HEADER MEMBRANE PROTEIN 12-JUN-19 6RZ6 TITLE CRYSTAL STRUCTURE OF THE HUMAN CYSTEINYL LEUKOTRIENE RECEPTOR 2 IN TITLE 2 COMPLEX WITH ONO-2570366 (C2221 SPACE GROUP) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CYSTEINYL LEUKOTRIENE RECEPTOR 2,SOLUBLE CYTOCHROME B562, COMPND 3 CYSTEINYL LEUKOTRIENE RECEPTOR 2; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYSLTR2,G-PROTEIN COUPLED RECEPTOR GPCR21,HGPCR21,G-PROTEIN COMPND 6 COUPLED RECEPTOR HG57,HPN321,CYTOCHROME B-562,CYSLTR2,G-PROTEIN COMPND 7 COUPLED RECEPTOR GPCR21,HGPCR21,G-PROTEIN COUPLED RECEPTOR HG57, COMPND 8 HPN321; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: CYSLTR2, CYSLT2, CYSLT2R, PSEC0146, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, LCP, MEMBRANE PROTEIN, CYSTEINYL LEUKOTRIENE, CYSLT2, CYSLTR2, KEYWDS 2 CYSLT2R, ASTHMA, BRIL, CYSTEINYL LEUKOTRIENE RECEPTOR 2 EXPDTA X-RAY DIFFRACTION AUTHOR A.GUSACH,A.LUGININA,E.MARIN,R.L.BROUILLETTE,E.BESSERER-OFFROY, AUTHOR 2 J.M.LONGPRE,A.ISHCHENKO,P.POPOV,T.FUJIMOTO,T.MARUYAMA,B.STAUCH, AUTHOR 3 M.ERGASHEVA,D.ROMANOVSKAYA,A.STEPKO,K.KOVALEV,M.SHEVTSOV,V.GORDELIY, AUTHOR 4 G.W.HAN,P.SARRET,V.KATRITCH,V.BORSHCHEVSKIY,A.MISHIN,V.CHEREZOV REVDAT 3 30-MAR-22 6RZ6 1 COMPND HETNAM REVDAT 2 18-DEC-19 6RZ6 1 JRNL REVDAT 1 11-DEC-19 6RZ6 0 JRNL AUTH A.GUSACH,A.LUGININA,E.MARIN,R.L.BROUILLETTE, JRNL AUTH 2 E.BESSERER-OFFROY,J.M.LONGPRE,A.ISHCHENKO,P.POPOV,N.PATEL, JRNL AUTH 3 T.FUJIMOTO,T.MARUYAMA,B.STAUCH,M.ERGASHEVA,D.ROMANOVSKAIA, JRNL AUTH 4 A.STEPKO,K.KOVALEV,M.SHEVTSOV,V.GORDELIY,G.W.HAN,V.KATRITCH, JRNL AUTH 5 V.BORSHCHEVSKIY,P.SARRET,A.MISHIN,V.CHEREZOV JRNL TITL STRUCTURAL BASIS OF LIGAND SELECTIVITY AND DISEASE MUTATIONS JRNL TITL 2 IN CYSTEINYL LEUKOTRIENE RECEPTORS. JRNL REF NAT COMMUN V. 10 5573 2019 JRNL REFN ESSN 2041-1723 JRNL PMID 31811124 JRNL DOI 10.1038/S41467-019-13348-2 REMARK 2 REMARK 2 RESOLUTION. 2.43 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.12-2829 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 3 NUMBER OF REFLECTIONS : 19660 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.196 REMARK 3 R VALUE (WORKING SET) : 0.194 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 982 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 28.9029 - 4.6430 0.99 2775 145 0.1903 0.2431 REMARK 3 2 4.6430 - 3.6877 1.00 2686 143 0.1583 0.1798 REMARK 3 3 3.6877 - 3.2222 1.00 2676 139 0.1935 0.2146 REMARK 3 4 3.2222 - 2.9279 1.00 2658 140 0.2180 0.2617 REMARK 3 5 2.9279 - 2.7182 1.00 2635 139 0.2195 0.2940 REMARK 3 6 2.7182 - 2.5581 1.00 2634 139 0.2512 0.2966 REMARK 3 7 2.5581 - 2.4300 1.00 2614 137 0.2713 0.3235 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.520 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 51.50 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 : 0.006 3328 REMARK 3 ANGLE : 1.022 4401 REMARK 3 CHIRALITY : 0.056 503 REMARK 3 PLANARITY : 0.007 515 REMARK 3 DIHEDRAL : 11.785 3122 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 29 THROUGH 232) REMARK 3 ORIGIN FOR THE GROUP (A): -19.3344 2.1588 -21.8558 REMARK 3 T TENSOR REMARK 3 T11: 0.2655 T22: 0.4020 REMARK 3 T33: 0.3026 T12: 0.0031 REMARK 3 T13: 0.0071 T23: -0.0187 REMARK 3 L TENSOR REMARK 3 L11: 1.5158 L22: 0.6588 REMARK 3 L33: 1.6887 L12: 0.2438 REMARK 3 L13: -0.1488 L23: -0.0841 REMARK 3 S TENSOR REMARK 3 S11: -0.0396 S12: 0.1748 S13: 0.0527 REMARK 3 S21: -0.1317 S22: 0.0354 S23: -0.0700 REMARK 3 S31: 0.0229 S32: -0.1000 S33: -0.0162 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1001 THROUGH 1106) REMARK 3 ORIGIN FOR THE GROUP (A): -18.3203 -42.8752 0.9680 REMARK 3 T TENSOR REMARK 3 T11: 1.3982 T22: 0.6634 REMARK 3 T33: 0.7746 T12: 0.0579 REMARK 3 T13: -0.1643 T23: -0.0740 REMARK 3 L TENSOR REMARK 3 L11: 2.1042 L22: 7.8899 REMARK 3 L33: 3.4102 L12: 1.1356 REMARK 3 L13: -2.1128 L23: -0.0046 REMARK 3 S TENSOR REMARK 3 S11: 0.0171 S12: 0.1655 S13: -0.6559 REMARK 3 S21: -0.7267 S22: 0.5593 S23: -0.1443 REMARK 3 S31: 1.9681 S32: 0.1039 S33: -0.6417 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 240 THROUGH 322) REMARK 3 ORIGIN FOR THE GROUP (A): -14.9312 1.4910 -13.9613 REMARK 3 T TENSOR REMARK 3 T11: 0.2811 T22: 0.3979 REMARK 3 T33: 0.2785 T12: -0.0219 REMARK 3 T13: -0.0124 T23: 0.0085 REMARK 3 L TENSOR REMARK 3 L11: 2.0110 L22: 2.0622 REMARK 3 L33: 1.7677 L12: 0.0521 REMARK 3 L13: -0.2226 L23: -0.0030 REMARK 3 S TENSOR REMARK 3 S11: -0.0729 S12: 0.0036 S13: -0.0136 REMARK 3 S21: 0.0975 S22: 0.0521 S23: -0.2210 REMARK 3 S31: 0.0367 S32: 0.1063 S33: -0.0044 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 6RZ6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-19. REMARK 100 THE DEPOSITION ID IS D_1200011359. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 22-APR-17; 22-APR-17 REMARK 200 TEMPERATURE (KELVIN) : 100; 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : ESRF; ESRF REMARK 200 BEAMLINE : ID29; ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M REMARK 200 WAVELENGTH OR RANGE (A) : 1.07228; 0.97625 REMARK 200 MONOCHROMATOR : NULL; NULL REMARK 200 OPTICS : NULL; NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL; PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M; DECTRIS REMARK 200 PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20161205 REMARK 200 DATA SCALING SOFTWARE : XSCALE 20180319 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19685 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.430 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 (%) : 99.8 REMARK 200 DATA REDUNDANCY : 9.200 REMARK 200 R MERGE (I) : 0.27900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.52 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 8.80 REMARK 200 R MERGE FOR SHELL (I) : 3.23000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.100 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 1.12-2829 REMARK 200 STARTING MODEL: 6RZ4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100-200 MM NH4 TARTRATE DIBASIC 28-32% REMARK 280 V/V PEG400 100 MM HEPES PH 8.0, LIPIDIC CUBIC PHASE, TEMPERATURE REMARK 280 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.89500 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.89500 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.90500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 85.44000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.90500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 85.44000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.89500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.90500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 85.44000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 42.89500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.90500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 85.44000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6080 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19770 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 24.0 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 17 REMARK 465 GLU A 18 REMARK 465 PRO A 19 REMARK 465 ASN A 20 REMARK 465 GLY A 21 REMARK 465 THR A 22 REMARK 465 PHE A 23 REMARK 465 SER A 24 REMARK 465 ASN A 25 REMARK 465 ASN A 26 REMARK 465 ASN A 27 REMARK 465 SER A 28 REMARK 465 LEU A 146 REMARK 465 LEU A 147 REMARK 465 HIS A 148 REMARK 465 GLY A 177 REMARK 465 SER A 178 REMARK 465 ASP A 1021 REMARK 465 ASN A 1022 REMARK 465 LYS A 1042 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 ALA A 1079 REMARK 465 ASN A 1080 REMARK 465 GLU A 1081 REMARK 465 GLY A 1082 REMARK 465 LYS A 1083 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 ARG A 29 CG CD NE CZ NH1 NH2 REMARK 470 ASN A 30 CG OD1 ND2 REMARK 470 GLU A 39 CG CD OE1 OE2 REMARK 470 LYS A 68 CG CD CE NZ REMARK 470 ARG A 145 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 149 CG1 CG2 REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2 REMARK 470 ASP A 175 OD1 OD2 REMARK 470 SER A 176 OG REMARK 470 ASN A 181 CG OD1 ND2 REMARK 470 SER A 183 OG REMARK 470 TYR A 193 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A1015 CG CD CE NZ REMARK 470 GLU A1018 CG CD OE1 OE2 REMARK 470 LYS A1019 CG CD CE NZ REMARK 470 GLN A1025 CG CD OE1 NE2 REMARK 470 LYS A1027 CG CD CE NZ REMARK 470 ASP A1028 CG OD1 OD2 REMARK 470 LYS A1032 CG CD CE NZ REMARK 470 ARG A1034 CG CD NE CZ NH1 NH2 REMARK 470 LEU A1038 CG CD1 CD2 REMARK 470 GLN A1041 CG CD OE1 NE2 REMARK 470 MET A1058 CG SD CE REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ASP A1060 CG OD1 OD2 REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 HIS A1063 CG ND1 CD2 CE1 NE2 REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ILE A1067 CG1 CG2 CD1 REMARK 470 GLN A1071 CG CD OE1 NE2 REMARK 470 ILE A1072 CG1 CG2 CD1 REMARK 470 ASP A1074 CG OD1 OD2 REMARK 470 LEU A1076 CG CD1 CD2 REMARK 470 LYS A1077 CG CD CE NZ REMARK 470 VAL A1084 CG1 CG2 REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 GLU A1086 CG CD OE1 OE2 REMARK 470 GLN A1088 CG CD OE1 NE2 REMARK 470 GLN A1093 CG CD OE1 NE2 REMARK 470 LYS A 317 CG CD CE NZ REMARK 470 ARG A 321 CZ NH1 NH2 REMARK 470 LYS A 322 CG CD CE NZ 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 SER A 183 -20.16 71.55 REMARK 500 CYS A 210 -60.53 -131.23 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 2004 REMARK 610 OLC A 2005 REMARK 610 OLC A 2006 REMARK 610 OLC A 2007 REMARK 610 OLC A 2008 REMARK 610 OLC A 2010 REMARK 610 OLC A 2011 REMARK 610 OLC A 2012 REMARK 610 OLC A 2013 REMARK 610 OLC A 2014 REMARK 610 OLC A 2015 REMARK 610 OLC A 2016 REMARK 610 OLC A 2017 REMARK 610 OLC A 2018 REMARK 610 OLC A 2019 REMARK 610 OLA A 2020 REMARK 610 OLA A 2021 REMARK 610 OLA A 2022 REMARK 610 OLA A 2025 REMARK 610 OLA A 2026 REMARK 610 OLA A 2029 REMARK 610 1PE A 2030 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue KNW A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TLA A 2003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2004 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2005 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2006 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2007 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2008 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2009 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2010 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2011 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2012 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2013 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2014 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2015 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2016 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2017 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2019 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2020 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2021 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2022 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2023 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2024 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2025 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2026 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2027 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2028 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2029 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 2030 DBREF 6RZ6 A 17 232 UNP Q9NS75 CLTR2_HUMAN 17 232 DBREF 6RZ6 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6RZ6 A 240 322 UNP Q9NS75 CLTR2_HUMAN 240 322 SEQADV 6RZ6 VAL A 51 UNP Q9NS75 TRP 51 ENGINEERED MUTATION SEQADV 6RZ6 ASN A 84 UNP Q9NS75 ASP 84 ENGINEERED MUTATION SEQADV 6RZ6 TYR A 137 UNP Q9NS75 PHE 137 ENGINEERED MUTATION SEQADV 6RZ6 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6RZ6 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6RZ6 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQRES 1 A 405 MET GLU PRO ASN GLY THR PHE SER ASN ASN ASN SER ARG SEQRES 2 A 405 ASN CYS THR ILE GLU ASN PHE LYS ARG GLU PHE PHE PRO SEQRES 3 A 405 ILE VAL TYR LEU ILE ILE PHE PHE VAL GLY VAL LEU GLY SEQRES 4 A 405 ASN GLY LEU SER ILE TYR VAL PHE LEU GLN PRO TYR LYS SEQRES 5 A 405 LYS SER THR SER VAL ASN VAL PHE MET LEU ASN LEU ALA SEQRES 6 A 405 ILE SER ASN LEU LEU PHE ILE SER THR LEU PRO PHE ARG SEQRES 7 A 405 ALA ASP TYR TYR LEU ARG GLY SER ASN TRP ILE PHE GLY SEQRES 8 A 405 ASP LEU ALA CYS ARG ILE MET SER TYR SER LEU TYR VAL SEQRES 9 A 405 ASN MET TYR SER SER ILE TYR PHE LEU THR VAL LEU SER SEQRES 10 A 405 VAL VAL ARG TYR LEU ALA MET VAL HIS PRO PHE ARG LEU SEQRES 11 A 405 LEU HIS VAL THR SER ILE ARG SER ALA TRP ILE LEU CYS SEQRES 12 A 405 GLY ILE ILE TRP ILE LEU ILE MET ALA SER SER ILE MET SEQRES 13 A 405 LEU LEU ASP SER GLY SER GLU GLN ASN GLY SER VAL THR SEQRES 14 A 405 SER CYS LEU GLU LEU ASN LEU TYR LYS ILE ALA LYS LEU SEQRES 15 A 405 GLN THR MET ASN TYR ILE ALA LEU VAL VAL GLY CYS LEU SEQRES 16 A 405 LEU PRO PHE PHE THR LEU SER ILE CYS TYR LEU LEU ILE SEQRES 17 A 405 ILE ARG VAL LEU LEU LYS VAL GLU ALA ASP LEU GLU ASP SEQRES 18 A 405 ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE GLU SEQRES 19 A 405 LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU THR SEQRES 20 A 405 LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA THR SEQRES 21 A 405 PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO GLU SEQRES 22 A 405 MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL GLY SEQRES 23 A 405 GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY LYS SEQRES 24 A 405 VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS THR SEQRES 25 A 405 THR ARG ASN ALA TYR ILE GLN LYS TYR LEU VAL SER HIS SEQRES 26 A 405 ARG LYS ALA LEU THR THR ILE ILE ILE THR LEU ILE ILE SEQRES 27 A 405 PHE PHE LEU CYS PHE LEU PRO TYR HIS THR LEU ARG THR SEQRES 28 A 405 VAL HIS LEU THR THR TRP LYS VAL GLY LEU CYS LYS ASP SEQRES 29 A 405 ARG LEU HIS LYS ALA LEU VAL ILE THR LEU ALA LEU ALA SEQRES 30 A 405 ALA ALA ASN ALA CYS PHE ASN PRO LEU LEU TYR TYR PHE SEQRES 31 A 405 ALA GLY GLU ASN PHE LYS ASP ARG LEU LYS SER ALA LEU SEQRES 32 A 405 ARG LYS HET KNW A2001 41 HET CLR A2002 28 HET TLA A2003 10 HET OLC A2004 21 HET OLC A2005 21 HET OLC A2006 17 HET OLC A2007 8 HET OLC A2008 8 HET OLC A2009 25 HET OLC A2010 8 HET OLC A2011 12 HET OLC A2012 11 HET OLC A2013 17 HET OLC A2014 12 HET OLC A2015 11 HET OLC A2016 16 HET OLC A2017 16 HET OLC A2018 14 HET OLC A2019 17 HET OLA A2020 16 HET OLA A2021 17 HET OLA A2022 12 HET OLA A2023 20 HET OLA A2024 20 HET OLA A2025 10 HET OLA A2026 19 HET OLA A2027 20 HET OLA A2028 20 HET OLA A2029 11 HET 1PE A2030 15 HETNAM KNW (2~{S})-8-[[4-[4-(2-CHLORANYL-5-FLUORANYL-PHENYL) HETNAM 2 KNW BUTOXY]PHENYL]CARBONYLAMINO]-4-(4-OXIDANYL-4- HETNAM 3 KNW OXIDANYLIDENE-BUTYL)-2,3- DIHYDRO-1,4-BENZOXAZINE-2- HETNAM 4 KNW CARBOXYLIC ACID HETNAM CLR CHOLESTEROL HETNAM TLA L(+)-TARTARIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETNAM 1PE PENTAETHYLENE GLYCOL HETSYN KNW ONO-2570366 HETSYN OLC 1-OLEOYL-R-GLYCEROL HETSYN 1PE PEG400 FORMUL 2 KNW C30 H30 CL F N2 O7 FORMUL 3 CLR C27 H46 O FORMUL 4 TLA C4 H6 O6 FORMUL 5 OLC 16(C21 H40 O4) FORMUL 21 OLA 10(C18 H34 O2) FORMUL 31 1PE C10 H22 O6 FORMUL 32 HOH *35(H2 O) HELIX 1 AA1 THR A 32 LEU A 64 1 33 HELIX 2 AA2 THR A 71 SER A 89 1 19 HELIX 3 AA3 THR A 90 ARG A 100 1 11 HELIX 4 AA4 GLY A 107 HIS A 142 1 36 HELIX 5 AA5 THR A 150 ILE A 171 1 22 HELIX 6 AA6 ILE A 171 SER A 176 1 6 HELIX 7 AA7 ASN A 191 CYS A 210 1 20 HELIX 8 AA8 CYS A 210 ALA A 1020 1 43 HELIX 9 AA9 ALA A 1024 GLN A 1041 1 18 HELIX 10 AB1 LYS A 1059 LEU A 1078 1 20 HELIX 11 AB2 LYS A 1085 GLU A 1092 1 8 HELIX 12 AB3 GLU A 1092 PHE A 260 1 36 HELIX 13 AB4 PHE A 260 TRP A 274 1 15 HELIX 14 AB5 LYS A 280 ASN A 301 1 22 HELIX 15 AB6 ASN A 301 GLY A 309 1 9 HELIX 16 AB7 ASN A 311 LYS A 322 1 12 SSBOND 1 CYS A 31 CYS A 279 1555 1555 2.03 SSBOND 2 CYS A 111 CYS A 187 1555 1555 2.04 SITE 1 AC1 15 LYS A 37 TYR A 119 TYR A 123 TYR A 127 SITE 2 AC1 15 SER A 170 MET A 201 ASN A 202 ILE A 204 SITE 3 AC1 15 ARG A 267 LEU A 271 HIS A 284 OLC A2015 SITE 4 AC1 15 HOH A2109 HOH A2112 HOH A2125 SITE 1 AC2 4 SER A 218 TYR A 221 THR A 265 HOH A2106 SITE 1 AC3 8 ARG A 243 LYS A 244 GLY A 309 ASN A 311 SITE 2 AC3 8 PHE A 312 LYS A 313 ASP A 314 HOH A2115 SITE 1 AC4 6 PHE A 36 GLU A 39 PHE A 40 OLC A2005 SITE 2 AC4 6 OLC A2006 OLC A2012 SITE 1 AC5 8 PHE A 36 PHE A 40 LYS A 285 ILE A 289 SITE 2 AC5 8 LEU A 293 OLC A2004 OLC A2007 OLC A2012 SITE 1 AC6 5 ASP A 96 LEU A 99 ARG A 100 OLC A2004 SITE 2 AC6 5 OLC A2011 SITE 1 AC7 4 LEU A 54 CYS A 299 OLC A2005 OLA A2024 SITE 1 AC8 2 PHE A 215 OLC A2019 SITE 1 AC9 5 PHE A 214 SER A 218 ARG A 226 OLA A2020 SITE 2 AC9 5 OLA A2022 SITE 1 AD1 2 TYR A 61 OLA A2024 SITE 1 AD2 4 PHE A 93 ASP A 96 OLC A2006 OLA A2026 SITE 1 AD3 2 OLC A2004 OLC A2005 SITE 1 AD4 5 GLU A 232 LEU A 246 THR A 247 LEU A1106 SITE 2 AD4 5 OLA A2028 SITE 1 AD5 2 TYR A 221 OLA A2023 SITE 1 AD6 7 TYR A 127 LEU A 165 SER A 169 ILE A 204 SITE 2 AD6 7 VAL A 208 KNW A2001 OLC A2019 SITE 1 AD7 1 TRP A 156 SITE 1 AD8 5 ILE A 105 PHE A 106 ALA A 110 MET A 114 SITE 2 AD8 5 OLA A2025 SITE 1 AD9 3 ILE A 161 OLC A2008 OLC A2015 SITE 1 AE1 4 TYR A 203 VAL A 207 THR A 268 OLC A2009 SITE 1 AE2 1 PHE A 215 SITE 1 AE3 2 ARG A 226 OLC A2009 SITE 1 AE4 6 TYR A 221 LEU A 229 GLU A 232 LEU A 253 SITE 2 AE4 6 OLC A2014 HOH A2102 SITE 1 AE5 8 LEU A 58 TYR A 61 TYR A 306 ALA A 319 SITE 2 AE5 8 OLC A2007 OLC A2010 OLA A2029 HOH A2120 SITE 1 AE6 1 OLC A2017 SITE 1 AE7 3 LEU A 64 GLN A 65 OLC A2011 SITE 1 AE8 5 SER A 83 LEU A 86 TRP A 156 TRP A 163 SITE 2 AE8 5 MET A 167 SITE 1 AE9 3 PHE A 307 OLC A2013 OLA A2029 SITE 1 AF1 2 OLA A2024 OLA A2028 SITE 1 AF2 4 GLU A 232 ARG A 282 GLU A1004 ILE A1102 CRYST1 69.810 170.880 85.790 90.00 90.00 90.00 C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.014325 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005852 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011656 0.00000 ATOM 1 N ARG A 29 -13.251 31.965 -22.964 1.00125.99 N ANISOU 1 N ARG A 29 16741 13783 17347 -356 342 774 N ATOM 2 CA ARG A 29 -12.910 30.943 -21.979 1.00129.20 C ANISOU 2 CA ARG A 29 17037 14361 17692 -392 327 600 C ATOM 3 C ARG A 29 -12.034 31.506 -20.862 1.00137.70 C ANISOU 3 C ARG A 29 18154 15323 18842 -532 345 446 C ATOM 4 O ARG A 29 -10.872 31.119 -20.726 1.00141.52 O ANISOU 4 O ARG A 29 18575 15909 19287 -694 353 403 O ATOM 5 CB ARG A 29 -12.200 29.767 -22.652 1.00124.90 C ANISOU 5 CB ARG A 29 16368 14066 17023 -471 324 645 C ATOM 6 N ASN A 30 -12.605 32.404 -20.051 1.00141.11 N ANISOU 6 N ASN A 30 18688 15552 19376 -468 351 359 N ATOM 7 CA ASN A 30 -11.826 33.085 -19.019 1.00137.81 C ANISOU 7 CA ASN A 30 18328 15001 19031 -608 369 209 C ATOM 8 C ASN A 30 -11.428 32.151 -17.876 1.00134.17 C ANISOU 8 C ASN A 30 17754 14727 18499 -655 347 29 C ATOM 9 O ASN A 30 -10.427 32.404 -17.195 1.00137.96 O ANISOU 9 O ASN A 30 18235 15185 18997 -821 354 -78 O ATOM 10 CB ASN A 30 -12.618 34.277 -18.477 1.00139.29 C ANISOU 10 CB ASN A 30 18661 14917 19346 -510 386 155 C ATOM 11 N CYS A 31 -12.172 31.066 -17.665 1.00117.73 N ANISOU 11 N CYS A 31 15571 12831 16330 -522 319 -1 N ATOM 12 CA CYS A 31 -12.011 30.249 -16.468 1.00 97.48 C ANISOU 12 CA CYS A 31 12915 10419 13704 -537 297 -169 C ATOM 13 C CYS A 31 -10.724 29.422 -16.538 1.00 87.62 C ANISOU 13 C CYS A 31 11557 9358 12379 -695 288 -174 C ATOM 14 O CYS A 31 -10.290 29.002 -17.613 1.00 90.04 O ANISOU 14 O CYS A 31 11816 9753 12640 -732 294 -43 O ATOM 15 CB CYS A 31 -13.216 29.325 -16.319 1.00 84.46 C ANISOU 15 CB CYS A 31 11194 8910 11987 -352 272 -178 C ATOM 16 SG CYS A 31 -14.799 30.200 -16.206 1.00 78.85 S ANISOU 16 SG CYS A 31 10585 8017 11359 -144 282 -173 S ATOM 17 N THR A 32 -10.123 29.169 -15.366 1.00 76.61 N ANISOU 17 N THR A 32 10113 8032 10961 -782 274 -329 N ATOM 18 CA THR A 32 -8.843 28.461 -15.269 1.00 70.36 C ANISOU 18 CA THR A 32 9211 7416 10106 -930 263 -348 C ATOM 19 C THR A 32 -8.973 26.956 -15.492 1.00 64.66 C ANISOU 19 C THR A 32 8357 6936 9275 -852 239 -314 C ATOM 20 O THR A 32 -7.969 26.264 -15.774 1.00 63.35 O ANISOU 20 O THR A 32 8093 6922 9054 -944 237 -286 O ATOM 21 CB THR A 32 -8.229 28.698 -13.890 1.00 73.14 C ANISOU 21 CB THR A 32 9553 7771 10464 -1039 249 -524 C ATOM 22 OG1 THR A 32 -9.090 28.136 -12.895 1.00 76.89 O ANISOU 22 OG1 THR A 32 9999 8321 10896 -915 225 -633 O ATOM 23 CG2 THR A 32 -8.101 30.184 -13.616 1.00 72.66 C ANISOU 23 CG2 THR A 32 9634 7459 10515 -1125 275 -577 C ATOM 24 N ILE A 33 -10.189 26.432 -15.352 1.00 57.98 N ANISOU 24 N ILE A 33 7504 6129 8399 -684 224 -320 N ATOM 25 CA ILE A 33 -10.421 25.019 -15.604 1.00 54.24 C ANISOU 25 CA ILE A 33 6919 5862 7828 -609 204 -286 C ATOM 26 C ILE A 33 -10.011 24.645 -17.017 1.00 52.28 C ANISOU 26 C ILE A 33 6638 5677 7546 -632 220 -138 C ATOM 27 O ILE A 33 -9.649 23.496 -17.279 1.00 52.75 O ANISOU 27 O ILE A 33 6600 5914 7530 -632 211 -119 O ATOM 28 CB ILE A 33 -11.896 24.671 -15.326 1.00 59.99 C ANISOU 28 CB ILE A 33 7656 6601 8537 -433 188 -305 C ATOM 29 CG1 ILE A 33 -12.076 23.157 -15.331 1.00 55.34 C ANISOU 29 CG1 ILE A 33 6955 6223 7848 -378 165 -299 C ATOM 30 CG2 ILE A 33 -12.823 25.371 -16.334 1.00 63.79 C ANISOU 30 CG2 ILE A 33 8220 6953 9066 -333 204 -188 C ATOM 31 CD1 ILE A 33 -11.320 22.498 -14.235 1.00 54.86 C ANISOU 31 CD1 ILE A 33 6818 6282 7745 -450 145 -408 C ATOM 32 N GLU A 34 -10.045 25.598 -17.947 1.00 51.95 N ANISOU 32 N GLU A 34 6682 5495 7561 -654 246 -31 N ATOM 33 CA GLU A 34 -9.728 25.258 -19.327 1.00 53.93 C ANISOU 33 CA GLU A 34 6904 5819 7767 -673 264 113 C ATOM 34 C GLU A 34 -8.235 24.997 -19.483 1.00 51.66 C ANISOU 34 C GLU A 34 6544 5630 7455 -834 281 113 C ATOM 35 O GLU A 34 -7.822 24.068 -20.193 1.00 50.14 O ANISOU 35 O GLU A 34 6267 5598 7187 -840 289 169 O ATOM 36 CB GLU A 34 -10.212 26.371 -20.254 1.00 55.78 C ANISOU 36 CB GLU A 34 7251 5880 8062 -648 284 240 C ATOM 37 CG GLU A 34 -11.726 26.551 -20.176 1.00 63.66 C ANISOU 37 CG GLU A 34 8302 6807 9080 -469 266 251 C ATOM 38 CD GLU A 34 -12.508 25.340 -20.675 1.00 65.81 C ANISOU 38 CD GLU A 34 8492 7259 9254 -351 243 292 C ATOM 39 OE1 GLU A 34 -12.063 24.679 -21.635 1.00 68.82 O ANISOU 39 OE1 GLU A 34 8818 7768 9563 -389 251 376 O ATOM 40 OE2 GLU A 34 -13.546 25.018 -20.064 1.00 64.31 O ANISOU 40 OE2 GLU A 34 8290 7090 9056 -228 220 229 O ATOM 41 N ASN A 35 -7.415 25.774 -18.781 1.00 48.47 N ANISOU 41 N ASN A 35 6166 5140 7109 -966 288 41 N ATOM 42 CA ASN A 35 -5.989 25.490 -18.744 1.00 52.96 C ANISOU 42 CA ASN A 35 6645 5826 7652 -1120 299 23 C ATOM 43 C ASN A 35 -5.721 24.129 -18.115 1.00 54.81 C ANISOU 43 C ASN A 35 6749 6269 7807 -1081 271 -55 C ATOM 44 O ASN A 35 -4.895 23.356 -18.618 1.00 52.76 O ANISOU 44 O ASN A 35 6388 6166 7491 -1124 283 -17 O ATOM 45 CB ASN A 35 -5.278 26.595 -17.977 1.00 60.75 C ANISOU 45 CB ASN A 35 7686 6682 8716 -1270 303 -56 C ATOM 46 CG ASN A 35 -5.350 27.908 -18.701 1.00 75.01 C ANISOU 46 CG ASN A 35 9621 8276 10604 -1330 337 38 C ATOM 47 OD1 ASN A 35 -5.182 27.959 -19.921 1.00 78.62 O ANISOU 47 OD1 ASN A 35 10082 8745 11044 -1347 366 181 O ATOM 48 ND2 ASN A 35 -5.656 28.975 -17.971 1.00 80.99 N ANISOU 48 ND2 ASN A 35 10491 8832 11450 -1354 336 -39 N ATOM 49 N PHE A 36 -6.416 23.807 -17.019 1.00 51.54 N ANISOU 49 N PHE A 36 6335 5861 7387 -995 236 -163 N ATOM 50 CA PHE A 36 -6.261 22.459 -16.471 1.00 47.60 C ANISOU 50 CA PHE A 36 5721 5553 6811 -946 209 -218 C ATOM 51 C PHE A 36 -6.627 21.383 -17.499 1.00 50.33 C ANISOU 51 C PHE A 36 6017 6013 7092 -848 219 -125 C ATOM 52 O PHE A 36 -5.878 20.419 -17.701 1.00 49.70 O ANISOU 52 O PHE A 36 5836 6088 6958 -868 222 -116 O ATOM 53 CB PHE A 36 -7.088 22.296 -15.197 1.00 47.41 C ANISOU 53 CB PHE A 36 5712 5517 6783 -864 174 -333 C ATOM 54 CG PHE A 36 -7.065 20.899 -14.654 1.00 47.62 C ANISOU 54 CG PHE A 36 5634 5727 6733 -804 145 -372 C ATOM 55 CD1 PHE A 36 -5.940 20.398 -14.020 1.00 50.81 C ANISOU 55 CD1 PHE A 36 5940 6260 7105 -888 127 -423 C ATOM 56 CD2 PHE A 36 -8.175 20.081 -14.795 1.00 47.42 C ANISOU 56 CD2 PHE A 36 5607 5745 6667 -662 134 -351 C ATOM 57 CE1 PHE A 36 -5.920 19.094 -13.530 1.00 52.00 C ANISOU 57 CE1 PHE A 36 6001 6568 7190 -823 100 -445 C ATOM 58 CE2 PHE A 36 -8.170 18.790 -14.304 1.00 51.93 C ANISOU 58 CE2 PHE A 36 6093 6467 7172 -611 110 -380 C ATOM 59 CZ PHE A 36 -7.038 18.289 -13.674 1.00 50.74 C ANISOU 59 CZ PHE A 36 5852 6431 6995 -687 93 -423 C ATOM 60 N LYS A 37 -7.784 21.534 -18.148 1.00 49.18 N ANISOU 60 N LYS A 37 5942 5796 6950 -741 223 -60 N ATOM 61 CA LYS A 37 -8.284 20.531 -19.086 1.00 46.90 C ANISOU 61 CA LYS A 37 5614 5612 6591 -649 228 15 C ATOM 62 C LYS A 37 -7.302 20.275 -20.226 1.00 50.85 C ANISOU 62 C LYS A 37 6066 6197 7057 -725 264 101 C ATOM 63 O LYS A 37 -7.058 19.115 -20.600 1.00 45.81 O ANISOU 63 O LYS A 37 5349 5705 6352 -693 270 109 O ATOM 64 CB LYS A 37 -9.633 20.999 -19.627 1.00 42.28 C ANISOU 64 CB LYS A 37 5115 4928 6022 -541 224 78 C ATOM 65 CG LYS A 37 -10.803 20.914 -18.637 1.00 45.94 C ANISOU 65 CG LYS A 37 5603 5358 6496 -430 192 -3 C ATOM 66 CD LYS A 37 -11.985 21.736 -19.147 1.00 45.97 C ANISOU 66 CD LYS A 37 5695 5235 6537 -337 193 64 C ATOM 67 CE LYS A 37 -12.598 21.176 -20.406 1.00 47.12 C ANISOU 67 CE LYS A 37 5825 5458 6621 -267 194 176 C ATOM 68 NZ LYS A 37 -13.778 21.979 -20.860 1.00 48.68 N ANISOU 68 NZ LYS A 37 6097 5547 6852 -165 188 249 N ATOM 69 N ARG A 38 -6.720 21.342 -20.787 1.00 47.15 N ANISOU 69 N ARG A 38 5645 5637 6632 -828 294 166 N ATOM 70 CA ARG A 38 -5.925 21.150 -21.994 1.00 50.76 C ANISOU 70 CA ARG A 38 6060 6180 7047 -894 335 262 C ATOM 71 C ARG A 38 -4.644 20.368 -21.729 1.00 50.56 C ANISOU 71 C ARG A 38 5911 6312 6987 -968 347 212 C ATOM 72 O ARG A 38 -4.089 19.773 -22.661 1.00 49.38 O ANISOU 72 O ARG A 38 5700 6283 6781 -983 382 269 O ATOM 73 CB ARG A 38 -5.586 22.491 -22.641 1.00 51.58 C ANISOU 73 CB ARG A 38 6244 6149 7204 -998 366 353 C ATOM 74 CG ARG A 38 -6.802 23.232 -23.149 1.00 57.58 C ANISOU 74 CG ARG A 38 7120 6763 7993 -911 359 434 C ATOM 75 CD ARG A 38 -6.380 24.484 -23.871 1.00 70.18 C ANISOU 75 CD ARG A 38 8797 8228 9640 -1017 393 542 C ATOM 76 NE ARG A 38 -7.518 25.284 -24.299 1.00 78.48 N ANISOU 76 NE ARG A 38 9964 9124 10731 -927 384 628 N ATOM 77 CZ ARG A 38 -7.983 26.319 -23.612 1.00 83.38 C ANISOU 77 CZ ARG A 38 10686 9546 11450 -914 371 594 C ATOM 78 NH1 ARG A 38 -7.350 26.707 -22.512 1.00 83.31 N ANISOU 78 NH1 ARG A 38 10679 9473 11501 -1005 368 474 N ATOM 79 NH2 ARG A 38 -9.034 26.999 -24.056 1.00 87.30 N ANISOU 79 NH2 ARG A 38 11280 9908 11982 -812 364 681 N ATOM 80 N GLU A 39 -4.157 20.365 -20.491 1.00 48.82 N ANISOU 80 N GLU A 39 5651 6102 6796 -1012 320 107 N ATOM 81 CA GLU A 39 -3.031 19.511 -20.152 1.00 53.56 C ANISOU 81 CA GLU A 39 6122 6867 7361 -1056 322 61 C ATOM 82 C GLU A 39 -3.485 18.145 -19.643 1.00 57.65 C ANISOU 82 C GLU A 39 6583 7493 7830 -930 293 6 C ATOM 83 O GLU A 39 -2.897 17.122 -20.010 1.00 56.29 O ANISOU 83 O GLU A 39 6319 7462 7609 -906 310 15 O ATOM 84 CB GLU A 39 -2.149 20.192 -19.108 1.00 51.21 C ANISOU 84 CB GLU A 39 5798 6549 7111 -1184 304 -15 C ATOM 85 N PHE A 40 -4.544 18.109 -18.830 1.00 53.23 N ANISOU 85 N PHE A 40 6078 6865 7282 -845 253 -50 N ATOM 86 CA PHE A 40 -4.964 16.874 -18.179 1.00 47.01 C ANISOU 86 CA PHE A 40 5241 6171 6451 -742 222 -104 C ATOM 87 C PHE A 40 -5.547 15.859 -19.163 1.00 45.97 C ANISOU 87 C PHE A 40 5102 6100 6263 -643 240 -49 C ATOM 88 O PHE A 40 -5.179 14.679 -19.120 1.00 45.79 O ANISOU 88 O PHE A 40 5003 6194 6199 -601 240 -66 O ATOM 89 CB PHE A 40 -5.968 17.191 -17.062 1.00 49.63 C ANISOU 89 CB PHE A 40 5634 6418 6806 -690 180 -176 C ATOM 90 CG PHE A 40 -6.474 15.977 -16.332 1.00 48.49 C ANISOU 90 CG PHE A 40 5446 6363 6616 -594 148 -224 C ATOM 91 CD1 PHE A 40 -5.652 15.294 -15.448 1.00 46.32 C ANISOU 91 CD1 PHE A 40 5081 6196 6320 -617 125 -277 C ATOM 92 CD2 PHE A 40 -7.784 15.541 -16.498 1.00 46.33 C ANISOU 92 CD2 PHE A 40 5218 6066 6320 -484 139 -212 C ATOM 93 CE1 PHE A 40 -6.110 14.177 -14.769 1.00 40.98 C ANISOU 93 CE1 PHE A 40 4372 5594 5604 -531 96 -309 C ATOM 94 CE2 PHE A 40 -8.252 14.425 -15.811 1.00 45.67 C ANISOU 94 CE2 PHE A 40 5098 6060 6195 -409 112 -252 C ATOM 95 CZ PHE A 40 -7.407 13.746 -14.945 1.00 41.71 C ANISOU 95 CZ PHE A 40 4518 5655 5676 -432 91 -297 C ATOM 96 N PHE A 41 -6.480 16.272 -20.033 1.00 44.26 N ANISOU 96 N PHE A 41 4964 5808 6043 -601 252 15 N ATOM 97 CA PHE A 41 -7.119 15.265 -20.882 1.00 42.31 C ANISOU 97 CA PHE A 41 4711 5630 5733 -512 262 52 C ATOM 98 C PHE A 41 -6.170 14.577 -21.855 1.00 42.72 C ANISOU 98 C PHE A 41 4696 5798 5739 -541 306 90 C ATOM 99 O PHE A 41 -6.291 13.350 -22.011 1.00 43.16 O ANISOU 99 O PHE A 41 4710 5942 5747 -473 309 68 O ATOM 100 CB PHE A 41 -8.334 15.805 -21.651 1.00 48.76 C ANISOU 100 CB PHE A 41 5615 6367 6544 -458 260 119 C ATOM 101 CG PHE A 41 -9.570 16.031 -20.813 1.00 52.01 C ANISOU 101 CG PHE A 41 6078 6703 6981 -381 219 77 C ATOM 102 CD1 PHE A 41 -10.253 14.942 -20.266 1.00 53.88 C ANISOU 102 CD1 PHE A 41 6286 7005 7180 -301 193 24 C ATOM 103 CD2 PHE A 41 -10.183 17.272 -20.775 1.00 51.68 C ANISOU 103 CD2 PHE A 41 6117 6527 6991 -377 213 105 C ATOM 104 CE1 PHE A 41 -11.447 15.126 -19.528 1.00 54.28 C ANISOU 104 CE1 PHE A 41 6375 7003 7245 -229 160 -12 C ATOM 105 CE2 PHE A 41 -11.402 17.459 -20.069 1.00 54.22 C ANISOU 105 CE2 PHE A 41 6480 6790 7332 -290 181 65 C ATOM 106 CZ PHE A 41 -12.027 16.390 -19.451 1.00 49.86 C ANISOU 106 CZ PHE A 41 5886 6320 6738 -219 156 6 C ATOM 107 N PRO A 42 -5.250 15.263 -22.563 1.00 41.37 N ANISOU 107 N PRO A 42 4511 5633 5576 -636 347 145 N ATOM 108 CA PRO A 42 -4.373 14.508 -23.479 1.00 44.08 C ANISOU 108 CA PRO A 42 4778 6106 5865 -652 396 171 C ATOM 109 C PRO A 42 -3.606 13.405 -22.770 1.00 46.39 C ANISOU 109 C PRO A 42 4969 6505 6150 -624 391 98 C ATOM 110 O PRO A 42 -3.521 12.281 -23.290 1.00 48.02 O ANISOU 110 O PRO A 42 5136 6803 6307 -560 414 90 O ATOM 111 CB PRO A 42 -3.435 15.585 -24.060 1.00 41.82 C ANISOU 111 CB PRO A 42 4486 5806 5599 -779 436 234 C ATOM 112 CG PRO A 42 -4.194 16.851 -23.951 1.00 42.82 C ANISOU 112 CG PRO A 42 4720 5773 5775 -805 414 274 C ATOM 113 CD PRO A 42 -4.969 16.709 -22.639 1.00 42.77 C ANISOU 113 CD PRO A 42 4741 5702 5807 -735 356 188 C ATOM 114 N ILE A 43 -3.127 13.677 -21.551 1.00 40.93 N ANISOU 114 N ILE A 43 4243 5802 5506 -662 356 43 N ATOM 115 CA ILE A 43 -2.372 12.680 -20.791 1.00 44.36 C ANISOU 115 CA ILE A 43 4577 6343 5935 -632 344 -14 C ATOM 116 C ILE A 43 -3.231 11.442 -20.512 1.00 43.77 C ANISOU 116 C ILE A 43 4517 6283 5831 -507 320 -47 C ATOM 117 O ILE A 43 -2.870 10.314 -20.884 1.00 45.51 O ANISOU 117 O ILE A 43 4683 6589 6019 -447 344 -53 O ATOM 118 CB ILE A 43 -1.822 13.301 -19.494 1.00 42.73 C ANISOU 118 CB ILE A 43 4338 6123 5775 -704 302 -65 C ATOM 119 CG1 ILE A 43 -0.825 14.410 -19.817 1.00 42.87 C ANISOU 119 CG1 ILE A 43 4330 6138 5820 -845 330 -36 C ATOM 120 CG2 ILE A 43 -1.122 12.259 -18.647 1.00 46.75 C ANISOU 120 CG2 ILE A 43 4741 6748 6272 -661 279 -113 C ATOM 121 CD1 ILE A 43 -0.415 15.282 -18.582 1.00 41.43 C ANISOU 121 CD1 ILE A 43 4140 5917 5685 -942 287 -93 C ATOM 122 N VAL A 44 -4.377 11.627 -19.851 1.00 39.76 N ANISOU 122 N VAL A 44 4083 5689 5335 -465 276 -71 N ATOM 123 CA VAL A 44 -5.146 10.457 -19.428 1.00 43.90 C ANISOU 123 CA VAL A 44 4615 6232 5833 -364 251 -103 C ATOM 124 C VAL A 44 -5.763 9.751 -20.626 1.00 46.86 C ANISOU 124 C VAL A 44 5023 6622 6161 -306 283 -71 C ATOM 125 O VAL A 44 -5.791 8.513 -20.675 1.00 48.77 O ANISOU 125 O VAL A 44 5239 6915 6375 -240 289 -93 O ATOM 126 CB VAL A 44 -6.212 10.819 -18.369 1.00 44.40 C ANISOU 126 CB VAL A 44 4736 6218 5914 -339 199 -140 C ATOM 127 CG1 VAL A 44 -5.557 11.317 -17.090 1.00 41.61 C ANISOU 127 CG1 VAL A 44 4345 5872 5594 -394 165 -188 C ATOM 128 CG2 VAL A 44 -7.191 11.857 -18.903 1.00 49.94 C ANISOU 128 CG2 VAL A 44 5529 6819 6628 -347 201 -106 C ATOM 129 N TYR A 45 -6.269 10.511 -21.606 1.00 41.38 N ANISOU 129 N TYR A 45 4388 5881 5452 -331 303 -19 N ATOM 130 CA TYR A 45 -6.847 9.892 -22.793 1.00 40.72 C ANISOU 130 CA TYR A 45 4333 5828 5310 -287 330 10 C ATOM 131 C TYR A 45 -5.820 9.057 -23.555 1.00 41.80 C ANISOU 131 C TYR A 45 4404 6065 5412 -287 384 7 C ATOM 132 O TYR A 45 -6.131 7.941 -23.990 1.00 38.67 O ANISOU 132 O TYR A 45 4009 5709 4973 -227 399 -17 O ATOM 133 CB TYR A 45 -7.482 10.955 -23.692 1.00 42.85 C ANISOU 133 CB TYR A 45 4672 6043 5568 -318 338 80 C ATOM 134 CG TYR A 45 -8.817 11.489 -23.202 1.00 43.24 C ANISOU 134 CG TYR A 45 4791 6003 5636 -279 291 84 C ATOM 135 CD1 TYR A 45 -9.585 10.763 -22.297 1.00 44.25 C ANISOU 135 CD1 TYR A 45 4921 6128 5765 -214 252 27 C ATOM 136 CD2 TYR A 45 -9.284 12.741 -23.608 1.00 43.39 C ANISOU 136 CD2 TYR A 45 4870 5941 5674 -304 287 147 C ATOM 137 CE1 TYR A 45 -10.803 11.242 -21.841 1.00 44.14 C ANISOU 137 CE1 TYR A 45 4958 6048 5765 -175 214 26 C ATOM 138 CE2 TYR A 45 -10.509 13.237 -23.160 1.00 43.21 C ANISOU 138 CE2 TYR A 45 4904 5840 5673 -252 248 148 C ATOM 139 CZ TYR A 45 -11.265 12.481 -22.273 1.00 46.51 C ANISOU 139 CZ TYR A 45 5313 6272 6087 -188 213 84 C ATOM 140 OH TYR A 45 -12.484 12.950 -21.804 1.00 42.62 O ANISOU 140 OH TYR A 45 4864 5718 5612 -133 179 80 O ATOM 141 N LEU A 46 -4.580 9.546 -23.701 1.00 39.98 N ANISOU 141 N LEU A 46 4112 5879 5200 -355 417 24 N ATOM 142 CA LEU A 46 -3.616 8.725 -24.430 1.00 43.81 C ANISOU 142 CA LEU A 46 4526 6472 5650 -343 475 15 C ATOM 143 C LEU A 46 -3.141 7.530 -23.603 1.00 42.74 C ANISOU 143 C LEU A 46 4325 6381 5533 -272 464 -46 C ATOM 144 O LEU A 46 -2.914 6.443 -24.165 1.00 39.81 O ANISOU 144 O LEU A 46 3930 6068 5130 -210 503 -70 O ATOM 145 CB LEU A 46 -2.445 9.586 -24.923 1.00 43.70 C ANISOU 145 CB LEU A 46 4454 6508 5642 -441 519 58 C ATOM 146 CG LEU A 46 -2.909 10.552 -26.023 1.00 42.89 C ANISOU 146 CG LEU A 46 4421 6370 5506 -500 543 135 C ATOM 147 CD1 LEU A 46 -1.831 11.530 -26.409 1.00 39.38 C ANISOU 147 CD1 LEU A 46 3932 5958 5074 -615 583 187 C ATOM 148 CD2 LEU A 46 -3.398 9.775 -27.260 1.00 36.25 C ANISOU 148 CD2 LEU A 46 3607 5585 4581 -448 582 144 C ATOM 149 N ILE A 47 -3.009 7.690 -22.274 1.00 43.33 N ANISOU 149 N ILE A 47 4376 6430 5657 -275 411 -71 N ATOM 150 CA ILE A 47 -2.675 6.531 -21.438 1.00 46.95 C ANISOU 150 CA ILE A 47 4781 6928 6131 -198 392 -114 C ATOM 151 C ILE A 47 -3.727 5.444 -21.608 1.00 43.87 C ANISOU 151 C ILE A 47 4456 6500 5713 -111 386 -136 C ATOM 152 O ILE A 47 -3.411 4.260 -21.816 1.00 41.46 O ANISOU 152 O ILE A 47 4124 6231 5397 -41 412 -161 O ATOM 153 CB ILE A 47 -2.535 6.927 -19.957 1.00 46.06 C ANISOU 153 CB ILE A 47 4643 6799 6060 -221 330 -133 C ATOM 154 CG1 ILE A 47 -1.367 7.893 -19.730 1.00 43.35 C ANISOU 154 CG1 ILE A 47 4222 6505 5743 -318 335 -122 C ATOM 155 CG2 ILE A 47 -2.334 5.673 -19.089 1.00 45.73 C ANISOU 155 CG2 ILE A 47 4555 6794 6025 -133 304 -161 C ATOM 156 CD1 ILE A 47 -1.378 8.529 -18.298 1.00 38.41 C ANISOU 156 CD1 ILE A 47 3590 5855 5150 -364 269 -150 C ATOM 157 N ILE A 48 -4.999 5.838 -21.512 1.00 44.26 N ANISOU 157 N ILE A 48 4592 6472 5752 -116 351 -130 N ATOM 158 CA ILE A 48 -6.095 4.889 -21.667 1.00 43.37 C ANISOU 158 CA ILE A 48 4541 6328 5610 -53 341 -150 C ATOM 159 C ILE A 48 -6.059 4.266 -23.050 1.00 47.30 C ANISOU 159 C ILE A 48 5052 6863 6056 -35 399 -152 C ATOM 160 O ILE A 48 -6.274 3.060 -23.199 1.00 45.85 O ANISOU 160 O ILE A 48 4883 6682 5856 24 412 -188 O ATOM 161 CB ILE A 48 -7.437 5.583 -21.384 1.00 44.20 C ANISOU 161 CB ILE A 48 4721 6363 5710 -67 297 -138 C ATOM 162 CG1 ILE A 48 -7.474 6.036 -19.918 1.00 41.60 C ANISOU 162 CG1 ILE A 48 4377 6003 5424 -77 244 -154 C ATOM 163 CG2 ILE A 48 -8.604 4.660 -21.738 1.00 40.15 C ANISOU 163 CG2 ILE A 48 4264 5834 5156 -20 290 -154 C ATOM 164 CD1 ILE A 48 -8.581 6.992 -19.606 1.00 41.07 C ANISOU 164 CD1 ILE A 48 4372 5871 5363 -94 210 -145 C ATOM 165 N PHE A 49 -5.755 5.065 -24.080 1.00 43.19 N ANISOU 165 N PHE A 49 4530 6372 5508 -89 437 -116 N ATOM 166 CA PHE A 49 -5.670 4.530 -25.432 1.00 40.14 C ANISOU 166 CA PHE A 49 4154 6040 5059 -80 496 -121 C ATOM 167 C PHE A 49 -4.687 3.373 -25.503 1.00 42.06 C ANISOU 167 C PHE A 49 4336 6339 5308 -23 543 -169 C ATOM 168 O PHE A 49 -5.051 2.255 -25.888 1.00 38.72 O ANISOU 168 O PHE A 49 3944 5912 4856 33 562 -215 O ATOM 169 CB PHE A 49 -5.253 5.621 -26.423 1.00 41.58 C ANISOU 169 CB PHE A 49 4328 6261 5210 -155 534 -63 C ATOM 170 CG PHE A 49 -5.103 5.120 -27.849 1.00 41.12 C ANISOU 170 CG PHE A 49 4274 6279 5072 -152 599 -68 C ATOM 171 CD1 PHE A 49 -6.220 4.882 -28.647 1.00 42.76 C ANISOU 171 CD1 PHE A 49 4554 6481 5210 -145 593 -66 C ATOM 172 CD2 PHE A 49 -3.855 4.852 -28.369 1.00 44.91 C ANISOU 172 CD2 PHE A 49 4679 6846 5538 -158 667 -81 C ATOM 173 CE1 PHE A 49 -6.085 4.411 -29.947 1.00 40.95 C ANISOU 173 CE1 PHE A 49 4330 6333 4896 -149 653 -81 C ATOM 174 CE2 PHE A 49 -3.710 4.380 -29.684 1.00 46.02 C ANISOU 174 CE2 PHE A 49 4822 7066 5595 -155 734 -97 C ATOM 175 CZ PHE A 49 -4.821 4.153 -30.464 1.00 42.12 C ANISOU 175 CZ PHE A 49 4409 6565 5029 -153 726 -99 C ATOM 176 N PHE A 50 -3.418 3.637 -25.171 1.00 39.23 N ANISOU 176 N PHE A 50 3886 6033 4985 -37 563 -161 N ATOM 177 CA PHE A 50 -2.410 2.599 -25.365 1.00 41.38 C ANISOU 177 CA PHE A 50 4089 6371 5263 29 615 -201 C ATOM 178 C PHE A 50 -2.665 1.388 -24.468 1.00 40.44 C ANISOU 178 C PHE A 50 3982 6202 5181 121 584 -242 C ATOM 179 O PHE A 50 -2.669 0.241 -24.954 1.00 41.36 O ANISOU 179 O PHE A 50 4117 6316 5282 191 624 -289 O ATOM 180 CB PHE A 50 -1.004 3.165 -25.181 1.00 40.90 C ANISOU 180 CB PHE A 50 3913 6395 5232 -8 640 -178 C ATOM 181 CG PHE A 50 -0.584 4.076 -26.301 1.00 45.19 C ANISOU 181 CG PHE A 50 4440 7002 5730 -93 695 -139 C ATOM 182 CD1 PHE A 50 -0.156 3.543 -27.512 1.00 48.85 C ANISOU 182 CD1 PHE A 50 4881 7544 6134 -71 776 -160 C ATOM 183 CD2 PHE A 50 -0.618 5.456 -26.161 1.00 47.73 C ANISOU 183 CD2 PHE A 50 4770 7302 6063 -197 668 -82 C ATOM 184 CE1 PHE A 50 0.225 4.390 -28.581 1.00 49.97 C ANISOU 184 CE1 PHE A 50 5007 7757 6223 -158 829 -114 C ATOM 185 CE2 PHE A 50 -0.233 6.307 -27.216 1.00 46.38 C ANISOU 185 CE2 PHE A 50 4590 7183 5849 -283 720 -32 C ATOM 186 CZ PHE A 50 0.186 5.771 -28.425 1.00 44.87 C ANISOU 186 CZ PHE A 50 4372 7085 5592 -265 799 -43 C ATOM 187 N VAL A 51 -2.920 1.616 -23.172 1.00 38.57 N ANISOU 187 N VAL A 51 3744 5921 4991 120 514 -228 N ATOM 188 CA VAL A 51 -3.214 0.493 -22.281 1.00 43.31 C ANISOU 188 CA VAL A 51 4361 6473 5622 200 481 -252 C ATOM 189 C VAL A 51 -4.430 -0.291 -22.781 1.00 44.93 C ANISOU 189 C VAL A 51 4670 6609 5792 225 485 -282 C ATOM 190 O VAL A 51 -4.436 -1.530 -22.760 1.00 48.99 O ANISOU 190 O VAL A 51 5205 7094 6317 298 502 -317 O ATOM 191 CB VAL A 51 -3.397 0.997 -20.832 1.00 43.56 C ANISOU 191 CB VAL A 51 4379 6481 5691 179 405 -228 C ATOM 192 CG1 VAL A 51 -3.823 -0.143 -19.901 1.00 40.19 C ANISOU 192 CG1 VAL A 51 3980 6005 5286 253 368 -239 C ATOM 193 CG2 VAL A 51 -2.093 1.619 -20.329 1.00 39.14 C ANISOU 193 CG2 VAL A 51 3708 6002 5162 150 401 -208 C ATOM 194 N GLY A 52 -5.449 0.407 -23.293 1.00 45.67 N ANISOU 194 N GLY A 52 4830 6680 5844 165 470 -269 N ATOM 195 CA GLY A 52 -6.695 -0.253 -23.652 1.00 45.96 C ANISOU 195 CA GLY A 52 4955 6664 5843 174 461 -296 C ATOM 196 C GLY A 52 -6.593 -1.022 -24.953 1.00 48.21 C ANISOU 196 C GLY A 52 5265 6974 6077 193 527 -340 C ATOM 197 O GLY A 52 -7.214 -2.079 -25.111 1.00 45.60 O ANISOU 197 O GLY A 52 4993 6599 5732 223 532 -385 O ATOM 198 N VAL A 53 -5.778 -0.524 -25.884 1.00 45.69 N ANISOU 198 N VAL A 53 4903 6729 5730 170 582 -333 N ATOM 199 CA VAL A 53 -5.504 -1.274 -27.107 1.00 49.77 C ANISOU 199 CA VAL A 53 5433 7287 6193 192 656 -386 C ATOM 200 C VAL A 53 -4.774 -2.564 -26.785 1.00 53.71 C ANISOU 200 C VAL A 53 5907 7763 6738 286 691 -441 C ATOM 201 O VAL A 53 -5.156 -3.636 -27.265 1.00 51.31 O ANISOU 201 O VAL A 53 5663 7421 6412 322 720 -505 O ATOM 202 CB VAL A 53 -4.712 -0.425 -28.113 1.00 50.89 C ANISOU 202 CB VAL A 53 5521 7526 6288 144 711 -359 C ATOM 203 CG1 VAL A 53 -4.243 -1.301 -29.267 1.00 52.00 C ANISOU 203 CG1 VAL A 53 5662 7723 6374 179 797 -427 C ATOM 204 CG2 VAL A 53 -5.610 0.680 -28.657 1.00 51.43 C ANISOU 204 CG2 VAL A 53 5637 7603 6301 60 681 -303 C ATOM 205 N LEU A 54 -3.726 -2.494 -25.953 1.00 54.04 N ANISOU 205 N LEU A 54 5862 7824 6845 327 686 -417 N ATOM 206 CA LEU A 54 -3.022 -3.731 -25.611 1.00 51.76 C ANISOU 206 CA LEU A 54 5548 7513 6608 434 716 -457 C ATOM 207 C LEU A 54 -3.956 -4.736 -24.944 1.00 46.75 C ANISOU 207 C LEU A 54 5000 6762 5999 472 674 -478 C ATOM 208 O LEU A 54 -4.099 -5.880 -25.406 1.00 44.16 O ANISOU 208 O LEU A 54 4728 6381 5670 527 716 -540 O ATOM 209 CB LEU A 54 -1.806 -3.448 -24.726 1.00 55.45 C ANISOU 209 CB LEU A 54 5897 8034 7137 470 704 -416 C ATOM 210 CG LEU A 54 -0.501 -3.071 -25.428 1.00 69.89 C ANISOU 210 CG LEU A 54 7617 9983 8954 474 774 -418 C ATOM 211 CD1 LEU A 54 -0.517 -1.699 -26.055 1.00 78.63 C ANISOU 211 CD1 LEU A 54 8707 11159 10010 357 780 -379 C ATOM 212 CD2 LEU A 54 0.625 -3.177 -24.424 1.00 75.41 C ANISOU 212 CD2 LEU A 54 8200 10730 9722 534 755 -387 C ATOM 213 N GLY A 55 -4.630 -4.305 -23.875 1.00 42.75 N ANISOU 213 N GLY A 55 4512 6216 5517 438 595 -430 N ATOM 214 CA GLY A 55 -5.475 -5.222 -23.126 1.00 45.39 C ANISOU 214 CA GLY A 55 4919 6452 5876 466 554 -437 C ATOM 215 C GLY A 55 -6.603 -5.803 -23.955 1.00 43.66 C ANISOU 215 C GLY A 55 4805 6180 5605 433 570 -490 C ATOM 216 O GLY A 55 -6.794 -7.020 -23.997 1.00 44.41 O ANISOU 216 O GLY A 55 4959 6198 5718 479 591 -534 O ATOM 217 N ASN A 56 -7.357 -4.946 -24.647 1.00 41.47 N ANISOU 217 N ASN A 56 4553 5943 5262 350 561 -485 N ATOM 218 CA ASN A 56 -8.508 -5.432 -25.396 1.00 44.94 C ANISOU 218 CA ASN A 56 5082 6352 5642 306 565 -531 C ATOM 219 C ASN A 56 -8.103 -6.193 -26.653 1.00 47.22 C ANISOU 219 C ASN A 56 5396 6655 5890 328 645 -610 C ATOM 220 O ASN A 56 -8.715 -7.225 -26.966 1.00 45.93 O ANISOU 220 O ASN A 56 5311 6429 5710 328 659 -672 O ATOM 221 CB ASN A 56 -9.417 -4.259 -25.723 1.00 46.67 C ANISOU 221 CB ASN A 56 5309 6621 5803 223 525 -491 C ATOM 222 CG ASN A 56 -10.154 -3.765 -24.502 1.00 48.97 C ANISOU 222 CG ASN A 56 5601 6879 6127 203 449 -438 C ATOM 223 OD1 ASN A 56 -10.730 -4.557 -23.762 1.00 50.52 O ANISOU 223 OD1 ASN A 56 5835 7012 6348 216 421 -448 O ATOM 224 ND2 ASN A 56 -10.034 -2.475 -24.214 1.00 47.75 N ANISOU 224 ND2 ASN A 56 5402 6764 5979 175 421 -383 N ATOM 225 N GLY A 57 -7.107 -5.709 -27.404 1.00 41.82 N ANISOU 225 N GLY A 57 4650 6056 5183 339 701 -613 N ATOM 226 CA GLY A 57 -6.640 -6.477 -28.545 1.00 44.04 C ANISOU 226 CA GLY A 57 4950 6359 5424 370 785 -698 C ATOM 227 C GLY A 57 -6.243 -7.880 -28.150 1.00 45.21 C ANISOU 227 C GLY A 57 5128 6410 5639 465 817 -757 C ATOM 228 O GLY A 57 -6.659 -8.859 -28.774 1.00 40.24 O ANISOU 228 O GLY A 57 4580 5727 4983 469 854 -842 O ATOM 229 N LEU A 58 -5.470 -8.005 -27.067 1.00 51.64 N ANISOU 229 N LEU A 58 5883 7196 6543 540 798 -710 N ATOM 230 CA LEU A 58 -5.065 -9.333 -26.628 1.00 53.30 C ANISOU 230 CA LEU A 58 6120 7304 6826 644 824 -749 C ATOM 231 C LEU A 58 -6.261 -10.153 -26.136 1.00 50.88 C ANISOU 231 C LEU A 58 5927 6872 6534 617 779 -763 C ATOM 232 O LEU A 58 -6.356 -11.357 -26.415 1.00 49.34 O ANISOU 232 O LEU A 58 5810 6578 6361 661 820 -835 O ATOM 233 CB LEU A 58 -3.994 -9.205 -25.549 1.00 59.89 C ANISOU 233 CB LEU A 58 6854 8157 7745 728 803 -680 C ATOM 234 CG LEU A 58 -3.423 -10.520 -25.026 1.00 73.87 C ANISOU 234 CG LEU A 58 8638 9829 9599 857 828 -699 C ATOM 235 CD1 LEU A 58 -2.786 -11.282 -26.161 1.00 80.88 C ANISOU 235 CD1 LEU A 58 9537 10715 10477 928 931 -797 C ATOM 236 CD2 LEU A 58 -2.391 -10.229 -23.959 1.00 77.77 C ANISOU 236 CD2 LEU A 58 9014 10374 10161 929 795 -617 C ATOM 237 N SER A 59 -7.192 -9.518 -25.415 1.00 45.70 N ANISOU 237 N SER A 59 5283 6214 5867 541 698 -699 N ATOM 238 CA SER A 59 -8.353 -10.241 -24.901 1.00 46.19 C ANISOU 238 CA SER A 59 5441 6173 5938 503 655 -704 C ATOM 239 C SER A 59 -9.208 -10.789 -26.038 1.00 45.38 C ANISOU 239 C SER A 59 5431 6046 5765 438 688 -795 C ATOM 240 O SER A 59 -9.626 -11.954 -26.014 1.00 37.65 O ANISOU 240 O SER A 59 4541 4955 4808 445 702 -847 O ATOM 241 CB SER A 59 -9.196 -9.331 -24.008 1.00 46.01 C ANISOU 241 CB SER A 59 5399 6180 5903 433 569 -625 C ATOM 242 OG SER A 59 -8.478 -8.927 -22.862 1.00 53.00 O ANISOU 242 OG SER A 59 6208 7082 6849 484 534 -551 O ATOM 243 N ILE A 60 -9.496 -9.949 -27.037 1.00 45.27 N ANISOU 243 N ILE A 60 5400 6138 5661 368 698 -812 N ATOM 244 CA ILE A 60 -10.302 -10.392 -28.171 1.00 47.32 C ANISOU 244 CA ILE A 60 5738 6403 5836 297 725 -898 C ATOM 245 C ILE A 60 -9.579 -11.488 -28.943 1.00 50.52 C ANISOU 245 C ILE A 60 6187 6759 6251 360 815 -1005 C ATOM 246 O ILE A 60 -10.191 -12.485 -29.347 1.00 49.83 O ANISOU 246 O ILE A 60 6196 6593 6145 329 835 -1091 O ATOM 247 CB ILE A 60 -10.667 -9.198 -29.072 1.00 47.06 C ANISOU 247 CB ILE A 60 5668 6509 5702 219 715 -876 C ATOM 248 CG1 ILE A 60 -11.580 -8.231 -28.325 1.00 47.84 C ANISOU 248 CG1 ILE A 60 5743 6635 5797 162 627 -783 C ATOM 249 CG2 ILE A 60 -11.329 -9.661 -30.355 1.00 47.94 C ANISOU 249 CG2 ILE A 60 5848 6654 5711 150 747 -969 C ATOM 250 CD1 ILE A 60 -11.837 -6.930 -29.075 1.00 46.63 C ANISOU 250 CD1 ILE A 60 5548 6605 5563 104 613 -737 C ATOM 251 N TYR A 61 -8.265 -11.337 -29.143 1.00 51.22 N ANISOU 251 N TYR A 61 6202 6891 6367 449 873 -1007 N ATOM 252 CA TYR A 61 -7.490 -12.413 -29.755 1.00 54.62 C ANISOU 252 CA TYR A 61 6665 7268 6820 534 964 -1111 C ATOM 253 C TYR A 61 -7.647 -13.729 -28.995 1.00 54.37 C ANISOU 253 C TYR A 61 6718 7059 6883 594 962 -1137 C ATOM 254 O TYR A 61 -7.812 -14.788 -29.610 1.00 52.61 O ANISOU 254 O TYR A 61 6589 6747 6655 603 1017 -1247 O ATOM 255 CB TYR A 61 -6.021 -12.014 -29.828 1.00 58.01 C ANISOU 255 CB TYR A 61 6981 7778 7282 632 1019 -1089 C ATOM 256 CG TYR A 61 -5.163 -13.075 -30.450 1.00 62.37 C ANISOU 256 CG TYR A 61 7553 8286 7860 737 1120 -1196 C ATOM 257 CD1 TYR A 61 -5.168 -13.280 -31.826 1.00 67.67 C ANISOU 257 CD1 TYR A 61 8260 9016 8435 705 1198 -1309 C ATOM 258 CD2 TYR A 61 -4.361 -13.889 -29.666 1.00 58.56 C ANISOU 258 CD2 TYR A 61 7054 7703 7492 872 1139 -1186 C ATOM 259 CE1 TYR A 61 -4.387 -14.254 -32.401 1.00 68.04 C ANISOU 259 CE1 TYR A 61 8327 9020 8505 807 1298 -1421 C ATOM 260 CE2 TYR A 61 -3.578 -14.864 -30.235 1.00 62.80 C ANISOU 260 CE2 TYR A 61 7609 8191 8060 984 1236 -1287 C ATOM 261 CZ TYR A 61 -3.595 -15.040 -31.600 1.00 66.04 C ANISOU 261 CZ TYR A 61 8056 8657 8377 951 1319 -1410 C ATOM 262 OH TYR A 61 -2.814 -16.013 -32.166 1.00 68.57 O ANISOU 262 OH TYR A 61 8397 8928 8729 1069 1423 -1523 O ATOM 263 N VAL A 62 -7.597 -13.685 -27.660 1.00 55.33 N ANISOU 263 N VAL A 62 6811 7123 7089 632 899 -1037 N ATOM 264 CA VAL A 62 -7.739 -14.906 -26.863 1.00 58.44 C ANISOU 264 CA VAL A 62 7284 7346 7574 689 891 -1039 C ATOM 265 C VAL A 62 -9.142 -15.491 -27.007 1.00 58.65 C ANISOU 265 C VAL A 62 7434 7287 7563 574 863 -1085 C ATOM 266 O VAL A 62 -9.304 -16.684 -27.291 1.00 59.97 O ANISOU 266 O VAL A 62 7707 7320 7760 589 906 -1169 O ATOM 267 CB VAL A 62 -7.393 -14.634 -25.386 1.00 60.52 C ANISOU 267 CB VAL A 62 7481 7595 7919 745 824 -910 C ATOM 268 CG1 VAL A 62 -7.739 -15.848 -24.533 1.00 64.82 C ANISOU 268 CG1 VAL A 62 8119 7965 8545 783 806 -892 C ATOM 269 CG2 VAL A 62 -5.903 -14.325 -25.245 1.00 55.22 C ANISOU 269 CG2 VAL A 62 6691 6996 7295 869 859 -878 C ATOM 270 N PHE A 63 -10.168 -14.659 -26.794 1.00 52.88 N ANISOU 270 N PHE A 63 6689 6632 6771 458 790 -1031 N ATOM 