HEADER MEMBRANE PROTEIN 02-MAR-18 6CM4 TITLE STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL TITLE 2 ANTIPSYCHOTIC DRUG RISPERIDONE COMPND MOL_ID: 1; COMPND 2 MOLECULE: D(2) DOPAMINE RECEPTOR, ENDOLYSIN CHIMERA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: DOPAMINE D2 RECEPTOR, LYSIS PROTEIN, LYSOZYME, MURAMIDASE, COMPND 5 DOPAMINE D2 RECEPTOR; COMPND 6 EC: 3.2.1.17; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4; SOURCE 3 ORGANISM_COMMON: HUMAN, BACTERIOPHAGE T4; SOURCE 4 ORGANISM_TAXID: 9606, 10665; SOURCE 5 GENE: DRD2, E, T4TP126; 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; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC1-HM KEYWDS GPCR, D2, DOPAMINE RECEPTOR, ANTIPSYCHOTIC, RISPERIDONE, MEMBRANE KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH REVDAT 5 27-NOV-19 6CM4 1 REMARK REVDAT 4 20-FEB-19 6CM4 1 REMARK REVDAT 3 11-APR-18 6CM4 1 DBREF REVDAT 2 21-MAR-18 6CM4 1 JRNL REVDAT 1 14-MAR-18 6CM4 0 SPRSDE 14-MAR-18 6CM4 6C38 JRNL AUTH S.WANG,T.CHE,A.LEVIT,B.K.SHOICHET,D.WACKER,B.L.ROTH JRNL TITL STRUCTURE OF THE D2 DOPAMINE RECEPTOR BOUND TO THE ATYPICAL JRNL TITL 2 ANTIPSYCHOTIC DRUG RISPERIDONE. JRNL REF NATURE V. 555 269 2018 JRNL REFN ESSN 1476-4687 JRNL PMID 29466326 JRNL DOI 10.1038/NATURE25758 REMARK 2 REMARK 2 RESOLUTION. 2.87 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.87 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2 REMARK 3 NUMBER OF REFLECTIONS : 12814 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) : 0.226 REMARK 3 FREE R VALUE : 0.249 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850 REMARK 3 FREE R VALUE TEST SET COUNT : 622 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.5504 - 4.5475 0.98 3287 157 0.2103 0.2188 REMARK 3 2 4.5475 - 3.6116 0.99 3151 170 0.2090 0.2511 REMARK 3 3 3.6116 - 3.1556 0.99 3111 162 0.2730 0.3034 REMARK 3 4 3.1556 - 2.8674 0.84 2643 133 0.3166 0.3214 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.640 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 : 0.003 3283 REMARK 3 ANGLE : 0.516 4483 REMARK 3 CHIRALITY : 0.037 544 REMARK 3 PLANARITY : 0.003 549 REMARK 3 DIHEDRAL : 10.862 1928 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 36 THROUGH 222 ) REMARK 3 ORIGIN FOR THE GROUP (A): 7.6595 9.9883 1.8227 REMARK 3 T TENSOR REMARK 3 T11: 0.3906 T22: 0.3948 REMARK 3 T33: 0.4097 T12: -0.0409 REMARK 3 T13: 0.0298 T23: 0.0323 REMARK 3 L TENSOR REMARK 3 L11: 4.8704 L22: 2.9655 REMARK 3 L33: 4.7317 L12: 0.7811 REMARK 3 L13: 2.8181 L23: 1.4507 REMARK 3 S TENSOR REMARK 3 S11: 0.0593 S12: -0.1051 S13: 0.0093 REMARK 3 S21: 0.1418 S22: -0.1464 S23: 0.1356 REMARK 3 S31: 0.4299 S32: -0.3974 S33: -0.0137 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1002 THROUGH 1161 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.7700 -7.7446 36.3658 REMARK 3 T TENSOR REMARK 3 T11: 0.6968 T22: 0.5198 REMARK 3 T33: 0.5000 T12: 0.0363 REMARK 3 T13: 0.0872 T23: 0.1084 REMARK 3 L TENSOR REMARK 3 L11: 6.6697 L22: 6.8821 REMARK 3 L33: 6.4568 L12: 1.6541 REMARK 3 L13: 1.9941 L23: 1.4205 REMARK 3 S TENSOR REMARK 3 S11: -0.2551 S12: 0.1211 S13: -0.2547 REMARK 3 S21: -0.3908 S22: -0.0566 S23: -0.4642 REMARK 3 S31: 0.4711 S32: 0.2364 S33: 0.3147 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 384 THROUGH 460 ) REMARK 3 ORIGIN FOR THE GROUP (A): 9.8885 -1.6530 -1.3224 REMARK 3 T TENSOR REMARK 3 T11: 0.6392 T22: 0.3770 REMARK 3 T33: 0.5276 T12: 0.0087 REMARK 3 T13: -0.0908 T23: 0.0140 REMARK 3 L TENSOR REMARK 3 L11: 6.0244 L22: 5.3813 REMARK 3 L33: 6.7255 L12: 0.3578 REMARK 3 L13: 1.1698 L23: 0.5209 REMARK 3 S TENSOR REMARK 3 S11: -0.0948 S12: 0.3307 S13: 0.0832 REMARK 3 S21: -0.4022 S22: 0.2772 S23: -0.0581 REMARK 3 S31: 1.2902 S32: -0.0417 S33: -0.2847 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 6CM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1000232947. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 13-AUG-17 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 : DOUBLE CRYSTAL CRYO-COOLED REMARK 200 SI(111) 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 : 12826 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.867 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3 REMARK 200 DATA REDUNDANCY : 5.500 REMARK 200 R MERGE (I) : 0.13400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.50 REMARK 200 R MERGE FOR SHELL (I) : 0.73800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.000 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 ENTRIES 5WIU & 2RH1 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.13 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, PH 7.8, 230 MM REMARK 280 LITHIUM NITRATE, 25% PEG400, 4% 1,3-BUTANEDIOL, LIPIDIC CUBIC REMARK 280 PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 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 25.48950 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.65350 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.26150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.65350 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.48950 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.26150 REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20460 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 12.0 KCAL/MOL 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 MET A 140 REMARK 465 LEU A 141 REMARK 465 TYR A 142 REMARK 465 ASN A 143 REMARK 465 LYS A 362 REMARK 465 LEU A 363 REMARK 465 CYS A 443 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 ASN A 35 CG OD1 ND2 REMARK 470 TYR A 36 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LEU A 43 CG CD1 CD2 REMARK 470 GLU A 62 CG CD OE1 OE2 REMARK 470 LYS A 63 CG CD CE NZ REMARK 470 VAL A 96 CG1 CG2 REMARK 470 GLU A 99 CG CD OE1 OE2 REMARK 470 LYS A 101 CG CD CE NZ REMARK 470 THR A 144 OG1 CG2 REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2 REMARK 470 SER A 147 OG REMARK 470 LYS A 149 CG CD CE NZ REMARK 470 ARG A 150 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 176 CG OD1 ND2 REMARK 470 ASP A 178 CG OD1 OD2 REMARK 470 GLN A 179 CG CD OE1 NE2 REMARK 470 ASN A 180 CG OD1 ND2 REMARK 470 LYS A 211 CE NZ REMARK 470 ARG A 217 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 221 CG CD CE NZ REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1016 CG CD CE NZ REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 GLU A1022 CG CD OE1 OE2 REMARK 470 LEU A1032 CG CD1 CD2 REMARK 470 LEU A1033 CG CD1 CD2 REMARK 470 LYS A1035 CG CD CE NZ REMARK 470 SER A1036 OG REMARK 470 SER A1038 OG REMARK 470 ASN A1040 CG OD1 ND2 REMARK 470 SER A1044 OG REMARK 470 GLU A1045 CG CD OE1 OE2 REMARK 470 LYS A1048 CG CD CE NZ REMARK 470 ILE A1050 CG1 CG2 CD1 REMARK 470 ASN A1053 CG OD1 ND2 REMARK 470 THR A1054 OG1 CG2 REMARK 470 ASN A1055 CG OD1 ND2 REMARK 470 VAL A1057 CG1 CG2 REMARK 470 LYS A1060 CG CD CE NZ REMARK 470 LYS A1065 CG CD CE NZ REMARK 470 ARG A1080 CG CD NE CZ NH1 NH2 REMARK 470 LYS A1083 CG CD CE NZ REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 ASN A1116 CG OD1 ND2 REMARK 470 ASP A1127 CG OD1 OD2 REMARK 470 VAL A1131 CG1 CG2 REMARK 470 LYS A1135 CG CD CE NZ REMARK 470 ARG A1137 CG CD NE CZ NH1 NH2 REMARK 470 GLN A1141 CG CD OE1 NE2 REMARK 470 LYS A1147 CG CD CE NZ REMARK 470 THR A1157 OG1 CG2 REMARK 470 SER A 364 OG REMARK 470 GLN A 365 CG CD OE1 NE2 REMARK 470 GLN A 366 CG CD OE1 NE2 REMARK 470 LYS A 367 CG CD CE NZ REMARK 470 LYS A 369 CG CD CE NZ REMARK 470 LYS A 370 CG CD CE NZ REMARK 470 ILE A 394 CG1 CG2 CD1 REMARK 470 HIS A 398 CG ND1 CD2 CE1 NE2 REMARK 470 ASP A 400 CG OD1 OD2 REMARK 470 VAL A 406 CG1 CG2 REMARK 470 LEU A 407 CG CD1 CD2 REMARK 470 ILE A 431 CG1 CG2 CD1 REMARK 470 GLU A 432 CG CD OE1 OE2 REMARK 470 ARG A 434 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 435 CG CD CE NZ REMARK 470 LEU A 438 CG CD1 CD2 REMARK 470 LYS A 439 CG CD CE NZ REMARK 470 HIS A 442 CG ND1 CD2 CE1 NE2 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 GLN A 66 70.23 -104.22 REMARK 500 VAL A 87 -52.46 -121.67 REMARK 500 PHE A 198 -60.72 -124.56 REMARK 500 ASN A1055 17.81 58.75 REMARK 500 PHE A1114 49.44 -89.78 REMARK 500 ASP A 400 11.47 57.92 REMARK 500 LEU A 441 33.98 -88.55 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 2005 REMARK 610 OLA A 2006 DBREF 6CM4 A 35 222 UNP P14416 DRD2_HUMAN 35 222 DBREF 6CM4 A 1002 1161 UNP D9IEF7 D9IEF7_BPT4 2 161 DBREF 6CM4 A 362 443 UNP P14416 DRD2_HUMAN 362 443 SEQADV 6CM4 ALA A 122 UNP P14416 ILE 122 CONFLICT SEQADV 6CM4 THR A 1054 UNP D9IEF7 CYS 54 CONFLICT SEQADV 6CM4 ALA A 1097 UNP D9IEF7 CYS 97 CONFLICT SEQADV 6CM4 ALA A 375 UNP P14416 LEU 375 CONFLICT SEQADV 6CM4 ALA A 379 UNP P14416 LEU 379 CONFLICT SEQRES 1 A 430 ASN TYR TYR ALA THR LEU LEU THR LEU LEU ILE ALA VAL SEQRES 2 A 430 ILE VAL PHE GLY ASN VAL LEU VAL CYS MET ALA VAL SER SEQRES 3 A 430 ARG GLU LYS ALA LEU GLN THR THR THR ASN TYR LEU ILE SEQRES 4 A 430 VAL SER LEU ALA VAL ALA ASP LEU LEU VAL ALA THR LEU SEQRES 5 A 430 VAL MET PRO TRP VAL VAL TYR LEU GLU VAL VAL GLY GLU SEQRES 6 A 430 TRP LYS PHE SER ARG ILE HIS CYS ASP ILE PHE VAL THR SEQRES 7 A 430 LEU ASP VAL MET MET CYS THR ALA SER ALA LEU ASN LEU SEQRES 8 A 430 CYS ALA ILE SER ILE ASP ARG TYR THR ALA VAL ALA MET SEQRES 9 A 430 PRO MET LEU TYR ASN THR ARG TYR SER SER LYS ARG ARG SEQRES 10 A 430 VAL THR VAL MET ILE SER ILE VAL TRP VAL LEU SER PHE SEQRES 11 A 430 THR ILE SER CYS PRO LEU LEU PHE GLY LEU ASN ASN ALA SEQRES 12 A 430 ASP GLN ASN GLU CYS ILE ILE ALA ASN PRO ALA PHE VAL SEQRES 13 A 430 VAL TYR SER SER ILE VAL SER PHE TYR VAL PRO PHE ILE SEQRES 14 A 430 VAL THR LEU LEU VAL TYR ILE LYS ILE TYR ILE VAL LEU SEQRES 15 A 430 ARG ARG ARG ARG LYS ARG ASN ILE PHE GLU MET LEU ARG SEQRES 16 A 430 ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP THR SEQRES 17 A 430 GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU THR SEQRES 18 A 430 LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU ASP SEQRES 19 A 430 LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR LYS SEQRES 20 A 430 ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP ALA SEQRES 21 A 430 ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS PRO SEQRES 22 A 430 VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA LEU SEQRES 23 A 430 ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL ALA SEQRES 24 A 430 GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS ARG SEQRES 25 A 430 TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG TRP SEQRES 26 A 430 TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE THR SEQRES 27 A 430 THR PHE ARG THR GLY THR TRP ASP ALA TYR LYS LEU SER SEQRES 28 A 430 GLN GLN LYS GLU LYS LYS ALA THR GLN MET ALA ALA ILE SEQRES 29 A 430 VAL ALA GLY VAL PHE ILE ILE CYS TRP LEU PRO PHE PHE SEQRES 30 A 430 ILE THR HIS ILE LEU ASN ILE HIS CYS ASP CYS ASN ILE SEQRES 31 A 430 PRO PRO VAL LEU TYR SER ALA PHE THR TRP LEU GLY TYR SEQRES 32 A 430 VAL ASN SER ALA VAL ASN PRO ILE ILE TYR THR THR PHE SEQRES 33 A 430 ASN ILE GLU PHE ARG LYS ALA PHE LEU LYS ILE LEU HIS SEQRES 34 A 430 CYS HET 8NU A2001 30 HET PEG A2002 7 HET PEG A2003 7 HET PEG A2004 7 HET OLA A2005 13 HET OLA A2006 12 HET OLA A2007 20 HETNAM 8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1- HETNAM 2 8NU YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2- HETNAM 3 8NU A]PYRIMIDIN-4-ONE HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM OLA OLEIC ACID FORMUL 2 8NU C23 H27 F N4 O2 FORMUL 3 PEG 3(C4 H10 O3) FORMUL 6 OLA 3(C18 H34 O2) FORMUL 9 HOH *16(H2 O) HELIX 1 AA1 ASN A 35 GLU A 62 1 28 HELIX 2 AA2 LYS A 63 GLN A 66 5 4 HELIX 3 AA3 THR A 67 VAL A 87 1 21 HELIX 4 AA4 VAL A 87 GLY A 98 1 12 HELIX 5 AA5 SER A 103 MET A 138 1 36 HELIX 6 AA6 TYR A 146 CYS A 168 1 23 HELIX 7 AA7 PRO A 169 ASN A 176 5 8 HELIX 8 AA8 CYS A 182 ASN A 186 5 5 HELIX 9 AA9 ALA A 188 VAL A 196 1 9 HELIX 10 AB1 PHE A 198 GLU A 1011 1 35 HELIX 11 AB2 SER A 1038 GLY A 1051 1 14 HELIX 12 AB3 THR A 1059 ASN A 1081 1 23 HELIX 13 AB4 LEU A 1084 LEU A 1091 1 8 HELIX 14 AB5 ASP A 1092 ALA A 1112 1 21 HELIX 15 AB6 PHE A 1114 GLN A 1123 1 10 HELIX 16 AB7 ARG A 1125 ALA A 1134 1 10 HELIX 17 AB8 SER A 1136 THR A 1142 1 7 HELIX 18 AB9 THR A 1142 GLY A 1156 1 15 HELIX 19 AC1 GLU A 368 CYS A 399 1 32 HELIX 20 AC2 PRO A 404 ASN A 418 1 15 HELIX 21 AC3 VAL A 421 ASN A 430 1 10 HELIX 22 AC4 ASN A 430 LEU A 441 1 12 SHEET 1 AA1 3 ARG A1014 LYS A1019 0 SHEET 2 AA1 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA1 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SSBOND 1 CYS A 107 CYS A 182 1555 1555 2.03 SSBOND 2 CYS A 399 CYS A 401 1555 1555 2.04 CRYST1 50.979 72.523 151.307 90.00 90.00 90.00 P 21 21 21 4 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 0.019616 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013789 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006609 0.00000 ATOM 1 N ASN A 35 -5.317 -8.666 -16.658 1.00108.95 N ATOM 2 CA ASN A 35 -3.999 -9.279 -16.550 1.00112.41 C ATOM 3 C ASN A 35 -3.770 -9.829 -15.148 1.00103.98 C ATOM 4 O ASN A 35 -4.596 -9.642 -14.253 1.00111.14 O ATOM 5 CB ASN A 35 -2.903 -8.271 -16.904 1.00115.88 C ATOM 6 N TYR A 36 -2.640 -10.512 -14.962 1.00122.79 N ANISOU 6 N TYR A 36 17290 13079 16284 -1997 -3163 -3043 N ATOM 7 CA TYR A 36 -2.284 -11.046 -13.653 1.00105.49 C ANISOU 7 CA TYR A 36 15314 10451 14315 -2168 -3210 -2776 C ATOM 8 C TYR A 36 -1.522 -10.036 -12.804 1.00100.38 C ANISOU 8 C TYR A 36 14564 10022 13555 -2013 -2870 -2480 C ATOM 9 O TYR A 36 -1.767 -9.933 -11.597 1.00 95.60 O ANISOU 9 O TYR A 36 13979 9308 13038 -2297 -2774 -2120 O ATOM 10 CB TYR A 36 -1.455 -12.323 -13.811 1.00 98.01 C ANISOU 10 CB TYR A 36 14721 8957 13564 -1967 -3571 -3071 C ATOM 11 N TYR A 37 -0.606 -9.280 -13.416 1.00105.86 N ANISOU 11 N TYR A 37 15140 11047 14036 -1589 -2687 -2627 N ATOM 12 CA TYR A 37 0.202 -8.334 -12.652 1.00101.50 C ANISOU 12 CA TYR A 37 14496 10678 13392 -1434 -2394 -2372 C ATOM 13 C TYR A 37 -0.596 -7.105 -12.233 1.00 97.18 C ANISOU 13 C TYR A 37 13669 10521 12732 -1638 -2109 -2055 C ATOM 14 O TYR A 37 -0.269 -6.474 -11.221 1.00 92.55 O ANISOU 14 O TYR A 37 13035 9983 12145 -1663 -1908 -1774 O ATOM 15 CB TYR A 37 1.435 -7.931 -13.459 1.00105.43 C ANISOU 15 CB TYR A 37 14938 11423 13698 -962 -2294 -2627 C ATOM 16 CG TYR A 37 2.442 -9.052 -13.603 1.00112.39 C ANISOU 16 CG TYR A 37 16060 11928 14715 -688 -2547 -2949 C ATOM 17 CD1 TYR A 37 2.745 -9.880 -12.528 1.00116.25 C ANISOU 17 CD1 TYR A 37 16804 11893 15472 -778 -2740 -2820 C ATOM 18 CD2 TYR A 37 3.084 -9.291 -14.814 1.00112.70 C ANISOU 18 CD2 TYR A 37 16070 12145 14606 -332 -2615 -3395 C ATOM 19 CE1 TYR A 37 3.662 -10.907 -12.650 1.00117.63 C ANISOU 19 CE1 TYR A 37 17203 11682 15808 -489 -3027 -3136 C ATOM 20 CE2 TYR A 37 4.002 -10.320 -14.944 1.00114.52 C ANISOU 20 CE2 TYR A 37 16488 12042 14980 -35 -2866 -3754 C ATOM 21 CZ TYR A 37 4.287 -11.123 -13.860 1.00116.82 C ANISOU 21 CZ TYR A 37 17037 11766 15584 -99 -3089 -3627 C ATOM 22 OH TYR A 37 5.200 -12.147 -13.987 1.00116.76 O ANISOU 22 OH TYR A 37 17222 11387 15756 236 -3393 -4004 O ATOM 23 N ALA A 38 -1.639 -6.750 -12.985 1.00 96.22 N ANISOU 23 N ALA A 38 13359 10676 12525 -1764 -2113 -2120 N ATOM 24 CA ALA A 38 -2.506 -5.655 -12.566 1.00 90.24 C ANISOU 24 CA ALA A 38 12324 10255 11709 -1946 -1899 -1864 C ATOM 25 C ALA A 38 -3.348 -6.039 -11.356 1.00 93.14 C ANISOU 25 C ALA A 38 12686 10447 12255 -2375 -1898 -1620 C ATOM 26 O ALA A 38 -3.625 -5.191 -10.500 1.00 89.27 O ANISOU 26 O ALA A 38 12015 10164 11737 -2476 -1673 -1375 O ATOM 27 CB ALA A 38 -3.409 -5.222 -13.721 1.00 92.04 C ANISOU 27 CB ALA A 38 12349 10812 11811 -1948 -1956 -2018 C ATOM 28 N THR A 39 -3.759 -7.307 -11.265 1.00101.53 N ANISOU 28 N THR A 39 13946 11141 13491 -2646 -2152 -1687 N ATOM 29 CA THR A 39 -4.521 -7.761 -10.105 1.00 98.62 C ANISOU 29 CA THR A 39 13594 10616 13261 -3121 -2155 -1423 C ATOM 30 C THR A 39 -3.673 -7.706 -8.839 1.00 94.46 C ANISOU 30 C THR A 39 13228 9915 12749 -3111 -2033 -1154 C ATOM 31 O THR A 39 -4.127 -7.220 -7.795 1.00 90.19 O ANISOU 31 O THR A 39 12545 9551 12174 -3363 -1831 -884 O ATOM 32 CB THR A 39 -5.041 -9.178 -10.345 1.00 96.91 C ANISOU 32 CB THR A 39 13602 9983 13235 -3430 -2502 -1538 C ATOM 33 OG1 THR A 39 -5.673 -9.242 -11.631 1.00 99.65 O ANISOU 33 OG1 THR A 39 13821 10489 13554 -3372 -2644 -1841 O ATOM 34 CG2 THR A 39 -6.044 -9.566 -9.272 1.00 85.14 C ANISOU 34 CG2 THR A 39 12068 8436 11847 -4016 -2487 -1245 C ATOM 35 N LEU A 40 -2.434 -8.202 -8.915 1.00 91.92 N ANISOU 35 N LEU A 40 13187 9271 12469 -2807 -2162 -1251 N ATOM 36 CA LEU A 40 -1.537 -8.138 -7.766 1.00 89.55 C ANISOU 36 CA LEU A 40 13043 8803 12179 -2751 -2081 -1015 C ATOM 37 C LEU A 40 -1.335 -6.702 -7.304 1.00 83.76 C ANISOU 37 C LEU A 40 12038 8512 11276 -2605 -1722 -856 C ATOM 38 O LEU A 40 -1.301 -6.429 -6.098 1.00 87.36 O ANISOU 38 O LEU A 40 12497 8987 11709 -2775 -1584 -580 O ATOM 39 CB LEU A 40 -0.191 -8.777 -8.104 1.00 87.94 C ANISOU 39 CB LEU A 40 13114 8249 12051 -2357 -2285 -1222 C ATOM 40 CG LEU A 40 -0.166 -10.273 -8.417 1.00 86.57 C ANISOU 40 CG LEU A 40 13274 7524 12094 -2433 -2707 -1405 C ATOM 41 CD1 LEU A 40 1.260 -10.798 -8.334 1.00 81.27 C ANISOU 41 CD1 LEU A 40 12855 6507 11518 -2029 -2890 -1557 C ATOM 42 CD2 LEU A 40 -1.085 -11.041 -7.480 1.00 87.43 C ANISOU 42 CD2 LEU A 40 13549 7331 12340 -3007 -2857 -1101 C ATOM 43 N LEU A 41 -1.202 -5.770 -8.248 1.00 77.53 N ANISOU 43 N LEU A 41 11027 8075 10356 -2302 -1588 -1023 N ATOM 44 CA LEU A 41 -1.025 -4.372 -7.871 1.00 83.20 C ANISOU 44 CA LEU A 41 11504 9166 10941 -2162 -1296 -879 C ATOM 45 C LEU A 41 -2.242 -3.847 -7.120 1.00 91.88 C ANISOU 45 C LEU A 41 12365 10511 12032 -2501 -1145 -694 C ATOM 46 O LEU A 41 -2.101 -3.145 -6.111 1.00 94.79 O ANISOU 46 O LEU A 41 12646 11017 12354 -2528 -951 -503 O ATOM 47 CB LEU A 41 -0.739 -3.520 -9.108 1.00 84.35 C ANISOU 47 CB LEU A 41 11487 9616 10946 -1830 -1231 -1064 C ATOM 48 CG LEU A 41 0.684 -3.615 -9.668 1.00 84.82 C ANISOU 48 CG LEU A 41 11682 9604 10941 -1449 -1257 -1222 C ATOM 49 CD1 LEU A 41 0.863 -2.686 -10.856 1.00 82.66 C ANISOU 49 CD1 LEU A 41 11233 9703 10473 -1206 -1167 -1345 C ATOM 50 CD2 LEU A 41 1.708 -3.304 -8.588 1.00 84.95 C ANISOU 50 CD2 LEU A 41 11768 9527 10981 -1340 -1134 -1042 C ATOM 51 N THR A 42 -3.447 -4.187 -7.587 1.00 91.95 N ANISOU 51 N THR A 42 12247 10603 12085 -2760 -1237 -778 N ATOM 52 CA THR A 42 -4.651 -3.758 -6.883 1.00 87.42 C ANISOU 52 CA THR A 42 11395 10312 11509 -3092 -1095 -650 C ATOM 53 C THR A 42 -4.741 -4.405 -5.507 1.00 89.21 C ANISOU 53 C THR A 42 11759 10370 11767 -3467 -1059 -402 C ATOM 54 O THR A 42 -5.141 -3.757 -4.533 1.00 90.48 O ANISOU 54 O THR A 42 11720 10805 11853 -3617 -841 -252 O ATOM 55 CB THR A 42 -5.894 -4.085 -7.708 1.00 81.63 C ANISOU 55 CB THR A 42 10483 9703 10829 -3302 -1229 -812 C ATOM 56 OG1 THR A 42 -5.719 -3.600 -9.045 1.00 80.89 O ANISOU 56 OG1 THR A 42 10326 9737 10673 -2956 -1306 -1030 O ATOM 57 CG2 THR A 42 -7.122 -3.427 -7.095 1.00 73.78 C ANISOU 57 CG2 THR A 42 9102 9107 9822 -3566 -1057 -743 C ATOM 58 N LEU A 43 -4.372 -5.685 -5.408 1.00 89.32 N ANISOU 58 N LEU A 43 12123 9933 11882 -3624 -1291 -363 N ATOM 59 CA LEU A 43 -4.291 -6.324 -4.100 1.00 89.41 C ANISOU 59 CA LEU A 43 12339 9733 11900 -3975 -1300 -78 C ATOM 60 C LEU A 43 -3.297 -5.599 -3.203 1.00 85.76 C ANISOU 60 C LEU A 43 11923 9332 11330 -3737 -1117 75 C ATOM 61 O LEU A 43 -3.540 -5.429 -2.003 1.00 86.73 O ANISOU 61 O LEU A 43 12007 9591 11355 -4009 -965 311 O ATOM 62 CB LEU A 43 -3.907 -7.795 -4.254 1.00 92.73 C ANISOU 62 CB LEU A 43 13182 9571 12480 -4106 -1657 -74 C ATOM 63 N LEU A 44 -2.173 -5.155 -3.773 1.00 83.60 N ANISOU 63 N LEU A 44 11715 8995 11055 -3246 -1124 -66 N ATOM 64 CA LEU A 44 -1.214 -4.375 -3.000 1.00 85.11 C ANISOU 64 CA LEU A 44 11914 9267 11155 -3006 -957 53 C ATOM 65 C LEU A 44 -1.839 -3.078 -2.502 1.00 85.13 C ANISOU 65 C LEU A 44 11557 9754 11035 -3039 -660 109 C ATOM 66 O LEU A 44 -1.633 -2.688 -1.347 1.00 86.93 O ANISOU 66 O LEU A 44 11776 10082 11172 -3118 -515 286 O ATOM 67 CB LEU A 44 0.031 -4.082 -3.838 1.00 87.56 C ANISOU 67 CB LEU A 44 12295 9491 11483 -2502 -1005 -135 C ATOM 68 CG LEU A 44 1.048 -3.125 -3.207 1.00 86.61 C ANISOU 68 CG LEU A 44 12129 9496 11281 -2230 -831 -46 C ATOM 69 CD1 LEU A 44 1.618 -3.719 -1.930 1.00 87.91 C ANISOU 69 CD1 LEU A 44 12554 9391 11458 -2363 -905 175 C ATOM 70 CD2 LEU A 44 2.164 -2.764 -4.177 1.00 83.34 C ANISOU 70 CD2 LEU A 44 11712 9091 10864 -1783 -849 -246 C ATOM 71 N ILE A 45 -2.611 -2.400 -3.356 1.00 82.86 N ANISOU 71 N ILE A 45 10974 9766 10745 -2965 -594 -59 N ATOM 72 CA ILE A 45 -3.287 -1.172 -2.940 1.00 83.78 C ANISOU 72 CA ILE A 45 10732 10317 10784 -2961 -364 -56 C ATOM 73 C ILE A 45 -4.154 -1.429 -1.715 1.00 85.75 C ANISOU 73 C ILE A 45 10876 10734 10969 -3402 -243 98 C ATOM 74 O ILE A 45 -4.169 -0.633 -0.767 1.00 85.46 O ANISOU 74 O ILE A 45 10685 10954 10832 -3395 -44 165 O ATOM 75 CB ILE A 45 -4.118 -0.594 -4.101 1.00 80.09 C ANISOU 75 CB ILE A 45 9986 10096 10350 -2847 -391 -260 C ATOM 76 CG1 ILE A 45 -3.232 -0.296 -5.309 1.00 82.72 C ANISOU 76 CG1 ILE A 45 10426 10322 10681 -2446 -492 -386 C ATOM 77 CG2 ILE A 45 -4.845 0.666 -3.657 1.00 71.03 C ANISOU 77 CG2 ILE A 45 8464 9363 9163 -2807 -205 -292 C ATOM 78 CD1 ILE A 45 -3.998 0.221 -6.511 1.00 85.25 C ANISOU 78 CD1 ILE A 45 10525 10865 11002 -2340 -563 -559 C ATOM 79 N ALA A 46 -4.887 -2.544 -1.711 1.00 89.24 N ANISOU 79 N ALA A 46 11398 11053 11455 -3812 -363 150 N ATOM 80 CA ALA A 46 -5.719 -2.875 -0.560 1.00 84.99 C ANISOU 80 CA ALA A 46 10762 10712 10819 -4309 -240 325 C ATOM 81 C ALA A 46 -4.868 -3.120 0.678 1.00 86.02 C ANISOU 81 C ALA A 46 11172 10680 10833 -4395 -199 583 C ATOM 82 O ALA A 46 -5.201 -2.653 1.773 1.00 82.61 O ANISOU 82 O ALA A 46 10575 10580 10232 -4584 19 688 O ATOM 83 CB ALA A 46 -6.581 -4.096 -0.869 1.00 77.37 C ANISOU 83 CB ALA A 46 9868 9590 9938 -4771 -418 360 C ATOM 84 N VAL A 47 -3.758 -3.841 0.522 1.00 84.11 N ANISOU 84 N VAL A 47 11343 9946 10669 -4238 -419 662 N ATOM 85 CA VAL A 47 -2.894 -4.117 1.664 1.00 83.65 C ANISOU 85 CA VAL A 47 11575 9696 10512 -4292 -436 908 C ATOM 86 C VAL A 47 -2.272 -2.829 2.191 1.00 82.63 C ANISOU 86 C VAL A 47 11279 9847 10269 -3948 -212 871 C ATOM 87 O VAL A 47 -2.139 -2.644 3.406 1.00 89.41 O ANISOU 87 O VAL A 47 12171 10845 10957 -4107 -91 1051 O ATOM 88 CB VAL A 47 -1.826 -5.156 1.281 1.00 85.45 C ANISOU 88 CB VAL A 47 12252 9322 10892 -4129 -768 941 C ATOM 89 CG1 VAL A 47 -0.873 -5.397 2.438 1.00 84.04 C ANISOU 89 CG1 VAL A 47 12375 8931 10627 -4135 -829 1190 C ATOM 90 CG2 VAL A 47 -2.490 -6.457 0.863 1.00 89.97 C ANISOU 90 CG2 VAL A 47 13015 9574 11594 -4506 -1029 979 C ATOM 91 N ILE A 48 -1.893 -1.915 1.294 1.00 78.76 N ANISOU 91 N ILE A 48 10618 9450 9859 -3495 -165 645 N ATOM 92 CA ILE A 48 -1.320 -0.643 1.730 1.00 77.79 C ANISOU 92 CA ILE A 48 10338 9559 9659 -3180 16 603 C ATOM 93 C ILE A 48 -2.344 0.158 2.522 1.00 82.81 C ANISOU 93 C ILE A 48 10623 10681 10158 -3375 261 582 C ATOM 94 O ILE A 48 -2.025 0.749 3.560 1.00 85.46 O ANISOU 94 O ILE A 48 10924 11187 10359 -3347 400 647 O ATOM 95 CB ILE A 48 -0.797 0.158 0.525 1.00 76.69 C ANISOU 95 CB ILE A 48 10090 9420 9628 -2722 -7 395 C ATOM 96 CG1 ILE A 48 0.350 -0.582 -0.162 1.00 81.09 C ANISOU 96 CG1 ILE A 48 10957 9571 10283 -2498 -216 373 C ATOM 97 CG2 ILE A 48 -0.339 1.535 0.969 1.00 73.83 C ANISOU 97 CG2 ILE A 48 9552 9290 9212 -2449 157 360 C ATOM 98 CD1 ILE A 48 0.859 0.105 -1.411 1.00 83.26 C ANISOU 98 CD1 ILE A 48 11128 9896 10613 -2110 -227 183 C ATOM 99 N VAL A 49 -3.590 0.189 2.047 1.00 85.62 N ANISOU 99 N VAL A 49 10696 11290 10545 -3560 309 458 N ATOM 100 CA VAL A 49 -4.628 0.950 2.736 1.00 86.41 C ANISOU 100 CA VAL A 49 10399 11901 10530 -3713 539 369 C ATOM 101 C VAL A 49 -5.028 0.256 4.033 1.00 86.76 C ANISOU 101 C VAL A 49 10505 12094 10367 -4215 646 582 C ATOM 102 O VAL A 49 -5.154 0.896 5.083 1.00 84.97 O ANISOU 102 O VAL A 49 10110 12216 9958 -4262 848 578 O ATOM 103 CB VAL A 49 -5.837 1.166 1.811 1.00 85.12 C ANISOU 103 CB VAL A 49 9887 11980 10477 -3747 531 151 C ATOM 104 CG1 VAL A 49 -7.004 1.745 2.592 1.00 88.42 C ANISOU 104 CG1 VAL A 49 9863 12953 10781 -3956 756 30 C ATOM 105 CG2 VAL A 49 -5.456 2.084 0.662 1.00 80.88 C ANISOU 105 CG2 VAL A 49 9274 11370 10087 -3251 439 -34 C ATOM 106 N PHE A 50 -5.229 -1.063 3.980 1.00 87.95 N ANISOU 106 N PHE A 50 10908 11980 10529 -4611 497 773 N ATOM 107 CA PHE A 50 -5.635 -1.794 5.177 1.00 89.88 C ANISOU 107 CA PHE A 50 11255 12333 10561 -5041 554 1009 C ATOM 108 C PHE A 50 -4.604 -1.654 6.289 1.00 92.06 C ANISOU 108 C PHE A 50 11792 12524 10663 -4962 580 1197 C ATOM 109 O PHE A 50 -4.957 -1.394 7.445 1.00 93.62 O ANISOU 109 O PHE A 50 11871 13085 10613 -5087 752 1242 O ATOM 110 CB PHE A 50 -5.857 -3.269 4.846 1.00 88.37 C ANISOU 110 CB PHE A 50 11370 11743 10463 -5313 300 1176 C ATOM 111 CG PHE A 50 -6.166 -4.119 6.048 1.00 91.54 C ANISOU 111 CG PHE A 50 11945 12184 10651 -5658 293 1438 C ATOM 112 CD1 PHE A 50 -7.465 -4.232 6.518 1.00 92.88 C ANISOU 112 CD1 PHE A 50 11823 12793 10672 -5976 452 1419 C ATOM 113 CD2 PHE A 50 -5.157 -4.805 6.708 1.00 90.81 C ANISOU 113 CD2 PHE A 50 12302 11702 10500 -5665 108 1698 C ATOM 114 CE1 PHE A 50 -7.752 -5.011 7.623 1.00 96.10 C ANISOU 114 CE1 PHE A 50 12394 13265 10853 -6335 441 1672 C ATOM 115 CE2 PHE A 50 -5.439 -5.583 7.816 1.00 94.85 C ANISOU 115 CE2 PHE A 50 12982 12260 10797 -6003 73 1952 C ATOM 116 CZ PHE A 50 -6.737 -5.688 8.272 1.00 98.38 C ANISOU 116 CZ PHE A 50 13146 13159 11074 -6358 245 1949 C ATOM 117 N GLY A 51 -3.324 -1.822 5.959 1.00 89.17 N ANISOU 117 N GLY A 51 11775 11692 10415 -4731 395 1283 N ATOM 118 CA GLY A 51 -2.301 -1.796 6.988 1.00 84.51 C ANISOU 118 CA GLY A 51 11458 10976 9676 -4664 370 1475 C ATOM 119 C GLY A 51 -2.075 -0.415 7.573 1.00 79.23 C ANISOU 119 C GLY A 51 10517 10705 8881 -4366 607 1313 C ATOM 120 O GLY A 51 -1.800 -0.278 8.767 1.00 79.21 O ANISOU 120 O GLY A 51 10593 10866 8639 -4497 694 1454 O ATOM 121 N ASN A 52 -2.183 0.626 6.746 1.00 74.87 N ANISOU 121 N ASN A 52 9661 10300 8487 -3969 686 1017 N ATOM 122 CA ASN A 52 -1.869 1.971 7.213 1.00 72.04 C ANISOU 122 CA ASN A 52 9081 10223 8066 -3641 847 847 C ATOM 123 C ASN A 52 -3.057 2.680 7.841 1.00 76.56 C ANISOU 123 C ASN A 52 9223 11393 8475 -3813 1107 674 C ATOM 124 O ASN A 52 -2.860 3.566 8.681 1.00 76.05 O ANISOU 124 O ASN A 52 9026 11599 8272 -3672 1243 574 O ATOM 125 CB ASN A 52 -1.305 2.809 6.069 1.00 68.61 C ANISOU 125 CB ASN A 52 8565 9624 7879 -3132 768 642 C ATOM 126 CG ASN A 52 0.113 2.416 5.715 1.00 79.96 C ANISOU 126 CG ASN A 52 10362 10592 9427 -2882 569 754 C ATOM 127 OD1 ASN A 52 1.065 2.835 6.370 1.00 77.35 O ANISOU 127 OD1 ASN A 52 10144 10206 9041 -2704 566 802 O ATOM 128 ND2 ASN A 52 0.261 1.600 4.681 1.00 80.13 N ANISOU 128 ND2 ASN A 52 10547 10294 9604 -2861 393 767 N ATOM 129 N VAL A 53 -4.286 2.318 7.468 1.00 82.38 N ANISOU 129 N VAL A 53 9715 12360 9224 -4106 1170 606 N ATOM 130 CA VAL A 53 -5.441 2.817 8.209 1.00 86.81 C ANISOU 130 CA VAL A 53 9853 13535 9597 -4309 1419 435 C ATOM 131 C VAL A 53 -5.398 2.300 9.643 1.00 91.28 C ANISOU 131 C VAL A 53 10607 14230 9845 -4566 1474 633 C ATOM 132 O VAL A 53 -5.768 3.009 10.588 1.00 98.44 O ANISOU 132 O VAL A 53 11273 15582 10548 -4528 1653 471 O ATOM 133 CB VAL A 53 -6.751 2.433 7.494 1.00 83.17 C ANISOU 133 CB VAL A 53 9126 13231 9243 -4473 1406 307 C ATOM 134 CG1 VAL A 53 -7.949 2.691 8.387 1.00 78.74 C ANISOU 134 CG1 VAL A 53 8217 13227 8475 -4616 1596 143 C ATOM 135 CG2 VAL A 53 -6.893 3.217 6.198 1.00 79.84 C ANISOU 135 CG2 VAL A 53 8453 12777 9107 -4129 1341 45 C ATOM 136 N LEU A 54 -4.923 1.065 9.827 1.00 86.53 N ANISOU 136 N LEU A 54 10442 13233 9201 -4813 1292 968 N ATOM 137 CA LEU A 54 -4.726 0.529 11.172 1.00 88.26 C ANISOU 137 CA LEU A 54 10891 13520 9123 -5054 1288 1196 C ATOM 138 C LEU A 54 -3.747 1.383 11.968 1.00 86.94 C ANISOU 138 C LEU A 54 10787 13428 8817 -4810 1356 1171 C ATOM 139 O LEU A 54 -4.002 1.722 13.130 1.00 94.33 O ANISOU 139 O LEU A 54 11611 14759 9469 -4901 1496 1127 O ATOM 140 CB LEU A 54 -4.224 -0.914 11.097 1.00 90.28 C ANISOU 140 CB LEU A 54 11637 13240 9427 -5281 1006 1548 C ATOM 141 CG LEU A 54 -5.198 -2.030 10.729 1.00 92.89 C ANISOU 141 CG LEU A 54 11990 13500 9806 -5638 909 1650 C ATOM 142 CD1 LEU A 54 -4.459 -3.354 10.614 1.00 97.20 C ANISOU 142 CD1 LEU A 54 13055 13428 10449 -5757 575 1961 C ATOM 143 CD2 LEU A 54 -6.301 -2.128 11.763 1.00 96.43 C ANISOU 143 CD2 LEU A 54 12213 14478 9948 -5990 1090 1654 C ATOM 144 N VAL A 55 -2.613 1.737 11.356 1.00 84.36 N ANISOU 144 N VAL A 55 10638 12737 8678 -4508 1252 1188 N ATOM 145 CA VAL A 55 -1.593 2.518 12.053 1.00 89.47 C ANISOU 145 CA VAL A 55 11371 13417 9208 -4276 1291 1178 C ATOM 146 C VAL A 55 -2.164 3.838 12.551 1.00 92.31 C ANISOU 146 C VAL A 55 11279 14347 9446 -4112 1550 831 C ATOM 147 O VAL A 55 -1.801 4.314 13.634 1.00 95.44 O ANISOU 147 O VAL A 55 11689 14966 9606 -4066 1624 802 O ATOM 148 CB VAL A 55 -0.374 2.741 11.133 1.00 85.96 C ANISOU 148 CB VAL A 55 11134 12447 9082 -3803 1074 1151 C ATOM 149 CG1 VAL A 55 0.679 3.587 11.829 1.00 76.85 C ANISOU 149 CG1 VAL A 55 10045 11292 7864 -3476 1063 1092 C ATOM 150 CG2 VAL A 55 0.217 1.408 10.697 1.00 86.37 C ANISOU 150 CG2 VAL A 55 11619 11948 9251 -3934 799 1439 C ATOM 151 N CYS A 56 -3.075 4.442 11.786 1.00 85.56 N ANISOU 151 N CYS A 56 10018 13731 8759 -3998 1660 538 N ATOM 152 CA CYS A 56 -3.627 5.737 12.175 1.00 80.56 C ANISOU 152 CA CYS A 56 8941 13592 8075 -3762 1850 148 C ATOM 153 C CYS A 56 -4.603 5.598 13.334 1.00 86.48 C ANISOU 153 C CYS A 56 9514 14821 8522 -4005 1984 66 C ATOM 154 O CYS A 56 -4.495 6.313 14.337 1.00 84.77 O ANISOU 154 O CYS A 56 9186 14923 8102 -3899 2089 -102 O ATOM 155 CB CYS A 56 -4.301 6.398 10.975 1.00 67.26 C ANISOU 155 CB CYS A 56 6920 11917 6720 -3468 1818 -150 C ATOM 156 SG CYS A 56 -3.139 6.859 9.688 1.00 71.11 S ANISOU 156 SG CYS A 56 7652 11761 7605 -2939 1540 -134 S ATOM 157 N MET A 57 -5.565 4.680 13.217 1.00 89.30 N ANISOU 157 N MET A 57 9839 15250 8838 -4343 1978 170 N ATOM 158 CA MET A 57 -6.547 4.508 14.283 1.00 99.11 C ANISOU 158 CA MET A 57 10893 16987 9777 -4621 2115 99 C ATOM 159 C MET A 57 -5.891 4.028 15.570 1.00100.31 C ANISOU 159 C MET A 57 11370 17145 9601 -4843 2094 365 C ATOM 160 O MET A 57 -6.282 4.448 16.665 1.00109.98 O ANISOU 160 O MET A 57 12410 18838 10541 -4909 2235 210 O ATOM 161 CB MET A 57 -7.633 3.529 13.845 1.00106.16 C ANISOU 161 CB MET A 57 11719 17920 10695 -4975 2095 198 C ATOM 162 CG MET A 57 -8.458 4.012 12.672 1.00104.93 C ANISOU 162 CG MET A 57 11195 17843 10830 -4777 2113 -94 C ATOM 163 SD MET A 57 -9.729 2.811 12.239 1.00106.23 S ANISOU 163 SD MET A 57 11291 18073 11000 -5226 2085 28 S ATOM 164 CE MET A 57 -8.718 1.360 11.965 1.00104.77 C ANISOU 164 CE MET A 57 11736 17203 10870 -5491 1838 545 C ATOM 165 N ALA A 58 -4.891 3.151 15.458 1.00 91.70 N ANISOU 165 N ALA A 58 10761 15535 8547 -4945 1896 749 N ATOM 166 CA ALA A 58 -4.253 2.590 16.647 1.00 94.86 C ANISOU 166 CA ALA A 58 11502 15887 8653 -5159 1819 1033 C ATOM 167 C ALA A 58 -3.578 3.673 17.478 1.00 93.98 C ANISOU 167 C ALA A 58 11323 16005 8380 -4887 1912 851 C ATOM 168 O ALA A 58 -3.795 3.769 18.691 1.00 97.13 O ANISOU 168 O ALA A 58 11671 16787 8447 -5049 2002 828 O ATOM 169 CB ALA A 58 -3.240 1.521 16.244 1.00 92.30 C ANISOU 169 CB ALA A 58 11700 14899 8471 -5223 1532 1429 C ATOM 170 N VAL A 59 -2.740 4.492 16.841 1.00 96.30 N ANISOU 170 N VAL A 59 11619 16077 8895 -4483 1883 717 N ATOM 171 CA VAL A 59 -2.102 5.595 17.551 1.00 91.92 C ANISOU 171 CA VAL A 59 10983 15733 8211 -4197 1959 504 C ATOM 172 C VAL A 59 -3.144 6.585 18.045 1.00 91.74 C ANISOU 172 C VAL A 59 10460 16322 8077 -4097 2177 56 C ATOM 173 O VAL A 59 -2.990 7.184 19.117 1.00 99.07 O ANISOU 173 O VAL A 59 11313 17573 8756 -4030 2251 -105 O ATOM 174 CB VAL A 59 -1.062 6.271 16.638 1.00 84.96 C ANISOU 174 CB VAL A 59 10179 14491 7608 -3805 1881 441 C ATOM 175 CG1 VAL A 59 -0.446 7.484 17.318 1.00 88.37 C ANISOU 175 CG1 VAL A 59 10505 15150 7923 -3491 1949 173 C ATOM 176 CG2 VAL A 59 0.009 5.267 16.235 1.00 77.23 C ANISOU 176 CG2 VAL A 59 9704 12913 6729 -3889 1637 864 C ATOM 177 N SER A 60 -4.229 6.759 17.291 1.00 95.26 N ANISOU 177 N SER A 60 10557 16933 8706 -4072 2257 -169 N ATOM 178 CA SER A 60 -5.247 7.733 17.658 1.00 98.05 C ANISOU 178 CA SER A 60 10416 17831 9007 -3917 2417 -638 C ATOM 179 C SER A 60 -6.057 7.307 18.875 1.00104.36 C ANISOU 179 C SER A 60 11113 19121 9420 -4286 2535 -633 C ATOM 180 O SER A 60 -6.732 8.148 19.479 1.00107.43 O ANISOU 180 O SER A 60 11125 20003 9691 -4157 2661 -1033 O ATOM 181 CB SER A 60 -6.183 7.974 16.473 1.00 97.14 C ANISOU 181 CB SER A 60 9973 17730 9205 -3784 2427 -864 C ATOM 182 OG SER A 60 -7.148 8.967 16.770 1.00 99.99 O ANISOU 182 OG SER A 60 9859 18573 9559 -3574 2531 -1349 O ATOM 183 N ARG A 61 -6.003 6.030 19.255 1.00 98.78 N ANISOU 183 N ARG A 61 10729 18286 8518 -4738 2478 -202 N ATOM 184 CA ARG A 61 -6.880 5.512 20.291 1.00103.46 C ANISOU 184 CA ARG A 61 11212 19353 8745 -5156 2589 -162 C ATOM 185 C ARG A 61 -6.159 4.772 21.410 1.00107.55 C ANISOU 185 C ARG A 61 12131 19803 8928 -5464 2513 219 C ATOM 186 O ARG A 61 -6.808 4.395 22.392 1.00117.52 O ANISOU 186 O ARG A 61 13311 21498 9842 -5828 2609 262 O ATOM 187 CB ARG A 61 -7.937 4.590 19.664 1.00104.53 C ANISOU 187 CB ARG A 61 11265 19502 8951 -5497 2593 -37 C ATOM 188 CG ARG A 61 -8.730 5.267 18.557 1.00 96.67 C ANISOU 188 CG ARG A 61 9865 18588 8277 -5209 2647 -407 C ATOM 189 CD ARG A 61 -10.016 4.534 18.248 1.00108.57 C ANISOU 189 CD ARG A 61 11174 20320 9758 -5564 2702 -387 C ATOM 190 NE ARG A 61 -9.801 3.362 17.409 1.00109.71 N ANISOU 190 NE ARG A 61 11662 19943 10079 -5797 2536 11 N ATOM 191 CZ ARG A 61 -10.778 2.566 16.987 1.00115.93 C ANISOU 191 CZ ARG A 61 12357 20800 10890 -6123 2537 93 C ATOM 192 NH1 ARG A 61 -12.034 2.820 17.330 1.00116.46 N ANISOU 192 NH1 ARG A 61 11988 21459 10801 -6264 2710 -185 N ATOM 193 NH2 ARG A 61 -10.501 1.519 16.223 1.00119.11 N ANISOU 193 NH2 ARG A 61 13096 20686 11475 -6303 2354 434 N ATOM 194 N GLU A 62 -4.853 4.558 21.301 1.00 96.97 N ANISOU 194 N GLU A 62 11215 17953 7675 -5333 2333 491 N ATOM 195 CA GLU A 62 -4.083 3.859 22.320 1.00101.43 C ANISOU 195 CA GLU A 62 12192 18393 7956 -5580 2207 858 C ATOM 196 C GLU A 62 -3.184 4.851 23.046 1.00102.22 C ANISOU 196 C GLU A 62 12307 18603 7928 -5257 2227 678 C ATOM 197 O GLU A 62 -2.426 5.591 22.409 1.00 92.57 O ANISOU 197 O GLU A 62 11100 17116 6955 -4842 2178 531 O ATOM 198 CB GLU A 62 -3.246 2.737 21.703 1.00100.84 C ANISOU 198 CB GLU A 62 12621 17618 8074 -5678 1928 1315 C ATOM 199 N LYS A 63 -3.269 4.854 24.378 1.00108.00 N ANISOU 199 N LYS A 63 13040 19738 8259 -5463 2293 691 N ATOM 200 CA LYS A 63 -2.467 5.770 25.183 1.00106.16 C ANISOU 200 CA LYS A 63 12820 19652 7864 -5180 2305 504 C ATOM 201 C LYS A 63 -0.976 5.535 24.970 1.00 98.83 C ANISOU 201 C LYS A 63 12367 18125 7059 -4996 2054 800 C ATOM 202 O LYS A 63 -0.243 6.439 24.552 1.00 90.24 O ANISOU 202 O LYS A 63 11250 16879 6157 -4571 2024 584 O ATOM 203 CB LYS A 63 -2.833 5.616 26.660 1.00114.28 C ANISOU 203 CB LYS A 63 13807 21206 8408 -5502 2401 526 C ATOM 204 N ALA A 64 -0.510 4.312 25.239 1.00108.15 N ANISOU 204 N ALA A 64 13988 18956 8148 -5308 1844 1286 N ATOM 205 CA ALA A 64 0.917 4.011 25.200 1.00103.75 C ANISOU 205 CA ALA A 64 13892 17853 7678 -5142 1563 1569 C ATOM 206 C ALA A 64 1.513 4.169 23.805 1.00 99.33 C ANISOU 206 C ALA A 64 13405 16779 7558 -4812 1452 1552 C ATOM 207 O ALA A 64 2.735 4.041 23.649 1.00 84.58 O ANISOU 207 O ALA A 64 11875 14464 5799 -4615 1215 1732 O ATOM 208 CB ALA A 64 1.164 2.590 25.719 1.00103.60 C ANISOU 208 CB ALA A 64 14310 17538 7516 -5540 1320 2073 C ATOM 209 N LEU A 65 0.685 4.450 22.798 1.00 91.85 N ANISOU 209 N LEU A 65 12140 15902 6858 -4745 1606 1334 N ATOM 210 CA LEU A 65 1.126 4.676 21.429 1.00 92.45 C ANISOU 210 CA LEU A 65 12233 15560 7334 -4450 1535 1288 C ATOM 211 C LEU A 65 1.071 6.143 21.021 1.00 91.55 C ANISOU 211 C LEU A 65 11741 15700 7344 -4047 1715 824 C ATOM 212 O LEU A 65 1.216 6.447 19.835 1.00 98.95 O ANISOU 212 O LEU A 65 12606 16387 8603 -3825 1705 736 O ATOM 213 CB LEU A 65 0.282 3.842 20.465 1.00 91.67 C ANISOU 213 CB LEU A 65 12087 15284 7459 -4662 1529 1402 C ATOM 214 CG LEU A 65 0.533 2.337 20.472 1.00 96.52 C ANISOU 214 CG LEU A 65 13133 15448 8091 -4973 1266 1854 C ATOM 215 CD1 LEU A 65 -0.389 1.627 19.490 1.00101.66 C ANISOU 215 CD1 LEU A 65 13694 15972 8962 -5162 1269 1895 C ATOM 216 CD2 LEU A 65 1.987 2.059 20.143 1.00 88.49 C ANISOU 216 CD2 LEU A 65 12531 13837 7256 -4733 974 2071 C ATOM 217 N GLN A 66 0.870 7.056 21.966 1.00 97.64 N ANISOU 217 N GLN A 66 12271 16951 7878 -3940 1858 509 N ATOM 218 CA GLN A 66 0.729 8.476 21.643 1.00 91.59 C ANISOU 218 CA GLN A 66 11125 16421 7256 -3531 1991 9 C ATOM 219 C GLN A 66 2.014 9.220 22.003 1.00 88.27 C ANISOU 219 C GLN A 66 10883 15873 6783 -3219 1872 -76 C ATOM 220 O GLN A 66 2.081 10.015 22.940 1.00 95.43 O ANISOU 220 O GLN A 66 11654 17116 7488 -3077 1921 -364 O ATOM 221 CB GLN A 66 -0.488 9.060 22.354 1.00 94.21 C ANISOU 221 CB GLN A 66 11011 17366 7418 -3569 2200 -377 C ATOM 222 CG GLN A 66 -1.806 8.615 21.747 1.00 90.38 C ANISOU 222 CG GLN A 66 10255 17032 7053 -3778 2313 -412 C ATOM 223 CD GLN A 66 -3.010 9.067 22.544 1.00 98.45 C ANISOU 223 CD GLN A 66 10853 18690 7865 -3861 2497 -767 C ATOM 224 OE1 GLN A 66 -2.887 9.506 23.689 1.00102.35 O ANISOU 224 OE1 GLN A 66 11295 19524 8070 -3847 2548 -921 O ATOM 225 NE2 GLN A 66 -4.187 8.960 21.941 1.00101.41 N ANISOU 225 NE2 GLN A 66 10914 19243 8376 -3945 2588 -913 N ATOM 226 N THR A 67 3.049 8.942 21.221 1.00 81.40 N ANISOU 226 N THR A 67 10313 14420 6193 -3058 1648 159 N ATOM 227 CA THR A 67 4.366 9.523 21.416 1.00 80.16 C ANISOU 227 CA THR A 67 10341 13928 6189 -2690 1412 112 C ATOM 228 C THR A 67 4.724 10.396 20.219 1.00 81.81 C ANISOU 228 C THR A 67 10385 13739 6959 -2223 1303 -122 C ATOM 229 O THR A 67 4.047 10.388 19.187 1.00 83.11 O ANISOU 229 O THR A 67 10366 13821 7392 -2189 1372 -182 O ATOM 230 CB THR A 67 5.424 8.430 21.618 1.00 74.28 C ANISOU 230 CB THR A 67 10089 12752 5384 -2838 1150 588 C ATOM 231 OG1 THR A 67 5.732 7.823 20.359 1.00 77.15 O ANISOU 231 OG1 THR A 67 10579 12565 6169 -2749 1000 784 O ATOM 232 CG2 THR A 67 4.909 7.358 22.566 1.00 76.90 C ANISOU 232 CG2 THR A 67 10631 13398 5190 -3391 1228 928 C ATOM 233 N THR A 68 5.803 11.165 20.370 1.00 86.60 N ANISOU 233 N THR A 68 11062 14111 7731 -1884 1119 -244 N ATOM 234 CA THR A 68 6.274 11.984 19.259 1.00 81.90 C ANISOU 234 CA THR A 68 10353 13120 7646 -1492 990 -405 C ATOM 235 C THR A 68 6.614 11.116 18.055 1.00 76.38 C ANISOU 235 C THR A 68 9828 11956 7236 -1519 883 -94 C ATOM 236 O THR A 68 6.157 11.379 16.939 1.00 74.99 O ANISOU 236 O THR A 68 9479 11652 7360 -1401 915 -182 O ATOM 237 CB THR A 68 7.490 12.816 19.681 1.00 80.77 C ANISOU 237 CB THR A 68 10291 12786 7611 -1198 788 -526 C ATOM 238 OG1 THR A 68 8.582 11.948 20.014 1.00 75.97 O ANISOU 238 OG1 THR A 68 10037 11917 6911 -1290 604 -182 O ATOM 239 CG2 THR A 68 7.155 13.692 20.878 1.00 83.25 C ANISOU 239 CG2 THR A 68 10436 13561 7636 -1147 872 -884 C ATOM 240 N THR A 69 7.412 10.066 18.270 1.00 78.37 N ANISOU 240 N THR A 69 10426 11955 7395 -1662 733 255 N ATOM 241 CA THR A 69 7.811 9.195 17.168 1.00 78.88 C ANISOU 241 CA THR A 69 10662 11578 7732 -1656 605 503 C ATOM 242 C THR A 69 6.596 8.584 16.482 1.00 78.27 C ANISOU 242 C THR A 69 10482 11594 7664 -1890 759 558 C ATOM 243 O THR A 69 6.522 8.550 15.247 1.00 73.15 O ANISOU 243 O THR A 69 9763 10702 7330 -1761 732 539 O ATOM 244 CB THR A 69 8.748 8.097 17.676 1.00 76.37 C ANISOU 244 CB THR A 69 10733 11000 7285 -1777 388 839 C ATOM 245 OG1 THR A 69 9.982 8.680 18.112 1.00 72.19 O ANISOU 245 OG1 THR A 69 10268 10338 6821 -1513 212 771 O ATOM 246 CG2 THR A 69 9.035 7.083 16.582 1.00 74.02 C ANISOU 246 CG2 THR A 69 10604 10273 7247 -1776 252 1050 C ATOM 247 N ASN A 70 5.625 8.114 17.269 1.00 82.86 N ANISOU 247 N ASN A 70 11039 12561 7884 -2256 925 618 N ATOM 248 CA ASN A 70 4.436 7.496 16.698 1.00 81.91 C ANISOU 248 CA ASN A 70 10800 12565 7757 -2530 1069 672 C ATOM 249 C ASN A 70 3.562 8.494 15.947 1.00 81.00 C ANISOU 249 C ASN A 70 10269 12649 7860 -2327 1221 314 C ATOM 250 O ASN A 70 2.805 8.084 15.063 1.00 74.10 O ANISOU 250 O ASN A 70 9290 11736 7128 -2431 1271 335 O ATOM 251 CB ASN A 70 3.629 6.801 17.798 1.00 79.20 C ANISOU 251 CB ASN A 70 10505 12647 6942 -3020 1221 832 C ATOM 252 CG ASN A 70 4.333 5.581 18.348 1.00 78.28 C ANISOU 252 CG ASN A 70 10856 12250 6638 -3286 1014 1268 C ATOM 253 OD1 ASN A 70 5.224 5.030 17.706 1.00 74.09 O ANISOU 253 OD1 ASN A 70 10588 11183 6379 -3127 762 1443 O ATOM 254 ND2 ASN A 70 3.941 5.152 19.542 1.00 73.15 N ANISOU 254 ND2 ASN A 70 10308 11972 5512 -3692 1103 1439 N ATOM 255 N TYR A 71 3.640 9.786 16.274 1.00 84.07 N ANISOU 255 N TYR A 71 10427 13227 8291 -2033 1261 -20 N ATOM 256 CA TYR A 71 2.933 10.782 15.475 1.00 77.80 C ANISOU 256 CA TYR A 71 9275 12516 7768 -1780 1321 -352 C ATOM 257 C TYR A 71 3.632 11.001 14.143 1.00 70.85 C ANISOU 257 C TYR A 71 8477 11134 7310 -1497 1135 -290 C ATOM 258 O TYR A 71 2.978 11.216 13.117 1.00 65.56 O ANISOU 258 O TYR A 71 7626 10422 6864 -1416 1148 -386 O ATOM 259 CB TYR A 71 2.809 12.094 16.246 1.00 74.68 C ANISOU 259 CB TYR A 71 8632 12431 7314 -1540 1370 -746 C ATOM 260 CG TYR A 71 1.783 12.035 17.350 1.00 80.29 C ANISOU 260 CG TYR A 71 9123 13772 7611 -1796 1612 -924 C ATOM 261 CD1 TYR A 71 0.690 11.189 17.253 1.00 82.22 C ANISOU 261 CD1 TYR A 71 9248 14311 7681 -2164 1796 -825 C ATOM 262 CD2 TYR A 71 1.912 12.814 18.492 1.00 84.10 C ANISOU 262 CD2 TYR A 71 9504 14589 7861 -1688 1658 -1202 C ATOM 263 CE1 TYR A 71 -0.250 11.123 18.258 1.00 91.89 C ANISOU 263 CE1 TYR A 71 10236 16183 8495 -2441 2045 -986 C ATOM 264 CE2 TYR A 71 0.976 12.756 19.503 1.00 85.39 C ANISOU 264 CE2 TYR A 71 9439 15406 7599 -1932 1905 -1392 C ATOM 265 CZ TYR A 71 -0.103 11.907 19.381 1.00 94.33 C ANISOU 265 CZ TYR A 71 10434 16859 8548 -2320 2110 -1275 C ATOM 266 OH TYR A 71 -1.045 11.839 20.381 1.00 99.85 O ANISOU 266 OH TYR A 71 10911 18103 8926 -2541 2275 -1429 O ATOM 267 N LEU A 72 4.963 10.950 14.139 1.00 66.28 N ANISOU 267 N LEU A 72 8155 10205 6825 -1355 960 -134 N ATOM 268 CA LEU A 72 5.688 10.938 12.880 1.00 65.47 C ANISOU 268 CA LEU A 72 8142 9678 7057 -1158 810 -34 C ATOM 269 C LEU A 72 5.520 9.612 12.156 1.00 66.26 C ANISOU 269 C LEU A 72 8411 9590 7173 -1363 790 218 C ATOM 270 O LEU A 72 5.755 9.545 10.947 1.00 70.26 O ANISOU 270 O LEU A 72 8925 9843 7928 -1232 713 248 O ATOM 271 CB LEU A 72 7.166 11.237 13.129 1.00 68.98 C ANISOU 271 CB LEU A 72 8763 9860 7585 -964 640 32 C ATOM 272 CG LEU A 72 7.464 12.668 13.586 1.00 71.02 C ANISOU 272 CG LEU A 72 8861 10200 7924 -721 600 -231 C ATOM 273 CD1 LEU A 72 8.795 12.745 14.308 1.00 68.45 C ANISOU 273 CD1 LEU A 72 8719 9732 7557 -638 454 -157 C ATOM 274 CD2 LEU A 72 7.449 13.618 12.399 1.00 69.98 C ANISOU 274 CD2 LEU A 72 8565 9884 8138 -488 531 -351 C ATOM 275 N ILE A 73 5.112 8.562 12.866 1.00 69.01 N ANISOU 275 N ILE A 73 8906 10062 7254 -1697 844 397 N ATOM 276 CA ILE A 73 4.844 7.288 12.214 1.00 67.68 C ANISOU 276 CA ILE A 73 8907 9691 7118 -1917 795 618 C ATOM 277 C ILE A 73 3.522 7.340 11.460 1.00 71.94 C ANISOU 277 C ILE A 73 9183 10422 7728 -2023 929 489 C ATOM 278 O ILE A 73 3.411 6.809 10.350 1.00 75.02 O ANISOU 278 O ILE A 73 9617 10582 8307 -2015 856 546 O ATOM 279 CB ILE A 73 4.880 6.148 13.249 1.00 69.17 C ANISOU 279 CB ILE A 73 9379 9898 7006 -2275 759 894 C ATOM 280 CG1 ILE A 73 6.327 5.743 13.542 1.00 66.13 C ANISOU 280 CG1 ILE A 73 9319 9150 6659 -2128 522 1069 C ATOM 281 CG2 ILE A 73 4.072 4.944 12.777 1.00 68.47 C ANISOU 281 CG2 ILE A 73 9386 9730 6900 -2615 755 1076 C ATOM 282 CD1 ILE A 73 6.453 4.548 14.461 1.00 67.07 C ANISOU 282 CD1 ILE A 73 9782 9188 6514 -2462 402 1387 C ATOM 283 N VAL A 74 2.507 7.996 12.029 1.00 70.79 N ANISOU 283 N VAL A 74 8739 10720 7436 -2102 1115 280 N ATOM 284 CA VAL A 74 1.244 8.128 11.308 1.00 74.58 C ANISOU 284 CA VAL A 74 8921 11407 8009 -2166 1221 118 C ATOM 285 C VAL A 74 1.392 9.116 10.161 1.00 73.54 C ANISOU 285 C VAL A 74 8633 11099 8211 -1776 1127 -73 C ATOM 286 O VAL A 74 0.708 8.995 9.137 1.00 75.63 O ANISOU 286 O VAL A 74 8769 11334 8631 -1776 1112 -121 O ATOM 287 CB VAL A 74 0.095 8.527 12.256 1.00 73.62 C ANISOU 287 CB VAL A 74 8477 11862 7633 -2350 1446 -95 C ATOM 288 CG1 VAL A 74 0.133 7.692 13.523 1.00 69.23 C ANISOU 288 CG1 VAL A 74 8110 11512 6684 -2747 1535 127 C ATOM 289 CG2 VAL A 74 0.126 10.011 12.581 1.00 69.08 C ANISOU 289 CG2 VAL A 74 7641 11478 7130 -1988 1471 -451 C ATOM 290 N SER A 75 2.276 10.106 10.306 1.00 69.43 N ANISOU 290 N SER A 75 8129 10455 7797 -1464 1043 -169 N ATOM 291 CA SER A 75 2.644 10.933 9.164 1.00 66.75 C ANISOU 291 CA SER A 75 7729 9871 7764 -1146 912 -253 C ATOM 292 C SER A 75 3.278 10.082 8.075 1.00 68.29 C ANISOU 292 C SER A 75 8151 9714 8082 -1158 801 -30 C ATOM 293 O SER A 75 3.025 10.291 6.882 1.00 67.91 O ANISOU 293 O SER A 75 8025 9564 8214 -1048 739 -65 O ATOM 294 CB SER A 75 3.595 12.044 9.605 1.00 65.59 C ANISOU 294 CB SER A 75 7599 9627 7697 -876 823 -350 C ATOM 295 OG SER A 75 4.148 12.722 8.492 1.00 65.64 O ANISOU 295 OG SER A 75 7609 9355 7975 -636 678 -344 O ATOM 296 N LEU A 76 4.099 9.107 8.470 1.00 69.61 N ANISOU 296 N LEU A 76 8600 9702 8145 -1281 755 185 N ATOM 297 CA LEU A 76 4.653 8.169 7.503 1.00 70.39 C ANISOU 297 CA LEU A 76 8904 9490 8352 -1284 641 344 C ATOM 298 C LEU A 76 3.555 7.304 6.898 1.00 71.56 C ANISOU 298 C LEU A 76 9015 9685 8488 -1514 675 369 C ATOM 299 O LEU A 76 3.587 6.994 5.700 1.00 67.72 O ANISOU 299 O LEU A 76 8556 9030 8146 -1442 597 372 O ATOM 300 CB LEU A 76 5.725 7.307 8.170 1.00 71.65 C ANISOU 300 CB LEU A 76 9365 9437 8421 -1339 541 534 C ATOM 301 CG LEU A 76 6.488 6.311 7.296 1.00 73.93 C ANISOU 301 CG LEU A 76 9872 9386 8833 -1283 387 648 C ATOM 302 CD1 LEU A 76 7.050 6.993 6.057 1.00 66.82 C ANISOU 302 CD1 LEU A 76 8859 8395 8135 -1003 352 542 C ATOM 303 CD2 LEU A 76 7.598 5.643 8.104 1.00 66.32 C ANISOU 303 CD2 LEU A 76 9178 8218 7804 -1274 247 796 C ATOM 304 N ALA A 77 2.567 6.918 7.708 1.00 76.17 N ANISOU 304 N ALA A 77 9525 10531 8886 -1810 794 379 N ATOM 305 CA ALA A 77 1.468 6.103 7.203 1.00 75.85 C ANISOU 305 CA ALA A 77 9422 10562 8836 -2078 825 401 C ATOM 306 C ALA A 77 0.603 6.875 