HEADER MEMBRANE PROTEIN 12-JUN-19 6RZ8 TITLE CRYSTAL STRUCTURE OF THE HUMAN CYSTEINYL LEUKOTRIENE RECEPTOR 2 IN TITLE 2 COMPLEX WITH ONO-2080365 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; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9 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 6RZ8 1 COMPND HETNAM REVDAT 2 18-DEC-19 6RZ8 1 JRNL REVDAT 1 11-DEC-19 6RZ8 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. 2.70 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) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.92 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 14226 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 : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 711 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 29.9260 - 4.6126 1.00 2712 152 0.1898 0.2143 REMARK 3 2 4.6126 - 3.6633 1.00 2724 140 0.1580 0.2329 REMARK 3 3 3.6633 - 3.2008 1.00 2687 147 0.2038 0.2496 REMARK 3 4 3.2008 - 2.9084 1.00 2706 135 0.2444 0.3387 REMARK 3 5 2.9084 - 2.7001 1.00 2688 137 0.2694 0.3450 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) : 0.390 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.040 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 3032 REMARK 3 ANGLE : 0.748 4078 REMARK 3 CHIRALITY : 0.048 482 REMARK 3 PLANARITY : 0.005 494 REMARK 3 DIHEDRAL : 11.593 1799 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 31 THROUGH 232) REMARK 3 ORIGIN FOR THE GROUP (A): 109.9799 64.5101 -6.7670 REMARK 3 T TENSOR REMARK 3 T11: 0.3851 T22: 0.2620 REMARK 3 T33: 0.4058 T12: 0.0283 REMARK 3 T13: 0.0266 T23: 0.0269 REMARK 3 L TENSOR REMARK 3 L11: 2.3757 L22: 2.1918 REMARK 3 L33: 2.1460 L12: 0.1641 REMARK 3 L13: -0.0575 L23: 1.1548 REMARK 3 S TENSOR REMARK 3 S11: -0.0145 S12: -0.0551 S13: 0.1332 REMARK 3 S21: 0.0673 S22: -0.0777 S23: 0.2397 REMARK 3 S31: -0.1369 S32: -0.0828 S33: 0.0307 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1001 THROUGH 1106) REMARK 3 ORIGIN FOR THE GROUP (A): 130.5640 53.2487 39.5294 REMARK 3 T TENSOR REMARK 3 T11: 1.0896 T22: 0.8718 REMARK 3 T33: 0.5252 T12: 0.0152 REMARK 3 T13: -0.1107 T23: 0.0568 REMARK 3 L TENSOR REMARK 3 L11: 7.5364 L22: 7.9508 REMARK 3 L33: 3.6519 L12: -1.6287 REMARK 3 L13: -0.0545 L23: 2.9554 REMARK 3 S TENSOR REMARK 3 S11: 0.4915 S12: 0.0041 S13: 0.0511 REMARK 3 S21: -0.4216 S22: -0.2195 S23: 0.0136 REMARK 3 S31: 1.6273 S32: -1.0023 S33: -0.2803 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 240 THROUGH 313) REMARK 3 ORIGIN FOR THE GROUP (A): 118.4617 58.1606 -6.7567 REMARK 3 T TENSOR REMARK 3 T11: 0.3073 T22: 0.3360 REMARK 3 T33: 0.4799 T12: -0.0303 REMARK 3 T13: -0.0533 T23: 0.0188 REMARK 3 L TENSOR REMARK 3 L11: 4.5140 L22: 3.6889 REMARK 3 L33: 4.6212 L12: 0.3309 REMARK 3 L13: -0.7012 L23: 0.6252 REMARK 3 S TENSOR REMARK 3 S11: 0.2431 S12: -0.4049 S13: -0.0665 REMARK 3 S21: 0.2641 S22: -0.1614 S23: 0.1132 REMARK 3 S31: 0.0751 S32: 0.4488 S33: -0.0482 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 6RZ8 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_1200011361. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JUN-17 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID23-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.976250 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 20161205 REMARK 200 DATA SCALING SOFTWARE : XSCALE 20180319 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14227 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700 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 (%) : 100.0 REMARK 200 DATA REDUNDANCY : 14.00 REMARK 200 R MERGE (I) : 0.23900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 13.80 REMARK 200 R MERGE FOR SHELL (I) : 2.75800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.200 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 1.12-2829 REMARK 200 STARTING MODEL: 6RZ4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM K FORMATE 30% V/V PEG400 100 MM REMARK 280 TRIS-HCL PH 8.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2 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 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 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 39.22000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.22000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 86.01500 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.22000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.22000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 86.01500 REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 39.22000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 39.22000 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 86.01500 REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 39.22000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 39.22000 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 86.01500 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: 990 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 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 ARG A 29 REMARK 465 ASN A 30 REMARK 465 PRO A 143 REMARK 465 PHE A 144 REMARK 465 ARG A 145 REMARK 465 LEU A 146 REMARK 465 LEU A 147 REMARK 465 HIS A 148 REMARK 465 VAL A 149 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 ASP A 314 REMARK 465 ARG A 315 REMARK 465 LEU A 316 REMARK 465 LYS A 317 REMARK 465 SER A 318 REMARK 465 ALA A 319 REMARK 465 LEU A 320 REMARK 465 ARG A 321 REMARK 465 LYS A 322 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 LYS A 68 CG CD CE NZ REMARK 470 LYS A 69 CG CD CE NZ REMARK 470 HIS A 142 CG ND1 CD2 CE1 NE2 REMARK 470 THR A 150 OG1 CG2 REMARK 470 GLU A 179 CG CD OE1 OE2 REMARK 470 TYR A 193 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A 230 CE NZ REMARK 470 GLU A1004 CD OE1 OE2 REMARK 470 LYS A1015 CE NZ REMARK 470 GLN A1025 CG CD OE1 NE2 REMARK 470 LYS A1042 CG CD CE NZ REMARK 470 THR A1044 OG1 CG2 REMARK 470 SER A1055 OG REMARK 470 GLU A1057 CG CD OE1 OE2 REMARK 470 MET A1058 CG SD CE REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 PHE A1061 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ARG A1062 CG CD NE CZ NH1 NH2 REMARK 470 PHE A1065 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A1077 CG CD CE NZ REMARK 470 LYS A1085 CG CD CE NZ REMARK 470 GLU A1092 CG CD OE1 OE2 REMARK 470 LEU A1094 CG CD1 CD2 REMARK 470 LYS A1095 CG CD CE NZ REMARK 470 THR A1096 OG1 CG2 REMARK 470 ARG A1098 CG CD NE CZ NH1 NH2 REMARK 470 TYR A1101 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 GLN A1103 CG CD OE1 NE2 REMARK 470 LEU A1106 CG CD1 CD2 REMARK 470 ARG A 243 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 244 CG CD CE NZ REMARK 470 LYS A 275 CG CD CE NZ REMARK 470 VAL A 276 CG1 CG2 REMARK 470 LEU A 278 CG CD1 CD2 REMARK 470 LYS A 280 CG CD CE NZ REMARK 470 GLU A 310 CG CD OE1 OE2 REMARK 470 ASN A 311 CG OD1 ND2 REMARK 470 PHE A 312 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 313 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 LYS A 197 -71.33 -56.18 REMARK 500 CYS A 210 -63.50 -128.18 REMARK 500 ALA A1043 33.16 -88.48 REMARK 500 LYS A 280 67.92 -105.22 REMARK 500 TYR A 306 -71.44 -54.21 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 2003 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 2009 REMARK 610 OLC A 2010 REMARK 610 OLC A 2011 REMARK 610 OLA A 2012 REMARK 610 OLA A 2013 REMARK 610 OLA A 2014 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue KNZ A 2001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC 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 2009 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2010 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2011 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2012 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2013 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2014 DBREF 6RZ8 A 17 232 UNP Q9NS75 CLTR2_HUMAN 17 232 DBREF 6RZ8 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 6RZ8 A 240 322 UNP Q9NS75 CLTR2_HUMAN 240 322 SEQADV 6RZ8 VAL A 51 UNP Q9NS75 TRP 51 ENGINEERED MUTATION SEQADV 6RZ8 ASN A 84 UNP Q9NS75 ASP 84 ENGINEERED MUTATION SEQADV 6RZ8 TYR A 137 UNP Q9NS75 PHE 137 ENGINEERED MUTATION SEQADV 6RZ8 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 6RZ8 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 6RZ8 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 KNZ A2001 43 HET OLC A2002 25 HET OLC A2003 22 HET OLC A2004 21 HET OLC A2005 14 HET OLC A2006 13 HET OLC A2007 9 HET OLC A2008 5 HET OLC A2009 15 HET OLC A2010 4 HET OLC A2011 21 HET OLA A2012 14 HET OLA A2013 9 HET OLA A2014 7 HETNAM KNZ (2~{S})-8-[[4-[4-[2,3-BIS(FLUORANYL)PHENOXY]BUTOXY]-2- HETNAM 2 KNZ FLUORANYL-PHENYL]CARBONYLAMINO]-4-(4-OXIDANYL-4- HETNAM 3 KNZ OXIDANYLIDENE-BUT YL)-2,3-DIHYDRO-1,4-BENZOXAZINE-2- HETNAM 4 KNZ CARBOXYLIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN KNZ ONO-2080365 HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 KNZ C30 H29 F3 N2 O8 FORMUL 3 OLC 10(C21 H40 O4) FORMUL 13 OLA 3(C18 H34 O2) FORMUL 16 HOH *17(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 SER A 151 SER A 170 1 20 HELIX 6 AA6 ILE A 171 SER A 176 5 6 HELIX 7 AA7 ASN A 191 CYS A 210 1 20 HELIX 8 AA8 CYS A 210 LYS A 1019 1 42 HELIX 9 AA9 ASN A 1022 ALA A 1043 1 22 HELIX 10 AB1 PRO A 1056 GLU A 1081 1 26 HELIX 11 AB2 LYS A 1083 TRP A 274 1 59 HELIX 12 AB3 LYS A 280 ALA A 296 1 17 HELIX 13 AB4 ALA A 296 ASN A 301 1 6 HELIX 14 AB5 ASN A 301 GLU A 310 1 10 SHEET 1 AA1 2 GLU A 179 ASN A 181 0 SHEET 2 AA1 2 VAL A 184 SER A 186 -1 O SER A 186 N GLU A 179 SSBOND 1 CYS A 31 CYS A 279 1555 1555 2.04 SSBOND 2 CYS A 111 CYS A 187 1555 1555 2.03 SITE 1 AC1 19 LYS A 37 TYR A 119 TYR A 127 ILE A 166 SITE 2 AC1 19 SER A 169 SER A 170 LEU A 188 LEU A 190 SITE 3 AC1 19 LYS A 194 LEU A 198 MET A 201 GLY A 209 SITE 4 AC1 19 ARG A 267 LEU A 271 HIS A 284 HOH A2108 SITE 5 AC1 19 HOH A2111 HOH A2112 HOH A2113 SITE 1 AC2 7 SER A 83 SER A 89 PHE A 93 PHE A 106 SITE 2 AC2 7 GLU A1081 OLC A2006 OLA A2013 SITE 1 AC3 10 ARG A 38 GLU A 39 PRO A 42 ILE A 43 SITE 2 AC3 10 ILE A 47 ARG A 282 ALA A 286 ILE A 289 SITE 3 AC3 10 LEU A 293 OLC A2011 SITE 1 AC4 13 LEU A 46 PHE A 49 PRO A 92 ASP A 96 SITE 2 AC4 13 LEU A 99 ARG A 100 THR A 265 VAL A 269 SITE 3 AC4 13 CYS A 279 LEU A 283 OLC A2010 OLA A2012 SITE 4 AC4 13 HOH A2101 SITE 1 AC5 2 PHE A 36 OLA A2014 SITE 1 AC6 2 LEU A 86 OLC A2002 SITE 1 AC7 1 THR A 272 SITE 1 AC8 4 CYS A 299 PHE A 300 LEU A 303 OLC A2011 SITE 1 AC9 2 VAL A 53 OLC A2004 SITE 1 AD1 8 LEU A 58 SER A 59 VAL A 62 PHE A 63 SITE 2 AD1 8 PRO A 302 TYR A 305 OLC A2003 OLC A2009 SITE 1 AD2 2 ASP A 96 OLC A2004 SITE 1 AD3 3 ILE A 105 GLU A1081 OLC A2002 SITE 1 AD4 2 LYS A 285 OLC A2005 CRYST1 78.440 78.440 172.030 90.00 90.00 90.00 I 4 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 0.012749 0.000000 0.000000 0.00000 SCALE2 0.000000 0.012749 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005813 0.00000 ATOM 1 N CYS A 31 115.239 56.115 -32.096 1.00148.48 N ANISOU 1 N CYS A 31 19299 19954 17163 -223 153 -600 N ATOM 2 CA CYS A 31 116.004 55.235 -32.964 1.00139.21 C ANISOU 2 CA CYS A 31 18072 18935 15888 -282 265 -809 C ATOM 3 C CYS A 31 115.518 53.816 -32.675 1.00131.56 C ANISOU 3 C CYS A 31 16951 17909 15129 -220 224 -1036 C ATOM 4 O CYS A 31 114.390 53.448 -33.014 1.00131.16 O ANISOU 4 O CYS A 31 16887 17884 15063 -176 90 -1102 O ATOM 5 CB CYS A 31 117.502 55.378 -32.684 1.00139.18 C ANISOU 5 CB CYS A 31 18035 18931 15918 -357 456 -815 C ATOM 6 SG CYS A 31 118.053 57.121 -32.560 1.00138.60 S ANISOU 6 SG CYS A 31 18125 18833 15704 -441 515 -523 S ATOM 7 N THR A 32 116.379 53.024 -32.040 1.00125.18 N ANISOU 7 N THR A 32 16026 17015 14523 -216 337 -1156 N ATOM 8 CA THR A 32 115.961 51.813 -31.352 1.00112.65 C ANISOU 8 CA THR A 32 14314 15285 13203 -150 302 -1305 C ATOM 9 C THR A 32 115.979 51.996 -29.842 1.00 93.90 C ANISOU 9 C THR A 32 11910 12694 11075 -100 295 -1169 C ATOM 10 O THR A 32 115.575 51.086 -29.110 1.00 96.34 O ANISOU 10 O THR A 32 12140 12856 11608 -49 267 -1246 O ATOM 11 CB THR A 32 116.847 50.631 -31.753 1.00112.01 C ANISOU 11 CB THR A 32 14129 15247 13183 -160 416 -1557 C ATOM 12 OG1 THR A 32 118.192 50.874 -31.325 1.00 97.55 O ANISOU 12 OG1 THR A 32 12265 13401 11401 -177 548 -1527 O ATOM 13 CG2 THR A 32 116.812 50.434 -33.270 1.00119.09 C ANISOU 13 CG2 THR A 32 15057 16378 13814 -216 431 -1714 C ATOM 14 N ILE A 33 116.452 53.151 -29.364 1.00 56.49 N ANISOU 14 N ILE A 33 7240 7932 6292 -121 325 -969 N ATOM 15 CA ILE A 33 116.235 53.561 -27.980 1.00 46.53 C ANISOU 15 CA ILE A 33 5976 6489 5215 -75 291 -820 C ATOM 16 C ILE A 33 114.753 53.563 -27.642 1.00 51.63 C ANISOU 16 C ILE A 33 6631 7056 5930 -26 157 -773 C ATOM 17 O ILE A 33 114.364 53.326 -26.490 1.00 44.96 O ANISOU 17 O ILE A 33 5745 6053 5283 17 134 -733 O ATOM 18 CB ILE A 33 116.880 54.946 -27.740 1.00 50.62 C ANISOU 18 CB ILE A 33 6580 7015 5637 -122 336 -627 C ATOM 19 CG1 ILE A 33 116.687 55.402 -26.291 1.00 44.04 C ANISOU 19 CG1 ILE A 33 5742 6006 4984 -77 302 -490 C ATOM 20 CG2 ILE A 33 116.346 55.979 -28.730 1.00 52.94 C ANISOU 20 CG2 ILE A 33 7008 7423 5683 -161 280 -508 C ATOM 21 CD1 ILE A 33 117.342 54.508 -25.273 1.00 51.37 C ANISOU 21 CD1 ILE A 33 6567 6826 6127 -35 352 -572 C ATOM 22 N GLU A 34 113.901 53.809 -28.639 1.00 39.34 N ANISOU 22 N GLU A 34 5122 5618 4206 -32 66 -787 N ATOM 23 CA GLU A 34 112.470 53.906 -28.388 1.00 50.92 C ANISOU 23 CA GLU A 34 6578 7035 5736 18 -70 -756 C ATOM 24 C GLU A 34 111.871 52.544 -28.063 1.00 48.01 C ANISOU 24 C GLU A 34 6089 6586 5565 35 -83 -938 C ATOM 25 O GLU A 34 110.991 52.439 -27.202 1.00 52.31 O ANISOU 25 O GLU A 34 6590 7010 6277 65 -132 -907 O ATOM 26 CB GLU A 34 111.780 54.534 -29.596 1.00 41.05 C ANISOU 26 CB GLU A 34 5406 5947 4244 20 -182 -728 C ATOM 27 CG GLU A 34 112.277 55.940 -29.892 1.00 67.51 C ANISOU 27 CG GLU A 34 8903 9343 7403 -1 -172 -519 C ATOM 28 CD GLU A 34 111.990 56.914 -28.759 1.00 96.26 C ANISOU 28 CD GLU A 34 12578 12825 11172 41 -201 -330 C ATOM 29 OE1 GLU A 34 110.956 56.754 -28.074 1.00106.35 O ANISOU 29 OE1 GLU A 34 13786 14011 12610 103 -287 -340 O ATOM 30 OE2 GLU A 34 112.807 57.835 -28.543 1.00100.11 O ANISOU 30 OE2 GLU A 34 13153 13280 11604 3 -129 -184 O ATOM 31 N ASN A 35 112.336 51.490 -28.734 1.00 52.02 N ANISOU 31 N ASN A 35 6546 7155 6066 8 -28 -1135 N ATOM 32 CA ASN A 35 111.878 50.146 -28.400 1.00 44.24 C ANISOU 32 CA ASN A 35 5458 6059 5291 14 -24 -1311 C ATOM 33 C ASN A 35 112.236 49.795 -26.960 1.00 47.77 C ANISOU 33 C ASN A 35 5879 6292 5977 40 42 -1238 C ATOM 34 O ASN A 35 111.409 49.252 -26.210 1.00 67.63 O ANISOU 34 O ASN A 35 8351 8671 8676 47 18 -1254 O ATOM 35 CB ASN A 35 112.485 49.135 -29.371 1.00 48.91 C ANISOU 35 CB ASN A 35 6007 6742 5835 -14 35 -1542 C ATOM 36 CG ASN A 35 111.967 49.303 -30.789 1.00 77.47 C ANISOU 36 CG ASN A 35 9648 10579 9208 -42 -44 -1643 C ATOM 37 OD1 ASN A 35 110.778 49.550 -31.006 1.00 80.47 O ANISOU 37 OD1 ASN A 35 10023 11001 9553 -32 -171 -1634 O ATOM 38 ND2 ASN A 35 112.861 49.155 -31.766 1.00 91.17 N ANISOU 38 ND2 ASN A 35 11403 12467 10769 -76 30 -1752 N ATOM 39 N PHE A 36 113.466 50.117 -26.550 1.00 44.86 N ANISOU 39 N PHE A 36 5539 5902 5604 50 128 -1158 N ATOM 40 CA PHE A 36 113.867 49.874 -25.169 1.00 38.85 C ANISOU 40 CA PHE A 36 4765 4958 5040 85 172 -1075 C ATOM 41 C PHE A 36 113.015 50.677 -24.199 1.00 47.19 C ANISOU 41 C PHE A 36 5857 5931 6142 97 118 -899 C ATOM 42 O PHE A 36 112.622 50.173 -23.145 1.00 39.07 O ANISOU 42 O PHE A 36 4810 4746 5289 113 126 -873 O ATOM 43 CB PHE A 36 115.341 50.211 -24.956 1.00 41.31 C ANISOU 43 CB PHE A 36 5084 5291 5321 96 255 -1030 C ATOM 44 CG PHE A 36 115.774 50.087 -23.520 1.00 47.05 C ANISOU 44 CG PHE A 36 5806 5851 6220 143 277 -931 C ATOM 45 CD1 PHE A 36 116.057 48.846 -22.970 1.00 46.77 C ANISOU 45 CD1 PHE A 36 5726 5672 6371 190 301 -1022 C ATOM 46 CD2 PHE A 36 115.847 51.210 -22.705 1.00 38.35 C ANISOU 46 CD2 PHE A 36 4754 4727 5089 143 264 -747 C ATOM 47 CE1 PHE A 36 116.438 48.730 -21.644 1.00 53.62 C ANISOU 47 CE1 PHE A 36 6607 6393 7372 241 305 -918 C ATOM 48 CE2 PHE A 36 116.223 51.098 -21.379 1.00 44.64 C ANISOU 48 CE2 PHE A 36 5552 5388 6020 186 275 -663 C ATOM 49 CZ PHE A 36 116.520 49.856 -20.849 1.00 47.38 C ANISOU 49 CZ PHE A 36 5863 5609 6532 237 291 -742 C ATOM 50 N LYS A 37 112.756 51.945 -24.518 1.00 41.76 N ANISOU 50 N LYS A 37 5229 5340 5299 89 70 -775 N ATOM 51 CA LYS A 37 111.921 52.766 -23.648 1.00 51.42 C ANISOU 51 CA LYS A 37 6477 6489 6571 110 17 -628 C ATOM 52 C LYS A 37 110.526 52.175 -23.509 1.00 40.89 C ANISOU 52 C LYS A 37 5080 5108 5347 112 -44 -706 C ATOM 53 O LYS A 37 109.986 52.096 -22.401 1.00 48.51 O ANISOU 53 O LYS A 37 6026 5949 6457 120 -33 -652 O ATOM 54 CB LYS A 37 111.848 54.192 -24.191 1.00 62.18 C ANISOU 54 CB LYS A 37 7922 7954 7750 110 -35 -497 C ATOM 55 CG LYS A 37 113.116 54.997 -23.997 1.00 49.33 C ANISOU 55 CG LYS A 37 6357 6337 6049 88 39 -388 C ATOM 56 CD LYS A 37 113.081 56.248 -24.848 1.00 48.11 C ANISOU 56 CD LYS A 37 6303 6285 5692 70 -3 -278 C ATOM 57 CE LYS A 37 111.982 57.185 -24.385 1.00 51.18 C ANISOU 57 CE LYS A 37 6729 6610 6107 118 -101 -155 C ATOM 58 NZ LYS A 37 112.016 58.475 -25.125 1.00 40.89 N ANISOU 58 NZ LYS A 37 5548 5369 4619 110 -146 -19 N ATOM 59 N ARG A 38 109.943 51.722 -24.621 1.00 42.79 N ANISOU 59 N ARG A 38 5282 5455 5520 96 -103 -846 N ATOM 60 CA ARG A 38 108.581 51.203 -24.590 1.00 40.18 C ANISOU 60 CA ARG A 38 4870 5101 5296 86 -167 -944 C ATOM 61 C ARG A 38 108.503 49.849 -23.897 1.00 53.04 C ANISOU 61 C ARG A 38 6439 6573 7142 52 -90 -1052 C ATOM 62 O ARG A 38 107.428 49.471 -23.418 1.00 41.88 O ANISOU 62 O ARG A 38 4959 5087 5864 26 -105 -1096 O ATOM 63 CB ARG A 38 108.021 51.104 -26.011 1.00 40.73 C ANISOU 63 CB ARG A 38 4911 5345 5219 79 -266 -1079 C ATOM 64 CG ARG A 38 107.986 52.449 -26.722 1.00 53.25 C ANISOU 64 CG ARG A 38 6581 7074 6578 118 -356 -950 C ATOM 65 CD ARG A 38 107.265 52.384 -28.052 1.00 51.29 C ANISOU 65 CD ARG A 38 6311 7005 6171 124 -482 -1071 C ATOM 66 NE ARG A 38 107.303 53.654 -28.776 1.00 69.96 N ANISOU 66 NE ARG A 38 8788 9496 8299 166 -572 -924 N ATOM 67 CZ ARG A 38 108.064 53.860 -29.844 1.00 73.14 C ANISOU 67 CZ ARG A 38 9284 10041 8465 142 -560 -922 C ATOM 68 NH1 ARG A 38 108.796 52.858 -30.308 1.00 92.41 N ANISOU 68 NH1 ARG A 38 11695 12527 10890 85 -465 -1085 N ATOM 69 NH2 ARG A 38 108.065 55.033 -30.470 1.00 59.69 N ANISOU 69 NH2 ARG A 38 7707 8433 6542 174 -638 -765 N ATOM 70 N GLU A 39 109.615 49.113 -23.830 1.00 51.81 N ANISOU 70 N GLU A 39 6302 6355 7026 51 -6 -1097 N ATOM 71 CA GLU A 39 109.639 47.906 -23.006 1.00 43.82 C ANISOU 71 CA GLU A 39 5267 5153 6230 34 66 -1154 C ATOM 72 C GLU A 39 109.900 48.229 -21.536 1.00 53.06 C ANISOU 72 C GLU A 39 6488 6182 7490 57 115 -973 C ATOM 73 O GLU A 39 109.313 47.603 -20.646 1.00 71.55 O ANISOU 73 O GLU A 39 8822 8374 9989 29 153 -963 O ATOM 74 CB GLU A 39 110.700 46.934 -23.523 1.00 61.08 C ANISOU 74 CB GLU A 39 7449 7317 8442 45 121 -1288 C ATOM 75 CG GLU A 39 110.396 46.331 -24.889 1.00 94.99 C ANISOU 75 CG GLU A 39 11687 11730 12674 11 88 -1510 C ATOM 76 CD GLU A 39 109.242 45.346 -24.855 1.00 98.89 C ANISOU 76 CD GLU A 39 12114 12126 13333 -47 73 -1654 C ATOM 77 OE1 GLU A 39 109.078 44.656 -23.826 1.00 94.71 O ANISOU 77 OE1 GLU A 39 11593 11389 13005 -62 131 -1619 O ATOM 78 OE2 GLU A 39 108.503 45.263 -25.860 1.00 98.10 O ANISOU 78 OE2 GLU A 39 11956 12161 13157 -83 3 -1804 O ATOM 79 N PHE A 40 110.760 49.213 -21.263 1.00 44.14 N ANISOU 79 N PHE A 40 5415 5102 6254 97 120 -834 N ATOM 80 CA PHE A 40 111.305 49.420 -19.926 1.00 37.33 C ANISOU 80 CA PHE A 40 4603 4121 5459 126 166 -689 C ATOM 81 C PHE A 40 110.404 50.297 -19.068 1.00 43.69 C ANISOU 81 C PHE A 40 5424 4906 6271 118 147 -563 C ATOM 82 O PHE A 40 110.074 49.932 -17.935 1.00 32.15 O ANISOU 82 O PHE A 40 3979 3315 4923 108 190 -507 O ATOM 83 CB PHE A 40 112.702 50.031 -20.040 1.00 39.96 C ANISOU 83 CB PHE A 40 4969 4524 5690 164 184 -630 C ATOM 84 CG PHE A 40 113.329 50.384 -18.722 1.00 33.90 C ANISOU 84 CG PHE A 40 4246 3667 4967 198 210 -491 C ATOM 85 CD1 PHE A 40 113.840 49.404 -17.887 1.00 40.85 C ANISOU 85 CD1 PHE A 40 5138 4406 5976 234 242 -492 C ATOM 86 CD2 PHE A 40 113.423 51.707 -18.329 1.00 31.95 C ANISOU 86 CD2 PHE A 40 4036 3475 4630 199 193 -362 C ATOM 87 CE1 PHE A 40 114.429 49.740 -16.681 1.00 31.23 C ANISOU 87 CE1 PHE A 40 3965 3126 4776 272 249 -366 C ATOM 88 CE2 PHE A 40 114.004 52.050 -17.127 1.00 36.80 C ANISOU 88 CE2 PHE A 40 4686 4023 5275 226 211 -254 C ATOM 89 CZ PHE A 40 114.508 51.067 -16.299 1.00 40.20 C ANISOU 89 CZ PHE A 40 5125 4336 5814 264 234 -256 C ATOM 90 N PHE A 41 110.009 51.464 -19.575 1.00 41.90 N ANISOU 90 N PHE A 41 5199 4799 5921 125 87 -516 N ATOM 91 CA PHE A 41 109.226 52.378 -18.746 1.00 33.41 C ANISOU 91 CA PHE A 41 4131 3700 4861 132 70 -409 C ATOM 92 C PHE A 41 107.919 51.796 -18.224 1.00 33.78 C ANISOU 92 C PHE A 41 4114 3677 5043 95 83 -465 C ATOM 93 O PHE A 41 107.611 52.036 -17.043 1.00 37.70 O ANISOU 93 O PHE A 41 4628 4094 5604 90 129 -383 O ATOM 94 CB PHE A 41 108.935 53.691 -19.483 1.00 37.25 C ANISOU 94 CB PHE A 41 4635 4310 5208 160 -12 -357 C ATOM 95 CG PHE A 41 110.085 54.654 -19.509 1.00 44.68 C ANISOU 95 CG PHE A 41 5655 5285 6034 177 0 -246 C ATOM 96 CD1 PHE A 41 110.595 55.171 -18.327 1.00 44.97 C ANISOU 96 CD1 PHE A 41 5733 5244 6109 188 45 -139 C ATOM 97 CD2 PHE A 41 110.570 55.145 -20.706 1.00 34.74 C ANISOU 97 CD2 PHE A 41 4433 4146 4621 174 -34 -248 C ATOM 98 CE1 PHE A 41 111.626 56.091 -18.340 1.00 43.90 C ANISOU 98 CE1 PHE A 41 5658 5139 5883 189 58 -54 C ATOM 99 CE2 PHE A 41 111.595 56.074 -20.720 1.00 47.01 C ANISOU 99 CE2 PHE A 41 6059 5724 6078 168 -6 -147 C ATOM 100 CZ PHE A 41 112.119 56.551 -19.534 1.00 41.20 C ANISOU 100 CZ PHE A 41 5348 4902 5405 174 39 -56 C ATOM 101 N PRO A 42 107.099 51.082 -19.005 1.00 42.57 N ANISOU 101 N PRO A 42 5149 4823 6201 60 52 -610 N ATOM 102 CA PRO A 42 105.853 50.547 -18.423 1.00 48.37 C ANISOU 102 CA PRO A 42 5808 5488 7083 4 84 -672 C ATOM 103 C PRO A 42 106.085 49.699 -17.184 1.00 44.41 C ANISOU 103 C PRO A 42 5353 4812 6708 -39 199 -622 C ATOM 104 O PRO A 42 105.420 49.905 -16.159 1.00 46.33 O ANISOU 104 O PRO A 42 5590 5000 7015 -69 253 -564 O ATOM 105 CB PRO A 42 105.252 49.727 -19.573 1.00 54.85 C ANISOU 105 CB PRO A 42 6540 6369 7932 -36 35 -862 C ATOM 106 CG PRO A 42 105.807 50.342 -20.794 1.00 50.95 C ANISOU 106 CG PRO A 42 6072 6029 7258 19 -57 -873 C ATOM 107 CD PRO A 42 107.202 50.772 -20.442 1.00 45.79 C ANISOU 107 CD PRO A 42 5527 5347 6524 59 -10 -738 C ATOM 108 N ILE A 43 107.045 48.776 -17.243 1.00 49.43 N ANISOU 108 N ILE A 43 6043 5363 7374 -36 238 -639 N ATOM 109 CA ILE A 43 107.291 47.867 -16.126 1.00 61.55 C ANISOU 109 CA ILE A 43 7645 6717 9026 -65 332 -581 C ATOM 110 C ILE A 43 107.646 48.650 -14.867 1.00 52.32 C ANISOU 110 C ILE A 43 6552 5519 7806 -32 362 -405 C ATOM 111 O ILE A 43 107.011 48.500 -13.814 1.00 62.57 O ANISOU 111 O ILE A 43 7873 6734 9168 -82 433 -347 O ATOM 112 CB ILE A 43 108.409 46.874 -16.483 1.00 52.86 C ANISOU 112 CB ILE A 43 6589 5534 7960 -32 342 -628 C ATOM 113 CG1 ILE A 43 108.081 46.125 -17.772 1.00 69.82 C ANISOU 113 CG1 ILE A 43 8659 7721 10148 -67 314 -827 C ATOM 114 CG2 ILE A 43 108.592 45.887 -15.353 1.00 50.43 C ANISOU 114 CG2 ILE A 43 6366 5017 7777 -50 422 -556 C ATOM 115 CD1 ILE A 43 109.246 45.329 -18.310 1.00 79.92 C ANISOU 115 CD1 ILE A 43 9966 8955 11445 -17 317 -902 C ATOM 116 N VAL A 44 108.674 49.496 -14.963 1.00 41.12 N ANISOU 116 N VAL A 44 5176 4179 6270 42 316 -329 N ATOM 117 CA VAL A 44 109.188 50.195 -13.790 1.00 59.82 C ANISOU 117 CA VAL A 44 7617 6524 8588 76 337 -183 C ATOM 118 C VAL A 44 108.164 51.196 -13.261 1.00 45.76 C ANISOU 118 C VAL A 44 5809 4793 6786 53 344 -142 C ATOM 119 O VAL A 44 107.991 51.337 -12.047 1.00 43.63 O ANISOU 119 O VAL A 44 5587 4465 6526 38 401 -57 O ATOM 120 CB VAL A 44 110.535 50.865 -14.123 1.00 66.25 C ANISOU 120 CB VAL A 44 8460 7417 9296 144 289 -140 C ATOM 121 CG1 VAL A 44 111.552 49.809 -14.501 1.00 82.23 C ANISOU 121 CG1 VAL A 44 10494 9386 11362 177 292 -197 C ATOM 122 CG2 VAL A 44 110.383 51.860 -15.261 1.00 68.91 C ANISOU 122 CG2 VAL A 44 8751 7899 9533 150 228 -179 C ATOM 123 N TYR A 45 107.459 51.894 -14.155 1.00 32.76 N ANISOU 123 N TYR A 45 4085 3255 5106 56 283 -206 N ATOM 124 CA TYR A 45 106.454 52.858 -13.715 1.00 35.44 C ANISOU 124 CA TYR A 45 4381 3637 5446 55 279 -187 C ATOM 125 C TYR A 45 105.293 52.175 -13.006 1.00 48.08 C ANISOU 125 C TYR A 45 5929 5172 7168 -23 363 -236 C ATOM 126 O TYR A 45 104.799 52.681 -11.993 1.00 50.42 O ANISOU 126 O TYR A 45 6228 5455 7475 -37 418 -189 O ATOM 127 CB TYR A 45 105.949 53.681 -14.901 1.00 34.94 C ANISOU 127 CB TYR A 45 4252 3698 5326 94 174 -243 C ATOM 128 CG TYR A 45 106.902 54.771 -15.318 1.00 33.67 C ANISOU 128 CG TYR A 45 4160 3598 5036 155 113 -158 C ATOM 129 CD1 TYR A 45 107.837 55.268 -14.426 1.00 45.54 C ANISOU 129 CD1 TYR A 45 5745 5059 6501 172 153 -51 C ATOM 130 CD2 TYR A 45 106.892 55.285 -16.607 1.00 37.54 C ANISOU 130 CD2 TYR A 45 4640 4190 5435 188 20 -185 C ATOM 131 CE1 TYR A 45 108.726 56.264 -14.798 1.00 30.38 C ANISOU 131 CE1 TYR A 45 3881 3186 4475 206 112 16 C ATOM 132 CE2 TYR A 45 107.778 56.283 -16.988 1.00 42.52 C ANISOU 132 CE2 TYR A 45 5348 4864 5945 223 -16 -97 C ATOM 133 CZ TYR A 45 108.697 56.764 -16.082 1.00 40.89 C ANISOU 133 CZ TYR A 45 5210 4604 5724 225 37 -2 C ATOM 134 OH TYR A 45 109.579 57.753 -16.463 1.00 31.69 O ANISOU 134 OH TYR A 45 4112 3475 4453 239 15 74 O ATOM 135 N LEU A 46 104.853 51.016 -13.502 1.00 44.11 N ANISOU 135 N LEU A 46 5376 4625 6758 -85 386 -342 N ATOM 136 CA LEU A 46 103.751 50.321 -12.845 1.00 55.03 C ANISOU 136 CA LEU A 46 6706 5937 8267 -185 485 -395 C ATOM 137 C LEU A 46 104.192 49.734 -11.509 1.00 48.07 C ANISOU 137 C LEU A 46 5946 4915 7402 -226 601 -277 C ATOM 138 O LEU A 46 103.436 49.757 -10.527 1.00 50.42 O ANISOU 138 O LEU A 46 6238 5181 7737 -294 701 -253 O ATOM 139 CB LEU A 46 103.188 49.245 -13.775 1.00 48.97 C ANISOU 139 CB LEU A 46 5851 5151 7603 -252 478 -554 C ATOM 140 CG LEU A 46 102.462 49.844 -14.985 1.00 54.86 C ANISOU 140 CG LEU A 46 6463 6056 8326 -217 357 -681 C ATOM 141 CD1 LEU A 46 102.094 48.777 -16.016 1.00 42.52 C ANISOU 141 CD1 LEU A 46 4820 4494 6842 -277 330 -856 C ATOM 142 CD2 LEU A 46 101.224 50.619 -14.532 1.00 60.22 C ANISOU 142 CD2 LEU A 46 7028 6803 9049 -228 364 -714 C ATOM 143 N ILE A 47 105.426 49.224 -11.443 1.00 39.24 N ANISOU 143 N ILE A 47 4940 3722 6247 -181 588 -202 N ATOM 144 CA ILE A 47 105.947 48.733 -10.169 1.00 41.23 C ANISOU 144 CA ILE A 47 5327 3849 6491 -194 667 -70 C ATOM 145 C ILE A 47 106.012 49.866 -9.148 1.00 47.34 C ANISOU 145 C ILE A 47 6141 4687 7159 -163 682 34 C ATOM 146 O ILE A 47 105.555 49.725 -8.003 1.00 56.59 O ANISOU 146 O ILE A 47 7367 5806 8329 -224 782 99 O ATOM 147 CB ILE A 47 107.324 48.075 -10.366 1.00 45.72 C ANISOU 147 CB ILE A 47 5987 4340 7044 -120 619 -24 C ATOM 148 CG1 ILE A 47 107.209 46.812 -11.218 1.00 48.61 C ANISOU 148 CG1 ILE A 47 6325 4611 7534 -159 626 -139 C ATOM 149 CG2 ILE A 47 107.947 47.754 -9.027 1.00 33.63 C ANISOU 149 CG2 ILE A 47 4601 2701 5474 -101 664 130 C ATOM 150 CD1 ILE A 47 108.555 46.239 -11.631 1.00 37.44 C ANISOU 150 CD1 ILE A 47 4966 3142 6119 -67 567 -136 C ATOM 151 N ILE A 48 106.601 51.000 -9.543 1.00 38.09 N ANISOU 151 N ILE A 48 4951 3628 5894 -77 590 48 N ATOM 152 CA ILE A 48 106.671 52.152 -8.653 1.00 35.95 C ANISOU 152 CA ILE A 48 4710 3414 5533 -47 596 122 C ATOM 153 C ILE A 48 105.272 52.565 -8.233 1.00 43.02 C ANISOU 153 C ILE A 48 5524 4346 6476 -109 668 67 C ATOM 154 O ILE A 48 105.029 52.837 -7.057 1.00 49.68 O ANISOU 154 O ILE A 48 6415 5180 7282 -138 748 121 O ATOM 155 CB ILE A 48 107.433 53.316 -9.320 1.00 33.64 C ANISOU 155 CB ILE A 48 4403 3221 5157 38 490 129 C ATOM 156 CG1 ILE A 48 108.885 52.940 -9.588 1.00 41.67 C ANISOU 156 CG1 ILE A 48 5485 4218 6130 91 440 172 C ATOM 157 CG2 ILE A 48 107.404 54.558 -8.453 1.00 29.37 C ANISOU 157 CG2 ILE A 48 3884 2728 4546 62 498 180 C ATOM 158 CD1 ILE A 48 109.593 53.899 -10.534 1.00 49.47 C ANISOU 158 CD1 ILE A 48 6445 5303 7049 145 355 157 C ATOM 159 N PHE A 49 104.321 52.572 -9.172 1.00 45.45 N ANISOU 159 N PHE A 49 5702 4703 6864 -130 640 -54 N ATOM 160 CA PHE A 49 102.964 52.986 -8.839 1.00 36.76 C ANISOU 160 CA PHE A 49 4489 3650 5827 -177 699 -133 C ATOM 161 C PHE A 49 102.371 52.112 -7.748 1.00 50.52 C ANISOU 161 C PHE A 49 6262 5310 7624 -297 860 -119 C ATOM 162 O PHE A 49 101.904 52.617 -6.723 1.00 48.13 O ANISOU 162 O PHE A 49 5962 5030 7293 -326 949 -100 O ATOM 163 CB PHE A 49 102.068 52.956 -10.075 1.00 33.31 C ANISOU 163 CB PHE A 49 3898 3283 5476 -176 625 -278 C ATOM 164 CG PHE A 49 100.622 53.250 -9.768 1.00 57.71 C ANISOU 164 CG PHE A 49 6840 6426 8660 -224 682 -388 C ATOM 165 CD1 PHE A 49 100.209 54.543 -9.493 1.00 34.29 C ANISOU 165 CD1 PHE A 49 3819 3537 5671 -149 648 -398 C ATOM 166 CD2 PHE A 49 99.681 52.228 -9.713 1.00 43.60 C ANISOU 166 CD2 PHE A 49 4962 4606 7000 -347 779 -492 C ATOM 167 CE1 PHE A 49 98.886 54.819 -9.195 1.00 44.71 C ANISOU 167 CE1 PHE A 49 4982 4914 7093 -181 702 -519 C ATOM 168 CE2 PHE A 49 98.355 52.502 -9.413 1.00 37.14 C ANISOU 168 CE2 PHE A 49 3981 3850 6279 -397 842 -613 C ATOM 169 CZ PHE A 49 97.956 53.800 -9.155 1.00 36.96 C ANISOU 169 CZ PHE A 49 3891 3918 6233 -306 801 -631 C ATOM 170 N PHE A 50 102.368 50.799 -7.947 1.00 34.75 N ANISOU 170 N PHE A 50 4293 3210 5700 -375 909 -132 N ATOM 171 CA PHE A 50 101.679 49.956 -6.977 1.00 53.77 C ANISOU 171 CA PHE A 50 6734 5527 8168 -511 1078 -117 C ATOM 172 C PHE A 50 102.408 49.948 -5.634 1.00 52.96 C ANISOU 172 C PHE A 50 6815 5364 7944 -508 1147 52 C ATOM 173 O PHE A 50 101.788 50.162 -4.577 1.00 78.22 O ANISOU 173 O PHE A 50 10030 8580 11111 -581 1274 75 O ATOM 174 CB PHE A 50 101.493 48.552 -7.545 1.00 47.17 C ANISOU 174 CB PHE A 50 5894 4570 7457 -601 1113 -175 C ATOM 175 CG PHE A 50 100.468 48.487 -8.648 1.00 48.35 C ANISOU 175 CG PHE A 50 5844 4796 7732 -641 1074 -370 C ATOM 176 CD1 PHE A 50 99.113 48.465 -8.357 1.00 61.68 C ANISOU 176 CD1 PHE A 50 7391 6524 9522 -757 1182 -484 C ATOM 177 CD2 PHE A 50 100.856 48.458 -9.973 1.00 43.92 C ANISOU 177 CD2 PHE A 50 5229 4280 7179 -565 929 -449 C ATOM 178 CE1 PHE A 50 98.171 48.407 -9.374 1.00 61.51 C ANISOU 178 CE1 PHE A 50 7168 6586 9618 -785 1125 -678 C ATOM 179 CE2 PHE A 50 99.923 48.402 -10.989 1.00 46.03 C ANISOU 179 CE2 PHE A 50 5317 4633 7540 -594 873 -631 C ATOM 180 CZ PHE A 50 98.581 48.379 -10.690 1.00 63.27 C ANISOU 180 CZ PHE A 50 7351 6855 9833 -698 961 -748 C ATOM 181 N VAL A 51 103.732 49.751 -5.656 1.00 51.95 N ANISOU 181 N VAL A 51 6818 5182 7738 -418 1061 161 N ATOM 182 CA VAL A 51 104.497 49.746 -4.409 1.00 53.58 C ANISOU 182 CA VAL A 51 7196 5344 7816 -397 1096 319 C ATOM 183 C VAL A 51 104.344 51.074 -3.671 1.00 52.64 C ANISOU 183 C VAL A 51 7059 5354 7588 -365 1105 326 C ATOM 184 O VAL A 51 104.197 51.106 -2.439 1.00 42.62 O ANISOU 184 O VAL A 51 5885 4081 6229 -415 1207 402 O ATOM 185 CB VAL A 51 105.975 49.419 -4.695 1.00 58.81 C ANISOU 185 CB VAL A 51 7961 5954 8431 -283 973 402 C ATOM 186 CG1 VAL A 51 106.827 49.610 -3.440 1.00 58.77 C ANISOU 186 CG1 VAL A 51 8114 5939 8277 -235 969 552 C ATOM 187 CG2 VAL A 51 106.111 47.996 -5.239 1.00 44.09 C ANISOU 187 CG2 VAL A 51 6134 3934 6684 -315 982 393 C ATOM 188 N GLY A 52 104.341 52.185 -4.405 1.00 36.88 N ANISOU 188 N GLY A 52 4949 3469 5595 -286 1006 245 N ATOM 189 CA GLY A 52 104.307 53.493 -3.796 1.00 33.26 C ANISOU 189 CA GLY A 52 4477 3110 5051 -240 999 242 C ATOM 190 C GLY A 52 102.947 53.893 -3.281 1.00 42.33 C ANISOU 190 C GLY A 52 5524 4314 6245 -315 1119 150 C ATOM 191 O GLY A 52 102.857 54.498 -2.214 1.00 53.84 O ANISOU 191 O GLY A 52 7026 5816 7614 -325 1188 171 O ATOM 192 N VAL A 53 101.883 53.583 -4.025 1.00 39.49 N ANISOU 192 N VAL A 53 5018 3965 6024 -367 1145 30 N ATOM 193 CA VAL A 53 100.541 53.746 -3.476 1.00 39.69 C ANISOU 193 CA VAL A 53 4927 4040 6113 -456 1282 -75 C ATOM 194 C VAL A 53 100.431 53.007 -2.152 1.00 48.86 C ANISOU 194 C VAL A 53 6216 5146 7205 -581 1462 11 C ATOM 195 O VAL A 53 100.016 53.583 -1.142 1.00 53.64 O ANISOU 195 O VAL A 53 6824 5814 7741 -613 1569 -4 O ATOM 196 CB VAL A 53 99.470 53.277 -4.478 1.00 52.14 C ANISOU 196 CB VAL A 53 6320 5631 7859 -508 1279 -223 C ATOM 197 CG1 VAL A 53 98.111 53.224 -3.804 1.00 55.50 C ANISOU 197 CG1 VAL A 53 6619 6104 8366 -627 1451 -338 C ATOM 198 CG2 VAL A 53 99.410 54.224 -5.652 1.00 57.82 C ANISOU 198 CG2 VAL A 53 6917 6433 8618 -376 1102 -307 C ATOM 199 N LEU A 54 100.848 51.735 -2.123 1.00 45.31 N ANISOU 199 N LEU A 54 5887 4569 6758 -647 1498 107 N ATOM 200 CA LEU A 54 100.752 50.968 -0.879 1.00 52.99 C ANISOU 200 CA LEU A 54 7014 5469 7651 -769 1667 217 C ATOM 201 C LEU A 54 101.526 51.641 0.258 1.00 59.66 C ANISOU 201 C LEU A 54 8009 6363 8294 -708 1662 333 C ATOM 202 O LEU A 54 100.956 51.969 1.314 1.00 54.97 O ANISOU 202 O LEU A 54 7436 5833 7616 -783 1805 325 O ATOM 203 CB LEU A 54 101.243 49.541 -1.118 1.00 47.63 C ANISOU 203 CB LEU A 54 6464 4616 7016 -817 1670 318 C ATOM 204 CG LEU A 54 101.158 48.536 0.032 1.00 65.49 C ANISOU 204 CG LEU A 54 8918 6758 9208 -949 1838 460 C ATOM 205 CD1 LEU A 54 99.745 48.431 0.565 1.00 76.94 C ANISOU 205 CD1 LEU A 54 10275 8246 10714 -1132 2059 368 C ATOM 206 CD2 LEU A 54 101.614 47.176 -0.467 1.00 55.18 C ANISOU 206 CD2 LEU A 54 7714 5255 7995 -971 1811 533 C ATOM 207 N GLY A 55 102.824 51.875 0.047 1.00 39.53 N ANISOU 207 N GLY A 55 5555 3800 5665 -575 1499 422 N ATOM 208 CA GLY A 55 103.651 52.443 1.101 1.00 40.16 C ANISOU 208 CA GLY A 55 5776 3930 5555 -516 1473 522 C ATOM 209 C GLY A 55 103.196 53.820 1.549 1.00 48.51 C ANISOU 209 C GLY A 55 6741 5129 6561 -493 1500 418 C ATOM 210 O GLY A 55 102.990 54.058 2.744 1.00 64.37 O ANISOU 210 O GLY A 55 8829 7192 8437 -545 1611 442 O ATOM 211 N ASN A 56 103.041 54.750 0.597 1.00 36.47 N ANISOU 211 N ASN A 56 5058 3662 5138 -411 1397 299 N ATOM 212 CA ASN A 56 102.666 56.122 0.927 1.00 47.42 C ANISOU 212 CA ASN A 56 6359 5156 6503 -366 1401 194 C ATOM 213 C ASN A 56 101.262 56.211 1.519 1.00 55.94 C ANISOU 213 C ASN A 56 7334 6293 7628 -470 1584 79 C ATOM 214 O ASN A 56 101.012 57.052 2.385 1.00 67.51 O ANISOU 214 O ASN A 56 8794 7840 9016 -468 1652 20 O ATOM 215 CB ASN A 56 102.796 57.002 -0.314 1.00 47.55 C ANISOU 215 CB ASN A 56 6248 5192 6626 -253 1245 114 C ATOM 216 CG ASN A 56 104.235 57.383 -0.601 1.00 56.71 C ANISOU 216 CG ASN A 56 7504 6337 7708 -155 1091 201 C ATOM 217 OD1 ASN A 56 104.951 57.858 0.285 1.00 46.05 O ANISOU 217 OD1 ASN A 56 6252 5016 6227 -131 1082 247 O ATOM 218 ND2 ASN A 56 104.676 57.148 -1.831 1.00 64.32 N ANISOU 218 ND2 ASN A 56 8431 7263 8744 -104 975 212 N ATOM 219 N GLY A 57 100.333 55.351 1.096 1.00 48.90 N ANISOU 219 N GLY A 57 6351 5365 6865 -569 1675 28 N ATOM 220 CA GLY A 57 99.022 55.341 1.725 1.00 57.84 C ANISOU 220 CA GLY A 57 7375 6558 8042 -688 1871 -88 C ATOM 221 C GLY A 57 99.080 54.918 3.177 1.00 59.28 C ANISOU 221 C GLY A 57 7727 6749 8047 -803 2048 6 C ATOM 222 O GLY A 57 98.530 55.592 4.057 1.00 79.73 O ANISOU 222 O GLY A 57 10281 9442 10571 -837 2171 -79 O ATOM 223 N LEU A 58 99.747 53.793 3.452 1.00 53.18 N ANISOU 223 N LEU A 58 7150 5868 7189 -858 2062 183 N ATOM 224 CA LEU A 58 99.939 53.402 4.847 1.00 67.26 C ANISOU 224 CA LEU A 58 9135 7656 8764 -950 2204 309 C ATOM 225 C LEU A 58 100.590 54.527 5.654 1.00 73.54 C ANISOU 225 C LEU A 58 10001 8564 9377 -853 2145 310 C ATOM 226 O LEU A 58 100.130 54.872 6.756 1.00 68.54 O ANISOU 226 O LEU A 58 9405 8027 8611 -928 2301 274 O ATOM 227 CB LEU A 58 100.780 52.126 4.923 1.00 67.28 C ANISOU 227 CB LEU A 58 9356 7504 8702 -971 2167 519 C ATOM 228 CG LEU A 58 100.120 50.845 4.412 1.00 70.48 C ANISOU 228 CG LEU A 58 9742 7773 9265 -1107 2270 533 C ATOM 229 CD1 LEU A 58 101.108 49.682 4.358 1.00 74.72 C ANISOU 229 CD1 LEU A 58 10494 8132 9762 -1082 2189 734 C ATOM 230 CD2 LEU A 58 98.940 50.503 5.302 1.00 83.02 C ANISOU 230 CD2 LEU A 58 11326 9392 10825 -1312 2545 496 C ATOM 231 N SER A 59 101.642 55.137 5.099 1.00 59.60 N ANISOU 231 