HEADER MEMBRANE PROTEIN 13-JUN-18 6DRX TITLE STRUCTURAL DETERMINANTS OF ACTIVATION AND BIASED AGONISM AT THE 5-HT2B TITLE 2 RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: 5HT2B RECEPTOR, BRIL CHIMERA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 5-HT2B,SEROTONIN RECEPTOR 2B,CYTOCHROME B-562; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: HTR2B, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS GPCR, 5HT2B, SETOTONIN RECEPTOR, LISURIDE, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.D.MCCORVY,D.WACKER,S.WANG,B.AGEGNEHU,J.LIU,K.LANSU,A.R.TRIBO, AUTHOR 2 R.H.J.OLSEN,T.CHE,J.JIN,B.L.ROTH REVDAT 4 04-DEC-19 6DRX 1 REMARK REVDAT 3 19-SEP-18 6DRX 1 JRNL REVDAT 2 05-SEP-18 6DRX 1 JRNL REVDAT 1 29-AUG-18 6DRX 0 JRNL AUTH J.D.MCCORVY,D.WACKER,S.WANG,B.AGEGNEHU,J.LIU,K.LANSU, JRNL AUTH 2 A.R.TRIBO,R.H.J.OLSEN,T.CHE,J.JIN,B.L.ROTH JRNL TITL STRUCTURAL DETERMINANTS OF 5-HT2BRECEPTOR ACTIVATION AND JRNL TITL 2 BIASED AGONISM. JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 787 2018 JRNL REFN ESSN 1545-9985 JRNL PMID 30127358 JRNL DOI 10.1038/S41594-018-0116-7 REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.9_1692 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.26 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5 REMARK 3 NUMBER OF REFLECTIONS : 10675 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.245 REMARK 3 R VALUE (WORKING SET) : 0.243 REMARK 3 FREE R VALUE : 0.286 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.640 REMARK 3 FREE R VALUE TEST SET COUNT : 495 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 29.2585 - 4.9109 0.96 2662 127 0.2263 0.2656 REMARK 3 2 4.9109 - 3.9008 0.97 2586 105 0.2356 0.2960 REMARK 3 3 3.9008 - 3.4086 0.98 2571 135 0.2599 0.2833 REMARK 3 4 3.4086 - 3.0973 0.91 2361 128 0.3092 0.3428 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.500 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.990 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.002 2789 REMARK 3 ANGLE : 0.761 3833 REMARK 3 CHIRALITY : 0.022 486 REMARK 3 PLANARITY : 0.004 462 REMARK 3 DIHEDRAL : 9.170 901 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 48 THROUGH 248 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.9820 -14.9377 -1.5081 REMARK 3 T TENSOR REMARK 3 T11: 0.6081 T22: 0.5193 REMARK 3 T33: 0.3824 T12: 0.0602 REMARK 3 T13: -0.0059 T23: 0.0610 REMARK 3 L TENSOR REMARK 3 L11: 3.1608 L22: 2.7138 REMARK 3 L33: 0.8315 L12: -0.2246 REMARK 3 L13: 0.1071 L23: 0.2364 REMARK 3 S TENSOR REMARK 3 S11: 0.0858 S12: 0.0559 S13: -0.0423 REMARK 3 S21: 0.0737 S22: -0.0405 S23: -0.1358 REMARK 3 S31: -0.0359 S32: 0.1253 S33: -0.0176 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): -47.1970 -5.5980 -45.0425 REMARK 3 T TENSOR REMARK 3 T11: 0.7478 T22: 1.7067 REMARK 3 T33: 0.6131 T12: 0.0954 REMARK 3 T13: 0.0068 T23: 0.1286 REMARK 3 L TENSOR REMARK 3 L11: 1.0633 L22: 5.7112 REMARK 3 L33: 6.5565 L12: 1.2811 REMARK 3 L13: -0.8090 L23: -1.1064 REMARK 3 S TENSOR REMARK 3 S11: -0.0408 S12: -0.0297 S13: 0.0599 REMARK 3 S21: -0.1467 S22: 0.0072 S23: 0.0388 REMARK 3 S31: -0.1873 S32: -0.5697 S33: -0.0073 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 314 THROUGH 400 ) REMARK 3 ORIGIN FOR THE GROUP (A): -25.0967 -22.8383 -5.0947 REMARK 3 T TENSOR REMARK 3 T11: 0.7979 T22: 0.5007 REMARK 3 T33: 0.4454 T12: -0.0454 REMARK 3 T13: 0.0142 T23: 0.0885 REMARK 3 L TENSOR REMARK 3 L11: 4.5918 L22: 3.0293 REMARK 3 L33: 4.4399 L12: -0.0797 REMARK 3 L13: -0.0734 L23: 0.4159 REMARK 3 S TENSOR REMARK 3 S11: 0.2565 S12: 0.3544 S13: -0.1119 REMARK 3 S21: -0.1363 S22: -0.0483 S23: 0.1751 REMARK 3 S31: 0.9927 S32: -0.7034 S33: -0.2159 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6DRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-18. REMARK 100 THE DEPOSITION ID IS D_1000235163. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-AUG-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10701 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1 REMARK 200 DATA REDUNDANCY : 4.400 REMARK 200 R MERGE (I) : 0.12200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.17 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1 REMARK 200 DATA REDUNDANCY IN SHELL : 4.30 REMARK 200 R MERGE FOR SHELL (I) : 0.95000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 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: 4IB4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 61.73 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS/HCL PH 7.4-7.7, 30-50 MM REMARK 280 AMMONIUM TARTRATE DIBASIC, 30% V/V PEG400, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.10150 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.10150 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.69000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.27500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.69000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.27500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 84.10150 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.69000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.27500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 84.10150 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.69000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.27500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 THR A 36 REMARK 465 GLU A 37 REMARK 465 SER A 38 REMARK 465 ILE A 39 REMARK 465 PRO A 40 REMARK 465 GLU A 41 REMARK 465 GLU A 42 REMARK 465 MET A 43 REMARK 465 LYS A 44 REMARK 465 GLN A 45 REMARK 465 ILE A 46 REMARK 465 ASP A 198 REMARK 465 VAL A 199 REMARK 465 ASP A 200 REMARK 465 ALA A 1037 REMARK 465 LEU A 1038 REMARK 465 ASP A 1039 REMARK 465 ALA A 1040 REMARK 465 GLN A 1041 REMARK 465 LYS A 1042 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 LYS A 1059 REMARK 465 ASP A 1060 REMARK 465 ALA A 401 REMARK 465 THR A 402 REMARK 465 LYS A 403 REMARK 465 SER A 404 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 GLU A 48 CG CD OE1 OE2 REMARK 470 GLU A 49 CG CD OE1 OE2 REMARK 470 GLN A 50 CG CD OE1 NE2 REMARK 470 LYS A 53 CG CD CE NZ REMARK 470 LEU A 59 CG CD1 CD2 REMARK 470 GLU A 82 CG CD OE1 OE2 REMARK 470 LYS A 84 CE NZ REMARK 470 GLU A 118 CG CD OE1 OE2 REMARK 470 MET A 120 CG SD CE REMARK 470 LEU A 123 CG CD1 CD2 REMARK 470 LEU A 125 CG CD1 CD2 REMARK 470 VAL A 126 CG1 CG2 REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 159 CG CD CE NZ REMARK 470 ILE A 161 CG1 CG2 CD1 REMARK 470 GLN A 162 CG CD OE1 NE2 REMARK 470 ASN A 164 CG OD1 ND2 REMARK 470 GLN A 165 CG CD OE1 NE2 REMARK 470 TYR A 166 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 169 CZ NH1 NH2 REMARK 470 LYS A 175 CG CD CE NZ REMARK 470 LYS A 193 CG CD CE NZ REMARK 470 GLU A 196 CG CD OE1 OE2 REMARK 470 THR A 197 OG1 CG2 REMARK 470 ASN A 201 CG OD1 ND2 REMARK 470 ASN A 203 CG OD1 ND2 REMARK 470 ILE A 205 CG1 CG2 CD1 REMARK 470 VAL A 208 CG1 CG2 REMARK 470 GLU A1004 CG CD OE1 OE2 REMARK 470 GLU A1008 CG CD OE1 OE2 REMARK 470 ASP A1012 CG OD1 OD2 REMARK 470 LYS A1015 CG CD CE NZ REMARK 470 ILE A1017 CG1 CG2 CD1 REMARK 470 GLU A1018 CG CD OE1 OE2 REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 ASP A1021 CG OD1 OD2 REMARK 470 ASN A1022 CG OD1 ND2 REMARK 470 LYS A1027 CG CD CE NZ REMARK 470 ASP A1028 CG OD1 OD2 REMARK 470 LEU A1030 CG CD1 CD2 REMARK 470 ARG A1034 CG CD NE CZ NH1 NH2 REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A1068 CG CD1 CD2 REMARK 470 VAL A1069 CG1 CG2 REMARK 470 ILE A1072 CG1 CG2 CD1 REMARK 470 ASP A1073 CG OD1 OD2 REMARK 470 ASP A1074 CG OD1 OD2 REMARK 470 LEU A1076 CG CD1 CD2 REMARK 470 LYS A1077 CG CD CE NZ REMARK 470 ASN A1080 CG OD1 ND2 REMARK 470 GLU A1081 CG CD OE1 OE2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 VAL A1084 CG1 CG2 REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 GLU A1086 CG CD OE1 OE2 REMARK 470 GLU A1092 CD OE1 OE2 REMARK 470 GLN A1093 CG CD OE1 NE2 REMARK 470 LYS A1095 CG CD CE NZ REMARK 470 ARG A1098 CG CD NE CZ NH1 NH2 REMARK 470 GLN A1103 CG CD OE1 NE2 REMARK 470 LYS A1104 CG CD CE NZ REMARK 470 TYR A1105 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 321 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 324 CD CE NZ REMARK 470 ASP A 351 CG OD1 OD2 REMARK 470 THR A 357 OG1 CG2 REMARK 470 MET A 360 CG SD CE REMARK 470 LYS A 385 CG CD CE NZ REMARK 470 ASN A 398 CG OD1 ND2 REMARK 470 ARG A 400 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 VAL A 64 -63.42 -124.57 REMARK 500 CYS A 207 88.78 -68.23 REMARK 500 ARG A 213 -55.68 -123.31 REMARK 500 PHE A 214 35.64 -93.50 REMARK 500 PHE A 226 -56.19 -122.72 REMARK 500 CYS A 350 99.04 -69.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1203 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue H8G A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1203 DBREF 6DRX A 36 248 UNP P41595 5HT2B_HUMAN 36 248 DBREF 6DRX A 1001 1101 UNP P0ABE7 C562_ECOLX 23 123 DBREF 6DRX A 314 404 UNP P41595 5HT2B_HUMAN 314 404 SEQADV 6DRX TRP A 144 UNP P41595 MET 144 ENGINEERED MUTATION SEQADV 6DRX TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6DRX ILE A 1102 UNP P0ABE7 LINKER SEQADV 6DRX GLN A 1103 UNP P0ABE7 LINKER SEQADV 6DRX LYS A 1104 UNP P0ABE7 LINKER SEQADV 6DRX TYR A 1105 UNP P0ABE7 LINKER SEQADV 6DRX LEU A 1106 UNP P0ABE7 LINKER SEQRES 1 A 410 THR GLU SER ILE PRO GLU GLU MET LYS GLN ILE VAL GLU SEQRES 2 A 410 GLU GLN GLY ASN LYS LEU HIS TRP ALA ALA LEU LEU ILE SEQRES 3 A 410 LEU MET VAL ILE ILE PRO THR ILE GLY GLY ASN THR LEU SEQRES 4 A 410 VAL ILE LEU ALA VAL SER LEU GLU LYS LYS LEU GLN TYR SEQRES 5 A 410 ALA THR ASN TYR PHE LEU MET SER LEU ALA VAL ALA ASP SEQRES 6 A 410 LEU LEU VAL GLY LEU PHE VAL MET PRO ILE ALA LEU LEU SEQRES 7 A 410 THR ILE MET PHE GLU ALA MET TRP PRO LEU PRO LEU VAL SEQRES 8 A 410 LEU CYS PRO ALA TRP LEU PHE LEU ASP VAL LEU PHE SER SEQRES 9 A 410 THR ALA SER ILE TRP HIS LEU CYS ALA ILE SER VAL ASP SEQRES 10 A 410 ARG TYR ILE ALA ILE LYS LYS PRO ILE GLN ALA ASN GLN SEQRES 11 A 410 TYR ASN SER ARG ALA THR ALA PHE ILE LYS ILE THR VAL SEQRES 12 A 410 VAL TRP LEU ILE SER ILE GLY ILE ALA ILE PRO VAL PRO SEQRES 13 A 410 ILE LYS GLY ILE GLU THR ASP VAL ASP ASN PRO ASN ASN SEQRES 14 A 410 ILE THR CYS VAL LEU THR LYS GLU ARG PHE GLY ASP PHE SEQRES 15 A 410 MET LEU PHE GLY SER LEU ALA ALA PHE PHE THR PRO LEU SEQRES 16 A 410 ALA ILE MET ILE VAL THR TYR PHE LEU THR ILE HIS ALA SEQRES 17 A 410 LEU GLN LYS LYS ALA ALA ASP LEU GLU ASP ASN TRP GLU SEQRES 18 A 410 THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP SEQRES 19 A 410 ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG SEQRES 20 A 410 ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS SEQRES 21 A 410 LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP SEQRES 22 A 410 PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP SEQRES 23 A 410 ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU SEQRES 24 A 410 ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN SEQRES 25 A 410 ALA TYR ILE GLN LYS TYR LEU GLN THR ILE SER ASN GLU SEQRES 26 A 410 GLN ARG ALA SER LYS VAL LEU GLY ILE VAL PHE PHE LEU SEQRES 27 A 410 PHE LEU LEU MET TRP CYS PRO PHE PHE ILE THR ASN ILE SEQRES 28 A 410 THR LEU VAL LEU CYS ASP SER CYS ASN GLN THR THR LEU SEQRES 29 A 410 GLN MET LEU LEU GLU ILE PHE VAL TRP ILE GLY TYR VAL SEQRES 30 A 410 SER SER GLY VAL ASN PRO LEU VAL TYR THR LEU PHE ASN SEQRES 31 A 410 LYS THR PHE ARG ASP ALA PHE GLY ARG TYR ILE THR CYS SEQRES 32 A 410 ASN TYR ARG ALA THR LYS SER HET H8G A1201 25 HET CLR A1202 28 HET OLC A1203 19 HETNAM H8G N,N-DIETHYL-N'-[(8ALPHA)-6-METHYL-9,10- HETNAM 2 H8G DIDEHYDROERGOLIN-8-YL]UREA HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN H8G LISURIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 H8G C20 H26 N4 O FORMUL 3 CLR C27 H46 O FORMUL 4 OLC C21 H40 O4 FORMUL 5 HOH *(H2 O) HELIX 1 AA1 LYS A 53 VAL A 64 1 12 HELIX 2 AA2 VAL A 64 GLU A 82 1 19 HELIX 3 AA3 LYS A 83 GLN A 86 5 4 HELIX 4 AA4 TYR A 87 ALA A 88 5 2 HELIX 5 AA5 THR A 89 VAL A 107 1 19 HELIX 6 AA6 VAL A 107 PHE A 117 1 11 HELIX 7 AA7 VAL A 126 LYS A 159 1 34 HELIX 8 AA8 ASN A 164 ILE A 188 1 25 HELIX 9 AA9 ILE A 188 GLY A 194 1 7 HELIX 10 AB1 PHE A 214 PHE A 226 1 13 HELIX 11 AB2 PHE A 226 LEU A 1010 1 33 HELIX 12 AB3 ASN A 1011 LYS A 1019 1 9 HELIX 13 AB4 ASN A 1022 LEU A 1030 1 9 HELIX 14 AB5 THR A 1031 ARG A 1034 5 4 HELIX 15 AB6 PHE A 1061 GLY A 1064 5 4 HELIX 16 AB7 PHE A 1065 GLY A 1082 1 18 HELIX 17 AB8 VAL A 1084 GLU A 1092 1 9 HELIX 18 AB9 LEU A 1094 CYS A 350 1 50 HELIX 19 AC1 GLN A 355 LEU A 382 1 28 HELIX 20 AC2 ASN A 384 THR A 396 1 13 SSBOND 1 CYS A 128 CYS A 207 1555 1555 2.03 SSBOND 2 CYS A 350 CYS A 353 1555 1555 2.03 SITE 1 AC1 13 TRP A 131 LEU A 132 ASP A 135 VAL A 136 SITE 2 AC1 13 SER A 139 THR A 140 VAL A 208 LEU A 209 SITE 3 AC1 13 PHE A 217 ALA A 225 TRP A 337 PHE A 340 SITE 4 AC1 13 VAL A 366 SITE 1 AC2 5 ILE A 66 ILE A 69 THR A 73 TYR A 394 SITE 2 AC2 5 TYR A 399 SITE 1 AC3 7 SER A 150 MET A 233 ILE A 234 TYR A 237 SITE 2 AC3 7 THR A 240 LEU A 326 PHE A 330 CRYST1 59.380 118.550 168.203 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.016841 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008435 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005945 0.00000 ATOM 1 N VAL A 47 -17.172 -41.317 31.978 1.00112.16 N ATOM 2 CA VAL A 47 -17.389 -40.136 31.152 1.00111.93 C ATOM 3 C VAL A 47 -17.114 -40.438 29.679 1.00106.51 C ATOM 4 O VAL A 47 -16.061 -40.968 29.326 1.00112.40 O ATOM 5 CB VAL A 47 -16.506 -38.954 31.617 1.00118.10 C ATOM 6 CG1 VAL A 47 -15.080 -39.416 31.889 1.00118.06 C ATOM 7 CG2 VAL A 47 -16.534 -37.824 30.596 1.00122.39 C ATOM 8 N GLU A 48 -18.077 -40.107 28.824 1.00204.30 N ANISOU 8 N GLU A 48 29173 25604 22848 981 -1408 6822 N ATOM 9 CA GLU A 48 -17.943 -40.344 27.392 1.00188.79 C ANISOU 9 CA GLU A 48 26924 23406 21402 987 -1426 6674 C ATOM 10 C GLU A 48 -17.581 -39.063 26.649 1.00171.27 C ANISOU 10 C GLU A 48 24635 21345 19095 996 -1493 6330 C ATOM 11 O GLU A 48 -18.420 -38.180 26.469 1.00166.39 O ANISOU 11 O GLU A 48 24060 20864 18298 907 -1294 6176 O ATOM 12 CB GLU A 48 -19.237 -40.933 26.825 1.00188.93 C ANISOU 12 CB GLU A 48 26830 23215 21739 870 -1129 6748 C ATOM 13 N GLU A 49 -16.327 -38.968 26.219 1.00162.81 N ANISOU 13 N GLU A 49 23444 20252 18164 1101 -1772 6215 N ATOM 14 CA GLU A 49 -15.855 -37.802 25.481 1.00156.42 C ANISOU 14 CA GLU A 49 22548 19576 17308 1110 -1861 5900 C ATOM 15 C GLU A 49 -15.986 -38.016 23.977 1.00153.54 C ANISOU 15 C GLU A 49 21926 18975 17438 1085 -1813 5762 C ATOM 16 O GLU A 49 -16.071 -39.151 23.508 1.00161.67 O ANISOU 16 O GLU A 49 22818 19723 18888 1096 -1795 5888 O ATOM 17 CB GLU A 49 -14.401 -37.491 25.844 1.00155.68 C ANISOU 17 CB GLU A 49 22450 19607 17096 1229 -2192 5832 C ATOM 18 N GLN A 50 -16.004 -36.919 23.226 1.00141.92 N ANISOU 18 N GLN A 50 20394 17616 15914 1051 -1795 5495 N ATOM 19 CA GLN A 50 -16.135 -36.982 21.774 1.00140.32 C ANISOU 19 CA GLN A 50 19968 17214 16134 1030 -1753 5342 C ATOM 20 C GLN A 50 -14.905 -37.619 21.135 1.00144.31 C ANISOU 20 C GLN A 50 20280 17522 17029 1125 -2008 5305 C ATOM 21 O GLN A 50 -13.802 -37.545 21.678 1.00146.91 O ANISOU 21 O GLN A 50 20633 17941 17247 1204 -2245 5313 O ATOM 22 CB GLN A 50 -16.366 -35.585 21.196 1.00134.18 C ANISOU 22 CB GLN A 50 19189 16617 15176 978 -1667 4997 C ATOM 23 N GLY A 51 -15.102 -38.242 19.977 1.00130.35 N ANISOU 23 N GLY A 51 18314 15483 15728 1123 -1948 5232 N ATOM 24 CA GLY A 51 -14.023 -38.919 19.280 1.00121.70 C ANISOU 24 CA GLY A 51 17018 14173 15050 1215 -2151 5167 C ATOM 25 C GLY A 51 -13.435 -38.101 18.147 1.00111.59 C ANISOU 25 C GLY A 51 15594 12929 13877 1226 -2176 4739 C ATOM 26 O GLY A 51 -13.615 -36.885 18.087 1.00109.90 O ANISOU 26 O GLY A 51 15455 12939 13362 1176 -2103 4516 O ATOM 27 N ASN A 52 -12.729 -38.775 17.245 1.00104.86 N ANISOU 27 N ASN A 52 14529 11850 13463 1295 -2271 4626 N ATOM 28 CA ASN A 52 -12.084 -38.110 16.119 1.00 94.46 C ANISOU 28 CA ASN A 52 13061 10553 12275 1314 -2287 4240 C ATOM 29 C ASN A 52 -13.071 -37.805 14.997 1.00 88.83 C ANISOU 29 C ASN A 52 12295 9799 11658 1240 -2032 3973 C ATOM 30 O ASN A 52 -14.076 -38.497 14.835 1.00 88.24 O ANISOU 30 O ASN A 52 12217 9572 11736 1199 -1877 4066 O ATOM 31 CB ASN A 52 -10.935 -38.970 15.586 1.00 90.15 C ANISOU 31 CB ASN A 52 12303 9789 12160 1422 -2473 4214 C ATOM 32 CG ASN A 52 -9.962 -38.184 14.727 1.00 84.73 C ANISOU 32 CG ASN A 52 11478 9180 11535 1454 -2535 3869 C ATOM 33 OD1 ASN A 52 -10.289 -37.114 14.213 1.00 82.55 O ANISOU 33 OD1 ASN A 52 11235 9065 11064 1389 -2400 3616 O ATOM 34 ND2 ASN A 52 -8.756 -38.716 14.564 1.00 85.12 N ANISOU 34 ND2 ASN A 52 11361 9106 11874 1555 -2735 3866 N ATOM 35 N LYS A 53 -12.776 -36.764 14.224 1.00 84.72 N ANISOU 35 N LYS A 53 11726 9409 11055 1224 -1995 3647 N ATOM 36 CA LYS A 53 -13.624 -36.369 13.106 1.00 79.86 C ANISOU 36 CA LYS A 53 11062 8778 10505 1164 -1779 3382 C ATOM 37 C LYS A 53 -12.782 -36.013 11.885 1.00 76.94 C ANISOU 37 C LYS A 53 10523 8390 10321 1207 -1810 3062 C ATOM 38 O LYS A 53 -13.152 -35.146 11.093 1.00 63.90 O ANISOU 38 O LYS A 53 8866 6837 8575 1160 -1678 2814 O ATOM 39 CB LYS A 53 -14.512 -35.186 13.498 1.00 77.56 C ANISOU 39 CB LYS A 53 10939 8718 9813 1074 -1633 3330 C ATOM 40 N LEU A 54 -11.647 -36.691 11.741 1.00 77.10 N ANISOU 40 N LEU A 54 10403 8282 10611 1298 -1979 3079 N ATOM 41 CA LEU A 54 -10.733 -36.445 10.632 1.00 75.34 C ANISOU 41 CA LEU A 54 10005 8038 10583 1347 -2002 2792 C ATOM 42 C LEU A 54 -11.336 -36.884 9.301 1.00 74.58 C ANISOU 42 C LEU A 54 9797 7800 10739 1340 -1833 2573 C ATOM 43 O LEU A 54 -11.087 -36.270 8.263 1.00 72.73 O ANISOU 43 O LEU A 54 9486 7633 10514 1338 -1754 2295 O ATOM 44 CB LEU A 54 -9.404 -37.168 10.866 1.00 77.60 C ANISOU 44 CB LEU A 54 10151 8203 11131 1454 -2222 2877 C ATOM 45 CG LEU A 54 -8.302 -36.934 9.832 1.00 68.07 C ANISOU 45 CG LEU A 54 8745 6981 10137 1512 -2249 2598 C ATOM 46 CD1 LEU A 54 -7.851 -35.481 9.845 1.00 68.50 C ANISOU 46 CD1 LEU A 54 8844 7284 9899 1467 -2250 2447 C ATOM 47 CD2 LEU A 54 -7.128 -37.867 10.079 1.00 70.68 C ANISOU 47 CD2 LEU A 54 8916 7144 10796 1626 -2457 2702 C ATOM 48 N HIS A 55 -12.130 -37.949 9.341 1.00 76.85 N ANISOU 48 N HIS A 55 10078 7891 11229 1335 -1780 2701 N ATOM 49 CA HIS A 55 -12.745 -38.499 8.139 1.00 75.48 C ANISOU 49 CA HIS A 55 9797 7565 11319 1331 -1646 2492 C ATOM 50 C HIS A 55 -13.711 -37.512 7.492 1.00 73.24 C ANISOU 50 C HIS A 55 9589 7441 10798 1246 -1465 2294 C ATOM 51 O HIS A 55 -13.882 -37.508 6.272 1.00 71.19 O ANISOU 51 O HIS A 55 9237 7149 10665 1253 -1376 2029 O ATOM 52 CB HIS A 55 -13.469 -39.808 8.464 1.00 76.15 C ANISOU 52 CB HIS A 55 9862 7397 11674 1329 -1634 2695 C ATOM 53 CG HIS A 55 -14.435 -39.698 9.601 1.00 73.39 C ANISOU 53 CG HIS A 55 9690 7109 11085 1251 -1580 2985 C ATOM 54 ND1 HIS A 55 -14.034 -39.683 10.920 1.00 73.38 N ANISOU 54 ND1 HIS A 55 9802 7180 10898 1263 -1703 3292 N ATOM 55 CD2 HIS A 55 -15.786 -39.605 9.618 1.00 72.72 C ANISOU 55 CD2 HIS A 55 9684 7031 10915 1161 -1412 3012 C ATOM 56 CE1 HIS A 55 -15.095 -39.581 11.700 1.00 75.14 C ANISOU 56 CE1 HIS A 55 10176 7462 10913 1184 -1595 3496 C ATOM 57 NE2 HIS A 55 -16.171 -39.533 10.936 1.00 72.67 N ANISOU 57 NE2 HIS A 55 9836 7104 10673 1119 -1413 3332 N ATOM 58 N TRP A 56 -14.341 -36.678 8.312 1.00 74.23 N ANISOU 58 N TRP A 56 9884 7742 10578 1172 -1416 2420 N ATOM 59 CA TRP A 56 -15.250 -35.660 7.803 1.00 77.82 C ANISOU 59 CA TRP A 56 10411 8349 10807 1097 -1258 2252 C ATOM 60 C TRP A 56 -14.481 -34.570 7.068 1.00 76.16 C ANISOU 60 C TRP A 56 10165 8303 10470 1111 -1261 2009 C ATOM 61 O TRP A 56 -14.885 -34.136 5.990 1.00 75.86 O ANISOU 61 O TRP A 56 10091 8304 10429 1091 -1150 1783 O ATOM 62 CB TRP A 56 -16.077 -35.052 8.938 1.00 83.53 C ANISOU 62 CB TRP A 56 11316 9212 11209 1021 -1199 2446 C ATOM 63 CG TRP A 56 -17.066 -36.006 9.536 1.00 91.38 C ANISOU 63 CG TRP A 56 12348 10059 12312 987 -1137 2676 C ATOM 64 CD1 TRP A 56 -17.091 -36.465 10.821 1.00 98.56 C ANISOU 64 CD1 TRP A 56 13355 10955 13138 983 -1190 2993 C ATOM 65 CD2 TRP A 56 -18.171 -36.627 8.867 1.00 93.57 C ANISOU 65 CD2 TRP A 56 12561 10182 12811 949 -1008 2612 C ATOM 66 NE1 TRP A 56 -18.147 -37.327 10.996 1.00 97.51 N ANISOU 66 NE1 TRP A 56 13218 10659 13170 941 -1083 3146 N ATOM 67 CE2 TRP A 56 -18.824 -37.445 9.811 1.00 96.20 C ANISOU 67 CE2 TRP A 56 12945 10397 13209 917 -975 2907 C ATOM 68 CE3 TRP A 56 -18.673 -36.568 7.563 1.00 94.49 C ANISOU 68 CE3 TRP A 56 12579 10250 13073 939 -923 2335 C ATOM 69 CZ2 TRP A 56 -19.952 -38.199 9.491 1.00 98.47 C ANISOU 69 CZ2 TRP A 56 13172 10505 13738 869 -857 2927 C ATOM 70 CZ3 TRP A 56 -19.792 -37.317 7.248 1.00 94.90 C ANISOU 70 CZ3 TRP A 56 12577 10135 13346 898 -827 2340 C ATOM 71 CH2 TRP A 56 -20.420 -38.121 8.208 1.00 97.22 C ANISOU 71 CH2 TRP A 56 12907 10297 13736 860 -793 2631 C ATOM 72 N ALA A 57 -13.368 -34.138 7.653 1.00 73.80 N ANISOU 72 N ALA A 57 9871 8097 10072 1144 -1393 2064 N ATOM 73 CA ALA A 57 -12.521 -33.120 7.039 1.00 71.36 C ANISOU 73 CA ALA A 57 9510 7927 9675 1153 -1400 1858 C ATOM 74 C ALA A 57 -11.940 -33.618 5.720 1.00 71.36 C ANISOU 74 C ALA A 57 9333 7823 9959 1215 -1371 1639 C ATOM 75 O ALA A 57 -11.796 -32.852 4.767 1.00 69.42 O ANISOU 75 O ALA A 57 9050 7676 9651 1203 -1281 1426 O ATOM 76 CB ALA A 57 -11.407 -32.712 7.989 1.00 73.42 C ANISOU 76 CB ALA A 57 9787 8279 9828 1179 -1572 1966 C ATOM 77 N ALA A 58 -11.611 -34.905 5.672 1.00 74.30 N ANISOU 77 N ALA A 58 9596 7992 10642 1283 -1443 1695 N ATOM 78 CA ALA A 58 -11.095 -35.521 4.456 1.00 75.29 C ANISOU 78 CA ALA A 58 9548 8001 11058 1351 -1410 1475 C ATOM 79 C ALA A 58 -12.174 -35.562 3.380 1.00 75.16 C ANISOU 79 C ALA A 58 9539 7970 11048 1315 -1249 1286 C ATOM 80 O ALA A 58 -11.904 -35.303 2.207 1.00 75.57 O ANISOU 80 O ALA A 58 9512 8069 11131 1338 -1167 1039 O ATOM 81 CB ALA A 58 -10.580 -36.921 4.745 1.00 78.50 C ANISOU 81 CB ALA A 58 9837 8169 11820 1434 -1530 1586 C ATOM 82 N LEU A 59 -13.396 -35.885 3.791 1.00 75.46 N ANISOU 82 N LEU A 59 9671 7949 11053 1259 -1204 1408 N ATOM 83 CA LEU A 59 -14.530 -35.932 2.876 1.00 74.15 C ANISOU 83 CA LEU A 59 9511 7764 10897 1220 -1074 1244 C ATOM 84 C LEU A 59 -14.862 -34.540 2.350 1.00 72.42 C ANISOU 84 C LEU A 59 9374 7773 10368 1167 -974 1106 C ATOM 85 O LEU A 59 -15.354 -34.389 1.231 1.00 74.35 O ANISOU 85 O LEU A 59 9591 8046 10613 1163 -885 896 O ATOM 86 CB LEU A 59 -15.753 -36.539 3.567 1.00 75.21 C ANISOU 86 CB LEU A 59 9715 7780 11080 1165 -1049 1431 C ATOM 87 N LEU A 60 -14.589 -33.525 3.164 1.00 70.78 N ANISOU 87 N LEU A 60 9267 7724 9901 1130 -998 1224 N ATOM 88 CA LEU A 60 -14.821 -32.142 2.765 1.00 68.30 C ANISOU 88 CA LEU A 60 9026 7609 9315 1081 -913 1114 C ATOM 89 C LEU A 60 -13.817 -31.703 1.706 1.00 72.24 C ANISOU 89 C LEU A 60 9427 8181 9840 1125 -891 909 C ATOM 90 O LEU A 60 -14.179 -31.033 0.744 1.00 71.84 O ANISOU 90 O LEU A 60 9387 8228 9680 1106 -790 750 O ATOM 91 CB LEU A 60 -14.749 -31.212 3.977 1.00 62.59 C ANISOU 91 CB LEU A 60 8430 7019 8335 1032 -953 1279 C ATOM 92 CG LEU A 60 -15.900 -31.321 4.978 1.00 60.48 C ANISOU 92 CG LEU A 60 8288 6739 7954 974 -922 1466 C ATOM 93 CD1 LEU A 60 -15.646 -30.442 6.190 1.00 59.68 C ANISOU 93 CD1 LEU A 60 8307 6780 7587 940 -973 1603 C ATOM 94 CD2 LEU A 60 -17.224 -30.967 4.319 1.00 57.77 C ANISOU 94 CD2 LEU A 60 7980 6419 7550 923 -784 1363 C ATOM 95 N ILE A 61 -12.556 -32.081 1.888 1.00 76.65 N ANISOU 95 N ILE A 61 9884 8692 10546 1185 -984 924 N ATOM 96 CA ILE A 61 -11.518 -31.748 0.919 1.00 77.65 C ANISOU 96 CA ILE A 61 9894 8879 10730 1229 -947 738 C ATOM 97 C ILE A 61 -11.863 -32.307 -0.457 1.00 80.34 C ANISOU 97 C ILE A 61 10161 9171 11192 1266 -844 518 C ATOM 98 O ILE A 61 -11.805 -31.594 -1.458 1.00 85.01 O ANISOU 98 O ILE A 61 10747 9888 11664 1259 -738 356 O ATOM 99 CB ILE A 61 -10.141 -32.285 1.353 1.00 81.30 C ANISOU 99 CB ILE A 61 10228 9263 11399 1299 -1070 787 C ATOM 100 CG1 ILE A 61 -9.678 -31.591 2.635 1.00 83.44 C ANISOU 100 CG1 ILE A 61 10570 9616 11518 1265 -1191 972 C ATOM 101 CG2 ILE A 61 -9.116 -32.084 0.248 1.00 82.29 C ANISOU 101 CG2 ILE A 61 10208 9433 11626 1348 -1000 578 C ATOM 102 CD1 ILE A 61 -8.324 -32.054 3.126 1.00 87.65 C ANISOU 102 CD1 ILE A 61 10971 10080 12252 1334 -1342 1031 C ATOM 103 N LEU A 62 -12.246 -33.578 -0.493 1.00 76.74 N ANISOU 103 N LEU A 62 9653 8532 10972 1304 -878 516 N ATOM 104 CA LEU A 62 -12.550 -34.259 -1.745 1.00 72.31 C ANISOU 104 CA LEU A 62 9014 7906 10557 1347 -805 284 C ATOM 105 C LEU A 62 -13.771 -33.683 -2.458 1.00 68.14 C ANISOU 105 C LEU A 62 8582 7482 9826 1291 -707 182 C ATOM 106 O LEU A 62 -13.774 -33.549 -3.682 1.00 68.34 O ANISOU 106 O LEU A 62 8573 7582 9811 1317 -626 -39 O ATOM 107 CB LEU A 62 -12.772 -35.754 -1.493 1.00 72.64 C ANISOU 107 CB LEU A 62 8976 7697 10926 1392 -879 317 C ATOM 108 CG LEU A 62 -11.613 -36.553 -0.896 1.00 72.80 C ANISOU 108 CG LEU A 62 8877 7570 11215 1467 -992 411 C ATOM 109 CD1 LEU A 62 -12.026 -38.000 -0.682 1.00 73.32 C ANISOU 109 CD1 LEU A 62 8874 7369 11615 1502 -1056 458 C ATOM 110 CD2 LEU A 62 -10.382 -36.470 -1.786 1.00 72.53 C ANISOU 110 CD2 LEU A 62 8701 7586 11271 1543 -951 200 C ATOM 111 N MET A 63 -14.804 -33.339 -1.695 1.00 63.71 N ANISOU 111 N MET A 63 8140 6934 9134 1218 -716 342 N ATOM 112 CA MET A 63 -16.097 -33.012 -2.287 1.00 60.29 C ANISOU 112 CA MET A 63 7776 6554 8578 1171 -646 257 C ATOM 113 C MET A 63 -16.537 -31.559 -2.110 1.00 57.99 C ANISOU 113 C MET A 63 7607 6452 7974 1104 -590 318 C ATOM 114 O MET A 63 -17.587 -31.166 -2.618 1.00 59.54 O ANISOU 114 O MET A 63 7856 6704 8062 1070 -539 253 O ATOM 115 CB MET A 63 -17.172 -33.938 -1.714 1.00 61.65 C ANISOU 115 CB MET A 63 7958 6552 8916 1141 -679 360 C ATOM 116 CG MET A 63 -16.936 -35.409 -2.013 1.00 61.50 C ANISOU 116 CG MET A 63 7809 6312 9245 1202 -731 278 C ATOM 117 SD MET A 63 -18.209 -36.477 -1.319 1.00 94.45 S ANISOU 117 SD MET A 63 11980 10257 13649 1153 -758 424 S ATOM 118 CE MET A 63 -17.645 -38.081 -1.879 1.00144.13 C ANISOU 118 CE MET A 63 18097 16289 20375 1241 -822 276 C ATOM 119 N VAL A 64 -15.751 -30.762 -1.394 1.00 57.82 N ANISOU 119 N VAL A 64 7623 6521 7825 1088 -611 435 N ATOM 120 CA VAL A 64 -16.082 -29.348 -1.227 1.00 54.11 C ANISOU 120 CA VAL A 64 7257 6214 7086 1028 -560 477 C ATOM 121 C VAL A 64 -14.937 -28.448 -1.673 1.00 53.33 C ANISOU 121 C VAL A 64 7126 6242 6896 1042 -532 411 C ATOM 122 O VAL A 64 -15.079 -27.680 -2.621 1.00 52.53 O ANISOU 122 O VAL A 64 7040 6252 6667 1034 -450 303 O ATOM 123 CB VAL A 64 -16.438 -29.005 0.235 1.00 54.46 C ANISOU 123 CB VAL A 64 7401 6261 7030 974 -603 689 C ATOM 124 CG1 VAL A 64 -16.927 -27.568 0.337 1.00 53.52 C ANISOU 124 CG1 VAL A 64 7382 6290 6661 915 -542 699 C ATOM 125 CG2 VAL A 64 -17.481 -29.968 0.772 1.00 57.76 C ANISOU 125 CG2 VAL A 64 7839 6543 7562 956 -614 787 C ATOM 126 N ILE A 65 -13.803 -28.552 -0.986 1.00 56.35 N ANISOU 126 N ILE A 65 7456 6601 7353 1063 -605 487 N ATOM 127 CA ILE A 65 -12.658 -27.686 -1.249 1.00 58.08 C ANISOU 127 CA ILE A 65 7625 6924 7519 1066 -585 443 C ATOM 128 C ILE A 65 -12.111 -27.854 -2.663 1.00 64.44 C ANISOU 128 C ILE A 65 8329 7763 8394 1117 -491 254 C ATOM 129 O ILE A 65 -12.033 -26.888 -3.420 1.00 68.07 O ANISOU 129 O ILE A 65 8806 8349 8709 1095 -394 186 O ATOM 130 CB ILE A 65 -11.524 -27.941 -0.240 1.00 57.32 C ANISOU 130 CB ILE A 65 7466 6778 7535 1087 -707 549 C ATOM 131 CG1 ILE A 65 -12.006 -27.648 1.181 1.00 54.25 C ANISOU 131 CG1 ILE A 65 7198 6395 7020 1037 -796 735 C ATOM 132 CG2 ILE A 65 -10.309 -27.093 -0.577 1.00 56.45 C ANISOU 132 CG2 ILE A 65 7271 6759 7418 1088 -683 487 C ATOM 133 CD1 ILE A 65 -10.923 -27.753 2.224 1.00 54.51 C ANISOU 133 CD1 ILE A 65 7189 6409 7115 1055 -941 845 C ATOM 134 N ILE A 66 -11.734 -29.081 -3.014 1.00 69.20 N ANISOU 134 N ILE A 66 8825 8251 9217 1188 -514 170 N ATOM 135 CA ILE A 66 -11.194 -29.367 -4.343 1.00 72.09 C ANISOU 135 CA ILE A 66 9090 8650 9650 1247 -416 -33 C ATOM 136 C ILE A 66 -12.175 -29.020 -5.478 1.00 71.39 C ANISOU 136 C ILE A 66 9077 8661 9387 1234 -314 -160 C ATOM 137 O ILE A 66 -11.767 -28.411 -6.468 1.00 78.19 O ANISOU 137 O ILE A 66 9920 9652 10135 1244 -203 -265 O ATOM 138 CB ILE A 66 -10.756 -30.849 -4.463 1.00 55.97 C ANISOU 138 CB ILE A 66 6920 6440 7905 1331 -467 -118 C ATOM 139 CG1 ILE A 66 -9.534 -31.115 -3.581 1.00 54.48 C ANISOU 139 CG1 ILE A 66 6626 6174 7899 1362 -566 -14 C ATOM 140 CG2 ILE A 66 -10.441 -31.208 -5.907 1.00 57.79 C ANISOU 140 CG2 ILE A 66 7064 6714 8178 1395 -350 -366 C ATOM 141 CD1 ILE A 66 -9.107 -32.565 -3.552 1.00 55.13 C ANISOU 141 CD1 ILE A 66 6577 6063 8307 1449 -634 -66 C ATOM 142 N PRO A 67 -13.466 -29.388 -5.347 1.00 67.28 N ANISOU 142 N PRO A 67 8637 8084 8844 1210 -350 -143 N ATOM 143 CA PRO A 67 -14.371 -28.944 -6.416 1.00 65.22 C ANISOU 143 CA PRO A 67 8444 7932 8406 1200 -275 -259 C ATOM 144 C PRO A 67 -14.556 -27.426 -6.466 1.00 62.71 C ANISOU 144 C PRO A 67 8222 7773 7834 1140 -217 -174 C ATOM 145 O PRO A 67 -14.842 -26.885 -7.534 1.00 62.73 O ANISOU 145 O PRO A 67 8259 7897 7677 1146 -140 -267 O ATOM 146 CB PRO A 67 -15.694 -29.635 -6.065 1.00 65.77 C ANISOU 146 CB PRO A 67 8558 7885 8545 1179 -343 -236 C ATOM 147 CG PRO A 67 -15.302 -30.809 -5.247 1.00 66.90 C ANISOU 147 CG PRO A 67 8623 7842 8954 1207 -425 -176 C ATOM 148 CD PRO A 67 -14.135 -30.339 -4.439 1.00 67.84 C ANISOU 148 CD PRO A 67 8719 7986 9071 1203 -449 -44 C ATOM 149 N THR A 68 -14.397 -26.753 -5.330 1.00 61.29 N ANISOU 149 N THR A 68 8085 7586 7615 1086 -258 -2 N ATOM 150 CA THR A 68 -14.561 -25.303 -5.274 1.00 60.99 C ANISOU 150 CA THR A 68 8128 7669 7375 1028 -210 75 C ATOM 151 C THR A 68 -13.417 -24.576 -5.973 1.00 63.76 C ANISOU 151 C THR A 68 8421 8126 7679 1037 -121 31 C ATOM 152 O THR A 68 -13.645 -23.751 -6.858 1.00 63.77 O ANISOU 152 O THR A 68 8465 8241 7524 1025 -33 1 O ATOM 153 CB THR A 68 -14.656 -24.796 -3.822 1.00 59.28 C ANISOU 153 CB THR A 68 7971 7418 7135 970 -281 243 C ATOM 154 OG1 THR A 68 -15.856 -25.294 -3.219 1.00 55.39 O ANISOU 154 OG1 THR A 68 7544 6849 6653 951 -328 301 O ATOM 155 CG2 THR A 68 -14.669 -23.275 -3.785 1.00 57.24 C ANISOU 155 CG2 THR A 68 7776 7265 6707 914 -232 298 C ATOM 156 N ILE A 69 -12.188 -24.882 -5.569 1.00 67.99 N ANISOU 156 N ILE A 69 8853 8619 8360 1058 -145 40 N ATOM 157 CA ILE A 69 -11.013 -24.233 -6.139 1.00 66.08 C ANISOU 157 CA ILE A 69 8528 8462 8117 1061 -52 6 C ATOM 158 C ILE A 69 -10.871 -24.556 -7.623 1.00 71.47 C ANISOU 158 C ILE A 69 9169 9225 8762 1117 76 -153 C ATOM 159 O ILE A 69 -10.637 -23.667 -8.441 1.00 76.92 O ANISOU 159 O ILE A 69 9871 10039 9314 1100 196 -162 O ATOM 160 CB ILE A 69 -9.720 -24.650 -5.413 1.00 61.69 C ANISOU 160 CB ILE A 69 7841 7830 7768 1083 -118 32 C ATOM 161 CG1 ILE A 69 -9.903 -24.572 -3.898 1.00 61.81 C ANISOU 161 CG1 ILE A 69 7909 7770 7805 1042 -269 180 C ATOM 162 CG2 ILE A 69 -8.561 -23.771 -5.846 1.00 61.00 C ANISOU 162 CG2 ILE A 69 7661 7826 7692 1064 -20 20 C ATOM 163 CD1 ILE A 69 -8.686 -25.025 -3.121 1.00 63.55 C ANISOU 163 CD1 ILE A 69 8007 7917 8224 1070 -373 217 C ATOM 164 N GLY A 70 -11.020 -25.832 -7.963 1.00 72.08 N ANISOU 164 N GLY A 70 9199 9230 8959 1184 50 -279 N ATOM 165 CA GLY A 70 -10.894 -26.276 -9.338 1.00 73.39 C ANISOU 165 CA GLY A 70 9327 9474 9086 1246 162 -465 C ATOM 166 C GLY A 70 -12.032 -25.805 -10.222 1.00 73.62 C ANISOU 166 C GLY A 70 9482 9619 8873 1234 204 -505 C ATOM 167 O GLY A 70 -11.813 -25.400 -11.365 1.00 74.51 O ANISOU 167 O GLY A 70 9605 9876 8830 1256 328 -586 O ATOM 168 N GLY A 71 -13.250 -25.857 -9.693 1.00 73.01 N ANISOU 168 N GLY A 71 9498 9480 8763 1201 101 -442 N ATOM 169 CA GLY A 71 -14.427 -25.461 -10.444 1.00 73.78 C ANISOU 169 CA GLY A 71 9703 9669 8662 1192 108 -476 C ATOM 170 C GLY A 71 -14.437 -23.987 -10.803 1.00 75.39 C ANISOU 170 C GLY A 71 9983 10015 8648 1147 189 -365 C ATOM 171 O GLY A 71 -14.860 -23.608 -11.895 1.00 76.43 O ANISOU 171 O GLY A 71 10173 10275 8590 1166 245 -420 O ATOM 172 N ASN A 72 -13.967 -23.154 -9.880 1.00 78.29 N ANISOU 172 N ASN A 72 10349 10354 9046 1088 186 -207 N ATOM 173 CA ASN A 72 -13.913 -21.716 -10.108 1.00 76.64 C ANISOU 173 CA ASN A 72 10197 10244 8680 1038 259 -90 C ATOM 174 C ASN A 72 -12.714 -21.319 -10.961 1.00 74.66 C ANISOU 174 C ASN A 72 9877 10099 8392 1053 406 -115 C ATOM 175 O ASN A 72 -12.762 -20.326 -11.687 1.00 77.11 O ANISOU 175 O ASN A 72 10239 10522 8539 1033 499 -52 O ATOM 176 CB ASN A 72 -13.877 -20.967 -8.776 1.00 79.23 C ANISOU 176 CB ASN A 72 10542 10492 9068 968 195 62 C ATOM 177 CG ASN A 72 -15.165 -21.115 -7.993 1.00 82.02 C ANISOU 177 CG ASN A 72 10978 10769 9416 945 88 107 C ATOM 178 OD1 ASN A 72 -16.138 -20.404 -8.239 1.00 84.29 O ANISOU 178 OD1 ASN A 72 11349 11096 9581 923 90 150 O ATOM 179 ND2 ASN A 72 -15.178 -22.041 -7.042 1.00 83.10 N ANISOU 179 ND2 ASN A 72 11084 10792 9696 950 0 108 N ATOM 180 N THR A 73 -11.642 -22.099 -10.870 1.00 71.46 N ANISOU 180 N THR A 73 9349 9652 8152 1090 432 -198 N ATOM 181 CA THR A 73 -10.443 -21.854 -11.662 1.00 69.41 C ANISOU 181 CA THR A 73 8996 9485 7891 1108 590 -237 C ATOM 182 C THR A 73 -10.740 -22.016 -13.150 1.00 69.33 C ANISOU 182 C THR A 73 9035 9629 7678 1163 706 -355 C ATOM 183 O THR A 73 -10.253 -21.246 -13.978 1.00 71.35 O ANISOU 183 O THR A 73 9293 10017 7798 1154 859 -314 O ATOM 184 CB THR A 73 -9.296 -22.803 -11.263 1.00 67.32 C ANISOU 184 CB THR A 73 8571 9131 7878 1150 583 -325 C ATOM 185 OG1 THR A 73 -9.041 -22.684 -9.858 1.00 63.32 O ANISOU 185 OG1 THR A 73 8030 8494 7533 1105 451 -211 O ATOM 186 CG2 THR A 73 -8.027 -22.468 -12.033 1.00 67.06 C ANISOU 186 CG2 THR A 73 8421 9192 7866 1163 767 -361 C ATOM 187 N LEU A 74 -11.550 -23.017 -13.478 1.00 67.88 N ANISOU 187 N LEU A 74 8889 9428 7473 1219 629 -500 N ATOM 188 CA LEU A 74 -11.941 -23.272 -14.859 1.00 70.09 C ANISOU 188 CA LEU A 74 9227 9860 7544 1279 704 -643 C ATOM 189 C LEU A 74 -12.749 -22.112 -15.435 1.00 71.00 C ANISOU 189 C LEU A 74 9482 10107 7389 1245 724 -517 C ATOM 190 O LEU A 74 -12.550 -21.717 -16.584 1.00 75.50 O ANISOU 190 O LEU A 74 10093 10851 7743 1272 853 -537 O ATOM 191 CB LEU A 74 -12.747 -24.569 -14.957 1.00 70.80 C ANISOU 191 CB LEU A 74 9323 9875 7704 1336 582 -830 C ATOM 192 CG LEU A 74 -11.991 -25.864 -14.656 1.00 72.75 C ANISOU 192 CG LEU A 74 9429 9993 8220 1391 568 -986 C ATOM 193 CD1 LEU A 74 -12.928 -27.059 -14.715 1.00 54.86 C ANISOU 193 CD1 LEU A 74 7173 7626 6046 1435 437 -1153 C ATOM 194 CD2 LEU A 74 -10.833 -26.040 -15.625 1.00 56.74 C ANISOU 194 CD2 LEU A 74 7313 8084 6161 1451 751 -1124 C ATOM 195 N VAL A 75 -13.658 -21.571 -14.629 1.00 67.54 N ANISOU 195 N VAL A 75 9115 9584 6963 1189 601 -381 N ATOM 196 CA VAL A 75 -14.502 -20.461 -15.057 1.00 65.16 C ANISOU 196 CA VAL A 75 8935 9374 6450 1160 596 -250 C ATOM 197 C VAL A 75 -13.670 -19.211 -15.332 1.00 68.44 C ANISOU 197 C VAL A 75 9346 9870 6787 1116 745 -86 C ATOM 198 O VAL A 75 -13.873 -18.530 -16.338 1.00 70.50 O ANISOU 198 O VAL A 75 9685 10277 6825 1127 824 -25 O ATOM 199 CB VAL A 75 -15.580 -20.134 -14.005 1.00 57.65 C ANISOU 199 CB VAL A 75 8036 8294 5574 1110 447 -146 C ATOM 200 CG1 VAL A 75 -16.433 -18.959 -14.461 1.00 54.61 C ANISOU 200 CG1 VAL A 75 7760 7989 5002 1088 439 -12 C ATOM 201 CG2 VAL A 75 -16.447 -21.355 -13.740 1.00 54.38 C ANISOU 201 CG2 VAL A 75 7616 7789 5257 1144 313 -289 C ATOM 202 N ILE A 76 -12.731 -18.921 -14.437 1.00 67.93 N ANISOU 202 N ILE A 76 9187 9707 6915 1066 777 -9 N ATOM 203 CA ILE A 76 -11.845 -17.773 -14.598 1.00 68.39 C ANISOU 203 CA ILE A 76 9211 9810 6963 1013 918 139 C ATOM 204 C ILE A 76 -10.973 -17.926 -15.841 1.00 71.41 C ANISOU 204 C ILE A 76 9550 10351 7231 1057 1112 76 C ATOM 205 O ILE A 76 -10.819 -16.985 -16.620 1.00 72.53 O ANISOU 205 O ILE A 76 9737 10608 7214 1037 1243 201 O ATOM 206 CB ILE A 76 -10.945 -17.577 -13.362 1.00 67.74 C ANISOU 206 CB ILE A 76 9014 9587 7138 954 890 194 C ATOM 207 CG1 ILE A 76 -11.797 -17.322 -12.118 1.00 66.22 C ANISOU 207 CG1 ILE A 76 8879 9261 7021 909 717 263 C ATOM 208 CG2 ILE A 76 -9.977 -16.426 -13.582 1.00 67.30 C ANISOU 208 CG2 ILE A 76 8897 9563 7109 894 1039 331 C ATOM 209 CD1 ILE A 76 -10.994 -17.203 -10.842 1.00 65.31 C ANISOU 209 CD1 ILE A 76 8668 9020 7126 859 657 300 C ATOM 210 N LEU A 77 -10.412 -19.118 -16.023 1.00 74.92 N ANISOU 210 N LEU A 77 9906 10799 7762 1119 1139 -114 N ATOM 211 CA LEU A 77 -9.577 -19.409 -17.186 1.00 80.87 C ANISOU 211 CA LEU A 77 10608 11706 8411 1172 1337 -215 C ATOM 212 C LEU A 77 -10.346 -19.247 -18.492 1.00 85.14 C ANISOU 212 C LEU A 77 11294 12443 8611 1219 1388 -239 C ATOM 213 O LEU A 77 -9.814 -18.728 -19.473 1.00 87.39 O ANISOU 213 O LEU A 77 11593 12893 8717 1226 1580 -186 O ATOM 214 CB LEU A 77 -9.006 -20.826 -17.098 1.00 79.98 C ANISOU 214 CB LEU A 77 10375 11539 8476 1243 1328 -446 C ATOM 215 CG LEU A 77 -7.810 -21.040 -16.170 1.00 78.86 C ANISOU 215 CG LEU A 77 10052 11256 8655 1218 1341 -438 C ATOM 216 CD1 LEU A 77 -7.372 -22.496 -16.194 1.00 80.88 C ANISOU 216 CD1 LEU A 77 10195 11451 9086 1304 1322 -671 C ATOM 217 CD2 LEU A 77 -6.661 -20.125 -16.564 1.00 78.58 C ANISOU 217 CD2 LEU A 77 9926 11300 8631 1175 1554 -328 C ATOM 218 N ALA A 78 -11.597 -19.694 -18.498 1.00 88.31 N ANISOU 218 N ALA A 78 11800 12830 8924 1250 1213 -313 N ATOM 219 CA ALA A 78 -12.433 -19.621 -19.691 1.00 85.85 C ANISOU 219 CA ALA A 78 11626 12701 8290 1303 1212 -355 C ATOM 220 C ALA A 78 -12.684 -18.175 -20.102 1.00 84.09 C ANISOU 220 C ALA A 78 11505 12573 7871 1255 1274 -98 C ATOM 221 O ALA A 78 -12.650 -17.841 -21.285 1.00 85.59 O ANISOU 221 O ALA A 78 11776 12965 7779 1292 1390 -70 O ATOM 222 CB ALA A 78 -13.748 -20.344 -19.458 1.00 83.83 C ANISOU 222 CB ALA A 78 11435 12376 8041 1334 987 -477 C ATOM 223 N VAL A 79 -12.935 -17.320 -19.116 1.00 80.82 N ANISOU 223 N VAL A 79 11089 12011 7609 1177 1196 90 N ATOM 224 CA VAL A 79 -13.159 -15.904 -19.375 1.00 78.94 C ANISOU 224 CA VAL A 79 10928 11814 7249 1127 1245 344 C ATOM 225 C VAL A 79 -11.849 -15.211 -19.742 1.00 78.28 C ANISOU 225 C VAL A 79 10772 11792 7180 1087 1483 471 C ATOM 226 O VAL A 79 -11.814 -14.355 -20.625 1.00 82.64 O ANISOU 226 O VAL A 79 11397 12476 7527 1082 1604 635 O ATOM 227 CB VAL A 79 -13.794 -15.202 -18.155 1.00 77.66 C ANISOU 227 CB VAL A 79 10773 11460 7274 1057 1097 479 C ATOM 228 CG1 VAL A 79 -13.999 -13.720 -18.433 1.00 77.50 C ANISOU 228 CG1 VAL A 79 10820 11458 7167 1009 1149 736 C ATOM 229 CG2 VAL A 79 -15.115 -15.862 -17.793 1.00 77.32 C ANISOU 229 CG2 VAL A 79 10789 11355 7232 1091 885 367 C ATOM 230 N SER A 80 -10.770 -15.598 -19.070 1.00 75.68 N ANISOU 230 N SER A 80 10289 11364 7102 1060 1549 402 N ATOM 231 CA SER A 80 -9.469 -14.970 -19.282 1.00 74.48 C ANISOU 231 CA SER A 80 10029 11239 7031 1011 1770 512 C ATOM 232 C SER A 80 -8.845 -15.344 -20.625 1.00 74.71 C ANISOU 232 C SER A 80 10057 11488 6841 1073 1993 436 C ATOM 233 O SER A 80 -8.380 -14.475 -21.362 1.00 76.31 O ANISOU 233 O SER A 80 10276 11802 6916 1044 2187 609 O ATOM 234 CB SER A 80 -8.512 -15.341 -18.147 1.00 73.89 C ANISOU 234 CB SER A 80 9776 10992 7305 972 1748 443 C ATOM 235 OG SER A 80 -9.001 -14.887 -16.898 1.00 71.92 O ANISOU 235 OG SER A 80 9535 10561 7232 910 1564 524 O ATOM 236 N LEU A 81 -8.835 -16.636 -20.938 1.00 75.19 N ANISOU 236 N LEU A 81 10097 11608 6863 1159 1973 175 N ATOM 237 CA LEU A 81 -8.167 -17.124 -22.143 1.00 78.91 C ANISOU 237 CA LEU A 81 10552 12288 7143 1227 2192 50 C ATOM 238 C LEU A 81 -9.021 -16.963 -23.398 1.00 83.22 C ANISOU 238 C LEU A 81 11291 13065 7266 1286 2208 63 C ATOM 239 O LEU A 81 -8.616 -16.294 -24.349 1.00 86.73 O ANISOU 239 O LEU A 81 11783 13690 7481 1283 2418 200 O ATOM 240 CB LEU A 81 -7.773 -18.591 -21.971 1.00 76.57 C ANISOU 240 CB LEU A 81 10144 11946 7004 1301 2163 -258 C ATOM 241 CG LEU A 81 -6.768 -18.882 -20.854 1.00 75.37 C ANISOU 241 CG LEU A 81 9786 11591 7259 1261 2158 -285 C ATOM 242 CD1 LEU A 81 -6.510 -20.375 -20.739 1.00 74.69 C ANISOU 242 CD1 LEU A 81 9601 11449 7328 1347 2107 -580 C ATOM 243 CD2 LEU A 81 -5.468 -18.124 -21.087 1.00 77.83 C ANISOU 243 CD2 LEU A 81 9967 11945 7660 1208 2415 -151 C ATOM 244 N GLU A 82 -10.197 -17.582 -23.401 1.00 83.98 N ANISOU 244 N GLU A 82 11491 13156 7260 1339 1984 -74 N ATOM 245 CA GLU A 82 -11.080 -17.536 -24.562 1.00 87.35 C ANISOU 245 CA GLU A 82 12096 13801 7289 1405 1950 -94 C ATOM 246 C GLU A 82 -11.631 -16.131 -24.786 1.00 89.21 C ANISOU 246 C GLU A 82 12457 14080 7360 1354 1938 232 C ATOM 247 O GLU A 82 -12.397 -15.616 -23.971 1.00 86.15 O ANISOU 247 O GLU A 82 12093 13527 7114 1305 1755 358 O ATOM 248 CB GLU A 82 -12.231 -18.532 -24.400 1.00 85.02 C ANISOU 248 CB GLU A 82 11857 13457 6991 1465 1688 -324 C ATOM 249 N LYS A 83 -11.238 -15.517 -25.899 1.00 94.74 N ANISOU 249 N LYS A 83 13233 15001 7763 1369 2143 370 N ATOM 250 CA LYS A 83 -11.679 -14.166 -26.228 1.00 96.91 C ANISOU 250 CA LYS A 83 13623 15319 7879 1326 2152 705 C ATOM 251 C LYS A 83 -13.122 -14.147 -26.722 1.00 97.58 C ANISOU 251 C LYS A 83 13885 15495 7696 1388 1916 704 C ATOM 252 O LYS A 83 -13.730 -13.084 -26.847 1.00101.92 O ANISOU 252 O LYS A 83 14529 16039 8158 1362 1852 972 O ATOM 253 CB LYS A 83 -10.759 -13.542 -27.279 1.00101.96 C ANISOU 253 CB LYS A 83 14287 16169 8284 1321 2463 878 C ATOM 254 CG LYS A 83 -9.366 -13.216 -26.769 1.00104.31 C ANISOU 254 CG LYS A 83 14395 16352 8884 1238 2701 958 C ATOM 255 CD LYS A 83 -8.538 -12.517 -27.834 1.00109.54 C ANISOU 255 CD LYS A 83 15081 17221 9319 1224 3025 1164 C ATOM 256 CE LYS A 83 -7.172 -12.121 -27.300 1.00111.21 C ANISOU 256 CE LYS A 83 15081 17298 9877 1131 3256 1255 C ATOM 257 NZ LYS A 83 -6.346 -11.446 -28.338 1.00115.67 N ANISOU 257 NZ LYS A 83 15653 18056 10240 1110 3600 1468 N ATOM 258 N LYS A 84 -13.666 -15.327 -27.000 1.00 95.87 N ANISOU 258 N LYS A 84 13698 15350 7377 1471 1777 398 N ATOM 259 CA LYS A 84 -15.049 -15.445 -27.443 1.00 95.90 C ANISOU 259 CA LYS A 84 13845 15433 7162 1533 1527 352 C ATOM 260 C LYS A 84 -16.000 -15.256 -26.263 1.00 92.86 C ANISOU 260 C LYS A 84 13423 14784 7076 1484 1278 400 C ATOM 261 O LYS A 84 -17.202 -15.058 -26.442 1.00 93.34 O ANISOU 261 O LYS A 84 13579 14858 7027 1514 1064 435 O ATOM 262 CB LYS A 84 -15.283 -16.803 -28.113 1.00 97.81 C ANISOU 262 CB LYS A 84 14112 15821 7229 1633 1460 -20 C ATOM 263 CG LYS A 84 -16.569 -16.894 -28.922 1.00 98.37 C ANISOU 263 CG LYS A 84 14342 16050 6985 1709 1233 -77 C ATOM 264 CD LYS A 84 -16.696 -18.245 -29.606 1.00 99.83 C ANISOU 264 CD LYS A 84 14541 16379 7012 1805 1177 -476 C ATOM 265 N LEU A 85 -15.448 -15.310 -25.054 1.00 90.97 N ANISOU 265 N LEU A 85 13040 14310 7212 1411 1308 402 N ATOM 266 CA LEU A 85 -16.236 -15.157 -23.836 1.00 86.48 C ANISOU 266 CA LEU A 85 12431 13496 6933 1360 1105 440 C ATOM 267 C LEU A 85 -15.932 -13.846 -23.119 1.00 86.96 C ANISOU 267 C LEU A 85 12458 13409 7174 1267 1169 734 C ATOM 268 O LEU A 85 -16.463 -13.584 -22.040 1.00 82.97 O ANISOU 268 O LEU A 85 11914 12700 6912 1218 1032 778 O ATOM 269 CB LEU A 85 -15.983 -16.332 -22.891 1.00 82.51 C ANISOU 269 CB LEU A 85 11799 12828 6722 1354 1046 193 C ATOM 270 CG LEU A 85 -16.547 -17.683 -23.325 1.00 82.88 C ANISOU 270 CG LEU A 85 11861 12939 6692 1437 920 -118 C ATOM 271 CD1 LEU A 85 -15.999 -18.796 -22.449 1.00 81.80 C ANISOU 271 CD1 LEU A 85 11582 12635 6865 1429 916 -323 C ATOM 272 CD2 LEU A 85 -18.066 -17.660 -23.277 1.00 83.29 C ANISOU 272 CD2 LEU A 85 11990 12954 6702 1456 668 -125 C ATOM 273 N GLN A 86 -15.078 -13.024 -23.720 1.00 93.04 N ANISOU 273 N GLN A 86 13238 14280 7831 1241 1383 930 N ATOM 274 CA GLN A 86 -14.668 -11.769 -23.099 1.00 96.28 C ANISOU 274 CA GLN A 86 13601 14541 8441 1147 1461 1199 C ATOM 275 C GLN A 86 -15.636 -10.629 -23.404 1.00 93.89 C ANISOU 275 C GLN A 86 13415 14234 8024 1145 1361 1453 C ATOM 276 O GLN A 86 -15.270 -9.651 -24.055 1.00 91.07 O ANISOU 276 O GLN A 86 13103 13951 7547 1123 1504 1704 O ATOM 277 CB GLN A 86 -13.257 -11.385 -23.547 1.00104.78 C ANISOU 277 CB GLN A 86 14608 15696 9508 1108 1750 1307 C ATOM 278 CG GLN A 86 -12.177 -12.351 -23.090 1.00107.84 C ANISOU 278 CG GLN A 86 14844 16043 10089 1100 1854 1085 C ATOM 279 CD GLN A 86 -10.778 -11.850 -23.387 1.00114.36 C ANISOU 279 CD GLN A 86 15566 16909 10977 1048 2140 1207 C ATOM 280 OE1 GLN A 86 -10.589 -10.701 -23.786 1.00121.57 O ANISOU 280 OE1 GLN A 86 16514 17846 11832 999 2262 1480 O ATOM 281 NE2 GLN A 86 -9.787 -12.713 -23.193 1.00114.90 N ANISOU 281 NE2 GLN A 86 15496 16973 11188 1057 2250 1011 N ATOM 282 N TYR A 87 -16.871 -10.760 -22.927 1.00 96.18 N ANISOU 282 N TYR A 87 13744 14429 8372 1167 1120 1394 N ATOM 283 CA TYR A 87 -17.850 -9.686 -23.044 1.00 98.22 C ANISOU 283 CA TYR A 87 14086 14640 8592 1168 1000 1621 C ATOM 284 C TYR A 87 -18.355 -9.266 -21.665 1.00 92.11 C ANISOU 284 C TYR A 87 13238 13597 8161 1106 873 1639 C ATOM 285 O TYR A 87 -18.060 -9.918 -20.663 1.00 86.87 O ANISOU 285 O TYR A 87 12478 12809 7718 1071 854 1467 O ATOM 286 CB TYR A 87 -19.017 -10.101 -23.948 1.00101.78 C ANISOU 286 CB TYR A 87 14660 15256 8755 1267 820 1551 C ATOM 287 CG TYR A 87 -19.601 -11.465 -23.654 1.00 98.98 C ANISOU 287 CG TYR A 87 14276 14896 8435 1313 660 1226 C ATOM 288 CD1 TYR A 87 -19.099 -12.605 -24.269 1.00 98.80 C ANISOU 288 CD1 TYR A 87 14254 15036 8250 1365 725 989 C ATOM 289 CD2 TYR A 87 -20.668 -11.610 -22.776 1.00 96.29 C ANISOU 289 CD2 TYR A 87 13900 14381 8305 1305 453 1156 C ATOM 290 CE1 TYR A 87 -19.633 -13.853 -24.008 1.00101.22 C ANISOU 290 CE1 TYR A 87 14524 15312 8622 1404 576 694 C ATOM 291 CE2 TYR A 87 -21.210 -12.854 -22.510 1.00 95.75 C ANISOU 291 CE2 TYR A 87 13795 14291 8293 1340 316 878 C ATOM 292 CZ TYR A 87 -20.689 -13.972 -23.128 1.00 97.77 C ANISOU 292 CZ TYR A 87 14050 14693 8405 1388 372 650 C ATOM 293 OH TYR A 87 -21.226 -15.211 -22.865 1.00 97.84 O ANISOU 293 OH TYR A 87 14013 14656 8505 1419 234 375 O ATOM 294 N ALA A 88 -19.117 -8.176 -21.629 1.00 92.45 N ANISOU 294 N ALA A 88 13328 13557 8241 1098 788 1850 N ATOM 295 CA ALA A 88 -19.503 -7.517 -20.381 1.00 89.84 C ANISOU 295 CA ALA A 88 12930 12974 8230 1035 707 1898 C ATOM 296 C ALA A 88 -20.232 -8.425 -19.391 1.00 90.08 C ANISOU 296 C ALA A 88 12913 12899 8414 1044 545 1659 C ATOM 297 O ALA A 88 -19.977 -8.367 -18.188 1.00 92.99 O ANISOU 297 O ALA A 88 13198 13094 9039 980 548 1606 O ATOM 298 CB ALA A 88 -20.363 -6.297 -20.690 1.00 92.38 C ANISOU 298 CB ALA A 88 13315 13239 8544 1050 625 2142 C ATOM 299 N THR A 89 -21.136 -9.257 -19.897 1.00 91.57 N ANISOU 299 N THR A 89 13154 13194 8445 1120 403 1519 N ATOM 300 CA THR A 89 -21.975 -10.093 -19.042 1.00 90.14 C ANISOU 300 CA THR A 89 12925 12907 8415 1127 248 1317 C ATOM 301 C THR A 89 -21.158 -11.116 -18.250 1.00 88.53 C ANISOU 301 C THR A 89 12637 12650 8350 1091 313 1125 C ATOM 302 O THR A 89 -21.494 -11.444 -17.111 1.00 89.14 O ANISOU 302 O THR A 89 12654 12575 8639 1058 245 1035 O ATOM 303 CB THR A 89 -23.045 -10.834 -19.870 1.00 93.09 C ANISOU 303 CB THR A 89 13358 13411 8601 1215 82 1193 C ATOM 304 OG1 THR A 89 -23.719 -9.903 -20.725 1.00 96.84 O ANISOU 304 OG1 THR A 89 13917 13960 8917 1260 11 1386 O ATOM 305 CG2 THR A 89 -24.062 -11.507 -18.958 1.00 91.91 C ANISOU 305 CG2 THR A 89 13148 13122 8651 1213 -76 1029 C ATOM 306 N ASN A 90 -20.078 -11.606 -18.850 1.00 88.48 N ANISOU 306 N ASN A 90 12622 12770 8224 1101 451 1069 N ATOM 307 CA ASN A 90 -19.260 -12.639 -18.222 1.00 86.26 C ANISOU 307 CA ASN A 90 12254 12446 8077 1081 506 887 C ATOM 308 C ASN A 90 -18.281 -12.102 -17.181 1.00 89.19 C ANISOU 308 C ASN A 90 12537 12672 8679 997 607 966 C ATOM 309 O ASN A 90 -17.525 -12.869 -16.584 1.00 90.53 O ANISOU 309 O ASN A 90 12624 12793 8978 980 644 840 O ATOM 310 CB ASN A 90 -18.494 -13.423 -19.288 1.00 84.16 C ANISOU 310 CB ASN A 90 11997 12369 7612 1134 616 769 C ATOM 311 CG ASN A 90 -19.361 -14.450 -19.986 1.00 82.92 C ANISOU 311 CG ASN A 90 11891 12321 7296 1217 483 572 C ATOM 312 OD1 ASN A 90 -20.580 -14.471 -19.812 1.00 82.21 O ANISOU 312 OD1 ASN A 90 11831 12177 7226 1234 308 554 O ATOM 313 ND2 ASN A 90 -18.736 -15.311 -20.782 1.00 84.36 N ANISOU 313 ND2 ASN A 90 12071 12650 7332 1268 567 409 N ATOM 314 N TYR A 91 -18.290 -10.791 -16.964 1.00 91.87 N ANISOU 314 N TYR A 91 12888 12936 9084 947 640 1170 N ATOM 315 CA TYR A 91 -17.457 -10.200 -15.924 1.00 94.19 C ANISOU 315 CA TYR A 91 13096 13080 9613 864 708 1229 C ATOM 316 C TYR A 91 -18.144 -10.325 -14.569 1.00 88.23 C ANISOU 316 C TYR A 91 12316 12158 9050 836 571 1154 C ATOM 317 O TYR A 91 -17.511 -10.176 -13.525 1.00 86.66 O ANISOU 317 O TYR A 91 12047 11843 9038 776 589 1136 O ATOM 318 CB TYR A 91 -17.140 -8.739 -16.239 1.00100.05 C ANISOU 318 CB TYR A 91 13850 13790 10376 817 804 1467 C ATOM 319 CG TYR A 91 -16.110 -8.575 -17.333 1.00107.77 C ANISOU 319 CG TYR A 91 14823 14913 11213 819 992 1560 C ATOM 320 CD1 TYR A 91 -14.767 -8.832 -17.091 1.00110.70 C ANISOU 320 CD1 TYR A 91 15086 15276 11699 775 1131 1513 C ATOM 321 CD2 TYR A 91 -16.480 -8.167 -18.607 1.00114.13 C ANISOU 321 CD2 TYR A 91 15728 15868 11767 868 1033 1701 C ATOM 322 CE1 TYR A 91 -13.820 -8.687 -18.088 1.00114.87 C ANISOU 322 CE1 TYR A 91 15597 15940 12110 775 1328 1596 C ATOM 323 CE2 TYR A 91 -15.541 -8.019 -19.611 1.00119.32 C ANISOU 323 CE2 TYR A 91 16389 16674 12274 870 1228 1797 C ATOM 324 CZ TYR A 91 -14.213 -8.279 -19.346 1.00120.47 C ANISOU 324 CZ TYR A 91 16416 16806 12551 821 1387 1741 C ATOM 325 OH TYR A 91 -13.275 -8.132 -20.342 1.00128.18 O ANISOU 325 OH TYR A 91 17382 17932 13387 821 1607 1835 O ATOM 326 N PHE A 92 -19.444 -10.597 -14.596 1.00 84.23 N ANISOU 326 N PHE A 92 11864 11647 8492 880 436 1107 N ATOM 327 CA PHE A 92 -20.172 -10.940 -13.382 1.00 80.68 C ANISOU 327 CA PHE A 92 11391 11064 8200 862 325 1017 C ATOM 328 C PHE A 92 -19.774 -12.339 -12.933 1.00 78.61 C ANISOU 328 C PHE A 92 11080 10805 7983 872 307 838 C ATOM 329 O PHE A 92 -19.584 -12.593 -11.745 1.00 84.33 O ANISOU 329 O PHE A 92 11760 11420 8861 832 281 791 O ATOM 330 CB PHE A 92 -21.684 -10.865 -13.606 1.00 85.58 C ANISOU 330 CB PHE A 92 12063 11677 8776 907 196 1018 C ATOM 331 CG PHE A 92 -22.225 -9.465 -13.654 1.00 91.98 C ANISOU 331 CG PHE A 92 12902 12421 9623 894 185 1189 C ATOM 332 CD1 PHE A 92 -22.259 -8.761 -14.845 1.00 98.02 C ANISOU 332 CD1 PHE A 92 13723 13282 10238 928 211 1337 C ATOM 333 CD2 PHE A 92 -22.710 -8.858 -12.507 1.00 93.73 C ANISOU 333 CD2 PHE A 92 13097 12485 10032 853 150 1203 C ATOM 334 CE1 PHE A 92 -22.760 -7.475 -14.892 1.00100.68 C ANISOU 334 CE1 PHE A 92 14079 13537 10637 921 193 1510 C ATOM 335 CE2 PHE A 92 -23.212 -7.572 -12.547 1.00 98.24 C ANISOU 335 CE2 PHE A 92 13682 12975 10669 847 139 1346 C ATOM 336 CZ PHE A 92 -23.238 -6.881 -13.741 1.00100.07 C ANISOU 336 CZ PHE A 92 13962 13282 10778 881 155 1506 C ATOM 337 N LEU A 93 -19.646 -13.241 -13.901 1.00 73.46 N ANISOU 337 N LEU A 93 10439 10280 7192 930 318 740 N ATOM 338 CA LEU A 93 -19.287 -14.627 -13.627 1.00 67.90 C ANISOU 338 CA LEU A 93 9682 9570 6547 951 299 565 C ATOM 339 C LEU A 93 -17.839 -14.757 -13.171 1.00 61.70 C ANISOU 339 C LEU A 93 8817 8759 5868 915 402 558 C ATOM 340 O LEU A 93 -17.531 -15.564 -12.295 1.00 61.04 O ANISOU 340 O LEU A 93 8675 8590 5926 905 364 470 O ATOM 341 CB LEU A 93 -19.525 -15.494 -14.864 1.00 69.91 C ANISOU 341 CB LEU A 93 9966 9967 6629 1026 284 438 C ATOM 342 CG LEU A 93 -20.983 -15.640 -15.301 1.00 69.44 C ANISOU 342 CG LEU A 93 9965 9932 6488 1069 144 399 C ATOM 343 CD1 LEU A 93 -21.094 -16.544 -16.519 1.00 70.73 C ANISOU 343 CD1 LEU A 93 10154 10244 6477 1145 120 240 C ATOM 344 CD2 LEU A 93 -21.826 -16.170 -14.154 1.00 67.71 C ANISOU 344 CD2 LEU A 93 9707 9556 6464 1045 34 338 C ATOM 345 N MET A 94 -16.953 -13.967 -13.769 1.00 57.76 N ANISOU 345 N MET A 94 8308 8328 5310 897 532 661 N ATOM 346 CA MET A 94 -15.543 -14.001 -13.399 1.00 55.82 C ANISOU 346 CA MET A 94 7964 8056 5188 860 634 658 C ATOM 347 C MET A 94 -15.341 -13.440 -11.997 1.00 56.39 C ANISOU 347 C MET A 94 7995 7973 5458 789 582 714 C ATOM 348 O MET A 94 -14.597 -14.006 -11.197 1.00 60.97 O ANISOU 348 O MET A 94 8495 8489 6180 772 564 646 O ATOM 349 CB MET A 94 -14.695 -13.223 -14.407 1.00 56.59 C ANISOU 349 CB MET A 94 8053 8261 5189 850 802 769 C ATOM 350 CG MET A 94 -13.202 -13.286 -14.120 1.00 56.49 C ANISOU 350 CG MET A 94 7913 8224 5326 814 919 757 C ATOM 351 SD MET A 94 -12.199 -12.503 -15.395 1.00 75.97 S ANISOU 351 SD MET A 94 10354 10828 7683 801 1154 887 S ATOM 352 CE MET A 94 -10.552 -12.785 -14.750 1.00 96.46 C ANISOU 352 CE MET A 94 12761 13351 10538 757 1248 828 C ATOM 353 N SER A 95 -16.009 -12.328 -11.704 1.00 52.25 N ANISOU 353 N SER A 95 7522 7390 4940 752 550 833 N ATOM 354 CA SER A 95 -15.957 -11.730 -10.375 1.00 46.53 C ANISOU 354 CA SER A 95 6773 6526 4380 688 493 863 C ATOM 355 C SER A 95 -16.527 -12.688 -9.335 1.00 43.95 C ANISOU 355 C SER A 95 6453 6135 4112 701 373 753 C ATOM 356 O SER A 95 -15.981 -12.831 -8.241 1.00 43.44 O ANISOU 356 O SER A 95 6341 5994 4169 665 334 724 O ATOM 357 CB SER A 95 -16.722 -10.406 -10.349 1.00 45.24 C ANISOU 357 CB SER A 95 6666 6307 4217 660 482 989 C ATOM 358 OG SER A 95 -16.790 -9.887 -9.033 1.00 44.37 O ANISOU 358 OG SER A 95 6538 6067 4252 606 422 981 O ATOM 359 N LEU A 96 -17.627 -13.343 -9.692 1.00 44.76 N ANISOU 359 N LEU A 96 6610 6269 4128 751 311 699 N ATOM 360 CA LEU A 96 -18.258 -14.331 -8.827 1.00 46.92 C ANISOU 360 CA LEU A 96 6886 6478 4461 763 214 610 C ATOM 361 C LEU A 96 -17.349 -15.535 -8.608 1.00 50.00 C ANISOU 361 C LEU A 96 7208 6868 4921 781 212 516 C ATOM 362 O LEU A 96 -17.244 -16.052 -7.495 1.00 50.86 O ANISOU 362 O LEU A 96 7295 6897 5132 764 151 493 O ATOM 363 CB LEU A 96 -19.591 -14.784 -9.422 1.00 49.04 C ANISOU 363 CB LEU A 96 7207 6778 4649 811 154 566 C ATOM 364 CG LEU A 96 -20.240 -16.016 -8.794 1.00 51.82 C ANISOU 364 CG LEU A 96 7546 7069 5075 827 71 469 C ATOM 365 CD1 LEU A 96 -20.655 -15.738 -7.360 1.00 50.38 C ANISOU 365 CD1 LEU A 96 7373 6781 4989 779 35 511 C ATOM 366 CD2 LEU A 96 -21.427 -16.467 -9.626 1.00 57.94 C ANISOU 366 CD2 LEU A 96 8348 7883 5783 875 12 408 C ATOM 367 N ALA A 97 -16.697 -15.978 -9.678 1.00 53.36 N ANISOU 367 N ALA A 97 7600 7384 5289 822 282 464 N ATOM 368 CA ALA A 97 -15.790 -17.116 -9.606 1.00 54.49 C ANISOU 368 CA ALA A 97 7662 7521 5521 851 290 363 C ATOM 369 C ALA A 97 -14.596 -16.804 -8.713 1.00 57.89 C ANISOU 369 C ALA A 97 8015 7892 6090 805 303 407 C ATOM 370 O ALA A 97 -14.122 -17.669 -7.978 1.00 60.59 O ANISOU 370 O ALA A 97 8298 8168 6553 815 244 356 O ATOM 371 CB ALA A 97 -15.323 -17.516 -10.998 1.00 55.06 C ANISOU 371 CB ALA A 97 7713 7716 5492 907 385 286 C ATOM 372 N VAL A 98 -14.117 -15.566 -8.782 1.00 62.17 N ANISOU 372 N VAL A 98 8549 8448 6626 756 370 504 N ATOM 373 CA VAL A 98 -13.010 -15.117 -7.943 1.00 67.83 C ANISOU 373 CA VAL A 98 9182 9103 7485 704 369 539 C ATOM 374 C VAL A 98 -13.398 -15.153 -6.468 1.00 68.21 C ANISOU 374 C VAL A 98 9260 9053 7603 672 237 546 C ATOM 375 O VAL A 98 -12.636 -15.634 -5.629 1.00 69.19 O ANISOU 375 O VAL A 98 9319 9130 7841 666 173 519 O ATOM 376 CB VAL A 98 -12.558 -13.691 -8.322 1.00 69.47 C ANISOU 376 CB VAL A 98 9376 9325 7695 647 466 645 C ATOM 377 CG1 VAL A 98 -11.689 -13.090 -7.226 1.00 72.94 C ANISOU 377 CG1 VAL A 98 9739 9676 8300 582 421 668 C ATOM 378 CG2 VAL A 98 -11.818 -13.703 -9.652 1.00 69.63 C ANISOU 378 CG2 VAL A 98 9343 9450 7662 672 621 653 C ATOM 379 N ALA A 99 -14.591 -14.650 -6.165 1.00 63.82 N ANISOU 379 N ALA A 99 8802 8475 6974 657 198 583 N ATOM 380 CA ALA A 99 -15.093 -14.616 -4.796 1.00 57.86 C ANISOU 380 CA ALA A 99 8090 7645 6250 628 98 589 C ATOM 381 C ALA A 99 -15.167 -16.017 -4.195 1.00 58.76 C ANISOU 381 C ALA A 99 8195 7731 6401 664 19 538 C ATOM 382 O ALA A 99 -14.709 -16.245 -3.076 1.00 58.66 O ANISOU 382 O ALA A 99 8165 7673 6449 646 -58 545 O ATOM 383 CB ALA A 99 -16.459 -13.949 -4.749 1.00 53.55 C ANISOU 383 CB ALA A 99 7637 7083 5626 619 94 623 C ATOM 384 N ASP A 100 -15.738 -16.950 -4.949 1.00 59.54 N ANISOU 384 N ASP A 100 8302 7852 6467 717 30 489 N ATOM 385 CA ASP A 100 -15.889 -18.325 -4.487 1.00 59.64 C ANISOU 385 CA ASP A 100 8299 7815 6546 752 -38 446 C ATOM 386 C ASP A 100 -14.549 -19.054 -4.458 1.00 63.28 C ANISOU 386 C ASP A 100 8657 8264 7125 778 -51 409 C ATOM 387 O ASP A 100 -14.351 -19.971 -3.659 1.00 69.84 O ANISOU 387 O ASP A 100 9463 9028 8046 794 -132 412 O ATOM 388 CB ASP A 100 -16.884 -19.076 -5.372 1.00 59.49 C ANISOU 388 CB ASP A 100 8304 7810 6488 798 -29 381 C ATOM 389 CG ASP A 100 -18.259 -18.439 -5.367 1.00 59.20 C ANISOU 389 CG ASP A 100 8349 7775 6368 778 -32 416 C ATOM 390 OD1 ASP A 100 -18.595 -17.765 -4.372 1.00 58.25 O ANISOU 390 OD1 ASP A 100 8272 7620 6242 734 -52 482 O ATOM 391 OD2 ASP A 100 -19.004 -18.609 -6.355 1.00 60.25 O ANISOU 391 OD2 ASP A 100 8500 7949 6444 811 -21 367 O ATOM 392 N LEU A 101 -13.634 -18.645 -5.331 1.00 63.44 N ANISOU 392 N LEU A 101 8610 8343 7151 784 35 384 N ATOM 393 CA LEU A 101 -12.287 -19.206 -5.352 1.00 66.10 C ANISOU 393 CA LEU A 101 8825 8668 7622 809 39 342 C ATOM 394 C LEU A 101 -11.555 -18.890 -4.054 1.00 66.79 C ANISOU 394 C LEU A 101 8876 8699 7804 768 -56 401 C ATOM 395 O LEU A 101 -10.853 -19.735 -3.499 1.00 67.53 O ANISOU 395 O LEU A 101 8894 8739 8024 797 -134 387 O ATOM 396 CB LEU A 101 -11.494 -18.666 -6.544 1.00 68.27 C ANISOU 396 CB LEU A 101 9033 9028 7878 814 179 315 C ATOM 397 CG LEU A 101 -10.028 -19.089 -6.642 1.00 69.09 C ANISOU 397 CG LEU A 101 8984 9124 8142 836 212 268 C ATOM 398 CD1 LEU A 101 -9.916 -20.573 -6.950 1.00 71.49 C ANISOU 398 CD1 LEU A 101 9233 9399 8531 917 192 157 C ATOM 399 CD2 LEU A 101 -9.293 -18.262 -7.685 1.00 69.85 C ANISOU 399 CD2 LEU A 101 9022 9309 8210 819 376 276 C ATOM 400 N LEU A 102 -11.732 -17.664 -3.574 1.00 66.52 N ANISOU 400 N LEU A 102 8893 8672 7711 705 -60 462 N ATOM 401 CA LEU A 102 -11.071 -17.209 -2.358 1.00 66.56 C ANISOU 401 CA LEU A 102 8872 8637 7783 661 -160 497 C ATOM 402 C LEU A 102 -11.641 -17.892 -1.119 1.00 66.51 C ANISOU 402 C LEU A 102 8938 8585 7747 670 -290 528 C ATOM 403 O LEU A 102 -10.991 -17.938 -0.075 1.00 68.07 O ANISOU 403 O LEU A 102 9110 8758 7996 657 -403 549 O ATOM 404 CB LEU A 102 -11.189 -15.689 -2.229 1.00 69.22 C ANISOU 404 CB LEU A 102 9244 8983 8073 592 -125 531 C ATOM 405 CG LEU A 102 -10.485 -14.892 -3.330 1.00 74.11 C ANISOU 405 CG LEU A 102 9783 9636 8740 570 6 537 C ATOM 406 CD1 LEU A 102 -10.738 -13.400 -3.176 1.00 71.86 C ANISOU 406 CD1 LEU A 102 9538 9332 8436 501 35 583 C ATOM 407 CD2 LEU A 102 -8.993 -15.190 -3.337 1.00 79.22 C ANISOU 407 CD2 LEU A 102 10271 10274 9556 574 1 506 C ATOM 408 N VAL A 103 -12.855 -18.422 -1.236 1.00 65.43 N ANISOU 408 N VAL A 103 8890 8441 7529 691 -274 535 N ATOM 409 CA VAL A 103 -13.456 -19.179 -0.145 1.00 65.75 C ANISOU 409 CA VAL A 103 8997 8437 7548 700 -368 583 C ATOM 410 C VAL A 103 -12.738 -20.511 0.022 1.00 69.25 C ANISOU 410 C VAL A 103 9359 8827 8125 754 -441 584 C ATOM 411 O VAL A 103 -12.374 -20.899 1.132 1.00 75.33 O ANISOU 411 O VAL A 103 10135 9566 8921 755 -555 646 O ATOM 412 CB VAL A 103 -14.955 -19.445 -0.378 1.00 62.38 C ANISOU 412 CB VAL A 103 8660 8001 7039 705 -320 590 C ATOM 413 CG1 VAL A 103 -15.569 -20.106 0.848 1.00 63.04 C ANISOU 413 CG1 VAL A 103 8811 8040 7099 700 -393 662 C ATOM 414 CG2 VAL A 103 -15.683 -18.158 -0.704 1.00 58.79 C ANISOU 414 CG2 VAL A 103 8268 7588 6480 665 -247 585 C ATOM 415 N GLY A 104 -12.531 -21.206 -1.091 1.00 67.78 N ANISOU 415 N GLY A 104 9098 8632 8023 803 -379 513 N ATOM 416 CA GLY A 104 -11.873 -22.499 -1.071 1.00 64.55 C ANISOU 416 CA GLY A 104 8597 8153 7778 864 -437 495 C ATOM 417 C GLY A 104 -10.383 -22.411 -0.800 1.00 62.86 C ANISOU 417 C GLY A 104 8259 7933 7690 875 -493 491 C ATOM 418 O GLY A 104 -9.742 -23.417 -0.499 1.00 62.77 O ANISOU 418 O GLY A 104 8164 7851 7835 926 -574 497 O ATOM 419 N LEU A 105 -9.832 -21.206 -0.900 1.00 63.22 N ANISOU 419 N LEU A 105 8282 8042 7696 827 -455 482 N ATOM 420 CA LEU A 105 -8.398 -21.003 -0.716 1.00 64.07 C ANISOU 420 CA LEU A 105 8250 8144 7949 828 -501 467 C ATOM 421 C LEU A 105 -8.046 -20.456 0.665 1.00 67.69 C ANISOU 421 C LEU A 105 8736 8597 8386 785 -654 536 C ATOM 422 O LEU A 105 -7.060 -20.877 1.270 1.00 70.86 O ANISOU 422 O LEU A 105 9039 8962 8923 810 -779 551 O ATOM 423 CB LEU A 105 -7.852 -20.061 -1.792 1.00 62.57 C ANISOU 423 CB LEU A 105 7986 8017 7770 800 -351 410 C ATOM 424 CG LEU A 105 -7.674 -20.633 -3.199 1.00 60.93 C ANISOU 424 CG LEU A 105 7706 7837 7608 854 -203 321 C ATOM 425 CD1 LEU A 105 -7.145 -19.565 -4.143 1.00 59.39 C ANISOU 425 CD1 LEU A 105 7454 7717 7392 816 -46 302 C ATOM 426 CD2 LEU A 105 -6.746 -21.836 -3.173 1.00 60.71 C ANISOU 426 CD2 LEU A 105 7534 7745 7789 928 -255 268 C ATOM 427 N PHE A 106 -8.848 -19.521 1.162 1.00 69.13 N ANISOU 427 N PHE A 106 9047 8817 8401 725 -651 567 N ATOM 428 CA PHE A 106 -8.509 -18.828 2.401 1.00 72.84 C ANISOU 428 CA PHE A 106 9549 9300 8827 680 -786 598 C ATOM 429 C PHE A 106 -9.552 -18.998 3.503 1.00 75.02 C ANISOU 429 C PHE A 106 9988 9586 8928 670 -859 666 C ATOM 430 O PHE A 106 -9.275 -18.720 4.670 1.00 76.25 O ANISOU 430 O PHE A 106 10185 9763 9024 650 -994 694 O ATOM 431 CB PHE A 106 -8.294 -17.339 2.122 1.00 72.63 C ANISOU 431 CB PHE A 106 9507 9305 8786 609 -717 551 C ATOM 432 CG PHE A 106 -7.156 -17.059 1.184 1.00 74.62 C ANISOU 432 CG PHE A 106 9588 9550 9214 605 -639 502 C ATOM 433 CD1 PHE A 106 -5.852 -17.016 1.650 1.00 76.97 C ANISOU 433 CD1 PHE A 106 9742 9825 9679 600 -750 480 C ATOM 434 CD2 PHE A 106 -7.387 -16.841 -0.164 1.00 75.51 C ANISOU 434 CD2 PHE A 106 9680 9687 9322 608 -453 482 C ATOM 435 CE1 PHE A 106 -4.801 -16.761 0.790 1.00 78.53 C ANISOU 435 CE1 PHE A 106 9766 10014 10060 593 -657 438 C ATOM 436 CE2 PHE A 106 -6.340 -16.585 -1.029 1.00 76.38 C ANISOU 436 CE2 PHE A 106 9636 9803 9582 603 -354 448 C ATOM 437 CZ PHE A 106 -5.045 -16.545 -0.551 1.00 78.25 C ANISOU 437 CZ PHE A 106 9717 10008 10007 594 -446 425 C ATOM 438 N VAL A 107 -10.746 -19.453 3.139 1.00 75.20 N ANISOU 438 N VAL A 107 10102 9600 8870 685 -768 690 N ATOM 439 CA VAL A 107 -11.813 -19.626 4.119 1.00 74.05 C ANISOU 439 CA VAL A 107 10102 9464 8570 672 -801 761 C ATOM 440 C VAL A 107 -12.024 -21.096 4.473 1.00 71.04 C ANISOU 440 C VAL A 107 9729 9024 8239 726 -860 848 C ATOM 441 O VAL A 107 -12.034 -21.464 5.647 1.00 70.01 O ANISOU 441 O VAL A 107 9663 8898 8039 729 -970 941 O ATOM 442 CB VAL A 107 -13.144 -19.037 3.615 1.00 74.40 C ANISOU 442 CB VAL A 107 10237 9527 8504 643 -663 737 C ATOM 443 CG1 VAL A 107 -14.244 -19.261 4.640 1.00 73.77 C ANISOU 443 CG1 VAL A 107 10290 9456 8285 630 -675 808 C ATOM 444 CG2 VAL A 107 -12.988 -17.556 3.305 1.00 78.60 C ANISOU 444 CG2 VAL A 107 10764 10096 9004 592 -608 671 C ATOM 445 N MET A 108 -12.192 -21.930 3.452 1.00 68.08 N ANISOU 445 N MET A 108 9289 8593 7984 768 -788 818 N ATOM 446 CA MET A 108 -12.434 -23.357 3.655 1.00 68.33 C ANISOU 446 CA MET A 108 9311 8538 8112 818 -832 890 C ATOM 447 C MET A 108 -11.264 -24.128 4.293 1.00 72.72 C ANISOU 447 C MET A 108 9783 9044 8803 865 -986 954 C ATOM 448 O MET A 108 -11.498 -24.951 5.178 1.00 79.25 O ANISOU 448 O MET A 108 10660 9822 9630 885 -1073 1081 O ATOM 449 CB MET A 108 -12.819 -24.022 2.328 1.00 68.04 C ANISOU 449 CB MET A 108 9211 8449 8191 854 -727 802 C ATOM 450 CG MET A 108 -14.143 -23.548 1.748 1.00 67.47 C ANISOU 450 CG MET A 108 9222 8410 8003 821 -607 761 C ATOM 451 SD MET A 108 -14.679 -24.561 0.355 1.00 70.63 S ANISOU 451 SD MET A 108 9558 8748 8532 871 -528 654 S ATOM 452 CE MET A 108 -16.036 -23.582 -0.281 1.00 63.67 C ANISOU 452 CE MET A 108 8767 7939 7486 827 -418 608 C ATOM 453 N PRO A 109 -10.011 -23.889 3.847 1.00 71.72 N ANISOU 453 N PRO A 109 9522 8924 8806 886 -1018 878 N ATOM 454 CA PRO A 109 -8.923 -24.648 4.481 1.00 72.34 C ANISOU 454 CA PRO A 109 9505 8945 9036 938 -1181 942 C ATOM 455 C PRO A 109 -8.777 -24.369 5.975 1.00 73.22 C ANISOU 455 C PRO A 109 9709 9104 9008 916 -1346 1061 C ATOM 456 O PRO A 109 -8.561 -25.298 6.753 1.00 72.41 O ANISOU 456 O PRO A 109 9612 8946 8956 961 -1481 1187 O ATOM 457 CB PRO A 109 -7.677 -24.174 3.725 1.00 73.21 C ANISOU 457 CB PRO A 109 9449 9071 9297 949 -1162 823 C ATOM 458 CG PRO A 109 -8.187 -23.710 2.415 1.00 72.59 C ANISOU 458 CG PRO A 109 9367 9027 9185 928 -963 709 C ATOM 459 CD PRO A 109 -9.512 -23.084 2.716 1.00 71.19 C ANISOU 459 CD PRO A 109 9366 8903 8782 870 -905 747 C ATOM 460 N ILE A 110 -8.895 -23.104 6.364 1.00 76.22 N ANISOU 460 N ILE A 110 10164 9584 9213 851 -1340 1020 N ATOM 461 CA ILE A 110 -8.794 -22.723 7.768 1.00 77.22 C ANISOU 461 CA ILE A 110 10391 9780 9168 828 -1492 1099 C ATOM 462 C ILE A 110 -10.003 -23.239 8.547 1.00 71.26 C ANISOU 462 C ILE A 110 9808 9035 8234 823 -1470 1231 C ATOM 463 O ILE A 110 -9.909 -23.541 9.738 1.00 70.75 O ANISOU 463 O ILE A 110 9825 9005 8051 835 -1609 1353 O ATOM 464 CB ILE A 110 -8.676 -21.192 7.925 1.00 75.39 C ANISOU 464 CB ILE A 110 10191 9641 8814 757 -1476 989 C ATOM 465 CG1 ILE A 110 -7.505 -20.662 7.094 1.00 74.29 C ANISOU 465 CG1 ILE A 110 9870 9481 8877 752 -1470 872 C ATOM 466 CG2 ILE A 110 -8.496 -20.808 9.383 1.00 75.75 C ANISOU 466 CG2 ILE A 110 10338 9768 8675 739 -1649 1036 C ATOM 467 CD1 ILE A 110 -7.250 -19.181 7.269 1.00 74.79 C ANISOU 467 CD1 ILE A 110 9937 9605 8876 679 -1471 770 C ATOM 468 N ALA A 111 -11.135 -23.358 7.860 1.00 69.74 N ANISOU 468 N ALA A 111 9662 8813 8022 807 -1295 1212 N ATOM 469 CA ALA A 111 -12.359 -23.862 8.473 1.00 73.23 C ANISOU 469 CA ALA A 111 10241 9250 8333 795 -1241 1332 C ATOM 470 C ALA A 111 -12.208 -25.318 8.909 1.00 77.02 C ANISOU 470 C ALA A 111 10702 9632 8929 852 -1332 1495 C ATOM 471 O ALA A 111 -12.907 -25.779 9.811 1.00 81.63 O ANISOU 471 O ALA A 111 11402 10222 9391 845 -1338 1647 O ATOM 472 CB ALA A 111 -13.530 -23.718 7.513 1.00 71.24 C ANISOU 472 CB ALA A 111 10006 8971 8089 770 -1050 1260 C ATOM 473 N LEU A 112 -11.294 -26.037 8.262 1.00 74.79 N ANISOU 473 N LEU A 112 10268 9255 8895 910 -1394 1467 N ATOM 474 CA LEU A 112 -11.014 -27.423 8.623 1.00 81.60 C ANISOU 474 CA LEU A 112 11087 9997 9921 973 -1496 1617 C ATOM 475 C LEU A 112 -10.359 -27.512 9.995 1.00 92.31 C ANISOU 475 C LEU A 112 12501 11405 11166 992 -1698 1775 C ATOM 476 O LEU A 112 -10.602 -28.456 10.746 1.00 92.34 O ANISOU 476 O LEU A 112 12562 11351 11173 1021 -1767 1972 O ATOM 477 CB LEU A 112 -10.116 -28.087 7.580 1.00 80.87 C ANISOU 477 CB LEU A 112 10801 9789 10136 1038 -1511 1517 C ATOM 478 CG LEU A 112 -10.705 -28.342 6.193 1.00 78.45 C ANISOU 478 CG LEU A 112 10432 9418 9959 1040 -1336 1371 C ATOM 479 CD1 LEU A 112 -9.713 -29.120 5.346 1.00 79.11 C ANISOU 479 CD1 LEU A 112 10327 9392 10338 1117 -1364 1278 C ATOM 480 CD2 LEU A 112 -12.029 -29.083 6.294 1.00 78.09 C ANISOU 480 CD2 LEU A 112 10473 9294 9904 1025 -1254 1461 C ATOM 481 N LEU A 113 -9.526 -26.525 10.313 1.00100.48 N ANISOU 481 N LEU A 113 13520 12549 12108 976 -1798 1691 N ATOM 482 CA LEU A 113 -8.816 -26.493 11.587 1.00107.97 C ANISOU 482 CA LEU A 113 14519 13570 12935 996 -2019 1809 C ATOM 483 C LEU A 113 -9.787 -26.432 12.761 1.00116.24 C ANISOU 483 C LEU A 113 15782 14714 13671 962 -2009 1961 C ATOM 484 O LEU A 113 -9.510 -26.963 13.835 1.00120.70 O ANISOU 484 O LEU A 113 16417 15305 14138 996 -2172 2144 O ATOM 485 CB LEU A 113 -7.854 -25.305 11.633 1.00101.75 C ANISOU 485 CB LEU A 113 13668 12881 12113 970 -2114 1651 C ATOM 486 CG LEU A 113 -6.798 -25.255 10.527 1.00 93.80 C ANISOU 486 CG LEU A 113 12437 11796 11406 997 -2109 1504 C ATOM 487 CD1 LEU A 113 -5.867 -24.068 10.724 1.00 90.64 C ANISOU 487 CD1 LEU A 113 11971 11485 10981 960 -2210 1371 C ATOM 488 CD2 LEU A 113 -6.012 -26.556 10.472 1.00 92.67 C ANISOU 488 CD2 LEU A 113 12157 11522 11532 1089 -2238 1605 C ATOM 489 N THR A 114 -10.926 -25.780 12.549 1.00118.69 N ANISOU 489 N THR A 114 16193 15078 13824 898 -1814 1890 N ATOM 490 CA THR A 114 -11.976 -25.731 13.558 1.00130.72 C ANISOU 490 CA THR A 114 17910 16690 15066 863 -1752 2018 C ATOM 491 C THR A 114 -12.571 -27.123 13.749 1.00130.12 C ANISOU 491 C THR A 114 17859 16496 15084 894 -1716 2241 C ATOM 492 O THR A 114 -12.926 -27.516 14.860 1.00129.64 O ANISOU 492 O THR A 114 17934 16490 14834 896 -1755 2441 O ATOM 493 CB THR A 114 -13.090 -24.738 13.169 1.00135.85 C ANISOU 493 CB THR A 114 18631 17401 15584 794 -1538 1876 C ATOM 494 OG1 THR A 114 -12.513 -23.458 12.883 1.00132.71 O ANISOU 494 OG1 THR A 114 18193 17080 15152 764 -1565 1673 O ATOM 495 CG2 THR A 114 -14.101 -24.593 14.297 1.00143.22 C ANISOU 495 CG2 THR A 114 19757 18443 16219 759 -1466 1990 C ATOM 496 N ILE A 115 -12.662 -27.867 12.651 1.00122.36 N ANISOU 496 N ILE A 115 16742 15350 14399 918 -1639 2204 N ATOM 497 CA ILE A 115 -13.184 -29.227 12.678 1.00118.80 C ANISOU 497 CA ILE A 115 16281 14747 14113 946 -1605 2390 C ATOM 498 C ILE A 115 -12.113 -30.222 13.116 1.00120.71 C ANISOU 498 C ILE A 115 16449 14895 14520 1025 -1818 2552 C ATOM 499 O ILE A 115 -12.362 -31.093 13.950 1.00122.05 O ANISOU 499 O ILE A 115 16692 15015 14667 1045 -1870 2802 O ATOM 500 CB ILE A 115 -13.718 -29.652 11.294 1.00115.89 C ANISOU 500 CB ILE A 115 15790 14232 14010 944 -1451 2256 C ATOM 501 CG1 ILE A 115 -14.697 -28.610 10.750 1.00112.41 C ANISOU 501 CG1 ILE A 115 15402 13881 13428 875 -1264 2088 C ATOM 502 CG2 ILE A 115 -14.373 -31.023 11.371 1.00118.73 C ANISOU 502 CG2 ILE A 115 16137 14418 14556 961 -1409 2436 C ATOM 503 CD1 ILE A 115 -15.951 -28.468 11.576 1.00111.86 C ANISOU 503 CD1 ILE A 115 15486 13874 13141 819 -1144 2210 C ATOM 504 N MET A 116 -10.920 -30.080 12.548 1.00121.42 N ANISOU 504 N MET A 116 16388 14957 14790 1071 -1936 2416 N ATOM 505 CA MET A 116 -9.841 -31.038 12.761 1.00122.55 C ANISOU 505 CA MET A 116 16416 14984 15163 1158 -2137 2535 C ATOM 506 C MET A 116 -9.184 -30.877 14.130 1.00126.23 C ANISOU 506 C MET A 116 16977 15569 15414 1181 -2366 2705 C ATOM 507 O MET A 116 -8.946 -31.862 14.829 1.00127.65 O ANISOU 507 O MET A 116 17172 15671 15659 1238 -2505 2946 O ATOM 508 CB MET A 116 -8.788 -30.898 11.659 1.00119.22 C ANISOU 508 CB MET A 116 15784 14499 15016 1199 -2167 2316 C ATOM 509 CG MET A 116 -7.826 -32.067 11.560 1.00118.80 C ANISOU 509 CG MET A 116 15566 14271 15301 1298 -2323 2401 C ATOM 510 SD MET A 116 -6.670 -31.883 10.189 1.00164.04 S ANISOU 510 SD MET A 116 21040 19938 21352 1344 -2303 2121 S ATOM 511 CE MET A 116 -7.806 -31.652 8.823 1.00 60.81 C ANISOU 511 CE MET A 116 7976 6846 8285 1286 -2003 1916 C ATOM 512 N PHE A 117 -8.890 -29.636 14.507 1.00129.08 N ANISOU 512 N PHE A 117 17401 16117 15526 1140 -2413 2579 N ATOM 513 CA PHE A 117 -8.226 -29.364 15.779 1.00133.57 C ANISOU 513 CA PHE A 117 18061 16824 15867 1161 -2650 2694 C ATOM 514 C PHE A 117 -9.236 -29.004 16.865 1.00140.28 C ANISOU 514 C PHE A 117 19157 17834 16309 1109 -2583 2820 C ATOM 515 O PHE A 117 -10.440 -29.204 16.699 1.00137.94 O ANISOU 515 O PHE A 117 18945 17508 15956 1064 -2363 2869 O ATOM 516 CB PHE A 117 -7.198 -28.235 15.629 1.00131.06 C ANISOU 516 CB PHE A 117 17651 16608 15538 1150 -2769 2467 C ATOM 517 CG PHE A 117 -5.968 -28.619 14.845 1.00128.20 C ANISOU 517 CG PHE A 117 17041 16113 15556 1213 -2881 2379 C ATOM 518 CD1 PHE A 117 -5.852 -29.871 14.261 1.00128.70 C ANISOU 518 CD1 PHE A 117 16979 15978 15942 1280 -2862 2471 C ATOM 519 CD2 PHE A 117 -4.919 -27.724 14.706 1.00125.00 C ANISOU 519 CD2 PHE A 117 16515 15774 15204 1205 -2999 2195 C ATOM 520 CE1 PHE A 117 -4.720 -30.216 13.544 1.00127.56 C ANISOU 520 CE1 PHE A 117 16599 15715 16153 1344 -2948 2372 C ATOM 521 CE2 PHE A 117 -3.784 -28.066 13.993 1.00124.00 C ANISOU 521 CE2 PHE A 117 16147 15529 15438 1263 -3081 2112 C ATOM 522 CZ PHE A 117 -3.685 -29.313 13.412 1.00125.42 C ANISOU 522 CZ PHE A 117 16208 15523 15924 1336 -3051 2197 C ATOM 523 N GLU A 118 -8.738 -28.471 17.976 1.00151.78 N ANISOU 523 N GLU A 118 20722 19464 17483 1115 -2775 2861 N ATOM 524 CA GLU A 118 -9.593 -28.095 19.096 1.00155.82 C ANISOU 524 CA GLU A 118 21475 20157 17572 1072 -2721 2966 C ATOM 525 C GLU A 118 -10.303 -26.771 18.833 1.00156.65 C ANISOU 525 C GLU A 118 21647 20382 17492 988 -2528 2715 C ATOM 526 O GLU A 118 -10.108 -26.148 17.790 1.00156.33 O ANISOU 526 O GLU A 118 21470 20281 17646 961 -2448 2481 O ATOM 527 CB GLU A 118 -8.776 -28.006 20.387 1.00160.44 C ANISOU 527 CB GLU A 118 22159 20901 17900 1117 -3015 3084 C ATOM 528 N ALA A 119 -11.122 -26.345 19.790 1.00160.54 N ANISOU 528 N ALA A 119 22348 21041 17608 949 -2448 2769 N ATOM 529 CA ALA A 119 -11.879 -25.105 19.660 1.00162.08 C ANISOU 529 CA ALA A 119 22615 21344 17624 875 -2261 2541 C ATOM 530 C ALA A 119 -10.969 -23.883 19.740 1.00166.08 C ANISOU 530 C ALA A 119 23079 21955 18069 861 -2421 2286 C ATOM 531 O ALA A 119 -11.319 -22.805 19.259 1.00172.56 O ANISOU 531 O ALA A 119 23882 22800 18881 806 -2287 2053 O ATOM 532 CB ALA A 119 -12.956 -25.031 20.730 1.00163.57 C ANISOU 532 CB ALA A 119 23031 21686 17432 845 -2130 2665 C ATOM 533 N MET A 120 -9.802 -24.059 20.351 1.00163.24 N ANISOU 533 N MET A 120 22692 21645 17686 913 -2714 2336 N ATOM 534 CA MET A 120 -8.831 -22.978 20.479 1.00154.95 C ANISOU 534 CA MET A 120 21579 20679 16616 900 -2899 2100 C ATOM 535 C MET A 120 -8.257 -22.594 19.120 1.00145.09 C ANISOU 535 C MET A 120 20095 19277 15756 882 -2849 1904 C ATOM 536 O MET A 120 -7.988 -23.455 18.283 1.00143.60 O ANISOU 536 O MET A 120 19759 18924 15877 919 -2821 1986 O ATOM 537 CB MET A 120 -7.704 -23.379 21.434 1.00156.62 C ANISOU 537 CB MET A 120 21797 20970 16742 966 -3248 2216 C ATOM 538 N TRP A 121 -8.073 -21.294 18.911 1.00136.90 N ANISOU 538 N TRP A 121 19024 18292 14701 826 -2831 1645 N ATOM 539 CA TRP A 121 -7.552 -20.767 17.654 1.00128.03 C ANISOU 539 CA TRP A 121 17691 17042 13912 799 -2762 1462 C ATOM 540 C TRP A 121 -6.040 -20.972 17.559 1.00132.07 C ANISOU 540 C TRP A 121 18012 17503 14668 842 -3020 1439 C ATOM 541 O TRP A 121 -5.278 -20.359 18.307 1.00142.18 O ANISOU 541 O TRP A 121 19289 18879 15853 837 -3244 1344 O ATOM 542 CB TRP A 121 -7.912 -19.284 17.527 1.00117.71 C ANISOU 542 CB TRP A 121 16416 15795 12512 721 -2652 1215 C ATOM 543 CG TRP A 121 -7.403 -18.609 16.292 1.00108.09 C ANISOU 543 CG TRP A 121 15001 14461 11609 684 -2571 1042 C ATOM 544 CD1 TRP A 121 -6.434 -17.652 16.225 1.00106.89 C ANISOU 544 CD1 TRP A 121 14726 14311 11579 651 -2698 858 C ATOM 545 CD2 TRP A 121 -7.847 -18.824 14.946 1.00101.43 C ANISOU 545 CD2 TRP A 121 14060 13488 10990 676 -2340 1041 C ATOM 546 NE1 TRP A 121 -6.241 -17.263 14.922 1.00103.28 N ANISOU 546 NE1 TRP A 121 14103 13732 11407 620 -2543 764 N ATOM 547 CE2 TRP A 121 -7.097 -17.967 14.117 1.00 99.83 C ANISOU 547 CE2 TRP A 121 13687 13224 11019 638 -2327 871 C ATOM 548 CE3 TRP A 121 -8.802 -19.662 14.362 1.00 97.79 C ANISOU 548 CE3 TRP A 121 13638 12959 10560 694 -2148 1165 C ATOM 549 CZ2 TRP A 121 -7.273 -17.922 12.736 1.00 96.36 C ANISOU 549 CZ2 TRP A 121 13134 12678 10802 625 -2126 832 C ATOM 550 CZ3 TRP A 121 -8.976 -19.614 12.991 1.00 95.14 C ANISOU 550 CZ3 TRP A 121 13182 12514 10452 682 -1968 1102 C ATOM 551 CH2 TRP A 121 -8.214 -18.751 12.194 1.00 94.84 C ANISOU 551 CH2 TRP A 121 12993 12437 10604 650 -1957 942 C ATOM 552 N PRO A 122 -5.603 -21.842 16.633 1.00126.57 N ANISOU 552 N PRO A 122 17143 16650 14299 886 -2990 1511 N ATOM 553 CA PRO A 122 -4.193 -22.226 16.491 1.00124.66 C ANISOU 553 CA PRO A 122 16694 16338 14334 940 -3215 1510 C ATOM 554 C PRO A 122 -3.326 -21.131 15.870 1.00119.76 C ANISOU 554 C PRO A 122 15891 15696 13917 891 -3233 1269 C ATOM 555 O PRO A 122 -2.190 -20.930 16.300 1.00121.55 O ANISOU 555 O PRO A 122 16000 15942 14242 909 -3482 1216 O ATOM 556 CB PRO A 122 -4.259 -23.450 15.576 1.00123.99 C ANISOU 556 CB PRO A 122 16496 16085 14529 997 -3102 1635 C ATOM 557 CG PRO A 122 -5.480 -23.234 14.758 1.00120.55 C ANISOU 557 CG PRO A 122 16134 15619 14052 945 -2788 1584 C ATOM 558 CD PRO A 122 -6.463 -22.527 15.650 1.00121.95 C ANISOU 558 CD PRO A 122 16542 15944 13849 891 -2734 1581 C ATOM 559 N LEU A 123 -3.862 -20.438 14.871 1.00113.46 N ANISOU 559 N LEU A 123 15063 14853 13192 829 -2975 1134 N ATOM 560 CA LEU A 123 -3.147 -19.358 14.201 1.00110.84 C ANISOU 560 CA LEU A 123 14564 14489 13061 772 -2948 928 C ATOM 561 C LEU A 123 -2.960 -18.167 15.144 1.00108.77 C ANISOU 561 C LEU A 123 14376 14342 12609 714 -3096 784 C ATOM 562 O LEU A 123 -3.527 -18.152 16.236 1.00109.92 O ANISOU 562 O LEU A 123 14723 14608 12431 719 -3181 833 O ATOM 563 CB LEU A 123 -3.905 -18.936 12.938 1.00112.17 C ANISOU 563 CB LEU A 123 14716 14591 13312 724 -2632 854 C ATOM 564 N PRO A 124 -2.139 -17.179 14.743 1.00107.61 N ANISOU 564 N PRO A 124 14061 14158 12669 660 -3128 603 N ATOM 565 CA PRO A 124 -2.067 -15.936 15.519 1.00108.35 C ANISOU 565 CA PRO A 124 14218 14337 12613 594 -3239 429 C ATOM 566 C PRO A 124 -3.437 -15.290 15.718 1.00107.89 C ANISOU 566 C PRO A 124 14382 14345 12268 547 -3044 384 C ATOM 567 O PRO A 124 -4.318 -15.440 14.870 1.00105.20 O ANISOU 567 O PRO A 124 14078 13948 11945 539 -2781 437 O ATOM 568 CB PRO A 124 -1.163 -15.048 14.665 1.00107.48 C ANISOU 568 CB PRO A 124 13866 14123 12848 532 -3203 266 C ATOM 569 CG PRO A 124 -0.254 -16.009 13.990 1.00108.79 C ANISOU 569 CG PRO A 124 13822 14196 13317 592 -3236 361 C ATOM 570 CD PRO A 124 -1.080 -17.241 13.717 1.00107.31 C ANISOU 570 CD PRO A 124 13750 13998 13025 663 -3104 553 C ATOM 571 N LEU A 125 -3.605 -14.580 16.830 1.00110.92 N ANISOU 571 N LEU A 125 14902 14847 12395 521 -3179 275 N ATOM 572 CA LEU A 125 -4.892 -13.992 17.190 1.00110.70 C ANISOU 572 CA LEU A 125 15087 14893 12081 486 -3009 222 C ATOM 573 C LEU A 125 -5.365 -12.953 16.177 1.00106.28 C ANISOU 573 C LEU A 125 14463 14229 11688 415 -2762 88 C ATOM 574 O LEU A 125 -6.564 -12.720 16.030 1.00107.15 O ANISOU 574 O LEU A 125 14709 14351 11652 400 -2549 94 O ATOM 575 CB LEU A 125 -4.812 -13.360 18.582 1.00113.89 C ANISOU 575 CB LEU A 125 15630 15450 12193 474 -3219 89 C ATOM 576 N VAL A 126 -4.419 -12.332 15.481 1.00100.55 N ANISOU 576 N VAL A 126 13525 13397 11281 372 -2791 -21 N ATOM 577 CA VAL A 126 -4.741 -11.289 14.512 1.00 98.21 C ANISOU 577 CA VAL A 126 13157 12995 11164 303 -2574 -128 C ATOM 578 C VAL A 126 -5.436 -11.850 13.274 1.00 96.55 C ANISOU 578 C VAL A 126 12935 12711 11040 323 -2305 13 C ATOM 579 O VAL A 126 -6.174 -11.140 12.592 1.00 97.40 O ANISOU 579 O VAL A 126 13065 12762 11179 282 -2097 -30 O ATOM 580 CB VAL A 126 -3.479 -10.525 14.070 1.00101.06 C ANISOU 580 CB VAL A 126 13278 13255 11864 247 -2666 -256 C ATOM 581 N LEU A 127 -5.198 -13.126 12.989 1.00 95.38 N ANISOU 581 N LEU A 127 12748 12558 10936 389 -2323 174 N ATOM 582 CA LEU A 127 -5.767 -13.762 11.806 1.00 92.75 C ANISOU 582 CA LEU A 127 12391 12157 10693 414 -2094 287 C ATOM 583 C LEU A 127 -7.176 -14.289 12.065 1.00 90.29 C ANISOU 583 C LEU A 127 12283 11897 10125 441 -1968 387 C ATOM 584 O LEU A 127 -7.862 -14.723 11.138 1.00 91.79 O ANISOU 584 O LEU A 127 12476 12037 10362 456 -1777 459 O ATOM 585 CB LEU A 127 -4.866 -14.901 11.319 1.00 92.59 C ANISOU 585 CB LEU A 127 12218 12088 10876 474 -2159 391 C ATOM 586 CG LEU A 127 -3.702 -14.550 10.386 1.00 92.49 C ANISOU 586 CG LEU A 127 11961 11986 11196 451 -2141 322 C ATOM 587 CD1 LEU A 127 -2.642 -13.711 11.089 1.00 94.69 C ANISOU 587 CD1 LEU A 127 12132 12271 11574 406 -2354 193 C ATOM 588 CD2 LEU A 127 -3.087 -15.815 9.802 1.00 92.70 C ANISOU 588 CD2 LEU A 127 11855 11961 11404 525 -2148 425 C ATOM 589 N CYS A 128 -7.605 -14.251 13.323 1.00 85.85 N ANISOU 589 N CYS A 128 11886 11441 9293 447 -2072 384 N ATOM 590 CA CYS A 128 -8.941 -14.720 13.686 1.00 82.95 C ANISOU 590 CA CYS A 128 11706 11130 8683 467 -1944 481 C ATOM 591 C CYS A 128 -10.057 -13.802 13.167 1.00 80.86 C ANISOU 591 C CYS A 128 11500 10837 8387 420 -1716 394 C ATOM 592 O CYS A 128 -11.002 -14.289 12.547 1.00 79.83 O ANISOU 592 O CYS A 128 11407 10671 8254 436 -1538 482 O ATOM 593 CB CYS A 128 -9.061 -14.888 15.205 1.00 83.28 C ANISOU 593 CB CYS A 128 11913 11311 8420 485 -2103 506 C ATOM 594 SG CYS A 128 -10.676 -15.491 15.759 1.00 90.71 S ANISOU 594 SG CYS A 128 13076 12326 9062 504 -1926 642 S ATOM 595 N PRO A 129 -9.967 -12.477 13.411 1.00 81.68 N ANISOU 595 N PRO A 129 11603 10945 8488 366 -1730 216 N ATOM 596 CA PRO A 129 -11.059 -11.666 12.862 1.00 78.50 C ANISOU 596 CA PRO A 129 11245 10496 8086 332 -1514 152 C ATOM 597 C PRO A 129 -10.966 -11.513 11.346 1.00 74.38 C ANISOU 597 C PRO A 129 10583 9854 7823 320 -1371 179 C ATOM 598 O PRO A 129 -11.977 -11.257 10.693 1.00 69.51 O ANISOU 598 O PRO A 129 10003 9198 7210 314 -1188 193 O ATOM 599 CB PRO A 129 -10.876 -10.316 13.560 1.00 81.51 C ANISOU 599 CB PRO A 129 11649 10896 8427 282 -1586 -52 C ATOM 600 CG PRO A 129 -9.424 -10.244 13.840 1.00 86.72 C ANISOU 600 CG PRO A 129 12187 11553 9209 270 -1812 -109 C ATOM 601 CD PRO A 129 -9.000 -11.650 14.161 1.00 85.93 C ANISOU 601 CD PRO A 129 12098 11515 9036 333 -1932 60 C ATOM 602 N ALA A 130 -9.764 -11.671 10.800 1.00 75.45 N ANISOU 602 N ALA A 130 10559 9940 8170 318 -1454 187 N ATOM 603 CA ALA A 130 -9.558 -11.582 9.359 1.00 74.91 C ANISOU 603 CA ALA A 130 10358 9778 8325 309 -1314 219 C ATOM 604 C ALA A 130 -10.235 -12.747 8.645 1.00 74.56 C ANISOU 604 C ALA A 130 10343 9731 8254 364 -1194 355 C ATOM 605 O ALA A 130 -10.946 -12.554 7.659 1.00 74.18 O ANISOU 605 O ALA A 130 10295 9643 8247 361 -1024 374 O ATOM 606 CB ALA A 130 -8.073 -11.550 9.036 1.00 76.06 C ANISOU 606 CB ALA A 130 10317 9882 8702 297 -1422 192 C ATOM 607 N