6.217 1.00 76.40 C ANISOU 306 C ALA A 77 9182 10781 9066 -1929 853 183 C ATOM 307 O ALA A 77 0.034 6.277 5.295 1.00 74.94 O ANISOU 307 O ALA A 77 8980 10529 8965 -2027 802 189 O ATOM 308 CB ALA A 77 0.618 5.589 8.364 1.00 77.54 C ANISOU 308 CB ALA A 77 9590 11086 8784 -2476 967 470 C ATOM 309 N VAL A 78 0.484 8.192 6.395 1.00 72.57 N ANISOU 309 N VAL A 78 8462 10479 8634 -1687 898 -17 N ATOM 310 CA VAL A 78 -0.263 9.001 5.438 1.00 73.72 C ANISOU 310 CA VAL A 78 8340 10714 8956 -1502 861 -213 C ATOM 311 C VAL A 78 0.492 9.092 4.118 1.00 73.77 C ANISOU 311 C VAL A 78 8495 10392 9143 -1286 699 -137 C ATOM 312 O VAL A 78 -0.108 9.025 3.037 1.00 75.36 O ANISOU 312 O VAL A 78 8606 10583 9444 -1265 631 -185 O ATOM 313 CB VAL A 78 -0.556 10.391 6.030 1.00 69.67 C ANISOU 313 CB VAL A 78 7563 10433 8477 -1281 899 -460 C ATOM 314 CG1 VAL A 78 -1.042 11.346 4.951 1.00 67.83 C ANISOU 314 CG1 VAL A 78 7129 10169 8475 -1016 769 -625 C ATOM 315 CG2 VAL A 78 -1.591 10.281 7.138 1.00 54.88 C ANISOU 315 CG2 VAL A 78 5447 9002 6402 -1505 1086 -609 C ATOM 316 N ALA A 79 1.819 9.239 4.180 1.00 71.40 N ANISOU 316 N ALA A 79 8408 9854 8865 -1136 637 -25 N ATOM 317 CA ALA A 79 2.617 9.243 2.959 1.00 72.25 C ANISOU 317 CA ALA A 79 8642 9715 9095 -969 515 48 C ATOM 318 C ALA A 79 2.382 7.976 2.148 1.00 78.12 C ANISOU 318 C ALA A 79 9512 10348 9824 -1122 472 118 C ATOM 319 O ALA A 79 2.254 8.030 0.919 1.00 82.23 O ANISOU 319 O ALA A 79 10005 10818 10420 -1035 394 87 O ATOM 320 CB ALA A 79 4.097 9.398 3.301 1.00 67.24 C ANISOU 320 CB ALA A 79 8191 8894 8464 -836 476 149 C ATOM 321 N ASP A 80 2.306 6.826 2.820 1.00 70.96 N ANISOU 321 N ASP A 80 8756 9392 8812 -1362 499 214 N ATOM 322 CA ASP A 80 2.041 5.580 2.113 1.00 74.85 C ANISOU 322 CA ASP A 80 9387 9736 9318 -1522 420 263 C ATOM 323 C ASP A 80 0.578 5.468 1.707 1.00 70.40 C ANISOU 323 C ASP A 80 8610 9377 8763 -1703 452 165 C ATOM 324 O ASP A 80 0.275 4.919 0.641 1.00 75.04 O ANISOU 324 O ASP A 80 9225 9874 9413 -1725 358 129 O ATOM 325 CB ASP A 80 2.453 4.386 2.975 1.00 85.13 C ANISOU 325 CB ASP A 80 10957 10859 10529 -1735 379 424 C ATOM 326 CG ASP A 80 3.955 4.316 3.193 1.00 91.73 C ANISOU 326 CG ASP A 80 12008 11459 11389 -1526 293 497 C ATOM 327 OD1 ASP A 80 4.707 4.814 2.326 1.00 90.12 O ANISOU 327 OD1 ASP A 80 11774 11187 11279 -1257 253 424 O ATOM 328 OD2 ASP A 80 4.383 3.762 4.231 1.00 93.76 O ANISOU 328 OD2 ASP A 80 12452 11616 11555 -1644 259 631 O ATOM 329 N LEU A 81 -0.340 5.974 2.535 1.00 74.65 N ANISOU 329 N LEU A 81 8912 10218 9233 -1827 580 91 N ATOM 330 CA LEU A 81 -1.751 5.961 2.159 1.00 71.55 C ANISOU 330 CA LEU A 81 8249 10074 8865 -1978 612 -40 C ATOM 331 C LEU A 81 -2.001 6.765 0.893 1.00 74.65 C ANISOU 331 C LEU A 81 8488 10471 9406 -1709 505 -178 C ATOM 332 O LEU A 81 -2.886 6.418 0.105 1.00 69.21 O ANISOU 332 O LEU A 81 7680 9851 8766 -1803 444 -254 O ATOM 333 CB LEU A 81 -2.611 6.504 3.297 1.00 69.87 C ANISOU 333 CB LEU A 81 7752 10250 8545 -2106 782 -153 C ATOM 334 CG LEU A 81 -3.075 5.485 4.331 1.00 74.99 C ANISOU 334 CG LEU A 81 8452 11043 8999 -2544 901 -27 C ATOM 335 CD1 LEU A 81 -3.852 6.179 5.437 1.00 74.69 C ANISOU 335 CD1 LEU A 81 8087 11477 8814 -2632 1099 -186 C ATOM 336 CD2 LEU A 81 -3.924 4.409 3.669 1.00 73.03 C ANISOU 336 CD2 LEU A 81 8197 10767 8785 -2854 842 14 C ATOM 337 N LEU A 82 -1.237 7.838 0.678 1.00 69.87 N ANISOU 337 N LEU A 82 7892 9789 8867 -1397 460 -196 N ATOM 338 CA LEU A 82 -1.409 8.637 -0.529 1.00 65.99 C ANISOU 338 CA LEU A 82 7299 9280 8492 -1167 327 -272 C ATOM 339 C LEU A 82 -0.757 7.982 -1.740 1.00 70.21 C ANISOU 339 C LEU A 82 8057 9596 9025 -1131 218 -180 C ATOM 340 O LEU A 82 -1.178 8.231 -2.875 1.00 71.57 O ANISOU 340 O LEU A 82 8160 9794 9239 -1047 101 -233 O ATOM 341 CB LEU A 82 -0.848 10.040 -0.313 1.00 59.37 C ANISOU 341 CB LEU A 82 6407 8421 7728 -892 291 -300 C ATOM 342 CG LEU A 82 -1.644 10.851 0.706 1.00 62.33 C ANISOU 342 CG LEU A 82 6510 9044 8130 -856 360 -482 C ATOM 343 CD1 LEU A 82 -1.091 12.261 0.855 1.00 55.10 C ANISOU 343 CD1 LEU A 82 5564 8044 7327 -570 267 -530 C ATOM 344 CD2 LEU A 82 -3.114 10.883 0.314 1.00 64.42 C ANISOU 344 CD2 LEU A 82 6475 9550 8451 -907 325 -667 C ATOM 345 N VAL A 83 0.261 7.147 -1.524 1.00 71.76 N ANISOU 345 N VAL A 83 8510 9592 9162 -1179 238 -64 N ATOM 346 CA VAL A 83 0.813 6.355 -2.620 1.00 69.53 C ANISOU 346 CA VAL A 83 8414 9139 8867 -1147 140 -43 C ATOM 347 C VAL A 83 -0.238 5.394 -3.158 1.00 73.89 C ANISOU 347 C VAL A 83 8937 9715 9422 -1353 76 -116 C ATOM 348 O VAL A 83 -0.404 5.247 -4.375 1.00 79.13 O ANISOU 348 O VAL A 83 9606 10373 10087 -1289 -32 -185 O ATOM 349 CB VAL A 83 2.078 5.608 -2.159 1.00 61.51 C ANISOU 349 CB VAL A 83 7653 7900 7818 -1130 147 49 C ATOM 350 CG1 VAL A 83 2.537 4.623 -3.222 1.00 56.33 C ANISOU 350 CG1 VAL A 83 7164 7084 7153 -1094 37 1 C ATOM 351 CG2 VAL A 83 3.187 6.592 -1.827 1.00 55.01 C ANISOU 351 CG2 VAL A 83 6836 7065 7001 -921 189 106 C ATOM 352 N ALA A 84 -0.973 4.732 -2.264 1.00 63.07 N ANISOU 352 N ALA A 84 7532 8393 8036 -1628 136 -100 N ATOM 353 CA ALA A 84 -1.979 3.777 -2.713 1.00 68.51 C ANISOU 353 CA ALA A 84 8190 9097 8744 -1877 65 -159 C ATOM 354 C ALA A 84 -3.109 4.458 -3.475 1.00 67.78 C ANISOU 354 C ALA A 84 7803 9251 8701 -1831 21 -306 C ATOM 355 O ALA A 84 -3.668 3.871 -4.408 1.00 63.21 O ANISOU 355 O ALA A 84 7217 8653 8146 -1911 -101 -386 O ATOM 356 CB ALA A 84 -2.540 3.003 -1.520 1.00 70.03 C ANISOU 356 CB ALA A 84 8393 9327 8888 -2241 149 -72 C ATOM 357 N THR A 85 -3.449 5.692 -3.108 1.00 59.88 N ANISOU 357 N THR A 85 6561 8463 7726 -1685 85 -362 N ATOM 358 CA THR A 85 -4.630 6.368 -3.632 1.00 70.05 C ANISOU 358 CA THR A 85 7536 9994 9087 -1632 16 -521 C ATOM 359 C THR A 85 -4.329 7.352 -4.758 1.00 73.23 C ANISOU 359 C THR A 85 7938 10354 9531 -1316 -140 -540 C ATOM 360 O THR A 85 -5.144 7.493 -5.674 1.00 73.60 O ANISOU 360 O THR A 85 7844 10501 9619 -1283 -285 -640 O ATOM 361 CB THR A 85 -5.355 7.103 -2.501 1.00 66.86 C ANISOU 361 CB THR A 85 6829 9873 8704 -1660 148 -625 C ATOM 362 OG1 THR A 85 -4.432 7.958 -1.812 1.00 68.22 O ANISOU 362 OG1 THR A 85 7080 9977 8864 -1454 215 -567 O ATOM 363 CG2 THR A 85 -5.948 6.109 -1.519 1.00 61.69 C ANISOU 363 CG2 THR A 85 6117 9358 7964 -2054 299 -604 C ATOM 364 N LEU A 86 -3.186 8.043 -4.718 1.00 62.95 N ANISOU 364 N LEU A 86 6792 8914 8211 -1106 -129 -431 N ATOM 365 CA LEU A 86 -2.875 9.074 -5.699 1.00 69.96 C ANISOU 365 CA LEU A 86 7691 9770 9119 -857 -279 -398 C ATOM 366 C LEU A 86 -1.823 8.663 -6.718 1.00 73.74 C ANISOU 366 C LEU A 86 8430 10102 9484 -805 -327 -290 C ATOM 367 O LEU A 86 -1.627 9.386 -7.700 1.00 78.44 O ANISOU 367 O LEU A 86 9050 10709 10044 -662 -458 -237 O ATOM 368 CB LEU A 86 -2.400 10.356 -5.000 1.00 71.90 C ANISOU 368 CB LEU A 86 7888 9995 9438 -669 -260 -361 C ATOM 369 CG LEU A 86 -3.358 11.015 -4.012 1.00 70.39 C ANISOU 369 CG LEU A 86 7407 9983 9357 -640 -226 -527 C ATOM 370 CD1 LEU A 86 -2.805 12.358 -3.572 1.00 66.08 C ANISOU 370 CD1 LEU A 86 6851 9355 8902 -408 -280 -511 C ATOM 371 CD2 LEU A 86 -4.735 11.169 -4.633 1.00 73.10 C ANISOU 371 CD2 LEU A 86 7488 10505 9781 -625 -371 -694 C ATOM 372 N VAL A 87 -1.137 7.538 -6.512 1.00 71.08 N ANISOU 372 N VAL A 87 8285 9640 9081 -916 -240 -262 N ATOM 373 CA VAL A 87 -0.068 7.087 -7.395 1.00 73.29 C ANISOU 373 CA VAL A 87 8777 9820 9251 -840 -268 -222 C ATOM 374 C VAL A 87 -0.364 5.702 -7.963 1.00 77.64 C ANISOU 374 C VAL A 87 9430 10309 9760 -973 -330 -334 C ATOM 375 O VAL A 87 -0.313 5.497 -9.179 1.00 73.98 O ANISOU 375 O VAL A 87 9018 9892 9199 -916 -433 -399 O ATOM 376 CB VAL A 87 1.295 7.094 -6.673 1.00 71.74 C ANISOU 376 CB VAL A 87 8723 9494 9039 -769 -152 -126 C ATOM 377 CG1 VAL A 87 2.408 6.688 -7.635 1.00 74.66 C ANISOU 377 CG1 VAL A 87 9249 9829 9290 -667 -171 -133 C ATOM 378 CG2 VAL A 87 1.561 8.458 -6.054 1.00 66.12 C ANISOU 378 CG2 VAL A 87 7914 8818 8388 -656 -114 -33 C ATOM 379 N MET A 88 -0.666 4.743 -7.091 1.00 80.11 N ANISOU 379 N MET A 88 9788 10515 10136 -1166 -284 -354 N ATOM 380 CA MET A 88 -0.910 3.374 -7.543 1.00 77.27 C ANISOU 380 CA MET A 88 9560 10025 9773 -1313 -382 -456 C ATOM 381 C MET A 88 -2.014 3.257 -8.587 1.00 74.77 C ANISOU 381 C MET A 88 9120 9842 9447 -1377 -521 -585 C ATOM 382 O MET A 88 -1.856 2.434 -9.508 1.00 75.54 O ANISOU 382 O MET A 88 9351 9858 9492 -1370 -641 -704 O ATOM 383 CB MET A 88 -1.213 2.478 -6.335 1.00 80.86 C ANISOU 383 CB MET A 88 10082 10339 10303 -1575 -337 -400 C ATOM 384 CG MET A 88 -0.060 2.322 -5.349 1.00 81.25 C ANISOU 384 CG MET A 88 10311 10211 10350 -1521 -256 -278 C ATOM 385 SD MET A 88 1.427 1.569 -6.040 1.00 83.45 S ANISOU 385 SD MET A 88 10860 10245 10603 -1297 -355 -350 S ATOM 386 CE MET A 88 0.780 0.002 -6.622 1.00 86.55 C ANISOU 386 CE MET A 88 11408 10421 11056 -1493 -560 -493 C ATOM 387 N PRO A 89 -3.134 3.998 -8.521 1.00 73.85 N ANISOU 387 N PRO A 89 8745 9932 9382 -1424 -534 -603 N ATOM 388 CA PRO A 89 -4.103 3.930 -9.629 1.00 74.48 C ANISOU 388 CA PRO A 89 8707 10146 9448 -1448 -704 -735 C ATOM 389 C PRO A 89 -3.480 4.213 -10.985 1.00 73.67 C ANISOU 389 C PRO A 89 8725 10074 9192 -1237 -816 -758 C ATOM 390 O PRO A 89 -3.834 3.559 -11.972 1.00 74.04 O ANISOU 390 O PRO A 89 8817 10141 9174 -1277 -962 -893 O ATOM 391 CB PRO A 89 -5.142 4.990 -9.248 1.00 73.14 C ANISOU 391 CB PRO A 89 8221 10200 9368 -1431 -703 -747 C ATOM 392 CG PRO A 89 -5.085 5.041 -7.779 1.00 71.74 C ANISOU 392 CG PRO A 89 7982 10016 9258 -1543 -514 -680 C ATOM 393 CD PRO A 89 -3.645 4.834 -7.418 1.00 67.98 C ANISOU 393 CD PRO A 89 7787 9325 8719 -1455 -417 -550 C ATOM 394 N TRP A 90 -2.552 5.170 -11.056 1.00 69.93 N ANISOU 394 N TRP A 90 8302 9624 8643 -1037 -753 -630 N ATOM 395 CA TRP A 90 -1.831 5.402 -12.301 1.00 70.06 C ANISOU 395 CA TRP A 90 8440 9716 8463 -885 -824 -623 C ATOM 396 C TRP A 90 -0.927 4.229 -12.652 1.00 73.43 C ANISOU 396 C TRP A 90 9074 10033 8794 -879 -795 -740 C ATOM 397 O TRP A 90 -0.713 3.948 -13.836 1.00 80.52 O ANISOU 397 O TRP A 90 10046 11036 9511 -815 -885 -849 O ATOM 398 CB TRP A 90 -0.996 6.677 -12.206 1.00 72.68 C ANISOU 398 CB TRP A 90 8778 10094 8744 -730 -758 -431 C ATOM 399 CG TRP A 90 -1.743 7.924 -11.827 1.00 78.23 C ANISOU 399 CG TRP A 90 9301 10853 9571 -681 -825 -337 C ATOM 400 CD1 TRP A 90 -2.061 8.338 -10.567 1.00 78.70 C ANISOU 400 CD1 TRP A 90 9229 10858 9814 -696 -738 -319 C ATOM 401 CD2 TRP A 90 -2.229 8.939 -12.716 1.00 88.37 C ANISOU 401 CD2 TRP A 90 10523 12253 10801 -588 -1022 -264 C ATOM 402 NE1 TRP A 90 -2.729 9.539 -10.616 1.00 79.87 N ANISOU 402 NE1 TRP A 90 9218 11075 10052 -589 -872 -284 N ATOM 403 CE2 TRP A 90 -2.844 9.929 -11.925 1.00 85.91 C ANISOU 403 CE2 TRP A 90 10036 11918 10690 -521 -1067 -232 C ATOM 404 CE3 TRP A 90 -2.213 9.101 -14.106 1.00 93.09 C ANISOU 404 CE3 TRP A 90 11205 12978 11187 -553 -1185 -228 C ATOM 405 CZ2 TRP A 90 -3.436 11.064 -12.476 1.00 91.05 C ANISOU 405 CZ2 TRP A 90 10603 12614 11379 -398 -1303 -166 C ATOM 406 CZ3 TRP A 90 -2.801 10.229 -14.651 1.00 88.71 C ANISOU 406 CZ3 TRP A 90 10584 12483 10637 -467 -1412 -117 C ATOM 407 CH2 TRP A 90 -3.404 11.195 -13.838 1.00 91.05 C ANISOU 407 CH2 TRP A 90 10716 12700 11179 -380 -1486 -87 C ATOM 408 N VAL A 91 -0.382 3.540 -11.646 1.00 69.25 N ANISOU 408 N VAL A 91 8640 9297 8374 -930 -690 -736 N ATOM 409 CA VAL A 91 0.555 2.453 -11.912 1.00 71.26 C ANISOU 409 CA VAL A 91 9090 9406 8578 -872 -701 -873 C ATOM 410 C VAL A 91 -0.181 1.188 -12.341 1.00 81.86 C ANISOU 410 C VAL A 91 10506 10626 9969 -1010 -867 -1076 C ATOM 411 O VAL A 91 0.272 0.468 -13.239 1.00 84.97 O ANISOU 411 O VAL A 91 11020 11005 10261 -913 -961 -1279 O ATOM 412 CB VAL A 91 1.447 2.203 -10.683 1.00 66.23 C ANISOU 412 CB VAL A 91 8549 8562 8051 -856 -583 -782 C ATOM 413 CG1 VAL A 91 2.331 0.984 -10.905 1.00 66.75 C ANISOU 413 CG1 VAL A 91 8812 8434 8116 -769 -652 -961 C ATOM 414 CG2 VAL A 91 2.295 3.427 -10.395 1.00 71.66 C ANISOU 414 CG2 VAL A 91 9171 9373 8685 -712 -442 -614 C ATOM 415 N VAL A 92 -1.320 0.890 -11.713 1.00 76.99 N ANISOU 415 N VAL A 92 9808 9938 9507 -1247 -911 -1047 N ATOM 416 CA VAL A 92 -2.100 -0.267 -12.139 1.00 83.11 C ANISOU 416 CA VAL A 92 10641 10591 10346 -1426 -1092 -1225 C ATOM 417 C VAL A 92 -2.714 -0.014 -13.513 1.00 85.39 C ANISOU 417 C VAL A 92 10837 11112 10496 -1365 -1232 -1373 C ATOM 418 O VAL A 92 -2.760 -0.914 -14.362 1.00 87.20 O ANISOU 418 O VAL A 92 11179 11274 10677 -1366 -1396 -1596 O ATOM 419 CB VAL A 92 -3.160 -0.626 -11.077 1.00 86.97 C ANISOU 419 CB VAL A 92 11035 10994 11015 -1752 -1083 -1133 C ATOM 420 CG1 VAL A 92 -4.059 0.557 -10.774 1.00 88.40 C ANISOU 420 CG1 VAL A 92 10916 11464 11208 -1788 -990 -1030 C ATOM 421 CG2 VAL A 92 -3.984 -1.823 -11.526 1.00 90.14 C ANISOU 421 CG2 VAL A 92 11495 11253 11500 -1988 -1291 -1301 C ATOM 422 N TYR A 93 -3.173 1.217 -13.762 1.00 86.77 N ANISOU 422 N TYR A 93 10817 11548 10602 -1298 -1201 -1261 N ATOM 423 CA TYR A 93 -3.600 1.598 -15.106 1.00 83.84 C ANISOU 423 CA TYR A 93 10389 11409 10056 -1209 -1354 -1357 C ATOM 424 C TYR A 93 -2.477 1.379 -16.111 1.00 80.40 C ANISOU 424 C TYR A 93 10133 11042 9375 -1017 -1359 -1466 C ATOM 425 O TYR A 93 -2.706 0.878 -17.219 1.00 74.40 O ANISOU 425 O TYR A 93 9423 10381 8465 -997 -1517 -1669 O ATOM 426 CB TYR A 93 -4.062 3.059 -15.102 1.00 86.78 C ANISOU 426 CB TYR A 93 10567 11993 10412 -1130 -1345 -1178 C ATOM 427 CG TYR A 93 -4.289 3.683 -16.465 1.00 96.56 C ANISOU 427 CG TYR A 93 11788 13469 11430 -1012 -1516 -1193 C ATOM 428 CD1 TYR A 93 -5.528 3.603 -17.096 1.00 94.66 C ANISOU 428 CD1 TYR A 93 11412 13349 11207 -1088 -1737 -1310 C ATOM 429 CD2 TYR A 93 -3.274 4.383 -17.106 1.00 98.40 C ANISOU 429 CD2 TYR A 93 12135 13829 11423 -849 -1468 -1073 C ATOM 430 CE1 TYR A 93 -5.739 4.185 -18.334 1.00 95.59 C ANISOU 430 CE1 TYR A 93 11537 13682 11100 -983 -1926 -1302 C ATOM 431 CE2 TYR A 93 -3.475 4.965 -18.343 1.00 97.04 C ANISOU 431 CE2 TYR A 93 11974 13889 11007 -780 -1636 -1042 C ATOM 432 CZ TYR A 93 -4.707 4.864 -18.952 1.00 96.39 C ANISOU 432 CZ TYR A 93 11785 13900 10937 -837 -1876 -1153 C ATOM 433 OH TYR A 93 -4.903 5.446 -20.182 1.00 95.53 O ANISOU 433 OH TYR A 93 11712 14022 10562 -771 -2074 -1102 O ATOM 434 N LEU A 94 -1.250 1.724 -15.722 1.00 88.56 N ANISOU 434 N LEU A 94 11244 12051 10355 -879 -1185 -1358 N ATOM 435 CA LEU A 94 -0.090 1.590 -16.592 1.00 90.25 C ANISOU 435 CA LEU A 94 11571 12398 10320 -698 -1144 -1470 C ATOM 436 C LEU A 94 0.187 0.143 -16.984 1.00 86.74 C ANISOU 436 C LEU A 94 11276 11802 9879 -668 -1251 -1798 C ATOM 437 O LEU A 94 0.806 -0.096 -18.027 1.00 79.60 O ANISOU 437 O LEU A 94 10426 11091 8726 -524 -1274 -1999 O ATOM 438 CB LEU A 94 1.131 2.192 -15.893 1.00 91.19 C ANISOU 438 CB LEU A 94 11704 12504 10440 -587 -935 -1297 C ATOM 439 CG LEU A 94 2.362 2.481 -16.745 1.00 96.59 C ANISOU 439 CG LEU A 94 12420 13445 10836 -422 -839 -1342 C ATOM 440 CD1 LEU A 94 1.952 3.241 -17.987 1.00 95.48 C ANISOU 440 CD1 LEU A 94 12233 13639 10407 -435 -921 -1281 C ATOM 441 CD2 LEU A 94 3.366 3.277 -15.931 1.00 94.01 C ANISOU 441 CD2 LEU A 94 12057 13105 10556 -364 -648 -1120 C ATOM 442 N GLU A 95 -0.244 -0.827 -16.175 1.00 91.64 N ANISOU 442 N GLU A 95 11967 12086 10767 -809 -1328 -1863 N ATOM 443 CA GLU A 95 -0.007 -2.228 -16.505 1.00 89.73 C ANISOU 443 CA GLU A 95 11897 11617 10578 -779 -1491 -2179 C ATOM 444 C GLU A 95 -1.104 -2.803 -17.392 1.00 87.68 C ANISOU 444 C GLU A 95 11631 11388 10293 -904 -1724 -2391 C ATOM 445 O GLU A 95 -0.812 -3.568 -18.317 1.00 89.77 O ANISOU 445 O GLU A 95 12002 11667 10441 -784 -1865 -2717 O ATOM 446 CB GLU A 95 0.121 -3.065 -15.229 1.00 87.59 C ANISOU 446 CB GLU A 95 11758 10917 10607 -899 -1515 -2120 C ATOM 447 CG GLU A 95 0.439 -4.539 -15.480 1.00 93.67 C ANISOU 447 CG GLU A 95 12747 11357 11487 -851 -1741 -2438 C ATOM 448 CD GLU A 95 1.851 -4.758 -16.002 1.00102.62 C ANISOU 448 CD GLU A 95 13952 12557 12482 -504 -1707 -2681 C ATOM 449 OE1 GLU A 95 2.722 -3.902 -15.740 1.00104.20 O ANISOU 449 OE1 GLU A 95 14062 12957 12571 -357 -1484 -2527 O ATOM 450 OE2 GLU A 95 2.093 -5.788 -16.670 1.00107.64 O ANISOU 450 OE2 GLU A 95 14717 13056 13125 -376 -1910 -3051 O ATOM 451 N VAL A 96 -2.362 -2.449 -17.129 1.00 78.94 N ANISOU 451 N VAL A 96 10382 10316 9297 -1131 -1774 -2245 N ATOM 452 CA VAL A 96 -3.462 -2.952 -17.947 1.00 80.52 C ANISOU 452 CA VAL A 96 10543 10563 9488 -1267 -2011 -2444 C ATOM 453 C VAL A 96 -3.331 -2.439 -19.375 1.00 85.05 C ANISOU 453 C VAL A 96 11087 11511 9717 -1081 -2072 -2578 C ATOM 454 O VAL A 96 -3.404 -3.209 -20.340 1.00 82.90 O ANISOU 454 O VAL A 96 10906 11266 9327 -1037 -2258 -2893 O ATOM 455 CB VAL A 96 -4.816 -2.561 -17.328 1.00 77.18 C ANISOU 455 CB VAL A 96 9907 10166 9251 -1538 -2032 -2265 C ATOM 456 N VAL A 97 -3.117 -1.130 -19.528 1.00 87.40 N ANISOU 456 N VAL A 97 11271 12099 9836 -979 -1932 -2336 N ATOM 457 CA VAL A 97 -2.995 -0.529 -20.854 1.00 88.86 C ANISOU 457 CA VAL A 97 11446 12664 9653 -847 -1994 -2384 C ATOM 458 C VAL A 97 -1.719 -0.983 -21.554 1.00 90.16 C ANISOU 458 C VAL A 97 11752 12956 9548 -647 -1919 -2608 C ATOM 459 O VAL A 97 -1.694 -1.122 -22.783 1.00 92.93 O ANISOU 459 O VAL A 97 12140 13588 9583 -572 -2028 -2817 O ATOM 460 CB VAL A 97 -3.061 1.005 -20.740 1.00 86.80 C ANISOU 460 CB VAL A 97 11060 12617 9305 -817 -1897 -2025 C ATOM 461 CG1 VAL A 97 -2.893 1.659 -22.106 1.00 88.76 C ANISOU 461 CG1 VAL A 97 11335 13252 9139 -721 -1981 -2009 C ATOM 462 CG2 VAL A 97 -4.372 1.434 -20.086 1.00 86.16 C ANISOU 462 CG2 VAL A 97 10792 12448 9495 -970 -1990 -1884 C ATOM 463 N GLY A 98 -0.650 -1.230 -20.800 1.00 88.15 N ANISOU 463 N GLY A 98 11562 12531 9400 -550 -1740 -2596 N ATOM 464 CA GLY A 98 0.613 -1.604 -21.402 1.00 89.34 C ANISOU 464 CA GLY A 98 11789 12846 9310 -334 -1652 -2837 C ATOM 465 C GLY A 98 1.360 -0.469 -22.059 1.00 91.48 C ANISOU 465 C GLY A 98 11987 13570 9202 -247 -1473 -2660 C ATOM 466 O GLY A 98 2.307 -0.717 -22.810 1.00 93.59 O ANISOU 466 O GLY A 98 12270 14114 9177 -92 -1395 -2892 O ATOM 467 N GLU A 99 0.962 0.772 -21.797 1.00 93.52 N ANISOU 467 N GLU A 99 12159 13918 9455 -352 -1418 -2264 N ATOM 468 CA GLU A 99 1.609 1.938 -22.378 1.00 95.54 C ANISOU 468 CA GLU A 99 12373 14557 9372 -328 -1286 -2022 C ATOM 469 C GLU A 99 1.259 3.151 -21.529 1.00 92.97 C ANISOU 469 C GLU A 99 11976 14105 9244 -422 -1241 -1593 C ATOM 470 O GLU A 99 0.253 3.163 -20.815 1.00 85.82 O ANISOU 470 O GLU A 99 11021 12937 8648 -506 -1345 -1519 O ATOM 471 CB GLU A 99 1.181 2.153 -23.835 1.00 94.86 C ANISOU 471 CB GLU A 99 12308 14866 8868 -355 -1437 -2092 C ATOM 472 N TRP A 100 2.110 4.174 -21.614 1.00 89.68 N ANISOU 472 N TRP A 100 11539 13894 8642 -414 -1089 -1330 N ATOM 473 CA TRP A 100 1.871 5.446 -20.932 1.00 88.27 C ANISOU 473 CA TRP A 100 11308 13606 8625 -483 -1080 -935 C ATOM 474 C TRP A 100 0.892 6.302 -21.742 1.00 91.37 C ANISOU 474 C TRP A 100 11702 14149 8867 -556 -1315 -744 C ATOM 475 O TRP A 100 1.217 7.382 -22.236 1.00 95.09 O ANISOU 475 O TRP A 100 12204 14809 9115 -605 -1334 -453 O ATOM 476 CB TRP A 100 3.188 6.177 -20.702 1.00 86.77 C ANISOU 476 CB TRP A 100 11107 13540 8322 -471 -861 -729 C ATOM 477 CG TRP A 100 4.148 5.471 -19.784 1.00 92.86 C ANISOU 477 CG TRP A 100 11859 14140 9283 -376 -663 -888 C ATOM 478 CD1 TRP A 100 4.731 4.252 -19.983 1.00 99.53 C ANISOU 478 CD1 TRP A 100 12726 15011 10078 -261 -605 -1253 C ATOM 479 CD2 TRP A 100 4.655 5.958 -18.534 1.00 93.04 C ANISOU 479 CD2 TRP A 100 11841 13932 9577 -369 -533 -700 C ATOM 480 NE1 TRP A 100 5.558 3.944 -18.928 1.00 99.78 N ANISOU 480 NE1 TRP A 100 12740 14828 10345 -179 -465 -1286 N ATOM 481 CE2 TRP A 100 5.530 4.975 -18.027 1.00 94.10 C ANISOU 481 CE2 TRP A 100 11981 13965 9809 -254 -408 -944 C ATOM 482 CE3 TRP A 100 4.449 7.125 -17.792 1.00 92.42 C ANISOU 482 CE3 TRP A 100 11726 13714 9675 -431 -538 -373 C ATOM 483 CZ2 TRP A 100 6.198 5.125 -16.811 1.00 92.35 C ANISOU 483 CZ2 TRP A 100 11733 13525 9830 -217 -285 -845 C ATOM 484 CZ3 TRP A 100 5.114 7.273 -16.583 1.00 87.83 C ANISOU 484 CZ3 TRP A 100 11114 12928 9330 -397 -398 -300 C ATOM 485 CH2 TRP A 100 5.977 6.279 -16.107 1.00 90.94 C ANISOU 485 CH2 TRP A 100 11517 13244 9792 -299 -271 -522 C ATOM 486 N LYS A 101 -0.329 5.791 -21.877 1.00 95.15 N ANISOU 486 N LYS A 101 12148 14527 9477 -577 -1521 -906 N ATOM 487 CA LYS A 101 -1.365 6.446 -22.678 1.00 96.45 C ANISOU 487 CA LYS A 101 12300 14824 9522 -619 -1798 -787 C ATOM 488 C LYS A 101 -2.121 7.498 -21.869 1.00 98.53 C ANISOU 488 C LYS A 101 12457 14876 10104 -621 -1907 -529 C ATOM 489 O LYS A 101 -3.351 7.502 -21.813 1.00100.15 O ANISOU 489 O LYS A 101 12553 15004 10495 -628 -2120 -595 O ATOM 490 CB LYS A 101 -2.319 5.405 -23.251 1.00 91.01 C ANISOU 490 CB LYS A 101 11597 14158 8826 -638 -1991 -1116 C ATOM 491 N PHE A 102 -1.377 8.397 -21.223 1.00 92.76 N ANISOU 491 N PHE A 102 11736 14060 9449 -605 -1768 -264 N ATOM 492 CA PHE A 102 -1.943 9.593 -20.620 1.00 93.22 C ANISOU 492 CA PHE A 102 11716 13947 9756 -575 -1904 -18 C ATOM 493 C PHE A 102 -1.857 10.735 -21.628 1.00 91.71 C ANISOU 493 C PHE A 102 11641 13918 9287 -599 -2119 289 C ATOM 494 O PHE A 102 -1.422 10.558 -22.768 1.00103.07 O ANISOU 494 O PHE A 102 13204 15642 10313 -665 -2138 313 O ATOM 495 CB PHE A 102 -1.202 9.983 -19.340 1.00 94.22 C ANISOU 495 CB PHE A 102 11808 13862 10129 -551 -1677 95 C ATOM 496 CG PHE A 102 -0.815 8.827 -18.469 1.00 91.97 C ANISOU 496 CG PHE A 102 11490 13455 10000 -556 -1432 -141 C ATOM 497 CD1 PHE A 102 -1.737 8.243 -17.618 1.00 88.34 C ANISOU 497 CD1 PHE A 102 10903 12822 9841 -574 -1444 -314 C ATOM 498 CD2 PHE A 102 0.483 8.344 -18.477 1.00 88.17 C ANISOU 498 CD2 PHE A 102 11097 13037 9364 -553 -1204 -181 C ATOM 499 CE1 PHE A 102 -1.375 7.184 -16.805 1.00 84.23 C ANISOU 499 CE1 PHE A 102 10394 12156 9452 -611 -1257 -481 C ATOM 500 CE2 PHE A 102 0.849 7.286 -17.667 1.00 83.36 C ANISOU 500 CE2 PHE A 102 10485 12270 8917 -538 -1037 -386 C ATOM 501 CZ PHE A 102 -0.082 6.706 -16.830 1.00 81.83 C ANISOU 501 CZ PHE A 102 10213 11865 9014 -578 -1075 -513 C ATOM 502 N SER A 103 -2.265 11.924 -21.210 1.00 88.70 N ANISOU 502 N SER A 103 11226 13356 9120 -550 -2299 526 N ATOM 503 CA SER A 103 -1.855 13.135 -21.896 1.00 82.43 C ANISOU 503 CA SER A 103 10589 12620 8110 -603 -2476 904 C ATOM 504 C SER A 103 -0.586 13.661 -21.237 1.00 83.13 C ANISOU 504 C SER A 103 10732 12623 8230 -660 -2230 1106 C ATOM 505 O SER A 103 -0.135 13.148 -20.210 1.00 83.31 O ANISOU 505 O SER A 103 10661 12526 8466 -622 -1957 945 O ATOM 506 CB SER A 103 -2.969 14.182 -21.869 1.00 79.20 C ANISOU 506 CB SER A 103 10137 12018 7939 -498 -2879 1043 C ATOM 507 OG SER A 103 -3.335 14.521 -20.542 1.00 76.16 O ANISOU 507 OG SER A 103 9579 11344 8016 -372 -2840 955 O ATOM 508 N ARG A 104 0.009 14.689 -21.845 1.00 84.27 N ANISOU 508 N ARG A 104 11037 12833 8148 -776 -2344 1478 N ATOM 509 CA ARG A 104 1.252 15.212 -21.290 1.00 80.60 C ANISOU 509 CA ARG A 104 10612 12312 7701 -868 -2123 1679 C ATOM 510 C ARG A 104 1.025 15.830 -19.921 1.00 77.44 C ANISOU 510 C ARG A 104 10113 11518 7794 -740 -2150 1682 C ATOM 511 O ARG A 104 1.913 15.783 -19.064 1.00 78.86 O ANISOU 511 O ARG A 104 10250 11620 8096 -755 -1890 1666 O ATOM 512 CB ARG A 104 1.881 16.231 -22.235 1.00 80.66 C ANISOU 512 CB ARG A 104 10815 12469 7362 -1078 -2266 2114 C ATOM 513 CG ARG A 104 3.382 16.383 -22.031 1.00 90.20 C ANISOU 513 CG ARG A 104 12038 13815 8417 -1248 -1948 2260 C ATOM 514 CD ARG A 104 3.766 17.736 -21.446 1.00101.17 C ANISOU 514 CD ARG A 104 13504 14894 10041 -1329 -2089 2624 C ATOM 515 NE ARG A 104 3.451 18.831 -22.359 1.00106.68 N ANISOU 515 NE ARG A 104 14414 15562 10556 -1484 -2476 3046 N ATOM 516 CZ ARG A 104 2.650 19.849 -22.059 1.00108.76 C ANISOU 516 CZ ARG A 104 14758 15416 11150 -1381 -2885 3220 C ATOM 517 NH1 ARG A 104 2.092 19.927 -20.857 1.00104.63 N ANISOU 517 NH1 ARG A 104 14088 14533 11136 -1126 -2918 2984 N ATOM 518 NH2 ARG A 104 2.417 20.795 -22.961 1.00112.28 N ANISOU 518 NH2 ARG A 104 15433 15822 11408 -1532 -3275 3626 N ATOM 519 N ILE A 105 -0.160 16.392 -19.688 1.00 79.98 N ANISOU 519 N ILE A 105 10379 11613 8397 -597 -2469 1666 N ATOM 520 CA ILE A 105 -0.435 17.000 -18.394 1.00 78.38 C ANISOU 520 CA ILE A 105 10057 11079 8646 -452 -2502 1613 C ATOM 521 C ILE A 105 -0.797 15.939 -17.359 1.00 74.85 C ANISOU 521 C ILE A 105 9401 10617 8423 -355 -2239 1232 C ATOM 522 O ILE A 105 -0.422 16.063 -16.189 1.00 73.96 O ANISOU 522 O ILE A 105 9211 10343 8549 -307 -2066 1171 O ATOM 523 CB ILE A 105 -1.528 18.076 -18.534 1.00 77.26 C ANISOU 523 CB ILE A 105 9910 10715 8730 -308 -2966 1710 C ATOM 524 CG1 ILE A 105 -1.691 18.858 -17.227 1.00 76.93 C ANISOU 524 CG1 ILE A 105 9750 10345 9133 -142 -3017 1643 C ATOM 525 CG2 ILE A 105 -2.847 17.465 -18.989 1.00 71.80 C ANISOU 525 CG2 ILE A 105 9083 10142 8055 -199 -3143 1458 C ATOM 526 CD1 ILE A 105 -0.522 19.761 -16.903 1.00 63.79 C ANISOU 526 CD1 ILE A 105 8244 8504 7489 -248 -2982 1938 C ATOM 527 N HIS A 106 -1.425 14.862 -17.789 1.00 78.10 N ANISOU 527 N HIS A 106 9732 11194 8747 -350 -2214 984 N ATOM 528 CA HIS A 106 -1.751 13.780 -16.889 1.00 72.04 C ANISOU 528 CA HIS A 106 8805 10412 8157 -326 -1967 668 C ATOM 529 C HIS A 106 -0.480 13.081 -16.470 1.00 75.28 C ANISOU 529 C HIS A 106 9289 10863 8451 -409 -1617 644 C ATOM 530 O HIS A 106 -0.345 12.663 -15.351 1.00 70.37 O ANISOU 530 O HIS A 106 8580 10125 8032 -389 -1418 503 O ATOM 531 CB HIS A 106 -2.690 12.806 -17.558 1.00 69.03 C ANISOU 531 CB HIS A 106 8344 10182 7701 -344 -2050 426 C ATOM 532 CG HIS A 106 -4.109 13.257 -17.558 1.00 86.66 C ANISOU 532 CG HIS A 106 10420 12382 10122 -239 -2375 359 C ATOM 533 ND1 HIS A 106 -4.497 14.469 -17.043 1.00 93.53 N ANISOU 533 ND1 HIS A 106 11265 13098 11175 -109 -2634 518 N ATOM 534 CD2 HIS A 106 -5.234 12.662 -18.003 1.00 92.54 C ANISOU 534 CD2 HIS A 106 11011 13228 10921 -235 -2507 125 C ATOM 535 CE1 HIS A 106 -5.801 14.602 -17.170 1.00 95.16 C ANISOU 535 CE1 HIS A 106 11292 13325 11539 -1 -2912 369 C ATOM 536 NE2 HIS A 106 -6.273 13.520 -17.751 1.00 94.46 N ANISOU 536 NE2 HIS A 106 11111 13409 11371 -89 -2829 134 N ATOM 537 N CYS A 107 0.459 12.953 -17.384 1.00 74.40 N ANISOU 537 N CYS A 107 9326 10942 8001 -501 -1547 768 N ATOM 538 CA CYS A 107 1.750 12.355 -17.073 1.00 74.41 C ANISOU 538 CA CYS A 107 9366 11008 7898 -548 -1239 725 C ATOM 539 C CYS A 107 2.520 13.220 -16.082 1.00 69.26 C ANISOU 539 C CYS A 107 8705 10174 7436 -541 -1146 902 C ATOM 540 O CYS A 107 3.036 12.718 -15.076 1.00 62.15 O ANISOU 540 O CYS A 107 7754 9173 6688 -508 -936 780 O ATOM 541 CB CYS A 107 2.542 12.149 -18.368 1.00 77.98 C ANISOU 541 CB CYS A 107 9930 11782 7918 -646 -1190 790 C ATOM 542 SG CYS A 107 4.200 11.445 -18.193 1.00 79.49 S ANISOU 542 SG CYS A 107 10119 12137 7945 -673 -832 689 S ATOM 543 N ASP A 108 2.590 14.530 -16.341 1.00 68.64 N ANISOU 543 N ASP A 108 8692 10029 7359 -576 -1335 1195 N ATOM 544 CA ASP A 108 3.289 15.433 -15.430 1.00 67.61 C ANISOU 544 CA ASP A 108 8561 9699 7427 -578 -1293 1358 C ATOM 545 C ASP A 108 2.673 15.405 -14.037 1.00 65.65 C ANISOU 545 C ASP A 108 8180 9208 7557 -435 -1270 1167 C ATOM 546 O ASP A 108 3.393 15.362 -13.033 1.00 66.27 O ANISOU 546 O ASP A 108 8226 9190 7765 -423 -1086 1133 O ATOM 547 CB ASP A 108 3.280 16.856 -15.990 1.00 70.02 C ANISOU 547 CB ASP A 108 8985 9912 7707 -648 -1582 1705 C ATOM 548 CG ASP A 108 4.274 17.047 -17.124 1.00 81.41 C ANISOU 548 CG ASP A 108 10562 11623 8747 -867 -1532 1967 C ATOM 549 OD1 ASP A 108 5.293 16.329 -17.150 1.00 84.41 O ANISOU 549 OD1 ASP A 108 10904 12225 8943 -940 -1226 1879 O ATOM 550 OD2 ASP A 108 4.043 17.922 -17.986 1.00 86.93 O ANISOU 550 OD2 ASP A 108 11397 12326 9305 -971 -1808 2260 O ATOM 551 N ILE A 109 1.341 15.424 -13.956 1.00 63.48 N ANISOU 551 N ILE A 109 7808 8870 7442 -332 -1455 1030 N ATOM 552 CA ILE A 109 0.665 15.365 -12.662 1.00 61.96 C ANISOU 552 CA ILE A 109 7449 8532 7562 -218 -1412 821 C ATOM 553 C ILE A 109 1.015 14.072 -11.937 1.00 63.72 C ANISOU 553 C ILE A 109 7629 8811 7771 -268 -1106 623 C ATOM 554 O ILE A 109 1.341 14.076 -10.743 1.00 59.23 O ANISOU 554 O ILE A 109 7010 8137 7359 -241 -960 564 O ATOM 555 CB ILE A 109 -0.856 15.511 -12.845 1.00 58.03 C ANISOU 555 CB ILE A 109 6805 8039 7204 -115 -1656 674 C ATOM 556 CG1 ILE A 109 -1.212 16.937 -13.262 1.00 58.42 C ANISOU 556 CG1 ILE A 109 6896 7940 7362 -12 -2018 855 C ATOM 557 CG2 ILE A 109 -1.588 15.133 -11.573 1.00 56.04 C ANISOU 557 CG2 ILE A 109 6336 7761 7197 -50 -1535 405 C ATOM 558 CD1 ILE A 109 -2.681 17.131 -13.524 1.00 59.89 C ANISOU 558 CD1 ILE A 109 6917 8142 7695 126 -2302 693 C ATOM 559 N PHE A 110 0.949 12.945 -12.648 1.00 61.78 N ANISOU 559 N PHE A 110 7422 8717 7335 -338 -1034 516 N ATOM 560 CA PHE A 110 1.250 11.658 -12.031 1.00 58.79 C ANISOU 560 CA PHE A 110 7039 8336 6961 -385 -808 335 C ATOM 561 C PHE A 110 2.679 11.622 -11.510 1.00 63.91 C ANISOU 561 C PHE A 110 7771 8939 7574 -390 -613 414 C ATOM 562 O PHE A 110 2.921 11.236 -10.361 1.00 59.44 O ANISOU 562 O PHE A 110 7180 8260 7146 -384 -476 340 O ATOM 563 CB PHE A 110 0.997 10.530 -13.034 1.00 61.38 C ANISOU 563 CB PHE A 110 7419 8803 7098 -442 -823 194 C ATOM 564 CG PHE A 110 1.692 9.234 -12.700 1.00 68.94 C ANISOU 564 CG PHE A 110 8447 9728 8016 -477 -636 42 C ATOM 565 CD1 PHE A 110 1.579 8.662 -11.444 1.00 75.18 C ANISOU 565 CD1 PHE A 110 9204 10361 8999 -508 -525 -42 C ATOM 566 CD2 PHE A 110 2.437 8.573 -13.660 1.00 71.59 C ANISOU 566 CD2 PHE A 110 8887 10201 8115 -474 -595 -28 C ATOM 567 CE1 PHE A 110 2.216 7.472 -11.150 1.00 77.40 C ANISOU 567 CE1 PHE A 110 9585 10560 9264 -531 -416 -161 C ATOM 568 CE2 PHE A 110 3.070 7.383 -13.372 1.00 74.90 C ANISOU 568 CE2 PHE A 110 9372 10553 8534 -462 -477 -203 C ATOM 569 CZ PHE A 110 2.960 6.833 -12.116 1.00 77.70 C ANISOU 569 CZ PHE A 110 9724 10690 9110 -489 -407 -255 C ATOM 570 N VAL A 111 3.641 12.034 -12.340 1.00 65.60 N ANISOU 570 N VAL A 111 8072 9264 7587 -416 -603 568 N ATOM 571 CA VAL A 111 5.043 11.987 -11.930 1.00 66.54 C ANISOU 571 CA VAL A 111 8228 9388 7667 -424 -420 620 C ATOM 572 C VAL A 111 5.288 12.924 -10.757 1.00 60.65 C ANISOU 572 C VAL A 111 7442 8452 7150 -393 -417 727 C ATOM 573 O VAL A 111 6.026 12.590 -9.822 1.00 56.21 O ANISOU 573 O VAL A 111 6872 7814 6670 -370 -270 674 O ATOM 574 CB VAL A 111 5.960 12.317 -13.119 1.00 69.81 C ANISOU 574 CB VAL A 111 8700 10035 7791 -499 -401 765 C ATOM 575 CG1 VAL A 111 7.405 12.336 -12.671 1.00 60.98 C ANISOU 575 CG1 VAL A 111 7563 8955 6651 -512 -214 801 C ATOM 576 CG2 VAL A 111 5.758 11.308 -14.235 1.00 72.95 C ANISOU 576 CG2 VAL A 111 9130 10652 7937 -508 -394 597 C ATOM 577 N THR A 112 4.669 14.106 -10.784 1.00 59.23 N ANISOU 577 N THR A 112 7242 8180 7083 -374 -610 861 N ATOM 578 CA THR A 112 4.789 15.036 -9.664 1.00 65.31 C ANISOU 578 CA THR A 112 7970 8754 8090 -319 -646 910 C ATOM 579 C THR A 112 4.286 14.407 -8.371 1.00 66.52 C ANISOU 579 C THR A 112 8031 8833 8410 -256 -532 693 C ATOM 580 O THR A 112 4.970 14.440 -7.343 1.00 76.31 O ANISOU 580 O THR A 112 9268 9991 9734 -241 -417 676 O ATOM 581 CB THR A 112 4.019 16.321 -9.963 1.00 64.71 C ANISOU 581 CB THR A 112 7889 8561 8139 -269 -933 1031 C ATOM 582 OG1 THR A 112 4.645 17.010 -11.052 1.00 63.73 O ANISOU 582 OG1 THR A 112 7888 8484 7843 -379 -1048 1304 O ATOM 583 CG2 THR A 112 3.995 17.223 -8.744 1.00 62.38 C ANISOU 583 CG2 THR A 112 7534 8052 8116 -171 -994 998 C ATOM 584 N LEU A 113 3.086 13.825 -8.407 1.00 61.29 N ANISOU 584 N LEU A 113 7289 8219 7778 -245 -569 534 N ATOM 585 CA LEU A 113 2.533 13.195 -7.214 1.00 68.29 C ANISOU 585 CA LEU A 113 8081 9085 8780 -248 -453 353 C ATOM 586 C LEU A 113 3.348 11.975 -6.799 1.00 67.53 C ANISOU 586 C LEU A 113 8081 8983 8595 -321 -257 312 C ATOM 587 O LEU A 113 3.573 11.752 -5.604 1.00 68.67 O ANISOU 587 O LEU A 113 8216 9064 8811 -332 -149 267 O ATOM 588 CB LEU A 113 1.075 12.808 -7.454 1.00 70.65 C ANISOU 588 CB LEU A 113 8249 9477 9119 -266 -536 201 C ATOM 589 CG LEU A 113 0.073 13.960 -7.517 1.00 65.91 C ANISOU 589 CG LEU A 113 7497 8872 8673 -146 -751 162 C ATOM 590 CD1 LEU A 113 -1.287 13.451 -7.958 1.00 61.41 C ANISOU 590 CD1 LEU A 113 6776 8439 8118 -174 -840 2 C ATOM 591 CD2 LEU A 113 -0.016 14.648 -6.165 1.00 61.76 C ANISOU 591 CD2 LEU A 113 6853 8287 8324 -59 -710 69 C ATOM 592 N ASP A 114 3.794 11.174 -7.768 1.00 63.91 N ANISOU 592 N ASP A 114 7718 8590 7975 -359 -233 311 N ATOM 593 CA ASP A 114 4.598 9.999 -7.445 1.00 66.05 C ANISOU 593 CA ASP A 114 8086 8820 8191 -384 -102 240 C ATOM 594 C ASP A 114 5.885 10.392 -6.734 1.00 66.08 C ANISOU 594 C ASP A 114 8124 8760 8225 -333 -12 324 C ATOM 595 O ASP A 114 6.262 9.778 -5.730 1.00 69.96 O ANISOU 595 O ASP A 114 8658 9151 8773 -337 64 278 O ATOM 596 CB ASP A 114 4.901 9.208 -8.720 1.00 75.01 C ANISOU 596 CB ASP A 114 9296 10059 9148 -388 -118 174 C ATOM 597 CG ASP A 114 5.951 8.133 -8.509 1.00 75.49 C ANISOU 597 CG ASP A 114 9451 10063 9168 -352 -25 76 C ATOM 598 OD1 ASP A 114 5.746 7.255 -7.648 1.00 74.37 O ANISOU 598 OD1 ASP A 114 9364 9766 9125 -388 -9 -2 O ATOM 599 OD2 ASP A 114 6.981 8.161 -9.214 1.00 76.15 O ANISOU 599 OD2 ASP A 114 9549 10268 9116 -291 20 74 O ATOM 600 N VAL A 115 6.568 11.421 -7.235 1.00 71.45 N ANISOU 600 N VAL A 115 8790 9494 8864 -306 -41 464 N ATOM 601 CA VAL A 115 7.809 11.865 -6.610 1.00 70.24 C ANISOU 601 CA VAL A 115 8641 9297 8749 -279 30 542 C ATOM 602 C VAL A 115 7.535 12.461 -5.234 1.00 69.24 C ANISOU 602 C VAL A 115 8477 9030 8802 -253 19 542 C ATOM 603 O VAL A 115 8.282 12.220 -4.279 1.00 70.91 O ANISOU 603 O VAL A 115 8710 9175 9059 -230 93 521 O ATOM 604 CB VAL A 115 8.536 12.862 -7.531 1.00 65.07 C ANISOU 604 CB VAL A 115 7975 8750 7999 -319 -9 719 C ATOM 605 CG1 VAL A 115 9.683 13.529 -6.804 1.00 60.52 C ANISOU 605 CG1 VAL A 115 7374 8118 7505 -321 36 809 C ATOM 606 CG2 VAL A 115 9.043 12.156 -8.778 1.00 62.56 C ANISOU 606 CG2 VAL A 115 7676 8649 7446 -346 53 680 C ATOM 607 N MET A 116 6.454 13.232 -5.103 1.00 72.12 N ANISOU 607 N MET A 116 8773 9364 9266 -239 -88 539 N ATOM 608 CA MET A 116 6.164 13.889 -3.832 1.00 68.31 C ANISOU 608 CA MET A 116 8226 8792 8936 -191 -103 487 C ATOM 609 C MET A 116 5.814 12.877 -2.746 1.00 67.37 C ANISOU 609 C MET A 116 8106 8685 8808 -232 19 357 C ATOM 610 O MET A 116 6.435 12.860 -1.677 1.00 67.14 O ANISOU 610 O MET A 116 8105 8604 8802 -221 83 349 O ATOM 611 CB MET A 116 5.031 14.896 -4.005 1.00 66.63 C ANISOU 611 CB MET A 116 7912 8564 8843 -129 -269 455 C ATOM 612 CG MET A 116 4.669 15.602 -2.718 1.00 65.54 C ANISOU 612 CG MET A 116 7676 8370 8856 -46 -291 332 C ATOM 613 SD MET A 116 3.209 16.636 -2.880 1.00 73.08 S ANISOU 613 SD MET A 116 8464 9323 9980 85 -509 199 S ATOM 614 CE MET A 116 3.000 17.178 -1.184 1.00 75.15 C ANISOU 614 CE MET A 116 8597 9592 10365 186 -462 -23 C ATOM 615 N MET A 117 4.820 12.023 -3.000 1.00 57.68 N ANISOU 615 N MET A 117 6854 7527 7535 -303 36 271 N ATOM 616 CA MET A 117 4.373 11.084 -1.977 1.00 63.01 C ANISOU 616 CA MET A 117 7536 8218 8187 -406 135 188 C ATOM 617 C MET A 117 5.457 10.093 -1.578 1.00 71.53 C ANISOU 617 C MET A 117 8783 9196 9201 -439 202 236 C ATOM 618 O MET A 117 5.388 9.526 -0.482 1.00 77.20 O ANISOU 618 O MET A 117 9549 9888 9894 -524 260 225 O ATOM 619 CB MET A 117 3.132 10.337 -2.457 1.00 61.50 C ANISOU 619 CB MET A 117 7283 8115 7968 -518 120 103 C ATOM 620 CG MET A 117 1.975 11.258 -2.770 1.00 64.85 C ANISOU 620 CG MET A 117 7509 8654 8476 -463 28 19 C ATOM 621 SD MET A 117 1.790 12.509 -1.489 1.00 62.59 S ANISOU 621 SD MET A 117 7071 8409 8301 -354 37 -66 S ATOM 622 CE MET A 117 0.518 13.548 -2.206 1.00 56.74 C ANISOU 622 CE MET A 117 6109 7754 7697 -221 -153 -189 C ATOM 623 N CYS A 118 6.449 9.867 -2.434 1.00 70.60 N ANISOU 623 N CYS A 118 8747 9036 9042 -373 183 282 N ATOM 624 CA CYS A 118 7.576 9.023 -2.062 1.00 70.67 C ANISOU 624 CA CYS A 118 8885 8946 9021 -346 211 289 C ATOM 625 C CYS A 118 8.689 9.813 -1.387 1.00 68.27 C ANISOU 625 C CYS A 118 8564 8615 8761 -260 228 351 C ATOM 626 O CYS A 118 9.435 9.249 -0.578 1.00 62.32 O ANISOU 626 O CYS A 118 7898 7774 8009 -239 233 351 O ATOM 627 CB CYS A 118 8.121 8.295 -3.295 1.00 71.86 C ANISOU 627 CB CYS A 118 9091 9112 9101 -295 188 239 C ATOM 628 SG CYS A 118 6.974 7.093 -4.021 1.00 68.74 S ANISOU 628 SG CYS A 118 8755 8698 8664 -398 132 131 S ATOM 629 N THR A 119 8.819 11.105 -1.703 1.00 71.90 N ANISOU 629 N THR A 119 8925 9128 9267 -218 203 409 N ATOM 630 CA THR A 119 9.769 11.947 -0.985 1.00 68.93 C ANISOU 630 CA THR A 119 8523 8711 8956 -165 196 461 C ATOM 631 C THR A 119 9.300 12.212 0.440 1.00 62.52 C ANISOU 631 C THR A 119 7704 7861 8191 -175 201 411 C ATOM 632 O THR A 119 10.125 12.295 1.357 1.00 61.89 O ANISOU 632 O THR A 119 7656 7732 8127 -144 202 417 O ATOM 633 CB THR A 119 9.981 13.271 -1.728 1.00 67.89 C ANISOU 633 CB THR A 119 8314 8606 8874 -156 129 558 C ATOM 634 OG1 THR A 119 10.268 13.009 -3.105 1.00 63.88 O ANISOU 634 OG1 THR A 119 7808 8202 8260 -182 139 610 O ATOM 635 CG2 THR A 119 11.148 14.045 -1.129 1.00 64.40 C ANISOU 635 CG2 THR A 119 7848 8113 8507 -132 108 616 C ATOM 636 N ALA A 120 7.987 12.343 0.642 1.00 61.79 N ANISOU 636 N ALA A 120 7547 7824 8105 -218 203 341 N ATOM 637 CA ALA A 120 7.457 12.486 1.992 1.00 59.49 C ANISOU 637 CA ALA A 120 7220 7579 7805 -246 240 258 C ATOM 638 C ALA A 120 7.815 11.283 2.852 1.00 61.28 C ANISOU 638 C ALA A 120 7585 7779 7919 -337 300 286 C ATOM 639 O ALA A 120 8.114 11.433 4.041 1.00 62.06 O ANISOU 639 O ALA A 120 7711 7891 7976 -343 316 271 O ATOM 640 CB ALA A 120 5.943 12.676 1.947 1.00 60.06 C ANISOU 640 CB ALA A 120 7153 7780 7886 -287 251 145 C ATOM 641 N SER A 121 7.784 10.080 2.268 1.00 59.91 N ANISOU 641 N SER A 121 7518 7552 7694 -409 305 325 N ATOM 642 CA SER A 121 8.208 8.889 2.998 1.00 65.17 C ANISOU 642 CA SER A 121 8361 8120 8282 -489 296 378 C ATOM 643 C SER A 121 9.662 9.003 3.431 1.00 68.85 C ANISOU 643 C SER A 121 8900 8486 8775 -361 241 416 C ATOM 644 O SER A 121 10.014 8.643 4.561 1.00 69.48 O ANISOU 644 O SER A 121 9088 8521 8792 -399 214 457 O ATOM 645 CB SER A 121 8.013 7.640 2.137 1.00 61.09 C ANISOU 645 CB SER A 121 7954 7505 7753 -550 254 383 C ATOM 646 OG SER A 121 6.661 7.485 1.747 1.00 71.73 O ANISOU 646 OG SER A 121 9221 8952 9081 -688 290 343 O ATOM 647 N ALA A 122 10.522 9.500 2.544 1.00 66.20 N ANISOU 647 N ALA A 122 8498 8140 8516 -228 219 409 N ATOM 648 CA ALA A 122 11.932 9.632 2.882 1.00 64.09 C ANISOU 648 CA ALA A 122 8247 7817 8288 -115 169 424 C ATOM 649 C ALA A 122 12.144 10.731 3.911 1.00 67.35 C ANISOU 649 C ALA A 122 8599 8264 8729 -99 162 428 C ATOM 650 O ALA A 122 12.870 10.544 4.893 1.00 67.60 O ANISOU 650 O ALA A 122 8699 8245 8739 -68 109 438 O ATOM 651 CB ALA A 122 12.746 9.905 1.621 1.00 62.95 C ANISOU 651 CB ALA A 122 8005 7723 8189 -24 175 411 C ATOM 652 N LEU A 123 11.511 11.886 3.707 1.00 62.65 N ANISOU 652 N LEU A 123 7879 7737 8186 -107 182 403 N ATOM 653 CA LEU A 123 11.661 12.982 4.654 1.00 64.73 C ANISOU 653 CA LEU A 123 8084 8013 8499 -71 145 360 C ATOM 654 C LEU A 123 11.002 12.677 5.993 1.00 68.58 C ANISOU 654 C LEU A 123 8623 8569 8865 -134 179 297 C ATOM 655 O LEU A 123 11.397 13.259 7.008 1.00 65.26 O ANISOU 655 O LEU A 123 8197 8165 8435 -96 140 244 O ATOM 656 CB LEU A 123 11.095 14.271 4.056 1.00 60.03 C ANISOU 656 CB LEU A 123 7361 7429 8020 -42 106 331 C ATOM 657 CG LEU A 123 12.060 15.137 3.236 1.00 62.40 C ANISOU 657 CG LEU A 123 7610 7663 8437 -13 31 421 C ATOM 658 CD1 LEU A 123 12.857 14.325 2.223 1.00 59.85 C ANISOU 658 CD1 LEU A 123 7308 7374 8057 -33 81 508 C ATOM 659 CD2 LEU A 123 11.293 16.248 2.540 1.00 58.42 C ANISOU 659 CD2 LEU A 123 7032 7125 8039 -7 -54 431 C ATOM 660 N ASN A 124 10.015 11.778 6.022 1.00 64.20 N ANISOU 660 N ASN A 124 8115 8078 8200 -253 250 303 N ATOM 661 CA ASN A 124 9.452 11.343 7.295 1.00 68.55 C ANISOU 661 CA ASN A 124 8724 8742 8580 -376 301 282 C ATOM 662 C ASN A 124 10.430 10.450 8.047 1.00 72.49 C ANISOU 662 C ASN A 124 9424 9133 8985 -402 229 393 C ATOM 663 O ASN A 124 10.617 10.600 9.260 1.00 78.80 O ANISOU 663 O ASN A 124 10273 10006 9661 -433 215 382 O ATOM 664 CB ASN A 124 8.129 10.616 7.067 1.00 63.03 C ANISOU 664 CB ASN A 124 8004 8152 7791 -549 391 281 C ATOM 665 CG ASN A 124 6.940 11.540 7.141 1.00 59.12 C ANISOU 665 CG ASN A 124 7283 7866 7312 -543 463 113 C ATOM 666 OD1 ASN A 124 6.864 12.399 8.016 1.00 58.74 O ANISOU 666 OD1 ASN A 124 7141 7941 7236 -481 474 -16 O ATOM 667 ND2 ASN A 124 6.000 11.373 6.218 1.00 59.97 N ANISOU 667 ND2 ASN A 124 7292 8020 7473 -588 490 83 N ATOM 668 N LEU A 125 11.062 9.508 7.343 1.00 66.29 N ANISOU 668 N LEU A 125 8756 8179 8253 -373 162 480 N ATOM 669 CA LEU A 125 12.084 8.682 7.972 1.00 65.46 C ANISOU 669 CA LEU A 125 8836 7929 8106 -343 35 565 C ATOM 670 C LEU A 125 13.243 9.524 8.477 1.00 65.97 C ANISOU 670 C LEU A 125 8840 7991 8234 -191 -37 522 C ATOM 671 O LEU A 125 13.922 9.139 9.436 1.00 61.15 O ANISOU 671 O LEU A 125 8360 7325 7547 -177 -149 572 O ATOM 672 CB LEU A 125 12.583 7.629 6.988 1.00 62.70 C ANISOU 672 CB LEU A 125 8578 7397 7847 -276 -48 593 C ATOM 673 CG LEU A 125 11.555 6.553 6.663 1.00 64.43 C ANISOU 673 CG LEU A 125 8919 7557 8006 -451 -38 646 C ATOM 674 CD1 LEU A 125 12.089 5.633 5.597 1.00 62.96 C ANISOU 674 CD1 LEU A 125 8802 7188 7932 -337 -140 608 C ATOM 675 CD2 LEU A 125 11.214 5.779 7.920 1.00 61.82 C ANISOU 675 CD2 LEU A 125 8799 7183 7505 -650 -100 783 C ATOM 676 N CYS A 126 13.482 10.673 7.849 1.00 67.22 N ANISOU 676 N CYS A 126 8812 8199 8530 -94 0 444 N ATOM 677 CA CYS A 126 14.522 11.568 8.333 1.00 68.85 C ANISOU 677 CA CYS A 126 8945 8402 8814 11 -78 401 C ATOM 678 C CYS A 126 14.084 12.257 9.617 1.00 71.84 C ANISOU 678 C CYS A 126 9323 8885 9086 -30 -78 330 C ATOM 679 O CYS A 126 14.848 12.331 10.588 1.00 74.42 O ANISOU 679 O CYS A 126 9709 9205 9362 8 -177 320 O ATOM 680 CB CYS A 126 14.866 12.592 7.257 1.00 64.79 C ANISOU 680 CB CYS A 126 8252 7891 8474 72 -60 375 C ATOM 681 SG CYS A 126 16.409 13.441 7.561 1.00 69.06 S ANISOU 681 SG CYS A 126 8693 8402 9146 160 -175 353 S ATOM 682 N ALA A 127 12.849 12.762 9.642 1.00 60.58 N ANISOU 682 N ALA A 127 7817 7582 7618 -95 24 250 N ATOM 683 CA ALA A 127 12.322 13.375 10.854 1.00 61.10 C ANISOU 683 CA ALA A 127 7852 7809 7555 -121 44 122 C ATOM 684 C ALA A 127 12.220 12.369 11.990 1.00 65.12 C ANISOU 684 C ALA A 127 8538 8411 7794 -256 52 201 C ATOM 685 O ALA A 127 12.407 12.729 13.158 1.00 65.71 O ANISOU 685 O ALA A 127 8640 8603 7724 -258 16 127 O ATOM 686 CB ALA A 127 10.957 13.996 10.570 1.00 60.25 C ANISOU 686 CB ALA A 127 7585 7843 7462 -141 147 -17 C ATOM 687 N ILE A 128 11.925 11.108 11.673 1.00 64.09 N ANISOU 687 N ILE A 128 8546 8221 7582 -384 77 357 N ATOM 688 CA ILE A 128 11.829 10.083 12.705 1.00 61.38 C ANISOU 688 CA ILE A 128 8417 7924 6982 -558 46 492 C ATOM 689 C ILE A 128 13.184 9.868 13.370 1.00 64.99 C ANISOU 689 C ILE A 128 9025 8241 7426 -455 -148 563 C ATOM 690 O ILE A 128 13.286 9.807 14.600 1.00 69.74 O ANISOU 690 O ILE A 128 9740 8959 7800 -534 -198 591 O ATOM 691 CB ILE A 128 11.271 8.779 12.108 1.00 62.32 C ANISOU 691 CB ILE A 128 8673 7934 7072 -722 61 653 C ATOM 692 CG1 ILE A 128 9.772 8.923 11.836 1.00 63.83 C ANISOU 692 CG1 ILE A 128 8711 8345 7195 -888 252 582 C ATOM 693 CG2 ILE A 128 11.548 7.604 13.028 1.00 64.88 C ANISOU 693 CG2 ILE A 128 9290 8172 7190 -886 -69 860 C ATOM 694 CD1 ILE A 128 9.120 7.668 11.294 1.00 68.59 C ANISOU 694 CD1 ILE A 128 9440 8852 7770 -1092 259 730 C ATOM 695 N SER A 129 14.244 9.756 12.565 1.00 66.20 N ANISOU 695 N SER A 129 9164 8178 7810 -278 -262 578 N ATOM 696 CA SER A 129 15.586 9.611 13.121 1.00 63.02 C ANISOU 696 CA SER A 129 8848 7658 7438 -147 -463 607 C ATOM 697 C SER A 129 15.949 10.799 13.998 1.00 65.47 C ANISOU 697 C SER A 129 9055 8109 7713 -86 -487 474 C ATOM 698 O SER A 129 16.527 10.629 15.078 1.00 65.88 O ANISOU 698 O SER A 129 9234 8177 7619 -82 -631 506 O ATOM 699 CB SER A 129 16.603 9.467 11.995 1.00 65.36 C ANISOU 699 CB SER A 129 9050 7784 7998 39 -538 582 C ATOM 700 OG SER A 129 16.749 10.693 11.302 1.00 65.87 O ANISOU 700 OG SER A 129 8871 7922 8235 114 -445 460 O ATOM 701 N ILE A 130 15.624 12.011 13.546 1.00 64.82 N ANISOU 701 N ILE A 130 8755 8106 7766 -35 -383 319 N ATOM 702 CA ILE A 130 15.959 13.208 14.313 1.00 68.76 C ANISOU 702 CA ILE A 130 9156 8695 8276 36 -439 156 C ATOM 703 C ILE A 130 15.205 13.216 15.636 1.00 70.22 C ANISOU 703 C ILE A 130 9425 9110 8144 -76 -395 92 C ATOM 704 O ILE A 130 15.775 13.502 16.695 1.00 76.17 O ANISOU 704 O ILE A 130 10235 9933 8773 -45 -514 30 O ATOM 705 CB ILE A 130 15.668 14.473 13.488 1.00 69.26 C ANISOU 705 CB ILE A 130 9002 8739 8574 105 -379 19 C ATOM 706 CG1 ILE A 130 16.553 14.504 12.241 1.00 65.51 C ANISOU 706 CG1 ILE A 130 8440 8094 8355 174 -420 103 C ATOM 707 CG2 ILE A 130 15.878 15.716 14.329 1.00 65.28 C ANISOU 707 CG2 ILE A 130 8415 8293 8097 175 -469 -180 C ATOM 708 CD1 ILE A 130 16.380 15.745 11.402 1.00 62.56 C ANISOU 708 CD1 ILE A 130 7895 7673 8203 202 -405 32 C ATOM 709 N ASP A 131 13.909 12.904 15.595 1.00 70.28 N ANISOU 709 N ASP A 131 9426 9280 7998 -221 -219 94 N ATOM 710 CA ASP A 131 13.155 12.749 16.833 1.00 71.28 C ANISOU 710 CA ASP A 131 9617 9702 7763 -378 -141 50 C ATOM 711 C ASP A 131 13.708 11.611 17.677 1.00 75.20 C ANISOU 711 C ASP A 131 10397 10170 8008 -506 -269 283 C ATOM 712 O ASP A 131 13.639 11.660 18.910 1.00 73.14 O ANISOU 712 O ASP A 131 10222 10134 7432 -599 -289 255 O ATOM 713 CB ASP A 131 11.678 12.515 16.525 1.00 70.71 C ANISOU 713 CB ASP A 131 9449 9834 7586 -540 79 22 C ATOM 714 CG ASP A 131 10.820 12.477 17.775 1.00 76.68 C ANISOU 714 CG ASP A 131 10201 10991 7942 -727 206 -66 C ATOM 715 OD1 ASP A 131 10.819 13.472 18.528 1.00 78.05 O ANISOU 715 OD1 ASP A 131 10254 11363 8039 -619 204 -327 O ATOM 716 OD2 ASP A 131 10.140 11.455 18.001 1.00 79.31 O ANISOU 716 OD2 ASP A 131 10647 11456 8030 -996 304 118 O ATOM 717 N ARG A 132 14.264 10.581 17.036 1.00 72.55 N ANISOU 717 N ARG A 132 10215 9556 7796 -504 -380 502 N ATOM 718 CA ARG A 132 14.921 9.521 17.791 1.00 74.39 C ANISOU 718 CA ARG A 132 10739 9679 7847 -579 -584 726 C ATOM 719 C ARG A 132 16.221 10.003 18.417 1.00 74.84 C ANISOU 719 C ARG A 132 10811 9673 7954 -388 -804 656 C ATOM 720 O ARG A 132 16.614 9.507 19.479 1.00 74.70 O ANISOU 720 O ARG A 132 11012 9686 7686 -458 -973 778 O ATOM 721 CB ARG A 132 15.175 8.307 16.894 1.00 71.71 C ANISOU 721 CB ARG A 132 10547 9024 7674 -578 -687 923 C ATOM 722 CG ARG A 132 13.976 7.378 16.715 1.00 69.10 C ANISOU 722 CG ARG A 132 10338 8727 7188 -858 -567 1086 C ATOM 723 CD ARG A 132 13.493 6.832 18.055 1.00 75.91 C ANISOU 723 CD ARG A 132 11433 9782 7627 -1155 -591 1269 C ATOM 724 NE ARG A 132 12.518 7.717 18.686 1.00 77.94 N ANISOU 724 NE ARG A 132 11497 10480 7636 -1291 -337 1099 N ATOM 725 CZ ARG A 132 12.271 7.756 19.990 1.00 77.58 C ANISOU 725 CZ ARG A 132 11552 10740 7186 -1484 -317 1141 C ATOM 726 NH1 ARG A 132 12.931 6.960 20.822 1.00 76.41 N ANISOU 726 NH1 ARG A 132 11728 10477 6827 -1585 -559 1394 N ATOM 727 NH2 ARG A 132 11.366 8.602 20.464 1.00 79.78 N ANISOU 727 NH2 ARG A 132 11599 11452 7261 -1565 -71 912 N ATOM 728 N TYR A 133 16.902 10.960 17.786 1.00 73.32 N ANISOU 728 N TYR A 133 10393 9395 8070 -171 -822 476 N ATOM 729 CA TYR A 133 18.124 11.492 18.379 1.00 72.55 C ANISOU 729 CA TYR A 133 10271 9257 8037 -13 -1032 389 C ATOM 730 C TYR A 133 17.813 12.311 19.624 1.00 76.41 C ANISOU 730 C TYR A 133 10753 10016 8263 -65 -1020 228 C ATOM 731 O TYR A 133 18.475 12.161 20.658 1.00 82.66 O ANISOU 731 O TYR A 133 11685 10852 8869 -54 -1214 255 O ATOM 732 CB TYR A 133 18.894 12.340 17.365 1.00 65.57 C ANISOU 732 CB TYR A 133 9133 8238 7542 169 -1045 254 C ATOM 733 CG TYR A 133 20.160 12.957 17.931 1.00 69.03 C ANISOU 733 CG TYR A 133 9504 8648 8079 305 -1262 149 C ATOM 734 CD1 TYR A 133 21.367 12.268 17.901 1.00 73.59 C ANISOU 734 CD1 TYR A 133 10124 9075 8760 424 -1482 232 C ATOM 735 CD2 TYR A 133 20.148 14.224 18.502 1.00 67.30 C ANISOU 735 CD2 TYR A 133 9162 8546 7862 326 -1271 -61 C ATOM 736 CE1 TYR A 133 22.526 12.825 18.419 1.00 73.44 C ANISOU 736 CE1 TYR A 133 10011 9052 8839 539 -1690 123 C ATOM 737 CE2 TYR A 133 21.303 14.789 19.022 1.00 69.25 C ANISOU 737 CE2 TYR A 133 9341 8760 8209 429 -1488 -164 C ATOM 738 CZ TYR A 133 22.488 14.084 18.977 1.00 74.54 C ANISOU 738 CZ TYR A 133 10039 9309 8975 524 -1689 -64 C ATOM 739 OH TYR A 133 23.637 14.640 19.490 1.00 78.51 O ANISOU 739 OH TYR A 133 10443 9800 9586 618 -1914 -178 O ATOM 740 N THR A 134 16.813 13.190 19.544 1.00 70.79 N ANISOU 740 N THR A 134 9871 9496 7530 -102 -814 34 N ATOM 741 CA THR A 134 16.526 14.064 20.674 1.00 74.84 C ANISOU 741 CA THR A 134 10337 10284 7814 -106 -805 -201 C ATOM 742 C THR A 134 16.021 13.276 21.876 1.00 73.81 C ANISOU 742 C THR A 134 10425 10433 7188 -319 -780 -82 C ATOM 743 O THR A 134 16.266 13.672 23.021 1.00 83.45 O ANISOU 743 O THR A 134 11696 11863 8150 -318 -870 -208 O ATOM 744 CB THR A 134 15.517 15.137 20.270 1.00 81.04 C ANISOU 744 CB THR A 134 10877 11199 8715 -61 -617 -471 C ATOM 745 OG1 THR A 134 14.231 14.541 20.084 1.00 85.24 O ANISOU 745 OG1 THR A 134 11407 11920 9060 -236 -387 -405 O ATOM 746 CG2 THR A 134 15.945 15.803 18.969 1.00 80.96 C ANISOU 746 CG2 THR A 134 10697 10893 9169 91 -653 -505 C ATOM 747 N ALA A 135 15.341 12.151 21.642 1.00 74.49 N ANISOU 747 N ALA A 135 10655 10530 7120 -527 -674 172 N ATOM 748 CA ALA A 135 14.858 11.340 22.756 1.00 76.81 C ANISOU 748 CA ALA A 135 11182 11087 6918 -800 -658 350 C ATOM 749 C ALA A 135 16.008 10.654 23.480 1.00 76.81 C ANISOU 749 C ALA A 135 11471 10921 6791 -787 -978 571 C ATOM 750 O ALA A 135 15.979 10.505 24.707 1.00 82.26 O ANISOU 750 O ALA A 135 12330 11871 7053 -935 -1044 623 O ATOM 751 CB ALA A 135 13.849 10.307 22.259 1.00 69.76 C ANISOU 751 CB ALA A 135 10373 10203 5930 -1063 -492 588 C ATOM 752 N VAL A 136 17.029 10.233 22.739 1.00 76.95 N ANISOU 752 N VAL A 136 11539 10534 7164 -603 -1189 688 N ATOM 753 CA VAL A 136 18.154 9.535 23.350 1.00 82.31 C ANISOU 753 CA VAL A 136 12472 11024 7777 -545 -1537 878 C ATOM 754 C VAL A 136 19.136 10.524 23.967 1.00 82.04 C ANISOU 754 C VAL A 136 12325 11053 7795 -336 -1708 644 C ATOM 755 O VAL A 136 19.554 10.367 25.120 1.00 81.48 O ANISOU 755 O VAL A 136 12446 11103 7411 -382 -1911 704 O ATOM 756 CB VAL A 136 18.839 8.630 22.309 1.00 77.31 C ANISOU 756 CB VAL A 136 11904 9961 7508 -406 -1706 1045 C ATOM 757 CG1 VAL A 136 20.246 8.278 22.755 1.00 77.43 C ANISOU 757 CG1 VAL A 136 12049 9764 7606 -210 -2095 1106 C ATOM 758 CG2 VAL A 136 18.017 7.366 22.083 1.00 72.64 C ANISOU 758 CG2 VAL A 136 11557 9266 6777 -655 -1667 1340 C ATOM 759 N ALA A 137 19.501 11.568 23.224 1.00 77.79 N ANISOU 759 N ALA A 137 11484 10437 7637 -128 -1644 384 N ATOM 760 CA ALA A 137 20.609 12.434 23.603 1.00 80.22 C ANISOU 760 CA ALA A 137 11669 10715 8097 69 -1852 182 C ATOM 761 C ALA A 137 20.209 13.605 24.491 1.00 87.12 C ANISOU 761 C ALA A 137 12440 11898 8765 54 -1780 -115 C ATOM 762 O ALA A 137 21.094 14.243 25.073 1.00 87.55 O ANISOU 762 O ALA A 137 12447 11955 8861 179 -1994 -277 O ATOM 763 CB ALA A 137 21.304 12.975 22.349 1.00 74.40 C ANISOU 763 CB ALA A 137 10663 9730 7877 260 -1849 74 C ATOM 764 N MET A 138 18.922 13.910 24.616 1.00 85.65 N ANISOU 764 N MET A 138 12198 11978 8368 -81 -1504 -224 N ATOM 765 CA MET A 138 18.517 15.099 25.348 1.00 91.36 C ANISOU 765 CA MET A 138 12776 12989 8948 -40 -1439 -587 C ATOM 766 C MET A 138 17.450 14.760 26.377 1.00 93.65 C ANISOU 766 C MET A 138 13184 13730 8670 -264 -1268 -595 C ATOM 767 O MET A 138 16.648 13.844 26.169 1.00 90.32 O ANISOU 767 O MET A 138 12865 13389 8064 -478 -1095 -353 O ATOM 768 CB MET A 138 18.001 16.181 24.387 1.00 94.18 C ANISOU 768 CB MET A 138 12839 13259 9687 83 -1276 -847 C ATOM 769 CG MET A 138 19.095 16.769 23.500 1.00 98.65 C ANISOU 769 CG MET A 138 13264 13452 10767 263 -1446 -874 C ATOM 770 SD MET A 138 18.521 18.077 22.402 1.00105.80 S ANISOU 770 SD MET A 138 13881 14215 12101 371 -1319 -1121 S ATOM 771 CE MET A 138 20.031 18.481 21.533 1.00105.56 C ANISOU 771 CE MET A 138 13744 13805 12559 477 -1542 -1039 C ATOM 772 N PRO A 139 17.425 15.482 27.515 1.00104.46 N ANISOU 772 N PRO A 139 14532 15425 9735 -241 -1315 -880 N ATOM 773 CA PRO A 139 16.509 15.224 28.635 1.00105.59 C ANISOU 773 CA PRO A 139 14765 16095 9259 -469 -1152 -923 C ATOM 774 C PRO A 139 15.042 15.103 28.221 1.00104.65 C ANISOU 774 C PRO A 139 14492 16238 9033 -630 -782 -969 C ATOM 775 O PRO A 139 14.317 16.097 28.261 1.00106.02 O ANISOU 775 O PRO A 139 14394 16653 9234 -519 -617 -1385 O ATOM 776 CB PRO A 139 16.714 16.446 29.535 1.00103.32 C ANISOU 776 CB PRO A 139 14347 16058 8852 -301 -1242 -1390 C ATOM 777 CG PRO A 139 18.112 16.868 29.263 1.00100.62 C ANISOU 777 CG PRO A 139 14009 15289 8934 -72 -1575 -1406 C ATOM 778 CD PRO A 139 18.340 16.603 27.805 1.00 97.12 C ANISOU 778 CD PRO A 139 13483 14389 9030 -4 -1545 -1193 C ATOM 779 N THR A 144 8.716 17.350 27.929 1.00103.31 N ANISOU 779 N THR A 144 12885 17966 8400 -718 631 -2535 N ATOM 780 CA THR A 144 7.590 18.233 28.208 1.00111.55 C ANISOU 780 CA THR A 144 13533 19499 9351 -578 832 -3111 C ATOM 781 C THR A 144 6.396 17.895 27.318 1.00111.78 C ANISOU 781 C THR A 144 13322 19627 9521 -685 1084 -3075 C ATOM 782 O THR A 144 6.556 17.666 26.122 1.00115.16 O ANISOU 782 O THR A 144 13802 19541 10411 -631 1006 -2812 O ATOM 783 CB THR A 144 7.971 19.712 28.006 1.00112.47 C ANISOU 783 CB THR A 144 13477 19327 9931 -104 597 -3618 C ATOM 784 N ARG A 145 5.198 17.868 27.907 1.00112.87 N ANISOU 784 N ARG A 145 13181 20279 9425 -824 1334 -3251 N ATOM 785 CA ARG A 145 4.002 17.509 27.151 1.00114.09 C ANISOU 785 CA ARG A 145 13078 20551 9719 -950 1551 -3212 C ATOM 786 C ARG A 145 3.581 18.596 26.170 1.00118.73 C ANISOU 786 C ARG A 145 13352 20930 10830 -531 1477 -3651 C ATOM 787 O ARG A 145 2.846 18.305 25.221 1.00119.01 O ANISOU 787 O ARG A 145 13234 20913 11072 -582 1585 -3578 O ATOM 788 CB ARG A 145 2.846 17.198 28.104 1.00118.50 C ANISOU 788 CB ARG A 145 13396 21689 9937 -1221 1786 -3270 C ATOM 789 N TYR A 146 4.024 19.834 26.375 1.00121.59 N ANISOU 789 N TYR A 146 13630 21133 11434 -123 1259 -4089 N ATOM 790 CA TYR A 146 3.700 20.948 25.491 1.00117.64 C ANISOU 790 CA TYR A 146 12880 20335 11482 295 1102 -4485 C ATOM 791 C TYR A 146 4.829 21.280 24.526 1.00108.31 C ANISOU 791 C TYR A 146 11951 18428 10772 498 805 -4303 C ATOM 792 O TYR A 146 4.573 21.530 23.344 1.00100.71 O ANISOU 792 O TYR A 146 10911 17078 10275 638 718 -4241 O ATOM 793 CB TYR A 146 3.345 22.185 26.325 1.00124.08 C ANISOU 793 CB TYR A 146 13429 21323 12394 606 974 -5030 C ATOM 794 CG TYR A 146 3.156 23.462 25.533 1.00125.41 C ANISOU 794 CG TYR A 146 13400 21084 13165 1062 702 -5422 C ATOM 795 CD1 TYR A 146 1.920 23.794 24.993 1.00128.22 C ANISOU 795 CD1 TYR A 146 13405 21556 13758 1181 740 -5641 C ATOM 796 CD2 TYR A 146 4.211 24.347 25.345 1.00125.84 C ANISOU 796 CD2 TYR A 146 13634 20614 13563 1355 362 -5554 C ATOM 797 CE1 TYR A 146 1.746 24.966 24.276 1.00131.82 C ANISOU 797 CE1 TYR A 146 13721 21595 14769 1588 432 -5955 C ATOM 798 CE2 TYR A 146 4.047 25.515 24.631 1.00128.03 C ANISOU 798 CE2 TYR A 146 13776 20456 14413 1732 64 -5846 C ATOM 799 CZ TYR A 146 2.815 25.821 24.099 1.00132.64 C ANISOU 799 CZ TYR A 146 14037 21147 15214 1852 92 -6034 C ATOM 800 OH TYR A 146 2.656 26.988 23.388 1.00136.93 O ANISOU 800 OH TYR A 146 14484 21222 16320 2213 -261 -6277 O ATOM 801 N SER A 147 6.076 21.287 25.005 1.00108.97 N ANISOU 801 N SER A 147 12336 18257 10810 490 611 -4125 N ATOM 802 CA SER A 147 7.206 21.602 24.138 1.00104.01 C ANISOU 802 CA SER A 147 11926 16901 10691 633 308 -3860 C ATOM 803 C SER A 147 7.407 20.541 23.065 1.00103.85 C ANISOU 803 C SER A 147 12083 16559 10818 407 370 -3277 C ATOM 804 O SER A 147 7.842 20.861 21.953 1.00 99.45 O ANISOU 804 O SER A 147 11570 15480 10738 539 199 -3123 O ATOM 805 CB SER A 147 8.481 21.758 24.972 1.00101.67 C ANISOU 805 CB SER A 147 11877 16479 10273 647 99 -3814 C ATOM 806 N SER A 148 7.103 19.279 23.375 1.00100.58 N ANISOU 806 N SER A 148 11778 16447 9991 56 598 -2950 N ATOM 807 CA SER A 148 7.325 18.214 22.404 1.00 97.98 C ANISOU 807 CA SER A 148 11636 15794 9798 -147 625 -2427 C ATOM 808 C SER A 148 6.273 18.239 21.303 1.00 88.88 C ANISOU 808 C SER A 148 10254 14611 8905 -117 745 -2472 C ATOM 809 O SER A 148 6.602 18.071 20.125 1.00 80.56 O ANISOU 809 O SER A 148 9283 13109 8218 -74 646 -2217 O ATOM 810 CB SER A 148 7.339 16.858 23.106 1.00103.00 C ANISOU 810 CB SER A 148 12497 16702 9935 -541 771 -2055 C ATOM 811 OG SER A 148 6.089 16.599 23.719 1.00106.17 O ANISOU 811 OG SER A 148 12692 17721 9926 -754 1057 -2228 O ATOM 812 N LYS A 149 5.003 18.446 21.667 1.00 92.05 N ANISOU 812 N LYS A 149 10349 15519 9108 -139 955 -2812 N ATOM 813 CA LYS A 149 3.946 18.506 20.661 1.00 84.26 C ANISOU 813 CA LYS A 149 9110 14536 8369 -93 1046 -2895 C ATOM 814 C LYS A 149 4.192 19.638 19.673 1.00 88.93 C ANISOU 814 C LYS A 149 9627 14634 9529 289 781 -3067 C ATOM 815 O LYS A 149 3.943 19.488 18.470 1.00 93.01 O ANISOU 815 O LYS A 149 10125 14862 10350 308 742 -2887 O ATOM 816 CB LYS A 149 2.585 18.670 21.333 1.00 79.97 C ANISOU 816 CB LYS A 149 8188 14678 7518 -142 1299 -3315 C ATOM 817 N ARG A 150 4.688 20.778 20.160 1.00 87.49 N ANISOU 817 N ARG A 150 9416 14340 9487 578 575 -3405 N ATOM 818 CA ARG A 150 5.060 21.865 19.261 1.00 81.69 C ANISOU 818 CA ARG A 150 8671 13071 9295 893 273 -3505 C ATOM 819 C ARG A 150 6.223 21.474 18.359 1.00 80.21 C ANISOU 819 C ARG A 150 8786 12341 9349 799 130 -2998 C ATOM 820 O ARG A 150 6.317 21.964 17.230 1.00 82.46 O ANISOU 820 O ARG A 150 9071 12222 10039 928 -38 -2909 O ATOM 821 CB ARG A 150 5.411 23.117 20.063 1.00 80.33 C ANISOU 821 CB ARG A 150 8437 12868 9215 1187 52 -3965 C ATOM 822 N ARG A 151 7.111 20.595 18.831 1.00 78.36 N ANISOU 822 N ARG A 151 8802 12110 8862 578 185 -2672 N ATOM 823 CA ARG A 151 8.234 20.166 18.003 1.00 72.71 C ANISOU 823 CA ARG A 151 8328 10937 8361 507 62 -2239 C ATOM 824 C ARG A 151 7.780 19.202 16.916 1.00 79.91 C ANISOU 824 C ARG A 151 9266 11777 9319 342 198 -1915 C ATOM 825 O ARG A 151 8.310 19.226 15.799 1.00 80.42 O ANISOU 825 O ARG A 151 9410 11464 9683 376 87 -1687 O ATOM 826 CB ARG A 151 9.319 19.528 18.870 1.00 74.01 C ANISOU 826 CB ARG A 151 8732 11123 8264 367 34 -2034 C ATOM 827 CG ARG A 151 10.576 19.134 18.110 1.00 82.30 C ANISOU 827 CG ARG A 151 9986 11745 9540 333 -108 -1658 C ATOM 828 CD ARG A 151 11.637 18.577 19.045 1.00 87.06 C ANISOU 828 CD ARG A 151 10798 12374 9905 242 -184 -1509 C ATOM 829 NE ARG A 151 11.097 17.537 19.917 1.00 91.56 N ANISOU 829 NE ARG A 151 11463 13317 10010 18 -7 -1413 N ATOM 830 CZ ARG A 151 11.047 16.249 19.600 1.00 88.57 C ANISOU 830 CZ ARG A 151 11241 12910 9500 -194 83 -1059 C ATOM 831 NH1 ARG A 151 10.538 15.370 20.453 1.00 83.32 N ANISOU 831 NH1 ARG A 151 10680 12574 8402 -440 216 -953 N ATOM 832 NH2 ARG A 151 11.506 15.837 18.428 1.00 87.56 N ANISOU 832 NH2 ARG A 151 11174 12429 9667 -175 27 -816 N ATOM 833 N VAL A 152 6.797 18.350 17.218 1.00 81.56 N ANISOU 833 N VAL A 152 9402 12365 9221 140 437 -1897 N ATOM 834 CA VAL A 152 6.288 17.429 16.204 1.00 81.36 C ANISOU 834 CA VAL A 152 9394 12272 9245 -25 549 -1623 C ATOM 835 C VAL A 152 5.564 18.196 15.104 1.00 80.65 C ANISOU 835 C VAL A 152 9093 12045 9504 168 481 -1785 C ATOM 836 O VAL A 152 5.709 17.888 13.915 1.00 78.73 O ANISOU 836 O VAL A 152 8921 11517 9474 149 431 -1543 O ATOM 837 CB VAL A 152 5.377 16.364 16.843 1.00 80.98 C ANISOU 837 CB VAL A 152 9312 12669 8787 -333 803 -1562 C ATOM 838 CG1 VAL A 152 5.106 15.241 15.863 1.00 82.24 C ANISOU 838 CG1 VAL A 152 9570 12682 8997 -541 871 -1224 C ATOM 839 CG2 VAL A 152 6.004 15.810 18.104 1.00 83.35 C ANISOU 839 CG2 VAL A 152 9819 13145 8703 -511 831 -1443 C ATOM 840 N THR A 153 4.781 19.211 15.482 1.00 84.22 N ANISOU 840 N THR A 153 9285 12700 10015 371 455 -2213 N ATOM 841 CA THR A 153 4.057 20.004 14.492 1.00 78.54 C ANISOU 841 CA THR A 153 8369 11830 9642 587 332 -2387 C ATOM 842 C THR A 153 5.011 20.696 13.525 1.00 75.61 C ANISOU 842 C THR A 153 8160 10910 9657 737 57 -2208 C ATOM 843 O THR A 153 4.738 20.779 12.322 1.00 76.21 O ANISOU 843 O THR A 153 8221 10766 9967 773 -25 -2073 O ATOM 844 CB THR A 153 3.168 21.031 15.195 1.00 80.46 C ANISOU 844 CB THR A 153 8306 12365 9901 832 300 -2933 C ATOM 845 OG1 THR A 153 2.144 20.354 15.937 1.00 82.11 O ANISOU 845 OG1 THR A 153 8305 13162 9733 652 595 -3096 O ATOM 846 CG2 THR A 153 2.527 21.976 14.186 1.00 77.79 C ANISOU 846 CG2 THR A 153 7796 11785 9977 1109 80 -3121 C ATOM 847 N VAL A 154 6.141 21.193 14.030 1.00 73.65 N ANISOU 847 N VAL A 154 8065 10459 9460 799 -90 -2194 N ATOM 848 CA VAL A 154 7.112 21.843 13.156 1.00 71.40 C ANISOU 848 CA VAL A 154 7922 9692 9516 880 -337 -2000 C ATOM 849 C VAL A 154 7.787 20.821 12.246 1.00 67.73 C ANISOU 849 C VAL A 154 7638 9069 9028 675 -255 -1548 C ATOM 850 O VAL A 154 8.007 21.079 11.057 1.00 61.81 O ANISOU 850 O VAL A 154 6927 8041 8515 690 -370 -1361 O ATOM 851 CB VAL A 154 8.137 22.627 13.993 1.00 65.37 C ANISOU 851 CB VAL A 154 7244 8781 8811 974 -518 -2127 C ATOM 852 CG1 VAL A 154 9.256 23.154 13.108 1.00 56.93 C ANISOU 852 CG1 VAL A 154 6321 7254 8055 968 -742 -1864 C ATOM 853 CG2 VAL A 154 7.453 23.767 14.722 1.00 60.75 C ANISOU 853 CG2 VAL A 154 6475 8294 8312 1228 -654 -2627 C ATOM 854 N MET A 155 8.122 19.645 12.784 1.00 69.04 N ANISOU 854 N MET A 155 7921 9413 8899 483 -75 -1374 N ATOM 855 CA MET A 155 8.784 18.630 11.972 1.00 68.64 C ANISOU 855 CA MET A 155 8035 9207 8837 329 -24 -1003 C ATOM 856 C MET A 155 7.875 18.134 10.856 1.00 64.55 C ANISOU 856 C MET A 155 7452 8706 8368 269 63 -905 C ATOM 857 O MET A 155 8.316 17.979 9.712 1.00 59.62 O ANISOU 857 O MET A 155 6898 7863 7894 252 8 -690 O ATOM 858 CB MET A 155 9.241 17.467 12.851 1.00 72.37 C ANISOU 858 CB MET A 155 8663 9833 9001 158 94 -859 C ATOM 859 CG MET A 155 10.407 17.803 13.768 1.00 80.64 C ANISOU 859 CG MET A 155 9815 10814 10011 208 -29 -884 C ATOM 860 SD MET A 155 11.031 16.373 14.674 1.00 89.65 S ANISOU 860 SD MET A 155 11184 12069 10810 19 37 -657 S ATOM 861 CE MET A 155 12.405 17.110 15.553 1.00 99.07 C ANISOU 861 CE MET A 155 12443 13153 12047 140 -171 -742 C ATOM 862 N ILE A 156 6.602 17.886 11.166 1.00 67.34 N ANISOU 862 N ILE A 156 7652 9352 8582 227 200 -1075 N ATOM 863 CA ILE A 156 5.685 17.372 10.156 1.00 68.91 C ANISOU 863 CA ILE A 156 7773 9590 8821 157 271 -1001 C ATOM 864 C ILE A 156 5.469 18.403 9.059 1.00 69.08 C ANISOU 864 C ILE A 156 7705 9384 9158 345 81 -1053 C ATOM 865 O ILE A 156 5.484 18.072 7.867 1.00 70.31 O ANISOU 865 O ILE A 156 7916 9392 9407 300 52 -852 O ATOM 866 CB ILE A 156 4.357 16.945 10.806 1.00 70.36 C ANISOU 866 CB ILE A 156 7765 10184 8786 48 458 -1197 C ATOM 867 CG1 ILE A 156 4.590 15.773 11.761 1.00 67.02 C ANISOU 867 CG1 ILE A 156 7488 9956 8020 -215 628 -1044 C ATOM 868 CG2 ILE A 156 3.332 16.571 9.742 1.00 64.85 C ANISOU 868 CG2 ILE A 156 6940 9528 8171 -3 496 -1169 C ATOM 869 CD1 ILE A 156 3.333 15.249 12.401 1.00 60.59 C ANISOU 869 CD1 ILE A 156 6493 9587 6942 -411 838 -1180 C ATOM 870 N SER A 157 5.271 19.668 9.439 1.00 67.59 N ANISOU 870 N SER A 157 7393 9155 9133 558 -76 -1325 N ATOM 871 CA SER A 157 5.081 20.719 8.446 1.00 66.91 C ANISOU 871 CA SER A 157 7261 8799 9364 734 -321 -1352 C ATOM 872 C SER A 157 6.261 20.789 7.488 1.00 65.20 C ANISOU 872 C SER A 157 7252 8247 9275 664 -437 -1006 C ATOM 873 O SER A 157 6.079 20.905 6.271 1.00 70.97 O ANISOU 873 O SER A 157 8005 8831 10130 658 -531 -845 O ATOM 874 CB SER A 157 4.876 22.064 9.138 1.00 53.19 C ANISOU 874 CB SER A 157 5403 7001 7805 983 -525 -1706 C ATOM 875 OG SER A 157 3.770 22.013 10.019 1.00 59.25 O ANISOU 875 OG SER A 157 5930 8154 8428 1059 -395 -2076 O ATOM 876 N ILE A 158 7.481 20.701 8.019 1.00 63.38 N ANISOU 876 N ILE A 158 7159 7930 8993 600 -428 -895 N ATOM 877 CA ILE A 158 8.662 20.757 7.168 1.00 62.29 C ANISOU 877 CA ILE A 158 7167 7544 8955 516 -512 -595 C ATOM 878 C ILE A 158 8.684 19.577 6.207 1.00 66.42 C ANISOU 878 C ILE A 158 7754 8134 9350 369 -356 -352 C ATOM 879 O ILE A 158 9.069 19.717 5.042 1.00 76.92 O ANISOU 879 O ILE A 158 9134 9324 10767 323 -426 -148 O ATOM 880 CB ILE A 158 9.935 20.815 8.030 1.00 62.52 C ANISOU 880 CB ILE A 158 7286 7519 8948 483 -529 -568 C ATOM 881 CG1 ILE A 158 9.969 22.114 8.833 1.00 61.54 C ANISOU 881 CG1 ILE A 158 7112 7280 8990 635 -734 -823 C ATOM 882 CG2 ILE A 158 11.177 20.683 7.165 1.00 56.51 C ANISOU 882 CG2 ILE A 158 6625 6594 8253 369 -564 -273 C ATOM 883 CD1 ILE A 158 11.102 22.178 9.819 1.00 68.44 C ANISOU 883 CD1 ILE A 158 8055 8136 9811 610 -764 -846 C ATOM 884 N VAL A 159 8.260 18.399 6.670 1.00 61.58 N ANISOU 884 N VAL A 159 7145 7737 8515 280 -157 -371 N ATOM 885 CA VAL A 159 8.270 17.217 5.808 1.00 61.95 C ANISOU 885 CA VAL A 159 7267 7816 8456 152 -40 -177 C ATOM 886 C VAL A 159 7.403 17.448 4.578 1.00 58.47 C ANISOU 886 C VAL A 159 6754 7353 8111 173 -97 -152 C ATOM 887 O VAL A 159 7.847 17.270 3.437 1.00 64.62 O ANISOU 887 O VAL A 159 7599 8038 8915 129 -128 32 O ATOM 888 CB VAL A 159 7.811 15.973 6.589 1.00 61.71 C ANISOU 888 CB VAL A 159 7270 7984 8194 28 136 -202 C ATOM 889 CG1 VAL A 159 7.571 14.812 5.641 1.00 58.85 C ANISOU 889 CG1 VAL A 159 6974 7622 7763 -90 212 -53 C ATOM 890 CG2 VAL A 159 8.840 15.593 7.634 1.00 64.69 C ANISOU 890 CG2 VAL A 159 7772 8351 8457 -6 154 -157 C ATOM 891 N TRP A 160 6.156 17.865 4.792 1.00 55.67 N ANISOU 891 N TRP A 160 6244 7112 7797 249 -122 -357 N ATOM 892 CA TRP A 160 5.209 17.964 3.688 1.00 61.87 C ANISOU 892 CA TRP A 160 6946 7902 8658 275 -191 -352 C ATOM 893 C TRP A 160 5.414 19.222 2.854 1.00 68.14 C ANISOU 893 C TRP A 160 7758 8458 9675 394 -447 -287 C ATOM 894 O TRP A 160 5.155 19.201 1.645 1.00 72.46 O ANISOU 894 O TRP A 160 8331 8951 10250 369 -527 -148 O ATOM 895 CB TRP A 160 3.778 17.893 4.226 1.00 54.20 C ANISOU 895 CB TRP A 160 5762 7176 7654 313 -130 -618 C ATOM 896 CG TRP A 160 3.447 16.528 4.729 1.00 59.47 C ANISOU 896 CG TRP A 160 6436 8074 8087 111 106 -599 C ATOM 897 CD1 TRP A 160 3.428 16.111 6.027 1.00 64.43 C ANISOU 897 CD1 TRP A 160 7047 8894 8538 21 258 -694 C ATOM 898 CD2 TRP A 160 3.129 15.380 3.933 1.00 65.48 C ANISOU 898 CD2 TRP A 160 7253 8873 8755 -53 190 -456 C ATOM 899 NE1 TRP A 160 3.105 14.776 6.089 1.00 64.83 N ANISOU 899 NE1 TRP A 160 7153 9080 8400 -211 420 -586 N ATOM 900 CE2 TRP A 160 2.917 14.305 4.817 1.00 67.13 C ANISOU 900 CE2 TRP A 160 7487 9263 8758 -251 374 -455 C ATOM 901 CE3 TRP A 160 2.997 15.161 2.558 1.00 66.76 C ANISOU 901 CE3 TRP A 160 7455 8935 8975 -62 110 -331 C ATOM 902 CZ2 TRP A 160 2.575 13.030 4.371 1.00 70.04 C ANISOU 902 CZ2 TRP A 160 7926 9666 9019 -454 457 -337 C ATOM 903 CZ3 TRP A 160 2.659 13.895 2.117 1.00 69.12 C ANISOU 903 CZ3 TRP A 160 7807 9302 9154 -239 209 -252 C ATOM 904 CH2 TRP A 160 2.451 12.846 3.021 1.00 68.25 C ANISOU 904 CH2 TRP A 160 7727 9325 8880 -431 370 -257 C ATOM 905 N VAL A 161 5.874 20.317 3.463 1.00 67.95 N ANISOU 905 N VAL A 161 7737 8280 9802 507 -599 -373 N ATOM 906 CA VAL A 161 6.140 21.520 2.680 1.00 69.19 C ANISOU 906 CA VAL A 161 7952 8155 10182 576 -883 -262 C ATOM 907 C VAL A 161 7.379 21.323 1.823 1.00 65.64 C ANISOU 907 C VAL A 161 7665 7597 9678 402 -867 76 C ATOM 908 O VAL A 161 7.447 21.799 0.684 1.00 71.00 O ANISOU 908 O VAL A 161 8411 8144 10420 354 -1023 278 O ATOM 909 CB VAL A 161 6.273 22.747 3.599 1.00 68.92 C ANISOU 909 CB VAL A 161 7883 7953 10351 740 -1087 -473 C ATOM 910 CG1 VAL A 161 6.754 23.958 2.810 1.00 55.10 C ANISOU 910 CG1 VAL A 161 6251 5845 8841 751 -1414 -291 C ATOM 911 CG2 VAL A 161 4.941 23.041 4.271 1.00 68.37 C ANISOU 911 CG2 VAL A 161 7604 8033 10340 947 -1123 -858 C ATOM 912 N LEU A 162 8.370 20.607 2.346 1.00 57.34 N ANISOU 912 N LEU A 162 6669 6627 8492 302 -683 137 N ATOM 913 CA LEU A 162 9.567 20.343 1.562 1.00 62.34 C ANISOU 913 CA LEU A 162 7399 7226 9060 152 -640 403 C ATOM 914 C LEU A 162 9.274 19.375 0.424 1.00 64.44 C ANISOU 914 C LEU A 162 7686 7633 9165 68 -521 527 C ATOM 915 O LEU A 162 9.756 19.565 -0.698 1.00 73.70 O ANISOU 915 O LEU A 162 8910 8787 10307 -32 -568 735 O ATOM 916 CB LEU A 162 10.668 19.803 2.467 1.00 66.33 C ANISOU 916 CB LEU A 162 7929 7786 9485 111 -507 389 C ATOM 917 CG LEU A 162 12.083 19.741 1.909 1.00 71.44 C ANISOU 917 CG LEU A 162 8616 8419 10108 -16 -484 596 C ATOM 918 CD1 LEU A 162 12.409 21.020 1.165 1.00 63.78 C ANISOU 918 CD1 LEU A 162 7665 7275 9293 -96 -691 765 C ATOM 919 CD2 LEU A 162 13.044 19.530 3.061 1.00 75.47 C ANISOU 919 CD2 LEU A 162 9125 8941 10610 0 -439 519 C ATOM 920 N SER A 163 8.481 18.334 0.691 1.00 62.39 N ANISOU 920 N SER A 163 7390 7531 8786 86 -371 399 N ATOM 921 CA SER A 163 8.099 17.410 -0.371 1.00 64.81 C ANISOU 921 CA SER A 163 7718 7951 8957 15 -289 475 C ATOM 922 C SER A 163 7.384 18.143 -1.499 1.00 65.90 C ANISOU 922 C SER A 163 7840 8039 9160 33 -467 552 C ATOM 923 O SER A 163 7.634 17.874 -2.680 1.00 71.94 O ANISOU 923 O SER A 163 8662 8855 9817 -51 -466 710 O ATOM 924 CB SER A 163 7.213 16.302 0.193 1.00 64.78 C ANISOU 924 CB SER A 163 7674 8087 8852 4 -146 321 C ATOM 925 OG SER A 163 7.785 15.740 1.357 1.00 61.15 O ANISOU 925 OG SER A 163 7254 7650 8329 -18 -31 269 O ATOM 926 N PHE A 164 6.497 19.078 -1.153 1.00 60.59 N ANISOU 926 N PHE A 164 7089 7277 8655 156 -639 427 N ATOM 927 CA PHE A 164 5.825 19.887 -2.164 1.00 61.72 C ANISOU 927 CA PHE A 164 7234 7322 8893 201 -880 505 C ATOM 928 C PHE A 164 6.833 20.691 -2.972 1.00 65.16 C ANISOU 928 C PHE A 164 7806 7601 9350 94 -1027 793 C ATOM 929 O PHE A 164 6.879 20.597 -4.203 1.00 65.92 O ANISOU 929 O PHE A 164 7974 7746 9327 -10 -1074 992 O ATOM 930 CB PHE A 164 4.803 20.813 -1.496 1.00 57.42 C ANISOU 930 CB PHE A 164 6564 6683 8568 400 -1076 267 C ATOM 931 CG PHE A 164 4.135 21.779 -2.443 1.00 61.42 C ANISOU 931 CG PHE A 164 7089 7023 9226 488 -1405 340 C ATOM 932 CD1 PHE A 164 3.067 21.374 -3.232 1.00 63.79 C ANISOU 932 CD1 PHE A 164 7317 7446 9476 519 -1453 302 C ATOM 933 CD2 PHE A 164 4.563 23.097 -2.528 1.00 60.79 C ANISOU 933 CD2 PHE A 164 7109 6640 9350 534 -1703 451 C ATOM 934 CE1 PHE A 164 2.450 22.259 -4.099 1.00 64.22 C ANISOU 934 CE1 PHE A 164 7400 7336 9667 615 -1799 378 C ATOM 935 CE2 PHE A 164 3.946 23.988 -3.393 1.00 65.28 C ANISOU 935 CE2 PHE A 164 7729 7008 10065 614 -2062 545 C ATOM 936 CZ PHE A 164 2.889 23.566 -4.178 1.00 64.54 C ANISOU 936 CZ PHE A 164 7564 7051 9906 666 -2113 510 C ATOM 937 N THR A 165 7.667 21.477 -2.285 1.00 60.91 N ANISOU 937 N THR A 165 7302 6899 8944 90 -1100 820 N ATOM 938 CA THR A 165 8.590 22.366 -2.984 1.00 68.08 C ANISOU 938 CA THR A 165 8326 7648 9893 -59 -1264 1109 C ATOM 939 C THR A 165 9.585 21.592 -3.836 1.00 67.06 C ANISOU 939 C THR A 165 8237 7731 9511 -266 -1055 1321 C ATOM 940 O THR A 165 10.068 22.114 -4.846 1.00 74.56 O ANISOU 940 O THR A 165 9269 8666 10395 -439 -1158 1596 O ATOM 941 CB THR A 165 9.335 23.256 -1.988 1.00 72.21 C ANISOU 941 CB THR A 165 8862 7963 10613 -43 -1373 1067 C ATOM 942 OG1 THR A 165 10.064 22.439 -1.068 1.00 84.36 O ANISOU 942 OG1 THR A 165 10343 9656 12055 -52 -1111 946 O ATOM 943 CG2 THR A 165 8.362 24.133 -1.215 1.00 69.54 C ANISOU 943 CG2 THR A 165 8475 7415 10531 191 -1616 813 C ATOM 944 N ILE A 166 9.898 20.352 -3.455 1.00 69.64 N ANISOU 944 N ILE A 166 8506 8267 9687 -255 -775 1193 N ATOM 945 CA ILE A 166 10.825 19.548 -4.247 1.00 72.15 C ANISOU 945 CA ILE A 166 8831 8805 9778 -397 -585 1317 C ATOM 946 C ILE A 166 10.150 19.043 -5.520 1.00 72.60 C ANISOU 946 C ILE A 166 8918 9016 9653 -435 -578 1379 C ATOM 947 O ILE A 166 10.751 19.045 -6.601 1.00 74.34 O ANISOU 947 O ILE A 166 9167 9388 9690 -588 -548 1564 O ATOM 948 CB ILE A 166 11.383 18.389 -3.402 1.00 64.44 C ANISOU 948 CB ILE A 166 7804 7945 8737 -337 -355 1141 C ATOM 949 CG1 ILE A 166 12.401 18.911 -2.386 1.00 65.09 C ANISOU 949 CG1 ILE A 166 7859 7927 8946 -345 -368 1133 C ATOM 950 CG2 ILE A 166 12.008 17.326 -4.294 1.00 61.90 C ANISOU 950 CG2 ILE A 166 7469 7861 8189 -405 -177 1168 C ATOM 951 CD1 ILE A 166 12.979 17.825 -1.505 1.00 55.41 C ANISOU 951 CD1 ILE A 166 6604 6788 7663 -276 -195 979 C ATOM 952 N SER A 167 8.896 18.605 -5.414 1.00 66.08 N ANISOU 952 N SER A 167 8070 8185 8852 -311 -603 1216 N ATOM 953 CA SER A 167 8.168 18.066 -6.554 1.00 69.77 C ANISOU 953 CA SER A 167 8557 8794 9156 -335 -616 1237 C ATOM 954 C SER A 167 7.500 19.138 -7.404 1.00 70.97 C ANISOU 954 C SER A 167 8769 8841 9355 -354 -900 1407 C ATOM 955 O SER A 167 7.132 18.860 -8.553 1.00 69.63 O ANISOU 955 O SER A 167 8642 8809 9005 -415 -942 1493 O ATOM 956 CB SER A 167 7.104 17.078 -6.070 1.00 67.68 C ANISOU 956 CB SER A 167 8226 8582 8907 -228 -531 989 C ATOM 957 OG SER A 167 6.153 17.737 -5.251 1.00 68.82 O ANISOU 957 OG SER A 167 8295 8591 9261 -104 -663 859 O ATOM 958 N CYS A 168 7.324 20.345 -6.871 1.00 72.75 N ANISOU 958 N CYS A 168 9009 8812 9819 -293 -1126 1446 N ATOM 959 CA CYS A 168 6.648 21.393 -7.631 1.00 73.51 C ANISOU 959 CA CYS A 168 9186 8743 10001 -284 -1466 1607 C ATOM 960 C CYS A 168 7.347 21.747 -8.942 1.00 77.62 C ANISOU 960 C CYS A 168 9848 9341 10301 -524 -1540 1966 C ATOM 961 O CYS A 168 6.638 22.045 -9.918 1.00 81.68 O ANISOU 961 O CYS A 168 10442 9849 10744 -540 -1760 2098 O ATOM 962 CB CYS A 168 6.478 22.640 -6.754 1.00 74.94 C ANISOU 962 CB CYS A 168 9371 8593 10510 -158 -1727 1556 C ATOM 963 SG CYS A 168 5.411 23.906 -7.472 1.00 83.98 S ANISOU 963 SG CYS A 168 10608 9450 11852 -51 -2231 1669 S ATOM 964 N PRO A 169 8.683 21.755 -9.044 1.00 78.38 N ANISOU 964 N PRO A 169 9970 9541 10269 -727 -1380 2136 N ATOM 965 CA PRO A 169 9.296 22.005 -10.360 1.00 83.73 C ANISOU 965 CA PRO A 169 10752 10394 10669 -996 -1410 2471 C ATOM 966 C PRO A 169 8.894 21.001 -11.428 1.00 84.95 C ANISOU 966 C PRO A 169 10900 10878 10501 -1015 -1280 2429 C ATOM 967 O PRO A 169 8.857 21.362 -12.611 1.00 84.19 O ANISOU 967 O PRO A 169 10915 10894 10178 -1189 -1413 2692 O ATOM 968 CB PRO A 169 10.799 21.935 -10.063 1.00 82.55 C ANISOU 968 CB PRO A 169 10540 10383 10443 -1178 -1179 2547 C ATOM 969 CG PRO A 169 10.912 22.332 -8.645 1.00 76.42 C ANISOU 969 CG PRO A 169 9712 9325 9998 -1032 -1220 2380 C ATOM 970 CD PRO A 169 9.698 21.762 -7.973 1.00 74.69 C ANISOU 970 CD PRO A 169 9435 9030 9916 -740 -1219 2057 C ATOM 971 N LEU A 170 8.584 19.755 -11.051 1.00 79.08 N ANISOU 971 N LEU A 170 10044 10281 9723 -856 -1047 2113 N ATOM 972 CA LEU A 170 8.270 18.731 -12.044 1.00 73.43 C ANISOU 972 CA LEU A 170 9322 9863 8714 -871 -932 2033 C ATOM 973 C LEU A 170 7.035 19.090 -12.860 1.00 76.56 C ANISOU 973 C LEU A 170 9801 10208 9081 -835 -1215 2109 C ATOM 974 O LEU A 170 6.917 18.677 -14.020 1.00 77.86 O ANISOU 974 O LEU A 170 10015 10626 8942 -927 -1211 2171 O ATOM 975 CB LEU A 170 8.080 17.380 -11.356 1.00 67.28 C ANISOU 975 CB LEU A 170 8435 9155 7972 -710 -697 1684 C ATOM 976 CG LEU A 170 9.176 16.975 -10.366 1.00 66.79 C ANISOU 976 CG LEU A 170 8297 9091 7988 -692 -470 1577 C ATOM 977 CD1 LEU A 170 8.737 15.773 -9.563 1.00 66.74 C ANISOU 977 CD1 LEU A 170 8235 9057 8068 -536 -332 1276 C ATOM 978 CD2 LEU A 170 10.488 16.689 -11.074 1.00 61.58 C ANISOU 978 CD2 LEU A 170 7607 8724 7065 -840 -287 1659 C ATOM 979 N LEU A 171 6.108 19.856 -12.280 1.00 72.91 N ANISOU 979 N LEU A 171 9340 9439 8925 -685 -1477 2076 N ATOM 980 CA LEU A 171 4.945 20.322 -13.024 1.00 75.80 C ANISOU 980 CA LEU A 171 9768 9727 9306 -622 -1806 2146 C ATOM 981 C LEU A 171 5.311 21.339 -14.094 1.00 79.71 C ANISOU 981 C LEU A 171 10460 10190 9637 -830 -2066 2561 C ATOM 982 O LEU A 171 4.541 21.531 -15.041 1.00 84.88 O ANISOU 982 O LEU A 171 11203 10874 10173 -833 -2320 2673 O ATOM 983 CB LEU A 171 3.917 20.942 -12.075 1.00 74.05 C ANISOU 983 CB LEU A 171 9460 9199 9478 -376 -2034 1961 C ATOM 984 CG LEU A 171 2.918 20.015 -11.385 1.00 69.74 C ANISOU 984 CG LEU A 171 8717 8733 9050 -185 -1900 1574 C ATOM 985 CD1 LEU A 171 2.056 20.807 -10.416 1.00 68.86 C ANISOU 985 CD1 LEU A 171 8486 8373 9305 44 -2112 1385 C ATOM 986 CD2 LEU A 171 2.059 19.311 -12.420 1.00 65.45 C ANISOU 986 CD2 LEU A 171 8160 8395 8313 -188 -1959 1520 C ATOM 987 N PHE A 172 6.460 21.995 -13.967 1.00 68.04 N ANISOU 987 N PHE A 172 9054 8656 8140 -1028 -2027 2807 N ATOM 988 CA PHE A 172 6.795 23.074 -14.882 1.00 78.77 C ANISOU 988 CA PHE A 172 10620 9942 9366 -1280 -2310 3252 C ATOM 989 C PHE A 172 8.096 22.777 -15.619 1.00 85.91 C ANISOU 989 C PHE A 172 11542 11237 9862 -1615 -2028 3473 C ATOM 990 O PHE A 172 9.011 23.607 -15.641 1.00 88.20 O ANISOU 990 O PHE A 172 11911 11460 10141 -1873 -2078 3779 O ATOM 991 CB PHE A 172 6.876 24.399 -14.118 1.00 84.73 C ANISOU 991 CB PHE A 172 11461 10224 10509 -1254 -2621 3391 C ATOM 992 CG PHE A 172 5.617 24.738 -13.360 1.00 85.93 C ANISOU 992 CG PHE A 172 11551 10035 11063 -893 -2895 3113 C ATOM 993 CD1 PHE A 172 4.602 25.461 -13.964 1.00 86.94 C ANISOU 993 CD1 PHE A 172 11803 9937 11293 -793 -3356 3232 C ATOM 994 CD2 PHE A 172 5.447 24.323 -12.046 1.00 83.56 C ANISOU 994 CD2 PHE A 172 11054 9673 11022 -654 -2699 2721 C ATOM 995 CE1 PHE A 172 3.443 25.769 -13.275 1.00 83.30 C ANISOU 995 CE1 PHE A 172 11232 9212 11208 -436 -3605 2923 C ATOM 996 CE2 PHE A 172 4.288 24.629 -11.350 1.00 82.96 C ANISOU 996 CE2 PHE A 172 10876 9366 11280 -334 -2919 2431 C ATOM 997 CZ PHE A 172 3.286 25.353 -11.967 1.00 83.10 C ANISOU 997 CZ PHE A 172 10978 9179 11417 -212 -3367 2511 C ATOM 998 N GLY A 173 8.179 21.592 -16.224 1.00 92.00 N ANISOU 998 N GLY A 173 12224 12431 10302 -1618 -1741 3296 N ATOM 999 CA GLY A 173 9.333 21.223 -17.023 1.00 99.29 C ANISOU 999 CA GLY A 173 13120 13810 10797 -1900 -1463 3431 C ATOM 1000 C GLY A 173 10.629 21.114 -16.255 1.00105.40 C ANISOU 1000 C GLY A 173 13746 14661 11642 -1983 -1167 3370 C ATOM 1001 O GLY A 173 11.703 21.225 -16.853 1.00109.34 O ANISOU 1001 O GLY A 173 14209 15498 11836 -2275 -998 3563 O ATOM 1002 N LEU A 174 10.558 20.899 -14.940 1.00100.46 N ANISOU 1002 N LEU A 174 13015 13761 11393 -1742 -1102 3100 N ATOM 1003 CA LEU A 174 11.734 20.873 -14.068 1.00103.35 C ANISOU 1003 CA LEU A 174 13246 14141 11880 -1788 -879 3034 C ATOM 1004 C LEU A 174 12.539 22.163 -14.183 1.00110.64 C ANISOU 1004 C LEU A 174 14250 14960 12828 -2107 -1028 3434 C ATOM 1005 O LEU A 174 13.746 22.179 -13.930 1.00113.38 O ANISOU 1005 O LEU A 174 14470 15481 13128 -2273 -823 3467 O ATOM 1006 CB LEU A 174 12.615 19.654 -14.361 1.00 97.67 C ANISOU 1006 CB LEU A 174 12350 13885 10875 -1796 -492 2806 C ATOM 1007 CG LEU A 174 13.534 19.118 -13.264 1.00 92.37 C ANISOU 1007 CG LEU A 174 11502 13215 10381 -1682 -254 2560 C ATOM 1008 CD1 LEU A 174 12.928 19.339 -11.890 1.00 88.80 C ANISOU 1008 CD1 LEU A 174 11078 12307 10354 -1450 -387 2419 C ATOM 1009 CD2 LEU A 174 13.792 17.638 -13.505 1.00 90.06 C ANISOU 1009 CD2 LEU A 174 11076 13252 9891 -1525 22 2210 C ATOM 1010 N ASN A 175 11.863 23.254 -14.556 1.00127.08 N ANISOU 1010 N ASN A 175 16542 16739 15004 -2196 -1417 3738 N ATOM 1011 CA ASN A 175 12.511 24.539 -14.814 1.00131.09 C ANISOU 1011 CA ASN A 175 17185 17092 15530 -2547 -1637 4178 C ATOM 1012 C ASN A 175 13.737 24.358 -15.706 1.00135.52 C ANISOU 1012 C ASN A 175 17627 18169 15696 -2875 -1339 4267 C ATOM 1013 O ASN A 175 14.777 24.991 -15.516 1.00141.49 O ANISOU 1013 O ASN A 175 18317 18930 16514 -3096 -1295 4368 O ATOM 1014 CB ASN A 175 12.876 25.244 -13.504 1.00127.19 C ANISOU 1014 CB ASN A 175 16665 16177 15484 -2475 -1748 4122 C ATOM 1015 CG ASN A 175 11.656 25.790 -12.774 1.00121.37 C ANISOU 1015 CG ASN A 175 16035 14913 15169 -2144 -2109 3974 C ATOM 1016 OD1 ASN A 175 10.689 26.228 -13.400 1.00120.30 O ANISOU 1016 OD1 ASN A 175 16064 14605 15041 -2092 -2430 4105 O ATOM 1017 ND2 ASN A 175 11.697 25.764 -11.445 1.00115.08 N ANISOU 1017 ND2 ASN A 175 15127 13886 14713 -1906 -2061 3672 N ATOM 1018 N ASN A 176 13.611 23.469 -16.686 1.00138.51 N ANISOU 1018 N ASN A 176 17960 19005 15662 -2893 -1141 4194 N ATOM 1019 CA ASN A 176 14.702 23.139 -17.593 1.00128.90 C ANISOU 1019 CA ASN A 176 16590 18346 14041 -3148 -837 4194 C ATOM 1020 C ASN A 176 14.143 23.135 -19.012 1.00130.29 C ANISOU 1020 C ASN A 176 16893 18756 13854 -3256 -934 4312 C ATOM 1021 O ASN A 176 13.054 23.656 -19.280 1.00128.25 O ANISOU 1021 O ASN A 176 16856 18174 13701 -3186 -1280 4456 O ATOM 1022 CB ASN A 176 15.347 21.804 -17.188 1.00114.40 C ANISOU 1022 CB ASN A 176 14490 16909 12066 -3004 -416 3849 C ATOM 1023 N ALA A 177 14.888 22.541 -19.940 1.00131.35 N ANISOU 1023 N ALA A 177 16876 19466 13564 -3410 -639 4223 N ATOM 1024 CA ALA A 177 14.518 22.512 -21.354 1.00133.06 C ANISOU 1024 CA ALA A 177 17193 19978 13388 -3547 -695 4324 C ATOM 1025 C ALA A 177 13.850 21.175 -21.665 1.00139.43 C ANISOU 1025 C ALA A 177 17953 21060 13966 -3279 -543 3999 C ATOM 1026 O ALA A 177 14.499 20.218 -22.087 1.00134.42 O ANISOU 1026 O ALA A 177 17113 20932 13028 -3260 -210 3722 O ATOM 1027 CB ALA A 177 15.744 22.740 -22.230 1.00132.82 C ANISOU 1027 CB ALA A 177 17018 20431 13018 -3895 -487 4415 C ATOM 1028 N ASP A 178 12.535 21.113 -21.456 1.00139.56 N ANISOU 1028 N ASP A 178 18147 20737 14141 -3057 -814 4002 N ATOM 1029 CA ASP A 178 11.738 19.985 -21.927 1.00140.00 C ANISOU 1029 CA ASP A 178 18203 21034 13957 -2843 -761 3735 C ATOM 1030 C ASP A 178 10.328 20.465 -22.235 1.00139.46 C ANISOU 1030 C ASP A 178 18375 20618 13994 -2746 -1185 3897 C ATOM 1031 O ASP A 178 9.372 20.082 -21.554 1.00142.64 O ANISOU 1031 O ASP A 178 18808 20766 14622 -2479 -1336 3761 O ATOM 1032 CB ASP A 178 11.711 18.857 -20.894 1.00137.06 C ANISOU 1032 CB ASP A 178 17675 20675 13728 -2556 -547 3368 C ATOM 1033 N GLN A 179 10.191 21.295 -23.270 1.00143.02 N ANISOU 1033 N GLN A 179 18983 21074 14284 -2960 -1392 4178 N ATOM 1034 CA GLN A 179 8.987 22.105 -23.424 1.00133.33 C ANISOU 1034 CA GLN A 179 17987 19403 13269 -2879 -1859 4383 C ATOM 1035 C GLN A 179 7.753 21.243 -23.675 1.00128.51 C ANISOU 1035 C GLN A 179 17406 18844 12578 -2605 -1987 4153 C ATOM 1036 O GLN A 179 6.787 21.279 -22.902 1.00124.40 O ANISOU 1036 O GLN A 179 16911 17946 12410 -2345 -2237 4071 O ATOM 1037 CB GLN A 179 9.188 23.117 -24.553 1.00132.56 C ANISOU 1037 CB GLN A 179 18056 19342 12970 -3191 -2041 4737 C ATOM 1038 N ASN A 180 7.766 20.455 -24.749 1.00126.77 N ANISOU 1038 N ASN A 180 17160 19104 11903 -2656 -1831 4014 N ATOM 1039 CA ASN A 180 6.565 19.780 -25.230 1.00115.92 C ANISOU 1039 CA ASN A 180 15839 17790 10414 -2448 -2017 3825 C ATOM 1040 C ASN A 180 6.535 18.292 -24.886 1.00111.57 C ANISOU 1040 C ASN A 180 15109 17542 9741 -2253 -1745 3379 C ATOM 1041 O ASN A 180 5.949 17.498 -25.625 1.00103.18 O ANISOU 1041 O ASN A 180 14050 16740 8415 -2166 -1771 3154 O ATOM 1042 CB ASN A 180 6.419 19.972 -26.739 1.00115.56 C ANISOU 1042 CB ASN A 180 15926 18028 9952 -2620 -2110 3964 C ATOM 1043 N GLU A 181 7.135 17.896 -23.764 1.00104.62 N ANISOU 1043 N GLU A 181 14065 16578 9107 -2156 -1490 3195 N ATOM 1044 CA GLU A 181 7.136 16.494 -23.369 1.00106.80 C ANISOU 1044 CA GLU A 181 14149 16965 9465 -1902 -1204 2656 C ATOM 1045 C GLU A 181 6.948 16.366 -21.867 1.00100.72 C ANISOU 1045 C GLU A 181 13266 15721 9281 -1661 -1157 2456 C ATOM 1046 O GLU A 181 7.211 17.295 -21.099 1.00102.83 O ANISOU 1046 O GLU A 181 13557 15677 9838 -1708 -1233 2688 O ATOM 1047 CB GLU A 181 8.426 15.780 -23.782 1.00111.20 C ANISOU 1047 CB GLU A 181 14562 18052 9639 -2014 -799 2478 C ATOM 1048 CG GLU A 181 8.455 15.363 -25.237 1.00118.18 C ANISOU 1048 CG GLU A 181 15491 19499 9912 -2150 -768 2439 C ATOM 1049 CD GLU A 181 9.558 14.373 -25.529 1.00125.80 C ANISOU 1049 CD GLU A 181 16244 20936 10620 -2119 -359 2054 C ATOM 1050 OE1 GLU A 181 9.649 13.356 -24.809 1.00127.00 O ANISOU 1050 OE1 GLU A 181 16258 20997 10999 -1858 -200 1630 O ATOM 1051 OE2 GLU A 181 10.339 14.618 -26.473 1.00132.18 O ANISOU 1051 OE2 GLU A 181 16999 22090 11133 -2311 -210 2123 O ATOM 1052 N CYS A 182 6.490 15.185 -21.461 1.00 85.77 N ANISOU 1052 N CYS A 182 11262 13784 7544 -1421 -1042 2020 N ATOM 1053 CA CYS A 182 6.326 14.886 -20.051 1.00 85.01 C ANISOU 1053 CA CYS A 182 11057 13309 7934 -1219 -963 1809 C ATOM 1054 C CYS A 182 7.659 15.034 -19.325 1.00 85.25 C ANISOU 1054 C CYS A 182 10998 13354 8038 -1280 -699 1848 C ATOM 1055 O CYS A 182 8.737 14.991 -19.927 1.00 87.66 O ANISOU 1055 O CYS A 182 11266 14030 8011 -1441 -506 1910 O ATOM 1056 CB CYS A 182 5.770 13.473 -19.864 1.00 85.07 C ANISOU 1056 CB CYS A 182 10980 13320 8021 -1022 -869 1364 C ATOM 1057 SG CYS A 182 5.430 13.056 -18.147 1.00 88.55 S ANISOU 1057 SG CYS A 182 11313 13325 9006 -826 -793 1143 S ATOM 1058 N ILE A 183 7.575 15.222 -18.009 1.00 86.69 N ANISOU 1058 N ILE A 183 11127 13162 8650 -1153 -694 1796 N ATOM 1059 CA ILE A 183 8.782 15.505 -17.243 1.00 88.06 C ANISOU 1059 CA ILE A 183 11221 13307 8931 -1209 -498 1856 C ATOM 1060 C ILE A 183 9.631 14.253 -17.070 1.00 90.76 C ANISOU 1060 C ILE A 183 11430 13873 9183 -1113 -193 1518 C ATOM 1061 O ILE A 183 10.856 14.349 -16.944 1.00 89.70 O ANISOU 1061 O ILE A 183 11199 13916 8966 -1199 -1 1550 O ATOM 1062 CB ILE A 183 8.428 16.141 -15.888 1.00 82.65 C ANISOU 1062 CB ILE A 183 10529 12169 8706 -1098 -610 1893 C ATOM 1063 CG1 ILE A 183 9.689 16.703 -15.236 1.00 81.90 C ANISOU 1063 CG1 ILE A 183 10377 12044 8696 -1203 -475 2026 C ATOM 1064 CG2 ILE A 183 7.755 15.134 -14.972 1.00 80.02 C ANISOU 1064 CG2 ILE A 183 10121 11657 8626 -869 -543 1542 C ATOM 1065 CD1 ILE A 183 10.562 17.486 -16.201 1.00 77.13 C ANISOU 1065 CD1 ILE A 183 9815 11711 7778 -1501 -472 2363 C ATOM 1066 N ILE A 184 9.020 13.066 -17.078 1.00 86.05 N ANISOU 1066 N ILE A 184 10817 13266 8612 -938 -167 1182 N ATOM 1067 CA ILE A 184 9.808 11.848 -16.945 1.00 81.50 C ANISOU 1067 CA ILE A 184 10141 12849 7978 -818 61 843 C ATOM 1068 C ILE A 184 10.649 11.603 -18.187 1.00 77.44 C ANISOU 1068 C ILE A 184 9566 12848 7010 -918 205 786 C ATOM 1069 O ILE A 184 11.589 10.802 -18.148 1.00 77.18 O ANISOU 1069 O ILE A 184 9408 13014 6904 -822 403 514 O ATOM 1070 CB ILE A 184 8.907 10.636 -16.645 1.00 80.64 C ANISOU 1070 CB ILE A 184 10060 12549 8030 -635 7 515 C ATOM 1071 CG1 ILE A 184 9.694 9.574 -15.876 1.00 78.25 C ANISOU 1071 CG1 ILE A 184 9688 12171 7873 -478 168 222 C ATOM 1072 CG2 ILE A 184 8.346 10.052 -17.932 1.00 83.92 C ANISOU 1072 CG2 ILE A 184 10523 13226 8137 -643 -67 367 C ATOM 1073 CD1 ILE A 184 8.861 8.383 -15.456 1.00 80.33 C ANISOU 1073 CD1 ILE A 184 10011 12185 8326 -346 90 -54 C ATOM 1074 N ALA A 185 10.335 12.279 -19.291 1.00 80.23 N ANISOU 1074 N ALA A 185 9999 13442 7044 -1105 98 1028 N ATOM 1075 CA ALA A 185 11.162 12.234 -20.487 1.00 83.51 C ANISOU 1075 CA ALA A 185 10349 14420 6960 -1262 251 1031 C ATOM 1076 C ALA A 185 12.352 13.177 -20.411 1.00 83.75 C ANISOU 1076 C ALA A 185 10288 14647 6887 -1499 393 1327 C ATOM 1077 O ALA A 185 13.207 13.143 -21.301 1.00 89.61 O ANISOU 1077 O ALA A 185 10921 15924 7202 -1661 576 1320 O ATOM 1078 CB ALA A 185 10.320 12.565 -21.723 1.00 73.89 C ANISOU 1078 CB ALA A 185 9279 13403 5395 -1401 57 1201 C ATOM 1079 N ASN A 186 12.425 14.011 -19.384 1.00 87.95 N ANISOU 1079 N ASN A 186 10846 14788 7782 -1536 315 1567 N ATOM 1080 CA ASN A 186 13.545 14.931 -19.235 1.00 90.37 C ANISOU 1080 CA ASN A 186 11066 15232 8039 -1784 421 1852 C ATOM 1081 C ASN A 186 14.781 14.156 -18.795 1.00 93.04 C ANISOU 1081 C ASN A 186 11153 15806 8392 -1671 718 1526 C ATOM 1082 O ASN A 186 14.734 13.472 -17.765 1.00 90.82 O ANISOU 1082 O ASN A 186 10830 15214 8462 -1399 737 1252 O ATOM 1083 CB ASN A 186 13.200 16.017 -18.220 1.00 86.22 C ANISOU 1083 CB ASN A 186 10651 14175 7934 -1820 209 2150 C ATOM 1084 CG ASN A 186 14.162 17.185 -18.259 1.00 89.29 C ANISOU 1084 CG ASN A 186 11013 14659 8255 -2152 225 2537 C ATOM 1085 OD1 ASN A 186 15.380 17.008 -18.241 1.00 95.97 O ANISOU 1085 OD1 ASN A 186 11655 15837 8971 -2255 479 2464 O ATOM 1086 ND2 ASN A 186 13.616 18.393 -18.314 1.00 87.60 N ANISOU 1086 ND2 ASN A 186 10997 14142 8145 -2325 -71 2943 N ATOM 1087 N PRO A 187 15.895 14.232 -19.527 1.00 95.07 N ANISOU 1087 N PRO A 187 11229 16621 8273 -1873 941 1541 N ATOM 1088 CA PRO A 187 17.095 13.486 -19.110 1.00 94.27 C ANISOU 1088 CA PRO A 187 10845 16765 8209 -1726 1203 1183 C ATOM 1089 C PRO A 187 17.587 13.857 -17.721 1.00 93.98 C ANISOU 1089 C PRO A 187 10749 16330 8627 -1662 1185 1242 C ATOM 1090 O PRO A 187 18.317 13.067 -17.109 1.00 94.56 O ANISOU 1090 O PRO A 187 10638 16436 8855 -1433 1319 896 O ATOM 1091 CB PRO A 187 18.127 13.845 -20.190 1.00 87.30 C ANISOU 1091 CB PRO A 187 9769 16534 6867 -2026 1406 1271 C ATOM 1092 CG PRO A 187 17.630 15.128 -20.784 1.00 81.91 C ANISOU 1092 CG PRO A 187 9311 15710 6102 -2368 1189 1793 C ATOM 1093 CD PRO A 187 16.135 15.035 -20.737 1.00 89.48 C ANISOU 1093 CD PRO A 187 10552 16349 7098 -2256 952 1890 C ATOM 1094 N ALA A 188 17.198 15.020 -17.198 1.00 89.90 N ANISOU 1094 N ALA A 188 10393 15427 8337 -1837 994 1648 N ATOM 1095 CA ALA A 188 17.621 15.462 -15.877 1.00 87.20 C ANISOU 1095 CA ALA A 188 10012 14708 8411 -1788 952 1704 C ATOM 1096 C ALA A 188 16.681 15.017 -14.764 1.00 83.84 C ANISOU 1096 C ALA A 188 9732 13727 8396 -1473 795 1536 C ATOM 1097 O ALA A 188 16.983 15.253 -13.591 1.00 75.80 O ANISOU 1097 O ALA A 188 8687 12406 7707 -1395 761 1530 O ATOM 1098 CB ALA A 188 17.750 16.987 -15.848 1.00 80.85 C ANISOU 1098 CB ALA A 188 9302 13764 7654 -2142 804 2201 C ATOM 1099 N PHE A 189 15.554 14.386 -15.094 1.00 80.92 N ANISOU 1099 N PHE A 189 9504 13244 7997 -1314 698 1400 N ATOM 1100 CA PHE A 189 14.640 13.936 -14.051 1.00 78.27 C ANISOU 1100 CA PHE A 189 9281 12440 8018 -1065 570 1248 C ATOM 1101 C PHE A 189 15.276 12.851 -13.193 1.00 80.35 C ANISOU 1101 C PHE A 189 9430 12648 8450 -824 697 901 C ATOM 1102 O PHE A 189 15.128 12.856 -11.964 1.00 75.11 O ANISOU 1102 O PHE A 189 8806 11626 8105 -710 633 876 O ATOM 1103 CB PHE A 189 13.335 13.437 -14.671 1.00 80.58 C ANISOU 1103 CB PHE A 189 9715 12675 8225 -983 445 1165 C ATOM 1104 CG PHE A 189 12.426 12.754 -13.693 1.00 85.91 C ANISOU 1104 CG PHE A 189 10465 12965 9214 -760 358 965 C ATOM 1105 CD1 PHE A 189 11.690 13.490 -12.780 1.00 86.83 C ANISOU 1105 CD1 PHE A 189 10658 12708 9625 -749 203 1115 C ATOM 1106 CD2 PHE A 189 12.306 11.375 -13.683 1.00 84.50 C ANISOU 1106 CD2 PHE A 189 10274 12804 9028 -575 421 619 C ATOM 1107 CE1 PHE A 189 10.853 12.861 -11.873 1.00 82.22 C ANISOU 1107 CE1 PHE A 189 10115 11841 9283 -588 152 936 C ATOM 1108 CE2 PHE A 189 11.471 10.742 -12.779 1.00 79.97 C ANISOU 1108 CE2 PHE A 189 9777 11887 8720 -435 339 479 C ATOM 1109 CZ PHE A 189 10.745 11.486 -11.874 1.00 75.49 C ANISOU 1109 CZ PHE A 189 9262 11015 8404 -457 224 645 C ATOM 1110 N VAL A 190 15.990 11.913 -13.820 1.00 82.64 N ANISOU 1110 N VAL A 190 9581 13296 8524 -736 857 620 N ATOM 1111 CA VAL A 190 16.608 10.825 -13.066 1.00 79.80 C ANISOU 1111 CA VAL A 190 9129 12855 8338 -476 921 274 C ATOM 1112 C VAL A 190 17.619 11.375 -12.070 1.00 73.96 C ANISOU 1112 C VAL A 190 8263 12038 7801 -501 965 362 C ATOM 1113 O VAL A 190 17.647 10.963 -10.905 1.00 69.81 O ANISOU 1113 O VAL A 190 7780 11184 7561 -328 899 257 O ATOM 1114 CB VAL A 190 17.246 9.799 -14.024 1.00 76.29 C ANISOU 1114 CB VAL A 190 8531 12834 7621 -350 1058 -85 C ATOM 1115 CG1 VAL A 190 18.329 8.997 -13.321 1.00 73.98 C ANISOU 1115 CG1 VAL A 190 8071 12543 7496 -111 1121 -401 C ATOM 1116 CG2 VAL A 190 16.181 8.863 -14.570 1.00 70.22 C ANISOU 1116 CG2 VAL A 190 7922 11973 6787 -219 957 -292 C ATOM 1117 N VAL A 191 18.449 12.327 -12.502 1.00 74.89 N ANISOU 1117 N VAL A 191 8232 12459 7764 -745 1062 574 N ATOM 1118 CA VAL A 191 19.440 12.910 -11.603 1.00 69.99 C ANISOU 1118 CA VAL A 191 7472 11783 7337 -800 1089 659 C ATOM 1119 C VAL A 191 18.756 13.666 -10.472 1.00 71.73 C ANISOU 1119 C VAL A 191 7882 11494 7879 -818 904 880 C ATOM 1120 O VAL A 191 19.167 13.580 -9.308 1.00 74.22 O ANISOU 1120 O VAL A 191 8168 11584 8449 -696 866 802 O ATOM 1121 CB VAL A 191 20.401 13.820 -12.387 1.00 69.86 C ANISOU 1121 CB VAL A 191 7256 12216 7071 -1128 1224 873 C ATOM 1122 CG1 VAL A 191 21.588 14.210 -11.518 1.00 61.69 C ANISOU 1122 CG1 VAL A 191 6014 11194 6229 -1167 1269 875 C ATOM 1123 CG2 VAL A 191 20.860 13.135 -13.669 1.00 71.25 C ANISOU 1123 CG2 VAL A 191 7250 12975 6848 -1136 1419 651 C ATOM 1124 N TYR A 192 17.698 14.409 -10.792 1.00 73.30 N ANISOU 1124 N TYR A 192 8269 11519 8064 -952 769 1133 N ATOM 1125 CA TYR A 192 17.008 15.209 -9.786 1.00 69.49 C ANISOU 1125 CA TYR A 192 7937 10591 7877 -952 585 1300 C ATOM 1126 C TYR A 192 16.386 14.323 -8.714 1.00 69.05 C ANISOU 1126 C TYR A 192 7966 10230 8040 -683 540 1063 C ATOM 1127 O TYR A 192 16.743 14.407 -7.534 1.00 70.50 O ANISOU 1127 O TYR A 192 8135 10210 8443 -602 510 1018 O ATOM 1128 CB TYR A 192 15.946 16.079 -10.460 1.00 70.53 C ANISOU 1128 CB TYR A 192 8235 10616 7948 -1102 419 1566 C ATOM 1129 CG TYR A 192 15.223 17.022 -9.524 1.00 71.79 C ANISOU 1129 CG TYR A 192 8522 10343 8412 -1083 204 1704 C ATOM 1130 CD1 TYR A 192 15.814 18.212 -9.114 1.00 72.52 C ANISOU 1130 CD1 TYR A 192 8604 10305 8647 -1251 105 1926 C