N SER A 59 8245 6794 7608 -694 1930 333 N ATOM 232 CA SER A 59 102.397 56.145 5.833 1.00 63.60 C ANISOU 232 CA SER A 59 8825 7392 7949 -607 1858 333 C ATOM 233 C SER A 59 101.549 57.373 6.140 1.00 67.83 C ANISOU 233 C SER A 59 9209 8046 8517 -605 1939 139 C ATOM 234 O SER A 59 101.558 57.872 7.270 1.00 62.05 O ANISOU 234 O SER A 59 8550 7409 7618 -630 2023 112 O ATOM 235 CB SER A 59 103.635 56.539 5.038 1.00 57.05 C ANISOU 235 CB SER A 59 8005 6525 7146 -458 1625 376 C ATOM 236 OG SER A 59 104.512 55.436 4.896 1.00 63.25 O ANISOU 236 OG SER A 59 8932 7210 7890 -444 1549 543 O ATOM 237 N ILE A 60 100.824 57.885 5.140 1.00 62.84 N ANISOU 237 N ILE A 60 8366 7413 8096 -563 1904 -5 N ATOM 238 CA ILE A 60 99.999 59.073 5.342 1.00 63.15 C ANISOU 238 CA ILE A 60 8246 7547 8200 -533 1961 -200 C ATOM 239 C ILE A 60 98.851 58.768 6.294 1.00 67.74 C ANISOU 239 C ILE A 60 8787 8207 8745 -680 2213 -287 C ATOM 240 O ILE A 60 98.420 59.634 7.067 1.00 70.26 O ANISOU 240 O ILE A 60 9056 8628 9012 -679 2308 -421 O ATOM 241 CB ILE A 60 99.486 59.607 3.992 1.00 57.64 C ANISOU 241 CB ILE A 60 7343 6821 7738 -438 1843 -317 C ATOM 242 CG1 ILE A 60 100.646 60.077 3.117 1.00 68.13 C ANISOU 242 CG1 ILE A 60 8722 8086 9077 -303 1614 -238 C ATOM 243 CG2 ILE A 60 98.530 60.767 4.198 1.00 56.64 C ANISOU 243 CG2 ILE A 60 7042 6775 7705 -393 1900 -524 C ATOM 244 CD1 ILE A 60 100.245 60.369 1.688 1.00 68.55 C ANISOU 244 CD1 ILE A 60 8618 8103 9327 -220 1488 -305 C ATOM 245 N TYR A 61 98.333 57.537 6.254 1.00 67.62 N ANISOU 245 N TYR A 61 8788 8143 8760 -817 2339 -223 N ATOM 246 CA TYR A 61 97.302 57.160 7.214 1.00 75.51 C ANISOU 246 CA TYR A 61 9767 9217 9706 -987 2606 -288 C ATOM 247 C TYR A 61 97.840 57.225 8.634 1.00 90.56 C ANISOU 247 C TYR A 61 11893 11190 11323 -1037 2701 -195 C ATOM 248 O TYR A 61 97.166 57.730 9.540 1.00113.52 O ANISOU 248 O TYR A 61 14758 14223 14151 -1105 2878 -322 O ATOM 249 CB TYR A 61 96.769 55.760 6.911 1.00 80.73 C ANISOU 249 CB TYR A 61 10436 9787 10451 -1143 2723 -215 C ATOM 250 CG TYR A 61 95.682 55.322 7.871 1.00100.52 C ANISOU 250 CG TYR A 61 12920 12364 12907 -1349 3024 -281 C ATOM 251 CD1 TYR A 61 94.390 55.821 7.763 1.00100.17 C ANISOU 251 CD1 TYR A 61 12605 12425 13029 -1396 3158 -526 C ATOM 252 CD2 TYR A 61 95.951 54.422 8.898 1.00111.94 C ANISOU 252 CD2 TYR A 61 14617 13777 14136 -1494 3178 -98 C ATOM 253 CE1 TYR A 61 93.392 55.430 8.642 1.00 91.89 C ANISOU 253 CE1 TYR A 61 11520 11456 11939 -1600 3455 -604 C ATOM 254 CE2 TYR A 61 94.957 54.025 9.785 1.00109.90 C ANISOU 254 CE2 TYR A 61 14352 13589 13817 -1703 3477 -151 C ATOM 255 CZ TYR A 61 93.679 54.535 9.651 1.00 99.79 C ANISOU 255 CZ TYR A 61 12783 12422 12710 -1764 3624 -412 C ATOM 256 OH TYR A 61 92.683 54.152 10.522 1.00100.83 O ANISOU 256 OH TYR A 61 12888 12636 12788 -1986 3941 -484 O ATOM 257 N VAL A 62 99.062 56.730 8.843 1.00 74.23 N ANISOU 257 N VAL A 62 10057 9053 9093 -996 2578 16 N ATOM 258 CA VAL A 62 99.656 56.773 10.178 1.00 72.92 C ANISOU 258 CA VAL A 62 10114 8962 8631 -1027 2634 115 C ATOM 259 C VAL A 62 99.927 58.212 10.601 1.00 70.11 C ANISOU 259 C VAL A 62 9703 8729 8207 -919 2568 -35 C ATOM 260 O VAL A 62 99.693 58.591 11.756 1.00 57.63 O ANISOU 260 O VAL A 62 8187 7275 6435 -982 2709 -95 O ATOM 261 CB VAL A 62 100.938 55.923 10.222 1.00 61.81 C ANISOU 261 CB VAL A 62 8947 7449 7088 -979 2481 366 C ATOM 262 CG1 VAL A 62 101.624 56.067 11.571 1.00 50.18 C ANISOU 262 CG1 VAL A 62 7699 6071 5296 -983 2495 462 C ATOM 263 CG2 VAL A 62 100.612 54.476 9.961 1.00 64.76 C ANISOU 263 CG2 VAL A 62 9400 7684 7524 -1099 2573 510 C ATOM 264 N PHE A 63 100.418 59.036 9.675 1.00 66.02 N ANISOU 264 N PHE A 63 9071 8173 7840 -764 2362 -103 N ATOM 265 CA PHE A 63 100.826 60.393 10.025 1.00 60.86 C ANISOU 265 CA PHE A 63 8387 7601 7136 -659 2280 -232 C ATOM 266 C PHE A 63 99.638 61.255 10.434 1.00 65.09 C ANISOU 266 C PHE A 63 8750 8240 7741 -691 2447 -473 C ATOM 267 O PHE A 63 99.760 62.099 11.330 1.00 74.11 O ANISOU 267 O PHE A 63 9926 9485 8749 -675 2488 -580 O ATOM 268 CB PHE A 63 101.568 61.022 8.849 1.00 59.43 C ANISOU 268 CB PHE A 63 8129 7332 7118 -505 2038 -236 C ATOM 269 CG PHE A 63 102.945 60.463 8.635 1.00 65.94 C ANISOU 269 CG PHE A 63 9117 8091 7847 -452 1863 -41 C ATOM 270 CD1 PHE A 63 103.643 59.881 9.681 1.00 70.64 C ANISOU 270 CD1 PHE A 63 9922 8727 8190 -494 1879 95 C ATOM 271 CD2 PHE A 63 103.525 60.479 7.379 1.00 63.25 C ANISOU 271 CD2 PHE A 63 8718 7651 7664 -359 1684 3 C ATOM 272 CE1 PHE A 63 104.909 59.361 9.486 1.00 74.36 C ANISOU 272 CE1 PHE A 63 10522 9140 8590 -428 1706 259 C ATOM 273 CE2 PHE A 63 104.787 59.954 7.178 1.00 61.63 C ANISOU 273 CE2 PHE A 63 8639 7394 7384 -308 1533 159 C ATOM 274 CZ PHE A 63 105.479 59.395 8.233 1.00 71.12 C ANISOU 274 CZ PHE A 63 10031 8635 8357 -336 1539 282 C ATOM 275 N LEU A 64 98.484 61.059 9.798 1.00 74.23 N ANISOU 275 N LEU A 64 9712 9379 9113 -732 2543 -578 N ATOM 276 CA LEU A 64 97.333 61.923 10.031 1.00 79.82 C ANISOU 276 CA LEU A 64 10212 10179 9936 -732 2678 -832 C ATOM 277 C LEU A 64 96.505 61.522 11.245 1.00 85.07 C ANISOU 277 C LEU A 64 10901 10973 10450 -907 2970 -899 C ATOM 278 O LEU A 64 95.529 62.214 11.556 1.00100.55 O ANISOU 278 O LEU A 64 12680 13028 12495 -916 3109 -1132 O ATOM 279 CB LEU A 64 96.431 61.951 8.794 1.00 84.53 C ANISOU 279 CB LEU A 64 10562 10718 10839 -684 2634 -939 C ATOM 280 CG LEU A 64 96.999 62.612 7.539 1.00 86.34 C ANISOU 280 CG LEU A 64 10730 10841 11235 -504 2366 -924 C ATOM 281 CD1 LEU A 64 96.021 62.470 6.395 1.00 90.17 C ANISOU 281 CD1 LEU A 64 10986 11290 11984 -473 2332 -1020 C ATOM 282 CD2 LEU A 64 97.296 64.072 7.798 1.00 77.32 C ANISOU 282 CD2 LEU A 64 9563 9718 10097 -372 2282 -1055 C ATOM 283 N GLN A 65 96.852 60.441 11.929 1.00 76.15 N ANISOU 283 N GLN A 65 9988 9845 9100 -1043 3069 -704 N ATOM 284 CA GLN A 65 96.094 60.042 13.109 1.00 92.85 C ANISOU 284 CA GLN A 65 12155 12084 11040 -1228 3364 -747 C ATOM 285 C GLN A 65 96.356 61.014 14.251 1.00108.21 C ANISOU 285 C GLN A 65 14172 14177 12764 -1201 3415 -863 C ATOM 286 O GLN A 65 97.521 61.323 14.543 1.00104.23 O ANISOU 286 O GLN A 65 13844 13667 12091 -1109 3243 -760 O ATOM 287 CB GLN A 65 96.457 58.622 13.533 1.00 87.96 C ANISOU 287 CB GLN A 65 11787 11405 10229 -1374 3443 -477 C ATOM 288 CG GLN A 65 96.088 57.554 12.520 1.00 78.00 C ANISOU 288 CG GLN A 65 10459 9996 9183 -1435 3436 -384 C ATOM 289 CD GLN A 65 94.606 57.548 12.196 1.00 85.30 C ANISOU 289 CD GLN A 65 11105 10969 10337 -1542 3635 -602 C ATOM 290 OE1 GLN A 65 94.203 57.869 11.079 1.00 85.03 O ANISOU 290 OE1 GLN A 65 10837 10889 10581 -1447 3518 -727 O ATOM 291 NE2 GLN A 65 93.785 57.205 13.182 1.00100.86 N ANISOU 291 NE2 GLN A 65 13094 13045 12184 -1739 3936 -656 N ATOM 292 N PRO A 66 95.320 61.514 14.929 1.00108.50 N ANISOU 292 N PRO A 66 14071 14356 12796 -1279 3649 -1094 N ATOM 293 CA PRO A 66 95.518 62.484 16.011 1.00108.27 C ANISOU 293 CA PRO A 66 14098 14477 12564 -1254 3706 -1242 C ATOM 294 C PRO A 66 95.980 61.871 17.323 1.00121.64 C ANISOU 294 C PRO A 66 16084 16277 13855 -1393 3838 -1086 C ATOM 295 O PRO A 66 96.253 62.614 18.272 1.00119.76 O ANISOU 295 O PRO A 66 15921 16176 13405 -1377 3873 -1198 O ATOM 296 CB PRO A 66 94.123 63.105 16.168 1.00 89.99 C ANISOU 296 CB PRO A 66 11503 12272 10419 -1294 3928 -1558 C ATOM 297 CG PRO A 66 93.196 62.010 15.770 1.00 91.94 C ANISOU 297 CG PRO A 66 11653 12487 10794 -1450 4098 -1509 C ATOM 298 CD PRO A 66 93.891 61.245 14.676 1.00 94.69 C ANISOU 298 CD PRO A 66 12079 12645 11253 -1391 3868 -1261 C ATOM 299 N TYR A 67 96.074 60.544 17.398 1.00131.45 N ANISOU 299 N TYR A 67 17503 17458 14985 -1527 3906 -832 N ATOM 300 CA TYR A 67 96.413 59.877 18.650 1.00138.04 C ANISOU 300 CA TYR A 67 18636 18387 15427 -1667 4043 -659 C ATOM 301 C TYR A 67 97.854 60.162 19.057 1.00132.40 C ANISOU 301 C TYR A 67 18153 17682 14473 -1535 3793 -520 C ATOM 302 O TYR A 67 98.115 60.684 20.146 1.00124.60 O ANISOU 302 O TYR A 67 17283 16858 13200 -1550 3845 -590 O ATOM 303 CB TYR A 67 96.168 58.376 18.499 1.00142.56 C ANISOU 303 CB TYR A 67 19342 18842 15981 -1828 4156 -408 C ATOM 304 CG TYR A 67 94.704 58.023 18.380 1.00143.36 C ANISOU 304 CG TYR A 67 19237 18973 16258 -2010 4457 -557 C ATOM 305 CD1 TYR A 67 93.725 58.843 18.929 1.00148.44 C ANISOU 305 CD1 TYR A 67 19673 19788 16941 -2043 4621 -846 C ATOM 306 CD2 TYR A 67 94.295 56.908 17.662 1.00148.40 C ANISOU 306 CD2 TYR A 67 19849 19456 17079 -2114 4507 -425 C ATOM 307 CE1 TYR A 67 92.383 58.533 18.811 1.00161.24 C ANISOU 307 CE1 TYR A 67 21064 21427 18772 -2164 4794 -985 C ATOM 308 CE2 TYR A 67 92.954 56.594 17.533 1.00159.69 C ANISOU 308 CE2 TYR A 67 21050 20905 18720 -2244 4681 -572 C ATOM 309 CZ TYR A 67 92.003 57.411 18.110 1.00166.73 C ANISOU 309 CZ TYR A 67 21736 21973 19641 -2267 4823 -851 C ATOM 310 OH TYR A 67 90.666 57.108 17.988 1.00172.15 O ANISOU 310 OH TYR A 67 22187 22685 20537 -2393 4987 -1008 O ATOM 311 N LYS A 68 98.805 59.823 18.191 1.00140.89 N ANISOU 311 N LYS A 68 19281 18592 15657 -1408 3520 -339 N ATOM 312 CA LYS A 68 100.213 59.997 18.517 1.00137.78 C ANISOU 312 CA LYS A 68 19087 18206 15059 -1284 3273 -206 C ATOM 313 C LYS A 68 100.575 61.476 18.569 1.00132.52 C ANISOU 313 C LYS A 68 18292 17623 14436 -1148 3147 -449 C ATOM 314 O LYS A 68 100.041 62.292 17.811 1.00137.08 O ANISOU 314 O LYS A 68 18618 18159 15307 -1079 3134 -655 O ATOM 315 CB LYS A 68 101.083 59.279 17.486 1.00139.14 C ANISOU 315 CB LYS A 68 19308 18181 15378 -1183 3028 15 C ATOM 316 N LYS A 69 101.486 61.822 19.478 1.00121.25 N ANISOU 316 N LYS A 69 17043 16310 12716 -1108 3048 -426 N ATOM 317 CA LYS A 69 101.956 63.197 19.572 1.00106.68 C ANISOU 317 CA LYS A 69 15098 14531 10905 -988 2917 -653 C ATOM 318 C LYS A 69 102.694 63.584 18.296 1.00113.07 C ANISOU 318 C LYS A 69 15786 15170 12007 -829 2649 -633 C ATOM 319 O LYS A 69 103.588 62.867 17.838 1.00108.99 O ANISOU 319 O LYS A 69 15377 14554 11480 -777 2468 -409 O ATOM 320 CB LYS A 69 102.868 63.364 20.787 1.00 90.97 C ANISOU 320 CB LYS A 69 13334 12703 8529 -984 2845 -621 C ATOM 321 N SER A 70 102.309 64.719 17.718 1.00120.15 N ANISOU 321 N SER A 70 16461 16028 13162 -752 2627 -868 N ATOM 322 CA SER A 70 102.905 65.161 16.465 1.00120.74 C ANISOU 322 CA SER A 70 16421 15940 13515 -616 2397 -855 C ATOM 323 C SER A 70 104.296 65.734 16.710 1.00108.02 C ANISOU 323 C SER A 70 14909 14349 11784 -527 2173 -845 C ATOM 324 O SER A 70 104.505 66.513 17.645 1.00108.19 O ANISOU 324 O SER A 70 14970 14499 11638 -532 2193 -1005 O ATOM 325 CB SER A 70 102.011 66.203 15.794 1.00122.98 C ANISOU 325 CB SER A 70 16456 16166 14107 -557 2444 -1096 C ATOM 326 OG SER A 70 101.934 67.384 16.575 1.00123.31 O ANISOU 326 OG SER A 70 16461 16306 14084 -534 2491 -1343 O ATOM 327 N THR A 71 105.249 65.337 15.871 1.00 97.15 N ANISOU 327 N THR A 71 13561 12854 10495 -452 1964 -673 N ATOM 328 CA THR A 71 106.614 65.842 15.902 1.00 83.86 C ANISOU 328 CA THR A 71 11934 11177 8751 -369 1738 -667 C ATOM 329 C THR A 71 106.912 66.557 14.590 1.00 85.75 C ANISOU 329 C THR A 71 12014 11258 9308 -275 1595 -720 C ATOM 330 O THR A 71 106.154 66.469 13.621 1.00 94.97 O ANISOU 330 O THR A 71 13056 12312 10715 -263 1642 -716 O ATOM 331 CB THR A 71 107.624 64.710 16.131 1.00 84.42 C ANISOU 331 CB THR A 71 12189 11262 8624 -360 1608 -415 C ATOM 332 OG1 THR A 71 107.599 63.818 15.014 1.00 72.13 O ANISOU 332 OG1 THR A 71 10598 9552 7256 -338 1562 -239 O ATOM 333 CG2 THR A 71 107.262 63.930 17.386 1.00 91.81 C ANISOU 333 CG2 THR A 71 13313 12337 9235 -457 1756 -325 C ATOM 334 N SER A 72 108.039 67.272 14.563 1.00 87.57 N ANISOU 334 N SER A 72 12254 11487 9532 -214 1418 -771 N ATOM 335 CA SER A 72 108.411 68.019 13.364 1.00 88.03 C ANISOU 335 CA SER A 72 12185 11395 9868 -141 1290 -814 C ATOM 336 C SER A 72 108.829 67.084 12.233 1.00 82.88 C ANISOU 336 C SER A 72 11528 10631 9332 -109 1187 -601 C ATOM 337 O SER A 72 108.463 67.297 11.064 1.00 96.73 O ANISOU 337 O SER A 72 13167 12254 11331 -72 1169 -598 O ATOM 338 CB SER A 72 109.530 69.005 13.702 1.00 75.97 C ANISOU 338 CB SER A 72 10670 9898 8296 -112 1147 -935 C ATOM 339 OG SER A 72 110.698 68.325 14.126 1.00 78.97 O ANISOU 339 OG SER A 72 11167 10363 8476 -107 1012 -804 O ATOM 340 N VAL A 73 109.599 66.044 12.563 1.00 63.92 N ANISOU 340 N VAL A 73 9254 8279 6754 -113 1112 -425 N ATOM 341 CA VAL A 73 110.012 65.071 11.558 1.00 68.70 C ANISOU 341 CA VAL A 73 9859 8781 7463 -80 1023 -236 C ATOM 342 C VAL A 73 108.791 64.453 10.891 1.00 72.37 C ANISOU 342 C VAL A 73 10262 9162 8074 -114 1159 -185 C ATOM 343 O VAL A 73 108.821 64.109 9.704 1.00 75.24 O ANISOU 343 O VAL A 73 10554 9412 8622 -82 1101 -111 O ATOM 344 CB VAL A 73 110.923 64.002 12.194 1.00 64.45 C ANISOU 344 CB VAL A 73 9479 8309 6701 -68 931 -64 C ATOM 345 CG1 VAL A 73 112.155 64.657 12.818 1.00 61.49 C ANISOU 345 CG1 VAL A 73 9137 8034 6193 -27 775 -140 C ATOM 346 CG2 VAL A 73 110.164 63.191 13.229 1.00 80.93 C ANISOU 346 CG2 VAL A 73 11704 10474 8574 -142 1086 15 C ATOM 347 N ASN A 74 107.687 64.327 11.634 1.00 72.24 N ANISOU 347 N ASN A 74 10260 9211 7977 -188 1347 -241 N ATOM 348 CA ASN A 74 106.464 63.798 11.042 1.00 74.74 C ANISOU 348 CA ASN A 74 10490 9463 8447 -233 1486 -226 C ATOM 349 C ASN A 74 105.833 64.788 10.074 1.00 79.21 C ANISOU 349 C ASN A 74 10867 9950 9280 -181 1478 -378 C ATOM 350 O ASN A 74 105.242 64.373 9.074 1.00 91.18 O ANISOU 350 O ASN A 74 12288 11379 10978 -174 1489 -340 O ATOM 351 CB ASN A 74 105.461 63.406 12.128 1.00 82.33 C ANISOU 351 CB ASN A 74 11505 10526 9250 -341 1707 -258 C ATOM 352 CG ASN A 74 105.892 62.177 12.898 1.00 87.77 C ANISOU 352 CG ASN A 74 12401 11255 9692 -401 1728 -56 C ATOM 353 OD1 ASN A 74 106.492 61.260 12.337 1.00 80.87 O ANISOU 353 OD1 ASN A 74 11590 10289 8848 -372 1622 124 O ATOM 354 ND2 ASN A 74 105.554 62.133 14.184 1.00105.33 N ANISOU 354 ND2 ASN A 74 14737 13613 11669 -483 1871 -84 N ATOM 355 N VAL A 75 105.950 66.090 10.342 1.00 68.35 N ANISOU 355 N VAL A 75 9440 8598 7933 -139 1451 -550 N ATOM 356 CA VAL A 75 105.480 67.086 9.381 1.00 60.05 C ANISOU 356 CA VAL A 75 8234 7444 7138 -68 1412 -671 C ATOM 357 C VAL A 75 106.264 66.971 8.077 1.00 51.27 C ANISOU 357 C VAL A 75 7105 6213 6163 -7 1240 -549 C ATOM 358 O VAL A 75 105.687 66.958 6.977 1.00 52.78 O ANISOU 358 O VAL A 75 7194 6315 6547 30 1220 -538 O ATOM 359 CB VAL A 75 105.581 68.499 9.981 1.00 62.97 C ANISOU 359 CB VAL A 75 8578 7836 7510 -35 1410 -875 C ATOM 360 CG1 VAL A 75 105.244 69.543 8.931 1.00 54.48 C ANISOU 360 CG1 VAL A 75 7374 6622 6704 53 1341 -969 C ATOM 361 CG2 VAL A 75 104.661 68.634 11.192 1.00 64.15 C ANISOU 361 CG2 VAL A 75 8722 8114 7537 -95 1603 -1026 C ATOM 362 N PHE A 76 107.592 66.876 8.180 1.00 52.29 N ANISOU 362 N PHE A 76 7329 6353 6186 3 1112 -465 N ATOM 363 CA PHE A 76 108.401 66.739 6.970 1.00 53.48 C ANISOU 363 CA PHE A 76 7460 6407 6453 48 966 -359 C ATOM 364 C PHE A 76 108.072 65.447 6.224 1.00 59.83 C ANISOU 364 C PHE A 76 8257 7171 7303 37 979 -212 C ATOM 365 O PHE A 76 107.936 65.445 4.995 1.00 64.39 O ANISOU 365 O PHE A 76 8759 7661 8044 72 924 -180 O ATOM 366 CB PHE A 76 109.888 66.809 7.313 1.00 55.02 C ANISOU 366 CB PHE A 76 7737 6643 6526 55 838 -318 C ATOM 367 CG PHE A 76 110.337 68.168 7.755 1.00 62.64 C ANISOU 367 CG PHE A 76 8688 7617 7494 62 800 -476 C ATOM 368 CD1 PHE A 76 110.523 69.178 6.828 1.00 64.13 C ANISOU 368 CD1 PHE A 76 8806 7691 7870 93 736 -533 C ATOM 369 CD2 PHE A 76 110.590 68.434 9.089 1.00 59.09 C ANISOU 369 CD2 PHE A 76 8308 7288 6857 32 826 -567 C ATOM 370 CE1 PHE A 76 110.935 70.429 7.223 1.00 77.36 C ANISOU 370 CE1 PHE A 76 10477 9350 9569 89 708 -682 C ATOM 371 CE2 PHE A 76 111.011 69.690 9.488 1.00 62.55 C ANISOU 371 CE2 PHE A 76 8728 7729 7310 31 791 -734 C ATOM 372 CZ PHE A 76 111.184 70.687 8.552 1.00 73.74 C ANISOU 372 CZ PHE A 76 10071 9009 8937 57 734 -793 C ATOM 373 N MET A 77 107.925 64.338 6.953 1.00 60.10 N ANISOU 373 N MET A 77 8380 7265 7191 -17 1055 -121 N ATOM 374 CA MET A 77 107.631 63.064 6.303 1.00 54.56 C ANISOU 374 CA MET A 77 7682 6507 6541 -38 1075 11 C ATOM 375 C MET A 77 106.242 63.060 5.681 1.00 56.67 C ANISOU 375 C MET A 77 7821 6735 6978 -60 1178 -60 C ATOM 376 O MET A 77 106.040 62.467 4.618 1.00 63.62 O ANISOU 376 O MET A 77 8644 7543 7985 -49 1143 -3 O ATOM 377 CB MET A 77 107.779 61.922 7.305 1.00 51.29 C ANISOU 377 CB MET A 77 7415 6143 5932 -96 1138 131 C ATOM 378 CG MET A 77 109.211 61.705 7.738 1.00 66.63 C ANISOU 378 CG MET A 77 9473 8117 7724 -51 997 222 C ATOM 379 SD MET A 77 109.439 60.406 8.964 1.00 96.51 S ANISOU 379 SD MET A 77 13463 11950 11256 -94 1042 388 S ATOM 380 CE MET A 77 111.202 60.578 9.235 1.00103.56 C ANISOU 380 CE MET A 77 14424 12894 12031 4 818 432 C ATOM 381 N LEU A 78 105.275 63.717 6.324 1.00 42.45 N ANISOU 381 N LEU A 78 5959 4989 5181 -86 1303 -202 N ATOM 382 CA LEU A 78 103.940 63.837 5.754 1.00 58.04 C ANISOU 382 CA LEU A 78 7780 6940 7333 -90 1388 -301 C ATOM 383 C LEU A 78 103.972 64.611 4.447 1.00 58.90 C ANISOU 383 C LEU A 78 7781 6962 7638 8 1252 -340 C ATOM 384 O LEU A 78 103.361 64.200 3.455 1.00 60.84 O ANISOU 384 O LEU A 78 7932 7162 8024 21 1234 -328 O ATOM 385 CB LEU A 78 103.006 64.519 6.752 1.00 41.06 C ANISOU 385 CB LEU A 78 5574 4875 5152 -122 1542 -472 C ATOM 386 CG LEU A 78 101.600 64.782 6.213 1.00 60.97 C ANISOU 386 CG LEU A 78 7902 7385 7877 -109 1622 -611 C ATOM 387 CD1 LEU A 78 100.875 63.477 5.906 1.00 59.31 C ANISOU 387 CD1 LEU A 78 7654 7174 7707 -200 1719 -542 C ATOM 388 CD2 LEU A 78 100.801 65.646 7.174 1.00 58.38 C ANISOU 388 CD2 LEU A 78 7503 7141 7536 -117 1761 -812 C ATOM 389 N ASN A 79 104.658 65.756 4.438 1.00 41.94 N ANISOU 389 N ASN A 79 5651 4790 5496 73 1156 -391 N ATOM 390 CA ASN A 79 104.740 66.537 3.234 1.00 55.17 C ANISOU 390 CA ASN A 79 7256 6370 7336 159 1031 -406 C ATOM 391 C ASN A 79 105.427 65.749 2.147 1.00 44.91 C ANISOU 391 C ASN A 79 5985 5023 6055 164 926 -258 C ATOM 392 O ASN A 79 105.072 65.841 0.991 1.00 43.89 O ANISOU 392 O ASN A 79 5783 4836 6056 211 860 -247 O ATOM 393 CB ASN A 79 105.421 67.866 3.505 1.00 35.41 C ANISOU 393 CB ASN A 79 4788 3833 4831 204 964 -481 C ATOM 394 CG ASN A 79 104.500 68.837 4.186 1.00 48.80 C ANISOU 394 CG ASN A 79 6414 5542 6586 231 1052 -665 C ATOM 395 OD1 ASN A 79 103.787 69.579 3.541 1.00 56.45 O ANISOU 395 OD1 ASN A 79 7287 6436 7727 309 1022 -743 O ATOM 396 ND2 ASN A 79 104.537 68.857 5.493 1.00 52.41 N ANISOU 396 ND2 ASN A 79 6922 6095 6897 176 1154 -739 N ATOM 397 N LEU A 80 106.454 64.978 2.511 1.00 34.05 N ANISOU 397 N LEU A 80 4719 3676 4544 123 901 -147 N ATOM 398 CA LEU A 80 107.181 64.202 1.511 1.00 45.02 C ANISOU 398 CA LEU A 80 6129 5022 5953 133 807 -25 C ATOM 399 C LEU A 80 106.314 63.090 0.939 1.00 43.58 C ANISOU 399 C LEU A 80 5894 4825 5841 104 859 11 C ATOM 400 O LEU A 80 106.317 62.850 -0.274 1.00 38.86 O ANISOU 400 O LEU A 80 5246 4182 5338 132 786 43 O ATOM 401 CB LEU A 80 108.457 63.635 2.127 1.00 46.40 C ANISOU 401 CB LEU A 80 6419 5232 5978 114 763 66 C ATOM 402 CG LEU A 80 109.315 62.735 1.244 1.00 34.42 C ANISOU 402 CG LEU A 80 4923 3678 4475 129 675 178 C ATOM 403 CD1 LEU A 80 109.769 63.463 0.003 1.00 45.77 C ANISOU 403 CD1 LEU A 80 6304 5069 6016 170 578 166 C ATOM 404 CD2 LEU A 80 110.505 62.214 2.043 1.00 37.05 C ANISOU 404 CD2 LEU A 80 5359 4055 4664 129 626 250 C ATOM 405 N ALA A 81 105.551 62.416 1.798 1.00 42.33 N ANISOU 405 N ALA A 81 5744 4706 5632 36 993 -1 N ATOM 406 CA ALA A 81 104.667 61.357 1.335 1.00 46.51 C ANISOU 406 CA ALA A 81 6215 5216 6241 -14 1061 14 C ATOM 407 C ALA A 81 103.553 61.915 0.457 1.00 41.57 C ANISOU 407 C ALA A 81 5426 4581 5788 24 1052 -101 C ATOM 408 O ALA A 81 103.197 61.308 -0.558 1.00 47.34 O ANISOU 408 O ALA A 81 6088 5281 6617 24 1014 -89 O ATOM 409 CB ALA A 81 104.098 60.597 2.533 1.00 35.02 C ANISOU 409 CB ALA A 81 4816 3802 4687 -115 1227 26 C ATOM 410 N ILE A 82 103.006 63.079 0.816 1.00 40.84 N ANISOU 410 N ILE A 82 5266 4514 5736 67 1075 -221 N ATOM 411 CA ILE A 82 101.973 63.690 -0.014 1.00 42.98 C ANISOU 411 CA ILE A 82 5379 4773 6178 133 1039 -331 C ATOM 412 C ILE A 82 102.540 64.068 -1.379 1.00 50.88 C ANISOU 412 C ILE A 82 6381 5710 7241 218 865 -271 C ATOM 413 O ILE A 82 101.908 63.828 -2.417 1.00 51.68 O ANISOU 413 O ILE A 82 6385 5801 7449 249 807 -291 O ATOM 414 CB ILE A 82 101.347 64.900 0.703 1.00 52.63 C ANISOU 414 CB ILE A 82 6537 6021 7439 179 1092 -480 C ATOM 415 CG1 ILE A 82 100.613 64.451 1.969 1.00 59.37 C ANISOU 415 CG1 ILE A 82 7370 6960 8228 80 1290 -558 C ATOM 416 CG2 ILE A 82 100.386 65.613 -0.223 1.00 54.67 C ANISOU 416 CG2 ILE A 82 6638 6251 7884 282 1017 -584 C ATOM 417 CD1 ILE A 82 100.185 65.587 2.865 1.00 74.24 C ANISOU 417 CD1 ILE A 82 9210 8881 10115 115 1362 -714 C ATOM 418 N SER A 83 103.742 64.654 -1.406 1.00 44.80 N ANISOU 418 N SER A 83 5720 4904 6397 249 781 -201 N ATOM 419 CA SER A 83 104.353 64.993 -2.688 1.00 37.10 C ANISOU 419 CA SER A 83 4762 3874 5460 308 638 -134 C ATOM 420 C SER A 83 104.567 63.745 -3.537 1.00 48.47 C ANISOU 420 C SER A 83 6203 5321 6893 272 609 -54 C ATOM 421 O SER A 83 104.196 63.708 -4.722 1.00 41.56 O ANISOU 421 O SER A 83 5267 4434 6091 313 529 -55 O ATOM 422 CB SER A 83 105.674 65.727 -2.462 1.00 40.05 C ANISOU 422 CB SER A 83 5247 4216 5755 315 582 -82 C ATOM 423 OG SER A 83 106.282 66.074 -3.698 1.00 53.07 O ANISOU 423 OG SER A 83 6918 5815 7430 352 467 -15 O ATOM 424 N ASN A 84 105.153 62.700 -2.941 1.00 39.93 N ANISOU 424 N ASN A 84 5195 4257 5721 202 667 11 N ATOM 425 CA ASN A 84 105.408 61.484 -3.702 1.00 51.63 C ANISOU 425 CA ASN A 84 6682 5727 7208 172 643 75 C ATOM 426 C ASN A 84 104.118 60.849 -4.192 1.00 46.87 C ANISOU 426 C ASN A 84 5962 5134 6711 147 684 6 C ATOM 427 O ASN A 84 104.090 60.295 -5.288 1.00 44.79 O ANISOU 427 O ASN A 84 5663 4862 6494 153 621 15 O ATOM 428 CB ASN A 84 106.190 60.461 -2.879 1.00 46.62 C ANISOU 428 CB ASN A 84 6153 5088 6471 115 696 158 C ATOM 429 CG ASN A 84 107.552 60.957 -2.468 1.00 46.51 C ANISOU 429 CG ASN A 84 6234 5080 6357 142 635 214 C ATOM 430 OD1 ASN A 84 107.913 60.901 -1.295 1.00 71.79 O ANISOU 430 OD1 ASN A 84 9512 8307 9460 120 680 236 O ATOM 431 ND2 ASN A 84 108.298 61.498 -3.422 1.00 46.36 N ANISOU 431 ND2 ASN A 84 6209 5049 6356 186 533 229 N ATOM 432 N LEU A 85 103.046 60.917 -3.404 1.00 45.51 N ANISOU 432 N LEU A 85 5721 4991 6578 111 794 -78 N ATOM 433 CA LEU A 85 101.792 60.295 -3.810 1.00 51.11 C ANISOU 433 CA LEU A 85 6295 5721 7403 72 844 -166 C ATOM 434 C LEU A 85 101.144 61.061 -4.957 1.00 55.75 C ANISOU 434 C LEU A 85 6759 6325 8100 168 722 -245 C ATOM 435 O LEU A 85 100.622 60.452 -5.902 1.00 56.20 O ANISOU 435 O LEU A 85 6727 6395 8231 162 676 -283 O ATOM 436 CB LEU A 85 100.850 60.207 -2.609 1.00 45.70 C ANISOU 436 CB LEU A 85 5560 5076 6728 -3 1013 -247 C ATOM 437 CG LEU A 85 99.575 59.396 -2.796 1.00 60.99 C ANISOU 437 CG LEU A 85 7352 7038 8783 -84 1107 -347 C ATOM 438 CD1 LEU A 85 99.929 57.958 -3.135 1.00 51.76 C ANISOU 438 CD1 LEU A 85 6250 5814 7604 -173 1129 -264 C ATOM 439 CD2 LEU A 85 98.737 59.451 -1.526 1.00 61.85 C ANISOU 439 CD2 LEU A 85 7418 7199 8884 -168 1296 -430 C ATOM 440 N LEU A 86 101.173 62.398 -4.891 1.00 51.33 N ANISOU 440 N LEU A 86 6196 5758 7549 261 661 -271 N ATOM 441 CA LEU A 86 100.717 63.202 -6.021 1.00 39.13 C ANISOU 441 CA LEU A 86 4571 4208 6089 373 519 -311 C ATOM 442 C LEU A 86 101.479 62.836 -7.287 1.00 36.40 C ANISOU 442 C LEU A 86 4288 3847 5695 390 396 -216 C ATOM 443 O LEU A 86 100.885 62.680 -8.360 1.00 39.48 O ANISOU 443 O LEU A 86 4593 4265 6142 432 304 -254 O ATOM 444 CB LEU A 86 100.879 64.692 -5.712 1.00 50.32 C ANISOU 444 CB LEU A 86 6022 5581 7515 468 472 -325 C ATOM 445 CG LEU A 86 99.968 65.289 -4.638 1.00 54.02 C ANISOU 445 CG LEU A 86 6401 6071 8054 483 574 -459 C ATOM 446 CD1 LEU A 86 100.361 66.733 -4.365 1.00 46.60 C ANISOU 446 CD1 LEU A 86 5525 5061 7119 573 520 -466 C ATOM 447 CD2 LEU A 86 98.504 65.187 -5.051 1.00 47.35 C ANISOU 447 CD2 LEU A 86 5356 5278 7358 528 564 -598 C ATOM 448 N PHE A 87 102.800 62.681 -7.177 1.00 45.12 N ANISOU 448 N PHE A 87 5532 4920 6690 357 394 -105 N ATOM 449 CA PHE A 87 103.583 62.259 -8.337 1.00 41.90 C ANISOU 449 CA PHE A 87 5178 4511 6231 360 303 -30 C ATOM 450 C PHE A 87 103.190 60.865 -8.812 1.00 42.90 C ANISOU 450 C PHE A 87 5244 4667 6389 299 328 -64 C ATOM 451 O PHE A 87 103.014 60.636 -10.014 1.00 39.52 O ANISOU 451 O PHE A 87 4776 4267 5973 325 237 -80 O ATOM 452 CB PHE A 87 105.068 62.306 -8.010 1.00 33.45 C ANISOU 452 CB PHE A 87 4242 3412 5055 332 312 70 C ATOM 453 CG PHE A 87 105.942 61.637 -9.037 1.00 28.85 C ANISOU 453 CG PHE A 87 3703 2840 4420 316 256 127 C ATOM 454 CD1 PHE A 87 106.089 62.177 -10.298 1.00 39.54 C ANISOU 454 CD1 PHE A 87 5065 4206 5754 362 152 150 C ATOM 455 CD2 PHE A 87 106.640 60.474 -8.725 1.00 28.42 C ANISOU 455 CD2 PHE A 87 3689 2782 4329 258 309 159 C ATOM 456 CE1 PHE A 87 106.894 61.558 -11.241 1.00 43.67 C ANISOU 456 CE1 PHE A 87 5622 4754 6216 340 118 186 C ATOM 457 CE2 PHE A 87 107.457 59.857 -9.658 1.00 46.46 C ANISOU 457 CE2 PHE A 87 5998 5077 6575 250 264 188 C ATOM 458 CZ PHE A 87 107.585 60.398 -10.915 1.00 38.94 C ANISOU 458 CZ PHE A 87 5042 4155 5598 285 177 193 C ATOM 459 N ILE A 88 103.071 59.915 -7.881 1.00 40.23 N ANISOU 459 N ILE A 88 4911 4318 6058 212 452 -73 N ATOM 460 CA ILE A 88 102.757 58.528 -8.224 1.00 42.02 C ANISOU 460 CA ILE A 88 5097 4540 6328 137 493 -103 C ATOM 461 C ILE A 88 101.435 58.444 -8.974 1.00 53.14 C ANISOU 461 C ILE A 88 6344 6000 7849 146 456 -228 C ATOM 462 O ILE A 88 101.263 57.614 -9.875 1.00 40.15 O ANISOU 462 O ILE A 88 4652 4367 6237 119 416 -271 O ATOM 463 CB ILE A 88 102.756 57.658 -6.950 1.00 48.66 C ANISOU 463 CB ILE A 88 5991 5341 7156 39 645 -76 C ATOM 464 CG1 ILE A 88 104.187 57.432 -6.455 1.00 45.28 C ANISOU 464 CG1 ILE A 88 5720 4869 6615 41 643 48 C ATOM 465 CG2 ILE A 88 102.037 56.348 -7.161 1.00 34.67 C ANISOU 465 CG2 ILE A 88 4155 3546 5471 -54 715 -134 C ATOM 466 CD1 ILE A 88 104.261 56.806 -5.091 1.00 53.37 C ANISOU 466 CD1 ILE A 88 6830 5858 7592 -31 769 100 C ATOM 467 N SER A 89 100.492 59.327 -8.642 1.00 44.20 N ANISOU 467 N SER A 89 5113 4901 6780 193 459 -306 N ATOM 468 CA SER A 89 99.202 59.303 -9.324 1.00 49.80 C ANISOU 468 CA SER A 89 5643 5673 7607 218 407 -442 C ATOM 469 C SER A 89 99.315 59.597 -10.824 1.00 55.14 C ANISOU 469 C SER A 89 6305 6385 8261 309 222 -438 C ATOM 470 O SER A 89 98.390 59.270 -11.574 1.00 43.93 O ANISOU 470 O SER A 89 4744 5028 6919 320 157 -550 O ATOM 471 CB SER A 89 98.238 60.288 -8.658 1.00 45.11 C ANISOU 471 CB SER A 89 4939 5108 7094 274 436 -535 C ATOM 472 OG SER A 89 98.665 61.623 -8.844 1.00 61.61 O ANISOU 472 OG SER A 89 7094 7172 9142 400 328 -478 O ATOM 473 N THR A 90 100.425 60.183 -11.288 1.00 35.34 N ANISOU 473 N THR A 90 3939 3849 5640 367 139 -316 N ATOM 474 CA THR A 90 100.600 60.443 -12.717 1.00 42.10 C ANISOU 474 CA THR A 90 4810 4746 6442 439 -21 -295 C ATOM 475 C THR A 90 101.255 59.284 -13.459 1.00 49.16 C ANISOU 475 C THR A 90 5746 5656 7276 368 -22 -284 C ATOM 476 O THR A 90 101.187 59.235 -14.693 1.00 45.62 O ANISOU 476 O THR A 90 5283 5269 6783 407 -141 -305 O ATOM 477 CB THR A 90 101.450 61.699 -12.940 1.00 35.90 C ANISOU 477 CB THR A 90 4158 3921 5563 520 -97 -173 C ATOM 478 OG1 THR A 90 102.795 61.444 -12.515 1.00 35.04 O ANISOU 478 OG1 THR A 90 4184 3765 5364 455 -21 -73 O ATOM 479 CG2 THR A 90 100.884 62.872 -12.148 1.00 38.02 C ANISOU 479 CG2 THR A 90 4396 4148 5901 595 -92 -193 C ATOM 480 N LEU A 91 101.876 58.354 -12.735 1.00 38.20 N ANISOU 480 N LEU A 91 4415 4215 5884 273 103 -255 N ATOM 481 CA LEU A 91 102.614 57.275 -13.387 1.00 42.88 C ANISOU 481 CA LEU A 91 5055 4802 6434 220 105 -249 C ATOM 482 C LEU A 91 101.762 56.381 -14.281 1.00 58.96 C ANISOU 482 C LEU A 91 6973 6892 8538 186 64 -382 C ATOM 483 O LEU A 91 102.292 55.916 -15.308 1.00 64.01 O ANISOU 483 O LEU A 91 7642 7564 9114 186 2 -396 O ATOM 484 CB LEU A 91 103.340 56.430 -12.333 1.00 32.00 C ANISOU 484 CB LEU A 91 3760 3339 5060 142 237 -192 C ATOM 485 CG LEU A 91 104.435 57.156 -11.563 1.00 48.49 C ANISOU 485 CG LEU A 91 5971 5390 7062 171 260 -71 C ATOM 486 CD1 LEU A 91 105.015 56.235 -10.494 1.00 33.42 C ANISOU 486 CD1 LEU A 91 4137 3406 5154 107 371 -20 C ATOM 487 CD2 LEU A 91 105.504 57.664 -12.517 1.00 43.15 C ANISOU 487 CD2 LEU A 91 5366 4745 6284 221 169 -12 C ATOM 488 N PRO A 92 100.488 56.071 -13.972 1.00 52.32 N ANISOU 488 N PRO A 92 5988 6070 7822 147 101 -501 N ATOM 489 CA PRO A 92 99.688 55.299 -14.941 1.00 48.79 C ANISOU 489 CA PRO A 92 5412 5688 7440 115 41 -650 C ATOM 490 C PRO A 92 99.595 55.958 -16.308 1.00 50.71 C ANISOU 490 C PRO A 92 5635 6040 7595 221 -148 -671 C ATOM 491 O PRO A 92 99.564 55.262 -17.330 1.00 54.79 O ANISOU 491 O PRO A 92 6117 6613 8086 199 -214 -756 O ATOM 492 CB PRO A 92 98.319 55.193 -14.253 1.00 45.41 C ANISOU 492 CB PRO A 92 4816 5273 7163 66 112 -772 C ATOM 493 CG PRO A 92 98.633 55.262 -12.814 1.00 53.54 C ANISOU 493 CG PRO A 92 5928 6213 8202 14 272 -680 C ATOM 494 CD PRO A 92 99.757 56.250 -12.701 1.00 47.80 C ANISOU 494 CD PRO A 92 5357 5465 7341 108 220 -524 C ATOM 495 N PHE A 93 99.589 57.290 -16.356 1.00 48.09 N ANISOU 495 N PHE A 93 5337 5731 7204 335 -237 -591 N ATOM 496 CA PHE A 93 99.516 57.976 -17.642 1.00 44.25 C ANISOU 496 CA PHE A 93 4864 5337 6614 440 -421 -580 C ATOM 497 C PHE A 93 100.817 57.821 -18.422 1.00 44.66 C ANISOU 497 C PHE A 93 5073 5394 6501 427 -440 -484 C ATOM 498 O PHE A 93 100.798 57.559 -19.631 1.00 41.24 O ANISOU 498 O PHE A 93 4635 5055 5979 444 -546 -533 O ATOM 499 CB PHE A 93 99.185 59.448 -17.417 1.00 45.74 C ANISOU 499 CB PHE A 93 5068 5513 6798 566 -503 -507 C ATOM 500 CG PHE A 93 97.852 59.669 -16.764 1.00 52.46 C ANISOU 500 CG PHE A 93 5738 6379 7814 597 -495 -629 C ATOM 501 CD1 PHE A 93 96.690 59.727 -17.514 1.00 52.01 C ANISOU 501 CD1 PHE A 93 5517 6426 7817 670 -639 -763 C ATOM 502 CD2 PHE A 93 97.758 59.782 -15.388 1.00 47.66 C ANISOU 502 CD2 PHE A 93 5115 5696 7299 550 -339 -626 C ATOM 503 CE1 PHE A 93 95.463 59.920 -16.901 1.00 59.32 C ANISOU 503 CE1 PHE A 93 6249 7377 8912 698 -623 -898 C ATOM 504 CE2 PHE A 93 96.533 59.972 -14.774 1.00 48.76 C ANISOU 504 CE2 PHE A 93 5076 5861 7590 568 -309 -756 C ATOM 505 CZ PHE A 93 95.387 60.041 -15.533 1.00 70.85 C ANISOU 505 CZ PHE A 93 7693 8760 10466 642 -448 -897 C ATOM 506 N ARG A 94 101.959 57.975 -17.747 1.00 38.26 N ANISOU 506 N ARG A 94 4393 4498 5645 395 -338 -362 N ATOM 507 CA ARG A 94 103.243 57.710 -18.387 1.00 45.79 C ANISOU 507 CA ARG A 94 5469 5461 6466 368 -329 -296 C ATOM 508 C ARG A 94 103.322 56.275 -18.897 1.00 49.18 C ANISOU 508 C ARG A 94 5850 5916 6919 291 -295 -415 C ATOM 509 O ARG A 94 103.760 56.037 -20.026 1.00 54.53 O ANISOU 509 O ARG A 94 6562 6674 7485 293 -355 -443 O ATOM 510 CB ARG A 94 104.384 58.003 -17.411 1.00 39.63 C ANISOU 510 CB ARG A 94 4801 4588 5668 343 -220 -175 C ATOM 511 CG ARG A 94 104.605 59.487 -17.157 1.00 40.74 C ANISOU 511 CG ARG A 94 5021 4701 5759 410 -260 -57 C ATOM 512 CD ARG A 94 105.692 59.724 -16.119 1.00 41.95 C ANISOU 512 CD ARG A 94 5262 4772 5903 375 -155 33 C ATOM 513 NE ARG A 94 105.954 61.145 -15.914 1.00 61.58 N ANISOU 513 NE ARG A 94 7827 7220 8351 425 -188 131 N ATOM 514 CZ ARG A 94 106.872 61.824 -16.593 1.00 69.39 C ANISOU 514 CZ ARG A 94 8922 8217 9226 427 -219 220 C ATOM 515 NH1 ARG A 94 107.061 63.116 -16.362 1.00 75.58 N ANISOU 515 NH1 ARG A 94 9782 8941 9994 462 -241 305 N ATOM 516 NH2 ARG A 94 107.605 61.201 -17.506 1.00 61.49 N ANISOU 516 NH2 ARG A 94 7951 7281 8131 385 -217 214 N ATOM 517 N ALA A 95 102.884 55.307 -18.088 1.00 48.66 N ANISOU 517 N ALA A 95 5711 5782 6997 218 -193 -492 N ATOM 518 CA ALA A 95 102.928 53.906 -18.504 1.00 40.05 C ANISOU 518 CA ALA A 95 4578 4680 5957 139 -153 -613 C ATOM 519 C ALA A 95 102.035 53.660 -19.715 1.00 41.85 C ANISOU 519 C ALA A 95 4697 5031 6174 149 -273 -764 C ATOM 520 O ALA A 95 102.430 52.956 -20.652 1.00 36.30 O ANISOU 520 O ALA A 95 4004 4376 5412 123 -301 -845 O ATOM 521 CB ALA A 95 102.521 53.000 -17.340 1.00 36.18 C ANISOU 521 CB ALA A 95 4047 4070 5629 50 -15 -648 C ATOM 522 N ASP A 96 100.818 54.218 -19.697 1.00 44.08 N ANISOU 522 N ASP A 96 4863 5372 6514 189 -350 -819 N ATOM 523 CA ASP A 96 99.914 54.160 -20.844 1.00 44.47 C ANISOU 523 CA ASP A 96 4797 5559 6539 222 -500 -961 C ATOM 524 C ASP A 96 100.579 54.708 -22.102 1.00 53.55 C ANISOU 524 C ASP A 96 6055 6818 7474 296 -629 -902 C ATOM 525 O ASP A 96 100.537 54.074 -23.166 1.00 50.05 O ANISOU 525 O ASP A 96 5583 6473 6960 275 -698 -1021 O ATOM 526 CB ASP A 96 98.622 54.920 -20.499 1.00 52.09 C ANISOU 526 CB ASP A 96 5624 6566 7600 286 -573 -1004 C ATOM 527 CG ASP A 96 97.597 54.949 -21.638 1.00 70.43 C ANISOU 527 CG ASP A 96 7807 9047 9905 343 -759 -1158 C ATOM 528 OD1 ASP A 96 97.919 54.614 -22.793 1.00 96.08 O ANISOU 528 OD1 ASP A 96 11095 12391 13022 348 -853 -1205 O ATOM 529 OD2 ASP A 96 96.430 55.295 -21.361 1.00 96.43 O ANISOU 529 OD2 ASP A 96 10939 12382 13319 384 -813 -1247 O ATOM 530 N TYR A 97 101.205 55.883 -21.995 1.00 52.91 N ANISOU 530 N TYR A 97 6103 6721 7280 372 -655 -722 N ATOM 531 CA TYR A 97 101.869 56.489 -23.147 1.00 48.47 C ANISOU 531 CA TYR A 97 5665 6252 6499 426 -756 -641 C ATOM 532 C TYR A 97 102.808 55.506 -23.834 1.00 54.39 C ANISOU 532 C TYR A 97 6467 7039 7159 348 -695 -704 C ATOM 533 O TYR A 97 102.778 55.352 -25.059 1.00 53.84 O ANISOU 533 O TYR A 97 6409 7105 6944 360 -794 -772 O ATOM 534 CB TYR A 97 102.629 57.745 -22.713 1.00 42.34 C ANISOU 534 CB TYR A 97 5036 5405 5646 478 -735 -434 C ATOM 535 CG TYR A 97 103.480 58.353 -23.803 1.00 45.40 C ANISOU 535 CG TYR A 97 5576 5868 5805 501 -795 -328 C ATOM 536 CD1 TYR A 97 102.914 59.081 -24.837 1.00 48.70 C ANISOU 536 CD1 TYR A 97 6029 6390 6085 590 -970 -297 C ATOM 537 CD2 TYR A 97 104.859 58.197 -23.792 1.00 48.68 C ANISOU 537 CD2 TYR A 97 6104 6255 6139 433 -677 -259 C ATOM 538 CE1 TYR A 97 103.702 59.636 -25.832 1.00 51.23 C ANISOU 538 CE1 TYR A 97 6511 6778 6174 596 -1008 -184 C ATOM 539 CE2 TYR A 97 105.651 58.746 -24.781 1.00 49.33 C ANISOU 539 CE2 TYR A 97 6321 6412 6009 432 -705 -168 C ATOM 540 CZ TYR A 97 105.069 59.464 -25.796 1.00 54.82 C ANISOU 540 CZ TYR A 97 7070 7205 6553 506 -863 -123 C ATOM 541 OH TYR A 97 105.862 60.013 -26.774 1.00 58.99 O ANISOU 541 OH TYR A 97 7755 7807 6852 490 -876 -18 O ATOM 542 N TYR A 98 103.645 54.822 -23.059 1.00 36.88 N ANISOU 542 N TYR A 98 4281 4709 5024 275 -539 -690 N ATOM 543 CA TYR A 98 104.623 53.933 -23.671 1.00 49.97 C ANISOU 543 CA TYR A 98 5983 6390 6612 218 -478 -755 C ATOM 544 C TYR A 98 103.987 52.621 -24.115 1.00 53.92 C ANISOU 544 C TYR A 98 6366 6917 7206 159 -484 -971 C ATOM 545 O TYR A 98 104.389 52.055 -25.139 1.00 49.19 O ANISOU 545 O TYR A 98 5778 6407 6504 136 -505 -1077 O ATOM 546 CB TYR A 98 105.782 53.685 -22.706 1.00 45.95 C ANISOU 546 CB TYR A 98 5545 5749 6164 184 -330 -666 C ATOM 547 CG TYR A 98 106.587 54.931 -22.408 1.00 51.12 C ANISOU 547 CG TYR A 98 6316 6392 6716 224 -319 -480 C ATOM 548 CD1 TYR A 98 107.492 55.431 -23.331 1.00 42.85 C ANISOU 548 CD1 TYR A 98 5364 5437 5482 228 -335 -426 C ATOM 549 CD2 TYR A 98 106.455 55.594 -21.196 1.00 49.04 C ANISOU 549 CD2 TYR A 98 6066 6025 6541 244 -281 -369 C ATOM 550 CE1 TYR A 98 108.235 56.567 -23.062 1.00 47.14 C ANISOU 550 CE1 TYR A 98 6011 5956 5946 244 -313 -263 C ATOM 551 CE2 TYR A 98 107.192 56.733 -20.912 1.00 50.39 C ANISOU 551 CE2 TYR A 98 6339 6175 6632 271 -270 -218 C ATOM 552 CZ TYR A 98 108.082 57.215 -21.848 1.00 53.61 C ANISOU 552 CZ TYR A 98 6838 6662 6871 266 -285 -164 C ATOM 553 OH TYR A 98 108.821 58.342 -21.567 1.00 58.33 O ANISOU 553 OH TYR A 98 7534 7226 7403 273 -262 -20 O ATOM 554 N LEU A 99 102.980 52.135 -23.384 1.00 39.39 N ANISOU 554 N LEU A 99 4407 5001 5557 123 -459 -1051 N ATOM 555 CA LEU A 99 102.276 50.929 -23.806 1.00 40.80 C ANISOU 555 CA LEU A 99 4463 5195 5843 51 -464 -1269 C ATOM 556 C LEU A 99 101.542 51.122 -25.125 1.00 54.49 C ANISOU 556 C LEU A 99 6126 7123 7455 88 -636 -1397 C ATOM 557 O LEU A 99 101.271 50.134 -25.817 1.00 57.78 O ANISOU 557 O LEU A 99 6467 7588 7898 29 -655 -1596 O ATOM 558 CB LEU A 99 101.287 50.482 -22.727 1.00 48.60 C ANISOU 558 CB LEU A 99 5337 6070 7060 -12 -389 -1321 C