HEADER MEMBRANE PROTEIN 13-JUN-18 6DRZ 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, METHYSERGIDE, 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 6DRZ 1 REMARK REVDAT 3 19-SEP-18 6DRZ 1 JRNL REVDAT 2 05-SEP-18 6DRZ 1 JRNL REVDAT 1 29-AUG-18 6DRZ 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 1.12_2829 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) : 27.96 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 92.7 REMARK 3 NUMBER OF REFLECTIONS : 10596 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.227 REMARK 3 R VALUE (WORKING SET) : 0.225 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.710 REMARK 3 FREE R VALUE TEST SET COUNT : 499 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 27.9559 - 4.9171 0.92 2584 125 0.2171 0.2273 REMARK 3 2 4.9171 - 3.9062 0.93 2542 106 0.2047 0.2758 REMARK 3 3 3.9062 - 3.4135 0.95 2554 135 0.2454 0.2855 REMARK 3 4 3.4135 - 3.1018 0.91 2417 133 0.2837 0.3300 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) : 0.490 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.380 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 : 0.004 2965 REMARK 3 ANGLE : 0.709 4073 REMARK 3 CHIRALITY : 0.039 514 REMARK 3 PLANARITY : 0.005 491 REMARK 3 DIHEDRAL : 9.483 1716 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 40 THROUGH 248 ) REMARK 3 ORIGIN FOR THE GROUP (A): 21.5178 16.1769 0.4502 REMARK 3 T TENSOR REMARK 3 T11: 0.3327 T22: 0.2874 REMARK 3 T33: 0.3794 T12: 0.0247 REMARK 3 T13: 0.0019 T23: 0.0063 REMARK 3 L TENSOR REMARK 3 L11: 3.5570 L22: 3.6831 REMARK 3 L33: 2.9008 L12: -0.4906 REMARK 3 L13: -0.5502 L23: 0.7946 REMARK 3 S TENSOR REMARK 3 S11: 0.0565 S12: -0.0799 S13: -0.0129 REMARK 3 S21: -0.0065 S22: -0.0459 S23: 0.3379 REMARK 3 S31: -0.2920 S32: -0.3326 S33: 0.0240 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.7489 5.5269 -44.5974 REMARK 3 T TENSOR REMARK 3 T11: 0.5601 T22: 1.0596 REMARK 3 T33: 0.6379 T12: -0.1366 REMARK 3 T13: 0.1453 T23: -0.1241 REMARK 3 L TENSOR REMARK 3 L11: 3.3411 L22: 8.6646 REMARK 3 L33: 7.0126 L12: -0.0587 REMARK 3 L13: 1.8870 L23: 0.1899 REMARK 3 S TENSOR REMARK 3 S11: -0.4519 S12: 0.6283 S13: -0.3509 REMARK 3 S21: -0.5753 S22: 0.2928 S23: -0.6059 REMARK 3 S31: 0.4853 S32: 0.5784 S33: 0.2114 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 313 THROUGH 400 ) REMARK 3 ORIGIN FOR THE GROUP (A): 27.5877 22.8860 -5.3558 REMARK 3 T TENSOR REMARK 3 T11: 0.7551 T22: 0.3353 REMARK 3 T33: 0.5068 T12: 0.0520 REMARK 3 T13: 0.0924 T23: -0.1387 REMARK 3 L TENSOR REMARK 3 L11: 4.5605 L22: 2.6711 REMARK 3 L33: 4.7426 L12: 0.1994 REMARK 3 L13: 0.2343 L23: -2.0024 REMARK 3 S TENSOR REMARK 3 S11: 0.2732 S12: -0.0514 S13: 0.0176 REMARK 3 S21: -0.0096 S22: -0.1854 S23: 0.1469 REMARK 3 S31: -0.8146 S32: 0.2211 S33: -0.1200 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 6DRZ 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_1000235165. 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 : 10618 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 (%) : 93.4 REMARK 200 DATA REDUNDANCY : 3.300 REMARK 200 R MERGE (I) : 0.16300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.7000 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) : 3.19 REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4 REMARK 200 DATA REDUNDANCY IN SHELL : 3.30 REMARK 200 R MERGE FOR SHELL (I) : 0.84500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 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 (%): 62.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.30 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS/HCL PH 7.3-7.5, 40-100 MM REMARK 280 MGCL2, 30% V/V PEG400, LIPIDIC CUBIC PHASE, 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 86.31200 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 86.31200 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 29.54750 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.64150 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.54750 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.64150 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 86.31200 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.54750 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.64150 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 86.31200 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.54750 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.64150 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 ASN A 164 REMARK 465 GLN A 165 REMARK 465 TYR A 166 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 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 ILE A 39 CG1 CG2 CD1 REMARK 470 GLU A 41 CG CD OE1 OE2 REMARK 470 GLU A 42 CG CD OE1 OE2 REMARK 470 MET A 43 CG SD CE REMARK 470 LYS A 44 CG CD CE NZ REMARK 470 GLN A 45 CG CD OE1 NE2 REMARK 470 ILE A 46 CG1 CG2 CD1 REMARK 470 VAL A 47 CG1 CG2 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 GLU A 82 CG CD OE1 OE2 REMARK 470 LYS A 83 CG CD CE NZ REMARK 470 LYS A 84 CG CD CE NZ REMARK 470 THR A 89 OG1 CG2 REMARK 470 TYR A 91 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLU A 118 CG CD OE1 OE2 REMARK 470 MET A 120 CG SD CE REMARK 470 LEU A 125 CG CD1 CD2 REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 158 CG CD CE NZ 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 167 CG OD1 ND2 REMARK 470 SER A 168 OG REMARK 470 ARG A 169 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 196 CG CD OE1 OE2 REMARK 470 THR A 197 OG1 CG2 REMARK 470 VAL A 199 CG1 CG2 REMARK 470 ASP A 200 CG OD1 OD2 REMARK 470 ASN A 201 CG OD1 ND2 REMARK 470 ASN A 203 CG OD1 ND2 REMARK 470 ASN A 204 CG OD1 ND2 REMARK 470 THR A 206 OG1 CG2 REMARK 470 ASP A 216 CG OD1 OD2 REMARK 470 HIS A 242 CG ND1 CD2 CE1 NE2 REMARK 470 LYS A 246 CG CD CE NZ 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 GLU A1018 CG CD OE1 OE2 REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 ASP A1021 CG OD1 OD2 REMARK 470 GLN A1025 CG CD OE1 NE2 REMARK 470 VAL A1026 CG1 CG2 REMARK 470 LYS A1027 CG CD CE NZ REMARK 470 ASP A1028 CG OD1 OD2 REMARK 470 LYS A1032 CG CD CE NZ REMARK 470 LYS A1042 CG CD CE NZ 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 GLN A1088 CG CD OE1 NE2 REMARK 470 GLU A1092 CG CD OE1 OE2 REMARK 470 GLN A1093 CG CD OE1 NE2 REMARK 470 LYS A1095 CG CD CE NZ REMARK 470 THR A1096 OG1 CG2 REMARK 470 GLN A1103 CG CD OE1 NE2 REMARK 470 LYS A1104 CG CD CE NZ REMARK 470 LEU A1106 CG CD1 CD2 REMARK 470 ARG A 321 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 324 CG CD CE NZ REMARK 470 ASP A 351 CG OD1 OD2 REMARK 470 GLU A 363 CG CD OE1 OE2 REMARK 470 LYS A 385 CG CD CE NZ 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 -60.19 -120.64 REMARK 500 TYR A 87 -170.26 -173.95 REMARK 500 PRO A 124 170.17 -55.20 REMARK 500 THR A 206 81.22 59.44 REMARK 500 LEU A 219 -68.65 -92.64 REMARK 500 PHE A 226 -54.57 -129.55 REMARK 500 LYS A1083 85.48 -69.15 REMARK 500 TYR A1101 -61.69 -122.36 REMARK 500 TYR A 399 -137.60 59.95 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 OLA A 1202 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 CLR A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA 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 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue H8J A 1206 DBREF 6DRZ A 36 248 UNP P41595 5HT2B_HUMAN 36 248 DBREF 6DRZ A 1001 1101 UNP P0ABE7 C562_ECOLX 23 123 DBREF 6DRZ A 313 404 UNP P41595 5HT2B_HUMAN 313 404 SEQADV 6DRZ TRP A 144 UNP P41595 MET 144 ENGINEERED MUTATION SEQADV 6DRZ GLY A 225 UNP P41595 ALA 225 ENGINEERED MUTATION SEQADV 6DRZ TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6DRZ ILE A 1102 UNP P0ABE7 LINKER SEQADV 6DRZ GLN A 1103 UNP P0ABE7 LINKER SEQADV 6DRZ LYS A 1104 UNP P0ABE7 LINKER SEQADV 6DRZ TYR A 1105 UNP P0ABE7 LINKER SEQADV 6DRZ LEU A 1106 UNP P0ABE7 LINKER SEQRES 1 A 411 THR GLU SER ILE PRO GLU GLU MET LYS GLN ILE VAL GLU SEQRES 2 A 411 GLU GLN GLY ASN LYS LEU HIS TRP ALA ALA LEU LEU ILE SEQRES 3 A 411 LEU MET VAL ILE ILE PRO THR ILE GLY GLY ASN THR LEU SEQRES 4 A 411 VAL ILE LEU ALA VAL SER LEU GLU LYS LYS LEU GLN TYR SEQRES 5 A 411 ALA THR ASN TYR PHE LEU MET SER LEU ALA VAL ALA ASP SEQRES 6 A 411 LEU LEU VAL GLY LEU PHE VAL MET PRO ILE ALA LEU LEU SEQRES 7 A 411 THR ILE MET PHE GLU ALA MET TRP PRO LEU PRO LEU VAL SEQRES 8 A 411 LEU CYS PRO ALA TRP LEU PHE LEU ASP VAL LEU PHE SER SEQRES 9 A 411 THR ALA SER ILE TRP HIS LEU CYS ALA ILE SER VAL ASP SEQRES 10 A 411 ARG TYR ILE ALA ILE LYS LYS PRO ILE GLN ALA ASN GLN SEQRES 11 A 411 TYR ASN SER ARG ALA THR ALA PHE ILE LYS ILE THR VAL SEQRES 12 A 411 VAL TRP LEU ILE SER ILE GLY ILE ALA ILE PRO VAL PRO SEQRES 13 A 411 ILE LYS GLY ILE GLU THR ASP VAL ASP ASN PRO ASN ASN SEQRES 14 A 411 ILE THR CYS VAL LEU THR LYS GLU ARG PHE GLY ASP PHE SEQRES 15 A 411 MET LEU PHE GLY SER LEU ALA GLY PHE PHE THR PRO LEU SEQRES 16 A 411 ALA ILE MET ILE VAL THR TYR PHE LEU THR ILE HIS ALA SEQRES 17 A 411 LEU GLN LYS LYS ALA ALA ASP LEU GLU ASP ASN TRP GLU SEQRES 18 A 411 THR LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP SEQRES 19 A 411 ASN ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG SEQRES 20 A 411 ALA ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS SEQRES 21 A 411 LEU GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP SEQRES 22 A 411 PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP SEQRES 23 A 411 ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU SEQRES 24 A 411 ALA GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN SEQRES 25 A 411 ALA TYR ILE GLN LYS TYR LEU VAL GLN THR ILE SER ASN SEQRES 26 A 411 GLU GLN ARG ALA SER LYS VAL LEU GLY ILE VAL PHE PHE SEQRES 27 A 411 LEU PHE LEU LEU MET TRP CYS PRO PHE PHE ILE THR ASN SEQRES 28 A 411 ILE THR LEU VAL LEU CYS ASP SER CYS ASN GLN THR THR SEQRES 29 A 411 LEU GLN MET LEU LEU GLU ILE PHE VAL TRP ILE GLY TYR SEQRES 30 A 411 VAL SER SER GLY VAL ASN PRO LEU VAL TYR THR LEU PHE SEQRES 31 A 411 ASN LYS THR PHE ARG ASP ALA PHE GLY ARG TYR ILE THR SEQRES 32 A 411 CYS ASN TYR ARG ALA THR LYS SER HET CLR A1201 28 HET OLA A1202 17 HET OLC A1203 19 HET PEG A1204 7 HET PO4 A1205 5 HET H8J A1206 26 HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM PO4 PHOSPHATE ION HETNAM H8J (8ALPHA)-N-[(2S)-1-HYDROXYBUTAN-2-YL]-1,6-DIMETHYL-9, HETNAM 2 H8J 10-DIDEHYDROERGOLINE-8-CARBOXAMIDE HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN H8J METHYSERGIDE FORMUL 2 CLR C27 H46 O FORMUL 3 OLA C18 H34 O2 FORMUL 4 OLC C21 H40 O4 FORMUL 5 PEG C4 H10 O3 FORMUL 6 PO4 O4 P 3- FORMUL 7 H8J C21 H27 N3 O2 FORMUL 8 HOH *3(H2 O) HELIX 1 AA1 ILE A 39 GLN A 50 1 12 HELIX 2 AA2 LYS A 53 VAL A 64 1 12 HELIX 3 AA3 VAL A 64 GLU A 82 1 19 HELIX 4 AA4 LYS A 83 GLN A 86 5 4 HELIX 5 AA5 TYR A 87 PHE A 117 1 31 HELIX 6 AA6 VAL A 126 LYS A 159 1 34 HELIX 7 AA7 SER A 168 ILE A 188 1 21 HELIX 8 AA8 ILE A 188 GLY A 194 1 7 HELIX 9 AA9 THR A 210 PHE A 226 1 17 HELIX 10 AB1 PHE A 226 LYS A 1019 1 42 HELIX 11 AB2 ALA A 1023 LYS A 1042 1 20 HELIX 12 AB3 ARG A 1062 GLY A 1082 1 21 HELIX 13 AB4 LYS A 1083 GLU A 1092 1 10 HELIX 14 AB5 GLN A 1093 TYR A 1101 1 9 HELIX 15 AB6 TYR A 1101 MET A 336 1 30 HELIX 16 AB7 TRP A 337 CYS A 350 1 14 HELIX 17 AB8 ASN A 354 VAL A 375 1 22 HELIX 18 AB9 VAL A 375 LEU A 382 1 8 HELIX 19 AC1 ASN A 384 THR A 396 1 13 SSBOND 1 CYS A 128 CYS A 207 1555 1555 2.00 SSBOND 2 CYS A 350 CYS A 353 1555 1555 2.03 SITE 1 AC1 4 ILE A 66 ILE A 69 TYR A 394 TYR A 399 SITE 1 AC2 5 GLY A 185 LYS A 193 ASP A 216 PHE A 217 SITE 2 AC2 5 PHE A 220 SITE 1 AC3 5 SER A 150 MET A 233 TYR A 237 THR A 240 SITE 2 AC3 5 LEU A 326 SITE 1 AC4 1 TYR A 380 SITE 1 AC5 3 ARG A 388 ASP A 389 GLY A 392 SITE 1 AC6 10 ASP A 135 SER A 139 THR A 140 VAL A 208 SITE 2 AC6 10 LEU A 209 PHE A 217 GLY A 221 GLY A 225 SITE 3 AC6 10 PHE A 340 HOH A1301 CRYST1 59.095 119.283 172.624 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 0.016922 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008383 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005793 0.00000 ATOM 1 N ILE A 39 21.941 37.446 37.528 1.00139.73 N ATOM 2 CA ILE A 39 22.384 38.792 37.187 1.00135.68 C ATOM 3 C ILE A 39 21.480 39.388 36.115 1.00126.77 C ATOM 4 O ILE A 39 21.550 38.989 34.954 1.00133.99 O ATOM 5 CB ILE A 39 23.855 38.790 36.729 1.00139.60 C ATOM 6 N PRO A 40 20.629 40.342 36.514 1.00194.35 N ANISOU 6 N PRO A 40 29490 25258 19098 1423 2122 -7451 N ATOM 7 CA PRO A 40 19.672 40.934 35.556 1.00159.93 C ANISOU 7 CA PRO A 40 24971 20564 15232 1630 2341 -7395 C ATOM 8 C PRO A 40 20.326 41.538 34.323 1.00168.07 C ANISOU 8 C PRO A 40 25832 21212 16813 1527 2103 -7398 C ATOM 9 O PRO A 40 19.765 41.436 33.224 1.00171.42 O ANISOU 9 O PRO A 40 26041 21464 17628 1630 2198 -7168 O ATOM 10 CB PRO A 40 18.953 41.996 36.400 1.00141.91 C ANISOU 10 CB PRO A 40 22903 18168 12849 1823 2573 -7741 C ATOM 11 CG PRO A 40 19.093 41.520 37.802 1.00148.98 C ANISOU 11 CG PRO A 40 24049 19443 13114 1767 2621 -7844 C ATOM 12 CD PRO A 40 20.417 40.826 37.887 1.00164.42 C ANISOU 12 CD PRO A 40 25998 21603 14870 1480 2243 -7765 C ATOM 13 N GLU A 41 21.500 42.159 34.468 1.00150.28 N ANISOU 13 N GLU A 41 23666 18828 14606 1316 1800 -7646 N ATOM 14 CA GLU A 41 22.215 42.704 33.319 1.00139.55 C ANISOU 14 CA GLU A 41 22153 17105 13763 1179 1587 -7633 C ATOM 15 C GLU A 41 22.644 41.628 32.329 1.00128.60 C ANISOU 15 C GLU A 41 20523 15821 12518 1063 1449 -7256 C ATOM 16 O GLU A 41 22.984 41.964 31.190 1.00122.99 O ANISOU 16 O GLU A 41 19660 14804 12267 990 1350 -7166 O ATOM 17 CB GLU A 41 23.436 43.502 33.784 1.00133.30 C ANISOU 17 CB GLU A 41 21489 16196 12964 951 1296 -7977 C ATOM 18 N GLU A 42 22.638 40.357 32.735 1.00128.89 N ANISOU 18 N GLU A 42 20533 16271 12170 1041 1448 -7031 N ATOM 19 CA GLU A 42 22.894 39.222 31.855 1.00124.84 C ANISOU 19 CA GLU A 42 19795 15886 11753 965 1355 -6662 C ATOM 20 C GLU A 42 21.616 38.530 31.404 1.00132.10 C ANISOU 20 C GLU A 42 20589 16886 12716 1172 1665 -6364 C ATOM 21 O GLU A 42 21.548 38.055 30.266 1.00139.98 O ANISOU 21 O GLU A 42 21373 17795 14018 1164 1647 -6104 O ATOM 22 CB GLU A 42 23.805 38.207 32.549 1.00120.06 C ANISOU 22 CB GLU A 42 19221 15683 10714 800 1118 -6583 C ATOM 23 N MET A 43 20.603 38.457 32.273 1.00131.26 N ANISOU 23 N MET A 43 20604 16953 12316 1352 1957 -6400 N ATOM 24 CA MET A 43 19.303 37.939 31.856 1.00127.95 C ANISOU 24 CA MET A 43 20036 16587 11991 1560 2275 -6147 C ATOM 25 C MET A 43 18.728 38.772 30.719 1.00133.39 C ANISOU 25 C MET A 43 20562 16884 13237 1704 2345 -6150 C ATOM 26 O MET A 43 18.196 38.224 29.745 1.00137.62 O ANISOU 26 O MET A 43 20866 17397 14029 1773 2420 -5874 O ATOM 27 CB MET A 43 18.340 37.906 33.042 1.00128.86 C ANISOU 27 CB MET A 43 20315 16921 11726 1727 2594 -6230 C ATOM 28 N LYS A 44 18.835 40.100 30.820 1.00119.48 N ANISOU 28 N LYS A 44 18918 14807 11670 1746 2311 -6456 N ATOM 29 CA LYS A 44 18.436 40.960 29.710 1.00123.91 C ANISOU 29 CA LYS A 44 19346 14962 12772 1857 2336 -6447 C ATOM 30 C LYS A 44 19.273 40.674 28.470 1.00134.30 C ANISOU 30 C LYS A 44 20502 16110 14415 1668 2096 -6247 C ATOM 31 O LYS A 44 18.774 40.761 27.342 1.00115.61 O ANISOU 31 O LYS A 44 17955 13532 12439 1761 2148 -6060 O ATOM 32 CB LYS A 44 18.555 42.431 30.109 1.00112.76 C ANISOU 32 CB LYS A 44 18125 13230 11490 1900 2322 -6815 C ATOM 33 N GLN A 45 20.548 40.320 28.659 1.00138.27 N ANISOU 33 N GLN A 45 21059 16715 14761 1405 1830 -6279 N ATOM 34 CA GLN A 45 21.408 40.021 27.517 1.00114.42 C ANISOU 34 CA GLN A 45 17883 13553 12039 1217 1611 -6097 C ATOM 35 C GLN A 45 20.940 38.769 26.785 1.00108.00 C ANISOU 35 C GLN A 45 16859 12936 11242 1263 1685 -5731 C ATOM 36 O GLN A 45 20.968 38.722 25.549 1.00107.41 O ANISOU 36 O GLN A 45 16624 12646 11540 1242 1647 -5543 O ATOM 37 CB GLN A 45 22.861 39.872 27.972 1.00116.92 C ANISOU 37 CB GLN A 45 18270 13984 12172 940 1307 -6224 C ATOM 38 N ILE A 46 20.503 37.745 27.525 1.00107.25 N ANISOU 38 N ILE A 46 16769 13238 10742 1318 1801 -5618 N ATOM 39 CA ILE A 46 19.960 36.551 26.882 1.00108.42 C ANISOU 39 CA ILE A 46 16716 13573 10906 1365 1901 -5277 C ATOM 40 C ILE A 46 18.601 36.848 26.271 1.00111.42 C ANISOU 40 C ILE A 46 16949 13801 11583 1609 2162 -5183 C ATOM 41 O ILE A 46 18.220 36.244 25.260 1.00111.88 O ANISOU 41 O ILE A 46 16796 13838 11875 1634 2199 -4929 O ATOM 42 CB ILE A 46 19.881 35.382 27.881 1.00108.43 C ANISOU 42 CB ILE A 46 16776 14029 10393 1341 1966 -5159 C ATOM 43 N VAL A 47 17.844 37.771 26.871 1.00130.01 N ANISOU 43 N VAL A 47 19400 16058 13938 1795 2338 -5392 N ATOM 44 CA VAL A 47 16.624 38.254 26.235 1.00125.42 C ANISOU 44 CA VAL A 47 18658 15295 13701 2038 2537 -5335 C ATOM 45 C VAL A 47 16.949 38.875 24.884 1.00129.48 C ANISOU 45 C VAL A 47 19084 15403 14711 2000 2387 -5265 C ATOM 46 O VAL A 47 16.164 38.767 23.936 1.00112.12 O ANISOU 46 O VAL A 47 16684 13097 12819 2131 2473 -5069 O ATOM 47 CB VAL A 47 15.889 39.246 27.159 1.00110.25 C ANISOU 47 CB VAL A 47 16876 13320 11695 2244 2724 -5610 C ATOM 48 N GLU A 48 18.113 39.520 24.769 1.00147.02 N ANISOU 48 N GLU A 48 21450 17393 17016 1811 2162 -5408 N ATOM 49 CA GLU A 48 18.572 40.025 23.481 1.00129.92 C ANISOU 49 CA GLU A 48 19222 14849 15291 1733 2021 -5301 C ATOM 50 C GLU A 48 19.119 38.910 22.598 1.00125.54 C ANISOU 50 C GLU A 48 18514 14400 14784 1567 1902 -5017 C ATOM 51 O GLU A 48 19.066 39.020 21.367 1.00133.23 O ANISOU 51 O GLU A 48 19383 15123 16117 1573 1870 -4823 O ATOM 52 CB GLU A 48 19.635 41.103 23.690 1.00126.06 C ANISOU 52 CB GLU A 48 18925 14081 14892 1568 1845 -5551 C ATOM 53 N GLU A 49 19.636 37.834 23.200 1.00122.57 N ANISOU 53 N GLU A 49 18138 14389 14044 1429 1837 -4978 N ATOM 54 CA GLU A 49 20.129 36.710 22.410 1.00103.85 C ANISOU 54 CA GLU A 49 15623 12136 11700 1283 1733 -4718 C ATOM 55 C GLU A 49 18.991 36.032 21.658 1.00100.61 C ANISOU 55 C GLU A 49 15014 11775 11439 1442 1923 -4450 C ATOM 56 O GLU A 49 19.131 35.692 20.476 1.00106.84 O ANISOU 56 O GLU A 49 15690 12413 12494 1388 1873 -4232 O ATOM 57 CB GLU A 49 20.857 35.710 23.313 1.00103.43 C ANISOU 57 CB GLU A 49 15618 12482 11196 1133 1617 -4730 C ATOM 58 N GLN A 50 17.854 35.822 22.327 1.00103.19 N ANISOU 58 N GLN A 50 15294 12313 11601 1634 2150 -4457 N ATOM 59 CA GLN A 50 16.644 35.314 21.676 1.00107.88 C ANISOU 59 CA GLN A 50 15667 12942 12378 1800 2346 -4228 C ATOM 60 C GLN A 50 15.908 36.477 21.012 1.00128.83 C ANISOU 60 C GLN A 50 18275 15242 15433 2004 2397 -4267 C ATOM 61 O GLN A 50 14.795 36.857 21.383 1.00103.45 O ANISOU 61 O GLN A 50 14989 12067 12252 2228 2580 -4332 O ATOM 62 CB GLN A 50 15.747 34.595 22.673 1.00106.07 C ANISOU 62 CB GLN A 50 15376 13098 11827 1902 2575 -4205 C ATOM 63 N GLY A 51 16.566 37.048 20.007 1.00129.50 N ANISOU 63 N GLY A 51 18404 14979 15822 1927 2227 -4215 N ATOM 64 CA GLY A 51 16.070 38.216 19.312 1.00103.59 C ANISOU 64 CA GLY A 51 15124 11325 12910 2101 2230 -4226 C ATOM 65 C GLY A 51 15.085 37.864 18.220 1.00106.91 C ANISOU 65 C GLY A 51 15326 11691 13604 2274 2297 -3947 C ATOM 66 O GLY A 51 14.442 36.812 18.235 1.00127.70 O ANISOU 66 O GLY A 51 17778 14603 16140 2313 2411 -3795 O ATOM 67 N ASN A 52 14.961 38.776 17.262 1.00106.90 N ANISOU 67 N ASN A 52 15345 11324 13947 2381 2218 -3871 N ATOM 68 CA ASN A 52 14.146 38.557 16.077 1.00108.26 C ANISOU 68 CA ASN A 52 15332 11410 14391 2550 2217 -3590 C ATOM 69 C ASN A 52 15.075 38.379 14.885 1.00 88.67 C ANISOU 69 C ASN A 52 12916 8717 12058 2383 2043 -3359 C ATOM 70 O ASN A 52 15.881 39.266 14.580 1.00 86.73 O ANISOU 70 O ASN A 52 12849 8169 11937 2285 1931 -3408 O ATOM 71 CB ASN A 52 13.173 39.712 15.849 1.00102.19 C ANISOU 71 CB ASN A 52 14538 10412 13879 2843 2253 -3643 C ATOM 72 CG ASN A 52 11.896 39.265 15.165 1.00 88.35 C ANISOU 72 CG ASN A 52 12509 8767 12294 3082 2304 -3432 C ATOM 73 OD1 ASN A 52 11.878 38.258 14.457 1.00 82.48 O ANISOU 73 OD1 ASN A 52 11625 8151 11564 3020 2263 -3187 O ATOM 74 ND2 ASN A 52 10.819 40.012 15.375 1.00 92.72 N ANISOU 74 ND2 ASN A 52 12978 9273 12977 3363 2387 -3534 N ATOM 75 N LYS A 53 14.965 37.231 14.221 1.00 82.45 N ANISOU 75 N LYS A 53 11988 8088 11252 2347 2034 -3103 N ATOM 76 CA LYS A 53 15.846 36.897 13.112 1.00 79.13 C ANISOU 76 CA LYS A 53 11612 7545 10910 2177 1850 -2849 C ATOM 77 C LYS A 53 15.044 36.658 11.838 1.00 70.75 C ANISOU 77 C LYS A 53 10389 6439 10052 2359 1784 -2533 C ATOM 78 O LYS A 53 15.270 35.670 11.133 1.00 69.55 O ANISOU 78 O LYS A 53 10125 6460 9839 2242 1650 -2270 O ATOM 79 CB LYS A 53 16.685 35.663 13.457 1.00 69.84 C ANISOU 79 CB LYS A 53 10386 6702 9446 1900 1743 -2760 C ATOM 80 N LEU A 54 14.100 37.554 11.539 1.00 72.66 N ANISOU 80 N LEU A 54 10606 6477 10526 2644 1842 -2558 N ATOM 81 CA LEU A 54 13.298 37.411 10.330 1.00 72.02 C ANISOU 81 CA LEU A 54 10375 6354 10635 2851 1755 -2278 C ATOM 82 C LEU A 54 14.049 37.847 9.080 1.00 82.19 C ANISOU 82 C LEU A 54 11831 7348 12050 2783 1586 -2051 C ATOM 83 O LEU A 54 13.785 37.324 7.992 1.00100.80 O ANISOU 83 O LEU A 54 14099 9747 14454 2856 1472 -1774 O ATOM 84 CB LEU A 54 12.003 38.212 10.452 1.00 74.76 C ANISOU 84 CB LEU A 54 10583 6660 11161 3161 1798 -2361 C ATOM 85 CG LEU A 54 10.756 37.428 10.855 1.00 75.22 C ANISOU 85 CG LEU A 54 10326 7062 11193 3323 1914 -2377 C ATOM 86 CD1 LEU A 54 9.528 38.292 10.666 1.00 92.56 C ANISOU 86 CD1 LEU A 54 12375 9175 13618 3646 1902 -2420 C ATOM 87 CD2 LEU A 54 10.647 36.150 10.043 1.00 72.63 C ANISOU 87 CD2 LEU A 54 9819 6943 10833 3272 1833 -2103 C ATOM 88 N HIS A 55 14.973 38.801 9.211 1.00 78.06 N ANISOU 88 N HIS A 55 11539 6548 11573 2636 1560 -2161 N ATOM 89 CA HIS A 55 15.711 39.281 8.047 1.00 76.93 C ANISOU 89 CA HIS A 55 11557 6122 11551 2548 1434 -1937 C ATOM 90 C HIS A 55 16.621 38.197 7.483 1.00 68.21 C ANISOU 90 C HIS A 55 10473 5137 10308 2321 1375 -1756 C ATOM 91 O HIS A 55 16.799 38.103 6.263 1.00 80.52 O ANISOU 91 O HIS A 55 12071 6601 11921 2330 1272 -1475 O ATOM 92 CB HIS A 55 16.510 40.531 8.418 1.00 89.35 C ANISOU 92 CB HIS A 55 13347 7382 13218 2415 1443 -2117 C ATOM 93 CG HIS A 55 17.156 40.456 9.767 1.00 74.85 C ANISOU 93 CG HIS A 55 11560 5664 11218 2217 1518 -2450 C ATOM 94 ND1 HIS A 55 16.447 40.604 10.940 1.00 75.42 N ANISOU 94 ND1 HIS A 55 11565 5885 11204 2346 1623 -2722 N ATOM 95 CD2 HIS A 55 18.444 40.253 10.130 1.00 74.29 C ANISOU 95 CD2 HIS A 55 11589 5603 11036 1902 1490 -2557 C ATOM 96 CE1 HIS A 55 17.270 40.490 11.967 1.00 75.63 C ANISOU 96 CE1 HIS A 55 11672 6016 11047 2125 1647 -2975 C ATOM 97 NE2 HIS A 55 18.488 40.278 11.503 1.00 81.34 N ANISOU 97 NE2 HIS A 55 12485 6658 11763 1854 1555 -2886 N ATOM 98 N TRP A 56 17.202 37.368 8.353 1.00 68.55 N ANISOU 98 N TRP A 56 10456 5452 10138 2094 1392 -1897 N ATOM 99 CA TRP A 56 18.012 36.251 7.877 1.00 64.38 C ANISOU 99 CA TRP A 56 9858 5151 9454 1850 1262 -1710 C ATOM 100 C TRP A 56 17.148 35.191 7.211 1.00 63.99 C ANISOU 100 C TRP A 56 9580 5380 9352 1968 1179 -1470 C ATOM 101 O TRP A 56 17.545 34.604 6.198 1.00 63.59 O ANISOU 101 O TRP A 56 9510 5376 9276 1880 1059 -1235 O ATOM 102 CB TRP A 56 18.809 35.646 9.031 1.00 63.86 C ANISOU 102 CB TRP A 56 9771 5324 9169 1602 1268 -1911 C ATOM 103 CG TRP A 56 19.737 36.615 9.678 1.00 68.49 C ANISOU 103 CG TRP A 56 10556 5667 9798 1452 1315 -2178 C ATOM 104 CD1 TRP A 56 19.679 37.073 10.960 1.00 77.62 C ANISOU 104 CD1 TRP A 56 11772 6846 10875 1456 1409 -2511 C ATOM 105 CD2 TRP A 56 20.861 37.259 9.071 1.00 75.20 C ANISOU 105 CD2 TRP A 56 11571 6214 10789 1266 1277 -2154 C ATOM 106 NE1 TRP A 56 20.703 37.959 11.193 1.00 74.92 N ANISOU 106 NE1 TRP A 56 11613 6230 10622 1277 1407 -2716 N ATOM 107 CE2 TRP A 56 21.443 38.091 10.047 1.00 79.47 C ANISOU 107 CE2 TRP A 56 12248 6596 11352 1150 1336 -2497 C ATOM 108 CE3 TRP A 56 21.435 37.212 7.797 1.00 77.11 C ANISOU 108 CE3 TRP A 56 11858 6308 11134 1177 1212 -1885 C ATOM 109 CZ2 TRP A 56 22.568 38.868 9.790 1.00 90.19 C ANISOU 109 CZ2 TRP A 56 13717 7709 12841 927 1280 -2539 C ATOM 110 CZ3 TRP A 56 22.551 37.984 7.543 1.00 86.98 C ANISOU 110 CZ3 TRP A 56 13271 7251 12526 968 1232 -1946 C ATOM 111 CH2 TRP A 56 23.107 38.801 8.535 1.00 98.14 C ANISOU 111 CH2 TRP A 56 14752 8569 13968 834 1243 -2257 C ATOM 112 N ALA A 57 15.962 34.931 7.767 1.00 63.96 N ANISOU 112 N ALA A 57 9395 5568 9339 2161 1252 -1542 N ATOM 113 CA ALA A 57 15.043 33.988 7.139 1.00 67.57 C ANISOU 113 CA ALA A 57 9608 6274 9792 2273 1175 -1345 C ATOM 114 C ALA A 57 14.607 34.482 5.766 1.00 92.74 C ANISOU 114 C ALA A 57 12823 9265 13150 2475 1061 -1126 C ATOM 115 O ALA A 57 14.572 33.708 4.802 1.00 93.71 O ANISOU 115 O ALA A 57 12852 9521 13231 2444 918 -909 O ATOM 116 CB ALA A 57 13.832 33.755 8.040 1.00 65.21 C ANISOU 116 CB ALA A 57 9094 6191 9490 2439 1309 -1487 C ATOM 117 N ALA A 58 14.277 35.773 5.655 1.00 82.13 N ANISOU 117 N ALA A 58 11621 7596 11990 2693 1118 -1181 N ATOM 118 CA ALA A 58 13.940 36.341 4.353 1.00 65.84 C ANISOU 118 CA ALA A 58 9635 5315 10068 2904 1002 -948 C ATOM 119 C ALA A 58 15.114 36.233 3.390 1.00 70.22 C ANISOU 119 C ALA A 58 10385 5747 10548 2689 906 -744 C ATOM 120 O ALA A 58 14.929 35.918 2.208 1.00113.64 O ANISOU 120 O ALA A 58 15867 11288 16024 2765 763 -495 O ATOM 121 CB ALA A 58 13.500 37.795 4.505 1.00 68.74 C ANISOU 121 CB ALA A 58 10119 5355 10644 3116 1064 -1043 C ATOM 122 N LEU A 59 16.333 36.486 3.878 1.00 63.78 N ANISOU 122 N LEU A 59 9748 4796 9689 2417 985 -861 N ATOM 123 CA LEU A 59 17.516 36.314 3.039 1.00 66.45 C ANISOU 123 CA LEU A 59 10237 5047 9964 2183 926 -690 C ATOM 124 C LEU A 59 17.619 34.890 2.513 1.00 60.66 C ANISOU 124 C LEU A 59 9321 4674 9052 2062 798 -538 C ATOM 125 O LEU A 59 17.943 34.676 1.340 1.00 59.16 O ANISOU 125 O LEU A 59 9198 4459 8820 2038 708 -309 O ATOM 126 CB LEU A 59 18.780 36.678 3.818 1.00 70.83 C ANISOU 126 CB LEU A 59 10935 5463 10514 1891 1023 -891 C ATOM 127 CG LEU A 59 19.245 38.132 3.781 1.00 91.00 C ANISOU 127 CG LEU A 59 13734 7584 13258 1877 1111 -955 C ATOM 128 CD1 LEU A 59 20.644 38.244 4.362 1.00105.91 C ANISOU 128 CD1 LEU A 59 15712 9401 15128 1530 1163 -1134 C ATOM 129 CD2 LEU A 59 19.207 38.654 2.358 1.00101.60 C ANISOU 129 CD2 LEU A 59 15184 8745 14673 1961 1036 -639 C ATOM 130 N LEU A 60 17.340 33.902 3.365 1.00 61.00 N ANISOU 130 N LEU A 60 9148 5045 8984 1988 800 -663 N ATOM 131 CA LEU A 60 17.482 32.510 2.950 1.00 59.14 C ANISOU 131 CA LEU A 60 8747 5121 8603 1855 693 -541 C ATOM 132 C LEU A 60 16.382 32.106 1.977 1.00 76.09 C ANISOU 132 C LEU A 60 10744 7392 10775 2073 568 -366 C ATOM 133 O LEU A 60 16.622 31.314 1.057 1.00 65.85 O ANISOU 133 O LEU A 60 9409 6222 9390 1997 451 -206 O ATOM 134 CB LEU A 60 17.492 31.602 4.178 1.00 57.76 C ANISOU 134 CB LEU A 60 8409 5227 8312 1718 746 -704 C ATOM 135 CG LEU A 60 18.713 31.799 5.077 1.00 57.33 C ANISOU 135 CG LEU A 60 8484 5115 8184 1481 812 -871 C ATOM 136 CD1 LEU A 60 18.537 31.066 6.370 1.00 67.97 C ANISOU 136 CD1 LEU A 60 9703 6730 9394 1412 869 -1026 C ATOM 137 CD2 LEU A 60 19.973 31.325 4.380 1.00 55.70 C ANISOU 137 CD2 LEU A 60 8344 4900 7920 1250 733 -752 C ATOM 138 N ILE A 61 15.170 32.633 2.164 1.00 62.98 N ANISOU 138 N ILE A 61 8986 5706 9238 2349 586 -414 N ATOM 139 CA ILE A 61 14.094 32.379 1.208 1.00 60.85 C ANISOU 139 CA ILE A 61 8559 5547 9015 2582 438 -264 C ATOM 140 C ILE A 61 14.460 32.950 -0.154 1.00 59.59 C ANISOU 140 C ILE A 61 8619 5177 8846 2665 324 -35 C ATOM 141 O ILE A 61 14.300 32.296 -1.191 1.00 58.98 O ANISOU 141 O ILE A 61 8482 5250 8678 2685 163 128 O ATOM 142 CB ILE A 61 12.764 32.970 1.713 1.00 62.28 C ANISOU 142 CB ILE A 61 8580 5720 9364 2885 489 -375 C ATOM 143 CG1 ILE A 61 12.333 32.316 3.023 1.00 73.69 C ANISOU 143 CG1 ILE A 61 9800 7409 10789 2799 630 -583 C ATOM 144 CG2 ILE A 61 11.674 32.805 0.661 1.00 62.38 C ANISOU 144 CG2 ILE A 61 8417 5842 9443 3146 300 -224 C ATOM 145 CD1 ILE A 61 11.034 32.873 3.571 1.00 63.68 C ANISOU 145 CD1 ILE A 61 8349 6153 9692 3089 719 -716 C ATOM 146 N LEU A 62 14.967 34.183 -0.166 1.00 71.27 N ANISOU 146 N LEU A 62 10370 6298 10410 2708 415 -22 N ATOM 147 CA LEU A 62 15.225 34.873 -1.424 1.00 69.04 C ANISOU 147 CA LEU A 62 10330 5775 10127 2819 341 222 C ATOM 148 C LEU A 62 16.422 34.276 -2.152 1.00 61.49 C ANISOU 148 C LEU A 62 9499 4863 9001 2540 319 355 C ATOM 149 O LEU A 62 16.381 34.085 -3.372 1.00 60.96 O ANISOU 149 O LEU A 62 9501 4833 8826 2614 194 575 O ATOM 150 CB LEU A 62 15.436 36.364 -1.153 1.00 64.37 C ANISOU 150 CB LEU A 62 9981 4769 9706 2902 471 189 C ATOM 151 CG LEU A 62 15.527 37.355 -2.314 1.00 65.71 C ANISOU 151 CG LEU A 62 10347 4711 9910 2974 401 434 C ATOM 152 CD1 LEU A 62 14.982 38.699 -1.866 1.00 77.27 C ANISOU 152 CD1 LEU A 62 11849 5913 11596 3132 457 345 C ATOM 153 CD2 LEU A 62 16.961 37.505 -2.798 1.00 64.99 C ANISOU 153 CD2 LEU A 62 10503 4453 9736 2680 487 541 C ATOM 154 N MET A 63 17.490 33.962 -1.422 1.00 76.47 N ANISOU 154 N MET A 63 11418 6774 10862 2231 434 216 N ATOM 155 CA MET A 63 18.759 33.609 -2.045 1.00 70.66 C ANISOU 155 CA MET A 63 10813 6021 10013 1968 453 320 C ATOM 156 C MET A 63 18.950 32.112 -2.255 1.00 73.32 C ANISOU 156 C MET A 63 10952 6717 10188 1813 356 328 C ATOM 157 O MET A 63 19.739 31.719 -3.121 1.00 78.81 O ANISOU 157 O MET A 63 11735 7438 10773 1676 338 458 O ATOM 158 CB MET A 63 19.918 34.145 -1.201 1.00 63.34 C ANISOU 158 CB MET A 63 10009 4895 9162 1715 616 158 C ATOM 159 CG MET A 63 20.128 35.648 -1.289 1.00116.50 C ANISOU 159 CG MET A 63 17010 11191 16065 1786 736 183 C ATOM 160 SD MET A 63 21.342 36.225 -0.086 1.00148.66 S ANISOU 160 SD MET A 63 21163 15068 20254 1479 902 -97 S ATOM 161 CE MET A 63 22.601 34.960 -0.245 1.00138.52 C ANISOU 161 CE MET A 63 19756 14069 18805 1136 868 -88 C ATOM 162 N VAL A 64 18.271 31.260 -1.485 1.00 58.51 N ANISOU 162 N VAL A 64 8819 5109 8302 1825 313 192 N ATOM 163 CA VAL A 64 18.590 29.836 -1.519 1.00 54.80 C ANISOU 163 CA VAL A 64 8180 4930 7710 1643 251 179 C ATOM 164 C VAL A 64 17.386 28.999 -1.936 1.00 61.87 C ANISOU 164 C VAL A 64 8849 6077 8582 1796 106 217 C ATOM 165 O VAL A 64 17.442 28.282 -2.942 1.00 53.01 O ANISOU 165 O VAL A 64 7702 5081 7357 1774 -12 328 O ATOM 166 CB VAL A 64 19.135 29.360 -0.160 1.00 55.14 C ANISOU 166 CB VAL A 64 8131 5073 7748 1440 345 -13 C ATOM 167 CG1 VAL A 64 19.797 28.006 -0.311 1.00 49.52 C ANISOU 167 CG1 VAL A 64 7312 4580 6923 1234 294 8 C ATOM 168 CG2 VAL A 64 20.114 30.371 0.412 1.00 51.96 C ANISOU 168 CG2 VAL A 64 7920 4417 7404 1321 471 -110 C ATOM 169 N ILE A 65 16.299 29.070 -1.163 1.00 55.97 N ANISOU 169 N ILE A 65 7922 5410 7935 1944 121 107 N ATOM 170 CA ILE A 65 15.161 28.177 -1.389 1.00 54.23 C ANISOU 170 CA ILE A 65 7426 5448 7729 2045 2 104 C ATOM 171 C ILE A 65 14.548 28.423 -2.761 1.00 56.13 C ANISOU 171 C ILE A 65 7689 5685 7951 2260 -183 260 C ATOM 172 O ILE A 65 14.340 27.488 -3.544 1.00 62.58 O ANISOU 172 O ILE A 65 8394 6697 8688 2227 -329 310 O ATOM 173 CB ILE A 65 14.118 28.337 -0.269 1.00 56.72 C ANISOU 173 CB ILE A 65 7538 5836 8175 2166 94 -49 C ATOM 174 CG1 ILE A 65 14.719 27.978 1.090 1.00 53.57 C ANISOU 174 CG1 ILE A 65 7133 5486 7736 1954 264 -195 C ATOM 175 CG2 ILE A 65 12.898 27.470 -0.552 1.00 68.99 C ANISOU 175 CG2 ILE A 65 8778 7648 9789 2262 -20 -57 C ATOM 176 CD1 ILE A 65 13.724 28.063 2.231 1.00 54.85 C ANISOU 176 CD1 ILE A 65 7108 5746 7987 2057 391 -347 C ATOM 177 N ILE A 66 14.237 29.686 -3.063 1.00 56.52 N ANISOU 177 N ILE A 66 7894 5511 8071 2494 -187 334 N ATOM 178 CA ILE A 66 13.656 30.016 -4.366 1.00 57.84 C ANISOU 178 CA ILE A 66 8115 5669 8194 2737 -380 509 C ATOM 179 C ILE A 66 14.572 29.625 -5.520 1.00 64.86 C ANISOU 179 C ILE A 66 9200 6568 8876 2602 -452 667 C ATOM 180 O ILE A 66 14.098 28.966 -6.460 1.00 72.36 O ANISOU 180 O ILE A 66 10055 7719 9718 2673 -646 730 O ATOM 181 CB ILE A 66 13.255 31.509 -4.402 1.00 68.24 C ANISOU 181 CB ILE A 66 9603 6692 9634 3021 -348 580 C ATOM 182 CG1 ILE A 66 12.006 31.755 -3.557 1.00 65.29 C ANISOU 182 CG1 ILE A 66 8964 6382 9461 3238 -332 427 C ATOM 183 CG2 ILE A 66 13.060 31.973 -5.831 1.00 84.99 C ANISOU 183 CG2 ILE A 66 11901 8741 11649 3242 -529 823 C ATOM 184 CD1 ILE A 66 11.582 33.200 -3.530 1.00 63.86 C ANISOU 184 CD1 ILE A 66 8938 5894 9431 3540 -294 475 C ATOM 185 N PRO A 67 15.867 29.976 -5.524 1.00 59.95 N ANISOU 185 N PRO A 67 8834 5751 8192 2405 -303 718 N ATOM 186 CA PRO A 67 16.732 29.515 -6.620 1.00 55.68 C ANISOU 186 CA PRO A 67 8452 5251 7452 2271 -342 854 C ATOM 187 C PRO A 67 16.907 28.006 -6.664 1.00 54.01 C ANISOU 187 C PRO A 67 8036 5333 7151 2074 -407 756 C ATOM 188 O PRO A 67 17.191 27.464 -7.740 1.00 55.24 O ANISOU 188 O PRO A 67 8258 5596 7134 2042 -501 845 O ATOM 189 CB PRO A 67 18.066 30.223 -6.340 1.00 55.25 C ANISOU 189 CB PRO A 67 8651 4924 7419 2074 -128 881 C ATOM 190 CG PRO A 67 17.703 31.395 -5.498 1.00 62.53 C ANISOU 190 CG PRO A 67 9630 5596 8531 2204 -30 822 C ATOM 191 CD PRO A 67 16.584 30.909 -4.636 1.00 56.24 C ANISOU 191 CD PRO A 67 8530 5004 7836 2312 -96 653 C ATOM 192 N THR A 68 16.752 27.314 -5.536 1.00 52.72 N ANISOU 192 N THR A 68 7644 5293 7094 1947 -350 578 N ATOM 193 CA THR A 68 16.836 25.858 -5.534 1.00 52.81 C ANISOU 193 CA THR A 68 7462 5551 7053 1774 -406 494 C ATOM 194 C THR A 68 15.626 25.242 -6.222 1.00 54.82 C ANISOU 194 C THR A 68 7512 6021 7296 1928 -618 487 C ATOM 195 O THR A 68 15.765 24.462 -7.173 1.00 77.03 O ANISOU 195 O THR A 68 10323 8968 9977 1878 -738 513 O ATOM 196 CB THR A 68 16.961 25.344 -4.100 1.00 57.47 C ANISOU 196 CB THR A 68 7890 6195 7750 1613 -278 337 C ATOM 197 OG1 THR A 68 18.175 25.834 -3.522 1.00 53.05 O ANISOU 197 OG1 THR A 68 7507 5465 7183 1454 -120 321 O ATOM 198 CG2 THR A 68 16.965 23.824 -4.075 1.00 72.40 C ANISOU 198 CG2 THR A 68 9586 8306 9614 1450 -330 270 C ATOM 199 N ILE A 69 14.425 25.583 -5.750 1.00 54.52 N ANISOU 199 N ILE A 69 7287 6025 7403 2117 -664 430 N ATOM 200 CA ILE A 69 13.202 25.033 -6.333 1.00 66.46 C ANISOU 200 CA ILE A 69 8551 7755 8946 2263 -877 395 C ATOM 201 C ILE A 69 13.102 25.406 -7.806 1.00 61.31 C ANISOU 201 C ILE A 69 8064 7110 8122 2443 -1080 544 C ATOM 202 O ILE A 69 12.879 24.549 -8.668 1.00 70.13 O ANISOU 202 O ILE A 69 9096 8421 9129 2418 -1258 522 O ATOM 203 CB ILE A 69 11.966 25.514 -5.549 1.00 74.56 C ANISOU 203 CB ILE A 69 9341 8807 10183 2458 -866 310 C ATOM 204 CG1 ILE A 69 12.038 25.054 -4.093 1.00 54.97 C ANISOU 204 CG1 ILE A 69 6708 6353 7825 2273 -651 166 C ATOM 205 CG2 ILE A 69 10.688 25.011 -6.209 1.00 64.59 C ANISOU 205 CG2 ILE A 69 7787 7777 8979 2616 -1105 264 C ATOM 206 CD1 ILE A 69 10.842 25.477 -3.272 1.00 56.23 C ANISOU 206 CD1 ILE A 69 6625 6555 8184 2450 -593 65 C ATOM 207 N GLY A 70 13.270 26.694 -8.113 1.00 57.40 N ANISOU 207 N GLY A 70 7824 6395 7591 2629 -1055 697 N ATOM 208 CA GLY A 70 13.191 27.132 -9.498 1.00 64.35 C ANISOU 208 CA GLY A 70 8907 7268 8274 2822 -1235 878 C ATOM 209 C GLY A 70 14.275 26.522 -10.366 1.00 64.66 C ANISOU 209 C GLY A 70 9149 7351 8069 2624 -1220 943 C ATOM 210 O GLY A 70 14.004 26.022 -11.461 1.00 71.59 O ANISOU 210 O GLY A 70 10034 8411 8758 2693 -1422 976 O ATOM 211 N GLY A 71 15.519 26.546 -9.880 1.00 60.33 N ANISOU 211 N GLY A 71 8755 6647 7520 2378 -981 943 N ATOM 212 CA GLY A 71 16.629 26.034 -10.667 1.00 59.83 C ANISOU 212 CA GLY A 71 8877 6609 7248 2193 -927 999 C ATOM 213 C GLY A 71 16.540 24.546 -10.935 1.00 60.40 C ANISOU 213 C GLY A 71 8742 6950 7257 2049 -1037 847 C ATOM 214 O GLY A 71 17.005 24.072 -11.974 1.00 75.54 O ANISOU 214 O GLY A 71 10786 8961 8957 2003 -1091 886 O ATOM 215 N ASN A 72 15.943 23.790 -10.011 1.00 57.76 N ANISOU 215 N ASN A 72 8099 6733 7114 1973 -1056 670 N ATOM 216 CA ASN A 72 15.801 22.352 -10.216 1.00 62.53 C ANISOU 216 CA ASN A 72 8500 7554 7702 1828 -1152 520 C ATOM 217 C ASN A 72 14.576 22.025 -11.060 1.00 64.09 C ANISOU 217 C ASN A 72 8538 7962 7850 2009 -1436 474 C ATOM 218 O ASN A 72 14.637 21.147 -11.928 1.00 63.25 O ANISOU 218 O ASN A 72 8418 8013 7601 1948 -1566 405 O ATOM 219 CB ASN A 72 15.732 21.631 -8.871 1.00 58.55 C ANISOU 219 CB ASN A 72 7754 7070 7422 1650 -1029 372 C ATOM 220 CG ASN A 72 17.053 21.657 -8.128 1.00 75.50 C ANISOU 220 CG ASN A 72 10036 9067 9584 1444 -796 384 C ATOM 221 OD1 ASN A 72 18.118 21.466 -8.718 1.00 55.84 O ANISOU 221 OD1 ASN A 72 7720 6539 6958 1332 -738 428 O ATOM 222 ND2 ASN A 72 16.990 21.900 -6.826 1.00107.10 N ANISOU 222 ND2 ASN A 72 13948 12998 13746 1398 -664 334 N ATOM 223 N THR A 73 13.456 22.711 -10.819 1.00 67.72 N ANISOU 223 N THR A 73 8861 8435 8434 2237 -1544 490 N ATOM 224 CA THR A 73 12.288 22.527 -11.673 1.00 74.85 C ANISOU 224 CA THR A 73 9600 9549 9292 2440 -1847 449 C ATOM 225 C THR A 73 12.595 22.892 -13.118 1.00 72.11 C ANISOU 225 C THR A 73 9546 9235 8617 2585 -2005 597 C ATOM 226 O THR A 73 11.989 22.333 -14.040 1.00 68.74 O ANISOU 226 O THR A 73 9026 9033 8060 2665 -2269 524 O ATOM 227 CB THR A 73 11.114 23.357 -11.154 1.00 62.07 C ANISOU 227 CB THR A 73 7792 7916 7875 2695 -1918 458 C ATOM 228 OG1 THR A 73 11.566 24.681 -10.846 1.00 61.04 O ANISOU 228 OG1 THR A 73 7927 7522 7743 2821 -1760 632 O ATOM 229 CG2 THR A 73 10.519 22.724 -9.906 1.00 70.63 C ANISOU 229 CG2 THR A 73 8516 9063 9256 2559 -1807 273 C ATOM 230 N LEU A 74 13.534 23.816 -13.337 1.00 70.59 N ANISOU 230 N LEU A 74 9712 8826 8283 2610 -1841 800 N ATOM 231 CA LEU A 74 13.947 24.149 -14.698 1.00 63.76 C ANISOU 231 CA LEU A 74 9169 7982 7076 2723 -1936 970 C ATOM 232 C LEU A 74 14.606 22.955 -15.377 1.00 62.22 C ANISOU 232 C LEU A 74 9003 7952 6686 2509 -1947 852 C ATOM 233 O LEU A 74 14.317 22.651 -16.540 1.00 71.68 O ANISOU 233 O LEU A 74 10275 9341 7619 2617 -2166 851 O ATOM 234 CB LEU A 74 14.894 25.350 -14.685 1.00 62.67 C ANISOU 234 CB LEU A 74 9398 7543 6872 2742 -1697 1210 C ATOM 235 CG LEU A 74 14.261 26.741 -14.668 1.00 67.34 C ANISOU 235 CG LEU A 74 10110 7953 7521 3053 -1748 1404 C ATOM 236 CD1 LEU A 74 15.339 27.812 -14.648 1.00 80.81 C ANISOU 236 CD1 LEU A 74 12189 9328 9188 3004 -1474 1620 C ATOM 237 CD2 LEU A 74 13.358 26.910 -15.874 1.00 70.84 C ANISOU 237 CD2 LEU A 74 10604 8579 7732 3366 -2079 1511 C ATOM 238 N VAL A 75 15.500 22.268 -14.663 1.00 64.77 N ANISOU 238 N VAL A 75 9273 8206 7130 2217 -1717 742 N ATOM 239 CA VAL A 75 16.176 21.108 -15.238 1.00 62.08 C ANISOU 239 CA VAL A 75 8952 7993 6643 2019 -1702 614 C ATOM 240 C VAL A 75 15.186 19.973 -15.468 1.00 64.18 C ANISOU 240 C VAL A 75 8917 8507 6962 2011 -1957 382 C ATOM 241 O VAL A 75 15.203 19.321 -16.519 1.00 72.83 O ANISOU 241 O VAL A 75 10070 9774 7828 2009 -2106 296 O ATOM 242 CB VAL A 75 17.343 20.668 -14.336 1.00 59.35 C ANISOU 242 CB VAL A 75 8597 7503 6451 1738 -1410 557 C ATOM 243 CG1 VAL A 75 18.079 19.492 -14.959 1.00 59.55 C ANISOU 243 CG1 VAL A 75 8647 7637 6341 1560 -1383 425 C ATOM 244 CG2 VAL A 75 18.289 21.834 -14.091 1.00 59.35 C ANISOU 244 CG2 VAL A 75 8862 7256 6430 1729 -1171 758 C ATOM 245 N ILE A 76 14.309 19.723 -14.493 1.00 66.24 N ANISOU 245 N ILE A 76 8852 8791 7527 1997 -1999 265 N ATOM 246 CA ILE A 76 13.303 18.674 -14.640 1.00 65.99 C ANISOU 246 CA ILE A 76 8495 8974 7602 1965 -2225 37 C ATOM 247 C ILE A 76 12.407 18.962 -15.836 1.00 70.45 C ANISOU 247 C ILE A 76 9071 9742 7954 2220 -2565 42 C ATOM 248 O ILE A 76 12.111 18.069 -16.638 1.00 94.55 O ANISOU 248 O ILE A 76 12040 12992 10891 2179 -2770 -135 O ATOM 249 CB ILE A 76 12.488 18.527 -13.342 1.00 63.60 C ANISOU 249 CB ILE A 76 7848 8647 7669 1918 -2168 -54 C ATOM 250 CG1 ILE A 76 13.402 18.141 -12.178 1.00 75.79 C ANISOU 250 CG1 ILE A 76 9400 10019 9376 1669 -1857 -60 C ATOM 251 CG2 ILE A 76 11.379 17.498 -13.517 1.00 62.09 C ANISOU 251 CG2 ILE A 76 7297 8669 7626 1874 -2392 -288 C ATOM 252 CD1 ILE A 76 12.672 17.988 -10.864 1.00 78.98 C ANISOU 252 CD1 ILE A 76 9506 10404 10099 1615 -1763 -133 C ATOM 253 N LEU A 77 11.969 20.217 -15.979 1.00 76.69 N ANISOU 253 N LEU A 77 9970 10481 8687 2497 -2641 239 N ATOM 254 CA LEU A 77 11.195 20.604 -17.156 1.00 72.01 C ANISOU 254 CA LEU A 77 9433 10077 7849 2782 -2980 289 C ATOM 255 C LEU A 77 12.004 20.417 -18.433 1.00 79.15 C ANISOU 255 C LEU A 77 10689 11058 8326 2774 -3020 350 C ATOM 256 O LEU A 77 11.462 19.997 -19.462 1.00 71.82 O ANISOU 256 O LEU A 77 9739 10379 7172 2881 -3324 247 O ATOM 257 CB LEU A 77 10.731 22.055 -17.029 1.00 68.78 C ANISOU 257 CB LEU A 77 9128 9542 7462 3096 -3013 531 C ATOM 258 CG LEU A 77 9.530 22.339 -16.129 1.00 70.95 C ANISOU 258 CG LEU A 77 9023 9834 8099 3228 -3093 451 C ATOM 259 CD1 LEU A 77 9.361 23.836 -15.940 1.00 91.13 C ANISOU 259 CD1 LEU A 77 11752 12179 10693 3479 -3012 701 C ATOM 260 CD2 LEU A 77 8.278 21.730 -16.731 1.00 85.25 C ANISOU 260 CD2 LEU A 77 10501 11941 9950 3286 -3414 258 C ATOM 261 N ALA A 78 13.304 20.718 -18.384 1.00 73.81 N ANISOU 261 N ALA A 78 10330 10182 7532 2644 -2712 501 N ATOM 262 CA ALA A 78 14.138 20.608 -19.578 1.00 70.60 C ANISOU 262 CA ALA A 78 10272 9840 6715 2633 -2691 574 C ATOM 263 C ALA A 78 14.222 19.165 -20.058 1.00 71.00 C ANISOU 263 C ALA A 78 10191 10097 6688 2445 -2789 278 C ATOM 264 O ALA A 78 14.092 18.887 -21.256 1.00 80.12 O ANISOU 264 O ALA A 78 11486 11462 7494 2542 -2995 227 O ATOM 265 CB ALA A 78 15.533 21.169 -19.299 1.00 65.91 C ANISOU 265 CB ALA A 78 9978 8981 6084 2493 -2304 767 C ATOM 266 N VAL A 79 14.436 18.229 -19.134 1.00 90.62 N ANISOU 266 N VAL A 79 12421 12520 9490 2182 -2644 77 N ATOM 267 CA VAL A 79 14.509 16.821 -19.511 1.00 71.41 C ANISOU 267 CA VAL A 79 9857 10235 7043 1994 -2720 -216 C ATOM 268 C VAL A 79 13.130 16.297 -19.896 1.00 71.01 C ANISOU 268 C VAL A 79 9512 10430 7039 2090 -3103 -434 C ATOM 269 O VAL A 79 12.997 15.476 -20.811 1.00 68.87 O ANISOU 269 O VAL A 79 9242 10352 6574 2057 -3293 -646 O ATOM 270 CB VAL A 79 15.133 15.998 -18.368 1.00 70.34 C ANISOU 270 CB VAL A 79 9548 9930 7248 1703 -2451 -333 C ATOM 271 CG1 VAL A 79 15.292 14.540 -18.779 1.00 72.17 C ANISOU 271 CG1 VAL A 79 9675 10263 7482 1513 -2503 -627 C ATOM 272 CG2 VAL A 79 16.471 16.596 -17.957 1.00 67.02 C ANISOU 272 CG2 VAL A 79 9381 9284 6798 1621 -2103 -129 C ATOM 273 N SER A 80 12.082 16.775 -19.220 1.00 85.89 N ANISOU 273 N SER A 80 11130 12319 9186 2211 -3223 -404 N ATOM 274 CA SER A 80 10.745 16.233 -19.449 1.00 82.42 C ANISOU 274 CA SER A 80 10332 12111 8871 2273 -3571 -638 C ATOM 275 C SER A 80 10.189 16.665 -20.800 1.00 90.96 C ANISOU 275 C SER A 80 11553 13417 9589 2523 -3890 -602 C ATOM 276 O SER A 80 9.583 15.857 -21.514 1.00100.21 O ANISOU 276 O SER A 80 12568 14781 10724 2448 -4091 -841 O ATOM 277 CB SER A 80 9.804 16.661 -18.323 1.00 80.52 C ANISOU 277 CB SER A 80 9751 11812 9031 2332 -3563 -611 C ATOM 278 OG SER A 80 10.266 