ATOM 1131 CD2 TYR A 192 13.943 16.733 -9.066 1.00 75.40 C ANISOU 1131 CD2 TYR A 192 9093 10543 9014 -904 92 1589 C ATOM 1132 CE1 TYR A 192 15.157 19.082 -8.265 1.00 72.60 C ANISOU 1132 CE1 TYR A 192 8724 9917 8942 -1200 -114 1996 C ATOM 1133 CE2 TYR A 192 13.275 17.600 -8.217 1.00 78.40 C ANISOU 1133 CE2 TYR A 192 9549 10580 9658 -860 -96 1656 C ATOM 1134 CZ TYR A 192 13.887 18.772 -7.820 1.00 72.16 C ANISOU 1134 CZ TYR A 192 8758 9648 9013 -988 -206 1843 C ATOM 1135 OH TYR A 192 13.226 19.632 -6.973 1.00 63.34 O ANISOU 1135 OH TYR A 192 7711 8188 8168 -909 -415 1853 O ATOM 1136 N SER A 193 15.457 13.449 -9.114 1.00 72.61 N ANISOU 1136 N SER A 193 8511 10659 8417 -566 526 916 N ATOM 1137 CA SER A 193 14.715 12.654 -8.139 1.00 77.34 C ANISOU 1137 CA SER A 193 9213 10968 9205 -382 469 746 C ATOM 1138 C SER A 193 15.615 11.681 -7.386 1.00 75.22 C ANISOU 1138 C SER A 193 8884 10678 9019 -217 535 524 C ATOM 1139 O SER A 193 15.294 11.286 -6.260 1.00 76.80 O ANISOU 1139 O SER A 193 9170 10614 9397 -116 473 460 O ATOM 1140 CB SER A 193 13.580 11.897 -8.830 1.00 79.11 C ANISOU 1140 CB SER A 193 9536 11195 9327 -336 430 640 C ATOM 1141 OG SER A 193 14.075 10.934 -9.741 1.00 69.99 O ANISOU 1141 OG SER A 193 8324 10300 7968 -274 524 442 O ATOM 1142 N SER A 194 16.739 11.283 -7.980 1.00 71.25 N ANISOU 1142 N SER A 194 8226 10467 8381 -186 646 398 N ATOM 1143 CA SER A 194 17.664 10.407 -7.271 1.00 72.26 C ANISOU 1143 CA SER A 194 8279 10561 8614 6 663 171 C ATOM 1144 C SER A 194 18.401 11.166 -6.177 1.00 76.18 C ANISOU 1144 C SER A 194 8709 10947 9290 -29 635 286 C ATOM 1145 O SER A 194 18.423 10.741 -5.014 1.00 72.02 O ANISOU 1145 O SER A 194 8263 10164 8939 99 550 218 O ATOM 1146 CB SER A 194 18.661 9.784 -8.246 1.00 72.31 C ANISOU 1146 CB SER A 194 8087 10955 8432 84 784 -57 C ATOM 1147 OG SER A 194 17.998 9.092 -9.286 1.00 80.43 O ANISOU 1147 OG SER A 194 9180 12101 9277 122 797 -194 O ATOM 1148 N ILE A 195 19.005 12.300 -6.530 1.00 77.08 N ANISOU 1148 N ILE A 195 8687 11249 9349 -226 688 474 N ATOM 1149 CA ILE A 195 19.847 13.021 -5.580 1.00 70.51 C ANISOU 1149 CA ILE A 195 7763 10342 8685 -272 652 555 C ATOM 1150 C ILE A 195 18.988 13.748 -4.552 1.00 66.52 C ANISOU 1150 C ILE A 195 7438 9466 8370 -304 511 708 C ATOM 1151 O ILE A 195 19.129 13.541 -3.341 1.00 74.63 O ANISOU 1151 O ILE A 195 8511 10286 9557 -186 438 633 O ATOM 1152 CB ILE A 195 20.787 13.987 -6.321 1.00 68.49 C ANISOU 1152 CB ILE A 195 7299 10412 8313 -520 744 715 C ATOM 1153 CG1 ILE A 195 21.784 13.200 -7.177 1.00 66.22 C ANISOU 1153 CG1 ILE A 195 6764 10568 7828 -459 911 488 C ATOM 1154 CG2 ILE A 195 21.510 14.892 -5.337 1.00 63.89 C ANISOU 1154 CG2 ILE A 195 6643 9700 7932 -613 668 829 C ATOM 1155 CD1 ILE A 195 22.738 14.064 -7.971 1.00 56.97 C ANISOU 1155 CD1 ILE A 195 5348 9813 6484 -752 1041 642 C ATOM 1156 N VAL A 196 18.073 14.597 -5.019 1.00 62.66 N ANISOU 1156 N VAL A 196 7052 8902 7854 -450 454 905 N ATOM 1157 CA VAL A 196 17.332 15.463 -4.105 1.00 67.97 C ANISOU 1157 CA VAL A 196 7847 9264 8715 -469 309 1012 C ATOM 1158 C VAL A 196 16.343 14.656 -3.269 1.00 67.07 C ANISOU 1158 C VAL A 196 7868 8944 8670 -296 275 861 C ATOM 1159 O VAL A 196 16.268 14.814 -2.046 1.00 61.49 O ANISOU 1159 O VAL A 196 7206 8054 8102 -231 210 818 O ATOM 1160 CB VAL A 196 16.626 16.582 -4.888 1.00 64.23 C ANISOU 1160 CB VAL A 196 7440 8750 8216 -643 212 1244 C ATOM 1161 CG1 VAL A 196 15.849 17.474 -3.945 1.00 52.97 C ANISOU 1161 CG1 VAL A 196 6116 7001 7009 -610 37 1287 C ATOM 1162 CG2 VAL A 196 17.638 17.392 -5.674 1.00 71.96 C ANISOU 1162 CG2 VAL A 196 8304 9935 9102 -883 238 1445 C ATOM 1163 N SER A 197 15.571 13.778 -3.911 1.00 68.31 N ANISOU 1163 N SER A 197 8091 9151 8712 -244 315 780 N ATOM 1164 CA SER A 197 14.505 13.073 -3.211 1.00 64.29 C ANISOU 1164 CA SER A 197 7706 8466 8256 -150 280 676 C ATOM 1165 C SER A 197 14.986 11.839 -2.460 1.00 64.86 C ANISOU 1165 C SER A 197 7819 8478 8346 -22 301 516 C ATOM 1166 O SER A 197 14.304 11.401 -1.528 1.00 71.84 O ANISOU 1166 O SER A 197 8812 9202 9284 7 262 476 O ATOM 1167 CB SER A 197 13.401 12.668 -4.191 1.00 64.34 C ANISOU 1167 CB SER A 197 7768 8525 8155 -175 281 661 C ATOM 1168 OG SER A 197 12.416 13.677 -4.297 1.00 65.40 O ANISOU 1168 OG SER A 197 7921 8583 8345 -241 188 775 O ATOM 1169 N PHE A 198 16.134 11.265 -2.824 1.00 56.65 N ANISOU 1169 N PHE A 198 6693 7571 7259 50 348 422 N ATOM 1170 CA PHE A 198 16.563 10.006 -2.225 1.00 61.84 C ANISOU 1170 CA PHE A 198 7413 8131 7953 205 308 258 C ATOM 1171 C PHE A 198 17.951 10.080 -1.597 1.00 66.94 C ANISOU 1171 C PHE A 198 7945 8814 8677 293 283 207 C ATOM 1172 O PHE A 198 18.076 9.853 -0.391 1.00 63.30 O ANISOU 1172 O PHE A 198 7574 8170 8306 352 191 202 O ATOM 1173 CB PHE A 198 16.518 8.887 -3.269 1.00 62.27 C ANISOU 1173 CB PHE A 198 7477 8279 7904 290 331 91 C ATOM 1174 CG PHE A 198 16.836 7.525 -2.714 1.00 71.87 C ANISOU 1174 CG PHE A 198 8800 9318 9188 461 226 -82 C ATOM 1175 CD1 PHE A 198 15.889 6.822 -1.986 1.00 73.26 C ANISOU 1175 CD1 PHE A 198 9194 9229 9414 432 130 -54 C ATOM 1176 CD2 PHE A 198 18.074 6.944 -2.927 1.00 66.14 C ANISOU 1176 CD2 PHE A 198 7955 8695 8481 641 204 -273 C ATOM 1177 CE1 PHE A 198 16.173 5.566 -1.481 1.00 70.07 C ANISOU 1177 CE1 PHE A 198 8932 8611 9079 560 -15 -171 C ATOM 1178 CE2 PHE A 198 18.365 5.687 -2.423 1.00 70.55 C ANISOU 1178 CE2 PHE A 198 8637 9036 9134 826 45 -436 C ATOM 1179 CZ PHE A 198 17.412 4.997 -1.700 1.00 69.64 C ANISOU 1179 CZ PHE A 198 8787 8602 9070 775 -79 -363 C ATOM 1180 N TYR A 199 18.996 10.380 -2.373 1.00 67.17 N ANISOU 1180 N TYR A 199 7766 9103 8654 290 360 166 N ATOM 1181 CA TYR A 199 20.356 10.230 -1.861 1.00 67.05 C ANISOU 1181 CA TYR A 199 7598 9159 8719 402 329 58 C ATOM 1182 C TYR A 199 20.656 11.224 -0.746 1.00 67.17 C ANISOU 1182 C TYR A 199 7604 9058 8859 323 261 193 C ATOM 1183 O TYR A 199 21.379 10.897 0.202 1.00 60.26 O ANISOU 1183 O TYR A 199 6716 8098 8082 445 161 112 O ATOM 1184 CB TYR A 199 21.367 10.375 -2.997 1.00 71.88 C ANISOU 1184 CB TYR A 199 7935 10155 9221 380 457 -32 C ATOM 1185 CG TYR A 199 21.372 9.197 -3.942 1.00 81.30 C ANISOU 1185 CG TYR A 199 9102 11489 10299 540 498 -275 C ATOM 1186 CD1 TYR A 199 21.185 7.907 -3.469 1.00 86.13 C ANISOU 1186 CD1 TYR A 199 9871 11856 10998 769 359 -463 C ATOM 1187 CD2 TYR A 199 21.545 9.374 -5.307 1.00 83.10 C ANISOU 1187 CD2 TYR A 199 9165 12088 10320 449 652 -315 C ATOM 1188 CE1 TYR A 199 21.177 6.825 -4.325 1.00 85.63 C ANISOU 1188 CE1 TYR A 199 9799 11878 10859 933 355 -719 C ATOM 1189 CE2 TYR A 199 21.538 8.297 -6.171 1.00 80.51 C ANISOU 1189 CE2 TYR A 199 8809 11905 9875 615 680 -585 C ATOM 1190 CZ TYR A 199 21.352 7.026 -5.674 1.00 76.43 C ANISOU 1190 CZ TYR A 199 8448 11104 9487 871 522 -803 C ATOM 1191 OH TYR A 199 21.344 5.950 -6.531 1.00 69.70 O ANISOU 1191 OH TYR A 199 7579 10355 8547 1053 510 -1106 O ATOM 1192 N VAL A 200 20.116 12.435 -0.831 1.00 65.74 N ANISOU 1192 N VAL A 200 7439 8856 8685 133 281 383 N ATOM 1193 CA VAL A 200 20.375 13.434 0.206 1.00 71.58 C ANISOU 1193 CA VAL A 200 8173 9468 9555 66 193 476 C ATOM 1194 C VAL A 200 19.616 13.076 1.483 1.00 70.25 C ANISOU 1194 C VAL A 200 8210 9046 9435 156 95 445 C ATOM 1195 O VAL A 200 20.203 13.156 2.571 1.00 66.48 O ANISOU 1195 O VAL A 200 7736 8490 9035 213 0 407 O ATOM 1196 CB VAL A 200 20.038 14.854 -0.281 1.00 71.46 C ANISOU 1196 CB VAL A 200 8129 9461 9562 -148 192 671 C ATOM 1197 CG1 VAL A 200 20.109 15.848 0.873 1.00 70.31 C ANISOU 1197 CG1 VAL A 200 8017 9123 9575 -187 60 720 C ATOM 1198 CG2 VAL A 200 20.992 15.264 -1.393 1.00 67.72 C ANISOU 1198 CG2 VAL A 200 7444 9277 9011 -300 285 742 C ATOM 1199 N PRO A 201 18.333 12.691 1.432 1.00 68.63 N ANISOU 1199 N PRO A 201 8167 8739 9171 150 111 459 N ATOM 1200 CA PRO A 201 17.717 12.147 2.655 1.00 67.01 C ANISOU 1200 CA PRO A 201 8135 8363 8962 204 43 424 C ATOM 1201 C PRO A 201 18.416 10.898 3.166 1.00 63.12 C ANISOU 1201 C PRO A 201 7712 7811 8461 342 -32 331 C ATOM 1202 O PRO A 201 18.541 10.711 4.383 1.00 64.72 O ANISOU 1202 O PRO A 201 8019 7903 8669 376 -131 332 O ATOM 1203 CB PRO A 201 16.275 11.860 2.217 1.00 66.92 C ANISOU 1203 CB PRO A 201 8227 8319 8879 142 97 446 C ATOM 1204 CG PRO A 201 16.022 12.833 1.137 1.00 66.63 C ANISOU 1204 CG PRO A 201 8086 8379 8852 55 144 523 C ATOM 1205 CD PRO A 201 17.319 12.916 0.383 1.00 66.70 C ANISOU 1205 CD PRO A 201 7946 8542 8857 61 178 525 C ATOM 1206 N PHE A 202 18.884 10.041 2.258 1.00 56.10 N ANISOU 1206 N PHE A 202 6771 6992 7551 435 -11 238 N ATOM 1207 CA PHE A 202 19.593 8.829 2.655 1.00 63.87 C ANISOU 1207 CA PHE A 202 7821 7882 8566 610 -137 119 C ATOM 1208 C PHE A 202 20.816 9.156 3.509 1.00 70.36 C ANISOU 1208 C PHE A 202 8539 8718 9475 697 -242 86 C ATOM 1209 O PHE A 202 20.977 8.621 4.613 1.00 72.54 O ANISOU 1209 O PHE A 202 8969 8826 9768 771 -400 91 O ATOM 1210 CB PHE A 202 19.992 8.047 1.402 1.00 62.85 C ANISOU 1210 CB PHE A 202 7591 7872 8416 726 -97 -41 C ATOM 1211 CG PHE A 202 20.499 6.659 1.671 1.00 70.17 C ANISOU 1211 CG PHE A 202 8620 8639 9403 941 -273 -200 C ATOM 1212 CD1 PHE A 202 20.468 6.114 2.942 1.00 73.47 C ANISOU 1212 CD1 PHE A 202 9254 8795 9864 982 -462 -139 C ATOM 1213 CD2 PHE A 202 21.014 5.899 0.638 1.00 76.10 C ANISOU 1213 CD2 PHE A 202 9257 9501 10156 1108 -271 -423 C ATOM 1214 CE1 PHE A 202 20.939 4.847 3.177 1.00 78.88 C ANISOU 1214 CE1 PHE A 202 10067 9279 10625 1182 -682 -264 C ATOM 1215 CE2 PHE A 202 21.485 4.628 0.866 1.00 75.62 C ANISOU 1215 CE2 PHE A 202 9296 9248 10187 1343 -483 -603 C ATOM 1216 CZ PHE A 202 21.447 4.100 2.137 1.00 79.28 C ANISOU 1216 CZ PHE A 202 10003 9395 10724 1380 -707 -507 C ATOM 1217 N ILE A 203 21.692 10.031 3.011 1.00 69.89 N ANISOU 1217 N ILE A 203 8223 8871 9462 667 -169 66 N ATOM 1218 CA ILE A 203 22.931 10.333 3.726 1.00 70.07 C ANISOU 1218 CA ILE A 203 8101 8940 9583 743 -275 9 C ATOM 1219 C ILE A 203 22.628 10.977 5.074 1.00 68.51 C ANISOU 1219 C ILE A 203 8043 8585 9403 671 -375 114 C ATOM 1220 O ILE A 203 23.185 10.584 6.106 1.00 61.96 O ANISOU 1220 O ILE A 203 7279 7659 8605 783 -545 72 O ATOM 1221 CB ILE A 203 23.843 11.227 2.870 1.00 67.00 C ANISOU 1221 CB ILE A 203 7390 8840 9226 648 -158 -7 C ATOM 1222 CG1 ILE A 203 24.189 10.534 1.555 1.00 68.52 C ANISOU 1222 CG1 ILE A 203 7420 9264 9349 728 -43 -152 C ATOM 1223 CG2 ILE A 203 25.111 11.566 3.623 1.00 62.39 C ANISOU 1223 CG2 ILE A 203 6625 8319 8761 704 -276 -75 C ATOM 1224 CD1 ILE A 203 24.882 11.438 0.566 1.00 75.16 C ANISOU 1224 CD1 ILE A 203 7956 10453 10148 555 118 -121 C ATOM 1225 N VAL A 204 21.738 11.974 5.082 1.00 68.09 N ANISOU 1225 N VAL A 204 8035 8512 9324 499 -292 232 N ATOM 1226 CA VAL A 204 21.439 12.706 6.313 1.00 64.98 C ANISOU 1226 CA VAL A 204 7739 8013 8938 443 -378 276 C ATOM 1227 C VAL A 204 20.881 11.767 7.375 1.00 65.55 C ANISOU 1227 C VAL A 204 8061 7945 8902 504 -469 277 C ATOM 1228 O VAL A 204 21.332 11.764 8.527 1.00 66.60 O ANISOU 1228 O VAL A 204 8259 8027 9017 550 -610 260 O ATOM 1229 CB VAL A 204 20.471 13.865 6.027 1.00 56.49 C ANISOU 1229 CB VAL A 204 6664 6928 7872 291 -296 354 C ATOM 1230 CG1 VAL A 204 19.900 14.399 7.325 1.00 59.98 C ANISOU 1230 CG1 VAL A 204 7227 7276 8289 274 -375 333 C ATOM 1231 CG2 VAL A 204 21.185 14.972 5.267 1.00 55.27 C ANISOU 1231 CG2 VAL A 204 6299 6869 7831 182 -275 403 C ATOM 1232 N THR A 205 19.886 10.960 7.005 1.00 66.29 N ANISOU 1232 N THR A 205 8302 7982 8903 478 -403 312 N ATOM 1233 CA THR A 205 19.340 9.991 7.947 1.00 66.07 C ANISOU 1233 CA THR A 205 8524 7824 8753 475 -492 356 C ATOM 1234 C THR A 205 20.407 9.003 8.395 1.00 73.22 C ANISOU 1234 C THR A 205 9501 8627 9694 637 -693 319 C ATOM 1235 O THR A 205 20.450 8.611 9.567 1.00 73.97 O ANISOU 1235 O THR A 205 9780 8626 9698 635 -843 376 O ATOM 1236 CB THR A 205 18.162 9.258 7.313 1.00 64.13 C ANISOU 1236 CB THR A 205 8398 7536 8434 391 -397 399 C ATOM 1237 OG1 THR A 205 17.159 10.210 6.937 1.00 70.05 O ANISOU 1237 OG1 THR A 205 9065 8385 9167 268 -244 415 O ATOM 1238 CG2 THR A 205 17.567 8.265 8.291 1.00 59.18 C ANISOU 1238 CG2 THR A 205 8038 6780 7668 317 -492 485 C ATOM 1239 N LEU A 206 21.282 8.594 7.476 1.00 71.22 N ANISOU 1239 N LEU A 206 9095 8407 9557 784 -714 211 N ATOM 1240 CA LEU A 206 22.343 7.663 7.839 1.00 69.37 C ANISOU 1240 CA LEU A 206 8891 8070 9395 992 -940 126 C ATOM 1241 C LEU A 206 23.325 8.302 8.810 1.00 67.69 C ANISOU 1241 C LEU A 206 8584 7907 9228 1046 -1074 104 C ATOM 1242 O LEU A 206 23.847 7.629 9.705 1.00 63.83 O ANISOU 1242 O LEU A 206 8237 7281 8736 1166 -1318 106 O ATOM 1243 CB LEU A 206 23.069 7.177 6.586 1.00 68.74 C ANISOU 1243 CB LEU A 206 8603 8086 9429 1162 -911 -54 C ATOM 1244 CG LEU A 206 24.254 6.253 6.864 1.00 66.60 C ANISOU 1244 CG LEU A 206 8300 7728 9276 1438 -1170 -212 C ATOM 1245 CD1 LEU A 206 23.779 4.999 7.577 1.00 68.61 C ANISOU 1245 CD1 LEU A 206 8929 7645 9495 1492 -1416 -131 C ATOM 1246 CD2 LEU A 206 24.981 5.908 5.578 1.00 65.91 C ANISOU 1246 CD2 LEU A 206 7933 7826 9284 1614 -1102 -453 C ATOM 1247 N LEU A 207 23.592 9.597 8.647 1.00 71.05 N ANISOU 1247 N LEU A 207 8784 8507 9703 951 -950 91 N ATOM 1248 CA LEU A 207 24.489 10.279 9.572 1.00 68.27 C ANISOU 1248 CA LEU A 207 8336 8199 9405 979 -1088 58 C ATOM 1249 C LEU A 207 23.856 10.418 10.949 1.00 68.21 C ANISOU 1249 C LEU A 207 8586 8088 9244 897 -1186 154 C ATOM 1250 O LEU A 207 24.552 10.352 11.967 1.00 66.32 O ANISOU 1250 O LEU A 207 8392 7815 8989 976 -1395 132 O ATOM 1251 CB LEU A 207 24.875 11.645 9.012 1.00 63.44 C ANISOU 1251 CB LEU A 207 7441 7765 8897 855 -953 35 C ATOM 1252 CG LEU A 207 25.757 11.605 7.765 1.00 58.28 C ANISOU 1252 CG LEU A 207 6481 7306 8356 900 -859 -62 C ATOM 1253 CD1 LEU A 207 25.869 12.987 7.135 1.00 58.28 C ANISOU 1253 CD1 LEU A 207 6266 7458 8418 685 -713 -2 C ATOM 1254 CD2 LEU A 207 27.133 11.057 8.115 1.00 60.06 C ANISOU 1254 CD2 LEU A 207 6537 7593 8688 1106 -1049 -219 C ATOM 1255 N VAL A 208 22.536 10.604 11.000 1.00 65.76 N ANISOU 1255 N VAL A 208 8427 7760 8800 740 -1039 244 N ATOM 1256 CA VAL A 208 21.850 10.728 12.283 1.00 70.01 C ANISOU 1256 CA VAL A 208 9179 8279 9143 643 -1090 309 C ATOM 1257 C VAL A 208 21.897 9.408 13.042 1.00 72.90 C ANISOU 1257 C VAL A 208 9821 8505 9370 686 -1284 405 C ATOM 1258 O VAL A 208 22.211 9.371 14.237 1.00 72.29 O ANISOU 1258 O VAL A 208 9878 8422 9167 690 -1459 437 O ATOM 1259 CB VAL A 208 20.403 11.205 12.072 1.00 62.31 C ANISOU 1259 CB VAL A 208 8243 7366 8066 475 -875 344 C ATOM 1260 CG1 VAL A 208 19.616 11.100 13.361 1.00 57.35 C ANISOU 1260 CG1 VAL A 208 7821 6784 7185 363 -898 391 C ATOM 1261 CG2 VAL A 208 20.388 12.634 11.560 1.00 55.34 C ANISOU 1261 CG2 VAL A 208 7134 6567 7324 438 -769 263 C ATOM 1262 N TYR A 209 21.584 8.304 12.360 1.00 67.17 N ANISOU 1262 N TYR A 209 9206 7651 8663 711 -1285 458 N ATOM 1263 CA TYR A 209 21.578 7.010 13.032 1.00 62.85 C ANISOU 1263 CA TYR A 209 8966 6907 8008 728 -1515 581 C ATOM 1264 C TYR A 209 22.975 6.598 13.468 1.00 67.38 C ANISOU 1264 C TYR A 209 9528 7379 8695 962 -1822 518 C ATOM 1265 O TYR A 209 23.130 5.942 14.504 1.00 76.08 O ANISOU 1265 O TYR A 209 10894 8346 9666 963 -2077 640 O ATOM 1266 CB TYR A 209 20.960 5.946 12.126 1.00 60.49 C ANISOU 1266 CB TYR A 209 8784 6452 7749 710 -1483 623 C ATOM 1267 CG TYR A 209 19.452 5.927 12.179 1.00 66.56 C ANISOU 1267 CG TYR A 209 9685 7270 8334 437 -1286 750 C ATOM 1268 CD1 TYR A 209 18.788 5.544 13.335 1.00 66.30 C ANISOU 1268 CD1 TYR A 209 9921 7223 8047 229 -1351 931 C ATOM 1269 CD2 TYR A 209 18.693 6.292 11.078 1.00 67.85 C ANISOU 1269 CD2 TYR A 209 9692 7530 8559 372 -1040 687 C ATOM 1270 CE1 TYR A 209 17.408 5.526 13.397 1.00 71.51 C ANISOU 1270 CE1 TYR A 209 10651 7990 8531 -39 -1153 1024 C ATOM 1271 CE2 TYR A 209 17.312 6.271 11.129 1.00 67.87 C ANISOU 1271 CE2 TYR A 209 9776 7601 8410 135 -874 776 C ATOM 1272 CZ TYR A 209 16.675 5.892 12.292 1.00 73.98 C ANISOU 1272 CZ TYR A 209 10778 8387 8944 -71 -920 933 C ATOM 1273 OH TYR A 209 15.301 5.875 12.350 1.00 78.65 O ANISOU 1273 OH TYR A 209 11400 9107 9378 -325 -736 998 O ATOM 1274 N ILE A 210 24.002 6.972 12.702 1.00 65.59 N ANISOU 1274 N ILE A 210 8989 7235 8698 1151 -1815 332 N ATOM 1275 CA ILE A 210 25.373 6.731 13.144 1.00 66.53 C ANISOU 1275 CA ILE A 210 9020 7316 8943 1384 -2102 228 C ATOM 1276 C ILE A 210 25.669 7.536 14.402 1.00 68.90 C ANISOU 1276 C ILE A 210 9347 7706 9128 1318 -2205 265 C ATOM 1277 O ILE A 210 26.296 7.036 15.343 1.00 66.82 O ANISOU 1277 O ILE A 210 9234 7337 8820 1429 -2518 299 O ATOM 1278 CB ILE A 210 26.368 7.053 12.015 1.00 68.77 C ANISOU 1278 CB ILE A 210 8898 7760 9473 1556 -2020 2 C ATOM 1279 CG1 ILE A 210 26.237 6.043 10.879 1.00 66.91 C ANISOU 1279 CG1 ILE A 210 8656 7435 9331 1685 -1991 -87 C ATOM 1280 CG2 ILE A 210 27.792 7.062 12.545 1.00 69.56 C ANISOU 1280 CG2 ILE A 210 8822 7898 9711 1774 -2291 -139 C ATOM 1281 CD1 ILE A 210 27.237 6.254 9.771 1.00 66.26 C ANISOU 1281 CD1 ILE A 210 8158 7579 9440 1852 -1900 -335 C ATOM 1282 N LYS A 211 25.221 8.797 14.439 1.00 68.09 N ANISOU 1282 N LYS A 211 9108 7786 8977 1147 -1974 247 N ATOM 1283 CA LYS A 211 25.368 9.607 15.645 1.00 72.77 C ANISOU 1283 CA LYS A 211 9739 8468 9442 1077 -2066 245 C ATOM 1284 C LYS A 211 24.551 9.044 16.798 1.00 75.75 C ANISOU 1284 C LYS A 211 10492 8790 9501 949 -2158 418 C ATOM 1285 O LYS A 211 24.918 9.225 17.965 1.00 75.16 O ANISOU 1285 O LYS A 211 10526 8758 9275 949 -2353 430 O ATOM 1286 CB LYS A 211 24.956 11.053 15.367 1.00 72.52 C ANISOU 1286 CB LYS A 211 9503 8598 9455 934 -1825 165 C ATOM 1287 CG LYS A 211 26.059 11.921 14.784 1.00 76.74 C ANISOU 1287 CG LYS A 211 9682 9223 10251 997 -1830 21 C ATOM 1288 CD LYS A 211 27.081 12.304 15.845 1.00 80.50 C ANISOU 1288 CD LYS A 211 10106 9734 10746 1072 -2092 -66 C ATOM 1289 N ILE A 212 23.444 8.363 16.492 1.00 76.82 N ANISOU 1289 N ILE A 212 10821 8858 9510 813 -2022 555 N ATOM 1290 CA ILE A 212 22.634 7.738 17.534 1.00 75.49 C ANISOU 1290 CA ILE A 212 11004 8670 9009 629 -2092 753 C ATOM 1291 C ILE A 212 23.351 6.523 18.110 1.00 78.85 C ANISOU 1291 C ILE A 212 11697 8862 9401 741 -2475 889 C ATOM 1292 O ILE A 212 23.426 6.348 19.332 1.00 81.23 O ANISOU 1292 O ILE A 212 12234 9186 9445 664 -2673 1015 O ATOM 1293 CB ILE A 212 21.244 7.368 16.983 1.00 72.94 C ANISOU 1293 CB ILE A 212 10775 8353 8584 420 -1838 858 C ATOM 1294 CG1 ILE A 212 20.367 8.618 16.858 1.00 72.24 C ANISOU 1294 CG1 ILE A 212 10488 8519 8442 291 -1522 738 C ATOM 1295 CG2 ILE A 212 20.575 6.319 17.861 1.00 71.22 C ANISOU 1295 CG2 ILE A 212 10941 8062 8058 211 -1961 1112 C ATOM 1296 CD1 ILE A 212 18.962 8.339 16.351 1.00 65.08 C ANISOU 1296 CD1 ILE A 212 9627 7664 7437 90 -1276 811 C ATOM 1297 N TYR A 213 23.890 5.666 17.237 1.00 80.40 N ANISOU 1297 N TYR A 213 11866 8833 9849 936 -2607 855 N ATOM 1298 CA TYR A 213 24.609 4.484 17.706 1.00 74.91 C ANISOU 1298 CA TYR A 213 11423 7857 9182 1095 -3032 956 C ATOM 1299 C TYR A 213 25.796 4.871 18.580 1.00 76.60 C ANISOU 1299 C TYR A 213 11566 8127 9414 1272 -3314 873 C ATOM 1300 O TYR A 213 26.091 4.197 19.574 1.00 75.58 O ANISOU 1300 O TYR A 213 11741 7846 9129 1288 -3670 1037 O ATOM 1301 CB TYR A 213 25.070 3.642 16.515 1.00 69.47 C ANISOU 1301 CB TYR A 213 10637 6949 8811 1339 -3122 828 C ATOM 1302 CG TYR A 213 25.850 2.401 16.899 1.00 82.87 C ANISOU 1302 CG TYR A 213 12578 8305 10605 1567 -3612 881 C ATOM 1303 CD1 TYR A 213 25.198 1.248 17.317 1.00 88.00 C ANISOU 1303 CD1 TYR A 213 13681 8643 11110 1422 -3838 1153 C ATOM 1304 CD2 TYR A 213 27.237 2.376 16.828 1.00 83.04 C ANISOU 1304 CD2 TYR A 213 12370 8305 10877 1924 -3876 656 C ATOM 1305 CE1 TYR A 213 25.906 0.107 17.664 1.00 88.45 C ANISOU 1305 CE1 TYR A 213 13945 8382 11281 1597 -4262 1171 C ATOM 1306 CE2 TYR A 213 27.955 1.241 17.174 1.00 84.14 C ANISOU 1306 CE2 TYR A 213 12701 8139 11130 2144 -4318 655 C ATOM 1307 CZ TYR A 213 27.286 0.109 17.589 1.00 88.74 C ANISOU 1307 CZ TYR A 213 13713 8432 11572 1950 -4461 892 C ATOM 1308 OH TYR A 213 27.998 -1.023 17.933 1.00 93.97 O ANISOU 1308 OH TYR A 213 14524 8828 12351 2091 -4813 843 O ATOM 1309 N ILE A 214 26.491 5.955 18.226 1.00 79.22 N ANISOU 1309 N ILE A 214 11503 8668 9929 1388 -3184 634 N ATOM 1310 CA ILE A 214 27.667 6.368 18.988 1.00 79.71 C ANISOU 1310 CA ILE A 214 11448 8796 10043 1553 -3456 525 C ATOM 1311 C ILE A 214 27.278 6.769 20.407 1.00 82.99 C ANISOU 1311 C ILE A 214 12112 9325 10094 1359 -3536 663 C ATOM 1312 O ILE A 214 27.993 6.468 21.373 1.00 77.18 O ANISOU 1312 O ILE A 214 11526 8534 9267 1459 -3903 709 O ATOM 1313 CB ILE A 214 28.405 7.505 18.256 1.00 74.49 C ANISOU 1313 CB ILE A 214 10301 8350 9651 1642 -3272 259 C ATOM 1314 CG1 ILE A 214 28.993 6.995 16.944 1.00 73.37 C ANISOU 1314 CG1 ILE A 214 9897 8156 9825 1855 -3239 102 C ATOM 1315 CG2 ILE A 214 29.508 8.085 19.125 1.00 79.54 C ANISOU 1315 CG2 ILE A 214 10802 9091 10328 1753 -3532 141 C ATOM 1316 CD1 ILE A 214 29.840 8.022 16.221 1.00 79.87 C ANISOU 1316 CD1 ILE A 214 10233 9224 10891 1906 -3079 -130 C ATOM 1317 N VAL A 215 26.138 7.447 20.558 1.00 80.48 N ANISOU 1317 N VAL A 215 11834 9193 9553 1092 -3207 710 N ATOM 1318 CA VAL A 215 25.693 7.866 21.883 1.00 80.01 C ANISOU 1318 CA VAL A 215 11978 9313 9108 905 -3241 790 C ATOM 1319 C VAL A 215 25.303 6.658 22.722 1.00 86.31 C ANISOU 1319 C VAL A 215 13235 9978 9582 774 -3480 1098 C ATOM 1320 O VAL A 215 25.668 6.557 23.900 1.00 89.76 O ANISOU 1320 O VAL A 215 13882 10466 9758 750 -3755 1189 O ATOM 1321 CB VAL A 215 24.532 8.868 21.764 1.00 69.82 C ANISOU 1321 CB VAL A 215 10575 8272 7681 685 -2829 710 C ATOM 1322 CG1 VAL A 215 23.873 9.073 23.115 1.00 70.46 C ANISOU 1322 CG1 VAL A 215 10891 8582 7299 474 -2833 787 C ATOM 1323 CG2 VAL A 215 25.035 10.188 21.201 1.00 70.96 C ANISOU 1323 CG2 VAL A 215 10323 8520 8117 791 -2692 435 C ATOM 1324 N LEU A 216 24.556 5.722 22.131 1.00 88.27 N ANISOU 1324 N LEU A 216 13660 10047 9830 664 -3400 1278 N ATOM 1325 CA LEU A 216 24.129 4.539 22.870 1.00 81.42 C ANISOU 1325 CA LEU A 216 13257 9014 8666 480 -3641 1616 C ATOM 1326 C LEU A 216 25.314 3.682 23.294 1.00 84.21 C ANISOU 1326 C LEU A 216 13802 9063 9129 728 -4180 1700 C ATOM 1327 O LEU A 216 25.268 3.046 24.353 1.00 81.69 O ANISOU 1327 O LEU A 216 13836 8687 8514 577 -4427 1947 O ATOM 1328 CB LEU A 216 23.148 3.725 22.025 1.00 83.40 C ANISOU 1328 CB LEU A 216 13629 9094 8967 318 -3470 1765 C ATOM 1329 CG LEU A 216 21.846 4.440 21.657 1.00 89.34 C ANISOU 1329 CG LEU A 216 14218 10142 9584 56 -2973 1707 C ATOM 1330 CD1 LEU A 216 21.017 3.625 20.676 1.00 88.79 C ANISOU 1330 CD1 LEU A 216 14221 9881 9633 -62 -2839 1814 C ATOM 1331 CD2 LEU A 216 21.046 4.736 22.911 1.00 97.88 C ANISOU 1331 CD2 LEU A 216 15482 11550 10159 -274 -2870 1850 C ATOM 1332 N ARG A 217 26.382 3.651 22.492 1.00 81.94 N ANISOU 1332 N ARG A 217 13237 8618 9279 1094 -4322 1464 N ATOM 1333 CA ARG A 217 27.561 2.877 22.871 1.00 83.41 C ANISOU 1333 CA ARG A 217 13486 8566 9641 1348 -4750 1435 C ATOM 1334 C ARG A 217 28.345 3.556 23.985 1.00 85.61 C ANISOU 1334 C ARG A 217 13711 9042 9775 1403 -4934 1364 C ATOM 1335 O ARG A 217 28.952 2.873 24.816 1.00 80.30 O ANISOU 1335 O ARG A 217 13221 8234 9057 1442 -5229 1443 O ATOM 1336 CB ARG A 217 28.460 2.641 21.658 1.00 74.00 C ANISOU 1336 CB ARG A 217 11946 7228 8942 1710 -4789 1141 C ATOM 1337 N ARG A 218 28.347 4.891 24.021 1.00 77.47 N ANISOU 1337 N ARG A 218 12427 8320 8687 1399 -4771 1198 N ATOM 1338 CA ARG A 218 28.948 5.589 25.152 1.00 79.95 C ANISOU 1338 CA ARG A 218 12725 8839 8812 1411 -4955 1127 C ATOM 1339 C ARG A 218 28.170 5.328 26.435 1.00 82.04 C ANISOU 1339 C ARG A 218 13403 9226 8543 1087 -4970 1402 C ATOM 1340 O ARG A 218 28.765 5.243 27.517 1.00 84.60 O ANISOU 1340 O ARG A 218 13838 9600 8707 1097 -5207 1432 O ATOM 1341 CB ARG A 218 29.022 7.089 24.868 1.00 75.14 C ANISOU 1341 CB ARG A 218 11692 8536 8320 1397 -4623 823 C ATOM 1342 N ARG A 219 26.847 5.179 26.326 1.00 85.99 N ANISOU 1342 N ARG A 219 14111 9803 8758 785 -4704 1599 N ATOM 1343 CA ARG A 219 26.016 4.885 27.490 1.00 84.46 C ANISOU 1343 CA ARG A 219 14260 9795 8035 425 -4645 1858 C ATOM 1344 C ARG A 219 26.340 3.511 28.066 1.00 86.08 C ANISOU 1344 C ARG A 219 14765 9710 8230 380 -4920 2118 C ATOM 1345 O ARG A 219 26.501 3.361 29.283 1.00 90.06 O ANISOU 1345 O ARG A 219 15467 10337 8414 256 -5076 2247 O ATOM 1346 CB ARG A 219 24.539 4.978 27.102 1.00 85.75 C ANISOU 1346 CB ARG A 219 14494 10127 7961 100 -4243 1970 C ATOM 1347 CG ARG A 219 23.566 4.985 28.270 1.00 97.90 C ANISOU 1347 CG ARG A 219 16277 12019 8900 -302 -4086 2160 C ATOM 1348 CD ARG A 219 22.137 5.191 27.780 1.00103.51 C ANISOU 1348 CD ARG A 219 16923 12951 9455 -597 -3619 2177 C ATOM 1349 NE ARG A 219 22.015 6.380 26.940 1.00103.98 N ANISOU 1349 NE ARG A 219 16513 13152 9842 -422 -3259 1780 N ATOM 1350 CZ ARG A 219 21.746 7.599 27.400 1.00102.81 C ANISOU 1350 CZ ARG A 219 16138 13388 9536 -439 -3032 1497 C ATOM 1351 NH1 ARG A 219 21.567 7.793 28.700 1.00112.25 N ANISOU 1351 NH1 ARG A 219 17509 14920 10223 -616 -3093 1534 N ATOM 1352 NH2 ARG A 219 21.656 8.624 26.563 1.00 90.07 N ANISOU 1352 NH2 ARG A 219 14137 11821 8266 -282 -2765 1173 N ATOM 1353 N ARG A 220 26.443 2.493 27.205 1.00 85.93 N ANISOU 1353 N ARG A 220 14788 9305 8558 483 -5002 2177 N ATOM 1354 CA ARG A 220 26.753 1.145 27.680 1.00 92.53 C ANISOU 1354 CA ARG A 220 15922 9808 9426 451 -5313 2391 C ATOM 1355 C ARG A 220 28.118 1.092 28.355 1.00 98.18 C ANISOU 1355 C ARG A 220 16600 10438 10265 730 -5700 2278 C ATOM 1356 O ARG A 220 28.296 0.384 29.353 1.00 99.06 O ANISOU 1356 O ARG A 220 17008 10452 10178 616 -5960 2492 O ATOM 1357 CB ARG A 220 26.686 0.149 26.522 1.00 94.83 C ANISOU 1357 CB ARG A 220 16221 9701 10109 561 -5350 2378 C ATOM 1358 CG ARG A 220 25.281 -0.055 25.969 1.00100.75 C ANISOU 1358 CG ARG A 220 17071 10487 10720 234 -5015 2543 C ATOM 1359 CD ARG A 220 25.299 -0.715 24.596 1.00102.73 C ANISOU 1359 CD ARG A 220 17220 10409 11403 417 -5011 2417 C ATOM 1360 NE ARG A 220 23.971 -0.712 23.986 1.00105.76 N ANISOU 1360 NE ARG A 220 17640 10872 11673 124 -4663 2533 N ATOM 1361 CZ ARG A 220 23.743 -0.876 22.687 1.00111.13 C ANISOU 1361 CZ ARG A 220 18166 11401 12658 249 -4533 2393 C ATOM 1362 NH1 ARG A 220 24.756 -1.052 21.850 1.00115.91 N ANISOU 1362 NH1 ARG A 220 18552 11801 13687 664 -4699 2115 N ATOM 1363 NH2 ARG A 220 22.500 -0.857 22.220 1.00109.07 N ANISOU 1363 NH2 ARG A 220 17943 11230 12267 -44 -4223 2509 N ATOM 1364 N LYS A 221 29.096 1.832 27.826 1.00 87.90 N ANISOU 1364 N LYS A 221 14922 9183 9293 1081 -5746 1943 N ATOM 1365 CA LYS A 221 30.396 1.903 28.485 1.00 91.01 C ANISOU 1365 CA LYS A 221 15227 9552 9800 1332 -6088 1803 C ATOM 1366 C LYS A 221 30.311 2.643 29.815 1.00 92.81 C ANISOU 1366 C LYS A 221 15563 10123 9576 1152 -6111 1881 C ATOM 1367 O LYS A 221 31.080 2.348 30.738 1.00 97.14 O ANISOU 1367 O LYS A 221 16229 10626 10054 1227 -6434 1922 O ATOM 1368 CB LYS A 221 31.420 2.575 27.569 1.00 88.24 C ANISOU 1368 CB LYS A 221 14391 9229 9907 1702 -6082 1409 C ATOM 1369 N ARG A 222 29.386 3.599 29.935 1.00 89.90 N ANISOU 1369 N ARG A 222 15156 10111 8890 923 -5782 1877 N ATOM 1370 CA ARG A 222 29.220 4.328 31.190 1.00 91.86 C ANISOU 1370 CA ARG A 222 15494 10740 8669 746 -5774 1897 C ATOM 1371 C ARG A 222 28.375 3.544 32.190 1.00 96.10 C ANISOU 1371 C ARG A 222 16450 11352 8712 379 -5763 2271 C ATOM 1372 O ARG A 222 28.677 3.536 33.390 1.00100.34 O ANISOU 1372 O ARG A 222 17145 12050 8928 306 -5948 2359 O ATOM 1373 CB ARG A 222 28.596 5.698 30.923 1.00 87.62 C ANISOU 1373 CB ARG A 222 14726 10572 7995 668 -5443 1670 C ATOM 1374 N ASN A1002 27.322 2.874 31.712 1.00 85.72 N ANISOU 1374 N ASN A1002 12716 9421 10431 154 -1889 1403 N ATOM 1375 CA ASN A1002 26.456 2.104 32.601 1.00 78.54 C ANISOU 1375 CA ASN A1002 11488 8720 9636 336 -1772 1042 C ATOM 1376 C ASN A1002 27.206 0.951 33.259 1.00 74.17 C ANISOU 1376 C ASN A1002 10829 8409 8943 253 -1283 980 C ATOM 1377 O ASN A1002 26.974 0.646 34.435 1.00 77.99 O ANISOU 1377 O ASN A1002 11066 9013 9552 361 -1151 748 O ATOM 1378 CB ASN A1002 25.242 1.584 31.828 1.00 72.27 C ANISOU 1378 CB ASN A1002 10694 8018 8747 370 -1959 956 C ATOM 1379 CG ASN A1002 24.296 2.693 31.414 1.00 85.39 C ANISOU 1379 CG ASN A1002 12363 9440 10641 548 -2522 954 C ATOM 1380 OD1 ASN A1002 24.569 3.871 31.643 1.00 91.93 O ANISOU 1380 OD1 ASN A1002 13249 9977 11701 641 -2774 1033 O ATOM 1381 ND2 ASN A1002 23.179 2.324 30.796 1.00 95.12 N ANISOU 1381 ND2 ASN A1002 13533 10764 11844 599 -2763 857 N ATOM 1382 N ILE A1003 28.104 0.295 32.520 1.00 69.88 N ANISOU 1382 N ILE A1003 10476 7942 8134 67 -1017 1180 N ATOM 1383 CA ILE A1003 28.844 -0.824 33.094 1.00 75.25 C ANISOU 1383 CA ILE A1003 11058 8796 8739 40 -607 1126 C ATOM 1384 C ILE A1003 29.846 -0.336 34.137 1.00 79.70 C ANISOU 1384 C ILE A1003 11473 9334 9474 69 -527 1154 C ATOM 1385 O ILE A1003 30.117 -1.035 35.121 1.00 81.90 O ANISOU 1385 O ILE A1003 11597 9734 9788 131 -334 1048 O ATOM 1386 CB ILE A1003 29.526 -1.644 31.981 1.00 76.66 C ANISOU 1386 CB ILE A1003 11445 9056 8624 -116 -342 1259 C ATOM 1387 CG1 ILE A1003 30.131 -2.927 32.553 1.00 83.23 C ANISOU 1387 CG1 ILE A1003 12171 10007 9446 -76 25 1164 C ATOM 1388 CG2 ILE A1003 30.599 -0.830 31.276 1.00 75.86 C ANISOU 1388 CG2 ILE A1003 11492 8897 8434 -279 -312 1524 C ATOM 1389 CD1 ILE A1003 30.765 -3.812 31.509 1.00 89.05 C ANISOU 1389 CD1 ILE A1003 13083 10813 9939 -170 311 1194 C ATOM 1390 N PHE A1004 30.403 0.862 33.954 1.00 72.73 N ANISOU 1390 N PHE A1004 10657 8281 8697 0 -708 1309 N ATOM 1391 CA PHE A1004 31.300 1.419 34.961 1.00 72.86 C ANISOU 1391 CA PHE A1004 10523 8260 8901 1 -698 1302 C ATOM 1392 C PHE A1004 30.561 1.658 36.271 1.00 75.78 C ANISOU 1392 C PHE A1004 10709 8641 9442 194 -837 1009 C ATOM 1393 O PHE A1004 31.045 1.293 37.349 1.00 75.51 O ANISOU 1393 O PHE A1004 10525 8740 9424 231 -703 911 O ATOM 1394 CB PHE A1004 31.920 2.718 34.446 1.00 74.85 C ANISOU 1394 CB PHE A1004 10908 8273 9256 -164 -904 1525 C ATOM 1395 CG PHE A1004 32.831 3.387 35.431 1.00 80.49 C ANISOU 1395 CG PHE A1004 11471 8921 10192 -205 -951 1497 C ATOM 1396 CD1 PHE A1004 34.093 2.876 35.685 1.00 79.31 C ANISOU 1396 CD1 PHE A1004 11166 8951 10018 -317 -675 1584 C ATOM 1397 CD2 PHE A1004 32.429 4.533 36.100 1.00 83.97 C ANISOU 1397 CD2 PHE A1004 11907 9110 10888 -118 -1297 1351 C ATOM 1398 CE1 PHE A1004 34.938 3.492 36.589 1.00 82.95 C ANISOU 1398 CE1 PHE A1004 11465 9368 10684 -377 -769 1550 C ATOM 1399 CE2 PHE A1004 33.269 5.154 37.007 1.00 85.07 C ANISOU 1399 CE2 PHE A1004 11928 9181 11215 -183 -1370 1289 C ATOM 1400 CZ PHE A1004 34.525 4.633 37.251 1.00 84.25 C ANISOU 1400 CZ PHE A1004 11666 9282 11062 -331 -1119 1402 C ATOM 1401 N GLU A1005 29.376 2.270 36.194 1.00 75.34 N ANISOU 1401 N GLU A1005 10654 8467 9503 325 -1114 852 N ATOM 1402 CA GLU A1005 28.576 2.488 37.395 1.00 80.23 C ANISOU 1402 CA GLU A1005 11062 9155 10266 516 -1188 504 C ATOM 1403 C GLU A1005 28.115 1.169 38.000 1.00 86.02 C ANISOU 1403 C GLU A1005 11656 10202 10825 527 -889 366 C ATOM 1404 O GLU A1005 28.046 1.030 39.227 1.00 90.45 O ANISOU 1404 O GLU A1005 12070 10923 11372 580 -788 167 O ATOM 1405 CB GLU A1005 27.375 3.375 37.076 1.00 77.92 C ANISOU 1405 CB GLU A1005 10741 8676 10189 694 -1544 334 C ATOM 1406 CG GLU A1005 27.742 4.831 36.890 1.00 84.80 C ANISOU 1406 CG GLU A1005 11751 9159 11311 720 -1903 409 C ATOM 1407 CD GLU A1005 28.491 5.393 38.081 1.00 89.89 C ANISOU 1407 CD GLU A1005 12315 9761 12076 724 -1883 248 C ATOM 1408 OE1 GLU A1005 27.991 5.262 39.219 1.00 89.61 O ANISOU 1408 OE1 GLU A1005 12069 9916 12064 880 -1796 -120 O ATOM 1409 OE2 GLU A1005 29.591 5.949 37.880 1.00 88.50 O ANISOU 1409 OE2 GLU A1005 12285 9394 11947 539 -1944 483 O ATOM 1410 N MET A1006 27.798 0.187 37.153 1.00 78.13 N ANISOU 1410 N MET A1006 10736 9284 9667 448 -755 474 N ATOM 1411 CA MET A1006 27.337 -1.104 37.657 1.00 72.09 C ANISOU 1411 CA MET A1006 9881 8748 8762 410 -494 376 C ATOM 1412 C MET A1006 28.381 -1.755 38.553 1.00 75.65 C ANISOU 1412 C MET A1006 10336 9295 9114 362 -262 468 C ATOM 1413 O MET A1006 28.038 -2.402 39.549 1.00 76.42 O ANISOU 1413 O MET A1006 10345 9565 9126 348 -119 363 O ATOM 1414 CB MET A1006 26.994 -2.033 36.497 1.00 63.48 C ANISOU 1414 CB MET A1006 8926 7661 7531 307 -419 476 C ATOM 1415 CG MET A1006 26.279 -3.292 36.913 1.00 70.23 C ANISOU 1415 CG MET A1006 9703 8684 8298 231 -215 360 C ATOM 1416 SD MET A1006 26.609 -4.663 35.798 1.00 70.93 S ANISOU 1416 SD MET A1006 10037 8714 8198 86 -29 502 S ATOM 1417 CE MET A1006 25.235 -5.747 36.183 1.00 79.60 C ANISOU 1417 CE MET A1006 11010 9948 9288 -46 55 311 C ATOM 1418 N LEU A1007 29.660 -1.591 38.223 1.00 74.32 N ANISOU 1418 N LEU A1007 10257 9030 8951 321 -234 678 N ATOM 1419 CA LEU A1007 30.716 -2.231 38.992 1.00 72.19 C ANISOU 1419 CA LEU A1007 9955 8841 8633 310 -74 777 C ATOM 1420 C LEU A1007 31.310 -1.346 40.078 1.00 77.91 C ANISOU 1420 C LEU A1007 10574 9585 9442 343 -217 715 C ATOM 1421 O LEU A1007 31.846 -1.881 41.054 1.00 81.18 O ANISOU 1421 O LEU A1007 10944 10120 9781 352 -154 740 O ATOM 1422 CB LEU A1007 31.835 -2.718 38.066 1.00 71.02 C ANISOU 1422 CB LEU A1007 9882 8633 8470 261 76 992 C ATOM 1423 CG LEU A1007 31.556 -4.102 37.475 1.00 67.80 C ANISOU 1423 CG LEU A1007 9585 8237 7941 251 288 1010 C ATOM 1424 CD1 LEU A1007 30.727 -4.015 36.198 1.00 65.13 C ANISOU 1424 CD1 LEU A1007 9386 7844 7514 183 249 974 C ATOM 1425 CD2 LEU A1007 32.848 -4.848 37.236 1.00 68.79 C ANISOU 1425 CD2 LEU A1007 9698 8348 8090 287 481 1140 C ATOM 1426 N ARG A1008 31.232 -0.018 39.954 1.00 81.15 N ANISOU 1426 N ARG A1008 10972 9855 10007 355 -447 635 N ATOM 1427 CA ARG A1008 31.610 0.793 41.106 1.00 79.83 C ANISOU 1427 CA ARG A1008 10721 9701 9912 383 -602 485 C ATOM 1428 C ARG A1008 30.583 0.693 42.224 1.00 79.95 C ANISOU 1428 C ARG A1008 10660 9903 9815 473 -581 181 C ATOM 1429 O ARG A1008 30.878 1.089 43.357 1.00 82.62 O ANISOU 1429 O ARG A1008 10953 10337 10104 486 -655 22 O ATOM 1430 CB ARG A1008 31.814 2.257 40.711 1.00 75.25 C ANISOU 1430 CB ARG A1008 10178 8848 9565 361 -878 461 C ATOM 1431 CG ARG A1008 30.548 3.009 40.384 1.00 84.73 C ANISOU 1431 CG ARG A1008 11405 9893 10893 488 -1070 258 C ATOM 1432 CD ARG A1008 30.759 4.502 40.562 1.00 91.79 C ANISOU 1432 CD ARG A1008 12342 10481 12053 509 -1399 147 C ATOM 1433 NE ARG A1008 30.802 4.870 41.973 1.00 97.78 N ANISOU 1433 NE ARG A1008 12996 11338 12815 587 -1451 -187 N ATOM 1434 CZ ARG A1008 29.731 5.209 42.684 1.00100.58 C ANISOU 1434 CZ ARG A1008 13254 11756 13206 785 -1504 -595 C ATOM 1435 NH1 ARG A1008 28.534 5.231 42.111 1.00 94.43 N ANISOU 1435 NH1 ARG A1008 12420 10935 12522 941 -1541 -707 N ATOM 1436 NH2 ARG A1008 29.857 5.526 43.966 1.00105.64 N ANISOU 1436 NH2 ARG A1008 13834 12529 13777 825 -1520 -917 N ATOM 1437 N ILE A1009 29.394 0.171 41.926 1.00 74.25 N ANISOU 1437 N ILE A1009 9910 9267 9034 507 -473 81 N ATOM 1438 CA ILE A1009 28.416 -0.151 42.956 1.00 75.30 C ANISOU 1438 CA ILE A1009 9929 9661 9019 531 -350 -186 C ATOM 1439 C ILE A1009 28.680 -1.535 43.536 1.00 78.79 C ANISOU 1439 C ILE A1009 10438 10305 9194 403 -107 -8 C ATOM 1440 O ILE A1009 28.534 -1.752 44.743 1.00 85.17 O ANISOU 1440 O ILE A1009 11227 11348 9787 355 -20 -120 O ATOM 1441 CB ILE A1009 26.996 -0.039 42.373 1.00 72.07 C ANISOU 1441 CB ILE A1009 9394 9267 8722 603 -364 -387 C ATOM 1442 CG1 ILE A1009 26.670 1.415 42.030 1.00 73.75 C ANISOU 1442 CG1 ILE A1009 9547 9243 9230 783 -675 -591 C ATOM 1443 CG2 ILE A1009 25.968 -0.620 43.332 1.00 70.49 C ANISOU 1443 CG2 ILE A1009 9027 9408 8349 556 -136 -634 C ATOM 1444 CD1 ILE A1009 25.423 1.572 41.190 1.00 76.17 C ANISOU 1444 CD1 ILE A1009 9730 9499 9713 890 -796 -718 C ATOM 1445 N ASP A1010 29.079 -2.490 42.694 1.00 72.06 N ANISOU 1445 N ASP A1010 9694 9350 8336 343 -7 269 N ATOM 1446 CA ASP A1010 29.286 -3.870 43.127 1.00 72.56 C ANISOU 1446 CA ASP A1010 9858 9501 8210 243 179 457 C ATOM 1447 C ASP A1010 30.708 -4.106 43.629 1.00 75.95 C ANISOU 1447 C ASP A1010 10352 9894 8612 272 117 675 C ATOM 1448 O ASP A1010 30.908 -4.550 44.763 1.00 79.91 O ANISOU 1448 O ASP A1010 10905 10541 8916 226 124 730 O ATOM 1449 CB ASP A1010 28.966 -4.834 41.979 1.00 68.87 C ANISOU 1449 CB ASP A1010 9481 8902 7784 190 300 582 C ATOM 1450 CG ASP A1010 27.482 -4.951 41.709 1.00 73.05 C ANISOU 1450 CG ASP A1010 9921 9528 8308 113 358 385 C ATOM 1451 OD1 ASP A1010 26.693 -4.307 42.432 1.00 67.48 O ANISOU 1451 OD1 ASP A1010 9046 9009 7582 124 341 140 O ATOM 1452 OD2 ASP A1010 27.105 -5.691 40.773 1.00 78.54 O1+ ANISOU 1452 OD2 ASP A1010 10691 10123 9026 43 418 440 O1+ ATOM 1453 N GLU A1011 31.702 -3.824 42.788 1.00 76.16 N ANISOU 1453 N GLU A1011 10363 9749 8825 334 50 808 N ATOM 1454 CA GLU A1011 33.088 -4.089 43.149 1.00 80.16 C ANISOU 1454 CA GLU A1011 10842 10236 9377 379 -14 997 C ATOM 1455 C GLU A1011 33.663 -2.965 44.003 1.00 86.62 C ANISOU 1455 C GLU A1011 11560 11131 10222 377 -238 897 C ATOM 1456 O GLU A1011 34.212 -3.213 45.081 1.00 98.58 O ANISOU 1456 O GLU A1011 13076 12768 11614 380 -345 952 O ATOM 1457 CB GLU A1011 33.926 -4.284 41.885 1.00 82.54 C ANISOU 1457 CB GLU A1011 11111 10383 9867 418 68 1140 C ATOM 1458 CG GLU A1011 35.344 -4.765 42.134 1.00 89.74 C ANISOU 1458 CG GLU A1011 11913 11291 10894 502 40 1313 C ATOM 1459 CD GLU A1011 35.393 -6.223 42.539 1.00 95.34 C ANISOU 1459 CD GLU A1011 12731 11959 11534 586 111 1445 C ATOM 1460 OE1 GLU A1011 35.895 -6.518 43.646 1.00 99.56 O ANISOU 1460 OE1 GLU A1011 13255 12559 12013 632 -51 1549 O ATOM 1461 OE2 GLU A1011 34.920 -7.072 41.751 1.00 94.59 O ANISOU 1461 OE2 GLU A1011 12763 11742 11436 596 295 1450 O ATOM 1462 N GLY A1012 33.549 -1.725 43.534 1.00 83.15 N ANISOU 1462 N GLY A1012 11062 10592 9938 362 -351 758 N ATOM 1463 CA GLY A1012 34.064 -0.590 44.272 1.00 80.42 C ANISOU 1463 CA GLY A1012 10644 10253 9660 339 -589 621 C ATOM 1464 C GLY A1012 35.145 0.176 43.536 1.00 76.41 C ANISOU 1464 C GLY A1012 10041 9573 9418 270 -701 745 C ATOM 1465 O GLY A1012 36.026 -0.422 42.909 1.00 75.35 O ANISOU 1465 O GLY A1012 9829 9430 9369 254 -588 972 O ATOM 1466 N LEU A1013 35.090 1.505 43.610 1.00 72.47 N ANISOU 1466 N LEU A1013 9539 8928 9066 216 -914 581 N ATOM 1467 CA LEU A1013 36.059 2.381 42.960 1.00 75.06 C ANISOU 1467 CA LEU A1013 9799 9069 9653 69 -1037 711 C ATOM 1468 C LEU A1013 37.076 2.842 43.998 1.00 85.43 C ANISOU 1468 C LEU A1013 10980 10447 11031 -12 -1266 645 C ATOM 1469 O LEU A1013 36.730 3.569 44.935 1.00 92.30 O ANISOU 1469 O LEU A1013 11906 11301 11864 3 -1478 364 O ATOM 1470 CB LEU A1013 35.362 3.575 42.309 1.00 76.93 C ANISOU 1470 CB LEU A1013 10164 9014 10053 35 -1188 614 C ATOM 1471 CG LEU A1013 36.264 4.677 41.743 1.00 81.85 C ANISOU 1471 CG LEU A1013 10778 9382 10939 -188 -1361 759 C ATOM 1472 CD1 LEU A1013 37.119 4.145 40.607 1.00 83.65 C ANISOU 1472 CD1 LEU A1013 10936 9672 11176 -345 -1119 1104 C ATOM 1473 CD2 LEU A1013 35.444 5.879 41.290 1.00 79.42 C ANISOU 1473 CD2 LEU A1013 10661 8711 10803 -183 -1600 657 C ATOM 1474 N ARG A1014 38.324 2.416 43.830 1.00 82.30 N ANISOU 1474 N ARG A1014 10388 10143 10740 -92 -1229 865 N ATOM 1475 CA ARG A1014 39.431 2.846 44.673 1.00 87.70 C ANISOU 1475 CA ARG A1014 10885 10900 11537 -200 -1487 834 C ATOM 1476 C ARG A1014 40.374 3.720 43.858 1.00 91.11 C ANISOU 1476 C ARG A1014 11154 11170 12293 -454 -1533 970 C ATOM 1477 O ARG A1014 40.854 3.301 42.800 1.00 93.58 O ANISOU 1477 O ARG A1014 11348 11510 12699 -513 -1278 1201 O ATOM 1478 CB ARG A1014 40.189 1.647 45.242 1.00 89.70 C ANISOU 1478 CB ARG A1014 10969 11409 11702 -83 -1465 977 C ATOM 1479 CG ARG A1014 39.445 0.867 46.311 1.00 95.14 C ANISOU 1479 CG ARG A1014 11845 12266 12037 80 -1493 888 C ATOM 1480 CD ARG A1014 40.338 0.658 47.527 1.00103.70 C ANISOU 1480 CD ARG A1014 12817 13547 13039 82 -1799 903 C ATOM 1481 NE ARG A1014 39.801 -0.327 48.462 1.00107.67 N ANISOU 1481 NE ARG A1014 13522 14230 13160 204 -1802 939 N ATOM 1482 CZ ARG A1014 40.399 -0.677 49.597 1.00111.85 C ANISOU 1482 CZ ARG A1014 14048 14948 13504 219 -2094 997 C ATOM 1483 NH1 ARG A1014 41.553 -0.119 49.939 1.00113.46 N ANISOU 1483 NH1 ARG A1014 14008 15196 13905 140 -2424 984 N ATOM 1484 NH2 ARG A1014 39.844 -1.584 50.391 1.00112.62 N ANISOU 1484 NH2 ARG A1014 14392 15192 13208 282 -2078 1085 N ATOM 1485 N LEU A1015 40.648 4.926 44.357 1.00 92.65 N ANISOU 1485 N LEU A1015 11353 11202 12646 -633 -1845 811 N ATOM 1486 CA LEU A1015 41.453 5.897 43.627 1.00 98.42 C ANISOU 1486 CA LEU A1015 11974 11728 13694 -955 -1914 952 C ATOM 1487 C LEU A1015 42.928 5.886 44.013 1.00100.85 C ANISOU 1487 C LEU A1015 11893 12218 14209 -1148 -2036 1034 C ATOM 1488 O LEU A1015 43.750 6.434 43.268 1.00 98.40 O ANISOU 1488 O LEU A1015 11399 11829 14161 -1460 -1984 1214 O ATOM 1489 CB LEU A1015 40.885 7.309 43.827 1.00 99.65 C ANISOU 1489 CB LEU A1015 12381 11497 13985 -1071 -2220 736 C ATOM 1490 CG LEU A1015 39.471 7.567 43.292 1.00 99.54 C ANISOU 1490 CG LEU A1015 12694 11242 13885 -893 -2166 655 C ATOM 1491 CD1 LEU A1015 39.000 8.964 43.667 1.00 99.18 C ANISOU 1491 CD1 LEU A1015 12859 10780 14044 -939 -2532 377 C ATOM 1492 CD2 LEU A1015 39.410 7.369 41.782 1.00 97.70 C ANISOU 1492 CD2 LEU A1015 12526 10927 13670 -996 -1904 1008 C ATOM 1493 N LYS A1016 43.285 5.285 45.145 1.00105.59 N ANISOU 1493 N LYS A1016 12353 13074 14693 -995 -2209 921 N ATOM 1494 CA LYS A1016 44.673 5.127 45.549 1.00101.07 C ANISOU 1494 CA LYS A1016 11354 12717 14330 -1119 -2373 997 C ATOM 1495 C LYS A1016 45.057 3.654 45.506 1.00 97.42 C ANISOU 1495 C LYS A1016 10673 12549 13792 -837 -2171 1168 C ATOM 1496 O LYS A1016 44.204 2.765 45.581 1.00 93.98 O ANISOU 1496 O LYS A1016 10480 12152 13076 -558 -2006 1179 O ATOM 1497 CB LYS A1016 44.913 5.693 46.953 1.00 96.36 C ANISOU 1497 CB LYS A1016 10775 12159 13680 -1180 -2856 730 C ATOM 1498 N ILE A1017 46.361 3.401 45.382 1.00 93.92 N ANISOU 1498 N ILE A1017 9745 12296 13643 -915 -2196 1291 N ATOM 1499 CA ILE A1017 46.835 2.030 45.257 1.00 95.27 C ANISOU 1499 CA ILE A1017 9663 12692 13845 -609 -2025 1434 C ATOM 1500 C ILE A1017 46.498 1.247 46.517 1.00 93.58 C ANISOU 1500 C ILE A1017 9634 12578 13344 -317 -2322 1390 C ATOM 1501 O ILE A1017 46.630 1.745 47.643 1.00 98.49 O ANISOU 1501 O ILE A1017 10306 13255 13861 -400 -2751 1258 O ATOM 1502 CB ILE A1017 48.346 2.013 44.968 1.00 99.88 C ANISOU 1502 CB ILE A1017 9604 13484 14862 -733 -2035 1517 C ATOM 1503 CG1 ILE A1017 48.641 2.776 43.677 1.00 99.15 C ANISOU 1503 CG1 ILE A1017 9368 13325 14980 -1097 -1674 1598 C ATOM 1504 CG2 ILE A1017 48.859 0.586 44.863 1.00102.32 C ANISOU 1504 CG2 ILE A1017 9624 13983 15272 -342 -1894 1617 C ATOM 1505 CD1 ILE A1017 50.072 2.657 43.214 1.00100.19 C ANISOU 1505 CD1 ILE A1017 8808 13728 15530 -1237 -1535 1668 C ATOM 1506 N TYR A1018 46.040 0.013 46.328 1.00 96.96 N ANISOU 1506 N TYR A1018 10204 13021 13613 -4 -2100 1503 N ATOM 1507 CA TYR A1018 45.693 -0.867 47.432 1.00100.96 C ANISOU 1507 CA TYR A1018 10937 13603 13821 241 -2341 1544 C ATOM 1508 C TYR A1018 45.961 -2.303 47.006 1.00113.96 C ANISOU 1508 C TYR A1018 12472 15250 15576 569 -2149 1734 C ATOM 1509 O TYR A1018 46.224 -2.587 45.835 1.00121.07 O ANISOU 1509 O TYR A1018 13172 16106 16722 616 -1774 1767 O ATOM 1510 CB TYR A1018 44.232 -0.693 47.850 1.00 93.06 C ANISOU 1510 CB TYR A1018 10474 12514 12372 220 -2278 1421 C ATOM 1511 CG TYR A1018 43.253 -1.208 46.822 1.00 94.64 C ANISOU 1511 CG TYR A1018 10901 12566 12493 308 -1824 1465 C ATOM 1512 CD1 TYR A1018 43.069 -0.541 45.617 1.00 98.44 C ANISOU 1512 CD1 TYR A1018 11346 12911 13146 160 -1544 1428 C ATOM 1513 CD2 TYR A1018 42.513 -2.358 47.053 1.00 92.36 C ANISOU 1513 CD2 TYR A1018 10884 12266 11944 505 -1704 1563 C ATOM 1514 CE1 TYR A1018 42.179 -1.007 44.669 1.00 97.08 C ANISOU 1514 CE1 TYR A1018 11389 12624 12873 230 -1183 1460 C ATOM 1515 CE2 TYR A1018 41.614 -2.831 46.111 1.00 95.41 C ANISOU 1515 CE2 TYR A1018 11463 12519 12271 556 -1325 1577 C ATOM 1516 CZ TYR A1018 41.450 -2.147 44.923 1.00 96.24 C ANISOU 1516 CZ TYR A1018 11515 12518 12534 430 -1079 1511 C ATOM 1517 OH TYR A1018 40.562 -2.611 43.980 1.00 94.30 O ANISOU 1517 OH TYR A1018 11469 12159 12201 471 -755 1517 O ATOM 1518 N LYS A1019 45.882 -3.212 47.972 1.00112.29 N ANISOU 1518 N LYS A1019 12428 15075 15161 787 -2416 1854 N ATOM 1519 CA LYS A1019 46.124 -4.629 47.736 1.00114.49 C ANISOU 1519 CA LYS A1019 12662 15272 15567 1129 -2330 2040 C ATOM 1520 C LYS A1019 44.796 -5.365 47.616 1.00112.47 C ANISOU 1520 C LYS A1019 12933 14846 14954 1191 -2067 2094 C ATOM 1521 O LYS A1019 43.893 -5.162 48.435 1.00114.99 O ANISOU 1521 O LYS A1019 13645 15200 14846 1061 -2176 2073 O ATOM 1522 CB LYS A1019 46.964 -5.233 48.863 1.00116.93 C ANISOU 1522 CB LYS A1019 12829 15675 15923 1330 -2866 2206 C ATOM 1523 N ASP A1020 44.677 -6.212 46.597 1.00112.39 N ANISOU 1523 N ASP A1020 12914 14672 15118 1369 -1707 2129 N ATOM 1524 CA ASP A1020 43.491 -7.038 46.453 1.00108.38 C ANISOU 1524 CA ASP A1020 12868 13981 14329 1415 -1485 2186 C ATOM 1525 C ASP A1020 43.556 -8.206 47.436 1.00111.34 C ANISOU 1525 C ASP A1020 13459 14255 14590 1619 -1796 2432 C ATOM 1526 O ASP A1020 44.475 -8.316 48.253 1.00111.64 O ANISOU 1526 O ASP A1020 13307 14376 14734 1741 -2219 2559 O ATOM 1527 CB ASP A1020 43.344 -7.520 45.010 1.00103.84 C ANISOU 1527 CB ASP A1020 12244 13254 13957 1507 -1026 2105 C ATOM 1528 CG ASP A1020 44.444 -8.477 44.594 1.00108.01 C ANISOU 1528 CG ASP A1020 12440 13694 14903 1844 -1010 2150 C ATOM 1529 OD1 ASP A1020 45.525 -8.453 45.217 1.00113.64 O ANISOU 1529 OD1 ASP A1020 12802 14515 15861 1981 -1346 2220 O ATOM 1530 OD2 ASP A1020 44.228 -9.253 43.639 1.00105.75 O1+ ANISOU 1530 OD2 ASP A1020 12227 13235 14718 1987 -677 2082 O1+ ATOM 1531 N THR A1021 42.571 -9.101 47.357 1.00111.86 N ANISOU 1531 N THR A1021 13936 14124 14441 1634 -1618 2524 N ATOM 1532 CA THR A1021 42.498 -10.201 48.311 1.00111.37 C ANISOU 1532 CA THR A1021 14180 13918 14216 1754 -1913 2816 C ATOM 1533 C THR A1021 43.592 -11.242 48.108 1.00113.87 C ANISOU 1533 C THR A1021 14272 14000 14994 2154 -2104 2966 C ATOM 1534 O THR A1021 43.713 -12.150 48.936 1.00122.97 O ANISOU 1534 O THR A1021 15669 14982 16073 2291 -2453 3261 O ATOM 1535 CB THR A1021 41.130 -10.879 48.236 1.00106.11 C ANISOU 1535 CB THR A1021 14000 13085 13230 1600 -1650 2877 C ATOM 1536 OG1 THR A1021 40.997 -11.555 46.980 1.00101.52 O ANISOU 1536 OG1 THR A1021 13390 12234 12949 1746 -1308 2783 O ATOM 1537 CG2 THR A1021 40.020 -9.844 48.372 1.00105.59 C ANISOU 1537 CG2 THR A1021 14074 13265 12778 1259 -1443 2671 C ATOM 1538 N GLU