ATOM 559 CG LEU A 99 101.881 49.866 -21.460 1.00 40.83 C ANISOU 559 CG LEU A 99 4418 4887 6209 -76 -213 -1238 C ATOM 560 CD1 LEU A 99 100.817 49.685 -20.396 1.00 38.92 C ANISOU 560 CD1 LEU A 99 4078 4559 6151 -139 -137 -1262 C ATOM 561 CD2 LEU A 99 102.520 48.538 -21.794 1.00 39.07 C ANISOU 561 CD2 LEU A 99 4222 4584 6038 -144 -142 -1347 C ATOM 562 N ARG A 100 101.203 52.363 -25.479 1.00 52.02 N ANISOU 562 N ARG A 100 5841 6915 7010 189 -770 -1292 N ATOM 563 CA ARG A 100 100.583 52.653 -26.766 1.00 61.59 C ANISOU 563 CA ARG A 100 7013 8322 8067 248 -959 -1383 C ATOM 564 C ARG A 100 101.597 52.875 -27.876 1.00 56.99 C ANISOU 564 C ARG A 100 6581 7852 7220 267 -994 -1330 C ATOM 565 O ARG A 100 101.217 53.308 -28.967 1.00 55.67 O ANISOU 565 O ARG A 100 6429 7856 6867 328 -1159 -1357 O ATOM 566 CB ARG A 100 99.680 53.885 -26.664 1.00 72.94 C ANISOU 566 CB ARG A 100 8415 9811 9487 365 -1106 -1292 C ATOM 567 CG ARG A 100 98.450 53.700 -25.815 1.00 73.29 C ANISOU 567 CG ARG A 100 8270 9804 9774 352 -1099 -1396 C ATOM 568 CD ARG A 100 97.537 54.920 -25.857 1.00 74.23 C ANISOU 568 CD ARG A 100 8336 9990 9879 493 -1267 -1336 C ATOM 569 NE ARG A 100 96.422 54.753 -24.930 1.00 74.57 N ANISOU 569 NE ARG A 100 8182 9983 10168 472 -1227 -1446 N ATOM 570 CZ ARG A 100 95.303 54.099 -25.225 1.00 82.54 C ANISOU 570 CZ ARG A 100 8978 11085 11299 437 -1296 -1677 C ATOM 571 NH1 ARG A 100 95.155 53.546 -26.421 1.00 84.25 N ANISOU 571 NH1 ARG A 100 9158 11448 11407 427 -1423 -1824 N ATOM 572 NH2 ARG A 100 94.335 53.983 -24.325 1.00108.30 N ANISOU 572 NH2 ARG A 100 12058 14302 14789 401 -1232 -1776 N ATOM 573 N GLY A 101 102.871 52.611 -27.625 1.00 56.48 N ANISOU 573 N GLY A 101 6626 7705 7127 218 -845 -1257 N ATOM 574 CA GLY A 101 103.883 52.914 -28.612 1.00 43.07 C ANISOU 574 CA GLY A 101 5067 6119 5180 225 -851 -1202 C ATOM 575 C GLY A 101 104.187 54.391 -28.719 1.00 55.22 C ANISOU 575 C GLY A 101 6746 7687 6550 301 -910 -968 C ATOM 576 O GLY A 101 104.337 54.911 -29.832 1.00 63.72 O ANISOU 576 O GLY A 101 7918 8914 7380 332 -1006 -929 O ATOM 577 N SER A 102 104.266 55.087 -27.581 1.00 55.58 N ANISOU 577 N SER A 102 6816 7586 6716 328 -854 -810 N ATOM 578 CA SER A 102 104.627 56.505 -27.528 1.00 44.21 C ANISOU 578 CA SER A 102 5515 6128 5153 390 -888 -586 C ATOM 579 C SER A 102 103.597 57.377 -28.246 1.00 46.30 C ANISOU 579 C SER A 102 5792 6496 5307 496 -1095 -544 C ATOM 580 O SER A 102 103.941 58.250 -29.045 1.00 58.93 O ANISOU 580 O SER A 102 7540 8166 6684 536 -1168 -409 O ATOM 581 CB SER A 102 106.029 56.742 -28.094 1.00 40.87 C ANISOU 581 CB SER A 102 5244 5747 4538 340 -797 -495 C ATOM 582 OG SER A 102 107.020 56.107 -27.307 1.00 54.40 O ANISOU 582 OG SER A 102 6943 7354 6372 269 -622 -514 O ATOM 583 N ASN A 103 102.322 57.135 -27.948 1.00 50.15 N ANISOU 583 N ASN A 103 6118 6986 5950 543 -1190 -660 N ATOM 584 CA ASN A 103 101.220 57.983 -28.391 1.00 52.95 C ANISOU 584 CA ASN A 103 6445 7415 6257 670 -1400 -632 C ATOM 585 C ASN A 103 100.522 58.570 -27.172 1.00 53.22 C ANISOU 585 C ASN A 103 6392 7313 6516 730 -1390 -585 C ATOM 586 O ASN A 103 100.134 57.833 -26.259 1.00 65.13 O ANISOU 586 O ASN A 103 7755 8749 8245 669 -1287 -704 O ATOM 587 CB ASN A 103 100.200 57.206 -29.224 1.00 62.22 C ANISOU 587 CB ASN A 103 7467 8753 7421 683 -1547 -855 C ATOM 588 CG ASN A 103 99.216 58.114 -29.928 1.00 66.94 C ANISOU 588 CG ASN A 103 8058 9463 7913 836 -1799 -817 C ATOM 589 OD1 ASN A 103 99.361 59.335 -29.917 1.00 73.99 O ANISOU 589 OD1 ASN A 103 9091 10304 8718 934 -1865 -608 O ATOM 590 ND2 ASN A 103 98.179 57.522 -30.507 1.00 87.21 N ANISOU 590 ND2 ASN A 103 10457 12175 10505 861 -1948 -1027 N ATOM 591 N TRP A 104 100.345 59.888 -27.164 1.00 50.34 N ANISOU 591 N TRP A 104 6121 6909 6096 847 -1493 -417 N ATOM 592 CA TRP A 104 99.680 60.575 -26.065 1.00 51.07 C ANISOU 592 CA TRP A 104 6136 6878 6390 920 -1491 -381 C ATOM 593 C TRP A 104 98.233 60.868 -26.442 1.00 52.53 C ANISOU 593 C TRP A 104 6170 7153 6634 1055 -1706 -483 C ATOM 594 O TRP A 104 97.971 61.471 -27.490 1.00 62.54 O ANISOU 594 O TRP A 104 7516 8519 7728 1165 -1904 -421 O ATOM 595 CB TRP A 104 100.410 61.871 -25.717 1.00 43.52 C ANISOU 595 CB TRP A 104 5371 5793 5373 967 -1461 -147 C ATOM 596 CG TRP A 104 99.923 62.503 -24.461 1.00 51.81 C ANISOU 596 CG TRP A 104 6349 6703 6634 1021 -1418 -126 C ATOM 597 CD1 TRP A 104 99.119 63.597 -24.347 1.00 49.85 C ANISOU 597 CD1 TRP A 104 6087 6407 6445 1173 -1557 -73 C ATOM 598 CD2 TRP A 104 100.219 62.082 -23.126 1.00 45.80 C ANISOU 598 CD2 TRP A 104 5525 5831 6046 927 -1221 -164 C ATOM 599 NE1 TRP A 104 98.896 63.885 -23.021 1.00 42.93 N ANISOU 599 NE1 TRP A 104 5134 5406 5773 1173 -1446 -93 N ATOM 600 CE2 TRP A 104 99.561 62.967 -22.251 1.00 40.98 C ANISOU 600 CE2 TRP A 104 4862 5125 5584 1019 -1239 -142 C ATOM 601 CE3 TRP A 104 100.979 61.041 -22.586 1.00 45.21 C ANISOU 601 CE3 TRP A 104 5439 5729 6010 784 -1037 -213 C ATOM 602 CZ2 TRP A 104 99.637 62.840 -20.865 1.00 53.31 C ANISOU 602 CZ2 TRP A 104 6365 6582 7308 958 -1072 -171 C ATOM 603 CZ3 TRP A 104 101.054 60.917 -21.209 1.00 49.00 C ANISOU 603 CZ3 TRP A 104 5872 6096 6652 734 -886 -222 C ATOM 604 CH2 TRP A 104 100.387 61.811 -20.365 1.00 43.12 C ANISOU 604 CH2 TRP A 104 5080 5275 6030 814 -901 -202 C ATOM 605 N ILE A 105 97.303 60.441 -25.589 1.00 46.17 N ANISOU 605 N ILE A 105 5149 6322 6071 1046 -1668 -640 N ATOM 606 CA ILE A 105 95.875 60.577 -25.862 1.00 64.49 C ANISOU 606 CA ILE A 105 7271 8744 8490 1163 -1857 -786 C ATOM 607 C ILE A 105 95.160 61.432 -24.829 1.00 68.80 C ANISOU 607 C ILE A 105 7721 9184 9237 1262 -1856 -770 C ATOM 608 O ILE A 105 93.933 61.547 -24.891 1.00 70.36 O ANISOU 608 O ILE A 105 7716 9457 9558 1362 -1995 -915 O ATOM 609 CB ILE A 105 95.188 59.201 -25.962 1.00 48.91 C ANISOU 609 CB ILE A 105 5074 6874 6635 1055 -1828 -1051 C ATOM 610 CG1 ILE A 105 95.201 58.499 -24.599 1.00 47.17 C ANISOU 610 CG1 ILE A 105 4750 6525 6646 914 -1582 -1125 C ATOM 611 CG2 ILE A 105 95.853 58.333 -27.011 1.00 49.14 C ANISOU 611 CG2 ILE A 105 5186 7009 6474 963 -1834 -1099 C ATOM 612 CD1 ILE A 105 94.297 57.285 -24.532 1.00 48.15 C ANISOU 612 CD1 ILE A 105 4634 6721 6941 808 -1547 -1388 C ATOM 613 N PHE A 106 95.876 62.032 -23.885 1.00 59.65 N ANISOU 613 N PHE A 106 6686 7861 8118 1240 -1705 -620 N ATOM 614 CA PHE A 106 95.243 62.629 -22.716 1.00 48.93 C ANISOU 614 CA PHE A 106 5217 6403 6973 1297 -1650 -648 C ATOM 615 C PHE A 106 95.082 64.141 -22.806 1.00 53.37 C ANISOU 615 C PHE A 106 5880 6886 7512 1485 -1797 -502 C ATOM 616 O PHE A 106 94.524 64.745 -21.882 1.00 59.42 O ANISOU 616 O PHE A 106 6552 7568 8456 1554 -1764 -538 O ATOM 617 CB PHE A 106 96.027 62.274 -21.448 1.00 45.23 C ANISOU 617 CB PHE A 106 4797 5803 6584 1149 -1384 -608 C ATOM 618 CG PHE A 106 96.077 60.803 -21.169 1.00 55.30 C ANISOU 618 CG PHE A 106 5971 7116 7924 975 -1231 -748 C ATOM 619 CD1 PHE A 106 94.952 60.136 -20.706 1.00 57.68 C ANISOU 619 CD1 PHE A 106 6033 7467 8418 932 -1193 -953 C ATOM 620 CD2 PHE A 106 97.253 60.088 -21.347 1.00 50.70 C ANISOU 620 CD2 PHE A 106 5530 6509 7224 851 -1118 -681 C ATOM 621 CE1 PHE A 106 94.992 58.783 -20.448 1.00 53.88 C ANISOU 621 CE1 PHE A 106 5476 6993 8005 762 -1046 -1072 C ATOM 622 CE2 PHE A 106 97.298 58.734 -21.084 1.00 62.88 C ANISOU 622 CE2 PHE A 106 6992 8058 8842 703 -984 -805 C ATOM 623 CZ PHE A 106 96.165 58.084 -20.632 1.00 47.84 C ANISOU 623 CZ PHE A 106 4869 6183 7124 655 -947 -993 C ATOM 624 N GLY A 107 95.552 64.770 -23.876 1.00 48.41 N ANISOU 624 N GLY A 107 5447 6274 6672 1567 -1949 -340 N ATOM 625 CA GLY A 107 95.363 66.191 -24.026 1.00 55.47 C ANISOU 625 CA GLY A 107 6456 7070 7549 1751 -2101 -191 C ATOM 626 C GLY A 107 96.603 67.001 -23.661 1.00 56.83 C ANISOU 626 C GLY A 107 6887 7068 7638 1702 -1977 35 C ATOM 627 O GLY A 107 97.515 66.519 -22.982 1.00 71.57 O ANISOU 627 O GLY A 107 8801 8881 9510 1538 -1757 51 O ATOM 628 N ASP A 108 96.614 68.253 -24.110 1.00 59.02 N ANISOU 628 N ASP A 108 7329 7249 7845 1851 -2126 206 N ATOM 629 CA ASP A 108 97.803 69.091 -23.977 1.00 53.35 C ANISOU 629 CA ASP A 108 6875 6368 7028 1797 -2028 427 C ATOM 630 C ASP A 108 98.054 69.503 -22.529 1.00 59.78 C ANISOU 630 C ASP A 108 7656 7017 8040 1754 -1846 407 C ATOM 631 O ASP A 108 99.213 69.659 -22.125 1.00 76.04 O ANISOU 631 O ASP A 108 9864 8982 10044 1624 -1680 514 O ATOM 632 CB ASP A 108 97.667 70.308 -24.897 1.00 57.84 C ANISOU 632 CB ASP A 108 7643 6862 7472 1967 -2245 621 C ATOM 633 CG ASP A 108 98.884 71.209 -24.869 1.00 83.30 C ANISOU 633 CG ASP A 108 11151 9910 10590 1894 -2142 854 C ATOM 634 OD1 ASP A 108 99.954 70.806 -25.378 1.00 86.24 O ANISOU 634 OD1 ASP A 108 11665 10335 10766 1735 -2032 942 O ATOM 635 OD2 ASP A 108 98.750 72.344 -24.366 1.00 97.43 O ANISOU 635 OD2 ASP A 108 13014 11504 12500 1998 -2172 938 O ATOM 636 N LEU A 109 96.998 69.651 -21.725 1.00 55.28 N ANISOU 636 N LEU A 109 6882 6425 7696 1853 -1869 254 N ATOM 637 CA LEU A 109 97.187 70.062 -20.334 1.00 57.03 C ANISOU 637 CA LEU A 109 7074 6507 8090 1814 -1696 220 C ATOM 638 C LEU A 109 97.820 68.949 -19.506 1.00 62.01 C ANISOU 638 C LEU A 109 7640 7188 8732 1605 -1456 138 C ATOM 639 O LEU A 109 98.726 69.203 -18.697 1.00 78.88 O ANISOU 639 O LEU A 109 9879 9217 10873 1507 -1295 203 O ATOM 640 CB LEU A 109 95.852 70.489 -19.720 1.00 57.17 C ANISOU 640 CB LEU A 109 6875 6507 8339 1975 -1773 58 C ATOM 641 CG LEU A 109 95.921 70.984 -18.270 1.00 63.57 C ANISOU 641 CG LEU A 109 7646 7186 9324 1950 -1601 -3 C ATOM 642 CD1 LEU A 109 96.833 72.197 -18.170 1.00 53.49 C ANISOU 642 CD1 LEU A 109 6621 5704 7998 1972 -1590 189 C ATOM 643 CD2 LEU A 109 94.534 71.307 -17.710 1.00 70.41 C ANISOU 643 CD2 LEU A 109 8267 8065 10422 2105 -1664 -198 C ATOM 644 N ALA A 110 97.348 67.712 -19.686 1.00 44.50 N ANISOU 644 N ALA A 110 5255 5127 6527 1536 -1437 -10 N ATOM 645 CA ALA A 110 97.905 66.588 -18.942 1.00 41.76 C ANISOU 645 CA ALA A 110 4860 4812 6195 1347 -1222 -78 C ATOM 646 C ALA A 110 99.378 66.385 -19.263 1.00 62.82 C ANISOU 646 C ALA A 110 7733 7453 8684 1223 -1133 71 C ATOM 647 O ALA A 110 100.163 66.036 -18.375 1.00 58.38 O ANISOU 647 O ALA A 110 7203 6838 8139 1102 -955 82 O ATOM 648 CB ALA A 110 97.114 65.316 -19.244 1.00 58.24 C ANISOU 648 CB ALA A 110 6746 7053 8328 1296 -1234 -258 C ATOM 649 N CYS A 111 99.773 66.608 -20.516 1.00 53.32 N ANISOU 649 N CYS A 111 6665 6292 7302 1253 -1255 182 N ATOM 650 CA CYS A 111 101.179 66.479 -20.885 1.00 63.98 C ANISOU 650 CA CYS A 111 8198 7629 8482 1133 -1162 311 C ATOM 651 C CYS A 111 102.033 67.496 -20.137 1.00 50.21 C ANISOU 651 C CYS A 111 6597 5722 6757 1110 -1067 439 C ATOM 652 O CYS A 111 103.116 67.165 -19.640 1.00 51.09 O ANISOU 652 O CYS A 111 6766 5807 6838 980 -912 468 O ATOM 653 CB CYS A 111 101.331 66.643 -22.398 1.00 71.39 C ANISOU 653 CB CYS A 111 9261 8653 9211 1173 -1310 404 C ATOM 654 SG CYS A 111 103.021 66.475 -23.012 1.00 77.39 S ANISOU 654 SG CYS A 111 10228 9427 9750 1017 -1187 541 S ATOM 655 N ARG A 112 101.553 68.739 -20.045 1.00 43.76 N ANISOU 655 N ARG A 112 5833 4791 6002 1240 -1167 506 N ATOM 656 CA ARG A 112 102.238 69.765 -19.263 1.00 62.50 C ANISOU 656 CA ARG A 112 8328 6993 8426 1221 -1081 599 C ATOM 657 C ARG A 112 102.371 69.339 -17.803 1.00 50.48 C ANISOU 657 C ARG A 112 6692 5446 7041 1140 -909 484 C ATOM 658 O ARG A 112 103.452 69.442 -17.198 1.00 61.25 O ANISOU 658 O ARG A 112 8142 6751 8380 1030 -775 532 O ATOM 659 CB ARG A 112 101.453 71.077 -19.368 1.00 58.47 C ANISOU 659 CB ARG A 112 7861 6355 7999 1400 -1232 652 C ATOM 660 CG ARG A 112 101.279 71.588 -20.803 1.00 51.81 C ANISOU 660 CG ARG A 112 7159 5523 7003 1499 -1424 793 C ATOM 661 CD ARG A 112 100.373 72.821 -20.890 1.00 55.95 C ANISOU 661 CD ARG A 112 7715 5910 7634 1708 -1601 839 C ATOM 662 NE ARG A 112 100.088 73.201 -22.275 1.00 69.17 N ANISOU 662 NE ARG A 112 9521 7613 9147 1821 -1810 975 N ATOM 663 CZ ARG A 112 100.831 74.038 -22.993 1.00 72.36 C ANISOU 663 CZ ARG A 112 10192 7904 9398 1806 -1843 1197 C ATOM 664 NH1 ARG A 112 101.911 74.591 -22.458 1.00 66.94 N ANISOU 664 NH1 ARG A 112 9649 7067 8718 1676 -1677 1291 N ATOM 665 NH2 ARG A 112 100.495 74.322 -24.247 1.00 71.33 N ANISOU 665 NH2 ARG A 112 10186 7817 9100 1913 -2040 1323 N ATOM 666 N ILE A 113 101.273 68.843 -17.230 1.00 49.46 N ANISOU 666 N ILE A 113 6367 5373 7051 1189 -911 326 N ATOM 667 CA ILE A 113 101.272 68.438 -15.828 1.00 53.83 C ANISOU 667 CA ILE A 113 6822 5912 7719 1114 -747 220 C ATOM 668 C ILE A 113 102.245 67.288 -15.581 1.00 45.04 C ANISOU 668 C ILE A 113 5729 4863 6523 951 -606 222 C ATOM 669 O ILE A 113 102.837 67.193 -14.504 1.00 42.22 O ANISOU 669 O ILE A 113 5389 4462 6191 871 -470 213 O ATOM 670 CB ILE A 113 99.838 68.088 -15.384 1.00 61.76 C ANISOU 670 CB ILE A 113 7606 6979 8880 1185 -767 45 C ATOM 671 CG1 ILE A 113 98.964 69.343 -15.423 1.00 55.64 C ANISOU 671 CG1 ILE A 113 6805 6120 8216 1365 -898 30 C ATOM 672 CG2 ILE A 113 99.840 67.455 -13.997 1.00 68.71 C ANISOU 672 CG2 ILE A 113 8396 7869 9842 1078 -576 -58 C ATOM 673 CD1 ILE A 113 97.500 69.067 -15.191 1.00 60.58 C ANISOU 673 CD1 ILE A 113 7190 6827 9001 1453 -943 -157 C ATOM 674 N MET A 114 102.434 66.405 -16.564 1.00 35.39 N ANISOU 674 N MET A 114 4506 3743 5198 907 -644 228 N ATOM 675 CA MET A 114 103.420 65.333 -16.418 1.00 43.32 C ANISOU 675 CA MET A 114 5535 4791 6133 771 -522 229 C ATOM 676 C MET A 114 104.785 65.883 -16.017 1.00 43.68 C ANISOU 676 C MET A 114 5726 4758 6111 704 -438 339 C ATOM 677 O MET A 114 105.329 65.532 -14.960 1.00 58.35 O ANISOU 677 O MET A 114 7575 6591 8006 632 -317 316 O ATOM 678 CB MET A 114 103.542 64.541 -17.723 1.00 52.58 C ANISOU 678 CB MET A 114 6714 6075 7191 747 -590 224 C ATOM 679 CG MET A 114 102.285 63.806 -18.168 1.00 46.94 C ANISOU 679 CG MET A 114 5839 5457 6538 789 -671 89 C ATOM 680 SD MET A 114 101.689 62.607 -16.964 1.00 57.45 S ANISOU 680 SD MET A 114 7002 6795 8033 705 -527 -64 S ATOM 681 CE MET A 114 100.272 63.461 -16.280 1.00 40.06 C ANISOU 681 CE MET A 114 4663 4565 5993 816 -574 -147 C ATOM 682 N SER A 115 105.362 66.734 -16.868 1.00 39.40 N ANISOU 682 N SER A 115 5321 4183 5466 721 -502 458 N ATOM 683 CA SER A 115 106.672 67.318 -16.590 1.00 63.96 C ANISOU 683 CA SER A 115 8559 7223 8521 643 -421 551 C ATOM 684 C SER A 115 106.651 68.115 -15.292 1.00 59.43 C ANISOU 684 C SER A 115 7985 6536 8060 656 -364 533 C ATOM 685 O SER A 115 107.569 68.000 -14.455 1.00 56.68 O ANISOU 685 O SER A 115 7655 6169 7712 571 -258 527 O ATOM 686 CB SER A 115 107.100 68.214 -17.757 1.00 70.62 C ANISOU 686 CB SER A 115 9556 8035 9241 654 -496 686 C ATOM 687 OG SER A 115 107.204 67.485 -18.968 1.00 93.04 O ANISOU 687 OG SER A 115 12406 10998 11945 632 -540 696 O ATOM 688 N TYR A 116 105.617 68.949 -15.115 1.00 48.33 N ANISOU 688 N TYR A 116 6553 5059 6750 770 -442 514 N ATOM 689 CA TYR A 116 105.563 69.799 -13.930 1.00 41.47 C ANISOU 689 CA TYR A 116 5688 4080 5990 789 -388 479 C ATOM 690 C TYR A 116 105.624 68.960 -12.659 1.00 53.36 C ANISOU 690 C TYR A 116 7093 5639 7542 721 -262 373 C ATOM 691 O TYR A 116 106.414 69.242 -11.752 1.00 64.40 O ANISOU 691 O TYR A 116 8537 6995 8939 656 -175 371 O ATOM 692 CB TYR A 116 104.298 70.655 -13.952 1.00 42.01 C ANISOU 692 CB TYR A 116 5710 4078 6176 941 -494 441 C ATOM 693 CG TYR A 116 104.230 71.712 -12.867 1.00 58.18 C ANISOU 693 CG TYR A 116 7774 5993 8338 975 -449 397 C ATOM 694 CD1 TYR A 116 104.980 72.879 -12.961 1.00 70.83 C ANISOU 694 CD1 TYR A 116 9533 7447 9931 964 -459 494 C ATOM 695 CD2 TYR A 116 103.404 71.555 -11.762 1.00 60.01 C ANISOU 695 CD2 TYR A 116 7866 6246 8688 1009 -389 249 C ATOM 696 CE1 TYR A 116 104.917 73.854 -11.981 1.00 65.83 C ANISOU 696 CE1 TYR A 116 8916 6686 9413 994 -419 434 C ATOM 697 CE2 TYR A 116 103.335 72.526 -10.776 1.00 49.29 C ANISOU 697 CE2 TYR A 116 6522 4778 7429 1041 -344 188 C ATOM 698 CZ TYR A 116 104.093 73.673 -10.892 1.00 57.16 C ANISOU 698 CZ TYR A 116 7673 5622 8423 1038 -365 275 C ATOM 699 OH TYR A 116 104.029 74.643 -9.918 1.00 54.86 O ANISOU 699 OH TYR A 116 7394 5212 8238 1067 -321 194 O ATOM 700 N SER A 117 104.819 67.899 -12.595 1.00 40.31 N ANISOU 700 N SER A 117 5312 4083 5922 726 -251 286 N ATOM 701 CA SER A 117 104.754 67.075 -11.395 1.00 40.86 C ANISOU 701 CA SER A 117 5303 4193 6027 660 -128 201 C ATOM 702 C SER A 117 106.035 66.280 -11.192 1.00 42.70 C ANISOU 702 C SER A 117 5599 4460 6166 550 -51 250 C ATOM 703 O SER A 117 106.515 66.170 -10.061 1.00 50.37 O ANISOU 703 O SER A 117 6584 5421 7134 499 39 231 O ATOM 704 CB SER A 117 103.554 66.135 -11.466 1.00 40.40 C ANISOU 704 CB SER A 117 5097 4217 6038 676 -127 99 C ATOM 705 OG SER A 117 103.708 65.211 -12.528 1.00 52.57 O ANISOU 705 OG SER A 117 6631 5830 7515 646 -173 120 O ATOM 706 N LEU A 118 106.603 65.709 -12.264 1.00 42.25 N ANISOU 706 N LEU A 118 5575 4450 6026 519 -88 302 N ATOM 707 CA LEU A 118 107.889 65.025 -12.127 1.00 43.76 C ANISOU 707 CA LEU A 118 5815 4670 6141 432 -24 337 C ATOM 708 C LEU A 118 108.894 65.907 -11.403 1.00 45.18 C ANISOU 708 C LEU A 118 6075 4791 6302 398 16 376 C ATOM 709 O LEU A 118 109.423 65.536 -10.346 1.00 42.90 O ANISOU 709 O LEU A 118 5781 4510 6010 356 86 352 O ATOM 710 CB LEU A 118 108.445 64.611 -13.496 1.00 46.24 C ANISOU 710 CB LEU A 118 6163 5040 6366 410 -70 381 C ATOM 711 CG LEU A 118 109.838 63.963 -13.466 1.00 44.90 C ANISOU 711 CG LEU A 118 6026 4903 6130 332 -7 400 C ATOM 712 CD1 LEU A 118 109.837 62.681 -12.652 1.00 42.52 C ANISOU 712 CD1 LEU A 118 5663 4622 5869 307 56 341 C ATOM 713 CD2 LEU A 118 110.394 63.703 -14.865 1.00 54.43 C ANISOU 713 CD2 LEU A 118 7266 6174 7240 307 -39 428 C ATOM 714 N TYR A 119 109.142 67.104 -11.937 1.00 49.08 N ANISOU 714 N TYR A 119 6647 5221 6781 416 -31 436 N ATOM 715 CA TYR A 119 110.250 67.875 -11.377 1.00 32.21 C ANISOU 715 CA TYR A 119 4581 3030 4626 358 12 463 C ATOM 716 C TYR A 119 109.887 68.525 -10.044 1.00 41.62 C ANISOU 716 C TYR A 119 5759 4161 5893 380 48 399 C ATOM 717 O TYR A 119 110.741 68.616 -9.146 1.00 37.18 O ANISOU 717 O TYR A 119 5213 3601 5313 322 102 374 O ATOM 718 CB TYR A 119 110.746 68.899 -12.395 1.00 44.35 C ANISOU 718 CB TYR A 119 6224 4505 6122 342 -29 554 C ATOM 719 CG TYR A 119 111.398 68.214 -13.572 1.00 55.44 C ANISOU 719 CG TYR A 119 7646 5995 7421 291 -32 603 C ATOM 720 CD1 TYR A 119 112.679 67.695 -13.464 1.00 52.84 C ANISOU 720 CD1 TYR A 119 7310 5727 7042 200 36 592 C ATOM 721 CD2 TYR A 119 110.726 68.063 -14.780 1.00 43.60 C ANISOU 721 CD2 TYR A 119 6163 4529 5872 339 -107 644 C ATOM 722 CE1 TYR A 119 113.281 67.056 -14.526 1.00 55.33 C ANISOU 722 CE1 TYR A 119 7628 6128 7266 155 47 613 C ATOM 723 CE2 TYR A 119 111.318 67.427 -15.847 1.00 46.40 C ANISOU 723 CE2 TYR A 119 6535 4977 6117 288 -101 670 C ATOM 724 CZ TYR A 119 112.598 66.923 -15.715 1.00 56.02 C ANISOU 724 CZ TYR A 119 7742 6250 7295 194 -16 651 C ATOM 725 OH TYR A 119 113.201 66.289 -16.778 1.00 63.31 O ANISOU 725 OH TYR A 119 8671 7271 8113 144 3 655 O ATOM 726 N VAL A 120 108.632 68.961 -9.876 1.00 40.13 N ANISOU 726 N VAL A 120 5530 3931 5788 465 16 355 N ATOM 727 CA VAL A 120 108.211 69.480 -8.577 1.00 41.67 C ANISOU 727 CA VAL A 120 5697 4086 6050 486 65 268 C ATOM 728 C VAL A 120 108.401 68.419 -7.501 1.00 53.10 C ANISOU 728 C VAL A 120 7096 5624 7457 430 152 215 C ATOM 729 O VAL A 120 108.989 68.687 -6.447 1.00 42.22 O ANISOU 729 O VAL A 120 5744 4243 6053 389 204 179 O ATOM 730 CB VAL A 120 106.758 69.989 -8.631 1.00 45.39 C ANISOU 730 CB VAL A 120 6103 4515 6630 596 21 207 C ATOM 731 CG1 VAL A 120 106.238 70.273 -7.224 1.00 32.01 C ANISOU 731 CG1 VAL A 120 4353 2813 4995 608 100 87 C ATOM 732 CG2 VAL A 120 106.669 71.259 -9.469 1.00 52.23 C ANISOU 732 CG2 VAL A 120 7050 5256 7539 666 -74 270 C ATOM 733 N ASN A 121 107.928 67.192 -7.756 1.00 36.08 N ANISOU 733 N ASN A 121 4876 3544 5289 425 165 212 N ATOM 734 CA ASN A 121 108.138 66.111 -6.803 1.00 42.30 C ANISOU 734 CA ASN A 121 5644 4395 6031 370 245 189 C ATOM 735 C ASN A 121 109.612 65.931 -6.507 1.00 39.05 C ANISOU 735 C ASN A 121 5301 4002 5536 312 254 235 C ATOM 736 O ASN A 121 110.011 65.870 -5.342 1.00 37.01 O ANISOU 736 O ASN A 121 5064 3763 5234 285 301 210 O ATOM 737 CB ASN A 121 107.593 64.787 -7.325 1.00 49.03 C ANISOU 737 CB ASN A 121 6437 5301 6893 359 254 190 C ATOM 738 CG ASN A 121 107.600 63.710 -6.256 1.00 41.72 C ANISOU 738 CG ASN A 121 5507 4411 5935 306 345 176 C ATOM 739 OD1 ASN A 121 107.626 64.012 -5.066 1.00 64.89 O ANISOU 739 OD1 ASN A 121 8466 7349 8842 290 404 149 O ATOM 740 ND2 ASN A 121 107.721 62.465 -6.671 1.00 69.24 N ANISOU 740 ND2 ASN A 121 8982 7918 9409 275 353 202 N ATOM 741 N MET A 122 110.430 65.803 -7.558 1.00 31.32 N ANISOU 741 N MET A 122 4348 3029 4525 294 207 295 N ATOM 742 CA MET A 122 111.839 65.472 -7.376 1.00 44.88 C ANISOU 742 CA MET A 122 6096 4780 6176 243 214 320 C ATOM 743 C MET A 122 112.524 66.468 -6.450 1.00 59.06 C ANISOU 743 C MET A 122 7929 6552 7959 217 226 290 C ATOM 744 O MET A 122 113.150 66.084 -5.448 1.00 40.47 O ANISOU 744 O MET A 122 5579 4243 5555 196 245 268 O ATOM 745 CB MET A 122 112.532 65.433 -8.736 1.00 47.13 C ANISOU 745 CB MET A 122 6394 5078 6436 222 177 369 C ATOM 746 CG MET A 122 113.965 64.967 -8.691 1.00 42.47 C ANISOU 746 CG MET A 122 5803 4539 5795 175 187 374 C ATOM 747 SD MET A 122 114.654 64.926 -10.345 1.00 45.86 S ANISOU 747 SD MET A 122 6238 5000 6186 139 171 412 S ATOM 748 CE MET A 122 113.756 63.545 -11.051 1.00 54.77 C ANISOU 748 CE MET A 122 7322 6167 7321 183 157 402 C ATOM 749 N TYR A 123 112.386 67.763 -6.750 1.00 31.97 N ANISOU 749 N TYR A 123 4531 3044 4571 221 206 286 N ATOM 750 CA TYR A 123 113.151 68.736 -5.979 1.00 43.20 C ANISOU 750 CA TYR A 123 5988 4434 5992 180 218 243 C ATOM 751 C TYR A 123 112.495 69.046 -4.633 1.00 50.66 C ANISOU 751 C TYR A 123 6925 5375 6948 205 253 159 C ATOM 752 O TYR A 123 113.202 69.333 -3.658 1.00 58.96 O ANISOU 752 O TYR A 123 7990 6452 7959 168 267 103 O ATOM 753 CB TYR A 123 113.399 69.984 -6.823 1.00 29.50 C ANISOU 753 CB TYR A 123 4309 2597 4303 158 193 277 C ATOM 754 CG TYR A 123 114.262 69.632 -8.021 1.00 42.66 C ANISOU 754 CG TYR A 123 5989 4297 5924 107 182 351 C ATOM 755 CD1 TYR A 123 115.603 69.292 -7.855 1.00 34.88 C ANISOU 755 CD1 TYR A 123 4979 3381 4891 33 202 334 C ATOM 756 CD2 TYR A 123 113.744 69.629 -9.308 1.00 45.22 C ANISOU 756 CD2 TYR A 123 6340 4597 6244 134 149 426 C ATOM 757 CE1 TYR A 123 116.397 68.952 -8.932 1.00 42.62 C ANISOU 757 CE1 TYR A 123 5956 4407 5833 -18 208 380 C ATOM 758 CE2 TYR A 123 114.539 69.294 -10.396 1.00 42.54 C ANISOU 758 CE2 TYR A 123 6015 4305 5843 79 153 483 C ATOM 759 CZ TYR A 123 115.862 68.957 -10.197 1.00 45.36 C ANISOU 759 CZ TYR A 123 6340 4731 6163 -1 193 454 C ATOM 760 OH TYR A 123 116.662 68.616 -11.261 1.00 45.55 O ANISOU 760 OH TYR A 123 6363 4814 6129 -60 213 489 O ATOM 761 N SER A 124 111.169 68.919 -4.523 1.00 51.72 N ANISOU 761 N SER A 124 7025 5496 7129 264 272 133 N ATOM 762 CA SER A 124 110.546 68.979 -3.206 1.00 40.23 C ANISOU 762 CA SER A 124 5553 4068 5664 276 331 44 C ATOM 763 C SER A 124 111.019 67.833 -2.321 1.00 45.54 C ANISOU 763 C SER A 124 6232 4845 6227 238 368 55 C ATOM 764 O SER A 124 111.222 68.018 -1.120 1.00 50.22 O ANISOU 764 O SER A 124 6848 5479 6755 218 402 -5 O ATOM 765 CB SER A 124 109.027 68.952 -3.341 1.00 40.49 C ANISOU 765 CB SER A 124 5524 4084 5778 340 355 4 C ATOM 766 OG SER A 124 108.573 70.111 -4.003 1.00 55.11 O ANISOU 766 OG SER A 124 7378 5829 7732 398 305 -11 O ATOM 767 N SER A 125 111.223 66.647 -2.898 1.00 43.65 N ANISOU 767 N SER A 125 5980 4644 5959 232 355 132 N ATOM 768 CA SER A 125 111.705 65.510 -2.116 1.00 49.21 C ANISOU 768 CA SER A 125 6708 5421 6568 210 376 162 C ATOM 769 C SER A 125 113.132 65.739 -1.647 1.00 51.49 C ANISOU 769 C SER A 125 7030 5748 6785 186 329 158 C ATOM 770 O SER A 125 113.472 65.477 -0.483 1.00 55.83 O ANISOU 770 O SER A 125 7615 6357 7239 178 338 141 O ATOM 771 CB SER A 125 111.617 64.224 -2.944 1.00 42.23 C ANISOU 771 CB SER A 125 5804 4542 5698 215 368 233 C ATOM 772 OG SER A 125 110.272 63.900 -3.234 1.00 59.29 O ANISOU 772 OG SER A 125 7920 6685 7923 227 413 217 O ATOM 773 N ILE A 126 113.988 66.207 -2.557 1.00 49.21 N ANISOU 773 N ILE A 126 6728 5435 6534 170 278 173 N ATOM 774 CA ILE A 126 115.370 66.494 -2.189 1.00 32.89 C ANISOU 774 CA ILE A 126 4664 3412 4421 137 235 146 C ATOM 775 C ILE A 126 115.414 67.519 -1.059 1.00 38.91 C ANISOU 775 C ILE A 126 5450 4178 5155 117 245 53 C ATOM 776 O ILE A 126 116.145 67.348 -0.074 1.00 46.01 O ANISOU 776 O ILE A 126 6359 5155 5966 108 217 15 O ATOM 777 CB ILE A 126 116.161 66.950 -3.430 1.00 41.81 C ANISOU 777 CB ILE A 126 5769 4510 5605 101 207 166 C ATOM 778 CG1 ILE A 126 116.334 65.780 -4.405 1.00 39.43 C ANISOU 778 CG1 ILE A 126 5439 4237 5304 120 196 233 C ATOM 779 CG2 ILE A 126 117.492 67.577 -3.050 1.00 36.92 C ANISOU 779 CG2 ILE A 126 5132 3927 4968 46 178 105 C ATOM 780 CD1 ILE A 126 116.918 66.165 -5.747 1.00 35.48 C ANISOU 780 CD1 ILE A 126 4922 3719 4839 79 190 255 C ATOM 781 N TYR A 127 114.589 68.568 -1.150 1.00 38.42 N ANISOU 781 N TYR A 127 5397 4033 5166 119 278 6 N ATOM 782 CA TYR A 127 114.597 69.591 -0.106 1.00 48.91 C ANISOU 782 CA TYR A 127 6746 5355 6483 99 294 -107 C ATOM 783 C TYR A 127 113.983 69.095 1.198 1.00 44.33 C ANISOU 783 C TYR A 127 6185 4857 5801 120 340 -150 C ATOM 784 O TYR A 127 114.466 69.445 2.277 1.00 43.69 O ANISOU 784 O TYR A 127 6126 4837 5636 97 333 -233 O ATOM 785 CB TYR A 127 113.906 70.862 -0.603 1.00 40.06 C ANISOU 785 CB TYR A 127 5633 4101 5487 109 312 -149 C ATOM 786 CG TYR A 127 114.880 71.768 -1.306 1.00 47.98 C ANISOU 786 CG TYR A 127 6652 5027 6553 50 277 -147 C ATOM 787 CD1 TYR A 127 115.585 72.732 -0.594 1.00 76.63 C ANISOU 787 CD1 TYR A 127 10293 8635 10189 -8 273 -256 C ATOM 788 CD2 TYR A 127 115.173 71.603 -2.652 1.00 47.70 C ANISOU 788 CD2 TYR A 127 6617 4950 6555 37 255 -43 C ATOM 789 CE1 TYR A 127 116.506 73.547 -1.214 1.00 70.56 C ANISOU 789 CE1 TYR A 127 9536 7788 9485 -86 258 -259 C ATOM 790 CE2 TYR A 127 116.103 72.415 -3.285 1.00 67.37 C ANISOU 790 CE2 TYR A 127 9131 7375 9093 -40 245 -35 C ATOM 791 CZ TYR A 127 116.764 73.383 -2.559 1.00 63.98 C ANISOU 791 CZ TYR A 127 8712 6912 8688 -106 250 -141 C ATOM 792 OH TYR A 127 117.686 74.197 -3.173 1.00 51.29 O ANISOU 792 OH TYR A 127 7123 5228 7135 -204 256 -139 O ATOM 793 N PHE A 128 112.934 68.279 1.132 1.00 43.15 N ANISOU 793 N PHE A 128 6030 4717 5650 153 392 -100 N ATOM 794 CA PHE A 128 112.361 67.726 2.354 1.00 48.91 C ANISOU 794 CA PHE A 128 6789 5527 6267 152 458 -126 C ATOM 795 C PHE A 128 113.390 66.890 3.103 1.00 50.85 C ANISOU 795 C PHE A 128 7087 5872 6362 140 411 -78 C ATOM 796 O PHE A 128 113.578 67.052 4.316 1.00 54.85 O ANISOU 796 O PHE A 128 7640 6460 6742 126 421 -138 O ATOM 797 CB PHE A 128 111.114 66.912 2.008 1.00 42.65 C ANISOU 797 CB PHE A 128 5969 4719 5516 169 529 -77 C ATOM 798 CG PHE A 128 109.920 67.760 1.649 1.00 42.93 C ANISOU 798 CG PHE A 128 5943 4686 5681 198 576 -158 C ATOM 799 CD1 PHE A 128 109.795 69.047 2.150 1.00 46.93 C ANISOU 799 CD1 PHE A 128 6447 5161 6224 207 588 -281 C ATOM 800 CD2 PHE A 128 108.954 67.294 0.769 1.00 46.07 C ANISOU 800 CD2 PHE A 128 6280 5047 6176 224 594 -123 C ATOM 801 CE1 PHE A 128 108.710 69.836 1.821 1.00 54.77 C ANISOU 801 CE1 PHE A 128 7380 6080 7352 257 617 -361 C ATOM 802 CE2 PHE A 128 107.868 68.085 0.427 1.00 47.44 C ANISOU 802 CE2 PHE A 128 6385 5164 6477 271 615 -204 C ATOM 803 CZ PHE A 128 107.748 69.356 0.957 1.00 55.01 C ANISOU 803 CZ PHE A 128 7344 6083 7476 295 624 -319 C ATOM 804 N LEU A 129 114.107 66.024 2.381 1.00 51.17 N ANISOU 804 N LEU A 129 7119 5912 6412 153 349 22 N ATOM 805 CA LEU A 129 115.138 65.202 3.010 1.00 41.38 C ANISOU 805 CA LEU A 129 5920 4755 5048 167 280 70 C ATOM 806 C LEU A 129 116.257 66.064 3.592 1.00 42.10 C ANISOU 806 C LEU A 129 6000 4907 5088 150 205 -25 C ATOM 807 O LEU A 129 116.692 65.859 4.736 1.00 70.73 O ANISOU 807 O LEU A 129 9675 8630 8568 159 167 -46 O ATOM 808 CB LEU A 129 115.691 64.209 1.990 1.00 46.61 C ANISOU 808 CB LEU A 129 6553 5389 5767 195 229 167 C ATOM 809 CG LEU A 129 114.667 63.176 1.511 1.00 57.42 C ANISOU 809 CG LEU A 129 7935 6704 7176 205 295 251 C ATOM 810 CD1 LEU A 129 115.209 62.361 0.343 1.00 49.90 C ANISOU 810 CD1 LEU A 129 6943 5716 6301 230 247 314 C ATOM 811 CD2 LEU A 129 114.252 62.263 2.663 1.00 50.95 C ANISOU 811 CD2 LEU A 129 7207 5921 6230 208 339 309 C ATOM 812 N THR A 130 116.722 67.054 2.824 1.00 49.90 N ANISOU 812 N THR A 130 6928 5840 6191 118 182 -86 N ATOM 813 CA THR A 130 117.827 67.894 3.278 1.00 61.89 C ANISOU 813 CA THR A 130 8419 7408 7687 81 117 -192 C ATOM 814 C THR A 130 117.447 68.699 4.514 1.00 61.71 C ANISOU 814 C THR A 130 8437 7425 7585 61 146 -314 C ATOM 815 O THR A 130 118.232 68.808 5.467 1.00 70.44 O ANISOU 815 O THR A 130 9551 8638 8577 52 81 -388 O ATOM 816 CB THR A 130 118.267 68.822 2.145 1.00 66.69 C ANISOU 816 CB THR A 130 8970 7924 8445 29 116 -223 C ATOM 817 OG1 THR A 130 118.774 68.036 1.057 1.00 63.93 O ANISOU 817 OG1 THR A 130 8579 7569 8142 41 89 -129 O ATOM 818 CG2 THR A 130 119.327 69.802 2.619 1.00 56.77 C ANISOU 818 CG2 THR A 130 7678 6701 7190 -35 68 -355 C ATOM 819 N VAL A 131 116.246 69.278 4.517 1.00 68.35 N ANISOU 819 N VAL A 131 9295 8190 8483 58 239 -351 N ATOM 820 CA VAL A 131 115.821 70.080 5.658 1.00 72.04 C ANISOU 820 CA VAL A 131 9793 8693 8885 40 283 -491 C ATOM 821 C VAL A 131 115.614 69.199 6.882 1.00 71.21 C ANISOU 821 C VAL A 131 9756 8726 8573 59 298 -468 C ATOM 822 O VAL A 131 115.949 69.594 8.005 1.00 70.29 O ANISOU 822 O VAL A 131 9674 8710 8325 40 279 -576 O ATOM 823 CB VAL A 131 114.555 70.882 5.311 1.00 69.53 C ANISOU 823 CB VAL A 131 9461 8256 8700 50 378 -546 C ATOM 824 CG1 VAL A 131 114.047 71.632 6.529 1.00 84.98 C ANISOU 824 CG1 VAL A 131 11442 10258 10591 38 438 -710 C ATOM 825 CG2 VAL A 131 114.846 71.852 4.184 1.00 64.06 C ANISOU 825 CG2 VAL A 131 8732 7417 8191 32 349 -557 C ATOM 826 N LEU A 132 115.058 67.995 6.692 1.00 64.11 N ANISOU 826 N LEU A 132 8891 7834 7636 89 336 -326 N ATOM 827 CA LEU A 132 114.969 67.050 7.801 1.00 71.03 C ANISOU 827 CA LEU A 132 9859 8826 8305 100 348 -268 C ATOM 828 C LEU A 132 116.347 66.780 8.396 1.00 69.18 C ANISOU 828 C LEU A 132 9652 8700 7934 121 207 -263 C ATOM 829 O LEU A 132 116.506 66.699 9.622 1.00 73.87 O ANISOU 829 O LEU A 132 10323 9417 8329 120 189 -298 O ATOM 830 CB LEU A 132 114.319 65.752 7.319 1.00 53.16 C ANISOU 830 CB LEU A 132 7624 6517 6055 119 401 -105 C ATOM 831 CG LEU A 132 114.067 64.647 8.344 1.00 59.90 C ANISOU 831 CG LEU A 132 8598 7451 6709 120 438 -6 C ATOM 832 CD1 LEU A 132 113.141 65.158 9.423 1.00 78.53 C ANISOU 832 CD1 LEU A 132 11002 9882 8952 72 564 -106 C ATOM 833 CD2 LEU A 132 113.462 63.417 7.679 1.00 50.19 C ANISOU 833 CD2 LEU A 132 7385 6139 5544 125 492 144 C ATOM 834 N SER A 133 117.362 66.675 7.540 1.00 67.03 N ANISOU 834 N SER A 133 9310 8397 7763 139 104 -231 N ATOM 835 CA SER A 133 118.711 66.387 8.022 1.00 81.09 C ANISOU 835 CA SER A 133 11084 10286 9441 171 -43 -241 C ATOM 836 C SER A 133 119.287 67.559 8.809 1.00 84.45 C ANISOU 836 C SER A 133 11481 10795 9810 128 -92 -427 C ATOM 837 O SER A 133 119.892 67.373 9.875 1.00 84.06 O ANISOU 837 O SER A 133 11475 10887 9578 152 -184 -464 O ATOM 838 CB SER A 133 119.603 66.042 6.838 1.00 84.50 C ANISOU 838 CB SER A 133 11422 10668 10018 193 -118 -190 C ATOM 839 OG SER A 133 119.066 64.908 6.192 1.00102.06 O ANISOU 839 OG SER A 133 13677 12820 12282 234 -77 -36 O ATOM 840 N VAL A 134 119.137 68.774 8.276 1.00 77.03 N ANISOU 840 N VAL A 134 10474 9766 9030 65 -39 -547 N ATOM 841 CA VAL A 134 119.591 69.963 8.998 1.00 54.48 C ANISOU 841 CA VAL A 134 7591 6961 6147 9 -69 -746 C ATOM 842 C VAL A 134 118.894 70.062 10.350 1.00 71.52 C ANISOU 842 C VAL A 134 9843 9221 8110 12 -18 -818 C ATOM 843 O VAL A 134 119.518 70.400 11.367 1.00 82.45 O ANISOU 843 O VAL A 134 11241 10740 9348 -2 -95 -943 O ATOM 844 CB VAL A 134 119.366 71.230 8.149 1.00 65.02 C ANISOU 844 CB VAL A 134 8864 8137 7704 -57 -1 -840 C ATOM 845 CG1 VAL A 134 119.666 72.486 8.959 1.00 62.23 C ANISOU 845 CG1 VAL A 134 8497 7810 7339 -121 -10 -1061 C ATOM 846 CG2 VAL A 134 120.227 71.187 6.896 1.00 66.94 C ANISOU 846 CG2 VAL A 134 9023 8309 8103 -80 -48 -781 C ATOM 847 N VAL A 135 117.593 69.762 10.383 1.00 79.32 N ANISOU 847 N VAL A 135 10891 10159 9088 23 115 -752 N ATOM 848 CA VAL A 135 116.839 69.815 11.633 1.00 82.27 C ANISOU 848 CA VAL A 135 11352 10635 9270 13 195 -822 C ATOM 849 C VAL A 135 117.393 68.814 12.637 1.00 86.32 C ANISOU 849 C VAL A 135 11965 11319 9512 49 107 -735 C ATOM 850 O VAL A 135 117.551 69.128 13.821 1.00 88.21 O ANISOU 850 O VAL A 135 12264 11703 9550 33 85 -848 O ATOM 851 CB VAL A 135 115.340 69.581 11.372 1.00 77.98 C ANISOU 851 CB VAL A 135 10830 10010 8790 12 364 -766 C ATOM 852 CG1 VAL A 135 114.612 69.318 12.680 1.00 76.27 C ANISOU 852 CG1 VAL A 135 10713 9926 8339 -7 463 -803 C ATOM 853 CG2 VAL A 135 114.733 70.789 10.664 1.00 68.60 C ANISOU 853 CG2 VAL A 135 9555 8672 7837 -7 435 -891 C ATOM 854 N ARG A 136 117.694 67.592 12.187 1.00 73.16 N ANISOU 854 N ARG A 136 10328 9636 7833 103 49 -536 N ATOM 855 CA ARG A 136 118.226 66.601 13.122 1.00 90.24 C ANISOU 855 CA ARG A 136 12605 11938 9743 156 -51 -430 C ATOM 856 C ARG A 136 119.595 67.010 13.664 1.00 95.05 C ANISOU 856 C ARG A 136 13172 12682 10262 180 -240 -546 C ATOM 857 O ARG A 136 119.865 66.872 14.869 1.00 92.95 O ANISOU 857 O ARG A 136 13001 12578 9736 199 -309 -574 O ATOM 858 CB ARG A 136 118.299 65.225 12.465 1.00 74.21 C ANISOU 858 CB ARG A 136 10611 9833 7753 219 -81 -202 C ATOM 859 CG ARG A 136 116.946 64.587 12.280 1.00 80.42 C ANISOU 859 CG ARG A 136 11469 10530 8557 189 96 -83 C ATOM 860 CD ARG A 136 117.071 63.126 11.917 1.00 88.92 C ANISOU 860 CD ARG A 136 12616 11543 9627 248 58 136 C ATOM 861 NE ARG A 136 115.757 62.508 11.799 1.00 96.63 N ANISOU 861 NE ARG A 136 13657 12437 10622 198 237 235 N ATOM 862 CZ ARG A 136 115.061 62.046 12.833 1.00100.89 C ANISOU 862 CZ ARG A 136 14343 13038 10952 158 340 298 C ATOM 863 NH1 ARG A 136 113.872 61.495 12.634 1.00110.74 N ANISOU 863 NH1 ARG A 136 15623 14207 12247 97 515 372 N ATOM 864 NH2 ARG A 136 115.545 62.148 14.066 1.00 79.05 N ANISOU 864 NH2 ARG A 136 11688 10424 7923 171 272 280 N ATOM 865 N TYR A 137 120.477 67.500 12.788 1.00 73.50 N ANISOU 865 N TYR A 137 10298 9897 7733 175 -325 -617 N ATOM 866 CA TYR A 137 121.776 67.985 13.247 1.00 77.57 C ANISOU 866 CA TYR A 137 10737 10541 8194 181 -496 -762 C ATOM 867 C TYR A 137 121.626 69.082 14.294 1.00 90.02 C ANISOU 867 C TYR A 137 12334 12220 9649 115 -474 -980 C ATOM 868 O TYR A 137 122.269 69.041 15.353 1.00 97.33 O ANISOU 868 O TYR A 137 13297 13328 10356 141 -603 -1055 O ATOM 869 CB TYR A 137 122.603 68.484 12.065 1.00 81.18 C ANISOU 869 CB TYR A 137 11026 10907 8912 149 -540 -825 C ATOM 870 CG TYR A 137 123.841 69.242 12.487 1.00 90.97 C ANISOU 870 CG TYR A 137 12154 12267 10142 117 -682 -1026 C ATOM 871 CD1 TYR A 137 124.910 68.594 13.094 1.00 85.05 C ANISOU 871 CD1 TYR A 137 11383 11685 9246 199 -877 -1023 C ATOM 872 CD2 TYR A 137 123.945 70.608 12.264 1.00 96.07 C ANISOU 872 CD2 TYR A 137 12713 12850 10938 4 -626 -1226 C ATOM 873 CE1 TYR A 137 126.040 69.291 13.475 1.00 94.66 C ANISOU 873 CE1 TYR A 137 12476 13027 10464 165 -1014 -1230 C ATOM 874 CE2 TYR A 137 125.071 71.311 12.640 1.00 98.84 C ANISOU 874 CE2 TYR A 137 12952 13306 11296 -45 -747 -1428 C ATOM 875 CZ TYR A 137 126.117 70.648 13.245 1.00107.42 C ANISOU 875 CZ TYR A 137 13999 14581 12235 32 -941 -1438 C ATOM 876 OH TYR A 137 127.243 71.347 13.622 1.00123.22 O ANISOU 876 OH TYR A 137 15865 16702 14250 -21 -1069 -1661 O ATOM 877 N LEU A 138 120.785 70.081 14.014 1.00 95.76 N ANISOU 877 N LEU A 138 13036 12834 10516 36 -320 -1094 N ATOM 878 CA LEU A 138 120.603 71.159 14.980 1.00 84.76 C ANISOU 878 CA LEU A 138 11657 11520 9029 -25 -287 -1326 C ATOM 879 C LEU A 138 119.945 70.662 16.259 1.00 91.09 C ANISOU 879 C LEU A 138 12612 12477 9521 -4 -242 -1301 C ATOM 880 O LEU A 138 120.214 71.196 17.342 1.00 76.84 O ANISOU 880 O LEU A 138 10838 10828 7529 -29 -289 -1476 O ATOM 881 CB LEU A 138 119.791 72.299 14.366 1.00 72.97 C ANISOU 881 CB LEU A 138 10107 