B 16 37.070 -36.881 9.066 1.00 95.71 C ANISOU 959 CD1 TYR B 16 14610 15433 6322 87 -1464 735 C ATOM 960 CD2 TYR B 16 35.861 -35.240 10.298 1.00103.61 C ANISOU 960 CD2 TYR B 16 14903 16451 8013 447 -1773 1166 C ATOM 961 CE1 TYR B 16 36.088 -36.885 8.097 1.00115.51 C ANISOU 961 CE1 TYR B 16 16950 18331 8608 -122 -1618 864 C ATOM 962 CE2 TYR B 16 34.876 -35.232 9.333 1.00 94.13 C ANISOU 962 CE2 TYR B 16 13508 15822 6434 229 -1978 1381 C ATOM 963 CZ TYR B 16 34.993 -36.056 8.235 1.00110.82 C ANISOU 963 CZ TYR B 16 15896 18051 8160 -68 -1890 1193 C ATOM 964 OH TYR B 16 34.017 -36.049 7.265 1.00114.10 O ANISOU 964 OH TYR B 16 16092 18919 8341 -271 -2052 1345 O ATOM 965 N SER B 17 39.794 -36.870 13.424 1.00 82.42 N ANISOU 965 N SER B 17 13182 11952 6182 927 -996 79 N ATOM 966 CA SER B 17 40.831 -36.670 14.431 1.00 86.33 C ANISOU 966 CA SER B 17 13677 12042 7084 1167 -874 -9 C ATOM 967 C SER B 17 41.797 -37.852 14.512 1.00 94.83 C ANISOU 967 C SER B 17 15133 12931 7968 1195 -661 -272 C ATOM 968 O SER B 17 43.012 -37.661 14.557 1.00104.65 O ANISOU 968 O SER B 17 16361 14007 9394 1405 -517 -219 O ATOM 969 CB SER B 17 40.190 -36.429 15.795 1.00 89.88 C ANISOU 969 CB SER B 17 13987 12306 7858 1174 -981 -141 C ATOM 970 OG SER B 17 39.182 -35.437 15.705 1.00 91.67 O ANISOU 970 OG SER B 17 13870 12691 8268 1159 -1135 93 O ATOM 971 N TRP B 18 41.257 -39.067 14.540 1.00 93.02 N ANISOU 971 N TRP B 18 15229 12723 7391 984 -615 -549 N ATOM 972 CA TRP B 18 42.090 -40.268 14.558 1.00 98.13 C ANISOU 972 CA TRP B 18 16090 13138 8056 970 -336 -747 C ATOM 973 C TRP B 18 42.951 -40.376 13.308 1.00 82.78 C ANISOU 973 C TRP B 18 14267 11290 5894 1005 -144 -659 C ATOM 974 O TRP B 18 44.103 -40.806 13.374 1.00 84.90 O ANISOU 974 O TRP B 18 14690 11335 6233 1214 79 -705 O ATOM 975 CB TRP B 18 41.230 -41.525 14.687 1.00113.05 C ANISOU 975 CB TRP B 18 18028 15026 9902 631 -250 -996 C ATOM 976 CG TRP B 18 42.017 -42.793 14.502 1.00115.29 C ANISOU 976 CG TRP B 18 18551 15078 10175 639 55 -1149 C ATOM 977 CD1 TRP B 18 41.926 -43.663 13.453 1.00116.61 C ANISOU 977 CD1 TRP B 18 18833 15366 10109 411 245 -1268 C ATOM 978 CD2 TRP B 18 43.026 -43.321 15.373 1.00113.22 C ANISOU 978 CD2 TRP B 18 18448 14438 10131 920 207 -1179 C ATOM 979 NE1 TRP B 18 42.806 -44.703 13.622 1.00116.48 N ANISOU 979 NE1 TRP B 18 19068 15008 10180 538 530 -1371 N ATOM 980 CE2 TRP B 18 43.494 -44.518 14.793 1.00109.78 C ANISOU 980 CE2 TRP B 18 18248 13864 9598 866 505 -1294 C ATOM 981 CE3 TRP B 18 43.574 -42.902 16.589 1.00109.99 C ANISOU 981 CE3 TRP B 18 17997 13828 9967 1217 118 -1115 C ATOM 982 CZ2 TRP B 18 44.483 -45.299 15.386 1.00109.39 C ANISOU 982 CZ2 TRP B 18 18411 13462 9692 1139 721 -1300 C ATOM 983 CZ3 TRP B 18 44.557 -43.680 17.176 1.00106.17 C ANISOU 983 CZ3 TRP B 18 17690 13061 9588 1469 301 -1128 C ATOM 984 CH2 TRP B 18 45.001 -44.864 16.574 1.00108.94 C ANISOU 984 CH2 TRP B 18 18292 13258 9842 1452 602 -1198 C ATOM 985 N LYS B 19 42.386 -39.992 12.170 1.00 74.43 N ANISOU 985 N LYS B 19 13127 10594 4558 801 -224 -517 N ATOM 986 CA LYS B 19 43.124 -39.989 10.914 1.00 84.73 C ANISOU 986 CA LYS B 19 14529 12038 5627 786 -46 -416 C ATOM 987 C LYS B 19 44.238 -38.955 10.983 1.00 87.85 C ANISOU 987 C LYS B 19 14828 12317 6234 1166 -12 -164 C ATOM 988 O LYS B 19 45.338 -39.169 10.477 1.00100.66 O ANISOU 988 O LYS B 19 16564 13848 7832 1285 241 -165 O ATOM 989 CB LYS B 19 42.193 -39.703 9.737 1.00 67.55 C ANISOU 989 CB LYS B 19 12218 10353 3097 467 -187 -268 C ATOM 990 CG LYS B 19 42.817 -39.956 8.380 1.00 96.78 C ANISOU 990 CG LYS B 19 16030 14243 6498 340 25 -236 C ATOM 991 CD LYS B 19 41.807 -39.738 7.265 1.00102.78 C ANISOU 991 CD LYS B 19 16603 15584 6867 32 -149 -90 C ATOM 992 CE LYS B 19 42.477 -39.750 5.903 1.00102.54 C ANISOU 992 CE LYS B 19 16659 15772 6530 -46 39 1 C ATOM 993 NZ LYS B 19 41.785 -38.855 4.936 1.00105.36 N ANISOU 993 NZ LYS B 19 16817 16629 6584 -64 -201 381 N ATOM 994 N GLY B 20 43.938 -37.829 11.619 1.00 90.38 N ANISOU 994 N GLY B 20 14779 12621 6942 1290 -230 45 N ATOM 995 CA GLY B 20 44.917 -36.778 11.817 1.00 89.80 C ANISOU 995 CA GLY B 20 14428 12403 7289 1545 -180 260 C ATOM 996 C GLY B 20 46.031 -37.205 12.750 1.00 84.79 C ANISOU 996 C GLY B 20 13839 11462 6914 1761 -29 79 C ATOM 997 O GLY B 20 47.189 -36.836 12.553 1.00 85.57 O ANISOU 997 O GLY B 20 13831 11493 7190 1930 130 172 O ATOM 998 N LEU B 21 45.687 -37.978 13.774 1.00 74.12 N ANISOU 998 N LEU B 21 12628 9953 5579 1755 -78 -160 N ATOM 999 CA LEU B 21 46.679 -38.458 14.730 1.00 73.29 C ANISOU 999 CA LEU B 21 12554 9607 5684 1977 33 -288 C ATOM 1000 C LEU B 21 47.707 -39.375 14.072 1.00 82.02 C ANISOU 1000 C LEU B 21 13908 10648 6607 2100 337 -354 C ATOM 1001 O LEU B 21 48.907 -39.248 14.312 1.00 87.37 O ANISOU 1001 O LEU B 21 14442 11244 7512 2339 463 -297 O ATOM 1002 CB LEU B 21 45.992 -39.193 15.882 1.00 72.52 C ANISOU 1002 CB LEU B 21 12614 9369 5573 1926 -68 -504 C ATOM 1003 CG LEU B 21 45.267 -38.322 16.908 1.00 74.00 C ANISOU 1003 CG LEU B 21 12529 9543 6046 1867 -312 -484 C ATOM 1004 CD1 LEU B 21 44.455 -39.186 17.854 1.00 86.10 C ANISOU 1004 CD1 LEU B 21 14283 10963 7468 1758 -382 -715 C ATOM 1005 CD2 LEU B 21 46.263 -37.477 17.683 1.00 56.83 C ANISOU 1005 CD2 LEU B 21 10041 7285 4267 2050 -322 -400 C ATOM 1006 N ARG B 22 47.229 -40.299 13.246 1.00 86.64 N ANISOU 1006 N ARG B 22 14854 11282 6783 1918 477 -489 N ATOM 1007 CA ARG B 22 48.106 -41.205 12.519 1.00 92.09 C ANISOU 1007 CA ARG B 22 15827 11879 7284 2001 836 -581 C ATOM 1008 C ARG B 22 48.984 -40.418 11.562 1.00 88.51 C ANISOU 1008 C ARG B 22 15173 11565 6891 2075 951 -378 C ATOM 1009 O ARG B 22 50.172 -40.702 11.416 1.00 95.22 O ANISOU 1009 O ARG B 22 16025 12300 7854 2301 1215 -374 O ATOM 1010 CB ARG B 22 47.295 -42.252 11.757 1.00100.06 C ANISOU 1010 CB ARG B 22 17087 12920 8010 1622 947 -772 C ATOM 1011 CG ARG B 22 46.436 -43.135 12.646 1.00 99.50 C ANISOU 1011 CG ARG B 22 17063 12686 8057 1453 862 -951 C ATOM 1012 CD ARG B 22 45.927 -44.373 11.920 1.00110.48 C ANISOU 1012 CD ARG B 22 18628 14068 9282 1101 1061 -1158 C ATOM 1013 NE ARG B 22 46.955 -45.387 11.710 1.00120.21 N ANISOU 1013 NE ARG B 22 20111 15002 10560 1268 1443 -1240 N ATOM 1014 CZ ARG B 22 47.526 -45.629 10.537 1.00128.39 C ANISOU 1014 CZ ARG B 22 21265 16092 11424 1203 1710 -1275 C ATOM 1015 NH1 ARG B 22 47.176 -44.916 9.475 1.00124.00 N ANISOU 1015 NH1 ARG B 22 20599 15908 10605 966 1610 -1219 N ATOM 1016 NH2 ARG B 22 48.445 -46.577 10.427 1.00136.12 N ANISOU 1016 NH2 ARG B 22 22470 16760 12488 1382 2086 -1345 N ATOM 1017 N ALA B 23 48.390 -39.426 10.908 1.00 77.24 N ANISOU 1017 N ALA B 23 13564 10389 5393 1894 767 -189 N ATOM 1018 CA ALA B 23 49.118 -38.585 9.968 1.00 84.70 C ANISOU 1018 CA ALA B 23 14335 11471 6378 1932 875 37 C ATOM 1019 C ALA B 23 50.243 -37.825 10.663 1.00 87.24 C ANISOU 1019 C ALA B 23 14309 11657 7183 2211 901 152 C ATOM 1020 O ALA B 23 51.359 -37.756 10.151 1.00 88.43 O ANISOU 1020 O ALA B 23 14407 11796 7397 2336 1147 202 O ATOM 1021 CB ALA B 23 48.172 -37.612 9.281 1.00 75.34 C ANISOU 1021 CB ALA B 23 13000 10570 5057 1723 647 283 C ATOM 1022 N ALA B 24 49.948 -37.256 11.828 1.00 62.35 N ANISOU 1022 N ALA B 24 10910 8422 4357 2275 664 173 N ATOM 1023 CA ALA B 24 50.961 -36.543 12.596 1.00 76.94 C ANISOU 1023 CA ALA B 24 12417 10185 6633 2467 676 236 C ATOM 1024 C ALA B 24 52.060 -37.502 13.021 1.00 77.86 C ANISOU 1024 C ALA B 24 12592 10193 6797 2703 873 99 C ATOM 1025 O ALA B 24 53.245 -37.171 12.982 1.00 85.86 O ANISOU 1025 O ALA B 24 13375 11231 8018 2858 1022 166 O ATOM 1026 CB ALA B 24 50.347 -35.878 13.812 1.00 68.52 C ANISOU 1026 CB ALA B 24 11130 9054 5850 2433 413 226 C ATOM 1027 N TRP B 25 51.649 -38.695 13.432 1.00 62.04 N ANISOU 1027 N TRP B 25 10890 8072 4609 2734 888 -78 N ATOM 1028 CA TRP B 25 52.580 -39.718 13.885 1.00 66.99 C ANISOU 1028 CA TRP B 25 11605 8564 5286 3009 1092 -164 C ATOM 1029 C TRP B 25 53.471 -40.221 12.759 1.00 82.12 C ANISOU 1029 C TRP B 25 13659 10469 7073 3112 1471 -159 C ATOM 1030 O TRP B 25 54.690 -40.302 12.904 1.00 92.57 O ANISOU 1030 O TRP B 25 14781 11787 8607 3378 1647 -99 O ATOM 1031 CB TRP B 25 51.828 -40.892 14.507 1.00 78.12 C ANISOU 1031 CB TRP B 25 13372 9797 6513 3000 1074 -339 C ATOM 1032 CG TRP B 25 52.748 -41.962 14.990 1.00 92.48 C ANISOU 1032 CG TRP B 25 15296 11442 8400 3331 1309 -368 C ATOM 1033 CD1 TRP B 25 53.111 -43.093 14.321 1.00 99.95 C ANISOU 1033 CD1 TRP B 25 16598 12212 9166 3445 1694 -455 C ATOM 1034 CD2 TRP B 25 53.454 -41.988 16.236 1.00 82.99 C ANISOU 1034 CD2 TRP B 25 13826 10237 7469 3607 1198 -283 C ATOM 1035 NE1 TRP B 25 53.986 -43.831 15.079 1.00 94.79 N ANISOU 1035 NE1 TRP B 25 15910 11412 8693 3827 1841 -394 N ATOM 1036 CE2 TRP B 25 54.214 -43.174 16.259 1.00 73.64 C ANISOU 1036 CE2 TRP B 25 12834 8876 6270 3931 1512 -273 C ATOM 1037 CE3 TRP B 25 53.512 -41.128 17.337 1.00 88.38 C ANISOU 1037 CE3 TRP B 25 14127 11064 8391 3595 880 -215 C ATOM 1038 CZ2 TRP B 25 55.021 -43.522 17.339 1.00 85.56 C ANISOU 1038 CZ2 TRP B 25 14131 10394 7985 4277 1475 -142 C ATOM 1039 CZ3 TRP B 25 54.314 -41.475 18.409 1.00 76.64 C ANISOU 1039 CZ3 TRP B 25 12443 9613 7065 3874 836 -134 C ATOM 1040 CH2 TRP B 25 55.058 -42.662 18.402 1.00 85.58 C ANISOU 1040 CH2 TRP B 25 13738 10611 8166 4229 1110 -71 C ATOM 1041 N ILE B 26 52.851 -40.559 11.636 1.00 86.13 N ANISOU 1041 N ILE B 26 14498 11008 7220 2880 1604 -228 N ATOM 1042 CA ILE B 26 53.572 -41.122 10.506 1.00 81.70 C ANISOU 1042 CA ILE B 26 14144 10423 6475 2914 2010 -274 C ATOM 1043 C ILE B 26 54.482 -40.086 9.848 1.00 84.23 C ANISOU 1043 C ILE B 26 14137 10907 6957 2952 2092 -89 C ATOM 1044 O ILE B 26 55.632 -40.377 9.518 1.00 92.96 O ANISOU 1044 O ILE B 26 15185 11968 8169 3159 2413 -86 O ATOM 1045 CB ILE B 26 52.582 -41.688 9.460 1.00 84.64 C ANISOU 1045 CB ILE B 26 14956 10852 6349 2559 2112 -423 C ATOM 1046 CG1 ILE B 26 51.938 -42.976 9.981 1.00 85.51 C ANISOU 1046 CG1 ILE B 26 15466 10737 6287 2524 2196 -668 C ATOM 1047 CG2 ILE B 26 53.266 -41.910 8.118 1.00 94.59 C ANISOU 1047 CG2 ILE B 26 16387 12166 7386 2494 2511 -451 C ATOM 1048 CD1 ILE B 26 50.783 -43.472 9.136 1.00 93.88 C ANISOU 1048 CD1 ILE B 26 16715 11901 7054 2003 2136 -814 C ATOM 1049 N ASN B 27 53.966 -38.874 9.670 1.00 80.89 N ANISOU 1049 N ASN B 27 13499 10660 6576 2761 1831 77 N ATOM 1050 CA ASN B 27 54.686 -37.838 8.931 1.00 79.32 C ANISOU 1050 CA ASN B 27 13050 10597 6489 2738 1935 265 C ATOM 1051 C ASN B 27 55.630 -36.952 9.749 1.00 79.58 C ANISOU 1051 C ASN B 27 12613 10632 6993 2918 1874 369 C ATOM 1052 O ASN B 27 56.730 -36.641 9.297 1.00 96.80 O ANISOU 1052 O ASN B 27 14611 12864 9305 3006 2116 430 O ATOM 1053 CB ASN B 27 53.685 -36.949 8.191 1.00 72.82 C ANISOU 1053 CB ASN B 27 12252 9953 5463 2451 1744 443 C ATOM 1054 CG ASN B 27 53.072 -37.644 6.993 1.00 84.77 C ANISOU 1054 CG ASN B 27 14169 11598 6442 2207 1876 375 C ATOM 1055 OD1 ASN B 27 53.561 -37.517 5.871 1.00108.91 O ANISOU 1055 OD1 ASN B 27 17311 14771 9297 2117 2121 444 O ATOM 1056 ND2 ASN B 27 51.995 -38.386 7.225 1.00 73.24 N ANISOU 1056 ND2 ASN B 27 12962 10141 4725 2060 1728 219 N ATOM 1057 N GLU B 28 55.209 -36.550 10.946 1.00 92.03 N ANISOU 1057 N GLU B 28 15365 11015 8586 3994 1375 -400 N ATOM 1058 CA GLU B 28 56.012 -35.632 11.752 1.00 80.63 C ANISOU 1058 CA GLU B 28 13554 9715 7366 4050 1398 -221 C ATOM 1059 C GLU B 28 56.833 -36.367 12.809 1.00100.55 C ANISOU 1059 C GLU B 28 16111 12116 9979 4224 1460 -207 C ATOM 1060 O GLU B 28 56.287 -37.085 13.647 1.00112.19 O ANISOU 1060 O GLU B 28 17749 13399 11480 4136 1388 -299 O ATOM 1061 CB GLU B 28 55.113 -34.592 12.433 1.00 78.55 C ANISOU 1061 CB GLU B 28 13055 9492 7298 3775 1220 -179 C ATOM 1062 CG GLU B 28 54.476 -33.571 11.493 1.00 91.82 C ANISOU 1062 CG GLU B 28 14598 11325 8966 3604 1139 -139 C ATOM 1063 CD GLU B 28 55.487 -32.714 10.750 1.00113.03 C ANISOU 1063 CD GLU B 28 17038 14244 11664 3752 1230 40 C ATOM 1064 OE1 GLU B 28 56.503 -32.309 11.353 1.00134.99 O ANISOU 1064 OE1 GLU B 28 19580 17098 14611 3895 1274 183 O ATOM 1065 OE2 GLU B 28 55.260 -32.446 9.551 1.00107.61 O ANISOU 1065 OE2 GLU B 28 16397 13664 10826 3722 1247 54 O ATOM 1066 N ALA B 29 58.148 -36.175 12.763 1.00100.71 N ANISOU 1066 N ALA B 29 15961 12246 10060 4469 1589 -69 N ATOM 1067 CA ALA B 29 59.051 -36.801 13.721 1.00 82.28 C ANISOU 1067 CA ALA B 29 13628 9799 7835 4649 1636 -31 C ATOM 1068 C ALA B 29 59.011 -36.090 15.068 1.00 80.91 C ANISOU 1068 C ALA B 29 13221 9622 7900 4530 1484 59 C ATOM 1069 O ALA B 29 59.154 -36.719 16.117 1.00 81.95 O ANISOU 1069 O ALA B 29 13446 9598 8092 4561 1445 33 O ATOM 1070 CB ALA B 29 60.470 -36.822 13.180 1.00 68.89 C ANISOU 1070 CB ALA B 29 11778 8229 6169 4887 1791 123 C ATOM 1071 N ALA B 30 58.832 -34.773 15.029 1.00 78.05 N ANISOU 1071 N ALA B 30 12565 9425 7667 4403 1389 165 N ATOM 1072 CA ALA B 30 58.737 -33.975 16.244 1.00 76.03 C ANISOU 1072 CA ALA B 30 12096 9170 7622 4298 1221 228 C ATOM 1073 C ALA B 30 57.549 -34.438 17.073 1.00 80.63 C ANISOU 1073 C ALA B 30 12879 9604 8154 4104 1129 80 C ATOM 1074 O ALA B 30 57.597 -34.447 18.301 1.00 76.98 O ANISOU 1074 O ALA B 30 12398 9065 7784 4096 1045 90 O ATOM 1075 CB ALA B 30 58.615 -32.499 15.911 1.00 80.75 C ANISOU 1075 CB ALA B 30 12367 9953 8362 4185 1116 344 C ATOM 1076 N PHE B 31 56.483 -34.829 16.384 1.00 80.56 N ANISOU 1076 N PHE B 31 13063 9551 7994 3952 1141 -45 N ATOM 1077 CA PHE B 31 55.285 -35.327 17.039 1.00 71.37 C ANISOU 1077 CA PHE B 31 12076 8245 6797 3759 1069 -158 C ATOM 1078 C PHE B 31 55.555 -36.660 17.730 1.00 75.41 C ANISOU 1078 C PHE B 31 12844 8558 7249 3863 1121 -207 C ATOM 1079 O PHE B 31 55.016 -36.933 18.800 1.00 68.98 O ANISOU 1079 O PHE B 31 12091 7647 6472 3766 1064 -223 O ATOM 1080 CB PHE B 31 54.151 -35.480 16.020 1.00 77.58 C ANISOU 1080 CB PHE B 31 13002 9008 7465 3577 1048 -260 C ATOM 1081 CG PHE B 31 52.860 -35.971 16.612 1.00 72.54 C ANISOU 1081 CG PHE B 31 12510 8220 6832 3362 973 -345 C ATOM 1082 CD1 PHE B 31 51.985 -35.095 17.232 1.00 72.63 C ANISOU 1082 CD1 PHE B 31 12336 8291 6970 3170 878 -325 C ATOM 1083 CD2 PHE B 31 52.521 -37.313 16.546 1.00 73.98 C ANISOU 1083 CD2 PHE B 31 13005 8195 6907 3360 996 -434 C ATOM 1084 CE1 PHE B 31 50.797 -35.548 17.773 1.00 67.12 C ANISOU 1084 CE1 PHE B 31 11745 7467 6290 2982 836 -373 C ATOM 1085 CE2 PHE B 31 51.336 -37.772 17.087 1.00 67.42 C ANISOU 1085 CE2 PHE B 31 12281 7224 6113 3155 927 -472 C ATOM 1086 CZ PHE B 31 50.473 -36.888 17.703 1.00 66.80 C ANISOU 1086 CZ PHE B 31 11998 7225 6159 2967 861 -432 C ATOM 1087 N ARG B 32 56.390 -37.489 17.113 1.00 82.16 N ANISOU 1087 N ARG B 32 13849 9357 8012 4069 1234 -223 N ATOM 1088 CA ARG B 32 56.718 -38.790 17.685 1.00 75.56 C ANISOU 1088 CA ARG B 32 13257 8316 7136 4183 1272 -267 C ATOM 1089 C ARG B 32 57.572 -38.676 18.946 1.00 81.93 C ANISOU 1089 C ARG B 32 13929 9114 8087 4281 1237 -152 C ATOM 1090 O ARG B 32 57.328 -39.371 19.934 1.00 86.39 O ANISOU 1090 O ARG B 32 14633 9533 8659 4237 1191 -164 O ATOM 1091 CB ARG B 32 57.442 -39.647 16.645 1.00 75.51 C ANISOU 1091 CB ARG B 32 13384 8284 7022 4332 1369 -295 C ATOM 1092 CG ARG B 32 56.536 -40.197 15.557 1.00 63.12 C ANISOU 1092 CG ARG B 32 12068 6635 5281 4240 1362 -443 C ATOM 1093 CD ARG B 32 57.247 -41.223 14.688 1.00 71.21 C ANISOU 1093 CD ARG B 32 13255 7605 6197 4391 1432 -483 C ATOM 1094 NE ARG B 32 57.261 -40.817 13.285 1.00 89.08 N ANISOU 1094 NE ARG B 32 15525 10006 8313 4440 1496 -514 N ATOM 1095 CZ ARG B 32 58.305 -40.270 12.672 1.00 88.58 C ANISOU 1095 CZ ARG B 32 15275 10140 8240 4620 1628 -403 C ATOM 1096 NH1 ARG B 32 59.437 -40.068 13.333 1.00 91.29 N ANISOU 1096 NH1 ARG B 32 15398 10552 8736 4761 1696 -258 N ATOM 1097 NH2 ARG B 32 58.218 -39.931 11.394 1.00108.54 N ANISOU 1097 NH2 ARG B 32 17839 12795 10607 4659 1690 -427 N ATOM 1098 N GLN B 33 58.573 -37.802 18.912 1.00 79.44 N ANISOU 1098 N GLN B 33 13338 8955 7892 4397 1240 -24 N ATOM 1099 CA GLN B 33 59.460 -37.614 20.060 1.00 65.54 C ANISOU 1099 CA GLN B 33 11425 7193 6286 4458 1160 95 C ATOM 1100 C GLN B 33 58.821 -36.873 21.229 1.00 77.01 C ANISOU 1100 C GLN B 33 12810 8645 7806 4352 1023 99 C ATOM 1101 O GLN B 33 59.001 -37.255 22.387 1.00 90.05 O ANISOU 1101 O GLN B 33 14525 10207 9483 4350 952 125 O ATOM 1102 CB GLN B 33 60.735 -36.887 19.631 1.00 66.14 C ANISOU 1102 CB GLN B 33 11203 7423 6503 4590 1181 247 C ATOM 1103 CG GLN B 33 61.749 -37.793 18.954 1.00 70.71 C ANISOU 1103 CG GLN B 33 11832 7982 7051 4743 1318 281 C ATOM 1104 CD GLN B 33 62.732 -37.029 18.096 1.00 89.68 C ANISOU 1104 CD GLN B 33 13956 10567 9552 4868 1402 428 C ATOM 1105 OE1 GLN B 33 62.879 -35.816 18.233 1.00104.59 O ANISOU 1105 OE1 GLN B 33 15569 12579 11591 4830 1315 540 O ATOM 1106 NE2 GLN B 33 63.431 -37.742 17.221 1.00 90.03 N ANISOU 1106 NE2 GLN B 33 14062 10626 9521 5017 1566 441 N ATOM 1107 N GLU B 34 58.077 -35.815 20.925 1.00 69.02 N ANISOU 1107 N GLU B 34 11648 7759 6817 4215 970 81 N ATOM 1108 CA GLU B 34 57.394 -35.051 21.960 1.00 63.74 C ANISOU 1108 CA GLU B 34 10890 7124 6205 4074 835 72 C ATOM 1109 C GLU B 34 56.310 -35.901 22.607 1.00 75.44 C ANISOU 1109 C GLU B 34 12621 8480 7563 3936 858 -17 C ATOM 1110 O GLU B 34 56.105 -35.843 23.816 1.00 81.59 O ANISOU 1110 O GLU B 34 13430 9225 8345 3914 791 -5 O ATOM 1111 CB GLU B 34 56.806 -33.762 21.379 1.00 61.69 C ANISOU 1111 CB GLU B 34 10396 7027 6015 3934 767 71 C ATOM 1112 CG GLU B 34 57.865 -32.757 20.942 1.00 90.85 C ANISOU 1112 CG GLU B 34 13796 10849 9874 4053 708 203 C ATOM 1113 CD GLU B 34 57.333 -31.712 19.979 1.00 94.25 C ANISOU 1113 CD GLU B 34 14027 11432 10354 3919 673 214 C ATOM 1114 OE1 GLU B 34 56.107 -31.686 19.742 1.00 98.35 O ANISOU 1114 OE1 GLU B 34 14625 11951 10791 3728 673 109 O ATOM 1115 OE2 GLU B 34 58.144 -30.919 19.456 1.00 85.55 O ANISOU 1115 OE2 GLU B 34 12674 10441 9389 4001 637 347 O ATOM 1116 N GLY B 35 55.644 -36.713 21.793 1.00 68.23 N ANISOU 1116 N GLY B 35 11892 7491 6541 3850 945 -96 N ATOM 1117 CA GLY B 35 54.624 -37.626 22.275 1.00 65.68 C ANISOU 1117 CA GLY B 35 11796 7027 6133 3710 963 -152 C ATOM 1118 C GLY B 35 55.140 -38.621 23.296 1.00 77.11 C ANISOU 1118 C GLY B 35 13421 8324 7555 3820 972 -109 C ATOM 1119 O GLY B 35 54.457 -38.924 24.274 1.00 83.08 O ANISOU 1119 O GLY B 35 14267 9021 8280 3719 954 -92 O ATOM 1120 N VAL B 36 56.348 -39.131 23.073 1.00 77.67 N ANISOU 1120 N VAL B 36 13533 8334 7642 4031 1004 -78 N ATOM 1121 CA VAL B 36 56.957 -40.064 24.013 1.00 66.17 C ANISOU 1121 CA VAL B 36 12234 6724 6185 4148 993 -27 C ATOM 1122 C VAL B 36 57.229 -39.391 25.351 1.00 71.62 C ANISOU 1122 C VAL B 36 12815 7473 6925 4170 892 56 C ATOM 1123 O VAL B 36 56.910 -39.941 26.406 1.00 76.46 O ANISOU 1123 O VAL B 36 13576 7994 7483 4130 866 88 O ATOM 1124 CB VAL B 36 58.277 -40.637 23.458 1.00 76.52 C ANISOU 1124 CB VAL B 36 13520 8014 7542 4312 1028 11 C ATOM 1125 CG1 VAL B 36 59.036 -41.389 24.543 1.00 67.70 C ANISOU 1125 CG1 VAL B 36 12474 6784 6464 4385 973 91 C ATOM 1126 CG2 VAL B 36 58.002 -41.538 22.267 1.00 70.34 C ANISOU 1126 CG2 VAL B 36 12912 7144 6670 4305 1114 -87 C ATOM 1127 N ALA B 37 57.811 -38.198 25.303 1.00 76.02 N ANISOU 1127 N ALA B 37 13121 8177 7584 4236 823 97 N ATOM 1128 CA ALA B 37 58.090 -37.438 26.514 1.00 65.56 C ANISOU 1128 CA ALA B 37 11698 6902 6310 4268 685 155 C ATOM 1129 C ALA B 37 56.794 -37.051 27.218 1.00 82.27 C ANISOU 1129 C ALA B 37 13852 9074 8332 4088 669 103 C ATOM 1130 O ALA B 37 56.713 -37.063 28.446 1.00 84.38 O ANISOU 1130 O ALA B 37 14202 9318 8540 4104 605 133 O ATOM 1131 CB ALA B 37 58.908 -36.200 26.187 1.00 74.55 C ANISOU 1131 CB ALA B 37 12513 8201 7611 4296 578 212 C ATOM 1132 N VAL B 38 55.783 -36.707 26.425 1.00 75.34 N ANISOU 1132 N VAL B 38 12914 8274 7438 3924 730 33 N ATOM 1133 CA VAL B 38 54.482 -36.325 26.958 1.00 71.53 C ANISOU 1133 CA VAL B 38 12432 7851 6896 3750 740 -9 C ATOM 1134 C VAL B 38 53.731 -37.469 27.623 1.00 72.39 C ANISOU 1134 C VAL B 38 12781 7838 6886 3664 825 13 C ATOM 1135 O VAL B 38 53.256 -37.343 28.754 1.00 81.48 O ANISOU 1135 O VAL B 38 13977 9016 7963 3638 821 41 O ATOM 1136 CB VAL B 38 53.582 -35.734 25.845 1.00 78.64 C ANISOU 1136 CB VAL B 38 13198 8842 7840 3586 772 -75 C ATOM 1137 CG1 VAL B 38 52.110 -35.766 26.249 1.00 53.91 C ANISOU 1137 CG1 VAL B 38 10107 5719 4657 3390 824 -104 C ATOM 1138 CG2 VAL B 38 54.031 -34.322 25.490 1.00 72.87 C ANISOU 1138 CG2 VAL B 38 12192 8261 7235 3629 663 -76 C ATOM 1139 N LEU B 39 53.646 -38.591 26.920 1.00 78.25 N ANISOU 1139 N LEU B 39 13680 8442 7607 3631 897 6 N ATOM 1140 CA LEU B 39 52.952 -39.767 27.422 1.00 95.07 C ANISOU 1140 CA LEU B 39 16030 10427 9664 3536 957 49 C ATOM 1141 C LEU B 39 53.652 -40.286 28.679 1.00 92.74 C ANISOU 1141 C LEU B 39 15865 10061 9311 3666 926 140 C ATOM 1142 O LEU B 39 53.002 -40.756 29.613 1.00 82.49 O ANISOU 1142 O LEU B 39 14684 8726 7933 3589 962 212 O ATOM 1143 CB LEU B 39 52.851 -40.832 26.328 1.00 95.60 C ANISOU 1143 CB LEU B 39 16247 10334 9743 3498 994 7 C ATOM 1144 CG LEU B 39 52.173 -42.155 26.659 1.00110.95 C ANISOU 1144 CG LEU B 39 18417 12082 11656 3391 1021 59 C ATOM 1145 CD1 LEU B 39 50.726 -41.911 27.033 1.00119.20 C ANISOU 1145 CD1 LEU B 39 19410 13177 12704 3166 1058 101 C ATOM 1146 CD2 LEU B 39 52.235 -43.048 25.436 1.00111.48 C ANISOU 1146 CD2 LEU B 39 18631 11983 11743 3392 1013 -20 C ATOM 1147 N LEU B 40 54.979 -40.201 28.689 1.00 88.09 N ANISOU 1147 N LEU B 40 15247 9452 8769 3863 857 154 N ATOM 1148 CA LEU B 40 55.767 -40.588 29.854 1.00 71.56 C ANISOU 1148 CA LEU B 40 13263 7286 6641 3997 788 243 C ATOM 1149 C LEU B 40 55.455 -39.669 31.034 1.00 76.07 C ANISOU 1149 C LEU B 40 13779 7989 7133 3991 726 265 C ATOM 1150 O LEU B 40 55.328 -40.121 32.173 1.00 76.65 O ANISOU 1150 O LEU B 40 14010 8020 7093 4002 717 342 O ATOM 1151 CB LEU B 40 57.263 -40.531 29.534 1.00 70.63 C ANISOU 1151 CB LEU B 40 13074 7126 6637 4209 712 262 C ATOM 1152 CG LEU B 40 57.960 -41.823 29.114 1.00 90.61 C ANISOU 1152 CG LEU B 40 15761 9461 9206 4313 749 285 C ATOM 1153 CD1 LEU B 40 59.445 -41.582 28.888 1.00 92.69 C ANISOU 1153 CD1 LEU B 40 15824 9788 9607 4425 673 323 C ATOM 1154 CD2 LEU B 40 57.745 -42.898 30.156 1.00 94.71 C ANISOU 1154 CD2 LEU B 40 16517 9826 9644 4284 733 368 C ATOM 1155 N ALA B 41 55.339 -38.376 30.748 1.00 80.75 N ANISOU 1155 N ALA B 41 14158 8741 7782 3982 677 198 N ATOM 1156 CA ALA B 41 55.033 -37.373 31.763 1.00 58.46 C ANISOU 1156 CA ALA B 41 11278 6045 4891 3997 601 183 C ATOM 1157 C ALA B 41 53.654 -37.601 32.379 1.00 75.81 C ANISOU 1157 C ALA B 41 13572 8289 6944 3850 730 193 C ATOM 1158 O ALA B 41 53.477 -37.482 33.592 1.00 74.90 O ANISOU 1158 O ALA B 41 13558 8215 6687 3898 716 229 O ATOM 1159 CB ALA B 41 55.123 -35.977 31.172 1.00 56.92 C ANISOU 1159 CB ALA B 41 10820 5987 4821 4003 512 105 C ATOM 1160 N VAL B 42 52.683 -37.920 31.528 1.00 78.45 N ANISOU 1160 N VAL B 42 13873 8617 7317 3675 854 171 N ATOM 1161 CA VAL B 42 51.309 -38.161 31.962 1.00 77.02 C ANISOU 1161 CA VAL B 42 13738 8472 7054 3516 989 209 C ATOM 1162 C VAL B 42 51.235 -39.339 32.932 1.00 84.49 C ANISOU 1162 C VAL B 42 14919 9310 7871 3521 1052 343 C ATOM 1163 O VAL B 42 50.579 -39.258 33.972 1.00 84.08 O ANISOU 1163 O VAL B 42 14924 9338 7685 3504 1128 409 O ATOM 1164 CB VAL B 42 50.378 -38.424 30.759 1.00 81.65 C ANISOU 