A1022 44.388 -11.136 47.045 1.00109.65 N ANISOU 1538 N GLU A1022 13282 13452 14927 2346 -1889 2772 N ATOM 1539 CA GLU A1022 45.477 -12.070 46.790 1.00109.91 C ANISOU 1539 CA GLU A1022 13002 13289 15472 2780 -2033 2824 C ATOM 1540 C GLU A1022 46.850 -11.447 47.014 1.00110.30 C ANISOU 1540 C GLU A1022 12423 13602 15882 2906 -2315 2766 C ATOM 1541 O GLU A1022 47.866 -12.107 46.769 1.00114.91 O ANISOU 1541 O GLU A1022 12609 14084 16969 3299 -2431 2752 O ATOM 1542 CB GLU A1022 45.376 -12.625 45.367 1.00110.94 C ANISOU 1542 CB GLU A1022 13056 13217 15878 2939 -1526 2594 C ATOM 1543 N GLY A1023 46.907 -10.195 47.471 1.00108.89 N ANISOU 1543 N GLY A1023 12123 13753 15498 2586 -2436 2704 N ATOM 1544 CA GLY A1023 48.156 -9.536 47.793 1.00110.44 C ANISOU 1544 CA GLY A1023 11736 14212 16013 2619 -2755 2653 C ATOM 1545 C GLY A1023 48.709 -8.632 46.710 1.00113.05 C ANISOU 1545 C GLY A1023 11548 14751 16654 2465 -2360 2382 C ATOM 1546 O GLY A1023 49.639 -7.862 46.986 1.00112.39 O ANISOU 1546 O GLY A1023 10982 14921 16798 2361 -2597 2323 O ATOM 1547 N TYR A1024 48.174 -8.700 45.495 1.00108.30 N ANISOU 1547 N TYR A1024 11043 14058 16046 2411 -1784 2230 N ATOM 1548 CA TYR A1024 48.663 -7.880 44.398 1.00113.34 C ANISOU 1548 CA TYR A1024 11259 14900 16907 2217 -1372 2019 C ATOM 1549 C TYR A1024 48.186 -6.439 44.545 1.00111.52 C ANISOU 1549 C TYR A1024 11170 14816 16386 1738 -1381 1979 C ATOM 1550 O TYR A1024 47.084 -6.173 45.033 1.00110.91 O ANISOU 1550 O TYR A1024 11615 14645 15882 1574 -1459 2021 O ATOM 1551 CB TYR A1024 48.188 -8.447 43.060 1.00116.94 C ANISOU 1551 CB TYR A1024 11856 15216 17360 2297 -787 1879 C ATOM 1552 CG TYR A1024 48.578 -9.890 42.820 1.00122.30 C ANISOU 1552 CG TYR A1024 12446 15674 18349 2790 -744 1850 C ATOM 1553 CD1 TYR A1024 49.830 -10.364 43.189 1.00128.61 C ANISOU 1553 CD1 TYR A1024 12689 16530 19645 3150 -1024 1848 C ATOM 1554 CD2 TYR A1024 47.689 -10.779 42.227 1.00118.01 C ANISOU 1554 CD2 TYR A1024 12364 14836 17638 2906 -460 1804 C ATOM 1555 CE1 TYR A1024 50.188 -11.681 42.970 1.00131.77 C ANISOU 1555 CE1 TYR A1024 13011 16664 20391 3655 -1019 1793 C ATOM 1556 CE2 TYR A1024 48.037 -12.096 42.004 1.00120.38 C ANISOU 1556 CE2 TYR A1024 12621 14859 18257 3363 -444 1744 C ATOM 1557 CZ TYR A1024 49.287 -12.542 42.377 1.00129.11 C ANISOU 1557 CZ TYR A1024 13187 15991 19879 3758 -723 1736 C ATOM 1558 OH TYR A1024 49.639 -13.855 42.158 1.00133.04 O ANISOU 1558 OH TYR A1024 13642 16152 20756 4269 -742 1651 O ATOM 1559 N TYR A1025 49.029 -5.504 44.113 1.00117.71 N ANISOU 1559 N TYR A1025 11469 15821 17433 1507 -1294 1881 N ATOM 1560 CA TYR A1025 48.682 -4.087 44.152 1.00110.35 C ANISOU 1560 CA TYR A1025 10659 14955 16314 1049 -1319 1834 C ATOM 1561 C TYR A1025 47.758 -3.760 42.985 1.00104.43 C ANISOU 1561 C TYR A1025 10246 14092 15339 855 -821 1781 C ATOM 1562 O TYR A1025 48.115 -3.979 41.822 1.00101.17 O ANISOU 1562 O TYR A1025 9617 13740 15082 859 -384 1729 O ATOM 1563 CB TYR A1025 49.939 -3.221 44.101 1.00111.84 C ANISOU 1563 CB TYR A1025 10220 15385 16890 814 -1427 1782 C ATOM 1564 CG TYR A1025 50.892 -3.432 45.257 1.00115.51 C ANISOU 1564 CG TYR A1025 10303 15992 17595 978 -1998 1822 C ATOM 1565 CD1 TYR A1025 50.776 -2.688 46.423 1.00114.38 C ANISOU 1565 CD1 TYR A1025 10332 15875 17252 775 -2517 1825 C ATOM 1566 CD2 TYR A1025 51.915 -4.369 45.177 1.00120.42 C ANISOU 1566 CD2 TYR A1025 10384 16722 18646 1352 -2046 1830 C ATOM 1567 CE1 TYR A1025 51.647 -2.875 47.481 1.00116.89 C ANISOU 1567 CE1 TYR A1025 10328 16345 17742 906 -3095 1869 C ATOM 1568 CE2 TYR A1025 52.791 -4.563 46.228 1.00124.27 C ANISOU 1568 CE2 TYR A1025 10509 17338 19372 1522 -2643 1887 C ATOM 1569 CZ TYR A1025 52.653 -3.813 47.377 1.00124.31 C ANISOU 1569 CZ TYR A1025 10724 17386 19121 1279 -3180 1923 C ATOM 1570 OH TYR A1025 53.523 -4.004 48.428 1.00131.17 O ANISOU 1570 OH TYR A1025 11258 18402 20177 1430 -3829 1986 O ATOM 1571 N THR A1026 46.569 -3.247 43.288 1.00104.70 N ANISOU 1571 N THR A1026 10799 13985 14997 692 -893 1776 N ATOM 1572 CA THR A1026 45.596 -2.892 42.268 1.00105.81 C ANISOU 1572 CA THR A1026 11282 14002 14919 524 -528 1739 C ATOM 1573 C THR A1026 45.108 -1.467 42.499 1.00102.55 C ANISOU 1573 C THR A1026 11058 13525 14382 179 -701 1694 C ATOM 1574 O THR A1026 45.449 -0.819 43.493 1.00 98.86 O ANISOU 1574 O THR A1026 10500 13102 13962 75 -1083 1653 O ATOM 1575 CB THR A1026 44.400 -3.858 42.255 1.00102.47 C ANISOU 1575 CB THR A1026 11323 13413 14198 735 -413 1745 C ATOM 1576 OG1 THR A1026 43.497 -3.517 43.312 1.00 98.43 O ANISOU 1576 OG1 THR A1026 11152 12846 13400 677 -704 1728 O ATOM 1577 CG2 THR A1026 44.861 -5.301 42.437 1.00103.30 C ANISOU 1577 CG2 THR A1026 11315 13487 14447 1108 -410 1798 C ATOM 1578 N ILE A1027 44.296 -0.982 41.560 1.00 99.57 N ANISOU 1578 N ILE A1027 10963 13018 13850 15 -450 1686 N ATOM 1579 CA ILE A1027 43.734 0.361 41.638 1.00 94.27 C ANISOU 1579 CA ILE A1027 10513 12198 13107 -265 -621 1637 C ATOM 1580 C ILE A1027 42.483 0.419 40.770 1.00 89.78 C ANISOU 1580 C ILE A1027 10350 11463 12301 -276 -407 1635 C ATOM 1581 O ILE A1027 42.233 -0.483 39.962 1.00 86.52 O ANISOU 1581 O ILE A1027 10008 11080 11787 -145 -97 1677 O ATOM 1582 CB ILE A1027 44.771 1.417 41.213 1.00 89.65 C ANISOU 1582 CB ILE A1027 9615 11643 12803 -620 -639 1700 C ATOM 1583 CG1 ILE A1027 44.397 2.796 41.761 1.00 84.69 C ANISOU 1583 CG1 ILE A1027 9187 10803 12189 -869 -988 1614 C ATOM 1584 CG2 ILE A1027 44.914 1.453 39.698 1.00 80.58 C ANISOU 1584 CG2 ILE A1027 8450 10512 11654 -794 -204 1829 C ATOM 1585 CD1 ILE A1027 45.403 3.866 41.434 1.00 82.74 C ANISOU 1585 CD1 ILE A1027 8667 10528 12241 -1282 -1056 1694 C ATOM 1586 N GLY A1028 41.681 1.469 40.938 1.00 90.15 N ANISOU 1586 N GLY A1028 10659 11318 12274 -414 -605 1560 N ATOM 1587 CA GLY A1028 40.491 1.617 40.118 1.00 84.64 C ANISOU 1587 CA GLY A1028 10306 10458 11396 -412 -482 1559 C ATOM 1588 C GLY A1028 39.429 0.607 40.504 1.00 83.32 C ANISOU 1588 C GLY A1028 10333 10329 10994 -142 -422 1455 C ATOM 1589 O GLY A1028 39.140 0.390 41.685 1.00 81.04 O ANISOU 1589 O GLY A1028 10066 10102 10624 -17 -599 1333 O ATOM 1590 N ILE A1029 38.832 -0.021 39.494 1.00 90.61 N ANISOU 1590 N ILE A1029 11415 11232 11782 -90 -168 1506 N ATOM 1591 CA ILE A1029 37.857 -1.077 39.728 1.00 88.98 C ANISOU 1591 CA ILE A1029 11375 11052 11381 109 -82 1426 C ATOM 1592 C ILE A1029 38.467 -2.405 39.306 1.00 96.86 C ANISOU 1592 C ILE A1029 12278 12138 12386 239 180 1504 C ATOM 1593 O ILE A1029 38.305 -2.841 38.160 1.00 98.47 O ANISOU 1593 O ILE A1029 12577 12322 12515 224 426 1527 O ATOM 1594 CB ILE A1029 36.538 -0.812 38.980 1.00 75.33 C ANISOU 1594 CB ILE A1029 9908 9202 9511 82 -63 1368 C ATOM 1595 CG1 ILE A1029 35.978 0.560 39.350 1.00 71.56 C ANISOU 1595 CG1 ILE A1029 9501 8581 9108 11 -352 1261 C ATOM 1596 CG2 ILE A1029 35.522 -1.900 39.298 1.00 63.88 C ANISOU 1596 CG2 ILE A1029 8583 7799 7889 229 23 1272 C ATOM 1597 CD1 ILE A1029 34.589 0.806 38.813 1.00 68.30 C ANISOU 1597 CD1 ILE A1029 9287 8054 8610 55 -413 1168 C ATOM 1598 N GLY A1030 39.179 -3.050 40.226 1.00 99.15 N ANISOU 1598 N GLY A1030 12396 12511 12765 380 101 1529 N ATOM 1599 CA GLY A1030 39.787 -4.335 39.947 1.00 98.18 C ANISOU 1599 CA GLY A1030 12171 12410 12722 571 291 1577 C ATOM 1600 C GLY A1030 40.760 -4.288 38.789 1.00 94.57 C ANISOU 1600 C GLY A1030 11485 12025 12421 523 562 1598 C ATOM 1601 O GLY A1030 40.506 -4.869 37.728 1.00 95.69 O ANISOU 1601 O GLY A1030 11749 12138 12469 550 849 1553 O ATOM 1602 N HIS A1031 41.878 -3.592 38.977 1.00 87.03 N ANISOU 1602 N HIS A1031 10189 11192 11687 421 486 1644 N ATOM 1603 CA HIS A1031 42.893 -3.436 37.938 1.00 89.86 C ANISOU 1603 CA HIS A1031 10256 11692 12196 312 785 1660 C ATOM 1604 C HIS A1031 44.259 -3.687 38.565 1.00 92.16 C ANISOU 1604 C HIS A1031 10046 12138 12831 439 693 1664 C ATOM 1605 O HIS A1031 44.848 -2.781 39.162 1.00 95.75 O ANISOU 1605 O HIS A1031 10270 12666 13443 260 450 1711 O ATOM 1606 CB HIS A1031 42.821 -2.053 37.308 1.00 89.34 C ANISOU 1606 CB HIS A1031 10256 11621 12066 -69 797 1742 C ATOM 1607 CG HIS A1031 43.762 -1.865 36.161 1.00 92.70 C ANISOU 1607 CG HIS A1031 10434 12232 12556 -271 1167 1789 C ATOM 1608 ND1 HIS A1031 43.332 -1.784 34.855 1.00 93.45 N ANISOU 1608 ND1 HIS A1031 10789 12339 12379 -440 1471 1824 N ATOM 1609 CD2 HIS A1031 45.109 -1.748 36.123 1.00 96.67 C ANISOU 1609 CD2 HIS A1031 10434 12956 13341 -356 1297 1798 C ATOM 1610 CE1 HIS A1031 44.375 -1.621 34.061 1.00 97.80 C ANISOU 1610 CE1 HIS A1031 11037 13125 12996 -641 1814 1858 C ATOM 1611 NE2 HIS A1031 45.465 -1.597 34.805 1.00100.11 N ANISOU 1611 NE2 HIS A1031 10830 13554 13654 -592 1731 1833 N ATOM 1612 N LEU A1032 44.761 -4.912 38.422 1.00 91.24 N ANISOU 1612 N LEU A1032 9754 12051 12863 756 853 1596 N ATOM 1613 CA LEU A1032 46.058 -5.267 38.982 1.00 95.11 C ANISOU 1613 CA LEU A1032 9720 12682 13737 952 730 1587 C ATOM 1614 C LEU A1032 47.161 -4.499 38.265 1.00 99.71 C ANISOU 1614 C LEU A1032 9815 13531 14540 697 975 1562 C ATOM 1615 O LEU A1032 47.347 -4.649 37.054 1.00 96.96 O ANISOU 1615 O LEU A1032 9403 13297 14140 624 1442 1479 O ATOM 1616 CB LEU A1032 46.290 -6.772 38.868 1.00 93.50 C ANISOU 1616 CB LEU A1032 9457 12381 13686 1392 849 1495 C ATOM 1617 N LEU A1033 47.887 -3.667 39.013 1.00 97.35 N ANISOU 1617 N LEU A1033 9181 13349 14459 521 666 1628 N ATOM 1618 CA LEU A1033 49.025 -2.964 38.434 1.00104.31 C ANISOU 1618 CA LEU A1033 9528 14502 15604 230 883 1619 C ATOM 1619 C LEU A1033 50.158 -3.934 38.121 1.00112.65 C ANISOU 1619 C LEU A1033 9983 15786 17034 550 1131 1473 C ATOM 1620 O LEU A1033 50.737 -3.897 37.029 1.00115.99 O ANISOU 1620 O LEU A1033 10102 16446 17521 410 1635 1381 O ATOM 1621 CB LEU A1033 49.494 -1.861 39.381 1.00103.46 C ANISOU 1621 CB LEU A1033 9213 14430 15668 -55 434 1699 C ATOM 1622 N THR A1034 50.477 -4.818 39.064 1.00114.71 N ANISOU 1622 N THR A1034 10071 15980 17534 990 782 1443 N ATOM 1623 CA THR A1034 51.514 -5.822 38.866 1.00119.05 C ANISOU 1623 CA THR A1034 10043 16677 18514 1403 933 1278 C ATOM 1624 C THR A1034 51.333 -6.919 39.904 1.00116.13 C ANISOU 1624 C THR A1034 9831 16045 18250 1915 470 1326 C ATOM 1625 O THR A1034 50.615 -6.756 40.893 1.00112.94 O ANISOU 1625 O THR A1034 9869 15449 17593 1873 24 1499 O ATOM 1626 CB THR A1034 52.919 -5.218 38.968 1.00123.11 C ANISOU 1626 CB THR A1034 9729 17558 19489 1237 901 1232 C ATOM 1627 OG1 THR A1034 53.898 -6.241 38.746 1.00127.31 O ANISOU 1627 OG1 THR A1034 9644 18240 20490 1707 1059 1022 O ATOM 1628 CG2 THR A1034 53.135 -4.617 40.344 1.00124.58 C ANISOU 1628 CG2 THR A1034 9836 17714 19783 1140 210 1384 C ATOM 1629 N LYS A1035 51.998 -8.046 39.660 1.00124.24 N ANISOU 1629 N LYS A1035 10499 17061 19647 2398 588 1165 N ATOM 1630 CA LYS A1035 52.071 -9.132 40.624 1.00115.60 C ANISOU 1630 CA LYS A1035 9471 15694 18757 2910 100 1245 C ATOM 1631 C LYS A1035 53.350 -9.089 41.448 1.00124.45 C ANISOU 1631 C LYS A1035 9878 17011 20395 3112 -361 1270 C ATOM 1632 O LYS A1035 53.591 -10.004 42.241 1.00126.86 O ANISOU 1632 O LYS A1035 10167 17100 20932 3572 -826 1360 O ATOM 1633 CB LYS A1035 51.953 -10.483 39.911 1.00108.04 C ANISOU 1633 CB LYS A1035 8621 14489 17940 3381 417 1046 C ATOM 1634 N SER A1036 54.169 -8.044 41.282 1.00124.75 N ANISOU 1634 N SER A1036 9333 17441 20626 2756 -279 1212 N ATOM 1635 CA SER A1036 55.429 -7.892 41.994 1.00130.16 C ANISOU 1635 CA SER A1036 9248 18374 21834 2880 -717 1205 C ATOM 1636 C SER A1036 55.191 -7.369 43.411 1.00127.51 C ANISOU 1636 C SER A1036 9199 17961 21290 2719 -1470 1465 C ATOM 1637 O SER A1036 54.249 -6.611 43.652 1.00124.62 O ANISOU 1637 O SER A1036 9437 17497 20415 2316 -1507 1585 O ATOM 1638 CB SER A1036 56.351 -6.937 41.243 1.00133.68 C ANISOU 1638 CB SER A1036 8966 19280 22547 2465 -307 1043 C ATOM 1639 N PRO A1037 56.041 -7.758 44.369 1.00132.59 N ANISOU 1639 N PRO A1037 9408 18656 22314 3043 -2094 1531 N ATOM 1640 CA PRO A1037 55.818 -7.332 45.758 1.00131.46 C ANISOU 1640 CA PRO A1037 9590 18465 21895 2895 -2836 1763 C ATOM 1641 C PRO A1037 56.251 -5.907 46.050 1.00131.07 C ANISOU 1641 C PRO A1037 9233 18724 21845 2324 -3004 1723 C ATOM 1642 O PRO A1037 55.767 -5.327 47.031 1.00128.15 O ANISOU 1642 O PRO A1037 9314 18300 21079 2075 -3470 1849 O ATOM 1643 CB PRO A1037 56.658 -8.330 46.564 1.00137.89 C ANISOU 1643 CB PRO A1037 10022 19225 23144 3474 -3467 1855 C ATOM 1644 CG PRO A1037 57.788 -8.659 45.647 1.00141.32 C ANISOU 1644 CG PRO A1037 9525 19887 24282 3748 -3098 1581 C ATOM 1645 CD PRO A1037 57.205 -8.654 44.250 1.00138.32 C ANISOU 1645 CD PRO A1037 9352 19476 23728 3597 -2186 1384 C ATOM 1646 N SER A1038 57.142 -5.329 45.249 1.00134.97 N ANISOU 1646 N SER A1038 8987 19535 22758 2087 -2636 1539 N ATOM 1647 CA SER A1038 57.615 -3.977 45.512 1.00138.82 C ANISOU 1647 CA SER A1038 9165 20272 23307 1497 -2818 1510 C ATOM 1648 C SER A1038 56.508 -2.965 45.234 1.00142.03 C ANISOU 1648 C SER A1038 10304 20506 23157 966 -2548 1556 C ATOM 1649 O SER A1038 55.905 -2.966 44.156 1.00142.81 O ANISOU 1649 O SER A1038 10685 20515 23061 864 -1905 1526 O ATOM 1650 CB SER A1038 58.845 -3.669 44.659 1.00137.97 C ANISOU 1650 CB SER A1038 8060 20560 23801 1331 -2429 1322 C ATOM 1651 N LEU A1039 56.235 -2.105 46.219 1.00148.93 N ANISOU 1651 N LEU A1039 11491 21326 23772 647 -3071 1607 N ATOM 1652 CA LEU A1039 55.237 -1.059 46.027 1.00137.41 C ANISOU 1652 CA LEU A1039 10670 19674 21866 176 -2887 1609 C ATOM 1653 C LEU A1039 55.728 -0.005 45.042 1.00134.86 C ANISOU 1653 C LEU A1039 9968 19484 21790 -372 -2464 1547 C ATOM 1654 O LEU A1039 54.942 0.522 44.246 1.00128.51 O ANISOU 1654 O LEU A1039 9617 18504 20707 -648 -2029 1577 O ATOM 1655 CB LEU A1039 54.882 -0.422 47.371 1.00133.76 C ANISOU 1655 CB LEU A1039 10606 19126 21088 8 -3557 1606 C ATOM 1656 CG LEU A1039 53.969 0.807 47.351 1.00123.44 C ANISOU 1656 CG LEU A1039 9880 17606 19417 -461 -3487 1537 C ATOM 1657 CD1 LEU A1039 52.634 0.486 46.697 1.00115.73 C ANISOU 1657 CD1 LEU A1039 9575 16373 18024 -334 -3002 1586 C ATOM 1658 CD2 LEU A1039 53.766 1.349 48.759 1.00121.51 C ANISOU 1658 CD2 LEU A1039 9948 17332 18887 -575 -4163 1451 C ATOM 1659 N ASN A1040 57.027 0.309 45.078 1.00140.78 N ANISOU 1659 N ASN A1040 9881 20545 23065 -557 -2602 1481 N ATOM 1660 CA ASN A1040 57.584 1.273 44.135 1.00137.59 C ANISOU 1660 CA ASN A1040 9069 20297 22910 -1145 -2171 1458 C ATOM 1661 C ASN A1040 57.424 0.803 42.695 1.00142.78 C ANISOU 1661 C ASN A1040 9696 21027 23528 -1086 -1335 1468 C ATOM 1662 O ASN A1040 57.214 1.623 41.793 1.00129.49 O ANISOU 1662 O ASN A1040 8176 19309 21715 -1595 -895 1536 O ATOM 1663 CB ASN A1040 59.058 1.528 44.452 1.00137.97 C ANISOU 1663 CB ASN A1040 8117 20728 23578 -1326 -2453 1368 C ATOM 1664 N ALA A1041 57.513 -0.508 42.459 1.00141.43 N ANISOU 1664 N ALA A1041 9359 20933 23447 -478 -1132 1401 N ATOM 1665 CA ALA A1041 57.326 -1.032 41.111 1.00146.42 C ANISOU 1665 CA ALA A1041 10009 21635 23988 -388 -344 1347 C ATOM 1666 C ALA A1041 55.865 -0.980 40.683 1.00137.93 C ANISOU 1666 C ALA A1041 9919 20195 22294 -425 -117 1454 C ATOM 1667 O ALA A1041 55.576 -0.783 39.497 1.00137.36 O ANISOU 1667 O ALA A1041 10016 20159 22015 -671 490 1467 O ATOM 1668 CB ALA A1041 57.852 -2.465 41.023 1.00155.04 C ANISOU 1668 CB ALA A1041 10644 22857 25406 310 -239 1186 C ATOM 1669 N ALA A1042 54.935 -1.157 41.626 1.00140.82 N ANISOU 1669 N ALA A1042 10925 20238 22341 -200 -595 1527 N ATOM 1670 CA ALA A1042 53.519 -1.060 41.288 1.00132.90 C ANISOU 1670 CA ALA A1042 10790 18913 20795 -244 -420 1604 C ATOM 1671 C ALA A1042 53.142 0.352 40.863 1.00133.14 C ANISOU 1671 C ALA A1042 11109 18838 20640 -869 -326 1693 C ATOM 1672 O ALA A1042 52.205 0.531 40.075 1.00130.01 O ANISOU 1672 O ALA A1042 11253 18260 19885 -986 1 1755 O ATOM 1673 CB ALA A1042 52.662 -1.505 42.472 1.00126.18 C ANISOU 1673 CB ALA A1042 10481 17801 19659 81 -937 1646 C ATOM 1674 N LYS A1043 53.853 1.361 41.370 1.00137.98 N ANISOU 1674 N LYS A1043 11384 19531 21510 -1275 -652 1703 N ATOM 1675 CA LYS A1043 53.613 2.736 40.950 1.00131.35 C ANISOU 1675 CA LYS A1043 10799 18530 20579 -1894 -598 1802 C ATOM 1676 C LYS A1043 54.204 3.022 39.577 1.00133.43 C ANISOU 1676 C LYS A1043 10730 19015 20952 -2291 34 1891 C ATOM 1677 O LYS A1043 53.705 3.899 38.864 1.00133.13 O ANISOU 1677 O LYS A1043 11108 18782 20694 -2733 227 2044 O ATOM 1678 CB LYS A1043 54.192 3.713 41.976 1.00128.92 C ANISOU 1678 CB LYS A1043 10263 18193 20526 -2230 -1186 1758 C ATOM 1679 CG LYS A1043 53.569 3.618 43.359 1.00124.36 C ANISOU 1679 CG LYS A1043 10090 17422 19739 -1936 -1811 1654 C ATOM 1680 CD LYS A1043 54.054 4.744 44.258 1.00124.45 C ANISOU 1680 CD LYS A1043 9973 17371 19941 -2345 -2374 1565 C ATOM 1681 CE LYS A1043 53.301 4.761 45.577 1.00122.13 C ANISOU 1681 CE LYS A1043 10189 16897 19319 -2105 -2935 1426 C ATOM 1682 NZ LYS A1043 53.698 5.919 46.425 1.00124.65 N ANISOU 1682 NZ LYS A1043 10461 17121 19779 -2520 -3485 1275 N ATOM 1683 N SER A1044 55.263 2.305 39.194 1.00130.51 N ANISOU 1683 N SER A1044 9619 19057 20914 -2142 357 1795 N ATOM 1684 CA SER A1044 55.858 2.511 37.879 1.00137.15 C ANISOU 1684 CA SER A1044 10108 20197 21806 -2533 1041 1845 C ATOM 1685 C SER A1044 54.904 2.086 36.770 1.00136.57 C ANISOU 1685 C SER A1044 10643 20016 21232 -2427 1563 1899 C ATOM 1686 O SER A1044 54.789 2.771 35.747 1.00141.22 O ANISOU 1686 O SER A1044 11441 20628 21589 -2937 1967 2067 O ATOM 1687 CB SER A1044 57.179 1.749 37.775 1.00143.25 C ANISOU 1687 CB SER A1044 9888 21468 23072 -2311 1285 1648 C ATOM 1688 N GLU A1045 54.211 0.960 36.954 1.00136.81 N ANISOU 1688 N GLU A1045 10988 19917 21076 -1800 1534 1777 N ATOM 1689 CA GLU A1045 53.243 0.521 35.955 1.00129.18 C ANISOU 1689 CA GLU A1045 10619 18832 19631 -1695 1960 1797 C ATOM 1690 C GLU A1045 52.010 1.415 35.939 1.00128.34 C ANISOU 1690 C GLU A1045 11333 18313 19118 -1974 1718 2002 C ATOM 1691 O GLU A1045 51.383 1.582 34.887 1.00126.75 O ANISOU 1691 O GLU A1045 11575 18053 18531 -2171 2069 2109 O ATOM 1692 CB GLU A1045 52.847 -0.934 36.210 1.00121.20 C ANISOU 1692 CB GLU A1045 9714 17751 18586 -982 1950 1604 C ATOM 1693 N LEU A1046 51.650 1.998 37.088 1.00131.91 N ANISOU 1693 N LEU A1046 11988 18485 19645 -1980 1106 2037 N ATOM 1694 CA LEU A1046 50.490 2.885 37.146 1.00126.43 C ANISOU 1694 CA LEU A1046 12012 17383 18643 -2189 846 2169 C ATOM 1695 C LEU A1046 50.730 4.156 36.342 1.00134.52 C ANISOU 1695 C LEU A1046 13116 18345 19652 -2860 993 2395 C ATOM 1696 O LEU A1046 49.873 4.579 35.558 1.00138.35 O ANISOU 1696 O LEU A1046 14165 18604 19797 -3036 1114 2555 O ATOM 1697 CB LEU A1046 50.156 3.227 38.600 1.00114.87 C ANISOU 1697 CB LEU A1046 10689 15684 17273 -2043 195 2081 C ATOM 1698 CG LEU A1046 49.189 4.395 38.827 1.00103.62 C ANISOU 1698 CG LEU A1046 9857 13838 15674 -2297 -138 2146 C ATOM 1699 CD1 LEU A1046 47.828 4.107 38.217 1.00 96.31 C ANISOU 1699 CD1 LEU A1046 9556 12698 14341 -2097 22 2183 C ATOM 1700 CD2 LEU A1046 49.056 4.722 40.308 1.00 99.47 C ANISOU 1700 CD2 LEU A1046 9379 13170 15245 -2171 -734 1980 C ATOM 1701 N ASP A1047 51.893 4.784 36.529 1.00127.49 N ANISOU 1701 N ASP A1047 11667 17635 19137 -3262 951 2433 N ATOM 1702 CA ASP A1047 52.188 6.012 35.801 1.00131.96 C ANISOU 1702 CA ASP A1047 12311 18112 19714 -3978 1078 2692 C ATOM 1703 C ASP A1047 52.444 5.742 34.324 1.00130.92 C ANISOU 1703 C ASP A1047 12130 18291 19323 -4228 1792 2837 C ATOM 1704 O ASP A1047 52.172 6.607 33.483 1.00133.98 O ANISOU 1704 O ASP A1047 12921 18510 19475 -4745 1927 3128 O ATOM 1705 CB ASP A1047 53.382 6.723 36.435 1.00141.47 C ANISOU 1705 CB ASP A1047 12895 19442 21416 -4390 835 2678 C ATOM 1706 CG ASP A1047 53.050 7.320 37.791 1.00139.91 C ANISOU 1706 CG ASP A1047 12900 18874 21385 -4305 95 2555 C ATOM 1707 OD1 ASP A1047 51.910 7.125 38.263 1.00133.93 O ANISOU 1707 OD1 ASP A1047 12719 17809 20359 -3898 -178 2466 O ATOM 1708 OD2 ASP A1047 53.925 7.988 38.382 1.00142.42 O ANISOU 1708 OD2 ASP A1047 12791 19231 22093 -4666 -203 2522 O ATOM 1709 N LYS A1048 52.958 4.557 33.986 1.00136.15 N ANISOU 1709 N LYS A1048 12332 19393 20008 -3866 2239 2634 N ATOM 1710 CA LYS A1048 53.156 4.211 32.584 1.00137.23 C ANISOU 1710 CA LYS A1048 12447 19868 19828 -4059 2961 2691 C ATOM 1711 C LYS A1048 51.836 3.990 31.855 1.00136.24 C ANISOU 1711 C LYS A1048 13159 19483 19123 -3907 3045 2785 C ATOM 1712 O LYS A1048 51.813 4.012 30.619 1.00135.03 O ANISOU 1712 O LYS A1048 13198 19529 18579 -4209 3556 2913 O ATOM 1713 CB LYS A1048 54.036 2.964 32.467 1.00137.25 C ANISOU 1713 CB LYS A1048 11720 20374 20055 -3634 3395 2361 C ATOM 1714 N ALA A1049 50.743 3.782 32.587 1.00134.09 N ANISOU 1714 N ALA A1049 13374 18806 18767 -3471 2557 2719 N ATOM 1715 CA ALA A1049 49.423 3.607 31.993 1.00136.97 C ANISOU 1715 CA ALA A1049 14488 18911 18642 -3319 2551 2790 C ATOM 1716 C ALA A1049 48.555 4.853 32.093 1.00139.86 C ANISOU 1716 C ALA A1049 15461 18785 18895 -3629 2088 3059 C ATOM 1717 O ALA A1049 47.775 5.130 31.178 1.00144.34 O ANISOU 1717 O ALA A1049 16587 19202 19054 -3792 2166 3254 O ATOM 1718 CB ALA A1049 48.697 2.429 32.649 1.00134.83 C ANISOU 1718 CB ALA A1049 14339 18543 18349 -2619 2376 2514 C ATOM 1719 N ILE A1050 48.667 5.615 33.186 1.00147.00 N ANISOU 1719 N ILE A1050 16279 19419 20157 -3696 1573 3052 N ATOM 1720 CA ILE A1050 47.884 6.843 33.320 1.00137.76 C ANISOU 1720 CA ILE A1050 15661 17727 18955 -3954 1109 3250 C ATOM 1721 C ILE A1050 48.527 8.029 32.621 1.00135.31 C ANISOU 1721 C ILE A1050 15376 17334 18700 -4696 1193 3602 C ATOM 1722 O ILE A1050 47.861 9.054 32.425 1.00132.09 O ANISOU 1722 O ILE A1050 15513 16449 18227 -4950 855 3834 O ATOM 1723 CB ILE A1050 47.649 7.192 34.802 1.00112.75 C ANISOU 1723 CB ILE A1050 12459 14272 16111 -3710 512 3036 C ATOM 1724 N GLY A1051 49.800 7.923 32.236 1.00128.26 N ANISOU 1724 N GLY A1051 13902 16884 17947 -5058 1630 3652 N ATOM 1725 CA GLY A1051 50.479 8.964 31.501 1.00126.01 C ANISOU 1725 CA GLY A1051 13606 16592 17681 -5844 1802 4017 C ATOM 1726 C GLY A1051 51.114 10.046 32.350 1.00125.68 C ANISOU 1726 C GLY A1051 13328 16279 18144 -6255 1362 4067 C ATOM 1727 O GLY A1051 52.053 10.703 31.888 1.00131.62 O ANISOU 1727 O GLY A1051 13814 17166 19028 -6906 1590 4283 O ATOM 1728 N ARG A1052 50.638 10.250 33.572 1.00125.39 N ANISOU 1728 N ARG A1052 13398 15875 18368 -5892 754 3830 N ATOM 1729 CA ARG A1052 51.137 11.295 34.452 1.00130.48 C ANISOU 1729 CA ARG A1052 13895 16207 19473 -6249 261 3810 C ATOM 1730 C ARG A1052 51.879 10.681 35.633 1.00133.64 C ANISOU 1730 C ARG A1052 13610 16936 20230 -5922 98 3432 C ATOM 1731 O ARG A1052 51.880 9.465 35.836 1.00139.15 O ANISOU 1731 O ARG A1052 14025 18014 20831 -5363 306 3204 O ATOM 1732 CB ARG A1052 49.986 12.174 34.954 1.00127.22 C ANISOU 1732 CB ARG A1052 14202 15072 19066 -6123 -369 3798 C ATOM 1733 CG ARG A1052 49.063 11.466 35.933 1.00118.27 C ANISOU 1733 CG ARG A1052 13210 13879 17849 -5343 -664 3404 C ATOM 1734 CD ARG A1052 47.922 12.363 36.372 1.00115.96 C ANISOU 1734 CD ARG A1052 13565 12916 17579 -5212 -1224 3339 C ATOM 1735 NE ARG A1052 47.116 11.751 37.424 1.00114.03 N ANISOU 1735 NE ARG A1052 13390 12676 17262 -4541 -1477 2931 N ATOM 1736 CZ ARG A1052 47.303 11.960 38.723 1.00115.93 C ANISOU 1736 CZ ARG A1052 13460 12852 17737 -4403 -1881 2594 C ATOM 1737 NH1 ARG A1052 48.271 12.768 39.132 1.00119.81 N ANISOU 1737 NH1 ARG A1052 13686 13244 18594 -4875 -2117 2592 N ATOM 1738 NH2 ARG A1052 46.523 11.364 39.613 1.00113.10 N ANISOU 1738 NH2 ARG A1052 13205 12544 17222 -3834 -2048 2259 N ATOM 1739 N ASN A1053 52.517 11.551 36.419 1.00125.16 N ANISOU 1739 N ASN A1053 12297 15678 19580 -6291 -324 3375 N ATOM 1740 CA ASN A1053 53.118 11.156 37.692 1.00123.03 C ANISOU 1740 CA ASN A1053 11481 15629 19636 -6002 -663 3022 C ATOM 1741 C ASN A1053 52.002 11.117 38.731 1.00122.77 C ANISOU 1741 C ASN A1053 11968 15217 19462 -5447 -1194 2750 C ATOM 1742 O ASN A1053 51.786 12.056 39.502 1.00122.02 O ANISOU 1742 O ASN A1053 12131 14690 19541 -5602 -1734 2626 O ATOM 1743 CB ASN A1053 54.234 12.115 38.089 1.00126.67 C ANISOU 1743 CB ASN A1053 11485 16063 20583 -6663 -923 3047 C ATOM 1744 N THR A1054 51.272 9.995 38.739 1.00124.33 N ANISOU 1744 N THR A1054 12319 15587 19333 -4804 -1013 2632 N ATOM 1745 CA THR A1054 50.060 9.901 39.547 1.00119.55 C ANISOU 1745 CA THR A1054 12244 14668 18513 -4306 -1394 2406 C ATOM 1746 C THR A1054 50.366 9.947 41.037 1.00119.71 C ANISOU 1746 C THR A1054 12048 14716 18720 -4133 -1918 2083 C ATOM 1747 O THR A1054 49.504 10.334 41.835 1.00120.96 O ANISOU 1747 O THR A1054 12645 14548 18764 -3922 -2315 1863 O ATOM 1748 CB THR A1054 49.295 8.620 39.212 1.00115.03 C ANISOU 1748 CB THR A1054 11827 14310 17568 -3728 -1059 2370 C ATOM 1749 N ASN A1055 51.577 9.556 41.433 1.00118.97 N ANISOU 1749 N ASN A1055 11271 15030 18901 -4213 -1934 2029 N ATOM 1750 CA ASN A1055 52.004 9.557 42.830 1.00116.22 C ANISOU 1750 CA ASN A1055 10681 14771 18707 -4084 -2473 1748 C ATOM 1751 C ASN A1055 51.115 8.687 43.711 1.00119.38 C ANISOU 1751 C ASN A1055 11395 15214 18750 -3437 -2650 1539 C ATOM 1752 O ASN A1055 51.131 8.822 44.935 1.00121.96 O ANISOU 1752 O ASN A1055 11754 15533 19052 -3324 -3143 1293 O ATOM 1753 CB ASN A1055 52.071 10.984 43.391 1.00109.11 C ANISOU 1753 CB ASN A1055 9992 13444 18023 -4552 -2980 1627 C ATOM 1754 N GLY A1056 50.340 7.783 43.111 1.00115.78 N ANISOU 1754 N GLY A1056 11183 14819 17987 -3045 -2253 1632 N ATOM 1755 CA GLY A1056 49.518 6.838 43.832 1.00115.99 C ANISOU 1755 CA GLY A1056 11480 14915 17677 -2485 -2341 1489 C ATOM 1756 C GLY A1056 48.027 7.076 43.671 1.00112.88 C ANISOU 1756 C GLY A1056 11762 14182 16944 -2317 -2293 1431 C ATOM 1757 O GLY A1056 47.247 6.120 43.742 1.00109.86 O ANISOU 1757 O GLY A1056 11592 13885 16264 -1902 -2132 1408 O ATOM 1758 N VAL A1057 47.618 8.323 43.454 1.00113.85 N ANISOU 1758 N VAL A1057 12208 13906 17145 -2632 -2448 1405 N ATOM 1759 CA VAL A1057 46.211 8.699 43.361 1.00103.36 C ANISOU 1759 CA VAL A1057 11467 12226 15579 -2456 -2483 1304 C ATOM 1760 C VAL A1057 45.881 9.003 41.907 1.00105.21 C ANISOU 1760 C VAL A1057 11904 12256 15814 -2653 -2149 1598 C ATOM 1761 O VAL A1057 46.708 9.560 41.176 1.00111.08 O ANISOU 1761 O VAL A1057 12459 12960 16785 -3103 -2041 1831 O ATOM 1762 CB VAL A1057 45.900 9.912 44.260 1.00 96.42 C ANISOU 1762 CB VAL A1057 10853 10979 14804 -2591 -2980 1005 C ATOM 1763 N ILE A1058 44.667 8.639 41.488 1.00104.59 N ANISOU 1763 N ILE A1058 12209 12071 15459 -2350 -1994 1597 N ATOM 1764 CA ILE A1058 44.203 8.889 40.131 1.00100.91 C ANISOU 1764 CA ILE A1058 12012 11414 14916 -2498 -1744 1872 C ATOM 1765 C ILE A1058 42.794 9.466 40.170 1.00 98.60 C ANISOU 1765 C ILE A1058 12224 10714 14524 -2295 -1978 1737 C ATOM 1766 O ILE A1058 42.091 9.405 41.182 1.00 92.24 O ANISOU 1766 O ILE A1058 11523 9875 13648 -1976 -2199 1403 O ATOM 1767 CB ILE A1058 44.229 7.619 39.253 1.00 94.08 C ANISOU 1767 CB ILE A1058 11024 10914 13808 -2321 -1243 2041 C ATOM 1768 CG1 ILE A1058 43.313 6.543 39.831 1.00 82.54 C ANISOU 1768 CG1 ILE A1058 9675 9599 12089 -1804 -1208 1830 C ATOM 1769 CG2 ILE A1058 45.650 7.101 39.083 1.00 91.55 C ANISOU 1769 CG2 ILE A1058 10149 10986 13649 -2498 -980 2147 C ATOM 1770 CD1 ILE A1058 43.175 5.325 38.950 1.00 80.94 C ANISOU 1770 CD1 ILE A1058 9440 9653 11661 -1618 -764 1951 C ATOM 1771 N THR A1059 42.391 10.038 39.038 1.00100.27 N ANISOU 1771 N THR A1059 12740 10636 14723 -2488 -1928 2000 N ATOM 1772 CA THR A1059 41.046 10.571 38.887 1.00100.12 C ANISOU 1772 CA THR A1059 13164 10218 14658 -2267 -2166 1907 C ATOM 1773 C THR A1059 40.043 9.431 38.714 1.00 93.93 C ANISOU 1773 C THR A1059 12445 9697 13549 -1832 -1928 1816 C ATOM 1774 O THR A1059 40.390 8.322 38.302 1.00 93.12 O ANISOU 1774 O THR A1059 12152 9988 13239 -1781 -1546 1935 O ATOM 1775 CB THR A1059 40.982 11.515 37.681 1.00103.74 C ANISOU 1775 CB THR A1059 13952 10269 15193 -2630 -2248 2286 C ATOM 1776 OG1 THR A1059 42.175 12.306 37.630 1.00105.14 O ANISOU 1776 OG1 THR A1059 13991 10320 15636 -3159 -2321 2476 O ATOM 1777 CG2 THR A1059 39.778 12.440 37.771 1.00108.32 C ANISOU 1777 CG2 THR A1059 14955 10292 15912 -2422 -2687 2144 C ATOM 1778 N LYS A1060 38.780 9.709 39.047 1.00 98.18 N ANISOU 1778 N LYS A1060 13229 10001 14072 -1515 -2161 1570 N ATOM 1779 CA LYS A1060 37.721 8.768 38.697 1.00 98.24 C ANISOU 1779 CA LYS A1060 13319 10201 13806 -1182 -1964 1522 C ATOM 1780 C LYS A1060 37.594 8.635 37.188 1.00 99.60 C ANISOU 1780 C LYS A1060 13688 10335 13819 -1346 -1790 1903 C ATOM 1781 O LYS A1060 37.139 7.599 36.688 1.00 95.67 O ANISOU 1781 O LYS A1060 13192 10106 13053 -1183 -1519 1935 O ATOM 1782 CB LYS A1060 36.389 9.207 39.307 1.00 93.38 C ANISOU 1782 CB LYS A1060 12863 9359 13257 -838 -2249 1162 C ATOM 1783 N ASP A1061 37.997 9.671 36.449 1.00103.09 N ANISOU 1783 N ASP A1061 14329 10441 14400 -1703 -1952 2200 N ATOM 1784 CA ASP A1061 38.006 9.603 34.993 1.00101.97 C ANISOU 1784 CA ASP A1061 14414 10301 14028 -1942 -1780 2607 C ATOM 1785 C ASP A1061 39.176 8.768 34.485 1.00100.34 C ANISOU 1785 C ASP A1061 13939 10555 13629 -2196 -1275 2797 C ATOM 1786 O ASP A1061 39.012 7.961 33.563 1.00 99.43 O ANISOU 1786 O ASP A1061 13894 10699 13185 -2180 -958 2926 O ATOM 1787 CB ASP A1061 38.055 11.015 34.413 1.00102.76 C ANISOU 1787 CB ASP A1061 14862 9863 14320 -2281 -2142 2907 C ATOM 1788 CG ASP A1061 37.962 11.029 32.903 1.00102.52 C ANISOU 1788 CG ASP A1061 15156 9822 13974 -2555 -2021 3367 C ATOM 1789 OD1 ASP A1061 36.881 10.700 32.371 1.00 98.49 O ANISOU 1789 OD1 ASP A1061 14872 9291 13258 -2289 -2114 3362 O ATOM 1790 OD2 ASP A1061 38.970 11.374 32.248 1.00105.90 O1+ ANISOU 1790 OD2 ASP A1061 15607 10290 14339 -3064 -1832 3728 O1+ ATOM 1791 N GLU A1062 40.362 8.948 35.075 1.00102.50 N ANISOU 1791 N GLU A1062 13880 10945 14119 -2420 -1205 2776 N ATOM 1792 CA GLU A1062 41.504 8.118 34.707 1.00 96.62 C ANISOU 1792 CA GLU A1062 12770 10671 13271 -2592 -725 2880 C ATOM 1793 C GLU A1062 41.237 6.651 35.014 1.00 88.82 C ANISOU 1793 C GLU A1062 11588 10061 12098 -2156 -455 2641 C ATOM 1794 O GLU A1062 41.657 5.764 34.262 1.00 83.40 O ANISOU 1794 O GLU A1062 10776 9705 11208 -2174 -28 2718 O ATOM 1795 CB GLU A1062 42.761 8.595 35.435 1.00 87.02 C ANISOU 1795 CB GLU A1062 11163 9509 12392 -2870 -785 2852 C ATOM 1796 CG GLU A1062 43.240 9.972 35.025 1.00 95.42 C ANISOU 1796 CG GLU A1062 12385 10212 13658 -3416 -988 3136 C ATOM 1797 CD GLU A1062 44.494 10.395 35.768 1.00 99.73 C ANISOU 1797 CD GLU A1062 12491 10838 14563 -3723 -1061 3077 C ATOM 1798 OE1 GLU A1062 44.628 10.042 36.959 1.00 95.17 O ANISOU 1798 OE1 GLU A1062 11645 10382 14135 -3431 -1231 2743 O ATOM 1799 OE2 GLU A1062 45.347 11.075 35.159 1.00104.48 O1+ ANISOU 1799 OE2 GLU A1062 13018 11399 15279 -4288 -958 3375 O1+ ATOM 1800 N ALA A1063 40.542 6.377 36.121 1.00 85.45 N ANISOU 1800 N ALA A1063 11151 9581 11735 -1777 -689 2337 N ATOM 1801 CA ALA A1063 40.186 5.003 36.456 1.00 86.64 C ANISOU 1801 CA ALA A1063 11186 10021 11712 -1400 -477 2151 C ATOM 1802 C ALA A1063 39.112 4.459 35.526 1.00 88.99 C ANISOU 1802 C ALA A1063 11790 10309 11715 -1259 -345 2190 C ATOM 1803 O ALA A1063 39.030 3.242 35.325 1.00 88.77 O ANISOU 1803 O ALA A1063 11692 10524 11512 -1068 -60 2120 O ATOM 1804 CB ALA A1063 39.719 4.914 37.909 1.00 84.46 C ANISOU 1804 CB ALA A1063 10850 9716 11524 -1112 -751 1850 C ATOM 1805 N GLU A1064 38.283 5.337 34.957 1.00 91.39 N ANISOU 1805 N GLU A1064 12438 10307 11980 -1346 -590 2294 N ATOM 1806 CA GLU A1064 37.273 4.882 34.009 1.00 91.30 C ANISOU 1806 CA GLU A1064 12709 10296 11686 -1243 -529 2345 C ATOM 1807 C GLU A1064 37.898 4.478 32.678 1.00 95.38 C ANISOU 1807 C GLU A1064 13297 11022 11922 -1504 -156 2596 C ATOM 1808 O GLU A1064 37.402 3.560 32.016 1.00 93.85 O ANISOU 1808 O GLU A1064 13219 10996 11445 -1384 47 2550 O ATOM 1809 CB GLU A1064 36.216 5.969 33.805 1.00 88.36 C ANISOU 1809 CB GLU A1064 12660 9522 11391 -1222 -972 2387 C ATOM 1810 CG GLU A1064 34.995 5.506 33.022 1.00 85.95 C ANISOU 1810 CG GLU A1064 12598 9220 10839 -1054 -1023 2379 C ATOM 1811 CD GLU A1064 33.877 6.532 33.012 1.00 92.64 C ANISOU 1811 CD GLU A1064 13676 9668 11857 -926 -1527 2353 C ATOM 1812 OE1 GLU A1064 32.798 6.224 32.460 1.00 92.14 O ANISOU 1812 OE1 GLU A1064 13758 9602 11649 -763 -1648 2318 O ATOM 1813 OE2 GLU A1064 34.072 7.641 33.555 1.00 96.90 O ANISOU 1813 OE2 GLU A1064 14234 9879 12704 -975 -1826 2343 O ATOM 1814 N LYS A1065 38.982 5.144 32.270 1.00 96.04 N ANISOU 1814 N LYS A1065 13309 11119 12064 -1890 -43 2837 N ATOM 1815 CA LYS A1065 39.706 4.695 31.086 1.00 95.76 C ANISOU 1815 CA LYS A1065 13269 11382 11732 -2158 412 3024 C ATOM 1816 C LYS A1065 40.338 3.328 31.321 1.00 92.50 C ANISOU 1816 C LYS A1065 12480 11360 11306 -1927 838 2784 C ATOM 1817 O LYS A1065 40.296 2.460 30.442 1.00 93.15 O ANISOU 1817 O LYS A1065 12640 11673 11077 -1892 1185 2745 O ATOM 1818 CB LYS A1065 40.767 5.724 30.695 1.00 97.00 C ANISOU 1818 CB LYS A1065 13372 11502 11982 -2673 474 3332 C ATOM 1819 N LEU A1066 40.918 3.114 32.505 1.00 86.38 N ANISOU 1819 N LEU A1066 11317 10638 10865 -1755 781 2609 N ATOM 1820 CA LEU A1066 41.504 1.814 32.815 1.00 89.95 C ANISOU 1820 CA LEU A1066 11422 11389 11367 -1482 1095 2400 C ATOM 1821 C LEU A1066 40.439 0.729 32.871 1.00 88.33 C ANISOU 1821 C LEU A1066 11426 11159 10977 -1113 1097 2208 C ATOM 1822 O LEU A1066 40.672 -0.401 32.428 1.00 91.55 O ANISOU 1822 O LEU A1066 11755 11759 11269 -957 1433 2085 O ATOM 1823 CB LEU A1066 42.265 1.875 34.139 1.00 96.43 C ANISOU 1823 CB LEU A1066 11833 12240 12567 -1373 917 2292 C ATOM 1824 CG LEU A1066 43.442 2.845 34.220 1.00110.23 C ANISOU 1824 CG LEU A1066 13274 14038 14572 -1754 899 2439 C ATOM 1825 CD1 LEU A1066 44.173 2.679 35.543 1.00109.37 C ANISOU 1825 CD1 LEU A1066 12741 14009 14807 -1592 693 2287 C ATOM 1826 CD2 LEU A1066 44.392 2.653 33.043 1.00117.21 C ANISOU 1826 CD2 LEU A1066 13951 15231 15353 -2035 1407 2560 C ATOM 1827 N PHE A1067 39.266 1.055 33.417 1.00 88.20 N ANISOU 1827 N PHE A1067 11656 10901 10956 -977 731 2152 N ATOM 1828 CA PHE A1067 38.202 0.064 33.527 1.00 86.10 C ANISOU 1828 CA PHE A1067 11554 10620 10539 -687 725 1975 C ATOM 1829 C PHE A1067 37.743 -0.409 32.155 1.00 85.87 C ANISOU 1829 C PHE A1067 11803 10657 10168 -762 941 2008 C ATOM 1830 O PHE A1067 37.513 -1.606 31.949 1.00 84.89 O ANISOU 1830 O PHE A1067 11703 10627 9925 -580 1146 1847 O ATOM 1831 CB PHE A1067 37.028 0.640 34.316 1.00 89.23 C ANISOU 1831 CB PHE A1067 12101 10796 11006 -569 323 1888 C ATOM 1832 CG PHE A1067 35.849 -0.282 34.400 1.00 87.05 C ANISOU 1832 CG PHE A1067 11964 10525 10586 -347 317 1719 C ATOM 1833 CD1 PHE A1067 35.865 -1.372 35.252 1.00 83.17 C ANISOU 1833 CD1 PHE A1067 11332 10130 10137 -136 418 1574 C ATOM 1834 CD2 PHE A1067 34.724 -0.058 33.627 1.00 86.11 C ANISOU 1834 CD2 PHE A1067 12115 10304 10299 -373 179 1726 C ATOM 1835 CE1 PHE A1067 34.781 -2.221 35.329 1.00 78.20 C ANISOU 1835 CE1 PHE A1067 10832 9493 9387 -3 424 1440 C ATOM 1836 CE2 PHE A1067 33.638 -0.903 33.702 1.00 81.95 C ANISOU 1836 CE2 PHE A1067 11664 9800 9671 -214 168 1558 C ATOM 1837 CZ PHE A1067 33.666 -1.985 34.553 1.00 78.15 C ANISOU 1837 CZ PHE A1067 11043 9414 9235 -52 312 1415 C ATOM 1838 N ASN A1068 37.604 0.516 31.201 1.00 90.24 N ANISOU 1838 N ASN A1068 12604 11140 10543 -1046 869 2222 N ATOM 1839 CA ASN A1068 37.203 0.127 29.853 1.00 83.46 C ANISOU 1839 CA ASN A1068 12053 10378 9278 -1159 1045 2269 C ATOM 1840 C ASN A1068 38.222 -0.816 29.228 1.00 82.78 C ANISOU 1840 C ASN A1068 11803 10602 9046 -1191 1575 2173 C ATOM 1841 O ASN A1068 37.856 -1.728 28.479 1.00 84.94 O ANISOU 1841 O ASN A1068 12255 10985 9033 -1118 1777 2024 O ATOM 1842 CB ASN A1068 37.008 1.367 28.984 1.00 87.76 C ANISOU 1842 CB ASN A1068 12920 10786 9638 -1498 837 2587 C ATOM 1843 CG ASN A1068 35.631 1.982 29.145 1.00 95.27 C ANISOU 1843 CG ASN A1068 14135 11430 10632 -1379 315 2609 C ATOM 1844 OD1 ASN A1068 34.845 2.027 28.198 1.00102.99 O ANISOU 1844 OD1 ASN A1068 15454 12372 11305 -1446 169 2702 O ATOM 1845 ND2 ASN A1068 35.327 2.448 30.350 1.00 94.72 N ANISOU 1845 ND2 ASN A1068 13890 11159 10939 -1190 20 2495 N ATOM 1846 N GLN A1069 39.507 -0.618 29.532 1.00 82.90 N ANISOU 1846 N GLN A1069 11450 10766 9281 -1289 1799 2217 N ATOM 1847 CA GLN A1069 40.533 -1.532 29.041 1.00 93.96 C ANISOU 1847 CA GLN A1069 12588 12479 10633 -1250 2317 2059 C ATOM 1848 C GLN A1069 40.355 -2.926 29.631 1.00 96.67 C ANISOU 1848 C GLN A1069 12801 12800 11129 -811 2383 1749 C ATOM 1849 O GLN A1069 40.472 -3.931 28.918 1.00 96.30 O ANISOU 1849 O GLN A1069 12800 12887 10901 -697 2721 1539 O ATOM 1850 CB GLN A1069 41.922 -0.978 29.364 1.00104.31 C ANISOU 1850 CB GLN A1069 13439 13961 12234 -1436 2488 2158 C ATOM 1851 CG GLN A1069 42.191 0.399 28.770 1.00112.15 C ANISOU 1851 CG GLN A1069 14573 14942 13096 -1947 2442 2503 C ATOM 1852 CD GLN A1069 43.505 1.002 29.237 1.00116.78 C ANISOU 1852 CD GLN A1069 14664 15667 14039 -2175 2548 2595 C ATOM 1853 OE1 GLN A1069 44.350 0.314 29.812 1.00124.86 O ANISOU 1853 OE1 GLN A1069 15191 16882 15370 -1946 2730 2385 O ATOM 1854 NE2 GLN A1069 43.681 2.297 28.993 1.00109.98 N ANISOU 1854 NE2 GLN A1069 13937 14684 13167 -2636 2395 2919 N ATOM 1855 N ASP A1070 40.068 -3.007 30.934 1.00 93.20 N ANISOU 1855 N ASP A1070 12231 12176 11004 -577 2056 1715 N ATOM 1856 CA ASP A1070 39.831 -4.304 31.560 1.00 92.78 C ANISOU 1856 CA ASP A1070 12121 12049 11083 -206 2064 1494 C ATOM 1857 C ASP A1070 38.580 -4.968 31.000 1.00 84.10 C ANISOU 1857 C ASP A1070 11427 10832 9697 -148 2030 1376 C ATOM 1858 O ASP A1070 38.532 -6.195 30.858 1.00 74.28 O ANISOU 1858 O ASP A1070 10218 9558 8448 64 2204 1167 O ATOM 1859 CB ASP A1070 39.714 -4.145 33.076 1.00 97.16 C ANISOU 1859 CB ASP A1070 12517 12464 11936 -46 1705 1529 C ATOM 1860 CG ASP A1070 40.993 -3.637 33.711 1.00101.50 C ANISOU 1860 CG ASP A1070 12635 13134 12794 -83 1688 1606 C ATOM 1861 OD1 ASP A1070 42.082 -3.940 33.181 1.00105.37 O ANISOU 1861 OD1 ASP A1070 12832 13826 13379 -89 2015 1558 O ATOM 1862 OD2 ASP A1070 40.905 -2.936 34.743 1.00 98.07 O1+ ANISOU 1862 OD2 ASP A1070 12136 12614 12514 -110 1349 1680 O1+ ATOM 1863 N VAL A1071 37.557 -4.174 30.679 1.00 85.78 N ANISOU 1863 N VAL A1071 11939 10950 9704 -328 1771 1495 N ATOM 1864 CA VAL A1071 36.322 -4.733 30.136 1.00 82.23 C ANISOU 1864 CA VAL A1071 11829 10413 9002 -301 1681 1379 C ATOM 1865 C VAL A1071 36.565 -5.310 28.749 1.00 86.97 C ANISOU 1865 C VAL A1071 12623 11169 9251 -401 2023 1266 C ATOM 1866 O VAL A1071 36.169 -6.443 28.455 1.00 91.66 O ANISOU 1866 O VAL A1071 13352 11723 9752 -267 2137 1029 O ATOM 1867 CB VAL A1071 35.214 -3.667 30.113 1.00 77.64 C ANISOU 1867 CB VAL A1071 11459 9702 8338 -435 1276 1525 C ATOM 1868 CG1 VAL A1071 34.018 -4.169 29.323 1.00 68.20 C ANISOU 1868 CG1 VAL A1071 10579 8473 6862 -455 1173 1415 C ATOM 1869 CG2 VAL A1071 34.807 -3.308 31.524 1.00 79.71 C ANISOU 1869 CG2 VAL A1071 11544 9829 8913 -289 982 1517 C ATOM 1870 N ASP A1072 37.208 -4.533 27.872 1.00 86.89 N ANISOU 1870 N ASP A1072 12656 11340 9019 -672 2197 1425 N ATOM 1871 CA ASP A1072 37.548 -5.045 26.549 1.00 93.69 C ANISOU 1871 CA ASP A1072 13699 12426 9474 -799 2587 1294 C ATOM 1872 C ASP A1072 38.419 -6.289 26.649 1.00 93.29 C ANISOU 1872 C ASP A1072 13380 12470 9598 -530 3002 969 C ATOM 1873 O ASP A1072 38.186 -7.273 25.940 1.00100.45 O ANISOU 1873 O ASP A1072 14485 13404 10277 -445 3208 683 O ATOM 1874 CB ASP A1072 38.246 -3.964 25.724 1.00101.72 C ANISOU 1874 CB ASP A1072 14764 13660 10224 -1186 2755 1563 C ATOM 1875 CG ASP A1072 37.274 -2.951 25.152 1.00105.64 C ANISOU 1875 CG ASP A1072 15691 14039 10407 -1457 2355 1858 C ATOM 1876 OD1 ASP A1072 36.104 -3.321 24.911 1.00105.43 O1+ ANISOU 1876 OD1 ASP A1072 15959 13888 10212 -1367 2080 1761 O1+ ATOM 1877 OD2 ASP A1072 37.677 -1.787 24.942 1.00108.66 O ANISOU 1877 OD2 ASP A1072 16112 14434 10740 -1764 2286 2192 O ATOM 1878 N ALA A1073 39.417 -6.269 27.537 1.00 84.98 N ANISOU 1878 N ALA A1073 11874 11440 8973 -376 3089 988 N ATOM 1879 CA ALA A1073 40.250 -7.451 27.738 1.00 87.42 C ANISOU 1879 CA ALA A1073 11887 11783 9546 -46 3401 685 C ATOM 1880 C ALA A1073 39.418 -8.640 28.199 1.00 88.42 C ANISOU 1880 C ALA A1073 12207 11603 9787 254 3220 480 C ATOM 1881 O ALA A1073 39.645 -9.774 27.760 1.00 91.45 O ANISOU 1881 O ALA A1073 12623 11947 10175 465 3482 159 O ATOM 1882 CB ALA A1073 41.357 -7.149 28.747 1.00 88.38 C ANISOU 1882 CB ALA A1073 11477 11958 10146 77 3385 785 C ATOM 1883 N ALA A1074 38.441 -8.397 29.079 1.00 83.01 N ANISOU 1883 N ALA A1074 11651 10689 9199 259 2785 645 N ATOM 1884 CA ALA A1074 37.590 -9.476 29.567 1.00 85.44 C ANISOU 1884 CA ALA A1074 12143 10714 9605 456 2615 500 C ATOM 1885 C ALA A1074 36.749 -10.084 28.454 1.00 93.89 C ANISOU 1885 C ALA A1074 13614 11749 10313 356 2695 279 C ATOM 1886 O ALA A1074 36.388 -11.263 28.528 1.00 97.64 O ANISOU 1886 O ALA A1074 14228 11998 10874 520 2705 57 O ATOM 1887 CB ALA A1074 36.686 -8.968 30.689 1.00 78.28 C ANISOU 1887 CB ALA A1074 11263 9662 8819 417 2191 709 C ATOM 1888 N VAL A1075 36.430 -9.305 27.419 1.00 95.22 N ANISOU 1888 N VAL A1075 13998 12114 10069 70 2718 348 N ATOM 1889 CA VAL A1075 35.614 -9.821 26.325 1.00 92.66 C ANISOU 1889 CA VAL A1075 14075 11790 9341 -54 2737 139 C ATOM 1890 C VAL A1075 36.457 -10.646 25.357 1.00100.97 C ANISOU 1890 C VAL A1075 15170 12983 10213 22 3217 -207 C ATOM 1891 O VAL A1075 35.987 -11.658 24.824 1.00101.40 O ANISOU 1891 O VAL A1075 15489 12912 10125 79 3272 -531 O ATOM 1892 CB VAL A1075 34.888 -8.661 25.617 1.00 82.73 C ANISOU 1892 CB VAL A1075 13071 10672 7689 -380 2491 377 C ATOM 1893 CG1 VAL A1075 34.069 -9.171 24.446 1.00 75.94 C ANISOU 1893 CG1 VAL A1075 12635 9852 6368 -528 2457 166 C ATOM 1894 CG2 VAL A1075 33.993 -7.930 26.604 1.00 76.88 C ANISOU 1894 CG2 VAL A1075 12256 9765 7192 -384 2023 620 C ATOM 1895 N ARG A1076 37.712 -10.240 25.115 1.00100.09 N ANISOU 1895 N ARG A1076 14776 13139 10116 17 3583 -182 N ATOM 1896 CA ARG A1076 38.592 -11.049 24.273 1.00106.02 C ANISOU 1896 CA ARG A1076 15475 14062 10744 139 4103 -579 C ATOM 1897 C ARG A1076 38.740 -12.458 24.828 1.00110.21 C ANISOU 1897 C ARG A1076 15911 14258 11706 564 4141 -922 C ATOM 1898 O ARG A1076 38.867 -13.421 24.062 1.00118.72 O ANISOU 1898 O ARG A1076 17153 15310 12647 690 4425 -1359 O ATOM 1899 CB ARG A1076 39.980 -10.411 24.143 1.00109.75 C ANISOU 1899 CB ARG A1076 15519 14893 11289 84 4503 -500 C ATOM 1900 CG ARG A1076 40.027 -8.904 24.227 1.00109.02 C ANISOU 1900 CG ARG A1076 15378 14979 11066 -286 4338 -22 C ATOM 1901 CD ARG A1076 39.706 -8.229 22.910 1.00113.54 C ANISOU 1901 CD ARG A1076 16360 15831 10947 -724 4457 91 C ATOM 1902 NE ARG A1076 39.657 -6.778 23.063 1.00113.48 N ANISOU 1902 NE ARG A1076 16365 15872 10879 -1069 4203 591 N ATOM 1903 CZ ARG A1076 39.507 -5.923 22.058 1.00114.12 C ANISOU 1903 CZ ARG A1076 16787 16166 10409 -1503 4233 842 C ATOM 1904 NH1 ARG A1076 39.395 -6.367 20.812 1.00118.70 N1+ ANISOU 1904 NH1 ARG A1076 17722 16997 10383 -1663 4528 629 N1+ ATOM 1905 NH2 ARG A1076 39.471 -4.619 22.301 1.00110.17 N ANISOU 1905 NH2 ARG A1076 16305 15605 9949 -1786 3945 1307 N ATOM 1906 N GLY A1077 38.727 -12.597 26.152 1.00104.33 N ANISOU 1906 N GLY A1077 14938 13235 11468 780 3843 -732 N ATOM 1907 CA GLY A1077 38.862 -13.893 26.781 1.00103.24 C ANISOU 1907 CA GLY A1077 14749 12715 11761 1164 3801 -960 C ATOM 1908 C GLY A1077 37.555 -14.652 26.832 1.00100.52 C ANISOU 1908 C GLY A1077 14844 12012 11338 1106 3509 -1046 C ATOM 1909 O GLY A1077 37.538 -15.875 26.663 1.00104.59 O ANISOU 1909 O GLY A1077 15516 12220 12003 1321 3586 -1382 O ATOM 1910 N ILE A1078 36.453 -13.936 27.070 1.00 99.32 N ANISOU 1910 N ILE A1078 14869 11880 10988 814 3165 -762 N ATOM 1911 CA ILE A1078 35.138 -14.573 27.087 1.00 95.36 C ANISOU 1911 CA ILE A1078 14721 11103 10410 692 2887 -841 C ATOM 1912 C ILE A1078 34.872 -15.266 25.758 1.00 94.23 C ANISOU 1912 C ILE A1078 14931 10962 9909 611 3076 -1259 C ATOM 1913 O ILE A1078 34.461 -16.432 25.713 1.00 91.07 O ANISOU 1913 O ILE A1078 14757 10213 9633 693 3032 -1537 O ATOM 1914 CB ILE A1078 34.042 -13.542 27.412 1.00 93.90 C ANISOU 1914 CB ILE A1078 14585 11030 10063 404 2522 -518 C ATOM 1915 CG1 ILE A1078 33.993 -13.263 28.917 1.00 93.60 C ANISOU 1915 CG1 ILE A1078 14291 10873 10400 497 2289 -213 C ATOM 1916 CG2 ILE A1078 32.692 -14.024 26.911 1.00 91.88 C ANISOU 1916 CG2 ILE A1078 14674 10646 9590 192 2300 -673 C ATOM 1917 CD1 ILE A1078 33.002 -12.183 29.313 1.00 86.14 C ANISOU 1917 CD1 ILE A1078 13326 10053 9351 273 1966 41 C ATOM 1918 N LEU A1079 35.121 -14.560 24.654 1.00 96.21 N ANISOU 1918 N LEU A1079 15266 11598 9690 421 3283 -1311 N ATOM 1919 CA LEU A1079 34.910 -15.148 23.339 1.00 99.06 C ANISOU 1919 CA LEU A1079 15997 12035 9608 315 3475 -1730 C ATOM 1920 C LEU A1079 35.911 -16.261 23.058 1.00104.43 C ANISOU 1920 C LEU A1079 16609 12586 10483 653 3898 -2204 C ATOM 1921 O LEU A1079 35.576 -17.237 22.375 1.00107.18 O ANISOU 1921 O LEU A1079 17287 12752 10686 675 3966 -2650 O ATOM 1922 CB LEU A1079 34.990 -14.061 22.271 1.00 97.08 C ANISOU 1922 CB LEU A1079 15879 12261 8747 -2 3592 -1606 C ATOM 1923 CG LEU A1079 34.022 -12.896 22.494 1.00 92.62 C ANISOU 1923 CG LEU A1079 15381 11775 8035 -286 3126 -1146 C ATOM 1924 CD1 LEU A1079 34.208 -11.832 21.427 1.00 87.85 C ANISOU 1924 CD1 LEU A1079 14956 11583 6838 -599 3216 -967 C ATOM 1925 CD2 LEU A1079 32.586 -13.395 22.521 1.00 89.61 C ANISOU 1925 CD2 LEU A1079 15271 11148 7628 -399 2691 -1233 C ATOM 1926 N ARG A1080 37.134 -16.141 23.574 1.00102.78 N ANISOU 1926 N ARG A1080 15961 12455 10635 932 4161 -2150 N ATOM 1927 CA ARG A1080 38.113 -17.215 23.463 1.00106.42 C ANISOU 1927 CA ARG A1080 16265 12749 11422 1346 4516 -2607 C ATOM 1928 C ARG A1080 37.864 -18.345 24.454 1.00114.00 C ANISOU 1928 C ARG A1080 17260 13084 12971 1658 4225 -2653 C ATOM 1929 O ARG A1080 38.585 -19.348 24.417 1.00121.35 O ANISOU 1929 O ARG A1080 18104 13749 14255 2055 4430 -3041 O ATOM 1930 CB ARG A1080 39.528 -16.662 23.652 1.00 95.46 C ANISOU 1930 CB ARG A1080 14320 11699 10249 1534 4874 -2535 C ATOM 1931 N ASN A1081 36.877 -18.203 25.339 1.00113.30 N ANISOU 1931 N ASN A1081 17292 12754 13003 1487 3760 -2268 N ATOM 1932 CA ASN A1081 36.488 -19.263 26.264 1.00110.82 C ANISOU 1932 CA ASN A1081 17098 11850 13160 1666 3466 -2242 C ATOM 1933 C ASN A1081 35.348 -20.052 25.630 1.00107.85 C ANISOU 1933 C ASN A1081 17225 11189 12565 1437 3324 -2533 C ATOM 1934 O ASN A1081 34.255 -19.516 25.418 1.00 96.74 O ANISOU 1934 O ASN A1081 16004 9943 10809 1044 3098 -2372 O ATOM 1935 CB ASN A1081 36.075 -18.682 27.614 1.00104.89 C