271 CA PHE A 63 -11.562 -15.068 -26.951 1.00 52.70 C ANISOU 271 CA PHE A 63 6760 6564 6699 334 757 -1067 C ATOM 272 C PHE A 63 -11.790 -15.875 -28.222 1.00 58.49 C ANISOU 272 C PHE A 63 7585 7262 7377 293 823 -1210 C ATOM 273 O PHE A 63 -12.425 -16.935 -28.193 1.00 66.87 O ANISOU 273 O PHE A 63 8755 8195 8457 247 829 -1269 O ATOM 274 CB PHE A 63 -12.462 -13.830 -26.954 1.00 52.59 C ANISOU 274 CB PHE A 63 6692 6688 6604 230 688 -1006 C ATOM 275 CG PHE A 63 -12.663 -13.197 -25.606 1.00 54.64 C ANISOU 275 CG PHE A 63 6893 6959 6909 237 613 -885 C ATOM 276 CD1 PHE A 63 -12.439 -13.904 -24.434 1.00 58.69 C ANISOU 276 CD1 PHE A 63 7427 7359 7514 295 595 -834 C ATOM 277 CD2 PHE A 63 -13.056 -11.873 -25.516 1.00 56.18 C ANISOU 277 CD2 PHE A 63 7014 7280 7053 189 563 -820 C ATOM 278 CE1 PHE A 63 -12.651 -13.307 -23.190 1.00 57.61 C ANISOU 278 CE1 PHE A 63 7235 7249 7403 293 527 -727 C ATOM 279 CE2 PHE A 63 -13.255 -11.266 -24.278 1.00 55.50 C ANISOU 279 CE2 PHE A 63 6878 7208 7004 194 499 -723 C ATOM 280 CZ PHE A 63 -13.049 -11.980 -23.116 1.00 54.70 C ANISOU 280 CZ PHE A 63 6793 7008 6981 243 481 -679 C ATOM 281 N LEU A 64 -11.288 -15.391 -29.351 1.00 55.53 N ANISOU 281 N LEU A 64 7170 7000 6927 299 876 -1269 N ATOM 282 CA LEU A 64 -11.589 -16.028 -30.622 1.00 55.55 C ANISOU 282 CA LEU A 64 7254 7000 6851 242 935 -1411 C ATOM 283 C LEU A 64 -10.758 -17.286 -30.852 1.00 62.67 C ANISOU 283 C LEU A 64 8228 7758 7826 346 1025 -1515 C ATOM 284 O LEU A 64 -10.741 -17.809 -31.977 1.00 67.69 O ANISOU 284 O LEU A 64 8925 8397 8398 321 1094 -1652 O ATOM 285 CB LEU A 64 -11.385 -15.021 -31.759 1.00 56.72 C ANISOU 285 CB LEU A 64 7333 7337 6880 206 959 -1430 C ATOM 286 CG LEU A 64 -12.315 -13.794 -31.699 1.00 59.66 C ANISOU 286 CG LEU A 64 7649 7844 7174 102 873 -1335 C ATOM 287 CD1 LEU A 64 -11.950 -12.761 -32.751 1.00 64.08 C ANISOU 287 CD1 LEU A 64 8138 8579 7629 83 899 -1329 C ATOM 288 CD2 LEU A 64 -13.791 -14.166 -31.809 1.00 60.76 C ANISOU 288 CD2 LEU A 64 7864 7967 7256 -30 820 -1367 C ATOM 289 N GLN A 65 -10.073 -17.787 -29.815 1.00 60.98 N ANISOU 289 N GLN A 65 8007 7421 7741 466 1027 -1455 N ATOM 290 CA GLN A 65 -9.318 -19.019 -30.025 1.00 65.79 C ANISOU 290 CA GLN A 65 8690 7879 8429 578 1113 -1551 C ATOM 291 C GLN A 65 -10.225 -20.232 -29.824 1.00 64.72 C ANISOU 291 C GLN A 65 8707 7552 8330 512 1106 -1611 C ATOM 292 O GLN A 65 -11.057 -20.241 -28.907 1.00 61.14 O ANISOU 292 O GLN A 65 8277 7048 7903 441 1027 -1522 O ATOM 293 CB GLN A 65 -8.130 -19.106 -29.069 1.00 70.78 C ANISOU 293 CB GLN A 65 9247 8463 9184 748 1121 -1459 C ATOM 294 CG GLN A 65 -7.100 -17.999 -29.255 1.00 77.57 C ANISOU 294 CG GLN A 65 9953 9505 10017 814 1136 -1407 C ATOM 295 CD GLN A 65 -6.367 -18.069 -30.581 1.00 81.88 C ANISOU 295 CD GLN A 65 10481 10129 10502 857 1241 -1532 C ATOM 296 OE1 GLN A 65 -5.982 -19.143 -31.041 1.00 84.65 O ANISOU 296 OE1 GLN A 65 10906 10365 10891 935 1322 -1646 O ATOM 297 NE2 GLN A 65 -6.205 -16.918 -31.223 1.00 83.65 N ANISOU 297 NE2 GLN A 65 10610 10546 10627 801 1241 -1514 N ATOM 298 N PRO A 66 -10.083 -21.241 -30.683 1.00 64.42 N ANISOU 298 N PRO A 66 8775 7410 8292 527 1191 -1765 N ATOM 299 CA PRO A 66 -10.950 -22.421 -30.589 1.00 65.82 C ANISOU 299 CA PRO A 66 9111 7394 8502 446 1191 -1837 C ATOM 300 C PRO A 66 -10.699 -23.184 -29.304 1.00 75.88 C ANISOU 300 C PRO A 66 10430 8473 9929 541 1170 -1740 C ATOM 301 O PRO A 66 -9.554 -23.359 -28.878 1.00 82.38 O ANISOU 301 O PRO A 66 11205 9247 10848 716 1206 -1696 O ATOM 302 CB PRO A 66 -10.547 -23.254 -31.807 1.00 65.71 C ANISOU 302 CB PRO A 66 9188 7317 8464 475 1302 -2031 C ATOM 303 CG PRO A 66 -9.948 -22.269 -32.753 1.00 66.77 C ANISOU 303 CG PRO A 66 9205 7676 8489 496 1338 -2062 C ATOM 304 CD PRO A 66 -9.240 -21.275 -31.889 1.00 65.22 C ANISOU 304 CD PRO A 66 8858 7584 8340 592 1292 -1893 C ATOM 305 N TYR A 67 -11.782 -23.640 -28.682 1.00 79.16 N ANISOU 305 N TYR A 67 10932 8784 10363 422 1111 -1702 N ATOM 306 CA TYR A 67 -11.650 -24.460 -27.489 1.00 80.78 C ANISOU 306 CA TYR A 67 11198 8792 10704 495 1091 -1607 C ATOM 307 C TYR A 67 -12.837 -25.415 -27.446 1.00 85.46 C ANISOU 307 C TYR A 67 11946 9224 11300 340 1077 -1660 C ATOM 308 O TYR A 67 -13.924 -25.094 -27.937 1.00 90.39 O ANISOU 308 O TYR A 67 12584 9945 11816 161 1041 -1708 O ATOM 309 CB TYR A 67 -11.558 -23.587 -26.230 1.00 74.79 C ANISOU 309 CB TYR A 67 10316 8132 9970 528 1003 -1414 C ATOM 310 CG TYR A 67 -11.202 -24.357 -24.982 1.00 75.04 C ANISOU 310 CG TYR A 67 10388 7988 10135 630 985 -1299 C ATOM 311 CD1 TYR A 67 -9.905 -24.823 -24.801 1.00 76.36 C ANISOU 311 CD1 TYR A 67 10537 8070 10406 832 1039 -1285 C ATOM 312 CD2 TYR A 67 -12.125 -24.578 -23.969 1.00 73.48 C ANISOU 312 CD2 TYR A 67 10235 7726 9956 532 912 -1195 C ATOM 313 CE1 TYR A 67 -9.542 -25.516 -23.674 1.00 75.96 C ANISOU 313 CE1 TYR A 67 10519 7869 10475 936 1019 -1167 C ATOM 314 CE2 TYR A 67 -11.770 -25.272 -22.826 1.00 75.82 C ANISOU 314 CE2 TYR A 67 10569 7871 10367 626 895 -1076 C ATOM 315 CZ TYR A 67 -10.472 -25.736 -22.688 1.00 80.89 C ANISOU 315 CZ TYR A 67 11196 8426 11111 831 946 -1060 C ATOM 316 OH TYR A 67 -10.093 -26.429 -21.562 1.00 88.30 O ANISOU 316 OH TYR A 67 12168 9220 12161 935 924 -930 O ATOM 317 N LYS A 68 -12.613 -26.598 -26.866 1.00 81.86 N ANISOU 317 N LYS A 68 11608 8523 10972 409 1105 -1647 N ATOM 318 CA LYS A 68 -13.607 -27.667 -26.941 1.00 79.69 C ANISOU 318 CA LYS A 68 11502 8061 10714 265 1110 -1718 C ATOM 319 C LYS A 68 -14.968 -27.243 -26.395 1.00 79.40 C ANISOU 319 C LYS A 68 11449 8114 10607 65 1015 -1635 C ATOM 320 O LYS A 68 -15.993 -27.799 -26.803 1.00 80.77 O ANISOU 320 O LYS A 68 11727 8225 10735 -110 1012 -1723 O ATOM 321 CB LYS A 68 -13.103 -28.908 -26.196 1.00 77.91 C ANISOU 321 CB LYS A 68 11397 7553 10652 384 1146 -1675 C ATOM 322 N LYS A 69 -15.011 -26.270 -25.485 1.00 76.14 N ANISOU 322 N LYS A 69 10902 7850 10177 84 937 -1473 N ATOM 323 CA LYS A 69 -16.270 -25.820 -24.906 1.00 75.60 C ANISOU 323 CA LYS A 69 10803 7877 10042 -87 851 -1390 C ATOM 324 C LYS A 69 -16.348 -24.299 -24.896 1.00 74.30 C ANISOU 324 C LYS A 69 10467 7982 9780 -93 794 -1323 C ATOM 325 O LYS A 69 -15.329 -23.606 -24.840 1.00 74.35 O ANISOU 325 O LYS A 69 10371 8076 9802 50 804 -1281 O ATOM 326 CB LYS A 69 -16.459 -26.388 -23.491 1.00 75.48 C ANISOU 326 CB LYS A 69 10832 7723 10125 -77 809 -1239 C ATOM 327 CG LYS A 69 -15.433 -25.943 -22.476 1.00 80.09 C ANISOU 327 CG LYS A 69 11315 8335 10780 104 786 -1089 C ATOM 328 CD LYS A 69 -15.664 -26.644 -21.143 1.00 86.85 C ANISOU 328 CD LYS A 69 12232 9044 11722 104 749 -945 C ATOM 329 CE LYS A 69 -14.628 -26.238 -20.103 1.00 90.93 C ANISOU 329 CE LYS A 69 12646 9601 12302 282 721 -793 C ATOM 330 NZ LYS A 69 -14.822 -26.927 -18.793 1.00 93.34 N ANISOU 330 NZ LYS A 69 13009 9774 12681 286 682 -641 N ATOM 331 N SER A 70 -17.575 -23.789 -24.978 1.00 76.95 N ANISOU 331 N SER A 70 10773 8448 10017 -264 735 -1317 N ATOM 332 CA SER A 70 -17.832 -22.354 -24.952 1.00 80.61 C ANISOU 332 CA SER A 70 11086 9152 10390 -283 678 -1252 C ATOM 333 C SER A 70 -19.060 -22.086 -24.090 1.00 73.78 C ANISOU 333 C SER A 70 10192 8349 9490 -415 599 -1156 C ATOM 334 O SER A 70 -19.859 -22.986 -23.817 1.00 73.61 O ANISOU 334 O SER A 70 10267 8214 9487 -529 592 -1167 O ATOM 335 CB SER A 70 -18.024 -21.789 -26.369 1.00 85.05 C ANISOU 335 CB SER A 70 11618 9865 10833 -342 699 -1373 C ATOM 336 OG SER A 70 -16.838 -21.921 -27.137 1.00 81.82 O ANISOU 336 OG SER A 70 11216 9426 10445 -214 776 -1455 O ATOM 337 N THR A 71 -19.208 -20.834 -23.665 1.00 67.56 N ANISOU 337 N THR A 71 9272 7744 8654 -400 543 -1064 N ATOM 338 CA THR A 71 -20.199 -20.485 -22.658 1.00 70.64 C ANISOU 338 CA THR A 71 9616 8202 9023 -488 473 -958 C ATOM 339 C THR A 71 -20.790 -19.116 -22.984 1.00 70.78 C ANISOU 339 C THR A 71 9510 8448 8937 -533 425 -941 C ATOM 340 O THR A 71 -20.219 -18.333 -23.745 1.00 74.63 O ANISOU 340 O THR A 71 9937 9033 9386 -469 441 -976 O ATOM 341 CB THR A 71 -19.555 -20.528 -21.254 1.00 76.12 C ANISOU 341 CB THR A 71 10285 8828 9808 -378 454 -823 C ATOM 342 OG1 THR A 71 -19.044 -21.845 -21.013 1.00 76.10 O ANISOU 342 OG1 THR A 71 10406 8605 9905 -332 498 -832 O ATOM 343 CG2 THR A 71 -20.550 -20.193 -20.142 1.00 78.76 C ANISOU 343 CG2 THR A 71 10572 9238 10116 -466 388 -715 C ATOM 344 N SER A 72 -21.965 -18.842 -22.415 1.00 67.02 N ANISOU 344 N SER A 72 8995 8055 8415 -644 369 -885 N ATOM 345 CA SER A 72 -22.598 -17.540 -22.586 1.00 64.74 C ANISOU 345 CA SER A 72 8586 7974 8037 -674 320 -855 C ATOM 346 C SER A 72 -21.767 -16.404 -21.987 1.00 56.98 C ANISOU 346 C SER A 72 7504 7065 7082 -538 304 -769 C ATOM 347 O SER A 72 -21.812 -15.267 -22.491 1.00 55.71 O ANISOU 347 O SER A 72 7259 7047 6862 -519 286 -768 O ATOM 348 CB SER A 72 -23.991 -17.576 -21.963 1.00 70.14 C ANISOU 348 CB SER A 72 9246 8725 8678 -808 269 -809 C ATOM 349 OG SER A 72 -23.921 -17.760 -20.557 1.00 72.42 O ANISOU 349 OG SER A 72 9530 8956 9030 -776 251 -703 O ATOM 350 N VAL A 73 -21.006 -16.678 -20.918 1.00 54.66 N ANISOU 350 N VAL A 73 7218 6676 6874 -447 307 -695 N ATOM 351 CA VAL A 73 -20.205 -15.609 -20.318 1.00 57.06 C ANISOU 351 CA VAL A 73 7426 7055 7199 -331 289 -621 C ATOM 352 C VAL A 73 -19.132 -15.145 -21.287 1.00 55.71 C ANISOU 352 C VAL A 73 7230 6908 7028 -241 330 -675 C ATOM 353 O VAL A 73 -18.739 -13.971 -21.281 1.00 61.20 O ANISOU 353 O VAL A 73 7836 7712 7704 -188 313 -641 O ATOM 354 CB VAL A 73 -19.595 -16.048 -18.970 1.00 60.50 C ANISOU 354 CB VAL A 73 7871 7400 7717 -257 280 -528 C ATOM 355 CG1 VAL A 73 -20.688 -16.347 -17.965 1.00 61.47 C ANISOU 355 CG1 VAL A 73 8003 7529 7824 -353 239 -463 C ATOM 356 CG2 VAL A 73 -18.729 -17.245 -19.155 1.00 60.46 C ANISOU 356 CG2 VAL A 73 7960 7221 7790 -192 331 -559 C ATOM 357 N ASN A 74 -18.660 -16.043 -22.148 1.00 49.53 N ANISOU 357 N ASN A 74 6529 6025 6264 -227 386 -763 N ATOM 358 CA ASN A 74 -17.754 -15.630 -23.208 1.00 52.66 C ANISOU 358 CA ASN A 74 6900 6464 6643 -158 432 -826 C ATOM 359 C ASN A 74 -18.434 -14.650 -24.161 1.00 53.71 C ANISOU 359 C ASN A 74 6980 6757 6668 -232 413 -857 C ATOM 360 O ASN A 74 -17.810 -13.681 -24.615 1.00 56.50 O ANISOU 360 O ASN A 74 7264 7206 6998 -176 421 -847 O ATOM 361 CB ASN A 74 -17.252 -16.866 -23.941 1.00 63.49 C ANISOU 361 CB ASN A 74 8378 7697 8050 -137 502 -927 C ATOM 362 CG ASN A 74 -16.478 -17.797 -23.020 1.00 77.19 C ANISOU 362 CG ASN A 74 10161 9267 9899 -39 522 -883 C ATOM 363 OD1 ASN A 74 -16.912 -18.924 -22.736 1.00 85.18 O ANISOU 363 OD1 ASN A 74 11276 10136 10952 -85 531 -899 O ATOM 364 ND2 ASN A 74 -15.335 -17.323 -22.529 1.00 75.02 N ANISOU 364 ND2 ASN A 74 9812 9014 9676 93 527 -821 N ATOM 365 N VAL A 75 -19.720 -14.871 -24.456 1.00 47.71 N ANISOU 365 N VAL A 75 6249 6036 5843 -361 384 -888 N ATOM 366 CA VAL A 75 -20.465 -13.929 -25.290 1.00 48.43 C ANISOU 366 CA VAL A 75 6282 6291 5830 -428 355 -901 C ATOM 367 C VAL A 75 -20.494 -12.551 -24.638 1.00 42.74 C ANISOU 367 C VAL A 75 5453 5679 5106 -380 308 -798 C ATOM 368 O VAL A 75 -20.211 -11.526 -25.278 1.00 43.78 O ANISOU 368 O VAL A 75 5526 5914 5194 -349 307 -788 O ATOM 369 CB VAL A 75 -21.892 -14.452 -25.554 1.00 53.44 C ANISOU 369 CB VAL A 75 6952 6956 6398 -577 325 -941 C ATOM 370 CG1 VAL A 75 -22.709 -13.421 -26.347 1.00 56.22 C ANISOU 370 CG1 VAL A 75 7228 7494 6639 -634 285 -936 C ATOM 371 CG2 VAL A 75 -21.873 -15.796 -26.275 1.00 52.08 C ANISOU 371 CG2 VAL A 75 6896 6669 6224 -638 374 -1058 C ATOM 372 N PHE A 76 -20.847 -12.503 -23.354 1.00 38.38 N ANISOU 372 N PHE A 76 4879 5105 4600 -377 270 -722 N ATOM 373 CA PHE A 76 -20.976 -11.194 -22.714 1.00 43.42 C ANISOU 373 CA PHE A 76 5421 5844 5232 -339 226 -639 C ATOM 374 C PHE A 76 -19.632 -10.475 -22.628 1.00 44.13 C ANISOU 374 C PHE A 76 5469 5931 5368 -225 248 -611 C ATOM 375 O PHE A 76 -19.542 -9.265 -22.886 1.00 45.56 O ANISOU 375 O PHE A 76 5583 6206 5520 -201 232 -581 O ATOM 376 CB PHE A 76 -21.597 -11.335 -21.329 1.00 43.47 C ANISOU 376 CB PHE A 76 5414 5835 5270 -361 187 -572 C ATOM 377 CG PHE A 76 -22.964 -11.928 -21.369 1.00 55.93 C ANISOU 377 CG PHE A 76 7016 7437 6798 -483 164 -591 C ATOM 378 CD1 PHE A 76 -24.025 -11.196 -21.874 1.00 60.30 C ANISOU 378 CD1 PHE A 76 7511 8129 7271 -544 130 -593 C ATOM 379 CD2 PHE A 76 -23.211 -13.178 -20.840 1.00 56.50 C ANISOU 379 CD2 PHE A 76 7163 7400 6905 -538 174 -598 C ATOM 380 CE1 PHE A 76 -25.295 -11.733 -21.926 1.00 61.57 C ANISOU 380 CE1 PHE A 76 7679 8332 7381 -663 107 -611 C ATOM 381 CE2 PHE A 76 -24.486 -13.718 -20.873 1.00 56.49 C ANISOU 381 CE2 PHE A 76 7180 7429 6856 -667 153 -615 C ATOM 382 CZ PHE A 76 -25.529 -12.993 -21.415 1.00 58.98 C ANISOU 382 CZ PHE A 76 7426 7898 7086 -732 119 -624 C ATOM 383 N MET A 77 -18.573 -11.209 -22.287 1.00 44.18 N ANISOU 383 N MET A 77 5510 5829 5446 -155 284 -618 N ATOM 384 CA MET A 77 -17.249 -10.602 -22.224 1.00 47.26 C ANISOU 384 CA MET A 77 5850 6228 5878 -54 306 -594 C ATOM 385 C MET A 77 -16.792 -10.094 -23.588 1.00 45.83 C ANISOU 385 C MET A 77 5654 6112 5647 -46 344 -645 C ATOM 386 O MET A 77 -16.242 -8.988 -23.692 1.00 46.87 O ANISOU 386 O MET A 77 5718 6318 5774 -8 341 -608 O ATOM 387 CB MET A 77 -16.256 -11.606 -21.644 1.00 47.40 C ANISOU 387 CB MET A 77 5904 6125 5981 25 337 -591 C ATOM 388 CG MET A 77 -16.463 -11.838 -20.162 1.00 51.93 C ANISOU 388 CG MET A 77 6472 6659 6602 34 295 -512 C ATOM 389 SD MET A 77 -15.305 -13.038 -19.493 1.00 55.87 S ANISOU 389 SD MET A 77 7012 7016 7198 137 325 -490 S ATOM 390 CE MET A 77 -15.805 -13.041 -17.770 1.00 57.97 C ANISOU 390 CE MET A 77 7259 7282 7484 121 261 -383 C ATOM 391 N LEU A 78 -16.996 -10.886 -24.642 1.00 40.72 N ANISOU 391 N LEU A 78 5072 5441 4960 -88 383 -730 N ATOM 392 CA LEU A 78 -16.602 -10.449 -25.978 1.00 43.18 C ANISOU 392 CA LEU A 78 5370 5830 5207 -88 422 -780 C ATOM 393 C LEU A 78 -17.308 -9.155 -26.378 1.00 44.47 C ANISOU 393 C LEU A 78 5473 6127 5295 -136 379 -734 C ATOM 394 O LEU A 78 -16.684 -8.248 -26.949 1.00 43.13 O ANISOU 394 O LEU A 78 5256 6030 5102 -105 396 -713 O ATOM 395 CB LEU A 78 -16.893 -11.560 -26.987 1.00 39.40 C ANISOU 395 CB LEU A 78 4978 5309 4684 -142 465 -890 C ATOM 396 CG LEU A 78 -16.485 -11.307 -28.446 1.00 44.64 C ANISOU 396 CG LEU A 78 5638 6055 5266 -149 515 -958 C ATOM 397 CD1 LEU A 78 -14.976 -11.123 -28.590 1.00 39.97 C ANISOU 397 CD1 LEU A 78 5010 5455 4722 -41 575 -958 C ATOM 398 CD2 LEU A 78 -16.980 -12.449 -29.371 1.00 45.42 C ANISOU 398 CD2 LEU A 78 5832 6117 5309 -223 551 -1080 C ATOM 399 N ASN A 79 -18.614 -9.060 -26.102 1.00 44.62 N ANISOU 399 N ASN A 79 5493 6182 5276 -210 325 -713 N ATOM 400 CA ASN A 79 -19.357 -7.849 -26.410 1.00 46.54 C ANISOU 400 CA ASN A 79 5677 6548 5456 -241 281 -661 C ATOM 401 C ASN A 79 -18.803 -6.658 -25.626 1.00 45.42 C ANISOU 401 C ASN A 79 5468 6421 5367 -171 261 -577 C ATOM 402 O ASN A 79 -18.665 -5.579 -26.169 1.00 41.66 O ANISOU 402 O ASN A 79 4951 6019 4859 -160 257 -541 O ATOM 403 CB ASN A 79 -20.846 -8.035 -26.135 1.00 46.88 C ANISOU 403 CB ASN A 79 5723 6632 5459 -323 228 -654 C ATOM 404 CG ASN A 79 -21.590 -8.593 -27.324 1.00 49.59 C ANISOU 404 CG ASN A 79 6102 7033 5706 -414 233 -725 C ATOM 405 OD1 ASN A 79 -22.033 -7.859 -28.188 1.00 47.65 O ANISOU 405 OD1 ASN A 79 5821 6905 5380 -440 214 -711 O ATOM 406 ND2 ASN A 79 -21.727 -9.897 -27.368 1.00 51.62 N ANISOU 406 ND2 ASN A 79 6433 7208 5971 -466 256 -800 N ATOM 407 N LEU A 80 -18.492 -6.858 -24.343 1.00 41.95 N ANISOU 407 N LEU A 80 5021 5911 5007 -131 249 -546 N ATOM 408 CA LEU A 80 -17.908 -5.776 -23.559 1.00 40.66 C ANISOU 408 CA LEU A 80 4798 5761 4891 -74 231 -480 C ATOM 409 C LEU A 80 -16.593 -5.297 -24.167 1.00 44.83 C ANISOU 409 C LEU A 80 5302 6299 5433 -24 275 -482 C ATOM 410 O LEU A 80 -16.353 -4.088 -24.284 1.00 43.32 O ANISOU 410 O LEU A 80 5064 6158 5237 -12 265 -437 O ATOM 411 CB LEU A 80 -17.700 -6.238 -22.121 1.00 40.60 C ANISOU 411 CB LEU A 80 4789 5684 4954 -43 213 -454 C ATOM 412 CG LEU A 80 -17.090 -5.281 -21.092 1.00 42.47 C ANISOU 412 CG LEU A 80 4968 5931 5240 8 191 -397 C ATOM 413 CD1 LEU A 80 -17.942 -4.028 -20.851 1.00 42.42 C ANISOU 413 CD1 LEU A 80 4920 5992 5206 -12 150 -359 C ATOM 414 CD2 LEU A 80 -16.913 -6.060 -19.780 1.00 39.83 C ANISOU 414 CD2 LEU A 80 4643 5534 4957 30 177 -377 C ATOM 415 N ALA A 81 -15.725 -6.237 -24.556 1.00 44.49 N ANISOU 415 N ALA A 81 5289 6204 5410 6 327 -533 N ATOM 416 CA ALA A 81 -14.403 -5.861 -25.052 1.00 44.55 C ANISOU 416 CA ALA A 81 5261 6231 5434 57 374 -536 C ATOM 417 C ALA A 81 -14.499 -5.162 -26.406 1.00 48.79 C ANISOU 417 C ALA A 81 5790 6858 5890 20 395 -543 C ATOM 418 O ALA A 81 -13.760 -4.202 -26.672 1.00 44.51 O ANISOU 418 O ALA A 81 5200 6364 5349 37 410 -505 O ATOM 419 CB ALA A 81 -13.498 -7.095 -25.143 1.00 37.18 C ANISOU 419 CB ALA A 81 4358 5225 4542 111 429 -593 C ATOM 420 N ILE A 82 -15.409 -5.621 -27.274 1.00 50.33 N ANISOU 420 N ILE A 82 6032 7083 6009 -39 396 -589 N ATOM 421 CA ILE A 82 -15.605 -4.929 -28.545 1.00 48.77 C ANISOU 421 CA ILE A 82 5824 6986 5718 -78 407 -584 C ATOM 422 C ILE A 82 -16.084 -3.511 -28.304 1.00 48.76 C ANISOU 422 C ILE A 82 5777 7040 5711 -87 356 -492 C ATOM 423 O ILE A 82 -15.553 -2.550 -28.884 1.00 47.07 O ANISOU 423 O ILE A 82 5530 6879 5474 -82 372 -448 O ATOM 424 CB ILE A 82 -16.568 -5.715 -29.453 1.00 45.24 C ANISOU 424 CB ILE A 82 5433 6574 5183 -148 407 -653 C ATOM 425 CG1 ILE A 82 -15.892 -7.020 -29.898 1.00 46.92 C ANISOU 425 CG1 ILE A 82 5699 6725 5401 -133 475 -756 C ATOM 426 CG2 ILE A 82 -17.057 -4.848 -30.613 1.00 37.87 C ANISOU 426 CG2 ILE A 82 4480 5766 4142 -195 395 -623 C ATOM 427 CD1 ILE A 82 -16.796 -7.991 -30.577 1.00 45.62 C ANISOU 427 CD1 ILE A 82 5602 6565 5165 -209 476 -843 C ATOM 428 N SER A 83 -17.089 -3.351 -27.440 1.00 46.23 N ANISOU 428 N SER A 83 5452 6703 5410 -100 297 -461 N ATOM 429 CA SER A 83 -17.556 -2.007 -27.126 1.00 45.29 C ANISOU 429 CA SER A 83 5292 6620 5295 -94 252 -380 C ATOM 430 C SER A 83 -16.415 -1.136 -26.610 1.00 43.54 C ANISOU 430 C SER A 83 5033 6367 5141 -48 268 -336 C ATOM 431 O SER A 83 -16.232 0.002 -27.074 1.00 42.12 O ANISOU 431 O SER A 83 4831 6225 4947 -49 267 -281 O ATOM 432 CB SER A 83 -18.688 -2.068 -26.113 1.00 41.85 C ANISOU 432 CB SER A 83 4851 6170 4880 -103 197 -365 C ATOM 433 OG SER A 83 -19.095 -0.749 -25.783 1.00 50.87 O ANISOU 433 OG SER A 83 5955 7338 6035 -83 161 -294 O ATOM 434 N ASN A 84 -15.619 -1.664 -25.665 1.00 37.96 N ANISOU 434 N ASN A 84 4319 5595 4509 -12 281 -357 N ATOM 435 CA ASN A 84 -14.549 -0.847 -25.101 1.00 39.22 C ANISOU 435 CA ASN A 84 4434 5737 4730 21 289 -320 C ATOM 436 C ASN A 84 -13.522 -0.468 -26.159 1.00 40.97 C ANISOU 436 C ASN A 84 4637 6002 4927 18 342 -315 C ATOM 437 O ASN A 84 -13.044 0.669 -26.174 1.00 43.15 O ANISOU 437 O ASN A 84 4882 6293 5220 12 342 -263 O ATOM 438 CB ASN A 84 -13.837 -1.520 -23.921 1.00 42.64 C ANISOU 438 CB ASN A 84 4853 6110 5237 62 290 -337 C ATOM 439 CG ASN A 84 -14.762 -1.793 -22.740 1.00 53.12 C ANISOU 439 CG ASN A 84 6193 7404 6587 60 239 -330 C ATOM 440 OD1 ASN A 84 -14.824 -2.913 -22.230 1.00 57.79 O ANISOU 440 OD1 ASN A 84 6809 7952 7199 73 240 -358 O ATOM 441 ND2 ASN A 84 -15.607 -0.816 -22.418 1.00 52.45 N ANISOU 441 ND2 ASN A 84 6097 7341 6493 43 198 -294 N ATOM 442 N LEU A 85 -13.177 -1.392 -27.061 1.00 43.72 N ANISOU 442 N LEU A 85 5007 6370 5234 18 392 -371 N ATOM 443 CA LEU A 85 -12.131 -1.094 -28.040 1.00 44.52 C ANISOU 443 CA LEU A 85 5083 6526 5306 16 452 -371 C ATOM 444 C LEU A 85 -12.620 -0.084 -29.079 1.00 43.53 C ANISOU 444 C LEU A 85 4962 6474 5103 -32 446 -318 C ATOM 445 O LEU A 85 -11.867 0.825 -29.486 1.00 43.50 O ANISOU 445 O LEU A 85 4925 6507 5096 -44 471 -269 O ATOM 446 CB LEU A 85 -11.649 -2.388 -28.705 1.00 43.95 C ANISOU 446 CB LEU A 85 5036 6455 5209 37 513 -457 C ATOM 447 CG LEU A 85 -10.451 -2.256 -29.656 1.00 45.52 C ANISOU 447 CG LEU A 85 5198 6719 5378 46 587 -471 C ATOM 448 CD1 LEU A 85 -9.245 -1.745 -28.888 1.00 40.99 C ANISOU 448 CD1 LEU A 85 4553 6136 4885 83 598 -432 C ATOM 449 CD2 LEU A 85 -10.102 -3.573 -30.353 1.00 47.86 C ANISOU 449 CD2 LEU A 85 5527 7014 5644 73 652 -572 C ATOM 450 N LEU A 86 -13.888 -0.204 -29.498 1.00 39.65 N ANISOU 450 N LEU A 86 4509 6009 4548 -63 410 -320 N ATOM 451 CA LEU A 86 -14.489 0.835 -30.330 1.00 47.59 C ANISOU 451 CA LEU A 86 5515 7084 5485 -99 389 -250 C ATOM 452 C LEU A 86 -14.374 2.206 -29.668 1.00 49.65 C ANISOU 452 C LEU A 86 5748 7309 5809 -87 357 -162 C ATOM 453 O LEU A 86 -13.875 3.162 -30.282 1.00 47.93 O ANISOU 453 O LEU A 86 5517 7123 5573 -105 376 -99 O ATOM 454 CB LEU A 86 -15.953 0.506 -30.657 1.00 47.48 C ANISOU 454 CB LEU A 86 5529 7108 5401 -127 342 -259 C ATOM 455 CG LEU A 86 -16.144 -0.658 -31.628 1.00 51.12 C ANISOU 455 CG LEU A 86 6025 7622 5774 -163 374 -344 C ATOM 456 CD1 LEU A 86 -17.616 -1.029 -31.868 1.00 51.18 C ANISOU 456 CD1 LEU A 86 6055 7678 5715 -205 321 -359 C ATOM 457 CD2 LEU A 86 -15.461 -0.275 -32.925 1.00 49.94 C ANISOU 457 CD2 LEU A 86 5870 7561 5543 -185 425 -329 C ATOM 458 N PHE A 87 -14.823 2.324 -28.413 1.00 45.25 N ANISOU 458 N PHE A 87 5186 6684 5324 -62 311 -159 N ATOM 459 CA PHE A 87 -14.694 3.607 -27.718 1.00 43.20 C ANISOU 459 CA PHE A 87 4908 6380 5128 -51 285 -93 C ATOM 460 C PHE A 87 -13.251 4.103 -27.665 1.00 43.53 C ANISOU 460 C PHE A 87 4918 6406 5214 -59 328 -78 C ATOM 461 O PHE A 87 -12.980 5.287 -27.909 1.00 43.33 O ANISOU 461 O PHE A 87 4888 6375 5201 -79 329 -11 O ATOM 462 CB PHE A 87 -15.268 3.516 -26.308 1.00 41.49 C ANISOU 462 CB PHE A 87 4686 6101 4975 -23 239 -111 C ATOM 463 CG PHE A 87 -14.959 4.720 -25.473 1.00 43.36 C ANISOU 463 CG PHE A 87 4907 6283 5283 -13 221 -69 C ATOM 464 CD1 PHE A 87 -15.540 5.944 -25.748 1.00 44.68 C ANISOU 464 CD1 PHE A 87 5087 6442 5448 -13 198 -3 C ATOM 465 CD2 PHE A 87 -14.084 4.619 -24.393 1.00 44.79 C ANISOU 465 CD2 PHE A 87 5063 6421 5533 -3 225 -97 C ATOM 466 CE1 PHE A 87 -15.236 7.073 -24.977 1.00 46.85 C ANISOU 466 CE1 PHE A 87 5357 6649 5794 -8 185 25 C ATOM 467 CE2 PHE A 87 -13.788 5.736 -23.601 1.00 50.29 C ANISOU 467 CE2 PHE A 87 5748 7069 6291 -6 208 -72 C ATOM 468 CZ PHE A 87 -14.367 6.972 -23.901 1.00 48.05 C ANISOU 468 CZ PHE A 87 5486 6762 6010 -11 190 -15 C ATOM 469 N ILE A 88 -12.318 3.222 -27.317 1.00 42.30 N ANISOU 469 N ILE A 88 4740 6244 5089 -42 362 -135 N ATOM 470 CA ILE A 88 -10.914 3.601 -27.249 1.00 42.00 C ANISOU 470 CA ILE A 88 4656 6213 5091 -50 402 -125 C ATOM 471 C ILE A 88 -10.416 4.197 -28.559 1.00 46.42 C ANISOU 471 C ILE A 88 5209 6838 5590 -91 449 -81 C ATOM 472 O ILE A 88 -9.581 5.115 -28.548 1.00 44.90 O ANISOU 472 O ILE A 88 4986 6647 5429 -122 467 -35 O ATOM 473 CB ILE A 88 -10.114 2.372 -26.787 1.00 47.00 C ANISOU 473 CB ILE A 88 5262 6841 5756 -9 431 -194 C ATOM 474 CG1 ILE A 88 -10.450 2.130 -25.303 1.00 50.92 C ANISOU 474 CG1 ILE A 88 5756 7272 6319 21 379 -208 C ATOM 475 CG2 ILE A 88 -8.616 2.486 -27.120 1.00 48.75 C ANISOU 475 CG2 ILE A 88 5423 7108 5993 -13 490 -194 C ATOM 476 CD1 ILE A 88 -9.990 0.792 -24.743 1.00 53.86 C ANISOU 476 CD1 ILE A 88 6117 7624 6722 71 392 -264 C ATOM 477 N SER A 89 -10.942 3.735 -29.704 1.00 44.60 N ANISOU 477 N SER A 89 5008 6668 5268 -102 468 -93 N ATOM 478 CA SER A 89 -10.463 4.310 -30.963 1.00 43.98 C ANISOU 478 CA SER A 89 4924 6668 5120 -146 514 -44 C ATOM 479 C SER A 89 -10.810 5.804 -31.125 1.00 44.44 C ANISOU 479 C SER A 89 4996 6707 5182 -181 483 64 C ATOM 480 O SER A 89 -10.241 6.461 -32.004 1.00 47.11 O ANISOU 480 O SER A 89 5325 7097 5478 -225 522 124 O ATOM 481 CB SER A 89 -10.992 3.524 -32.170 1.00 41.61 C ANISOU 481 CB SER A 89 4654 6450 4706 -156 538 -83 C ATOM 482 OG SER A 89 -12.399 3.674 -32.322 1.00 46.06 O ANISOU 482 OG SER A 89 5259 7016 5226 -162 478 -56 O ATOM 483 N THR A 90 -11.690 6.375 -30.299 1.00 35.51 N ANISOU 483 N THR A 90 3887 5501 4103 -162 420 94 N ATOM 484 CA THR A 90 -12.017 7.795 -30.441 1.00 42.08 C ANISOU 484 CA THR A 90 4741 6298 4951 -183 395 195 C ATOM 485 C THR A 90 -11.096 8.710 -29.641 1.00 46.86 C ANISOU 485 C THR A 90 5326 6828 5651 -207 401 220 C ATOM 486 O THR A 90 -11.113 9.930 -29.861 1.00 49.93 O ANISOU 486 O THR A 90 5738 7175 6059 -237 395 305 O ATOM 487 CB THR A 90 -13.465 8.104 -29.997 1.00 38.27 C ANISOU 487 CB THR A 90 4292 5772 4479 -143 327 218 C ATOM 488 OG1 THR A 90 -13.606 7.845 -28.595 1.00 36.59 O ANISOU 488 OG1 THR A 90 4068 5486 4348 -109 296 159 O ATOM 489 CG2 THR A 90 -14.456 7.245 -30.740 1.00 35.58 C ANISOU 489 CG2 THR A 90 3964 5513 4042 -132 311 194 C ATOM 490 N LEU A 91 -10.309 8.163 -28.719 1.00 43.28 N ANISOU 490 N LEU A 91 4832 6355 5257 -197 412 150 N ATOM 491 CA LEU A 91 -9.570 8.972 -27.759 1.00 41.97 C ANISOU 491 CA LEU A 91 4645 6123 5181 -223 405 159 C ATOM 492 C LEU A 91 -8.467 9.837 -28.377 1.00 45.72 C ANISOU 492 C LEU A 91 5097 6619 5658 -297 452 219 C ATOM 493 O LEU A 91 -8.245 10.963 -27.898 1.00 47.00 O ANISOU 493 O LEU A 91 5270 6705 5882 -338 437 259 O ATOM 494 CB LEU A 91 -8.986 8.063 -26.685 1.00 43.06 C ANISOU 494 CB LEU A 91 4734 6260 5365 -194 402 75 C ATOM 495 CG LEU A 91 -10.083 7.304 -25.919 1.00 47.86 C ANISOU 495 CG LEU A 91 5369 6837 5979 -133 353 25 C ATOM 496 CD1 LEU A 91 -9.489 6.377 -24.862 1.00 48.71 C ANISOU 496 CD1 LEU A 91 5433 6944 6129 -102 349 -42 C ATOM 497 CD2 LEU A 91 -11.189 8.210 -25.350 1.00 41.76 C ANISOU 497 CD2 LEU A 91 4640 5991 5236 -122 300 56 C ATOM 498 N PRO A 92 -7.739 9.374 -29.407 1.00 45.84 N ANISOU 498 N PRO A 92 5079 6731 5607 -321 512 222 N ATOM 499 CA PRO A 92 -6.718 10.255 -30.007 1.00 47.06 C ANISOU 499 CA PRO A 92 5207 6915 5759 -403 559 289 C ATOM 500 C PRO A 92 -7.301 11.536 -30.560 1.00 48.39 C ANISOU 500 C PRO A 92 5439 7028 5918 -444 542 398 C ATOM 501 O PRO A 92 -6.629 12.578 -30.542 1.00 50.91 O ANISOU 501 O PRO A 92 5756 7307 6278 -518 559 458 O ATOM 502 CB PRO A 92 -6.106 9.392 -31.117 1.00 48.03 C ANISOU 502 CB PRO A 92 5289 7167 5791 -405 628 266 C ATOM 503 CG PRO A 92 -6.357 7.990 -30.679 1.00 52.19 C ANISOU 503 CG PRO A 92 5803 7711 6317 -325 620 162 C ATOM 504 CD PRO A 92 -7.703 8.026 -30.009 1.00 46.47 C ANISOU 504 CD PRO A 92 5139 6899 5617 -281 546 157 C ATOM 505 N PHE A 93 -8.562 11.497 -30.997 1.00 46.24 N ANISOU 505 N PHE A 93 5225 6747 5598 -398 506 428 N ATOM 506 CA PHE A 93 -9.226 12.691 -31.503 1.00 46.99 C ANISOU 506 CA PHE A 93 5382 6785 5688 -417 484 542 C ATOM 507 C PHE A 93 -9.547 13.671 -30.378 1.00 48.03 C ANISOU 507 C PHE A 93 5550 6769 5932 -408 437 553 C ATOM 508 O PHE A 93 -9.360 14.887 -30.534 1.00 52.28 O ANISOU 508 O PHE A 93 6126 7228 6509 -457 441 640 O ATOM 509 CB PHE A 93 -10.496 12.281 -32.243 1.00 50.01 C ANISOU 509 CB PHE A 93 5799 7220 5982 -362 453 566 C ATOM 510 CG PHE A 93 -10.240 11.464 -33.480 1.00 53.52 C ANISOU 510 CG PHE A 93 6221 7810 6304 -382 500 557 C ATOM 511 CD1 PHE A 93 -9.882 12.074 -34.676 1.00 54.60 C ANISOU 511 CD1 PHE A 93 6368 8013 6365 -442 538 659 C ATOM 512 CD2 PHE A 93 -10.357 10.082 -33.444 1.00 55.43 C ANISOU 512 CD2 PHE A 93 6436 8120 6503 -344 509 447 C ATOM 513 CE1 PHE A 93 -9.653 11.320 -35.821 1.00 59.06 C ANISOU 513 CE1 PHE A 93 6911 8724 6804 -462 585 642 C ATOM 514 CE2 PHE A 93 -10.134 9.316 -34.584 1.00 56.54 C ANISOU 514 CE2 PHE A 93 6563 8391 6529 -362 557 423 C ATOM 515 CZ PHE A 93 -9.775 9.936 -35.774 1.00 58.97 C ANISOU 515 CZ PHE A 93 6876 8778 6753 -420 596 516 C ATOM 516 N ARG A 94 -10.045 13.165 -29.242 1.00 40.37 N ANISOU 516 N ARG A 94 4573 5756 5011 -349 396 466 N ATOM 517 CA ARG A 94 -10.314 14.040 -28.103 1.00 45.09 C ANISOU 517 CA ARG A 94 5201 6222 5708 -340 358 456 C ATOM 518 C ARG A 94 -9.015 14.674 -27.608 1.00 48.11 C ANISOU 518 C ARG A 94 5560 6563 6158 -426 386 448 C ATOM 519 O ARG A 94 -8.952 15.892 -27.344 1.00 48.36 O ANISOU 519 O ARG A 94 5637 6482 6255 -467 379 494 O ATOM 520 CB ARG A 94 -10.995 13.228 -27.000 1.00 50.71 C ANISOU 520 CB ARG A 94 5899 6925 6443 -268 316 359 C ATOM 521 CG ARG A 94 -12.324 12.589 -27.458 1.00 55.11 C ANISOU 521 CG ARG A 94 6474 7532 6934 -195 286 364 C ATOM 522 CD ARG A 94 -12.957 11.713 -26.389 1.00 56.47 C ANISOU 522 CD ARG A 94 6629 7705 7123 -138 251 272 C ATOM 523 NE ARG A 94 -13.540 12.478 -25.297 1.00 63.65 N ANISOU 523 NE ARG A 94 7563 8516 8106 -106 214 258 N ATOM 524 CZ ARG A 94 -14.826 12.835 -25.248 1.00 59.46 C ANISOU 524 CZ ARG A 94 7062 7959 7573 -45 177 284 C ATOM 525 NH1 ARG A 94 -15.675 12.427 -26.192 1.00 50.12 N ANISOU 525 NH1 ARG A 94 5881 6850 6313 -15 166 326 N ATOM 526 NH2 ARG A 94 -15.276 13.555 -24.226 1.00 54.95 N ANISOU 526 NH2 ARG A 94 6510 7297 7071 -12 152 261 N ATOM 527 N ALA A 95 -7.948 13.865 -27.532 1.00 46.28 N ANISOU 527 N ALA A 95 5253 6422 5910 -456 421 391 N ATOM 528 CA ALA A 95 -6.633 14.402 -27.193 1.00 47.35 C ANISOU 528 CA ALA A 95 5345 6550 6094 -548 450 388 C ATOM 529 C ALA A 95 -6.217 15.498 -28.164 1.00 46.48 C ANISOU 529 C ALA A 95 5267 6418 5975 -637 487 498 C ATOM 530 O ALA A 95 -5.709 16.538 -27.739 1.00 49.49 O ANISOU 530 O ALA A 95 5666 6711 6425 -715 487 521 O ATOM 531 CB ALA A 95 -5.587 13.286 -27.165 1.00 46.80 C ANISOU 531 CB ALA A 95 5179 6606 5996 -552 486 324 C ATOM 532 N ASP A 96 -6.421 15.284 -29.468 1.00 42.32 N ANISOU 532 N ASP A 96 4750 5969 5360 -632 518 567 N ATOM 533 CA ASP A 96 -6.101 16.313 -30.453 1.00 46.02 C ANISOU 533 CA ASP A 96 5254 6423 5808 -716 552 689 C ATOM 534 C ASP A 96 -6.856 17.611 -30.174 1.00 47.81 C ANISOU 534 C ASP A 96 5578 6481 6106 -717 513 761 C ATOM 535 O ASP A 96 -6.270 18.709 -30.183 1.00 42.71 O ANISOU 535 O ASP A 96 4962 5751 5514 -810 531 824 O ATOM 536 CB ASP A 96 -6.399 15.786 -31.862 1.00 50.08 C ANISOU 536 CB ASP A 96 5768 7061 6200 -697 584 746 C ATOM 537 CG ASP A 96 -5.985 16.768 -32.960 1.00 63.14 C ANISOU 537 CG ASP A 96 7451 8724 7814 -789 625 884 C ATOM 538 OD1 ASP A 96 -5.584 17.906 -32.665 1.00 68.84 O ANISOU 538 OD1 ASP A 96 8207 9335 8612 -866 627 943 O ATOM 539 OD2 ASP A 96 -5.999 16.385 -34.139 1.00 71.80 O ANISOU 539 OD2 ASP A 96 8537 9944 8800 -795 661 932 O ATOM 540 N TYR A 97 -8.172 17.503 -29.977 1.00 47.16 N ANISOU 540 N TYR A 97 5546 6350 6024 -613 461 757 N ATOM 541 CA TYR A 97 -8.965 18.667 -29.613 1.00 45.81 C ANISOU 541 CA TYR A 97 5462 6015 5928 -588 424 813 C ATOM 542 C TYR A 97 -8.272 19.496 -28.546 1.00 47.64 C ANISOU 542 C TYR A 97 5709 6119 6271 -658 424 768 C ATOM 543 O TYR A 97 -8.025 20.698 -28.732 1.00 44.98 O ANISOU 543 O TYR A 97 5435 5665 5990 -726 436 848 O ATOM 544 CB TYR A 97 -10.350 18.230 -29.140 1.00 47.38 C ANISOU 544 CB TYR A 97 5681 6196 6125 -460 368 768 C ATOM 545 CG TYR A 97 -11.190 19.390 -28.671 1.00 50.81 C ANISOU 545 CG TYR A 97 6198 6464 6644 -414 332 811 C ATOM 546 CD1 TYR A 97 -11.722 20.304 -29.578 1.00 46.22 C ANISOU 546 CD1 TYR A 97 5684 5824 6054 -399 329 951 C ATOM 547 CD2 TYR A 97 -11.468 19.563 -27.312 1.00 52.60 C ANISOU 547 CD2 TYR A 97 6435 6594 6956 -377 303 711 C ATOM 548 CE1 TYR A 97 -12.482 21.369 -29.152 1.00 47.43 C ANISOU 548 CE1 TYR A 97 5914 5812 6293 -342 300 991 C ATOM 549 CE2 TYR A 97 -12.242 20.621 -26.875 1.00 51.63 C ANISOU 549 CE2 TYR A 97 6388 6315 6912 -325 277 738 C ATOM 550 CZ TYR A 97 -12.743 21.519 -27.799 1.00 51.19 C ANISOU 550 CZ TYR A 97 6401 6191 6858 -303 277 878 C ATOM 551 OH TYR A 97 -13.503 22.570 -27.360 1.00 56.03 O ANISOU 551 OH TYR A 97 7092 6639 7559 -237 255 904 O ATOM 552 N TYR A 98 -7.915 18.858 -27.428 1.00 47.47 N ANISOU 552 N TYR A 98 5631 6122 6282 -650 410 640 N ATOM 553 CA TYR A 98 -7.352 19.667 -26.343 1.00 48.45 C ANISOU 553 CA TYR A 98 5772 6132 6506 -719 402 587 C ATOM 554 C TYR A 98 -5.941 20.156 -26.668 1.00 51.63 C ANISOU 554 C TYR A 98 6139 6556 6920 -866 450 622 C ATOM 555 O TYR A 98 -5.579 21.283 -26.302 1.00 52.60 O ANISOU 555 O TYR A 98 6314 6550 7121 -952 453 638 O ATOM 556 CB TYR A 98 -7.376 18.890 -25.027 1.00 43.39 C ANISOU 556 CB TYR A 98 5079 5522 5886 -674 369 450 C ATOM 557 CG TYR A 98 -8.776 18.587 -24.590 1.00 43.05 C ANISOU 557 CG TYR A 98 5073 5444 5841 -546 324 417 C ATOM 558 CD1 TYR A 98 -9.556 19.536 -23.929 1.00 43.24 C ANISOU 558 CD1 TYR A 98 5174 5318 5937 -510 295 407 C ATOM 559 CD2 TYR A 98 -9.346 17.346 -24.873 1.00 42.60 C ANISOU 559 CD2 TYR A 98 4973 5503 5709 -462 313 395 C ATOM 560 CE1 TYR A 98 -10.867 19.232 -23.544 1.00 41.49 C ANISOU 560 CE1 TYR A 98 4974 5084 5709 -388 258 378 C ATOM 561 CE2 TYR A 98 -10.646 17.042 -24.504 1.00 34.88 C ANISOU 561 CE2 TYR A 98 4021 4509 4724 -356 273 369 C ATOM 562 CZ TYR A 98 -11.395 17.981 -23.843 1.00 36.17 C ANISOU 562 CZ TYR A 98 4247 4540 4954 -318 246 363 C ATOM 563 OH TYR A 98 -12.676 17.653 -23.481 1.00 37.16 O ANISOU 563 OH TYR A 98 4384 4668 5068 -212 211 337 O ATOM 564 N LEU A 99 -5.144 19.353 -27.380 1.00 48.42 N ANISOU 564 N LEU A 99 5648 6310 6438 -899 491 632 N ATOM 565 CA LEU A 99 -3.802 19.788 -27.750 1.00 49.96 C ANISOU 565 CA LEU A 99 5795 6551 6637 -1040 542 669 C ATOM 566 C LEU A 99 -3.792 20.969 -28.713 1.00 54.19 C ANISOU 566 C LEU A 99 6411 7002 7178 -1121 572 811 C ATOM 567 O LEU A 99 -2.762 21.642 -28.820 1.00 55.83 O ANISOU 567 O LEU A 99 6600 7199 7413 -1260 608 845 O ATOM 568 CB LEU A 99 -3.006 18.634 -28.348 1.00 46.74 C ANISOU 568 CB LEU A 99 5274 6343 6143 -1041 587 647 C ATOM 569 CG LEU A 99 -2.602 17.575 -27.333 1.00 49.41 C ANISOU 569 CG LEU A 99 5519 6762 6490 -992 567 519 C ATOM 570 CD1 LEU A 99 -1.941 16.410 -28.028 1.00 55.00 C ANISOU 570 CD1 LEU A 99 6129 7652 7117 -967 616 501 C ATOM 571 CD2 LEU A 99 -1.645 18.199 -26.327 1.00 43.47 C ANISOU 571 CD2 LEU A 99 4727 5973 5815 -1099 559 471 C ATOM 572 N ARG A 100 -4.894 21.235 -29.421 1.00 55.12 N ANISOU 572 N ARG A 100 6611 7064 7267 -1043 556 899 N ATOM 573 CA ARG A 100 -4.973 22.410 -30.283 1.00 54.20 C ANISOU 573 CA ARG A 100 6583 6850 7162 -1109 577 1049 C ATOM 574 C ARG A 100 -5.527 23.636 -29.574 1.00 52.25 C ANISOU 574 C ARG A 100 6449 6372 7033 -1107 542 1064 C ATOM 575 O ARG A 100 -5.917 24.590 -30.245 1.00 53.21 O ANISOU 575 O ARG A 100 6663 6381 7172 -1120 547 1196 O ATOM 576 CB ARG A 100 -5.837 22.131 -31.516 1.00 57.85 C ANISOU 576 CB ARG A 100 7074 7383 7524 -1028 576 1156 C ATOM 577 CG ARG A 100 -5.252 21.125 -32.452 1.00 63.67 C ANISOU 577 CG ARG A 100 7720 8335 8137 -1048 624 1159 C ATOM 578 CD ARG A 100 -6.085 20.917 -33.703 1.00 66.04 C ANISOU 578 CD ARG A 100 8052 8714 8327 -985 622 1263 C ATOM 579 NE ARG A 100 -5.500 19.803 -34.432 1.00 68.66 N ANISOU 579 NE ARG A 100 8291 9255 8540 -998 670 1225 N ATOM 580 CZ ARG A 100 -4.514 19.913 -35.308 1.00 72.16 C ANISOU 580 CZ ARG A 100 8692 9807 8918 -1105 738 1289 C ATOM 581 NH1 ARG A 100 -4.002 21.105 -35.597 1.00 75.71 N ANISOU 581 NH1 ARG A 100 9188 10174 9407 -1219 764 1408 N ATOM 582 NH2 ARG A 100 -4.039 18.821 -35.888 1.00 73.24 N ANISOU 582 NH2 ARG A 100 8743 10133 8951 -1097 784 1231 N ATOM 583 N GLY A 101 -5.598 23.632 -28.249 1.00 52.76 N ANISOU 583 N GLY A 101 6510 6360 7175 -1086 508 935 N ATOM 584 CA GLY A 101 -6.193 24.766 -27.565 1.00 54.58 C ANISOU 584 CA GLY A 101 6854 6369 7516 -1071 480 933 C ATOM 585 C GLY A 101 -7.706 24.750 -27.608 1.00 57.65 C ANISOU 585 C GLY A 101 7306 6695 7905 -903 437 957 C ATOM 586 O GLY A 101 -8.333 25.817 -27.597 1.00 59.00 O ANISOU 586 O GLY A 101 7585 6683 8149 -873 426 1021 O ATOM 587 N SER A 102 -8.305 23.556 -27.667 1.00 59.26 N ANISOU 587 N SER A 102 7442 7045 8028 -794 415 909 N ATOM 588 CA SER A 102 -9.758 23.389 -27.722 1.00 58.89 C ANISOU 588 CA SER A 102 7432 6977 7967 -637 373 927 C ATOM 589 C SER A 102 -10.309 23.864 -29.073 1.00 64.12 C ANISOU 589 C SER A 102 8149 7634 8581 -607 378 1099 C ATOM 590 O SER A 102 -11.233 24.673 -29.130 1.00 67.20 O ANISOU 590 O SER A 102 8620 7891 9020 -527 353 1169 O ATOM 591 CB SER A 102 -10.439 24.120 -26.559 1.00 56.37 C ANISOU 591 CB SER A 102 7181 6481 7755 -575 341 855 C ATOM 592 OG SER A 102 -9.991 23.637 -25.295 1.00 52.18 O ANISOU 592 OG SER A 102 6597 5975 7253 -601 331 697 O ATOM 593 N ASN A 103 -9.713 23.379 -30.168 1.00 64.91 N ANISOU 593 N ASN A 103 8200 7882 8580 -670 413 1170 N ATOM 594 CA ASN A 103 -10.165 23.657 -31.530 1.00 60.03 C ANISOU 594 CA ASN A 103 7618 7306 7886 -650 418 1334 C ATOM 595 C ASN A 103 -10.386 22.327 -32.242 1.00 56.61 C ANISOU 595 C ASN A 103 7100 7095 7313 -607 418 1312 C ATOM 596 O ASN A 103 -9.438 21.563 -32.454 1.00 56.06 O ANISOU 596 O ASN A 103 6955 7160 7185 -681 459 1258 O ATOM 597 CB ASN A 103 -9.152 24.511 -32.300 1.00 64.99 C ANISOU 597 CB ASN A 103 8280 7897 8517 -794 470 1457 C ATOM 598 CG ASN A 103 -9.709 25.029 -33.630 1.00 74.19 C ANISOU 598 CG ASN A 103 9502 9075 9613 -770 469 1649 C ATOM 599 OD1 ASN A 103 -10.865 24.784 -33.971 1.00 75.48 O ANISOU 599 OD1 ASN A 103 9676 9275 9729 -643 426 1689 O ATOM 600 ND2 ASN A 103 -8.872 25.723 -34.397 1.00 81.10 N ANISOU 600 ND2 ASN A 103 10406 9933 10474 -897 517 1773 N ATOM 601 N TRP A 104 -11.632 22.061 -32.617 1.00 56.87 N ANISOU 601 N TRP A 104 7145 7167 7295 -488 375 1350 N ATOM 602 CA TRP A 104 -12.026 20.826 -33.286 1.00 52.95 C ANISOU 602 CA TRP A 104 6582 6871 6667 -444 368 1322 C ATOM 603 C TRP A 104 -11.846 20.980 -34.796 1.00 57.86 C ANISOU 603 C TRP A 104 7212 7601 7172 -494 395 1468 C ATOM 604 O TRP A 104 -12.360 21.931 -35.391 1.00 60.29 O ANISOU 604 O TRP A 104 7586 7839 7483 -473 378 1618 O ATOM 605 CB TRP A 104 -13.476 20.501 -32.933 1.00 48.83 C ANISOU 605 CB TRP A 104 6064 6349 6142 -306 305 1292 C ATOM 606 CG TRP A 104 -13.979 19.237 -33.514 1.00 50.34 C ANISOU 606 CG TRP A 104 6191 6729 6205 -267 292 1251 C ATOM 607 CD1 TRP A 104 -14.805 19.099 -34.599 1.00 53.10 C ANISOU 607 CD1 TRP A 104 6543 7189 6446 -225 267 1346 C ATOM 608 CD2 TRP A 104 -13.699 17.916 -33.050 1.00 50.04 C ANISOU 608 CD2 TRP A 104 6084 6793 6134 -272 302 1101 C ATOM 609 NE1 TRP A 104 -15.052 17.765 -34.839 1.00 55.24 N ANISOU 609 NE1 TRP A 104 6751 7622 6616 -212 263 1254 N ATOM 610 CE2 TRP A 104 -14.386 17.019 -33.900 1.00 54.23 C ANISOU 610 CE2 TRP A 104 6584 7482 6538 -237 286 1105 C ATOM 611 CE3 TRP A 104 -12.937 17.401 -31.996 1.00 47.35 C ANISOU 611 CE3 TRP A 104 5706 6426 5857 -301 321 968 C ATOM 612 CZ2 TRP A 104 -14.326 15.633 -33.727 1.00 55.04 C ANISOU 612 CZ2 TRP A 104 6630 7698 6586 -233 293 976 C ATOM 613 CZ3 TRP A 104 -12.883 16.023 -31.823 1.00 49.25 C ANISOU 613 CZ3 TRP A 104 5886 6784 6043 -287 325 853 C ATOM 614 CH2 TRP A 104 -13.567 15.157 -32.687 1.00 50.89 C ANISOU 614 CH2 TRP A 104 6073 7128 6133 -254 314 856 C ATOM 615 N ILE A 105 -11.113 20.067 -35.425 1.00 57.65 N ANISOU 615 N ILE A 105 7117 7745 7041 -557 440 1429 N ATOM 616 CA ILE A 105 -10.871 20.203 -36.858 1.00 58.82 C ANISOU 616 CA ILE A 105 7270 8014 7066 -614 473 1560 C ATOM 617 C ILE A 105 -11.456 19.056 -37.659 1.00 59.77 C ANISOU 617 C ILE A 105 7341 8331 7036 -567 462 1527 C ATOM 618 O ILE A 105 -11.306 19.040 -38.885 1.00 58.46 O ANISOU 618 O ILE A 105 7172 8294 6745 -612 490 1621 O ATOM 619 CB ILE A 105 -9.372 20.362 -37.183 1.00 57.85 C ANISOU 619 CB ILE A 105 7116 7933 6932 -754 551 1573 C ATOM 620 CG1 ILE A 105 -8.600 19.091 -36.830 1.00 60.67 C ANISOU 620 CG1 ILE A 105 7377 8415 7258 -772 589 1407 C ATOM 621 CG2 ILE A 105 -8.794 21.568 -36.449 1.00 50.51 C ANISOU 621 CG2 ILE A 105 6238 6806 6146 -822 560 1611 C ATOM 622 CD1 ILE A 105 -7.187 19.076 -37.368 1.00 59.28 C ANISOU 622 CD1 ILE A 105 7148 8336 7040 -897 670 1422 C ATOM 623 N PHE A 106 -12.150 18.114 -37.017 1.00 59.07 N ANISOU 623 N PHE A 106 7220 8271 6952 -483 424 1397 N ATOM 624 CA PHE A 106 -12.513 16.864 -37.674 1.00 56.09 C ANISOU 624 CA PHE A 106 6794 8079 6440 -461 424 1330 C ATOM 625 C PHE A 106 -13.919 16.871 -38.267 1.00 58.74 C ANISOU 625 C PHE A 106 7149 8473 6695 -383 360 1403 C ATOM 626 O PHE A 106 -14.376 15.833 -38.762 1.00 58.85 O ANISOU 626 O PHE A 106 7128 8637 6598 -367 350 1339 O ATOM 627 CB PHE A 106 -12.373 15.698 -36.695 1.00 53.46 C ANISOU 627 CB PHE A 106 6410 7754 6148 -430 425 1145 C ATOM 628 CG PHE A 106 -10.976 15.506 -36.195 1.00 58.03 C ANISOU 628 CG PHE A 106 6949 8314 6783 -499 486 1068 C ATOM 629 CD1 PHE A 106 -9.999 14.959 -37.019 1.00 55.60 C ANISOU 629 CD1 PHE A 106 6597 8144 6385 -568 556 1051 C ATOM 630 CD2 PHE A 106 -10.655 15.802 -34.867 1.00 55.83 C ANISOU 630 CD2 PHE A 106 6671 7899 6644 -492 474 1003 C ATOM 631 CE1 PHE A 106 -8.720 14.769 -36.559 1.00 52.06 C ANISOU 631 CE1 PHE A 106 6097 7693 5989 -624 611 983 C ATOM 632 CE2 PHE A 106 -9.374 15.607 -34.389 1.00 49.28 C ANISOU 632 CE2 PHE A 106 5793 7069 5861 -556 523 934 C ATOM 633 CZ PHE A 106 -8.409 15.084 -35.236 1.00 53.22 C ANISOU 633 CZ PHE A 106 6240 7706 6274 -618 591 927 C ATOM 634 N GLY A 107 -14.618 17.995 -38.226 1.00 59.06 N ANISOU 634 N GLY A 107 7244 8404 6792 -334 315 1532 N ATOM 635 CA GLY A 107 -15.920 18.070 -38.845 1.00 59.36 C ANISOU 635 CA GLY A 107 7289 8515 6750 -256 251 1619 C ATOM 636 C GLY A 107 -17.052 17.829 -37.859 1.00 66.00 C ANISOU 636 C GLY A 107 8117 9296 7663 -147 188 1541 C ATOM 637 O GLY A 107 -16.873 17.280 -36.767 1.00 70.52 O ANISOU 637 O GLY A 107 8667 9809 8317 -135 194 1396 O ATOM 638 N ASP A 108 -18.247 18.227 -38.288 1.00 68.27 N ANISOU 638 N ASP A 108 8412 9617 7911 -65 126 1646 N ATOM 639 CA ASP A 108 -19.419 18.245 -37.417 1.00 66.39 C ANISOU 639 CA ASP A 108 8159 9321 7745 48 65 1604 C ATOM 640 C ASP A 108 -19.900 16.834 -37.071 1.00 61.85 C ANISOU 640 C ASP A 108 7518 8870 7112 55 48 1445 C ATOM 641 O ASP A 108 -20.212 16.528 -35.906 1.00 62.64 O ANISOU 641 O ASP A 108 7601 8895 7302 101 34 1332 O ATOM 642 CB ASP A 108 -20.515 19.048 -38.110 1.00 71.47 C ANISOU 642 CB ASP A 108 8816 9990 8349 134 5 1775 C ATOM 643 CG ASP A 108 -21.728 19.213 -37.259 1.00 84.69 C ANISOU 643 CG ASP A 108 10470 11608 10102 261 -53 1748 C ATOM 644 OD1 ASP A 108 -21.676 20.000 -36.290 1.00 90.19 O ANISOU 644 OD1 ASP A 108 11208 12113 10948 312 -47 1737 O ATOM 645 OD2 ASP A 108 -22.740 18.554 -37.566 1.00 91.98 O ANISOU 645 OD2 ASP A 108 11332 12686 10931 305 -104 1733 O ATOM 646 N LEU A 109 -19.991 15.970 -38.082 1.00 59.80 N ANISOU 646 N LEU A 109 7224 8800 6697 7 49 1434 N ATOM 647 CA LEU A 109 -20.394 14.587 -37.858 1.00 61.06 C ANISOU 647 CA LEU A 109 7332 9072 6798 -2 38 1282 C ATOM 648 C LEU A 109 -19.461 13.884 -36.879 1.00 61.15 C ANISOU 648 C LEU A 109 7339 9003 6893 -42 90 1125 C ATOM 649 O LEU A 109 -19.909 13.118 -36.017 1.00 60.31 O ANISOU 649 O LEU A 109 7206 8886 6824 -14 71 1006 O ATOM 650 CB LEU A 109 -20.426 13.854 -39.199 1.00 64.05 C ANISOU 650 CB LEU A 109 7688 9655 6993 -67 45 1292 C ATOM 651 CG LEU A 109 -20.826 12.380 -39.186 1.00 63.58 C ANISOU 651 CG LEU A 109 7587 9719 6854 -94 38 1137 C ATOM 652 CD1 LEU A 109 -22.246 12.185 -38.679 1.00 62.46 C ANISOU 652 CD1 LEU A 109 7407 9603 6723 -22 -38 1120 C ATOM 653 CD2 LEU A 109 -20.647 11.791 -40.578 1.00 62.58 C ANISOU 653 CD2 LEU A 109 7451 9782 6545 -171 57 1143 C ATOM 654 N ALA A 110 -18.156 14.142 -36.996 1.00 59.54 N ANISOU 654 N ALA A 110 7157 8749 6716 -109 154 1129 N ATOM 655 CA ALA A 110 -17.187 13.504 -36.114 1.00 50.49 C ANISOU 655 CA ALA A 110 5997 7541 5645 -144 201 992 C ATOM 656 C ALA A 110 -17.392 13.922 -34.657 1.00 49.26 C ANISOU 656 C ALA A 110 5851 7225 5640 -88 177 946 C ATOM 657 O ALA A 110 -17.208 13.112 -33.739 1.00 47.04 O ANISOU 657 O ALA A 110 5545 6921 5405 -84 183 817 O ATOM 658 CB ALA A 110 -15.776 13.834 -36.592 1.00 45.55 C ANISOU 658 CB ALA A 110 5383 6910 5015 -228 272 1025 C ATOM 659 N CYS A 111 -17.772 15.183 -34.427 1.00 48.67 N ANISOU 659 N CYS A 111 5815 7037 5641 -43 150 1050 N ATOM 660 CA CYS A 111 -18.057 15.661 -33.073 1.00 55.58 C ANISOU 660 CA CYS A 111 6702 7763 6651 15 128 1002 C ATOM 661 C CYS A 111 -19.270 14.940 -32.488 1.00 53.00 C ANISOU 661 C CYS A 111 6337 7487 6314 89 79 927 C ATOM 662 O CYS A 111 -19.249 14.444 -31.339 1.00 50.50 O ANISOU 662 O CYS A 111 6002 7123 6061 102 78 811 O ATOM 663 CB CYS A 111 -18.288 17.179 -33.126 1.00 62.64 C ANISOU 663 CB CYS A 111 7655 8526 7621 54 114 1135 C ATOM 664 SG CYS A 111 -18.648 18.020 -31.562 1.00 64.24 S ANISOU 664 SG CYS A 111 7889 8530 7990 129 94 1083 S ATOM 665 N ARG A 112 -20.345 14.890 -33.284 1.00 51.69 N ANISOU 665 N ARG A 112 6154 7426 6059 132 35 998 N ATOM 666 CA ARG A 112 -21.529 14.123 -32.922 1.00 53.19 C ANISOU 666 CA ARG A 112 6296 7698 6215 184 -12 934 C ATOM 667 C ARG A 112 -21.137 12.710 -32.486 1.00 52.89 C ANISOU 667 C ARG A 112 6228 7715 6152 129 12 784 C ATOM 668 O ARG A 112 -21.581 12.214 -31.435 1.00 54.51 O ANISOU 668 O ARG A 112 6411 7894 6408 158 -4 692 O ATOM 669 CB ARG A 112 -22.464 14.076 -34.132 1.00 57.56 C ANISOU 669 CB ARG A 112 6825 8403 6642 202 -54 1030 C ATOM 670 CG ARG A 112 -22.967 15.438 -34.619 1.00 61.41 C ANISOU 670 CG ARG A 112 7339 8845 7150 273 -85 1197 C ATOM 671 CD ARG A 112 -23.773 15.283 -35.923 1.00 70.47 C ANISOU 671 CD ARG A 112 8454 10174 8149 278 -129 1297 C ATOM 672 NE ARG A 112 -24.075 16.562 -36.575 1.00 76.82 N ANISOU 672 NE ARG A 112 9288 10942 8958 339 -155 1481 N ATOM 673 CZ ARG A 112 -25.185 17.269 -36.413 1.00 81.07 C ANISOU 673 CZ ARG A 112 9808 11462 9532 456 -210 1567 C ATOM 674 NH1 ARG A 112 -26.162 16.801 -35.666 1.00 90.06 N ANISOU 674 NH1 ARG A 112 10887 12640 10693 519 -246 1485 N ATOM 675 NH2 ARG A 112 -25.331 18.429 -37.041 1.00 78.20 N ANISOU 675 NH2 ARG A 112 9483 11051 9180 511 -227 1743 N ATOM 676 N ILE A 113 -20.276 12.059 -33.281 1.00 50.19 N ANISOU 676 N ILE A 113 5889 7447 5733 50 54 760 N ATOM 677 CA ILE A 113 -19.883 10.680 -32.988 1.00 49.03 C ANISOU 677 CA ILE A 113 5721 7347 5561 5 80 623 C ATOM 678 C ILE A 113 -19.066 10.587 -31.701 1.00 48.66 C ANISOU 678 C ILE A 113 5679 7178 5633 5 108 539 C ATOM 679 O ILE A 113 -19.184 9.605 -30.960 1.00 44.74 O ANISOU 679 O ILE A 113 5162 6684 5152 6 106 434 O ATOM 680 CB ILE A 113 -19.138 10.059 -34.184 1.00 52.51 C ANISOU 680 CB ILE A 113 6165 7896 5892 -68 126 613 C ATOM 681 CG1 ILE A 113 -20.082 9.884 -35.370 1.00 47.68 C ANISOU 681 CG1 ILE A 113 5542 7433 5142 -75 90 669 C ATOM 682 CG2 ILE A 113 -18.489 8.727 -33.812 1.00 54.08 C ANISOU 682 CG2 ILE A 113 6352 8106 6091 -104 166 471 C ATOM 683 CD1 ILE A 113 -19.376 9.490 -36.636 1.00 41.76 C ANISOU 683 CD1 ILE A 113 4799 6797 4272 -147 137 673 C ATOM 684 N MET A 114 -18.217 11.580 -31.410 1.00 49.70 N ANISOU 684 N MET A 114 5835 7205 5845 -4 133 585 N ATOM 685 CA MET A 114 -17.531 11.575 -30.112 1.00 47.75 C ANISOU 685 CA MET A 114 5585 6852 5706 -4 149 507 C ATOM 686 C MET A 114 -18.540 11.410 -28.978 1.00 47.96 C ANISOU 686 C MET A 114 5598 6841 5782 58 104 453 C ATOM 687 O MET A 114 -18.443 10.491 -28.142 1.00 43.72 O ANISOU 687 O MET A 114 5040 6307 5265 55 106 354 O ATOM 688 CB MET A 114 -16.734 12.867 -29.901 1.00 46.58 C ANISOU 688 CB MET A 114 5468 6588 5641 -24 170 570 C ATOM 689 CG MET A 114 -15.575 13.082 -30.844 1.00 49.69 C ANISOU 689 CG MET A 114 5867 7013 5998 -99 222 621 C ATOM 690 SD MET A 114 -14.305 11.795 -30.750 1.00 52.54 S ANISOU 690 SD MET A 114 6182 7445 6336 -155 277 508 S ATOM 691 CE MET A 114 -14.692 10.884 -32.251 1.00 43.91 C ANISOU 691 CE MET A 114 5080 6513 5089 -169 291 519 C ATOM 692 N SER A 115 -19.523 12.315 -28.950 1.00 49.38 N ANISOU 692 N SER A 115 5790 6989 5983 119 66 523 N ATOM 693 CA SER A 115 -20.553 12.261 -27.909 1.00 50.29 C ANISOU 693 CA SER A 115 5885 7081 6140 185 28 477 C ATOM 694 C SER A 115 -21.241 10.893 -27.866 1.00 52.10 C ANISOU 694 C SER A 115 6074 7424 6298 177 10 404 C ATOM 695 O SER A 115 -21.349 10.238 -26.805 1.00 46.90 O ANISOU 695 O SER A 115 5396 6749 5673 180 7 316 O ATOM 696 CB SER A 115 -21.577 13.362 -28.165 1.00 50.35 C ANISOU 696 CB SER A 115 5903 7064 6162 263 -7 574 C ATOM 697 