1164 CB VAL B 42 14252 9023 7747 3320 1069 178 C ATOM 1165 CG1 VAL B 42 49.012 -38.900 31.228 1.00 83.72 C ANISOU 1165 CG1 VAL B 42 14562 9281 7966 3149 1205 265 C ATOM 1166 CG2 VAL B 42 50.244 -37.169 29.910 1.00 79.66 C ANISOU 1166 CG2 VAL B 42 13761 8900 7606 3290 1013 65 C ATOM 1167 N VAL B 43 51.916 -40.425 32.585 1.00 83.45 N ANISOU 1167 N VAL B 43 14925 9001 7781 3556 1024 390 N ATOM 1168 CA VAL B 43 51.954 -41.621 33.421 1.00 81.42 C ANISOU 1168 CA VAL B 43 14891 8612 7433 3559 1055 531 C ATOM 1169 C VAL B 43 52.509 -41.306 34.811 1.00 92.29 C ANISOU 1169 C VAL B 43 16357 10055 8653 3709 992 591 C ATOM 1170 O VAL B 43 51.936 -41.709 35.825 1.00101.40 O ANISOU 1170 O VAL B 43 17639 11230 9658 3673 1071 712 O ATOM 1171 CB VAL B 43 52.801 -42.729 32.768 1.00 84.33 C ANISOU 1171 CB VAL B 43 15379 8765 7896 3613 998 543 C ATOM 1172 CG1 VAL B 43 53.064 -43.852 33.753 1.00 82.33 C ANISOU 1172 CG1 VAL B 43 15348 8369 7565 3647 985 695 C ATOM 1173 CG2 VAL B 43 52.105 -43.260 31.524 1.00 69.73 C ANISOU 1173 CG2 VAL B 43 13517 6819 6158 3460 1052 492 C ATOM 1174 N ILE B 44 53.622 -40.579 34.846 1.00 93.22 N ANISOU 1174 N ILE B 44 16410 10204 8807 3879 842 519 N ATOM 1175 CA ILE B 44 54.257 -40.189 36.101 1.00 93.20 C ANISOU 1175 CA ILE B 44 16501 10243 8669 4036 724 555 C ATOM 1176 C ILE B 44 53.325 -39.317 36.942 1.00 99.64 C ANISOU 1176 C ILE B 44 17298 11248 9313 4017 787 528 C ATOM 1177 O ILE B 44 53.207 -39.504 38.154 1.00108.88 O ANISOU 1177 O ILE B 44 18642 12450 10278 4077 798 612 O ATOM 1178 CB ILE B 44 55.579 -39.433 35.846 1.00 86.83 C ANISOU 1178 CB ILE B 44 15577 9423 7992 4207 520 485 C ATOM 1179 CG1 ILE B 44 56.642 -40.389 35.306 1.00 94.26 C ANISOU 1179 CG1 ILE B 44 16567 10174 9072 4279 468 540 C ATOM 1180 CG2 ILE B 44 56.076 -38.758 37.116 1.00 96.91 C ANISOU 1180 CG2 ILE B 44 16932 10753 9136 4357 355 492 C ATOM 1181 CD1 ILE B 44 57.982 -39.734 35.075 1.00100.67 C ANISOU 1181 CD1 ILE B 44 17241 10964 10046 4450 281 516 C ATOM 1182 N ALA B 45 52.647 -38.382 36.285 1.00 88.43 N ANISOU 1182 N ALA B 45 15673 9953 7973 3940 835 415 N ATOM 1183 CA ALA B 45 51.732 -37.464 36.955 1.00 83.18 C ANISOU 1183 CA ALA B 45 14957 9469 7176 3936 903 364 C ATOM 1184 C ALA B 45 50.566 -38.191 37.621 1.00 87.60 C ANISOU 1184 C ALA B 45 15636 10069 7578 3826 1126 496 C ATOM 1185 O ALA B 45 50.037 -37.731 38.633 1.00 82.68 O ANISOU 1185 O ALA B 45 15072 9584 6759 3890 1196 506 O ATOM 1186 CB ALA B 45 51.209 -36.430 35.970 1.00 67.98 C ANISOU 1186 CB ALA B 45 12771 7643 5415 3853 907 230 C ATOM 1187 N CYS B 46 50.167 -39.325 37.058 1.00 79.88 N ANISOU 1187 N CYS B 46 14696 8967 6689 3670 1233 605 N ATOM 1188 CA CYS B 46 49.046 -40.079 37.605 1.00 88.37 C ANISOU 1188 CA CYS B 46 15849 10059 7667 3542 1436 772 C ATOM 1189 C CYS B 46 49.451 -40.896 38.827 1.00 98.29 C ANISOU 1189 C CYS B 46 17359 11269 8718 3632 1440 937 C ATOM 1190 O CYS B 46 48.606 -41.295 39.627 1.00112.96 O ANISOU 1190 O CYS B 46 19294 13197 10430 3578 1611 1096 O ATOM 1191 CB CYS B 46 48.470 -41.013 36.540 1.00 81.89 C ANISOU 1191 CB CYS B 46 14980 9088 7046 3333 1502 836 C ATOM 1192 SG CYS B 46 47.591 -40.182 35.203 1.00122.87 S ANISOU 1192 SG CYS B 46 19893 14342 12449 3176 1535 694 S ATOM 1193 N TRP B 47 50.747 -41.156 38.949 1.00 88.71 N ANISOU 1193 N TRP B 47 16264 9936 7505 3768 1251 918 N ATOM 1194 CA TRP B 47 51.284 -41.973 40.036 1.00 88.54 C ANISOU 1194 CA TRP B 47 16491 9839 7311 3855 1208 1076 C ATOM 1195 C TRP B 47 51.912 -41.205 41.211 1.00 87.84 C ANISOU 1195 C TRP B 47 16529 9857 6990 4066 1082 1034 C ATOM 1196 O TRP B 47 52.225 -41.803 42.240 1.00107.74 O ANISOU 1196 O TRP B 47 19274 12342 9320 4138 1054 1176 O ATOM 1197 CB TRP B 47 52.256 -42.999 39.454 1.00100.40 C ANISOU 1197 CB TRP B 47 18066 11096 8983 3857 1077 1116 C ATOM 1198 CG TRP B 47 51.476 -44.144 38.870 1.00120.20 C ANISOU 1198 CG TRP B 47 20583 13472 11614 3657 1205 1236 C ATOM 1199 CD1 TRP B 47 50.187 -44.479 39.177 1.00132.24 C ANISOU 1199 CD1 TRP B 47 22100 15062 13082 3498 1398 1379 C ATOM 1200 CD2 TRP B 47 51.903 -45.080 37.870 1.00121.85 C ANISOU 1200 CD2 TRP B 47 20806 13454 12037 3601 1137 1227 C ATOM 1201 NE1 TRP B 47 49.791 -45.570 38.446 1.00135.61 N ANISOU 1201 NE1 TRP B 47 22534 15297 13693 3331 1423 1467 N ATOM 1202 CE2 TRP B 47 50.824 -45.959 37.635 1.00130.59 C ANISOU 1202 CE2 TRP B 47 21929 14478 13211 3399 1261 1359 C ATOM 1203 CE3 TRP B 47 53.090 -45.266 37.157 1.00113.14 C ANISOU 1203 CE3 TRP B 47 19702 12206 11081 3715 985 1125 C ATOM 1204 CZ2 TRP B 47 50.898 -47.005 36.719 1.00129.23 C ANISOU 1204 CZ2 TRP B 47 21800 14068 13234 3310 1208 1367 C ATOM 1205 CZ3 TRP B 47 53.161 -46.309 36.247 1.00111.36 C ANISOU 1205 CZ3 TRP B 47 19518 11766 11028 3643 971 1129 C ATOM 1206 CH2 TRP B 47 52.072 -47.163 36.036 1.00121.55 C ANISOU 1206 CH2 TRP B 47 20851 12963 12368 3444 1067 1237 C ATOM 1207 N LEU B 48 52.102 -39.895 41.064 1.00 86.76 N ANISOU 1207 N LEU B 48 16258 9837 6868 4166 984 844 N ATOM 1208 CA LEU B 48 52.684 -39.082 42.139 1.00 89.01 C ANISOU 1208 CA LEU B 48 16671 10204 6946 4375 819 777 C ATOM 1209 C LEU B 48 51.746 -38.807 43.307 1.00 96.26 C ANISOU 1209 C LEU B 48 17723 11312 7538 4426 987 825 C ATOM 1210 O LEU B 48 50.524 -38.787 43.158 1.00103.96 O ANISOU 1210 O LEU B 48 18597 12409 8493 4307 1239 861 O ATOM 1211 CB LEU B 48 53.170 -37.731 41.602 1.00 76.00 C ANISOU 1211 CB LEU B 48 14827 8602 5447 4464 632 563 C ATOM 1212 CG LEU B 48 54.279 -37.658 40.563 1.00 87.77 C ANISOU 1212 CG LEU B 48 16165 9947 7238 4477 438 505 C ATOM 1213 CD1 LEU B 48 54.607 -36.205 40.277 1.00 97.62 C ANISOU 1213 CD1 LEU B 48 17223 11270 8598 4567 256 328 C ATOM 1214 CD2 LEU B 48 55.499 -38.370 41.107 1.00 91.29 C ANISOU 1214 CD2 LEU B 48 16794 10223 7670 4593 251 609 C ATOM 1215 N ASP B 49 52.346 -38.600 44.477 1.00100.84 N ANISOU 1215 N ASP B 49 18538 11913 7864 4615 839 832 N ATOM 1216 CA ASP B 49 51.606 -38.233 45.677 1.00111.59 C ANISOU 1216 CA ASP B 49 20068 13470 8862 4723 977 854 C ATOM 1217 C ASP B 49 51.387 -36.727 45.703 1.00107.27 C ANISOU 1217 C ASP B 49 19399 13062 8295 4846 901 607 C ATOM 1218 O ASP B 49 52.066 -35.993 46.422 1.00107.38 O ANISOU 1218 O ASP B 49 19503 13067 8231 5019 653 478 O ATOM 1219 CB ASP B 49 52.373 -38.681 46.925 1.00134.33 C ANISOU 1219 CB ASP B 49 23202 16282 11557 4838 818 937 C ATOM 1220 CG ASP B 49 51.587 -38.479 48.206 1.00167.11 C ANISOU 1220 CG ASP B 49 27442 20613 15440 4891 980 963 C ATOM 1221 OD1 ASP B 49 50.340 -38.502 48.155 1.00184.46 O ANISOU 1221 OD1 ASP B 49 29525 22968 17593 4795 1291 1028 O ATOM 1222 OD2 ASP B 49 52.223 -38.293 49.266 1.00173.56 O ANISOU 1222 OD2 ASP B 49 28441 21409 16095 5034 793 926 O ATOM 1223 N VAL B 50 50.431 -36.279 44.897 1.00100.70 N ANISOU 1223 N VAL B 50 18316 12329 7616 4725 1087 537 N ATOM 1224 CA VAL B 50 50.095 -34.867 44.783 1.00 97.06 C ANISOU 1224 CA VAL B 50 17707 11994 7178 4819 1031 307 C ATOM 1225 C VAL B 50 48.586 -34.665 44.833 1.00 96.10 C ANISOU 1225 C VAL B 50 17433 12054 7028 4724 1363 331 C ATOM 1226 O VAL B 50 47.819 -35.609 44.638 1.00 92.34 O ANISOU 1226 O VAL B 50 16947 11597 6541 4569 1637 526 O ATOM 1227 CB VAL B 50 50.646 -34.254 43.480 1.00 95.06 C ANISOU 1227 CB VAL B 50 17175 11634 7308 4741 830 164 C ATOM 1228 CG1 VAL B 50 52.169 -34.215 43.505 1.00 84.15 C ANISOU 1228 CG1 VAL B 50 15875 10082 6018 4854 477 134 C ATOM 1229 CG2 VAL B 50 50.136 -35.027 42.271 1.00 71.73 C ANISOU 1229 CG2 VAL B 50 14021 8617 4616 4489 1014 267 C ATOM 1230 N ASP B 51 48.163 -33.433 45.096 1.00 78.00 N ANISOU 1230 N ASP B 51 15016 9880 4739 4819 1325 146 N ATOM 1231 CA ASP B 51 46.744 -33.099 45.103 1.00 88.28 C ANISOU 1231 CA ASP B 51 16140 11355 6047 4747 1624 154 C ATOM 1232 C ASP B 51 46.209 -33.002 43.673 1.00 85.68 C ANISOU 1232 C ASP B 51 15558 11009 5986 4572 1726 122 C ATOM 1233 O ASP B 51 46.977 -33.040 42.711 1.00 78.13 O ANISOU 1233 O ASP B 51 14513 9905 5267 4493 1522 71 O ATOM 1234 CB ASP B 51 46.503 -31.794 45.865 1.00 85.43 C ANISOU 1234 CB ASP B 51 15742 11112 5607 4923 1529 -42 C ATOM 1235 CG ASP B 51 47.351 -30.652 45.346 1.00113.55 C ANISOU 1235 CG ASP B 51 19216 14586 9342 5016 1165 -282 C ATOM 1236 OD1 ASP B 51 48.540 -30.890 45.047 1.00131.17 O ANISOU 1236 OD1 ASP B 51 21547 16664 11630 5048 909 -291 O ATOM 1237 OD2 ASP B 51 46.836 -29.519 45.240 1.00122.91 O ANISOU 1237 OD2 ASP B 51 20230 15854 10617 5062 1130 -452 O ATOM 1238 N ALA B 52 44.890 -32.880 43.544 1.00 81.38 N ANISOU 1238 N ALA B 52 14846 10598 5477 4481 2017 170 N ATOM 1239 CA ALA B 52 44.227 -32.918 42.242 1.00 74.64 C ANISOU 1239 CA ALA B 52 13698 9698 4963 4244 2100 185 C ATOM 1240 C ALA B 52 44.665 -31.782 41.319 1.00 91.18 C ANISOU 1240 C ALA B 52 15586 11743 7314 4247 1837 -53 C ATOM 1241 O ALA B 52 44.994 -32.015 40.155 1.00 87.54 O ANISOU 1241 O ALA B 52 14981 11151 7130 4075 1723 -48 O ATOM 1242 CB ALA B 52 42.719 -32.889 42.425 1.00 76.44 C ANISOU 1242 CB ALA B 52 13776 10082 5188 4171 2446 288 C ATOM 1243 N CYS B 53 44.661 -30.559 41.842 1.00 97.58 N ANISOU 1243 N CYS B 53 16390 12657 8027 4448 1737 -255 N ATOM 1244 CA CYS B 53 45.021 -29.380 41.059 1.00 87.42 C ANISOU 1244 CA CYS B 53 14894 11328 6992 4458 1475 -468 C ATOM 1245 C CYS B 53 46.431 -29.493 40.489 1.00 94.26 C ANISOU 1245 C CYS B 53 15791 12025 8001 4449 1155 -491 C ATOM 1246 O CYS B 53 46.678 -29.125 39.341 1.00 95.50 O ANISOU 1246 O CYS B 53 15724 12108 8455 4323 1017 -542 O ATOM 1247 CB CYS B 53 44.900 -28.114 41.910 1.00 86.01 C ANISOU 1247 CB CYS B 53 14716 11250 6713 4666 1352 -659 C ATOM 1248 SG CYS B 53 43.243 -27.818 42.566 1.00130.96 S ANISOU 1248 SG CYS B 53 20300 17149 12312 4675 1714 -632 S ATOM 1249 N THR B 54 47.350 -30.009 41.298 1.00 92.99 N ANISOU 1249 N THR B 54 15902 11804 7625 4586 1046 -439 N ATOM 1250 CA THR B 54 48.727 -30.204 40.866 1.00 85.18 C ANISOU 1250 CA THR B 54 14944 10649 6773 4595 759 -432 C ATOM 1251 C THR B 54 48.817 -31.284 39.795 1.00 94.84 C ANISOU 1251 C THR B 54 16078 11764 8195 4370 859 -277 C ATOM 1252 O THR B 54 49.534 -31.133 38.806 1.00 88.24 O ANISOU 1252 O THR B 54 15094 10827 7607 4308 689 -304 O ATOM 1253 CB THR B 54 49.634 -30.588 42.047 1.00 69.89 C ANISOU 1253 CB THR B 54 13330 8662 4562 4791 618 -392 C ATOM 1254 OG1 THR B 54 49.609 -29.544 43.027 1.00 76.11 O ANISOU 1254 OG1 THR B 54 14231 9533 5152 5020 482 -561 O ATOM 1255 CG2 THR B 54 51.065 -30.806 41.580 1.00 79.85 C ANISOU 1255 CG2 THR B 54 14590 9741 6009 4800 327 -363 C ATOM 1256 N ARG B 55 48.071 -32.367 39.994 1.00 84.36 N ANISOU 1256 N ARG B 55 14840 10454 6757 4257 1134 -110 N ATOM 1257 CA ARG B 55 48.069 -33.482 39.056 1.00 76.31 C ANISOU 1257 CA ARG B 55 13776 9311 5907 4053 1220 31 C ATOM 1258 C ARG B 55 47.541 -33.022 37.703 1.00 71.25 C ANISOU 1258 C ARG B 55 12847 8667 5558 3877 1232 -39 C ATOM 1259 O ARG B 55 48.076 -33.388 36.659 1.00 76.12 O ANISOU 1259 O ARG B 55 13391 9166 6365 3780 1145 -27 O ATOM 1260 CB ARG B 55 47.215 -34.632 39.592 1.00 83.51 C ANISOU 1260 CB ARG B 55 14819 10240 6670 3956 1498 233 C ATOM 1261 CG ARG B 55 47.310 -35.920 38.788 1.00 76.03 C ANISOU 1261 CG ARG B 55 13887 9125 5875 3770 1544 382 C ATOM 1262 CD ARG B 55 46.450 -37.009 39.411 1.00 73.23 C ANISOU 1262 CD ARG B 55 13652 8779 5395 3673 1790 607 C ATOM 1263 NE ARG B 55 46.658 -37.115 40.852 1.00 82.37 N ANISOU 1263 NE ARG B 55 15044 10023 6229 3851 1833 681 N ATOM 1264 CZ ARG B 55 47.644 -37.795 41.425 1.00 92.51 C ANISOU 1264 CZ ARG B 55 16562 11203 7383 3947 1710 758 C ATOM 1265 NH1 ARG B 55 48.532 -38.439 40.681 1.00 97.51 N ANISOU 1265 NH1 ARG B 55 17211 11642 8196 3893 1550 767 N ATOM 1266 NH2 ARG B 55 47.743 -37.828 42.747 1.00 98.43 N ANISOU 1266 NH2 ARG B 55 17536 12046 7817 4107 1746 827 N ATOM 1267 N VAL B 56 46.489 -32.209 37.737 1.00 65.71 N ANISOU 1267 N VAL B 56 11988 8098 4881 3849 1340 -114 N ATOM 1268 CA VAL B 56 45.904 -31.642 36.527 1.00 66.21 C ANISOU 1268 CA VAL B 56 11773 8166 5216 3684 1332 -182 C ATOM 1269 C VAL B 56 46.890 -30.721 35.812 1.00 70.68 C ANISOU 1269 C VAL B 56 12209 8691 5957 3742 1048 -322 C ATOM 1270 O VAL B 56 47.048 -30.794 34.591 1.00 67.21 O ANISOU 1270 O VAL B 56 11625 8182 5729 3604 990 -318 O ATOM 1271 CB VAL B 56 44.608 -30.866 36.845 1.00 67.60 C ANISOU 1271 CB VAL B 56 11801 8493 5392 3672 1492 -236 C ATOM 1272 CG1 VAL B 56 44.156 -30.051 35.639 1.00 64.99 C ANISOU 1272 CG1 VAL B 56 11177 8162 5356 3529 1413 -332 C ATOM 1273 CG2 VAL B 56 43.512 -31.825 37.284 1.00 67.39 C ANISOU 1273 CG2 VAL B 56 11829 8502 5273 3564 1798 -48 C ATOM 1274 N LEU B 57 47.555 -29.860 36.577 1.00 76.63 N ANISOU 1274 N LEU B 57 13015 9482 6619 3951 862 -435 N ATOM 1275 CA LEU B 57 48.509 -28.909 36.011 1.00 59.12 C ANISOU 1275 CA LEU B 57 10653 7220 4590 4015 569 -541 C ATOM 1276 C LEU B 57 49.697 -29.625 35.389 1.00 68.75 C ANISOU 1276 C LEU B 57 11914 8306 5901 3997 459 -449 C ATOM 1277 O LEU B 57 50.236 -29.185 34.372 1.00 68.77 O ANISOU 1277 O LEU B 57 11731 8271 6127 3949 319 -467 O ATOM 1278 CB LEU B 57 48.993 -27.927 37.078 1.00 73.75 C ANISOU 1278 CB LEU B 57 12588 9107 6326 4252 358 -671 C ATOM 1279 CG LEU B 57 48.025 -26.827 37.508 1.00 74.45 C ANISOU 1279 CG LEU B 57 12580 9319 6388 4316 384 -821 C ATOM 1280 CD1 LEU B 57 48.575 -26.090 38.716 1.00 62.87 C ANISOU 1280 CD1 LEU B 57 11287 7862 4739 4582 169 -952 C ATOM 1281 CD2 LEU B 57 47.776 -25.866 36.360 1.00 59.18 C ANISOU 1281 CD2 LEU B 57 10325 7389 4772 4194 268 -900 C ATOM 1282 N LEU B 58 50.113 -30.727 36.000 1.00 65.65 N ANISOU 1282 N LEU B 58 11761 7844 5337 4045 528 -339 N ATOM 1283 CA LEU B 58 51.213 -31.519 35.464 1.00 66.84 C ANISOU 1283 CA LEU B 58 11963 7859 5573 4045 448 -248 C ATOM 1284 C LEU B 58 50.831 -32.160 34.136 1.00 69.10 C ANISOU 1284 C LEU B 58 12141 8101 6014 3848 585 -196 C ATOM 1285 O LEU B 58 51.649 -32.237 33.219 1.00 63.63 O ANISOU 1285 O LEU B 58 11361 7339 5478 3843 491 -180 O ATOM 1286 CB LEU B 58 51.651 -32.594 36.457 1.00 69.50 C ANISOU 1286 CB LEU B 58 12587 8121 5698 4133 489 -139 C ATOM 1287 CG LEU B 58 52.376 -32.128 37.721 1.00 75.70 C ANISOU 1287 CG LEU B 58 13533 8906 6322 4352 293 -175 C ATOM 1288 CD1 LEU B 58 52.651 -33.309 38.638 1.00 72.87 C ANISOU 1288 CD1 LEU B 58 13466 8477 5745 4405 361 -41 C ATOM 1289 CD2 LEU B 58 53.666 -31.400 37.374 1.00 64.26 C ANISOU 1289 CD2 LEU B 58 11962 7378 5075 4461 -16 -220 C ATOM 1290 N ILE B 59 49.590 -32.620 34.031 1.00 69.03 N ANISOU 1290 N ILE B 59 12139 8128 5961 3694 801 -161 N ATOM 1291 CA ILE B 59 49.126 -33.303 32.832 1.00 57.02 C ANISOU 1291 CA ILE B 59 10555 6540 4570 3502 906 -115 C ATOM 1292 C ILE B 59 48.791 -32.339 31.700 1.00 69.90 C ANISOU 1292 C ILE B 59 11927 8229 6401 3401 841 -205 C ATOM 1293 O ILE B 59 49.245 -32.512 30.566 1.00 64.20 O ANISOU 1293 O ILE B 59 11140 7449 5805 3346 791 -202 O ATOM 1294 CB ILE B 59 47.880 -34.163 33.130 1.00 62.79 C ANISOU 1294 CB ILE B 59 11372 7264 5222 3355 1132 -18 C ATOM 1295 CG1 ILE B 59 48.238 -35.253 34.145 1.00 78.13 C ANISOU 1295 CG1 ILE B 59 13575 9135 6976 3433 1195 106 C ATOM 1296 CG2 ILE B 59 47.351 -34.803 31.857 1.00 71.88 C ANISOU 1296 CG2 ILE B 59 12464 8321 6527 3151 1190 15 C ATOM 1297 CD1 ILE B 59 47.059 -36.093 34.583 1.00 82.51 C ANISOU 1297 CD1 ILE B 59 14205 9687 7459 3298 1413 245 C ATOM 1298 N SER B 60 47.986 -31.326 32.015 1.00 68.77 N ANISOU 1298 N SER B 60 11643 8204 6281 3387 846 -282 N ATOM 1299 CA SER B 60 47.523 -30.377 31.009 1.00 72.29 C ANISOU 1299 CA SER B 60 11835 8704 6927 3275 779 -357 C ATOM 1300 C SER B 60 48.641 -29.593 30.335 1.00 53.74 C ANISOU 1300 C SER B 60 9348 6352 4720 3353 559 -402 C ATOM 1301 O SER B 60 48.589 -29.353 29.131 1.00 78.79 O ANISOU 1301 O SER B 60 12369 9523 8046 3238 522 -403 O ATOM 1302 CB SER B 60 46.510 -29.405 31.615 1.00 64.64 C ANISOU 1302 CB SER B 60 10743 7854 5964 3279 815 -437 C ATOM 1303 OG SER B 60 45.303 -30.058 31.959 1.00 97.52 O ANISOU 1303 OG SER B 60 14957 12034 10061 3167 1045 -365 O ATOM 1304 N SER B 61 49.639 -29.189 31.112 1.00 66.20 N ANISOU 1304 N SER B 61 10975 7926 6251 3546 405 -423 N ATOM 1305 CA SER B 61 50.759 -28.414 30.581 1.00 59.38 C ANISOU 1305 CA SER B 61 9956 7051 5554 3629 179 -431 C ATOM 1306 C SER B 61 51.504 -29.223 29.536 1.00 73.68 C ANISOU 1306 C SER B 61 11781 8789 7424 3591 217 -336 C ATOM 1307 O SER B 61 51.996 -28.696 28.536 1.00 79.02 O ANISOU 1307 O SER B 61 12272 9485 8268 3569 124 -315 O ATOM 1308 CB SER B 61 51.708 -28.001 31.701 1.00 57.10 C ANISOU 1308 CB SER B 61 9750 6737 5210 3842 -13 -451 C ATOM 1309 OG SER B 61 52.281 -29.146 32.303 1.00 60.18 O ANISOU 1309 OG SER B 61 10385 7042 5439 3923 56 -370 O ATOM 1310 N VAL B 62 51.584 -30.521 29.793 1.00 74.51 N ANISOU 1310 N VAL B 62 12113 8810 7386 3596 360 -274 N ATOM 1311 CA VAL B 62 52.268 -31.448 28.918 1.00 56.26 C ANISOU 1311 CA VAL B 62 9864 6412 5100 3591 414 -202 C ATOM 1312 C VAL B 62 51.419 -31.820 27.700 1.00 68.41 C ANISOU 1312 C VAL B 62 11368 7949 6677 3402 539 -212 C ATOM 1313 O VAL B 62 51.938 -31.936 26.591 1.00 71.04 O ANISOU 1313 O VAL B 62 11642 8266 7082 3397 531 -191 O ATOM 1314 CB VAL B 62 52.665 -32.704 29.705 1.00 58.63 C ANISOU 1314 CB VAL B 62 10430 6599 5248 3673 490 -136 C ATOM 1315 CG1 VAL B 62 53.327 -33.687 28.825 1.00 79.75 C ANISOU 1315 CG1 VAL B 62 13181 9171 7951 3687 549 -81 C ATOM 1316 CG2 VAL B 62 53.607 -32.329 30.815 1.00 71.39 C ANISOU 1316 CG2 VAL B 62 12090 8202 6832 3863 330 -120 C ATOM 1317 N MET B 63 50.115 -31.995 27.898 1.00 71.36 N ANISOU 1317 N MET B 63 11776 8337 7003 3254 649 -237 N ATOM 1318 CA MET B 63 49.216 -32.286 26.781 1.00 65.64 C ANISOU 1318 CA MET B 63 11015 7590 6335 3058 725 -246 C ATOM 1319 C MET B 63 49.078 -31.089 25.843 1.00 65.84 C ANISOU 1319 C MET B 63 10786 7713 6516 2991 618 -294 C ATOM 1320 O MET B 63 48.810 -31.252 24.652 1.00 65.21 O ANISOU 1320 O MET B 63 10677 7615 6486 2874 630 -294 O ATOM 1321 CB MET B 63 47.840 -32.733 27.277 1.00 63.12 C ANISOU 1321 CB MET B 63 10759 7251 5971 2910 855 -231 C ATOM 1322 CG MET B 63 47.860 -34.075 27.989 1.00 81.17 C ANISOU 1322 CG MET B 63 13297 9424 8122 2933 967 -149 C ATOM 1323 SD MET B 63 46.228 -34.822 28.150 1.00114.81 S ANISOU 1323 SD MET B 63 17605 13626 12391 2712 1122 -75 S ATOM 1324 CE MET B 63 45.934 -35.360 26.468 1.00 86.41 C ANISOU 1324 CE MET B 63 14017 9905 8911 2539 1075 -97 C ATOM 1325 N LEU B 64 49.248 -29.887 26.389 1.00 55.22 N ANISOU 1325 N LEU B 64 9273 6465 5245 3066 498 -333 N ATOM 1326 CA LEU B 64 49.179 -28.666 25.592 1.00 48.66 C ANISOU 1326 CA LEU B 64 8182 5719 4587 3009 365 -362 C ATOM 1327 C LEU B 64 50.260 -28.675 24.518 1.00 58.31 C ANISOU 1327 C LEU B 64 9345 6941 5868 3059 306 -300 C ATOM 1328 O LEU B 64 50.057 -28.162 23.418 1.00 63.15 O ANISOU 1328 O LEU B 64 9808 7604 6582 2956 263 -290 O ATOM 1329 CB LEU B 64 49.325 -27.424 26.473 1.00 48.51 C ANISOU 1329 CB LEU B 64 8014 5773 4646 3114 210 -419 C ATOM 1330 CG LEU B 64 49.291 -26.086 25.728 1.00 63.45 C ANISOU 1330 CG LEU B 64 9619 7739 6750 3057 38 -438 C ATOM 1331 CD1 LEU B 64 47.934 -25.868 25.075 1.00 58.01 C ANISOU 1331 CD1 LEU B 64 8830 7079 6133 2847 100 -475 C ATOM 1332 CD2 LEU B 64 49.630 -24.937 26.661 1.00 47.71 C ANISOU 1332 CD2 LEU B 64 7510 5779 4839 3196 -158 -500 C ATOM 1333 N VAL B 65 51.410 -29.255 24.851 1.00 52.66 N ANISOU 1333 N VAL B 65 8744 6173 5092 3226 310 -246 N ATOM 1334 CA VAL B 65 52.508 -29.386 23.902 1.00 61.54 C ANISOU 1334 CA VAL B 65 9818 7301 6265 3308 295 -167 C ATOM 1335 C VAL B 65 52.053 -30.187 22.685 1.00 63.70 C ANISOU 1335 C VAL B 65 10198 7543 6461 3193 428 -172 C ATOM 1336 O VAL B 65 52.389 -29.852 21.549 1.00 64.21 O ANISOU 1336 O VAL B 65 10151 7669 6578 3180 413 -131 O ATOM 1337 CB VAL B 65 53.736 -30.071 24.546 1.00 53.44 C ANISOU 1337 CB VAL B 65 8920 6197 5190 3508 299 -104 C ATOM 1338 CG1 VAL B 65 54.818 -30.333 23.508 1.00 49.81 C ANISOU 1338 CG1 VAL B 65 8406 5742 4777 3606 333 -12 C ATOM 1339 CG2 VAL B 65 54.280 -29.225 25.687 1.00 49.53 C ANISOU 1339 CG2 VAL B 65 8328 5715 4775 3630 118 -97 C ATOM 1340 N MET B 66 51.275 -31.238 22.929 1.00 59.93 N ANISOU 1340 N MET B 66 9944 6967 5861 3110 544 -215 N ATOM 1341 CA MET B 66 50.746 -32.068 21.851 1.00 65.20 C ANISOU 1341 CA MET B 66 10750 7566 6456 2996 631 -237 C ATOM 1342 C MET B 66 49.698 -31.327 21.027 1.00 67.13 C ANISOU 1342 C MET B 66 10848 7875 6782 2796 578 -270 C ATOM 1343 O MET B 66 49.642 -31.470 19.805 1.00 70.57 O ANISOU 1343 O MET B 66 11309 8311 7192 2738 582 -274 O ATOM 1344 CB MET B 66 50.150 -33.359 22.413 1.00 62.16 C ANISOU 1344 CB MET B 66 10623 7033 5960 2945 731 -254 C ATOM 1345 CG MET B 66 51.145 -34.194 23.192 1.00 80.77 C ANISOU 1345 CG MET B 66 13144 9306 8238 3130 774 -214 C ATOM 1346 SD MET B 66 52.685 -34.452 22.289 1.00100.50 S ANISOU 1346 SD MET B 66 15653 11804 10730 3337 785 -179 S ATOM 1347 CE MET B 66 52.105 -35.422 20.906 1.00102.95 C ANISOU 1347 CE MET B 66 16161 12014 10943 3236 860 -244 C ATOM 1348 N ILE B 67 48.866 -30.541 21.702 1.00 72.09 N ANISOU 1348 N ILE B 67 11334 8555 7503 2703 527 -296 N ATOM 1349 CA ILE B 67 47.825 -29.771 21.032 1.00 61.59 C ANISOU 1349 CA ILE B 67 9839 7275 6287 2511 461 -323 C ATOM 1350 C ILE B 67 48.433 -28.746 20.081 1.00 66.28 C ANISOU 1350 C ILE B 67 10224 7981 6978 2531 346 -287 C ATOM 1351 O ILE B 67 48.025 -28.637 18.923 1.00 67.84 O ANISOU 1351 O ILE B 67 10394 8192 7189 2405 317 -282 O ATOM 1352 CB ILE B 67 46.921 -29.047 22.047 1.00 59.30 C ANISOU 1352 CB ILE B 67 9414 7027 6090 2451 437 -359 C ATOM 1353 CG1 ILE B 67 46.166 -30.058 22.909 1.00 67.88 C ANISOU 1353 CG1 ILE B 67 10687 8020 7086 2407 574 -358 C ATOM 1354 CG2 ILE B 67 45.945 -28.132 21.336 1.00 47.44 C ANISOU 1354 CG2 ILE B 67 7703 5575 4747 2267 348 -380 C ATOM 1355 CD1 ILE B 67 45.350 -29.424 24.010 1.00 49.18 C ANISOU 1355 CD1 ILE B 67 8206 5711 4770 2394 598 -385 C ATOM 1356 N VAL B 68 49.414 -28.000 20.577 1.00 58.90 N ANISOU 1356 N VAL B 68 9144 7120 6115 2686 267 -249 N ATOM 1357 CA VAL B 68 50.085 -26.979 19.782 1.00 60.48 C ANISOU 1357 CA VAL B 68 9111 7427 6440 2713 148 -175 C ATOM 1358 C VAL B 68 50.869 -27.605 18.629 1.00 62.13 C ANISOU 1358 C VAL B 68 9414 7648 6544 2777 233 -104 C ATOM 1359 O VAL B 68 50.904 -27.061 17.525 1.00 60.06 O ANISOU 1359 O VAL B 68 9027 7470 6324 2714 189 -46 O ATOM 1360 CB VAL B 68 51.030 -26.128 20.655 1.00 51.76 C ANISOU 1360 CB VAL B 68 7838 6366 5463 2875 17 -133 C ATOM 1361 CG1 VAL B 68 51.794 -25.123 19.805 1.00 57.54 C ANISOU 1361 CG1 VAL B 68 8308 7197 6356 2899 -112 -15 C ATOM 1362 CG2 VAL B 68 50.238 -25.417 21.738 1.00 49.27 C ANISOU 1362 CG2 VAL B 68 7444 6048 5229 2837 -75 -226 C ATOM 1363 N GLU B 69 51.487 -28.754 18.888 1.00 52.63 N ANISOU 1363 N GLU B 69 8437 6363 5197 2911 360 -107 N ATOM 1364 CA GLU B 69 52.240 -29.467 17.861 1.00 49.01 C ANISOU 1364 CA GLU B 69 8100 5905 4616 3010 468 -60 C ATOM 1365 C GLU B 69 51.339 -29.910 16.711 1.00 69.55 C ANISOU 1365 C GLU B 69 10844 8478 7102 2854 505 -120 C ATOM 1366 O GLU B 69 51.717 -29.807 15.543 1.00 73.25 O ANISOU 1366 O GLU B 69 11301 9021 7508 2883 532 -71 O ATOM 1367 CB GLU B 69 52.960 -30.675 18.461 1.00 60.81 C ANISOU 1367 CB GLU B 69 9823 7286 5995 3181 583 -71 C ATOM 1368 CG GLU B 69 53.699 -31.522 17.436 1.00 89.08 C ANISOU 1368 CG GLU B 69 13559 10851 9437 3312 713 -49 C ATOM 1369 CD GLU B 69 54.772 -30.746 16.692 