ANISOU 1935 CB ASN A1081 16179 11052 12621 1564 3094 -1681 C ATOM 1936 CG ASN A1081 35.935 -19.745 28.696 1.00100.82 C ANISOU 1936 CG ASN A1081 15751 9964 12593 1757 2830 -1573 C ATOM 1937 OD1 ASN A1081 35.536 -20.881 28.430 1.00 96.54 O ANISOU 1937 OD1 ASN A1081 15540 8975 12166 1793 2783 -1851 O ATOM 1938 ND2 ASN A1081 36.265 -19.375 29.927 1.00 99.41 N ANISOU 1938 ND2 ASN A1081 15308 9782 12683 1855 2634 -1158 N ATOM 1939 N ALA A1082 35.603 -21.330 25.335 1.00104.72 N ANISOU 1939 N ALA A1082 17030 10346 12412 1693 3425 -2982 N ATOM 1940 CA ALA A1082 34.620 -22.148 24.633 1.00104.56 C ANISOU 1940 CA ALA A1082 17500 10033 12195 1466 3305 -3342 C ATOM 1941 C ALA A1082 33.348 -22.360 25.442 1.00101.54 C ANISOU 1941 C ALA A1082 17302 9334 11945 1142 2845 -3001 C ATOM 1942 O ALA A1082 32.300 -22.654 24.856 1.00101.98 O ANISOU 1942 O ALA A1082 17693 9314 11739 801 2679 -3190 O ATOM 1943 CB ALA A1082 35.231 -23.499 24.264 1.00107.82 C ANISOU 1943 CB ALA A1082 18086 9944 12935 1850 3489 -3914 C ATOM 1944 N LYS A1083 33.409 -22.219 26.764 1.00105.02 N ANISOU 1944 N LYS A1083 17519 9623 12760 1215 2642 -2520 N ATOM 1945 CA LYS A1083 32.243 -22.435 27.607 1.00 99.72 C ANISOU 1945 CA LYS A1083 16986 8701 12202 885 2273 -2194 C ATOM 1946 C LYS A1083 31.446 -21.163 27.871 1.00 97.98 C ANISOU 1946 C LYS A1083 16574 8985 11668 541 2119 -1821 C ATOM 1947 O LYS A1083 30.317 -21.253 28.366 1.00 96.09 O ANISOU 1947 O LYS A1083 16414 8652 11442 209 1857 -1636 O ATOM 1948 CB LYS A1083 32.666 -23.061 28.941 1.00 98.15 C ANISOU 1948 CB LYS A1083 16717 8046 12528 1114 2120 -1873 C ATOM 1949 N LEU A1084 31.992 -19.986 27.551 1.00 99.46 N ANISOU 1949 N LEU A1084 16502 9689 11600 605 2275 -1719 N ATOM 1950 CA LEU A1084 31.288 -18.729 27.771 1.00 97.55 C ANISOU 1950 CA LEU A1084 16090 9867 11109 333 2100 -1390 C ATOM 1951 C LEU A1084 30.919 -17.993 26.491 1.00101.44 C ANISOU 1951 C LEU A1084 16699 10753 11090 121 2131 -1554 C ATOM 1952 O LEU A1084 30.009 -17.161 26.521 1.00102.09 O ANISOU 1952 O LEU A1084 16730 11072 10987 -136 1884 -1351 O ATOM 1953 CB LEU A1084 32.124 -17.790 28.654 1.00 93.67 C ANISOU 1953 CB LEU A1084 15216 9609 10766 522 2147 -1024 C ATOM 1954 CG LEU A1084 32.376 -18.250 30.092 1.00 99.39 C ANISOU 1954 CG LEU A1084 15814 10040 11911 678 2020 -744 C ATOM 1955 CD1 LEU A1084 33.068 -17.160 30.896 1.00100.96 C ANISOU 1955 CD1 LEU A1084 15645 10540 12174 797 2010 -411 C ATOM 1956 CD2 LEU A1084 31.075 -18.668 30.757 1.00 98.30 C ANISOU 1956 CD2 LEU A1084 15830 9700 11820 371 1756 -602 C ATOM 1957 N LYS A1085 31.598 -18.269 25.378 1.00102.45 N ANISOU 1957 N LYS A1085 16983 10965 10978 227 2417 -1917 N ATOM 1958 CA LYS A1085 31.262 -17.597 24.126 1.00 99.55 C ANISOU 1958 CA LYS A1085 16799 10990 10037 -13 2431 -2041 C ATOM 1959 C LYS A1085 29.850 -17.899 23.627 1.00 99.81 C ANISOU 1959 C LYS A1085 17128 10950 9847 -354 2083 -2182 C ATOM 1960 O LYS A1085 29.193 -16.966 23.138 1.00 92.79 O ANISOU 1960 O LYS A1085 16268 10388 8598 -594 1861 -2023 O ATOM 1961 CB LYS A1085 32.301 -17.947 23.053 1.00 96.22 C ANISOU 1961 CB LYS A1085 16501 10703 9355 149 2870 -2453 C ATOM 1962 N PRO A1086 29.335 -19.137 23.693 1.00105.32 N ANISOU 1962 N PRO A1086 18044 11220 10751 -402 1987 -2468 N ATOM 1963 CA PRO A1086 27.961 -19.366 23.201 1.00106.72 C ANISOU 1963 CA PRO A1086 18449 11373 10729 -778 1625 -2606 C ATOM 1964 C PRO A1086 26.904 -18.527 23.902 1.00101.72 C ANISOU 1964 C PRO A1086 17551 10915 10184 -1000 1260 -2201 C ATOM 1965 O PRO A1086 26.130 -17.830 23.232 1.00 97.88 O ANISOU 1965 O PRO A1086 17104 10733 9353 -1226 992 -2175 O ATOM 1966 CB PRO A1086 27.759 -20.868 23.445 1.00108.18 C ANISOU 1966 CB PRO A1086 18857 10979 11267 -780 1611 -2917 C ATOM 1967 CG PRO A1086 29.125 -21.438 23.364 1.00108.60 C ANISOU 1967 CG PRO A1086 18951 10834 11479 -369 2012 -3150 C ATOM 1968 CD PRO A1086 30.018 -20.411 23.991 1.00103.81 C ANISOU 1968 CD PRO A1086 17951 10542 10950 -127 2192 -2744 C ATOM 1969 N VAL A1087 26.844 -18.575 25.235 1.00 98.45 N ANISOU 1969 N VAL A1087 16867 10324 10214 -932 1231 -1899 N ATOM 1970 CA VAL A1087 25.825 -17.817 25.956 1.00 96.16 C ANISOU 1970 CA VAL A1087 16290 10223 10024 -1125 937 -1588 C ATOM 1971 C VAL A1087 26.024 -16.321 25.749 1.00 94.05 C ANISOU 1971 C VAL A1087 15830 10386 9517 -1049 881 -1337 C ATOM 1972 O VAL A1087 25.055 -15.564 25.617 1.00 93.16 O ANISOU 1972 O VAL A1087 15592 10501 9302 -1221 565 -1236 O ATOM 1973 CB VAL A1087 25.834 -18.196 27.449 1.00 97.74 C ANISOU 1973 CB VAL A1087 16281 10182 10673 -1078 978 -1328 C ATOM 1974 CG1 VAL A1087 27.238 -18.088 28.024 1.00102.40 C ANISOU 1974 CG1 VAL A1087 16780 10706 11420 -706 1259 -1166 C ATOM 1975 CG2 VAL A1087 24.863 -17.323 28.230 1.00 89.97 C ANISOU 1975 CG2 VAL A1087 14954 9465 9765 -1245 754 -1058 C ATOM 1976 N TYR A1088 27.284 -15.876 25.692 1.00 89.69 N ANISOU 1976 N TYR A1088 15242 9934 8902 -793 1168 -1242 N ATOM 1977 CA TYR A1088 27.580 -14.457 25.515 1.00 90.57 C ANISOU 1977 CA TYR A1088 15204 10393 8813 -755 1125 -975 C ATOM 1978 C TYR A1088 26.959 -13.916 24.234 1.00 95.61 C ANISOU 1978 C TYR A1088 16073 11277 8976 -968 892 -1053 C ATOM 1979 O TYR A1088 26.470 -12.781 24.202 1.00 93.98 O ANISOU 1979 O TYR A1088 15753 11275 8682 -1035 611 -805 O ATOM 1980 CB TYR A1088 29.095 -14.250 25.512 1.00 93.94 C ANISOU 1980 CB TYR A1088 15566 10885 9242 -509 1510 -919 C ATOM 1981 CG TYR A1088 29.544 -12.810 25.574 1.00 98.44 C ANISOU 1981 CG TYR A1088 15953 11742 9710 -493 1488 -591 C ATOM 1982 CD1 TYR A1088 29.740 -12.178 26.794 1.00 98.86 C ANISOU 1982 CD1 TYR A1088 15682 11781 10099 -378 1424 -304 C ATOM 1983 CD2 TYR A1088 29.792 -12.088 24.415 1.00103.73 C ANISOU 1983 CD2 TYR A1088 16808 12681 9923 -622 1523 -565 C ATOM 1984 CE1 TYR A1088 30.162 -10.863 26.860 1.00 99.84 C ANISOU 1984 CE1 TYR A1088 15661 12107 10167 -380 1378 -29 C ATOM 1985 CE2 TYR A1088 30.213 -10.771 24.470 1.00106.12 C ANISOU 1985 CE2 TYR A1088 16981 13181 10158 -650 1482 -232 C ATOM 1986 CZ TYR A1088 30.395 -10.164 25.696 1.00103.83 C ANISOU 1986 CZ TYR A1088 16357 12826 10268 -522 1402 20 C ATOM 1987 OH TYR A1088 30.810 -8.854 25.759 1.00103.35 O ANISOU 1987 OH TYR A1088 16189 12904 10176 -568 1333 326 O ATOM 1988 N ASP A1089 26.969 -14.714 23.164 1.00102.12 N ANISOU 1988 N ASP A1089 17248 12069 9485 -1067 973 -1406 N ATOM 1989 CA ASP A1089 26.320 -14.293 21.927 1.00102.51 C ANISOU 1989 CA ASP A1089 17573 12361 9018 -1301 696 -1486 C ATOM 1990 C ASP A1089 24.810 -14.185 22.110 1.00 97.68 C ANISOU 1990 C ASP A1089 16847 11734 8531 -1503 175 -1453 C ATOM 1991 O ASP A1089 24.193 -13.208 21.669 1.00 94.27 O ANISOU 1991 O ASP A1089 16405 11528 7886 -1603 -198 -1266 O ATOM 1992 CB ASP A1089 26.658 -15.270 20.798 1.00107.75 C ANISOU 1992 CB ASP A1089 18652 12996 9292 -1371 911 -1943 C ATOM 1993 CG ASP A1089 28.153 -15.360 20.522 1.00109.36 C ANISOU 1993 CG ASP A1089 18906 13282 9365 -1158 1468 -2039 C ATOM 1994 OD1 ASP A1089 28.859 -14.349 20.724 1.00107.83 O ANISOU 1994 OD1 ASP A1089 18522 13306 9142 -1077 1610 -1702 O ATOM 1995 OD2 ASP A1089 28.623 -16.442 20.104 1.00108.54 O1+ ANISOU 1995 OD2 ASP A1089 19006 13016 9217 -1074 1762 -2478 O1+ ATOM 1996 N SER A1090 24.200 -15.124 22.768 1.00 95.52 N ANISOU 1996 N SER A1090 16469 11190 8635 -1571 131 -1622 N ATOM 1997 CA SER A1090 22.775 -15.087 22.914 1.00100.79 C ANISOU 1997 CA SER A1090 16964 11869 9463 -1805 -311 -1652 C ATOM 1998 C SER A1090 22.220 -13.982 23.739 1.00102.57 C ANISOU 1998 C SER A1090 16755 12269 9949 -1733 -541 -1311 C ATOM 1999 O SER A1090 21.034 -13.763 23.747 1.00106.04 O ANISOU 1999 O SER A1090 16983 12810 10497 -1894 -938 -1340 O ATOM 2000 CB SER A1090 22.377 -16.406 23.588 1.00 99.01 C ANISOU 2000 CB SER A1090 16709 11296 9615 -1937 -227 -1860 C ATOM 2001 OG SER A1090 21.208 -16.357 24.395 1.00 95.53 O ANISOU 2001 OG SER A1090 15874 10901 9522 -2092 -478 -1730 O ATOM 2002 N LEU A1091 23.062 -13.325 24.481 1.00 99.87 N ANISOU 2002 N LEU A1091 16250 11965 9730 -1492 -315 -1031 N ATOM 2003 CA LEU A1091 22.607 -12.416 25.517 1.00 95.87 C ANISOU 2003 CA LEU A1091 15324 11551 9550 -1398 -463 -783 C ATOM 2004 C LEU A1091 22.327 -11.026 24.968 1.00 97.76 C ANISOU 2004 C LEU A1091 15525 12007 9612 -1342 -816 -587 C ATOM 2005 O LEU A1091 23.032 -10.535 24.083 1.00 95.64 O ANISOU 2005 O LEU A1091 15549 11818 8971 -1317 -786 -485 O ATOM 2006 CB LEU A1091 23.641 -12.333 26.638 1.00 87.84 C ANISOU 2006 CB LEU A1091 14159 10436 8780 -1181 -92 -597 C ATOM 2007 CG LEU A1091 23.680 -13.560 27.542 1.00 82.06 C ANISOU 2007 CG LEU A1091 13386 9458 8336 -1224 143 -690 C ATOM 2008 CD1 LEU A1091 24.786 -13.425 28.573 1.00 80.82 C ANISOU 2008 CD1 LEU A1091 13114 9224 8371 -989 440 -482 C ATOM 2009 CD2 LEU A1091 22.327 -13.769 28.206 1.00 80.36 C ANISOU 2009 CD2 LEU A1091 12890 9277 8367 -1435 -70 -736 C ATOM 2010 N ASP A1092 21.376 -10.343 25.562 1.00 96.05 N ANISOU 2010 N ASP A1092 14944 11880 9672 -1329 -1151 -538 N ATOM 2011 CA ASP A1092 21.052 -8.988 25.248 1.00 94.58 C ANISOU 2011 CA ASP A1092 14656 11809 9469 -1194 -1512 -321 C ATOM 2012 C ASP A1092 22.222 -8.197 25.771 1.00 90.97 C ANISOU 2012 C ASP A1092 14182 11304 9080 -989 -1249 -61 C ATOM 2013 O ASP A1092 22.961 -8.670 26.567 1.00 94.84 O ANISOU 2013 O ASP A1092 14566 11715 9754 -916 -857 -59 O ATOM 2014 CB ASP A1092 19.780 -8.669 26.007 1.00101.30 C ANISOU 2014 CB ASP A1092 15029 12751 10711 -1166 -1868 -406 C ATOM 2015 CG ASP A1092 19.607 -7.210 26.318 1.00111.33 C ANISOU 2015 CG ASP A1092 16080 14045 12176 -914 -2131 -205 C ATOM 2016 OD1 ASP A1092 20.277 -6.361 25.708 1.00117.45 O ANISOU 2016 OD1 ASP A1092 17125 14798 12702 -861 -2417 -1 O ATOM 2017 OD2 ASP A1092 18.756 -6.904 27.171 1.00112.11 O ANISOU 2017 OD2 ASP A1092 15757 14174 12666 -784 -2057 -258 O ATOM 2018 N ALA A1093 22.381 -6.966 25.331 1.00 96.88 N ANISOU 2018 N ALA A1093 15054 12081 9674 -916 -1505 178 N ATOM 2019 CA ALA A1093 23.488 -6.122 25.778 1.00 91.46 C ANISOU 2019 CA ALA A1093 14374 11336 9042 -782 -1292 431 C ATOM 2020 C ALA A1093 23.421 -5.832 27.272 1.00 93.10 C ANISOU 2020 C ALA A1093 14165 11492 9718 -603 -1188 414 C ATOM 2021 O ALA A1093 24.464 -5.712 27.927 1.00 87.73 O ANISOU 2021 O ALA A1093 13451 10765 9118 -524 -866 519 O ATOM 2022 CB ALA A1093 23.503 -4.814 24.988 1.00 88.70 C ANISOU 2022 CB ALA A1093 14227 10970 8505 -779 -1676 717 C ATOM 2023 N VAL A1094 22.214 -5.720 27.829 1.00 97.94 N ANISOU 2023 N VAL A1094 14439 12147 10627 -546 -1450 262 N ATOM 2024 CA VAL A1094 22.076 -5.445 29.257 1.00 93.00 C ANISOU 2024 CA VAL A1094 13427 11531 10378 -399 -1324 200 C ATOM 2025 C VAL A1094 22.441 -6.680 30.072 1.00 88.59 C ANISOU 2025 C VAL A1094 12819 10982 9860 -491 -879 98 C ATOM 2026 O VAL A1094 23.204 -6.601 31.041 1.00 83.02 O ANISOU 2026 O VAL A1094 12036 10247 9261 -400 -616 175 O ATOM 2027 CB VAL A1094 20.652 -4.956 29.576 1.00 91.34 C ANISOU 2027 CB VAL A1094 12822 11413 10469 -310 -1694 21 C ATOM 2028 CG1 VAL A1094 20.546 -4.549 31.038 1.00 87.18 C ANISOU 2028 CG1 VAL A1094 11914 10940 10271 -155 -1529 -81 C ATOM 2029 CG2 VAL A1094 20.261 -3.802 28.656 1.00 92.19 C ANISOU 2029 CG2 VAL A1094 13027 11445 10557 -192 -2230 148 C ATOM 2030 N ARG A1095 21.898 -7.840 29.694 1.00 90.63 N ANISOU 2030 N ARG A1095 13144 11253 10038 -685 -833 -66 N ATOM 2031 CA ARG A1095 22.284 -9.087 30.344 1.00 90.96 C ANISOU 2031 CA ARG A1095 13231 11214 10116 -790 -456 -122 C ATOM 2032 C ARG A1095 23.746 -9.427 30.091 1.00 87.34 C ANISOU 2032 C ARG A1095 13078 10619 9487 -715 -154 0 C ATOM 2033 O ARG A1095 24.354 -10.144 30.893 1.00 79.42 O ANISOU 2033 O ARG A1095 12074 9515 8587 -689 132 31 O ATOM 2034 CB ARG A1095 21.389 -10.229 29.864 1.00 87.99 C ANISOU 2034 CB ARG A1095 12907 10817 9709 -1046 -517 -333 C ATOM 2035 CG ARG A1095 19.913 -9.890 29.887 1.00 88.08 C ANISOU 2035 CG ARG A1095 12562 11010 9896 -1139 -853 -486 C ATOM 2036 CD ARG A1095 19.099 -10.979 29.236 1.00 93.06 C ANISOU 2036 CD ARG A1095 13265 11616 10479 -1439 -963 -697 C ATOM 2037 NE ARG A1095 17.793 -10.502 28.791 1.00103.22 N ANISOU 2037 NE ARG A1095 14244 13099 11877 -1501 -1404 -846 N ATOM 2038 CZ ARG A1095 16.679 -10.583 29.511 1.00102.98 C ANISOU 2038 CZ ARG A1095 13724 13246 12157 -1620 -1455 -997 C ATOM 2039 NH1 ARG A1095 16.705 -11.126 30.720 1.00101.20 N1+ ANISOU 2039 NH1 ARG A1095 13324 13034 12095 -1735 -1072 -988 N1+ ATOM 2040 NH2 ARG A1095 15.535 -10.122 29.020 1.00102.93 N ANISOU 2040 NH2 ARG A1095 13394 13427 12289 -1634 -1897 -1154 N ATOM 2041 N ARG A1096 24.321 -8.920 29.001 1.00 90.45 N ANISOU 2041 N ARG A1096 13718 11024 9623 -685 -218 78 N ATOM 2042 CA ARG A1096 25.730 -9.168 28.728 1.00 86.04 C ANISOU 2042 CA ARG A1096 13368 10402 8921 -614 110 159 C ATOM 2043 C ARG A1096 26.623 -8.481 29.750 1.00 81.52 C ANISOU 2043 C ARG A1096 12598 9829 8548 -445 250 350 C ATOM 2044 O ARG A1096 27.697 -8.997 30.076 1.00 76.37 O ANISOU 2044 O ARG A1096 11967 9110 7940 -359 548 380 O ATOM 2045 CB ARG A1096 26.072 -8.706 27.313 1.00 85.80 C ANISOU 2045 CB ARG A1096 13637 10453 8510 -686 38 205 C ATOM 2046 CG ARG A1096 26.974 -9.657 26.568 1.00 82.89 C ANISOU 2046 CG ARG A1096 13541 10054 7898 -716 389 63 C ATOM 2047 CD ARG A1096 27.247 -9.180 25.159 1.00 85.44 C ANISOU 2047 CD ARG A1096 14183 10531 7750 -844 350 102 C ATOM 2048 NE ARG A1096 26.098 -9.355 24.282 1.00 94.36 N ANISOU 2048 NE ARG A1096 15514 11710 8629 -1018 -6 -32 N ATOM 2049 CZ ARG A1096 26.167 -9.297 22.957 1.00 97.59 C ANISOU 2049 CZ ARG A1096 16291 12257 8531 -1179 -60 -72 C ATOM 2050 NH1 ARG A1096 27.333 -9.075 22.369 1.00 93.17 N ANISOU 2050 NH1 ARG A1096 15919 11820 7663 -1201 286 6 N ATOM 2051 NH2 ARG A1096 25.078 -9.465 22.222 1.00102.27 N ANISOU 2051 NH2 ARG A1096 17053 12899 8906 -1338 -456 -197 N ATOM 2052 N ALA A1097 26.196 -7.325 30.270 1.00 83.15 N ANISOU 2052 N ALA A1097 12599 10095 8899 -381 10 450 N ATOM 2053 CA ALA A1097 26.963 -6.656 31.316 1.00 74.83 C ANISOU 2053 CA ALA A1097 11361 9035 8036 -245 100 585 C ATOM 2054 C ALA A1097 26.946 -7.446 32.617 1.00 73.67 C ANISOU 2054 C ALA A1097 11047 8874 8072 -207 277 525 C ATOM 2055 O ALA A1097 27.942 -7.452 33.348 1.00 74.45 O ANISOU 2055 O ALA A1097 11087 8949 8253 -111 442 628 O ATOM 2056 CB ALA A1097 26.423 -5.246 31.550 1.00 63.51 C ANISOU 2056 CB ALA A1097 9778 7621 6732 -175 -226 643 C ATOM 2057 N ALA A1098 25.832 -8.117 32.923 1.00 71.99 N ANISOU 2057 N ALA A1098 10755 8685 7912 -311 230 379 N ATOM 2058 CA ALA A1098 25.774 -8.940 34.125 1.00 74.69 C ANISOU 2058 CA ALA A1098 11001 9011 8365 -346 407 373 C ATOM 2059 C ALA A1098 26.760 -10.098 34.047 1.00 83.58 C ANISOU 2059 C ALA A1098 12344 9949 9462 -326 646 434 C ATOM 2060 O ALA A1098 27.358 -10.485 35.059 1.00 82.43 O ANISOU 2060 O ALA A1098 12168 9750 9403 -262 768 547 O ATOM 2061 CB ALA A1098 24.351 -9.450 34.338 1.00 76.99 C ANISOU 2061 CB ALA A1098 11160 9381 8710 -537 335 213 C ATOM 2062 N LEU A1099 26.946 -10.665 32.852 1.00 86.05 N ANISOU 2062 N LEU A1099 12886 10156 9651 -363 693 343 N ATOM 2063 CA LEU A1099 27.950 -11.710 32.691 1.00 84.37 C ANISOU 2063 CA LEU A1099 12858 9742 9457 -276 922 336 C ATOM 2064 C LEU A1099 29.360 -11.153 32.838 1.00 75.62 C ANISOU 2064 C LEU A1099 11669 8675 8388 -65 1050 473 C ATOM 2065 O LEU A1099 30.242 -11.829 33.380 1.00 59.72 O ANISOU 2065 O LEU A1099 9651 6525 6517 79 1192 528 O ATOM 2066 CB LEU A1099 27.785 -12.397 31.335 1.00 88.81 C ANISOU 2066 CB LEU A1099 13687 10211 9847 -362 961 126 C ATOM 2067 CG LEU A1099 28.635 -13.647 31.091 1.00 89.13 C ANISOU 2067 CG LEU A1099 13929 9988 9947 -253 1195 11 C ATOM 2068 CD1 LEU A1099 28.246 -14.750 32.060 1.00 88.78 C ANISOU 2068 CD1 LEU A1099 13929 9678 10126 -318 1188 43 C ATOM 2069 CD2 LEU A1099 28.496 -14.118 29.655 1.00 91.08 C ANISOU 2069 CD2 LEU A1099 14451 10201 9955 -337 1240 -262 C ATOM 2070 N ILE A1100 29.591 -9.928 32.363 1.00 70.27 N ANISOU 2070 N ILE A1100 10921 8168 7612 -56 974 541 N ATOM 2071 CA ILE A1100 30.888 -9.294 32.557 1.00 70.30 C ANISOU 2071 CA ILE A1100 10796 8234 7680 77 1083 680 C ATOM 2072 C ILE A1100 31.120 -9.006 34.034 1.00 76.98 C ANISOU 2072 C ILE A1100 11428 9092 8729 165 1006 808 C ATOM 2073 O ILE A1100 32.244 -9.120 34.537 1.00 80.54 O ANISOU 2073 O ILE A1100 11764 9529 9310 301 1104 897 O ATOM 2074 CB ILE A1100 30.983 -8.022 31.697 1.00 68.88 C ANISOU 2074 CB ILE A1100 10638 8193 7340 -10 989 761 C ATOM 2075 CG1 ILE A1100 30.869 -8.386 30.212 1.00 75.73 C ANISOU 2075 CG1 ILE A1100 11771 9090 7912 -120 1082 646 C ATOM 2076 CG2 ILE A1100 32.279 -7.281 31.978 1.00 63.94 C ANISOU 2076 CG2 ILE A1100 9841 7638 6817 56 1090 917 C ATOM 2077 CD1 ILE A1100 30.869 -7.196 29.275 1.00 65.67 C ANISOU 2077 CD1 ILE A1100 10607 7938 6405 -260 954 784 C ATOM 2078 N ASN A1101 30.057 -8.645 34.757 1.00 76.26 N ANISOU 2078 N ASN A1101 11262 9055 8656 88 828 795 N ATOM 2079 CA ASN A1101 30.161 -8.449 36.200 1.00 71.74 C ANISOU 2079 CA ASN A1101 10532 8535 8191 138 773 876 C ATOM 2080 C ASN A1101 30.619 -9.725 36.896 1.00 69.64 C ANISOU 2080 C ASN A1101 10339 8134 7987 190 891 949 C ATOM 2081 O ASN A1101 31.439 -9.679 37.821 1.00 64.42 O ANISOU 2081 O ASN A1101 9588 7486 7403 297 869 1078 O ATOM 2082 CB ASN A1101 28.811 -7.981 36.750 1.00 72.99 C ANISOU 2082 CB ASN A1101 10589 8814 8330 34 629 774 C ATOM 2083 CG ASN A1101 28.882 -7.542 38.204 1.00 79.76 C ANISOU 2083 CG ASN A1101 11293 9793 9219 68 586 807 C ATOM 2084 OD1 ASN A1101 29.385 -8.264 39.065 1.00 88.11 O ANISOU 2084 OD1 ASN A1101 12391 10824 10262 80 664 919 O ATOM 2085 ND2 ASN A1101 28.363 -6.353 38.484 1.00 77.04 N ANISOU 2085 ND2 ASN A1101 10794 9569 8909 92 434 696 N ATOM 2086 N MET A1102 30.111 -10.877 36.452 1.00 67.47 N ANISOU 2086 N MET A1102 10246 7696 7691 110 973 875 N ATOM 2087 CA MET A1102 30.457 -12.137 37.100 1.00 68.00 C ANISOU 2087 CA MET A1102 10442 7546 7851 150 1035 971 C ATOM 2088 C MET A1102 31.900 -12.539 36.815 1.00 75.21 C ANISOU 2088 C MET A1102 11354 8314 8910 407 1126 1011 C ATOM 2089 O MET A1102 32.611 -12.984 37.723 1.00 77.63 O ANISOU 2089 O MET A1102 11635 8519 9341 543 1075 1172 O ATOM 2090 CB MET A1102 29.492 -13.233 36.655 1.00 70.40 C ANISOU 2090 CB MET A1102 10958 7659 8132 -38 1075 861 C ATOM 2091 CG MET A1102 28.072 -13.024 37.150 1.00 76.57 C ANISOU 2091 CG MET A1102 11663 8605 8824 -310 1005 826 C ATOM 2092 SD MET A1102 27.010 -14.445 36.822 1.00 81.97 S ANISOU 2092 SD MET A1102 12572 9042 9532 -608 1039 733 S ATOM 2093 CE MET A1102 27.916 -15.743 37.652 1.00 80.68 C ANISOU 2093 CE MET A1102 12664 8490 9502 -523 1086 972 C ATOM 2094 N VAL A1103 32.352 -12.395 35.565 1.00 79.58 N ANISOU 2094 N VAL A1103 11918 8879 9439 475 1257 861 N ATOM 2095 CA VAL A1103 33.743 -12.721 35.251 1.00 82.54 C ANISOU 2095 CA VAL A1103 12205 9184 9974 728 1400 840 C ATOM 2096 C VAL A1103 34.689 -11.726 35.912 1.00 80.24 C ANISOU 2096 C VAL A1103 11618 9095 9774 826 1331 1000 C ATOM 2097 O VAL A1103 35.848 -12.053 36.198 1.00 82.23 O ANISOU 2097 O VAL A1103 11705 9299 10238 1051 1366 1045 O ATOM 2098 CB VAL A1103 33.969 -12.782 33.727 1.00 84.75 C ANISOU 2098 CB VAL A1103 12570 9500 10133 729 1619 609 C ATOM 2099 CG1 VAL A1103 32.942 -13.689 33.066 1.00 85.19 C ANISOU 2099 CG1 VAL A1103 12933 9364 10070 590 1631 415 C ATOM 2100 CG2 VAL A1103 33.931 -11.394 33.115 1.00 83.71 C ANISOU 2100 CG2 VAL A1103 12339 9665 9801 582 1615 646 C ATOM 2101 N PHE A1104 34.222 -10.502 36.163 1.00 72.46 N ANISOU 2101 N PHE A1104 10543 8321 8669 670 1206 1064 N ATOM 2102 CA PHE A1104 35.025 -9.556 36.927 1.00 74.27 C ANISOU 2102 CA PHE A1104 10521 8703 8994 721 1090 1196 C ATOM 2103 C PHE A1104 35.203 -10.013 38.369 1.00 79.15 C ANISOU 2103 C PHE A1104 11108 9268 9696 808 920 1340 C ATOM 2104 O PHE A1104 36.258 -9.779 38.969 1.00 81.90 O ANISOU 2104 O PHE A1104 11250 9676 10191 937 827 1439 O ATOM 2105 CB PHE A1104 34.382 -8.171 36.883 1.00 67.54 C ANISOU 2105 CB PHE A1104 9633 8010 8019 545 959 1195 C ATOM 2106 CG PHE A1104 35.032 -7.234 35.911 1.00 71.68 C ANISOU 2106 CG PHE A1104 10068 8632 8534 483 1036 1205 C ATOM 2107 CD1 PHE A1104 34.785 -7.340 34.554 1.00 74.18 C ANISOU 2107 CD1 PHE A1104 10546 8950 8690 396 1191 1126 C ATOM 2108 CD2 PHE A1104 35.892 -6.243 36.356 1.00 80.86 C ANISOU 2108 CD2 PHE A1104 11011 9893 9821 465 944 1303 C ATOM 2109 CE1 PHE A1104 35.384 -6.477 33.659 1.00 78.16 C ANISOU 2109 CE1 PHE A1104 11011 9565 9121 278 1280 1183 C ATOM 2110 CE2 PHE A1104 36.492 -5.376 35.467 1.00 85.63 C ANISOU 2110 CE2 PHE A1104 11550 10576 10412 335 1028 1354 C ATOM 2111 CZ PHE A1104 36.238 -5.493 34.115 1.00 81.25 C ANISOU 2111 CZ PHE A1104 11176 10035 9661 234 1209 1314 C ATOM 2112 N GLN A1105 34.192 -10.669 38.935 1.00 80.45 N ANISOU 2112 N GLN A1105 11475 9341 9754 708 866 1365 N ATOM 2113 CA GLN A1105 34.237 -11.118 40.319 1.00 76.17 C ANISOU 2113 CA GLN A1105 10978 8769 9193 723 706 1544 C ATOM 2114 C GLN A1105 34.839 -12.508 40.465 1.00 79.87 C ANISOU 2114 C GLN A1105 11579 8938 9829 899 695 1660 C ATOM 2115 O GLN A1105 35.670 -12.731 41.352 1.00 77.78 O ANISOU 2115 O GLN A1105 11252 8640 9660 1051 517 1841 O ATOM 2116 CB GLN A1105 32.830 -11.107 40.918 1.00 71.88 C ANISOU 2116 CB GLN A1105 10574 8313 8426 472 687 1531 C ATOM 2117 CG GLN A1105 32.752 -11.692 42.313 1.00 71.95 C ANISOU 2117 CG GLN A1105 10707 8315 8315 408 569 1741 C ATOM 2118 CD GLN A1105 31.379 -11.534 42.928 1.00 72.70 C ANISOU 2118 CD GLN A1105 10864 8598 8159 121 622 1689 C ATOM 2119 OE1 GLN A1105 30.414 -11.193 42.241 1.00 76.06 O ANISOU 2119 OE1 GLN A1105 11232 9099 8567 -1 727 1488 O ATOM 2120 NE2 GLN A1105 31.282 -11.777 44.230 1.00 68.30 N ANISOU 2120 NE2 GLN A1105 10410 8146 7396 7 545 1865 N ATOM 2121 N MET A1106 34.433 -13.446 39.607 1.00 80.28 N ANISOU 2121 N MET A1106 11826 8743 9934 892 842 1548 N ATOM 2122 CA MET A1106 34.803 -14.847 39.734 1.00 82.95 C ANISOU 2122 CA MET A1106 12358 8697 10463 1051 807 1630 C ATOM 2123 C MET A1106 35.843 -15.311 38.725 1.00 89.43 C ANISOU 2123 C MET A1106 13075 9350 11554 1362 949 1444 C ATOM 2124 O MET A1106 36.305 -16.452 38.830 1.00 92.75 O ANISOU 2124 O MET A1106 13623 9404 12215 1580 890 1476 O ATOM 2125 CB MET A1106 33.551 -15.727 39.604 1.00 79.57 C ANISOU 2125 CB MET A1106 12259 8043 9930 793 855 1607 C ATOM 2126 CG MET A1106 32.706 -15.755 40.856 1.00 84.73 C ANISOU 2126 CG MET A1106 13038 8785 10370 512 733 1843 C ATOM 2127 SD MET A1106 30.984 -16.135 40.503 1.00 86.03 S ANISOU 2127 SD MET A1106 13388 8937 10364 82 862 1721 S ATOM 2128 CE MET A1106 30.421 -14.540 39.929 1.00 88.27 C ANISOU 2128 CE MET A1106 13356 9694 10490 13 937 1471 C ATOM 2129 N GLY A1107 36.219 -14.477 37.763 1.00 83.47 N ANISOU 2129 N GLY A1107 12104 8844 10768 1383 1136 1249 N ATOM 2130 CA GLY A1107 37.045 -14.923 36.668 1.00 86.98 C ANISOU 2130 CA GLY A1107 12460 9202 11389 1617 1365 1006 C ATOM 2131 C GLY A1107 36.292 -15.824 35.707 1.00 88.79 C ANISOU 2131 C GLY A1107 13014 9179 11544 1543 1521 764 C ATOM 2132 O GLY A1107 35.264 -16.426 36.027 1.00 86.13 O ANISOU 2132 O GLY A1107 12973 8625 11128 1354 1409 824 O ATOM 2133 N GLU A1108 36.843 -15.917 34.497 1.00 89.49 N ANISOU 2133 N GLU A1108 13038 9319 11644 1667 1796 468 N ATOM 2134 CA GLU A1108 36.262 -16.761 33.464 1.00 87.52 C ANISOU 2134 CA GLU A1108 13103 8850 11300 1613 1951 163 C ATOM 2135 C GLU A1108 36.230 -18.231 33.861 1.00 85.64 C ANISOU 2135 C GLU A1108 13113 8070 11356 1798 1837 124 C ATOM 2136 O GLU A1108 35.365 -18.973 33.377 1.00 84.49 O ANISOU 2136 O GLU A1108 13313 7661 11130 1634 1842 -46 O ATOM 2137 CB GLU A1108 37.029 -16.590 32.160 1.00 95.88 C ANISOU 2137 CB GLU A1108 14037 10114 12279 1733 2303 -169 C ATOM 2138 CG GLU A1108 36.931 -15.181 31.598 1.00102.62 C ANISOU 2138 CG GLU A1108 14756 11443 12792 1470 2402 -100 C ATOM 2139 CD GLU A1108 37.375 -15.104 30.157 1.00109.37 C ANISOU 2139 CD GLU A1108 15629 12514 13413 1456 2771 -421 C ATOM 2140 OE1 GLU A1108 37.716 -16.168 29.591 1.00113.53 O ANISOU 2140 OE1 GLU A1108 16260 12832 14044 1672 2970 -764 O ATOM 2141 OE2 GLU A1108 37.380 -13.985 29.593 1.00105.41 O1+ ANISOU 2141 OE2 GLU A1108 15063 12377 12612 1221 2859 -335 O1+ ATOM 2142 N THR A1109 37.155 -18.669 34.719 1.00 90.70 N ANISOU 2142 N THR A1109 13597 8510 12353 2124 1695 286 N ATOM 2143 CA THR A1109 37.120 -20.042 35.207 1.00 95.84 C ANISOU 2143 CA THR A1109 14532 8571 13311 2298 1506 331 C ATOM 2144 C THR A1109 35.855 -20.297 36.012 1.00 92.70 C ANISOU 2144 C THR A1109 14477 8003 12741 1906 1273 629 C ATOM 2145 O THR A1109 35.133 -21.269 35.766 1.00 95.09 O ANISOU 2145 O THR A1109 15151 7895 13084 1765 1241 533 O ATOM 2146 CB THR A1109 38.349 -20.335 36.066 1.00 97.86 C ANISOU 2146 CB THR A1109 14535 8674 13974 2728 1309 517 C ATOM 2147 OG1 THR A1109 39.538 -19.920 35.381 1.00102.45 O ANISOU 2147 OG1 THR A1109 14672 9535 14718 3048 1561 242 O ATOM 2148 CG2 THR A1109 38.427 -21.828 36.376 1.00 97.85 C ANISOU 2148 CG2 THR A1109 14861 7969 14349 2976 1099 531 C ATOM 2149 N GLY A1110 35.567 -19.420 36.975 1.00 95.75 N ANISOU 2149 N GLY A1110 14731 8720 12931 1701 1128 965 N ATOM 2150 CA GLY A1110 34.456 -19.660 37.880 1.00 94.88 C ANISOU 2150 CA GLY A1110 14887 8513 12649 1331 949 1253 C ATOM 2151 C GLY A1110 33.103 -19.552 37.204 1.00 88.67 C ANISOU 2151 C GLY A1110 14261 7826 11602 922 1075 1072 C ATOM 2152 O GLY A1110 32.191 -20.329 37.497 1.00 82.42 O ANISOU 2152 O GLY A1110 13765 6760 10793 635 997 1160 O ATOM 2153 N VAL A1111 32.952 -18.588 36.296 1.00 85.36 N ANISOU 2153 N VAL A1111 13649 7799 10986 866 1244 836 N ATOM 2154 CA VAL A1111 31.676 -18.422 35.606 1.00 83.59 C ANISOU 2154 CA VAL A1111 13541 7694 10525 508 1297 660 C ATOM 2155 C VAL A1111 31.371 -19.646 34.751 1.00 86.94 C ANISOU 2155 C VAL A1111 14292 7686 11055 469 1346 385 C ATOM 2156 O VAL A1111 30.217 -20.080 34.649 1.00 84.62 O ANISOU 2156 O VAL A1111 14188 7281 10681 116 1284 338 O ATOM 2157 CB VAL A1111 31.689 -17.125 34.776 1.00 78.72 C ANISOU 2157 CB VAL A1111 12692 7539 9679 492 1403 508 C ATOM 2158 CG1 VAL A1111 30.403 -16.979 33.994 1.00 82.94 C ANISOU 2158 CG1 VAL A1111 13340 8183 9992 166 1385 324 C ATOM 2159 CG2 VAL A1111 31.894 -15.925 35.684 1.00 68.67 C ANISOU 2159 CG2 VAL A1111 11133 6621 8339 498 1317 755 C ATOM 2160 N ALA A1112 32.402 -20.242 34.147 1.00 83.83 N ANISOU 2160 N ALA A1112 13946 7039 10867 828 1457 166 N ATOM 2161 CA ALA A1112 32.208 -21.434 33.331 1.00 86.95 C ANISOU 2161 CA ALA A1112 14676 6976 11386 838 1502 -166 C ATOM 2162 C ALA A1112 31.727 -22.636 34.137 1.00 97.68 C ANISOU 2162 C ALA A1112 16361 7762 12989 696 1293 31 C ATOM 2163 O ALA A1112 31.408 -23.672 33.541 1.00107.07 O ANISOU 2163 O ALA A1112 17878 8495 14308 634 1283 -236 O ATOM 2164 CB ALA A1112 33.504 -21.784 32.597 1.00 82.87 C ANISOU 2164 CB ALA A1112 14088 6331 11068 1312 1699 -487 C ATOM 2165 N GLY A1113 31.670 -22.528 35.467 1.00 94.08 N ANISOU 2165 N GLY A1113 15859 7311 12576 613 1121 490 N ATOM 2166 CA GLY A1113 31.127 -23.580 36.301 1.00 91.96 C ANISOU 2166 CA GLY A1113 15934 6547 12461 374 924 767 C ATOM 2167 C GLY A1113 29.632 -23.536 36.499 1.00 88.01 C ANISOU 2167 C GLY A1113 15526 6189 11726 -228 907 854 C ATOM 2168 O GLY A1113 29.067 -24.463 37.088 1.00 90.55 O ANISOU 2168 O GLY A1113 16155 6098 12153 -532 780 1074 O ATOM 2169 N PHE A1114 28.975 -22.477 36.030 1.00 89.32 N ANISOU 2169 N PHE A1114 15419 6923 11597 -417 1020 697 N ATOM 2170 CA PHE A1114 27.518 -22.347 36.101 1.00 93.06 C ANISOU 2170 CA PHE A1114 15868 7604 11887 -955 1007 701 C ATOM 2171 C PHE A1114 26.844 -22.935 34.867 1.00 97.68 C ANISOU 2171 C PHE A1114 16640 7982 12490 -1154 1008 293 C ATOM 2172 O PHE A1114 25.996 -22.294 34.250 1.00100.46 O ANISOU 2172 O PHE A1114 16812 8720 12638 -1379 1016 94 O ATOM 2173 CB PHE A1114 27.127 -20.883 36.266 1.00 94.49 C ANISOU 2173 CB PHE A1114 15638 8468 11794 -1010 1062 728 C ATOM 2174 CG PHE A1114 27.602 -20.258 37.542 1.00 95.33 C ANISOU 2174 CG PHE A1114 15570 8818 11834 -900 1044 1086 C ATOM 2175 CD1 PHE A1114 26.863 -20.382 38.706 1.00 96.26 C ANISOU 2175 CD1 PHE A1114 15694 9032 11847 -1255 1023 1375 C ATOM 2176 CD2 PHE A1114 28.773 -19.521 37.572 1.00 93.76 C ANISOU 2176 CD2 PHE A1114 15190 8788 11647 -478 1057 1113 C ATOM 2177 CE1 PHE A1114 27.293 -19.799 39.881 1.00 93.49 C ANISOU 2177 CE1 PHE A1114 15219 8937 11366 -1170 999 1669 C ATOM 2178 CE2 PHE A1114 29.209 -18.933 38.743 1.00 90.99 C ANISOU 2178 CE2 PHE A1114 14688 8664 11219 -396 999 1410 C ATOM 2179 CZ PHE A1114 28.468 -19.072 39.900 1.00 89.90 C ANISOU 2179 CZ PHE A1114 14603 8619 10937 -731 961 1678 C ATOM 2180 N THR A1115 27.213 -24.163 34.496 1.00 93.63 N ANISOU 2180 N THR A1115 16502 6840 12234 -1062 963 146 N ATOM 2181 CA THR A1115 26.755 -24.715 33.225 1.00 97.80 C ANISOU 2181 CA THR A1115 17241 7160 12760 -1192 960 -325 C ATOM 2182 C THR A1115 25.237 -24.821 33.175 1.00101.53 C ANISOU 2182 C THR A1115 17699 7752 13126 -1809 862 -353 C ATOM 2183 O THR A1115 24.618 -24.467 32.164 1.00100.69 O ANISOU 2183 O THR A1115 17515 7914 12829 -1958 838 -694 O ATOM 2184 CB THR A1115 27.395 -26.081 32.984 1.00104.56 C ANISOU 2184 CB THR A1115 18523 7240 13966 -980 909 -494 C ATOM 2185 OG1 THR A1115 26.936 -27.010 33.974 1.00111.74 O ANISOU 2185 OG1 THR A1115 19700 7650 15106 -1304 745 -134 O ATOM 2186 CG2 THR A1115 28.912 -25.975 33.059 1.00103.25 C ANISOU 2186 CG2 THR A1115 18273 6991 13964 -334 1002 -493 C ATOM 2187 N ASN A1116 24.617 -25.292 34.259 1.00109.01 N ANISOU 2187 N ASN A1116 18703 8536 14180 -2193 797 12 N ATOM 2188 CA ASN A1116 23.168 -25.450 34.256 1.00114.25 C ANISOU 2188 CA ASN A1116 19286 9335 14790 -2821 734 -24 C ATOM 2189 C ASN A1116 22.464 -24.103 34.180 1.00108.33 C ANISOU 2189 C ASN A1116 18027 9368 13766 -2910 776 -69 C ATOM 2190 O ASN A1116 21.401 -23.993 33.560 1.00112.39 O ANISOU 2190 O ASN A1116 18389 10096 14219 -3257 688 -317 O ATOM 2191 CB ASN A1116 22.716 -26.227 35.496 1.00119.12 C ANISOU 2191 CB ASN A1116 20066 9646 15546 -3254 712 417 C ATOM 2192 N SER A1117 23.040 -23.071 34.794 1.00107.10 N ANISOU 2192 N SER A1117 17599 9621 13474 -2592 871 149 N ATOM 2193 CA SER A1117 22.434 -21.748 34.719 1.00102.31 C ANISOU 2193 CA SER A1117 16531 9686 12658 -2613 880 85 C ATOM 2194 C SER A1117 22.674 -21.101 33.361 1.00102.29 C ANISOU 2194 C SER A1117 16484 9870 12513 -2343 814 -265 C ATOM 2195 O SER A1117 21.756 -20.507 32.785 1.00100.23 O ANISOU 2195 O SER A1117 15984 9960 12139 -2521 696 -453 O ATOM 2196 CB SER A1117 22.981 -20.857 35.835 1.00 98.47 C ANISOU 2196 CB SER A1117 15811 9527 12076 -2381 982 404 C ATOM 2197 OG SER A1117 22.892 -21.504 37.092 1.00 97.73 O ANISOU 2197 OG SER A1117 15842 9258 12035 -2624 1039 761 O ATOM 2198 N LEU A1118 23.897 -21.215 32.836 1.00104.26 N ANISOU 2198 N LEU A1118 16951 9904 12761 -1923 883 -351 N ATOM 2199 CA LEU A1118 24.243 -20.548 31.585 1.00100.23 C ANISOU 2199 CA LEU A1118 16425 9622 12038 -1690 875 -637 C ATOM 2200 C LEU A1118 23.389 -21.046 30.427 1.00107.73 C ANISOU 2200 C LEU A1118 17547 10492 12892 -1976 724 -1011 C ATOM 2201 O LEU A1118 23.041 -20.274 29.525 1.00110.02 O ANISOU 2201 O LEU A1118 17736 11135 12931 -1982 613 -1185 O ATOM 2202 CB LEU A1118 25.722 -20.757 31.279 1.00 92.05 C ANISOU 2202 CB LEU A1118 15569 8366 11040 -1233 1041 -692 C ATOM 2203 CG LEU A1118 26.695 -19.998 32.171 1.00 86.98 C ANISOU 2203 CG LEU A1118 14695 7910 10443 -907 1144 -375 C ATOM 2204 CD1 LEU A1118 28.100 -20.549 32.003 1.00 86.56 C ANISOU 2204 CD1 LEU A1118 14792 7548 10551 -488 1291 -444 C ATOM 2205 CD2 LEU A1118 26.654 -18.516 31.846 1.00 86.67 C ANISOU 2205 CD2 LEU A1118 14359 8413 10159 -835 1133 -349 C ATOM 2206 N ARG A1119 23.046 -22.333 30.429 1.00104.44 N ANISOU 2206 N ARG A1119 17422 9590 12668 -2232 680 -1129 N ATOM 2207 CA ARG A1119 22.191 -22.858 29.372 1.00103.70 C ANISOU 2207 CA ARG A1119 17500 9406 12496 -2554 498 -1514 C ATOM 2208 C ARG A1119 20.795 -22.250 29.433 1.00102.63 C ANISOU 2208 C ARG A1119 16991 9707 12297 -2952 292 -1490 C ATOM 2209 O ARG A1119 20.133 -22.113 28.398 1.00102.11 O ANISOU 2209 O ARG A1119 16930 9811 12055 -3119 75 -1792 O ATOM 2210 CB ARG A1119 22.123 -24.383 29.466 1.00105.66 C ANISOU 2210 CB ARG A1119 18150 8971 13026 -2774 474 -1635 C ATOM 2211 CG ARG A1119 21.461 -25.066 28.282 1.00110.68 C ANISOU 2211 CG ARG A1119 19053 9414 13586 -3068 283 -2116 C ATOM 2212 CD ARG A1119 21.400 -26.576 28.478 1.00119.37 C ANISOU 2212 CD ARG A1119 20574 9750 15030 -3303 239 -2220 C ATOM 2213 NE ARG A1119 20.881 -26.936 29.795 1.00121.59 N ANISOU 2213 NE ARG A1119 20741 9865 15590 -3652 240 -1772 N ATOM 2214 CZ ARG A1119 21.609 -27.484 30.763 1.00120.23 C ANISOU 2214 CZ ARG A1119 20757 9256 15669 -3483 350 -1432 C ATOM 2215 NH1 ARG A1119 22.893 -27.748 30.561 1.00119.50 N1+ ANISOU 2215 NH1 ARG A1119 20917 8831 15658 -2927 455 -1524 N1+ ATOM 2216 NH2 ARG A1119 21.053 -27.772 31.933 1.00120.62 N ANISOU 2216 NH2 ARG A1119 20732 9219 15878 -3878 351 -1000 N ATOM 2217 N MET A1120 20.338 -21.863 30.627 1.00100.48 N ANISOU 2217 N MET A1120 16375 9649 12155 -3093 347 -1158 N ATOM 2218 CA MET A1120 19.012 -21.263 30.756 1.00103.10 C ANISOU 2218 CA MET A1120 16260 10430 12486 -3427 184 -1176 C ATOM 2219 C MET A1120 19.000 -19.818 30.272 1.00100.31 C ANISOU 2219 C MET A1120 15604 10594 11915 -3129 66 -1209 C ATOM 2220 O MET A1120 18.009 -19.365 29.686 1.00100.24 O ANISOU 2220 O MET A1120 15342 10888 11857 -3303 -198 -1388 O ATOM 2221 CB MET A1120 18.535 -21.349 32.203 1.00106.18 C ANISOU 2221 CB MET A1120 16380 10910 13054 -3686 341 -856 C ATOM 2222 CG MET A1120 18.420 -22.776 32.714 1.00117.71 C ANISOU 2222 CG MET A1120 18166 11832 14725 -4073 415 -750 C ATOM 2223 SD MET A1120 17.789 -22.885 34.401 1.00123.98 S ANISOU 2223 SD MET A1120 18683 12804 15620 -4485 629 -335 S ATOM 2224 CE MET A1120 17.761 -24.663 34.625 1.00131.09 C ANISOU 2224 CE MET A1120 20134 12916 16760 -4951 624 -214 C ATOM 2225 N LEU A1121 20.082 -19.075 30.519 1.00100.35 N ANISOU 2225 N LEU A1121 15626 10687 11815 -2692 222 -1026 N ATOM 2226 CA LEU A1121 20.236 -17.769 29.884 1.00100.41 C ANISOU 2226 CA LEU A1121 15473 11071 11608 -2415 91 -1049 C ATOM 2227 C LEU A1121 20.299 -17.911 28.369 1.00105.95 C ANISOU 2227 C LEU A1121 16480 11732 12045 -2411 -85 -1340 C ATOM 2228 O LEU A1121 19.794 -17.057 27.629 1.00108.90 O ANISOU 2228 O LEU A1121 16728 12416 12235 -2399 -355 -1411 O ATOM 2229 CB LEU A1121 21.498 -17.077 30.396 1.00 89.96 C ANISOU 2229 CB LEU A1121 14156 9787 10238 -2005 306 -807 C ATOM 2230 CG LEU A1121 21.578 -16.711 31.874 1.00 82.79 C ANISOU 2230 CG LEU A1121 12972 8988 9494 -1956 454 -522 C ATOM 2231 CD1 LEU A1121 22.975 -16.220 32.204 1.00 72.92 C ANISOU 2231 CD1 LEU A1121 11799 7708 8200 -1566 625 -331 C ATOM 2232 CD2 LEU A1121 20.549 -15.649 32.207 1.00 85.66 C ANISOU 2232 CD2 LEU A1121 12882 9776 9890 -2027 296 -524 C ATOM 2233 N GLN A1122 20.920 -18.991 27.892 1.00 98.13 N ANISOU 2233 N GLN A1122 15913 10351 11023 -2411 46 -1520 N ATOM 2234 CA GLN A1122 21.020 -19.232 26.459 1.00 98.26 C ANISOU 2234 CA GLN A1122 16271 10336 10727 -2427 -75 -1857 C ATOM 2235 C GLN A1122 19.667 -19.584 25.852 1.00 96.39 C ANISOU 2235 C GLN A1122 15998 10161 10466 -2846 -440 -2111 C ATOM 2236 O GLN A1122 19.425 -19.301 24.674 1.00 98.68 O ANISOU 2236 O GLN A1122 16445 10634 10417 -2889 -682 -2330 O ATOM 2237 CB GLN A1122 22.036 -20.346 26.201 1.00103.05 C ANISOU 2237 CB GLN A1122 17309 10483 11362 -2283 189 -2053 C ATOM 2238 CG GLN A1122 22.347 -20.616 24.747 1.00107.55 C ANISOU 2238 CG GLN A1122 18269 11042 11552 -2252 165 -2458 C ATOM 2239 CD GLN A1122 23.447 -21.645 24.581 1.00111.75 C ANISOU 2239 CD GLN A1122 19160 11128 12172 -2017 475 -2696 C ATOM 2240 OE1 GLN A1122 24.039 -22.100 25.559 1.00115.12 O ANISOU 2240 OE1 GLN A1122 19540 11237 12962 -1840 666 -2506 O ATOM 2241 NE2 GLN A1122 23.726 -22.017 23.338 1.00113.25 N ANISOU 2241 NE2 GLN A1122 19714 11294 12023 -1998 511 -3131 N ATOM 2242 N GLN A1123 18.773 -20.184 26.639 1.00102.08 N ANISOU 2242 N GLN A1123 16506 10761 11521 -3189 -495 -2073 N ATOM 2243 CA GLN A1123 17.459 -20.603 26.168 1.00103.74 C ANISOU 2243 CA GLN A1123 16604 11025 11786 -3643 -839 -2321 C ATOM 2244 C GLN A1123 16.362 -19.590 26.496 1.00108.72 C ANISOU 2244 C GLN A1123 16638 12153 12517 -3742 -1093 -2203 C ATOM 2245 O GLN A1123 15.179 -19.947 26.486 1.00110.87 O ANISOU 2245 O GLN A1123 16643 12510 12973 -4152 -1332 -2352 O ATOM 2246 CB GLN A1123 17.101 -21.971 26.754 1.00101.84 C ANISOU 2246 CB GLN A1123 16492 10326 11878 -4039 -744 -2378 C ATOM 2247 CG GLN A1123 17.964 -23.119 26.251 1.00 99.00 C ANISOU 2247 CG GLN A1123 16739 9389 11487 -3971 -604 -2613 C ATOM 2248 CD GLN A1123 17.609 -24.442 26.905 1.00109.60 C ANISOU 2248 CD GLN A1123 18244 10191 13208 -4372 -553 -2607 C ATOM 2249 OE1 GLN A1123 17.694 -24.589 28.124 1.00109.83 O ANISOU 2249 OE1 GLN A1123 18131 10108 13491 -4423 -352 -2243 O ATOM 2250 NE2 GLN A1123 17.200 -25.410 26.095 1.00111.61 N ANISOU 2250 NE2 GLN A1123 18833 10095 13478 -4692 -754 -3005 N ATOM 2251 N LYS A1124 16.728 -18.344 26.794 1.00101.10 N ANISOU 2251 N LYS A1124 15436 11503 11475 -3376 -1053 -1965 N ATOM 2252 CA LYS A1124 15.801 -17.264 27.128 1.00102.00 C ANISOU 2252 CA LYS A1124 14979 12055 11722 -3354 -1290 -1880 C ATOM 2253 C LYS A1124 14.956 -17.560 28.362 1.00106.14 C ANISOU 2253 C LYS A1124 15026 12671 12629 -3642 -1145 -1813 C ATOM 2254 O LYS A1124 13.969 -16.858 28.613 1.00108.27 O ANISOU 2254 O LYS A1124 14746 13316 13075 -3688 -1344 -1851 O ATOM 2255 CB LYS A1124 14.875 -16.927 25.950 1.00104.85 C ANISOU 2255 CB LYS A1124 15253 12649 11937 -3482 -1823 -2115 C ATOM 2256 CG LYS A1124 15.585 -16.569 24.655 1.00106.34 C ANISOU 2256 CG LYS A1124 15931 12827 11648 -3267 -1994 -2170 C ATOM 2257 CD LYS A1124 16.318 -15.246 24.762 1.00102.53 C ANISOU 2257 CD LYS A1124 15411 12521 11026 -2834 -1939 -1876 C ATOM 2258 CE LYS A1124 16.710 -14.725 23.392 1.00104.63 C ANISOU 2258 CE LYS A1124 16088 12882 10786 -2721 -2205 -1897 C ATOM 2259 NZ LYS A1124 15.510 -14.429 22.560 1.00109.17 N ANISOU 2259 NZ LYS A1124 16517 13684 11279 -2897 -2828 -2043 N ATOM 2260 N ARG A1125 15.311 -18.583 29.142 1.00109.81 N ANISOU 2260 N ARG A1125 15685 12809 13228 -3839 -806 -1713 N ATOM 2261 CA ARG A1125 14.563 -18.937 30.349 1.00105.46 C ANISOU 2261 CA ARG A1125 14749 12354 12966 -4188 -611 -1603 C ATOM 2262 C ARG A1125 15.011 -18.038 31.502 1.00105.15 C ANISOU 2262 C ARG A1125 14454 12555 12943 -3878 -338 -1327 C ATOM 2263 O ARG A1125 15.645 -18.469 32.467 1.00102.11 O ANISOU 2263 O ARG A1125 14245 11977 12576 -3884 -12 -1083 O ATOM 2264 CB ARG A1125 14.757 -20.408 30.687 1.00100.56 C ANISOU 2264 CB ARG A1125 14519 11232 12456 -4562 -413 -1558 C ATOM 2265 CG ARG A1125 14.118 -21.370 29.702 1.00104.76 C ANISOU 2265 CG ARG A1125 15255 11516 13034 -4972 -689 -1879 C ATOM 2266 CD ARG A1125 14.117 -22.790 30.251 1.00109.68 C ANISOU 2266 CD ARG A1125 16197 11614 13861 -5418 -505 -1800 C ATOM 2267 NE ARG A1125 15.435 -23.419 30.187 1.00111.71 N ANISOU 2267 NE ARG A1125 17086 11317 14042 -5114 -333 -1714 N ATOM 2268 CZ ARG A1125 15.756 -24.551 30.807 1.00114.79 C ANISOU 2268 CZ ARG A1125 17840 11156 14619 -5338 -166 -1549 C ATOM 2269 NH1 ARG A1125 14.859 -25.182 31.553 1.00117.33 N1+ ANISOU 2269 NH1 ARG A1125 17995 11419 15168 -5934 -115 -1411 N1+ ATOM 2270 NH2 ARG A1125 16.978 -25.051 30.689 1.00114.27 N ANISOU 2270 NH2 ARG A1125 18294 10594 14529 -4971 -54 -1512 N ATOM 2271 N TRP A1126 14.657 -16.753 31.387 1.00102.43 N ANISOU 2271 N TRP A1126 13702 12620 12595 -3599 -520 -1377 N ATOM 2272 CA TRP A1126 15.103 -15.775 32.375 1.00 99.11 C ANISOU 2272 CA TRP A1126 13061 12418 12179 -3267 -310 -1183 C ATOM 2273 C TRP A1126 14.567 -16.088 33.763 1.00100.00 C ANISOU 2273 C TRP A1126 12842 12708 12447 -3564 17 -1092 C ATOM 2274 O TRP A1126 15.235 -15.807 34.763 1.00 95.88 O ANISOU 2274 O TRP A1126 12367 12211 11852 -3395 296 -877 O ATOM 2275 CB TRP A1126 14.683 -14.363 31.959 1.00 98.18 C ANISOU 2275 CB TRP A1126 12566 12644 12092 -2934 -622 -1293 C ATOM 2276 CG TRP A1126 15.001 -14.027 30.537 1.00 99.97 C ANISOU 2276 CG TRP A1126 13108 12760 12116 -2737 -990 -1360 C ATOM 2277 CD1 TRP A1126 14.127 -13.586 29.588 1.00102.49 C ANISOU 2277 CD1 TRP A1126 13224 13259 12460 -2750 -1458 -1549 C ATOM 2278 CD2 TRP A1126 16.280 -14.113 29.895 1.00100.88 C ANISOU 2278 CD2 TRP A1126 13796 12592 11940 -2519 -920 -1236 C ATOM 2279 NE1 TRP A1126 14.782 -13.387 28.397 1.00102.69 N ANISOU 2279 NE1 TRP A1126 13720 13132 12164 -2582 -1684 -1520 N ATOM 2280 CE2 TRP A1126 16.105 -13.705 28.559 1.00102.48 C ANISOU 2280 CE2 TRP A1126 14155 12841 11942 -2447 -1322 -1348 C ATOM 2281 CE3 TRP A1126 17.558 -14.494 30.321 1.00101.84 C ANISOU 2281 CE3 TRP A1126 14288 12451 11954 -2377 -563 -1048 C ATOM 2282 CZ2 TRP A1126 17.157 -13.666 27.646 1.00107.44 C ANISOU 2282 CZ2 TRP A1126 15302 13297 12222 -2277 -1308 -1288 C ATOM 2283 CZ3 TRP A1126 18.601 -14.457 29.411 1.00101.67 C ANISOU 2283 CZ3 TRP A1126 14713 12253 11664 -2171 -560 -1020 C ATOM 2284 CH2 TRP A1126 18.393 -14.051 28.088 1.00104.96 C ANISOU 2284 CH2 TRP A1126 15284 12756 11842 -2142 -895 -1146 C ATOM 2285 N ASP A1127 13.370 -16.667 33.848 1.00105.05 N ANISOU 2285 N ASP A1127 13142 13500 13273 -4040 -10 -1251 N ATOM 2286 CA ASP A1127 12.801 -16.985 35.152 1.00105.65 C ANISOU 2286 CA ASP A1127 12891 13805 13446 -4403 350 -1159 C ATOM 2287 C ASP A1127 13.638 -18.034 35.873 1.00102.58 C ANISOU 2287 C ASP A1127 13044 13002 12929 -4604 661 -828 C ATOM 2288 O ASP A1127 14.085 -17.819 37.005 1.00 97.10 O ANISOU 2288 O ASP A1127 12362 12413 12117 -4531 958 -598 O ATOM 2289 CB ASP A1127 11.355 -17.458 34.988 1.00113.14 C ANISOU 2289 CB ASP A1127 13346 15002 14642 -4937 260 -1403 C ATOM 2290 N GLU A1128 13.877 -19.175 35.221 1.00105.05 N ANISOU 2290 N GLU A1128 13834 12818 13263 -4840 560 -812 N ATOM 2291 CA GLU A1128 14.589 -20.266 35.881 1.00101.37 C ANISOU 2291 CA GLU A1128 13890 11878 12749 -5036 788 -497 C ATOM 2292 C GLU A1128 16.064 -19.940 36.072 1.00 98.59 C ANISOU 2292 C GLU A1128 13939 11292 12227 -4482 856 -278 C ATOM 2293 O GLU A1128 16.652 -20.294 37.101 1.00 98.75 O ANISOU 2293 O GLU A1128 14183 11164 12175 -4507 1075 48 O ATOM 2294 CB GLU A1128 14.433 -21.557 35.083 1.00102.72 C ANISOU 2294 CB GLU A1128 14465 11516 13047 -5400 625 -601 C ATOM 2295 CG GLU A1128 13.004 -22.014 34.909 1.00109.16 C ANISOU 2295 CG GLU A1128 14894 12518 14063 -6031 538 -807 C ATOM 2296 CD GLU A1128 12.920 -23.465 34.496 1.00117.05 C ANISOU 2296 CD GLU A1128 16374 12895 15205 -6501 444 -827 C ATOM 2297 OE1 GLU A1128 13.445 -24.324 35.236 1.00119.18 O ANISOU 2297 OE1 GLU A1128 17078 12716 15487 -6681 639 -499 O ATOM 2298 OE2 GLU A1128 12.343 -23.744 33.426 1.00122.20 O ANISOU 2298 OE2 GLU A1128 16997 13477 15956 -6685 137 -1171 O ATOM 2299 N ALA A1129 16.686 -19.280 35.090 1.00106.39 N ANISOU 2299 N ALA A1129 15026 12259 13140 -4007 658 -438 N ATOM 2300 CA ALA A1129 18.089 -18.904 35.232 1.00 98.44 C ANISOU 2300 CA ALA A1129 14315 11087 12002 -3503 734 -256 C ATOM 2301 C ALA A1129 18.313 -18.065 36.481 1.00 99.96 C ANISOU 2301 C ALA A1129 14247 11624 12110 -3345 925 -40 C ATOM 2302 O ALA A1129 19.394 -18.111 37.080 1.00 91.71 O ANISOU 2302 O ALA A1129 13458 10403 10986 -3100 1037 208 O ATOM 2303 CB ALA A1129 18.562 -18.146 33.991 1.00 90.27 C ANISOU 2303 CB ALA A1129 13335 10100 10864 -3097 524 -462 C ATOM 2304 N ALA A1130 17.300 -17.301 36.894 1.00101.90 N ANISOU 2304 N ALA A1130 13969 12366 12382 -3472 950 -165 N ATOM 2305 CA ALA A1130 17.396 -16.557 38.143 1.00100.47 C ANISOU 2305 CA ALA A1130 13541 12535 12097 -3370 1159 -30 C ATOM 2306 C ALA A1130 17.236 -17.478 39.344 1.00 96.24 C ANISOU 2306 C ALA A1130 13135 11951 11481 -3804 1437 243 C ATOM 2307 O ALA A1130 17.958 -17.340 40.339 1.00 91.99 O ANISOU 2307 O ALA A1130 12752 11434 10767 -3682 1586 498 O ATOM 2308 CB ALA A1130 16.348 -15.446 38.172 1.00102.74 C ANISOU 2308 CB ALA A1130 13205 13359 12471 -3324 1106 -319 C ATOM 2309 N VAL A1131 16.303 -18.428 39.267 1.00 92.07 N ANISOU 2309 N VAL A1131 12568 11350 11062 -4347 1484 213 N ATOM 2310 CA VAL A1131 16.030 -19.294 40.409 1.00 92.71 C ANISOU 2310 CA VAL A1131 12779 11404 11044 -4858 1755 513 C ATOM 2311 C VAL A1131 17.210 -20.220 40.681 1.00 93.11 C ANISOU 2311 C VAL A1131 13506 10845 11028 -4781 1726 899 C ATOM 2312 O VAL A1131 17.533 -20.509 41.839 1.00 94.49 O ANISOU 2312 O VAL A1131 13879 11018 11005 -4935 1900 1255 O ATOM 2313 CB VAL A1131 14.728 -20.083 40.179 1.00 91.93 C ANISOU 2313 CB VAL A1131 12455 11353 11120 -5514 1797 386 C ATOM 2314 N ASN A1132 17.877 -20.696 39.626 1.00 98.73 N ANISOU 2314 N ASN A1132 14580 11039 11893 -4528 1494 823 N ATOM 2315 CA ASN A1132 19.028 -21.572 39.827 1.00 99.57 C ANISOU 2315 CA ASN A1132 15279 10537 12016 -4371 1439 1132 C ATOM 2316 C ASN A1132 20.208 -20.804 40.407 1.00 98.88 C ANISOU 2316 C ASN A1132 15239 10564 11768 -3840 1452 1311 C ATOM 2317 O ASN A1132 20.866 -21.282 41.338 1.00106.13 O ANISOU 2317 O ASN A1132 16469 11262 12593 -3844 1482 1689 O ATOM 2318 CB ASN A1132 19.417 -22.244 38.508 1.00100.70 C ANISOU 2318 CB ASN A1132 15748 10141 12372 -4206 1226 906 C ATOM 2319 CG ASN A1132 20.355 -23.432 38.702 1.00102.63 C ANISOU 2319 CG ASN A1132 16592 9660 12743 -4136 1159 1173 C ATOM 2320 OD1 ASN A1132 21.259 -23.402 39.538 1.00 99.29 O ANISOU 2320 OD1 ASN A1132 16345 9141 12242 -3883 1185 1501 O ATOM 2321 ND2 ASN A1132 20.136 -24.489 37.929 1.00107.31 N ANISOU 2321 ND2 ASN A1132 17502 9719 13554 -4348 1034 1014 N ATOM 2322 N LEU A1133 20.483 -19.606 39.881 1.00 85.10 N ANISOU 2322 N LEU A1133 13195 9149 9988 -3405 1394 1062 N ATOM 2323 CA LEU A1133 21.652 -18.849 40.317 1.00 79.83 C ANISOU 2323 CA LEU A1133 12558 8566 9209 -2920 1377 1196 C ATOM 2324 C LEU A1133 21.591 -18.470 41.792 1.00 85.06 C ANISOU 2324 C LEU A1133 13112 9576 9629 -3048 1529 1445 C ATOM 2325 O LEU A1133 22.638 -18.221 42.399 1.00 82.43 O ANISOU 2325 O LEU A1133 12927 9198 9193 -2748 1484 1656 O ATOM 2326 CB LEU A1133 21.813 -17.596 39.454 1.00 84.72 C ANISOU 2326 CB LEU A1133 12879 9469 9842 -2527 1283 893 C ATOM 2327 CG LEU A1133 22.459 -17.798 38.079 1.00 88.21 C ANISOU 2327 CG LEU A1133 13529 9583 10405 -2245 1143 716 C ATOM 2328 CD1 LEU A1133 22.334 -16.537 37.242 1.00 90.94 C ANISOU 2328 CD1 LEU A1133 13587 10258 10710 -1997 1039 463 C ATOM 2329 CD2 LEU A1133 23.920 -18.203 38.219 1.00 83.43 C ANISOU 2329 CD2 LEU A1133 13242 8615 9844 -1895 1135 911 C ATOM 2330 N ALA A1134 20.399 -18.433 42.386 1.00 84.49 N ANISOU 2330 N ALA A1134 12774 9880 9449 -3501 1713 1404 N ATOM 2331 CA ALA A1134 20.263 -18.129 43.804 1.00 83.30 