16.196 -17.066 1.00102.24 O ANISOU 278 OG SER A 80 12378 14362 12106 2073 -3238 -644 O ATOM 279 N LEU A 81 10.384 17.930 -21.169 1.00 93.58 N ANISOU 279 N LEU A 81 12184 13671 9703 2748 -3839 -285 N ATOM 280 CA LEU A 81 9.777 18.481 -22.377 1.00 95.42 C ANISOU 280 CA LEU A 81 12540 14056 9660 2943 -4043 -189 C ATOM 281 C LEU A 81 10.626 18.216 -23.617 1.00 89.96 C ANISOU 281 C LEU A 81 12221 13454 8506 2910 -4022 -172 C ATOM 282 O LEU A 81 10.135 17.658 -24.605 1.00118.12 O ANISOU 282 O LEU A 81 15744 17243 11892 2906 -4242 -343 O ATOM 283 CB LEU A 81 9.541 19.985 -22.202 1.00 89.83 C ANISOU 283 CB LEU A 81 11973 13195 8963 3196 -3986 149 C ATOM 284 CG LEU A 81 8.587 20.398 -21.081 1.00 76.31 C ANISOU 284 CG LEU A 81 9901 11407 7685 3273 -4004 139 C ATOM 285 CD1 LEU A 81 8.454 21.910 -21.029 1.00 87.17 C ANISOU 285 CD1 LEU A 81 11470 12606 9047 3525 -3932 466 C ATOM 286 CD2 LEU A 81 7.229 19.744 -21.268 1.00 78.25 C ANISOU 286 CD2 LEU A 81 9721 11894 8116 3267 -4289 -118 C ATOM 287 N GLU A 82 11.895 18.619 -23.582 1.00 80.21 N ANISOU 287 N GLU A 82 11349 12047 7079 2879 -3742 28 N ATOM 288 CA GLU A 82 12.772 18.492 -24.741 1.00 93.84 C ANISOU 288 CA GLU A 82 13448 13844 8362 2850 -3656 77 C ATOM 289 C GLU A 82 12.941 17.034 -25.149 1.00106.04 C ANISOU 289 C GLU A 82 14885 15562 9844 2644 -3732 -291 C ATOM 290 O GLU A 82 13.613 16.261 -24.458 1.00 78.38 O ANISOU 290 O GLU A 82 11314 11971 6495 2448 -3579 -451 O ATOM 291 CB GLU A 82 14.135 19.125 -24.451 1.00 79.92 C ANISOU 291 CB GLU A 82 12044 11840 6483 2809 -3288 338 C ATOM 292 N LYS A 83 12.326 16.652 -26.272 1.00135.61 N ANISOU 292 N LYS A 83 18613 19543 13368 2687 -3973 -434 N ATOM 293 CA LYS A 83 12.436 15.279 -26.752 1.00111.81 C ANISOU 293 CA LYS A 83 15507 16678 10299 2490 -4045 -802 C ATOM 294 C LYS A 83 13.857 14.947 -27.189 1.00101.56 C ANISOU 294 C LYS A 83 14555 15328 8705 2374 -3762 -800 C ATOM 295 O LYS A 83 14.268 13.783 -27.118 1.00111.84 O ANISOU 295 O LYS A 83 15772 16642 10079 2169 -3706 -1102 O ATOM 296 CB LYS A 83 11.453 15.041 -27.899 1.00115.37 C ANISOU 296 CB LYS A 83 15886 17391 10558 2576 -4370 -943 C ATOM 297 N LYS A 84 14.621 15.947 -27.637 1.00108.33 N ANISOU 297 N LYS A 84 15794 16110 9256 2490 -3558 -466 N ATOM 298 CA LYS A 84 16.005 15.741 -28.049 1.00102.69 C ANISOU 298 CA LYS A 84 15406 15342 8271 2379 -3238 -435 C ATOM 299 C LYS A 84 16.963 15.611 -26.873 1.00 92.59 C ANISOU 299 C LYS A 84 14118 13827 7234 2238 -2944 -413 C ATOM 300 O LYS A 84 18.127 15.252 -27.084 1.00 89.79 O ANISOU 300 O LYS A 84 13970 13425 6720 2116 -2664 -449 O ATOM 301 CB LYS A 84 16.460 16.887 -28.959 1.00 93.88 C ANISOU 301 CB LYS A 84 14684 14217 6768 2530 -3094 -72 C ATOM 302 N LEU A 85 16.507 15.886 -25.650 1.00 85.41 N ANISOU 302 N LEU A 85 12971 12779 6703 2252 -2994 -362 N ATOM 303 CA LEU A 85 17.323 15.783 -24.446 1.00 91.08 C ANISOU 303 CA LEU A 85 13575 13212 7818 2031 -2641 -322 C ATOM 304 C LEU A 85 17.147 14.462 -23.710 1.00 86.01 C ANISOU 304 C LEU A 85 12567 12541 7571 1794 -2655 -661 C ATOM 305 O LEU A 85 17.749 14.275 -22.649 1.00 69.46 O ANISOU 305 O LEU A 85 10347 10223 5823 1613 -2389 -639 O ATOM 306 CB LEU A 85 16.992 16.927 -23.488 1.00 95.50 C ANISOU 306 CB LEU A 85 14069 13576 8641 2128 -2585 -41 C ATOM 307 CG LEU A 85 17.839 18.192 -23.577 1.00 79.39 C ANISOU 307 CG LEU A 85 12379 11347 6437 2205 -2309 330 C ATOM 308 CD1 LEU A 85 17.472 19.146 -22.448 1.00 74.97 C ANISOU 308 CD1 LEU A 85 11695 10565 6224 2263 -2253 523 C ATOM 309 CD2 LEU A 85 19.313 17.836 -23.536 1.00 68.90 C ANISOU 309 CD2 LEU A 85 11196 9889 5093 1971 -1917 318 C ATOM 310 N GLN A 86 16.352 13.544 -24.246 1.00111.00 N ANISOU 310 N GLN A 86 15565 15918 10691 1790 -2958 -971 N ATOM 311 CA GLN A 86 15.951 12.343 -23.527 1.00108.26 C ANISOU 311 CA GLN A 86 14848 15525 10761 1576 -3005 -1279 C ATOM 312 C GLN A 86 16.900 11.190 -23.813 1.00101.79 C ANISOU 312 C GLN A 86 14096 14660 9922 1371 -2816 -1520 C ATOM 313 O GLN A 86 16.871 10.623 -24.912 1.00 90.37 O ANISOU 313 O GLN A 86 12768 13404 8163 1397 -2966 -1744 O ATOM 314 CB GLN A 86 14.543 11.940 -23.932 1.00 86.30 C ANISOU 314 CB GLN A 86 11812 12979 7997 1658 -3438 -1517 C ATOM 315 CG GLN A 86 13.490 12.945 -23.600 1.00 87.24 C ANISOU 315 CG GLN A 86 11791 13153 8202 1871 -3649 -1326 C ATOM 316 CD GLN A 86 12.148 12.511 -24.133 1.00134.94 C ANISOU 316 CD GLN A 86 17549 19396 14324 1893 -3977 -1539 C ATOM 317 OE1 GLN A 86 12.074 11.792 -25.135 1.00152.42 O ANISOU 317 OE1 GLN A 86 19814 21754 16345 1830 -4083 -1753 O ATOM 318 NE2 GLN A 86 11.078 12.925 -23.464 1.00142.96 N ANISOU 318 NE2 GLN A 86 18256 20412 15649 1967 -4106 -1487 N ATOM 319 N TYR A 87 17.710 10.820 -22.816 1.00 89.61 N ANISOU 319 N TYR A 87 12467 12868 8711 1180 -2503 -1491 N ATOM 320 CA TYR A 87 18.593 9.665 -22.942 1.00 91.92 C ANISOU 320 CA TYR A 87 12779 13081 9066 996 -2319 -1723 C ATOM 321 C TYR A 87 19.321 9.330 -21.645 1.00 93.48 C ANISOU 321 C TYR A 87 12832 13002 9684 817 -2023 -1654 C ATOM 322 O TYR A 87 19.036 9.891 -20.577 1.00 79.21 O ANISOU 322 O TYR A 87 10882 11075 8137 812 -1977 -1464 O ATOM 323 CB TYR A 87 19.610 9.868 -24.073 1.00104.81 C ANISOU 323 CB TYR A 87 14777 14804 10242 1063 -2164 -1692 C ATOM 324 CG TYR A 87 20.224 11.253 -24.181 1.00110.09 C ANISOU 324 CG TYR A 87 15719 15436 10673 1192 -1976 -1309 C ATOM 325 CD1 TYR A 87 19.546 12.292 -24.802 1.00115.27 C ANISOU 325 CD1 TYR A 87 16539 16247 11011 1415 -2180 -1112 C ATOM 326 CD2 TYR A 87 21.502 11.506 -23.710 1.00111.65 C ANISOU 326 CD2 TYR A 87 16015 15442 10967 1092 -1597 -1150 C ATOM 327 CE1 TYR A 87 20.098 13.545 -24.913 1.00116.79 C ANISOU 327 CE1 TYR A 87 16999 16367 11009 1524 -1993 -755 C ATOM 328 CE2 TYR A 87 22.073 12.767 -23.826 1.00109.03 C ANISOU 328 CE2 TYR A 87 15926 15054 10445 1181 -1410 -816 C ATOM 329 CZ TYR A 87 21.364 13.783 -24.429 1.00112.77 C ANISOU 329 CZ TYR A 87 16579 15651 10619 1392 -1598 -613 C ATOM 330 OH TYR A 87 21.920 15.041 -24.549 1.00112.54 O ANISOU 330 OH TYR A 87 16811 15527 10423 1474 -1397 -268 O ATOM 331 N ALA A 88 20.285 8.416 -21.766 1.00106.02 N ANISOU 331 N ALA A 88 14468 14497 11318 687 -1825 -1816 N ATOM 332 CA ALA A 88 20.797 7.672 -20.618 1.00 92.51 C ANISOU 332 CA ALA A 88 12570 12545 10035 512 -1627 -1847 C ATOM 333 C ALA A 88 21.315 8.590 -19.514 1.00 83.27 C ANISOU 333 C ALA A 88 11392 11219 9027 512 -1420 -1528 C ATOM 334 O ALA A 88 20.965 8.423 -18.340 1.00105.50 O ANISOU 334 O ALA A 88 13993 13904 12189 432 -1404 -1477 O ATOM 335 CB ALA A 88 21.898 6.713 -21.089 1.00109.77 C ANISOU 335 CB ALA A 88 14856 14665 12188 427 -1433 -2043 C ATOM 336 N THR A 89 22.193 9.533 -19.861 1.00 75.60 N ANISOU 336 N THR A 89 10659 10255 7812 587 -1241 -1322 N ATOM 337 CA THR A 89 22.847 10.338 -18.833 1.00 91.05 C ANISOU 337 CA THR A 89 12611 12048 9937 559 -1028 -1064 C ATOM 338 C THR A 89 21.880 11.339 -18.204 1.00 93.33 C ANISOU 338 C THR A 89 12826 12337 10299 649 -1162 -875 C ATOM 339 O THR A 89 21.933 11.582 -16.992 1.00 95.16 O ANISOU 339 O THR A 89 12925 12428 10805 591 -1071 -765 O ATOM 340 CB THR A 89 24.065 11.051 -19.414 1.00 78.95 C ANISOU 340 CB THR A 89 11336 10508 8155 587 -782 -917 C ATOM 341 N ASN A 90 20.988 11.931 -19.006 1.00 76.04 N ANISOU 341 N ASN A 90 10723 10310 7859 808 -1383 -840 N ATOM 342 CA ASN A 90 20.060 12.931 -18.484 1.00 71.18 C ANISOU 342 CA ASN A 90 10038 9693 7314 929 -1510 -664 C ATOM 343 C ASN A 90 19.087 12.350 -17.467 1.00 71.03 C ANISOU 343 C ASN A 90 9686 9643 7660 857 -1630 -777 C ATOM 344 O ASN A 90 18.567 13.096 -16.631 1.00 81.13 O ANISOU 344 O ASN A 90 10867 10861 9096 914 -1635 -633 O ATOM 345 CB ASN A 90 19.286 13.577 -19.632 1.00 76.77 C ANISOU 345 CB ASN A 90 10898 10596 7674 1141 -1754 -615 C ATOM 346 CG ASN A 90 20.191 14.297 -20.611 1.00 88.71 C ANISOU 346 CG ASN A 90 12774 12131 8799 1224 -1608 -446 C ATOM 347 OD1 ASN A 90 21.384 14.007 -20.698 1.00101.30 O ANISOU 347 OD1 ASN A 90 14482 13646 10362 1102 -1346 -458 O ATOM 348 ND2 ASN A 90 19.628 15.242 -21.354 1.00104.32 N ANISOU 348 ND2 ASN A 90 14935 14217 10487 1439 -1767 -279 N ATOM 349 N TYR A 91 18.825 11.042 -17.521 1.00 75.30 N ANISOU 349 N TYR A 91 10055 10212 8344 730 -1708 -1036 N ATOM 350 CA TYR A 91 17.979 10.413 -16.511 1.00 69.61 C ANISOU 350 CA TYR A 91 9021 9436 7993 627 -1768 -1131 C ATOM 351 C TYR A 91 18.636 10.481 -15.137 1.00 68.15 C ANISOU 351 C TYR A 91 8780 9046 8069 520 -1513 -988 C ATOM 352 O TYR A 91 17.989 10.831 -14.142 1.00 79.38 O ANISOU 352 O TYR A 91 10037 10425 9698 523 -1509 -902 O ATOM 353 CB TYR A 91 17.679 8.967 -16.902 1.00 73.15 C ANISOU 353 CB TYR A 91 9326 9914 8553 491 -1874 -1437 C ATOM 354 N PHE A 92 19.929 10.155 -15.068 1.00 66.06 N ANISOU 354 N PHE A 92 8646 8667 7785 434 -1301 -970 N ATOM 355 CA PHE A 92 20.667 10.269 -13.814 1.00 60.97 C ANISOU 355 CA PHE A 92 7966 7852 7347 350 -1084 -834 C ATOM 356 C PHE A 92 20.731 11.719 -13.352 1.00 72.60 C ANISOU 356 C PHE A 92 9533 9300 8753 452 -1021 -602 C ATOM 357 O PHE A 92 20.507 12.021 -12.174 1.00 74.81 O ANISOU 357 O PHE A 92 9700 9499 9224 427 -958 -511 O ATOM 358 CB PHE A 92 22.071 9.694 -13.992 1.00 63.94 C ANISOU 358 CB PHE A 92 8454 8139 7702 268 -897 -874 C ATOM 359 CG PHE A 92 22.702 9.226 -12.716 1.00 53.84 C ANISOU 359 CG PHE A 92 7068 6699 6691 159 -739 -821 C ATOM 360 CD1 PHE A 92 22.148 8.179 -12.001 1.00 58.98 C ANISOU 360 CD1 PHE A 92 7528 7276 7604 64 -775 -910 C ATOM 361 CD2 PHE A 92 23.861 9.817 -12.244 1.00 52.49 C ANISOU 361 CD2 PHE A 92 6988 6449 6508 151 -557 -682 C ATOM 362 CE1 PHE A 92 22.729 7.740 -10.831 1.00 69.99 C ANISOU 362 CE1 PHE A 92 8853 8529 9210 -15 -639 -835 C ATOM 363 CE2 PHE A 92 24.447 9.381 -11.077 1.00 58.24 C ANISOU 363 CE2 PHE A 92 7619 7054 7455 71 -447 -636 C ATOM 364 CZ PHE A 92 23.881 8.341 -10.368 1.00 60.18 C ANISOU 364 CZ PHE A 92 7703 7234 7927 0 -490 -701 C ATOM 365 N LEU A 93 21.037 12.633 -14.278 1.00 71.23 N ANISOU 365 N LEU A 93 9581 9185 8300 568 -1024 -504 N ATOM 366 CA LEU A 93 21.049 14.055 -13.955 1.00 74.34 C ANISOU 366 CA LEU A 93 10087 9524 8637 672 -968 -287 C ATOM 367 C LEU A 93 19.698 14.507 -13.415 1.00 57.90 C ANISOU 367 C LEU A 93 7843 7480 6677 773 -1126 -258 C ATOM 368 O LEU A 93 19.632 15.311 -12.479 1.00 70.21 O ANISOU 368 O LEU A 93 9380 8941 8357 800 -1041 -135 O ATOM 369 CB LEU A 93 21.433 14.859 -15.196 1.00 66.24 C ANISOU 369 CB LEU A 93 9338 8553 7277 788 -962 -181 C ATOM 370 CG LEU A 93 21.604 16.364 -15.028 1.00 57.80 C ANISOU 370 CG LEU A 93 8441 7381 6141 890 -873 59 C ATOM 371 CD1 LEU A 93 22.641 16.648 -13.958 1.00 56.08 C ANISOU 371 CD1 LEU A 93 8209 6986 6115 753 -631 124 C ATOM 372 CD2 LEU A 93 22.009 16.983 -16.352 1.00 59.11 C ANISOU 372 CD2 LEU A 93 8901 7597 5959 990 -847 174 C ATOM 373 N MET A 94 18.609 13.987 -13.986 1.00 56.00 N ANISOU 373 N MET A 94 7470 7389 6419 830 -1357 -394 N ATOM 374 CA MET A 94 17.277 14.324 -13.496 1.00 56.55 C ANISOU 374 CA MET A 94 7331 7516 6638 926 -1508 -394 C ATOM 375 C MET A 94 17.027 13.750 -12.106 1.00 55.93 C ANISOU 375 C MET A 94 7012 7352 6888 784 -1397 -441 C ATOM 376 O MET A 94 16.343 14.380 -11.292 1.00 54.44 O ANISOU 376 O MET A 94 6705 7143 6836 852 -1386 -371 O ATOM 377 CB MET A 94 16.219 13.832 -14.483 1.00 59.11 C ANISOU 377 CB MET A 94 7540 8040 6879 1004 -1796 -557 C ATOM 378 CG MET A 94 14.788 14.099 -14.059 1.00 74.26 C ANISOU 378 CG MET A 94 9189 10047 8981 1106 -1969 -588 C ATOM 379 SD MET A 94 13.605 13.582 -15.315 1.00 87.40 S ANISOU 379 SD MET A 94 10704 11973 10531 1205 -2350 -801 S ATOM 380 CE MET A 94 13.942 11.824 -15.403 1.00107.70 C ANISOU 380 CE MET A 94 13155 14527 13238 923 -2315 -1081 C ATOM 381 N SER A 95 17.571 12.563 -11.817 1.00 54.36 N ANISOU 381 N SER A 95 6750 7095 6809 600 -1305 -553 N ATOM 382 CA SER A 95 17.492 12.021 -10.463 1.00 54.22 C ANISOU 382 CA SER A 95 6558 6978 7066 467 -1170 -553 C ATOM 383 C SER A 95 18.143 12.970 -9.466 1.00 55.78 C ANISOU 383 C SER A 95 6857 7062 7272 489 -987 -376 C ATOM 384 O SER A 95 17.592 13.238 -8.392 1.00 52.16 O ANISOU 384 O SER A 95 6272 6579 6967 490 -928 -331 O ATOM 385 CB SER A 95 18.151 10.642 -10.410 1.00 56.54 C ANISOU 385 CB SER A 95 6823 7196 7464 291 -1094 -670 C ATOM 386 OG SER A 95 18.161 10.121 -9.091 1.00 49.70 O ANISOU 386 OG SER A 95 5829 6223 6833 174 -954 -631 O ATOM 387 N LEU A 96 19.318 13.498 -9.817 1.00 54.18 N ANISOU 387 N LEU A 96 6883 6796 6908 501 -889 -290 N ATOM 388 CA LEU A 96 19.985 14.480 -8.970 1.00 50.47 C ANISOU 388 CA LEU A 96 6515 6216 6444 513 -733 -149 C ATOM 389 C LEU A 96 19.118 15.718 -8.777 1.00 50.28 C ANISOU 389 C LEU A 96 6496 6201 6407 672 -785 -61 C ATOM 390 O LEU A 96 18.912 16.174 -7.648 1.00 52.61 O ANISOU 390 O LEU A 96 6727 6439 6824 673 -699 -20 O ATOM 391 CB LEU A 96 21.336 14.856 -9.578 1.00 57.65 C ANISOU 391 CB LEU A 96 7647 7064 7193 489 -625 -89 C ATOM 392 CG LEU A 96 22.048 16.055 -8.957 1.00 55.26 C ANISOU 392 CG LEU A 96 7471 6642 6882 500 -483 41 C ATOM 393 CD1 LEU A 96 22.372 15.774 -7.502 1.00 54.94 C ANISOU 393 CD1 LEU A 96 7316 6539 7021 398 -383 30 C ATOM 394 CD2 LEU A 96 23.307 16.391 -9.739 1.00 64.90 C ANISOU 394 CD2 LEU A 96 8887 7813 7958 462 -369 90 C ATOM 395 N ALA A 97 18.598 16.275 -9.876 1.00 52.84 N ANISOU 395 N ALA A 97 6903 6598 6574 823 -930 -34 N ATOM 396 CA ALA A 97 17.760 17.467 -9.781 1.00 53.41 C ANISOU 396 CA ALA A 97 6986 6664 6644 1011 -994 58 C ATOM 397 C ALA A 97 16.535 17.212 -8.913 1.00 61.17 C ANISOU 397 C ALA A 97 7686 7710 7844 1034 -1047 -20 C ATOM 398 O ALA A 97 16.094 18.097 -8.170 1.00 60.85 O ANISOU 398 O ALA A 97 7616 7612 7891 1133 -992 39 O ATOM 399 CB ALA A 97 17.347 17.932 -11.177 1.00 55.21 C ANISOU 399 CB ALA A 97 7342 6982 6651 1188 -1177 105 C ATOM 400 N VAL A 98 15.973 16.004 -8.990 1.00 83.33 N ANISOU 400 N VAL A 98 10282 10626 10755 937 -1134 -162 N ATOM 401 CA VAL A 98 14.838 15.652 -8.139 1.00 57.71 C ANISOU 401 CA VAL A 98 6745 7440 7742 921 -1143 -239 C ATOM 402 C VAL A 98 15.252 15.667 -6.673 1.00 54.15 C ANISOU 402 C VAL A 98 6276 6880 7418 814 -913 -191 C ATOM 403 O VAL A 98 14.546 16.211 -5.816 1.00 58.96 O ANISOU 403 O VAL A 98 6768 7492 8142 883 -849 -175 O ATOM 404 CB VAL A 98 14.261 14.284 -8.550 1.00 54.79 C ANISOU 404 CB VAL A 98 6162 7177 7478 797 -1262 -409 C ATOM 405 CG1 VAL A 98 13.372 13.728 -7.446 1.00 67.99 C ANISOU 405 CG1 VAL A 98 7543 8866 9424 701 -1177 -471 C ATOM 406 CG2 VAL A 98 13.480 14.414 -9.845 1.00 67.17 C ANISOU 406 CG2 VAL A 98 7685 8902 8936 942 -1534 -486 C ATOM 407 N ALA A 99 16.413 15.081 -6.369 1.00 61.24 N ANISOU 407 N ALA A 99 7290 7691 8286 657 -788 -174 N ATOM 408 CA ALA A 99 16.906 15.068 -4.995 1.00 48.19 C ANISOU 408 CA ALA A 99 5644 5954 6713 565 -597 -126 C ATOM 409 C ALA A 99 17.033 16.483 -4.446 1.00 49.33 C ANISOU 409 C ALA A 99 5908 6031 6806 685 -519 -43 C ATOM 410 O ALA A 99 16.536 16.784 -3.355 1.00 53.11 O ANISOU 410 O ALA A 99 6297 6509 7375 702 -420 -43 O ATOM 411 CB ALA A 99 18.248 14.338 -4.921 1.00 45.58 C ANISOU 411 CB ALA A 99 5434 5546 6338 419 -515 -113 C ATOM 412 N ASP A 100 17.680 17.374 -5.203 1.00 48.45 N ANISOU 412 N ASP A 100 6007 5852 6549 765 -547 22 N ATOM 413 CA ASP A 100 17.888 18.741 -4.735 1.00 50.82 C ANISOU 413 CA ASP A 100 6445 6042 6822 864 -464 92 C ATOM 414 C ASP A 100 16.575 19.509 -4.644 1.00 49.46 C ANISOU 414 C ASP A 100 6165 5903 6723 1057 -527 89 C ATOM 415 O ASP A 100 16.395 20.331 -3.739 1.00 47.51 O ANISOU 415 O ASP A 100 5932 5584 6535 1120 -423 92 O ATOM 416 CB ASP A 100 18.874 19.458 -5.653 1.00 55.95 C ANISOU 416 CB ASP A 100 7346 6591 7321 886 -460 177 C ATOM 417 CG ASP A 100 20.273 18.893 -5.554 1.00 74.37 C ANISOU 417 CG ASP A 100 9764 8878 9614 705 -360 171 C ATOM 418 OD1 ASP A 100 20.647 18.411 -4.463 1.00102.94 O ANISOU 418 OD1 ASP A 100 13306 12493 13315 591 -274 129 O ATOM 419 OD2 ASP A 100 21.003 18.932 -6.563 1.00 86.21 O ANISOU 419 OD2 ASP A 100 11406 10356 10993 686 -366 211 O ATOM 420 N LEU A 101 15.652 19.269 -5.578 1.00 49.48 N ANISOU 420 N LEU A 101 6055 6020 6724 1165 -704 66 N ATOM 421 CA LEU A 101 14.330 19.875 -5.466 1.00 51.29 C ANISOU 421 CA LEU A 101 6123 6308 7059 1361 -781 46 C ATOM 422 C LEU A 101 13.630 19.416 -4.194 1.00 54.60 C ANISOU 422 C LEU A 101 6295 6786 7664 1292 -659 -41 C ATOM 423 O LEU A 101 12.981 20.216 -3.508 1.00 57.71 O ANISOU 423 O LEU A 101 6621 7158 8150 1424 -589 -51 O ATOM 424 CB LEU A 101 13.486 19.543 -6.696 1.00 51.90 C ANISOU 424 CB LEU A 101 6086 6533 7101 1474 -1027 14 C ATOM 425 CG LEU A 101 12.026 19.996 -6.620 1.00 55.30 C ANISOU 425 CG LEU A 101 6273 7062 7677 1682 -1140 -30 C ATOM 426 CD1 LEU A 101 11.943 21.510 -6.518 1.00 81.13 C ANISOU 426 CD1 LEU A 101 9705 10194 10926 1917 -1110 80 C ATOM 427 CD2 LEU A 101 11.234 19.488 -7.812 1.00 62.20 C ANISOU 427 CD2 LEU A 101 7000 8118 8517 1766 -1418 -95 C ATOM 428 N LEU A 102 13.769 18.132 -3.851 1.00 51.76 N ANISOU 428 N LEU A 102 5813 6491 7363 1089 -613 -101 N ATOM 429 CA LEU A 102 13.186 17.626 -2.612 1.00 51.02 C ANISOU 429 CA LEU A 102 5515 6445 7424 1000 -460 -154 C ATOM 430 C LEU A 102 13.815 18.293 -1.397 1.00 51.08 C ANISOU 430 C LEU A 102 5670 6352 7385 986 -260 -114 C ATOM 431 O LEU A 102 13.127 18.563 -0.405 1.00 71.42 O ANISOU 431 O LEU A 102 8124 8962 10048 1027 -130 -150 O ATOM 432 CB LEU A 102 13.341 16.107 -2.539 1.00 70.41 C ANISOU 432 CB LEU A 102 7862 8946 9946 780 -441 -195 C ATOM 433 CG LEU A 102 12.483 15.307 -3.522 1.00 63.62 C ANISOU 433 CG LEU A 102 6788 8199 9185 763 -624 -292 C ATOM 434 CD1 LEU A 102 12.901 13.847 -3.547 1.00 54.03 C ANISOU 434 CD1 LEU A 102 5537 6964 8029 537 -597 -333 C ATOM 435 CD2 LEU A 102 11.011 15.438 -3.165 1.00 54.08 C ANISOU 435 CD2 LEU A 102 5268 7107 8173 843 -626 -366 C ATOM 436 N VAL A 103 15.123 18.564 -1.454 1.00 50.00 N ANISOU 436 N VAL A 103 5786 6103 7110 923 -230 -57 N ATOM 437 CA VAL A 103 15.777 19.354 -0.408 1.00 51.92 C ANISOU 437 CA VAL A 103 6180 6249 7298 918 -80 -46 C ATOM 438 C VAL A 103 15.063 20.689 -0.246 1.00 55.08 C ANISOU 438 C VAL A 103 6592 6596 7739 1125 -59 -66 C ATOM 439 O VAL A 103 14.545 21.019 0.827 1.00 49.35 O ANISOU 439 O VAL A 103 5794 5891 7067 1166 74 -124 O ATOM 440 CB VAL A 103 17.266 19.572 -0.731 1.00 49.53 C ANISOU 440 CB VAL A 103 6118 5832 6870 830 -82 3 C ATOM 441 CG1 VAL A 103 17.950 20.334 0.401 1.00 45.51 C ANISOU 441 CG1 VAL A 103 5739 5235 6317 803 52 -21 C ATOM 442 CG2 VAL A 103 17.964 18.265 -0.996 1.00 49.23 C ANISOU 442 CG2 VAL A 103 6059 5837 6809 662 -110 15 C ATOM 443 N GLY A 104 15.012 21.467 -1.328 1.00 63.81 N ANISOU 443 N GLY A 104 7801 7629 8815 1270 -184 -15 N ATOM 444 CA GLY A 104 14.424 22.794 -1.298 1.00 55.29 C ANISOU 444 CA GLY A 104 6768 6454 7785 1493 -177 -14 C ATOM 445 C GLY A 104 12.936 22.821 -1.024 1.00 54.68 C ANISOU 445 C GLY A 104 6420 6496 7860 1651 -192 -82 C ATOM 446 O GLY A 104 12.398 23.901 -0.756 1.00 55.60 O ANISOU 446 O GLY A 104 6549 6530 8047 1849 -152 -103 O ATOM 447 N LEU A 105 12.260 21.676 -1.083 1.00 61.95 N ANISOU 447 N LEU A 105 7085 7596 8857 1567 -237 -126 N ATOM 448 CA LEU A 105 10.823 21.612 -0.844 1.00 73.76 C ANISOU 448 CA LEU A 105 8269 9226 10531 1692 -242 -206 C ATOM 449 C LEU A 105 10.463 21.186 0.573 1.00 73.07 C ANISOU 449 C LEU A 105 8029 9209 10525 1584 -6 -283 C ATOM 450 O LEU A 105 9.522 21.734 1.152 1.00 76.37 O ANISOU 450 O LEU A 105 8284 9668 11066 1731 90 -353 O ATOM 451 CB LEU A 105 10.163 20.661 -1.845 1.00 74.48 C ANISOU 451 CB LEU A 105 8138 9474 10687 1665 -444 -229 C ATOM 452 CG LEU A 105 9.762 21.289 -3.181 1.00 70.42 C ANISOU 452 CG LEU A 105 7650 8970 10137 1893 -702 -186 C ATOM 453 CD1 LEU A 105 9.206 20.241 -4.131 1.00 57.13 C ANISOU 453 CD1 LEU A 105 5755 7464 8489 1834 -916 -246 C ATOM 454 CD2 LEU A 105 8.748 22.401 -2.956 1.00 57.36 C ANISOU 454 CD2 LEU A 105 5875 7305 8614 2181 -708 -207 C ATOM 455 N PHE A 106 11.185 20.230 1.154 1.00 78.87 N ANISOU 455 N PHE A 106 8819 9961 11188 1345 99 -264 N ATOM 456 CA PHE A 106 10.837 19.683 2.462 1.00 75.31 C ANISOU 456 CA PHE A 106 8241 9592 10780 1232 327 -305 C ATOM 457 C PHE A 106 11.845 20.002 3.555 1.00 59.51 C ANISOU 457 C PHE A 106 6487 7512 8612 1155 490 -291 C ATOM 458 O PHE A 106 11.449 20.208 4.705 1.00 75.92 O ANISOU 458 O PHE A 106 8522 9640 10685 1171 689 -345 O ATOM 459 CB PHE A 106 10.665 18.161 2.368 1.00 76.28 C ANISOU 459 CB PHE A 106 8195 9811 10977 1020 325 -287 C ATOM 460 CG PHE A 106 9.517 17.732 1.494 1.00 81.62 C ANISOU 460 CG PHE A 106 8567 10597 11847 1064 182 -347 C ATOM 461 CD1 PHE A 106 8.208 17.939 1.899 1.00 73.24 C ANISOU 461 CD1 PHE A 106 7207 9648 10972 1161 270 -429 C ATOM 462 CD2 PHE A 106 9.744 17.119 0.272 1.00 91.51 C ANISOU 462 CD2 PHE A 106 9819 11855 13096 1008 -43 -342 C ATOM 463 CE1 PHE A 106 7.148 17.549 1.100 1.00 71.95 C ANISOU 463 CE1 PHE A 106 6728 9604 11006 1198 115 -506 C ATOM 464 CE2 PHE A 106 8.687 16.725 -0.531 1.00 92.19 C ANISOU 464 CE2 PHE A 106 9617 12060 13350 1045 -204 -426 C ATOM 465 CZ PHE A 106 7.388 16.942 -0.116 1.00 79.70 C ANISOU 465 CZ PHE A 106 7717 10593 11971 1138 -136 -509 C ATOM 466 N VAL A 107 13.137 20.053 3.234 1.00 54.29 N ANISOU 466 N VAL A 107 6075 6743 7810 1074 411 -234 N ATOM 467 CA VAL A 107 14.158 20.206 4.267 1.00 53.14 C ANISOU 467 CA VAL A 107 6133 6549 7510 978 530 -236 C ATOM 468 C VAL A 107 14.297 21.663 4.692 1.00 59.43 C ANISOU 468 C VAL A 107 7083 7235 8265 1121 588 -315 C ATOM 469 O VAL A 107 14.200 21.992 5.880 1.00 71.67 O ANISOU 469 O VAL A 107 8664 8815 9751 1132 751 -392 O ATOM 470 CB VAL A 107 15.500 19.634 3.774 1.00 51.70 C ANISOU 470 CB VAL A 107 6111 6304 7227 828 425 -162 C ATOM 471 CG1 VAL A 107 16.569 19.769 4.849 1.00 51.71 C ANISOU 471 CG1 VAL A 107 6293 6279 7077 736 514 -176 C ATOM 472 CG2 VAL A 107 15.334 18.183 3.350 1.00 50.74 C ANISOU 472 CG2 VAL A 107 5847 6262 7170 696 375 -105 C ATOM 473 N MET A 108 14.533 22.554 3.732 1.00 55.79 N ANISOU 473 N MET A 108 6734 6633 7830 1234 465 -298 N ATOM 474 CA MET A 108 14.900 23.928 4.068 1.00 64.27 C ANISOU 474 CA MET A 108 8000 7541 8877 1337 519 -366 C ATOM 475 C MET A 108 13.792 24.730 4.748 1.00 70.62 C ANISOU 475 C MET A 108 8708 8350 9774 1530 644 -477 C ATOM 476 O MET A 108 14.106 25.462 5.703 1.00 70.79 O ANISOU 476 O MET A 108 8862 8300 9736 1543 771 -589 O ATOM 477 CB MET A 108 15.393 24.639 2.803 1.00 67.54 C ANISOU 477 CB MET A 108 8571 7782 9308 1406 376 -286 C ATOM 478 CG MET A 108 16.059 23.704 1.805 1.00 60.06 C ANISOU 478 CG MET A 108 7638 6879 8304 1269 244 -176 C ATOM 479 SD MET A 108 16.854 24.603 0.466 1.00 71.14 S ANISOU 479 SD MET A 108 9282 8077 9671 1320 137 -72 S ATOM 480 CE MET A 108 18.078 25.502 1.398 1.00 57.41 C ANISOU 480 CE MET A 108 7766 6158 7891 1209 271 -152 C ATOM 481 N PRO A 109 12.522 24.672 4.324 1.00 63.72 N ANISOU 481 N PRO A 109 7602 7559 9049 1688 614 -475 N ATOM 482 CA PRO A 109 11.501 25.493 5.000 1.00 59.68 C ANISOU 482 CA PRO A 109 6985 7047 8645 1891 752 -596 C ATOM 483 C PRO A 109 11.340 25.176 6.478 1.00 61.98 C ANISOU 483 C PRO A 109 7229 7465 8857 1805 989 -705 C ATOM 484 O PRO A 109 11.095 26.093 7.271 1.00 66.61 O ANISOU 484 O PRO A 109 7876 7990 9444 1929 1136 -841 O ATOM 485 CB PRO A 109 10.222 25.186 4.203 1.00 73.57 C ANISOU 485 CB PRO A 109 8443 8923 10587 2040 647 -565 C ATOM 486 CG PRO A 109 10.495 23.889 3.517 1.00 58.34 C ANISOU 486 CG PRO A 109 6432 7111 8622 1846 515 -463 C ATOM 487 CD PRO A 109 11.947 23.954 3.173 1.00 56.72 C ANISOU 487 CD PRO A 109 6532 6767 8251 1708 441 -386 C ATOM 488 N ILE A 110 11.477 23.907 6.873 1.00 61.71 N ANISOU 488 N ILE A 110 7107 7596 8745 1601 1038 -648 N ATOM 489 CA ILE A 110 11.440 23.559 8.290 1.00 66.34 C ANISOU 489 CA ILE A 110 7698 8307 9202 1510 1267 -715 C ATOM 490 C ILE A 110 12.716 24.020 8.982 1.00 62.13 C ANISOU 490 C ILE A 110 7470 7682 8453 1423 1282 -766 C ATOM 491 O ILE A 110 12.678 24.560 10.093 1.00 70.57 O ANISOU 491 O ILE A 110 8628 8777 9410 1464 1449 -900 O ATOM 492 CB ILE A 110 11.221 22.047 8.466 1.00 68.47 C ANISOU 492 CB ILE A 110 7804 8749 9463 1321 1316 -606 C ATOM 493 CG1 ILE A 110 9.928 21.591 7.786 1.00 71.57 C ANISOU 493 CG1 ILE A 110 7858 9235 10099 1383 1293 -591 C ATOM 494 CG2 ILE A 110 11.202 21.689 9.940 1.00 66.67 C ANISOU 494 CG2 ILE A 110 7618 8649 9064 1236 1564 -639 C ATOM 495 CD1 ILE A 110 9.660 20.117 7.961 1.00 63.17 C ANISOU 495 CD1 ILE A 110 6628 8305 9070 1178 1362 -498 C ATOM 496 N ALA A 111 13.867 23.817 8.336 1.00 58.70 N ANISOU 496 N ALA A 111 7192 7154 7959 1302 1108 -679 N ATOM 497 CA ALA A 111 15.125 24.318 8.882 1.00 60.75 C ANISOU 497 CA ALA A 111 7708 7321 8051 1215 1091 -746 C ATOM 498 C ALA A 111 15.060 25.820 9.158 1.00 62.89 C ANISOU 498 C ALA A 111 8113 7425 8358 1367 1148 -914 C ATOM 499 O ALA A 111 15.738 26.317 10.069 1.00 62.18 O ANISOU 499 O ALA A 111 8195 7307 8126 1317 1207 -1049 O ATOM 500 CB ALA A 111 16.273 23.982 7.932 1.00 53.68 C ANISOU 500 CB ALA A 111 6913 6334 7147 1086 901 -634 C ATOM 501 N LEU A 112 14.244 26.552 8.390 1.00 84.07 N ANISOU 501 N LEU A 112 10719 9990 11232 1561 1123 -917 N ATOM 502 CA LEU A 112 13.958 27.952 8.696 1.00 67.43 C ANISOU 502 CA LEU A 112 8716 7704 9200 1743 1205 -1077 C ATOM 503 C LEU A 112 13.246 28.097 10.039 1.00 73.65 C ANISOU 503 C LEU A 112 9443 8625 9917 1814 1433 -1253 C ATOM 504 O LEU A 112 13.640 28.915 10.875 1.00 80.62 O ANISOU 504 O LEU A 112 10502 9420 10710 1830 1526 -1438 O ATOM 505 CB LEU A 112 13.107 28.568 7.580 1.00 64.01 C ANISOU 505 CB LEU A 112 8189 7140 8991 1971 1121 -1010 C ATOM 506 CG LEU A 112 13.706 29.029 6.251 1.00 59.25 C ANISOU 506 CG LEU A 112 7729 6324 8461 1991 933 -871 C ATOM 507 CD1 LEU A 112 12.684 29.928 5.574 1.00 60.24 C ANISOU 507 CD1 LEU A 112 7790 6314 8783 2289 897 -853 C ATOM 508 CD2 LEU A 112 15.016 29.748 6.457 1.00 59.17 C ANISOU 508 CD2 LEU A 112 8004 6100 8376 1861 936 -932 C ATOM 509 N LEU A 113 12.167 27.334 10.248 1.00 81.33 N ANISOU 509 N LEU A 113 10159 9808 10934 1857 1537 -1213 N ATOM 510 CA LEU A 113 11.395 27.464 11.484 1.00 95.77 C ANISOU 510 CA LEU A 113 11912 11778 12696 1934 1794 -1371 C ATOM 511 C LEU A 113 12.290 27.316 12.711 1.00 74.33 C ANISOU 511 C LEU A 113 9413 9146 9681 1775 1886 -1466 C ATOM 512 O LEU A 113 12.113 28.025 13.710 1.00 73.52 O ANISOU 512 O LEU A 113 9405 9052 9478 1859 2059 -1674 O ATOM 513 CB LEU A 113 10.258 26.446 11.497 1.00 89.03 C ANISOU 513 CB LEU A 113 10739 11154 11933 1933 1901 -1281 C ATOM 514 CG LEU A 113 9.404 26.562 10.233 1.00 73.61 C ANISOU 514 CG LEU A 113 8554 9145 10270 2090 1757 -1203 C ATOM 515 CD1 LEU A 113 8.261 25.570 10.252 1.00 83.35 C ANISOU 515 CD1 LEU A 113 9433 10604 11630 2068 1858 -1148 C ATOM 516 CD2 LEU A 113 8.886 27.987 10.047 1.00 73.02 C ANISOU 516 CD2 LEU A 113 8500 8884 10360 2377 1772 -1341 C ATOM 517 N THR A 114 13.292 26.434 12.627 1.00 72.61 N ANISOU 517 N THR A 114 9284 8988 9315 1560 1757 -1329 N ATOM 518 CA THR A 114 14.311 26.327 13.667 1.00 74.78 C ANISOU 518 CA THR A 114 9776 9335 9302 1419 1773 -1408 C ATOM 519 C THR A 114 15.097 27.629 13.844 1.00 78.57 C ANISOU 519 C THR A 114 10488 9608 9758 1452 1713 -1616 C ATOM 520 O THR A 114 15.491 27.961 14.970 1.00 89.95 O ANISOU 520 O THR A 114 12084 11115 10976 1423 1793 -1798 O ATOM 521 CB THR A 114 15.259 25.169 13.343 1.00 77.31 C ANISOU 521 CB THR A 114 10121 9726 9528 1214 1609 -1208 C ATOM 522 OG1 THR A 114 16.065 25.506 12.206 1.00108.30 O ANISOU 522 OG1 THR A 114 14110 13450 13589 1174 1393 -1154 O ATOM 523 CG2 THR A 114 14.472 23.897 13.024 1.00 75.96 C ANISOU 523 CG2 THR A 114 9722 9703 9436 1169 1660 -1008 C ATOM 524 N ILE A 115 15.361 28.368 12.758 1.00 77.29 N ANISOU 524 N ILE A 115 10364 9191 9813 1503 1574 -1596 N ATOM 525 CA ILE A 115 16.001 29.678 12.903 1.00 76.08 C ANISOU 525 CA ILE A 115 10425 8794 9690 1531 1550 -1799 C ATOM 526 C ILE A 115 15.130 30.588 13.753 1.00 95.35 C ANISOU 526 C ILE A 115 12883 11204 12140 1722 1757 -2042 C ATOM 527 O ILE A 115 15.594 31.190 14.727 1.00104.17 O ANISOU 527 O ILE A 115 14174 12304 13103 1692 1821 -2283 O ATOM 528 CB ILE A 115 16.280 30.325 11.533 1.00 81.63 C ANISOU 528 CB ILE A 115 11168 9206 10640 1572 1405 -1696 C ATOM 529 CG1 ILE A 115 16.777 29.317 10.514 1.00 87.97 C ANISOU 529 CG1 ILE A 115 11894 10070 11460 1436 1237 -1438 C ATOM 530 CG2 ILE A 115 17.321 31.442 11.647 1.00 70.74 C ANISOU 530 CG2 ILE A 115 10029 7563 9284 1500 1360 -1868 C ATOM 531 CD1 ILE A 115 17.080 29.994 9.193 1.00105.39 C ANISOU 531 CD1 ILE A 115 14176 12006 13862 1479 1117 -1333 C ATOM 532 N MET A 116 13.852 30.710 13.388 1.00108.10 N ANISOU 532 N MET A 116 14309 12821 13943 1930 1859 -2002 N ATOM 533 CA MET A 116 12.972 31.656 14.064 1.00 89.56 C ANISOU 533 CA MET A 116 11956 10415 11658 2149 2065 -2240 C ATOM 534 C MET A 116 12.665 31.203 15.488 1.00101.76 C ANISOU 534 C MET A 116 13492 12247 12927 2114 2284 -2383 C ATOM 535 O MET A 116 12.932 31.928 16.454 1.00114.44 O ANISOU 535 O MET A 116 15279 13820 14384 2136 2391 -2651 O ATOM 536 CB MET A 116 11.687 31.840 13.255 1.00 74.19 C ANISOU 536 CB MET A 116 9768 8418 10002 2393 2097 -2148 C ATOM 537 CG MET A 116 11.915 32.063 11.760 1.00 83.06 C ANISOU 537 CG MET A 116 10894 9319 11345 2432 1865 -1944 C ATOM 538 SD MET A 116 10.372 31.991 10.825 1.00136.98 S ANISOU 538 SD MET A 116 17392 16188 18468 2711 1848 -1813 S ATOM 539 CE MET A 116 10.951 31.992 9.128 1.00101.90 C ANISOU 539 CE MET A 116 13022 11551 14144 2686 1542 -1543 C ATOM 540 N PHE A 117 12.092 30.007 15.638 1.00102.43 N ANISOU 540 N PHE A 117 13376 12608 12935 2057 2363 -2212 N ATOM 541 CA PHE A 117 11.710 29.466 16.946 1.00 93.89 C ANISOU 541 CA PHE A 117 12282 11814 11579 2023 2604 -2293 C ATOM 542 C PHE A 117 12.902 28.710 17.536 1.00105.18 C ANISOU 542 C PHE A 117 13902 13386 12676 1784 2497 -2225 C ATOM 543 O PHE A 117 12.954 27.479 17.560 1.00108.96 O ANISOU 543 O PHE A 117 14296 14053 13049 1648 2485 -2001 O ATOM 544 CB PHE A 117 10.491 28.556 16.815 1.00 83.80 C ANISOU 544 CB PHE A 117 10687 10740 10413 2065 2764 -2132 C ATOM 545 CG PHE A 117 9.325 29.169 16.070 1.00 80.12 C ANISOU 545 CG PHE A 117 9975 10157 10310 2307 2811 -2167 C ATOM 546 CD1 PHE A 117 9.356 29.332 14.690 1.00 81.05 C ANISOU 546 CD1 PHE A 117 10010 10084 10703 2360 2565 -2024 C ATOM 547 CD2 PHE A 117 8.175 29.536 16.749 1.00 79.78 C ANISOU 547 CD2 PHE A 117 9772 10217 10323 2492 3103 -2335 C ATOM 548 CE1 PHE A 117 8.278 29.882 14.012 1.00 81.67 C ANISOU 548 CE1 PHE A 117 9860 10073 11097 2607 2576 -2045 C ATOM 549 CE2 PHE A 117 7.092 30.082 16.075 1.00 78.71 C ANISOU 549 CE2 PHE A 117 9380 9988 10538 2738 3129 -2369 C ATOM 550 CZ PHE A 117 7.144 30.255 14.706 1.00 76.76 C ANISOU 550 CZ PHE A 117 9060 9551 10556 2801 2849 -2219 C ATOM 551 N GLU A 118 13.878 29.486 18.014 1.00108.05 N ANISOU 551 N GLU A 118 14522 13643 12889 1738 2409 -2433 N ATOM 552 CA GLU A 118 15.176 28.911 18.356 1.00115.53 C ANISOU 552 CA GLU A 118 15636 14684 13577 1525 2226 -2376 C ATOM 553 C GLU A 118 15.071 27.886 19.481 1.00110.69 C ANISOU 553 C GLU A 118 15048 14408 12602 1453 2361 -2303 C ATOM 554 O GLU A 118 15.739 26.846 19.446 1.00 97.02 O ANISOU 554 O GLU A 118 13330 12797 10737 1300 2227 -2088 O ATOM 555 CB GLU A 118 16.153 30.028 18.739 1.00111.33 C ANISOU 555 CB GLU A 118 15346 13983 12971 1492 2117 -2665 C ATOM 556 N ALA A 119 14.225 28.149 20.478 1.00125.47 N ANISOU 556 N ALA A 119 16931 16429 14312 1571 2641 -2466 N ATOM 557 CA ALA A 119 14.288 27.378 21.716 1.00131.80 C ANISOU 557 CA ALA A 119 17842 17545 14692 1506 2779 -2432 C ATOM 558 C ALA A 119 13.789 25.949 21.523 1.00128.10 C ANISOU 558 C ALA A 119 17196 17244 14232 1423 2864 -2079 C ATOM 559 O ALA A 119 14.536 24.984 21.731 1.00112.20 O ANISOU 559 O ALA A 119 15267 15349 12013 1280 2737 -1879 O ATOM 560 CB ALA A 119 13.491 28.088 22.814 1.00108.04 C ANISOU 560 CB ALA A 119 14902 14652 11497 1659 3090 -2716 C ATOM 561 N MET A 120 12.526 25.788 21.137 1.00128.42 N ANISOU 561 N MET A 120 16980 17288 14526 1513 3076 -2007 N ATOM 562 CA MET A 120 11.867 24.491 21.157 1.00128.78 C ANISOU 562 CA MET A 120 16847 17503 14580 1429 3233 -1724 C ATOM 563 C MET A 120 11.334 24.116 19.779 1.00109.83 C ANISOU 563 C MET A 120 14154 14956 12620 1421 3129 -1551 C ATOM 564 O MET A 120 10.926 24.977 18.994 1.00108.70 O ANISOU 564 O MET A 120 13890 14635 12778 1555 3067 -1673 O ATOM 565 CB MET A 120 10.721 24.485 22.173 1.00118.84 C ANISOU 565 CB MET A 120 15518 16453 13181 1519 3645 -1807 C ATOM 566 N TRP A 121 11.332 22.817 19.502 1.00 99.92 N ANISOU 566 N TRP A 121 12798 13775 11393 1270 3107 -1268 N ATOM 567 CA TRP A 121 10.839 22.289 18.234 1.00 99.78 C ANISOU 567 CA TRP A 121 12504 13650 11757 1236 3000 -1109 C ATOM 568 C TRP A 121 9.336 22.498 18.140 1.00100.42 C ANISOU 568 C TRP A 121 12277 13785 12093 1358 3253 -1180 C ATOM 569 O TRP A 121 8.593 21.929 18.952 1.00 93.03 O ANISOU 569 O TRP A 121 11250 13035 11063 1320 3562 -1131 O ATOM 570 CB TRP A 121 11.184 20.806 18.106 1.00 93.67 C ANISOU 570 CB TRP A 121 11712 12938 10941 1037 2947 -817 C ATOM 571 CG TRP A 121 10.544 20.105 16.935 1.00 83.60 C ANISOU 571 CG TRP A 121 10139 11587 10037 980 2879 -673 C ATOM 572 CD1 TRP A 121 9.442 19.298 16.965 1.00 77.36 C ANISOU 572 CD1 TRP A 121 9086 10893 9414 920 3101 -568 C ATOM 573 CD2 TRP A 121 10.982 20.132 15.568 1.00 91.93 C ANISOU 573 CD2 TRP A 121 11132 12465 11332 967 2567 -632 C ATOM 574 NE1 TRP A 121 9.165 18.825 15.704 1.00 74.99 N ANISOU 574 NE1 TRP A 121 8557 10489 9446 871 2921 -486 N ATOM 575 CE2 TRP A 121 10.096 19.321 14.829 1.00 73.76 C ANISOU 575 CE2 TRP A 121 8532 10173 9319 908 2595 -519 C ATOM 576 CE3 TRP A 121 12.036 20.763 14.898 1.00 98.34 C ANISOU 576 CE3 TRP A 121 12110 13116 12139 992 2281 -685 C ATOM 577 CZ2 TRP A 121 10.232 19.126 13.455 1.00 73.92 C ANISOU 577 CZ2 TRP A 121 8437 10063 9586 888 2331 -467 C ATOM 578 CZ3 TRP A 121 12.170 20.565 13.532 1.00 84.85 C ANISOU 578 CZ3 TRP A 121 10290 11274 10676 970 2050 -609 C ATOM 579 CH2 TRP A 121 11.272 19.754 12.827 1.00 72.41 C ANISOU 579 CH2 TRP A 121 8437 9727 9349 927 2068 -505 C ATOM 580 N PRO A 122 8.842 23.287 17.183 1.00105.35 N ANISOU 580 N PRO A 122 12729 14258 13041 1509 3143 -1287 N ATOM 581 CA PRO A 122 7.414 23.642 17.209 1.00 95.28 C ANISOU 581 CA PRO A 122 11149 13049 12006 1668 3382 -1398 C ATOM 582 C PRO A 122 6.515 22.545 16.672 1.00 97.84 C ANISOU 582 C PRO A 122 11122 13465 12586 1567 3446 -1222 C ATOM 583 O PRO A 122 5.388 22.383 17.158 1.00110.26 O ANISOU 583 O PRO A 122 12446 15187 14260 1606 3749 -1268 O ATOM 584 CB PRO A 122 7.353 24.913 16.341 1.00 89.79 C ANISOU 584 CB PRO A 122 10433 12133 11549 1885 3188 -1556 C ATOM 585 CG PRO A 122 8.795 25.301 16.063 1.00 98.17 C ANISOU 585 CG PRO A 122 11830 13020 12451 1817 2906 -1551 C ATOM 586 CD PRO A 122 9.576 24.032 16.150 1.00103.88 C ANISOU 586 CD PRO A 122 12642 13836 12991 1568 2818 -1329 C ATOM 587 N LEU A 123 6.988 21.773 15.695 1.00107.23 N ANISOU 587 N LEU A 123 12278 14572 13891 1427 3180 -1038 N ATOM 588 CA LEU A 123 6.159 20.797 15.009 1.00 95.67 C ANISOU 588 CA LEU A 123 10472 13161 12716 1328 3186 -910 C ATOM 589 C LEU A 123 5.904 19.584 15.901 1.00 86.33 C ANISOU 589 C LEU A 123 9254 12138 11410 1119 3471 -757 C ATOM 590 O LEU A 123 6.482 19.460 16.984 1.00 83.49 O ANISOU 590 O LEU A 123 9169 11852 10703 1061 3622 -719 O ATOM 591 CB LEU A 123 6.829 20.379 13.700 1.00 92.33 C ANISOU 591 CB LEU A 123 10068 12592 12422 1246 2813 -788 C ATOM 592 CG LEU A 123 7.016 21.482 12.659 1.00 98.52 C ANISOU 592 CG LEU A 123 10878 13209 13345 1441 2535 -890 C ATOM 593 CD1 LEU A 123 7.516 20.897 11.347 1.00108.60 C ANISOU 593 CD1 LEU A 123 12137 14385 14741 1346 2213 -758 C ATOM 594 CD2 LEU A 123 5.718 22.245 12.453 1.00 90.22 C ANISOU 594 CD2 LEU A 123 9526 12193 12562 1671 2628 -1041 C ATOM 595 N PRO A 124 5.010 18.676 15.482 1.00 82.30 N ANISOU 595 N PRO A 124 8406 11684 11181 1003 3554 -666 N ATOM 596 CA PRO A 124 4.836 17.419 16.225 1.00 88.68 C ANISOU 596 CA PRO A 124 9198 12593 11902 772 3820 -480 C ATOM 597 C PRO A 124 6.114 16.609 16.421 1.00 94.91 C ANISOU 597 C PRO A 124 10331 13310 12419 605 3682 -272 C ATOM 598 O PRO A 124 7.153 16.889 15.814 1.00 93.87 O ANISOU 598 O PRO A 124 10403 13050 12213 636 3352 -272 O ATOM 599 CB PRO A 124 3.826 16.656 15.361 1.00 77.28 C ANISOU 599 CB PRO A 124 7323 11153 10886 667 3812 -446 C ATOM 600 CG PRO A 124 2.988 17.726 14.764 1.00 74.19 C ANISOU 600 CG PRO A 124 6656 10780 10755 906 3737 -667 C ATOM 601 CD PRO A 124 3.908 18.900 14.526 1.00 74.89 C ANISOU 601 CD PRO A 124 7054 10746 10653 1107 3481 -767 C ATOM 602 N LEU A 125 6.017 15.576 17.262 1.00 92.86 N ANISOU 602 N LEU A 125 10125 13129 12027 428 3947 -85 N ATOM 603 CA LEU A 125 7.185 14.800 17.664 1.00 79.31 C ANISOU 603 CA LEU A 125 8750 11363 10021 301 3856 128 C ATOM 604 C LEU A 125 7.695 13.921 16.530 1.00 77.55 C ANISOU 604 C LEU A 125 8477 10967 10021 167 3557 256 C ATOM 605 O LEU A 125 8.909 13.767 16.353 1.00 87.90 O ANISOU 605 O LEU A 125 10052 12186 11161 154 3304 334 O ATOM 606 CB LEU A 125 6.828 13.952 18.888 1.00 80.96 C ANISOU 606 CB LEU A 125 9035 11696 10029 169 4251 317 C ATOM 607 N VAL A 126 6.778 13.339 15.757 1.00 77.56 N ANISOU 607 N VAL A 126 8129 10930 10411 67 3582 258 N ATOM 608 CA VAL A 126 7.143 12.457 14.649 1.00 82.29 C ANISOU 608 CA VAL A 126 8659 11369 11238 -67 3317 346 C ATOM 609 C VAL A 126 7.966 13.201 13.604 1.00 66.98 C ANISOU 609 C VAL A 126 6819 9330 9299 66 2915 229 C ATOM 610 O VAL A 126 8.843 12.621 12.951 1.00 67.31 O ANISOU 610 O VAL A 126 6984 9244 9347 -11 2674 316 O ATOM 611 CB VAL A 126 5.868 11.855 14.032 1.00 97.34 C ANISOU 611 CB VAL A 126 10134 13279 13570 -187 3418 305 C ATOM 612 CG1 VAL A 126 5.282 10.802 14.949 1.00 93.06 C ANISOU 612 CG1 VAL A 126 9529 12773 13056 -393 3809 482 C ATOM 613 CG2 VAL A 126 4.862 12.963 13.789 1.00101.11 C ANISOU 613 CG2 VAL A 126 10325 13875 14218 -2 3452 70 C ATOM 614 N LEU A 127 7.697 14.494 13.425 1.00 67.67 N ANISOU 614 N LEU A 127 6859 9465 9388 270 2854 34 N ATOM 615 CA LEU A 127 8.326 15.240 12.340 1.00 67.09 C ANISOU 615 CA LEU A 127 6854 9282 9354 393 2501 -65 C ATOM 616 C LEU A 127 9.800 15.522 12.592 1.00 62.62 C ANISOU 616 C LEU A 127 6666 8644 8484 411 2341 -19 C ATOM 617 O LEU A 127 10.524 15.828 11.641 1.00 59.90 O ANISOU 617 O LEU A 127 6401 8185 8171 449 2058 -48 O ATOM 618 CB LEU A 127 7.594 16.553 12.095 1.00 72.35 C ANISOU 618 CB LEU A 127 7373 9987 10128 619 2494 -268 C ATOM 619 CG LEU A 127 6.184 16.449 11.516 1.00 75.78 C ANISOU 619 CG LEU A 127 7382 10491 10920 651 2546 -352 C ATOM 620 CD1 LEU A 127 5.908 17.673 10.663 1.00 74.24 C ANISOU 620 CD1 LEU A 127 7106 10253 10849 898 2334 -509 C ATOM 621 CD2 LEU A 127 6.013 15.169 10.706 1.00 73.99 C ANISOU 621 CD2 LEU A 127 6973 10224 10915 447 2433 -254 C ATOM 622 N CYS A 128 10.254 15.455 13.842 1.00 63.83 N ANISOU 622 N CYS A 128 7044 8871 8336 387 2514 43 N ATOM 623 CA CYS A 128 11.675 15.635 14.123 1.00 63.22 C ANISOU 623 CA CYS A 128 7294 8745 7980 392 2342 78 C ATOM 624 C CYS A 128 12.530 14.512 13.551 1.00 76.14 C ANISOU 624 C CYS A 128 8997 10275 9656 250 2156 252 C ATOM 625 O CYS A 128 13.580 14.817 12.956 1.00 60.04 O ANISOU 625 O CYS A 128 7094 8143 7576 276 1899 223 O ATOM 626 CB CYS A 128 11.876 15.762 15.632 1.00 63.17 C ANISOU 626 CB CYS A 128 7501 8877 7622 408 2560 99 C ATOM 627 SG CYS A 128 13.542 16.135 16.168 1.00 93.12 S ANISOU 627 SG CYS A 128 11666 12661 11053 434 2344 90 S ATOM 628 N PRO A 129 12.173 13.213 13.694 1.00 74.86 N ANISOU 628 N PRO A 129 8750 10105 9587 98 2283 429 N ATOM 629 CA PRO A 129 12.931 12.180 12.973 1.00 62.36 C ANISOU 629 CA PRO A 129 7208 8384 8101 -16 2091 561 C ATOM 630 C PRO A 129 12.640 12.163 11.481 1.00 69.50 C ANISOU 630 C PRO A 129 7905 9189 9314 -27 1890 464 C ATOM 631 O PRO A 129 13.535 11.871 10.684 1.00 84.88 O ANISOU 631 O PRO A 129 9933 11027 11290 -50 1659 484 O ATOM 632 CB PRO A 129 12.481 10.874 13.644 1.00 60.05 C ANISOU 632 CB PRO A 129 6888 8090 7839 -171 2329 769 C ATOM 633 CG PRO A 129 11.974 11.278 14.979 1.00 62.37 C ANISOU 633 CG PRO A 129 7254 8548 7897 -125 2622 785 C ATOM 634 CD PRO A 129 11.327 12.609 14.745 1.00 62.51 C ANISOU 634 CD PRO A 129 7132 8648 7972 21 2628 540 C ATOM 635 N ALA A 130 11.395 12.451 11.094 1.00 65.91 N ANISOU 635 N ALA A 130 7175 8784 9083 -2 1974 356 N ATOM 636 CA ALA A 130 11.055 12.513 9.676 1.00 56.55 C ANISOU 636 CA ALA A 130 5793 7536 8156 14 1757 251 C ATOM 637 C ALA A 130 11.923 13.535 8.953 1.00 57.58 C ANISOU 637 C ALA A 130 6082 7611 8184 155 1500 160 C ATOM 638 O ALA A 130 12.597 13.215 7.967 1.00 81.85 O ANISOU 638 O ALA A 130 9205 10588 11304 121 1281 170 O ATOM 639 CB ALA A 130 9.572 12.848 9.506 1.00 58.16 C ANISOU 639 CB ALA A 130 5668 7837 8594 61 1874 132 C ATOM 640 N TRP A 131 11.931 14.774 9.450 1.00 55.33 N ANISOU 640 N TRP A 131 5888 7376 7760 308 1545 64 N ATOM 641 CA TRP A 131 12.655 15.848 8.776 1.00 54.03 C ANISOU 641 CA TRP A 131 5866 7132 7531 435 1335 -24 C ATOM 642 C TRP A 131 14.161 15.614 8.801 1.00 52.57 C ANISOU 642 C TRP A 131 5938 6868 7166 367 1203 49 C ATOM 643 O TRP A 131 14.849 15.862 7.804 1.00 56.03 O ANISOU 643 O TRP A 131 6442 7213 7633 385 1000 30 O ATOM 644 CB TRP A 131 12.303 17.188 9.420 1.00 55.26 C ANISOU 644 CB TRP A 131 6066 7328 7601 602 1442 -153 C ATOM 645 CG TRP A 131 13.218 18.300 9.049 1.00 56.38 C ANISOU 645 CG TRP A 131 6417 7360 7644 702 1279 -227 C ATOM 646 CD1 TRP A 131 13.305 18.919 7.837 1.00 55.47 C ANISOU 646 CD1 TRP A 131 6293 7140 7644 793 1085 -264 C ATOM 647 CD2 TRP A 131 14.170 18.946 9.901 1.00 56.51 C ANISOU 647 CD2 TRP A 131 6685 7356 7430 715 1304 -276 C ATOM 648 NE1 TRP A 131 14.259 19.906 7.879 1.00 56.05 N ANISOU 648 NE1 TRP A 131 6598 7106 7593 845 1014 -319 N ATOM 649 CE2 TRP A 131 14.804 19.943 9.136 1.00 54.35 C ANISOU 649 CE2 TRP A 131 6531 6942 7178 793 1135 -346 C ATOM 650 CE3 TRP A 131 14.549 18.775 11.236 1.00 55.43 C ANISOU 650 CE3 TRP A 131 6688 7313 7060 665 1446 -271 C ATOM 651 CZ2 TRP A 131 15.797 20.768 9.661 1.00 55.16 C ANISOU 651 CZ2 TRP A 131 6860 6980 7118 801 1109 -430 C ATOM 652 CZ3 TRP A 131 15.536 19.595 11.755 1.00 56.53 C ANISOU 652 CZ3 TRP A 131 7056 7414 7007 692 1390 -366 C ATOM 653 CH2 TRP A 131 16.148 20.578 10.968 1.00 55.14 C ANISOU 653 CH2 TRP A 131 6969 7084 6899 748 1224 -455 C ATOM 654 N LEU A 132 14.692 15.138 9.929 1.00 53.22 N ANISOU 654 N LEU A 132 6164 6998 7058 297 1317 135 N ATOM 655 CA LEU A 132 16.123 14.861 10.013 1.00 52.17 C ANISOU 655 CA LEU A 132 6242 6810 6771 245 1179 200 C ATOM 656 C LEU A 132 