1.00 92.64 C ANISOU 1369 CD GLU B 69 13781 11454 9963 3440 715 89 C ATOM 1370 OE1 GLU B 69 55.682 -30.202 17.350 1.00107.08 O ANISOU 1370 OE1 GLU B 69 15421 13324 11943 3565 658 192 O ATOM 1371 OE2 GLU B 69 54.706 -30.685 15.446 1.00 89.24 O ANISOU 1371 OE2 GLU B 69 13363 11100 9444 3418 768 108 O ATOM 1372 N LEU B 70 50.152 -30.406 17.046 1.00 60.93 N ANISOU 1372 N LEU B 70 9890 7275 5984 2693 502 -212 N ATOM 1373 CA LEU B 70 49.182 -30.817 16.036 1.00 52.04 C ANISOU 1373 CA LEU B 70 8901 6087 4783 2521 489 -268 C ATOM 1374 C LEU B 70 48.744 -29.625 15.194 1.00 63.68 C ANISOU 1374 C LEU B 70 10148 7684 6363 2381 369 -229 C ATOM 1375 O LEU B 70 48.585 -29.736 13.978 1.00 61.68 O ANISOU 1375 O LEU B 70 9976 7444 6014 2325 352 -230 O ATOM 1376 CB LEU B 70 47.967 -31.477 16.688 1.00 50.31 C ANISOU 1376 CB LEU B 70 8814 5719 4581 2361 489 -337 C ATOM 1377 CG LEU B 70 48.162 -32.901 17.209 1.00 65.06 C ANISOU 1377 CG LEU B 70 10968 7426 6326 2447 591 -370 C ATOM 1378 CD1 LEU B 70 47.021 -33.289 18.131 1.00 63.00 C ANISOU 1378 CD1 LEU B 70 10747 7057 6134 2294 594 -382 C ATOM 1379 CD2 LEU B 70 48.254 -33.867 16.043 1.00 60.89 C ANISOU 1379 CD2 LEU B 70 10702 6794 5641 2464 609 -421 C ATOM 1380 N LEU B 71 48.545 -28.488 15.850 1.00 59.25 N ANISOU 1380 N LEU B 71 9313 7204 5993 2333 271 -199 N ATOM 1381 CA LEU B 71 48.187 -27.256 15.159 1.00 65.34 C ANISOU 1381 CA LEU B 71 9834 8086 6907 2206 132 -149 C ATOM 1382 C LEU B 71 49.343 -26.791 14.280 1.00 70.10 C ANISOU 1382 C LEU B 71 10329 8823 7481 2333 134 -29 C ATOM 1383 O LEU B 71 49.134 -26.304 13.168 1.00 59.44 O ANISOU 1383 O LEU B 71 8910 7549 6127 2237 71 25 O ATOM 1384 CB LEU B 71 47.800 -26.170 16.164 1.00 58.38 C ANISOU 1384 CB LEU B 71 8693 7241 6246 2163 20 -159 C ATOM 1385 CG LEU B 71 46.458 -26.400 16.862 1.00 69.03 C ANISOU 1385 CG LEU B 71 10086 8493 7650 2012 26 -252 C ATOM 1386 CD1 LEU B 71 46.217 -25.368 17.952 1.00 62.24 C ANISOU 1386 CD1 LEU B 71 8999 7680 6970 2032 -57 -279 C ATOM 1387 CD2 LEU B 71 45.327 -26.382 15.846 1.00 46.82 C ANISOU 1387 CD2 LEU B 71 7278 5637 4873 1781 -42 -264 C ATOM 1388 N ASN B 72 50.561 -26.949 14.787 1.00 58.28 N ANISOU 1388 N ASN B 72 8815 7357 5971 2549 206 30 N ATOM 1389 CA ASN B 72 51.758 -26.626 14.023 1.00 60.62 C ANISOU 1389 CA ASN B 72 8999 7780 6253 2697 244 176 C ATOM 1390 C ASN B 72 51.878 -27.500 12.779 1.00 63.51 C ANISOU 1390 C ASN B 72 9608 8154 6370 2736 379 168 C ATOM 1391 O ASN B 72 52.212 -27.016 11.698 1.00 64.55 O ANISOU 1391 O ASN B 72 9646 8415 6463 2744 383 278 O ATOM 1392 CB ASN B 72 53.006 -26.783 14.894 1.00 61.82 C ANISOU 1392 CB ASN B 72 9100 7929 6459 2924 294 243 C ATOM 1393 CG ASN B 72 54.292 -26.649 14.101 1.00 65.59 C ANISOU 1393 CG ASN B 72 9469 8527 6924 3099 375 416 C ATOM 1394 OD1 ASN B 72 54.448 -25.728 13.300 1.00 70.25 O ANISOU 1394 OD1 ASN B 72 9837 9252 7603 3051 309 550 O ATOM 1395 ND2 ASN B 72 55.221 -27.573 14.320 1.00 63.53 N ANISOU 1395 ND2 ASN B 72 9354 8221 6564 3307 525 431 N ATOM 1396 N SER B 73 51.602 -28.791 12.942 1.00 61.79 N ANISOU 1396 N SER B 73 9711 7789 5976 2767 483 41 N ATOM 1397 CA SER B 73 51.648 -29.736 11.832 1.00 52.77 C ANISOU 1397 CA SER B 73 8856 6615 4580 2821 590 -10 C ATOM 1398 C SER B 73 50.587 -29.422 10.781 1.00 61.72 C ANISOU 1398 C SER B 73 10034 7759 5659 2606 481 -44 C ATOM 1399 O SER B 73 50.815 -29.595 9.583 1.00 65.79 O ANISOU 1399 O SER B 73 10674 8339 5984 2657 528 -24 O ATOM 1400 CB SER B 73 51.469 -31.166 12.345 1.00 53.50 C ANISOU 1400 CB SER B 73 9276 6508 4542 2877 674 -146 C ATOM 1401 OG SER B 73 52.543 -31.537 13.190 1.00 90.96 O ANISOU 1401 OG SER B 73 14005 11239 9317 3091 775 -105 O ATOM 1402 N ALA B 74 49.428 -28.960 11.238 1.00 70.85 N ANISOU 1402 N ALA B 74 11091 8850 6977 2376 334 -92 N ATOM 1403 CA ALA B 74 48.348 -28.578 10.338 1.00 62.32 C ANISOU 1403 CA ALA B 74 10017 7761 5900 2149 195 -113 C ATOM 1404 C ALA B 74 48.756 -27.368 9.509 1.00 62.90 C ANISOU 1404 C ALA B 74 9835 8033 6029 2135 129 36 C ATOM 1405 O ALA B 74 48.479 -27.302 8.311 1.00 63.22 O ANISOU 1405 O ALA B 74 9970 8117 5935 2064 83 56 O ATOM 1406 CB ALA B 74 47.080 -28.287 11.121 1.00 56.09 C ANISOU 1406 CB ALA B 74 9126 6867 5321 1926 69 -174 C ATOM 1407 N ILE B 75 49.416 -26.414 10.156 1.00 63.22 N ANISOU 1407 N ILE B 75 9560 8187 6273 2203 106 148 N ATOM 1408 CA ILE B 75 49.902 -25.221 9.477 1.00 62.94 C ANISOU 1408 CA ILE B 75 9240 8334 6339 2195 30 325 C ATOM 1409 C ILE B 75 50.987 -25.595 8.469 1.00 65.42 C ANISOU 1409 C ILE B 75 9657 8776 6422 2393 196 436 C ATOM 1410 O ILE B 75 51.016 -25.072 7.354 1.00 61.76 O ANISOU 1410 O ILE B 75 9136 8442 5887 2346 166 551 O ATOM 1411 CB ILE B 75 50.441 -24.183 10.483 1.00 65.71 C ANISOU 1411 CB ILE B 75 9240 8743 6984 2242 -58 419 C ATOM 1412 CG1 ILE B 75 49.298 -23.651 11.351 1.00 72.46 C ANISOU 1412 CG1 ILE B 75 9978 9498 8054 2057 -222 310 C ATOM 1413 CG2 ILE B 75 51.127 -23.036 9.762 1.00 63.13 C ANISOU 1413 CG2 ILE B 75 8611 8595 6780 2257 -135 640 C ATOM 1414 CD1 ILE B 75 49.745 -22.711 12.447 1.00 60.60 C ANISOU 1414 CD1 ILE B 75 8190 8021 6815 2121 -331 354 C ATOM 1415 N GLU B 76 51.866 -26.514 8.861 1.00 61.45 N ANISOU 1415 N GLU B 76 9312 8238 5797 2621 379 407 N ATOM 1416 CA GLU B 76 52.900 -27.010 7.957 1.00 66.11 C ANISOU 1416 CA GLU B 76 10023 8940 6155 2847 577 494 C ATOM 1417 C GLU B 76 52.294 -27.700 6.742 1.00 71.50 C ANISOU 1417 C GLU B 76 11047 9595 6525 2803 608 391 C ATOM 1418 O GLU B 76 52.806 -27.575 5.630 1.00 66.77 O ANISOU 1418 O GLU B 76 10480 9152 5738 2905 704 499 O ATOM 1419 CB GLU B 76 53.835 -27.983 8.674 1.00 67.14 C ANISOU 1419 CB GLU B 76 10283 8997 6230 3094 754 453 C ATOM 1420 CG GLU B 76 54.837 -27.354 9.620 1.00 86.56 C ANISOU 1420 CG GLU B 76 12423 11514 8952 3214 747 604 C ATOM 1421 CD GLU B 76 55.674 -28.407 10.314 1.00114.38 C ANISOU 1421 CD GLU B 76 16104 14938 12418 3444 903 553 C ATOM 1422 OE1 GLU B 76 55.416 -29.605 10.073 1.00127.72 O ANISOU 1422 OE1 GLU B 76 18146 16511 13872 3500 1011 394 O ATOM 1423 OE2 GLU B 76 56.599 -28.050 11.073 1.00127.08 O ANISOU 1423 OE2 GLU B 76 17488 16571 14225 3569 898 677 O ATOM 1424 N ALA B 77 51.200 -28.423 6.961 1.00 75.28 N ANISOU 1424 N ALA B 77 11781 9873 6949 2654 519 190 N ATOM 1425 CA ALA B 77 50.527 -29.143 5.887 1.00 58.69 C ANISOU 1425 CA ALA B 77 10036 7692 4572 2596 491 68 C ATOM 1426 C ALA B 77 49.941 -28.157 4.887 1.00 58.95 C ANISOU 1426 C ALA B 77 9948 7844 4608 2408 338 165 C ATOM 1427 O ALA B 77 49.966 -28.390 3.679 1.00 61.06 O ANISOU 1427 O ALA B 77 10432 8171 4597 2453 363 165 O ATOM 1428 CB ALA B 77 49.441 -30.050 6.446 1.00 58.31 C ANISOU 1428 CB ALA B 77 10231 7380 4544 2448 389 -132 C ATOM 1429 N VAL B 78 49.411 -27.055 5.405 1.00 56.99 N ANISOU 1429 N VAL B 78 9362 7623 4668 2206 170 243 N ATOM 1430 CA VAL B 78 48.868 -25.995 4.567 1.00 57.07 C ANISOU 1430 CA VAL B 78 9201 7739 4744 2013 -1 357 C ATOM 1431 C VAL B 78 49.975 -25.362 3.724 1.00 58.38 C ANISOU 1431 C VAL B 78 9215 8161 4806 2171 112 582 C ATOM 1432 O VAL B 78 49.805 -25.144 2.524 1.00 60.23 O ANISOU 1432 O VAL B 78 9544 8493 4847 2125 75 651 O ATOM 1433 CB VAL B 78 48.175 -24.909 5.411 1.00 57.51 C ANISOU 1433 CB VAL B 78 8897 7766 5189 1797 -198 394 C ATOM 1434 CG1 VAL B 78 47.774 -23.743 4.536 1.00 58.80 C ANISOU 1434 CG1 VAL B 78 8846 8047 5448 1617 -380 541 C ATOM 1435 CG2 VAL B 78 46.957 -25.482 6.114 1.00 55.01 C ANISOU 1435 CG2 VAL B 78 8713 7217 4970 1626 -297 204 C ATOM 1436 N VAL B 79 51.103 -25.062 4.362 1.00 82.11 N ANISOU 1436 N VAL B 79 11980 11270 7946 2356 243 712 N ATOM 1437 CA VAL B 79 52.255 -24.482 3.676 1.00 72.42 C ANISOU 1437 CA VAL B 79 10560 10286 6671 2523 374 967 C ATOM 1438 C VAL B 79 52.741 -25.400 2.556 1.00 76.35 C ANISOU 1438 C VAL B 79 11408 10863 6737 2731 595 947 C ATOM 1439 O VAL B 79 53.035 -24.949 1.446 1.00 64.02 O ANISOU 1439 O VAL B 79 9816 9495 5013 2764 644 1119 O ATOM 1440 CB VAL B 79 53.415 -24.209 4.657 1.00 70.26 C ANISOU 1440 CB VAL B 79 9999 10063 6634 2705 471 1097 C ATOM 1441 CG1 VAL B 79 54.668 -23.784 3.905 1.00 60.39 C ANISOU 1441 CG1 VAL B 79 8560 9056 5331 2902 641 1384 C ATOM 1442 CG2 VAL B 79 53.012 -23.149 5.671 1.00 65.87 C ANISOU 1442 CG2 VAL B 79 9093 9449 6486 2524 232 1128 C ATOM 1443 N ASP B 80 52.807 -26.694 2.857 1.00 62.72 N ANISOU 1443 N ASP B 80 10024 8985 4824 2876 723 737 N ATOM 1444 CA ASP B 80 53.222 -27.701 1.887 1.00 65.66 C ANISOU 1444 CA ASP B 80 10781 9390 4777 3102 924 661 C ATOM 1445 C ASP B 80 52.237 -27.752 0.721 1.00 67.15 C ANISOU 1445 C ASP B 80 11249 9558 4707 2943 780 576 C ATOM 1446 O ASP B 80 52.624 -27.987 -0.424 1.00 85.03 O ANISOU 1446 O ASP B 80 13724 11960 6622 3102 911 617 O ATOM 1447 CB ASP B 80 53.336 -29.072 2.556 1.00 65.82 C ANISOU 1447 CB ASP B 80 11110 9196 4703 3254 1027 429 C ATOM 1448 CG ASP B 80 54.441 -29.124 3.596 1.00110.33 C ANISOU 1448 CG ASP B 80 16515 14857 10549 3448 1182 521 C ATOM 1449 OD1 ASP B 80 55.029 -28.063 3.893 1.00107.83 O ANISOU 1449 OD1 ASP B 80 15787 14697 10485 3441 1174 754 O ATOM 1450 OD2 ASP B 80 54.717 -30.224 4.121 1.00105.01 O ANISOU 1450 OD2 ASP B 80 16069 14028 9801 3603 1287 368 O ATOM 1451 N ARG B 81 50.962 -27.529 1.027 1.00 79.37 N ANISOU 1451 N ARG B 81 12797 10934 6427 2637 507 463 N ATOM 1452 CA ARG B 81 49.913 -27.483 0.016 1.00 82.49 C ANISOU 1452 CA ARG B 81 13420 11276 6648 2440 306 394 C ATOM 1453 C ARG B 81 50.135 -26.300 -0.921 1.00 67.54 C ANISOU 1453 C ARG B 81 11295 9640 4729 2382 271 650 C ATOM 1454 O ARG B 81 49.946 -26.406 -2.131 1.00 70.91 O ANISOU 1454 O ARG B 81 11975 10137 4830 2394 249 657 O ATOM 1455 CB ARG B 81 48.540 -27.391 0.689 1.00 77.06 C ANISOU 1455 CB ARG B 81 12691 10349 6239 2119 26 261 C ATOM 1456 CG ARG B 81 47.352 -27.238 -0.250 1.00 78.09 C ANISOU 1456 CG ARG B 81 12999 10392 6280 1870 -236 209 C ATOM 1457 CD ARG B 81 47.088 -28.497 -1.051 1.00 72.61 C ANISOU 1457 CD ARG B 81 12846 9547 5196 1963 -244 6 C ATOM 1458 NE ARG B 81 45.870 -28.378 -1.849 1.00 97.14 N ANISOU 1458 NE ARG B 81 16126 12524 8258 1700 -547 -51 N ATOM 1459 CZ ARG B 81 45.840 -28.022 -3.129 1.00100.92 C ANISOU 1459 CZ ARG B 81 16751 13131 8462 1692 -620 26 C ATOM 1460 NH1 ARG B 81 46.965 -27.743 -3.771 1.00103.03 N ANISOU 1460 NH1 ARG B 81 17001 13681 8466 1941 -381 175 N ATOM 1461 NH2 ARG B 81 44.679 -27.942 -3.765 1.00106.79 N ANISOU 1461 NH2 ARG B 81 17653 13723 9200 1436 -933 -31 N ATOM 1462 N ILE B 82 50.543 -25.173 -0.345 1.00 65.69 N ANISOU 1462 N ILE B 82 10584 9535 4839 2324 250 865 N ATOM 1463 CA ILE B 82 50.891 -23.987 -1.119 1.00 73.21 C ANISOU 1463 CA ILE B 82 11251 10736 5830 2277 220 1155 C ATOM 1464 C ILE B 82 52.141 -24.228 -1.962 1.00 81.06 C ANISOU 1464 C ILE B 82 12324 11977 6498 2592 529 1324 C ATOM 1465 O ILE B 82 52.200 -23.840 -3.130 1.00 71.70 O ANISOU 1465 O ILE B 82 11193 10974 5076 2595 544 1478 O ATOM 1466 CB ILE B 82 51.119 -22.776 -0.199 1.00 71.80 C ANISOU 1466 CB ILE B 82 10540 10608 6134 2164 109 1339 C ATOM 1467 CG1 ILE B 82 49.812 -22.364 0.467 1.00 85.85 C ANISOU 1467 CG1 ILE B 82 12220 12181 8220 1853 -193 1197 C ATOM 1468 CG2 ILE B 82 51.687 -21.601 -0.971 1.00 69.67 C ANISOU 1468 CG2 ILE B 82 9948 10597 5924 2150 98 1680 C ATOM 1469 CD1 ILE B 82 49.976 -21.205 1.403 1.00 97.30 C ANISOU 1469 CD1 ILE B 82 13188 13653 10128 1761 -324 1334 C ATOM 1470 N GLY B 83 53.127 -24.882 -1.361 1.00 76.89 N ANISOU 1470 N GLY B 83 11803 11455 5957 2862 779 1301 N ATOM 1471 CA GLY B 83 54.385 -25.155 -2.023 1.00 88.94 C ANISOU 1471 CA GLY B 83 13366 13209 7220 3194 1108 1466 C ATOM 1472 C GLY B 83 54.294 -26.087 -3.222 1.00 93.39 C ANISOU 1472 C GLY B 83 14441 13805 7238 3363 1245 1326 C ATOM 1473 O GLY B 83 55.186 -26.119 -4.053 1.00 87.65 O ANISOU 1473 O GLY B 83 13748 13317 6240 3617 1509 1496 O ATOM 1474 N SER B 84 53.195 -26.846 -3.305 1.00 74.67 N ANISOU 1474 N SER B 84 7877 14054 6441 3306 301 -1408 N ATOM 1475 CA SER B 84 53.019 -27.750 -4.438 1.00 84.53 C ANISOU 1475 CA SER B 84 8987 15767 7364 3435 205 -1825 C ATOM 1476 C SER B 84 52.546 -26.992 -5.673 1.00 91.66 C ANISOU 1476 C SER B 84 9958 17175 7692 3581 157 -1591 C ATOM 1477 O SER B 84 52.797 -27.417 -6.801 1.00103.38 O ANISOU 1477 O SER B 84 11362 19168 8750 3676 169 -1822 O ATOM 1478 CB SER B 84 52.044 -28.862 -4.077 1.00 81.82 C ANISOU 1478 CB SER B 84 8528 15246 7315 3455 -28 -2276 C ATOM 1479 OG SER B 84 50.780 -28.332 -3.699 1.00 94.20 O ANISOU 1479 OG SER B 84 10133 16673 8985 3478 -203 -2096 O ATOM 1480 N GLU B 85 51.828 -25.899 -5.461 1.00 90.09 N ANISOU 1480 N GLU B 85 9917 16845 7468 3628 90 -1150 N ATOM 1481 CA GLU B 85 51.445 -25.000 -6.545 1.00 89.45 C ANISOU 1481 CA GLU B 85 9971 17181 6835 3801 52 -807 C ATOM 1482 C GLU B 85 52.482 -23.894 -6.791 1.00 94.28 C ANISOU 1482 C GLU B 85 10801 17802 7217 3698 359 -285 C ATOM 1483 O GLU B 85 52.849 -23.621 -7.926 1.00119.12 O ANISOU 1483 O GLU B 85 14016 21423 9819 3765 463 -147 O ATOM 1484 CB GLU B 85 50.071 -24.390 -6.285 1.00113.30 C ANISOU 1484 CB GLU B 85 13052 20075 9923 3965 -203 -611 C ATOM 1485 CG GLU B 85 48.961 -25.418 -6.212 1.00137.41 C ANISOU 1485 CG GLU B 85 15857 23218 13136 4040 -496 -1132 C ATOM 1486 CD GLU B 85 48.666 -26.051 -7.563 1.00160.47 C ANISOU 1486 CD GLU B 85 18635 26795 15541 4205 -654 -1482 C ATOM 1487 OE1 GLU B 85 48.787 -25.352 -8.594 1.00169.83 O ANISOU 1487 OE1 GLU B 85 19953 28413 16161 4376 -639 -1182 O ATOM 1488 OE2 GLU B 85 48.314 -27.252 -7.589 1.00173.71 O ANISOU 1488 OE2 GLU B 85 20083 28548 17370 4156 -788 -2062 O ATOM 1489 N TYR B 86 52.907 -23.238 -5.713 1.00 91.29 N ANISOU 1489 N TYR B 86 10537 16901 7247 3517 507 1 N ATOM 1490 CA TYR B 86 53.786 -22.073 -5.784 1.00 84.44 C ANISOU 1490 CA TYR B 86 9890 15938 6255 3361 802 509 C ATOM 1491 C TYR B 86 55.256 -22.456 -5.544 1.00 84.32 C ANISOU 1491 C TYR B 86 9735 15935 6369 3106 1093 345 C ATOM 1492 O TYR B 86 55.542 -23.350 -4.748 1.00 89.57 O ANISOU 1492 O TYR B 86 10202 16400 7430 3044 1049 -41 O ATOM 1493 CB TYR B 86 53.300 -21.036 -4.779 1.00 88.11 C ANISOU 1493 CB TYR B 86 10560 15836 7080 3325 772 892 C ATOM 1494 CG TYR B 86 51.885 -20.597 -5.098 1.00114.11 C ANISOU 1494 CG TYR B 86 13966 19176 10215 3625 489 1055 C ATOM 1495 CD1 TYR B 86 51.444 -20.517 -6.405 1.00138.41 C ANISOU 1495 CD1 TYR B 86 17099 22779 12713 3864 380 1142 C ATOM 1496 CD2 TYR B 86 50.963 -20.362 -4.080 1.00120.23 C ANISOU 1496 CD2 TYR B 86 14748 19527 11407 3695 310 1063 C ATOM 1497 CE1 TYR B 86 50.149 -20.157 -6.705 1.00150.99 C ANISOU 1497 CE1 TYR B 86 18750 24471 14149 4182 84 1255 C ATOM 1498 CE2 TYR B 86 49.656 -20.010 -4.372 1.00130.67 C ANISOU 1498 CE2 TYR B 86 16109 20946 12594 4000 36 1157 C ATOM 1499 CZ TYR B 86 49.256 -19.903 -5.682 1.00151.80 C ANISOU 1499 CZ TYR B 86 18832 24145 14700 4253 -89 1254 C ATOM 1500 OH TYR B 86 47.959 -19.543 -5.976 1.00164.47 O ANISOU 1500 OH TYR B 86 20444 25890 16157 4596 -391 1333 O ATOM 1501 N HIS B 87 56.193 -21.764 -6.201 1.00 84.24 N ANISOU 1501 N HIS B 87 9825 16154 6029 2960 1397 648 N ATOM 1502 CA HIS B 87 57.615 -22.110 -6.055 1.00 79.36 C ANISOU 1502 CA HIS B 87 9010 15640 5503 2725 1682 459 C ATOM 1503 C HIS B 87 58.364 -21.589 -4.821 1.00 94.78 C ANISOU 1503 C HIS B 87 10957 17102 7952 2450 1841 590 C ATOM 1504 O HIS B 87 59.147 -22.330 -4.220 1.00 96.43 O ANISOU 1504 O HIS B 87 10914 17275 8451 2368 1886 231 O ATOM 1505 CB HIS B 87 58.412 -21.660 -7.296 1.00 84.92 C ANISOU 1505 CB HIS B 87 9764 16871 5631 2630 1994 675 C ATOM 1506 CG HIS B 87 58.028 -22.352 -8.569 1.00 88.45 C ANISOU 1506 CG HIS B 87 10143 17935 5530 2875 1889 431 C ATOM 1507 ND1 HIS B 87 58.731 -22.184 -9.743 1.00102.53 N ANISOU 1507 ND1 HIS B 87 11935 20144 6879 2771 2103 519 N ATOM 1508 CD2 HIS B 87 57.029 -23.219 -8.850 1.00 87.84 C ANISOU 1508 CD2 HIS B 87 9978 18015 5383 3155 1551 65 C ATOM 1509 CE1 HIS B 87 58.185 -22.924 -10.691 1.00 96.20 C ANISOU 1509 CE1 HIS B 87 11055 19693 5803 2983 1874 218 C ATOM 1510 NE2 HIS B 87 57.146 -23.558 -10.177 1.00 92.71 N ANISOU 1510 NE2 HIS B 87 10546 19119 5560 3217 1541 -66 N ATOM 1511 N GLU B 88 58.129 -20.339 -4.433 1.00 84.78 N ANISOU 1511 N GLU B 88 9967 15460 6786 2331 1911 1076 N ATOM 1512 CA GLU B 88 58.926 -19.711 -3.376 1.00 80.05 C ANISOU 1512 CA GLU B 88 9369 14446 6598 2030 2093 1200 C ATOM 1513 C GLU B 88 58.279 -19.762 -1.996 1.00 73.84 C ANISOU 1513 C GLU B 88 8604 13114 6338 2077 1860 1110 C ATOM 1514 O GLU B 88 57.143 -19.327 -1.815 1.00 83.22 O ANISOU 1514 O GLU B 88 9997 14049 7575 2242 1669 1303 O ATOM 1515 CB GLU B 88 59.202 -18.250 -3.731 1.00 92.41 C ANISOU 1515 CB GLU B 88 11247 15874 7990 1810 2361 1770 C ATOM 1516 CG GLU B 88 60.465 -18.011 -4.522 1.00125.88 C ANISOU 1516 CG GLU B 88 15401 20509 11917 1530 2753 1857 C ATOM 1517 CD GLU B 88 61.186 -16.740 -4.103 1.00144.68 C ANISOU 1517 CD GLU B 88 17959 22535 14478 1127 3066 2242 C ATOM 1518 OE1 GLU B 88 61.220 -16.450 -2.888 1.00143.37 O ANISOU 1518 OE1 GLU B 88 17783 21882 14811 1006 2996 2189 O ATOM 1519 OE2 GLU B 88 61.726 -16.038 -4.986 1.00156.86 O ANISOU 1519 OE2 GLU B 88 19656 24288 15656 914 3393 2588 O ATOM 1520 N LEU B 89 58.985 -20.352 -1.038 1.00 81.76 N ANISOU 1520 N LEU B 89 9377 13979 7708 1962 1868 795 N ATOM 1521 CA LEU B 89 58.495 -20.443 0.333 1.00 79.64 C ANISOU 1521 CA LEU B 89 9124 13228 7907 1985 1678 702 C ATOM 1522 C LEU B 89 59.386 -19.645 1.290 1.00 68.08 C ANISOU 1522 C LEU B 89 7664 11459 6743 1685 1855 823 C ATOM 1523 O LEU B 89 60.554 -19.986 1.475 1.00 62.85 O ANISOU 1523 O LEU B 89 6761 10968 6150 1529 1994 613 O ATOM 1524 CB LEU B 89 58.395 -21.905 0.762 1.00 73.80 C ANISOU 1524 CB LEU B 89 8152 12544 7346 2152 1478 222 C ATOM 1525 CG LEU B 89 57.195 -22.619 0.133 1.00 72.26 C ANISOU 1525 CG LEU B 89 7979 12499 6978 2420 1245 75 C ATOM 1526 CD1 LEU B 89 57.006 -24.029 0.693 1.00 69.37 C ANISOU 1526 CD1 LEU B 89 7441 12057 6861 2542 1058 -380 C ATOM 1527 CD2 LEU B 89 55.944 -21.775 0.304 1.00 69.33 C ANISOU 1527 CD2 LEU B 89 7842 11871 6630 2505 1112 382 C ATOM 1528 N SER B 90 58.838 -18.594 1.897 1.00 61.75 N ANISOU 1528 N SER B 90 7116 10225 6123 1617 1840 1122 N ATOM 1529 CA SER B 90 59.606 -17.773 2.837 1.00 70.13 C ANISOU 1529 CA SER B 90 8196 10969 7481 1316 1994 1204 C ATOM 1530 C SER B 90 59.963 -18.512 4.127 1.00 72.28 C ANISOU 1530 C SER B 90 8244 11108 8110 1311 1857 842 C ATOM 1531 O SER B 90 60.959 -18.192 4.774 1.00 85.46 O ANISOU 1531 O SER B 90 9787 12717 9965 1063 1982 765 O ATOM 1532 CB SER B 90 58.841 -16.489 3.175 1.00 66.28 C ANISOU 1532 CB SER B 90 8061 10014 7110 1286 1993 1577 C ATOM 1533 OG SER B 90 57.704 -16.762 3.971 1.00 66.08 O ANISOU 1533 OG SER B 90 8091 9720 7295 1526 1723 1479 O ATOM 1534 N GLY B 91 59.137 -19.484 4.508 1.00 60.74 N ANISOU 1534 N GLY B 91 6739 9603 6735 1576 1601 625 N ATOM 1535 CA GLY B 91 59.368 -20.214 5.744 1.00 68.65 C ANISOU 1535 CA GLY B 91 7594 10450 8041 1605 1462 335 C ATOM 1536 C GLY B 91 58.833 -19.552 7.002 1.00 71.63 C ANISOU 1536 C GLY B 91 8131 10379 8706 1551 1381 429 C ATOM 1537 O GLY B 91 58.853 -20.156 8.076 1.00 51.39 O ANISOU 1537 O GLY B 91 5489 7681 6356 1602 1249 221 O ATOM 1538 N ARG B 92 58.353 -18.318 6.876 1.00 76.40 N ANISOU 1538 N ARG B 92 8976 10749 9304 1468 1463 741 N ATOM 1539 CA ARG B 92 57.893 -17.546 8.032 1.00 68.81 C ANISOU 1539 CA ARG B 92 8173 9360 8612 1412 1415 812 C ATOM 1540 C ARG B 92 56.758 -18.208 8.814 1.00 67.47 C ANISOU 1540 C ARG B 92 8022 9038 8576 1642 1189 671 C ATOM 1541 O ARG B 92 56.771 -18.213 10.044 1.00 83.01 O ANISOU 1541 O ARG B 92 9982 10790 10766 1598 1129 549 O ATOM 1542 CB ARG B 92 57.460 -16.145 7.589 1.00 66.23 C ANISOU 1542 CB ARG B 92 8139 8783 8240 1348 1534 1179 C ATOM 1543 CG ARG B 92 58.633 -15.257 7.215 1.00 82.16 C ANISOU 1543 CG ARG B 92 10187 10804 10227 1010 1806 1333 C ATOM 1544 CD ARG B 92 58.242 -13.792 7.122 1.00 98.73 C ANISOU 1544 CD ARG B 92 12639 12491 12383 917 1925 1689 C ATOM 1545 NE ARG B 92 57.512 -13.488 5.896 1.00 99.32 N ANISOU 1545 NE ARG B 92 12935 12642 12160 1118 1933 2019 N ATOM 1546 CZ ARG B 92 58.082 -13.134 4.748 1.00119.06 C ANISOU 1546 CZ ARG B 92 15518 15343 14379 983 2147 2269 C ATOM 1547 NH1 ARG B 92 59.401 -13.036 4.649 1.00126.94 N ANISOU 1547 NH1 ARG B 92 16361 16492 15378 615 2395 2208 N ATOM 1548 NH2 ARG B 92 57.323 -12.873 3.695 1.00125.45 N ANISOU 1548 NH2 ARG B 92 16550 16233 14883 1220 2114 2577 N ATOM 1549 N ALA B 93 55.781 -18.757 8.099 1.00 64.05 N ANISOU 1549 N ALA B 93 7602 8743 7990 1868 1073 677 N ATOM 1550 CA ALA B 93 54.653 -19.438 8.729 1.00 55.77 C ANISOU 1550 CA ALA B 93 6540 7589 7061 2045 888 530 C ATOM 1551 C ALA B 93 55.111 -20.623 9.578 1.00 62.22 C ANISOU 1551 C ALA B 93 7203 8422 8016 2030 816 240 C ATOM 1552 O ALA B 93 54.616 -20.833 10.684 1.00 65.72 O ANISOU 1552 O ALA B 93 7679 8652 8640 2049 739 158 O ATOM 1553 CB ALA B 93 53.660 -19.896 7.676 1.00 58.87 C ANISOU 1553 CB ALA B 93 6915 8204 7248 2254 780 532 C ATOM 1554 N LYS B 94 56.057 -21.391 9.049 1.00 57.51 N ANISOU 1554 N LYS B 94 6451 8083 7317 2016 848 93 N ATOM 1555 CA LYS B 94 56.582 -22.565 9.744 1.00 52.10 C ANISOU 1555 CA LYS B 94 5640 7408 6746 2058 767 -169 C ATOM 1556 C LYS B 94 57.466 -22.178 10.926 1.00 70.01 C ANISOU 1556 C LYS B 94 7886 9536 9180 1927 796 -193 C ATOM 1557 O LYS B 94 57.532 -22.900 11.922 1.00 65.86 O ANISOU 1557 O LYS B 94 7347 8898 8780 1989 692 -334 O ATOM 1558 CB LYS B 94 57.352 -23.464 8.773 1.00 42.94 C ANISOU 1558 CB LYS B 94 4309 6577 5428 2129 788 -349 C ATOM 1559 CG LYS B 94 56.444 -24.283 7.868 1.00 52.64 C ANISOU 1559 CG LYS B 94 5536 7937 6527 2288 698 -458 C ATOM 1560 CD LYS B 94 57.216 -25.286 7.030 1.00 60.95 C ANISOU 1560 CD LYS B 94 6422 9290 7446 2381 710 -707 C ATOM 1561 CE LYS B 94 56.263 -26.226 6.306 1.00 71.40 C ANISOU 1561 CE LYS B 94 7745 10698 8685 2524 593 -891 C ATOM 1562 NZ LYS B 94 56.967 -27.115 5.343 1.00 71.74 N ANISOU 1562 NZ LYS B 94 7638 11055 8567 2629 615 -1160 N ATOM 1563 N ASP B 95 58.153 -21.046 10.805 1.00 64.00 N ANISOU 1563 N ASP B 95 7126 8786 8406 1738 938 -58 N ATOM 1564 CA ASP B 95 58.979 -20.531 11.893 1.00 60.41 C ANISOU 1564 CA ASP B 95 6627 8222 8105 1577 963 -112 C ATOM 1565 C ASP B 95 58.113 -20.171 13.098 1.00 66.85 C ANISOU 1565 C ASP B 95 7613 8710 9076 1596 877 -78 C ATOM 1566 O ASP B 95 58.438 -20.515 14.234 1.00 64.72 O ANISOU 1566 O ASP B 95 7308 8380 8904 1605 789 -218 O ATOM 1567 CB ASP B 95 59.774 -19.304 11.437 1.00 52.49 C ANISOU 1567 CB ASP B 95 5609 7258 7076 1313 1163 24 C ATOM 1568 CG ASP B 95 60.881 -19.651 10.462 1.00 68.24 C ANISOU 1568 CG ASP B 95 7376 9635 8918 1246 1285 -57 C ATOM 1569 OD1 ASP B 95 61.338 -20.813 10.468 1.00 75.80 O ANISOU 1569 OD1 ASP B 95 8141 10814 9845 1407 1189 -289 O ATOM 1570 OD2 ASP B 95 61.298 -18.760 9.693 1.00 83.88 O ANISOU 1570 OD2 ASP B 95 9379 11686 10806 1036 1490 113 O ATOM 1571 N LEU B 96 57.012 -19.474 12.836 1.00 55.91 N ANISOU 1571 N LEU B 96 6408 7144 7691 1627 899 102 N ATOM 1572 CA LEU B 96 56.076 -19.075 13.881 1.00 51.56 C ANISOU 1572 CA LEU B 96 6002 6313 7275 1665 841 119 C ATOM 1573 C LEU B 96 55.443 -20.286 14.558 1.00 59.52 C ANISOU 1573 C LEU B 96 6987 7319 8310 1816 708 -26 C ATOM 1574 O LEU B 96 55.245 -20.297 15.773 1.00 66.19 O ANISOU 1574 O LEU B 96 7886 8017 9247 1806 666 -95 O ATOM 1575 CB LEU B 96 54.991 -18.168 13.301 1.00 42.26 C ANISOU 1575 CB LEU B 96 