OG SER A 115 -22.636 13.279 -27.238 1.00 60.55 O ANISOU 697 OG SER A 115 7164 8357 7484 331 -39 528 O ATOM 698 N TYR A 116 -21.699 10.446 -29.037 1.00 51.77 N ANISOU 698 N TYR A 116 6019 7498 6152 157 -2 442 N ATOM 699 CA TYR A 116 -22.499 9.232 -29.118 1.00 49.65 C ANISOU 699 CA TYR A 116 5717 7337 5811 140 -23 379 C ATOM 700 C TYR A 116 -21.698 8.015 -28.647 1.00 47.93 C ANISOU 700 C TYR A 116 5503 7108 5600 86 12 270 C ATOM 701 O TYR A 116 -22.204 7.182 -27.881 1.00 46.60 O ANISOU 701 O TYR A 116 5316 6951 5440 85 -2 198 O ATOM 702 CB TYR A 116 -22.987 9.065 -30.557 1.00 49.01 C ANISOU 702 CB TYR A 116 5626 7386 5608 116 -40 439 C ATOM 703 CG TYR A 116 -23.941 7.927 -30.794 1.00 48.12 C ANISOU 703 CG TYR A 116 5478 7395 5408 86 -69 382 C ATOM 704 CD1 TYR A 116 -25.286 8.042 -30.463 1.00 47.66 C ANISOU 704 CD1 TYR A 116 5375 7394 5342 132 -122 401 C ATOM 705 CD2 TYR A 116 -23.497 6.730 -31.341 1.00 45.35 C ANISOU 705 CD2 TYR A 116 5140 7105 4988 10 -41 305 C ATOM 706 CE1 TYR A 116 -26.166 7.002 -30.688 1.00 47.83 C ANISOU 706 CE1 TYR A 116 5359 7534 5280 89 -149 348 C ATOM 707 CE2 TYR A 116 -24.361 5.685 -31.565 1.00 44.40 C ANISOU 707 CE2 TYR A 116 4996 7085 4790 -31 -67 246 C ATOM 708 CZ TYR A 116 -25.691 5.822 -31.235 1.00 49.16 C ANISOU 708 CZ TYR A 116 5550 7748 5380 1 -122 269 C ATOM 709 OH TYR A 116 -26.550 4.766 -31.449 1.00 53.81 O ANISOU 709 OH TYR A 116 6111 8443 5891 -56 -148 209 O ATOM 710 N ASER A 117 -20.439 7.901 -29.082 0.71 46.58 N ANISOU 710 N ASER A 117 5355 6915 5429 43 59 261 N ATOM 711 N BSER A 117 -20.444 7.907 -29.101 0.29 46.91 N ANISOU 711 N BSER A 117 5396 6957 5469 43 59 262 N ATOM 712 CA ASER A 117 -19.627 6.749 -28.705 0.71 46.58 C ANISOU 712 CA ASER A 117 5355 6903 5438 6 95 165 C ATOM 713 CA BSER A 117 -19.586 6.788 -28.723 0.29 46.42 C ANISOU 713 CA BSER A 117 5336 6881 5419 6 96 167 C ATOM 714 C ASER A 117 -19.337 6.741 -27.207 0.71 44.11 C ANISOU 714 C ASER A 117 5036 6498 5226 31 92 115 C ATOM 715 C BSER A 117 -19.357 6.751 -27.217 0.29 44.26 C ANISOU 715 C BSER A 117 5056 6518 5245 31 91 116 C ATOM 716 O ASER A 117 -19.437 5.689 -26.560 0.71 42.71 O ANISOU 716 O ASER A 117 4851 6321 5054 23 91 41 O ATOM 717 O BSER A 117 -19.480 5.693 -26.584 0.29 43.23 O ANISOU 717 O BSER A 117 4917 6390 5118 24 90 43 O ATOM 718 CB ASER A 117 -18.329 6.720 -29.523 0.71 48.06 C ANISOU 718 CB ASER A 117 5556 7101 5603 -35 150 171 C ATOM 719 CB BSER A 117 -18.253 6.891 -29.470 0.29 47.65 C ANISOU 719 CB BSER A 117 5504 7038 5562 -33 151 179 C ATOM 720 OG ASER A 117 -17.420 7.727 -29.126 0.71 47.77 O ANISOU 720 OG ASER A 117 5524 6981 5644 -32 170 212 O ATOM 721 OG BSER A 117 -17.261 6.070 -28.877 0.29 46.65 O ANISOU 721 OG BSER A 117 5372 6875 5477 -47 188 99 O ATOM 722 N LEU A 118 -19.015 7.901 -26.627 1.00 42.69 N ANISOU 722 N LEU A 118 4863 6237 5122 56 89 155 N ATOM 723 CA LEU A 118 -18.824 7.971 -25.178 1.00 43.40 C ANISOU 723 CA LEU A 118 4944 6252 5294 77 82 104 C ATOM 724 C LEU A 118 -20.013 7.372 -24.432 1.00 45.73 C ANISOU 724 C LEU A 118 5219 6577 5578 104 46 64 C ATOM 725 O LEU A 118 -19.867 6.459 -23.595 1.00 42.36 O ANISOU 725 O LEU A 118 4782 6146 5166 94 48 -1 O ATOM 726 CB LEU A 118 -18.604 9.425 -24.739 1.00 42.39 C ANISOU 726 CB LEU A 118 4832 6035 5239 100 78 150 C ATOM 727 CG LEU A 118 -18.431 9.681 -23.232 1.00 46.02 C ANISOU 727 CG LEU A 118 5286 6422 5777 117 69 94 C ATOM 728 CD1 LEU A 118 -17.222 8.972 -22.668 1.00 50.69 C ANISOU 728 CD1 LEU A 118 5862 7007 6392 76 94 35 C ATOM 729 CD2 LEU A 118 -18.332 11.184 -22.930 1.00 45.51 C ANISOU 729 CD2 LEU A 118 5249 6260 5781 136 67 133 C ATOM 730 N TYR A 119 -21.217 7.850 -24.753 1.00 45.32 N ANISOU 730 N TYR A 119 5158 6565 5498 140 13 109 N ATOM 731 CA TYR A 119 -22.314 7.445 -23.879 1.00 37.55 C ANISOU 731 CA TYR A 119 4144 5610 4513 166 -17 72 C ATOM 732 C TYR A 119 -22.806 6.028 -24.185 1.00 38.08 C ANISOU 732 C TYR A 119 4198 5761 4509 121 -23 28 C ATOM 733 O TYR A 119 -23.175 5.285 -23.253 1.00 37.94 O ANISOU 733 O TYR A 119 4165 5749 4501 113 -31 -25 O ATOM 734 CB TYR A 119 -23.422 8.484 -23.921 1.00 36.26 C ANISOU 734 CB TYR A 119 3963 5458 4355 232 -48 130 C ATOM 735 CG TYR A 119 -22.945 9.793 -23.319 1.00 44.16 C ANISOU 735 CG TYR A 119 4989 6347 5444 275 -38 150 C ATOM 736 CD1 TYR A 119 -22.758 9.919 -21.939 1.00 46.86 C ANISOU 736 CD1 TYR A 119 5329 6628 5848 289 -33 87 C ATOM 737 CD2 TYR A 119 -22.750 10.917 -24.105 1.00 47.60 C ANISOU 737 CD2 TYR A 119 5452 6737 5895 298 -35 232 C ATOM 738 CE1 TYR A 119 -22.329 11.105 -21.376 1.00 45.76 C ANISOU 738 CE1 TYR A 119 5217 6383 5786 318 -23 91 C ATOM 739 CE2 TYR A 119 -22.338 12.114 -23.543 1.00 49.36 C ANISOU 739 CE2 TYR A 119 5709 6841 6204 329 -24 246 C ATOM 740 CZ TYR A 119 -22.128 12.201 -22.180 1.00 46.80 C ANISOU 740 CZ TYR A 119 5384 6456 5942 336 -18 168 C ATOM 741 OH TYR A 119 -21.725 13.390 -21.614 1.00 43.14 O ANISOU 741 OH TYR A 119 4958 5872 5561 358 -6 167 O ATOM 742 N VAL A 120 -22.747 5.600 -25.452 1.00 41.75 N ANISOU 742 N VAL A 120 4673 6289 4901 84 -16 44 N ATOM 743 CA VAL A 120 -23.160 4.235 -25.774 1.00 42.62 C ANISOU 743 CA VAL A 120 4781 6467 4946 30 -18 -11 C ATOM 744 C VAL A 120 -22.223 3.234 -25.114 1.00 42.86 C ANISOU 744 C VAL A 120 4836 6434 5016 3 16 -82 C ATOM 745 O VAL A 120 -22.681 2.263 -24.491 1.00 36.85 O ANISOU 745 O VAL A 120 4071 5678 4251 -21 7 -131 O ATOM 746 CB VAL A 120 -23.246 4.022 -27.297 1.00 40.76 C ANISOU 746 CB VAL A 120 4555 6316 4615 -9 -14 11 C ATOM 747 CG1 VAL A 120 -23.514 2.563 -27.598 1.00 39.80 C ANISOU 747 CG1 VAL A 120 4445 6244 4433 -75 -8 -66 C ATOM 748 CG2 VAL A 120 -24.382 4.850 -27.889 1.00 39.93 C ANISOU 748 CG2 VAL A 120 4416 6295 4460 21 -59 88 C ATOM 749 N ASN A 121 -20.898 3.462 -25.213 1.00 41.49 N ANISOU 749 N ASN A 121 4682 6203 4881 6 53 -83 N ATOM 750 CA ASN A 121 -19.956 2.577 -24.534 1.00 41.34 C ANISOU 750 CA ASN A 121 4675 6127 4905 -3 82 -140 C ATOM 751 C ASN A 121 -20.254 2.502 -23.043 1.00 38.82 C ANISOU 751 C ASN A 121 4340 5767 4643 18 59 -158 C ATOM 752 O ASN A 121 -20.266 1.416 -22.447 1.00 32.65 O ANISOU 752 O ASN A 121 3567 4971 3868 2 61 -201 O ATOM 753 CB ASN A 121 -18.527 3.079 -24.657 1.00 46.11 C ANISOU 753 CB ASN A 121 5281 6686 5552 6 119 -128 C ATOM 754 CG ASN A 121 -17.526 2.053 -24.166 1.00 49.53 C ANISOU 754 CG ASN A 121 5718 7081 6020 4 150 -183 C ATOM 755 OD1 ASN A 121 -17.830 0.862 -24.086 1.00 49.99 O ANISOU 755 OD1 ASN A 121 5794 7141 6060 -9 152 -229 O ATOM 756 ND2 ASN A 121 -16.483 2.555 -23.528 1.00 50.41 N ANISOU 756 ND2 ASN A 121 5811 7149 6194 21 162 -174 N ATOM 757 N MET A 122 -20.392 3.671 -22.408 1.00 37.73 N ANISOU 757 N MET A 122 4185 5604 4548 54 41 -125 N ATOM 758 CA MET A 122 -20.565 3.715 -20.957 1.00 41.44 C ANISOU 758 CA MET A 122 4639 6042 5064 74 24 -147 C ATOM 759 C MET A 122 -21.756 2.854 -20.522 1.00 48.10 C ANISOU 759 C MET A 122 5470 6934 5871 59 1 -170 C ATOM 760 O MET A 122 -21.627 1.968 -19.657 1.00 42.87 O ANISOU 760 O MET A 122 4811 6256 5222 43 2 -202 O ATOM 761 CB MET A 122 -20.744 5.177 -20.512 1.00 39.58 C ANISOU 761 CB MET A 122 4393 5776 4871 115 11 -118 C ATOM 762 CG MET A 122 -20.723 5.453 -19.004 1.00 45.39 C ANISOU 762 CG MET A 122 5114 6478 5653 134 0 -149 C ATOM 763 SD MET A 122 -21.026 7.212 -18.578 1.00 47.62 S ANISOU 763 SD MET A 122 5397 6710 5986 185 -10 -130 S ATOM 764 CE MET A 122 -19.531 8.012 -19.156 1.00 43.84 C ANISOU 764 CE MET A 122 4946 6158 5551 161 17 -105 C ATOM 765 N TYR A 123 -22.926 3.058 -21.146 1.00 49.12 N ANISOU 765 N TYR A 123 5583 7131 5951 58 -21 -147 N ATOM 766 CA TYR A 123 -24.063 2.345 -20.564 1.00 50.03 C ANISOU 766 CA TYR A 123 5673 7299 6035 37 -43 -167 C ATOM 767 C TYR A 123 -24.144 0.896 -21.054 1.00 52.28 C ANISOU 767 C TYR A 123 5983 7604 6276 -30 -34 -202 C ATOM 768 O TYR A 123 -24.612 0.018 -20.308 1.00 48.52 O ANISOU 768 O TYR A 123 5505 7134 5795 -64 -40 -227 O ATOM 769 CB TYR A 123 -25.364 3.134 -20.773 1.00 36.72 C ANISOU 769 CB TYR A 123 3943 5689 4320 69 -73 -132 C ATOM 770 CG TYR A 123 -25.271 4.440 -20.017 1.00 39.18 C ANISOU 770 CG TYR A 123 4241 5955 4691 139 -75 -115 C ATOM 771 CD1 TYR A 123 -25.356 4.458 -18.616 1.00 36.27 C ANISOU 771 CD1 TYR A 123 3858 5568 4357 154 -74 -147 C ATOM 772 CD2 TYR A 123 -25.100 5.658 -20.690 1.00 39.22 C ANISOU 772 CD2 TYR A 123 4254 5934 4715 187 -76 -66 C ATOM 773 CE1 TYR A 123 -25.239 5.636 -17.902 1.00 34.69 C ANISOU 773 CE1 TYR A 123 3651 5321 4207 214 -72 -148 C ATOM 774 CE2 TYR A 123 -24.990 6.853 -19.986 1.00 39.40 C ANISOU 774 CE2 TYR A 123 4277 5895 4800 247 -74 -59 C ATOM 775 CZ TYR A 123 -25.057 6.833 -18.593 1.00 39.53 C ANISOU 775 CZ TYR A 123 4279 5892 4848 260 -71 -107 C ATOM 776 OH TYR A 123 -24.952 8.010 -17.891 1.00 36.81 O ANISOU 776 OH TYR A 123 3940 5484 4561 315 -66 -115 O ATOM 777 N SER A 124 -23.621 0.597 -22.248 1.00 48.51 N ANISOU 777 N SER A 124 5536 7128 5768 -54 -15 -208 N ATOM 778 CA SER A 124 -23.529 -0.801 -22.648 1.00 47.29 C ANISOU 778 CA SER A 124 5419 6967 5582 -114 2 -257 C ATOM 779 C SER A 124 -22.604 -1.564 -21.717 1.00 42.79 C ANISOU 779 C SER A 124 4877 6308 5072 -108 26 -285 C ATOM 780 O SER A 124 -22.886 -2.712 -21.359 1.00 41.21 O ANISOU 780 O SER A 124 4702 6088 4869 -149 28 -316 O ATOM 781 CB SER A 124 -23.051 -0.908 -24.092 1.00 51.76 C ANISOU 781 CB SER A 124 6012 7555 6100 -134 26 -267 C ATOM 782 OG SER A 124 -23.992 -0.325 -24.974 1.00 52.03 O ANISOU 782 OG SER A 124 6017 7687 6065 -146 -3 -234 O ATOM 783 N SER A 125 -21.493 -0.937 -21.317 1.00 41.96 N ANISOU 783 N SER A 125 4768 6151 5024 -58 42 -270 N ATOM 784 CA SER A 125 -20.587 -1.538 -20.347 1.00 45.57 C ANISOU 784 CA SER A 125 5238 6540 5538 -41 56 -285 C ATOM 785 C SER A 125 -21.296 -1.813 -19.030 1.00 46.85 C ANISOU 785 C SER A 125 5385 6705 5711 -49 29 -279 C ATOM 786 O SER A 125 -21.196 -2.919 -18.478 1.00 42.98 O ANISOU 786 O SER A 125 4921 6178 5233 -69 34 -292 O ATOM 787 CB SER A 125 -19.388 -0.621 -20.113 1.00 46.86 C ANISOU 787 CB SER A 125 5383 6672 5751 4 69 -266 C ATOM 788 OG SER A 125 -18.600 -0.472 -21.279 1.00 45.39 O ANISOU 788 OG SER A 125 5207 6486 5554 6 102 -269 O ATOM 789 N ILE A 126 -22.006 -0.806 -18.503 1.00 45.23 N ANISOU 789 N ILE A 126 5141 6543 5503 -30 3 -257 N ATOM 790 CA ILE A 126 -22.694 -0.997 -17.226 1.00 43.33 C ANISOU 790 CA ILE A 126 4878 6322 5262 -37 -17 -254 C ATOM 791 C ILE A 126 -23.649 -2.191 -17.295 1.00 41.57 C ANISOU 791 C ILE A 126 4669 6127 4998 -100 -23 -265 C ATOM 792 O ILE A 126 -23.638 -3.061 -16.407 1.00 40.09 O ANISOU 792 O ILE A 126 4497 5915 4820 -125 -23 -265 O ATOM 793 CB ILE A 126 -23.386 0.307 -16.774 1.00 43.85 C ANISOU 793 CB ILE A 126 4898 6434 5328 1 -37 -239 C ATOM 794 CG1 ILE A 126 -22.329 1.360 -16.386 1.00 39.19 C ANISOU 794 CG1 ILE A 126 4306 5795 4790 48 -30 -236 C ATOM 795 CG2 ILE A 126 -24.335 0.067 -15.614 1.00 40.26 C ANISOU 795 CG2 ILE A 126 4414 6029 4855 -13 -52 -242 C ATOM 796 CD1 ILE A 126 -22.900 2.760 -16.110 1.00 33.66 C ANISOU 796 CD1 ILE A 126 3575 5113 4100 93 -42 -229 C ATOM 797 N TYR A 127 -24.427 -2.301 -18.386 1.00 35.69 N ANISOU 797 N TYR A 127 3924 5433 4204 -136 -28 -273 N ATOM 798 CA TYR A 127 -25.343 -3.446 -18.512 1.00 35.14 C ANISOU 798 CA TYR A 127 3868 5393 4092 -215 -34 -291 C ATOM 799 C TYR A 127 -24.643 -4.786 -18.766 1.00 39.15 C ANISOU 799 C TYR A 127 4447 5814 4616 -254 -7 -321 C ATOM 800 O TYR A 127 -25.099 -5.821 -18.265 1.00 43.82 O ANISOU 800 O TYR A 127 5064 6385 5202 -312 -8 -328 O ATOM 801 CB TYR A 127 -26.421 -3.155 -19.553 1.00 33.27 C ANISOU 801 CB TYR A 127 3599 5253 3788 -248 -53 -292 C ATOM 802 CG TYR A 127 -27.544 -2.394 -18.917 1.00 45.33 C ANISOU 802 CG TYR A 127 5054 6873 5298 -229 -81 -264 C ATOM 803 CD1 TYR A 127 -28.579 -3.096 -18.303 1.00 47.52 C ANISOU 803 CD1 TYR A 127 5305 7208 5544 -294 -93 -268 C ATOM 804 CD2 TYR A 127 -27.519 -1.009 -18.783 1.00 47.54 C ANISOU 804 CD2 TYR A 127 5293 7172 5598 -146 -90 -236 C ATOM 805 CE1 TYR A 127 -29.613 -2.445 -17.668 1.00 51.49 C ANISOU 805 CE1 TYR A 127 5731 7806 6027 -272 -112 -248 C ATOM 806 CE2 TYR A 127 -28.552 -0.344 -18.123 1.00 48.76 C ANISOU 806 CE2 TYR A 127 5380 7405 5741 -117 -109 -219 C ATOM 807 CZ TYR A 127 -29.594 -1.072 -17.577 1.00 48.87 C ANISOU 807 CZ TYR A 127 5357 7494 5716 -177 -119 -226 C ATOM 808 OH TYR A 127 -30.627 -0.448 -16.922 1.00 46.60 O ANISOU 808 OH TYR A 127 4994 7299 5413 -145 -132 -213 O ATOM 809 N PHE A 128 -23.559 -4.815 -19.538 1.00 36.51 N ANISOU 809 N PHE A 128 4147 5424 4301 -223 21 -340 N ATOM 810 CA PHE A 128 -22.854 -6.081 -19.733 1.00 38.32 C ANISOU 810 CA PHE A 128 4444 5563 4555 -242 52 -374 C ATOM 811 C PHE A 128 -22.275 -6.588 -18.418 1.00 38.32 C ANISOU 811 C PHE A 128 4456 5490 4613 -213 54 -348 C ATOM 812 O PHE A 128 -22.326 -7.791 -18.127 1.00 38.95 O ANISOU 812 O PHE A 128 4587 5503 4707 -250 64 -357 O ATOM 813 CB PHE A 128 -21.766 -5.893 -20.784 1.00 44.31 C ANISOU 813 CB PHE A 128 5221 6293 5320 -202 86 -399 C ATOM 814 CG PHE A 128 -22.289 -5.756 -22.184 1.00 45.88 C ANISOU 814 CG PHE A 128 5426 6558 5449 -245 89 -429 C ATOM 815 CD1 PHE A 128 -23.513 -6.312 -22.547 1.00 45.73 C ANISOU 815 CD1 PHE A 128 5415 6590 5369 -329 70 -453 C ATOM 816 CD2 PHE A 128 -21.614 -4.945 -23.104 1.00 45.19 C ANISOU 816 CD2 PHE A 128 5324 6500 5347 -208 107 -425 C ATOM 817 CE1 PHE A 128 -24.007 -6.167 -23.839 1.00 46.68 C ANISOU 817 CE1 PHE A 128 5533 6791 5412 -372 66 -479 C ATOM 818 CE2 PHE A 128 -22.098 -4.772 -24.384 1.00 48.61 C ANISOU 818 CE2 PHE A 128 5759 7009 5703 -247 107 -443 C ATOM 819 CZ PHE A 128 -23.308 -5.378 -24.760 1.00 49.01 C ANISOU 819 CZ PHE A 128 5818 7116 5688 -328 83 -471 C ATOM 820 N LEU A 129 -21.759 -5.671 -17.595 1.00 35.46 N ANISOU 820 N LEU A 129 4049 5142 4282 -153 41 -313 N ATOM 821 CA LEU A 129 -21.250 -6.025 -16.270 1.00 39.60 C ANISOU 821 CA LEU A 129 4574 5626 4848 -127 35 -281 C ATOM 822 C LEU A 129 -22.360 -6.572 -15.373 1.00 43.28 C ANISOU 822 C LEU A 129 5039 6118 5287 -185 14 -260 C ATOM 823 O LEU A 129 -22.194 -7.606 -14.697 1.00 40.87 O ANISOU 823 O LEU A 129 4773 5754 5003 -202 17 -239 O ATOM 824 CB LEU A 129 -20.594 -4.790 -15.641 1.00 29.30 C ANISOU 824 CB LEU A 129 3215 4351 3567 -66 22 -260 C ATOM 825 CG LEU A 129 -19.305 -4.367 -16.340 1.00 33.36 C ANISOU 825 CG LEU A 129 3726 4834 4114 -16 46 -271 C ATOM 826 CD1 LEU A 129 -18.802 -2.992 -15.902 1.00 33.69 C ANISOU 826 CD1 LEU A 129 3717 4909 4174 22 33 -257 C ATOM 827 CD2 LEU A 129 -18.257 -5.411 -16.004 1.00 35.32 C ANISOU 827 CD2 LEU A 129 4002 5010 4407 15 64 -265 C ATOM 828 N THR A 130 -23.504 -5.878 -15.350 1.00 44.56 N ANISOU 828 N THR A 130 5154 6373 5404 -214 -7 -259 N ATOM 829 CA THR A 130 -24.603 -6.308 -14.492 1.00 43.02 C ANISOU 829 CA THR A 130 4944 6227 5176 -273 -23 -239 C ATOM 830 C THR A 130 -25.092 -7.696 -14.892 1.00 42.28 C ANISOU 830 C THR A 130 4909 6088 5068 -359 -13 -251 C ATOM 831 O THR A 130 -25.243 -8.587 -14.033 1.00 43.24 O ANISOU 831 O THR A 130 5059 6174 5197 -400 -12 -221 O ATOM 832 CB THR A 130 -25.729 -5.275 -14.552 1.00 41.38 C ANISOU 832 CB THR A 130 4665 6135 4922 -276 -43 -241 C ATOM 833 OG1 THR A 130 -25.200 -4.012 -14.140 1.00 38.67 O ANISOU 833 OG1 THR A 130 4283 5807 4602 -196 -48 -236 O ATOM 834 CG2 THR A 130 -26.853 -5.650 -13.602 1.00 41.13 C ANISOU 834 CG2 THR A 130 4601 6174 4853 -335 -54 -221 C ATOM 835 N VAL A 131 -25.299 -7.913 -16.198 1.00 37.32 N ANISOU 835 N VAL A 131 4304 5456 4418 -393 -3 -294 N ATOM 836 CA VAL A 131 -25.716 -9.231 -16.668 1.00 44.26 C ANISOU 836 CA VAL A 131 5250 6281 5284 -484 10 -322 C ATOM 837 C VAL A 131 -24.688 -10.289 -16.288 1.00 42.55 C ANISOU 837 C VAL A 131 5114 5922 5132 -462 36 -314 C ATOM 838 O VAL A 131 -25.050 -11.396 -15.866 1.00 40.17 O ANISOU 838 O VAL A 131 4866 5559 4838 -530 41 -302 O ATOM 839 CB VAL A 131 -25.987 -9.204 -18.186 1.00 49.23 C ANISOU 839 CB VAL A 131 5891 6941 5872 -520 17 -380 C ATOM 840 CG1 VAL A 131 -26.243 -10.624 -18.724 1.00 46.91 C ANISOU 840 CG1 VAL A 131 5683 6571 5571 -617 36 -428 C ATOM 841 CG2 VAL A 131 -27.208 -8.321 -18.482 1.00 46.47 C ANISOU 841 CG2 VAL A 131 5459 6743 5456 -549 -16 -373 C ATOM 842 N LEU A 132 -23.395 -9.968 -16.420 1.00 41.64 N ANISOU 842 N LEU A 132 5005 5753 5064 -366 53 -315 N ATOM 843 CA LEU A 132 -22.362 -10.953 -16.121 1.00 46.13 C ANISOU 843 CA LEU A 132 5640 6191 5696 -325 78 -305 C ATOM 844 C LEU A 132 -22.425 -11.409 -14.663 1.00 46.15 C ANISOU 844 C LEU A 132 5645 6169 5719 -328 60 -233 C ATOM 845 O LEU A 132 -22.350 -12.614 -14.369 1.00 48.12 O ANISOU 845 O LEU A 132 5968 6315 6001 -356 73 -214 O ATOM 846 CB LEU A 132 -20.990 -10.371 -16.440 1.00 52.62 C ANISOU 846 CB LEU A 132 6442 6993 6559 -219 95 -312 C ATOM 847 CG LEU A 132 -19.872 -11.386 -16.226 1.00 65.12 C ANISOU 847 CG LEU A 132 8082 8450 8210 -160 124 -303 C ATOM 848 CD1 LEU A 132 -20.044 -12.570 -17.181 1.00 63.95 C ANISOU 848 CD1 LEU A 132 8026 8204 8068 -206 161 -365 C ATOM 849 CD2 LEU A 132 -18.516 -10.731 -16.414 1.00 72.04 C ANISOU 849 CD2 LEU A 132 8916 9333 9123 -57 138 -303 C ATOM 850 N SER A 133 -22.561 -10.464 -13.733 1.00 38.29 N ANISOU 850 N SER A 133 4577 5266 4706 -301 32 -191 N ATOM 851 CA SER A 133 -22.702 -10.864 -12.333 1.00 39.92 C ANISOU 851 CA SER A 133 4780 5473 4913 -314 14 -122 C ATOM 852 C SER A 133 -23.942 -11.730 -12.112 1.00 40.53 C ANISOU 852 C SER A 133 4891 5553 4956 -429 12 -108 C ATOM 853 O SER A 133 -23.891 -12.741 -11.385 1.00 39.88 O ANISOU 853 O SER A 133 4862 5398 4894 -458 15 -54 O ATOM 854 CB SER A 133 -22.740 -9.639 -11.419 1.00 41.36 C ANISOU 854 CB SER A 133 4877 5769 5069 -275 -12 -98 C ATOM 855 OG SER A 133 -21.492 -8.970 -11.381 1.00 42.17 O ANISOU 855 OG SER A 133 4954 5860 5208 -181 -13 -100 O ATOM 856 N VAL A 134 -25.071 -11.342 -12.715 1.00 39.82 N ANISOU 856 N VAL A 134 4766 5551 4811 -499 7 -148 N ATOM 857 CA VAL A 134 -26.289 -12.132 -12.530 1.00 46.29 C ANISOU 857 CA VAL A 134 5604 6392 5592 -623 4 -137 C ATOM 858 C VAL A 134 -26.077 -13.554 -13.028 1.00 51.60 C ANISOU 858 C VAL A 134 6387 6914 6304 -680 29 -151 C ATOM 859 O VAL A 134 -26.495 -14.534 -12.387 1.00 55.11 O ANISOU 859 O VAL A 134 6881 7305 6752 -758 32 -106 O ATOM 860 CB VAL A 134 -27.487 -11.465 -13.232 1.00 45.39 C ANISOU 860 CB VAL A 134 5423 6412 5413 -682 -9 -181 C ATOM 861 CG1 VAL A 134 -28.708 -12.393 -13.178 1.00 50.34 C ANISOU 861 CG1 VAL A 134 6066 7062 5999 -826 -9 -177 C ATOM 862 CG2 VAL A 134 -27.810 -10.132 -12.573 1.00 33.65 C ANISOU 862 CG2 VAL A 134 3831 5059 3893 -624 -29 -162 C ATOM 863 N VAL A 135 -25.431 -13.688 -14.184 1.00 48.95 N ANISOU 863 N VAL A 135 6097 6506 5997 -643 50 -216 N ATOM 864 CA VAL A 135 -25.205 -15.006 -14.755 1.00 48.40 C ANISOU 864 CA VAL A 135 6140 6284 5967 -689 81 -249 C ATOM 865 C VAL A 135 -24.331 -15.855 -13.838 1.00 48.34 C ANISOU 865 C VAL A 135 6199 6138 6032 -634 93 -181 C ATOM 866 O VAL A 135 -24.624 -17.035 -13.611 1.00 46.48 O ANISOU 866 O VAL A 135 6049 5790 5820 -707 106 -161 O ATOM 867 CB VAL A 135 -24.621 -14.863 -16.171 1.00 49.61 C ANISOU 867 CB VAL A 135 6318 6406 6126 -648 106 -339 C ATOM 868 CG1 VAL A 135 -24.139 -16.199 -16.698 1.00 46.36 C ANISOU 868 CG1 VAL A 135 6028 5818 5768 -666 147 -384 C ATOM 869 CG2 VAL A 135 -25.708 -14.330 -17.100 1.00 48.57 C ANISOU 869 CG2 VAL A 135 6138 6404 5914 -734 91 -397 C ATOM 870 N ARG A 136 -23.243 -15.287 -13.301 1.00 44.21 N ANISOU 870 N ARG A 136 5636 5619 5543 -506 86 -140 N ATOM 871 CA ARG A 136 -22.402 -16.088 -12.409 1.00 44.56 C ANISOU 871 CA ARG A 136 5732 5547 5651 -445 91 -63 C ATOM 872 C ARG A 136 -23.159 -16.554 -11.165 1.00 50.31 C ANISOU 872 C ARG A 136 6468 6294 6355 -523 69 29 C ATOM 873 O ARG A 136 -22.986 -17.700 -10.723 1.00 50.44 O ANISOU 873 O ARG A 136 6571 6177 6417 -539 80 85 O ATOM 874 CB ARG A 136 -21.142 -15.330 -12.004 1.00 44.29 C ANISOU 874 CB ARG A 136 5636 5546 5647 -305 81 -33 C ATOM 875 CG ARG A 136 -20.127 -15.105 -13.119 1.00 46.28 C ANISOU 875 CG ARG A 136 5891 5755 5937 -216 111 -105 C ATOM 876 CD ARG A 136 -19.506 -16.440 -13.543 1.00 49.49 C ANISOU 876 CD ARG A 136 6405 5981 6417 -183 151 -119 C ATOM 877 NE ARG A 136 -18.369 -16.270 -14.445 1.00 52.55 N ANISOU 877 NE ARG A 136 6786 6336 6844 -79 186 -179 N ATOM 878 CZ ARG A 136 -17.696 -17.269 -15.016 1.00 55.68 C ANISOU 878 CZ ARG A 136 7264 6586 7305 -26 231 -215 C ATOM 879 NH1 ARG A 136 -18.057 -18.535 -14.820 1.00 59.51 N ANISOU 879 NH1 ARG A 136 7857 6924 7829 -70 247 -199 N ATOM 880 NH2 ARG A 136 -16.656 -17.002 -15.790 1.00 51.29 N ANISOU 880 NH2 ARG A 136 6683 6029 6776 72 265 -269 N ATOM 881 N TYR A 137 -23.969 -15.678 -10.561 1.00 51.35 N ANISOU 881 N TYR A 137 6509 6587 6416 -566 41 49 N ATOM 882 CA TYR A 137 -24.837 -16.124 -9.469 1.00 48.30 C ANISOU 882 CA TYR A 137 6123 6239 5991 -659 27 128 C ATOM 883 C TYR A 137 -25.717 -17.299 -9.887 1.00 48.19 C ANISOU 883 C TYR A 137 6197 6135 5978 -798 46 116 C ATOM 884 O TYR A 137 -25.744 -18.356 -9.224 1.00 50.74 O ANISOU 884 O TYR A 137 6596 6353 6328 -844 53 193 O ATOM 885 CB TYR A 137 -25.688 -14.959 -8.960 1.00 49.27 C ANISOU 885 CB TYR A 137 6130 6560 6032 -686 3 126 C ATOM 886 CG TYR A 137 -26.782 -15.399 -8.020 1.00 52.14 C ANISOU 886 CG TYR A 137 6483 6990 6340 -802 -3 190 C ATOM 887 CD1 TYR A 137 -26.508 -15.833 -6.731 1.00 55.23 C ANISOU 887 CD1 TYR A 137 6888 7370 6726 -796 -12 294 C ATOM 888 CD2 TYR A 137 -28.103 -15.378 -8.437 1.00 52.96 C ANISOU 888 CD2 TYR A 137 6554 7181 6388 -922 0 151 C ATOM 889 CE1 TYR A 137 -27.527 -16.253 -5.895 1.00 55.77 C ANISOU 889 CE1 TYR A 137 6945 7508 6736 -913 -13 357 C ATOM 890 CE2 TYR A 137 -29.118 -15.781 -7.610 1.00 56.02 C ANISOU 890 CE2 TYR A 137 6922 7642 6721 -1037 0 209 C ATOM 891 CZ TYR A 137 -28.830 -16.221 -6.344 1.00 58.03 C ANISOU 891 CZ TYR A 137 7198 7881 6972 -1034 -5 312 C ATOM 892 OH TYR A 137 -29.870 -16.619 -5.530 1.00 65.57 O ANISOU 892 OH TYR A 137 8130 8921 7864 -1158 -1 374 O ATOM 893 N LEU A 138 -26.453 -17.131 -10.987 1.00 48.74 N ANISOU 893 N LEU A 138 6257 6245 6017 -871 55 24 N ATOM 894 CA LEU A 138 -27.356 -18.194 -11.422 1.00 52.71 C ANISOU 894 CA LEU A 138 6836 6678 6512 -1023 70 0 C ATOM 895 C LEU A 138 -26.596 -19.490 -11.693 1.00 56.52 C ANISOU 895 C LEU A 138 7462 6931 7083 -1010 102 2 C ATOM 896 O LEU A 138 -27.121 -20.583 -11.447 1.00 58.60 O ANISOU 896 O LEU A 138 7812 7093 7362 -1124 114 34 O ATOM 897 CB LEU A 138 -28.141 -17.746 -12.657 1.00 50.97 C ANISOU 897 CB LEU A 138 6575 6552 6239 -1092 69 -106 C ATOM 898 CG LEU A 138 -29.111 -16.575 -12.422 1.00 53.97 C ANISOU 898 CG LEU A 138 6816 7156 6534 -1116 40 -103 C ATOM 899 CD1 LEU A 138 -29.754 -16.091 -13.732 1.00 58.21 C ANISOU 899 CD1 LEU A 138 7309 7787 7021 -1161 33 -199 C ATOM 900 CD2 LEU A 138 -30.189 -16.937 -11.400 1.00 50.94 C ANISOU 900 CD2 LEU A 138 6401 6850 6103 -1237 31 -33 C ATOM 901 N ALA A 139 -25.347 -19.389 -12.145 1.00 54.98 N ANISOU 901 N ALA A 139 7294 6648 6949 -869 117 -28 N ATOM 902 CA ALA A 139 -24.552 -20.580 -12.409 1.00 60.15 C ANISOU 902 CA ALA A 139 8079 7081 7694 -830 152 -31 C ATOM 903 C ALA A 139 -24.137 -21.267 -11.117 1.00 66.23 C ANISOU 903 C ALA A 139 8895 7758 8512 -794 145 103 C ATOM 904 O ALA A 139 -24.324 -22.480 -10.972 1.00 63.57 O ANISOU 904 O ALA A 139 8675 7257 8222 -862 165 136 O ATOM 905 CB ALA A 139 -23.321 -20.223 -13.238 1.00 62.77 C ANISOU 905 CB ALA A 139 8408 7370 8073 -681 175 -99 C ATOM 906 N MET A 140 -23.567 -20.514 -10.164 1.00 72.37 N ANISOU 906 N MET A 140 9585 8636 9276 -691 115 185 N ATOM 907 CA MET A 140 -23.160 -21.147 -8.911 1.00 70.72 C ANISOU 907 CA MET A 140 9413 8359 9100 -655 101 323 C ATOM 908 C MET A 140 -24.322 -21.859 -8.262 1.00 73.93 C ANISOU 908 C MET A 140 9865 8756 9470 -818 98 391 C ATOM 909 O MET A 140 -24.103 -22.848 -7.554 1.00 72.52 O ANISOU 909 O MET A 140 9773 8445 9337 -823 101 497 O ATOM 910 CB MET A 140 -22.560 -20.161 -7.892 1.00 66.23 C ANISOU 910 CB MET A 140 8731 7939 8496 -551 63 396 C ATOM 911 CG MET A 140 -23.515 -19.118 -7.337 1.00 66.19 C ANISOU 911 CG MET A 140 8612 8149 8387 -626 34 398 C ATOM 912 SD MET A 140 -22.818 -17.983 -6.096 1.00 69.73 S ANISOU 912 SD MET A 140 8939 8765 8789 -516 -8 468 S ATOM 913 CE MET A 140 -22.776 -18.957 -4.599 1.00 73.49 C ANISOU 913 CE MET A 140 9465 9199 9258 -540 -26 637 C ATOM 914 N VAL A 141 -25.555 -21.402 -8.505 1.00 81.82 N ANISOU 914 N VAL A 141 10805 9893 10388 -953 92 339 N ATOM 915 CA VAL A 141 -26.698 -22.185 -8.028 1.00 90.22 C ANISOU 915 CA VAL A 141 11915 10945 11419 -1128 95 394 C ATOM 916 C VAL A 141 -26.693 -23.595 -8.634 1.00105.55 C ANISOU 916 C VAL A 141 14018 12645 13439 -1200 131 373 C ATOM 917 O VAL A 141 -27.028 -24.574 -7.955 1.00106.47 O ANISOU 917 O VAL A 141 14220 12657 13576 -1290 138 469 O ATOM 918 CB VAL A 141 -28.024 -21.448 -8.302 1.00 82.57 C ANISOU 918 CB VAL A 141 10844 10178 10351 -1255 84 331 C ATOM 919 CG1 VAL A 141 -29.205 -22.320 -7.921 1.00 79.20 C ANISOU 919 CG1 VAL A 141 10461 9741 9892 -1451 93 380 C ATOM 920 CG2 VAL A 141 -28.083 -20.149 -7.515 1.00 79.71 C ANISOU 920 CG2 VAL A 141 10335 10033 9916 -1185 54 363 C ATOM 921 N HIS A 142 -26.284 -23.733 -9.905 1.00120.19 N ANISOU 921 N HIS A 142 15925 14401 15341 -1163 157 248 N ATOM 922 CA HIS A 142 -26.447 -24.987 -10.657 1.00126.77 C ANISOU 922 CA HIS A 142 16910 15019 16237 -1253 196 190 C ATOM 923 C HIS A 142 -25.130 -25.467 -11.262 1.00127.26 C ANISOU 923 C HIS A 142 17063 14885 16403 -1094 230 146 C ATOM 924 O HIS A 142 -24.922 -25.361 -12.479 1.00125.23 O ANISOU 924 O HIS A 142 16824 14602 16155 -1075 255 8 O ATOM 925 CB HIS A 142 -27.477 -24.806 -11.772 1.00130.71 C ANISOU 925 CB HIS A 142 17389 15603 16673 -1401 202 54 C ATOM 926 CG HIS A 142 -28.829 -24.405 -11.279 1.00135.35 C ANISOU 926 CG HIS A 142 17882 16386 17160 -1560 174 88 C ATOM 927 ND1 HIS A 142 -29.686 -25.281 -10.649 1.00139.26 N ANISOU 927 ND1 HIS A 142 18435 16832 17647 -1728 178 161 N ATOM 928 CD2 HIS A 142 -29.471 -23.214 -11.323 1.00135.48 C ANISOU 928 CD2 HIS A 142 17745 16649 17083 -1572 144 61 C ATOM 929 CE1 HIS A 142 -30.799 -24.646 -10.326 1.00139.27 C ANISOU 929 CE1 HIS A 142 18312 17056 17547 -1837 154 174 C ATOM 930 NE2 HIS A 142 -30.694 -23.391 -10.725 1.00136.62 N ANISOU 930 NE2 HIS A 142 17849 16900 17162 -1738 133 113 N ATOM 931 N PRO A 143 -24.226 -26.030 -10.450 1.00127.93 N ANISOU 931 N PRO A 143 17206 14835 16567 -977 232 261 N ATOM 932 CA PRO A 143 -22.902 -26.410 -10.982 1.00126.87 C ANISOU 932 CA PRO A 143 17137 14535 16534 -801 265 223 C ATOM 933 C PRO A 143 -22.924 -27.567 -11.974 1.00126.42 C ANISOU 933 C PRO A 143 17241 14240 16551 -852 321 119 C ATOM 934 O PRO A 143 -21.991 -27.678 -12.781 1.00123.66 O ANISOU 934 O PRO A 143 16926 13798 16263 -722 357 31 O ATOM 935 CB PRO A 143 -22.110 -26.783 -9.721 1.00125.79 C ANISOU 935 CB PRO A 143 17015 14328 16452 -681 246 395 C ATOM 936 CG PRO A 143 -22.795 -26.058 -8.620 1.00125.34 C ANISOU 936 CG PRO A 143 16846 14481 16297 -754 195 498 C ATOM 937 CD PRO A 143 -24.255 -26.084 -8.979 1.00128.03 C ANISOU 937 CD PRO A 143 17191 14891 16564 -970 199 435 C ATOM 938 N PHE A 144 -23.938 -28.432 -11.944 1.00127.99 N ANISOU 938 N PHE A 144 17543 14341 16749 -1040 332 121 N ATOM 939 CA PHE A 144 -23.999 -29.589 -12.830 1.00129.58 C ANISOU 939 CA PHE A 144 17912 14299 17023 -1105 386 17 C ATOM 940 C PHE A 144 -25.001 -29.412 -13.966 1.00131.11 C ANISOU 940 C PHE A 144 18100 14579 17139 -1282 396 -148 C ATOM 941 O PHE A 144 -25.331 -30.391 -14.646 1.00133.35 O ANISOU 941 O PHE A 144 18524 14681 17461 -1392 436 -242 O ATOM 942 CB PHE A 144 -24.324 -30.851 -12.026 1.00128.95 C ANISOU 942 CB PHE A 144 17978 14003 17013 -1196 397 136 C ATOM 943 CG PHE A 144 -23.226 -31.269 -11.090 1.00127.75 C ANISOU 943 CG PHE A 144 17867 13717 16956 -1009 395 290 C ATOM 944 CD1 PHE A 144 -22.136 -31.983 -11.560 1.00128.52 C ANISOU 944 CD1 PHE A 144 18073 13583 17176 -846 442 252 C ATOM 945 CD2 PHE A 144 -23.276 -30.938 -9.746 1.00127.61 C ANISOU 945 CD2 PHE A 144 17771 13817 16901 -990 346 473 C ATOM 946 CE1 PHE A 144 -21.119 -32.367 -10.705 1.00130.21 C ANISOU 946 CE1 PHE A 144 18312 13684 17476 -663 436 402 C ATOM 947 CE2 PHE A 144 -22.262 -31.320 -8.884 1.00128.89 C ANISOU 947 CE2 PHE A 144 17961 13871 17140 -818 337 622 C ATOM 948 CZ PHE A 144 -21.183 -32.037 -9.365 1.00129.98 C ANISOU 948 CZ PHE A 144 18204 13780 17405 -651 380 592 C ATOM 949 N ARG A 145 -25.481 -28.193 -14.194 1.00130.64 N ANISOU 949 N ARG A 145 17881 14788 16969 -1309 359 -187 N ATOM 950 CA ARG A 145 -26.461 -27.931 -15.244 1.00129.77 C ANISOU 950 CA ARG A 145 17742 14793 16770 -1470 358 -328 C ATOM 951 C ARG A 145 -26.101 -26.673 -16.030 1.00127.71 C ANISOU 951 C ARG A 145 17350 14731 16445 -1366 345 -414 C ATOM 952 O ARG A 145 -26.101 -26.675 -17.262 1.00128.39 O ANISOU 952 O ARG A 145 17460 14815 16506 -1391 370 -561 O ATOM 953 CB ARG A 145 -27.866 -27.796 -14.647 1.00129.79 C ANISOU 953 CB ARG A 145 17682 14947 16686 -1671 320 -267 C ATOM 954 N VAL A 149 -24.449 -23.961 -26.501 1.00140.88 N ANISOU 954 N VAL A 149 18916 16962 17649 -1271 527 -1510 N ATOM 955 CA VAL A 149 -25.108 -23.631 -27.760 1.00139.39 C ANISOU 955 CA VAL A 149 18698 16942 17324 -1389 515 -1625 C ATOM 956 C VAL A 149 -26.531 -23.142 -27.499 1.00136.65 C ANISOU 956 C VAL A 149 18258 16778 16885 -1549 435 -1567 C ATOM 957 O VAL A 149 -26.962 -22.128 -28.052 1.00137.34 O ANISOU 957 O VAL A 149 18228 17090 16864 -1567 393 -1559 O ATOM 958 CB VAL A 149 -25.111 -24.837 -28.722 1.00140.30 C ANISOU 958 CB VAL A 149 18968 16909 17432 -1485 576 -1805 C ATOM 959 N THR A 150 -27.257 -23.875 -26.652 1.00127.77 N ANISOU 959 N THR A 150 17184 15557 15806 -1663 417 -1520 N ATOM 960 CA THR A 150 -28.627 -23.497 -26.323 1.00114.94 C ANISOU 960 CA THR A 150 15465 14106 14101 -1817 347 -1463 C ATOM 961 C THR A 150 -28.676 -22.154 -25.597 1.00 99.71 C ANISOU 961 C THR A 150 13374 12357 12155 -1709 294 -1319 C ATOM 962 O THR A 150 -29.526 -21.305 -25.893 1.00 94.89 O ANISOU 962 O THR A 150 12642 11970 11441 -1768 241 -1299 O ATOM 963 CB THR A 150 -29.270 -24.593 -25.473 1.00115.84 C ANISOU 963 CB THR A 150 15670 14067 14277 -1953 347 -1432 C ATOM 964 OG1 THR A 150 -28.545 -24.733 -24.245 1.00112.33 O ANISOU 964 OG1 THR A 150 15250 13476 13954 -1820 361 -1307 O ATOM 965 CG2 THR A 150 -29.233 -25.921 -26.218 1.00120.35 C ANISOU 965 CG2 THR A 150 16415 14441 14871 -2067 401 -1585 C ATOM 966 N SER A 151 -27.775 -21.943 -24.643 1.00 88.70 N ANISOU 966 N SER A 151 11974 10869 10860 -1549 309 -1218 N ATOM 967 CA SER A 151 -27.718 -20.678 -23.931 1.00 81.98 C ANISOU 967 CA SER A 151 10981 10169 9998 -1443 265 -1094 C ATOM 968 C SER A 151 -26.781 -19.674 -24.596 1.00 74.02 C ANISOU 968 C SER A 151 9911 9243 8971 -1290 277 -1108 C ATOM 969 O SER A 151 -26.865 -18.478 -24.299 1.00 73.74 O ANISOU 969 O SER A 151 9753 9361 8904 -1223 239 -1029 O ATOM 970 CB SER A 151 -27.294 -20.924 -22.478 1.00 88.08 C ANISOU 970 CB SER A 151 11770 10821 10874 -1365 267 -972 C ATOM 971 OG SER A 151 -27.240 -19.719 -21.736 1.00 94.01 O ANISOU 971 OG SER A 151 12391 11715 11615 -1269 227 -864 O ATOM 972 N ILE A 152 -25.924 -20.122 -25.520 1.00 66.99 N ANISOU 972 N ILE A 152 9101 8258 8094 -1241 334 -1212 N ATOM 973 CA ILE A 152 -25.059 -19.199 -26.254 1.00 64.94 C ANISOU 973 CA ILE A 152 8782 8090 7804 -1115 350 -1229 C ATOM 974 C ILE A 152 -25.878 -18.294 -27.176 1.00 67.82 C ANISOU 974 C ILE A 152 9053 8682 8034 -1190 308 -1253 C ATOM 975 O ILE A 152 -25.675 -17.069 -27.209 1.00 66.76 O ANISOU 975 O ILE A 152 8812 8684 7869 -1104 282 -1185 O ATOM 976 CB ILE A 152 -23.973 -19.990 -27.013 1.00 60.55 C ANISOU 976 CB ILE A 152 8334 7382 7291 -1048 429 -1341 C ATOM 977 CG1 ILE A 152 -23.040 -20.670 -26.010 1.00 67.45 C ANISOU 977 CG1 ILE A 152 9274 8049 8305 -932 465 -1287 C ATOM 978 CG2 ILE A 152 -23.188 -19.108 -27.962 1.00 50.43 C ANISOU 978 CG2 ILE A 152 6991 6215 5954 -950 452 -1375 C ATOM 979 CD1 ILE A 152 -22.082 -21.640 -26.619 1.00 70.15 C ANISOU 979 CD1 ILE A 152 9733 8214 8706 -866 545 -1396 C ATOM 980 N ARG A 153 -26.820 -18.875 -27.932 1.00 69.07 N ANISOU 980 N ARG A 153 9250 8884 8110 -1353 297 -1346 N ATOM 981 CA ARG A 153 -27.690 -18.067 -28.786 1.00 66.26 C ANISOU 981 CA ARG A 153 8798 8758 7618 -1430 248 -1358 C ATOM 982 C ARG A 153 -28.553 -17.128 -27.955 1.00 60.34 C ANISOU 982 C ARG A 153 7920 8156 6852 -1432 178 -1230 C ATOM 983 O ARG A 153 -28.821 -15.992 -28.362 1.00 59.10 O ANISOU 983 O ARG A 153 7655 8179 6623 -1396 140 -1184 O ATOM 984 CB ARG A 153 -28.567 -18.965 -29.660 1.00 66.89 C ANISOU 984 CB ARG A 153 8942 8861 7611 -1619 245 -1484 C ATOM 985 N SER A 154 -28.990 -17.580 -26.783 1.00 57.19 N ANISOU 985 N SER A 154 7530 7681 6518 -1472 164 -1168 N ATOM 986 CA SER A 154 -29.715 -16.691 -25.886 1.00 59.01 C ANISOU 986 CA SER A 154 7638 8044 6740 -1456 108 -1050 C ATOM 987 C SER A 154 -28.830 -15.539 -25.419 1.00 54.87 C ANISOU 987 C SER A 154 7046 7539 6263 -1274 109 -962 C ATOM 988 O SER A 154 -29.300 -14.402 -25.275 1.00 50.63 O ANISOU 988 O SER A 154 6394 7158 5684 -1235 65 -892 O ATOM 989 CB SER A 154 -30.256 -17.483 -24.700 1.00 61.58 C ANISOU 989 CB SER A 154 7996 8279 7124 -1536 103 -1003 C ATOM 990 OG SER A 154 -31.206 -18.437 -25.145 1.00 65.36 O ANISOU 990 OG SER A 154 8524 8760 7550 -1726 97 -1079 O ATOM 991 N ALA A 155 -27.543 -15.812 -25.183 1.00 50.45 N ANISOU 991 N ALA A 155 6555 6822 5792 -1160 158 -966 N ATOM 992 CA ALA A 155 -26.636 -14.748 -24.764 1.00 45.92 C ANISOU 992 CA ALA A 155 5918 6267 5262 -1001 159 -890 C ATOM 993 C ALA A 155 -26.480 -13.704 -25.862 1.00 50.45 C ANISOU 993 C ALA A 155 6428 6980 5759 -958 151 -906 C ATOM 994 O ALA A 155 -26.481 -12.498 -25.589 1.00 51.15 O ANISOU 994 O ALA A 155 6425 7169 5841 -883 121 -829 O ATOM 995 CB ALA A 155 -25.283 -15.337 -24.375 1.00 38.86 C ANISOU 995 CB ALA A 155 5104 5190 4472 -895 213 -896 C ATOM 996 N TRP A 156 -26.369 -14.155 -27.115 1.00 50.37 N ANISOU 996 N TRP A 156 6472 6979 5688 -1010 178 -1006 N ATOM 997 CA TRP A 156 -26.334 -13.221 -28.238 1.00 49.55 C ANISOU 997 CA TRP A 156 6310 7025 5493 -989 168 -1016 C ATOM 998 C TRP A 156 -27.635 -12.432 -28.381 1.00 52.37 C ANISOU 998 C TRP A 156 6565 7573 5761 -1054 98 -964 C ATOM 999 O TRP A 156 -27.604 -11.225 -28.659 1.00 50.18 O ANISOU 999 O TRP A 156 6206 7411 5448 -984 73 -899 O ATOM 1000 CB TRP A 156 -26.021 -13.945 -29.544 1.00 47.18 C ANISOU 1000 CB TRP A 156 6089 6708 5130 -1045 212 -1143 C ATOM 1001 CG TRP A 156 -24.620 -14.380 -29.646 1.00 52.94 C ANISOU 1001 CG TRP A 156 6891 7292 5933 -945 285 -1188 C ATOM 1002 CD1 TRP A 156 -24.117 -15.638 -29.455 1.00 57.55 C ANISOU 1002 CD1 TRP A 156 7585 7692 6588 -950 339 -1265 C ATOM 1003 CD2 TRP A 156 -23.502 -13.533 -29.902 1.00 51.94 C ANISOU 1003 CD2 TRP A 156 6724 7188 5823 -815 314 -1153 C ATOM 1004 NE1 TRP A 156 -22.752 -15.627 -29.626 1.00 56.08 N ANISOU 1004 NE1 TRP A 156 7423 7426 6458 -822 400 -1283 N ATOM 1005 CE2 TRP A 156 -22.351 -14.344 -29.895 1.00 53.63 C ANISOU 1005 CE2 TRP A 156 7018 7246 6113 -745 386 -1215 C ATOM 1006 CE3 TRP A 156 -23.365 -12.168 -30.165 1.00 53.19 C ANISOU 1006 CE3 TRP A 156 6788 7482 5940 -755 288 -1073 C ATOM 1007 CZ2 TRP A 156 -21.080 -13.831 -30.134 1.00 55.38 C ANISOU 1007 CZ2 TRP A 156 7214 7462 6365 -622 432 -1202 C ATOM 1008 CZ3 TRP A 156 -22.101 -11.661 -30.401 1.00 53.89 C ANISOU 1008 CZ3 TRP A 156 6864 7552 6061 -644 334 -1059 C ATOM 1009 CH2 TRP A 156 -20.975 -12.490 -30.381 1.00 53.89 C ANISOU 1009 CH2 TRP A 156 6932 7414 6131 -581 405 -1124 C ATOM 1010 N ILE A 157 -28.784 -13.100 -28.254 1.00 47.04 N ANISOU 1010 N ILE A 157 5892 6935 5046 -1189 68 -991 N ATOM 1011 CA ILE A 157 -30.059 -12.392 -28.320 1.00 48.88 C ANISOU 1011 CA ILE A 157 6014 7361 5197 -1245 1 -938 C ATOM 1012 C ILE A 157 -30.118 -11.295 -27.265 1.00 48.68 C ANISOU 1012 C ILE A 157 5897 7372 5227 -1134 -27 -818 C ATOM 1013 O ILE A 157 -30.479 -10.146 -27.555 1.00 47.17 O ANISOU 1013 O ILE A 157 5612 7320 4989 -1081 -64 -757 O ATOM 1014 CB ILE A 157 -31.229 -13.380 -28.184 1.00 56.31 C ANISOU 1014 CB ILE A 157 6968 8328 6099 -1415 -23 -984 C ATOM 1015 CG1 ILE A 157 -31.301 -14.272 -29.426 1.00 59.97 C ANISOU 1015 CG1 ILE A 157 7512 8793 6483 -1537 -4 -1113 C ATOM 1016 CG2 ILE A 157 -32.550 -12.644 -27.923 1.00 57.49 C ANISOU 1016 CG2 ILE A 157 6982 8676 6185 -1455 -91 -910 C ATOM 1017 CD1 ILE A 157 -32.246 -15.438 -29.269 1.00 64.07 C ANISOU 1017 CD1 ILE A 157 8074 9289 6982 -1718 -14 -1177 C ATOM 1018 N LEU A 158 -29.751 -11.628 -26.027 1.00 47.23 N ANISOU 1018 N LEU A 158 5743 7060 5144 -1095 -8 -783 N ATOM 1019 CA LEU A 158 -29.761 -10.622 -24.972 1.00 47.58 C ANISOU 1019 CA LEU A 158 5707 7134 5237 -994 -29 -684 C ATOM 1020 C LEU A 158 -28.801 -9.480 -25.287 1.00 53.38 C ANISOU 1020 C LEU A 158 6416 7874 5992 -857 -19 -647 C ATOM 1021 O LEU A 158 -29.145 -8.301 -25.102 1.00 56.49 O ANISOU 1021 O LEU A 158 6723 8368 6374 -793 -51 -578 O ATOM 1022 CB LEU A 158 -29.430 -11.268 -23.628 1.00 42.75 C ANISOU 1022 CB LEU A 158 5140 6386 4718 -982 -9 -658 C ATOM 1023 CG LEU A 158 -29.405 -10.331 -22.426 1.00 45.20 C ANISOU 1023 CG LEU A 158 5376 6723 5076 -887 -26 -568 C ATOM 1024 CD1 LEU A 158 -30.765 -9.663 -22.214 1.00 53.82 C ANISOU 1024 CD1 LEU A 158 6357 7987 6105 -924 -74 -527 C ATOM 1025 CD2 LEU A 158 -29.037 -11.129 -21.187 1.00 44.78 C ANISOU 1025 CD2 LEU A 158 5376 6539 5098 -889 -6 -544 C ATOM 1026 N CYS A 159 -27.588 -9.800 -25.750 1.00 50.08 N ANISOU 1026 N CYS A 159 6073 7349 5608 -810 29 -690 N ATOM 1027 CA CYS A 159 -26.666 -8.725 -26.087 1.00 48.83 C ANISOU 1027 CA CYS A 159 5886 7203 5464 -696 42 -653 C ATOM 1028 C CYS A 159 -27.274 -7.808 -27.131 1.00 46.67 C ANISOU 1028 C CYS A 159 5549 7089 5095 -706 8 -631 C ATOM 1029 O CYS A 159 -27.198 -6.579 -27.004 1.00 47.34 O ANISOU 1029 O CYS A 159 5571 7227 5188 -624 -11 -557 O ATOM 1030 CB CYS A 159 -25.320 -9.286 -26.555 1.00 51.21 C ANISOU 1030 CB CYS A 159 6268 7387 5804 -655 103 -710 C ATOM 1031 SG CYS A 159 -24.362 -10.082 -25.211 1.00 52.29 S ANISOU 1031 SG CYS A 159 6461 7337 6069 -595 138 -701 S ATOM 1032 N GLY A 160 -27.890 -8.388 -28.160 1.00 50.20 N ANISOU 1032 N GLY A 160 6014 7611 5448 -808 0 -694 N ATOM 1033 CA GLY A 160 -28.508 -7.573 -29.192 1.00 52.37 C ANISOU 1033 CA GLY A 160 6225 8054 5620 -821 -38 -665 C ATOM 1034 C GLY A 160 -29.591 -6.674 -28.633 1.00 51.93 C ANISOU 1034 C GLY A 160 6065 8112 5553 -798 -98 -577 C ATOM 1035 O GLY A 160 -29.712 -5.510 -29.034 1.00 48.29 O ANISOU 1035 O GLY A 160 5543 7743 5063 -730 -124 -506 O ATOM 1036 N ILE A 161 -30.382 -7.197 -27.687 1.00 49.55 N ANISOU 1036 N ILE A 161 5744 7804 5279 -851 -116 -579 N ATOM 1037 CA ILE A 161 -31.398 -6.376 -27.032 1.00 49.47 C ANISOU 1037 CA ILE A 161 5628 7902 5266 -820 -164 -501 C ATOM 1038 C ILE A 161 -30.745 -5.165 -26.376 1.00 49.49 C ANISOU 1038 C ILE A 161 5603 7854 5345 -675 -157 -426 C ATOM 1039 O ILE A 161 -31.215 -4.026 -26.503 1.00 48.46 O ANISOU 1039 O ILE A 161 5397 7818 5196 -607 -190 -357 O ATOM 1040 CB ILE A 161 -32.183 -7.196 -25.993 1.00 51.18 C ANISOU 1040 CB ILE A 161 5833 8107 5506 -900 -172 -516 C ATOM 1041 CG1 ILE A 161 -32.853 -8.422 -26.614 1.00 58.19 C ANISOU 1041 CG1 ILE A 161 6754 9034 6321 -1062 -179 -595 C ATOM 1042 CG2 ILE A 161 -33.225 -6.307 -25.323 1.00 45.85 C ANISOU 1042 CG2 ILE A 161 5039 7558 4824 -857 -214 -442 C ATOM 1043 CD1 ILE A 161 -33.861 -8.090 -27.648 1.00 65.56 C ANISOU 1043 CD1 ILE A 161 7608 10164 7137 -1121 -230 -593 C ATOM 1044 N ILE A 162 -29.666 -5.407 -25.633 1.00 43.99 N ANISOU 1044 N ILE A 162 4970 7005 4740 -628 -114 -438 N ATOM 1045 CA ILE A 162 -29.039 -4.324 -24.886 1.00 42.97 C ANISOU 1045 CA ILE A 162 4817 6824 4685 -508 -108 -378 C ATOM 1046 C ILE A 162 -28.505 -3.263 -25.840 1.00 45.47 C ANISOU 1046 C ILE A 162 5125 7172 4982 -439 -107 -340 C ATOM 1047 O ILE A 162 -28.716 -2.049 -25.642 1.00 39.59 O ANISOU 1047 O ILE A 162 4326 6465 4254 -360 -128 -272 O ATOM 1048 CB ILE A 162 -27.942 -4.872 -23.958 1.00 42.05 C ANISOU 1048 CB ILE A 162 4764 6553 4659 -480 -66 -399 C ATOM 1049 CG1 ILE A 162 -28.558 -5.722 -22.830 1.00 41.84 C ANISOU 1049 CG1 ILE A 162 4739 6503 4656 -537 -72 -408 C ATOM 1050 CG2 ILE A 162 -27.080 -3.755 -23.423 1.00 38.14 C ANISOU 1050 CG2 ILE A 162 4254 6007 4231 -369 -57 -350 C ATOM 1051 CD1 ILE A 162 -27.530 -6.479 -21.990 1.00 37.84 C ANISOU 1051 CD1 ILE A 162 4302 5848 4228 -519 -36 -424 C ATOM 1052 N TRP A 163 -27.818 -3.711 -26.899 1.00 44.01 N ANISOU 1052 N TRP A 163 4996 6969 4759 -471 -79 -383 N ATOM 1053 CA TRP A 163 -27.301 -2.775 -27.892 1.00 42.70 C ANISOU 1053 CA TRP A 163 4822 6842 4559 -421 -75 -342 C ATOM 1054 C TRP A 163 -28.417 -1.935 -28.489 1.00 41.59 C ANISOU 1054 C TRP A 163 4607 6851 4343 -415 -129 -278 C ATOM 1055 O TRP A 163 -28.311 -0.705 -28.551 1.00 37.73 O ANISOU 1055 O TRP A 163 4086 6376 3873 -332 -141 -199 O ATOM 1056 CB TRP A 163 -26.543 -3.479 -29.021 1.00 41.79 C ANISOU 1056 CB TRP A 163 4772 6716 4392 -469 -34 -407 C ATOM 1057 CG TRP A 163 -25.174 -4.035 -28.729 1.00 45.64 C ANISOU 1057 CG TRP A 163 5325 7064 4952 -441 27 -456 C ATOM 1058 CD1 TRP A 163 -24.830 -5.344 -28.530 1.00 49.23 C ANISOU 1058 CD1 TRP A 163 5844 7432 5431 -487 62 -540 C ATOM 1059 CD2 TRP A 163 -23.963 -3.284 -28.613 1.00 50.41 C ANISOU 1059 CD2 TRP A 163 5933 7605 5616 -359 60 -419 C ATOM 1060 NE1 TRP A 163 -23.468 -5.457 -28.329 1.00 46.58 N ANISOU 1060 NE1 TRP A 163 5545 6989 5164 -426 114 -555 N ATOM 1061 CE2 TRP A 163 -22.915 -4.206 -28.366 1.00 50.54 C ANISOU 1061 CE2 TRP A 163 6006 7512 5687 -353 113 -483 C ATOM 1062 CE3 TRP A 163 -23.656 -1.922 -28.707 1.00 55.98 C ANISOU 1062 CE3 TRP A 163 6600 8332 6337 -293 50 -336 C ATOM 1063 CZ2 TRP A 163 -21.586 -3.804 -28.198 1.00 53.62 C ANISOU 1063 CZ2 TRP A 163 6400 7833 6138 -285 154 -468 C ATOM 1064 CZ3 TRP A 163 -22.331 -1.525 -28.539 1.00 58.84 C ANISOU 1064 CZ3 TRP A 163 6978 8617 6763 -239 93 -323 C ATOM 1065 CH2 TRP A 163 -21.317 -2.463 -28.287 1.00 56.82 C ANISOU 1065 CH2 TRP A 163 6764 8273 6553 -237 143 -389 C ATOM 1066 N ILE A 164 -29.482 -2.585 -28.969 1.00 42.09 N ANISOU 1066 N ILE A 164 4644 7027 4320 -505 -162 -309 N ATOM 1067 CA ILE A 164 -30.582 -1.834 -29.574 1.00 46.75 C ANISOU 1067 CA ILE A 164 5151 7781 4831 -496 -219 -243 C ATOM 1068 C ILE A 164 -31.119 -0.798 -28.590 1.00 45.58 C ANISOU 1068 C ILE A 164 4932 7636 4749 -398 -245 -165 C ATOM 1069 O ILE A 164 -31.308 0.378 -28.938 1.00 42.07 O ANISOU 1069 O ILE A 164 4445 7243 4298 -315 -269 -79 O ATOM 1070 CB ILE A 164 -31.708 -2.779 -30.037 1.00 56.04 C ANISOU 1070 CB ILE A 164 6298 9087 5909 -620 -254 -295 C ATOM 1071 CG1 ILE A 164 -31.213 -3.808 -31.062 1.00 59.03 C ANISOU 1071 CG1 ILE A 164 6754 9460 6215 -722 -225 -388 C ATOM 1072 CG2 ILE A 164 -32.876 -1.957 -30.618 1.00 58.26 C ANISOU 1072 CG2 ILE A 164 6474 9557 6107 -600 -320 -215 C ATOM 1073 CD1 ILE A 164 -30.686 -3.197 -32.329 1.00 62.85 C ANISOU 1073 CD1 ILE A 164 7250 10007 6625 -695 -221 -358 C ATOM 1074 N LEU A 165 -31.394 -1.216 -27.347 1.00 37.26 N ANISOU 1074 N LEU A 165 3869 6530 3759 -405 -238 -192 N ATOM 1075 CA LEU A 165 -32.071 -0.288 -26.449 1.00 39.74 C ANISOU 1075 CA LEU A 165 4107 6873 4119 -319 -262 -131 C ATOM 1076 C LEU A 165 -31.200 0.926 -26.156 1.00 39.83 C ANISOU 1076 C LEU A 165 4140 6783 4211 -199 -242 -78 C ATOM 1077 O LEU A 165 -31.680 2.067 -26.202 1.00 38.03 O ANISOU 1077 O LEU A 165 3858 6601 3992 -111 -267 -6 O ATOM 1078 CB LEU A 165 -32.510 -0.976 -25.154 1.00 39.50 C ANISOU 1078 CB LEU A 165 4061 6816 4130 -356 -254 -170 C ATOM 1079 CG LEU A 165 -33.646 -1.980 -25.376 1.00 41.84 C ANISOU 1079 CG LEU A 165 4315 7236 4347 -478 -282 -207 C ATOM 1080 CD1 LEU A 165 -34.032 -2.714 -24.079 1.00 35.94 C ANISOU 1080 CD1 LEU A 165 3559 6458 3639 -527 -268 -238 C ATOM 1081 CD2 LEU A 165 -34.840 -1.291 -26.000 1.00 37.21 C ANISOU 1081 CD2 LEU A 165 3620 6833 3686 -456 -336 -151 C ATOM 1082 N ILE A 166 -29.911 0.706 -25.904 1.00 34.32 N ANISOU 1082 N ILE A 166 3520 5947 3573 -195 -197 -110 N ATOM 1083 CA ILE A 166 -29.036 1.819 -25.564 1.00 34.29 C ANISOU 1083 CA ILE A 166 3537 5845 3647 -99 -177 -67 C ATOM 1084 C ILE A 166 -28.750 2.695 -26.779 1.00 41.69 C ANISOU 1084 C ILE A 166 4480 6814 4547 -65 -183 -3 C ATOM 1085 O ILE A 166 -28.686 3.926 -26.667 1.00 43.39 O ANISOU 1085 O ILE A 166 4681 6999 4805 22 -190 64 O ATOM 1086 CB ILE A 166 -27.754 1.273 -24.925 1.00 41.51 C ANISOU 1086 CB ILE A 166 4518 6624 4629 -112 -130 -119 C ATOM 1087 CG1 ILE A 166 -28.131 0.598 -23.598 1.00 46.77 C ANISOU 1087 CG1 ILE A 166 5172 7264 5333 -132 -130 -159 C ATOM 1088 CG2 ILE A 166 -26.717 2.377 -24.748 1.00 39.01 C ANISOU 1088 CG2 ILE A 166 4225 6215 4383 -36 -108 -80 C ATOM 1089 CD1 ILE A 166 -27.044 -0.254 -23.012 1.00 47.59 C ANISOU 1089 CD1 ILE A 166 5337 7256 5488 -157 -92 -208 C ATOM 1090 N MET A 167 -28.601 2.095 -27.963 1.00 38.83 N ANISOU 1090 N MET A 167 4142 6513 4101 -133 -181 -21 N ATOM 1091 CA MET A 167 -28.342 2.894 -29.155 1.00 43.33 C ANISOU 1091 CA MET A 167 4716 7128 4619 -108 -187 49 C ATOM 1092 C MET A 167 -29.556 3.739 -29.530 1.00 45.44 C ANISOU 1092 C MET A 167 4910 7516 4840 -58 -244 136 C ATOM 1093 O MET A 167 -29.405 4.906 -29.913 1.00 39.24 O ANISOU 1093 O MET A 167 4121 6718 4069 16 -252 227 O ATOM 1094 CB MET A 167 -27.912 1.993 -30.315 1.00 43.83 C ANISOU 1094 CB MET A 167 4821 7242 4590 -197 -167 -2 C ATOM 1095 CG MET A 167 -26.515 1.373 -30.148 1.00 49.65 C ANISOU 1095 CG MET A 167 5631 7858 5378 -218 -103 -71 C ATOM 1096 SD MET A 167 -26.034 0.226 -31.478 1.00 62.12 S ANISOU 1096 SD MET A 167 7261 9492 6849 -316 -68 -154 S ATOM 1097 CE MET A 167 -25.804 1.333 -32.875 1.00 63.90 C ANISOU 1097 CE MET A 167 7476 9815 6988 -294 -75 -57 C ATOM 1098 N ALA A 168 -30.766 3.182 -29.405 1.00 43.56 N ANISOU 1098 N ALA A 168 4609 7393 4549 -97 -283 114 N ATOM 1099 CA ALA A 168 -31.971 3.967 -29.647 1.00 44.49 C ANISOU 1099 CA ALA A 168 4639 7637 4629 -36 -339 198 C ATOM 1100 C ALA A 168 -32.154 5.057 -28.593 1.00 47.27 C ANISOU 1100 C ALA A 168 4964 7910 5088 86 -339 246 C ATOM 1101 O ALA A 168 -32.603 6.167 -28.902 1.00 46.90 O ANISOU 1101 O ALA A 168 4878 7896 5045 181 -367 341 O ATOM 1102 CB ALA A 168 -33.191 3.052 -29.676 1.00 40.78 C ANISOU 1102 CB ALA A 168 4099 7318 4079 -118 -378 155 C ATOM 1103 N SER A 169 -31.823 4.760 -27.338 1.00 46.16 N ANISOU 1103 N SER A 169 4844 7664 5031 88 -306 182 N ATOM 1104 CA SER A 169 -31.976 5.767 -26.296 1.00 47.92 C ANISOU 1104 CA SER A 169 5045 7813 5349 198 -300 210 C ATOM 1105 C SER A 169 -30.988 6.913 -26.447 1.00 54.91 C ANISOU 1105 C SER A 169 5992 8569 6305 273 -277 264 C ATOM 1106 O SER A 169 -31.214 7.987 -25.878 1.00 57.01 O ANISOU 1106 O SER A 169 6243 8779 6640 375 -278 304 O ATOM 1107 CB SER A 169 -31.784 5.126 -24.927 1.00 48.04 C ANISOU 1107 CB SER A 169 5072 7758 5423 170 -271 126 C ATOM 1108 OG SER A 169 -32.746 4.120 -24.715 1.00 47.65 O ANISOU 1108 OG SER A 169 4966 7823 5314 96 -290 84 O ATOM 1109 N SER A 170 -29.901 6.708 -27.193 1.00 55.34 N ANISOU 1109 N SER A 170 6114 8571 6341 221 -251 263 N ATOM 1110 CA SER A 170 -28.809 7.666 -27.283 1.00 50.72 C ANISOU 1110 CA SER A 170 5591 7857 5824 265 -221 305 C ATOM 1111 C SER A 170 -28.789 8.458 -28.589 1.00 54.33 C ANISOU 1111 C SER A 170 6056 8357 6230 291 -239 411 C ATOM 1112 O SER A 170 -27.920 9.324 -28.746 1.00 51.01 O ANISOU 1112 O SER A 170 5687 7831 5863 320 -214 460 O ATOM 1113 CB SER A 170 -27.469 6.943 -27.125 1.00 49.57 C ANISOU 1113 CB SER A 170 5510 7624 5702 193 -173 234 C ATOM 1114 OG SER A 170 -27.339 6.331 -25.854 1.00 