16.523 13.755 9.045 1.00 56.81 C ANISOU 656 C LEU A 132 6776 7304 7507 142 1043 294 C ATOM 657 O LEU A 132 17.537 13.863 8.343 1.00 75.53 O ANISOU 657 O LEU A 132 9237 9595 9867 141 863 279 O ATOM 658 CB LEU A 132 16.502 14.489 11.446 1.00 56.29 C ANISOU 658 CB LEU A 132 6916 7425 7046 212 1313 289 C ATOM 659 CG LEU A 132 16.531 15.633 12.462 1.00 58.73 C ANISOU 659 CG LEU A 132 7355 7828 7132 313 1404 162 C ATOM 660 CD1 LEU A 132 16.805 15.096 13.855 1.00 56.42 C ANISOU 660 CD1 LEU A 132 7215 7658 6563 280 1536 268 C ATOM 661 CD2 LEU A 132 17.568 16.672 12.073 1.00 54.37 C ANISOU 661 CD2 LEU A 132 6935 7198 6523 368 1207 29 C ATOM 662 N PHE A 133 15.730 12.683 8.990 1.00 56.57 N ANISOU 662 N PHE A 133 6591 7273 7629 47 1143 377 N ATOM 663 CA PHE A 133 16.012 11.592 8.062 1.00 50.82 C ANISOU 663 CA PHE A 133 5806 6439 7066 -54 1026 435 C ATOM 664 C PHE A 133 16.020 12.086 6.622 1.00 48.79 C ANISOU 664 C PHE A 133 5475 6132 6930 -2 829 313 C ATOM 665 O PHE A 133 16.964 11.821 5.870 1.00 57.77 O ANISOU 665 O PHE A 133 6698 7188 8064 -22 674 317 O ATOM 666 CB PHE A 133 14.988 10.473 8.243 1.00 55.02 C ANISOU 666 CB PHE A 133 6161 6963 7781 -178 1186 512 C ATOM 667 CG PHE A 133 14.986 9.469 7.131 1.00 68.79 C ANISOU 667 CG PHE A 133 7800 8589 9748 -280 1064 505 C ATOM 668 CD1 PHE A 133 15.998 8.530 7.026 1.00 70.78 C ANISOU 668 CD1 PHE A 133 8185 8721 9988 -345 993 605 C ATOM 669 CD2 PHE A 133 13.969 9.460 6.191 1.00 57.44 C ANISOU 669 CD2 PHE A 133 6125 7166 8534 -300 1012 382 C ATOM 670 CE1 PHE A 133 15.996 7.604 6.007 1.00 55.92 C ANISOU 670 CE1 PHE A 133 6216 6720 8312 -435 893 570 C ATOM 671 CE2 PHE A 133 13.962 8.537 5.169 1.00 51.80 C ANISOU 671 CE2 PHE A 133 5322 6353 8009 -398 890 342 C ATOM 672 CZ PHE A 133 14.977 7.607 5.076 1.00 50.78 C ANISOU 672 CZ PHE A 133 5342 6089 7865 -470 841 430 C ATOM 673 N LEU A 134 14.971 12.812 6.222 1.00 49.83 N ANISOU 673 N LEU A 134 5451 6321 7163 78 837 208 N ATOM 674 CA LEU A 134 14.924 13.378 4.876 1.00 48.86 C ANISOU 674 CA LEU A 134 5284 6164 7115 158 643 113 C ATOM 675 C LEU A 134 16.140 14.253 4.605 1.00 49.05 C ANISOU 675 C LEU A 134 5532 6127 6978 229 529 98 C ATOM 676 O LEU A 134 16.725 14.197 3.517 1.00 57.96 O ANISOU 676 O LEU A 134 6709 7193 8118 226 374 84 O ATOM 677 CB LEU A 134 13.638 14.182 4.687 1.00 49.63 C ANISOU 677 CB LEU A 134 5194 6341 7321 278 668 16 C ATOM 678 CG LEU A 134 12.326 13.404 4.600 1.00 52.73 C ANISOU 678 CG LEU A 134 5292 6803 7938 208 740 -11 C ATOM 679 CD1 LEU A 134 11.151 14.361 4.499 1.00 56.29 C ANISOU 679 CD1 LEU A 134 5551 7347 8492 366 757 -116 C ATOM 680 CD2 LEU A 134 12.355 12.464 3.408 1.00 50.25 C ANISOU 680 CD2 LEU A 134 4891 6442 7760 111 565 -36 C ATOM 681 N ASP A 135 16.539 15.058 5.591 1.00 52.41 N ANISOU 681 N ASP A 135 6092 6571 7250 282 614 90 N ATOM 682 CA ASP A 135 17.679 15.953 5.433 1.00 56.72 C ANISOU 682 CA ASP A 135 6832 7048 7671 326 524 57 C ATOM 683 C ASP A 135 18.947 15.180 5.087 1.00 49.83 C ANISOU 683 C ASP A 135 6053 6119 6760 226 426 119 C ATOM 684 O ASP A 135 19.557 15.400 4.035 1.00 48.87 O ANISOU 684 O ASP A 135 5979 5928 6659 231 306 98 O ATOM 685 CB ASP A 135 17.856 16.775 6.714 1.00 52.89 C ANISOU 685 CB ASP A 135 6461 6603 7033 373 638 11 C ATOM 686 CG ASP A 135 19.179 17.504 6.765 1.00 52.98 C ANISOU 686 CG ASP A 135 6661 6543 6925 368 552 -33 C ATOM 687 OD1 ASP A 135 20.180 16.888 7.187 1.00 61.06 O ANISOU 687 OD1 ASP A 135 7761 7580 7857 283 515 18 O ATOM 688 OD2 ASP A 135 19.220 18.690 6.380 1.00 62.69 O ANISOU 688 OD2 ASP A 135 7954 7694 8170 450 522 -117 O ATOM 689 N VAL A 136 19.353 14.259 5.965 1.00 48.79 N ANISOU 689 N VAL A 136 5951 6017 6570 145 485 203 N ATOM 690 CA VAL A 136 20.561 13.470 5.729 1.00 50.88 C ANISOU 690 CA VAL A 136 6287 6227 6818 75 393 262 C ATOM 691 C VAL A 136 20.452 12.702 4.419 1.00 47.58 C ANISOU 691 C VAL A 136 5780 5741 6556 32 308 260 C ATOM 692 O VAL A 136 21.407 12.642 3.634 1.00 44.27 O ANISOU 692 O VAL A 136 5418 5264 6139 20 207 240 O ATOM 693 CB VAL A 136 20.820 12.525 6.916 1.00 46.17 C ANISOU 693 CB VAL A 136 5733 5669 6142 24 471 381 C ATOM 694 CG1 VAL A 136 22.127 11.770 6.723 1.00 45.45 C ANISOU 694 CG1 VAL A 136 5707 5517 6045 -14 362 439 C ATOM 695 CG2 VAL A 136 20.825 13.304 8.222 1.00 47.67 C ANISOU 695 CG2 VAL A 136 6021 5957 6135 74 555 361 C ATOM 696 N LEU A 137 19.282 12.112 4.162 1.00 45.33 N ANISOU 696 N LEU A 137 5346 5471 6407 4 353 262 N ATOM 697 CA LEU A 137 19.070 11.312 2.960 1.00 43.95 C ANISOU 697 CA LEU A 137 5078 5242 6377 -46 262 228 C ATOM 698 C LEU A 137 19.383 12.107 1.698 1.00 51.10 C ANISOU 698 C LEU A 137 6029 6136 7251 25 128 142 C ATOM 699 O LEU A 137 20.262 11.736 0.912 1.00 62.24 O ANISOU 699 O LEU A 137 7504 7491 8654 -2 48 128 O ATOM 700 CB LEU A 137 17.625 10.806 2.934 1.00 45.05 C ANISOU 700 CB LEU A 137 5019 5420 6678 -87 325 206 C ATOM 701 CG LEU A 137 17.129 10.181 1.634 1.00 46.41 C ANISOU 701 CG LEU A 137 5063 5566 7004 -130 206 116 C ATOM 702 CD1 LEU A 137 17.854 8.877 1.385 1.00 60.50 C ANISOU 702 CD1 LEU A 137 6890 7237 8862 -239 186 146 C ATOM 703 CD2 LEU A 137 15.625 9.968 1.693 1.00 48.74 C ANISOU 703 CD2 LEU A 137 5123 5928 7470 -161 259 65 C ATOM 704 N PHE A 138 18.671 13.218 1.498 1.00 44.52 N ANISOU 704 N PHE A 138 5170 5349 6396 127 116 93 N ATOM 705 CA PHE A 138 18.848 14.008 0.286 1.00 44.28 C ANISOU 705 CA PHE A 138 5202 5300 6322 210 -3 45 C ATOM 706 C PHE A 138 20.244 14.615 0.212 1.00 47.03 C ANISOU 706 C PHE A 138 5737 5580 6550 208 -10 64 C ATOM 707 O PHE A 138 20.867 14.623 -0.857 1.00 62.44 O ANISOU 707 O PHE A 138 7759 7495 8468 206 -84 51 O ATOM 708 CB PHE A 138 17.786 15.101 0.228 1.00 44.69 C ANISOU 708 CB PHE A 138 5196 5396 6388 345 -9 10 C ATOM 709 CG PHE A 138 16.380 14.584 0.175 1.00 46.25 C ANISOU 709 CG PHE A 138 5164 5679 6732 352 -15 -32 C ATOM 710 CD1 PHE A 138 16.075 13.419 -0.512 1.00 45.56 C ANISOU 710 CD1 PHE A 138 4954 5609 6748 259 -90 -68 C ATOM 711 CD2 PHE A 138 15.359 15.267 0.813 1.00 48.22 C ANISOU 711 CD2 PHE A 138 5302 5986 7034 447 63 -56 C ATOM 712 CE1 PHE A 138 14.776 12.949 -0.559 1.00 47.31 C ANISOU 712 CE1 PHE A 138 4932 5908 7135 241 -98 -128 C ATOM 713 CE2 PHE A 138 14.061 14.803 0.771 1.00 47.66 C ANISOU 713 CE2 PHE A 138 4978 6005 7126 446 68 -107 C ATOM 714 CZ PHE A 138 13.768 13.642 0.084 1.00 47.82 C ANISOU 714 CZ PHE A 138 4863 6046 7262 333 -16 -143 C ATOM 715 N SER A 139 20.750 15.132 1.336 1.00 48.12 N ANISOU 715 N SER A 139 5952 5710 6621 204 70 83 N ATOM 716 CA SER A 139 22.071 15.756 1.339 1.00 46.18 C ANISOU 716 CA SER A 139 5851 5404 6292 184 61 77 C ATOM 717 C SER A 139 23.148 14.767 0.917 1.00 44.82 C ANISOU 717 C SER A 139 5687 5208 6134 97 22 97 C ATOM 718 O SER A 139 24.104 15.135 0.225 1.00 47.40 O ANISOU 718 O SER A 139 6092 5486 6434 81 -3 79 O ATOM 719 CB SER A 139 22.382 16.327 2.723 1.00 45.68 C ANISOU 719 CB SER A 139 5845 5358 6152 182 133 62 C ATOM 720 OG SER A 139 21.392 17.256 3.123 1.00 53.16 O ANISOU 720 OG SER A 139 6786 6318 7094 275 190 22 O ATOM 721 N THR A 140 23.006 13.503 1.320 1.00 48.93 N ANISOU 721 N THR A 140 6128 5750 6713 44 31 136 N ATOM 722 CA THR A 140 23.934 12.474 0.869 1.00 40.38 C ANISOU 722 CA THR A 140 5042 4624 5675 -14 -5 146 C ATOM 723 C THR A 140 23.691 12.122 -0.593 1.00 41.84 C ANISOU 723 C THR A 140 5202 4787 5909 -14 -63 91 C ATOM 724 O THR A 140 24.643 11.906 -1.352 1.00 52.26 O ANISOU 724 O THR A 140 6565 6072 7221 -32 -84 61 O ATOM 725 CB THR A 140 23.801 11.231 1.747 1.00 40.78 C ANISOU 725 CB THR A 140 5037 4671 5788 -59 30 220 C ATOM 726 OG1 THR A 140 23.803 11.620 3.126 1.00 47.65 O ANISOU 726 OG1 THR A 140 5946 5594 6564 -44 85 274 O ATOM 727 CG2 THR A 140 24.952 10.273 1.497 1.00 40.15 C ANISOU 727 CG2 THR A 140 4968 4527 5759 -90 -7 235 C ATOM 728 N ALA A 141 22.420 12.072 -1.003 1.00 41.05 N ANISOU 728 N ALA A 141 5023 4722 5854 11 -89 64 N ATOM 729 CA ALA A 141 22.080 11.661 -2.362 1.00 41.60 C ANISOU 729 CA ALA A 141 5063 4796 5947 16 -173 -9 C ATOM 730 C ALA A 141 22.733 12.560 -3.400 1.00 43.59 C ANISOU 730 C ALA A 141 5444 5046 6074 70 -207 -28 C ATOM 731 O ALA A 141 23.213 12.081 -4.434 1.00 42.60 O ANISOU 731 O ALA A 141 5355 4912 5921 54 -241 -81 O ATOM 732 CB ALA A 141 20.562 11.655 -2.548 1.00 42.65 C ANISOU 732 CB ALA A 141 5064 4992 6147 46 -220 -48 C ATOM 733 N SER A 142 22.757 13.870 -3.145 1.00 47.46 N ANISOU 733 N SER A 142 6015 5532 6487 134 -180 12 N ATOM 734 CA SER A 142 23.370 14.801 -4.087 1.00 45.29 C ANISOU 734 CA SER A 142 5882 5225 6100 176 -181 24 C ATOM 735 C SER A 142 24.855 14.510 -4.257 1.00 43.85 C ANISOU 735 C SER A 142 5760 4998 5903 96 -119 17 C ATOM 736 O SER A 142 25.363 14.451 -5.383 1.00 45.53 O ANISOU 736 O SER A 142 6044 5209 6047 94 -116 -3 O ATOM 737 CB SER A 142 23.156 16.238 -3.614 1.00 48.34 C ANISOU 737 CB SER A 142 6347 5569 6449 248 -143 69 C ATOM 738 OG SER A 142 23.860 16.478 -2.407 1.00 69.88 O ANISOU 738 OG SER A 142 9086 8262 9206 188 -66 71 O ATOM 739 N ILE A 143 25.565 14.326 -3.141 1.00 40.53 N ANISOU 739 N ILE A 143 5306 4556 5540 37 -70 28 N ATOM 740 CA ILE A 143 27.007 14.092 -3.190 1.00 39.76 C ANISOU 740 CA ILE A 143 5223 4428 5457 -29 -22 11 C ATOM 741 C ILE A 143 27.316 12.826 -3.976 1.00 41.08 C ANISOU 741 C ILE A 143 5342 4600 5665 -50 -38 -36 C ATOM 742 O ILE A 143 28.140 12.830 -4.899 1.00 41.52 O ANISOU 742 O ILE A 143 5443 4646 5686 -66 7 -72 O ATOM 743 CB ILE A 143 27.590 14.018 -1.767 1.00 40.97 C ANISOU 743 CB ILE A 143 5328 4584 5655 -65 -11 26 C ATOM 744 CG1 ILE A 143 27.238 15.276 -0.974 1.00 41.78 C ANISOU 744 CG1 ILE A 143 5487 4679 5709 -45 9 35 C ATOM 745 CG2 ILE A 143 29.097 13.809 -1.821 1.00 38.90 C ANISOU 745 CG2 ILE A 143 5042 4306 5432 -120 16 -4 C ATOM 746 CD1 ILE A 143 27.689 15.214 0.465 1.00 43.16 C ANISOU 746 CD1 ILE A 143 5629 4887 5882 -71 1 32 C ATOM 747 N TRP A 144 26.658 11.720 -3.622 1.00 39.51 N ANISOU 747 N TRP A 144 5055 4406 5550 -55 -83 -44 N ATOM 748 CA TRP A 144 26.930 10.454 -4.291 1.00 43.85 C ANISOU 748 CA TRP A 144 5563 4928 6170 -76 -95 -110 C ATOM 749 C TRP A 144 26.499 10.482 -5.751 1.00 40.84 C ANISOU 749 C TRP A 144 5234 4582 5703 -52 -129 -190 C ATOM 750 O TRP A 144 27.106 9.802 -6.586 1.00 42.65 O ANISOU 750 O TRP A 144 5476 4795 5933 -64 -109 -273 O ATOM 751 CB TRP A 144 26.251 9.313 -3.538 1.00 44.12 C ANISOU 751 CB TRP A 144 5504 4925 6336 -102 -121 -90 C ATOM 752 CG TRP A 144 27.063 8.834 -2.376 1.00 47.59 C ANISOU 752 CG TRP A 144 5916 5322 6846 -112 -91 -15 C ATOM 753 CD1 TRP A 144 26.951 9.227 -1.075 1.00 54.89 C ANISOU 753 CD1 TRP A 144 6839 6274 7741 -107 -80 79 C ATOM 754 CD2 TRP A 144 28.130 7.881 -2.416 1.00 61.87 C ANISOU 754 CD2 TRP A 144 7697 7062 8748 -109 -81 -31 C ATOM 755 NE1 TRP A 144 27.877 8.570 -0.300 1.00 49.65 N ANISOU 755 NE1 TRP A 144 6159 5578 7130 -98 -83 135 N ATOM 756 CE2 TRP A 144 28.613 7.738 -1.101 1.00 55.31 C ANISOU 756 CE2 TRP A 144 6849 6226 7938 -93 -86 73 C ATOM 757 CE3 TRP A 144 28.720 7.130 -3.438 1.00 52.74 C ANISOU 757 CE3 TRP A 144 6532 5853 7655 -104 -68 -131 C ATOM 758 CZ2 TRP A 144 29.659 6.876 -0.780 1.00 46.00 C ANISOU 758 CZ2 TRP A 144 5634 4989 6856 -58 -97 97 C ATOM 759 CZ3 TRP A 144 29.758 6.275 -3.118 1.00 43.28 C ANISOU 759 CZ3 TRP A 144 5290 4583 6573 -74 -55 -123 C ATOM 760 CH2 TRP A 144 30.217 6.155 -1.801 1.00 43.93 C ANISOU 760 CH2 TRP A 144 5345 4658 6689 -45 -79 -2 C ATOM 761 N HIS A 145 25.462 11.258 -6.078 1.00 41.54 N ANISOU 761 N HIS A 145 5353 4723 5706 -4 -185 -174 N ATOM 762 CA HIS A 145 25.126 11.490 -7.479 1.00 43.04 C ANISOU 762 CA HIS A 145 5624 4971 5760 45 -239 -231 C ATOM 763 C HIS A 145 26.304 12.100 -8.227 1.00 45.39 C ANISOU 763 C HIS A 145 6056 5260 5931 47 -142 -215 C ATOM 764 O HIS A 145 26.678 11.632 -9.308 1.00 45.37 O ANISOU 764 O HIS A 145 6108 5287 5844 48 -128 -295 O ATOM 765 CB HIS A 145 23.899 12.395 -7.588 1.00 44.27 C ANISOU 765 CB HIS A 145 5788 5184 5846 129 -326 -188 C ATOM 766 CG HIS A 145 22.599 11.655 -7.636 1.00 47.16 C ANISOU 766 CG HIS A 145 6015 5605 6300 132 -444 -264 C ATOM 767 ND1 HIS A 145 21.953 11.208 -6.504 1.00 48.43 N ANISOU 767 ND1 HIS A 145 6029 5744 6627 87 -431 -248 N ATOM 768 CD2 HIS A 145 21.821 11.289 -8.682 1.00 54.58 C ANISOU 768 CD2 HIS A 145 6928 6627 7183 167 -576 -365 C ATOM 769 CE1 HIS A 145 20.834 10.597 -6.850 1.00 69.98 C ANISOU 769 CE1 HIS A 145 8630 8527 9432 78 -534 -337 C ATOM 770 NE2 HIS A 145 20.731 10.632 -8.166 1.00 56.11 N ANISOU 770 NE2 HIS A 145 6936 6839 7546 128 -641 -421 N ATOM 771 N LEU A 146 26.906 13.150 -7.658 1.00 47.24 N ANISOU 771 N LEU A 146 6343 5451 6154 37 -60 -124 N ATOM 772 CA LEU A 146 28.055 13.779 -8.302 1.00 47.21 C ANISOU 772 CA LEU A 146 6448 5423 6065 11 64 -103 C ATOM 773 C LEU A 146 29.215 12.804 -8.437 1.00 51.11 C ANISOU 773 C LEU A 146 6872 5909 6639 -50 143 -186 C ATOM 774 O LEU A 146 29.891 12.773 -9.472 1.00 47.07 O ANISOU 774 O LEU A 146 6431 5418 6034 -59 235 -225 O ATOM 775 CB LEU A 146 28.494 15.018 -7.519 1.00 44.56 C ANISOU 775 CB LEU A 146 6153 5020 5759 -17 136 -18 C ATOM 776 CG LEU A 146 27.653 16.283 -7.686 1.00 49.01 C ANISOU 776 CG LEU A 146 6839 5553 6230 60 110 72 C ATOM 777 CD1 LEU A 146 28.541 17.505 -7.572 1.00 45.81 C ANISOU 777 CD1 LEU A 146 6535 5045 5826 5 243 134 C ATOM 778 CD2 LEU A 146 26.920 16.277 -9.015 1.00 66.10 C ANISOU 778 CD2 LEU A 146 9109 7780 8226 154 44 88 C ATOM 779 N CYS A 147 29.463 12.006 -7.396 1.00 52.37 N ANISOU 779 N CYS A 147 6896 6039 6964 -81 115 -207 N ATOM 780 CA CYS A 147 30.522 11.004 -7.456 1.00 46.49 C ANISOU 780 CA CYS A 147 6067 5272 6325 -107 172 -283 C ATOM 781 C CYS A 147 30.296 10.040 -8.615 1.00 47.75 C ANISOU 781 C CYS A 147 6251 5450 6441 -81 164 -398 C ATOM 782 O CYS A 147 31.201 9.799 -9.422 1.00 56.30 O ANISOU 782 O CYS A 147 7353 6544 7494 -86 270 -474 O ATOM 783 CB CYS A 147 30.598 10.255 -6.125 1.00 44.68 C ANISOU 783 CB CYS A 147 5713 5001 6262 -112 112 -256 C ATOM 784 SG CYS A 147 31.824 8.932 -6.060 1.00 47.23 S ANISOU 784 SG CYS A 147 5918 5273 6752 -101 151 -331 S ATOM 785 N ALA A 148 29.080 9.497 -8.727 1.00 46.99 N ANISOU 785 N ALA A 148 6147 5363 6344 -60 47 -433 N ATOM 786 CA ALA A 148 28.785 8.558 -9.806 1.00 51.12 C ANISOU 786 CA ALA A 148 6691 5903 6829 -47 15 -580 C ATOM 787 C ALA A 148 28.928 9.218 -11.171 1.00 48.68 C ANISOU 787 C ALA A 148 6534 5688 6276 -13 62 -615 C ATOM 788 O ALA A 148 29.441 8.603 -12.113 1.00 46.40 O ANISOU 788 O ALA A 148 6285 5419 5924 -6 123 -745 O ATOM 789 CB ALA A 148 27.380 7.981 -9.632 1.00 46.60 C ANISOU 789 CB ALA A 148 6058 5329 6319 -52 -130 -620 C ATOM 790 N ILE A 149 28.478 10.470 -11.297 1.00 45.83 N ANISOU 790 N ILE A 149 6272 5376 5765 18 42 -496 N ATOM 791 CA ILE A 149 28.624 11.193 -12.558 1.00 48.20 C ANISOU 791 CA ILE A 149 6752 5756 5807 62 97 -481 C ATOM 792 C ILE A 149 30.096 11.331 -12.925 1.00 47.61 C ANISOU 792 C ILE A 149 6717 5662 5712 16 312 -487 C ATOM 793 O ILE A 149 30.480 11.160 -14.089 1.00 48.97 O ANISOU 793 O ILE A 149 6998 5900 5708 35 399 -560 O ATOM 794 CB ILE A 149 27.928 12.566 -12.474 1.00 54.05 C ANISOU 794 CB ILE A 149 7596 6509 6432 117 47 -319 C ATOM 795 CG1 ILE A 149 26.406 12.399 -12.446 1.00 48.17 C ANISOU 795 CG1 ILE A 149 6802 5823 5676 187 -167 -344 C ATOM 796 CG2 ILE A 149 28.346 13.456 -13.637 1.00 49.20 C ANISOU 796 CG2 ILE A 149 7197 5938 5558 157 153 -243 C ATOM 797 CD1 ILE A 149 25.657 13.715 -12.437 1.00 48.70 C ANISOU 797 CD1 ILE A 149 6964 5901 5639 280 -229 -195 C ATOM 798 N SER A 150 30.944 11.635 -11.938 1.00 48.33 N ANISOU 798 N SER A 150 6709 5675 5980 -45 402 -423 N ATOM 799 CA SER A 150 32.381 11.725 -12.184 1.00 46.87 C ANISOU 799 CA SER A 150 6500 5477 5832 -100 605 -446 C ATOM 800 C SER A 150 32.919 10.416 -12.746 1.00 47.32 C ANISOU 800 C SER A 150 6489 5553 5937 -83 657 -620 C ATOM 801 O SER A 150 33.618 10.405 -13.766 1.00 48.58 O ANISOU 801 O SER A 150 6721 5765 5973 -85 820 -684 O ATOM 802 CB SER A 150 33.111 12.094 -10.893 1.00 45.78 C ANISOU 802 CB SER A 150 6219 5268 5907 -163 634 -386 C ATOM 803 OG SER A 150 32.516 13.219 -10.274 1.00 66.41 O ANISOU 803 OG SER A 150 8892 7846 8493 -173 576 -258 O ATOM 804 N VAL A 151 32.593 9.299 -12.092 1.00 46.44 N ANISOU 804 N VAL A 151 6248 5390 6008 -65 535 -698 N ATOM 805 CA VAL A 151 33.063 7.990 -12.542 1.00 55.10 C ANISOU 805 CA VAL A 151 7279 6461 7194 -38 577 -874 C ATOM 806 C VAL A 151 32.595 7.712 -13.965 1.00 68.34 C ANISOU 806 C VAL A 151 9107 8223 8635 -3 584 -1007 C ATOM 807 O VAL A 151 33.370 7.244 -14.808 1.00 50.41 O ANISOU 807 O VAL A 151 6860 5982 6312 15 730 -1144 O ATOM 808 CB VAL A 151 32.595 6.895 -11.565 1.00 51.27 C ANISOU 808 CB VAL A 151 6663 5869 6946 -26 436 -901 C ATOM 809 CG1 VAL A 151 33.060 5.523 -12.032 1.00 46.71 C ANISOU 809 CG1 VAL A 151 6031 5223 6492 11 481 -1088 C ATOM 810 CG2 VAL A 151 33.100 7.192 -10.158 1.00 44.65 C ANISOU 810 CG2 VAL A 151 5701 4977 6288 -45 420 -764 C ATOM 811 N ASP A 152 31.324 8.004 -14.257 1.00 65.72 N ANISOU 811 N ASP A 152 8874 7947 8149 17 423 -982 N ATOM 812 CA ASP A 152 30.799 7.794 -15.603 1.00 50.75 C ANISOU 812 CA ASP A 152 7129 6162 5992 61 384 -1113 C ATOM 813 C ASP A 152 31.567 8.616 -16.627 1.00 52.14 C ANISOU 813 C ASP A 152 7476 6437 5897 77 579 -1068 C ATOM 814 O ASP A 152 32.034 8.087 -17.642 1.00 53.65 O ANISOU 814 O ASP A 152 7745 6694 5945 100 688 -1227 O ATOM 815 CB ASP A 152 29.312 8.145 -15.648 1.00 65.11 C ANISOU 815 CB ASP A 152 8994 8042 7701 92 155 -1069 C ATOM 816 CG ASP A 152 28.480 7.231 -14.792 1.00 95.61 C ANISOU 816 CG ASP A 152 12688 11815 11823 58 -7 -1136 C ATOM 817 OD1 ASP A 152 28.952 6.112 -14.509 1.00105.35 O ANISOU 817 OD1 ASP A 152 13821 12943 13265 25 38 -1259 O ATOM 818 OD2 ASP A 152 27.364 7.628 -14.401 1.00101.56 O ANISOU 818 OD2 ASP A 152 13409 12596 12583 67 -165 -1061 O ATOM 819 N ARG A 153 31.709 9.920 -16.374 1.00 51.79 N ANISOU 819 N ARG A 153 7502 6394 5782 60 642 -854 N ATOM 820 CA ARG A 153 32.415 10.788 -17.309 1.00 63.36 C ANISOU 820 CA ARG A 153 9146 7927 7000 58 855 -772 C ATOM 821 C ARG A 153 33.846 10.322 -17.536 1.00 72.28 C ANISOU 821 C ARG A 153 10192 9045 8226 9 1116 -877 C ATOM 822 O ARG A 153 34.416 10.570 -18.606 1.00 62.05 O ANISOU 822 O ARG A 153 9042 7835 6698 13 1319 -895 O ATOM 823 CB ARG A 153 32.396 12.232 -16.805 1.00 52.64 C ANISOU 823 CB ARG A 153 7853 6513 5637 28 893 -526 C ATOM 824 N TYR A 154 34.437 9.638 -16.555 1.00 65.64 N ANISOU 824 N TYR A 154 9117 8105 7717 -26 1120 -944 N ATOM 825 CA TYR A 154 35.788 9.115 -16.720 1.00 54.54 C ANISOU 825 CA TYR A 154 7587 6690 6446 -48 1347 -1062 C ATOM 826 C TYR A 154 35.797 7.849 -17.569 1.00 55.83 C ANISOU 826 C TYR A 154 7770 6892 6552 20 1365 -1310 C ATOM 827 O TYR A 154 36.583 7.736 -18.516 1.00 70.13 O ANISOU 827 O TYR A 154 9637 8778 8230 30 1596 -1414 O ATOM 828 CB TYR A 154 36.420 8.842 -15.355 1.00 58.63 C ANISOU 828 CB TYR A 154 7846 7097 7331 -81 1312 -1038 C ATOM 829 CG TYR A 154 37.654 7.980 -15.447 1.00 51.77 C ANISOU 829 CG TYR A 154 6801 6211 6657 -60 1479 -1197 C ATOM 830 CD1 TYR A 154 38.818 8.466 -16.024 1.00 59.49 C ANISOU 830 CD1 TYR A 154 7748 7250 7606 -106 1761 -1212 C ATOM 831 CD2 TYR A 154 37.653 6.676 -14.970 1.00 51.31 C ANISOU 831 CD2 TYR A 154 6603 6066 6828 11 1369 -1329 C ATOM 832 CE1 TYR A 154 39.948 7.682 -16.121 1.00 61.74 C ANISOU 832 CE1 TYR A 154 7841 7530 8088 -70 1921 -1372 C ATOM 833 CE2 TYR A 154 38.781 5.883 -15.062 1.00 52.12 C ANISOU 833 CE2 TYR A 154 6537 6141 7126 61 1516 -1476 C ATOM 834 CZ TYR A 154 39.925 6.392 -15.638 1.00 53.38 C ANISOU 834 CZ TYR A 154 6642 6382 7256 26 1788 -1505 C ATOM 835 OH TYR A 154 41.053 5.612 -15.734 1.00 56.96 O ANISOU 835 OH TYR A 154 6898 6819 7925 91 1942 -1664 O ATOM 836 N ILE A 155 34.940 6.880 -17.231 1.00 56.30 N ANISOU 836 N ILE A 155 7780 6891 6722 59 1142 -1419 N ATOM 837 CA ILE A 155 34.870 5.640 -18.001 1.00 54.67 C ANISOU 837 CA ILE A 155 7595 6688 6489 115 1141 -1684 C ATOM 838 C ILE A 155 34.494 5.924 -19.449 1.00 56.82 C ANISOU 838 C ILE A 155 8115 7130 6345 147 1186 -1769 C ATOM 839 O ILE A 155 34.976 5.250 -20.367 1.00 58.71 O ANISOU 839 O ILE A 155 8410 7422 6476 187 1325 -1987 O ATOM 840 CB ILE A 155 33.883 4.655 -17.340 1.00 54.62 C ANISOU 840 CB ILE A 155 7501 6562 6692 122 888 -1764 C ATOM 841 CG1 ILE A 155 34.312 4.345 -15.905 1.00 51.85 C ANISOU 841 CG1 ILE A 155 6936 6052 6715 107 856 -1657 C ATOM 842 CG2 ILE A 155 33.785 3.370 -18.146 1.00 59.27 C ANISOU 842 CG2 ILE A 155 8119 7122 7279 165 884 -2066 C ATOM 843 CD1 ILE A 155 33.402 3.356 -15.208 1.00 51.06 C ANISOU 843 CD1 ILE A 155 6759 5810 6832 103 653 -1705 C ATOM 844 N ALA A 156 33.642 6.928 -19.681 1.00 56.99 N ANISOU 844 N ALA A 156 8297 7243 6112 146 1069 -1600 N ATOM 845 CA ALA A 156 33.296 7.308 -21.047 1.00 59.31 C ANISOU 845 CA ALA A 156 8853 7716 5965 198 1095 -1638 C ATOM 846 C ALA A 156 34.529 7.719 -21.842 1.00 60.75 C ANISOU 846 C ALA A 156 9137 7976 5969 189 1445 -1624 C ATOM 847 O ALA A 156 34.583 7.512 -23.060 1.00 63.49 O ANISOU 847 O ALA A 156 9674 8468 5981 240 1539 -1761 O ATOM 848 CB ALA A 156 32.264 8.435 -21.035 1.00 59.22 C ANISOU 848 CB ALA A 156 8982 7768 5750 222 914 -1409 C ATOM 849 N ILE A 157 35.527 8.299 -21.173 1.00 77.61 N ANISOU 849 N ILE A 157 11140 10027 8319 118 1648 -1473 N ATOM 850 CA ILE A 157 36.789 8.612 -21.834 1.00 61.11 C ANISOU 850 CA ILE A 157 9086 7998 6136 85 2016 -1477 C ATOM 851 C ILE A 157 37.634 7.356 -21.992 1.00 62.82 C ANISOU 851 C ILE A 157 9135 8193 6542 117 2158 -1761 C ATOM 852 O ILE A 157 38.250 7.136 -23.041 1.00 63.92 O ANISOU 852 O ILE A 157 9376 8444 6468 144 2410 -1899 O ATOM 853 CB ILE A 157 37.543 9.703 -21.050 1.00 59.96 C ANISOU 853 CB ILE A 157 8828 7766 6187 -21 2170 -1238 C ATOM 854 CG1 ILE A 157 36.675 10.952 -20.894 1.00 59.48 C ANISOU 854 CG1 ILE A 157 8948 7693 5959 -36 2033 -968 C ATOM 855 CG2 ILE A 157 38.859 10.044 -21.735 1.00 61.68 C ANISOU 855 CG2 ILE A 157 9049 8044 6341 -80 2577 -1244 C ATOM 856 CD1 ILE A 157 37.348 12.057 -20.111 1.00 58.50 C ANISOU 856 CD1 ILE A 157 8729 7459 6038 -153 2171 -758 C ATOM 857 N LYS A 158 37.672 6.514 -20.957 1.00 79.00 N ANISOU 857 N LYS A 158 10936 10094 8985 126 2011 -1846 N ATOM 858 CA LYS A 158 38.495 5.310 -20.998 1.00 63.91 C ANISOU 858 CA LYS A 158 8851 8122 7309 180 2134 -2100 C ATOM 859 C LYS A 158 38.009 4.351 -22.078 1.00 62.63 C ANISOU 859 C LYS A 158 8850 8025 6923 259 2102 -2385 C ATOM 860 O LYS A 158 38.752 4.007 -23.004 1.00 64.73 O ANISOU 860 O LYS A 158 9165 8376 7053 300 2361 -2571 O ATOM 861 CB LYS A 158 38.496 4.632 -19.625 1.00 69.07 C ANISOU 861 CB LYS A 158 9247 8588 8409 191 1945 -2088 C ATOM 862 N LYS A 159 36.754 3.910 -21.978 1.00 74.31 N ANISOU 862 N LYS A 159 10402 9469 8362 275 1792 -2442 N ATOM 863 CA LYS A 159 36.160 2.956 -22.914 1.00 71.68 C ANISOU 863 CA LYS A 159 10205 9184 7847 332 1703 -2746 C ATOM 864 C LYS A 159 35.023 3.639 -23.660 1.00 70.52 C ANISOU 864 C LYS A 159 10315 9216 7264 332 1520 -2680 C ATOM 865 O LYS A 159 33.866 3.606 -23.211 1.00 64.09 O ANISOU 865 O LYS A 159 9486 8363 6502 314 1212 -2635 O ATOM 866 CB LYS A 159 35.662 1.710 -22.183 1.00 62.98 C ANISOU 866 CB LYS A 159 8942 7872 7118 341 1488 -2911 C ATOM 867 N PRO A 160 35.300 4.263 -24.809 1.00 79.56 N ANISOU 867 N PRO A 160 11696 10564 7970 362 1701 -2669 N ATOM 868 CA PRO A 160 34.251 5.005 -25.522 1.00 88.91 C ANISOU 868 CA PRO A 160 13138 11929 8713 392 1512 -2566 C ATOM 869 C PRO A 160 33.372 4.114 -26.384 1.00 87.13 C ANISOU 869 C PRO A 160 13039 11810 8259 450 1291 -2889 C ATOM 870 O PRO A 160 32.228 4.467 -26.687 1.00 82.27 O ANISOU 870 O PRO A 160 12549 11311 7400 479 1005 -2846 O ATOM 871 CB PRO A 160 35.054 5.992 -26.378 1.00 74.30 C ANISOU 871 CB PRO A 160 11501 10237 6493 403 1839 -2403 C ATOM 872 CG PRO A 160 36.320 5.259 -26.665 1.00 71.14 C ANISOU 872 CG PRO A 160 11000 9811 6219 403 2178 -2623 C ATOM 873 CD PRO A 160 36.625 4.450 -25.426 1.00 68.77 C ANISOU 873 CD PRO A 160 10360 9271 6497 370 2106 -2698 C ATOM 874 N ILE A 161 33.897 2.957 -26.791 1.00 75.40 N ANISOU 874 N ILE A 161 11509 10282 6857 471 1413 -3233 N ATOM 875 CA ILE A 161 33.132 2.059 -27.646 1.00 89.33 C ANISOU 875 CA ILE A 161 13392 12136 8413 512 1215 -3595 C ATOM 876 C ILE A 161 32.146 1.214 -26.853 1.00103.51 C ANISOU 876 C ILE A 161 14993 13746 10591 457 880 -3725 C ATOM 877 O ILE A 161 31.200 0.669 -27.435 1.00120.94 O ANISOU 877 O ILE A 161 17278 16033 12643 463 626 -3982 O ATOM 878 CB ILE A 161 34.073 1.150 -28.454 1.00 81.72 C ANISOU 878 CB ILE A 161 12477 11189 7383 561 1496 -3945 C ATOM 879 N GLN A 162 32.334 1.094 -25.540 1.00102.23 N ANISOU 879 N GLN A 162 14581 13345 10917 399 876 -3557 N ATOM 880 CA GLN A 162 31.486 0.238 -24.713 1.00106.75 C ANISOU 880 CA GLN A 162 14966 13712 11882 335 615 -3656 C ATOM 881 C GLN A 162 30.379 1.073 -24.071 1.00119.76 C ANISOU 881 C GLN A 162 16572 15401 13529 292 348 -3382 C ATOM 882 O GLN A 162 30.386 1.371 -22.875 1.00103.49 O ANISOU 882 O GLN A 162 14343 13194 11783 246 334 -3132 O ATOM 883 CB GLN A 162 32.323 -0.482 -23.664 1.00100.59 C ANISOU 883 CB GLN A 162 13957 12648 11616 316 766 -3637 C ATOM 884 N ALA A 163 29.406 1.438 -24.900 1.00119.83 N ANISOU 884 N ALA A 163 16736 15627 13167 320 128 -3446 N ATOM 885 CA ALA A 163 28.250 2.202 -24.444 1.00102.83 C ANISOU 885 CA ALA A 163 14540 13538 10993 307 -146 -3229 C ATOM 886 C ALA A 163 27.092 2.106 -25.435 1.00 89.82 C ANISOU 886 C ALA A 163 13008 12109 9012 344 -450 -3440 C ATOM 887 O ALA A 163 27.231 1.541 -26.521 1.00 91.12 O ANISOU 887 O ALA A 163 13321 12394 8905 380 -442 -3745 O ATOM 888 CB ALA A 163 28.633 3.655 -24.217 1.00103.23 C ANISOU 888 CB ALA A 163 14682 13670 10870 353 -20 -2833 C ATOM 889 N ASN A 167 25.677 1.567 -21.807 1.00112.82 N ANISOU 889 N ASN A 167 15236 14458 13172 93 -697 -3083 N ATOM 890 CA ASN A 167 24.934 2.763 -21.426 1.00113.66 C ANISOU 890 CA ASN A 167 15327 14685 13174 133 -834 -2798 C ATOM 891 C ASN A 167 23.521 2.744 -21.998 1.00122.41 C ANISOU 891 C ASN A 167 16403 15966 14143 143 -1169 -2953 C ATOM 892 O ASN A 167 23.175 3.558 -22.855 1.00101.65 O ANISOU 892 O ASN A 167 13934 13575 11112 257 -1292 -2904 O ATOM 893 CB ASN A 167 25.668 4.022 -21.890 1.00 98.62 C ANISOU 893 CB ASN A 167 13637 12926 10910 241 -677 -2554 C ATOM 894 N SER A 168 22.708 1.809 -21.523 1.00123.19 N ANISOU 894 N SER A 168 16286 15940 14580 25 -1318 -3136 N ATOM 895 CA SER A 168 21.314 1.726 -21.929 1.00 92.33 C ANISOU 895 CA SER A 168 12272 12185 10624 10 -1648 -3304 C ATOM 896 C SER A 168 20.466 2.518 -20.932 1.00 81.60 C ANISOU 896 C SER A 168 10735 10826 9444 11 -1745 -3026 C ATOM 897 O SER A 168 20.991 3.333 -20.168 1.00 63.93 O ANISOU 897 O SER A 168 8527 8523 7242 55 -1573 -2706 O ATOM 898 CB SER A 168 20.891 0.257 -22.037 1.00 73.97 C ANISOU 898 CB SER A 168 9802 9716 8586 -142 -1739 -3688 C ATOM 899 N ARG A 169 19.149 2.301 -20.933 1.00 64.93 N ANISOU 899 N ARG A 169 8424 8795 7451 -37 -2017 -3166 N ATOM 900 CA ARG A 169 18.307 2.854 -19.878 1.00 63.59 C ANISOU 900 CA ARG A 169 8037 8596 7528 -56 -2076 -2946 C ATOM 901 C ARG A 169 18.422 2.033 -18.599 1.00 93.67 C ANISOU 901 C ARG A 169 11657 12110 11823 -229 -1897 -2906 C ATOM 902 O ARG A 169 18.434 2.594 -17.497 1.00 88.41 O ANISOU 902 O ARG A 169 10916 11360 11318 -227 -1777 -2625 O ATOM 903 CB ARG A 169 16.851 2.924 -20.338 1.00 65.54 C ANISOU 903 CB ARG A 169 8103 9049 7749 -40 -2424 -3115 C ATOM 904 N ALA A 170 18.530 0.706 -18.733 1.00 91.05 N ANISOU 904 N ALA A 170 11268 11611 11715 -373 -1871 -3184 N ATOM 905 CA ALA A 170 18.630 -0.161 -17.563 1.00 61.29 C ANISOU 905 CA ALA A 170 7345 7539 8403 -532 -1700 -3134 C ATOM 906 C ALA A 170 19.868 0.164 -16.739 1.00 60.21 C ANISOU 906 C ALA A 170 7329 7253 8295 -476 -1421 -2839 C ATOM 907 O ALA A 170 19.821 0.143 -15.503 1.00 80.38 O ANISOU 907 O ALA A 170 9770 9652 11117 -535 -1301 -2625 O ATOM 908 CB ALA A 170 18.640 -1.627 -17.995 1.00 62.91 C ANISOU 908 CB ALA A 170 7514 7563 8826 -676 -1712 -3492 C ATOM 909 N THR A 171 20.988 0.460 -17.404 1.00 59.05 N ANISOU 909 N THR A 171 7403 7163 7869 -364 -1311 -2831 N ATOM 910 CA THR A 171 22.185 0.893 -16.688 1.00 61.71 C ANISOU 910 CA THR A 171 7830 7397 8219 -305 -1067 -2564 C ATOM 911 C THR A 171 21.882 2.094 -15.804 1.00 58.62 C ANISOU 911 C THR A 171 7392 7078 7805 -256 -1060 -2239 C ATOM 912 O THR A 171 22.185 2.090 -14.605 1.00 81.37 O ANISOU 912 O THR A 171 10200 9808 10911 -294 -928 -2039 O ATOM 913 CB THR A 171 23.299 1.232 -17.677 1.00 58.77 C ANISOU 913 CB THR A 171 7682 7130 7516 -193 -956 -2609 C ATOM 914 OG1 THR A 171 23.564 0.096 -18.507 1.00 67.88 O ANISOU 914 OG1 THR A 171 8884 8221 8688 -229 -952 -2944 O ATOM 915 CG2 THR A 171 24.571 1.619 -16.930 1.00 55.57 C ANISOU 915 CG2 THR A 171 7325 6617 7172 -151 -709 -2365 C ATOM 916 N ALA A 172 21.262 3.128 -16.381 1.00 56.62 N ANISOU 916 N ALA A 172 7188 7052 7271 -160 -1210 -2187 N ATOM 917 CA ALA A 172 20.928 4.323 -15.613 1.00 55.05 C ANISOU 917 CA ALA A 172 6956 6911 7050 -96 -1207 -1902 C ATOM 918 C ALA A 172 20.020 3.991 -14.436 1.00 68.70 C ANISOU 918 C ALA A 172 8447 8536 9122 -198 -1232 -1845 C ATOM 919 O ALA A 172 20.197 4.530 -13.337 1.00 61.61 O ANISOU 919 O ALA A 172 7514 7568 8326 -192 -1112 -1612 O ATOM 920 CB ALA A 172 20.276 5.366 -16.522 1.00 56.75 C ANISOU 920 CB ALA A 172 7260 7370 6933 42 -1393 -1878 C ATOM 921 N PHE A 173 19.046 3.099 -14.643 1.00 57.53 N ANISOU 921 N PHE A 173 6863 7111 7886 -302 -1376 -2068 N ATOM 922 CA PHE A 173 18.143 2.718 -13.560 1.00 54.97 C ANISOU 922 CA PHE A 173 6300 6684 7902 -421 -1368 -2020 C ATOM 923 C PHE A 173 18.900 2.031 -12.431 1.00 58.10 C ANISOU 923 C PHE A 173 6696 6824 8556 -513 -1136 -1889 C ATOM 924 O PHE A 173 18.680 2.327 -11.250 1.00 64.35 O ANISOU 924 O PHE A 173 7402 7557 9491 -537 -1035 -1679 O ATOM 925 CB PHE A 173 17.034 1.808 -14.089 1.00 57.03 C ANISOU 925 CB PHE A 173 6370 6966 8333 -544 -1554 -2315 C ATOM 926 CG PHE A 173 15.869 2.544 -14.687 1.00 74.07 C ANISOU 926 CG PHE A 173 8411 9385 10349 -463 -1810 -2386 C ATOM 927 CD1 PHE A 173 16.029 3.794 -15.265 1.00 93.95 C ANISOU 927 CD1 PHE A 173 11087 12107 12502 -260 -1897 -2258 C ATOM 928 CD2 PHE A 173 14.603 1.984 -14.657 1.00 99.80 C ANISOU 928 CD2 PHE A 173 11389 12673 13857 -587 -1964 -2576 C ATOM 929 CE1 PHE A 173 14.947 4.465 -15.812 1.00 87.86 C ANISOU 929 CE1 PHE A 173 10209 11570 11604 -153 -2153 -2308 C ATOM 930 CE2 PHE A 173 13.520 2.648 -15.199 1.00108.44 C ANISOU 930 CE2 PHE A 173 12341 14022 14839 -493 -2224 -2651 C ATOM 931 CZ PHE A 173 13.691 3.890 -15.777 1.00 99.98 C ANISOU 931 CZ PHE A 173 11441 13157 13389 -260 -2329 -2511 C ATOM 932 N ILE A 174 19.788 1.096 -12.779 1.00 53.51 N ANISOU 932 N ILE A 174 6213 6091 8027 -552 -1051 -2015 N ATOM 933 CA ILE A 174 20.653 0.469 -11.782 1.00 52.12 C ANISOU 933 CA ILE A 174 6061 5675 8067 -595 -847 -1874 C ATOM 934 C ILE A 174 21.418 1.533 -11.006 1.00 63.28 C ANISOU 934 C ILE A 174 7561 7138 9345 -488 -730 -1582 C ATOM 935 O ILE A 174 21.499 1.492 -9.771 1.00 83.56 O ANISOU 935 O ILE A 174 10078 9598 12074 -519 -621 -1383 O ATOM 936 CB ILE A 174 21.612 -0.531 -12.454 1.00 52.81 C ANISOU 936 CB ILE A 174 6257 5616 8191 -599 -783 -2065 C ATOM 937 CG1 ILE A 174 20.838 -1.670 -13.122 1.00 54.89 C ANISOU 937 CG1 ILE A 174 6433 5791 8633 -727 -894 -2383 C ATOM 938 CG2 ILE A 174 22.612 -1.079 -11.440 1.00 51.52 C ANISOU 938 CG2 ILE A 174 6124 5219 8231 -595 -591 -1892 C ATOM 939 CD1 ILE A 174 21.709 -2.559 -13.984 1.00 55.97 C ANISOU 939 CD1 ILE A 174 6694 5811 8762 -709 -846 -2628 C ATOM 940 N LYS A 175 21.976 2.514 -11.721 1.00 51.07 N ANISOU 940 N LYS A 175 6154 5756 7494 -367 -747 -1555 N ATOM 941 CA LYS A 175 22.774 3.549 -11.069 1.00 69.14 C ANISOU 941 CA LYS A 175 8526 8077 9667 -284 -634 -1311 C ATOM 942 C LYS A 175 21.939 4.376 -10.105 1.00 63.98 C ANISOU 942 C LYS A 175 7781 7480 9049 -280 -657 -1129 C ATOM 943 O LYS A 175 22.374 4.665 -8.984 1.00 73.40 O ANISOU 943 O LYS A 175 8971 8608 10312 -278 -545 -943 O ATOM 944 CB LYS A 175 23.413 4.460 -12.117 1.00 53.08 C ANISOU 944 CB LYS A 175 6661 6194 7312 -177 -634 -1322 C ATOM 945 CG LYS A 175 24.340 3.786 -13.087 1.00 58.33 C ANISOU 945 CG LYS A 175 7431 6832 7901 -165 -571 -1499 C ATOM 946 CD LYS A 175 25.227 4.828 -13.723 1.00 80.61 C ANISOU 946 CD LYS A 175 10419 9774 10435 -72 -483 -1415 C ATOM 947 CE LYS A 175 26.627 4.702 -13.193 1.00 97.11 C ANISOU 947 CE LYS A 175 12521 11753 12626 -70 -288 -1334 C ATOM 948 NZ LYS A 175 27.494 4.207 -14.289 1.00102.42 N ANISOU 948 NZ LYS A 175 13289 12443 13182 -41 -193 -1514 N ATOM 949 N ILE A 176 20.759 4.808 -10.544 1.00 52.84 N ANISOU 949 N ILE A 176 6294 6206 7575 -263 -807 -1191 N ATOM 950 CA ILE A 176 19.868 5.571 -9.675 1.00 52.45 C ANISOU 950 CA ILE A 176 6135 6216 7579 -245 -822 -1047 C ATOM 951 C ILE A 176 19.549 4.769 -8.423 1.00 51.18 C ANISOU 951 C ILE A 176 5833 5907 7704 -364 -716 -980 C ATOM 952 O ILE A 176 19.702 5.254 -7.295 1.00 78.19 O ANISOU 952 O ILE A 176 9255 9301 11152 -349 -605 -793 O ATOM 953 CB ILE A 176 18.584 5.960 -10.432 1.00 53.46 C ANISOU 953 CB ILE A 176 6159 6513 7639 -199 -1023 -1161 C ATOM 954 CG1 ILE A 176 18.915 6.884 -11.606 1.00 65.39 C ANISOU 954 CG1 ILE A 176 7852 8174 8820 -53 -1121 -1169 C ATOM 955 CG2 ILE A 176 17.576 6.605 -9.495 1.00 50.93 C ANISOU 955 CG2 ILE A 176 5680 6242 7429 -180 -1022 -1042 C ATOM 956 CD1 ILE A 176 17.738 7.138 -12.528 1.00 57.23 C ANISOU 956 CD1 ILE A 176 6736 7324 7685 19 -1363 -1300 C ATOM 957 N THR A 177 19.100 3.527 -8.611 1.00 51.99 N ANISOU 957 N THR A 177 5829 5907 8017 -489 -742 -1137 N ATOM 958 CA THR A 177 18.716 2.674 -7.491 1.00 48.94 C ANISOU 958 CA THR A 177 5322 5359 7916 -618 -624 -1062 C ATOM 959 C THR A 177 19.854 2.522 -6.491 1.00 48.59 C ANISOU 959 C THR A 177 5397 5176 7888 -596 -457 -862 C ATOM 960 O THR A 177 19.665 2.718 -5.286 1.00 74.15 O ANISOU 960 O THR A 177 8601 8388 11185 -612 -350 -677 O ATOM 961 CB THR A 177 18.275 1.311 -8.022 1.00 51.80 C ANISOU 961 CB THR A 177 5588 5586 8509 -763 -669 -1281 C ATOM 962 OG1 THR A 177 17.188 1.496 -8.937 1.00 51.79 O ANISOU 962 OG1 THR A 177 5452 5745 8480 -779 -859 -1486 O ATOM 963 CG2 THR A 177 17.827 0.411 -6.881 1.00 55.83 C ANISOU 963 CG2 THR A 177 5985 5900 9329 -911 -522 -1180 C ATOM 964 N VAL A 178 21.050 2.190 -6.979 1.00 46.78 N ANISOU 964 N VAL A 178 5305 4874 7595 -549 -435 -905 N ATOM 965 CA VAL A 178 22.188 1.963 -6.090 1.00 45.61 C ANISOU 965 CA VAL A 178 5245 4604 7482 -514 -307 -736 C ATOM 966 C VAL A 178 22.504 3.222 -5.291 1.00 48.48 C ANISOU 966 C VAL A 178 5658 5091 7673 -429 -268 -542 C ATOM 967 O VAL A 178 22.685 3.172 -4.068 1.00 60.19 O ANISOU 967 O VAL A 178 7142 6519 9208 -433 -181 -366 O ATOM 968 CB VAL A 178 23.407 1.478 -6.893 1.00 45.67 C ANISOU 968 CB VAL A 178 5358 4540 7456 -460 -296 -848 C ATOM 969 CG1 VAL A 178 24.664 1.539 -6.040 1.00 44.54 C ANISOU 969 CG1 VAL A 178 5283 4330 7311 -386 -198 -674 C ATOM 970 CG2 VAL A 178 23.173 0.063 -7.397 1.00 47.36 C ANISOU 970 CG2 VAL A 178 5533 4568 7893 -548 -304 -1033 C ATOM 971 N VAL A 179 22.562 4.370 -5.969 1.00 50.40 N ANISOU 971 N VAL A 179 5955 5497 7699 -350 -332 -574 N ATOM 972 CA VAL A 179 22.897 5.625 -5.296 1.00 57.10 C ANISOU 972 CA VAL A 179 6861 6437 8398 -276 -293 -420 C ATOM 973 C VAL A 179 21.897 5.922 -4.187 1.00 44.09 C ANISOU 973 C VAL A 179 5121 4817 6813 -302 -259 -309 C ATOM 974 O VAL A 179 22.275 6.205 -3.044 1.00 59.39 O ANISOU 974 O VAL A 179 7089 6741 8734 -288 -178 -164 O ATOM 975 CB VAL A 179 22.969 6.779 -6.313 1.00 43.42 C ANISOU 975 CB VAL A 179 5212 4840 6446 -193 -359 -469 C ATOM 976 CG1 VAL A 179 22.982 8.112 -5.591 1.00 42.76 C ANISOU 976 CG1 VAL A 179 5169 4823 6253 -132 -324 -330 C ATOM 977 CG2 VAL A 179 24.205 6.633 -7.185 1.00 43.33 C ANISOU 977 CG2 VAL A 179 5310 4808 6344 -165 -329 -539 C ATOM 978 N TRP A 180 20.603 5.849 -4.505 1.00 44.18 N ANISOU 978 N TRP A 180 5008 4883 6894 -339 -322 -389 N ATOM 979 CA TRP A 180 19.583 6.110 -3.497 1.00 44.41 C ANISOU 979 CA TRP A 180 4923 4951 7000 -365 -263 -302 C ATOM 980 C TRP A 180 19.622 5.082 -2.374 1.00 45.50 C ANISOU 980 C TRP A 180 5029 4952 7305 -463 -130 -192 C ATOM 981 O TRP A 180 19.329 5.415 -1.220 1.00 65.94 O ANISOU 981 O TRP A 180 7604 7568 9882 -462 -25 -56 O ATOM 982 CB TRP A 180 18.203 6.150 -4.148 1.00 45.79 C ANISOU 982 CB TRP A 180 4928 5218 7252 -386 -365 -433 C ATOM 983 CG TRP A 180 17.929 7.438 -4.858 1.00 47.89 C ANISOU 983 CG TRP A 180 5226 5637 7334 -249 -480 -465 C ATOM 984 CD1 TRP A 180 18.010 7.672 -6.199 1.00 48.38 C ANISOU 984 CD1 TRP A 180 5345 5771 7266 -185 -630 -583 C ATOM 985 CD2 TRP A 180 17.537 8.676 -4.257 1.00 48.31 C ANISOU 985 CD2 TRP A 180 5277 5777 7302 -146 -448 -367 C ATOM 986 NE1 TRP A 180 17.686 8.979 -6.471 1.00 54.87 N ANISOU 986 NE1 TRP A 180 6208 6709 7932 -43 -697 -538 N ATOM 987 CE2 TRP A 180 17.392 9.617 -5.295 1.00 54.32 C ANISOU 987 CE2 TRP A 180 6097 6637 7905 -16 -587 -415 C ATOM 988 CE3 TRP A 180 17.291 9.080 -2.941 1.00 49.91 C ANISOU 988 CE3 TRP A 180 5447 5979 7539 -142 -309 -248 C ATOM 989 CZ2 TRP A 180 17.011 10.936 -5.059 1.00 58.45 C ANISOU 989 CZ2 TRP A 180 6642 7229 8339 119 -591 -343 C ATOM 990 CZ3 TRP A 180 16.914 10.389 -2.708 1.00 49.97 C ANISOU 990 CZ3 TRP A 180 5468 6069 7448 -14 -311 -208 C ATOM 991 CH2 TRP A 180 16.778 11.301 -3.761 1.00 62.05 C ANISOU 991 CH2 TRP A 180 7053 7668 8857 117 -451 -254 C ATOM 992 N LEU A 181 19.988 3.836 -2.684 1.00 44.78 N ANISOU 992 N LEU A 181 4944 4707 7362 -541 -123 -246 N ATOM 993 CA LEU A 181 20.147 2.834 -1.635 1.00 45.09 C ANISOU 993 CA LEU A 181 4994 4583 7556 -615 7 -105 C ATOM 994 C LEU A 181 21.285 3.203 -0.693 1.00 45.09 C ANISOU 994 C LEU A 181 5136 4583 7412 -523 63 73 C ATOM 995 O LEU A 181 21.166 3.043 0.528 1.00 44.45 O ANISOU 995 O LEU A 181 5076 4476 7337 -538 171 247 O ATOM 996 CB LEU A 181 20.382 1.456 -2.250 1.00 45.93 C ANISOU 996 CB LEU A 181 5096 4490 7865 -698 -5 -212 C ATOM 997 CG LEU A 181 19.150 0.780 -2.852 1.00 47.46 C ANISOU 997 CG LEU A 181 5123 4638 8270 -839 -38 -382 C ATOM 998 CD1 LEU A 181 19.533 -0.520 -3.535 1.00 48.36 C ANISOU 998 CD1 LEU A 181 5263 4535 8576 -911 -55 -524 C ATOM 999 CD2 LEU A 181 18.106 0.538 -1.779 1.00 48.42 C ANISOU 999 CD2 LEU A 181 5125 4728 8545 -951 101 -252 C ATOM 1000 N ILE A 182 22.396 3.698 -1.243 1.00 45.22 N ANISOU 1000 N ILE A 182 5248 4641 7293 -430 -7 28 N ATOM 1001 CA ILE A 182 23.498 4.174 -0.408 1.00 57.60 C ANISOU 1001 CA ILE A 182 6918 6238 8729 -346 17 161 C ATOM 1002 C ILE A 182 23.020 5.295 0.504 1.00 43.56 C ANISOU 1002 C ILE A 182 5146 4600 6804 -317 55 252 C ATOM 1003 O ILE A 182 23.275 5.289 1.714 1.00 50.73 O ANISOU 1003 O ILE A 182 6104 5515 7655 -297 115 398 O ATOM 1004 CB ILE A 182 24.681 4.633 -1.281 1.00 44.52 C ANISOU 1004 CB ILE A 182 5324 4616 6975 -273 -49 68 C ATOM 1005 CG1 ILE A 182 25.223 3.474 -2.117 1.00 41.95 C ANISOU 1005 CG1 ILE A 182 4997 4150 6793 -285 -63 -37 C ATOM 1006 CG2 ILE A 182 25.783 5.232 -0.416 1.00 40.89 C ANISOU 1006 CG2 ILE A 182 4931 4207 6399 -201 -41 176 C ATOM 1007 CD1 ILE A 182 26.355 3.880 -3.035 1.00 41.49 C ANISOU 1007 CD1 ILE A 182 4986 4136 6641 -220 -91 -140 C ATOM 1008 N SER A 183 22.312 6.273 -0.069 1.00 45.84 N ANISOU 1008 N SER A 183 5392 5003 7020 -299 15 161 N ATOM 1009 CA SER A 183 21.852 7.422 0.704 1.00 53.13 C ANISOU 1009 CA SER A 183 6324 6045 7818 -253 55 216 C ATOM 1010 C SER A 183 20.934 6.990 1.838 1.00 48.53 C ANISOU 1010 C SER A 183 5678 5463 7300 -306 175 320 C ATOM 1011 O SER A 183 21.056 7.474 2.969 1.00 44.72 O ANISOU 1011 O SER A 183 5255 5039 6697 -272 247 419 O ATOM 1012 CB SER A 183 21.144 8.416 -0.215 1.00 51.21 C ANISOU 1012 CB SER A 183 6038 5894 7524 -206 -15 105 C ATOM 1013 OG SER A 183 19.993 7.825 -0.788 1.00 84.71 O ANISOU 1013 OG SER A 183 10139 10137 11908 -261 -43 25 O ATOM 1014 N ILE A 184 20.003 6.076 1.552 1.00 47.32 N ANISOU 1014 N ILE A 184 5402 5246 7333 -401 207 288 N ATOM 1015 CA ILE A 184 19.144 5.534 2.602 1.00 50.59 C ANISOU 1015 CA ILE A 184 5748 5640 7835 -479 360 401 C ATOM 1016 C ILE A 184 19.980 4.832 3.665 1.00 47.13 C ANISOU 1016 C ILE A 184 5446 5111 7352 -480 441 586 C ATOM 1017 O ILE A 184 19.753 5.006 4.869 1.00 53.98 O ANISOU 1017 O ILE A 184 6358 6034 8118 -472 564 723 O ATOM 1018 CB ILE A 184 18.091 4.582 2.003 1.00 49.03 C ANISOU 1018 CB ILE A 184 5378 5361 7892 -609 378 315 C ATOM 1019 CG1 ILE A 184 17.139 5.334 1.072 1.00 46.39 C ANISOU 1019 CG1 ILE A 184 4889 5157 7582 -585 276 139 C ATOM 1020 CG2 ILE A 184 17.307 3.896 3.110 1.00 47.83 C ANISOU 1020 CG2 ILE A 184 5162 5156 7856 -718 579 455 C ATOM 1021 CD1 ILE A 184 16.097 4.441 0.436 1.00 47.71 C ANISOU 1021 CD1 ILE A 184 4854 5269 8005 -720 258 13 C ATOM 1022 N GLY A 185 20.959 4.028 3.238 1.00 45.11 N ANISOU 1022 N GLY A 185 5260 4721 7160 -475 372 592 N ATOM 1023 CA GLY A 185 21.766 3.282 4.193 1.00 62.18 C ANISOU 1023 CA GLY A 185 7544 6785 9295 -449 421 779 C ATOM 1024 C GLY A 185 22.533 4.180 5.143 1.00 68.53 C ANISOU 1024 C GLY A 185 8465 7730 9842 -339 398 867 C ATOM 1025 O GLY A 185 22.734 3.839 6.312 1.00 90.51 O ANISOU 1025 O GLY A 185 11344 10512 12534 -314 468 1050 O ATOM 1026 N ILE A 186 22.959 5.345 4.660 1.00 58.59 N ANISOU 1026 N ILE A 186 7209 6594 8460 -275 300 738 N ATOM 1027 CA ILE A 186 23.656 6.287 5.526 1.00 48.95 C ANISOU 1027 CA ILE A 186 6083 5502 7013 -191 270 777 C ATOM 1028 C ILE A 186 22.667 7.076 6.379 1.00 48.78 C ANISOU 1028 C ILE A 186 6060 5607 6867 -194 380 799 C ATOM 1029 O ILE A 186 23.003 7.503 7.488 1.00 49.81 O ANISOU 1029 O ILE A 186 6288 5834 6804 -142 402 870 O ATOM 1030 CB ILE A 186 24.549 7.215 4.683 1.00 47.34 C ANISOU 1030 CB ILE A 186 5885 5345 6756 -142 148 631 C ATOM 1031 CG1 ILE A 186 25.529 6.397 3.839 1.00 46.26 C ANISOU 1031 CG1 ILE A 186 5737 5094 6744 -133 71 597 C ATOM 1032 CG2 ILE A 186 25.317 8.183 5.568 1.00 48.27 C ANISOU 1032 CG2 ILE A 186 6086 5580 6674 -79 107 639 C ATOM 1033 CD1 ILE A 186 26.530 7.242 3.080 1.00 54.66 C ANISOU 1033 CD1 ILE A 186 6806 6205 7755 -97 -13 473 C ATOM 1034 N ALA A 187 21.436 7.259 5.903 1.00 50.30 N ANISOU 1034 N ALA A 187 6134 5813 7164 -246 448 725 N ATOM 1035 CA ALA A 187 20.482 8.134 6.571 1.00 46.27 C ANISOU 1035 CA ALA A 187 5593 5428 6559 -227 557 708 C ATOM 1036 C ALA A 187 19.651 7.441 7.641 1.00 49.34 C ANISOU 1036 C ALA A 187 5967 5825 6956 -288 750 854 C ATOM 1037 O ALA A 187 19.072 8.126 8.491 1.00 50.72 O ANISOU 1037 O ALA A 187 6151 6121 6998 -256 869 861 O ATOM 1038 CB ALA A 187 19.539 8.763 5.544 1.00 45.74 C ANISOU 