4990 4987 6080 1733 879 326 C ATOM 1576 CG LEU B 96 55.479 -16.788 12.857 1.00 55.66 C ANISOU 1576 CG LEU B 96 6812 6549 7787 1572 1028 523 C ATOM 1577 CD1 LEU B 96 54.416 -16.077 12.038 1.00 49.98 C ANISOU 1577 CD1 LEU B 96 6269 5724 6997 1727 1035 762 C ATOM 1578 CD2 LEU B 96 55.876 -15.951 14.064 1.00 51.06 C ANISOU 1578 CD2 LEU B 96 6298 5704 7399 1401 1071 449 C ATOM 1579 N GLY B 97 55.121 -21.301 13.763 1.00 61.35 N ANISOU 1579 N GLY B 97 7151 7709 8452 1939 655 -77 N ATOM 1580 CA GLY B 97 54.566 -22.535 14.287 1.00 56.68 C ANISOU 1580 CA GLY B 97 6557 7080 7900 2043 556 -211 C ATOM 1581 C GLY B 97 55.554 -23.232 15.202 1.00 64.80 C ANISOU 1581 C GLY B 97 7547 8104 8968 2045 502 -337 C ATOM 1582 O GLY B 97 55.175 -23.775 16.239 1.00 56.31 O ANISOU 1582 O GLY B 97 6556 6887 7951 2080 446 -378 O ATOM 1583 N SER B 98 56.825 -23.216 14.811 1.00 47.85 N ANISOU 1583 N SER B 98 5268 6138 6774 2016 522 -394 N ATOM 1584 CA SER B 98 57.886 -23.797 15.623 1.00 61.14 C ANISOU 1584 CA SER B 98 6873 7875 8481 2062 444 -527 C ATOM 1585 C SER B 98 58.064 -23.003 16.910 1.00 66.41 C ANISOU 1585 C SER B 98 7602 8422 9210 1959 431 -509 C ATOM 1586 O SER B 98 58.375 -23.564 17.961 1.00 67.30 O ANISOU 1586 O SER B 98 7742 8504 9326 2041 326 -585 O ATOM 1587 CB SER B 98 59.201 -23.841 14.844 1.00 60.37 C ANISOU 1587 CB SER B 98 6556 8063 8320 2048 484 -626 C ATOM 1588 OG SER B 98 59.217 -24.919 13.926 1.00 72.59 O ANISOU 1588 OG SER B 98 8038 9740 9802 2206 456 -727 O ATOM 1589 N ALA B 99 57.868 -21.692 16.819 1.00 50.08 N ANISOU 1589 N ALA B 99 5574 6278 7177 1792 535 -411 N ATOM 1590 CA ALA B 99 57.979 -20.820 17.980 1.00 58.47 C ANISOU 1590 CA ALA B 99 6699 7210 8305 1676 535 -435 C ATOM 1591 C ALA B 99 56.872 -21.109 18.987 1.00 62.45 C ANISOU 1591 C ALA B 99 7375 7529 8823 1766 483 -418 C ATOM 1592 O ALA B 99 57.102 -21.089 20.195 1.00 66.58 O ANISOU 1592 O ALA B 99 7938 8024 9334 1762 421 -499 O ATOM 1593 CB ALA B 99 57.939 -19.361 17.554 1.00 58.36 C ANISOU 1593 CB ALA B 99 6733 7087 8354 1484 675 -334 C ATOM 1594 N ALA B 100 55.673 -21.380 18.479 1.00 65.39 N ANISOU 1594 N ALA B 100 7830 7814 9202 1841 513 -329 N ATOM 1595 CA ALA B 100 54.529 -21.685 19.329 1.00 59.46 C ANISOU 1595 CA ALA B 100 7205 6922 8466 1896 503 -321 C ATOM 1596 C ALA B 100 54.756 -22.961 20.134 1.00 66.60 C ANISOU 1596 C ALA B 100 8152 7840 9314 1983 416 -380 C ATOM 1597 O ALA B 100 54.379 -23.043 21.303 1.00 63.06 O ANISOU 1597 O ALA B 100 7815 7310 8834 1983 411 -387 O ATOM 1598 CB ALA B 100 53.265 -21.808 18.490 1.00 40.24 C ANISOU 1598 CB ALA B 100 4781 4456 6051 1952 544 -253 C ATOM 1599 N VAL B 101 55.370 -23.956 19.500 1.00 64.01 N ANISOU 1599 N VAL B 101 7753 7608 8961 2071 353 -418 N ATOM 1600 CA VAL B 101 55.660 -25.221 20.165 1.00 60.78 C ANISOU 1600 CA VAL B 101 7423 7161 8509 2196 259 -451 C ATOM 1601 C VAL B 101 56.717 -25.042 21.250 1.00 66.38 C ANISOU 1601 C VAL B 101 8126 7950 9146 2234 163 -500 C ATOM 1602 O VAL B 101 56.611 -25.624 22.331 1.00 70.03 O ANISOU 1602 O VAL B 101 8739 8337 9532 2312 104 -469 O ATOM 1603 CB VAL B 101 56.129 -26.290 19.158 1.00 59.06 C ANISOU 1603 CB VAL B 101 7128 7011 8301 2318 208 -518 C ATOM 1604 CG1 VAL B 101 56.468 -27.591 19.872 1.00 61.96 C ANISOU 1604 CG1 VAL B 101 7625 7273 8646 2484 103 -536 C ATOM 1605 CG2 VAL B 101 55.061 -26.520 18.103 1.00 47.59 C ANISOU 1605 CG2 VAL B 101 5669 5521 6894 2280 278 -511 C ATOM 1606 N LEU B 102 57.726 -24.225 20.963 1.00 59.18 N ANISOU 1606 N LEU B 102 7037 7208 8241 2167 153 -578 N ATOM 1607 CA LEU B 102 58.791 -23.955 21.924 1.00 58.44 C ANISOU 1607 CA LEU B 102 6870 7253 8080 2182 45 -682 C ATOM 1608 C LEU B 102 58.241 -23.334 23.204 1.00 66.44 C ANISOU 1608 C LEU B 102 8035 8169 9039 2110 53 -670 C ATOM 1609 O LEU B 102 58.566 -23.775 24.307 1.00 66.25 O ANISOU 1609 O LEU B 102 8087 8198 8888 2220 -66 -697 O ATOM 1610 CB LEU B 102 59.851 -23.035 21.316 1.00 53.49 C ANISOU 1610 CB LEU B 102 5997 6823 7503 2036 81 -791 C ATOM 1611 CG LEU B 102 60.995 -22.662 22.262 1.00 63.03 C ANISOU 1611 CG LEU B 102 7062 8229 8659 2013 -38 -960 C ATOM 1612 CD1 LEU B 102 61.768 -23.902 22.683 1.00 59.77 C ANISOU 1612 CD1 LEU B 102 6588 7978 8142 2297 -235 -1030 C ATOM 1613 CD2 LEU B 102 61.920 -21.637 21.623 1.00 67.62 C ANISOU 1613 CD2 LEU B 102 7393 8977 9323 1777 53 -1075 C ATOM 1614 N ILE B 103 57.408 -22.310 23.047 1.00 56.10 N ANISOU 1614 N ILE B 103 6777 6730 7810 1951 189 -632 N ATOM 1615 CA ILE B 103 56.805 -21.627 24.186 1.00 56.23 C ANISOU 1615 CA ILE B 103 6924 6657 7784 1887 223 -660 C ATOM 1616 C ILE B 103 55.947 -22.590 25.003 1.00 58.11 C ANISOU 1616 C ILE B 103 7353 6819 7907 2000 218 -572 C ATOM 1617 O ILE B 103 55.918 -22.519 26.232 1.00 71.32 O ANISOU 1617 O ILE B 103 9132 8527 9441 2018 183 -610 O ATOM 1618 CB ILE B 103 55.951 -20.426 23.730 1.00 54.69 C ANISOU 1618 CB ILE B 103 6759 6300 7721 1755 373 -633 C ATOM 1619 CG1 ILE B 103 56.804 -19.456 22.912 1.00 57.81 C ANISOU 1619 CG1 ILE B 103 7020 6721 8226 1607 412 -675 C ATOM 1620 CG2 ILE B 103 55.339 -19.710 24.924 1.00 48.81 C ANISOU 1620 CG2 ILE B 103 6136 5471 6939 1714 415 -712 C ATOM 1621 CD1 ILE B 103 58.018 -18.940 23.654 1.00 46.90 C ANISOU 1621 CD1 ILE B 103 5529 5470 6819 1495 337 -862 C ATOM 1622 N ALA B 104 55.259 -23.496 24.316 1.00 44.30 N ANISOU 1622 N ALA B 104 5651 4976 6204 2057 263 -463 N ATOM 1623 CA ALA B 104 54.454 -24.510 24.986 1.00 58.63 C ANISOU 1623 CA ALA B 104 7653 6687 7935 2114 293 -366 C ATOM 1624 C ALA B 104 55.325 -25.470 25.793 1.00 65.01 C ANISOU 1624 C ALA B 104 8570 7546 8585 2272 146 -334 C ATOM 1625 O ALA B 104 54.972 -25.854 26.909 1.00 73.37 O ANISOU 1625 O ALA B 104 9823 8568 9486 2302 157 -258 O ATOM 1626 CB ALA B 104 53.620 -25.277 23.973 1.00 36.25 C ANISOU 1626 CB ALA B 104 4817 3741 5216 2106 366 -303 C ATOM 1627 N ILE B 105 56.464 -25.851 25.223 1.00 57.48 N ANISOU 1627 N ILE B 105 7489 6695 7656 2393 10 -390 N ATOM 1628 CA ILE B 105 57.396 -26.751 25.894 1.00 57.54 C ANISOU 1628 CA ILE B 105 7572 6771 7521 2614 -169 -373 C ATOM 1629 C ILE B 105 58.050 -26.072 27.095 1.00 62.96 C ANISOU 1629 C ILE B 105 8241 7656 8026 2635 -281 -455 C ATOM 1630 O ILE B 105 58.152 -26.665 28.170 1.00 70.47 O ANISOU 1630 O ILE B 105 9386 8620 8769 2783 -376 -370 O ATOM 1631 CB ILE B 105 58.486 -27.251 24.925 1.00 50.94 C ANISOU 1631 CB ILE B 105 6541 6045 6768 2765 -286 -466 C ATOM 1632 CG1 ILE B 105 57.866 -28.163 23.864 1.00 50.28 C ANISOU 1632 CG1 ILE B 105 6516 5766 6821 2787 -205 -411 C ATOM 1633 CG2 ILE B 105 59.583 -27.988 25.680 1.00 44.47 C ANISOU 1633 CG2 ILE B 105 5748 5349 5798 3048 -510 -485 C ATOM 1634 CD1 ILE B 105 58.844 -28.640 22.817 1.00 48.57 C ANISOU 1634 CD1 ILE B 105 6100 5674 6681 2937 -290 -537 C ATOM 1635 N ILE B 106 58.485 -24.829 26.907 1.00 56.07 N ANISOU 1635 N ILE B 106 7152 6930 7221 2479 -266 -622 N ATOM 1636 CA ILE B 106 59.054 -24.035 27.994 1.00 63.79 C ANISOU 1636 CA ILE B 106 8083 8102 8053 2444 -362 -769 C ATOM 1637 C ILE B 106 58.053 -23.895 29.138 1.00 64.90 C ANISOU 1637 C ILE B 106 8474 8159 8027 2407 -280 -696 C ATOM 1638 O ILE B 106 58.412 -24.010 30.310 1.00 60.39 O ANISOU 1638 O ILE B 106 7995 7744 7207 2512 -405 -728 O ATOM 1639 CB ILE B 106 59.489 -22.633 27.510 1.00 57.68 C ANISOU 1639 CB ILE B 106 7071 7407 7438 2206 -301 -964 C ATOM 1640 CG1 ILE B 106 60.633 -22.751 26.501 1.00 59.07 C ANISOU 1640 CG1 ILE B 106 6968 7746 7729 2220 -367 -1055 C ATOM 1641 CG2 ILE B 106 59.919 -21.764 28.685 1.00 61.47 C ANISOU 1641 CG2 ILE B 106 7519 8052 7786 2129 -384 -1165 C ATOM 1642 CD1 ILE B 106 61.079 -21.428 25.918 1.00 68.55 C ANISOU 1642 CD1 ILE B 106 7960 8990 9096 1940 -263 -1206 C ATOM 1643 N ASP B 107 56.796 -23.653 28.785 1.00 55.93 N ANISOU 1643 N ASP B 107 7430 6814 7007 2271 -70 -611 N ATOM 1644 CA ASP B 107 55.724 -23.544 29.766 1.00 51.77 C ANISOU 1644 CA ASP B 107 7105 6226 6338 2221 57 -556 C ATOM 1645 C ASP B 107 55.571 -24.835 30.565 1.00 60.79 C ANISOU 1645 C ASP B 107 8502 7349 7246 2375 17 -359 C ATOM 1646 O ASP B 107 55.368 -24.807 31.780 1.00 61.04 O ANISOU 1646 O ASP B 107 8698 7478 7016 2400 24 -341 O ATOM 1647 CB ASP B 107 54.406 -23.196 29.075 1.00 62.13 C ANISOU 1647 CB ASP B 107 8413 7349 7844 2081 277 -510 C ATOM 1648 CG ASP B 107 53.220 -23.283 30.009 1.00 89.31 C ANISOU 1648 CG ASP B 107 12029 10757 11148 2033 440 -456 C ATOM 1649 OD1 ASP B 107 53.104 -22.423 30.907 1.00100.17 O ANISOU 1649 OD1 ASP B 107 13424 12231 12405 1992 472 -594 O ATOM 1650 OD2 ASP B 107 52.405 -24.215 29.847 1.00112.48 O ANISOU 1650 OD2 ASP B 107 15070 13574 14093 2019 550 -298 O ATOM 1651 N ALA B 108 55.673 -25.965 29.874 1.00 51.75 N ANISOU 1651 N ALA B 108 7410 6066 6187 2479 -15 -213 N ATOM 1652 CA ALA B 108 55.546 -27.270 30.511 1.00 60.21 C ANISOU 1652 CA ALA B 108 8772 7027 7077 2626 -42 9 C ATOM 1653 C ALA B 108 56.713 -27.538 31.458 1.00 67.66 C ANISOU 1653 C ALA B 108 9785 8178 7744 2875 -293 11 C ATOM 1654 O ALA B 108 56.540 -28.150 32.512 1.00 71.67 O ANISOU 1654 O ALA B 108 10582 8678 7973 2981 -307 189 O ATOM 1655 CB ALA B 108 55.453 -28.364 29.460 1.00 60.65 C ANISOU 1655 CB ALA B 108 8862 6848 7333 2683 -29 113 C ATOM 1656 N VAL B 109 57.901 -27.076 31.077 1.00 55.87 N ANISOU 1656 N VAL B 109 8019 6896 6312 2966 -488 -185 N ATOM 1657 CA VAL B 109 59.086 -27.234 31.912 1.00 61.62 C ANISOU 1657 CA VAL B 109 8726 7900 6789 3218 -765 -247 C ATOM 1658 C VAL B 109 58.956 -26.396 33.181 1.00 67.72 C ANISOU 1658 C VAL B 109 9552 8895 7283 3143 -777 -347 C ATOM 1659 O VAL B 109 59.243 -26.870 34.281 1.00 73.46 O ANISOU 1659 O VAL B 109 10480 9767 7665 3349 -922 -249 O ATOM 1660 CB VAL B 109 60.371 -26.832 31.157 1.00 67.47 C ANISOU 1660 CB VAL B 109 9080 8869 7687 3278 -942 -495 C ATOM 1661 CG1 VAL B 109 61.564 -26.806 32.102 1.00 63.96 C ANISOU 1661 CG1 VAL B 109 8536 8792 6975 3515 -1242 -630 C ATOM 1662 CG2 VAL B 109 60.628 -27.785 29.999 1.00 63.08 C ANISOU 1662 CG2 VAL B 109 8477 8148 7342 3418 -956 -420 C ATOM 1663 N ILE B 110 58.514 -25.152 33.017 1.00 69.95 N ANISOU 1663 N ILE B 110 9675 9199 7705 2867 -627 -545 N ATOM 1664 CA ILE B 110 58.297 -24.250 34.144 1.00 64.19 C ANISOU 1664 CA ILE B 110 8983 8656 6749 2771 -608 -703 C ATOM 1665 C ILE B 110 57.248 -24.793 35.109 1.00 66.43 C ANISOU 1665 C ILE B 110 9620 8867 6752 2792 -458 -478 C ATOM 1666 O ILE B 110 57.456 -24.801 36.323 1.00 74.63 O ANISOU 1666 O ILE B 110 10802 10141 7414 2901 -557 -491 O ATOM 1667 CB ILE B 110 57.865 -22.848 33.664 1.00 69.05 C ANISOU 1667 CB ILE B 110 9407 9202 7628 2480 -439 -940 C ATOM 1668 CG1 ILE B 110 59.024 -22.148 32.955 1.00 70.70 C ANISOU 1668 CG1 ILE B 110 9283 9531 8049 2408 -573 -1183 C ATOM 1669 CG2 ILE B 110 57.396 -21.995 34.830 1.00 70.47 C ANISOU 1669 CG2 ILE B 110 9675 9511 7591 2389 -373 -1111 C ATOM 1670 CD1 ILE B 110 58.673 -20.772 32.440 1.00 77.85 C ANISOU 1670 CD1 ILE B 110 10053 10300 9225 2127 -405 -1377 C ATOM 1671 N THR B 111 56.128 -25.254 34.560 1.00 69.71 N ANISOU 1671 N THR B 111 10162 8989 7336 2676 -212 -282 N ATOM 1672 CA THR B 111 55.046 -25.817 35.360 1.00 62.10 C ANISOU 1672 CA THR B 111 9508 7942 6145 2632 -8 -61 C ATOM 1673 C THR B 111 55.536 -26.978 36.220 1.00 69.94 C ANISOU 1673 C THR B 111 10812 8985 6778 2884 -156 203 C ATOM 1674 O THR B 111 55.288 -27.017 37.425 1.00 80.67 O ANISOU 1674 O THR B 111 12394 10508 7747 2918 -120 282 O ATOM 1675 CB THR B 111 53.883 -26.298 34.471 1.00 62.02 C ANISOU 1675 CB THR B 111 9530 7614 6418 2461 253 89 C ATOM 1676 OG1 THR B 111 53.239 -25.166 33.871 1.00 70.73 O ANISOU 1676 OG1 THR B 111 10393 8699 7782 2266 401 -127 O ATOM 1677 CG2 THR B 111 52.865 -27.074 35.292 1.00 58.52 C ANISOU 1677 CG2 THR B 111 9405 7086 5743 2389 478 338 C ATOM 1678 N TRP B 112 56.240 -27.917 35.597 1.00 69.44 N ANISOU 1678 N TRP B 112 10775 8782 6828 3082 -324 340 N ATOM 1679 CA TRP B 112 56.760 -29.081 36.306 1.00 62.75 C ANISOU 1679 CA TRP B 112 10252 7918 5672 3384 -492 618 C ATOM 1680 C TRP B 112 57.839 -28.711 37.314 1.00 80.32 C ANISOU 1680 C TRP B 112 12436 10561 7521 3634 -799 491 C ATOM 1681 O TRP B 112 57.907 -29.293 38.396 1.00 78.44 O ANISOU 1681 O TRP B 112 12525 10417 6861 3830 -875 716 O ATOM 1682 CB TRP B 112 57.301 -30.111 35.314 1.00 62.31 C ANISOU 1682 CB TRP B 112 10202 7600 5872 3573 -613 733 C ATOM 1683 CG TRP B 112 56.231 -31.013 34.810 1.00 64.47 C ANISOU 1683 CG TRP B 112 10719 7442 6336 3412 -345 975 C ATOM 1684 CD1 TRP B 112 55.191 -30.673 33.999 1.00 58.44 C ANISOU 1684 CD1 TRP B 112 9814 6511 5881 3083 -75 892 C ATOM 1685 CD2 TRP B 112 56.077 -32.408 35.099 1.00 65.00 C ANISOU 1685 CD2 TRP B 112 11216 7180 6299 3562 -323 1329 C ATOM 1686 NE1 TRP B 112 54.400 -31.768 33.763 1.00 59.46 N ANISOU 1686 NE1 TRP B 112 10216 6264 6110 2989 114 1133 N ATOM 1687 CE2 TRP B 112 54.923 -32.848 34.423 1.00 63.48 C ANISOU 1687 CE2 TRP B 112 11100 6633 6387 3260 -18 1410 C ATOM 1688 CE3 TRP B 112 56.804 -33.328 35.861 1.00 69.54 C ANISOU 1688 CE3 TRP B 112 12130 7717 6574 3934 -539 1585 C ATOM 1689 CZ2 TRP B 112 54.478 -34.166 34.484 1.00 66.37 C ANISOU 1689 CZ2 TRP B 112 11873 6575 6770 3264 104 1722 C ATOM 1690 CZ3 TRP B 112 56.360 -34.638 35.921 1.00 72.43 C ANISOU 1690 CZ3 TRP B 112 12945 7629 6948 3978 -421 1938 C ATOM 1691 CH2 TRP B 112 55.208 -35.044 35.236 1.00 70.84 C ANISOU 1691 CH2 TRP B 112 12814 7046 7057 3617 -89 1996 C ATOM 1692 N CYS B 113 58.677 -27.743 36.963 1.00 70.59 N ANISOU 1692 N CYS B 113 10803 9589 6428 3616 -972 131 N ATOM 1693 CA CYS B 113 59.730 -27.298 37.866 1.00 68.22 C ANISOU 1693 CA CYS B 113 10384 9735 5802 3814 -1279 -74 C ATOM 1694 C CYS B 113 59.133 -26.659 39.115 1.00 87.30 C ANISOU 1694 C CYS B 113 12959 12371 7839 3699 -1178 -134 C ATOM 1695 O CYS B 113 59.472 -27.040 40.234 1.00 88.18 O ANISOU 1695 O CYS B 113 13290 12737 7477 3940 -1351 -26 O ATOM 1696 CB CYS B 113 60.671 -26.319 37.162 1.00 74.81 C ANISOU 1696 CB CYS B 113 10727 10779 6919 3721 -1426 -483 C ATOM 1697 SG CYS B 113 61.917 -27.117 36.121 1.00 94.40 S ANISOU 1697 SG CYS B 113 12965 13263 9638 4006 -1682 -491 S ATOM 1698 N ILE B 114 58.247 -25.688 38.914 1.00 87.31 N ANISOU 1698 N ILE B 114 12853 12288 8034 3358 -903 -314 N ATOM 1699 CA ILE B 114 57.618 -24.969 40.019 1.00 84.87 C ANISOU 1699 CA ILE B 114 12652 12188 7406 3233 -772 -442 C ATOM 1700 C ILE B 114 56.832 -25.894 40.950 1.00 87.04 C ANISOU 1700 C ILE B 114 13377 12430 7266 3315 -615 -60 C ATOM 1701 O ILE B 114 56.962 -25.813 42.173 1.00 80.29 O ANISOU 1701 O ILE B 114 12691 11904 5912 3431 -697 -74 O ATOM 1702 CB ILE B 114 56.677 -23.859 39.499 1.00 77.98 C ANISOU 1702 CB ILE B 114 11602 11150 6877 2892 -477 -675 C ATOM 1703 CG1 ILE B 114 57.486 -22.737 38.847 1.00 73.99 C ANISOU 1703 CG1 ILE B 114 10706 10711 6694 2781 -617 -1070 C ATOM 1704 CG2 ILE B 114 55.830 -23.295 40.628 1.00 68.04 C ANISOU 1704 CG2 ILE B 114 10493 10069 5291 2788 -285 -780 C ATOM 1705 CD1 ILE B 114 56.641 -21.586 38.346 1.00 65.22 C ANISOU 1705 CD1 ILE B 114 9458 9405 5917 2496 -359 -1286 C ATOM 1706 N LEU B 115 56.031 -26.780 40.370 1.00 86.47 N ANISOU 1706 N LEU B 115 13499 11969 7385 3237 -383 274 N ATOM 1707 CA LEU B 115 55.192 -27.682 41.156 1.00 80.53 C ANISOU 1707 CA LEU B 115 13184 11122 6293 3233 -164 660 C ATOM 1708 C LEU B 115 55.994 -28.717 41.939 1.00 93.10 C ANISOU 1708 C LEU B 115 15119 12813 7442 3602 -425 976 C ATOM 1709 O LEU B 115 55.691 -28.988 43.100 1.00101.88 O ANISOU 1709 O LEU B 115 16564 14103 8045 3662 -354 1177 O ATOM 1710 CB LEU B 115 54.177 -28.391 40.260 1.00 71.94 C ANISOU 1710 CB LEU B 115 12187 9576 5572 3018 143 898 C ATOM 1711 CG LEU B 115 53.070 -27.503 39.695 1.00 74.98 C ANISOU 1711 CG LEU B 115 12314 9884 6291 2674 453 663 C ATOM 1712 CD1 LEU B 115 52.164 -28.304 38.782 1.00 68.08 C ANISOU 1712 CD1 LEU B 115 11497 8607 5763 2487 702 874 C ATOM 1713 CD2 LEU B 115 52.272 -26.873 40.825 1.00 85.94 C ANISOU 1713 CD2 LEU B 115 13784 11543 7327 2537 681 568 C ATOM 1714 N LEU B 116 57.009 -29.299 41.310 1.00 86.46 N ANISOU 1714 N LEU B 116 14205 11871 6773 3873 -723 1027 N ATOM 1715 CA LEU B 116 57.774 -30.352 41.964 1.00 82.99 C ANISOU 1715 CA LEU B 116 14103 11480 5950 4293 -996 1348 C ATOM 1716 C LEU B 116 58.679 -29.780 43.050 1.00 89.28 C ANISOU 1716 C LEU B 116 14819 12850 6252 4548 -1330 1141 C ATOM 1717 O LEU B 116 58.938 -30.426 44.064 1.00 99.20 O ANISOU 1717 O LEU B 116 16445 14266 6980 4847 -1476 1428 O ATOM 1718 CB LEU B 116 58.619 -31.109 40.935 1.00 96.85 C ANISOU 1718 CB LEU B 116 15755 12983 8059 4548 -1228 1402 C ATOM 1719 CG LEU B 116 57.925 -32.119 40.017 1.00 96.79 C ANISOU 1719 CG LEU B 116 15960 12386 8428 4431 -985 1691 C ATOM 1720 CD1 LEU B 116 58.951 -32.878 39.186 1.00101.10 C ANISOU 1720 CD1 LEU B 116 16420 12766 9228 4781 -1275 1702 C ATOM 1721 CD2 LEU B 116 57.061 -33.082 40.812 1.00 96.20 C ANISOU 1721 CD2 LEU B 116 16470 12039 8043 4393 -741 2174 C ATOM 1722 N TRP B 117 59.154 -28.561 42.828 1.00 85.59 N ANISOU 1722 N TRP B 117 13880 12690 5952 4423 -1450 640 N ATOM 1723 CA TRP B 117 59.998 -27.864 43.794 1.00 98.63 C ANISOU 1723 CA TRP B 117 15374 14914 7186 4595 -1763 330 C ATOM 1724 C TRP B 117 59.269 -27.396 45.056 1.00101.06 C ANISOU 1724 C TRP B 117 15914 15502 6982 4475 -1592 311 C ATOM 1725 O TRP B 117 59.896 -27.194 46.094 1.00101.77 O ANISOU 1725 O TRP B 117 16034 16077 6558 4704 -1865 186 O ATOM 1726 CB TRP B 117 60.701 -26.696 43.102 1.00110.51 C ANISOU 1726 CB TRP B 117 16305 16599 9085 4427 -1900 -220 C ATOM 1727 CG TRP B 117 61.913 -26.221 43.827 1.00133.62 C ANISOU 1727 CG TRP B 117 18985 20098 11687 4657 -2320 -566 C ATOM 1728 CD1 TRP B 117 61.976 -25.238 44.768 1.00142.97 C ANISOU 1728 CD1 TRP B 117 20063 21709 12552 4552 -2383 -935 C ATOM 1729 CD2 TRP B 117 63.223 -26.796 43.761 1.00150.89 C ANISOU 1729 CD2 TRP B 117 21012 22531 13790 5067 -2753 -583 C ATOM 1730 NE1 TRP B 117 63.261 -25.113 45.237 1.00153.57 N ANISOU 1730 NE1 TRP B 117 21150 23558 13640 4830 -2834 -1212 N ATOM 1731 CE2 TRP B 117 64.044 -26.067 44.642 1.00161.82 C ANISOU 1731 CE2 TRP B 117 22147 24519 14818 5163 -3071 -994 C ATOM 1732 CE3 TRP B 117 63.785 -27.842 43.027 1.00156.93 C ANISOU 1732 CE3 TRP B 117 21792 23078 14756 5373 -2906 -331 C ATOM 1733 CZ2 TRP B 117 65.398 -26.349 44.804 1.00170.25 C ANISOU 1733 CZ2 TRP B 117 22907 25889 15892 5440 -3432 -1146 C ATOM 1734 CZ3 TRP B 117 65.127 -28.118 43.185 1.00164.59 C ANISOU 1734 CZ3 TRP B 117 22481 24368 15689 5690 -3279 -494 C ATOM 1735 CH2 TRP B 117 65.919 -27.375 44.066 1.00168.37 C ANISOU 1735 CH2 TRP B 117 22661 25394 15920 5699 -3515 -891 C ATOM 1736 N SER B 118 57.954 -27.213 44.974 1.00 96.81 N ANISOU 1736 N SER B 118 15513 14705 6567 4128 -1147 405 N ATOM 1737 CA SER B 118 57.205 -26.706 46.121 1.00108.03 C ANISOU 1737 CA SER B 118 17111 16415 7523 3995 -938 337 C ATOM 1738 C SER B 118 56.765 -27.790 47.104 1.00117.10 C ANISOU 1738 C SER B 118 18823 17582 8088 4157 -825 868 C ATOM 1739 O SER B 118 56.867 -27.611 48.317 1.00146.99 O ANISOU 1739 O SER B 118 22787 21812 11251 4287 -903 843 O ATOM 1740 CB SER B 118 55.972 -25.942 45.637 1.00103.16 C ANISOU 1740 CB SER B 118 16341 15570 7285 3567 -503 152 C ATOM 1741 OG SER B 118 55.114 -26.792 44.896 1.00106.76 O ANISOU 1741 OG SER B 118 16971 15542 8051 3419 -204 531 O ATOM 1742 N HIS B 119 56.283 -28.912 46.580 1.00105.71 N ANISOU 1742 N HIS B 119 17673 15654 6836 4137 -636 1343 N ATOM 1743 CA HIS B 119 55.816 -30.007 47.422 1.00142.34 C ANISOU 1743 CA HIS B 119 22899 20206 10977 4241 -476 1905 C ATOM 1744 C HIS B 119 57.013 -30.810 47.923 1.00158.52 C ANISOU 1744 C HIS B 119 25044 22327 12861 4636 -902 2097 C ATOM 1745 O HIS B 119 57.153 -31.065 49.120 1.00172.93 O ANISOU 1745 O HIS B 119 27064 24408 14232 4724 -962 2244 O ATOM 1746 CB HIS B 119 54.829 -30.911 46.677 1.00145.58 C ANISOU 1746 CB HIS B 119 23538 20002 11775 3978 -85 2289 C ATOM 1747 CG HIS B 119 54.185 -31.945 47.550 1.00170.60 C ANISOU 1747 CG HIS B 119 27221 23011 14590 3900 178 2809 C ATOM 1748 ND1 HIS B 119 53.437 -31.612 48.660 1.00176.43 N ANISOU 1748 ND1 HIS B 119 28081 24067 14888 3683 455 2821 N ATOM 1749 CD2 HIS B 119 54.172 -33.297 47.480 1.00178.63 C ANISOU 1749 CD2 HIS B 119 28578 23561 15733 3936 215 3277 C ATOM 1750 CE1 HIS B 119 52.992 -32.715 49.236 1.00182.24 C ANISOU 1750 CE1 HIS B 119 29218 24557 15467 3580 653 3306 C ATOM 1751 NE2 HIS B 119 53.424 -33.751 48.540 1.00184.81 N ANISOU 1751 NE2 HIS B 119 29694 24387 16139 3728 511 3588 N ATOM 1752 N PHE B 120 57.867 -31.206 46.984 1.00149.82 N ANISOU 1752 N PHE B 120 23772 21004 12151 4867 -1185 2074 N ATOM 1753 CA PHE B 120 59.019 -32.053 47.266 1.00138.56 C ANISOU 1753 CA PHE B 120 22379 19581 10685 5253 -1562 2222 C ATOM 1754 C PHE B 120 60.242 -31.253 47.713 1.00141.36 C ANISOU 1754 C PHE B 120 22321 20524 10867 5494 -2000 1771 C ATOM 1755 O PHE B 120 61.305 -31.822 47.958 1.00155.20 O ANISOU 1755 O PHE B 120 24020 22372 12578 5837 -2337 1811 O ATOM 1756 CB PHE B 120 59.372 -32.863 46.018 1.00130.38 C ANISOU 1756 CB PHE B 120 21300 18047 10190 5372 -1631 2344 C ATOM 1757 CG PHE B 120 58.273 -33.776 45.559 1.00127.80 C ANISOU 1757 CG PHE B 120 21363 17107 10090 5127 -1229 2762 C ATOM 1758 CD1 PHE B 120 57.222 -33.282 44.800 1.00118.35 C ANISOU 1758 CD1 PHE B 120 20123 15709 9136 4774 -878 2696 C ATOM 1759 CD2 PHE B 120 58.287 -35.122 45.876 1.00135.27 C ANISOU 1759 CD2 PHE B 120 22704 17675 11017 5235 -1197 3198 C ATOM 1760 CE1 PHE B 120 56.205 -34.109 44.373 1.00121.87 C ANISOU 1760 CE1 PHE B 120 20877 15609 9817 4505 -498 3034 C ATOM 1761 CE2 PHE B 120 57.272 -35.957 45.450 1.00135.46 C ANISOU 1761 CE2 PHE B 120 23055 17130 11285 4951 -819 3535 C ATOM 1762 CZ PHE B 120 56.230 -35.449 44.697 1.00134.43 C ANISOU 1762 CZ PHE B 120 22841 16824 11412 4572 -467 3439 C ATOM 1763 N GLY B 121 60.090 -29.938 47.823 1.00132.45 N ANISOU 1763 N GLY B 121 20888 19782 9654 5298 -1981 1312 N ATOM 1764 CA GLY B 121 61.181 -29.083 48.255 1.00130.14 C ANISOU 1764 CA GLY B 121 20169 20041 9236 5435 -2360 819 C ATOM 1765 C GLY B 121 61.043 -28.632 49.697 1.00141.65 C ANISOU 1765 C GLY B 121 21726 21953 10139 5396 -2362 722 C ATOM 1766 O GLY B 121 59.988 -28.784 50.312 1.00137.99 O ANISOU 1766 O GLY B 121 21622 21417 9390 5208 -2025 980 O ATOM 1767 OXT GLY B 121 61.985 -28.104 50.289 1.00151.93 O ANISOU 1767 OXT GLY B 121 22736 23723 11269 5533 -2690 367 O TER 1768 GLY B 121 ATOM 1769 N TYR C 16 37.641 -8.619 13.159 1.00 89.03 N ANISOU 1769 N TYR C 16 15802 10273 7753 3024 1925 -2070 N ATOM 1770 CA TYR C 16 38.430 -9.712 13.724 1.00100.17 C ANISOU 1770 CA TYR C 16 16876 11615 9568 2667 1882 -2294 C ATOM 1771 C TYR C 16 37.737 -10.591 14.755 1.00112.02 C ANISOU 1771 C TYR C 16 17860 13342 11361 2792 1770 -2121 C ATOM 1772 O TYR C 16 36.796 -11.322 14.441 1.00118.96 O ANISOU 1772 O TYR C 16 18325 14537 12337 2856 1605 -1990 O ATOM 1773 CB TYR C 16 39.715 -9.167 14.353 1.00108.58 C ANISOU 1773 CB TYR C 16 18302 12321 10633 2465 2037 -2443 C ATOM 1774 CG TYR C 16 40.841 -8.946 13.375 1.00 99.46 C ANISOU 1774 CG TYR C 16 17262 10976 9552 2066 2062 -2625 C ATOM 1775 CD1 TYR C 16 40.911 -9.682 12.201 1.00 90.21 C ANISOU 1775 CD1 TYR C 16 15966 9835 8474 1862 2074 -2837 C ATOM 1776 CD2 TYR C 16 41.858 -8.041 13.644 1.00102.24 C ANISOU 1776 CD2 TYR C 16 17841 11123 9883 1847 2087 -2568 C ATOM 1777 CE1 TYR C 16 41.947 -9.506 11.307 1.00106.65 C ANISOU 1777 CE1 TYR C 16 18102 11745 10677 1501 2133 -2969 C ATOM 1778 CE2 TYR C 16 42.901 -7.856 12.754 1.00120.32 C ANISOU 1778 CE2 TYR C 16 20168 13269 12280 1530 2110 -2683 C ATOM 1779 CZ TYR C 16 42.940 -8.592 11.586 1.00114.41 C ANISOU 1779 CZ TYR C 16 19247 12550 11674 1384 2142 -2875 C ATOM 1780 OH TYR C 16 43.973 -8.415 10.694 1.00105.25 O ANISOU 1780 OH TYR C 16 18127 11228 10634 1093 2210 -2968 O ATOM 1781 N SER C 17 38.236 -10.515 15.985 1.00110.70 N ANISOU 1781 N SER C 17 17736 13025 11300 2759 1842 -2103 N ATOM 1782 CA SER C 17 37.803 -11.388 17.068 1.00109.52 C ANISOU 1782 CA SER C 17 17107 13056 11451 2795 1741 -1962 C ATOM 1783 C SER C 17 36.299 -11.471 17.290 1.00104.90 C ANISOU 1783 C SER C 17 16280 12772 10805 3237 1682 -1671 C ATOM 1784 O SER C 17 35.740 -12.566 17.301 1.00 98.07 O ANISOU 1784 O SER C 17 14854 12178 10231 3203 1503 -1608 O ATOM 1785 CB SER C 17 38.473 -10.945 18.369 1.00120.44 C ANISOU 1785 CB SER C 17 18751 14241 12770 2662 1831 -1920 C ATOM 1786 OG SER C 17 39.870 -10.785 18.197 1.00127.21 O ANISOU 1786 OG SER C 17 19798 14852 13684 2234 1857 -2075 O ATOM 1787 N TRP C 18 35.638 -10.329 17.452 1.00119.23 N ANISOU 1787 N TRP C 18 18503 14520 12278 3653 1871 -1455 N ATOM 1788 CA TRP C 18 34.193 -10.345 17.637 1.00131.37 C ANISOU 1788 CA TRP C 18 19762 16327 13825 4122 1872 -1063 C ATOM 1789 C TRP C 18 33.522 -10.808 16.345 1.00120.10 C ANISOU 1789 C TRP C 18 17965 15247 12422 4098 1611 -925 C ATOM 1790 O TRP C 18 32.530 -11.536 16.366 1.00123.79 O ANISOU 1790 O TRP C 18 17909 16073 13055 4212 1418 -657 O ATOM 1791 CB TRP C 18 33.666 -8.976 18.065 1.00147.33 C ANISOU 1791 CB TRP C 18 22317 18115 15548 4605 2265 -800 C ATOM 1792 CG TRP C 18 32.181 -8.976 18.206 1.00166.98 C ANISOU 1792 CG TRP C 18 24449 20858 18139 5134 2328 -287 C ATOM 1793 CD1 TRP C 18 31.275 -8.328 17.421 1.00176.32 C ANISOU 1793 CD1 TRP C 18 25585 22166 19243 5535 2405 161 C ATOM 1794 CD2 TRP C 18 31.425 -9.689 19.191 1.00169.78 C ANISOU 1794 CD2 TRP C 18 24371 21398 18739 5310 2309 -86 C ATOM 1795 NE1 TRP C 18 29.999 -8.583 17.865 1.00181.51 N ANISOU 1795 NE1 TRP C 18 25780 23074 20112 5965 2449 674 N ATOM 1796 CE2 TRP C 18 30.065 -9.418 18.950 1.00177.06 C ANISOU 1796 CE2 TRP C 18 24998 22541 19737 5842 2400 496 C ATOM 1797 CE3 TRP C 18 31.767 -10.527 20.257 1.00163.17 C ANISOU 1797 CE3 TRP C 18 23337 20576 18085 5060 2220 -286 C ATOM 1798 CZ2 TRP C 18 29.047 -9.956 19.734 1.00176.23 C ANISOU 1798 CZ2 TRP C 18 24430 22649 19882 6148 2425 848 C ATOM 1799 CZ3 TRP C 18 30.757 -11.058 21.035 1.00163.05 C ANISOU 1799 CZ3 TRP C 18 22896 20774 18282 5349 2233 19 C ATOM 1800 CH2 TRP C 18 29.413 -10.770 20.770 1.00171.19 C ANISOU 1800 CH2 TRP C 18 23662 22001 19381 5898 2347 563 C ATOM 1801 N LYS C 19 34.083 -10.375 15.221 1.00 81.90 N ANISOU 1801 N LYS C 19 13431 10309 7377 3885 1594 -1096 N ATOM 1802 CA LYS C 19 33.602 -10.765 13.902 1.00 92.75 C ANISOU 1802 CA LYS C 19 14583 11997 8661 3686 1339 -1006 C ATOM 1803 C LYS C 19 33.804 -12.260 13.645 1.00109.33 C ANISOU 1803 C LYS C 19 16248 14262 11031 3199 1123 -1271 C ATOM 1804 O LYS C 19 32.947 -12.915 13.053 1.00 83.90 O ANISOU 1804 O LYS C 19 12676 11417 7786 3058 875 -1077 O ATOM 1805 CB LYS C 19 34.319 -9.954 12.823 1.00 92.23 C ANISOU 1805 CB LYS C 19 15024 11730 8291 3500 1415 -1191 C ATOM 1806 CG LYS C 19 33.726 -10.076 11.431 1.00 87.41 C ANISOU 1806 CG LYS C 19 14308 11455 7448 3271 1162 -1009 C ATOM 1807 CD LYS C 19 34.471 -9.183 10.448 1.00101.64 C ANISOU 1807 CD LYS C 19 16653 13032 8934 3107 1266 -1190 C ATOM 1808 CE LYS C 19 34.068 -9.480 9.012 1.00113.82 C ANISOU 1808 CE LYS C 19 18141 14909 10198 2671 989 -1093 C ATOM 1809 NZ LYS C 19 35.189 -9.257 8.054 1.00104.89 N ANISOU 1809 NZ LYS C 19 17499 13493 8863 2233 1104 -1551 N ATOM 1810 N GLY C 20 34.943 -12.785 14.086 1.00108.01 N ANISOU 1810 N GLY C 20 16109 13803 11127 2911 1244 -1664 N ATOM 1811 CA GLY C 20 35.246 -14.197 13.954 1.00 77.86 C ANISOU 1811 CA GLY C 20 11896 10024 7665 2492 1179 -1904 C ATOM 1812 C GLY C 20 34.351 -15.079 14.813 1.00 88.11 C ANISOU 1812 C GLY C 20 12634 11614 9230 2644 1022 -1678 C ATOM 1813 O GLY C 20 33.948 -16.161 14.405 1.00 78.54 O ANISOU 1813 O GLY C 20 11075 10602 8164 2364 894 -1722 O ATOM 1814 N LEU C 21 34.062 -14.586 16.021 1.00 76.75 N ANISOU 1814 N LEU C 21 11170 10166 7824 3052 1071 -1450 N ATOM 1815 CA LEU C 21 33.199 -15.294 16.966 1.00 79.78 C ANISOU 1815 CA LEU C 21 11054 10810 8448 3254 952 -1206 C ATOM 1816 C LEU C 21 31.796 -15.427 16.389 1.00 92.76 C ANISOU 1816 C LEU C 21 12414 12886 9945 3428 731 -830 C ATOM 1817 O LEU C 21 31.169 -16.491 16.485 1.00 96.16 O ANISOU 1817 O LEU C 21 12350 13603 10585 3308 537 -737 O ATOM 1818 CB LEU C 21 33.181 -14.586 18.322 1.00 75.90 C ANISOU 1818 CB LEU C 21 10740 10173 7926 3611 1122 -1048 C ATOM 1819 CG LEU C 21 34.424 -14.743 19.202 1.00 76.03 C ANISOU 1819 CG LEU C 21 10859 9898 8132 3326 1223 -1283 C ATOM 1820 CD1 LEU C 21 34.312 -13.821 20.402 1.00 77.55 C ANISOU 1820 CD1 LEU C 21 11431 9942 8094 3581 1416 -1128 C ATOM 1821 CD2 LEU C 21 34.613 -16.196 19.637 1.00 71.77 C ANISOU 1821 CD2 LEU C 21 9697 9481 8091 3052 1079 -1338 C ATOM 1822 N ARG C 22 31.318 -14.338 15.798 1.00 86.27 N ANISOU 1822 N ARG C 22 11882 12119 8779 3690 760 -556 N ATOM 1823 CA ARG C 22 30.005 -14.308 15.162 1.00 90.66 C ANISOU 1823 CA ARG C 22 12136 13123 9186 3830 522 -40 C ATOM 1824 C ARG C 22 29.962 -15.311 14.020 1.00 91.67 C ANISOU 1824 C ARG C 22 12083 13510 9235 3196 226 -204 C ATOM 1825 O ARG C 22 29.006 -16.074 13.891 1.00 94.16 O ANISOU 1825 O ARG C 22 11941 14242 9592 3074 -53 91 O ATOM 1826 CB ARG C 22 29.703 -12.901 14.637 1.00101.24 C ANISOU 1826 CB ARG C 22 13835 14416 10214 4181 653 314 C ATOM 1827 CG ARG C 22 28.422 -12.778 13.845 1.00124.31 C ANISOU 1827 CG ARG C 22 16399 17837 12995 4269 375 985 C ATOM 1828 CD ARG C 22 28.307 -11.371 13.299 1.00140.24 C ANISOU 1828 CD ARG C 22 18774 19742 14768 4602 558 1338 C ATOM 1829 NE ARG C 22 27.128 -11.215 12.456 1.00143.77 N ANISOU 1829 NE ARG C 22 18818 20709 15097 4629 253 2108 N ATOM 1830 CZ ARG C 22 26.713 -10.055 11.960 1.00161.12 C ANISOU 1830 CZ ARG C 22 21127 22925 17168 4979 375 2671 C ATOM 1831 NH1 ARG C 22 27.395 -8.946 12.203 1.00165.04 N ANISOU 1831 NH1 ARG C 22 22200 22903 17605 5329 832 2463 N ATOM 1832 NH2 ARG C 22 25.620 -10.006 11.209 1.00168.18 N ANISOU 1832 NH2 ARG C 22 21539 24365 17995 4940 34 3494 N ATOM 1833 N ALA C 23 31.022 -15.333 13.217 1.00 85.81 N ANISOU 1833 N ALA C 23 11740 12492 8371 2750 326 -685 N ATOM 1834 CA ALA C 23 31.119 -16.263 12.106 1.00 88.97 C ANISOU 1834 CA ALA C 23 12139 13016 8651 2062 181 -937 C ATOM 1835 C ALA C 23 31.145 -17.694 12.610 1.00 96.59 C ANISOU 1835 C ALA C 23 12710 13991 9999 1793 179 -1162 C ATOM 1836 O ALA C 23 30.476 -18.558 12.058 1.00 96.61 O ANISOU 1836 O ALA C 23 12501 14304 9902 1374 -36 -1091 O ATOM 1837 CB ALA C 23 32.351 -15.967 11.260 1.00 86.75 C ANISOU 1837 CB ALA C 23 12407 12331 8224 1690 418 -1430 C ATOM 1838 N ALA C 24 31.924 -17.934 13.658 1.00 96.17 N ANISOU 1838 N ALA C 24 12567 13605 10368 1988 415 -1397 N ATOM 1839 CA ALA C 24 32.044 -19.272 14.230 1.00 96.57 C ANISOU 1839 CA ALA C 24 12205 13620 10869 1781 461 -1571 C ATOM 1840 C ALA C 24 30.729 -19.780 14.811 1.00102.44 C ANISOU 1840 C ALA C 24 12425 14824 11674 1990 168 -1156 C ATOM 1841 O ALA C 24 30.396 -20.956 14.665 1.00108.63 O ANISOU 1841 O ALA C 24 12912 15748 12615 1631 87 -1233 O ATOM 1842 CB ALA C 24 33.124 -19.291 15.297 1.00102.00 C ANISOU 1842 CB ALA C 24 12847 13919 11989 1951 717 -1754 C ATOM 1843 N TRP C 25 29.991 -18.895 15.471 1.00103.16 N ANISOU 1843 N TRP C 25 12427 15112 11658 2566 67 -708 N ATOM 1844 CA TRP C 25 28.730 -19.272 16.098 1.00106.35 C ANISOU 1844 CA TRP C 25 12312 15933 12163 2848 -163 -239 C ATOM 1845 C TRP C 25 27.667 -19.680 15.084 1.00109.98 C ANISOU 1845 C TRP C 25 12559 16884 12345 2511 -519 90 C ATOM 1846 O TRP C 25 27.056 -20.739 15.210 1.00116.01 O ANISOU 1846 O TRP C 25 12908 17924 13248 2278 -716 177 O ATOM 1847 CB TRP C 25 28.203 -18.117 16.956 1.00111.73 C ANISOU 1847 CB TRP C 25 13033 16623 12798 3556 -53 194 C ATOM 1848 CG TRP C 25 26.899 -18.416 17.630 1.00113.50 C ANISOU 1848 CG TRP C 25 12721 17234 13168 3916 -211 736 C ATOM 1849 CD1 TRP C 25 25.653 -18.082 17.185 1.00119.17 C ANISOU 1849 CD1 TRP C 25 13166 18380 13733 4127 -419 1388 C ATOM 1850 CD2 TRP C 25 26.709 -19.114 18.867 1.00109.20 C ANISOU 1850 CD2 TRP C 25 11807 16704 12980 4097 -175 742 C ATOM 1851 NE1 TRP C 25 24.699 -18.524 18.068 1.00124.78 N ANISOU 1851 NE1 TRP C 25 13360 19347 14703 4457 -485 1794 N ATOM 1852 CE2 TRP C 25 25.321 -19.162 19.109 1.00114.93 C ANISOU 1852 CE2 TRP C 25 12072 17847 13748 4442 -337 1370 C ATOM 1853 CE3 TRP C 25 27.576 -19.701 19.793 1.00107.75 C ANISOU 1853 CE3 TRP C 25 11599 16241 13101 3982 -33 343 C ATOM 1854 CZ2 TRP C 25 24.781 -19.773 20.239 1.00112.33 C ANISOU 1854 CZ2 TRP C 25 11315 17636 13728 4688 -335 1537 C ATOM 1855 CZ3 TRP C 25 27.038 -20.307 20.914 1.00109.78 C ANISOU 1855 CZ3 TRP C 25 11426 16641 13644 4194 -66 525 C ATOM 1856 CH2 TRP C 25 25.654 -20.339 21.127 1.00111.21 C ANISOU 1856 CH2 TRP C 25 11208 17213 13835 4550 -204 1080 C ATOM 1857 N ILE C 26 27.451 -18.840 14.078 1.00111.25 N ANISOU 1857 N ILE C 26 13005 17176 12090 2432 -624 309 N ATOM 1858 CA ILE C 26 26.427 -19.110 13.074 1.00120.28 C ANISOU 1858 CA ILE C 26 13954 18858 12891 2019 -1031 744 C ATOM 1859 C ILE C 26 26.815 -20.258 12.133 1.00127.72 C ANISOU 1859 C ILE C 26 15081 19785 13660 1102 -1099 253 C ATOM 1860 O ILE C 26 25.987 -21.118 11.825 1.00130.05 O ANISOU 1860 O ILE C 26 15082 20492 13838 657 -1410 474 O ATOM 1861 CB ILE C 26 26.098 -17.839 12.249 1.00130.02 C ANISOU 1861 CB ILE C 26 15415 20255 13730 2162 -1133 1207 C ATOM 1862 CG1 ILE C 26 25.163 -16.918 13.040 1.00141.23 C ANISOU 1862 CG1 ILE C 26 16491 21846 15324 3007 -1096 1964 C ATOM 1863 CG2 ILE C 26 25.398 -18.198 10.954 1.00132.50 C ANISOU 1863 CG2 ILE C 26 15670 21088 13586 1435 -1579 1535 C ATOM 1864 CD1 ILE C 26 25.861 -15.874 13.886 1.00145.30 C ANISOU 1864 CD1 ILE C 26 17373 21827 16008 3667 -613 1768 C ATOM 1865 N ASN C 27 28.074 -20.289 11.703 1.00121.46 N ANISOU 1865 N ASN C 27 14799 18486 12865 797 -758 -402 N ATOM 1866 CA ASN C 27 28.505 -21.242 10.678 1.00122.28 C ANISOU 1866 CA ASN C 27 15229 18461 12772 -90 -667 -890 C ATOM 1867 C ASN C 27 28.925 -22.621 11.211 1.00124.69 C ANISOU 1867 C ASN C 27 15351 18480 13545 -335 -396 -1333 C ATOM 1868 O ASN C 27 28.586 -23.639 10.611 1.00126.78 O ANISOU 1868 O ASN C 27 15662 18860 13650 -1028 -442 -1476 O ATOM 1869 CB ASN C 27 29.649 -20.636 9.865 1.00110.48 C ANISOU 1869 CB ASN C 27 14376 16519 11082 -314 -348 -1343 C ATOM 1870 CG ASN C 27 29.180 -19.524 8.947 1.00112.25 C ANISOU 1870 CG ASN C 27 14849 17067 10735 -365 -639 -938 C ATOM 1871 OD1 ASN C 27 29.896 -18.549 8.722 1.00114.82 O ANISOU 1871 OD1 ASN C 27 15545 17107 10976 -132 -449 -1068 O ATOM 1872 ND2 ASN C 27 27.963 -19.655 8.428 1.00115.15 N ANISOU 1872 ND2 ASN C 27 14975 18055 10722 -684 -1119 -377 N ATOM 1873 N GLU C 28 29.651 -22.655 12.328 1.00134.48 N ANISOU 1873 N GLU C 28 16398 19350 15346 179 -108 -1512 N ATOM 1874 CA GLU C 28 30.093 -23.920 12.931 1.00139.75 C ANISOU 1874 CA GLU C 28 16803 19735 16560 23 171 -1830 C ATOM 1875 C GLU C 28 29.170 -24.343 14.073 1.00143.77 C ANISOU 1875 C GLU C 28 16673 20608 17348 430 -104 -1433 C ATOM 1876 O GLU C 28 28.967 -23.598 15.032 1.00150.52 O ANISOU 1876 O GLU C 28 17303 21564 18325 1087 -209 -1117 O ATOM 1877 CB GLU C 28 31.538 -23.822 13.452 1.00144.42 C ANISOU 1877 CB GLU C 28 17504 19719 17651 232 643 -2189 C ATOM 1878 CG GLU C 28 32.690 -23.913 12.429 1.00167.77 C ANISOU 1878 CG GLU C 28 21003 22152 20590 -255 1110 -2685 C ATOM 1879 CD GLU C 28 32.764 -25.278 11.737 1.00189.21 C ANISOU 1879 CD GLU C 28 23835 24637 23419 -961 1448 -3046 C ATOM 1880 OE1 GLU C 28 32.494 -26.290 12.417 1.00198.25 O ANISOU 1880 OE1 GLU C 28 24540 25798 24989 -953 1497 -3006 O ATOM 1881 OE2 GLU C 28 33.171 -25.363 10.553 1.00195.04 O ANISOU 1881 OE2 GLU C 28 25143 25111 23853 -1538 1741 -3396 O ATOM 1882 N ALA C 29 28.610 -25.545 13.957 1.00131.08 N ANISOU 1882 N ALA C 29 16852 17409 15545 422 830 975 N ATOM 1883 CA ALA C 29 27.711 -26.088 14.973 1.00124.10 C ANISOU 1883 CA ALA C 29 15753 16702 14695 548 794 1289 C ATOM 1884 C ALA C 29 28.462 -26.605 16.199 1.00119.53 C ANISOU 1884 C ALA C 29 15220 16003 14194 721 847 1088 C ATOM 1885 O ALA C 29 27.971 -26.506 17.324 1.00117.90 O ANISOU 1885 O ALA C 29 14880 15941 13977 977 917 1287 O ATOM 1886 CB ALA C 29 26.855 -27.197 14.378 1.00123.31 C ANISOU 1886 CB ALA C 29 15539 16714 14600 205 573 1555 C ATOM 1887 N ALA C 30 29.646 -27.164 15.970 1.00120.84 N ANISOU 1887 N ALA C 30 15568 15920 14425 592 815 698 N ATOM 1888 CA ALA C 30 30.487 -27.676 17.047 1.00113.00 C ANISOU 1888 CA ALA C 30 14637 14777 13523 738 833 477 C ATOM 1889 C ALA C 30 30.862 -26.563 18.020 1.00104.55 C ANISOU 1889 C ALA C 30 13602 13691 12432 1107 1004 399 C ATOM 1890 O ALA C 30 30.975 -26.782 19.225 1.00 94.54 O ANISOU 1890 O ALA C 30 12318 12420 11182 1313 1026 410 O ATOM 1891 CB ALA C 30 31.741 -28.327 16.480 1.00105.72 C ANISOU 1891 CB ALA C 30 13888 13603 12679 565 778 52 C ATOM 1892 N PHE C 31 31.048 -25.367 17.475 1.00100.17 N ANISOU 1892 N PHE C 31 13124 13111 11825 1179 1100 325 N ATOM 1893 CA PHE C 31 31.412 -24.196 18.259 1.00 92.56 C ANISOU 1893 CA PHE C 31 12252 12082 10834 1512 1218 235 C ATOM 1894 C PHE C 31 30.302 -23.754 19.215 1.00103.95 C ANISOU 1894 C PHE C 31 13571 13742 12182 1842 1285 559 C ATOM 1895 O PHE C 31 30.578 -23.281 20.317 1.00112.32 O ANISOU 1895 O PHE C 31 14713 14754 13210 2159 1354 479 O ATOM 1896 CB PHE C 31 31.790 -23.049 17.316 1.00 93.24 C ANISOU 1896 CB PHE C 31 12462 12076 10889 1456 1259 124 C ATOM 1897 CG PHE C 31 32.220 -21.798 18.021 1.00 89.89 C ANISOU 1897 CG PHE C 31 12185 11523 10446 1763 1326 19 C ATOM 1898 CD1 PHE C 31 33.512 -21.668 18.500 1.00 87.43 C ANISOU 1898 CD1 PHE C 31 12019 10985 10216 1795 1328 -310 C ATOM 1899 CD2 PHE C 31 31.339 -20.742 18.181 1.00 89.09 C ANISOU 1899 CD2 PHE C 31 12088 11512 10252 2023 1360 246 C ATOM 1900 CE1 PHE C 31 33.910 -20.516 19.146 1.00 86.25 C ANISOU 1900 CE1 PHE C 31 12040 10683 10048 2051 1340 -403 C ATOM 1901 CE2 PHE C 31 31.733 -19.587 18.823 1.00 96.03 C ANISOU 1901 CE2 PHE C 31 13157 12225 11104 2318 1381 128 C ATOM 1902 CZ PHE C 31 33.022 -19.473 19.306 1.00 94.19 C ANISOU 1902 CZ PHE C 31 13094 11747 10947 2314 1359 -195 C ATOM 1903 N ARG C 32 29.051 -23.907 18.790 1.00113.63 N ANISOU 1903 N ARG C 32 14598 15224 13354 1776 1260 926 N ATOM 1904 CA ARG C 32 27.910 -23.522 19.619 1.00123.03 C ANISOU 1904 CA ARG C 32 15607 16693 14445 2100 1348 1269 C ATOM 1905 C ARG C 32 27.802 -24.431 20.832 1.00130.46 C ANISOU 1905 C ARG C 32 16451 17742 15374 2191 1361 1360 C ATOM 1906 O ARG C 32 27.452 -23.992 21.929 1.00134.71 O ANISOU 1906 O ARG C 32 16954 18424 15806 2564 1485 1461 O ATOM 1907 CB ARG C 32 26.606 -23.585 18.836 1.00125.15 C ANISOU 1907 CB ARG C 32 15629 17239 14682 1966 1297 1673 C ATOM 1908 CG ARG C 32 26.429 -22.506 17.800 1.00127.40 C ANISOU 1908 CG ARG C 32 15985 17480 14943 1961 1288 1682 C ATOM 1909 CD ARG C 32 25.001 -22.513 17.311 1.00133.78 C ANISOU 1909 CD ARG C 32 16504 18610 15716 1920 1238 2137 C ATOM 1910 NE ARG C 32 24.791 -23.590 16.354 1.00134.29 N ANISOU 1910 NE ARG C 32 16492 18701 15833 1436 1057 2241 N ATOM 1911 CZ ARG C 32 24.979 -23.489 15.046 1.00122.23 C ANISOU 1911 CZ ARG C 32 15082 17056 14304 1128 941 2164 C ATOM 1912 NH1 ARG C 32 25.413 -22.353 14.518 1.00120.28 N ANISOU 1912 NH1 ARG C 32 15021 16660 14021 1222 990 2001 N ATOM 1913 NH2 ARG C 32 24.751 -24.538 14.269 1.00118.68 N ANISOU 1913 NH2 ARG C 32 14592 16625 13876 714 758 2249 N ATOM 1914 N GLN C 33 28.093 -25.709 20.615 1.00127.98 N ANISOU 1914 N GLN C 33 16116 17356 15156 1852 1222 1326 N ATOM 1915 CA GLN C 33 28.021 -26.708 21.670 1.00129.28 C ANISOU 1915 CA GLN C 33 16205 17592 15324 1862 1183 1436 C ATOM 1916 C GLN C 33 29.097 -26.407 22.708 1.00126.29 C ANISOU 1916 C GLN C 33 16041 17005 14940 2126 1251 1107 C ATOM 1917 O GLN C 33 28.869 -26.541 23.911 1.00135.80 O ANISOU 1917 O GLN C 33 17206 18341 16053 2355 1313 1231 O ATOM 1918 CB GLN C 33 28.184 -28.115 21.088 1.00128.63 C ANISOU 1918 CB GLN C 33 16114 17396 15364 1429 964 1433 C ATOM 1919 CG GLN C 33 26.922 -28.632 20.402 1.00127.65 C ANISOU 1919 CG GLN C 33 15750 17521 15229 1159 847 1860 C ATOM 1920 CD GLN C 33 27.199 -29.725 19.387 1.00128.51 C ANISOU 1920 CD GLN C 33 15956 17428 15446 718 600 1755 C ATOM 1921 OE1 GLN C 33 28.256 -30.349 19.404 1.00126.29 O ANISOU 1921 OE1 GLN C 33 15879 16852 15254 632 515 1404 O ATOM 1922 NE2 GLN C 33 26.246 -29.957 18.491 1.00130.16 N ANISOU 1922 NE2 GLN C 33 16023 17789 15641 453 469 2053 N ATOM 1923 N GLU C 34 30.269 -26.000 22.233 1.00115.02 N ANISOU 1923 N GLU C 34 14834 15271 13599 2079 1233 705 N ATOM 1924 CA GLU C 34 31.357 -25.603 23.118 1.00111.31 C ANISOU 1924 CA GLU C 34 14570 14581 13141 2303 1264 386 C ATOM 1925 C GLU C 34 31.015 -24.323 23.878 1.00119.00 C ANISOU 1925 C GLU C 34 15616 15640 13959 2728 1405 437 C ATOM 1926 O GLU C 34 31.351 -24.182 25.054 1.00126.45 O ANISOU 1926 O GLU C 34 16674 16542 14830 2990 1433 351 O ATOM 1927 CB GLU C 34 32.642 -25.392 22.323 1.00112.44 C ANISOU 1927 CB GLU C 34 14880 14424 13420 2129 1214 -11 C ATOM 1928 CG GLU C 34 33.226 -26.646 21.714 1.00124.04 C ANISOU 1928 CG GLU C 34 16332 15764 15033 1796 1080 -164 C ATOM 1929 CD GLU C 34 34.199 -26.329 20.602 1.00129.13 C ANISOU 1929 CD GLU C 34 17070 16231 15762 1612 1085 -478 C ATOM 1930 OE1 GLU C 34 34.488 -25.131 20.404 1.00139.91 O ANISOU 1930 OE1 GLU C 34 18519 17552 17089 1718 1172 -563 O ATOM 1931 OE2 GLU C 34 34.674 -27.269 19.932 1.00116.30 O ANISOU 1931 OE2 GLU C 34 15444 14515 14231 1369 997 -636 O ATOM 1932 N GLY C 35 30.350 -23.393 23.195 1.00115.08 N ANISOU 1932 N GLY C 35 15078 15245 13401 2805 1474 569 N ATOM 1933 CA GLY C 35 29.918 -22.149 23.809 1.00118.08 C ANISOU 1933 CA GLY C 35 15543 15692 13630 3241 1588 620 C ATOM 1934 C GLY C 35 28.971 -22.394 24.966 1.00126.79 C ANISOU 1934 C GLY C 35 16493 17118 14563 3549 1701 906 C ATOM 1935 O GLY C 35 29.062 -21.750 26.011 1.00129.25 O ANISOU 1935 O GLY C 35 16960 17421 14729 3947 1781 821 O ATOM 1936 N VAL C 36 28.055 -23.336 24.767 1.00132.28 N ANISOU 1936 N VAL C 36 16888 18108 15263 3352 1698 1255 N ATOM 1937 CA VAL C 36 27.132 -23.755 25.811 1.00135.76 C ANISOU 1937 CA VAL C 36 17118 18920 15545 3563 1808 1590 C ATOM 1938 C VAL C 36 27.916 -24.439 26.926 1.00128.84 C ANISOU 1938 C VAL C 36 16389 17921 14642 3585 1769 1429 C ATOM 1939 O VAL C 36 27.677 -24.198 28.111 1.00134.31 O ANISOU 1939 O VAL C 36 17112 18782 15136 3943 1892 1496 O ATOM 1940 CB VAL C 36 26.046 -24.703 25.266 1.00134.50 C ANISOU 1940 CB VAL C 36 16591 19082 15430 3249 1760 2030 C ATOM 1941 CG1 VAL C 36 25.255 -25.323 26.407 1.00133.70 C ANISOU 1941 CG1 VAL C 36 16256 19366 15176 3384 1857 2392 C ATOM 1942 CG2 VAL C 36 25.120 -23.956 24.318 1.00135.66 C ANISOU 1942 CG2 VAL C 36 16562 19407 15574 3290 1801 2247 C ATOM 1943 N ALA C 37 28.861 -25.288 26.530 1.00118.55 N ANISOU 1943 N ALA C 37 15186 16329 13529 3218 1592 1209 N ATOM 1944 CA ALA C 37 29.700 -26.015 27.476 1.00111.15 C ANISOU 1944 CA ALA C 37 14393 15229 12611 3199 1505 1043 C ATOM 1945 C ALA C 37 30.508 -25.054 28.341 1.00101.42 C ANISOU 1945 C ALA C 37 13455 13800 11279 3566 1557 726 C ATOM 1946 O ALA C 37 30.723 -25.309 29.524 1.00101.13 O ANISOU 1946 O ALA C 37 13514 13789 11123 3743 1560 717 O ATOM 1947 CB ALA C 37 30.625 -26.973 26.739 1.00108.44 C ANISOU 1947 CB ALA C 37 14111 14579 12512 2784 1299 816 C ATOM 1948 N VAL C 38 30.957 -23.953 27.745 1.00105.64 N ANISOU 1948 N VAL C 38 14153 14129 11855 3658 1571 482 N ATOM 1949 CA VAL C 38 31.691 -22.929 28.482 1.00103.35 C ANISOU 1949 CA VAL C 38 14173 13618 11477 3986 1576 191 C ATOM 1950 C VAL C 38 30.755 -22.284 29.498 1.00109.08 C ANISOU 1950 C VAL C 38 14913 14624 11909 4468 1744 383 C ATOM 1951 O VAL C 38 31.119 -22.094 30.660 1.00103.57 O ANISOU 1951 O VAL C 38 14425 13874 11054 4744 1747 260 O ATOM 1952 CB VAL C 38 32.284 -21.858 27.546 1.00 96.13 C ANISOU 1952 CB VAL C 38 13422 12429 10674 3940 1530 -56 C ATOM 1953 CG1 VAL C 38 32.680 -20.616 28.329 1.00 94.37 C ANISOU 1953 CG1 VAL C 38 13522 12019 10315 4332 1524 -265 C ATOM 1954 CG2 VAL C 38 33.480 -22.422 26.801 1.00101.60 C ANISOU 1954 CG2 VAL C 38 14144 12842 11619 3536 1384 -319 C ATOM 1955 N LEU C 39 29.546 -21.960 29.050 1.00115.25 N ANISOU 1955 N LEU C 39 15467 15717 12605 4580 1883 687 N ATOM 1956 CA LEU C 39 28.534 -21.375 29.921 1.00107.90 C ANISOU 1956 CA LEU C 39 14486 15125 11386 5073 2080 899 C ATOM 1957 C LEU C 39 28.188 -22.320 31.064 1.00109.22 C ANISOU 1957 C LEU C 39 14524 15590 11384 5130 2156 1119 C ATOM 1958 O LEU C 39 28.053 -21.900 32.212 1.00111.54 O ANISOU 1958 O LEU C 39 14965 16006 11409 5555 2270 1094 O ATOM 1959 CB LEU C 39 27.267 -21.048 29.125 1.00113.67 C ANISOU 1959 CB LEU C 39 14908 16178 12104 5125 2198 1235 C ATOM 1960 CG LEU C 39 26.069 -20.527 29.923 1.00135.80 C ANISOU 1960 CG LEU C 39 17557 19422 14617 5652 2435 1510 C ATOM 1961 CD1 LEU C 39 26.371 -19.180 30.560 1.00143.64 C ANISOU 1961 CD1 LEU C 39 18936 20216 15425 6200 2480 1209 C ATOM 1962 CD2 LEU C 39 24.821 -20.462 29.054 1.00137.48 C ANISOU 1962 CD2 LEU C 39 17374 19987 14875 5611 2518 1899 C ATOM 1963 N LEU C 40 28.060 -23.601 30.739 1.00120.92 N ANISOU 1963 N LEU C 40 15759 17174 13011 4695 2073 1334 N ATOM 1964 CA LEU C 40 27.785 -24.622 31.740 1.00125.23 C ANISOU 1964 CA LEU C 40 16182 17973 13427 4653 2096 1579 C ATOM 1965 C LEU C 40 28.966 -24.795 32.688 1.00119.34 C ANISOU 1965 C LEU C 40 15778 16917 12649 4711 1975 1254 C ATOM 1966 O LEU C 40 28.784 -24.945 33.894 1.00131.82 O ANISOU 1966 O LEU C 40 17413 18697 13976 4953 2059 1359 O ATOM 1967 CB LEU C 40 27.434 -25.951 31.069 1.00129.65 C ANISOU 1967 CB LEU C 40 16446 18631 14185 4128 1964 1871 C ATOM 1968 CG LEU C 40 25.937 -26.242 30.922 1.00138.55 C ANISOU 1968 CG LEU C 40 17142 20287 15213 4100 2100 2415 C ATOM 1969 CD1 LEU C 40 25.230 -25.134 30.155 1.00143.45 C ANISOU 1969 CD1 LEU C 40 17647 21044 15815 4330 2237 2466 C ATOM 1970 CD2 LEU C 40 25.714 -27.586 30.247 1.00138.04 C ANISOU 1970 CD2 LEU C 40 16857 20230 15363 3531 1892 2671 C ATOM 1971 N ALA C 41 30.175 -24.773 32.135 1.00105.65 N ANISOU 1971 N ALA C 41 14261 14718 11161 4487 1778 873 N ATOM 1972 CA ALA C 41 31.379 -24.935 32.941 1.00104.19 C ANISOU 1972 CA ALA C 41 14379 14215 10995 4511 1625 558 C ATOM 1973 C ALA C 41 31.525 -23.803 33.949 1.00105.73 C ANISOU 1973 C ALA C 41 14880 14380 10914 5011 1710 378 C ATOM 1974 O ALA C 41 31.824 -24.043 35.115 1.00110.79 O ANISOU 1974 O ALA C 41 15689 15031 11376 5169 1678 343 O ATOM 1975 CB ALA C 41 32.609 -25.009 32.051 1.00100.99 C ANISOU 1975 CB ALA C 41 14091 13365 10914 4200 1423 198 C ATOM 1976 N VAL C 42 31.306 -22.572 33.497 1.00 99.19 N ANISOU 1976 N VAL C 42 14149 13496 10040 5259 1794 264 N ATOM 1977 CA VAL C 42 31.408 -21.411 34.375 1.00 94.90 C ANISOU 1977 CA VAL C 42 13948 12878 9232 5759 1843 68 C ATOM 1978 C VAL C 42 30.366 -21.445 