C ANISOU 2331 CA ALA A1134 12544 10115 8992 -3684 1912 1604 C ATOM 2332 C ALA A1134 20.570 -19.322 44.697 1.00 95.28 C ANISOU 2332 C ALA A1134 14547 11297 10359 -4027 1952 2087 C ATOM 2333 O ALA A1134 20.536 -19.181 45.925 1.00100.46 O ANISOU 2333 O ALA A1134 15234 12260 10675 -4222 2106 2315 O ATOM 2334 CB ALA A1134 18.855 -17.614 44.103 1.00 88.70 C ANISOU 2334 CB ALA A1134 12701 11389 9612 -4038 2147 1331 C ATOM 2335 N LYS A1135 20.860 -20.486 44.116 1.00 88.10 N ANISOU 2335 N LYS A1135 14044 9751 9678 -4109 1800 2243 N ATOM 2336 CA LYS A1135 21.205 -21.680 44.871 1.00 87.20 C ANISOU 2336 CA LYS A1135 14461 9179 9491 -4398 1755 2737 C ATOM 2337 C LYS A1135 22.701 -21.967 44.852 1.00 86.32 C ANISOU 2337 C LYS A1135 14744 8566 9488 -3866 1479 2966 C ATOM 2338 O LYS A1135 23.109 -23.103 45.109 1.00102.38 O ANISOU 2338 O LYS A1135 17270 10011 11619 -3979 1327 3328 O ATOM 2339 CB LYS A1135 20.432 -22.884 44.332 1.00 91.82 C ANISOU 2339 CB LYS A1135 15253 9320 10313 -4902 1752 2756 C ATOM 2340 N SER A1136 23.523 -20.968 44.553 1.00 82.36 N ANISOU 2340 N SER A1136 14022 8267 9005 -3296 1395 2765 N ATOM 2341 CA SER A1136 24.959 -21.160 44.431 1.00 83.52 C ANISOU 2341 CA SER A1136 14419 8004 9312 -2765 1149 2911 C ATOM 2342 C SER A1136 25.684 -20.619 45.656 1.00 88.67 C ANISOU 2342 C SER A1136 15092 8930 9667 -2607 1075 3205 C ATOM 2343 O SER A1136 25.148 -19.816 46.424 1.00 92.03 O ANISOU 2343 O SER A1136 15281 9935 9752 -2806 1240 3175 O ATOM 2344 CB SER A1136 25.494 -20.477 43.171 1.00 79.24 C ANISOU 2344 CB SER A1136 13626 7476 9007 -2270 1101 2495 C ATOM 2345 OG SER A1136 25.423 -19.068 43.285 1.00 73.97 O ANISOU 2345 OG SER A1136 12540 7401 8165 -2108 1183 2288 O ATOM 2346 N ARG A1137 26.926 -21.078 45.832 1.00 91.39 N ANISOU 2346 N ARG A1137 15712 8855 10158 -2229 806 3459 N ATOM 2347 CA ARG A1137 27.767 -20.540 46.894 1.00 91.41 C ANISOU 2347 CA ARG A1137 15721 9100 9909 -2019 652 3712 C ATOM 2348 C ARG A1137 28.177 -19.101 46.613 1.00 85.85 C ANISOU 2348 C ARG A1137 14558 8882 9179 -1656 695 3357 C ATOM 2349 O ARG A1137 28.655 -18.413 47.521 1.00 85.58 O ANISOU 2349 O ARG A1137 14453 9182 8883 -1561 604 3470 O ATOM 2350 CB ARG A1137 29.009 -21.414 47.089 1.00 94.63 C ANISOU 2350 CB ARG A1137 16484 8915 10557 -1666 293 4057 C ATOM 2351 N TRP A1138 28.013 -18.639 45.372 1.00 85.61 N ANISOU 2351 N TRP A1138 14253 8876 9400 -1476 803 2943 N ATOM 2352 CA TRP A1138 28.240 -17.235 45.053 1.00 83.05 C ANISOU 2352 CA TRP A1138 13523 8984 9049 -1214 846 2628 C ATOM 2353 C TRP A1138 27.118 -16.360 45.596 1.00 83.65 C ANISOU 2353 C TRP A1138 13343 9618 8821 -1522 1044 2460 C ATOM 2354 O TRP A1138 27.378 -15.303 46.181 1.00 74.31 O ANISOU 2354 O TRP A1138 11960 8813 7461 -1395 1022 2377 O ATOM 2355 CB TRP A1138 28.387 -17.069 43.541 1.00 81.72 C ANISOU 2355 CB TRP A1138 13205 8653 9191 -970 885 2291 C ATOM 2356 CG TRP A1138 28.200 -15.675 43.038 1.00 80.37 C ANISOU 2356 CG TRP A1138 12659 8893 8984 -845 952 1971 C ATOM 2357 CD1 TRP A1138 29.008 -14.601 43.270 1.00 79.75 C ANISOU 2357 CD1 TRP A1138 12375 9046 8880 -571 866 1931 C ATOM 2358 CD2 TRP A1138 27.151 -15.209 42.179 1.00 79.40 C ANISOU 2358 CD2 TRP A1138 12339 8950 8882 -990 1065 1659 C ATOM 2359 NE1 TRP A1138 28.520 -13.492 42.620 1.00 74.10 N ANISOU 2359 NE1 TRP A1138 11385 8600 8171 -543 925 1634 N ATOM 2360 CE2 TRP A1138 27.381 -13.840 41.944 1.00 77.74 C ANISOU 2360 CE2 TRP A1138 11841 9040 8657 -775 1031 1470 C ATOM 2361 CE3 TRP A1138 26.036 -15.814 41.592 1.00 70.14 C ANISOU 2361 CE3 TRP A1138 11201 7697 7754 -1292 1152 1527 C ATOM 2362 CZ2 TRP A1138 26.539 -13.069 41.149 1.00 75.61 C ANISOU 2362 CZ2 TRP A1138 11345 8968 8416 -815 1054 1185 C ATOM 2363 CZ3 TRP A1138 25.201 -15.044 40.801 1.00 72.99 C ANISOU 2363 CZ3 TRP A1138 11290 8307 8136 -1332 1174 1217 C ATOM 2364 CH2 TRP A1138 25.457 -13.689 40.588 1.00 72.54 C ANISOU 2364 CH2 TRP A1138 10974 8524 8064 -1078 1113 1063 C ATOM 2365 N TYR A1139 25.867 -16.790 45.424 1.00 82.65 N ANISOU 2365 N TYR A1139 13198 9549 8658 -1927 1233 2375 N ATOM 2366 CA TYR A1139 24.743 -16.053 45.987 1.00 86.12 C ANISOU 2366 CA TYR A1139 13337 10541 8845 -2219 1452 2182 C ATOM 2367 C TYR A1139 24.771 -16.040 47.509 1.00 83.42 C ANISOU 2367 C TYR A1139 13129 10492 8073 -2444 1516 2445 C ATOM 2368 O TYR A1139 24.214 -15.122 48.120 1.00 85.20 O ANISOU 2368 O TYR A1139 13075 11244 8055 -2528 1680 2223 O ATOM 2369 CB TYR A1139 23.424 -16.647 45.483 1.00 93.06 C ANISOU 2369 CB TYR A1139 14126 11418 9815 -2639 1632 2048 C ATOM 2370 CG TYR A1139 22.187 -15.947 45.998 1.00 97.27 C ANISOU 2370 CG TYR A1139 14256 12545 10156 -2931 1887 1793 C ATOM 2371 CD1 TYR A1139 21.714 -14.791 45.393 1.00 97.09 C ANISOU 2371 CD1 TYR A1139 13784 12829 10275 -2703 1891 1360 C ATOM 2372 CD2 TYR A1139 21.487 -16.449 47.086 1.00101.31 C ANISOU 2372 CD2 TYR A1139 14831 13310 10352 -3435 2125 1984 C ATOM 2373 CE1 TYR A1139 20.582 -14.152 45.862 1.00 98.45 C ANISOU 2373 CE1 TYR A1139 13534 13534 10340 -2906 2113 1072 C ATOM 2374 CE2 TYR A1139 20.357 -15.817 47.560 1.00102.23 C ANISOU 2374 CE2 TYR A1139 14515 14020 10307 -3689 2412 1691 C ATOM 2375 CZ TYR A1139 19.909 -14.671 46.946 1.00 98.03 C ANISOU 2375 CZ TYR A1139 13492 13774 9981 -3392 2400 1210 C ATOM 2376 OH TYR A1139 18.781 -14.044 47.424 1.00 96.25 O ANISOU 2376 OH TYR A1139 12784 14130 9656 -3586 2677 868 O ATOM 2377 N ASN A1140 25.410 -17.028 48.134 1.00 84.98 N ANISOU 2377 N ASN A1140 13766 10358 8165 -2531 1372 2902 N ATOM 2378 CA ASN A1140 25.511 -17.069 49.585 1.00 81.09 C ANISOU 2378 CA ASN A1140 13485 10139 7189 -2767 1384 3212 C ATOM 2379 C ASN A1140 26.720 -16.316 50.123 1.00 81.14 C ANISOU 2379 C ASN A1140 13495 10255 7081 -2354 1121 3259 C ATOM 2380 O ASN A1140 26.732 -15.963 51.308 1.00 91.34 O ANISOU 2380 O ASN A1140 14868 11933 7905 -2514 1139 3371 O ATOM 2381 CB ASN A1140 25.564 -18.521 50.073 1.00 83.93 C ANISOU 2381 CB ASN A1140 14351 10066 7474 -3090 1289 3738 C ATOM 2382 CG ASN A1140 24.263 -19.268 49.834 1.00 88.69 C ANISOU 2382 CG ASN A1140 14898 10646 8154 -3583 1553 3682 C ATOM 2383 OD1 ASN A1140 23.328 -19.182 50.631 1.00 94.13 O ANISOU 2383 OD1 ASN A1140 15427 11795 8542 -3964 1814 3633 O ATOM 2384 ND2 ASN A1140 24.203 -20.015 48.739 1.00 88.26 N ANISOU 2384 ND2 ASN A1140 14971 10056 8508 -3583 1485 3663 N ATOM 2385 N GLN A1141 27.731 -16.058 49.292 1.00 79.05 N ANISOU 2385 N GLN A1141 13135 9692 7209 -1861 889 3159 N ATOM 2386 CA GLN A1141 28.944 -15.389 49.751 1.00 83.34 C ANISOU 2386 CA GLN A1141 13640 10316 7710 -1493 612 3207 C ATOM 2387 C GLN A1141 28.857 -13.872 49.622 1.00 86.83 C ANISOU 2387 C GLN A1141 13669 11193 8130 -1321 691 2761 C ATOM 2388 O GLN A1141 29.270 -13.148 50.534 1.00 90.33 O ANISOU 2388 O GLN A1141 14085 11948 8290 -1274 578 2742 O ATOM 2389 CB GLN A1141 30.158 -15.908 48.974 1.00 81.76 C ANISOU 2389 CB GLN A1141 13505 9595 7966 -1066 339 3330 C ATOM 2390 N THR A1142 28.341 -13.378 48.497 1.00 81.15 N ANISOU 2390 N THR A1142 12660 10468 7708 -1228 841 2404 N ATOM 2391 CA THR A1142 28.099 -11.952 48.276 1.00 75.62 C ANISOU 2391 CA THR A1142 11594 10099 7040 -1081 896 1987 C ATOM 2392 C THR A1142 26.654 -11.815 47.825 1.00 80.15 C ANISOU 2392 C THR A1142 11953 10861 7638 -1313 1170 1698 C ATOM 2393 O THR A1142 26.373 -11.645 46.629 1.00 76.21 O ANISOU 2393 O THR A1142 11292 10208 7456 -1195 1180 1504 O ATOM 2394 CB THR A1142 29.064 -11.368 47.245 1.00 71.01 C ANISOU 2394 CB THR A1142 10854 9291 6836 -689 721 1873 C ATOM 2395 OG1 THR A1142 28.852 -12.004 45.979 1.00 61.90 O ANISOU 2395 OG1 THR A1142 9720 7819 5981 -656 792 1847 O ATOM 2396 CG2 THR A1142 30.507 -11.581 47.678 1.00 64.20 C ANISOU 2396 CG2 THR A1142 10120 8261 6011 -463 447 2144 C ATOM 2397 N PRO A1143 25.702 -11.890 48.760 1.00 78.66 N ANISOU 2397 N PRO A1143 11743 11039 7106 -1659 1396 1658 N ATOM 2398 CA PRO A1143 24.288 -11.947 48.355 1.00 77.44 C ANISOU 2398 CA PRO A1143 11332 11073 7019 -1917 1663 1400 C ATOM 2399 C PRO A1143 23.754 -10.645 47.786 1.00 81.38 C ANISOU 2399 C PRO A1143 11396 11793 7731 -1681 1672 913 C ATOM 2400 O PRO A1143 22.964 -10.679 46.836 1.00 67.23 O ANISOU 2400 O PRO A1143 9390 9947 6208 -1709 1715 723 O ATOM 2401 CB PRO A1143 23.575 -12.337 49.655 1.00 74.02 C ANISOU 2401 CB PRO A1143 10976 11033 6115 -2363 1931 1502 C ATOM 2402 CG PRO A1143 24.484 -11.856 50.733 1.00 74.95 C ANISOU 2402 CG PRO A1143 11275 11318 5883 -2235 1792 1614 C ATOM 2403 CD PRO A1143 25.873 -12.037 50.213 1.00 80.85 C ANISOU 2403 CD PRO A1143 12236 11590 6893 -1870 1423 1866 C ATOM 2404 N ASN A1144 24.148 -9.498 48.346 1.00 79.84 N ANISOU 2404 N ASN A1144 11080 11820 7435 -1453 1593 702 N ATOM 2405 CA ASN A1144 23.656 -8.219 47.839 1.00 82.18 C ANISOU 2405 CA ASN A1144 11000 12248 7977 -1203 1550 249 C ATOM 2406 C ASN A1144 24.024 -8.031 46.372 1.00 83.32 C ANISOU 2406 C ASN A1144 11122 12002 8536 -947 1323 262 C ATOM 2407 O ASN A1144 23.168 -7.712 45.538 1.00 77.89 O ANISOU 2407 O ASN A1144 10184 11322 8089 -907 1317 25 O ATOM 2408 CB ASN A1144 24.209 -7.072 48.683 1.00 86.17 C ANISOU 2408 CB ASN A1144 11466 12947 8328 -999 1448 44 C ATOM 2409 CG ASN A1144 23.399 -6.831 49.942 1.00 91.58 C ANISOU 2409 CG ASN A1144 12020 14149 8626 -1210 1730 -220 C ATOM 2410 OD1 ASN A1144 22.445 -6.054 49.938 1.00 89.43 O ANISOU 2410 OD1 ASN A1144 11378 14135 8467 -1137 1861 -680 O ATOM 2411 ND2 ASN A1144 23.778 -7.496 51.028 1.00 95.06 N ANISOU 2411 ND2 ASN A1144 12763 14756 8600 -1466 1818 62 N ATOM 2412 N ARG A1145 25.302 -8.228 46.040 1.00 83.54 N ANISOU 2412 N ARG A1145 11397 11711 8633 -780 1132 536 N ATOM 2413 CA ARG A1145 25.740 -8.103 44.655 1.00 77.75 C ANISOU 2413 CA ARG A1145 10673 10652 8215 -579 973 561 C ATOM 2414 C ARG A1145 25.101 -9.167 43.774 1.00 76.82 C ANISOU 2414 C ARG A1145 10624 10365 8200 -753 1062 630 C ATOM 2415 O ARG A1145 24.721 -8.887 42.631 1.00 82.58 O ANISOU 2415 O ARG A1145 11252 10993 9130 -675 981 488 O ATOM 2416 CB ARG A1145 27.264 -8.189 44.587 1.00 73.67 C ANISOU 2416 CB ARG A1145 10353 9896 7744 -393 814 816 C ATOM 2417 CG ARG A1145 27.829 -8.227 43.179 1.00 69.75 C ANISOU 2417 CG ARG A1145 9893 9104 7505 -234 729 865 C ATOM 2418 CD ARG A1145 29.352 -8.232 43.189 1.00 73.59 C ANISOU 2418 CD ARG A1145 10468 9428 8064 -50 612 1067 C ATOM 2419 NE ARG A1145 29.897 -8.135 41.837 1.00 80.75 N ANISOU 2419 NE ARG A1145 11375 10131 9175 79 594 1070 N ATOM 2420 CZ ARG A1145 31.175 -7.901 41.556 1.00 82.83 C ANISOU 2420 CZ ARG A1145 11612 10298 9561 237 528 1175 C ATOM 2421 NH1 ARG A1145 32.054 -7.734 42.535 1.00 82.57 N ANISOU 2421 NH1 ARG A1145 11535 10328 9508 307 415 1287 N ATOM 2422 NH2 ARG A1145 31.574 -7.829 40.293 1.00 85.74 N ANISOU 2422 NH2 ARG A1145 11982 10541 10053 302 578 1158 N ATOM 2423 N ALA A1146 24.974 -10.393 44.287 1.00 78.38 N ANISOU 2423 N ALA A1146 11025 10507 8249 -1011 1196 857 N ATOM 2424 CA ALA A1146 24.412 -11.480 43.491 1.00 77.28 C ANISOU 2424 CA ALA A1146 10992 10148 8224 -1212 1259 913 C ATOM 2425 C ALA A1146 22.965 -11.191 43.114 1.00 83.69 C ANISOU 2425 C ALA A1146 11482 11202 9113 -1389 1341 610 C ATOM 2426 O ALA A1146 22.575 -11.340 41.951 1.00 81.20 O ANISOU 2426 O ALA A1146 11127 10738 8988 -1380 1252 495 O ATOM 2427 CB ALA A1146 24.519 -12.800 44.253 1.00 75.31 C ANISOU 2427 CB ALA A1146 11049 9751 7813 -1491 1359 1239 C ATOM 2428 N LYS A1147 22.154 -10.771 44.090 1.00 81.29 N ANISOU 2428 N LYS A1147 10927 11303 8657 -1547 1506 451 N ATOM 2429 CA LYS A1147 20.760 -10.442 43.804 1.00 80.52 C ANISOU 2429 CA LYS A1147 10420 11486 8686 -1680 1585 116 C ATOM 2430 C LYS A1147 20.649 -9.302 42.799 1.00 83.83 C ANISOU 2430 C LYS A1147 10611 11866 9377 -1325 1329 -152 C ATOM 2431 O LYS A1147 19.710 -9.273 41.995 1.00 68.30 O ANISOU 2431 O LYS A1147 8403 9940 7609 -1375 1246 -350 O ATOM 2432 CB LYS A1147 20.023 -10.088 45.098 1.00 67.35 C ANISOU 2432 CB LYS A1147 8483 10311 6797 -1863 1853 -63 C ATOM 2433 N ARG A1148 21.599 -8.365 42.815 1.00 85.54 N ANISOU 2433 N ARG A1148 10910 11984 9606 -988 1167 -140 N ATOM 2434 CA ARG A1148 21.574 -7.277 41.842 1.00 79.68 C ANISOU 2434 CA ARG A1148 10031 11139 9107 -685 892 -317 C ATOM 2435 C ARG A1148 21.891 -7.783 40.437 1.00 82.33 C ANISOU 2435 C ARG A1148 10589 11152 9539 -673 733 -165 C ATOM 2436 O ARG A1148 21.289 -7.330 39.457 1.00 90.33 O ANISOU 2436 O ARG A1148 11469 12136 10717 -591 526 -312 O ATOM 2437 CB ARG A1148 22.555 -6.182 42.261 1.00 70.66 C ANISOU 2437 CB ARG A1148 8952 9944 7952 -403 768 -316 C ATOM 2438 CG ARG A1148 21.892 -4.860 42.620 1.00 71.12 C ANISOU 2438 CG ARG A1148 8676 10192 8155 -198 669 -688 C ATOM 2439 CD ARG A1148 22.475 -4.260 43.892 1.00 73.19 C ANISOU 2439 CD ARG A1148 8962 10601 8247 -122 743 -769 C ATOM 2440 NE ARG A1148 23.934 -4.303 43.899 1.00 73.07 N ANISOU 2440 NE ARG A1148 9271 10346 8145 -63 641 -461 N ATOM 2441 CZ ARG A1148 24.686 -4.003 44.953 1.00 72.04 C ANISOU 2441 CZ ARG A1148 9236 10306 7829 -40 656 -444 C ATOM 2442 NH1 ARG A1148 24.121 -3.632 46.093 1.00 77.77 N ANISOU 2442 NH1 ARG A1148 9809 11363 8378 -79 795 -729 N ATOM 2443 NH2 ARG A1148 26.005 -4.075 44.867 1.00 70.75 N ANISOU 2443 NH2 ARG A1148 9301 9933 7647 15 532 -167 N ATOM 2444 N VAL A1149 22.824 -8.727 40.321 1.00 86.59 N ANISOU 2444 N VAL A1149 11473 11454 9974 -742 812 112 N ATOM 2445 CA VAL A1149 23.201 -9.252 39.011 1.00 82.53 C ANISOU 2445 CA VAL A1149 11189 10655 9513 -723 713 200 C ATOM 2446 C VAL A1149 22.160 -10.240 38.500 1.00 89.46 C ANISOU 2446 C VAL A1149 12052 11515 10424 -1007 747 112 C ATOM 2447 O VAL A1149 21.841 -10.260 37.304 1.00 88.71 O ANISOU 2447 O VAL A1149 11995 11326 10387 -1003 583 17 O ATOM 2448 CB VAL A1149 24.603 -9.881 39.089 1.00 69.15 C ANISOU 2448 CB VAL A1149 9812 8710 7751 -638 790 459 C ATOM 2449 CG1 VAL A1149 24.961 -10.583 37.793 1.00 62.41 C ANISOU 2449 CG1 VAL A1149 9197 7590 6927 -632 765 483 C ATOM 2450 CG2 VAL A1149 25.636 -8.812 39.423 1.00 65.57 C ANISOU 2450 CG2 VAL A1149 9323 8286 7303 -385 710 522 C ATOM 2451 N ILE A1150 21.606 -11.063 39.394 1.00 84.73 N ANISOU 2451 N ILE A1150 11413 11014 9767 -1295 945 151 N ATOM 2452 CA ILE A1150 20.566 -12.008 38.997 1.00 83.24 C ANISOU 2452 CA ILE A1150 11179 10809 9639 -1639 980 64 C ATOM 2453 C ILE A1150 19.315 -11.263 38.545 1.00 84.16 C ANISOU 2453 C ILE A1150 10861 11211 9905 -1651 831 -246 C ATOM 2454 O ILE A1150 18.622 -11.692 37.612 1.00 93.69 O ANISOU 2454 O ILE A1150 12028 12360 11209 -1807 688 -369 O ATOM 2455 CB ILE A1150 20.272 -12.986 40.152 1.00 84.83 C ANISOU 2455 CB ILE A1150 11442 11060 9730 -2003 1240 225 C ATOM 2456 CG1 ILE A1150 21.486 -13.878 40.414 1.00 82.12 C ANISOU 2456 CG1 ILE A1150 11568 10333 9299 -1964 1285 553 C ATOM 2457 CG2 ILE A1150 19.059 -13.839 39.844 1.00 86.81 C ANISOU 2457 CG2 ILE A1150 11564 11344 10076 -2432 1287 113 C ATOM 2458 CD1 ILE A1150 21.367 -14.717 41.663 1.00 70.60 C ANISOU 2458 CD1 ILE A1150 10253 8891 7682 -2294 1484 806 C ATOM 2459 N THR A1151 19.009 -10.131 39.188 1.00 79.62 N ANISOU 2459 N THR A1151 9946 10934 9371 -1467 829 -404 N ATOM 2460 CA THR A1151 17.920 -9.283 38.713 1.00 85.27 C ANISOU 2460 CA THR A1151 10223 11875 10301 -1363 618 -716 C ATOM 2461 C THR A1151 18.194 -8.785 37.302 1.00 88.73 C ANISOU 2461 C THR A1151 10820 12078 10815 -1128 245 -709 C ATOM 2462 O THR A1151 17.290 -8.744 36.460 1.00 89.80 O ANISOU 2462 O THR A1151 10761 12268 11090 -1177 -2 -876 O ATOM 2463 CB THR A1151 17.713 -8.098 39.655 1.00 85.11 C ANISOU 2463 CB THR A1151 9861 12141 10338 -1127 668 -919 C ATOM 2464 OG1 THR A1151 17.364 -8.577 40.957 1.00 90.34 O ANISOU 2464 OG1 THR A1151 10377 13098 10849 -1398 1046 -947 O ATOM 2465 CG2 THR A1151 16.602 -7.194 39.144 1.00 80.06 C ANISOU 2465 CG2 THR A1151 8743 11680 9998 -942 398 -1262 C ATOM 2466 N THR A1152 19.440 -8.402 37.023 1.00 89.05 N ANISOU 2466 N THR A1152 11208 11880 10745 -898 191 -508 N ATOM 2467 CA THR A1152 19.772 -7.948 35.679 1.00 88.03 C ANISOU 2467 CA THR A1152 11283 11556 10607 -736 -114 -459 C ATOM 2468 C THR A1152 19.666 -9.080 34.665 1.00 84.57 C ANISOU 2468 C THR A1152 11105 10963 10066 -967 -143 -432 C ATOM 2469 O THR A1152 19.276 -8.846 33.516 1.00 88.93 O ANISOU 2469 O THR A1152 11704 11483 10603 -948 -442 -501 O ATOM 2470 CB THR A1152 21.170 -7.335 35.670 1.00 84.93 C ANISOU 2470 CB THR A1152 11169 10986 10115 -508 -96 -248 C ATOM 2471 OG1 THR A1152 21.238 -6.314 36.674 1.00 87.26 O ANISOU 2471 OG1 THR A1152 11240 11404 10511 -322 -88 -315 O ATOM 2472 CG2 THR A1152 21.473 -6.721 34.321 1.00 75.79 C ANISOU 2472 CG2 THR A1152 10215 9677 8903 -385 -386 -175 C ATOM 2473 N PHE A1153 19.988 -10.311 35.069 1.00 80.31 N ANISOU 2473 N PHE A1153 10763 10305 9447 -1189 130 -341 N ATOM 2474 CA PHE A1153 19.838 -11.445 34.163 1.00 86.85 C ANISOU 2474 CA PHE A1153 11850 10938 10209 -1417 102 -378 C ATOM 2475 C PHE A1153 18.375 -11.753 33.876 1.00 94.28 C ANISOU 2475 C PHE A1153 12493 12048 11280 -1692 -61 -605 C ATOM 2476 O PHE A1153 18.051 -12.271 32.802 1.00 97.03 O ANISOU 2476 O PHE A1153 13001 12289 11578 -1834 -250 -712 O ATOM 2477 CB PHE A1153 20.524 -12.681 34.744 1.00 85.98 C ANISOU 2477 CB PHE A1153 12033 10584 10052 -1564 394 -224 C ATOM 2478 CG PHE A1153 21.973 -12.790 34.388 1.00 82.81 C ANISOU 2478 CG PHE A1153 11993 9932 9541 -1323 479 -73 C ATOM 2479 CD1 PHE A1153 22.400 -12.549 33.096 1.00 87.89 C ANISOU 2479 CD1 PHE A1153 12840 10494 10062 -1196 348 -140 C ATOM 2480 CD2 PHE A1153 22.908 -13.132 35.345 1.00 77.41 C ANISOU 2480 CD2 PHE A1153 11425 9126 8862 -1234 685 132 C ATOM 2481 CE1 PHE A1153 23.735 -12.650 32.764 1.00 85.44 C ANISOU 2481 CE1 PHE A1153 12792 10012 9660 -991 485 -39 C ATOM 2482 CE2 PHE A1153 24.244 -13.233 35.021 1.00 77.07 C ANISOU 2482 CE2 PHE A1153 11625 8883 8776 -993 759 238 C ATOM 2483 CZ PHE A1153 24.658 -12.992 33.729 1.00 80.39 C ANISOU 2483 CZ PHE A1153 12194 9251 9099 -874 690 135 C ATOM 2484 N ARG A1154 17.484 -11.446 34.817 1.00 88.53 N ANISOU 2484 N ARG A1154 11311 11612 10713 -1783 15 -710 N ATOM 2485 CA ARG A1154 16.070 -11.771 34.679 1.00 90.56 C ANISOU 2485 CA ARG A1154 11175 12087 11146 -2076 -96 -944 C ATOM 2486 C ARG A1154 15.287 -10.657 33.990 1.00 94.08 C ANISOU 2486 C ARG A1154 11255 12736 11753 -1845 -507 -1151 C ATOM 2487 O ARG A1154 14.589 -10.908 33.004 1.00 98.43 O ANISOU 2487 O ARG A1154 11752 13292 12353 -1977 -823 -1290 O ATOM 2488 CB ARG A1154 15.471 -12.072 36.056 1.00 91.66 C ANISOU 2488 CB ARG A1154 10967 12492 11368 -2333 250 -973 C ATOM 2489 CG ARG A1154 13.953 -12.110 36.087 1.00 98.75 C ANISOU 2489 CG ARG A1154 11273 13741 12505 -2600 179 -1261 C ATOM 2490 CD ARG A1154 13.450 -12.527 37.460 1.00 98.15 C ANISOU 2490 CD ARG A1154 10903 13957 12432 -2937 616 -1264 C ATOM 2491 NE ARG A1154 14.141 -11.809 38.526 1.00 96.23 N ANISOU 2491 NE ARG A1154 10691 13830 12042 -2666 855 -1169 N ATOM 2492 CZ ARG A1154 13.729 -10.656 39.043 1.00 99.35 C ANISOU 2492 CZ ARG A1154 10627 14571 12550 -2384 862 -1413 C ATOM 2493 NH1 ARG A1154 12.618 -10.085 38.594 1.00102.81 N1+ ANISOU 2493 NH1 ARG A1154 10503 15271 13290 -2299 634 -1752 N1+ ATOM 2494 NH2 ARG A1154 14.426 -10.074 40.011 1.00 97.58 N ANISOU 2494 NH2 ARG A1154 10500 14418 12157 -2171 1067 -1343 N ATOM 2495 N THR A1155 15.394 -9.425 34.492 1.00 91.70 N ANISOU 2495 N THR A1155 10720 12575 11545 -1493 -553 -1180 N ATOM 2496 CA THR A1155 14.626 -8.327 33.913 1.00 95.66 C ANISOU 2496 CA THR A1155 10869 13211 12265 -1227 -991 -1368 C ATOM 2497 C THR A1155 15.189 -7.887 32.570 1.00 97.84 C ANISOU 2497 C THR A1155 11567 13229 12380 -1038 -1391 -1215 C ATOM 2498 O THR A1155 14.426 -7.500 31.678 1.00103.63 O ANISOU 2498 O THR A1155 12148 14011 13216 -975 -1852 -1325 O ATOM 2499 CB THR A1155 14.590 -7.135 34.871 1.00 96.53 C ANISOU 2499 CB THR A1155 10639 13482 12554 -890 -932 -1480 C ATOM 2500 OG1 THR A1155 15.865 -6.481 34.875 1.00 89.26 O ANISOU 2500 OG1 THR A1155 10139 12306 11469 -624 -926 -1243 O ATOM 2501 CG2 THR A1155 14.254 -7.597 36.282 1.00102.13 C ANISOU 2501 CG2 THR A1155 11038 14480 13285 -1108 -443 -1599 C ATOM 2502 N GLY A1156 16.506 -7.938 32.402 1.00 98.59 N ANISOU 2502 N GLY A1156 12176 13074 12209 -961 -1232 -958 N ATOM 2503 CA GLY A1156 17.109 -7.426 31.192 1.00 97.17 C ANISOU 2503 CA GLY A1156 12393 12702 11824 -813 -1538 -796 C ATOM 2504 C GLY A1156 17.208 -5.922 31.139 1.00 94.99 C ANISOU 2504 C GLY A1156 12028 12391 11674 -459 -1843 -727 C ATOM 2505 O GLY A1156 17.414 -5.364 30.057 1.00 94.83 O ANISOU 2505 O GLY A1156 12287 12241 11502 -370 -2199 -582 O ATOM 2506 N THR A1157 17.055 -5.243 32.275 1.00 98.59 N ANISOU 2506 N THR A1157 12130 12944 12386 -269 -1724 -831 N ATOM 2507 CA THR A1157 17.188 -3.793 32.334 1.00 99.99 C ANISOU 2507 CA THR A1157 12241 13012 12740 83 -2014 -798 C ATOM 2508 C THR A1157 18.117 -3.396 33.475 1.00 95.58 C ANISOU 2508 C THR A1157 11722 12408 12187 197 -1666 -741 C ATOM 2509 O THR A1157 18.739 -4.258 34.103 1.00 99.83 O ANISOU 2509 O THR A1157 12385 12993 12552 13 -1238 -673 O ATOM 2510 CB THR A1157 15.819 -3.130 32.503 1.00100.53 C ANISOU 2510 CB THR A1157 11744 13243 13210 283 -2359 -1106 C ATOM 2511 N TRP A1158 18.225 -2.094 33.747 1.00 93.22 N ANISOU 2511 N TRP A1158 11337 11987 12095 500 -1890 -770 N ATOM 2512 CA TRP A1158 19.077 -1.577 34.810 1.00 93.29 C ANISOU 2512 CA TRP A1158 11380 11944 12121 611 -1638 -757 C ATOM 2513 C TRP A1158 18.284 -1.180 36.050 1.00100.83 C ANISOU 2513 C TRP A1158 11839 13130 13343 767 -1520 -1143 C ATOM 2514 O TRP A1158 18.687 -0.262 36.773 1.00104.41 O ANISOU 2514 O TRP A1158 12262 13494 13913 976 -1523 -1234 O ATOM 2515 CB TRP A1158 19.888 -0.380 34.315 1.00 93.24 C ANISOU 2515 CB TRP A1158 11675 11603 12148 796 -1939 -534 C ATOM 2516 CG TRP A1158 20.831 -0.689 33.202 1.00 90.86 C ANISOU 2516 CG TRP A1158 11861 11134 11527 615 -1955 -159 C ATOM 2517 CD1 TRP A1158 20.661 -0.401 31.878 1.00 92.31 C ANISOU 2517 CD1 TRP A1158 12294 11175 11605 591 -2335 30 C ATOM 2518 CD2 TRP A1158 22.100 -1.341 33.312 1.00 84.64 C ANISOU 2518 CD2 TRP A1158 11359 10335 10467 435 -1569 52 C ATOM 2519 NE1 TRP A1158 21.746 -0.835 31.158 1.00 87.61 N ANISOU 2519 NE1 TRP A1158 12125 10516 10649 382 -2146 322 N ATOM 2520 CE2 TRP A1158 22.643 -1.417 32.015 1.00 81.33 C ANISOU 2520 CE2 TRP A1158 11324 9793 9787 307 -1675 322 C ATOM 2521 CE3 TRP A1158 22.829 -1.871 34.381 1.00 79.01 C ANISOU 2521 CE3 TRP A1158 10605 9715 9699 377 -1161 35 C ATOM 2522 CZ2 TRP A1158 23.881 -2.001 31.759 1.00 77.25 C ANISOU 2522 CZ2 TRP A1158 11088 9260 9004 149 -1343 521 C ATOM 2523 CZ3 TRP A1158 24.059 -2.452 34.124 1.00 69.87 C ANISOU 2523 CZ3 TRP A1158 9733 8502 8314 244 -903 268 C ATOM 2524 CH2 TRP A1158 24.572 -2.511 32.824 1.00 69.73 C ANISOU 2524 CH2 TRP A1158 10033 8375 8085 144 -972 482 C ATOM 2525 N ASP A1159 17.156 -1.850 36.306 1.00 98.45 N ANISOU 2525 N ASP A1159 11135 13138 13133 646 -1402 -1399 N ATOM 2526 CA ASP A1159 16.331 -1.497 37.457 1.00 97.23 C ANISOU 2526 CA ASP A1159 10456 13283 13205 769 -1227 -1814 C ATOM 2527 C ASP A1159 17.098 -1.638 38.765 1.00 90.66 C ANISOU 2527 C ASP A1159 9725 12569 12151 685 -774 -1819 C ATOM 2528 O ASP A1159 16.820 -0.916 39.727 1.00 92.33 O ANISOU 2528 O ASP A1159 9651 12933 12497 879 -679 -2146 O ATOM 2529 CB ASP A1159 15.076 -2.368 37.498 1.00105.69 C ANISOU 2529 CB ASP A1159 11073 14718 14366 540 -1095 -2046 C ATOM 2530 CG ASP A1159 14.329 -2.379 36.182 1.00109.35 C ANISOU 2530 CG ASP A1159 11447 15092 15007 573 -1581 -2031 C ATOM 2531 OD1 ASP A1159 14.839 -2.991 35.220 1.00106.95 O1+ ANISOU 2531 OD1 ASP A1159 11588 14593 14457 378 -1693 -1714 O1+ ATOM 2532 OD2 ASP A1159 13.231 -1.786 36.115 1.00113.68 O ANISOU 2532 OD2 ASP A1159 11472 15783 15940 804 -1860 -2361 O ATOM 2533 N ALA A1160 18.061 -2.558 38.822 1.00 90.75 N ANISOU 2533 N ALA A1160 10142 12514 11824 416 -516 -1483 N ATOM 2534 CA ALA A1160 18.793 -2.777 40.062 1.00 83.07 C ANISOU 2534 CA ALA A1160 9285 11661 10616 322 -147 -1445 C ATOM 2535 C ALA A1160 19.805 -1.671 40.330 1.00 83.07 C ANISOU 2535 C ALA A1160 9492 11427 10644 577 -301 -1398 C ATOM 2536 O ALA A1160 20.159 -1.427 41.488 1.00 80.26 O ANISOU 2536 O ALA A1160 9111 11213 10170 595 -98 -1520 O ATOM 2537 CB ALA A1160 19.490 -4.133 40.023 1.00 69.19 C ANISOU 2537 CB ALA A1160 7878 9858 8554 -5 110 -1098 C ATOM 2538 N TYR A1161 20.270 -0.989 39.289 1.00 85.89 N ANISOU 2538 N TYR A1161 10067 11436 11131 737 -663 -1221 N ATOM 2539 CA TYR A1161 21.312 0.021 39.439 1.00 81.29 C ANISOU 2539 CA TYR A1161 9712 10587 10590 902 -820 -1122 C ATOM 2540 C TYR A1161 20.830 1.413 39.031 1.00 86.56 C ANISOU 2540 C TYR A1161 10259 11009 11620 1221 -1257 -1309 C ATOM 2541 O TYR A1161 19.780 1.882 39.473 1.00 90.75 O ANISOU 2541 O TYR A1161 10405 11678 12398 1423 -1325 -1710 O ATOM 2542 CB TYR A1161 22.541 -0.357 38.608 1.00 78.82 C ANISOU 2542 CB TYR A1161 9822 10037 10089 757 -833 -681 C ATOM 2543 CG TYR A1161 23.144 -1.708 38.932 1.00 79.07 C ANISOU 2543 CG TYR A1161 10004 10209 9831 508 -467 -486 C ATOM 2544 CD1 TYR A1161 22.612 -2.876 38.400 1.00 78.87 C ANISOU 2544 CD1 TYR A1161 9993 10274 9701 320 -342 -427 C ATOM 2545 CD2 TYR A1161 24.263 -1.813 39.748 1.00 75.01 C ANISOU 2545 CD2 TYR A1161 9629 9697 9174 468 -297 -359 C ATOM 2546 CE1 TYR A1161 23.166 -4.110 38.683 1.00 74.50 C ANISOU 2546 CE1 TYR A1161 9613 9760 8934 118 -53 -248 C ATOM 2547 CE2 TYR A1161 24.824 -3.042 40.039 1.00 67.83 C ANISOU 2547 CE2 TYR A1161 8865 8860 8048 288 -30 -162 C ATOM 2548 CZ TYR A1161 24.272 -4.189 39.504 1.00 71.43 C ANISOU 2548 CZ TYR A1161 9359 9354 8428 123 94 -104 C ATOM 2549 OH TYR A1161 24.829 -5.416 39.787 1.00 69.66 O ANISOU 2549 OH TYR A1161 9313 9118 8037 -32 319 91 O ATOM 2550 N SER A 364 17.508 3.047 36.367 1.00104.00 N ATOM 2551 CA SER A 364 18.568 3.670 35.585 1.00104.92 C ATOM 2552 C SER A 364 18.623 3.097 34.167 1.00111.72 C ATOM 2553 O SER A 364 19.675 3.111 33.526 1.00111.66 O ATOM 2554 CB SER A 364 19.919 3.488 36.282 1.00 97.65 C ATOM 2555 N GLN A 365 17.486 2.600 33.682 1.00122.15 N ATOM 2556 CA GLN A 365 17.397 1.937 32.386 1.00115.38 C ATOM 2557 C GLN A 365 16.553 2.767 31.428 1.00110.61 C ATOM 2558 O GLN A 365 15.419 3.137 31.753 1.00 98.43 O ATOM 2559 CB GLN A 365 16.796 0.536 32.527 1.00106.22 C ATOM 2560 N GLN A 366 17.101 3.039 30.246 1.00120.06 N ATOM 2561 CA GLN A 366 16.385 3.791 29.223 1.00115.06 C ATOM 2562 C GLN A 366 15.363 2.887 28.544 1.00110.82 C ATOM 2563 O GLN A 366 15.719 1.836 27.999 1.00106.83 O ATOM 2564 CB GLN A 366 17.364 4.363 28.199 1.00114.61 C ATOM 2565 N LYS A 367 14.097 3.295 28.574 1.00106.95 N ATOM 2566 CA LYS A 367 13.014 2.529 27.974 1.00112.85 C ATOM 2567 C LYS A 367 12.771 2.895 26.516 1.00109.20 C ATOM 2568 O LYS A 367 11.803 2.410 25.921 1.00103.35 O ATOM 2569 CB LYS A 367 11.727 2.721 28.781 1.00115.42 C ATOM 2570 N GLU A 368 13.626 3.733 25.930 1.00114.20 N ATOM 2571 CA GLU A 368 13.436 4.206 24.566 1.00 99.97 C ATOM 2572 C GLU A 368 14.152 3.361 23.525 1.00100.67 C ATOM 2573 O GLU A 368 13.805 3.444 22.342 1.00 97.34 O ATOM 2574 CB GLU A 368 13.920 5.655 24.437 1.00 81.44 C ATOM 2575 CG GLU A 368 13.087 6.681 25.188 1.00 79.48 C ATOM 2576 CD GLU A 368 11.923 7.216 24.368 1.00 87.69 C ATOM 2577 OE1 GLU A 368 11.484 6.529 23.419 1.00 87.57 O ATOM 2578 OE2 GLU A 368 11.451 8.332 24.674 1.00 90.78 O ATOM 2579 N LYS A 369 15.139 2.557 23.932 1.00101.97 N ATOM 2580 CA LYS A 369 15.965 1.842 22.963 1.00 93.96 C ATOM 2581 C LYS A 369 15.123 0.959 22.051 1.00 87.89 C ATOM 2582 O LYS A 369 15.377 0.886 20.844 1.00 84.82 O ATOM 2583 CB LYS A 369 17.025 1.012 23.689 1.00 94.15 C ATOM 2584 N LYS A 370 14.107 0.291 22.605 1.00 95.07 N ATOM 2585 CA LYS A 370 13.254 -0.567 21.787 1.00 92.51 C ATOM 2586 C LYS A 370 12.587 0.220 20.665 1.00 85.60 C ATOM 2587 O LYS A 370 12.454 -0.280 19.541 1.00 77.93 O ATOM 2588 CB LYS A 370 12.203 -1.254 22.662 1.00 85.65 C ATOM 2589 N ALA A 371 12.167 1.454 20.944 1.00 85.70 N ATOM 2590 CA ALA A 371 11.556 2.271 19.901 1.00 78.85 C ATOM 2591 C ALA A 371 12.589 2.776 18.902 1.00 73.40 C ATOM 2592 O ALA A 371 12.274 2.940 17.718 1.00 67.94 O ATOM 2593 CB ALA A 371 10.805 3.440 20.520 1.00 20.00 C ATOM 2594 N THR A 372 13.820 3.030 19.357 1.00 75.36 N ATOM 2595 CA THR A 372 14.875 3.470 18.451 1.00 64.07 C ATOM 2596 C THR A 372 15.326 2.343 17.535 1.00 71.79 C ATOM 2597 O THR A 372 15.714 2.593 16.389 1.00 80.74 O ATOM 2598 CB THR A 372 16.066 4.010 19.246 1.00 69.33 C ATOM 2599 OG1 THR A 372 15.634 5.071 20.104 1.00 74.68 O ATOM 2600 CG2 THR A 372 17.138 4.544 18.316 1.00 68.04 C ATOM 2601 N GLN A 373 15.283 1.100 18.019 1.00 68.72 N ATOM 2602 CA GLN A 373 15.663 -0.031 17.180 1.00 79.96 C ATOM 2603 C GLN A 373 14.624 -0.283 16.095 1.00 79.40 C ATOM 2604 O GLN A 373 14.972 -0.633 14.961 1.00 75.09 O ATOM 2605 CB GLN A 373 15.857 -1.276 18.043 1.00 95.27 C ATOM 2606 CG GLN A 373 17.006 -1.162 19.028 1.00107.01 C ATOM 2607 CD GLN A 373 16.835 -2.074 20.228 1.00113.19 C ATOM 2608 OE1 GLN A 373 15.768 -2.652 20.438 1.00109.22 O ATOM 2609 NE2 GLN A 373 17.889 -2.204 21.025 1.00117.08 N ATOM 2610 N MET A 374 13.345 -0.105 16.421 1.00 79.17 N ATOM 2611 CA MET A 374 12.307 -0.277 15.413 1.00 76.40 C ATOM 2612 C MET A 374 12.384 0.814 14.350 1.00 70.69 C ATOM 2613 O MET A 374 12.182 0.543 13.160 1.00 68.25 O ATOM 2614 CB MET A 374 10.934 -0.292 16.079 1.00 77.49 C ATOM 2615 CG MET A 374 9.801 -0.689 15.153 1.00 81.14 C ATOM 2616 SD MET A 374 8.219 -0.741 16.009 1.00 84.97 S ATOM 2617 CE MET A 374 8.086 0.958 16.565 1.00103.28 C ATOM 2618 N ALA A 375 12.684 2.052 14.756 1.00 72.85 N ATOM 2619 CA ALA A 375 12.789 3.144 13.793 1.00 69.01 C ATOM 2620 C ALA A 375 13.899 2.887 12.783 1.00 71.99 C ATOM 2621 O ALA A 375 13.756 3.203 11.596 1.00 68.65 O ATOM 2622 CB ALA A 375 13.021 4.464 14.513 1.00 20.00 C ATOM 2623 N ALA A 376 15.014 2.312 13.234 1.00 72.30 N ATOM 2624 CA ALA A 376 16.110 2.018 12.320 1.00 74.21 C ATOM 2625 C ALA A 376 15.790 0.830 11.427 1.00 77.19 C ATOM 2626 O ALA A 376 16.261 0.771 10.285 1.00 87.02 O ATOM 2627 CB ALA A 376 17.398 1.765 13.104 1.00 74.32 C ATOM 2628 N ILE A 377 15.001 -0.125 11.921 1.00 87.67 N ATOM 2629 CA ILE A 377 14.633 -1.265 11.089 1.00 95.90 C ATOM 2630 C ILE A 377 13.706 -0.839 9.957 1.00101.03 C ATOM 2631 O ILE A 377 13.826 -1.331 8.830 1.00 92.85 O ATOM 2632 CB ILE A 377 13.963 -2.361 11.939 1.00 20.00 C ATOM 2633 CG1 ILE A 377 14.964 -2.954 12.932 1.00 20.00 C ATOM 2634 CG2 ILE A 377 13.385 -3.448 11.046 1.00 20.00 C ATOM 2635 CD1 ILE A 377 14.332 -3.844 13.978 1.00 20.00 C ATOM 2636 N VAL A 378 12.786 0.088 10.234 1.00 89.06 N ATOM 2637 CA VAL A 378 11.896 0.596 9.192 1.00 75.68 C ATOM 2638 C VAL A 378 12.683 1.387 8.156 1.00 75.18 C ATOM 2639 O VAL A 378 12.445 1.268 6.948 1.00 76.19 O ATOM 2640 CB VAL A 378 10.775 1.445 9.820 1.00 64.00 C ATOM 2641 CG1 VAL A 378 9.960 2.132 8.740 1.00 62.64 C ATOM 2642 CG2 VAL A 378 9.887 0.580 10.701 1.00 69.48 C ATOM 2643 N ALA A 379 13.629 2.210 8.612 1.00 84.87 N ATOM 2644 CA ALA A 379 14.470 2.963 7.688 1.00 87.10 C ATOM 2645 C ALA A 379 15.330 2.035 6.842 1.00 88.96 C ATOM 2646 O ALA A 379 15.578 2.310 5.662 1.00 81.40 O ATOM 2647 CB ALA A 379 15.348 3.945 8.463 1.00 44.79 C ATOM 2648 N GLY A 380 15.802 0.935 7.428 1.00 77.23 N ATOM 2649 CA GLY A 380 16.620 0.001 6.670 1.00 80.45 C ATOM 2650 C GLY A 380 15.818 -0.749 5.624 1.00 77.59 C ATOM 2651 O GLY A 380 16.246 -0.884 4.475 1.00 69.34 O ATOM 2652 N VAL A 381 14.642 -1.252 6.012 1.00 81.99 N ATOM 2653 CA VAL A 381 13.758 -1.918 5.057 1.00 83.38 C ATOM 2654 C VAL A 381 13.412 -0.978 3.910 1.00 77.79 C ATOM 2655 O VAL A 381 13.311 -1.397 2.751 1.00 66.26 O ATOM 2656 CB VAL A 381 12.494 -2.434 5.772 1.00 76.89 C ATOM 2657 CG1 VAL A 381 11.472 -2.937 4.769 1.00 69.18 C ATOM 2658 CG2 VAL A 381 12.858 -3.534 6.752 1.00 75.31 C ATOM 2659 N PHE A 382 13.231 0.308 4.214 1.00 79.75 N ATOM 2660 CA PHE A 382 13.014 1.298 3.166 1.00 68.40 C ATOM 2661 C PHE A 382 14.165 1.294 2.171 1.00 73.80 C ATOM 2662 O PHE A 382 13.953 1.186 0.958 1.00 78.38 O ATOM 2663 CB PHE A 382 12.844 2.679 3.796 1.00 62.89 C ATOM 2664 CG PHE A 382 12.514 3.767 2.815 1.00 69.81 C ATOM 2665 CD1 PHE A 382 11.203 4.013 2.452 1.00 78.17 C ATOM 2666 CD2 PHE A 382 13.513 4.560 2.276 1.00 67.00 C ATOM 2667 CE1 PHE A 382 10.895 5.021 1.557 1.00 75.89 C ATOM 2668 CE2 PHE A 382 13.211 5.566 1.380 1.00 62.38 C ATOM 2669 CZ PHE A 382 11.900 5.797 1.021 1.00 65.04 C ATOM 2670 N ILE A 383 15.399 1.395 2.672 1.00 79.94 N ATOM 2671 CA ILE A 383 16.564 1.405 1.792 1.00 76.66 C ATOM 2672 C ILE A 383 16.668 0.093 1.027 1.00 74.25 C ATOM 2673 O ILE A 383 17.053 0.072 -0.148 1.00 81.52 O ATOM 2674 CB ILE A 383 17.840 1.702 2.601 1.00 71.78 C ATOM 2675 CG1 ILE A 383 17.851 3.163 3.035 1.00 63.66 C ATOM 2676 CG2 ILE A 383 19.084 1.400 1.789 1.00 79.30 C ATOM 2677 CD1 ILE A 383 17.701 4.126 1.880 1.00 64.10 C ATOM 2678 N ILE A 384 16.309 -1.019 1.668 1.00 77.47 N ANISOU 2678 N ILE A 384 10269 8636 10532 1676 -785 -446 N ATOM 2679 CA ILE A 384 16.346 -2.312 0.990 1.00 77.09 C ANISOU 2679 CA ILE A 384 10626 8415 10249 1786 -743 -487 C ATOM 2680 C ILE A 384 15.395 -2.323 -0.203 1.00 79.25 C ANISOU 2680 C ILE A 384 11068 8660 10381 1476 -652 -397 C ATOM 2681 O ILE A 384 15.699 -2.905 -1.252 1.00 79.85 O ANISOU 2681 O ILE A 384 11325 8712 10302 1540 -544 -477 O ATOM 2682 CB ILE A 384 16.026 -3.439 1.989 1.00 74.75 C ANISOU 2682 CB ILE A 384 10740 7870 9793 1895 -906 -471 C ATOM 2683 CG1 ILE A 384 17.200 -3.648 2.941 1.00 77.41 C ANISOU 2683 CG1 ILE A 384 10961 8240 10210 2294 -1026 -570 C ATOM 2684 CG2 ILE A 384 15.704 -4.737 1.267 1.00 71.60 C ANISOU 2684 CG2 ILE A 384 10844 7191 9169 1898 -891 -497 C ATOM 2685 CD1 ILE A 384 18.443 -4.186 2.256 1.00 79.90 C ANISOU 2685 CD1 ILE A 384 11224 8571 10564 2673 -951 -738 C ATOM 2686 N CYS A 385 14.245 -1.657 -0.076 1.00 75.66 N ANISOU 2686 N CYS A 385 10540 8236 9971 1156 -704 -252 N ATOM 2687 CA CYS A 385 13.214 -1.744 -1.106 1.00 79.40 C ANISOU 2687 CA CYS A 385 11178 8693 10298 856 -690 -152 C ATOM 2688 C CYS A 385 13.483 -0.807 -2.281 1.00 77.99 C ANISOU 2688 C CYS A 385 10754 8710 10168 769 -575 -84 C ATOM 2689 O CYS A 385 13.199 -1.160 -3.432 1.00 80.47 O ANISOU 2689 O CYS A 385 11270 9043 10261 646 -531 -66 O ATOM 2690 CB CYS A 385 11.842 -1.449 -0.500 1.00 80.67 C ANISOU 2690 CB CYS A 385 11312 8841 10500 576 -801 -23 C ATOM 2691 SG CYS A 385 11.235 -2.722 0.645 1.00 83.19 S ANISOU 2691 SG CYS A 385 12017 8939 10653 532 -901 -25 S ATOM 2692 N TRP A 386 14.018 0.384 -2.024 1.00 68.60 N ANISOU 2692 N TRP A 386 9160 7658 9246 804 -535 -37 N ATOM 2693 CA TRP A 386 14.213 1.350 -3.095 1.00 71.32 C ANISOU 2693 CA TRP A 386 9293 8158 9646 667 -432 98 C ATOM 2694 C TRP A 386 15.618 1.346 -3.677 1.00 73.91 C ANISOU 2694 C TRP A 386 9483 8642 9959 842 -227 12 C ATOM 2695 O TRP A 386 15.812 1.874 -4.776 1.00 77.41 O ANISOU 2695 O TRP A 386 9849 9237 10328 705 -92 139 O ATOM 2696 CB TRP A 386 13.885 2.767 -2.612 1.00 68.85 C ANISOU 2696 CB TRP A 386 8631 7857 9670 543 -510 230 C ATOM 2697 CG TRP A 386 12.415 3.071 -2.565 1.00 72.68 C ANISOU 2697 CG TRP A 386 9161 8279 10174 338 -661 365 C ATOM 2698 CD1 TRP A 386 11.648 3.236 -1.448 1.00 67.00 C ANISOU 2698 CD1 TRP A 386 8370 7494 9594 332 -777 320 C ATOM 2699 CD2 TRP A 386 11.534 3.244 -3.684 1.00 78.89 C ANISOU 2699 CD2 TRP A 386 10042 9108 10823 121 -715 558 C ATOM 2700 NE1 TRP A 386 10.348 3.502 -1.801 1.00 70.95 N ANISOU 2700 NE1 TRP A 386 8865 8000 10093 139 -882 461 N ATOM 2701 CE2 TRP A 386 10.251 3.512 -3.168 1.00 76.55 C ANISOU 2701 CE2 TRP A 386 9677 8767 10641 9 -876 617 C ATOM 2702 CE3 TRP A 386 11.706 3.200 -5.072 1.00 78.88 C ANISOU 2702 CE3 TRP A 386 10168 9215 10586 17 -646 682 C ATOM 2703 CZ2 TRP A 386 9.146 3.736 -3.988 1.00 75.36 C ANISOU 2703 CZ2 TRP A 386 9547 8666 10419 -188 -1008 800 C ATOM 2704 CZ3 TRP A 386 10.606 3.421 -5.885 1.00 78.84 C ANISOU 2704 CZ3 TRP A 386 10240 9252 10462 -196 -791 875 C ATOM 2705 CH2 TRP A 386 9.343 3.684 -5.340 1.00 78.30 C ANISOU 2705 CH2 TRP A 386 10069 9128 10555 -289 -989 935 C ATOM 2706 N LEU A 387 16.599 0.779 -2.986 1.00 71.16 N ANISOU 2706 N LEU A 387 9082 8289 9666 1138 -199 -185 N ATOM 2707 CA LEU A 387 17.963 0.908 -3.486 1.00 77.39 C ANISOU 2707 CA LEU A 387 9613 9290 10501 1307 10 -275 C ATOM 2708 C LEU A 387 18.178 0.130 -4.783 1.00 81.59 C ANISOU 2708 C LEU A 387 10394 9919 10687 1358 212 -346 C ATOM 2709 O LEU A 387 18.816 0.661 -5.701 1.00 86.35 O ANISOU 2709 O LEU A 387 10786 10774 11250 1288 442 -288 O ATOM 2710 CB LEU A 387 18.985 0.473 -2.436 1.00 76.08 C ANISOU 2710 CB LEU A 387 9284 9129 10492 1656 -47 -481 C ATOM 2711 CG LEU A 387 20.393 0.933 -2.792 1.00 73.95 C ANISOU 2711 CG LEU A 387 8566 9145 10385 1779 152 -557 C ATOM 2712 CD1 LEU A 387 20.380 2.425 -3.067 1.00 70.62 C ANISOU 2712 CD1 LEU A 387 7792 8838 10202 1432 210 -352 C ATOM 2713 CD2 LEU A 387 21.363 0.599 -1.677 1.00 74.27 C ANISOU 2713 CD2 LEU A 387 8384 9220 10617 2125 25 -752 C ATOM 2714 N PRO A 388 17.692 -1.112 -4.913 1.00 79.42 N ANISOU 2714 N PRO A 388 10576 9454 10144 1463 148 -479 N ATOM 2715 CA PRO A 388 17.785 -1.780 -6.223 1.00 83.37 C ANISOU 2715 CA PRO A 388 11355 10040 10283 1481 328 -585 C ATOM 2716 C PRO A 388 17.190 -0.967 -7.356 1.00 88.60 C ANISOU 2716 C PRO A 388 12005 10889 10771 1117 400 -357 C ATOM 2717 O PRO A 388 17.670 -1.054 -8.493 1.00 89.35 O ANISOU 2717 O PRO A 388 12143 11216 10591 1123 637 -407 O ATOM 2718 CB PRO A 388 17.015 -3.085 -5.998 1.00 78.09 C ANISOU 2718 CB PRO A 388 11219 9031 9418 1534 148 -722 C ATOM 2719 CG PRO A 388 17.214 -3.371 -4.563 1.00 73.10 C ANISOU 2719 CG PRO A 388 10537 8200 9037 1742 -22 -758 C ATOM 2720 CD PRO A 388 17.196 -2.039 -3.878 1.00 74.29 C ANISOU 2720 CD PRO A 388 10229 8503 9495 1588 -73 -564 C ATOM 2721 N PHE A 389 16.157 -0.168 -7.077 1.00 87.86 N ANISOU 2721 N PHE A 389 11851 10717 10815 821 202 -105 N ATOM 2722 CA PHE A 389 15.588 0.699 -8.103 1.00 88.83 C ANISOU 2722 CA PHE A 389 11946 10997 10808 504 215 164 C ATOM 2723 C PHE A 389 16.581 1.776 -8.524 1.00 87.11 C ANISOU 2723 C PHE A 389 11342 11030 10726 460 445 317 C ATOM 2724 O PHE A 389 16.791 2.009 -9.719 1.00 91.58 O ANISOU 2724 O PHE A 389 11960 11831 11005 327 627 435 O ATOM 2725 CB PHE A 389 14.287 1.323 -7.592 1.00 81.78 C ANISOU 2725 CB PHE A 389 11019 9946 10106 271 -69 378 C ATOM 2726 CG PHE A 389 13.670 2.319 -8.536 1.00 78.75 C ANISOU 2726 CG PHE A 389 10580 9686 9656 -11 -125 698 C ATOM 2727 CD1 PHE A 389 12.947 1.897 -9.638 1.00 72.20 C ANISOU 2727 CD1 PHE A 389 10065 8946 8421 -182 -197 758 C ATOM 2728 CD2 PHE A 389 13.795 3.677 -8.309 1.00 74.32 C ANISOU 2728 CD2 PHE A 389 9675 9124 9438 -104 -142 940 C ATOM 2729 CE1 PHE A 389 12.374 2.812 -10.501 1.00 66.21 C ANISOU 2729 CE1 PHE A 389 9270 8308 7580 -418 -296 1089 C ATOM 2730 CE2 PHE A 389 13.221 4.593 -9.169 1.00 73.66 C ANISOU 2730 CE2 PHE A 389 9576 9102 9309 -336 -229 1275 C ATOM 2731 CZ PHE A 389 12.508 4.160 -10.263 1.00 67.96 C ANISOU 2731 CZ PHE A 389 9160 8501 8161 -483 -313 1367 C ATOM 2732 N PHE A 390 17.211 2.438 -7.553 1.00 78.28 N ANISOU 2732 N PHE A 390 9842 9876 10022 542 440 319 N ATOM 2733 CA PHE A 390 18.154 3.503 -7.865 1.00 77.80 C ANISOU 2733 CA PHE A 390 9387 10020 10154 435 640 473 C ATOM 2734 C PHE A 390 19.520 2.977 -8.285 1.00 85.50 C ANISOU 2734 C PHE A 390 10201 11281 11003 650 968 266 C ATOM 2735 O PHE A 390 20.266 3.699 -8.955 1.00 80.65 O ANISOU 2735 O PHE A 390 9313 10928 10401 495 1220 418 O ATOM 2736 CB PHE A 390 18.290 4.441 -6.666 1.00 72.78 C ANISOU 2736 CB PHE A 390 8403 9227 10023 409 479 515 C ATOM 2737 CG PHE A 390 17.046 5.229 -6.384 1.00 71.97 C ANISOU 2737 CG PHE A 390 8367 8891 10086 201 217 731 C ATOM 2738 CD1 PHE A 390 16.770 6.384 -7.095 1.00 73.92 C ANISOU 2738 CD1 PHE A 390 8531 9132 10422 -77 215 1066 C ATOM 2739 CD2 PHE A 390 16.146 4.810 -5.423 1.00 69.40 C ANISOU 2739 CD2 PHE A 390 8185 8358 9824 295 -21 611 C ATOM 2740 CE1 PHE A 390 15.624 7.110 -6.848 1.00 69.85 C ANISOU 2740 CE1 PHE A 390 8056 8392 10093 -202 -42 1247 C ATOM 2741 CE2 PHE A 390 14.995 5.533 -5.171 1.00 69.17 C ANISOU 2741 CE2 PHE A 390 8161 8162 9960 142 -234 777 C ATOM 2742 CZ PHE A 390 14.735 6.685 -5.884 1.00 63.89 C ANISOU 2742 CZ PHE A 390 7389 7471 9415 -78 -256 1080 C ATOM 2743 N ILE A 391 19.865 1.744 -7.905 1.00 83.05 N ANISOU 2743 N ILE A 391 10043 10926 10586 1005 976 -67 N ATOM 2744 CA ILE A 391 21.044 1.100 -8.477 1.00 88.93 C ANISOU 2744 CA ILE A 391 10677 11954 11158 1273 1299 -305 C ATOM 2745 C ILE A 391 20.854 0.907 -9.975 1.00 91.28 C ANISOU 2745 C ILE A 391 11243 12480 10960 1127 1541 -254 C ATOM 2746 O ILE A 391 21.789 1.084 -10.766 1.00 94.74 O ANISOU 2746 O ILE A 391 11451 13294 11253 1139 1904 -276 O ATOM 2747 CB ILE A 391 21.321 -0.238 -7.761 1.00 85.00 C ANISOU 2747 CB ILE A 391 10370 11271 10655 1728 1197 -664 C ATOM 2748 CG1 ILE A 391 21.803 0.004 -6.329 1.00 81.99 C ANISOU 2748 CG1 ILE A 391 9657 10782 10715 1901 995 -715 C ATOM 2749 CG2 ILE A 391 22.336 -1.068 -8.534 1.00 85.18 C ANISOU 2749 CG2 ILE A 391 10376 11551 10438 2063 1525 -960 C ATOM 2750 CD1 ILE A 391 22.006 -1.268 -5.531 1.00 79.71 C ANISOU 2750 CD1 ILE A 391 9598 10266 10423 2344 833 -991 C ATOM 2751 N THR A 392 19.633 0.564 -10.388 1.00 91.03 N ANISOU 2751 N THR A 392 11682 12262 10642 965 1345 -183 N ATOM 2752 CA THR A 392 19.347 0.341 -11.801 1.00 92.03 C ANISOU 2752 CA THR A 392 12124 12607 10236 813 1511 -151 C ATOM 2753 C THR A 392 19.510 1.622 -12.611 1.00 96.64 C ANISOU 2753 C THR A 392 12473 13487 10758 456 1684 247 C ATOM 2754 O THR A 392 19.972 1.585 -13.759 1.00 99.51 O ANISOU 2754 O THR A 392 12896 14212 10701 394 2002 256 O ATOM 2755 CB THR A 392 17.934 -0.222 -11.949 1.00 85.65 C ANISOU 2755 CB THR A 392 11821 11527 9195 670 1183 -144 C ATOM 2756 OG1 THR A 392 17.843 -1.462 -11.238 1.00 86.36 O ANISOU 2756 OG1 THR A 392 12169 11313 9330 965 1047 -489 O ATOM 2757 CG2 THR A 392 17.589 -0.458 -13.404 1.00 82.50 C ANISOU 2757 CG2 THR A 392 11776 11367 8203 498 1292 -131 C ATOM 2758 N HIS A 393 19.187 2.742 -12.031 1.00 88.71 N ANISOU 2758 N HIS A 393 11226 12324 10155 219 1485 579 N ATOM 2759 CA HIS A 393 19.363 3.957 -12.738 1.00 88.98 C ANISOU 2759 CA HIS A 393 11056 12550 10202 -130 1618 1001 C ATOM 2760 C HIS A 393 20.809 4.181 -13.033 1.00 88.31 C ANISOU 2760 C HIS A 393 10554 12829 10172 -105 2051 965 C ATOM 2761 O HIS A 393 21.145 4.651 -14.071 1.00 90.40 O ANISOU 2761 O HIS A 393 10759 13392 10197 -381 2313 1255 O ATOM 2762 CB HIS A 393 18.863 5.074 -11.893 1.00 92.81 C ANISOU 2762 CB HIS A 393 11357 12712 11192 -324 1304 1294 C ATOM 2763 CG HIS A 393 17.412 5.334 -12.064 1.00 96.38 C ANISOU 2763 CG HIS A 393 12141 12922 11557 -443 932 1454 C ATOM 2764 ND1 HIS A 393 16.815 5.355 -13.296 1.00101.35 N ANISOU 2764 ND1 HIS A 393 12985 13642 11882 -712 860 1815 N ATOM 2765 CD2 HIS A 393 16.440 5.591 -11.168 1.00 93.09 C ANISOU 2765 CD2 HIS A 393 11851 12212 11307 -333 611 1312 C ATOM 2766 CE1 HIS A 393 15.536 5.622 -13.155 1.00 98.51 C ANISOU 2766 CE1 HIS A 393 12830 13059 11540 -744 489 1868 C ATOM 2767 NE2 HIS A 393 15.282 5.762 -11.872 1.00 93.35 N ANISOU 2767 NE2 HIS A 393 12117 12180 11171 -533 357 1563 N ATOM 2768 N ILE A 394 21.675 3.869 -12.094 1.00 95.53 N ANISOU 2768 N ILE A 394 11157 13746 11395 209 2124 635 N ATOM 2769 CA ILE A 394 23.103 4.065 -12.304 1.00100.46 C ANISOU 2769 CA ILE A 394 11300 14765 12104 258 2532 556 C ATOM 2770 C ILE A 394 23.590 3.234 -13.480 1.00110.00 C ANISOU 2770 C ILE A 394 12669 16389 12736 410 2939 349 C ATOM 2771 O ILE A 394 24.530 3.628 -14.181 1.00116.65 O ANISOU 2771 O ILE A 394 13187 17679 13455 283 3367 434 O ATOM 2772 CB ILE A 394 23.876 3.735 -11.014 1.00 95.87 C ANISOU 2772 CB ILE A 394 10335 14092 12001 599 2436 239 C ATOM 2773 N LEU A 395 22.959 2.084 -13.726 1.00109.05 N ANISOU 2773 N LEU A 395 13051 16136 12246 661 2828 65 N ATOM 2774 CA LEU A 395 23.384 1.213 -14.816 1.00115.80 C ANISOU 2774 CA LEU A 395 14119 17349 12533 853 3195 -221 C ATOM 2775 C LEU A 395 22.911 1.731 -16.169 1.00123.98 C ANISOU 2775 C LEU A 395 15434 18666 13007 451 3352 106 C ATOM 2776 O LEU A 395 23.622 1.591 -17.170 1.00132.70 O ANISOU 2776 O LEU A 395 16488 20259 13673 459 3812 22 O ATOM 2777 CB LEU A 395 22.873 -0.208 -14.578 1.00113.04 C ANISOU 2777 CB LEU A 395 14254 16684 12011 1243 2983 -662 C ATOM 2778 CG LEU A 395 23.285 -0.827 -13.242 1.00107.58 C ANISOU 2778 CG LEU A 395 13379 15684 11813 1666 2788 -952 C ATOM 2779 CD1 LEU A 395 22.874 -2.287 -13.174 1.00109.94 C ANISOU 2779 CD1 LEU A 395 14213 15663 11896 2035 2631 -1369 C ATOM 2780 CD2 LEU A 395 24.782 -0.681 -13.009 1.00102.89 C ANISOU 2780 CD2 LEU A 395 12151 15454 11490 1927 3132 -1110 C ATOM 2781 N ASN A 396 21.713 2.324 -16.219 1.00120.69 N ANISOU 2781 N ASN A 396 15306 17974 12576 116 2975 478 N ATOM 2782 CA ASN A 396 21.242 2.943 -17.454 1.00120.58 C ANISOU 2782 CA ASN A 396 15547 18214 12053 -278 3052 871 C ATOM 2783 C ASN A 396 22.194 4.031 -17.930 1.00122.42 C ANISOU 2783 C ASN A 396 15355 18837 12322 -573 3455 1241 C ATOM 2784 O ASN A 396 22.387 4.205 -19.139 1.00125.81 O ANISOU 2784 O ASN A 396 15933 19697 12171 -784 3770 1420 O ATOM 2785 CB ASN A 396 19.841 3.523 -17.251 1.00116.75 C ANISOU 2785 CB ASN A 396 15328 17340 11693 -546 2527 1239 C ATOM 2786 CG ASN A 396 18.760 2.676 -17.888 1.00117.94 C ANISOU 2786 CG ASN A 396 16062 17433 11316 -534 2274 1087 C ATOM 2787 OD1 ASN A 396 18.987 1.516 -18.228 1.00121.59 O ANISOU 2787 OD1 ASN A 396 16780 18007 11413 -276 2424 626 O ATOM 2788 ND2 ASN A 396 17.576 3.253 -18.057 1.00116.24 N ANISOU 2788 ND2 ASN A 396 16052 17032 11079 -807 1870 1457 N ATOM 2789 N ILE A 397 22.806 4.760 -16.997 1.00128.30 N ANISOU 2789 N ILE A 397 15581 19448 13721 -619 3450 1356 N ATOM 2790 CA ILE A 397 23.706 5.849 -17.357 1.00131.63 C ANISOU 2790 CA ILE A 397 15568 20182 14265 -972 3805 1730 C ATOM 2791 C ILE A 397 25.103 5.322 -17.667 1.00137.13 C ANISOU 2791 C ILE A 397 15858 21427 14818 -764 4380 1392 C ATOM 2792 O ILE A 397 25.789 5.839 -18.556 1.00140.52 O ANISOU 2792 O ILE A 397 16093 22338 14959 -1056 4838 1642 O ATOM 2793 CB ILE A 397 23.731 6.896 -16.228 1.00123.72 C ANISOU 2793 CB ILE A 397 14191 18774 14042 -1149 3517 1971 C ATOM 2794 CG1 ILE A 397 22.331 7.473 -16.007 1.00113.56 C ANISOU 2794 CG1 ILE A 397 13280 16985 12883 -1327 2987 2301 C ATOM 2795 CG2 ILE A 397 24.735 8.002 -16.530 1.00125.40 C ANISOU 2795 CG2 ILE A 397 13930 19262 14453 -1557 3873 2337 C ATOM 2796 CD1 ILE A 397 22.251 8.459 -14.860 1.00102.21 C ANISOU 2796 CD1 ILE A 397 11537 15104 12195 -1449 2680 2462 C ATOM 2797 N HIS