1038 CB ALA A 187 5382 5390 6606 -226 527 555 C ATOM 1039 N ILE A 188 19.581 6.115 7.629 1.00 53.06 N ANISOU 1039 N ILE A 188 6423 6159 7580 -375 803 969 N ATOM 1040 CA ILE A 188 18.632 5.377 8.462 1.00 62.31 C ANISOU 1040 CA ILE A 188 7557 7303 8813 -467 1021 1113 C ATOM 1041 C ILE A 188 18.959 5.372 9.957 1.00 64.09 C ANISOU 1041 C ILE A 188 7962 7607 8781 -416 1139 1306 C ATOM 1042 O ILE A 188 18.036 5.154 10.754 1.00 58.35 O ANISOU 1042 O ILE A 188 7212 6920 8039 -477 1362 1409 O ATOM 1043 CB ILE A 188 18.475 3.935 7.946 1.00 63.10 C ANISOU 1043 CB ILE A 188 7600 7189 9185 -589 1048 1175 C ATOM 1044 CG1 ILE A 188 17.070 3.418 8.248 1.00 67.70 C ANISOU 1044 CG1 ILE A 188 8029 7743 9950 -734 1272 1217 C ATOM 1045 CG2 ILE A 188 19.497 3.002 8.577 1.00 54.37 C ANISOU 1045 CG2 ILE A 188 6682 5955 8021 -557 1041 1382 C ATOM 1046 CD1 ILE A 188 15.963 4.216 7.593 1.00 60.50 C ANISOU 1046 CD1 ILE A 188 6887 6956 9143 -756 1267 1010 C ATOM 1047 N PRO A 189 20.203 5.575 10.418 1.00 65.13 N ANISOU 1047 N PRO A 189 8268 7777 8700 -309 1008 1362 N ATOM 1048 CA PRO A 189 20.408 5.573 11.877 1.00 63.00 C ANISOU 1048 CA PRO A 189 8175 7614 8149 -253 1107 1538 C ATOM 1049 C PRO A 189 19.664 6.680 12.605 1.00 71.32 C ANISOU 1049 C PRO A 189 9226 8865 9005 -223 1241 1458 C ATOM 1050 O PRO A 189 19.327 6.505 13.783 1.00 58.35 O ANISOU 1050 O PRO A 189 7696 7310 7166 -217 1417 1608 O ATOM 1051 CB PRO A 189 21.929 5.729 12.020 1.00 54.24 C ANISOU 1051 CB PRO A 189 7201 6530 6878 -135 879 1546 C ATOM 1052 CG PRO A 189 22.477 5.188 10.767 1.00 52.88 C ANISOU 1052 CG PRO A 189 6938 6189 6962 -158 734 1474 C ATOM 1053 CD PRO A 189 21.501 5.620 9.718 1.00 60.73 C ANISOU 1053 CD PRO A 189 7755 7167 8154 -240 776 1291 C ATOM 1054 N VAL A 190 19.399 7.809 11.954 1.00 75.06 N ANISOU 1054 N VAL A 190 9592 9407 9518 -193 1174 1231 N ATOM 1055 CA VAL A 190 18.736 8.939 12.604 1.00 59.00 C ANISOU 1055 CA VAL A 190 7558 7541 7319 -140 1294 1125 C ATOM 1056 C VAL A 190 17.298 8.575 12.971 1.00 77.73 C ANISOU 1056 C VAL A 190 9801 9939 9794 -221 1572 1184 C ATOM 1057 O VAL A 190 16.908 8.761 14.132 1.00 86.26 O ANISOU 1057 O VAL A 190 10969 11147 10659 -198 1767 1253 O ATOM 1058 CB VAL A 190 18.795 10.204 11.729 1.00 54.98 C ANISOU 1058 CB VAL A 190 6968 7052 6867 -78 1155 885 C ATOM 1059 CG1 VAL A 190 18.100 11.357 12.422 1.00 62.66 C ANISOU 1059 CG1 VAL A 190 7946 8168 7695 -6 1288 766 C ATOM 1060 CG2 VAL A 190 20.231 10.559 11.407 1.00 54.24 C ANISOU 1060 CG2 VAL A 190 6989 6932 6689 -25 918 830 C ATOM 1061 N PRO A 191 16.465 8.068 12.052 1.00 65.99 N ANISOU 1061 N PRO A 191 8098 8349 8625 -319 1609 1147 N ATOM 1062 CA PRO A 191 15.117 7.659 12.476 1.00 59.12 C ANISOU 1062 CA PRO A 191 7076 7508 7880 -416 1891 1203 C ATOM 1063 C PRO A 191 15.106 6.389 13.306 1.00 60.39 C ANISOU 1063 C PRO A 191 7344 7588 8014 -520 2080 1470 C ATOM 1064 O PRO A 191 14.208 6.223 14.140 1.00 61.33 O ANISOU 1064 O PRO A 191 7426 7778 8098 -580 2369 1562 O ATOM 1065 CB PRO A 191 14.371 7.471 11.149 1.00 55.98 C ANISOU 1065 CB PRO A 191 6406 7023 7842 -493 1814 1060 C ATOM 1066 CG PRO A 191 15.431 7.114 10.183 1.00 58.75 C ANISOU 1066 CG PRO A 191 6828 7238 8254 -484 1547 1036 C ATOM 1067 CD PRO A 191 16.630 7.921 10.592 1.00 63.22 C ANISOU 1067 CD PRO A 191 7617 7876 8527 -347 1407 1026 C ATOM 1068 N ILE A 192 16.062 5.480 13.097 1.00 71.03 N ANISOU 1068 N ILE A 192 8822 8779 9387 -539 1942 1606 N ATOM 1069 CA ILE A 192 16.094 4.250 13.882 1.00 70.05 C ANISOU 1069 CA ILE A 192 8831 8542 9245 -619 2116 1891 C ATOM 1070 C ILE A 192 16.370 4.557 15.349 1.00 61.64 C ANISOU 1070 C ILE A 192 8006 7645 7768 -524 2245 2052 C ATOM 1071 O ILE A 192 15.700 4.030 16.245 1.00 65.83 O ANISOU 1071 O ILE A 192 8591 8190 8231 -597 2537 2247 O ATOM 1072 CB ILE A 192 17.128 3.265 13.303 1.00 75.01 C ANISOU 1072 CB ILE A 192 9550 8951 10000 -621 1918 1985 C ATOM 1073 CG1 ILE A 192 16.603 2.624 12.016 1.00 76.65 C ANISOU 1073 CG1 ILE A 192 9532 8969 10625 -760 1877 1861 C ATOM 1074 CG2 ILE A 192 17.474 2.191 14.320 1.00 60.85 C ANISOU 1074 CG2 ILE A 192 7979 7054 8089 -630 2052 2315 C ATOM 1075 CD1 ILE A 192 17.529 1.566 11.443 1.00106.44 C ANISOU 1075 CD1 ILE A 192 13389 12503 14552 -766 1722 1936 C ATOM 1076 N LYS A 193 17.352 5.417 15.622 1.00 70.25 N ANISOU 1076 N LYS A 193 9247 8871 8572 -368 2038 1967 N ATOM 1077 CA LYS A 193 17.713 5.708 17.006 1.00 62.71 C ANISOU 1077 CA LYS A 193 8538 8097 7192 -267 2114 2093 C ATOM 1078 C LYS A 193 16.698 6.641 17.659 1.00 64.10 C ANISOU 1078 C LYS A 193 8664 8476 7216 -258 2356 1974 C ATOM 1079 O LYS A 193 16.253 6.396 18.786 1.00 66.47 O ANISOU 1079 O LYS A 193 9094 8880 7280 -266 2615 2142 O ATOM 1080 CB LYS A 193 19.119 6.306 17.065 1.00 61.66 C ANISOU 1080 CB LYS A 193 8555 8043 6832 -119 1793 2006 C ATOM 1081 CG LYS A 193 19.737 6.313 18.450 1.00 66.31 C ANISOU 1081 CG LYS A 193 9420 8799 6976 -8 1793 2164 C ATOM 1082 CD LYS A 193 21.222 6.623 18.380 1.00 82.19 C ANISOU 1082 CD LYS A 193 11531 10850 8846 117 1439 2093 C ATOM 1083 CE LYS A 193 21.887 6.446 19.733 1.00 94.07 C ANISOU 1083 CE LYS A 193 13309 12523 9911 238 1392 2272 C ATOM 1084 NZ LYS A 193 23.363 6.616 19.647 1.00101.93 N ANISOU 1084 NZ LYS A 193 14359 13556 10815 355 1028 2208 N ATOM 1085 N GLY A 194 16.318 7.710 16.968 1.00 68.78 N ANISOU 1085 N GLY A 194 9076 9123 7934 -230 2287 1690 N ATOM 1086 CA GLY A 194 15.317 8.626 17.469 1.00 73.48 C ANISOU 1086 CA GLY A 194 9590 9888 8443 -200 2511 1547 C ATOM 1087 C GLY A 194 15.900 9.702 18.367 1.00 69.56 C ANISOU 1087 C GLY A 194 9301 9586 7543 -54 2454 1429 C ATOM 1088 O GLY A 194 17.074 9.688 18.746 1.00 68.60 O ANISOU 1088 O GLY A 194 9393 9495 7178 17 2246 1479 O ATOM 1089 N ILE A 195 15.046 10.661 18.714 1.00 70.82 N ANISOU 1089 N ILE A 195 9381 9881 7647 -4 2637 1248 N ATOM 1090 CA ILE A 195 15.431 11.792 19.551 1.00 73.28 C ANISOU 1090 CA ILE A 195 9872 10370 7602 130 2613 1076 C ATOM 1091 C ILE A 195 14.940 11.537 20.969 1.00 80.13 C ANISOU 1091 C ILE A 195 10903 11422 8121 139 2933 1211 C ATOM 1092 O ILE A 195 13.794 11.114 21.173 1.00103.01 O ANISOU 1092 O ILE A 195 13663 14338 11137 61 3263 1299 O ATOM 1093 CB ILE A 195 14.877 13.118 19.003 1.00 72.70 C ANISOU 1093 CB ILE A 195 9631 10307 7686 208 2601 764 C ATOM 1094 CG1 ILE A 195 15.795 13.694 17.919 1.00 71.49 C ANISOU 1094 CG1 ILE A 195 9455 10018 7689 244 2244 618 C ATOM 1095 CG2 ILE A 195 14.772 14.135 20.112 1.00 86.42 C ANISOU 1095 CG2 ILE A 195 11525 12234 9078 323 2735 594 C ATOM 1096 CD1 ILE A 195 15.793 12.942 16.610 1.00 69.76 C ANISOU 1096 CD1 ILE A 195 9053 9615 7837 152 2105 703 C ATOM 1097 N GLU A 196 15.803 11.810 21.947 1.00 79.51 N ANISOU 1097 N GLU A 196 11112 11492 7607 231 2839 1217 N ATOM 1098 CA GLU A 196 15.500 11.524 23.343 1.00 89.18 C ANISOU 1098 CA GLU A 196 12554 12914 8415 255 3116 1368 C ATOM 1099 C GLU A 196 14.287 12.311 23.826 1.00 79.61 C ANISOU 1099 C GLU A 196 11244 11845 7160 285 3467 1183 C ATOM 1100 O GLU A 196 14.146 13.506 23.545 1.00 74.93 O ANISOU 1100 O GLU A 196 10561 11275 6634 369 3403 865 O ATOM 1101 CB GLU A 196 16.717 11.842 24.212 1.00 92.17 C ANISOU 1101 CB GLU A 196 13249 13451 8322 372 2879 1343 C ATOM 1102 N THR A 197 13.418 11.632 24.569 1.00 89.90 N ANISOU 1102 N THR A 197 12566 13232 8357 220 3858 1390 N ATOM 1103 CA THR A 197 12.216 12.220 25.134 1.00106.52 C ANISOU 1103 CA THR A 197 14569 15493 10413 243 4255 1247 C ATOM 1104 C THR A 197 12.236 12.077 26.650 1.00119.08 C ANISOU 1104 C THR A 197 16434 17307 11503 259 4401 1334 C ATOM 1105 O THR A 197 12.935 11.227 27.210 1.00114.41 O ANISOU 1105 O THR A 197 16082 16727 10662 226 4287 1598 O ATOM 1106 CB THR A 197 10.951 11.561 24.566 1.00 96.29 C ANISOU 1106 CB THR A 197 12929 14084 9572 93 4545 1348 C ATOM 1107 N ASP A 198 11.454 12.925 27.312 1.00117.17 N ANISOU 1107 N ASP A 198 16141 17241 11139 311 4619 1093 N ATOM 1108 CA ASP A 198 11.338 12.924 28.762 1.00108.86 C ANISOU 1108 CA ASP A 198 15312 16424 9625 315 4763 1117 C ATOM 1109 C ASP A 198 9.894 12.635 29.140 1.00110.67 C ANISOU 1109 C ASP A 198 15311 16722 10015 207 5169 1153 C ATOM 1110 O ASP A 198 8.969 13.235 28.580 1.00115.64 O ANISOU 1110 O ASP A 198 15629 17325 10984 227 5321 938 O ATOM 1111 CB ASP A 198 11.790 14.264 29.356 1.00112.51 C ANISOU 1111 CB ASP A 198 15945 17064 9739 478 4649 757 C ATOM 1112 CG ASP A 198 12.090 14.175 30.845 1.00129.89 C ANISOU 1112 CG ASP A 198 18456 19514 11383 487 4682 802 C ATOM 1113 OD1 ASP A 198 11.755 13.145 31.466 1.00144.79 O ANISOU 1113 OD1 ASP A 198 20407 21448 13157 376 4856 1110 O ATOM 1114 OD2 ASP A 198 12.671 15.137 31.394 1.00136.69 O ANISOU 1114 OD2 ASP A 198 19498 20515 11921 599 4527 523 O ATOM 1115 N VAL A 199 9.706 11.709 30.083 1.00110.26 N ANISOU 1115 N VAL A 199 15407 16759 9729 100 5335 1427 N ATOM 1116 CA VAL A 199 8.373 11.467 30.624 1.00120.65 C ANISOU 1116 CA VAL A 199 16534 18180 11125 -3 5738 1456 C ATOM 1117 C VAL A 199 7.827 12.733 31.269 1.00131.21 C ANISOU 1117 C VAL A 199 17833 19756 12265 125 5901 1096 C ATOM 1118 O VAL A 199 6.612 12.967 31.269 1.00136.54 O ANISOU 1118 O VAL A 199 18215 20495 13170 98 6197 979 O ATOM 1119 CB VAL A 199 8.403 10.289 31.618 1.00126.20 C ANISOU 1119 CB VAL A 199 17466 18939 11545 -130 5878 1825 C ATOM 1120 N ASP A 200 8.708 13.578 31.812 1.00139.54 N ANISOU 1120 N ASP A 200 19165 20943 12912 270 5699 896 N ATOM 1121 CA ASP A 200 8.259 14.818 32.435 1.00143.14 C ANISOU 1121 CA ASP A 200 19602 21605 13180 397 5834 520 C ATOM 1122 C ASP A 200 7.829 15.839 31.388 1.00140.31 C ANISOU 1122 C ASP A 200 18941 21118 13253 508 5794 196 C ATOM 1123 O ASP A 200 6.767 16.460 31.512 1.00151.67 O ANISOU 1123 O ASP A 200 20139 22646 14841 564 6045 -20 O ATOM 1124 CB ASP A 200 9.363 15.392 33.322 1.00130.55 C ANISOU 1124 CB ASP A 200 18394 20172 11037 496 5603 379 C ATOM 1125 N ASN A 201 8.642 16.028 30.346 1.00124.99 N ANISOU 1125 N ASN A 201 17005 18968 11517 556 5476 162 N ATOM 1126 CA ASN A 201 8.422 17.064 29.338 1.00116.19 C ANISOU 1126 CA ASN A 201 15663 17713 10773 681 5386 -140 C ATOM 1127 C ASN A 201 8.303 16.419 27.963 1.00129.63 C ANISOU 1127 C ASN A 201 17113 19166 12976 602 5298 37 C ATOM 1128 O ASN A 201 9.286 16.364 27.208 1.00146.27 O ANISOU 1128 O ASN A 201 19323 21113 15138 621 5006 85 O ATOM 1129 CB ASN A 201 9.550 18.093 29.352 1.00101.32 C ANISOU 1129 CB ASN A 201 14030 15810 8658 821 5077 -408 C ATOM 1130 N PRO A 202 7.116 15.927 27.599 1.00125.17 N ANISOU 1130 N PRO A 202 16203 18570 12786 509 5536 123 N ATOM 1131 CA PRO A 202 6.942 15.389 26.242 1.00120.45 C ANISOU 1131 CA PRO A 202 15331 17741 12692 429 5433 239 C ATOM 1132 C PRO A 202 7.053 16.451 25.165 1.00114.63 C ANISOU 1132 C PRO A 202 14442 16863 12248 586 5242 -35 C ATOM 1133 O PRO A 202 7.376 16.125 24.016 1.00133.65 O ANISOU 1133 O PRO A 202 16736 19080 14966 547 5059 47 O ATOM 1134 CB PRO A 202 5.534 14.771 26.280 1.00120.46 C ANISOU 1134 CB PRO A 202 14984 17788 12998 299 5736 326 C ATOM 1135 CG PRO A 202 5.190 14.644 27.735 1.00113.68 C ANISOU 1135 CG PRO A 202 14295 17171 11729 272 6005 374 C ATOM 1136 CD PRO A 202 5.906 15.765 28.420 1.00114.63 C ANISOU 1136 CD PRO A 202 14709 17420 11426 457 5899 125 C ATOM 1137 N ASN A 203 6.825 17.720 25.506 1.00111.27 N ANISOU 1137 N ASN A 203 14026 16518 11733 766 5275 -361 N ATOM 1138 CA ASN A 203 6.729 18.746 24.475 1.00111.55 C ANISOU 1138 CA ASN A 203 13884 16394 12105 924 5121 -616 C ATOM 1139 C ASN A 203 8.103 19.202 24.000 1.00124.21 C ANISOU 1139 C ASN A 203 15762 17850 13581 989 4782 -676 C ATOM 1140 O ASN A 203 8.294 19.468 22.807 1.00146.86 O ANISOU 1140 O ASN A 203 18476 20519 16804 1005 4480 -720 O ATOM 1141 CB ASN A 203 5.923 19.937 24.994 1.00119.83 C ANISOU 1141 CB ASN A 203 14830 17548 13152 1103 5271 -941 C ATOM 1142 N ASN A 204 9.071 19.300 24.913 1.00121.88 N ANISOU 1142 N ASN A 204 15847 17660 12802 998 4708 -685 N ATOM 1143 CA ASN A 204 10.345 19.964 24.633 1.00135.53 C ANISOU 1143 CA ASN A 204 17799 19275 14420 1044 4292 -824 C ATOM 1144 C ASN A 204 11.347 18.961 24.061 1.00143.34 C ANISOU 1144 C ASN A 204 18861 20162 15440 897 3972 -542 C ATOM 1145 O ASN A 204 12.282 18.505 24.721 1.00156.30 O ANISOU 1145 O ASN A 204 20780 21895 16711 852 3854 -419 O ATOM 1146 CB ASN A 204 10.881 20.628 25.893 1.00115.15 C ANISOU 1146 CB ASN A 204 15561 16873 11319 1134 4345 -1024 C ATOM 1147 N ILE A 205 11.140 18.641 22.786 1.00109.30 N ANISOU 1147 N ILE A 205 14289 15659 11581 838 3820 -453 N ATOM 1148 CA ILE A 205 11.999 17.685 22.100 1.00 95.16 C ANISOU 1148 CA ILE A 205 12528 13746 9883 707 3534 -209 C ATOM 1149 C ILE A 205 13.340 18.318 21.757 1.00 94.47 C ANISOU 1149 C ILE A 205 12625 13558 9711 742 3143 -336 C ATOM 1150 O ILE A 205 14.401 17.757 22.053 1.00101.37 O ANISOU 1150 O ILE A 205 13700 14460 10356 683 2954 -198 O ATOM 1151 CB ILE A 205 11.287 17.158 20.848 1.00 94.16 C ANISOU 1151 CB ILE A 205 12061 13465 10251 633 3510 -109 C ATOM 1152 CG1 ILE A 205 10.122 16.278 21.258 1.00100.00 C ANISOU 1152 CG1 ILE A 205 12620 14303 11073 542 3888 57 C ATOM 1153 CG2 ILE A 205 12.229 16.393 19.958 1.00 85.75 C ANISOU 1153 CG2 ILE A 205 11022 12242 9319 525 3183 66 C ATOM 1154 CD1 ILE A 205 9.305 15.928 20.102 1.00106.10 C ANISOU 1154 CD1 ILE A 205 13029 14953 12333 481 3868 81 C ATOM 1155 N THR A 206 13.307 19.488 21.114 1.00103.05 N ANISOU 1155 N THR A 206 13635 14517 11002 841 3020 -593 N ATOM 1156 CA THR A 206 14.499 20.236 20.722 1.00100.65 C ANISOU 1156 CA THR A 206 13478 14091 10675 862 2686 -742 C ATOM 1157 C THR A 206 15.398 19.432 19.789 1.00 93.94 C ANISOU 1157 C THR A 206 12602 13112 9978 745 2393 -539 C ATOM 1158 O THR A 206 16.414 18.874 20.220 1.00 88.96 O ANISOU 1158 O THR A 206 12147 12543 9112 683 2241 -429 O ATOM 1159 CB THR A 206 15.289 20.686 21.955 1.00 83.12 C ANISOU 1159 CB THR A 206 11558 12022 8001 895 2657 -887 C ATOM 1160 N CYS A 207 15.053 19.413 18.502 1.00109.92 N ANISOU 1160 N CYS A 207 14410 14965 12390 733 2303 -506 N ATOM 1161 CA CYS A 207 15.776 18.617 17.513 1.00103.80 C ANISOU 1161 CA CYS A 207 13587 14066 11785 628 2060 -329 C ATOM 1162 C CYS A 207 17.228 19.039 17.384 1.00 85.13 C ANISOU 1162 C CYS A 207 11401 11635 9311 609 1772 -406 C ATOM 1163 O CYS A 207 17.529 20.192 17.057 1.00116.24 O ANISOU 1163 O CYS A 207 15377 15472 13317 668 1672 -615 O ATOM 1164 CB CYS A 207 15.079 18.723 16.163 1.00105.69 C ANISOU 1164 CB CYS A 207 13579 14156 12422 644 2014 -332 C ATOM 1165 SG CYS A 207 13.433 18.127 16.361 1.00140.29 S ANISOU 1165 SG CYS A 207 17707 18639 16959 642 2336 -254 S ATOM 1166 N VAL A 208 18.127 18.089 17.626 1.00 74.19 N ANISOU 1166 N VAL A 208 10113 10296 7781 526 1645 -232 N ATOM 1167 CA VAL A 208 19.554 18.302 17.419 1.00 70.27 C ANISOU 1167 CA VAL A 208 9730 9746 7225 493 1359 -284 C ATOM 1168 C VAL A 208 20.275 16.961 17.507 1.00 69.28 C ANISOU 1168 C VAL A 208 9641 9656 7026 421 1249 -33 C ATOM 1169 O VAL A 208 19.900 16.091 18.301 1.00 87.53 O ANISOU 1169 O VAL A 208 12008 12086 9163 413 1395 147 O ATOM 1170 CB VAL A 208 20.121 19.320 18.432 1.00 63.12 C ANISOU 1170 CB VAL A 208 9015 8941 6027 546 1317 -521 C ATOM 1171 CG1 VAL A 208 19.988 18.802 19.851 1.00 74.95 C ANISOU 1171 CG1 VAL A 208 10671 10675 7134 571 1450 -446 C ATOM 1172 CG2 VAL A 208 21.567 19.664 18.099 1.00 79.22 C ANISOU 1172 CG2 VAL A 208 11117 10909 8075 494 1019 -614 C ATOM 1173 N LEU A 209 21.298 16.776 16.677 1.00 63.08 N ANISOU 1173 N LEU A 209 8825 8757 6385 373 1008 -10 N ATOM 1174 CA LEU A 209 22.105 15.558 16.712 1.00 59.99 C ANISOU 1174 CA LEU A 209 8464 8377 5952 329 879 206 C ATOM 1175 C LEU A 209 23.122 15.704 17.834 1.00 65.86 C ANISOU 1175 C LEU A 209 9390 9281 6354 367 738 161 C ATOM 1176 O LEU A 209 24.211 16.252 17.653 1.00 66.69 O ANISOU 1176 O LEU A 209 9511 9368 6459 357 516 16 O ATOM 1177 CB LEU A 209 22.777 15.304 15.367 1.00 58.18 C ANISOU 1177 CB LEU A 209 8114 7975 6016 275 697 227 C ATOM 1178 CG LEU A 209 21.855 14.890 14.217 1.00 68.01 C ANISOU 1178 CG LEU A 209 9186 9083 7573 237 792 299 C ATOM 1179 CD1 LEU A 209 22.662 14.360 13.039 1.00 74.46 C ANISOU 1179 CD1 LEU A 209 9925 9763 8605 187 614 350 C ATOM 1180 CD2 LEU A 209 20.832 13.861 14.678 1.00 59.26 C ANISOU 1180 CD2 LEU A 209 8040 8019 6457 213 1001 490 C ATOM 1181 N THR A 210 22.753 15.203 19.011 1.00 65.30 N ANISOU 1181 N THR A 210 9452 9377 5982 407 871 285 N ATOM 1182 CA THR A 210 23.596 15.336 20.189 1.00 67.94 C ANISOU 1182 CA THR A 210 9979 9905 5928 464 737 243 C ATOM 1183 C THR A 210 24.912 14.594 20.003 1.00 67.18 C ANISOU 1183 C THR A 210 9886 9794 5844 464 450 367 C ATOM 1184 O THR A 210 24.951 13.488 19.456 1.00 78.95 O ANISOU 1184 O THR A 210 11307 11175 7517 441 446 607 O ATOM 1185 CB THR A 210 22.861 14.798 21.420 1.00 74.55 C ANISOU 1185 CB THR A 210 10977 10925 6424 514 966 407 C ATOM 1186 OG1 THR A 210 21.575 15.421 21.518 1.00 92.45 O ANISOU 1186 OG1 THR A 210 13197 13201 8730 517 1263 292 O ATOM 1187 CG2 THR A 210 23.654 15.083 22.687 1.00 92.60 C ANISOU 1187 CG2 THR A 210 13486 13448 8249 593 819 326 C ATOM 1188 N LYS A 211 26.001 15.223 20.451 1.00 70.24 N ANISOU 1188 N LYS A 211 10340 10290 6059 490 205 180 N ATOM 1189 CA LYS A 211 27.303 14.564 20.444 1.00 68.19 C ANISOU 1189 CA LYS A 211 10068 10061 5781 515 -83 277 C ATOM 1190 C LYS A 211 27.273 13.289 21.278 1.00 73.14 C ANISOU 1190 C LYS A 211 10835 10798 6158 600 -62 606 C ATOM 1191 O LYS A 211 27.799 12.250 20.865 1.00 71.32 O ANISOU 1191 O LYS A 211 10548 10475 6074 620 -169 825 O ATOM 1192 CB LYS A 211 28.373 15.529 20.959 1.00 77.74 C ANISOU 1192 CB LYS A 211 11314 11406 6819 524 -340 -13 C ATOM 1193 CG LYS A 211 29.762 14.929 21.114 1.00 70.52 C ANISOU 1193 CG LYS A 211 10364 10572 5857 570 -663 55 C ATOM 1194 CD LYS A 211 30.720 15.945 21.722 1.00 66.66 C ANISOU 1194 CD LYS A 211 9894 10243 5191 562 -913 -270 C ATOM 1195 CE LYS A 211 32.096 15.346 21.962 1.00 68.37 C ANISOU 1195 CE LYS A 211 10045 10578 5354 625 -1257 -215 C ATOM 1196 NZ LYS A 211 33.033 16.331 22.572 1.00 81.67 N ANISOU 1196 NZ LYS A 211 11718 12432 6879 600 -1521 -560 N ATOM 1197 N GLU A 212 26.643 13.346 22.456 1.00 76.58 N ANISOU 1197 N GLU A 212 11465 11420 6211 658 95 650 N ATOM 1198 CA GLU A 212 26.591 12.172 23.323 1.00 80.20 C ANISOU 1198 CA GLU A 212 12098 11984 6392 743 139 992 C ATOM 1199 C GLU A 212 25.785 11.048 22.684 1.00 70.76 C ANISOU 1199 C GLU A 212 10828 10577 5481 687 371 1297 C ATOM 1200 O GLU A 212 26.157 9.873 22.784 1.00 77.39 O ANISOU 1200 O GLU A 212 11723 11360 6320 736 311 1597 O ATOM 1201 CB GLU A 212 25.999 12.542 24.685 1.00101.69 C ANISOU 1201 CB GLU A 212 15057 14957 8624 807 306 966 C ATOM 1202 CG GLU A 212 26.746 13.638 25.439 1.00116.60 C ANISOU 1202 CG GLU A 212 17044 17071 10187 860 76 635 C ATOM 1203 CD GLU A 212 26.256 15.036 25.099 1.00109.84 C ANISOU 1203 CD GLU A 212 16099 16164 9470 784 185 248 C ATOM 1204 OE1 GLU A 212 26.640 15.566 24.035 1.00 82.13 O ANISOU 1204 OE1 GLU A 212 12392 12467 6348 705 67 73 O ATOM 1205 OE2 GLU A 212 25.479 15.605 25.896 1.00111.50 O ANISOU 1205 OE2 GLU A 212 16449 16515 9402 813 403 125 O ATOM 1206 N ARG A 213 24.688 11.388 22.010 1.00 67.08 N ANISOU 1206 N ARG A 213 10228 9982 5278 589 626 1215 N ATOM 1207 CA ARG A 213 23.786 10.387 21.457 1.00 66.39 C ANISOU 1207 CA ARG A 213 10053 9710 5462 515 864 1461 C ATOM 1208 C ARG A 213 24.218 9.915 20.071 1.00 72.51 C ANISOU 1208 C ARG A 213 10626 10242 6681 454 719 1474 C ATOM 1209 O ARG A 213 24.254 8.708 19.810 1.00 73.37 O ANISOU 1209 O ARG A 213 10728 10208 6940 439 741 1731 O ATOM 1210 CB ARG A 213 22.360 10.946 21.410 1.00 66.50 C ANISOU 1210 CB ARG A 213 9989 9727 5550 448 1195 1355 C ATOM 1211 CG ARG A 213 21.288 9.927 21.058 1.00 68.09 C ANISOU 1211 CG ARG A 213 10095 9780 5996 354 1475 1595 C ATOM 1212 CD ARG A 213 19.901 10.551 21.124 1.00 67.11 C ANISOU 1212 CD ARG A 213 9866 9701 5931 306 1794 1466 C ATOM 1213 NE ARG A 213 18.845 9.583 20.843 1.00 67.24 N ANISOU 1213 NE ARG A 213 9761 9591 6195 195 2069 1676 N ATOM 1214 CZ ARG A 213 18.173 8.918 21.777 1.00 70.92 C ANISOU 1214 CZ ARG A 213 10342 10130 6475 167 2366 1908 C ATOM 1215 NH1 ARG A 213 18.446 9.116 23.060 1.00 72.10 N ANISOU 1215 NH1 ARG A 213 10751 10497 6145 261 2419 1967 N ATOM 1216 NH2 ARG A 213 17.228 8.056 21.430 1.00 86.42 N ANISOU 1216 NH2 ARG A 213 12161 11951 8725 37 2615 2074 N ATOM 1217 N PHE A 214 24.557 10.845 19.177 1.00 66.79 N ANISOU 1217 N PHE A 214 9754 9459 6166 420 583 1199 N ATOM 1218 CA PHE A 214 24.843 10.531 17.781 1.00 62.56 C ANISOU 1218 CA PHE A 214 9030 8708 6032 358 486 1180 C ATOM 1219 C PHE A 214 26.297 10.793 17.399 1.00 58.81 C ANISOU 1219 C PHE A 214 8513 8230 5600 394 174 1061 C ATOM 1220 O PHE A 214 26.588 11.084 16.238 1.00 56.92 O ANISOU 1220 O PHE A 214 8123 7857 5647 340 99 933 O ATOM 1221 CB PHE A 214 23.919 11.321 16.855 1.00 60.87 C ANISOU 1221 CB PHE A 214 8659 8402 6068 284 620 992 C ATOM 1222 CG PHE A 214 22.493 10.859 16.874 1.00 58.51 C ANISOU 1222 CG PHE A 214 8306 8063 5864 229 911 1109 C ATOM 1223 CD1 PHE A 214 22.088 9.790 16.092 1.00 57.70 C ANISOU 1223 CD1 PHE A 214 8089 7787 6049 154 975 1265 C ATOM 1224 CD2 PHE A 214 21.553 11.499 17.663 1.00 62.33 C ANISOU 1224 CD2 PHE A 214 8837 8681 6166 247 1128 1039 C ATOM 1225 CE1 PHE A 214 20.772 9.363 16.102 1.00 59.85 C ANISOU 1225 CE1 PHE A 214 8276 8021 6441 81 1241 1351 C ATOM 1226 CE2 PHE A 214 20.235 11.077 17.676 1.00 63.23 C ANISOU 1226 CE2 PHE A 214 8862 8768 6397 188 1412 1135 C ATOM 1227 CZ PHE A 214 19.845 10.007 16.896 1.00 63.46 C ANISOU 1227 CZ PHE A 214 8758 8625 6729 97 1463 1292 C ATOM 1228 N GLY A 215 27.218 10.689 18.354 1.00 60.42 N ANISOU 1228 N GLY A 215 8844 8592 5522 485 -7 1100 N ATOM 1229 CA GLY A 215 28.621 10.948 18.081 1.00 60.04 C ANISOU 1229 CA GLY A 215 8722 8567 5524 517 -306 971 C ATOM 1230 C GLY A 215 29.198 10.067 16.993 1.00 67.27 C ANISOU 1230 C GLY A 215 9492 9291 6777 506 -394 1074 C ATOM 1231 O GLY A 215 29.738 10.569 16.003 1.00 75.14 O ANISOU 1231 O GLY A 215 10337 10202 8013 449 -484 894 O ATOM 1232 N ASP A 216 29.077 8.747 17.166 1.00 63.56 N ANISOU 1232 N ASP A 216 9079 8741 6330 560 -350 1363 N ATOM 1233 CA ASP A 216 29.596 7.817 16.168 1.00 68.32 C ANISOU 1233 CA ASP A 216 9556 9144 7257 563 -418 1454 C ATOM 1234 C ASP A 216 28.948 8.033 14.807 1.00 65.53 C ANISOU 1234 C ASP A 216 9052 8613 7234 436 -279 1329 C ATOM 1235 O ASP A 216 29.593 7.824 13.773 1.00 56.73 O ANISOU 1235 O ASP A 216 7802 7378 6375 421 -372 1259 O ATOM 1236 CB ASP A 216 29.387 6.376 16.635 1.00 59.58 C ANISOU 1236 CB ASP A 216 8564 7941 6132 635 -351 1792 C ATOM 1237 N PHE A 217 27.682 8.458 14.782 1.00 60.65 N ANISOU 1237 N PHE A 217 8449 7990 6606 355 -61 1295 N ATOM 1238 CA PHE A 217 27.027 8.730 13.508 1.00 58.82 C ANISOU 1238 CA PHE A 217 8074 7616 6658 255 39 1171 C ATOM 1239 C PHE A 217 27.538 10.024 12.887 1.00 60.98 C ANISOU 1239 C PHE A 217 8269 7925 6974 229 -65 905 C ATOM 1240 O PHE A 217 27.692 10.113 11.664 1.00 61.54 O ANISOU 1240 O PHE A 217 8223 7876 7282 180 -89 814 O ATOM 1241 CB PHE A 217 25.511 8.788 13.688 1.00 68.25 C ANISOU 1241 CB PHE A 217 9277 8807 7849 192 290 1212 C ATOM 1242 CG PHE A 217 24.791 9.344 12.497 1.00 65.73 C ANISOU 1242 CG PHE A 217 8811 8397 7766 116 357 1050 C ATOM 1243 CD1 PHE A 217 24.580 8.562 11.373 1.00 60.39 C ANISOU 1243 CD1 PHE A 217 8021 7552 7372 58 367 1080 C ATOM 1244 CD2 PHE A 217 24.341 10.653 12.492 1.00 67.97 C ANISOU 1244 CD2 PHE A 217 9080 8762 7984 116 398 861 C ATOM 1245 CE1 PHE A 217 23.927 9.072 10.271 1.00 57.68 C ANISOU 1245 CE1 PHE A 217 7554 7151 7210 6 399 934 C ATOM 1246 CE2 PHE A 217 23.689 11.170 11.393 1.00 70.36 C ANISOU 1246 CE2 PHE A 217 9260 8984 8491 74 439 735 C ATOM 1247 CZ PHE A 217 23.482 10.378 10.280 1.00 63.87 C ANISOU 1247 CZ PHE A 217 8328 8022 7919 22 430 776 C ATOM 1248 N MET A 218 27.794 11.045 13.708 1.00 62.24 N ANISOU 1248 N MET A 218 8503 8241 6903 255 -118 774 N ATOM 1249 CA MET A 218 28.361 12.281 13.184 1.00 63.81 C ANISOU 1249 CA MET A 218 8641 8443 7161 217 -211 526 C ATOM 1250 C MET A 218 29.784 12.085 12.682 1.00 80.72 C ANISOU 1250 C MET A 218 10689 10557 9423 221 -412 481 C ATOM 1251 O MET A 218 30.292 12.934 11.941 1.00 81.64 O ANISOU 1251 O MET A 218 10727 10626 9668 162 -459 302 O ATOM 1252 CB MET A 218 28.326 13.377 14.248 1.00 60.05 C ANISOU 1252 CB MET A 218 8272 8125 6421 236 -222 373 C ATOM 1253 CG MET A 218 26.922 13.771 14.678 1.00 60.77 C ANISOU 1253 CG MET A 218 8431 8246 6412 239 2 369 C ATOM 1254 SD MET A 218 26.902 15.169 15.813 1.00 76.81 S ANISOU 1254 SD MET A 218 10592 10438 8154 266 2 127 S ATOM 1255 CE MET A 218 28.170 14.675 16.972 1.00 58.02 C ANISOU 1255 CE MET A 218 8313 8253 5481 329 -234 176 C ATOM 1256 N LEU A 219 30.430 10.985 13.064 1.00 72.89 N ANISOU 1256 N LEU A 219 9703 9587 8404 295 -519 645 N ATOM 1257 CA LEU A 219 31.776 10.666 12.578 1.00 73.11 C ANISOU 1257 CA LEU A 219 9609 9590 8578 320 -701 608 C ATOM 1258 C LEU A 219 31.685 9.781 11.339 1.00 85.73 C ANISOU 1258 C LEU A 219 11111 10998 10464 299 -630 687 C ATOM 1259 O LEU A 219 32.012 10.213 10.230 1.00 68.77 O ANISOU 1259 O LEU A 219 8855 8769 8505 233 -619 549 O ATOM 1260 CB LEU A 219 32.593 9.992 13.682 1.00 61.31 C ANISOU 1260 CB LEU A 219 8165 8229 6901 446 -885 732 C ATOM 1261 CG LEU A 219 34.074 9.765 13.379 1.00 60.87 C ANISOU 1261 CG LEU A 219 7952 8192 6983 497 -1103 667 C ATOM 1262 CD1 LEU A 219 34.812 11.088 13.439 1.00 76.48 C ANISOU 1262 CD1 LEU A 219 9844 10284 8933 421 -1219 388 C ATOM 1263 CD2 LEU A 219 34.687 8.756 14.341 1.00 62.17 C ANISOU 1263 CD2 LEU A 219 8169 8448 7004 664 -1277 866 C ATOM 1264 N PHE A 220 31.234 8.537 11.522 1.00 85.37 N ANISOU 1264 N PHE A 220 11118 10871 10446 352 -570 905 N ATOM 1265 CA PHE A 220 31.225 7.571 10.427 1.00 71.02 C ANISOU 1265 CA PHE A 220 9218 8865 8902 340 -519 962 C ATOM 1266 C PHE A 220 30.204 7.926 9.352 1.00 73.11 C ANISOU 1266 C PHE A 220 9443 9029 9308 228 -361 869 C ATOM 1267 O PHE A 220 30.380 7.546 8.188 1.00 84.27 O ANISOU 1267 O PHE A 220 10768 10318 10932 199 -346 814 O ATOM 1268 CB PHE A 220 30.959 6.171 10.973 1.00 60.57 C ANISOU 1268 CB PHE A 220 7978 7449 7586 414 -486 1219 C ATOM 1269 CG PHE A 220 32.077 5.627 11.812 1.00 74.35 C ANISOU 1269 CG PHE A 220 9751 9264 9233 562 -673 1337 C ATOM 1270 CD1 PHE A 220 32.178 5.958 13.153 1.00 91.60 C ANISOU 1270 CD1 PHE A 220 12060 11639 11106 633 -754 1411 C ATOM 1271 CD2 PHE A 220 33.025 4.781 11.262 1.00 75.45 C ANISOU 1271 CD2 PHE A 220 9793 9290 9586 647 -776 1365 C ATOM 1272 CE1 PHE A 220 33.202 5.458 13.929 1.00 68.77 C ANISOU 1272 CE1 PHE A 220 9194 8833 8104 790 -961 1524 C ATOM 1273 CE2 PHE A 220 34.054 4.276 12.034 1.00 92.40 C ANISOU 1273 CE2 PHE A 220 11947 11505 11655 812 -971 1478 C ATOM 1274 CZ PHE A 220 34.142 4.616 13.370 1.00 75.23 C ANISOU 1274 CZ PHE A 220 9896 9531 9156 886 -1077 1564 C ATOM 1275 N GLY A 221 29.127 8.627 9.715 1.00 56.37 N ANISOU 1275 N GLY A 221 7383 6968 7068 179 -245 844 N ATOM 1276 CA GLY A 221 28.193 9.094 8.703 1.00 53.29 C ANISOU 1276 CA GLY A 221 6939 6507 6803 99 -131 743 C ATOM 1277 C GLY A 221 28.808 10.138 7.792 1.00 53.58 C ANISOU 1277 C GLY A 221 6915 6543 6899 67 -191 554 C ATOM 1278 O GLY A 221 28.509 10.188 6.595 1.00 66.00 O ANISOU 1278 O GLY A 221 8431 8028 8618 25 -150 489 O ATOM 1279 N SER A 222 29.684 10.980 8.343 1.00 69.34 N ANISOU 1279 N SER A 222 8928 8639 8781 81 -287 461 N ATOM 1280 CA SER A 222 30.419 11.937 7.525 1.00 55.82 C ANISOU 1280 CA SER A 222 7158 6905 7148 32 -327 295 C ATOM 1281 C SER A 222 31.514 11.248 6.721 1.00 72.54 C ANISOU 1281 C SER A 222 9171 8962 9429 37 -394 289 C ATOM 1282 O SER A 222 31.805 11.656 5.591 1.00 86.59 O ANISOU 1282 O SER A 222 10899 10676 11325 -14 -357 195 O ATOM 1283 CB SER A 222 31.018 13.036 8.401 1.00 55.53 C ANISOU 1283 CB SER A 222 7155 6977 6966 21 -405 172 C ATOM 1284 OG SER A 222 30.012 13.729 9.120 1.00 69.30 O ANISOU 1284 OG SER A 222 9000 8771 8558 27 -324 149 O ATOM 1285 N LEU A 223 32.129 10.205 7.286 1.00 61.05 N ANISOU 1285 N LEU A 223 7690 7527 7980 111 -483 394 N ATOM 1286 CA LEU A 223 33.154 9.463 6.558 1.00 54.65 C ANISOU 1286 CA LEU A 223 6766 6653 7347 142 -537 383 C ATOM 1287 C LEU A 223 32.558 8.737 5.360 1.00 81.81 C ANISOU 1287 C LEU A 223 10193 9947 10946 119 -426 403 C ATOM 1288 O LEU A 223 33.110 8.780 4.255 1.00 93.01 O ANISOU 1288 O LEU A 223 11534 11313 12491 92 -399 303 O ATOM 1289 CB LEU A 223 33.852 8.472 7.489 1.00 55.92 C ANISOU 1289 CB LEU A 223 6911 6853 7482 260 -666 511 C ATOM 1290 CG LEU A 223 34.707 9.062 8.608 1.00 82.10 C ANISOU 1290 CG LEU A 223 10211 10342 10643 302 -832 466 C ATOM 1291 CD1 LEU A 223 35.399 7.953 9.384 1.00 83.85 C ANISOU 1291 CD1 LEU A 223 10418 10595 10848 454 -980 618 C ATOM 1292 CD2 LEU A 223 35.719 10.033 8.030 1.00 70.59 C ANISOU 1292 CD2 LEU A 223 8612 8926 9282 227 -876 255 C ATOM 1293 N ALA A 224 31.430 8.055 5.562 1.00 64.09 N ANISOU 1293 N ALA A 224 8019 7641 8692 122 -355 520 N ATOM 1294 CA ALA A 224 30.790 7.335 4.469 1.00 59.76 C ANISOU 1294 CA ALA A 224 7450 6958 8296 88 -270 511 C ATOM 1295 C ALA A 224 30.024 8.267 3.540 1.00 73.15 C ANISOU 1295 C ALA A 224 9154 8665 9976 13 -199 395 C ATOM 1296 O ALA A 224 29.814 7.933 2.369 1.00 67.29 O ANISOU 1296 O ALA A 224 8382 7847 9338 -14 -162 328 O ATOM 1297 CB ALA A 224 29.853 6.263 5.022 1.00 50.62 C ANISOU 1297 CB ALA A 224 6346 5719 7170 95 -214 667 C ATOM 1298 N GLY A 225 29.610 9.432 4.030 1.00 65.99 N ANISOU 1298 N GLY A 225 8293 7847 8933 -9 -185 366 N ATOM 1299 CA GLY A 225 28.746 10.299 3.253 1.00 44.73 C ANISOU 1299 CA GLY A 225 5619 5152 6226 -49 -125 288 C ATOM 1300 C GLY A 225 29.433 11.419 2.500 1.00 53.48 C ANISOU 1300 C GLY A 225 6733 6267 7319 -74 -128 175 C ATOM 1301 O GLY A 225 28.878 11.936 1.525 1.00 78.52 O ANISOU 1301 O GLY A 225 9929 9409 10497 -89 -87 128 O ATOM 1302 N PHE A 226 30.632 11.815 2.927 1.00 46.84 N ANISOU 1302 N PHE A 226 5870 5465 6462 -82 -178 134 N ATOM 1303 CA PHE A 226 31.270 12.968 2.304 1.00 45.38 C ANISOU 1303 CA PHE A 226 5693 5270 6282 -134 -151 31 C ATOM 1304 C PHE A 226 32.706 12.705 1.867 1.00 56.63 C ANISOU 1304 C PHE A 226 7019 6691 7805 -157 -170 -25 C ATOM 1305 O PHE A 226 33.053 12.935 0.704 1.00 69.72 O ANISOU 1305 O PHE A 226 8669 8303 9518 -194 -96 -76 O ATOM 1306 CB PHE A 226 31.243 14.169 3.251 1.00 44.86 C ANISOU 1306 CB PHE A 226 5680 5248 6116 -156 -167 -19 C ATOM 1307 CG PHE A 226 31.927 15.382 2.693 1.00 50.09 C ANISOU 1307 CG PHE A 226 6357 5863 6813 -229 -125 -121 C ATOM 1308 CD1 PHE A 226 31.351 16.097 1.658 1.00 44.00 C ANISOU 1308 CD1 PHE A 226 5664 5007 6048 -242 -35 -123 C ATOM 1309 CD2 PHE A 226 33.150 15.801 3.192 1.00 58.32 C ANISOU 1309 CD2 PHE A 226 7330 6941 7887 -288 -178 -211 C ATOM 1310 CE1 PHE A 226 31.977 17.209 1.132 1.00 44.64 C ANISOU 1310 CE1 PHE A 226 5782 5014 6167 -317 30 -187 C ATOM 1311 CE2 PHE A 226 33.781 16.916 2.671 1.00 68.87 C ANISOU 1311 CE2 PHE A 226 8672 8208 9287 -384 -113 -305 C ATOM 1312 CZ PHE A 226 33.192 17.621 1.640 1.00 59.02 C ANISOU 1312 CZ PHE A 226 7530 6850 8045 -401 5 -281 C ATOM 1313 N PHE A 227 33.555 12.247 2.789 1.00 50.29 N ANISOU 1313 N PHE A 227 6139 5951 7019 -127 -267 -17 N ATOM 1314 CA PHE A 227 34.979 12.150 2.488 1.00 57.30 C ANISOU 1314 CA PHE A 227 6892 6856 8022 -144 -293 -94 C ATOM 1315 C PHE A 227 35.307 10.960 1.594 1.00 74.53 C ANISOU 1315 C PHE A 227 9005 8980 10332 -93 -256 -76 C ATOM 1316 O PHE A 227 36.276 11.020 0.827 1.00 77.54 O ANISOU 1316 O PHE A 227 9286 9355 10820 -122 -202 -161 O ATOM 1317 CB PHE A 227 35.783 12.085 3.786 1.00 54.10 C ANISOU 1317 CB PHE A 227 6409 6557 7588 -107 -443 -103 C ATOM 1318 CG PHE A 227 35.688 13.334 4.617 1.00 49.34 C ANISOU 1318 CG PHE A 227 5863 6016 6867 -170 -482 -180 C ATOM 1319 CD1 PHE A 227 36.357 14.488 4.239 1.00 54.06 C ANISOU 1319 CD1 PHE A 227 6415 6598 7529 -285 -438 -320 C ATOM 1320 CD2 PHE A 227 34.928 13.357 5.773 1.00 48.31 C ANISOU 1320 CD2 PHE A 227 5838 5950 6565 -121 -542 -120 C ATOM 1321 CE1 PHE A 227 36.268 15.640 5.000 1.00 44.98 C ANISOU 1321 CE1 PHE A 227 5324 5475 6292 -350 -471 -416 C ATOM 1322 CE2 PHE A 227 34.836 14.503 6.537 1.00 54.31 C ANISOU 1322 CE2 PHE A 227 6659 6765 7211 -172 -571 -221 C ATOM 1323 CZ PHE A 227 35.507 15.646 6.151 1.00 45.75 C ANISOU 1323 CZ PHE A 227 5528 5644 6210 -286 -543 -379 C ATOM 1324 N THR A 228 34.523 9.877 1.671 1.00 66.81 N ANISOU 1324 N THR A 228 8075 7950 9359 -26 -267 21 N ATOM 1325 CA THR A 228 34.766 8.745 0.782 1.00 47.56 C ANISOU 1325 CA THR A 228 5586 5428 7055 20 -225 9 C ATOM 1326 C THR A 228 34.525 9.106 -0.683 1.00 57.67 C ANISOU 1326 C THR A 228 6906 6671 8336 -41 -102 -82 C ATOM 1327 O THR A 228 35.439 8.910 -1.498 1.00 77.58 O ANISOU 1327 O THR A 228 9348 9183 10946 -39 -39 -167 O ATOM 1328 CB THR A 228 33.929 7.539 1.220 1.00 49.36 C ANISOU 1328 CB THR A 228 5867 5578 7310 82 -255 126 C ATOM 1329 OG1 THR A 228 34.235 7.211 2.581 1.00 51.62 O ANISOU 1329 OG1 THR A 228 6144 5908 7561 152 -363 237 O ATOM 1330 CG2 THR A 228 34.216 6.342 0.335 1.00 44.69 C ANISOU 1330 CG2 THR A 228 5229 4871 6880 129 -215 86 C ATOM 1331 N PRO A 229 33.357 9.636 -1.080 1.00 53.77 N ANISOU 1331 N PRO A 229 6525 6166 7738 -81 -62 -68 N ATOM 1332 CA PRO A 229 33.210 10.051 -2.485 1.00 57.78 C ANISOU 1332 CA PRO A 229 7089 6659 8207 -119 35 -141 C ATOM 1333 C PRO A 229 34.130 11.193 -2.863 1.00 42.47 C ANISOU 1333 C PRO A 229 5139 4751 6245 -183 113 -194 C ATOM 1334 O PRO A 229 34.466 11.331 -4.044 1.00 65.02 O ANISOU 1334 O PRO A 229 8021 7599 9085 -206 219 -250 O ATOM 1335 CB PRO A 229 31.736 10.463 -2.578 1.00 54.85 C ANISOU 1335 CB PRO A 229 6823 6286 7730 -125 19 -98 C ATOM 1336 CG PRO A 229 31.393 10.897 -1.206 1.00 43.82 C ANISOU 1336 CG PRO A 229 5431 4921 6297 -122 -39 -26 C ATOM 1337 CD PRO A 229 32.158 9.979 -0.295 1.00 44.55 C ANISOU 1337 CD PRO A 229 5438 5015 6474 -85 -99 11 C ATOM 1338 N LEU A 230 34.540 12.014 -1.895 1.00 44.03 N ANISOU 1338 N LEU A 230 5307 4984 6437 -219 72 -184 N ATOM 1339 CA LEU A 230 35.553 13.030 -2.149 1.00 47.42 C ANISOU 1339 CA LEU A 230 5696 5424 6898 -306 151 -250 C ATOM 1340 C LEU A 230 36.855 12.395 -2.622 1.00 45.24 C ANISOU 1340 C LEU A 230 5261 5167 6759 -306 205 -325 C ATOM 1341 O LEU A 230 37.389 12.759 -3.676 1.00 62.10 O ANISOU 1341 O LEU A 230 7395 7288 8909 -364 355 -375 O ATOM 1342 CB LEU A 230 35.778 13.860 -0.886 1.00 42.78 C ANISOU 1342 CB LEU A 230 5084 4871 6301 -347 67 -262 C ATOM 1343 CG LEU A 230 36.940 14.849 -0.900 1.00 43.23 C ANISOU 1343 CG LEU A 230 5055 4930 6440 -461 125 -357 C ATOM 1344 CD1 LEU A 230 36.711 15.921 -1.946 1.00 43.21 C ANISOU 1344 CD1 LEU A 230 5184 4838 6397 -545 290 -350 C ATOM 1345 CD2 LEU A 230 37.124 15.468 0.475 1.00 52.22 C ANISOU 1345 CD2 LEU A 230 6160 6117 7563 -491 -1 -403 C ATOM 1346 N ALA A 231 37.376 11.431 -1.856 1.00 46.99 N ANISOU 1346 N ALA A 231 5350 5422 7082 -229 94 -325 N ATOM 1347 CA ALA A 231 38.599 10.740 -2.255 1.00 47.38 C ANISOU 1347 CA ALA A 231 5223 5489 7292 -196 136 -404 C ATOM 1348 C ALA A 231 38.423 10.051 -3.601 1.00 57.29 C ANISOU 1348 C ALA A 231 6527 6691 8551 -165 270 -442 C ATOM 1349 O ALA A 231 39.314 10.098 -4.458 1.00 48.94 O ANISOU 1349 O ALA A 231 5383 5649 7565 -194 413 -532 O ATOM 1350 CB ALA A 231 39.010 9.729 -1.183 1.00 43.48 C ANISOU 1350 CB ALA A 231 4606 5020 6892 -76 -32 -367 C ATOM 1351 N ILE A 232 37.271 9.404 -3.803 1.00 48.53 N ANISOU 1351 N ILE A 232 5550 5525 7363 -114 233 -390 N ATOM 1352 CA ILE A 232 36.973 8.769 -5.086 1.00 42.85 C ANISOU 1352 CA ILE A 232 4898 4764 6620 -90 336 -454 C ATOM 1353 C ILE A 232 37.093 9.782 -6.217 1.00 43.31 C ANISOU 1353 C ILE A 232 5045 4858 6554 -175 497 -495 C ATOM 1354 O ILE A 232 37.706 9.513 -7.256 1.00 52.16 O ANISOU 1354 O ILE A 232 6146 5990 7684 -173 641 -586 O ATOM 1355 CB ILE A 232 35.572 8.128 -5.057 1.00 42.32 C ANISOU 1355 CB ILE A 232 4953 4639 6489 -55 252 -404 C ATOM 1356 CG1 ILE A 232 35.526 6.966 -4.062 1.00 42.24 C ANISOU 1356 CG1 ILE A 232 4873 4561 6616 27 137 -348 C ATOM 1357 CG2 ILE A 232 35.163 7.663 -6.452 1.00 42.84 C ANISOU 1357 CG2 ILE A 232 5105 4682 6490 -48 336 -502 C ATOM 1358 CD1 ILE A 232 34.151 6.341 -3.930 1.00 41.79 C ANISOU 1358 CD1 ILE A 232 4913 4434 6532 31 77 -295 C ATOM 1359 N MET A 233 36.521 10.973 -6.019 1.00 46.65 N ANISOU 1359 N MET A 233 5579 5290 6855 -243 488 -421 N ATOM 1360 CA MET A 233 36.523 11.980 -7.075 1.00 44.64 C ANISOU 1360 CA MET A 233 5451 5042 6468 -312 639 -416 C ATOM 1361 C MET A 233 37.916 12.548 -7.319 1.00 59.21 C ANISOU 1361 C MET A 233 7182 6907 8408 -400 802 -470 C ATOM 1362 O MET A 233 38.234 12.931 -8.451 1.00 86.89 O ANISOU 1362 O MET A 233 10764 10420 11830 -445 987 -486 O ATOM 1363 CB MET A 233 35.529 13.092 -6.738 1.00 42.98 C ANISOU 1363 CB MET A 233 5388 4807 6135 -339 582 -317 C ATOM 1364 CG MET A 233 34.076 12.644 -6.823 1.00 60.98 C ANISOU 1364 CG MET A 233 7774 7085 8312 -261 462 -277 C ATOM 1365 SD MET A 233 32.901 13.893 -6.273 1.00 92.34 S ANISOU 1365 SD MET A 233 11875 11029 12180 -259 390 -173 S ATOM 1366 CE MET A 233 33.143 15.158 -7.518 1.00 51.92 C ANISOU 1366 CE MET A 233 6927 5877 6923 -300 550 -127 C ATOM 1367 N ILE A 234 38.757 12.609 -6.285 1.00 52.05 N ANISOU 1367 N ILE A 234 6088 6017 7670 -428 738 -500 N ATOM 1368 CA ILE A 234 40.150 12.998 -6.486 1.00 45.35 C ANISOU 1368 CA ILE A 234 5067 5199 6964 -517 884 -581 C ATOM 1369 C ILE A 234 40.867 11.955 -7.331 1.00 52.78 C ANISOU 1369 C ILE A 234 5896 6174 7984 -452 1004 -677 C ATOM 1370 O ILE A 234 41.570 12.285 -8.293 1.00 49.53 O ANISOU 1370 O ILE A 234 5463 5782 7575 -522 1233 -729 O ATOM 1371 CB ILE A 234 40.857 13.202 -5.134 1.00 46.40 C ANISOU 1371 CB ILE A 234 4999 5369 7262 -546 739 -617 C ATOM 1372 CG1 ILE A 234 40.155 14.277 -4.306 1.00 56.04 C ANISOU 1372 CG1 ILE A 234 6346 6554 8394 -611 638 -554 C ATOM 1373 CG2 ILE A 234 42.314 13.573 -5.347 1.00 47.75 C ANISOU 1373 CG2 ILE A 234 4941 5582 7619 -649 880 -726 C ATOM 1374 CD1 ILE A 234 40.771 14.480 -2.939 1.00 44.65 C ANISOU 1374 CD1 ILE A 234 4731 5168 7066 -634 470 -610 C ATOM 1375 N VAL A 235 40.698 10.678 -6.976 1.00 45.79 N ANISOU 1375 N VAL A 235 4944 5283 7169 -316 870 -703 N ATOM 1376 CA VAL A 235 41.309 9.588 -7.735 1.00 48.48 C ANISOU 1376 CA VAL A 235 5187 5630 7603 -228 975 -814 C ATOM 1377 C VAL A 235 40.870 9.646 -9.192 1.00 49.84 C ANISOU 1377 C VAL A 235 5553 5804 7581 -247 1160 -847 C ATOM 1378 O VAL A 235 41.698 9.647 -10.110 1.00 73.86 O ANISOU 1378 O VAL A 235 8537 8887 10638 -272 1383 -940 O ATOM 1379 CB VAL A 235 40.964 8.231 -7.095 1.00 46.38 C ANISOU 1379 CB VAL A 235 4877 5308 7437 -75 791 -811 C ATOM 1380 CG1 VAL A 235 41.443 7.083 -7.978 1.00 47.46 C ANISOU 1380 CG1 VAL A 235 4951 5415 7668 27 907 -944 C ATOM 1381 CG2 VAL A 235 41.574 8.135 -5.706 1.00 52.21 C ANISOU 1381 CG2 VAL A 235 5424 6070 8342 -32 613 -771 C ATOM 1382 N THR A 236 39.557 9.718 -9.424 1.00 46.69 N ANISOU 1382 N THR A 236 5380 5374 6985 -233 1072 -776 N ATOM 1383 CA THR A 236 39.053 9.776 -10.792 1.00 47.52 C ANISOU 1383 CA THR A 236 5685 5504 6866 -234 1202 -807 C ATOM 1384 C THR A 236 39.505 11.042 -11.509 1.00 48.44 C ANISOU 1384 C THR A 236 5891 5660 6855 -348 1416 -754 C ATOM 1385 O THR A 236 39.601 11.052 -12.742 1.00 63.75 O ANISOU 1385 O THR A 236 7954 7644 8623 -348 1596 -797 O ATOM 1386 CB THR A 236 37.529 9.682 -10.797 1.00 49.18 C ANISOU 1386 CB THR A 236 6084 5689 6913 -195 1027 -742 C ATOM 1387 OG1 THR A 236 36.982 10.756 -10.023 1.00 73.53 O ANISOU 1387 OG1 THR A 236 9225 8757 9957 -251 934 -602 O ATOM 1388 CG2 THR A 236 37.079 8.355 -10.204 1.00 46.10 C ANISOU 1388 CG2 THR A 236 5617 5236 6662 -105 860 -794 C ATOM 1389 N TYR A 237 39.788 12.112 -10.763 1.00 48.00 N ANISOU 1389 N TYR A 237 5787 5578 6872 -448 1409 -665 N ATOM 1390 CA TYR A 237 40.322 13.325 -11.374 1.00 49.01 C ANISOU 1390 CA TYR A 237 5988 5703 6932 -577 1637 -608 C ATOM 1391 C TYR A 237 41.688 13.061 -11.995 1.00 52.96 C ANISOU 1391 C TYR A 237 6315 6258 7552 -625 1893 -722 C ATOM 1392 O TYR A 237 41.877 13.223 -13.206 1.00 60.00 O ANISOU 1392 O TYR A 237 7336 7186 8276 -648 2130 -726 O ATOM 1393 CB TYR A 237 40.402 14.445 -10.335 1.00 48.28 C ANISOU 1393 CB TYR A 237 5852 5546 6946 -684 1567 -528 C ATOM 1394 CG TYR A 237 41.177 15.660 -10.796 1.00 52.72 C ANISOU 1394 CG TYR A 237 6437 6066 7530 -850 1819 -486 C ATOM 1395 CD1 TYR A 237 40.575 16.636 -11.579 1.00 63.77 C ANISOU 1395 CD1 TYR A 237 8118 7400 8713 -889 1938 -345 C ATOM 1396 CD2 TYR A 237 42.509 15.834 -10.442 1.00 50.22 C ANISOU 1396 CD2 TYR A 237 5851 5766 7463 -967 1939 -581 C ATOM 1397 CE1 TYR A 237 41.277 17.747 -12.000 1.00 51.40 C ANISOU 1397 CE1 TYR A 237 6593 5760 7179 -1051 2194 -283 C ATOM 1398 CE2 TYR A 237 43.219 16.942 -10.860 1.00 51.53 C ANISOU 1398 CE2 TYR A 237 6024 5875 7682 -1147 2193 -547 C ATOM 1399 CZ TYR A 237 42.597 17.895 -11.638 1.00 52.10 C ANISOU 1399 CZ TYR A 237 6405 5855 7535 -1195 2332 -389 C ATOM 1400 OH TYR A 237 43.298 19.001 -12.058 1.00 55.29 O ANISOU 1400 OH TYR A 237 6838 6168 8003 -1385 2610 -332 O ATOM 1401 N PHE A 238 42.656 12.647 -11.172 1.00 62.57 N ANISOU 1401 N PHE A 238 7230 7494 9052 -629 1851 -818 N ATOM 1402 CA PHE A 238 43.990 12.348 -11.684 1.00 56.18 C ANISOU 1402 CA PHE A 238 6196 6745 8404 -661 2090 -947 C ATOM 1403 C PHE A 238 43.946 11.242 -12.730 1.00 52.82 C ANISOU 1403 C PHE A 238 5830 6365 7875 -534 2201 -1055 C ATOM 1404 O PHE A 238 44.688 11.286 -13.719 1.00 54.52 O ANISOU 1404 O PHE A 238 6020 6638 8057 -574 2497 -1128 O ATOM 1405 CB PHE A 238 44.921 11.965 -10.533 1.00 53.04 C ANISOU 1405 CB PHE A 238 5447 6374 8333 -642 1954 -1037 C ATOM 1406 CG PHE A 238 45.272 13.112 -9.628 1.00 51.61 C ANISOU 1406 CG PHE A 238 5163 6172 8274 -797 1894 -992 C ATOM 1407 CD1 PHE A 238 46.152 14.096 -10.047 1.00 53.02 C ANISOU 1407 CD1 PHE A 238 5249 6352 8542 -986 2155 -1014 C ATOM 1408 CD2 PHE A 238 44.735 13.200 -8.355 1.00 50.21 C ANISOU 1408 CD2 PHE A 238 4983 5969 8125 -764 1593 -940 C ATOM 1409 CE1 PHE A 238 46.482 15.151 -9.218 1.00 63.66 C ANISOU 1409 CE1 PHE A 238 6500 7662 10027 -1147 2097 -1004 C ATOM 1410 CE2 PHE A 238 45.062 14.252 -7.520 1.00 53.06 C ANISOU 1410 CE2 PHE A 238 5258 6314 8588 -906 1532 -935 C ATOM 1411 CZ PHE A 238 45.936 15.229 -7.952 1.00 55.15 C ANISOU 1411 CZ PHE A 238 5425 6565 8963 -1102 1775 -977 C ATOM 1412 N LEU A 239 43.084 10.240 -12.530 1.00 51.87 N ANISOU 1412 N LEU A 239 5789 6214 7703 -388 1983 -1079 N ATOM 1413 CA LEU A 239 42.917 9.198 -13.539 1.00 56.95 C ANISOU 1413 CA LEU