50.84 O ANISOU 1114 OG SER A 170 5671 7729 5918 179 -157 153 O ATOM 1115 N ILE A 171 -29.704 8.184 -29.530 1.00 52.69 N ANISOU 1115 N ILE A 171 5798 8305 5917 272 -282 452 N ATOM 1116 CA ILE A 171 -29.606 8.796 -30.859 1.00 55.70 C ANISOU 1116 CA ILE A 171 6191 8745 6229 282 -299 557 C ATOM 1117 C ILE A 171 -29.785 10.301 -30.823 1.00 58.16 C ANISOU 1117 C ILE A 171 6504 8987 6608 401 -313 674 C ATOM 1118 O ILE A 171 -29.395 10.990 -31.771 1.00 57.50 O ANISOU 1118 O ILE A 171 6452 8900 6496 413 -314 773 O ATOM 1119 CB ILE A 171 -30.624 8.202 -31.848 1.00 59.67 C ANISOU 1119 CB ILE A 171 6629 9449 6593 236 -350 577 C ATOM 1120 CG1 ILE A 171 -32.046 8.387 -31.331 1.00 67.08 C ANISOU 1120 CG1 ILE A 171 7473 10480 7534 301 -401 598 C ATOM 1121 CG2 ILE A 171 -30.283 6.768 -32.204 1.00 58.69 C ANISOU 1121 CG2 ILE A 171 6527 9381 6390 105 -330 466 C ATOM 1122 CD1 ILE A 171 -33.076 8.029 -32.352 1.00 76.45 C ANISOU 1122 CD1 ILE A 171 8585 11879 8583 265 -461 640 C ATOM 1123 N AMET A 172 -30.351 10.832 -29.742 0.38 61.77 N ANISOU 1123 N AMET A 172 6932 9383 7156 489 -319 665 N ATOM 1124 N CMET A 172 -30.382 10.826 -29.751 0.62 61.88 N ANISOU 1124 N CMET A 172 6943 9401 7168 490 -321 665 N ATOM 1125 CA AMET A 172 -30.548 12.266 -29.638 0.38 64.04 C ANISOU 1125 CA AMET A 172 7229 9583 7520 612 -328 765 C ATOM 1126 CA CMET A 172 -30.576 12.260 -29.607 0.62 63.99 C ANISOU 1126 CA CMET A 172 7221 9578 7516 614 -328 764 C ATOM 1127 C AMET A 172 -29.231 13.020 -29.811 0.38 62.39 C ANISOU 1127 C AMET A 172 7116 9211 7377 602 -284 803 C ATOM 1128 C CMET A 172 -29.256 13.038 -29.751 0.62 62.57 C ANISOU 1128 C CMET A 172 7138 9231 7405 606 -284 800 C ATOM 1129 O AMET A 172 -29.212 14.131 -30.321 0.38 62.25 O ANISOU 1129 O AMET A 172 7126 9139 7387 669 -292 918 O ATOM 1130 O CMET A 172 -29.248 14.159 -30.237 0.62 62.06 O ANISOU 1130 O CMET A 172 7101 9109 7369 675 -292 915 O ATOM 1131 CB AMET A 172 -31.200 12.616 -28.304 0.38 67.13 C ANISOU 1131 CB AMET A 172 7583 9918 8004 700 -326 716 C ATOM 1132 CB CMET A 172 -31.261 12.549 -28.274 0.62 66.99 C ANISOU 1132 CB CMET A 172 7561 9910 7983 698 -327 711 C ATOM 1133 CG AMET A 172 -31.209 14.097 -27.986 0.38 71.79 C ANISOU 1133 CG AMET A 172 8207 10369 8702 827 -318 791 C ATOM 1134 CG CMET A 172 -31.263 14.002 -27.855 0.62 71.82 C ANISOU 1134 CG CMET A 172 8204 10377 8706 825 -317 776 C ATOM 1135 SD AMET A 172 -32.524 14.551 -26.845 0.38 71.69 S ANISOU 1135 SD AMET A 172 8112 10374 8751 963 -333 762 S ATOM 1136 SD CMET A 172 -30.229 14.262 -26.405 0.62 78.07 S ANISOU 1136 SD CMET A 172 9069 10965 9628 814 -257 665 S ATOM 1137 CE AMET A 172 -33.066 16.120 -27.511 0.38 73.61 C ANISOU 1137 CE AMET A 172 8361 10564 9042 1124 -360 923 C ATOM 1138 CE CMET A 172 -30.465 16.014 -26.130 0.62 78.92 C ANISOU 1138 CE CMET A 172 9216 10916 9854 967 -252 746 C ATOM 1139 N LEU A 173 -28.148 12.426 -29.299 1.00 59.28 N ANISOU 1139 N LEU A 173 6770 8737 7016 520 -237 705 N ATOM 1140 CA LEU A 173 -26.818 13.017 -29.375 1.00 61.15 C ANISOU 1140 CA LEU A 173 7086 8835 7314 491 -192 724 C ATOM 1141 C LEU A 173 -26.387 13.190 -30.817 1.00 64.39 C ANISOU 1141 C LEU A 173 7522 9304 7640 447 -192 822 C ATOM 1142 O LEU A 173 -25.687 14.148 -31.158 1.00 66.06 O ANISOU 1142 O LEU A 173 7789 9417 7895 456 -170 902 O ATOM 1143 CB LEU A 173 -25.837 12.095 -28.647 1.00 53.83 C ANISOU 1143 CB LEU A 173 6180 7859 6413 407 -149 598 C ATOM 1144 CG LEU A 173 -26.070 11.860 -27.149 1.00 51.54 C ANISOU 1144 CG LEU A 173 5873 7511 6200 434 -144 499 C ATOM 1145 CD1 LEU A 173 -25.204 10.731 -26.652 1.00 49.19 C ANISOU 1145 CD1 LEU A 173 5586 7203 5899 347 -112 393 C ATOM 1146 CD2 LEU A 173 -25.773 13.114 -26.354 1.00 55.94 C ANISOU 1146 CD2 LEU A 173 6467 7913 6873 500 -128 515 C ATOM 1147 N LEU A 174 -26.788 12.260 -31.679 1.00 69.84 N ANISOU 1147 N LEU A 174 8173 10158 8204 391 -213 813 N ATOM 1148 CA LEU A 174 -26.486 12.394 -33.091 1.00 78.32 C ANISOU 1148 CA LEU A 174 9265 11317 9177 348 -215 904 C ATOM 1149 C LEU A 174 -27.218 13.569 -33.722 1.00101.72 C ANISOU 1149 C LEU A 174 12219 14301 12129 439 -259 1064 C ATOM 1150 O LEU A 174 -26.784 14.054 -34.772 1.00105.28 O ANISOU 1150 O LEU A 174 12702 14776 12523 417 -254 1170 O ATOM 1151 CB LEU A 174 -26.838 11.103 -33.823 1.00 64.46 C ANISOU 1151 CB LEU A 174 7471 9738 7282 265 -230 842 C ATOM 1152 CG LEU A 174 -25.989 9.908 -33.404 1.00 57.17 C ANISOU 1152 CG LEU A 174 6571 8787 6365 175 -181 697 C ATOM 1153 CD1 LEU A 174 -26.483 8.655 -34.077 1.00 57.35 C ANISOU 1153 CD1 LEU A 174 6563 8969 6259 97 -197 628 C ATOM 1154 CD2 LEU A 174 -24.521 10.166 -33.736 1.00 54.48 C ANISOU 1154 CD2 LEU A 174 6290 8361 6047 131 -119 705 C ATOM 1155 N ASP A 175 -28.316 14.046 -33.119 1.00120.25 N ANISOU 1155 N ASP A 175 14520 16643 14527 545 -300 1090 N ATOM 1156 CA ASP A 175 -29.036 15.134 -33.774 1.00127.28 C ANISOU 1156 CA ASP A 175 15397 17557 15406 645 -344 1252 C ATOM 1157 C ASP A 175 -28.290 16.454 -33.639 1.00136.34 C ANISOU 1157 C ASP A 175 16630 18506 16669 695 -312 1341 C ATOM 1158 O ASP A 175 -28.360 17.297 -34.543 1.00142.33 O ANISOU 1158 O ASP A 175 17412 19267 17399 734 -331 1495 O ATOM 1159 CB ASP A 175 -30.457 15.259 -33.222 1.00127.49 C ANISOU 1159 CB ASP A 175 15339 17650 15452 755 -396 1257 C ATOM 1160 CG ASP A 175 -31.519 14.980 -34.273 1.00130.04 C ANISOU 1160 CG ASP A 175 15577 18197 15634 766 -463 1341 C ATOM 1161 N SER A 176 -27.556 16.642 -32.542 1.00130.10 N ANISOU 1161 N SER A 176 15888 17543 16001 686 -264 1249 N ATOM 1162 CA SER A 176 -26.774 17.860 -32.335 1.00119.51 C ANISOU 1162 CA SER A 176 14634 16000 14774 712 -229 1313 C ATOM 1163 C SER A 176 -25.586 17.605 -31.414 1.00109.04 C ANISOU 1163 C SER A 176 13354 14548 13529 631 -171 1186 C ATOM 1164 O SER A 176 -24.987 18.541 -30.884 1.00105.43 O ANISOU 1164 O SER A 176 12962 13911 13185 646 -141 1197 O ATOM 1165 CB SER A 176 -27.654 18.974 -31.760 1.00117.22 C ANISOU 1165 CB SER A 176 14346 15603 14588 863 -253 1374 C ATOM 1166 N GLU A 179 -17.909 21.961 -32.719 1.00142.87 N ANISOU 1166 N GLU A 179 18064 18099 18122 109 127 1478 N ATOM 1167 CA GLU A 179 -18.266 22.494 -34.021 1.00141.94 C ANISOU 1167 CA GLU A 179 17973 18027 17929 125 113 1662 C ATOM 1168 C GLU A 179 -19.241 23.668 -33.871 1.00142.36 C ANISOU 1168 C GLU A 179 18087 17930 18071 249 75 1770 C ATOM 1169 O GLU A 179 -19.481 24.427 -34.809 1.00144.96 O ANISOU 1169 O GLU A 179 18461 18242 18375 272 63 1947 O ATOM 1170 CB GLU A 179 -18.844 21.386 -34.913 1.00141.81 C ANISOU 1170 CB GLU A 179 17882 18248 17750 138 86 1667 C ATOM 1171 CG GLU A 179 -19.190 21.840 -36.322 1.00148.27 C ANISOU 1171 CG GLU A 179 18719 19152 18465 145 68 1857 C ATOM 1172 CD GLU A 179 -17.979 22.271 -37.142 1.00153.81 C ANISOU 1172 CD GLU A 179 19461 19847 19131 18 124 1952 C ATOM 1173 OE1 GLU A 179 -16.862 21.757 -36.905 1.00154.27 O ANISOU 1173 OE1 GLU A 179 19499 19926 19190 -88 179 1849 O ATOM 1174 OE2 GLU A 179 -18.151 23.168 -38.010 1.00157.37 O ANISOU 1174 OE2 GLU A 179 19963 20273 19558 28 115 2138 O ATOM 1175 N GLN A 180 -19.772 23.825 -32.660 1.00140.00 N ANISOU 1175 N GLN A 180 17791 17523 17879 333 59 1664 N ATOM 1176 CA GLN A 180 -20.747 24.880 -32.407 1.00140.15 C ANISOU 1176 CA GLN A 180 17861 17398 17991 471 28 1744 C ATOM 1177 C GLN A 180 -20.131 26.279 -32.526 1.00140.84 C ANISOU 1177 C GLN A 180 18064 17258 18188 438 59 1855 C ATOM 1178 O GLN A 180 -20.751 27.191 -33.090 1.00140.88 O ANISOU 1178 O GLN A 180 18123 17182 18221 527 36 2014 O ATOM 1179 CB GLN A 180 -21.364 24.659 -31.023 1.00137.96 C ANISOU 1179 CB GLN A 180 17556 17069 17796 557 15 1583 C ATOM 1180 CG GLN A 180 -22.500 25.586 -30.634 1.00138.34 C ANISOU 1180 CG GLN A 180 17636 16992 17936 723 -15 1632 C ATOM 1181 CD GLN A 180 -22.002 26.966 -30.172 1.00139.07 C ANISOU 1181 CD GLN A 180 17849 16808 18182 721 20 1661 C ATOM 1182 OE1 GLN A 180 -22.451 27.995 -30.673 1.00141.45 O ANISOU 1182 OE1 GLN A 180 18217 16991 18536 807 8 1810 O ATOM 1183 NE2 GLN A 180 -21.072 26.983 -29.219 1.00136.93 N ANISOU 1183 NE2 GLN A 180 17608 16435 17983 622 60 1521 N ATOM 1184 N ASN A 181 -18.910 26.464 -32.020 1.00139.48 N ANISOU 1184 N ASN A 181 17932 16985 18080 307 109 1778 N ATOM 1185 CA ASN A 181 -18.392 27.784 -31.672 1.00137.73 C ANISOU 1185 CA ASN A 181 17825 16509 17999 274 140 1824 C ATOM 1186 C ASN A 181 -18.041 28.627 -32.901 1.00136.56 C ANISOU 1186 C ASN A 181 17749 16307 17830 223 153 2039 C ATOM 1187 O ASN A 181 -18.006 28.154 -34.040 1.00135.18 O ANISOU 1187 O ASN A 181 17532 16310 17521 190 146 2146 O ATOM 1188 CB ASN A 181 -17.161 27.658 -30.774 1.00133.86 C ANISOU 1188 CB ASN A 181 17340 15954 17568 132 185 1673 C ATOM 1189 N GLY A 182 -17.775 29.903 -32.639 1.00137.86 N ANISOU 1189 N GLY A 182 18030 16220 18130 211 176 2100 N ATOM 1190 CA GLY A 182 -17.350 30.851 -33.657 1.00141.99 C ANISOU 1190 CA GLY A 182 18643 16647 18660 148 195 2307 C ATOM 1191 C GLY A 182 -15.947 31.378 -33.341 1.00144.16 C ANISOU 1191 C GLY A 182 18981 16783 19011 -41 256 2270 C ATOM 1192 O GLY A 182 -15.590 31.517 -32.170 1.00144.70 O ANISOU 1192 O GLY A 182 19068 16729 19183 -74 274 2106 O ATOM 1193 N SER A 183 -15.182 31.640 -34.406 1.00143.93 N ANISOU 1193 N SER A 183 18977 16793 18918 -168 287 2423 N ATOM 1194 CA SER A 183 -13.773 32.045 -34.354 1.00141.90 C ANISOU 1194 CA SER A 183 18757 16456 18700 -373 347 2415 C ATOM 1195 C SER A 183 -12.866 30.884 -33.934 1.00137.67 C ANISOU 1195 C SER A 183 18103 16113 18093 -487 373 2235 C ATOM 1196 O SER A 183 -11.653 30.914 -34.178 1.00138.85 O ANISOU 1196 O SER A 183 18241 16295 18223 -662 423 2242 O ATOM 1197 CB SER A 183 -13.577 33.250 -33.427 1.00143.21 C ANISOU 1197 CB SER A 183 19049 16307 19056 -395 366 2375 C ATOM 1198 N VAL A 184 -13.442 29.862 -33.295 1.00131.18 N ANISOU 1198 N VAL A 184 17191 15418 17233 -388 340 2079 N ATOM 1199 CA VAL A 184 -12.785 28.582 -33.040 1.00125.06 C ANISOU 1199 CA VAL A 184 16294 14851 16370 -458 356 1929 C ATOM 1200 C VAL A 184 -13.863 27.510 -33.147 1.00118.92 C ANISOU 1200 C VAL A 184 15435 14253 15495 -315 308 1881 C ATOM 1201 O VAL A 184 -15.060 27.801 -33.115 1.00122.05 O ANISOU 1201 O VAL A 184 15860 14597 15915 -166 263 1928 O ATOM 1202 CB VAL A 184 -12.106 28.517 -31.650 1.00123.93 C ANISOU 1202 CB VAL A 184 16139 14623 16327 -524 372 1734 C ATOM 1203 CG1 VAL A 184 -13.157 28.465 -30.549 1.00124.02 C ANISOU 1203 CG1 VAL A 184 16158 14551 16411 -373 328 1614 C ATOM 1204 CG2 VAL A 184 -11.115 27.356 -31.556 1.00120.48 C ANISOU 1204 CG2 VAL A 184 15583 14389 15804 -627 399 1619 C ATOM 1205 N THR A 185 -13.445 26.258 -33.267 1.00106.01 N ANISOU 1205 N THR A 185 13696 12831 13754 -359 319 1785 N ATOM 1206 CA THR A 185 -14.376 25.144 -33.378 1.00 94.41 C ANISOU 1206 CA THR A 185 12147 11536 12187 -249 278 1728 C ATOM 1207 C THR A 185 -14.333 24.328 -32.091 1.00 83.57 C ANISOU 1207 C THR A 185 10715 10181 10855 -228 270 1522 C ATOM 1208 O THR A 185 -13.339 23.647 -31.811 1.00 79.94 O ANISOU 1208 O THR A 185 10199 9801 10374 -324 303 1421 O ATOM 1209 CB THR A 185 -14.041 24.277 -34.588 1.00 91.11 C ANISOU 1209 CB THR A 185 11665 11348 11607 -306 297 1780 C ATOM 1210 OG1 THR A 185 -14.098 25.070 -35.780 1.00 94.13 O ANISOU 1210 OG1 THR A 185 12102 11722 11940 -328 303 1983 O ATOM 1211 CG2 THR A 185 -15.028 23.137 -34.703 1.00 84.86 C ANISOU 1211 CG2 THR A 185 10800 10726 10716 -205 253 1715 C ATOM 1212 N SER A 186 -15.413 24.387 -31.318 1.00 75.05 N ANISOU 1212 N SER A 186 9645 9039 9832 -99 226 1465 N ATOM 1213 CA SER A 186 -15.467 23.745 -30.016 1.00 74.20 C ANISOU 1213 CA SER A 186 9491 8932 9768 -75 217 1281 C ATOM 1214 C SER A 186 -16.378 22.531 -30.071 1.00 70.78 C ANISOU 1214 C SER A 186 8977 8676 9240 13 180 1223 C ATOM 1215 O SER A 186 -17.495 22.598 -30.589 1.00 73.43 O ANISOU 1215 O SER A 186 9312 9053 9535 116 143 1303 O ATOM 1216 CB SER A 186 -15.942 24.711 -28.934 1.00 75.64 C ANISOU 1216 CB SER A 186 9742 8909 10088 -7 203 1235 C ATOM 1217 OG SER A 186 -17.286 25.065 -29.137 1.00 77.45 O ANISOU 1217 OG SER A 186 9992 9111 10324 142 164 1306 O ATOM 1218 N CYS A 187 -15.877 21.428 -29.547 1.00 67.59 N ANISOU 1218 N CYS A 187 8505 8377 8801 -32 191 1090 N ATOM 1219 CA CYS A 187 -16.611 20.196 -29.368 1.00 64.94 C ANISOU 1219 CA CYS A 187 8097 8187 8391 30 162 1007 C ATOM 1220 C CYS A 187 -16.359 19.766 -27.929 1.00 64.27 C ANISOU 1220 C CYS A 187 7985 8064 8371 27 163 848 C ATOM 1221 O CYS A 187 -15.441 20.275 -27.278 1.00 68.05 O ANISOU 1221 O CYS A 187 8489 8442 8927 -43 188 804 O ATOM 1222 CB CYS A 187 -16.137 19.145 -30.380 1.00 65.11 C ANISOU 1222 CB CYS A 187 8064 8389 8285 -32 182 1018 C ATOM 1223 SG CYS A 187 -17.027 17.598 -30.396 1.00 69.42 S ANISOU 1223 SG CYS A 187 8534 9112 8730 25 151 929 S ATOM 1224 N LEU A 188 -17.205 18.877 -27.409 1.00 53.84 N ANISOU 1224 N LEU A 188 6614 6825 7018 98 132 767 N ATOM 1225 CA LEU A 188 -17.001 18.226 -26.121 1.00 49.77 C ANISOU 1225 CA LEU A 188 6063 6313 6536 92 130 623 C ATOM 1226 C LEU A 188 -17.316 19.125 -24.924 1.00 55.50 C ANISOU 1226 C LEU A 188 6828 6891 7368 137 120 569 C ATOM 1227 O LEU A 188 -16.998 18.767 -23.777 1.00 60.53 O ANISOU 1227 O LEU A 188 7443 7519 8037 118 121 452 O ATOM 1228 CB LEU A 188 -15.560 17.718 -25.993 1.00 49.45 C ANISOU 1228 CB LEU A 188 5993 6305 6489 -18 167 567 C ATOM 1229 CG LEU A 188 -15.130 16.711 -27.051 1.00 52.80 C ANISOU 1229 CG LEU A 188 6374 6877 6810 -61 188 591 C ATOM 1230 CD1 LEU A 188 -13.663 16.373 -26.844 1.00 56.63 C ANISOU 1230 CD1 LEU A 188 6826 7384 7306 -157 228 539 C ATOM 1231 CD2 LEU A 188 -16.013 15.484 -27.036 1.00 54.12 C ANISOU 1231 CD2 LEU A 188 6496 7163 6905 -3 161 537 C ATOM 1232 N GLU A 189 -17.943 20.278 -25.144 1.00 55.61 N ANISOU 1232 N GLU A 189 6903 6789 7437 200 112 649 N ATOM 1233 CA GLU A 189 -18.079 21.322 -24.138 1.00 57.76 C ANISOU 1233 CA GLU A 189 7232 6893 7820 234 115 601 C ATOM 1234 C GLU A 189 -19.537 21.449 -23.693 1.00 66.34 C ANISOU 1234 C GLU A 189 8309 7976 8920 376 84 585 C ATOM 1235 O GLU A 189 -20.454 21.401 -24.522 1.00 73.63 O ANISOU 1235 O GLU A 189 9216 8963 9796 456 60 680 O ATOM 1236 CB GLU A 189 -17.627 22.677 -24.704 1.00 57.88 C ANISOU 1236 CB GLU A 189 7339 6747 7907 200 136 707 C ATOM 1237 CG GLU A 189 -16.175 22.799 -25.199 1.00 58.99 C ANISOU 1237 CG GLU A 189 7492 6878 8043 50 173 740 C ATOM 1238 CD GLU A 189 -15.130 22.648 -24.115 1.00 63.20 C ANISOU 1238 CD GLU A 189 8009 7385 8619 -48 191 608 C ATOM 1239 OE1 GLU A 189 -15.410 22.967 -22.939 1.00 65.98 O ANISOU 1239 OE1 GLU A 189 8380 7653 9036 -14 182 504 O ATOM 1240 OE2 GLU A 189 -13.998 22.250 -24.460 1.00 65.36 O ANISOU 1240 OE2 GLU A 189 8248 7729 8858 -160 216 610 O ATOM 1241 N LEU A 190 -19.756 21.645 -22.391 1.00 59.71 N ANISOU 1241 N LEU A 190 7474 7072 8141 409 85 467 N ATOM 1242 CA LEU A 190 -21.076 22.029 -21.906 1.00 56.94 C ANISOU 1242 CA LEU A 190 7121 6692 7821 549 66 450 C ATOM 1243 C LEU A 190 -21.331 23.499 -22.211 1.00 60.40 C ANISOU 1243 C LEU A 190 7651 6944 8354 613 76 534 C ATOM 1244 O LEU A 190 -20.437 24.339 -22.066 1.00 64.53 O ANISOU 1244 O LEU A 190 8252 7315 8953 539 104 531 O ATOM 1245 CB LEU A 190 -21.212 21.773 -20.402 1.00 56.05 C ANISOU 1245 CB LEU A 190 6985 6578 7734 561 70 292 C ATOM 1246 CG LEU A 190 -22.574 22.108 -19.764 1.00 63.00 C ANISOU 1246 CG LEU A 190 7849 7446 8640 706 60 254 C ATOM 1247 CD1 LEU A 190 -23.704 21.274 -20.362 1.00 62.71 C ANISOU 1247 CD1 LEU A 190 7729 7581 8517 783 27 312 C ATOM 1248 CD2 LEU A 190 -22.550 21.948 -18.235 1.00 65.21 C ANISOU 1248 CD2 LEU A 190 8114 7721 8941 699 72 93 C ATOM 1249 N ASN A 191 -22.557 23.810 -22.629 1.00 59.85 N ANISOU 1249 N ASN A 191 7570 6887 8283 751 54 611 N ATOM 1250 CA ASN A 191 -22.893 25.159 -23.073 1.00 66.22 C ANISOU 1250 CA ASN A 191 8463 7521 9178 834 59 718 C ATOM 1251 C ASN A 191 -24.398 25.373 -22.954 1.00 63.97 C ANISOU 1251 C ASN A 191 8139 7264 8901 1016 35 740 C ATOM 1252 O ASN A 191 -25.168 24.432 -22.749 1.00 61.48 O ANISOU 1252 O ASN A 191 7725 7125 8508 1060 10 696 O ATOM 1253 CB ASN A 191 -22.380 25.401 -24.500 1.00 70.89 C ANISOU 1253 CB ASN A 191 9089 8113 9734 775 57 887 C ATOM 1254 CG ASN A 191 -23.013 24.471 -25.529 1.00 77.36 C ANISOU 1254 CG ASN A 191 9822 9147 10424 804 19 976 C ATOM 1255 OD1 ASN A 191 -23.992 23.785 -25.258 1.00 77.69 O ANISOU 1255 OD1 ASN A 191 9782 9322 10415 884 -9 932 O ATOM 1256 ND2 ASN A 191 -22.383 24.381 -26.691 1.00 83.72 N ANISOU 1256 ND2 ASN A 191 10641 10001 11169 720 22 1092 N ATOM 1257 N LEU A 192 -24.803 26.636 -23.093 1.00 70.48 N ANISOU 1257 N LEU A 192 9043 7911 9825 1120 43 814 N ATOM 1258 CA LEU A 192 -26.195 27.026 -22.875 1.00 73.72 C ANISOU 1258 CA LEU A 192 9421 8323 10266 1311 27 830 C ATOM 1259 C LEU A 192 -27.152 26.240 -23.768 1.00 73.41 C ANISOU 1259 C LEU A 192 9271 8509 10112 1378 -23 933 C ATOM 1260 O LEU A 192 -28.177 25.719 -23.302 1.00 72.46 O ANISOU 1260 O LEU A 192 9056 8521 9953 1470 -41 875 O ATOM 1261 CB LEU A 192 -26.346 28.527 -23.120 1.00 77.73 C ANISOU 1261 CB LEU A 192 10043 8588 10901 1409 43 924 C ATOM 1262 CG LEU A 192 -27.736 29.109 -22.873 1.00 88.49 C ANISOU 1262 CG LEU A 192 11382 9922 12319 1629 34 944 C ATOM 1263 CD1 LEU A 192 -28.132 28.965 -21.407 1.00 92.81 C ANISOU 1263 CD1 LEU A 192 11896 10468 12900 1678 61 743 C ATOM 1264 CD2 LEU A 192 -27.803 30.560 -23.327 1.00 90.23 C ANISOU 1264 CD2 LEU A 192 11725 9893 12664 1725 48 1069 C ATOM 1265 N TYR A 193 -26.800 26.107 -25.053 1.00 71.40 N ANISOU 1265 N TYR A 193 9024 8314 9791 1318 -44 1080 N ATOM 1266 CA TYR A 193 -27.659 25.425 -26.017 1.00 69.32 C ANISOU 1266 CA TYR A 193 8662 8265 9409 1368 -94 1185 C ATOM 1267 C TYR A 193 -28.120 24.062 -25.515 1.00 66.51 C ANISOU 1267 C TYR A 193 8189 8126 8957 1338 -111 1064 C ATOM 1268 O TYR A 193 -29.287 23.692 -25.678 1.00 74.77 O ANISOU 1268 O TYR A 193 9141 9323 9947 1436 -148 1090 O ATOM 1269 CB TYR A 193 -26.928 25.270 -27.353 1.00 70.21 C ANISOU 1269 CB TYR A 193 8802 8431 9443 1259 -104 1322 C ATOM 1270 N LYS A 194 -27.233 23.304 -24.887 1.00 56.57 N ANISOU 1270 N LYS A 194 6930 6885 7679 1204 -86 934 N ATOM 1271 CA LYS A 194 -27.608 21.955 -24.513 1.00 59.64 C ANISOU 1271 CA LYS A 194 7217 7471 7973 1164 -102 837 C ATOM 1272 C LYS A 194 -27.938 21.793 -23.031 1.00 58.61 C ANISOU 1272 C LYS A 194 7059 7321 7889 1200 -82 679 C ATOM 1273 O LYS A 194 -28.383 20.702 -22.635 1.00 57.73 O ANISOU 1273 O LYS A 194 6861 7370 7703 1176 -96 604 O ATOM 1274 CB LYS A 194 -26.498 20.981 -24.932 1.00 63.83 C ANISOU 1274 CB LYS A 194 7748 8076 8426 998 -92 812 C ATOM 1275 CG LYS A 194 -25.191 21.189 -24.228 1.00 67.47 C ANISOU 1275 CG LYS A 194 8279 8401 8955 895 -49 725 C ATOM 1276 CD LYS A 194 -24.141 20.198 -24.694 1.00 67.66 C ANISOU 1276 CD LYS A 194 8290 8514 8902 749 -39 707 C ATOM 1277 CE LYS A 194 -23.630 20.522 -26.078 1.00 62.88 C ANISOU 1277 CE LYS A 194 7722 7911 8259 702 -38 847 C ATOM 1278 NZ LYS A 194 -22.477 19.628 -26.409 1.00 60.83 N ANISOU 1278 NZ LYS A 194 7451 7723 7937 563 -15 810 N ATOM 1279 N ILE A 195 -27.807 22.851 -22.220 1.00 54.06 N ANISOU 1279 N ILE A 195 6553 6559 7429 1258 -51 629 N ATOM 1280 CA ILE A 195 -27.913 22.663 -20.769 1.00 54.54 C ANISOU 1280 CA ILE A 195 6595 6607 7521 1265 -26 464 C ATOM 1281 C ILE A 195 -29.251 22.026 -20.379 1.00 49.16 C ANISOU 1281 C ILE A 195 5797 6099 6781 1360 -47 428 C ATOM 1282 O ILE A 195 -29.276 20.935 -19.786 1.00 49.25 O ANISOU 1282 O ILE A 195 5745 6243 6724 1291 -49 336 O ATOM 1283 CB ILE A 195 -27.646 23.985 -20.006 1.00 60.00 C ANISOU 1283 CB ILE A 195 7386 7067 8344 1319 14 409 C ATOM 1284 CG1 ILE A 195 -27.587 23.767 -18.482 1.00 60.24 C ANISOU 1284 CG1 ILE A 195 7403 7094 8393 1302 42 227 C ATOM 1285 CG2 ILE A 195 -28.605 25.082 -20.398 1.00 62.65 C ANISOU 1285 CG2 ILE A 195 7744 7309 8750 1493 9 503 C ATOM 1286 CD1 ILE A 195 -26.405 22.944 -17.995 1.00 56.92 C ANISOU 1286 CD1 ILE A 195 6985 6713 7929 1132 50 139 C ATOM 1287 N ALA A 196 -30.368 22.647 -20.767 1.00 45.18 N ANISOU 1287 N ALA A 196 5261 5606 6298 1514 -64 510 N ATOM 1288 CA ALA A 196 -31.666 22.105 -20.384 1.00 48.41 C ANISOU 1288 CA ALA A 196 5548 6191 6653 1604 -82 477 C ATOM 1289 C ALA A 196 -31.801 20.664 -20.859 1.00 50.33 C ANISOU 1289 C ALA A 196 5702 6655 6765 1498 -117 486 C ATOM 1290 O ALA A 196 -32.190 19.775 -20.088 1.00 54.65 O ANISOU 1290 O ALA A 196 6175 7329 7260 1465 -114 389 O ATOM 1291 CB ALA A 196 -32.795 22.975 -20.935 1.00 41.86 C ANISOU 1291 CB ALA A 196 4687 5359 5860 1788 -102 589 C ATOM 1292 N LYS A 197 -31.382 20.404 -22.101 1.00 47.97 N ANISOU 1292 N LYS A 197 5420 6395 6411 1430 -145 597 N ATOM 1293 CA LYS A 197 -31.497 19.061 -22.644 1.00 49.32 C ANISOU 1293 CA LYS A 197 5517 6763 6458 1328 -175 602 C ATOM 1294 C LYS A 197 -30.799 18.067 -21.735 1.00 50.27 C ANISOU 1294 C LYS A 197 5641 6904 6557 1202 -150 466 C ATOM 1295 O LYS A 197 -31.401 17.082 -21.284 1.00 49.96 O ANISOU 1295 O LYS A 197 5520 7011 6453 1175 -161 403 O ATOM 1296 CB LYS A 197 -30.910 19.013 -24.053 1.00 57.91 C ANISOU 1296 CB LYS A 197 6644 7864 7494 1260 -197 723 C ATOM 1297 CG LYS A 197 -31.727 19.784 -25.055 1.00 73.06 C ANISOU 1297 CG LYS A 197 8542 9812 9405 1379 -235 876 C ATOM 1298 CD LYS A 197 -31.157 19.694 -26.460 1.00 80.92 C ANISOU 1298 CD LYS A 197 9573 10844 10331 1303 -256 998 C ATOM 1299 CE LYS A 197 -32.027 20.498 -27.418 1.00 87.26 C ANISOU 1299 CE LYS A 197 10350 11685 11121 1430 -299 1163 C ATOM 1300 NZ LYS A 197 -31.546 20.473 -28.820 1.00 90.84 N ANISOU 1300 NZ LYS A 197 10835 12188 11493 1361 -321 1294 N ATOM 1301 N LEU A 198 -29.535 18.347 -21.399 1.00 46.33 N ANISOU 1301 N LEU A 198 5232 6256 6114 1126 -117 422 N ATOM 1302 CA LEU A 198 -28.788 17.353 -20.648 1.00 46.28 C ANISOU 1302 CA LEU A 198 5224 6279 6079 1007 -100 312 C ATOM 1303 C LEU A 198 -29.342 17.243 -19.233 1.00 48.59 C ANISOU 1303 C LEU A 198 5478 6592 6394 1049 -83 195 C ATOM 1304 O LEU A 198 -29.384 16.146 -18.659 1.00 49.55 O ANISOU 1304 O LEU A 198 5551 6818 6457 980 -84 124 O ATOM 1305 CB LEU A 198 -27.294 17.681 -20.661 1.00 48.51 C ANISOU 1305 CB LEU A 198 5599 6421 6412 914 -72 298 C ATOM 1306 CG LEU A 198 -26.632 17.610 -22.049 1.00 53.65 C ANISOU 1306 CG LEU A 198 6283 7078 7024 850 -81 405 C ATOM 1307 CD1 LEU A 198 -25.164 18.018 -21.990 1.00 50.99 C ANISOU 1307 CD1 LEU A 198 6026 6606 6740 759 -48 391 C ATOM 1308 CD2 LEU A 198 -26.782 16.237 -22.700 1.00 50.75 C ANISOU 1308 CD2 LEU A 198 5855 6885 6544 778 -103 412 C ATOM 1309 N GLN A 199 -29.866 18.352 -18.692 1.00 47.88 N ANISOU 1309 N GLN A 199 5403 6409 6380 1168 -66 180 N ATOM 1310 CA GLN A 199 -30.509 18.269 -17.382 1.00 48.63 C ANISOU 1310 CA GLN A 199 5450 6544 6482 1217 -46 68 C ATOM 1311 C GLN A 199 -31.634 17.242 -17.392 1.00 46.90 C ANISOU 1311 C GLN A 199 5113 6537 6171 1227 -71 70 C ATOM 1312 O GLN A 199 -31.745 16.426 -16.469 1.00 48.32 O ANISOU 1312 O GLN A 199 5250 6802 6309 1173 -61 -18 O ATOM 1313 CB GLN A 199 -31.014 19.642 -16.947 1.00 49.64 C ANISOU 1313 CB GLN A 199 5609 6545 6706 1362 -22 53 C ATOM 1314 CG GLN A 199 -29.910 20.619 -16.573 1.00 53.88 C ANISOU 1314 CG GLN A 199 6268 6865 7340 1334 11 11 C ATOM 1315 CD GLN A 199 -30.446 22.011 -16.278 1.00 59.08 C ANISOU 1315 CD GLN A 199 6972 7376 8100 1483 37 2 C ATOM 1316 OE1 GLN A 199 -31.631 22.291 -16.487 1.00 59.00 O ANISOU 1316 OE1 GLN A 199 6899 7427 8092 1623 28 48 O ATOM 1317 NE2 GLN A 199 -29.586 22.880 -15.765 1.00 60.85 N ANISOU 1317 NE2 GLN A 199 7302 7407 8410 1455 70 -61 N ATOM 1318 N THR A 200 -32.424 17.198 -18.465 1.00 41.36 N ANISOU 1318 N THR A 200 4357 5930 5428 1278 -107 177 N ATOM 1319 CA THR A 200 -33.470 16.183 -18.511 1.00 45.67 C ANISOU 1319 CA THR A 200 4787 6686 5882 1265 -133 176 C ATOM 1320 C THR A 200 -32.875 14.786 -18.716 1.00 46.45 C ANISOU 1320 C THR A 200 4883 6865 5899 1104 -145 153 C ATOM 1321 O THR A 200 -33.260 13.835 -18.019 1.00 45.62 O ANISOU 1321 O THR A 200 4720 6871 5742 1048 -142 87 O ATOM 1322 CB THR A 200 -34.503 16.542 -19.585 1.00 52.10 C ANISOU 1322 CB THR A 200 5533 7594 6667 1364 -173 295 C ATOM 1323 OG1 THR A 200 -35.151 17.768 -19.221 1.00 61.66 O ANISOU 1323 OG1 THR A 200 6736 8732 7959 1532 -157 306 O ATOM 1324 CG2 THR A 200 -35.556 15.459 -19.724 1.00 49.59 C ANISOU 1324 CG2 THR A 200 5090 7506 6245 1329 -204 296 C ATOM 1325 N AMET A 201 -31.878 14.662 -19.593 0.50 43.99 N ANISOU 1325 N AMET A 201 4642 6490 5582 1026 -152 202 N ATOM 1326 N BMET A 201 -31.933 14.648 -19.656 0.50 43.99 N ANISOU 1326 N BMET A 201 4639 6498 5579 1028 -154 207 N ATOM 1327 CA AMET A 201 -31.410 13.325 -19.951 0.50 44.83 C ANISOU 1327 CA AMET A 201 4744 6678 5611 890 -163 185 C ATOM 1328 CA BMET A 201 -31.375 13.336 -19.998 0.50 44.89 C ANISOU 1328 CA BMET A 201 4754 6683 5619 888 -163 188 C ATOM 1329 C AMET A 201 -30.653 12.685 -18.801 0.50 44.70 C ANISOU 1329 C AMET A 201 4756 6620 5609 810 -133 80 C ATOM 1330 C BMET A 201 -30.669 12.696 -18.805 0.50 44.72 C ANISOU 1330 C BMET A 201 4757 6622 5611 811 -134 81 C ATOM 1331 O AMET A 201 -30.785 11.477 -18.550 0.50 42.61 O ANISOU 1331 O AMET A 201 4456 6452 5283 728 -139 41 O ATOM 1332 O BMET A 201 -30.811 11.490 -18.554 0.50 42.77 O ANISOU 1332 O BMET A 201 4475 6474 5303 730 -139 42 O ATOM 1333 CB AMET A 201 -30.534 13.388 -21.197 0.50 46.60 C ANISOU 1333 CB AMET A 201 5030 6853 5821 836 -171 260 C ATOM 1334 CB BMET A 201 -30.391 13.470 -21.166 0.50 46.63 C ANISOU 1334 CB BMET A 201 5045 6837 5835 835 -167 258 C ATOM 1335 CG AMET A 201 -31.312 13.448 -22.482 0.50 48.97 C ANISOU 1335 CG AMET A 201 5286 7263 6058 868 -211 365 C ATOM 1336 CG BMET A 201 -30.980 13.822 -22.518 0.50 48.51 C ANISOU 1336 CG BMET A 201 5259 7145 6028 879 -203 376 C ATOM 1337 SD AMET A 201 -30.207 13.260 -23.888 0.50 53.59 S ANISOU 1337 SD AMET A 201 5940 7821 6600 777 -214 435 S ATOM 1338 SD BMET A 201 -32.084 12.552 -23.137 0.50 51.92 S ANISOU 1338 SD BMET A 201 5588 7807 6332 827 -246 387 S ATOM 1339 CE AMET A 201 -29.628 14.933 -24.086 0.50 55.61 C ANISOU 1339 CE AMET A 201 6278 7893 6959 863 -196 514 C ATOM 1340 CE BMET A 201 -31.026 11.105 -23.055 0.50 47.48 C ANISOU 1340 CE BMET A 201 5069 7245 5725 663 -225 303 C ATOM 1341 N ASN A 202 -29.862 13.487 -18.087 1.00 47.78 N ANISOU 1341 N ASN A 202 5211 6866 6078 830 -104 37 N ATOM 1342 CA ASN A 202 -29.185 13.010 -16.889 1.00 45.65 C ANISOU 1342 CA ASN A 202 4959 6566 5818 766 -80 -60 C ATOM 1343 C ASN A 202 -30.177 12.265 -16.010 1.00 48.42 C ANISOU 1343 C ASN A 202 5231 7049 6118 768 -82 -114 C ATOM 1344 O ASN A 202 -29.906 11.156 -15.521 1.00 49.82 O ANISOU 1344 O ASN A 202 5397 7282 6252 680 -81 -154 O ATOM 1345 CB ASN A 202 -28.631 14.181 -16.091 1.00 45.86 C ANISOU 1345 CB ASN A 202 5044 6447 5931 812 -52 -110 C ATOM 1346 CG ASN A 202 -27.690 13.732 -15.010 1.00 52.44 C ANISOU 1346 CG ASN A 202 5904 7251 6770 731 -34 -198 C ATOM 1347 OD1 ASN A 202 -27.265 12.583 -14.992 1.00 50.46 O ANISOU 1347 OD1 ASN A 202 5640 7063 6468 643 -42 -206 O ATOM 1348 ND2 ASN A 202 -27.511 14.576 -13.999 1.00 61.23 N ANISOU 1348 ND2 ASN A 202 7046 8282 7936 767 -11 -271 N ATOM 1349 N TYR A 203 -31.376 12.844 -15.880 1.00 48.08 N ANISOU 1349 N TYR A 203 5128 7063 6079 872 -84 -103 N ATOM 1350 CA TYR A 203 -32.317 12.354 -14.892 1.00 51.08 C ANISOU 1350 CA TYR A 203 5428 7564 6417 884 -76 -161 C ATOM 1351 C TYR A 203 -32.606 10.892 -15.192 1.00 50.06 C ANISOU 1351 C TYR A 203 5251 7569 6201 777 -98 -146 C ATOM 1352 O TYR A 203 -32.614 10.040 -14.293 1.00 47.01 O ANISOU 1352 O TYR A 203 4844 7238 5778 709 -86 -201 O ATOM 1353 CB TYR A 203 -33.619 13.146 -14.961 1.00 50.22 C ANISOU 1353 CB TYR A 203 5245 7518 6319 1019 -77 -137 C ATOM 1354 CG TYR A 203 -34.446 13.083 -13.715 1.00 55.62 C ANISOU 1354 CG TYR A 203 5857 8291 6983 1059 -50 -215 C ATOM 1355 CD1 TYR A 203 -34.329 14.073 -12.761 1.00 62.99 C ANISOU 1355 CD1 TYR A 203 6822 9132 7979 1141 -12 -288 C ATOM 1356 CD2 TYR A 203 -35.149 11.941 -13.377 1.00 61.71 C ANISOU 1356 CD2 TYR A 203 6545 9231 7672 989 -58 -229 C ATOM 1357 CE1 TYR A 203 -35.059 14.031 -11.586 1.00 70.59 C ANISOU 1357 CE1 TYR A 203 7719 10187 8916 1178 19 -368 C ATOM 1358 CE2 TYR A 203 -35.855 11.861 -12.186 1.00 66.73 C ANISOU 1358 CE2 TYR A 203 7114 9959 8282 1014 -27 -299 C ATOM 1359 CZ TYR A 203 -35.807 12.911 -11.290 1.00 72.11 C ANISOU 1359 CZ TYR A 203 7817 10561 9019 1112 12 -370 C ATOM 1360 OH TYR A 203 -36.511 12.840 -10.103 1.00 76.14 O ANISOU 1360 OH TYR A 203 8259 11176 9495 1139 48 -446 O ATOM 1361 N ILE A 204 -32.783 10.577 -16.476 1.00 46.49 N ANISOU 1361 N ILE A 204 4789 7162 5713 753 -129 -72 N ATOM 1362 CA ILE A 204 -33.092 9.206 -16.856 1.00 46.46 C ANISOU 1362 CA ILE A 204 4748 7277 5628 646 -149 -64 C ATOM 1363 C ILE A 204 -31.845 8.336 -16.760 1.00 45.66 C ANISOU 1363 C ILE A 204 4722 7100 5525 536 -138 -95 C ATOM 1364 O ILE A 204 -31.867 7.243 -16.177 1.00 48.40 O ANISOU 1364 O ILE A 204 5059 7496 5835 453 -133 -133 O ATOM 1365 CB ILE A 204 -33.687 9.178 -18.274 1.00 45.55 C ANISOU 1365 CB ILE A 204 4596 7245 5465 653 -187 17 C ATOM 1366 CG1 ILE A 204 -34.933 10.027 -18.326 1.00 58.22 C ANISOU 1366 CG1 ILE A 204 6114 8935 7072 776 -201 54 C ATOM 1367 CG2 ILE A 204 -34.109 7.771 -18.670 1.00 37.54 C ANISOU 1367 CG2 ILE A 204 3543 6357 4363 535 -208 11 C ATOM 1368 CD1 ILE A 204 -35.427 10.218 -19.769 1.00 68.70 C ANISOU 1368 CD1 ILE A 204 7409 10339 8356 800 -244 150 C ATOM 1369 N ALA A 205 -30.727 8.824 -17.296 1.00 39.60 N ANISOU 1369 N ALA A 205 4033 6211 4803 536 -132 -75 N ATOM 1370 CA ALA A 205 -29.551 7.969 -17.348 1.00 40.99 C ANISOU 1370 CA ALA A 205 4268 6330 4975 441 -121 -97 C ATOM 1371 C ALA A 205 -29.029 7.702 -15.944 1.00 41.87 C ANISOU 1371 C ALA A 205 4394 6401 5112 417 -100 -165 C ATOM 1372 O ALA A 205 -28.610 6.583 -15.634 1.00 47.70 O ANISOU 1372 O ALA A 205 5146 7154 5825 337 -97 -188 O ATOM 1373 CB ALA A 205 -28.473 8.593 -18.240 1.00 40.46 C ANISOU 1373 CB ALA A 205 4268 6158 4946 445 -115 -58 C ATOM 1374 N LEU A 206 -29.061 8.715 -15.078 1.00 39.23 N ANISOU 1374 N LEU A 206 4061 6019 4826 486 -85 -197 N ATOM 1375 CA LEU A 206 -28.721 8.499 -13.677 1.00 44.18 C ANISOU 1375 CA LEU A 206 4690 6636 5459 464 -67 -265 C ATOM 1376 C LEU A 206 -29.531 7.350 -13.093 1.00 44.06 C ANISOU 1376 C LEU A 206 4620 6743 5377 413 -72 -280 C ATOM 1377 O LEU A 206 -28.973 6.439 -12.471 1.00 40.82 O ANISOU 1377 O LEU A 206 4228 6334 4949 342 -68 -300 O ATOM 1378 CB LEU A 206 -28.976 9.771 -12.866 1.00 48.01 C ANISOU 1378 CB LEU A 206 5174 7079 5991 552 -49 -308 C ATOM 1379 CG LEU A 206 -28.612 9.665 -11.387 1.00 46.68 C ANISOU 1379 CG LEU A 206 5007 6910 5817 528 -31 -385 C ATOM 1380 CD1 LEU A 206 -27.106 9.472 -11.195 1.00 40.90 C ANISOU 1380 CD1 LEU A 206 4338 6090 5111 461 -31 -400 C ATOM 1381 CD2 LEU A 206 -29.114 10.883 -10.639 1.00 50.54 C ANISOU 1381 CD2 LEU A 206 5487 7374 6341 620 -9 -441 C ATOM 1382 N VAL A 207 -30.854 7.360 -13.299 1.00 41.76 N ANISOU 1382 N VAL A 207 4258 6561 5050 447 -80 -262 N ATOM 1383 CA VAL A 207 -31.676 6.399 -12.576 1.00 38.16 C ANISOU 1383 CA VAL A 207 3743 6225 4532 394 -78 -280 C ATOM 1384 C VAL A 207 -31.638 5.040 -13.256 1.00 44.28 C ANISOU 1384 C VAL A 207 4528 7037 5261 288 -96 -249 C ATOM 1385 O VAL A 207 -31.308 4.029 -12.623 1.00 47.03 O ANISOU 1385 O VAL A 207 4896 7388 5587 209 -90 -265 O ATOM 1386 CB VAL A 207 -33.109 6.926 -12.404 1.00 39.61 C ANISOU 1386 CB VAL A 207 3832 6526 4691 467 -76 -280 C ATOM 1387 CG1 VAL A 207 -33.996 5.858 -11.786 1.00 35.14 C ANISOU 1387 CG1 VAL A 207 3198 6100 4053 393 -74 -289 C ATOM 1388 CG2 VAL A 207 -33.086 8.148 -11.473 1.00 35.59 C ANISOU 1388 CG2 VAL A 207 3324 5969 4229 568 -48 -332 C ATOM 1389 N VAL A 208 -31.916 5.001 -14.557 1.00 41.91 N ANISOU 1389 N VAL A 208 4221 6757 4945 284 -117 -206 N ATOM 1390 CA VAL A 208 -31.990 3.727 -15.255 1.00 41.93 C ANISOU 1390 CA VAL A 208 4235 6799 4898 181 -131 -191 C ATOM 1391 C VAL A 208 -30.609 3.239 -15.693 1.00 44.07 C ANISOU 1391 C VAL A 208 4597 6952 5197 135 -124 -194 C ATOM 1392 O VAL A 208 -30.385 2.027 -15.813 1.00 40.51 O ANISOU 1392 O VAL A 208 4175 6497 4720 46 -123 -202 O ATOM 1393 CB VAL A 208 -32.935 3.832 -16.461 1.00 41.20 C ANISOU 1393 CB VAL A 208 4090 6804 4761 187 -160 -150 C ATOM 1394 CG1 VAL A 208 -32.962 2.516 -17.194 1.00 44.77 C ANISOU 1394 CG1 VAL A 208 4563 7289 5160 68 -172 -150 C ATOM 1395 CG2 VAL A 208 -34.339 4.240 -16.024 1.00 36.33 C ANISOU 1395 CG2 VAL A 208 3366 6323 4115 236 -167 -145 C ATOM 1396 N GLY A 209 -29.666 4.150 -15.915 1.00 42.65 N ANISOU 1396 N GLY A 209 4461 6673 5071 192 -116 -188 N ATOM 1397 CA GLY A 209 -28.371 3.724 -16.406 1.00 43.98 C ANISOU 1397 CA GLY A 209 4700 6747 5262 153 -106 -189 C ATOM 1398 C GLY A 209 -27.293 3.555 -15.365 1.00 45.30 C ANISOU 1398 C GLY A 209 4905 6836 5470 143 -88 -220 C ATOM 1399 O GLY A 209 -26.235 3.006 -15.676 1.00 46.33 O ANISOU 1399 O GLY A 209 5083 6903 5617 109 -79 -222 O ATOM 1400 N CYS A 210 -27.512 4.003 -14.130 1.00 45.58 N ANISOU 1400 N CYS A 210 4917 6884 5519 175 -83 -246 N ATOM 1401 CA CYS A 210 -26.465 3.878 -13.124 1.00 42.35 C ANISOU 1401 CA CYS A 210 4537 6415 5139 162 -73 -273 C ATOM 1402 C CYS A 210 -26.995 3.282 -11.826 1.00 40.64 C ANISOU 1402 C CYS A 210 4291 6264 4887 135 -71 -294 C ATOM 1403 O CYS A 210 -26.551 2.212 -11.404 1.00 40.36 O ANISOU 1403 O CYS A 210 4276 6220 4838 80 -72 -287 O ATOM 1404 CB CYS A 210 -25.823 5.241 -12.849 1.00 45.38 C ANISOU 1404 CB CYS A 210 4936 6729 5576 222 -65 -292 C ATOM 1405 SG CYS A 210 -24.412 5.160 -11.692 1.00 49.35 S ANISOU 1405 SG CYS A 210 5467 7175 6107 197 -59 -327 S ATOM 1406 N LEU A 211 -27.958 3.958 -11.201 1.00 42.48 N ANISOU 1406 N LEU A 211 4473 6563 5104 178 -68 -314 N ATOM 1407 CA LEU A 211 -28.404 3.570 -9.868 1.00 42.46 C ANISOU 1407 CA LEU A 211 4438 6632 5062 156 -60 -337 C ATOM 1408 C LEU A 211 -29.161 2.241 -9.874 1.00 43.65 C ANISOU 1408 C LEU A 211 4568 6861 5158 77 -65 -308 C ATOM 1409 O LEU A 211 -28.958 1.412 -8.984 1.00 49.87 O ANISOU 1409 O LEU A 211 5364 7664 5919 24 -62 -303 O ATOM 1410 CB LEU A 211 -29.257 4.688 -9.265 1.00 43.37 C ANISOU 1410 CB LEU A 211 4502 6803 5174 229 -47 -375 C ATOM 1411 CG LEU A 211 -28.574 6.031 -8.941 1.00 43.46 C ANISOU 1411 CG LEU A 211 4542 6730 5240 299 -37 -419 C ATOM 1412 CD1 LEU A 211 -29.582 7.081 -8.424 1.00 42.26 C ANISOU 1412 CD1 LEU A 211 4341 6629 5086 383 -17 -462 C ATOM 1413 CD2 LEU A 211 -27.424 5.849 -7.936 1.00 36.53 C ANISOU 1413 CD2 LEU A 211 3701 5813 4365 261 -36 -449 C ATOM 1414 N LEU A 212 -30.053 2.018 -10.844 1.00 44.33 N ANISOU 1414 N LEU A 212 4624 6998 5221 63 -74 -286 N ATOM 1415 CA LEU A 212 -30.735 0.725 -10.912 1.00 41.30 C ANISOU 1415 CA LEU A 212 4227 6679 4788 -30 -79 -264 C ATOM 1416 C LEU A 212 -29.763 -0.436 -11.111 1.00 45.75 C ANISOU 1416 C LEU A 212 4866 7152 5365 -99 -80 -247 C ATOM 1417 O LEU A 212 -29.914 -1.464 -10.423 1.00 44.49 O ANISOU 1417 O LEU A 212 4716 7011 5178 -169 -77 -233 O ATOM 1418 CB LEU A 212 -31.807 0.755 -12.006 1.00 42.79 C ANISOU 1418 CB LEU A 212 4366 6947 4946 -39 -93 -248 C ATOM 1419 CG LEU A 212 -32.624 -0.537 -12.195 1.00 48.62 C ANISOU 1419 CG LEU A 212 5085 7759 5628 -152 -100 -232 C ATOM 1420 CD1 LEU A 212 -33.437 -0.901 -10.951 1.00 48.96 C ANISOU 1420 CD1 LEU A 212 5072 7904 5627 -192 -86 -233 C ATOM 1421 CD2 LEU A 212 -33.531 -0.447 -13.426 1.00 49.40 C ANISOU 1421 CD2 LEU A 212 5137 7940 5694 -163 -121 -219 C ATOM 1422 N PRO A 213 -28.759 -0.353 -12.001 1.00 45.22 N ANISOU 1422 N PRO A 213 4854 6987 5339 -80 -82 -246 N ATOM 1423 CA PRO A 213 -27.773 -1.451 -12.078 1.00 45.37 C ANISOU 1423 CA PRO A 213 4943 6919 5379 -128 -78 -235 C ATOM 1424 C PRO A 213 -26.980 -1.649 -10.802 1.00 45.90 C ANISOU 1424 C PRO A 213 5027 6952 5462 -121 -74 -230 C ATOM 1425 O PRO A 213 -26.701 -2.797 -10.420 1.00 40.23 O ANISOU 1425 O PRO A 213 4345 6202 4739 -173 -72 -207 O ATOM 1426 CB PRO A 213 -26.859 -1.020 -13.231 1.00 44.00 C ANISOU 1426 CB PRO A 213 4807 6668 5244 -91 -75 -240 C ATOM 1427 CG PRO A 213 -27.700 -0.114 -14.066 1.00 39.42 C ANISOU 1427 CG PRO A 213 4185 6148 4646 -58 -84 -240 C ATOM 1428 CD PRO A 213 -28.567 0.621 -13.094 1.00 40.75 C ANISOU 1428 CD PRO A 213 4291 6394 4800 -21 -87 -247 C ATOM 1429 N PHE A 214 -26.578 -0.556 -10.146 1.00 41.90 N ANISOU 1429 N PHE A 214 4499 6448 4973 -59 -73 -250 N ATOM 1430 CA PHE A 214 -25.827 -0.690 -8.905 1.00 41.44 C ANISOU 1430 CA PHE A 214 4449 6379 4917 -57 -75 -248 C ATOM 1431 C PHE A 214 -26.678 -1.340 -7.813 1.00 44.31 C ANISOU 1431 C PHE A 214 4785 6828 5223 -106 -74 -231 C ATOM 1432 O PHE A 214 -26.165 -2.116 -6.991 1.00 46.25 O ANISOU 1432 O PHE A 214 5053 7062 5457 -136 -78 -200 O ATOM 1433 CB PHE A 214 -25.302 0.672 -8.450 1.00 45.01 C ANISOU 1433 CB PHE A 214 4884 6823 5393 7 -75 -286 C ATOM 1434 CG PHE A 214 -24.517 0.590 -7.185 1.00 52.00 C ANISOU 1434 CG PHE A 214 5772 7715 6270 3 -81 -289 C ATOM 1435 CD1 PHE A 214 -23.229 0.071 -7.190 1.00 50.64 C ANISOU 1435 CD1 PHE A 214 5634 7479 6129 -2 -90 -265 C ATOM 1436 CD2 PHE A 214 -25.083 0.966 -5.977 1.00 50.57 C ANISOU 1436 CD2 PHE A 214 5553 7618 6041 5 -78 -313 C ATOM 1437 CE1 PHE A 214 -22.512 -0.049 -6.017 1.00 45.96 C ANISOU 1437 CE1 PHE A 214 5035 6909 5520 -7 -104 -259 C ATOM 1438 CE2 PHE A 214 -24.371 0.852 -4.811 1.00 48.69 C ANISOU 1438 CE2 PHE A 214 5315 7403 5781 -6 -89 -314 C ATOM 1439 CZ PHE A 214 -23.079 0.342 -4.832 1.00 44.67 C ANISOU 1439 CZ PHE A 214 4838 6832 5302 -13 -105 -283 C ATOM 1440 N PHE A 215 -27.984 -1.054 -7.806 1.00 42.00 N ANISOU 1440 N PHE A 215 4439 6629 4890 -114 -67 -243 N ATOM 1441 CA PHE A 215 -28.910 -1.757 -6.919 1.00 48.14 C ANISOU 1441 CA PHE A 215 5183 7502 5606 -175 -61 -222 C ATOM 1442 C PHE A 215 -28.948 -3.254 -7.230 1.00 47.41 C ANISOU 1442 C PHE A 215 5137 7370 5506 -265 -64 -173 C ATOM 1443 O PHE A 215 -28.912 -4.100 -6.316 1.00 47.38 O ANISOU 1443 O PHE A 215 5149 7380 5475 -319 -63 -134 O ATOM 1444 CB PHE A 215 -30.299 -1.134 -7.060 1.00 52.30 C ANISOU 1444 CB PHE A 215 5633 8144 6097 -161 -52 -245 C ATOM 1445 CG PHE A 215 -31.351 -1.747 -6.174 1.00 57.36 C ANISOU 1445 CG PHE A 215 6221 8905 6666 -228 -40 -226 C ATOM 1446 CD1 PHE A 215 -31.401 -1.455 -4.819 1.00 63.51 C ANISOU 1446 CD1 PHE A 215 6970 9756 7404 -217 -26 -239 C ATOM 1447 CD2 PHE A 215 -32.306 -2.595 -6.701 1.00 58.08 C ANISOU 1447 CD2 PHE A 215 6291 9050 6727 -310 -41 -199 C ATOM 1448 CE1 PHE A 215 -32.384 -2.009 -4.003 1.00 63.53 C ANISOU 1448 CE1 PHE A 215 6920 9884 7333 -283 -9 -218 C ATOM 1449 CE2 PHE A 215 -33.287 -3.147 -5.893 1.00 62.46 C ANISOU 1449 CE2 PHE A 215 6792 9725 7214 -383 -27 -178 C ATOM 1450 CZ PHE A 215 -33.325 -2.856 -4.543 1.00 62.85 C ANISOU 1450 CZ PHE A 215 6811 9849 7222 -368 -9 -184 C ATOM 1451 N THR A 216 -29.019 -3.594 -8.521 1.00 44.46 N ANISOU 1451 N THR A 216 4790 6945 5156 -284 -68 -176 N ATOM 1452 CA THR A 216 -29.007 -5.000 -8.929 1.00 48.51 C ANISOU 1452 CA THR A 216 5360 7399 5670 -370 -67 -145 C ATOM 1453 C THR A 216 -27.729 -5.706 -8.464 1.00 48.62 C ANISOU 1453 C THR A 216 5446 7304 5725 -361 -67 -114 C ATOM 1454 O THR A 216 -27.769 -6.829 -7.941 1.00 46.19 O ANISOU 1454 O THR A 216 5175 6967 5406 -424 -65 -69 O ATOM 1455 CB THR A 216 -29.162 -5.086 -10.450 1.00 44.82 C ANISOU 1455 CB THR A 216 4913 6899 5219 -382 -70 -169 C ATOM 1456 OG1 THR A 216 -30.408 -4.490 -10.828 1.00 43.51 O ANISOU 1456 OG1 THR A 216 4671 6851 5010 -390 -76 -185 O ATOM 1457 CG2 THR A 216 -29.131 -6.530 -10.930 1.00 45.09 C ANISOU 1457 CG2 THR A 216 5016 6858 5257 -473 -65 -155 C ATOM 1458 N LEU A 217 -26.584 -5.042 -8.631 1.00 43.72 N ANISOU 1458 N LEU A 217 4839 6623 5150 -281 -71 -131 N ATOM 1459 CA LEU A 217 -25.318 -5.584 -8.145 1.00 40.57 C ANISOU 1459 CA LEU A 217 4488 6140 4788 -257 -74 -100 C ATOM 1460 C LEU A 217 -25.331 -5.807 -6.638 1.00 40.58 C ANISOU 1460 C LEU A 217 4472 6196 4751 -272 -83 -58 C ATOM 1461 O LEU A 217 -24.793 -6.804 -6.151 1.00 40.64 O ANISOU 1461 O LEU A 217 4523 6149 4768 -291 -87 -4 O ATOM 1462 CB LEU A 217 -24.176 -4.654 -8.524 1.00 37.08 C ANISOU 1462 CB LEU A 217 4042 5654 4391 -177 -77 -129 C ATOM 1463 CG LEU A 217 -23.958 -4.617 -10.031 1.00 48.45 C ANISOU 1463 CG LEU A 217 5510 7034 5865 -166 -65 -157 C ATOM 1464 CD1 LEU A 217 -22.926 -3.562 -10.381 1.00 53.45 C ANISOU 1464 CD1 LEU A 217 6130 7640 6537 -96 -65 -181 C ATOM 1465 CD2 LEU A 217 -23.505 -5.976 -10.529 1.00 43.57 C ANISOU 1465 CD2 LEU A 217 4959 6322 5273 -195 -54 -137 C ATOM 1466 N SER A 218 -25.909 -4.877 -5.880 1.00 39.11 N ANISOU 1466 N SER A 218 4223 6118 4520 -259 -84 -82 N ATOM 1467 CA SER A 218 -25.853 -5.000 -4.428 1.00 45.53 C ANISOU 1467 CA SER A 218 5017 6999 5285 -272 -91 -49 C ATOM 1468 C SER A 218 -26.673 -6.200 -3.949 1.00 46.50 C ANISOU 1468 C SER A 218 5154 7151 5361 -362 -85 13 C ATOM 1469 O SER A 218 -26.232 -6.982 -3.081 1.00 48.85 O ANISOU 1469 O SER A 218 5480 7436 5643 -385 -93 79 O ATOM 1470 CB SER A 218 -26.332 -3.696 -3.798 1.00 48.27 C ANISOU 1470 CB SER A 218 5295 7453 5590 -235 -86 -106 C ATOM 1471 OG SER A 218 -25.462 -2.644 -4.184 1.00 44.25 O ANISOU 1471 OG SER A 218 4787 6897 5130 -163 -92 -155 O ATOM 1472 N ILE A 219 -27.859 -6.384 -4.535 1.00 41.12 N ANISOU 1472 N ILE A 219 4453 6510 4659 -418 -71 -2 N ATOM 1473 CA ILE A 219 -28.622 -7.602 -4.253 1.00 44.72 C ANISOU 1473 CA ILE A 219 4931 6979 5081 -523 -63 57 C ATOM 1474 C ILE A 219 -27.837 -8.857 -4.673 1.00 45.30 C ANISOU 1474 C ILE A 219 5102 6900 5211 -548 -67 107 C ATOM 1475 O ILE A 219 -27.835 -9.867 -3.955 1.00 43.09 O ANISOU 1475 O ILE A 219 4862 6595 4915 -606 -67 181 O ATOM 1476 CB ILE A 219 -30.003 -7.530 -4.924 1.00 46.92 C ANISOU 1476 CB ILE A 219 5161 7337 5328 -583 -51 25 C ATOM 1477 CG1 ILE A 219 -30.820 -6.432 -4.249 1.00 58.23 C ANISOU 1477 CG1 ILE A 219 6494 8929 6702 -552 -41 -11 C ATOM 1478 CG2 ILE A 219 -30.718 -8.885 -4.895 1.00 48.42 C ANISOU 1478 CG2 ILE A 219 5386 7516 5495 -711 -43 80 C ATOM 1479 CD1 ILE A 219 -32.085 -6.119 -4.961 1.00 68.89 C ANISOU 1479 CD1 ILE A 219 7777 10372 8027 -580 -33 -46 C ATOM 1480 N ACYS A 220 -27.172 -8.796 -5.828 0.62 44.31 N ANISOU 1480 N ACYS A 220 5015 6670 5149 -502 -68 68 N ATOM 1481 N BCYS A 220 -27.183 -8.795 -5.834 0.38 44.85 N ANISOU 1481 N BCYS A 220 5083 6740 5218 -503 -68 68 N ATOM 1482 CA ACYS A 220 -26.399 -9.947 -6.291 0.62 47.35 C ANISOU 1482 CA ACYS A 220 5492 6905 5593 -511 -64 101 C ATOM 1483 CA BCYS A 220 -26.382 -9.922 -6.310 0.38 47.36 C ANISOU 1483 CA BCYS A 220 5493 6906 5595 -509 -64 100 C ATOM 1484 C ACYS A 220 -25.298 -10.313 -5.299 0.62 47.49 C ANISOU 1484 C ACYS A 220 5538 6877 5630 -461 -77 168 C ATOM 1485 C BCYS A 220 -25.306 -10.305 -5.302 0.38 47.04 C ANISOU 1485 C BCYS A 220 5480 6820 5572 -461 -77 167 C ATOM 1486 O ACYS A 220 -25.056 -11.498 -5.037 0.62 45.91 O ANISOU 1486 O ACYS A 220 5405 6586 5451 -493 -75 235 O ATOM 1487 O BCYS A 220 -25.088 -11.493 -5.033 0.38 46.07 O ANISOU 1487 O BCYS A 220 5425 6610 5471 -495 -75 234 O ATOM 1488 CB ACYS A 220 -25.795 -9.647 -7.662 0.62 51.21 C ANISOU 1488 CB ACYS A 220 6005 7314 6138 -458 -58 39 C ATOM 1489 CB BCYS A 220 -25.748 -9.559 -7.653 0.38 50.69 C ANISOU 1489 CB BCYS A 220 5936 7252 6073 -451 -59 37 C ATOM 1490 SG ACYS A 220 -26.953 -9.814 -9.039 0.62 48.67 S ANISOU 1490 SG ACYS A 220 5686 7008 5798 -537 -46 -19 S ATOM 1491 SG BCYS A 220 -25.032 -10.929 -8.563 0.38 53.00 S ANISOU 1491 SG BCYS A 220 6338 7365 6435 -463 -41 44 S ATOM 1492 N TYR A 221 -24.609 -9.308 -4.754 1.00 43.49 N ANISOU 1492 N TYR A 221 4979 6428 5115 -383 -93 153 N ATOM 1493 CA TYR A 221 -23.587 -9.570 -3.745 1.00 44.77 C ANISOU 1493 CA TYR A 221 5151 6579 5282 -338 -112 217 C ATOM 1494 C TYR A 221 -24.184 -10.291 -2.545 1.00 48.33 C ANISOU 1494 C TYR A 221 5607 7087 5670 -407 -118 301 C ATOM 1495 O TYR A 221 -23.658 -11.320 -2.086 1.00 49.16 O ANISOU 1495 O TYR A 221 5767 7119 5793 -410 -126 388 O ATOM 1496 CB TYR A 221 -22.942 -8.263 -3.293 1.00 45.10 C ANISOU 1496 CB TYR A 221 5126 6701 5308 -267 -129 174 C ATOM 1497 CG TYR A 221 -21.835 -8.453 -2.279 1.00 50.74 C ANISOU 1497 CG TYR A 221 5837 7425 6018 -222 -157 235 C ATOM 1498 CD1 TYR A 221 -20.576 -8.890 -2.671 1.00 55.29 C ANISOU 1498 CD1 TYR A 221 6443 7903 6663 -157 -166 261 C ATOM 1499 CD2 TYR A 221 -22.050 -8.212 -0.928 1.00 60.29 C ANISOU 1499 CD2 TYR A 221 7005 8754 7147 -244 -174 268 C ATOM 1500 CE1 TYR A 221 -19.556 -9.070 -1.751 1.00 60.41 C ANISOU 1500 CE1 TYR A 221 7076 8574 7304 -112 -197 324 C ATOM 1501 CE2 TYR A 221 -21.039 -8.390 0.005 1.00 66.85 C ANISOU 1501 CE2 TYR A 221 7826 9612 7962 -207 -206 329 C ATOM 1502 CZ TYR A 221 -19.791 -8.818 -0.416 1.00 68.48 C ANISOU 1502 CZ TYR A 221 8057 9721 8241 -140 -220 360 C ATOM 1503 OH TYR A 221 -18.781 -9.001 0.504 1.00 70.85 O ANISOU 1503 OH TYR A 221 8336 10061 8523 -98 -257 428 O ATOM 1504 N LEU A 222 -25.278 -9.745 -2.012 1.00 45.76 N ANISOU 1504 N LEU A 222 5223 6896 5269 -460 -110 279 N ATOM 1505 CA LEU A 222 -25.924 -10.380 -0.873 1.00 46.92 C ANISOU 1505 CA LEU A 222 5366 7119 5343 -537 -109 359 C ATOM 1506 C LEU A 222 -26.238 -11.851 -1.161 1.00 50.11 C ANISOU 1506 C LEU A 222 5854 7409 5776 -618 -98 434 C ATOM 1507 O LEU A 222 -25.947 -12.745 -0.346 1.00 43.08 O ANISOU 1507 O LEU A 222 5008 6487 4874 -643 -108 537 O ATOM 1508 CB LEU A 222 -27.183 -9.597 -0.529 1.00 49.35 C ANISOU 1508 CB LEU A 222 5592 7586 5571 -582 -92 308 C ATOM 1509 CG LEU A 222 -27.995 -9.931 0.708 1.00 59.69 C ANISOU 1509 CG LEU A 222 6869 9026 6783 -662 -83 370 C ATOM 1510 CD1 LEU A 222 -28.688 -8.661 1.176 1.00 69.56 C ANISOU 1510 CD1 LEU A 222 8021 10445 7964 -640 -69 289 C ATOM 1511 CD2 LEU A 222 -29.024 -10.996 0.375 1.00 55.84 C ANISOU 1511 CD2 LEU A 222 6413 8514 6288 -781 -62 416 C ATOM 1512 N LEU A 223 -26.823 -12.119 -2.335 1.00 48.88 N ANISOU 1512 N LEU A 223 5725 7188 5658 -662 -80 383 N ATOM 1513 CA LEU A 223 -27.276 -13.475 -2.629 1.00 46.73 C ANISOU 1513 CA LEU A 223 5535 6811 5409 -760 -65 437 C ATOM 1514 C LEU A 223 -26.096 -14.423 -2.818 1.00 44.58 C ANISOU 1514 C LEU A 223 5362 6356 5221 -706 -71 491 C ATOM 1515 O LEU A 223 -26.142 -15.585 -2.381 1.00 41.51 O ANISOU 1515 O LEU A 223 5047 5881 4843 -763 -67 584 O ATOM 1516 CB LEU A 223 -28.159 -13.466 -3.873 1.00 45.15 C ANISOU 1516 CB LEU A 223 5334 6601 5222 -823 -47 356 C ATOM 1517 CG LEU A 223 -29.464 -12.679 -3.775 1.00 47.91 C ANISOU 1517 CG LEU A 223 5582 7130 5493 -879 -40 310 C ATOM 1518 CD1 LEU A 223 -30.145 -12.700 -5.133 1.00 50.70 C ANISOU 1518 CD1 LEU A 223 5935 7466 5865 -928 -32 235 C ATOM 1519 CD2 LEU A 223 -30.398 -13.198 -2.676 1.00 45.58 C ANISOU 1519 CD2 LEU A 223 5261 6936 5120 -989 -30 385 C ATOM 1520 N ILE A 224 -25.026 -13.937 -3.458 1.00 40.46 N ANISOU 1520 N ILE A 224 4840 5773 4759 -593 -78 440 N ATOM 1521 CA ILE A 224 -23.826 -14.742 -3.648 1.00 35.62 C ANISOU 1521 CA ILE A 224 4305 5001 4227 -520 -80 485 C ATOM 1522 C ILE A 224 -23.243 -15.158 -2.303 1.00 41.30 C ANISOU 1522 C ILE A 224 5029 5736 4925 -490 -105 606 C ATOM 1523 O ILE A 224 -22.968 -16.347 -2.069 1.00 40.30 O ANISOU 1523 O ILE A 224 4988 5485 4840 -500 -103 696 O ATOM 1524 CB ILE A 224 -22.813 -13.971 -4.514 1.00 37.82 C ANISOU 1524 CB ILE A 224 4558 5253 4560 -407 -81 404 C ATOM 1525 CG1 ILE A 224 -23.361 -13.820 -5.942 1.00 42.99 C ANISOU 1525 CG1 ILE A 224 5228 5870 5235 -443 -55 302 C ATOM 1526 CG2 ILE A 224 -21.449 -14.629 -4.484 1.00 32.21 C ANISOU 1526 CG2 ILE A 224 3896 4417 3923 -308 -86 457 C ATOM 1527 CD1 ILE A 224 -22.618 -12.843 -6.810 1.00 41.52 C ANISOU 1527 CD1 ILE A 224 5001 5694 5079 -354 -53 220 C ATOM 1528 N ILE A 225 -23.076 -14.191 -1.387 