9845 7772 -94 -133 -1446 C ATOM 882 CG LEU A 138 120.516 73.113 13.294 1.00 89.15 C ANISOU 882 CG LEU A 138 12026 11750 10099 -146 -172 -1517 C ATOM 883 CD1 LEU A 138 119.583 74.138 12.675 1.00 85.09 C ANISOU 883 CD1 LEU A 138 11491 11031 9807 -191 -25 -1593 C ATOM 884 CD2 LEU A 138 121.743 73.791 13.884 1.00 88.81 C ANISOU 884 CD2 LEU A 138 11910 11821 10011 -198 -309 -1723 C ATOM 885 N ALA A 139 119.097 69.635 16.162 1.00 85.07 N ANISOU 885 N ALA A 139 11950 11679 8692 33 -146 -1090 N ATOM 886 CA ALA A 139 118.496 69.056 17.357 1.00 91.94 C ANISOU 886 CA ALA A 139 12984 12696 9252 39 -87 -1036 C ATOM 887 C ALA A 139 119.552 68.416 18.245 1.00123.07 C ANISOU 887 C ALA A 139 17011 16831 12920 103 -289 -982 C ATOM 888 O ALA A 139 119.465 68.491 19.476 1.00136.82 O ANISOU 888 O ALA A 139 18866 18751 14368 91 -296 -1053 O ATOM 889 CB ALA A 139 117.430 68.035 16.965 1.00 72.82 C ANISOU 889 CB ALA A 139 10645 10177 6847 48 61 -813 C ATOM 890 N MET A 140 120.556 67.775 17.642 1.00129.36 N ANISOU 890 N MET A 140 17751 17601 13798 179 -459 -863 N ATOM 891 CA MET A 140 121.637 67.229 18.463 1.00126.46 C ANISOU 891 CA MET A 140 17441 17418 13190 263 -683 -831 C ATOM 892 C MET A 140 122.522 68.331 19.037 1.00128.39 C ANISOU 892 C MET A 140 17583 17810 13390 229 -814 -1109 C ATOM 893 O MET A 140 122.902 68.273 20.212 1.00143.27 O ANISOU 893 O MET A 140 19558 19902 14976 258 -931 -1168 O ATOM 894 CB MET A 140 122.477 66.223 17.677 1.00120.04 C ANISOU 894 CB MET A 140 16579 16539 12493 368 -833 -649 C ATOM 895 CG MET A 140 121.846 64.844 17.572 1.00121.58 C ANISOU 895 CG MET A 140 16933 16649 12613 428 -772 -359 C ATOM 896 SD MET A 140 122.935 63.639 16.792 1.00119.56 S ANISOU 896 SD MET A 140 16624 16326 12478 575 -972 -174 S ATOM 897 CE MET A 140 121.915 62.165 16.851 1.00137.04 C ANISOU 897 CE MET A 140 19064 18416 14589 609 -850 142 C ATOM 898 N VAL A 141 122.862 69.341 18.233 1.00121.70 N ANISOU 898 N VAL A 141 16554 16859 12829 162 -797 -1285 N ATOM 899 CA VAL A 141 123.789 70.366 18.713 1.00123.35 C ANISOU 899 CA VAL A 141 16650 17191 13027 115 -924 -1559 C ATOM 900 C VAL A 141 123.122 71.276 19.740 1.00136.22 C ANISOU 900 C VAL A 141 18352 18912 14495 36 -821 -1770 C ATOM 901 O VAL A 141 123.707 71.583 20.787 1.00146.81 O ANISOU 901 O VAL A 141 19710 20460 15610 36 -952 -1934 O ATOM 902 CB VAL A 141 124.364 71.170 17.533 1.00114.95 C ANISOU 902 CB VAL A 141 15384 15970 12321 47 -919 -1675 C ATOM 903 CG1 VAL A 141 125.140 72.379 18.043 1.00118.17 C ANISOU 903 CG1 VAL A 141 15678 16475 12746 -38 -1004 -1988 C ATOM 904 CG2 VAL A 141 125.266 70.286 16.702 1.00102.56 C ANISOU 904 CG2 VAL A 141 13726 14375 10866 128 -1051 -1518 C ATOM 905 N HIS A 142 121.904 71.730 19.463 1.00136.03 N ANISOU 905 N HIS A 142 18360 18744 14583 -27 -593 -1786 N ATOM 906 CA HIS A 142 121.224 72.667 20.357 1.00133.45 C ANISOU 906 CA HIS A 142 18078 18484 14140 -100 -475 -2016 C ATOM 907 C HIS A 142 120.588 71.956 21.548 1.00128.14 C ANISOU 907 C HIS A 142 17601 17998 13087 -73 -426 -1932 C ATOM 908 O HIS A 142 120.057 70.852 21.418 1.00117.04 O ANISOU 908 O HIS A 142 16307 16565 11597 -24 -367 -1669 O ATOM 909 CB HIS A 142 120.160 73.461 19.595 1.00129.10 C ANISOU 909 CB HIS A 142 17473 17705 13874 -162 -257 -2082 C ATOM 910 N THR A 150 105.958 74.533 18.947 1.00147.90 N ANISOU 910 N THR A 150 19586 19479 17130 -236 1897 -2512 N ATOM 911 CA THR A 150 106.566 75.662 18.257 1.00144.79 C ANISOU 911 CA THR A 150 19120 18896 16996 -164 1743 -2618 C ATOM 912 C THR A 150 107.348 75.188 17.040 1.00131.01 C ANISOU 912 C THR A 150 17382 17000 15396 -127 1560 -2356 C ATOM 913 O THR A 150 107.162 75.694 15.928 1.00130.30 O ANISOU 913 O THR A 150 17196 16702 15610 -59 1505 -2341 O ATOM 914 CB THR A 150 107.499 76.454 19.186 1.00147.08 C ANISOU 914 CB THR A 150 19479 19282 17123 -195 1663 -2815 C ATOM 915 N SER A 151 108.228 74.207 17.256 1.00115.40 N ANISOU 915 N SER A 151 15524 15132 13191 -166 1465 -2150 N ATOM 916 CA SER A 151 108.967 73.621 16.145 1.00102.43 C ANISOU 916 CA SER A 151 13885 13369 11664 -134 1308 -1906 C ATOM 917 C SER A 151 108.046 72.931 15.150 1.00102.53 C ANISOU 917 C SER A 151 13830 13273 11855 -106 1379 -1746 C ATOM 918 O SER A 151 108.411 72.791 13.981 1.00 99.93 O ANISOU 918 O SER A 151 13459 12796 11712 -64 1267 -1606 O ATOM 919 CB SER A 151 110.013 72.632 16.666 1.00 94.15 C ANISOU 919 CB SER A 151 12972 12468 10334 -166 1197 -1730 C ATOM 920 OG SER A 151 109.395 71.509 17.267 1.00 98.96 O ANISOU 920 OG SER A 151 13672 13206 10722 -208 1320 -1600 O ATOM 921 N ILE A 152 106.848 72.526 15.577 1.00 88.80 N ANISOU 921 N ILE A 152 12067 11608 10063 -136 1567 -1782 N ATOM 922 CA ILE A 152 105.881 71.950 14.646 1.00 84.79 C ANISOU 922 CA ILE A 152 11467 11003 9745 -114 1639 -1673 C ATOM 923 C ILE A 152 105.387 73.012 13.667 1.00 90.08 C ANISOU 923 C ILE A 152 11988 11485 10753 -24 1605 -1796 C ATOM 924 O ILE A 152 105.342 72.792 12.447 1.00 90.29 O ANISOU 924 O ILE A 152 11958 11371 10976 27 1521 -1660 O ATOM 925 CB ILE A 152 104.717 71.303 15.419 1.00 71.69 C ANISOU 925 CB ILE A 152 9806 9483 7950 -187 1866 -1709 C ATOM 926 CG1 ILE A 152 105.205 70.100 16.235 1.00 90.56 C ANISOU 926 CG1 ILE A 152 12376 12026 10008 -275 1889 -1522 C ATOM 927 CG2 ILE A 152 103.593 70.900 14.471 1.00 74.94 C ANISOU 927 CG2 ILE A 152 10079 9797 8599 -166 1947 -1662 C ATOM 928 CD1 ILE A 152 105.638 70.430 17.650 1.00114.39 C ANISOU 928 CD1 ILE A 152 15516 15232 12717 -325 1924 -1646 C ATOM 929 N ARG A 153 105.009 74.181 14.189 1.00 88.46 N ANISOU 929 N ARG A 153 11724 11271 10615 3 1665 -2056 N ATOM 930 CA ARG A 153 104.627 75.291 13.324 1.00 94.30 C ANISOU 930 CA ARG A 153 12347 11810 11675 104 1612 -2173 C ATOM 931 C ARG A 153 105.801 75.729 12.454 1.00 92.41 C ANISOU 931 C ARG A 153 12153 11413 11546 134 1411 -2064 C ATOM 932 O ARG A 153 105.616 76.090 11.287 1.00 92.89 O ANISOU 932 O ARG A 153 12152 11291 11852 209 1333 -2002 O ATOM 933 CB ARG A 153 104.107 76.449 14.177 1.00 95.61 C ANISOU 933 CB ARG A 153 12457 11992 11879 127 1713 -2488 C ATOM 934 CG ARG A 153 103.485 77.606 13.407 1.00107.88 C ANISOU 934 CG ARG A 153 13887 13328 13775 250 1680 -2630 C ATOM 935 CD ARG A 153 102.892 78.632 14.369 1.00125.52 C ANISOU 935 CD ARG A 153 16060 15592 16038 275 1802 -2963 C ATOM 936 NE ARG A 153 102.315 79.780 13.676 1.00134.12 N ANISOU 936 NE ARG A 153 17041 16450 17468 412 1758 -3104 N ATOM 937 CZ ARG A 153 101.063 79.834 13.233 1.00141.05 C ANISOU 937 CZ ARG A 153 17766 17279 18548 509 1826 -3171 C ATOM 938 NH1 ARG A 153 100.248 78.803 13.412 1.00141.83 N ANISOU 938 NH1 ARG A 153 17793 17547 18547 464 1960 -3121 N ATOM 939 NH2 ARG A 153 100.624 80.921 12.613 1.00142.81 N ANISOU 939 NH2 ARG A 153 17907 17277 19078 652 1757 -3291 N ATOM 940 N SER A 154 107.021 75.679 13.000 1.00 74.11 N ANISOU 940 N SER A 154 9942 9173 9042 73 1326 -2038 N ATOM 941 CA SER A 154 108.204 76.008 12.208 1.00 70.11 C ANISOU 941 CA SER A 154 9469 8541 8629 79 1151 -1939 C ATOM 942 C SER A 154 108.395 75.025 11.059 1.00 77.53 C ANISOU 942 C SER A 154 10408 9425 9624 94 1077 -1670 C ATOM 943 O SER A 154 108.753 75.424 9.945 1.00 70.71 O ANISOU 943 O SER A 154 9521 8397 8949 129 978 -1594 O ATOM 944 CB SER A 154 109.445 76.031 13.101 1.00 66.80 C ANISOU 944 CB SER A 154 9141 8253 7988 9 1075 -1982 C ATOM 945 OG SER A 154 109.357 77.060 14.071 1.00 90.74 O ANISOU 945 OG SER A 154 12171 11321 10986 -8 1128 -2254 O ATOM 946 N ALA A 155 108.163 73.735 11.313 1.00 81.36 N ANISOU 946 N ALA A 155 10929 10043 9941 62 1130 -1526 N ATOM 947 CA ALA A 155 108.247 72.732 10.258 1.00 71.88 C ANISOU 947 CA ALA A 155 9723 8792 8796 75 1074 -1293 C ATOM 948 C ALA A 155 107.191 72.966 9.187 1.00 68.21 C ANISOU 948 C ALA A 155 9149 8187 8580 143 1102 -1288 C ATOM 949 O ALA A 155 107.477 72.842 7.991 1.00 54.87 O ANISOU 949 O ALA A 155 7441 6383 7023 176 1004 -1155 O ATOM 950 CB ALA A 155 108.103 71.333 10.855 1.00 54.32 C ANISOU 950 CB ALA A 155 7568 6718 6351 23 1142 -1159 C ATOM 951 N TRP A 156 105.960 73.288 9.595 1.00 50.22 N ANISOU 951 N TRP A 156 6793 5929 6361 166 1234 -1438 N ATOM 952 CA TRP A 156 104.932 73.595 8.603 1.00 55.28 C ANISOU 952 CA TRP A 156 7313 6443 7248 250 1240 -1457 C ATOM 953 C TRP A 156 105.307 74.811 7.767 1.00 61.13 C ANISOU 953 C TRP A 156 8041 6989 8196 327 1114 -1493 C ATOM 954 O TRP A 156 105.092 74.821 6.550 1.00 64.14 O ANISOU 954 O TRP A 156 8383 7248 8739 390 1033 -1387 O ATOM 955 CB TRP A 156 103.569 73.793 9.267 1.00 45.98 C ANISOU 955 CB TRP A 156 6029 5332 6109 266 1405 -1646 C ATOM 956 CG TRP A 156 102.883 72.498 9.572 1.00 60.35 C ANISOU 956 CG TRP A 156 7829 7291 7809 194 1535 -1568 C ATOM 957 CD1 TRP A 156 102.731 71.906 10.791 1.00 68.45 C ANISOU 957 CD1 TRP A 156 8913 8491 8602 95 1683 -1605 C ATOM 958 CD2 TRP A 156 102.298 71.605 8.616 1.00 68.03 C ANISOU 958 CD2 TRP A 156 8732 8235 8883 202 1528 -1432 C ATOM 959 NE1 TRP A 156 102.058 70.714 10.656 1.00 71.23 N ANISOU 959 NE1 TRP A 156 9239 8907 8920 35 1781 -1494 N ATOM 960 CE2 TRP A 156 101.787 70.504 9.329 1.00 64.77 C ANISOU 960 CE2 TRP A 156 8333 7966 8312 98 1686 -1398 C ATOM 961 CE3 TRP A 156 102.149 71.637 7.224 1.00 62.80 C ANISOU 961 CE3 TRP A 156 8001 7438 8421 283 1404 -1340 C ATOM 962 CZ2 TRP A 156 101.138 69.444 8.700 1.00 65.52 C ANISOU 962 CZ2 TRP A 156 8366 8064 8466 66 1727 -1289 C ATOM 963 CZ3 TRP A 156 101.507 70.588 6.602 1.00 51.85 C ANISOU 963 CZ3 TRP A 156 6548 6075 7077 260 1433 -1240 C ATOM 964 CH2 TRP A 156 101.007 69.505 7.338 1.00 71.58 C ANISOU 964 CH2 TRP A 156 9051 8707 9438 150 1595 -1222 C ATOM 965 N ILE A 157 105.887 75.837 8.394 1.00 51.67 N ANISOU 965 N ILE A 157 6888 5756 6989 317 1096 -1639 N ATOM 966 CA ILE A 157 106.301 77.020 7.645 1.00 61.19 C ANISOU 966 CA ILE A 157 8104 6753 8393 372 988 -1667 C ATOM 967 C ILE A 157 107.423 76.673 6.666 1.00 59.63 C ANISOU 967 C ILE A 157 7975 6494 8188 335 858 -1454 C ATOM 968 O ILE A 157 107.429 77.133 5.516 1.00 53.71 O ANISOU 968 O ILE A 157 7222 5575 7609 389 775 -1369 O ATOM 969 CB ILE A 157 106.705 78.147 8.611 1.00 69.01 C ANISOU 969 CB ILE A 157 9128 7720 9374 348 1010 -1890 C ATOM 970 CG1 ILE A 157 105.481 78.626 9.398 1.00 70.86 C ANISOU 970 CG1 ILE A 157 9276 7988 9661 405 1143 -2124 C ATOM 971 CG2 ILE A 157 107.352 79.299 7.856 1.00 67.34 C ANISOU 971 CG2 ILE A 157 8956 7276 9353 372 899 -1893 C ATOM 972 CD1 ILE A 157 105.811 79.579 10.519 1.00 72.23 C ANISOU 972 CD1 ILE A 157 9479 8179 9785 372 1187 -2373 C ATOM 973 N LEU A 158 108.385 75.853 7.102 1.00 50.82 N ANISOU 973 N LEU A 158 6921 5518 6869 249 838 -1365 N ATOM 974 CA LEU A 158 109.464 75.434 6.207 1.00 41.69 C ANISOU 974 CA LEU A 158 5809 4327 5705 214 727 -1182 C ATOM 975 C LEU A 158 108.924 74.644 5.020 1.00 58.34 C ANISOU 975 C LEU A 158 7880 6396 7889 260 705 -1007 C ATOM 976 O LEU A 158 109.360 74.831 3.876 1.00 69.68 O ANISOU 976 O LEU A 158 9330 7719 9426 272 621 -895 O ATOM 977 CB LEU A 158 110.503 74.606 6.968 1.00 49.96 C ANISOU 977 CB LEU A 158 6913 5545 6524 137 704 -1134 C ATOM 978 CG LEU A 158 111.438 75.354 7.922 1.00 67.10 C ANISOU 978 CG LEU A 158 9123 7764 8610 79 674 -1286 C ATOM 979 CD1 LEU A 158 112.281 74.394 8.751 1.00 78.49 C ANISOU 979 CD1 LEU A 158 10615 9402 9805 29 639 -1234 C ATOM 980 CD2 LEU A 158 112.346 76.290 7.141 1.00 65.52 C ANISOU 980 CD2 LEU A 158 8927 7408 8562 51 585 -1292 C ATOM 981 N CYS A 159 107.963 73.758 5.274 1.00 44.90 N ANISOU 981 N CYS A 159 6133 4791 6135 277 788 -989 N ATOM 982 CA CYS A 159 107.397 72.966 4.188 1.00 47.89 C ANISOU 982 CA CYS A 159 6465 5143 6587 313 768 -848 C ATOM 983 C CYS A 159 106.595 73.836 3.229 1.00 45.43 C ANISOU 983 C CYS A 159 6092 4677 6493 409 726 -880 C ATOM 984 O CYS A 159 106.628 73.619 2.013 1.00 60.23 O ANISOU 984 O CYS A 159 7961 6481 8442 441 646 -750 O ATOM 985 CB CYS A 159 106.533 71.838 4.752 1.00 66.02 C ANISOU 985 CB CYS A 159 8723 7573 8789 288 879 -840 C ATOM 986 SG CYS A 159 107.461 70.600 5.686 1.00 76.08 S ANISOU 986 SG CYS A 159 10100 9007 9800 193 903 -738 S ATOM 987 N GLY A 160 105.871 74.826 3.751 1.00 47.56 N ANISOU 987 N GLY A 160 6317 4892 6862 465 774 -1056 N ATOM 988 CA GLY A 160 105.173 75.749 2.870 1.00 53.09 C ANISOU 988 CA GLY A 160 6970 5423 7777 579 711 -1085 C ATOM 989 C GLY A 160 106.130 76.540 2.002 1.00 50.56 C ANISOU 989 C GLY A 160 6744 4937 7528 579 594 -989 C ATOM 990 O GLY A 160 105.894 76.723 0.803 1.00 61.02 O ANISOU 990 O GLY A 160 8073 6150 8962 646 506 -880 O ATOM 991 N ILE A 161 107.232 77.008 2.594 1.00 51.69 N ANISOU 991 N ILE A 161 6968 5071 7601 496 593 -1031 N ATOM 992 CA ILE A 161 108.257 77.707 1.824 1.00 64.03 C ANISOU 992 CA ILE A 161 8620 6487 9222 460 505 -943 C ATOM 993 C ILE A 161 108.804 76.803 0.725 1.00 51.92 C ANISOU 993 C ILE A 161 7109 4991 7626 425 444 -732 C ATOM 994 O ILE A 161 108.995 77.232 -0.417 1.00 52.47 O ANISOU 994 O ILE A 161 7227 4927 7783 446 372 -619 O ATOM 995 CB ILE A 161 109.379 78.214 2.749 1.00 75.08 C ANISOU 995 CB ILE A 161 10075 7907 10546 356 523 -1049 C ATOM 996 CG1 ILE A 161 108.860 79.293 3.701 1.00 66.32 C ANISOU 996 CG1 ILE A 161 8950 6726 9521 393 577 -1277 C ATOM 997 CG2 ILE A 161 110.555 78.745 1.935 1.00 78.85 C ANISOU 997 CG2 ILE A 161 10630 8259 11069 284 450 -950 C ATOM 998 CD1 ILE A 161 109.855 79.666 4.789 1.00 53.44 C ANISOU 998 CD1 ILE A 161 7356 5161 7786 287 599 -1417 C ATOM 999 N ILE A 162 109.066 75.537 1.055 1.00 57.52 N ANISOU 999 N ILE A 162 7795 5880 8180 373 475 -675 N ATOM 1000 CA ILE A 162 109.616 74.613 0.064 1.00 45.97 C ANISOU 1000 CA ILE A 162 6347 4459 6661 342 423 -499 C ATOM 1001 C ILE A 162 108.628 74.401 -1.078 1.00 54.98 C ANISOU 1001 C ILE A 162 7449 5544 7897 430 385 -414 C ATOM 1002 O ILE A 162 108.995 74.453 -2.261 1.00 52.34 O ANISOU 1002 O ILE A 162 7154 5142 7590 431 315 -289 O ATOM 1003 CB ILE A 162 110.009 73.282 0.728 1.00 47.44 C ANISOU 1003 CB ILE A 162 6520 4828 6678 286 461 -465 C ATOM 1004 CG1 ILE A 162 111.225 73.481 1.640 1.00 46.20 C ANISOU 1004 CG1 ILE A 162 6406 4733 6415 205 457 -524 C ATOM 1005 CG2 ILE A 162 110.266 72.222 -0.330 1.00 45.02 C ANISOU 1005 CG2 ILE A 162 6207 4557 6342 279 418 -306 C ATOM 1006 CD1 ILE A 162 111.541 72.286 2.504 1.00 47.26 C ANISOU 1006 CD1 ILE A 162 6544 5038 6373 172 483 -500 C ATOM 1007 N TRP A 163 107.362 74.139 -0.738 1.00 50.20 N ANISOU 1007 N TRP A 163 6759 4980 7333 499 431 -489 N ATOM 1008 CA TRP A 163 106.328 74.003 -1.760 1.00 48.11 C ANISOU 1008 CA TRP A 163 6434 4675 7171 594 381 -441 C ATOM 1009 C TRP A 163 106.301 75.214 -2.682 1.00 48.48 C ANISOU 1009 C TRP A 163 6536 4534 7348 669 284 -403 C ATOM 1010 O TRP A 163 106.335 75.069 -3.911 1.00 49.89 O ANISOU 1010 O TRP A 163 6744 4673 7538 697 200 -271 O ATOM 1011 CB TRP A 163 104.956 73.796 -1.115 1.00 51.26 C ANISOU 1011 CB TRP A 163 6712 5137 7626 655 455 -576 C ATOM 1012 CG TRP A 163 104.689 72.409 -0.612 1.00 48.39 C ANISOU 1012 CG TRP A 163 6295 4940 7152 587 544 -567 C ATOM 1013 CD1 TRP A 163 104.709 71.978 0.682 1.00 45.79 C ANISOU 1013 CD1 TRP A 163 5963 4722 6712 516 661 -646 C ATOM 1014 CD2 TRP A 163 104.355 71.270 -1.408 1.00 50.91 C ANISOU 1014 CD2 TRP A 163 6567 5321 7454 578 523 -470 C ATOM 1015 NE1 TRP A 163 104.404 70.640 0.742 1.00 59.92 N ANISOU 1015 NE1 TRP A 163 7719 6623 8424 462 720 -588 N ATOM 1016 CE2 TRP A 163 104.184 70.181 -0.530 1.00 55.19 C ANISOU 1016 CE2 TRP A 163 7086 5992 7893 497 638 -489 C ATOM 1017 CE3 TRP A 163 104.183 71.064 -2.780 1.00 59.47 C ANISOU 1017 CE3 TRP A 163 7635 6366 8596 627 420 -371 C ATOM 1018 CZ2 TRP A 163 103.850 68.905 -0.980 1.00 49.42 C ANISOU 1018 CZ2 TRP A 163 6312 5328 7137 459 656 -419 C ATOM 1019 CZ3 TRP A 163 103.851 69.796 -3.224 1.00 70.81 C ANISOU 1019 CZ3 TRP A 163 9017 7890 9998 592 433 -319 C ATOM 1020 CH2 TRP A 163 103.687 68.734 -2.326 1.00 55.51 C ANISOU 1020 CH2 TRP A 163 7052 6058 7980 508 552 -346 C ATOM 1021 N ILE A 164 106.247 76.419 -2.108 1.00 37.79 N ANISOU 1021 N ILE A 164 5211 3060 6088 702 295 -516 N ATOM 1022 CA ILE A 164 106.117 77.620 -2.929 1.00 56.37 C ANISOU 1022 CA ILE A 164 7633 5202 8583 785 203 -476 C ATOM 1023 C ILE A 164 107.350 77.807 -3.807 1.00 59.35 C ANISOU 1023 C ILE A 164 8140 5506 8904 695 152 -313 C ATOM 1024 O ILE A 164 107.238 78.088 -5.006 1.00 42.80 O ANISOU 1024 O ILE A 164 6105 3309 6847 746 64 -180 O ATOM 1025 CB ILE A 164 105.853 78.856 -2.050 1.00 56.34 C ANISOU 1025 CB ILE A 164 7636 5067 8704 832 236 -650 C ATOM 1026 CG1 ILE A 164 104.545 78.685 -1.278 1.00 68.46 C ANISOU 1026 CG1 ILE A 164 9025 6684 10301 927 297 -825 C ATOM 1027 CG2 ILE A 164 105.802 80.112 -2.904 1.00 60.85 C ANISOU 1027 CG2 ILE A 164 8306 5384 9429 917 137 -589 C ATOM 1028 CD1 ILE A 164 103.332 78.494 -2.167 1.00 64.08 C ANISOU 1028 CD1 ILE A 164 8379 6117 9853 1071 219 -790 C ATOM 1029 N LEU A 165 108.541 77.654 -3.226 1.00 68.50 N ANISOU 1029 N LEU A 165 9339 6724 9964 559 207 -326 N ATOM 1030 CA LEU A 165 109.775 77.762 -3.997 1.00 65.82 C ANISOU 1030 CA LEU A 165 9096 6341 9571 454 180 -195 C ATOM 1031 C LEU A 165 109.750 76.837 -5.205 1.00 63.16 C ANISOU 1031 C LEU A 165 8757 6081 9160 462 132 -32 C ATOM 1032 O LEU A 165 109.916 77.276 -6.351 1.00 44.25 O ANISOU 1032 O LEU A 165 6448 3579 6785 469 74 96 O ATOM 1033 CB LEU A 165 110.972 77.429 -3.105 1.00 54.24 C ANISOU 1033 CB LEU A 165 7623 4988 7999 320 240 -257 C ATOM 1034 CG LEU A 165 112.352 77.465 -3.770 1.00 48.59 C ANISOU 1034 CG LEU A 165 6971 4260 7231 193 231 -158 C ATOM 1035 CD1 LEU A 165 112.739 78.886 -4.140 1.00 55.32 C ANISOU 1035 CD1 LEU A 165 7928 4890 8200 152 221 -152 C ATOM 1036 CD2 LEU A 165 113.416 76.820 -2.898 1.00 50.42 C ANISOU 1036 CD2 LEU A 165 7155 4655 7346 91 268 -225 C ATOM 1037 N ILE A 166 109.527 75.545 -4.963 1.00 36.09 N ANISOU 1037 N ILE A 166 5239 2834 5638 458 160 -37 N ATOM 1038 CA ILE A 166 109.662 74.569 -6.034 1.00 41.20 C ANISOU 1038 CA ILE A 166 5880 3567 6207 446 124 92 C ATOM 1039 C ILE A 166 108.568 74.754 -7.080 1.00 57.80 C ANISOU 1039 C ILE A 166 7979 5606 8377 565 41 155 C ATOM 1040 O ILE A 166 108.821 74.635 -8.284 1.00 66.76 O ANISOU 1040 O ILE A 166 9171 6729 9467 558 -16 282 O ATOM 1041 CB ILE A 166 109.666 73.150 -5.446 1.00 54.29 C ANISOU 1041 CB ILE A 166 7452 5406 7768 414 175 63 C ATOM 1042 CG1 ILE A 166 110.768 73.041 -4.396 1.00 52.83 C ANISOU 1042 CG1 ILE A 166 7280 5283 7508 318 231 6 C ATOM 1043 CG2 ILE A 166 109.901 72.132 -6.537 1.00 52.80 C ANISOU 1043 CG2 ILE A 166 7257 5296 7509 396 143 175 C ATOM 1044 CD1 ILE A 166 112.143 73.336 -4.938 1.00 51.10 C ANISOU 1044 CD1 ILE A 166 7124 5039 7254 223 215 71 C ATOM 1045 N MET A 167 107.339 75.063 -6.651 1.00 54.27 N ANISOU 1045 N MET A 167 7460 5127 8033 678 29 58 N ATOM 1046 CA MET A 167 106.253 75.203 -7.617 1.00 51.56 C ANISOU 1046 CA MET A 167 7091 4741 7760 809 -71 101 C ATOM 1047 C MET A 167 106.393 76.476 -8.444 1.00 51.18 C ANISOU 1047 C MET A 167 7175 4494 7776 864 -162 197 C ATOM 1048 O MET A 167 106.141 76.462 -9.654 1.00 62.53 O ANISOU 1048 O MET A 167 8661 5911 9188 920 -261 319 O ATOM 1049 CB MET A 167 104.901 75.167 -6.905 1.00 43.64 C ANISOU 1049 CB MET A 167 5947 3770 6864 916 -55 -52 C ATOM 1050 CG MET A 167 104.553 73.801 -6.331 1.00 57.02 C ANISOU 1050 CG MET A 167 7518 5654 8492 863 30 -117 C ATOM 1051 SD MET A 167 102.948 73.748 -5.518 1.00 67.90 S ANISOU 1051 SD MET A 167 8716 7086 9996 962 79 -308 S ATOM 1052 CE MET A 167 101.856 73.863 -6.934 1.00 68.11 C ANISOU 1052 CE MET A 167 8675 7082 10121 1116 -82 -265 C ATOM 1053 N ALA A 168 106.788 77.586 -7.817 1.00 48.18 N ANISOU 1053 N ALA A 168 6868 3963 7475 846 -131 145 N ATOM 1054 CA ALA A 168 106.963 78.827 -8.562 1.00 51.77 C ANISOU 1054 CA ALA A 168 7473 4195 8002 886 -206 247 C ATOM 1055 C ALA A 168 108.127 78.719 -9.536 1.00 60.18 C ANISOU 1055 C ALA A 168 8669 5256 8941 756 -205 421 C ATOM 1056 O ALA A 168 107.999 79.066 -10.714 1.00 71.19 O ANISOU 1056 O ALA A 168 10170 6566 10313 803 -293 573 O ATOM 1057 CB ALA A 168 107.172 79.993 -7.596 1.00 45.18 C ANISOU 1057 CB ALA A 168 6681 3191 7293 877 -158 130 C ATOM 1058 N SER A 169 109.271 78.222 -9.066 1.00 54.59 N ANISOU 1058 N SER A 169 7951 4651 8141 596 -106 398 N ATOM 1059 CA SER A 169 110.460 78.140 -9.905 1.00 57.28 C ANISOU 1059 CA SER A 169 8392 5000 8374 458 -81 532 C ATOM 1060 C SER A 169 110.342 77.112 -11.026 1.00 64.44 C ANISOU 1060 C SER A 169 9282 6051 9152 469 -125 644 C ATOM 1061 O SER A 169 111.211 77.087 -11.904 1.00 59.16 O ANISOU 1061 O SER A 169 8701 5390 8385 367 -106 760 O ATOM 1062 CB SER A 169 111.679 77.811 -9.044 1.00 51.26 C ANISOU 1062 CB SER A 169 7586 4331 7560 301 24 447 C ATOM 1063 OG SER A 169 111.557 76.517 -8.479 1.00 65.15 O ANISOU 1063 OG SER A 169 9210 6297 9245 307 51 375 O ATOM 1064 N SER A 170 109.302 76.276 -11.031 1.00 61.66 N ANISOU 1064 N SER A 170 8815 5816 8798 578 -172 599 N ATOM 1065 CA SER A 170 109.138 75.236 -12.042 1.00 49.25 C ANISOU 1065 CA SER A 170 7213 4388 7112 587 -215 674 C ATOM 1066 C SER A 170 108.051 75.547 -13.070 1.00 56.08 C ANISOU 1066 C SER A 170 8113 5202 7992 732 -351 752 C ATOM 1067 O SER A 170 107.759 74.693 -13.915 1.00 58.44 O ANISOU 1067 O SER A 170 8376 5630 8199 753 -401 792 O ATOM 1068 CB SER A 170 108.827 73.894 -11.369 1.00 36.44 C ANISOU 1068 CB SER A 170 5431 2948 5467 583 -168 564 C ATOM 1069 OG SER A 170 109.912 73.450 -10.574 1.00 61.59 O ANISOU 1069 OG SER A 170 8594 6200 8605 459 -66 516 O ATOM 1070 N ILE A 171 107.462 76.747 -13.034 1.00 48.27 N ANISOU 1070 N ILE A 171 7194 4028 7120 840 -421 768 N ATOM 1071 CA ILE A 171 106.262 77.024 -13.822 1.00 63.09 C ANISOU 1071 CA ILE A 171 9072 5864 9036 1017 -575 814 C ATOM 1072 C ILE A 171 106.532 76.989 -15.324 1.00 67.67 C ANISOU 1072 C ILE A 171 9790 6459 9462 1007 -659 999 C ATOM 1073 O ILE A 171 105.628 76.679 -16.110 1.00 63.14 O ANISOU 1073 O ILE A 171 9181 5953 8857 1131 -790 1026 O ATOM 1074 CB ILE A 171 105.645 78.366 -13.375 1.00 68.49 C ANISOU 1074 CB ILE A 171 9805 6323 9896 1147 -633 782 C ATOM 1075 CG1 ILE A 171 105.035 78.229 -11.978 1.00 74.31 C ANISOU 1075 CG1 ILE A 171 10366 7096 10771 1190 -564 567 C ATOM 1076 CG2 ILE A 171 104.587 78.844 -14.344 1.00 79.12 C ANISOU 1076 CG2 ILE A 171 11191 7593 11277 1342 -818 865 C ATOM 1077 CD1 ILE A 171 104.545 79.525 -11.375 1.00 90.52 C ANISOU 1077 CD1 ILE A 171 12451 8933 13010 1304 -593 494 C ATOM 1078 N MET A 172 107.763 77.283 -15.758 1.00 67.09 N ANISOU 1078 N MET A 172 9868 6339 9284 855 -584 1118 N ATOM 1079 CA MET A 172 108.020 77.269 -17.196 1.00 77.96 C ANISOU 1079 CA MET A 172 11389 7742 10491 833 -648 1294 C ATOM 1080 C MET A 172 107.901 75.871 -17.787 1.00 61.81 C ANISOU 1080 C MET A 172 9232 5945 8309 815 -659 1260 C ATOM 1081 O MET A 172 107.724 75.740 -19.003 1.00 65.14 O ANISOU 1081 O MET A 172 9738 6424 8589 846 -749 1373 O ATOM 1082 CB MET A 172 109.398 77.844 -17.526 1.00103.93 C ANISOU 1082 CB MET A 172 14851 10943 13695 648 -536 1415 C ATOM 1083 CG MET A 172 109.558 79.310 -17.185 1.00132.94 C ANISOU 1083 CG MET A 172 18675 14341 17495 651 -531 1475 C ATOM 1084 SD MET A 172 111.112 79.967 -17.815 1.00147.79 S ANISOU 1084 SD MET A 172 20769 16123 19263 412 -397 1633 S ATOM 1085 CE MET A 172 110.696 80.145 -19.550 1.00130.63 C ANISOU 1085 CE MET A 172 18799 13942 16893 481 -526 1875 C ATOM 1086 N LEU A 173 107.982 74.825 -16.957 1.00 53.25 N ANISOU 1086 N LEU A 173 7970 5003 7259 765 -572 1108 N ATOM 1087 CA LEU A 173 107.720 73.475 -17.445 1.00 58.26 C ANISOU 1087 CA LEU A 173 8489 5848 7801 761 -588 1054 C ATOM 1088 C LEU A 173 106.316 73.364 -18.031 1.00 63.12 C ANISOU 1088 C LEU A 173 9043 6502 8438 934 -753 1038 C ATOM 1089 O LEU A 173 106.077 72.550 -18.931 1.00 70.96 O ANISOU 1089 O LEU A 173 10004 7642 9316 942 -812 1042 O ATOM 1090 CB LEU A 173 107.907 72.464 -16.312 1.00 50.04 C ANISOU 1090 CB LEU A 173 7280 4908 6822 698 -475 900 C ATOM 1091 CG LEU A 173 109.299 72.342 -15.682 1.00 46.61 C ANISOU 1091 CG LEU A 173 6869 4479 6362 539 -329 888 C ATOM 1092 CD1 LEU A 173 109.269 71.383 -14.499 1.00 44.49 C ANISOU 1092 CD1 LEU A 173 6449 4299 6157 515 -250 748 C ATOM 1093 CD2 LEU A 173 110.345 71.918 -16.702 1.00 50.89 C ANISOU 1093 CD2 LEU A 173 7484 5109 6744 424 -286 969 C ATOM 1094 N LEU A 174 105.382 74.183 -17.537 1.00 56.28 N ANISOU 1094 N LEU A 174 8148 5510 7725 1077 -834 1002 N ATOM 1095 CA LEU A 174 104.021 74.213 -18.053 1.00 48.19 C ANISOU 1095 CA LEU A 174 7048 4515 6746 1260 -1008 972 C ATOM 1096 C LEU A 174 103.942 74.780 -19.467 1.00 59.63 C ANISOU 1096 C LEU A 174 8673 5929 8056 1333 -1163 1151 C ATOM 1097 O LEU A 174 102.930 74.572 -20.143 1.00 75.60 O ANISOU 1097 O LEU A 174 10632 8031 10063 1474 -1328 1133 O ATOM 1098 CB LEU A 174 103.141 75.026 -17.104 1.00 59.92 C ANISOU 1098 CB LEU A 174 8454 5866 8447 1397 -1042 875 C ATOM 1099 CG LEU A 174 103.014 74.422 -15.701 1.00 60.41 C ANISOU 1099 CG LEU A 174 8335 5989 8629 1337 -897 688 C ATOM 1100 CD1 LEU A 174 102.327 75.389 -14.756 1.00 71.54 C ANISOU 1100 CD1 LEU A 174 9693 7253 10235 1454 -905 591 C ATOM 1101 CD2 LEU A 174 102.265 73.098 -15.750 1.00 42.93 C ANISOU 1101 CD2 LEU A 174 5924 3978 6411 1341 -901 561 C ATOM 1102 N ASP A 175 104.975 75.492 -19.931 1.00 73.52 N ANISOU 1102 N ASP A 175 10652 7575 9706 1236 -1115 1321 N ATOM 1103 CA ASP A 175 104.980 75.968 -21.313 1.00 83.39 C ANISOU 1103 CA ASP A 175 12099 8804 10783 1282 -1245 1513 C ATOM 1104 C ASP A 175 105.213 74.831 -22.299 1.00 94.08 C ANISOU 1104 C ASP A 175 13429 10394 11924 1207 -1250 1515 C ATOM 1105 O ASP A 175 104.755 74.903 -23.446 1.00 87.88 O ANISOU 1105 O ASP A 175 12732 9666 10991 1295 -1405 1613 O ATOM 1106 CB ASP A 175 106.041 77.055 -21.494 1.00102.01 C ANISOU 1106 CB ASP A 175 14705 10966 13088 1172 -1164 1694 C ATOM 1107 CG ASP A 175 105.604 78.398 -20.937 1.00135.30 C ANISOU 1107 CG ASP A 175 19004 14911 17492 1294 -1227 1733 C ATOM 1108 OD1 ASP A 175 104.391 78.696 -20.975 1.00146.51 O ANISOU 1108 OD1 ASP A 175 20362 16287 19016 1510 -1402 1699 O ATOM 1109 OD2 ASP A 175 106.471 79.154 -20.452 1.00146.90 O ANISOU 1109 OD2 ASP A 175 20590 16210 19017 1176 -1103 1782 O ATOM 1110 N SER A 176 105.922 73.783 -21.879 1.00110.10 N ANISOU 1110 N SER A 176 15343 12560 13931 1053 -1089 1404 N ATOM 1111 CA SER A 176 106.160 72.630 -22.738 1.00114.95 C ANISOU 1111 CA SER A 176 15916 13392 14367 980 -1079 1372 C ATOM 1112 C SER A 176 104.913 71.754 -22.758 1.00 96.20 C ANISOU 1112 C SER A 176 13338 11157 12058 1102 -1198 1216 C ATOM 1113 O SER A 176 104.471 71.266 -21.712 1.00 98.30 O ANISOU 1113 O SER A 176 13419 11432 12500 1116 -1144 1059 O ATOM 1114 CB SER A 176 107.372 71.835 -22.255 1.00121.07 C ANISOU 1114 CB SER A 176 16638 14243 15121 789 -873 1302 C ATOM 1115 OG SER A 176 108.557 72.607 -22.322 1.00126.06 O ANISOU 1115 OG SER A 176 17438 14770 15689 660 -759 1428 O ATOM 1116 N GLY A 177 104.344 71.558 -23.943 1.00 92.27 N ANISOU 1116 N GLY A 177 12874 10773 11412 1183 -1356 1253 N ATOM 1117 CA GLY A 177 103.138 70.765 -24.077 1.00 84.70 C ANISOU 1117 CA GLY A 177 11714 9954 10513 1293 -1483 1094 C ATOM 1118 C GLY A 177 103.282 69.594 -25.029 1.00 74.95 C ANISOU 1118 C GLY A 177 10439 8937 9101 1220 -1493 1027 C ATOM 1119 O GLY A 177 104.386 69.284 -25.491 1.00 79.23 O ANISOU 1119 O GLY A 177 11090 9532 9481 1075 -1375 1086 O ATOM 1120 N SER A 178 102.168 68.929 -25.325 1.00 64.97 N ANISOU 1120 N SER A 178 9004 7805 7875 1316 -1628 883 N ATOM 1121 CA SER A 178 102.188 67.805 -26.250 1.00 58.03 C ANISOU 1121 CA SER A 178 8074 7134 6840 1255 -1654 790 C ATOM 1122 C SER A 178 102.430 68.294 -27.673 1.00 59.27 C ANISOU 1122 C SER A 178 8444 7362 6714 1286 -1782 950 C ATOM 1123 O SER A 178 101.692 69.143 -28.183 1.00 76.05 O ANISOU 1123 O SER A 178 10646 9454 8796 1448 -1985 1048 O ATOM 1124 CB SER A 178 100.874 67.028 -26.167 1.00 56.51 C ANISOU 1124 CB SER A 178 7634 7058 6780 1343 -1769 580 C ATOM 1125 OG SER A 178 99.784 67.826 -26.591 1.00 65.55 O ANISOU 1125 OG SER A 178 8770 8196 7941 1540 -2005 612 O ATOM 1126 N GLU A 179 103.471 67.765 -28.309 1.00 69.60 N ANISOU 1126 N GLU A 179 9852 8769 7826 1135 -1664 977 N ATOM 1127 CA GLU A 179 103.766 68.047 -29.706 1.00 73.00 C ANISOU 1127 CA GLU A 179 10483 9305 7949 1132 -1755 1110 C ATOM 1128 C GLU A 179 103.257 66.907 -30.584 1.00 69.24 C ANISOU 1128 C GLU A 179 9889 9069 7349 1136 -1850 937 C ATOM 1129 O GLU A 179 103.242 65.744 -30.171 1.00 91.06 O ANISOU 1129 O GLU A 179 12459 11909 10230 1060 -1754 731 O ATOM 1130 CB GLU A 179 105.268 68.251 -29.918 1.00 72.20 C ANISOU 1130 CB GLU A 179 10565 9173 7694 951 -1548 1238 C ATOM 1131 N GLN A 180 102.835 67.250 -31.802 1.00 66.70 N ANISOU 1131 N GLN A 180 9696 8863 6784 1225 -2045 1022 N ATOM 1132 CA GLN A 180 102.183 66.294 -32.687 1.00 77.04 C ANISOU 1132 CA GLN A 180 10892 10410 7970 1255 -2181 847 C ATOM 1133 C GLN A 180 102.880 66.246 -34.036 1.00 90.62 C ANISOU 1133 C GLN A 180 12824 12292 9317 1177 -2183 940 C ATOM 1134 O GLN A 180 103.218 67.283 -34.613 1.00 91.74 O ANISOU 1134 O GLN A 180 13223 12379 9256 1202 -2232 1184 O ATOM 1135 CB GLN A 180 100.703 66.639 -32.878 1.00 81.39 C ANISOU 1135 CB GLN A 180 11341 10996 8589 1473 -2471 805 C ATOM 1136 CG GLN A 180 99.941 65.633 -33.728 1.00 86.81 C ANISOU 1136 CG GLN A 180 11875 11935 9174 1504 -2627 589 C ATOM 1137 CD GLN A 180 98.460 65.934 -33.785 1.00119.64 C ANISOU 1137 CD GLN A 180 15881 16132 13445 1721 -2911 512 C ATOM 1138 OE1 GLN A 180 97.996 66.907 -33.193 1.00140.06 O ANISOU 1138 OE1 GLN A 180 18478 18549 16189 1859 -2990 621 O ATOM 1139 NE2 GLN A 180 97.710 65.105 -34.503 1.00132.64 N ANISOU 1139 NE2 GLN A 180 17374 18003 15019 1754 -3068 305 N ATOM 1140 N ASN A 181 103.078 65.030 -34.537 1.00114.16 N ANISOU 1140 N ASN A 181 15700 15469 12208 1076 -2124 738 N ATOM 1141 CA ASN A 181 103.698 64.779 -35.836 1.00132.69 C ANISOU 1141 CA ASN A 181 18210 18011 14194 990 -2111 765 C ATOM 1142 C ASN A 181 102.854 63.723 -36.539 1.00123.87 C ANISOU 1142 C ASN A 181 16926 17129 13011 1033 -2267 514 C ATOM 1143 O ASN A 181 103.002 62.526 -36.276 1.00125.39 O ANISOU 1143 O ASN A 181 16929 17384 13328 935 -2146 273 O ATOM 1144 CB ASN A 181 105.143 64.320 -35.679 1.00148.46 C ANISOU 1144 CB ASN A 181 20251 20000 16155 782 -1811 747 C ATOM 1145 CG ASN A 181 106.068 65.443 -35.268 1.00158.94 C ANISOU 1145 CG ASN A 181 21776 21137 17475 719 -1669 1002 C ATOM 1146 OD1 ASN A 181 106.006 66.546 -35.816 1.00170.12 O ANISOU 1146 OD1 ASN A 181 23422 22506 18708 775 -1769 1238 O ATOM 1147 ND2 ASN A 181 106.923 65.177 -34.289 1.00150.38 N ANISOU 1147 ND2 ASN A 181 20609 19934 16596 603 -1440 954 N ATOM 1148 N GLY A 182 101.960 64.169 -37.415 1.00113.24 N ANISOU 1148 N GLY A 182 15649 15902 11477 1183 -2542 567 N ATOM 1149 CA GLY A 182 101.060 63.260 -38.093 1.00118.71 C ANISOU 1149 CA GLY A 182 16172 16824 12108 1236 -2723 319 C ATOM 1150 C GLY A 182 99.968 62.718 -37.194 1.00110.52 C ANISOU 1150 C GLY A 182 14819 15736 11437 1314 -2799 99 C ATOM 1151 O GLY A 182 99.065 63.453 -36.786 1.00 98.73 O ANISOU 1151 O GLY A 182 13273 14150 10091 1480 -2973 166 O ATOM 1152 N SER A 183 100.039 61.429 -36.874 1.00114.88 N ANISOU 1152 N SER A 183 15160 16341 12147 1191 -2662 -171 N ATOM 1153 CA SER A 183 99.015 60.764 -36.081 1.00113.92 C ANISOU 1153 CA SER A 183 14736 16187 12361 1227 -2707 -403 C ATOM 1154 C SER A 183 99.523 60.343 -34.712 1.00102.76 C ANISOU 1154 C SER A 183 13216 14565 11264 1113 -2439 -440 C ATOM 1155 O SER A 183 98.813 59.642 -33.989 1.00106.06 O ANISOU 1155 O SER A 183 13392 14947 11960 1100 -2419 -638 O ATOM 1156 CB SER A 183 98.468 59.549 -36.840 1.00125.53 C ANISOU 1156 CB SER A 183 16036 17886 13776 1184 -2796 -708 C ATOM 1157 OG SER A 183 99.463 58.548 -36.987 1.00131.83 O ANISOU 1157 OG SER A 183 16849 18717 14525 1001 -2569 -828 O ATOM 1158 N VAL A 184 100.724 60.751 -34.335 1.00 88.43 N ANISOU 1158 N VAL A 184 11573 12619 9409 1026 -2236 -258 N ATOM 1159 CA VAL A 184 101.349 60.298 -33.101 1.00 87.88 C ANISOU 1159 CA VAL A 184 11421 12372 9598 914 -1987 -292 C ATOM 1160 C VAL A 184 101.633 61.547 -32.277 1.00 79.07 C ANISOU 1160 C VAL A 184 10424 11054 8567 970 -1944 -47 C ATOM 1161 O VAL A 184 102.665 62.202 -32.443 1.00116.56 O ANISOU 1161 O VAL A 184 15379 15745 13164 918 -1844 145 O ATOM 1162 CB VAL A 184 102.623 59.494 -33.363 1.00 78.84 C ANISOU 1162 CB VAL A 184 10339 11266 8351 749 -1773 -347 C ATOM 1163 CG1 VAL A 184 103.211 58.979 -32.050 1.00 65.41 C ANISOU 1163 CG1 VAL A 184 8545 9383 6926 657 -1545 -385 C ATOM 1164 CG2 VAL A 184 102.340 58.357 -34.334 1.00 80.10 C ANISOU 1164 CG2 VAL A 184 10405 11633 8395 704 -1833 -593 C ATOM 1165 N THR A 185 100.709 61.889 -31.384 1.00 56.51 N ANISOU 1165 N THR A 185 7429 8087 5957 1068 -2011 -68 N ATOM 1166 CA THR A 185 100.976 62.923 -30.391 1.00 62.54 C ANISOU 1166 CA THR A 185 8269 8640 6854 1105 -1938 114 C ATOM 1167 C THR A 185 102.029 62.422 -29.413 1.00 47.39 C ANISOU 1167 C THR A 185 6339 6602 5064 953 -1669 102 C ATOM 1168 O THR A 185 101.832 61.402 -28.748 1.00 56.48 O ANISOU 1168 O THR A 185 7314 7745 6403 886 -1571 -75 O ATOM 1169 CB THR A 185 99.692 63.299 -29.647 1.00 50.46 C ANISOU 1169 CB THR A 185 6565 7040 5568 1244 -2062 50 C ATOM 1170 OG1 THR A 185 98.733 63.823 -30.576 1.00 66.97 O ANISOU 1170 OG1 THR A 185 8663 9242 7540 1409 -2338 64 O ATOM 1171 CG2 THR A 185 99.981 64.338 -28.578 1.00 60.81 C ANISOU 1171 CG2 THR A 185 7950 8132 7023 1277 -1974 211 C ATOM 1172 N SER A 186 103.149 63.127 -29.331 1.00 46.73 N ANISOU 1172 N SER A 186 6447 6427 4882 895 -1552 290 N ATOM 1173 CA SER A 186 104.219 62.725 -28.434 1.00 65.39 C ANISOU 1173 CA SER A 186 8801 8689 7353 764 -1317 283 C ATOM 1174 C SER A 186 104.197 63.564 -27.166 1.00 43.07 C ANISOU 1174 C SER A 186 5975 5666 4723 800 -1261 381 C ATOM 1175 O SER A 186 103.678 64.680 -27.129 1.00 49.02 O ANISOU 1175 O SER A 186 6798 6340 5485 912 -1378 503 O ATOM 1176 CB SER A 186 105.587 62.847 -29.108 1.00 59.51 C ANISOU 1176 CB SER A 186 8234 7988 6388 652 -1197 385 C ATOM 1177 OG SER A 186 105.929 64.205 -29.299 1.00 70.62 O ANISOU 1177 OG SER A 186 9840 9308 7683 682 -1225 614 O ATOM 1178 N CYS A 187 104.765 62.995 -26.114 1.00 56.40 N ANISOU 1178 N CYS A 187 7586 7275 6569 710 -1085 320 N ATOM 1179 CA CYS A 187 104.934 63.687 -24.850 1.00 42.83 C ANISOU 1179 CA CYS A 187 5873 5386 5016 719 -1003 395 C ATOM 1180 C CYS A 187 106.101 63.009 -24.153 1.00 53.25 C ANISOU 1180 C CYS A 187 7180 6668 6385 589 -805 363 C ATOM 1181 O CYS A 187 106.512 61.909 -24.535 1.00 51.54 O ANISOU 1181 O CYS A 187 6915 6542 6127 516 -744 257 O ATOM 1182 CB CYS A 187 103.650 63.643 -24.005 1.00 51.82 C ANISOU 1182 CB CYS A 187 6843 6476 6370 809 -1067 295 C ATOM 1183 SG CYS A 187 103.657 64.617 -22.488 1.00 68.32 S ANISOU 1183 SG CYS A 187 8936 8373 8648 840 -987 367 S ATOM 1184 N LEU A 188 106.647 63.684 -23.144 1.00 55.88 N ANISOU 1184 N LEU A 188 7558 6865 6807 569 -713 449 N ATOM 1185 CA LEU A 188 107.703 63.179 -22.273 1.00 47.96 C ANISOU 1185 CA LEU A 188 6536 5815 5872 470 -546 424 C ATOM 1186 C LEU A 188 109.045 63.088 -22.994 1.00 50.02 C ANISOU 1186 C LEU A 188 6896 6137 5975 373 -461 469 C ATOM 1187 O LEU A 188 109.997 62.546 -22.416 1.00 59.14 O ANISOU 1187 O LEU A 188 8018 7275 7178 298 -335 430 O ATOM 1188 CB LEU A 188 107.363 61.794 -21.697 1.00 42.85 C ANISOU 1188 CB LEU A 188 5733 5192 5355 443 -492 265 C ATOM 1189 CG LEU A 188 105.993 61.700 -21.022 1.00 40.05 C ANISOU 1189 CG LEU A 188 5255 4802 5160 513 -550 190 C ATOM 1190 CD1 LEU A 188 105.711 60.274 -20.581 1.00 36.67 C ANISOU 1190 CD1 LEU A 188 4697 4392 4846 460 -481 43 C ATOM 1191 CD2 LEU A 188 105.850 62.683 -19.875 1.00 58.69 C ANISOU 1191 CD2 LEU A 188 7633 7038 7627 551 -523 261 C ATOM 1192 N GLU A 189 109.157 63.572 -24.229 1.00 57.39 N ANISOU 1192 N GLU A 189 7944 7145 6715 372 -523 546 N ATOM 1193 CA GLU A 189 110.370 63.422 -25.017 1.00 54.57 C ANISOU 1193 CA GLU A 189 7669 6874 6192 267 -426 568 C ATOM 1194 C GLU A 189 111.219 64.683 -24.916 1.00 63.75 C ANISOU 1194 C GLU A 189 8979 7946 7298 211 -362 732 C ATOM 1195 O GLU A 189 110.712 65.775 -24.644 1.00 79.14 O ANISOU 1195 O GLU A 189 11008 9780 9283 273 -435 849 O ATOM 1196 CB GLU A 189 110.051 63.171 -26.494 1.00 39.37 C ANISOU 1196 CB GLU A 189 5798 5105 4054 276 -513 551 C ATOM 1197 CG GLU A 189 