35.487 1.00109.15 C ANISOU 1978 C VAL C 42 15682 15143 10646 6172 2072 342 C ATOM 1979 O VAL C 42 30.692 -21.253 36.659 1.00110.98 O ANISOU 1979 O VAL C 42 16198 15343 10625 6462 2060 209 O ATOM 1980 CB VAL C 42 31.257 -20.098 33.587 1.00 90.12 C ANISOU 1980 CB VAL C 42 13458 12116 8666 5940 1865 -67 C ATOM 1981 CG1 VAL C 42 31.115 -18.917 34.536 1.00 96.82 C ANISOU 1981 CG1 VAL C 42 14665 12925 9197 6523 1920 -227 C ATOM 1982 CG2 VAL C 42 32.442 -19.906 32.658 1.00 84.30 C ANISOU 1982 CG2 VAL C 42 12852 10920 8259 5570 1641 -367 C ATOM 1983 N VAL C 43 29.114 -21.696 35.113 1.00105.29 N ANISOU 1983 N VAL C 43 14804 15102 10097 6190 2277 735 N ATOM 1984 CA VAL C 43 28.025 -21.774 36.082 1.00109.40 C ANISOU 1984 CA VAL C 43 15164 16155 10247 6564 2536 1058 C ATOM 1985 C VAL C 43 28.259 -22.882 37.101 1.00106.45 C ANISOU 1985 C VAL C 43 14781 15918 9747 6415 2499 1196 C ATOM 1986 O VAL C 43 28.152 -22.658 38.308 1.00111.36 O ANISOU 1986 O VAL C 43 15587 16716 10007 6799 2612 1187 O ATOM 1987 CB VAL C 43 26.665 -22.010 35.390 1.00105.39 C ANISOU 1987 CB VAL C 43 14154 16129 9762 6507 2730 1516 C ATOM 1988 CG1 VAL C 43 25.602 -22.393 36.411 1.00101.89 C ANISOU 1988 CG1 VAL C 43 13449 16303 8960 6782 2996 1923 C ATOM 1989 CG2 VAL C 43 26.244 -20.777 34.607 1.00106.22 C ANISOU 1989 CG2 VAL C 43 14282 16174 9903 6790 2799 1422 C ATOM 1990 N ILE C 44 28.584 -24.074 36.611 1.00 99.81 N ANISOU 1990 N ILE C 44 13753 14982 9189 5866 2326 1318 N ATOM 1991 CA ILE C 44 28.827 -25.205 37.495 1.00108.97 C ANISOU 1991 CA ILE C 44 14906 16225 10271 5671 2238 1472 C ATOM 1992 C ILE C 44 30.034 -24.955 38.393 1.00113.92 C ANISOU 1992 C ILE C 44 15997 16470 10816 5819 2067 1074 C ATOM 1993 O ILE C 44 29.951 -25.159 39.596 1.00113.91 O ANISOU 1993 O ILE C 44 16119 16663 10499 6026 2122 1167 O ATOM 1994 CB ILE C 44 29.023 -26.512 36.698 1.00106.75 C ANISOU 1994 CB ILE C 44 14389 15823 10350 5057 2026 1631 C ATOM 1995 CG1 ILE C 44 27.689 -26.962 36.101 1.00100.78 C ANISOU 1995 CG1 ILE C 44 13163 15526 9604 4887 2170 2130 C ATOM 1996 CG2 ILE C 44 29.588 -27.607 37.590 1.00101.91 C ANISOU 1996 CG2 ILE C 44 13879 15128 9713 4849 1844 1688 C ATOM 1997 CD1 ILE C 44 27.763 -28.262 35.332 1.00103.24 C ANISOU 1997 CD1 ILE C 44 13272 15718 10235 4291 1935 2309 C ATOM 1998 N ALA C 45 31.125 -24.444 37.829 1.00119.11 N ANISOU 1998 N ALA C 45 16910 16615 11732 5728 1864 648 N ATOM 1999 CA ALA C 45 32.335 -24.197 38.615 1.00118.92 C ANISOU 1999 CA ALA C 45 17305 16204 11674 5824 1655 276 C ATOM 2000 C ALA C 45 32.088 -23.170 39.715 1.00124.46 C ANISOU 2000 C ALA C 45 18330 17022 11938 6398 1789 167 C ATOM 2001 O ALA C 45 32.698 -23.233 40.782 1.00133.55 O ANISOU 2001 O ALA C 45 19789 18052 12900 6527 1667 22 O ATOM 2002 CB ALA C 45 33.474 -23.740 37.718 1.00115.43 C ANISOU 2002 CB ALA C 45 17020 15245 11595 5615 1433 -119 C ATOM 2003 N CYS C 46 31.195 -22.224 39.446 1.00127.12 N ANISOU 2003 N CYS C 46 18613 17582 12107 6756 2022 230 N ATOM 2004 CA CYS C 46 30.854 -21.189 40.416 1.00129.29 C ANISOU 2004 CA CYS C 46 19204 17976 11944 7368 2167 110 C ATOM 2005 C CYS C 46 29.841 -21.672 41.451 1.00131.50 C ANISOU 2005 C CYS C 46 19316 18856 11792 7636 2444 479 C ATOM 2006 O CYS C 46 29.698 -21.070 42.514 1.00132.46 O ANISOU 2006 O CYS C 46 19742 19100 11485 8133 2549 372 O ATOM 2007 CB CYS C 46 30.323 -19.944 39.706 1.00128.61 C ANISOU 2007 CB CYS C 46 19147 17861 11859 7688 2285 12 C ATOM 2008 SG CYS C 46 31.586 -19.010 38.811 1.00142.88 S ANISOU 2008 SG CYS C 46 21303 18949 14035 7504 1955 -463 S ATOM 2009 N TRP C 47 29.143 -22.761 41.141 1.00135.71 N ANISOU 2009 N TRP C 47 19373 19767 12422 7299 2551 919 N ATOM 2010 CA TRP C 47 28.106 -23.274 42.029 1.00141.05 C ANISOU 2010 CA TRP C 47 19807 21078 12708 7486 2827 1351 C ATOM 2011 C TRP C 47 28.710 -24.343 42.935 1.00134.16 C ANISOU 2011 C TRP C 47 19051 20165 11759 7215 2655 1431 C ATOM 2012 O TRP C 47 28.229 -24.577 44.042 1.00150.40 O ANISOU 2012 O TRP C 47 21119 22636 13388 7450 2829 1658 O ATOM 2013 CB TRP C 47 26.937 -23.825 41.177 1.00153.88 C ANISOU 2013 CB TRP C 47 20832 23152 14484 7245 3010 1839 C ATOM 2014 CG TRP C 47 25.781 -24.569 41.865 1.00167.30 C ANISOU 2014 CG TRP C 47 22129 25567 15871 7276 3280 2410 C ATOM 2015 CD1 TRP C 47 25.756 -25.120 43.116 1.00168.68 C ANISOU 2015 CD1 TRP C 47 22388 26019 15685 7353 3344 2586 C ATOM 2016 CD2 TRP C 47 24.487 -24.828 41.299 1.00173.41 C ANISOU 2016 CD2 TRP C 47 22334 26881 16672 7199 3507 2906 C ATOM 2017 NE1 TRP C 47 24.539 -25.702 43.361 1.00171.30 N ANISOU 2017 NE1 TRP C 47 22229 27043 15815 7319 3611 3170 N ATOM 2018 CE2 TRP C 47 23.741 -25.536 42.262 1.00176.94 C ANISOU 2018 CE2 TRP C 47 22524 27932 16773 7224 3709 3379 C ATOM 2019 CE3 TRP C 47 23.889 -24.529 40.071 1.00170.71 C ANISOU 2019 CE3 TRP C 47 21671 26579 16610 7097 3543 3014 C ATOM 2020 CZ2 TRP C 47 22.429 -25.948 42.037 1.00181.03 C ANISOU 2020 CZ2 TRP C 47 22449 29100 17235 7140 3946 3965 C ATOM 2021 CZ3 TRP C 47 22.586 -24.939 39.849 1.00172.73 C ANISOU 2021 CZ3 TRP C 47 21357 27459 16813 7026 3760 3580 C ATOM 2022 CH2 TRP C 47 21.871 -25.641 40.827 1.00178.96 C ANISOU 2022 CH2 TRP C 47 21872 28852 17273 7043 3959 4054 C ATOM 2023 N LEU C 48 29.833 -24.916 42.520 1.00119.12 N ANISOU 2023 N LEU C 48 17271 17746 10243 6764 2307 1215 N ATOM 2024 CA LEU C 48 30.461 -25.942 43.337 1.00122.64 C ANISOU 2024 CA LEU C 48 17839 18102 10657 6505 2097 1281 C ATOM 2025 C LEU C 48 31.263 -25.273 44.450 1.00123.40 C ANISOU 2025 C LEU C 48 18472 17961 10454 6871 1989 916 C ATOM 2026 O LEU C 48 31.779 -24.171 44.267 1.00117.67 O ANISOU 2026 O LEU C 48 18058 16898 9753 7132 1926 507 O ATOM 2027 CB LEU C 48 31.364 -26.841 42.491 1.00125.42 C ANISOU 2027 CB LEU C 48 18113 18000 11540 5928 1757 1180 C ATOM 2028 CG LEU C 48 30.695 -27.470 41.257 1.00133.38 C ANISOU 2028 CG LEU C 48 18660 19145 12873 5540 1799 1470 C ATOM 2029 CD1 LEU C 48 31.572 -28.523 40.564 1.00131.75 C ANISOU 2029 CD1 LEU C 48 18410 18517 13132 5000 1458 1377 C ATOM 2030 CD2 LEU C 48 29.238 -27.916 41.451 1.00141.15 C ANISOU 2030 CD2 LEU C 48 19235 20783 13614 5552 2078 2045 C ATOM 2031 N ASP C 49 31.371 -25.935 45.598 1.00132.77 N ANISOU 2031 N ASP C 49 19787 19306 11352 6868 1940 1074 N ATOM 2032 CA ASP C 49 32.200 -25.421 46.684 1.00140.46 C ANISOU 2032 CA ASP C 49 21298 20028 12041 7161 1780 735 C ATOM 2033 C ASP C 49 33.635 -25.893 46.504 1.00132.75 C ANISOU 2033 C ASP C 49 20523 18436 11480 6770 1330 440 C ATOM 2034 O ASP C 49 34.064 -26.866 47.125 1.00136.63 O ANISOU 2034 O ASP C 49 21059 18884 11971 6521 1128 572 O ATOM 2035 CB ASP C 49 31.669 -25.856 48.052 1.00155.99 C ANISOU 2035 CB ASP C 49 23343 22470 13455 7365 1935 1039 C ATOM 2036 CG ASP C 49 32.395 -25.174 49.199 1.00174.01 C ANISOU 2036 CG ASP C 49 26226 24531 15359 7744 1795 677 C ATOM 2037 OD1 ASP C 49 32.901 -24.049 48.995 1.00182.69 O ANISOU 2037 OD1 ASP C 49 27659 25258 16497 8020 1705 233 O ATOM 2038 OD2 ASP C 49 32.464 -25.758 50.303 1.00178.24 O ANISOU 2038 OD2 ASP C 49 26918 25252 15553 7749 1750 846 O ATOM 2039 N VAL C 50 34.373 -25.191 45.651 1.00123.56 N ANISOU 2039 N VAL C 50 19468 16809 10669 6721 1171 55 N ATOM 2040 CA VAL C 50 35.748 -25.557 45.342 1.00108.16 C ANISOU 2040 CA VAL C 50 17641 14303 9151 6365 770 -233 C ATOM 2041 C VAL C 50 36.684 -24.365 45.496 1.00100.98 C ANISOU 2041 C VAL C 50 17172 12952 8244 6595 574 -711 C ATOM 2042 O VAL C 50 36.245 -23.214 45.512 1.00113.52 O ANISOU 2042 O VAL C 50 18942 14596 9594 6986 740 -845 O ATOM 2043 CB VAL C 50 35.874 -26.113 43.906 1.00104.68 C ANISOU 2043 CB VAL C 50 16808 13713 9252 5922 720 -194 C ATOM 2044 CG1 VAL C 50 35.122 -27.429 43.774 1.00 97.35 C ANISOU 2044 CG1 VAL C 50 15495 13120 8374 5613 800 265 C ATOM 2045 CG2 VAL C 50 35.360 -25.098 42.894 1.00 95.95 C ANISOU 2045 CG2 VAL C 50 15590 12641 8226 6069 931 -286 C ATOM 2046 N ASP C 51 37.976 -24.651 45.609 1.00 99.48 N ANISOU 2046 N ASP C 51 17150 12314 8333 6349 197 -957 N ATOM 2047 CA ASP C 51 38.986 -23.608 45.736 1.00 99.48 C ANISOU 2047 CA ASP C 51 17545 11861 8392 6476 -59 -1384 C ATOM 2048 C ASP C 51 39.238 -22.913 44.400 1.00109.95 C ANISOU 2048 C ASP C 51 18722 12947 10105 6339 -51 -1573 C ATOM 2049 O ASP C 51 38.733 -23.341 43.361 1.00 98.76 O ANISOU 2049 O ASP C 51 16901 11689 8934 6120 128 -1396 O ATOM 2050 CB ASP C 51 40.285 -24.190 46.300 1.00103.52 C ANISOU 2050 CB ASP C 51 18229 12010 9094 6238 -478 -1543 C ATOM 2051 CG ASP C 51 40.788 -25.374 45.501 1.00127.76 C ANISOU 2051 CG ASP C 51 20902 14967 12674 5761 -609 -1451 C ATOM 2052 OD1 ASP C 51 39.954 -26.208 45.093 1.00132.70 O ANISOU 2052 OD1 ASP C 51 21181 15905 13334 5617 -398 -1131 O ATOM 2053 OD2 ASP C 51 42.015 -25.476 45.288 1.00142.32 O ANISOU 2053 OD2 ASP C 51 22779 16414 14881 5538 -934 -1694 O ATOM 2054 N ALA C 52 40.016 -21.836 44.441 1.00 68.84 N ANISOU 2054 N ALA C 52 11411 8731 6013 2365 1293 -275 N ATOM 2055 CA ALA C 52 40.226 -20.978 43.279 1.00 70.91 C ANISOU 2055 CA ALA C 52 11502 8879 6561 2604 1231 -351 C ATOM 2056 C ALA C 52 40.874 -21.716 42.112 1.00 69.94 C ANISOU 2056 C ALA C 52 11404 8508 6663 2472 1050 -250 C ATOM 2057 O ALA C 52 40.408 -21.620 40.977 1.00 69.45 O ANISOU 2057 O ALA C 52 11105 8535 6747 2503 1066 -226 O ATOM 2058 CB ALA C 52 41.068 -19.776 43.667 1.00 66.98 C ANISOU 2058 CB ALA C 52 11135 8162 6152 2909 1175 -524 C ATOM 2059 N CYS C 53 41.952 -22.440 42.396 1.00 73.54 N ANISOU 2059 N CYS C 53 12142 8660 7141 2335 872 -201 N ATOM 2060 CA CYS C 53 42.683 -23.173 41.367 1.00 75.83 C ANISOU 2060 CA CYS C 53 12475 8682 7655 2200 694 -126 C ATOM 2061 C CYS C 53 41.784 -24.179 40.658 1.00 78.07 C ANISOU 2061 C CYS C 53 12561 9178 7926 1931 769 10 C ATOM 2062 O CYS C 53 41.855 -24.337 39.441 1.00 72.66 O ANISOU 2062 O CYS C 53 11734 8431 7442 1904 705 30 O ATOM 2063 CB CYS C 53 43.893 -23.887 41.971 1.00 66.96 C ANISOU 2063 CB CYS C 53 11685 7230 6526 2088 497 -98 C ATOM 2064 SG CYS C 53 45.082 -22.782 42.761 1.00127.37 S ANISOU 2064 SG CYS C 53 19558 14623 14216 2386 379 -304 S ATOM 2065 N THR C 54 40.932 -24.847 41.428 1.00 75.11 N ANISOU 2065 N THR C 54 12171 9057 7309 1727 921 90 N ATOM 2066 CA THR C 54 40.005 -25.825 40.876 1.00 72.16 C ANISOU 2066 CA THR C 54 11596 8907 6913 1445 1028 191 C ATOM 2067 C THR C 54 38.970 -25.150 39.988 1.00 72.69 C ANISOU 2067 C THR C 54 11278 9295 7047 1580 1147 117 C ATOM 2068 O THR C 54 38.634 -25.653 38.915 1.00 81.62 O ANISOU 2068 O THR C 54 12207 10501 8302 1455 1130 150 O ATOM 2069 CB THR C 54 39.282 -26.604 41.990 1.00 73.83 C ANISOU 2069 CB THR C 54 11889 9324 6840 1196 1207 275 C ATOM 2070 OG1 THR C 54 40.246 -27.293 42.796 1.00 73.87 O ANISOU 2070 OG1 THR C 54 12273 9030 6764 1084 1080 369 O ATOM 2071 CG2 THR C 54 38.304 -27.610 41.401 1.00 62.72 C ANISOU 2071 CG2 THR C 54 10252 8144 5433 885 1346 348 C ATOM 2072 N ARG C 55 38.476 -24.003 40.440 1.00 77.17 N ANISOU 2072 N ARG C 55 11741 10050 7529 1848 1260 9 N ATOM 2073 CA ARG C 55 37.468 -23.251 39.706 1.00 75.52 C ANISOU 2073 CA ARG C 55 11172 10153 7368 2033 1368 -66 C ATOM 2074 C ARG C 55 38.046 -22.788 38.371 1.00 78.55 C ANISOU 2074 C ARG C 55 11493 10344 8010 2215 1208 -75 C ATOM 2075 O ARG C 55 37.384 -22.849 37.334 1.00 79.53 O ANISOU 2075 O ARG C 55 11339 10672 8205 2221 1223 -68 O ATOM 2076 CB ARG C 55 37.007 -22.045 40.522 1.00 71.85 C ANISOU 2076 CB ARG C 55 10653 9858 6788 2316 1506 -188 C ATOM 2077 CG ARG C 55 35.782 -21.339 39.980 1.00 84.09 C ANISOU 2077 CG ARG C 55 11818 11785 8346 2503 1644 -267 C ATOM 2078 CD ARG C 55 35.418 -20.166 40.875 1.00100.88 C ANISOU 2078 CD ARG C 55 13917 14037 10375 2779 1782 -399 C ATOM 2079 NE ARG C 55 35.461 -20.519 42.293 1.00112.23 N ANISOU 2079 NE ARG C 55 15559 15501 11581 2612 1883 -411 N ATOM 2080 CZ ARG C 55 34.487 -21.125 42.963 1.00110.42 C ANISOU 2080 CZ ARG C 55 15222 15594 11138 2383 2074 -409 C ATOM 2081 NH1 ARG C 55 33.369 -21.480 42.349 1.00115.97 N ANISOU 2081 NH1 ARG C 55 15585 16634 11845 2279 2185 -417 N ATOM 2082 NH2 ARG C 55 34.641 -21.391 44.252 1.00109.64 N ANISOU 2082 NH2 ARG C 55 15359 15487 10815 2250 2159 -406 N ATOM 2083 N VAL C 56 39.293 -22.330 38.418 1.00 63.04 N ANISOU 2083 N VAL C 56 9787 7990 6175 2359 1060 -102 N ATOM 2084 CA VAL C 56 40.017 -21.892 37.230 1.00 67.43 C ANISOU 2084 CA VAL C 56 10345 8300 6977 2513 919 -114 C ATOM 2085 C VAL C 56 40.244 -23.040 36.252 1.00 71.30 C ANISOU 2085 C VAL C 56 10800 8713 7578 2238 807 -21 C ATOM 2086 O VAL C 56 40.032 -22.893 35.048 1.00 64.25 O ANISOU 2086 O VAL C 56 9724 7884 6806 2301 774 -13 O ATOM 2087 CB VAL C 56 41.377 -21.267 37.607 1.00 63.36 C ANISOU 2087 CB VAL C 56 10128 7364 6583 2676 800 -192 C ATOM 2088 CG1 VAL C 56 42.246 -21.074 36.371 1.00 52.22 C ANISOU 2088 CG1 VAL C 56 8755 5655 5432 2749 661 -197 C ATOM 2089 CG2 VAL C 56 41.169 -19.947 38.327 1.00 72.19 C ANISOU 2089 CG2 VAL C 56 11242 8542 7642 2990 918 -314 C ATOM 2090 N LEU C 57 40.667 -24.184 36.780 1.00 70.88 N ANISOU 2090 N LEU C 57 10928 8525 7478 1938 752 47 N ATOM 2091 CA LEU C 57 40.960 -25.348 35.951 1.00 66.26 C ANISOU 2091 CA LEU C 57 10332 7829 7013 1655 651 123 C ATOM 2092 C LEU C 57 39.711 -25.886 35.259 1.00 74.23 C ANISOU 2092 C LEU C 57 11006 9228 7971 1493 768 151 C ATOM 2093 O LEU C 57 39.781 -26.363 34.127 1.00 75.28 O ANISOU 2093 O LEU C 57 11015 9345 8243 1383 694 165 O ATOM 2094 CB LEU C 57 41.605 -26.452 36.792 1.00 73.87 C ANISOU 2094 CB LEU C 57 11575 8567 7925 1386 584 198 C ATOM 2095 CG LEU C 57 43.068 -26.246 37.192 1.00 72.27 C ANISOU 2095 CG LEU C 57 11697 7930 7832 1488 398 158 C ATOM 2096 CD1 LEU C 57 43.504 -27.300 38.198 1.00 72.75 C ANISOU 2096 CD1 LEU C 57 12026 7836 7778 1261 345 248 C ATOM 2097 CD2 LEU C 57 43.968 -26.266 35.967 1.00 56.48 C ANISOU 2097 CD2 LEU C 57 9700 5647 6114 1505 236 120 C ATOM 2098 N LEU C 58 38.572 -25.811 35.942 1.00 66.80 N ANISOU 2098 N LEU C 58 9904 8647 6829 1472 955 138 N ATOM 2099 CA LEU C 58 37.310 -26.264 35.366 1.00 66.10 C ANISOU 2099 CA LEU C 58 9460 8970 6686 1327 1082 125 C ATOM 2100 C LEU C 58 36.880 -25.386 34.192 1.00 75.83 C ANISOU 2100 C LEU C 58 10412 10389 8011 1603 1048 62 C ATOM 2101 O LEU C 58 36.372 -25.884 33.188 1.00 70.80 O ANISOU 2101 O LEU C 58 9526 9949 7426 1484 1035 53 O ATOM 2102 CB LEU C 58 36.213 -26.288 36.435 1.00 70.27 C ANISOU 2102 CB LEU C 58 9880 9837 6982 1257 1306 97 C ATOM 2103 CG LEU C 58 36.339 -27.370 37.511 1.00 72.32 C ANISOU 2103 CG LEU C 58 10376 9997 7104 923 1386 182 C ATOM 2104 CD1 LEU C 58 35.252 -27.211 38.562 1.00 71.25 C ANISOU 2104 CD1 LEU C 58 10137 10206 6729 886 1631 138 C ATOM 2105 CD2 LEU C 58 36.287 -28.756 36.888 1.00 71.63 C ANISOU 2105 CD2 LEU C 58 10240 9874 7103 544 1377 247 C ATOM 2106 N ILE C 59 37.091 -24.080 34.325 1.00 79.80 N ANISOU 2106 N ILE C 59 10963 10828 8529 1977 1036 16 N ATOM 2107 CA ILE C 59 36.701 -23.123 33.293 1.00 68.81 C ANISOU 2107 CA ILE C 59 9349 9588 7209 2292 1011 -22 C ATOM 2108 C ILE C 59 37.700 -23.074 32.136 1.00 70.91 C ANISOU 2108 C ILE C 59 9728 9541 7674 2344 835 15 C ATOM 2109 O ILE C 59 37.314 -23.189 30.973 1.00 66.15 O ANISOU 2109 O ILE C 59 8909 9109 7116 2358 789 23 O ATOM 2110 CB ILE C 59 36.548 -21.704 33.876 1.00 69.63 C ANISOU 2110 CB ILE C 59 9475 9710 7272 2682 1089 -84 C ATOM 2111 CG1 ILE C 59 35.481 -21.686 34.970 1.00 70.06 C ANISOU 2111 CG1 ILE C 59 9385 10110 7126 2642 1280 -143 C ATOM 2112 CG2 ILE C 59 36.206 -20.709 32.777 1.00 61.36 C ANISOU 2112 CG2 ILE C 59 8236 8773 6304 3032 1058 -97 C ATOM 2113 CD1 ILE C 59 35.343 -20.350 35.658 1.00 68.27 C ANISOU 2113 CD1 ILE C 59 9184 9893 6861 3000 1370 -224 C ATOM 2114 N SER C 60 38.979 -22.908 32.465 1.00 62.49 N ANISOU 2114 N SER C 60 8993 8032 6719 2368 739 23 N ATOM 2115 CA SER C 60 40.028 -22.743 31.458 1.00 58.38 C ANISOU 2115 CA SER C 60 8606 7176 6400 2430 593 34 C ATOM 2116 C SER C 60 40.156 -23.947 30.521 1.00 60.85 C ANISOU 2116 C SER C 60 8840 7490 6792 2115 501 74 C ATOM 2117 O SER C 60 40.394 -23.785 29.323 1.00 69.54 O ANISOU 2117 O SER C 60 9876 8544 8000 2184 424 79 O ATOM 2118 CB SER C 60 41.375 -22.475 32.137 1.00 51.33 C ANISOU 2118 CB SER C 60 8068 5822 5615 2468 515 -2 C ATOM 2119 OG SER C 60 41.736 -23.550 32.985 1.00 91.99 O ANISOU 2119 OG SER C 60 13374 10862 10716 2167 478 23 O ATOM 2120 N SER C 61 39.999 -25.148 31.072 1.00 68.88 N ANISOU 2120 N SER C 61 9871 8550 7750 1770 520 101 N ATOM 2121 CA SER C 61 40.110 -26.378 30.288 1.00 72.74 C ANISOU 2121 CA SER C 61 10287 9023 8327 1440 452 124 C ATOM 2122 C SER C 61 39.047 -26.441 29.195 1.00 82.51 C ANISOU 2122 C SER C 61 11155 10674 9523 1444 492 100 C ATOM 2123 O SER C 61 39.303 -26.931 28.095 1.00 89.27 O ANISOU 2123 O SER C 61 11935 11496 10490 1323 403 92 O ATOM 2124 CB SER C 61 40.003 -27.605 31.195 1.00 75.29 C ANISOU 2124 CB SER C 61 10697 9329 8581 1084 504 167 C ATOM 2125 OG SER C 61 38.729 -27.680 31.812 1.00 77.37 O ANISOU 2125 OG SER C 61 10755 9995 8647 1035 683 160 O ATOM 2126 N VAL C 62 37.857 -25.940 29.505 1.00 74.84 N ANISOU 2126 N VAL C 62 9943 10104 8389 1589 621 73 N ATOM 2127 CA VAL C 62 36.752 -25.947 28.553 1.00 72.62 C ANISOU 2127 CA VAL C 62 9279 10267 8047 1626 652 27 C ATOM 2128 C VAL C 62 36.935 -24.827 27.534 1.00 63.40 C ANISOU 2128 C VAL C 62 8073 9086 6928 2004 563 35 C ATOM 2129 O VAL C 62 36.632 -24.992 26.351 1.00 76.21 O ANISOU 2129 O VAL C 62 9492 10900 8565 2006 498 20 O ATOM 2130 CB VAL C 62 35.394 -25.791 29.268 1.00 69.73 C ANISOU 2130 CB VAL C 62 8649 10347 7498 1659 825 -29 C ATOM 2131 CG1 VAL C 62 34.254 -25.728 28.257 1.00 63.39 C ANISOU 2131 CG1 VAL C 62 7423 10027 6636 1737 836 -104 C ATOM 2132 CG2 VAL C 62 35.178 -26.941 30.236 1.00 69.85 C ANISOU 2132 CG2 VAL C 62 8717 10372 7450 1262 942 -26 C ATOM 2133 N MET C 63 37.446 -23.693 28.000 1.00 64.66 N ANISOU 2133 N MET C 63 8443 9014 7110 2320 568 57 N ATOM 2134 CA MET C 63 37.722 -22.562 27.125 1.00 60.96 C ANISOU 2134 CA MET C 63 8003 8459 6699 2689 510 81 C ATOM 2135 C MET C 63 38.833 -22.913 26.140 1.00 63.69 C ANISOU 2135 C MET C 63 8522 8470 7208 2576 377 108 C ATOM 2136 O MET C 63 38.866 -22.399 25.022 1.00 60.48 O ANISOU 2136 O MET C 63 8061 8094 6824 2769 323 135 O ATOM 2137 CB MET C 63 38.100 -21.326 27.946 1.00 69.24 C ANISOU 2137 CB MET C 63 9261 9283 7763 3012 573 79 C ATOM 2138 CG MET C 63 36.962 -20.770 28.792 1.00 70.13 C ANISOU 2138 CG MET C 63 9183 9742 7720 3188 712 37 C ATOM 2139 SD MET C 63 37.276 -19.104 29.406 1.00 97.53 S ANISOU 2139 SD MET C 63 12838 12992 11229 3647 791 17 S ATOM 2140 CE MET C 63 37.080 -18.141 27.912 1.00 62.78 C ANISOU 2140 CE MET C 63 8332 8646 6876 4030 737 81 C ATOM 2141 N LEU C 64 39.738 -23.794 26.562 1.00 59.96 N ANISOU 2141 N LEU C 64 8260 7679 6842 2267 327 100 N ATOM 2142 CA LEU C 64 40.822 -24.254 25.701 1.00 58.52 C ANISOU 2142 CA LEU C 64 8231 7170 6834 2116 206 99 C ATOM 2143 C LEU C 64 40.272 -24.994 24.487 1.00 66.74 C ANISOU 2143 C LEU C 64 9006 8499 7852 1946 160 90 C ATOM 2144 O LEU C 64 40.799 -24.871 23.382 1.00 56.76 O ANISOU 2144 O LEU C 64 7777 7116 6674 1985 81 92 O ATOM 2145 CB LEU C 64 41.779 -25.162 26.474 1.00 50.63 C ANISOU 2145 CB LEU C 64 7475 5814 5948 1815 155 82 C ATOM 2146 CG LEU C 64 42.946 -25.741 25.668 1.00 57.80 C ANISOU 2146 CG LEU C 64 8533 6367 7060 1631 30 55 C ATOM 2147 CD1 LEU C 64 43.875 -24.636 25.193 1.00 57.46 C ANISOU 2147 CD1 LEU C 64 8686 6006 7141 1907 -4 33 C ATOM 2148 CD2 LEU C 64 43.706 -26.776 26.480 1.00 55.41 C ANISOU 2148 CD2 LEU C 64 8428 5772 6853 1330 -27 42 C ATOM 2149 N VAL C 65 39.206 -25.758 24.705 1.00 65.29 N ANISOU 2149 N VAL C 65 8555 8703 7550 1748 222 65 N ATOM 2150 CA VAL C 65 38.539 -26.480 23.628 1.00 62.40 C ANISOU 2150 CA VAL C 65 7886 8676 7149 1578 191 20 C ATOM 2151 C VAL C 65 38.007 -25.497 22.588 1.00 65.31 C ANISOU 2151 C VAL C 65 8079 9311 7424 1937 157 34 C ATOM 2152 O VAL C 65 38.098 -25.740 21.384 1.00 69.50 O ANISOU 2152 O VAL C 65 8511 9924 7973 1896 73 18 O ATOM 2153 CB VAL C 65 37.386 -27.356 24.162 1.00 67.33 C ANISOU 2153 CB VAL C 65 8233 9691 7660 1321 299 -36 C ATOM 2154 CG1 VAL C 65 36.618 -27.997 23.014 1.00 59.53 C ANISOU 2154 CG1 VAL C 65 6888 9100 6631 1173 272 -119 C ATOM 2155 CG2 VAL C 65 37.927 -28.422 25.104 1.00 68.83 C ANISOU 2155 CG2 VAL C 65 8623 9596 7932 953 336 -24 C ATOM 2156 N AMET C 66 37.461 -24.382 23.063 0.45 68.31 N ANISOU 2156 N AMET C 66 8430 9824 7700 2297 222 66 N ATOM 2157 N BMET C 66 37.459 -24.382 23.062 0.55 68.18 N ANISOU 2157 N BMET C 66 8413 9809 7684 2298 222 66 N ATOM 2158 CA AMET C 66 36.930 -23.347 22.183 0.45 70.57 C ANISOU 2158 CA AMET C 66 8578 10346 7890 2695 193 101 C ATOM 2159 CA BMET C 66 36.930 -23.352 22.174 0.55 70.53 C ANISOU 2159 CA BMET C 66 8571 10342 7885 2694 193 101 C ATOM 2160 C AMET C 66 38.042 -22.649 21.406 0.45 71.81 C ANISOU 2160 C AMET C 66 9020 10108 8156 2883 123 173 C ATOM 2161 C BMET C 66 38.043 -22.650 21.404 0.55 72.18 C ANISOU 2161 C BMET C 66 9067 10155 8203 2883 122 173 C ATOM 2162 O AMET C 66 37.883 -22.330 20.227 0.45 73.21 O ANISOU 2162 O AMET C 66 9110 10431 8277 3049 57 207 O ATOM 2163 O BMET C 66 37.882 -22.322 20.228 0.55 73.37 O ANISOU 2163 O BMET C 66 9130 10450 8296 3051 58 208 O ATOM 2164 CB AMET C 66 36.133 -22.319 22.989 0.45 69.11 C ANISOU 2164 CB AMET C 66 8314 10350 7597 3037 293 110 C ATOM 2165 CB BMET C 66 36.116 -22.326 22.964 0.55 68.91 C ANISOU 2165 CB BMET C 66 8281 10332 7568 3037 292 110 C ATOM 2166 CG AMET C 66 35.706 -21.102 22.185 0.45 62.87 C ANISOU 2166 CG AMET C 66 7444 9718 6724 3509 265 171 C ATOM 2167 CG BMET C 66 34.620 -22.408 22.722 0.55 76.76 C ANISOU 2167 CG BMET C 66 8841 11931 8392 3115 318 43 C ATOM 2168 SD AMET C 66 34.858 -19.862 23.179 0.45 85.79 S ANISOU 2168 SD AMET C 66 10270 12785 9539 3922 390 168 S ATOM 2169 SD BMET C 66 33.709 -21.069 23.512 0.55110.14 S ANISOU 2169 SD BMET C 66 12963 16372 12512 3574 427 43 S ATOM 2170 CE AMET C 66 33.330 -20.717 23.553 0.45107.06 C ANISOU 2170 CE AMET C 66 12492 16105 12081 3717 445 36 C ATOM 2171 CE BMET C 66 34.500 -19.642 22.776 0.55 80.73 C ANISOU 2171 CE BMET C 66 9524 12299 8850 4050 368 177 C ATOM 2172 N ILE C 67 39.168 -22.421 22.074 1.00 68.54 N ANISOU 2172 N ILE C 67 8949 9202 7891 2854 141 187 N ATOM 2173 CA ILE C 67 40.314 -21.766 21.452 1.00 68.99 C ANISOU 2173 CA ILE C 67 9295 8837 8080 2999 104 228 C ATOM 2174 C ILE C 67 40.864 -22.600 20.298 1.00 76.90 C ANISOU 2174 C ILE C 67 10293 9771 9156 2741 5 206 C ATOM 2175 O ILE C 67 41.104 -22.086 19.204 1.00 68.39 O ANISOU 2175 O ILE C 67 9261 8657 8067 2912 -26 252 O ATOM 2176 CB ILE C 67 41.437 -21.507 22.476 1.00 63.43 C ANISOU 2176 CB ILE C 67 8927 7634 7539 2966 138 199 C ATOM 2177 CG1 ILE C 67 40.965 -20.522 23.548 1.00 70.55 C ANISOU 2177 CG1 ILE C 67 9852 8583 8370 3257 245 207 C ATOM 2178 CG2 ILE C 67 42.680 -20.976 21.783 1.00 54.31 C ANISOU 2178 CG2 ILE C 67 8043 6042 6550 3021 112 200 C ATOM 2179 CD1 ILE C 67 41.963 -20.305 24.664 1.00 64.22 C ANISOU 2179 CD1 ILE C 67 9335 7366 7699 3186 272 150 C ATOM 2180 N VAL C 68 41.055 -23.890 20.551 1.00 67.85 N ANISOU 2180 N VAL C 68 9099 8602 8080 2329 -33 138 N ATOM 2181 CA VAL C 68 41.572 -24.805 19.541 1.00 70.70 C ANISOU 2181 CA VAL C 68 9437 8895 8530 2041 -118 90 C ATOM 2182 C VAL C 68 40.582 -24.967 18.388 1.00 70.66 C ANISOU 2182 C VAL C 68 9108 9380 8359 2082 -156 85 C ATOM 2183 O VAL