1.00 41.69 N ANISOU 1528 N ILE A 225 4991 5941 4908 -456 -130 610 N ATOM 1529 CA ILE A 225 -22.507 -14.499 -0.074 1.00 42.29 C ANISOU 1529 CA ILE A 225 5061 6062 4946 -429 -160 724 C ATOM 1530 C ILE A 225 -23.379 -15.502 0.669 1.00 46.50 C ANISOU 1530 C ILE A 225 5642 6594 5432 -539 -152 830 C ATOM 1531 O ILE A 225 -22.884 -16.479 1.261 1.00 50.73 O ANISOU 1531 O ILE A 225 6239 7050 5987 -527 -166 952 O ATOM 1532 CB ILE A 225 -22.327 -13.216 0.753 1.00 47.67 C ANISOU 1532 CB ILE A 225 5638 6926 5548 -395 -184 688 C ATOM 1533 CG1 ILE A 225 -21.378 -12.254 0.036 1.00 45.96 C ANISOU 1533 CG1 ILE A 225 5381 6698 5384 -295 -192 594 C ATOM 1534 CG2 ILE A 225 -21.864 -13.559 2.186 1.00 45.88 C ANISOU 1534 CG2 ILE A 225 5400 6775 5257 -386 -218 809 C ATOM 1535 CD1 ILE A 225 -20.020 -12.843 -0.170 1.00 43.47 C ANISOU 1535 CD1 ILE A 225 5100 6269 5146 -201 -208 646 C ATOM 1536 N ARG A 226 -24.689 -15.259 0.676 1.00 45.16 N ANISOU 1536 N ARG A 226 5441 6518 5199 -647 -130 791 N ATOM 1537 CA ARG A 226 -25.595 -16.138 1.403 1.00 53.27 C ANISOU 1537 CA ARG A 226 6502 7568 6172 -770 -119 890 C ATOM 1538 C ARG A 226 -25.474 -17.581 0.907 1.00 53.47 C ANISOU 1538 C ARG A 226 6655 7380 6283 -809 -105 960 C ATOM 1539 O ARG A 226 -25.224 -18.520 1.693 1.00 49.19 O ANISOU 1539 O ARG A 226 6174 6776 5739 -827 -115 1096 O ATOM 1540 CB ARG A 226 -27.019 -15.595 1.254 1.00 58.65 C ANISOU 1540 CB ARG A 226 7117 8386 6783 -874 -93 816 C ATOM 1541 CG ARG A 226 -28.090 -16.379 1.963 1.00 71.19 C ANISOU 1541 CG ARG A 226 8719 10028 8302 -1018 -75 906 C ATOM 1542 CD ARG A 226 -29.445 -15.714 1.779 1.00 82.79 C ANISOU 1542 CD ARG A 226 10098 11658 9701 -1104 -50 822 C ATOM 1543 NE ARG A 226 -30.505 -16.467 2.433 1.00 96.30 N ANISOU 1543 NE ARG A 226 11812 13436 11342 -1255 -28 907 N ATOM 1544 CZ ARG A 226 -31.180 -17.443 1.837 1.00105.64 C ANISOU 1544 CZ ARG A 226 13059 14519 12559 -1377 -8 928 C ATOM 1545 NH1 ARG A 226 -30.892 -17.769 0.583 1.00106.51 N ANISOU 1545 NH1 ARG A 226 13238 14462 12768 -1359 -8 863 N ATOM 1546 NH2 ARG A 226 -32.136 -18.092 2.490 1.00111.81 N ANISOU 1546 NH2 ARG A 226 13838 15372 13272 -1525 12 1010 N ATOM 1547 N VAL A 227 -25.615 -17.768 -0.412 1.00 52.21 N ANISOU 1547 N VAL A 227 6540 7100 6198 -818 -83 868 N ATOM 1548 CA VAL A 227 -25.611 -19.119 -0.970 1.00 51.85 C ANISOU 1548 CA VAL A 227 6622 6844 6234 -868 -62 910 C ATOM 1549 C VAL A 227 -24.273 -19.795 -0.704 1.00 46.15 C ANISOU 1549 C VAL A 227 5972 5973 5589 -748 -78 999 C ATOM 1550 O VAL A 227 -24.221 -20.951 -0.267 1.00 43.54 O ANISOU 1550 O VAL A 227 5737 5515 5291 -783 -75 1116 O ATOM 1551 CB VAL A 227 -25.952 -19.086 -2.474 1.00 49.34 C ANISOU 1551 CB VAL A 227 6331 6445 5970 -895 -36 776 C ATOM 1552 CG1 VAL A 227 -25.788 -20.472 -3.081 1.00 52.99 C ANISOU 1552 CG1 VAL A 227 6938 6673 6525 -934 -12 801 C ATOM 1553 CG2 VAL A 227 -27.374 -18.612 -2.665 1.00 43.73 C ANISOU 1553 CG2 VAL A 227 5552 5882 5180 -1025 -24 713 C ATOM 1554 N LEU A 228 -23.177 -19.076 -0.966 1.00 41.60 N ANISOU 1554 N LEU A 228 5347 5412 5047 -604 -96 949 N ATOM 1555 CA LEU A 228 -21.831 -19.604 -0.776 1.00 41.97 C ANISOU 1555 CA LEU A 228 5438 5342 5168 -471 -112 1024 C ATOM 1556 C LEU A 228 -21.612 -20.106 0.649 1.00 48.14 C ANISOU 1556 C LEU A 228 6225 6162 5902 -469 -144 1193 C ATOM 1557 O LEU A 228 -21.126 -21.227 0.864 1.00 52.84 O ANISOU 1557 O LEU A 228 6914 6599 6562 -435 -145 1305 O ATOM 1558 CB LEU A 228 -20.831 -18.504 -1.123 1.00 42.84 C ANISOU 1558 CB LEU A 228 5459 5527 5292 -340 -129 941 C ATOM 1559 CG LEU A 228 -19.345 -18.822 -1.135 1.00 53.02 C ANISOU 1559 CG LEU A 228 6761 6725 6659 -187 -145 989 C ATOM 1560 CD1 LEU A 228 -18.677 -17.853 -2.079 1.00 55.93 C ANISOU 1560 CD1 LEU A 228 7065 7127 7060 -104 -138 860 C ATOM 1561 CD2 LEU A 228 -18.744 -18.718 0.277 1.00 48.12 C ANISOU 1561 CD2 LEU A 228 6086 6217 5981 -136 -195 1118 C ATOM 1562 N LEU A 229 -21.932 -19.274 1.644 1.00 49.36 N ANISOU 1562 N LEU A 229 6282 6529 5943 -498 -170 1214 N ATOM 1563 CA LEU A 229 -21.694 -19.695 3.023 1.00 51.65 C ANISOU 1563 CA LEU A 229 6571 6883 6171 -498 -203 1375 C ATOM 1564 C LEU A 229 -22.484 -20.953 3.349 1.00 50.11 C ANISOU 1564 C LEU A 229 6481 6580 5979 -617 -183 1493 C ATOM 1565 O LEU A 229 -21.954 -21.904 3.958 1.00 48.71 O ANISOU 1565 O LEU A 229 6374 6303 5829 -582 -200 1646 O ATOM 1566 CB LEU A 229 -22.028 -18.560 3.999 1.00 54.09 C ANISOU 1566 CB LEU A 229 6758 7448 6344 -526 -227 1356 C ATOM 1567 CG LEU A 229 -21.102 -17.331 3.975 1.00 53.90 C ANISOU 1567 CG LEU A 229 6633 7536 6309 -411 -256 1266 C ATOM 1568 CD1 LEU A 229 -21.637 -16.224 4.881 1.00 57.71 C ANISOU 1568 CD1 LEU A 229 7011 8258 6657 -459 -268 1224 C ATOM 1569 CD2 LEU A 229 -19.676 -17.703 4.400 1.00 47.46 C ANISOU 1569 CD2 LEU A 229 5823 6676 5535 -282 -298 1365 C ATOM 1570 N LYS A 230 -23.743 -21.010 2.896 1.00 50.88 N ANISOU 1570 N LYS A 230 6593 6687 6052 -760 -146 1428 N ATOM 1571 CA LYS A 230 -24.562 -22.155 3.291 1.00 56.69 C ANISOU 1571 CA LYS A 230 7421 7341 6778 -898 -126 1543 C ATOM 1572 C LYS A 230 -24.074 -23.435 2.602 1.00 54.29 C ANISOU 1572 C LYS A 230 7267 6749 6612 -869 -108 1588 C ATOM 1573 O LYS A 230 -23.957 -24.501 3.239 1.00 52.70 O ANISOU 1573 O LYS A 230 7159 6431 6433 -893 -112 1746 O ATOM 1574 CB LYS A 230 -26.040 -21.875 2.992 1.00 62.03 C ANISOU 1574 CB LYS A 230 8060 8120 7390 -1064 -92 1460 C ATOM 1575 CG LYS A 230 -27.006 -22.839 3.679 1.00 73.59 C ANISOU 1575 CG LYS A 230 9583 9572 8804 -1233 -73 1587 C ATOM 1576 CD LYS A 230 -27.340 -24.075 2.860 1.00 81.38 C ANISOU 1576 CD LYS A 230 10714 10314 9894 -1325 -41 1597 C ATOM 1577 CE LYS A 230 -28.442 -24.883 3.532 1.00 85.55 C ANISOU 1577 CE LYS A 230 11285 10859 10361 -1520 -20 1712 C ATOM 1578 NZ LYS A 230 -28.021 -25.448 4.847 1.00 88.22 N ANISOU 1578 NZ LYS A 230 11659 11201 10658 -1506 -42 1914 N ATOM 1579 N VAL A 231 -23.746 -23.341 1.308 1.00 51.49 N ANISOU 1579 N VAL A 231 6940 6273 6351 -812 -87 1451 N ATOM 1580 CA VAL A 231 -23.319 -24.533 0.576 1.00 56.13 C ANISOU 1580 CA VAL A 231 7674 6583 7070 -784 -61 1468 C ATOM 1581 C VAL A 231 -22.000 -25.057 1.127 1.00 56.00 C ANISOU 1581 C VAL A 231 7697 6462 7119 -620 -88 1597 C ATOM 1582 O VAL A 231 -21.814 -26.272 1.275 1.00 51.50 O ANISOU 1582 O VAL A 231 7255 5687 6624 -620 -77 1709 O ATOM 1583 CB VAL A 231 -23.232 -24.253 -0.939 1.00 56.23 C ANISOU 1583 CB VAL A 231 7697 6514 7153 -755 -30 1283 C ATOM 1584 CG1 VAL A 231 -22.637 -25.452 -1.672 1.00 44.81 C ANISOU 1584 CG1 VAL A 231 6401 4780 5844 -702 1 1288 C ATOM 1585 CG2 VAL A 231 -24.610 -23.973 -1.503 1.00 53.60 C ANISOU 1585 CG2 VAL A 231 7341 6262 6762 -928 -5 1178 C ATOM 1586 N GLU A 232 -21.061 -24.164 1.443 1.00 55.45 N ANISOU 1586 N GLU A 232 7518 6528 7022 -479 -125 1587 N ATOM 1587 CA GLU A 232 -19.780 -24.675 1.912 1.00 52.80 C ANISOU 1587 CA GLU A 232 7207 6105 6749 -317 -154 1709 C ATOM 1588 C GLU A 232 -19.888 -25.259 3.316 1.00 51.96 C ANISOU 1588 C GLU A 232 7123 6039 6579 -353 -188 1917 C ATOM 1589 O GLU A 232 -19.175 -26.220 3.638 1.00 50.73 O ANISOU 1589 O GLU A 232 7050 5727 6498 -262 -200 2057 O ATOM 1590 CB GLU A 232 -18.723 -23.585 1.836 1.00 53.32 C ANISOU 1590 CB GLU A 232 7146 6311 6803 -169 -186 1640 C ATOM 1591 CG GLU A 232 -18.485 -23.168 0.405 1.00 59.10 C ANISOU 1591 CG GLU A 232 7872 6974 7609 -123 -149 1458 C ATOM 1592 CD GLU A 232 -17.409 -22.128 0.274 1.00 63.05 C ANISOU 1592 CD GLU A 232 8251 7599 8105 14 -175 1393 C ATOM 1593 OE1 GLU A 232 -16.889 -21.697 1.326 1.00 64.17 O ANISOU 1593 OE1 GLU A 232 8310 7891 8181 65 -226 1482 O ATOM 1594 OE2 GLU A 232 -17.113 -21.722 -0.873 1.00 63.70 O ANISOU 1594 OE2 GLU A 232 8320 7641 8242 59 -146 1253 O ATOM 1595 N ALA A1001 -20.797 -24.736 4.150 1.00 50.06 N ANISOU 1595 N ALA A1001 5116 7128 6776 -240 2349 531 N ATOM 1596 CA ALA A1001 -21.048 -25.391 5.430 1.00 51.35 C ANISOU 1596 CA ALA A1001 5367 7198 6947 -329 2240 581 C ATOM 1597 C ALA A1001 -21.553 -26.823 5.227 1.00 56.55 C ANISOU 1597 C ALA A1001 6325 7655 7507 -383 1729 700 C ATOM 1598 O ALA A1001 -21.070 -27.770 5.880 1.00 55.71 O ANISOU 1598 O ALA A1001 6466 7465 7237 -304 1500 548 O ATOM 1599 CB ALA A1001 -22.038 -24.563 6.257 1.00 45.04 C ANISOU 1599 CB ALA A1001 4322 6367 6423 -543 2616 880 C ATOM 1600 N ASP A1002 -22.518 -27.003 4.306 1.00 60.69 N ANISOU 1600 N ASP A1002 6843 8089 8126 -522 1527 973 N ATOM 1601 CA ASP A1002 -23.011 -28.355 4.004 1.00 63.24 C ANISOU 1601 CA ASP A1002 7465 8209 8353 -617 1042 1063 C ATOM 1602 C ASP A1002 -21.900 -29.269 3.492 1.00 59.61 C ANISOU 1602 C ASP A1002 7364 7709 7575 -396 777 713 C ATOM 1603 O ASP A1002 -21.822 -30.445 3.876 1.00 60.01 O ANISOU 1603 O ASP A1002 7710 7586 7507 -384 492 659 O ATOM 1604 CB ASP A1002 -24.133 -28.312 2.967 1.00 69.04 C ANISOU 1604 CB ASP A1002 8120 8885 9226 -815 824 1380 C ATOM 1605 CG ASP A1002 -25.399 -27.717 3.502 1.00 81.27 C ANISOU 1605 CG ASP A1002 9304 10399 11176 -1043 1010 1774 C ATOM 1606 OD1 ASP A1002 -25.623 -27.820 4.726 1.00 85.70 O ANISOU 1606 OD1 ASP A1002 9818 10880 11864 -1118 1211 1823 O ATOM 1607 OD2 ASP A1002 -26.181 -27.166 2.693 1.00 88.14 O ANISOU 1607 OD2 ASP A1002 9952 11300 12239 -1145 953 2044 O ATOM 1608 N LEU A1003 -21.061 -28.756 2.589 1.00 52.17 N ANISOU 1608 N LEU A1003 6417 6890 6513 -220 901 483 N ATOM 1609 CA LEU A1003 -19.992 -29.572 2.023 1.00 52.72 C ANISOU 1609 CA LEU A1003 6805 6890 6336 0 727 143 C ATOM 1610 C LEU A1003 -19.005 -30.014 3.093 1.00 54.06 C ANISOU 1610 C LEU A1003 7003 7069 6467 211 743 -114 C ATOM 1611 O LEU A1003 -18.507 -31.148 3.057 1.00 51.89 O ANISOU 1611 O LEU A1003 7031 6632 6051 349 475 -270 O ATOM 1612 CB LEU A1003 -19.270 -28.805 0.916 1.00 51.39 C ANISOU 1612 CB LEU A1003 6608 6835 6083 136 966 -61 C ATOM 1613 CG LEU A1003 -20.071 -28.509 -0.352 1.00 53.93 C ANISOU 1613 CG LEU A1003 7033 7120 6340 -31 864 162 C ATOM 1614 CD1 LEU A1003 -19.256 -27.652 -1.300 1.00 53.51 C ANISOU 1614 CD1 LEU A1003 6990 7162 6180 119 1194 -55 C ATOM 1615 CD2 LEU A1003 -20.503 -29.800 -1.033 1.00 55.90 C ANISOU 1615 CD2 LEU A1003 7715 7138 6387 -147 390 208 C ATOM 1616 N GLU A1004 -18.702 -29.134 4.053 1.00 58.36 N ANISOU 1616 N GLU A1004 7251 7790 7132 239 1045 -157 N ATOM 1617 CA GLU A1004 -17.797 -29.546 5.118 1.00 62.35 C ANISOU 1617 CA GLU A1004 7794 8316 7580 421 982 -376 C ATOM 1618 C GLU A1004 -18.420 -30.672 5.925 1.00 59.38 C ANISOU 1618 C GLU A1004 7705 7721 7136 331 663 -182 C ATOM 1619 O GLU A1004 -17.729 -31.632 6.283 1.00 59.02 O ANISOU 1619 O GLU A1004 7894 7564 6965 529 407 -339 O ATOM 1620 CB GLU A1004 -17.460 -28.391 6.060 1.00 68.18 C ANISOU 1620 CB GLU A1004 8214 9272 8420 400 1338 -448 C ATOM 1621 CG GLU A1004 -16.826 -27.178 5.435 1.00 72.13 C ANISOU 1621 CG GLU A1004 8417 9978 9010 466 1728 -649 C ATOM 1622 CD GLU A1004 -16.416 -26.156 6.471 1.00 84.85 C ANISOU 1622 CD GLU A1004 9760 11778 10699 422 2057 -763 C ATOM 1623 OE1 GLU A1004 -16.537 -26.442 7.667 1.00 91.34 O ANISOU 1623 OE1 GLU A1004 10667 12573 11465 359 1948 -705 O ATOM 1624 OE2 GLU A1004 -16.123 -25.009 6.103 1.00 92.10 O ANISOU 1624 OE2 GLU A1004 10424 12848 11724 406 2457 -874 O ATOM 1625 N ASP A1005 -19.722 -30.561 6.242 1.00 54.21 N ANISOU 1625 N ASP A1005 7027 6979 6592 38 701 166 N ATOM 1626 CA ASP A1005 -20.371 -31.652 6.971 1.00 58.20 C ANISOU 1626 CA ASP A1005 7832 7235 7047 -80 448 351 C ATOM 1627 C ASP A1005 -20.275 -32.965 6.206 1.00 61.64 C ANISOU 1627 C ASP A1005 8631 7449 7339 -4 62 289 C ATOM 1628 O ASP A1005 -20.000 -34.021 6.793 1.00 62.24 O ANISOU 1628 O ASP A1005 9030 7334 7285 98 -167 246 O ATOM 1629 CB ASP A1005 -21.837 -31.343 7.252 1.00 64.90 C ANISOU 1629 CB ASP A1005 8551 7994 8113 -425 586 729 C ATOM 1630 CG ASP A1005 -22.014 -30.258 8.273 1.00 78.33 C ANISOU 1630 CG ASP A1005 10001 9816 9944 -521 1004 808 C ATOM 1631 OD1 ASP A1005 -21.101 -30.065 9.108 1.00 84.05 O ANISOU 1631 OD1 ASP A1005 10779 10639 10520 -368 1088 595 O ATOM 1632 OD2 ASP A1005 -23.101 -29.647 8.284 1.00 84.25 O ANISOU 1632 OD2 ASP A1005 10516 10539 10956 -762 1239 1093 O ATOM 1633 N ASN A1006 -20.526 -32.915 4.898 1.00 63.72 N ANISOU 1633 N ASN A1006 8892 7712 7606 -65 -7 295 N ATOM 1634 CA ASN A1006 -20.491 -34.120 4.074 1.00 63.36 C ANISOU 1634 CA ASN A1006 9241 7433 7401 -43 -340 223 C ATOM 1635 C ASN A1006 -19.105 -34.760 4.105 1.00 62.06 C ANISOU 1635 C ASN A1006 9284 7213 7081 327 -410 -122 C ATOM 1636 O ASN A1006 -18.965 -35.970 4.349 1.00 65.46 O ANISOU 1636 O ASN A1006 10077 7391 7405 408 -655 -155 O ATOM 1637 CB ASN A1006 -20.927 -33.758 2.649 1.00 65.09 C ANISOU 1637 CB ASN A1006 9439 7689 7603 -185 -378 272 C ATOM 1638 CG ASN A1006 -21.119 -34.967 1.760 1.00 72.14 C ANISOU 1638 CG ASN A1006 10785 8316 8309 -264 -721 228 C ATOM 1639 OD1 ASN A1006 -20.853 -36.096 2.158 1.00 85.16 O ANISOU 1639 OD1 ASN A1006 12761 9737 9861 -180 -896 142 O ATOM 1640 ND2 ASN A1006 -21.628 -34.739 0.559 1.00 73.90 N ANISOU 1640 ND2 ASN A1006 11064 8546 8467 -443 -827 303 N ATOM 1641 N TRP A1007 -18.065 -33.949 3.898 1.00 57.85 N ANISOU 1641 N TRP A1007 8504 6902 6575 560 -175 -378 N ATOM 1642 CA TRP A1007 -16.700 -34.465 3.899 1.00 60.81 C ANISOU 1642 CA TRP A1007 8973 7237 6895 930 -214 -713 C ATOM 1643 C TRP A1007 -16.319 -35.026 5.265 1.00 60.33 C ANISOU 1643 C TRP A1007 8976 7121 6825 1086 -378 -706 C ATOM 1644 O TRP A1007 -15.633 -36.054 5.357 1.00 59.54 O ANISOU 1644 O TRP A1007 9130 6828 6665 1343 -587 -843 O ATOM 1645 CB TRP A1007 -15.745 -33.353 3.462 1.00 61.08 C ANISOU 1645 CB TRP A1007 8655 7531 7023 1097 118 -978 C ATOM 1646 CG TRP A1007 -14.305 -33.735 3.356 1.00 65.38 C ANISOU 1646 CG TRP A1007 9184 8050 7606 1476 135 -1342 C ATOM 1647 CD1 TRP A1007 -13.310 -33.423 4.237 1.00 65.73 C ANISOU 1647 CD1 TRP A1007 8938 8260 7776 1710 177 -1532 C ATOM 1648 CD2 TRP A1007 -13.692 -34.498 2.312 1.00 67.88 C ANISOU 1648 CD2 TRP A1007 9771 8150 7870 1662 119 -1562 C ATOM 1649 NE1 TRP A1007 -12.116 -33.942 3.804 1.00 63.47 N ANISOU 1649 NE1 TRP A1007 8658 7883 7576 2049 176 -1845 N ATOM 1650 CE2 TRP A1007 -12.324 -34.609 2.626 1.00 66.77 C ANISOU 1650 CE2 TRP A1007 9433 8049 7889 2033 179 -1872 C ATOM 1651 CE3 TRP A1007 -14.167 -35.103 1.144 1.00 75.38 C ANISOU 1651 CE3 TRP A1007 11125 8862 8653 1537 60 -1533 C ATOM 1652 CZ2 TRP A1007 -11.427 -35.296 1.814 1.00 74.37 C ANISOU 1652 CZ2 TRP A1007 10563 8797 8896 2303 246 -2148 C ATOM 1653 CZ3 TRP A1007 -13.272 -35.786 0.337 1.00 79.60 C ANISOU 1653 CZ3 TRP A1007 11902 9179 9163 1780 132 -1821 C ATOM 1654 CH2 TRP A1007 -11.918 -35.876 0.677 1.00 80.29 C ANISOU 1654 CH2 TRP A1007 11760 9288 9458 2171 254 -2122 C ATOM 1655 N GLU A1008 -16.786 -34.383 6.337 1.00 55.88 N ANISOU 1655 N GLU A1008 8229 6695 6308 931 -280 -532 N ATOM 1656 CA GLU A1008 -16.453 -34.822 7.688 1.00 64.13 C ANISOU 1656 CA GLU A1008 9395 7691 7282 1049 -438 -509 C ATOM 1657 C GLU A1008 -17.097 -36.167 8.012 1.00 66.75 C ANISOU 1657 C GLU A1008 10201 7669 7493 983 -725 -309 C ATOM 1658 O GLU A1008 -16.443 -37.056 8.575 1.00 65.32 O ANISOU 1658 O GLU A1008 10276 7332 7212 1239 -966 -378 O ATOM 1659 CB GLU A1008 -16.887 -33.743 8.682 1.00 64.06 C ANISOU 1659 CB GLU A1008 9144 7880 7316 840 -195 -375 C ATOM 1660 CG GLU A1008 -16.547 -33.983 10.137 1.00 71.63 C ANISOU 1660 CG GLU A1008 10259 8817 8141 915 -328 -353 C ATOM 1661 CD GLU A1008 -16.988 -32.820 11.022 1.00 82.08 C ANISOU 1661 CD GLU A1008 11382 10317 9486 666 -7 -251 C ATOM 1662 OE1 GLU A1008 -17.568 -31.844 10.488 1.00 85.86 O ANISOU 1662 OE1 GLU A1008 11569 10925 10130 462 330 -183 O ATOM 1663 OE2 GLU A1008 -16.767 -32.882 12.249 1.00 85.92 O ANISOU 1663 OE2 GLU A1008 12040 10791 9814 671 -84 -230 O ATOM 1664 N THR A1009 -18.378 -36.340 7.664 1.00 71.74 N ANISOU 1664 N THR A1009 10946 8158 8154 641 -707 -53 N ATOM 1665 CA THR A1009 -19.028 -37.623 7.924 1.00 74.34 C ANISOU 1665 CA THR A1009 11728 8127 8391 535 -942 121 C ATOM 1666 C THR A1009 -18.405 -38.733 7.083 1.00 74.70 C ANISOU 1666 C THR A1009 12097 7945 8341 765 -1168 -66 C ATOM 1667 O THR A1009 -18.255 -39.872 7.557 1.00 76.71 O ANISOU 1667 O THR A1009 12752 7907 8486 891 -1373 -39 O ATOM 1668 CB THR A1009 -20.532 -37.530 7.667 1.00 76.67 C ANISOU 1668 CB THR A1009 11999 8327 8806 93 -875 415 C ATOM 1669 OG1 THR A1009 -20.758 -37.203 6.296 1.00 89.61 O ANISOU 1669 OG1 THR A1009 13489 10052 10507 -6 -875 367 O ATOM 1670 CG2 THR A1009 -21.154 -36.458 8.534 1.00 69.18 C ANISOU 1670 CG2 THR A1009 10740 7549 7998 -116 -580 605 C ATOM 1671 N LEU A1010 -18.011 -38.418 5.842 1.00 69.47 N ANISOU 1671 N LEU A1010 11307 7382 7707 829 -1098 -258 N ATOM 1672 CA LEU A1010 -17.297 -39.406 5.039 1.00 74.23 C ANISOU 1672 CA LEU A1010 12232 7749 8223 1067 -1230 -476 C ATOM 1673 C LEU A1010 -16.006 -39.848 5.721 1.00 80.41 C ANISOU 1673 C LEU A1010 13043 8494 9017 1525 -1311 -667 C ATOM 1674 O LEU A1010 -15.729 -41.049 5.820 1.00 80.03 O ANISOU 1674 O LEU A1010 13388 8121 8900 1707 -1498 -689 O ATOM 1675 CB LEU A1010 -16.998 -38.861 3.643 1.00 72.80 C ANISOU 1675 CB LEU A1010 11930 7682 8047 1064 -1071 -671 C ATOM 1676 CG LEU A1010 -16.268 -39.868 2.746 1.00 75.24 C ANISOU 1676 CG LEU A1010 12621 7703 8264 1288 -1127 -918 C ATOM 1677 CD1 LEU A1010 -17.113 -41.109 2.501 1.00 69.89 C ANISOU 1677 CD1 LEU A1010 12469 6643 7443 1059 -1361 -778 C ATOM 1678 CD2 LEU A1010 -15.848 -39.238 1.431 1.00 76.75 C ANISOU 1678 CD2 LEU A1010 12732 8000 8431 1301 -901 -1137 C ATOM 1679 N ASN A1011 -15.189 -38.890 6.178 1.00 87.17 N ANISOU 1679 N ASN A1011 13475 9667 9978 1718 -1183 -807 N ATOM 1680 CA ASN A1011 -13.937 -39.272 6.833 1.00 90.99 C ANISOU 1680 CA ASN A1011 13917 10141 10514 2155 -1323 -982 C ATOM 1681 C ASN A1011 -14.177 -40.024 8.136 1.00 88.64 C ANISOU 1681 C ASN A1011 13927 9663 10088 2196 -1594 -763 C ATOM 1682 O ASN A1011 -13.389 -40.907 8.482 1.00 89.90 O ANISOU 1682 O ASN A1011 14281 9630 10246 2556 -1817 -830 O ATOM 1683 CB ASN A1011 -13.041 -38.056 7.075 1.00 96.12 C ANISOU 1683 CB ASN A1011 14025 11181 11316 2299 -1152 -1189 C ATOM 1684 CG ASN A1011 -12.367 -37.567 5.805 1.00103.38 C ANISOU 1684 CG ASN A1011 14701 12197 12382 2410 -882 -1481 C ATOM 1685 OD1 ASN A1011 -11.875 -38.364 5.005 1.00108.91 O ANISOU 1685 OD1 ASN A1011 15612 12655 13115 2617 -892 -1639 O ATOM 1686 ND2 ASN A1011 -12.338 -36.254 5.615 1.00104.02 N ANISOU 1686 ND2 ASN A1011 14377 12598 12547 2269 -596 -1559 N ATOM 1687 N ASP A1012 -15.255 -39.714 8.859 1.00 83.77 N ANISOU 1687 N ASP A1012 13383 9071 9374 1844 -1556 -492 N ATOM 1688 CA ASP A1012 -15.581 -40.496 10.050 1.00 86.57 C ANISOU 1688 CA ASP A1012 14139 9190 9565 1843 -1765 -269 C ATOM 1689 C ASP A1012 -15.855 -41.952 9.692 1.00 89.46 C ANISOU 1689 C ASP A1012 15031 9106 9853 1895 -1938 -196 C ATOM 1690 O ASP A1012 -15.292 -42.875 10.298 1.00 94.09 O ANISOU 1690 O ASP A1012 15941 9456 10353 2200 -2173 -175 O ATOM 1691 CB ASP A1012 -16.788 -39.898 10.770 1.00 87.42 C ANISOU 1691 CB ASP A1012 14246 9351 9618 1411 -1590 0 C ATOM 1692 CG ASP A1012 -16.481 -38.572 11.408 1.00 91.32 C ANISOU 1692 CG ASP A1012 14334 10222 10142 1372 -1414 -58 C ATOM 1693 OD1 ASP A1012 -15.306 -38.351 11.763 1.00 96.18 O ANISOU 1693 OD1 ASP A1012 14783 11013 10750 1694 -1545 -260 O ATOM 1694 OD2 ASP A1012 -17.415 -37.760 11.569 1.00 91.74 O ANISOU 1694 OD2 ASP A1012 14227 10381 10250 1014 -1140 97 O ATOM 1695 N ASN A1013 -16.725 -42.175 8.705 1.00 88.04 N ANISOU 1695 N ASN A1013 14959 8791 9700 1592 -1838 -150 N ATOM 1696 CA ASN A1013 -17.043 -43.544 8.310 1.00 88.58 C ANISOU 1696 CA ASN A1013 15555 8415 9687 1578 -1975 -103 C ATOM 1697 C ASN A1013 -15.807 -44.273 7.792 1.00 91.03 C ANISOU 1697 C ASN A1013 15997 8562 10028 2050 -2074 -355 C ATOM 1698 O ASN A1013 -15.603 -45.460 8.084 1.00 93.01 O ANISOU 1698 O ASN A1013 16701 8434 10206 2248 -2231 -309 O ATOM 1699 CB ASN A1013 -18.148 -43.540 7.257 1.00 87.14 C ANISOU 1699 CB ASN A1013 15416 8163 9530 1136 -1886 -43 C ATOM 1700 CG ASN A1013 -19.467 -43.065 7.815 1.00 91.71 C ANISOU 1700 CG ASN A1013 15893 8800 10153 680 -1796 245 C ATOM 1701 OD1 ASN A1013 -19.825 -43.391 8.943 1.00100.69 O ANISOU 1701 OD1 ASN A1013 17238 9789 11233 625 -1812 436 O ATOM 1702 ND2 ASN A1013 -20.210 -42.309 7.022 1.00 91.24 N ANISOU 1702 ND2 ASN A1013 15530 8929 10206 355 -1688 289 N ATOM 1703 N LEU A1014 -14.961 -43.573 7.036 1.00 93.57 N ANISOU 1703 N LEU A1014 15929 9139 10483 2244 -1943 -619 N ATOM 1704 CA LEU A1014 -13.765 -44.212 6.502 1.00103.68 C ANISOU 1704 CA LEU A1014 17282 10247 11865 2696 -1963 -874 C ATOM 1705 C LEU A1014 -12.743 -44.502 7.591 1.00109.04 C ANISOU 1705 C LEU A1014 17891 10923 12617 3162 -2179 -879 C ATOM 1706 O LEU A1014 -12.029 -45.503 7.506 1.00111.94 O ANISOU 1706 O LEU A1014 18504 10976 13051 3540 -2285 -956 O ATOM 1707 CB LEU A1014 -13.144 -43.355 5.401 1.00105.83 C ANISOU 1707 CB LEU A1014 17163 10767 12281 2756 -1705 -1164 C ATOM 1708 CG LEU A1014 -13.981 -43.237 4.127 1.00107.21 C ANISOU 1708 CG LEU A1014 17507 10881 12348 2364 -1542 -1184 C ATOM 1709 CD1 LEU A1014 -13.336 -42.270 3.135 1.00109.52 C ANISOU 1709 CD1 LEU A1014 17442 11425 12746 2429 -1256 -1453 C ATOM 1710 CD2 LEU A1014 -14.193 -44.608 3.501 1.00106.15 C ANISOU 1710 CD2 LEU A1014 17981 10256 12095 2348 -1610 -1208 C ATOM 1711 N LYS A1015 -12.659 -43.658 8.622 1.00111.32 N ANISOU 1711 N LYS A1015 17867 11539 12891 3143 -2257 -792 N ATOM 1712 CA LYS A1015 -11.787 -43.973 9.749 1.00117.60 C ANISOU 1712 CA LYS A1015 18660 12326 13696 3543 -2553 -755 C ATOM 1713 C LYS A1015 -12.302 -45.188 10.507 1.00124.53 C ANISOU 1713 C LYS A1015 20174 12781 14361 3561 -2781 -478 C ATOM 1714 O LYS A1015 -11.512 -46.015 10.975 1.00129.78 O ANISOU 1714 O LYS A1015 21030 13225 15055 3998 -3039 -460 O ATOM 1715 CB LYS A1015 -11.667 -42.768 10.683 1.00114.34 C ANISOU 1715 CB LYS A1015 17847 12345 13250 3440 -2583 -731 C ATOM 1716 N VAL A1016 -13.626 -45.313 10.632 1.00123.88 N ANISOU 1716 N VAL A1016 20415 12562 14092 3097 -2677 -253 N ATOM 1717 CA VAL A1016 -14.203 -46.498 11.266 1.00125.00 C ANISOU 1717 CA VAL A1016 21204 12252 14039 3061 -2819 0 C ATOM 1718 C VAL A1016 -13.846 -47.752 10.475 1.00125.69 C ANISOU 1718 C VAL A1016 21660 11904 14194 3316 -2850 -95 C ATOM 1719 O VAL A1016 -13.445 -48.776 11.044 1.00131.57 O ANISOU 1719 O VAL A1016 22818 12298 14875 3643 -3052 13 O ATOM 1720 CB VAL A1016 -15.726 -46.341 11.419 1.00124.21 C ANISOU 1720 CB VAL A1016 21301 12084 13812 2470 -2636 225 C ATOM 1721 CG1 VAL A1016 -16.340 -47.622 11.956 1.00127.12 C ANISOU 1721 CG1 VAL A1016 22359 11936 14006 2400 -2719 458 C ATOM 1722 CG2 VAL A1016 -16.046 -45.174 12.340 1.00123.95 C ANISOU 1722 CG2 VAL A1016 20973 12409 13715 2253 -2557 335 C ATOM 1723 N ILE A1017 -13.986 -47.692 9.148 1.00118.19 N ANISOU 1723 N ILE A1017 20607 10943 13355 3168 -2637 -293 N ATOM 1724 CA ILE A1017 -13.631 -48.846 8.322 1.00115.26 C ANISOU 1724 CA ILE A1017 20623 10134 13036 3380 -2603 -419 C ATOM 1725 C ILE A1017 -12.132 -49.127 8.397 1.00117.99 C ANISOU 1725 C ILE A1017 20793 10442 13597 4030 -2706 -591 C ATOM 1726 O ILE A1017 -11.706 -50.288 8.423 1.00122.87 O ANISOU 1726 O ILE A1017 21818 10618 14249 4363 -2782 -571 O ATOM 1727 CB ILE A1017 -14.107 -48.643 6.871 1.00110.10 C ANISOU 1727 CB ILE A1017 19944 9489 12402 3040 -2356 -606 C ATOM 1728 CG1 ILE A1017 -15.639 -48.610 6.811 1.00106.40 C ANISOU 1728 CG1 ILE A1017 19685 8973 11768 2414 -2325 -401 C ATOM 1729 CG2 ILE A1017 -13.547 -49.719 5.958 1.00111.43 C ANISOU 1729 CG2 ILE A1017 20497 9217 12623 3287 -2261 -801 C ATOM 1730 CD1 ILE A1017 -16.198 -48.182 5.466 1.00102.10 C ANISOU 1730 CD1 ILE A1017 19045 8531 11215 2030 -2167 -541 C ATOM 1731 N GLU A1018 -11.310 -48.076 8.451 1.00116.50 N ANISOU 1731 N GLU A1018 19977 10696 13592 4224 -2702 -757 N ATOM 1732 CA GLU A1018 -9.867 -48.269 8.558 1.00119.30 C ANISOU 1732 CA GLU A1018 20053 11045 14232 4835 -2816 -924 C ATOM 1733 C GLU A1018 -9.496 -48.960 9.864 1.00124.63 C ANISOU 1733 C GLU A1018 20968 11545 14842 5193 -3213 -682 C ATOM 1734 O GLU A1018 -8.669 -49.878 9.873 1.00132.46 O ANISOU 1734 O GLU A1018 22105 12210 16014 5692 -3333 -703 O ATOM 1735 CB GLU A1018 -9.147 -46.924 8.436 1.00114.09 C ANISOU 1735 CB GLU A1018 18645 10916 13786 4896 -2732 -1150 C ATOM 1736 N LYS A1019 -10.108 -48.543 10.974 1.00123.11 N ANISOU 1736 N LYS A1019 20855 11534 14386 4950 -3404 -438 N ATOM 1737 CA LYS A1019 -9.797 -49.143 12.268 1.00130.84 C ANISOU 1737 CA LYS A1019 22141 12348 15223 5257 -3802 -185 C ATOM 1738 C LYS A1019 -10.337 -50.567 12.359 1.00137.79 C ANISOU 1738 C LYS A1019 23797 12620 15935 5290 -3821 31 C ATOM 1739 O LYS A1019 -9.573 -51.530 12.493 1.00145.00 O ANISOU 1739 O LYS A1019 24932 13190 16971 5799 -4005 71 O ATOM 1740 CB LYS A1019 -10.358 -48.274 13.397 1.00129.64 C ANISOU 1740 CB LYS A1019 21947 12523 14786 4930 -3928 -2 C ATOM 1741 N ALA A1020 -11.656 -50.720 12.290 1.00135.47 N ANISOU 1741 N ALA A1020 23909 12169 15394 4752 -3620 175 N ATOM 1742 CA ALA A1020 -12.266 -52.040 12.383 1.00139.42 C ANISOU 1742 CA ALA A1020 25162 12078 15731 4703 -3594 369 C ATOM 1743 C ALA A1020 -12.822 -52.479 11.031 1.00136.98 C ANISOU 1743 C ALA A1020 25015 11527 15504 4413 -3264 195 C ATOM 1744 O ALA A1020 -12.076 -52.924 10.158 1.00136.76 O ANISOU 1744 O ALA A1020 24943 11327 15692 4729 -3171 -21 O ATOM 1745 CB ALA A1020 -13.360 -52.046 13.439 1.00140.15 C ANISOU 1745 CB ALA A1020 25674 12090 15488 4299 -3618 679 C ATOM 1746 N ALA A1023 -14.454 -58.094 10.134 1.00148.46 N ANISOU 1746 N ALA A1023 29004 10798 16605 4054 -2692 441 N ATOM 1747 CA ALA A1023 -15.190 -57.759 8.920 1.00145.57 C ANISOU 1747 CA ALA A1023 28647 10414 16248 3571 -2500 237 C ATOM 1748 C ALA A1023 -16.686 -57.646 9.199 1.00146.93 C ANISOU 1748 C ALA A1023 29031 10560 16236 2887 -2451 399 C ATOM 1749 O ALA A1023 -17.446 -57.143 8.368 1.00143.98 O ANISOU 1749 O ALA A1023 28581 10253 15871 2413 -2376 287 O ATOM 1750 CB ALA A1023 -14.929 -58.797 7.841 1.00146.29 C ANISOU 1750 CB ALA A1023 29046 10137 16400 3601 -2255 26 C ATOM 1751 N ALA A1024 -17.097 -58.121 10.379 1.00150.19 N ANISOU 1751 N ALA A1024 29688 10877 16499 2831 -2485 663 N ATOM 1752 CA ALA A1024 -18.510 -58.089 10.746 1.00146.19 C ANISOU 1752 CA ALA A1024 29339 10331 15875 2191 -2374 819 C ATOM 1753 C ALA A1024 -19.045 -56.664 10.771 1.00140.68 C ANISOU 1753 C ALA A1024 28199 10020 15233 1886 -2433 857 C ATOM 1754 O ALA A1024 -20.152 -56.399 10.288 1.00135.75 O ANISOU 1754 O ALA A1024 27525 9403 14651 1301 -2325 854 O ATOM 1755 CB ALA A1024 -18.713 -58.761 12.105 1.00144.70 C ANISOU 1755 CB ALA A1024 29473 9993 15514 2249 -2361 1075 C ATOM 1756 N GLN A1025 -18.274 -55.732 11.334 1.00144.13 N ANISOU 1756 N GLN A1025 28287 10787 15690 2266 -2610 898 N ATOM 1757 CA GLN A1025 -18.702 -54.341 11.408 1.00145.92 C ANISOU 1757 CA GLN A1025 27999 11472 15974 1991 -2614 925 C ATOM 1758 C GLN A1025 -18.454 -53.586 10.112 1.00148.58 C ANISOU 1758 C GLN A1025 27784 12187 16483 1919 -2571 638 C ATOM 1759 O GLN A1025 -19.064 -52.531 9.898 1.00147.65 O ANISOU 1759 O GLN A1025 27188 12478 16436 1548 -2501 634 O ATOM 1760 CB GLN A1025 -17.994 -53.629 12.563 1.00145.06 C ANISOU 1760 CB GLN A1025 27650 11680 15785 2357 -2786 1047 C ATOM 1761 N VAL A1026 -17.579 -54.100 9.244 1.00150.25 N ANISOU 1761 N VAL A1026 28081 12241 16767 2267 -2578 406 N ATOM 1762 CA VAL A1026 -17.344 -53.458 7.953 1.00143.18 C ANISOU 1762 CA VAL A1026 26775 11637 15991 2181 -2490 124 C ATOM 1763 C VAL A1026 -18.615 -53.487 7.115 1.00142.43 C ANISOU 1763 C VAL A1026 26782 11480 15856 1508 -2392 107 C ATOM 1764 O VAL A1026 -19.026 -52.474 6.533 1.00137.51 O ANISOU 1764 O VAL A1026 25690 11266 15290 1203 -2365 45 O ATOM 1765 CB VAL A1026 -16.172 -54.136 7.223 1.00136.72 C ANISOU 1765 CB VAL A1026 26125 10560 15262 2682 -2445 -122 C ATOM 1766 CG1 VAL A1026 -15.986 -53.527 5.843 1.00129.12 C ANISOU 1766 CG1 VAL A1026 24852 9833 14374 2545 -2296 -420 C ATOM 1767 CG2 VAL A1026 -14.900 -54.025 8.048 1.00135.82 C ANISOU 1767 CG2 VAL A1026 25790 10554 15263 3356 -2597 -95 C ATOM 1768 N LYS A1027 -19.258 -54.656 7.046 1.00147.69 N ANISOU 1768 N LYS A1027 28062 11622 16431 1264 -2353 169 N ATOM 1769 CA LYS A1027 -20.532 -54.767 6.344 1.00150.23 C ANISOU 1769 CA LYS A1027 28485 11862 16735 582 -2317 169 C ATOM 1770 C LYS A1027 -21.586 -53.857 6.964 1.00150.16 C ANISOU 1770 C LYS A1027 28053 12191 16810 151 -2327 400 C ATOM 1771 O LYS A1027 -22.378 -53.240 6.247 1.00149.35 O ANISOU 1771 O LYS A1027 27626 12334 16787 -309 -2348 375 O ATOM 1772 CB LYS A1027 -21.008 -56.220 6.349 1.00154.59 C ANISOU 1772 CB LYS A1027 29786 11758 17191 396 -2257 202 C ATOM 1773 N ASP A1028 -21.612 -53.760 8.296 1.00152.78 N ANISOU 1773 N ASP A1028 28403 12521 17128 295 -2307 634 N ATOM 1774 CA ASP A1028 -22.589 -52.897 8.953 1.00146.93 C ANISOU 1774 CA ASP A1028 27289 12052 16486 -100 -2236 850 C ATOM 1775 C ASP A1028 -22.392 -51.441 8.549 1.00141.36 C ANISOU 1775 C ASP A1028 25853 11960 15898 -90 -2249 772 C ATOM 1776 O ASP A1028 -23.353 -50.743 8.199 1.00139.00 O ANISOU 1776 O ASP A1028 25175 11887 15750 -549 -2203 842 O ATOM 1777 CB ASP A1028 -22.492 -53.053 10.472 1.00148.31 C ANISOU 1777 CB ASP A1028 27709 12085 16557 99 -2182 1090 C ATOM 1778 N ALA A1029 -21.145 -50.965 8.596 1.00137.82 N ANISOU 1778 N ALA A1029 25183 11771 15411 436 -2306 633 N ATOM 1779 CA ALA A1029 -20.863 -49.590 8.195 1.00127.54 C ANISOU 1779 CA ALA A1029 23218 11024 14216 466 -2280 535 C ATOM 1780 C ALA A1029 -21.220 -49.361 6.731 1.00125.84 C ANISOU 1780 C ALA A1029 22841 10912 14058 176 -2285 368 C ATOM 1781 O ALA A1029 -21.796 -48.323 6.378 1.00122.62 O ANISOU 1781 O ALA A1029 21961 10864 13766 -112 -2244 413 O ATOM 1782 CB ALA A1029 -19.392 -49.257 8.451 1.00120.76 C ANISOU 1782 CB ALA A1029 22177 10372 13336 1077 -2339 379 C ATOM 1783 N LEU A1030 -20.910 -50.330 5.866 1.00127.16 N ANISOU 1783 N LEU A1030 23439 10743 14132 240 -2331 184 N ATOM 1784 CA LEU A1030 -21.206 -50.157 4.449 1.00125.95 C ANISOU 1784 CA LEU A1030 23238 10659 13958 -48 -2356 12 C ATOM 1785 C LEU A1030 -22.708 -50.151 4.187 1.00130.30 C ANISOU 1785 C LEU A1030 23763 11174 14573 -708 -2436 184 C ATOM 1786 O LEU A1030 -23.184 -49.404 3.328 1.00132.43 O ANISOU 1786 O LEU A1030 23712 11722 14885 -1000 -2499 160 O ATOM 1787 CB LEU A1030 -20.512 -51.241 3.626 1.00124.81 C ANISOU 1787 CB LEU A1030 23638 10109 13676 158 -2341 -239 C ATOM 1788 CG LEU A1030 -18.987 -51.127 3.639 1.00121.73 C ANISOU 1788 CG LEU A1030 23154 9785 13313 812 -2245 -441 C ATOM 1789 CD1 LEU A1030 -18.343 -52.294 2.916 1.00125.36 C ANISOU 1789 CD1 LEU A1030 24187 9761 13685 1029 -2162 -669 C ATOM 1790 CD2 LEU A1030 -18.554 -49.804 3.034 1.00117.31 C ANISOU 1790 CD2 LEU A1030 22021 9730 12821 880 -2172 -578 C ATOM 1791 N THR A1031 -23.475 -50.956 4.926 1.00133.37 N ANISOU 1791 N THR A1031 24468 11216 14990 -951 -2434 368 N ATOM 1792 CA THR A1031 -24.925 -50.950 4.745 1.00133.27 C ANISOU 1792 CA THR A1031 24353 11162 15122 -1593 -2500 534 C ATOM 1793 C THR A1031 -25.544 -49.664 5.275 1.00125.22 C ANISOU 1793 C THR A1031 22666 10573 14337 -1757 -2429 754 C ATOM 1794 O THR A1031 -26.485 -49.130 4.675 1.00124.56 O ANISOU 1794 O THR A1031 22231 10671 14423 -2190 -2522 838 O ATOM 1795 CB THR A1031 -25.563 -52.172 5.413 1.00139.64 C ANISOU 1795 CB THR A1031 25684 11443 15930 -1821 -2451 657 C ATOM 1796 OG1 THR A1031 -25.251 -52.181 6.813 1.00143.16 O ANISOU 1796 OG1 THR A1031 26195 11825 16375 -1518 -2292 828 O ATOM 1797 CG2 THR A1031 -25.098 -53.466 4.757 1.00142.10 C ANISOU 1797 CG2 THR A1031 26680 11282 16030 -1735 -2496 438 C ATOM 1798 N LYS A1032 -25.032 -49.144 6.393 1.00120.02 N ANISOU 1798 N LYS A1032 21834 10073 13695 -1419 -2271 852 N ATOM 1799 CA LYS A1032 -25.513 -47.852 6.870 1.00112.58 C ANISOU 1799 CA LYS A1032 20281 9530 12962 -1546 -2142 1029 C ATOM 1800 C LYS A1032 -25.221 -46.757 5.855 1.00111.79 C ANISOU 1800 C LYS A1032 19699 9875 12903 -1497 -2202 908 C ATOM 1801 O LYS A1032 -26.081 -45.910 5.574 1.00112.14 O ANISOU 1801 O LYS A1032 19279 10163 13169 -1824 -2188 1053 O ATOM 1802 CB LYS A1032 -24.879 -47.513 8.218 1.00105.57 C ANISOU 1802 CB LYS A1032 19385 8719 12009 -1185 -1974 1112 C ATOM 1803 N MET A1033 -24.012 -46.765 5.286 1.00113.03 N ANISOU 1803 N MET A1033 19961 10115 12870 -1083 -2247 650 N ATOM 1804 CA MET A1033 -23.659 -45.766 4.282 1.00114.06 C ANISOU 1804 CA MET A1033 19711 10621 13004 -1026 -2258 515 C ATOM 1805 C MET A1033 -24.513 -45.918 3.029 1.00119.99 C ANISOU 1805 C MET A1033 20518 11321 13752 -1468 -2451 511 C ATOM 1806 O MET A1033 -24.927 -44.920 2.431 1.00121.09 O ANISOU 1806 O MET A1033 20238 11780 13991 -1644 -2481 577 O ATOM 1807 CB MET A1033 -22.174 -45.877 3.944 1.00112.31 C ANISOU 1807 CB MET A1033 19634 10424 12613 -502 -2215 221 C ATOM 1808 CG MET A1033 -21.255 -45.513 5.095 1.00107.17 C ANISOU 1808 CG MET A1033 18814 9918 11986 -60 -2094 216 C ATOM 1809 SD MET A1033 -19.518 -45.776 4.698 1.00104.41 S ANISOU 1809 SD MET A1033 18578 9550 11543 558 -2065 -128 S ATOM 1810 CE MET A1033 -19.229 -44.461 3.517 1.00 99.68 C ANISOU 1810 CE MET A1033 17508 9375 10990 525 -1929 -306 C ATOM 1811 N ARG A1034 -24.799 -47.160 2.627 1.00126.63 N ANISOU 1811 N ARG A1034 21895 11752 14469 -1664 -2599 440 N ATOM 1812 CA ARG A1034 -25.649 -47.391 1.464 1.00130.50 C ANISOU 1812 CA ARG A1034 22493 12170 14921 -2140 -2843 428 C ATOM 1813 C ARG A1034 -27.067 -46.894 1.710 1.00133.73 C ANISOU 1813 C ARG A1034 22457 12710 15646 -2631 -2939 734 C ATOM 1814 O ARG A1034 -27.685 -46.306 0.817 1.00135.00 O ANISOU 1814 O ARG A1034 22347 13079 15868 -2927 -3139 796 O ATOM 1815 CB ARG A1034 -25.656 -48.877 1.102 1.00133.77 C ANISOU 1815 CB ARG A1034 23614 12075 15139 -2272 -2947 275 C ATOM 1816 N ALA A1035 -27.600 -47.116 2.915 1.00133.28 N ANISOU 1816 N ALA A1035 22321 12514 15805 -2716 -2788 938 N ATOM 1817 CA ALA A1035 -28.926 -46.594 3.234 1.00129.49 C ANISOU 1817 CA ALA A1035 21355 12137 15709 -3155 -2794 1232 C ATOM 1818 C ALA A1035 -28.932 -45.071 3.223 1.00124.68 C ANISOU 1818 C ALA A1035 20084 12006 15284 -3040 -2685 1358 C ATOM 1819 O ALA A1035 -29.847 -44.452 2.664 1.00125.32 O ANISOU 1819 O ALA A1035 19733 12268 15613 -3373 -2835 1527 O ATOM 1820 CB ALA A1035 -29.392 -47.126 4.588 1.00127.92 C ANISOU 1820 CB ALA A1035 21270 11649 15683 -3239 -2553 1405 C ATOM 1821 N ALA A1036 -27.914 -44.451 3.829 1.00121.98 N ANISOU 1821 N ALA A1036 19648 11863 14835 -2573 -2435 1281 N ATOM 1822 CA ALA A1036 -27.826 -42.995 3.823 1.00118.31 C ANISOU 1822 CA ALA A1036 18600 11830 14523 -2452 -2282 1370 C ATOM 1823 C ALA A1036 -27.749 -42.456 2.401 1.00123.70 C ANISOU 1823 C ALA A1036 19150 12741 15110 -2502 -2504 1281 C ATOM 1824 O ALA A1036 -28.371 -41.435 2.079 1.00123.80 O ANISOU 1824 O ALA A1036 18664 13021 15354 -2659 -2509 1466 O ATOM 1825 CB ALA A1036 -26.616 -42.541 4.637 1.00110.64 C ANISOU 1825 CB ALA A1036 17625 11009 13404 -1955 -2017 1239 C ATOM 1826 N ALA A1037 -26.998 -43.137 1.532 1.00131.10 N ANISOU 1826 N ALA A1037 20565 13546 15702 -2368 -2668 1007 N ATOM 1827 CA ALA A1037 -26.874 -42.702 0.146 1.00143.33 C ANISOU 1827 CA ALA A1037 22121 15259 17078 -2427 -2859 902 C ATOM 1828 C ALA A1037 -28.185 -42.881 -0.609 1.00162.87 C ANISOU 1828 C ALA A1037 24530 17678 19673 -2968 -3229 1089 C ATOM 1829 O ALA A1037 -28.552 -42.036 -1.434 1.00166.22 O ANISOU 1829 O ALA A1037 24671 18353 20130 -3097 -3386 1192 O ATOM 1830 CB ALA A1037 -25.747 -43.470 -0.543 1.00141.10 C ANISOU 1830 CB ALA A1037 22429 14781 16403 -2164 -2873 547 C ATOM 1831 N LEU A1038 -28.899 -43.979 -0.345 1.00179.60 N ANISOU 1831 N LEU A1038 26911 19462 21866 -3296 -3387 1140 N ATOM 1832 CA LEU A1038 -30.194 -44.193 -0.983 1.00182.42 C ANISOU 1832 CA LEU A1038 27150 19761 22400 -3853 -3773 1317 C ATOM 1833 C LEU A1038 -31.185 -43.113 -0.577 1.00180.65 C ANISOU 1833 C LEU A1038 26157 19809 22672 -4025 -3737 1675 C ATOM 1834 O LEU A1038 -31.949 -42.615 -1.413 1.00184.23 O ANISOU 1834 O LEU A1038 26312 20428 23257 -4312 -4066 1838 O ATOM 1835 CB LEU A1038 -30.732 -45.581 -0.630 1.00186.60 C ANISOU 1835 CB LEU A1038 28087 19852 22961 -4173 -3873 1286 C ATOM 1836 N ASP A1039 -31.182 -42.727 0.703 1.00168.97 N ANISOU 1836 N ASP A1039 24367 18363 21471 -3847 -3334 1810 N ATOM 1837 CA ASP A1039 -32.053 -41.645 1.141 1.00152.68 C ANISOU 1837 CA ASP A1039 21581 16526 19904 -3970 -3194 2139 C ATOM 1838 C ASP A1039 -31.613 -40.292 0.596 1.00140.67 C ANISOU 1838 C ASP A1039 19703 15403 18342 -3707 -3131 2174 C ATOM 1839 O ASP A1039 -32.428 -39.364 0.547 1.00138.78 O ANISOU 1839 O ASP A1039 18873 15356 18502 -3847 -3126 2461 O ATOM 1840 CB ASP A1039 -32.120 -41.598 2.669 1.00143.24 C ANISOU 1840 CB ASP A1039 20248 15218 18957 -3864 -2722 2248 C ATOM 1841 CG ASP A1039 -32.861 -42.785 3.254 1.00143.75 C ANISOU 1841 CG ASP A1039 20563 14873 19181 -4207 -2736 2301 C ATOM 1842 OD1 ASP A1039 -33.748 -43.332 2.565 1.00147.55 O ANISOU 1842 OD1 ASP A1039 21022 15223 19816 -4638 -3097 2365 O ATOM 1843 OD2 ASP A1039 -32.567 -43.163 4.409 1.00142.76 O ANISOU 1843 OD2 ASP A1039 20670 14549 19022 -4061 -2392 2283 O ATOM 1844 N ALA A1040 -30.351 -40.159 0.180 1.00133.73 N ANISOU 1844 N ALA A1040 19160 14626 17024 -3327 -3055 1892 N ATOM 1845 CA ALA A1040 -29.880 -38.899 -0.385 1.00129.10 C ANISOU 1845 CA ALA A1040 18292 14384 16375 -3087 -2955 1897 C ATOM 1846 C ALA A1040 -30.436 -38.640 -1.779 1.00134.82 C ANISOU 1846 C ALA A1040 18993 15211 17021 -3339 -3396 1991 C ATOM 1847 O ALA A1040 -30.450 -37.486 -2.221 1.00134.39 O ANISOU 1847 O ALA A1040 18595 15430 17037 -3233 -3344 2121 O ATOM 1848 CB ALA A1040 -28.352 -38.878 -0.428 1.00122.97 C ANISOU 1848 CB ALA A1040 17872 13658 15194 -2626 -2719 1547 C ATOM 1849 N GLN A1041 -30.891 -39.678 -2.477 1.00141.48 N ANISOU 1849 N GLN A1041 20227 15829 17700 -3677 -3832 1931 N ATOM 1850 CA GLN A1041 -31.397 -39.522 -3.835 1.00148.07 C ANISOU 1850 CA GLN A1041 21140 16742 18378 -3950 -4326 2004 C ATOM 1851 C GLN A1041 -32.744 -38.802 -3.847 1.00152.32 C ANISOU 1851 C GLN A1041 20984 17442 19450 -4250 -4559 2432 C ATOM 1852 O GLN A1041 -33.446 -38.758 -2.835 1.00153.22 O ANISOU 1852 O GLN A1041 20635 17508 20073 -4355 -4366 2645 O ATOM 1853 CB GLN A1041 -31.522 -40.886 -4.519 1.00153.83 C ANISOU 1853 CB GLN A1041 22521 17157 18771 -4274 -4726 1798 C ATOM 1854 N MET A1058 -28.517 -35.384 -10.148 1.00141.93 N ANISOU 1854 N MET A1058 21733 16764 15432 -3211 -4531 1644 N ATOM 1855 CA MET A1058 -27.278 -36.116 -10.375 1.00146.39 C ANISOU 1855 CA MET A1058 22955 17105 15562 -3018 -4206 1166 C ATOM 1856 C MET A1058 -27.481 -37.609 -10.148 1.00158.28 C ANISOU 1856 C MET A1058 24831 18309 16998 -3266 -4450 994 C ATOM 1857 O MET A1058 -26.875 -38.198 -9.251 1.00157.18 O ANISOU 1857 O MET A1058 24675 18048 16999 -3051 -4111 788 O ATOM 1858 CB MET A1058 -26.169 -35.586 -9.464 1.00137.96 C ANISOU 1858 CB MET A1058 21582 16139 14695 -2531 -3509 971 C ATOM 1859 N LYS A1059 -28.340 -38.215 -10.972 1.00172.89 N ANISOU 1859 N LYS A1059 27034 20031 18624 -3729 -5058 1086 N ATOM 1860 CA LYS A1059 -28.635 -39.637 -10.823 1.00179.87 C ANISOU 1860 CA LYS A1059 28297 20603 19441 -4029 -5306 930 C ATOM 1861 C LYS A1059 -27.403 -40.492 -11.094 1.00184.05 C ANISOU 1861 C LYS A1059 29578 20820 19531 -3821 -4940 452 C ATOM 1862 O LYS A1059 -27.144 -41.466 -10.375 1.00185.62 O ANISOU 1862 O LYS A1059 29898 20785 19843 -3766 -4779 281 O ATOM 1863 CB LYS A1059 -29.781 -40.034 -11.755 1.00186.90 C ANISOU 1863 CB LYS A1059 29430 21431 20152 -4605 -6059 1105 C ATOM 1864 N ASP A1060 -26.626 -40.142 -12.123 1.00186.71 N ANISOU 1864 N ASP A1060 30438 21121 19383 -3691 -4773 239 N ATOM 1865 CA ASP A1060 -25.428 -40.913 -12.442 1.00186.82 C ANISOU 1865 CA ASP A1060 31150 20807 19027 -3477 -4361 -221 C ATOM 1866 C ASP A1060 -24.381 -40.796 -11.339 1.00180.00 C ANISOU 1866 C ASP A1060 29904 19981 18507 -2935 -3740 -384 C ATOM 1867 O ASP A1060 -23.680 -41.767 -11.035 1.00180.98 O ANISOU 1867 O ASP A1060 30367 19809 18588 -2770 -3490 -674 O ATOM 1868 CB ASP A1060 -24.853 -40.461 -13.785 1.00189.23 C ANISOU 1868 CB ASP A1060 32082 21054 18762 -3467 -4252 -401 C ATOM 1869 N PHE A1061 -24.268 -39.619 -10.716 1.00173.34 N ANISOU 1869 N PHE A1061 28358 19489 18012 -2656 -3499 -195 N ATOM 1870 CA PHE A1061 -23.310 -39.441 -9.626 1.00164.16 C ANISOU 1870 CA PHE A1061 26802 18396 17174 -2177 -2974 -338 C ATOM 1871 C PHE A1061 -23.684 -40.299 -8.422 1.00158.53 C ANISOU 1871 C PHE A1061 25862 17574 16796 -2206 -3071 -259 C ATOM 1872 O PHE A1061 -22.832 -40.988 -7.838 1.00158.66 O ANISOU 1872 O PHE A1061 26022 17401 16860 -1912 -2787 -501 O ATOM 1873 CB PHE A1061 -23.235 -37.964 -9.234 1.00162.57 C ANISOU 1873 CB PHE A1061 25925 18587 17255 -1952 -2724 -142 C ATOM 1874 N ARG A1062 -24.961 -40.256 -8.029 1.00153.11 N ANISOU 1874 N ARG A1062 24814 16992 16370 -2550 -3461 92 N ATOM 1875 CA ARG A1062 -25.429 -41.088 -6.926 1.00147.44 C ANISOU 1875 CA ARG A1062 23937 16129 15952 -2636 -3537 184 C ATOM 1876 C ARG A1062 -25.248 -42.567 -7.242 1.00146.35 C ANISOU 1876 C ARG A1062 24514 15559 15535 -2779 -3658 -71 C ATOM 1877 O ARG A1062 -24.856 -43.354 -6.370 1.00142.42 O ANISOU 1877 O ARG A1062 24097 14855 15161 -2594 -3476 -175 O ATOM 1878 CB ARG A1062 -26.894 -40.774 -6.617 1.00146.30 C ANISOU 1878 CB ARG A1062 23295 16135 16157 -3032 -3911 596 C ATOM 1879 N HIS A1063 -25.504 -42.960 -8.494 1.00147.62 N ANISOU 1879 N HIS A1063 25243 15556 15291 -3105 -3956 -175 N ATOM 1880 CA HIS A1063 -25.322 -44.354 -8.885 1.00148.38 C ANISOU 1880 CA HIS A1063 26088 15203 15087 -3270 -4030 -444 C ATOM 1881 C HIS A1063 -23.854 -44.761 -8.830 1.00145.00 C ANISOU 1881 C HIS A1063 26031 14553 14509 -2775 -3510 -817 C ATOM 1882 O HIS A1063 -23.535 -45.885 -8.435 1.00144.68 O ANISOU 1882 O HIS A1063 26346 14159 14466 -2700 -3402 -982 O ATOM 1883 CB HIS A1063 -25.892 -44.588 -10.284 1.00153.10 C ANISOU 1883 CB HIS A1063 27256 15682 15233 -3754 -4460 -489 C ATOM 1884 N GLY A1064 -22.946 -43.862 -9.213 1.00141.91 N ANISOU 1884 N GLY A1064 25545 14348 14029 -2427 -3167 -948 N ATOM 1885 CA GLY A1064 -21.528 -44.183 -9.140 1.00142.18 C ANISOU 1885 CA GLY A1064 25821 14184 14017 -1939 -2654 -1299 C ATOM 1886 C GLY A1064 -21.050 -44.370 -7.712 1.00139.34 C ANISOU 1886 C GLY A1064 25005 13862 14077 -1540 -2436 -1263 C ATOM 1887 O GLY A1064 -20.314 -45.314 -7.404 1.00139.50 O ANISOU 1887 O GLY A1064 25335 13558 14112 -1279 -2230 -1478 O ATOM 1888 N PHE A1065 -21.468 -43.468 -6.816 1.00135.72 N ANISOU 1888 N PHE A1065 23829 13782 13957 -1487 -2478 -981 N ATOM 1889 CA PHE A1065 -21.103 -43.618 -5.407 1.00129.92 C ANISOU 1889 CA PHE A1065 22709 13088 13569 -1160 -2319 -922 C ATOM 1890 C PHE A1065 -21.687 -44.900 -4.822 1.00131.20 C ANISOU 1890 C PHE A1065 23169 12909 13771 -1351 -2536 -846 C ATOM 1891 O PHE A1065 -21.003 -45.635 -4.097 1.00133.17 O ANISOU 1891 O PHE A1065 23553 12937 14107 -1028 -2371 -958 O ATOM 1892 CB PHE A1065 -21.568 -42.402 -4.605 1.00124.75 C ANISOU 1892 CB PHE A1065 21307 12867 13227 -1148 -2309 -631 C ATOM 1893 N ASP A1066 -22.950 -45.192 -5.136 1.00132.66 N ANISOU 1893 N ASP A1066 23463 13033 13908 -1879 -2912 -650 N ATOM 1894 CA ASP A1066 -23.570 -46.411 -4.636 1.00139.05 C ANISOU 1894 CA ASP A1066 24577 13492 14764 -2120 -3093 -588 C ATOM 1895 C ASP A1066 -22.908 -47.654 -5.221 1.00147.41 C ANISOU 1895 C ASP A1066 26410 14071 15527 -2047 -2998 -910 C ATOM 1896 O ASP A1066 -22.851 -48.689 -4.558 1.00152.50 O ANISOU 1896 O ASP A1066 27325 14381 16238 -1982 -2954 -931 O ATOM 1897 CB ASP A1066 -25.066 -46.385 -4.954 1.00143.55 C ANISOU 1897 CB ASP A1066 25038 14115 15391 -2737 -3523 -329 C ATOM 1898 CG ASP A1066 -25.844 -47.499 -4.272 1.00149.11 C ANISOU 1898 CG ASP A1066 25925 14490 16238 -3031 -3671 -224 C ATOM 1899 OD1 ASP A1066 -25.246 -48.321 -3.550 1.00150.60 O ANISOU 1899 OD1 ASP A1066 26386 14393 16444 -2750 -3449 -333 O ATOM 1900 OD2 ASP A1066 -27.075 -47.557 -4.473 1.00152.68 O ANISOU 1900 OD2 ASP A1066 26248 14959 16806 -3551 -4018 -24 O ATOM 1901 N ILE A1067 -22.399 -47.577 -6.451 1.00150.48 N ANISOU 1901 N ILE A1067 27205 14387 15584 -2054 -2925 -1159 N ATOM 1902 CA ILE A1067 -21.708 -48.722 -7.035 1.00150.89 C ANISOU 1902 CA ILE A1067 28020 13947 15367 -1965 -2747 -1487 C ATOM 1903 C ILE A1067 -20.361 -48.930 -6.362 1.00147.13 C ANISOU 1903 C ILE A1067 27470 13359 15075 -1306 -2315 -1662 C ATOM 1904 O ILE A1067 -19.929 -50.068 -6.158 1.00150.08 O ANISOU 1904 O ILE A1067 28297 13293 15432 -1144 -2178 -1808 O ATOM 1905 CB ILE A1067 -21.561 -48.543 -8.556 1.00154.71 C ANISOU 1905 CB ILE A1067 29010 14358 15415 -2185 -2750 -1709 C ATOM 1906 N LEU A1068 -19.675 -47.836 -6.022 1.00135.64 N ANISOU 1906 N LEU A1068 25439 12287 13813 -920 -2102 -1648 N ATOM 1907 CA LEU A1068 -18.510 -47.931 -5.146 1.00123.24 C ANISOU 1907 CA LEU A1068 23627 10691 12508 -312 -1794 -1749 C ATOM 1908 C LEU A1068 -18.864 -48.651 -3.849 1.00117.95 C ANISOU 1908 C LEU A1068 22884 9885 12047 -251 -1941 -1540 C ATOM 1909 O LEU A1068 -18.163 -49.581 -3.425 1.00116.23 O ANISOU 1909 O LEU A1068 22946 9320 11897 93 -1799 -1652 O ATOM 1910 CB LEU A1068 -17.958 -46.529 -4.875 1.00113.16 C ANISOU 1910 CB LEU A1068 21662 9906 11427 -25 -1618 -1722 C ATOM 1911 CG LEU A1068 -17.272 -45.851 -6.063 1.00110.00 C ANISOU 1911 CG LEU A1068 21360 9580 10854 54 -1335 -1979 C ATOM 1912 CD1 LEU A1068 -16.959 -44.378 -5.832 1.00100.23 C ANISOU 1912 CD1 LEU A1068 19442 8840 9800 226 -1182 -1916 C ATOM 1913 CD2 LEU A1068 -15.972 -46.608 -6.302 1.00114.90 C ANISOU 1913 CD2 LEU A1068 22318 9827 11513 499 -955 -2322 C ATOM 1914 N VAL A1069 -19.971 -48.244 -3.221 1.00115.88 N ANISOU 1914 N VAL A1069 22270 9861 11896 -585 -2206 -1225 N ATOM 1915 CA VAL A1069 -20.397 -48.863 -1.965 1.00114.07 C ANISOU 1915 CA VAL A1069 22004 9492 11845 -576 -2308 -1009 C ATOM 1916 C VAL A1069 -20.712 -50.345 -2.162 1.00117.32 C ANISOU 1916 C VAL A1069 23123 9346 12107 -774 -2382 -1079 C ATOM 1917 O VAL A1069 -20.332 -51.187 -1.344 1.00117.00 O ANISOU 1917 O VAL A1069 23301 9006 12148 -496 -2302 -1061 O ATOM 1918 CB VAL A1069 -21.595 -48.096 -1.370 1.00109.08 C ANISOU 1918 CB VAL A1069 20871 9190 11386 -948 -2507 -671 C ATOM 1919 CG1 VAL A1069 -22.150 -48.820 -0.148 1.00110.37 C ANISOU 1919 CG1 VAL A1069 21106 9135 11696 -1018 -2569 -455 C ATOM 1920 CG2 VAL A1069 -21.173 -46.683 -0.984 1.00102.29 C ANISOU 1920 CG2 VAL A1069 19342 8831 10694 -691 -2365 -607 C ATOM 1921 N GLY A1070 -21.407 -50.685 -3.247 1.00119.58 N ANISOU 1921 N GLY A1070 23805 9473 12159 -1263 -2544 -1158 N ATOM 1922 CA GLY A1070 -21.762 -52.073 -3.490 1.00124.32 C ANISOU 1922 CA GLY A1070 25105 9530 12602 -1520 -2603 -1247 C ATOM 1923 C GLY A1070 -20.556 -52.938 -3.801 1.00130.49 C ANISOU 1923 C GLY A1070 26425 9884 13272 -1080 -2288 -1549 C ATOM 1924 O GLY A1070 -20.486 -54.094 -3.377 1.00133.67 O ANISOU 1924 O GLY A1070 27281 9824 13684 -1005 -2218 -1569 O ATOM 1925 N GLN A1071 -19.583 -52.388 -4.533 1.00130.54 N ANISOU 1925 N GLN A1071 26387 10011 13201 -770 -2054 -1783 N ATOM 1926 CA GLN A1071 -18.344 -53.114 -4.792 1.00131.47 C ANISOU 1926 CA GLN A1071 26914 9729 13308 -286 -1686 -2070 C ATOM 1927 C GLN A1071 -17.578 -53.358 -3.497 1.00131.40 C ANISOU 1927 C GLN A1071 26612 9684 13629 312 -1574 -1963 C ATOM 1928 O GLN A1071 -17.052 -54.455 -3.268 1.00130.01 O ANISOU 1928 O GLN A1071 26823 9070 13505 596 -1408 -2032 O ATOM 1929 CB GLN A1071 -17.486 -52.340 -5.797 1.00126.94 C ANISOU 1929 CB GLN A1071 26235 9349 12646 -91 -1409 -2318 C ATOM 1930 N ILE A1072 -17.520 -52.344 -2.625 1.00130.87 N ANISOU 1930 N ILE A1072 25829 10111 13785 500 -1668 -1763 N ATOM 1931 CA ILE A1072 -16.850 -52.512 -1.337 