109.085 62.036 -26.807 1.00 61.81 C ANISOU 1197 CG GLU A 189 8504 8047 6935 329 -602 379 C ATOM 1198 CD GLU A 189 109.586 60.664 -26.413 1.00 75.26 C ANISOU 1198 CD GLU A 189 10074 9776 8745 265 -486 207 C ATOM 1199 OE1 GLU A 189 110.816 60.446 -26.389 1.00 80.86 O ANISOU 1199 OE1 GLU A 189 10807 10497 9421 179 -349 202 O ATOM 1200 OE2 GLU A 189 108.735 59.787 -26.148 1.00 64.16 O ANISOU 1200 OE2 GLU A 189 8536 8377 7466 301 -533 71 O ATOM 1201 N LEU A 190 112.521 64.525 -25.139 1.00 40.26 N ANISOU 1201 N LEU A 190 6032 5018 4246 92 -222 727 N ATOM 1202 CA LEU A 190 113.347 65.687 -25.414 1.00 48.15 C ANISOU 1202 CA LEU A 190 7186 5965 5145 8 -154 878 C ATOM 1203 C LEU A 190 113.143 66.074 -26.876 1.00 54.58 C ANISOU 1203 C LEU A 190 8153 6874 5709 -1 -215 975 C ATOM 1204 O LEU A 190 112.875 65.226 -27.730 1.00 95.19 O ANISOU 1204 O LEU A 190 13261 12172 10733 11 -254 884 O ATOM 1205 CB LEU A 190 114.825 65.383 -25.166 1.00 45.86 C ANISOU 1205 CB LEU A 190 6850 5710 4863 -125 25 820 C ATOM 1206 CG LEU A 190 115.781 66.488 -24.667 1.00 53.91 C ANISOU 1206 CG LEU A 190 7948 6619 5915 -224 128 922 C ATOM 1207 CD1 LEU A 190 117.183 65.916 -24.410 1.00 59.29 C ANISOU 1207 CD1 LEU A 190 8525 7376 6628 -339 289 811 C ATOM 1208 CD2 LEU A 190 115.836 67.771 -25.485 1.00 83.41 C ANISOU 1208 CD2 LEU A 190 11894 10301 9496 -278 123 1109 C ATOM 1209 N ASN A 191 113.265 67.364 -27.169 1.00 64.40 N ANISOU 1209 N ASN A 191 9580 8022 6868 -24 -227 1161 N ATOM 1210 CA ASN A 191 113.148 67.844 -28.540 1.00 82.73 C ANISOU 1210 CA ASN A 191 12087 10421 8925 -40 -281 1291 C ATOM 1211 C ASN A 191 113.888 69.172 -28.637 1.00 71.96 C ANISOU 1211 C ASN A 191 10920 8925 7497 -143 -195 1487 C ATOM 1212 O ASN A 191 114.289 69.745 -27.620 1.00 65.88 O ANISOU 1212 O ASN A 191 10127 7996 6906 -176 -126 1507 O ATOM 1213 CB ASN A 191 111.671 67.946 -28.957 1.00100.96 C ANISOU 1213 CB ASN A 191 14421 12739 11201 134 -512 1324 C ATOM 1214 CG ASN A 191 110.870 68.896 -28.081 1.00107.10 C ANISOU 1214 CG ASN A 191 15216 13310 12168 257 -621 1412 C ATOM 1215 OD1 ASN A 191 111.431 69.678 -27.318 1.00114.34 O ANISOU 1215 OD1 ASN A 191 16180 14065 13200 203 -531 1485 O ATOM 1216 ND2 ASN A 191 109.545 68.807 -28.167 1.00100.45 N ANISOU 1216 ND2 ASN A 191 14317 12478 11370 424 -816 1382 N ATOM 1217 N LEU A 192 114.079 69.666 -29.868 1.00 82.38 N ANISOU 1217 N LEU A 192 12442 10309 8551 -203 -194 1630 N ATOM 1218 CA LEU A 192 114.753 70.956 -30.019 1.00100.05 C ANISOU 1218 CA LEU A 192 14891 12400 10724 -317 -102 1833 C ATOM 1219 C LEU A 192 113.950 72.070 -29.353 1.00124.38 C ANISOU 1219 C LEU A 192 18061 15233 13965 -190 -238 1969 C ATOM 1220 O LEU A 192 114.522 72.960 -28.708 1.00122.81 O ANISOU 1220 O LEU A 192 17925 14851 13888 -271 -143 2045 O ATOM 1221 CB LEU A 192 115.002 71.288 -31.493 1.00100.43 C ANISOU 1221 CB LEU A 192 15168 12558 10433 -402 -81 1984 C ATOM 1222 CG LEU A 192 113.925 71.942 -32.373 1.00108.47 C ANISOU 1222 CG LEU A 192 16402 13545 11268 -263 -298 2177 C ATOM 1223 CD1 LEU A 192 114.572 72.592 -33.592 1.00101.40 C ANISOU 1223 CD1 LEU A 192 15785 12694 10047 -412 -205 2378 C ATOM 1224 CD2 LEU A 192 112.864 70.951 -32.802 1.00113.74 C ANISOU 1224 CD2 LEU A 192 16946 14392 11877 -101 -488 2041 C ATOM 1225 N TYR A 193 112.616 72.009 -29.467 1.00137.75 N ANISOU 1225 N TYR A 193 19740 16919 15679 11 -461 1977 N ATOM 1226 CA TYR A 193 111.755 73.014 -28.846 1.00144.43 C ANISOU 1226 CA TYR A 193 20646 17538 16694 160 -604 2079 C ATOM 1227 C TYR A 193 112.054 73.171 -27.357 1.00138.09 C ANISOU 1227 C TYR A 193 19698 16587 16183 137 -509 1977 C ATOM 1228 O TYR A 193 111.915 74.265 -26.797 1.00136.30 O ANISOU 1228 O TYR A 193 19565 16136 16087 173 -533 2076 O ATOM 1229 CB TYR A 193 110.287 72.642 -29.060 1.00139.79 C ANISOU 1229 CB TYR A 193 19978 17013 16124 382 -847 2026 C ATOM 1230 N LYS A 194 112.477 72.089 -26.700 1.00129.52 N ANISOU 1230 N LYS A 194 18393 15620 15198 82 -406 1777 N ATOM 1231 CA LYS A 194 112.807 72.126 -25.282 1.00116.35 C ANISOU 1231 CA LYS A 194 16588 13845 13776 58 -319 1672 C ATOM 1232 C LYS A 194 114.287 72.358 -24.987 1.00104.45 C ANISOU 1232 C LYS A 194 15098 12316 12274 -144 -111 1669 C ATOM 1233 O LYS A 194 114.605 72.763 -23.863 1.00122.87 O ANISOU 1233 O LYS A 194 17372 14524 14792 -169 -54 1624 O ATOM 1234 CB LYS A 194 112.384 70.820 -24.595 1.00109.99 C ANISOU 1234 CB LYS A 194 15538 13161 13092 124 -336 1464 C ATOM 1235 CG LYS A 194 110.890 70.603 -24.417 1.00100.31 C ANISOU 1235 CG LYS A 194 14228 11929 11955 314 -518 1414 C ATOM 1236 CD LYS A 194 110.668 69.275 -23.706 1.00108.50 C ANISOU 1236 CD LYS A 194 15039 13076 13113 330 -487 1213 C ATOM 1237 CE LYS A 194 109.200 68.949 -23.496 1.00114.75 C ANISOU 1237 CE LYS A 194 15715 13880 14005 492 -641 1134 C ATOM 1238 NZ LYS A 194 109.025 67.639 -22.799 1.00 94.65 N ANISOU 1238 NZ LYS A 194 12967 11421 11574 481 -588 951 N ATOM 1239 N ILE A 195 115.201 72.118 -25.936 1.00 77.09 N ANISOU 1239 N ILE A 195 11698 8979 8613 -290 6 1699 N ATOM 1240 CA ILE A 195 116.599 71.927 -25.538 1.00 91.19 C ANISOU 1240 CA ILE A 195 13403 10807 10438 -471 206 1613 C ATOM 1241 C ILE A 195 117.196 73.210 -24.962 1.00100.09 C ANISOU 1241 C ILE A 195 14634 11727 11668 -573 289 1708 C ATOM 1242 O ILE A 195 117.754 73.204 -23.856 1.00108.86 O ANISOU 1242 O ILE A 195 15616 12790 12957 -618 361 1598 O ATOM 1243 CB ILE A 195 117.457 71.372 -26.691 1.00 86.52 C ANISOU 1243 CB ILE A 195 12838 10413 9621 -611 331 1597 C ATOM 1244 CG1 ILE A 195 118.880 71.173 -26.161 1.00 84.95 C ANISOU 1244 CG1 ILE A 195 12514 10258 9504 -780 530 1480 C ATOM 1245 CG2 ILE A 195 117.436 72.276 -27.922 1.00 79.94 C ANISOU 1245 CG2 ILE A 195 12271 9552 8553 -678 333 1812 C ATOM 1246 CD1 ILE A 195 119.805 70.441 -27.065 1.00 85.46 C ANISOU 1246 CD1 ILE A 195 12533 10537 9401 -909 673 1397 C ATOM 1247 N ALA A 196 117.090 74.324 -25.694 1.00 99.53 N ANISOU 1247 N ALA A 196 14804 11526 11485 -612 275 1912 N ATOM 1248 CA ALA A 196 117.763 75.556 -25.288 1.00103.06 C ANISOU 1248 CA ALA A 196 15370 11766 12022 -744 377 2004 C ATOM 1249 C ALA A 196 117.445 75.902 -23.840 1.00 89.76 C ANISOU 1249 C ALA A 196 13574 9922 10607 -658 327 1911 C ATOM 1250 O ALA A 196 118.336 76.253 -23.058 1.00 77.40 O ANISOU 1250 O ALA A 196 11947 8293 9170 -787 449 1836 O ATOM 1251 CB ALA A 196 117.362 76.701 -26.219 1.00107.04 C ANISOU 1251 CB ALA A 196 16174 12108 12388 -744 321 2260 C ATOM 1252 N LYS A 197 116.175 75.776 -23.465 1.00 73.24 N ANISOU 1252 N LYS A 197 11444 7784 8601 -445 148 1895 N ATOM 1253 CA LYS A 197 115.749 75.887 -22.079 1.00 77.71 C ANISOU 1253 CA LYS A 197 11876 8246 9402 -348 101 1775 C ATOM 1254 C LYS A 197 116.511 74.884 -21.221 1.00 77.46 C ANISOU 1254 C LYS A 197 11617 8367 9447 -417 203 1575 C ATOM 1255 O LYS A 197 117.432 75.252 -20.477 1.00 72.06 O ANISOU 1255 O LYS A 197 10889 7630 8862 -539 314 1511 O ATOM 1256 CB LYS A 197 114.241 75.641 -21.994 1.00 78.81 C ANISOU 1256 CB LYS A 197 11975 8378 9590 -115 -92 1764 C ATOM 1257 CG LYS A 197 113.429 76.599 -22.857 1.00106.91 C ANISOU 1257 CG LYS A 197 15753 11793 13077 -10 -228 1960 C ATOM 1258 CD LYS A 197 111.957 76.220 -22.922 1.00119.87 C ANISOU 1258 CD LYS A 197 17319 13474 14751 222 -428 1926 C ATOM 1259 CE LYS A 197 111.228 76.524 -21.624 1.00122.79 C ANISOU 1259 CE LYS A 197 17566 13717 15370 348 -482 1810 C ATOM 1260 NZ LYS A 197 109.766 76.261 -21.767 1.00127.24 N ANISOU 1260 NZ LYS A 197 18054 14316 15974 569 -673 1776 N ATOM 1261 N LEU A 198 116.170 73.603 -21.402 1.00 78.82 N ANISOU 1261 N LEU A 198 11652 8732 9565 -343 162 1478 N ATOM 1262 CA LEU A 198 116.587 72.546 -20.484 1.00 78.64 C ANISOU 1262 CA LEU A 198 11415 8829 9634 -348 212 1296 C ATOM 1263 C LEU A 198 118.067 72.628 -20.146 1.00 51.79 C ANISOU 1263 C LEU A 198 7962 5461 6255 -526 370 1232 C ATOM 1264 O LEU A 198 118.439 72.595 -18.968 1.00 41.09 O ANISOU 1264 O LEU A 198 6495 4079 5038 -535 397 1124 O ATOM 1265 CB LEU A 198 116.257 71.175 -21.078 1.00 72.09 C ANISOU 1265 CB LEU A 198 10486 8196 8710 -288 176 1223 C ATOM 1266 CG LEU A 198 114.762 70.906 -21.228 1.00 68.30 C ANISOU 1266 CG LEU A 198 9999 7710 8242 -111 15 1234 C ATOM 1267 CD1 LEU A 198 114.515 69.559 -21.884 1.00 90.35 C ANISOU 1267 CD1 LEU A 198 12695 10691 10941 -77 -10 1148 C ATOM 1268 CD2 LEU A 198 114.069 71.002 -19.879 1.00 62.66 C ANISOU 1268 CD2 LEU A 198 9189 6898 7722 -9 -36 1158 C ATOM 1269 N GLN A 199 118.917 72.764 -21.167 1.00 43.18 N ANISOU 1269 N GLN A 199 6947 4437 5021 -670 475 1291 N ATOM 1270 CA GLN A 199 120.360 72.823 -20.956 1.00 62.60 C ANISOU 1270 CA GLN A 199 9333 6950 7503 -851 635 1213 C ATOM 1271 C GLN A 199 120.705 73.792 -19.827 1.00 55.03 C ANISOU 1271 C GLN A 199 8371 5824 6713 -903 660 1187 C ATOM 1272 O GLN A 199 121.179 73.376 -18.762 1.00 54.69 O ANISOU 1272 O GLN A 199 8163 5827 6788 -899 674 1039 O ATOM 1273 CB GLN A 199 121.049 73.194 -22.275 1.00 72.70 C ANISOU 1273 CB GLN A 199 10744 8279 8600 -1014 755 1315 C ATOM 1274 CG GLN A 199 122.557 72.993 -22.313 1.00 90.77 C ANISOU 1274 CG GLN A 199 12917 10686 10885 -1206 937 1203 C ATOM 1275 CD GLN A 199 123.109 73.031 -23.730 1.00104.75 C ANISOU 1275 CD GLN A 199 14793 12566 12441 -1354 1064 1280 C ATOM 1276 OE1 GLN A 199 122.386 73.311 -24.689 1.00107.86 O ANISOU 1276 OE1 GLN A 199 15375 12933 12673 -1317 1009 1439 O ATOM 1277 NE2 GLN A 199 124.385 72.695 -23.872 1.00106.08 N ANISOU 1277 NE2 GLN A 199 14830 12876 12600 -1513 1230 1155 N ATOM 1278 N THR A 200 120.393 75.080 -20.000 1.00 55.34 N ANISOU 1278 N THR A 200 8597 5661 6770 -934 649 1326 N ATOM 1279 CA THR A 200 120.633 76.017 -18.906 1.00 56.47 C ANISOU 1279 CA THR A 200 8739 5633 7087 -977 666 1282 C ATOM 1280 C THR A 200 119.798 75.647 -17.692 1.00 56.72 C ANISOU 1280 C THR A 200 8654 5646 7251 -801 547 1176 C ATOM 1281 O THR A 200 120.310 75.598 -16.565 1.00 58.36 O ANISOU 1281 O THR A 200 8735 5866 7573 -829 573 1037 O ATOM 1282 CB THR A 200 120.339 77.453 -19.340 1.00 57.21 C ANISOU 1282 CB THR A 200 9070 5479 7189 -1024 666 1456 C ATOM 1283 OG1 THR A 200 118.995 77.542 -19.820 1.00 69.62 O ANISOU 1283 OG1 THR A 200 10760 6980 8713 -837 514 1580 O ATOM 1284 CG2 THR A 200 121.295 77.891 -20.419 1.00 59.05 C ANISOU 1284 CG2 THR A 200 9427 5719 7290 -1238 816 1561 C ATOM 1285 N MET A 201 118.517 75.340 -17.912 1.00 43.66 N ANISOU 1285 N MET A 201 7034 3983 5573 -622 418 1230 N ATOM 1286 CA MET A 201 117.658 74.921 -16.817 1.00 41.57 C ANISOU 1286 CA MET A 201 6656 3718 5422 -465 324 1127 C ATOM 1287 C MET A 201 118.241 73.725 -16.077 1.00 50.98 C ANISOU 1287 C MET A 201 7650 5089 6630 -475 360 971 C ATOM 1288 O MET A 201 117.984 73.566 -14.880 1.00 55.16 O ANISOU 1288 O MET A 201 8088 5608 7261 -410 329 869 O ATOM 1289 CB MET A 201 116.263 74.589 -17.341 1.00 68.72 C ANISOU 1289 CB MET A 201 10128 7163 8820 -290 192 1192 C ATOM 1290 CG MET A 201 115.211 74.459 -16.253 1.00 75.00 C ANISOU 1290 CG MET A 201 10833 7917 9748 -137 106 1102 C ATOM 1291 SD MET A 201 113.620 73.918 -16.917 1.00 96.56 S ANISOU 1291 SD MET A 201 13555 10693 12441 55 -42 1142 S ATOM 1292 CE MET A 201 113.192 75.295 -17.985 1.00105.05 C ANISOU 1292 CE MET A 201 14859 11582 13472 91 -120 1336 C ATOM 1293 N ASN A 202 119.038 72.892 -16.752 1.00 37.43 N ANISOU 1293 N ASN A 202 5873 3535 4813 -552 427 948 N ATOM 1294 CA ASN A 202 119.734 71.831 -16.038 1.00 38.21 C ANISOU 1294 CA ASN A 202 5793 3780 4943 -558 457 802 C ATOM 1295 C ASN A 202 120.709 72.411 -15.028 1.00 57.60 C ANISOU 1295 C ASN A 202 8190 6199 7496 -657 515 711 C ATOM 1296 O ASN A 202 120.600 72.145 -13.827 1.00 50.20 O ANISOU 1296 O ASN A 202 7164 5270 6640 -592 472 616 O ATOM 1297 CB ASN A 202 120.489 70.932 -17.005 1.00 47.78 C ANISOU 1297 CB ASN A 202 6949 5162 6045 -623 524 779 C ATOM 1298 CG ASN A 202 121.013 69.688 -16.335 1.00 49.82 C ANISOU 1298 CG ASN A 202 7028 5558 6345 -582 525 636 C ATOM 1299 OD1 ASN A 202 120.690 69.406 -15.180 1.00 68.59 O ANISOU 1299 OD1 ASN A 202 9340 7912 8810 -497 466 575 O ATOM 1300 ND2 ASN A 202 121.865 68.960 -17.035 1.00 71.92 N ANISOU 1300 ND2 ASN A 202 9751 8496 9078 -643 595 581 N ATOM 1301 N TYR A 203 121.665 73.215 -15.501 1.00 44.81 N ANISOU 1301 N TYR A 203 6620 4542 5863 -823 615 736 N ATOM 1302 CA TYR A 203 122.816 73.565 -14.677 1.00 52.25 C ANISOU 1302 CA TYR A 203 7463 5499 6890 -941 680 614 C ATOM 1303 C TYR A 203 122.393 74.198 -13.364 1.00 55.85 C ANISOU 1303 C TYR A 203 7920 5836 7466 -886 617 556 C ATOM 1304 O TYR A 203 122.803 73.746 -12.288 1.00 60.28 O ANISOU 1304 O TYR A 203 8347 6479 8077 -859 590 423 O ATOM 1305 CB TYR A 203 123.742 74.506 -15.431 1.00 54.78 C ANISOU 1305 CB TYR A 203 7858 5764 7191 -1147 809 659 C ATOM 1306 CG TYR A 203 124.905 74.939 -14.578 1.00 89.14 C ANISOU 1306 CG TYR A 203 12092 10130 11648 -1280 873 513 C ATOM 1307 CD1 TYR A 203 125.956 74.072 -14.320 1.00 90.48 C ANISOU 1307 CD1 TYR A 203 12060 10495 11822 -1316 907 364 C ATOM 1308 CD2 TYR A 203 124.936 76.201 -13.998 1.00 97.46 C ANISOU 1308 CD2 TYR A 203 13225 10999 12806 -1360 888 508 C ATOM 1309 CE1 TYR A 203 127.014 74.453 -13.528 1.00 76.13 C ANISOU 1309 CE1 TYR A 203 10115 8708 10102 -1429 946 214 C ATOM 1310 CE2 TYR A 203 125.993 76.593 -13.206 1.00 94.80 C ANISOU 1310 CE2 TYR A 203 12767 10685 12567 -1488 938 353 C ATOM 1311 CZ TYR A 203 127.027 75.715 -12.975 1.00 89.01 C ANISOU 1311 CZ TYR A 203 11825 10167 11828 -1522 962 206 C ATOM 1312 OH TYR A 203 128.078 76.100 -12.185 1.00 93.97 O ANISOU 1312 OH TYR A 203 12316 10834 12555 -1642 995 37 O ATOM 1313 N ILE A 204 121.586 75.259 -13.439 1.00 38.75 N ANISOU 1313 N ILE A 204 5908 3475 5341 -863 590 649 N ATOM 1314 CA ILE A 204 121.010 75.857 -12.237 1.00 50.01 C ANISOU 1314 CA ILE A 204 7340 4784 6879 -791 530 583 C ATOM 1315 C ILE A 204 120.405 74.775 -11.350 1.00 54.77 C ANISOU 1315 C ILE A 204 7825 5508 7476 -637 450 501 C ATOM 1316 O ILE A 204 120.796 74.605 -10.190 1.00 65.83 O ANISOU 1316 O ILE A 204 9128 6966 8920 -636 439 373 O ATOM 1317 CB ILE A 204 119.968 76.923 -12.620 1.00 51.42 C ANISOU 1317 CB ILE A 204 7697 4741 7100 -732 489 706 C ATOM 1318 CG1 ILE A 204 120.631 78.065 -13.395 1.00 59.49 C ANISOU 1318 CG1 ILE A 204 8861 5611 8132 -901 577 799 C ATOM 1319 CG2 ILE A 204 119.266 77.449 -11.398 1.00 49.29 C ANISOU 1319 CG2 ILE A 204 7417 4364 6947 -638 431 615 C ATOM 1320 CD1 ILE A 204 119.655 79.062 -13.987 1.00 74.52 C ANISOU 1320 CD1 ILE A 204 10968 7286 10062 -832 525 955 C ATOM 1321 N ALA A 205 119.470 73.998 -11.905 1.00 41.24 N ANISOU 1321 N ALA A 205 6125 3843 5702 -515 396 574 N ATOM 1322 CA ALA A 205 118.847 72.905 -11.159 1.00 49.59 C ANISOU 1322 CA ALA A 205 7083 5004 6753 -386 337 511 C ATOM 1323 C ALA A 205 119.872 71.884 -10.670 1.00 46.80 C ANISOU 1323 C ALA A 205 6594 4818 6370 -419 358 414 C ATOM 1324 O ALA A 205 119.674 71.265 -9.620 1.00 66.40 O ANISOU 1324 O ALA A 205 9006 7360 8865 -346 320 341 O ATOM 1325 CB ALA A 205 117.792 72.209 -12.025 1.00 48.44 C ANISOU 1325 CB ALA A 205 6964 4890 6551 -279 286 596 C ATOM 1326 N LEU A 206 120.960 71.678 -11.415 1.00 39.10 N ANISOU 1326 N LEU A 206 5581 3922 5353 -523 418 411 N ATOM 1327 CA LEU A 206 122.026 70.804 -10.933 1.00 47.91 C ANISOU 1327 CA LEU A 206 6553 5188 6463 -544 428 303 C ATOM 1328 C LEU A 206 122.698 71.391 -9.697 1.00 50.12 C ANISOU 1328 C LEU A 206 6777 5460 6807 -593 420 191 C ATOM 1329 O LEU A 206 122.960 70.675 -8.724 1.00 55.29 O ANISOU 1329 O LEU A 206 7339 6208 7460 -529 368 108 O ATOM 1330 CB LEU A 206 123.053 70.551 -12.047 1.00 49.30 C ANISOU 1330 CB LEU A 206 6684 5455 6591 -651 508 303 C ATOM 1331 CG LEU A 206 124.267 69.696 -11.667 1.00 53.90 C ANISOU 1331 CG LEU A 206 7098 6196 7187 -667 516 175 C ATOM 1332 CD1 LEU A 206 123.806 68.328 -11.213 1.00 72.51 C ANISOU 1332 CD1 LEU A 206 9396 8626 9528 -511 436 156 C ATOM 1333 CD2 LEU A 206 125.262 69.567 -12.816 1.00 69.92 C ANISOU 1333 CD2 LEU A 206 9072 8316 9177 -786 617 154 C ATOM 1334 N VAL A 207 122.971 72.696 -9.710 1.00 45.33 N ANISOU 1334 N VAL A 207 6234 4736 6253 -706 466 187 N ATOM 1335 CA VAL A 207 123.668 73.316 -8.589 1.00 52.61 C ANISOU 1335 CA VAL A 207 7096 5655 7239 -771 460 56 C ATOM 1336 C VAL A 207 122.739 73.449 -7.391 1.00 52.80 C ANISOU 1336 C VAL A 207 7152 5628 7282 -659 388 20 C ATOM 1337 O VAL A 207 123.039 72.966 -6.292 1.00 52.96 O ANISOU 1337 O VAL A 207 7088 5751 7285 -613 336 -81 O ATOM 1338 CB VAL A 207 124.244 74.679 -9.010 1.00 47.36 C ANISOU 1338 CB VAL A 207 6495 4860 6640 -945 545 54 C ATOM 1339 CG1 VAL A 207 124.829 75.399 -7.811 1.00 47.00 C ANISOU 1339 CG1 VAL A 207 6390 4795 6671 -1013 532 -101 C ATOM 1340 CG2 VAL A 207 125.295 74.490 -10.080 1.00 53.79 C ANISOU 1340 CG2 VAL A 207 7256 5758 7424 -1079 638 66 C ATOM 1341 N VAL A 208 121.589 74.086 -7.591 1.00 52.36 N ANISOU 1341 N VAL A 208 7218 5421 7254 -606 383 99 N ATOM 1342 CA VAL A 208 120.747 74.492 -6.474 1.00 58.45 C ANISOU 1342 CA VAL A 208 8019 6127 8062 -525 341 39 C ATOM 1343 C VAL A 208 119.827 73.363 -6.012 1.00 63.77 C ANISOU 1343 C VAL A 208 8662 6892 8675 -378 290 57 C ATOM 1344 O VAL A 208 119.539 73.248 -4.816 1.00 71.71 O ANISOU 1344 O VAL A 208 9642 7936 9667 -326 263 -27 O ATOM 1345 CB VAL A 208 119.941 75.743 -6.868 1.00 64.15 C ANISOU 1345 CB VAL A 208 8873 6634 8866 -526 357 98 C ATOM 1346 CG1 VAL A 208 119.102 76.252 -5.694 1.00 73.15 C ANISOU 1346 CG1 VAL A 208 10029 7705 10059 -446 326 4 C ATOM 1347 CG2 VAL A 208 120.867 76.830 -7.385 1.00 59.52 C ANISOU 1347 CG2 VAL A 208 8338 5934 8341 -692 422 99 C ATOM 1348 N GLY A 209 119.371 72.515 -6.929 1.00 58.50 N ANISOU 1348 N GLY A 209 8000 6264 7964 -320 284 159 N ATOM 1349 CA GLY A 209 118.457 71.451 -6.563 1.00 47.56 C ANISOU 1349 CA GLY A 209 6588 4945 6537 -200 250 176 C ATOM 1350 C GLY A 209 119.097 70.109 -6.271 1.00 50.58 C ANISOU 1350 C GLY A 209 6884 5480 6854 -178 231 155 C ATOM 1351 O GLY A 209 118.432 69.210 -5.748 1.00 56.75 O ANISOU 1351 O GLY A 209 7653 6309 7602 -93 210 162 O ATOM 1352 N CYS A 210 120.380 69.949 -6.591 1.00 53.92 N ANISOU 1352 N CYS A 210 7246 5975 7265 -252 242 125 N ATOM 1353 CA CYS A 210 121.023 68.655 -6.390 1.00 68.16 C ANISOU 1353 CA CYS A 210 8964 7911 9023 -210 211 102 C ATOM 1354 C CYS A 210 122.315 68.782 -5.597 1.00 64.60 C ANISOU 1354 C CYS A 210 8427 7546 8571 -258 185 -7 C ATOM 1355 O CYS A 210 122.423 68.250 -4.489 1.00 64.04 O ANISOU 1355 O CYS A 210 8329 7544 8459 -194 126 -51 O ATOM 1356 CB CYS A 210 121.295 67.977 -7.736 1.00 63.10 C ANISOU 1356 CB CYS A 210 8296 7308 8369 -221 239 155 C ATOM 1357 SG CYS A 210 122.004 66.325 -7.599 1.00 69.62 S ANISOU 1357 SG CYS A 210 9018 8266 9167 -147 199 121 S ATOM 1358 N LEU A 211 123.300 69.486 -6.155 1.00 62.48 N ANISOU 1358 N LEU A 211 8115 7282 8342 -375 226 -52 N ATOM 1359 CA LEU A 211 124.620 69.516 -5.531 1.00 47.54 C ANISOU 1359 CA LEU A 211 6106 5496 6462 -425 196 -176 C ATOM 1360 C LEU A 211 124.599 70.262 -4.202 1.00 50.90 C ANISOU 1360 C LEU A 211 6545 5907 6887 -435 152 -267 C ATOM 1361 O LEU A 211 125.206 69.810 -3.224 1.00 49.68 O ANISOU 1361 O LEU A 211 6316 5866 6694 -391 74 -351 O ATOM 1362 CB LEU A 211 125.651 70.124 -6.486 1.00 56.18 C ANISOU 1362 CB LEU A 211 7140 6599 7607 -573 275 -215 C ATOM 1363 CG LEU A 211 125.929 69.287 -7.735 1.00 62.95 C ANISOU 1363 CG LEU A 211 7957 7517 8446 -570 321 -164 C ATOM 1364 CD1 LEU A 211 126.956 69.944 -8.653 1.00 62.26 C ANISOU 1364 CD1 LEU A 211 7813 7449 8394 -739 424 -208 C ATOM 1365 CD2 LEU A 211 126.367 67.886 -7.353 1.00 54.08 C ANISOU 1365 CD2 LEU A 211 6724 6525 7299 -448 245 -209 C ATOM 1366 N LEU A 212 123.907 71.408 -4.120 1.00 50.47 N ANISOU 1366 N LEU A 212 6588 5716 6873 -484 193 -259 N ATOM 1367 CA LEU A 212 123.795 72.109 -2.861 1.00 51.16 C ANISOU 1367 CA LEU A 212 6692 5789 6959 -490 159 -363 C ATOM 1368 C LEU A 212 123.160 71.251 -1.774 1.00 58.20 C ANISOU 1368 C LEU A 212 7601 6758 7753 -357 92 -358 C ATOM 1369 O LEU A 212 123.743 71.116 -0.686 1.00 70.31 O ANISOU 1369 O LEU A 212 9084 8400 9229 -343 24 -459 O ATOM 1370 CB LEU A 212 123.036 73.434 -3.036 1.00 65.08 C ANISOU 1370 CB LEU A 212 8564 7366 8798 -544 217 -353 C ATOM 1371 CG LEU A 212 122.751 74.122 -1.688 1.00 69.64 C ANISOU 1371 CG LEU A 212 9163 7925 9372 -535 188 -479 C ATOM 1372 CD1 LEU A 212 124.034 74.608 -1.021 1.00 90.50 C ANISOU 1372 CD1 LEU A 212 11710 10645 12029 -640 159 -644 C ATOM 1373 CD2 LEU A 212 121.716 75.234 -1.808 1.00 67.39 C ANISOU 1373 CD2 LEU A 212 8991 7444 9170 -537 236 -464 C ATOM 1374 N PRO A 213 121.978 70.652 -1.988 1.00 66.20 N ANISOU 1374 N PRO A 213 8686 7728 8737 -264 108 -248 N ATOM 1375 CA PRO A 213 121.403 69.826 -0.922 1.00 61.00 C ANISOU 1375 CA PRO A 213 8054 7143 7982 -162 65 -240 C ATOM 1376 C PRO A 213 122.208 68.580 -0.644 1.00 54.23 C ANISOU 1376 C PRO A 213 7133 6420 7053 -103 -7 -228 C ATOM 1377 O PRO A 213 122.240 68.136 0.505 1.00 70.49 O ANISOU 1377 O PRO A 213 9208 8561 9015 -46 -65 -254 O ATOM 1378 CB PRO A 213 120.003 69.491 -1.449 1.00 46.60 C ANISOU 1378 CB PRO A 213 6300 5234 6173 -101 115 -133 C ATOM 1379 CG PRO A 213 119.708 70.543 -2.433 1.00 64.49 C ANISOU 1379 CG PRO A 213 8597 7368 8538 -159 165 -113 C ATOM 1380 CD PRO A 213 121.021 70.819 -3.094 1.00 49.28 C ANISOU 1380 CD PRO A 213 6612 5467 6646 -254 165 -138 C ATOM 1381 N PHE A 214 122.876 68.008 -1.648 1.00 64.47 N ANISOU 1381 N PHE A 214 8363 7742 8391 -110 -8 -191 N ATOM 1382 CA PHE A 214 123.735 66.858 -1.383 1.00 49.61 C ANISOU 1382 CA PHE A 214 6408 5976 6465 -38 -88 -197 C ATOM 1383 C PHE A 214 124.879 67.236 -0.451 1.00 57.38 C ANISOU 1383 C PHE A 214 7310 7070 7420 -61 -172 -328 C ATOM 1384 O PHE A 214 125.189 66.506 0.496 1.00 57.29 O ANISOU 1384 O PHE A 214 7294 7153 7322 30 -269 -337 O ATOM 1385 CB PHE A 214 124.284 66.269 -2.682 1.00 46.66 C ANISOU 1385 CB PHE A 214 5960 5612 6155 -47 -62 -166 C ATOM 1386 CG PHE A 214 125.258 65.140 -2.459 1.00 60.83 C ANISOU 1386 CG PHE A 214 7662 7517 7933 38 -150 -194 C ATOM 1387 CD1 PHE A 214 124.826 63.922 -1.950 1.00 61.56 C ANISOU 1387 CD1 PHE A 214 7810 7614 7968 164 -206 -115 C ATOM 1388 CD2 PHE A 214 126.601 65.294 -2.767 1.00 62.49 C ANISOU 1388 CD2 PHE A 214 7728 7818 8197 -7 -173 -302 C ATOM 1389 CE1 PHE A 214 125.716 62.884 -1.742 1.00 67.72 C ANISOU 1389 CE1 PHE A 214 8515 8471 8744 262 -300 -133 C ATOM 1390 CE2 PHE A 214 127.498 64.257 -2.566 1.00 77.73 C ANISOU 1390 CE2 PHE A 214 9557 9848 10128 94 -267 -341 C ATOM 1391 CZ PHE A 214 127.054 63.051 -2.054 1.00 80.99 C ANISOU 1391 CZ PHE A 214 10040 10249 10485 238 -339 -251 C ATOM 1392 N PHE A 215 125.515 68.380 -0.705 1.00 50.94 N ANISOU 1392 N PHE A 215 6436 6244 6677 -183 -138 -431 N ATOM 1393 CA PHE A 215 126.606 68.831 0.153 1.00 46.65 C ANISOU 1393 CA PHE A 215 5795 5810 6121 -222 -218 -584 C ATOM 1394 C PHE A 215 126.105 69.153 1.555 1.00 48.15 C ANISOU 1394 C PHE A 215 6064 6026 6206 -186 -272 -631 C ATOM 1395 O PHE A 215 126.751 68.803 2.551 1.00 58.18 O ANISOU 1395 O PHE A 215 7287 7430 7387 -130 -389 -705 O ATOM 1396 CB PHE A 215 127.287 70.049 -0.472 1.00 62.52 C ANISOU 1396 CB PHE A 215 7735 7775 8245 -389 -145 -686 C ATOM 1397 CG PHE A 215 128.067 69.736 -1.721 1.00 81.08 C ANISOU 1397 CG PHE A 215 9982 10149 10675 -443 -92 -675 C ATOM 1398 CD1 PHE A 215 128.450 68.433 -2.011 1.00 86.58 C ANISOU 1398 CD1 PHE A 215 10608 10940 11350 -333 -145 -635 C ATOM 1399 CD2 PHE A 215 128.408 70.744 -2.611 1.00 89.66 C ANISOU 1399 CD2 PHE A 215 11052 11158 11859 -608 19 -705 C ATOM 1400 CE1 PHE A 215 129.168 68.146 -3.159 1.00 69.84 C ANISOU 1400 CE1 PHE A 215 8383 8853 9299 -384 -85 -648 C ATOM 1401 CE2 PHE A 215 129.123 70.462 -3.762 1.00 89.26 C ANISOU 1401 CE2 PHE A 215 10910 11144 11861 -672 87 -700 C ATOM 1402 CZ PHE A 215 129.502 69.163 -4.035 1.00 76.85 C ANISOU 1402 CZ PHE A 215 9252 9685 10264 -558 37 -682 C ATOM 1403 N THR A 216 124.950 69.814 1.650 1.00 43.76 N ANISOU 1403 N THR A 216 5624 5350 5652 -210 -192 -596 N ATOM 1404 CA THR A 216 124.371 70.136 2.952 1.00 41.96 C ANISOU 1404 CA THR A 216 5473 5150 5319 -181 -218 -653 C ATOM 1405 C THR A 216 124.060 68.872 3.744 1.00 48.16 C ANISOU 1405 C THR A 216 6315 6032 5952 -50 -287 -566 C ATOM 1406 O THR A 216 124.419 68.757 4.925 1.00 56.58 O ANISOU 1406 O THR A 216 7390 7219 6889 -14 -378 -635 O ATOM 1407 CB THR A 216 123.108 70.968 2.743 1.00 41.89 C ANISOU 1407 CB THR A 216 5564 4986 5365 -213 -109 -628 C ATOM 1408 OG1 THR A 216 123.435 72.147 1.997 1.00 53.69 O ANISOU 1408 OG1 THR A 216 7032 6367 7002 -332 -50 -689 O ATOM 1409 CG2 THR A 216 122.497 71.365 4.064 1.00 46.50 C ANISOU 1409 CG2 THR A 216 6218 5604 5847 -192 -114 -713 C ATOM 1410 N LEU A 217 123.376 67.920 3.102 1.00 69.21 N ANISOU 1410 N LEU A 217 9029 8641 8627 15 -246 -413 N ATOM 1411 CA LEU A 217 123.069 66.621 3.689 1.00 57.11 C ANISOU 1411 CA LEU A 217 7563 7164 6972 128 -295 -305 C ATOM 1412 C LEU A 217 124.339 65.938 4.180 1.00 62.57 C ANISOU 1412 C LEU A 217 8184 7990 7598 196 -441 -337 C ATOM 1413 O LEU A 217 124.431 65.487 5.331 1.00 63.02 O ANISOU 1413 O LEU A 217 8302 8140 7501 266 -528 -328 O ATOM 1414 CB LEU A 217 122.387 65.754 2.627 1.00 61.08 C ANISOU 1414 CB LEU A 217 8092 7572 7545 164 -228 -164 C ATOM 1415 CG LEU A 217 121.652 64.455 2.958 1.00 66.39 C ANISOU 1415 CG LEU A 217 8859 8232 8136 252 -224 -29 C ATOM 1416 CD1 LEU A 217 120.300 64.794 3.509 1.00 69.21 C ANISOU 1416 CD1 LEU A 217 9315 8542 8441 228 -127 -10 C ATOM 1417 CD2 LEU A 217 121.519 63.537 1.755 1.00 81.39 C ANISOU 1417 CD2 LEU A 217 10732 10059 10133 284 -195 65 C ATOM 1418 N SER A 218 125.342 65.868 3.303 1.00 62.23 N ANISOU 1418 N SER A 218 8010 7965 7669 179 -471 -378 N ATOM 1419 CA SER A 218 126.579 65.175 3.630 1.00 63.20 C ANISOU 1419 CA SER A 218 8035 8216 7764 261 -617 -422 C ATOM 1420 C SER A 218 127.256 65.799 4.837 1.00 66.31 C ANISOU 1420 C SER A 218 8394 8744 8059 251 -728 -563 C ATOM 1421 O SER A 218 127.684 65.093 5.751 1.00 82.18 O ANISOU 1421 O SER A 218 10422 10861 9940 363 -869 -549 O ATOM 1422 CB SER A 218 127.509 65.195 2.421 1.00 58.25 C ANISOU 1422 CB SER A 218 7248 7592 7292 218 -599 -479 C ATOM 1423 OG SER A 218 126.916 64.507 1.342 1.00 76.89 O ANISOU 1423 OG SER A 218 9645 9850 9721 240 -511 -357 O ATOM 1424 N ILE A 219 127.349 67.131 4.862 1.00 52.94 N ANISOU 1424 N ILE A 219 6657 7038 6420 118 -673 -700 N ATOM 1425 CA ILE A 219 128.055 67.803 5.950 1.00 63.28 C ANISOU 1425 CA ILE A 219 7914 8480 7650 90 -779 -870 C ATOM 1426 C ILE A 219 127.316 67.624 7.271 1.00 57.26 C ANISOU 1426 C ILE A 219 7306 7770 6680 156 -820 -835 C ATOM 1427 O ILE A 219 127.933 67.337 8.305 1.00 50.92 O ANISOU 1427 O ILE A 219 6495 7122 5732 228 -973 -892 O ATOM 1428 CB ILE A 219 128.269 69.290 5.610 1.00 60.43 C ANISOU 1428 CB ILE A 219 7482 8060 7417 -84 -691 -1029 C ATOM 1429 CG1 ILE A 219 129.216 69.438 4.414 1.00 55.28 C ANISOU 1429 CG1 ILE A 219 6669 7392 6944 -164 -655 -1077 C ATOM 1430 CG2 ILE A 219 128.769 70.066 6.825 1.00 56.62 C ANISOU 1430 CG2 ILE A 219 6966 7699 6847 -125 -785 -1222 C ATOM 1431 CD1 ILE A 219 130.592 68.858 4.645 1.00 77.22 C ANISOU 1431 CD1 ILE A 219 9272 10347 9721 -105 -807 -1179 C ATOM 1432 N CYS A 220 125.990 67.794 7.268 1.00 45.86 N ANISOU 1432 N CYS A 220 6002 6211 5212 133 -687 -746 N ATOM 1433 CA CYS A 220 125.233 67.598 8.502 1.00 64.66 C ANISOU 1433 CA CYS A 220 8531 8649 7387 181 -696 -715 C ATOM 1434 C CYS A 220 125.420 66.189 9.041 1.00 76.35 C ANISOU 1434 C CYS A 220 10084 10212 8712 324 -811 -570 C ATOM 1435 O CYS A 220 125.647 65.994 10.244 1.00 86.65 O ANISOU 1435 O CYS A 220 11457 11653 9814 379 -919 -593 O ATOM 1436 CB CYS A 220 123.746 67.879 8.271 1.00 71.33 C ANISOU 1436 CB CYS A 220 9488 9355 8260 140 -522 -643 C ATOM 1437 SG CYS A 220 123.337 69.604 7.914 1.00 87.80 S ANISOU 1437 SG CYS A 220 11534 11324 10501 0 -400 -808 S ATOM 1438 N TYR A 221 125.362 65.191 8.158 1.00 74.58 N ANISOU 1438 N TYR A 221 9855 9904 8577 387 -794 -421 N ATOM 1439 CA TYR A 221 125.464 63.812 8.622 1.00 76.11 C ANISOU 1439 CA TYR A 221 10140 10134 8646 526 -894 -268 C ATOM 1440 C TYR A 221 126.888 63.433 9.011 1.00 72.11 C ANISOU 1440 C TYR A 221 9530 9769 8099 625 -1107 -332 C ATOM 1441 O TYR A 221 127.082 62.609 9.914 1.00 78.78 O ANISOU 1441 O TYR A 221 10474 10690 8768 745 -1236 -244 O ATOM 1442 CB TYR A 221 124.913 62.876 7.557 1.00 80.27 C ANISOU 1442 CB TYR A 221 10692 10512 9296 558 -805 -109 C ATOM 1443 CG TYR A 221 123.409 62.886 7.535 1.00 82.05 C ANISOU 1443 CG TYR A 221 11050 10628 9498 501 -634 -16 C ATOM 1444 CD1 TYR A 221 122.689 63.381 8.618 1.00 93.01 C ANISOU 1444 CD1 TYR A 221 12550 12066 10725 460 -584 -43 C ATOM 1445 CD2 TYR A 221 122.706 62.402 6.445 1.00 85.45 C ANISOU 1445 CD2 TYR A 221 11483 10919 10067 487 -522 80 C ATOM 1446 CE1 TYR A 221 121.314 63.390 8.614 1.00 95.91 C ANISOU 1446 CE1 TYR A 221 13012 12346 11082 407 -420 20 C ATOM 1447 CE2 TYR A 221 121.328 62.410 6.431 1.00 90.11 C ANISOU 1447 CE2 TYR A 221 12168 11421 10647 436 -373 145 C ATOM 1448 CZ TYR A 221 120.639 62.900 7.520 1.00 93.88 C ANISOU 1448 CZ TYR A 221 12742 11951 10976 397 -320 114 C ATOM 1449 OH TYR A 221 119.261 62.917 7.513 1.00 83.44 O ANISOU 1449 OH TYR A 221 11491 10554 9658 346 -164 158 O ATOM 1450 N LEU A 222 127.895 64.032 8.374 1.00 56.71 N ANISOU 1450 N LEU A 222 7382 7861 6305 578 -1147 -487 N ATOM 1451 CA LEU A 222 129.269 63.805 8.808 1.00 66.04 C ANISOU 1451 CA LEU A 222 8430 9202 7459 667 -1355 -591 C ATOM 1452 C LEU A 222 129.504 64.407 10.189 1.00 66.76 C ANISOU 1452 C LEU A 222 8560 9454 7351 662 -1471 -708 C ATOM 1453 O LEU A 222 130.143 63.784 11.043 1.00 78.58 O ANISOU 1453 O LEU A 222 10073 11085 8697 797 -1668 -695 O ATOM 1454 CB LEU A 222 130.261 64.380 7.790 1.00 81.80 C ANISOU 1454 CB LEU A 222 10189 11214 9678 586 -1343 -752 C ATOM 1455 CG LEU A 222 130.307 63.741 6.396 1.00 88.51 C ANISOU 1455 CG LEU A 222 10969 11948 10714 600 -1255 -670 C ATOM 1456 CD1 LEU A 222 131.292 64.463 5.473 1.00 96.16 C ANISOU 1456 CD1 LEU A 222 11709 12953 11875 487 -1217 -846 C ATOM 1457 CD2 LEU A 222 130.608 62.254 6.477 1.00 80.50 C ANISOU 1457 CD2 LEU A 222 9982 10939 9665 794 -1383 -541 C ATOM 1458 N LEU A 223 128.966 65.608 10.438 1.00 55.74 N ANISOU 1458 N LEU A 223 7188 8045 5945 517 -1356 -824 N ATOM 1459 CA LEU A 223 129.078 66.220 11.762 1.00 51.10 C ANISOU 1459 CA LEU A 223 6649 7610 5157 501 -1447 -953 C ATOM 1460 C LEU A 223 128.358 65.389 12.822 1.00 65.60 C ANISOU 1460 C LEU A 223 8714 9491 6720 607 -1485 -785 C ATOM 1461 O LEU A 223 128.844 65.258 13.958 1.00 61.41 O ANISOU 1461 O LEU A 223 8226 9135 5971 680 -1656 -832 O ATOM 1462 CB LEU A 223 128.525 67.648 11.727 1.00 50.11 C ANISOU 1462 CB LEU A 223 6516 7424 5102 326 -1292 -1110 C ATOM 1463 CG LEU A 223 129.254 68.657 10.830 1.00 59.17 C ANISOU 1463 CG LEU A 223 7462 8523 6496 191 -1246 -1288 C ATOM 1464 CD1 LEU A 223 128.522 69.989 10.775 1.00 65.41 C ANISOU 1464 CD1 LEU A 223 8289 9200 7362 35 -1082 -1402 C ATOM 1465 CD2 LEU A 223 130.689 68.862 11.268 1.00 65.99 C ANISOU 1465 CD2 LEU A 223 8144 9574 7356 200 -1438 -1484 C ATOM 1466 N ILE A 224 127.206 64.810 12.466 1.00 53.76 N ANISOU 1466 N ILE A 224 7362 7840 5223 609 -1329 -591 N ATOM 1467 CA ILE A 224 126.484 63.953 13.406 1.00 60.49 C ANISOU 1467 CA ILE A 224 8441 8718 5826 688 -1335 -414 C ATOM 1468 C ILE A 224 127.283 62.688 13.709 1.00 61.64 C ANISOU 1468 C ILE A 224 8623 8924 5875 867 -1542 -277 C ATOM 1469 O ILE A 224 127.402 62.275 14.870 1.00 68.54 O ANISOU 1469 O ILE A 224 9637 9923 6484 951 -1669 -218 O ATOM 1470 CB ILE A 224 125.081 63.614 12.870 1.00 59.93 C ANISOU 1470 CB ILE A 224 8491 8465 5813 635 -1110 -255 C ATOM 1471 CG1 ILE A 224 124.210 64.871 12.818 1.00 63.23 C ANISOU 1471 CG1 ILE A 224 8896 8839 6288 486 -928 -393 C ATOM 1472 CG2 ILE A 224 124.422 62.584 13.754 1.00 64.35 C ANISOU 1472 CG2 ILE A 224 9280 9037 6133 704 -1105 -56 C ATOM 1473 CD1 ILE A 224 122.901 64.683 12.090 1.00 65.29 C ANISOU 1473 CD1 ILE A 224 9219 8925 6664 433 -718 -277 C ATOM 1474 N ILE A 225 127.822 62.042 12.672 1.00 64.83 N ANISOU 1474 N ILE A 225 8911 9236 6485 934 -1578 -221 N ATOM 1475 CA ILE A 225 128.693 60.886 12.884 1.00 60.16 C ANISOU 1475 CA ILE A 225 8325 8690 5845 1123 -1792 -119 C ATOM 1476 C ILE A 225 129.859 61.256 13.789 1.00 63.41 C ANISOU 1476 C ILE A 225 8642 9327 6125 1195 -2035 -278 C ATOM 1477 O ILE A 225 130.274 60.474 14.652 1.00 73.33 O ANISOU 1477 O ILE A 225 10003 10674 7186 1354 -2232 -180 O ATOM 1478 CB ILE A 225 129.177 60.331 11.531 1.00 61.42 C ANISOU 1478 CB ILE A 225 8326 8730 6282 1168 -1779 -100 C ATOM 1479 CG1 ILE A 225 128.010 59.691 10.771 1.00 75.81 C ANISOU 1479 CG1 ILE A 225 10273 10339 8191 1131 -1578 84 C ATOM 1480 CG2 ILE A 225 130.325 59.360 11.723 1.00 52.75 C ANISOU 1480 CG2 ILE A 225 7166 7700 5177 1373 -2027 -68 C ATOM 1481 CD1 ILE A 225 128.337 59.308 9.346 1.00 84.43 C ANISOU 1481 CD1 ILE A 225 11211 11315 9552 1141 -1527 75 C ATOM 1482 N ARG A 226 130.391 62.463 13.614 1.00 61.66 N ANISOU 1482 N ARG A 226 8224 9195 6007 1077 -2028 -528 N ATOM 1483 CA ARG A 226 131.517 62.930 14.415 1.00 72.29 C ANISOU 1483 CA ARG A 226 9444 10767 7254 1121 -2254 -725 C ATOM 1484 C ARG A 226 131.148 63.072 15.890 1.00 73.17 C ANISOU 1484 C ARG A 226 9752 11024 7025 1142 -2334 -711 C ATOM 1485 O ARG A 226 131.889 62.609 16.769 1.00 98.38 O ANISOU 1485 O ARG A 226 12968 14385 10028 1290 -2583 -710 O ATOM 1486 CB ARG A 226 132.007 64.248 13.820 1.00 76.86 C ANISOU 1486 CB ARG A 226 9786 11373 8044 948 -2178 -994 C ATOM 1487 CG ARG A 226 133.071 64.992 14.567 1.00 83.61 C ANISOU 1487 CG ARG A 226 10480 12452 8835 934 -2367 -1252 C ATOM 1488 CD ARG A 226 133.519 66.152 13.698 1.00 94.40 C ANISOU 1488 CD ARG A 226 11614 13781 10472 745 -2249 -1483 C ATOM 1489 NE ARG A 226 134.335 67.110 14.424 1.00120.58 N ANISOU 1489 NE ARG A 226 14784 17288 13743 672 -2377 -1765 N ATOM 1490 CZ ARG A 226 133.831 68.171 15.045 1.00135.56 C ANISOU 1490 CZ ARG A 226 16752 19205 15552 533 -2294 -1900 C ATOM 1491 NH1 ARG A 226 132.522 68.392 15.018 1.00134.68 N ANISOU 1491 NH1 ARG A 226 16844 18939 15390 464 -2086 -1776 N ATOM 1492 NH2 ARG A 226 134.629 69.009 15.690 1.00141.69 N ANISOU 1492 NH2 ARG A 226 17383 20156 16298 464 -2420 -2177 N ATOM 1493 N VAL A 227 130.004 63.697 16.188 1.00 63.70 N ANISOU 1493 N VAL A 227 8697 9771 5735 1003 -2130 -706 N ATOM 1494 CA VAL A 227 129.608 63.839 17.590 1.00 74.94 C ANISOU 1494 CA VAL A 227 10314 11344 6817 1010 -2180 -704 C ATOM 1495 C VAL A 227 129.301 62.472 18.195 1.00 75.92 C ANISOU 1495 C VAL A 227 10683 11457 6706 1168 -2262 -416 C ATOM 1496 O VAL A 227 129.597 62.218 19.372 1.00 64.57 O ANISOU 1496 O VAL A 227 9373 10196 4963 1260 -2440 -391 O ATOM 1497 CB VAL A 227 128.416 64.810 17.752 1.00 69.30 C ANISOU 1497 CB VAL A 227 9685 10571 6075 829 -1926 -781 C ATOM 1498 CG1 VAL A 227 128.729 66.161 17.142 1.00 78.99 C ANISOU 1498 CG1 VAL A 227 10693 11774 7546 677 -1849 -1050 C ATOM 1499 CG2 VAL A 227 127.133 64.234 17.183 1.00 84.36 C ANISOU 1499 CG2 VAL A 227 11741 12267 8044 795 -1692 -558 C ATOM 1500 N LEU A 228 128.710 61.566 17.403 1.00 59.94 N ANISOU 1500 N LEU A 228 8736 9224 4814 1200 -2139 -192 N ATOM 1501 CA LEU A 228 128.421 60.228 17.910 1.00 61.34 C ANISOU 1501 CA LEU A 228 9155 9351 4798 1339 -2205 93 C ATOM 1502 C LEU A 228 129.704 59.476 18.233 1.00 79.27 C ANISOU 1502 C LEU A 228 11380 11728 7011 1557 -2527 127 C ATOM 1503 O LEU A 228 129.795 58.802 19.267 1.00 83.64 O ANISOU 1503 O LEU A 228 12140 12367 7272 1681 -2683 278 O ATOM 1504 CB LEU A 228 127.583 59.438 16.903 1.00 58.97 C ANISOU 1504 CB LEU A 228 8919 8793 4694 1318 -2008 292 C ATOM 1505 CG LEU A 228 126.132 59.882 16.693 1.00 74.80 C ANISOU 1505 CG LEU A 228 11017 10683 6720 1137 -1700 318 C ATOM 1506 CD1 LEU A 228 125.459 59.048 15.614 1.00 69.88 C ANISOU 1506 CD1 LEU A 228 10419 9820 6313 1130 -1545 490 C ATOM 1507 CD2 LEU A 228 125.336 59.816 17.984 1.00 73.86 C ANISOU 1507 CD2 LEU A 228 11154 10655 6255 1098 -1637 408 C ATOM 1508 N LEU A 229 130.708 59.575 17.359 1.00 77.90 N ANISOU 1508 N LEU A 229 10935 11551 7112 1608 -2631 -12 N ATOM 1509 CA LEU A 229 131.984 58.927 17.634 1.00 69.27 C ANISOU 1509 CA LEU A 229 9751 10572 5995 1826 -2948 -19 C ATOM 1510 C LEU A 229 132.645 59.524 18.866 1.00 72.72 C ANISOU 1510 C LEU A 229 10177 