A 398 25.537 4.278 -16.959 1.00136.75 N ANISOU 2797 N HIS A 398 15674 21329 14958 -248 4372 832 N ATOM 2798 CA HIS A 398 26.930 3.846 -17.033 1.00140.25 C ANISOU 2798 CA HIS A 398 15599 22260 15431 23 4867 485 C ATOM 2799 C HIS A 398 27.250 3.199 -18.376 1.00154.68 C ANISOU 2799 C HIS A 398 17644 24638 16490 117 5371 293 C ATOM 2800 O HIS A 398 28.121 3.674 -19.114 1.00162.37 O ANISOU 2800 O HIS A 398 18256 26184 17254 -111 5901 448 O ATOM 2801 CB HIS A 398 27.240 2.881 -15.886 1.00132.50 C ANISOU 2801 CB HIS A 398 14462 21019 14861 602 4649 -39 C ATOM 2802 N CYS A 399 26.570 2.103 -18.707 1.00157.99 N ANISOU 2802 N CYS A 399 18652 24908 16468 436 5229 -65 N ATOM 2803 CA CYS A 399 26.929 1.309 -19.875 1.00171.19 C ANISOU 2803 CA CYS A 399 20554 27077 17414 635 5693 -403 C ATOM 2804 C CYS A 399 25.915 1.388 -21.006 1.00172.38 C ANISOU 2804 C CYS A 399 21379 27292 16826 306 5614 -163 C ATOM 2805 O CYS A 399 26.152 0.799 -22.069 1.00171.94 O ANISOU 2805 O CYS A 399 21574 27683 16070 417 5999 -433 O ATOM 2806 CB CYS A 399 27.145 -0.157 -19.472 1.00177.68 C ANISOU 2806 CB CYS A 399 21527 27720 18264 1324 5648 -1118 C ATOM 2807 SG CYS A 399 25.689 -1.129 -18.956 1.00177.65 S ANISOU 2807 SG CYS A 399 22318 26935 18245 1520 4957 -1341 S ATOM 2808 N ASP A 400 24.802 2.093 -20.815 1.00169.42 N ANISOU 2808 N ASP A 400 21292 26506 16572 -73 5118 313 N ATOM 2809 CA ASP A 400 23.708 2.176 -21.779 1.00172.19 C ANISOU 2809 CA ASP A 400 22278 26866 16282 -369 4909 565 C ATOM 2810 C ASP A 400 23.130 0.810 -22.126 1.00178.49 C ANISOU 2810 C ASP A 400 23661 27552 16606 -24 4760 1 C ATOM 2811 O ASP A 400 22.354 0.694 -23.084 1.00180.90 O ANISOU 2811 O ASP A 400 24500 27979 16254 -230 4642 91 O ATOM 2812 CB ASP A 400 24.139 2.903 -23.061 1.00174.58 C ANISOU 2812 CB ASP A 400 22570 27804 15958 -772 5382 965 C ATOM 2813 N CYS A 401 23.494 -0.229 -21.377 1.00180.63 N ANISOU 2813 N CYS A 401 23862 27575 17194 489 4738 -576 N ATOM 2814 CA CYS A 401 22.923 -1.551 -21.583 1.00179.00 C ANISOU 2814 CA CYS A 401 24242 27130 16641 806 4543 -1120 C ATOM 2815 C CYS A 401 21.440 -1.519 -21.252 1.00170.63 C ANISOU 2815 C CYS A 401 23622 25538 15671 556 3881 -897 C ATOM 2816 O CYS A 401 21.063 -1.243 -20.109 1.00166.40 O ANISOU 2816 O CYS A 401 22893 24541 15789 548 3513 -729 O ATOM 2817 CB CYS A 401 23.624 -2.583 -20.701 1.00179.14 C ANISOU 2817 CB CYS A 401 24079 26891 17096 1410 4598 -1700 C ATOM 2818 SG CYS A 401 25.421 -2.457 -20.478 1.00183.37 S ANISOU 2818 SG CYS A 401 23801 27930 17940 1774 5237 -1908 S ATOM 2819 N ASN A 402 20.597 -1.793 -22.244 1.00163.09 N ANISOU 2819 N ASN A 402 23235 24683 14049 348 3727 -908 N ATOM 2820 CA ASN A 402 19.171 -1.877 -21.964 1.00152.09 C ANISOU 2820 CA ASN A 402 22222 22828 12736 126 3092 -755 C ATOM 2821 C ASN A 402 18.914 -3.031 -21.004 1.00144.87 C ANISOU 2821 C ASN A 402 21476 21352 12215 479 2819 -1242 C ATOM 2822 O ASN A 402 19.334 -4.167 -21.242 1.00148.09 O ANISOU 2822 O ASN A 402 22151 21737 12380 836 2997 -1823 O ATOM 2823 CB ASN A 402 18.364 -2.039 -23.255 1.00153.00 C ANISOU 2823 CB ASN A 402 22907 23202 12025 -153 2955 -727 C ATOM 2824 CG ASN A 402 18.644 -3.344 -23.970 1.00154.48 C ANISOU 2824 CG ASN A 402 23550 23525 11619 142 3169 -1424 C ATOM 2825 OD1 ASN A 402 18.048 -4.376 -23.657 1.00152.23 O ANISOU 2825 OD1 ASN A 402 23645 22801 11394 294 2842 -1846 O ATOM 2826 ND2 ASN A 402 19.540 -3.303 -24.949 1.00156.47 N ANISOU 2826 ND2 ASN A 402 23784 24383 11285 209 3730 -1554 N ATOM 2827 N ILE A 403 18.259 -2.719 -19.893 1.00137.95 N ANISOU 2827 N ILE A 403 20445 20015 11956 389 2403 -999 N ATOM 2828 CA ILE A 403 18.056 -3.664 -18.801 1.00126.08 C ANISOU 2828 CA ILE A 403 19041 17968 10897 679 2150 -1342 C ATOM 2829 C ILE A 403 16.725 -4.370 -19.025 1.00123.67 C ANISOU 2829 C ILE A 403 19300 17348 10341 476 1691 -1463 C ATOM 2830 O ILE A 403 15.774 -3.737 -19.506 1.00123.23 O ANISOU 2830 O ILE A 403 19345 17396 10082 73 1419 -1099 O ATOM 2831 CB ILE A 403 18.121 -2.936 -17.448 1.00116.57 C ANISOU 2831 CB ILE A 403 17344 16498 10450 680 1990 -1029 C ATOM 2832 CG1 ILE A 403 19.571 -2.545 -17.154 1.00117.76 C ANISOU 2832 CG1 ILE A 403 16950 16923 10871 944 2430 -1064 C ATOM 2833 CG2 ILE A 403 17.524 -3.771 -16.324 1.00111.83 C ANISOU 2833 CG2 ILE A 403 16927 15326 10238 834 1619 -1235 C ATOM 2834 CD1 ILE A 403 19.744 -1.682 -15.938 1.00115.05 C ANISOU 2834 CD1 ILE A 403 16103 16396 11214 903 2293 -760 C ATOM 2835 N PRO A 404 16.628 -5.671 -18.745 1.00118.90 N ANISOU 2835 N PRO A 404 19074 16363 9738 731 1581 -1960 N ATOM 2836 CA PRO A 404 15.360 -6.387 -18.918 1.00118.90 C ANISOU 2836 CA PRO A 404 19598 16036 9542 479 1130 -2089 C ATOM 2837 C PRO A 404 14.199 -5.600 -18.342 1.00114.46 C ANISOU 2837 C PRO A 404 18849 15327 9312 80 700 -1589 C ATOM 2838 O PRO A 404 14.149 -5.345 -17.130 1.00111.06 O ANISOU 2838 O PRO A 404 18106 14611 9479 144 589 -1414 O ATOM 2839 CB PRO A 404 15.590 -7.690 -18.142 1.00118.42 C ANISOU 2839 CB PRO A 404 19799 15435 9759 841 1069 -2563 C ATOM 2840 CG PRO A 404 17.050 -7.938 -18.305 1.00121.83 C ANISOU 2840 CG PRO A 404 20054 16085 10152 1347 1569 -2883 C ATOM 2841 CD PRO A 404 17.718 -6.580 -18.344 1.00119.79 C ANISOU 2841 CD PRO A 404 19169 16331 10014 1271 1867 -2444 C ATOM 2842 N PRO A 405 13.257 -5.175 -19.187 1.00111.48 N ANISOU 2842 N PRO A 405 18639 15168 8549 -316 448 -1354 N ATOM 2843 CA PRO A 405 12.126 -4.381 -18.686 1.00109.02 C ANISOU 2843 CA PRO A 405 18100 14751 8571 -653 36 -886 C ATOM 2844 C PRO A 405 11.320 -5.093 -17.621 1.00107.40 C ANISOU 2844 C PRO A 405 17974 14039 8792 -700 -301 -1012 C ATOM 2845 O PRO A 405 10.656 -4.425 -16.820 1.00106.74 O ANISOU 2845 O PRO A 405 17562 13840 9155 -851 -528 -666 O ATOM 2846 CB PRO A 405 11.292 -4.119 -19.948 1.00110.35 C ANISOU 2846 CB PRO A 405 18539 15248 8141 -1009 -207 -731 C ATOM 2847 CG PRO A 405 11.691 -5.197 -20.899 1.00113.76 C ANISOU 2847 CG PRO A 405 19491 15789 7942 -900 -38 -1264 C ATOM 2848 CD PRO A 405 13.141 -5.456 -20.627 1.00117.16 C ANISOU 2848 CD PRO A 405 19780 16246 8490 -452 496 -1536 C ATOM 2849 N VAL A 406 11.356 -6.428 -17.580 1.00111.87 N ANISOU 2849 N VAL A 406 18978 14290 9236 -579 -329 -1496 N ATOM 2850 CA VAL A 406 10.738 -7.139 -16.469 1.00102.56 C ANISOU 2850 CA VAL A 406 17881 12600 8486 -624 -592 -1581 C ATOM 2851 C VAL A 406 11.508 -6.882 -15.181 1.00104.10 C ANISOU 2851 C VAL A 406 17697 12610 9246 -300 -398 -1479 C ATOM 2852 O VAL A 406 10.926 -6.894 -14.090 1.00102.17 O ANISOU 2852 O VAL A 406 17313 12081 9424 -395 -602 -1324 O ATOM 2853 CB VAL A 406 10.640 -8.644 -16.776 1.00 94.49 C ANISOU 2853 CB VAL A 406 17480 11217 7203 -584 -680 -2114 C ATOM 2854 N LEU A 407 12.818 -6.639 -15.277 1.00103.82 N ANISOU 2854 N LEU A 407 17468 12769 9209 74 -3 -1567 N ATOM 2855 CA LEU A 407 13.592 -6.296 -14.089 1.00100.38 C ANISOU 2855 CA LEU A 407 16623 12220 9296 369 146 -1462 C ATOM 2856 C LEU A 407 13.390 -4.838 -13.698 1.00 94.26 C ANISOU 2856 C LEU A 407 15315 11675 8824 182 114 -975 C ATOM 2857 O LEU A 407 13.200 -4.533 -12.516 1.00 88.29 O ANISOU 2857 O LEU A 407 14299 10718 8529 200 -8 -812 O ATOM 2858 CB LEU A 407 15.077 -6.584 -14.317 1.00101.90 C ANISOU 2858 CB LEU A 407 16737 12562 9418 837 561 -1755 C ATOM 2859 N TYR A 408 13.370 -3.956 -14.650 1.00 94.06 N ANISOU 2859 N TYR A 408 15152 12055 8531 5 218 -738 N ATOM 2860 CA TYR A 408 13.143 -2.599 -14.299 1.00 92.67 C ANISOU 2860 CA TYR A 408 14536 12021 8655 -189 141 -264 C ATOM 2861 C TYR A 408 11.764 -2.493 -13.713 1.00 95.64 C ANISOU 2861 C TYR A 408 14901 12179 9258 -462 -278 -65 C ATOM 2862 O TYR A 408 11.578 -1.795 -12.766 1.00 92.85 O ANISOU 2862 O TYR A 408 14175 11751 9352 -489 -366 194 O ATOM 2863 CB TYR A 408 13.263 -1.746 -15.521 1.00 92.66 C ANISOU 2863 CB TYR A 408 14496 12449 8263 -369 283 -7 C ATOM 2864 CG TYR A 408 13.909 -0.444 -15.274 1.00 92.93 C ANISOU 2864 CG TYR A 408 14043 12651 8617 -377 472 359 C ATOM 2865 CD1 TYR A 408 13.694 0.227 -14.129 1.00 88.51 C ANISOU 2865 CD1 TYR A 408 13122 11858 8651 -379 316 564 C ATOM 2866 CD2 TYR A 408 14.725 0.122 -16.199 1.00 98.66 C ANISOU 2866 CD2 TYR A 408 14681 13767 9040 -406 819 487 C ATOM 2867 CE1 TYR A 408 14.287 1.434 -13.904 1.00 87.26 C ANISOU 2867 CE1 TYR A 408 12549 11797 8809 -413 462 866 C ATOM 2868 CE2 TYR A 408 15.323 1.331 -15.973 1.00 98.99 C ANISOU 2868 CE2 TYR A 408 14288 13921 9401 -474 985 837 C ATOM 2869 CZ TYR A 408 15.086 1.974 -14.814 1.00 95.40 C ANISOU 2869 CZ TYR A 408 13502 13174 9570 -479 786 1014 C ATOM 2870 OH TYR A 408 15.640 3.178 -14.533 1.00 98.94 O ANISOU 2870 OH TYR A 408 13550 13681 10361 -572 923 1329 O ATOM 2871 N SER A 409 10.781 -3.173 -14.278 1.00105.38 N ANISOU 2871 N SER A 409 16521 13320 10198 -667 -536 -211 N ATOM 2872 CA SER A 409 9.431 -3.119 -13.727 1.00100.18 C ANISOU 2872 CA SER A 409 15802 12496 9765 -940 -916 -53 C ATOM 2873 C SER A 409 9.363 -3.750 -12.341 1.00 91.59 C ANISOU 2873 C SER A 409 14684 11035 9081 -825 -948 -193 C ATOM 2874 O SER A 409 8.543 -3.336 -11.513 1.00 85.61 O ANISOU 2874 O SER A 409 13671 10195 8661 -967 -1137 4 O ATOM 2875 CB SER A 409 8.447 -3.811 -14.672 1.00102.06 C ANISOU 2875 CB SER A 409 16434 12778 9567 -1245 -1202 -175 C ATOM 2876 OG SER A 409 8.493 -3.239 -15.967 1.00105.65 O ANISOU 2876 OG SER A 409 16956 13611 9576 -1354 -1197 -26 O ATOM 2877 N ALA A 410 10.216 -4.740 -12.069 1.00 90.76 N ANISOU 2877 N ALA A 410 14837 10715 8935 -552 -765 -524 N ATOM 2878 CA ALA A 410 10.196 -5.405 -10.769 1.00 84.55 C ANISOU 2878 CA ALA A 410 14089 9558 8478 -436 -813 -622 C ATOM 2879 C ALA A 410 10.716 -4.488 -9.669 1.00 85.46 C ANISOU 2879 C ALA A 410 13726 9716 9028 -244 -702 -420 C ATOM 2880 O ALA A 410 10.097 -4.365 -8.607 1.00 76.26 O ANISOU 2880 O ALA A 410 12411 8410 8155 -337 -841 -294 O ATOM 2881 CB ALA A 410 11.018 -6.693 -10.829 1.00 79.54 C ANISOU 2881 CB ALA A 410 13883 8649 7690 -141 -680 -1016 C ATOM 2882 N PHE A 411 11.858 -3.837 -9.904 1.00 82.88 N ANISOU 2882 N PHE A 411 13149 9606 8736 5 -442 -403 N ATOM 2883 CA PHE A 411 12.446 -2.977 -8.883 1.00 81.51 C ANISOU 2883 CA PHE A 411 12529 9464 8975 175 -355 -259 C ATOM 2884 C PHE A 411 11.593 -1.745 -8.614 1.00 76.95 C ANISOU 2884 C PHE A 411 11608 8991 8637 -75 -511 73 C ATOM 2885 O PHE A 411 11.658 -1.179 -7.516 1.00 76.38 O ANISOU 2885 O PHE A 411 11240 8854 8929 0 -536 155 O ATOM 2886 CB PHE A 411 13.859 -2.567 -9.293 1.00 88.89 C ANISOU 2886 CB PHE A 411 13244 10633 9898 438 -44 -321 C ATOM 2887 CG PHE A 411 14.856 -3.688 -9.233 1.00 94.35 C ANISOU 2887 CG PHE A 411 14147 11212 10488 811 121 -674 C ATOM 2888 CD1 PHE A 411 14.562 -4.860 -8.555 1.00 93.62 C ANISOU 2888 CD1 PHE A 411 14407 10746 10418 926 -36 -865 C ATOM 2889 CD2 PHE A 411 16.092 -3.568 -9.846 1.00 94.90 C ANISOU 2889 CD2 PHE A 411 14052 11548 10457 1055 438 -805 C ATOM 2890 CE1 PHE A 411 15.480 -5.891 -8.497 1.00 91.66 C ANISOU 2890 CE1 PHE A 411 14375 10339 10112 1324 82 -1184 C ATOM 2891 CE2 PHE A 411 17.013 -4.595 -9.790 1.00 91.21 C ANISOU 2891 CE2 PHE A 411 13738 10988 9931 1464 585 -1156 C ATOM 2892 CZ PHE A 411 16.707 -5.757 -9.115 1.00 90.35 C ANISOU 2892 CZ PHE A 411 14011 10453 9865 1623 389 -1349 C ATOM 2893 N THR A 412 10.799 -1.310 -9.596 1.00 86.37 N ANISOU 2893 N THR A 412 12841 10347 9628 -346 -634 251 N ATOM 2894 CA THR A 412 9.854 -0.225 -9.353 1.00 83.78 C ANISOU 2894 CA THR A 412 12208 10075 9551 -541 -831 553 C ATOM 2895 C THR A 412 8.712 -0.693 -8.459 1.00 78.58 C ANISOU 2895 C THR A 412 11565 9242 9050 -678 -1053 522 C ATOM 2896 O THR A 412 8.335 -0.005 -7.503 1.00 75.36 O ANISOU 2896 O THR A 412 10841 8797 8997 -662 -1111 634 O ATOM 2897 CB THR A 412 9.310 0.315 -10.677 1.00 83.99 C ANISOU 2897 CB THR A 412 12287 10328 9297 -765 -948 775 C ATOM 2898 OG1 THR A 412 10.397 0.624 -11.557 1.00 88.79 O ANISOU 2898 OG1 THR A 412 12926 11134 9675 -676 -690 805 O ATOM 2899 CG2 THR A 412 8.491 1.578 -10.436 1.00 76.49 C ANISOU 2899 CG2 THR A 412 10981 9411 8671 -879 -1149 1106 C ATOM 2900 N TRP A 413 8.148 -1.866 -8.758 1.00 79.97 N ANISOU 2900 N TRP A 413 12110 9314 8961 -831 -1168 357 N ATOM 2901 CA TRP A 413 7.078 -2.406 -7.927 1.00 79.43 C ANISOU 2901 CA TRP A 413 12060 9094 9024 -1024 -1347 342 C ATOM 2902 C TRP A 413 7.576 -2.703 -6.520 1.00 73.46 C ANISOU 2902 C TRP A 413 11258 8138 8517 -819 -1224 254 C ATOM 2903 O TRP A 413 6.853 -2.491 -5.539 1.00 70.81 O ANISOU 2903 O TRP A 413 10714 7782 8407 -915 -1295 340 O ATOM 2904 CB TRP A 413 6.498 -3.667 -8.569 1.00 85.80 C ANISOU 2904 CB TRP A 413 13317 9783 9501 -1268 -1494 166 C ATOM 2905 CG TRP A 413 5.728 -3.398 -9.828 1.00 91.51 C ANISOU 2905 CG TRP A 413 14070 10739 9962 -1534 -1703 261 C ATOM 2906 CD1 TRP A 413 5.242 -2.195 -10.250 1.00 85.59 C ANISOU 2906 CD1 TRP A 413 12966 10256 9299 -1598 -1823 542 C ATOM 2907 CD2 TRP A 413 5.358 -4.354 -10.833 1.00 96.72 C ANISOU 2907 CD2 TRP A 413 15160 11373 10216 -1760 -1855 72 C ATOM 2908 NE1 TRP A 413 4.589 -2.343 -11.449 1.00 88.41 N ANISOU 2908 NE1 TRP A 413 13492 10790 9309 -1846 -2056 571 N ATOM 2909 CE2 TRP A 413 4.646 -3.658 -11.829 1.00 95.02 C ANISOU 2909 CE2 TRP A 413 14808 11468 9826 -1963 -2077 265 C ATOM 2910 CE3 TRP A 413 5.558 -5.731 -10.985 1.00100.43 C ANISOU 2910 CE3 TRP A 413 16143 11559 10456 -1802 -1850 -252 C ATOM 2911 CZ2 TRP A 413 4.135 -4.290 -12.963 1.00 98.69 C ANISOU 2911 CZ2 TRP A 413 15618 12022 9858 -2226 -2299 130 C ATOM 2912 CZ3 TRP A 413 5.049 -6.356 -12.111 1.00103.40 C ANISOU 2912 CZ3 TRP A 413 16876 11980 10432 -2067 -2053 -417 C ATOM 2913 CH2 TRP A 413 4.347 -5.636 -13.085 1.00102.66 C ANISOU 2913 CH2 TRP A 413 16621 12251 10133 -2286 -2277 -233 C ATOM 2914 N LEU A 414 8.817 -3.184 -6.402 1.00 75.32 N ANISOU 2914 N LEU A 414 11667 8256 8695 -521 -1041 79 N ATOM 2915 CA LEU A 414 9.384 -3.467 -5.087 1.00 69.21 C ANISOU 2915 CA LEU A 414 10863 7310 8123 -291 -967 10 C ATOM 2916 C LEU A 414 9.434 -2.210 -4.226 1.00 77.59 C ANISOU 2916 C LEU A 414 11447 8517 9516 -215 -939 159 C ATOM 2917 O LEU A 414 9.179 -2.265 -3.016 1.00 79.71 O ANISOU 2917 O LEU A 414 11637 8710 9938 -194 -969 169 O ATOM 2918 CB LEU A 414 10.778 -4.078 -5.238 1.00 67.92 C ANISOU 2918 CB LEU A 414 10893 7049 7867 71 -800 -201 C ATOM 2919 CG LEU A 414 11.552 -4.368 -3.947 1.00 71.97 C ANISOU 2919 CG LEU A 414 11370 7408 8567 375 -760 -268 C ATOM 2920 CD1 LEU A 414 10.756 -5.279 -3.035 1.00 56.68 C ANISOU 2920 CD1 LEU A 414 9726 5197 6611 226 -906 -242 C ATOM 2921 CD2 LEU A 414 12.904 -4.980 -4.260 1.00 76.87 C ANISOU 2921 CD2 LEU A 414 12133 7966 9108 768 -617 -490 C ATOM 2922 N GLY A 415 9.747 -1.065 -4.832 1.00 76.07 N ANISOU 2922 N GLY A 415 10960 8524 9421 -187 -885 275 N ATOM 2923 CA GLY A 415 9.745 0.179 -4.081 1.00 72.96 C ANISOU 2923 CA GLY A 415 10144 8207 9369 -132 -886 390 C ATOM 2924 C GLY A 415 8.357 0.581 -3.618 1.00 74.19 C ANISOU 2924 C GLY A 415 10131 8394 9665 -339 -1044 507 C ATOM 2925 O GLY A 415 8.180 1.043 -2.488 1.00 75.00 O ANISOU 2925 O GLY A 415 10010 8487 9999 -269 -1044 489 O ATOM 2926 N TYR A 416 7.355 0.423 -4.485 1.00 71.29 N ANISOU 2926 N TYR A 416 9841 8097 9148 -588 -1184 609 N ATOM 2927 CA TYR A 416 5.978 0.695 -4.089 1.00 65.72 C ANISOU 2927 CA TYR A 416 8925 7466 8580 -782 -1337 704 C ATOM 2928 C TYR A 416 5.494 -0.288 -3.030 1.00 74.23 C ANISOU 2928 C TYR A 416 10136 8452 9617 -880 -1320 595 C ATOM 2929 O TYR A 416 4.629 0.058 -2.215 1.00 72.94 O ANISOU 2929 O TYR A 416 9706 8378 9627 -957 -1345 631 O ATOM 2930 CB TYR A 416 5.065 0.646 -5.312 1.00 62.97 C ANISOU 2930 CB TYR A 416 8626 7243 8059 -1034 -1533 831 C ATOM 2931 CG TYR A 416 5.257 1.800 -6.266 1.00 72.57 C ANISOU 2931 CG TYR A 416 9671 8573 9328 -975 -1592 1030 C ATOM 2932 CD1 TYR A 416 5.334 3.107 -5.802 1.00 77.77 C ANISOU 2932 CD1 TYR A 416 9966 9229 10353 -816 -1582 1149 C ATOM 2933 CD2 TYR A 416 5.362 1.584 -7.633 1.00 70.98 C ANISOU 2933 CD2 TYR A 416 9709 8467 8795 -1089 -1663 1103 C ATOM 2934 CE1 TYR A 416 5.505 4.166 -6.675 1.00 81.18 C ANISOU 2934 CE1 TYR A 416 10288 9707 10852 -788 -1652 1381 C ATOM 2935 CE2 TYR A 416 5.537 2.637 -8.513 1.00 78.84 C ANISOU 2935 CE2 TYR A 416 10587 9572 9796 -1063 -1716 1345 C ATOM 2936 CZ TYR A 416 5.608 3.925 -8.030 1.00 78.01 C ANISOU 2936 CZ TYR A 416 10131 9419 10091 -919 -1715 1507 C ATOM 2937 OH TYR A 416 5.781 4.974 -8.906 1.00 66.59 O ANISOU 2937 OH TYR A 416 8612 8022 8665 -917 -1783 1795 O ATOM 2938 N VAL A 417 6.036 -1.510 -3.031 1.00 75.00 N ANISOU 2938 N VAL A 417 10650 8367 9481 -873 -1268 468 N ATOM 2939 CA VAL A 417 5.682 -2.503 -2.019 1.00 75.22 C ANISOU 2939 CA VAL A 417 10882 8250 9450 -979 -1253 416 C ATOM 2940 C VAL A 417 6.049 -2.017 -0.621 1.00 75.65 C ANISOU 2940 C VAL A 417 10726 8332 9686 -769 -1144 400 C ATOM 2941 O VAL A 417 5.383 -2.367 0.363 1.00 73.28 O ANISOU 2941 O VAL A 417 10419 8044 9381 -909 -1125 429 O ATOM 2942 CB VAL A 417 6.357 -3.847 -2.359 1.00 69.42 C ANISOU 2942 CB VAL A 417 10679 7234 8461 -938 -1241 282 C ATOM 2943 CG1 VAL A 417 6.474 -4.740 -1.133 1.00 66.88 C ANISOU 2943 CG1 VAL A 417 10605 6693 8112 -911 -1204 262 C ATOM 2944 CG2 VAL A 417 5.575 -4.550 -3.446 1.00 68.97 C ANISOU 2944 CG2 VAL A 417 10878 7133 8193 -1268 -1387 262 C ATOM 2945 N ASN A 418 7.086 -1.184 -0.510 1.00 69.14 N ANISOU 2945 N ASN A 418 9719 7544 9007 -464 -1071 354 N ATOM 2946 CA ASN A 418 7.506 -0.674 0.790 1.00 59.69 C ANISOU 2946 CA ASN A 418 8331 6385 7962 -263 -1004 296 C ATOM 2947 C ASN A 418 6.365 0.000 1.544 1.00 72.46 C ANISOU 2947 C ASN A 418 9629 8176 9728 -397 -1007 338 C ATOM 2948 O ASN A 418 6.372 0.033 2.780 1.00 78.40 O ANISOU 2948 O ASN A 418 10330 8974 10483 -321 -946 277 O ATOM 2949 CB ASN A 418 8.666 0.302 0.607 1.00 65.48 C ANISOU 2949 CB ASN A 418 8842 7154 8882 6 -958 240 C ATOM 2950 CG ASN A 418 9.105 0.938 1.907 1.00 70.06 C ANISOU 2950 CG ASN A 418 9208 7784 9627 195 -932 141 C ATOM 2951 OD1 ASN A 418 9.915 0.373 2.644 1.00 72.31 O ANISOU 2951 OD1 ASN A 418 9648 8008 9820 376 -923 50 O ATOM 2952 ND2 ASN A 418 8.575 2.123 2.197 1.00 73.88 N ANISOU 2952 ND2 ASN A 418 9344 8372 10354 175 -946 143 N ATOM 2953 N SER A 419 5.371 0.528 0.828 1.00 73.71 N ANISOU 2953 N SER A 419 9563 8456 9988 -577 -1081 433 N ATOM 2954 CA SER A 419 4.257 1.208 1.479 1.00 74.87 C ANISOU 2954 CA SER A 419 9342 8795 10311 -653 -1075 444 C ATOM 2955 C SER A 419 3.387 0.269 2.304 1.00 71.13 C ANISOU 2955 C SER A 419 8963 8398 9665 -899 -1010 455 C ATOM 2956 O SER A 419 2.578 0.748 3.105 1.00 79.35 O ANISOU 2956 O SER A 419 9691 9646 10814 -930 -935 423 O ATOM 2957 CB SER A 419 3.402 1.927 0.433 1.00 76.98 C ANISOU 2957 CB SER A 419 9339 9174 10737 -757 -1215 564 C ATOM 2958 OG SER A 419 4.102 3.028 -0.124 1.00 76.00 O ANISOU 2958 OG SER A 419 9078 8985 10813 -542 -1256 597 O ATOM 2959 N ALA A 420 3.532 -1.043 2.146 1.00 64.52 N ANISOU 2959 N ALA A 420 8553 7392 8567 -1076 -1023 494 N ATOM 2960 CA ALA A 420 2.711 -1.998 2.873 1.00 70.62 C ANISOU 2960 CA ALA A 420 9465 8194 9173 -1382 -964 556 C ATOM 2961 C ALA A 420 3.486 -2.802 3.908 1.00 76.87 C ANISOU 2961 C ALA A 420 10638 8808 9762 -1279 -878 546 C ATOM 2962 O ALA A 420 2.886 -3.634 4.598 1.00 79.00 O ANISOU 2962 O ALA A 420 11085 9071 9862 -1550 -815 643 O ATOM 2963 CB ALA A 420 2.026 -2.954 1.892 1.00 69.09 C ANISOU 2963 CB ALA A 420 9496 7901 8853 -1760 -1092 637 C ATOM 2964 N VAL A 421 4.793 -2.590 4.035 1.00 77.91 N ANISOU 2964 N VAL A 421 10893 8806 9904 -910 -888 455 N ATOM 2965 CA VAL A 421 5.579 -3.412 4.946 1.00 79.27 C ANISOU 2965 CA VAL A 421 11443 8799 9879 -770 -869 464 C ATOM 2966 C VAL A 421 5.680 -2.792 6.335 1.00 78.59 C ANISOU 2966 C VAL A 421 11159 8929 9775 -616 -776 415 C ATOM 2967 O VAL A 421 5.844 -3.521 7.319 1.00 80.37 O ANISOU 2967 O VAL A 421 11677 9096 9766 -626 -753 490 O ATOM 2968 CB VAL A 421 6.980 -3.686 4.367 1.00 73.59 C ANISOU 2968 CB VAL A 421 10961 7841 9160 -437 -947 375 C ATOM 2969 CG1 VAL A 421 6.871 -4.312 2.991 1.00 71.39 C ANISOU 2969 CG1 VAL A 421 10910 7375 8838 -578 -1015 377 C ATOM 2970 CG2 VAL A 421 7.810 -2.409 4.324 1.00 65.73 C ANISOU 2970 CG2 VAL A 421 9584 7002 8387 -121 -934 246 C ATOM 2971 N ASN A 422 5.581 -1.466 6.440 1.00 74.03 N ANISOU 2971 N ASN A 422 10123 8582 9422 -475 -738 288 N ATOM 2972 CA ASN A 422 5.742 -0.820 7.742 1.00 73.83 C ANISOU 2972 CA ASN A 422 9929 8759 9366 -304 -662 170 C ATOM 2973 C ASN A 422 4.697 -1.265 8.756 1.00 74.68 C ANISOU 2973 C ASN A 422 10063 9076 9236 -564 -510 254 C ATOM 2974 O ASN A 422 5.081 -1.611 9.887 1.00 76.59 O ANISOU 2974 O ASN A 422 10516 9367 9218 -484 -475 261 O ATOM 2975 CB ASN A 422 5.757 0.700 7.560 1.00 72.41 C ANISOU 2975 CB ASN A 422 9279 8717 9517 -120 -663 -7 C ATOM 2976 CG ASN A 422 7.075 1.199 7.026 1.00 70.46 C ANISOU 2976 CG ASN A 422 9018 8305 9448 152 -777 -94 C ATOM 2977 OD1 ASN A 422 8.006 0.419 6.829 1.00 69.93 O ANISOU 2977 OD1 ASN A 422 9248 8068 9254 251 -842 -54 O ATOM 2978 ND2 ASN A 422 7.166 2.500 6.780 1.00 74.23 N ANISOU 2978 ND2 ASN A 422 9142 8823 10239 275 -798 -213 N ATOM 2979 N PRO A 423 3.396 -1.299 8.444 1.00 74.98 N ANISOU 2979 N PRO A 423 9889 9275 9326 -884 -418 332 N ATOM 2980 CA PRO A 423 2.439 -1.829 9.431 1.00 79.39 C ANISOU 2980 CA PRO A 423 10466 10068 9629 -1180 -229 435 C ATOM 2981 C PRO A 423 2.722 -3.267 9.832 1.00 83.90 C ANISOU 2981 C PRO A 423 11615 10404 9861 -1378 -249 663 C ATOM 2982 O PRO A 423 2.406 -3.662 10.961 1.00 90.16 O ANISOU 2982 O PRO A 423 12538 11363 10356 -1521 -99 763 O ATOM 2983 CB PRO A 423 1.089 -1.697 8.713 1.00 72.48 C ANISOU 2983 CB PRO A 423 9227 9375 8937 -1503 -180 488 C ATOM 2984 CG PRO A 423 1.299 -0.620 7.719 1.00 68.97 C ANISOU 2984 CG PRO A 423 8463 8890 8854 -1250 -321 353 C ATOM 2985 CD PRO A 423 2.703 -0.792 7.246 1.00 69.67 C ANISOU 2985 CD PRO A 423 8902 8634 8934 -993 -481 335 C ATOM 2986 N ILE A 424 3.313 -4.062 8.939 1.00 83.26 N ANISOU 2986 N ILE A 424 11907 9927 9801 -1380 -427 747 N ATOM 2987 CA ILE A 424 3.682 -5.430 9.285 1.00 83.10 C ANISOU 2987 CA ILE A 424 12489 9580 9504 -1500 -487 952 C ATOM 2988 C ILE A 424 4.819 -5.441 10.300 1.00 81.27 C ANISOU 2988 C ILE A 424 12492 9304 9083 -1119 -542 931 C ATOM 2989 O ILE A 424 4.919 -6.359 11.125 1.00 80.08 O ANISOU 2989 O ILE A 424 12773 9025 8629 -1213 -546 1138 O ATOM 2990 CB ILE A 424 4.040 -6.206 8.002 1.00 78.55 C ANISOU 2990 CB ILE A 424 12237 8582 9027 -1536 -666 971 C ATOM 2991 CG1 ILE A 424 2.825 -6.276 7.073 1.00 73.56 C ANISOU 2991 CG1 ILE A 424 11398 8028 8524 -1971 -654 1003 C ATOM 2992 CG2 ILE A 424 4.560 -7.600 8.325 1.00 80.22 C ANISOU 2992 CG2 ILE A 424 13116 8357 9008 -1567 -766 1149 C ATOM 2993 CD1 ILE A 424 3.095 -6.975 5.758 1.00 71.89 C ANISOU 2993 CD1 ILE A 424 11502 7446 8367 -2028 -834 970 C ATOM 2994 N ILE A 425 5.680 -4.422 10.275 1.00 72.91 N ANISOU 2994 N ILE A 425 11155 8352 8197 -705 -607 699 N ATOM 2995 CA ILE A 425 6.795 -4.363 11.215 1.00 77.19 C ANISOU 2995 CA ILE A 425 11857 8894 8577 -341 -708 646 C ATOM 2996 C ILE A 425 6.320 -3.961 12.608 1.00 86.64 C ANISOU 2996 C ILE A 425 12947 10469 9504 -403 -561 636 C ATOM 2997 O ILE A 425 6.863 -4.432 13.615 1.00 84.58 O ANISOU 2997 O ILE A 425 13008 10207 8921 -280 -633 733 O ATOM 2998 CB ILE A 425 7.877 -3.406 10.689 1.00 71.65 C ANISOU 2998 CB ILE A 425 10863 8188 8172 58 -830 392 C ATOM 2999 CG1 ILE A 425 8.343 -3.850 9.303 1.00 71.05 C ANISOU 2999 CG1 ILE A 425 10906 7796 8294 111 -926 402 C ATOM 3000 CG2 ILE A 425 9.062 -3.360 11.634 1.00 68.37 C ANISOU 3000 CG2 ILE A 425 10565 7798 7613 422 -980 318 C ATOM 3001 CD1 ILE A 425 9.377 -2.939 8.685 1.00 69.86 C ANISOU 3001 CD1 ILE A 425 10448 7667 8427 435 -1000 194 C ATOM 3002 N TYR A 426 5.302 -3.102 12.695 1.00 80.85 N ANISOU 3002 N TYR A 426 11769 10077 8874 -571 -359 514 N ATOM 3003 CA TYR A 426 4.811 -2.668 13.999 1.00 87.40 C ANISOU 3003 CA TYR A 426 12467 11316 9424 -609 -172 444 C ATOM 3004 C TYR A 426 4.159 -3.813 14.767 1.00 95.75 C ANISOU 3004 C TYR A 426 13906 12427 10045 -980 -30 771 C ATOM 3005 O TYR A 426 4.175 -3.815 16.004 1.00 99.16 O ANISOU 3005 O TYR A 426 14463 13130 10085 -961 67 794 O ATOM 3006 CB TYR A 426 3.826 -1.511 13.828 1.00 86.99 C ANISOU 3006 CB TYR A 426 11825 11596 9630 -664 22 214 C ATOM 3007 CG TYR A 426 4.370 -0.345 13.027 1.00 85.70 C ANISOU 3007 CG TYR A 426 11311 11332 9920 -350 -120 -55 C ATOM 3008 CD1 TYR A 426 5.706 0.027 13.118 1.00 83.30 C ANISOU 3008 CD1 TYR A 426 11097 10869 9684 2 -327 -201 C ATOM 3009 CD2 TYR A 426 3.547 0.381 12.176 1.00 83.93 C ANISOU 3009 CD2 TYR A 426 10656 11172 10061 -422 -61 -137 C ATOM 3010 CE1 TYR A 426 6.206 1.093 12.385 1.00 79.72 C ANISOU 3010 CE1 TYR A 426 10330 10311 9648 224 -438 -408 C ATOM 3011 CE2 TYR A 426 4.037 1.447 11.441 1.00 82.37 C ANISOU 3011 CE2 TYR A 426 10186 10845 10265 -163 -196 -323 C ATOM 3012 CZ TYR A 426 5.368 1.799 11.548 1.00 77.29 C ANISOU 3012 CZ TYR A 426 9656 10030 9679 135 -368 -452 C ATOM 3013 OH TYR A 426 5.859 2.858 10.815 1.00 65.48 O ANISOU 3013 OH TYR A 426 7898 8395 8588 330 -485 -601 O ATOM 3014 N THR A 427 3.583 -4.790 14.059 1.00 94.12 N ANISOU 3014 N THR A 427 13912 11967 9880 -1346 -21 1029 N ATOM 3015 CA THR A 427 2.981 -5.936 14.735 1.00 94.73 C ANISOU 3015 CA THR A 427 14395 12024 9574 -1766 104 1385 C ATOM 3016 C THR A 427 4.036 -6.873 15.301 1.00 93.77 C ANISOU 3016 C THR A 427 14923 11553 9151 -1581 -115 1608 C ATOM 3017 O THR A 427 3.779 -7.565 16.293 1.00107.23 O ANISOU 3017 O THR A 427 16989 13325 10429 -1808 -22 1896 O ATOM 3018 CB THR A 427 2.076 -6.711 13.777 1.00 92.02 C ANISOU 3018 CB THR A 427 14101 11462 9402 -2246 135 1572 C ATOM 3019 OG1 THR A 427 2.869 -7.267 12.722 1.00 87.69 O ANISOU 3019 OG1 THR A 427 13873 10378 9067 -2083 -148 1577 O ATOM 3020 CG2 THR A 427 1.028 -5.801 13.182 1.00 92.49 C ANISOU 3020 CG2 THR A 427 13488 11881 9771 -2397 298 1371 C ATOM 3021 N THR A 428 5.216 -6.918 14.687 1.00 86.78 N ANISOU 3021 N THR A 428 14188 10309 8477 -1167 -404 1497 N ATOM 3022 CA THR A 428 6.250 -7.850 15.112 1.00 80.90 C ANISOU 3022 CA THR A 428 14030 9197 7512 -924 -656 1699 C ATOM 3023 C THR A 428 7.087 -7.298 16.260 1.00 88.26 C ANISOU 3023 C THR A 428 14945 10410 8178 -536 -758 1595 C ATOM 3024 O THR A 428 7.228 -7.954 17.297 1.00 98.04 O ANISOU 3024 O THR A 428 16618 11653 8981 -567 -810 1867 O ATOM 3025 CB THR A 428 7.162 -8.200 13.934 1.00 75.14 C ANISOU 3025 CB THR A 428 13433 7992 7124 -626 -905 1599 C ATOM 3026 OG1 THR A 428 6.369 -8.438 12.764 1.00 66.95 O ANISOU 3026 OG1 THR A 428 12310 6784 6344 -965 -819 1592 O ATOM 3027 CG2 THR A 428 7.977 -9.450 14.258 1.00 74.10 C ANISOU 3027 CG2 THR A 428 13971 7385 6798 -439 -1156 1861 C ATOM 3028 N PHE A 429 7.642 -6.097 16.092 1.00 82.80 N ANISOU 3028 N PHE A 429 13778 9948 7733 -194 -807 1216 N ATOM 3029 CA PHE A 429 8.628 -5.569 17.024 1.00 85.65 C ANISOU 3029 CA PHE A 429 14115 10520 7909 205 -988 1057 C ATOM 3030 C PHE A 429 8.031 -4.731 18.145 1.00 88.27 C ANISOU 3030 C PHE A 429 14208 11398 7933 109 -780 904 C ATOM 3031 O PHE A 429 8.759 -4.373 19.077 1.00 94.52 O ANISOU 3031 O PHE A 429 15046 12401 8467 386 -940 780 O ATOM 3032 CB PHE A 429 9.666 -4.731 16.274 1.00 81.51 C ANISOU 3032 CB PHE A 429 13220 9923 7826 606 -1176 717 C ATOM 3033 CG PHE A 429 10.610 -5.545 15.451 1.00 86.84 C ANISOU 3033 CG PHE A 429 14151 10141 8702 848 -1415 814 C ATOM 3034 CD1 PHE A 429 11.723 -6.132 16.031 1.00 95.71 C ANISOU 3034 CD1 PHE A 429 15590 11131 9647 1208 -1714 909 C ATOM 3035 CD2 PHE A 429 10.383 -5.736 14.099 1.00 90.50 C ANISOU 3035 CD2 PHE A 429 14539 10330 9515 740 -1348 797 C ATOM 3036 CE1 PHE A 429 12.597 -6.891 15.275 1.00100.77 C ANISOU 3036 CE1 PHE A 429 16434 11359 10493 1488 -1918 962 C ATOM 3037 CE2 PHE A 429 11.253 -6.492 13.334 1.00 94.15 C ANISOU 3037 CE2 PHE A 429 15239 10395 10137 990 -1533 835 C ATOM 3038 CZ PHE A 429 12.362 -7.070 13.923 1.00 99.97 C ANISOU 3038 CZ PHE A 429 16261 10992 10733 1381 -1805 907 C ATOM 3039 N ASN A 430 6.743 -4.409 18.090 1.00 83.72 N ANISOU 3039 N ASN A 430 13363 11080 7368 -257 -438 882 N ATOM 3040 CA ASN A 430 6.116 -3.571 19.103 1.00 88.98 C ANISOU 3040 CA ASN A 430 13756 12293 7759 -315 -190 673 C ATOM 3041 C ASN A 430 4.910 -4.295 19.678 1.00 94.26 C ANISOU 3041 C ASN A 430 14603 13185 8026 -804 139 994 C ATOM 3042 O ASN A 430 3.949 -4.578 18.954 1.00 90.37 O ANISOU 3042 O ASN A 430 13952 12628 7755 -1162 332 1116 O ATOM 3043 CB ASN A 430 5.708 -2.218 18.523 1.00 82.34 C ANISOU 3043 CB ASN A 430 12274 11632 7378 -219 -60 251 C ATOM 3044 CG ASN A 430 5.177 -1.278 19.577 1.00 86.94 C ANISOU 3044 CG ASN A 430 12575 12746 7711 -183 175 -57 C ATOM 3045 OD1 ASN A 430 3.978 -1.247 19.844 1.00 86.57 O ANISOU 3045 OD1 ASN A 430 12339 13023 7531 -474 525 -28 O ATOM 3046 ND2 ASN A 430 6.069 -0.510 20.193 1.00 93.49 N ANISOU 3046 ND2 ASN A 430 13362 13689 8473 174 -14 -380 N ATOM 3047 N ILE A 431 4.963 -4.590 20.979 1.00 96.66 N ANISOU 3047 N ILE A 431 15226 13779 7721 -842 197 1137 N ATOM 3048 CA ILE A 431 3.848 -5.262 21.638 1.00 92.58 C ANISOU 3048 CA ILE A 431 14883 13536 6757 -1346 552 1472 C ATOM 3049 C ILE A 431 2.630 -4.348 21.695 1.00 98.55 C ANISOU 3049 C ILE A 431 15013 14819 7614 -1537 984 1175 C ATOM 3050 O ILE A 431 1.488 -4.806 21.569 1.00 98.81 O ANISOU 3050 O ILE A 431 14936 14997 7611 -2018 1303 1397 O ATOM 3051 CB ILE A 431 4.263 -5.738 23.042 1.00 91.00 C ANISOU 3051 CB ILE A 431 15200 13558 5818 -1318 503 1710 C ATOM 3052 N GLU A 432 2.851 -3.043 21.881 1.00 96.20 N ANISOU 3052 N GLU A 432 14279 14803 7470 -1163 992 657 N ATOM 3053 CA GLU A 432 1.733 -2.109 21.979 1.00 93.30 C ANISOU 3053 CA GLU A 432 13305 14920 7225 -1248 1385 325 C ATOM 3054 C GLU A 432 1.005 -1.971 20.646 1.00 90.82 C ANISOU 3054 C GLU A 432 12560 14400 7549 -1408 1437 316 C ATOM 3055 O GLU A 432 -0.230 -1.927 20.610 1.00 84.30 O ANISOU 3055 O GLU A 432 11363 13912 6757 -1725 1791 333 O ATOM 3056 CB GLU A 432 2.229 -0.750 22.471 1.00 88.42 C ANISOU 3056 CB GLU A 432 12394 14544 6659 -774 1324 -250 C ATOM 3057 N PHE A 433 1.747 -1.901 19.538 1.00 90.26 N ANISOU 3057 N PHE A 433 12509 13817 7970 -1197 1087 288 N ATOM 3058 CA PHE A 433 1.098 -1.850 18.232 1.00 93.03 C ANISOU 3058 CA PHE A 433 12520 13969 8860 -1363 1090 317 C ATOM 3059 C PHE A 433 0.366 -3.155 17.929 1.00 92.59 C ANISOU 3059 C PHE A 433 12717 13789 8674 -1909 1194 776 C ATOM 3060 O PHE A 433 -0.768 -3.136 17.438 1.00 86.48 O ANISOU 3060 O PHE A 433 11554 13195 8111 -2229 1396 805 O ATOM 3061 CB PHE A 433 2.125 -1.540 17.137 1.00 94.23 C ANISOU 3061 CB PHE A 433 12696 13628 9479 -1036 712 208 C ATOM 3062 CG PHE A 433 2.253 -0.070 16.807 1.00 90.02 C ANISOU 3062 CG PHE A 433 11657 13176 9371 -672 669 -233 C ATOM 3063 CD1 PHE A 433 1.220 0.604 16.178 1.00 82.18 C ANISOU 3063 CD1 PHE A 433 10137 12335 8753 -746 821 -367 C ATOM 3064 CD2 PHE A 433 3.413 0.630 17.106 1.00 88.82 C ANISOU 3064 CD2 PHE A 433 11559 12920 9269 -265 446 -498 C ATOM 3065 CE1 PHE A 433 1.331 1.949 15.867 1.00 78.56 C ANISOU 3065 CE1 PHE A 433 9265 11877 8709 -401 756 -738 C ATOM 3066 CE2 PHE A 433 3.531 1.976 16.796 1.00 82.75 C ANISOU 3066 CE2 PHE A 433 10368 12155 8919 24 394 -882 C ATOM 3067 CZ PHE A 433 2.487 2.635 16.177 1.00 81.74 C ANISOU 3067 CZ PHE A 433 9768 12128 9161 -34 550 -991 C ATOM 3068 N ARG A 434 0.991 -4.296 18.232 1.00 96.08 N ANISOU 3068 N ARG A 434 13805 13913 8786 -2025 1037 1134 N ATOM 3069 CA ARG A 434 0.385 -5.588 17.918 1.00 91.88 C ANISOU 3069 CA ARG A 434 13600 13146 8164 -2562 1089 1576 C ATOM 3070 C ARG A 434 -0.930 -5.778 18.663 1.00 88.38 C ANISOU 3070 C ARG A 434 12942 13229 7411 -3068 1532 1730 C ATOM 3071 O ARG A 434 -1.944 -6.162 18.068 1.00 89.59 O ANISOU 3071 O ARG A 434 12864 13413 7764 -3530 1674 1870 O ATOM 3072 CB ARG A 434 1.360 -6.718 18.249 1.00 91.99 C ANISOU 3072 CB ARG A 434 14390 12689 7871 -2520 823 1923 C ATOM 3073 N LYS A 435 -0.934 -5.515 19.973 1.00 92.30 N ANISOU 3073 N LYS A 435 13491 14183 7397 -3005 1759 1697 N ATOM 3074 CA LYS A 435 -2.157 -5.679 20.753 1.00 95.80 C ANISOU 3074 CA LYS A 435 13709 15207 7485 -3485 2243 1837 C ATOM 3075 C LYS A 435 -3.199 -4.633 20.385 1.00 95.39 C ANISOU 3075 C LYS A 435 12798 15636 7810 -3466 2525 1447 C ATOM 3076 O LYS A 435 -4.399 -4.865 20.566 1.00100.11 O ANISOU 3076 O LYS A 435 13054 16654 8329 -3942 2904 1572 O ATOM 3077 CB LYS A 435 -1.843 -5.617 22.249 1.00100.45 C ANISOU 3077 CB LYS A 435 14594 16206 7366 -3383 2418 1871 C ATOM 3078 N ALA A 436 -2.763 -3.482 19.869 1.00 97.48 N ANISOU 3078 N ALA A 436 12695 15840 8503 -2926 2339 989 N ATOM 3079 CA ALA A 436 -3.711 -2.457 19.446 1.00 99.12 C ANISOU 3079 CA ALA A 436 12109 16422 9131 -2835 2542 627 C ATOM 3080 C ALA A 436 -4.463 -2.884 18.193 1.00 98.71 C ANISOU 3080 C ALA A 436 11791 16164 9549 -3194 2456 809 C ATOM 3081 O ALA A 436 -5.682 -2.702 18.103 1.00 98.79 O ANISOU 3081 O ALA A 436 11222 16613 9701 -3464 2744 764 O ATOM 3082 CB ALA A 436 -2.984 -1.133 19.210 1.00 94.08 C ANISOU 3082 CB ALA A 436 11230 15675 8839 -2179 2321 134 C ATOM 3083 N PHE A 437 -3.753 -3.456 17.217 1.00 90.64 N ANISOU 3083 N PHE A 437 11168 14510 8763 -3193 2056 991 N ATOM 3084 CA PHE A 437 -4.405 -3.888 15.985 1.00 89.75 C ANISOU 3084 CA PHE A 437 10864 14185 9052 -3536 1925 1136 C ATOM 3085 C PHE A 437 -5.403 -5.004 16.256 1.00 98.61 C ANISOU 3085 C PHE A 437 12055 15479 9935 -4263 2173 1518 C ATOM 3086 O PHE A 437 -6.491 -5.031 15.669 1.00 97.68 O ANISOU 3086 O PHE A 437 11436 15585 10092 -4617 2265 1534 O ATOM 3087 CB PHE A 437 -3.365 -4.353 14.965 1.00 85.17 C ANISOU 3087 CB PHE A 437 10775 12904 8681 -3381 1477 1231 C ATOM 3088 CG PHE A 437 -2.480 -3.255 14.437 1.00 86.40 C ANISOU 3088 CG PHE A 437 10779 12886 9165 -2763 1230 890 C ATOM 3089 CD1 PHE A 437 -2.661 -1.937 14.822 1.00 90.40 C ANISOU 3089 CD1 PHE A 437 10767 13767 9814 -2388 1365 522 C ATOM 3090 CD2 PHE A 437 -1.469 -3.548 13.540 1.00 80.59 C ANISOU 3090 CD2 PHE A 437 10422 11598 8603 -2569 873 931 C ATOM 3091 CE1 PHE A 437 -1.838 -0.938 14.328 1.00 85.90 C ANISOU 3091 CE1 PHE A 437 10090 12981 9568 -1879 1127 241 C ATOM 3092 CE2 PHE A 437 -0.645 -2.555 13.044 1.00 80.08 C ANISOU 3092 CE2 PHE A 437 10206 11388 8833 -2065 672 655 C ATOM 3093 CZ PHE A 437 -0.831 -1.248 13.438 1.00 81.28 C ANISOU 3093 CZ PHE A 437 9867 11875 9140 -1744 789 329 C ATOM 3094 N LEU A 438 -5.047 -5.938 17.144 1.00 97.43 N ANISOU 3094 N LEU A 438 12520 15222 9276 -4511 2262 1848 N ATOM 3095 CA LEU A 438 -5.930 -7.059 17.446 1.00 99.16 C ANISOU 3095 CA LEU A 438 12887 15540 9250 -5265 2497 2270 C ATOM 3096 C LEU A 438 -7.187 -6.605 18.176 1.00104.88 C ANISOU 3096 C LEU A 438 12926 17091 9832 -5548 3020 2189 C ATOM 3097 O LEU A 438 -8.233 -7.257 18.066 1.00112.28 O ANISOU 3097 O LEU A 438 13646 18228 10786 -6211 3228 2440 O ATOM 3098 CB LEU A 438 -5.179 -8.106 18.269 1.00101.79 C ANISOU 3098 CB LEU A 438 14093 15526 9057 -5410 2445 2676 C ATOM 3099 N LYS A 439 -7.108 -5.501 18.923 1.00104.77 N ANISOU 3099 N LYS A 439 12553 17573 9684 -5064 3242 1817 N ATOM 3100 CA LYS A 439 -8.295 -4.960 19.574 1.00111.86 C ANISOU 3100 CA LYS A 439 12728 19296 10480 -5232 3763 1648 C ATOM 3101 C LYS A 439 -9.200 -4.234 18.588 1.00113.57 C ANISOU 3101 C LYS A 439 12089 19730 11334 -5165 3740 1359 C ATOM 3102 O LYS A 439 -10.419 -4.192 18.788 1.00116.22 O ANISOU 3102 O LYS A 439 11788 20658 11710 -5514 4113 1349 O ATOM 3103 CB LYS A 439 -7.894 -4.019 20.711 1.00111.35 C ANISOU 3103 CB LYS A 439 12602 19665 10042 -4703 3997 1288 C ATOM 3104 N ILE A 440 -8.629 -3.664 17.526 1.00111.11 N ANISOU 3104 N ILE A 440 11741 18958 11519 -4713 3295 1139 N ATOM 3105 CA ILE A 440 -9.451 -3.036 16.502 1.00110.51 C ANISOU 3105 CA ILE A 440 10923 19028 12037 -4650 3192 931 C ATOM 3106 C ILE A 440 -10.182 -4.088 15.675 1.00112.85 C ANISOU 3106 C ILE A 440 11191 19185 12503 -5352 3077 1285 C ATOM 3107 O ILE A 440 -11.326 -3.874 15.259 1.00112.91 O ANISOU 3107 O ILE A 440 10465 19613 12823 -5584 3184 1219 O ATOM 3108 CB ILE A 440 -8.581 -2.115 15.629 1.00104.69 C ANISOU 3108 CB ILE A 440 10219 17834 11725 -3988 2753 640 C ATOM 3109 CG1 ILE A 440 -7.927 -1.040 16.500 1.00107.61 C ANISOU 3109 CG1 ILE A 440 10580 18352 11953 -3351 2868 257 C ATOM 3110 CG2 ILE A 440 -9.411 -1.469 14.537 1.00101.39 C ANISOU 3110 CG2 ILE A 440 9088 17539 11896 -3905 2594 477 C ATOM 3111 CD1 ILE A 440 -7.131 -0.015 15.728 1.00100.57 C ANISOU 3111 CD1 ILE A 440 9658 17052 11502 -2734 2483 -35 C ATOM 3112 N LEU A 441 -9.554 -5.245 15.440 1.00112.02 N ANISOU 3112 N LEU A 441 11866 18490 12207 -5698 2844 1648 N ATOM 3113 CA LEU A 441 -10.167 -6.342 14.697 1.00113.38 C ANISOU 3113 CA LEU A 441 12136 18432 12510 -6402 2704 1969 C ATOM 3114 C LEU A 441 -10.959 -7.287 15.593 1.00125.26 C ANISOU 3114 C LEU A 441 13779 20090 13724 -6864 2989 2236 C ATOM 3115 O LEU A 441 -11.000 -8.499 15.335 1.00130.59 O ANISOU 3115 O LEU A 441 14979 20276 14364 -7284 2800 2536 O ATOM 3116 CB LEU A 441 -9.096 -7.115 13.924 1.00105.56 C ANISOU 3116 CB LEU A 441 11981 16582 11546 -6372 2234 2137 C ATOM 3117 CG LEU A 441 -8.272 -6.304 12.915 1.00100.01 C ANISOU 3117 CG LEU A 441 11276 15521 11203 -5710 1825 1833 C ATOM 3118 CD1 LEU A 441 -7.049 -7.083 12.435 1.00 92.92 C ANISOU 3118 CD1 LEU A 441 11249 13839 10218 -5600 1460 1975 C ATOM 3119 CD2 LEU A 441 -9.133 -5.880 11.735 1.00101.27 C ANISOU 3119 CD2 LEU A 441 10791 15843 11843 -5803 1635 1687 C ATOM 3120 N HIS A 442 -11.587 -6.766 16.640 1.00118.20 N ANISOU 3120 N HIS A 442 12431 19851 12628 -6779 3439 2114 N ATOM 3121 CA HIS A 442 -12.365 -7.591 17.554 1.00126.48 C ANISOU 3121 CA HIS A 442 13562 21110 13385 -7224 3754 2376 C ATOM 3122 C HIS A 442 -13.375 -6.752 18.337 1.00131.96 C ANISOU 3122 C HIS A 442 13462 22622 14057 -7071 4227 2114 C ATOM 3123 O HIS A 442 -14.028 -5.864 17.785 1.00131.46 O ANISOU 3123 O HIS A 442 12638 22887 14424 -6809 4221 1787 O ATOM 3124 CB HIS A 442 -11.436 -8.335 18.515 1.00127.27 C ANISOU 3124 CB HIS A 442 14545 20900 12913 -7295 3807 2692 C TER 3125 HIS A 442 HETATM 3126 C01 8NU A2001 5.798 4.520 -12.898 1.00 53.67 C HETATM 3127 C02 8NU A2001 7.144 4.033 -13.365 1.00 73.44 C HETATM 3128 C03 8NU A2001 8.262 4.600 -12.909 1.00 81.52 C HETATM 3129 C04 8NU A2001 8.206 5.746 -11.897 1.00 83.19 C HETATM 3130 C05 8NU A2001 8.798 5.236 -10.556 1.00 77.95 C HETATM 3131 C07 8NU A2001 9.857 7.323 -9.903 1.00 83.90 C HETATM 3132 C08 8NU A2001 10.085 8.347 -8.777 1.00 87.68 C HETATM 3133 C09 8NU A2001 10.598 7.582 -7.553 1.00 81.18 C HETATM 3134 C10 8NU A2001 9.569 6.528 -7.120 1.00 68.50 C HETATM 3135 C11 8NU A2001 9.363 5.565 -8.280 1.00 79.77 C HETATM 3136 C12 8NU A2001 10.978 8.513 -6.434 1.00 83.67 C HETATM 3137 C15 8NU A2001 11.604 9.387 -4.561 1.00 77.42 C HETATM 3138 C16 8NU A2001 11.346 8.184 -5.148 1.00 77.32 C HETATM 3139 C17 8NU A2001 11.480 6.976 -4.482 1.00 58.28 C HETATM 3140 C18 8NU A2001 11.893 7.042 -3.152 1.00 57.84 C HETATM 3141 C19 8NU A2001 12.158 8.271 -2.538 1.00 70.59 C HETATM 3142 C21 8NU A2001 12.017 9.471 -3.239 1.00 71.68 C HETATM 3143 C22 8NU A2001 9.544 4.089 -13.391 1.00 77.92 C HETATM 3144 C25 8NU A2001 10.828 2.550 -14.812 1.00 72.98 C HETATM 3145 C26 8NU A2001 10.659 1.689 -16.072 1.00 63.09 C HETATM 3146 C27 8NU A2001 9.633 0.613 -15.771 1.00 79.48 C HETATM 3147 C28 8NU A2001 8.257 1.284 -15.641 1.00 81.12 C HETATM 3148 C29 8NU A2001 8.311 2.465 -14.703 1.00 76.00 C HETATM 3149 F20 8NU A2001 12.555 8.290 -1.257 1.00 71.11 F HETATM 3150 N06 8NU A2001 8.882 6.272 -9.486 1.00 82.54 N HETATM 3151 N13 8NU A2001 11.047 9.842 -6.521 1.00 87.02 N HETATM 3152 N24 8NU A2001 9.552 3.033 -14.306 1.00 78.56 N HETATM 3153 N30 8NU A2001 7.209 2.946 -14.270 1.00 76.66 N HETATM 3154 O14 8NU A2001 11.404 10.328 -5.431 1.00 84.77 O HETATM 3155 O23 8NU A2001 10.714 4.653 -12.983 1.00 74.60 O HETATM 3156 C1 PEG A2002 13.738 19.153 11.296 1.00 72.10 C HETATM 3157 O1 PEG A2002 13.425 19.871 12.503 1.00 65.09 O HETATM 3158 C2 PEG A2002 12.621 18.262 10.668 1.00 83.14 C HETATM 3159 O2 PEG A2002 12.675 18.051 9.395 1.00 87.46 O HETATM 3160 C3 PEG A2002 12.767 16.692 8.891 1.00 81.97 C HETATM 3161 C4 PEG A2002 12.969 16.518 7.378 1.00 79.46 C HETATM 3162 O4 PEG A2002 14.040 17.136 6.817 1.00 81.73 O HETATM 3163 C1 PEG A2003 22.198 2.267 14.051 1.00 85.07 C HETATM 3164 O1 PEG A2003 22.242 2.005 12.633 1.00 77.13 O HETATM 3165 C2 PEG A2003 20.827 2.102 14.782 1.00 84.42 C HETATM 3166 O2 PEG A2003 20.817 2.118 16.075 1.00 85.32 O HETATM 3167 C3 PEG A2003 19.883 1.249 16.778 1.00 93.34 C HETATM 3168 C4 PEG A2003 20.010 1.103 18.306 1.00 94.49 C HETATM 3169 O4 PEG A2003 21.115 0.493 18.807 1.00 88.36 O HETATM 3170 C1 PEG A2004 -5.266 7.216 -12.595 1.00 78.78 C HETATM 3171 O1 PEG A2004 -5.406 6.769 -13.959 1.00 82.42 O HETATM 3172 C2 PEG A2004 -6.274 8.287 -12.075 1.00 83.69 C HETATM 3173 O2 PEG A2004 -5.917 9.017 -11.072 1.00 95.26 O HETATM 3174 C3 PEG A2004 -6.353 8.668 -9.728 1.00 95.45 C HETATM 3175 C4 PEG A2004 -6.658 9.830 -8.768 1.00 93.47 C HETATM 3176 O4 PEG A2004 -5.847 10.916 -8.828 1.00 94.71 O HETATM 3177 C1 OLA A2005 19.754 16.684 15.996 1.00103.47 C HETATM 3178 O1 OLA A2005 19.134 17.736 15.945 1.00106.47 O1- HETATM 3179 O2 OLA A2005 19.858 16.092 17.050 1.00100.57 O HETATM 3180 C2 OLA A2005 20.380 16.079 14.781 1.00100.30 C HETATM 3181 C3 OLA A2005 21.721 15.459 15.111 1.00 85.16 C HETATM 3182 C4 OLA A2005 22.296 14.616 13.989 1.00 75.85 C HETATM 3183 C5 OLA A2005 22.315 15.351 12.658 1.00 76.55 C HETATM 3184 C6 OLA A2005 23.649 15.221 11.960 1.00 84.25 C HETATM 3185 C7 OLA A2005 23.502 15.265 10.460 1.00 79.47 C HETATM 3186 C8 OLA A2005 23.089 16.616 9.956 1.00 79.39 C HETATM 3187 C9 OLA A2005 23.686 16.861 8.593 1.00 69.85 C HETATM 3188 C10 OLA A2005 24.899 17.367 8.461 1.00 53.24 C HETATM 3189 C11 OLA A2005 25.483 17.608 7.100 1.00 53.87 C HETATM 3190 C1 OLA A2006 20.492 1.698 9.419 1.00 90.11 C HETATM 3191 O1 OLA A2006 20.499 0.477 9.482 1.00 88.05 O1- HETATM 3192 O2 OLA A2006 21.139 2.360 10.195 1.00 99.57 O HETATM 3193 C2 OLA A2006 19.685 2.399 8.399 1.00 78.95 C HETATM 3194 C3 OLA A2006 20.418 3.603 7.911 1.00 70.44 C HETATM 3195 C4 OLA A2006 19.398 4.667 7.677 1.00 69.07 C HETATM 3196 C5 OLA A2006 18.568 4.321 6.487 1.00 67.97 C HETATM 3197 C6 OLA A2006 18.593 5.497 5.570 1.00 62.32 C HETATM 3198 C7 OLA A2006 17.322 6.257 5.694 1.00 57.29 C HETATM 3199 C8 OLA A2006 17.070 6.697 4.296 1.00 63.53 C HETATM 3200 C9 OLA A2006 15.693 7.225 4.217 1.00 74.02 C HETATM 3201 C10 OLA A2006 15.463 8.094 3.273 1.00 81.56 C HETATM 3202 C1 OLA A2007 20.946 19.605 5.507 1.00104.81 C HETATM 3203 O1 OLA A2007 20.786 19.480 4.293 1.00106.45 O1- HETATM 3204 O2 OLA A2007 21.833 19.000 6.102 1.00106.45 O HETATM 3205 C2 OLA A2007 20.063 20.532 6.282 1.00 99.47 C HETATM 3206 C3 OLA A2007 19.930 20.039 7.714 1.00 92.83 C HETATM 3207 C4 OLA A2007 19.660 21.205 8.650 1.00 89.51 C HETATM 3208 C5 OLA A2007 18.925 20.737 9.890 1.00 90.62 C HETATM 3209 C6 OLA A2007 18.698 21.919 10.797 1.00 87.43 C HETATM 3210 C7 OLA A2007 19.145 21.568 12.187 1.00 87.56 C HETATM 3211 C8 OLA A2007 17.984 21.172 13.062 1.00 92.99 C HETATM 3212 C9 OLA A2007 18.045 22.031 14.289 1.00 97.77 C HETATM 3213 C10 OLA A2007 17.496 21.625 15.424 1.00104.05 C HETATM 3214 C11 OLA A2007 16.783 20.300 15.516 1.00106.41 C HETATM 3215 C12 OLA A2007 15.861 20.259 16.733 1.00108.65 C HETATM 3216 C13 OLA A2007 16.546 20.802 17.987 1.00108.30 C HETATM 3217 C14 OLA A2007 16.078 20.161 19.288 1.00104.26 C HETATM 3218 C15 OLA A2007 15.097 21.040 20.036 1.00103.67 C HETATM 3219 C16 OLA A2007 14.019 21.544 19.086 1.00108.16 C HETATM 3220 C17 OLA A2007 13.012 22.466 19.761 1.00101.56 C HETATM 3221 C18 OLA A2007 12.822 23.759 18.999 1.00 93.87 C HETATM 3222 O HOH A2101 15.559 11.273 -16.923 1.00 85.24 O HETATM 3223 O HOH A2102 13.685 6.206 10.425 1.00 56.75 O HETATM 3224 O HOH A2103 11.676 4.647 10.912 1.00 71.92 O HETATM 3225 O HOH A2104 51.603 -6.966 43.388 1.00114.99 O HETATM 3226 O HOH A2105 13.506 9.763 -16.484 1.00 75.43 O HETATM 3227 O HOH A2106 6.801 19.222 -16.747 1.00 81.47 O HETATM 3228 O HOH A2107 50.953 6.133 28.786 1.00111.89 O HETATM 3229 O HOH A2108 0.325 -2.269 5.124 1.00 63.44 O HETATM 3230 O HOH A2109 18.297 11.785 27.570 1.00 76.28 O HETATM 3231 O HOH A2110 25.722 -23.567 29.432 1.00109.39 O HETATM 3232 O HOH A2111 39.760 0.401 36.535 1.00 72.69 O HETATM 3233 O HOH A2112 12.468 7.264 -12.152 1.00 90.82 O HETATM 3234 O HOH A2113 41.115 12.799 34.547 1.00 88.30 O HETATM 3235 O HOH A2114 17.478 -27.491 32.936 1.00101.23 O HETATM 3236 O HOH A2115 6.185 -5.781 -16.925 1.00 97.58 O HETATM 3237 O HOH A2116 -8.638 -1.389 -3.037 1.00 71.84 O CONECT 542 1057 CONECT 1057 542 CONECT 2807 2818 CONECT 2818 2807 CONECT 3126 3127 CONECT 3127 3126 3128 3153 CONECT 3128 3127 3129 3143 CONECT 3129 3128 3130 CONECT 3130 3129 3150 CONECT 3131 3132 3150 CONECT 3132 3131 3133 CONECT 3133 3132 3134 3136 CONECT 3134 3133 3135 CONECT 3135 3134 3150 CONECT 3136 3133 3138 3151 CONECT 3137 3138 3142 3154 CONECT 3138 3136 3137 3139 CONECT 3139 3138 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 3149 CONECT 3142 3137 3141 CONECT 3143 3128 3152 3155 CONECT 3144 3145 3152 CONECT 3145 3144 3146 CONECT 3146 3145 3147 CONECT 3147 3146 3148 CONECT 3148 3147 3152 3153 CONECT 3149 3141 CONECT 3150 3130 3131 3135 CONECT 3151 3136 3154 CONECT 3152 3143 3144 3148 CONECT 3153 3127 3148 CONECT 3154 3137 3151 CONECT 3155 3143 CONECT 3156 3157 3158 CONECT 3157 3156 CONECT 3158 3156 3159 CONECT 3159 3158 3160 CONECT 3160 3159 3161 CONECT 3161 3160 3162 CONECT 3162 3161 CONECT 3163 3164 3165 CONECT 3164 3163 CONECT 3165 3163 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3168 CONECT 3168 3167 3169 CONECT 3169 3168 CONECT 3170 3171 3172 CONECT 3171 3170 CONECT 3172 3170 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 CONECT 3177 3178 3179 3180 CONECT 3178 3177 CONECT 3179 3177 CONECT 3180 3177 3181 CONECT 3181 3180 3182 CONECT 3182 3181 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 CONECT 3185 3184 3186 CONECT 3186 3185 3187 CONECT 3187 3186 3188 CONECT 3188 3187 3189 CONECT 3189 3188 CONECT 3190 3191 3192 3193 CONECT 3191 3190 CONECT 3192 3190 CONECT 3193 3190 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 CONECT 3198 3197 3199 CONECT 3199 3198 3200 CONECT 3200 3199 3201 CONECT 3201 3200 CONECT 3202 3203 3204 3205 CONECT 3203 3202 CONECT 3204 3202 CONECT 3205 3202 3206 CONECT 3206 3205 3207 CONECT 3207 3206 3208 CONECT 3208 3207 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3214 3216 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 CONECT 3221 3220 MASTER 364 0 7 22 3 0 0 6 3236 1 100 34 END