1.00132.90 C ANISOU 1931 CA ILE A1072 25817 10370 14309 1026 -1641 -1637 C ATOM 1932 C ILE A1072 -17.589 -53.530 -0.477 1.00142.00 C ANISOU 1932 C ILE A1072 27328 11179 15447 861 -1808 -1411 C ATOM 1933 O ILE A1072 -16.973 -54.364 0.199 1.00144.03 O ANISOU 1933 O ILE A1072 27819 11100 15805 1279 -1738 -1388 O ATOM 1934 CB ILE A1072 -16.724 -51.157 -0.620 1.00125.85 C ANISOU 1934 CB ILE A1072 24135 10080 13602 1171 -1710 -1486 C ATOM 1935 N ASP A1073 -18.922 -53.490 -0.501 1.00150.23 N ANISOU 1935 N ASP A1073 28421 12277 16384 252 -2024 -1234 N ATOM 1936 CA ASP A1073 -19.707 -54.374 0.348 1.00154.50 C ANISOU 1936 CA ASP A1073 29267 12498 16938 39 -2140 -1014 C ATOM 1937 C ASP A1073 -19.640 -55.809 -0.163 1.00157.74 C ANISOU 1937 C ASP A1073 30482 12255 17195 -23 -2031 -1180 C ATOM 1938 O ASP A1073 -19.740 -56.756 0.625 1.00162.01 O ANISOU 1938 O ASP A1073 31343 12441 17773 75 -2002 -1047 O ATOM 1939 CB ASP A1073 -21.151 -53.861 0.415 1.00155.81 C ANISOU 1939 CB ASP A1073 29175 12913 17114 -610 -2367 -793 C ATOM 1940 CG ASP A1073 -21.959 -54.492 1.541 1.00160.10 C ANISOU 1940 CG ASP A1073 29863 13218 17749 -804 -2427 -526 C ATOM 1941 OD1 ASP A1073 -21.415 -55.342 2.276 1.00164.06 O ANISOU 1941 OD1 ASP A1073 30722 13356 18256 -436 -2319 -495 O ATOM 1942 OD2 ASP A1073 -23.143 -54.120 1.699 1.00160.36 O ANISOU 1942 OD2 ASP A1073 29645 13414 17869 -1317 -2569 -334 O ATOM 1943 N ASP A1074 -19.432 -55.987 -1.470 1.00157.10 N ANISOU 1943 N ASP A1074 30693 12068 16929 -172 -1922 -1454 N ATOM 1944 CA ASP A1074 -19.189 -57.319 -2.011 1.00158.51 C ANISOU 1944 CA ASP A1074 31376 11871 16978 -167 -1702 -1580 C ATOM 1945 C ASP A1074 -17.798 -57.819 -1.630 1.00159.34 C ANISOU 1945 C ASP A1074 31495 11789 17257 571 -1411 -1660 C ATOM 1946 O ASP A1074 -17.642 -58.956 -1.168 1.00162.62 O ANISOU 1946 O ASP A1074 32220 11858 17709 739 -1296 -1589 O ATOM 1947 CB ASP A1074 -19.365 -57.305 -3.530 1.00155.39 C ANISOU 1947 CB ASP A1074 31207 11518 16317 -555 -1644 -1807 C ATOM 1948 N ALA A1075 -16.772 -56.981 -1.817 1.00157.53 N ANISOU 1948 N ALA A1075 30896 11793 17167 1019 -1286 -1803 N ATOM 1949 CA ALA A1075 -15.417 -57.357 -1.418 1.00158.97 C ANISOU 1949 CA ALA A1075 30948 11848 17604 1735 -1047 -1864 C ATOM 1950 C ALA A1075 -15.330 -57.654 0.075 1.00157.44 C ANISOU 1950 C ALA A1075 30653 11582 17586 2085 -1225 -1586 C ATOM 1951 O ALA A1075 -14.442 -58.395 0.512 1.00161.91 O ANISOU 1951 O ALA A1075 31254 11932 18332 2596 -1091 -1563 O ATOM 1952 CB ALA A1075 -14.429 -56.252 -1.796 1.00158.54 C ANISOU 1952 CB ALA A1075 30397 12124 17716 2101 -906 -2054 C ATOM 1953 N LEU A1076 -16.232 -57.078 0.870 1.00152.08 N ANISOU 1953 N LEU A1076 29839 11083 16864 1812 -1519 -1358 N ATOM 1954 CA LEU A1076 -16.317 -57.427 2.284 1.00148.80 C ANISOU 1954 CA LEU A1076 29416 10586 16534 2040 -1675 -1060 C ATOM 1955 C LEU A1076 -17.036 -58.758 2.479 1.00149.85 C ANISOU 1955 C LEU A1076 30080 10326 16531 1743 -1625 -935 C ATOM 1956 O LEU A1076 -16.464 -59.712 3.017 1.00151.73 O ANISOU 1956 O LEU A1076 30523 10293 16833 2129 -1529 -857 O ATOM 1957 CB LEU A1076 -17.027 -56.314 3.062 1.00143.07 C ANISOU 1957 CB LEU A1076 28280 10257 15823 1811 -1924 -844 C ATOM 1958 N LYS A1077 -18.294 -58.844 2.032 1.00147.73 N ANISOU 1958 N LYS A1077 30012 10025 16092 1049 -1693 -917 N ATOM 1959 CA LYS A1077 -19.087 -60.047 2.259 1.00149.62 C ANISOU 1959 CA LYS A1077 30706 9920 16222 710 -1639 -806 C ATOM 1960 C LYS A1077 -18.461 -61.290 1.633 1.00155.35 C ANISOU 1960 C LYS A1077 31874 10257 16896 907 -1364 -980 C ATOM 1961 O LYS A1077 -18.773 -62.406 2.064 1.00158.83 O ANISOU 1961 O LYS A1077 32696 10362 17289 843 -1269 -875 O ATOM 1962 CB LYS A1077 -20.508 -59.846 1.727 1.00145.38 C ANISOU 1962 CB LYS A1077 30207 9465 15566 -89 -1778 -795 C ATOM 1963 N LEU A1078 -17.589 -61.128 0.639 1.00156.60 N ANISOU 1963 N LEU A1078 31991 10439 17073 1137 -1191 -1242 N ATOM 1964 CA LEU A1078 -16.844 -62.261 0.084 1.00162.76 C ANISOU 1964 CA LEU A1078 33142 10837 17863 1394 -868 -1401 C ATOM 1965 C LEU A1078 -15.955 -62.908 1.142 1.00165.47 C ANISOU 1965 C LEU A1078 33474 10973 18425 2052 -799 -1237 C ATOM 1966 O LEU A1078 -15.381 -62.221 1.988 1.00163.51 O ANISOU 1966 O LEU A1078 32806 10964 18356 2494 -962 -1105 O ATOM 1967 CB LEU A1078 -15.992 -61.826 -1.114 1.00163.77 C ANISOU 1967 CB LEU A1078 33144 11065 18016 1549 -647 -1702 C ATOM 1968 CG LEU A1078 -15.184 -62.947 -1.774 1.00169.27 C ANISOU 1968 CG LEU A1078 34198 11355 18761 1798 -250 -1881 C ATOM 1969 CD1 LEU A1078 -16.119 -64.018 -2.303 1.00175.38 C ANISOU 1969 CD1 LEU A1078 35583 11798 19255 1230 -172 -1917 C ATOM 1970 CD2 LEU A1078 -14.284 -62.409 -2.888 1.00166.84 C ANISOU 1970 CD2 LEU A1078 33702 11170 18518 1968 18 -2169 C ATOM 1971 N VAL A1084 -10.734 -58.419 3.722 1.00133.59 N ANISOU 1971 N VAL A1084 26434 8561 15764 4897 -1386 -1190 N ATOM 1972 CA VAL A1084 -10.580 -57.239 4.561 1.00126.64 C ANISOU 1972 CA VAL A1084 25036 8134 14948 5066 -1700 -1086 C ATOM 1973 C VAL A1084 -9.597 -56.268 3.920 1.00146.91 C ANISOU 1973 C VAL A1084 26991 11024 17805 5342 -1552 -1371 C ATOM 1974 O VAL A1084 -9.670 -55.061 4.143 1.00141.21 O ANISOU 1974 O VAL A1084 25856 10713 17085 5301 -1704 -1399 O ATOM 1975 CB VAL A1084 -10.125 -57.616 5.979 1.00129.23 C ANISOU 1975 CB VAL A1084 25274 8467 15360 5497 -2015 -786 C ATOM 1976 N LYS A1085 -8.673 -56.799 3.118 1.00151.64 N ANISOU 1976 N LYS A1085 27521 11423 18671 5606 -1210 -1586 N ATOM 1977 CA LYS A1085 -7.730 -55.939 2.411 1.00154.98 C ANISOU 1977 CA LYS A1085 27364 12120 19399 5814 -971 -1878 C ATOM 1978 C LYS A1085 -8.391 -55.250 1.221 1.00154.79 C ANISOU 1978 C LYS A1085 27477 12217 19118 5287 -726 -2114 C ATOM 1979 O LYS A1085 -8.310 -54.024 1.078 1.00151.65 O ANISOU 1979 O LYS A1085 26640 12229 18751 5235 -739 -2232 O ATOM 1980 CB LYS A1085 -6.518 -56.755 1.956 1.00161.37 C ANISOU 1980 CB LYS A1085 28040 12639 20635 6244 -635 -2019 C ATOM 1981 N GLU A1086 -9.068 -56.027 0.369 1.00160.18 N ANISOU 1981 N GLU A1086 28773 12558 19529 4871 -517 -2176 N ATOM 1982 CA GLU A1086 -9.629 -55.478 -0.863 1.00158.16 C ANISOU 1982 CA GLU A1086 28685 12402 19007 4359 -303 -2393 C ATOM 1983 C GLU A1086 -10.743 -54.476 -0.578 1.00152.32 C ANISOU 1983 C GLU A1086 27915 11983 17976 3935 -623 -2277 C ATOM 1984 O GLU A1086 -10.809 -53.416 -1.211 1.00150.82 O ANISOU 1984 O GLU A1086 27478 12106 17721 3746 -533 -2435 O ATOM 1985 CB GLU A1086 -10.141 -56.610 -1.754 1.00162.02 C ANISOU 1985 CB GLU A1086 29858 12461 19243 3983 -81 -2460 C ATOM 1986 N ALA A1087 -11.622 -54.785 0.379 1.00149.99 N ANISOU 1986 N ALA A1087 27859 11604 17527 3774 -971 -1993 N ATOM 1987 CA ALA A1087 -12.739 -53.890 0.676 1.00141.31 C ANISOU 1987 CA ALA A1087 26602 10873 16217 3286 -1237 -1828 C ATOM 1988 C ALA A1087 -12.257 -52.597 1.329 1.00135.85 C ANISOU 1988 C ALA A1087 25102 10791 15722 3506 -1346 -1772 C ATOM 1989 O ALA A1087 -12.687 -51.498 0.951 1.00129.33 O ANISOU 1989 O ALA A1087 23919 10404 14816 3172 -1339 -1796 O ATOM 1990 CB ALA A1087 -13.757 -54.600 1.569 1.00137.76 C ANISOU 1990 CB ALA A1087 26517 10216 15609 3016 -1499 -1516 C ATOM 1991 N GLN A1088 -11.360 -52.709 2.313 1.00139.80 N ANISOU 1991 N GLN A1088 25319 11319 16481 4065 -1460 -1692 N ATOM 1992 CA GLN A1088 -10.820 -51.515 2.956 1.00141.26 C ANISOU 1992 CA GLN A1088 24756 12065 16853 4270 -1573 -1670 C ATOM 1993 C GLN A1088 -10.057 -50.651 1.960 1.00146.19 C ANISOU 1993 C GLN A1088 24960 12934 17652 4365 -1259 -1997 C ATOM 1994 O GLN A1088 -10.101 -49.417 2.037 1.00141.90 O ANISOU 1994 O GLN A1088 23882 12899 17134 4221 -1264 -2014 O ATOM 1995 CB GLN A1088 -9.919 -51.910 4.128 1.00143.83 C ANISOU 1995 CB GLN A1088 24906 12328 17415 4865 -1803 -1541 C ATOM 1996 N ALA A1089 -9.354 -51.281 1.014 1.00158.62 N ANISOU 1996 N ALA A1089 26799 14118 19350 4601 -933 -2265 N ATOM 1997 CA ALA A1089 -8.667 -50.518 -0.023 1.00160.91 C ANISOU 1997 CA ALA A1089 26789 14567 19781 4654 -552 -2594 C ATOM 1998 C ALA A1089 -9.659 -49.809 -0.936 1.00157.78 C ANISOU 1998 C ALA A1089 26544 14378 19026 4026 -463 -2630 C ATOM 1999 O ALA A1089 -9.493 -48.620 -1.240 1.00156.26 O ANISOU 1999 O ALA A1089 25885 14608 18877 3935 -338 -2730 O ATOM 2000 CB ALA A1089 -7.755 -51.440 -0.833 1.00167.78 C ANISOU 2000 CB ALA A1089 27850 15029 20869 4912 -155 -2809 C ATOM 2001 N ALA A1090 -10.699 -50.522 -1.381 1.00152.58 N ANISOU 2001 N ALA A1090 26535 13418 18019 3584 -540 -2542 N ATOM 2002 CA ALA A1090 -11.729 -49.915 -2.213 1.00139.83 C ANISOU 2002 CA ALA A1090 25074 11993 16063 2973 -555 -2531 C ATOM 2003 C ALA A1090 -12.436 -48.769 -1.506 1.00129.64 C ANISOU 2003 C ALA A1090 23234 11269 14754 2718 -821 -2280 C ATOM 2004 O ALA A1090 -12.988 -47.887 -2.174 1.00127.14 O ANISOU 2004 O ALA A1090 22803 11233 14273 2346 -788 -2288 O ATOM 2005 CB ALA A1090 -12.746 -50.977 -2.637 1.00135.23 C ANISOU 2005 CB ALA A1090 25247 10981 15152 2536 -677 -2458 C ATOM 2006 N ALA A1091 -12.439 -48.766 -0.172 1.00126.61 N ANISOU 2006 N ALA A1091 22549 11033 14524 2910 -1070 -2050 N ATOM 2007 CA ALA A1091 -13.099 -47.688 0.558 1.00125.39 C ANISOU 2007 CA ALA A1091 21908 11374 14359 2668 -1261 -1819 C ATOM 2008 C ALA A1091 -12.470 -46.323 0.275 1.00127.12 C ANISOU 2008 C ALA A1091 21520 12052 14728 2778 -1058 -1978 C ATOM 2009 O ALA A1091 -13.170 -45.303 0.304 1.00124.30 O ANISOU 2009 O ALA A1091 20864 12067 14297 2447 -1099 -1849 O ATOM 2010 CB ALA A1091 -13.077 -47.989 2.056 1.00126.24 C ANISOU 2010 CB ALA A1091 21893 11502 14569 2886 -1523 -1574 C ATOM 2011 N GLU A1092 -11.162 -46.277 0.000 1.00132.99 N ANISOU 2011 N GLU A1092 22062 12754 15715 3236 -810 -2256 N ATOM 2012 CA GLU A1092 -10.502 -44.997 -0.258 1.00133.95 C ANISOU 2012 CA GLU A1092 21605 13281 16010 3337 -572 -2434 C ATOM 2013 C GLU A1092 -10.934 -44.359 -1.573 1.00133.72 C ANISOU 2013 C GLU A1092 21727 13318 15763 2970 -317 -2556 C ATOM 2014 O GLU A1092 -10.853 -43.134 -1.713 1.00131.52 O ANISOU 2014 O GLU A1092 21012 13426 15534 2886 -171 -2595 O ATOM 2015 CB GLU A1092 -8.982 -45.166 -0.243 1.00140.04 C ANISOU 2015 CB GLU A1092 22095 13954 17161 3913 -350 -2714 C ATOM 2016 CG GLU A1092 -8.392 -45.392 1.129 1.00144.28 C ANISOU 2016 CG GLU A1092 22287 14579 17955 4312 -647 -2592 C ATOM 2017 CD GLU A1092 -8.479 -44.143 1.987 1.00143.82 C ANISOU 2017 CD GLU A1092 21629 15068 17950 4213 -787 -2487 C ATOM 2018 OE1 GLU A1092 -8.396 -43.031 1.420 1.00142.23 O ANISOU 2018 OE1 GLU A1092 21097 15168 17778 4049 -520 -2633 O ATOM 2019 OE2 GLU A1092 -8.632 -44.265 3.221 1.00144.91 O ANISOU 2019 OE2 GLU A1092 21672 15308 18078 4287 -1138 -2260 O ATOM 2020 N GLN A1093 -11.382 -45.153 -2.547 1.00138.11 N ANISOU 2020 N GLN A1093 22928 13493 16055 2741 -263 -2617 N ATOM 2021 CA GLN A1093 -11.700 -44.584 -3.854 1.00139.45 C ANISOU 2021 CA GLN A1093 23319 13696 15971 2412 -44 -2744 C ATOM 2022 C GLN A1093 -12.844 -43.576 -3.775 1.00136.13 C ANISOU 2022 C GLN A1093 22663 13679 15384 1965 -263 -2475 C ATOM 2023 O GLN A1093 -12.935 -42.675 -4.618 1.00135.60 O ANISOU 2023 O GLN A1093 22540 13794 15189 1785 -79 -2545 O ATOM 2024 CB GLN A1093 -12.031 -45.697 -4.847 1.00145.67 C ANISOU 2024 CB GLN A1093 24914 13977 16456 2202 -4 -2851 C ATOM 2025 N LEU A1094 -13.720 -43.706 -2.774 1.00131.01 N ANISOU 2025 N LEU A1094 21886 13145 14748 1791 -622 -2159 N ATOM 2026 CA LEU A1094 -14.776 -42.716 -2.568 1.00122.05 C ANISOU 2026 CA LEU A1094 20437 12382 13553 1413 -789 -1886 C ATOM 2027 C LEU A1094 -14.217 -41.340 -2.236 1.00115.47 C ANISOU 2027 C LEU A1094 18960 11988 12927 1588 -569 -1931 C ATOM 2028 O LEU A1094 -14.863 -40.322 -2.510 1.00106.90 O ANISOU 2028 O LEU A1094 17647 11186 11783 1314 -552 -1791 O ATOM 2029 CB LEU A1094 -15.710 -43.172 -1.447 1.00114.29 C ANISOU 2029 CB LEU A1094 19432 11387 12607 1235 -1127 -1564 C ATOM 2030 CG LEU A1094 -16.661 -44.343 -1.659 1.00110.76 C ANISOU 2030 CG LEU A1094 19549 10567 11967 903 -1386 -1437 C ATOM 2031 CD1 LEU A1094 -17.274 -44.736 -0.341 1.00108.63 C ANISOU 2031 CD1 LEU A1094 19192 10275 11809 847 -1607 -1159 C ATOM 2032 CD2 LEU A1094 -17.763 -43.863 -2.571 1.00109.47 C ANISOU 2032 CD2 LEU A1094 19466 10513 11615 393 -1520 -1310 C ATOM 2033 N LYS A1095 -13.021 -41.290 -1.652 1.00118.45 N ANISOU 2033 N LYS A1095 19028 12414 13562 2038 -405 -2120 N ATOM 2034 CA LYS A1095 -12.491 -40.027 -1.158 1.00113.56 C ANISOU 2034 CA LYS A1095 17776 12210 13160 2179 -226 -2167 C ATOM 2035 C LYS A1095 -12.157 -39.082 -2.309 1.00113.44 C ANISOU 2035 C LYS A1095 17683 12319 13100 2117 149 -2368 C ATOM 2036 O LYS A1095 -12.508 -37.896 -2.267 1.00114.04 O ANISOU 2036 O LYS A1095 17411 12728 13190 1946 247 -2267 O ATOM 2037 CB LYS A1095 -11.274 -40.311 -0.279 1.00114.43 C ANISOU 2037 CB LYS A1095 17587 12319 13570 2662 -210 -2331 C ATOM 2038 CG LYS A1095 -10.712 -39.137 0.476 1.00115.48 C ANISOU 2038 CG LYS A1095 17068 12872 13936 2793 -105 -2380 C ATOM 2039 CD LYS A1095 -9.501 -39.591 1.269 1.00122.30 C ANISOU 2039 CD LYS A1095 17680 13696 15093 3270 -183 -2542 C ATOM 2040 CE LYS A1095 -9.925 -40.452 2.454 1.00125.50 C ANISOU 2040 CE LYS A1095 18276 13981 15427 3317 -614 -2274 C ATOM 2041 NZ LYS A1095 -8.768 -40.835 3.313 1.00129.60 N ANISOU 2041 NZ LYS A1095 18535 14490 16219 3792 -775 -2384 N ATOM 2042 N THR A1096 -11.523 -39.596 -3.368 1.00113.99 N ANISOU 2042 N THR A1096 18127 12086 13097 2239 396 -2643 N ATOM 2043 CA THR A1096 -11.140 -38.735 -4.488 1.00111.88 C ANISOU 2043 CA THR A1096 17867 11884 12756 2188 807 -2850 C ATOM 2044 C THR A1096 -12.357 -38.281 -5.294 1.00109.55 C ANISOU 2044 C THR A1096 17876 11653 12096 1717 680 -2627 C ATOM 2045 O THR A1096 -12.430 -37.118 -5.721 1.00107.71 O ANISOU 2045 O THR A1096 17433 11665 11827 1606 895 -2615 O ATOM 2046 CB THR A1096 -10.129 -39.456 -5.379 1.00112.98 C ANISOU 2046 CB THR A1096 18380 11631 12917 2440 1159 -3212 C ATOM 2047 OG1 THR A1096 -10.715 -40.657 -5.897 1.00116.93 O ANISOU 2047 OG1 THR A1096 19577 11732 13121 2262 958 -3161 O ATOM 2048 CG2 THR A1096 -8.876 -39.804 -4.585 1.00111.99 C ANISOU 2048 CG2 THR A1096 17840 11468 13244 2944 1275 -3417 C ATOM 2049 N THR A1097 -13.329 -39.175 -5.504 1.00105.48 N ANISOU 2049 N THR A1097 17842 10912 11321 1431 318 -2441 N ATOM 2050 CA THR A1097 -14.562 -38.770 -6.176 1.00 99.71 C ANISOU 2050 CA THR A1097 17328 10265 10290 972 91 -2189 C ATOM 2051 C THR A1097 -15.334 -37.733 -5.361 1.00 94.61 C ANISOU 2051 C THR A1097 16107 10030 9812 824 -61 -1864 C ATOM 2052 O THR A1097 -15.892 -36.782 -5.931 1.00 93.47 O ANISOU 2052 O THR A1097 15880 10077 9557 602 -34 -1719 O ATOM 2053 CB THR A1097 -15.427 -40.001 -6.473 1.00 98.31 C ANISOU 2053 CB THR A1097 17737 9759 9856 676 -294 -2074 C ATOM 2054 OG1 THR A1097 -15.755 -40.683 -5.255 1.00 95.75 O ANISOU 2054 OG1 THR A1097 17243 9406 9732 727 -567 -1902 O ATOM 2055 CG2 THR A1097 -14.686 -40.957 -7.392 1.00103.24 C ANISOU 2055 CG2 THR A1097 19002 9942 10282 791 -75 -2409 C ATOM 2056 N ARG A1098 -15.352 -37.871 -4.031 1.00 93.00 N ANISOU 2056 N ARG A1098 15524 9942 9871 955 -191 -1743 N ATOM 2057 CA ARG A1098 -16.022 -36.873 -3.206 1.00 91.20 C ANISOU 2057 CA ARG A1098 14773 10065 9814 822 -249 -1462 C ATOM 2058 C ARG A1098 -15.279 -35.539 -3.233 1.00 91.88 C ANISOU 2058 C ARG A1098 14408 10450 10051 999 155 -1602 C ATOM 2059 O ARG A1098 -15.914 -34.473 -3.215 1.00 87.32 O ANISOU 2059 O ARG A1098 13542 10124 9514 813 212 -1393 O ATOM 2060 CB ARG A1098 -16.157 -37.394 -1.776 1.00 88.44 C ANISOU 2060 CB ARG A1098 14233 9719 9651 910 -448 -1325 C ATOM 2061 CG ARG A1098 -16.981 -36.503 -0.877 1.00 87.23 C ANISOU 2061 CG ARG A1098 13632 9855 9656 724 -487 -1021 C ATOM 2062 CD ARG A1098 -18.424 -36.486 -1.368 1.00 90.07 C ANISOU 2062 CD ARG A1098 14118 10182 9923 290 -730 -702 C ATOM 2063 NE ARG A1098 -19.013 -37.825 -1.364 1.00 95.61 N ANISOU 2063 NE ARG A1098 15257 10561 10512 122 -1064 -621 N ATOM 2064 CZ ARG A1098 -19.582 -38.391 -0.302 1.00 96.72 C ANISOU 2064 CZ ARG A1098 15373 10611 10764 34 -1235 -428 C ATOM 2065 NH1 ARG A1098 -19.654 -37.730 0.843 1.00 96.46 N ANISOU 2065 NH1 ARG A1098 14928 10788 10935 91 -1112 -293 N ATOM 2066 NH2 ARG A1098 -20.090 -39.613 -0.386 1.00 96.79 N ANISOU 2066 NH2 ARG A1098 15813 10297 10667 -135 -1500 -377 N ATOM 2067 N ASN A1099 -13.943 -35.580 -3.305 1.00 99.26 N ANISOU 2067 N ASN A1099 15270 11340 11103 1352 459 -1957 N ATOM 2068 CA ASN A1099 -13.165 -34.350 -3.415 1.00100.25 C ANISOU 2068 CA ASN A1099 14986 11716 11388 1498 885 -2139 C ATOM 2069 C ASN A1099 -13.464 -33.630 -4.730 1.00102.00 C ANISOU 2069 C ASN A1099 15442 11935 11377 1301 1106 -2135 C ATOM 2070 O ASN A1099 -13.519 -32.395 -4.784 1.00104.24 O ANISOU 2070 O ASN A1099 15407 12468 11730 1245 1358 -2081 O ATOM 2071 CB ASN A1099 -11.672 -34.668 -3.311 1.00102.88 C ANISOU 2071 CB ASN A1099 15191 11956 11942 1905 1153 -2535 C ATOM 2072 CG ASN A1099 -10.819 -33.421 -3.178 1.00105.03 C ANISOU 2072 CG ASN A1099 14944 12505 12459 2048 1578 -2741 C ATOM 2073 OD1 ASN A1099 -11.334 -32.305 -3.081 1.00100.95 O ANISOU 2073 OD1 ASN A1099 14178 12247 11934 1855 1690 -2581 O ATOM 2074 ND2 ASN A1099 -9.507 -33.603 -3.186 1.00111.34 N ANISOU 2074 ND2 ASN A1099 15564 13231 13511 2384 1839 -3100 N ATOM 2075 N ALA A1100 -13.638 -34.393 -5.812 1.00 99.11 N ANISOU 2075 N ALA A1100 15682 11266 10710 1191 1027 -2196 N ATOM 2076 CA ALA A1100 -13.985 -33.780 -7.094 1.00 95.84 C ANISOU 2076 CA ALA A1100 15601 10821 9994 978 1170 -2165 C ATOM 2077 C ALA A1100 -15.385 -33.176 -7.057 1.00 93.01 C ANISOU 2077 C ALA A1100 15134 10660 9544 634 838 -1726 C ATOM 2078 O ALA A1100 -15.611 -32.065 -7.574 1.00 91.39 O ANISOU 2078 O ALA A1100 14832 10616 9275 543 1024 -1620 O ATOM 2079 CB ALA A1100 -13.875 -34.813 -8.214 1.00 93.03 C ANISOU 2079 CB ALA A1100 15992 10066 9288 903 1130 -2337 C ATOM 2080 N TYR A1101 -16.342 -33.906 -6.468 1.00 89.78 N ANISOU 2080 N TYR A1101 14743 10215 9154 446 365 -1462 N ATOM 2081 CA TYR A1101 -17.683 -33.363 -6.269 1.00 87.25 C ANISOU 2081 CA TYR A1101 14202 10078 8871 139 60 -1034 C ATOM 2082 C TYR A1101 -17.649 -32.040 -5.507 1.00 82.41 C ANISOU 2082 C TYR A1101 12953 9797 8560 231 345 -914 C ATOM 2083 O TYR A1101 -18.345 -31.087 -5.875 1.00 82.71 O ANISOU 2083 O TYR A1101 12842 9987 8595 69 358 -659 O ATOM 2084 CB TYR A1101 -18.562 -34.389 -5.547 1.00 91.16 C ANISOU 2084 CB TYR A1101 14738 10462 9436 -44 -396 -820 C ATOM 2085 CG TYR A1101 -19.965 -33.899 -5.240 1.00 95.13 C ANISOU 2085 CG TYR A1101 14940 11127 10080 -358 -685 -378 C ATOM 2086 CD1 TYR A1101 -20.930 -33.789 -6.238 1.00100.79 C ANISOU 2086 CD1 TYR A1101 15882 11812 10603 -677 -998 -148 C ATOM 2087 CD2 TYR A1101 -20.322 -33.554 -3.942 1.00 93.32 C ANISOU 2087 CD2 TYR A1101 14201 11064 10190 -338 -643 -189 C ATOM 2088 CE1 TYR A1101 -22.210 -33.334 -5.945 1.00102.68 C ANISOU 2088 CE1 TYR A1101 15763 12191 11060 -940 -1262 270 C ATOM 2089 CE2 TYR A1101 -21.592 -33.105 -3.642 1.00 95.37 C ANISOU 2089 CE2 TYR A1101 14154 11436 10648 -610 -833 209 C ATOM 2090 CZ TYR A1101 -22.532 -32.997 -4.643 1.00101.38 C ANISOU 2090 CZ TYR A1101 15063 12171 11287 -898 -1144 442 C ATOM 2091 OH TYR A1101 -23.793 -32.547 -4.331 1.00105.82 O ANISOU 2091 OH TYR A1101 15242 12835 12130 -1148 -1333 852 O ATOM 2092 N ILE A1102 -16.839 -31.959 -4.448 1.00 77.63 N ANISOU 2092 N ILE A1102 11986 9297 8215 488 567 -1092 N ATOM 2093 CA ILE A1102 -16.714 -30.708 -3.696 1.00 74.44 C ANISOU 2093 CA ILE A1102 11022 9188 8074 555 875 -1029 C ATOM 2094 C ILE A1102 -16.092 -29.604 -4.557 1.00 74.16 C ANISOU 2094 C ILE A1102 10949 9244 7985 640 1329 -1194 C ATOM 2095 O ILE A1102 -16.579 -28.460 -4.582 1.00 71.59 O ANISOU 2095 O ILE A1102 10360 9099 7742 538 1503 -987 O ATOM 2096 CB ILE A1102 -15.908 -30.955 -2.404 1.00 71.66 C ANISOU 2096 CB ILE A1102 10362 8911 7956 793 953 -1216 C ATOM 2097 CG1 ILE A1102 -16.680 -31.878 -1.453 1.00 65.57 C ANISOU 2097 CG1 ILE A1102 9638 8049 7227 677 547 -984 C ATOM 2098 CG2 ILE A1102 -15.538 -29.652 -1.728 1.00 72.30 C ANISOU 2098 CG2 ILE A1102 9927 9277 8267 862 1329 -1253 C ATOM 2099 CD1 ILE A1102 -15.860 -32.377 -0.276 1.00 60.91 C ANISOU 2099 CD1 ILE A1102 8903 7464 6776 926 525 -1160 C ATOM 2100 N GLN A1103 -15.008 -29.927 -5.273 1.00 76.97 N ANISOU 2100 N GLN A1103 11578 9445 8223 831 1571 -1567 N ATOM 2101 CA GLN A1103 -14.299 -28.925 -6.067 1.00 79.44 C ANISOU 2101 CA GLN A1103 11885 9801 8496 919 2081 -1770 C ATOM 2102 C GLN A1103 -15.164 -28.276 -7.137 1.00 80.15 C ANISOU 2102 C GLN A1103 12262 9877 8314 687 2051 -1499 C ATOM 2103 O GLN A1103 -14.939 -27.108 -7.475 1.00 84.12 O ANISOU 2103 O GLN A1103 12623 10492 8846 712 2457 -1510 O ATOM 2104 CB GLN A1103 -13.059 -29.541 -6.707 1.00 85.28 C ANISOU 2104 CB GLN A1103 12922 10307 9172 1144 2359 -2212 C ATOM 2105 CG GLN A1103 -11.960 -29.798 -5.724 1.00 86.91 C ANISOU 2105 CG GLN A1103 12713 10578 9733 1438 2506 -2511 C ATOM 2106 CD GLN A1103 -11.470 -28.493 -5.142 1.00 93.25 C ANISOU 2106 CD GLN A1103 12934 11677 10821 1503 2883 -2587 C ATOM 2107 OE1 GLN A1103 -11.675 -28.197 -3.962 1.00 93.07 O ANISOU 2107 OE1 GLN A1103 12487 11870 11005 1497 2767 -2475 O ATOM 2108 NE2 GLN A1103 -10.864 -27.671 -5.994 1.00 99.30 N ANISOU 2108 NE2 GLN A1103 13593 12530 11605 1479 3026 -2582 N ATOM 2109 N LYS A1104 -16.129 -29.002 -7.699 1.00 78.14 N ANISOU 2109 N LYS A1104 12424 9474 7792 458 1569 -1257 N ATOM 2110 CA LYS A1104 -16.975 -28.396 -8.730 1.00 80.34 C ANISOU 2110 CA LYS A1104 12979 9746 7801 237 1449 -970 C ATOM 2111 C LYS A1104 -17.704 -27.165 -8.162 1.00 81.07 C ANISOU 2111 C LYS A1104 12528 10109 8165 176 1520 -616 C ATOM 2112 O LYS A1104 -17.635 -26.043 -8.709 1.00 79.88 O ANISOU 2112 O LYS A1104 12355 10030 7967 198 1851 -551 O ATOM 2113 CB LYS A1104 -17.959 -29.458 -9.239 1.00 87.00 C ANISOU 2113 CB LYS A1104 14277 10411 8369 -36 823 -759 C ATOM 2114 CG LYS A1104 -18.716 -29.181 -10.528 1.00 91.87 C ANISOU 2114 CG LYS A1104 15367 10947 8591 -281 568 -523 C ATOM 2115 CD LYS A1104 -17.697 -29.274 -11.670 1.00 98.52 C ANISOU 2115 CD LYS A1104 16840 11554 9041 -184 948 -898 C ATOM 2116 CE LYS A1104 -18.284 -29.103 -13.077 1.00108.75 C ANISOU 2116 CE LYS A1104 18795 12710 9813 -430 706 -723 C ATOM 2117 NZ LYS A1104 -19.164 -30.249 -13.487 1.00116.26 N ANISOU 2117 NZ LYS A1104 20200 13494 10478 -746 24 -583 N ATOM 2118 N TYR A1105 -18.372 -27.360 -7.018 1.00 80.37 N ANISOU 2118 N TYR A1105 12016 10145 8377 109 1270 -396 N ATOM 2119 CA TYR A1105 -19.007 -26.262 -6.294 1.00 79.70 C ANISOU 2119 CA TYR A1105 11388 10282 8614 67 1413 -92 C ATOM 2120 C TYR A1105 -18.014 -25.165 -5.934 1.00 77.26 C ANISOU 2120 C TYR A1105 10761 10118 8477 275 2051 -338 C ATOM 2121 O TYR A1105 -18.295 -23.967 -6.106 1.00 78.53 O ANISOU 2121 O TYR A1105 10723 10385 8730 258 2340 -155 O ATOM 2122 CB TYR A1105 -19.678 -26.794 -5.023 1.00 79.78 C ANISOU 2122 CB TYR A1105 11060 10344 8909 -24 1137 94 C ATOM 2123 CG TYR A1105 -20.956 -27.570 -5.243 1.00 84.50 C ANISOU 2123 CG TYR A1105 11808 10835 9464 -295 550 439 C ATOM 2124 CD1 TYR A1105 -22.169 -26.907 -5.360 1.00 85.70 C ANISOU 2124 CD1 TYR A1105 11706 11064 9792 -482 389 887 C ATOM 2125 CD2 TYR A1105 -20.952 -28.954 -5.359 1.00 88.28 C ANISOU 2125 CD2 TYR A1105 12667 11118 9760 -368 167 317 C ATOM 2126 CE1 TYR A1105 -23.346 -27.594 -5.560 1.00 90.01 C ANISOU 2126 CE1 TYR A1105 12319 11519 10362 -751 -163 1197 C ATOM 2127 CE2 TYR A1105 -22.127 -29.653 -5.565 1.00 92.37 C ANISOU 2127 CE2 TYR A1105 13308 11530 10257 -656 -362 612 C ATOM 2128 CZ TYR A1105 -23.320 -28.966 -5.666 1.00 94.91 C ANISOU 2128 CZ TYR A1105 13325 11955 10783 -855 -539 1047 C ATOM 2129 OH TYR A1105 -24.494 -29.649 -5.871 1.00100.78 O ANISOU 2129 OH TYR A1105 14125 12600 11565 -1161 -1085 1334 O ATOM 2130 N LEU A1106 -16.863 -25.554 -5.386 1.00 73.09 N ANISOU 2130 N LEU A1106 10153 9590 8028 470 2268 -745 N ATOM 2131 CA LEU A1106 -15.928 -24.534 -4.927 1.00 75.68 C ANISOU 2131 CA LEU A1106 10114 10072 8568 630 2838 -998 C ATOM 2132 C LEU A1106 -15.479 -23.632 -6.073 1.00 79.10 C ANISOU 2132 C LEU A1106 10753 10459 8844 672 3283 -1106 C ATOM 2133 O LEU A1106 -15.360 -22.409 -5.898 1.00 80.25 O ANISOU 2133 O LEU A1106 10564 10745 9181 665 3526 -1036 O ATOM 2134 CB LEU A1106 -14.735 -25.183 -4.231 1.00 79.16 C ANISOU 2134 CB LEU A1106 10428 10514 9136 837 2919 -1418 C ATOM 2135 CG LEU A1106 -15.186 -25.877 -2.942 1.00 79.92 C ANISOU 2135 CG LEU A1106 10315 10668 9384 799 2538 -1278 C ATOM 2136 CD1 LEU A1106 -14.019 -26.577 -2.253 1.00 81.31 C ANISOU 2136 CD1 LEU A1106 10388 10835 9672 1030 2532 -1653 C ATOM 2137 CD2 LEU A1106 -15.904 -24.900 -2.007 1.00 74.87 C ANISOU 2137 CD2 LEU A1106 9258 10221 8967 664 2667 -1003 C ATOM 2138 N VAL A 240 -15.248 -24.212 -7.256 1.00 66.34 N ANISOU 2138 N VAL A 240 9486 6512 9208 468 477 1136 N ATOM 2139 CA VAL A 240 -14.868 -23.417 -8.418 1.00 56.97 C ANISOU 2139 CA VAL A 240 8158 5471 8017 462 465 929 C ATOM 2140 C VAL A 240 -15.977 -22.440 -8.798 1.00 53.35 C ANISOU 2140 C VAL A 240 7645 5198 7427 276 488 827 C ATOM 2141 O VAL A 240 -15.709 -21.260 -9.088 1.00 48.06 O ANISOU 2141 O VAL A 240 6860 4744 6658 281 430 753 O ATOM 2142 CB VAL A 240 -14.477 -24.332 -9.596 1.00 57.48 C ANISOU 2142 CB VAL A 240 8232 5344 8265 495 544 775 C ATOM 2143 CG1 VAL A 240 -14.245 -23.504 -10.853 1.00 56.32 C ANISOU 2143 CG1 VAL A 240 7954 5359 8085 461 551 561 C ATOM 2144 CG2 VAL A 240 -13.218 -25.113 -9.265 1.00 51.31 C ANISOU 2144 CG2 VAL A 240 7468 4407 7621 715 510 867 C ATOM 2145 N SER A 241 -17.233 -22.905 -8.812 1.00 55.30 N ANISOU 2145 N SER A 241 7968 5361 7684 110 573 824 N ATOM 2146 CA SER A 241 -18.318 -21.981 -9.158 1.00 56.50 C ANISOU 2146 CA SER A 241 8050 5693 7722 -55 589 734 C ATOM 2147 C SER A 241 -18.410 -20.814 -8.179 1.00 55.71 C ANISOU 2147 C SER A 241 7907 5811 7448 -36 519 838 C ATOM 2148 O SER A 241 -18.672 -19.668 -8.590 1.00 54.19 O ANISOU 2148 O SER A 241 7613 5816 7160 -86 489 744 O ATOM 2149 CB SER A 241 -19.651 -22.732 -9.277 1.00 63.62 C ANISOU 2149 CB SER A 241 9023 6469 8680 -239 689 721 C ATOM 2150 OG SER A 241 -20.073 -23.244 -8.000 1.00 76.23 O ANISOU 2150 OG SER A 241 10727 7979 10260 -253 721 924 O ATOM 2151 N HIS A 242 -18.152 -21.073 -6.897 1.00 58.73 N ANISOU 2151 N HIS A 242 8372 6160 7784 42 489 1029 N ATOM 2152 CA HIS A 242 -18.269 -19.994 -5.927 1.00 58.82 C ANISOU 2152 CA HIS A 242 8359 6374 7615 55 427 1113 C ATOM 2153 C HIS A 242 -17.121 -18.999 -6.068 1.00 56.56 C ANISOU 2153 C HIS A 242 7967 6247 7277 178 311 1060 C ATOM 2154 O HIS A 242 -17.335 -17.786 -5.943 1.00 57.17 O ANISOU 2154 O HIS A 242 7973 6518 7229 144 271 1017 O ATOM 2155 CB HIS A 242 -18.308 -20.519 -4.485 1.00 65.18 C ANISOU 2155 CB HIS A 242 9294 7119 8354 102 423 1334 C ATOM 2156 CG HIS A 242 -19.399 -21.498 -4.201 1.00 72.86 C ANISOU 2156 CG HIS A 242 10375 7930 9377 -23 547 1416 C ATOM 2157 ND1 HIS A 242 -20.735 -21.183 -4.308 1.00 73.56 N ANISOU 2157 ND1 HIS A 242 10439 8086 9423 -199 638 1368 N ATOM 2158 CD2 HIS A 242 -19.338 -22.722 -3.616 1.00 77.19 C ANISOU 2158 CD2 HIS A 242 11061 8264 10002 7 591 1573 C ATOM 2159 CE1 HIS A 242 -21.445 -22.223 -3.904 1.00 76.37 C ANISOU 2159 CE1 HIS A 242 10903 8270 9844 -287 740 1476 C ATOM 2160 NE2 HIS A 242 -20.623 -23.162 -3.465 1.00 78.49 N ANISOU 2160 NE2 HIS A 242 11282 8360 10182 -166 716 1606 N ATOM 2161 N ARG A 243 -15.890 -19.498 -6.242 1.00 51.89 N ANISOU 2161 N ARG A 243 7362 5569 6785 325 257 1073 N ATOM 2162 CA ARG A 243 -14.755 -18.625 -6.501 1.00 57.09 C ANISOU 2162 CA ARG A 243 7899 6369 7424 430 156 1011 C ATOM 2163 C ARG A 243 -15.068 -17.674 -7.636 1.00 51.80 C ANISOU 2163 C ARG A 243 7119 5829 6734 336 183 829 C ATOM 2164 O ARG A 243 -14.841 -16.463 -7.526 1.00 53.67 O ANISOU 2164 O ARG A 243 7273 6248 6872 336 116 797 O ATOM 2165 CB ARG A 243 -13.527 -19.446 -6.868 1.00 69.92 C ANISOU 2165 CB ARG A 243 9500 7860 9205 584 132 1012 C ATOM 2166 CG ARG A 243 -12.316 -18.543 -7.097 1.00 76.83 C ANISOU 2166 CG ARG A 243 10230 8890 10073 687 32 955 C ATOM 2167 CD ARG A 243 -11.114 -19.297 -7.625 1.00 86.90 C ANISOU 2167 CD ARG A 243 11449 10049 11521 840 27 930 C ATOM 2168 NE ARG A 243 -11.408 -19.843 -8.949 1.00 94.14 N ANISOU 2168 NE ARG A 243 12365 10851 12551 782 153 773 N ATOM 2169 CZ ARG A 243 -11.383 -19.127 -10.073 1.00 98.49 C ANISOU 2169 CZ ARG A 243 12818 11513 13091 717 192 605 C ATOM 2170 NH1 ARG A 243 -11.659 -19.702 -11.235 1.00102.35 N ANISOU 2170 NH1 ARG A 243 13325 11897 13664 666 301 462 N ATOM 2171 NH2 ARG A 243 -11.129 -17.821 -10.035 1.00 96.38 N ANISOU 2171 NH2 ARG A 243 12446 11457 12718 694 123 578 N ATOM 2172 N LYS A 244 -15.555 -18.220 -8.757 1.00 49.67 N ANISOU 2172 N LYS A 244 6851 5462 6558 256 275 708 N ATOM 2173 CA LYS A 244 -15.826 -17.380 -9.926 1.00 52.92 C ANISOU 2173 CA LYS A 244 7166 5996 6944 172 296 542 C ATOM 2174 C LYS A 244 -16.870 -16.301 -9.623 1.00 50.43 C ANISOU 2174 C LYS A 244 6827 5845 6491 57 287 543 C ATOM 2175 O LYS A 244 -16.670 -15.114 -9.943 1.00 47.57 O ANISOU 2175 O LYS A 244 6374 5643 6057 53 242 481 O ATOM 2176 CB LYS A 244 -16.264 -18.250 -11.102 1.00 58.11 C ANISOU 2176 CB LYS A 244 7852 6521 7707 97 390 414 C ATOM 2177 CG LYS A 244 -15.151 -19.131 -11.653 1.00 62.44 C ANISOU 2177 CG LYS A 244 8402 6925 8395 220 412 367 C ATOM 2178 CD LYS A 244 -15.648 -19.955 -12.825 1.00 66.21 C ANISOU 2178 CD LYS A 244 8922 7273 8960 133 508 217 C ATOM 2179 CE LYS A 244 -14.557 -20.859 -13.363 1.00 70.02 C ANISOU 2179 CE LYS A 244 9415 7600 9588 265 547 158 C ATOM 2180 NZ LYS A 244 -15.044 -21.677 -14.504 1.00 74.38 N ANISOU 2180 NZ LYS A 244 10025 8020 10217 176 643 -9 N ATOM 2181 N ALA A 245 -17.994 -16.688 -9.002 1.00 49.47 N ANISOU 2181 N ALA A 245 6782 5676 6338 -35 338 614 N ATOM 2182 CA ALA A 245 -19.035 -15.695 -8.722 1.00 49.29 C ANISOU 2182 CA ALA A 245 6726 5805 6198 -135 345 609 C ATOM 2183 C ALA A 245 -18.527 -14.599 -7.774 1.00 46.04 C ANISOU 2183 C ALA A 245 6291 5541 5663 -58 260 676 C ATOM 2184 O ALA A 245 -18.770 -13.399 -7.995 1.00 43.24 O ANISOU 2184 O ALA A 245 5861 5335 5232 -90 234 612 O ATOM 2185 CB ALA A 245 -20.289 -16.374 -8.158 1.00 46.01 C ANISOU 2185 CB ALA A 245 6387 5312 5782 -245 430 682 C ATOM 2186 N LEU A 246 -17.781 -14.985 -6.734 1.00 44.94 N ANISOU 2186 N LEU A 246 6215 5359 5502 46 209 801 N ATOM 2187 CA LEU A 246 -17.348 -13.987 -5.753 1.00 47.70 C ANISOU 2187 CA LEU A 246 6554 5850 5719 106 120 857 C ATOM 2188 C LEU A 246 -16.326 -13.022 -6.348 1.00 45.78 C ANISOU 2188 C LEU A 246 6196 5712 5486 165 35 763 C ATOM 2189 O LEU A 246 -16.416 -11.799 -6.137 1.00 49.99 O ANISOU 2189 O LEU A 246 6683 6387 5925 144 -7 725 O ATOM 2190 CB LEU A 246 -16.807 -14.682 -4.498 1.00 46.98 C ANISOU 2190 CB LEU A 246 6565 5697 5589 202 71 1021 C ATOM 2191 CG LEU A 246 -16.352 -13.759 -3.366 1.00 48.92 C ANISOU 2191 CG LEU A 246 6820 6089 5677 262 -33 1081 C ATOM 2192 CD1 LEU A 246 -17.493 -12.877 -2.902 1.00 45.11 C ANISOU 2192 CD1 LEU A 246 6357 5724 5058 163 20 1060 C ATOM 2193 CD2 LEU A 246 -15.845 -14.582 -2.193 1.00 50.28 C ANISOU 2193 CD2 LEU A 246 7104 6197 5803 358 -87 1255 C ATOM 2194 N THR A 247 -15.368 -13.546 -7.118 1.00 47.50 N ANISOU 2194 N THR A 247 6366 5857 5826 234 21 719 N ATOM 2195 CA THR A 247 -14.383 -12.683 -7.769 1.00 47.88 C ANISOU 2195 CA THR A 247 6293 6001 5898 278 -40 631 C ATOM 2196 C THR A 247 -15.065 -11.689 -8.699 1.00 46.49 C ANISOU 2196 C THR A 247 6054 5923 5688 173 2 513 C ATOM 2197 O THR A 247 -14.766 -10.478 -8.677 1.00 42.08 O ANISOU 2197 O THR A 247 5429 5489 5072 169 -54 478 O ATOM 2198 CB THR A 247 -13.377 -13.537 -8.543 1.00 50.48 C ANISOU 2198 CB THR A 247 6579 6226 6374 364 -26 596 C ATOM 2199 OG1 THR A 247 -12.686 -14.402 -7.637 1.00 54.24 O ANISOU 2199 OG1 THR A 247 7106 6612 6890 482 -80 720 O ATOM 2200 CG2 THR A 247 -12.379 -12.675 -9.288 1.00 49.26 C ANISOU 2200 CG2 THR A 247 6290 6174 6252 398 -65 505 C ATOM 2201 N THR A 248 -15.987 -12.187 -9.532 1.00 45.82 N ANISOU 2201 N THR A 248 5991 5778 5641 85 93 453 N ATOM 2202 CA THR A 248 -16.691 -11.301 -10.452 1.00 43.10 C ANISOU 2202 CA THR A 248 5588 5529 5261 -9 122 353 C ATOM 2203 C THR A 248 -17.358 -10.158 -9.699 1.00 43.21 C ANISOU 2203 C THR A 248 5598 5661 5161 -47 92 384 C ATOM 2204 O THR A 248 -17.166 -8.982 -10.041 1.00 42.79 O ANISOU 2204 O THR A 248 5477 5712 5070 -54 56 334 O ATOM 2205 CB THR A 248 -17.732 -12.085 -11.250 1.00 43.59 C ANISOU 2205 CB THR A 248 5681 5514 5366 -107 207 296 C ATOM 2206 OG1 THR A 248 -17.091 -13.139 -11.974 1.00 49.61 O ANISOU 2206 OG1 THR A 248 6459 6155 6234 -69 242 248 O ATOM 2207 CG2 THR A 248 -18.445 -11.169 -12.231 1.00 37.72 C ANISOU 2207 CG2 THR A 248 4872 4881 4578 -194 219 203 C ATOM 2208 N ILE A 249 -18.136 -10.485 -8.655 1.00 45.00 N ANISOU 2208 N ILE A 249 5900 5865 5333 -69 115 468 N ATOM 2209 CA ILE A 249 -18.936 -9.445 -8.011 1.00 45.35 C ANISOU 2209 CA ILE A 249 5943 6017 5272 -109 113 479 C ATOM 2210 C ILE A 249 -18.043 -8.422 -7.311 1.00 46.89 C ANISOU 2210 C ILE A 249 6120 6300 5395 -38 20 491 C ATOM 2211 O ILE A 249 -18.341 -7.219 -7.323 1.00 44.75 O ANISOU 2211 O ILE A 249 5811 6124 5070 -62 4 444 O ATOM 2212 CB ILE A 249 -19.982 -10.051 -7.053 1.00 44.37 C ANISOU 2212 CB ILE A 249 5901 5857 5100 -153 180 565 C ATOM 2213 CG1 ILE A 249 -20.982 -8.970 -6.628 1.00 46.23 C ANISOU 2213 CG1 ILE A 249 6116 6207 5244 -200 207 549 C ATOM 2214 CG2 ILE A 249 -19.341 -10.679 -5.835 1.00 38.60 C ANISOU 2214 CG2 ILE A 249 5265 5076 4326 -76 146 684 C ATOM 2215 CD1 ILE A 249 -21.843 -8.454 -7.776 1.00 49.03 C ANISOU 2215 CD1 ILE A 249 6379 6607 5642 -278 243 455 C ATOM 2216 N ILE A 250 -16.924 -8.863 -6.717 1.00 47.18 N ANISOU 2216 N ILE A 250 6181 6304 5440 50 -49 549 N ATOM 2217 CA ILE A 250 -16.067 -7.908 -6.007 1.00 46.34 C ANISOU 2217 CA ILE A 250 6053 6287 5267 105 -153 553 C ATOM 2218 C ILE A 250 -15.386 -6.951 -6.983 1.00 45.59 C ANISOU 2218 C ILE A 250 5846 6249 5227 99 -189 456 C ATOM 2219 O ILE A 250 -15.386 -5.723 -6.778 1.00 45.21 O ANISOU 2219 O ILE A 250 5771 6285 5123 78 -228 414 O ATOM 2220 CB ILE A 250 -15.049 -8.643 -5.117 1.00 51.72 C ANISOU 2220 CB ILE A 250 6775 6932 5944 203 -236 648 C ATOM 2221 CG1 ILE A 250 -15.772 -9.339 -3.959 1.00 51.63 C ANISOU 2221 CG1 ILE A 250 6894 6886 5837 204 -204 762 C ATOM 2222 CG2 ILE A 250 -13.949 -7.695 -4.631 1.00 54.96 C ANISOU 2222 CG2 ILE A 250 7130 7438 6314 254 -365 628 C ATOM 2223 CD1 ILE A 250 -14.893 -10.276 -3.181 1.00 54.77 C ANISOU 2223 CD1 ILE A 250 7348 7225 6238 305 -277 880 C ATOM 2224 N ILE A 251 -14.804 -7.488 -8.062 1.00 42.86 N ANISOU 2224 N ILE A 251 5440 5852 4993 114 -166 418 N ATOM 2225 CA ILE A 251 -14.198 -6.612 -9.067 1.00 43.88 C ANISOU 2225 CA ILE A 251 5466 6036 5169 98 -177 335 C ATOM 2226 C ILE A 251 -15.230 -5.642 -9.650 1.00 45.31 C ANISOU 2226 C ILE A 251 5638 6273 5306 12 -131 279 C ATOM 2227 O ILE A 251 -14.933 -4.460 -9.880 1.00 38.89 O ANISOU 2227 O ILE A 251 4771 5525 4480 -6 -164 239 O ATOM 2228 CB ILE A 251 -13.518 -7.450 -10.167 1.00 42.00 C ANISOU 2228 CB ILE A 251 5177 5735 5045 128 -133 298 C ATOM 2229 CG1 ILE A 251 -12.333 -8.230 -9.584 1.00 42.03 C ANISOU 2229 CG1 ILE A 251 5166 5692 5114 235 -192 354 C ATOM 2230 CG2 ILE A 251 -13.098 -6.577 -11.332 1.00 39.22 C ANISOU 2230 CG2 ILE A 251 4733 5445 4724 93 -114 217 C ATOM 2231 CD1 ILE A 251 -11.781 -9.263 -10.531 1.00 41.63 C ANISOU 2231 CD1 ILE A 251 5084 5553 5182 281 -129 320 C ATOM 2232 N THR A 252 -16.464 -6.110 -9.880 1.00 47.98 N ANISOU 2232 N THR A 252 6022 6582 5627 -43 -58 279 N ATOM 2233 CA THR A 252 -17.454 -5.237 -10.508 1.00 48.66 C ANISOU 2233 CA THR A 252 6081 6725 5683 -112 -23 232 C ATOM 2234 C THR A 252 -17.908 -4.122 -9.564 1.00 43.98 C ANISOU 2234 C THR A 252 5507 6195 5009 -114 -52 246 C ATOM 2235 O THR A 252 -18.043 -2.964 -9.989 1.00 47.29 O ANISOU 2235 O THR A 252 5884 6665 5419 -134 -64 205 O ATOM 2236 CB THR A 252 -18.644 -6.063 -10.997 1.00 57.06 C ANISOU 2236 CB THR A 252 7170 7750 6761 -175 52 224 C ATOM 2237 OG1 THR A 252 -18.181 -7.042 -11.939 1.00 59.08 O ANISOU 2237 OG1 THR A 252 7418 7940 7090 -175 80 188 O ATOM 2238 CG2 THR A 252 -19.663 -5.172 -11.691 1.00 57.96 C ANISOU 2238 CG2 THR A 252 7240 7932 6849 -236 72 181 C ATOM 2239 N LEU A 253 -18.147 -4.442 -8.284 1.00 38.82 N ANISOU 2239 N LEU A 253 4924 5533 4292 -90 -59 302 N ATOM 2240 CA LEU A 253 -18.474 -3.389 -7.323 1.00 39.17 C ANISOU 2240 CA LEU A 253 4997 5638 4247 -84 -82 300 C ATOM 2241 C LEU A 253 -17.351 -2.367 -7.212 1.00 45.45 C ANISOU 2241 C LEU A 253 5756 6469 5042 -55 -172 262 C ATOM 2242 O LEU A 253 -17.614 -1.164 -7.067 1.00 40.69 O ANISOU 2242 O LEU A 253 5147 5906 4408 -70 -183 218 O ATOM 2243 CB LEU A 253 -18.786 -3.970 -5.940 1.00 40.53 C ANISOU 2243 CB LEU A 253 5264 5804 4329 -61 -72 371 C ATOM 2244 CG LEU A 253 -20.088 -4.756 -5.762 1.00 46.58 C ANISOU 2244 CG LEU A 253 6071 6544 5082 -106 33 414 C ATOM 2245 CD1 LEU A 253 -20.164 -5.381 -4.370 1.00 50.15 C ANISOU 2245 CD1 LEU A 253 6629 6988 5437 -79 44 503 C ATOM 2246 CD2 LEU A 253 -21.275 -3.837 -5.977 1.00 39.23 C ANISOU 2246 CD2 LEU A 253 5101 5669 4134 -149 93 365 C ATOM 2247 N ILE A 254 -16.090 -2.819 -7.255 1.00 47.34 N ANISOU 2247 N ILE A 254 5968 6691 5328 -14 -236 277 N ATOM 2248 CA ILE A 254 -15.002 -1.848 -7.188 1.00 43.40 C ANISOU 2248 CA ILE A 254 5414 6229 4845 -3 -323 237 C ATOM 2249 C ILE A 254 -15.019 -0.938 -8.412 1.00 41.91 C ANISOU 2249 C ILE A 254 5151 6051 4721 -50 -292 179 C ATOM 2250 O ILE A 254 -14.839 0.285 -8.294 1.00 39.13 O ANISOU 2250 O ILE A 254 4782 5726 4360 -72 -328 139 O ATOM 2251 CB ILE A 254 -13.650 -2.552 -7.008 1.00 44.56 C ANISOU 2251 CB ILE A 254 5521 6365 5045 55 -398 269 C ATOM 2252 CG1 ILE A 254 -13.621 -3.257 -5.649 1.00 41.21 C ANISOU 2252 CG1 ILE A 254 5184 5938 4534 108 -449 342 C ATOM 2253 CG2 ILE A 254 -12.497 -1.547 -7.137 1.00 44.54 C ANISOU 2253 CG2 ILE A 254 5430 6406 5089 48 -481 220 C ATOM 2254 CD1 ILE A 254 -12.441 -4.206 -5.456 1.00 42.22 C ANISOU 2254 CD1 ILE A 254 5277 6041 4722 186 -520 397 C ATOM 2255 N ILE A 255 -15.258 -1.507 -9.601 1.00 42.17 N ANISOU 2255 N ILE A 255 5149 6060 4813 -70 -225 174 N ATOM 2256 CA ILE A 255 -15.381 -0.674 -10.801 1.00 42.99 C ANISOU 2256 CA ILE A 255 5198 6182 4954 -115 -192 134 C ATOM 2257 C ILE A 255 -16.461 0.388 -10.620 1.00 44.09 C ANISOU 2257 C ILE A 255 5365 6342 5044 -144 -177 121 C ATOM 2258 O ILE A 255 -16.261 1.548 -10.974 1.00 42.30 O ANISOU 2258 O ILE A 255 5110 6127 4836 -164 -193 97 O ATOM 2259 CB ILE A 255 -15.667 -1.524 -12.050 1.00 41.87 C ANISOU 2259 CB ILE A 255 5036 6022 4851 -134 -122 125 C ATOM 2260 CG1 ILE A 255 -14.472 -2.405 -12.416 1.00 43.87 C ANISOU 2260 CG1 ILE A 255 5248 6248 5172 -97 -123 122 C ATOM 2261 CG2 ILE A 255 -16.125 -0.624 -13.217 1.00 39.01 C ANISOU 2261 CG2 ILE A 255 4641 5693 4488 -184 -90 99 C ATOM 2262 CD1 ILE A 255 -14.815 -3.423 -13.528 1.00 45.13 C ANISOU 2262 CD1 ILE A 255 5413 6377 5359 -113 -47 95 C ATOM 2263 N PHE A 256 -17.642 -0.001 -10.128 1.00 43.40 N ANISOU 2263 N PHE A 256 5330 6254 4907 -145 -136 138 N ATOM 2264 CA PHE A 256 -18.693 0.991 -9.868 1.00 45.27 C ANISOU 2264 CA PHE A 256 5583 6512 5107 -156 -113 123 C ATOM 2265 C PHE A 256 -18.285 2.068 -8.863 1.00 49.43 C ANISOU 2265 C PHE A 256 6141 7043 5596 -135 -165 96 C ATOM 2266 O PHE A 256 -18.592 3.253 -9.062 1.00 47.73 O ANISOU 2266 O PHE A 256 5917 6826 5394 -143 -164 66 O ATOM 2267 CB PHE A 256 -19.984 0.303 -9.438 1.00 44.19 C ANISOU 2267 CB PHE A 256 5479 6380 4931 -162 -50 148 C ATOM 2268 CG PHE A 256 -20.855 -0.095 -10.575 1.00 52.88 C ANISOU 2268 CG PHE A 256 6533 7488 6070 -202 -1 148 C ATOM 2269 CD1 PHE A 256 -21.863 0.773 -10.992 1.00 53.11 C ANISOU 2269 CD1 PHE A 256 6526 7549 6104 -212 20 136 C ATOM 2270 CD2 PHE A 256 -20.579 -1.214 -11.344 1.00 56.76 C ANISOU 2270 CD2 PHE A 256 7013 7955 6599 -226 12 151 C ATOM 2271 CE1 PHE A 256 -22.680 0.460 -12.057 1.00 52.38 C ANISOU 2271 CE1 PHE A 256 6383 7480 6039 -250 44 136 C ATOM 2272 CE2 PHE A 256 -21.373 -1.521 -12.437 1.00 55.15 C ANISOU 2272 CE2 PHE A 256 6770 7767 6417 -273 43 135 C ATOM 2273 CZ PHE A 256 -22.432 -0.683 -12.786 1.00 55.13 C ANISOU 2273 CZ PHE A 256 6727 7812 6408 -287 52 131 C ATOM 2274 N PHE A 257 -17.631 1.686 -7.760 1.00 44.59 N ANISOU 2274 N PHE A 257 5574 6435 4935 -108 -215 104 N ATOM 2275 CA PHE A 257 -17.268 2.722 -6.802 1.00 44.45 C ANISOU 2275 CA PHE A 257 5594 6428 4868 -99 -273 60 C ATOM 2276 C PHE A 257 -16.225 3.673 -7.372 1.00 48.34 C ANISOU 2276 C PHE A 257 6025 6905 5435 -125 -333 21 C ATOM 2277 O PHE A 257 -16.210 4.857 -7.018 1.00 51.99 O ANISOU 2277 O PHE A 257 6508 7354 5891 -138 -358 -32 O ATOM 2278 CB PHE A 257 -16.764 2.136 -5.481 1.00 51.71 C ANISOU 2278 CB PHE A 257 6579 7371 5698 -66 -332 80 C ATOM 2279 CG PHE A 257 -17.838 1.501 -4.639 1.00 59.83 C ANISOU 2279 CG PHE A 257 7689 8415 6629 -48 -264 118 C ATOM 2280 CD1 PHE A 257 -18.744 2.298 -3.956 1.00 62.93 C ANISOU 2280 CD1 PHE A 257 8137 8828 6947 -44 -217 76 C ATOM 2281 CD2 PHE A 257 -17.877 0.135 -4.429 1.00 61.81 C ANISOU 2281 CD2 PHE A 257 7967 8656 6862 -31 -244 194 C ATOM 2282 CE1 PHE A 257 -19.731 1.736 -3.156 1.00 60.11 C ANISOU 2282 CE1 PHE A 257 7847 8494 6497 -32 -137 113 C ATOM 2283 CE2 PHE A 257 -18.860 -0.432 -3.620 1.00 58.63 C ANISOU 2283 CE2 PHE A 257 7641 8265 6371 -26 -170 240 C ATOM 2284 CZ PHE A 257 -19.783 0.376 -2.984 1.00 55.74 C ANISOU 2284 CZ PHE A 257 7318 7934 5926 -29 -113 199 C ATOM 2285 N LEU A 258 -15.354 3.183 -8.248 1.00 47.03 N ANISOU 2285 N LEU A 258 5787 6736 5346 -136 -347 42 N ATOM 2286 CA LEU A 258 -14.269 4.011 -8.755 1.00 46.91 C ANISOU 2286 CA LEU A 258 5704 6713 5408 -170 -393 14 C ATOM 2287 C LEU A 258 -14.671 4.807 -9.999 1.00 43.88 C ANISOU 2287 C LEU A 258 5286 6306 5082 -208 -333 14 C ATOM 2288 O LEU A 258 -14.400 6.010 -10.078 1.00 43.81 O ANISOU 2288 O LEU A 258 5268 6268 5109 -242 -353 -15 O ATOM 2289 CB LEU A 258 -13.051 3.129 -9.058 1.00 52.38 C ANISOU 2289 CB LEU A 258 6322 7421 6160 -156 -427 37 C ATOM 2290 CG LEU A 258 -11.777 3.829 -9.533 1.00 56.19 C ANISOU 2290 CG LEU A 258 6708 7907 6735 -195 -470 13 C ATOM 2291 CD1 LEU A 258 -11.210 4.761 -8.459 1.00 54.20 C ANISOU 2291 CD1 LEU A 258 6466 7659 6467 -218 -572 -36 C ATOM 2292 CD2 LEU A 258 -10.741 2.811 -9.977 1.00 59.60 C ANISOU 2292 CD2 LEU A 258 7053 8358 7236 -166 -474 39 C ATOM 2293 N CYS A 259 -15.359 4.171 -10.944 1.00 37.06 N ANISOU 2293 N CYS A 259 4411 5450 4221 -206 -263 47 N ATOM 2294 CA CYS A 259 -15.547 4.674 -12.299 1.00 37.49 C ANISOU 2294 CA CYS A 259 4427 5500 4316 -239 -216 63 C ATOM 2295 C CYS A 259 -16.872 5.385 -12.536 1.00 37.47 C ANISOU 2295 C CYS A 259 4458 5488 4290 -236 -181 72 C ATOM 2296 O CYS A 259 -16.908 6.341 -13.315 1.00 41.19 O ANISOU 2296 O CYS A 259 4914 5940 4795 -258 -170 87 O ATOM 2297 CB CYS A 259 -15.422 3.516 -13.304 1.00 43.13 C ANISOU 2297 CB CYS A 259 5108 6239 5041 -241 -169 83 C ATOM 2298 SG CYS A 259 -13.732 2.802 -13.388 1.00 45.02 S ANISOU 2298 SG CYS A 259 5277 6485 5343 -232 -191 75 S ATOM 2299 N PHE A 260 -17.959 4.962 -11.894 1.00 35.73 N ANISOU 2299 N PHE A 260 4278 5280 4019 -206 -161 70 N ATOM 2300 CA PHE A 260 -19.302 5.357 -12.313 1.00 35.44 C ANISOU 2300 CA PHE A 260 4242 5251 3973 -196 -120 86 C ATOM 2301 C PHE A 260 -20.042 6.206 -11.288 1.00 42.29 C ANISOU 2301 C PHE A 260 5151 6097 4822 -161 -115 59 C ATOM 2302 O PHE A 260 -20.621 7.239 -11.660 1.00 45.49 O ANISOU 2302 O PHE A 260 5550 6477 5258 -145 -103 64 O ATOM 2303 CB PHE A 260 -20.064 4.074 -12.642 1.00 32.47 C ANISOU 2303 CB PHE A 260 3853 4913 3571 -202 -82 105 C ATOM 2304 CG PHE A 260 -19.567 3.399 -13.901 1.00 36.44 C ANISOU 2304 CG PHE A 260 4320 5434 4091 -235 -75 117 C ATOM 2305 CD1 PHE A 260 -19.009 4.141 -14.928 1.00 38.18 C ANISOU 2305 CD1 PHE A 260 4514 5656 4336 -256 -81 130 C ATOM 2306 CD2 PHE A 260 -19.455 2.018 -13.956 1.00 36.43 C ANISOU 2306 CD2 PHE A 260 4322 5437 4081 -245 -56 111 C ATOM 2307 CE1 PHE A 260 -18.505 3.513 -16.081 1.00 39.77 C ANISOU 2307 CE1 PHE A 260 4692 5884 4536 -284 -60 133 C ATOM 2308 CE2 PHE A 260 -18.930 1.385 -15.073 1.00 34.97 C ANISOU 2308 CE2 PHE A 260 4114 5263 3910 -269 -40 104 C ATOM 2309 CZ PHE A 260 -18.453 2.132 -16.140 1.00 35.58 C ANISOU 2309 CZ PHE A 260 4164 5360 3995 -289 -39 110 C ATOM 2310 N LEU A 261 -20.011 5.829 -9.992 1.00 37.49 N ANISOU 2310 N LEU A 261 4592 5494 4158 -141 -120 31 N ATOM 2311 CA LEU A 261 -20.806 6.556 -8.998 1.00 37.48 C ANISOU 2311 CA LEU A 261 4638 5481 4121 -103 -94 -7 C ATOM 2312 C LEU A 261 -20.270 7.959 -8.722 1.00 40.26 C ANISOU 2312 C LEU A 261 5020 5773 4504 -100 -132 -58 C ATOM 2313 O LEU A 261 -21.082 8.908 -8.658 1.00 41.09 O ANISOU 2313 O LEU A 261 5137 5842 4632 -65 -97 -80 O ATOM 2314 CB LEU A 261 -20.920 5.722 -7.714 1.00 37.69 C ANISOU 2314 CB LEU A 261 4722 5541 4057 -87 -81 -16 C ATOM 2315 CG LEU A 261 -21.649 4.373 -7.799 1.00 40.32 C ANISOU 2315 CG LEU A 261 5039 5913 4366 -94 -26 36 C ATOM 2316 CD1 LEU A 261 -21.601 3.624 -6.450 1.00 41.13 C ANISOU 2316 CD1 LEU A 261 5217 6038 4371 -80 -15 44 C ATOM 2317 CD2 LEU A 261 -23.096 4.497 -8.310 1.00 41.59 C ANISOU 2317 CD2 LEU A 261 5149 6095 4558 -88 46 50 C ATOM 2318 N PRO A 262 -18.955 8.186 -8.550 1.00 44.54 N ANISOU 2318 N PRO A 262 5569 6293 5062 -135 -201 -83 N ATOM 2319 CA PRO A 262 -18.491 9.578 -8.374 1.00 43.75 C ANISOU 2319 CA PRO A 262 5494 6119 5009 -150 -235 -138 C ATOM 2320 C PRO A 262 -18.799 10.450 -9.576 1.00 42.26 C ANISOU 2320 C PRO A 262 5270 5876 4912 -157 -207 -98 C ATOM 2321 O PRO A 262 -19.225 11.606 -9.416 1.00 42.51 O ANISOU 2321 O PRO A 262 5337 5832 4982 -135 -192 -130 O ATOM 2322 CB PRO A 262 -16.975 9.428 -8.171 1.00 38.03 C ANISOU 2322 CB PRO A 262 4750 5400 4300 -202 -318 -158 C ATOM 2323 CG PRO A 262 -16.788 8.050 -7.690 1.00 39.38 C ANISOU 2323 CG PRO A 262 4919 5645 4399 -184 -333 -132 C ATOM 2324 CD PRO A 262 -17.839 7.229 -8.403 1.00 41.15 C ANISOU 2324 CD PRO A 262 5121 5899 4616 -159 -254 -69 C ATOM 2325 N TYR A 263 -18.567 9.915 -10.781 1.00 39.54 N ANISOU 2325 N TYR A 263 4862 5562 4597 -184 -198 -28 N ATOM 2326 CA TYR A 263 -18.873 10.635 -12.015 1.00 36.55 C ANISOU 2326 CA TYR A 263 4456 5148 4281 -190 -174 31 C ATOM 2327 C TYR A 263 -20.342 11.024 -12.109 1.00 38.15 C ANISOU 2327 C TYR A 263 4668 5345 4484 -125 -132 50 C ATOM 2328 O TYR A 263 -20.659 12.181 -12.404 1.00 37.77 O ANISOU 2328 O TYR A 263 4635 5221 4496 -102 -125 65 O ATOM 2329 CB TYR A 263 -18.442 9.805 -13.218 1.00 37.96 C ANISOU 2329 CB TYR A 263 4579 5387 4458 -227 -165 92 C ATOM 2330 CG TYR A 263 -18.964 10.349 -14.509 1.00 38.88 C ANISOU 2330 CG TYR A 263 4677 5496 4600 -225 -141 165 C ATOM 2331 CD1 TYR A 263 -18.512 11.555 -15.037 1.00 40.13 C ANISOU 2331 CD1 TYR A 263 4847 5578 4823 -251 -143 199 C ATOM 2332 CD2 TYR A 263 -19.901 9.629 -15.226 1.00 34.36 C ANISOU 2332 CD2 TYR A 263 4077 4994 3984 -205 -120 205 C ATOM 2333 CE1 TYR A 263 -19.030 12.040 -16.229 1.00 36.51 C ANISOU 2333 CE1 TYR A 263 4382 5117 4373 -242 -126 286 C ATOM 2334 CE2 TYR A 263 -20.396 10.088 -16.411 1.00 35.13 C ANISOU 2334 CE2 TYR A 263 4160 5102 4086 -201 -114 277 C ATOM 2335 CZ TYR A 263 -19.970 11.289 -16.912 1.00 36.86 C ANISOU 2335 CZ TYR A 263 4400 5249 4357 -213 -118 324 C ATOM 2336 OH TYR A 263 -20.501 11.713 -18.105 1.00 37.40 O ANISOU 2336 OH TYR A 263 4462 5334 4414 -202 -117 414 O ATOM 2337 N HIS A 264 -21.263 10.090 -11.852 1.00 33.18 N ANISOU 2337 N HIS A 264 4020 4787 3799 -93 -101 54 N ATOM 2338 CA HIS A 264 -22.672 10.467 -11.964 1.00 36.80 C ANISOU 2338 CA HIS A 264 4458 5250 4273 -30 -61 73 C ATOM 2339 C HIS A 264 -23.079 11.462 -10.876 1.00 38.48 C ANISOU 2339 C HIS A 264 