11288 6165 1863 -3172 -179 C ATOM 1511 O LEU A 229 133.242 58.800 19.669 1.00 77.10 O ANISOU 1511 O LEU A 229 10828 11954 6515 2062 -3438 -81 O ATOM 1512 CB LEU A 229 132.912 59.033 16.423 1.00 76.52 C ANISOU 1512 CB LEU A 229 10348 11453 7272 1845 -2982 -180 C ATOM 1513 CG LEU A 229 132.480 58.266 15.168 1.00 82.81 C ANISOU 1513 CG LEU A 229 11140 11997 8329 1851 -2816 -32 C ATOM 1514 CD1 LEU A 229 133.463 58.474 14.022 1.00 88.14 C ANISOU 1514 CD1 LEU A 229 11487 12674 9329 1855 -2843 -223 C ATOM 1515 CD2 LEU A 229 132.299 56.782 15.456 1.00 88.36 C ANISOU 1515 CD2 LEU A 229 12068 12574 8930 2048 -2917 257 C ATOM 1516 N LYS A 230 132.538 60.842 19.044 1.00 73.97 N ANISOU 1516 N LYS A 230 10226 11558 6320 1679 -3075 -426 N ATOM 1517 CA LYS A 230 133.104 61.466 20.238 1.00 88.82 C ANISOU 1517 CA LYS A 230 12097 13712 7938 1695 -3276 -605 C ATOM 1518 C LYS A 230 132.463 60.910 21.505 1.00 83.20 C ANISOU 1518 C LYS A 230 11730 13074 6808 1765 -3326 -396 C ATOM 1519 O LYS A 230 133.163 60.489 22.442 1.00 76.70 O ANISOU 1519 O LYS A 230 10974 12437 5730 1934 -3615 -370 O ATOM 1520 CB LYS A 230 132.937 62.986 20.172 1.00 95.04 C ANISOU 1520 CB LYS A 230 12736 14564 8812 1464 -3121 -903 C ATOM 1521 CG LYS A 230 133.029 63.683 21.523 1.00 97.82 C ANISOU 1521 CG LYS A 230 13164 15166 8837 1431 -3238 -1067 C ATOM 1522 CD LYS A 230 134.254 64.584 21.602 1.00108.14 C ANISOU 1522 CD LYS A 230 14168 16670 10252 1399 -3424 -1415 C ATOM 1523 N VAL A 231 131.127 60.899 21.552 1.00 76.98 N ANISOU 1523 N VAL A 231 11162 12149 5936 1636 -3047 -248 N ATOM 1524 CA VAL A 231 130.462 60.456 22.774 1.00 75.31 C ANISOU 1524 CA VAL A 231 11282 12020 5313 1665 -3052 -63 C ATOM 1525 C VAL A 231 130.735 58.975 23.018 1.00 89.11 C ANISOU 1525 C VAL A 231 13224 13700 6931 1890 -3238 252 C ATOM 1526 O VAL A 231 130.954 58.554 24.161 1.00100.41 O ANISOU 1526 O VAL A 231 14862 15289 8000 2007 -3432 361 O ATOM 1527 CB VAL A 231 128.951 60.774 22.739 1.00 83.29 C ANISOU 1527 CB VAL A 231 12458 12902 6285 1467 -2692 5 C ATOM 1528 CG1 VAL A 231 128.718 62.276 22.552 1.00 90.98 C ANISOU 1528 CG1 VAL A 231 13247 13932 7390 1268 -2534 -315 C ATOM 1529 CG2 VAL A 231 128.221 59.971 21.674 1.00 92.50 C ANISOU 1529 CG2 VAL A 231 13671 13775 7699 1452 -2490 230 C ATOM 1530 N GLU A 232 130.785 58.170 21.949 1.00 97.04 N ANISOU 1530 N GLU A 232 14168 14473 8231 1961 -3196 396 N ATOM 1531 CA GLU A 232 131.027 56.738 22.107 1.00 99.51 C ANISOU 1531 CA GLU A 232 14667 14678 8463 2179 -3363 695 C ATOM 1532 C GLU A 232 132.447 56.463 22.584 1.00 79.27 C ANISOU 1532 C GLU A 232 11974 12285 5859 2391 -3735 625 C ATOM 1533 O GLU A 232 132.667 55.575 23.415 1.00 83.68 O ANISOU 1533 O GLU A 232 12700 12833 6261 2489 -3850 838 O ATOM 1534 CB GLU A 232 130.756 56.017 20.786 1.00 98.04 C ANISOU 1534 CB GLU A 232 14413 14199 8639 2189 -3215 818 C ATOM 1535 CG GLU A 232 130.954 54.510 20.829 1.00106.85 C ANISOU 1535 CG GLU A 232 15719 15152 9726 2408 -3363 1121 C ATOM 1536 CD GLU A 232 130.650 53.852 19.494 1.00111.33 C ANISOU 1536 CD GLU A 232 16206 15433 10659 2399 -3199 1206 C ATOM 1537 OE1 GLU A 232 130.304 54.576 18.535 1.00108.70 O ANISOU 1537 OE1 GLU A 232 15673 15047 10583 2228 -2982 1038 O ATOM 1538 OE2 GLU A 232 130.750 52.612 19.400 1.00112.24 O ANISOU 1538 OE2 GLU A 232 16469 15373 10803 2566 -3291 1442 O ATOM 1539 N ALA A1001 133.426 57.214 22.076 1.00107.39 N ANISOU 1539 N ALA A1001 19756 14735 6311 4613 1207 2348 N ATOM 1540 CA ALA A1001 134.803 57.033 22.519 1.00104.95 C ANISOU 1540 CA ALA A1001 19489 14054 6334 4696 1858 2315 C ATOM 1541 C ALA A1001 134.948 57.394 23.987 1.00107.99 C ANISOU 1541 C ALA A1001 19268 14181 7582 4444 1867 2310 C ATOM 1542 O ALA A1001 135.554 56.647 24.765 1.00105.30 O ANISOU 1542 O ALA A1001 18778 13578 7653 4234 1866 1947 O ATOM 1543 CB ALA A1001 135.748 57.874 21.662 1.00109.41 C ANISOU 1543 CB ALA A1001 20169 14475 6929 5038 2649 2699 C ATOM 1544 N ASP A1002 134.380 58.536 24.388 1.00108.16 N ANISOU 1544 N ASP A1002 18872 14257 7968 4445 1825 2662 N ATOM 1545 CA ASP A1002 134.470 58.937 25.789 1.00107.54 C ANISOU 1545 CA ASP A1002 18129 13960 8770 4180 1799 2578 C ATOM 1546 C ASP A1002 133.785 57.916 26.691 1.00109.79 C ANISOU 1546 C ASP A1002 18299 14346 9071 3764 1159 2141 C ATOM 1547 O ASP A1002 134.278 57.595 27.785 1.00108.24 O ANISOU 1547 O ASP A1002 17799 13914 9413 3545 1176 1903 O ATOM 1548 CB ASP A1002 133.841 60.315 25.978 1.00114.91 C ANISOU 1548 CB ASP A1002 18653 14961 10047 4270 1811 2982 C ATOM 1549 CG ASP A1002 134.502 61.383 25.122 1.00139.01 C ANISOU 1549 CG ASP A1002 21828 17839 13149 4663 2487 3493 C ATOM 1550 OD1 ASP A1002 135.693 61.231 24.764 1.00146.43 O ANISOU 1550 OD1 ASP A1002 22945 18516 14175 4801 3097 3496 O ATOM 1551 OD2 ASP A1002 133.821 62.384 24.811 1.00145.44 O ANISOU 1551 OD2 ASP A1002 22552 18758 13951 4836 2425 3900 O ATOM 1552 N LEU A1003 132.656 57.375 26.229 1.00115.70 N ANISOU 1552 N LEU A1003 19300 15434 9226 3658 592 2027 N ATOM 1553 CA LEU A1003 131.883 56.440 27.034 1.00113.17 C ANISOU 1553 CA LEU A1003 18859 15197 8944 3221 22 1650 C ATOM 1554 C LEU A1003 132.599 55.101 27.173 1.00106.80 C ANISOU 1554 C LEU A1003 18381 14137 8062 3080 17 1273 C ATOM 1555 O LEU A1003 132.605 54.506 28.254 1.00 94.69 O ANISOU 1555 O LEU A1003 16653 12437 6887 2748 -165 1052 O ATOM 1556 CB LEU A1003 130.493 56.286 26.412 1.00121.41 C ANISOU 1556 CB LEU A1003 20027 16650 9454 3162 -564 1598 C ATOM 1557 CG LEU A1003 129.374 55.498 27.088 1.00119.53 C ANISOU 1557 CG LEU A1003 19595 16563 9258 2687 -1167 1248 C ATOM 1558 CD1 LEU A1003 128.036 56.161 26.785 1.00117.49 C ANISOU 1558 CD1 LEU A1003 19082 16700 8860 2709 -1596 1343 C ATOM 1559 CD2 LEU A1003 129.385 54.077 26.560 1.00123.22 C ANISOU 1559 CD2 LEU A1003 20565 16987 9267 2556 -1440 853 C ATOM 1560 N GLU A1004 133.232 54.623 26.098 1.00110.20 N ANISOU 1560 N GLU A1004 19324 14522 8025 3351 233 1201 N ATOM 1561 CA GLU A1004 134.054 53.417 26.193 1.00106.01 C ANISOU 1561 CA GLU A1004 19081 13689 7509 3285 284 828 C ATOM 1562 C GLU A1004 135.240 53.636 27.125 1.00100.28 C ANISOU 1562 C GLU A1004 18031 12571 7502 3309 704 837 C ATOM 1563 O GLU A1004 135.585 52.758 27.931 1.00104.90 O ANISOU 1563 O GLU A1004 18599 12887 8370 3101 530 557 O ATOM 1564 CB GLU A1004 134.537 53.004 24.799 1.00113.77 C ANISOU 1564 CB GLU A1004 20643 14735 7851 3625 509 728 C ATOM 1565 CG GLU A1004 134.242 51.560 24.423 1.00120.92 C ANISOU 1565 CG GLU A1004 21981 15627 8338 3472 66 237 C ATOM 1566 N ASP A1005 135.869 54.811 27.034 1.00 98.58 N ANISOU 1566 N ASP A1005 17547 12295 7614 3571 1239 1154 N ATOM 1567 CA ASP A1005 137.006 55.120 27.893 1.00113.52 C ANISOU 1567 CA ASP A1005 19052 13822 10256 3619 1621 1110 C ATOM 1568 C ASP A1005 136.622 55.033 29.365 1.00109.11 C ANISOU 1568 C ASP A1005 18082 13212 10163 3287 1232 994 C ATOM 1569 O ASP A1005 137.301 54.369 30.158 1.00100.32 O ANISOU 1569 O ASP A1005 16913 11818 9386 3209 1165 735 O ATOM 1570 CB ASP A1005 137.545 56.510 27.553 1.00130.42 C ANISOU 1570 CB ASP A1005 20910 15908 12735 3903 2238 1482 C ATOM 1571 CG ASP A1005 138.791 56.863 28.339 1.00141.19 C ANISOU 1571 CG ASP A1005 21825 16882 14940 3978 2653 1366 C ATOM 1572 OD1 ASP A1005 139.877 56.331 28.021 1.00145.31 O ANISOU 1572 OD1 ASP A1005 22495 17150 15569 4143 2993 1148 O ATOM 1573 OD2 ASP A1005 138.681 57.678 29.279 1.00142.64 O ANISOU 1573 OD2 ASP A1005 21477 17018 15703 3884 2623 1444 O ATOM 1574 N ASN A1006 135.527 55.698 29.750 1.00102.85 N ANISOU 1574 N ASN A1006 17006 12697 9374 3110 966 1178 N ATOM 1575 CA ASN A1006 135.105 55.638 31.150 1.00 96.31 C ANISOU 1575 CA ASN A1006 15803 11876 8916 2788 645 1064 C ATOM 1576 C ASN A1006 134.633 54.239 31.540 1.00 97.92 C ANISOU 1576 C ASN A1006 16322 12058 8827 2453 168 796 C ATOM 1577 O ASN A1006 134.854 53.800 32.680 1.00 83.67 O ANISOU 1577 O ASN A1006 14390 10091 7309 2259 18 656 O ATOM 1578 CB ASN A1006 134.008 56.669 31.418 1.00 92.18 C ANISOU 1578 CB ASN A1006 14880 11667 8478 2683 505 1278 C ATOM 1579 CG ASN A1006 134.555 58.080 31.548 1.00104.48 C ANISOU 1579 CG ASN A1006 15984 13123 10592 2942 952 1503 C ATOM 1580 OD1 ASN A1006 135.560 58.306 32.226 1.00 96.96 O ANISOU 1580 OD1 ASN A1006 14763 11894 10183 3023 1216 1391 O ATOM 1581 ND2 ASN A1006 133.902 59.033 30.892 1.00119.77 N ANISOU 1581 ND2 ASN A1006 17823 15252 12431 3088 1015 1805 N ATOM 1582 N TRP A1007 133.972 53.538 30.616 1.00104.37 N ANISOU 1582 N TRP A1007 17557 13024 9075 2387 -81 722 N ATOM 1583 CA TRP A1007 133.586 52.151 30.835 1.00 91.27 C ANISOU 1583 CA TRP A1007 16228 11258 7190 2071 -492 447 C ATOM 1584 C TRP A1007 134.775 51.312 31.261 1.00 98.00 C ANISOU 1584 C TRP A1007 17279 11669 8288 2149 -384 248 C ATOM 1585 O TRP A1007 134.652 50.438 32.130 1.00101.79 O ANISOU 1585 O TRP A1007 17844 11954 8877 1863 -671 118 O ATOM 1586 CB TRP A1007 132.980 51.581 29.550 1.00 97.39 C ANISOU 1586 CB TRP A1007 17437 12211 7357 2104 -710 319 C ATOM 1587 CG TRP A1007 132.488 50.185 29.691 1.00105.66 C ANISOU 1587 CG TRP A1007 18793 13118 8237 1753 -1140 6 C ATOM 1588 CD1 TRP A1007 133.131 49.040 29.317 1.00105.64 C ANISOU 1588 CD1 TRP A1007 19233 12787 8117 1806 -1176 -282 C ATOM 1589 CD2 TRP A1007 131.235 49.783 30.241 1.00127.05 C ANISOU 1589 CD2 TRP A1007 21365 15970 10940 1281 -1569 -70 C ATOM 1590 NE1 TRP A1007 132.352 47.946 29.609 1.00120.69 N ANISOU 1590 NE1 TRP A1007 21306 14584 9965 1388 -1618 -511 N ATOM 1591 CE2 TRP A1007 131.180 48.377 30.175 1.00137.68 C ANISOU 1591 CE2 TRP A1007 23102 17026 12185 1043 -1843 -378 C ATOM 1592 CE3 TRP A1007 130.152 50.477 30.786 1.00134.62 C ANISOU 1592 CE3 TRP A1007 21879 17254 12016 1030 -1724 72 C ATOM 1593 CZ2 TRP A1007 130.085 47.654 30.636 1.00151.91 C ANISOU 1593 CZ2 TRP A1007 24866 18833 14019 533 -2230 -518 C ATOM 1594 CZ3 TRP A1007 129.071 49.758 31.243 1.00141.81 C ANISOU 1594 CZ3 TRP A1007 22732 18213 12937 534 -2096 -93 C ATOM 1595 CH2 TRP A1007 129.042 48.362 31.162 1.00148.83 C ANISOU 1595 CH2 TRP A1007 24018 18790 13740 275 -2330 -371 C ATOM 1596 N GLU A1008 135.934 51.550 30.642 1.00102.99 N ANISOU 1596 N GLU A1008 17992 12120 9020 2544 40 229 N ATOM 1597 CA GLU A1008 137.078 50.687 30.913 1.00103.72 C ANISOU 1597 CA GLU A1008 18265 11782 9360 2668 111 -24 C ATOM 1598 C GLU A1008 137.601 50.907 32.329 1.00 98.84 C ANISOU 1598 C GLU A1008 17275 10967 9314 2616 78 -13 C ATOM 1599 O GLU A1008 137.933 49.946 33.035 1.00104.25 O ANISOU 1599 O GLU A1008 18131 11352 10128 2518 -185 -184 O ATOM 1600 CB GLU A1008 138.181 50.930 29.888 1.00 97.31 C ANISOU 1600 CB GLU A1008 17568 10849 8555 3099 631 -86 C ATOM 1601 CG GLU A1008 139.148 49.787 29.795 1.00110.61 C ANISOU 1601 CG GLU A1008 19550 12129 10346 3235 631 -444 C ATOM 1602 CD GLU A1008 138.478 48.549 29.211 1.00130.86 C ANISOU 1602 CD GLU A1008 22643 14685 12392 3057 230 -682 C ATOM 1603 OE1 GLU A1008 137.496 48.711 28.455 1.00133.57 O ANISOU 1603 OE1 GLU A1008 23151 15386 12215 2960 102 -600 O ATOM 1604 OE2 GLU A1008 138.923 47.416 29.495 1.00136.45 O ANISOU 1604 OE2 GLU A1008 23592 15012 13240 3028 15 -972 O ATOM 1605 N THR A1009 137.666 52.170 32.763 1.00 94.64 N ANISOU 1605 N THR A1009 16247 10591 9122 2698 315 180 N ATOM 1606 CA THR A1009 138.054 52.477 34.137 1.00100.63 C ANISOU 1606 CA THR A1009 16621 11240 10374 2657 234 147 C ATOM 1607 C THR A1009 137.083 51.856 35.136 1.00100.63 C ANISOU 1607 C THR A1009 16710 11347 10177 2243 -241 167 C ATOM 1608 O THR A1009 137.503 51.273 36.147 1.00 85.16 O ANISOU 1608 O THR A1009 14800 9169 8387 2194 -455 65 O ATOM 1609 CB THR A1009 138.118 53.994 34.329 1.00 89.89 C ANISOU 1609 CB THR A1009 14696 10052 9407 2792 557 315 C ATOM 1610 OG1 THR A1009 139.068 54.555 33.414 1.00100.92 O ANISOU 1610 OG1 THR A1009 16019 11294 11032 3149 1078 334 O ATOM 1611 CG2 THR A1009 138.522 54.346 35.747 1.00 79.60 C ANISOU 1611 CG2 THR A1009 12976 8674 8593 2777 444 203 C ATOM 1612 N LEU A1010 135.778 51.979 34.870 1.00103.75 N ANISOU 1612 N LEU A1010 17124 12077 10218 1950 -404 302 N ATOM 1613 CA LEU A1010 134.786 51.389 35.767 1.00 96.09 C ANISOU 1613 CA LEU A1010 16213 11216 9083 1506 -773 320 C ATOM 1614 C LEU A1010 134.953 49.876 35.871 1.00 96.14 C ANISOU 1614 C LEU A1010 16743 10868 8915 1347 -1046 183 C ATOM 1615 O LEU A1010 134.946 49.323 36.977 1.00101.27 O ANISOU 1615 O LEU A1010 17475 11372 9633 1148 -1245 203 O ATOM 1616 CB LEU A1010 133.369 51.762 35.322 1.00 93.18 C ANISOU 1616 CB LEU A1010 15721 11253 8432 1237 -891 423 C ATOM 1617 CG LEU A1010 132.736 52.978 36.012 1.00 99.20 C ANISOU 1617 CG LEU A1010 15916 12363 9412 1157 -817 553 C ATOM 1618 CD1 LEU A1010 133.489 54.261 35.712 1.00111.43 C ANISOU 1618 CD1 LEU A1010 17111 13920 11309 1573 -450 642 C ATOM 1619 CD2 LEU A1010 131.269 53.112 35.604 1.00112.17 C ANISOU 1619 CD2 LEU A1010 17452 14373 10794 868 -1019 593 C ATOM 1620 N ASN A1011 135.106 49.187 34.733 1.00 88.72 N ANISOU 1620 N ASN A1011 16189 9776 7743 1446 -1058 44 N ATOM 1621 CA ASN A1011 135.319 47.739 34.779 1.00 92.66 C ANISOU 1621 CA ASN A1011 17181 9867 8158 1324 -1316 -125 C ATOM 1622 C ASN A1011 136.582 47.373 35.547 1.00100.85 C ANISOU 1622 C ASN A1011 18279 10490 9549 1580 -1305 -194 C ATOM 1623 O ASN A1011 136.567 46.442 36.361 1.00108.18 O ANISOU 1623 O ASN A1011 19474 11122 10507 1388 -1587 -182 O ATOM 1624 CB ASN A1011 135.358 47.150 33.369 1.00100.22 C ANISOU 1624 CB ASN A1011 18507 10750 8823 1452 -1310 -343 C ATOM 1625 CG ASN A1011 133.978 46.859 32.824 1.00124.85 C ANISOU 1625 CG ASN A1011 21731 14134 11571 1088 -1571 -379 C ATOM 1626 OD1 ASN A1011 133.477 47.555 31.940 1.00135.36 O ANISOU 1626 OD1 ASN A1011 22947 15841 12643 1189 -1492 -351 O ATOM 1627 ND2 ASN A1011 133.369 45.784 33.324 1.00132.89 N ANISOU 1627 ND2 ASN A1011 22983 14926 12582 672 -1898 -452 N ATOM 1628 N ASP A1012 137.682 48.096 35.317 1.00 92.37 N ANISOU 1628 N ASP A1012 16953 9370 8773 2017 -987 -263 N ATOM 1629 CA ASP A1012 138.928 47.767 36.005 1.00101.01 C ANISOU 1629 CA ASP A1012 18039 10074 10266 2309 -1020 -401 C ATOM 1630 C ASP A1012 138.781 47.914 37.518 1.00101.37 C ANISOU 1630 C ASP A1012 17916 10157 10443 2159 -1261 -258 C ATOM 1631 O ASP A1012 139.147 47.012 38.287 1.00 98.06 O ANISOU 1631 O ASP A1012 17783 9400 10076 2158 -1565 -283 O ATOM 1632 CB ASP A1012 140.059 48.652 35.482 1.00105.11 C ANISOU 1632 CB ASP A1012 18202 10571 11162 2764 -582 -527 C ATOM 1633 CG ASP A1012 140.387 48.377 34.028 1.00118.60 C ANISOU 1633 CG ASP A1012 20158 12209 12694 2964 -298 -684 C ATOM 1634 OD1 ASP A1012 140.173 47.234 33.569 1.00121.30 O ANISOU 1634 OD1 ASP A1012 20974 12355 12758 2866 -521 -832 O ATOM 1635 OD2 ASP A1012 140.853 49.309 33.343 1.00123.29 O ANISOU 1635 OD2 ASP A1012 20481 12938 13426 3216 169 -664 O ATOM 1636 N ASN A1013 138.219 49.039 37.967 1.00 97.18 N ANISOU 1636 N ASN A1013 16947 10038 9938 2045 -1139 -105 N ATOM 1637 CA ASN A1013 138.130 49.262 39.405 1.00 88.48 C ANISOU 1637 CA ASN A1013 15670 9031 8919 1946 -1331 -20 C ATOM 1638 C ASN A1013 137.075 48.370 40.055 1.00 98.19 C ANISOU 1638 C ASN A1013 17271 10282 9754 1468 -1629 166 C ATOM 1639 O ASN A1013 137.234 47.977 41.216 1.00102.48 O ANISOU 1639 O ASN A1013 17954 10720 10266 1422 -1855 242 O ATOM 1640 CB ASN A1013 137.861 50.738 39.691 1.00 87.53 C ANISOU 1640 CB ASN A1013 14943 9324 8990 1980 -1095 25 C ATOM 1641 CG ASN A1013 138.995 51.636 39.222 1.00 98.09 C ANISOU 1641 CG ASN A1013 15880 10561 10829 2431 -764 -144 C ATOM 1642 OD1 ASN A1013 138.807 52.504 38.372 1.00101.62 O ANISOU 1642 OD1 ASN A1013 16074 11181 11358 2495 -431 -81 O ATOM 1643 ND2 ASN A1013 140.188 51.415 39.768 1.00105.65 N ANISOU 1643 ND2 ASN A1013 16780 11214 12149 2752 -854 -356 N ATOM 1644 N LEU A1014 136.016 47.998 39.327 1.00 89.22 N ANISOU 1644 N LEU A1014 16317 9262 8320 1115 -1638 234 N ATOM 1645 CA LEU A1014 135.044 47.064 39.890 1.00 95.66 C ANISOU 1645 CA LEU A1014 17470 10022 8854 621 -1872 386 C ATOM 1646 C LEU A1014 135.631 45.662 39.993 1.00 98.58 C ANISOU 1646 C LEU A1014 18419 9809 9227 657 -2120 356 C ATOM 1647 O LEU A1014 135.317 44.917 40.928 1.00 97.96 O ANISOU 1647 O LEU A1014 18648 9547 9024 383 -2312 544 O ATOM 1648 CB LEU A1014 133.764 47.057 39.050 1.00104.35 C ANISOU 1648 CB LEU A1014 18532 11388 9727 244 -1847 389 C ATOM 1649 CG LEU A1014 132.527 46.305 39.563 1.00133.50 C ANISOU 1649 CG LEU A1014 22407 15105 13214 -357 -2003 517 C ATOM 1650 CD1 LEU A1014 131.267 46.993 39.057 1.00137.43 C ANISOU 1650 CD1 LEU A1014 22515 16092 13612 -638 -1930 491 C ATOM 1651 CD2 LEU A1014 132.528 44.833 39.145 1.00145.73 C ANISOU 1651 CD2 LEU A1014 24527 16138 14707 -538 -2220 445 C ATOM 1652 N LYS A1015 136.478 45.280 39.034 1.00 94.49 N ANISOU 1652 N LYS A1015 18071 8978 8853 997 -2097 129 N ATOM 1653 CA LYS A1015 137.193 44.015 39.154 1.00 93.76 C ANISOU 1653 CA LYS A1015 18479 8284 8863 1125 -2344 51 C ATOM 1654 C LYS A1015 138.114 44.032 40.366 1.00101.67 C ANISOU 1654 C LYS A1015 19477 9095 10059 1416 -2505 129 C ATOM 1655 O LYS A1015 138.227 43.032 41.089 1.00 98.40 O ANISOU 1655 O LYS A1015 19506 8277 9603 1341 -2799 267 O ATOM 1656 CB LYS A1015 137.980 43.741 37.872 1.00 91.95 C ANISOU 1656 CB LYS A1015 18349 7816 8773 1485 -2233 -276 C ATOM 1657 CG LYS A1015 137.141 43.171 36.735 1.00 86.01 C ANISOU 1657 CG LYS A1015 17844 7076 7762 1210 -2247 -408 C ATOM 1658 CD LYS A1015 137.953 43.070 35.453 1.00 87.36 C ANISOU 1658 CD LYS A1015 18086 7118 7989 1617 -2066 -753 C ATOM 1659 N VAL A1016 138.766 45.172 40.613 1.00111.22 N ANISOU 1659 N VAL A1016 20190 10579 11491 1758 -2335 39 N ATOM 1660 CA VAL A1016 139.582 45.310 41.819 1.00105.43 C ANISOU 1660 CA VAL A1016 19381 9748 10929 2051 -2540 54 C ATOM 1661 C VAL A1016 138.723 45.161 43.073 1.00 99.31 C ANISOU 1661 C VAL A1016 18780 9161 9791 1676 -2717 382 C ATOM 1662 O VAL A1016 139.130 44.517 44.048 1.00 95.22 O ANISOU 1662 O VAL A1016 18605 8374 9201 1785 -3032 508 O ATOM 1663 CB VAL A1016 140.339 46.649 41.806 1.00 96.57 C ANISOU 1663 CB VAL A1016 17609 8903 10180 2437 -2300 -162 C ATOM 1664 CG1 VAL A1016 141.044 46.863 43.132 1.00 90.72 C ANISOU 1664 CG1 VAL A1016 16741 8144 9585 2717 -2574 -202 C ATOM 1665 CG2 VAL A1016 141.340 46.665 40.669 1.00110.27 C ANISOU 1665 CG2 VAL A1016 19225 10380 12294 2827 -2081 -468 C ATOM 1666 N ILE A1017 137.531 45.764 43.073 1.00 98.04 N ANISOU 1666 N ILE A1017 18391 9472 9389 1250 -2510 525 N ATOM 1667 CA ILE A1017 136.644 45.671 44.235 1.00101.85 C ANISOU 1667 CA ILE A1017 18997 10185 9515 855 -2580 816 C ATOM 1668 C ILE A1017 136.221 44.225 44.472 1.00113.87 C ANISOU 1668 C ILE A1017 21199 11262 10805 515 -2783 1071 C ATOM 1669 O ILE A1017 136.229 43.736 45.607 1.00122.65 O ANISOU 1669 O ILE A1017 22659 12256 11686 445 -2960 1331 O ATOM 1670 CB ILE A1017 135.423 46.591 44.063 1.00102.45 C ANISOU 1670 CB ILE A1017 18628 10836 9461 470 -2294 855 C ATOM 1671 CG1 ILE A1017 135.857 48.055 44.046 1.00101.64 C ANISOU 1671 CG1 ILE A1017 17870 11119 9630 812 -2105 648 C ATOM 1672 CG2 ILE A1017 134.412 46.354 45.172 1.00 90.67 C ANISOU 1672 CG2 ILE A1017 17284 9568 7598 -6 -2293 1134 C ATOM 1673 CD1 ILE A1017 134.759 48.999 43.657 1.00 89.18 C ANISOU 1673 CD1 ILE A1017 15831 10036 8018 529 -1845 651 C ATOM 1674 N GLU A1018 135.821 43.526 43.406 1.00119.40 N ANISOU 1674 N GLU A1018 22112 11701 11554 296 -2758 1002 N ATOM 1675 CA GLU A1018 135.485 42.108 43.534 1.00133.60 C ANISOU 1675 CA GLU A1018 24540 12968 13254 -22 -2949 1197 C ATOM 1676 C GLU A1018 136.657 41.302 44.074 1.00138.07 C ANISOU 1676 C GLU A1018 25560 12957 13944 399 -3273 1250 C ATOM 1677 O GLU A1018 136.474 40.425 44.927 1.00128.46 O ANISOU 1677 O GLU A1018 24857 11400 12553 203 -3452 1585 O ATOM 1678 CB GLU A1018 135.016 41.537 42.196 1.00142.92 C ANISOU 1678 CB GLU A1018 25821 13948 14536 -236 -2913 983 C ATOM 1679 CG GLU A1018 133.548 41.774 41.909 1.00151.72 C ANISOU 1679 CG GLU A1018 26710 15455 15483 -826 -2734 1028 C ATOM 1680 CD GLU A1018 133.132 41.258 40.549 1.00161.83 C ANISOU 1680 CD GLU A1018 28066 16580 16844 -970 -2770 740 C ATOM 1681 OE1 GLU A1018 134.024 41.012 39.710 1.00165.80 O ANISOU 1681 OE1 GLU A1018 28694 16809 17491 -551 -2843 473 O ATOM 1682 OE2 GLU A1018 131.918 41.053 40.334 1.00171.18 O ANISOU 1682 OE2 GLU A1018 29182 17908 17952 -1499 -2732 746 O ATOM 1683 N LYS A1019 137.868 41.578 43.595 1.00142.25 N ANISOU 1683 N LYS A1019 25907 13350 14791 985 -3344 932 N ATOM 1684 CA LYS A1019 139.055 40.923 44.139 1.00145.72 C ANISOU 1684 CA LYS A1019 26677 13273 15416 1467 -3697 919 C ATOM 1685 C LYS A1019 139.607 41.788 45.273 1.00148.95 C ANISOU 1685 C LYS A1019 26802 14026 15766 1797 -3798 960 C ATOM 1686 O LYS A1019 140.690 42.372 45.207 1.00154.91 O ANISOU 1686 O LYS A1019 27190 14810 16858 2334 -3856 644 O ATOM 1687 CB LYS A1019 140.076 40.662 43.039 1.00141.29 C ANISOU 1687 CB LYS A1019 26050 12350 15286 1917 -3717 494 C ATOM 1688 CG LYS A1019 139.573 39.630 42.029 1.00145.35 C ANISOU 1688 CG LYS A1019 26940 12465 15820 1622 -3703 413 C ATOM 1689 CD LYS A1019 140.523 39.409 40.865 1.00150.37 C ANISOU 1689 CD LYS A1019 27500 12812 16820 2058 -3655 -57 C ATOM 1690 CE LYS A1019 141.714 38.568 41.275 1.00157.68 C ANISOU 1690 CE LYS A1019 28672 13154 18083 2529 -4000 -165 C ATOM 1691 NZ LYS A1019 142.535 38.174 40.098 1.00161.02 N ANISOU 1691 NZ LYS A1019 28875 13457 18846 2821 -3858 -642 N ATOM 1692 N ALA A1020 138.806 41.863 46.335 1.00138.11 N ANISOU 1692 N ALA A1020 25586 12927 13964 1448 -3799 1328 N ATOM 1693 CA ALA A1020 139.078 42.736 47.466 1.00121.81 C ANISOU 1693 CA ALA A1020 23255 11301 11726 1676 -3873 1354 C ATOM 1694 C ALA A1020 140.054 42.088 48.434 1.00136.89 C ANISOU 1694 C ALA A1020 25607 12822 13583 2139 -4361 1462 C ATOM 1695 O ALA A1020 139.939 40.904 48.762 1.00142.35 O ANISOU 1695 O ALA A1020 26863 13080 14144 1978 -4520 1741 O ATOM 1696 CB ALA A1020 137.788 43.088 48.206 1.00111.39 C ANISOU 1696 CB ALA A1020 21925 10483 9916 1118 -3633 1672 C ATOM 1697 N ASP A1021 141.009 42.886 48.894 1.00151.31 N ANISOU 1697 N ASP A1021 27024 14863 15604 2679 -4541 1159 N ATOM 1698 CA ASP A1021 141.969 42.508 49.922 1.00164.51 C ANISOU 1698 CA ASP A1021 28891 16356 17257 3151 -4999 1133 C ATOM 1699 C ASP A1021 141.711 43.171 51.265 1.00165.51 C ANISOU 1699 C ASP A1021 28913 17042 16930 3147 -5055 1239 C ATOM 1700 O ASP A1021 141.936 42.547 52.305 1.00155.79 O ANISOU 1700 O ASP A1021 28024 15737 15430 3227 -5291 1424 O ATOM 1701 CB ASP A1021 143.385 42.843 49.446 1.00165.02 C ANISOU 1701 CB ASP A1021 28510 16212 17979 3816 -5210 592 C ATOM 1702 CG ASP A1021 143.485 44.247 48.879 1.00147.87 C ANISOU 1702 CG ASP A1021 25550 14471 16161 3916 -4876 209 C ATOM 1703 OD1 ASP A1021 142.428 44.894 48.739 1.00138.01 O ANISOU 1703 OD1 ASP A1021 24088 13689 14660 3437 -4471 344 O ATOM 1704 OD2 ASP A1021 144.608 44.698 48.570 1.00142.75 O ANISOU 1704 OD2 ASP A1021 24418 13715 16106 4420 -4952 -259 O ATOM 1705 N ASN A1022 141.230 44.410 51.277 1.00170.42 N ANISOU 1705 N ASN A1022 29062 18239 17450 3056 -4827 1113 N ATOM 1706 CA ASN A1022 140.988 45.134 52.521 1.00162.62 C ANISOU 1706 CA ASN A1022 27904 17836 16046 3071 -4857 1113 C ATOM 1707 C ASN A1022 140.054 46.304 52.227 1.00154.19 C ANISOU 1707 C ASN A1022 26249 17371 14964 2689 -4370 989 C ATOM 1708 O ASN A1022 139.485 46.405 51.135 1.00156.28 O ANISOU 1708 O ASN A1022 26293 17597 15488 2341 -3990 981 O ATOM 1709 CB ASN A1022 142.317 45.563 53.159 1.00159.43 C ANISOU 1709 CB ASN A1022 27205 17450 15922 3787 -5317 680 C ATOM 1710 CG ASN A1022 143.151 46.461 52.256 1.00158.98 C ANISOU 1710 CG ASN A1022 26400 17360 16647 4171 -5268 110 C ATOM 1711 OD1 ASN A1022 142.673 46.985 51.248 1.00170.62 O ANISOU 1711 OD1 ASN A1022 27460 18942 18428 3856 -4772 21 O ATOM 1712 ND2 ASN A1022 144.426 46.612 52.604 1.00159.50 N ANISOU 1712 ND2 ASN A1022 26228 17265 17112 4823 -5721 -302 N ATOM 1713 N ALA A1023 139.886 47.191 53.207 1.00142.25 N ANISOU 1713 N ALA A1023 24444 16430 13174 2760 -4375 852 N ATOM 1714 CA ALA A1023 138.978 48.318 53.045 1.00127.28 C ANISOU 1714 CA ALA A1023 21936 15107 11317 2404 -3906 702 C ATOM 1715 C ALA A1023 139.622 49.520 52.369 1.00125.27 C ANISOU 1715 C ALA A1023 20828 14960 11807 2727 -3788 157 C ATOM 1716 O ALA A1023 138.902 50.359 51.817 1.00126.06 O ANISOU 1716 O ALA A1023 20427 15366 12105 2435 -3370 65 O ATOM 1717 CB ALA A1023 138.414 48.741 54.403 1.00124.64 C ANISOU 1717 CB ALA A1023 21660 15354 10342 2301 -3905 771 C ATOM 1718 N ALA A1024 140.952 49.626 52.395 1.00125.95 N ANISOU 1718 N ALA A1024 20726 14781 12350 3323 -4137 -203 N ATOM 1719 CA ALA A1024 141.608 50.766 51.761 1.00115.33 C ANISOU 1719 CA ALA A1024 18553 13481 11785 3605 -3963 -711 C ATOM 1720 C ALA A1024 141.594 50.642 50.241 1.00104.54 C ANISOU 1720 C ALA A1024 17065 11778 10876 3457 -3598 -666 C ATOM 1721 O ALA A1024 141.350 51.628 49.534 1.00 93.56 O ANISOU 1721 O ALA A1024 15097 10566 9883 3356 -3196 -829 O ATOM 1722 CB ALA A1024 143.040 50.904 52.279 1.00110.09 C ANISOU 1722 CB ALA A1024 17667 12630 11534 4272 -4438 -1161 C ATOM 1723 N GLN A1025 141.849 49.440 49.718 1.00106.50 N ANISOU 1723 N GLN A1025 17873 11532 11059 3461 -3737 -448 N ATOM 1724 CA GLN A1025 141.873 49.258 48.270 1.00119.91 C ANISOU 1724 CA GLN A1025 19508 12935 13118 3358 -3411 -450 C ATOM 1725 C GLN A1025 140.481 49.419 47.670 1.00116.18 C ANISOU 1725 C GLN A1025 19065 12741 12339 2772 -3008 -162 C ATOM 1726 O GLN A1025 140.331 49.952 46.562 1.00123.11 O ANISOU 1726 O GLN A1025 19607 13647 13523 2702 -2648 -249 O ATOM 1727 CB GLN A1025 142.455 47.889 47.922 1.00137.49 C ANISOU 1727 CB GLN A1025 22334 14562 15344 3514 -3689 -345 C ATOM 1728 N VAL A1026 139.450 48.970 48.389 1.00102.72 N ANISOU 1728 N VAL A1026 17753 11246 10031 2355 -3060 180 N ATOM 1729 CA VAL A1026 138.080 49.150 47.914 1.00 92.65 C ANISOU 1729 CA VAL A1026 16424 10265 8516 1794 -2711 394 C ATOM 1730 C VAL A1026 137.731 50.631 47.848 1.00 94.02 C ANISOU 1730 C VAL A1026 15855 10931 8938 1789 -2412 171 C ATOM 1731 O VAL A1026 137.143 51.103 46.867 1.00 98.57 O ANISOU 1731 O VAL A1026 16155 11621 9677 1596 -2109 175 O ATOM 1732 CB VAL A1026 137.096 48.375 48.808 1.00 85.80 C ANISOU 1732 CB VAL A1026 16079 9508 7013 1337 -2780 780 C ATOM 1733 CG1 VAL A1026 135.664 48.653 48.384 1.00 89.28 C ANISOU 1733 CG1 VAL A1026 16337 10292 7294 760 -2423 919 C ATOM 1734 CG2 VAL A1026 137.390 46.892 48.743 1.00 84.87 C ANISOU 1734 CG2 VAL A1026 16712 8805 6731 1315 -3046 1039 C ATOM 1735 N LYS A1027 138.098 51.390 48.883 1.00 78.71 N ANISOU 1735 N LYS A1027 13589 9275 7040 2033 -2524 -45 N ATOM 1736 CA LYS A1027 137.858 52.829 48.868 1.00 81.10 C ANISOU 1736 CA LYS A1027 13155 9979 7681 2071 -2262 -309 C ATOM 1737 C LYS A1027 138.614 53.505 47.733 1.00 88.31 C ANISOU 1737 C LYS A1027 13613 10655 9286 2370 -2052 -539 C ATOM 1738 O LYS A1027 138.096 54.428 47.096 1.00 77.23 O ANISOU 1738 O LYS A1027 11761 9444 8138 2255 -1722 -568 O ATOM 1739 CB LYS A1027 138.256 53.447 50.206 1.00 76.61 C ANISOU 1739 CB LYS A1027 12332 9711 7064 2334 -2475 -587 C ATOM 1740 CG LYS A1027 137.994 54.936 50.264 1.00 84.72 C ANISOU 1740 CG LYS A1027 12579 11114 8497 2372 -2218 -905 C ATOM 1741 CD LYS A1027 138.332 55.526 51.615 1.00 89.33 C ANISOU 1741 CD LYS A1027 12913 12028 9000 2625 -2453 -1253 C ATOM 1742 CE LYS A1027 138.091 57.023 51.591 1.00 88.81 C ANISOU 1742 CE LYS A1027 12030 12258 9454 2668 -2188 -1616 C ATOM 1743 NZ LYS A1027 138.382 57.691 52.883 1.00 81.14 N ANISOU 1743 NZ LYS A1027 10747 11641 8440 2920 -2415 -2056 N ATOM 1744 N ASP A1028 139.844 53.063 47.474 1.00101.23 N ANISOU 1744 N ASP A1028 15358 11861 11243 2765 -2224 -695 N ATOM 1745 CA ASP A1028 140.641 53.638 46.393 1.00109.96 C ANISOU 1745 CA ASP A1028 16057 12715 13010 3042 -1950 -905 C ATOM 1746 C ASP A1028 139.983 53.398 45.035 1.00102.30 C ANISOU 1746 C ASP A1028 15275 11669 11926 2771 -1629 -643 C ATOM 1747 O ASP A1028 139.843 54.323 44.217 1.00108.00 O ANISOU 1747 O ASP A1028 15586 12478 12973 2782 -1259 -666 O ATOM 1748 CB ASP A1028 142.049 53.041 46.442 1.00122.11 C ANISOU 1748 CB ASP A1028 17704 13805 14889 3498 -2211 -1147 C ATOM 1749 CG ASP A1028 142.991 53.674 45.447 1.00133.17 C ANISOU 1749 CG ASP A1028 18624 14943 17032 3798 -1868 -1412 C ATOM 1750 OD1 ASP A1028 143.405 54.832 45.665 1.00135.43 O ANISOU 1750 OD1 ASP A1028 18254 15337 17867 3983 -1710 -1705 O ATOM 1751 OD2 ASP A1028 143.330 53.010 44.446 1.00136.23 O ANISOU 1751 OD2 ASP A1028 19285 15003 17474 3845 -1730 -1344 O ATOM 1752 N ALA A1029 139.570 52.152 44.783 1.00 80.95 N ANISOU 1752 N ALA A1029 13208 8788 8760 2540 -1784 -393 N ATOM 1753 CA ALA A1029 138.869 51.838 43.543 1.00 79.76 C ANISOU 1753 CA ALA A1029 13269 8603 8434 2277 -1559 -200 C ATOM 1754 C ALA A1029 137.582 52.641 43.416 1.00 80.18 C ANISOU 1754 C ALA A1029 13034 9113 8318 1925 -1350 -55 C ATOM 1755 O ALA A1029 137.247 53.116 42.326 1.00 77.73 O ANISOU 1755 O ALA A1029 12566 8868 8100 1896 -1085 -5 O ATOM 1756 CB ALA A1029 138.574 50.341 43.466 1.00 78.15 C ANISOU 1756 CB ALA A1029 13770 8117 7805 2052 -1811 -10 C ATOM 1757 N LEU A1030 136.850 52.807 44.520 1.00 75.43 N ANISOU 1757 N LEU A1030 12365 8841 7454 1678 -1465 5 N ATOM 1758 CA LEU A1030 135.610 53.576 44.473 1.00 67.93 C ANISOU 1758 CA LEU A1030 11079 8331 6401 1356 -1278 87 C ATOM 1759 C LEU A1030 135.874 55.048 44.172 1.00 70.00 C ANISOU 1759 C LEU A1030 10671 8743 7182 1620 -1018 -91 C ATOM 1760 O LEU A1030 135.099 55.685 43.451 1.00 80.34 O ANISOU 1760 O LEU A1030 11733 10245 8549 1491 -817 -2 O ATOM 1761 CB LEU A1030 134.852 53.423 45.789 1.00 73.68 C ANISOU 1761 CB LEU A1030 11866 9382 6748 1051 -1402 149 C ATOM 1762 CG LEU A1030 134.228 52.062 46.081 1.00 68.16 C ANISOU 1762 CG LEU A1030 11802 8570 5527 651 -1562 414 C ATOM 1763 CD1 LEU A1030 133.745 51.999 47.517 1.00 70.56 C ANISOU 1763 CD1 LEU A1030 12173 9180 5456 437 -1622 479 C ATOM 1764 CD2 LEU A1030 133.083 51.820 45.124 1.00 67.93 C ANISOU 1764 CD2 LEU A1030 11809 8623 5379 247 -1432 551 C ATOM 1765 N THR A1031 136.957 55.607 44.719 1.00 69.30 N ANISOU 1765 N THR A1031 10272 8543 7515 1998 -1038 -351 N ATOM 1766 CA THR A1031 137.325 56.985 44.402 1.00 77.42 C ANISOU 1766 CA THR A1031 10653 9604 9157 2251 -759 -532 C ATOM 1767 C THR A1031 137.612 57.139 42.913 1.00 83.83 C ANISOU 1767 C THR A1031 11488 10162 10200 2378 -456 -396 C ATOM 1768 O THR A1031 137.127 58.077 42.264 1.00 88.53 O ANISOU 1768 O THR A1031 11757 10878 11002 2365 -185 -299 O ATOM 1769 CB THR A1031 138.539 57.408 45.234 1.00 82.85 C ANISOU 1769 CB THR A1031 11010 10152 10317 2635 -871 -902 C ATOM 1770 OG1 THR A1031 138.230 57.298 46.631 1.00 92.24 O ANISOU 1770 OG1 THR A1031 12224 11642 11182 2546 -1166 -1027 O ATOM 1771 CG2 THR A1031 138.938 58.845 44.917 1.00 69.84 C ANISOU 1771 CG2 THR A1031 8655 8464 9416 2864 -548 -1108 C ATOM 1772 N LYS A1032 138.402 56.216 42.355 1.00 75.27 N ANISOU 1772 N LYS A1032 10811 8722 9064 2525 -495 -386 N ATOM 1773 CA LYS A1032 138.667 56.246 40.917 1.00 80.05 C ANISOU 1773 CA LYS A1032 11526 9124 9768 2645 -181 -263 C ATOM 1774 C LYS A1032 137.376 56.143 40.108 1.00 87.64 C ANISOU 1774 C LYS A1032 12711 10332 10255 2339 -144 23 C ATOM 1775 O LYS A1032 137.180 56.887 39.132 1.00 96.70 O ANISOU 1775 O LYS A1032 13696 11525 11519 2426 153 161 O ATOM 1776 CB LYS A1032 139.629 55.120 40.539 1.00 70.87 C ANISOU 1776 CB LYS A1032 10796 7568 8563 2827 -266 -354 C ATOM 1777 CG LYS A1032 141.040 55.291 41.082 1.00 69.62 C ANISOU 1777 CG LYS A1032 10342 7119 8991 3212 -277 -686 C ATOM 1778 CD LYS A1032 141.932 54.121 40.684 1.00 86.23 C ANISOU 1778 CD LYS A1032 12867 8825 11072 3404 -385 -799 C ATOM 1779 CE LYS A1032 143.371 54.356 41.104 1.00 97.63 C ANISOU 1779 CE LYS A1032 13925 9971 13199 3823 -383 -1182 C ATOM 1780 NZ LYS A1032 143.513 54.406 42.581 1.00 99.41 N ANISOU 1780 NZ LYS A1032 13992 10301 13477 3888 -832 -1366 N ATOM 1781 N MET A1033 136.492 55.220 40.499 1.00 74.33 N ANISOU 1781 N MET A1033 11400 8792 8049 1986 -449 116 N ATOM 1782 CA MET A1033 135.208 55.060 39.825 1.00 78.87 C ANISOU 1782 CA MET A1033 12131 9614 8221 1670 -483 309 C ATOM 1783 C MET A1033 134.409 56.354 39.842 1.00 78.26 C ANISOU 1783 C MET A1033 11522 9883 8330 1626 -334 369 C ATOM 1784 O MET A1033 133.841 56.756 38.828 1.00 86.91 O ANISOU 1784 O MET A1033 12588 11091 9343 1637 -227 516 O ATOM 1785 CB MET A1033 134.403 53.944 40.486 1.00 82.82 C ANISOU 1785 CB MET A1033 13006 10190 8270 1253 -798 358 C ATOM 1786 CG MET A1033 134.932 52.555 40.263 1.00 81.15 C ANISOU 1786 CG MET A1033 13392 9597 7844 1245 -979 345 C ATOM 1787 SD MET A1033 133.985 51.365 41.216 1.00 92.98 S ANISOU 1787 SD MET A1033 15292 11125 8911 723 -1284 460 S ATOM 1788 CE MET A1033 132.397 51.456 40.400 1.00 95.99 C ANISOU 1788 CE MET A1033 15581 11844 9046 306 -1269 540 C ATOM 1789 N ARG A1034 134.332 57.006 40.996 1.00 73.95 N ANISOU 1789 N ARG A1034 10565 9516 8018 1599 -357 239 N ATOM 1790 CA ARG A1034 133.524 58.215 41.118 1.00 77.35 C ANISOU 1790 CA ARG A1034 10457 10260 8673 1554 -240 244 C ATOM 1791 C ARG A1034 134.106 59.347 40.285 1.00 85.41 C ANISOU 1791 C ARG A1034 11146 11111 10195 1917 81 297 C ATOM 1792 O ARG A1034 133.357 60.115 39.667 1.00 80.56 O ANISOU 1792 O ARG A1034 10309 10653 9647 1919 180 449 O ATOM 1793 CB ARG A1034 133.404 58.628 42.591 1.00 72.81 C ANISOU 1793 CB ARG A1034 9525 9910 8228 1472 -324 22 C ATOM 1794 CG ARG A1034 132.471 59.800 42.811 1.00 78.47 C ANISOU 1794 CG ARG A1034 9670 10963 9183 1399 -225 -34 C ATOM 1795 CD ARG A1034 132.323 60.106 44.288 1.00 79.87 C ANISOU 1795 CD ARG A1034 9541 11410 9396 1308 -301 -306 C ATOM 1796 NE ARG A1034 131.421 61.233 44.512 1.00 91.46 N ANISOU 1796 NE ARG A1034 10421 13190 11138 1252 -197 -421 N ATOM 1797 CZ ARG A1034 131.810 62.504 44.513 1.00109.08 C ANISOU 1797 CZ ARG A1034 12104 15339 14004 1549 -31 -587 C ATOM 1798 NH1 ARG A1034 133.082 62.805 44.293 1.00122.20 N ANISOU 1798 NH1 ARG A1034 13711 16624 16097 1893 78 -657 N ATOM 1799 NH2 ARG A1034 130.933 63.476 44.723 1.00109.43 N ANISOU 1799 NH2 ARG A1034 11623 15643 14314 1501 37 -705 N ATOM 1800 N ALA A1035 135.438 59.456 40.240 1.00 91.56 N ANISOU 1800 N ALA A1035 11885 11546 11357 2230 253 184 N ATOM 1801 CA ALA A1035 136.065 60.436 39.358 1.00 89.89 C ANISOU 1801 CA ALA A1035 11410 11105 11639 2545 649 278 C ATOM 1802 C ALA A1035 135.670 60.189 37.906 1.00 97.10 C ANISOU 1802 C ALA A1035 12721 12007 12165 2564 773 600 C ATOM 1803 O ALA A1035 135.215 61.101 37.197 1.00 96.20 O ANISOU 1803 O ALA A1035 12426 11956 12170 2662 969 825 O ATOM 1804 CB ALA A1035 137.583 60.390 39.523 1.00 90.61 C ANISOU 1804 CB ALA A1035 11409 10811 12208 2837 822 58 C ATOM 1805 N ALA A1036 135.827 58.943 37.450 1.00101.81 N ANISOU 1805 N ALA A1036 13884 12521 12279 2492 633 614 N ATOM 1806 CA ALA A1036 135.502 58.620 36.064 1.00109.35 C ANISOU 1806 CA ALA A1036 15259 13493 12797 2537 714 845 C ATOM 1807 C ALA A1036 134.029 58.872 35.767 1.00113.48 C ANISOU 1807 C ALA A1036 15757 14391 12971 2326 490 1013 C ATOM 1808 O ALA A1036 133.675 59.314 34.668 1.00133.38 O ANISOU 1808 O ALA A1036 18382 16984 15314 2476 607 1249 O ATOM 1809 CB ALA A1036 135.868 57.167 35.763 1.00112.52 C ANISOU 1809 CB ALA A1036 16242 13738 12774 2473 543 737 C ATOM 1810 N ALA A1037 133.158 58.610 36.743 1.00100.48 N ANISOU 1810 N ALA A1037 13964 12992 11222 1993 171 889 N ATOM 1811 CA ALA A1037 131.727 58.795 36.530 1.00 98.38 C ANISOU 1811 CA ALA A1037 13597 13086 10698 1769 -59 974 C ATOM 1812 C ALA A1037 131.367 60.271 36.454 1.00 98.30 C ANISOU 1812 C ALA A1037 13054 13193 11104 1955 106 1094 C ATOM 1813 O ALA A1037 130.489 60.661 35.676 1.00102.24 O ANISOU 1813 O ALA A1037 13530 13883 11433 1992 5 1262 O ATOM 1814 CB ALA A1037 130.934 58.110 37.642 1.00 90.04 C ANISOU 1814 CB ALA A1037 12497 12244 9470 1334 -354 797 C ATOM 1815 N LEU A1038 132.029 61.108 37.254 1.00102.91 N ANISOU 1815 N LEU A1038 13195 13645 12263 2095 326 986 N ATOM 1816 CA LEU A1038 131.743 62.535 37.181 1.00109.50 C ANISOU 1816 CA LEU A1038 13509 14507 13590 2287 500 1085 C ATOM 1817 C LEU A1038 132.294 63.151 35.902 1.00124.28 C ANISOU 1817 C LEU A1038 15527 16117 15579 2650 832 1417 C ATOM 1818 O LEU A1038 131.717 64.117 35.389 1.00121.20 O ANISOU 1818 O LEU A1038 14919 15775 15356 2804 888 1645 O ATOM 1819 CB LEU A1038 132.284 63.257 38.414 1.00111.23 C ANISOU 