TRP A 131 -10.007 -13.954 9.154 1.00 75.42 N ANISOU 607 N TRP A 131 10473 9877 8305 416 -1297 448 N ATOM 608 CA TRP A 131 -10.618 -15.158 8.603 1.00 75.79 C ANISOU 608 CA TRP A 131 10543 9906 8349 468 -1207 567 C ATOM 609 C TRP A 131 -12.138 -15.112 8.729 1.00 72.22 C ANISOU 609 C TRP A 131 10237 9475 7731 463 -1070 595 C ATOM 610 O TRP A 131 -12.858 -15.548 7.830 1.00 69.62 O ANISOU 610 O TRP A 131 9902 9106 7446 481 -935 638 O ATOM 611 CB TRP A 131 -10.062 -16.399 9.302 1.00 78.23 C ANISOU 611 CB TRP A 131 10848 10234 8642 522 -1363 670 C ATOM 612 CG TRP A 131 -10.811 -17.659 8.999 1.00 71.59 C ANISOU 612 CG TRP A 131 10049 9362 7790 571 -1286 794 C ATOM 613 CD1 TRP A 131 -10.818 -18.346 7.821 1.00 68.72 C ANISOU 613 CD1 TRP A 131 9593 8926 7591 603 -1187 815 C ATOM 614 CD2 TRP A 131 -11.651 -18.393 9.897 1.00 69.95 C ANISOU 614 CD2 TRP A 131 9981 9189 7406 591 -1299 908 C ATOM 615 NE1 TRP A 131 -11.617 -19.458 7.927 1.00 68.10 N ANISOU 615 NE1 TRP A 131 9580 8821 7474 640 -1151 922 N ATOM 616 CE2 TRP A 131 -12.139 -19.510 9.193 1.00 68.21 C ANISOU 616 CE2 TRP A 131 9733 8895 7287 630 -1211 995 C ATOM 617 CE3 TRP A 131 -12.040 -18.212 11.228 1.00 71.82 C ANISOU 617 CE3 TRP A 131 10365 9517 7406 579 -1368 944 C ATOM 618 CZ2 TRP A 131 -12.995 -20.442 9.773 1.00 68.38 C ANISOU 618 CZ2 TRP A 131 9856 8912 7214 651 -1189 1130 C ATOM 619 CZ3 TRP A 131 -12.891 -19.138 11.802 1.00 71.92 C ANISOU 619 CZ3 TRP A 131 10489 9544 7295 602 -1331 1089 C ATOM 620 CH2 TRP A 131 -13.359 -20.239 11.075 1.00 69.99 C ANISOU 620 CH2 TRP A 131 10201 9205 7187 634 -1241 1188 C ATOM 621 N LEU A 132 -12.619 -14.582 9.848 1.00 70.43 N ANISOU 621 N LEU A 132 10133 9313 7315 441 -1107 557 N ATOM 622 CA LEU A 132 -14.049 -14.394 10.053 1.00 67.40 C ANISOU 622 CA LEU A 132 9874 8950 6787 433 -966 564 C ATOM 623 C LEU A 132 -14.598 -13.375 9.063 1.00 70.15 C ANISOU 623 C LEU A 132 10183 9238 7234 402 -820 482 C ATOM 624 O LEU A 132 -15.690 -13.545 8.522 1.00 75.62 O ANISOU 624 O LEU A 132 10907 9906 7919 413 -682 519 O ATOM 625 CB LEU A 132 -14.338 -13.944 11.486 1.00 64.96 C ANISOU 625 CB LEU A 132 9698 8736 6248 417 -1028 515 C ATOM 626 CG LEU A 132 -14.191 -14.982 12.598 1.00 61.59 C ANISOU 626 CG LEU A 132 9362 8391 5648 451 -1144 635 C ATOM 627 CD1 LEU A 132 -14.374 -14.333 13.959 1.00 61.60 C ANISOU 627 CD1 LEU A 132 9499 8510 5395 433 -1205 554 C ATOM 628 CD2 LEU A 132 -15.192 -16.106 12.404 1.00 58.92 C ANISOU 628 CD2 LEU A 132 9072 8031 5284 480 -1021 790 C ATOM 629 N PHE A 133 -13.829 -12.317 8.830 1.00 68.22 N ANISOU 629 N PHE A 133 9861 8963 7096 365 -858 380 N ATOM 630 CA PHE A 133 -14.232 -11.259 7.911 1.00 61.26 C ANISOU 630 CA PHE A 133 8938 8014 6325 335 -733 323 C ATOM 631 C PHE A 133 -14.289 -11.757 6.471 1.00 55.24 C ANISOU 631 C PHE A 133 8094 7205 5690 359 -632 402 C ATOM 632 O PHE A 133 -15.251 -11.487 5.752 1.00 52.04 O ANISOU 632 O PHE A 133 7712 6771 5290 364 -506 418 O ATOM 633 CB PHE A 133 -13.277 -10.069 8.016 1.00 59.51 C ANISOU 633 CB PHE A 133 8637 7753 6221 284 -803 210 C ATOM 634 CG PHE A 133 -13.480 -9.035 6.946 1.00 55.17 C ANISOU 634 CG PHE A 133 8022 7114 5824 253 -680 188 C ATOM 635 CD1 PHE A 133 -14.585 -8.202 6.971 1.00 51.95 C ANISOU 635 CD1 PHE A 133 7684 6673 5381 242 -581 143 C ATOM 636 CD2 PHE A 133 -12.562 -8.894 5.918 1.00 52.81 C ANISOU 636 CD2 PHE A 133 7589 6764 5711 238 -658 223 C ATOM 637 CE1 PHE A 133 -14.774 -7.250 5.987 1.00 49.06 C ANISOU 637 CE1 PHE A 133 7260 6218 5164 220 -480 148 C ATOM 638 CE2 PHE A 133 -12.745 -7.944 4.932 1.00 49.52 C ANISOU 638 CE2 PHE A 133 7122 6272 5423 210 -540 233 C ATOM 639 CZ PHE A 133 -13.852 -7.120 4.967 1.00 50.09 C ANISOU 639 CZ PHE A 133 7270 6304 5459 202 -461 203 C ATOM 640 N LEU A 134 -13.254 -12.482 6.056 1.00 55.76 N ANISOU 640 N LEU A 134 8062 7267 5855 379 -692 443 N ATOM 641 CA LEU A 134 -13.182 -13.008 4.697 1.00 52.88 C ANISOU 641 CA LEU A 134 7620 6874 5598 408 -598 496 C ATOM 642 C LEU A 134 -14.302 -14.005 4.426 1.00 54.85 C ANISOU 642 C LEU A 134 7939 7133 5769 452 -530 560 C ATOM 643 O LEU A 134 -14.825 -14.073 3.314 1.00 60.82 O ANISOU 643 O LEU A 134 8677 7873 6561 468 -425 575 O ATOM 644 CB LEU A 134 -11.823 -13.664 4.444 1.00 49.49 C ANISOU 644 CB LEU A 134 7065 6440 5300 427 -676 509 C ATOM 645 CG LEU A 134 -10.619 -12.722 4.406 1.00 46.93 C ANISOU 645 CG LEU A 134 6625 6091 5116 380 -722 447 C ATOM 646 CD1 LEU A 134 -9.354 -13.483 4.048 1.00 47.03 C ANISOU 646 CD1 LEU A 134 6491 6095 5281 408 -777 462 C ATOM 647 CD2 LEU A 134 -10.863 -11.585 3.428 1.00 48.15 C ANISOU 647 CD2 LEU A 134 6751 6206 5338 340 -582 431 C ATOM 648 N ASP A 135 -14.666 -14.775 5.446 1.00 51.68 N ANISOU 648 N ASP A 135 7615 6758 5263 470 -594 602 N ATOM 649 CA ASP A 135 -15.762 -15.727 5.323 1.00 49.17 C ANISOU 649 CA ASP A 135 7354 6432 4896 501 -530 667 C ATOM 650 C ASP A 135 -17.067 -15.016 4.988 1.00 48.40 C ANISOU 650 C ASP A 135 7314 6327 4750 485 -409 640 C ATOM 651 O ASP A 135 -17.746 -15.369 4.027 1.00 46.58 O ANISOU 651 O ASP A 135 7063 6070 4565 507 -330 655 O ATOM 652 CB ASP A 135 -15.930 -16.535 6.610 1.00 49.76 C ANISOU 652 CB ASP A 135 7509 6536 4860 513 -609 739 C ATOM 653 CG ASP A 135 -17.166 -17.413 6.586 1.00 47.05 C ANISOU 653 CG ASP A 135 7221 6171 4485 532 -525 812 C ATOM 654 OD1 ASP A 135 -17.400 -18.083 5.558 1.00 45.11 O ANISOU 654 OD1 ASP A 135 6913 5874 4351 559 -476 823 O ATOM 655 OD2 ASP A 135 -17.912 -17.422 7.587 1.00 47.95 O ANISOU 655 OD2 ASP A 135 7435 6320 4465 518 -504 851 O ATOM 656 N VAL A 136 -17.407 -14.010 5.787 1.00 50.28 N ANISOU 656 N VAL A 136 7617 6584 4902 451 -402 589 N ATOM 657 CA VAL A 136 -18.642 -13.262 5.593 1.00 51.49 C ANISOU 657 CA VAL A 136 7814 6720 5030 440 -292 556 C ATOM 658 C VAL A 136 -18.596 -12.452 4.299 1.00 52.17 C ANISOU 658 C VAL A 136 7832 6762 5229 436 -233 531 C ATOM 659 O VAL A 136 -19.592 -12.353 3.584 1.00 50.52 O ANISOU 659 O VAL A 136 7626 6529 5040 451 -152 544 O ATOM 660 CB VAL A 136 -18.921 -12.317 6.780 1.00 43.51 C ANISOU 660 CB VAL A 136 6881 5737 3915 408 -297 481 C ATOM 661 CG1 VAL A 136 -20.273 -11.642 6.618 1.00 43.14 C ANISOU 661 CG1 VAL A 136 6867 5660 3865 407 -175 445 C ATOM 662 CG2 VAL A 136 -18.865 -13.085 8.090 1.00 44.56 C ANISOU 662 CG2 VAL A 136 7096 5938 3896 414 -359 519 C ATOM 663 N LEU A 137 -17.432 -11.884 3.999 1.00 53.13 N ANISOU 663 N LEU A 137 7887 6872 5429 414 -277 504 N ATOM 664 CA LEU A 137 -17.254 -11.060 2.805 1.00 51.26 C ANISOU 664 CA LEU A 137 7586 6596 5294 405 -214 506 C ATOM 665 C LEU A 137 -17.514 -11.835 1.519 1.00 53.63 C ANISOU 665 C LEU A 137 7852 6908 5616 447 -157 563 C ATOM 666 O LEU A 137 -18.343 -11.439 0.699 1.00 56.86 O ANISOU 666 O LEU A 137 8272 7304 6028 460 -87 582 O ATOM 667 CB LEU A 137 -15.841 -10.471 2.774 1.00 50.51 C ANISOU 667 CB LEU A 137 7407 6485 5299 369 -264 479 C ATOM 668 CG LEU A 137 -15.424 -9.745 1.493 1.00 50.88 C ANISOU 668 CG LEU A 137 7376 6497 5459 355 -185 512 C ATOM 669 CD1 LEU A 137 -16.292 -8.519 1.258 1.00 53.76 C ANISOU 669 CD1 LEU A 137 7776 6803 5847 336 -118 510 C ATOM 670 CD2 LEU A 137 -13.952 -9.365 1.547 1.00 49.87 C ANISOU 670 CD2 LEU A 137 7143 6349 5455 315 -231 490 C ATOM 671 N PHE A 138 -16.803 -12.945 1.352 1.00 51.52 N ANISOU 671 N PHE A 138 7541 6667 5367 473 -198 581 N ATOM 672 CA PHE A 138 -16.868 -13.722 0.121 1.00 47.79 C ANISOU 672 CA PHE A 138 7028 6211 4919 516 -151 603 C ATOM 673 C PHE A 138 -18.185 -14.479 -0.019 1.00 47.55 C ANISOU 673 C PHE A 138 7050 6177 4839 549 -129 613 C ATOM 674 O PHE A 138 -18.712 -14.614 -1.123 1.00 53.63 O ANISOU 674 O PHE A 138 7809 6960 5607 578 -81 612 O ATOM 675 CB PHE A 138 -15.692 -14.697 0.054 1.00 49.78 C ANISOU 675 CB PHE A 138 7203 6475 5236 539 -201 599 C ATOM 676 CG PHE A 138 -14.348 -14.027 0.072 1.00 51.80 C ANISOU 676 CG PHE A 138 7376 6730 5577 507 -219 584 C ATOM 677 CD1 PHE A 138 -14.161 -12.805 -0.551 1.00 52.44 C ANISOU 677 CD1 PHE A 138 7431 6802 5691 472 -148 589 C ATOM 678 CD2 PHE A 138 -13.273 -14.616 0.717 1.00 53.34 C ANISOU 678 CD2 PHE A 138 7507 6920 5838 513 -313 575 C ATOM 679 CE1 PHE A 138 -12.927 -12.184 -0.535 1.00 54.03 C ANISOU 679 CE1 PHE A 138 7538 6988 6003 433 -157 578 C ATOM 680 CE2 PHE A 138 -12.036 -13.998 0.740 1.00 55.42 C ANISOU 680 CE2 PHE A 138 7673 7175 6208 480 -337 553 C ATOM 681 CZ PHE A 138 -11.864 -12.781 0.112 1.00 55.17 C ANISOU 681 CZ PHE A 138 7610 7132 6221 436 -253 552 C ATOM 682 N SER A 139 -18.715 -14.972 1.096 1.00 44.83 N ANISOU 682 N SER A 139 6760 5821 4453 544 -165 625 N ATOM 683 CA SER A 139 -19.981 -15.699 1.076 1.00 46.72 C ANISOU 683 CA SER A 139 7034 6043 4676 565 -136 640 C ATOM 684 C SER A 139 -21.142 -14.774 0.725 1.00 51.47 C ANISOU 684 C SER A 139 7663 6633 5259 558 -72 626 C ATOM 685 O SER A 139 -22.099 -15.185 0.071 1.00 55.60 O ANISOU 685 O SER A 139 8177 7145 5803 584 -46 624 O ATOM 686 CB SER A 139 -20.239 -16.375 2.423 1.00 47.52 C ANISOU 686 CB SER A 139 7186 6135 4734 555 -170 680 C ATOM 687 OG SER A 139 -19.190 -17.266 2.755 1.00 49.20 O ANISOU 687 OG SER A 139 7368 6347 4978 570 -248 710 O ATOM 688 N THR A 140 -21.053 -13.524 1.169 1.00 57.14 N ANISOU 688 N THR A 140 8406 7347 5958 527 -57 608 N ATOM 689 CA THR A 140 -22.066 -12.525 0.852 1.00 52.95 C ANISOU 689 CA THR A 140 7889 6789 5439 525 -2 596 C ATOM 690 C THR A 140 -21.925 -12.076 -0.599 1.00 53.91 C ANISOU 690 C THR A 140 7970 6915 5598 546 16 618 C ATOM 691 O THR A 140 -22.916 -11.814 -1.282 1.00 54.61 O ANISOU 691 O THR A 140 8059 6992 5700 570 40 629 O ATOM 692 CB THR A 140 -21.963 -11.301 1.783 1.00 49.47 C ANISOU 692 CB THR A 140 7481 6324 4989 487 8 555 C ATOM 693 OG1 THR A 140 -22.007 -11.732 3.148 1.00 46.50 O ANISOU 693 OG1 THR A 140 7158 5972 4537 471 -10 535 O ATOM 694 CG2 THR A 140 -23.101 -10.327 1.525 1.00 49.88 C ANISOU 694 CG2 THR A 140 7538 6329 5085 494 66 540 C ATOM 695 N ALA A 141 -20.681 -11.998 -1.061 1.00 53.18 N ANISOU 695 N ALA A 141 7840 6846 5520 538 4 629 N ATOM 696 CA ALA A 141 -20.388 -11.587 -2.428 1.00 54.65 C ANISOU 696 CA ALA A 141 7993 7056 5716 555 39 665 C ATOM 697 C ALA A 141 -20.959 -12.575 -3.438 1.00 55.49 C ANISOU 697 C ALA A 141 8095 7207 5783 607 38 661 C ATOM 698 O ALA A 141 -21.354 -12.190 -4.537 1.00 61.84 O ANISOU 698 O ALA A 141 8901 8039 6557 633 60 690 O ATOM 699 CB ALA A 141 -18.887 -11.437 -2.626 1.00 58.46 C ANISOU 699 CB ALA A 141 8420 7556 6234 532 45 674 C ATOM 700 N SER A 142 -21.004 -13.847 -3.057 1.00 52.99 N ANISOU 700 N SER A 142 7772 6895 5469 624 3 624 N ATOM 701 CA SER A 142 -21.526 -14.886 -3.935 1.00 52.30 C ANISOU 701 CA SER A 142 7668 6834 5369 671 -11 591 C ATOM 702 C SER A 142 -23.028 -14.737 -4.139 1.00 49.56 C ANISOU 702 C SER A 142 7343 6466 5022 686 -19 588 C ATOM 703 O SER A 142 -23.529 -14.867 -5.255 1.00 51.21 O ANISOU 703 O SER A 142 7544 6712 5200 725 -33 570 O ATOM 704 CB SER A 142 -21.210 -16.273 -3.373 1.00 55.88 C ANISOU 704 CB SER A 142 8098 7264 5869 681 -50 558 C ATOM 705 OG SER A 142 -21.879 -16.490 -2.143 1.00 62.33 O ANISOU 705 OG SER A 142 8947 8028 6707 656 -64 580 O ATOM 706 N ILE A 143 -23.742 -14.461 -3.053 1.00 47.55 N ANISOU 706 N ILE A 143 7112 6157 4798 659 -12 598 N ATOM 707 CA ILE A 143 -25.194 -14.353 -3.099 1.00 45.70 C ANISOU 707 CA ILE A 143 6877 5890 4598 672 -11 591 C ATOM 708 C ILE A 143 -25.634 -13.068 -3.796 1.00 45.44 C ANISOU 708 C ILE A 143 6849 5859 4556 685 -2 622 C ATOM 709 O ILE A 143 -26.607 -13.064 -4.550 1.00 49.09 O ANISOU 709 O ILE A 143 7293 6323 5035 720 -31 617 O ATOM 710 CB ILE A 143 -25.803 -14.404 -1.684 1.00 44.63 C ANISOU 710 CB ILE A 143 6760 5703 4494 639 22 593 C ATOM 711 CG1 ILE A 143 -25.224 -15.582 -0.898 1.00 43.60 C ANISOU 711 CG1 ILE A 143 6636 5570 4363 625 8 600 C ATOM 712 CG2 ILE A 143 -27.317 -14.507 -1.755 1.00 46.00 C ANISOU 712 CG2 ILE A 143 6905 5837 4736 653 34 578 C ATOM 713 CD1 ILE A 143 -25.766 -15.706 0.510 1.00 44.18 C ANISOU 713 CD1 ILE A 143 6743 5614 4431 593 51 622 C ATOM 714 N TRP A 144 -24.909 -11.981 -3.551 1.00 45.01 N ANISOU 714 N TRP A 144 6813 5795 4494 658 28 657 N ATOM 715 CA TRP A 144 -25.260 -10.690 -4.132 1.00 47.65 C ANISOU 715 CA TRP A 144 7151 6107 4849 668 40 707 C ATOM 716 C TRP A 144 -24.844 -10.581 -5.594 1.00 50.59 C ANISOU 716 C TRP A 144 7521 6546 5156 701 27 760 C ATOM 717 O TRP A 144 -25.381 -9.758 -6.337 1.00 51.41 O ANISOU 717 O TRP A 144 7628 6642 5262 726 16 822 O ATOM 718 CB TRP A 144 -24.640 -9.551 -3.323 1.00 48.37 C ANISOU 718 CB TRP A 144 7253 6142 4984 622 77 717 C ATOM 719 CG TRP A 144 -25.473 -9.157 -2.145 1.00 50.34 C ANISOU 719 CG TRP A 144 7513 6326 5289 606 99 667 C ATOM 720 CD1 TRP A 144 -25.402 -9.665 -0.883 1.00 51.23 C ANISOU 720 CD1 TRP A 144 7648 6440 5376 578 113 610 C ATOM 721 CD2 TRP A 144 -26.519 -8.179 -2.125 1.00 52.26 C ANISOU 721 CD2 TRP A 144 7744 6498 5616 622 117 669 C ATOM 722 NE1 TRP A 144 -26.333 -9.060 -0.074 1.00 51.45 N ANISOU 722 NE1 TRP A 144 7684 6415 5451 574 155 567 N ATOM 723 CE2 TRP A 144 -27.032 -8.143 -0.814 1.00 53.63 C ANISOU 723 CE2 TRP A 144 7929 6636 5810 602 159 593 C ATOM 724 CE3 TRP A 144 -27.069 -7.327 -3.088 1.00 53.50 C ANISOU 724 CE3 TRP A 144 7879 6617 5833 657 102 733 C ATOM 725 CZ2 TRP A 144 -28.068 -7.290 -0.441 1.00 55.99 C ANISOU 725 CZ2 TRP A 144 8209 6859 6205 616 197 559 C ATOM 726 CZ3 TRP A 144 -28.095 -6.482 -2.717 1.00 55.19 C ANISOU 726 CZ3 TRP A 144 8069 6741 6158 673 121 712 C ATOM 727 CH2 TRP A 144 -28.585 -6.470 -1.405 1.00 55.27 C ANISOU 727 CH2 TRP A 144 8081 6714 6204 652 174 615 C ATOM 728 N HIS A 145 -23.886 -11.405 -6.005 1.00 53.85 N ANISOU 728 N HIS A 145 7925 7026 5508 704 31 740 N ATOM 729 CA HIS A 145 -23.513 -11.482 -7.412 1.00 56.72 C ANISOU 729 CA HIS A 145 8292 7480 5779 742 35 772 C ATOM 730 C HIS A 145 -24.659 -12.079 -8.214 1.00 58.13 C ANISOU 730 C HIS A 145 8476 7699 5913 798 -33 735 C ATOM 731 O HIS A 145 -25.007 -11.577 -9.281 1.00 60.63 O ANISOU 731 O HIS A 145 8813 8069 6154 835 -54 790 O ATOM 732 CB HIS A 145 -22.242 -12.312 -7.603 1.00 53.84 C ANISOU 732 CB HIS A 145 7905 7175 5378 738 65 731 C ATOM 733 CG HIS A 145 -20.982 -11.506 -7.563 1.00 52.99 C ANISOU 733 CG HIS A 145 7778 7066 5289 698 134 793 C ATOM 734 ND1 HIS A 145 -20.435 -11.034 -6.388 1.00 52.44 N ANISOU 734 ND1 HIS A 145 7691 6921 5314 643 140 793 N ATOM 735 CD2 HIS A 145 -20.161 -11.086 -8.554 1.00 54.61 C ANISOU 735 CD2 HIS A 145 7973 7339 5439 702 201 856 C ATOM 736 CE1 HIS A 145 -19.332 -10.360 -6.658 1.00 52.89 C ANISOU 736 CE1 HIS A 145 7714 6983 5398 612 199 846 C ATOM 737 NE2 HIS A 145 -19.143 -10.377 -7.966 1.00 54.38 N ANISOU 737 NE2 HIS A 145 7905 7256 5501 645 249 894 N ATOM 738 N LEU A 146 -25.247 -13.149 -7.687 1.00 57.38 N ANISOU 738 N LEU A 146 8358 7574 5868 802 -73 647 N ATOM 739 CA LEU A 146 -26.380 -13.796 -8.336 1.00 59.16 C ANISOU 739 CA LEU A 146 8568 7819 6092 847 -150 589 C ATOM 740 C LEU A 146 -27.584 -12.866 -8.371 1.00 61.21 C ANISOU 740 C LEU A 146 8823 8032 6402 861 -185 640 C ATOM 741 O LEU A 146 -28.350 -12.869 -9.332 1.00 65.81 O ANISOU 741 O LEU A 146 9400 8658 6947 909 -262 634 O ATOM 742 CB LEU A 146 -26.743 -15.101 -7.626 1.00 58.67 C ANISOU 742 CB LEU A 146 8466 7703 6122 836 -172 498 C ATOM 743 CG LEU A 146 -25.673 -16.192 -7.627 1.00 57.18 C ANISOU 743 CG LEU A 146 8266 7539 5920 835 -158 438 C ATOM 744 CD1 LEU A 146 -26.295 -17.534 -7.293 1.00 55.71 C ANISOU 744 CD1 LEU A 146 8034 7291 5841 838 -203 354 C ATOM 745 CD2 LEU A 146 -24.955 -16.249 -8.965 1.00 57.21 C ANISOU 745 CD2 LEU A 146 8284 7656 5798 878 -157 411 C ATOM 746 N CYS A 147 -27.745 -12.072 -7.317 1.00 59.20 N ANISOU 746 N CYS A 147 8567 7691 6236 822 -136 680 N ATOM 747 CA CYS A 147 -28.802 -11.072 -7.272 1.00 51.96 C ANISOU 747 CA CYS A 147 7633 6711 5396 838 -155 725 C ATOM 748 C CYS A 147 -28.579 -10.033 -8.363 1.00 50.14 C ANISOU 748 C CYS A 147 7432 6520 5097 870 -176 831 C ATOM 749 O CYS A 147 -29.521 -9.601 -9.027 1.00 48.00 O ANISOU 749 O CYS A 147 7147 6246 4845 917 -247 869 O ATOM 750 CB CYS A 147 -28.858 -10.401 -5.900 1.00 48.71 C ANISOU 750 CB CYS A 147 7219 6204 5084 792 -81 724 C ATOM 751 SG CYS A 147 -30.149 -9.146 -5.741 1.00 45.86 S ANISOU 751 SG CYS A 147 6821 5745 4861 817 -88 756 S ATOM 752 N ALA A 148 -27.322 -9.640 -8.545 1.00 49.37 N ANISOU 752 N ALA A 148 7370 6459 4930 845 -115 888 N ATOM 753 CA ALA A 148 -26.956 -8.693 -9.590 1.00 49.68 C ANISOU 753 CA ALA A 148 7440 6539 4896 866 -110 1015 C ATOM 754 C ALA A 148 -27.201 -9.300 -10.966 1.00 50.36 C ANISOU 754 C ALA A 148 7551 6757 4826 928 -180 1017 C ATOM 755 O ALA A 148 -27.751 -8.647 -11.851 1.00 52.30 O ANISOU 755 O ALA A 148 7818 7032 5022 975 -238 1113 O ATOM 756 CB ALA A 148 -25.503 -8.272 -9.443 1.00 43.49 C ANISOU 756 CB ALA A 148 6670 5761 4093 816 -14 1066 C ATOM 757 N ILE A 149 -26.792 -10.553 -11.135 1.00 44.16 N ANISOU 757 N ILE A 149 6764 6050 3964 933 -184 906 N ATOM 758 CA ILE A 149 -27.009 -11.273 -12.384 1.00 50.30 C ANISOU 758 CA ILE A 149 7565 6961 4587 994 -254 859 C ATOM 759 C ILE A 149 -28.501 -11.461 -12.648 1.00 55.60 C ANISOU 759 C ILE A 149 8209 7614 5303 1041 -389 815 C ATOM 760 O ILE A 149 -28.965 -11.296 -13.776 1.00 58.03 O ANISOU 760 O ILE A 149 8547 8015 5488 1100 -478 848 O ATOM 761 CB ILE A 149 -26.308 -12.648 -12.371 1.00 44.82 C ANISOU 761 CB ILE A 149 6855 6321 3852 990 -231 716 C ATOM 762 CG1 ILE A 149 -24.790 -12.469 -12.299 1.00 44.70 C ANISOU 762 CG1 ILE A 149 6851 6339 3793 954 -106 759 C ATOM 763 CG2 ILE A 149 -26.676 -13.456 -13.605 1.00 46.05 C ANISOU 763 CG2 ILE A 149 7029 6606 3863 1056 -317 622 C ATOM 764 CD1 ILE A 149 -24.023 -13.768 -12.202 1.00 44.44 C ANISOU 764 CD1 ILE A 149 6787 6339 3757 955 -79 623 C ATOM 765 N SER A 150 -29.247 -11.794 -11.599 1.00 61.41 N ANISOU 765 N SER A 150 8884 8233 6214 1014 -404 744 N ATOM 766 CA SER A 150 -30.691 -11.980 -11.709 1.00 70.70 C ANISOU 766 CA SER A 150 10007 9370 7487 1050 -520 695 C ATOM 767 C SER A 150 -31.385 -10.704 -12.177 1.00 69.76 C ANISOU 767 C SER A 150 9893 9230 7384 1089 -578 824 C ATOM 768 O SER A 150 -32.320 -10.752 -12.975 1.00 72.50 O ANISOU 768 O SER A 150 10218 9616 7713 1148 -712 815 O ATOM 769 CB SER A 150 -31.275 -12.431 -10.369 1.00 81.64 C ANISOU 769 CB SER A 150 11323 10627 9069 1003 -481 622 C ATOM 770 OG SER A 150 -32.681 -12.589 -10.448 1.00 95.19 O ANISOU 770 OG SER A 150 12964 12294 10911 1032 -577 576 O ATOM 771 N VAL A 151 -30.920 -9.565 -11.675 1.00 67.04 N ANISOU 771 N VAL A 151 9569 8815 7088 1059 -488 941 N ATOM 772 CA VAL A 151 -31.474 -8.273 -12.062 1.00 67.12 C ANISOU 772 CA VAL A 151 9579 8776 7147 1095 -533 1081 C ATOM 773 C VAL A 151 -30.984 -7.860 -13.448 1.00 71.87 C ANISOU 773 C VAL A 151 10258 9507 7543 1141 -573 1211 C ATOM 774 O VAL A 151 -31.767 -7.403 -14.282 1.00 76.22 O ANISOU 774 O VAL A 151 10813 10086 8062 1206 -693 1293 O ATOM 775 CB VAL A 151 -31.110 -7.175 -11.041 1.00 64.18 C ANISOU 775 CB VAL A 151 9198 8266 6922 1045 -420 1147 C ATOM 776 CG1 VAL A 151 -31.501 -5.802 -11.563 1.00 64.75 C ANISOU 776 CG1 VAL A 151 9272 8276 7056 1085 -461 1310 C ATOM 777 CG2 VAL A 151 -31.783 -7.448 -9.707 1.00 63.96 C ANISOU 777 CG2 VAL A 151 9102 8125 7076 1012 -381 1028 C ATOM 778 N ASP A 152 -29.688 -8.034 -13.690 1.00 74.33 N ANISOU 778 N ASP A 152 10628 9902 7713 1109 -471 1234 N ATOM 779 CA ASP A 152 -29.082 -7.654 -14.963 1.00 80.13 C ANISOU 779 CA ASP A 152 11441 10773 8232 1144 -466 1368 C ATOM 780 C ASP A 152 -29.662 -8.452 -16.128 1.00 79.88 C ANISOU 780 C ASP A 152 11441 10903 8008 1219 -603 1301 C ATOM 781 O ASP A 152 -29.806 -7.934 -17.235 1.00 83.01 O ANISOU 781 O ASP A 152 11899 11403 8238 1276 -667 1433 O ATOM 782 CB ASP A 152 -27.564 -7.840 -14.909 1.00 89.33 C ANISOU 782 CB ASP A 152 12637 11994 9309 1091 -311 1374 C ATOM 783 CG ASP A 152 -26.878 -7.412 -16.191 1.00 99.30 C ANISOU 783 CG ASP A 152 13977 13403 10348 1120 -267 1524 C ATOM 784 OD1 ASP A 152 -26.542 -6.215 -16.315 1.00101.20 O ANISOU 784 OD1 ASP A 152 14235 13586 10629 1102 -205 1718 O ATOM 785 OD2 ASP A 152 -26.675 -8.271 -17.075 1.00108.79 O ANISOU 785 OD2 ASP A 152 15222 14775 11338 1161 -288 1447 O ATOM 786 N ARG A 153 -29.993 -9.713 -15.874 1.00 75.19 N ANISOU 786 N ARG A 153 10804 10327 7436 1220 -654 1098 N ATOM 787 CA ARG A 153 -30.586 -10.563 -16.899 1.00 70.61 C ANISOU 787 CA ARG A 153 10240 9885 6703 1287 -800 988 C ATOM 788 C ARG A 153 -32.026 -10.148 -17.178 1.00 65.47 C ANISOU 788 C ARG A 153 9547 9193 6136 1344 -981 1021 C ATOM 789 O ARG A 153 -32.537 -10.348 -18.280 1.00 65.81 O ANISOU 789 O ARG A 153 9623 9368 6015 1415 -1131 1006 O ATOM 790 CB ARG A 153 -30.532 -12.033 -16.481 1.00 70.34 C ANISOU 790 CB ARG A 153 10154 9846 6725 1265 -803 757 C ATOM 791 N TYR A 154 -32.675 -9.568 -16.173 1.00 61.00 N ANISOU 791 N TYR A 154 8903 8449 5827 1315 -968 1057 N ATOM 792 CA TYR A 154 -34.052 -9.110 -16.317 1.00 61.24 C ANISOU 792 CA TYR A 154 8865 8413 5991 1369 -1127 1088 C ATOM 793 C TYR A 154 -34.144 -7.849 -17.168 1.00 63.26 C ANISOU 793 C TYR A 154 9181 8703 6152 1426 -1189 1315 C ATOM 794 O TYR A 154 -35.000 -7.749 -18.049 1.00 67.39 O ANISOU 794 O TYR A 154 9700 9294 6611 1504 -1376 1347 O ATOM 795 CB TYR A 154 -34.685 -8.855 -14.948 1.00 59.38 C ANISOU 795 CB TYR A 154 8522 7976 6064 1323 -1066 1049 C ATOM 796 CG TYR A 154 -35.915 -7.979 -15.013 1.00 59.12 C ANISOU 796 CG TYR A 154 8413 7845 6206 1377 -1185 1130 C ATOM 797 CD1 TYR A 154 -37.095 -8.446 -15.576 1.00 60.11 C ANISOU 797 CD1 TYR A 154 8462 7997 6379 1438 -1378 1051 C ATOM 798 CD2 TYR A 154 -35.896 -6.682 -14.515 1.00 58.37 C ANISOU 798 CD2 TYR A 154 8308 7618 6250 1370 -1111 1274 C ATOM 799 CE1 TYR A 154 -38.221 -7.648 -15.642 1.00 61.02 C ANISOU 799 CE1 TYR A 154 8490 8016 6678 1494 -1496 1124 C ATOM 800 CE2 TYR A 154 -37.017 -5.877 -14.576 1.00 59.12 C ANISOU 800 CE2 TYR A 154 8321 7609 6533 1428 -1220 1344 C ATOM 801 CZ TYR A 154 -38.177 -6.364 -15.140 1.00 61.56 C ANISOU 801 CZ TYR A 154 8550 7951 6888 1492 -1412 1274 C ATOM 802 OH TYR A 154 -39.296 -5.566 -15.203 1.00 65.42 O ANISOU 802 OH TYR A 154 8940 8329 7588 1555 -1529 1343 O ATOM 803 N ILE A 155 -33.265 -6.887 -16.903 1.00 62.88 N ANISOU 803 N ILE A 155 9182 8603 6106 1388 -1043 1477 N ATOM 804 CA ILE A 155 -33.283 -5.621 -17.627 1.00 65.88 C ANISOU 804 CA ILE A 155 9615 8983 6432 1434 -1080 1724 C ATOM 805 C ILE A 155 -32.827 -5.803 -19.072 1.00 67.79 C ANISOU 805 C ILE A 155 9976 9455 6327 1488 -1135 1813 C ATOM 806 O ILE A 155 -33.065 -4.943 -19.919 1.00 69.43 O ANISOU 806 O ILE A 155 10237 9704 6438 1548 -1218 2023 O ATOM 807 CB ILE A 155 -32.394 -4.560 -16.944 1.00 66.26 C ANISOU 807 CB ILE A 155 9674 8897 6603 1368 -898 1866 C ATOM 808 CG1 ILE A 155 -30.915 -4.922 -17.082 1.00 70.81 C ANISOU 808 CG1 ILE A 155 10325 9581 6997 1310 -732 1865 C ATOM 809 CG2 ILE A 155 -32.781 -4.403 -15.481 1.00 63.44 C ANISOU 809 CG2 ILE A 155 9214 8337 6553 1316 -833 1753 C ATOM 810 CD1 ILE A 155 -29.979 -3.899 -16.478 1.00 73.43 C ANISOU 810 CD1 ILE A 155 10656 9784 7458 1240 -566 1996 C ATOM 811 N ALA A 156 -32.175 -6.929 -19.349 1.00 66.56 N ANISOU 811 N ALA A 156 9862 9447 5981 1472 -1088 1654 N ATOM 812 CA ALA A 156 -31.750 -7.252 -20.704 1.00 68.36 C ANISOU 812 CA ALA A 156 10204 9916 5855 1527 -1127 1690 C ATOM 813 C ALA A 156 -32.942 -7.710 -21.537 1.00 72.77 C ANISOU 813 C ALA A 156 10758 10580 6311 1618 -1383 1608 C ATOM 814 O ALA A 156 -32.920 -7.638 -22.766 1.00 76.55 O ANISOU 814 O ALA A 156 11339 11256 6489 1688 -1474 1689 O ATOM 815 CB ALA A 156 -30.670 -8.322 -20.683 1.00 66.65 C ANISOU 815 CB ALA A 156 10015 9807 5500 1484 -988 1518 C ATOM 816 N ILE A 157 -33.982 -8.178 -20.854 1.00 73.28 N ANISOU 816 N ILE A 157 10701 10516 6626 1616 -1498 1446 N ATOM 817 CA ILE A 157 -35.196 -8.637 -21.515 1.00 76.14 C ANISOU 817 CA ILE A 157 11023 10946 6961 1695 -1757 1344 C ATOM 818 C ILE A 157 -36.161 -7.479 -21.747 1.00 81.05 C ANISOU 818 C ILE A 157 11613 11488 7696 1759 -1909 1548 C ATOM 819 O ILE A 157 -36.679 -7.303 -22.851 1.00 84.89 O ANISOU 819 O ILE A 157 12152 12116 7988 1848 -2109 1623 O ATOM 820 CB ILE A 157 -35.901 -9.734 -20.696 1.00 72.66 C ANISOU 820 CB ILE A 157 10444 10394 6770 1660 -1805 1075 C ATOM 821 CG1 ILE A 157 -34.961 -10.923 -20.483 1.00 67.32 C ANISOU 821 CG1 ILE A 157 9793 9781 6005 1605 -1671 879 C ATOM 822 CG2 ILE A 157 -37.181 -10.178 -21.386 1.00 76.45 C ANISOU 822 CG2 ILE A 157 10859 10929 7259 1737 -2085 961 C ATOM 823 CD1 ILE A 157 -35.576 -12.057 -19.699 1.00 68.28 C ANISOU 823 CD1 ILE A 157 9784 9785 6373 1565 -1705 637 C ATOM 824 N LYS A 158 -36.396 -6.693 -20.701 1.00 83.32 N ANISOU 824 N LYS A 158 11812 11550 8297 1718 -1820 1632 N ATOM 825 CA LYS A 158 -37.251 -5.513 -20.795 1.00 86.80 C ANISOU 825 CA LYS A 158 12204 11874 8904 1777 -1939 1828 C ATOM 826 C LYS A 158 -36.694 -4.508 -21.797 1.00 90.90 C ANISOU 826 C LYS A 158 12861 12496 9183 1824 -1943 2123 C ATOM 827 O LYS A 158 -37.425 -3.982 -22.637 1.00 90.97 O ANISOU 827 O LYS A 158 12885 12553 9127 1917 -2148 2270 O ATOM 828 CB LYS A 158 -37.408 -4.854 -19.423 1.00 86.19 C ANISOU 828 CB LYS A 158 12016 11535 9196 1716 -1796 1840 C ATOM 829 CG LYS A 158 -38.660 -5.272 -18.670 1.00 87.74 C ANISOU 829 CG LYS A 158 12042 11592 9703 1721 -1887 1661 C ATOM 830 CD LYS A 158 -39.911 -4.761 -19.368 1.00 92.51 C ANISOU 830 CD LYS A 158 12575 12179 10396 1827 -2144 1748 C ATOM 831 CE LYS A 158 -41.165 -5.082 -18.572 1.00 93.98 C ANISOU 831 CE LYS A 158 12564 12207 10936 1829 -2211 1578 C ATOM 832 NZ LYS A 158 -42.385 -4.525 -19.219 1.00 99.37 N ANISOU 832 NZ LYS A 158 13154 12856 11747 1936 -2470 1666 N ATOM 833 N LYS A 159 -35.395 -4.246 -21.700 1.00 98.05 N ANISOU 833 N LYS A 159 13858 13429 9966 1760 -1718 2219 N ATOM 834 CA LYS A 159 -34.719 -3.350 -22.628 1.00105.53 C ANISOU 834 CA LYS A 159 14937 14477 10683 1789 -1676 2510 C ATOM 835 C LYS A 159 -33.648 -4.105 -23.407 1.00105.74 C ANISOU 835 C LYS A 159 15095 14756 10326 1775 -1573 2462 C ATOM 836 O LYS A 159 -32.499 -4.179 -22.971 1.00116.00 O ANISOU 836 O LYS A 159 16417 16041 11616 1693 -1340 2449 O ATOM 837 CB LYS A 159 -34.100 -2.166 -21.883 1.00106.72 C ANISOU 837 CB LYS A 159 15066 14417 11067 1723 -1485 2702 C ATOM 838 N PRO A 160 -34.030 -4.674 -24.562 1.00112.50 N ANISOU 838 N PRO A 160 16030 15847 10867 1859 -1750 2419 N ATOM 839 CA PRO A 160 -33.135 -5.457 -25.424 1.00126.16 C ANISOU 839 CA PRO A 160 17887 17844 12205 1864 -1670 2339 C ATOM 840 C PRO A 160 -31.876 -4.687 -25.812 1.00140.46 C ANISOU 840 C PRO A 160 19809 19721 13840 1828 -1436 2600 C ATOM 841 O PRO A 160 -30.765 -5.169 -25.588 1.00140.27 O ANISOU 841 O PRO A 160 19802 19744 13749 1761 -1218 2505 O ATOM 842 CB PRO A 160 -33.999 -5.743 -26.655 1.00128.14 C ANISOU 842 CB PRO A 160 18207 18310 12169 1981 -1948 2327 C ATOM 843 CG PRO A 160 -35.398 -5.684 -26.150 1.00124.52 C ANISOU 843 CG PRO A 160 17605 17678 12028 2015 -2180 2249 C ATOM 844 CD PRO A 160 -35.396 -4.608 -25.107 1.00117.94 C ANISOU 844 CD PRO A 160 16683 16561 11569 1960 -2055 2424 C ATOM 845 N ILE A 161 -32.054 -3.502 -26.386 1.00147.08 N ANISOU 845 N ILE A 161 20709 20551 14625 1873 -1482 2932 N ATOM 846 CA ILE A 161 -30.928 -2.647 -26.740 1.00150.51 C ANISOU 846 CA ILE A 161 21233 21015 14940 1832 -1256 3219 C ATOM 847 C ILE A 161 -30.558 -1.744 -25.569 1.00151.20 C ANISOU 847 C ILE A 161 21215 20795 15441 1739 -1094 3326 C ATOM 848 O ILE A 161 -30.789 -0.535 -25.609 1.00154.75 O ANISOU 848 O ILE A 161 21659 21099 16039 1752 -1114 3610 O ATOM 849 CB ILE A 161 -31.237 -1.780 -27.975 1.00153.83 C ANISOU 849 CB ILE A 161 21768 21550 15132 1895 -1369 3532 C ATOM 850 N GLN A 162 -29.988 -2.341 -24.526 1.00149.22 N ANISOU 850 N GLN A 162 20877 20441 15378 1650 -944 3092 N ATOM 851 CA GLN A 162 -29.613 -1.606 -23.323 1.00148.52 C ANISOU 851 CA GLN A 162 20686 20074 15670 1559 -801 3135 C ATOM 852 C GLN A 162 -28.537 -0.566 -23.617 1.00156.65 C ANISOU 852 C GLN A 162 21765 21070 16683 1507 -598 3431 C ATOM 853 O GLN A 162 -28.739 0.628 -23.397 1.00161.23 O ANISOU 853 O GLN A 162 22312 21454 17494 1499 -600 3657 O ATOM 854 CB GLN A 162 -29.129 -2.568 -22.238 1.00142.61 C ANISOU 854 CB GLN A 162 19856 19268 15062 1479 -690 2827 C ATOM 855 N ALA A 163 -27.396 -1.029 -24.115 1.00160.72 N ANISOU 855 N ALA A 163 22349 21768 16951 1472 -417 3424 N ATOM 856 CA ALA A 163 -26.288 -0.143 -24.451 1.00165.44 C ANISOU 856 CA ALA A 163 22982 22351 17527 1414 -198 3700 C ATOM 857 C ALA A 163 -25.345 -0.806 -25.448 1.00161.87 C ANISOU 857 C ALA A 163 22633 22193 16678 1421 -49 3700 C ATOM 858 O ALA A 163 -25.522 -1.971 -25.803 1.00161.89 O ANISOU 858 O ALA A 163 22674 22395 16441 1469 -119 3457 O ATOM 859 CB ALA A 163 -25.532 0.261 -23.194 1.00163.01 C ANISOU 859 CB ALA A 163 22552 21793 17592 1297 -31 3644 C ATOM 860 N ASN A 164 -24.344 -0.056 -25.897 1.00165.20 N ANISOU 860 N ASN A 164 23089 22633 17047 1371 166 3966 N ATOM 861 CA ASN A 164 -23.348 -0.585 -26.820 1.00164.88 C ANISOU 861 CA ASN A 164 23117 22835 16696 1341 344 3931 C ATOM 862 C ASN A 164 -22.381 -1.530 -26.115 1.00156.66 C ANISOU 862 C ASN A 164 22002 21825 15697 1297 518 3683 C ATOM 863 O ASN A 164 -22.517 -1.790 -24.920 1.00163.64 O ANISOU 863 O ASN A 164 22770 22509 16896 1248 469 3475 O ATOM 864 CB ASN A 164 -22.575 0.556 -27.485 1.00166.73 C ANISOU 864 CB ASN A 164 23376 23024 16950 1261 522 4244 C ATOM 865 N GLN A 165 -21.406 -2.041 -26.858 1.00139.04 N ANISOU 865 N GLN A 165 19813 19806 13209 1280 707 3644 N ATOM 866 CA GLN A 165 -20.419 -2.956 -26.296 1.00137.09 C ANISOU 866 CA GLN A 165 19482 19586 13021 1234 871 3394 C ATOM 867 C GLN A 165 -19.498 -2.237 -25.315 1.00136.63 C ANISOU 867 C GLN A 165 19287 19274 13353 1111 1044 3478 C ATOM 868 O GLN A 165 -19.094 -2.803 -24.298 1.00133.87 O ANISOU 868 O GLN A 165 18823 18805 13238 1057 1064 3239 O ATOM 869 CB GLN A 165 -19.597 -3.607 -27.410 1.00139.17 C ANISOU 869 CB GLN A 165 19816 20140 12922 1254 1045 3341 C ATOM 870 N TYR A 166 -19.174 -0.986 -25.625 1.00138.29 N ANISOU 870 N TYR A 166 19507 19400 13638 1069 1157 3823 N ATOM 871 CA TYR A 166 -18.285 -0.193 -24.786 1.00137.33 C ANISOU 871 CA TYR A 166 19250 19031 13897 949 1317 3918 C ATOM 872 C TYR A 166 -19.007 0.346 -23.555 1.00133.60 C ANISOU 872 C TYR A 166 18693 18255 13814 917 1144 3859 C ATOM 873 O TYR A 166 -18.482 0.294 -22.443 1.00130.93 O ANISOU 873 O TYR A 166 18229 17740 13780 836 1185 3700 O ATOM 874 CB TYR A 166 -17.687 0.964 -25.590 1.00140.24 C ANISOU 874 CB TYR A 166 19651 19401 14231 910 1509 4318 C ATOM 875 N ASN A 167 -20.215 0.861 -23.762 1.00129.36 N ANISOU 875 N ASN A 167 18222 17666 13262 986 947 3980 N ATOM 876 CA ASN A 167 -20.987 1.469 -22.684 1.00121.46 C ANISOU 876 CA ASN A 167 17144 16382 12625 967 793 3939 C ATOM 877 C ASN A 167 -21.473 0.451 -21.656 1.00115.55 C ANISOU 877 C ASN A 167 16337 15595 11972 975 660 3568 C ATOM 878 O ASN A 167 -21.771 0.805 -20.515 1.00114.10 O ANISOU 878 O ASN A 167 16063 15179 12109 933 597 3471 O ATOM 879 CB ASN A 167 -22.180 2.236 -23.258 1.00120.89 C ANISOU 879 CB ASN A 167 17149 16274 12511 1051 615 4167 C ATOM 880 CG ASN A 167 -21.762 3.298 -24.257 1.00122.93 C ANISOU 880 CG ASN A 167 17471 16553 12683 1046 738 4575 C ATOM 881 OD1 ASN A 167 -21.734 3.055 -25.464 1.00120.66 O ANISOU 881 OD1 ASN A 167 17299 16507 12039 1090 750 4670 O ATOM 882 ND2 ASN A 167 -21.433 4.484 -23.758 1.00126.17 N ANISOU 882 ND2 ASN A 167 17797 16690 13454 969 817 4764 N ATOM 883 N SER A 168 -21.552 -0.813 -22.063 1.00113.68 N ANISOU 883 N SER A 168 16150 15584 11457 1030 622 3361 N ATOM 884 CA SER A 168 -21.988 -1.875 -21.163 1.00105.97 C ANISOU 884 CA SER A 168 15121 14579 10562 1037 507 3027 C ATOM 885 C SER A 168 -20.801 -2.507 -20.443 1.00 98.61 C ANISOU 885 C SER A 168 14101 13628 9738 958 660 2844 C ATOM 886 O SER A 168 -20.969 -3.196 -19.437 1.00 95.82 O ANISOU 886 O SER A 168 13684 13193 9531 940 592 2603 O ATOM 887 CB SER A 168 -22.767 -2.945 -21.929 1.00105.04 C ANISOU 887 CB SER A 168 15088 14686 10136 1138 362 2881 C ATOM 888 OG SER A 168 -21.952 -3.573 -22.903 1.00104.84 O ANISOU 888 OG SER A 168 15127 14907 9800 1158 493 2867 O ATOM 889 N ARG A 169 -19.603 -2.268 -20.966 1.00 95.15 N ANISOU 889 N ARG A 169 13656 13265 9233 913 868 2969 N ATOM 890 CA ARG A 169 -18.386 -2.811 -20.375 1.00 90.37 C ANISOU 890 CA ARG A 169 12951 12643 8742 841 1017 2815 C ATOM 891 C ARG A 169 -18.077 -2.108 -19.057 1.00 89.36 C ANISOU 891 C ARG A 169 12707 12245 9002 748 1020 2800 C ATOM 892 O ARG A 169 -17.632 -2.736 -18.097 1.00 89.04 O ANISOU 892 O ARG A 169 12583 12142 9106 708 1016 2585 O ATOM 893 CB ARG A 169 -17.212 -2.675 -21.351 1.00 91.90 C ANISOU 893 CB ARG A 169 13153 12990 8774 818 1253 2966 C ATOM 894 CG ARG A 169 -16.025 -3.588 -21.057 1.00 91.10 C ANISOU 894 CG ARG A 169 12958 12950 8708 780 1395 2766 C ATOM 895 CD ARG A 169 -15.020 -2.937 -20.119 1.00 89.56 C ANISOU 895 CD ARG A 169 12616 12545 8867 666 1505 2801 C ATOM 896 NE ARG A 169 -13.860 -3.792 -19.884 1.00 88.61 N ANISOU 896 NE ARG A 169 12392 12483 8792 635 1632 2622 N ATOM 897 N ALA A 170 -18.318 -0.801 -19.020 1.00 89.63 N ANISOU 897 N ALA A 170 12735 12116 9203 717 1020 3026 N ATOM 898 CA ALA A 170 -18.090 -0.014 -17.815 1.00 85.55 C ANISOU 898 CA ALA A 170 12112 11335 9057 632 1014 3004 C ATOM 899 C ALA A 170 -19.195 -0.254 -16.793 1.00 81.35 C ANISOU 899 C ALA A 170 11576 10688 8645 662 820 2812 C ATOM 900 O ALA A 170 -18.962 -0.182 -15.587 1.00 79.64 O ANISOU 900 O ALA A 170 11278 10318 8665 603 800 2663 O ATOM 901 CB ALA A 170 -17.993 1.463 -18.156 1.00 89.56 C ANISOU 901 CB ALA A 170 12609 11691 9729 592 1082 3305 C ATOM 902 N THR A 171 -20.397 -0.536 -17.287 1.00 82.26 N ANISOU 902 N THR A 171 11776 10887 8592 754 679 2815 N ATOM 903 CA THR A 171 -21.544 -0.816 -16.429 1.00 80.72 C ANISOU 903 CA THR A 171 11571 10599 8500 788 509 2642 C ATOM 904 C THR A 171 -21.286 -2.056 -15.579 1.00 81.84 C ANISOU 904 C THR A 171 11674 10785 8636 771 492 2359 C ATOM 905 O THR A 171 -21.737 -2.147 -14.436 1.00 83.61 O ANISOU 905 O THR A 171 11853 10882 9032 752 419 2208 O ATOM 906 CB THR A 171 -22.830 -1.017 -17.257 1.00 80.26 C ANISOU 906 CB THR A 171 11597 10645 8252 893 357 2693 C ATOM 907 OG1 THR A 171 -23.039 0.122 -18.101 1.00 84.57 O ANISOU 907 OG1 THR A 171 12186 11158 8787 918 363 2986 O ATOM 908 CG2 THR A 171 -24.038 -1.196 -16.350 1.00 76.39 C ANISOU 908 CG2 THR A 171 11072 10037 7915 923 200 2530 C ATOM 909 N ALA A 172 -20.548 -3.005 -16.147 1.00 82.56 N ANISOU 909 N ALA A 172 11782 11057 8530 780 568 2292 N ATOM 910 CA ALA A 172 -20.178 -4.223 -15.438 1.00 77.02 C ANISOU 910 CA ALA A 172 11038 10395 7831 767 560 2046 C ATOM 911 C ALA A 172 -19.300 -3.907 -14.232 1.00 75.74 C ANISOU 911 C ALA A 172 10781 10078 7920 677 620 1982 C ATOM 912 O ALA A 172 -19.596 -4.330 -13.116 1.00 73.68 O ANISOU 912 O ALA A 172 10489 9734 7773 662 541 1817 O ATOM 913 CB ALA A 172 -19.467 -5.186 -16.374 1.00 76.74 C ANISOU 913 CB ALA A 172 11027 10570 7559 799 645 1997 C ATOM 914 N PHE A 173 -18.226 -3.156 -14.466 1.00 78.73 N ANISOU 914 N PHE A 173 11113 10420 8381 615 757 2118 N ATOM 915 CA PHE A 173 -17.294 -2.778 -13.406 1.00 79.48 C ANISOU 915 CA PHE A 173 11105 10370 8724 525 805 2059 C ATOM 916 C PHE A 173 -17.992 -2.040 -12.267 1.00 75.82 C ANISOU 916 C PHE A 173 10624 9709 8477 498 702 2011 C ATOM 917 O PHE A 173 -17.700 -2.275 -11.095 1.00 72.63 O ANISOU 917 O PHE A 173 10167 9226 8204 456 661 1850 O ATOM 918 CB PHE A 173 -16.167 -1.909 -13.968 1.00 85.72 C ANISOU 918 CB PHE A 173 11836 11132 9601 461 970 2243 C ATOM 919 CG PHE A 173 -15.158 -2.670 -14.779 1.00 90.96 C ANISOU 919 CG PHE A 173 12478 11973 10107 467 1108 2241 C ATOM 920 CD1 PHE A 173 -15.075 -4.050 -14.692 1.00 91.48 C ANISOU 920 CD1 PHE A 173 12551 12171 10038 514 1072 2041 C ATOM 921 CD2 PHE A 173 -14.285 -2.004 -15.624 1.00 96.39 C ANISOU 921 CD2 PHE A 173 13133 12690 10802 427 1286 2441 C ATOM 922 CE1 PHE A 173 -14.144 -4.751 -15.437 1.00 93.40 C ANISOU 922 CE1 PHE A 173 12764 12570 10155 527 1207 2018 C ATOM 923 CE2 PHE A 173 -13.353 -2.699 -16.370 1.00101.64 C ANISOU 923 CE2 PHE A 173 13769 13525 11323 436 1437 2428 C ATOM 924 CZ PHE A 173 -13.282 -4.074 -16.276 1.00 98.42 C ANISOU 924 CZ PHE A 173 13365 13248 10783 489 1395 2205 C ATOM 925 N ILE A 174 -18.911 -1.147 -12.620 1.00 74.51 N ANISOU 925 N ILE A 174 10501 9467 8342 527 658 2149 N ATOM 926 CA ILE A 174 -19.672 -0.399 -11.627 1.00 72.15 C ANISOU 926 CA ILE A 174 10183 8979 8253 513 571 2097 C ATOM 927 C ILE A 174 -20.552 -1.329 -10.799 1.00 66.68 C ANISOU 927 C ILE A 174 9514 8315 7508 554 457 1885 C ATOM 928 O ILE A 174 -20.549 -1.271 -9.569 1.00 63.72 O ANISOU 928 O ILE A 174 9101 7837 7273 516 423 1739 O ATOM 929 CB ILE A 174 -20.554 0.678 -12.286 1.00 75.93 C ANISOU 929 CB ILE A 174 10696 9371 8781 553 539 2296 C ATOM 930 CG1 ILE A 174 -19.690 1.681 -13.052 1.00 55.39 C ANISOU 930 CG1 ILE A 174 8070 6717 6259 505 664 2537 C ATOM 931 CG2 ILE A 174 -21.398 1.392 -11.240 1.00 52.69 C ANISOU 931 CG2 ILE A 174 7723 6229 6068 550 455 2210 C ATOM 932 CD1 ILE A 174 -20.487 2.730 -13.798 1.00 57.20 C ANISOU 932 CD1 ILE A 174 8338 6862 6534 549 632 2775 C ATOM 933 N LYS A 175 -21.298 -2.191 -11.485 1.00 65.71 N ANISOU 933 N LYS A 175 9452 8335 7179 630 400 1870 N ATOM 934 CA LYS A 175 -22.197 -3.132 -10.826 1.00 63.45 C ANISOU 934 CA LYS A 175 9180 8075 6853 668 301 1691 C ATOM 935 C LYS A 175 -21.429 -4.126 -9.960 1.00 62.22 C ANISOU 935 C LYS A 175 8993 7956 6692 628 319 1519 C ATOM 936 O LYS A 175 -21.862 -4.464 -8.860 1.00 57.31 O ANISOU 936 O LYS A 175 8359 7276 6139 618 268 1382 O ATOM 937 CB LYS A 175 -23.040 -3.879 -11.861 1.00 64.47 C ANISOU 937 CB LYS A 175 9368 8350 6778 752 231 1707 C ATOM 938 N ILE A 176 -20.290 -4.592 -10.466 1.00 69.01 N ANISOU 938 N ILE A 176 9836 8913 7471 610 397 1534 N ATOM 939 CA ILE A 176 -19.431 -5.501 -9.715 1.00 65.26 C ANISOU 939 CA ILE A 176 9317 8465 7013 577 410 1391 C ATOM 940 C ILE A 176 -18.895 -4.820 -8.461 1.00 62.62 C ANISOU 940 C ILE A 176 8929 7990 6876 504 409 1341 C ATOM 941 O ILE A 176 -18.904 -5.401 -7.375 1.00 62.76 O ANISOU 941 O ILE A 176 8937 7985 6925 491 353 1204 O ATOM 942 CB ILE A 176 -18.252 -6.005 -10.575 1.00 67.54 C ANISOU 942 CB ILE A 176 9579 8876 7209 575 508 1422 C ATOM 943 CG1 ILE A 176 -18.751 -6.977 -11.645 1.00 67.04 C ANISOU 943 CG1 ILE A 176 9572 8973 6927 654 492 1399 C ATOM 944 CG2 ILE A 176 -17.202 -6.683 -9.712 1.00 65.93 C ANISOU 944 CG2 ILE A 176 9302 8660 7087 534 518 1297 C ATOM 945 CD1 ILE A 176 -19.524 -8.148 -11.085 1.00 69.43 C ANISOU 945 CD1 ILE A 176 9892 9290 7199 692 386 1235 C ATOM 946 N THR A 177 -18.444 -3.580 -8.620 1.00 60.65 N ANISOU 946 N THR A 177 8644 7642 6757 457 466 1456 N ATOM 947 CA THR A 177 -17.907 -2.801 -7.509 1.00 57.68 C ANISOU 947 CA THR A 177 8208 7121 6585 384 457 1397 C ATOM 948 C THR A 177 -18.935 -2.612 -6.398 1.00 55.28 C ANISOU 948 C THR A 177 7936 6728 6338 394 369 1280 C ATOM 949 O THR A 177 -18.632 -2.816 -5.222 1.00 51.58 O ANISOU 949 O THR A 177 7450 6227 5923 360 325 1140 O ATOM 950 CB THR A 177 -17.425 -1.418 -7.977 1.00 58.79 C ANISOU 950 CB THR A 177 8302 7145 6890 333 533 1552 C ATOM 951 OG1 THR A 177 -16.381 -1.576 -8.946 1.00 60.23 O ANISOU 951 OG1 THR A 177 8445 7414 7024 315 643 1664 O ATOM 952 CG2 THR A 177 -16.903 -0.614 -6.800 1.00 59.62 C ANISOU 952 CG2 THR A 177 8338 7089 7226 257 506 1456 C ATOM 953 N VAL A 178 -20.146 -2.220 -6.781 1.00 57.65 N ANISOU 953 N VAL A 178 8282 6997 6624 444 344 1339 N ATOM 954 CA VAL A 178 -21.228 -2.008 -5.825 1.00 61.15 C ANISOU 954 CA VAL A 178 8746 7359 7130 461 283 1232 C ATOM 955 C VAL A 178 -21.502 -3.272 -5.015 1.00 61.96 C ANISOU 955 C VAL A 178 8875 7549 7118 477 238 1082 C ATOM 956 O VAL A 178 -21.609 -3.217 -3.791 1.00 67.13 O ANISOU 956 O VAL A 178 9530 8153 7824 452 213 956 O ATOM 957 CB VAL A 178 -22.526 -1.560 -6.531 1.00 64.55 C ANISOU 957 CB VAL A 178 9206 7759 7563 527 256 1328 C ATOM 958 CG1 VAL A 178 -23.708 -1.619 -5.574 1.00 45.55 C ANISOU 958 CG1 VAL A 178 6807 5294 5205 554 208 1198 C ATOM 959 CG2 VAL A 178 -22.365 -0.158 -7.096 1.00 47.77 C ANISOU 959 CG2 VAL A 178 7053 5505 5595 510 292 1485 C ATOM 960 N VAL A 179 -21.596 -4.406 -5.704 1.00 58.27 N ANISOU 960 N VAL A 179 8432 7213 6494 520 228 1096 N ATOM 961 CA VAL A 179 -21.823 -5.691 -5.048 1.00 56.33 C ANISOU 961 CA VAL A 179 8204 7038 6159 535 189 978 C ATOM 962 C VAL A 179 -20.736 -5.985 -4.015 1.00 53.92 C ANISOU 962 C VAL A 179 7876 6729 5883 481 184 891 C ATOM 963 O VAL A 179 -21.029 -6.415 -2.898 1.00 52.80 O ANISOU 963 O VAL A 179 7753 6579 5728 474 149 793 O ATOM 964 CB VAL A 179 -21.881 -6.843 -6.074 1.00 57.43 C ANISOU 964 CB VAL A 179 8359 7306 6156 585 180 999 C ATOM 965 CG1 VAL A 179 -21.856 -8.192 -5.372 1.00 