A 239 6519 6881 8239 -275 2069 -1209 C ATOM 1414 C LEU A 239 42.431 9.785 -14.858 1.00 55.03 C ANISOU 1414 C LEU A 239 6568 6691 7648 -323 2255 -1171 C ATOM 1415 O LEU A 239 42.831 9.327 -15.936 1.00 55.45 O ANISOU 1415 O LEU A 239 6665 6810 7595 -286 2472 -1297 O ATOM 1416 CB LEU A 239 41.946 8.125 -13.043 1.00 51.63 C ANISOU 1416 CB LEU A 239 5899 6134 7586 -144 1792 -1230 C ATOM 1417 CG LEU A 239 42.452 7.133 -11.996 1.00 51.18 C ANISOU 1417 CG LEU A 239 5590 6014 7843 -37 1636 -1284 C ATOM 1418 CD1 LEU A 239 41.348 6.161 -11.621 1.00 50.20 C ANISOU 1418 CD1 LEU A 239 5574 5790 7709 62 1404 -1274 C ATOM 1419 CD2 LEU A 239 43.670 6.390 -12.514 1.00 52.86 C ANISOU 1419 CD2 LEU A 239 5594 6252 8238 41 1833 -1464 C ATOM 1420 N THR A 240 41.574 10.808 -14.794 1.00 54.89 N ANISOU 1420 N THR A 240 6764 6652 7440 -392 2175 -997 N ATOM 1421 CA THR A 240 41.087 11.441 -16.016 1.00 54.39 C ANISOU 1421 CA THR A 240 7000 6640 7026 -417 2326 -923 C ATOM 1422 C THR A 240 42.201 12.200 -16.725 1.00 56.16 C ANISOU 1422 C THR A 240 7207 6907 7225 -537 2693 -900 C ATOM 1423 O THR A 240 42.293 12.166 -17.958 1.00 57.92 O ANISOU 1423 O THR A 240 7606 7212 7189 -522 2915 -929 O ATOM 1424 CB THR A 240 39.916 12.370 -15.695 1.00 53.39 C ANISOU 1424 CB THR A 240 7085 6461 6741 -436 2138 -732 C ATOM 1425 OG1 THR A 240 38.858 11.610 -15.101 1.00 52.02 O ANISOU 1425 OG1 THR A 240 6911 6261 6592 -334 1830 -764 O ATOM 1426 CG2 THR A 240 39.399 13.036 -16.961 1.00 54.87 C ANISOU 1426 CG2 THR A 240 7595 6704 6550 -431 2267 -630 C ATOM 1427 N ILE A 241 43.057 12.887 -15.964 1.00 55.95 N ANISOU 1427 N ILE A 241 6967 6830 7460 -665 2769 -857 N ATOM 1428 CA ILE A 241 44.220 13.546 -16.555 1.00 57.80 C ANISOU 1428 CA ILE A 241 7123 7094 7743 -808 3142 -855 C ATOM 1429 C ILE A 241 45.079 12.529 -17.293 1.00 59.36 C ANISOU 1429 C ILE A 241 7171 7398 7986 -738 3364 -1058 C ATOM 1430 O ILE A 241 45.449 12.728 -18.456 1.00 61.38 O ANISOU 1430 O ILE A 241 7559 7726 8035 -775 3689 -1063 O ATOM 1431 CB ILE A 241 45.031 14.293 -15.477 1.00 57.31 C ANISOU 1431 CB ILE A 241 6789 6964 8023 -962 3139 -832 C ATOM 1432 CG1 ILE A 241 44.492 15.711 -15.264 1.00 56.93 C ANISOU 1432 CG1 ILE A 241 6953 6798 7879 -1092 3126 -624 C ATOM 1433 CG2 ILE A 241 46.507 14.351 -15.853 1.00 83.50 C ANISOU 1433 CG2 ILE A 241 9835 10340 11551 -1076 3486 -944 C ATOM 1434 CD1 ILE A 241 43.185 15.781 -14.507 1.00 63.86 C ANISOU 1434 CD1 ILE A 241 7987 7611 8667 -997 2763 -534 C ATOM 1435 N HIS A 242 45.392 11.411 -16.631 1.00 66.81 N ANISOU 1435 N HIS A 242 7849 8345 9189 -623 3199 -1224 N ATOM 1436 CA HIS A 242 46.220 10.386 -17.257 1.00 70.53 C ANISOU 1436 CA HIS A 242 8155 8895 9748 -529 3399 -1439 C ATOM 1437 C HIS A 242 45.526 9.781 -18.471 1.00 61.16 C ANISOU 1437 C HIS A 242 7269 7767 8201 -420 3468 -1513 C ATOM 1438 O HIS A 242 46.174 9.482 -19.479 1.00 63.27 O ANISOU 1438 O HIS A 242 7540 8127 8373 -402 3782 -1644 O ATOM 1439 CB HIS A 242 46.570 9.300 -16.238 1.00 80.01 C ANISOU 1439 CB HIS A 242 9044 10055 11302 -396 3164 -1574 C ATOM 1440 N ALA A 243 44.204 9.606 -18.398 1.00 59.84 N ANISOU 1440 N ALA A 243 7350 7560 7827 -348 3180 -1448 N ATOM 1441 CA ALA A 243 43.474 9.005 -19.510 1.00 60.91 C ANISOU 1441 CA ALA A 243 7760 7763 7619 -245 3190 -1547 C ATOM 1442 C ALA A 243 43.490 9.913 -20.734 1.00 62.85 C ANISOU 1442 C ALA A 243 8290 8115 7475 -320 3477 -1443 C ATOM 1443 O ALA A 243 43.727 9.454 -21.858 1.00 64.92 O ANISOU 1443 O ALA A 243 8673 8487 7506 -264 3698 -1586 O ATOM 1444 CB ALA A 243 42.039 8.686 -19.089 1.00 59.21 C ANISOU 1444 CB ALA A 243 7705 7486 7307 -171 2804 -1499 C ATOM 1445 N LEU A 244 43.239 11.210 -20.536 1.00 62.41 N ANISOU 1445 N LEU A 244 8362 8019 7332 -439 3486 -1191 N ATOM 1446 CA LEU A 244 43.273 12.151 -21.652 1.00 64.43 C ANISOU 1446 CA LEU A 244 8912 8347 7222 -509 3770 -1042 C ATOM 1447 C LEU A 244 44.671 12.239 -22.251 1.00 66.64 C ANISOU 1447 C LEU A 244 9048 8696 7575 -602 4229 -1119 C ATOM 1448 O LEU A 244 44.837 12.197 -23.475 1.00 68.99 O ANISOU 1448 O LEU A 244 9558 9117 7538 -579 4507 -1151 O ATOM 1449 CB LEU A 244 42.799 13.531 -21.194 1.00 71.27 C ANISOU 1449 CB LEU A 244 9918 9105 8056 -617 3693 -752 C ATOM 1450 CG LEU A 244 41.332 13.658 -20.790 1.00 87.48 C ANISOU 1450 CG LEU A 244 12157 11108 9973 -522 3291 -646 C ATOM 1451 CD1 LEU A 244 41.034 15.070 -20.316 1.00107.13 C ANISOU 1451 CD1 LEU A 244 14758 13468 12478 -624 3266 -378 C ATOM 1452 CD2 LEU A 244 40.434 13.282 -21.953 1.00 63.77 C ANISOU 1452 CD2 LEU A 244 9476 8235 6520 -385 3224 -675 C ATOM 1453 N GLN A 245 45.692 12.361 -21.398 1.00 78.86 N ANISOU 1453 N GLN A 245 10225 10181 9556 -705 4315 -1159 N ATOM 1454 CA GLN A 245 47.062 12.454 -21.893 1.00 75.16 C ANISOU 1454 CA GLN A 245 9554 9782 9220 -806 4758 -1247 C ATOM 1455 C GLN A 245 47.494 11.173 -22.595 1.00 80.27 C ANISOU 1455 C GLN A 245 10117 10547 9836 -648 4850 -1514 C ATOM 1456 O GLN A 245 48.369 11.211 -23.468 1.00 72.38 O ANISOU 1456 O GLN A 245 9089 9638 8773 -673 5109 -1540 O ATOM 1457 CB GLN A 245 48.018 12.786 -20.745 1.00 67.58 C ANISOU 1457 CB GLN A 245 8170 8743 8765 -936 4755 -1263 C ATOM 1458 CG GLN A 245 47.850 14.191 -20.182 1.00 90.75 C ANISOU 1458 CG GLN A 245 11175 11551 11754 -1126 4723 -1017 C ATOM 1459 CD GLN A 245 48.924 14.549 -19.172 1.00 97.75 C ANISOU 1459 CD GLN A 245 11637 12382 13121 -1268 4714 -1068 C ATOM 1460 OE1 GLN A 245 49.016 13.942 -18.104 1.00106.81 O ANISOU 1460 OE1 GLN A 245 12499 13518 14567 -1199 4451 -1193 O ATOM 1461 NE2 GLN A 245 49.746 15.536 -19.508 1.00 69.94 N ANISOU 1461 NE2 GLN A 245 8088 8823 9663 -1447 4925 -964 N ATOM 1462 N LYS A 246 46.896 10.035 -22.236 1.00 78.23 N ANISOU 1462 N LYS A 246 9821 10268 9633 -478 4575 -1694 N ATOM 1463 CA LYS A 246 47.202 8.789 -22.929 1.00 70.03 C ANISOU 1463 CA LYS A 246 8740 9310 8559 -319 4662 -1969 C ATOM 1464 C LYS A 246 46.478 8.705 -24.267 1.00 71.74 C ANISOU 1464 C LYS A 246 9375 9645 8237 -252 4717 -1979 C ATOM 1465 O LYS A 246 47.042 8.214 -25.251 1.00 74.23 O ANISOU 1465 O LYS A 246 9714 10073 8418 -185 4898 -2109 O ATOM 1466 CB LYS A 246 46.841 7.592 -22.051 1.00 68.24 C ANISOU 1466 CB LYS A 246 8329 8978 8619 -165 4321 -2142 C ATOM 1467 N LYS A 247 45.231 9.179 -24.323 1.00 88.85 N ANISOU 1467 N LYS A 247 11868 11798 10091 -254 4515 -1833 N ATOM 1468 CA LYS A 247 44.485 9.161 -25.578 1.00 72.52 C ANISOU 1468 CA LYS A 247 10208 9868 7480 -180 4540 -1843 C ATOM 1469 C LYS A 247 45.122 10.080 -26.613 1.00 75.21 C ANISOU 1469 C LYS A 247 10700 10324 7554 -262 4843 -1650 C ATOM 1470 O LYS A 247 45.171 9.747 -27.803 1.00 77.82 O ANISOU 1470 O LYS A 247 11215 10812 7542 -178 4949 -1736 O ATOM 1471 CB LYS A 247 43.029 9.557 -25.327 1.00 70.88 C ANISOU 1471 CB LYS A 247 10257 9617 7057 -149 4140 -1673 C ATOM 1472 CG LYS A 247 42.272 9.993 -26.574 1.00 72.95 C ANISOU 1472 CG LYS A 247 10964 10033 6721 -98 4172 -1584 C ATOM 1473 CD LYS A 247 40.824 10.337 -26.261 1.00 71.40 C ANISOU 1473 CD LYS A 247 10958 9798 6373 -45 3734 -1430 C ATOM 1474 CE LYS A 247 40.005 9.088 -25.976 1.00 76.03 C ANISOU 1474 CE LYS A 247 11462 10365 7058 71 3366 -1692 C ATOM 1475 NZ LYS A 247 38.555 9.398 -25.837 1.00 72.01 N ANISOU 1475 NZ LYS A 247 11135 9857 6368 126 2964 -1568 N ATOM 1476 N ALA A 248 45.626 11.237 -26.177 1.00 87.91 N ANISOU 1476 N ALA A 248 12229 11850 9324 -429 4983 -1398 N ATOM 1477 CA ALA A 248 46.167 12.210 -27.121 1.00 77.51 C ANISOU 1477 CA ALA A 248 11073 10604 7773 -524 5265 -1184 C ATOM 1478 C ALA A 248 47.404 11.673 -27.829 1.00 81.15 C ANISOU 1478 C ALA A 248 11339 11182 8311 -513 5562 -1353 C ATOM 1479 O ALA A 248 47.632 11.971 -29.007 1.00 85.21 O ANISOU 1479 O ALA A 248 12064 11834 8478 -506 5777 -1280 O ATOM 1480 CB ALA A 248 46.486 13.519 -26.399 1.00 76.58 C ANISOU 1480 CB ALA A 248 10878 10327 7892 -721 5335 -910 C ATOM 1481 N ALA A1001 48.216 10.878 -27.130 1.00 82.23 N ANISOU 1481 N ALA A1001 11176 11563 8505 888 -2386 -528 N ATOM 1482 CA ALA A1001 49.463 10.397 -27.715 1.00 81.89 C ANISOU 1482 CA ALA A1001 10612 11597 8907 814 -2617 -515 C ATOM 1483 C ALA A1001 49.201 9.338 -28.779 1.00 81.75 C ANISOU 1483 C ALA A1001 10197 11759 9104 751 -2123 -498 C ATOM 1484 O ALA A1001 49.810 9.363 -29.856 1.00102.04 O ANISOU 1484 O ALA A1001 12208 14518 12045 583 -2060 -527 O ATOM 1485 CB ALA A1001 50.381 9.857 -26.619 1.00 85.00 C ANISOU 1485 CB ALA A1001 11274 11768 9252 1053 -3125 -485 C ATOM 1486 N ASP A1002 48.295 8.396 -28.497 1.00 82.56 N ANISOU 1486 N ASP A1002 10611 11795 8961 864 -1757 -452 N ATOM 1487 CA ASP A1002 47.987 7.349 -29.468 1.00 83.00 C ANISOU 1487 CA ASP A1002 10377 11964 9195 792 -1330 -451 C ATOM 1488 C ASP A1002 47.487 7.942 -30.779 1.00 85.49 C ANISOU 1488 C ASP A1002 10287 12531 9666 524 -1026 -506 C ATOM 1489 O ASP A1002 47.773 7.409 -31.858 1.00111.19 O ANISOU 1489 O ASP A1002 13159 15920 13171 423 -830 -548 O ATOM 1490 CB ASP A1002 46.956 6.378 -28.892 1.00 86.45 C ANISOU 1490 CB ASP A1002 11261 12260 9326 877 -998 -371 C ATOM 1491 CG ASP A1002 47.437 5.701 -27.625 1.00 87.34 C ANISOU 1491 CG ASP A1002 11872 12086 9226 1134 -1296 -285 C ATOM 1492 OD1 ASP A1002 48.664 5.531 -27.470 1.00 89.37 O ANISOU 1492 OD1 ASP A1002 11994 12262 9701 1282 -1736 -304 O ATOM 1493 OD2 ASP A1002 46.587 5.343 -26.784 1.00 87.85 O ANISOU 1493 OD2 ASP A1002 12462 12012 8907 1187 -1091 -189 O ATOM 1494 N LEU A1003 46.747 9.053 -30.707 1.00 77.54 N ANISOU 1494 N LEU A1003 9402 11569 8491 434 -1000 -515 N ATOM 1495 CA LEU A1003 46.267 9.705 -31.922 1.00 74.78 C ANISOU 1495 CA LEU A1003 8733 11418 8262 197 -795 -549 C ATOM 1496 C LEU A1003 47.423 10.245 -32.752 1.00 74.08 C ANISOU 1496 C LEU A1003 8227 11444 8476 18 -1002 -566 C ATOM 1497 O LEU A1003 47.415 10.139 -33.983 1.00 72.75 O ANISOU 1497 O LEU A1003 7731 11451 8458 -172 -765 -584 O ATOM 1498 CB LEU A1003 45.295 10.829 -31.567 1.00 73.07 C ANISOU 1498 CB LEU A1003 8766 11178 7818 208 -796 -562 C ATOM 1499 CG LEU A1003 43.973 10.409 -30.926 1.00 73.30 C ANISOU 1499 CG LEU A1003 9095 11179 7576 344 -463 -549 C ATOM 1500 CD1 LEU A1003 43.191 11.632 -30.483 1.00 72.67 C ANISOU 1500 CD1 LEU A1003 9243 11073 7297 441 -502 -600 C ATOM 1501 CD2 LEU A1003 43.164 9.576 -31.905 1.00 72.05 C ANISOU 1501 CD2 LEU A1003 8666 11173 7535 190 -57 -540 C ATOM 1502 N GLU A1004 48.424 10.835 -32.094 1.00 76.27 N ANISOU 1502 N GLU A1004 8521 11625 8835 53 -1442 -558 N ATOM 1503 CA GLU A1004 49.600 11.318 -32.812 1.00 75.20 C ANISOU 1503 CA GLU A1004 7923 11615 9034 -158 -1622 -554 C ATOM 1504 C GLU A1004 50.363 10.160 -33.439 1.00 76.71 C ANISOU 1504 C GLU A1004 7703 11944 9501 -108 -1429 -586 C ATOM 1505 O GLU A1004 50.745 10.220 -34.614 1.00 83.59 O ANISOU 1505 O GLU A1004 8163 13026 10570 -314 -1200 -601 O ATOM 1506 CB GLU A1004 50.502 12.117 -31.872 1.00 76.75 C ANISOU 1506 CB GLU A1004 8211 11657 9295 -147 -2193 -541 C ATOM 1507 N ASP A1005 50.589 9.091 -32.669 1.00 79.35 N ANISOU 1507 N ASP A1005 8186 12141 9821 184 -1510 -601 N ATOM 1508 CA ASP A1005 51.252 7.916 -33.225 1.00 81.47 C ANISOU 1508 CA ASP A1005 8121 12488 10346 311 -1333 -659 C ATOM 1509 C ASP A1005 50.505 7.395 -34.443 1.00 87.05 C ANISOU 1509 C ASP A1005 8739 13336 11001 184 -802 -709 C ATOM 1510 O ASP A1005 51.121 7.117 -35.474 1.00128.29 O ANISOU 1510 O ASP A1005 13550 18744 16450 114 -588 -780 O ATOM 1511 CB ASP A1005 51.388 6.828 -32.161 1.00 84.90 C ANISOU 1511 CB ASP A1005 8881 12673 10706 665 -1522 -647 C ATOM 1512 CG ASP A1005 52.376 7.201 -31.074 1.00107.11 C ANISOU 1512 CG ASP A1005 11726 15352 13619 818 -2125 -616 C ATOM 1513 OD1 ASP A1005 53.185 8.128 -31.300 1.00111.00 O ANISOU 1513 OD1 ASP A1005 11829 15980 14367 640 -2377 -625 O ATOM 1514 OD2 ASP A1005 52.347 6.568 -29.999 1.00 94.89 O ANISOU 1514 OD2 ASP A1005 10617 13548 11889 1090 -2372 -572 O ATOM 1515 N ASN A1006 49.174 7.296 -34.358 1.00 97.99 N ANISOU 1515 N ASN A1006 10497 14647 12089 142 -587 -682 N ATOM 1516 CA ASN A1006 48.383 6.892 -35.519 1.00 87.56 C ANISOU 1516 CA ASN A1006 9112 13444 10714 -17 -169 -731 C ATOM 1517 C ASN A1006 48.599 7.842 -36.692 1.00 73.49 C ANISOU 1517 C ASN A1006 7017 11895 9012 -303 -76 -742 C ATOM 1518 O ASN A1006 48.758 7.405 -37.838 1.00 74.15 O ANISOU 1518 O ASN A1006 6892 12120 9160 -402 206 -814 O ATOM 1519 CB ASN A1006 46.896 6.833 -35.156 1.00 75.84 C ANISOU 1519 CB ASN A1006 7996 11868 8950 -51 -15 -685 C ATOM 1520 CG ASN A1006 46.565 5.699 -34.204 1.00 78.44 C ANISOU 1520 CG ASN A1006 8670 11971 9165 155 19 -649 C ATOM 1521 OD1 ASN A1006 45.852 5.891 -33.220 1.00 78.12 O ANISOU 1521 OD1 ASN A1006 8965 11818 8897 215 -11 -573 O ATOM 1522 ND2 ASN A1006 47.082 4.510 -34.493 1.00 80.07 N ANISOU 1522 ND2 ASN A1006 8828 12090 9505 271 99 -704 N ATOM 1523 N TRP A1007 48.611 9.150 -36.415 1.00 75.07 N ANISOU 1523 N TRP A1007 7245 12105 9172 -440 -318 -668 N ATOM 1524 CA TRP A1007 48.691 10.156 -37.472 1.00 72.61 C ANISOU 1524 CA TRP A1007 6749 11958 8884 -749 -259 -633 C ATOM 1525 C TRP A1007 49.940 9.977 -38.326 1.00 80.62 C ANISOU 1525 C TRP A1007 7314 13168 10151 -868 -129 -662 C ATOM 1526 O TRP A1007 49.853 9.835 -39.550 1.00 70.30 O ANISOU 1526 O TRP A1007 5887 12024 8800 -1038 194 -693 O ATOM 1527 CB TRP A1007 48.651 11.556 -36.859 1.00 70.95 C ANISOU 1527 CB TRP A1007 6698 11643 8616 -845 -618 -550 C ATOM 1528 CG TRP A1007 49.058 12.644 -37.794 1.00 73.81 C ANISOU 1528 CG TRP A1007 6886 12113 9044 -1187 -649 -477 C ATOM 1529 CD1 TRP A1007 50.289 13.227 -37.893 1.00 70.69 C ANISOU 1529 CD1 TRP A1007 6194 11780 8887 -1388 -827 -420 C ATOM 1530 CD2 TRP A1007 48.227 13.296 -38.758 1.00 72.29 C ANISOU 1530 CD2 TRP A1007 6823 11963 8680 -1396 -519 -429 C ATOM 1531 NE1 TRP A1007 50.275 14.200 -38.861 1.00 70.38 N ANISOU 1531 NE1 TRP A1007 6129 11807 8806 -1742 -774 -321 N ATOM 1532 CE2 TRP A1007 49.020 14.262 -39.408 1.00 72.85 C ANISOU 1532 CE2 TRP A1007 6734 12095 8850 -1731 -609 -326 C ATOM 1533 CE3 TRP A1007 46.889 13.155 -39.137 1.00 77.69 C ANISOU 1533 CE3 TRP A1007 7731 12634 9153 -1343 -364 -455 C ATOM 1534 CZ2 TRP A1007 48.518 15.083 -40.414 1.00 81.02 C ANISOU 1534 CZ2 TRP A1007 7913 13144 9727 -1996 -558 -235 C ATOM 1535 CZ3 TRP A1007 46.393 13.970 -40.135 1.00 81.80 C ANISOU 1535 CZ3 TRP A1007 8340 13185 9555 -1572 -357 -386 C ATOM 1536 CH2 TRP A1007 47.205 14.922 -40.763 1.00 83.45 C ANISOU 1536 CH2 TRP A1007 8472 13421 9814 -1886 -457 -272 C ATOM 1537 N GLU A1008 51.113 9.971 -37.694 1.00 75.13 N ANISOU 1537 N GLU A1008 6362 12468 9717 -773 -375 -660 N ATOM 1538 CA GLU A1008 52.372 9.814 -38.406 1.00 91.40 C ANISOU 1538 CA GLU A1008 7891 14751 12085 -860 -231 -694 C ATOM 1539 C GLU A1008 52.704 8.354 -38.705 1.00 97.49 C ANISOU 1539 C GLU A1008 8501 15570 12969 -564 54 -841 C ATOM 1540 O GLU A1008 53.576 8.105 -39.540 1.00122.34 O ANISOU 1540 O GLU A1008 11214 18943 16326 -602 323 -909 O ATOM 1541 CB GLU A1008 53.510 10.478 -37.613 1.00 83.98 C ANISOU 1541 CB GLU A1008 6663 13797 11448 -900 -671 -632 C ATOM 1542 N THR A1009 52.054 7.391 -38.032 1.00 84.88 N ANISOU 1542 N THR A1009 7259 13752 11239 -268 13 -890 N ATOM 1543 CA THR A1009 51.995 6.018 -38.548 1.00 81.62 C ANISOU 1543 CA THR A1009 6863 13315 10834 -43 331 -1033 C ATOM 1544 C THR A1009 51.380 6.014 -39.934 1.00 83.26 C ANISOU 1544 C THR A1009 7117 13675 10844 -282 757 -1092 C ATOM 1545 O THR A1009 51.962 5.510 -40.906 1.00 77.58 O ANISOU 1545 O THR A1009 6152 13115 10209 -254 1085 -1220 O ATOM 1546 CB THR A1009 51.143 5.123 -37.632 1.00 79.42 C ANISOU 1546 CB THR A1009 7072 12728 10375 195 224 -1025 C ATOM 1547 OG1 THR A1009 51.658 5.144 -36.292 1.00 99.12 O ANISOU 1547 OG1 THR A1009 9645 15050 12966 421 -208 -956 O ATOM 1548 CG2 THR A1009 51.084 3.685 -38.146 1.00 85.45 C ANISOU 1548 CG2 THR A1009 7922 13390 11154 407 500 -1172 C ATOM 1549 N LEU A1010 50.179 6.579 -40.021 1.00 81.14 N ANISOU 1549 N LEU A1010 7180 13351 10296 -494 742 -1009 N ATOM 1550 CA LEU A1010 49.473 6.759 -41.279 1.00 70.63 C ANISOU 1550 CA LEU A1010 5954 12140 8744 -749 1025 -1036 C ATOM 1551 C LEU A1010 50.304 7.551 -42.284 1.00 76.04 C ANISOU 1551 C LEU A1010 6327 13086 9477 -1004 1193 -1010 C ATOM 1552 O LEU A1010 50.532 7.096 -43.409 1.00 76.95 O ANISOU 1552 O LEU A1010 6378 13346 9514 -1060 1550 -1118 O ATOM 1553 CB LEU A1010 48.155 7.470 -40.972 1.00 67.82 C ANISOU 1553 CB LEU A1010 5920 11684 8165 -894 859 -928 C ATOM 1554 CG LEU A1010 47.259 7.831 -42.135 1.00 76.91 C ANISOU 1554 CG LEU A1010 7217 12921 9084 -1153 1007 -925 C ATOM 1555 CD1 LEU A1010 46.721 6.535 -42.634 1.00114.74 C ANISOU 1555 CD1 LEU A1010 12161 17644 13790 -1074 1228 -1068 C ATOM 1556 CD2 LEU A1010 46.145 8.738 -41.653 1.00 69.31 C ANISOU 1556 CD2 LEU A1010 6463 11873 7998 -1227 772 -813 C ATOM 1557 N ASN A1011 50.727 8.761 -41.902 1.00 72.51 N ANISOU 1557 N ASN A1011 5739 12685 9126 -1188 947 -862 N ATOM 1558 CA ASN A1011 51.515 9.621 -42.785 1.00 76.82 C ANISOU 1558 CA ASN A1011 6005 13460 9723 -1512 1098 -784 C ATOM 1559 C ASN A1011 52.813 8.948 -43.243 1.00 82.93 C ANISOU 1559 C ASN A1011 6292 14458 10761 -1409 1414 -899 C ATOM 1560 O ASN A1011 53.161 9.009 -44.430 1.00 93.65 O ANISOU 1560 O ASN A1011 7523 16039 12020 -1605 1818 -924 O ATOM 1561 CB ASN A1011 51.812 10.946 -42.080 1.00 80.43 C ANISOU 1561 CB ASN A1011 6413 13852 10295 -1716 699 -608 C ATOM 1562 CG ASN A1011 51.063 12.116 -42.694 1.00 95.75 C ANISOU 1562 CG ASN A1011 8661 15753 11966 -2058 638 -463 C ATOM 1563 OD1 ASN A1011 50.626 12.051 -43.841 1.00 98.37 O ANISOU 1563 OD1 ASN A1011 9138 16184 12056 -2217 926 -467 O ATOM 1564 ND2 ASN A1011 50.927 13.203 -41.934 1.00111.71 N ANISOU 1564 ND2 ASN A1011 10831 17600 14013 -2157 224 -341 N ATOM 1565 N ASP A1012 53.564 8.333 -42.321 1.00 79.26 N ANISOU 1565 N ASP A1012 5550 13942 10623 -1086 1236 -971 N ATOM 1566 CA ASP A1012 54.814 7.674 -42.707 1.00 87.35 C ANISOU 1566 CA ASP A1012 6038 15186 11965 -912 1517 -1103 C ATOM 1567 C ASP A1012 54.590 6.657 -43.823 1.00105.31 C ANISOU 1567 C ASP A1012 8436 17540 14035 -774 2036 -1301 C ATOM 1568 O ASP A1012 55.285 6.678 -44.844 1.00112.26 O ANISOU 1568 O ASP A1012 9012 18704 14940 -884 2482 -1366 O ATOM 1569 CB ASP A1012 55.458 6.998 -41.494 1.00 86.60 C ANISOU 1569 CB ASP A1012 5730 14949 12224 -494 1161 -1167 C ATOM 1570 N ASN A1013 53.622 5.753 -43.643 1.00117.48 N ANISOU 1570 N ASN A1013 10450 18825 15361 -550 1996 -1402 N ATOM 1571 CA ASN A1013 53.411 4.684 -44.619 1.00113.03 C ANISOU 1571 CA ASN A1013 10073 18264 14609 -395 2411 -1622 C ATOM 1572 C ASN A1013 53.025 5.227 -45.991 1.00 98.78 C ANISOU 1572 C ASN A1013 8446 16649 12435 -767 2765 -1608 C ATOM 1573 O ASN A1013 53.406 4.649 -47.017 1.00 90.16 O ANISOU 1573 O ASN A1013 7330 15701 11227 -695 3215 -1792 O ATOM 1574 CB ASN A1013 52.354 3.709 -44.112 1.00 97.50 C ANISOU 1574 CB ASN A1013 8613 15944 12489 -183 2234 -1692 C ATOM 1575 CG ASN A1013 52.964 2.531 -43.378 1.00112.60 C ANISOU 1575 CG ASN A1013 10436 17665 14684 301 2138 -1831 C ATOM 1576 OD1 ASN A1013 54.180 2.459 -43.202 1.00130.40 O ANISOU 1576 OD1 ASN A1013 12199 20063 17284 525 2162 -1888 O ATOM 1577 ND2 ASN A1013 52.123 1.604 -42.944 1.00103.28 N ANISOU 1577 ND2 ASN A1013 9717 16146 13376 457 2011 -1876 N ATOM 1578 N LEU A1014 52.247 6.310 -46.035 1.00 87.72 N ANISOU 1578 N LEU A1014 7283 15228 10818 -1135 2558 -1403 N ATOM 1579 CA LEU A1014 52.058 7.032 -47.289 1.00 85.67 C ANISOU 1579 CA LEU A1014 7177 15149 10224 -1518 2824 -1334 C ATOM 1580 C LEU A1014 53.391 7.316 -47.973 1.00 85.64 C ANISOU 1580 C LEU A1014 6706 15481 10351 -1634 3248 -1340 C ATOM 1581 O LEU A1014 53.566 7.014 -49.161 1.00 86.12 O ANISOU 1581 O LEU A1014 6870 15712 10141 -1702 3720 -1456 O ATOM 1582 CB LEU A1014 51.298 8.328 -47.032 1.00 75.89 C ANISOU 1582 CB LEU A1014 6159 13823 8851 -1850 2456 -1082 C ATOM 1583 CG LEU A1014 49.785 8.255 -47.229 1.00 73.17 C ANISOU 1583 CG LEU A1014 6340 13277 8183 -1898 2262 -1080 C ATOM 1584 CD1 LEU A1014 49.192 9.652 -47.180 1.00 72.01 C ANISOU 1584 CD1 LEU A1014 6370 13078 7912 -2200 1950 -846 C ATOM 1585 CD2 LEU A1014 49.437 7.550 -48.533 1.00 74.67 C ANISOU 1585 CD2 LEU A1014 6829 13519 8023 -1941 2594 -1243 C ATOM 1586 N LYS A1015 54.346 7.892 -47.237 1.00 87.50 N ANISOU 1586 N LYS A1015 6424 15825 10998 -1670 3094 -1222 N ATOM 1587 CA LYS A1015 55.683 8.090 -47.784 1.00 94.00 C ANISOU 1587 CA LYS A1015 6665 17001 12051 -1777 3514 -1229 C ATOM 1588 C LYS A1015 56.314 6.772 -48.215 1.00105.71 C ANISOU 1588 C LYS A1015 7975 18546 13643 -1319 3929 -1511 C ATOM 1589 O LYS A1015 57.092 6.748 -49.174 1.00108.37 O ANISOU 1589 O LYS A1015 8189 19026 13962 -1344 4380 -1507 O ATOM 1590 CB LYS A1015 56.575 8.790 -46.761 1.00 91.92 C ANISOU 1590 CB LYS A1015 5842 16787 12294 -1854 3158 -1074 C ATOM 1591 N VAL A1016 56.014 5.675 -47.512 1.00115.73 N ANISOU 1591 N VAL A1016 9323 19620 15030 -862 3743 -1719 N ATOM 1592 CA VAL A1016 56.520 4.367 -47.921 1.00109.47 C ANISOU 1592 CA VAL A1016 8418 18860 14314 -391 4126 -2037 C ATOM 1593 C VAL A1016 55.888 3.934 -49.240 1.00102.72 C ANISOU 1593 C VAL A1016 8125 17990 12913 -466 4553 -2186 C ATOM 1594 O VAL A1016 56.577 3.433 -50.137 1.00102.85 O ANISOU 1594 O VAL A1016 8104 18092 12882 -280 5010 -2315 O ATOM 1595 CB VAL A1016 56.283 3.330 -46.807 1.00114.47 C ANISOU 1595 CB VAL A1016 9182 19132 15178 100 3708 -2153 C ATOM 1596 CG1 VAL A1016 56.706 1.948 -47.269 1.00125.93 C ANISOU 1596 CG1 VAL A1016 10638 20533 16678 612 4060 -2496 C ATOM 1597 CG2 VAL A1016 57.029 3.734 -45.542 1.00111.38 C ANISOU 1597 CG2 VAL A1016 8280 18741 15296 206 3251 -2011 C ATOM 1598 N ILE A1017 54.571 4.118 -49.381 1.00106.21 N ANISOU 1598 N ILE A1017 9193 18216 12945 -703 4314 -2113 N ATOM 1599 CA ILE A1017 53.898 3.781 -50.636 1.00104.85 C ANISOU 1599 CA ILE A1017 9588 18025 12226 -824 4626 -2253 C ATOM 1600 C ILE A1017 54.467 4.605 -51.781 1.00 97.70 C ANISOU 1600 C ILE A1017 8671 17360 11090 -1144 5009 -2102 C ATOM 1601 O ILE A1017 54.651 4.103 -52.898 1.00102.13 O ANISOU 1601 O ILE A1017 9519 17947 11338 -1054 5419 -2250 O ATOM 1602 CB ILE A1017 52.376 3.988 -50.510 1.00 96.11 C ANISOU 1602 CB ILE A1017 9085 16622 10809 -1050 4176 -2135 C ATOM 1603 CG1 ILE A1017 51.801 3.090 -49.422 1.00 86.69 C ANISOU 1603 CG1 ILE A1017 8018 15075 9844 -731 3783 -2209 C ATOM 1604 CG2 ILE A1017 51.683 3.711 -51.839 1.00 89.20 C ANISOU 1604 CG2 ILE A1017 8802 15722 9366 -1212 4405 -2270 C ATOM 1605 CD1 ILE A1017 50.320 3.278 -49.189 1.00 82.92 C ANISOU 1605 CD1 ILE A1017 8007 14349 9149 -948 3374 -2089 C ATOM 1606 N GLU A1018 54.758 5.881 -51.520 1.00 97.01 N ANISOU 1606 N GLU A1018 8327 17388 11145 -1512 4844 -1782 N ATOM 1607 CA GLU A1018 55.182 6.788 -52.582 1.00101.14 C ANISOU 1607 CA GLU A1018 8943 18061 11425 -1881 5140 -1571 C ATOM 1608 C GLU A1018 56.480 6.315 -53.226 1.00108.72 C ANISOU 1608 C GLU A1018 9557 19203 12549 -1640 5691 -1657 C ATOM 1609 O GLU A1018 56.612 6.313 -54.455 1.00113.28 O ANISOU 1609 O GLU A1018 10450 19867 12726 -1732 6118 -1664 O ATOM 1610 CB GLU A1018 55.334 8.204 -52.023 1.00108.62 C ANISOU 1610 CB GLU A1018 9649 19051 12570 -2305 4822 -1229 C ATOM 1611 N LYS A1019 57.447 5.897 -52.409 1.00117.63 N ANISOU 1611 N LYS A1019 10037 20400 14258 -1308 5682 -1721 N ATOM 1612 CA LYS A1019 58.758 5.477 -52.888 1.00118.66 C ANISOU 1612 CA LYS A1019 9706 20734 14645 -1039 6186 -1783 C ATOM 1613 C LYS A1019 58.873 3.961 -53.013 1.00120.92 C ANISOU 1613 C LYS A1019 10066 20942 14937 -423 6414 -2166 C ATOM 1614 O LYS A1019 59.971 3.410 -52.882 1.00136.19 O ANISOU 1614 O LYS A1019 11462 23002 17283 -31 6658 -2264 O ATOM 1615 CB LYS A1019 59.852 6.018 -51.966 1.00120.92 C ANISOU 1615 CB LYS A1019 9182 21152 15610 -1062 6007 -1600 C ATOM 1616 N ALA A1020 57.763 3.275 -53.262 1.00117.15 N ANISOU 1616 N ALA A1020 10245 20241 14025 -328 6319 -2387 N ATOM 1617 CA ALA A1020 57.756 1.823 -53.356 1.00120.13 C ANISOU 1617 CA ALA A1020 10805 20461 14377 235 6478 -2775 C ATOM 1618 C ALA A1020 57.948 1.397 -54.808 1.00129.90 C ANISOU 1618 C ALA A1020 12457 21772 15128 335 7048 -2923 C ATOM 1619 O ALA A1020 57.075 1.631 -55.651 1.00131.16 O ANISOU 1619 O ALA A1020 13276 21861 14696 29 7072 -2912 O ATOM 1620 CB ALA A1020 56.453 1.256 -52.795 1.00113.88 C ANISOU 1620 CB ALA A1020 10510 19358 13403 267 6051 -2949 C ATOM 1621 N ASP A1021 59.089 0.767 -55.095 1.00147.54 N ANISOU 1621 N ASP A1021 14310 24148 17600 788 7488 -3065 N ATOM 1622 CA ASP A1021 59.329 0.170 -56.403 1.00154.46 C ANISOU 1622 CA ASP A1021 15590 25090 18007 1018 8054 -3265 C ATOM 1623 C ASP A1021 58.799 -1.251 -56.501 1.00150.89 C ANISOU 1623 C ASP A1021 15682 24305 17344 1512 8015 -3706 C ATOM 1624 O ASP A1021 58.575 -1.740 -57.614 1.00149.84 O ANISOU 1624 O ASP A1021 16152 24131 16650 1623 8335 -3906 O ATOM 1625 CB ASP A1021 60.825 0.177 -56.728 1.00149.08 C ANISOU 1625 CB ASP A1021 14233 24751 17659 1298 8601 -3206 C ATOM 1626 N ASN A1022 58.593 -1.916 -55.368 1.00156.54 N ANISOU 1626 N ASN A1022 16241 24761 18475 1806 7607 -3864 N ATOM 1627 CA ASN A1022 58.035 -3.257 -55.324 1.00147.57 C ANISOU 1627 CA ASN A1022 15653 23226 17191 2239 7495 -4277 C ATOM 1628 C ASN A1022 56.514 -3.187 -55.202 1.00155.53 C ANISOU 1628 C ASN A1022 17328 23955 17813 1825 7054 -4300 C ATOM 1629 O ASN A1022 55.941 -2.158 -54.831 1.00142.29 O ANISOU 1629 O ASN A1022 15560 22382 16122 1303 6758 -3998 O ATOM 1630 CB ASN A1022 58.629 -4.046 -54.154 1.00141.80 C ANISOU 1630 CB ASN A1022 14435 22322 17121 2795 7269 -4432 C ATOM 1631 CG ASN A1022 58.443 -5.547 -54.300 1.00139.91 C ANISOU 1631 CG ASN A1022 14731 21653 16776 3382 7294 -4887 C ATOM 1632 OD1 ASN A1022 57.411 -6.099 -53.916 1.00135.26 O ANISOU 1632 OD1 ASN A1022 14682 20670 16040 3339 6916 -5064 O ATOM 1633 ND2 ASN A1022 59.448 -6.215 -54.854 1.00160.82 N ANISOU 1633 ND2 ASN A1022 17244 24354 19506 3933 7743 -5077 N ATOM 1634 N ALA A1023 55.861 -4.306 -55.529 1.00163.98 N ANISOU 1634 N ALA A1023 19085 24646 18575 2067 6999 -4668 N ATOM 1635 CA ALA A1023 54.405 -4.391 -55.473 1.00139.44 C ANISOU 1635 CA ALA A1023 16629 21238 15113 1681 6589 -4728 C ATOM 1636 C ALA A1023 53.892 -4.829 -54.107 1.00126.01 C ANISOU 1636 C ALA A1023 14820 19223 13836 1772 6087 -4751 C ATOM 1637 O ALA A1023 52.922 -4.251 -53.600 1.00122.27 O ANISOU 1637 O ALA A1023 14472 18644 13340 1328 5598 -4436 O ATOM 1638 CB ALA A1023 53.883 -5.344 -56.551 1.00140.47 C ANISOU 1638 CB ALA A1023 17636 21059 14677 1808 6699 -5084 C ATOM 1639 N ALA A1024 54.532 -5.834 -53.508 1.00141.90 N ANISOU 1639 N ALA A1024 16666 20995 16255 2371 6065 -4969 N ATOM 1640 CA ALA A1024 54.082 -6.365 -52.230 1.00133.26 C ANISOU 1640 CA ALA A1024 15634 19458 15540 2494 5452 -4829 C ATOM 1641 C ALA A1024 53.881 -5.256 -51.193 1.00135.02 C ANISOU 1641 C ALA A1024 15374 19875 16053 2124 5068 -4367 C ATOM 1642 O ALA A1024 52.846 -5.214 -50.521 1.00138.70 O ANISOU 1642 O ALA A1024 16145 20056 16498 1836 4579 -4147 O ATOM 1643 CB ALA A1024 55.089 -7.417 -51.752 1.00133.03 C ANISOU 1643 CB ALA A1024 15371 19225 15948 3244 5523 -5100 C ATOM 1644 N GLN A1025 54.835 -4.315 -51.081 1.00130.75 N ANISOU 1644 N GLN A1025 14090 19821 15768 2096 5301 -4220 N ATOM 1645 CA GLN A1025 54.820 -3.384 -49.945 1.00131.59 C ANISOU 1645 CA GLN A1025 13741 20040 16215 1856 4884 -3830 C ATOM 1646 C GLN A1025 53.562 -2.523 -49.935 1.00141.33 C ANISOU 1646 C GLN A1025 15332 21244 17122 1239 4581 -3537 C ATOM 1647 O GLN A1025 53.006 -2.241 -48.865 1.00142.83 O ANISOU 1647 O GLN A1025 15522 21262 17484 1106 4101 -3286 O ATOM 1648 CB GLN A1025 56.075 -2.500 -49.933 1.00143.38 C ANISOU 1648 CB GLN A1025 14386 22052 18041 1868 5174 -3734 C ATOM 1649 N VAL A1026 53.085 -2.112 -51.113 1.00151.35 N ANISOU 1649 N VAL A1026 16934 22669 17904 886 4845 -3575 N ATOM 1650 CA VAL A1026 51.809 -1.404 -51.178 1.00128.71 C ANISOU 1650 CA VAL A1026 14439 19730 14734 364 4510 -3334 C ATOM 1651 C VAL A1026 50.749 -2.146 -50.373 1.00118.84 C ANISOU 1651 C VAL A1026 13583 18016 13556 390 4026 -3306 C ATOM 1652 O VAL A1026 49.985 -1.532 -49.623 1.00118.03 O ANISOU 1652 O VAL A1026 13456 17860 13529 119 3643 -3029 O ATOM 1653 CB VAL A1026 51.371 -1.199 -52.640 1.00 97.58 C ANISOU 1653 CB VAL A1026 10967 15904 10206 71 4796 -3448 C ATOM 1654 N LYS A1027 50.715 -3.477 -50.468 1.00113.40 N ANISOU 1654 N LYS A1027 13255 16971 12859 722 4051 -3588 N ATOM 1655 CA LYS A1027 49.777 -4.236 -49.645 1.00114.36 C ANISOU 1655 CA LYS A1027 13742 16630 13079 711 3617 -3531 C ATOM 1656 C LYS A1027 50.091 -4.077 -48.158 1.00111.28 C ANISOU 1656 C LYS A1027 12976 16179 13126 877 3326 -3292 C ATOM 1657 O LYS A1027 49.187 -3.850 -47.347 1.00123.75 O ANISOU 1657 O LYS A1027 14667 17610 14743 630 2977 -3052 O ATOM 1658 CB LYS A1027 49.790 -5.712 -50.055 1.00109.26 C ANISOU 1658 CB LYS A1027 13604 15562 12347 1038 3691 -3885 C ATOM 1659 N ASP A1028 51.372 -4.194 -47.780 1.00106.42 N ANISOU 1659 N ASP A1028 11910 15686 12839 1305 3461 -3363 N ATOM 1660 CA ASP A1028 51.756 -4.056 -46.374 1.00105.17 C ANISOU 1660 CA ASP A1028 11435 15453 13070 1489 3125 -3149 C ATOM 1661 C ASP A1028 51.499 -2.638 -45.865 1.00 97.14 C ANISOU 1661 C ASP A1028 10101 14732 12076 1097 2944 -2818 C ATOM 1662 O ASP A1028 50.780 -2.441 -44.877 1.00 96.49 O ANISOU 1662 O ASP A1028 10165 14474 12022 951 2589 -2592 O ATOM 1663 CB ASP A1028 53.229 -4.445 -46.190 1.00103.56 C ANISOU 1663 CB ASP A1028 10756 15347 13247 2042 3269 -3316 C ATOM 1664 N ALA A1029 52.075 -1.637 -46.533 1.00 97.84 N ANISOU 1664 N ALA A1029 9789 15253 12132 919 3203 -2787 N ATOM 1665 CA ALA A1029 51.823 -0.247 -46.160 1.00 90.33 C ANISOU 1665 CA ALA A1029 8609 14537 11177 531 3019 -2488 C ATOM 1666 C ALA A1029 50.324 0.061 -46.076 1.00 87.30 C ANISOU 1666 C ALA A1029 8675 13991 10506 159 2778 -2335 C ATOM 1667 O ALA A1029 49.861 0.659 -45.096 1.00 92.30 O ANISOU 1667 O ALA A1029 9278 14569 11221 37 2454 -2107 O ATOM 1668 CB ALA A1029 52.523 0.688 -47.143 1.00 89.21 C ANISOU 1668 CB ALA A1029 8110 14829 10957 314 3382 -2482 C ATOM 1669 N LEU A1030 49.545 -0.336 -47.091 1.00 83.69 N ANISOU 1669 N LEU A1030 8630 13456 9711 -14 2922 -2470 N ATOM 1670 CA LEU A1030 48.103 -0.084 -47.046 1.00 80.56 C ANISOU 1670 CA LEU A1030 8578 12925 9106 -357 2669 -2337 C ATOM 1671 C LEU A1030 47.441 -0.824 -45.891 1.00 85.51 C ANISOU 1671 C LEU A1030 9399 13201 9888 -255 2386 -2264 C ATOM 1672 O LEU A1030 46.534 -0.287 -45.244 1.00 85.38 O ANISOU 1672 O LEU A1030 9418 13156 9866 -469 2150 -2059 O ATOM 1673 CB LEU A1030 47.439 -0.477 -48.364 1.00 82.95 C ANISOU 1673 CB LEU A1030 9296 13183 9038 -550 2808 -2518 C ATOM 1674 CG LEU A1030 47.724 0.447 -49.551 1.00 81.85 C ANISOU 1674 CG LEU A1030 9113 13378 8608 -782 3044 -2516 C ATOM 1675 CD1 LEU A1030 47.399 -0.216 -50.886 1.00 90.07 C ANISOU 1675 CD1 LEU A1030 10632 14342 9247 -849 3231 -2773 C ATOM 1676 CD2 LEU A1030 46.962 1.740 -49.390 1.00 78.25 C ANISOU 1676 CD2 LEU A1030 8596 13053 8083 -1138 2775 -2235 C ATOM 1677 N THR A1031 47.850 -2.071 -45.641 1.00 84.51 N ANISOU 1677 N THR A1031 9436 12790 9884 75 2423 -2431 N ATOM 1678 CA THR A1031 47.299 -2.811 -44.508 1.00 86.59 C ANISOU 1678 CA THR A1031 9942 12687 10272 153 2170 -2327 C ATOM 1679 C THR A1031 47.549 -2.072 -43.201 1.00 94.62 C ANISOU 1679 C THR A1031 10692 13784 11476 216 1951 -2073 C ATOM 1680 O THR A1031 46.633 -1.894 -42.390 1.00 97.17 O ANISOU 1680 O THR A1031 11164 13994 11761 37 1768 -1880 O ATOM 1681 CB THR A1031 47.892 -4.220 -44.453 1.00 96.66 C ANISOU 1681 CB THR A1031 11459 13609 11658 549 2217 -2542 C ATOM 1682 OG1 THR A1031 47.161 -5.079 -45.336 1.00109.13 O ANISOU 1682 OG1 THR A1031 13500 14940 13023 403 2288 -2735 O ATOM 1683 CG2 THR A1031 47.826 -4.775 -43.038 1.00112.84 C ANISOU 1683 CG2 THR A1031 13661 15324 13888 725 1943 -2372 C ATOM 1684 N LYS A1032 48.785 -1.610 -42.989 1.00104.15 N ANISOU 1684 N LYS A1032 11495 15195 12883 459 1970 -2078 N ATOM 1685 CA LYS A1032 49.097 -0.918 -41.743 1.00 85.70 C ANISOU 1685 CA LYS A1032 8952 12900 10709 525 1695 -1861 C ATOM 1686 C LYS A1032 48.377 0.423 -41.666 1.00 85.66 C ANISOU 1686 C LYS A1032 8865 13118 10564 154 1613 -1669 C ATOM 1687 O LYS A1032 47.916 0.823 -40.590 1.00100.29 O ANISOU 1687 O LYS A1032 10811 14887 12409 118 1381 -1487 O ATOM 1688 CB LYS A1032 50.609 -0.743 -41.596 1.00 86.06 C ANISOU 1688 CB LYS A1032 8532 13116 11052 841 1684 -1924 C ATOM 1689 N MET A1033 48.245 1.121 -42.801 1.00 76.67 N ANISOU 1689 N MET A1033 7607 12240 9284 -104 1799 -1711 N ATOM 1690 CA MET A1033 47.455 2.351 -42.823 1.00 72.70 C ANISOU 1690 CA MET A1033 7093 11892 8639 -431 1686 -1540 C ATOM 1691 C MET A1033 46.003 2.075 -42.461 1.00 71.07 C ANISOU 1691 C MET A1033 7209 11498 8297 -582 1580 -1469 C ATOM 1692 O MET A1033 45.371 2.861 -41.745 1.00 68.87 O ANISOU 1692 O MET A1033 6931 11241 7994 -680 1410 -1305 O ATOM 1693 CB MET A1033 47.534 3.020 -44.195 1.00 77.65 C ANISOU 1693 CB MET A1033 7636 12775 9092 -681 1887 -1590 C ATOM 1694 CG MET A1033 48.813 3.788 -44.455 1.00 87.84 C ANISOU 1694 CG MET A1033 8531 14330 10514 -678 1994 -1565 C ATOM 1695 SD MET A1033 48.785 4.658 -46.036 1.00 92.47 S ANISOU 1695 SD MET A1033 9137 15192 10806 -1045 2249 -1559 S ATOM 1696 CE MET A1033 47.268 5.599 -45.903 1.00 69.05 C ANISOU 1696 CE MET A1033 6458 12143 7633 -1336 1923 -1373 C ATOM 1697 N ARG A1034 45.457 0.962 -42.955 1.00 72.77 N ANISOU 1697 N ARG A1034 7692 11525 8434 -605 1686 -1600 N ATOM 1698 CA ARG A1034 44.090 0.582 -42.617 1.00 76.12 C ANISOU 1698 CA ARG A1034 8359 11773 8788 -792 1602 -1528 C ATOM 1699 C ARG A1034 43.952 0.328 -41.122 1.00 73.08 C ANISOU 1699 C ARG A1034 8063 11202 8502 -649 1483 -1371 C ATOM 1700 O ARG A1034 43.008 0.808 -40.483 1.00 71.30 O ANISOU 1700 O ARG A1034 7857 10998 8236 -791 1415 -1221 O ATOM 1701 CB ARG A1034 43.687 -0.653 -43.421 1.00 80.49 C ANISOU 1701 CB ARG A1034 9206 12109 9266 -862 1699 -1710 C ATOM 1702 CG ARG A1034 42.206 -0.965 -43.407 1.00 75.77 C ANISOU 1702 CG ARG A1034 8786 11385 8619 -1170 1612 -1650 C ATOM 1703 CD ARG A1034 41.918 -2.207 -44.228 1.00 79.99 C ANISOU 1703 CD ARG A1034 9652 11657 9085 -1262 1651 -1849 C ATOM 1704 NE ARG A1034 40.487 -2.395 -44.432 1.00 81.36 N ANISOU 1704 NE ARG A1034 9915 11757 9240 -1635 1529 -1803 N ATOM 1705 CZ ARG A1034 39.685 -3.009 -43.570 1.00 89.29 C ANISOU 1705 CZ ARG A1034 11014 12545 10366 -1777 1491 -1672 C ATOM 1706 NH1 ARG A1034 40.173 -3.499 -42.438 1.00 93.05 N ANISOU 1706 NH1 ARG A1034 11600 12824 10930 -1561 1547 -1566 N ATOM 1707 NH2 ARG A1034 38.393 -3.132 -43.839 1.00 96.92 N ANISOU 1707 NH2 ARG A1034 11964 13494 11368 -2148 1387 -1635 N ATOM 1708 N ALA A1035 44.898 -0.417 -40.543 1.00 81.59 N ANISOU 1708 N ALA A1035 9208 12095 9696 -343 1457 -1408 N ATOM 1709 CA ALA A1035 44.872 -0.676 -39.106 1.00 78.46 C ANISOU 1709 CA ALA A1035 8984 11494 9334 -190 1312 -1245 C ATOM 1710 C ALA A1035 44.969 0.623 -38.316 1.00 76.03 C ANISOU 1710 C ALA A1035 8497 11384 9007 -182 1163 -1092 C ATOM 1711 O ALA A1035 44.229 0.829 -37.347 1.00 75.79 O ANISOU 1711 O ALA A1035 8639 11284 8876 -235 1115 -938 O ATOM 1712 CB ALA A1035 46.005 -1.630 -38.722 1.00 83.32 C ANISOU 1712 CB ALA A1035 9697 11870 10090 187 1234 -1321 C ATOM 1713 N ALA A1036 45.875 1.517 -38.721 1.00 88.09 N ANISOU 1713 N ALA A1036 9699 13153 10620 -131 1106 -1135 N ATOM 1714 CA ALA A1036 46.008 2.798 -38.033 1.00 73.36 C ANISOU 1714 CA ALA A1036 7704 11429 8738 -148 916 -1007 C ATOM 1715 C ALA A1036 44.721 3.608 -38.126 1.00 69.75 C ANISOU 1715 C ALA A1036 7303 11077 8123 -399 956 -927 C ATOM 1716 O ALA A1036 44.309 4.246 -37.150 1.00 69.64 O ANISOU 1716 O ALA A1036 7393 11040 8025 -365 836 -814 O ATOM 1717 CB ALA A1036 47.185 3.588 -38.606 1.00 73.22 C ANISOU 1717 CB ALA A1036 7311 11641 8868 -137 863 -1058 C ATOM 1718 N ALA A1037 44.066 3.587 -39.290 1.00 67.56 N ANISOU 1718 N ALA A1037 6971 10904 7795 -623 1106 -1000 N ATOM 1719 CA ALA A1037 42.834 4.351 -39.461 1.00 64.96 C ANISOU 1719 CA ALA A1037 6637 10678 7365 -826 1097 -936 C ATOM 1720 C ALA A1037 41.728 3.816 -38.559 1.00 65.61 C ANISOU 1720 C ALA A1037 6900 10621 7406 -839 1163 -855 C ATOM 1721 O ALA A1037 41.017 4.588 -37.906 1.00 64.72 O ANISOU 1721 O ALA A1037 6781 10571 7239 -835 1127 -766 O ATOM 1722 CB ALA A1037 42.397 4.328 -40.926 1.00 63.94 C ANISOU 1722 CB ALA A1037 6450 10662 7182 -1056 1178 -1033 C ATOM 1723 N LEU A1038 41.568 2.491 -38.513 1.00 86.12 N ANISOU 1723 N LEU A1038 9675 13020 10028 -856 1280 -886 N ATOM 1724 CA LEU A1038 40.550 1.895 -37.652 1.00 85.09 C ANISOU 1724 CA LEU A1038 9725 12746 9860 -932 1391 -776 C ATOM 1725 C LEU A1038 40.840 2.182 -36.185 1.00 73.54 C ANISOU 1725 C LEU A1038 8436 11204 8302 -714 1343 -642 C ATOM 1726 O LEU A1038 39.938 2.547 -35.421 1.00 70.53 O ANISOU 1726 O LEU A1038 8103 10866 7828 -754 1444 -538 O ATOM 1727 CB LEU A1038 40.466 0.388 -37.899 1.00 72.87 C ANISOU 1727 CB LEU A1038 8405 10930 8354 -1016 1486 -823 C ATOM 1728 CG LEU A1038 39.913 -0.052 -39.253 1.00 72.99 C ANISOU 1728 CG LEU A1038 8356 10964 8413 -1276 1521 -963 C ATOM 1729 CD1 LEU A1038 39.774 -1.565 -39.299 1.00 80.13 C ANISOU 1729 CD1 LEU A1038 9573 11523 9349 -1363 1583 -1002 C ATOM 1730 CD2 LEU A1038 38.579 0.622 -39.522 1.00 71.16 C ANISOU 1730 CD2 LEU A1038 7900 10937 8200 -1537 1529 -913 C ATOM 1731 N ASP A1039 42.100 2.020 -35.774 1.00 72.72 N ANISOU 1731 N ASP A1039 8428 10988 8214 -466 1184 -655 N ATOM 1732 CA ASP A1039 42.478 2.315 -34.396 1.00 74.88 C ANISOU 1732 CA ASP A1039 8928 11162 8362 -248 1050 -539 C ATOM 1733 C ASP A1039 42.180 3.767 -34.041 1.00 72.44 C ANISOU 1733 C ASP A1039 8511 11051 7961 -234 970 -511 C ATOM 1734 O ASP A1039 41.654 4.053 -32.959 1.00 73.37 O ANISOU 1734 O ASP A1039 8863 11124 7890 -160 1012 -416 O ATOM 1735 CB ASP A1039 43.958 1.994 -34.183 1.00 91.51 C ANISOU 1735 CB ASP A1039 11059 13142 10568 20 802 -580 C ATOM 1736 CG ASP A1039 44.467 2.458 -32.836 1.00100.89 C ANISOU 1736 CG ASP A1039 12480 14233 11620 245 548 -477 C ATOM 1737 OD1 ASP A1039 43.749 2.275 -31.830 1.00126.67 O ANISOU 1737 OD1 ASP A1039 16112 17368 14648 250 634 -349 O ATOM 1738 OD2 ASP A1039 45.592 2.998 -32.784 1.00 95.92 O ANISOU 1738 OD2 ASP A1039 11674 13658 11112 400 262 -525 O ATOM 1739 N ALA A1040 42.489 4.697 -34.947 1.00 69.92 N ANISOU 1739 N ALA A1040 7887 10932 7747 -302 868 -595 N ATOM 1740 CA ALA A1040 42.204 6.105 -34.690 1.00 68.61 C ANISOU 1740 CA ALA A1040 7666 10897 7504 -285 749 -577 C ATOM 1741 C ALA A1040 40.706 6.375 -34.630 1.00 67.09 C ANISOU 1741 C ALA A1040 7462 10795 7236 -383 958 -551 C ATOM 1742 O ALA A1040 40.265 7.249 -33.875 1.00 79.61 O ANISOU 1742 O ALA A1040 9148 12407 8693 -263 929 -526 O ATOM 1743 CB ALA A1040 42.863 6.981 -35.753 1.00 67.27 C ANISOU 1743 CB ALA A1040 7217 10882 7460 -387 597 -641 C ATOM 1744 N GLN A1041 39.910 5.640 -35.411 1.00 66.92 N ANISOU 1744 N GLN A1041 7306 10817 7302 -587 1156 -572 N ATOM 1745 CA GLN A1041 38.465 5.837 -35.390 1.00 65.70 C ANISOU 1745 CA GLN A1041 7033 10776 7152 -694 1340 -549 C ATOM 1746 C GLN A1041 37.839 5.256 -34.130 1.00 68.09 C ANISOU 1746 C GLN A1041 7557 10987 7328 -643 1591 -443 C ATOM 1747 O GLN A1041 36.774 5.715 -33.700 1.00 68.64 O ANISOU 1747 O GLN A1041 7533 11181 7367 -630 1772 -417 O ATOM 1748 CB GLN A1041 37.834 5.214 -36.635 1.00 67.79 C ANISOU 1748 CB GLN A1041 7084 11103 7569 -967 1404 -606 C ATOM 1749 CG GLN A1041 36.368 5.559 -36.837 1.00 65.16 C ANISOU 1749 CG GLN A1041 6497 10933 7327 -1091 1503 -599 C ATOM 1750 CD GLN A1041 35.755 4.818 -38.007 1.00 83.38 C ANISOU 1750 CD GLN A1041 8636 13262 9782 -1390 1494 -657 C ATOM 1751 OE1 GLN A1041 36.202 3.730 -38.370 1.00107.00 O ANISOU 1751 OE1 GLN A1041 11782 16093 12779 -1516 1525 -687 O ATOM 1752 NE2 GLN A1041 34.727 5.406 -38.607 1.00 81.23 N ANISOU 1752 NE2 GLN A1041 8071 13163 9630 -1483 1411 -686 N ATOM 1753 N LYS A1042 38.482 4.260 -33.522 1.00 70.29 N ANISOU 1753 N LYS A1042 8139 11045 7523 -598 1617 -377 N ATOM 1754 CA LYS A1042 37.965 3.597 -32.330 1.00 73.40 C ANISOU 1754 CA LYS A1042 8844 11307 7738 -589 1867 -238 C ATOM 1755 C LYS A1042 38.143 4.424 -31.059 1.00 80.72 C ANISOU 1755 C LYS A1042 10057 12225 8390 -316 1836 -194 C ATOM 1756 O LYS A1042 37.886 3.909 -29.967 1.00111.86 O ANISOU 1756 O LYS A1042 14367 16037 12096 -276 2035 -66 O ATOM 1757 CB LYS A1042 38.637 2.231 -32.158 1.00 76.37 C ANISOU 1757 CB LYS A1042 9530 11386 8099 -617 1838 -173 C ATOM 1758 N ALA A1043 38.572 5.680 -31.171 1.00 74.62 N ANISOU 1758 N ALA A1043 9185 11557 7611 -144 1584 -291 N ATOM 1759 CA ALA A1043 38.735 6.562 -30.025 1.00 74.06 C ANISOU 1759 CA ALA A1043 9430 11447 7264 120 1498 -289 C ATOM 1760 C ALA A1043 37.523 7.455 -29.797 1.00 91.89 C ANISOU 1760 C ALA A1043 11561 13896 9457 189 1744 -336 C ATOM 1761 O ALA A1043 37.577 8.347 -28.946 1.00 76.82 O ANISOU 1761 O ALA A1043 9925 11957 7307 440 1674 -381 O ATOM 1762 CB ALA A1043 39.991 7.419 -30.197 1.00 73.36 C ANISOU 1762 CB ALA A1043 9352 11303 7216 257 1028 -370 C ATOM 1763 N THR A1044 36.432 7.240 -30.537 1.00116.44 N ANISOU 1763 N THR A1044 14265 17192 12785 -6 2005 -344 N ATOM 1764 CA THR A1044 35.264 8.107 -30.459 1.00100.84 C ANISOU 1764 CA THR A1044 12050 15426 10839 98 2210 -411 C ATOM 1765 C THR A1044 33.993 7.276 -30.603 1.00 85.17 C ANISOU 1765 C THR A1044 9748 13597 9015 -145 2646 -338 C ATOM 1766 O THR A1044 33.913 6.421 -31.505 1.00 98.97 O ANISOU 1766 O THR A1044 11267 15339 11000 -450 2617 -305 O ATOM 1767 CB THR A1044 35.318 9.193 -31.542 1.00 89.63 C ANISOU 1767 CB THR A1044 10315 14105 9634 134 1878 -534 C ATOM 1768 OG1 THR A1044 36.484 10.003 -31.353 1.00103.62 O ANISOU 1768 OG1 THR A1044 12371 15724 11275 302 1487 -582 O ATOM 1769 CG2 THR A1044 34.079 10.082 -31.488 1.00 94.39 C ANISOU 1769 CG2 THR A1044 10653 14901 10309 305 2043 -617 C ATOM 1770 N PRO A1045 32.997 7.493 -29.749 1.00 81.73 N ANISOU 1770 N PRO A1045 9290 13302 8464 -31 3057 -320 N ATOM 1771 CA PRO A1045 31.712 6.806 -29.911 1.00 89.58 C ANISOU 1771 CA PRO A1045 9862 14490 9682 -299 3485 -248 C ATOM 1772 C PRO A1045 31.008 7.261 -31.176 1.00 95.59 C ANISOU 1772 C PRO A1045 9999 15460 10861 -393 3301 -358 C ATOM 1773 O PRO A1045 30.987 8.461 -31.486 1.00 95.93 O ANISOU 1773 O PRO A1045 9917 15580 10950 -114 3054 -496 O ATOM 1774 CB PRO A1045 30.928 7.223 -28.656 1.00 84.17 C ANISOU 1774 CB PRO A1045 9287 13945 8747 -62 3978 -237 C ATOM 1775 CG PRO A1045 31.574 8.501 -28.216 1.00 86.25 C ANISOU 1775 CG PRO A1045 9889 14129 8751 387 3695 -387 C ATOM 1776 CD PRO A1045 33.028 8.330 -28.539 1.00 81.65 C ANISOU 1776 CD PRO A1045 9663 13269 8090 343 3174 -369 C ATOM 1777 N PRO A1046 30.418 6.329 -31.940 1.00 83.72 N ANISOU 1777 N PRO A1046 8139 