4724 5394 4502 27 -37 6 C ATOM 2340 O HIS A 264 -23.858 12.390 -11.139 1.00 39.29 O ANISOU 2340 O HIS A 264 4817 5447 4664 85 -15 21 O ATOM 2341 CB HIS A 264 -23.579 9.225 -11.996 1.00 33.77 C ANISOU 2341 CB HIS A 264 4027 4961 3841 -26 -29 92 C ATOM 2342 CG HIS A 264 -23.551 8.500 -13.312 1.00 44.42 C ANISOU 2342 CG HIS A 264 5324 6366 5187 -68 -48 150 C ATOM 2343 ND1 HIS A 264 -22.646 7.504 -13.612 1.00 46.72 N ANISOU 2343 ND1 HIS A 264 5618 6686 5449 -124 -63 150 N ATOM 2344 CD2 HIS A 264 -24.295 8.681 -14.436 1.00 47.84 C ANISOU 2344 CD2 HIS A 264 5705 6833 5640 -58 -57 207 C ATOM 2345 CE1 HIS A 264 -22.850 7.087 -14.854 1.00 49.27 C ANISOU 2345 CE1 HIS A 264 5900 7056 5766 -151 -70 192 C ATOM 2346 NE2 HIS A 264 -23.847 7.783 -15.375 1.00 44.18 N ANISOU 2346 NE2 HIS A 264 5222 6421 5142 -116 -74 229 N ATOM 2347 N THR A 265 -22.502 11.340 -9.676 1.00 38.78 N ANISOU 2347 N THR A 265 4823 5424 4487 14 -45 -70 N ATOM 2348 CA THR A 265 -22.834 12.282 -8.611 1.00 41.42 C ANISOU 2348 CA THR A 265 5225 5695 4819 63 -18 -155 C ATOM 2349 C THR A 265 -22.398 13.698 -8.989 1.00 44.23 C ANISOU 2349 C THR A 265 5610 5924 5271 61 -44 -171 C ATOM 2350 O THR A 265 -23.208 14.647 -8.980 1.00 43.05 O ANISOU 2350 O THR A 265 5473 5702 5182 131 -3 -184 O ATOM 2351 CB THR A 265 -22.164 11.833 -7.305 1.00 41.99 C ANISOU 2351 CB THR A 265 5366 5796 4792 38 -41 -232 C ATOM 2352 OG1 THR A 265 -22.585 10.496 -6.984 1.00 40.64 O ANISOU 2352 OG1 THR A 265 5177 5727 4539 39 -9 -198 O ATOM 2353 CG2 THR A 265 -22.553 12.749 -6.166 1.00 37.07 C ANISOU 2353 CG2 THR A 265 4826 5119 4141 87 -6 -337 C ATOM 2354 N LEU A 266 -21.107 13.856 -9.328 1.00 41.41 N ANISOU 2354 N LEU A 266 5260 5533 4942 -18 -107 -166 N ATOM 2355 CA LEU A 266 -20.584 15.183 -9.645 1.00 42.65 C ANISOU 2355 CA LEU A 266 5450 5557 5199 -41 -128 -179 C ATOM 2356 C LEU A 266 -21.238 15.751 -10.891 1.00 42.49 C ANISOU 2356 C LEU A 266 5393 5491 5260 -4 -101 -75 C ATOM 2357 O LEU A 266 -21.509 16.954 -10.946 1.00 42.36 O ANISOU 2357 O LEU A 266 5417 5349 5330 33 -87 -82 O ATOM 2358 CB LEU A 266 -19.062 15.149 -9.810 1.00 40.47 C ANISOU 2358 CB LEU A 266 5165 5268 4943 -145 -194 -186 C ATOM 2359 CG LEU A 266 -18.299 14.887 -8.515 1.00 48.03 C ANISOU 2359 CG LEU A 266 6165 6251 5833 -181 -247 -295 C ATOM 2360 CD1 LEU A 266 -16.808 14.686 -8.750 1.00 50.80 C ANISOU 2360 CD1 LEU A 266 6469 6615 6215 -280 -319 -291 C ATOM 2361 CD2 LEU A 266 -18.523 16.065 -7.591 1.00 50.96 C ANISOU 2361 CD2 LEU A 266 6628 6511 6225 -161 -244 -408 C ATOM 2362 N ARG A 267 -21.514 14.901 -11.886 1.00 40.61 N ANISOU 2362 N ARG A 267 5084 5351 4994 -9 -99 21 N ATOM 2363 CA ARG A 267 -22.184 15.345 -13.100 1.00 40.31 C ANISOU 2363 CA ARG A 267 5011 5298 5008 29 -89 129 C ATOM 2364 C ARG A 267 -23.534 15.965 -12.764 1.00 44.61 C ANISOU 2364 C ARG A 267 5555 5803 5592 142 -50 121 C ATOM 2365 O ARG A 267 -23.878 17.056 -13.256 1.00 42.22 O ANISOU 2365 O ARG A 267 5268 5396 5378 193 -47 172 O ATOM 2366 CB ARG A 267 -22.366 14.148 -14.033 1.00 41.61 C ANISOU 2366 CB ARG A 267 5106 5598 5108 4 -96 203 C ATOM 2367 CG ARG A 267 -22.774 14.518 -15.429 1.00 50.04 C ANISOU 2367 CG ARG A 267 6143 6672 6199 20 -107 321 C ATOM 2368 CD ARG A 267 -22.926 13.317 -16.385 1.00 50.07 C ANISOU 2368 CD ARG A 267 6088 6813 6123 -15 -119 373 C ATOM 2369 NE ARG A 267 -24.155 12.540 -16.226 1.00 52.13 N ANISOU 2369 NE ARG A 267 6292 7167 6347 32 -112 363 N ATOM 2370 CZ ARG A 267 -24.378 11.384 -16.847 1.00 47.83 C ANISOU 2370 CZ ARG A 267 5701 6737 5736 -5 -123 379 C ATOM 2371 NH1 ARG A 267 -23.427 10.856 -17.607 1.00 43.76 N ANISOU 2371 NH1 ARG A 267 5196 6254 5175 -78 -132 397 N ATOM 2372 NH2 ARG A 267 -25.533 10.749 -16.704 1.00 44.26 N ANISOU 2372 NH2 ARG A 267 5188 6360 5267 26 -117 370 N ATOM 2373 N THR A 268 -24.315 15.277 -11.914 1.00 38.45 N ANISOU 2373 N THR A 268 4754 5101 4754 187 -14 62 N ATOM 2374 CA THR A 268 -25.648 15.764 -11.576 1.00 38.15 C ANISOU 2374 CA THR A 268 4691 5045 4758 300 38 50 C ATOM 2375 C THR A 268 -25.570 17.123 -10.884 1.00 42.13 C ANISOU 2375 C THR A 268 5279 5391 5339 352 63 -26 C ATOM 2376 O THR A 268 -26.288 18.066 -11.253 1.00 42.15 O ANISOU 2376 O THR A 268 5271 5306 5438 442 82 12 O ATOM 2377 CB THR A 268 -26.372 14.737 -10.698 1.00 38.81 C ANISOU 2377 CB THR A 268 4740 5245 4761 319 90 -4 C ATOM 2378 OG1 THR A 268 -26.477 13.494 -11.402 1.00 34.79 O ANISOU 2378 OG1 THR A 268 4158 4861 4198 265 67 64 O ATOM 2379 CG2 THR A 268 -27.770 15.217 -10.351 1.00 38.73 C ANISOU 2379 CG2 THR A 268 4683 5230 4804 437 159 -18 C ATOM 2380 N VAL A 269 -24.669 17.259 -9.900 1.00 38.97 N ANISOU 2380 N VAL A 269 4963 4943 4900 296 55 -136 N ATOM 2381 CA VAL A 269 -24.588 18.540 -9.195 1.00 40.15 C ANISOU 2381 CA VAL A 269 5204 4933 5119 335 78 -233 C ATOM 2382 C VAL A 269 -24.061 19.646 -10.118 1.00 40.29 C ANISOU 2382 C VAL A 269 5249 4798 5262 313 42 -165 C ATOM 2383 O VAL A 269 -24.508 20.800 -10.046 1.00 36.40 O ANISOU 2383 O VAL A 269 4802 4155 4874 389 74 -185 O ATOM 2384 CB VAL A 269 -23.745 18.409 -7.915 1.00 47.49 C ANISOU 2384 CB VAL A 269 6221 5862 5962 271 62 -376 C ATOM 2385 CG1 VAL A 269 -23.581 19.778 -7.239 1.00 51.64 C ANISOU 2385 CG1 VAL A 269 6852 6210 6560 295 77 -495 C ATOM 2386 CG2 VAL A 269 -24.406 17.437 -6.956 1.00 46.53 C ANISOU 2386 CG2 VAL A 269 6089 5877 5713 308 114 -429 C ATOM 2387 N HIS A 270 -23.122 19.319 -11.008 1.00 42.15 N ANISOU 2387 N HIS A 270 5460 5063 5494 212 -13 -79 N ATOM 2388 CA HIS A 270 -22.619 20.312 -11.950 1.00 42.33 C ANISOU 2388 CA HIS A 270 5508 4949 5626 179 -34 7 C ATOM 2389 C HIS A 270 -23.749 20.837 -12.830 1.00 45.30 C ANISOU 2389 C HIS A 270 5850 5288 6074 294 -13 128 C ATOM 2390 O HIS A 270 -23.873 22.052 -13.043 1.00 43.75 O ANISOU 2390 O HIS A 270 5709 4918 5997 339 -1 157 O ATOM 2391 CB HIS A 270 -21.508 19.692 -12.803 1.00 43.58 C ANISOU 2391 CB HIS A 270 5628 5182 5749 57 -78 86 C ATOM 2392 CG HIS A 270 -20.870 20.647 -13.767 1.00 48.29 C ANISOU 2392 CG HIS A 270 6252 5651 6446 2 -86 184 C ATOM 2393 ND1 HIS A 270 -19.961 21.605 -13.375 1.00 51.98 N ANISOU 2393 ND1 HIS A 270 6787 5959 7005 -75 -95 122 N ATOM 2394 CD2 HIS A 270 -21.023 20.802 -15.103 1.00 49.40 C ANISOU 2394 CD2 HIS A 270 6367 5798 6605 7 -86 343 C ATOM 2395 CE1 HIS A 270 -19.572 22.301 -14.429 1.00 50.56 C ANISOU 2395 CE1 HIS A 270 6620 5685 6906 -118 -88 247 C ATOM 2396 NE2 HIS A 270 -20.202 21.832 -15.490 1.00 50.87 N ANISOU 2396 NE2 HIS A 270 6607 5827 6893 -66 -82 387 N ATOM 2397 N LEU A 271 -24.595 19.931 -13.340 1.00 44.47 N ANISOU 2397 N LEU A 271 5654 5341 5903 342 -14 201 N ATOM 2398 CA LEU A 271 -25.729 20.365 -14.158 1.00 52.57 C ANISOU 2398 CA LEU A 271 6628 6357 6990 457 -12 317 C ATOM 2399 C LEU A 271 -26.715 21.209 -13.362 1.00 52.79 C ANISOU 2399 C LEU A 271 6672 6278 7108 596 43 248 C ATOM 2400 O LEU A 271 -27.228 22.210 -13.873 1.00 47.27 O ANISOU 2400 O LEU A 271 5982 5457 6521 690 43 328 O ATOM 2401 CB LEU A 271 -26.457 19.163 -14.763 1.00 55.65 C ANISOU 2401 CB LEU A 271 6907 6948 7289 468 -33 384 C ATOM 2402 CG LEU A 271 -25.794 18.355 -15.868 1.00 53.15 C ANISOU 2402 CG LEU A 271 6563 6743 6889 364 -82 475 C ATOM 2403 CD1 LEU A 271 -26.625 17.120 -16.144 1.00 53.89 C ANISOU 2403 CD1 LEU A 271 6556 7023 6898 375 -95 491 C ATOM 2404 CD2 LEU A 271 -25.724 19.224 -17.111 1.00 51.15 C ANISOU 2404 CD2 LEU A 271 6331 6416 6688 381 -117 626 C ATOM 2405 N THR A 272 -27.010 20.814 -12.117 1.00 56.66 N ANISOU 2405 N THR A 272 7167 6813 7549 618 95 105 N ATOM 2406 CA THR A 272 -28.060 21.504 -11.360 1.00 56.12 C ANISOU 2406 CA THR A 272 7100 6669 7555 761 168 30 C ATOM 2407 C THR A 272 -27.667 22.933 -10.995 1.00 52.80 C ANISOU 2407 C THR A 272 6799 6008 7253 793 189 -34 C ATOM 2408 O THR A 272 -28.529 23.813 -10.902 1.00 50.41 O ANISOU 2408 O THR A 272 6496 5591 7065 934 237 -37 O ATOM 2409 CB THR A 272 -28.412 20.706 -10.104 1.00 55.49 C ANISOU 2409 CB THR A 272 7009 6703 7370 765 233 -106 C ATOM 2410 OG1 THR A 272 -28.940 19.435 -10.490 1.00 57.03 O ANISOU 2410 OG1 THR A 272 7088 7097 7483 744 223 -37 O ATOM 2411 CG2 THR A 272 -29.438 21.429 -9.252 1.00 57.70 C ANISOU 2411 CG2 THR A 272 7295 6909 7719 912 331 -201 C ATOM 2412 N THR A 273 -26.385 23.191 -10.781 1.00 53.43 N ANISOU 2412 N THR A 273 6976 6003 7321 665 154 -91 N ATOM 2413 CA THR A 273 -25.952 24.498 -10.309 1.00 55.30 C ANISOU 2413 CA THR A 273 7335 6005 7671 670 173 -180 C ATOM 2414 C THR A 273 -25.364 25.352 -11.414 1.00 59.61 C ANISOU 2414 C THR A 273 7917 6396 8336 626 130 -44 C ATOM 2415 O THR A 273 -24.887 26.455 -11.133 1.00 61.03 O ANISOU 2415 O THR A 273 8204 6359 8628 605 141 -106 O ATOM 2416 CB THR A 273 -24.923 24.347 -9.184 1.00 55.60 C ANISOU 2416 CB THR A 273 7461 6037 7628 550 161 -356 C ATOM 2417 OG1 THR A 273 -23.751 23.686 -9.688 1.00 57.09 O ANISOU 2417 OG1 THR A 273 7627 6311 7754 393 86 -297 O ATOM 2418 CG2 THR A 273 -25.508 23.525 -8.045 1.00 49.62 C ANISOU 2418 CG2 THR A 273 6687 5431 6736 595 212 -479 C ATOM 2419 N TRP A 274 -25.400 24.878 -12.657 1.00 63.77 N ANISOU 2419 N TRP A 274 8367 7025 8839 606 85 137 N ATOM 2420 CA TRP A 274 -24.682 25.544 -13.734 1.00 67.11 C ANISOU 2420 CA TRP A 274 8829 7329 9339 536 49 279 C ATOM 2421 C TRP A 274 -25.292 26.914 -13.998 1.00 71.58 C ANISOU 2421 C TRP A 274 9457 7666 10076 661 76 342 C ATOM 2422 O TRP A 274 -26.516 27.075 -14.011 1.00 71.97 O ANISOU 2422 O TRP A 274 9455 7722 10167 828 99 374 O ATOM 2423 CB TRP A 274 -24.751 24.722 -15.018 1.00 67.67 C ANISOU 2423 CB TRP A 274 8811 7577 9324 509 2 458 C ATOM 2424 CG TRP A 274 -23.846 25.242 -16.085 1.00 68.88 C ANISOU 2424 CG TRP A 274 9011 7643 9519 410 -22 599 C ATOM 2425 CD1 TRP A 274 -22.490 25.119 -16.128 1.00 68.55 C ANISOU 2425 CD1 TRP A 274 9000 7590 9457 242 -29 573 C ATOM 2426 CD2 TRP A 274 -24.203 26.101 -17.173 1.00 72.58 C ANISOU 2426 CD2 TRP A 274 9506 8000 10072 475 -32 787 C ATOM 2427 NE1 TRP A 274 -21.990 25.764 -17.233 1.00 72.66 N ANISOU 2427 NE1 TRP A 274 9557 8016 10033 189 -32 737 N ATOM 2428 CE2 TRP A 274 -23.021 26.389 -17.883 1.00 72.47 C ANISOU 2428 CE2 TRP A 274 9543 7925 10068 330 -35 875 C ATOM 2429 CE3 TRP A 274 -25.412 26.624 -17.638 1.00 77.30 C ANISOU 2429 CE3 TRP A 274 10081 8554 10734 646 -41 901 C ATOM 2430 CZ2 TRP A 274 -23.012 27.180 -19.031 1.00 72.09 C ANISOU 2430 CZ2 TRP A 274 9541 7769 10079 344 -40 1078 C ATOM 2431 CZ3 TRP A 274 -25.402 27.410 -18.778 1.00 77.69 C ANISOU 2431 CZ3 TRP A 274 10176 8497 10845 670 -63 1104 C ATOM 2432 CH2 TRP A 274 -24.210 27.681 -19.460 1.00 74.38 C ANISOU 2432 CH2 TRP A 274 9825 8015 10422 517 -59 1194 C ATOM 2433 N LYS A 275 -24.431 27.905 -14.213 1.00 78.70 N ANISOU 2433 N LYS A 275 10460 8355 11087 580 74 364 N ATOM 2434 CA LYS A 275 -24.856 29.261 -14.539 1.00 80.23 C ANISOU 2434 CA LYS A 275 10732 8293 11461 684 99 442 C ATOM 2435 C LYS A 275 -23.904 29.839 -15.575 1.00 83.65 C ANISOU 2435 C LYS A 275 11223 8605 11956 562 76 603 C ATOM 2436 O LYS A 275 -22.726 29.475 -15.639 1.00 83.34 O ANISOU 2436 O LYS A 275 11189 8614 11861 381 59 579 O ATOM 2437 CB LYS A 275 -24.920 30.161 -13.297 1.00 77.09 C ANISOU 2437 CB LYS A 275 10437 7679 11174 729 156 236 C ATOM 2438 CG LYS A 275 -26.011 29.781 -12.318 1.00 75.23 C ANISOU 2438 CG LYS A 275 10153 7540 10892 877 205 93 C ATOM 2439 CD LYS A 275 -26.033 30.728 -11.133 1.00 80.90 C ANISOU 2439 CD LYS A 275 10991 8037 11708 920 270 -120 C ATOM 2440 CE LYS A 275 -27.220 30.436 -10.220 1.00 85.98 C ANISOU 2440 CE LYS A 275 11586 8772 12312 1087 344 -250 C ATOM 2441 NZ LYS A 275 -27.131 29.104 -9.550 1.00 88.17 N ANISOU 2441 NZ LYS A 275 11793 9324 12382 1016 339 -346 N ATOM 2442 N VAL A 276 -24.433 30.762 -16.381 1.00 89.01 N ANISOU 2442 N VAL A 276 11942 9122 12757 669 80 776 N ATOM 2443 CA VAL A 276 -23.773 31.139 -17.631 1.00 90.34 C ANISOU 2443 CA VAL A 276 12148 9229 12948 577 60 993 C ATOM 2444 C VAL A 276 -22.440 31.831 -17.364 1.00 86.09 C ANISOU 2444 C VAL A 276 11712 8491 12506 390 88 928 C ATOM 2445 O VAL A 276 -21.421 31.514 -17.993 1.00 86.32 O ANISOU 2445 O VAL A 276 11729 8592 12478 223 80 1007 O ATOM 2446 CB VAL A 276 -24.702 32.026 -18.479 1.00 95.76 C ANISOU 2446 CB VAL A 276 12865 9774 13747 750 52 1201 C ATOM 2447 CG1 VAL A 276 -23.979 32.502 -19.727 1.00 96.04 C ANISOU 2447 CG1 VAL A 276 12964 9728 13798 648 43 1434 C ATOM 2448 CG2 VAL A 276 -25.970 31.270 -18.845 1.00 97.44 C ANISOU 2448 CG2 VAL A 276 12949 10214 13859 916 7 1275 C ATOM 2449 N GLY A 277 -22.424 32.789 -16.443 1.00 78.33 N ANISOU 2449 N GLY A 277 10827 7259 11677 412 124 777 N ATOM 2450 CA GLY A 277 -21.233 33.591 -16.255 1.00 75.80 C ANISOU 2450 CA GLY A 277 10606 6717 11477 233 144 724 C ATOM 2451 C GLY A 277 -20.420 33.260 -15.022 1.00 73.48 C ANISOU 2451 C GLY A 277 10315 6460 11146 95 134 458 C ATOM 2452 O GLY A 277 -19.793 34.150 -14.437 1.00 77.95 O ANISOU 2452 O GLY A 277 10980 6790 11848 -1 150 334 O ATOM 2453 N LEU A 278 -20.405 31.990 -14.617 1.00 64.25 N ANISOU 2453 N LEU A 278 9042 5578 9791 78 102 368 N ATOM 2454 CA LEU A 278 -19.711 31.587 -13.406 1.00 60.97 C ANISOU 2454 CA LEU A 278 8626 5224 9314 -33 78 126 C ATOM 2455 C LEU A 278 -18.883 30.344 -13.689 1.00 61.75 C ANISOU 2455 C LEU A 278 8613 5594 9257 -165 34 154 C ATOM 2456 O LEU A 278 -19.344 29.415 -14.357 1.00 65.40 O ANISOU 2456 O LEU A 278 8984 6269 9596 -103 26 277 O ATOM 2457 CB LEU A 278 -20.710 31.353 -12.266 1.00 65.40 C ANISOU 2457 CB LEU A 278 9197 5836 9816 121 96 -56 C ATOM 2458 CG LEU A 278 -21.435 32.638 -11.824 1.00 73.23 C ANISOU 2458 CG LEU A 278 10306 6539 10977 253 152 -128 C ATOM 2459 CD1 LEU A 278 -22.549 32.348 -10.844 1.00 82.17 C ANISOU 2459 CD1 LEU A 278 11429 7749 12041 427 193 -280 C ATOM 2460 CD2 LEU A 278 -20.475 33.649 -11.218 1.00 72.52 C ANISOU 2460 CD2 LEU A 278 10341 6192 11022 108 151 -280 C ATOM 2461 N CYS A 279 -17.653 30.339 -13.177 1.00 63.53 N ANISOU 2461 N CYS A 279 8840 5804 9495 -347 2 34 N ATOM 2462 CA CYS A 279 -16.684 29.301 -13.516 1.00 65.40 C ANISOU 2462 CA CYS A 279 8967 6261 9623 -482 -35 69 C ATOM 2463 C CYS A 279 -16.906 28.015 -12.726 1.00 64.41 C ANISOU 2463 C CYS A 279 8768 6388 9315 -437 -74 -51 C ATOM 2464 O CYS A 279 -16.885 26.921 -13.299 1.00 65.07 O ANISOU 2464 O CYS A 279 8756 6690 9279 -433 -83 43 O ATOM 2465 CB CYS A 279 -15.270 29.831 -13.284 1.00 70.23 C ANISOU 2465 CB CYS A 279 9588 6758 10338 -694 -59 -5 C ATOM 2466 SG CYS A 279 -14.802 31.150 -14.413 1.00 79.49 S ANISOU 2466 SG CYS A 279 10827 7660 11717 -790 0 181 S ATOM 2467 N LYS A 280 -17.115 28.128 -11.413 1.00 60.30 N ANISOU 2467 N LYS A 280 8304 5837 8771 -405 -94 -258 N ATOM 2468 CA LYS A 280 -17.168 26.977 -10.505 1.00 50.65 C ANISOU 2468 CA LYS A 280 7032 4837 7376 -385 -133 -381 C ATOM 2469 C LYS A 280 -15.995 26.026 -10.739 1.00 49.53 C ANISOU 2469 C LYS A 280 6786 4872 7162 -525 -189 -354 C ATOM 2470 O LYS A 280 -16.161 24.813 -10.873 1.00 48.58 O ANISOU 2470 O LYS A 280 6584 4967 6907 -488 -200 -309 O ATOM 2471 CB LYS A 280 -18.498 26.230 -10.608 1.00 46.22 C ANISOU 2471 CB LYS A 280 6433 4421 6708 -210 -94 -323 C ATOM 2472 CG LYS A 280 -19.693 27.011 -10.114 1.00 54.42 C ANISOU 2472 CG LYS A 280 7552 5320 7803 -53 -36 -386 C ATOM 2473 CD LYS A 280 -20.955 26.175 -10.178 1.00 63.65 C ANISOU 2473 CD LYS A 280 8654 6661 8870 102 1 -333 C ATOM 2474 CE LYS A 280 -22.158 26.935 -9.648 1.00 65.48 C ANISOU 2474 CE LYS A 280 8945 6766 9168 270 70 -402 C ATOM 2475 NZ LYS A 280 -22.505 28.075 -10.552 1.00 61.48 N ANISOU 2475 NZ LYS A 280 8475 6048 8838 335 96 -272 N ATOM 2476 N ASP A 281 -14.786 26.593 -10.756 1.00 51.41 N ANISOU 2476 N ASP A 281 7023 5009 7502 -690 -224 -388 N ATOM 2477 CA ASP A 281 -13.613 25.836 -11.186 1.00 59.96 C ANISOU 2477 CA ASP A 281 7988 6239 8556 -821 -263 -336 C ATOM 2478 C ASP A 281 -13.334 24.614 -10.313 1.00 60.56 C ANISOU 2478 C ASP A 281 8000 6533 8475 -816 -331 -442 C ATOM 2479 O ASP A 281 -12.829 23.604 -10.815 1.00 60.01 O ANISOU 2479 O ASP A 281 7822 6638 8343 -846 -343 -362 O ATOM 2480 CB ASP A 281 -12.399 26.759 -11.237 1.00 64.57 C ANISOU 2480 CB ASP A 281 8571 6664 9298 -1004 -286 -371 C ATOM 2481 CG ASP A 281 -12.462 27.727 -12.406 1.00 71.31 C ANISOU 2481 CG ASP A 281 9462 7334 10299 -1033 -207 -202 C ATOM 2482 OD1 ASP A 281 -13.033 27.349 -13.451 1.00 71.65 O ANISOU 2482 OD1 ASP A 281 9480 7452 10293 -949 -150 -22 O ATOM 2483 OD2 ASP A 281 -11.966 28.868 -12.279 1.00 76.31 O ANISOU 2483 OD2 ASP A 281 10158 7745 11092 -1140 -204 -247 O ATOM 2484 N ARG A 282 -13.679 24.661 -9.028 1.00 58.28 N ANISOU 2484 N ARG A 282 7784 6241 8118 -771 -372 -615 N ATOM 2485 CA ARG A 282 -13.348 23.546 -8.145 1.00 54.93 C ANISOU 2485 CA ARG A 282 7314 6017 7541 -771 -444 -705 C ATOM 2486 C ARG A 282 -14.261 22.349 -8.398 1.00 51.77 C ANISOU 2486 C ARG A 282 6873 5794 7002 -639 -402 -613 C ATOM 2487 O ARG A 282 -13.788 21.216 -8.592 1.00 51.92 O ANISOU 2487 O ARG A 282 6798 5985 6944 -658 -432 -560 O ATOM 2488 CB ARG A 282 -13.443 24.014 -6.702 1.00 56.49 C ANISOU 2488 CB ARG A 282 7618 6157 7688 -769 -496 -915 C ATOM 2489 CG ARG A 282 -12.445 25.100 -6.376 1.00 66.45 C ANISOU 2489 CG ARG A 282 8913 7253 9081 -922 -558 -1030 C ATOM 2490 CD ARG A 282 -12.650 25.616 -4.970 1.00 76.01 C ANISOU 2490 CD ARG A 282 10252 8402 10226 -912 -605 -1254 C ATOM 2491 NE ARG A 282 -11.717 26.684 -4.623 1.00 87.20 N ANISOU 2491 NE ARG A 282 11708 9649 11774 -1072 -673 -1386 N ATOM 2492 CZ ARG A 282 -11.947 27.981 -4.827 1.00 92.96 C ANISOU 2492 CZ ARG A 282 12535 10119 12665 -1095 -618 -1425 C ATOM 2493 NH1 ARG A 282 -13.076 28.379 -5.400 1.00 93.27 N ANISOU 2493 NH1 ARG A 282 12636 10046 12756 -956 -499 -1330 N ATOM 2494 NH2 ARG A 282 -11.041 28.883 -4.468 1.00 94.64 N ANISOU 2494 NH2 ARG A 282 12780 10181 12999 -1260 -688 -1556 N ATOM 2495 N LEU A 283 -15.576 22.586 -8.417 1.00 51.79 N ANISOU 2495 N LEU A 283 6939 5752 6987 -504 -329 -594 N ATOM 2496 CA LEU A 283 -16.504 21.527 -8.803 1.00 48.74 C ANISOU 2496 CA LEU A 283 6502 5520 6495 -393 -284 -495 C ATOM 2497 C LEU A 283 -16.200 21.015 -10.204 1.00 45.40 C ANISOU 2497 C LEU A 283 5982 5167 6099 -426 -267 -321 C ATOM 2498 O LEU A 283 -16.235 19.801 -10.452 1.00 45.54 O ANISOU 2498 O LEU A 283 5929 5354 6019 -407 -271 -267 O ATOM 2499 CB LEU A 283 -17.948 22.023 -8.699 1.00 45.01 C ANISOU 2499 CB LEU A 283 6091 4976 6033 -248 -209 -496 C ATOM 2500 CG LEU A 283 -19.042 21.033 -9.111 1.00 46.93 C ANISOU 2500 CG LEU A 283 6274 5370 6189 -137 -161 -399 C ATOM 2501 CD1 LEU A 283 -19.014 19.747 -8.295 1.00 36.53 C ANISOU 2501 CD1 LEU A 283 4929 4236 4715 -134 -184 -455 C ATOM 2502 CD2 LEU A 283 -20.405 21.722 -8.966 1.00 48.56 C ANISOU 2502 CD2 LEU A 283 6524 5487 6438 4 -88 -409 C ATOM 2503 N HIS A 284 -15.850 21.919 -11.121 1.00 42.86 N ANISOU 2503 N HIS A 284 5666 4712 5906 -481 -244 -234 N ATOM 2504 CA HIS A 284 -15.627 21.511 -12.502 1.00 47.33 C ANISOU 2504 CA HIS A 284 6157 5346 6481 -508 -213 -65 C ATOM 2505 C HIS A 284 -14.382 20.625 -12.604 1.00 45.54 C ANISOU 2505 C HIS A 284 5834 5250 6217 -615 -251 -69 C ATOM 2506 O HIS A 284 -14.390 19.607 -13.310 1.00 44.25 O ANISOU 2506 O HIS A 284 5601 5232 5980 -598 -233 15 O ATOM 2507 CB HIS A 284 -15.534 22.767 -13.375 1.00 53.07 C ANISOU 2507 CB HIS A 284 6928 5889 7348 -544 -173 35 C ATOM 2508 CG HIS A 284 -15.685 22.514 -14.842 1.00 53.96 C ANISOU 2508 CG HIS A 284 6997 6062 7445 -535 -129 224 C ATOM 2509 ND1 HIS A 284 -15.484 23.499 -15.786 1.00 55.57 N ANISOU 2509 ND1 HIS A 284 7236 6125 7752 -578 -89 351 N ATOM 2510 CD2 HIS A 284 -16.036 21.401 -15.530 1.00 53.90 C ANISOU 2510 CD2 HIS A 284 6923 6235 7320 -490 -118 306 C ATOM 2511 CE1 HIS A 284 -15.708 23.006 -16.992 1.00 53.68 C ANISOU 2511 CE1 HIS A 284 6958 5993 7445 -557 -57 506 C ATOM 2512 NE2 HIS A 284 -16.045 21.735 -16.864 1.00 54.47 N ANISOU 2512 NE2 HIS A 284 6996 6288 7414 -505 -76 472 N ATOM 2513 N LYS A 285 -13.328 20.965 -11.854 1.00 43.34 N ANISOU 2513 N LYS A 285 5550 4927 5992 -721 -309 -179 N ATOM 2514 CA LYS A 285 -12.128 20.131 -11.817 1.00 46.95 C ANISOU 2514 CA LYS A 285 5899 5512 6428 -809 -356 -193 C ATOM 2515 C LYS A 285 -12.432 18.738 -11.282 1.00 51.05 C ANISOU 2515 C LYS A 285 6385 6211 6800 -729 -386 -223 C ATOM 2516 O LYS A 285 -11.979 17.726 -11.854 1.00 47.55 O ANISOU 2516 O LYS A 285 5851 5896 6319 -737 -377 -157 O ATOM 2517 CB LYS A 285 -11.056 20.811 -10.974 1.00 44.65 C ANISOU 2517 CB LYS A 285 5603 5141 6221 -931 -433 -320 C ATOM 2518 CG LYS A 285 -9.719 20.101 -11.005 1.00 52.24 C ANISOU 2518 CG LYS A 285 6428 6224 7195 -1027 -486 -325 C ATOM 2519 CD LYS A 285 -8.650 20.928 -10.319 1.00 57.56 C ANISOU 2519 CD LYS A 285 7082 6810 7979 -1168 -567 -442 C ATOM 2520 CE LYS A 285 -7.295 20.250 -10.410 1.00 61.81 C ANISOU 2520 CE LYS A 285 7456 7475 8552 -1259 -621 -438 C ATOM 2521 NZ LYS A 285 -6.236 21.103 -9.792 1.00 67.27 N ANISOU 2521 NZ LYS A 285 8109 8085 9366 -1413 -709 -551 N ATOM 2522 N ALA A 286 -13.203 18.667 -10.190 1.00 48.17 N ANISOU 2522 N ALA A 286 6098 5850 6354 -650 -411 -321 N ATOM 2523 CA ALA A 286 -13.595 17.360 -9.668 1.00 46.30 C ANISOU 2523 CA ALA A 286 5844 5770 5978 -574 -427 -334 C ATOM 2524 C ALA A 286 -14.351 16.546 -10.722 1.00 43.27 C ANISOU 2524 C ALA A 286 5419 5469 5551 -506 -356 -206 C ATOM 2525 O ALA A 286 -14.150 15.324 -10.846 1.00 40.13 O ANISOU 2525 O ALA A 286 4963 5201 5084 -492 -363 -175 O ATOM 2526 CB ALA A 286 -14.434 17.539 -8.402 1.00 43.96 C ANISOU 2526 CB ALA A 286 5649 5456 5596 -501 -438 -447 C ATOM 2527 N LEU A 287 -15.225 17.211 -11.497 1.00 42.92 N ANISOU 2527 N LEU A 287 5409 5348 5550 -461 -293 -133 N ATOM 2528 CA LEU A 287 -15.957 16.512 -12.560 1.00 40.30 C ANISOU 2528 CA LEU A 287 5039 5100 5174 -405 -241 -16 C ATOM 2529 C LEU A 287 -15.014 15.981 -13.639 1.00 40.34 C ANISOU 2529 C LEU A 287 4964 5172 5193 -478 -229 67 C ATOM 2530 O LEU A 287 -15.155 14.836 -14.078 1.00 37.46 O ANISOU 2530 O LEU A 287 4552 4927 4754 -453 -214 105 O ATOM 2531 CB LEU A 287 -17.025 17.423 -13.181 1.00 37.43 C ANISOU 2531 CB LEU A 287 4721 4641 4858 -340 -195 54 C ATOM 2532 CG LEU A 287 -17.792 16.832 -14.389 1.00 39.88 C ANISOU 2532 CG LEU A 287 4989 5041 5120 -291 -159 179 C ATOM 2533 CD1 LEU A 287 -18.540 15.548 -14.046 1.00 41.57 C ANISOU 2533 CD1 LEU A 287 5172 5395 5229 -231 -157 155 C ATOM 2534 CD2 LEU A 287 -18.755 17.854 -14.994 1.00 38.22 C ANISOU 2534 CD2 LEU A 287 4818 4733 4969 -221 -132 260 C ATOM 2535 N VAL A 288 -14.088 16.822 -14.109 1.00 38.69 N ANISOU 2535 N VAL A 288 4739 4878 5082 -569 -224 94 N ATOM 2536 CA VAL A 288 -13.084 16.407 -15.092 1.00 41.44 C ANISOU 2536 CA VAL A 288 5005 5290 5451 -646 -195 165 C ATOM 2537 C VAL A 288 -12.348 15.144 -14.638 1.00 41.97 C ANISOU 2537 C VAL A 288 4994 5486 5467 -654 -230 110 C ATOM 2538 O VAL A 288 -12.130 14.206 -15.428 1.00 41.88 O ANISOU 2538 O VAL A 288 4924 5576 5411 -648 -191 163 O ATOM 2539 CB VAL A 288 -12.118 17.575 -15.366 1.00 44.11 C ANISOU 2539 CB VAL A 288 5335 5507 5919 -759 -185 183 C ATOM 2540 CG1 VAL A 288 -10.906 17.126 -16.151 1.00 45.75 C ANISOU 2540 CG1 VAL A 288 5437 5791 6157 -847 -149 233 C ATOM 2541 CG2 VAL A 288 -12.857 18.648 -16.156 1.00 47.26 C ANISOU 2541 CG2 VAL A 288 5810 5784 6362 -739 -134 285 C ATOM 2542 N ILE A 289 -11.969 15.086 -13.358 1.00 38.07 N ANISOU 2542 N ILE A 289 4504 4989 4973 -661 -305 1 N ATOM 2543 CA ILE A 289 -11.251 13.898 -12.890 1.00 41.70 C ANISOU 2543 CA ILE A 289 4890 5564 5389 -657 -350 -37 C ATOM 2544 C ILE A 289 -12.150 12.663 -12.911 1.00 46.51 C ANISOU 2544 C ILE A 289 5518 6269 5886 -561 -327 -14 C ATOM 2545 O ILE A 289 -11.736 11.576 -13.354 1.00 49.00 O ANISOU 2545 O ILE A 289 5769 6673 6177 -550 -310 16 O ATOM 2546 CB ILE A 289 -10.650 14.139 -11.498 1.00 42.36 C ANISOU 2546 CB ILE A 289 4981 5633 5482 -686 -452 -151 C ATOM 2547 CG1 ILE A 289 -9.560 15.215 -11.587 1.00 46.08 C ANISOU 2547 CG1 ILE A 289 5404 6020 6084 -807 -480 -178 C ATOM 2548 CG2 ILE A 289 -10.124 12.848 -10.931 1.00 38.83 C ANISOU 2548 CG2 ILE A 289 4474 5306 4973 -652 -508 -173 C ATOM 2549 CD1 ILE A 289 -9.056 15.700 -10.245 1.00 44.54 C ANISOU 2549 CD1 ILE A 289 5231 5793 5899 -851 -593 -306 C ATOM 2550 N THR A 290 -13.393 12.794 -12.444 1.00 44.04 N ANISOU 2550 N THR A 290 5289 5932 5511 -491 -319 -30 N ATOM 2551 CA THR A 290 -14.194 11.574 -12.413 1.00 44.95 C ANISOU 2551 CA THR A 290 5411 6137 5532 -418 -297 -10 C ATOM 2552 C THR A 290 -14.647 11.171 -13.814 1.00 44.55 C ANISOU 2552 C THR A 290 5332 6125 5470 -409 -230 79 C ATOM 2553 O THR A 290 -14.913 9.989 -14.065 1.00 43.75 O ANISOU 2553 O THR A 290 5209 6102 5311 -379 -211 95 O ATOM 2554 CB THR A 290 -15.370 11.718 -11.443 1.00 47.16 C ANISOU 2554 CB THR A 290 5771 6400 5749 -351 -299 -56 C ATOM 2555 OG1 THR A 290 -16.256 12.753 -11.869 1.00 47.92 O ANISOU 2555 OG1 THR A 290 5908 6419 5882 -327 -259 -31 O ATOM 2556 CG2 THR A 290 -14.841 12.045 -10.035 1.00 45.04 C ANISOU 2556 CG2 THR A 290 5543 6108 5461 -364 -370 -154 C ATOM 2557 N LEU A 291 -14.677 12.118 -14.757 1.00 41.45 N ANISOU 2557 N LEU A 291 4943 5676 5129 -441 -195 138 N ATOM 2558 CA LEU A 291 -14.896 11.751 -16.155 1.00 43.24 C ANISOU 2558 CA LEU A 291 5145 5955 5328 -444 -140 223 C ATOM 2559 C LEU A 291 -13.727 10.932 -16.701 1.00 44.63 C ANISOU 2559 C LEU A 291 5247 6200 5509 -491 -117 228 C ATOM 2560 O LEU A 291 -13.936 9.924 -17.395 1.00 40.26 O ANISOU 2560 O LEU A 291 4675 5726 4894 -471 -82 247 O ATOM 2561 CB LEU A 291 -15.151 12.997 -17.009 1.00 35.14 C ANISOU 2561 CB LEU A 291 4151 4853 4347 -464 -111 302 C ATOM 2562 CG LEU A 291 -15.348 12.786 -18.523 1.00 38.17 C ANISOU 2562 CG LEU A 291 4524 5297 4681 -474 -60 402 C ATOM 2563 CD1 LEU A 291 -16.497 11.849 -18.846 1.00 43.04 C ANISOU 2563 CD1 LEU A 291 5147 6005 5202 -410 -62 410 C ATOM 2564 CD2 LEU A 291 -15.615 14.137 -19.205 1.00 32.36 C ANISOU 2564 CD2 LEU A 291 3836 4468 3991 -485 -42 496 C ATOM 2565 N ALA A 292 -12.489 11.352 -16.406 1.00 38.88 N ANISOU 2565 N ALA A 292 4471 5442 4861 -554 -134 202 N ATOM 2566 CA ALA A 292 -11.347 10.506 -16.750 1.00 37.76 C ANISOU 2566 CA ALA A 292 4238 5370 4739 -582 -112 195 C ATOM 2567 C ALA A 292 -11.517 9.086 -16.198 1.00 36.43 C ANISOU 2567 C ALA A 292 4059 5271 4511 -516 -136 151 C ATOM 2568 O ALA A 292 -11.342 8.104 -16.933 1.00 38.32 O ANISOU 2568 O ALA A 292 4265 5574 4721 -499 -86 165 O ATOM 2569 CB ALA A 292 -10.043 11.127 -16.245 1.00 37.87 C ANISOU 2569 CB ALA A 292 4181 5347 4860 -656 -148 160 C ATOM 2570 N LEU A 293 -11.863 8.952 -14.913 1.00 32.59 N ANISOU 2570 N LEU A 293 3612 4769 4003 -477 -207 98 N ATOM 2571 CA LEU A 293 -12.025 7.605 -14.336 1.00 40.18 C ANISOU 2571 CA LEU A 293 4574 5784 4909 -416 -228 73 C ATOM 2572 C LEU A 293 -13.093 6.779 -15.075 1.00 41.23 C ANISOU 2572 C LEU A 293 4744 5951 4972 -378 -168 104 C ATOM 2573 O LEU A 293 -12.893 5.579 -15.394 1.00 44.99 O ANISOU 2573 O LEU A 293 5195 6469 5431 -354 -142 102 O ATOM 2574 CB LEU A 293 -12.360 7.711 -12.843 1.00 39.73 C ANISOU 2574 CB LEU A 293 4574 5708 4816 -384 -304 24 C ATOM 2575 CG LEU A 293 -11.225 8.203 -11.951 1.00 42.46 C ANISOU 2575 CG LEU A 293 4880 6040 5212 -420 -389 -25 C ATOM 2576 CD1 LEU A 293 -11.686 8.460 -10.518 1.00 39.26 C ANISOU 2576 CD1 LEU A 293 4557 5621 4741 -392 -460 -81 C ATOM 2577 CD2 LEU A 293 -10.137 7.145 -11.971 1.00 43.45 C ANISOU 2577 CD2 LEU A 293 4914 6225 5370 -404 -412 -19 C ATOM 2578 N ALA A 294 -14.243 7.404 -15.355 1.00 35.63 N ANISOU 2578 N ALA A 294 4090 5220 4228 -371 -151 129 N ATOM 2579 CA ALA A 294 -15.278 6.715 -16.120 1.00 37.71 C ANISOU 2579 CA ALA A 294 4373 5525 4429 -348 -109 155 C ATOM 2580 C ALA A 294 -14.744 6.255 -17.473 1.00 39.13 C ANISOU 2580 C ALA A 294 4516 5751 4602 -378 -53 180 C ATOM 2581 O ALA A 294 -14.983 5.115 -17.889 1.00 46.94 O ANISOU 2581 O ALA A 294 5504 6782 5550 -364 -26 165 O ATOM 2582 CB ALA A 294 -16.508 7.610 -16.299 1.00 31.17 C ANISOU 2582 CB ALA A 294 3587 4674 3581 -333 -107 186 C ATOM 2583 N ALA A 295 -13.997 7.113 -18.163 1.00 34.20 N ANISOU 2583 N ALA A 295 3865 5114 4016 -424 -28 214 N ATOM 2584 CA ALA A 295 -13.431 6.682 -19.439 1.00 39.88 C ANISOU 2584 CA ALA A 295 4552 5887 4714 -452 42 234 C ATOM 2585 C ALA A 295 -12.476 5.500 -19.249 1.00 42.85 C ANISOU 2585 C ALA A 295 4871 6292 5119 -436 61 182 C ATOM 2586 O ALA A 295 -12.480 4.556 -20.052 1.00 41.21 O ANISOU 2586 O ALA A 295 4661 6130 4866 -426 116 166 O ATOM 2587 CB ALA A 295 -12.716 7.844 -20.131 1.00 35.05 C ANISOU 2587 CB ALA A 295 3919 5253 4143 -512 79 290 C ATOM 2588 N ALA A 296 -11.679 5.521 -18.174 1.00 38.08 N ANISOU 2588 N ALA A 296 4222 5659 4586 -426 11 152 N ATOM 2589 CA ALA A 296 -10.627 4.524 -17.958 1.00 37.16 C ANISOU 2589 CA ALA A 296 4034 5566 4520 -399 19 116 C ATOM 2590 C ALA A 296 -11.179 3.122 -17.720 1.00 40.04 C ANISOU 2590 C ALA A 296 4436 5937 4841 -338 19 87 C ATOM 2591 O ALA A 296 -10.406 2.144 -17.729 1.00 37.42 O ANISOU 2591 O ALA A 296 4054 5613 4549 -300 40 62 O ATOM 2592 CB ALA A 296 -9.757 4.946 -16.772 1.00 31.77 C ANISOU 2592 CB ALA A 296 3297 4859 3916 -402 -63 97 C ATOM 2593 N ASN A 297 -12.491 3.016 -17.485 1.00 37.66 N ANISOU 2593 N ASN A 297 4215 5623 4470 -327 0 93 N ATOM 2594 CA ASN A 297 -13.101 1.704 -17.281 1.00 43.15 C ANISOU 2594 CA ASN A 297 4950 6313 5132 -287 7 70 C ATOM 2595 C ASN A 297 -12.804 0.833 -18.488 1.00 45.03 C ANISOU 2595 C ASN A 297 5172 6576 5360 -289 86 43 C ATOM 2596 O ASN A 297 -12.708 -0.375 -18.381 1.00 36.96 O ANISOU 2596 O ASN A 297 4159 5533 4352 -253 104 12 O ATOM 2597 CB ASN A 297 -14.635 1.804 -17.093 1.00 45.86 C ANISOU 2597 CB ASN A 297 5363 6653 5408 -292 -8 82 C ATOM 2598 CG ASN A 297 -15.369 0.464 -17.287 1.00 47.55 C ANISOU 2598 CG ASN A 297 5613 6864 5591 -282 20 57 C ATOM 2599 OD1 ASN A 297 -16.088 0.279 -18.253 1.00 49.29 O ANISOU 2599 OD1 ASN A 297 5850 7114 5765 -311 51 48 O ATOM 2600 ND2 ASN A 297 -15.173 -0.448 -16.357 1.00 46.08 N ANISOU 2600 ND2 ASN A 297 5440 6638 5428 -243 3 50 N ATOM 2601 N ALA A 298 -12.721 1.450 -19.672 1.00 39.35 N ANISOU 2601 N ALA A 298 4444 5899 4609 -333 138 56 N ATOM 2602 CA ALA A 298 -12.566 0.673 -20.890 1.00 43.72 C ANISOU 2602 CA ALA A 298 5002 6488 5122 -341 220 19 C ATOM 2603 C ALA A 298 -11.227 -0.055 -20.947 1.00 47.10 C ANISOU 2603 C ALA A 298 5359 6909 5627 -303 273 -19 C ATOM 2604 O ALA A 298 -11.121 -1.066 -21.650 1.00 46.27 O ANISOU 2604 O ALA A 298 5267 6808 5504 -285 341 -74 O ATOM 2605 CB ALA A 298 -12.745 1.578 -22.117 1.00 43.81 C ANISOU 2605 CB ALA A 298 5028 6557 5062 -395 263 55 C ATOM 2606 N CYS A 299 -10.203 0.422 -20.232 1.00 44.41 N ANISOU 2606 N CYS A 299 4939 6557 5378 -289 243 1 N ATOM 2607 CA CYS A 299 -8.978 -0.358 -20.126 1.00 45.36 C ANISOU 2607 CA CYS A 299 4973 6672 5591 -235 277 -32 C ATOM 2608 C CYS A 299 -8.892 -1.112 -18.814 1.00 46.07 C ANISOU 2608 C CYS A 299 5062 6708 5737 -165 193 -33 C ATOM 2609 O CYS A 299 -7.991 -1.936 -18.658 1.00 50.62 O ANISOU 2609 O CYS A 299 5572 7267 6394 -99 210 -54 O ATOM 2610 CB CYS A 299 -7.718 0.513 -20.266 1.00 46.35 C ANISOU 2610 CB CYS A 299 4981 6833 5798 -264 299 -10 C ATOM 2611 SG CYS A 299 -7.365 1.651 -18.902 1.00 47.01 S ANISOU 2611 SG CYS A 299 5017 6895 5950 -291 169 30 S ATOM 2612 N PHE A 300 -9.785 -0.841 -17.862 1.00 46.16 N ANISOU 2612 N PHE A 300 5142 6692 5705 -171 108 -5 N ATOM 2613 CA PHE A 300 -9.758 -1.638 -16.636 1.00 45.65 C ANISOU 2613 CA PHE A 300 5096 6581 5670 -105 37 6 C ATOM 2614 C PHE A 300 -10.409 -3.013 -16.826 1.00 47.88 C ANISOU 2614 C PHE A 300 5450 6810 5932 -69 80 -17 C ATOM 2615 O PHE A 300 -9.950 -3.994 -16.230 1.00 49.24 O ANISOU 2615 O PHE A 300 5615 6933 6161 3 62 -11 O ATOM 2616 CB PHE A 300 -10.435 -0.879 -15.483 1.00 52.00 C ANISOU 2616 CB PHE A 300 5953 7380 6426 -125 -56 39 C ATOM 2617 CG PHE A 300 -9.658 0.333 -14.979 1.00 57.55 C ANISOU 2617 CG PHE A 300 6589 8109 7167 -154 -121 49 C ATOM 2618 CD1 PHE A 300 -8.308 0.504 -15.276 1.00 60.14 C ANISOU 2618 CD1 PHE A 300 6799 8465 7588 -153 -115 40 C ATOM 2619 CD2 PHE A 300 -10.297 1.309 -14.218 1.00 55.48 C ANISOU 2619 CD2 PHE A 300 6383 7843 6856 -187 -183 59 C ATOM 2620 CE1 PHE A 300 -7.610 1.618 -14.808 1.00 58.26 C ANISOU 2620 CE1 PHE A 300 6495 8246 7396 -198 -180 42 C ATOM 2621 CE2 PHE A 300 -9.600 2.431 -13.750 1.00 53.77 C ANISOU 2621 CE2 PHE A 300 6116 7636 6679 -225 -245 52 C ATOM 2622 CZ PHE A 300 -8.267 2.585 -14.046 1.00 53.45 C ANISOU 2622 CZ PHE A 300 5956 7620 6733 -237 -248 45 C ATOM 2623 N ASN A 301 -11.450 -3.121 -17.658 1.00 48.22 N ANISOU 2623 N ASN A 301 5560 6858 5902 -119 132 -42 N ATOM 2624 CA ASN A 301 -12.230 -4.368 -17.683 1.00 44.08 C ANISOU 2624 CA ASN A 301 5112 6274 5362 -106 159 -67 C ATOM 2625 C ASN A 301 -11.478 -5.673 -17.999 1.00 47.70 C ANISOU 2625 C ASN A 301 5558 6670 5895 -41 217 -111 C ATOM 2626 O ASN A 301 -11.973 -6.737 -17.573 1.00 46.56 O ANISOU 2626 O ASN A 301 5479 6443 5768 -17 217 -112 O ATOM 2627 CB ASN A 301 -13.414 -4.236 -18.653 1.00 44.60 C ANISOU 2627 CB ASN A 301 5233 6371 5341 -180 196 -98 C ATOM 2628 CG ASN A 301 -14.476 -3.293 -18.135 1.00 46.48 C ANISOU 2628 CG ASN A 301 5499 6641 5521 -223 138 -52 C ATOM 2629 OD1 ASN A 301 -14.733 -3.247 -16.926 1.00 47.97 O ANISOU 2629 OD1 ASN A 301 5705 6801 5719 -200 85 -12 O ATOM 2630 ND2 ASN A 301 -15.146 -2.581 -19.044 1.00 38.94 N ANISOU 2630 ND2 ASN A 301 4551 5745 4498 -278 150 -56 N ATOM 2631 N PRO A 302 -10.354 -5.713 -18.725 1.00 48.28 N ANISOU 2631 N PRO A 302 5554 6767 6023 -9 277 -147 N ATOM 2632 CA PRO A 302 -9.722 -7.027 -18.969 1.00 44.85 C ANISOU 2632 CA PRO A 302 5114 6257 5671 70 340 -196 C ATOM 2633 C PRO A 302 -9.170 -7.712 -17.717 1.00 45.14 C ANISOU 2633 C PRO A 302 5132 6218 5802 167 272 -140 C ATOM 2634 O PRO A 302 -8.912 -8.932 -17.754 1.00 44.61 O ANISOU 2634 O PRO A 302 5087 6054 5807 239 314 -167 O ATOM 2635 CB PRO A 302 -8.622 -6.709 -19.984 1.00 40.48 C ANISOU 2635 CB PRO A 302 4463 5766 5150 82 427 -242 C ATOM 2636 CG PRO A 302 -9.107 -5.471 -20.675 1.00 39.94 C ANISOU 2636 CG PRO A 302 4404 5796 4977 -19 436 -232 C ATOM 2637 CD PRO A 302 -9.786 -4.674 -19.610 1.00 41.55 C ANISOU 2637 CD PRO A 302 4633 6005 5150 -52 321 -157 C ATOM 2638 N LEU A 303 -8.989 -6.981 -16.612 1.00 43.77 N ANISOU 2638 N LEU A 303 4925 6079 5626 174 167 -65 N ATOM 2639 CA LEU A 303 -8.756 -7.636 -15.323 1.00 49.88 C ANISOU 2639 CA LEU A 303 5717 6789 6447 255 84 3 C ATOM 2640 C LEU A 303 -9.793 -8.707 -15.052 1.00 48.85 C ANISOU 2640 C LEU A 303 5715 6555 6292 254 105 14 C ATOM 2641 O LEU A 303 -9.474 -9.789 -14.543 1.00 45.45 O ANISOU 2641 O LEU A 303 5309 6026 5932 340 97 48 O ATOM 2642 CB LEU A 303 -8.770 -6.610 -14.192 1.00 52.15 C ANISOU 2642 CB LEU A 303 5991 7140 6685 234 -34 68 C ATOM 2643 CG LEU A 303 -7.536 -5.725 -14.242 1.00 50.70 C ANISOU 2643 CG LEU A 303 5666 7037 6560 242 -72 63 C ATOM 2644 CD1 LEU A 303 -7.645 -4.571 -13.273 1.00 51.23 C ANISOU 2644 CD1 LEU A 303 5733 7164 6569 196 -183 99 C ATOM 2645 CD2 LEU A 303 -6.374 -6.625 -13.887 1.00 46.57 C ANISOU 2645 CD2 LEU A 303 5060 6479 6157 363 -99 85 C ATOM 2646 N LEU A 304 -11.043 -8.420 -15.390 1.00 49.64 N ANISOU 2646 N LEU A 304 5891 6671 6301 156 131 -8 N ATOM 2647 CA LEU A 304 -12.110 -9.375 -15.142 1.00 45.77 C ANISOU 2647 CA LEU A 304 5510 6087 5792 131 154 1 C ATOM 2648 C LEU A 304 -11.962 -10.596 -16.044 1.00 46.22 C ANISOU 2648 C LEU A 304 5597 6044 5920 155 245 -75 C ATOM 2649 O LEU A 304 -12.214 -11.731 -15.618 1.00 48.80 O ANISOU 2649 O LEU A 304 5997 6246 6300 186 260 -53 O ATOM 2650 CB LEU A 304 -13.442 -8.669 -15.352 1.00 46.25 C ANISOU 2650 CB LEU A 304 5614 6208 5751 20 155 -10 C ATOM 2651 CG LEU A 304 -14.765 -9.325 -14.990 1.00 54.95 C ANISOU 2651 CG LEU A 304 6807 7248 6822 -38 172 8 C ATOM 2652 CD1 LEU A 304 -14.827 -9.586 -13.478 1.00 51.92 C ANISOU 2652 CD1 LEU A 304 6470 6822 6436 8 118 112 C ATOM 2653 CD2 LEU A 304 -15.921 -8.414 -15.430 1.00 53.38 C ANISOU 2653 CD2 LEU A 304 6606 7140 6536 -136 171 -15 C ATOM 2654 N TYR A 305 -11.517 -10.393 -17.283 1.00 40.61 N ANISOU 2654 N TYR A 305 4837 5381 5212 141 314 -165 N ATOM 2655 CA TYR A 305 -11.350 -11.531 -18.179 1.00 40.79 C ANISOU 2655 CA TYR A 305 4895 5309 5292 165 409 -260 C ATOM 2656 C TYR A 305 -10.265 -12.442 -17.627 1.00 47.73 C ANISOU 2656 C TYR A 305 5746 6083 6308 303 413 -230 C ATOM 2657 O TYR A 305 -10.352 -13.674 -17.731 1.00 44.81 O ANISOU 2657 O TYR A 305 5445 5569 6012 343 465 -264 O ATOM 2658 CB TYR A 305 -10.950 -11.050 -19.576 1.00 37.61 C ANISOU 2658 CB TYR A 305 4445 4999 4848 133 488 -359 C ATOM 2659 CG TYR A 305 -11.897 -10.040 -20.182 1.00 39.17 C ANISOU 2659 CG TYR A 305 4660 5312 4909 13 473 -372 C ATOM 2660 CD1 TYR A 305 -13.218 -9.906 -19.741 1.00 41.15 C ANISOU 2660 CD1 TYR A 305 4976 5561 5097 -67 417 -337 C ATOM 2661 CD2 TYR A 305 -11.400 -9.083 -21.053 1.00 37.92 C ANISOU 2661 CD2 TYR A 305 4439 5274 4697 -12 507 -396 C ATOM 2662 CE1 TYR A 305 -14.036 -8.905 -20.250 1.00 44.46 C ANISOU 2662 CE1 TYR A 305 5395 6091 5406 -158 392 -337 C ATOM 2663 CE2 TYR A 305 -12.188 -8.086 -21.560 1.00 41.39 C ANISOU 2663 CE2 TYR A 305 4892 5815 5019 -106 484 -386 C ATOM 2664 CZ TYR A 305 -13.509 -7.997 -21.168 1.00 43.58 C ANISOU 2664 CZ TYR A 305 5232 6088 5240 -173 421 -357 C ATOM 2665 OH TYR A 305 -14.285 -6.991 -21.692 1.00 38.16 O ANISOU 2665 OH TYR A 305 4549 5502 4448 -250 392 -341 O ATOM 2666 N TYR A 306 -9.226 -11.842 -17.030 1.00 49.01 N ANISOU 2666 N TYR A 306 5801 6310 6512 379 353 -164 N ATOM 2667 CA TYR A 306 -8.092 -12.652 -16.589 1.00 50.15 C ANISOU 2667 CA TYR A 306 5890 6371 6795 525 347 -132 C ATOM 2668 C TYR A 306 -8.400 -13.378 -15.287 1.00 49.21 C ANISOU 2668 C TYR A 306 5851 6143 6704 579 267 -19 C ATOM 2669 O TYR A 306 -8.107 -14.571 -15.147 1.00 49.89 O ANISOU 2669 O TYR A 306 5977 6083 6897 674 298 -9 O ATOM 2670 CB TYR A 306 -6.826 -11.818 -16.408 1.00 47.84 C ANISOU 2670 CB TYR A 306 5435 6191 6550 585 301 -103 C ATOM 2671 CG TYR A 306 -5.672 -12.723 -16.010 1.00 50.40 C ANISOU 2671 CG TYR A 306 5686 6434 7032 748 292 -71 C ATOM 2672 CD1 TYR A 306 -5.036 -13.515 -16.959 1.00 53.45 C ANISOU 2672 CD1 TYR A 306 6032 6753 7522 826 416 -165 C ATOM 2673 CD2 TYR A 306 -5.270 -12.840 -14.687 1.00 48.95 C ANISOU 2673 CD2 TYR A 306 5479 6234 6886 832 160 51 C ATOM 2674 CE1 TYR A 306 -4.009 -14.364 -16.614 1.00 53.94 C ANISOU 2674 CE1 TYR A 306 6020 6731 7744 991 412 -135 C ATOM 2675 CE2 TYR A 306 -4.244 -13.691 -14.326 1.00 50.79 C ANISOU 2675 CE2 TYR A 306 5640 6390 7267 993 139 92 C ATOM 2676 CZ TYR A 306 -3.613 -14.452 -15.299 1.00 56.91 C ANISOU 2676 CZ TYR A 306 6364 7094 8166 1077 268 0 C ATOM 2677 OH TYR A 306 -2.585 -15.305 -14.957 1.00 59.37 O ANISOU 2677 OH TYR A 306 6592 7322 8643 1256 252 42 O ATOM 2678 N PHE A 307 -8.970 -12.677 -14.314 1.00 43.29 N ANISOU 2678 N PHE A 307 5131 5458 5860 526 170 69 N ATOM 2679 CA PHE A 307 -9.159 -13.301 -13.016 1.00 47.11 C ANISOU 2679 CA PHE A 307 5691 5858 6352 582 96 191 C ATOM 2680 C PHE A 307 -10.481 -14.049 -12.886 1.00 49.31 C ANISOU 2680 C PHE A 307 6118 6026 6591 505 144 203 C ATOM 2681 O PHE A 307 -10.608 -14.885 -11.989 1.00 51.30 O ANISOU 2681 O PHE A 307 6450 6167 6873 558 118 303 O ATOM 2682 CB PHE A 307 -9.015 -12.260 -11.897 1.00 51.64 C ANISOU 2682 CB PHE A 307 6229 6553 6837 576 -32 280 C ATOM 2683 CG PHE A 307 -7.613 -11.707 -11.768 1.00 53.94 C ANISOU 2683 CG PHE A 307 6368 6933 7192 660 -104 287 C ATOM 2684 CD1 PHE A 307 -6.617 -12.448 -11.153 1.00 56.24 C ANISOU 2684 CD1 PHE A 307 6614 7169 7587 804 -166 360 C ATOM 2685 CD2 PHE A 307 -7.298 -10.446 -12.248 1.00 53.74 C ANISOU 2685 CD2 PHE A 307 6242 7043 7132 593 -113 229 C ATOM 2686 CE1 PHE A 307 -5.320 -11.952 -11.035 1.00 56.99 C ANISOU 2686 CE1 PHE A 307 6544 7355 7753 877 -240 364 C ATOM 2687 CE2 PHE A 307 -6.005 -9.938 -12.134 1.00 54.46 C ANISOU 2687 CE2 PHE A 307 6180 7216 7297 653 -176 233 C ATOM 2688 CZ PHE A 307 -5.013 -10.694 -11.527 1.00 56.57 C ANISOU 2688 CZ PHE A 307 6383 7439 7670 794 -242 297 C ATOM 2689 N ALA A 308 -11.453 -13.819 -13.773 1.00 49.88 N ANISOU 2689 N ALA A 308 6225 6123 6604 380 214 110 N ATOM 2690 CA ALA A 308 -12.713 -14.544 -13.646 1.00 54.28 C ANISOU 2690 CA ALA A 308 6903 6579 7140 295 257 119 C ATOM 2691 C ALA A 308 -13.238 -15.061 -14.985 1.00 55.01 C ANISOU 2691 C ALA A 308 7027 6619 7256 216 357 -22 C ATOM 2692 O ALA A 308 -14.444 -15.315 -15.112 1.00 52.36 O ANISOU 2692 O ALA A 308 6762 6252 6882 102 385 -44 O ATOM 2693 CB ALA A 308 -13.781 -13.664 -12.973 1.00 54.37 C ANISOU 2693 CB ALA A 308 6940 6693 7025 195 212 175 C ATOM 2694 N GLY A 309 -12.375 -15.234 -15.977 1.00 54.02 N ANISOU 2694 N GLY A 309 6848 6488 7189 271 411 -123 N ATOM 2695 CA GLY A 309 -12.817 -15.698 -17.273 1.00 52.46 C ANISOU 2695 CA GLY A 309 6690 6253 6989 197 502 -271 C ATOM 2696 C GLY A 309 -13.250 -17.149 -17.257 1.00 54.91 C ANISOU 2696 C GLY A 309 7114 6355 7395 191 559 -300 C ATOM 2697 O GLY A 309 -13.139 -17.861 -16.260 1.00 57.97 O ANISOU 2697 O GLY A 309 7552 6613 7861 257 537 -192 O ATOM 2698 N GLU A 310 -13.764 -17.595 -18.402 1.00 55.13 N ANISOU 2698 N GLU A 310 7189 6346 7410 105 632 -449 N ATOM 2699 CA GLU A 310 -14.291 -18.948 -18.563 1.00 57.53 C ANISOU 2699 CA GLU A 310 7609 6444 7805 67 693 -510 C ATOM 2700 C GLU A 310 -13.470 -19.613 -19.663 1.00 63.24 C ANISOU 2700 C GLU A 310 8342 7089 8599 137 789 -667 C ATOM 2701 O GLU A 310 -13.727 -19.393 -20.851 1.00 65.77 O ANISOU 2701 O GLU A 310 8664 7489 8836 57 833 -817 O ATOM 2702 CB GLU A 310 -15.770 -18.911 -18.918 1.00 55.72 C ANISOU 2702 CB GLU A 310 7432 6244 7496 -118 687 -566 C ATOM 2703 CG GLU A 310 -16.467 -20.260 -18.991 1.00 65.07 C ANISOU 2703 CG GLU A 310 8733 7212 8778 -193 741 -624 C ATOM 2704 CD GLU A 310 -16.594 -20.928 -17.632 1.00 75.00 C ANISOU 2704 CD GLU A 310 10052 8313 10133 -152 727 -457 C ATOM 2705 OE1 GLU A 310 -16.624 -20.200 -16.616 1.00 74.03 O ANISOU 2705 OE1 GLU A 310 9884 8290 9952 -123 661 -303 O ATOM 2706 OE2 GLU A 310 -16.667 -22.181 -17.583 1.00 82.33 O ANISOU 2706 OE2 GLU A 310 11081 9012 11190 -151 786 -481 O ATOM 2707 N ASN A 311 -12.472 -20.405 -19.269 1.00 59.74 N ANISOU 2707 N ASN A 311 7903 6495 8301 294 823 -632 N ATOM 2708 CA ASN A 311 -11.522 -21.015 -20.198 1.00 66.03 C ANISOU 2708 CA ASN A 311 8691 7214 9184 397 926 -774 C ATOM 2709 C ASN A 311 -10.677 -19.965 -20.905 1.00 60.87 C ANISOU 2709 C ASN A 311 7906 6770 8450 438 944 -824 C ATOM 2710 O ASN A 311 -10.168 -20.200 -22.007 1.00 57.52 O ANISOU 2710 O ASN A 311 7476 6349 8030 467 1048 -979 O ATOM 2711 CB ASN A 311 -12.233 -21.894 -21.232 1.00 76.18 C ANISOU 2711 CB ASN A 311 10096 8377 10472 290 1014 -964 C ATOM 2712 CG ASN A 311 -13.006 -23.019 -20.596 1.00 82.75 C ANISOU 2712 CG ASN A 311 11057 8973 11411 241 1013 -923 C ATOM 2713 OD1 ASN A 311 -14.235 -23.075 -20.689 1.00 85.77 O ANISOU 2713 OD1 ASN A 311 11503 9355 11729 68 990 -952 O ATOM 2714 ND2 ASN A 311 -12.297 -23.908 -19.912 1.00 83.01 N ANISOU 2714 ND2 ASN A 311 11122 8805 11614 392 1036 -843 N ATOM 2715 N PHE A 312 -10.551 -18.793 -20.286 1.00 59.16 N ANISOU 2715 N PHE A 312 7593 6728 8156 433 851 -697 N ATOM 2716 CA PHE A 312 -9.735 -17.728 -20.848 1.00 55.23 C ANISOU 2716 CA PHE A 312 6967 6422 7596 462 864 -721 C ATOM 2717 C PHE A 312 -8.270 -18.127 -20.830 1.00 56.88 C ANISOU 2717 C PHE A 312 7081 6581 7951 643 919 -724 C ATOM 2718 O PHE A 312 -7.606 -18.136 -21.871 1.00 60.27 O ANISOU 2718 O PHE A 312 7463 7053 8385 679 1028 -849 O ATOM 2719 CB PHE A 312 -9.958 -16.441 -20.051 1.00 53.54 C ANISOU 2719 CB PHE A 312 6682 6372 7289 414 746 -581 C ATOM 2720 CG PHE A 312 -9.279 -15.239 -20.630 1.00 49.28 C ANISOU 2720 CG PHE A 312 6021 6024 6679 409 755 -597 C ATOM 2721 CD1 PHE A 312 -9.834 -14.573 -21.718 1.00 49.67 C ANISOU 2721 CD1 PHE A 312 6087 6196 6588 290 795 -685 C ATOM 2722 CD2 PHE A 312 -8.083 -14.788 -20.114 1.00 45.36 C ANISOU 2722 CD2 PHE A 312 5392 5583 6259 520 724 -522 C ATOM 2723 CE1 PHE A 312 -9.216 -13.447 -22.262 1.00 50.04 C ANISOU 2723 CE1 PHE A 312 6033 6410 6572 279 813 -684 C ATOM 2724 CE2 PHE A 312 -7.451 -13.674 -20.662 1.00 48.93 C ANISOU 2724 CE2 PHE A 312 5730 6203 6660 500 743 -535 C ATOM 2725 CZ PHE A 312 -8.018 -13.001 -21.727 1.00 48.94 C ANISOU 2725 CZ PHE A 312 5760 6314 6521 379 793 -610 C ATOM 2726 N LYS A 313 -7.764 -18.497 -19.649 1.00 61.79 N ANISOU 2726 N LYS A 313 7673 7114 8691 764 846 -586 N ATOM 2727 CA LYS A 313 -6.399 -18.999 -19.532 1.00 60.97 C ANISOU 2727 CA LYS A 313 7468 6946 8751 954 883 -576 C ATOM 2728 C LYS A 313 -6.179 -20.257 -20.362 1.00 60.14 C ANISOU 2728 C LYS A 313 7435 6655 8758 1026 1026 -724 C ATOM 2729 O LYS A 313 -5.075 -20.469 -20.874 1.00 63.06 O ANISOU 2729 O LYS A 313 7705 7024 9230 1157 1115 -792 O ATOM 2730 CB LYS A 313 -6.062 -19.279 -18.070 1.00 61.21 C ANISOU 2730 CB LYS A 313 7480 6903 8875 1066 759 -389 C ATOM 2731 CG LYS A 313 -5.984 -18.048 -17.180 1.00 62.54 C ANISOU 2731 CG LYS A 313 7558 7254 8949 1028 618 -255 C ATOM 2732 CD LYS A 313 -5.559 -18.465 -15.781 1.00 71.18 C ANISOU 2732 CD LYS A 313 8645 8273 10127 1154 497 -81 C ATOM 2733 CE LYS A 313 -5.446 -17.297 -14.828 1.00 74.92 C ANISOU 2733 CE LYS A 313 9041 8922 10502 1120 350 40 C ATOM 2734 NZ LYS A 313 -4.986 -17.790 -13.498 1.00 79.61 N ANISOU 2734 NZ LYS A 313 9637 9447 11163 1251 227 206 N ATOM 2735 N ASP A 314 -7.197 -21.112 -20.493 1.00 57.35 N ANISOU 2735 N ASP A 314 7251 6139 8400 943 1054 -781 N ATOM 2736 CA ASP A 314 -7.062 -22.287 -21.353 1.00 62.36 C ANISOU 2736 CA ASP A 314 7974 6587 9135 992 1194 -949 C ATOM 2737 C ASP A 314 -6.811 -21.874 -22.796 1.00 60.28 C ANISOU 2737 C ASP A 314 7675 6458 8772 944 1316 -1142 C ATOM 2738 O ASP A 314 -5.882 -22.371 -23.450 1.00 59.42 O ANISOU 2738 O ASP A 314 7523 6295 8760 1071 1441 -1256 O ATOM 2739 CB ASP A 314 -8.316 -23.158 -21.263 1.00 66.95 C ANISOU 2739 CB ASP A 314 8741 6982 9713 870 1193 -983 C ATOM 2740 CG ASP A 314 -8.461 -23.840 -19.918 1.00 76.74 C ANISOU 2740 CG ASP A 314 10040 8042 11076 938 1112 -799 C ATOM 2741 OD1 ASP A 314 -7.428 -24.146 -19.287 1.00 83.16 O ANISOU 2741 OD1 ASP A 314 10781 8788 12028 1128 1093 -697 O ATOM 2742 OD2 ASP A 314 -9.610 -24.055 -19.478 1.00 79.54 O ANISOU 2742 OD2 ASP A 314 10507 8330 11384 801 1066 -749 O ATOM 2743 N ARG A 315 -7.637 -20.959 -23.309 1.00 57.65 N ANISOU 2743 N ARG A 315 7360 6303 8240 767 1284 -1176 N ATOM 2744 CA ARG A 315 -7.412 -20.442 -24.651 1.00 60.79 C ANISOU 2744 CA ARG A 315 7730 6855 8512 715 1388 -1332 C ATOM 2745 C ARG A 315 -6.058 -19.765 -24.771 1.00 57.33 C ANISOU 2745 C ARG A 315 7111 6555 8116 839 1436 -1297 C ATOM 2746 O ARG A 315 -5.389 -19.910 -25.796 1.00 55.71 O ANISOU 2746 O ARG A 315 6876 6385 7908 888 1582 -1439 O ATOM 2747 CB ARG A 315 -8.542 -19.488 -25.054 1.00 63.62 C ANISOU 2747 CB ARG A 315 8132 7389 8654 515 1320 -1335 C ATOM 2748 CG ARG A 315 -9.847 -20.194 -25.386 1.00 66.69 C ANISOU 2748 CG ARG A 315 8685 7669 8985 372 1308 -1436 C ATOM 2749 CD ARG A 315 -10.961 -19.229 -25.761 1.00 63.10 C ANISOU 2749 CD ARG A 315 8249 7398 8328 189 1227 -1427 C ATOM 2750 NE ARG A 315 -12.148 -19.945 -26.217 1.00 62.69 N ANISOU 2750 NE ARG A 315 8335 7256 8227 49 1220 -1547 N ATOM 2751 CZ ARG A 315 -13.120 -20.382 -25.424 1.00 66.61 C ANISOU 2751 CZ ARG A 315 8892 7639 8777 -29 1140 -1478 C ATOM 2752 NH1 ARG A 315 -13.051 -20.203 -24.107 1.00 67.02 N ANISOU 2752 NH1 ARG A 315 8896 7651 8918 29 1064 -1287 N ATOM 2753 NH2 ARG A 315 -14.156 -21.020 -25.951 1.00 68.87 N ANISOU 2753 NH2 ARG A 315 9288 7853 9025 -169 1138 -1605 N ATOM 2754 N LEU A 316 -5.634 -19.039 -23.737 1.00 59.78 N ANISOU 2754 N LEU A 316 7299 6947 8469 886 1321 -1116 