56.47 C ANISOU 965 CG1 VAL A 179 8241 7233 5984 590 145 888 C ATOM 966 CG2 VAL A 179 -23.123 -6.715 -6.942 1.00 58.59 C ANISOU 966 CG2 VAL A 179 8533 7469 6260 645 147 1055 C ATOM 967 N TRP A 180 -19.484 -5.736 -4.387 1.00 55.22 N ANISOU 967 N TRP A 180 7993 6902 6085 445 219 935 N ATOM 968 CA TRP A 180 -18.365 -5.939 -3.474 1.00 58.22 C ANISOU 968 CA TRP A 180 8332 7274 6515 396 195 857 C ATOM 969 C TRP A 180 -18.412 -4.966 -2.299 1.00 63.47 C ANISOU 969 C TRP A 180 8994 7831 7290 349 162 780 C ATOM 970 O TRP A 180 -18.106 -5.339 -1.167 1.00 76.00 O ANISOU 970 O TRP A 180 10589 9427 8861 329 104 676 O ATOM 971 CB TRP A 180 -17.033 -5.802 -4.213 1.00 57.47 C ANISOU 971 CB TRP A 180 8163 7202 6470 366 251 922 C ATOM 972 CG TRP A 180 -16.637 -7.038 -4.957 1.00 58.97 C ANISOU 972 CG TRP A 180 8343 7513 6551 408 273 929 C ATOM 973 CD1 TRP A 180 -16.730 -7.253 -6.300 1.00 62.55 C ANISOU 973 CD1 TRP A 180 8806 8047 6914 448 341 1012 C ATOM 974 CD2 TRP A 180 -16.090 -8.238 -4.396 1.00 60.08 C ANISOU 974 CD2 TRP A 180 8460 7705 6661 420 223 842 C ATOM 975 NE1 TRP A 180 -16.271 -8.510 -6.613 1.00 64.91 N ANISOU 975 NE1 TRP A 180 9085 8441 7136 484 344 958 N ATOM 976 CE2 TRP A 180 -15.873 -9.136 -5.460 1.00 61.88 C ANISOU 976 CE2 TRP A 180 8676 8030 6806 468 271 861 C ATOM 977 CE3 TRP A 180 -15.762 -8.640 -3.098 1.00 59.38 C ANISOU 977 CE3 TRP A 180 8364 7592 6605 399 137 753 C ATOM 978 CZ2 TRP A 180 -15.342 -10.409 -5.266 1.00 61.98 C ANISOU 978 CZ2 TRP A 180 8656 8093 6802 495 238 789 C ATOM 979 CZ3 TRP A 180 -15.235 -9.904 -2.907 1.00 59.73 C ANISOU 979 CZ3 TRP A 180 8382 7691 6620 427 97 708 C ATOM 980 CH2 TRP A 180 -15.031 -10.774 -3.985 1.00 61.72 C ANISOU 980 CH2 TRP A 180 8609 8017 6824 474 149 725 C ATOM 981 N LEU A 181 -18.798 -3.723 -2.570 1.00 57.67 N ANISOU 981 N LEU A 181 8251 6993 6667 335 195 829 N ATOM 982 CA LEU A 181 -18.906 -2.712 -1.523 1.00 52.98 C ANISOU 982 CA LEU A 181 7650 6281 6198 295 168 733 C ATOM 983 C LEU A 181 -20.028 -3.047 -0.549 1.00 51.27 C ANISOU 983 C LEU A 181 7500 6078 5903 327 137 623 C ATOM 984 O LEU A 181 -19.920 -2.787 0.650 1.00 44.56 O ANISOU 984 O LEU A 181 6664 5199 5070 298 101 492 O ATOM 985 CB LEU A 181 -19.130 -1.329 -2.132 1.00 51.74 C ANISOU 985 CB LEU A 181 7461 5989 6209 280 214 823 C ATOM 986 CG LEU A 181 -17.915 -0.721 -2.833 1.00 46.98 C ANISOU 986 CG LEU A 181 6779 5339 5734 226 262 927 C ATOM 987 CD1 LEU A 181 -18.260 0.626 -3.439 1.00 48.26 C ANISOU 987 CD1 LEU A 181 6914 5352 6069 216 309 1044 C ATOM 988 CD2 LEU A 181 -16.750 -0.591 -1.865 1.00 47.50 C ANISOU 988 CD2 LEU A 181 6782 5370 5897 156 216 802 C ATOM 989 N ILE A 182 -21.108 -3.620 -1.073 1.00 50.06 N ANISOU 989 N ILE A 182 7386 5974 5662 385 154 672 N ATOM 990 CA ILE A 182 -22.204 -4.098 -0.239 1.00 50.34 C ANISOU 990 CA ILE A 182 7470 6031 5627 415 146 585 C ATOM 991 C ILE A 182 -21.712 -5.212 0.676 1.00 49.10 C ANISOU 991 C ILE A 182 7344 5967 5347 402 108 513 C ATOM 992 O ILE A 182 -22.030 -5.244 1.864 1.00 47.67 O ANISOU 992 O ILE A 182 7201 5789 5122 392 99 411 O ATOM 993 CB ILE A 182 -23.384 -4.614 -1.090 1.00 42.48 C ANISOU 993 CB ILE A 182 6486 5068 4584 478 160 656 C ATOM 994 CG1 ILE A 182 -24.041 -3.461 -1.850 1.00 43.22 C ANISOU 994 CG1 ILE A 182 6556 5064 4803 502 179 732 C ATOM 995 CG2 ILE A 182 -24.414 -5.315 -0.217 1.00 42.05 C ANISOU 995 CG2 ILE A 182 6465 5044 4467 500 166 573 C ATOM 996 CD1 ILE A 182 -25.102 -3.905 -2.833 1.00 42.99 C ANISOU 996 CD1 ILE A 182 6529 5074 4730 566 164 811 C ATOM 997 N SER A 183 -20.916 -6.114 0.110 1.00 50.84 N ANISOU 997 N SER A 183 7546 6263 5509 405 88 569 N ATOM 998 CA SER A 183 -20.402 -7.266 0.840 1.00 51.49 C ANISOU 998 CA SER A 183 7647 6424 5494 402 41 528 C ATOM 999 C SER A 183 -19.451 -6.863 1.964 1.00 53.04 C ANISOU 999 C SER A 183 7839 6607 5708 353 -16 444 C ATOM 1000 O SER A 183 -19.422 -7.498 3.018 1.00 57.78 O ANISOU 1000 O SER A 183 8483 7257 6213 352 -62 390 O ATOM 1001 CB SER A 183 -19.699 -8.225 -0.122 1.00 51.77 C ANISOU 1001 CB SER A 183 7645 6524 5502 423 35 596 C ATOM 1002 OG SER A 183 -20.573 -8.619 -1.165 1.00 51.41 O ANISOU 1002 OG SER A 183 7608 6502 5424 470 70 652 O ATOM 1003 N ILE A 184 -18.672 -5.810 1.735 1.00 54.28 N ANISOU 1003 N ILE A 184 7940 6696 5989 312 -18 436 N ATOM 1004 CA ILE A 184 -17.743 -5.318 2.746 1.00 54.44 C ANISOU 1004 CA ILE A 184 7939 6692 6053 262 -90 336 C ATOM 1005 C ILE A 184 -18.495 -4.754 3.948 1.00 58.37 C ANISOU 1005 C ILE A 184 8505 7166 6508 255 -102 211 C ATOM 1006 O ILE A 184 -18.190 -5.089 5.093 1.00 62.60 O ANISOU 1006 O ILE A 184 9082 7758 6943 244 -174 122 O ATOM 1007 CB ILE A 184 -16.806 -4.232 2.180 1.00 53.99 C ANISOU 1007 CB ILE A 184 7789 6542 6182 211 -79 354 C ATOM 1008 CG1 ILE A 184 -15.917 -4.813 1.080 1.00 50.20 C ANISOU 1008 CG1 ILE A 184 7236 6105 5731 214 -50 466 C ATOM 1009 CG2 ILE A 184 -15.948 -3.638 3.285 1.00 55.79 C ANISOU 1009 CG2 ILE A 184 7987 6731 6480 156 -172 220 C ATOM 1010 CD1 ILE A 184 -15.001 -3.795 0.435 1.00 47.39 C ANISOU 1010 CD1 ILE A 184 6780 5661 5566 160 -9 514 C ATOM 1011 N GLY A 185 -19.485 -3.908 3.677 1.00 58.58 N ANISOU 1011 N GLY A 185 8541 7111 6605 268 -32 204 N ATOM 1012 CA GLY A 185 -20.272 -3.278 4.723 1.00 60.60 C ANISOU 1012 CA GLY A 185 8848 7334 6843 269 -18 70 C ATOM 1013 C GLY A 185 -21.023 -4.258 5.602 1.00 60.91 C ANISOU 1013 C GLY A 185 8974 7482 6687 300 -6 37 C ATOM 1014 O GLY A 185 -21.285 -3.982 6.772 1.00 63.55 O ANISOU 1014 O GLY A 185 9364 7839 6943 293 -10 -93 O ATOM 1015 N ILE A 186 -21.373 -5.407 5.034 1.00 59.56 N ANISOU 1015 N ILE A 186 8813 7378 6439 334 15 152 N ATOM 1016 CA ILE A 186 -22.069 -6.450 5.776 1.00 59.40 C ANISOU 1016 CA ILE A 186 8863 7448 6261 359 37 154 C ATOM 1017 C ILE A 186 -21.076 -7.285 6.580 1.00 61.23 C ANISOU 1017 C ILE A 186 9129 7770 6365 343 -56 151 C ATOM 1018 O ILE A 186 -21.390 -7.769 7.666 1.00 64.49 O ANISOU 1018 O ILE A 186 9618 8256 6628 347 -56 119 O ATOM 1019 CB ILE A 186 -22.883 -7.364 4.830 1.00 57.68 C ANISOU 1019 CB ILE A 186 8627 7243 6046 400 86 270 C ATOM 1020 CG1 ILE A 186 -23.930 -6.545 4.074 1.00 57.54 C ANISOU 1020 CG1 ILE A 186 8573 7141 6149 425 155 278 C ATOM 1021 CG2 ILE A 186 -23.562 -8.487 5.599 1.00 59.05 C ANISOU 1021 CG2 ILE A 186 8857 7489 6089 416 115 287 C ATOM 1022 CD1 ILE A 186 -24.785 -7.365 3.134 1.00 58.14 C ANISOU 1022 CD1 ILE A 186 8626 7230 6235 466 182 370 C ATOM 1023 N ALA A 187 -19.866 -7.431 6.051 1.00 61.77 N ANISOU 1023 N ALA A 187 9137 7835 6496 326 -132 192 N ATOM 1024 CA ALA A 187 -18.855 -8.276 6.677 1.00 62.72 C ANISOU 1024 CA ALA A 187 9269 8031 6532 320 -238 204 C ATOM 1025 C ALA A 187 -18.010 -7.524 7.702 1.00 65.67 C ANISOU 1025 C ALA A 187 9651 8413 6887 281 -337 81 C ATOM 1026 O ALA A 187 -17.411 -8.135 8.588 1.00 71.05 O ANISOU 1026 O ALA A 187 10370 9173 7452 281 -440 70 O ATOM 1027 CB ALA A 187 -17.960 -8.888 5.616 1.00 60.91 C ANISOU 1027 CB ALA A 187 8953 7795 6396 328 -267 296 C ATOM 1028 N ILE A 188 -17.965 -6.202 7.583 1.00 63.97 N ANISOU 1028 N ILE A 188 9400 8111 6796 249 -319 -14 N ATOM 1029 CA ILE A 188 -17.102 -5.393 8.442 1.00 64.14 C ANISOU 1029 CA ILE A 188 9408 8119 6841 205 -425 -157 C ATOM 1030 C ILE A 188 -17.573 -5.178 9.898 1.00 63.29 C ANISOU 1030 C ILE A 188 9413 8085 6551 207 -454 -300 C ATOM 1031 O ILE A 188 -16.787 -4.707 10.720 1.00 64.52 O ANISOU 1031 O ILE A 188 9570 8259 6686 177 -575 -431 O ATOM 1032 CB ILE A 188 -16.850 -4.004 7.803 1.00 63.35 C ANISOU 1032 CB ILE A 188 9217 7876 6976 164 -395 -214 C ATOM 1033 CG1 ILE A 188 -15.433 -3.520 8.131 1.00 63.37 C ANISOU 1033 CG1 ILE A 188 9137 7847 7093 111 -528 -299 C ATOM 1034 CG2 ILE A 188 -17.911 -2.995 8.232 1.00 49.09 C ANISOU 1034 CG2 ILE A 188 7460 6005 5188 168 -318 -332 C ATOM 1035 CD1 ILE A 188 -14.969 -2.356 7.290 1.00 63.75 C ANISOU 1035 CD1 ILE A 188 9067 7741 7414 62 -491 -300 C ATOM 1036 N PRO A 189 -18.840 -5.504 10.235 1.00 62.11 N ANISOU 1036 N PRO A 189 9352 7981 6265 242 -344 -286 N ATOM 1037 CA PRO A 189 -19.094 -5.475 11.682 1.00 62.73 C ANISOU 1037 CA PRO A 189 9544 8164 6126 245 -372 -409 C ATOM 1038 C PRO A 189 -18.274 -6.489 12.483 1.00 65.38 C ANISOU 1038 C PRO A 189 9936 8632 6272 251 -510 -358 C ATOM 1039 O PRO A 189 -18.089 -6.301 13.685 1.00 65.49 O ANISOU 1039 O PRO A 189 10037 8741 6105 246 -586 -476 O ATOM 1040 CB PRO A 189 -20.584 -5.804 11.775 1.00 60.68 C ANISOU 1040 CB PRO A 189 9349 7929 5775 281 -205 -367 C ATOM 1041 CG PRO A 189 -21.149 -5.260 10.528 1.00 60.19 C ANISOU 1041 CG PRO A 189 9197 7733 5941 288 -110 -323 C ATOM 1042 CD PRO A 189 -20.105 -5.499 9.474 1.00 61.56 C ANISOU 1042 CD PRO A 189 9277 7857 6256 272 -191 -215 C ATOM 1043 N VAL A 190 -17.790 -7.541 11.829 1.00 67.73 N ANISOU 1043 N VAL A 190 10187 8938 6610 266 -549 -190 N ATOM 1044 CA VAL A 190 -17.044 -8.589 12.523 1.00 69.77 C ANISOU 1044 CA VAL A 190 10487 9303 6718 281 -685 -113 C ATOM 1045 C VAL A 190 -15.638 -8.154 12.976 1.00 75.37 C ANISOU 1045 C VAL A 190 11146 10025 7466 253 -884 -214 C ATOM 1046 O VAL A 190 -15.305 -8.313 14.150 1.00 81.15 O ANISOU 1046 O VAL A 190 11964 10869 8001 258 -1007 -268 O ATOM 1047 CB VAL A 190 -16.924 -9.863 11.655 1.00 64.61 C ANISOU 1047 CB VAL A 190 9780 8632 6136 311 -670 82 C ATOM 1048 CG1 VAL A 190 -16.099 -10.917 12.373 1.00 63.94 C ANISOU 1048 CG1 VAL A 190 9726 8634 5933 333 -824 168 C ATOM 1049 CG2 VAL A 190 -18.299 -10.401 11.314 1.00 61.19 C ANISOU 1049 CG2 VAL A 190 9393 8191 5666 337 -500 173 C ATOM 1050 N PRO A 191 -14.806 -7.607 12.065 1.00 79.00 N ANISOU 1050 N PRO A 191 11463 10376 8177 223 -919 -236 N ATOM 1051 CA PRO A 191 -13.470 -7.250 12.558 1.00 78.87 C ANISOU 1051 CA PRO A 191 11381 10368 8219 192 -1115 -335 C ATOM 1052 C PRO A 191 -13.473 -6.032 13.481 1.00 79.46 C ANISOU 1052 C PRO A 191 11498 10446 8247 156 -1176 -562 C ATOM 1053 O PRO A 191 -12.569 -5.892 14.305 1.00 80.77 O ANISOU 1053 O PRO A 191 11658 10668 8364 141 -1367 -667 O ATOM 1054 CB PRO A 191 -12.693 -6.953 11.274 1.00 77.96 C ANISOU 1054 CB PRO A 191 11092 10127 8401 164 -1092 -290 C ATOM 1055 CG PRO A 191 -13.726 -6.497 10.318 1.00 76.62 C ANISOU 1055 CG PRO A 191 10924 9873 8317 165 -892 -249 C ATOM 1056 CD PRO A 191 -14.944 -7.319 10.624 1.00 78.45 C ANISOU 1056 CD PRO A 191 11286 10185 8338 214 -797 -168 C ATOM 1057 N ILE A 192 -14.473 -5.168 13.342 1.00 79.51 N ANISOU 1057 N ILE A 192 11539 10388 8281 147 -1026 -647 N ATOM 1058 CA ILE A 192 -14.578 -3.982 14.186 1.00 82.81 C ANISOU 1058 CA ILE A 192 11995 10794 8676 118 -1065 -887 C ATOM 1059 C ILE A 192 -14.918 -4.368 15.623 1.00 83.67 C ANISOU 1059 C ILE A 192 12271 11083 8436 148 -1127 -969 C ATOM 1060 O ILE A 192 -14.298 -3.881 16.570 1.00 91.08 O ANISOU 1060 O ILE A 192 13237 12079 9288 129 -1288 -1151 O ATOM 1061 CB ILE A 192 -15.638 -2.999 13.652 1.00 84.56 C ANISOU 1061 CB ILE A 192 12205 10889 9037 111 -878 -950 C ATOM 1062 CG1 ILE A 192 -15.207 -2.447 12.291 1.00 83.89 C ANISOU 1062 CG1 ILE A 192 11961 10629 9285 77 -832 -872 C ATOM 1063 CG2 ILE A 192 -15.855 -1.856 14.631 1.00 88.23 C ANISOU 1063 CG2 ILE A 192 12718 11342 9464 92 -907 -1220 C ATOM 1064 CD1 ILE A 192 -16.201 -1.485 11.679 1.00 85.31 C ANISOU 1064 CD1 ILE A 192 12119 10669 9624 77 -668 -901 C ATOM 1065 N LYS A 193 -15.900 -5.250 15.779 1.00 78.79 N ANISOU 1065 N LYS A 193 11762 10556 7617 193 -999 -831 N ATOM 1066 CA LYS A 193 -16.283 -5.744 17.096 1.00 78.23 C ANISOU 1066 CA LYS A 193 11861 10671 7193 223 -1026 -859 C ATOM 1067 C LYS A 193 -15.183 -6.624 17.682 1.00 80.89 C ANISOU 1067 C LYS A 193 12220 11124 7390 236 -1250 -774 C ATOM 1068 O LYS A 193 -14.736 -6.408 18.809 1.00 79.58 O ANISOU 1068 O LYS A 193 12139 11082 7017 237 -1404 -908 O ATOM 1069 CB LYS A 193 -17.598 -6.521 17.019 1.00 74.96 C ANISOU 1069 CB LYS A 193 11533 10304 6646 261 -817 -703 C ATOM 1070 N GLY A 194 -14.750 -7.615 16.909 1.00 85.84 N ANISOU 1070 N GLY A 194 12769 11712 8135 251 -1274 -559 N ATOM 1071 CA GLY A 194 -13.667 -8.489 17.321 1.00 91.27 C ANISOU 1071 CA GLY A 194 13447 12478 8752 271 -1489 -460 C ATOM 1072 C GLY A 194 -14.123 -9.640 18.195 1.00 92.82 C ANISOU 1072 C GLY A 194 13801 12831 8636 319 -1493 -297 C ATOM 1073 O GLY A 194 -15.277 -9.689 18.623 1.00 91.60 O ANISOU 1073 O GLY A 194 13772 12741 8290 331 -1323 -284 O ATOM 1074 N ILE A 195 -13.212 -10.570 18.460 1.00 96.46 N ANISOU 1074 N ILE A 195 14246 13344 9061 347 -1682 -161 N ATOM 1075 CA ILE A 195 -13.509 -11.713 19.315 1.00104.69 C ANISOU 1075 CA ILE A 195 15433 14525 9820 394 -1710 27 C ATOM 1076 C ILE A 195 -13.114 -11.433 20.762 1.00112.20 C ANISOU 1076 C ILE A 195 16524 15661 10446 405 -1899 -80 C ATOM 1077 O ILE A 195 -12.306 -10.543 21.033 1.00122.63 O ANISOU 1077 O ILE A 195 17793 16988 11812 380 -2071 -291 O ATOM 1078 CB ILE A 195 -12.799 -12.991 18.819 1.00111.02 C ANISOU 1078 CB ILE A 195 16145 15273 10765 431 -1814 259 C ATOM 1079 CG1 ILE A 195 -11.486 -12.645 18.110 1.00120.34 C ANISOU 1079 CG1 ILE A 195 17128 16345 12250 414 -1977 177 C ATOM 1080 CG2 ILE A 195 -13.701 -13.759 17.867 1.00109.87 C ANISOU 1080 CG2 ILE A 195 15969 15025 10754 443 -1589 430 C ATOM 1081 CD1 ILE A 195 -10.345 -12.281 19.039 1.00131.66 C ANISOU 1081 CD1 ILE A 195 18557 17870 13596 415 -2267 60 C ATOM 1082 N GLU A 196 -13.692 -12.192 21.687 1.00111.69 N ANISOU 1082 N GLU A 196 16636 15749 10053 441 -1866 67 N ATOM 1083 CA GLU A 196 -13.440 -11.996 23.110 1.00116.39 C ANISOU 1083 CA GLU A 196 17397 16555 10271 459 -2029 -17 C ATOM 1084 C GLU A 196 -11.993 -12.316 23.473 1.00117.09 C ANISOU 1084 C GLU A 196 17429 16685 10376 482 -2376 7 C ATOM 1085 O GLU A 196 -11.545 -13.453 23.333 1.00120.93 O ANISOU 1085 O GLU A 196 17881 17151 10916 522 -2472 255 O ATOM 1086 CB GLU A 196 -14.391 -12.857 23.945 1.00120.59 C ANISOU 1086 CB GLU A 196 18128 17241 10449 493 -1892 187 C ATOM 1087 N THR A 197 -11.270 -11.303 23.939 1.00114.10 N ANISOU 1087 N THR A 197 17027 16352 9973 459 -2569 -261 N ATOM 1088 CA THR A 197 -9.873 -11.471 24.320 1.00113.08 C ANISOU 1088 CA THR A 197 16824 16262 9879 478 -2920 -277 C ATOM 1089 C THR A 197 -9.744 -11.818 25.799 1.00116.70 C ANISOU 1089 C THR A 197 17493 16975 9871 526 -3116 -244 C ATOM 1090 O THR A 197 -9.063 -11.122 26.553 1.00120.78 O ANISOU 1090 O THR A 197 18034 17598 10258 520 -3358 -468 O ATOM 1091 CB THR A 197 -9.052 -10.201 24.026 1.00111.97 C ANISOU 1091 CB THR A 197 16521 16023 9997 422 -3056 -589 C ATOM 1092 N ASN A 201 -7.374 -14.622 33.350 1.00170.63 N ANISOU 1092 N ASN A 201 25022 25220 14591 709 -4336 372 N ATOM 1093 CA ASN A 201 -6.474 -14.080 32.339 1.00168.07 C ANISOU 1093 CA ASN A 201 24499 24663 14697 717 -4530 169 C ATOM 1094 C ASN A 201 -6.490 -14.908 31.059 1.00165.92 C ANISOU 1094 C ASN A 201 24112 24130 14799 761 -4447 410 C ATOM 1095 O ASN A 201 -5.675 -15.816 30.891 1.00169.55 O ANISOU 1095 O ASN A 201 24453 24523 15446 813 -4642 638 O ATOM 1096 CB ASN A 201 -5.049 -13.995 32.888 1.00169.82 C ANISOU 1096 CB ASN A 201 24594 24953 14978 730 -4943 86 C ATOM 1097 N PRO A 202 -7.424 -14.595 30.148 1.00160.57 N ANISOU 1097 N PRO A 202 23467 23302 14239 740 -4158 354 N ATOM 1098 CA PRO A 202 -7.557 -15.315 28.876 1.00156.04 C ANISOU 1098 CA PRO A 202 22801 22481 14004 770 -4054 559 C ATOM 1099 C PRO A 202 -6.377 -15.073 27.937 1.00153.32 C ANISOU 1099 C PRO A 202 22170 21929 14158 755 -4245 445 C ATOM 1100 O PRO A 202 -6.233 -13.980 27.389 1.00148.26 O ANISOU 1100 O PRO A 202 21398 21186 13746 690 -4193 151 O ATOM 1101 CB PRO A 202 -8.852 -14.746 28.285 1.00156.30 C ANISOU 1101 CB PRO A 202 22877 22439 14072 713 -3648 452 C ATOM 1102 CG PRO A 202 -8.994 -13.401 28.910 1.00156.95 C ANISOU 1102 CG PRO A 202 23045 22651 13939 675 -3670 80 C ATOM 1103 CD PRO A 202 -8.438 -13.536 30.295 1.00161.88 C ANISOU 1103 CD PRO A 202 23760 23528 14218 690 -3909 86 C ATOM 1104 N ASN A 203 -5.544 -16.093 27.759 1.00156.08 N ANISOU 1104 N ASN A 203 22406 22207 14692 813 -4447 683 N ATOM 1105 CA ASN A 203 -4.401 -16.002 26.858 1.00154.58 C ANISOU 1105 CA ASN A 203 21919 21818 14996 803 -4601 604 C ATOM 1106 C ASN A 203 -4.784 -16.386 25.434 1.00145.45 C ANISOU 1106 C ASN A 203 20599 20420 14245 779 -4301 704 C ATOM 1107 O ASN A 203 -4.524 -15.641 24.488 1.00141.89 O ANISOU 1107 O ASN A 203 19960 19816 14136 720 -4208 507 O ATOM 1108 CB ASN A 203 -3.258 -16.891 27.352 1.00159.10 C ANISOU 1108 CB ASN A 203 22427 22426 15600 885 -4979 790 C ATOM 1109 N ASN A 204 -5.404 -17.552 25.289 1.00141.10 N ANISOU 1109 N ASN A 204 20123 19836 13654 823 -4153 1012 N ATOM 1110 CA ASN A 204 -5.871 -18.016 23.988 1.00136.66 C ANISOU 1110 CA ASN A 204 19428 19061 13435 807 -3870 1108 C ATOM 1111 C ASN A 204 -7.222 -17.412 23.629 1.00129.16 C ANISOU 1111 C ASN A 204 18584 18107 12385 745 -3509 1012 C ATOM 1112 O ASN A 204 -7.741 -16.557 24.346 1.00130.65 O ANISOU 1112 O ASN A 204 18926 18441 12272 712 -3469 847 O ATOM 1113 CB ASN A 204 -5.960 -19.544 23.963 1.00142.96 C ANISOU 1113 CB ASN A 204 20243 19799 14275 879 -3874 1464 C ATOM 1114 CG ASN A 204 -4.607 -20.209 24.120 1.00152.65 C ANISOU 1114 CG ASN A 204 21322 20985 15694 950 -4217 1569 C ATOM 1115 OD1 ASN A 204 -3.649 -19.593 24.586 1.00160.59 O ANISOU 1115 OD1 ASN A 204 22264 22063 16688 951 -4496 1404 O ATOM 1116 ND2 ASN A 204 -4.522 -21.476 23.729 1.00154.66 N ANISOU 1116 ND2 ASN A 204 21507 21108 16149 1010 -4205 1836 N ATOM 1117 N ILE A 205 -7.789 -17.864 22.516 1.00120.97 N ANISOU 1117 N ILE A 205 17457 16900 11607 733 -3254 1106 N ATOM 1118 CA ILE A 205 -9.076 -17.358 22.057 1.00114.16 C ANISOU 1118 CA ILE A 205 16665 16011 10700 680 -2920 1030 C ATOM 1119 C ILE A 205 -9.812 -18.397 21.220 1.00105.94 C ANISOU 1119 C ILE A 205 15589 14832 9831 696 -2694 1248 C ATOM 1120 O ILE A 205 -9.193 -19.192 20.514 1.00101.98 O ANISOU 1120 O ILE A 205 14933 14194 9621 730 -2756 1363 O ATOM 1121 CB ILE A 205 -8.912 -16.071 21.226 1.00113.75 C ANISOU 1121 CB ILE A 205 16473 15865 10881 614 -2839 741 C ATOM 1122 N THR A 206 -11.138 -18.388 21.312 1.00102.89 N ANISOU 1122 N THR A 206 15337 14479 9277 672 -2433 1291 N ATOM 1123 CA THR A 206 -11.971 -19.267 20.501 1.00 97.25 C ANISOU 1123 CA THR A 206 14586 13630 8735 676 -2206 1463 C ATOM 1124 C THR A 206 -12.593 -18.485 19.351 1.00 94.29 C ANISOU 1124 C THR A 206 14115 13143 8569 624 -1976 1282 C ATOM 1125 O THR A 206 -13.594 -17.792 19.531 1.00 94.18 O ANISOU 1125 O THR A 206 14197 13183 8403 586 -1791 1183 O ATOM 1126 CB THR A 206 -13.084 -19.926 21.337 1.00 95.69 C ANISOU 1126 CB THR A 206 14584 13528 8246 684 -2061 1668 C ATOM 1127 OG1 THR A 206 -13.877 -18.911 21.967 1.00 95.38 O ANISOU 1127 OG1 THR A 206 14687 13631 7920 644 -1928 1504 O ATOM 1128 CG2 THR A 206 -12.482 -20.830 22.402 1.00 98.57 C ANISOU 1128 CG2 THR A 206 15047 13992 8412 743 -2286 1901 C ATOM 1129 N CYS A 207 -11.990 -18.598 18.172 1.00 92.06 N ANISOU 1129 N CYS A 207 13641 12707 8633 627 -1988 1243 N ATOM 1130 CA CYS A 207 -12.430 -17.837 17.009 1.00 89.61 C ANISOU 1130 CA CYS A 207 13231 12294 8524 583 -1799 1085 C ATOM 1131 C CYS A 207 -13.799 -18.300 16.528 1.00 88.77 C ANISOU 1131 C CYS A 207 13171 12131 8426 575 -1542 1178 C ATOM 1132 O CYS A 207 -13.904 -19.183 15.676 1.00 86.44 O ANISOU 1132 O CYS A 207 12786 11716 8341 596 -1480 1286 O ATOM 1133 CB CYS A 207 -11.409 -17.952 15.877 1.00 86.49 C ANISOU 1133 CB CYS A 207 12625 11765 8471 593 -1868 1043 C ATOM 1134 SG CYS A 207 -11.657 -16.778 14.530 1.00 75.88 S ANISOU 1134 SG CYS A 207 11162 10323 7344 538 -1684 841 S ATOM 1135 N VAL A 208 -14.845 -17.697 17.082 1.00 92.00 N ANISOU 1135 N VAL A 208 13713 12626 8618 544 -1396 1121 N ATOM 1136 CA VAL A 208 -16.211 -18.046 16.718 1.00 88.54 C ANISOU 1136 CA VAL A 208 13311 12140 8190 532 -1152 1195 C ATOM 1137 C VAL A 208 -17.184 -16.916 17.034 1.00 86.40 C ANISOU 1137 C VAL A 208 13125 11937 7767 493 -989 1035 C ATOM 1138 O VAL A 208 -17.060 -16.249 18.061 1.00 87.53 O ANISOU 1138 O VAL A 208 13378 12213 7666 485 -1049 939 O ATOM 1139 CB VAL A 208 -16.677 -19.323 17.442 1.00 91.59 C ANISOU 1139 CB VAL A 208 13796 12558 8446 559 -1129 1449 C ATOM 1140 N LEU A 209 -18.149 -16.702 16.146 1.00 82.80 N ANISOU 1140 N LEU A 209 12613 11388 7460 474 -791 996 N ATOM 1141 CA LEU A 209 -19.181 -15.699 16.376 1.00 83.04 C ANISOU 1141 CA LEU A 209 12703 11458 7389 445 -620 854 C ATOM 1142 C LEU A 209 -20.090 -16.141 17.516 1.00 87.93 C ANISOU 1142 C LEU A 209 13474 12193 7740 448 -504 960 C ATOM 1143 O LEU A 209 -20.716 -17.198 17.449 1.00 91.19 O ANISOU 1143 O LEU A 209 13894 12570 8186 455 -407 1150 O ATOM 1144 CB LEU A 209 -20.000 -15.453 15.107 1.00 73.58 C ANISOU 1144 CB LEU A 209 11398 10127 6433 433 -456 810 C ATOM 1145 CG LEU A 209 -19.272 -14.838 13.911 1.00 62.62 C ANISOU 1145 CG LEU A 209 9870 8635 5288 426 -523 701 C ATOM 1146 CD1 LEU A 209 -20.248 -14.567 12.775 1.00 60.08 C ANISOU 1146 CD1 LEU A 209 9472 8209 5147 419 -358 670 C ATOM 1147 CD2 LEU A 209 -18.551 -13.564 14.317 1.00 60.75 C ANISOU 1147 CD2 LEU A 209 9641 8441 5001 404 -622 513 C ATOM 1148 N THR A 210 -20.153 -15.329 18.566 1.00 90.37 N ANISOU 1148 N THR A 210 13903 12644 7791 439 -508 832 N ATOM 1149 CA THR A 210 -20.938 -15.664 19.747 1.00 90.48 C ANISOU 1149 CA THR A 210 14076 12801 7501 443 -388 922 C ATOM 1150 C THR A 210 -22.310 -14.996 19.699 1.00 90.66 C ANISOU 1150 C THR A 210 14108 12817 7522 421 -124 810 C ATOM 1151 O THR A 210 -22.439 -13.858 19.250 1.00 91.92 O ANISOU 1151 O THR A 210 14208 12924 7795 408 -91 589 O ATOM 1152 CB THR A 210 -20.210 -15.243 21.041 1.00 95.16 C ANISOU 1152 CB THR A 210 14813 13584 7760 454 -550 843 C ATOM 1153 OG1 THR A 210 -18.827 -15.611 20.955 1.00 97.03 O ANISOU 1153 OG1 THR A 210 15002 13807 8059 475 -826 895 O ATOM 1154 CG2 THR A 210 -20.835 -15.913 22.254 1.00100.05 C ANISOU 1154 CG2 THR A 210 15608 14368 8038 466 -450 1013 C ATOM 1155 N LYS A 211 -23.332 -15.714 20.157 1.00 90.35 N ANISOU 1155 N LYS A 211 14133 12817 7376 419 66 969 N ATOM 1156 CA LYS A 211 -24.687 -15.175 20.210 1.00 88.76 C ANISOU 1156 CA LYS A 211 13932 12616 7178 402 331 876 C ATOM 1157 C LYS A 211 -24.778 -14.016 21.197 1.00 90.96 C ANISOU 1157 C LYS A 211 14325 13048 7189 403 368 645 C ATOM 1158 O LYS A 211 -25.496 -13.042 20.965 1.00 92.41 O ANISOU 1158 O LYS A 211 14461 13190 7461 396 509 448 O ATOM 1159 CB LYS A 211 -25.688 -16.268 20.595 1.00 88.26 C ANISOU 1159 CB LYS A 211 13907 12570 7058 394 528 1113 C ATOM 1160 CG LYS A 211 -27.111 -15.763 20.786 1.00 85.94 C ANISOU 1160 CG LYS A 211 13606 12289 6757 378 816 1023 C ATOM 1161 CD LYS A 211 -28.002 -16.810 21.433 1.00 84.61 C ANISOU 1161 CD LYS A 211 13495 12170 6482 363 1018 1265 C ATOM 1162 CE LYS A 211 -29.365 -16.229 21.777 1.00 82.81 C ANISOU 1162 CE LYS A 211 13259 11980 6224 348 1315 1156 C ATOM 1163 NZ LYS A 211 -30.258 -17.233 22.418 1.00 84.01 N ANISOU 1163 NZ LYS A 211 13455 12179 6288 326 1539 1401 N ATOM 1164 N GLU A 212 -24.038 -14.123 22.296 1.00 91.26 N ANISOU 1164 N GLU A 212 14510 13260 6905 417 230 663 N ATOM 1165 CA GLU A 212 -24.060 -13.107 23.343 1.00 94.16 C ANISOU 1165 CA GLU A 212 15004 13796 6975 423 247 431 C ATOM 1166 C GLU A 212 -23.372 -11.814 22.910 1.00 91.77 C ANISOU 1166 C GLU A 212 14624 13424 6822 416 99 134 C ATOM 1167 O GLU A 212 -23.413 -10.814 23.626 1.00 93.26 O ANISOU 1167 O GLU A 212 14888 13714 6834 419 110 -114 O ATOM 1168 CB GLU A 212 -23.404 -13.640 24.620 1.00103.12 C ANISOU 1168 CB GLU A 212 16325 15152 7706 444 108 543 C ATOM 1169 CG GLU A 212 -24.270 -14.604 25.423 1.00111.37 C ANISOU 1169 CG GLU A 212 17495 16319 8500 447 313 794 C ATOM 1170 CD GLU A 212 -24.400 -15.971 24.775 1.00114.43 C ANISOU 1170 CD GLU A 212 17800 16567 9111 441 333 1126 C ATOM 1171 OE1 GLU A 212 -23.626 -16.268 23.841 1.00113.28 O ANISOU 1171 OE1 GLU A 212 17527 16265 9249 445 146 1167 O ATOM 1172 OE2 GLU A 212 -25.279 -16.749 25.203 1.00120.06 O ANISOU 1172 OE2 GLU A 212 18570 17322 9724 432 543 1339 O ATOM 1173 N ARG A 213 -22.740 -11.836 21.741 1.00 88.88 N ANISOU 1173 N ARG A 213 14103 12880 6786 407 -32 155 N ATOM 1174 CA ARG A 213 -22.053 -10.656 21.234 1.00 87.01 C ANISOU 1174 CA ARG A 213 13774 12552 6734 394 -163 -90 C ATOM 1175 C ARG A 213 -22.569 -10.248 19.857 1.00 78.11 C ANISOU 1175 C ARG A 213 12478 11215 5986 380 -52 -120 C ATOM 1176 O ARG A 213 -22.999 -9.112 19.658 1.00 76.15 O ANISOU 1176 O ARG A 213 12186 10902 5847 372 31 -331 O ATOM 1177 CB ARG A 213 -20.545 -10.901 21.174 1.00 64.38 C ANISOU 1177 CB ARG A 213 10878 9689 3894 395 -461 -57 C ATOM 1178 CG ARG A 213 -19.734 -9.650 20.884 1.00 81.79 C ANISOU 1178 CG ARG A 213 12998 11821 6258 373 -607 -317 C ATOM 1179 CD ARG A 213 -18.250 -9.901 21.076 1.00 82.64 C ANISOU 1179 CD ARG A 213 13083 11962 6353 375 -904 -297 C ATOM 1180 NE ARG A 213 -17.504 -8.654 21.215 1.00 85.87 N ANISOU 1180 NE ARG A 213 13444 12345 6837 349 -1050 -576 N ATOM 1181 CZ ARG A 213 -16.214 -8.588 21.523 1.00 91.67 C ANISOU 1181 CZ ARG A 213 14150 13115 7567 344 -1321 -631 C ATOM 1182 NH1 ARG A 213 -15.523 -9.701 21.724 1.00 93.65 N ANISOU 1182 NH1 ARG A 213 14417 13431 7734 371 -1479 -420 N ATOM 1183 NH2 ARG A 213 -15.614 -7.410 21.631 1.00 97.05 N ANISOU 1183 NH2 ARG A 213 14773 13753 8351 312 -1441 -899 N ATOM 1184 N PHE A 214 -22.525 -11.179 18.910 1.00 71.51 N ANISOU 1184 N PHE A 214 11549 10272 5348 382 -59 88 N ATOM 1185 CA PHE A 214 -22.936 -10.895 17.541 1.00 65.73 C ANISOU 1185 CA PHE A 214 10666 9359 4951 375 19 79 C ATOM 1186 C PHE A 214 -24.400 -11.249 17.296 1.00 66.76 C ANISOU 1186 C PHE A 214 10777 9450 5138 380 260 158 C ATOM 1187 O PHE A 214 -24.760 -11.698 16.209 1.00 62.74 O ANISOU 1187 O PHE A 214 10160 8818 4861 382 303 260 O ATOM 1188 CB PHE A 214 -22.047 -11.650 16.550 1.00 60.59 C ANISOU 1188 CB PHE A 214 9913 8614 4495 377 -126 225 C ATOM 1189 CG PHE A 214 -20.607 -11.220 16.577 1.00 61.92 C ANISOU 1189 CG PHE A 214 10051 8787 4688 369 -353 139 C ATOM 1190 CD1 PHE A 214 -20.186 -10.119 15.849 1.00 61.59 C ANISOU 1190 CD1 PHE A 214 9907 8639 4855 348 -394 -18 C ATOM 1191 CD2 PHE A 214 -19.674 -11.919 17.325 1.00 64.07 C ANISOU 1191 CD2 PHE A 214 10387 9161 4794 382 -529 227 C ATOM 1192 CE1 PHE A 214 -18.863 -9.720 15.869 1.00 61.03 C ANISOU 1192 CE1 PHE A 214 9788 8560 4839 333 -593 -97 C ATOM 1193 CE2 PHE A 214 -18.348 -11.525 17.348 1.00 65.43 C ANISOU 1193 CE2 PHE A 214 10511 9332 5018 373 -747 140 C ATOM 1194 CZ PHE A 214 -17.943 -10.424 16.620 1.00 62.35 C ANISOU 1194 CZ PHE A 214 10007 8832 4849 345 -773 -27 C ATOM 1195 N GLY A 215 -25.238 -11.041 18.306 1.00 74.41 N ANISOU 1195 N GLY A 215 11847 10529 5897 383 417 100 N ATOM 1196 CA GLY A 215 -26.658 -11.323 18.192 1.00 79.51 C ANISOU 1196 CA GLY A 215 12462 11142 6605 385 660 160 C ATOM 1197 C GLY A 215 -27.328 -10.505 17.104 1.00 80.66 C ANISOU 1197 C GLY A 215 12466 11126 7057 388 740 46 C ATOM 1198 O GLY A 215 -28.032 -11.049 16.252 1.00 76.99 O ANISOU 1198 O GLY A 215 11902 10558 6792 390 820 161 O ATOM 1199 N ASP A 216 -27.103 -9.195 17.133 1.00 85.47 N ANISOU 1199 N ASP A 216 13061 11705 7708 390 706 -181 N ATOM 1200 CA ASP A 216 -27.655 -8.293 16.128 1.00 85.15 C ANISOU 1200 CA ASP A 216 12889 11502 7960 398 761 -284 C ATOM 1201 C ASP A 216 -27.110 -8.610 14.740 1.00 77.40 C ANISOU 1201 C ASP A 216 11796 10393 7218 395 634 -165 C ATOM 1202 O ASP A 216 -27.839 -8.557 13.750 1.00 73.01 O ANISOU 1202 O ASP A 216 11135 9721 6884 407 702 -125 O ATOM 1203 CB ASP A 216 -27.350 -6.836 16.485 1.00 92.73 C ANISOU 1203 CB ASP A 216 13858 12440 8933 399 727 -544 C ATOM 1204 CG ASP A 216 -28.087 -6.371 17.725 1.00103.99 C ANISOU 1204 CG ASP A 216 15377 13980 10154 412 888 -708 C ATOM 1205 OD1 ASP A 216 -28.460 -7.229 18.553 1.00114.18 O ANISOU 1205 OD1 ASP A 216 16765 15416 11201 413 985 -606 O ATOM 1206 OD2 ASP A 216 -28.292 -5.148 17.874 1.00108.54 O ANISOU 1206 OD2 ASP A 216 15927 14498 10816 421 925 -938 O ATOM 1207 N PHE A 217 -25.824 -8.937 14.675 1.00 75.52 N ANISOU 1207 N PHE A 217 11581 10184 6931 382 448 -114 N ATOM 1208 CA PHE A 217 -25.179 -9.237 13.405 1.00 72.42 C ANISOU 1208 CA PHE A 217 11088 9688 6742 380 336 -15 C ATOM 1209 C PHE A 217 -25.652 -10.570 12.831 1.00 74.39 C ANISOU 1209 C PHE A 217 11301 9918 7044 391 379 184 C ATOM 1210 O PHE A 217 -25.772 -10.721 11.616 1.00 75.60 O ANISOU 1210 O PHE A 217 11356 9972 7397 399 368 240 O ATOM 1211 CB PHE A 217 -23.658 -9.246 13.564 1.00 69.65 C ANISOU 1211 CB PHE A 217 10754 9373 6337 364 135 -25 C ATOM 1212 CG PHE A 217 -22.930 -9.759 12.357 1.00 66.32 C ANISOU 1212 CG PHE A 217 10234 8871 6094 365 38 90 C ATOM 1213 CD1 PHE A 217 -22.841 -8.992 11.208 1.00 64.97 C ANISOU 1213 CD1 PHE A 217 9960 8581 6145 361 38 49 C ATOM 1214 CD2 PHE A 217 -22.341 -11.012 12.369 1.00 65.29 C ANISOU 1214 CD2 PHE A 217 10115 8784 5910 374 -46 243 C ATOM 1215 CE1 PHE A 217 -22.176 -9.465 10.093 1.00 62.15 C ANISOU 1215 CE1 PHE A 217 9520 8170 5925 365 -32 149 C ATOM 1216 CE2 PHE A 217 -21.673 -11.489 11.258 1.00 63.85 C ANISOU 1216 CE2 PHE A 217 9836 8530 5892 381 -121 326 C ATOM 1217 CZ PHE A 217 -21.592 -10.715 10.118 1.00 61.53 C ANISOU 1217 CZ PHE A 217 9448 8139 5792 375 -107 274 C ATOM 1218 N MET A 218 -25.859 -11.542 13.682 1.00 76.08 N ANISOU 1218 N MET A 218 11597 10227 7082 390 428 292 N ATOM 1219 CA MET A 218 -26.299 -12.798 13.169 1.00 76.37 C ANISOU 1219 CA MET A 218 11596 10229 7192 396 474 477 C ATOM 1220 C MET A 218 -27.666 -12.616 12.570 1.00 76.35 C ANISOU 1220 C MET A 218 11512 10147 7351 401 642 468 C ATOM 1221 O MET A 218 -27.941 -13.126 11.513 1.00 75.13 O ANISOU 1221 O MET A 218 11281 9920 7346 406 657 578 O ATOM 1222 CB MET A 218 -26.309 -13.846 14.267 1.00 79.57 C ANISOU 1222 CB MET A 218 12110 10746 7378 390 495 614 C ATOM 1223 CG MET A 218 -24.926 -14.229 14.769 1.00 79.67 C ANISOU 1223 CG MET A 218 12167 10805 7300 395 299 704 C ATOM 1224 SD MET A 218 -24.960 -15.560 15.975 1.00129.86 S ANISOU 1224 SD MET A 218 18659 17286 13396 395 325 905 S ATOM 1225 CE MET A 218 -23.226 -15.920 16.155 1.00 71.09 C ANISOU 1225 CE MET A 218 11216 9849 5946 414 57 1001 C ATOM 1226 N LEU A 219 -28.537 -11.898 13.255 1.00 78.78 N ANISOU 1226 N LEU A 219 11826 10462 7643 404 759 325 N ATOM 1227 CA LEU A 219 -29.870 -11.682 12.726 1.00 79.66 C ANISOU 1227 CA LEU A 219 11847 10497 7922 415 916 304 C ATOM 1228 C LEU A 219 -29.949 -10.738 11.557 1.00 77.93 C ANISOU 1228 C LEU A 219 11520 10155 7934 434 861 219 C ATOM 1229 O LEU A 219 -30.545 -11.039 10.553 1.00 75.69 O ANISOU 1229 O LEU A 219 11140 9788 7831 446 846 292 O ATOM 1230 CB LEU A 219 -30.767 -11.142 13.821 1.00 81.85 C ANISOU 1230 CB LEU A 219 12179 10846 8073 415 1098 197 C ATOM 1231 CG LEU A 219 -32.155 -10.749 13.363 1.00 81.92 C ANISOU 1231 CG LEU A 219 12080 10778 8267 428 1278 167 C ATOM 1232 CD1 LEU A 219 -32.985 -11.986 13.155 1.00 81.13 C ANISOU 1232 CD1 LEU A 219 11920 10647 8259 414 1339 350 C ATOM 1233 CD2 LEU A 219 -32.801 -9.840 14.379 1.00 86.00 C ANISOU 1233 CD2 LEU A 219 12649 11374 8654 434 1466 30 C ATOM 1234 N PHE A 220 -29.362 -9.570 11.703 1.00 80.56 N ANISOU 1234 N PHE A 220 11872 10477 8262 437 826 67 N ATOM 1235 CA PHE A 220 -29.371 -8.596 10.629 1.00 83.14 C ANISOU 1235 CA PHE A 220 12104 10681 8806 456 785 0 C ATOM 1236 C PHE A 220 -28.469 -8.895 9.461 1.00 85.67 C ANISOU 1236 C PHE A 220 12387 10959 9205 452 626 87 C ATOM 1237 O PHE A 220 -28.844 -8.714 8.330 1.00 86.19 O ANISOU 1237 O PHE A 220 12365 10936 9445 472 602 122 O ATOM 1238 CB PHE A 220 -29.225 -7.187 11.159 1.00 85.14 C ANISOU 1238 CB PHE A 220 12382 10915 9053 456 797 -189 C ATOM 1239 CG PHE A 220 -30.432 -6.726 11.891 1.00 91.28 C ANISOU 1239 CG PHE A 220 13166 11709 9806 472 975 -308 C ATOM 1240 CD1 PHE A 220 -31.674 -6.945 11.361 1.00 93.25 C ANISOU 1240 CD1 PHE A 220 13340 11924 10166 493 1110 -251 C ATOM 1241 CD2 PHE A 220 -30.332 -6.101 13.099 1.00 96.34 C ANISOU 1241 CD2 PHE A 220 13880 12401 10322 468 1009 -492 C ATOM 1242 CE1 PHE A 220 -32.806 -6.542 12.016 1.00 95.73 C ANISOU 1242 CE1 PHE A 220 13644 12253 10475 509 1295 -365 C ATOM 1243 CE2 PHE A 220 -31.460 -5.692 13.768 1.00101.93 C ANISOU 1243 CE2 PHE A 220 14592 13132 11004 488 1193 -620 C ATOM 1244 CZ PHE A 220 -32.700 -5.913 13.224 1.00100.42 C ANISOU 1244 CZ PHE A 220 14318 12905 10932 509 1345 -551 C ATOM 1245 N GLY A 221 -27.280 -9.380 9.744 1.00 86.68 N ANISOU 1245 N GLY A 221 12578 11158 9199 431 518 122 N ATOM 1246 CA GLY A 221 -26.357 -9.692 8.695 1.00 82.71 C ANISOU 1246 CA GLY A 221 12034 10627 8765 428 386 200 C ATOM 1247 C GLY A 221 -26.990 -10.746 7.844 1.00 74.08 C ANISOU 1247 C GLY A 221 10888 9512 7748 445 393 331 C ATOM 1248 O GLY A 221 -26.887 -10.717 6.646 1.00 68.98 O ANISOU 1248 O GLY A 221 10177 8815 7216 458 333 371 O ATOM 1249 N SER A 222 -27.659 -11.691 8.465 1.00 71.51 N ANISOU 1249 N SER A 222 10589 9225 7356 444 470 395 N ATOM 1250 CA SER A 222 -28.294 -12.753 7.729 1.00 69.85 C ANISOU 1250 CA SER A 222 10318 8977 7246 456 483 500 C ATOM 1251 C SER A 222 -29.346 -12.191 6.839 1.00 63.52 C ANISOU 1251 C SER A 222 9422 8093 6619 479 532 467 C ATOM 1252 O SER A 222 -29.508 -12.610 5.733 1.00 61.37 O ANISOU 1252 O SER A 222 9083 7778 6456 497 477 511 O ATOM 1253 CB SER A 222 -28.916 -13.747 8.681 1.00 77.57 C ANISOU 1253 CB SER A 222 11337 9997 8137 442 571 584 C ATOM 1254 OG SER A 222 -27.917 -14.385 9.438 1.00 89.36 O ANISOU 1254 OG SER A 222 12753 11429 9770 448 590 668 O ATOM 1255 N LEU A 223 -30.088 -11.233 7.324 1.00 62.21 N ANISOU 1255 N LEU A 223 9250 7910 6478 484 631 380 N ATOM 1256 CA LEU A 223 -31.136 -10.658 6.491 1.00 60.58 C ANISOU 1256 CA LEU A 223 8947 7619 6452 513 667 346 C ATOM 1257 C LEU A 223 -30.540 -9.893 5.316 1.00 58.90 C ANISOU 1257 C LEU A 223 8701 7357 6323 533 556 338 C ATOM 1258 O LEU A 223 -31.053 -9.954 4.201 1.00 59.47 O ANISOU 1258 O LEU A 223 8698 7379 6519 562 517 373 O ATOM 1259 CB LEU A 223 -32.032 -9.729 7.315 1.00 61.74 C ANISOU 1259 CB LEU A 223 9089 7750 6621 520 800 241 C ATOM 1260 CG LEU A 223 -32.918 -10.364 8.387 1.00 64.19 C ANISOU 1260 CG LEU A 223 9413 8107 6869 504 956 250 C ATOM 1261 CD1 LEU A 223 -33.652 -9.289 9.172 1.00 65.89 C ANISOU 1261 CD1 LEU A 223 9624 8314 7099 517 1093 114 C ATOM 1262 CD2 LEU A 223 -33.903 -11.340 7.763 1.00 64.07 C ANISOU 1262 CD2 LEU A 223 9296 8042 7005 510 987 336 C ATOM 1263 N ALA A 224 -29.447 -9.183 5.576 1.00 58.88 N ANISOU 1263 N ALA A 224 8751 7370 6250 516 503 297 N ATOM 1264 CA ALA A 224 -28.828 -8.322 4.575 1.00 59.45 C ANISOU 1264 CA ALA A 224 8791 7389 6407 526 423 300 C ATOM 1265 C ALA A 224 -27.996 -9.104 3.564 1.00 59.15 C ANISOU 1265 C ALA A 224 8741 7380 6352 529 329 392 C ATOM 1266 O ALA A 224 -27.741 -8.624 2.460 1.00 60.55 O ANISOU 1266 O ALA A 224 8882 7525 6601 546 281 428 O ATOM 1267 CB ALA A 224 -27.967 -7.268 5.256 1.00 59.44 C ANISOU 1267 CB ALA A 224 8833 7379 6371 499 407 213 C ATOM 1268 N ALA A 225 -27.577 -10.308 3.937 1.00 57.85 N ANISOU 1268 N ALA A 225 8607 7279 6095 516 308 434 N ATOM 1269 CA ALA A 225 -26.680 -11.089 3.092 1.00 55.87 C ANISOU 1269 CA ALA A 225 8341 7054 5834 522 226 497 C ATOM 1270 C ALA A 225 -27.407 -12.157 2.282 1.00 57.20 C ANISOU 1270 C ALA A 225 8461 7215 6057 549 218 542 C ATOM 1271 O ALA A 225 -26.968 -12.520 1.190 1.00 63.63 O ANISOU 1271 O ALA A 225 9245 8039 6892 570 160 568 O ATOM 1272 CB ALA A 225 -25.593 -11.729 3.936 1.00 55.28 C ANISOU 1272 CB ALA A 225 8315 7034 5653 496 182 510 C ATOM 1273 N PHE A 226 -28.515 -12.664 2.813 1.00 54.14 N ANISOU 1273 N PHE A 226 8062 6812 5698 549 283 543 N ATOM 1274 CA PHE A 226 -29.237 -13.742 2.149 1.00 52.74 C ANISOU 1274 CA PHE A 226 7825 6612 5601 567 269 572 C ATOM 1275 C PHE A 226 -30.692 -13.393 1.847 1.00 51.43 C ANISOU 1275 C PHE A 226 7592 6395 5555 587 316 545 C ATOM 1276 O PHE A 226 -31.125 -13.464 0.699 1.00 51.33 O ANISOU 1276 O PHE A 226 7520 6363 5621 619 254 540 O ATOM 1277 CB PHE A 226 -29.181 -15.016 2.994 1.00 55.25 C ANISOU 1277 CB PHE A 226 8164 6940 5890 544 294 621 C ATOM 1278 CG PHE A 226 -29.910 -16.179 2.383 1.00 55.51 C ANISOU 1278 CG PHE A 226 8124 6926 6040 555 279 641 C ATOM 1279 CD1 PHE A 226 -29.340 -16.902 1.347 1.00 54.25 C ANISOU 1279 CD1 PHE A 226 7934 6764 5914 578 186 635 C ATOM 1280 CD2 PHE A 226 -31.163 -16.549 2.843 1.00 56.68 C ANISOU 1280 CD2 PHE A 226 8226 7030 6280 541 364 652 C ATOM 1281 CE1 PHE A 226 -30.008 -17.971 0.781 1.00 54.28 C ANISOU 1281 CE1 PHE A 226 7866 6717 6042 588 160 625 C ATOM 1282 CE2 PHE A 226 -31.836 -17.618 2.281 1.00 59.82 C ANISOU 1282 CE2 PHE A 226 8541 7369 6820 545 341 659 C ATOM 1283 CZ PHE A 226 -31.257 -18.330 1.249 1.00 57.05 C ANISOU 1283 CZ PHE A 226 8164 7011 6502 569 230 639 C ATOM 1284 N PHE A 227 -31.445 -13.021 2.877 1.00 51.55 N ANISOU 1284 N PHE A 227 7611 6394 5581 570 421 522 N ATOM 1285 CA PHE A 227 -32.881 -12.801 2.725 1.00 53.99 C ANISOU 1285 CA PHE A 227 7835 6647 6033 588 480 494 C ATOM 1286 C PHE A 227 -33.213 -11.548 1.919 1.00 58.62 C ANISOU 1286 C PHE A 227 8380 7192 6701 628 439 458 C ATOM 1287 O PHE A 227 -34.280 -11.464 1.311 1.00 64.67 O ANISOU 1287 O PHE A 227 9055 7909 7608 659 425 446 O ATOM 1288 CB PHE A 227 -33.552 -12.732 4.098 1.00 53.81 C ANISOU 1288 CB PHE A 227 7825 6627 5994 562 631 474 C ATOM 1289 CG PHE A 227 -33.572 -14.044 4.825 1.00 52.89 C ANISOU 1289 CG PHE A 227 7729 6534 5833 526 685 544 C ATOM 1290 CD1 PHE A 227 -34.483 -15.028 4.479 1.00 52.37 C ANISOU 1290 CD1 PHE A 227 7569 6414 5916 521 703 579 C ATOM 1291 CD2 PHE A 227 -32.677 -14.296 5.850 1.00 51.69 C ANISOU 1291 CD2 PHE A 227 7686 6451 5503 497 708 581 C ATOM 1292 CE1 PHE A 227 -34.502 -16.239 5.142 1.00 51.58 C ANISOU 1292 CE1 PHE A 227 7481 6314 5802 485 758 662 C ATOM 1293 CE2 PHE A 227 -32.691 -15.505 6.518 1.00 51.09 C ANISOU 1293 CE2 PHE A 227 7633 6389 5390 468 753 674 C ATOM 1294 CZ PHE A 227 -33.605 -16.477 6.163 1.00 50.86 C ANISOU 1294 CZ PHE A 227 7508 6291 5525 460 786 721 C ATOM 1295 N THR A 228 -32.306 -10.577 1.912 1.00 58.49 N ANISOU 1295 N THR A 228 8422 7187 6615 627 412 446 N ATOM 1296 CA THR A 228 -32.519 -9.362 1.129 1.00 58.86 C ANISOU 1296 CA THR A 228 8434 7180 6750 663 370 439 C ATOM 1297 C THR A 228 -32.304 -9.601 -0.373 1.00 60.53 C ANISOU 1297 C THR A 228 8621 7408 6970 697 250 501 C ATOM 1298 O THR A 228 -33.157 -9.218 -1.175 1.00 68.70 O ANISOU 1298 O THR A 228 9591 8402 8110 740 204 514 O ATOM 1299 CB THR A 228 -31.611 -8.202 1.604 1.00 58.76 C ANISOU 1299 CB THR A 228 8481 7154 6691 645 385 408 C ATOM 1300 OG1 THR A 228 -31.870 -7.919 2.985 1.00 60.20 O ANISOU 1300 OG1 THR A 228 8693 7335 6847 621 492 325 O ATOM 1301 CG2 THR A 228 -31.868 -6.952 0.777 1.00 58.66 C ANISOU 1301 CG2 THR A 228 8425 7062 6801 682 346 425 C ATOM 1302 N PRO A 229 -31.177 -10.234 -0.768 1.00 56.83 N ANISOU 1302 N PRO A 229 8201 7004 6387 682 196 535 N ATOM 1303 CA PRO A 229 -31.078 -10.511 -2.206 1.00 57.95 C ANISOU 1303 CA PRO A 229 8323 7179 6518 719 98 577 C ATOM 1304 C PRO A 229 -32.088 -11.557 -2.666 1.00 63.21 C ANISOU 1304 C PRO A 229 8923 7845 7249 743 55 553 C ATOM 1305 O PRO A 229 -32.556 -11.485 -3.801 1.00 68.18 O ANISOU 1305 O PRO A 229 9515 8485 7904 787 -32 565 O ATOM 1306 CB PRO A 229 -29.644 -11.025 -2.371 1.00 56.06 C ANISOU 1306 CB PRO A 229 8139 7007 6156 697 77 597 C ATOM 1307 CG PRO A 229 -29.272 -11.546 -1.035 1.00 54.05 C ANISOU 1307 CG PRO A 229 7917 6754 5867 653 136 569 C ATOM 1308 CD PRO A 229 -29.950 -10.640 -0.057 1.00 55.01 C ANISOU 1308 CD PRO A 229 8039 6822 6039 640 212 535 C ATOM 1309 N LEU A 230 -32.414 -12.510 -1.797 1.00 66.65 N ANISOU 1309 N LEU A 230 9343 8267 7714 712 111 525 N ATOM 1310 CA LEU A 230 -33.440 -13.503 -2.096 1.00 63.76 C ANISOU 1310 CA LEU A 230 8895 7874 7457 722 82 497 C ATOM 1311 C LEU A 230 -34.770 -12.818 -2.381 1.00 63.00 C ANISOU 1311 C LEU A 230 8711 7722 7505 756 71 478 C ATOM 1312 O LEU A 230 -35.481 -13.190 -3.312 1.00 67.63 O ANISOU 1312 O LEU A 230 9225 8301 8170 790 -26 456 O ATOM 1313 CB LEU A 230 -33.589 -14.496 -0.942 1.00 63.93 C ANISOU 1313 CB LEU A 230 8913 7873 7505 675 172 497 C ATOM 1314 CG LEU A 230 -34.797 -15.439 -0.959 1.00 64.33 C ANISOU 1314 CG LEU A 230 8857 7863 7720 669 180 474 C ATOM 1315 CD1 LEU A 230 -34.809 -16.296 -2.213 1.00 64.31 C ANISOU 1315 CD1 LEU A 230 8808 7868 7758 697 44 436 C ATOM 1316 CD2 LEU A 230 -34.806 -16.313 0.285 1.00 65.76 C ANISOU 1316 CD2 LEU A 230 9052 8022 7911 616 293 512 C ATOM 1317 N ALA A 231 -35.092 -11.809 -1.577 1.00 58.66 N ANISOU 1317 N ALA A 231 8162 7130 6997 750 163 474 N ATOM 1318 CA ALA A 231 -36.315 -11.037 -1.764 1.00 56.61 C ANISOU 1318 CA ALA A 231 7808 6801 6900 789 162 453 C ATOM 1319 C ALA A 231 -36.322 -10.352 -3.126 1.00 54.91 C ANISOU 1319 C ALA A 231 7582 6594 6688 848 20 493 C ATOM 1320 O ALA A 231 -37.358 -10.267 -3.783 1.00 55.76 O ANISOU 1320 O ALA A 231 7595 6667 6926 893 -60 484 O