14014 9658 -789 3365 -299 N ATOM 1778 CA PRO A1046 29.683 6.645 -33.170 1.00 78.56 C ANISOU 1778 CA PRO A1046 6914 13543 9392 -913 3137 -394 C ATOM 1779 C PRO A1046 28.454 7.513 -32.917 1.00 85.31 C ANISOU 1779 C PRO A1046 7284 14699 10432 -690 3348 -469 C ATOM 1780 O PRO A1046 27.847 7.395 -31.852 1.00121.99 O ANISOU 1780 O PRO A1046 11903 19464 14983 -614 3852 -411 O ATOM 1781 CB PRO A1046 29.273 5.266 -33.700 1.00 79.48 C ANISOU 1781 CB PRO A1046 6861 13610 9726 -1414 3228 -297 C ATOM 1782 CG PRO A1046 29.295 4.376 -32.503 1.00 81.93 C ANISOU 1782 CG PRO A1046 7513 13802 9815 -1529 3683 -126 C ATOM 1783 CD PRO A1046 30.424 4.883 -31.662 1.00 83.98 C ANISOU 1783 CD PRO A1046 8356 13892 9661 -1156 3610 -133 C ATOM 1784 N ASP A1060 30.927 16.017 -38.798 1.00 79.23 N ANISOU 1784 N ASP A1060 7200 13250 9653 564 -279 -961 N ATOM 1785 CA ASP A1060 31.189 14.592 -38.632 1.00 81.30 C ANISOU 1785 CA ASP A1060 7358 13627 9904 241 75 -914 C ATOM 1786 C ASP A1060 32.436 14.177 -39.407 1.00 79.43 C ANISOU 1786 C ASP A1060 7408 13275 9497 -107 -68 -832 C ATOM 1787 O ASP A1060 32.342 13.550 -40.463 1.00 71.26 O ANISOU 1787 O ASP A1060 6262 12298 8517 -399 -166 -808 O ATOM 1788 CB ASP A1060 29.985 13.764 -39.088 1.00 83.39 C ANISOU 1788 CB ASP A1060 7108 14117 10458 85 188 -928 C ATOM 1789 CG ASP A1060 30.148 12.283 -38.796 1.00 94.64 C ANISOU 1789 CG ASP A1060 8471 15607 11881 -242 562 -878 C ATOM 1790 OD1 ASP A1060 30.948 11.933 -37.902 1.00 99.09 O ANISOU 1790 OD1 ASP A1060 9332 16078 12239 -222 820 -844 O ATOM 1791 OD2 ASP A1060 29.481 11.467 -39.467 1.00 95.40 O ANISOU 1791 OD2 ASP A1060 8255 15813 12179 -521 550 -871 O ATOM 1792 N PHE A1061 33.605 14.537 -38.877 1.00 95.19 N ANISOU 1792 N PHE A1061 9767 15112 11289 -66 -84 -804 N ATOM 1793 CA PHE A1061 34.872 14.151 -39.483 1.00 74.42 C ANISOU 1793 CA PHE A1061 7338 12407 8532 -360 -151 -737 C ATOM 1794 C PHE A1061 35.218 12.688 -39.246 1.00 72.28 C ANISOU 1794 C PHE A1061 7003 12198 8263 -547 171 -731 C ATOM 1795 O PHE A1061 36.106 12.162 -39.926 1.00 81.46 O ANISOU 1795 O PHE A1061 8249 13337 9367 -778 157 -706 O ATOM 1796 CB PHE A1061 36.000 15.036 -38.950 1.00 82.85 C ANISOU 1796 CB PHE A1061 8741 13291 9448 -270 -310 -708 C ATOM 1797 CG PHE A1061 35.685 16.505 -38.979 1.00 91.45 C ANISOU 1797 CG PHE A1061 9991 14237 10518 -56 -639 -719 C ATOM 1798 CD1 PHE A1061 35.859 17.241 -40.139 1.00 86.22 C ANISOU 1798 CD1 PHE A1061 9439 13491 9831 -217 -973 -644 C ATOM 1799 CD2 PHE A1061 35.219 17.150 -37.845 1.00 94.74 C ANISOU 1799 CD2 PHE A1061 10513 14573 10910 319 -614 -807 C ATOM 1800 CE1 PHE A1061 35.570 18.590 -40.169 1.00 88.39 C ANISOU 1800 CE1 PHE A1061 9927 13570 10088 -13 -1318 -642 C ATOM 1801 CE2 PHE A1061 34.929 18.498 -37.868 1.00 99.70 C ANISOU 1801 CE2 PHE A1061 11340 15016 11524 560 -940 -842 C ATOM 1802 CZ PHE A1061 35.104 19.220 -39.031 1.00102.47 C ANISOU 1802 CZ PHE A1061 11802 15250 11882 391 -1315 -752 C ATOM 1803 N ARG A1062 34.541 12.027 -38.304 1.00 73.36 N ANISOU 1803 N ARG A1062 7015 12400 8459 -447 476 -751 N ATOM 1804 CA ARG A1062 34.821 10.624 -38.019 1.00 69.19 C ANISOU 1804 CA ARG A1062 6498 11868 7925 -623 756 -725 C ATOM 1805 C ARG A1062 34.513 9.744 -39.223 1.00 79.45 C ANISOU 1805 C ARG A1062 7631 13222 9336 -935 727 -740 C ATOM 1806 O ARG A1062 35.231 8.773 -39.493 1.00 71.25 O ANISOU 1806 O ARG A1062 6715 12108 8250 -1105 812 -740 O ATOM 1807 CB ARG A1062 34.014 10.181 -36.800 1.00 68.62 C ANISOU 1807 CB ARG A1062 6358 11847 7869 -494 1103 -710 C ATOM 1808 CG ARG A1062 34.387 8.830 -36.235 1.00 72.80 C ANISOU 1808 CG ARG A1062 7031 12293 8338 -639 1375 -649 C ATOM 1809 CD ARG A1062 33.621 8.579 -34.949 1.00 69.32 C ANISOU 1809 CD ARG A1062 6604 11896 7838 -514 1745 -603 C ATOM 1810 NE ARG A1062 33.990 7.308 -34.342 1.00 70.62 N ANISOU 1810 NE ARG A1062 7002 11925 7906 -655 1977 -510 N ATOM 1811 CZ ARG A1062 33.393 6.154 -34.614 1.00 73.13 C ANISOU 1811 CZ ARG A1062 7180 12244 8363 -954 2174 -454 C ATOM 1812 NH1 ARG A1062 32.392 6.112 -35.482 1.00 78.04 N ANISOU 1812 NH1 ARG A1062 7384 13022 9243 -1153 2151 -494 N ATOM 1813 NH2 ARG A1062 33.798 5.042 -34.018 1.00 90.47 N ANISOU 1813 NH2 ARG A1062 9678 14252 10446 -1060 2346 -356 N ATOM 1814 N HIS A1063 33.449 10.074 -39.962 1.00 86.03 N ANISOU 1814 N HIS A1063 8205 14167 10315 -988 573 -769 N ATOM 1815 CA HIS A1063 33.119 9.342 -41.182 1.00 71.69 C ANISOU 1815 CA HIS A1063 6289 12379 8571 -1291 454 -800 C ATOM 1816 C HIS A1063 34.276 9.345 -42.175 1.00 66.37 C ANISOU 1816 C HIS A1063 5898 11619 7700 -1430 299 -812 C ATOM 1817 O HIS A1063 34.395 8.421 -42.987 1.00 73.93 O ANISOU 1817 O HIS A1063 6916 12547 8626 -1669 308 -862 O ATOM 1818 CB HIS A1063 31.864 9.940 -41.818 1.00 70.63 C ANISOU 1818 CB HIS A1063 5848 12369 8620 -1276 193 -827 C ATOM 1819 CG HIS A1063 31.446 9.271 -43.091 1.00 86.69 C ANISOU 1819 CG HIS A1063 7819 14415 10704 -1590 -23 -870 C ATOM 1820 ND1 HIS A1063 31.323 7.904 -43.210 1.00 86.24 N ANISOU 1820 ND1 HIS A1063 7742 14319 10706 -1873 144 -900 N ATOM 1821 CD2 HIS A1063 31.113 9.786 -44.298 1.00 94.18 C ANISOU 1821 CD2 HIS A1063 8786 15375 11623 -1667 -433 -891 C ATOM 1822 CE1 HIS A1063 30.937 7.604 -44.437 1.00 89.79 C ANISOU 1822 CE1 HIS A1063 8196 14759 11159 -2112 -156 -959 C ATOM 1823 NE2 HIS A1063 30.802 8.728 -45.118 1.00 89.32 N ANISOU 1823 NE2 HIS A1063 8164 14741 11032 -1990 -510 -949 N ATOM 1824 N GLY A1064 35.142 10.365 -42.120 1.00 64.05 N ANISOU 1824 N GLY A1064 5790 11278 7270 -1298 175 -772 N ATOM 1825 CA GLY A1064 36.287 10.411 -43.016 1.00 63.04 C ANISOU 1825 CA GLY A1064 5880 11107 6966 -1451 106 -766 C ATOM 1826 C GLY A1064 37.193 9.201 -42.903 1.00 66.32 C ANISOU 1826 C GLY A1064 6376 11475 7346 -1535 366 -811 C ATOM 1827 O GLY A1064 37.938 8.888 -43.836 1.00 64.84 O ANISOU 1827 O GLY A1064 6311 11289 7037 -1683 388 -850 O ATOM 1828 N PHE A1065 37.148 8.505 -41.763 1.00 69.86 N ANISOU 1828 N PHE A1065 6788 11872 7883 -1422 575 -809 N ATOM 1829 CA PHE A1065 37.897 7.260 -41.627 1.00 63.98 C ANISOU 1829 CA PHE A1065 6148 11033 7129 -1463 778 -853 C ATOM 1830 C PHE A1065 37.286 6.157 -42.481 1.00 65.06 C ANISOU 1830 C PHE A1065 6291 11138 7292 -1687 824 -938 C ATOM 1831 O PHE A1065 38.001 5.464 -43.214 1.00 68.75 O ANISOU 1831 O PHE A1065 6900 11545 7677 -1766 882 -1027 O ATOM 1832 CB PHE A1065 37.951 6.827 -40.163 1.00 61.61 C ANISOU 1832 CB PHE A1065 5896 10641 6872 -1289 942 -799 C ATOM 1833 CG PHE A1065 38.903 7.626 -39.332 1.00 62.42 C ANISOU 1833 CG PHE A1065 6089 10714 6915 -1076 863 -749 C ATOM 1834 CD1 PHE A1065 40.270 7.424 -39.431 1.00 61.17 C ANISOU 1834 CD1 PHE A1065 5994 10506 6744 -1037 838 -768 C ATOM 1835 CD2 PHE A1065 38.432 8.575 -38.445 1.00 80.18 C ANISOU 1835 CD2 PHE A1065 8350 12980 9135 -906 801 -700 C ATOM 1836 CE1 PHE A1065 41.147 8.160 -38.663 1.00 61.93 C ANISOU 1836 CE1 PHE A1065 6141 10566 6822 -880 699 -722 C ATOM 1837 CE2 PHE A1065 39.303 9.311 -37.675 1.00 66.56 C ANISOU 1837 CE2 PHE A1065 6764 11186 7338 -733 666 -670 C ATOM 1838 CZ PHE A1065 40.662 9.105 -37.782 1.00 62.78 C ANISOU 1838 CZ PHE A1065 6327 10654 6871 -743 589 -672 C ATOM 1839 N ASP A1066 35.965 5.973 -42.384 1.00 64.26 N ANISOU 1839 N ASP A1066 6027 11071 7317 -1789 799 -925 N ATOM 1840 CA ASP A1066 35.264 5.001 -43.219 1.00 79.85 C ANISOU 1840 CA ASP A1066 7998 12997 9344 -2056 757 -1006 C ATOM 1841 C ASP A1066 35.673 5.143 -44.680 1.00 77.39 C ANISOU 1841 C ASP A1066 7854 12700 8851 -2181 572 -1104 C ATOM 1842 O ASP A1066 36.225 4.213 -45.280 1.00 82.57 O ANISOU 1842 O ASP A1066 8734 13239 9401 -2275 652 -1215 O ATOM 1843 CB ASP A1066 33.750 5.177 -43.076 1.00 71.47 C ANISOU 1843 CB ASP A1066 6621 12043 8492 -2160 668 -969 C ATOM 1844 CG ASP A1066 33.271 5.011 -41.653 1.00 81.07 C ANISOU 1844 CG ASP A1066 7683 13273 9846 -2057 938 -870 C ATOM 1845 OD1 ASP A1066 33.865 4.199 -40.913 1.00 98.94 O ANISOU 1845 OD1 ASP A1066 10153 15384 12054 -2033 1169 -835 O ATOM 1846 OD2 ASP A1066 32.298 5.695 -41.274 1.00 97.19 O ANISOU 1846 OD2 ASP A1066 9418 15474 12037 -1980 924 -828 O ATOM 1847 N ILE A1067 35.403 6.315 -45.258 1.00 73.53 N ANISOU 1847 N ILE A1067 7308 12335 8297 -2166 329 -1065 N ATOM 1848 CA ILE A1067 35.846 6.701 -46.594 1.00 89.57 C ANISOU 1848 CA ILE A1067 9564 14389 10078 -2278 162 -1112 C ATOM 1849 C ILE A1067 37.285 6.261 -46.817 1.00 83.28 C ANISOU 1849 C ILE A1067 8989 13548 9107 -2243 416 -1172 C ATOM 1850 O ILE A1067 37.580 5.508 -47.752 1.00 71.17 O ANISOU 1850 O ILE A1067 7681 11960 7402 -2369 472 -1302 O ATOM 1851 CB ILE A1067 35.723 8.224 -46.791 1.00 67.27 C ANISOU 1851 CB ILE A1067 6713 11654 7194 -2190 -87 -999 C ATOM 1852 CG1 ILE A1067 34.305 8.706 -46.482 1.00 67.42 C ANISOU 1852 CG1 ILE A1067 6447 11729 7439 -2130 -331 -960 C ATOM 1853 CG2 ILE A1067 36.143 8.618 -48.200 1.00 68.89 C ANISOU 1853 CG2 ILE A1067 7222 11868 7085 -2351 -247 -1009 C ATOM 1854 CD1 ILE A1067 34.164 10.211 -46.555 1.00 67.08 C ANISOU 1854 CD1 ILE A1067 6413 11713 7361 -1971 -603 -860 C ATOM 1855 N LEU A1068 38.183 6.740 -45.950 1.00 74.43 N ANISOU 1855 N LEU A1068 7795 12450 8037 -2055 560 -1093 N ATOM 1856 CA LEU A1068 39.604 6.426 -46.052 1.00 66.88 C ANISOU 1856 CA LEU A1068 6926 11487 6997 -1986 789 -1141 C ATOM 1857 C LEU A1068 39.834 4.924 -46.177 1.00 69.93 C ANISOU 1857 C LEU A1068 7434 11742 7396 -1980 985 -1297 C ATOM 1858 O LEU A1068 40.457 4.455 -47.136 1.00 69.28 O ANISOU 1858 O LEU A1068 7524 11659 7142 -2027 1113 -1427 O ATOM 1859 CB LEU A1068 40.338 6.991 -44.834 1.00 63.23 C ANISOU 1859 CB LEU A1068 6320 11033 6672 -1782 835 -1037 C ATOM 1860 CG LEU A1068 41.863 6.989 -44.894 1.00 63.05 C ANISOU 1860 CG LEU A1068 6268 11053 6636 -1709 1001 -1056 C ATOM 1861 CD1 LEU A1068 42.347 7.987 -45.932 1.00 70.67 C ANISOU 1861 CD1 LEU A1068 7276 12151 7425 -1882 968 -1001 C ATOM 1862 CD2 LEU A1068 42.451 7.297 -43.529 1.00 61.79 C ANISOU 1862 CD2 LEU A1068 5982 10850 6646 -1504 964 -973 C ATOM 1863 N VAL A1069 39.314 4.153 -45.214 1.00 69.45 N ANISOU 1863 N VAL A1069 7324 11546 7516 -1921 1023 -1286 N ATOM 1864 CA VAL A1069 39.443 2.695 -45.246 1.00 69.52 C ANISOU 1864 CA VAL A1069 7510 11351 7552 -1923 1162 -1416 C ATOM 1865 C VAL A1069 38.969 2.143 -46.584 1.00 73.57 C ANISOU 1865 C VAL A1069 8241 11812 7902 -2144 1084 -1576 C ATOM 1866 O VAL A1069 39.656 1.337 -47.223 1.00 99.54 O ANISOU 1866 O VAL A1069 11762 14993 11066 -2100 1222 -1749 O ATOM 1867 CB VAL A1069 38.668 2.059 -44.078 1.00 72.61 C ANISOU 1867 CB VAL A1069 7862 11594 8135 -1926 1184 -1328 C ATOM 1868 CG1 VAL A1069 38.676 0.538 -44.207 1.00 78.44 C ANISOU 1868 CG1 VAL A1069 8857 12052 8894 -1986 1271 -1449 C ATOM 1869 CG2 VAL A1069 39.259 2.491 -42.750 1.00 74.28 C ANISOU 1869 CG2 VAL A1069 7979 11818 8426 -1678 1255 -1195 C ATOM 1870 N GLY A1070 37.785 2.568 -47.023 1.00 74.84 N ANISOU 1870 N GLY A1070 8338 12037 8059 -2361 840 -1537 N ATOM 1871 CA GLY A1070 37.261 2.177 -48.318 1.00 80.99 C ANISOU 1871 CA GLY A1070 9353 12764 8655 -2592 664 -1681 C ATOM 1872 C GLY A1070 38.256 2.376 -49.443 1.00 79.64 C ANISOU 1872 C GLY A1070 9456 12658 8146 -2555 771 -1799 C ATOM 1873 O GLY A1070 38.572 1.429 -50.171 1.00 80.75 O ANISOU 1873 O GLY A1070 9916 12655 8110 -2584 864 -2002 O ATOM 1874 N GLN A1071 38.765 3.605 -49.578 1.00 76.41 N ANISOU 1874 N GLN A1071 8947 12452 7633 -2496 780 -1674 N ATOM 1875 CA GLN A1071 39.818 3.887 -50.549 1.00 76.55 C ANISOU 1875 CA GLN A1071 9180 12573 7334 -2485 975 -1742 C ATOM 1876 C GLN A1071 40.984 2.916 -50.400 1.00 76.73 C ANISOU 1876 C GLN A1071 9251 12528 7375 -2280 1354 -1904 C ATOM 1877 O GLN A1071 41.428 2.306 -51.380 1.00 79.18 O ANISOU 1877 O GLN A1071 9865 12803 7417 -2286 1528 -2103 O ATOM 1878 CB GLN A1071 40.308 5.327 -50.387 1.00 77.59 C ANISOU 1878 CB GLN A1071 9141 12894 7444 -2466 962 -1536 C ATOM 1879 CG GLN A1071 39.219 6.385 -50.408 1.00100.93 C ANISOU 1879 CG GLN A1071 12040 15886 10422 -2579 566 -1373 C ATOM 1880 CD GLN A1071 39.774 7.779 -50.191 1.00 89.83 C ANISOU 1880 CD GLN A1071 10539 14592 8999 -2554 537 -1176 C ATOM 1881 OE1 GLN A1071 39.063 8.685 -49.757 1.00 83.99 O ANISOU 1881 OE1 GLN A1071 9682 13848 8383 -2526 252 -1039 O ATOM 1882 NE2 GLN A1071 41.054 7.957 -50.495 1.00100.01 N ANISOU 1882 NE2 GLN A1071 11871 15974 10153 -2563 834 -1167 N ATOM 1883 N ILE A1072 41.490 2.762 -49.170 1.00 84.67 N ANISOU 1883 N ILE A1072 9983 13504 8685 -2065 1469 -1833 N ATOM 1884 CA ILE A1072 42.610 1.854 -48.909 1.00 80.81 C ANISOU 1884 CA ILE A1072 9492 12933 8280 -1805 1766 -1978 C ATOM 1885 C ILE A1072 42.306 0.461 -49.448 1.00 78.69 C ANISOU 1885 C ILE A1072 9582 12404 7913 -1804 1803 -2221 C ATOM 1886 O ILE A1072 43.131 -0.152 -50.135 1.00 80.94 O ANISOU 1886 O ILE A1072 10049 12661 8045 -1655 2059 -2435 O ATOM 1887 CB ILE A1072 42.930 1.809 -47.403 1.00 72.79 C ANISOU 1887 CB ILE A1072 8205 11855 7599 -1590 1751 -1848 C ATOM 1888 CG1 ILE A1072 43.353 3.187 -46.892 1.00 69.74 C ANISOU 1888 CG1 ILE A1072 7520 11687 7291 -1583 1690 -1643 C ATOM 1889 CG2 ILE A1072 44.018 0.778 -47.120 1.00 74.72 C ANISOU 1889 CG2 ILE A1072 8460 11968 7963 -1280 1974 -2001 C ATOM 1890 CD1 ILE A1072 43.669 3.205 -45.416 1.00 72.22 C ANISOU 1890 CD1 ILE A1072 7639 11928 7871 -1372 1625 -1526 C ATOM 1891 N ASP A1073 41.111 -0.056 -49.139 1.00 79.91 N ANISOU 1891 N ASP A1073 9838 12358 8166 -1976 1555 -2198 N ATOM 1892 CA ASP A1073 40.691 -1.357 -49.655 1.00 93.19 C ANISOU 1892 CA ASP A1073 11906 13737 9767 -2053 1510 -2417 C ATOM 1893 C ASP A1073 40.828 -1.422 -51.172 1.00 89.65 C ANISOU 1893 C ASP A1073 11824 13324 8914 -2148 1545 -2636 C ATOM 1894 O ASP A1073 41.506 -2.306 -51.708 1.00 88.99 O ANISOU 1894 O ASP A1073 12049 13086 8676 -1975 1758 -2890 O ATOM 1895 CB ASP A1073 39.248 -1.647 -49.236 1.00 96.66 C ANISOU 1895 CB ASP A1073 12325 14022 10378 -2344 1203 -2317 C ATOM 1896 CG ASP A1073 39.097 -1.826 -47.740 1.00 94.50 C ANISOU 1896 CG ASP A1073 11808 13664 10434 -2254 1242 -2125 C ATOM 1897 OD1 ASP A1073 40.016 -2.391 -47.109 1.00107.52 O ANISOU 1897 OD1 ASP A1073 13509 15176 12169 -1973 1431 -2154 O ATOM 1898 OD2 ASP A1073 38.058 -1.397 -47.195 1.00 99.51 O ANISOU 1898 OD2 ASP A1073 12209 14371 11230 -2447 1083 -1948 O ATOM 1899 N ASP A1074 40.191 -0.483 -51.880 1.00 85.51 N ANISOU 1899 N ASP A1074 11314 12986 8189 -2397 1330 -2545 N ATOM 1900 CA ASP A1074 40.311 -0.432 -53.336 1.00 87.78 C ANISOU 1900 CA ASP A1074 12028 13317 8009 -2506 1345 -2722 C ATOM 1901 C ASP A1074 41.768 -0.348 -53.773 1.00 88.09 C ANISOU 1901 C ASP A1074 12115 13517 7839 -2252 1830 -2835 C ATOM 1902 O ASP A1074 42.167 -0.988 -54.752 1.00 92.42 O ANISOU 1902 O ASP A1074 13090 13986 8039 -2193 2024 -3102 O ATOM 1903 CB ASP A1074 39.526 0.757 -53.891 1.00 90.75 C ANISOU 1903 CB ASP A1074 12386 13879 8215 -2769 1014 -2543 C ATOM 1904 CG ASP A1074 38.034 0.508 -53.924 1.00111.20 C ANISOU 1904 CG ASP A1074 15005 16314 10932 -3040 513 -2525 C ATOM 1905 OD1 ASP A1074 37.539 -0.284 -53.094 1.00121.77 O ANISOU 1905 OD1 ASP A1074 16183 17466 12618 -3058 451 -2532 O ATOM 1906 OD2 ASP A1074 37.358 1.096 -54.796 1.00116.10 O ANISOU 1906 OD2 ASP A1074 15809 16996 11309 -3248 170 -2495 O ATOM 1907 N ALA A1075 42.578 0.438 -53.057 1.00 93.95 N ANISOU 1907 N ALA A1075 12413 14489 8794 -2101 2037 -2647 N ATOM 1908 CA ALA A1075 43.999 0.531 -53.378 1.00 85.86 C ANISOU 1908 CA ALA A1075 11295 13657 7669 -1877 2516 -2735 C ATOM 1909 C ALA A1075 44.669 -0.836 -53.295 1.00 91.18 C ANISOU 1909 C ALA A1075 12096 14122 8426 -1540 2782 -3030 C ATOM 1910 O ALA A1075 45.314 -1.279 -54.253 1.00 91.98 O ANISOU 1910 O ALA A1075 12476 14254 8219 -1413 3120 -3282 O ATOM 1911 CB ALA A1075 44.686 1.537 -52.453 1.00 88.20 C ANISOU 1911 CB ALA A1075 11048 14188 8277 -1804 2593 -2475 C ATOM 1912 N LEU A1076 44.508 -1.533 -52.167 1.00 90.70 N ANISOU 1912 N LEU A1076 11884 13822 8754 -1376 2639 -3007 N ATOM 1913 CA LEU A1076 45.088 -2.865 -52.019 1.00103.04 C ANISOU 1913 CA LEU A1076 13623 15107 10421 -1028 2815 -3273 C ATOM 1914 C LEU A1076 44.354 -3.926 -52.833 1.00 94.94 C ANISOU 1914 C LEU A1076 13218 13731 9121 -1134 2681 -3544 C ATOM 1915 O LEU A1076 44.776 -5.087 -52.821 1.00 98.37 O ANISOU 1915 O LEU A1076 13911 13865 9601 -842 2799 -3799 O ATOM 1916 CB LEU A1076 45.148 -3.268 -50.537 1.00103.06 C ANISOU 1916 CB LEU A1076 13357 14919 10881 -837 2665 -3130 C ATOM 1917 CG LEU A1076 43.907 -3.212 -49.644 1.00 97.27 C ANISOU 1917 CG LEU A1076 12608 14019 10331 -1108 2279 -2896 C ATOM 1918 CD1 LEU A1076 43.059 -4.471 -49.768 1.00123.04 C ANISOU 1918 CD1 LEU A1076 16338 16844 13568 -1226 2091 -3046 C ATOM 1919 CD2 LEU A1076 44.321 -2.982 -48.202 1.00 87.47 C ANISOU 1919 CD2 LEU A1076 10995 12793 9448 -910 2238 -2676 C ATOM 1920 N LYS A1077 43.274 -3.562 -53.534 1.00 97.23 N ANISOU 1920 N LYS A1077 13774 14025 9143 -1533 2389 -3503 N ATOM 1921 CA LYS A1077 42.755 -4.425 -54.591 1.00 99.01 C ANISOU 1921 CA LYS A1077 14642 13969 9008 -1652 2269 -3801 C ATOM 1922 C LYS A1077 43.636 -4.336 -55.831 1.00101.61 C ANISOU 1922 C LYS A1077 15281 14474 8851 -1493 2678 -4052 C ATOM 1923 O LYS A1077 44.038 -5.362 -56.390 1.00105.73 O ANISOU 1923 O LYS A1077 16252 14751 9169 -1257 2868 -4404 O ATOM 1924 CB LYS A1077 41.310 -4.060 -54.933 1.00 98.58 C ANISOU 1924 CB LYS A1077 14736 13866 8852 -2128 1757 -3677 C ATOM 1925 N LEU A1078 43.959 -3.110 -56.260 1.00107.12 N ANISOU 1925 N LEU A1078 15771 15584 9346 -1614 2842 -3871 N ATOM 1926 CA LEU A1078 44.918 -2.922 -57.346 1.00102.56 C ANISOU 1926 CA LEU A1078 15417 15239 8311 -1479 3345 -4056 C ATOM 1927 C LEU A1078 46.266 -3.543 -57.003 1.00104.31 C ANISOU 1927 C LEU A1078 15370 15506 8756 -977 3880 -4252 C ATOM 1928 O LEU A1078 46.882 -4.207 -57.843 1.00109.63 O ANISOU 1928 O LEU A1078 16416 16139 9100 -725 4272 -4598 O ATOM 1929 CB LEU A1078 45.082 -1.434 -57.655 1.00100.34 C ANISOU 1929 CB LEU A1078 14892 15374 7857 -1732 3428 -3749 C ATOM 1930 CG LEU A1078 43.831 -0.669 -58.081 1.00 99.14 C ANISOU 1930 CG LEU A1078 14992 15205 7470 -2173 2888 -3545 C ATOM 1931 CD1 LEU A1078 44.137 0.812 -58.229 1.00 97.24 C ANISOU 1931 CD1 LEU A1078 14500 15323 7122 -2368 2978 -3217 C ATOM 1932 CD2 LEU A1078 43.287 -1.239 -59.378 1.00103.52 C ANISOU 1932 CD2 LEU A1078 16344 15563 7424 -2313 2745 -3819 C ATOM 1933 N ALA A1079 46.741 -3.333 -55.770 1.00113.06 N ANISOU 1933 N ALA A1079 15840 16696 10420 -800 3887 -4050 N ATOM 1934 CA ALA A1079 47.982 -3.967 -55.334 1.00113.82 C ANISOU 1934 CA ALA A1079 15624 16807 10816 -287 4287 -4228 C ATOM 1935 C ALA A1079 47.876 -5.485 -55.373 1.00116.13 C ANISOU 1935 C ALA A1079 16395 16614 11115 29 4231 -4586 C ATOM 1936 O ALA A1079 48.859 -6.168 -55.682 1.00111.61 O ANISOU 1936 O ALA A1079 15853 16022 10532 489 4650 -4895 O ATOM 1937 CB ALA A1079 48.356 -3.491 -53.931 1.00112.09 C ANISOU 1937 CB ALA A1079 14715 16696 11179 -189 4151 -3930 C ATOM 1938 N ASN A1080 46.696 -6.032 -55.066 1.00134.53 N ANISOU 1938 N ASN A1080 19093 18540 13483 -211 3723 -4554 N ATOM 1939 CA ASN A1080 46.464 -7.464 -55.210 1.00115.14 C ANISOU 1939 CA ASN A1080 17214 15550 10983 -11 3605 -4885 C ATOM 1940 C ASN A1080 46.370 -7.892 -56.667 1.00116.57 C ANISOU 1940 C ASN A1080 18101 15633 10558 -33 3763 -5260 C ATOM 1941 O ASN A1080 46.664 -9.051 -56.978 1.00127.68 O ANISOU 1941 O ASN A1080 19983 16658 11869 306 3864 -5637 O ATOM 1942 CB ASN A1080 45.191 -7.876 -54.468 1.00109.86 C ANISOU 1942 CB ASN A1080 16706 14492 10542 -357 3026 -4705 C ATOM 1943 N GLU A1081 45.972 -6.986 -57.565 1.00114.43 N ANISOU 1943 N GLU A1081 17970 15662 9847 -405 3762 -5173 N ATOM 1944 CA GLU A1081 45.938 -7.303 -58.988 1.00120.19 C ANISOU 1944 CA GLU A1081 19433 16326 9909 -426 3926 -5521 C ATOM 1945 C GLU A1081 47.323 -7.247 -59.617 1.00131.19 C ANISOU 1945 C GLU A1081 20747 18039 11059 12 4691 -5760 C ATOM 1946 O GLU A1081 47.570 -7.929 -60.618 1.00148.95 O ANISOU 1946 O GLU A1081 23550 20135 12908 256 4848 -6068 O ATOM 1947 CB GLU A1081 44.997 -6.348 -59.722 1.00118.83 C ANISOU 1947 CB GLU A1081 19492 16335 9322 -978 3598 -5319 C ATOM 1948 N GLY A1082 48.233 -6.448 -59.057 1.00122.91 N ANISOU 1948 N GLY A1082 18915 17437 10348 153 5059 -5521 N ATOM 1949 CA GLY A1082 49.587 -6.307 -59.566 1.00134.46 C ANISOU 1949 CA GLY A1082 20062 19254 11772 573 5686 -5574 C ATOM 1950 C GLY A1082 49.926 -4.896 -60.006 1.00140.52 C ANISOU 1950 C GLY A1082 20459 20543 12390 273 5895 -5183 C ATOM 1951 O GLY A1082 51.100 -4.512 -59.984 1.00147.64 O ANISOU 1951 O GLY A1082 20793 21798 13505 531 6357 -5064 O ATOM 1952 N LYS A1083 48.919 -4.116 -60.400 1.00133.99 N ANISOU 1952 N LYS A1083 19949 19739 11221 -275 5529 -4969 N ATOM 1953 CA LYS A1083 49.142 -2.756 -60.877 1.00123.91 C ANISOU 1953 CA LYS A1083 18456 18865 9759 -594 5662 -4588 C ATOM 1954 C LYS A1083 49.591 -1.847 -59.742 1.00118.48 C ANISOU 1954 C LYS A1083 16921 18463 9632 -690 5701 -4259 C ATOM 1955 O LYS A1083 48.771 -1.163 -59.120 1.00118.22 O ANISOU 1955 O LYS A1083 16767 18438 9712 -1068 5285 -4039 O ATOM 1956 CB LYS A1083 47.873 -2.203 -61.530 1.00126.32 C ANISOU 1956 CB LYS A1083 19353 19058 9584 -1110 5157 -4458 C ATOM 1957 N VAL A1084 50.898 -1.831 -59.471 1.00121.14 N ANISOU 1957 N VAL A1084 16658 19041 10328 -338 6168 -4226 N ATOM 1958 CA VAL A1084 51.418 -1.006 -58.387 1.00116.84 C ANISOU 1958 CA VAL A1084 15302 18743 10350 -412 6152 -3923 C ATOM 1959 C VAL A1084 51.448 0.460 -58.798 1.00124.04 C ANISOU 1959 C VAL A1084 16102 19938 11089 -877 6156 -3512 C ATOM 1960 O VAL A1084 51.166 1.350 -57.987 1.00116.74 O ANISOU 1960 O VAL A1084 14816 19101 10440 -1164 5858 -3231 O ATOM 1961 CB VAL A1084 52.808 -1.507 -57.951 1.00120.70 C ANISOU 1961 CB VAL A1084 15169 19368 11325 116 6567 -4024 C ATOM 1962 N LYS A1085 51.788 0.738 -60.061 1.00122.04 N ANISOU 1962 N LYS A1085 16199 19813 10357 -949 6487 -3472 N ATOM 1963 CA LYS A1085 51.844 2.120 -60.530 1.00122.33 C ANISOU 1963 CA LYS A1085 16218 20067 10194 -1400 6505 -3082 C ATOM 1964 C LYS A1085 50.469 2.778 -60.518 1.00123.36 C ANISOU 1964 C LYS A1085 16785 20039 10046 -1861 5911 -2923 C ATOM 1965 O LYS A1085 50.370 3.996 -60.331 1.00130.13 O ANISOU 1965 O LYS A1085 17470 21020 10952 -2229 5745 -2573 O ATOM 1966 CB LYS A1085 52.450 2.180 -61.932 1.00130.68 C ANISOU 1966 CB LYS A1085 17640 21279 10734 -1364 6999 -3093 C ATOM 1967 N GLU A1086 49.404 1.998 -60.717 1.00115.87 N ANISOU 1967 N GLU A1086 16402 18805 8817 -1848 5560 -3176 N ATOM 1968 CA GLU A1086 48.052 2.541 -60.641 1.00111.38 C ANISOU 1968 CA GLU A1086 16184 18096 8040 -2250 4945 -3041 C ATOM 1969 C GLU A1086 47.558 2.637 -59.203 1.00104.17 C ANISOU 1969 C GLU A1086 14778 17162 7638 -2294 4593 -2979 C ATOM 1970 O GLU A1086 46.745 3.514 -58.890 1.00108.74 O ANISOU 1970 O GLU A1086 15337 17705 8273 -2580 4101 -2696 O ATOM 1971 CB GLU A1086 47.093 1.688 -61.470 1.00113.88 C ANISOU 1971 CB GLU A1086 17291 18108 7870 -2260 4648 -3323 C ATOM 1972 N ALA A1087 48.038 1.756 -58.320 1.00102.93 N ANISOU 1972 N ALA A1087 14210 16936 7962 -1921 4729 -3167 N ATOM 1973 CA ALA A1087 47.610 1.794 -56.926 1.00100.95 C ANISOU 1973 CA ALA A1087 13495 16534 8325 -1850 4278 -3000 C ATOM 1974 C ALA A1087 48.263 2.949 -56.177 1.00105.16 C ANISOU 1974 C ALA A1087 13403 17334 9221 -1948 4330 -2670 C ATOM 1975 O ALA A1087 47.597 3.650 -55.405 1.00 91.08 O ANISOU 1975 O ALA A1087 11446 15479 7681 -2106 3867 -2411 O ATOM 1976 CB ALA A1087 47.920 0.463 -56.243 1.00101.03 C ANISOU 1976 CB ALA A1087 13367 16320 8701 -1415 4350 -3275 C ATOM 1977 N GLN A1088 49.564 3.163 -56.388 1.00107.94 N ANISOU 1977 N GLN A1088 13399 17990 9625 -1857 4890 -2687 N ATOM 1978 CA GLN A1088 50.251 4.284 -55.755 1.00 99.58 C ANISOU 1978 CA GLN A1088 11756 17169 8911 -2010 4918 -2373 C ATOM 1979 C GLN A1088 49.692 5.628 -56.205 1.00 98.14 C ANISOU 1979 C GLN A1088 11828 17048 8413 -2493 4681 -2045 C ATOM 1980 O GLN A1088 49.814 6.613 -55.470 1.00108.45 O ANISOU 1980 O GLN A1088 12777 18404 10026 -2656 4447 -1759 O ATOM 1981 CB GLN A1088 51.751 4.216 -56.043 1.00108.72 C ANISOU 1981 CB GLN A1088 12502 18508 10299 -1785 5426 -2369 C ATOM 1982 N ALA A1089 49.082 5.690 -57.392 1.00 97.96 N ANISOU 1982 N ALA A1089 12467 16956 7797 -2692 4662 -2071 N ATOM 1983 CA ALA A1089 48.463 6.932 -57.843 1.00 97.36 C ANISOU 1983 CA ALA A1089 12717 16894 7381 -3129 4368 -1763 C ATOM 1984 C ALA A1089 47.206 7.244 -57.039 1.00 99.07 C ANISOU 1984 C ALA A1089 12950 16845 7848 -3152 3628 -1628 C ATOM 1985 O ALA A1089 46.920 8.413 -56.753 1.00109.05 O ANISOU 1985 O ALA A1089 14158 18093 9182 -3378 3307 -1324 O ATOM 1986 CB ALA A1089 48.147 6.855 -59.335 1.00102.47 C ANISOU 1986 CB ALA A1089 14107 17457 7372 -3260 4440 -1812 C ATOM 1987 N ALA A1090 46.441 6.213 -56.669 1.00 92.37 N ANISOU 1987 N ALA A1090 12183 15772 7141 -2920 3364 -1851 N ATOM 1988 CA ALA A1090 45.281 6.411 -55.805 1.00 87.69 C ANISOU 1988 CA ALA A1090 11498 14967 6851 -2915 2752 -1738 C ATOM 1989 C ALA A1090 45.688 6.642 -54.356 1.00 97.41 C ANISOU 1989 C ALA A1090 12121 16215 8674 -2741 2697 -1620 C ATOM 1990 O ALA A1090 45.042 7.427 -53.653 1.00 94.75 O ANISOU 1990 O ALA A1090 11655 15803 8543 -2808 2290 -1415 O ATOM 1991 CB ALA A1090 44.332 5.219 -55.906 1.00 98.36 C ANISOU 1991 CB ALA A1090 13130 16075 8166 -2798 2514 -1993 C ATOM 1992 N ALA A1091 46.748 5.971 -53.894 1.00 90.39 N ANISOU 1992 N ALA A1091 10880 15413 8052 -2488 3080 -1760 N ATOM 1993 CA ALA A1091 47.304 6.260 -52.578 1.00 91.53 C ANISOU 1993 CA ALA A1091 10481 15586 8710 -2335 3012 -1638 C ATOM 1994 C ALA A1091 47.853 7.678 -52.487 1.00 86.78 C ANISOU 1994 C ALA A1091 9662 15153 8156 -2589 2996 -1350 C ATOM 1995 O ALA A1091 47.920 8.232 -51.385 1.00 82.77 O ANISOU 1995 O ALA A1091 8843 14599 8005 -2546 2735 -1199 O ATOM 1996 CB ALA A1091 48.397 5.250 -52.231 1.00108.30 C ANISOU 1996 CB ALA A1091 12282 17767 11100 -1994 3389 -1854 C ATOM 1997 N GLU A1092 48.250 8.272 -53.616 1.00 99.07 N ANISOU 1997 N GLU A1092 11429 16879 9333 -2870 3265 -1268 N ATOM 1998 CA GLU A1092 48.672 9.666 -53.655 1.00112.54 C ANISOU 1998 CA GLU A1092 13037 18690 11032 -3197 3219 -961 C ATOM 1999 C GLU A1092 47.512 10.634 -53.481 1.00128.49 C ANISOU 1999 C GLU A1092 15362 20499 12959 -3365 2639 -746 C ATOM 2000 O GLU A1092 47.755 11.833 -53.299 1.00151.61 O ANISOU 2000 O GLU A1092 18240 23424 15941 -3601 2485 -485 O ATOM 2001 CB GLU A1092 49.398 9.963 -54.971 1.00 97.47 C ANISOU 2001 CB GLU A1092 11337 17011 8688 -3482 3723 -915 C ATOM 2002 N GLN A1093 46.266 10.149 -53.540 1.00 89.44 N ANISOU 2002 N GLN A1093 10715 15368 7901 -3248 2304 -855 N ATOM 2003 CA GLN A1093 45.081 10.964 -53.289 1.00 85.52 C ANISOU 2003 CA GLN A1093 10415 14682 7397 -3315 1741 -693 C ATOM 2004 C GLN A1093 44.279 10.455 -52.095 1.00 85.71 C ANISOU 2004 C GLN A1093 10196 14560 7807 -3029 1446 -786 C ATOM 2005 O GLN A1093 43.150 10.904 -51.873 1.00 78.20 O ANISOU 2005 O GLN A1093 9356 13473 6886 -3015 1017 -714 O ATOM 2006 CB GLN A1093 44.195 11.039 -54.535 1.00 82.76 C ANISOU 2006 CB GLN A1093 10632 14261 6553 -3490 1548 -693 C ATOM 2007 N LEU A1094 44.832 9.512 -51.328 1.00101.21 N ANISOU 2007 N LEU A1094 11839 16551 10066 -2790 1676 -943 N ATOM 2008 CA LEU A1094 44.410 9.360 -49.942 1.00 78.10 C ANISOU 2008 CA LEU A1094 8648 13503 7522 -2561 1446 -939 C ATOM 2009 C LEU A1094 44.662 10.636 -49.153 1.00 87.36 C ANISOU 2009 C LEU A1094 9659 14660 8876 -2602 1224 -723 C ATOM 2010 O LEU A1094 44.027 10.847 -48.113 1.00102.54 O ANISOU 2010 O LEU A1094 11492 16462 11009 -2443 956 -688 O ATOM 2011 CB LEU A1094 45.145 8.195 -49.276 1.00 70.50 C ANISOU 2011 CB LEU A1094 7430 12546 6810 -2302 1713 -1110 C ATOM 2012 CG LEU A1094 44.796 6.755 -49.657 1.00 71.37 C ANISOU 2012 CG LEU A1094 7712 12565 6841 -2176 1860 -1353 C ATOM 2013 CD1 LEU A1094 45.904 5.805 -49.236 1.00 72.15 C ANISOU 2013 CD1 LEU A1094 7582 12681 7151 -1913 2171 -1506 C ATOM 2014 CD2 LEU A1094 43.487 6.341 -49.013 1.00 69.98 C ANISOU 2014 CD2 LEU A1094 7605 12200 6783 -2121 1555 -1363 C ATOM 2015 N LYS A1095 45.570 11.489 -49.640 1.00 80.91 N ANISOU 2015 N LYS A1095 8830 13949 7965 -2829 1346 -580 N ATOM 2016 CA LYS A1095 45.912 12.720 -48.937 1.00 83.53 C ANISOU 2016 CA LYS A1095 9050 14219 8467 -2916 1108 -379 C ATOM 2017 C LYS A1095 44.714 13.652 -48.828 1.00 76.47 C ANISOU 2017 C LYS A1095 8434 13134 7486 -2928 653 -260 C ATOM 2018 O LYS A1095 44.561 14.352 -47.821 1.00 90.45 O ANISOU 2018 O LYS A1095 10134 14773 9460 -2818 374 -186 O ATOM 2019 CB LYS A1095 47.071 13.423 -49.646 1.00 83.40 C ANISOU 2019 CB LYS A1095 8992 14345 8351 -3246 1346 -228 C ATOM 2020 N THR A1096 43.864 13.692 -49.860 1.00 75.85 N ANISOU 2020 N THR A1096 8692 13028 7101 -3035 547 -252 N ATOM 2021 CA THR A1096 42.699 14.573 -49.825 1.00 79.90 C ANISOU 2021 CA THR A1096 9433 13363 7565 -2997 80 -151 C ATOM 2022 C THR A1096 41.790 14.226 -48.651 1.00 83.65 C ANISOU 2022 C THR A1096 9688 13759 8335 -2665 -103 -262 C ATOM 2023 O THR A1096 41.387 15.104 -47.879 1.00 68.55 O ANISOU 2023 O THR A1096 7769 11711 6566 -2529 -391 -187 O ATOM 2024 CB THR A1096 41.935 14.489 -51.148 1.00 76.41 C ANISOU 2024 CB THR A1096 9366 12909 6755 -3141 -45 -149 C ATOM 2025 N THR A1097 41.474 12.939 -48.490 1.00102.34 N ANISOU 2025 N THR A1097 11905 16196 10783 -2535 84 -444 N ATOM 2026 CA THR A1097 40.698 12.499 -47.334 1.00 71.44 C ANISOU 2026 CA THR A1097 7779 12228 7137 -2268 7 -529 C ATOM 2027 C THR A1097 41.465 12.728 -46.038 1.00 76.54 C ANISOU 2027 C THR A1097 8240 12841 8002 -2110 73 -500 C ATOM 2028 O THR A1097 40.874 13.086 -45.012 1.00 89.96 O ANISOU 2028 O THR A1097 9879 14455 9847 -1903 -86 -492 O ATOM 2029 CB THR A1097 40.334 11.023 -47.488 1.00 71.80 C ANISOU 2029 CB THR A1097 7757 12315 7208 -2235 207 -703 C ATOM 2030 OG1 THR A1097 39.663 10.830 -48.738 1.00 99.77 O ANISOU 2030 OG1 THR A1097 11520 15869 10520 -2406 85 -744 O ATOM 2031 CG2 THR A1097 39.427 10.569 -46.354 1.00 69.72 C ANISOU 2031 CG2 THR A1097 7298 11999 7196 -2026 160 -753 C ATOM 2032 N ARG A1098 42.787 12.535 -46.074 1.00 70.37 N ANISOU 2032 N ARG A1098 7367 12132 7240 -2196 300 -493 N ATOM 2033 CA ARG A1098 43.614 12.723 -44.887 1.00 68.58 C ANISOU 2033 CA ARG A1098 6964 11867 7228 -2064 291 -469 C ATOM 2034 C ARG A1098 43.598 14.171 -44.413 1.00 82.74 C ANISOU 2034 C ARG A1098 8869 13527 9042 -2091 -34 -329 C ATOM 2035 O ARG A1098 43.731 14.434 -43.212 1.00 76.34 O ANISOU 2035 O ARG A1098 8016 12614 8375 -1908 -172 -333 O ATOM 2036 CB ARG A1098 45.045 12.270 -45.181 1.00 69.56 C ANISOU 2036 CB ARG A1098 6893 12123 7414 -2163 570 -492 C ATOM 2037 CG ARG A1098 45.993 12.323 -43.991 1.00 68.18 C ANISOU 2037 CG ARG A1098 6493 11915 7497 -2025 508 -482 C ATOM 2038 CD ARG A1098 47.426 12.425 -44.475 1.00 86.76 C ANISOU 2038 CD ARG A1098 8592 14426 9948 -2210 701 -446 C ATOM 2039 NE ARG A1098 47.719 13.741 -45.036 1.00 77.56 N ANISOU 2039 NE ARG A1098 7513 13262 8694 -2544 583 -264 N ATOM 2040 CZ ARG A1098 48.839 14.042 -45.686 1.00 83.89 C ANISOU 2040 CZ ARG A1098 8113 14225 9538 -2821 793 -183 C ATOM 2041 NH1 ARG A1098 49.788 13.128 -45.853 1.00 93.24 N ANISOU 2041 NH1 ARG A1098 8942 15609 10876 -2747 1140 -298 N ATOM 2042 NH2 ARG A1098 49.017 15.271 -46.154 1.00 97.24 N ANISOU 2042 NH2 ARG A1098 9952 15868 11129 -3170 663 17 N ATOM 2043 N ASN A1099 43.424 15.120 -45.333 1.00101.26 N ANISOU 2043 N ASN A1099 11425 15834 11215 -2311 -186 -205 N ATOM 2044 CA ASN A1099 43.421 16.537 -44.994 1.00 76.50 C ANISOU 2044 CA ASN A1099 8474 12507 8085 -2354 -531 -67 C ATOM 2045 C ASN A1099 42.027 17.055 -44.660 1.00 94.72 C ANISOU 2045 C ASN A1099 10949 14664 10377 -2103 -830 -94 C ATOM 2046 O ASN A1099 41.862 17.808 -43.695 1.00106.45 O ANISOU 2046 O ASN A1099 12516 15977 11952 -1914 -1063 -92 O ATOM 2047 CB ASN A1099 44.008 17.355 -46.147 1.00 80.17 C ANISOU 2047 CB ASN A1099 9135 12962 8362 -2742 -555 115 C ATOM 2048 CG ASN A1099 45.412 16.915 -46.520 1.00 92.96 C ANISOU 2048 CG ASN A1099 10517 14778 10024 -2997 -195 141 C ATOM 2049 OD1 ASN A1099 46.170 16.438 -45.677 1.00 77.59 O ANISOU 2049 OD1 ASN A1099 8263 12898 8320 -2887 -87 65 O ATOM 2050 ND2 ASN A1099 45.763 17.072 -47.792 1.00100.55 N ANISOU 2050 ND2 ASN A1099 11621 15839 10743 -3323 -6 249 N ATOM 2051 N ALA A1100 41.017 16.660 -45.437 1.00 93.71 N ANISOU 2051 N ALA A1100 10864 14598 10143 -2080 -838 -136 N ATOM 2052 CA ALA A1100 39.689 17.245 -45.285 1.00 99.04 C ANISOU 2052 CA ALA A1100 11629 15156 10845 -1845 -1146 -154 C ATOM 2053 C ALA A1100 38.990 16.767 -44.018 1.00100.45 C ANISOU 2053 C ALA A1100 11584 15359 11225 -1495 -1062 -295 C ATOM 2054 O ALA A1100 38.111 17.464 -43.499 1.00100.56 O ANISOU 2054 O ALA A1100 11632 15265 11311 -1227 -1278 -323 O ATOM 2055 CB ALA A1100 38.836 16.927 -46.511 1.00 98.61 C ANISOU 2055 CB ALA A1100 11648 15171 10649 -1945 -1235 -157 C ATOM 2056 N TYR A1101 39.359 15.593 -43.508 1.00 88.37 N ANISOU 2056 N TYR A1101 9848 13956 9773 -1479 -738 -384 N ATOM 2057 CA TYR A1101 38.660 14.985 -42.381 1.00 75.69 C ANISOU 2057 CA TYR A1101 8074 12381 8305 -1205 -597 -489 C ATOM 2058 C TYR A1101 39.580 14.712 -41.201 1.00 71.85 C ANISOU 2058 C TYR A1101 7587 11850 7861 -1105 -460 -508 C ATOM 2059 O TYR A1101 39.365 15.266 -40.118 1.00 86.78 O ANISOU 2059 O TYR A1101 9568 13637 9769 -863 -547 -531 O ATOM 2060 CB TYR A1101 37.983 13.682 -42.829 1.00 71.52 C ANISOU 2060 CB TYR A1101 7358 11995 7821 -1278 -384 -568 C ATOM 2061 CG TYR A1101 36.874 13.854 -43.842 1.00 68.74 C ANISOU 2061 CG TYR A1101 6974 11685 7459 -1342 -587 -573 C ATOM 2062 CD1 TYR A1101 37.149 13.919 -45.202 1.00 78.12 C ANISOU 2062 CD1 TYR A1101 8327 12885 8469 -1600 -703 -529 C ATOM 2063 CD2 TYR A1101 35.547 13.936 -43.438 1.00 67.26 C ANISOU 2063 CD2 TYR A1101 6585 11535 7436 -1141 -662 -624 C ATOM 2064 CE1 TYR A1101 36.135 14.071 -46.131 1.00 83.87 C ANISOU 2064 CE1 TYR A1101 9076 13627 9163 -1653 -970 -532 C ATOM 2065 CE2 TYR A1101 34.527 14.087 -44.359 1.00 90.25 C ANISOU 2065 CE2 TYR A1101 9415 14487 10388 -1186 -920 -633 C ATOM 2066 CZ TYR A1101 34.826 14.154 -45.703 1.00 90.30 C ANISOU 2066 CZ TYR A1101 9642 14471 10196 -1441 -1112 -585 C ATOM 2067 OH TYR A1101 33.812 14.305 -46.621 1.00 90.79 O ANISOU 2067 OH TYR A1101 9672 14550 10274 -1480 -1447 -591 O ATOM 2068 N ILE A1102 40.597 13.866 -41.386 1.00 69.65 N ANISOU 2068 N ILE A1102 7232 11641 7591 -1255 -266 -512 N ATOM 2069 CA ILE A1102 41.354 13.313 -40.263 1.00 67.94 C ANISOU 2069 CA ILE A1102 6986 11388 7441 -1123 -158 -542 C ATOM 2070 C ILE A1102 41.992 14.425 -39.442 1.00 70.05 C ANISOU 2070 C ILE A1102 7401 11507 7706 -1044 -421 -495 C ATOM 2071 O ILE A1102 41.889 14.450 -38.209 1.00 81.88 O ANISOU 2071 O ILE A1102 9011 12909 9190 -810 -462 -533 O ATOM 2072 CB ILE A1102 42.412 12.316 -40.772 1.00 65.14 C ANISOU 2072 CB ILE A1102 6495 11124 7132 -1267 47 -564 C ATOM 2073 CG1 ILE A1102 41.816 11.413 -41.858 1.00 61.18 C ANISOU 2073 CG1 ILE A1102 5943 10724 6580 -1395 241 -626 C ATOM 2074 CG2 ILE A1102 42.981 11.498 -39.617 1.00 62.46 C ANISOU 2074 CG2 ILE A1102 6131 10726 6875 -1076 128 -603 C ATOM 2075 CD1 ILE A1102 40.692 10.519 -41.376 1.00 61.74 C ANISOU 2075 CD1 ILE A1102 5994 10775 6688 -1276 359 -689 C ATOM 2076 N GLN A1103 42.666 15.360 -40.117 1.00 81.83 N ANISOU 2076 N GLN A1103 8943 12960 9188 -1264 -608 -406 N ATOM 2077 CA GLN A1103 43.405 16.403 -39.411 1.00 78.14 C ANISOU 2077 CA GLN A1103 8626 12316 8746 -1267 -905 -357 C ATOM 2078 C GLN A1103 42.479 17.252 -38.548 1.00 87.23 C ANISOU 2078 C GLN A1103 10049 13279 9817 -981 -1121 -407 C ATOM 2079 O GLN A1103 42.807 17.569 -37.398 1.00 83.63 O ANISOU 2079 O GLN A1103 9761 12673 9340 -812 -1281 -450 O ATOM 2080 CB GLN A1103 44.170 17.272 -40.411 1.00 70.57 C ANISOU 2080 CB GLN A1103 7685 11336 7791 -1627 -1042 -222 C ATOM 2081 N LYS A1104 41.310 17.619 -39.078 1.00 80.07 N ANISOU 2081 N LYS A1104 9195 12372 8857 -895 -1141 -418 N ATOM 2082 CA LYS A1104 40.345 18.369 -38.282 1.00 69.86 C ANISOU 2082 CA LYS A1104 8105 10927 7510 -550 -1288 -500 C ATOM 2083 C LYS A1104 39.726 17.503 -37.193 1.00 82.32 C ANISOU 2083 C LYS A1104 9610 12598 9070 -256 -1005 -613 C ATOM 2084 O LYS A1104 39.340 18.016 -36.136 1.00 86.03 O ANISOU 2084 O LYS A1104 10297 12939 9452 51 -1064 -699 O ATOM 2085 CB LYS A1104 39.257 18.952 -39.182 1.00 68.30 C ANISOU 2085 CB LYS A1104 7916 10721 7314 -502 -1410 -485 C ATOM 2086 N TYR A1105 39.632 16.192 -37.427 1.00 71.82 N ANISOU 2086 N TYR A1105 8027 11468 7794 -351 -687 -613 N ATOM 2087 CA TYR A1105 39.071 15.293 -36.425 1.00 70.97 C ANISOU 2087 CA TYR A1105 7883 11428 7653 -143 -393 -678 C ATOM 2088 C TYR A1105 39.968 15.197 -35.199 1.00 70.00 C ANISOU 2088 C TYR A1105 8000 11174 7423 -26 -447 -689 C ATOM 2089 O TYR A1105 39.475 15.103 -34.068 1.00 78.16 O ANISOU 2089 O TYR A1105 9214 12163 8321 235 -320 -745 O ATOM 2090 CB TYR A1105 38.849 13.912 -37.041 1.00 70.95 C ANISOU 2090 CB TYR A1105 7617 11602 7739 -325 -100 -662 C ATOM 2091 CG TYR A1105 38.616 12.805 -36.040 1.00 68.95 C ANISOU 2091 CG TYR A1105 7382 11372 7446 -214 199 -678 C ATOM 2092 CD1 TYR A1105 37.346 12.553 -35.540 1.00 73.02 C ANISOU 2092 CD1 TYR A1105 7816 11968 7960 -73 447 -709 C ATOM 2093 CD2 TYR A1105 39.663 12.002 -35.608 1.00 70.45 C ANISOU 2093 CD2 TYR A1105 7660 11498 7608 -257 237 -650 C ATOM 2094 CE1 TYR A1105 37.129 11.539 -34.631 1.00 67.84 C ANISOU 2094 CE1 TYR A1105 7226 11316 7235 -27 752 -686 C ATOM 2095 CE2 TYR A1105 39.456 10.988 -34.699 1.00 69.01 C ANISOU 2095 CE2 TYR A1105 7580 11285 7354 -164 477 -635 C ATOM 2096 CZ TYR A1105 38.187 10.760 -34.215 1.00 67.19 C ANISOU 2096 CZ TYR A1105 7326 11123 7082 -75 749 -641 C ATOM 2097 OH TYR A1105 37.974 9.749 -33.311 1.00 67.80 O ANISOU 2097 OH TYR A1105 7551 11153 7056 -36 1019 -591 O ATOM 2098 N LEU A1106 41.288 15.220 -35.403 1.00 68.62 N ANISOU 2098 N LEU A1106 7828 10943 7300 -218 -636 -635 N ATOM 2099 CA LEU A1106 42.218 14.978 -34.304 1.00 69.67 C ANISOU 2099 CA LEU A1106 8142 10959 7373 -123 -755 -642 C ATOM 2100 C LEU A1106 42.114 16.064 -33.240 1.00 72.05 C ANISOU 2100 C LEU A1106 8837 11041 7498 109 -1022 -704 C ATOM 2101 O LEU A1106 41.992 15.769 -32.046 1.00 97.95 O ANISOU 2101 O LEU A1106 12386 14240 10590 348 -973 -753 O ATOM 2102 CB LEU A1106 43.647 14.877 -34.841 1.00 75.90 C ANISOU 2102 CB LEU A1106 8744 11764 8331 -380 -928 -579 C ATOM 2103 N VAL A 313 42.160 17.331 -33.656 1.00108.95 N ANISOU 2103 N VAL A 313 15198 18517 7679 3690 3437 -1998 N ATOM 2104 CA VAL A 313 42.107 18.426 -32.692 1.00101.52 C ANISOU 2104 CA VAL A 313 14143 17536 6893 3436 3392 -1600 C ATOM 2105 C VAL A 313 40.734 18.518 -32.041 1.00 96.79 C ANISOU 2105 C VAL A 313 13805 16477 6493 3302 3073 -1766 C ATOM 2106 O VAL A 313 40.620 18.904 -30.870 1.00 99.70 O ANISOU 2106 O VAL A 313 14123 16616 7142 3173 3018 -1619 O ATOM 2107 CB VAL A 313 42.499 19.752 -33.372 1.00103.57 C ANISOU 2107 CB VAL A 313 14286 18257 6809 3242 3507 -1104 C ATOM 2108 CG1 VAL A 313 43.965 19.726 -33.768 1.00107.93 C ANISOU 2108 CG1 VAL A 313 14507 19257 7244 3340 3826 -866 C ATOM 2109 CG2 VAL A 313 41.619 20.004 -34.588 1.00108.33 C ANISOU 2109 CG2 VAL A 313 15142 18981 7037 3219 3366 -1196 C ATOM 2110 N GLN A 314 39.675 18.165 -32.771 1.00106.19 N ANISOU 2110 N GLN A 314 15269 17541 7536 3324 2859 -2065 N ATOM 2111 CA GLN A 314 38.320 18.310 -32.248 1.00 93.76 C ANISOU 2111 CA GLN A 314 13918 15578 6130 3191 2544 -2184 C ATOM 2112 C GLN A 314 38.104 17.412 -31.036 1.00 90.33 C ANISOU 2112 C GLN A 314 13487 14651 6185 3236 2438 -2444 C ATOM 2113 O GLN A 314 37.697 17.878 -29.966 1.00 95.76 O ANISOU 2113 O GLN A 314 14179 15080 7126 3108 2333 -2317 O ATOM 2114 CB GLN A 314 37.304 17.998 -33.348 1.00 96.27 C ANISOU 2114 CB GLN A 314 14484 15917 6179 3201 2335 -2445 C ATOM 2115 CG GLN A 314 35.858 18.221 -32.953 1.00 92.93 C ANISOU 2115 CG GLN A 314 14260 15167 5883 3064 1996 -2520 C ATOM 2116 CD GLN A 314 34.896 17.777 -34.035 1.00105.84 C ANISOU 2116 CD GLN A 314 16109 16854 7253 3065 1778 -2790 C ATOM 2117 OE1 GLN A 314 35.087 16.734 -34.660 1.00119.29 O ANISOU 2117 OE1 GLN A 314 17877 18563 8883 3180 1810 -3130 O ATOM 2118 NE2 GLN A 314 33.861 18.574 -34.270 1.00120.84 N ANISOU 2118 NE2 GLN A 314 18125 18798 8991 2939 1555 -2626 N ATOM 2119 N THR A 315 38.388 16.117 -31.187 1.00 92.54 N ANISOU 2119 N THR A 315 13774 14787 6600 3417 2475 -2792 N ATOM 2120 CA THR A 315 38.227 15.165 -30.093 1.00108.68 C ANISOU 2120 CA THR A 315 15810 16362 9123 3457 2377 -3009 C ATOM 2121 C THR A 315 38.991 15.612 -28.852 1.00 86.79 C ANISOU 2121 C THR A 315 12798 13571 6607 3424 2514 -2719 C ATOM 2122 O THR A 315 38.423 15.721 -27.760 1.00 82.66 O ANISOU 2122 O THR A 315 12303 12709 6394 3304 2355 -2698 O ATOM 2123 CB THR A 315 38.702 13.783 -30.541 1.00 93.90 C ANISOU 2123 CB THR A 315 13959 14403 7316 3682 2473 -3348 C ATOM 2124 OG1 THR A 315 37.976 13.386 -31.709 1.00 97.26 O ANISOU 2124 OG1 THR A 315 14631 14858 7465 3686 2345 -3630 O ATOM 2125 CG2 THR A 315 38.484 12.760 -29.438 1.00101.78 C ANISOU 2125 CG2 THR A 315 14956 14895 8822 3707 2357 -3538 C ATOM 2126 N ILE A 316 40.288 15.882 -29.018 1.00 89.08 N ANISOU 2126 N ILE A 316 12838 14252 6756 3517 2813 -2475 N ATOM 2127 CA ILE A 316 41.148 16.228 -27.887 1.00 86.93 C ANISOU 2127 CA ILE A 316 12295 14033 6700 3481 2964 -2181 C ATOM 2128 C ILE A 316 40.621 17.467 -27.178 1.00 82.93 C ANISOU 2128 C ILE A 316 11825 13443 6242 3173 2840 -1879 C ATOM 2129 O ILE A 316 40.383 17.458 -25.965 1.00 79.32 O ANISOU 2129 O ILE A 316 11323 12613 6204 2994 2691 -1822 O ATOM 2130 CB ILE A 316 42.597 16.430 -28.360 1.00 90.80 C ANISOU 2130 CB ILE A 316 12475 15036 6987 3585 3292 -1906 C ATOM 2131 CG1 ILE A 316 43.147 15.139 -28.967 1.00 95.09 C ANISOU 2131 CG1 ILE A 316 12992 15584 7554 3897 3412 -2207 C ATOM 2132 CG2 ILE A 316 43.472 16.916 -27.210 1.00 89.64 C ANISOU 2132 CG2 ILE A 316 12011 15013 7033 3481 3433 -1534 C ATOM 2133 CD1 ILE A 316 44.560 15.276 -29.487 1.00116.63 C ANISOU 2133 CD1 ILE A 316 15404 18825 10084 4034 3737 -1944 C ATOM 2134 N SER A 317 40.427 18.551 -27.932 1.00 83.89 N ANISOU 2134 N SER A 317 12007 13815 6053 3001 2837 -1630 N ATOM 2135 CA SER A 317 39.996 19.809 -27.332 1.00 80.86 C ANISOU 2135 CA SER A 317 11641 13239 5843 2603 2673 -1274 C ATOM 2136 C SER A 317 38.633 19.671 -26.664 1.00 77.63 C ANISOU 2136 C SER A 317 11461 12302 5734 2501 2359 -1481 C ATOM 2137 O SER A 317 38.400 20.243 -25.592 1.00 76.74 O ANISOU 2137 O SER A 317 11323 11885 5950 2242 2238 -1301 O ATOM 2138 CB SER A 317 39.965 20.907 -28.393 1.00 83.26 C ANISOU 2138 CB SER A 317 11996 13888 5751 2484 2723 -977 C ATOM 2139 OG SER A 317 39.066 20.570 -29.434 1.00 92.26 O ANISOU 