N ATOM 2755 CA LEU A 316 -4.343 -18.361 -23.784 1.00 56.94 C ANISOU 2755 CA LEU A 316 6747 6721 8165 988 1352 -1076 C ATOM 2756 C LEU A 316 -3.191 -19.358 -23.870 1.00 62.49 C ANISOU 2756 C LEU A 316 7380 7291 9074 1191 1459 -1133 C ATOM 2757 O LEU A 316 -2.282 -19.191 -24.688 1.00 65.57 O ANISOU 2757 O LEU A 316 7662 7764 9487 1253 1592 -1224 O ATOM 2758 CB LEU A 316 -4.202 -17.444 -22.571 1.00 56.71 C ANISOU 2758 CB LEU A 316 6615 6791 8141 986 1186 -881 C ATOM 2759 CG LEU A 316 -2.910 -16.648 -22.478 1.00 61.75 C ANISOU 2759 CG LEU A 316 7040 7575 8847 1068 1189 -826 C ATOM 2760 CD1 LEU A 316 -2.748 -15.768 -23.689 1.00 62.36 C ANISOU 2760 CD1 LEU A 316 7069 7828 8797 972 1301 -919 C ATOM 2761 CD2 LEU A 316 -2.963 -15.791 -21.218 1.00 65.83 C ANISOU 2761 CD2 LEU A 316 7492 8173 9350 1041 1004 -649 C ATOM 2762 N LYS A 317 -3.214 -20.404 -23.045 1.00 64.67 N ANISOU 2762 N LYS A 317 7715 7354 9502 1299 1412 -1075 N ATOM 2763 CA LYS A 317 -2.182 -21.428 -23.130 1.00 69.92 C ANISOU 2763 CA LYS A 317 8324 7865 10379 1507 1514 -1127 C ATOM 2764 C LYS A 317 -2.201 -22.101 -24.494 1.00 72.19 C ANISOU 2764 C LYS A 317 8700 8080 10647 1503 1713 -1363 C ATOM 2765 O LYS A 317 -1.146 -22.457 -25.040 1.00 73.54 O ANISOU 2765 O LYS A 317 8769 8236 10937 1652 1853 -1456 O ATOM 2766 CB LYS A 317 -2.371 -22.450 -22.009 1.00 72.90 C ANISOU 2766 CB LYS A 317 8785 8008 10908 1610 1421 -1009 C ATOM 2767 N SER A 318 -3.394 -22.265 -25.073 1.00 75.59 N ANISOU 2767 N SER A 318 9315 8478 10926 1332 1729 -1470 N ATOM 2768 CA SER A 318 -3.483 -22.823 -26.421 1.00 79.25 C ANISOU 2768 CA SER A 318 9880 8899 11333 1304 1907 -1711 C ATOM 2769 C SER A 318 -2.804 -21.910 -27.430 1.00 69.96 C ANISOU 2769 C SER A 318 8583 7964 10036 1286 2021 -1791 C ATOM 2770 O SER A 318 -2.050 -22.365 -28.296 1.00 73.23 O ANISOU 2770 O SER A 318 8970 8356 10497 1386 2202 -1949 O ATOM 2771 CB SER A 318 -4.945 -23.046 -26.809 1.00 88.78 C ANISOU 2771 CB SER A 318 11292 10058 12383 1101 1869 -1800 C ATOM 2772 OG SER A 318 -5.554 -24.005 -25.966 1.00 98.17 O ANISOU 2772 OG SER A 318 12599 11003 13697 1111 1795 -1741 O ATOM 2773 N ALA A 319 -3.072 -20.609 -27.331 1.00 65.50 N ANISOU 2773 N ALA A 319 7949 7623 9314 1160 1927 -1682 N ATOM 2774 CA ALA A 319 -2.413 -19.635 -28.195 1.00 72.34 C ANISOU 2774 CA ALA A 319 8696 8721 10069 1133 2029 -1720 C ATOM 2775 C ALA A 319 -0.896 -19.682 -28.034 1.00 79.30 C ANISOU 2775 C ALA A 319 9365 9621 11144 1326 2120 -1692 C ATOM 2776 O ALA A 319 -0.157 -19.631 -29.025 1.00 81.85 O ANISOU 2776 O ALA A 319 9622 10028 11447 1370 2305 -1816 O ATOM 2777 CB ALA A 319 -2.943 -18.230 -27.890 1.00 68.41 C ANISOU 2777 CB ALA A 319 8156 8425 9411 978 1890 -1574 C ATOM 2778 N LEU A 320 -0.423 -19.789 -26.793 1.00 80.82 N ANISOU 2778 N LEU A 320 9445 9742 11519 1442 1994 -1529 N ATOM 2779 CA LEU A 320 1.009 -19.877 -26.532 1.00 80.46 C ANISOU 2779 CA LEU A 320 9177 9714 11681 1634 2053 -1490 C ATOM 2780 C LEU A 320 1.630 -21.098 -27.184 1.00 85.37 C ANISOU 2780 C LEU A 320 9815 10173 12450 1804 2246 -1660 C ATOM 2781 O LEU A 320 2.793 -21.045 -27.597 1.00 94.05 O ANISOU 2781 O LEU A 320 10732 11344 13658 1931 2384 -1706 O ATOM 2782 CB LEU A 320 1.275 -19.904 -25.031 1.00 77.16 C ANISOU 2782 CB LEU A 320 8666 9233 11418 1729 1855 -1285 C ATOM 2783 CG LEU A 320 0.908 -18.594 -24.350 1.00 73.13 C ANISOU 2783 CG LEU A 320 8102 8901 10783 1585 1679 -1125 C ATOM 2784 CD1 LEU A 320 1.068 -18.724 -22.855 1.00 73.43 C ANISOU 2784 CD1 LEU A 320 8084 8869 10945 1673 1479 -939 C ATOM 2785 CD2 LEU A 320 1.781 -17.482 -24.910 1.00 71.02 C ANISOU 2785 CD2 LEU A 320 7637 8863 10485 1551 1753 -1128 C ATOM 2786 N ARG A 321 0.892 -22.207 -27.270 1.00 86.69 N ANISOU 2786 N ARG A 321 10189 10114 12634 1811 2264 -1757 N ATOM 2787 CA ARG A 321 1.436 -23.369 -27.970 1.00 99.30 C ANISOU 2787 CA ARG A 321 11824 11541 14366 1968 2462 -1945 C ATOM 2788 C ARG A 321 1.659 -23.089 -29.455 1.00112.26 C ANISOU 2788 C ARG A 321 13477 13327 15850 1908 2681 -2153 C ATOM 2789 O ARG A 321 2.572 -23.660 -30.063 1.00116.07 O ANISOU 2789 O ARG A 321 13886 13762 16452 2066 2878 -2289 O ATOM 2790 CB ARG A 321 0.514 -24.575 -27.796 1.00 98.64 C ANISOU 2790 CB ARG A 321 11980 11174 14326 1957 2437 -2017 C ATOM 2791 CG ARG A 321 1.160 -25.750 -27.077 1.00101.42 C ANISOU 2791 CG ARG A 321 12302 11259 14972 2196 2443 -1974 C ATOM 2792 CD ARG A 321 0.595 -25.922 -25.681 1.00 99.39 C ANISOU 2792 CD ARG A 321 12098 10881 14785 2188 2219 -1751 C ATOM 2793 NE ARG A 321 -0.843 -26.163 -25.707 1.00 98.92 N ANISOU 2793 NE ARG A 321 12278 10727 14580 1986 2154 -1787 N ATOM 2794 N LYS A 322 0.845 -22.222 -30.052 1.00122.70 N ANISOU 2794 N LYS A 322 14890 14828 16903 1688 2655 -2176 N ATOM 2795 CA LYS A 322 0.924 -21.936 -31.485 1.00127.01 C ANISOU 2795 CA LYS A 322 15483 15523 17254 1611 2851 -2363 C ATOM 2796 C LYS A 322 2.168 -21.123 -31.839 1.00129.03 C ANISOU 2796 C LYS A 322 15497 15988 17539 1681 2979 -2325 C ATOM 2797 O LYS A 322 3.235 -21.682 -32.088 1.00133.36 O ANISOU 2797 O LYS A 322 15924 16487 18261 1865 3148 -2409 O ATOM 2798 CB LYS A 322 -0.334 -21.192 -31.952 1.00125.38 C ANISOU 2798 CB LYS A 322 15436 15452 16749 1361 2758 -2367 C TER 2799 LYS A 322 HETATM 2800 C4 KNW A2001 -18.756 18.830 -19.588 1.00 59.02 C HETATM 2801 C14 KNW A2001 -25.450 13.589 -19.851 1.00 49.08 C HETATM 2802 C5 KNW A2001 -17.802 17.895 -18.861 1.00 54.24 C HETATM 2803 C6 KNW A2001 -16.611 18.627 -18.266 1.00 52.41 C HETATM 2804 C11 KNW A2001 -23.014 16.743 -17.781 1.00 46.24 C HETATM 2805 C7 KNW A2001 -15.776 19.337 -19.312 1.00 54.31 C HETATM 2806 C8 KNW A2001 -20.950 17.706 -19.378 1.00 50.27 C HETATM 2807 C9 KNW A2001 -21.107 18.148 -18.060 1.00 47.44 C HETATM 2808 C10 KNW A2001 -22.136 17.675 -17.282 1.00 46.47 C HETATM 2809 C12 KNW A2001 -22.864 16.262 -19.070 1.00 46.86 C HETATM 2810 C13 KNW A2001 -24.801 14.662 -19.036 1.00 50.44 C HETATM 2811 N1 KNW A2001 -19.908 18.125 -20.172 1.00 56.03 N HETATM 2812 N2 KNW A2001 -23.748 15.293 -19.614 1.00 48.55 N HETATM 2813 C3 KNW A2001 -19.827 17.758 -21.587 1.00 50.91 C HETATM 2814 C1 KNW A2001 -21.149 17.169 -22.075 1.00 50.22 C HETATM 2815 C15 KNW A2001 -24.977 13.173 -21.093 1.00 51.29 C HETATM 2816 C16 KNW A2001 -25.616 12.170 -21.798 1.00 48.82 C HETATM 2817 C17 KNW A2001 -26.759 11.581 -21.270 1.00 50.07 C HETATM 2818 C18 KNW A2001 -26.865 9.936 -23.037 1.00 51.14 C HETATM 2819 C19 KNW A2001 -27.800 8.840 -23.489 1.00 47.96 C HETATM 2820 C2 KNW A2001 -20.968 16.422 -23.386 1.00 57.79 C HETATM 2821 C20 KNW A2001 -28.126 7.808 -22.411 1.00 40.49 C HETATM 2822 C21 KNW A2001 -29.109 6.744 -22.886 1.00 41.93 C HETATM 2823 C22 KNW A2001 -29.493 5.833 -21.752 1.00 41.26 C HETATM 2824 C23 KNW A2001 -28.783 4.669 -21.453 1.00 42.34 C HETATM 2825 C24 KNW A2001 -29.201 3.874 -20.408 1.00 48.36 C HETATM 2826 C25 KNW A2001 -30.301 4.159 -19.654 1.00 46.91 C HETATM 2827 C26 KNW A2001 -31.011 5.305 -19.938 1.00 45.33 C HETATM 2828 C27 KNW A2001 -30.617 6.117 -20.982 1.00 43.28 C HETATM 2829 C28 KNW A2001 -27.238 11.987 -20.035 1.00 44.76 C HETATM 2830 C29 KNW A2001 -26.588 12.982 -19.337 1.00 43.41 C HETATM 2831 C30 KNW A2001 -21.830 16.744 -19.870 1.00 46.55 C HETATM 2832 F1 KNW A2001 -28.509 2.742 -20.106 1.00 45.60 F HETATM 2833 O1 KNW A2001 -20.616 17.030 -24.372 1.00 63.15 O HETATM 2834 O2 KNW A2001 -21.169 15.226 -23.424 1.00 58.55 O1- HETATM 2835 O3 KNW A2001 -15.696 20.579 -19.264 1.00 53.50 O HETATM 2836 O4 KNW A2001 -15.227 18.641 -20.188 1.00 57.58 O1- HETATM 2837 O5 KNW A2001 -25.216 14.913 -17.908 1.00 50.86 O HETATM 2838 O6 KNW A2001 -27.452 10.581 -21.900 1.00 50.23 O HETATM 2839 O7 KNW A2001 -21.722 16.259 -21.144 1.00 46.25 O HETATM 2840 CL1 KNW A2001 -31.574 7.543 -21.293 1.00 50.82 CL HETATM 2841 C1 CLR A2002 -28.553 -11.587 5.979 1.00 47.22 C HETATM 2842 C2 CLR A2002 -29.097 -12.854 6.650 1.00 48.11 C HETATM 2843 C3 CLR A2002 -28.581 -14.112 5.943 1.00 50.80 C HETATM 2844 C4 CLR A2002 -27.051 -14.123 5.958 1.00 46.09 C HETATM 2845 C5 CLR A2002 -26.507 -12.866 5.315 1.00 46.27 C HETATM 2846 C6 CLR A2002 -25.567 -12.953 4.344 1.00 48.20 C HETATM 2847 C7 CLR A2002 -25.027 -11.744 3.595 1.00 48.65 C HETATM 2848 C8 CLR A2002 -25.245 -10.455 4.376 1.00 46.71 C HETATM 2849 C9 CLR A2002 -26.694 -10.409 4.850 1.00 45.19 C HETATM 2850 C10 CLR A2002 -27.025 -11.541 5.820 1.00 43.24 C HETATM 2851 C11 CLR A2002 -27.076 -9.060 5.465 1.00 46.10 C HETATM 2852 C12 CLR A2002 -26.694 -7.864 4.597 1.00 48.57 C HETATM 2853 C13 CLR A2002 -25.207 -7.906 4.250 1.00 54.38 C HETATM 2854 C14 CLR A2002 -24.968 -9.221 3.516 1.00 51.48 C HETATM 2855 C15 CLR A2002 -23.581 -9.063 2.905 1.00 52.49 C HETATM 2856 C16 CLR A2002 -23.503 -7.570 2.561 1.00 54.87 C HETATM 2857 C17 CLR A2002 -24.709 -6.882 3.220 1.00 58.58 C HETATM 2858 C18 CLR A2002 -24.329 -7.851 5.512 1.00 52.22 C HETATM 2859 C19 CLR A2002 -26.327 -11.300 7.155 1.00 37.38 C HETATM 2860 C20 CLR A2002 -24.404 -5.426 3.628 1.00 65.62 C HETATM 2861 C21 CLR A2002 -25.366 -4.759 4.605 1.00 68.99 C HETATM 2862 C22 CLR A2002 -24.546 -4.559 2.392 1.00 69.81 C HETATM 2863 C23 CLR A2002 -23.258 -3.993 1.826 1.00 70.10 C HETATM 2864 C24 CLR A2002 -23.389 -4.135 0.313 1.00 69.69 C HETATM 2865 C25 CLR A2002 -22.795 -2.947 -0.409 1.00 67.08 C HETATM 2866 C26 CLR A2002 -23.056 -3.029 -1.898 1.00 57.54 C HETATM 2867 C27 CLR A2002 -23.402 -1.681 0.160 1.00 74.85 C HETATM 2868 O1 CLR A2002 -29.105 -15.299 6.582 1.00 54.63 O HETATM 2869 O1 TLA A2003 -8.994 -20.787 -18.283 1.00114.57 O HETATM 2870 O11 TLA A2003 -9.888 -18.983 -17.412 1.00114.96 O HETATM 2871 C1 TLA A2003 -9.483 -20.163 -17.316 1.00115.37 C HETATM 2872 C2 TLA A2003 -9.576 -20.855 -15.980 1.00117.23 C HETATM 2873 O2 TLA A2003 -9.082 -22.198 -16.092 1.00116.83 O HETATM 2874 C3 TLA A2003 -11.017 -20.857 -15.455 1.00116.70 C HETATM 2875 O3 TLA A2003 -11.910 -21.402 -16.437 1.00113.55 O HETATM 2876 C4 TLA A2003 -11.106 -21.645 -14.174 1.00117.23 C HETATM 2877 O4 TLA A2003 -11.727 -22.731 -14.162 1.00117.54 O HETATM 2878 O41 TLA A2003 -10.550 -21.183 -13.156 1.00117.38 O HETATM 2879 C10 OLC A2004 -2.931 7.217 -11.149 1.00 83.02 C HETATM 2880 C9 OLC A2004 -2.757 8.278 -11.913 1.00 78.26 C HETATM 2881 C11 OLC A2004 -3.555 5.947 -11.722 1.00 83.43 C HETATM 2882 C8 OLC A2004 -3.167 8.259 -13.384 1.00 70.15 C HETATM 2883 C24 OLC A2004 -2.385 20.859 -15.562 1.00 89.80 C HETATM 2884 C12 OLC A2004 -3.050 4.739 -10.939 1.00 83.34 C HETATM 2885 C7 OLC A2004 -2.153 9.060 -14.197 1.00 66.48 C HETATM 2886 C13 OLC A2004 -3.538 3.456 -11.610 1.00 83.19 C HETATM 2887 C6 OLC A2004 -2.730 10.431 -14.529 1.00 65.43 C HETATM 2888 C14 OLC A2004 -3.260 2.270 -10.690 1.00 82.22 C HETATM 2889 C5 OLC A2004 -1.820 11.545 -14.013 1.00 64.60 C HETATM 2890 C4 OLC A2004 -1.960 12.769 -14.923 1.00 64.76 C HETATM 2891 C3 OLC A2004 -1.941 14.064 -14.112 1.00 67.24 C HETATM 2892 C2 OLC A2004 -1.985 15.269 -15.054 1.00 73.37 C HETATM 2893 C21 OLC A2004 -2.374 18.888 -14.010 1.00 81.68 C HETATM 2894 C1 OLC A2004 -2.045 16.573 -14.254 1.00 77.02 C HETATM 2895 C22 OLC A2004 -1.632 20.157 -14.432 1.00 90.61 C HETATM 2896 O19 OLC A2004 -2.097 16.517 -13.075 1.00 81.30 O HETATM 2897 O25 OLC A2004 -1.548 21.815 -16.160 1.00 88.55 O HETATM 2898 O23 OLC A2004 -1.518 21.037 -13.342 1.00 95.92 O HETATM 2899 O20 OLC A2004 -2.037 17.802 -14.872 1.00 77.42 O HETATM 2900 C10 OLC A2005 -5.474 6.184 -16.487 1.00 64.24 C HETATM 2901 C9 OLC A2005 -6.165 7.229 -16.085 1.00 68.27 C HETATM 2902 C11 OLC A2005 -5.573 4.838 -15.778 1.00 63.11 C HETATM 2903 C8 OLC A2005 -7.108 7.148 -14.887 1.00 74.91 C HETATM 2904 C24 OLC A2005 -4.038 18.521 -10.632 1.00 87.71 C HETATM 2905 C12 OLC A2005 -4.601 3.864 -16.453 1.00 67.90 C HETATM 2906 C7 OLC A2005 -7.567 8.555 -14.495 1.00 77.32 C HETATM 2907 C13 OLC A2005 -3.918 2.983 -15.406 1.00 70.64 C HETATM 2908 C6 OLC A2005 -7.086 8.828 -13.069 1.00 80.59 C HETATM 2909 C14 OLC A2005 -3.294 1.758 -16.068 1.00 69.34 C HETATM 2910 C5 OLC A2005 -7.148 10.321 -12.741 1.00 79.06 C HETATM 2911 C4 OLC A2005 -5.956 10.693 -11.856 1.00 75.33 C HETATM 2912 C3 OLC A2005 -6.421 11.640 -10.753 1.00 75.63 C HETATM 2913 C2 OLC A2005 -5.237 12.401 -10.156 1.00 78.69 C HETATM 2914 C21 OLC A2005 -4.844 16.160 -10.398 1.00 84.51 C HETATM 2915 C1 OLC A2005 -5.297 13.860 -10.604 1.00 85.29 C HETATM 2916 C22 OLC A2005 -3.668 17.113 -10.166 1.00 87.73 C HETATM 2917 O19 OLC A2005 -6.051 14.162 -11.461 1.00 93.33 O HETATM 2918 O25 OLC A2005 -4.247 19.361 -9.529 1.00 85.41 O HETATM 2919 O23 OLC A2005 -3.341 17.147 -8.805 1.00 91.15 O HETATM 2920 O20 OLC A2005 -4.492 14.820 -10.041 1.00 84.98 O HETATM 2921 C10 OLC A2006 -2.492 6.091 -32.774 1.00 82.20 C HETATM 2922 C9 OLC A2006 -1.802 7.016 -32.141 1.00 81.08 C HETATM 2923 C8 OLC A2006 -2.314 8.450 -32.081 1.00 79.56 C HETATM 2924 C24 OLC A2006 -0.900 20.680 -31.595 1.00112.49 C HETATM 2925 C7 OLC A2006 -1.487 9.226 -31.064 1.00 79.73 C HETATM 2926 C6 OLC A2006 -1.498 10.710 -31.419 1.00 81.85 C HETATM 2927 C5 OLC A2006 -2.852 11.318 -31.064 1.00 85.65 C HETATM 2928 C4 OLC A2006 -2.642 12.755 -30.598 1.00 90.18 C HETATM 2929 C3 OLC A2006 -2.348 13.644 -31.803 1.00 94.41 C HETATM 2930 C2 OLC A2006 -1.833 14.998 -31.323 1.00101.84 C HETATM 2931 C21 OLC A2006 -1.187 18.220 -31.976 1.00111.54 C HETATM 2932 C1 OLC A2006 -1.987 16.049 -32.423 1.00110.51 C HETATM 2933 C22 OLC A2006 -1.621 19.615 -32.419 1.00114.72 C HETATM 2934 O19 OLC A2006 -1.834 15.756 -33.562 1.00116.24 O HETATM 2935 O25 OLC A2006 -1.378 21.952 -31.945 1.00111.16 O HETATM 2936 O23 OLC A2006 -1.307 19.773 -33.775 1.00120.19 O HETATM 2937 O20 OLC A2006 -2.306 17.342 -32.097 1.00111.22 O HETATM 2938 C10 OLC A2007 -4.528 -4.989 -18.076 1.00 74.15 C HETATM 2939 C9 OLC A2007 -4.037 -5.610 -19.129 1.00 78.03 C HETATM 2940 C11 OLC A2007 -4.281 -3.502 -17.869 1.00 73.22 C HETATM 2941 C8 OLC A2007 -3.204 -4.875 -20.181 1.00 76.20 C HETATM 2942 C12 OLC A2007 -5.327 -2.969 -16.898 1.00 74.58 C HETATM 2943 C7 OLC A2007 -2.055 -5.781 -20.628 1.00 75.47 C HETATM 2944 C13 OLC A2007 -4.682 -2.776 -15.532 1.00 77.70 C HETATM 2945 C14 OLC A2007 -4.856 -1.316 -15.126 1.00 81.29 C HETATM 2946 C10 OLC A2008 -30.667 -10.368 -8.734 1.00 67.01 C HETATM 2947 C9 OLC A2008 -30.476 -11.655 -8.953 1.00 65.42 C HETATM 2948 C11 OLC A2008 -31.936 -9.653 -9.195 1.00 66.68 C HETATM 2949 C8 OLC A2008 -31.510 -12.508 -9.682 1.00 64.10 C HETATM 2950 C12 OLC A2008 -31.955 -8.258 -8.571 1.00 67.71 C HETATM 2951 C15 OLC A2008 -34.445 -5.398 -8.551 1.00 67.50 C HETATM 2952 C13 OLC A2008 -33.362 -7.660 -8.600 1.00 66.46 C HETATM 2953 C14 OLC A2008 -33.267 -6.213 -9.077 1.00 67.03 C HETATM 2954 C18 OLC A2009 -28.282 -5.345 -0.488 1.00 77.19 C HETATM 2955 C10 OLC A2009 -28.962 1.641 -4.806 1.00 73.56 C HETATM 2956 C9 OLC A2009 -29.658 2.686 -5.207 1.00 71.10 C HETATM 2957 C17 OLC A2009 -28.023 -4.004 0.195 1.00 78.39 C HETATM 2958 C11 OLC A2009 -28.717 1.384 -3.318 1.00 75.92 C HETATM 2959 C8 OLC A2009 -30.237 3.674 -4.197 1.00 68.89 C HETATM 2960 C24 OLC A2009 -34.196 15.001 -6.238 1.00 84.93 C HETATM 2961 C16 OLC A2009 -29.128 -3.019 -0.177 1.00 80.11 C HETATM 2962 C12 OLC A2009 -27.576 0.377 -3.152 1.00 79.14 C HETATM 2963 C7 OLC A2009 -30.078 5.100 -4.728 1.00 68.56 C HETATM 2964 C15 OLC A2009 -28.904 -2.509 -1.601 1.00 84.21 C HETATM 2965 C13 OLC A2009 -27.667 -0.331 -1.799 1.00 79.99 C HETATM 2966 C6 OLC A2009 -30.791 6.082 -3.798 1.00 66.86 C HETATM 2967 C14 OLC A2009 -29.040 -0.985 -1.654 1.00 83.93 C HETATM 2968 C5 OLC A2009 -30.500 7.525 -4.204 1.00 65.35 C HETATM 2969 C4 OLC A2009 -31.629 8.415 -3.684 1.00 66.62 C HETATM 2970 C3 OLC A2009 -31.306 9.892 -3.915 1.00 69.20 C HETATM 2971 C2 OLC A2009 -32.592 10.716 -3.994 1.00 73.14 C HETATM 2972 C21 OLC A2009 -32.502 14.458 -4.508 1.00 79.21 C HETATM 2973 C1 OLC A2009 -32.247 12.206 -3.948 1.00 79.37 C HETATM 2974 C22 OLC A2009 -33.622 15.414 -4.888 1.00 87.50 C HETATM 2975 O19 OLC A2009 -31.297 12.569 -3.342 1.00 86.82 O HETATM 2976 O25 OLC A2009 -34.475 16.147 -6.995 1.00 86.14 O HETATM 2977 O23 OLC A2009 -34.633 15.323 -3.926 1.00 97.03 O HETATM 2978 O20 OLC A2009 -33.017 13.133 -4.599 1.00 77.77 O HETATM 2979 C9 OLC A2010 -2.989 -5.528 -29.952 1.00 88.10 C HETATM 2980 C8 OLC A2010 -2.840 -7.043 -29.800 1.00 87.99 C HETATM 2981 C7 OLC A2010 -3.320 -7.751 -31.069 1.00 85.45 C HETATM 2982 C6 OLC A2010 -2.826 -9.197 -31.054 1.00 82.44 C HETATM 2983 C5 OLC A2010 -3.016 -9.847 -32.423 1.00 83.82 C HETATM 2984 C4 OLC A2010 -2.345 -11.221 -32.410 1.00 88.73 C HETATM 2985 C3 OLC A2010 -1.992 -11.671 -33.828 1.00 91.89 C HETATM 2986 C2 OLC A2010 -3.262 -11.792 -34.669 1.00 93.97 C HETATM 2987 C10 OLC A2011 -6.504 9.957 -34.948 1.00 85.72 C HETATM 2988 C9 OLC A2011 -5.818 11.084 -34.912 1.00 86.23 C HETATM 2989 C11 OLC A2011 -5.795 8.606 -35.090 1.00 80.27 C HETATM 2990 C8 OLC A2011 -4.295 11.051 -35.008 1.00 86.29 C HETATM 2991 C12 OLC A2011 -6.695 7.509 -34.521 1.00 74.36 C HETATM 2992 C7 OLC A2011 -3.803 12.272 -35.783 1.00 84.80 C HETATM 2993 C15 OLC A2011 -6.416 3.774 -34.677 1.00 70.77 C HETATM 2994 C13 OLC A2011 -6.505 6.193 -35.274 1.00 69.52 C HETATM 2995 C6 OLC A2011 -4.518 13.516 -35.264 1.00 81.11 C HETATM 2996 C14 OLC A2011 -7.186 5.075 -34.485 1.00 67.54 C HETATM 2997 C5 OLC A2011 -4.478 14.604 -36.334 1.00 80.34 C HETATM 2998 C4 OLC A2011 -3.036 15.055 -36.535 1.00 81.15 C HETATM 2999 C10 OLC A2012 -8.187 8.266 -6.964 1.00 94.06 C HETATM 3000 C9 OLC A2012 -8.311 9.558 -6.724 1.00 94.17 C HETATM 3001 C11 OLC A2012 -7.131 7.742 -7.935 1.00 93.01 C HETATM 3002 C8 OLC A2012 -7.404 10.582 -7.406 1.00 90.73 C HETATM 3003 C12 OLC A2012 -7.631 6.442 -8.562 1.00 92.43 C HETATM 3004 C7 OLC A2012 -7.841 11.989 -7.008 1.00 88.89 C HETATM 3005 C15 OLC A2012 -6.665 4.535 -10.509 1.00 88.22 C HETATM 3006 C13 OLC A2012 -6.747 5.276 -8.125 1.00 92.24 C HETATM 3007 C6 OLC A2012 -6.614 12.790 -6.577 1.00 90.65 C HETATM 3008 C14 OLC A2012 -6.947 4.096 -9.074 1.00 89.64 C HETATM 3009 C5 OLC A2012 -7.027 14.226 -6.250 1.00 90.31 C HETATM 3010 C10 OLC A2013 -8.887 -6.363 -5.424 1.00 84.80 C HETATM 3011 C9 OLC A2013 -9.601 -7.258 -4.768 1.00 84.65 C HETATM 3012 C8 OLC A2013 -9.895 -8.618 -5.402 1.00 85.44 C HETATM 3013 C24 OLC A2013 -14.110 -20.091 -2.171 1.00 84.88 C HETATM 3014 C7 OLC A2013 -10.663 -9.505 -4.424 1.00 86.32 C HETATM 3015 C6 OLC A2013 -10.986 -10.864 -5.049 1.00 84.63 C HETATM 3016 C5 OLC A2013 -11.561 -11.779 -3.963 1.00 84.90 C HETATM 3017 C4 OLC A2013 -11.631 -13.225 -4.456 1.00 84.09 C HETATM 3018 C3 OLC A2013 -12.021 -14.153 -3.304 1.00 82.16 C HETATM 3019 C2 OLC A2013 -12.733 -15.384 -3.869 1.00 82.58 C HETATM 3020 C21 OLC A2013 -14.044 -17.648 -1.674 1.00 87.73 C HETATM 3021 C1 OLC A2013 -12.427 -16.621 -3.025 1.00 87.07 C HETATM 3022 C22 OLC A2013 -14.866 -18.928 -1.529 1.00 86.90 C HETATM 3023 O19 OLC A2013 -11.387 -16.711 -2.458 1.00 92.65 O HETATM 3024 O25 OLC A2013 -15.026 -21.066 -2.586 1.00 79.51 O HETATM 3025 O23 OLC A2013 -15.073 -19.196 -0.168 1.00 85.61 O HETATM 3026 O20 OLC A2013 -13.352 -17.632 -2.922 1.00 85.71 O HETATM 3027 C18 OLC A2014 -10.707 -2.306 -1.783 1.00 85.06 C HETATM 3028 C10 OLC A2014 -15.805 -10.392 0.494 1.00 75.31 C HETATM 3029 C9 OLC A2014 -15.087 -11.489 0.580 1.00 75.43 C HETATM 3030 C17 OLC A2014 -10.786 -3.679 -1.117 1.00 83.73 C HETATM 3031 C11 OLC A2014 -15.254 -9.092 1.073 1.00 78.47 C HETATM 3032 C8 OLC A2014 -13.712 -11.448 1.249 1.00 77.09 C HETATM 3033 C16 OLC A2014 -12.170 -4.276 -1.355 1.00 83.49 C HETATM 3034 C12 OLC A2014 -15.124 -8.031 -0.015 1.00 80.81 C HETATM 3035 C7 OLC A2014 -12.620 -11.775 0.229 1.00 76.70 C HETATM 3036 C15 OLC A2014 -12.168 -5.761 -0.993 1.00 84.19 C HETATM 3037 C13 OLC A2014 -13.692 -7.503 -0.028 1.00 84.89 C HETATM 3038 C14 OLC A2014 -13.617 -6.235 -0.878 1.00 85.43 C HETATM 3039 C18 OLC A2015 -34.520 4.263 -19.702 1.00 67.64 C HETATM 3040 C10 OLC A2015 -32.375 -4.107 -21.114 1.00 53.79 C HETATM 3041 C9 OLC A2015 -32.572 -5.339 -20.695 1.00 59.04 C HETATM 3042 C17 OLC A2015 -33.516 3.506 -20.563 1.00 78.23 C HETATM 3043 C11 OLC A2015 -31.277 -3.193 -20.601 1.00 50.26 C HETATM 3044 C8 OLC A2015 -31.699 -5.988 -19.626 1.00 64.98 C HETATM 3045 C16 OLC A2015 -33.599 1.984 -20.510 1.00 77.93 C HETATM 3046 C12 OLC A2015 -31.919 -1.859 -20.232 1.00 52.57 C HETATM 3047 C15 OLC A2015 -32.547 1.435 -21.477 1.00 66.96 C HETATM 3048 C13 OLC A2015 -31.592 -0.823 -21.298 1.00 53.87 C HETATM 3049 C14 OLC A2015 -31.586 0.565 -20.677 1.00 55.88 C HETATM 3050 C9 OLC A2016 -13.462 -5.336 -33.427 1.00 82.08 C HETATM 3051 C8 OLC A2016 -12.950 -6.468 -34.314 1.00 83.71 C HETATM 3052 C24 OLC A2016 -18.532 -16.122 -30.409 1.00117.80 C HETATM 3053 C7 OLC A2016 -13.183 -7.811 -33.627 1.00 84.61 C HETATM 3054 C6 OLC A2016 -13.958 -8.730 -34.566 1.00 89.24 C HETATM 3055 C5 OLC A2016 -15.315 -9.065 -33.951 1.00 95.65 C HETATM 3056 C4 OLC A2016 -15.335 -10.535 -33.536 1.00101.44 C HETATM 3057 C3 OLC A2016 -16.456 -11.281 -34.262 1.00105.94 C HETATM 3058 C2 OLC A2016 -17.303 -12.067 -33.258 1.00109.71 C HETATM 3059 C21 OLC A2016 -17.381 -15.382 -32.518 1.00116.67 C HETATM 3060 C1 OLC A2016 -17.647 -13.450 -33.818 1.00113.16 C HETATM 3061 C22 OLC A2016 -18.154 -16.514 -31.840 1.00119.38 C HETATM 3062 O19 OLC A2016 -17.377 -13.715 -34.942 1.00116.87 O HETATM 3063 O25 OLC A2016 -19.636 -16.877 -29.990 1.00116.25 O HETATM 3064 O23 OLC A2016 -19.304 -16.814 -32.585 1.00121.43 O HETATM 3065 O20 OLC A2016 -18.270 -14.392 -33.035 1.00113.69 O HETATM 3066 C9 OLC A2017 -13.533 6.947 -35.127 1.00 60.25 C HETATM 3067 C8 OLC A2017 -14.095 8.348 -34.873 1.00 64.65 C HETATM 3068 C24 OLC A2017 -14.617 16.851 -42.408 1.00109.71 C HETATM 3069 C7 OLC A2017 -14.599 8.993 -36.167 1.00 71.92 C HETATM 3070 C6 OLC A2017 -13.627 10.076 -36.645 1.00 79.68 C HETATM 3071 C5 OLC A2017 -14.155 10.786 -37.898 1.00 86.04 C HETATM 3072 C4 OLC A2017 -13.078 10.811 -38.990 1.00 91.24 C HETATM 3073 C3 OLC A2017 -12.587 12.233 -39.276 1.00 93.07 C HETATM 3074 C2 OLC A2017 -12.952 12.653 -40.702 1.00 96.09 C HETATM 3075 C21 OLC A2017 -12.342 16.246 -41.563 1.00104.17 C HETATM 3076 C1 OLC A2017 -12.256 13.963 -41.081 1.00 97.94 C HETATM 3077 C22 OLC A2017 -13.163 17.302 -42.301 1.00107.03 C HETATM 3078 O19 OLC A2017 -11.114 14.127 -40.820 1.00 96.86 O HETATM 3079 O25 OLC A2017 -15.101 17.109 -43.696 1.00112.47 O HETATM 3080 O23 OLC A2017 -13.094 18.517 -41.607 1.00107.23 O HETATM 3081 O20 OLC A2017 -12.936 14.960 -41.732 1.00101.10 O HETATM 3082 C10 OLC A2018 -12.864 -7.156 5.209 1.00 75.38 C HETATM 3083 C9 OLC A2018 -12.673 -8.307 5.822 1.00 72.87 C HETATM 3084 C11 OLC A2018 -14.073 -6.978 4.288 1.00 78.08 C HETATM 3085 C8 OLC A2018 -13.655 -9.456 5.600 1.00 70.93 C HETATM 3086 C12 OLC A2018 -13.871 -5.784 3.353 1.00 82.95 C HETATM 3087 C7 OLC A2018 -13.329 -10.546 6.616 1.00 73.41 C HETATM 3088 C15 OLC A2018 -12.833 -2.156 3.733 1.00 84.51 C HETATM 3089 C13 OLC A2018 -13.662 -4.491 4.147 1.00 85.56 C HETATM 3090 C6 OLC A2018 -13.279 -11.913 5.933 1.00 74.24 C HETATM 3091 C14 OLC A2018 -13.700 -3.295 3.194 1.00 87.06 C HETATM 3092 C5 OLC A2018 -12.078 -12.678 6.489 1.00 73.37 C HETATM 3093 C4 OLC A2018 -12.362 -14.177 6.518 1.00 70.02 C HETATM 3094 C3 OLC A2018 -11.037 -14.907 6.715 1.00 69.72 C HETATM 3095 C2 OLC A2018 -11.228 -16.403 6.465 1.00 70.98 C HETATM 3096 C18 OLC A2019 -32.890 -12.702 -14.127 1.00 83.31 C HETATM 3097 C10 OLC A2019 -32.400 -4.143 -14.496 1.00 87.74 C HETATM 3098 C9 OLC A2019 -31.129 -4.417 -14.751 1.00 88.96 C HETATM 3099 C17 OLC A2019 -33.062 -11.650 -13.034 1.00 82.89 C HETATM 3100 C11 OLC A2019 -33.433 -5.246 -14.262 1.00 88.22 C HETATM 3101 C8 OLC A2019 -30.613 -5.857 -14.809 1.00 88.08 C HETATM 3102 C16 OLC A2019 -33.068 -10.251 -13.645 1.00 85.15 C HETATM 3103 C12 OLC A2019 -33.736 -5.401 -12.774 1.00 89.18 C HETATM 3104 C7 OLC A2019 -30.792 -6.482 -16.195 1.00 87.73 C HETATM 3105 C15 OLC A2019 -33.442 -9.233 -12.567 1.00 87.90 C HETATM 3106 C13 OLC A2019 -34.162 -6.839 -12.469 1.00 88.96 C HETATM 3107 C6 OLC A2019 -30.299 -7.927 -16.134 1.00 88.85 C HETATM 3108 C14 OLC A2019 -33.156 -7.819 -13.067 1.00 89.00 C HETATM 3109 C5 OLC A2019 -31.030 -8.837 -17.120 1.00 89.88 C HETATM 3110 C4 OLC A2019 -30.338 -10.201 -17.073 1.00 88.18 C HETATM 3111 C3 OLC A2019 -31.313 -11.353 -17.306 1.00 84.58 C HETATM 3112 C2 OLC A2019 -30.543 -12.672 -17.203 1.00 81.55 C HETATM 3113 C1 OLA A2020 -31.832 16.087 -10.810 1.00 85.91 C HETATM 3114 O1 OLA A2020 -31.664 16.207 -12.047 1.00 87.96 O HETATM 3115 O2 OLA A2020 -32.397 16.946 -10.094 1.00 89.66 O HETATM 3116 C2 OLA A2020 -31.322 14.838 -10.140 1.00 82.13 C HETATM 3117 C3 OLA A2020 -32.465 14.184 -9.385 1.00 78.32 C HETATM 3118 C4 OLA A2020 -32.437 12.676 -9.572 1.00 75.60 C HETATM 3119 C5 OLA A2020 -32.344 11.999 -8.214 1.00 76.26 C HETATM 3120 C6 OLA A2020 -33.664 11.348 -7.835 1.00 74.85 C HETATM 3121 C7 OLA A2020 -33.661 9.903 -8.301 1.00 75.81 C HETATM 3122 C8 OLA A2020 -33.547 8.951 -7.121 1.00 76.85 C HETATM 3123 C9 OLA A2020 -34.900 8.325 -6.905 1.00 74.93 C HETATM 3124 C10 OLA A2020 -35.048 7.012 -7.046 1.00 73.68 C HETATM 3125 C11 OLA A2020 -33.862 6.151 -7.402 1.00 77.04 C HETATM 3126 C12 OLA A2020 -34.316 4.695 -7.455 1.00 82.37 C HETATM 3127 C13 OLA A2020 -33.138 3.742 -7.285 1.00 82.47 C HETATM 3128 C14 OLA A2020 -32.999 2.812 -8.481 1.00 80.93 C HETATM 3129 C1 OLA A2021 -33.637 -15.723 -5.635 1.00108.48 C HETATM 3130 O1 OLA A2021 -33.268 -15.732 -6.835 1.00109.34 O HETATM 3131 O2 OLA A2021 -33.862 -16.763 -4.977 1.00110.84 O HETATM 3132 C2 OLA A2021 -33.810 -14.397 -4.932 1.00101.99 C HETATM 3133 C3 OLA A2021 -34.201 -13.329 -5.944 1.00 94.44 C HETATM 3134 C4 OLA A2021 -35.289 -12.436 -5.373 1.00 90.70 C HETATM 3135 C5 OLA A2021 -34.748 -11.097 -4.900 1.00 87.25 C HETATM 3136 C6 OLA A2021 -35.600 -9.988 -5.497 1.00 88.22 C HETATM 3137 C7 OLA A2021 -35.439 -8.672 -4.755 1.00 94.07 C HETATM 3138 C8 OLA A2021 -36.393 -7.632 -5.328 1.00 97.14 C HETATM 3139 C9 OLA A2021 -36.448 -6.446 -4.393 1.00100.14 C HETATM 3140 C10 OLA A2021 -36.882 -5.260 -4.819 1.00102.80 C HETATM 3141 C11 OLA A2021 -37.359 -5.065 -6.242 1.00102.84 C HETATM 3142 C12 OLA A2021 -37.798 -3.618 -6.442 1.00101.26 C HETATM 3143 C13 OLA A2021 -36.573 -2.720 -6.558 1.00 98.49 C HETATM 3144 C14 OLA A2021 -36.917 -1.328 -7.069 1.00 94.17 C HETATM 3145 C15 OLA A2021 -35.948 -0.906 -8.167 1.00 88.65 C HETATM 3146 C1 OLA A2022 -34.096 -17.639 -0.101 1.00117.97 C HETATM 3147 O1 OLA A2022 -33.900 -17.666 -1.337 1.00122.72 O HETATM 3148 O2 OLA A2022 -34.174 -18.673 0.601 1.00116.59 O HETATM 3149 C2 OLA A2022 -34.261 -16.294 0.569 1.00112.83 C HETATM 3150 C3 OLA A2022 -33.220 -15.324 0.017 1.00107.81 C HETATM 3151 C4 OLA A2022 -33.862 -14.201 -0.790 1.00105.41 C HETATM 3152 C5 OLA A2022 -33.967 -12.915 0.022 1.00100.68 C HETATM 3153 C6 OLA A2022 -33.296 -11.743 -0.687 1.00 93.04 C HETATM 3154 C7 OLA A2022 -34.054 -10.450 -0.420 1.00 87.05 C HETATM 3155 C8 OLA A2022 -33.292 -9.236 -0.930 1.00 82.85 C HETATM 3156 C9 OLA A2022 -34.083 -7.979 -0.649 1.00 78.26 C HETATM 3157 C10 OLA A2022 -33.485 -6.908 -0.131 1.00 76.05 C HETATM 3158 C1 OLA A2023 -16.030 -19.938 4.270 1.00 64.82 C HETATM 3159 O1 OLA A2023 -16.982 -20.052 3.460 1.00 62.38 O HETATM 3160 O2 OLA A2023 -15.639 -20.885 4.996 1.00 67.16 O HETATM 3161 C2 OLA A2023 -15.328 -18.601 4.380 1.00 59.67 C HETATM 3162 C3 OLA A2023 -15.788 -17.697 3.244 1.00 62.59 C HETATM 3163 C4 OLA A2023 -15.991 -16.257 3.710 1.00 67.96 C HETATM 3164 C5 OLA A2023 -16.440 -15.380 2.542 1.00 71.48 C HETATM 3165 C6 OLA A2023 -16.430 -13.889 2.881 1.00 72.14 C HETATM 3166 C7 OLA A2023 -17.694 -13.439 3.603 1.00 69.47 C HETATM 3167 C8 OLA A2023 -17.825 -11.919 3.659 1.00 66.01 C HETATM 3168 C9 OLA A2023 -18.942 -11.586 4.620 1.00 67.65 C HETATM 3169 C10 OLA A2023 -19.375 -10.345 4.846 1.00 67.54 C HETATM 3170 C11 OLA A2023 -18.808 -9.145 4.135 1.00 65.29 C HETATM 3171 C12 OLA A2023 -19.693 -7.936 4.407 1.00 63.77 C HETATM 3172 C13 OLA A2023 -18.947 -6.654 4.061 1.00 63.77 C HETATM 3173 C14 OLA A2023 -19.409 -6.109 2.720 1.00 67.98 C HETATM 3174 C15 OLA A2023 -18.242 -5.485 1.973 1.00 75.42 C HETATM 3175 C16 OLA A2023 -18.690 -4.754 0.709 1.00 80.93 C HETATM 3176 C17 OLA A2023 -18.039 -5.354 -0.535 1.00 82.08 C HETATM 3177 C18 OLA A2023 -17.888 -4.340 -1.650 1.00 79.59 C HETATM 3178 C1 OLA A2024 0.957 -16.092 -30.904 1.00103.76 C HETATM 3179 O1 OLA A2024 0.229 -17.110 -30.934 1.00102.00 O HETATM 3180 O2 OLA A2024 2.113 -16.064 -31.386 1.00104.36 O HETATM 3181 C2 OLA A2024 0.412 -14.839 -30.255 1.00103.98 C HETATM 3182 C3 OLA A2024 0.148 -13.792 -31.330 1.00104.74 C HETATM 3183 C4 OLA A2024 1.107 -12.617 -31.210 1.00103.22 C HETATM 3184 C5 OLA A2024 0.522 -11.545 -30.303 1.00100.85 C HETATM 3185 C6 OLA A2024 1.357 -11.386 -29.044 1.00 98.56 C HETATM 3186 C7 OLA A2024 1.862 -9.954 -28.903 1.00 96.12 C HETATM 3187 C8 OLA A2024 3.001 -9.898 -27.893 1.00 91.63 C HETATM 3188 C9 OLA A2024 3.169 -8.492 -27.377 1.00 87.49 C HETATM 3189 C10 OLA A2024 3.705 -8.277 -26.176 1.00 87.32 C HETATM 3190 C11 OLA A2024 4.175 -9.410 -25.290 1.00 85.15 C HETATM 3191 C12 OLA A2024 5.276 -8.918 -24.348 1.00 83.63 C HETATM 3192 C13 OLA A2024 4.991 -9.308 -22.897 1.00 83.47 C HETATM 3193 C14 OLA A2024 4.610 -10.784 -22.771 1.00 85.32 C HETATM 3194 C15 OLA A2024 3.191 -10.966 -22.227 1.00 81.59 C HETATM 3195 C16 OLA A2024 2.506 -12.218 -22.775 1.00 73.21 C HETATM 3196 C17 OLA A2024 1.120 -11.890 -23.326 1.00 66.70 C HETATM 3197 C18 OLA A2024 0.630 -12.943 -24.302 1.00 62.90 C HETATM 3198 C1 OLA A2025 -8.360 18.196 -42.125 1.00114.92 C HETATM 3199 O1 OLA A2025 -9.530 18.449 -42.486 1.00118.01 O HETATM 3200 O2 OLA A2025 -7.584 19.067 -41.669 1.00118.19 O HETATM 3201 C2 OLA A2025 -7.863 16.773 -42.241 1.00105.21 C HETATM 3202 C3 OLA A2025 -7.685 16.222 -40.833 1.00 96.17 C HETATM 3203 C4 OLA A2025 -6.934 14.901 -40.827 1.00 88.35 C HETATM 3204 C5 OLA A2025 -7.874 13.719 -41.004 1.00 82.56 C HETATM 3205 C6 OLA A2025 -7.592 12.672 -39.933 1.00 78.70 C HETATM 3206 C7 OLA A2025 -7.458 11.273 -40.518 1.00 75.99 C HETATM 3207 C8 OLA A2025 -6.278 10.537 -39.892 1.00 76.96 C HETATM 3208 C1 OLA A2026 -7.430 -16.411 -34.658 1.00108.60 C HETATM 3209 O1 OLA A2026 -8.552 -16.965 -34.628 1.00110.41 O HETATM 3210 O2 OLA A2026 -6.352 -17.007 -34.413 1.00107.45 O HETATM 3211 C2 OLA A2026 -7.375 -14.945 -35.015 1.00105.74 C HETATM 3212 C3 OLA A2026 -8.769 -14.342 -34.907 1.00103.00 C HETATM 3213 C4 OLA A2026 -8.730 -12.831 -35.096 1.00103.49 C HETATM 3214 C5 OLA A2026 -8.075 -12.130 -33.912 1.00102.30 C HETATM 3215 C6 OLA A2026 -8.109 -10.613 -34.071 1.00 97.51 C HETATM 3216 C7 OLA A2026 -7.988 -9.913 -32.722 1.00 92.92 C HETATM 3217 C8 OLA A2026 -7.395 -8.522 -32.888 1.00 88.95 C HETATM 3218 C9 OLA A2026 -8.489 -7.487 -32.965 1.00 88.16 C HETATM 3219 C10 OLA A2026 -8.173 -6.199 -32.840 1.00 89.18 C HETATM 3220 C11 OLA A2026 -6.731 -5.785 -32.648 1.00 90.12 C HETATM 3221 C12 OLA A2026 -6.669 -4.280 -32.414 1.00 90.86 C HETATM 3222 C13 OLA A2026 -6.104 -3.525 -33.608 1.00 92.14 C HETATM 3223 C14 OLA A2026 -7.033 -2.382 -34.005 1.00 91.55 C HETATM 3224 C15 OLA A2026 -7.146 -1.323 -32.909 1.00 85.34 C HETATM 3225 C16 OLA A2026 -6.747 0.045 -33.450 1.00 78.20 C HETATM 3226 C17 OLA A2026 -7.484 1.149 -32.710 1.00 75.81 C HETATM 3227 C1 OLA A2027 -27.499 -10.783 -32.564 1.00 90.32 C HETATM 3228 O1 OLA A2027 -28.278 -9.942 -33.061 1.00 93.48 O HETATM 3229 O2 OLA A2027 -27.732 -12.016 -32.562 1.00 91.45 O HETATM 3230 C2 OLA A2027 -26.222 -10.282 -31.932 1.00 83.49 C HETATM 3231 C3 OLA A2027 -26.040 -8.792 -32.194 1.00 76.33 C HETATM 3232 C4 OLA A2027 -24.933 -8.253 -31.300 1.00 74.80 C HETATM 3233 C5 OLA A2027 -23.661 -7.926 -32.073 1.00 80.16 C HETATM 3234 C6 OLA A2027 -23.538 -6.421 -32.285 1.00 83.34 C HETATM 3235 C7 OLA A2027 -22.114 -5.938 -32.027 1.00 82.90 C HETATM 3236 C8 OLA A2027 -22.135 -4.478 -31.587 1.00 79.40 C HETATM 3237 C9 OLA A2027 -20.903 -3.785 -32.103 1.00 75.14 C HETATM 3238 C10 OLA A2027 -20.909 -2.493 -32.418 1.00 73.51 C HETATM 3239 C11 OLA A2027 -22.114 -1.601 -32.265 1.00 73.78 C HETATM 3240 C12 OLA A2027 -21.593 -0.165 -32.306 1.00 76.69 C HETATM 3241 C13 OLA A2027 -22.492 0.843 -31.592 1.00 74.21 C HETATM 3242 C14 OLA A2027 -21.736 2.135 -31.289 1.00 70.32 C HETATM 3243 C15 OLA A2027 -20.453 1.817 -30.539 1.00 65.89 C HETATM 3244 C16 OLA A2027 -19.857 3.029 -29.839 1.00 62.12 C HETATM 3245 C17 OLA A2027 -18.731 2.572 -28.918 1.00 60.35 C HETATM 3246 C18 OLA A2027 -19.136 1.305 -28.180 1.00 56.95 C HETATM 3247 C1 OLA A2028 -8.007 -13.764 -7.023 1.00 99.64 C HETATM 3248 O1 OLA A2028 -8.627 -14.448 -6.179 1.00102.95 O HETATM 3249 O2 OLA A2028 -7.513 -14.260 -8.059 1.00102.34 O HETATM 3250 C2 OLA A2028 -7.837 -12.282 -6.784 1.00 92.68 C HETATM 3251 C3 OLA A2028 -7.971 -11.549 -8.113 1.00 88.72 C HETATM 3252 C4 OLA A2028 -8.086 -10.039 -7.944 1.00 87.11 C HETATM 3253 C5 OLA A2028 -6.863 -9.309 -8.486 1.00 87.65 C HETATM 3254 C6 OLA A2028 -7.046 -7.791 -8.487 1.00 88.78 C HETATM 3255 C7 OLA A2028 -5.795 -7.107 -9.041 1.00 89.79 C HETATM 3256 C8 OLA A2028 -5.890 -5.584 -9.017 1.00 90.66 C HETATM 3257 C9 OLA A2028 -4.669 -4.968 -9.671 1.00 89.67 C HETATM 3258 C10 OLA A2028 -4.686 -3.724 -10.156 1.00 89.08 C HETATM 3259 C11 OLA A2028 -5.939 -2.887 -10.043 1.00 91.25 C HETATM 3260 C12 OLA A2028 -5.790 -1.534 -10.736 1.00 91.30 C HETATM 3261 C13 OLA A2028 -7.085 -1.193 -11.476 1.00 91.20 C HETATM 3262 C14 OLA A2028 -8.273 -1.118 -10.513 1.00 89.96 C HETATM 3263 C15 OLA A2028 -9.576 -1.683 -11.086 1.00 86.02 C HETATM 3264 C16 OLA A2028 -10.028 -2.965 -10.379 1.00 82.35 C HETATM 3265 C17 OLA A2028 -9.397 -3.142 -8.998 1.00 81.34 C HETATM 3266 C18 OLA A2028 -9.640 -4.532 -8.447 1.00 80.84 C HETATM 3267 C1 OLA A2029 -3.408 -13.936 -7.391 1.00105.44 C HETATM 3268 O1 OLA A2029 -3.899 -14.724 -8.228 1.00106.65 O HETATM 3269 O2 OLA A2029 -2.845 -14.319 -6.345 1.00106.79 O HETATM 3270 C2 OLA A2029 -3.491 -12.451 -7.640 1.00103.45 C HETATM 3271 C3 OLA A2029 -2.203 -11.979 -8.301 1.00102.08 C HETATM 3272 C4 OLA A2029 -1.941 -10.513 -7.982 1.00 99.22 C HETATM 3273 C5 OLA A2029 -1.786 -9.689 -9.251 1.00 96.27 C HETATM 3274 C6 OLA A2029 -1.791 -8.206 -8.915 1.00 95.90 C HETATM 3275 C7 OLA A2029 -2.310 -7.384 -10.088 1.00 94.28 C HETATM 3276 C8 OLA A2029 -1.246 -7.162 -11.154 1.00 91.58 C HETATM 3277 C9 OLA A2029 -1.887 -6.482 -12.340 1.00 91.48 C HETATM 3278 C12 1PE A2030 -12.838 -23.014 0.629 1.00102.66 C HETATM 3279 C22 1PE A2030 -13.470 -24.330 1.062 1.00105.41 C HETATM 3280 OH3 1PE A2030 -14.805 -24.103 1.520 1.00107.46 O HETATM 3281 C13 1PE A2030 -14.810 -26.497 1.921 1.00102.65 C HETATM 3282 C23 1PE A2030 -15.301 -25.130 2.384 1.00104.97 C HETATM 3283 OH4 1PE A2030 -15.793 -27.491 2.178 1.00102.70 O HETATM 3284 C14 1PE A2030 -14.661 -29.558 1.683 1.00108.40 C HETATM 3285 C24 1PE A2030 -15.199 -28.642 2.764 1.00104.20 C HETATM 3286 OH5 1PE A2030 -13.319 -29.883 2.022 1.00112.80 O HETATM 3287 C15 1PE A2030 -11.125 -30.467 1.257 1.00116.27 C HETATM 3288 C25 1PE A2030 -12.607 -30.437 0.922 1.00114.87 C HETATM 3289 OH6 1PE A2030 -10.392 -30.508 0.040 1.00117.27 O HETATM 3290 C16 1PE A2030 -9.431 -28.463 -0.715 1.00117.46 C HETATM 3291 C26 1PE A2030 -9.226 -29.702 0.143 1.00117.52 C HETATM 3292 OH7 1PE A2030 -8.664 -27.385 -0.170 1.00117.53 O HETATM 3293 O HOH A2101 -12.147 22.898 -23.332 1.00 39.30 O HETATM 3294 O HOH A2102 -16.987 -23.362 4.737 1.00 63.13 O HETATM 3295 O HOH A2103 -13.843 -15.954 -20.249 1.00 73.81 O HETATM 3296 O HOH A2104 -13.355 15.369 -22.731 1.00 38.07 O HETATM 3297 O HOH A2105 -19.861 -8.295 -13.303 1.00 65.84 O HETATM 3298 O HOH A2106 -30.124 -17.629 6.939 1.00 89.05 O HETATM 3299 O HOH A2107 -15.674 26.352 -15.507 1.00 70.82 O HETATM 3300 O HOH A2108 -36.471 13.155 -7.522 1.00101.91 O HETATM 3301 O HOH A2109 -15.754 16.703 -21.871 1.00 48.34 O HETATM 3302 O HOH A2110 -16.405 1.548 -20.525 1.00 50.72 O HETATM 3303 O HOH A2111 -16.957 -14.061 -14.661 1.00 47.00 O HETATM 3304 O HOH A2112 -14.259 19.672 -22.429 1.00 48.24 O HETATM 3305 O HOH A2113 -30.913 23.091 -23.652 1.00 68.55 O HETATM 3306 O HOH A2114 -19.452 23.337 -17.560 1.00 58.76 O HETATM 3307 O HOH A2115 -9.745 -16.682 -15.343 1.00 59.93 O HETATM 3308 O HOH A2116 -14.315 20.956 -37.270 1.00 80.07 O HETATM 3309 O HOH A2117 -16.670 14.886 -39.838 1.00 59.98 O HETATM 3310 O HOH A2118 -19.834 14.260 -18.729 1.00 59.23 O HETATM 3311 O HOH A2119 -12.806 -4.732 -21.962 1.00 47.84 O HETATM 3312 O HOH A2120 -2.487 -18.668 -12.734 1.00 82.97 O HETATM 3313 O HOH A2121 -15.370 9.950 -27.383 1.00 56.62 O HETATM 3314 O HOH A2122 -23.620 -23.771 -4.970 1.00 59.86 O HETATM 3315 O HOH A2123 -9.101 18.911 -33.279 1.00 55.15 O HETATM 3316 O HOH A2124 -12.296 -17.840 -22.720 1.00 54.41 O HETATM 3317 O HOH A2125 -17.631 22.423 -20.174 1.00 52.12 O HETATM 3318 O HOH A2126 -17.367 5.374 -22.562 1.00 37.66 O HETATM 3319 O HOH A2127 -6.508 -2.858 -21.144 1.00 59.81 O HETATM 3320 O HOH A2128 -20.352 -19.093 -10.949 1.00 63.45 O HETATM 3321 O HOH A2129 -15.899 8.264 -11.261 1.00 39.99 O HETATM 3322 O HOH A2130 -21.867 24.137 -12.342 1.00 75.92 O HETATM 3323 O HOH A2131 -19.071 21.963 -27.418 1.00 76.02 O HETATM 3324 O HOH A2132 -19.145 -21.536 5.335 1.00 74.66 O HETATM 3325 O HOH A2133 -17.158 4.140 -19.950 1.00 50.10 O HETATM 3326 O HOH A2134 -18.664 14.035 -25.402 1.00 69.26 O HETATM 3327 O HOH A2135 -17.026 13.120 -42.330 1.00 84.29 O CONECT 16 2466 CONECT 664 1223 CONECT 1223 664 CONECT 2466 16 CONECT 2800 2802 2811 CONECT 2801 2810 2815 2830 CONECT 2802 2800 2803 CONECT 2803 2802 2805 CONECT 2804 2808 2809 CONECT 2805 2803 2835 2836 CONECT 2806 2807 2811 2831 CONECT 2807 2806 2808 CONECT 2808 2804 2807 CONECT 2809 2804 2812 2831 CONECT 2810 2801 2812 2837 CONECT 2811 2800 2806 2813 CONECT 2812 2809 2810 CONECT 2813 2811 2814 CONECT 2814 2813 2820 2839 CONECT 2815 2801 2816 CONECT 2816 2815 2817 CONECT 2817 2816 2829 2838 CONECT 2818 2819 2838 CONECT 2819 2818 2821 CONECT 2820 2814 2833 2834 CONECT 2821 2819 2822 CONECT 2822 2821 2823 CONECT 2823 2822 2824 2828 CONECT 2824 2823 2825 CONECT 2825 2824 2826 2832 CONECT 2826 2825 2827 CONECT 2827 2826 2828 CONECT 2828 2823 2827 2840 CONECT 2829 2817 2830 CONECT 2830 2801 2829 CONECT 2831 2806 2809 2839 CONECT 2832 2825 CONECT 2833 2820 CONECT 2834 2820 CONECT 2835 2805 CONECT 2836 2805 CONECT 2837 2810 CONECT 2838 2817 2818 CONECT 2839 2814 2831 CONECT 2840 2828 CONECT 2841 2842 2850 CONECT 2842 2841 2843 CONECT 2843 2842 2844 2868 CONECT 2844 2843 2845 CONECT 2845 2844 2846 2850 CONECT 2846 2845 2847 CONECT 2847 2846 2848 CONECT 2848 2847 2849 2854 CONECT 2849 2848 2850 2851 CONECT 2850 2841 2845 2849 2859 CONECT 2851 2849 2852 CONECT 2852 2851 2853 CONECT 2853 2852 2854 2857 2858 CONECT 2854 2848 2853 2855 CONECT 2855 2854 2856 CONECT 2856 2855 2857 CONECT 2857 2853 2856 2860 CONECT 2858 2853 CONECT 2859 2850 CONECT 2860 2857 2861 2862 CONECT 2861 2860 CONECT 2862 2860 2863 CONECT 2863 2862 2864 CONECT 2864 2863 2865 CONECT 2865 2864 2866 2867 CONECT 2866 2865 CONECT 2867 2865 CONECT 2868 2843 CONECT 2869 2871 CONECT 2870 2871 CONECT 2871 2869 2870 2872 CONECT 2872 2871 2873 2874 CONECT 2873 2872 CONECT 2874 2872 2875 2876 CONECT 2875 2874 CONECT 2876 2874 2877 2878 CONECT 2877 2876 CONECT 2878 2876 CONECT 2879 2880 2881 CONECT 2880 2879 2882 CONECT 2881 2879 2884 CONECT 2882 2880 2885 CONECT 2883 2895 2897 CONECT 2884 2881 2886 CONECT 2885 2882 2887 CONECT 2886 2884 2888 CONECT 2887 2885 2889 CONECT 2888 2886 CONECT 2889 2887 2890 CONECT 2890 2889 2891 CONECT 2891 2890 2892 CONECT 2892 2891 2894 CONECT 2893 2895 2899 CONECT 2894 2892 2896 2899 CONECT 2895 2883 2893 2898 CONECT 2896 2894 CONECT 2897 2883 CONECT 2898 2895 CONECT 2899 2893 2894 CONECT 2900 2901 2902 CONECT 2901 2900 2903 CONECT 2902 2900 2905 CONECT 2903 2901 2906 CONECT 2904 2916 2918 CONECT 2905 2902 2907 CONECT 2906 2903 2908 CONECT 2907 2905 2909 CONECT 2908 2906 2910 CONECT 2909 2907 CONECT 2910 2908 2911 CONECT 2911 2910 2912 CONECT 2912 2911 2913 CONECT 2913 2912 2915 CONECT 2914 2916 2920 CONECT 2915 2913 2917 2920 CONECT 2916 2904 2914 2919 CONECT 2917 2915 CONECT 2918 2904 CONECT 2919 2916 CONECT 2920 2914 2915 CONECT 2921 2922 CONECT 2922 2921 2923 CONECT 2923 2922 2925 CONECT 2924 2933 2935 CONECT 2925 2923 2926 CONECT 2926 2925 2927 CONECT 2927 2926 2928 CONECT 2928 2927 2929 CONECT 2929 2928 2930 CONECT 2930 2929 2932 CONECT 2931 2933 2937 CONECT 2932 2930 2934 2937 CONECT 2933 2924 2931 2936 CONECT 2934 2932 CONECT 2935 2924 CONECT 2936 2933 CONECT 2937 2931 2932 CONECT 2938 2939 2940 CONECT 2939 2938 2941 CONECT 2940 2938 2942 CONECT 2941 2939 2943 CONECT 2942 2940 2944 CONECT 2943 2941 CONECT 2944 2942 2945 CONECT 2945 2944 CONECT 2946 2947 2948 CONECT 2947 2946 2949 CONECT 2948 2946 2950 CONECT 2949 2947 CONECT 2950 2948 2952 CONECT 2951 2953 CONECT 2952 2950 2953 CONECT 2953 2951 2952 CONECT 2954 2957 CONECT 2955 2956 2958 CONECT 2956 2955 2959 CONECT 2957 2954 2961 CONECT 2958 2955 2962 CONECT 2959 2956 2963 CONECT 2960 2974 2976 CONECT 2961 2957 2964 CONECT 2962 2958 2965 CONECT 2963 2959 2966 CONECT 2964 2961 2967 CONECT 2965 2962 2967 CONECT 2966 2963 2968 CONECT 2967 2964 2965 CONECT 2968 2966 2969 CONECT 2969 2968 2970 CONECT 2970 2969 2971 CONECT 2971 2970 2973 CONECT 2972 2974 2978 CONECT 2973 2971 2975 2978 CONECT 2974 2960 2972 2977 CONECT 2975 2973 CONECT 2976 2960 CONECT 2977 2974 CONECT 2978 2972 2973 CONECT 2979 2980 CONECT 2980 2979 2981 CONECT 2981 2980 2982 CONECT 2982 2981 2983 CONECT 2983 2982 2984 CONECT 2984 2983 2985 CONECT 2985 2984 2986 CONECT 2986 2985 CONECT 2987 2988 2989 CONECT 2988 2987 2990 CONECT 2989 2987 2991 CONECT 2990 2988 2992 CONECT 2991 2989 2994 CONECT 2992 2990 2995 CONECT 2993 2996 CONECT 2994 2991 2996 CONECT 2995 2992 2997 CONECT 2996 2993 2994 CONECT 2997 2995 2998 CONECT 2998 2997 CONECT 2999 3000 3001 CONECT 3000 2999 3002 CONECT 3001 2999 3003 CONECT 3002 3000 3004 CONECT 3003 3001 3006 CONECT 3004 3002 3007 CONECT 3005 3008 CONECT 3006 3003 3008 CONECT 3007 3004 3009 CONECT 3008 3005 3006 CONECT 3009 3007 CONECT 3010 3011 CONECT 3011 3010 3012 CONECT 3012 3011 3014 CONECT 3013 3022 3024 CONECT 3014 3012 3015 CONECT 3015 3014 3016 CONECT 3016 3015 3017 CONECT 3017 3016 3018 CONECT 3018 3017 3019 CONECT 3019 3018 3021 CONECT 3020 3022 3026 CONECT 3021 3019 3023 3026 CONECT 3022 3013 3020 3025 CONECT 3023 3021 CONECT 3024 3013 CONECT 3025 3022 CONECT 3026 3020 3021 CONECT 3027 3030 CONECT 3028 3029 3031 CONECT 3029 3028 3032 CONECT 3030 3027 3033 CONECT 3031 3028 3034 CONECT 3032 3029 3035 CONECT 3033 3030 3036 CONECT 3034 3031 3037 CONECT 3035 3032 CONECT 3036 3033 3038 CONECT 3037 3034 3038 CONECT 3038 3036 3037 CONECT 3039 3042 CONECT 3040 3041 3043 CONECT 3041 3040 3044 CONECT 3042 3039 3045 CONECT 3043 3040 3046 CONECT 3044 3041 CONECT 3045 3042 3047 CONECT 3046 3043 3048 CONECT 3047 3045 3049 CONECT 3048 3046 3049 CONECT 3049 3047 3048 CONECT 3050 3051 CONECT 3051 3050 3053 CONECT 3052 3061 3063 CONECT 3053 3051 3054 CONECT 3054 3053 3055 CONECT 3055 3054 3056 CONECT 3056 3055 3057 CONECT 3057 3056 3058 CONECT 3058 3057 3060 CONECT 3059 3061 3065 CONECT 3060 3058 3062 3065 CONECT 3061 3052 3059 3064 CONECT 3062 3060 CONECT 3063 3052 CONECT 3064 3061 CONECT 3065 3059 3060 CONECT 3066 3067 CONECT 3067 3066 3069 CONECT 3068 3077 3079 CONECT 3069 3067 3070 CONECT 3070 3069 3071 CONECT 3071 3070 3072 CONECT 3072 3071 3073 CONECT 3073 3072 3074 CONECT 3074 3073 3076 CONECT 3075 3077 3081 CONECT 3076 3074 3078 3081 CONECT 3077 3068 3075 3080 CONECT 3078 3076 CONECT 3079 3068 CONECT 3080 3077 CONECT 3081 3075 3076 CONECT 3082 3083 3084 CONECT 3083 3082 3085 CONECT 3084 3082 3086 CONECT 3085 3083 3087 CONECT 3086 3084 3089 CONECT 3087 3085 3090 CONECT 3088 3091 CONECT 3089 3086 3091 CONECT 3090 3087 3092 CONECT 3091 3088 3089 CONECT 3092 3090 3093 CONECT 3093 3092 3094 CONECT 3094 3093 3095 CONECT 3095 3094 CONECT 3096 3099 CONECT 3097 3098 3100 CONECT 3098 3097 3101 CONECT 3099 3096 3102 CONECT 3100 3097 3103 CONECT 3101 3098 3104 CONECT 3102 3099 3105 CONECT 3103 3100 3106 CONECT 3104 3101 3107 CONECT 3105 3102 3108 CONECT 3106 3103 3108 CONECT 3107 3104 3109 CONECT 3108 3105 3106 CONECT 3109 3107 3110 CONECT 3110 3109 3111 CONECT 3111 3110 3112 CONECT 3112 3111 CONECT 3113 3114 3115 3116 CONECT 3114 3113 CONECT 3115 3113 CONECT 3116 3113 3117 CONECT 3117 3116 3118 CONECT 3118 3117 3119 CONECT 3119 3118 3120 CONECT 3120 3119 3121 CONECT 3121 3120 3122 CONECT 3122 3121 3123 CONECT 3123 3122 3124 CONECT 3124 3123 3125 CONECT 3125 3124 3126 CONECT 3126 3125 3127 CONECT 3127 3126 3128 CONECT 3128 3127 CONECT 3129 3130 3131 3132 CONECT 3130 3129 CONECT 3131 3129 CONECT 3132 3129 3133 CONECT 3133 3132 3134 CONECT 3134 3133 3135 CONECT 3135 3134 3136 CONECT 3136 3135 3137 CONECT 3137 3136 3138 CONECT 3138 3137 3139 CONECT 3139 3138 3140 CONECT 3140 3139 3141 CONECT 3141 3140 3142 CONECT 3142 3141 3143 CONECT 3143 3142 3144 CONECT 3144 3143 3145 CONECT 3145 3144 CONECT 3146 3147 3148 3149 CONECT 3147 3146 CONECT 3148 3146 CONECT 3149 3146 3150 CONECT 3150 3149 3151 CONECT 3151 3150 3152 CONECT 3152 3151 3153 CONECT 3153 3152 3154 CONECT 3154 3153 3155 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3156 CONECT 3158 3159 3160 3161 CONECT 3159 3158 CONECT 3160 3158 CONECT 3161 3158 3162 CONECT 3162 3161 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 CONECT 3165 3164 3166 CONECT 3166 3165 3167 CONECT 3167 3166 3168 CONECT 3168 3167 3169 CONECT 3169 3168 3170 CONECT 3170 3169 3171 CONECT 3171 3170 3172 CONECT 3172 3171 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 3177 CONECT 3177 3176 CONECT 3178 3179 3180 3181 CONECT 3179 3178 CONECT 3180 3178 CONECT 3181 3178 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 3190 CONECT 3190 3189 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 CONECT 3193 3192 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 CONECT 3198 3199 3200 3201 CONECT 3199 3198 CONECT 3200 3198 CONECT 3201 3198 3202 CONECT 3202 3201 3203 CONECT 3203 3202 3204 CONECT 3204 3203 3205 CONECT 3205 3204 3206 CONECT 3206 3205 3207 CONECT 3207 3206 CONECT 3208 3209 3210 3211 CONECT 3209 3208 CONECT 3210 3208 CONECT 3211 3208 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 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3223 3225 CONECT 3225 3224 3226 CONECT 3226 3225 CONECT 3227 3228 3229 3230 CONECT 3228 3227 CONECT 3229 3227 CONECT 3230 3227 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 CONECT 3236 3235 3237 CONECT 3237 3236 3238 CONECT 3238 3237 3239 CONECT 3239 3238 3240 CONECT 3240 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 CONECT 3243 3242 3244 CONECT 3244 3243 3245 CONECT 3245 3244 3246 CONECT 3246 3245 CONECT 3247 3248 3249 3250 CONECT 3248 3247 CONECT 3249 3247 CONECT 3250 3247 3251 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 3265 CONECT 3265 3264 3266 CONECT 3266 3265 CONECT 3267 3268 3269 3270 CONECT 3268 3267 CONECT 3269 3267 CONECT 3270 3267 3271 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 3276 CONECT 3276 3275 3277 CONECT 3277 3276 CONECT 3278 3279 CONECT 3279 3278 3280 CONECT 3280 3279 3282 CONECT 3281 3282 3283 CONECT 3282 3280 3281 CONECT 3283 3281 3285 CONECT 3284 3285 3286 CONECT 3285 3283 3284 CONECT 3286 3284 3288 CONECT 3287 3288 3289 CONECT 3288 3286 3287 CONECT 3289 3287 3291 CONECT 3290 3291 3292 CONECT 3291 3289 3290 CONECT 3292 3290 MASTER 520 0 30 16 0 0 43 6 3298 1 497 32 END