ATOM 1321 CB ALA A 231 -36.470 -10.011 -0.653 1.00 55.95 C ANISOU 1321 CB ALA A 231 7737 6671 6850 776 293 425 C ATOM 1322 N ILE A 232 -35.157 -9.870 -3.545 1.00 52.05 N ANISOU 1322 N ILE A 232 7313 6279 6182 848 -12 544 N ATOM 1323 CA ILE A 232 -35.022 -9.203 -4.833 1.00 52.18 C ANISOU 1323 CA ILE A 232 7341 6319 6166 900 -128 612 C ATOM 1324 C ILE A 232 -35.110 -10.208 -5.979 1.00 55.32 C ANISOU 1324 C ILE A 232 7728 6797 6496 928 -253 605 C ATOM 1325 O ILE A 232 -35.810 -9.977 -6.965 1.00 60.48 O ANISOU 1325 O ILE A 232 8336 7458 7186 985 -372 627 O ATOM 1326 CB ILE A 232 -33.693 -8.431 -4.928 1.00 50.85 C ANISOU 1326 CB ILE A 232 7269 6177 5876 881 -103 677 C ATOM 1327 CG1 ILE A 232 -33.603 -7.396 -3.805 1.00 48.41 C ANISOU 1327 CG1 ILE A 232 6967 5781 5646 854 4 656 C ATOM 1328 CG2 ILE A 232 -33.559 -7.759 -6.286 1.00 52.18 C ANISOU 1328 CG2 ILE A 232 7454 6375 5999 933 -206 777 C ATOM 1329 CD1 ILE A 232 -32.296 -6.635 -3.775 1.00 47.03 C ANISOU 1329 CD1 ILE A 232 6868 5611 5392 824 29 704 C ATOM 1330 N MET A 233 -34.407 -11.327 -5.835 1.00 52.18 N ANISOU 1330 N MET A 233 7367 6455 6003 893 -235 566 N ATOM 1331 CA MET A 233 -34.396 -12.366 -6.859 1.00 50.38 C ANISOU 1331 CA MET A 233 7129 6299 5713 918 -345 525 C ATOM 1332 C MET A 233 -35.775 -12.994 -7.038 1.00 52.52 C ANISOU 1332 C MET A 233 7285 6523 6146 938 -418 455 C ATOM 1333 O MET A 233 -36.095 -13.509 -8.109 1.00 53.85 O ANISOU 1333 O MET A 233 7426 6743 6291 979 -552 412 O ATOM 1334 CB MET A 233 -33.364 -13.443 -6.517 1.00 47.16 C ANISOU 1334 CB MET A 233 6769 5932 5216 877 -298 489 C ATOM 1335 CG MET A 233 -31.928 -12.942 -6.556 1.00 46.92 C ANISOU 1335 CG MET A 233 6834 5959 5036 862 -250 547 C ATOM 1336 SD MET A 233 -30.722 -14.169 -6.021 1.00 53.41 S ANISOU 1336 SD MET A 233 7691 6809 5792 820 -201 507 S ATOM 1337 CE MET A 233 -30.929 -15.420 -7.283 1.00 44.43 C ANISOU 1337 CE MET A 233 6519 5730 4632 864 -313 417 C ATOM 1338 N ILE A 234 -36.588 -12.945 -5.989 1.00 52.96 N ANISOU 1338 N ILE A 234 7268 6486 6368 909 -327 436 N ATOM 1339 CA ILE A 234 -37.966 -13.418 -6.065 1.00 56.07 C ANISOU 1339 CA ILE A 234 7526 6817 6963 922 -378 375 C ATOM 1340 C ILE A 234 -38.832 -12.417 -6.825 1.00 56.68 C ANISOU 1340 C ILE A 234 7540 6874 7121 990 -488 400 C ATOM 1341 O ILE A 234 -39.627 -12.798 -7.685 1.00 57.17 O ANISOU 1341 O ILE A 234 7518 6943 7260 1030 -637 354 O ATOM 1342 CB ILE A 234 -38.559 -13.660 -4.661 1.00 59.44 C ANISOU 1342 CB ILE A 234 7889 7155 7542 868 -215 357 C ATOM 1343 CG1 ILE A 234 -37.963 -14.926 -4.043 1.00 58.75 C ANISOU 1343 CG1 ILE A 234 7837 7075 7411 808 -144 342 C ATOM 1344 CG2 ILE A 234 -40.073 -13.786 -4.728 1.00 60.97 C ANISOU 1344 CG2 ILE A 234 7917 7267 7982 885 -247 307 C ATOM 1345 CD1 ILE A 234 -38.342 -15.133 -2.594 1.00 57.80 C ANISOU 1345 CD1 ILE A 234 7690 6893 7378 751 36 358 C ATOM 1346 N VAL A 235 -38.668 -11.136 -6.510 1.00 57.03 N ANISOU 1346 N VAL A 235 7621 6888 7160 1004 -428 470 N ATOM 1347 CA VAL A 235 -39.413 -10.080 -7.187 1.00 58.02 C ANISOU 1347 CA VAL A 235 7690 6977 7378 1074 -532 519 C ATOM 1348 C VAL A 235 -39.049 -10.011 -8.667 1.00 58.81 C ANISOU 1348 C VAL A 235 7850 7180 7313 1131 -711 575 C ATOM 1349 O VAL A 235 -39.928 -9.999 -9.530 1.00 59.19 O ANISOU 1349 O VAL A 235 7823 7235 7430 1192 -873 569 O ATOM 1350 CB VAL A 235 -39.164 -8.704 -6.537 1.00 59.20 C ANISOU 1350 CB VAL A 235 7873 7055 7565 1076 -425 581 C ATOM 1351 CG1 VAL A 235 -39.721 -7.589 -7.410 1.00 48.75 C ANISOU 1351 CG1 VAL A 235 6509 5691 6322 1156 -552 664 C ATOM 1352 CG2 VAL A 235 -39.778 -8.656 -5.148 1.00 59.23 C ANISOU 1352 CG2 VAL A 235 7803 6966 7737 1037 -256 509 C ATOM 1353 N THR A 236 -37.751 -9.981 -8.955 1.00 59.26 N ANISOU 1353 N THR A 236 8042 7325 7151 1113 -680 627 N ATOM 1354 CA THR A 236 -37.272 -9.922 -10.332 1.00 62.68 C ANISOU 1354 CA THR A 236 8550 7878 7387 1163 -814 686 C ATOM 1355 C THR A 236 -37.656 -11.176 -11.112 1.00 64.15 C ANISOU 1355 C THR A 236 8701 8145 7527 1184 -949 575 C ATOM 1356 O THR A 236 -37.740 -11.149 -12.340 1.00 70.57 O ANISOU 1356 O THR A 236 9544 9060 8208 1245 -1102 596 O ATOM 1357 CB THR A 236 -35.743 -9.740 -10.395 1.00 62.98 C ANISOU 1357 CB THR A 236 8721 7991 7217 1130 -721 751 C ATOM 1358 OG1 THR A 236 -35.100 -10.822 -9.710 1.00 64.12 O ANISOU 1358 OG1 THR A 236 8884 8152 7328 1069 -628 657 O ATOM 1359 CG2 THR A 236 -35.336 -8.422 -9.754 1.00 63.53 C ANISOU 1359 CG2 THR A 236 8820 7974 7343 1111 -612 854 C ATOM 1360 N TYR A 237 -37.884 -12.272 -10.395 1.00 60.68 N ANISOU 1360 N TYR A 237 8200 7661 7197 1133 -892 458 N ATOM 1361 CA TYR A 237 -38.340 -13.513 -11.012 1.00 58.73 C ANISOU 1361 CA TYR A 237 7893 7452 6970 1145 -1017 329 C ATOM 1362 C TYR A 237 -39.709 -13.324 -11.655 1.00 61.50 C ANISOU 1362 C TYR A 237 8124 7777 7466 1204 -1195 297 C ATOM 1363 O TYR A 237 -39.878 -13.562 -12.849 1.00 67.01 O ANISOU 1363 O TYR A 237 8835 8576 8051 1261 -1378 258 O ATOM 1364 CB TYR A 237 -38.390 -14.643 -9.981 1.00 57.02 C ANISOU 1364 CB TYR A 237 7616 7153 6894 1072 -906 237 C ATOM 1365 CG TYR A 237 -39.090 -15.896 -10.462 1.00 57.36 C ANISOU 1365 CG TYR A 237 7559 7184 7052 1075 -1030 94 C ATOM 1366 CD1 TYR A 237 -38.433 -16.818 -11.267 1.00 49.18 C ANISOU 1366 CD1 TYR A 237 6576 6238 5873 1087 -1110 1 C ATOM 1367 CD2 TYR A 237 -40.404 -16.162 -10.100 1.00 49.83 C ANISOU 1367 CD2 TYR A 237 6444 6120 6370 1063 -1061 38 C ATOM 1368 CE1 TYR A 237 -39.069 -17.965 -11.705 1.00 60.10 C ANISOU 1368 CE1 TYR A 237 7859 7594 7383 1088 -1232 -153 C ATOM 1369 CE2 TYR A 237 -41.047 -17.306 -10.533 1.00 50.95 C ANISOU 1369 CE2 TYR A 237 6476 6232 6651 1058 -1180 -102 C ATOM 1370 CZ TYR A 237 -40.375 -18.204 -11.335 1.00 51.19 C ANISOU 1370 CZ TYR A 237 6566 6345 6537 1070 -1272 -202 C ATOM 1371 OH TYR A 237 -41.011 -19.344 -11.768 1.00 52.49 O ANISOU 1371 OH TYR A 237 6616 6466 6861 1064 -1400 -363 O ATOM 1372 N PHE A 238 -40.681 -12.891 -10.856 1.00 60.07 N ANISOU 1372 N PHE A 238 7823 7467 7533 1193 -1142 307 N ATOM 1373 CA PHE A 238 -42.030 -12.645 -11.356 1.00 60.06 C ANISOU 1373 CA PHE A 238 7680 7420 7721 1250 -1307 280 C ATOM 1374 C PHE A 238 -42.043 -11.498 -12.360 1.00 59.72 C ANISOU 1374 C PHE A 238 7695 7443 7553 1337 -1451 402 C ATOM 1375 O PHE A 238 -42.882 -11.461 -13.260 1.00 60.86 O ANISOU 1375 O PHE A 238 7766 7616 7742 1405 -1664 382 O ATOM 1376 CB PHE A 238 -42.988 -12.345 -10.201 1.00 60.99 C ANISOU 1376 CB PHE A 238 7652 7382 8141 1220 -1180 270 C ATOM 1377 CG PHE A 238 -43.217 -13.513 -9.287 1.00 61.80 C ANISOU 1377 CG PHE A 238 7675 7415 8393 1140 -1054 169 C ATOM 1378 CD1 PHE A 238 -44.010 -14.576 -9.689 1.00 62.99 C ANISOU 1378 CD1 PHE A 238 7693 7540 8701 1133 -1177 48 C ATOM 1379 CD2 PHE A 238 -42.645 -13.548 -8.027 1.00 61.57 C ANISOU 1379 CD2 PHE A 238 7701 7343 8351 1070 -819 200 C ATOM 1380 CE1 PHE A 238 -44.224 -15.653 -8.852 1.00 62.38 C ANISOU 1380 CE1 PHE A 238 7536 7381 8785 1054 -1052 -21 C ATOM 1381 CE2 PHE A 238 -42.855 -14.623 -7.185 1.00 60.85 C ANISOU 1381 CE2 PHE A 238 7544 7190 8387 997 -700 139 C ATOM 1382 CZ PHE A 238 -43.647 -15.677 -7.598 1.00 62.28 C ANISOU 1382 CZ PHE A 238 7589 7331 8744 987 -809 38 C ATOM 1383 N LEU A 239 -41.112 -10.563 -12.198 1.00 58.03 N ANISOU 1383 N LEU A 239 7608 7248 7193 1334 -1342 535 N ATOM 1384 CA LEU A 239 -40.944 -9.479 -13.158 1.00 58.45 C ANISOU 1384 CA LEU A 239 7736 7361 7110 1409 -1455 686 C ATOM 1385 C LEU A 239 -40.451 -10.031 -14.492 1.00 61.91 C ANISOU 1385 C LEU A 239 8277 7984 7261 1449 -1609 676 C ATOM 1386 O LEU A 239 -40.831 -9.544 -15.556 1.00 64.70 O ANISOU 1386 O LEU A 239 8649 8412 7523 1530 -1794 755 O ATOM 1387 CB LEU A 239 -39.968 -8.426 -12.628 1.00 54.68 C ANISOU 1387 CB LEU A 239 7364 6846 6566 1381 -1284 823 C ATOM 1388 CG LEU A 239 -40.457 -7.511 -11.503 1.00 53.35 C ANISOU 1388 CG LEU A 239 7112 6505 6654 1365 -1157 849 C ATOM 1389 CD1 LEU A 239 -39.339 -6.589 -11.045 1.00 51.85 C ANISOU 1389 CD1 LEU A 239 7034 6287 6381 1329 -1003 955 C ATOM 1390 CD2 LEU A 239 -41.669 -6.708 -11.948 1.00 54.28 C ANISOU 1390 CD2 LEU A 239 7112 6541 6970 1450 -1307 906 C ATOM 1391 N THR A 240 -39.603 -11.053 -14.422 1.00 62.55 N ANISOU 1391 N THR A 240 8426 8142 7199 1398 -1532 576 N ATOM 1392 CA THR A 240 -39.054 -11.686 -15.615 1.00 54.45 C ANISOU 1392 CA THR A 240 7497 7296 5896 1433 -1646 529 C ATOM 1393 C THR A 240 -40.100 -12.551 -16.311 1.00 56.11 C ANISOU 1393 C THR A 240 7607 7543 6170 1477 -1869 370 C ATOM 1394 O THR A 240 -40.207 -12.542 -17.537 1.00 57.93 O ANISOU 1394 O THR A 240 7892 7920 6200 1549 -2054 369 O ATOM 1395 CB THR A 240 -37.825 -12.551 -15.278 1.00 52.93 C ANISOU 1395 CB THR A 240 7386 7153 5571 1369 -1489 451 C ATOM 1396 OG1 THR A 240 -36.838 -11.748 -14.618 1.00 51.54 O ANISOU 1396 OG1 THR A 240 7290 6942 5351 1326 -1298 587 O ATOM 1397 CG2 THR A 240 -37.224 -13.148 -16.542 1.00 54.18 C ANISOU 1397 CG2 THR A 240 7643 7504 5438 1413 -1587 388 C ATOM 1398 N ILE A 241 -40.867 -13.298 -15.521 1.00 58.64 N ANISOU 1398 N ILE A 241 7779 7732 6769 1430 -1850 235 N ATOM 1399 CA ILE A 241 -41.930 -14.141 -16.057 1.00 60.84 C ANISOU 1399 CA ILE A 241 7927 8009 7178 1458 -2058 69 C ATOM 1400 C ILE A 241 -42.974 -13.290 -16.771 1.00 67.18 C ANISOU 1400 C ILE A 241 8663 8824 8039 1546 -2275 141 C ATOM 1401 O ILE A 241 -43.458 -13.652 -17.844 1.00 68.17 O ANISOU 1401 O ILE A 241 8772 9054 8077 1609 -2518 54 O ATOM 1402 CB ILE A 241 -42.614 -14.970 -14.949 1.00 59.58 C ANISOU 1402 CB ILE A 241 7601 7677 7360 1382 -1964 -52 C ATOM 1403 CG1 ILE A 241 -41.587 -15.829 -14.211 1.00 56.59 C ANISOU 1403 CG1 ILE A 241 7290 7280 6933 1300 -1763 -101 C ATOM 1404 CG2 ILE A 241 -43.714 -15.843 -15.532 1.00 63.93 C ANISOU 1404 CG2 ILE A 241 7997 8210 8084 1404 -2187 -231 C ATOM 1405 CD1 ILE A 241 -40.761 -16.710 -15.120 1.00 56.90 C ANISOU 1405 CD1 ILE A 241 7430 7459 6731 1316 -1839 -215 C ATOM 1406 N HIS A 242 -43.306 -12.151 -16.172 1.00 71.91 N ANISOU 1406 N HIS A 242 9223 9312 8788 1555 -2196 295 N ATOM 1407 CA HIS A 242 -44.262 -11.223 -16.762 1.00 75.57 C ANISOU 1407 CA HIS A 242 9615 9760 9340 1645 -2392 392 C ATOM 1408 C HIS A 242 -43.678 -10.547 -17.997 1.00 77.91 C ANISOU 1408 C HIS A 242 10081 10232 9289 1725 -2524 542 C ATOM 1409 O HIS A 242 -44.399 -10.243 -18.945 1.00 82.54 O ANISOU 1409 O HIS A 242 10637 10884 9840 1815 -2777 577 O ATOM 1410 CB HIS A 242 -44.692 -10.169 -15.739 1.00 79.32 C ANISOU 1410 CB HIS A 242 10000 10053 10084 1634 -2247 506 C ATOM 1411 CG HIS A 242 -45.619 -9.132 -16.294 1.00 86.13 C ANISOU 1411 CG HIS A 242 10782 10875 11070 1733 -2439 624 C ATOM 1412 ND1 HIS A 242 -46.839 -9.446 -16.854 1.00 90.18 N ANISOU 1412 ND1 HIS A 242 11133 11376 11754 1792 -2689 534 N ATOM 1413 CD2 HIS A 242 -45.504 -7.785 -16.375 1.00 87.71 C ANISOU 1413 CD2 HIS A 242 11029 11028 11267 1785 -2426 827 C ATOM 1414 CE1 HIS A 242 -47.435 -8.338 -17.257 1.00 90.63 C ANISOU 1414 CE1 HIS A 242 11144 11389 11902 1883 -2829 684 C ATOM 1415 NE2 HIS A 242 -46.646 -7.316 -16.978 1.00 90.23 N ANISOU 1415 NE2 HIS A 242 11220 11311 11752 1880 -2669 867 N ATOM 1416 N ALA A 243 -42.369 -10.316 -17.981 1.00 77.35 N ANISOU 1416 N ALA A 243 10185 10240 8964 1693 -2353 638 N ATOM 1417 CA ALA A 243 -41.694 -9.664 -19.098 1.00 80.18 C ANISOU 1417 CA ALA A 243 10714 10768 8983 1757 -2427 804 C ATOM 1418 C ALA A 243 -41.681 -10.552 -20.337 1.00 83.89 C ANISOU 1418 C ALA A 243 11249 11450 9177 1808 -2629 677 C ATOM 1419 O ALA A 243 -41.899 -10.079 -21.450 1.00 87.77 O ANISOU 1419 O ALA A 243 11810 12078 9460 1898 -2824 781 O ATOM 1420 CB ALA A 243 -40.275 -9.282 -18.709 1.00 78.18 C ANISOU 1420 CB ALA A 243 10606 10535 8563 1697 -2173 919 C ATOM 1421 N LEU A 244 -41.427 -11.841 -20.135 1.00 82.33 N ANISOU 1421 N LEU A 244 11029 11276 8978 1754 -2584 450 N ATOM 1422 CA LEU A 244 -41.342 -12.790 -21.239 1.00 85.82 C ANISOU 1422 CA LEU A 244 11528 11909 9169 1796 -2757 279 C ATOM 1423 C LEU A 244 -42.703 -13.054 -21.876 1.00 90.47 C ANISOU 1423 C LEU A 244 11989 12511 9877 1865 -3072 164 C ATOM 1424 O LEU A 244 -42.822 -13.103 -23.100 1.00 95.48 O ANISOU 1424 O LEU A 244 12703 13339 10237 1948 -3292 142 O ATOM 1425 CB LEU A 244 -40.726 -14.106 -20.761 1.00 86.23 C ANISOU 1425 CB LEU A 244 11568 11943 9252 1718 -2620 58 C ATOM 1426 CG LEU A 244 -39.250 -14.052 -20.362 1.00 61.50 C ANISOU 1426 CG LEU A 244 8572 8844 5950 1662 -2348 135 C ATOM 1427 CD1 LEU A 244 -38.809 -15.366 -19.741 1.00 60.07 C ANISOU 1427 CD1 LEU A 244 8344 8600 5881 1588 -2232 -76 C ATOM 1428 CD2 LEU A 244 -38.389 -13.715 -21.568 1.00 66.77 C ANISOU 1428 CD2 LEU A 244 9424 9749 6196 1723 -2371 221 C ATOM 1429 N GLN A 245 -43.726 -13.223 -21.044 1.00 91.79 N ANISOU 1429 N GLN A 245 11952 12477 10447 1831 -3093 88 N ATOM 1430 CA GLN A 245 -45.066 -13.525 -21.539 1.00 96.92 C ANISOU 1430 CA GLN A 245 12439 13109 11279 1887 -3389 -39 C ATOM 1431 C GLN A 245 -45.705 -12.307 -22.198 1.00 95.06 C ANISOU 1431 C GLN A 245 12207 12913 11000 1992 -3591 166 C ATOM 1432 O GLN A 245 -46.653 -12.437 -22.972 1.00 97.35 O ANISOU 1432 O GLN A 245 12410 13257 11320 2066 -3895 89 O ATOM 1433 CB GLN A 245 -45.955 -14.040 -20.404 1.00107.60 C ANISOU 1433 CB GLN A 245 13556 14224 13103 1813 -3319 -165 C ATOM 1434 CG GLN A 245 -46.253 -13.014 -19.324 1.00116.68 C ANISOU 1434 CG GLN A 245 14626 15187 14519 1788 -3138 15 C ATOM 1435 CD GLN A 245 -47.005 -13.609 -18.147 1.00119.41 C ANISOU 1435 CD GLN A 245 14758 15321 15291 1706 -3015 -110 C ATOM 1436 OE1 GLN A 245 -47.169 -14.826 -18.051 1.00119.60 O ANISOU 1436 OE1 GLN A 245 14702 15320 15419 1653 -3033 -312 O ATOM 1437 NE2 GLN A 245 -47.467 -12.751 -17.245 1.00122.36 N ANISOU 1437 NE2 GLN A 245 15036 15537 15921 1695 -2879 10 N ATOM 1438 N LYS A 246 -45.182 -11.125 -21.888 1.00 92.12 N ANISOU 1438 N LYS A 246 11928 12502 10572 1998 -3430 426 N ATOM 1439 CA LYS A 246 -45.654 -9.890 -22.503 1.00 92.31 C ANISOU 1439 CA LYS A 246 11971 12547 10555 2099 -3600 660 C ATOM 1440 C LYS A 246 -44.890 -9.613 -23.792 1.00 89.66 C ANISOU 1440 C LYS A 246 11866 12473 9729 2170 -3700 791 C ATOM 1441 O LYS A 246 -45.447 -9.097 -24.760 1.00 93.33 O ANISOU 1441 O LYS A 246 12355 13042 10063 2275 -3967 903 O ATOM 1442 CB LYS A 246 -45.506 -8.714 -21.534 1.00 93.85 C ANISOU 1442 CB LYS A 246 12141 12550 10968 2071 -3380 873 C ATOM 1443 CG LYS A 246 -45.936 -7.370 -22.104 1.00 99.03 C ANISOU 1443 CG LYS A 246 12812 13191 11623 2175 -3536 1139 C ATOM 1444 CD LYS A 246 -45.676 -6.243 -21.116 1.00 99.02 C ANISOU 1444 CD LYS A 246 12790 12986 11846 2141 -3298 1320 C ATOM 1445 CE LYS A 246 -46.039 -4.890 -21.708 1.00101.99 C ANISOU 1445 CE LYS A 246 13183 13327 12242 2246 -3449 1600 C ATOM 1446 NZ LYS A 246 -45.751 -3.775 -20.764 1.00102.98 N ANISOU 1446 NZ LYS A 246 13285 13240 12603 2213 -3218 1756 N ATOM 1447 N LYS A 247 -43.608 -9.966 -23.793 1.00 84.93 N ANISOU 1447 N LYS A 247 11432 11980 8856 2113 -3482 780 N ATOM 1448 CA LYS A 247 -42.749 -9.771 -24.955 1.00 84.50 C ANISOU 1448 CA LYS A 247 11601 12185 8321 2168 -3515 896 C ATOM 1449 C LYS A 247 -43.197 -10.652 -26.117 1.00 87.01 C ANISOU 1449 C LYS A 247 11945 12720 8395 2240 -3807 693 C ATOM 1450 O LYS A 247 -43.035 -10.292 -27.283 1.00 85.76 O ANISOU 1450 O LYS A 247 11939 12786 7861 2328 -3959 813 O ATOM 1451 CB LYS A 247 -41.292 -10.066 -24.592 1.00 82.60 C ANISOU 1451 CB LYS A 247 11494 11990 7901 2083 -3198 890 C ATOM 1452 CG LYS A 247 -40.274 -9.618 -25.624 1.00 86.45 C ANISOU 1452 CG LYS A 247 12206 12714 7927 2126 -3149 1069 C ATOM 1453 CD LYS A 247 -38.858 -9.834 -25.110 1.00 86.10 C ANISOU 1453 CD LYS A 247 12253 12674 7789 2036 -2818 1068 C ATOM 1454 CE LYS A 247 -37.821 -9.312 -26.089 1.00 91.28 C ANISOU 1454 CE LYS A 247 13116 13552 8016 2071 -2731 1268 C ATOM 1455 NZ LYS A 247 -36.439 -9.476 -25.560 1.00 87.04 N ANISOU 1455 NZ LYS A 247 12641 13003 7429 1982 -2409 1269 N ATOM 1456 N ALA A 248 -43.765 -11.808 -25.788 1.00 91.56 N ANISOU 1456 N ALA A 248 12373 13228 9188 2201 -3884 386 N ATOM 1457 CA ALA A 248 -44.258 -12.736 -26.797 1.00 98.38 C ANISOU 1457 CA ALA A 248 13231 14268 9880 2260 -4174 139 C ATOM 1458 C ALA A 248 -45.710 -12.437 -27.157 1.00101.28 C ANISOU 1458 C ALA A 248 13439 14589 10452 2341 -4522 135 C ATOM 1459 O ALA A 248 -46.191 -12.835 -28.217 1.00103.46 O ANISOU 1459 O ALA A 248 13738 15048 10525 2423 -4830 4 O ATOM 1460 CB ALA A 248 -44.116 -14.170 -26.311 1.00100.75 C ANISOU 1460 CB ALA A 248 13440 14502 10337 2176 -4092 -198 C ATOM 1461 N ALA A1001 -46.403 -11.735 -26.266 1.00118.89 N ANISOU 1461 N ALA A1001 15042 21149 8980 -570 -305 1571 N ATOM 1462 CA ALA A1001 -47.792 -11.361 -26.502 1.00125.20 C ANISOU 1462 CA ALA A1001 15724 22092 9754 -554 98 1415 C ATOM 1463 C ALA A1001 -47.882 -10.271 -27.563 1.00122.51 C ANISOU 1463 C ALA A1001 15028 21873 9646 -357 162 1336 C ATOM 1464 O ALA A1001 -48.803 -10.260 -28.379 1.00128.67 O ANISOU 1464 O ALA A1001 15507 22824 10558 -269 391 1266 O ATOM 1465 CB ALA A1001 -48.447 -10.898 -25.210 1.00131.62 C ANISOU 1465 CB ALA A1001 16942 22834 10234 -691 307 1333 C ATOM 1466 N ASP A1002 -46.918 -9.357 -27.544 1.00119.10 N ANISOU 1466 N ASP A1002 14648 21356 9250 -311 -61 1359 N ATOM 1467 CA ASP A1002 -46.875 -8.270 -28.513 1.00115.11 C ANISOU 1467 CA ASP A1002 13887 20918 8934 -142 -22 1295 C ATOM 1468 C ASP A1002 -46.402 -8.773 -29.872 1.00110.80 C ANISOU 1468 C ASP A1002 12949 20458 8692 -30 -133 1359 C ATOM 1469 O ASP A1002 -46.766 -8.220 -30.910 1.00112.81 O ANISOU 1469 O ASP A1002 12947 20809 9106 111 -21 1301 O ATOM 1470 CB ASP A1002 -45.965 -7.145 -28.017 1.00115.01 C ANISOU 1470 CB ASP A1002 14112 20764 8824 -197 -221 1299 C ATOM 1471 CG ASP A1002 -46.400 -6.595 -26.673 1.00112.90 C ANISOU 1471 CG ASP A1002 14327 20364 8207 -323 -96 1224 C ATOM 1472 OD1 ASP A1002 -47.602 -6.698 -26.347 1.00112.25 O ANISOU 1472 OD1 ASP A1002 14308 20332 8010 -282 251 1131 O ATOM 1473 OD2 ASP A1002 -45.541 -6.058 -25.942 1.00111.58 O ANISOU 1473 OD2 ASP A1002 14479 20045 7871 -480 -336 1260 O ATOM 1474 N LEU A1003 -45.588 -9.824 -29.860 1.00104.99 N ANISOU 1474 N LEU A1003 12204 19667 8022 -80 -342 1486 N ATOM 1475 CA LEU A1003 -45.096 -10.426 -31.094 1.00101.32 C ANISOU 1475 CA LEU A1003 11432 19244 7821 32 -403 1548 C ATOM 1476 C LEU A1003 -46.215 -11.169 -31.814 1.00103.74 C ANISOU 1476 C LEU A1003 11602 19656 8159 43 -164 1487 C ATOM 1477 O LEU A1003 -46.344 -11.084 -33.036 1.00106.64 O ANISOU 1477 O LEU A1003 11718 20101 8699 140 -103 1460 O ATOM 1478 CB LEU A1003 -43.932 -11.376 -30.805 1.00100.42 C ANISOU 1478 CB LEU A1003 11369 19022 7765 24 -661 1713 C ATOM 1479 CG LEU A1003 -43.355 -12.114 -32.014 1.00 98.41 C ANISOU 1479 CG LEU A1003 10853 18768 7772 168 -674 1783 C ATOM 1480 CD1 LEU A1003 -42.876 -11.127 -33.068 1.00 97.10 C ANISOU 1480 CD1 LEU A1003 10409 18670 7814 269 -672 1748 C ATOM 1481 CD2 LEU A1003 -42.226 -13.042 -31.593 1.00 99.96 C ANISOU 1481 CD2 LEU A1003 11103 18848 8028 218 -910 1967 C ATOM 1482 N GLU A1004 -47.022 -11.897 -31.049 1.00104.57 N ANISOU 1482 N GLU A1004 11895 19764 8075 -94 -37 1471 N ATOM 1483 CA GLU A1004 -48.169 -12.605 -31.602 1.00103.84 C ANISOU 1483 CA GLU A1004 11678 19797 7978 -164 183 1418 C ATOM 1484 C GLU A1004 -49.220 -11.613 -32.086 1.00106.18 C ANISOU 1484 C GLU A1004 11732 20292 8319 -87 382 1307 C ATOM 1485 O GLU A1004 -50.000 -11.910 -32.991 1.00106.10 O ANISOU 1485 O GLU A1004 11485 20437 8391 -100 489 1277 O ATOM 1486 CB GLU A1004 -48.772 -13.553 -30.563 1.00102.95 C ANISOU 1486 CB GLU A1004 11846 19641 7631 -372 290 1430 C ATOM 1487 N ASP A1005 -49.230 -10.433 -31.475 1.00109.62 N ANISOU 1487 N ASP A1005 12252 20712 8686 -7 418 1255 N ATOM 1488 CA ASP A1005 -50.144 -9.369 -31.867 1.00112.93 C ANISOU 1488 CA ASP A1005 12474 21282 9151 140 609 1166 C ATOM 1489 C ASP A1005 -49.760 -8.824 -33.240 1.00113.01 C ANISOU 1489 C ASP A1005 12233 21328 9377 303 499 1175 C ATOM 1490 O ASP A1005 -50.612 -8.655 -34.112 1.00111.82 O ANISOU 1490 O ASP A1005 11815 21351 9321 386 601 1148 O ATOM 1491 CB ASP A1005 -50.138 -8.247 -30.824 1.00114.49 C ANISOU 1491 CB ASP A1005 12938 21378 9186 195 694 1107 C ATOM 1492 CG ASP A1005 -51.374 -7.369 -30.898 1.00117.54 C ANISOU 1492 CG ASP A1005 13176 21913 9570 365 992 1019 C ATOM 1493 OD1 ASP A1005 -51.949 -7.226 -31.997 1.00115.09 O ANISOU 1493 OD1 ASP A1005 12510 21779 9438 499 1032 1020 O ATOM 1494 OD2 ASP A1005 -51.772 -6.818 -29.850 1.00124.56 O ANISOU 1494 OD2 ASP A1005 14319 22735 10271 377 1191 958 O ATOM 1495 N ASN A1006 -48.471 -8.556 -33.425 1.00114.25 N ANISOU 1495 N ASN A1006 12474 21329 9606 331 284 1224 N ATOM 1496 CA ASN A1006 -47.966 -8.058 -34.699 1.00114.85 C ANISOU 1496 CA ASN A1006 12361 21408 9867 455 197 1236 C ATOM 1497 C ASN A1006 -48.086 -9.100 -35.804 1.00120.96 C ANISOU 1497 C ASN A1006 12948 22251 10759 424 189 1271 C ATOM 1498 O ASN A1006 -48.452 -8.780 -36.934 1.00121.14 O ANISOU 1498 O ASN A1006 12792 22360 10876 508 220 1251 O ATOM 1499 CB ASN A1006 -46.510 -7.610 -34.561 1.00110.96 C ANISOU 1499 CB ASN A1006 11977 20756 9429 446 -11 1292 C ATOM 1500 CG ASN A1006 -46.360 -6.374 -33.698 1.00109.29 C ANISOU 1500 CG ASN A1006 11994 20452 9079 445 -20 1245 C ATOM 1501 OD1 ASN A1006 -47.244 -6.044 -32.907 1.00111.38 O ANISOU 1501 OD1 ASN A1006 12412 20730 9177 453 143 1177 O ATOM 1502 ND2 ASN A1006 -45.237 -5.681 -33.846 1.00107.22 N ANISOU 1502 ND2 ASN A1006 11778 20087 8874 418 -190 1281 N ATOM 1503 N TRP A1007 -47.786 -10.351 -35.465 1.00127.74 N ANISOU 1503 N TRP A1007 13905 23047 11585 298 146 1328 N ATOM 1504 CA TRP A1007 -47.847 -11.450 -36.424 1.00136.61 C ANISOU 1504 CA TRP A1007 14958 24174 12774 243 157 1357 C ATOM 1505 C TRP A1007 -49.276 -11.706 -36.892 1.00143.40 C ANISOU 1505 C TRP A1007 15676 25232 13578 150 299 1301 C ATOM 1506 O TRP A1007 -49.495 -12.313 -37.940 1.00147.79 O ANISOU 1506 O TRP A1007 16164 25817 14171 88 301 1307 O ATOM 1507 CB TRP A1007 -47.257 -12.723 -35.809 1.00142.00 C ANISOU 1507 CB TRP A1007 15850 24704 13401 147 98 1436 C ATOM 1508 CG TRP A1007 -47.230 -13.898 -36.743 1.00147.35 C ANISOU 1508 CG TRP A1007 16555 25316 14114 95 136 1464 C ATOM 1509 CD1 TRP A1007 -46.338 -14.122 -37.748 1.00148.43 C ANISOU 1509 CD1 TRP A1007 16657 25341 14398 210 102 1504 C ATOM 1510 CD2 TRP A1007 -48.132 -15.012 -36.751 1.00151.79 C ANISOU 1510 CD2 TRP A1007 17236 25899 14539 -108 241 1448 C ATOM 1511 NE1 TRP A1007 -46.628 -15.304 -38.386 1.00150.37 N ANISOU 1511 NE1 TRP A1007 17036 25508 14591 110 186 1508 N ATOM 1512 CE2 TRP A1007 -47.726 -15.870 -37.792 1.00152.14 C ANISOU 1512 CE2 TRP A1007 17362 25810 14634 -107 254 1475 C ATOM 1513 CE3 TRP A1007 -49.244 -15.366 -35.980 1.00155.85 C ANISOU 1513 CE3 TRP A1007 17812 26525 14879 -314 348 1412 C ATOM 1514 CZ2 TRP A1007 -48.390 -17.059 -38.082 1.00153.94 C ANISOU 1514 CZ2 TRP A1007 17773 25993 14723 -326 344 1464 C ATOM 1515 CZ3 TRP A1007 -49.903 -16.547 -36.270 1.00155.93 C ANISOU 1515 CZ3 TRP A1007 17948 26524 14773 -548 434 1409 C ATOM 1516 CH2 TRP A1007 -49.474 -17.379 -37.313 1.00155.55 C ANISOU 1516 CH2 TRP A1007 18022 26322 14758 -564 417 1434 C ATOM 1517 N GLU A1008 -50.246 -11.236 -36.115 1.00144.92 N ANISOU 1517 N GLU A1008 15824 25565 13675 129 421 1254 N ATOM 1518 CA GLU A1008 -51.652 -11.443 -36.440 1.00145.49 C ANISOU 1518 CA GLU A1008 15681 25883 13716 35 555 1222 C ATOM 1519 C GLU A1008 -52.292 -10.197 -37.047 1.00143.90 C ANISOU 1519 C GLU A1008 15219 25852 13605 241 589 1193 C ATOM 1520 O GLU A1008 -53.335 -10.284 -37.696 1.00151.78 O ANISOU 1520 O GLU A1008 15955 27082 14632 202 628 1197 O ATOM 1521 CB GLU A1008 -52.428 -11.870 -35.193 1.00147.68 C ANISOU 1521 CB GLU A1008 16040 26235 13837 -124 723 1202 C ATOM 1522 N THR A1009 -51.669 -9.040 -36.841 1.00137.48 N ANISOU 1522 N THR A1009 14490 24918 12826 450 558 1175 N ATOM 1523 CA THR A1009 -52.238 -7.786 -37.325 1.00133.57 C ANISOU 1523 CA THR A1009 13827 24527 12395 686 605 1155 C ATOM 1524 C THR A1009 -51.695 -7.398 -38.698 1.00130.29 C ANISOU 1524 C THR A1009 13359 24056 12089 780 451 1182 C ATOM 1525 O THR A1009 -52.304 -6.593 -39.402 1.00131.88 O ANISOU 1525 O THR A1009 13403 24366 12340 954 452 1190 O ATOM 1526 CB THR A1009 -51.982 -6.624 -36.340 1.00131.22 C ANISOU 1526 CB THR A1009 13734 24096 12028 850 693 1110 C ATOM 1527 OG1 THR A1009 -52.824 -5.515 -36.679 1.00131.86 O ANISOU 1527 OG1 THR A1009 13663 24286 12150 1109 802 1094 O ATOM 1528 CG2 THR A1009 -50.530 -6.182 -36.386 1.00128.01 C ANISOU 1528 CG2 THR A1009 13566 23435 11636 856 525 1120 C ATOM 1529 N LEU A1010 -50.555 -7.966 -39.081 1.00126.37 N ANISOU 1529 N LEU A1010 13001 23386 11627 683 333 1207 N ATOM 1530 CA LEU A1010 -49.999 -7.701 -40.403 1.00121.60 C ANISOU 1530 CA LEU A1010 12380 22714 11109 741 234 1228 C ATOM 1531 C LEU A1010 -50.456 -8.783 -41.374 1.00121.04 C ANISOU 1531 C LEU A1010 12225 22734 11030 584 203 1251 C ATOM 1532 O LEU A1010 -50.491 -8.569 -42.585 1.00122.71 O ANISOU 1532 O LEU A1010 12402 22955 11266 613 140 1265 O ATOM 1533 CB LEU A1010 -48.467 -7.611 -40.353 1.00118.07 C ANISOU 1533 CB LEU A1010 12102 22038 10723 741 161 1248 C ATOM 1534 CG LEU A1010 -47.599 -8.848 -40.101 1.00114.71 C ANISOU 1534 CG LEU A1010 11766 21496 10321 610 126 1291 C ATOM 1535 CD1 LEU A1010 -47.212 -9.532 -41.404 1.00111.92 C ANISOU 1535 CD1 LEU A1010 11410 21083 10031 576 126 1314 C ATOM 1536 CD2 LEU A1010 -46.353 -8.466 -39.315 1.00114.11 C ANISOU 1536 CD2 LEU A1010 11794 21275 10290 634 45 1325 C ATOM 1537 N ASN A1011 -50.808 -9.945 -40.832 1.00121.37 N ANISOU 1537 N ASN A1011 12291 22821 11005 389 247 1253 N ATOM 1538 CA ASN A1011 -51.385 -11.017 -41.631 1.00124.42 C ANISOU 1538 CA ASN A1011 12650 23289 11335 175 226 1267 C ATOM 1539 C ASN A1011 -52.832 -10.704 -41.990 1.00130.65 C ANISOU 1539 C ASN A1011 13153 24386 12100 141 216 1274 C ATOM 1540 O ASN A1011 -53.331 -11.129 -43.032 1.00137.56 O ANISOU 1540 O ASN A1011 13969 25360 12937 -3 128 1297 O ATOM 1541 CB ASN A1011 -51.304 -12.352 -40.887 1.00124.41 C ANISOU 1541 CB ASN A1011 12819 23208 11243 -43 285 1272 C ATOM 1542 CG ASN A1011 -49.903 -12.931 -40.879 1.00125.05 C ANISOU 1542 CG ASN A1011 13156 22996 11362 -3 264 1299 C ATOM 1543 OD1 ASN A1011 -48.938 -12.257 -41.237 1.00123.67 O ANISOU 1543 OD1 ASN A1011 12990 22702 11297 177 222 1311 O ATOM 1544 ND2 ASN A1011 -49.784 -14.187 -40.464 1.00128.69 N ANISOU 1544 ND2 ASN A1011 13822 23339 11736 -166 303 1320 N ATOM 1545 N ASP A1012 -53.498 -9.955 -41.118 1.00130.11 N ANISOU 1545 N ASP A1012 12913 24470 12052 277 307 1264 N ATOM 1546 CA ASP A1012 -54.882 -9.558 -41.344 1.00132.35 C ANISOU 1546 CA ASP A1012 12846 25081 12357 313 321 1293 C ATOM 1547 C ASP A1012 -54.961 -8.377 -42.305 1.00134.23 C ANISOU 1547 C ASP A1012 12978 25351 12671 584 210 1328 C ATOM 1548 O ASP A1012 -56.013 -8.105 -42.884 1.00141.67 O ANISOU 1548 O ASP A1012 13621 26563 13645 629 140 1387 O ATOM 1549 CB ASP A1012 -55.562 -9.206 -40.019 1.00132.87 C ANISOU 1549 CB ASP A1012 12787 25279 12418 396 525 1270 C ATOM 1550 N ASN A1013 -53.842 -7.679 -42.469 1.00130.02 N ANISOU 1550 N ASN A1013 12689 24547 12165 755 183 1305 N ATOM 1551 CA ASN A1013 -53.788 -6.519 -43.350 1.00126.09 C ANISOU 1551 CA ASN A1013 12185 24015 11710 1001 92 1336 C ATOM 1552 C ASN A1013 -53.216 -6.853 -44.725 1.00120.79 C ANISOU 1552 C ASN A1013 11657 23228 11009 885 -58 1359 C ATOM 1553 O ASN A1013 -53.200 -6.005 -45.618 1.00121.64 O ANISOU 1553 O ASN A1013 11798 23299 11119 1042 -152 1395 O ATOM 1554 CB ASN A1013 -52.972 -5.399 -42.703 1.00122.90 C ANISOU 1554 CB ASN A1013 11992 23379 11325 1228 174 1295 C ATOM 1555 CG ASN A1013 -53.767 -4.621 -41.671 1.00119.13 C ANISOU 1555 CG ASN A1013 11413 23003 10849 1444 332 1280 C ATOM 1556 OD1 ASN A1013 -54.327 -3.566 -41.970 1.00118.70 O ANISOU 1556 OD1 ASN A1013 11283 22995 10822 1726 344 1312 O ATOM 1557 ND2 ASN A1013 -53.826 -5.142 -40.451 1.00116.17 N ANISOU 1557 ND2 ASN A1013 11069 22640 10430 1330 471 1235 N ATOM 1558 N LEU A1014 -52.744 -8.084 -44.893 1.00115.64 N ANISOU 1558 N LEU A1014 11138 22490 10310 617 -59 1340 N ATOM 1559 CA LEU A1014 -52.305 -8.549 -46.204 1.00115.42 C ANISOU 1559 CA LEU A1014 11286 22346 10223 483 -152 1353 C ATOM 1560 C LEU A1014 -53.391 -9.418 -46.826 1.00120.28 C ANISOU 1560 C LEU A1014 11783 23182 10736 223 -263 1388 C ATOM 1561 O LEU A1014 -53.446 -9.586 -48.044 1.00122.67 O ANISOU 1561 O LEU A1014 12204 23457 10946 111 -385 1414 O ATOM 1562 CB LEU A1014 -50.976 -9.312 -46.108 1.00113.79 C ANISOU 1562 CB LEU A1014 11352 21856 10028 391 -56 1316 C ATOM 1563 CG LEU A1014 -50.855 -10.617 -45.313 1.00115.85 C ANISOU 1563 CG LEU A1014 11687 22074 10257 198 26 1297 C ATOM 1564 CD1 LEU A1014 -51.240 -11.834 -46.147 1.00116.98 C ANISOU 1564 CD1 LEU A1014 11969 22210 10267 -84 -2 1299 C ATOM 1565 CD2 LEU A1014 -49.439 -10.770 -44.779 1.00116.27 C ANISOU 1565 CD2 LEU A1014 11911 21871 10395 289 111 1290 C ATOM 1566 N LYS A1015 -54.254 -9.968 -45.977 1.00126.65 N ANISOU 1566 N LYS A1015 12379 24204 11537 90 -218 1390 N ATOM 1567 CA LYS A1015 -55.405 -10.732 -46.441 1.00128.38 C ANISOU 1567 CA LYS A1015 12423 24693 11663 -206 -334 1434 C ATOM 1568 C LYS A1015 -56.406 -9.797 -47.107 1.00129.00 C ANISOU 1568 C LYS A1015 12175 25059 11780 -54 -511 1524 C ATOM 1569 O LYS A1015 -57.076 -10.169 -48.071 1.00139.72 O ANISOU 1569 O LYS A1015 13463 26585 13041 -276 -714 1585 O ATOM 1570 CB LYS A1015 -56.063 -11.483 -45.282 1.00131.21 C ANISOU 1570 CB LYS A1015 12621 25221 12013 -396 -207 1418 C ATOM 1571 N VAL A1016 -56.500 -8.580 -46.582 1.00121.45 N ANISOU 1571 N VAL A1016 11050 24146 10951 326 -445 1539 N ATOM 1572 CA VAL A1016 -57.340 -7.551 -47.177 1.00118.61 C ANISOU 1572 CA VAL A1016 10413 24008 10645 577 -599 1641 C ATOM 1573 C VAL A1016 -56.612 -6.948 -48.378 1.00113.67 C ANISOU 1573 C VAL A1016 10095 23140 9954 685 -746 1660 C ATOM 1574 O VAL A1016 -57.233 -6.388 -49.282 1.00114.25 O ANISOU 1574 O VAL A1016 10051 23357 10002 788 -960 1763 O ATOM 1575 CB VAL A1016 -57.707 -6.449 -46.152 1.00118.43 C ANISOU 1575 CB VAL A1016 10173 24065 10762 979 -425 1646 C ATOM 1576 CG1 VAL A1016 -56.472 -5.664 -45.735 1.00117.66 C ANISOU 1576 CG1 VAL A1016 10447 23584 10676 1209 -287 1564 C ATOM 1577 CG2 VAL A1016 -58.778 -5.519 -46.710 1.00118.20 C ANISOU 1577 CG2 VAL A1016 9793 24312 10806 1269 -575 1780 C ATOM 1578 N ILE A1017 -55.289 -7.086 -48.386 1.00108.94 N ANISOU 1578 N ILE A1017 9887 22181 9324 655 -629 1572 N ATOM 1579 CA ILE A1017 -54.477 -6.636 -49.509 1.00105.77 C ANISOU 1579 CA ILE A1017 9814 21527 8849 701 -706 1577 C ATOM 1580 C ILE A1017 -54.501 -7.677 -50.622 1.00106.61 C ANISOU 1580 C ILE A1017 10112 21607 8788 348 -835 1585 C ATOM 1581 O ILE A1017 -54.430 -7.339 -51.803 1.00108.13 O ANISOU 1581 O ILE A1017 10497 21721 8866 337 -981 1630 O ATOM 1582 CB ILE A1017 -53.020 -6.367 -49.091 1.00100.96 C ANISOU 1582 CB ILE A1017 9495 20572 8293 793 -511 1491 C ATOM 1583 N GLU A1018 -54.599 -8.945 -50.235 1.00106.99 N ANISOU 1583 N GLU A1018 10169 21690 8792 47 -770 1541 N ATOM 1584 CA GLU A1018 -54.726 -10.032 -51.198 1.00109.47 C ANISOU 1584 CA GLU A1018 10720 21965 8911 -331 -873 1540 C ATOM 1585 C GLU A1018 -56.069 -9.938 -51.911 1.00112.96 C ANISOU 1585 C GLU A1018 10911 22752 9258 -477 -1177 1651 C ATOM 1586 O GLU A1018 -56.129 -9.847 -53.137 1.00112.93 O ANISOU 1586 O GLU A1018 11123 22697 9089 -587 -1368 1698 O ATOM 1587 CB GLU A1018 -54.582 -11.390 -50.508 1.00111.42 C ANISOU 1587 CB GLU A1018 11067 22148 9118 -611 -724 1473 C ATOM 1588 N LYS A1019 -57.145 -9.958 -51.132 1.00117.67 N ANISOU 1588 N LYS A1019 11044 23712 9955 -486 -1221 1704 N ATOM 1589 CA LYS A1019 -58.487 -9.789 -51.674 1.00124.57 C ANISOU 1589 CA LYS A1019 11541 24995 10796 -587 -1522 1840 C ATOM 1590 C LYS A1019 -58.846 -8.309 -51.744 1.00131.66 C ANISOU 1590 C LYS A1019 12163 26023 11839 -105 -1616 1942 C ATOM 1591 O LYS A1019 -59.644 -7.815 -50.946 1.00131.67 O ANISOU 1591 O LYS A1019 11695 26317 12016 124 -1571 2000 O ATOM 1592 CB LYS A1019 -59.511 -10.545 -50.826 1.00125.68 C ANISOU 1592 CB LYS A1019 11268 25497 10990 -842 -1495 1862 C ATOM 1593 N AALA A1020 -58.251 -7.606 -52.702 0.44134.72 N ANISOU 1593 N AALA A1020 12879 26168 12139 56 -1719 1963 N ATOM 1594 N BALA A1020 -58.251 -7.606 -52.702 0.56134.66 N ANISOU 1594 N BALA A1020 12872 26162 12133 56 -1719 1963 N ATOM 1595 CA ALA A1020 -58.495 -6.179 -52.870 1.00140.61 C ANISOU 1595 CA ALA A1020 13485 26958 12984 520 -1809 2063 C ATOM 1596 C ALA A1020 -59.212 -5.893 -54.185 1.00150.49 C ANISOU 1596 C ALA A1020 14717 28373 14088 467 -2210 2225 C ATOM 1597 O ALA A1020 -58.756 -6.302 -55.253 1.00152.16 O ANISOU 1597 O ALA A1020 15361 28382 14070 191 -2340 2211 O ATOM 1598 CB ALA A1020 -57.188 -5.406 -52.801 1.00137.83 C ANISOU 1598 CB ALA A1020 13552 26170 12648 780 -1591 1969 C ATOM 1599 N ASP A1021 -60.334 -5.187 -54.099 1.00158.29 N ANISOU 1599 N ASP A1021 15215 29725 15204 744 -2401 2389 N ATOM 1600 CA ASP A1021 -61.113 -4.842 -55.282 1.00161.09 C ANISOU 1600 CA ASP A1021 15483 30286 15436 738 -2840 2585 C ATOM 1601 C ASP A1021 -60.566 -3.591 -55.962 1.00162.36 C ANISOU 1601 C ASP A1021 16022 30134 15532 1132 -2900 2637 C ATOM 1602 O ASP A1021 -60.504 -3.518 -57.189 1.00164.41 O ANISOU 1602 O ASP A1021 16614 30294 15561 989 -3189 2719 O ATOM 1603 CB ASP A1021 -62.584 -4.640 -54.914 1.00165.46 C ANISOU 1603 CB ASP A1021 15282 31403 16182 895 -3033 2771 C ATOM 1604 N ASN A1022 -60.170 -2.610 -55.158 1.00171.02 N ANISOU 1604 N ASN A1022 17121 31056 16803 1598 -2620 2589 N ATOM 1605 CA ASN A1022 -59.643 -1.356 -55.685 1.00182.53 C ANISOU 1605 CA ASN A1022 18969 32188 18196 1971 -2636 2633 C ATOM 1606 C ASN A1022 -58.453 -0.847 -54.879 1.00177.23 C ANISOU 1606 C ASN A1022 18631 31112 17597 2144 -2222 2455 C ATOM 1607 O ASN A1022 -58.153 -1.365 -53.804 1.00178.83 O ANISOU 1607 O ASN A1022 18697 31323 17926 2054 -1941 2319 O ATOM 1608 CB ASN A1022 -60.741 -0.291 -55.716 1.00118.95 C ANISOU 1608 CB ASN A1022 10534 24394 10269 2478 -2845 2851 C ATOM 1609 N ALA A1023 -57.780 0.170 -55.408 1.00161.71 N ANISOU 1609 N ALA A1023 17120 28793 15531 2364 -2202 2465 N ATOM 1610 CA ALA A1023 -56.653 0.783 -54.715 1.00159.57 C ANISOU 1610 CA ALA A1023 17174 28146 15310 2500 -1851 2317 C ATOM 1611 C ALA A1023 -57.141 1.591 -53.518 1.00165.57 C ANISOU 1611 C ALA A1023 17658 28984 16266 2936 -1674 2327 C ATOM 1612 O ALA A1023 -56.391 1.836 -52.574 1.00162.76 O ANISOU 1612 O ALA A1023 17447 28415 15978 2979 -1372 2189 O ATOM 1613 CB ALA A1023 -55.856 1.661 -55.665 1.00159.74 C ANISOU 1613 CB ALA A1023 17773 27775 15146 2565 -1880 2336 C ATOM 1614 N ALA A1024 -58.405 2.002 -53.570 1.00176.13 N ANISOU 1614 N ALA A1024 18602 30631 17687 3260 -1862 2500 N ATOM 1615 CA ALA A1024 -59.028 2.718 -52.464 1.00180.36 C ANISOU 1615 CA ALA A1024 18846 31270 18413 3711 -1660 2523 C ATOM 1616 C ALA A1024 -59.180 1.797 -51.258 1.00179.97 C ANISOU 1616 C ALA A1024 18430 31441 18510 3510 -1419 2399 C ATOM 1617 O ALA A1024 -59.117 2.240 -50.111 1.00180.67 O ANISOU 1617 O ALA A1024 18500 31447 18700 3740 -1114 2317 O ATOM 1618 CB ALA A1024 -60.378 3.276 -52.883 1.00185.30 C ANISOU 1618 CB ALA A1024 19067 32220 19120 4121 -1919 2764 C ATOM 1619 N GLN A1025 -59.378 0.511 -51.530 1.00172.12 N ANISOU 1619 N GLN A1025 17207 30698 17493 3058 -1554 2386 N ATOM 1620 CA GLN A1025 -59.455 -0.499 -50.482 1.00164.36 C ANISOU 1620 CA GLN A1025 15954 29890 16606 2792 -1343 2270 C ATOM 1621 C GLN A1025 -58.077 -0.699 -49.857 1.00156.33 C ANISOU 1621 C GLN A1025 15375 28485 15540 2612 -1072 2072 C ATOM 1622 O GLN A1025 -57.955 -1.135 -48.712 1.00152.87 O ANISOU 1622 O GLN A1025 14834 28073 15177 2532 -831 1967 O ATOM 1623 CB GLN A1025 -59.992 -1.817 -51.046 1.00162.58 C ANISOU 1623 CB GLN A1025 15463 29985 16326 2320 -1577 2315 C ATOM 1624 CG GLN A1025 -60.298 -2.880 -50.002 1.00157.55 C ANISOU 1624 CG GLN A1025 14516 29570 15774 2040 -1382 2227 C ATOM 1625 CD GLN A1025 -60.894 -4.137 -50.608 1.00153.27 C ANISOU 1625 CD GLN A1025 13759 29329 15147 1542 -1625 2279 C ATOM 1626 OE1 GLN A1025 -61.045 -4.241 -51.825 1.00152.01 O ANISOU 1626 OE1 GLN A1025 13702 29205 14848 1386 -1953 2375 O ATOM 1627 NE2 GLN A1025 -61.236 -5.099 -49.759 1.00151.42 N ANISOU 1627 NE2 GLN A1025 13277 29293 14964 1259 -1467 2216 N ATOM 1628 N VAL A1026 -57.043 -0.369 -50.623 1.00154.16 N ANISOU 1628 N VAL A1026 15581 27858 15134 2542 -1119 2035 N ATOM 1629 CA VAL A1026 -55.666 -0.462 -50.156 1.00151.55 C ANISOU 1629 CA VAL A1026 15630 27178 14775 2384 -895 1877 C ATOM 1630 C VAL A1026 -55.200 0.896 -49.630 1.00157.03 C ANISOU 1630 C VAL A1026 16595 27589 15481 2728 -729 1847 C ATOM 1631 O VAL A1026 -54.225 0.988 -48.884 1.00157.04 O ANISOU 1631 O VAL A1026 16822 27356 15489 2645 -529 1728 O ATOM 1632 CB VAL A1026 -54.724 -0.941 -51.281 1.00145.31 C ANISOU 1632 CB VAL A1026 15199 26170 13842 2072 -987 1847 C ATOM 1633 CG1 VAL A1026 -53.383 -1.381 -50.714 1.00138.09 C ANISOU 1633 CG1 VAL A1026 14518 24999 12950 1864 -756 1703 C ATOM 1634 CG2 VAL A1026 -55.366 -2.082 -52.054 1.00147.89 C ANISOU 1634 CG2 VAL A1026 15355 26745 14092 1761 -1200 1903 C ATOM 1635 N LYS A1027 -55.919 1.948 -50.012 1.00162.98 N ANISOU 1635 N LYS A1027 17339 28361 16227 3112 -826 1968 N ATOM 1636 CA LYS A1027 -55.564 3.310 -49.625 1.00166.34 C ANISOU 1636 CA LYS A1027 18105 28473 16622 3453 -673 1951 C ATOM 1637 C LYS A1027 -55.748 3.559 -48.130 1.00169.99 C ANISOU 1637 C LYS A1027 18469 28941 17177 3625 -390 1866 C ATOM 1638 O LYS A1027 -55.242 4.543 -47.591 1.00169.80 O ANISOU 1638 O LYS A1027 18815 28605 17098 3802 -217 1806 O ATOM 1639 CB LYS A1027 -56.392 4.321 -50.422 1.00171.88 C ANISOU 1639 CB LYS A1027 18833 29188 17286 3869 -852 2124 C ATOM 1640 N ASP A1028 -56.477 2.669 -47.463 1.00174.03 N ANISOU 1640 N ASP A1028 18529 29791 17803 3542 -336 1858 N ATOM 1641 CA ASP A1028 -56.718 2.803 -46.031 1.00177.95 C ANISOU 1641 CA ASP A1028 18945 30306 18362 3675 -45 1775 C ATOM 1642 C ASP A1028 -56.192 1.597 -45.259 1.00177.01 C ANISOU 1642 C ASP A1028 18754 30249 18253 3251 48 1655 C ATOM 1643 O ASP A1028 -55.833 1.709 -44.087 1.00178.13 O ANISOU 1643 O ASP A1028 19048 30258 18375 3238 273 1551 O ATOM 1644 CB ASP A1028 -58.211 2.990 -45.756 1.00182.51 C ANISOU 1644 CB ASP A1028 19039 31235 19070 4038 9 1891 C ATOM 1645 N ALA A1029 -56.148 0.447 -45.922 1.00175.55 N ANISOU 1645 N ALA A1029 18387 30240 18074 2904 -131 1674 N ATOM 1646 CA ALA A1029 -55.720 -0.792 -45.281 1.00168.39 C ANISOU 1646 CA ALA A1029 17425 29386 17171 2522 -60 1582 C ATOM 1647 C ALA A1029 -54.200 -0.896 -45.198 1.00159.85 C ANISOU 1647 C ALA A1029 16750 27962 16025 2305 -30 1484 C ATOM 1648 O ALA A1029 -53.657 -1.342 -44.187 1.00157.65 O ANISOU 1648 O ALA A1029 16549 27606 15744 2151 100 1400 O ATOM 1649 CB ALA A1029 -56.291 -1.990 -46.021 1.00169.21 C ANISOU 1649 CB ALA A1029 17231 29778 17281 2232 -245 1642 C ATOM 1650 N LEU A1030 -53.517 -0.488 -46.263 1.00163.84 N ANISOU 1650 N LEU A1030 17502 28273 16476 2287 -154 1508 N ATOM 1651 CA LEU A1030 -52.060 -0.560 -46.307 1.00162.08 C ANISOU 1651 CA LEU A1030 17598 27763 16221 2081 -118 1436 C ATOM 1652 C LEU A1030 -51.422 0.490 -45.405 1.00158.17 C ANISOU 1652 C LEU A1030 17376 27021 15700 2208 21 1376 C ATOM 1653 O LEU A1030 -50.300 0.314 -44.930 1.00159.79 O ANISOU 1653 O LEU A1030 17747 27061 15906 2010 69 1314 O ATOM 1654 CB LEU A1030 -51.556 -0.390 -47.741 1.00163.40 C ANISOU 1654 CB LEU A1030 17962 27798 16326 2012 -246 1479 C ATOM 1655 N THR A1031 -52.144 1.582 -45.171 1.00153.94 N ANISOU 1655 N THR A1031 16896 26459 15136 2538 79 1403 N ATOM 1656 CA THR A1031 -51.650 2.660 -44.320 1.00153.22 C ANISOU 1656 CA THR A1031 17148 26098 14973 2655 222 1341 C ATOM 1657 C THR A1031 -51.608 2.235 -42.856 1.00153.38 C ANISOU 1657 C THR A1031 17132 26153 14991 2557 370 1260 C ATOM 1658 O THR A1031 -50.912 2.844 -42.043 1.00156.11 O ANISOU 1658 O THR A1031 17803 26263 15250 2506 457 1192 O ATOM 1659 CB THR A1031 -52.516 3.925 -44.453 1.00158.74 C ANISOU 1659 CB THR A1031 17967 26722 15624 3087 282 1396 C ATOM 1660 OG1 THR A1031 -53.878 3.612 -44.135 1.00164.35 O ANISOU 1660 OG1 THR A1031 18276 27746 16422 3321 338 1449 O ATOM 1661 CG2 THR A1031 -52.445 4.473 -45.870 1.00161.67 C ANISOU 1661 CG2 THR A1031 18480 26995 15952 3179 117 1485 C ATOM 1662 N LYS A1032 -52.357 1.187 -42.526 1.00148.36 N ANISOU 1662 N LYS A1032 16137 25807 14428 2495 388 1271 N ATOM 1663 CA LYS A1032 -52.382 0.654 -41.169 1.00144.66 C ANISOU 1663 CA LYS A1032 15649 25380 13934 2374 529 1203 C ATOM 1664 C LYS A1032 -51.095 -0.104 -40.856 1.00143.66 C ANISOU 1664 C LYS A1032 15654 25133 13796 2020 445 1162 C ATOM 1665 O LYS A1032 -50.791 -0.378 -39.695 1.00145.34 O ANISOU 1665 O LYS A1032 15978 25295 13951 1894 518 1111 O ATOM 1666 CB LYS A1032 -53.594 -0.261 -40.976 