2139 OG SER A 317 13383 15094 6579 2662 2620 -1255 O ATOM 2140 N ASN A 318 37.721 18.912 -27.279 1.00 77.75 N ANISOU 2140 N ASN A 318 11696 12219 5627 2694 2223 -1859 N ATOM 2141 CA ASN A 318 36.381 18.758 -26.718 1.00 74.64 C ANISOU 2141 CA ASN A 318 11484 11373 5501 2595 1922 -2028 C ATOM 2142 C ASN A 318 36.421 18.035 -25.378 1.00 71.72 C ANISOU 2142 C ASN A 318 11026 10625 5599 2578 1862 -2143 C ATOM 2143 O ASN A 318 35.895 18.531 -24.375 1.00 85.31 O ANISOU 2143 O ASN A 318 12746 12043 7626 2355 1719 -2000 O ATOM 2144 CB ASN A 318 35.481 18.010 -27.701 1.00 92.15 C ANISOU 2144 CB ASN A 318 13932 13607 7474 2781 1776 -2409 C ATOM 2145 CG ASN A 318 35.091 18.852 -28.896 1.00 91.19 C ANISOU 2145 CG ASN A 318 13922 13810 6916 2739 1746 -2256 C ATOM 2146 OD1 ASN A 318 35.583 19.967 -29.073 1.00 90.41 O ANISOU 2146 OD1 ASN A 318 13728 13936 6690 2596 1866 -1856 O ATOM 2147 ND2 ASN A 318 34.208 18.319 -29.730 1.00 80.94 N ANISOU 2147 ND2 ASN A 318 12827 12543 5383 2846 1572 -2558 N ATOM 2148 N GLU A 319 37.036 16.849 -25.346 1.00 73.25 N ANISOU 2148 N GLU A 319 11152 10834 5848 2829 1978 -2398 N ATOM 2149 CA GLU A 319 37.121 16.096 -24.099 1.00 70.95 C ANISOU 2149 CA GLU A 319 10760 10201 5996 2829 1924 -2475 C ATOM 2150 C GLU A 319 37.897 16.871 -23.043 1.00 69.58 C ANISOU 2150 C GLU A 319 10350 10057 6029 2596 2009 -2088 C ATOM 2151 O GLU A 319 37.551 16.836 -21.856 1.00 80.53 O ANISOU 2151 O GLU A 319 11702 11132 7764 2437 1876 -2037 O ATOM 2152 CB GLU A 319 37.767 14.733 -24.352 1.00 73.77 C ANISOU 2152 CB GLU A 319 11078 10580 6371 3168 2063 -2773 C ATOM 2153 CG GLU A 319 37.044 13.890 -25.389 1.00 80.93 C ANISOU 2153 CG GLU A 319 12173 11371 7204 3216 1913 -3098 C ATOM 2154 CD GLU A 319 37.496 12.444 -25.377 1.00100.47 C ANISOU 2154 CD GLU A 319 14605 13656 9911 3396 1964 -3336 C ATOM 2155 OE1 GLU A 319 37.510 11.808 -26.452 1.00101.76 O ANISOU 2155 OE1 GLU A 319 14883 13890 9891 3509 1994 -3566 O ATOM 2156 OE2 GLU A 319 37.838 11.943 -24.285 1.00101.49 O ANISOU 2156 OE2 GLU A 319 14599 13562 10399 3429 1979 -3288 O ATOM 2157 N GLN A 320 38.943 17.583 -23.463 1.00 72.08 N ANISOU 2157 N GLN A 320 10501 10768 6118 2553 2223 -1806 N ATOM 2158 CA GLN A 320 39.708 18.424 -22.548 1.00 72.34 C ANISOU 2158 CA GLN A 320 10321 10858 6309 2273 2280 -1423 C ATOM 2159 C GLN A 320 38.816 19.468 -21.889 1.00 70.39 C ANISOU 2159 C GLN A 320 10223 10312 6212 1940 2074 -1271 C ATOM 2160 O GLN A 320 38.766 19.578 -20.658 1.00 68.83 O ANISOU 2160 O GLN A 320 9969 9870 6314 1755 1982 -1192 O ATOM 2161 CB GLN A 320 40.855 19.093 -23.307 1.00 75.68 C ANISOU 2161 CB GLN A 320 10556 11777 6420 2250 2522 -1125 C ATOM 2162 CG GLN A 320 41.622 20.119 -22.507 1.00 95.72 C ANISOU 2162 CG GLN A 320 12896 14395 9078 1889 2552 -702 C ATOM 2163 CD GLN A 320 42.575 19.482 -21.528 1.00 86.91 C ANISOU 2163 CD GLN A 320 11486 13326 8211 1911 2628 -630 C ATOM 2164 OE1 GLN A 320 43.486 18.752 -21.918 1.00 78.84 O ANISOU 2164 OE1 GLN A 320 10242 12618 7098 2183 2838 -645 O ATOM 2165 NE2 GLN A 320 42.369 19.748 -20.245 1.00 79.07 N ANISOU 2165 NE2 GLN A 320 10485 12037 7522 1642 2464 -545 N ATOM 2166 N ARG A 321 38.094 20.244 -22.701 1.00 70.77 N ANISOU 2166 N ARG A 321 10465 10386 6040 1879 2005 -1225 N ATOM 2167 CA ARG A 321 37.268 21.322 -22.165 1.00 69.45 C ANISOU 2167 CA ARG A 321 10446 9938 6005 1608 1841 -1060 C ATOM 2168 C ARG A 321 36.153 20.775 -21.282 1.00 66.16 C ANISOU 2168 C ARG A 321 10140 9104 5894 1622 1634 -1289 C ATOM 2169 O ARG A 321 35.890 21.305 -20.198 1.00 73.43 O ANISOU 2169 O ARG A 321 11076 9770 7054 1413 1552 -1176 O ATOM 2170 CB ARG A 321 36.692 22.159 -23.309 1.00 70.93 C ANISOU 2170 CB ARG A 321 10804 10252 5896 1597 1811 -950 C ATOM 2171 N ALA A 322 35.492 19.704 -21.730 1.00 65.15 N ANISOU 2171 N ALA A 322 10093 8909 5751 1857 1547 -1613 N ATOM 2172 CA ALA A 322 34.386 19.138 -20.963 1.00 62.14 C ANISOU 2172 CA ALA A 322 9795 8159 5657 1856 1343 -1803 C ATOM 2173 C ALA A 322 34.860 18.632 -19.605 1.00 60.57 C ANISOU 2173 C ALA A 322 9439 7788 5785 1790 1358 -1786 C ATOM 2174 O ALA A 322 34.271 18.959 -18.568 1.00 58.50 O ANISOU 2174 O ALA A 322 9199 7273 5755 1628 1248 -1718 O ATOM 2175 CB ALA A 322 33.715 18.017 -21.757 1.00 69.26 C ANISOU 2175 CB ALA A 322 10807 9035 6475 2087 1238 -2152 C ATOM 2176 N SER A 323 35.929 17.831 -19.592 1.00 61.84 N ANISOU 2176 N SER A 323 9433 8107 5957 1930 1503 -1834 N ATOM 2177 CA SER A 323 36.483 17.366 -18.324 1.00 67.10 C ANISOU 2177 CA SER A 323 9917 8661 6915 1868 1518 -1763 C ATOM 2178 C SER A 323 36.931 18.530 -17.453 1.00 61.48 C ANISOU 2178 C SER A 323 9128 7980 6253 1554 1541 -1449 C ATOM 2179 O SER A 323 36.849 18.450 -16.222 1.00 75.11 O ANISOU 2179 O SER A 323 10791 9528 8219 1414 1466 -1393 O ATOM 2180 CB SER A 323 37.654 16.418 -18.572 1.00 67.81 C ANISOU 2180 CB SER A 323 9814 8963 6987 2103 1696 -1814 C ATOM 2181 OG SER A 323 38.786 17.132 -19.036 1.00 67.01 O ANISOU 2181 OG SER A 323 9563 9243 6657 2053 1893 -1571 O ATOM 2182 N LYS A 324 37.395 19.619 -18.070 1.00 63.57 N ANISOU 2182 N LYS A 324 9408 8462 6282 1424 1636 -1241 N ATOM 2183 CA LYS A 324 37.853 20.770 -17.300 1.00 64.50 C ANISOU 2183 CA LYS A 324 9489 8576 6441 1091 1643 -955 C ATOM 2184 C LYS A 324 36.695 21.436 -16.567 1.00 62.14 C ANISOU 2184 C LYS A 324 9403 7920 6287 927 1480 -976 C ATOM 2185 O LYS A 324 36.758 21.650 -15.351 1.00 84.52 O ANISOU 2185 O LYS A 324 12208 10605 9299 735 1426 -912 O ATOM 2186 CB LYS A 324 38.562 21.769 -18.215 1.00 67.42 C ANISOU 2186 CB LYS A 324 9843 9235 6538 980 1773 -710 C ATOM 2187 N VAL A 325 35.624 21.770 -17.292 1.00 61.19 N ANISOU 2187 N VAL A 325 9488 7683 6077 1014 1403 -1060 N ATOM 2188 CA VAL A 325 34.498 22.453 -16.659 1.00 59.27 C ANISOU 2188 CA VAL A 325 9430 7122 5968 905 1275 -1057 C ATOM 2189 C VAL A 325 33.824 21.541 -15.642 1.00 56.19 C ANISOU 2189 C VAL A 325 9001 6515 5833 967 1166 -1237 C ATOM 2190 O VAL A 325 33.384 21.997 -14.581 1.00 54.79 O ANISOU 2190 O VAL A 325 8883 6129 5806 823 1112 -1197 O ATOM 2191 CB VAL A 325 33.505 22.972 -17.719 1.00 59.61 C ANISOU 2191 CB VAL A 325 9658 7132 5859 1010 1213 -1065 C ATOM 2192 CG1 VAL A 325 34.227 23.832 -18.742 1.00 62.94 C ANISOU 2192 CG1 VAL A 325 10101 7798 6016 945 1328 -846 C ATOM 2193 CG2 VAL A 325 32.764 21.829 -18.400 1.00 65.94 C ANISOU 2193 CG2 VAL A 325 10460 7963 6633 1266 1122 -1323 C ATOM 2194 N LEU A 326 33.757 20.238 -15.932 1.00 55.37 N ANISOU 2194 N LEU A 326 8805 6454 5780 1178 1138 -1434 N ATOM 2195 CA LEU A 326 33.190 19.295 -14.974 1.00 59.25 C ANISOU 2195 CA LEU A 326 9237 6743 6532 1220 1033 -1566 C ATOM 2196 C LEU A 326 34.013 19.271 -13.692 1.00 53.35 C ANISOU 2196 C LEU A 326 8339 6003 5927 1055 1079 -1436 C ATOM 2197 O LEU A 326 33.462 19.304 -12.586 1.00 83.42 O ANISOU 2197 O LEU A 326 12157 9636 9903 951 1003 -1423 O ATOM 2198 CB LEU A 326 33.105 17.900 -15.598 1.00 63.51 C ANISOU 2198 CB LEU A 326 9728 7298 7106 1463 997 -1795 C ATOM 2199 CG LEU A 326 32.434 16.780 -14.798 1.00 70.03 C ANISOU 2199 CG LEU A 326 10503 7890 8216 1516 866 -1928 C ATOM 2200 CD1 LEU A 326 31.691 15.851 -15.739 1.00 83.03 C ANISOU 2200 CD1 LEU A 326 12242 9458 9847 1703 753 -2181 C ATOM 2201 CD2 LEU A 326 33.454 15.995 -13.984 1.00 51.55 C ANISOU 2201 CD2 LEU A 326 7964 5581 6040 1532 939 -1875 C ATOM 2202 N GLY A 327 35.340 19.228 -13.826 1.00 55.84 N ANISOU 2202 N GLY A 327 8496 6560 6159 1026 1206 -1320 N ATOM 2203 CA GLY A 327 36.191 19.259 -12.647 1.00 61.09 C ANISOU 2203 CA GLY A 327 8992 7287 6930 840 1230 -1162 C ATOM 2204 C GLY A 327 36.001 20.521 -11.828 1.00 56.99 C ANISOU 2204 C GLY A 327 8600 6661 6392 538 1192 -1031 C ATOM 2205 O GLY A 327 35.927 20.473 -10.598 1.00 56.38 O ANISOU 2205 O GLY A 327 8487 6494 6439 397 1133 -1000 O ATOM 2206 N ILE A 328 35.900 21.668 -12.504 1.00 67.62 N ANISOU 2206 N ILE A 328 10116 8003 7573 441 1227 -956 N ATOM 2207 CA ILE A 328 35.780 22.941 -11.796 1.00 70.96 C ANISOU 2207 CA ILE A 328 10707 8276 7979 158 1202 -846 C ATOM 2208 C ILE A 328 34.474 22.996 -11.013 1.00 61.73 C ANISOU 2208 C ILE A 328 9698 6813 6944 196 1109 -979 C ATOM 2209 O ILE A 328 34.464 23.293 -9.812 1.00 54.66 O ANISOU 2209 O ILE A 328 8836 5819 6113 17 1078 -963 O ATOM 2210 CB ILE A 328 35.902 24.124 -12.774 1.00 60.16 C ANISOU 2210 CB ILE A 328 9498 6925 6433 72 1258 -715 C ATOM 2211 CG1 ILE A 328 37.327 24.240 -13.319 1.00 66.53 C ANISOU 2211 CG1 ILE A 328 10115 8066 7099 -43 1364 -518 C ATOM 2212 CG2 ILE A 328 35.502 25.420 -12.086 1.00 60.46 C ANISOU 2212 CG2 ILE A 328 9787 6693 6491 -169 1220 -654 C ATOM 2213 CD1 ILE A 328 37.555 25.485 -14.164 1.00 65.80 C ANISOU 2213 CD1 ILE A 328 10165 7999 6839 -194 1416 -325 C ATOM 2214 N VAL A 329 33.353 22.705 -11.678 1.00 65.02 N ANISOU 2214 N VAL A 329 10204 7116 7386 427 1063 -1104 N ATOM 2215 CA VAL A 329 32.055 22.837 -11.021 1.00 50.20 C ANISOU 2215 CA VAL A 329 8449 4995 5630 479 990 -1191 C ATOM 2216 C VAL A 329 31.916 21.827 -9.887 1.00 55.92 C ANISOU 2216 C VAL A 329 9020 5703 6526 485 938 -1258 C ATOM 2217 O VAL A 329 31.361 22.141 -8.828 1.00 65.23 O ANISOU 2217 O VAL A 329 10264 6750 7772 405 919 -1265 O ATOM 2218 CB VAL A 329 30.909 22.715 -12.045 1.00 49.09 C ANISOU 2218 CB VAL A 329 8389 4788 5474 707 932 -1271 C ATOM 2219 CG1 VAL A 329 30.982 23.847 -13.059 1.00 51.29 C ANISOU 2219 CG1 VAL A 329 8831 5080 5577 688 980 -1155 C ATOM 2220 CG2 VAL A 329 30.929 21.361 -12.741 1.00 73.31 C ANISOU 2220 CG2 VAL A 329 11307 7983 8566 894 881 -1401 C ATOM 2221 N PHE A 330 32.426 20.606 -10.079 1.00 48.95 N ANISOU 2221 N PHE A 330 7936 4952 5711 591 923 -1299 N ATOM 2222 CA PHE A 330 32.368 19.610 -9.013 1.00 48.20 C ANISOU 2222 CA PHE A 330 7681 4837 5796 593 869 -1314 C ATOM 2223 C PHE A 330 33.256 20.007 -7.842 1.00 49.98 C ANISOU 2223 C PHE A 330 7838 5156 5995 347 901 -1181 C ATOM 2224 O PHE A 330 32.879 19.828 -6.678 1.00 51.51 O ANISOU 2224 O PHE A 330 8003 5295 6274 270 857 -1167 O ATOM 2225 CB PHE A 330 32.772 18.237 -9.547 1.00 48.79 C ANISOU 2225 CB PHE A 330 7582 4987 5968 782 852 -1382 C ATOM 2226 CG PHE A 330 31.685 17.535 -10.309 1.00 59.29 C ANISOU 2226 CG PHE A 330 8972 6182 7375 985 761 -1548 C ATOM 2227 CD1 PHE A 330 30.466 18.151 -10.546 1.00 79.81 C ANISOU 2227 CD1 PHE A 330 11724 8656 9945 998 701 -1590 C ATOM 2228 CD2 PHE A 330 31.879 16.248 -10.775 1.00 49.34 C ANISOU 2228 CD2 PHE A 330 7613 4912 6221 1161 727 -1660 C ATOM 2229 CE1 PHE A 330 29.467 17.496 -11.245 1.00 80.82 C ANISOU 2229 CE1 PHE A 330 11879 8693 10135 1148 587 -1722 C ATOM 2230 CE2 PHE A 330 30.886 15.589 -11.471 1.00 60.86 C ANISOU 2230 CE2 PHE A 330 9146 6235 7743 1302 613 -1830 C ATOM 2231 CZ PHE A 330 29.679 16.213 -11.706 1.00 81.51 C ANISOU 2231 CZ PHE A 330 11888 8768 10316 1277 531 -1852 C ATOM 2232 N PHE A 331 34.441 20.549 -8.134 1.00 60.52 N ANISOU 2232 N PHE A 331 9135 6663 7198 206 969 -1068 N ATOM 2233 CA PHE A 331 35.322 21.019 -7.071 1.00 55.02 C ANISOU 2233 CA PHE A 331 8376 6080 6449 -80 970 -932 C ATOM 2234 C PHE A 331 34.670 22.140 -6.272 1.00 60.81 C ANISOU 2234 C PHE A 331 9361 6625 7119 -269 950 -968 C ATOM 2235 O PHE A 331 34.741 22.154 -5.038 1.00 63.34 O ANISOU 2235 O PHE A 331 9662 6963 7441 -433 911 -947 O ATOM 2236 CB PHE A 331 36.653 21.476 -7.666 1.00 58.36 C ANISOU 2236 CB PHE A 331 8702 6735 6739 -218 1040 -779 C ATOM 2237 CG PHE A 331 37.588 22.081 -6.665 1.00 63.44 C ANISOU 2237 CG PHE A 331 9286 7512 7306 -570 1012 -624 C ATOM 2238 CD1 PHE A 331 38.157 21.304 -5.671 1.00 66.80 C ANISOU 2238 CD1 PHE A 331 9469 8108 7804 -634 961 -532 C ATOM 2239 CD2 PHE A 331 37.909 23.426 -6.726 1.00 78.04 C ANISOU 2239 CD2 PHE A 331 11325 9316 9012 -854 1020 -557 C ATOM 2240 CE1 PHE A 331 39.021 21.859 -4.751 1.00 69.29 C ANISOU 2240 CE1 PHE A 331 9721 8584 8021 -988 908 -383 C ATOM 2241 CE2 PHE A 331 38.773 23.986 -5.810 1.00 76.95 C ANISOU 2241 CE2 PHE A 331 11149 9296 8791 -1224 965 -429 C ATOM 2242 CZ PHE A 331 39.330 23.202 -4.821 1.00 74.48 C ANISOU 2242 CZ PHE A 331 10583 9194 8524 -1296 903 -347 C ATOM 2243 N LEU A 332 34.018 23.083 -6.957 1.00 74.05 N ANISOU 2243 N LEU A 332 11284 8122 8728 -231 982 -1023 N ATOM 2244 CA LEU A 332 33.339 24.164 -6.249 1.00 68.92 C ANISOU 2244 CA LEU A 332 10904 7248 8034 -352 986 -1078 C ATOM 2245 C LEU A 332 32.133 23.656 -5.470 1.00 49.21 C ANISOU 2245 C LEU A 332 8413 4637 5647 -194 959 -1187 C ATOM 2246 O LEU A 332 31.766 24.249 -4.450 1.00 49.02 O ANISOU 2246 O LEU A 332 8540 4506 5579 -304 974 -1236 O ATOM 2247 CB LEU A 332 32.923 25.263 -7.227 1.00 85.06 C ANISOU 2247 CB LEU A 332 13196 9113 10011 -308 1031 -1074 C ATOM 2248 CG LEU A 332 34.064 26.118 -7.782 1.00 84.15 C ANISOU 2248 CG LEU A 332 13134 9072 9769 -547 1064 -928 C ATOM 2249 CD1 LEU A 332 33.519 27.345 -8.494 1.00 68.10 C ANISOU 2249 CD1 LEU A 332 11393 6793 7688 -529 1101 -900 C ATOM 2250 CD2 LEU A 332 35.022 26.519 -6.670 1.00 81.46 C ANISOU 2250 CD2 LEU A 332 12790 8795 9365 -907 1034 -873 C ATOM 2251 N PHE A 333 31.505 22.571 -5.929 1.00 57.21 N ANISOU 2251 N PHE A 333 9270 5675 6793 53 921 -1227 N ATOM 2252 CA PHE A 333 30.451 21.944 -5.137 1.00 48.81 C ANISOU 2252 CA PHE A 333 8146 4549 5850 167 885 -1279 C ATOM 2253 C PHE A 333 31.011 21.390 -3.834 1.00 47.15 C ANISOU 2253 C PHE A 333 7783 4478 5655 9 860 -1218 C ATOM 2254 O PHE A 333 30.480 21.657 -2.751 1.00 47.04 O ANISOU 2254 O PHE A 333 7834 4431 5608 -53 875 -1238 O ATOM 2255 CB PHE A 333 29.769 20.834 -5.937 1.00 50.93 C ANISOU 2255 CB PHE A 333 8271 4810 6270 409 818 -1322 C ATOM 2256 CG PHE A 333 28.818 19.997 -5.122 1.00 77.20 C ANISOU 2256 CG PHE A 333 11474 8107 9752 487 763 -1325 C ATOM 2257 CD1 PHE A 333 27.491 20.369 -4.989 1.00 92.44 C ANISOU 2257 CD1 PHE A 333 13485 9924 11715 598 768 -1355 C ATOM 2258 CD2 PHE A 333 29.252 18.841 -4.487 1.00 60.82 C ANISOU 2258 CD2 PHE A 333 9180 6129 7798 455 709 -1264 C ATOM 2259 CE1 PHE A 333 26.616 19.605 -4.242 1.00 65.01 C ANISOU 2259 CE1 PHE A 333 9864 6459 8379 653 723 -1320 C ATOM 2260 CE2 PHE A 333 28.383 18.075 -3.739 1.00 44.26 C ANISOU 2260 CE2 PHE A 333 6959 4008 5849 503 655 -1226 C ATOM 2261 CZ PHE A 333 27.063 18.457 -3.616 1.00 57.37 C ANISOU 2261 CZ PHE A 333 8689 5580 7529 591 663 -1252 C ATOM 2262 N LEU A 334 32.086 20.605 -3.926 1.00 67.92 N ANISOU 2262 N LEU A 334 10198 7286 8321 -40 829 -1129 N ATOM 2263 CA LEU A 334 32.667 19.973 -2.748 1.00 57.35 C ANISOU 2263 CA LEU A 334 8672 6113 7008 -175 787 -1022 C ATOM 2264 C LEU A 334 33.327 20.975 -1.814 1.00 55.15 C ANISOU 2264 C LEU A 334 8505 5918 6531 -484 798 -984 C ATOM 2265 O LEU A 334 33.461 20.692 -0.619 1.00 54.36 O ANISOU 2265 O LEU A 334 8317 5942 6397 -614 759 -920 O ATOM 2266 CB LEU A 334 33.685 18.915 -3.173 1.00 56.04 C ANISOU 2266 CB LEU A 334 8238 6110 6945 -109 763 -917 C ATOM 2267 CG LEU A 334 33.128 17.718 -3.943 1.00 51.76 C ANISOU 2267 CG LEU A 334 7591 5467 6608 178 731 -978 C ATOM 2268 CD1 LEU A 334 34.255 16.836 -4.444 1.00 54.24 C ANISOU 2268 CD1 LEU A 334 7687 5921 6999 274 744 -900 C ATOM 2269 CD2 LEU A 334 32.179 16.928 -3.059 1.00 51.00 C ANISOU 2269 CD2 LEU A 334 7416 5289 6671 231 662 -957 C ATOM 2270 N LEU A 335 33.741 22.135 -2.326 1.00 61.46 N ANISOU 2270 N LEU A 335 9506 6654 7193 -622 839 -1014 N ATOM 2271 CA LEU A 335 34.436 23.106 -1.490 1.00 67.50 C ANISOU 2271 CA LEU A 335 10405 7470 7770 -963 824 -993 C ATOM 2272 C LEU A 335 33.503 23.752 -0.471 1.00 56.81 C ANISOU 2272 C LEU A 335 9303 5958 6324 -1007 849 -1133 C ATOM 2273 O LEU A 335 33.947 24.112 0.625 1.00 59.67 O ANISOU 2273 O LEU A 335 9723 6420 6531 -1271 811 -1135 O ATOM 2274 CB LEU A 335 35.096 24.167 -2.369 1.00 58.80 C ANISOU 2274 CB LEU A 335 9461 6305 6573 -1114 854 -969 C ATOM 2275 CG LEU A 335 35.997 25.182 -1.669 1.00 60.93 C ANISOU 2275 CG LEU A 335 9867 6620 6662 -1529 808 -930 C ATOM 2276 CD1 LEU A 335 37.083 24.463 -0.889 1.00 83.82 C ANISOU 2276 CD1 LEU A 335 12453 9870 9525 -1730 719 -765 C ATOM 2277 CD2 LEU A 335 36.603 26.137 -2.681 1.00 68.64 C ANISOU 2277 CD2 LEU A 335 10971 7524 7586 -1670 835 -861 C ATOM 2278 N MET A 336 32.219 23.896 -0.801 1.00 51.53 N ANISOU 2278 N MET A 336 8775 5073 5732 -747 914 -1248 N ATOM 2279 CA MET A 336 31.258 24.596 0.044 1.00 50.90 C ANISOU 2279 CA MET A 336 8942 4836 5564 -723 980 -1386 C ATOM 2280 C MET A 336 30.631 23.697 1.099 1.00 67.28 C ANISOU 2280 C MET A 336 10841 7057 7667 -638 973 -1365 C ATOM 2281 O MET A 336 29.933 24.201 1.988 1.00 70.96 O ANISOU 2281 O MET A 336 11478 7466 8016 -627 1044 -1470 O ATOM 2282 CB MET A 336 30.163 25.225 -0.819 1.00 48.94 C ANISOU 2282 CB MET A 336 8893 4314 5389 -463 1062 -1474 C ATOM 2283 CG MET A 336 30.692 26.144 -1.899 1.00 59.26 C ANISOU 2283 CG MET A 336 10379 5469 6667 -534 1073 -1458 C ATOM 2284 SD MET A 336 29.370 26.864 -2.889 1.00 68.57 S ANISOU 2284 SD MET A 336 11766 6354 7933 -210 1156 -1509 S ATOM 2285 CE MET A 336 28.498 27.815 -1.648 1.00 70.35 C ANISOU 2285 CE MET A 336 12301 6363 8065 -177 1270 -1671 C ATOM 2286 N TRP A 337 30.861 22.383 1.015 1.00 64.39 N ANISOU 2286 N TRP A 337 10144 6871 7452 -566 899 -1225 N ATOM 2287 CA TRP A 337 30.505 21.436 2.070 1.00 52.41 C ANISOU 2287 CA TRP A 337 8418 5527 5970 -545 869 -1136 C ATOM 2288 C TRP A 337 31.603 21.244 3.107 1.00 55.43 C ANISOU 2288 C TRP A 337 8685 6171 6205 -830 797 -1023 C ATOM 2289 O TRP A 337 31.306 20.813 4.226 1.00 57.07 O ANISOU 2289 O TRP A 337 8798 6539 6348 -871 787 -958 O ATOM 2290 CB TRP A 337 30.162 20.067 1.478 1.00 51.66 C ANISOU 2290 CB TRP A 337 8038 5446 6144 -329 809 -1026 C ATOM 2291 CG TRP A 337 28.778 19.985 1.003 1.00 55.80 C ANISOU 2291 CG TRP A 337 8603 5804 6795 -80 848 -1094 C ATOM 2292 CD1 TRP A 337 28.367 19.943 -0.287 1.00 53.98 C ANISOU 2292 CD1 TRP A 337 8402 5417 6690 100 836 -1152 C ATOM 2293 CD2 TRP A 337 27.595 19.946 1.806 1.00 69.84 C ANISOU 2293 CD2 TRP A 337 10374 7593 8568 13 903 -1090 C ATOM 2294 NE1 TRP A 337 27.001 19.875 -0.348 1.00 46.17 N ANISOU 2294 NE1 TRP A 337 7413 4340 5791 285 859 -1175 N ATOM 2295 CE2 TRP A 337 26.502 19.876 0.926 1.00 65.94 C ANISOU 2295 CE2 TRP A 337 9883 6945 8225 245 911 -1130 C ATOM 2296 CE3 TRP A 337 27.354 19.962 3.181 1.00 53.47 C ANISOU 2296 CE3 TRP A 337 8279 5680 6356 -77 949 -1045 C ATOM 2297 CZ2 TRP A 337 25.193 19.822 1.371 1.00 65.16 C ANISOU 2297 CZ2 TRP A 337 9738 6852 8169 390 966 -1105 C ATOM 2298 CZ3 TRP A 337 26.058 19.908 3.619 1.00 53.34 C ANISOU 2298 CZ3 TRP A 337 8232 5669 6365 84 1025 -1034 C ATOM 2299 CH2 TRP A 337 24.991 19.839 2.718 1.00 54.90 C ANISOU 2299 CH2 TRP A 337 8405 5714 6740 317 1035 -1053 C ATOM 2300 N CYS A 338 32.854 21.534 2.758 1.00 56.48 N ANISOU 2300 N CYS A 338 8795 6387 6276 -1031 743 -968 N ATOM 2301 CA CYS A 338 33.957 21.272 3.678 1.00 59.31 C ANISOU 2301 CA CYS A 338 8984 7043 6508 -1309 648 -814 C ATOM 2302 C CYS A 338 33.746 21.876 5.070 1.00 60.20 C ANISOU 2302 C CYS A 338 9271 7254 6348 -1526 646 -893 C ATOM 2303 O CYS A 338 33.823 21.116 6.052 1.00 61.74 O ANISOU 2303 O CYS A 338 9258 7698 6501 -1579 589 -747 O ATOM 2304 CB CYS A 338 35.269 21.728 3.017 1.00 65.61 C ANISOU 2304 CB CYS A 338 9751 7916 7262 -1511 602 -745 C ATOM 2305 SG CYS A 338 35.829 20.676 1.631 1.00 86.68 S ANISOU 2305 SG CYS A 338 12109 10622 10204 -1254 607 -598 S ATOM 2306 N PRO A 339 33.445 23.172 5.235 1.00 59.48 N ANISOU 2306 N PRO A 339 9563 6976 6063 -1640 710 -1117 N ATOM 2307 CA PRO A 339 33.200 23.696 6.591 1.00 60.78 C ANISOU 2307 CA PRO A 339 9922 7235 5937 -1820 723 -1234 C ATOM 2308 C PRO A 339 32.245 22.846 7.407 1.00 77.43 C ANISOU 2308 C PRO A 339 11871 9488 8060 -1621 773 -1172 C ATOM 2309 O PRO A 339 32.593 22.484 8.536 1.00100.16 O ANISOU 2309 O PRO A 339 14632 12671 10755 -1804 706 -1070 O ATOM 2310 CB PRO A 339 32.630 25.109 6.333 1.00 59.79 C ANISOU 2310 CB PRO A 339 10262 6752 5703 -1804 836 -1519 C ATOM 2311 CG PRO A 339 32.329 25.194 4.864 1.00 67.20 C ANISOU 2311 CG PRO A 339 11205 7427 6901 -1561 889 -1512 C ATOM 2312 CD PRO A 339 33.287 24.222 4.214 1.00 66.03 C ANISOU 2312 CD PRO A 339 10682 7485 6920 -1597 779 -1273 C ATOM 2313 N PHE A 340 31.058 22.512 6.876 1.00 65.31 N ANISOU 2313 N PHE A 340 10309 7775 6731 -1272 879 -1200 N ATOM 2314 CA PHE A 340 30.096 21.725 7.652 1.00 60.16 C ANISOU 2314 CA PHE A 340 9485 7271 6102 -1103 930 -1108 C ATOM 2315 C PHE A 340 30.720 20.442 8.190 1.00 62.14 C ANISOU 2315 C PHE A 340 9350 7832 6428 -1198 799 -814 C ATOM 2316 O PHE A 340 30.587 20.123 9.377 1.00 63.90 O ANISOU 2316 O PHE A 340 9484 8320 6475 -1290 793 -715 O ATOM 2317 CB PHE A 340 28.849 21.371 6.833 1.00 58.27 C ANISOU 2317 CB PHE A 340 9186 6824 6131 -746 1017 -1115 C ATOM 2318 CG PHE A 340 27.876 20.526 7.608 1.00 59.87 C ANISOU 2318 CG PHE A 340 9171 7199 6378 -604 1059 -974 C ATOM 2319 CD1 PHE A 340 26.963 21.109 8.464 1.00 73.56 C ANISOU 2319 CD1 PHE A 340 11063 8988 7898 -526 1211 -1085 C ATOM 2320 CD2 PHE A 340 27.929 19.148 7.549 1.00 60.96 C ANISOU 2320 CD2 PHE A 340 8947 7454 6758 -561 952 -715 C ATOM 2321 CE1 PHE A 340 26.094 20.315 9.218 1.00 65.22 C ANISOU 2321 CE1 PHE A 340 9770 8145 6866 -413 1259 -911 C ATOM 2322 CE2 PHE A 340 27.063 18.371 8.301 1.00 65.17 C ANISOU 2322 CE2 PHE A 340 9271 8153 7339 -472 980 -542 C ATOM 2323 CZ PHE A 340 26.152 18.955 9.128 1.00 63.77 C ANISOU 2323 CZ PHE A 340 9217 8073 6939 -406 1134 -626 C ATOM 2324 N PHE A 341 31.397 19.683 7.329 1.00 74.37 N ANISOU 2324 N PHE A 341 10666 9357 8235 -1158 703 -659 N ATOM 2325 CA PHE A 341 31.831 18.353 7.737 1.00 70.76 C ANISOU 2325 CA PHE A 341 9834 9127 7926 -1164 595 -360 C ATOM 2326 C PHE A 341 33.106 18.396 8.570 1.00 65.66 C ANISOU 2326 C PHE A 341 9083 8802 7064 -1479 481 -213 C ATOM 2327 O PHE A 341 33.297 17.551 9.450 1.00 67.14 O ANISOU 2327 O PHE A 341 9016 9256 7240 -1536 407 38 O ATOM 2328 CB PHE A 341 31.988 17.458 6.511 1.00 63.66 C ANISOU 2328 CB PHE A 341 8741 8055 7393 -951 554 -272 C ATOM 2329 CG PHE A 341 30.688 16.975 5.970 1.00 62.86 C ANISOU 2329 CG PHE A 341 8629 7732 7523 -674 607 -319 C ATOM 2330 CD1 PHE A 341 29.949 16.049 6.677 1.00 64.48 C ANISOU 2330 CD1 PHE A 341 8636 8023 7839 -602 589 -140 C ATOM 2331 CD2 PHE A 341 30.154 17.497 4.811 1.00 62.85 C ANISOU 2331 CD2 PHE A 341 8810 7461 7610 -512 667 -519 C ATOM 2332 CE1 PHE A 341 28.717 15.617 6.211 1.00 64.29 C ANISOU 2332 CE1 PHE A 341 8582 7817 8030 -388 619 -161 C ATOM 2333 CE2 PHE A 341 28.918 17.060 4.345 1.00 65.33 C ANISOU 2333 CE2 PHE A 341 9092 7609 8123 -285 691 -544 C ATOM 2334 CZ PHE A 341 28.208 16.123 5.048 1.00 60.59 C ANISOU 2334 CZ PHE A 341 8282 7094 7644 -235 663 -367 C ATOM 2335 N ILE A 342 33.990 19.360 8.319 1.00 65.53 N ANISOU 2335 N ILE A 342 9240 8782 6876 -1705 450 -332 N ATOM 2336 CA ILE A 342 35.152 19.496 9.193 1.00 67.63 C ANISOU 2336 CA ILE A 342 9407 9391 6898 -2054 319 -190 C ATOM 2337 C ILE A 342 34.722 19.968 10.582 1.00 68.43 C ANISOU 2337 C ILE A 342 9682 9684 6634 -2237 328 -278 C ATOM 2338 O ILE A 342 35.262 19.520 11.601 1.00 70.28 O ANISOU 2338 O ILE A 342 9719 10285 6697 -2434 215 -66 O ATOM 2339 CB ILE A 342 36.211 20.429 8.571 1.00 70.11 C ANISOU 2339 CB ILE A 342 9852 9664 7123 -2295 267 -274 C ATOM 2340 CG1 ILE A 342 36.421 20.116 7.091 1.00 66.69 C ANISOU 2340 CG1 ILE A 342 9311 9020 7008 -2061 311 -246 C ATOM 2341 CG2 ILE A 342 37.536 20.248 9.265 1.00 89.50 C ANISOU 2341 CG2 ILE A 342 12066 12520 9420 -2628 97 -30 C ATOM 2342 CD1 ILE A 342 37.363 21.112 6.394 1.00 67.06 C ANISOU 2342 CD1 ILE A 342 9491 9022 6967 -2291 286 -311 C ATOM 2343 N THR A 343 33.725 20.855 10.651 1.00 67.36 N ANISOU 2343 N THR A 343 9910 9321 6363 -2153 470 -581 N ATOM 2344 CA THR A 343 33.171 21.230 11.949 1.00 68.54 C ANISOU 2344 CA THR A 343 10232 9651 6158 -2253 523 -690 C ATOM 2345 C THR A 343 32.475 20.046 12.609 1.00 69.18 C ANISOU 2345 C THR A 343 10005 9957 6324 -2070 547 -436 C ATOM 2346 O THR A 343 32.642 19.809 13.811 1.00 70.92 O ANISOU 2346 O THR A 343 10138 10541 6268 -2245 494 -310 O ATOM 2347 CB THR A 343 32.203 22.402 11.797 1.00 67.55 C ANISOU 2347 CB THR A 343 10554 9201 5909 -2125 705 -1065 C ATOM 2348 OG1 THR A 343 32.866 23.490 11.144 1.00 66.98 O ANISOU 2348 OG1 THR A 343 10774 8882 5793 -2310 671 -1267 O ATOM 2349 CG2 THR A 343 31.709 22.868 13.159 1.00 69.41 C ANISOU 2349 CG2 THR A 343 11004 9638 5730 -2220 784 -1219 C ATOM 2350 N ASN A 344 31.695 19.290 11.833 1.00 68.00 N ANISOU 2350 N ASN A 344 9685 9604 6547 -1742 614 -344 N ATOM 2351 CA ASN A 344 30.969 18.149 12.379 1.00 68.83 C ANISOU 2351 CA ASN A 344 9496 9874 6782 -1583 628 -80 C ATOM 2352 C ASN A 344 31.924 17.063 12.864 1.00 70.05 C ANISOU 2352 C ASN A 344 9275 10330 7009 -1724 454 302 C ATOM 2353 O ASN A 344 31.662 16.405 13.878 1.00 71.30 O ANISOU 2353 O ASN A 344 9240 10781 7070 -1759 433 543 O ATOM 2354 CB ASN A 344 30.015 17.604 11.317 1.00 68.86 C ANISOU 2354 CB ASN A 344 9413 9558 7191 -1249 698 -75 C ATOM 2355 CG ASN A 344 28.874 16.809 11.905 1.00 88.02 C ANISOU 2355 CG ASN A 344 11646 12096 9703 -1088 763 111 C ATOM 2356 OD1 ASN A 344 28.394 17.100 13.000 1.00 92.44 O ANISOU 2356 OD1 ASN A 344 12263 12904 9957 -1144 851 107 O ATOM 2357 ND2 ASN A 344 28.431 15.793 11.175 1.00 76.42 N ANISOU 2357 ND2 ASN A 344 9946 10449 8640 -898 718 277 N ATOM 2358 N ILE A 345 33.040 16.864 12.157 1.00 79.06 N ANISOU 2358 N ILE A 345 10295 11425 8319 -1794 336 387 N ATOM 2359 CA ILE A 345 34.006 15.843 12.556 1.00 75.26 C ANISOU 2359 CA ILE A 345 9439 11221 7937 -1887 178 772 C ATOM 2360 C ILE A 345 34.751 16.275 13.813 1.00 72.74 C ANISOU 2360 C ILE A 345 9120 11338 7180 -2245 74 858 C ATOM 2361 O ILE A 345 34.852 15.517 14.785 1.00 74.08 O ANISOU 2361 O ILE A 345 9036 11838 7272 -2312 -5 1175 O ATOM 2362 CB ILE A 345 34.976 15.537 11.399 1.00 74.24 C ANISOU 2362 CB ILE A 345 9168 10936 8104 -1817 113 833 C ATOM 2363 CG1 ILE A 345 34.269 14.723 10.312 1.00 71.67 C ANISOU 2363 CG1 ILE A 345 8766 10245 8219 -1460 178 826 C ATOM 2364 CG2 ILE A 345 36.212 14.810 11.910 1.00 72.30 C ANISOU 2364 CG2 ILE A 345 8564 11033 7872 -1959 -46 1211 C ATOM 2365 CD1 ILE A 345 33.759 13.381 10.780 1.00 72.80 C ANISOU 2365 CD1 ILE A 345 8627 10425 8609 -1310 139 1135 C ATOM 2366 N THR A 346 35.287 17.499 13.811 1.00 72.91 N ANISOU 2366 N THR A 346 9431 11368 6903 -2498 58 589 N ATOM 2367 CA THR A 346 36.026 17.985 14.972 1.00 91.99 C ANISOU 2367 CA THR A 346 11885 14196 8870 -2888 -71 631 C ATOM 2368 C THR A 346 35.137 18.087 16.204 1.00 76.98 C ANISOU 2368 C THR A 346 10111 12516 6623 -2919 4 576 C ATOM 2369 O THR A 346 35.612 17.885 17.327 1.00 77.71 O ANISOU 2369 O THR A 346 10072 13053 6401 -3167 -119 775 O ATOM 2370 CB THR A 346 36.660 19.341 14.664 1.00 96.37 C ANISOU 2370 CB THR A 346 12782 14640 9193 -3173 -105 313 C ATOM 2371 OG1 THR A 346 35.641 20.262 14.256 1.00106.66 O ANISOU 2371 OG1 THR A 346 14513 15554 10460 -3022 82 -95 O ATOM 2372 CG2 THR A 346 37.697 19.209 13.557 1.00 96.66 C ANISOU 2372 CG2 THR A 346 12629 14575 9521 -3185 -187 439 C ATOM 2373 N LEU A 347 33.850 18.385 16.016 1.00 74.74 N ANISOU 2373 N LEU A 347 10058 11964 6377 -2662 209 331 N ATOM 2374 CA LEU A 347 32.933 18.486 17.147 1.00 75.98 C ANISOU 2374 CA LEU A 347 10320 12349 6200 -2643 323 280 C ATOM 2375 C LEU A 347 32.887 17.184 17.942 1.00 83.25 C ANISOU 2375 C LEU A 347 10812 13645 7173 -2619 247 753 C ATOM 2376 O LEU A 347 32.789 17.205 19.175 1.00 89.89 O ANISOU 2376 O LEU A 347 11651 14898 7606 -2780 238 834 O ATOM 2377 CB LEU A 347 31.546 18.871 16.642 1.00 74.79 C ANISOU 2377 CB LEU A 347 10395 11845 6178 -2307 565 13 C ATOM 2378 CG LEU A 347 30.405 18.836 17.652 1.00 89.28 C ANISOU 2378 CG LEU A 347 12273 13903 7748 -2184 737 1 C ATOM 2379 CD1 LEU A 347 30.655 19.820 18.782 1.00105.06 C ANISOU 2379 CD1 LEU A 347 14602 16178 9140 -2452 758 -258 C ATOM 2380 CD2 LEU A 347 29.078 19.120 16.971 1.00 80.66 C ANISOU 2380 CD2 LEU A 347 11319 12458 6869 -1818 964 -199 C ATOM 2381 N VAL A 348 32.956 16.040 17.250 1.00 95.56 N ANISOU 2381 N VAL A 348 12021 15061 9226 -2418 190 1069 N ATOM 2382 CA VAL A 348 33.109 14.750 17.926 1.00 77.21 C ANISOU 2382 CA VAL A 348 9276 13045 7018 -2414 83 1572 C ATOM 2383 C VAL A 348 34.493 14.639 18.561 1.00 79.73 C ANISOU 2383 C VAL A 348 9409 13768 7118 -2730 -136 1822 C ATOM 2384 O VAL A 348 34.636 14.204 19.712 1.00104.31 O ANISOU 2384 O VAL A 348 12334 17332 9968 -2884 -219 2124 O ATOM 2385 CB VAL A 348 32.864 13.586 16.936 1.00 78.55 C ANISOU 2385 CB VAL A 348 9171 12873 7803 -2114 73 1804 C ATOM 2386 CG1 VAL A 348 32.921 12.227 17.653 1.00 77.19 C ANISOU 2386 CG1 VAL A 348 8584 12953 7792 -2092 -31 2343 C ATOM 2387 CG2 VAL A 348 31.560 13.753 16.161 1.00 86.28 C ANISOU 2387 CG2 VAL A 348 10324 13451 9007 -1833 254 1549 C ATOM 2388 N LEU A 349 35.527 15.054 17.826 1.00 78.48 N ANISOU 2388 N LEU A 349 9283 13489 7046 -2842 -234 1721 N ATOM 2389 CA LEU A 349 36.918 14.703 18.087 1.00 84.03 C ANISOU 2389 CA LEU A 349 9690 14520 7716 -3069 -453 2048 C ATOM 2390 C LEU A 349 37.636 15.693 18.993 1.00 84.22 C ANISOU 2390 C LEU A 349 9890 14942 7167 -3513 -581 1920 C ATOM 2391 O LEU A 349 38.868 15.655 19.088 1.00 86.08 O ANISOU 2391 O LEU A 349 9914 15448 7346 -3754 -777 2136 O ATOM 2392 CB LEU A 349 37.676 14.567 16.768 1.00 96.76 C ANISOU 2392 CB LEU A 349 11197 15829 9739 -2942 -482 2045 C ATOM 2393 CG LEU A 349 37.280 13.353 15.931 1.00 90.36 C ANISOU 2393 CG LEU A 349 10142 14690 9500 -2537 -418 2250 C ATOM 2394 CD1 LEU A 349 38.328 13.088 14.863 1.00 77.88 C ANISOU 2394 CD1 LEU A 349 8379 12967 8243 -2441 -471 2334 C ATOM 2395 CD2 LEU A 349 37.078 12.134 16.820 1.00 80.31 C ANISOU 2395 CD2 LEU A 349 8528 13663 8325 -2468 -486 2720 C ATOM 2396 N CYS A 350 36.900 16.570 19.667 1.00 94.46 N ANISOU 2396 N CYS A 350 11565 16291 8034 -3628 -479 1575 N ATOM 2397 CA CYS A 350 37.513 17.593 20.509 1.00 93.30 C ANISOU 2397 CA CYS A 350 11670 16467 7314 -4068 -601 1371 C ATOM 2398 C CYS A 350 36.764 17.706 21.830 1.00 94.64 C ANISOU 2398 C CYS A 350 11981 16988 6992 -4145 -535 1320 C ATOM 2399 O CYS A 350 35.678 18.289 21.889 1.00 89.14 O ANISOU 2399 O CYS A 350 11634 16075 6161 -3981 -312 955 O ATOM 2400 CB CYS A 350 37.530 18.926 19.791 1.00 89.76 C ANISOU 2400 CB CYS A 350 11689 15619 6795 -4165 -530 851 C ATOM 2401 SG CYS A 350 38.439 20.154 20.672 1.00134.90 S ANISOU 2401 SG CYS A 350 17726 21654 11878 -4757 -729 599 S ATOM 2402 N ASP A 351 37.376 17.192 22.889 1.00107.75 N ANISOU 2402 N ASP A 351 13364 19218 8358 -4393 -725 1691 N ATOM 2403 CA ASP A 351 36.930 17.465 24.244 1.00118.39 C ANISOU 2403 CA ASP A 351 14872 21010 9102 -4570 -703 1623 C ATOM 2404 C ASP A 351 37.497 18.768 24.784 1.00126.43 C ANISOU 2404 C ASP A 351 16317 22187 9534 -5015 -815 1201 C ATOM 2405 O ASP A 351 37.089 19.202 25.865 1.00130.79 O ANISOU 2405 O ASP A 351 17093 22994 9609 -5126 -762 1005 O ATOM 2406 CB ASP A 351 37.321 16.303 25.159 1.00 98.42 C ANISOU 2406 CB ASP A 351 11848 19052 6497 -4647 -871 2247 C ATOM 2407 N SER A 352 38.420 19.401 24.055 1.00118.45 N ANISOU 2407 N SER A 352 15407 20957 8643 -5236 -956 1045 N ATOM 2408 CA SER A 352 38.980 20.686 24.455 1.00122.54 C ANISOU 2408 CA SER A 352 16342 21489 8730 -5663 -1072 623 C ATOM 2409 C SER A 352 38.188 21.871 23.919 1.00119.00 C ANISOU 2409 C SER A 352 16495 20462 8260 -5535 -838 -6 C ATOM 2410 O SER A 352 38.149 22.923 24.566 1.00116.29 O ANISOU 2410 O SER A 352 16548 19994 7645 -5693 -812 -412 O ATOM 2411 CB SER A 352 40.433 20.799 23.986 1.00119.64 C ANISOU 2411 CB SER A 352 15749 21210 8498 -6015 -1358 824 C ATOM 2412 OG SER A 352 41.176 19.642 24.329 1.00131.22 O ANISOU 2412 OG SER A 352 16614 23169 10074 -6059 -1557 1452 O ATOM 2413 N CYS A 353 37.551 21.731 22.762 1.00112.51 N ANISOU 2413 N CYS A 353 15694 19154 7900 -5148 -641 -75 N ATOM 2414 CA CYS A 353 36.849 22.850 22.151 1.00 97.92 C ANISOU 2414 CA CYS A 353 14383 16739 6081 -5006 -429 -622 C ATOM 2415 C CYS A 353 35.511 23.118 22.833 1.00 96.22 C ANISOU 2415 C CYS A 353 14476 16505 5580 -4738 -150 -912 C ATOM 2416 O CYS A 353 34.900 22.231 23.436 1.00 93.03 O ANISOU 2416 O CYS A 353 13789 16423 5136 -4531 -63 -632 O ATOM 2417 CB CYS A 353 36.595 22.582 20.668 1.00 96.92 C ANISOU 2417 CB CYS A 353 14127 16096 6604 -4639 -308 -566 C ATOM 2418 SG CYS A 353 37.954 21.871 19.710 1.00121.28 S ANISOU 2418 SG CYS A 353 16708 19226 10145 -4753 -546 -119 S ATOM 2419 N ASN A 354 35.036 24.350 22.676 1.00105.11 N ANISOU 2419 N ASN A 354 16132 17175 6629 -4670 8 -1436 N ATOM 2420 CA ASN A 354 33.717 24.732 23.160 1.00100.53 C ANISOU 2420 CA ASN A 354 15829 16457 5912 -4296 315 -1728 C ATOM 2421 C ASN A 354 32.643 24.158 22.242 1.00104.87 C ANISOU 2421 C ASN A 354 16252 16772 6822 -3838 566 -1640 C ATOM 2422 O ASN A 354 32.703 24.328 21.020 1.00128.72 O ANISOU 2422 O ASN A 354 19281 19325 10301 -3699 578 -1675 O ATOM 2423 CB ASN A 354 33.623 26.255 23.222 1.00 98.86 C ANISOU 2423 CB ASN A 354 16170 15758 5633 -4297 386 -2257 C ATOM 2424 CG ASN A 354 32.421 26.739 23.992 1.00104.08 C ANISOU 2424 CG ASN A 354 17108 16371 6066 -3934 666 -2553 C ATOM 2425 OD1 ASN A 354 31.320 26.210 23.853 1.00108.45 O ANISOU 2425 OD1 ASN A 354 17548 16964 6693 -3539 917 -2477 O ATOM 2426 ND2 ASN A 354 32.626 27.761 24.812 1.00117.96 N ANISOU 2426 ND2 ASN A 354 19225 18058 7536 -4063 627 -2885 N ATOM 2427 N GLN A 355 31.660 23.474 22.830 1.00 91.01 N ANISOU 2427 N GLN A 355 14295 15286 4999 -3543 752 -1467 N ATOM 2428 CA GLN A 355 30.633 22.818 22.028 1.00 94.93 C ANISOU 2428 CA GLN A 355 14536 15530 6004 -3065 948 -1286 C ATOM 2429 C GLN A 355 29.549 23.785 21.568 1.00 94.36 C ANISOU 2429 C GLN A 355 14882 14998 5973 -2719 1248 -1724 C ATOM 2430 O GLN A 355 28.962 23.584 20.497 1.00101.36 O ANISOU 2430 O GLN A 355 15654 15510 7348 -2395 1349 -1667 O ATOM 2431 CB GLN A 355 30.008 21.666 22.818 1.00 87.48 C ANISOU 2431 CB GLN A 355 13170 15060 5008 -2912 1015 -869 C ATOM 2432 CG GLN A 355 31.006 20.625 23.309 1.00 96.34 C ANISOU 2432 CG GLN A 355 13845 16640 6119 -3204 729 -371 C ATOM 2433 CD GLN A 355 30.331 19.343 23.766 1.00122.07 C ANISOU 2433 CD GLN A 355 16634 20229 9517 -3000 789 123 C ATOM 2434 OE1 GLN A 355 29.472 18.800 23.071 1.00119.52 O ANISOU 2434 OE1 GLN A 355 16124 19641 9647 -2654 927 257 O ATOM 2435 NE2 GLN A 355 30.717 18.856 24.940 1.00110.95 N ANISOU 2435 NE2 GLN A 355 15031 19410 7717 -3235 672 414 N ATOM 2436 N THR A 356 29.276 24.833 22.349 1.00 91.20 N ANISOU 2436 N THR A 356 14970 14618 5065 -2773 1389 -2162 N ATOM 2437 CA THR A 356 28.188 25.752 22.027 1.00 91.88 C ANISOU 2437 CA THR A 356 15404 14259 5247 -2353 1682 -2532 C ATOM 2438 C THR A 356 28.457 26.492 20.724 1.00 89.23 C ANISOU 2438 C THR A 356 15305 13293 5304 -2322 1642 -2736 C ATOM 2439 O THR A 356 27.712 26.351 19.748 1.00 99.62 O ANISOU 2439 O THR A 356 16556 14305 6991 -1986 1802 -2699 O ATOM 2440 CB THR A 356 27.986 26.744 23.173 1.00118.82 C ANISOU 2440 CB THR A 356 19154 17707 8286 -2295 1744 -2867 C ATOM 2441 OG1 THR A 356 27.668 26.031 24.374 1.00100.56 O ANISOU 2441 OG1 THR A 356 16611 15998 5601 -2289 1801 -2654 O ATOM 2442 CG2 THR A 356 26.859 27.713 22.843 1.00118.53 C ANISOU 2442 CG2 THR A 356 19423 17227 8385 -1809 2032 -3207 C ATOM 2443 N THR A 357 29.513 27.309 20.702 1.00103.04 N ANISOU 2443 N THR A 357 17287 14836 7027 -2654 1412 -2908 N ATOM 2444 CA THR A 357 29.874 28.032 19.487 1.00110.33 C ANISOU 2444 CA THR A 357 18403 15196 8321 -2668 1352 -3043 C ATOM 2445 C THR A 357 30.122 27.083 18.324 1.00 83.46 C ANISOU 2445 C THR A 357 14694 11771 5248 -2687 1294 -2752 C ATOM 2446 O THR A 357 29.806 27.411 17.175 1.00 83.98 O ANISOU 2446 O THR A 357 14833 11382 5695 -2459 1370 -2808 O ATOM 2447 CB THR A 357 31.112 28.888 19.740 1.00106.99 C ANISOU 2447 CB THR A 357 18195 14670 7785 -3117 1090 -3179 C ATOM 2448 OG1 THR A 357 32.191 28.042 20.156 1.00107.02 O ANISOU 2448 OG1 THR A 357 17891 15164 7609 -3555 830 -2884 O ATOM 2449 CG2 THR A 357 30.833 29.912 20.829 1.00 98.21 C ANISOU 2449 CG2 THR A 357 17433 13518 6363 -3076 1152 -3513 C ATOM 2450 N LEU A 358 30.677 25.901 18.605 1.00 82.02 N ANISOU 2450 N LEU A 358 14012 12030 5120 -2836 1112 -2329 N ATOM 2451 CA LEU A 358 30.877 24.901 17.563 1.00 85.10 C ANISOU 2451 CA LEU A 358 13936 12357 6040 -2701 1015 -1945 C ATOM 2452 C LEU A 358 29.551 24.431 16.984 1.00 75.96 C ANISOU 2452 C LEU A 358 12618 11018 5224 -2196 1241 -1863 C ATOM 2453 O LEU A 358 29.500 23.980 15.834 1.00 73.55 O ANISOU 2453 O LEU A 358 12100 10470 5376 -2024 1210 -1703 O ATOM 2454 CB LEU A 358 31.665 23.719 18.122 1.00 80.58 C ANISOU 2454 CB LEU A 358 12882 12289 5444 -2924 797 -1507 C ATOM 2455 CG LEU A 358 32.701 23.069 17.209 1.00 76.77 C ANISOU 2455 CG LEU A 358 12051 11770 5349 -3043 580 -1198 C ATOM 2456 CD1 LEU A 358 33.633 24.125 16.645 1.00 81.13 C ANISOU 2456 CD1 LEU A 358 12906 12061 5859 -3342 463 -1432 C ATOM 2457 CD2 LEU A 358 33.482 22.030 17.990 1.00 78.24 C ANISOU 2457 CD2 LEU A 358 11808 12482 5437 -3265 377 -781 C ATOM 2458 N GLN A 359 28.470 24.522 17.762 1.00 77.51 N ANISOU 2458 N GLN A 359 12902 11358 5189 -1962 1467 -1965 N ATOM 2459 CA GLN A 359 27.147 24.207 17.239 1.00 76.43 C ANISOU 2459 CA GLN A 359 12623 11064 5355 -1496 1687 -1896 C ATOM 2460 C GLN A 359 26.590 25.365 16.422 1.00 83.00 C ANISOU 2460 C GLN A 359 13861 11373 6303 -1258 1857 -2252 C ATOM 2461 O GLN A 359 25.940 25.145 15.393 1.00 82.18 O ANISOU 2461 O GLN A 359 13612 11007 6604 -959 1921 -2157 O ATOM 2462 CB GLN A 359 26.198 23.848 18.380 1.00 78.93 C ANISOU 2462 CB GLN A 359 12827 11780 5381 -1325 1880 -1819 C ATOM 2463 CG GLN A 359 24.918 23.177 17.926 1.00 90.01 C ANISOU 2463 CG GLN A 359 13915 13152 7132 -909 2049 -1596 C ATOM 2464 CD GLN A 359 25.177 21.845 17.255 1.00104.40 C ANISOU 2464 CD GLN A 359 15241 15011 9418 -938 1847 -1157 C ATOM 2465 OE1 GLN A 359 26.103 21.121 17.623 1.00118.65 O ANISOU 2465 OE1 GLN A 359 16820 17069 11193 -1219 1634 -909 O ATOM 2466 NE2 GLN A 359 24.364 21.516 16.259 1.00104.60 N ANISOU 2466 NE2 GLN A 359 15097 14774 9871 -642 1907 -1061 N ATOM 2467 N MET A 360 26.837 26.603 16.863 1.00 91.51 N ANISOU 2467 N MET A 360 15457 12284 7029 -1394 1919 -2658 N ATOM 2468 CA MET A 360 26.432 27.764 16.078 1.00 78.47 C ANISOU 2468 CA MET A 360 14224 10086 5505 -1191 2061 -2980 C ATOM 2469 C MET A 360 27.089 27.750 14.705 1.00 75.62 C ANISOU 2469 C MET A 360 13779 9389 5563 -1281 1882 -2863 C ATOM 2470 O MET A 360 26.444 28.063 13.697 1.00 78.63 O ANISOU 2470 O MET A 360 14211 9408 6256 -974 1991 -2892 O ATOM 2471 CB MET A 360 26.783 29.056 16.818 1.00 83.41 C ANISOU 2471 CB MET A 360 15202 10573 5918 -1311 1999 -3280 C ATOM 2472 CG MET A 360 26.305 29.121 18.261 1.00145.65 C ANISOU 2472 CG MET A 360 23135 18826 13377 -1241 2120 -3394 C ATOM 2473 SD MET A 360 26.439 30.785 18.953 1.00136.00 S ANISOU 2473 SD MET A 360 22381 17318 11973 -1257 2102 -3815 S ATOM 2474 CE MET A 360 28.148 31.181 18.589 1.00136.32 C ANISOU 2474 CE MET A 360 22558 17182 12055 -1860 1744 -3812 C ATOM 2475 N LEU A 361 28.376 27.388 14.646 1.00 75.22 N ANISOU 2475 N LEU A 361 13582 9489 5509 -1693 1612 -2711 N ATOM 2476 CA LEU A 361 29.079 27.327 13.367 1.00 70.72 C ANISOU 2476 CA LEU A 361 12902 8666 5303 -1781 1455 -2579 C ATOM 2477 C LEU A 361 28.408 26.347 12.414 1.00 80.59 C ANISOU 2477 C LEU A 361 13743 9887 6991 -1430 1492 -2298 C ATOM 2478 O LEU A 361 28.262 26.632 11.220 1.00 79.92 O ANISOU 2478 O LEU A 361 13706 9460 7202 -1274 1507 -2312 O ATOM 2479 CB LEU A 361 30.541 26.940 13.587 1.00 70.83 C ANISOU 2479 CB LEU A 361 12734 8952 5226 -2250 1176 -2403 C ATOM 2480 CG LEU A 361 31.404 27.935 14.360 1.00 75.07 C ANISOU 2480 CG LEU A 361 13666 9505 5352 -2698 1066 -2663 C ATOM 2481 CD1 LEU A 361 32.805 27.381 14.546 1.00 75.09 C ANISOU 2481 CD1 LEU A 361 13368 9860 5301 -3137 778 -2397 C ATOM 2482 CD2 LEU A 361 31.441 29.269 13.636 1.00 76.28 C ANISOU 2482 CD2 LEU A 361 14228 9119 5636 -2687 1103 -2915 C ATOM 2483 N LEU A 362 27.999 25.181 12.923 1.00 80.91 N ANISOU 2483 N LEU A 362 13387 10284 7072 -1323 1492 -2034 N ATOM 2484 CA LEU A 362 27.221 24.251 12.112 1.00 67.38 C ANISOU 2484 CA LEU A 362 11317 8524 5759 -1000 1525 -1794 C ATOM 2485 C LEU A 362 25.919 24.893 11.653 1.00 65.55 C ANISOU 2485 C LEU A 362 11272 8008 5627 -611 1753 -1963 C ATOM 2486 O LEU A 362 25.569 24.836 10.469 1.00 66.90 O ANISOU 2486 O LEU A 362 11374 7918 6127 -413 1749 -1914 O ATOM 2487 CB LEU A 362 26.937 22.971 12.895 1.00 67.80 C ANISOU 2487 CB LEU A 362 10954 8992 5816 -979 1494 -1481 C ATOM 2488 CG LEU A 362 28.091 21.994 13.095 1.00 68.28 C ANISOU 2488 CG LEU A 362 10695 9322 5929 -1263 1258 -1192 C ATOM 2489 CD1 LEU A 362 27.637 20.833 13.958 1.00 93.14 C ANISOU 2489 CD1 LEU A 362 13475 12844 9071 -1213 1255 -876 C ATOM 2490 CD2 LEU A 362 28.593 21.500 11.751 1.00 66.20 C ANISOU 2490 CD2 LEU A 362 10251 8825 6076 -1218 1129 -1065 C ATOM 2491 N GLU A 363 25.199 25.533 12.580 1.00 67.64 N ANISOU 2491 N GLU A 363 11774 8336 5590 -487 1957 -2162 N ATOM 2492 CA GLU A 363 23.928 26.171 12.252 1.00 67.48 C ANISOU 2492 CA GLU A 363 11910 8080 5649 -76 2201 -2303 C ATOM 2493 C GLU A 363 24.071 27.243 11.179 1.00 75.64 C ANISOU 2493 C GLU A 363 13289 8616 6835 -10 2213 -2509 C ATOM 2494 O GLU A 363 23.066 27.638 10.580 1.00 93.34 O ANISOU 2494 O GLU A 363 15581 10633 9251 354 2371 -2542 O ATOM 2495 CB GLU A 363 23.306 26.777 13.512 1.00 71.02 C ANISOU 2495 CB GLU A 363 12605 8687 5691 38 2438 -2522 C ATOM 2496 N ILE A 364 25.286 27.725 10.931 1.00 79.22 N ANISOU 2496 N ILE A 364 13961 8913 7228 -358 2046 -2613 N ATOM 2497 CA ILE A 364 25.525 28.662 9.838 1.00 65.99 C ANISOU 2497 CA ILE A 364 12521 6800 5754 -335 2006 -2709 C ATOM 2498 C ILE A 364 25.979 27.935 8.579 1.00 62.95 C ANISOU 2498 C ILE A 364 11865 6366 5685 -375 1853 -2484 C ATOM 2499 O ILE A 364 25.509 28.236 7.480 1.00 90.31 O ANISOU 2499 O ILE A 364 15363 9555 9396 -146 1893 -2462 O ATOM 2500 CB ILE A 364 26.553 29.728 10.270 1.00 69.87 C ANISOU 2500 CB ILE A 364 13299 7174 6073 -684 1868 -2869 C ATOM 2501 CG1 ILE A 364 26.067 30.491 11.504 1.00 76.25 C ANISOU 2501 CG1 ILE A 364 14319 8036 6615 -607 1981 -3082 C ATOM 2502 CG2 ILE A 364 26.840 30.695 9.128 1.00 68.95 C ANISOU 2502 CG2 ILE A 364 13312 6664 6221 -676 1788 -2855 C ATOM 2503 CD1 ILE A 364 27.026 31.575 11.959 1.00 77.22 C ANISOU 2503 CD1 ILE A 364 14753 8013 6575 -951 1844 -3260 C ATOM 2504 N PHE A 365 26.890 26.967 8.724 1.00 73.38 N ANISOU 2504 N PHE A 365 12874 7983 7023 -643 1661 -2282 N ATOM 2505 CA PHE A 365 27.476 26.312 7.559 1.00 63.07 C ANISOU 2505 CA PHE A 365 11302 6650 6012 -685 1503 -2075 C ATOM 2506 C PHE A 365 