C 68 40.977 -25.046 17.223 1.00 75.05 O ANISOU 2183 O VAL C 68 9677 9906 8933 2057 -219 78 O ATOM 2184 CB VAL C 68 41.884 -26.187 20.153 1.00 75.06 C ANISOU 2184 CB VAL C 68 9995 9326 9198 1597 -138 19 C ATOM 2185 CG1 VAL C 68 42.351 -27.160 19.081 1.00 78.35 C ANISOU 2185 CG1 VAL C 68 10357 9692 9720 1293 -217 -50 C ATOM 2186 CG2 VAL C 68 42.936 -26.053 21.240 1.00 62.60 C ANISOU 2186 CG2 VAL C 68 8745 7269 7771 1573 -132 18 C ATOM 2187 N GLU C 69 39.294 -24.996 18.719 1.00 61.39 N ANISOU 2187 N GLU C 69 7638 8671 7018 2150 -115 74 N ATOM 2188 CA GLU C 69 38.244 -25.142 17.718 1.00 57.75 C ANISOU 2188 CA GLU C 69 6824 8735 6385 2209 -161 41 C ATOM 2189 C GLU C 69 38.251 -23.968 16.743 1.00 66.03 C ANISOU 2189 C GLU C 69 7931 9829 7328 2633 -205 137 C ATOM 2190 O GLU C 69 38.087 -24.149 15.536 1.00 70.25 O ANISOU 2190 O GLU C 69 8334 10583 7777 2637 -286 123 O ATOM 2191 CB GLU C 69 36.874 -25.258 18.387 1.00 55.49 C ANISOU 2191 CB GLU C 69 6210 8921 5952 2238 -94 -10 C ATOM 2192 CG GLU C 69 35.713 -25.385 17.414 1.00 92.45 C ANISOU 2192 CG GLU C 69 10484 14190 10451 2319 -150 -78 C ATOM 2193 CD GLU C 69 35.812 -26.633 16.555 1.00115.97 C ANISOU 2193 CD GLU C 69 13301 17289 13474 1921 -212 -193 C ATOM 2194 OE1 GLU C 69 35.861 -27.743 17.127 1.00124.56 O ANISOU 2194 OE1 GLU C 69 14345 18313 14669 1510 -154 -280 O ATOM 2195 OE2 GLU C 69 35.845 -26.506 15.313 1.00115.34 O ANISOU 2195 OE2 GLU C 69 13147 17360 13317 2020 -312 -197 O ATOM 2196 N LEU C 70 38.439 -22.765 17.279 1.00 64.02 N ANISOU 2196 N LEU C 70 7884 9365 7077 2992 -145 234 N ATOM 2197 CA LEU C 70 38.515 -21.559 16.461 1.00 71.05 C ANISOU 2197 CA LEU C 70 8891 10221 7884 3419 -158 351 C ATOM 2198 C LEU C 70 39.711 -21.596 15.517 1.00 73.72 C ANISOU 2198 C LEU C 70 9496 10185 8330 3327 -195 377 C ATOM 2199 O LEU C 70 39.610 -21.192 14.358 1.00 66.35 O ANISOU 2199 O LEU C 70 8551 9382 7276 3519 -242 444 O ATOM 2200 CB LEU C 70 38.591 -20.314 17.348 1.00 56.15 C ANISOU 2200 CB LEU C 70 7200 8107 6027 3778 -56 429 C ATOM 2201 CG LEU C 70 37.293 -19.877 18.024 1.00 70.58 C ANISOU 2201 CG LEU C 70 8760 10346 7710 4018 -11 423 C ATOM 2202 CD1 LEU C 70 37.573 -18.879 19.135 1.00 61.93 C ANISOU 2202 CD1 LEU C 70 7887 8947 6698 4257 106 457 C ATOM 2203 CD2 LEU C 70 36.363 -19.273 16.990 1.00 71.57 C ANISOU 2203 CD2 LEU C 70 8667 10893 7633 4383 -77 489 C ATOM 2204 N LEU C 71 40.842 -22.080 16.020 1.00 65.18 N ANISOU 2204 N LEU C 71 8655 8642 7467 3039 -172 320 N ATOM 2205 CA LEU C 71 42.044 -22.220 15.206 1.00 70.18 C ANISOU 2205 CA LEU C 71 9530 8899 8237 2899 -196 306 C ATOM 2206 C LEU C 71 41.859 -23.271 14.117 1.00 75.41 C ANISOU 2206 C LEU C 71 9979 9831 8842 2616 -290 233 C ATOM 2207 O LEU C 71 42.327 -23.098 12.992 1.00 61.89 O ANISOU 2207 O LEU C 71 8362 8048 7106 2651 -316 255 O ATOM 2208 CB LEU C 71 43.244 -22.576 16.081 1.00 59.00 C ANISOU 2208 CB LEU C 71 8376 6960 7079 2651 -167 229 C ATOM 2209 CG LEU C 71 43.758 -21.450 16.978 1.00 66.33 C ANISOU 2209 CG LEU C 71 9572 7530 8098 2913 -70 269 C ATOM 2210 CD1 LEU C 71 44.852 -21.957 17.900 1.00 63.07 C ANISOU 2210 CD1 LEU C 71 9308 6736 7920 2534 -70 157 C ATOM 2211 CD2 LEU C 71 44.256 -20.285 16.136 1.00 57.29 C ANISOU 2211 CD2 LEU C 71 8524 6287 6957 2902 -3 314 C ATOM 2212 N ASN C 72 41.176 -24.358 14.460 1.00 65.36 N ANISOU 2212 N ASN C 72 8423 8866 7546 2327 -325 137 N ATOM 2213 CA ASN C 72 40.869 -25.403 13.494 1.00 60.66 C ANISOU 2213 CA ASN C 72 7577 8573 6898 2042 -403 37 C ATOM 2214 C ASN C 72 39.992 -24.845 12.381 1.00 65.94 C ANISOU 2214 C ASN C 72 8041 9707 7305 2341 -460 90 C ATOM 2215 O ASN C 72 40.200 -25.138 11.205 1.00 56.37 O ANISOU 2215 O ASN C 72 6791 8591 6037 2259 -523 57 O ATOM 2216 CB ASN C 72 40.180 -26.589 14.176 1.00 64.68 C ANISOU 2216 CB ASN C 72 7811 9332 7431 1698 -396 -78 C ATOM 2217 CG ASN C 72 39.689 -27.630 13.185 1.00 62.89 C ANISOU 2217 CG ASN C 72 7271 9481 7142 1417 -460 -208 C ATOM 2218 OD1 ASN C 72 40.417 -28.035 12.279 1.00 70.41 O ANISOU 2218 OD1 ASN C 72 8302 10281 8170 1246 -509 -260 O ATOM 2219 ND2 ASN C 72 38.446 -28.069 13.355 1.00 65.97 N ANISOU 2219 ND2 ASN C 72 7294 10371 7399 1361 -451 -284 N ATOM 2220 N SER C 73 39.014 -24.032 12.766 1.00 59.51 N ANISOU 2220 N SER C 73 7097 9187 6327 2700 -441 168 N ATOM 2221 CA SER C 73 38.122 -23.395 11.807 1.00 63.02 C ANISOU 2221 CA SER C 73 7350 10084 6509 3054 -509 231 C ATOM 2222 C SER C 73 38.888 -22.435 10.899 1.00 68.78 C ANISOU 2222 C SER C 73 8399 10535 7198 3338 -510 375 C ATOM 2223 O SER C 73 38.564 -22.291 9.719 1.00 75.75 O ANISOU 2223 O SER C 73 9189 11709 7885 3484 -591 410 O ATOM 2224 CB SER C 73 37.001 -22.652 12.536 1.00 55.96 C ANISOU 2224 CB SER C 73 6277 9499 5486 3403 -479 280 C ATOM 2225 OG SER C 73 36.183 -23.551 13.263 1.00 85.08 O ANISOU 2225 OG SER C 73 9642 13503 9183 3134 -463 136 O ATOM 2226 N ALA C 74 39.898 -21.776 11.458 1.00 64.52 N ANISOU 2226 N ALA C 74 8239 9437 6838 3414 -411 451 N ATOM 2227 CA ALA C 74 40.736 -20.858 10.694 1.00 65.64 C ANISOU 2227 CA ALA C 74 8725 9236 6981 3647 -366 577 C ATOM 2228 C ALA C 74 41.550 -21.594 9.634 1.00 70.36 C ANISOU 2228 C ALA C 74 9398 9712 7625 3334 -408 503 C ATOM 2229 O ALA C 74 41.675 -21.131 8.499 1.00 65.37 O ANISOU 2229 O ALA C 74 8865 9129 6842 3512 -422 590 O ATOM 2230 CB ALA C 74 41.660 -20.087 11.626 1.00 57.08 C ANISOU 2230 CB ALA C 74 7999 7575 6114 3742 -235 621 C ATOM 2231 N ILE C 75 42.097 -22.744 10.014 1.00 59.30 N ANISOU 2231 N ILE C 75 7955 8150 6428 2872 -422 343 N ATOM 2232 CA ILE C 75 42.874 -23.576 9.102 1.00 59.88 C ANISOU 2232 CA ILE C 75 8067 8101 6581 2527 -457 234 C ATOM 2233 C ILE C 75 41.984 -24.128 7.993 1.00 65.79 C ANISOU 2233 C ILE C 75 8486 9426 7084 2484 -567 187 C ATOM 2234 O ILE C 75 42.380 -24.179 6.828 1.00 62.18 O ANISOU 2234 O ILE C 75 8096 8983 6546 2446 -592 180 O ATOM 2235 CB ILE C 75 43.559 -24.733 9.856 1.00 68.86 C ANISOU 2235 CB ILE C 75 9207 8954 8003 2058 -456 70 C ATOM 2236 CG1 ILE C 75 44.593 -24.178 10.836 1.00 71.09 C ANISOU 2236 CG1 ILE C 75 9834 8652 8523 2103 -366 95 C ATOM 2237 CG2 ILE C 75 44.208 -25.711 8.885 1.00 59.68 C ANISOU 2237 CG2 ILE C 75 8017 7733 6925 1686 -500 -69 C ATOM 2238 CD1 ILE C 75 45.234 -25.229 11.705 1.00 75.30 C ANISOU 2238 CD1 ILE C 75 10388 8905 9318 1706 -381 -44 C ATOM 2239 N GLU C 76 40.771 -24.521 8.368 1.00 68.82 N ANISOU 2239 N GLU C 76 8506 10297 7343 2492 -625 138 N ATOM 2240 CA GLU C 76 39.786 -25.020 7.418 1.00 60.77 C ANISOU 2240 CA GLU C 76 7117 9888 6083 2473 -736 61 C ATOM 2241 C GLU C 76 39.453 -23.947 6.389 1.00 79.05 C ANISOU 2241 C GLU C 76 9502 12423 8112 2933 -784 222 C ATOM 2242 O GLU C 76 39.250 -24.240 5.210 1.00 93.54 O ANISOU 2242 O GLU C 76 11205 14576 9760 2905 -872 178 O ATOM 2243 CB GLU C 76 38.518 -25.453 8.152 1.00 63.56 C ANISOU 2243 CB GLU C 76 7079 10701 6369 2445 -762 -25 C ATOM 2244 CG GLU C 76 38.662 -26.734 8.949 1.00 93.80 C ANISOU 2244 CG GLU C 76 10784 14425 10429 1947 -721 -197 C ATOM 2245 CD GLU C 76 37.404 -27.068 9.723 1.00124.05 C ANISOU 2245 CD GLU C 76 14255 18687 14191 1928 -708 -275 C ATOM 2246 OE1 GLU C 76 36.431 -26.291 9.638 1.00139.66 O ANISOU 2246 OE1 GLU C 76 16060 21053 15951 2311 -744 -212 O ATOM 2247 OE2 GLU C 76 37.397 -28.087 10.441 1.00133.28 O ANISOU 2247 OE2 GLU C 76 15324 19790 15528 1538 -654 -398 O ATOM 2248 N ALA C 77 39.401 -22.700 6.848 1.00 69.69 N ANISOU 2248 N ALA C 77 8529 11061 6887 3362 -722 410 N ATOM 2249 CA ALA C 77 39.088 -21.571 5.981 1.00 70.01 C ANISOU 2249 CA ALA C 77 8684 11252 6664 3850 -751 601 C ATOM 2250 C ALA C 77 40.194 -21.331 4.956 1.00 72.17 C ANISOU 2250 C ALA C 77 9306 11179 6937 3813 -706 669 C ATOM 2251 O ALA C 77 39.917 -21.020 3.797 1.00 66.34 O ANISOU 2251 O ALA C 77 8563 10716 5928 4024 -775 753 O ATOM 2252 CB ALA C 77 38.854 -20.317 6.811 1.00 65.79 C ANISOU 2252 CB ALA C 77 8320 10538 6141 4291 -667 773 C ATOM 2253 N VAL C 78 41.444 -21.470 5.388 1.00 69.14 N ANISOU 2253 N VAL C 78 9224 10199 6847 3549 -588 626 N ATOM 2254 CA VAL C 78 42.584 -21.311 4.491 1.00 79.31 C ANISOU 2254 CA VAL C 78 10840 11115 8179 3455 -516 652 C ATOM 2255 C VAL C 78 42.604 -22.398 3.421 1.00 75.43 C ANISOU 2255 C VAL C 78 10145 10920 7594 3115 -615 496 C ATOM 2256 O VAL C 78 42.773 -22.115 2.234 1.00 78.28 O ANISOU 2256 O VAL C 78 10620 11371 7751 3223 -625 564 O ATOM 2257 CB VAL C 78 43.919 -21.342 5.260 1.00 77.08 C ANISOU 2257 CB VAL C 78 10870 10151 8266 3208 -379 582 C ATOM 2258 CG1 VAL C 78 45.085 -21.346 4.288 1.00 87.88 C ANISOU 2258 CG1 VAL C 78 12522 11169 9697 3044 -301 555 C ATOM 2259 CG2 VAL C 78 44.020 -20.156 6.199 1.00 81.83 C ANISOU 2259 CG2 VAL C 78 11709 10427 8954 3556 -263 724 C ATOM 2260 N VAL C 79 42.415 -23.642 3.853 1.00 57.88 N ANISOU 2260 N VAL C 79 7629 8848 5516 2704 -677 285 N ATOM 2261 CA VAL C 79 42.404 -24.786 2.948 1.00 63.72 C ANISOU 2261 CA VAL C 79 8136 9867 6209 2336 -761 96 C ATOM 2262 C VAL C 79 41.322 -24.657 1.875 1.00 72.73 C ANISOU 2262 C VAL C 79 9013 11667 6954 2576 -891 129 C ATOM 2263 O VAL C 79 41.576 -24.907 0.696 1.00 79.98 O ANISOU 2263 O VAL C 79 9941 12721 7725 2484 -928 82 O ATOM 2264 CB VAL C 79 42.202 -26.100 3.728 1.00 52.44 C ANISOU 2264 CB VAL C 79 6414 8509 5003 1891 -792 -123 C ATOM 2265 CG1 VAL C 79 42.005 -27.265 2.776 1.00 63.76 C ANISOU 2265 CG1 VAL C 79 7555 10297 6373 1533 -875 -334 C ATOM 2266 CG2 VAL C 79 43.387 -26.352 4.648 1.00 62.39 C ANISOU 2266 CG2 VAL C 79 7944 9120 6640 1630 -690 -171 C ATOM 2267 N ASP C 80 40.121 -24.255 2.284 1.00 75.68 N ANISOU 2267 N ASP C 80 9145 12459 7152 2891 -963 198 N ATOM 2268 CA ASP C 80 39.020 -24.057 1.345 1.00 77.21 C ANISOU 2268 CA ASP C 80 9064 13309 6961 3178 -1109 225 C ATOM 2269 C ASP C 80 39.341 -22.928 0.374 1.00 81.06 C ANISOU 2269 C ASP C 80 9889 13708 7200 3591 -1098 462 C ATOM 2270 O ASP C 80 38.978 -22.979 -0.801 1.00 89.63 O ANISOU 2270 O ASP C 80 10870 15204 7981 3694 -1207 462 O ATOM 2271 CB ASP C 80 37.717 -23.753 2.090 1.00 71.70 C ANISOU 2271 CB ASP C 80 8054 13028 6159 3463 -1176 246 C ATOM 2272 CG ASP C 80 37.229 -24.926 2.914 1.00 88.39 C ANISOU 2272 CG ASP C 80 9797 15325 8463 3051 -1181 3 C ATOM 2273 OD1 ASP C 80 37.971 -25.924 3.015 1.00108.81 O ANISOU 2273 OD1 ASP C 80 12410 17646 11288 2564 -1129 -155 O ATOM 2274 OD2 ASP C 80 36.107 -24.854 3.458 1.00103.61 O ANISOU 2274 OD2 ASP C 80 11410 17652 10304 3213 -1229 -34 O ATOM 2275 N ARG C 81 40.027 -21.911 0.883 1.00 86.26 N ANISOU 2275 N ARG C 81 10961 13825 7987 3823 -956 660 N ATOM 2276 CA ARG C 81 40.447 -20.772 0.078 1.00 91.92 C ANISOU 2276 CA ARG C 81 12068 14344 8514 4203 -892 905 C ATOM 2277 C ARG C 81 41.476 -21.178 -0.974 1.00 88.35 C ANISOU 2277 C ARG C 81 11831 13679 8058 3910 -838 844 C ATOM 2278 O ARG C 81 41.464 -20.668 -2.096 1.00 84.34 O ANISOU 2278 O ARG C 81 11478 13316 7250 4149 -857 983 O ATOM 2279 CB ARG C 81 41.004 -19.664 0.971 1.00 87.95 C ANISOU 2279 CB ARG C 81 11945 13263 8209 4458 -720 1087 C ATOM 2280 CG ARG C 81 41.529 -18.469 0.205 1.00104.49 C ANISOU 2280 CG ARG C 81 14482 15058 10161 4805 -599 1331 C ATOM 2281 CD ARG C 81 41.567 -17.227 1.073 1.00126.42 C ANISOU 2281 CD ARG C 81 17462 17418 13153 4969 -388 1406 C ATOM 2282 NE ARG C 81 42.509 -16.237 0.561 1.00135.08 N ANISOU 2282 NE ARG C 81 19000 18018 14306 5012 -169 1513 N ATOM 2283 CZ ARG C 81 42.730 -15.055 1.126 1.00142.63 C ANISOU 2283 CZ ARG C 81 20165 18611 15417 5086 32 1556 C ATOM 2284 NH1 ARG C 81 42.069 -14.707 2.221 1.00142.71 N ANISOU 2284 NH1 ARG C 81 20010 18685 15529 5146 35 1520 N ATOM 2285 NH2 ARG C 81 43.611 -14.219 0.593 1.00146.44 N ANISOU 2285 NH2 ARG C 81 21009 18694 15937 5077 229 1623 N ATOM 2286 N ILE C 82 42.365 -22.097 -0.607 1.00 77.68 N ANISOU 2286 N ILE C 82 10493 11984 7037 3398 -769 635 N ATOM 2287 CA ILE C 82 43.348 -22.619 -1.548 1.00 82.03 C ANISOU 2287 CA ILE C 82 11200 12340 7627 3064 -715 524 C ATOM 2288 C ILE C 82 42.620 -23.339 -2.671 1.00 76.56 C ANISOU 2288 C ILE C 82 10173 12294 6622 2976 -880 408 C ATOM 2289 O ILE C 82 42.962 -23.196 -3.846 1.00 85.14 O ANISOU 2289 O ILE C 82 11414 13446 7491 3001 -870 446 O ATOM 2290 CB ILE C 82 44.331 -23.598 -0.873 1.00 76.26 C ANISOU 2290 CB ILE C 82 10478 11168 7330 2527 -640 289 C ATOM 2291 CG1 ILE C 82 45.178 -22.881 0.174 1.00 73.29 C ANISOU 2291 CG1 ILE C 82 10448 10139 7259 2602 -480 377 C ATOM 2292 CG2 ILE C 82 45.221 -24.268 -1.910 1.00 72.29 C ANISOU 2292 CG2 ILE C 82 10057 10546 6862 2159 -602 130 C ATOM 2293 CD1 ILE C 82 46.138 -23.794 0.901 1.00 82.95 C ANISOU 2293 CD1 ILE C 82 11685 10931 8899 2125 -428 154 C ATOM 2294 N GLY C 83 41.600 -24.100 -2.298 1.00 90.41 N ANISOU 2294 N GLY C 83 12193 14722 7437 2474 -731 2298 N ATOM 2295 CA GLY C 83 40.822 -24.845 -3.261 1.00 94.10 C ANISOU 2295 CA GLY C 83 12390 16000 7362 2414 -1019 2117 C ATOM 2296 C GLY C 83 39.876 -25.827 -2.607 1.00 97.73 C ANISOU 2296 C GLY C 83 12304 16849 7979 2234 -1256 1670 C ATOM 2297 O GLY C 83 40.204 -26.457 -1.598 1.00100.16 O ANISOU 2297 O GLY C 83 12501 16777 8779 1928 -1105 1350 O ATOM 2298 N SER C 84 38.692 -25.956 -3.190 1.00105.56 N ANISOU 2298 N SER C 84 12953 18627 8528 2418 -1627 1652 N ATOM 2299 CA SER C 84 37.687 -26.900 -2.722 1.00111.77 C ANISOU 2299 CA SER C 84 13176 19904 9387 2180 -1854 1211 C ATOM 2300 C SER C 84 38.041 -28.292 -3.228 1.00116.41 C ANISOU 2300 C SER C 84 13724 20681 9826 1536 -1791 684 C ATOM 2301 O SER C 84 37.594 -29.305 -2.692 1.00107.18 O ANISOU 2301 O SER C 84 12232 19643 8848 1138 -1825 232 O ATOM 2302 CB SER C 84 36.289 -26.500 -3.190 1.00117.45 C ANISOU 2302 CB SER C 84 13473 21479 9674 2607 -2289 1361 C ATOM 2303 OG SER C 84 36.208 -26.430 -4.602 1.00133.00 O ANISOU 2303 OG SER C 84 15556 24021 10957 2699 -2489 1489 O ATOM 2304 N GLU C 85 38.869 -28.316 -4.267 1.00129.94 N ANISOU 2304 N GLU C 85 15813 22369 11190 1435 -1660 750 N ATOM 2305 CA GLU C 85 39.322 -29.550 -4.881 1.00128.53 C ANISOU 2305 CA GLU C 85 15692 22323 10820 886 -1556 265 C ATOM 2306 C GLU C 85 40.087 -30.416 -3.887 1.00130.75 C ANISOU 2306 C GLU C 85 16039 21938 11701 485 -1239 -98 C ATOM 2307 O GLU C 85 40.583 -29.925 -2.874 1.00126.59 O ANISOU 2307 O GLU C 85 15612 20795 11690 634 -1054 89 O ATOM 2308 CB GLU C 85 40.187 -29.219 -6.091 1.00130.46 C ANISOU 2308 CB GLU C 85 16376 22586 10607 933 -1399 473 C ATOM 2309 CG GLU C 85 39.427 -28.388 -7.107 1.00159.85 C ANISOU 2309 CG GLU C 85 20094 26978 13664 1367 -1729 869 C ATOM 2310 CD GLU C 85 38.351 -29.181 -7.817 1.00177.92 C ANISOU 2310 CD GLU C 85 21988 30193 15419 1174 -2129 493 C ATOM 2311 OE1 GLU C 85 38.578 -30.385 -8.043 1.00189.06 O ANISOU 2311 OE1 GLU C 85 23367 31680 16785 620 -2038 -63 O ATOM 2312 OE2 GLU C 85 37.279 -28.601 -8.131 1.00174.77 O ANISOU 2312 OE2 GLU C 85 21309 30445 14651 1582 -2535 737 O ATOM 2313 N TYR C 86 40.181 -31.706 -4.194 1.00133.84 N ANISOU 2313 N TYR C 86 16405 22453 11997 -10 -1183 -622 N ATOM 2314 CA TYR C 86 40.726 -32.688 -3.268 1.00117.97 C ANISOU 2314 CA TYR C 86 14451 19870 10501 -366 -927 -994 C ATOM 2315 C TYR C 86 42.218 -32.931 -3.458 1.00113.33 C ANISOU 2315 C TYR C 86 14265 18731 10065 -455 -547 -1045 C ATOM 2316 O TYR C 86 42.681 -33.234 -4.558 1.00123.00 O ANISOU 2316 O TYR C 86 15688 20163 10885 -579 -454 -1173 O ATOM 2317 CB TYR C 86 39.957 -34.015 -3.414 1.00130.04 C ANISOU 2317 CB TYR C 86 15768 21762 11878 -868 -1044 -1561 C ATOM 2318 CG TYR C 86 40.533 -35.191 -2.644 1.00138.20 C ANISOU 2318 CG TYR C 86 16971 22188 13350 -1252 -757 -1966 C ATOM 2319 CD1 TYR C 86 41.569 -35.954 -3.171 1.00140.04 C ANISOU 2319 CD1 TYR C 86 17564 22111 13533 -1458 -481 -2242 C ATOM 2320 CD2 TYR C 86 40.020 -35.555 -1.406 1.00133.29 C ANISOU 2320 CD2 TYR C 86 16170 21314 13160 -1381 -749 -2069 C ATOM 2321 CE1 TYR C 86 42.096 -37.025 -2.478 1.00134.39 C ANISOU 2321 CE1 TYR C 86 17042 20817 13203 -1723 -225 -2583 C ATOM 2322 CE2 TYR C 86 40.541 -36.630 -0.704 1.00132.08 C ANISOU 2322 CE2 TYR C 86 16240 20576 13368 -1688 -488 -2392 C ATOM 2323 CZ TYR C 86 41.578 -37.361 -1.246 1.00136.54 C ANISOU 2323 CZ TYR C 86 17178 20814 13887 -1833 -238 -2640 C ATOM 2324 OH TYR C 86 42.100 -38.432 -0.557 1.00142.34 O ANISOU 2324 OH TYR C 86 18171 20945 14968 -2056 16 -2936 O ATOM 2325 N HIS C 87 42.955 -32.787 -2.364 1.00110.70 N ANISOU 2325 N HIS C 87 14021 17741 10300 -379 -331 -958 N ATOM 2326 CA HIS C 87 44.388 -33.019 -2.346 1.00101.25 C ANISOU 2326 CA HIS C 87 13103 16035 9331 -435 21 -1024 C ATOM 2327 C HIS C 87 44.680 -33.759 -1.050 1.00104.04 C ANISOU 2327 C HIS C 87 13433 15858 10240 -558 137 -1257 C ATOM 2328 O HIS C 87 43.804 -33.882 -0.192 1.00 82.72 O ANISOU 2328 O HIS C 87 10538 13163 7728 -583 -27 -1288 O ATOM 2329 CB HIS C 87 45.182 -31.714 -2.452 1.00 88.55 C ANISOU 2329 CB HIS C 87 11657 14204 7785 -130 162 -548 C ATOM 2330 CG HIS C 87 46.627 -31.913 -2.796 1.00 92.96 C ANISOU 2330 CG HIS C 87 12434 14454 8434 -222 527 -632 C ATOM 2331 ND1 HIS C 87 47.649 -31.577 -1.934 1.00 88.92 N ANISOU 2331 ND1 HIS C 87 11958 13408 8419 -154 742 -538 N ATOM 2332 CD2 HIS C 87 47.220 -32.424 -3.901 1.00103.30 C ANISOU 2332 CD2 HIS C 87 13902 15960 9388 -375 719 -828 C ATOM 2333 CE1 HIS C 87 48.809 -31.863 -2.497 1.00 79.95 C ANISOU 2333 CE1 HIS C 87 10945 12182 7251 -253 1051 -665 C ATOM 2334 NE2 HIS C 87 48.577 -32.379 -3.691 1.00109.19 N ANISOU 2334 NE2 HIS C 87 14741 16304 10442 -378 1064 -839 N ATOM 2335 N GLU C 88 45.907 -34.230 -0.889 1.00105.92 N ANISOU 2335 N GLU C 88 13858 15662 10725 -606 424 -1406 N ATOM 2336 CA GLU C 88 46.261 -35.079 0.242 1.00 95.92 C ANISOU 2336 CA GLU C 88 12625 13903 9916 -689 532 -1641 C ATOM 2337 C GLU C 88 46.839 -34.226 1.352 1.00 97.85 C ANISOU 2337 C GLU C 88 12834 13742 10605 -435 570 -1338 C ATOM 2338 O GLU C 88 46.955 -34.650 2.503 1.00 98.55 O ANISOU 2338 O GLU C 88 12922 13459 11063 -427 586 -1424 O ATOM 2339 CB GLU C 88 47.291 -36.131 -0.192 1.00110.98 C ANISOU 2339 CB GLU C 88 14747 15587 11834 -811 808 -1995 C ATOM 2340 CG GLU C 88 47.849 -37.017 0.925 1.00121.17 C ANISOU 2340 CG GLU C 88 16137 16323 13578 -802 940 -2199 C ATOM 2341 CD GLU C 88 49.286 -37.438 0.640 1.00143.69 C ANISOU 2341 CD GLU C 88 19130 18918 16549 -683 1237 -2350 C ATOM 2342 OE1 GLU C 88 49.921 -36.826 -0.250 1.00150.76 O ANISOU 2342 OE1 GLU C 88 20003 20034 17244 -614 1365 -2236 O ATOM 2343 OE2 GLU C 88 49.777 -38.380 1.293 1.00150.34 O ANISOU 2343 OE2 GLU C 88 20104 19351 17666 -641 1357 -2576 O ATOM 2344 N LEU C 89 47.101 -32.973 1.019 1.00 93.71 N ANISOU 2344 N LEU C 89 12303 13297 10006 -237 571 -970 N ATOM 2345 CA LEU C 89 47.711 -32.074 1.968 1.00 82.48 C ANISOU 2345 CA LEU C 89 10875 11491 8972 -46 624 -712 C ATOM 2346 C LEU C 89 46.622 -31.158 2.482 1.00 79.50 C ANISOU 2346 C LEU C 89 10395 11212 8600 132 394 -429 C ATOM 2347 O LEU C 89 46.709 -30.629 3.590 1.00 73.38 O ANISOU 2347 O LEU C 89 9599 10116 8167 263 374 -304 O ATOM 2348 CB LEU C 89 48.844 -31.284 1.310 1.00 81.09 C ANISOU 2348 CB LEU C 89 10807 11251 8754 6 847 -516 C ATOM 2349 CG LEU C 89 50.148 -32.046 1.063 1.00 85.30 C ANISOU 2349 CG LEU C 89 11373 11638 9400 -100 1123 -786 C ATOM 2350 CD1 LEU C 89 51.214 -31.104 0.538 1.00 79.66 C ANISOU 2350 CD1 LEU C 89 10702 10886 8677 -89 1367 -563 C ATOM 2351 CD2 LEU C 89 50.617 -32.746 2.332 1.00 72.45 C ANISOU 2351 CD2 LEU C 89 9677 9625 8227 -66 1126 -998 C ATOM 2352 N SER C 90 45.578 -31.004 1.676 1.00 85.37 N ANISOU 2352 N SER C 90 11062 12435 8941 157 214 -354 N ATOM 2353 CA SER C 90 44.412 -30.228 2.068 1.00 66.07 C ANISOU 2353 CA SER C 90 8463 10182 6459 384 -19 -115 C ATOM 2354 C SER C 90 43.686 -30.948 3.199 1.00 81.29 C ANISOU 2354 C SER C 90 10200 12044 8641 276 -110 -346 C ATOM 2355 O SER C 90 43.333 -30.334 4.207 1.00 78.40 O ANISOU 2355 O SER C 90 9768 11493 8526 468 -161 -190 O ATOM 2356 CB SER C 90 43.476 -30.008 0.879 1.00 70.62 C ANISOU 2356 CB SER C 90 8947 11385 6501 459 -223 -10 C ATOM 2357 OG SER C 90 44.089 -29.199 -0.111 1.00 77.82 O ANISOU 2357 OG SER C 90 10094 12334 7142 600 -124 285 O ATOM 2358 N GLY C 91 43.469 -32.253 3.040 1.00 78.52 N ANISOU 2358 N GLY C 91 9803 11817 8213 -49 -99 -727 N ATOM 2359 CA GLY C 91 42.731 -32.991 4.045 1.00 68.74 C ANISOU 2359 CA GLY C 91 8425 10520 7173 -216 -144 -938 C ATOM 2360 C GLY C 91 43.617 -33.406 5.202 1.00 72.26 C ANISOU 2360 C GLY C 91 9054 10357 8046 -234 34 -1017 C ATOM 2361 O GLY C 91 43.116 -33.777 6.262 1.00 80.69 O ANISOU 2361 O GLY C 91 10068 11277 9313 -299 27 -1094 O ATOM 2362 N ARG C 92 44.932 -33.350 5.002 1.00 73.15 N ANISOU 2362 N ARG C 92 9366 10155 8273 -170 197 -998 N ATOM 2363 CA ARG C 92 45.865 -33.697 6.064 1.00 58.60 C ANISOU 2363 CA ARG C 92 7660 7800 6807 -127 326 -1063 C ATOM 2364 C ARG C 92 45.762 -32.638 7.146 1.00 65.50 C ANISOU 2364 C ARG C 92 8479 8486 7922 107 254 -801 C ATOM 2365 O ARG C 92 45.644 -32.933 8.334 1.00 66.35 O ANISOU 2365 O ARG C 92 8612 8342 8254 120 248 -851 O ATOM 2366 CB ARG C 92 47.304 -33.794 5.551 1.00 59.88 C ANISOU 2366 CB ARG C 92 7952 7770 7028 -87 508 -1113 C ATOM 2367 CG ARG C 92 48.273 -34.303 6.607 1.00 68.63 C ANISOU 2367 CG ARG C 92 9154 8430 8493 -8 602 -1218 C ATOM 2368 CD ARG C 92 49.690 -34.398 6.074 1.00 75.45 C ANISOU 2368 CD ARG C 92 10052 9196 9421 55 786 -1292 C ATOM 2369 NE ARG C 92 49.875 -35.498 5.130 1.00 83.87 N ANISOU 2369 NE ARG C 92 11227 10352 10287 -75 924 -1580 N ATOM 2370 CZ ARG C 92 51.016 -35.727 4.489 1.00 80.87 C ANISOU 2370 CZ ARG C 92 10862 9960 9905 -19 1125 -1697 C ATOM 2371 NH1 ARG C 92 52.051 -34.933 4.713 1.00 76.10 N ANISOU 2371 NH1 ARG C 92 10127 9288 9501 119 1199 -1547 N ATOM 2372 NH2 ARG C 92 51.134 -36.732 3.628 1.00 77.61 N ANISOU 2372 NH2 ARG C 92 10583 9615 9289 -121 1270 -1989 N ATOM 2373 N ALA C 93 45.777 -31.393 6.681 1.00 64.25 N ANISOU 2373 N ALA C 93 8290 8445 7676 292 214 -520 N ATOM 2374 CA ALA C 93 45.697 -30.212 7.526 1.00 56.57 C ANISOU 2374 CA ALA C 93 7323 7275 6897 528 169 -269 C ATOM 2375 C ALA C 93 44.406 -30.172 8.323 1.00 69.73 C ANISOU 2375 C ALA C 93 8843 9076 8576 604 39 -257 C ATOM 2376 O ALA C 93 44.409 -29.820 9.502 1.00 69.39 O ANISOU 2376 O ALA C 93 8833 8763 8767 717 43 -218 O ATOM 2377 CB ALA C 93 45.841 -28.957 6.681 1.00 55.05 C ANISOU 2377 CB ALA C 93 7199 7167 6549 698 179 37 C ATOM 2378 N LYS C 94 43.303 -30.529 7.675 1.00 62.86 N ANISOU 2378 N LYS C 94 7785 8666 7432 531 -70 -312 N ATOM 2379 CA LYS C 94 42.003 -30.506 8.330 1.00 72.66 C ANISOU 2379 CA LYS C 94 8798 10147 8663 583 -174 -322 C ATOM 2380 C LYS C 94 41.895 -31.628 9.355 1.00 75.52 C ANISOU 2380 C LYS C 94 9180 10310 9203 325 -87 -580 C ATOM 2381 O LYS C 94 41.273 -31.463 10.405 1.00 71.44 O ANISOU 2381 O LYS C 94 8580 9752 8813 397 -83 -559 O ATOM 2382 CB LYS C 94 40.886 -30.631 7.294 1.00 59.96 C ANISOU 2382 CB LYS C 94 6914 9177 6691 541 -335 -346 C ATOM 2383 CG LYS C 94 40.629 -29.362 6.500 1.00 62.41 C ANISOU 2383 CG LYS C 94 7193 9734 6787 919 -459 -10 C ATOM 2384 CD LYS C 94 39.413 -29.517 5.605 1.00 78.12 C ANISOU 2384 CD LYS C 94 8843 12447 8390 925 -677 -44 C ATOM 2385 CE LYS C 94 39.028 -28.196 4.968 1.00 77.82 C ANISOU 2385 CE LYS C 94 8792 12648 8129 1417 -822 347 C ATOM 2386 NZ LYS C 94 37.945 -28.360 3.960 1.00 86.37 N ANISOU 2386 NZ LYS C 94 9529 14520 8767 1457 -1083 319 N ATOM 2387 N ASP C 95 42.504 -32.767 9.043 1.00 77.95 N ANISOU 2387 N ASP C 95 9638 10477 9504 44 6 -815 N ATOM 2388 CA ASP C 95 42.557 -33.891 9.970 1.00 70.24 C ANISOU 2388 CA ASP C 95 8797 9208 8684 -180 118 -1027 C ATOM 2389 C ASP C 95 43.406 -33.546 11.189 1.00 71.68 C ANISOU 2389 C ASP C 95 9172 8910 9153 29 175 -918 C ATOM 2390 O ASP C 95 43.020 -33.824 12.325 1.00 64.73 O ANISOU 2390 O ASP C 95 8339 7876 8381 3 216 -942 O ATOM 2391 CB ASP C 95 43.096 -35.143 9.275 1.00 78.29 C ANISOU 2391 CB ASP C 95 10000 10122 9623 -459 220 -1296 C ATOM 2392 CG ASP C 95 42.107 -35.732 8.288 1.00 97.26 C ANISOU 2392 CG ASP C 95 12235 12995 11725 -776 166 -1501 C ATOM 2393 OD1 ASP C 95 40.893 -35.484 8.445 1.00 98.62 O ANISOU 2393 OD1 ASP C 95 12117 13557 11798 -845 65 -1481 O ATOM 2394 OD2 ASP C 95 42.541 -36.443 7.358 1.00102.46 O ANISOU 2394 OD2 ASP C 95 13028 13666 12234 -957 226 -1706 O ATOM 2395 N LEU C 96 44.568 -32.945 10.943 1.00 69.15 N ANISOU 2395 N LEU C 96 8954 8388 8932 209 184 -812 N ATOM 2396 CA LEU C 96 45.470 -32.544 12.018 1.00 56.69 C ANISOU 2396 CA LEU C 96 7514 6422 7603 386 201 -741 C ATOM 2397 C LEU C 96 44.805 -31.512 12.919 1.00 64.82 C ANISOU 2397 C LEU C 96 8480 7451 8697 571 138 -577 C ATOM 2398 O LEU C 96 44.940 -31.561 14.142 1.00 60.16 O ANISOU 2398 O LEU C 96 7997 6620 8242 634 147 -593 O ATOM 2399 CB LEU C 96 46.770 -31.978 11.443 1.00 56.67 C ANISOU 2399 CB LEU C 96 7552 6301 7680 482 232 -679 C ATOM 2400 CG LEU C 96 47.686 -32.970 10.726 1.00 72.11 C ANISOU 2400 CG LEU C 96 9577 8206 9615 372 333 -864 C ATOM 2401 CD1 LEU C 96 48.776 -32.243 9.958 1.00 68.27 C ANISOU 2401 CD1 LEU C 96 9049 7733 9156 430 401 -785 C ATOM 2402 CD2 LEU C 96 48.291 -33.939 11.715 1.00 57.65 C ANISOU 2402 CD2 LEU C 96 7895 6054 7953 406 362 -1011 C ATOM 2403 N GLY C 97 44.086 -30.579 12.303 1.00 66.17 N ANISOU 2403 N GLY C 97 8500 7898 8745 694 79 -418 N ATOM 2404 CA GLY C 97 43.340 -29.576 13.038 1.00 59.49 C ANISOU 2404 CA GLY C 97 7593 7070 7940 928 41 -272 C ATOM 2405 C GLY C 97 42.237 -30.213 13.858 1.00 69.61 C ANISOU 2405 C GLY C 97 8752 8510 9188 838 65 -384 C ATOM 2406 O GLY C 97 41.987 -29.821 14.998 1.00 74.15 O ANISOU 2406 O GLY C 97 9375 8938 9861 971 98 -359 O ATOM 2407 N SER C 98 41.575 -31.204 13.270 1.00 61.07 N ANISOU 2407 N SER C 98 7518 7735 7950 576 70 -528 N ATOM 2408 CA SER C 98 40.516 -31.937 13.952 1.00 66.99 C ANISOU 2408 CA SER C 98 8133 8661 8657 379 138 -662 C ATOM 2409 C SER C 98 41.080 -32.749 15.116 1.00 74.90 C ANISOU 2409 C SER C 98 9432 9228 9797 248 262 -757 C ATOM 2410 O SER C 98 40.429 -32.904 16.150 1.00 74.65 O ANISOU 2410 O SER C 98 9394 9190 9778 210 355 -777 O ATOM 2411 CB SER C 98 39.783 -32.852 12.967 1.00 58.98 C ANISOU 2411 CB SER C 98 6910 8059 7440 39 120 -840 C ATOM 2412 OG SER C 98 38.631 -33.428 13.557 1.00 74.05 O ANISOU 2412 OG SER C 98 8619 10216 9302 -200 205 -970 O ATOM 2413 N ALA C 99 42.293 -33.265 14.938 1.00 69.90 N ANISOU 2413 N ALA C 99 9058 8256 9244 209 271 -807 N ATOM 2414 CA ALA C 99 42.971 -34.038 15.976 1.00 57.04 C ANISOU 2414 CA ALA C 99 7742 6211 7720 174 351 -866 C ATOM 2415 C ALA C 99 43.327 -33.171 17.180 1.00 74.13 C ANISOU 2415 C ALA C 99 10004 8167 9995 447 312 -745 C ATOM 2416 O ALA C 99 43.241 -33.615 18.325 1.00 66.25 O ANISOU 2416 O ALA C 99 9195 6980 8997 432 380 -760 O ATOM 2417 CB ALA C 99 44.222 -34.698 15.412 1.00 54.83 C ANISOU 2417 CB ALA C 99 7653 5680 7498 161 351 -949 C ATOM 2418 N ALA C 100 43.729 -31.933 16.910 1.00 63.36 N ANISOU 2418 N ALA C 100 8551 6823 8699 676 217 -631 N ATOM 2419 CA ALA C 100 44.099 -30.990 17.959 1.00 52.64 C ANISOU 2419 CA ALA C 100 7301 5260 7438 904 176 -560 C ATOM 2420 C ALA C 100 42.920 -30.701 18.884 1.00 64.39 C ANISOU 2420 C ALA C 100 8738 6872 8855 966 250 -540 C ATOM 2421 O ALA C 100 43.090 -30.557 20.094 1.00 65.30 O ANISOU 2421 O ALA C 100 9033 6795 8984 1057 269 -554 O ATOM 2422 CB ALA C 100 44.623 -29.700 17.350 1.00 52.70 C ANISOU 2422 CB ALA C 100 7255 5242 7526 1072 106 -451 C ATOM 2423 N VAL C 101 41.728 -30.613 18.304 1.00 68.42 N ANISOU 2423 N VAL C 101 8980 7752 9265 925 291 -521 N ATOM 2424 CA VAL C 101 40.517 -30.357 19.073 1.00 72.64 C ANISOU 2424 CA VAL C 101 9372 8500 9728 991 392 -521 C ATOM 2425 C VAL C 101 40.213 -31.540 19.986 1.00 72.97 C ANISOU 2425 C VAL C 101 9550 8473 9703 725 543 -625 C ATOM 2426 O VAL C 101 39.785 -31.363 21.128 1.00 74.47 O ANISOU 2426 O VAL C 101 9816 8629 9852 797 654 -627 O ATOM 2427 CB VAL C 101 39.311 -30.085 18.151 1.00 72.36 C ANISOU 2427 CB VAL C 101 8930 8975 9588 1014 377 -494 C ATOM 2428 CG1 VAL C 101 38.050 -29.850 18.970 1.00 53.88 C ANISOU 2428 CG1 VAL C 101 6366 6920 7184 1100 508 -519 C ATOM 2429 CG2 VAL C 101 39.593 -28.894 17.251 1.00 51.48 C ANISOU 2429 CG2 VAL C 101 6234 6358 6969 1322 242 -334 C ATOM 2430 N LEU C 102 40.450 -32.745 19.477 1.00 64.69 N ANISOU 2430 N LEU C 102 8582 7372 8626 418 571 -711 N ATOM 2431 CA LEU C 102 40.218 -33.967 20.241 1.00 75.63 C ANISOU 2431 CA LEU C 102 10193 8604 9940 133 744 -787 C ATOM 2432 C LEU C 102 41.042 -34.018 21.524 1.00 80.91 C ANISOU 2432 C LEU C 102 11257 8865 10620 303 750 -727 C ATOM 2433 O LEU C 102 40.508 -34.285 22.601 1.00 74.82 O ANISOU 2433 O LEU C 102 10625 8060 9744 240 908 -715 O ATOM 2434 CB LEU C 102 40.531 -35.195 19.382 1.00 63.58 C ANISOU 2434 CB LEU C 102 8780 6979 8399 -179 771 -899 C ATOM 2435 CG LEU C 102 40.371 -36.553 20.068 1.00 70.98 C ANISOU 2435 CG LEU C 102 10060 7643 9266 -492 980 -963 C ATOM 2436 CD1 LEU C 102 38.930 -36.777 20.499 1.00 76.81 C ANISOU 2436 CD1 LEU C 102 10593 8700 9892 -802 1193 -1018 C ATOM 2437 CD2 LEU C 102 40.847 -37.683 19.163 1.00 59.81 C ANISOU 2437 CD2 LEU C 102 8835 6033 7858 -735 1005 -1093 C ATOM 2438 N ILE C 103 42.340 -33.752 21.402 1.00 76.42 N ANISOU 2438 N ILE C 103 10847 8034 10154 510 578 -697 N ATOM 2439 CA ILE C 103 43.247 -33.773 22.545 1.00 69.08 C ANISOU 2439 CA ILE C 103 10246 6786 9215 698 513 -660 C ATOM 2440 C ILE C 103 42.828 -32.736 23.586 1.00 72.31 C ANISOU 2440 C ILE C 103 10649 7259 9567 886 527 -629 C ATOM 2441 O ILE C 103 42.931 -32.974 24.789 1.00 78.12 O ANISOU 2441 O ILE C 103 11662 7844 10175 942 569 -612 O ATOM 2442 CB ILE C 103 44.705 -33.520 22.106 1.00 64.28 C ANISOU 2442 CB ILE C 103 9675 6003 8747 876 309 -670 C ATOM 2443 CG1 ILE C 103 45.126 -34.548 21.057 1.00 60.83 C ANISOU 2443 CG1 ILE C 103 9254 5507 8354 730 329 -727 C ATOM 2444 CG2 ILE C 103 45.648 -33.576 23.297 1.00 74.55 C ANISOU 2444 CG2 ILE C 103 11254 7061 10010 1078 193 -656 C ATOM 2445 CD1 ILE C 103 45.007 -35.979 21.530 1.00 57.56 C ANISOU 2445 CD1 ILE C 103 9173 4858 7837 592 465 -742 C ATOM 2446 N ALA C 104 42.340 -31.592 23.115 1.00 64.43 N ANISOU 2446 N ALA C 104 9372 6473 8635 1007 502 -620 N ATOM 2447 CA ALA C 104 41.845 -30.551 24.007 1.00 62.03 C ANISOU 2447 CA ALA C 104 9069 6216 8283 1216 550 -619 C ATOM 2448 C ALA C 104 40.624 -31.043 24.778 1.00 76.77 C ANISOU 2448 C ALA C 104 10914 8275 9981 1094 792 -634 C ATOM 2449 O ALA C 104 40.473 -30.761 25.967 1.00 75.27 O ANISOU 2449 O ALA C 104 10912 8020 9669 1206 878 -653 O ATOM 2450 CB ALA C 104 41.509 -29.294 23.222 1.00 52.89 C ANISOU 2450 CB ALA C 104 7655 5210 7231 1411 500 -583 C ATOM 2451 N ILE C 105 39.755 -31.777 24.090 1.00 68.24 N ANISOU 2451 N ILE C 105 9595 7458 8877 833 916 -648 N ATOM 2452 CA ILE C 105 38.561 -32.341 24.708 1.00 75.85 C ANISOU 2452 CA ILE C 105 10474 8653 9691 617 1187 -683 C ATOM 2453 C ILE C 105 38.947 -33.432 25.702 1.00 79.10 C ANISOU 2453 C ILE C 105 11344 8750 9962 427 1312 -657 C ATOM 2454 O ILE C 105 38.413 -33.489 26.810 1.00 79.04 O ANISOU 2454 O ILE C 105 11475 8770 9786 407 1518 -648 O ATOM 2455 CB ILE C 105 37.592 -32.914 23.655 1.00 71.88 C ANISOU 2455 CB ILE C 105 9572 8542 9195 304 1268 -746 C ATOM 2456 CG1 ILE C 105 37.009 -31.787 22.801 1.00 61.16 C ANISOU 2456 CG1 ILE C 105 7751 7577 7909 567 1151 -736 C ATOM 2457 CG2 ILE C 105 36.475 -33.702 24.324 1.00 67.07 C ANISOU 2457 CG2 ILE C 105 8895 8149 8441 -45 1586 -808 C ATOM 2458 CD1 ILE C 105 36.103 -32.268 21.689 1.00 61.26 C ANISOU 2458 CD1 ILE C 105 7319 8065 7890 294 1157 -813 C ATOM 2459 N ILE C 106 39.878 -34.291 25.296 1.00 80.03 N ANISOU 2459 N ILE C 106 11716 8564 10127 323 1201 -636 N ATOM 2460 CA ILE C 106 40.402 -35.334 26.172 1.00 71.96 C ANISOU 2460 CA ILE C 106 11198 7178 8965 240 1280 -570 C ATOM 2461 C ILE C 106 40.983 -34.702 27.431 1.00 76.94 C ANISOU 2461 C ILE C 106 12103 7659 9472 565 1188 -515 C ATOM 2462 O ILE C 106 40.767 -35.185 28.543 1.00 88.02 O ANISOU 2462 O ILE C 106 13846 8951 10648 520 1353 -448 O ATOM 2463 CB ILE C 106 41.491 -36.176 25.474 1.00 70.97 C ANISOU 2463 CB ILE C 106 11287 6738 8940 227 1129 -563 C ATOM 2464 CG1 ILE C 106 40.917 -36.910 24.260 1.00 71.70 C ANISOU 2464 CG1 ILE C 106 11181 6954 9107 -138 1238 -660 C ATOM 2465 CG2 ILE C 106 42.123 -37.157 26.452 1.00 69.33 C ANISOU 2465 CG2 ILE C 106 11644 6126 8573 277 1174 -456 C ATOM 2466 CD1 ILE C 106 39.779 -37.839 24.588 1.00 82.14 C ANISOU 2466 CD1 ILE C 106 12589 8328 10293 -581 1570 -690 C ATOM 2467 N ASP C 107 41.715 -33.609 27.241 1.00 72.42 N ANISOU 2467 N ASP C 107 11401 7090 9027 861 933 -553 N ATOM 2468 CA ASP C 107 42.294 -32.855 28.345 1.00 73.81 C ANISOU 2468 CA ASP C 107 11792 7162 9090 1138 809 -565 C ATOM 2469 C ASP C 107 41.221 -32.315 29.288 1.00 79.69 C ANISOU 2469 C ASP C 107 12531 8095 9652 1165 1043 -594 C ATOM 2470 O ASP C 107 41.381 -32.349 30.509 1.00 72.87 O ANISOU 2470 O ASP C 107 12004 7139 8546 1260 1078 -581 O ATOM 2471 CB ASP C 107 43.146 -31.704 27.805 1.00 75.90 C ANISOU 2471 CB ASP C 107 11874 7405 9561 1352 542 -638 C ATOM 2472 CG ASP C 107 43.593 -30.749 28.892 1.00105.61 C ANISOU 2472 CG ASP C 107 15815 11096 13214 1576 429 -717 C ATOM 2473 OD1 ASP C 107 44.446 -31.140 29.717 1.00110.38 O ANISOU 2473 OD1 ASP C 107 16716 11555 13667 1660 280 -715 O ATOM 2474 OD2 ASP C 107 43.093 -29.605 28.920 1.00116.52 O ANISOU 2474 OD2 ASP C 107 17057 12570 14646 1687 483 -791 O ATOM 2475 N ALA C 108 40.131 -31.814 28.715 1.00 66.85 N ANISOU 2475 N ALA C 108 10511 6769 8118 1110 1202 -638 N ATOM 2476 CA ALA C 108 39.037 -31.260 29.505 1.00 68.54 C ANISOU 2476 CA ALA C 108 10633 7225 8184 1177 1458 -689 C ATOM 2477 C ALA C 108 38.303 -32.337 30.299 1.00 76.62 C ANISOU 2477 C ALA C 108 11842 8311 8960 888 1782 -637 C ATOM 2478 O ALA C 108 37.881 -32.104 31.432 1.00 70.28 O ANISOU 2478 O ALA C 108 11213 7569 7922 961 1980 -658 O ATOM 2479 CB ALA C 108 38.064 -30.514 28.603 1.00 70.09 C ANISOU 2479 CB ALA C 108 10308 7778 8545 1248 1524 -736 C ATOM 2480 N VAL C 109 38.156 -33.517 29.703 1.00 62.18 N ANISOU 2480 N VAL C 109 10011 6446 7166 537 1865 -580 N ATOM 2481 CA VAL C 109 37.496 -34.635 30.370 1.00 74.48 C ANISOU 2481 CA VAL C 109 11807 7989 8502 178 2211 -518 C ATOM 2482 C VAL C 109 38.329 -35.143 31.544 1.00 82.17 C ANISOU 2482 C VAL C 109 13432 8577 9212 288 2185 -389 C ATOM 2483 O VAL C 109 37.807 -35.379 32.635 1.00 81.24 O ANISOU 2483 O VAL C 109 13575 8489 8804 204 2468 -335 O ATOM 2484 CB VAL C 109 37.227 -35.796 29.391 1.00 79.32 C ANISOU 2484 CB VAL C 109 12336 8574 9229 -260 2301 -518 C ATOM 2485 CG1 VAL C 109 36.734 -37.025 30.140 1.00 82.65 C ANISOU 2485 CG1 VAL C 109 13151 8835 9417 -669 2675 -433 C ATOM 2486 CG2 VAL C 109 36.219 -35.373 28.334 1.00 84.90 C ANISOU 2486 CG2 VAL C 109 12371 9776 10111 -404 2342 -654 C ATOM 2487 N ILE C 110 39.628 -35.301 31.310 1.00 89.29 N ANISOU 2487 N ILE C 110 14575 9158 10191 494 1843 -337 N ATOM 2488 CA ILE C 110 40.559 -35.730 32.348 1.00105.05 C ANISOU 2488 CA ILE C 110 17144 10838 11930 692 1722 -211 C ATOM 2489 C ILE C 110 40.586 -34.728 33.502 1.00110.94 C ANISOU 2489 C ILE C 110 17999 11711 12444 968 1684 -270 C ATOM 2490 O ILE C 110 40.536 -35.113 34.671 1.00119.16 O ANISOU 2490 O ILE C 110 19485 12670 13119 993 1820 -168 O ATOM 2491 CB ILE C 110 41.985 -35.911 31.782 1.00 82.86 C ANISOU 2491 CB ILE C 110 14422 7773 9289 924 1321 -191 C ATOM 2492 CG1 ILE C 110 42.024 -37.092 30.809 1.00 77.46 C ANISOU 2492 CG1 ILE C 110 13782 6888 8761 673 1400 -137 C ATOM 2493 CG2 ILE C 110 42.992 -36.116 32.903 1.00 79.36 C ANISOU 2493 CG2 ILE C 110 14469 7121 8564 1232 1111 -87 C ATOM 2494 CD1 ILE C 110 43.381 -37.328 30.183 1.00 79.86 C ANISOU 2494 CD1 ILE C 110 14129 6975 9238 920 1058 -135 C ATOM 2495 N THR C 111 40.663 -33.444 33.160 1.00 97.12 N ANISOU 2495 N THR C 111 15885 10134 10882 1171 1514 -435 N ATOM 2496 CA THR C 111 40.680 -32.366 34.146 1.00 83.31 C ANISOU 2496 CA THR C 111 14231 8477 8945 1426 1482 -555 C ATOM 2497 C THR C 111 39.460 -32.407 35.065 1.00 84.09 C ANISOU 2497 C THR C 111 14410 8787 8752 1319 1914 -557 C ATOM 2498 O THR C 111 39.590 -32.361 36.288 1.00 97.16 O ANISOU 2498 O THR C 111 16467 10412 10039 1430 1969 -550 O ATOM 2499 CB THR C 111 40.743 -30.982 33.462 1.00 74.87 C ANISOU 2499 CB THR C 111 12766 7511 8172 1614 1320 -732 C ATOM 2500 OG1 THR C 111 42.014 -30.817 32.821 1.00 83.54 O ANISOU 2500 OG1 THR C 111 13838 8419 9485 1710 935 -749 O ATOM 2501 CG2 THR C 111 40.546 -29.867 34.479 1.00 68.82 C ANISOU 2501 CG2 THR C 111 12126 6812 7210 1845 1374 -897 C ATOM 2502 N TRP C 112 38.277 -32.501 34.466 1.00 82.55 N ANISOU 2502 N TRP C 112 13810 8854 8700 1097 2220 -577 N ATOM 2503 CA TRP C 112 37.030 -32.530 35.223 1.00 78.83 C ANISOU 2503 CA TRP C 112 13290 8670 7993 963 2678 -604 C ATOM 2504 C TRP C 112 36.899 -33.798 36.064 1.00 91.11 C ANISOU 2504 C TRP C 112 15340 10080 9198 670 2951 -419 C ATOM 2505 O TRP C 112 36.367 -33.761 37.173 1.00 90.63 O ANISOU 2505 O TRP C 112 15513 10139 8783 658 3261 -414 O ATOM 2506 CB TRP C 112 35.834 -32.397 34.279 1.00 79.03 C ANISOU 2506 CB TRP C 112 12671 9083 8273 781 2902 -682 C ATOM 2507 CG TRP C 112 35.498 -30.973 33.947 1.00 73.53 C ANISOU 2507 CG TRP C 112 11560 8616 7761 1154 2820 -849 C ATOM 2508 CD1 TRP C 112 36.245 -30.108 33.202 1.00 73.31 C ANISOU 2508 CD1 TRP C 112 11423 8434 7996 1439 2448 -898 C ATOM 2509 CD2 TRP C 112 34.326 -30.250 34.344 1.00 80.57 C ANISOU 2509 CD2 TRP C 112 12121 9908 8585 1301 3148 -980 C ATOM 2510 NE1 TRP C 112 35.614 -28.891 33.113 1.00 77.73 N ANISOU 2510 NE1 TRP C 112 11671 9211 8652 1766 2520 -1029 N ATOM 2511 CE2 TRP C 112 34.433 -28.952 33.805 1.00 79.32 C ANISOU 2511 CE2 TRP C 112 11712 9767 8658 1724 2937 -1090 C ATOM 2512 CE3 TRP C 112 33.197 -30.574 35.103 1.00 81.67 C ANISOU 2512 CE3 TRP C 112 12153 10393 8485 1123 3627 -1015 C ATOM 2513 CZ2 TRP C 112 33.455 -27.979 34.001 1.00 92.35 C ANISOU 2513 CZ2 TRP C 112 13029 11745 10314 2042 3169 -1230 C ATOM 2514 CZ3 TRP C 112 32.227 -29.606 35.297 1.00 84.61 C ANISOU 2514 CZ3 TRP C 112 12122 11160 8867 1418 3863 -1177 C ATOM 2515 CH2 TRP C 112 32.362 -28.325 34.748 1.00 91.09 C ANISOU 2515 CH2 TRP C 112 12717 11967 9927 1907 3623 -1282 C ATOM 2516 N CYS C 113 37.387 -34.915 35.532 1.00 93.21 N ANISOU 2516 N CYS C 113 15806 10064 9545 446 2862 -264 N ATOM 2517 CA CYS C 113 37.337 -36.190 36.244 1.00 86.72 C ANISOU 2517 CA CYS C 113 15551 8994 8404 179 3122 -47 C ATOM 2518 C CYS C 113 38.173 -36.153 37.517 1.00 92.07 C ANISOU 2518 C CYS C 113 16857 9461 8666 501 2971 70 C ATOM 2519 O CYS C 113 37.683 -36.473 38.599 1.00106.27 O ANISOU 2519 O CYS C 113 19038 11288 10051 401 3308 174 O ATOM 2520 CB CYS C 113 37.822 -37.329 35.345 1.00 79.92 C ANISOU 2520 CB CYS C 113 14830 7792 7743 -44 3019 73 C ATOM 2521 SG CYS C 113 36.598 -37.956 34.178 1.00131.66 S ANISOU 2521 SG CYS C 113 20876 14566 14582 -646 3363 -25 S ATOM 2522 N ILE C 114 39.434 -35.758 37.377 1.00 82.39 N ANISOU 2522 N ILE C 114 15714 8063 7526 873 2466 43 N ATOM 2523 CA ILE C 114 40.367 -35.715 38.497 1.00 89.73 C ANISOU 2523 CA ILE C 114 17180 8852 8061 1205 2216 126 C ATOM 2524 C ILE C 114 39.863 -34.803 39.615 1.00 97.08 C ANISOU 2524 C ILE C 114 18187 10052 8645 1332 2382 -13 C ATOM 2525 O ILE C 114 39.894 -35.169 40.791 1.00109.47 O ANISOU 2525 O ILE C 114 20299 11584 9710 1390 2504 121 O ATOM 2526 CB ILE C 114 41.763 -35.242 38.035 1.00 87.32 C ANISOU 2526 CB ILE C 114 16761 8442 7974 1549 1631 36 C ATOM 2527 CG1 ILE C 114 42.391 -36.275 37.097 1.00 95.04 C ANISOU 2527 CG1 ILE C 114 17773 9131 9208 1493 1482 187 C ATOM 2528 CG2 ILE C 114 42.669 -34.968 39.229 1.00 80.07 C ANISOU 2528 CG2 ILE C 114 16274 7518 6633 1897 1325 42 C ATOM 2529 CD1 ILE C 114 43.776 -35.904 36.616 1.00 89.11 C ANISOU 2529 CD1 ILE C 114 16863 8322 8674 1813 951 100 C ATOM 2530 N LEU C 115 39.386 -33.620 39.240 1.00 96.61 N ANISOU 2530 N LEU C 115 17622 10251 8834 1397 2402 -276 N ATOM 2531 CA LEU C 115 38.919 -32.640 40.213 1.00 95.40 C ANISOU 2531 CA LEU C 115 17522 10332 8395 1564 2566 -466 C ATOM 2532 C LEU C 115 37.634 -33.087 40.914 1.00102.00 C ANISOU 2532 C LEU C 115 18461 11379 8916 1308 3173 -391 C ATOM 2533 O LEU C 115 37.519 -32.991 42.135 1.00107.95 O ANISOU 2533 O LEU C 115 19635 12205 9175 1398 3344 -392 O ATOM 2534 CB LEU C 115 38.701 -31.291 39.526 1.00 93.28 C ANISOU 2534 CB LEU C 115 16712 10218 8511 1732 2465 -748 C ATOM 2535 CG LEU C 115 39.976 -30.596 39.040 1.00 83.73 C ANISOU 2535 CG LEU C 115 15444 8821 7550 1966 1918 -872 C ATOM 2536 CD1 LEU C 115 39.649 -29.302 38.314 1.00 76.51 C ANISOU 2536 CD1 LEU C 115 14068 7992 7010 2104 1896 -1103 C ATOM 2537 CD2 LEU C 115 40.925 -30.337 40.200 1.00 80.25 C ANISOU 2537 CD2 LEU C 115 15491 8304 6697 2179 1636 -951 C ATOM 2538 N LEU C 116 36.672 -33.571 40.135 1.00100.89 N ANISOU 2538 N LEU C 116 17918 11373 9044 966 3504 -346 N ATOM 2539 CA LEU C 116 35.376 -34.001 40.668 1.00110.57 C ANISOU 2539 CA LEU C 116 19112 12866 10033 640 4124 -306 C ATOM 2540 C LEU C 116 35.395 -35.363 41.360 1.00116.65 C ANISOU 2540 C LEU C 116 20523 13392 10406 325 4393 3 C ATOM 2541 O LEU C 116 34.543 -35.625 42.210 1.00130.53 O ANISOU 2541 O LEU C 116 22460 15335 11800 106 4908 53 O ATOM 2542 CB LEU C 116 34.301 -33.994 39.576 1.00118.25 C ANISOU 2542 CB LEU C 116 19347 14153 11428 354 4369 -408 C ATOM 2543 CG LEU C 116 33.642 -32.650 39.226 1.00121.14 C ANISOU 2543 CG LEU C 116 19074 14917 12037 643 4393 -690 C ATOM 2544 CD1 LEU C 116 34.638 -31.548 38.886 1.00124.35 C ANISOU 2544 CD1 LEU C 116 19466 15128 12653 1117 3865 -825 C ATOM 2545 CD2 LEU C 116 32.638 -32.832 38.096 1.00125.32 C ANISOU 2545 CD2 LEU C 116 18876 15799 12942 362 4574 -749 C ATOM 2546 N TRP C 117 36.339 -36.234 41.003 1.00113.98 N ANISOU 2546 N TRP C 117 20549 12631 10126 311 4084 218 N ATOM 2547 CA TRP C 117 36.408 -37.549 41.641 1.00115.13 C ANISOU 2547 CA TRP C 117 21402 12453 9891 68 4335 549 C ATOM 2548 C TRP C 117 36.688 -37.377 43.123 1.00130.82 C ANISOU 2548 C TRP C 117 24015 14449 11239 332 4380 651 C ATOM 2549 O TRP C 117 36.323 -38.223 43.939 1.00152.59 O ANISOU 2549 O TRP C 117 27345 17081 13551 103 4783 907 O ATOM 2550 CB TRP C 117 37.517 -38.420 41.045 1.00107.94 C ANISOU 2550 CB TRP C 117 20817 11057 9140 160 3940 751 C ATOM 2551 CG TRP C 117 37.319 -39.898 41.259 1.00110.18 C ANISOU 2551 CG TRP C 117 21718 10939 9207 -205 4297 1080 C ATOM 2552 CD1 TRP C 117 37.542 -40.594 42.412 1.00115.99 C ANISOU 2552 CD1 TRP C 117 23285 11414 9374 -140 4462 1393 C ATOM 2553 CD2 TRP C 117 37.003 -40.879 40.260 1.00131.90 C ANISOU 2553 CD2 TRP C 117 24391 13430 12294 -653 4485 1137 C ATOM 2554 NE1 TRP C 117 37.300 -41.931 42.216 1.00135.65 N ANISOU 2554 NE1 TRP C 117 26238 13464 11838 -540 4801 1659 N ATOM 2555 CE2 TRP C 117 36.981 -42.135 40.900 1.00138.90 C ANISOU 2555 CE2 TRP C 117 26104 13861 12811 -878 4819 1483 C ATOM 2556 CE3 TRP C 117 36.707 -40.814 38.894 1.00131.38 C ANISOU 2556 CE3 TRP C 117 23671 13474 12775 -900 4418 922 C ATOM 2557 CZ2 TRP C 117 36.675 -43.315 40.224 1.00142.87 C ANISOU 2557 CZ2 TRP C 117 26809 13970 13504 -1370 5106 1590 C ATOM 2558 CZ3 TRP C 117 36.404 -41.987 38.224 1.00132.92 C ANISOU 2558 CZ3 TRP C 117 24028 13344 13131 -1389 4675 1008 C ATOM 2559 CH2 TRP C 117 36.390 -43.220 38.889 1.00141.87 C ANISOU 2559 CH2 TRP C 117 26003 13980 13920 -1635 5024 1324 C ATOM 2560 N SER C 118 37.335 -36.270 43.470 1.00122.11 N ANISOU 2560 N SER C 118 22832 13493 10072 790 3975 442 N ATOM 2561 CA SER C 118 37.668 -36.009 44.857 1.00144.71 C ANISOU 2561 CA SER C 118 26269 16415 12298 1063 3947 478 C ATOM 2562 C SER C 118 36.519 -35.310 45.581 1.00138.66 C ANISOU 2562 C SER C 118 25350 16058 11275 966 4469 278 C ATOM 2563 O SER C 118 36.200 -35.662 46.716 1.00143.59 O ANISOU 2563 O SER C 118 26517 16738 11302 905 4817 424 O ATOM 2564 CB SER C 118 38.943 -35.167 44.946 1.00149.55 C ANISOU 2564 CB SER C 118 26890 17006 12925 1550 3264 299 C ATOM 2565 OG SER C 118 38.774 -33.918 44.297 1.00145.55 O ANISOU 2565 OG SER C 118 25731 16711 12860 1649 3133 -72 O ATOM 2566 N HIS C 119 35.902 -34.320 44.935 1.00136.56 N ANISOU 2566 N HIS C 119 24367 16083 11437 987 4538 -46 N ATOM 2567 CA HIS C 119 34.800 -33.589 45.567 1.00143.32 C ANISOU 2567 CA HIS C 119 25011 17354 12090 976 5039 -271 C ATOM 2568 C HIS C 119 33.406 -34.232 45.452 1.00161.72 C ANISOU 2568 C HIS C 119 27050 19946 14449 481 5744 -191 C ATOM 2569 O HIS C 119 32.856 -34.686 46.454 1.00157.67 O ANISOU 2569 O HIS C 119 26940 19545 13421 283 6241 -67 O ATOM 2570 CB HIS C 119 34.746 -32.166 45.012 1.00133.41 C ANISOU 2570 CB HIS C 119 23162 16287 11243 1306 4814 -655 C ATOM 2571 CG HIS C 119 33.709 -31.310 45.664 1.00138.27 C ANISOU 2571 CG HIS C 119 23572 17303 11662 1420 5290 -923 C ATOM 2572 ND1 HIS C 119 33.678 -31.087 47.024 1.00163.18 N ANISOU 2572 ND1 HIS C 119 27264 20559 14179 1556 5506 -989 N ATOM 2573 CD2 HIS C 119 32.685 -30.599 45.143 1.00142.08 C ANISOU 2573 CD2 HIS C 119 23370 18129 12484 1470 5584 -1152 C ATOM 2574 CE1 HIS C 119 32.662 -30.294 47.313 1.00166.77 C ANISOU 2574 CE1 HIS C 119 27374 21386 14603 1668 5954 -1262 C ATOM 2575 NE2 HIS C 119 32.042 -29.981 46.190 1.00161.69 N ANISOU 2575 NE2 HIS C 119 25976 20901 14559 1643 6003 -1359 N ATOM 2576 N PHE C 120 32.837 -34.279 44.248 1.00185.87 N ANISOU 2576 N PHE C 120 29410 23135 18077 257 5795 -268 N ATOM 2577 CA PHE C 120 31.525 -34.909 44.067 1.00200.20 C ANISOU 2577 CA PHE C 120 30857 25263 19948 -275 6431 -234 C ATOM 2578 C PHE C 120 31.680 -36.387 43.742 1.00201.92 C ANISOU 2578 C PHE C 120 31440 25110 20171 -787 6529 91 C ATOM 2579 O PHE C 120 31.681 -37.228 44.640 1.00203.81 O ANISOU 2579 O PHE C 120 32368 25144 19927 -1019 6849 353 O ATOM 2580 CB PHE C 120 30.682 -34.223 42.979 1.00206.79 C ANISOU 2580 CB PHE C 120 30707 26530 21336 -276 6472 -507 C ATOM 2581 CG PHE C 120 30.186 -32.851 43.348 1.00211.52 C ANISOU 2581 CG PHE C 120 30926 27528 21914 185 6571 -823 C ATOM 2582 CD1 PHE C 120 29.085 -32.707 44.185 1.00217.87 C ANISOU 2582 CD1 PHE C 120 31590 28790 22401 83 7213 -934 C ATOM 2583 CD2 PHE C 120 30.776 -31.717 42.826 1.00210.42 C ANISOU 2583 CD2 PHE C 120 30568 27301 22082 706 6071 -1017 C ATOM 2584 CE1 PHE C 120 28.604 -31.457 44.520 1.00222.42 C ANISOU 2584 CE1 PHE C 120 31835 29714 22961 556 7338 -1244 C ATOM 2585 CE2 PHE C 120 30.300 -30.469 43.160 1.00212.92 C ANISOU 2585 CE2 PHE C 120 30607 27907 22385 1145 6197 -1310 C ATOM 2586 CZ PHE C 120 29.213 -30.334 44.007 1.00220.68 C ANISOU 2586 CZ PHE C 120 31463 29335 23049 1102 6824 -1431 C TER 2587 PHE C 120 HETATM 2588 ZN ZN C1121 34.615 -26.841 10.227 0.85175.13 Zn HETATM 2589 ZN ZN C1122 37.642 -29.979 9.958 0.85108.67 Zn END If you find results from this site helpful for your research, please cite one of our papers:
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