1.00142.13 C ANISOU 1666 CB LYS A1032 14908 25410 13686 2379 584 1237 C ATOM 1667 CG LYS A1032 -54.933 0.426 -41.200 1.00140.89 C ANISOU 1667 CG LYS A1032 14511 25439 13582 2754 671 1305 C ATOM 1668 CD LYS A1032 -56.085 -0.566 -41.147 1.00137.28 C ANISOU 1668 CD LYS A1032 13562 25384 13215 2680 693 1356 C ATOM 1669 CE LYS A1032 -56.162 -1.259 -39.797 1.00132.00 C ANISOU 1669 CE LYS A1032 12896 24760 12500 2494 902 1277 C ATOM 1670 NZ LYS A1032 -57.299 -2.217 -39.728 1.00129.79 N ANISOU 1670 NZ LYS A1032 12146 24874 12296 2373 948 1327 N ATOM 1671 N MET A1033 -50.343 -0.437 -41.901 1.00142.71 N ANISOU 1671 N MET A1033 15529 24967 13728 1875 297 1194 N ATOM 1672 CA MET A1033 -49.093 -1.173 -41.751 1.00141.00 C ANISOU 1672 CA MET A1033 15378 24655 13542 1594 226 1181 C ATOM 1673 C MET A1033 -47.889 -0.237 -41.744 1.00137.78 C ANISOU 1673 C MET A1033 15260 23989 13100 1533 195 1165 C ATOM 1674 O MET A1033 -46.744 -0.688 -41.727 1.00137.93 O ANISOU 1674 O MET A1033 15294 23940 13173 1323 127 1177 O ATOM 1675 CB MET A1033 -48.942 -2.202 -42.874 1.00143.65 C ANISOU 1675 CB MET A1033 15542 25085 13953 1461 136 1224 C ATOM 1676 CG MET A1033 -50.061 -3.226 -42.937 1.00148.97 C ANISOU 1676 CG MET A1033 15954 26012 14638 1427 139 1243 C ATOM 1677 SD MET A1033 -49.930 -4.301 -44.379 1.00156.16 S ANISOU 1677 SD MET A1033 16790 26973 15572 1251 36 1284 S ATOM 1678 CE MET A1033 -48.303 -5.006 -44.131 1.00 91.57 C ANISOU 1678 CE MET A1033 8760 18583 7451 1068 60 1269 C ATOM 1679 N ARG A1034 -48.156 1.066 -41.761 1.00134.93 N ANISOU 1679 N ARG A1034 15127 23488 12652 1718 250 1149 N ATOM 1680 CA ARG A1034 -47.098 2.070 -41.792 1.00132.32 C ANISOU 1680 CA ARG A1034 15121 22898 12256 1621 226 1132 C ATOM 1681 C ARG A1034 -46.229 2.009 -40.539 1.00132.13 C ANISOU 1681 C ARG A1034 15241 22783 12180 1391 200 1095 C ATOM 1682 O ARG A1034 -45.016 2.212 -40.603 1.00126.81 O ANISOU 1682 O ARG A1034 14666 21995 11522 1161 112 1109 O ATOM 1683 CB ARG A1034 -47.694 3.470 -41.947 1.00133.28 C ANISOU 1683 CB ARG A1034 15534 22849 12256 1886 312 1120 C ATOM 1684 N ALA A1035 -46.857 1.729 -39.402 1.00138.79 N ANISOU 1684 N ALA A1035 16090 23689 12953 1436 271 1059 N ATOM 1685 CA ALA A1035 -46.139 1.618 -38.139 1.00142.80 C ANISOU 1685 CA ALA A1035 16775 24114 13369 1209 218 1034 C ATOM 1686 C ALA A1035 -46.333 0.236 -37.524 1.00139.11 C ANISOU 1686 C ALA A1035 16065 23834 12956 1117 190 1055 C ATOM 1687 O ALA A1035 -47.281 0.009 -36.772 1.00142.65 O ANISOU 1687 O ALA A1035 16520 24356 13323 1214 321 1019 O ATOM 1688 CB ALA A1035 -46.595 2.699 -37.172 1.00147.70 C ANISOU 1688 CB ALA A1035 17798 24547 13774 1307 354 960 C ATOM 1689 N ALA A1036 -45.430 -0.683 -37.851 1.00130.66 N ANISOU 1689 N ALA A1036 14797 22828 12020 940 45 1118 N ATOM 1690 CA ALA A1036 -45.503 -2.046 -37.336 1.00131.78 C ANISOU 1690 CA ALA A1036 14764 23102 12204 853 7 1152 C ATOM 1691 C ALA A1036 -44.122 -2.692 -37.295 1.00129.69 C ANISOU 1691 C ALA A1036 14413 22813 12050 659 -175 1234 C ATOM 1692 O ALA A1036 -43.912 -3.767 -37.856 1.00128.33 O ANISOU 1692 O ALA A1036 14021 22724 12014 655 -195 1288 O ATOM 1693 CB ALA A1036 -46.453 -2.881 -38.180 1.00133.57 C ANISOU 1693 CB ALA A1036 14723 23505 12522 970 93 1160 C ATOM 1694 N PHE A1061 -30.034 -5.198 -35.085 1.00144.71 N ANISOU 1694 N PHE A1061 13567 25620 15796 -594 -2411 2889 N ATOM 1695 CA PHE A1061 -30.201 -4.602 -36.404 1.00143.65 C ANISOU 1695 CA PHE A1061 13402 25435 15743 -576 -2027 2746 C ATOM 1696 C PHE A1061 -31.309 -3.553 -36.405 1.00142.43 C ANISOU 1696 C PHE A1061 13797 25082 15236 -736 -1912 2508 C ATOM 1697 O PHE A1061 -32.492 -3.886 -36.481 1.00139.80 O ANISOU 1697 O PHE A1061 13778 24602 14737 -534 -1731 2366 O ATOM 1698 CB PHE A1061 -30.503 -5.683 -37.445 1.00141.47 C ANISOU 1698 CB PHE A1061 12984 25104 15663 -160 -1657 2724 C ATOM 1699 N ARG A1062 -30.917 -2.284 -36.320 1.00145.81 N ANISOU 1699 N ARG A1062 14337 25510 15556 -1100 -2012 2474 N ATOM 1700 CA ARG A1062 -31.870 -1.179 -36.365 1.00154.19 C ANISOU 1700 CA ARG A1062 15937 26355 16293 -1224 -1883 2263 C ATOM 1701 C ARG A1062 -32.469 -1.049 -37.762 1.00159.24 C ANISOU 1701 C ARG A1062 16612 26896 16995 -1003 -1476 2132 C ATOM 1702 O ARG A1062 -33.518 -0.433 -37.949 1.00156.77 O ANISOU 1702 O ARG A1062 16713 26403 16448 -945 -1319 1965 O ATOM 1703 CB ARG A1062 -31.197 0.131 -35.952 1.00157.55 C ANISOU 1703 CB ARG A1062 16523 26768 16571 -1695 -2091 2271 C ATOM 1704 N HIS A1063 -31.784 -1.637 -38.737 1.00164.58 N ANISOU 1704 N HIS A1063 16858 27690 17983 -867 -1307 2219 N ATOM 1705 CA HIS A1063 -32.259 -1.694 -40.114 1.00166.47 C ANISOU 1705 CA HIS A1063 17132 27839 18281 -660 -932 2117 C ATOM 1706 C HIS A1063 -33.499 -2.577 -40.225 1.00168.50 C ANISOU 1706 C HIS A1063 17576 28003 18442 -329 -797 2024 C ATOM 1707 O HIS A1063 -34.242 -2.509 -41.205 1.00165.47 O ANISOU 1707 O HIS A1063 17353 27517 18001 -184 -545 1912 O ATOM 1708 CB HIS A1063 -31.144 -2.213 -41.026 1.00166.87 C ANISOU 1708 CB HIS A1063 16693 28031 18679 -600 -762 2243 C ATOM 1709 CG HIS A1063 -31.595 -2.557 -42.412 1.00160.74 C ANISOU 1709 CG HIS A1063 15974 27150 17950 -364 -375 2153 C ATOM 1710 ND1 HIS A1063 -32.085 -1.616 -43.292 1.00157.76 N ANISOU 1710 ND1 HIS A1063 15910 26625 17408 -450 -182 2019 N ATOM 1711 CD2 HIS A1063 -31.624 -3.739 -43.071 1.00156.37 C ANISOU 1711 CD2 HIS A1063 15258 26596 17562 -60 -154 2182 C ATOM 1712 CE1 HIS A1063 -32.399 -2.205 -44.432 1.00154.07 C ANISOU 1712 CE1 HIS A1063 15457 26087 16994 -227 117 1973 C ATOM 1713 NE2 HIS A1063 -32.128 -3.494 -44.324 1.00153.08 N ANISOU 1713 NE2 HIS A1063 15060 26041 17062 1 153 2062 N ATOM 1714 N GLY A1064 -33.716 -3.396 -39.200 1.00175.42 N ANISOU 1714 N GLY A1064 18446 28920 19286 -242 -984 2081 N ATOM 1715 CA GLY A1064 -34.810 -4.349 -39.176 1.00175.04 C ANISOU 1715 CA GLY A1064 18547 28807 19152 16 -876 2014 C ATOM 1716 C GLY A1064 -36.191 -3.777 -39.436 1.00171.64 C ANISOU 1716 C GLY A1064 18486 28255 18476 66 -729 1836 C ATOM 1717 O GLY A1064 -36.920 -4.267 -40.299 1.00169.05 O ANISOU 1717 O GLY A1064 18188 27891 18153 249 -520 1769 O ATOM 1718 N PHE A1065 -36.553 -2.739 -38.691 1.00168.42 N ANISOU 1718 N PHE A1065 18365 27780 17845 -94 -842 1766 N ATOM 1719 CA PHE A1065 -37.877 -2.141 -38.814 1.00163.14 C ANISOU 1719 CA PHE A1065 18025 27006 16957 1 -702 1616 C ATOM 1720 C PHE A1065 -38.013 -1.312 -40.088 1.00157.73 C ANISOU 1720 C PHE A1065 17406 26244 16280 34 -516 1551 C ATOM 1721 O PHE A1065 -39.122 -1.062 -40.556 1.00160.11 O ANISOU 1721 O PHE A1065 17878 26488 16466 196 -378 1458 O ATOM 1722 CB PHE A1065 -38.183 -1.271 -37.593 1.00164.82 C ANISOU 1722 CB PHE A1065 18581 27129 16914 -149 -835 1563 C ATOM 1723 N ASP A1066 -36.882 -0.897 -40.650 1.00151.07 N ANISOU 1723 N ASP A1066 16416 25411 15573 -126 -516 1613 N ATOM 1724 CA ASP A1066 -36.883 -0.004 -41.805 1.00145.33 C ANISOU 1724 CA ASP A1066 15818 24582 14820 -150 -347 1559 C ATOM 1725 C ASP A1066 -36.998 -0.765 -43.126 1.00141.14 C ANISOU 1725 C ASP A1066 15123 24078 14428 29 -134 1564 C ATOM 1726 O ASP A1066 -37.576 -0.263 -44.090 1.00140.37 O ANISOU 1726 O ASP A1066 15217 23881 14235 106 9 1498 O ATOM 1727 CB ASP A1066 -35.616 0.857 -41.804 1.00147.92 C ANISOU 1727 CB ASP A1066 16098 24903 15202 -468 -418 1619 C ATOM 1728 CG ASP A1066 -35.808 2.186 -42.514 1.00150.45 C ANISOU 1728 CG ASP A1066 16769 25038 15357 -564 -298 1539 C ATOM 1729 OD1 ASP A1066 -36.619 2.252 -43.462 1.00150.52 O ANISOU 1729 OD1 ASP A1066 16925 24961 15306 -353 -123 1475 O ATOM 1730 OD2 ASP A1066 -35.146 3.169 -42.121 1.00153.77 O ANISOU 1730 OD2 ASP A1066 17346 25390 15690 -869 -397 1549 O ATOM 1731 N ILE A1067 -36.452 -1.978 -43.165 1.00140.25 N ANISOU 1731 N ILE A1067 14696 24075 14517 103 -115 1647 N ATOM 1732 CA ILE A1067 -36.439 -2.772 -44.392 1.00137.61 C ANISOU 1732 CA ILE A1067 14258 23730 14296 252 113 1651 C ATOM 1733 C ILE A1067 -37.849 -3.195 -44.806 1.00135.02 C ANISOU 1733 C ILE A1067 14135 23358 13810 431 180 1560 C ATOM 1734 O ILE A1067 -38.084 -3.560 -45.958 1.00136.56 O ANISOU 1734 O ILE A1067 14381 23503 14002 509 354 1535 O ATOM 1735 CB ILE A1067 -35.552 -4.030 -44.239 1.00135.84 C ANISOU 1735 CB ILE A1067 13695 23602 14317 334 137 1768 C ATOM 1736 CG1 ILE A1067 -35.125 -4.562 -45.610 1.00135.06 C ANISOU 1736 CG1 ILE A1067 13515 23454 14347 431 437 1778 C ATOM 1737 CG2 ILE A1067 -36.269 -5.103 -43.433 1.00133.51 C ANISOU 1737 CG2 ILE A1067 13425 23332 13971 480 31 1772 C ATOM 1738 CD1 ILE A1067 -34.279 -5.816 -45.544 1.00136.01 C ANISOU 1738 CD1 ILE A1067 13333 23631 14714 582 520 1896 C ATOM 1739 N LEU A1068 -38.786 -3.135 -43.865 1.00132.29 N ANISOU 1739 N LEU A1068 13907 23036 13321 474 43 1517 N ATOM 1740 CA LEU A1068 -40.170 -3.500 -44.139 1.00130.17 C ANISOU 1740 CA LEU A1068 13763 22778 12917 617 84 1447 C ATOM 1741 C LEU A1068 -41.071 -2.269 -44.133 1.00132.19 C ANISOU 1741 C LEU A1068 14251 22983 12993 655 61 1376 C ATOM 1742 O LEU A1068 -42.147 -2.275 -44.730 1.00134.82 O ANISOU 1742 O LEU A1068 14659 23334 13231 778 103 1336 O ATOM 1743 CB LEU A1068 -40.668 -4.525 -43.119 1.00128.75 C ANISOU 1743 CB LEU A1068 13518 22680 12723 661 3 1459 C ATOM 1744 N VAL A1069 -40.624 -1.216 -43.455 1.00132.57 N ANISOU 1744 N VAL A1069 14422 22963 12987 551 -15 1370 N ATOM 1745 CA VAL A1069 -41.378 0.031 -43.390 1.00131.63 C ANISOU 1745 CA VAL A1069 14586 22741 12688 617 -9 1307 C ATOM 1746 C VAL A1069 -41.413 0.715 -44.751 1.00129.47 C ANISOU 1746 C VAL A1069 14453 22363 12378 655 89 1300 C ATOM 1747 O VAL A1069 -42.482 1.061 -45.255 1.00131.71 O ANISOU 1747 O VAL A1069 14863 22628 12553 840 116 1274 O ATOM 1748 CB VAL A1069 -40.784 1.003 -42.355 1.00133.47 C ANISOU 1748 CB VAL A1069 15010 22871 12831 448 -102 1298 C ATOM 1749 N GLY A1070 -40.237 0.908 -45.340 1.00126.37 N ANISOU 1749 N GLY A1070 14027 21912 12074 478 139 1338 N ATOM 1750 CA GLY A1070 -40.137 1.491 -46.664 1.00124.25 C ANISOU 1750 CA GLY A1070 13929 21526 11755 471 255 1336 C ATOM 1751 C GLY A1070 -40.682 0.546 -47.716 1.00121.41 C ANISOU 1751 C GLY A1070 13484 21228 11419 601 333 1342 C ATOM 1752 O GLY A1070 -41.189 0.977 -48.751 1.00121.34 O ANISOU 1752 O GLY A1070 13680 21133 11290 673 377 1335 O ATOM 1753 N GLN A1071 -40.576 -0.751 -47.442 1.00119.36 N ANISOU 1753 N GLN A1071 12966 21098 11288 618 339 1361 N ATOM 1754 CA GLN A1071 -41.100 -1.775 -48.336 1.00116.38 C ANISOU 1754 CA GLN A1071 12555 20761 10903 698 409 1359 C ATOM 1755 C GLN A1071 -42.622 -1.710 -48.385 1.00116.21 C ANISOU 1755 C GLN A1071 12618 20807 10730 848 304 1331 C ATOM 1756 O GLN A1071 -43.228 -1.899 -49.439 1.00114.74 O ANISOU 1756 O GLN A1071 12536 20613 10449 885 316 1333 O ATOM 1757 CB GLN A1071 -40.640 -3.163 -47.887 1.00113.44 C ANISOU 1757 CB GLN A1071 11944 20475 10684 687 443 1389 C ATOM 1758 CG GLN A1071 -41.006 -4.287 -48.841 1.00110.20 C ANISOU 1758 CG GLN A1071 11572 20054 10245 723 550 1381 C ATOM 1759 CD GLN A1071 -40.469 -5.629 -48.386 1.00106.28 C ANISOU 1759 CD GLN A1071 10905 19586 9891 739 610 1417 C ATOM 1760 OE1 GLN A1071 -39.925 -5.753 -47.289 1.00106.86 O ANISOU 1760 OE1 GLN A1071 10801 19716 10085 739 530 1460 O ATOM 1761 NE2 GLN A1071 -40.617 -6.644 -49.231 1.00103.68 N ANISOU 1761 NE2 GLN A1071 10675 19194 9525 751 744 1407 N ATOM 1762 N ILE A1072 -43.232 -1.439 -47.236 1.00119.10 N ANISOU 1762 N ILE A1072 12935 21247 11070 923 203 1314 N ATOM 1763 CA ILE A1072 -44.677 -1.271 -47.157 1.00123.44 C ANISOU 1763 CA ILE A1072 13496 21895 11510 1089 128 1301 C ATOM 1764 C ILE A1072 -45.085 0.077 -47.740 1.00129.61 C ANISOU 1764 C ILE A1072 14514 22563 12169 1216 108 1308 C ATOM 1765 O ILE A1072 -46.188 0.232 -48.265 1.00131.82 O ANISOU 1765 O ILE A1072 14802 22916 12366 1373 43 1331 O ATOM 1766 CB ILE A1072 -45.185 -1.375 -45.707 1.00122.59 C ANISOU 1766 CB ILE A1072 13285 21888 11406 1142 87 1277 C ATOM 1767 N ASP A1073 -44.186 1.051 -47.642 1.00134.19 N ANISOU 1767 N ASP A1073 15290 22965 12733 1137 151 1299 N ATOM 1768 CA ASP A1073 -44.425 2.376 -48.201 1.00133.67 C ANISOU 1768 CA ASP A1073 15535 22725 12527 1241 150 1309 C ATOM 1769 C ASP A1073 -44.232 2.360 -49.713 1.00131.06 C ANISOU 1769 C ASP A1073 15341 22316 12141 1191 181 1345 C ATOM 1770 O ASP A1073 -44.831 3.159 -50.434 1.00130.49 O ANISOU 1770 O ASP A1073 15508 22145 11928 1334 135 1379 O ATOM 1771 CB ASP A1073 -43.496 3.408 -47.558 1.00135.39 C ANISOU 1771 CB ASP A1073 15975 22754 12712 1104 189 1284 C ATOM 1772 N ASP A1074 -43.391 1.446 -50.186 1.00125.40 N ANISOU 1772 N ASP A1074 14500 21626 11521 1003 270 1345 N ATOM 1773 CA ASP A1074 -43.146 1.295 -51.615 1.00123.48 C ANISOU 1773 CA ASP A1074 14422 21291 11203 927 347 1367 C ATOM 1774 C ASP A1074 -44.378 0.733 -52.314 1.00124.00 C ANISOU 1774 C ASP A1074 14483 21468 11163 1050 224 1394 C ATOM 1775 O ASP A1074 -44.662 1.074 -53.462 1.00120.93 O ANISOU 1775 O ASP A1074 14345 20984 10616 1060 194 1430 O ATOM 1776 CB ASP A1074 -41.938 0.390 -51.863 1.00121.43 C ANISOU 1776 CB ASP A1074 14021 21029 11089 731 525 1359 C ATOM 1777 N ALA A1075 -45.105 -0.131 -51.613 1.00127.88 N ANISOU 1777 N ALA A1075 14701 22165 11723 1112 140 1385 N ATOM 1778 CA ALA A1075 -46.322 -0.725 -52.151 1.00132.70 C ANISOU 1778 CA ALA A1075 15245 22932 12242 1174 -4 1419 C ATOM 1779 C ALA A1075 -47.440 0.308 -52.228 1.00133.52 C ANISOU 1779 C ALA A1075 15404 23080 12246 1415 -169 1478 C ATOM 1780 O ALA A1075 -48.312 0.232 -53.094 1.00135.82 O ANISOU 1780 O ALA A1075 15732 23454 12420 1465 -325 1542 O ATOM 1781 CB ALA A1075 -46.753 -1.913 -51.306 1.00134.81 C ANISOU 1781 CB ALA A1075 15209 23402 12608 1134 -25 1395 C ATOM 1782 N LEU A1076 -47.407 1.275 -51.316 1.00132.67 N ANISOU 1782 N LEU A1076 15320 22913 12177 1569 -139 1464 N ATOM 1783 CA LEU A1076 -48.394 2.347 -51.299 1.00140.99 C ANISOU 1783 CA LEU A1076 16456 23964 13148 1865 -245 1523 C ATOM 1784 C LEU A1076 -48.186 3.290 -52.478 1.00153.01 C ANISOU 1784 C LEU A1076 18371 25258 14509 1906 -285 1581 C ATOM 1785 O LEU A1076 -49.122 3.948 -52.933 1.00160.31 O ANISOU 1785 O LEU A1076 19379 26195 15336 2158 -431 1671 O ATOM 1786 CB LEU A1076 -48.324 3.123 -49.982 1.00140.16 C ANISOU 1786 CB LEU A1076 16373 23789 13092 2005 -152 1477 C ATOM 1787 N LYS A1077 -46.951 3.351 -52.967 1.00156.43 N ANISOU 1787 N LYS A1077 19038 25486 14913 1661 -149 1541 N ATOM 1788 CA LYS A1077 -46.621 4.172 -54.125 1.00157.53 C ANISOU 1788 CA LYS A1077 19600 25380 14873 1632 -145 1587 C ATOM 1789 C LYS A1077 -47.290 3.620 -55.379 1.00158.86 C ANISOU 1789 C LYS A1077 19824 25629 14907 1619 -301 1660 C ATOM 1790 O LYS A1077 -47.663 4.372 -56.279 1.00170.19 O ANISOU 1790 O LYS A1077 21579 26929 16155 1725 -418 1745 O ATOM 1791 CB LYS A1077 -45.106 4.245 -54.321 1.00157.94 C ANISOU 1791 CB LYS A1077 19826 25237 14949 1330 81 1526 C ATOM 1792 N LEU A1078 -47.437 2.300 -55.428 1.00150.52 N ANISOU 1792 N LEU A1078 18499 24772 13920 1471 -315 1633 N ATOM 1793 CA LEU A1078 -48.115 1.646 -56.540 1.00148.25 C ANISOU 1793 CA LEU A1078 18275 24575 13479 1394 -485 1695 C ATOM 1794 C LEU A1078 -49.626 1.785 -56.396 1.00155.81 C ANISOU 1794 C LEU A1078 18992 25787 14421 1641 -780 1799 C ATOM 1795 O LEU A1078 -50.359 1.760 -57.385 1.00161.88 O ANISOU 1795 O LEU A1078 19873 26615 15021 1648 -1014 1900 O ATOM 1796 CB LEU A1078 -47.725 0.167 -56.624 1.00138.59 C ANISOU 1796 CB LEU A1078 16910 23437 12310 1129 -374 1623 C ATOM 1797 CG LEU A1078 -46.423 -0.201 -57.343 1.00130.47 C ANISOU 1797 CG LEU A1078 16160 22173 11238 884 -102 1560 C ATOM 1798 CD1 LEU A1078 -45.197 0.290 -56.585 1.00124.24 C ANISOU 1798 CD1 LEU A1078 15318 21259 10629 867 146 1500 C ATOM 1799 CD2 LEU A1078 -46.347 -1.704 -57.570 1.00129.52 C ANISOU 1799 CD2 LEU A1078 15964 22124 11122 686 -25 1511 C ATOM 1800 N ALA A1079 -50.084 1.932 -55.157 1.00156.16 N ANISOU 1800 N ALA A1079 18701 25992 14640 1836 -765 1782 N ATOM 1801 CA ALA A1079 -51.505 2.104 -54.878 1.00159.96 C ANISOU 1801 CA ALA A1079 18875 26747 15157 2107 -984 1884 C ATOM 1802 C ALA A1079 -51.983 3.476 -55.337 1.00169.16 C ANISOU 1802 C ALA A1079 20280 27779 16213 2444 -1115 2004 C ATOM 1803 O ALA A1079 -53.044 3.602 -55.948 1.00174.93 O ANISOU 1803 O ALA A1079 20906 28684 16876 2611 -1387 2147 O ATOM 1804 CB ALA A1079 -51.782 1.912 -53.395 1.00156.98 C ANISOU 1804 CB ALA A1079 18127 26539 14980 2221 -860 1822 C ATOM 1805 N ASN A1080 -51.193 4.502 -55.037 1.00173.93 N ANISOU 1805 N ASN A1080 21220 28072 16794 2535 -935 1956 N ATOM 1806 CA ASN A1080 -51.514 5.863 -55.447 1.00173.31 C ANISOU 1806 CA ASN A1080 21483 27781 16584 2856 -1019 2062 C ATOM 1807 C ASN A1080 -51.370 6.042 -56.954 1.00173.39 C ANISOU 1807 C ASN A1080 21894 27631 16357 2738 -1179 2152 C ATOM 1808 O ASN A1080 -52.063 6.858 -57.563 1.00177.39 O ANISOU 1808 O ASN A1080 22596 28073 16732 3024 -1385 2302 O ATOM 1809 CB ASN A1080 -50.624 6.867 -54.713 1.00172.82 C ANISOU 1809 CB ASN A1080 21750 27393 16523 2898 -768 1971 C ATOM 1810 N GLU A1081 -50.464 5.273 -57.550 1.00169.87 N ANISOU 1810 N GLU A1081 21592 27105 15845 2333 -1072 2069 N ATOM 1811 CA GLU A1081 -50.250 5.317 -58.991 1.00167.64 C ANISOU 1811 CA GLU A1081 21740 26651 15304 2160 -1176 2134 C ATOM 1812 C GLU A1081 -51.401 4.643 -59.729 1.00165.20 C ANISOU 1812 C GLU A1081 21248 26621 14900 2167 -1530 2261 C ATOM 1813 O GLU A1081 -51.684 4.964 -60.884 1.00172.48 O ANISOU 1813 O GLU A1081 22524 27438 15572 2158 -1747 2380 O ATOM 1814 CB GLU A1081 -48.923 4.649 -59.358 1.00166.08 C ANISOU 1814 CB GLU A1081 21736 26288 15080 1741 -891 2000 C ATOM 1815 N GLY A1082 -52.062 3.707 -59.054 1.00157.59 N ANISOU 1815 N GLY A1082 19749 26012 14116 2150 -1602 2242 N ATOM 1816 CA GLY A1082 -53.196 3.008 -59.630 1.00157.13 C ANISOU 1816 CA GLY A1082 19446 26271 13984 2099 -1952 2363 C ATOM 1817 C GLY A1082 -52.938 1.528 -59.840 1.00154.11 C ANISOU 1817 C GLY A1082 18976 26003 13576 1662 -1899 2262 C ATOM 1818 O GLY A1082 -53.851 0.773 -60.174 1.00159.48 O ANISOU 1818 O GLY A1082 19427 26968 14200 1529 -2173 2339 O ATOM 1819 N LYS A1083 -51.691 1.114 -59.644 1.00146.79 N ANISOU 1819 N LYS A1083 18236 24850 12688 1436 -1545 2099 N ATOM 1820 CA LYS A1083 -51.310 -0.282 -59.832 1.00140.12 C ANISOU 1820 CA LYS A1083 17385 24039 11816 1065 -1429 1997 C ATOM 1821 C LYS A1083 -51.750 -1.141 -58.651 1.00130.54 C ANISOU 1821 C LYS A1083 15644 23118 10837 1055 -1396 1942 C ATOM 1822 O LYS A1083 -51.041 -1.248 -57.651 1.00146.42 O ANISOU 1822 O LYS A1083 17508 25075 13049 1092 -1127 1835 O ATOM 1823 CB LYS A1083 -49.798 -0.401 -60.033 1.00138.61 C ANISOU 1823 CB LYS A1083 17538 23512 11614 884 -1038 1864 C ATOM 1824 N VAL A1084 -52.923 -1.754 -58.775 1.00131.08 N ANISOU 1824 N VAL A1084 15437 23501 10864 977 -1685 2026 N ATOM 1825 CA VAL A1084 -53.461 -2.598 -57.714 1.00127.73 C ANISOU 1825 CA VAL A1084 14533 23369 10630 925 -1661 1986 C ATOM 1826 C VAL A1084 -52.898 -4.014 -57.792 1.00119.33 C ANISOU 1826 C VAL A1084 13602 22228 9511 542 -1492 1866 C ATOM 1827 O VAL A1084 -52.375 -4.536 -56.808 1.00118.87 O ANISOU 1827 O VAL A1084 13388 22151 9628 525 -1246 1762 O ATOM 1828 CB VAL A1084 -54.999 -2.665 -57.771 1.00135.08 C ANISOU 1828 CB VAL A1084 15056 24711 11558 976 -2031 2138 C ATOM 1829 N LYS A1085 -53.009 -4.627 -58.966 1.00113.80 N ANISOU 1829 N LYS A1085 13234 21459 8544 240 -1627 1887 N ATOM 1830 CA LYS A1085 -52.530 -5.990 -59.175 1.00109.00 C ANISOU 1830 CA LYS A1085 12852 20728 7835 -118 -1456 1778 C ATOM 1831 C LYS A1085 -51.020 -6.088 -58.980 1.00104.90 C ANISOU 1831 C LYS A1085 12586 19862 7408 -79 -1024 1647 C ATOM 1832 O LYS A1085 -50.509 -7.108 -58.519 1.00101.26 O ANISOU 1832 O LYS A1085 12127 19328 7019 -210 -797 1552 O ATOM 1833 CB LYS A1085 -52.911 -6.482 -60.573 1.00109.70 C ANISOU 1833 CB LYS A1085 13363 20756 7564 -452 -1678 1826 C ATOM 1834 N GLU A1086 -50.312 -5.020 -59.335 1.00106.39 N ANISOU 1834 N GLU A1086 12981 19842 7598 102 -916 1656 N ATOM 1835 CA GLU A1086 -48.865 -4.973 -59.172 1.00106.31 C ANISOU 1835 CA GLU A1086 13142 19548 7702 136 -519 1555 C ATOM 1836 C GLU A1086 -48.487 -4.812 -57.703 1.00105.82 C ANISOU 1836 C GLU A1086 12667 19580 7959 332 -379 1512 C ATOM 1837 O GLU A1086 -47.394 -5.198 -57.287 1.00103.21 O ANISOU 1837 O GLU A1086 12338 19106 7772 318 -86 1437 O ATOM 1838 CB GLU A1086 -48.268 -3.833 -60.000 1.00 95.57 C ANISOU 1838 CB GLU A1086 12136 17951 6227 215 -452 1585 C ATOM 1839 N ALA A1087 -49.398 -4.240 -56.923 1.00109.33 N ANISOU 1839 N ALA A1087 12763 20268 8507 522 -590 1571 N ATOM 1840 CA ALA A1087 -49.169 -4.035 -55.497 1.00110.09 C ANISOU 1840 CA ALA A1087 12522 20450 8857 692 -480 1532 C ATOM 1841 C ALA A1087 -49.449 -5.309 -54.708 1.00111.37 C ANISOU 1841 C ALA A1087 12443 20768 9104 557 -446 1488 C ATOM 1842 O ALA A1087 -48.776 -5.597 -53.717 1.00111.05 O ANISOU 1842 O ALA A1087 12270 20690 9234 593 -270 1431 O ATOM 1843 CB ALA A1087 -50.028 -2.892 -54.981 1.00 90.65 C ANISOU 1843 CB ALA A1087 9847 18145 6449 971 -658 1606 C ATOM 1844 N GLN A1088 -50.447 -6.067 -55.152 1.00115.23 N ANISOU 1844 N GLN A1088 12898 21430 9456 377 -636 1524 N ATOM 1845 CA GLN A1088 -50.809 -7.323 -54.506 1.00119.74 C ANISOU 1845 CA GLN A1088 13304 22133 10058 192 -611 1486 C ATOM 1846 C GLN A1088 -49.680 -8.340 -54.623 1.00123.90 C ANISOU 1846 C GLN A1088 14107 22392 10579 43 -341 1401 C ATOM 1847 O GLN A1088 -49.384 -9.066 -53.674 1.00124.48 O ANISOU 1847 O GLN A1088 14055 22466 10775 29 -209 1358 O ATOM 1848 CB GLN A1088 -52.094 -7.890 -55.113 1.00123.46 C ANISOU 1848 CB GLN A1088 13721 22839 10348 -41 -889 1552 C ATOM 1849 CG GLN A1088 -53.312 -6.997 -54.938 1.00125.95 C ANISOU 1849 CG GLN A1088 13665 23478 10710 141 -1161 1665 C ATOM 1850 CD GLN A1088 -54.547 -7.555 -55.619 1.00129.94 C ANISOU 1850 CD GLN A1088 14069 24258 11045 -126 -1477 1756 C ATOM 1851 OE1 GLN A1088 -54.521 -8.654 -56.173 1.00130.87 O ANISOU 1851 OE1 GLN A1088 14442 24305 10978 -493 -1493 1718 O ATOM 1852 NE2 GLN A1088 -55.637 -6.798 -55.581 1.00132.99 N ANISOU 1852 NE2 GLN A1088 14086 24957 11486 56 -1733 1885 N ATOM 1853 N ALA A1089 -49.054 -8.386 -55.795 1.00122.55 N ANISOU 1853 N ALA A1089 14329 21980 10256 -49 -245 1384 N ATOM 1854 CA ALA A1089 -47.920 -9.273 -56.025 1.00119.76 C ANISOU 1854 CA ALA A1089 14251 21347 9907 -130 66 1312 C ATOM 1855 C ALA A1089 -46.695 -8.773 -55.269 1.00114.31 C ANISOU 1855 C ALA A1089 13404 20550 9478 97 299 1291 C ATOM 1856 O ALA A1089 -45.814 -9.553 -54.907 1.00113.31 O ANISOU 1856 O ALA A1089 13302 20285 9465 112 534 1256 O ATOM 1857 CB ALA A1089 -47.623 -9.383 -57.511 1.00120.66 C ANISOU 1857 CB ALA A1089 14850 21228 9767 -286 143 1299 C ATOM 1858 N ALA A1090 -46.646 -7.465 -55.038 1.00112.16 N ANISOU 1858 N ALA A1090 12985 20340 9293 270 219 1324 N ATOM 1859 CA ALA A1090 -45.558 -6.860 -54.281 1.00109.43 C ANISOU 1859 CA ALA A1090 12486 19922 9172 428 383 1314 C ATOM 1860 C ALA A1090 -45.728 -7.136 -52.793 1.00106.78 C ANISOU 1860 C ALA A1090 11816 19745 9011 508 331 1312 C ATOM 1861 O ALA A1090 -44.752 -7.181 -52.044 1.00107.13 O ANISOU 1861 O ALA A1090 11740 19731 9236 574 464 1306 O ATOM 1862 CB ALA A1090 -45.495 -5.363 -54.543 1.00111.25 C ANISOU 1862 CB ALA A1090 12761 20125 9385 542 315 1345 C ATOM 1863 N ALA A1091 -46.974 -7.320 -52.370 1.00109.83 N ANISOU 1863 N ALA A1091 12050 20345 9337 486 132 1327 N ATOM 1864 CA ALA A1091 -47.273 -7.633 -50.979 1.00114.22 C ANISOU 1864 CA ALA A1091 12338 21048 10013 532 101 1321 C ATOM 1865 C ALA A1091 -46.851 -9.060 -50.647 1.00121.42 C ANISOU 1865 C ALA A1091 13302 21881 10951 411 226 1297 C ATOM 1866 O ALA A1091 -46.574 -9.383 -49.492 1.00 82.31 O ANISOU 1866 O ALA A1091 8203 16955 6115 457 260 1297 O ATOM 1867 CB ALA A1091 -48.754 -7.437 -50.695 1.00 84.22 C ANISOU 1867 CB ALA A1091 8341 17513 6144 537 -101 1349 C ATOM 1868 N GLU A1092 -46.801 -9.908 -51.669 1.00128.77 N ANISOU 1868 N GLU A1092 14496 22685 11745 258 298 1282 N ATOM 1869 CA GLU A1092 -46.387 -11.295 -51.496 1.00135.41 C ANISOU 1869 CA GLU A1092 15483 23388 12580 163 449 1261 C ATOM 1870 C GLU A1092 -44.869 -11.404 -51.390 1.00146.75 C ANISOU 1870 C GLU A1092 16953 24611 14194 319 689 1268 C ATOM 1871 O GLU A1092 -44.335 -12.460 -51.052 1.00148.39 O ANISOU 1871 O GLU A1092 17240 24688 14454 335 832 1273 O ATOM 1872 CB GLU A1092 -46.899 -12.156 -52.652 1.00131.81 C ANISOU 1872 CB GLU A1092 15370 22835 11875 -74 456 1236 C ATOM 1873 CG GLU A1092 -48.413 -12.180 -52.784 1.00129.90 C ANISOU 1873 CG GLU A1092 15045 22847 11463 -277 184 1252 C ATOM 1874 N GLN A1093 -44.179 -10.307 -51.683 1.00157.75 N ANISOU 1874 N GLN A1093 18282 25974 15683 433 734 1280 N ATOM 1875 CA GLN A1093 -42.727 -10.260 -51.565 1.00161.11 C ANISOU 1875 CA GLN A1093 18644 26261 16311 563 948 1305 C ATOM 1876 C GLN A1093 -42.318 -10.068 -50.109 1.00163.28 C ANISOU 1876 C GLN A1093 18608 26645 16785 670 857 1349 C ATOM 1877 O GLN A1093 -41.166 -10.300 -49.741 1.00167.53 O ANISOU 1877 O GLN A1093 19024 27115 17515 771 981 1398 O ATOM 1878 CB GLN A1093 -42.150 -9.139 -52.431 1.00160.86 C ANISOU 1878 CB GLN A1093 18674 26161 16285 580 1035 1305 C ATOM 1879 N LEU A1094 -43.270 -9.642 -49.285 1.00154.98 N ANISOU 1879 N LEU A1094 17431 25770 15683 649 643 1340 N ATOM 1880 CA LEU A1094 -43.028 -9.466 -47.858 1.00146.98 C ANISOU 1880 CA LEU A1094 16203 24847 14794 713 543 1372 C ATOM 1881 C LEU A1094 -43.199 -10.786 -47.115 1.00145.95 C ANISOU 1881 C LEU A1094 16092 24705 14658 689 546 1391 C ATOM 1882 O LEU A1094 -42.921 -10.874 -45.919 1.00147.35 O ANISOU 1882 O LEU A1094 16147 24924 14915 731 468 1430 O ATOM 1883 CB LEU A1094 -43.967 -8.407 -47.269 1.00138.88 C ANISOU 1883 CB LEU A1094 15087 23982 13699 721 371 1348 C ATOM 1884 CG LEU A1094 -43.648 -6.930 -47.521 1.00131.59 C ANISOU 1884 CG LEU A1094 14162 23042 12796 777 345 1344 C ATOM 1885 CD1 LEU A1094 -43.992 -6.513 -48.944 1.00131.94 C ANISOU 1885 CD1 LEU A1094 14375 23033 12724 758 379 1328 C ATOM 1886 CD2 LEU A1094 -44.370 -6.047 -46.513 1.00126.28 C ANISOU 1886 CD2 LEU A1094 13418 22483 12081 834 215 1329 C ATOM 1887 N LYS A1095 -43.660 -11.807 -47.830 1.00144.25 N ANISOU 1887 N LYS A1095 16084 24408 14315 596 628 1366 N ATOM 1888 CA LYS A1095 -43.850 -13.130 -47.246 1.00143.57 C ANISOU 1888 CA LYS A1095 16106 24260 14182 546 654 1381 C ATOM 1889 C LYS A1095 -42.514 -13.740 -46.838 1.00147.58 C ANISOU 1889 C LYS A1095 16597 24604 14872 717 776 1456 C ATOM 1890 O LYS A1095 -42.403 -14.364 -45.784 1.00158.18 O ANISOU 1890 O LYS A1095 17918 25936 16247 752 717 1508 O ATOM 1891 CB LYS A1095 -44.573 -14.054 -48.229 1.00142.32 C ANISOU 1891 CB LYS A1095 16247 24013 13815 366 725 1333 C ATOM 1892 N THR A1096 -41.501 -13.552 -47.678 1.00144.09 N ANISOU 1892 N THR A1096 16157 24041 14549 831 950 1476 N ATOM 1893 CA THR A1096 -40.160 -14.035 -47.374 1.00141.43 C ANISOU 1893 CA THR A1096 15714 23588 14434 1037 1079 1572 C ATOM 1894 C THR A1096 -39.397 -13.010 -46.542 1.00136.10 C ANISOU 1894 C THR A1096 14683 23067 13960 1107 930 1642 C ATOM 1895 O THR A1096 -38.288 -13.272 -46.077 1.00137.48 O ANISOU 1895 O THR A1096 14669 23219 14347 1264 955 1752 O ATOM 1896 CB THR A1096 -39.364 -14.346 -48.656 1.00142.24 C ANISOU 1896 CB THR A1096 15958 23498 14591 1133 1393 1568 C ATOM 1897 OG1 THR A1096 -39.293 -13.171 -49.474 1.00140.74 O ANISOU 1897 OG1 THR A1096 15709 23374 14392 1059 1422 1521 O ATOM 1898 CG2 THR A1096 -40.033 -15.464 -49.440 1.00142.87 C ANISOU 1898 CG2 THR A1096 16476 23374 14433 1037 1545 1500 C ATOM 1899 N THR A1097 -40.003 -11.841 -46.358 1.00129.98 N ANISOU 1899 N THR A1097 13832 22445 13111 989 768 1587 N ATOM 1900 CA THR A1097 -39.400 -10.777 -45.565 1.00127.29 C ANISOU 1900 CA THR A1097 13244 22225 12896 992 615 1634 C ATOM 1901 C THR A1097 -39.857 -10.854 -44.113 1.00128.73 C ANISOU 1901 C THR A1097 13391 22500 13020 955 390 1657 C ATOM 1902 O THR A1097 -39.043 -10.796 -43.191 1.00127.48 O ANISOU 1902 O THR A1097 13076 22376 12985 992 266 1750 O ATOM 1903 CB THR A1097 -39.745 -9.385 -46.129 1.00126.75 C ANISOU 1903 CB THR A1097 13191 22216 12754 901 588 1563 C ATOM 1904 OG1 THR A1097 -39.280 -9.285 -47.481 1.00129.37 O ANISOU 1904 OG1 THR A1097 13600 22445 13111 911 804 1546 O ATOM 1905 CG2 THR A1097 -39.096 -8.292 -45.292 1.00128.11 C ANISOU 1905 CG2 THR A1097 13183 22472 13019 860 438 1605 C ATOM 1906 N ARG A1098 -41.165 -10.988 -43.917 1.00131.19 N ANISOU 1906 N ARG A1098 13848 22862 13136 866 339 1579 N ATOM 1907 CA ARG A1098 -41.740 -11.055 -42.578 1.00131.64 C ANISOU 1907 CA ARG A1098 13916 22999 13101 812 182 1584 C ATOM 1908 C ARG A1098 -41.356 -12.349 -41.869 1.00132.04 C ANISOU 1908 C ARG A1098 14032 22960 13177 857 165 1669 C ATOM 1909 O ARG A1098 -40.904 -12.325 -40.725 1.00134.09 O ANISOU 1909 O ARG A1098 14244 23240 13466 868 13 1743 O ATOM 1910 CB ARG A1098 -43.263 -10.927 -42.643 1.00130.44 C ANISOU 1910 CB ARG A1098 13854 22949 12757 711 180 1489 C ATOM 1911 N ASN A1099 -41.536 -13.473 -42.557 1.00131.93 N ANISOU 1911 N ASN A1099 14178 22824 13124 874 313 1663 N ATOM 1912 CA ASN A1099 -41.252 -14.785 -41.983 1.00135.82 C ANISOU 1912 CA ASN A1099 14816 23179 13610 934 326 1745 C ATOM 1913 C ASN A1099 -39.801 -14.941 -41.543 1.00145.46 C ANISOU 1913 C ASN A1099 15872 24340 15057 1138 272 1894 C ATOM 1914 O ASN A1099 -39.524 -15.514 -40.492 1.00154.57 O ANISOU 1914 O ASN A1099 17068 25454 16207 1187 139 1994 O ATOM 1915 CB ASN A1099 -41.605 -15.888 -42.982 1.00134.25 C ANISOU 1915 CB ASN A1099 14884 22810 13315 911 530 1705 C ATOM 1916 CG ASN A1099 -43.090 -15.956 -43.276 1.00132.97 C ANISOU 1916 CG ASN A1099 14869 22736 12916 662 529 1590 C ATOM 1917 OD1 ASN A1099 -43.823 -14.991 -43.058 1.00132.57 O ANISOU 1917 OD1 ASN A1099 14665 22887 12818 567 424 1533 O ATOM 1918 ND2 ASN A1099 -43.543 -17.100 -43.775 1.00133.79 N ANISOU 1918 ND2 ASN A1099 15274 22688 12871 555 649 1563 N ATOM 1919 N ALA A1100 -38.877 -14.425 -42.347 1.00139.34 N ANISOU 1919 N ALA A1100 14897 23569 14476 1248 370 1921 N ATOM 1920 CA ALA A1100 -37.454 -14.537 -42.045 1.00137.22 C ANISOU 1920 CA ALA A1100 14377 23294 14467 1444 331 2081 C ATOM 1921 C ALA A1100 -37.029 -13.556 -40.956 1.00135.24 C ANISOU 1921 C ALA A1100 13894 23220 14272 1355 38 2147 C ATOM 1922 O ALA A1100 -35.890 -13.588 -40.490 1.00135.81 O ANISOU 1922 O ALA A1100 13714 23341 14548 1467 -84 2304 O ATOM 1923 CB ALA A1100 -36.630 -14.316 -43.303 1.00137.37 C ANISOU 1923 CB ALA A1100 14247 23273 14673 1560 582 2086 C ATOM 1924 N TYR A1101 -37.950 -12.688 -40.551 1.00132.92 N ANISOU 1924 N TYR A1101 13693 23021 13788 1153 -75 2034 N ATOM 1925 CA TYR A1101 -37.642 -11.647 -39.579 1.00129.13 C ANISOU 1925 CA TYR A1101 13097 22668 13300 1029 -324 2065 C ATOM 1926 C TYR A1101 -38.202 -11.948 -38.193 1.00125.35 C ANISOU 1926 C TYR A1101 12809 22189 12629 943 -523 2084 C ATOM 1927 O TYR A1101 -37.486 -11.855 -37.195 1.00124.85 O ANISOU 1927 O TYR A1101 12677 22162 12598 917 -765 2205 O ATOM 1928 CB TYR A1101 -38.168 -10.299 -40.072 1.00125.13 C ANISOU 1928 CB TYR A1101 12607 22229 12709 890 -281 1930 C ATOM 1929 CG TYR A1101 -37.076 -9.373 -40.544 1.00120.42 C ANISOU 1929 CG TYR A1101 11774 21687 12292 858 -288 1977 C ATOM 1930 CD1 TYR A1101 -36.323 -9.672 -41.672 1.00118.95 C ANISOU 1930 CD1 TYR A1101 11424 21467 12304 972 -79 2017 C ATOM 1931 CD2 TYR A1101 -36.792 -8.202 -39.859 1.00117.18 C ANISOU 1931 CD2 TYR A1101 11337 21349 11836 686 -480 1979 C ATOM 1932 CE1 TYR A1101 -35.319 -8.829 -42.104 1.00118.14 C ANISOU 1932 CE1 TYR A1101 11089 21430 12368 907 -56 2064 C ATOM 1933 CE2 TYR A1101 -35.794 -7.355 -40.284 1.00116.74 C ANISOU 1933 CE2 TYR A1101 11079 21346 11929 596 -487 2025 C ATOM 1934 CZ TYR A1101 -35.059 -7.670 -41.405 1.00116.83 C ANISOU 1934 CZ TYR A1101 10880 21352 12156 702 -272 2070 C ATOM 1935 OH TYR A1101 -34.061 -6.822 -41.826 1.00117.32 O ANISOU 1935 OH TYR A1101 10725 21484 12368 578 -251 2118 O ATOM 1936 N ILE A1102 -39.480 -12.305 -38.131 1.00121.90 N ANISOU 1936 N ILE A1102 12613 21720 11982 874 -424 1971 N ATOM 1937 CA ILE A1102 -40.123 -12.580 -36.853 1.00119.95 C ANISOU 1937 CA ILE A1102 12581 21470 11527 767 -550 1971 C ATOM 1938 C ILE A1102 -39.704 -13.939 -36.298 1.00120.36 C ANISOU 1938 C ILE A1102 12751 21397 11584 861 -616 2108 C ATOM 1939 O ILE A1102 -39.633 -14.120 -35.084 1.00121.86 O ANISOU 1939 O ILE A1102 13083 21568 11652 798 -806 2182 O ATOM 1940 CB ILE A1102 -41.656 -12.520 -36.997 1.00 30.00 C ATOM 1941 CG1 ILE A1102 -42.104 -11.095 -37.329 1.00 30.00 C ATOM 1942 CG2 ILE A1102 -42.330 -13.013 -35.727 1.00 30.00 C ATOM 1943 CD1 ILE A1102 -43.555 -10.994 -37.745 1.00 30.00 C ATOM 1944 N GLN A1103 -39.424 -14.889 -37.186 1.00121.03 N ANISOU 1944 N GLN A1103 12833 21368 11785 1017 -451 2144 N ATOM 1945 CA GLN A1103 -38.946 -16.202 -36.764 1.00124.49 C ANISOU 1945 CA GLN A1103 13419 21642 12241 1165 -486 2289 C ATOM 1946 C GLN A1103 -37.534 -16.087 -36.203 1.00126.58 C ANISOU 1946 C GLN A1103 13436 21940 12717 1329 -724 2491 C ATOM 1947 O GLN A1103 -37.138 -16.855 -35.327 1.00129.84 O ANISOU 1947 O GLN A1103 13968 22262 13101 1420 -896 2645 O ATOM 1948 CB GLN A1103 -38.978 -17.197 -37.924 1.00126.22 C ANISOU 1948 CB GLN A1103 13750 21690 12515 1304 -210 2268 C ATOM 1949 N LYS A1104 -36.780 -15.122 -36.719 1.00125.74 N ANISOU 1949 N LYS A1104 12983 21972 12819 1350 -746 2502 N ATOM 1950 CA LYS A1104 -35.460 -14.815 -36.187 1.00127.32 C ANISOU 1950 CA LYS A1104 12867 22276 13230 1433 -1005 2696 C ATOM 1951 C LYS A1104 -35.602 -14.137 -34.830 1.00125.82 C ANISOU 1951 C LYS A1104 12783 22176 12847 1197 -1343 2719 C ATOM 1952 O LYS A1104 -34.717 -14.230 -33.979 1.00132.39 O ANISOU 1952 O LYS A1104 13495 23061 13747 1224 -1654 2911 O ATOM 1953 CB LYS A1104 -34.678 -13.923 -37.153 1.00128.68 C ANISOU 1953 CB LYS A1104 12657 22580 13655 1450 -903 2688 C ATOM 1954 N TYR A1105 -36.727 -13.456 -34.638 1.00119.10 N ANISOU 1954 N TYR A1105 12168 21340 11745 972 -1277 2529 N ATOM 1955 CA TYR A1105 -37.029 -12.808 -33.368 1.00117.17 C ANISOU 1955 CA TYR A1105 12127 21133 11258 742 -1518 2513 C ATOM 1956 C TYR A1105 -37.858 -13.729 -32.480 1.00115.42 C ANISOU 1956 C TYR A1105 12295 20785 10773 702 -1524 2510 C ATOM 1957 O TYR A1105 -38.088 -13.434 -31.307 1.00117.96 O ANISOU 1957 O TYR A1105 12862 21098 10859 525 -1709 2518 O ATOM 1958 CB TYR A1105 -37.767 -11.488 -33.598 1.00114.81 C ANISOU 1958 CB TYR A1105 11885 20903 10834 556 -1405 2317 C ATOM 1959 N LEU A1106 -38.307 -14.844 -33.048 1.00111.54 N ANISOU 1959 N LEU A1106 11906 20177 10295 838 -1304 2494 N ATOM 1960 CA LEU A1106 -39.066 -15.836 -32.296 1.00108.65 C ANISOU 1960 CA LEU A1106 11930 19673 9680 778 -1279 2499 C ATOM 1961 C LEU A1106 -38.108 -16.715 -31.502 1.00112.55 C ANISOU 1961 C LEU A1106 12505 20053 10205 923 -1547 2740 C ATOM 1962 O LEU A1106 -38.355 -17.026 -30.337 1.00111.94 O ANISOU 1962 O LEU A1106 12752 19900 9880 802 -1714 2797 O ATOM 1963 CB LEU A1106 -39.929 -16.687 -33.233 1.00104.36 C ANISOU 1963 CB LEU A1106 11509 19034 9108 811 -952 2390 C ATOM 1964 CG LEU A1106 -41.293 -17.164 -32.724 1.00103.10 C ANISOU 1964 CG LEU A1106 11703 18827 8643 592 -809 2276 C ATOM 1965 CD1 LEU A1106 -42.113 -17.733 -33.871 1.00103.48 C ANISOU 1965 CD1 LEU A1106 11784 18844 8689 562 -515 2156 C ATOM 1966 CD2 LEU A1106 -41.151 -18.194 -31.611 1.00104.31 C ANISOU 1966 CD2 LEU A1106 12217 18801 8614 576 -948 2415 C ATOM 1967 N GLN A 314 -37.011 -17.113 -32.140 1.00135.84 N ANISOU 1967 N GLN A 314 17134 24839 9638 1050 -3227 2675 N ATOM 1968 CA GLN A 314 -35.979 -17.885 -31.463 1.00132.20 C ANISOU 1968 CA GLN A 314 16968 24009 9252 883 -2989 2391 C ATOM 1969 C GLN A 314 -35.228 -16.998 -30.478 1.00126.27 C ANISOU 1969 C GLN A 314 16208 22833 8935 1092 -2650 2732 C ATOM 1970 O GLN A 314 -34.619 -17.487 -29.527 1.00116.96 O ANISOU 1970 O GLN A 314 15155 21336 7949 965 -2479 2557 O ATOM 1971 CB GLN A 314 -35.006 -18.506 -32.467 1.00136.92 C ANISOU 1971 CB GLN A 314 17976 24610 9438 857 -2878 2158 C ATOM 1972 CG GLN A 314 -34.201 -17.496 -33.267 1.00141.41 C ANISOU 1972 CG GLN A 314 18676 25147 9906 1172 -2639 2561 C ATOM 1973 CD GLN A 314 -33.052 -18.137 -34.021 1.00147.64 C ANISOU 1973 CD GLN A 314 19861 25885 10351 1137 -2447 2315 C ATOM 1974 OE1 GLN A 314 -32.642 -19.257 -33.715 1.00149.46 O ANISOU 1974 OE1 GLN A 314 20298 25977 10512 928 -2419 1866 O ATOM 1975 NE2 GLN A 314 -32.527 -17.428 -35.013 1.00150.73 N ANISOU 1975 NE2 GLN A 314 20357 26387 10526 1344 -2306 2605 N ATOM 1976 N THR A 315 -35.276 -15.691 -30.717 1.00131.55 N ANISOU 1976 N THR A 315 16740 23480 9763 1408 -2557 3211 N ATOM 1977 CA THR A 315 -34.680 -14.722 -29.807 1.00105.64 C ANISOU 1977 CA THR A 315 13421 19778 6941 1610 -2253 3544 C ATOM 1978 C THR A 315 -35.366 -14.800 -28.450 1.00102.31 C ANISOU 1978 C THR A 315 12723 19254 6898 1514 -2320 3492 C ATOM 1979 O THR A 315 -34.709 -14.806 -27.412 1.00104.45 O ANISOU 1979 O THR A 315 13069 19153 7464 1491 -2089 3480 O ATOM 1980 CB THR A 315 -34.782 -13.286 -30.355 1.00108.40 C ANISOU 1980 CB THR A 315 13660 20118 7410 1945 -2182 4050 C ATOM 1981 OG1 THR A 315 -34.114 -13.205 -31.620 1.00117.91 O ANISOU 1981 OG1 THR A 315 15121 21439 8239 2011 -2105 4120 O ATOM 1982 CG2 THR A 315 -34.149 -12.298 -29.387 1.00104.31 C ANISOU 1982 CG2 THR A 315 13118 19110 7406 2124 -1863 4345 C ATOM 1983 N ILE A 316 -36.694 -14.870 -28.471 1.00105.19 N ANISOU 1983 N ILE A 316 12753 19973 7243 1450 -2638 3456 N ATOM 1984 CA ILE A 316 -37.475 -15.019 -27.249 1.00104.62 C ANISOU 1984 CA ILE A 316 12366 19894 7490 1321 -2728 3380 C ATOM 1985 C ILE A 316 -37.343 -16.438 -26.705 1.00100.65 C ANISOU 1985 C ILE A 316 12003 19367 6871 899 -2789 2899 C ATOM 1986 O ILE A 316 -37.263 -16.643 -25.494 1.00 96.74 O ANISOU 1986 O ILE A 316 11482 18452 6822 747 -2615 2746 O ATOM 1987 CB ILE A 316 -38.964 -14.695 -27.486 1.00107.31 C ANISOU 1987 CB ILE A 316 12265 20660 7849 1365 -3049 3462 C ATOM 1988 CG1 ILE A 316 -39.116 -13.301 -28.096 1.00110.26 C ANISOU 1988 CG1 ILE A 316 12535 21033 8325 1789 -3002 3932 C ATOM 1989 CG2 ILE A 316 -39.753 -14.800 -26.188 1.00105.15 C ANISOU 1989 CG2 ILE A 316 11627 20398 7929 1232 -3109 3389 C ATOM 1990 CD1 ILE A 316 -40.552 -12.877 -28.297 1.00115.34 C ANISOU 1990 CD1 ILE A 316 12733 22070 9020 1896 -3298 4042 C ATOM 1991 N SER A 317 -37.316 -17.411 -27.612 1.00106.21 N ANISOU 1991 N SER A 317 12910 20285 7159 681 -2953 2560 N ATOM 1992 CA SER A 317 -37.177 -18.815 -27.240 1.00102.27 C ANISOU 1992 CA SER A 317 12609 19666 6584 260 -3001 2046 C ATOM 1993 C SER A 317 -35.879 -19.062 -26.478 1.00 97.10 C ANISOU 1993 C SER A 317 12305 18372 6218 251 -2618 1937 C ATOM 1994 O SER A 317 -35.871 -19.746 -25.456 1.00 94.25 O ANISOU 1994 O SER A 317 11991 17639 6180 -15 -2535 1667 O ATOM 1995 CB SER A 317 -37.234 -19.705 -28.483 1.00106.79 C ANISOU 1995 CB SER A 317 13388 20538 6650 95 -3215 1712 C ATOM 1996 OG SER A 317 -37.054 -21.069 -28.144 1.00105.97 O ANISOU 1996 OG SER A 317 13511 20283 6468 -309 -3263 1205 O ATOM 1997 N ASN A 318 -34.785 -18.501 -26.983 1.00 96.27 N ANISOU 1997 N ASN A 318 12433 18160 5985 539 -2388 2163 N ATOM 1998 CA ASN A 318 -33.497 -18.603 -26.309 1.00 98.02 C ANISOU 1998 CA ASN A 318 12940 17820 6483 575 -2026 2099 C ATOM 1999 C ASN A 318 -33.473 -17.763 -25.039 1.00 93.68 C ANISOU 1999 C ASN A 318 12203 16878 6513 684 -1820 2339 C ATOM 2000 O ASN A 318 -32.828 -18.123 -24.055 1.00 83.78 O ANISOU 2000 O ASN A 318 11092 15154 5587 580 -1611 2169 O ATOM 2001 CB ASN A 318 -32.364 -18.174 -27.242 1.00 97.17 C ANISOU 2001 CB ASN A 318 13082 17762 6074 842 -1828 2290 C ATOM 2002 CG ASN A 318 -32.237 -19.072 -28.455 1.00103.95 C ANISOU 2002 CG ASN A 318 14174 18983 6340 740 -1984 1992 C ATOM 2003 OD1 ASN A 318 -32.522 -20.268 -28.390 1.00105.95 O ANISOU 2003 OD1 ASN A 318 14541 19221 6495 436 -2142 1526 O ATOM 2004 ND2 ASN A 318 -31.809 -18.499 -29.574 1.00108.54 N ANISOU 2004 ND2 ASN A 318 14846 19684 6708 953 -1893 2191 N ATOM 2005 N GLU A 319 -34.184 -16.640 -25.070 1.00 94.45 N ANISOU 2005 N GLU A 319 11984 17176 6726 911 -1890 2728 N ATOM 2006 CA GLU A 319 -34.270 -15.748 -23.921 1.00 90.13 C ANISOU 2006 CA GLU A 319 11237 16292 6716 1043 -1709 2945 C ATOM 2007 C GLU A 319 -35.072 -16.404 -22.803 1.00 86.83 C ANISOU 2007 C GLU A 319 10641 15765 6585 743 -1789 2655 C ATOM 2008 O GLU A 319 -34.792 -16.204 -21.621 1.00 83.06 O ANISOU 2008 O GLU A 319 10147 14884 6527 723 -1579 2633 O ATOM 2009 CB GLU A 319 -34.906 -14.417 -24.324 1.00 95.20 C ANISOU 2009 CB GLU A 319 11589 17185 7396 1385 -1786 3420 C ATOM 2010 CG GLU A 319 -34.478 -13.230 -23.483 1.00 95.22 C ANISOU 2010 CG GLU A 319 11522 16764 7893 1637 -1506 3720 C ATOM 2011 CD GLU A 319 -34.973 -11.915 -24.050 1.00100.73 C ANISOU 2011 CD GLU A 319 12006 17662 8604 2014 -1574 4218 C ATOM 2012 OE1 GLU A 319 -34.340 -10.872 -23.783 1.00101.24 O ANISOU 2012 