26.468 25.440 6.823 1.00 64.29 C ANISOU 2506 C PHE A 365 11144 6811 6473 -337 1538 -1901 C ATOM 2507 O PHE A 365 26.649 25.166 5.630 1.00 81.70 O ANISOU 2507 O PHE A 365 13233 8890 8919 -275 1456 -1808 O ATOM 2508 CB PHE A 365 28.686 25.477 7.978 1.00 62.48 C ANISOU 2508 CB PHE A 365 10962 6897 5880 -1017 1310 -1895 C ATOM 2509 CG PHE A 365 29.819 26.285 8.550 1.00 64.15 C ANISOU 2509 CG PHE A 365 11431 7132 5809 -1424 1220 -2024 C ATOM 2510 CD1 PHE A 365 29.974 27.626 8.230 1.00 79.78 C ANISOU 2510 CD1 PHE A 365 13847 8763 7701 -1517 1265 -2263 C ATOM 2511 CD2 PHE A 365 30.735 25.698 9.406 1.00 63.73 C ANISOU 2511 CD2 PHE A 365 11178 7449 5587 -1731 1072 -1886 C ATOM 2512 CE1 PHE A 365 31.021 28.363 8.758 1.00 83.47 C ANISOU 2512 CE1 PHE A 365 14559 9241 7916 -1942 1153 -2380 C ATOM 2513 CE2 PHE A 365 31.782 26.427 9.936 1.00 75.70 C ANISOU 2513 CE2 PHE A 365 12910 9021 6832 -2146 957 -1990 C ATOM 2514 CZ PHE A 365 31.926 27.761 9.612 1.00 75.84 C ANISOU 2514 CZ PHE A 365 13374 8679 6763 -2268 992 -2247 C ATOM 2515 N VAL A 366 25.410 24.991 7.508 1.00 63.09 N ANISOU 2515 N VAL A 366 10848 6824 6298 -125 1652 -1850 N ATOM 2516 CA VAL A 366 24.392 24.154 6.873 1.00 56.67 C ANISOU 2516 CA VAL A 366 9725 6033 5775 164 1663 -1671 C ATOM 2517 C VAL A 366 23.808 24.834 5.646 1.00 66.08 C ANISOU 2517 C VAL A 366 11062 6900 7145 404 1716 -1744 C ATOM 2518 O VAL A 366 23.401 24.166 4.689 1.00 91.01 O ANISOU 2518 O VAL A 366 13985 10028 10565 544 1636 -1602 O ATOM 2519 CB VAL A 366 23.283 23.794 7.885 1.00 58.93 C ANISOU 2519 CB VAL A 366 9861 6555 5973 344 1807 -1601 C ATOM 2520 CG1 VAL A 366 23.770 22.749 8.860 1.00 68.35 C ANISOU 2520 CG1 VAL A 366 10783 8107 7079 130 1710 -1411 C ATOM 2521 CG2 VAL A 366 22.823 25.034 8.620 1.00 72.07 C ANISOU 2521 CG2 VAL A 366 11899 8135 7349 453 2029 -1857 C ATOM 2522 N TRP A 367 23.757 26.165 5.647 1.00 62.42 N ANISOU 2522 N TRP A 367 10997 6180 6539 448 1840 -1962 N ATOM 2523 CA TRP A 367 23.195 26.908 4.529 1.00 54.71 C ANISOU 2523 CA TRP A 367 10175 4890 5721 687 1897 -2002 C ATOM 2524 C TRP A 367 24.194 27.107 3.400 1.00 67.45 C ANISOU 2524 C TRP A 367 11862 6330 7434 507 1747 -1981 C ATOM 2525 O TRP A 367 23.786 27.234 2.237 1.00 72.88 O ANISOU 2525 O TRP A 367 12490 6885 8314 682 1711 -1897 O ATOM 2526 CB TRP A 367 22.662 28.253 5.021 1.00 58.10 C ANISOU 2526 CB TRP A 367 10893 5154 6029 825 2040 -2159 C ATOM 2527 CG TRP A 367 21.495 28.084 5.932 1.00 59.88 C ANISOU 2527 CG TRP A 367 11046 5542 6164 1098 2243 -2177 C ATOM 2528 CD1 TRP A 367 21.504 28.122 7.294 1.00 62.15 C ANISOU 2528 CD1 TRP A 367 11437 6014 6164 1033 2365 -2303 C ATOM 2529 CD2 TRP A 367 20.144 27.817 5.546 1.00 61.85 C ANISOU 2529 CD2 TRP A 367 11079 5831 6588 1481 2356 -2042 C ATOM 2530 NE1 TRP A 367 20.237 27.910 7.781 1.00 63.58 N ANISOU 2530 NE1 TRP A 367 11473 6356 6328 1372 2571 -2250 N ATOM 2531 CE2 TRP A 367 19.384 27.719 6.726 1.00 62.22 C ANISOU 2531 CE2 TRP A 367 11094 6095 6451 1650 2569 -2082 C ATOM 2532 CE3 TRP A 367 19.501 27.659 4.314 1.00 58.41 C ANISOU 2532 CE3 TRP A 367 10463 5303 6429 1689 2294 -1881 C ATOM 2533 CZ2 TRP A 367 18.014 27.470 6.713 1.00 63.16 C ANISOU 2533 CZ2 TRP A 367 10978 6344 6678 2028 2732 -1940 C ATOM 2534 CZ3 TRP A 367 18.141 27.412 4.304 1.00 59.35 C ANISOU 2534 CZ3 TRP A 367 10367 5532 6651 2046 2434 -1754 C ATOM 2535 CH2 TRP A 367 17.413 27.319 5.494 1.00 61.70 C ANISOU 2535 CH2 TRP A 367 10604 6052 6787 2215 2653 -1770 C ATOM 2536 N ILE A 368 25.491 27.131 3.711 1.00 53.20 N ANISOU 2536 N ILE A 368 10126 4587 5498 151 1640 -2015 N ATOM 2537 CA ILE A 368 26.503 27.075 2.661 1.00 60.62 C ANISOU 2537 CA ILE A 368 11031 5465 6538 -25 1498 -1936 C ATOM 2538 C ILE A 368 26.402 25.753 1.911 1.00 67.62 C ANISOU 2538 C ILE A 368 11515 6529 7647 81 1386 -1744 C ATOM 2539 O ILE A 368 26.397 25.718 0.675 1.00 47.73 O ANISOU 2539 O ILE A 368 8956 3906 5273 180 1338 -1687 O ATOM 2540 CB ILE A 368 27.910 27.282 3.249 1.00 54.46 C ANISOU 2540 CB ILE A 368 10339 4783 5570 -440 1400 -1970 C ATOM 2541 CG1 ILE A 368 27.974 28.587 4.044 1.00 56.04 C ANISOU 2541 CG1 ILE A 368 10980 4778 5534 -576 1490 -2199 C ATOM 2542 CG2 ILE A 368 28.953 27.290 2.137 1.00 51.64 C ANISOU 2542 CG2 ILE A 368 9922 4390 5307 -604 1282 -1863 C ATOM 2543 CD1 ILE A 368 29.339 28.877 4.620 1.00 57.57 C ANISOU 2543 CD1 ILE A 368 11278 5069 5526 -1034 1364 -2235 C ATOM 2544 N GLY A 369 26.312 24.645 2.650 1.00 64.74 N ANISOU 2544 N GLY A 369 10864 6429 7305 59 1341 -1643 N ATOM 2545 CA GLY A 369 26.107 23.357 2.009 1.00 52.00 C ANISOU 2545 CA GLY A 369 8904 4929 5925 169 1235 -1481 C ATOM 2546 C GLY A 369 24.773 23.271 1.295 1.00 47.42 C ANISOU 2546 C GLY A 369 8263 4242 5514 478 1274 -1459 C ATOM 2547 O GLY A 369 24.676 22.695 0.208 1.00 45.83 O ANISOU 2547 O GLY A 369 7920 4007 5487 567 1177 -1395 O ATOM 2548 N TYR A 370 23.727 23.851 1.892 1.00 57.30 N ANISOU 2548 N TYR A 370 9615 5458 6698 649 1418 -1510 N ATOM 2549 CA TYR A 370 22.402 23.819 1.277 1.00 48.76 C ANISOU 2549 CA TYR A 370 8436 4317 5772 948 1456 -1451 C ATOM 2550 C TYR A 370 22.401 24.532 -0.068 1.00 63.41 C ANISOU 2550 C TYR A 370 10455 5946 7692 1051 1433 -1486 C ATOM 2551 O TYR A 370 21.903 23.998 -1.066 1.00 67.71 O ANISOU 2551 O TYR A 370 10827 6498 8403 1174 1333 -1396 O ATOM 2552 CB TYR A 370 21.371 24.447 2.214 1.00 49.80 C ANISOU 2552 CB TYR A 370 8655 4471 5796 1139 1653 -1494 C ATOM 2553 CG TYR A 370 20.824 23.515 3.271 1.00 51.81 C ANISOU 2553 CG TYR A 370 8626 5012 6049 1143 1677 -1370 C ATOM 2554 CD1 TYR A 370 20.895 22.135 3.122 1.00 51.76 C ANISOU 2554 CD1 TYR A 370 8276 5167 6224 1047 1509 -1190 C ATOM 2555 CD2 TYR A 370 20.230 24.020 4.419 1.00 62.29 C ANISOU 2555 CD2 TYR A 370 10039 6441 7188 1249 1875 -1426 C ATOM 2556 CE1 TYR A 370 20.391 21.286 4.093 1.00 54.27 C ANISOU 2556 CE1 TYR A 370 8328 5737 6554 1032 1525 -1032 C ATOM 2557 CE2 TYR A 370 19.726 23.183 5.391 1.00 56.57 C ANISOU 2557 CE2 TYR A 370 9038 6016 6439 1247 1908 -1277 C ATOM 2558 CZ TYR A 370 19.808 21.818 5.224 1.00 63.05 C ANISOU 2558 CZ TYR A 370 9504 6992 7461 1127 1726 -1061 C ATOM 2559 OH TYR A 370 19.306 20.981 6.192 1.00 63.47 O ANISOU 2559 OH TYR A 370 9274 7336 7505 1106 1752 -870 O ATOM 2560 N VAL A 371 22.955 25.746 -0.116 1.00 59.97 N ANISOU 2560 N VAL A 371 10362 5307 7118 982 1512 -1610 N ATOM 2561 CA VAL A 371 23.011 26.473 -1.378 1.00 48.32 C ANISOU 2561 CA VAL A 371 8995 3662 5703 1046 1465 -1579 C ATOM 2562 C VAL A 371 24.001 25.834 -2.342 1.00 50.01 C ANISOU 2562 C VAL A 371 9137 3908 5958 895 1332 -1543 C ATOM 2563 O VAL A 371 23.870 25.999 -3.561 1.00 62.55 O ANISOU 2563 O VAL A 371 10711 5442 7612 987 1270 -1480 O ATOM 2564 CB VAL A 371 23.351 27.958 -1.135 1.00 81.24 C ANISOU 2564 CB VAL A 371 13439 7669 9759 957 1521 -1640 C ATOM 2565 CG1 VAL A 371 24.825 28.131 -0.800 1.00 77.14 C ANISOU 2565 CG1 VAL A 371 13075 7134 9100 606 1475 -1713 C ATOM 2566 CG2 VAL A 371 22.958 28.800 -2.341 1.00 51.48 C ANISOU 2566 CG2 VAL A 371 9737 3744 6079 1104 1500 -1548 C ATOM 2567 N SER A 372 24.985 25.093 -1.827 1.00 53.90 N ANISOU 2567 N SER A 372 9501 4567 6412 660 1260 -1539 N ATOM 2568 CA SER A 372 25.894 24.362 -2.703 1.00 47.09 C ANISOU 2568 CA SER A 372 8484 3802 5606 554 1134 -1479 C ATOM 2569 C SER A 372 25.167 23.239 -3.427 1.00 48.02 C ANISOU 2569 C SER A 372 8343 4002 5902 735 1035 -1415 C ATOM 2570 O SER A 372 25.344 23.055 -4.637 1.00 51.78 O ANISOU 2570 O SER A 372 8793 4466 6416 790 964 -1402 O ATOM 2571 CB SER A 372 27.071 23.811 -1.899 1.00 76.35 C ANISOU 2571 CB SER A 372 12084 7680 9247 294 1088 -1459 C ATOM 2572 OG SER A 372 27.946 23.052 -2.716 1.00 61.43 O ANISOU 2572 OG SER A 372 10022 5896 7423 241 995 -1396 O ATOM 2573 N SER A 373 24.337 22.483 -2.708 1.00 58.23 N ANISOU 2573 N SER A 373 9447 5386 7292 814 1022 -1372 N ATOM 2574 CA SER A 373 23.572 21.415 -3.336 1.00 55.90 C ANISOU 2574 CA SER A 373 8916 5143 7181 946 903 -1310 C ATOM 2575 C SER A 373 22.404 21.946 -4.158 1.00 44.92 C ANISOU 2575 C SER A 373 7568 3669 5831 1163 906 -1292 C ATOM 2576 O SER A 373 21.984 21.289 -5.116 1.00 57.96 O ANISOU 2576 O SER A 373 9091 5343 7587 1238 774 -1267 O ATOM 2577 CB SER A 373 23.059 20.442 -2.275 1.00 46.09 C ANISOU 2577 CB SER A 373 7440 4030 6044 926 878 -1223 C ATOM 2578 OG SER A 373 24.129 19.778 -1.625 1.00 52.39 O ANISOU 2578 OG SER A 373 8152 4924 6831 740 843 -1196 O ATOM 2579 N GLY A 374 21.877 23.123 -3.815 1.00 59.20 N ANISOU 2579 N GLY A 374 9560 5379 7552 1271 1049 -1304 N ATOM 2580 CA GLY A 374 20.654 23.587 -4.452 1.00 64.84 C ANISOU 2580 CA GLY A 374 10264 6045 8327 1515 1060 -1237 C ATOM 2581 C GLY A 374 20.865 24.039 -5.885 1.00 67.44 C ANISOU 2581 C GLY A 374 10708 6290 8628 1563 988 -1230 C ATOM 2582 O GLY A 374 20.104 23.669 -6.784 1.00 90.04 O ANISOU 2582 O GLY A 374 13430 9212 11567 1686 871 -1158 O ATOM 2583 N VAL A 375 21.898 24.851 -6.117 1.00 53.14 N ANISOU 2583 N VAL A 375 9142 4357 6690 1448 1048 -1287 N ATOM 2584 CA VAL A 375 22.146 25.419 -7.438 1.00 54.74 C ANISOU 2584 CA VAL A 375 9468 4494 6835 1486 1005 -1246 C ATOM 2585 C VAL A 375 23.095 24.571 -8.271 1.00 45.61 C ANISOU 2585 C VAL A 375 8214 3469 5645 1348 882 -1276 C ATOM 2586 O VAL A 375 23.450 24.974 -9.387 1.00 70.73 O ANISOU 2586 O VAL A 375 11487 6647 8740 1358 854 -1239 O ATOM 2587 CB VAL A 375 22.682 26.862 -7.320 1.00 60.61 C ANISOU 2587 CB VAL A 375 10519 5035 7474 1426 1131 -1245 C ATOM 2588 CG1 VAL A 375 21.726 27.717 -6.496 1.00 55.87 C ANISOU 2588 CG1 VAL A 375 9968 4346 6913 1567 1241 -1219 C ATOM 2589 CG2 VAL A 375 24.077 26.870 -6.708 1.00 63.38 C ANISOU 2589 CG2 VAL A 375 10958 5394 7731 1133 1156 -1326 C ATOM 2590 N ASN A 376 23.503 23.404 -7.774 1.00 43.34 N ANISOU 2590 N ASN A 376 7742 3303 5422 1240 819 -1331 N ATOM 2591 CA ASN A 376 24.490 22.596 -8.490 1.00 45.03 C ANISOU 2591 CA ASN A 376 7876 3624 5608 1145 736 -1376 C ATOM 2592 C ASN A 376 23.996 22.083 -9.839 1.00 73.08 C ANISOU 2592 C ASN A 376 11360 7244 9163 1271 605 -1387 C ATOM 2593 O ASN A 376 24.723 22.250 -10.835 1.00 76.05 O ANISOU 2593 O ASN A 376 11810 7676 9410 1253 601 -1401 O ATOM 2594 CB ASN A 376 24.960 21.449 -7.588 1.00 51.50 C ANISOU 2594 CB ASN A 376 8513 4525 6528 1037 701 -1409 C ATOM 2595 CG ASN A 376 25.672 20.358 -8.357 1.00 74.29 C ANISOU 2595 CG ASN A 376 11280 7502 9444 1025 608 -1464 C ATOM 2596 OD1 ASN A 376 25.094 19.308 -8.637 1.00 94.49 O ANISOU 2596 OD1 ASN A 376 13700 10070 12131 1098 487 -1502 O ATOM 2597 ND2 ASN A 376 26.931 20.600 -8.706 1.00 49.35 N ANISOU 2597 ND2 ASN A 376 8177 4407 6167 933 666 -1469 N ATOM 2598 N PRO A 377 22.817 21.453 -9.960 1.00 75.00 N ANISOU 2598 N PRO A 377 11459 7512 9526 1381 489 -1376 N ATOM 2599 CA PRO A 377 22.433 20.915 -11.279 1.00 69.59 C ANISOU 2599 CA PRO A 377 10725 6908 8809 1457 333 -1414 C ATOM 2600 C PRO A 377 22.233 21.992 -12.330 1.00 78.76 C ANISOU 2600 C PRO A 377 12035 8083 9807 1552 350 -1335 C ATOM 2601 O PRO A 377 22.644 21.810 -13.482 1.00 65.28 O ANISOU 2601 O PRO A 377 10369 6475 7959 1559 284 -1381 O ATOM 2602 CB PRO A 377 21.128 20.156 -10.988 1.00 53.22 C ANISOU 2602 CB PRO A 377 8455 4854 6912 1510 197 -1380 C ATOM 2603 CG PRO A 377 21.088 19.980 -9.510 1.00 59.56 C ANISOU 2603 CG PRO A 377 9173 5613 7846 1449 290 -1339 C ATOM 2604 CD PRO A 377 21.784 21.175 -8.948 1.00 52.94 C ANISOU 2604 CD PRO A 377 8525 4704 6884 1425 485 -1320 C ATOM 2605 N LEU A 378 21.605 23.111 -11.961 1.00 84.01 N ANISOU 2605 N LEU A 378 12786 8652 10481 1641 444 -1209 N ATOM 2606 CA LEU A 378 21.409 24.207 -12.904 1.00 68.78 C ANISOU 2606 CA LEU A 378 11005 6704 8424 1743 466 -1087 C ATOM 2607 C LEU A 378 22.744 24.733 -13.416 1.00 49.50 C ANISOU 2607 C LEU A 378 8736 4257 5814 1624 551 -1094 C ATOM 2608 O LEU A 378 22.945 24.881 -14.627 1.00 51.25 O ANISOU 2608 O LEU A 378 9001 4593 5880 1651 496 -1048 O ATOM 2609 CB LEU A 378 20.606 25.323 -12.237 1.00 53.50 C ANISOU 2609 CB LEU A 378 9157 4608 6564 1881 587 -960 C ATOM 2610 CG LEU A 378 20.393 26.592 -13.060 1.00 51.68 C ANISOU 2610 CG LEU A 378 9102 4292 6242 2007 632 -793 C ATOM 2611 CD1 LEU A 378 19.487 26.309 -14.246 1.00 54.35 C ANISOU 2611 CD1 LEU A 378 9298 4815 6538 2143 454 -682 C ATOM 2612 CD2 LEU A 378 19.825 27.699 -12.190 1.00 54.76 C ANISOU 2612 CD2 LEU A 378 9630 4449 6727 2149 798 -712 C ATOM 2613 N VAL A 379 23.673 25.018 -12.499 1.00 53.46 N ANISOU 2613 N VAL A 379 9323 4661 6327 1474 679 -1135 N ATOM 2614 CA VAL A 379 25.003 25.484 -12.887 1.00 48.54 C ANISOU 2614 CA VAL A 379 8821 4061 5559 1320 756 -1112 C ATOM 2615 C VAL A 379 25.662 24.494 -13.838 1.00 53.60 C ANISOU 2615 C VAL A 379 9341 4930 6095 1302 680 -1189 C ATOM 2616 O VAL A 379 26.284 24.884 -14.834 1.00 58.05 O ANISOU 2616 O VAL A 379 9973 5601 6484 1281 705 -1119 O ATOM 2617 CB VAL A 379 25.863 25.731 -11.632 1.00 47.29 C ANISOU 2617 CB VAL A 379 8724 3806 5440 1126 864 -1154 C ATOM 2618 CG1 VAL A 379 27.341 25.800 -11.994 1.00 49.10 C ANISOU 2618 CG1 VAL A 379 8969 4147 5539 934 910 -1128 C ATOM 2619 CG2 VAL A 379 25.422 27.009 -10.938 1.00 47.79 C ANISOU 2619 CG2 VAL A 379 9007 3616 5536 1136 967 -1095 C ATOM 2620 N TYR A 380 25.513 23.196 -13.564 1.00 63.78 N ANISOU 2620 N TYR A 380 10457 6291 7485 1323 593 -1329 N ATOM 2621 CA TYR A 380 26.141 22.186 -14.410 1.00 55.57 C ANISOU 2621 CA TYR A 380 9331 5427 6357 1338 536 -1445 C ATOM 2622 C TYR A 380 25.504 22.144 -15.795 1.00 67.73 C ANISOU 2622 C TYR A 380 10901 7087 7748 1465 424 -1451 C ATOM 2623 O TYR A 380 26.206 21.990 -16.802 1.00 72.39 O ANISOU 2623 O TYR A 380 11518 7847 8139 1481 441 -1488 O ATOM 2624 CB TYR A 380 26.058 20.818 -13.733 1.00 59.54 C ANISOU 2624 CB TYR A 380 9669 5909 7042 1334 460 -1586 C ATOM 2625 CG TYR A 380 26.736 19.714 -14.506 1.00 66.17 C ANISOU 2625 CG TYR A 380 10448 6873 7822 1379 418 -1737 C ATOM 2626 CD1 TYR A 380 28.120 19.607 -14.528 1.00 73.26 C ANISOU 2626 CD1 TYR A 380 11321 7875 8639 1330 544 -1741 C ATOM 2627 CD2 TYR A 380 25.993 18.777 -15.210 1.00 64.94 C ANISOU 2627 CD2 TYR A 380 10257 6730 7685 1473 254 -1880 C ATOM 2628 CE1 TYR A 380 28.746 18.599 -15.234 1.00 80.24 C ANISOU 2628 CE1 TYR A 380 12152 8868 9466 1424 538 -1889 C ATOM 2629 CE2 TYR A 380 26.610 17.764 -15.918 1.00 80.52 C ANISOU 2629 CE2 TYR A 380 12219 8780 9595 1538 228 -2062 C ATOM 2630 CZ TYR A 380 27.987 17.680 -15.926 1.00 86.62 C ANISOU 2630 CZ TYR A 380 12973 9649 10290 1537 386 -2069 C ATOM 2631 OH TYR A 380 28.610 16.675 -16.629 1.00 84.58 O ANISOU 2631 OH TYR A 380 12705 9464 9966 1651 393 -2257 O ATOM 2632 N THR A 381 24.180 22.286 -15.869 1.00 60.99 N ANISOU 2632 N THR A 381 10026 6183 6965 1558 310 -1401 N ATOM 2633 CA THR A 381 23.484 22.215 -17.148 1.00 55.65 C ANISOU 2633 CA THR A 381 9356 5653 6136 1659 166 -1391 C ATOM 2634 C THR A 381 23.619 23.486 -17.974 1.00 66.03 C ANISOU 2634 C THR A 381 10811 7027 7249 1698 233 -1192 C ATOM 2635 O THR A 381 23.412 23.436 -19.191 1.00 75.20 O ANISOU 2635 O THR A 381 11991 8380 8203 1759 136 -1175 O ATOM 2636 CB THR A 381 22.000 21.917 -16.925 1.00 55.11 C ANISOU 2636 CB THR A 381 9169 5548 6224 1732 4 -1361 C ATOM 2637 OG1 THR A 381 21.440 22.910 -16.056 1.00 85.65 O ANISOU 2637 OG1 THR A 381 13056 9263 10225 1781 106 -1186 O ATOM 2638 CG2 THR A 381 21.819 20.547 -16.302 1.00 52.39 C ANISOU 2638 CG2 THR A 381 8679 5157 6070 1672 -99 -1536 C ATOM 2639 N LEU A 382 23.954 24.619 -17.351 1.00 62.54 N ANISOU 2639 N LEU A 382 10482 6422 6859 1653 388 -1037 N ATOM 2640 CA LEU A 382 24.065 25.879 -18.079 1.00 59.57 C ANISOU 2640 CA LEU A 382 10255 6046 6334 1677 450 -811 C ATOM 2641 C LEU A 382 25.245 25.914 -19.039 1.00 62.95 C ANISOU 2641 C LEU A 382 10729 6682 6508 1595 510 -789 C ATOM 2642 O LEU A 382 25.344 26.857 -19.830 1.00 86.42 O ANISOU 2642 O LEU A 382 13807 9704 9325 1607 543 -574 O ATOM 2643 CB LEU A 382 24.166 27.050 -17.101 1.00 63.28 C ANISOU 2643 CB LEU A 382 10871 6227 6943 1628 597 -682 C ATOM 2644 CG LEU A 382 22.849 27.536 -16.493 1.00 64.90 C ANISOU 2644 CG LEU A 382 11083 6243 7332 1790 581 -603 C ATOM 2645 CD1 LEU A 382 23.099 28.712 -15.566 1.00 64.81 C ANISOU 2645 CD1 LEU A 382 11279 5922 7425 1743 748 -526 C ATOM 2646 CD2 LEU A 382 21.867 27.910 -17.591 1.00 63.97 C ANISOU 2646 CD2 LEU A 382 10941 6232 7131 1972 467 -417 C ATOM 2647 N PHE A 383 26.144 24.933 -18.983 1.00 80.88 N ANISOU 2647 N PHE A 383 12913 9082 8736 1527 539 -979 N ATOM 2648 CA PHE A 383 27.233 24.818 -19.940 1.00 63.35 C ANISOU 2648 CA PHE A 383 10696 7119 6257 1492 613 -971 C ATOM 2649 C PHE A 383 26.841 23.989 -21.154 1.00 69.07 C ANISOU 2649 C PHE A 383 11381 8098 6763 1624 484 -1109 C ATOM 2650 O PHE A 383 27.718 23.483 -21.864 1.00 63.66 O ANISOU 2650 O PHE A 383 10672 7650 5864 1639 549 -1204 O ATOM 2651 CB PHE A 383 28.472 24.237 -19.254 1.00 59.49 C ANISOU 2651 CB PHE A 383 10120 6653 5830 1382 734 -1083 C ATOM 2652 CG PHE A 383 29.061 25.147 -18.212 1.00 63.84 C ANISOU 2652 CG PHE A 383 10726 7015 6515 1199 851 -935 C ATOM 2653 CD1 PHE A 383 28.544 25.181 -16.928 1.00 59.47 C ANISOU 2653 CD1 PHE A 383 10181 6206 6208 1157 830 -987 C ATOM 2654 CD2 PHE A 383 30.123 25.979 -18.522 1.00 80.10 C ANISOU 2654 CD2 PHE A 383 12831 9166 8437 1050 977 -741 C ATOM 2655 CE1 PHE A 383 29.075 26.023 -15.973 1.00 57.70 C ANISOU 2655 CE1 PHE A 383 10042 5809 6070 974 924 -888 C ATOM 2656 CE2 PHE A 383 30.660 26.823 -17.569 1.00 71.05 C ANISOU 2656 CE2 PHE A 383 11758 7829 7408 838 1055 -621 C ATOM 2657 CZ PHE A 383 30.136 26.845 -16.294 1.00 59.43 C ANISOU 2657 CZ PHE A 383 10327 6091 6162 801 1025 -714 C ATOM 2658 N ASN A 384 25.541 23.841 -21.403 1.00 86.64 N ANISOU 2658 N ASN A 384 13597 10297 9027 1719 304 -1125 N ATOM 2659 CA ASN A 384 25.017 23.104 -22.544 1.00 79.94 C ANISOU 2659 CA ASN A 384 12731 9684 7957 1809 134 -1262 C ATOM 2660 C ASN A 384 24.025 23.994 -23.278 1.00 77.04 C ANISOU 2660 C ASN A 384 12403 9399 7470 1877 19 -1014 C ATOM 2661 O ASN A 384 23.100 24.531 -22.661 1.00 92.67 O ANISOU 2661 O ASN A 384 14356 11187 9669 1910 -30 -865 O ATOM 2662 CB ASN A 384 24.343 21.801 -22.093 1.00 68.10 C ANISOU 2662 CB ASN A 384 11138 8090 6646 1824 -33 -1534 C ATOM 2663 CG ASN A 384 23.962 20.902 -23.258 1.00 77.44 C ANISOU 2663 CG ASN A 384 12339 9496 7588 1876 -220 -1745 C ATOM 2664 OD1 ASN A 384 22.923 21.092 -23.893 1.00 72.95 O ANISOU 2664 OD1 ASN A 384 11763 9037 6919 1903 -409 -1665 O ATOM 2665 ND2 ASN A 384 24.800 19.911 -23.538 1.00108.82 N ANISOU 2665 ND2 ASN A 384 16340 13541 11465 1895 -171 -2020 N ATOM 2666 N LYS A 385 24.212 24.139 -24.592 1.00 72.40 N ANISOU 2666 N LYS A 385 11868 9117 6525 1914 -15 -956 N ATOM 2667 CA LYS A 385 23.395 25.078 -25.358 1.00 75.97 C ANISOU 2667 CA LYS A 385 12349 9680 6835 1979 -115 -656 C ATOM 2668 C LYS A 385 21.925 24.675 -25.343 1.00 77.31 C ANISOU 2668 C LYS A 385 12418 9839 7117 2044 -369 -685 C ATOM 2669 O LYS A 385 21.040 25.517 -25.143 1.00 79.06 O ANISOU 2669 O LYS A 385 12607 9957 7476 2117 -415 -411 O ATOM 2670 CB LYS A 385 23.917 25.176 -26.793 1.00 78.17 C ANISOU 2670 CB LYS A 385 12689 10351 6662 1997 -111 -599 C ATOM 2671 N THR A 386 21.647 23.385 -25.553 1.00 76.67 N ANISOU 2671 N THR A 386 12282 9859 6991 2018 -537 -1005 N ATOM 2672 CA THR A 386 20.269 22.901 -25.571 1.00 89.37 C ANISOU 2672 CA THR A 386 13767 11488 8702 2029 -810 -1029 C ATOM 2673 C THR A 386 19.550 23.242 -24.273 1.00100.99 C ANISOU 2673 C THR A 386 15124 12658 10590 2055 -776 -891 C ATOM 2674 O THR A 386 18.472 23.848 -24.287 1.00117.68 O ANISOU 2674 O THR A 386 17140 14788 12786 2138 -879 -635 O ATOM 2675 CB THR A 386 20.249 21.392 -25.807 1.00 96.71 C ANISOU 2675 CB THR A 386 14689 12481 9577 1952 -978 -1433 C ATOM 2676 OG1 THR A 386 21.083 21.078 -26.929 1.00 96.18 O ANISOU 2676 OG1 THR A 386 14759 12680 9106 1961 -947 -1606 O ATOM 2677 CG2 THR A 386 18.829 20.920 -26.086 1.00 92.75 C ANISOU 2677 CG2 THR A 386 14059 12073 9110 1912 -1307 -1431 C ATOM 2678 N PHE A 387 20.141 22.860 -23.138 1.00 91.09 N ANISOU 2678 N PHE A 387 13870 11152 9588 2001 -625 -1047 N ATOM 2679 CA PHE A 387 19.582 23.216 -21.839 1.00 74.79 C ANISOU 2679 CA PHE A 387 11716 8822 7877 2029 -553 -931 C ATOM 2680 C PHE A 387 19.390 24.721 -21.710 1.00 73.56 C ANISOU 2680 C PHE A 387 11630 8565 7755 2139 -414 -596 C ATOM 2681 O PHE A 387 18.368 25.182 -21.187 1.00 73.22 O ANISOU 2681 O PHE A 387 11491 8421 7907 2247 -438 -420 O ATOM 2682 CB PHE A 387 20.492 22.705 -20.720 1.00 69.91 C ANISOU 2682 CB PHE A 387 11118 7993 7452 1941 -387 -1124 C ATOM 2683 CG PHE A 387 20.250 21.272 -20.336 1.00 69.61 C ANISOU 2683 CG PHE A 387 10967 7923 7560 1864 -528 -1384 C ATOM 2684 CD1 PHE A 387 19.197 20.939 -19.501 1.00 64.82 C ANISOU 2684 CD1 PHE A 387 10196 7211 7224 1858 -627 -1339 C ATOM 2685 CD2 PHE A 387 21.086 20.261 -20.788 1.00 92.49 C ANISOU 2685 CD2 PHE A 387 13921 10884 10338 1807 -549 -1659 C ATOM 2686 CE1 PHE A 387 18.971 19.627 -19.134 1.00 65.73 C ANISOU 2686 CE1 PHE A 387 10206 7271 7497 1761 -767 -1541 C ATOM 2687 CE2 PHE A 387 20.864 18.943 -20.422 1.00 91.04 C ANISOU 2687 CE2 PHE A 387 13660 10609 10323 1738 -683 -1889 C ATOM 2688 CZ PHE A 387 19.804 18.628 -19.593 1.00 81.03 C ANISOU 2688 CZ PHE A 387 12229 9221 9336 1696 -803 -1820 C ATOM 2689 N ARG A 388 20.362 25.504 -22.191 1.00 74.68 N ANISOU 2689 N ARG A 388 11935 8727 7713 2121 -261 -491 N ATOM 2690 CA ARG A 388 20.319 26.952 -22.008 1.00 79.21 C ANISOU 2690 CA ARG A 388 12622 9126 8351 2201 -117 -181 C ATOM 2691 C ARG A 388 19.088 27.560 -22.666 1.00 84.07 C ANISOU 2691 C ARG A 388 13166 9845 8934 2370 -260 105 C ATOM 2692 O ARG A 388 18.311 28.272 -22.019 1.00108.36 O ANISOU 2692 O ARG A 388 16219 12715 12238 2511 -208 287 O ATOM 2693 CB ARG A 388 21.590 27.598 -22.562 1.00 77.56 C ANISOU 2693 CB ARG A 388 12580 8957 7930 2109 37 -91 C ATOM 2694 CG ARG A 388 22.764 27.596 -21.609 1.00 75.22 C ANISOU 2694 CG ARG A 388 12363 8465 7751 1960 234 -225 C ATOM 2695 CD ARG A 388 23.778 28.651 -22.015 1.00 78.77 C ANISOU 2695 CD ARG A 388 12972 8894 8064 1866 389 -7 C ATOM 2696 NE ARG A 388 24.253 28.461 -23.382 1.00 88.71 N ANISOU 2696 NE ARG A 388 14218 10516 8972 1855 348 48 N ATOM 2697 CZ ARG A 388 25.367 27.810 -23.702 1.00 91.80 C ANISOU 2697 CZ ARG A 388 14578 11120 9181 1755 423 -111 C ATOM 2698 NH1 ARG A 388 26.126 27.287 -22.749 1.00 86.66 N ANISOU 2698 NH1 ARG A 388 13891 10349 8687 1650 524 -311 N ATOM 2699 NH2 ARG A 388 25.724 27.684 -24.973 1.00117.74 N ANISOU 2699 NH2 ARG A 388 17858 14763 12113 1775 403 -57 N ATOM 2700 N ASP A 389 18.895 27.295 -23.954 1.00 83.10 N ANISOU 2700 N ASP A 389 13003 10056 8513 2373 -436 153 N ATOM 2701 CA ASP A 389 17.784 27.869 -24.701 1.00 92.20 C ANISOU 2701 CA ASP A 389 14066 11371 9593 2523 -596 466 C ATOM 2702 C ASP A 389 16.480 27.110 -24.499 1.00 91.86 C ANISOU 2702 C ASP A 389 13782 11435 9685 2569 -826 416 C ATOM 2703 O ASP A 389 15.438 27.553 -24.993 1.00118.40 O ANISOU 2703 O ASP A 389 17013 14947 13027 2703 -973 702 O ATOM 2704 CB ASP A 389 18.144 27.942 -26.185 1.00109.23 C ANISOU 2704 CB ASP A 389 16281 13893 11330 2486 -699 563 C ATOM 2705 CG ASP A 389 19.441 28.687 -26.424 1.00111.32 C ANISOU 2705 CG ASP A 389 16747 14095 11455 2420 -471 659 C ATOM 2706 OD1 ASP A 389 19.522 29.877 -26.052 1.00117.85 O ANISOU 2706 OD1 ASP A 389 17678 14655 12445 2487 -317 944 O ATOM 2707 OD2 ASP A 389 20.386 28.072 -26.961 1.00105.53 O ANISOU 2707 OD2 ASP A 389 16067 13571 10459 2300 -441 450 O ATOM 2708 N ALA A 390 16.513 25.976 -23.796 1.00 83.33 N ANISOU 2708 N ALA A 390 12622 10293 8747 2453 -868 92 N ATOM 2709 CA ALA A 390 15.294 25.451 -23.194 1.00 80.99 C ANISOU 2709 CA ALA A 390 12086 9995 8693 2489 -1017 103 C ATOM 2710 C ALA A 390 14.900 26.297 -21.991 1.00 85.19 C ANISOU 2710 C ALA A 390 12589 10229 9548 2653 -806 284 C ATOM 2711 O ALA A 390 13.743 26.715 -21.865 1.00 79.30 O ANISOU 2711 O ALA A 390 11664 9528 8939 2823 -867 541 O ATOM 2712 CB ALA A 390 15.478 23.990 -22.793 1.00 82.21 C ANISOU 2712 CB ALA A 390 12176 10142 8918 2301 -1124 -270 C ATOM 2713 N PHE A 391 15.869 26.579 -21.112 1.00 94.12 N ANISOU 2713 N PHE A 391 13900 11074 10790 2611 -551 155 N ATOM 2714 CA PHE A 391 15.631 27.472 -19.980 1.00 74.00 C ANISOU 2714 CA PHE A 391 11396 8222 8498 2761 -327 283 C ATOM 2715 C PHE A 391 15.129 28.835 -20.441 1.00 74.70 C ANISOU 2715 C PHE A 391 11553 8249 8580 2991 -266 648 C ATOM 2716 O PHE A 391 14.197 29.391 -19.848 1.00 74.52 O ANISOU 2716 O PHE A 391 11438 8110 8766 3213 -196 830 O ATOM 2717 CB PHE A 391 16.911 27.638 -19.159 1.00 69.44 C ANISOU 2717 CB PHE A 391 11041 7381 7963 2631 -95 90 C ATOM 2718 CG PHE A 391 17.382 26.375 -18.501 1.00 66.66 C ANISOU 2718 CG PHE A 391 10610 7044 7673 2447 -122 -224 C ATOM 2719 CD1 PHE A 391 16.489 25.367 -18.178 1.00 75.64 C ANISOU 2719 CD1 PHE A 391 11505 8294 8941 2436 -281 -299 C ATOM 2720 CD2 PHE A 391 18.722 26.196 -18.205 1.00 66.69 C ANISOU 2720 CD2 PHE A 391 10767 6954 7619 2280 6 -410 C ATOM 2721 CE1 PHE A 391 16.926 24.203 -17.573 1.00 64.53 C ANISOU 2721 CE1 PHE A 391 10036 6867 7615 2269 -310 -557 C ATOM 2722 CE2 PHE A 391 19.165 25.035 -17.602 1.00 61.39 C ANISOU 2722 CE2 PHE A 391 10014 6290 7022 2137 -17 -665 C ATOM 2723 CZ PHE A 391 18.266 24.038 -17.285 1.00 61.22 C ANISOU 2723 CZ PHE A 391 9777 6342 7140 2136 -174 -739 C ATOM 2724 N GLY A 392 15.744 29.393 -21.488 1.00 76.83 N ANISOU 2724 N GLY A 392 11980 8595 8615 2959 -279 777 N ATOM 2725 CA GLY A 392 15.336 30.706 -21.968 1.00 80.04 C ANISOU 2725 CA GLY A 392 12469 8917 9027 3172 -225 1160 C ATOM 2726 C GLY A 392 13.884 30.745 -22.405 1.00 82.10 C ANISOU 2726 C GLY A 392 12460 9402 9330 3388 -411 1433 C ATOM 2727 O GLY A 392 13.188 31.742 -22.198 1.00 81.91 O ANISOU 2727 O GLY A 392 12431 9214 9476 3658 -317 1733 O ATOM 2728 N ARG A 393 13.406 29.659 -23.012 1.00 82.59 N ANISOU 2728 N ARG A 393 12296 9840 9246 3274 -683 1336 N ATOM 2729 CA ARG A 393 11.996 29.570 -23.363 1.00 86.62 C ANISOU 2729 CA ARG A 393 12497 10612 9803 3430 -897 1593 C ATOM 2730 C ARG A 393 11.123 29.320 -22.141 1.00 94.82 C ANISOU 2730 C ARG A 393 13323 11531 11175 3553 -827 1572 C ATOM 2731 O ARG A 393 9.937 29.664 -22.156 1.00 86.11 O ANISOU 2731 O ARG A 393 11969 10551 10196 3780 -895 1880 O ATOM 2732 CB ARG A 393 11.773 28.466 -24.395 1.00 87.31 C ANISOU 2732 CB ARG A 393 12428 11134 9611 3219 -1238 1473 C ATOM 2733 CG ARG A 393 12.480 28.690 -25.720 1.00 89.31 C ANISOU 2733 CG ARG A 393 12853 11606 9475 3128 -1323 1524 C ATOM 2734 CD ARG A 393 12.088 27.630 -26.736 1.00 91.78 C ANISOU 2734 CD ARG A 393 13020 12363 9490 2943 -1677 1395 C ATOM 2735 NE ARG A 393 12.417 26.283 -26.279 1.00 90.37 N ANISOU 2735 NE ARG A 393 12838 12150 9351 2712 -1744 935 N ATOM 2736 CZ ARG A 393 13.564 25.667 -26.542 1.00 96.50 C ANISOU 2736 CZ ARG A 393 13827 12912 9928 2539 -1689 584 C ATOM 2737 NH1 ARG A 393 14.497 26.277 -27.260 1.00 89.92 N ANISOU 2737 NH1 ARG A 393 13208 12137 8823 2551 -1562 646 N ATOM 2738 NH2 ARG A 393 13.779 24.440 -26.087 1.00 88.42 N ANISOU 2738 NH2 ARG A 393 12790 11820 8985 2362 -1753 196 N ATOM 2739 N TYR A 394 11.689 28.735 -21.081 1.00 88.48 N ANISOU 2739 N TYR A 394 12594 10518 10507 3416 -685 1242 N ATOM 2740 CA TYR A 394 10.905 28.420 -19.891 1.00 78.75 C ANISOU 2740 CA TYR A 394 11152 9213 9558 3511 -609 1220 C ATOM 2741 C TYR A 394 10.693 29.650 -19.016 1.00 78.96 C ANISOU 2741 C TYR A 394 11294 8913 9795 3818 -299 1389 C ATOM 2742 O TYR A 394 9.594 29.854 -18.488 1.00 88.42 O ANISOU 2742 O TYR A 394 12256 10156 11186 4060 -253 1584 O ATOM 2743 CB TYR A 394 11.585 27.309 -19.089 1.00 84.87 C ANISOU 2743 CB TYR A 394 11958 9905 10384 3248 -584 831 C ATOM 2744 CG TYR A 394 11.667 25.984 -19.814 1.00 94.08 C ANISOU 2744 CG TYR A 394 13010 11339 11396 2971 -885 631 C ATOM 2745 CD1 TYR A 394 10.821 25.699 -20.879 1.00 91.07 C ANISOU 2745 CD1 TYR A 394 12425 11298 10880 2954 -1188 795 C ATOM 2746 CD2 TYR A 394 12.590 25.019 -19.436 1.00 93.89 C ANISOU 2746 CD2 TYR A 394 13093 11222 11359 2729 -873 276 C ATOM 2747 CE1 TYR A 394 10.892 24.493 -21.545 1.00 90.37 C ANISOU 2747 CE1 TYR A 394 12280 11421 10635 2689 -1471 570 C ATOM 2748 CE2 TYR A 394 12.668 23.809 -20.096 1.00 99.20 C ANISOU 2748 CE2 TYR A 394 13703 12083 11904 2501 -1135 66 C ATOM 2749 CZ TYR A 394 11.817 23.552 -21.150 1.00 94.11 C ANISOU 2749 CZ TYR A 394 12893 11748 11116 2474 -1435 193 C ATOM 2750 OH TYR A 394 11.890 22.348 -21.811 1.00103.19 O ANISOU 2750 OH TYR A 394 14026 13056 12125 2234 -1707 -57 O ATOM 2751 N ILE A 395 11.732 30.472 -18.842 1.00 81.48 N ANISOU 2751 N ILE A 395 11977 8901 10079 3811 -80 1314 N ATOM 2752 CA ILE A 395 11.605 31.694 -18.049 1.00 75.37 C ANISOU 2752 CA ILE A 395 11389 7755 9492 4087 211 1434 C ATOM 2753 C ILE A 395 10.847 32.786 -18.780 1.00 86.16 C ANISOU 2753 C ILE A 395 12733 9113 10892 4412 207 1854 C ATOM 2754 O ILE A 395 10.436 33.769 -18.151 1.00117.74 O ANISOU 2754 O ILE A 395 16837 12816 15084 4722 436 1991 O ATOM 2755 CB ILE A 395 12.988 32.222 -17.625 1.00 73.07 C ANISOU 2755 CB ILE A 395 11508 7096 9159 3921 415 1221 C ATOM 2756 CG1 ILE A 395 13.842 32.521 -18.857 1.00 86.01 C ANISOU 2756 CG1 ILE A 395 13320 8793 10566 3761 314 1311 C ATOM 2757 CG2 ILE A 395 13.678 31.219 -16.714 1.00 72.38 C ANISOU 2757 CG2 ILE A 395 11421 7002 9077 3650 448 844 C ATOM 2758 CD1 ILE A 395 15.243 32.972 -18.527 1.00 95.62 C ANISOU 2758 CD1 ILE A 395 14889 9709 11733 3547 484 1137 C ATOM 2759 N THR A 396 10.661 32.650 -20.090 1.00 89.41 N ANISOU 2759 N THR A 396 13023 9840 11110 4361 -44 2062 N ATOM 2760 CA THR A 396 9.741 33.488 -20.843 1.00 89.08 C ANISOU 2760 CA THR A 396 12853 9899 11094 4673 -110 2518 C ATOM 2761 C THR A 396 8.365 32.848 -20.977 1.00 90.35 C ANISOU 2761 C THR A 396 12540 10472 11316 4794 -322 2705 C ATOM 2762 O THR A 396 7.504 33.392 -21.674 1.00 96.73 O ANISOU 2762 O THR A 396 13159 11465 12130 5041 -429 3117 O ATOM 2763 CB THR A 396 10.317 33.800 -22.226 1.00 99.06 C ANISOU 2763 CB THR A 396 14249 11312 12079 4546 -268 2692 C ATOM 2764 OG1 THR A 396 10.611 32.576 -22.910 1.00110.17 O ANISOU 2764 OG1 THR A 396 15524 13118 13218 4215 -536 2475 O ATOM 2765 CG2 THR A 396 11.595 34.613 -22.098 1.00 97.22 C ANISOU 2765 CG2 THR A 396 14454 10665 11819 4447 -46 2603 C ATOM 2766 N CYS A 397 8.152 31.697 -20.332 1.00 90.24 N ANISOU 2766 N CYS A 397 12317 10616 11353 4610 -397 2440 N ATOM 2767 CA CYS A 397 6.851 31.028 -20.269 1.00 97.58 C ANISOU 2767 CA CYS A 397 12776 11920 12380 4679 -588 2609 C ATOM 2768 C CYS A 397 6.330 30.641 -21.652 1.00106.64 C ANISOU 2768 C CYS A 397 13684 13529 13304 4565 -974 2836 C ATOM 2769 O CYS A 397 5.120 30.651 -21.895 1.00122.14 O ANISOU 2769 O CYS A 397 15263 15803 15343 4734 -1129 3175 O ATOM 2770 CB CYS A 397 5.824 31.893 -19.530 1.00106.88 C ANISOU 2770 CB CYS A 397 13785 12989 13835 5139 -359 2915 C ATOM 2771 SG CYS A 397 6.372 32.473 -17.905 1.00 95.94 S ANISOU 2771 SG CYS A 397 12724 11065 12665 5304 106 2637 S ATOM 2772 N ASN A 398 7.228 30.269 -22.564 1.00113.76 N ANISOU 2772 N ASN A 398 14796 14516 13911 4271 -1137 2651 N ATOM 2773 CA ASN A 398 6.838 29.921 -23.925 1.00127.69 C ANISOU 2773 CA ASN A 398 16392 16730 15394 4141 -1504 2824 C ATOM 2774 C ASN A 398 6.529 28.432 -24.070 1.00119.61 C ANISOU 2774 C ASN A 398 15140 16024 14281 3794 -1822 2564 C ATOM 2775 O ASN A 398 5.485 28.066 -24.622 1.00135.51 O ANISOU 2775 O ASN A 398 16805 18435 16246 3765 -2128 2792 O ATOM 2776 CB ASN A 398 7.934 30.344 -24.909 1.00119.00 C ANISOU 2776 CB ASN A 398 15639 15595 13981 4029 -1502 2781 C ATOM 2777 CG ASN A 398 7.927 31.840 -25.181 1.00102.25 C ANISOU 2777 CG ASN A 398 13662 13277 11912 4357 -1317 3193 C ATOM 2778 OD1 ASN A 398 8.908 32.537 -24.922 1.00 94.11 O ANISOU 2778 OD1 ASN A 398 12986 11867 10906 4377 -1057 3113 O ATOM 2779 ND2 ASN A 398 6.813 32.339 -25.707 1.00 97.98 N ANISOU 2779 ND2 ASN A 398 12839 12988 11401 4607 -1461 3658 N ATOM 2780 N TYR A 399 7.419 27.572 -23.587 1.00103.76 N ANISOU 2780 N TYR A 399 13324 13839 12261 3526 -1766 2107 N ATOM 2781 CA TYR A 399 7.234 26.106 -23.594 1.00113.01 C ANISOU 2781 CA TYR A 399 14339 15203 13397 3188 -2039 1814 C ATOM 2782 C TYR A 399 7.076 25.643 -25.046 1.00137.09 C ANISOU 2782 C TYR A 399 17351 18653 16082 2985 -2422 1824 C ATOM 2783 O TYR A 399 7.805 26.110 -25.936 1.00143.43 O ANISOU 2783 O TYR A 399 18407 19497 16592 2989 -2406 1820 O ATOM 2784 CB TYR A 399 6.074 25.710 -22.704 1.00109.49 C ANISOU 2784 CB TYR A 399 13501 14839 13262 3242 -2081 1961 C ATOM 2785 CG TYR A 399 6.209 26.082 -21.255 1.00110.78 C ANISOU 2785 CG TYR A 399 13704 14654 13734 3433 -1706 1920 C ATOM 2786 CD1 TYR A 399 5.722 27.292 -20.785 1.00111.08 C ANISOU 2786 CD1 TYR A 399 13693 14571 13942 3835 -1444 2245 C ATOM 2787 CD2 TYR A 399 6.797 25.212 -20.348 1.00 98.23 C ANISOU 2787 CD2 TYR A 399 12203 12861 12258 3222 -1616 1559 C ATOM 2788 CE1 TYR A 399 5.830 27.633 -19.457 1.00 99.54 C ANISOU 2788 CE1 TYR A 399 12295 12804 12723 4011 -1098 2173 C ATOM 2789 CE2 TYR A 399 6.910 25.544 -19.016 1.00 98.17 C ANISOU 2789 CE2 TYR A 399 12231 12580 12490 3383 -1284 1523 C ATOM 2790 CZ TYR A 399 6.424 26.757 -18.577 1.00100.94 C ANISOU 2790 CZ TYR A 399 12554 12826 12972 3772 -1026 1812 C ATOM 2791 OH TYR A 399 6.532 27.098 -17.253 1.00118.64 O ANISOU 2791 OH TYR A 399 14862 14805 15412 3935 -692 1742 O ATOM 2792 N ARG A 400 6.141 24.733 -25.306 1.00134.99 N ANISOU 2792 N ARG A 400 16777 18699 15813 2789 -2772 1841 N ATOM 2793 CA ARG A 400 5.876 24.195 -26.633 1.00121.75 C ANISOU 2793 CA ARG A 400 15055 17428 13775 2557 -3180 1819 C ATOM 2794 C ARG A 400 4.484 23.577 -26.659 1.00119.16 C ANISOU 2794 C ARG A 400 14275 17438 13563 2426 -3535 2026 C ATOM 2795 O ARG A 400 4.141 22.771 -25.792 1.00125.24 O ANISOU 2795 O ARG A 400 14879 18102 14605 2280 -3561 1891 O ATOM 2796 CB ARG A 400 6.920 23.148 -27.020 1.00121.75 C ANISOU 2796 CB ARG A 400 15375 17347 13539 2240 -3264 1277 C TER 2797 ARG A 400 HETATM 2798 C1 CLR A1201 7.172 28.555 -12.571 1.00107.10 C HETATM 2799 C2 CLR A1201 7.431 28.019 -13.971 1.00 99.19 C HETATM 2800 C3 CLR A1201 8.515 28.835 -14.656 1.00 97.68 C HETATM 2801 C4 CLR A1201 9.819 28.678 -13.886 1.00 96.42 C HETATM 2802 C5 CLR A1201 9.632 28.935 -12.407 1.00103.57 C HETATM 2803 C6 CLR A1201 10.616 29.597 -11.772 1.00114.76 C HETATM 2804 C7 CLR A1201 10.461 30.206 -10.400 1.00 90.48 C HETATM 2805 C8 CLR A1201 9.430 29.423 -9.608 1.00 91.63 C HETATM 2806 C9 CLR A1201 8.150 29.268 -10.423 1.00 93.43 C HETATM 2807 C10 CLR A1201 8.401 28.436 -11.677 1.00104.39 C HETATM 2808 C11 CLR A1201 6.992 28.682 -9.602 1.00103.42 C HETATM 2809 C12 CLR A1201 6.804 29.313 -8.219 1.00107.75 C HETATM 2810 C13 CLR A1201 8.129 29.319 -7.467 1.00 88.90 C HETATM 2811 C14 CLR A1201 9.100 30.124 -8.302 1.00 85.57 C HETATM 2812 C15 CLR A1201 10.252 30.451 -7.367 1.00101.32 C HETATM 2813 C16 CLR A1201 9.588 30.565 -5.994 1.00 92.24 C HETATM 2814 C17 CLR A1201 8.147 30.066 -6.135 1.00 84.95 C HETATM 2815 C18 CLR A1201 8.626 27.891 -7.243 1.00102.12 C HETATM 2816 C19 CLR A1201 8.631 26.981 -11.291 1.00107.08 C HETATM 2817 C20 CLR A1201 7.697 29.223 -4.941 1.00 82.06 C HETATM 2818 C21 CLR A1201 6.191 29.335 -4.716 1.00 84.79 C HETATM 2819 C22 CLR A1201 8.471 29.572 -3.670 1.00 83.95 C HETATM 2820 C23 CLR A1201 7.782 30.657 -2.847 1.00 83.58 C HETATM 2821 C24 CLR A1201 8.768 31.344 -1.907 1.00101.40 C HETATM 2822 C25 CLR A1201 8.567 30.929 -0.451 1.00109.39 C HETATM 2823 C26 CLR A1201 7.094 30.705 -0.123 1.00104.89 C HETATM 2824 C27 CLR A1201 9.404 29.702 -0.102 1.00 96.52 C HETATM 2825 O1 CLR A1201 8.693 28.344 -15.989 1.00102.10 O HETATM 2826 C1 OLA A1202 25.243 5.842 16.541 1.00 98.21 C HETATM 2827 O1 OLA A1202 24.031 6.118 16.677 1.00 77.77 O HETATM 2828 O2 OLA A1202 26.092 6.543 17.134 1.00 76.83 O HETATM 2829 C2 OLA A1202 25.672 4.675 15.682 1.00103.41 C HETATM 2830 C3 OLA A1202 26.406 5.178 14.443 1.00 79.11 C HETATM 2831 C4 OLA A1202 26.008 4.395 13.197 1.00 64.10 C HETATM 2832 C5 OLA A1202 27.168 4.337 12.208 1.00 55.27 C HETATM 2833 C6 OLA A1202 26.692 4.246 10.761 1.00 58.92 C HETATM 2834 C7 OLA A1202 27.675 4.956 9.835 1.00 74.96 C HETATM 2835 C8 OLA A1202 27.155 5.060 8.406 1.00 66.21 C HETATM 2836 C9 OLA A1202 27.286 3.728 7.706 1.00 75.78 C HETATM 2837 C10 OLA A1202 26.328 3.325 6.875 1.00 77.53 C HETATM 2838 C11 OLA A1202 26.650 3.007 5.434 1.00 67.27 C HETATM 2839 C12 OLA A1202 25.739 1.884 4.955 1.00 69.68 C HETATM 2840 C13 OLA A1202 25.945 1.585 3.476 1.00 52.60 C HETATM 2841 C14 OLA A1202 24.603 1.506 2.760 1.00 54.81 C HETATM 2842 C15 OLA A1202 24.592 0.383 1.731 1.00 44.73 C HETATM 2843 C10 OLC A1203 44.113 17.696 -3.904 1.00 67.63 C HETATM 2844 C9 OLC A1203 43.139 17.862 -4.796 1.00 74.56 C HETATM 2845 C11 OLC A1203 45.457 17.156 -4.330 1.00 82.49 C HETATM 2846 C8 OLC A1203 43.356 17.504 -6.247 1.00 77.35 C HETATM 2847 C24 OLC A1203 35.689 13.100 -13.675 1.00 95.46 C HETATM 2848 C12 OLC A1203 46.540 18.176 -3.999 1.00 81.78 C HETATM 2849 C7 OLC A1203 42.009 17.264 -6.923 1.00 63.06 C HETATM 2850 C6 OLC A1203 41.217 18.564 -7.006 1.00 51.08 C HETATM 2851 C5 OLC A1203 39.905 18.382 -7.761 1.00 46.10 C HETATM 2852 C4 OLC A1203 38.960 17.442 -7.020 1.00 51.64 C HETATM 2853 C3 OLC A1203 37.654 17.255 -7.785 1.00 56.63 C HETATM 2854 C2 OLC A1203 37.930 16.989 -9.260 1.00 65.93 C HETATM 2855 C21 OLC A1203 36.190 14.523 -11.691 1.00 76.61 C HETATM 2856 C1 OLC A1203 36.920 16.014 -9.817 1.00103.24 C HETATM 2857 C22 OLC A1203 36.668 14.105 -13.077 1.00 73.93 C HETATM 2858 O19 OLC A1203 35.974 15.641 -9.144 1.00104.50 O HETATM 2859 O25 OLC A1203 36.170 12.651 -14.948 1.00 73.92 O HETATM 2860 O23 OLC A1203 36.752 15.262 -13.916 1.00 85.09 O HETATM 2861 O20 OLC A1203 37.084 15.504 -11.170 1.00 90.46 O HETATM 2862 C1 PEG A1204 29.651 19.482 -20.236 1.00 81.41 C HETATM 2863 O1 PEG A1204 30.662 20.143 -21.020 1.00 84.68 O HETATM 2864 C2 PEG A1204 28.641 20.379 -19.456 1.00 62.07 C HETATM 2865 O2 PEG A1204 27.587 19.809 -18.976 1.00 56.25 O HETATM 2866 C3 PEG A1204 26.776 18.975 -19.849 1.00 60.29 C HETATM 2867 C4 PEG A1204 25.517 18.325 -19.253 1.00 52.99 C HETATM 2868 O4 PEG A1204 24.797 17.501 -20.054 1.00 60.37 O HETATM 2869 P PO4 A1205 19.666 31.565 -21.629 1.00148.78 P HETATM 2870 O1 PO4 A1205 19.529 31.360 -23.119 1.00139.72 O HETATM 2871 O2 PO4 A1205 20.585 32.734 -21.364 1.00128.77 O HETATM 2872 O3 PO4 A1205 20.242 30.319 -20.999 1.00141.16 O HETATM 2873 O4 PO4 A1205 18.309 31.848 -21.031 1.00146.65 O HETATM 2874 CAA H8J A1206 22.959 22.397 12.467 1.00 56.10 C HETATM 2875 CAB H8J A1206 22.530 18.930 6.267 1.00 69.73 C HETATM 2876 CAC H8J A1206 26.389 12.385 5.162 1.00 49.45 C HETATM 2877 CAF H8J A1206 22.943 16.706 9.672 1.00 74.57 C HETATM 2878 CAG H8J A1206 25.819 13.499 9.499 1.00 39.70 C HETATM 2879 CAH H8J A1206 24.998 14.618 9.664 1.00 47.99 C HETATM 2880 CAI H8J A1206 26.121 12.991 8.239 1.00 39.90 C HETATM 2881 CAJ H8J A1206 24.934 14.354 5.270 1.00 54.69 C HETATM 2882 CAK H8J A1206 21.605 21.780 12.644 1.00 55.80 C HETATM 2883 CAL H8J A1206 20.806 19.842 13.955 1.00 62.45 C HETATM 2884 CAM H8J A1206 23.565 16.289 6.121 1.00 43.28 C HETATM 2885 CAN H8J A1206 22.423 18.736 8.616 1.00 68.81 C HETATM 2886 CAP H8J A1206 22.404 18.639 11.109 1.00 57.29 C HETATM 2887 CAQ H8J A1206 23.652 16.355 8.517 1.00 67.73 C HETATM 2888 CAR H8J A1206 24.386 15.165 6.157 1.00 55.88 C HETATM 2889 CAS H8J A1206 24.484 15.219 8.514 1.00 61.36 C HETATM 2890 CAT H8J A1206 25.612 13.592 7.166 1.00 61.73 C HETATM 2891 CAU H8J A1206 24.816 14.678 7.334 1.00 61.47 C HETATM 2892 CAV H8J A1206 22.133 17.849 9.811 1.00 66.44 C HETATM 2893 CAW H8J A1206 21.742 20.278 12.846 1.00 65.53 C HETATM 2894 CAX H8J A1206 23.662 17.160 7.375 1.00 59.02 C HETATM 2895 NAO H8J A1206 21.444 19.573 11.633 1.00 65.26 N HETATM 2896 NAY H8J A1206 22.465 17.997 7.363 1.00 59.75 N HETATM 2897 NAZ H8J A1206 25.661 13.421 5.849 1.00 50.24 N HETATM 2898 OAD H8J A1206 23.458 18.472 11.694 1.00 51.14 O HETATM 2899 OAE H8J A1206 21.303 18.634 14.545 1.00 55.94 O HETATM 2900 O HOH A1301 25.964 18.057 13.397 1.00 50.54 O HETATM 2901 O HOH A1302 17.776 27.549 16.452 1.00 80.62 O HETATM 2902 O HOH A1303 46.525 4.378 -15.090 1.00 56.71 O CONECT 627 1165 CONECT 1165 627 CONECT 2401 2418 CONECT 2418 2401 CONECT 2798 2799 2807 CONECT 2799 2798 2800 CONECT 2800 2799 2801 2825 CONECT 2801 2800 2802 CONECT 2802 2801 2803 2807 CONECT 2803 2802 2804 CONECT 2804 2803 2805 CONECT 2805 2804 2806 2811 CONECT 2806 2805 2807 2808 CONECT 2807 2798 2802 2806 2816 CONECT 2808 2806 2809 CONECT 2809 2808 2810 CONECT 2810 2809 2811 2814 2815 CONECT 2811 2805 2810 2812 CONECT 2812 2811 2813 CONECT 2813 2812 2814 CONECT 2814 2810 2813 2817 CONECT 2815 2810 CONECT 2816 2807 CONECT 2817 2814 2818 2819 CONECT 2818 2817 CONECT 2819 2817 2820 CONECT 2820 2819 2821 CONECT 2821 2820 2822 CONECT 2822 2821 2823 2824 CONECT 2823 2822 CONECT 2824 2822 CONECT 2825 2800 CONECT 2826 2827 2828 2829 CONECT 2827 2826 CONECT 2828 2826 CONECT 2829 2826 2830 CONECT 2830 2829 2831 CONECT 2831 2830 2832 CONECT 2832 2831 2833 CONECT 2833 2832 2834 CONECT 2834 2833 2835 CONECT 2835 2834 2836 CONECT 2836 2835 2837 CONECT 2837 2836 2838 CONECT 2838 2837 2839 CONECT 2839 2838 2840 CONECT 2840 2839 2841 CONECT 2841 2840 2842 CONECT 2842 2841 CONECT 2843 2844 2845 CONECT 2844 2843 2846 CONECT 2845 2843 2848 CONECT 2846 2844 2849 CONECT 2847 2857 2859 CONECT 2848 2845 CONECT 2849 2846 2850 CONECT 2850 2849 2851 CONECT 2851 2850 2852 CONECT 2852 2851 2853 CONECT 2853 2852 2854 CONECT 2854 2853 2856 CONECT 2855 2857 2861 CONECT 2856 2854 2858 2861 CONECT 2857 2847 2855 2860 CONECT 2858 2856 CONECT 2859 2847 CONECT 2860 2857 CONECT 2861 2855 2856 CONECT 2862 2863 2864 CONECT 2863 2862 CONECT 2864 2862 2865 CONECT 2865 2864 2866 CONECT 2866 2865 2867 CONECT 2867 2866 2868 CONECT 2868 2867 CONECT 2869 2870 2871 2872 2873 CONECT 2870 2869 CONECT 2871 2869 CONECT 2872 2869 CONECT 2873 2869 CONECT 2874 2882 CONECT 2875 2896 CONECT 2876 2897 CONECT 2877 2887 2892 CONECT 2878 2879 2880 CONECT 2879 2878 2889 CONECT 2880 2878 2890 CONECT 2881 2888 2897 CONECT 2882 2874 2893 CONECT 2883 2893 2899 CONECT 2884 2888 2894 CONECT 2885 2892 2896 CONECT 2886 2892 2895 2898 CONECT 2887 2877 2889 2894 CONECT 2888 2881 2884 2891 CONECT 2889 2879 2887 2891 CONECT 2890 2880 2891 2897 CONECT 2891 2888 2889 2890 CONECT 2892 2877 2885 2886 CONECT 2893 2882 2883 2895 CONECT 2894 2884 2887 2896 CONECT 2895 2886 2893 CONECT 2896 2875 2885 2894 CONECT 2897 2876 2881 2890 CONECT 2898 2886 CONECT 2899 2883 MASTER 419 0 6 19 0 0 10 6 2901 1 106 32 END