OE1 GLU A 319 12122 17381 8964 2257 -1326 4521 O ATOM 2013 OE2 GLU A 319 -35.997 -11.924 -24.766 1.00104.35 O ANISOU 2013 OE2 GLU A 319 12247 18607 8795 2061 -1879 4297 O ATOM 2014 N GLN A 320 -36.070 -17.191 -23.191 1.00 91.52 N ANISOU 2014 N GLN A 320 11098 16742 6934 493 -2093 2430 N ATOM 2015 CA GLN A 320 -36.907 -17.904 -22.237 1.00 86.95 C ANISOU 2015 CA GLN A 320 10340 16115 6582 152 -2179 2155 C ATOM 2016 C GLN A 320 -36.197 -19.155 -21.731 1.00 89.74 C ANISOU 2016 C GLN A 320 11054 16079 6963 -173 -2070 1763 C ATOM 2017 O GLN A 320 -36.357 -19.547 -20.576 1.00 82.15 O ANISOU 2017 O GLN A 320 10062 14833 6317 -386 -1973 1619 O ATOM 2018 CB GLN A 320 -38.250 -18.272 -22.874 1.00 91.82 C ANISOU 2018 CB GLN A 320 10647 17303 6938 -23 -2554 2060 C ATOM 2019 CG GLN A 320 -39.255 -18.896 -21.920 1.00 98.94 C ANISOU 2019 CG GLN A 320 11284 18223 8085 -388 -2639 1824 C ATOM 2020 CD GLN A 320 -40.586 -19.184 -22.588 1.00103.55 C ANISOU 2020 CD GLN A 320 11505 19415 8425 -561 -3018 1739 C ATOM 2021 OE1 GLN A 320 -40.753 -18.960 -23.787 1.00107.01 O ANISOU 2021 OE1 GLN A 320 11911 20272 8477 -403 -3244 1843 O ATOM 2022 NE2 GLN A 320 -41.542 -19.683 -21.813 1.00103.53 N ANISOU 2022 NE2 GLN A 320 11215 19491 8632 -897 -3092 1553 N ATOM 2023 N ARG A 321 -35.408 -19.776 -22.602 1.00 91.49 N ANISOU 2023 N ARG A 321 11624 16293 6844 -191 -2081 1599 N ATOM 2024 CA ARG A 321 -34.670 -20.983 -22.246 1.00 83.57 C ANISOU 2024 CA ARG A 321 10994 14907 5852 -446 -1989 1225 C ATOM 2025 C ARG A 321 -33.505 -20.667 -21.314 1.00 78.82 C ANISOU 2025 C ARG A 321 10579 13775 5592 -290 -1650 1311 C ATOM 2026 O ARG A 321 -33.185 -21.450 -20.420 1.00 76.61 O ANISOU 2026 O ARG A 321 10475 13115 5519 -499 -1559 1084 O ATOM 2027 CB ARG A 321 -34.159 -21.691 -23.502 1.00 87.04 C ANISOU 2027 CB ARG A 321 11738 15517 5817 -465 -2090 1003 C ATOM 2028 N ALA A 322 -32.873 -19.518 -21.528 1.00 77.62 N ANISOU 2028 N ALA A 322 10390 13603 5499 69 -1472 1648 N ATOM 2029 CA ALA A 322 -31.738 -19.105 -20.712 1.00 73.55 C ANISOU 2029 CA ALA A 322 10015 12625 5304 223 -1162 1736 C ATOM 2030 C ALA A 322 -32.188 -18.652 -19.327 1.00 70.93 C ANISOU 2030 C ALA A 322 9463 12068 5419 180 -1073 1816 C ATOM 2031 O ALA A 322 -31.482 -18.854 -18.340 1.00 67.71 O ANISOU 2031 O ALA A 322 9196 11257 5274 139 -888 1723 O ATOM 2032 CB ALA A 322 -30.962 -17.995 -21.405 1.00 73.69 C ANISOU 2032 CB ALA A 322 10049 12694 5255 579 -998 2074 C ATOM 2033 N SER A 323 -33.366 -18.041 -19.261 1.00 72.66 N ANISOU 2033 N SER A 323 9326 12575 5706 204 -1208 1980 N ATOM 2034 CA SER A 323 -33.903 -17.555 -17.995 1.00 70.82 C ANISOU 2034 CA SER A 323 8848 12193 5869 184 -1118 2043 C ATOM 2035 C SER A 323 -34.373 -18.711 -17.117 1.00 86.75 C ANISOU 2035 C SER A 323 10900 14098 7963 -210 -1173 1731 C ATOM 2036 O SER A 323 -34.290 -18.642 -15.891 1.00 80.68 O ANISOU 2036 O SER A 323 10104 13055 7496 -272 -1016 1701 O ATOM 2037 CB SER A 323 -35.053 -16.577 -18.238 1.00 78.76 C ANISOU 2037 CB SER A 323 9439 13565 6922 358 -1246 2301 C ATOM 2038 OG SER A 323 -36.134 -17.213 -18.895 1.00 82.84 O ANISOU 2038 OG SER A 323 9788 14524 7164 155 -1544 2180 O ATOM 2039 N LYS A 324 -34.870 -19.770 -17.750 1.00 92.78 N ANISOU 2039 N LYS A 324 11736 15074 8444 -488 -1396 1499 N ATOM 2040 CA LYS A 324 -35.319 -20.953 -17.023 1.00 73.09 C ANISOU 2040 CA LYS A 324 9311 12451 6010 -905 -1456 1211 C ATOM 2041 C LYS A 324 -34.143 -21.689 -16.393 1.00 75.43 C ANISOU 2041 C LYS A 324 10020 12238 6404 -976 -1278 1043 C ATOM 2042 O LYS A 324 -34.247 -22.206 -15.281 1.00 68.76 O ANISOU 2042 O LYS A 324 9224 11140 5764 -1197 -1201 943 O ATOM 2043 CB LYS A 324 -36.096 -21.894 -17.946 1.00 77.25 C ANISOU 2043 CB LYS A 324 9830 13308 6213 -1198 -1750 984 C ATOM 2044 CG LYS A 324 -37.502 -21.421 -18.276 1.00 80.69 C ANISOU 2044 CG LYS A 324 9793 14269 6596 -1237 -1967 1092 C ATOM 2045 N VAL A 325 -33.026 -21.736 -17.112 1.00 69.47 N ANISOU 2045 N VAL A 325 9552 11354 5488 -777 -1211 1024 N ATOM 2046 CA VAL A 325 -31.809 -22.346 -16.591 1.00 89.93 C ANISOU 2046 CA VAL A 325 12508 13485 8177 -770 -1044 882 C ATOM 2047 C VAL A 325 -31.266 -21.519 -15.431 1.00 86.67 C ANISOU 2047 C VAL A 325 12019 12800 8113 -591 -809 1066 C ATOM 2048 O VAL A 325 -30.899 -22.059 -14.388 1.00 85.77 O ANISOU 2048 O VAL A 325 12057 12352 8178 -718 -718 960 O ATOM 2049 CB VAL A 325 -30.729 -22.484 -17.682 1.00 89.83 C ANISOU 2049 CB VAL A 325 12764 13458 7911 -561 -1004 824 C ATOM 2050 CG1 VAL A 325 -29.413 -22.950 -17.077 1.00 64.84 C ANISOU 2050 CG1 VAL A 325 9909 9833 4894 -485 -813 710 C ATOM 2051 CG2 VAL A 325 -31.193 -23.443 -18.765 1.00 71.32 C ANISOU 2051 CG2 VAL A 325 10548 11349 5200 -758 -1236 567 C ATOM 2052 N LEU A 326 -31.230 -20.203 -15.620 1.00 85.43 N ANISOU 2052 N LEU A 326 11634 12783 8043 -300 -720 1342 N ATOM 2053 CA LEU A 326 -30.757 -19.288 -14.588 1.00 84.87 C ANISOU 2053 CA LEU A 326 11470 12472 8306 -125 -505 1500 C ATOM 2054 C LEU A 326 -31.635 -19.365 -13.342 1.00 81.36 C ANISOU 2054 C LEU A 326 10840 11996 8079 -324 -501 1460 C ATOM 2055 O LEU A 326 -31.148 -19.232 -12.221 1.00 78.00 O ANISOU 2055 O LEU A 326 10468 11289 7882 -313 -344 1445 O ATOM 2056 CB LEU A 326 -30.717 -17.853 -15.126 1.00 85.56 C ANISOU 2056 CB LEU A 326 11344 12712 8452 204 -432 1806 C ATOM 2057 CG LEU A 326 -30.163 -16.751 -14.218 1.00 84.41 C ANISOU 2057 CG LEU A 326 11107 12305 8659 409 -208 1965 C ATOM 2058 CD1 LEU A 326 -29.361 -15.751 -15.032 1.00 89.55 C ANISOU 2058 CD1 LEU A 326 11777 12942 9306 708 -89 2207 C ATOM 2059 CD2 LEU A 326 -31.281 -16.040 -13.472 1.00 83.68 C ANISOU 2059 CD2 LEU A 326 10681 12326 8787 419 -217 2060 C ATOM 2060 N GLY A 327 -32.930 -19.584 -13.546 1.00 83.68 N ANISOU 2060 N GLY A 327 10901 12610 8283 -510 -673 1436 N ATOM 2061 CA GLY A 327 -33.874 -19.656 -12.446 1.00 80.90 C ANISOU 2061 CA GLY A 327 10326 12303 8110 -716 -656 1403 C ATOM 2062 C GLY A 327 -33.667 -20.866 -11.557 1.00 75.10 C ANISOU 2062 C GLY A 327 9848 11288 7399 -1042 -628 1195 C ATOM 2063 O GLY A 327 -33.598 -20.743 -10.334 1.00 72.58 O ANISOU 2063 O GLY A 327 9509 10791 7278 -1085 -480 1205 O ATOM 2064 N ILE A 328 -33.566 -22.040 -12.173 1.00 74.86 N ANISOU 2064 N ILE A 328 10075 11211 7159 -1266 -771 1008 N ATOM 2065 CA ILE A 328 -33.407 -23.288 -11.434 1.00 73.80 C ANISOU 2065 CA ILE A 328 10224 10773 7043 -1587 -768 824 C ATOM 2066 C ILE A 328 -32.057 -23.358 -10.726 1.00 75.59 C ANISOU 2066 C ILE A 328 10757 10570 7393 -1417 -596 824 C ATOM 2067 O ILE A 328 -31.982 -23.734 -9.555 1.00 81.76 O ANISOU 2067 O ILE A 328 11631 11128 8306 -1561 -507 810 O ATOM 2068 CB ILE A 328 -33.559 -24.509 -12.362 1.00 75.03 C ANISOU 2068 CB ILE A 328 10614 10935 6959 -1842 -969 597 C ATOM 2069 CG1 ILE A 328 -34.936 -24.498 -13.029 1.00 79.51 C ANISOU 2069 CG1 ILE A 328 10852 11965 7395 -2050 -1172 573 C ATOM 2070 CG2 ILE A 328 -33.356 -25.802 -11.586 1.00 75.76 C ANISOU 2070 CG2 ILE A 328 11041 10641 7105 -2161 -960 431 C ATOM 2071 CD1 ILE A 328 -35.154 -25.631 -14.005 1.00 82.61 C ANISOU 2071 CD1 ILE A 328 11449 12401 7537 -2318 -1392 315 C ATOM 2072 N VAL A 329 -30.995 -22.991 -11.438 1.00 73.31 N ANISOU 2072 N VAL A 329 10609 10197 7049 -1113 -549 849 N ATOM 2073 CA VAL A 329 -29.645 -23.028 -10.882 1.00 67.91 C ANISOU 2073 CA VAL A 329 10175 9148 6479 -928 -401 839 C ATOM 2074 C VAL A 329 -29.501 -22.080 -9.693 1.00 65.38 C ANISOU 2074 C VAL A 329 9677 8755 6409 -803 -232 985 C ATOM 2075 O VAL A 329 -28.964 -22.459 -8.651 1.00 65.80 O ANISOU 2075 O VAL A 329 9894 8537 6569 -848 -156 944 O ATOM 2076 CB VAL A 329 -28.588 -22.673 -11.949 1.00 63.70 C ANISOU 2076 CB VAL A 329 9751 8612 5840 -625 -358 854 C ATOM 2077 CG1 VAL A 329 -27.219 -22.493 -11.310 1.00 58.02 C ANISOU 2077 CG1 VAL A 329 9188 7574 5282 -413 -193 866 C ATOM 2078 CG2 VAL A 329 -28.540 -23.746 -13.024 1.00 57.78 C ANISOU 2078 CG2 VAL A 329 9244 7886 4822 -735 -505 647 C ATOM 2079 N PHE A 330 -29.989 -20.852 -9.846 1.00 62.69 N ANISOU 2079 N PHE A 330 9011 8655 6155 -637 -182 1150 N ATOM 2080 CA PHE A 330 -29.916 -19.867 -8.770 1.00 63.01 C ANISOU 2080 CA PHE A 330 8871 8632 6438 -507 -21 1254 C ATOM 2081 C PHE A 330 -30.794 -20.274 -7.592 1.00 66.65 C ANISOU 2081 C PHE A 330 9244 9120 6959 -775 -9 1202 C ATOM 2082 O PHE A 330 -30.509 -19.925 -6.447 1.00 68.51 O ANISOU 2082 O PHE A 330 9467 9220 7344 -739 123 1210 O ATOM 2083 CB PHE A 330 -30.327 -18.477 -9.264 1.00 62.25 C ANISOU 2083 CB PHE A 330 8457 8757 6438 -259 22 1439 C ATOM 2084 CG PHE A 330 -29.277 -17.784 -10.090 1.00 60.64 C ANISOU 2084 CG PHE A 330 8328 8469 6243 32 92 1548 C ATOM 2085 CD1 PHE A 330 -28.132 -18.450 -10.494 1.00 58.86 C ANISOU 2085 CD1 PHE A 330 8399 8055 5910 59 103 1454 C ATOM 2086 CD2 PHE A 330 -29.434 -16.455 -10.450 1.00 63.05 C ANISOU 2086 CD2 PHE A 330 8402 8878 6677 281 161 1751 C ATOM 2087 CE1 PHE A 330 -27.171 -17.809 -11.252 1.00 59.44 C ANISOU 2087 CE1 PHE A 330 8513 8086 5986 305 194 1561 C ATOM 2088 CE2 PHE A 330 -28.474 -15.808 -11.205 1.00 63.24 C ANISOU 2088 CE2 PHE A 330 8497 8819 6712 515 246 1882 C ATOM 2089 CZ PHE A 330 -27.342 -16.486 -11.607 1.00 60.95 C ANISOU 2089 CZ PHE A 330 8479 8382 6297 514 271 1785 C ATOM 2090 N PHE A 331 -31.865 -21.006 -7.879 1.00 72.13 N ANISOU 2090 N PHE A 331 9869 10013 7523 -1059 -143 1144 N ATOM 2091 CA PHE A 331 -32.763 -21.482 -6.835 1.00 74.65 C ANISOU 2091 CA PHE A 331 10095 10392 7877 -1365 -119 1107 C ATOM 2092 C PHE A 331 -32.071 -22.519 -5.959 1.00 71.35 C ANISOU 2092 C PHE A 331 10044 9623 7442 -1540 -83 1024 C ATOM 2093 O PHE A 331 -32.191 -22.487 -4.735 1.00 68.44 O ANISOU 2093 O PHE A 331 9655 9198 7151 -1629 33 1047 O ATOM 2094 CB PHE A 331 -34.037 -22.070 -7.441 1.00 78.83 C ANISOU 2094 CB PHE A 331 10451 11224 8276 -1663 -282 1057 C ATOM 2095 CG PHE A 331 -34.991 -22.627 -6.423 1.00 79.29 C ANISOU 2095 CG PHE A 331 10397 11365 8363 -2027 -241 1025 C ATOM 2096 CD1 PHE A 331 -35.761 -21.782 -5.642 1.00 78.68 C ANISOU 2096 CD1 PHE A 331 9950 11529 8415 -1983 -111 1102 C ATOM 2097 CD2 PHE A 331 -35.120 -23.996 -6.250 1.00 79.43 C ANISOU 2097 CD2 PHE A 331 10682 11214 8283 -2414 -318 919 C ATOM 2098 CE1 PHE A 331 -36.639 -22.291 -4.704 1.00 80.64 C ANISOU 2098 CE1 PHE A 331 10076 11895 8669 -2328 -43 1079 C ATOM 2099 CE2 PHE A 331 -35.997 -24.510 -5.315 1.00 80.30 C ANISOU 2099 CE2 PHE A 331 10691 11404 8414 -2780 -258 921 C ATOM 2100 CZ PHE A 331 -36.757 -23.656 -4.541 1.00 83.77 C ANISOU 2100 CZ PHE A 331 10739 12132 8957 -2742 -113 1004 C ATOM 2101 N LEU A 332 -31.346 -23.435 -6.594 1.00 72.68 N ANISOU 2101 N LEU A 332 10553 9563 7499 -1569 -183 928 N ATOM 2102 CA LEU A 332 -30.622 -24.476 -5.875 1.00 76.18 C ANISOU 2102 CA LEU A 332 11376 9637 7932 -1688 -174 863 C ATOM 2103 C LEU A 332 -29.502 -23.883 -5.027 1.00 80.54 C ANISOU 2103 C LEU A 332 12002 9991 8609 -1412 -37 920 C ATOM 2104 O LEU A 332 -29.177 -24.408 -3.963 1.00 87.08 O ANISOU 2104 O LEU A 332 13019 10610 9456 -1506 4 927 O ATOM 2105 CB LEU A 332 -30.056 -25.510 -6.850 1.00 75.97 C ANISOU 2105 CB LEU A 332 11684 9404 7777 -1717 -309 722 C ATOM 2106 CG LEU A 332 -31.084 -26.350 -7.611 1.00 79.53 C ANISOU 2106 CG LEU A 332 12138 9988 8090 -2055 -474 608 C ATOM 2107 CD1 LEU A 332 -30.392 -27.348 -8.526 1.00 84.23 C ANISOU 2107 CD1 LEU A 332 13103 10338 8562 -2044 -591 425 C ATOM 2108 CD2 LEU A 332 -32.017 -27.061 -6.643 1.00 80.28 C ANISOU 2108 CD2 LEU A 332 12232 10053 8217 -2472 -472 625 C ATOM 2109 N PHE A 333 -28.913 -22.792 -5.506 1.00 80.25 N ANISOU 2109 N PHE A 333 11814 10025 8650 -1084 28 968 N ATOM 2110 CA PHE A 333 -27.899 -22.074 -4.743 1.00 78.36 C ANISOU 2110 CA PHE A 333 11583 9636 8552 -837 154 1004 C ATOM 2111 C PHE A 333 -28.486 -21.552 -3.439 1.00 70.46 C ANISOU 2111 C PHE A 333 10401 8730 7642 -920 262 1050 C ATOM 2112 O PHE A 333 -27.972 -21.832 -2.356 1.00 67.57 O ANISOU 2112 O PHE A 333 10186 8197 7289 -944 307 1035 O ATOM 2113 CB PHE A 333 -27.323 -20.915 -5.564 1.00 84.09 C ANISOU 2113 CB PHE A 333 12145 10438 9366 -520 217 1064 C ATOM 2114 CG PHE A 333 -26.399 -20.014 -4.785 1.00 86.18 C ANISOU 2114 CG PHE A 333 12356 10577 9813 -301 350 1089 C ATOM 2115 CD1 PHE A 333 -25.048 -20.301 -4.691 1.00 89.18 C ANISOU 2115 CD1 PHE A 333 12943 10724 10218 -158 362 1034 C ATOM 2116 CD2 PHE A 333 -26.882 -18.874 -4.157 1.00 84.74 C ANISOU 2116 CD2 PHE A 333 11901 10513 9783 -234 459 1144 C ATOM 2117 CE1 PHE A 333 -24.196 -19.475 -3.980 1.00 86.71 C ANISOU 2117 CE1 PHE A 333 12555 10317 10074 15 466 1035 C ATOM 2118 CE2 PHE A 333 -26.035 -18.045 -3.446 1.00 83.21 C ANISOU 2118 CE2 PHE A 333 11665 10192 9760 -59 570 1130 C ATOM 2119 CZ PHE A 333 -24.691 -18.345 -3.357 1.00 83.45 C ANISOU 2119 CZ PHE A 333 11891 10008 9809 50 567 1076 C ATOM 2120 N LEU A 334 -29.567 -20.788 -3.559 1.00 66.26 N ANISOU 2120 N LEU A 334 9535 8484 7155 -944 301 1101 N ATOM 2121 CA LEU A 334 -30.227 -20.189 -2.408 1.00 62.42 C ANISOU 2121 CA LEU A 334 8829 8137 6751 -994 427 1118 C ATOM 2122 C LEU A 334 -30.810 -21.250 -1.482 1.00 66.08 C ANISOU 2122 C LEU A 334 9417 8598 7093 -1343 423 1099 C ATOM 2123 O LEU A 334 -30.790 -21.098 -0.261 1.00 68.47 O ANISOU 2123 O LEU A 334 9716 8894 7405 -1381 535 1096 O ATOM 2124 CB LEU A 334 -31.328 -19.231 -2.869 1.00 62.43 C ANISOU 2124 CB LEU A 334 8432 8457 6830 -924 455 1172 C ATOM 2125 CG LEU A 334 -30.881 -18.077 -3.769 1.00 60.41 C ANISOU 2125 CG LEU A 334 8043 8207 6704 -581 470 1244 C ATOM 2126 CD1 LEU A 334 -32.082 -17.346 -4.346 1.00 61.13 C ANISOU 2126 CD1 LEU A 334 7766 8618 6843 -519 449 1325 C ATOM 2127 CD2 LEU A 334 -29.982 -17.115 -3.007 1.00 58.45 C ANISOU 2127 CD2 LEU A 334 7796 7774 6640 -346 617 1228 C ATOM 2128 N LEU A 335 -31.320 -22.328 -2.071 1.00 69.05 N ANISOU 2128 N LEU A 335 9914 8976 7345 -1610 297 1084 N ATOM 2129 CA LEU A 335 -31.941 -23.403 -1.304 1.00 68.42 C ANISOU 2129 CA LEU A 335 9965 8870 7161 -1993 294 1091 C ATOM 2130 C LEU A 335 -30.930 -24.116 -0.411 1.00 67.68 C ANISOU 2130 C LEU A 335 10259 8435 7021 -2000 306 1106 C ATOM 2131 O LEU A 335 -31.269 -24.571 0.680 1.00 73.55 O ANISOU 2131 O LEU A 335 11077 9172 7696 -2223 377 1161 O ATOM 2132 CB LEU A 335 -32.611 -24.411 -2.241 1.00 69.29 C ANISOU 2132 CB LEU A 335 10147 9006 7174 -2285 137 1047 C ATOM 2133 CG LEU A 335 -33.444 -25.511 -1.583 1.00 72.92 C ANISOU 2133 CG LEU A 335 10701 9453 7551 -2750 137 1066 C ATOM 2134 CD1 LEU A 335 -34.583 -24.909 -0.774 1.00 73.82 C ANISOU 2134 CD1 LEU A 335 10420 9937 7690 -2893 287 1123 C ATOM 2135 CD2 LEU A 335 -33.978 -26.479 -2.627 1.00 76.55 C ANISOU 2135 CD2 LEU A 335 11252 9896 7939 -3033 -41 980 C ATOM 2136 N MET A 336 -29.688 -24.211 -0.877 1.00 63.07 N ANISOU 2136 N MET A 336 9910 7590 6464 -1747 239 1068 N ATOM 2137 CA MET A 336 -28.640 -24.875 -0.111 1.00 61.88 C ANISOU 2137 CA MET A 336 10110 7121 6279 -1695 220 1084 C ATOM 2138 C MET A 336 -28.058 -23.953 0.957 1.00 59.72 C ANISOU 2138 C MET A 336 9734 6893 6063 -1483 337 1104 C ATOM 2139 O MET A 336 -27.422 -24.413 1.906 1.00 59.69 O ANISOU 2139 O MET A 336 9962 6719 6000 -1479 331 1140 O ATOM 2140 CB MET A 336 -27.532 -25.376 -1.039 1.00 60.56 C ANISOU 2140 CB MET A 336 10203 6682 6123 -1493 105 1013 C ATOM 2141 CG MET A 336 -27.950 -26.534 -1.932 1.00 61.61 C ANISOU 2141 CG MET A 336 10545 6691 6173 -1720 -27 951 C ATOM 2142 SD MET A 336 -26.631 -27.094 -3.027 1.00 92.14 S ANISOU 2142 SD MET A 336 14708 10264 10038 -1442 -133 824 S ATOM 2143 CE MET A 336 -25.445 -27.717 -1.839 1.00 83.50 C ANISOU 2143 CE MET A 336 13946 8810 8972 -1305 -141 878 C ATOM 2144 N TRP A 337 -28.275 -22.651 0.801 1.00 60.50 N ANISOU 2144 N TRP A 337 9494 7215 6277 -1303 434 1077 N ATOM 2145 CA TRP A 337 -27.865 -21.687 1.816 1.00 61.69 C ANISOU 2145 CA TRP A 337 9519 7424 6495 -1132 551 1053 C ATOM 2146 C TRP A 337 -28.976 -21.474 2.838 1.00 58.60 C ANISOU 2146 C TRP A 337 8944 7284 6036 -1336 678 1071 C ATOM 2147 O TRP A 337 -28.747 -20.911 3.909 1.00 55.21 O ANISOU 2147 O TRP A 337 8463 6914 5599 -1260 777 1032 O ATOM 2148 CB TRP A 337 -27.477 -20.349 1.181 1.00 66.47 C ANISOU 2148 CB TRP A 337 9878 8088 7290 -828 607 1007 C ATOM 2149 CG TRP A 337 -26.032 -20.247 0.794 1.00 68.52 C ANISOU 2149 CG TRP A 337 10289 8119 7627 -581 555 974 C ATOM 2150 CD1 TRP A 337 -25.526 -20.144 -0.470 1.00 71.72 C ANISOU 2150 CD1 TRP A 337 10703 8455 8091 -429 507 980 C ATOM 2151 CD2 TRP A 337 -24.904 -20.235 1.679 1.00 68.65 C ANISOU 2151 CD2 TRP A 337 10444 7984 7655 -460 550 926 C ATOM 2152 NE1 TRP A 337 -24.154 -20.068 -0.426 1.00 67.86 N ANISOU 2152 NE1 TRP A 337 10333 7781 7669 -227 493 938 N ATOM 2153 CE2 TRP A 337 -23.748 -20.122 0.881 1.00 67.31 C ANISOU 2153 CE2 TRP A 337 10335 7658 7580 -239 505 900 C ATOM 2154 CE3 TRP A 337 -24.759 -20.309 3.068 1.00 68.89 C ANISOU 2154 CE3 TRP A 337 10543 8028 7605 -516 577 902 C ATOM 2155 CZ2 TRP A 337 -22.466 -20.081 1.425 1.00 67.28 C ANISOU 2155 CZ2 TRP A 337 10426 7513 7622 -77 476 844 C ATOM 2156 CZ3 TRP A 337 -23.486 -20.269 3.606 1.00 66.72 C ANISOU 2156 CZ3 TRP A 337 10385 7615 7353 -348 526 849 C ATOM 2157 CH2 TRP A 337 -22.356 -20.158 2.786 1.00 66.33 C ANISOU 2157 CH2 TRP A 337 10365 7412 7428 -131 472 816 C ATOM 2158 N CYS A 338 -30.179 -21.926 2.498 1.00 59.88 N ANISOU 2158 N CYS A 338 8992 7618 6141 -1601 676 1112 N ATOM 2159 CA CYS A 338 -31.333 -21.805 3.388 1.00 62.76 C ANISOU 2159 CA CYS A 338 9144 8268 6435 -1824 815 1131 C ATOM 2160 C CYS A 338 -31.169 -22.486 4.757 1.00 64.93 C ANISOU 2160 C CYS A 338 9654 8486 6529 -2012 876 1188 C ATOM 2161 O CYS A 338 -31.489 -21.871 5.773 1.00 65.47 O ANISOU 2161 O CYS A 338 9561 8764 6552 -2000 1031 1155 O ATOM 2162 CB CYS A 338 -32.591 -22.348 2.700 1.00 64.64 C ANISOU 2162 CB CYS A 338 9223 8696 6643 -2118 775 1167 C ATOM 2163 SG CYS A 338 -33.368 -21.202 1.543 1.00 63.09 S ANISOU 2163 SG CYS A 338 8567 8790 6613 -1918 768 1124 S ATOM 2164 N PRO A 339 -30.683 -23.748 4.799 1.00 66.30 N ANISOU 2164 N PRO A 339 10220 8381 6592 -2174 756 1276 N ATOM 2165 CA PRO A 339 -30.602 -24.399 6.115 1.00 67.81 C ANISOU 2165 CA PRO A 339 10643 8532 6589 -2356 812 1380 C ATOM 2166 C PRO A 339 -29.729 -23.654 7.123 1.00 67.50 C ANISOU 2166 C PRO A 339 10622 8516 6508 -2092 869 1327 C ATOM 2167 O PRO A 339 -29.965 -23.766 8.324 1.00 73.64 O ANISOU 2167 O PRO A 339 11447 9433 7101 -2223 973 1384 O ATOM 2168 CB PRO A 339 -29.991 -25.766 5.793 1.00 68.79 C ANISOU 2168 CB PRO A 339 11212 8266 6661 -2467 640 1478 C ATOM 2169 CG PRO A 339 -30.349 -26.013 4.381 1.00 68.42 C ANISOU 2169 CG PRO A 339 11101 8163 6734 -2518 539 1414 C ATOM 2170 CD PRO A 339 -30.272 -24.671 3.724 1.00 67.17 C ANISOU 2170 CD PRO A 339 10588 8205 6729 -2209 577 1289 C ATOM 2171 N PHE A 340 -28.743 -22.905 6.643 1.00 63.31 N ANISOU 2171 N PHE A 340 10049 7870 6135 -1743 804 1216 N ATOM 2172 CA PHE A 340 -27.865 -22.154 7.532 1.00 62.34 C ANISOU 2172 CA PHE A 340 9921 7768 5997 -1504 836 1129 C ATOM 2173 C PHE A 340 -28.517 -20.878 8.055 1.00 64.69 C ANISOU 2173 C PHE A 340 9857 8377 6345 -1436 1022 996 C ATOM 2174 O PHE A 340 -28.664 -20.697 9.264 1.00 72.21 O ANISOU 2174 O PHE A 340 10803 9502 7129 -1492 1126 965 O ATOM 2175 CB PHE A 340 -26.558 -21.799 6.826 1.00 59.89 C ANISOU 2175 CB PHE A 340 9670 7224 5860 -1184 712 1051 C ATOM 2176 CG PHE A 340 -25.735 -20.781 7.562 1.00 56.06 C ANISOU 2176 CG PHE A 340 9084 6791 5425 -945 748 915 C ATOM 2177 CD1 PHE A 340 -25.054 -21.127 8.717 1.00 56.29 C ANISOU 2177 CD1 PHE A 340 9315 6802 5271 -931 693 929 C ATOM 2178 CD2 PHE A 340 -25.645 -19.477 7.102 1.00 53.17 C ANISOU 2178 CD2 PHE A 340 8428 6487 5289 -742 826 775 C ATOM 2179 CE1 PHE A 340 -24.299 -20.193 9.400 1.00 55.33 C ANISOU 2179 CE1 PHE A 340 9088 6749 5185 -734 706 769 C ATOM 2180 CE2 PHE A 340 -24.890 -18.538 7.781 1.00 51.23 C ANISOU 2180 CE2 PHE A 340 8093 6261 5110 -557 856 621 C ATOM 2181 CZ PHE A 340 -24.217 -18.897 8.931 1.00 52.68 C ANISOU 2181 CZ PHE A 340 8461 6453 5102 -560 792 600 C ATOM 2182 N PHE A 341 -28.898 -19.996 7.135 1.00 60.01 N ANISOU 2182 N PHE A 341 8972 7852 5975 -1299 1064 915 N ATOM 2183 CA PHE A 341 -29.421 -18.682 7.494 1.00 59.26 C ANISOU 2183 CA PHE A 341 8535 7988 5993 -1162 1232 770 C ATOM 2184 C PHE A 341 -30.748 -18.756 8.247 1.00 62.16 C ANISOU 2184 C PHE A 341 8716 8689 6213 -1395 1403 777 C ATOM 2185 O PHE A 341 -31.053 -17.883 9.059 1.00 61.07 O ANISOU 2185 O PHE A 341 8381 8752 6070 -1306 1564 635 O ATOM 2186 CB PHE A 341 -29.581 -17.815 6.242 1.00 56.91 C ANISOU 2186 CB PHE A 341 7992 7662 5969 -959 1221 738 C ATOM 2187 CG PHE A 341 -28.276 -17.356 5.651 1.00 52.93 C ANISOU 2187 CG PHE A 341 7586 6890 5634 -697 1125 698 C ATOM 2188 CD1 PHE A 341 -27.548 -16.343 6.251 1.00 49.41 C ANISOU 2188 CD1 PHE A 341 7077 6392 5305 -490 1185 549 C ATOM 2189 CD2 PHE A 341 -27.782 -17.933 4.493 1.00 53.17 C ANISOU 2189 CD2 PHE A 341 7761 6735 5706 -670 984 793 C ATOM 2190 CE1 PHE A 341 -26.349 -15.916 5.711 1.00 45.19 C ANISOU 2190 CE1 PHE A 341 6602 5626 4941 -285 1110 516 C ATOM 2191 CE2 PHE A 341 -26.584 -17.509 3.948 1.00 51.80 C ANISOU 2191 CE2 PHE A 341 7650 6352 5681 -440 924 761 C ATOM 2192 CZ PHE A 341 -25.867 -16.500 4.558 1.00 51.98 C ANISOU 2192 CZ PHE A 341 7588 6327 5835 -258 989 634 C ATOM 2193 N ILE A 342 -31.538 -19.791 7.977 1.00 67.02 N ANISOU 2193 N ILE A 342 9384 9367 6713 -1700 1380 924 N ATOM 2194 CA ILE A 342 -32.781 -19.993 8.713 1.00 75.11 C ANISOU 2194 CA ILE A 342 10228 10726 7582 -1972 1556 951 C ATOM 2195 C ILE A 342 -32.460 -20.453 10.133 1.00 80.96 C ANISOU 2195 C ILE A 342 11209 11514 8039 -2104 1630 990 C ATOM 2196 O ILE A 342 -33.125 -20.059 11.092 1.00 85.88 O ANISOU 2196 O ILE A 342 11652 12452 8526 -2175 1833 923 O ATOM 2197 CB ILE A 342 -33.703 -21.016 8.015 1.00 59.95 C ANISOU 2197 CB ILE A 342 8294 8853 5631 -2314 1502 1097 C ATOM 2198 CG1 ILE A 342 -34.177 -20.467 6.668 1.00 64.02 C ANISOU 2198 CG1 ILE A 342 8518 9422 6383 -2179 1431 1051 C ATOM 2199 CG2 ILE A 342 -34.906 -21.346 8.883 1.00 63.54 C ANISOU 2199 CG2 ILE A 342 8577 9660 5907 -2647 1699 1147 C ATOM 2200 CD1 ILE A 342 -35.057 -21.423 5.894 1.00 65.96 C ANISOU 2200 CD1 ILE A 342 8726 9733 6602 -2513 1344 1152 C ATOM 2201 N THR A 343 -31.421 -21.272 10.262 1.00 79.65 N ANISOU 2201 N THR A 343 11446 11048 7770 -2112 1466 1097 N ATOM 2202 CA THR A 343 -30.988 -21.762 11.565 1.00 78.00 C ANISOU 2202 CA THR A 343 11508 10863 7268 -2205 1492 1172 C ATOM 2203 C THR A 343 -30.232 -20.679 12.333 1.00 76.95 C ANISOU 2203 C THR A 343 11307 10811 7121 -1905 1531 967 C ATOM 2204 O THR A 343 -30.317 -20.600 13.560 1.00 79.27 O ANISOU 2204 O THR A 343 11641 11325 7153 -1967 1644 941 O ATOM 2205 CB THR A 343 -30.090 -23.009 11.428 1.00 76.78 C ANISOU 2205 CB THR A 343 11808 10337 7026 -2269 1277 1364 C ATOM 2206 OG1 THR A 343 -30.730 -23.971 10.579 1.00 76.37 O ANISOU 2206 OG1 THR A 343 11832 10153 7033 -2538 1222 1506 O ATOM 2207 CG2 THR A 343 -29.825 -23.638 12.787 1.00 79.66 C ANISOU 2207 CG2 THR A 343 12462 10754 7052 -2401 1300 1508 C ATOM 2208 N ASN A 344 -29.500 -19.844 11.603 1.00 73.34 N ANISOU 2208 N ASN A 344 10746 10183 6936 -1596 1442 816 N ATOM 2209 CA ASN A 344 -28.695 -18.792 12.214 1.00 73.11 C ANISOU 2209 CA ASN A 344 10653 10178 6948 -1327 1456 596 C ATOM 2210 C ASN A 344 -29.552 -17.740 12.913 1.00 78.91 C ANISOU 2210 C ASN A 344 11071 11246 7667 -1295 1695 392 C ATOM 2211 O ASN A 344 -29.210 -17.272 13.999 1.00 89.79 O ANISOU 2211 O ASN A 344 12472 12764 8882 -1225 1756 233 O ATOM 2212 CB ASN A 344 -27.805 -18.126 11.164 1.00 68.57 C ANISOU 2212 CB ASN A 344 10015 9334 6704 -1046 1333 502 C ATOM 2213 CG ASN A 344 -26.702 -17.288 11.780 1.00 68.37 C ANISOU 2213 CG ASN A 344 9997 9257 6723 -815 1292 298 C ATOM 2214 OD1 ASN A 344 -26.316 -17.498 12.930 1.00 69.15 O ANISOU 2214 OD1 ASN A 344 10245 9465 6563 -852 1274 260 O ATOM 2215 ND2 ASN A 344 -26.187 -16.332 11.016 1.00 68.29 N ANISOU 2215 ND2 ASN A 344 9827 9087 7033 -588 1273 171 N ATOM 2216 N ILE A 345 -30.667 -17.370 12.288 1.00 77.70 N ANISOU 2216 N ILE A 345 10615 11233 7676 -1332 1823 380 N ATOM 2217 CA ILE A 345 -31.586 -16.406 12.885 1.00 79.01 C ANISOU 2217 CA ILE A 345 10450 11720 7852 -1276 2063 182 C ATOM 2218 C ILE A 345 -32.434 -17.074 13.962 1.00 82.54 C ANISOU 2218 C ILE A 345 10913 12512 7934 -1573 2235 257 C ATOM 2219 O ILE A 345 -32.955 -16.409 14.856 1.00 80.93 O ANISOU 2219 O ILE A 345 10520 12611 7617 -1536 2447 69 O ATOM 2220 CB ILE A 345 -32.509 -15.760 11.829 1.00 79.55 C ANISOU 2220 CB ILE A 345 10155 11843 8229 -1177 2130 157 C ATOM 2221 CG1 ILE A 345 -33.408 -16.813 11.179 1.00 80.70 C ANISOU 2221 CG1 ILE A 345 10270 12079 8314 -1472 2099 392 C ATOM 2222 CG2 ILE A 345 -31.689 -15.029 10.777 1.00 77.31 C ANISOU 2222 CG2 ILE A 345 9858 11231 8285 -885 1987 110 C ATOM 2223 CD1 ILE A 345 -34.380 -16.247 10.168 1.00 82.20 C ANISOU 2223 CD1 ILE A 345 10080 12387 8766 -1383 2137 382 C ATOM 2224 N THR A 346 -32.565 -18.394 13.871 1.00 88.94 N ANISOU 2224 N THR A 346 11962 13269 8564 -1874 2153 531 N ATOM 2225 CA THR A 346 -33.286 -19.163 14.877 1.00 96.99 C ANISOU 2225 CA THR A 346 13051 14578 9222 -2204 2312 666 C ATOM 2226 C THR A 346 -32.459 -19.223 16.156 1.00 98.27 C ANISOU 2226 C THR A 346 13489 14790 9057 -2163 2304 630 C ATOM 2227 O THR A 346 -33.000 -19.234 17.263 1.00104.29 O ANISOU 2227 O THR A 346 14216 15904 9505 -2306 2507 608 O ATOM 2228 CB THR A 346 -33.596 -20.592 14.386 1.00 69.07 C ANISOU 2228 CB THR A 346 9734 10895 5614 -2557 2211 982 C ATOM 2229 OG1 THR A 346 -34.287 -20.531 13.132 1.00 89.81 O ANISOU 2229 OG1 THR A 346 12106 13485 8531 -2587 2177 990 O ATOM 2230 CG2 THR A 346 -34.458 -21.336 15.397 1.00 73.31 C ANISOU 2230 CG2 THR A 346 10311 11743 5801 -2940 2413 1147 C ATOM 2231 N LEU A 347 -31.141 -19.246 15.990 1.00 90.42 N ANISOU 2231 N LEU A 347 12753 13474 8126 -1959 2067 618 N ATOM 2232 CA LEU A 347 -30.215 -19.273 17.117 1.00 89.95 C ANISOU 2232 CA LEU A 347 12947 13456 7775 -1881 1998 573 C ATOM 2233 C LEU A 347 -30.330 -17.999 17.950 1.00 90.23 C ANISOU 2233 C LEU A 347 12743 13788 7755 -1699 2173 221 C ATOM 2234 O LEU A 347 -30.012 -17.992 19.139 1.00 96.56 O ANISOU 2234 O LEU A 347 13684 14801 8203 -1713 2204 156 O ATOM 2235 CB LEU A 347 -28.779 -19.452 16.619 1.00 87.58 C ANISOU 2235 CB LEU A 347 12890 12765 7624 -1667 1699 598 C ATOM 2236 CG LEU A 347 -27.701 -19.778 17.655 1.00 90.66 C ANISOU 2236 CG LEU A 347 13584 13158 7705 -1598 1545 625 C ATOM 2237 CD1 LEU A 347 -27.858 -21.201 18.164 1.00 93.44 C ANISOU 2237 CD1 LEU A 347 14288 13500 7716 -1867 1498 992 C ATOM 2238 CD2 LEU A 347 -26.311 -19.562 17.076 1.00 90.43 C ANISOU 2238 CD2 LEU A 347 13641 12801 7917 -1319 1284 544 C ATOM 2239 N VAL A 348 -30.793 -16.925 17.318 1.00 85.48 N ANISOU 2239 N VAL A 348 11790 13194 7497 -1522 2282 -9 N ATOM 2240 CA VAL A 348 -30.939 -15.635 17.984 1.00 83.44 C ANISOU 2240 CA VAL A 348 11292 13149 7261 -1320 2454 -382 C ATOM 2241 C VAL A 348 -32.342 -15.442 18.552 1.00 85.44 C ANISOU 2241 C VAL A 348 11271 13839 7355 -1455 2775 -453 C ATOM 2242 O VAL A 348 -32.506 -15.129 19.732 1.00 87.75 O ANISOU 2242 O VAL A 348 11551 14454 7334 -1466 2941 -636 O ATOM 2243 CB VAL A 348 -30.628 -14.473 17.022 1.00 79.99 C ANISOU 2243 CB VAL A 348 10633 12444 7317 -1014 2406 -598 C ATOM 2244 CG1 VAL A 348 -30.896 -13.136 17.697 1.00 81.77 C ANISOU 2244 CG1 VAL A 348 10615 12848 7605 -811 2603 -999 C ATOM 2245 CG2 VAL A 348 -29.190 -14.556 16.544 1.00 64.28 C ANISOU 2245 CG2 VAL A 348 8874 10071 5478 -878 2124 -565 C ATOM 2246 N LEU A 349 -33.350 -15.629 17.706 1.00 73.18 N ANISOU 2246 N LEU A 349 9480 12321 6003 -1557 2860 -320 N ATOM 2247 CA LEU A 349 -34.737 -15.411 18.101 1.00 79.46 C ANISOU 2247 CA LEU A 349 9936 13547 6707 -1670 3167 -391 C ATOM 2248 C LEU A 349 -35.213 -16.451 19.112 1.00 83.00 C ANISOU 2248 C LEU A 349 10542 14328 6667 -2040 3308 -183 C ATOM 2249 O LEU A 349 -35.630 -16.108 20.218 1.00 89.51 O ANISOU 2249 O LEU A 349 11274 15543 7195 -2062 3550 -353 O ATOM 2250 CB LEU A 349 -35.649 -15.424 16.873 1.00 75.67 C ANISOU 2250 CB LEU A 349 9149 13033 6568 -1696 3176 -278 C ATOM 2251 CG LEU A 349 -35.333 -14.399 15.781 1.00 75.33 C ANISOU 2251 CG LEU A 349 8931 12687 7002 -1339 3056 -426 C ATOM 2252 CD1 LEU A 349 -36.359 -14.473 14.660 1.00 75.74 C ANISOU 2252 CD1 LEU A 349 8664 12798 7314 -1380 3065 -295 C ATOM 2253 CD2 LEU A 349 -35.262 -12.994 16.359 1.00 73.98 C ANISOU 2253 CD2 LEU A 349 8570 12587 6951 -1007 3210 -813 C ATOM 2254 N CYS A 350 -35.151 -17.721 18.724 1.00 80.86 N ANISOU 2254 N CYS A 350 10521 13892 6310 -2332 3166 184 N ATOM 2255 CA CYS A 350 -35.598 -18.807 19.589 1.00 84.94 C ANISOU 2255 CA CYS A 350 11226 14658 6391 -2722 3291 450 C ATOM 2256 C CYS A 350 -34.662 -18.996 20.778 1.00 87.93 C ANISOU 2256 C CYS A 350 11975 15078 6355 -2693 3233 457 C ATOM 2257 O CYS A 350 -33.611 -19.628 20.661 1.00 85.69 O ANISOU 2257 O CYS A 350 12074 14454 6030 -2671 2958 635 O ATOM 2258 CB CYS A 350 -35.710 -20.111 18.796 1.00 83.62 C ANISOU 2258 CB CYS A 350 11266 14217 6291 -3035 3130 830 C ATOM 2259 SG CYS A 350 -36.213 -21.544 19.780 1.00 87.11 S ANISOU 2259 SG CYS A 350 11973 14750 6376 -3445 3184 1197 S ATOM 2260 N ASP A 351 -35.051 -18.446 21.924 1.00 93.29 N ANISOU 2260 N ASP A 351 12528 16178 6742 -2659 3473 252 N ATOM 2261 CA ASP A 351 -34.253 -18.560 23.138 1.00 97.24 C ANISOU 2261 CA ASP A 351 13341 16752 6852 -2592 3392 234 C ATOM 2262 C ASP A 351 -34.599 -19.831 23.905 1.00102.80 C ANISOU 2262 C ASP A 351 14291 17494 7275 -2867 3380 627 C ATOM 2263 O ASP A 351 -34.017 -20.114 24.952 1.00105.24 O ANISOU 2263 O ASP A 351 14877 17879 7232 -2835 3305 693 O ATOM 2264 CB ASP A 351 -34.455 -17.334 24.031 1.00 99.92 C ANISOU 2264 CB ASP A 351 13442 17444 7079 -2356 3599 -207 C ATOM 2265 N SER A 352 -35.548 -20.597 23.376 1.00105.98 N ANISOU 2265 N SER A 352 14583 17843 7839 -3137 3449 882 N ATOM 2266 CA SER A 352 -35.984 -21.832 24.017 1.00112.21 C ANISOU 2266 CA SER A 352 15579 18636 8419 -3426 3465 1252 C ATOM 2267 C SER A 352 -35.291 -23.048 23.409 1.00115.49 C ANISOU 2267 C SER A 352 16389 18569 8922 -3558 3172 1614 C ATOM 2268 O SER A 352 -35.323 -24.140 23.976 1.00122.29 O ANISOU 2268 O SER A 352 17522 19335 9606 -3746 3127 1936 O ATOM 2269 CB SER A 352 -37.503 -21.984 23.906 1.00113.35 C ANISOU 2269 CB SER A 352 15354 19028 8684 -3670 3725 1290 C ATOM 2270 OG SER A 352 -38.172 -20.883 24.495 1.00115.16 O ANISOU 2270 OG SER A 352 15214 19692 8849 -3514 4000 951 O ATOM 2271 N CYS A 353 -34.663 -22.850 22.254 1.00111.10 N ANISOU 2271 N CYS A 353 15867 17698 8650 -3442 2983 1553 N ATOM 2272 CA CYS A 353 -33.989 -23.935 21.550 1.00110.61 C ANISOU 2272 CA CYS A 353 16162 17144 8721 -3523 2699 1845 C ATOM 2273 C CYS A 353 -32.689 -24.337 22.239 1.00110.67 C ANISOU 2273 C CYS A 353 16598 16970 8481 -3351 2465 1971 C ATOM 2274 O CYS A 353 -32.051 -23.524 22.908 1.00105.15 O ANISOU 2274 O CYS A 353 15904 16477 7571 -3119 2460 1755 O ATOM 2275 CB CYS A 353 -33.708 -23.537 20.099 1.00110.91 C ANISOU 2275 CB CYS A 353 16097 16924 9119 -3430 2580 1725 C ATOM 2276 SG CYS A 353 -35.186 -23.169 19.124 1.00166.23 S ANISOU 2276 SG CYS A 353 22593 24124 16443 -3612 2793 1615 S ATOM 2277 N ASN A 354 -32.304 -25.598 22.070 1.00117.69 N ANISOU 2277 N ASN A 354 17832 17476 9408 -3454 2262 2303 N ATOM 2278 CA ASN A 354 -31.071 -26.112 22.652 1.00 91.92 C ANISOU 2278 CA ASN A 354 14965 14014 5948 -3269 2010 2463 C ATOM 2279 C ASN A 354 -29.853 -25.560 21.922 1.00101.26 C ANISOU 2279 C ASN A 354 16237 14961 7277 -2975 1769 2292 C ATOM 2280 O ASN A 354 -29.574 -25.947 20.789 1.00 98.38 O ANISOU 2280 O ASN A 354 15954 14208 7219 -2969 1617 2350 O ATOM 2281 CB ASN A 354 -31.063 -27.643 22.616 1.00113.15 C ANISOU 2281 CB ASN A 354 17974 16330 8687 -3444 1877 2857 C ATOM 2282 CG ASN A 354 -30.014 -28.248 23.533 1.00114.58 C ANISOU 2282 CG ASN A 354 18525 16411 8599 -3263 1672 3072 C ATOM 2283 OD1 ASN A 354 -28.897 -27.741 23.646 1.00112.14 O ANISOU 2283 OD1 ASN A 354 18310 16092 8208 -2962 1480 2945 O ATOM 2284 ND2 ASN A 354 -30.373 -29.342 24.196 1.00118.25 N ANISOU 2284 ND2 ASN A 354 19194 16813 8924 -3448 1709 3404 N ATOM 2285 N GLN A 355 -29.130 -24.660 22.584 1.00104.00 N ANISOU 2285 N GLN A 355 16569 15550 7398 -2738 1735 2063 N ATOM 2286 CA GLN A 355 -27.979 -23.985 21.991 1.00102.97 C ANISOU 2286 CA GLN A 355 16492 15253 7378 -2469 1531 1854 C ATOM 2287 C GLN A 355 -26.910 -24.957 21.498 1.00106.99 C ANISOU 2287 C GLN A 355 17355 15281 8014 -2341 1195 2101 C ATOM 2288 O GLN A 355 -26.306 -24.744 20.447 1.00104.73 O ANISOU 2288 O GLN A 355 17028 14685 8078 -2158 1040 1986 O ATOM 2289 CB GLN A 355 -27.359 -23.016 23.001 1.00104.48 C ANISOU 2289 CB GLN A 355 16628 15795 7273 -2256 1520 1564 C ATOM 2290 CG GLN A 355 -28.313 -21.956 23.536 1.00108.34 C ANISOU 2290 CG GLN A 355 16756 16753 7655 -2312 1852 1245 C ATOM 2291 CD GLN A 355 -28.340 -20.697 22.688 1.00109.36 C ANISOU 2291 CD GLN A 355 16487 16802 8263 -2078 1897 829 C ATOM 2292 OE1 GLN A 355 -28.164 -19.591 23.199 1.00112.86 O ANISOU 2292 OE1 GLN A 355 16734 17474 8673 -1894 1965 450 O ATOM 2293 NE2 GLN A 355 -28.568 -20.858 21.391 1.00108.24 N ANISOU 2293 NE2 GLN A 355 16237 16327 8562 -2087 1857 897 N ATOM 2294 N THR A 356 -26.682 -26.022 22.259 1.00115.69 N ANISOU 2294 N THR A 356 18718 16301 8936 -2362 1079 2407 N ATOM 2295 CA THR A 356 -25.655 -27.002 21.923 1.00121.03 C ANISOU 2295 CA THR A 356 19715 16537 9733 -2200 765 2636 C ATOM 2296 C THR A 356 -26.013 -27.801 20.674 1.00117.74 C ANISOU 2296 C THR A 356 19352 15675 9710 -2332 737 2765 C ATOM 2297 O THR A 356 -25.172 -28.019 19.802 1.00117.70 O ANISOU 2297 O THR A 356 19471 15303 9945 -2141 521 2750 O ATOM 2298 CB THR A 356 -25.413 -27.983 23.085 1.00136.92 C ANISOU 2298 CB THR A 356 21983 18584 11456 -2192 675 2951 C ATOM 2299 OG1 THR A 356 -26.620 -28.702 23.366 1.00151.99 O ANISOU 2299 OG1 THR A 356 23881 20533 13337 -2518 901 3168 O ATOM 2300 CG2 THR A 356 -24.972 -27.233 24.333 1.00140.30 C ANISOU 2300 CG2 THR A 356 22374 19470 11462 -2038 666 2813 C ATOM 2301 N THR A 357 -27.267 -28.233 20.591 1.00113.66 N ANISOU 2301 N THR A 357 18729 15206 9251 -2657 954 2869 N ATOM 2302 CA THR A 357 -27.720 -29.058 19.477 1.00108.13 C ANISOU 2302 CA THR A 357 18075 14118 8889 -2830 926 2969 C ATOM 2303 C THR A 357 -28.233 -28.217 18.312 1.00100.50 C ANISOU 2303 C THR A 357 16817 13190 8178 -2883 1032 2719 C ATOM 2304 O THR A 357 -28.856 -28.740 17.389 1.00 97.40 O ANISOU 2304 O THR A 357 16388 12585 8035 -3076 1050 2756 O ATOM 2305 CB THR A 357 -28.831 -30.030 19.916 1.00112.56 C ANISOU 2305 CB THR A 357 18673 14698 9399 -3187 1084 3210 C ATOM 2306 N LEU A 358 -27.968 -26.915 18.356 1.00 98.47 N ANISOU 2306 N LEU A 358 16356 13207 7850 -2715 1100 2458 N ATOM 2307 CA LEU A 358 -28.410 -26.015 17.297 1.00 94.81 C ANISOU 2307 CA LEU A 358 15578 12799 7648 -2709 1207 2215 C ATOM 2308 C LEU A 358 -27.221 -25.412 16.556 1.00 89.35 C ANISOU 2308 C LEU A 358 14825 11875 7249 -2296 991 1991 C ATOM 2309 O LEU A 358 -27.277 -25.202 15.344 1.00 85.14 O ANISOU 2309 O LEU A 358 14134 11156 7059 -2224 954 1878 O ATOM 2310 CB LEU A 358 -29.294 -24.904 17.870 1.00 74.83 C ANISOU 2310 CB LEU A 358 12647 10768 5018 -2758 1489 1986 C ATOM 2311 CG LEU A 358 -30.115 -24.086 16.873 1.00 74.15 C ANISOU 2311 CG LEU A 358 12121 10774 5277 -2747 1625 1754 C ATOM 2312 CD1 LEU A 358 -30.982 -25.002 16.027 1.00 75.13 C ANISOU 2312 CD1 LEU A 358 12268 10740 5537 -3075 1647 1950 C ATOM 2313 CD2 LEU A 358 -30.972 -23.063 17.602 1.00 74.06 C ANISOU 2313 CD2 LEU A 358 11744 11254 5142 -2768 1911 1538 C ATOM 2314 N GLN A 359 -26.147 -25.134 17.288 1.00 89.14 N ANISOU 2314 N GLN A 359 14912 11885 7070 -2038 848 1932 N ATOM 2315 CA GLN A 359 -24.933 -24.599 16.684 1.00 85.28 C ANISOU 2315 CA GLN A 359 14359 11198 6846 -1669 645 1732 C ATOM 2316 C GLN A 359 -24.101 -25.728 16.088 1.00 84.57 C ANISOU 2316 C GLN A 359 14608 10668 6857 -1575 397 1942 C ATOM 2317 O GLN A 359 -23.219 -25.494 15.262 1.00 81.48 O ANISOU 2317 O GLN A 359 14157 10059 6742 -1310 249 1809 O ATOM 2318 CB GLN A 359 -24.116 -23.813 17.712 1.00 87.57 C ANISOU 2318 CB GLN A 359 14592 11734 6945 -1445 581 1547 C ATOM 2319 CG GLN A 359 -23.540 -24.658 18.834 1.00 93.86 C ANISOU 2319 CG GLN A 359 15755 12567 7341 -1447 426 1794 C ATOM 2320 CD GLN A 359 -23.026 -23.818 19.987 1.00 97.95 C ANISOU 2320 CD GLN A 359 16179 13449 7590 -1299 402 1583 C ATOM 2321 OE1 GLN A 359 -23.426 -22.666 20.157 1.00 99.68 O ANISOU 2321 OE1 GLN A 359 16079 13936 7859 -1284 577 1268 O ATOM 2322 NE2 GLN A 359 -22.133 -24.391 20.786 1.00101.04 N ANISOU 2322 NE2 GLN A 359 16849 13847 7693 -1178 174 1745 N ATOM 2323 N MET A 360 -24.389 -26.954 16.514 1.00 91.18 N ANISOU 2323 N MET A 360 15803 11367 7474 -1795 366 2273 N ATOM 2324 CA MET A 360 -23.748 -28.134 15.949 1.00 88.98 C ANISOU 2324 CA MET A 360 15881 10624 7304 -1725 150 2482 C ATOM 2325 C MET A 360 -24.285 -28.390 14.546 1.00 87.46 C ANISOU 2325 C MET A 360 15609 10177 7443 -1841 192 2424 C ATOM 2326 O MET A 360 -23.598 -28.960 13.699 1.00 89.13 O ANISOU 2326 O MET A 360 15984 10017 7862 -1675 20 2433 O ATOM 2327 CB MET A 360 -23.975 -29.355 16.841 1.00 91.81 C ANISOU 2327 CB MET A 360 16476 10908 7500 -1871 116 2772 C ATOM 2328 N LEU A 361 -25.523 -27.966 14.314 1.00 86.84 N ANISOU 2328 N LEU A 361 15267 10329 7401 -2117 418 2352 N ATOM 2329 CA LEU A 361 -26.134 -28.058 12.995 1.00 84.42 C ANISOU 2329 CA LEU A 361 14821 9874 7382 -2234 456 2267 C ATOM 2330 C LEU A 361 -25.553 -26.990 12.078 1.00 80.58 C ANISOU 2330 C LEU A 361 14027 9410 7179 -1905 415 1975 C ATOM 2331 O LEU A 361 -25.389 -27.210 10.878 1.00 76.79 O ANISOU 2331 O LEU A 361 13547 8694 6934 -1837 334 1912 O ATOM 2332 CB LEU A 361 -27.654 -27.907 13.087 1.00 86.12 C ANISOU 2332 CB LEU A 361 14805 10380 7537 -2620 699 2287 C ATOM 2333 CG LEU A 361 -28.390 -28.911 13.975 1.00 91.65 C ANISOU 2333 CG LEU A 361 15663 11114 8047 -2948 775 2527 C ATOM 2334 CD1 LEU A 361 -29.884 -28.625 13.979 1.00 92.08 C ANISOU 2334 CD1 LEU A 361 15390 11509 8088 -3297 1025 2495 C ATOM 2335 CD2 LEU A 361 -28.113 -30.335 13.518 1.00 96.62 C ANISOU 2335 CD2 LEU A 361 16612 11274 8826 -2996 591 2673 C ATOM 2336 N LEU A 362 -25.247 -25.832 12.655 1.00 82.12 N ANISOU 2336 N LEU A 362 13971 9889 7341 -1714 478 1794 N ATOM 2337 CA LEU A 362 -24.629 -24.740 11.914 1.00 80.96 C ANISOU 2337 CA LEU A 362 13543 9754 7465 -1412 453 1537 C ATOM 2338 C LEU A 362 -23.254 -25.144 11.399 1.00 84.09 C ANISOU 2338 C LEU A 362 14127 9834 7990 -1125 227 1534 C ATOM 2339 O LEU A 362 -22.848 -24.742 10.312 1.00 83.64 O ANISOU 2339 O LEU A 362 13927 9660 8193 -952 194 1402 O ATOM 2340 CB LEU A 362 -24.514 -23.490 12.788 1.00 78.94 C ANISOU 2340 CB LEU A 362 13029 9822 7141 -1286 556 1338 C ATOM 2341 CG LEU A 362 -25.812 -22.754 13.120 1.00 78.03 C ANISOU 2341 CG LEU A 362 12620 10049 6978 -1473 808 1247 C ATOM 2342 CD1 LEU A 362 -25.537 -21.591 14.059 1.00 58.72 C ANISOU 2342 CD1 LEU A 362 9982 7876 4455 -1316 890 1016 C ATOM 2343 CD2 LEU A 362 -26.481 -22.269 11.846 1.00 56.38 C ANISOU 2343 CD2 LEU A 362 9604 7281 4538 -1477 886 1158 C ATOM 2344 N GLU A 363 -22.547 -25.951 12.184 1.00 91.31 N ANISOU 2344 N GLU A 363 15357 10626 8710 -1066 77 1694 N ATOM 2345 CA GLU A 363 -21.215 -26.415 11.812 1.00 91.59 C ANISOU 2345 CA GLU A 363 15565 10380 8854 -767 -145 1700 C ATOM 2346 C GLU A 363 -21.273 -27.323 10.586 1.00 86.42 C ANISOU 2346 C GLU A 363 15084 9370 8381 -793 -205 1762 C ATOM 2347 O GLU A 363 -20.266 -27.538 9.912 1.00 87.63 O ANISOU 2347 O GLU A 363 15293 9306 8699 -523 -342 1697 O ATOM 2348 CB GLU A 363 -20.559 -27.146 12.986 1.00101.88 C ANISOU 2348 CB GLU A 363 17179 11645 9887 -694 -306 1893 C ATOM 2349 CG GLU A 363 -19.043 -27.212 12.911 1.00109.46 C ANISOU 2349 CG GLU A 363 18182 12467 10942 -308 -535 1832 C ATOM 2350 CD GLU A 363 -18.433 -27.958 14.081 1.00121.72 C ANISOU 2350 CD GLU A 363 20039 14001 12208 -214 -722 2050 C ATOM 2351 OE1 GLU A 363 -19.015 -28.978 14.507 1.00130.69 O ANISOU 2351 OE1 GLU A 363 21512 14994 13150 -421 -722 2334 O ATOM 2352 OE2 GLU A 363 -17.373 -27.522 14.579 1.00123.69 O ANISOU 2352 OE2 GLU A 363 20188 14385 12425 58 -874 1949 O ATOM 2353 N ILE A 364 -22.459 -27.851 10.302 1.00 81.09 N ANISOU 2353 N ILE A 364 14481 8657 7672 -1127 -99 1866 N ATOM 2354 CA ILE A 364 -22.668 -28.696 9.132 1.00 74.40 C ANISOU 2354 CA ILE A 364 13794 7496 6980 -1206 -150 1886 C ATOM 2355 C ILE A 364 -23.320 -27.910 7.996 1.00 68.10 C ANISOU 2355 C ILE A 364 12656 6846 6373 -1258 -31 1698 C ATOM 2356 O ILE A 364 -22.954 -28.065 6.831 1.00 67.24 O ANISOU 2356 O ILE A 364 12553 6558 6436 -1127 -95 1597 O ATOM 2357 CB ILE A 364 -23.546 -29.919 9.471 1.00 74.60 C ANISOU 2357 CB ILE A 364 14144 7341 6860 -1578 -137 2125 C ATOM 2358 CG1 ILE A 364 -22.976 -30.670 10.675 1.00 75.84 C ANISOU 2358 CG1 ILE A 364 14589 7394 6834 -1513 -245 2330 C ATOM 2359 CG2 ILE A 364 -23.664 -30.846 8.269 1.00 74.46 C ANISOU 2359 CG2 ILE A 364 14325 6957 7010 -1654 -216 2103 C ATOM 2360 CD1 ILE A 364 -23.793 -31.877 11.083 1.00 69.72 C ANISOU 2360 CD1 ILE A 364 13984 6491 6016 -1831 -217 2505 C ATOM 2361 N PHE A 365 -24.279 -27.056 8.346 1.00 64.73 N ANISOU 2361 N PHE A 365 11931 6763 5901 -1428 142 1654 N ATOM 2362 CA PHE A 365 -25.045 -26.300 7.358 1.00 59.69 C ANISOU 2362 CA PHE A 365 10961 6295 5426 -1482 250 1515 C ATOM 2363 C PHE A 365 -24.193 -25.293 6.588 1.00 58.16 C ANISOU 2363 C PHE A 365 10541 6118 5438 -1138 229 1334 C ATOM 2364 O PHE A 365 -24.526 -24.926 5.460 1.00 55.42 O ANISOU 2364 O PHE A 365 10018 5801 5238 -1118 258 1253 O ATOM 2365 CB PHE A 365 -26.211 -25.575 8.034 1.00 58.39 C ANISOU 2365 CB PHE A 365 10511 6502 5171 -1692 444 1507 C ATOM 2366 CG PHE A 365 -27.291 -26.496 8.531 1.00 61.11 C ANISOU 2366 CG PHE A 365 10994 6884 5341 -2099 511 1683 C ATOM 2367 CD1 PHE A 365 -27.421 -27.775 8.015 1.00 59.88 C ANISOU 2367 CD1 PHE A 365 11146 6419 5185 -2298 404 1804 C ATOM 2368 CD2 PHE A 365 -28.178 -26.081 9.512 1.00 61.31 C ANISOU 2368 CD2 PHE A 365 10838 7248 5207 -2293 694 1715 C ATOM 2369 CE1 PHE A 365 -28.412 -28.624 8.469 1.00 63.15 C ANISOU 2369 CE1 PHE A 365 11688 6845 5461 -2715 474 1975 C ATOM 2370 CE2 PHE A 365 -29.172 -26.926 9.969 1.00 63.63 C ANISOU 2370 CE2 PHE A 365 11238 7599 5341 -2698 780 1891 C ATOM 2371 CZ PHE A 365 -29.288 -28.199 9.446 1.00 66.84 C ANISOU 2371 CZ PHE A 365 11953 7676 5765 -2925 668 2032 C ATOM 2372 N VAL A 366 -23.103 -24.845 7.202 1.00 61.92 N ANISOU 2372 N VAL A 366 11018 6592 5917 -882 178 1280 N ATOM 2373 CA VAL A 366 -22.184 -23.919 6.550 1.00 63.15 C ANISOU 2373 CA VAL A 366 10967 6746 6280 -581 166 1122 C ATOM 2374 C VAL A 366 -21.528 -24.580 5.340 1.00 68.06 C ANISOU 2374 C VAL A 366 11734 7108 7017 -443 58 1112 C ATOM 2375 O VAL A 366 -21.401 -23.970 4.276 1.00 73.45 O ANISOU 2375 O VAL A 366 12228 7817 7862 -328 102 1019 O ATOM 2376 CB VAL A 366 -21.094 -23.422 7.526 1.00 60.79 C ANISOU 2376 CB VAL A 366 10645 6500 5954 -368 108 1055 C ATOM 2377 CG1 VAL A 366 -19.956 -22.762 6.773 1.00 56.26 C ANISOU 2377 CG1 VAL A 366 9912 5857 5607 -80 70 917 C ATOM 2378 CG2 VAL A 366 -21.685 -22.457 8.537 1.00 61.89 C ANISOU 2378 CG2 VAL A 366 10573 6931 6012 -457 242 981 C ATOM 2379 N TRP A 367 -21.129 -25.837 5.504 1.00 69.19 N ANISOU 2379 N TRP A 367 12226 6998 7067 -451 -76 1213 N ATOM 2380 CA TRP A 367 -20.468 -26.576 4.435 1.00 68.04 C ANISOU 2380 CA TRP A 367 12252 6585 7016 -299 -177 1175 C ATOM 2381 C TRP A 367 -21.416 -26.875 3.280 1.00 64.70 C ANISOU 2381 C TRP A 367 11824 6136 6623 -493 -133 1148 C ATOM 2382 O TRP A 367 -20.987 -26.977 2.131 1.00 65.71 O ANISOU 2382 O TRP A 367 11952 6169 6845 -348 -160 1049 O ATOM 2383 CB TRP A 367 -19.870 -27.873 4.979 1.00 71.58 C ANISOU 2383 CB TRP A 367 13095 6733 7368 -244 -336 1292 C ATOM 2384 CG TRP A 367 -18.706 -27.633 5.881 1.00 74.58 C ANISOU 2384 CG TRP A 367 13468 7142 7728 25 -428 1299 C ATOM 2385 CD1 TRP A 367 -18.708 -27.644 7.244 1.00 78.15 C ANISOU 2385 CD1 TRP A 367 13993 7696 8004 -29 -466 1416 C ATOM 2386 CD2 TRP A 367 -17.365 -27.326 5.484 1.00 77.09 C ANISOU 2386 CD2 TRP A 367 13673 7427 8190 382 -498 1175 C ATOM 2387 NE1 TRP A 367 -17.449 -27.372 7.722 1.00 80.17 N ANISOU 2387 NE1 TRP A 367 14192 7986 8284 278 -582 1364 N ATOM 2388 CE2 TRP A 367 -16.606 -27.171 6.661 1.00 78.86 C ANISOU 2388 CE2 TRP A 367 13896 7737 8330 528 -599 1215 C ATOM 2389 CE3 TRP A 367 -16.731 -27.171 4.247 1.00 79.33 C ANISOU 2389 CE3 TRP A 367 13845 7646 8650 585 -478 1033 C ATOM 2390 CZ2 TRP A 367 -15.246 -26.870 6.637 1.00 80.37 C ANISOU 2390 CZ2 TRP A 367 13952 7950 8637 861 -694 1109 C ATOM 2391 CZ3 TRP A 367 -15.382 -26.871 4.226 1.00 82.90 C ANISOU 2391 CZ3 TRP A 367 14166 8117 9213 912 -542 940 C ATOM 2392 CH2 TRP A 367 -14.655 -26.724 5.413 1.00 80.53 C ANISOU 2392 CH2 TRP A 367 13842 7901 8855 1042 -654 974 C ATOM 2393 N ILE A 368 -22.702 -27.017 3.587 1.00 61.49 N ANISOU 2393 N ILE A 368 11397 5845 6122 -826 -67 1227 N ATOM 2394 CA ILE A 368 -23.715 -27.190 2.553 1.00 58.21 C ANISOU 2394 CA ILE A 368 10912 5479 5727 -1040 -37 1188 C ATOM 2395 C ILE A 368 -23.760 -25.941 1.681 1.00 52.41 C ANISOU 2395 C ILE A 368 9812 4984 5116 -881 47 1079 C ATOM 2396 O ILE A 368 -23.881 -26.024 0.459 1.00 49.90 O ANISOU 2396 O ILE A 368 9466 4657 4838 -858 21 1007 O ATOM 2397 CB ILE A 368 -25.107 -27.460 3.153 1.00 57.87 C ANISOU 2397 CB ILE A 368 10839 5578 5571 -1438 34 1294 C ATOM 2398 CG1 ILE A 368 -25.076 -28.718 4.024 1.00 56.76 C ANISOU 2398 CG1 ILE A 368 11091 5174 5303 -1624 -37 1449 C ATOM 2399 CG2 ILE A 368 -26.151 -27.598 2.053 1.00 57.89 C ANISOU 2399 CG2 ILE A 368 10720 5675 5601 -1659 38 1235 C ATOM 2400 CD1 ILE A 368 -26.407 -29.055 4.657 1.00 58.92 C ANISOU 2400 CD1 ILE A 368 11342 5588 5456 -2053 56 1575 C ATOM 2401 N GLY A 369 -23.649 -24.783 2.321 1.00 50.26 N ANISOU 2401 N GLY A 369 9280 4921 4897 -769 147 1066 N ATOM 2402 CA GLY A 369 -23.569 -23.525 1.605 1.00 49.34 C ANISOU 2402 CA GLY A 369 8842 4978 4926 -591 233 990 C ATOM 2403 C GLY A 369 -22.240 -23.394 0.888 1.00 51.09 C ANISOU 2403 C GLY A 369 9103 5057 5253 -293 189 920 C ATOM 2404 O GLY A 369 -22.156 -22.789 -0.181 1.00 49.55 O ANISOU 2404 O GLY A 369 8746 4933 5147 -178 233 884 O ATOM 2405 N TYR A 370 -21.196 -23.967 1.481 1.00 57.33 N ANISOU 2405 N TYR A 370 10098 5663 6021 -163 104 914 N ATOM 2406 CA TYR A 370 -19.870 -23.958 0.874 1.00 62.37 C ANISOU 2406 CA TYR A 370 10759 6180 6758 125 64 839 C ATOM 2407 C TYR A 370 -19.847 -24.789 -0.405 1.00 73.56 C ANISOU 2407 C TYR A 370 12343 7463 8145 143 15 799 C ATOM 2408 O TYR A 370 -19.193 -24.420 -1.380 1.00 79.00 O ANISOU 2408 O TYR A 370 12930 8176 8911 335 55 730 O ATOM 2409 CB TYR A 370 -18.821 -24.475 1.861 1.00 59.92 C ANISOU 2409 CB TYR A 370 10619 5727 6422 271 -42 846 C ATOM 2410 CG TYR A 370 -18.366 -23.440 2.866 1.00 60.47 C ANISOU 2410 CG TYR A 370 10473 5954 6549 353 -2 813 C ATOM 2411 CD1 TYR A 370 -18.796 -22.122 2.777 1.00 57.87 C ANISOU 2411 CD1 TYR A 370 9833 5824 6329 322 137 765 C ATOM 2412 CD2 TYR A 370 -17.499 -23.778 3.897 1.00 60.64 C ANISOU 2412 CD2 TYR A 370 10605 5920 6516 473 -116 821 C ATOM 2413 CE1 TYR A 370 -18.383 -21.172 3.691 1.00 57.07 C ANISOU 2413 CE1 TYR A 370 9550 5841 6292 385 172 694 C ATOM 2414 CE2 TYR A 370 -17.078 -22.834 4.814 1.00 59.91 C ANISOU 2414 CE2 TYR A 370 10313 5991 6458 532 -97 754 C ATOM 2415 CZ TYR A 370 -17.522 -21.533 4.706 1.00 58.82 C ANISOU 2415 CZ TYR A 370 9880 6029 6440 478 52 674 C ATOM 2416 OH TYR A 370 -17.108 -20.591 5.619 1.00 58.66 O ANISOU 2416 OH TYR A 370 9676 6146 6465 524 70 568 O ATOM 2417 N VAL A 371 -20.559 -25.912 -0.391 1.00 77.83 N ANISOU 2417 N VAL A 371 13143 7862 8566 -72 -65 834 N ATOM 2418 CA VAL A 371 -20.738 -26.720 -1.590 1.00 78.90 C ANISOU 2418 CA VAL A 371 13447 7876 8655 -108 -118 758 C ATOM 2419 C VAL A 371 -21.490 -25.909 -2.635 1.00 81.24 C ANISOU 2419 C VAL A 371 13481 8434 8952 -173 -38 732 C ATOM 2420 O VAL A 371 -21.136 -25.905 -3.814 1.00 86.03 O ANISOU 2420 O VAL A 371 14080 9060 9549 -41 -33 646 O ATOM 2421 CB VAL A 371 -21.512 -28.021 -1.297 1.00 76.97 C ANISOU 2421 CB VAL A 371 13522 7419 8303 -395 -216 798 C ATOM 2422 CG1 VAL A 371 -21.847 -28.748 -2.589 1.00 75.39 C ANISOU 2422 CG1 VAL A 371 13467 7125 8054 -475 -272 674 C ATOM 2423 CG2 VAL A 371 -20.715 -28.918 -0.370 1.00 77.25 C ANISOU 2423 CG2 VAL A 371 13867 7155 8332 -295 -312 857 C ATOM 2424 N SER A 372 -22.525 -25.211 -2.178 1.00 80.56 N ANISOU 2424 N SER A 372 13175 8567 8867 -360 26 811 N ATOM 2425 CA SER A 372 -23.359 -24.390 -3.045 1.00 83.77 C ANISOU 2425 CA SER A 372 13310 9239 9279 -410 85 821 C ATOM 2426 C SER A 372 -22.567 -23.269 -3.709 1.00 88.67 C ANISOU 2426 C SER A 372 13717 9963 10010 -123 176 815 C ATOM 2427 O SER A 372 -22.629 -23.095 -4.925 1.00 89.95 O ANISOU 2427 O SER A 372 13822 10224 10131 -58 180 797 O ATOM 2428 CB SER A 372 -24.525 -23.802 -2.249 1.00 81.12 C ANISOU 2428 CB SER A 372 12754 9115 8954 -613 149 903 C ATOM 2429 OG SER A 372 -25.331 -22.970 -3.063 1.00 79.44 O ANISOU 2429 OG SER A 372 12257 9162 8765 -619 192 927 O ATOM 2430 N SER A 373 -21.825 -22.514 -2.907 1.00 94.66 N ANISOU 2430 N SER A 373 14363 10705 10899 32 248 831 N ATOM 2431 CA SER A 373 -21.045 -21.393 -3.419 1.00 95.61 C ANISOU 2431 CA SER A 373 14273 10896 11160 265 351 837 C ATOM 2432 C SER A 373 -19.900 -21.869 -4.307 1.00 90.94 C ANISOU 2432 C SER A 373 13808 10195 10549 460 337 768 C ATOM 2433 O SER A 373 -19.532 -21.199 -5.270 1.00 92.87 O ANISOU 2433 O SER A 373 13914 10538 10835 596 423 791 O ATOM 2434 CB SER A 373 -20.496 -20.550 -2.265 1.00 96.68 C ANISOU 2434 CB SER A 373 14269 11020 11446 348 416 831 C ATOM 2435 OG SER A 373 -19.573 -21.291 -1.486 1.00102.04 O ANISOU 2435 OG SER A 373 15135 11534 12101 412 335 774 O ATOM 2436 N GLY A 374 -19.347 -23.032 -3.981 1.00 87.32 N ANISOU 2436 N GLY A 374 13617 9536 10026 482 237 694 N ATOM 2437 CA GLY A 374 -18.214 -23.569 -4.710 1.00 85.70 C ANISOU 2437 CA GLY A 374 13530 9221 9811 699 227 600 C ATOM 2438 C GLY A 374 -18.530 -23.982 -6.135 1.00 84.32 C ANISOU 2438 C GLY A 374 13436 9105 9496 691 227 543 C ATOM 2439 O GLY A 374 -17.774 -23.679 -7.058 1.00 83.05 O ANISOU 2439 O GLY A 374 13200 9020 9336 881 313 504 O ATOM 2440 N VAL A 375 -19.651 -24.672 -6.318 1.00 83.18 N ANISOU 2440 N VAL A 375 13437 8950 9219 456 134 531 N ATOM 2441 CA VAL A 375 -20.014 -25.196 -7.630 1.00 81.67 C ANISOU 2441 CA VAL A 375 13350 8821 8860 418 98 437 C ATOM 2442 C VAL A 375 -21.001 -24.292 -8.364 1.00 80.25 C ANISOU 2442 C VAL A 375 12927 8950 8615 316 137 534 C ATOM 2443 O VAL A 375 -21.465 -24.626 -9.454 1.00 79.50 O ANISOU 2443 O VAL A 375 12887 8974 8347 258 87 468 O ATOM 2444 CB VAL A 375 -20.626 -26.608 -7.520 1.00 79.10 C ANISOU 2444 CB VAL A 375 13347 8280 8426 200 -52 333 C ATOM 2445 CG1 VAL A 375 -19.692 -27.530 -6.752 1.00 78.01 C ANISOU 2445 CG1 VAL A 375 13476 7803 8361 325 -107 274 C ATOM 2446 CG2 VAL A 375 -21.991 -26.547 -6.851 1.00 76.09 C ANISOU 2446 CG2 VAL A 375 12895 7982 8034 -130 -101 435 C ATOM 2447 N ASN A 376 -21.314 -23.145 -7.769 1.00 82.06 N ANISOU 2447 N ASN A 376 12890 9311 8980 310 217 681 N ATOM 2448 CA ASN A 376 -22.303 -22.235 -8.343 1.00 86.33 C ANISOU 2448 CA ASN A 376 13185 10125 9491 245 244 800 C ATOM 2449 C ASN A 376 -21.912 -21.655 -9.711 1.00 88.66 C ANISOU 2449 C ASN A 376 13390 10597 9700 425 315 846 C ATOM 2450 O ASN A 376 -22.720 -21.691 -10.639 1.00100.90 O ANISOU 2450 O ASN A 376 14906 12353 11079 348 249 866 O ATOM 2451 CB ASN A 376 -22.608 -21.096 -7.363 1.00 87.69 C ANISOU 2451 CB ASN A 376 13105 10354 9859 248 332 927 C ATOM 2452 CG ASN A 376 -23.563 -20.073 -7.941 1.00 92.43 C ANISOU 2452 CG ASN A 376 13440 11212 10469 243 365 1065 C ATOM 2453 OD1 ASN A 376 -23.170 -18.951 -8.261 1.00 89.62 O ANISOU 2453 OD1 ASN A 376 12909 10912 10232 421 478 1177 O ATOM 2454 ND2 ASN A 376 -24.825 -20.459 -8.091 1.00100.16 N ANISOU 2454 ND2 ASN A 376 14381 12343 11331 38 261 1066 N ATOM 2455 N PRO A 377 -20.683 -21.115 -9.852 1.00 79.98 N ANISOU 2455 N PRO A 377 12240 9445 8704 653 447 869 N ATOM 2456 CA PRO A 377 -20.365 -20.597 -11.188 1.00 76.09 C ANISOU 2456 CA PRO A 377 11673 9143 8094 797 534 940 C ATOM 2457 C PRO A 377 -20.159 -21.709 -12.213 1.00 72.60 C ANISOU 2457 C PRO A 377 11466 8733 7388 813 467 767 C ATOM 2458 O PRO A 377 -20.496 -21.532 -13.383 1.00 73.66 O ANISOU 2458 O PRO A 377 11574 9102 7313 834 467 808 O ATOM 2459 CB PRO A 377 -19.060 -19.819 -10.966 1.00 75.66 C ANISOU 2459 CB PRO A 377 11498 9010 8239 996 707 995 C ATOM 2460 CG PRO A 377 -18.983 -19.591 -9.491 1.00 74.85 C ANISOU 2460 CG PRO A 377 11337 8731 8373 943 695 984 C ATOM 2461 CD PRO A 377 -19.615 -20.800 -8.888 1.00 76.29 C ANISOU 2461 CD PRO A 377 11734 8800 8452 775 531 857 C ATOM 2462 N LEU A 378 -19.615 -22.839 -11.771 1.00 67.75 N ANISOU 2462 N LEU A 378 11087 7879 6775 815 406 572 N ATOM 2463 CA LEU A 378 -19.337 -23.962 -12.659 1.00 62.99 C ANISOU 2463 CA LEU A 378 10738 7244 5952 852 349 358 C ATOM 2464 C LEU A 378 -20.610 -24.513 -13.296 1.00 61.10 C ANISOU 2464 C LEU A 378 10593 7136 5486 622 190 289 C ATOM 2465 O LEU A 378 -20.720 -24.572 -14.520 1.00 62.25 O ANISOU 2465 O LEU A 378 10765 7499 5387 661 185 231 O ATOM 2466 CB LEU A 378 -18.612 -25.076 -11.901 1.00 61.47 C ANISOU 2466 CB LEU A 378 10791 6710 5852 905 293 181 C ATOM 2467 CG LEU A 378 -18.296 -26.338 -12.707 1.00 62.19 C ANISOU 2467 CG LEU A 378 11183 6688 5758 964 231 -83 C ATOM 2468 CD1 LEU A 378 -17.348 -26.025 -13.856 1.00 62.45 C ANISOU 2468 CD1 LEU A 378 11149 6917 5662 1223 391 -144 C ATOM 2469 CD2 LEU A 378 -17.716 -27.419 -11.808 1.00 61.71 C ANISOU 2469 CD2 LEU A 378 11377 6240 5831 1018 152 -215 C ATOM 2470 N VAL A 379 -21.562 -24.912 -12.457 1.00 58.64 N ANISOU 2470 N VAL A 379 10319 6717 5243 371 61 293 N ATOM 2471 CA VAL A 379 -22.827 -25.480 -12.918 1.00 58.35 C ANISOU 2471 CA VAL A 379 10341 6803 5028 100 -105 216 C ATOM 2472 C VAL A 379 -23.562 -24.535 -13.867 1.00 58.08 C ANISOU 2472 C VAL A 379 10052 7174 4843 103 -109 359 C ATOM 2473 O VAL A 379 -24.070 -24.955 -14.907 1.00 57.76 O ANISOU 2473 O VAL A 379 10076 7326 4545 21 -219 245 O ATOM 2474 CB VAL A 379 -23.749 -25.827 -11.728 1.00 56.24 C ANISOU 2474 CB VAL A 379 10074 6400 4895 -185 -196 257 C ATOM 2475 CG1 VAL A 379 -25.152 -26.167 -12.209 1.00 57.42 C ANISOU 2475 CG1 VAL A 379 10173 6754 4888 -489 -353 210 C ATOM 2476 CG2 VAL A 379 -23.163 -26.976 -10.919 1.00 56.17 C ANISOU 2476 CG2 VAL A 379 10383 5983 4977 -221 -234 124 C ATOM 2477 N TYR A 380 -23.600 -23.256 -13.508 1.00 56.78 N ANISOU 2477 N TYR A 380 9606 7131 4837 210 1 604 N ATOM 2478 CA TYR A 380 -24.267 -22.244 -14.321 1.00 58.23 C ANISOU 2478 CA TYR A 380 9541 7666 4916 259 1 796 C ATOM 2479 C TYR A 380 -23.628 -22.113 -15.701 1.00 63.32 C ANISOU 2479 C TYR A 380 10244 8502 5311 448 59 790 C ATOM 2480 O TYR A 380 -24.311 -21.835 -16.687 1.00 66.60 O ANISOU 2480 O TYR A 380 10573 9239 5494 435 -24 863 O ATOM 2481 CB TYR A 380 -24.248 -20.893 -13.601 1.00 55.63 C ANISOU 2481 CB TYR A 380 8940 7340 4856 374 133 1048 C ATOM 2482 CG TYR A 380 -24.855 -19.755 -14.392 1.00 57.55 C ANISOU 2482 CG TYR A 380 8937 7892 5038 475 144 1289 C ATOM 2483 CD1 TYR A 380 -26.232 -19.600 -14.481 1.00 54.19 C ANISOU 2483 CD1 TYR A 380 8336 7702 4554 337 -3 1356 C ATOM 2484 CD2 TYR A 380 -24.049 -18.827 -15.040 1.00 59.64 C ANISOU 2484 CD2 TYR A 380 9134 8214 5311 712 303 1468 C ATOM 2485 CE1 TYR A 380 -26.790 -18.558 -15.200 1.00 64.96 C ANISOU 2485 CE1 TYR A 380 9472 9344 5865 470 -12 1599 C ATOM 2486 CE2 TYR A 380 -24.597 -17.783 -15.760 1.00 62.00 C ANISOU 2486 CE2 TYR A 380 9236 8765 5556 819 309 1730 C ATOM 2487 CZ TYR A 380 -25.967 -17.653 -15.837 1.00 64.54 C ANISOU 2487 CZ TYR A 380 9395 9310 5817 716 141 1797 C ATOM 2488 OH TYR A 380 -26.515 -16.613 -16.554 1.00 67.70 O ANISOU 2488 OH TYR A 380 9597 9958 6167 862 128 2079 O ATOM 2489 N THR A 381 -22.316 -22.322 -15.766 1.00 65.90 N ANISOU 2489 N THR A 381 10708 8660 5671 630 201 705 N ATOM 2490 CA THR A 381 -21.583 -22.190 -17.020 1.00 69.05 C ANISOU 2490 CA THR A 381 11154 9251 5829 821 305 696 C ATOM 2491 C THR A 381 -21.514 -23.504 -17.797 1.00 72.94 C ANISOU 2491 C THR A 381 11931 9753 6028 772 200 373 C ATOM 2492 O THR A 381 -20.985 -23.546 -18.906 1.00 75.67 O ANISOU 2492 O THR A 381 12342 10297 6111 917 278 313 O ATOM 2493 CB THR A 381 -20.149 -21.681 -16.779 1.00 67.77 C ANISOU 2493 CB THR A 381 10945 8952 5853 1052 541 761 C ATOM 2494 OG1 THR A 381 -19.514 -22.490 -15.780 1.00 66.81 O ANISOU 2494 OG1 THR A 381 10969 8488 5927 1051 530 569 O ATOM 2495 CG2 THR A 381 -20.170 -20.233 -16.316 1.00 65.62 C ANISOU 2495 CG2 THR A 381 10394 8707 5833 1110 663 1078 C ATOM 2496 N LEU A 382 -22.049 -24.573 -17.217 1.00 73.59 N ANISOU 2496 N LEU A 382 12192 9615 6153 561 33 160 N ATOM 2497 CA LEU A 382 -22.063 -25.868 -17.890 1.00 72.06 C ANISOU 2497 CA LEU A 382 12297 9365 5719 486 -83 -179 C ATOM 2498 C LEU A 382 -23.147 -25.923 -18.962 1.00 75.54 C ANISOU 2498 C LEU A 382 12704 10175 5822 327 -252 -226 C ATOM 2499 O LEU A 382 -23.154 -26.821 -19.803 1.00 81.19 O ANISOU 2499 O LEU A 382 13644 10937 6266 284 -341 -518 O ATOM 2500 CB LEU A 382 -22.266 -27.001 -16.882 1.00 70.95 C ANISOU 2500 CB LEU A 382 12382 8814 5761 292 -204 -367 C ATOM 2501 CG LEU A 382 -21.070 -27.368 -16.001 1.00 67.92 C ANISOU 2501 CG LEU A 382 12132 8046 5627 476 -88 -417 C ATOM 2502 CD1 LEU A 382 -21.437 -28.485 -15.037 1.00 68.55 C ANISOU 2502 CD1 LEU A 382 12456 7732 5857 260 -230 -549 C ATOM 2503 CD2 LEU A 382 -19.873 -27.761 -16.852 1.00 68.65 C ANISOU 2503 CD2 LEU A 382 12375 8129 5580 763 33 -618 C ATOM 2504 N PHE A 383 -24.060 -24.957 -18.927 1.00 75.92 N ANISOU 2504 N PHE A 383 12466 10491 5888 252 -305 48 N ATOM 2505 CA PHE A 383 -25.155 -24.908 -19.888 1.00 80.02 C ANISOU 2505 CA PHE A 383 12897 11411 6096 114 -494 41 C ATOM 2506 C PHE A 383 -24.810 -24.020 -21.080 1.00 79.25 C ANISOU 2506 C PHE A 383 12692 11702 5716 357 -398 229 C ATOM 2507 O PHE A 383 -25.546 -23.974 -22.066 1.00 83.04 O ANISOU 2507 O PHE A 383 13123 12568 5862 300 -554 224 O ATOM 2508 CB PHE A 383 -26.436 -24.420 -19.211 1.00 80.48 C ANISOU 2508 CB PHE A 383 12685 11573 6320 -91 -626 229 C ATOM 2509 CG PHE A 383 -26.941 -25.344 -18.140 1.00 80.40 C ANISOU 2509 CG PHE A 383 12777 11248 6522 -386 -727 58 C ATOM 2510 CD1 PHE A 383 -27.804 -26.382 -18.452 1.00 84.08 C ANISOU 2510 CD1 PHE A 383 13361 11757 6828 -699 -948 -202 C ATOM 2511 CD2 PHE A 383 -26.546 -25.181 -16.823 1.00 77.92 C ANISOU 2511 CD2 PHE A 383 12448 10600 6557 -366 -599 160 C ATOM 2512 CE1 PHE A 383 -28.267 -27.237 -17.469 1.00 86.09 C ANISOU 2512 CE1 PHE A 383 13722 11705 7283 -999 -1022 -327 C ATOM 2513 CE2 PHE A 383 -27.005 -26.032 -15.836 1.00 78.09 C ANISOU 2513 CE2 PHE A 383 12581 10346 6743 -642 -678 40 C ATOM 2514 CZ PHE A 383 -27.867 -27.061 -16.160 1.00 83.02 C ANISOU 2514 CZ PHE A 383 13329 10994 7222 -964 -880 -188 C ATOM 2515 N ASN A 384 -23.686 -23.317 -20.982 1.00 76.11 N ANISOU 2515 N ASN A 384 12254 11215 5448 617 -145 403 N ATOM 2516 CA ASN A 384 -23.178 -22.529 -22.098 1.00 78.88 C ANISOU 2516 CA ASN A 384 12540 11896 5537 843 -4 595 C ATOM 2517 C ASN A 384 -22.187 -23.348 -22.917 1.00 81.47 C ANISOU 2517 C ASN A 384 13126 12243 5587 965 100 299 C ATOM 2518 O ASN A 384 -21.239 -23.911 -22.371 1.00 79.70 O ANISOU 2518 O ASN A 384 13040 11688 5556 1041 224 113 O ATOM 2519 CB ASN A 384 -22.521 -21.242 -21.597 1.00 77.72 C ANISOU 2519 CB ASN A 384 12184 11655 5691 1028 233 959 C ATOM 2520 CG ASN A 384 -22.055 -20.346 -22.729 1.00 82.20 C ANISOU 2520 CG ASN A 384 12677 12551 6004 1232 394 1224 C ATOM 2521 OD1 ASN A 384 -20.929 -20.468 -23.210 1.00 85.83 O ANISOU 2521 OD1 ASN A 384 13237 13021 6354 1383 601 1156 O ATOM 2522 ND2 ASN A 384 -22.923 -19.439 -23.161 1.00 83.53 N ANISOU 2522 ND2 ASN A 384 12663 13000 6076 1244 306 1543 N ATOM 2523 N LYS A 385 -22.412 -23.413 -24.226 1.00 84.81 N ANISOU 2523 N LYS A 385 13605 13072 5545 1000 44 251 N ATOM 2524 CA LYS A 385 -21.602 -24.248 -25.109 1.00 87.42 C ANISOU 2524 CA LYS A 385 14188 13479 5550 1112 132 -82 C ATOM 2525 C LYS A 385 -20.135 -23.827 -25.128 1.00 88.10 C ANISOU 2525 C LYS A 385 14253 13482 5740 1383 474 11 C ATOM 2526 O LYS A 385 -19.242 -24.669 -25.031 1.00 78.21 O ANISOU 2526 O LYS A 385 13182 12007 4526 1481 579 -304 O ATOM 2527 CB LYS A 385 -22.168 -24.218 -26.531 1.00 90.22 C ANISOU 2527 CB LYS A 385 14576 14363 5340 1104 12 -109 C ATOM 2528 N THR A 386 -19.891 -22.526 -25.251 1.00 76.84 N ANISOU 2528 N THR A 386 12596 12225 4376 1503 647 444 N ATOM 2529 CA THR A 386 -18.529 -22.006 -25.324 1.00 80.03 C ANISOU 2529 CA THR A 386 12931 12596 4880 1723 985 570 C ATOM 2530 C THR A 386 -17.778 -22.235 -24.015 1.00 75.70 C ANISOU 2530 C THR A 386 12357 11570 4834 1749 1073 473 C ATOM 2531 O THR A 386 -16.606 -22.613 -24.019 1.00 73.40 O ANISOU 2531 O THR A 386 12118 11176 4593 1910 1270 299 O ATOM 2532 CB THR A 386 -18.517 -20.503 -25.661 1.00 79.98 C ANISOU 2532 CB THR A 386 12687 12818 4884 1801 1140 1091 C ATOM 2533 OG1 THR A 386 -19.400 -20.249 -26.761 1.00 83.43 O ANISOU 2533 OG1 THR A 386 13136 13698 4864 1774 998 1234 O ATOM 2534 CG2 THR A 386 -17.112 -20.050 -26.027 1.00 77.44 C ANISOU 2534 CG2 THR A 386 12305 12552 4565 1992 1505 1197 C ATOM 2535 N PHE A 387 -18.460 -21.999 -22.899 1.00 73.86 N ANISOU 2535 N PHE A 387 12029 11078 4955 1601 925 585 N ATOM 2536 CA PHE A 387 -17.900 -22.260 -21.577 1.00 71.71 C ANISOU 2536 CA PHE A 387 11747 10375 5125 1602 959 494 C ATOM 2537 C PHE A 387 -17.587 -23.742 -21.397 1.00 72.92 C ANISOU 2537 C PHE A 387 12177 10288 5241 1601 867 55 C ATOM 2538 O PHE A 387 -16.521 -24.110 -20.904 1.00 66.88 O ANISOU 2538 O PHE A 387 11449 9288 4676 1748 993 -81 O ATOM 2539 CB PHE A 387 -18.870 -21.800 -20.485 1.00 70.39 C ANISOU 2539 CB PHE A 387 11448 10033 5264 1423 801 671 C ATOM 2540 CG PHE A 387 -18.551 -20.449 -19.911 1.00 71.19 C ANISOU 2540 CG PHE A 387 11287 10078 5682 1488 963 1022 C ATOM 2541 CD1 PHE A 387 -17.276 -20.156 -19.457 1.00 71.94 C ANISOU 2541 CD1 PHE A 387 11308 10003 6023 1627 1181 1036 C ATOM 2542 CD2 PHE A 387 -19.529 -19.473 -19.819 1.00 71.17 C ANISOU 2542 CD2 PHE A 387 11104 10188 5747 1413 892 1320 C ATOM 2543 CE1 PHE A 387 -16.982 -18.914 -18.926 1.00 69.20 C ANISOU 2543 CE1 PHE A 387 10728 9582 5983 1655 1323 1327 C ATOM 2544 CE2 PHE A 387 -19.242 -18.229 -19.289 1.00 70.20 C ANISOU 2544 CE2 PHE A 387 10766 9967 5939 1474 1043 1616 C ATOM 2545 CZ PHE A 387 -17.966 -17.949 -18.842 1.00 67.83 C ANISOU 2545 CZ PHE A 387 10411 9479 5882 1578 1258 1612 C ATOM 2546 N ARG A 388 -18.530 -24.584 -21.807 1.00 75.94 N ANISOU 2546 N ARG A 388 12748 10727 5380 1436 638 -166 N ATOM 2547 CA ARG A 388 -18.415 -26.028 -21.643 1.00 77.32 C ANISOU 2547 CA ARG A 388 13223 10619 5535 1395 519 -585 C ATOM 2548 C ARG A 388 -17.324 -26.619 -22.533 1.00 79.56 C ANISOU 2548 C ARG A 388 13665 10980 5584 1641 688 -865 C ATOM 2549 O ARG A 388 -16.595 -27.519 -22.116 1.00 77.58 O ANISOU 2549 O ARG A 388 13590 10402 5483 1757 715 -1136 O ATOM 2550 CB ARG A 388 -19.760 -26.693 -21.938 1.00 80.30 C ANISOU 2550 CB ARG A 388 13739 11063 5707 1112 233 -749 C ATOM 2551 CG ARG A 388 -19.807 -28.187 -21.689 1.00 85.13 C ANISOU 2551 CG ARG A 388 14686 11314 6345 1007 86 -1167 C ATOM 2552 CD ARG A 388 -21.243 -28.682 -21.754 1.00 89.61 C ANISOU 2552 CD ARG A 388 15323 11926 6800 651 -201 -1269 C ATOM 2553 NE ARG A 388 -21.918 -28.218 -22.963 1.00 93.48 N ANISOU 2553 NE ARG A 388 15706 12933 6878 602 -279 -1225 N ATOM 2554 CZ ARG A 388 -23.236 -28.212 -23.128 1.00 95.55 C ANISOU 2554 CZ ARG A 388 15884 13401 7021 318 -521 -1201 C ATOM 2555 NH1 ARG A 388 -24.031 -28.641 -22.156 1.00 94.75 N ANISOU 2555 NH1 ARG A 388 15786 13029 7187 35 -681 -1217 N ATOM 2556 NH2 ARG A 388 -23.762 -27.771 -24.263 1.00 98.52 N ANISOU 2556 NH2 ARG A 388 16158 14280 6996 316 -602 -1149 N ATOM 2557 N ASP A 389 -17.216 -26.111 -23.757 1.00 83.63 N ANISOU 2557 N ASP A 389 14116 11937 5721 1736 806 -793 N ATOM 2558 CA ASP A 389 -16.171 -26.557 -24.671 1.00 90.86 C ANISOU 2558 CA ASP A 389 15145 13005 6373 1981 1010 -1046 C ATOM 2559 C ASP A 389 -14.800 -26.112 -24.175 1.00 87.39 C ANISOU 2559 C ASP A 389 14533 12443 6230 2224 1296 -930 C ATOM 2560 O ASP A 389 -13.801 -26.803 -24.379 1.00 90.43 O ANISOU 2560 O ASP A 389 15020 12748 6593 2445 1438 -1220 O ATOM 2561 CB ASP A 389 -16.419 -26.026 -26.085 1.00 98.87 C ANISOU 2561 CB ASP A 389 16118 14575 6873 2010 1080 -945 C ATOM 2562 CG ASP A 389 -17.633 -26.656 -26.741 1.00106.63 C ANISOU 2562 CG ASP A 389 17287 15732 7495 1798 786 -1163 C ATOM 2563 OD1 ASP A 389 -18.044 -27.751 -26.304 1.00112.64 O ANISOU 2563 OD1 ASP A 389 18271 16165 8362 1658 580 -1506 O ATOM 2564 OD2 ASP A 389 -18.171 -26.060 -27.697 1.00109.21 O ANISOU 2564 OD2 ASP A 389 17539 16525 7431 1764 756 -985 O ATOM 2565 N ALA A 390 -14.761 -24.956 -23.522 1.00 82.70 N ANISOU 2565 N ALA A 390 13664 11837 5922 2185 1374 -524 N ATOM 2566 CA ALA A 390 -13.522 -24.431 -22.966 1.00 81.33 C ANISOU 2566 CA ALA A 390 13283 11555 6064 2365 1621 -399 C ATOM 2567 C ALA A 390 -13.046 -25.293 -21.804 1.00 79.48 C ANISOU 2567 C ALA A 390 13146 10862 6191 2425 1531 -631 C ATOM 2568 O ALA A 390 -11.858 -25.595 -21.692 1.00 82.05 O ANISOU 2568 O ALA A 390 13429 11111 6635 2656 1698 -779 O ATOM 2569 CB ALA A 390 -13.707 -22.989 -22.518 1.00 81.13 C ANISOU 2569 CB ALA A 390 12966 11589 6271 2272 1697 65 C ATOM 2570 N PHE A 391 -13.981 -25.688 -20.945 1.00 75.78 N ANISOU 2570 N PHE A 391 12798 10109 5888 2221 1267 -649 N ATOM 2571 CA PHE A 391 -13.662 -26.520 -19.789 1.00 74.46 C ANISOU 2571 CA PHE A 391 12757 9496 6039 2253 1153 -821 C ATOM 2572 C PHE A 391 -13.107 -27.873 -20.220 1.00 81.20 C ANISOU 2572 C PHE A 391 13897 10191 6763 2435 1141 -1246 C ATOM 2573 O PHE A 391 -12.228 -28.430 -19.565 1.00 81.40 O ANISOU 2573 O PHE A 391 13966 9934 7027 2629 1167 -1383 O ATOM 2574 CB PHE A 391 -14.900 -26.728 -18.909 1.00 69.53 C ANISOU 2574 CB PHE A 391 12228 8640 5549 1962 887 -750 C ATOM 2575 CG PHE A 391 -15.435 -25.465 -18.295 1.00 64.79 C ANISOU 2575 CG PHE A 391 11353 8133 5134 1816 893 -371 C ATOM 2576 CD1 PHE A 391 -14.639 -24.337 -18.184 1.00 63.53 C ANISOU 2576 CD1 PHE A 391 10909 8099 5132 1946 1108 -131 C ATOM 2577 CD2 PHE A 391 -16.736 -25.409 -17.822 1.00 61.69 C ANISOU 2577 CD2 PHE A 391 10977 7693 4771 1544 692 -271 C ATOM 2578 CE1 PHE A 391 -15.133 -23.178 -17.619 1.00 60.51 C ANISOU 2578 CE1 PHE A 391 10296 7757 4940 1821 1115 187 C ATOM 2579 CE2 PHE A 391 -17.234 -24.252 -17.255 1.00 59.11 C ANISOU 2579 CE2 PHE A 391 10396 7443 4622 1443 707 48 C ATOM 2580 CZ PHE A 391 -16.431 -23.136 -17.153 1.00 57.88 C ANISOU 2580 CZ PHE A 391 9990 7374 4629 1589 916 270 C ATOM 2581 N GLY A 392 -13.625 -28.392 -21.328 1.00 89.28 N ANISOU 2581 N GLY A 392 15117 11402 7405 2385 1091 -1464 N ATOM 2582 CA GLY A 392 -13.232 -29.699 -21.820 1.00 97.72 C ANISOU 2582 CA GLY A 392 16494 12306 8330 2541 1067 -1914 C ATOM 2583 C GLY A 392 -11.775 -29.793 -22.234 1.00102.73 C ANISOU 2583 C GLY A 392 17042 13038 8955 2920 1342 -2067 C ATOM 2584 O GLY A 392 -11.167 -30.859 -22.142 1.00106.60 O ANISOU 2584 O GLY A 392 17741 13245 9518 3132 1333 -2408 O ATOM 2585 N ARG A 393 -11.212 -28.679 -22.690 1.00103.18 N ANISOU 2585 N ARG A 393 16782 13487 8934 3010 1595 -1811 N ATOM 2586 CA ARG A 393 -9.827 -28.665 -23.149 1.00111.37 C ANISOU 2586 CA ARG A 393 17673 14696 9947 3346 1894 -1934 C ATOM 2587 C ARG A 393 -8.879 -28.128 -22.081 1.00108.23 C ANISOU 2587 C ARG A 393 16983 14145 9995 3471 1997 -1730 C ATOM 2588 O ARG A 393 -7.661 -28.241 -22.210 1.00111.45 O ANISOU 2588 O ARG A 393 17239 14629 10478 3760 2214 -1855 O ATOM 2589 CB ARG A 393 -9.693 -27.840 -24.432 1.00116.99 C ANISOU 2589 CB ARG A 393 18223 15970 10257 3363 2145 -1796 C ATOM 2590 CG ARG A 393 -10.072 -26.377 -24.283 1.00117.08 C ANISOU 2590 CG ARG A 393 17947 16200 10340 3163 2205 -1282 C ATOM 2591 CD ARG A 393 -9.860 -25.625 -25.588 1.00121.69 C ANISOU 2591 CD ARG A 393 18403 17323 10510 3202 2468 -1120 C ATOM 2592 NE ARG A 393 -10.232 -24.217 -25.480 1.00122.69 N ANISOU 2592 NE ARG A 393 18283 17612 10722 3024 2525 -608 N ATOM 2593 CZ ARG A 393 -11.436 -23.738 -25.774 1.00124.54 C ANISOU 2593 CZ ARG A 393 18573 17979 10770 2810 2349 -381 C ATOM 2594 NH1 ARG A 393 -12.392 -24.555 -26.197 1.00128.86 N ANISOU 2594 NH1 ARG A 393 19392 18547 11022 2714 2098 -629 N ATOM 2595 NH2 ARG A 393 -11.686 -22.442 -25.647 1.00124.42 N ANISOU 2595 NH2 ARG A 393 18332 18067 10875 2695 2417 86 N ATOM 2596 N TYR A 394 -9.438 -27.544 -21.026 1.00105.63 N ANISOU 2596 N TYR A 394 16556 13625 9954 3254 1841 -1436 N ATOM 2597 CA TYR A 394 -8.624 -27.039 -19.927 1.00103.48 C ANISOU 2597 CA TYR A 394 16019 13202 10096 3339 1896 -1265 C ATOM 2598 C TYR A 394 -8.288 -28.164 -18.953 1.00104.42 C ANISOU 2598 C TYR A 394 16328 12874 10471 3487 1711 -1498 C ATOM 2599 O TYR A 394 -7.265 -28.122 -18.271 1.00109.69 O ANISOU 2599 O TYR A 394 16808 13450 11417 3691 1773 -1495 O ATOM 2600 CB TYR A 394 -9.336 -25.896 -19.201 1.00 96.24 C ANISOU 2600 CB TYR A 394 14919 12282 9366 3060 1820 -873 C ATOM 2601 CG TYR A 394 -9.482 -24.641 -20.034 1.00 90.99 C ANISOU 2601 CG TYR A 394 14028 12014 8530 2958 2022 -576 C ATOM 2602 CD1 TYR A 394 -8.690 -24.431 -21.155 1.00 91.39 C ANISOU 2602 CD1 TYR A 394 13966 12417 8341 3124 2305 -614 C ATOM 2603 CD2 TYR A 394 -10.413 -23.666 -19.699 1.00 84.40 C ANISOU 2603 CD2 TYR A 394 13096 11200 7771 2707 1938 -248 C ATOM 2604 CE1 TYR A 394 -8.821 -23.288 -21.920 1.00 88.46 C ANISOU 2604 CE1 TYR A 394 13413 12394 7802 3025 2494 -299 C ATOM 2605 CE2 TYR A 394 -10.551 -22.519 -20.458 1.00 82.54 C ANISOU 2605 CE2 TYR A 394 12679 11287 7397 2635 2114 53 C ATOM 2606 CZ TYR A 394 -9.752 -22.335 -21.567 1.00 83.20 C ANISOU 2606 CZ TYR A 394 12675 11702 7235 2785 2389 44 C ATOM 2607 OH TYR A 394 -9.886 -21.195 -22.326 1.00 81.30 O ANISOU 2607 OH TYR A 394 12277 11768 6844 2708 2568 387 O ATOM 2608 N ILE A 395 -9.157 -29.168 -18.896 1.00 99.63 N ANISOU 2608 N ILE A 395 16095 11990 9770 3377 1476 -1688 N ATOM 2609 CA ILE A 395 -8.906 -30.357 -18.091 1.00101.91 C ANISOU 2609 CA ILE A 395 16639 11814 10270 3518 1296 -1906 C ATOM 2610 C ILE A 395 -7.803 -31.192 -18.735 1.00107.78 C ANISOU 2610 C ILE A 395 17454 12550 10948 3917 1441 -2263 C ATOM 2611 O ILE A 395 -6.966 -31.777 -18.047 1.00109.34 O ANISOU 2611 O ILE A 395 17662 12480 11402 4188 1404 -2369 O ATOM 2612 CB ILE A 395 -10.182 -31.211 -17.926 1.00103.91 C ANISOU 2612 CB ILE A 395 17284 11756 10440 3247 1023 -2010 C ATOM 2613 CG1 ILE A 395 -11.280 -30.400 -17.235 1.00101.54 C ANISOU 2613 CG1 ILE A 395 16879 11486 10216 2873 892 -1667 C ATOM 2614 CG2 ILE A 395 -9.889 -32.475 -17.134 1.00106.57 C ANISOU 2614 CG2 ILE A 395 17925 11570 10997 3397 851 -2209 C ATOM 2615 CD1 ILE A 395 -12.583 -31.151 -17.073 1.00104.78 C ANISOU 2615 CD1 ILE A 395 17611 11650 10550 2560 642 -1744 C ATOM 2616 N THR A 396 -7.799 -31.223 -20.064 1.00109.01 N ANISOU 2616 N THR A 396 17646 13026 10747 3970 1607 -2448 N ATOM 2617 CA THR A 396 -6.798 -31.973 -20.815 1.00114.89 C ANISOU 2617 CA THR A 396 18448 13826 11379 4355 1783 -2823 C ATOM 2618 C THR A 396 -5.496 -31.188 -20.959 1.00122.39 C ANISOU 2618 C THR A 396 18953 15131 12419 4612 2092 -2715 C ATOM 2619 O THR A 396 -4.589 -31.606 -21.681 1.00126.09 O ANISOU 2619 O THR A 396 19285 15770 12852 4813 2250 -2928 O ATOM 2620 CB THR A 396 -7.314 -32.349 -22.216 1.00115.90 C ANISOU 2620 CB THR A 396 18784 14199 11052 4287 1839 -3087 C ATOM 2621 OG1 THR A 396 -7.560 -31.157 -22.973 1.00114.84 O ANISOU 2621 OG1 THR A 396 18410 14592 10631 4134 2026 -2829 O ATOM 2622 CG2 THR A 396 -8.602 -33.151 -22.110 1.00115.39 C ANISOU 2622 CG2 THR A 396 19154 13795 10895 4017 1533 -3237 C ATOM 2623 N CYS A 397 -5.423 -30.049 -20.273 1.00125.38 N ANISOU 2623 N CYS A 397 19001 15627 13012 4449 2122 -2323 N ATOM 2624 CA CYS A 397 -4.229 -29.205 -20.245 1.00131.47 C ANISOU 2624 CA CYS A 397 19315 16703 13935 4616 2394 -2181 C ATOM 2625 C CYS A 397 -3.804 -28.740 -21.637 1.00141.32 C ANISOU 2625 C CYS A 397 20399 18466 14832 4688 2739 -2223 C ATOM 2626 O CYS A 397 -2.614 -28.699 -21.948 1.00147.77 O ANISOU 2626 O CYS A 397 20917 19501 15729 4902 2964 -2308 O ATOM 2627 CB CYS A 397 -3.069 -29.942 -19.569 1.00131.49 C ANISOU 2627 CB CYS A 397 19213 16489 14259 4963 2361 -2375 C ATOM 2628 SG CYS A 397 -3.454 -30.599 -17.929 1.00 96.80 S ANISOU 2628 SG CYS A 397 15048 11502 10231 4936 1964 -2318 S ATOM 2629 N ASN A 398 -4.780 -28.383 -22.466 1.00143.59 N ANISOU 2629 N ASN A 398 20832 18962 14762 4437 2742 -2123 N ATOM 2630 CA ASN A 398 -4.497 -27.921 -23.821 1.00149.88 C ANISOU 2630 CA ASN A 398 21513 20275 15158 4478 3057 -2122 C ATOM 2631 C ASN A 398 -4.166 -26.433 -23.865 1.00150.14 C ANISOU 2631 C ASN A 398 21141 20636 15270 4320 3291 -1674 C ATOM 2632 O ASN A 398 -3.096 -26.043 -24.334 1.00159.97 O ANISOU 2632 O ASN A 398 22083 22200 16498 4474 3617 -1658 O ATOM 2633 CB ASN A 398 -5.681 -28.217 -24.743 1.00152.04 C ANISOU 2633 CB ASN A 398 22129 20664 14976 4294 2936 -2213 C ATOM 2634 N TYR A 399 -5.098 -25.613 -23.381 1.00141.96 N ANISOU 2634 N TYR A 399 20097 19506 14336 4000 3128 -1317 N ATOM 2635 CA TYR A 399 -4.941 -24.159 -23.335 1.00137.45 C ANISOU 2635 CA TYR A 399 19188 19150 13885 3816 3310 -871 C ATOM 2636 C TYR A 399 -4.685 -23.548 -24.712 1.00138.89 C ANISOU 2636 C TYR A 399 19265 19845 13663 3818 3644 -733 C ATOM 2637 O TYR A 399 -4.095 -22.472 -24.816 1.00138.09 O ANISOU 2637 O TYR A 399 18841 19952 13674 3746 3902 -422 O ATOM 2638 CB TYR A 399 -3.808 -23.770 -22.379 1.00134.64 C ANISOU 2638 CB TYR A 399 18474 18684 13996 3910 3411 -810 C ATOM 2639 CG TYR A 399 -4.025 -24.213 -20.950 1.00128.07 C ANISOU 2639 CG TYR A 399 17721 17388 13551 3896 3089 -877 C ATOM 2640 CD1 TYR A 399 -4.723 -23.415 -20.054 1.00121.40 C ANISOU 2640 CD1 TYR A 399 16826 16351 12949 3626 2918 -581 C ATOM 2641 CD2 TYR A 399 -3.527 -25.427 -20.497 1.00129.06 C ANISOU 2641 CD2 TYR A 399 17979 17270 13788 4167 2961 -1232 C ATOM 2642 CE1 TYR A 399 -4.922 -23.816 -18.746 1.00117.06 C ANISOU 2642 CE1 TYR A 399 16353 15418 12706 3607 2639 -636 C ATOM 2643 CE2 TYR A 399 -3.721 -25.836 -19.191 1.00123.85 C ANISOU 2643 CE2 TYR A 399 17410 16200 13449 4155 2668 -1254 C ATOM 2644 CZ TYR A 399 -4.419 -25.027 -18.320 1.00117.76 C ANISOU 2644 CZ TYR A 399 16582 15284 12877 3865 2512 -955 C ATOM 2645 OH TYR A 399 -4.614 -25.431 -17.020 1.00114.31 O ANISOU 2645 OH TYR A 399 16240 14477 12714 3847 2235 -972 O ATOM 2646 N ARG A 400 -5.139 -24.239 -25.756 1.00140.43 N ANISOU 2646 N ARG A 400 19741 20237 13379 3884 3635 -965 N ATOM 2647 CA ARG A 400 -4.971 -23.794 -27.139 1.00142.39 C ANISOU 2647 CA ARG A 400 19928 20987 13187 3863 3902 -857 C ATOM 2648 C ARG A 400 -3.511 -23.504 -27.480 1.00144.18 C ANISOU 2648 C ARG A 400 19782 21444 13555 3970 4240 -859 C ATOM 2649 O ARG A 400 -2.600 -24.149 -26.961 1.00144.00 O ANISOU 2649 O ARG A 400 19641 21258 13812 4179 4266 -1142 O ATOM 2650 CB ARG A 400 -5.827 -22.554 -27.412 1.00140.44 C ANISOU 2650 CB ARG A 400 19643 20918 12799 3601 3910 -349 C TER 2651 ARG A 400 HETATM 2652 CAA H8G A1201 -16.347 -19.751 9.164 1.00 84.71 C HETATM 2653 CAB H8G A1201 -17.528 -18.822 13.521 1.00 85.96 C HETATM 2654 CAC H8G A1201 -20.745 -18.474 5.427 1.00 75.87 C HETATM 2655 CAE H8G A1201 -21.178 -17.135 9.192 1.00 76.96 C HETATM 2656 CAF H8G A1201 -23.722 -13.783 9.817 1.00 74.34 C HETATM 2657 CAG H8G A1201 -22.948 -14.929 9.670 1.00 74.41 C HETATM 2658 CAH H8G A1201 -23.996 -12.998 8.701 1.00 72.03 C HETATM 2659 CAI H8G A1201 -22.898 -13.663 5.490 1.00 71.04 C HETATM 2660 CAJ H8G A1201 -16.584 -18.734 10.242 1.00 84.11 C HETATM 2661 CAK H8G A1201 -17.180 -19.792 12.394 1.00 85.13 C HETATM 2662 CAL H8G A1201 -21.593 -15.792 5.815 1.00 71.93 C HETATM 2663 CAM H8G A1201 -20.866 -18.952 7.701 1.00 77.15 C HETATM 2664 CAP H8G A1201 -18.983 -19.139 10.796 1.00 82.34 C HETATM 2665 CAQ H8G A1201 -21.697 -16.378 8.141 1.00 75.71 C HETATM 2666 CAR H8G A1201 -22.374 -14.688 6.138 1.00 71.27 C HETATM 2667 CAS H8G A1201 -22.475 -15.258 8.405 1.00 73.95 C HETATM 2668 CAT H8G A1201 -23.523 -13.344 7.498 1.00 71.44 C HETATM 2669 CAU H8G A1201 -22.780 -14.460 7.392 1.00 72.39 C HETATM 2670 CAV H8G A1201 -20.742 -18.456 9.129 1.00 77.81 C HETATM 2671 CAW H8G A1201 -21.739 -16.910 6.854 1.00 74.58 C HETATM 2672 NAN H8G A1201 -19.354 -18.548 9.517 1.00 79.28 N HETATM 2673 NAO H8G A1201 -23.584 -12.851 6.264 1.00 71.33 N HETATM 2674 NAX H8G A1201 -20.673 -17.906 6.692 1.00 75.45 N HETATM 2675 NAY H8G A1201 -17.573 -19.225 11.155 1.00 84.06 N HETATM 2676 OAD H8G A1201 -19.856 -19.558 11.562 1.00 83.88 O HETATM 2677 C1 CLR A1202 -7.234 -29.193 -13.031 1.00 88.23 C HETATM 2678 C2 CLR A1202 -6.881 -28.885 -14.480 1.00 88.35 C HETATM 2679 C3 CLR A1202 -7.299 -27.470 -14.853 1.00 86.29 C HETATM 2680 C4 CLR A1202 -6.547 -26.476 -13.982 1.00 85.84 C HETATM 2681 C5 CLR A1202 -6.667 -26.835 -12.519 1.00 86.84 C HETATM 2682 C6 CLR A1202 -6.899 -25.828 -11.663 1.00 88.31 C HETATM 2683 C7 CLR A1202 -7.284 -26.038 -10.221 1.00 89.10 C HETATM 2684 C8 CLR A1202 -6.692 -27.346 -9.734 1.00 88.71 C HETATM 2685 C9 CLR A1202 -7.090 -28.479 -10.672 1.00 90.00 C HETATM 2686 C10 CLR A1202 -6.501 -28.271 -12.066 1.00 89.28 C HETATM 2687 C11 CLR A1202 -6.714 -29.859 -10.113 1.00 91.24 C HETATM 2688 C12 CLR A1202 -7.067 -30.075 -8.637 1.00 90.59 C HETATM 2689 C13 CLR A1202 -6.542 -28.921 -7.788 1.00 89.03 C HETATM 2690 C14 CLR A1202 -7.186 -27.668 -8.336 1.00 88.02 C HETATM 2691 C15 CLR A1202 -6.989 -26.614 -7.263 1.00 86.58 C HETATM 2692 C16 CLR A1202 -7.075 -27.412 -5.963 1.00 87.04 C HETATM 2693 C17 CLR A1202 -6.991 -28.897 -6.324 1.00 87.62 C HETATM 2694 C18 CLR A1202 -5.015 -28.844 -7.860 1.00 89.11 C HETATM 2695 C19 CLR A1202 -5.014 -28.599 -12.050 1.00 90.40 C HETATM 2696 C20 CLR A1202 -6.089 -29.635 -5.336 1.00 85.98 C HETATM 2697 C21 CLR A1202 -6.264 -31.149 -5.400 1.00 88.29 C HETATM 2698 C22 CLR A1202 -6.364 -29.147 -3.917 1.00 82.52 C HETATM 2699 C23 CLR A1202 -5.075 -28.904 -3.141 1.00 79.88 C HETATM 2700 C24 CLR A1202 -5.087 -29.650 -1.811 1.00 76.50 C HETATM 2701 C25 CLR A1202 -5.580 -28.784 -0.650 1.00 73.66 C HETATM 2702 C26 CLR A1202 -5.331 -27.298 -0.886 1.00 72.77 C HETATM 2703 C27 CLR A1202 -7.051 -29.050 -0.344 1.00 73.10 C HETATM 2704 O1 CLR A1202 -6.964 -27.230 -16.224 1.00 86.48 O HETATM 2705 C10 OLC A1203 -39.541 -19.061 -1.576 1.00 82.02 C HETATM 2706 C9 OLC A1203 -39.881 -18.281 -2.599 1.00 81.31 C HETATM 2707 C11 OLC A1203 -38.818 -20.363 -1.825 1.00 83.11 C HETATM 2708 C8 OLC A1203 -39.554 -18.699 -4.012 1.00 81.31 C HETATM 2709 C24 OLC A1203 -34.204 -14.027 -12.893 1.00 89.17 C HETATM 2710 C12 OLC A1203 -37.416 -20.282 -1.231 1.00 84.27 C HETATM 2711 C7 OLC A1203 -40.291 -17.800 -4.998 1.00 81.04 C HETATM 2712 C6 OLC A1203 -40.229 -18.352 -6.418 1.00 81.12 C HETATM 2713 C5 OLC A1203 -38.808 -18.706 -6.847 1.00 80.55 C HETATM 2714 C4 OLC A1203 -37.910 -17.477 -6.922 1.00 80.31 C HETATM 2715 C3 OLC A1203 -36.633 -17.784 -7.694 1.00 80.16 C HETATM 2716 C2 OLC A1203 -35.576 -16.716 -7.443 1.00 82.04 C HETATM 2717 C21 OLC A1203 -34.297 -15.455 -10.855 1.00 87.13 C HETATM 2718 C1 OLC A1203 -34.688 -16.575 -8.657 1.00 84.52 C HETATM 2719 C22 OLC A1203 -35.085 -14.951 -12.059 1.00 89.43 C HETATM 2720 O19 OLC A1203 -33.533 -16.966 -8.632 1.00 85.80 O HETATM 2721 O25 OLC A1203 -34.925 -13.580 -14.046 1.00 88.60 O HETATM 2722 O23 OLC A1203 -35.496 -16.064 -12.861 1.00 91.67 O HETATM 2723 O20 OLC A1203 -35.200 -15.950 -9.867 1.00 86.47 O HETATM 2724 O HOH A1301 -22.984 -18.431 13.070 1.00 59.93 O CONECT 594 1134 CONECT 1134 594 CONECT 2259 2276 CONECT 2276 2259 CONECT 2652 2660 CONECT 2653 2661 CONECT 2654 2674 CONECT 2655 2665 2670 CONECT 2656 2657 2658 CONECT 2657 2656 2667 CONECT 2658 2656 2668 CONECT 2659 2666 2673 CONECT 2660 2652 2675 CONECT 2661 2653 2675 CONECT 2662 2666 2671 CONECT 2663 2670 2674 CONECT 2664 2672 2675 2676 CONECT 2665 2655 2667 2671 CONECT 2666 2659 2662 2669 CONECT 2667 2657 2665 2669 CONECT 2668 2658 2669 2673 CONECT 2669 2666 2667 2668 CONECT 2670 2655 2663 2672 CONECT 2671 2662 2665 2674 CONECT 2672 2664 2670 CONECT 2673 2659 2668 CONECT 2674 2654 2663 2671 CONECT 2675 2660 2661 2664 CONECT 2676 2664 CONECT 2677 2678 2686 CONECT 2678 2677 2679 CONECT 2679 2678 2680 2704 CONECT 2680 2679 2681 CONECT 2681 2680 2682 2686 CONECT 2682 2681 2683 CONECT 2683 2682 2684 CONECT 2684 2683 2685 2690 CONECT 2685 2684 2686 2687 CONECT 2686 2677 2681 2685 2695 CONECT 2687 2685 2688 CONECT 2688 2687 2689 CONECT 2689 2688 2690 2693 2694 CONECT 2690 2684 2689 2691 CONECT 2691 2690 2692 CONECT 2692 2691 2693 CONECT 2693 2689 2692 2696 CONECT 2694 2689 CONECT 2695 2686 CONECT 2696 2693 2697 2698 CONECT 2697 2696 CONECT 2698 2696 2699 CONECT 2699 2698 2700 CONECT 2700 2699 2701 CONECT 2701 2700 2702 2703 CONECT 2702 2701 CONECT 2703 2701 CONECT 2704 2679 CONECT 2705 2706 2707 CONECT 2706 2705 2708 CONECT 2707 2705 2710 CONECT 2708 2706 2711 CONECT 2709 2719 2721 CONECT 2710 2707 CONECT 2711 2708 2712 CONECT 2712 2711 2713 CONECT 2713 2712 2714 CONECT 2714 2713 2715 CONECT 2715 2714 2716 CONECT 2716 2715 2718 CONECT 2717 2719 2723 CONECT 2718 2716 2720 2723 CONECT 2719 2709 2717 2722 CONECT 2720 2718 CONECT 2721 2709 CONECT 2722 2719 CONECT 2723 2717 2718 MASTER 422 0 3 20 0 0 8 6 2722 1 76 32 END