1819 CB LEU A1038 13187 14645 14430 2329 624 805 C ATOM 1820 CG LEU A1038 131.529 62.946 39.710 1.00108.34 C ANISOU 1820 CG LEU A1038 12611 14626 13928 1997 344 513 C ATOM 1821 CD1 LEU A1038 132.176 63.635 40.904 1.00114.31 C ANISOU 1821 CD1 LEU A1038 12880 15322 15232 2096 443 183 C ATOM 1822 CD2 LEU A1038 130.063 63.337 39.586 1.00 98.02 C ANISOU 1822 CD2 LEU A1038 11060 13677 12507 1823 170 565 C ATOM 1823 N ASP A1039 133.393 62.613 35.364 1.00142.49 N ANISOU 1823 N ASP A1039 18208 18138 17795 2802 1071 1463 N ATOM 1824 CA ASP A1039 133.826 63.054 34.039 1.00150.11 C ANISOU 1824 CA ASP A1039 19420 18906 18710 3116 1431 1818 C ATOM 1825 C ASP A1039 132.770 62.750 32.982 1.00147.35 C ANISOU 1825 C ASP A1039 19480 18844 17663 3113 1168 2065 C ATOM 1826 O ASP A1039 132.482 63.591 32.123 1.00163.77 O ANISOU 1826 O ASP A1039 21574 20919 19734 3361 1315 2416 O ATOM 1827 CB ASP A1039 135.161 62.413 33.658 1.00154.31 C ANISOU 1827 CB ASP A1039 20277 19120 19236 3257 1753 1756 C ATOM 1828 CG ASP A1039 136.347 63.093 34.317 1.00159.52 C ANISOU 1828 CG ASP A1039 20461 19418 20729 3402 2131 1585 C ATOM 1829 OD1 ASP A1039 136.267 64.308 34.594 1.00162.22 O ANISOU 1829 OD1 ASP A1039 20299 19667 21669 3494 2315 1657 O ATOM 1830 OD2 ASP A1039 137.370 62.416 34.547 1.00160.85 O ANISOU 1830 OD2 ASP A1039 20736 19373 21008 3438 2227 1346 O ATOM 1831 N ALA A1040 132.172 61.556 33.036 1.00128.01 N ANISOU 1831 N ALA A1040 17364 16629 14643 2843 755 1882 N ATOM 1832 CA ALA A1040 131.176 61.182 32.037 1.00121.52 C ANISOU 1832 CA ALA A1040 16906 16090 13176 2836 438 2018 C ATOM 1833 C ALA A1040 129.928 62.050 32.144 1.00129.83 C ANISOU 1833 C ALA A1040 17550 17423 14357 2813 173 2112 C ATOM 1834 O ALA A1040 129.316 62.397 31.127 1.00132.41 O ANISOU 1834 O ALA A1040 18052 17900 14358 3025 39 2361 O ATOM 1835 CB ALA A1040 130.821 59.702 32.180 1.00107.10 C ANISOU 1835 CB ALA A1040 15450 14391 10852 2506 57 1733 C ATOM 1836 N GLN A1041 129.537 62.414 33.368 1.00130.85 N ANISOU 1836 N GLN A1041 17133 17638 14947 2587 80 1896 N ATOM 1837 CA GLN A1041 128.347 63.238 33.558 1.00139.14 C ANISOU 1837 CA GLN A1041 17717 18949 16199 2563 -161 1912 C ATOM 1838 C GLN A1041 128.539 64.628 32.966 1.00138.08 C ANISOU 1838 C GLN A1041 17378 18627 16459 2984 107 2269 C ATOM 1839 O GLN A1041 127.595 65.218 32.426 1.00144.29 O ANISOU 1839 O GLN A1041 18047 19588 17187 3133 -132 2441 O ATOM 1840 CB GLN A1041 128.009 63.326 35.048 1.00137.45 C ANISOU 1840 CB GLN A1041 16971 18866 16387 2242 -231 1564 C ATOM 1841 CG GLN A1041 126.709 64.053 35.372 1.00135.85 C ANISOU 1841 CG GLN A1041 16227 18971 16420 2164 -482 1473 C ATOM 1842 CD GLN A1041 126.395 64.052 36.860 1.00132.21 C ANISOU 1842 CD GLN A1041 15286 18685 16261 1830 -493 1095 C ATOM 1843 OE1 GLN A1041 127.185 63.571 37.672 1.00125.99 O ANISOU 1843 OE1 GLN A1041 14590 17781 15498 1693 -338 935 O ATOM 1844 NE2 GLN A1041 125.229 64.578 37.221 1.00137.16 N ANISOU 1844 NE2 GLN A1041 15408 19611 17095 1719 -687 938 N ATOM 1845 N LYS A1042 129.756 65.167 33.053 1.00136.16 N ANISOU 1845 N LYS A1042 17078 17995 16663 3186 600 2383 N ATOM 1846 CA LYS A1042 130.011 66.496 32.509 1.00142.60 C ANISOU 1846 CA LYS A1042 17707 18540 17936 3560 932 2759 C ATOM 1847 C LYS A1042 130.004 66.482 30.985 1.00149.24 C ANISOU 1847 C LYS A1042 19143 19362 18199 3874 1002 3229 C ATOM 1848 O LYS A1042 129.428 67.376 30.353 1.00152.09 O ANISOU 1848 O LYS A1042 19458 19722 18606 4151 950 3585 O ATOM 1849 CB LYS A1042 131.341 67.033 33.040 1.00141.38 C ANISOU 1849 CB LYS A1042 17282 17944 18493 3648 1465 2700 C ATOM 1850 N ALA A1043 130.632 65.473 30.376 1.00147.87 N ANISOU 1850 N ALA A1043 19552 19177 17455 3865 1108 3229 N ATOM 1851 CA ALA A1043 130.711 65.360 28.925 1.00147.37 C ANISOU 1851 CA ALA A1043 20123 19141 16730 4174 1208 3626 C ATOM 1852 C ALA A1043 129.529 64.607 28.328 1.00152.80 C ANISOU 1852 C ALA A1043 21149 20285 16622 4113 570 3541 C ATOM 1853 O ALA A1043 129.692 63.899 27.326 1.00160.03 O ANISOU 1853 O ALA A1043 22686 21306 16811 4241 541 3618 O ATOM 1854 CB ALA A1043 132.026 64.693 28.518 1.00140.13 C ANISOU 1854 CB ALA A1043 19635 17981 15630 4227 1687 3611 C ATOM 1855 N THR A1044 128.343 64.730 28.923 1.00150.93 N ANISOU 1855 N THR A1044 20489 20326 16530 3920 60 3330 N ATOM 1856 CA THR A1044 127.160 64.101 28.340 1.00156.50 C ANISOU 1856 CA THR A1044 21419 21453 16591 3867 -571 3207 C ATOM 1857 C THR A1044 126.812 64.644 26.959 1.00173.83 C ANISOU 1857 C THR A1044 24025 23750 18272 4347 -689 3657 C ATOM 1858 O THR A1044 126.436 63.834 26.090 1.00171.79 O ANISOU 1858 O THR A1044 24271 23763 17239 4404 -1045 3578 O ATOM 1859 CB THR A1044 125.968 64.245 29.296 1.00143.70 C ANISOU 1859 CB THR A1044 19158 20091 15351 3564 -1020 2877 C ATOM 1860 N PRO A1045 126.890 65.962 26.677 1.00193.22 N ANISOU 1860 N PRO A1045 26326 25999 21089 4718 -440 4128 N ATOM 1861 CA PRO A1045 126.621 66.391 25.300 1.00202.38 C ANISOU 1861 CA PRO A1045 28014 27254 21629 5214 -548 4624 C ATOM 1862 C PRO A1045 127.641 65.849 24.301 1.00206.00 C ANISOU 1862 C PRO A1045 29241 27621 21407 5404 -110 4849 C ATOM 1863 O PRO A1045 127.788 66.426 23.223 1.00214.74 O ANISOU 1863 O PRO A1045 30684 28636 22270 5655 84 5186 O ATOM 1864 CB PRO A1045 126.710 67.920 25.382 1.00205.47 C ANISOU 1864 CB PRO A1045 28060 27302 22709 5526 -233 5110 C ATOM 1865 CG PRO A1045 126.430 68.240 26.804 1.00200.92 C ANISOU 1865 CG PRO A1045 26652 26649 23038 5177 -292 4705 C ATOM 1866 CD PRO A1045 127.038 67.117 27.585 1.00196.80 C ANISOU 1866 CD PRO A1045 26113 26155 22506 4717 -153 4207 C ATOM 1867 N SER A1055 113.860 66.669 26.821 1.00143.26 N ANISOU 1867 N SER A1055 15663 22996 15772 4567 -6862 1231 N ATOM 1868 CA SER A1055 114.238 65.457 26.105 1.00151.48 C ANISOU 1868 CA SER A1055 17435 24149 15970 4428 -6978 1154 C ATOM 1869 C SER A1055 114.022 64.224 26.976 1.00153.77 C ANISOU 1869 C SER A1055 17449 24556 16419 3625 -6852 539 C ATOM 1870 O SER A1055 114.441 64.198 28.132 1.00153.51 O ANISOU 1870 O SER A1055 17119 24349 16858 3185 -6262 467 O ATOM 1871 CB SER A1055 115.697 65.532 25.651 1.00153.98 C ANISOU 1871 CB SER A1055 18606 24120 15778 4673 -6367 1767 C ATOM 1872 N PRO A1056 113.367 63.203 26.420 1.00158.56 N ANISOU 1872 N PRO A1056 18167 25446 16632 3444 -7414 93 N ATOM 1873 CA PRO A1056 113.117 61.979 27.194 1.00155.12 C ANISOU 1873 CA PRO A1056 17499 25065 16375 2659 -7293 -466 C ATOM 1874 C PRO A1056 114.360 61.116 27.358 1.00149.03 C ANISOU 1874 C PRO A1056 17429 24002 15193 2381 -6719 -293 C ATOM 1875 O PRO A1056 114.615 60.590 28.445 1.00142.25 O ANISOU 1875 O PRO A1056 16376 23001 14673 1799 -6251 -461 O ATOM 1876 CB PRO A1056 112.040 61.263 26.373 1.00169.91 C ANISOU 1876 CB PRO A1056 19308 27211 18037 2588 -8041 -956 C ATOM 1877 CG PRO A1056 112.272 61.731 24.974 1.00180.58 C ANISOU 1877 CG PRO A1056 21331 28501 18781 3236 -8268 -510 C ATOM 1878 CD PRO A1056 112.743 63.156 25.086 1.00177.58 C ANISOU 1878 CD PRO A1056 20911 27960 18599 3775 -7989 99 C ATOM 1879 N GLU A1057 115.139 60.959 26.285 1.00150.33 N ANISOU 1879 N GLU A1057 18420 24082 14616 2813 -6748 41 N ATOM 1880 CA GLU A1057 116.335 60.126 26.358 1.00132.65 C ANISOU 1880 CA GLU A1057 16834 21559 12007 2599 -6231 164 C ATOM 1881 C GLU A1057 117.440 60.808 27.157 1.00128.22 C ANISOU 1881 C GLU A1057 16287 20648 11784 2622 -5447 611 C ATOM 1882 O GLU A1057 118.188 60.144 27.885 1.00115.36 O ANISOU 1882 O GLU A1057 14806 18783 10241 2220 -4979 553 O ATOM 1883 CB GLU A1057 116.820 59.783 24.950 1.00124.65 C ANISOU 1883 CB GLU A1057 16669 20595 10097 3074 -6464 336 C ATOM 1884 N MET A1058 117.556 62.134 27.039 1.00138.98 N ANISOU 1884 N MET A1058 17483 21946 13376 3103 -5322 1042 N ATOM 1885 CA MET A1058 118.603 62.854 27.757 1.00145.35 C ANISOU 1885 CA MET A1058 18249 22397 14581 3148 -4603 1418 C ATOM 1886 C MET A1058 118.336 62.900 29.258 1.00150.30 C ANISOU 1886 C MET A1058 18167 23003 15936 2625 -4342 1105 C ATOM 1887 O MET A1058 119.284 62.891 30.052 1.00139.82 O ANISOU 1887 O MET A1058 16886 21408 14831 2444 -3774 1203 O ATOM 1888 CB MET A1058 118.745 64.271 27.201 1.00147.43 C ANISOU 1888 CB MET A1058 18509 22543 14965 3790 -4544 1955 C ATOM 1889 N LYS A1059 117.066 62.953 29.667 1.00160.70 N ANISOU 1889 N LYS A1059 18820 24617 17622 2394 -4744 705 N ATOM 1890 CA LYS A1059 116.753 62.967 31.093 1.00159.30 C ANISOU 1890 CA LYS A1059 17986 24475 18065 1885 -4456 386 C ATOM 1891 C LYS A1059 117.100 61.636 31.749 1.00155.10 C ANISOU 1891 C LYS A1059 17700 23881 17350 1271 -4217 132 C ATOM 1892 O LYS A1059 117.627 61.606 32.869 1.00148.71 O ANISOU 1892 O LYS A1059 16753 22934 16817 974 -3733 113 O ATOM 1893 CB LYS A1059 115.276 63.303 31.304 1.00164.15 C ANISOU 1893 CB LYS A1059 17811 25437 19123 1781 -4914 -15 C ATOM 1894 N ASP A1060 116.815 60.526 31.064 1.00158.54 N ANISOU 1894 N ASP A1060 18516 24401 17322 1097 -4574 -74 N ATOM 1895 CA ASP A1060 117.131 59.210 31.610 1.00157.49 C ANISOU 1895 CA ASP A1060 18665 24137 17039 530 -4377 -289 C ATOM 1896 C ASP A1060 118.630 59.044 31.825 1.00151.57 C ANISOU 1896 C ASP A1060 18490 23019 16082 631 -3853 48 C ATOM 1897 O ASP A1060 119.059 58.476 32.835 1.00157.63 O ANISOU 1897 O ASP A1060 19281 23629 16985 220 -3501 -24 O ATOM 1898 CB ASP A1060 116.599 58.119 30.682 1.00171.80 C ANISOU 1898 CB ASP A1060 20796 26054 18427 399 -4894 -590 C ATOM 1899 CG ASP A1060 115.083 58.051 30.671 1.00183.61 C ANISOU 1899 CG ASP A1060 21629 27894 20241 152 -5403 -1057 C ATOM 1900 OD1 ASP A1060 114.466 58.387 31.704 1.00185.51 O ANISOU 1900 OD1 ASP A1060 21191 28253 21042 -186 -5217 -1232 O ATOM 1901 OD2 ASP A1060 114.510 57.662 29.631 1.00189.28 O ANISOU 1901 OD2 ASP A1060 22484 28780 20655 305 -5990 -1288 O ATOM 1902 N PHE A1061 119.444 59.550 30.893 1.00144.15 N ANISOU 1902 N PHE A1061 18011 21936 14823 1190 -3786 422 N ATOM 1903 CA PHE A1061 120.893 59.413 31.017 1.00128.97 C ANISOU 1903 CA PHE A1061 16581 19656 12764 1312 -3281 701 C ATOM 1904 C PHE A1061 121.433 60.214 32.196 1.00119.68 C ANISOU 1904 C PHE A1061 15002 18329 12142 1273 -2801 822 C ATOM 1905 O PHE A1061 122.247 59.707 32.980 1.00115.29 O ANISOU 1905 O PHE A1061 14600 17554 11650 1040 -2460 794 O ATOM 1906 CB PHE A1061 121.572 59.848 29.718 1.00123.18 C ANISOU 1906 CB PHE A1061 16384 18828 11592 1912 -3255 1073 C ATOM 1907 N ARG A1062 121.004 61.473 32.329 1.00113.16 N ANISOU 1907 N ARG A1062 13660 17604 11731 1530 -2801 934 N ATOM 1908 CA ARG A1062 121.439 62.286 33.461 1.00102.05 C ANISOU 1908 CA ARG A1062 11808 16074 10894 1502 -2386 960 C ATOM 1909 C ARG A1062 120.984 61.679 34.783 1.00106.03 C ANISOU 1909 C ARG A1062 11960 16727 11598 921 -2318 584 C ATOM 1910 O ARG A1062 121.741 61.671 35.762 1.00109.62 O ANISOU 1910 O ARG A1062 12387 17029 12236 788 -1948 563 O ATOM 1911 CB ARG A1062 120.915 63.714 33.313 1.00 88.79 C ANISOU 1911 CB ARG A1062 9607 14461 9667 1879 -2458 1094 C ATOM 1912 N HIS A1063 119.752 61.165 34.831 1.00116.66 N ANISOU 1912 N HIS A1063 13037 18377 12910 574 -2665 278 N ATOM 1913 CA HIS A1063 119.274 60.512 36.046 1.00128.29 C ANISOU 1913 CA HIS A1063 14227 19991 14527 -21 -2535 -41 C ATOM 1914 C HIS A1063 120.115 59.289 36.384 1.00136.74 C ANISOU 1914 C HIS A1063 15897 20812 15245 -319 -2342 -4 C ATOM 1915 O HIS A1063 120.459 59.065 37.552 1.00142.00 O ANISOU 1915 O HIS A1063 16506 21433 16015 -601 -2030 -62 O ATOM 1916 CB HIS A1063 117.808 60.115 35.891 1.00129.11 C ANISOU 1916 CB HIS A1063 13934 20424 14697 -356 -2920 -385 C ATOM 1917 CG HIS A1063 117.242 59.436 37.097 1.00122.14 C ANISOU 1917 CG HIS A1063 12760 19684 13965 -1007 -2714 -683 C ATOM 1918 ND1 HIS A1063 116.884 60.122 38.237 1.00118.99 N ANISOU 1918 ND1 HIS A1063 11758 19482 13973 -1156 -2423 -843 N ATOM 1919 CD2 HIS A1063 116.995 58.129 37.350 1.00120.73 C ANISOU 1919 CD2 HIS A1063 12838 19458 13574 -1550 -2716 -834 C ATOM 1920 CE1 HIS A1063 116.426 59.269 39.135 1.00123.85 C ANISOU 1920 CE1 HIS A1063 12292 20203 14563 -1764 -2229 -1053 C ATOM 1921 NE2 HIS A1063 116.482 58.053 38.622 1.00124.25 N ANISOU 1921 NE2 HIS A1063 12860 20080 14270 -2022 -2398 -1029 N ATOM 1922 N GLY A1064 120.436 58.474 35.376 1.00131.14 N ANISOU 1922 N GLY A1064 15777 19944 14104 -239 -2549 76 N ATOM 1923 CA GLY A1064 121.277 57.314 35.613 1.00122.08 C ANISOU 1923 CA GLY A1064 15213 18504 12669 -463 -2397 106 C ATOM 1924 C GLY A1064 122.648 57.692 36.135 1.00117.20 C ANISOU 1924 C GLY A1064 14787 17608 12134 -205 -1995 328 C ATOM 1925 O GLY A1064 123.165 57.060 37.057 1.00124.56 O ANISOU 1925 O GLY A1064 15892 18384 13052 -466 -1797 298 O ATOM 1926 N PHE A1065 123.248 58.738 35.562 1.00111.52 N ANISOU 1926 N PHE A1065 14030 16809 11533 316 -1875 555 N ATOM 1927 CA PHE A1065 124.548 59.203 36.040 1.00 97.31 C ANISOU 1927 CA PHE A1065 12306 14732 9936 569 -1486 711 C ATOM 1928 C PHE A1065 124.467 59.672 37.491 1.00111.15 C ANISOU 1928 C PHE A1065 13566 16590 12077 367 -1286 557 C ATOM 1929 O PHE A1065 125.324 59.328 38.319 1.00115.14 O ANISOU 1929 O PHE A1065 14224 16918 12606 297 -1083 527 O ATOM 1930 CB PHE A1065 125.065 60.324 35.138 1.00 91.15 C ANISOU 1930 CB PHE A1065 11504 13833 9296 1123 -1352 990 C ATOM 1931 N ASP A1066 123.440 60.464 37.816 1.00120.27 N ANISOU 1931 N ASP A1066 14121 18048 13527 301 -1362 428 N ATOM 1932 CA ASP A1066 123.284 60.950 39.184 1.00124.66 C ANISOU 1932 CA ASP A1066 14186 18762 14416 121 -1160 224 C ATOM 1933 C ASP A1066 123.135 59.798 40.169 1.00111.11 C ANISOU 1933 C ASP A1066 12675 17120 12423 -392 -1116 73 C ATOM 1934 O ASP A1066 123.811 59.761 41.204 1.00111.53 O ANISOU 1934 O ASP A1066 12758 17111 12506 -435 -901 22 O ATOM 1935 CB ASP A1066 122.090 61.903 39.286 1.00138.81 C ANISOU 1935 CB ASP A1066 15286 20882 16574 124 -1265 58 C ATOM 1936 CG ASP A1066 122.400 63.286 38.743 1.00153.94 C ANISOU 1936 CG ASP A1066 16917 22662 18912 660 -1209 220 C ATOM 1937 OD1 ASP A1066 123.582 63.688 38.790 1.00157.21 O ANISOU 1937 OD1 ASP A1066 17488 22767 19479 948 -956 371 O ATOM 1938 OD2 ASP A1066 121.471 63.980 38.283 1.00157.51 O ANISOU 1938 OD2 ASP A1066 16970 23287 19591 799 -1416 193 O ATOM 1939 N ILE A1067 122.257 58.839 39.869 1.00102.70 N ANISOU 1939 N ILE A1067 11761 16168 11093 -780 -1326 2 N ATOM 1940 CA ILE A1067 122.059 57.763 40.833 1.00 98.53 C ANISOU 1940 CA ILE A1067 11432 15662 10341 -1301 -1231 -88 C ATOM 1941 C ILE A1067 123.257 56.817 40.867 1.00 96.47 C ANISOU 1941 C ILE A1067 11872 15005 9777 -1255 -1186 88 C ATOM 1942 O ILE A1067 123.511 56.201 41.906 1.00100.92 O ANISOU 1942 O ILE A1067 12635 15518 10194 -1522 -1042 91 O ATOM 1943 CB ILE A1067 120.731 57.024 40.576 1.00109.25 C ANISOU 1943 CB ILE A1067 12671 17214 11626 -1785 -1427 -253 C ATOM 1944 CG1 ILE A1067 120.678 56.394 39.187 1.00115.76 C ANISOU 1944 CG1 ILE A1067 13887 17863 12234 -1686 -1771 -203 C ATOM 1945 CG2 ILE A1067 119.550 57.964 40.780 1.00109.77 C ANISOU 1945 CG2 ILE A1067 11954 17692 12063 -1846 -1446 -490 C ATOM 1946 CD1 ILE A1067 121.101 54.964 39.176 1.00114.62 C ANISOU 1946 CD1 ILE A1067 14386 17395 11768 -1981 -1799 -147 C ATOM 1947 N LEU A1068 124.035 56.719 39.784 1.00 97.87 N ANISOU 1947 N LEU A1068 12431 14901 9852 -890 -1290 236 N ATOM 1948 CA LEU A1068 125.283 55.962 39.844 1.00 96.61 C ANISOU 1948 CA LEU A1068 12853 14353 9503 -768 -1225 355 C ATOM 1949 C LEU A1068 126.266 56.613 40.808 1.00 99.66 C ANISOU 1949 C LEU A1068 13094 14670 10104 -521 -988 363 C ATOM 1950 O LEU A1068 126.890 55.930 41.634 1.00 84.53 O ANISOU 1950 O LEU A1068 11485 12586 8047 -623 -943 374 O ATOM 1951 CB LEU A1068 125.903 55.842 38.450 1.00 95.26 C ANISOU 1951 CB LEU A1068 13055 13939 9199 -398 -1323 468 C ATOM 1952 CG LEU A1068 127.212 55.045 38.403 1.00 91.56 C ANISOU 1952 CG LEU A1068 13148 13052 8589 -239 -1252 537 C ATOM 1953 CD1 LEU A1068 126.981 53.593 38.799 1.00 73.36 C ANISOU 1953 CD1 LEU A1068 11274 10576 6023 -675 -1400 485 C ATOM 1954 CD2 LEU A1068 127.892 55.135 37.039 1.00 94.09 C ANISOU 1954 CD2 LEU A1068 13766 13181 8803 179 -1241 627 C ATOM 1955 N VAL A1069 126.420 57.937 40.713 1.00 99.12 N ANISOU 1955 N VAL A1069 12556 14706 10401 -174 -864 344 N ATOM 1956 CA VAL A1069 127.288 58.642 41.652 1.00 80.95 C ANISOU 1956 CA VAL A1069 10018 12353 8387 56 -667 261 C ATOM 1957 C VAL A1069 126.762 58.486 43.074 1.00 84.75 C ANISOU 1957 C VAL A1069 10306 13120 8776 -292 -621 89 C ATOM 1958 O VAL A1069 127.536 58.383 44.035 1.00 94.86 O ANISOU 1958 O VAL A1069 11683 14333 10028 -222 -555 16 O ATOM 1959 CB VAL A1069 127.425 60.122 41.251 1.00 79.61 C ANISOU 1959 CB VAL A1069 9336 12203 8711 453 -532 256 C ATOM 1960 CG1 VAL A1069 128.238 60.876 42.285 1.00 74.57 C ANISOU 1960 CG1 VAL A1069 8369 11519 8447 657 -354 73 C ATOM 1961 CG2 VAL A1069 128.073 60.238 39.882 1.00 86.83 C ANISOU 1961 CG2 VAL A1069 10532 12816 9643 809 -498 487 C ATOM 1962 N GLY A1070 125.438 58.439 43.227 1.00 88.97 N ANISOU 1962 N GLY A1070 10573 13990 9243 -665 -655 7 N ATOM 1963 CA GLY A1070 124.864 58.244 44.551 1.00 93.76 C ANISOU 1963 CA GLY A1070 11019 14898 9707 -1037 -532 -143 C ATOM 1964 C GLY A1070 125.187 56.880 45.129 1.00 95.85 C ANISOU 1964 C GLY A1070 11914 14988 9515 -1337 -551 -5 C ATOM 1965 O GLY A1070 125.528 56.753 46.308 1.00103.44 O ANISOU 1965 O GLY A1070 12969 16035 10298 -1394 -442 -45 O ATOM 1966 N GLN A1071 125.084 55.837 44.305 1.00 91.90 N ANISOU 1966 N GLN A1071 11877 14227 8813 -1511 -708 155 N ATOM 1967 CA GLN A1071 125.408 54.493 44.768 1.00 92.80 C ANISOU 1967 CA GLN A1071 12627 14075 8558 -1782 -744 315 C ATOM 1968 C GLN A1071 126.898 54.358 45.067 1.00 93.68 C ANISOU 1968 C GLN A1071 13115 13858 8620 -1369 -791 392 C ATOM 1969 O GLN A1071 127.286 53.631 45.990 1.00106.56 O ANISOU 1969 O GLN A1071 15144 15374 9972 -1484 -793 492 O ATOM 1970 CB GLN A1071 124.974 53.464 43.723 1.00 97.20 C ANISOU 1970 CB GLN A1071 13542 14387 9003 -2029 -927 396 C ATOM 1971 CG GLN A1071 123.496 53.536 43.371 1.00110.15 C ANISOU 1971 CG GLN A1071 14770 16335 10745 -2431 -946 259 C ATOM 1972 CD GLN A1071 123.090 52.524 42.321 1.00120.33 C ANISOU 1972 CD GLN A1071 16387 17381 11951 -2653 -1183 257 C ATOM 1973 OE1 GLN A1071 123.897 51.701 41.895 1.00125.20 O ANISOU 1973 OE1 GLN A1071 17575 17586 12410 -2535 -1305 367 O ATOM 1974 NE2 GLN A1071 121.841 52.602 41.873 1.00127.71 N ANISOU 1974 NE2 GLN A1071 16923 18571 13029 -2949 -1276 77 N ATOM 1975 N ILE A1072 127.747 55.066 44.318 1.00 87.08 N ANISOU 1975 N ILE A1072 12152 12864 8072 -877 -823 349 N ATOM 1976 CA ILE A1072 129.179 55.040 44.611 1.00 87.24 C ANISOU 1976 CA ILE A1072 12403 12583 8161 -468 -855 345 C ATOM 1977 C ILE A1072 129.474 55.756 45.926 1.00 86.45 C ANISOU 1977 C ILE A1072 11989 12727 8133 -345 -772 179 C ATOM 1978 O ILE A1072 130.342 55.331 46.696 1.00 89.41 O ANISOU 1978 O ILE A1072 12662 12945 8365 -193 -868 172 O ATOM 1979 CB ILE A1072 129.987 55.637 43.443 1.00 81.99 C ANISOU 1979 CB ILE A1072 11640 11680 7833 -11 -825 334 C ATOM 1980 CG1 ILE A1072 129.913 54.725 42.217 1.00 77.74 C ANISOU 1980 CG1 ILE A1072 11558 10880 7100 -78 -937 465 C ATOM 1981 CG2 ILE A1072 131.433 55.860 43.852 1.00 72.16 C ANISOU 1981 CG2 ILE A1072 10428 10173 6817 418 -810 238 C ATOM 1982 CD1 ILE A1072 130.521 55.338 40.979 1.00 68.00 C ANISOU 1982 CD1 ILE A1072 10250 9488 6097 335 -842 488 C ATOM 1983 N ASP A1073 128.768 56.854 46.205 1.00 86.85 N ANISOU 1983 N ASP A1073 11427 13163 8408 -375 -628 6 N ATOM 1984 CA ASP A1073 128.906 57.485 47.516 1.00 88.06 C ANISOU 1984 CA ASP A1073 11279 13606 8573 -300 -553 -220 C ATOM 1985 C ASP A1073 128.421 56.555 48.621 1.00 86.05 C ANISOU 1985 C ASP A1073 11403 13538 7753 -698 -542 -125 C ATOM 1986 O ASP A1073 129.007 56.510 49.709 1.00 95.91 O ANISOU 1986 O ASP A1073 12792 14865 8785 -561 -588 -211 O ATOM 1987 CB ASP A1073 128.138 58.805 47.558 1.00 96.45 C ANISOU 1987 CB ASP A1073 11597 15032 10017 -275 -392 -456 C ATOM 1988 CG ASP A1073 128.760 59.876 46.681 1.00107.76 C ANISOU 1988 CG ASP A1073 12652 16244 12046 174 -363 -526 C ATOM 1989 OD1 ASP A1073 129.993 59.850 46.482 1.00107.71 O ANISOU 1989 OD1 ASP A1073 12822 15890 12212 520 -411 -520 O ATOM 1990 OD2 ASP A1073 128.012 60.753 46.200 1.00115.26 O ANISOU 1990 OD2 ASP A1073 13118 17353 13321 184 -278 -583 O ATOM 1991 N ASP A1074 127.342 55.815 48.361 1.00 85.05 N ANISOU 1991 N ASP A1074 11446 13483 7386 -1192 -478 49 N ATOM 1992 CA ASP A1074 126.885 54.789 49.296 1.00105.11 C ANISOU 1992 CA ASP A1074 14431 16102 9404 -1625 -404 227 C ATOM 1993 C ASP A1074 127.985 53.779 49.587 1.00104.63 C ANISOU 1993 C ASP A1074 15092 15614 9047 -1454 -613 449 C ATOM 1994 O ASP A1074 128.241 53.439 50.746 1.00 86.94 O ANISOU 1994 O ASP A1074 13159 13467 6405 -1472 -610 521 O ATOM 1995 CB ASP A1074 125.639 54.089 48.743 1.00118.85 C ANISOU 1995 CB ASP A1074 16216 17860 11081 -2186 -312 361 C ATOM 1996 CG ASP A1074 124.364 54.875 48.995 1.00130.95 C ANISOU 1996 CG ASP A1074 17072 19910 12772 -2473 -69 135 C ATOM 1997 OD1 ASP A1074 124.228 55.456 50.095 1.00136.45 O ANISOU 1997 OD1 ASP A1074 17508 20989 13349 -2470 126 -29 O ATOM 1998 OD2 ASP A1074 123.505 54.941 48.085 1.00136.28 O ANISOU 1998 OD2 ASP A1074 17454 20624 13703 -2669 -97 78 O ATOM 1999 N ALA A1075 128.646 53.289 48.538 1.00111.13 N ANISOU 1999 N ALA A1075 16204 15972 10047 -1256 -806 549 N ATOM 2000 CA ALA A1075 129.722 52.318 48.724 1.00100.27 C ANISOU 2000 CA ALA A1075 15478 14141 8478 -1049 -1034 721 C ATOM 2001 C ALA A1075 130.903 52.928 49.475 1.00 98.07 C ANISOU 2001 C ALA A1075 15098 13887 8276 -519 -1168 531 C ATOM 2002 O ALA A1075 131.510 52.271 50.330 1.00 90.90 O ANISOU 2002 O ALA A1075 14663 12838 7038 -408 -1345 646 O ATOM 2003 CB ALA A1075 130.170 51.769 47.371 1.00 80.84 C ANISOU 2003 CB ALA A1075 13260 11212 6242 -919 -1177 781 C ATOM 2004 N LEU A1076 131.242 54.183 49.168 1.00 91.19 N ANISOU 2004 N LEU A1076 13609 13172 7867 -177 -1107 233 N ATOM 2005 CA LEU A1076 132.353 54.855 49.841 1.00 87.23 C ANISOU 2005 CA LEU A1076 12897 12685 7562 320 -1240 -40 C ATOM 2006 C LEU A1076 132.080 55.055 51.326 1.00 99.70 C ANISOU 2006 C LEU A1076 14455 14695 8732 252 -1240 -149 C ATOM 2007 O LEU A1076 132.990 54.917 52.153 1.00105.51 O ANISOU 2007 O LEU A1076 15397 15381 9311 584 -1486 -255 O ATOM 2008 CB LEU A1076 132.638 56.195 49.166 1.00 84.35 C ANISOU 2008 CB LEU A1076 11834 12361 7853 628 -1107 -326 C ATOM 2009 CG LEU A1076 133.442 56.124 47.874 1.00 85.86 C ANISOU 2009 CG LEU A1076 12075 12092 8455 902 -1117 -277 C ATOM 2010 CD1 LEU A1076 133.371 57.438 47.127 1.00 87.42 C ANISOU 2010 CD1 LEU A1076 11628 12354 9232 1081 -890 -432 C ATOM 2011 CD2 LEU A1076 134.881 55.822 48.246 1.00 75.13 C ANISOU 2011 CD2 LEU A1076 10906 10405 7235 1335 -1347 -419 C ATOM 2012 N LYS A1077 130.843 55.416 51.681 1.00 98.07 N ANISOU 2012 N LYS A1077 13975 14939 8348 -146 -975 -164 N ATOM 2013 CA LYS A1077 130.463 55.467 53.090 1.00104.57 C ANISOU 2013 CA LYS A1077 14863 16212 8658 -274 -904 -235 C ATOM 2014 C LYS A1077 130.815 54.160 53.781 1.00109.74 C ANISOU 2014 C LYS A1077 16361 16661 8675 -351 -1082 122 C ATOM 2015 O LYS A1077 131.443 54.145 54.842 1.00 96.86 O ANISOU 2015 O LYS A1077 14953 15164 6687 -69 -1273 35 O ATOM 2016 CB LYS A1077 128.966 55.746 53.225 1.00101.20 C ANISOU 2016 CB LYS A1077 14104 16231 8115 -792 -534 -237 C ATOM 2017 N LEU A1078 130.444 53.047 53.158 1.00118.73 N ANISOU 2017 N LEU A1078 17989 17440 9685 -702 -1057 518 N ATOM 2018 CA LEU A1078 130.744 51.729 53.701 1.00119.87 C ANISOU 2018 CA LEU A1078 18977 17272 9299 -796 -1220 920 C ATOM 2019 C LEU A1078 132.247 51.486 53.776 1.00104.68 C ANISOU 2019 C LEU A1078 17350 14954 7469 -186 -1667 857 C ATOM 2020 O LEU A1078 132.727 50.780 54.674 1.00 99.71 O ANISOU 2020 O LEU A1078 17317 14220 6348 -47 -1896 1066 O ATOM 2021 CB LEU A1078 130.053 50.684 52.830 1.00132.09 C ANISOU 2021 CB LEU A1078 20869 18440 10879 -1285 -1108 1266 C ATOM 2022 CG LEU A1078 128.583 50.383 53.117 1.00132.40 C ANISOU 2022 CG LEU A1078 20889 18766 10650 -1982 -705 1454 C ATOM 2023 CD1 LEU A1078 127.735 51.629 53.251 1.00116.12 C ANISOU 2023 CD1 LEU A1078 18023 17324 8772 -2101 -406 1100 C ATOM 2024 CD2 LEU A1078 128.070 49.629 51.916 1.00135.20 C ANISOU 2024 CD2 LEU A1078 21357 18713 11298 -2337 -689 1603 C ATOM 2025 N ALA A1079 133.011 52.076 52.848 1.00 99.03 N ANISOU 2025 N ALA A1079 16219 14017 7391 197 -1789 569 N ATOM 2026 CA ALA A1079 134.455 51.861 52.839 1.00 93.28 C ANISOU 2026 CA ALA A1079 15676 12896 6871 771 -2185 444 C ATOM 2027 C ALA A1079 135.150 52.616 53.967 1.00 98.70 C ANISOU 2027 C ALA A1079 16118 13905 7478 1216 -2404 89 C ATOM 2028 O ALA A1079 136.178 52.156 54.478 1.00104.83 O ANISOU 2028 O ALA A1079 17243 14448 8141 1635 -2811 58 O ATOM 2029 CB ALA A1079 135.054 52.268 51.493 1.00 89.09 C ANISOU 2029 CB ALA A1079 14758 12035 7056 1015 -2161 241 C ATOM 2030 N ASN A1080 134.635 53.786 54.354 1.00105.91 N ANISOU 2030 N ASN A1080 16410 15341 8490 1170 -2182 -233 N ATOM 2031 CA ASN A1080 135.143 54.423 55.567 1.00126.59 C ANISOU 2031 CA ASN A1080 18850 18331 10918 1542 -2399 -603 C ATOM 2032 C ASN A1080 134.907 53.554 56.796 1.00136.66 C ANISOU 2032 C ASN A1080 20859 19804 11259 1435 -2536 -289 C ATOM 2033 O ASN A1080 135.798 53.420 57.643 1.00153.83 O ANISOU 2033 O ASN A1080 23288 21994 13167 1891 -2960 -430 O ATOM 2034 CB ASN A1080 134.530 55.811 55.769 1.00137.33 C ANISOU 2034 CB ASN A1080 19411 20207 12560 1480 -2109 -1030 C ATOM 2035 CG ASN A1080 135.339 56.910 55.101 1.00138.18 C ANISOU 2035 CG ASN A1080 18781 20132 13589 1884 -2155 -1498 C ATOM 2036 OD1 ASN A1080 136.570 56.929 55.180 1.00132.89 O ANISOU 2036 OD1 ASN A1080 18082 19184 13225 2365 -2499 -1741 O ATOM 2037 ND2 ASN A1080 134.648 57.846 54.458 1.00139.95 N ANISOU 2037 ND2 ASN A1080 18387 20493 14293 1698 -1803 -1631 N ATOM 2038 N GLU A1081 133.720 52.956 56.923 1.00130.88 N ANISOU 2038 N GLU A1081 20481 19223 10024 845 -2185 138 N ATOM 2039 CA GLU A1081 133.488 52.100 58.087 1.00126.41 C ANISOU 2039 CA GLU A1081 20678 18809 8542 716 -2239 519 C ATOM 2040 C GLU A1081 134.331 50.829 58.085 1.00122.17 C ANISOU 2040 C GLU A1081 20963 17669 7788 942 -2660 924 C ATOM 2041 O GLU A1081 134.315 50.099 59.084 1.00123.93 O ANISOU 2041 O GLU A1081 21689 17946 7452 899 -2702 1260 O ATOM 2042 CB GLU A1081 131.998 51.735 58.218 1.00134.86 C ANISOU 2042 CB GLU A1081 21900 20141 9199 -22 -1687 885 C ATOM 2043 CG GLU A1081 131.134 52.674 59.059 1.00136.28 C ANISOU 2043 CG GLU A1081 21620 21083 9079 -213 -1312 588 C ATOM 2044 CD GLU A1081 130.853 54.043 58.485 1.00131.04 C ANISOU 2044 CD GLU A1081 19950 20698 9139 -152 -1140 23 C ATOM 2045 OE1 GLU A1081 131.234 54.318 57.326 1.00134.48 O ANISOU 2045 OE1 GLU A1081 20023 20751 10324 -12 -1249 -97 O ATOM 2046 OE2 GLU A1081 130.287 54.860 59.238 1.00138.32 O ANISOU 2046 OE2 GLU A1081 20468 22227 9861 -213 -895 -307 O ATOM 2047 N GLY A1082 135.069 50.549 57.017 1.00124.39 N ANISOU 2047 N GLY A1082 21180 17376 8705 1158 -2876 881 N ATOM 2048 CA GLY A1082 135.846 49.334 56.990 1.00125.33 C ANISOU 2048 CA GLY A1082 21971 16892 8757 1367 -3242 1215 C ATOM 2049 C GLY A1082 135.027 48.075 56.838 1.00131.15 C ANISOU 2049 C GLY A1082 23260 17306 9267 793 -2961 1818 C ATOM 2050 O GLY A1082 135.521 46.987 57.157 1.00137.49 O ANISOU 2050 O GLY A1082 24579 17668 9991 911 -3178 2131 O ATOM 2051 N LYS A1083 133.786 48.184 56.372 1.00129.50 N ANISOU 2051 N LYS A1083 22933 17279 8993 181 -2499 1958 N ATOM 2052 CA LYS A1083 132.903 47.034 56.200 1.00128.94 C ANISOU 2052 CA LYS A1083 23299 16896 8796 -409 -2202 2461 C ATOM 2053 C LYS A1083 133.005 46.619 54.741 1.00116.80 C ANISOU 2053 C LYS A1083 21787 14807 7783 -513 -2277 2451 C ATOM 2054 O LYS A1083 132.369 47.219 53.871 1.00101.66 O ANISOU 2054 O LYS A1083 19386 13066 6173 -781 -2033 2248 O ATOM 2055 CB LYS A1083 131.472 47.376 56.597 1.00137.56 C ANISOU 2055 CB LYS A1083 24199 18522 9546 -1032 -1653 2561 C ATOM 2056 CG LYS A1083 131.294 47.661 58.095 1.00149.02 C ANISOU 2056 CG LYS A1083 25699 20534 10388 -947 -1517 2601 C ATOM 2057 CD LYS A1083 129.813 47.876 58.446 1.00155.35 C ANISOU 2057 CD LYS A1083 26314 21809 10901 -1608 -893 2702 C ATOM 2058 CE LYS A1083 129.294 49.170 57.846 1.00147.73 C ANISOU 2058 CE LYS A1083 24620 21325 10184 -1768 -712 2218 C ATOM 2059 NZ LYS A1083 128.050 49.747 58.432 1.00149.72 N ANISOU 2059 NZ LYS A1083 24482 22237 10167 -2249 -152 2110 N ATOM 2060 N VAL A1084 133.797 45.577 54.480 1.00117.42 N ANISOU 2060 N VAL A1084 22321 14235 8059 -278 -2586 2619 N ATOM 2061 CA VAL A1084 134.215 45.300 53.111 1.00108.80 C ANISOU 2061 CA VAL A1084 21233 12637 7468 -183 -2745 2489 C ATOM 2062 C VAL A1084 133.080 44.659 52.312 1.00114.74 C ANISOU 2062 C VAL A1084 22140 13182 8276 -860 -2441 2718 C ATOM 2063 O VAL A1084 132.898 44.964 51.130 1.00114.58 O ANISOU 2063 O VAL A1084 21726 13122 8686 -932 -2353 2463 O ATOM 2064 CB VAL A1084 135.488 44.430 53.104 1.00106.22 C ANISOU 2064 CB VAL A1084 21309 11688 7361 328 -3192 2511 C ATOM 2065 CG1 VAL A1084 135.981 44.225 51.693 1.00104.06 C ANISOU 2065 CG1 VAL A1084 21013 10939 7586 486 -3332 2315 C ATOM 2066 CG2 VAL A1084 136.583 45.066 53.931 1.00105.55 C ANISOU 2066 CG2 VAL A1084 21037 11824 7243 981 -3534 2239 C ATOM 2067 N LYS A1085 132.291 43.778 52.938 1.00119.83 N ANISOU 2067 N LYS A1085 23171 13719 8641 -1345 -2219 3116 N ATOM 2068 CA LYS A1085 131.277 43.023 52.195 1.00132.18 C ANISOU 2068 CA LYS A1085 24926 14978 10320 -2002 -1985 3312 C ATOM 2069 C LYS A1085 130.162 43.930 51.674 1.00148.94 C ANISOU 2069 C LYS A1085 26400 17649 12543 -2435 -1622 3077 C ATOM 2070 O LYS A1085 129.778 43.860 50.492 1.00160.45 O ANISOU 2070 O LYS A1085 27581 18961 14420 -2620 -1590 2869 O ATOM 2071 CB LYS A1085 130.697 41.922 53.085 1.00138.89 C ANISOU 2071 CB LYS A1085 26283 15583 10907 -2418 -1783 3780 C ATOM 2072 N GLU A1086 129.611 44.766 52.558 1.00149.11 N ANISOU 2072 N GLU A1086 26086 18323 12245 -2561 -1343 3044 N ATOM 2073 CA GLU A1086 128.576 45.722 52.175 1.00153.66 C ANISOU 2073 CA GLU A1086 25888 19463 13031 -2882 -1001 2740 C ATOM 2074 C GLU A1086 128.987 46.524 50.939 1.00151.53 C ANISOU 2074 C GLU A1086 25038 19228 13307 -2510 -1173 2302 C ATOM 2075 O GLU A1086 128.189 46.726 50.007 1.00149.94 O ANISOU 2075 O GLU A1086 24430 19117 13421 -2804 -1038 2131 O ATOM 2076 CB GLU A1086 128.290 46.652 53.358 1.00151.02 C ANISOU 2076 CB GLU A1086 25255 19820 12306 -2850 -764 2662 C ATOM 2077 CG GLU A1086 127.534 46.057 54.544 1.00159.46 C ANISOU 2077 CG GLU A1086 26770 21038 12782 -3346 -410 3075 C ATOM 2078 CD GLU A1086 128.422 45.314 55.528 1.00170.67 C ANISOU 2078 CD GLU A1086 28832 22155 13859 -2948 -641 3390 C ATOM 2079 OE1 GLU A1086 129.638 45.189 55.272 1.00171.68 O ANISOU 2079 OE1 GLU A1086 29138 21934 14157 -2355 -1113 3305 O ATOM 2080 OE2 GLU A1086 127.903 44.878 56.580 1.00179.10 O ANISOU 2080 OE2 GLU A1086 30153 23358 14536 -3194 -335 3692 O ATOM 2081 N ALA A1087 130.243 46.981 50.914 1.00141.36 N ANISOU 2081 N ALA A1087 23713 17861 12137 -1849 -1472 2120 N ATOM 2082 CA ALA A1087 130.731 47.784 49.797 1.00121.97 C ANISOU 2082 CA ALA A1087 20739 15420 10184 -1473 -1565 1750 C ATOM 2083 C ALA A1087 130.692 47.002 48.490 1.00123.74 C ANISOU 2083 C ALA A1087 21169 15161 10684 -1590 -1660 1762 C ATOM 2084 O ALA A1087 130.317 47.543 47.442 1.00138.45 O ANISOU 2084 O ALA A1087 22596 17162 12845 -1613 -1577 1541 O ATOM 2085 CB ALA A1087 132.153 48.269 50.085 1.00113.40 C ANISOU 2085 CB ALA A1087 19609 14256 9223 -777 -1841 1558 C ATOM 2086 N GLN A1088 131.067 45.721 48.533 1.00106.70 N ANISOU 2086 N GLN A1088 19695 12429 8418 -1643 -1850 2009 N ATOM 2087 CA GLN A1088 131.125 44.926 47.312 1.00108.69 C ANISOU 2087 CA GLN A1088 20168 12192 8937 -1708 -1971 1951 C ATOM 2088 C GLN A1088 129.722 44.656 46.783 1.00115.65 C ANISOU 2088 C GLN A1088 20898 13187 9857 -2355 -1762 1958 C ATOM 2089 O GLN A1088 129.496 44.633 45.563 1.00119.41 O ANISOU 2089 O GLN A1088 21203 13586 10583 -2379 -1810 1731 O ATOM 2090 CB GLN A1088 131.851 43.608 47.582 1.00105.37 C ANISOU 2090 CB GLN A1088 20507 11085 8442 -1603 -2240 2195 C ATOM 2091 CG GLN A1088 133.147 43.739 48.373 1.00 97.86 C ANISOU 2091 CG GLN A1088 19754 10022 7406 -995 -2505 2220 C ATOM 2092 CD GLN A1088 133.890 42.421 48.482 1.00116.42 C ANISOU 2092 CD GLN A1088 22838 11633 9763 -827 -2829 2434 C ATOM 2093 OE1 GLN A1088 133.560 41.453 47.792 1.00143.73 O ANISOU 2093 OE1 GLN A1088 26621 14618 13372 -1115 -2850 2498 O ATOM 2094 NE2 GLN A1088 134.841 42.350 49.405 1.00112.81 N ANISOU 2094 NE2 GLN A1088 22656 11064 9144 -365 -3110 2537 N ATOM 2095 N ALA A1089 128.766 44.449 47.693 1.00128.67 N ANISOU 2095 N ALA A1089 22600 15034 11253 -2877 -1525 2196 N ATOM 2096 CA ALA A1089 127.371 44.319 47.273 1.00140.56 C ANISOU 2096 CA ALA A1089 23820 16713 12874 -3509 -1302 2135 C ATOM 2097 C ALA A1089 126.891 45.585 46.564 1.00135.67 C ANISOU 2097 C ALA A1089 22422 16656 12472 -3396 -1225 1773 C ATOM 2098 O ALA A1089 126.255 45.525 45.493 1.00148.45 O ANISOU 2098 O ALA A1089 23803 18275 14327 -3581 -1279 1561 O ATOM 2099 CB ALA A1089 126.490 44.014 48.484 1.00148.37 C ANISOU 2099 CB ALA A1089 24933 17874 13568 -4068 -969 2443 C ATOM 2100 N ALA A1090 127.184 46.747 47.159 1.00113.64 N ANISOU 2100 N ALA A1090 19232 14337 9609 -3072 -1129 1686 N ATOM 2101 CA ALA A1090 126.825 48.009 46.518 1.00104.69 C ANISOU 2101 CA ALA A1090 17379 13672 8726 -2899 -1068 1377 C ATOM 2102 C ALA A1090 127.452 48.119 45.132 1.00104.61 C ANISOU 2102 C ALA A1090 17355 13421 8971 -2499 -1293 1199 C ATOM 2103 O ALA A1090 126.809 48.587 44.180 1.00109.08 O ANISOU 2103 O ALA A1090 17535 14192 9719 -2548 -1302 1012 O ATOM 2104 CB ALA A1090 127.252 49.183 47.396 1.00103.06 C ANISOU 2104 CB ALA A1090 16800 13893 8467 -2549 -960 1288 C ATOM 2105 N ALA A1091 128.707 47.682 45.001 1.00100.78 N ANISOU 2105 N ALA A1091 17298 12508 8484 -2082 -1477 1249 N ATOM 2106 CA ALA A1091 129.387 47.738 43.709 1.00 96.46 C ANISOU 2106 CA ALA A1091 16777 11730 8144 -1691 -1621 1077 C ATOM 2107 C ALA A1091 128.680 46.875 42.668 1.00 94.91 C ANISOU 2107 C ALA A1091 16783 11315 7962 -2022 -1730 1007 C ATOM 2108 O ALA A1091 128.529 47.283 41.507 1.00 99.26 O ANISOU 2108 O ALA A1091 17118 11982 8613 -1865 -1776 816 O ATOM 2109 CB ALA A1091 130.843 47.304 43.870 1.00 94.01 C ANISOU 2109 CB ALA A1091 16875 10975 7868 -1220 -1779 1108 C ATOM 2110 N GLU A1092 128.249 45.674 43.061 1.00103.40 N ANISOU 2110 N GLU A1092 18291 12057 8938 -2472 -1780 1156 N ATOM 2111 CA GLU A1092 127.530 44.812 42.124 1.00114.34 C ANISOU 2111 CA GLU A1092 19833 13208 10404 -2826 -1907 1021 C ATOM 2112 C GLU A1092 126.247 45.477 41.631 1.00124.05 C ANISOU 2112 C GLU A1092 20483 14939 11712 -3125 -1843 830 C ATOM 2113 O GLU A1092 125.935 45.453 40.425 1.00132.28 O ANISOU 2113 O GLU A1092 21430 16008 12822 -3071 -2014 579 O ATOM 2114 CB GLU A1092 127.218 43.467 42.780 1.00124.22 C ANISOU 2114 CB GLU A1092 21599 13980 11617 -3317 -1917 1240 C ATOM 2115 N GLN A1093 125.490 46.086 42.546 1.00141.71 N ANISOU 2115 N GLN A1093 22319 17597 13928 -3410 -1614 917 N ATOM 2116 CA GLN A1093 124.238 46.702 42.109 1.00146.59 C ANISOU 2116 CA GLN A1093 22335 18678 14686 -3683 -1580 700 C ATOM 2117 C GLN A1093 124.510 47.900 41.197 1.00142.49 C ANISOU 2117 C GLN A1093 21419 18486 14234 -3146 -1676 524 C ATOM 2118 O GLN A1093 123.769 48.148 40.228 1.00146.81 O ANISOU 2118 O GLN A1093 21675 19236 14871 -3183 -1836 304 O ATOM 2119 CB GLN A1093 123.394 47.096 43.322 1.00154.49 C ANISOU 2119 CB GLN A1093 22968 20060 15673 -4092 -1268 796 C ATOM 2120 CG GLN A1093 121.937 47.358 42.989 1.00160.71 C ANISOU 2120 CG GLN A1093 23167 21215 16682 -4530 -1231 549 C ATOM 2121 CD GLN A1093 121.092 47.566 44.226 1.00163.23 C ANISOU 2121 CD GLN A1093 23158 21866 16994 -5001 -850 626 C ATOM 2122 OE1 GLN A1093 121.611 47.635 45.341 1.00159.86 O ANISOU 2122 OE1 GLN A1093 22954 21460 16325 -4949 -620 871 O ATOM 2123 NE2 GLN A1093 119.779 47.637 44.041 1.00169.13 N ANISOU 2123 NE2 GLN A1093 23376 22887 18000 -5459 -784 388 N ATOM 2124 N LEU A1094 125.595 48.633 41.471 1.00137.65 N ANISOU 2124 N LEU A1094 20808 17898 13593 -2630 -1595 620 N ATOM 2125 CA LEU A1094 125.997 49.719 40.579 1.00128.93 C ANISOU 2125 CA LEU A1094 19405 16996 12587 -2110 -1629 516 C ATOM 2126 C LEU A1094 126.325 49.197 39.183 1.00135.11 C ANISOU 2126 C LEU A1094 20522 17518 13295 -1896 -1845 403 C ATOM 2127 O LEU A1094 126.019 49.852 38.176 1.00130.94 O ANISOU 2127 O LEU A1094 19755 17224 12771 -1673 -1928 295 O ATOM 2128 CB LEU A1094 127.194 50.463 41.171 1.00111.32 C ANISOU 2128 CB LEU A1094 17132 14742 10425 -1636 -1480 611 C ATOM 2129 N LYS A1095 126.962 48.025 39.103 1.00141.56 N ANISOU 2129 N LYS A1095 21914 17848 14023 -1927 -1943 422 N ATOM 2130 CA LYS A1095 127.235 47.424 37.798 1.00138.18 C ANISOU 2130 CA LYS A1095 21825 17176 13500 -1748 -2142 247 C ATOM 2131 C LYS A1095 125.943 47.150 37.040 1.00149.70 C ANISOU 2131 C LYS A1095 23126 18831 14924 -2100 -2360 26 C ATOM 2132 O LYS A1095 125.855 47.394 35.824 1.00164.35 O ANISOU 2132 O LYS A1095 24974 20822 16650 -1835 -2519 -149 O ATOM 2133 CB LYS A1095 128.030 46.130 37.967 1.00129.22 C ANISOU 2133 CB LYS A1095 21305 15448 12347 -1774 -2226 264 C ATOM 2134 N THR A1096 124.939 46.612 37.738 1.00148.07 N ANISOU 2134 N THR A1096 22800 18635 14824 -2695 -2369 17 N ATOM 2135 CA THR A1096 123.637 46.397 37.105 1.00154.75 C ANISOU 2135 CA THR A1096 23375 19684 15737 -3064 -2590 -256 C ATOM 2136 C THR A1096 123.096 47.694 36.499 1.00157.60 C ANISOU 2136 C THR A1096 23190 20604 16088 -2780 -2657 -348 C ATOM 2137 O THR A1096 122.675 47.734 35.327 1.00166.41 O ANISOU 2137 O THR A1096 24266 21863 17098 -2634 -2953 -590 O ATOM 2138 CB THR A1096 122.645 45.828 38.122 1.00150.12 C ANISOU 2138 CB THR A1096 22621 19067 15352 -3766 -2466 -222 C ATOM 2139 N THR A1097 123.104 48.768 37.297 1.00144.78 N ANISOU 2139 N THR A1097 21153 19289 14566 -2673 -2407 -166 N ATOM 2140 CA THR A1097 122.638 50.065 36.799 1.00138.27 C ANISOU 2140 CA THR A1097 19805 18934 13799 -2368 -2459 -214 C ATOM 2141 C THR A1097 123.390 50.496 35.538 1.00136.93 C ANISOU 2141 C THR A1097 19877 18739 13410 -1757 -2580 -194 C ATOM 2142 O THR A1097 122.780 50.947 34.552 1.00135.29 O ANISOU 2142 O THR A1097 19488 18803 13113 -1574 -2831 -322 O ATOM 2143 CB THR A1097 122.785 51.129 37.884 1.00126.45 C ANISOU 2143 CB THR A1097 17890 17676 12477 -2279 -2144 -39 C ATOM 2144 OG1 THR A1097 121.857 50.875 38.946 1.00126.21 O ANISOU 2144 OG1 THR A1097 17556 17797 12600 -2847 -2008 -92 O ATOM 2145 CG2 THR A1097 122.547 52.503 37.294 1.00126.28 C ANISOU 2145 CG2 THR A1097 17402 18018 12561 -1859 -2190 -46 C ATOM 2146 N ARG A1098 124.723 50.392 35.567 1.00131.67 N ANISOU 2146 N ARG A1098 19614 17760 12653 -1417 -2392 -30 N ATOM 2147 CA ARG A1098 125.525 50.837 34.430 1.00124.59 C ANISOU 2147 CA ARG A1098 18946 16833 11558 -846 -2384 17 C ATOM 2148 C ARG A1098 125.166 50.070 33.163 1.00136.62 C ANISOU 2148 C ARG A1098 20812 18325 12772 -831 -2719 -228 C ATOM 2149 O ARG A1098 125.063 50.658 32.076 1.00127.81 O ANISOU 2149 O ARG A1098 19700 17442 11422 -456 -2834 -239 O ATOM 2150 CB ARG A1098 127.012 50.683 34.744 1.00115.33 C ANISOU 2150 CB ARG A1098 18114 15289 10419 -549 -2111 160 C ATOM 2151 N ASN A1099 124.971 48.753 33.281 1.00164.92 N ANISOU 2151 N ASN A1099 24707 21613 16342 -1224 -2889 -432 N ATOM 2152 CA ASN A1099 124.610 47.970 32.100 1.00174.16 C ANISOU 2152 CA ASN A1099 26182 22741 17249 -1225 -3244 -759 C ATOM 2153 C ASN A1099 123.261 48.406 31.539 1.00176.87 C ANISOU 2153 C ASN A1099 26108 23538 17555 -1336 -3592 -961 C ATOM 2154 O ASN A1099 123.082 48.481 30.312 1.00191.43 O ANISOU 2154 O ASN A1099 28105 25570 19058 -1025 -3878 -1146 O ATOM 2155 CB ASN A1099 124.596 46.478 32.429 1.00174.26 C ANISOU 2155 CB ASN A1099 26552 22283 17374 -1672 -3359 -960 C ATOM 2156 CG ASN A1099 125.977 45.937 32.720 1.00170.45 C ANISOU 2156 CG ASN A1099 26551 21320 16891 -1455 -3128 -827 C ATOM 2157 OD1 ASN A1099 126.963 46.358 32.112 1.00166.76 O ANISOU 2157 OD1 ASN A1099 26282 20844 16235 -927 -2977 -765 O ATOM 2158 ND2 ASN A1099 126.055 44.979 33.635 1.00172.49 N ANISOU 2158 ND2 ASN A1099 27005 21156 17377 -1855 -3093 -784 N ATOM 2159 N ALA A1100 122.296 48.693 32.421 1.00154.96 N ANISOU 2159 N ALA A1100 22802 20962 15115 -1756 -3581 -953 N ATOM 2160 CA ALA A1100 121.006 49.199 31.945 1.00144.59 C ANISOU 2160 CA ALA A1100 20992 20090 13854 -1828 -3925 -1173 C ATOM 2161 C ALA A1100 121.181 50.480 31.130 1.00138.86 C ANISOU 2161 C ALA A1100 20157 19715 12889 -1189 -3975 -995 C ATOM 2162 O ALA A1100 120.638 50.614 30.017 1.00148.57 O ANISOU 2162 O ALA A1100 21401 21200 13847 -944 -4386 -1193 O ATOM 2163 CB ALA A1100 120.068 49.438 33.127 1.00138.80 C ANISOU 2163 CB ALA A1100 19651 19521 13564 -2342 -3789 -1174 C ATOM 2164 N TYR A1101 121.935 51.439 31.680 1.00130.61 N ANISOU 2164 N TYR A1101 19008 18670 11949 -902 -3572 -619 N ATOM 2165 CA TYR A1101 122.150 52.703 30.976 1.00129.64 C ANISOU 2165 CA TYR A1101 18786 18795 11678 -313 -3544 -381 C ATOM 2166 C TYR A1101 122.799 52.478 29.613 1.00136.99 C ANISOU 2166 C TYR A1101 20309 19668 12073 155 -3654 -374 C ATOM 2167 O TYR A1101 122.438 53.133 28.622 1.00137.33 O ANISOU 2167 O TYR A1101 20354 20001 11826 554 -3891 -324 O ATOM 2168 CB TYR A1101 123.007 53.642 31.825 1.00126.50 C ANISOU 2168 CB TYR A1101 18208 18298 11559 -118 -3051 -27 C ATOM 2169 N ILE A1102 123.750 51.544 29.539 1.00139.42 N ANISOU 2169 N ILE A1102 21141 19610 12223 134 -3487 -430 N ATOM 2170 CA ILE A1102 124.456 51.319 28.279 1.00142.76 C ANISOU 2170 CA ILE A1102 22135 19985 12122 587 -3506 -454 C ATOM 2171 C ILE A1102 123.533 50.700 27.234 1.00150.57 C ANISOU 2171 C ILE A1102 23283 21205 12724 558 -4080 -856 C ATOM 2172 O ILE A1102 123.605 51.047 26.049 1.00150.79 O ANISOU 2172 O ILE A1102 23600 21462 12230 1033 -4225 -835 O ATOM 2173 CB ILE A1102 125.715 50.465 28.507 1.00146.27 C ANISOU 2173 CB ILE A1102 23040 19964 12571 584 -3185 -475 C ATOM 2174 CG1 ILE A1102 126.696 51.230 29.388 1.00137.17 C ANISOU 2174 CG1 ILE A1102 21710 18633 11774 732 -2666 -108 C ATOM 2175 CG2 ILE A1102 126.366 50.102 27.182 1.00155.65 C ANISOU 2175 CG2 ILE A1102 24810 21124 13207 1011 -3192 -596 C ATOM 2176 CD1 ILE A1102 127.103 52.556 28.807 1.00133.52 C ANISOU 2176 CD1 ILE A1102 21156 18362 11213 1255 -2393 232 C ATOM 2177 N GLN A1103 122.668 49.767 27.641 1.00158.79 N ANISOU 2177 N GLN A1103 24150 22181 14002 9 -4410 -1238 N ATOM 2178 CA GLN A1103 121.692 49.228 26.692 1.00166.69 C ANISOU 2178 CA GLN A1103 25189 23415 14731 -41 -5017 -1704 C ATOM 2179 C GLN A1103 120.811 50.341 26.123 1.00167.81 C ANISOU 2179 C GLN A1103 24963 24074 14722 283 -5348 -1630 C ATOM 2180 O GLN A1103 120.614 50.445 24.895 1.00167.80 O ANISOU 2180 O GLN A1103 25241 24349 14166 707 -5725 -1773 O ATOM 2181 CB GLN A1103 120.842 48.151 27.368 1.00170.45 C ANISOU 2181 CB GLN A1103 25410 23697 15658 -756 -5251 -2107 C ATOM 2182 N LYS A1104 120.276 51.189 27.011 1.00167.43 N ANISOU 2182 N LYS A1104 24300 24167 15148 120 -5224 -1415 N ATOM 2183 CA LYS A1104 119.406 52.276 26.561 1.00169.22 C ANISOU 2183 CA LYS A1104 24120 24840 15337 436 -5558 -1345 C ATOM 2184 C LYS A1104 120.129 53.218 25.605 1.00165.57 C ANISOU 2184 C LYS A1104 24057 24505 14346 1177 -5430 -923 C ATOM 2185 O LYS A1104 119.530 53.721 24.645 1.00178.37 O ANISOU 2185 O LYS A1104 25689 26473 15610 1577 -5869 -943 O ATOM 2186 CB LYS A1104 118.866 53.043 27.764 1.00167.47 C ANISOU 2186 CB LYS A1104 23174 24693 15762 152 -5347 -1191 C ATOM 2187 CG LYS A1104 117.827 52.268 28.548 1.00169.14 C ANISOU 2187 CG LYS A1104 22900 24902 16462 -558 -5529 -1622 C ATOM 2188 CD LYS A1104 117.448 52.979 29.840 1.00163.08 C ANISOU 2188 CD LYS A1104 21475 24204 16284 -848 -5190 -1466 C ATOM 2189 CE LYS A1104 116.737 54.312 29.597 1.00162.19 C ANISOU 2189 CE LYS A1104 20821 24482 16322 -466 -5412 -1374 C ATOM 2190 NZ LYS A1104 116.315 54.925 30.893 1.00152.35 N ANISOU 2190 NZ LYS A1104 18897 23311 15677 -784 -5076 -1325 N ATOM 2191 N TYR A1105 121.414 53.480 25.851 1.00152.56 N ANISOU 2191 N TYR A1105 22729 22569 12669 1370 -4816 -528 N ATOM 2192 CA TYR A1105 122.156 54.325 24.917 1.00147.63 C ANISOU 2192 CA TYR A1105 22509 22016 11566 2034 -4596 -107 C ATOM 2193 C TYR A1105 122.406 53.628 23.584 1.00146.28 C ANISOU 2193 C TYR A1105 22854 21872 10855 2222 -4683 -290 C ATOM 2194 O TYR A1105 122.300 54.258 22.523 1.00144.30 O ANISOU 2194 O TYR A1105 22731 21819 10279 2629 -4721 -77 O ATOM 2195 CB TYR A1105 123.483 54.779 25.517 1.00138.14 C ANISOU 2195 CB TYR A1105 21404 20461 10620 2139 -3851 309 C ATOM 2196 CG TYR A1105 124.418 55.315 24.448 1.00131.62 C ANISOU 2196 CG TYR A1105 21079 19605 9324 2716 -3496 676 C ATOM 2197 CD1 TYR A1105 124.152 56.511 23.789 1.00141.07 C ANISOU 2197 CD1 TYR A1105 22174 20986 10439 3128 -3476 1067 C ATOM 2198 CD2 TYR A1105 125.559 54.610 24.083 1.00130.57 C ANISOU 2198 CD2 TYR A1105 21417 19190 9002 2762 -3094 621 C ATOM 2199 CE1 TYR A1105 125.003 56.990 22.795 1.00160.66 C ANISOU 2199 CE1 TYR A1105 25044 23365 12633 3531 -3031 1416 C ATOM 2200 CE2 TYR A1105 126.415 55.082 23.097 1.00153.67 C ANISOU 2200 CE2 TYR A1105 24675 22058 11654 3183 -2651 922 C ATOM 2201 CZ TYR A1105 126.134 56.271 22.455 1.00165.72 C ANISOU 2201 CZ TYR A1105 26122 23764 13080 3545 -2603 1330 C ATOM 2202 OH TYR A1105 126.986 56.738 21.474 1.00164.47 O ANISOU 2202 OH TYR A1105 26325 23526 12641 3929 -2126 1644 O ATOM 2203 N LEU A1106 122.768 52.344 23.616 1.00140.81 N ANISOU 2203 N LEU A1106 22456 20949 10095 1930 -4684 -674 N ATOM 2204 CA LEU A1106 123.210 51.673 22.398 1.00134.51 C ANISOU 2204 CA LEU A1106 22133 20141 8833 2135 -4655 -861 C ATOM 2205 C LEU A1106 122.073 51.532 21.395 1.00152.42 C ANISOU 2205 C LEU A1106 24307 22784 10821 2194 -5255 -1172 C ATOM 2206 O LEU A1106 122.288 51.665 20.180 1.00163.16 O ANISOU 2206 O LEU A1106 25998 24300 11694 2574 -5232 -1110 O ATOM 2207 CB LEU A1106 123.802 50.306 22.736 1.00135.30 C ANISOU 2207 CB LEU A1106 22529 19869 9009 1815 -4569 -1247 C ATOM 2208 N VAL A 240 120.855 51.262 21.879 1.00153.27 N ANISOU 2208 N VAL A 240 21987 24532 11718 -1584 -1260 3566 N ATOM 2209 CA VAL A 240 119.721 51.169 20.953 1.00156.04 C ANISOU 2209 CA VAL A 240 22330 24476 12480 -1728 -886 3560 C ATOM 2210 C VAL A 240 119.505 52.502 20.233 1.00155.95 C ANISOU 2210 C VAL A 240 22058 24538 12659 -1962 -762 2989 C ATOM 2211 O VAL A 240 119.328 52.552 19.001 1.00159.96 O ANISOU 2211 O VAL A 240 22385 24706 13687 -1920 -721 2913 O ATOM 2212 CB VAL A 240 118.452 50.706 21.692 1.00157.21 C ANISOU 2212 CB VAL A 240 22783 24507 12441 -1909 -438 3743 C ATOM 2213 CG1 VAL A 240 117.241 50.806 20.777 1.00154.20 C ANISOU 2213 CG1 VAL A 240 22338 23755 12495 -2110 -30 3632 C ATOM 2214 CG2 VAL A 240 118.619 49.275 22.187 1.00160.60 C ANISOU 2214 CG2 VAL A 240 23496 24745 12780 -1665 -536 4349 C ATOM 2215 N SER A 241 119.516 53.601 20.997 1.00152.44 N ANISOU 2215 N SER A 241 21593 24457 11869 -2175 -686 2539 N ATOM 2216 CA SER A 241 119.367 54.930 20.412 1.00141.72 C ANISOU 2216 CA SER A 241 20020 23141 10684 -2388 -562 1957 C ATOM 2217 C SER A 241 120.464 55.212 19.392 1.00151.92 C ANISOU 2217 C SER A 241 21010 24400 12314 -2233 -935 1846 C ATOM 2218 O SER A 241 120.197 55.767 18.317 1.00148.44 O ANISOU 2218 O SER A 241 20364 23590 12448 -2227 -799 1545 O ATOM 2219 CB SER A 241 119.380 55.986 21.517 1.00131.82 C ANISOU 2219 CB SER A 241 18814 22257 9015 -2600 -469 1502 C ATOM 2220 OG SER A 241 119.303 57.293 20.976 1.00128.88 O ANISOU 2220 OG SER A 241 18253 21869 8846 -2787 -352 919 O ATOM 2221 N HIS A 242 121.704 54.835 19.717 1.00154.38 N ANISOU 2221 N HIS A 242 21241 24938 12479 -2019 -1370 2032 N ATOM 2222 CA HIS A 242 122.828 55.040 18.805 1.00144.59 C ANISOU 2222 CA HIS A 242 19678 23702 11559 -1858 -1723 1940 C ATOM 2223 C HIS A 242 122.594 54.326 17.478 1.00134.78 C ANISOU 2223 C HIS A 242 18340 21947 10921 -1639 -1680 2178 C ATOM 2224 O HIS A 242 122.775 54.909 16.396 1.00104.02 O ANISOU 2224 O HIS A 242 14191 17806 7525 -1618 -1661 1877 O ATOM 2225 CB HIS A 242 124.116 54.541 19.465 1.00146.66 C ANISOU 2225 CB HIS A 242 19874 24233 11616 -1609 -2154 2151 C ATOM 2226 CG HIS A 242 125.361 54.841 18.686 1.00149.03 C ANISOU 2226 CG HIS A 242 19802 24599 12226 -1463 -2496 2000 C ATOM 2227 ND1 HIS A 242 125.970 56.077 18.706 1.00151.96 N ANISOU 2227 ND1 HIS A 242 19940 25212 12585 -1673 -2576 1488 N ATOM 2228 CD2 HIS A 242 126.106 54.068 17.861 1.00149.10 C ANISOU 2228 CD2 HIS A 242 19625 24434 12591 -1133 -2745 2275 C ATOM 2229 CE1 HIS A 242 127.041 56.051 17.933 1.00150.06 C ANISOU 2229 CE1 HIS A 242 19375 24968 12673 -1496 -2854 1470 C ATOM 2230 NE2 HIS A 242 127.145 54.844 17.406 1.00148.55 N ANISOU 2230 NE2 HIS A 242 19198 24538 12705 -1155 -2960 1933 N ATOM 2231 N ARG A 243 122.197 53.051 17.545 1.00153.80 N ANISOU 2231 N ARG A 243 20959 24119 13358 -1458 -1641 2697 N ATOM 2232 CA ARG A 243 121.981 52.276 16.325 1.00155.97 C ANISOU 2232 CA ARG A 243 21161 23834 14267 -1226 -1588 2891 C ATOM 2233 C ARG A 243 120.888 52.893 15.459 1.00154.34 C ANISOU 2233 C ARG A 243 20883 23221 14540 -1392 -1194 2532 C ATOM 2234 O ARG A 243 121.059 53.030 14.240 1.00169.04 O ANISOU 2234 O ARG A 243 22527 24772 16928 -1272 -1220 2382 O ATOM 2235 CB ARG A 243 121.637 50.828 16.671 1.00162.32 C ANISOU 2235 CB ARG A 243 22255 24426 14994 -1058 -1571 3490 C ATOM 2236 N LYS A 244 119.756 53.268 16.065 1.00134.25 N ANISOU 2236 N LYS A 244 18510 20688 11810 -1655 -825 2392 N ATOM 2237 CA LYS A 244 118.693 53.900 15.280 1.00124.30 C ANISOU 2237 CA LYS A 244 17151 19074 11004 -1787 -465 2046 C ATOM 2238 C LYS A 244 119.171 55.200 14.635 1.00114.92 C ANISOU 2238 C LYS A 244 15699 17927 10038 -1840 -531 1545 C ATOM 2239 O LYS A 244 118.893 55.464 13.448 1.00112.40 O ANISOU 2239 O LYS A 244 15211 17243 10255 -1775 -447 1380 O ATOM 2240 CB LYS A 244 117.472 54.160 16.163 1.00125.08 C ANISOU 2240 CB LYS A 244 17442 19257 10826 -2053 -58 1951 C ATOM 2241 N ALA A 245 119.887 56.025 15.410 1.00104.91 N ANISOU 2241 N ALA A 245 14407 17104 8351 -1973 -681 1302 N ATOM 2242 CA ALA A 245 120.373 57.304 14.907 1.00 99.86 C ANISOU 2242 CA ALA A 245 13547 16501 7896 -2072 -728 820 C ATOM 2243 C ALA A 245 121.272 57.122 13.691 1.00122.50 C ANISOU 2243 C ALA A 245 16162 19178 11203 -1854 -988 879 C ATOM 2244 O ALA A 245 121.184 57.892 12.730 1.00119.03 O ANISOU 2244 O ALA A 245 15560 18488 11178 -1882 -892 584 O ATOM 2245 CB ALA A 245 121.111 58.057 16.014 1.00 97.08 C ANISOU 2245 CB ALA A 245 13218 16686 6982 -2267 -892 577 C ATOM 2246 N LEU A 246 122.146 56.113 13.710 1.00134.90 N ANISOU 2246 N LEU A 246 17702 20864 12688 -1622 -1310 1264 N ATOM 2247 CA LEU A 246 123.001 55.898 12.540 1.00127.21 C ANISOU 2247 CA LEU A 246 16475 19723 12135 -1399 -1527 1307 C ATOM 2248 C LEU A 246 122.229 55.294 11.371 1.00111.31 C ANISOU 2248 C LEU A 246 14470 17166 10655 -1247 -1334 1433 C ATOM 2249 O LEU A 246 122.514 55.607 10.202 1.00110.94 O ANISOU 2249 O LEU A 246 14224 16902 11024 -1168 -1352 1278 O ATOM 2250 CB LEU A 246 124.198 55.017 12.894 1.00133.68 C ANISOU 2250 CB LEU A 246 17226 20835 12731 -1158 -1930 1657 C ATOM 2251 CG LEU A 246 125.311 55.723 13.660 1.00139.87 C ANISOU 2251 CG LEU A 246 17855 22186 13105 -1276 -2225 1465 C ATOM 2252 CD1 LEU A 246 126.388 54.732 14.059 1.00152.29 C ANISOU 2252 CD1 LEU A 246 19354 24056 14452 -988 -2634 1868 C ATOM 2253 CD2 LEU A 246 125.896 56.832 12.797 1.00127.09 C ANISOU 2253 CD2 LEU A 246 15935 20548 11805 -1396 -2240 1032 C ATOM 2254 N THR A 247 121.261 54.417 11.659 1.00103.49 N ANISOU 2254 N THR A 247 13710 15965 9647 -1222 -1150 1713 N ATOM 2255 CA THR A 247 120.536 53.750 10.582 1.00107.36 C ANISOU 2255 CA THR A 247 14206 15958 10628 -1097 -994 1829 C ATOM 2256 C THR A 247 119.772 54.754 9.726 1.00 93.87 C ANISOU 2256 C THR A 247 12377 14011 9278 -1233 -744 1439 C ATOM 2257 O THR A 247 119.822 54.690 8.487 1.00 86.05 O ANISOU 2257 O THR A 247 11246 12731 8716 -1105 -761 1384 O ATOM 2258 CB THR A 247 119.585 52.697 11.155 1.00116.46 C ANISOU 2258 CB THR A 247 15627 16943 11679 -1114 -814 2175 C ATOM 2259 OG1 THR A 247 120.331 51.767 11.949 1.00115.24 O ANISOU 2259 OG1 THR A 247 15613 16991 11183 -961 -1061 2582 O ATOM 2260 CG2 THR A 247 118.892 51.941 10.029 1.00113.27 C ANISOU 2260 CG2 THR A 247 15216 16031 11789 -1005 -683 2277 C ATOM 2261 N THR A 248 119.064 55.695 10.363 1.00 83.23 N ANISOU 2261 N THR A 248 11086 12783 7753 -1475 -511 1163 N ATOM 2262 CA THR A 248 118.315 56.676 9.572 1.00 93.36 C ANISOU 2262 CA THR A 248 12259 13823 9391 -1566 -281 811 C ATOM 2263 C THR A 248 119.246 57.497 8.675 1.00 81.48 C ANISOU 2263 C THR A 248 10545 12308 8107 -1518 -449 578 C ATOM 2264 O THR A 248 118.963 57.708 7.484 1.00 73.46 O ANISOU 2264 O THR A 248 9417 10986 7508 -1440 -388 488 O ATOM 2265 CB THR A 248 117.477 57.579 10.486 1.00110.45 C ANISOU 2265 CB THR A 248 14518 16127 11321 -1806 2 533 C ATOM 2266 OG1 THR A 248 116.738 58.523 9.698 1.00118.43 O ANISOU 2266 OG1 THR A 248 15416 16873 12709 -1847 215 215 O ATOM 2267 CG2 THR A 248 118.337 58.324 11.490 1.00121.69 C ANISOU 2267 CG2 THR A 248 15971 17977 12290 -1952 -129 344 C ATOM 2268 N ILE A 249 120.382 57.932 9.225 1.00 96.40 N ANISOU 2268 N ILE A 249 12372 14549 9706 -1573 -669 492 N ATOM 2269 CA ILE A 249 121.350 58.733 8.479 1.00 98.32 C ANISOU 2269 CA ILE A 249 12405 14825 10128 -1578 -815 270 C ATOM 2270 C ILE A 249 121.831 57.985 7.243 1.00 84.59 C ANISOU 2270 C ILE A 249 10526 12868 8745 -1328 -956 471 C ATOM 2271 O ILE A 249 121.840 58.522 6.122 1.00 58.25 O ANISOU 2271 O ILE A 249 7070 9307 5755 -1308 -896 315 O ATOM 2272 CB ILE A 249 122.532 59.099 9.393 1.00 95.07 C ANISOU 2272 CB ILE A 249 11927 14884 9311 -1687 -1063 184 C ATOM 2273 CG1 ILE A 249 122.076 60.004 10.543 1.00 88.23 C ANISOU 2273 CG1 ILE A 249 11204 14232 8088 -1966 -904 -105 C ATOM 2274 CG2 ILE A 249 123.653 59.725 8.590 1.00 80.96 C ANISOU 2274 CG2 ILE A 249 9886 13149 7726 -1692 -1231 10 C ATOM 2275 CD1 ILE A 249 123.108 60.125 11.641 1.00 80.07 C ANISOU 2275 CD1 ILE A 249 10148 13720 6556 -2079 -1171 -144 C ATOM 2276 N ILE A 250 122.267 56.739 7.435 1.00 77.73 N ANISOU 2276 N ILE A 250 9687 12065 7782 -1125 -1142 822 N ATOM 2277 CA ILE A 250 122.861 55.998 6.328 1.00 65.38 C ANISOU 2277 CA ILE A 250 7988 10324 6529 -868 -1284 985 C ATOM 2278 C ILE A 250 121.811 55.671 5.271 1.00 69.23 C ANISOU 2278 C ILE A 250 8532 10361 7410 -801 -1077 999 C ATOM 2279 O ILE A 250 122.096 55.697 4.065 1.00 55.70 O ANISOU 2279 O ILE A 250 6685 8470 6009 -687 -1100 939 O ATOM 2280 CB ILE A 250 123.571 54.737 6.850 1.00 60.52 C ANISOU 2280 CB ILE A 250 7406 9859 5731 -637 -1531 1358 C ATOM 2281 CG1 ILE A 250 124.742 55.129 7.755 1.00 66.47 C ANISOU 2281 CG1 ILE A 250 8033 11114 6108 -684 -1793 1321 C ATOM 2282 CG2 ILE A 250 124.075 53.896 5.695 1.00 67.87 C ANISOU 2282 CG2 ILE A 250 8218 10558 7013 -347 -1634 1504 C ATOM 2283 CD1 ILE A 250 125.350 53.967 8.516 1.00 81.01 C ANISOU 2283 CD1 ILE A 250 9937 13155 7690 -454 -2051 1716 C ATOM 2284 N ILE A 251 120.577 55.377 5.694 1.00 72.53 N ANISOU 2284 N ILE A 251 9135 10616 7806 -885 -868 1066 N ATOM 2285 CA ILE A 251 119.523 55.116 4.715 1.00 59.73 C ANISOU 2285 CA ILE A 251 7534 8605 6555 -850 -687 1049 C ATOM 2286 C ILE A 251 119.252 56.356 3.875 1.00 63.57 C ANISOU 2286 C ILE A 251 7895 8990 7269 -939 -572 724 C ATOM 2287 O ILE A 251 119.066 56.266 2.653 1.00 65.72 O ANISOU 2287 O ILE A 251 8091 9019 7862 -835 -559 692 O ATOM 2288 CB ILE A 251 118.247 54.609 5.409 1.00 68.71 C ANISOU 2288 CB ILE A 251 8854 9631 7623 -959 -470 1167 C ATOM 2289 CG1 ILE A 251 118.494 53.230 6.015 1.00 75.13 C ANISOU 2289 CG1 ILE A 251 9826 10445 8277 -845 -579 1552 C ATOM 2290 CG2 ILE A 251 117.093 54.533 4.422 1.00 47.81 C ANISOU 2290 CG2 ILE A 251 6173 6634 5359 -964 -286 1083 C ATOM 2291 CD1 ILE A 251 118.806 52.177 4.979 1.00 79.33 C ANISOU 2291 CD1 ILE A 251 10332 10686 9123 -610 -700 1726 C ATOM 2292 N THR A 252 119.219 57.533 4.507 1.00 72.89 N ANISOU 2292 N THR A 252 9071 10344 8281 -1129 -484 480 N ATOM 2293 CA THR A 252 118.987 58.745 3.726 1.00 55.66 C ANISOU 2293 CA THR A 252 6799 8020 6330 -1200 -372 196 C ATOM 2294 C THR A 252 120.126 58.993 2.747 1.00 57.53 C ANISOU 2294 C THR A 252 6881 8270 6710 -1115 -541 162 C ATOM 2295 O THR A 252 119.885 59.352 1.589 1.00 46.75 O ANISOU 2295 O THR A 252 5454 6677 5632 -1060 -484 89 O ATOM 2296 CB THR A 252 118.795 59.954 4.638 1.00 69.54 C ANISOU 2296 CB THR A 252 8605 9927 7890 -1419 -236 -80 C ATOM 2297 OG1 THR A 252 117.652 59.740 5.472 1.00 69.61 O ANISOU 2297 OG1 THR A 252 8743 9926 7780 -1494 -31 -67 O ATOM 2298 CG2 THR A 252 118.585 61.224 3.804 1.00 43.40 C ANISOU 2298 CG2 THR A 252 5229 6411 4851 -1471 -118 -348 C ATOM 2299 N LEU A 253 121.375 58.803 3.183 1.00 75.32 N ANISOU 2299 N LEU A 253 9053 10811 8754 -1101 -749 220 N ATOM 2300 CA LEU A 253 122.485 58.981 2.249 1.00 60.55 C ANISOU 2300 CA LEU A 253 6997 8982 7027 -1025 -886 188 C ATOM 2301 C LEU A 253 122.377 58.017 1.073 1.00 58.24 C ANISOU 2301 C LEU A 253 6675 8452 7003 -786 -914 362 C ATOM 2302 O LEU A 253 122.584 58.414 -0.077 1.00 45.98 O ANISOU 2302 O LEU A 253 5029 6770 5670 -751 -883 275 O ATOM 2303 CB LEU A 253 123.833 58.832 2.960 1.00 69.16 C ANISOU 2303 CB LEU A 253 7957 10464 7857 -1032 -1123 229 C ATOM 2304 CG LEU A 253 124.304 60.058 3.747 1.00 75.18 C ANISOU 2304 CG LEU A 253 8675 11488 8403 -1310 -1128 -43 C ATOM 2305 CD1 LEU A 253 125.528 59.745 4.592 1.00 73.91 C ANISOU 2305 CD1 LEU A 253 8374 11769 7938 -1309 -1402 21 C ATOM 2306 CD2 LEU A 253 124.611 61.180 2.761 1.00 74.40 C ANISOU 2306 CD2 LEU A 253 8464 11252 8554 -1434 -1032 -277 C ATOM 2307 N ILE A 254 122.014 56.760 1.332 1.00 58.49 N ANISOU 2307 N ILE A 254 6806 8404 7014 -635 -956 602 N ATOM 2308 CA ILE A 254 121.936 55.777 0.251 1.00 50.73 C ANISOU 2308 CA ILE A 254 5813 7179 6282 -416 -984 735 C ATOM 2309 C ILE A 254 120.837 56.151 -0.737 1.00 50.42 C ANISOU 2309 C ILE A 254 5812 6842 6501 -456 -811 613 C ATOM 2310 O ILE A 254 121.060 56.201 -1.957 1.00 42.29 O ANISOU 2310 O ILE A 254 4704 5698 5668 -362 -821 559 O ATOM 2311 CB ILE A 254 121.724 54.364 0.824 1.00 41.90 C ANISOU 2311 CB ILE A 254 4830 5988 5101 -273 -1049 1017 C ATOM 2312 CG1 ILE A 254 122.957 53.920 1.620 1.00 44.81 C ANISOU 2312 CG1 ILE A 254 5134 6658 5232 -158 -1272 1176 C ATOM 2313 CG2 ILE A 254 121.416 53.381 -0.287 1.00 40.68 C ANISOU 2313 CG2 ILE A 254 4705 5517 5234 -88 -1037 1100 C ATOM 2314 CD1 ILE A 254 122.733 52.666 2.442 1.00 47.31 C ANISOU 2314 CD1 ILE A 254 5634 6917 5425 -38 -1333 1493 C ATOM 2315 N ILE A 255 119.626 56.400 -0.228 1.00 60.27 N ANISOU 2315 N ILE A 255 7172 7987 7740 -586 -652 572 N ATOM 2316 CA ILE A 255 118.509 56.762 -1.100 1.00 59.54 C ANISOU 2316 CA ILE A 255 7086 7644 7893 -606 -510 463 C ATOM 2317 C ILE A 255 118.867 57.988 -1.930 1.00 59.15 C ANISOU 2317 C ILE A 255 6942 7590 7942 -642 -489 275 C ATOM 2318 O ILE A 255 118.793 57.971 -3.166 1.00 50.11 O ANISOU 2318 O ILE A 255 5753 6299 6988 -546 -503 259 O ATOM 2319 CB ILE A 255 117.225 56.995 -0.282 1.00 56.36 C ANISOU 2319 CB ILE A 255 6767 7191 7454 -747 -327 418 C ATOM 2320 CG1 ILE A 255 116.730 55.694 0.356 1.00 56.73 C ANISOU 2320 CG1 ILE A 255 6924 7188 7443 -732 -311 635 C ATOM 2321 CG2 ILE A 255 116.131 57.601 -1.148 1.00 58.01 C ANISOU 2321 CG2 ILE A 255 6929 7194 7920 -754 -200 277 C ATOM 2322 CD1 ILE A 255 115.605 55.897 1.363 1.00 69.49 C ANISOU 2322 CD1 ILE A 255 8612 8830 8961 -899 -104 603 C ATOM 2323 N PHE A 256 119.296 59.060 -1.255 1.00 67.61 N ANISOU 2323 N PHE A 256 7997 8821 8870 -794 -456 134 N ATOM 2324 CA PHE A 256 119.608 60.305 -1.946 1.00 69.71 C ANISOU 2324 CA PHE A 256 8208 9041 9238 -865 -407 -35 C ATOM 2325 C PHE A 256 120.660 60.079 -3.020 1.00 56.21 C ANISOU 2325 C PHE A 256 6388 7366 7602 -762 -521 18 C ATOM 2326 O PHE A 256 120.482 60.488 -4.173 1.00 71.68 O ANISOU 2326 O PHE A 256 8334 9168 9731 -717 -476 -13 O ATOM 2327 CB PHE A 256 120.108 61.351 -0.950 1.00 78.59 C ANISOU 2327 CB PHE A 256 9338 10342 10181 -1071 -371 -208 C ATOM 2328 CG PHE A 256 120.228 62.730 -1.533 1.00 79.49 C ANISOU 2328 CG PHE A 256 9443 10331 10427 -1181 -272 -391 C ATOM 2329 CD1 PHE A 256 119.147 63.591 -1.523 1.00 80.75 C ANISOU 2329 CD1 PHE A 256 9695 10272 10715 -1223 -95 -521 C ATOM 2330 CD2 PHE A 256 121.398 63.145 -2.143 1.00 85.32 C ANISOU 2330 CD2 PHE A 256 10079 11153 11185 -1232 -343 -420 C ATOM 2331 CE1 PHE A 256 119.248 64.857 -2.066 1.00 87.63 C ANISOU 2331 CE1 PHE A 256 10592 10975 11728 -1305 -1 -660 C ATOM 2332 CE2 PHE A 256 121.496 64.404 -2.697 1.00 94.35 C ANISOU 2332 CE2 PHE A 256 11246 12142 12460 -1353 -233 -558 C ATOM 2333 CZ PHE A 256 120.423 65.264 -2.656 1.00 92.54 C ANISOU 2333 CZ PHE A 256 11145 11658 12357 -1383 -67 -668 C ATOM 2334 N PHE A 257 121.767 59.424 -2.656 1.00 56.12 N ANISOU 2334 N PHE A 257 6289 7579 7454 -709 -669 105 N ATOM 2335 CA PHE A 257 122.886 59.214 -3.559 1.00 57.86 C ANISOU 2335 CA PHE A 257 6365 7888 7732 -610 -759 133 C ATOM 2336 C PHE A 257 122.377 58.508 -4.800 1.00 51.53 C ANISOU 2336 C PHE A 257 5598 6862 7118 -427 -738 207 C ATOM 2337 O PHE A 257 122.369 59.071 -5.896 1.00 65.91 O ANISOU 2337 O PHE A 257 7400 8587 9054 -430 -673 144 O ATOM 2338 CB PHE A 257 123.951 58.312 -2.940 1.00 70.14 C ANISOU 2338 CB PHE A 257 7809 9699 9142 -500 -936 252 C ATOM 2339 CG PHE A 257 125.345 58.585 -3.429 1.00 82.39 C ANISOU 2339 CG PHE A 257 9139 11473 10694 -493 -1011 200 C ATOM 2340 CD1 PHE A 257 126.347 58.895 -2.525 1.00 85.95 C ANISOU 2340 CD1 PHE A 257 9439 12255 10962 -599 -1131 155 C ATOM 2341 CD2 PHE A 257 125.607 58.743 -4.787 1.00 98.98 C ANISOU 2341 CD2 PHE A 257 11171 13477 12960 -432 -939 162 C ATOM 2342 CE1 PHE A 257 127.627 59.174 -2.953 1.00 83.49 C ANISOU 2342 CE1 PHE A 257 8875 12179 10668 -618 -1191 91 C ATOM 2343 CE2 PHE A 257 126.883 59.059 -5.223 1.00 97.67 C ANISOU 2343 CE2 PHE A 257 10779 13537 12793 -459 -968 103 C ATOM 2344 CZ PHE A 257 127.890 59.272 -4.304 1.00 88.22 C ANISOU 2344 CZ PHE A 257 9399 12670 11449 -555 -1091 64 C ATOM 2345 N LEU A 258 121.937 57.261 -4.608 1.00 49.58 N ANISOU 2345 N LEU A 258 5421 6528 6891 -281 -792 343 N ATOM 2346 CA LEU A 258 121.704 56.370 -5.737 1.00 60.63 C ANISOU 2346 CA LEU A 258 6840 7750 8448 -101 -807 393 C ATOM 2347 C LEU A 258 120.525 56.818 -6.591 1.00 55.10 C ANISOU 2347 C LEU A 258 6213 6831 7890 -143 -707 315 C ATOM 2348 O LEU A 258 120.523 56.588 -7.806 1.00 71.52 O ANISOU 2348 O LEU A 258 8283 8824 10066 -42 -713 290 O ATOM 2349 CB LEU A 258 121.479 54.947 -5.230 1.00 56.07 C ANISOU 2349 CB LEU A 258 6345 7084 7874 34 -878 551 C ATOM 2350 CG LEU A 258 122.653 54.349 -4.446 1.00 64.97 C ANISOU 2350 CG LEU A 258 7399 8420 8866 144 -1014 674 C ATOM 2351 CD1 LEU A 258 122.303 52.957 -3.943 1.00 59.37 C ANISOU 2351 CD1 LEU A 258 6827 7554 8178 281 -1066 869 C ATOM 2352 CD2 LEU A 258 123.927 54.324 -5.272 1.00 72.15 C ANISOU 2352 CD2 LEU A 258 8127 9473 9814 285 -1079 627 C ATOM 2353 N CYS A 259 119.515 57.452 -5.989 1.00 42.77 N ANISOU 2353 N CYS A 259 4718 5200 6334 -275 -617 270 N ATOM 2354 CA CYS A 259 118.355 57.845 -6.780 1.00 44.16 C ANISOU 2354 CA CYS A 259 4930 5189 6661 -279 -547 209 C ATOM 2355 C CYS A 259 118.627 59.081 -7.626 1.00 53.25 C ANISOU 2355 C CYS A 259 6054 6334 7844 -313 -503 126 C ATOM 2356 O CYS A 259 118.076 59.201 -8.725 1.00 64.47 O ANISOU 2356 O CYS A 259 7490 7638 9366 -243 -505 116 O ATOM 2357 CB CYS A 259 117.143 58.083 -5.877 1.00 44.21 C ANISOU 2357 CB CYS A 259 4983 5125 6690 -381 -446 182 C ATOM 2358 SG CYS A 259 116.418 56.586 -5.169 1.00 51.85 S ANISOU 2358 SG CYS A 259 6011 6020 7668 -367 -452 306 S ATOM 2359 N PHE A 260 119.472 60.000 -7.156 1.00 38.37 N ANISOU 2359 N PHE A 260 4138 4574 5868 -431 -469 72 N ATOM 2360 CA PHE A 260 119.544 61.316 -7.777 1.00 51.02 C ANISOU 2360 CA PHE A 260 5756 6106 7522 -508 -388 2 C ATOM 2361 C PHE A 260 120.878 61.633 -8.445 1.00 40.68 C ANISOU 2361 C PHE A 260 4373 4925 6159 -541 -400 4 C ATOM 2362 O PHE A 260 120.877 62.151 -9.566 1.00 47.89 O ANISOU 2362 O PHE A 260 5317 5754 7127 -518 -357 23 O ATOM 2363 CB PHE A 260 119.207 62.408 -6.748 1.00 37.94 C ANISOU 2363 CB PHE A 260 4148 4417 5850 -671 -282 -110 C ATOM 2364 CG PHE A 260 117.811 62.305 -6.183 1.00 47.99 C ANISOU 2364 CG PHE A 260 5473 5567 7194 -645 -219 -135 C ATOM 2365 CD1 PHE A 260 116.695 62.499 -6.989 1.00 41.72 C ANISOU 2365 CD1 PHE A 260 4698 4587 6568 -539 -191 -121 C ATOM 2366 CD2 PHE A 260 117.616 62.078 -4.828 1.00 42.28 C ANISOU 2366 CD2 PHE A 260 4767 4943 6356 -734 -182 -178 C ATOM 2367 CE1 PHE A 260 115.411 62.417 -6.457 1.00 40.11 C ANISOU 2367 CE1 PHE A 260 4490 4301 6450 -519 -120 -160 C ATOM 2368 CE2 PHE A 260 116.334 62.004 -4.295 1.00 48.65 C ANISOU 2368 CE2 PHE A 260 5601 5660 7225 -727 -84 -211 C ATOM 2369 CZ PHE A 260 115.235 62.176 -5.110 1.00 46.09 C ANISOU 2369 CZ PHE A 260 5257 5152 7102 -621 -48 -210 C ATOM 2370 N LEU A 261 122.011 61.359 -7.799 1.00 35.75 N ANISOU 2370 N LEU A 261 3640 4522 5421 -594 -455 -7 N ATOM 2371 CA LEU A 261 123.290 61.776 -8.390 1.00 48.01 C ANISOU 2371 CA LEU A 261 5075 6227 6941 -659 -440 -27 C ATOM 2372 C LEU A 261 123.619 61.068 -9.694 1.00 31.76 C ANISOU 2372 C LEU A 261 2975 4181 4913 -486 -456 40 C ATOM 2373 O LEU A 261 124.120 61.755 -10.624 1.00 48.02 O ANISOU 2373 O LEU A 261 5016 6252 6979 -551 -369 33 O ATOM 2374 CB LEU A 261 124.422 61.614 -7.360 1.00 42.83 C ANISOU 2374 CB LEU A 261 4262 5852 6159 -745 -521 -66 C ATOM 2375 CG LEU A 261 124.587 62.784 -6.365 1.00 52.54 C ANISOU 2375 CG LEU A 261 5503 7134 7327 -1011 -472 -203 C ATOM 2376 CD1 LEU A 261 123.470 62.821 -5.319 1.00 59.87 C ANISOU 2376 CD1 LEU A 261 6579 7952 8218 -1035 -455 -237 C ATOM 2377 CD2 LEU A 261 125.947 62.799 -5.668 1.00 84.74 C ANISOU 2377 CD2 LEU A 261 9373 11550 11275 -1130 -569 -265 C ATOM 2378 N PRO A 262 123.388 59.766 -9.890 1.00 41.03 N ANISOU 2378 N PRO A 262 4150 5340 6100 -283 -542 98 N ATOM 2379 CA PRO A 262 123.575 59.195 -11.231 1.00 39.87 C ANISOU 2379 CA PRO A 262 3996 5178 5975 -130 -534 114 C ATOM 2380 C PRO A 262 122.694 59.849 -12.276 1.00 37.73 C ANISOU 2380 C PRO A 262 3860 4735 5740 -146 -469 119 C ATOM 2381 O PRO A 262 123.161 60.151 -13.382 1.00 60.25 O ANISOU 2381 O PRO A 262 6707 7638 8548 -137 -405 124 O ATOM 2382 CB PRO A 262 123.226 57.712 -11.049 1.00 31.36 C ANISOU 2382 CB PRO A 262 2943 4036 4935 66 -635 151 C ATOM 2383 CG PRO A 262 123.460 57.446 -9.615 1.00 31.52 C ANISOU 2383 CG PRO A 262 2920 4142 4913 31 -704 193 C ATOM 2384 CD PRO A 262 123.060 58.711 -8.905 1.00 43.32 C ANISOU 2384 CD PRO A 262 4455 5629 6375 -191 -641 149 C ATOM 2385 N TYR A 263 121.422 60.078 -11.941 1.00 47.58 N ANISOU 2385 N TYR A 263 5220 5801 7058 -164 -483 126 N ATOM 2386 CA TYR A 263 120.496 60.691 -12.887 1.00 37.43 C ANISOU 2386 CA TYR A 263 4044 4364 5815 -143 -457 149 C ATOM 2387 C TYR A 263 120.918 62.108 -13.252 1.00 42.41 C ANISOU 2387 C TYR A 263 4715 4976 6425 -276 -346 172 C ATOM 2388 O TYR A 263 120.896 62.475 -14.429 1.00 44.53 O ANISOU 2388 O TYR A 263 5051 5218 6652 -240 -316 231 O ATOM 2389 CB TYR A 263 119.072 60.670 -12.328 1.00 29.81 C ANISOU 2389 CB TYR A 263 3135 3236 4955 -128 -489 140 C ATOM 2390 CG TYR A 263 118.130 61.617 -13.037 1.00 38.50 C ANISOU 2390 CG TYR A 263 4318 4193 6120 -108 -468 169 C ATOM 2391 CD1 TYR A 263 117.750 61.408 -14.352 1.00 46.98 C ANISOU 2391 CD1 TYR A 263 5435 5254 7163 7 -534 209 C ATOM 2392 CD2 TYR A 263 117.607 62.715 -12.373 1.00 32.39 C ANISOU 2392 CD2 TYR A 263 3580 3297 5428 -188 -390 153 C ATOM 2393 CE1 TYR A 263 116.882 62.288 -14.997 1.00 48.07 C ANISOU 2393 CE1 TYR A 263 5642 5276 7345 55 -546 269 C ATOM 2394 CE2 TYR A 263 116.742 63.597 -12.998 1.00 34.35 C ANISOU 2394 CE2 TYR A 263 3900 3392 5760 -126 -379 200 C ATOM 2395 CZ TYR A 263 116.380 63.383 -14.310 1.00 53.36 C ANISOU 2395 CZ TYR A 263 6340 5804 8131 3 -470 276 C ATOM 2396 OH TYR A 263 115.520 64.267 -14.926 1.00 45.11 O ANISOU 2396 OH TYR A 263 5361 4622 7156 95 -488 353 O ATOM 2397 N HIS A 264 121.304 62.926 -12.273 1.00 36.30 N ANISOU 2397 N HIS A 264 3918 4207 5668 -445 -279 128 N ATOM 2398 CA HIS A 264 121.727 64.281 -12.614 1.00 50.82 C ANISOU 2398 CA HIS A 264 5816 5977 7516 -602 -156 144 C ATOM 2399 C HIS A 264 123.019 64.279 -13.421 1.00 51.49 C ANISOU 2399 C HIS A 264 5816 6241 7505 -660 -95 173 C ATOM 2400 O HIS A 264 123.156 65.047 -14.384 1.00 52.66 O ANISOU 2400 O HIS A 264 6056 6319 7633 -712 2 254 O ATOM 2401 CB HIS A 264 121.870 65.134 -11.357 1.00 46.86 C ANISOU 2401 CB HIS A 264 5314 5434 7057 -797 -93 42 C ATOM 2402 CG HIS A 264 120.568 65.644 -10.829 1.00 43.56 C ANISOU 2402 CG HIS A 264 5013 4788 6750 -764 -72 10 C ATOM 2403 ND1 HIS A 264 119.778 64.929 -9.955 1.00 44.20 N ANISOU 2403 ND1 HIS A 264 5067 4884 6845 -688 -133 -38 N ATOM 2404 CD2 HIS A 264 119.922 66.811 -11.054 1.00 47.53 C ANISOU 2404 CD2 HIS A 264 5653 5038 7368 -787 22 21 C ATOM 2405 CE1 HIS A 264 118.700 65.636 -9.665 1.00 47.90 C ANISOU 2405 CE1 HIS A 264 5622 5149 7430 -669 -70 -76 C ATOM 2406 NE2 HIS A 264 118.764 66.783 -10.318 1.00 42.56 N ANISOU 2406 NE2 HIS A 264 5048 4297 6828 -709 16 -43 N ATOM 2407 N THR A 265 123.970 63.412 -13.066 1.00 49.67 N ANISOU 2407 N THR A 265 5408 6249 7214 -640 -143 122 N ATOM 2408 CA THR A 265 125.207 63.348 -13.836 1.00 35.35 C ANISOU 2408 CA THR A 265 3467 4641 5323 -677 -66 129 C ATOM 2409 C THR A 265 124.920 62.979 -15.286 1.00 35.00 C ANISOU 2409 C THR A 265 3515 4571 5211 -522 -40 202 C ATOM 2410 O THR A 265 125.365 63.660 -16.223 1.00 44.69 O ANISOU 2410 O THR A 265 4785 5825 6371 -613 92 264 O ATOM 2411 CB THR A 265 126.168 62.337 -13.214 1.00 39.16 C ANISOU 2411 CB THR A 265 3719 5385 5774 -606 -149 64 C ATOM 2412 OG1 THR A 265 126.375 62.651 -11.831 1.00 57.89 O ANISOU 2412 OG1 THR A 265 6017 7816 8161 -747 -205 0 O ATOM 2413 CG2 THR A 265 127.501 62.379 -13.940 1.00 36.90 C ANISOU 2413 CG2 THR A 265 3246 5343 5430 -656 -43 47 C ATOM 2414 N LEU A 266 124.158 61.903 -15.489 1.00 45.41 N ANISOU 2414 N LEU A 266 4880 5841 6532 -307 -160 194 N ATOM 2415 CA LEU A 266 123.886 61.437 -16.842 1.00 50.10 C ANISOU 2415 CA LEU A 266 5560 6445 7033 -163 -159 220 C ATOM 2416 C LEU A 266 122.992 62.404 -17.603 1.00 42.07 C ANISOU 2416 C LEU A 266 4739 5259 5987 -195 -135 329 C ATOM 2417 O LEU A 266 123.134 62.541 -18.820 1.00 46.51 O ANISOU 2417 O LEU A 266 5381 5882 6409 -163 -79 388 O ATOM 2418 CB LEU A 266 123.269 60.040 -16.793 1.00 41.09 C ANISOU 2418 CB LEU A 266 4421 5268 5925 41 -299 153 C ATOM 2419 CG LEU A 266 124.279 58.973 -16.347 1.00 45.41 C ANISOU 2419 CG LEU A 266 4796 5973 6485 138 -316 77 C ATOM 2420 CD1 LEU A 266 123.635 57.622 -16.095 1.00 62.36 C ANISOU 2420 CD1 LEU A 266 6980 8008 8706 315 -444 27 C ATOM 2421 CD2 LEU A 266 125.385 58.834 -17.387 1.00 42.23 C ANISOU 2421 CD2 LEU A 266 4301 5778 5967 181 -195 37 C ATOM 2422 N ARG A 267 122.092 63.102 -16.910 1.00 35.60 N ANISOU 2422 N ARG A 267 4000 4238 5288 -245 -171 361 N ATOM 2423 CA ARG A 267 121.261 64.098 -17.571 1.00 38.81 C ANISOU 2423 CA ARG A 267 4583 4466 5697 -241 -157 484 C ATOM 2424 C ARG A 267 122.114 65.256 -18.072 1.00 47.21 C ANISOU 2424 C ARG A 267 5716 5522 6698 -413 17 588 C ATOM 2425 O ARG A 267 121.933 65.729 -19.201 1.00 37.50 O ANISOU 2425 O ARG A 267 4633 4259 5356 -379 53 730 O ATOM 2426 CB ARG A 267 120.178 64.589 -16.605 1.00 39.33 C ANISOU 2426 CB ARG A 267 4687 4317 5939 -239 -207 468 C ATOM 2427 CG ARG A 267 119.058 65.405 -17.243 1.00 50.35 C ANISOU 2427 CG ARG A 267 6235 5516 7379 -144 -243 591 C ATOM 2428 CD ARG A 267 118.052 65.883 -16.202 1.00 41.72 C ANISOU 2428 CD ARG A 267 5140 4226 6484 -129 -259 541 C ATOM 2429 NE ARG A 267 118.584 66.983 -15.403 1.00 56.95 N ANISOU 2429 NE ARG A 267 7114 6023 8500 -312 -106 512 N ATOM 2430 CZ ARG A 267 118.020 67.450 -14.295 1.00 62.98 C ANISOU 2430 CZ ARG A 267 7873 6642 9416 -348 -67 413 C ATOM 2431 NH1 ARG A 267 116.905 66.900 -13.832 1.00 43.35 N ANISOU 2431 NH1 ARG A 267 5318 4138 7016 -215 -155 353 N ATOM 2432 NH2 ARG A 267 118.577 68.466 -13.645 1.00 60.32 N ANISOU 2432 NH2 ARG A 267 7596 6182 9142 -537 76 354 N ATOM 2433 N THR A 268 123.074 65.704 -17.255 1.00 36.45 N ANISOU 2433 N THR A 268 4249 4206 5393 -616 126 523 N ATOM 2434 CA THR A 268 123.986 66.760 -17.687 1.00 38.74 C ANISOU 2434 CA THR A 268 4582 4494 5645 -836 316 603 C ATOM 2435 C THR A 268 124.777 66.326 -18.912 1.00 52.85 C ANISOU 2435 C THR A 268 6331 6512 7237 -811 401 659 C ATOM 2436 O THR A 268 124.824 67.045 -19.922 1.00 51.57 O ANISOU 2436 O THR A 268 6333 6292 6969 -866 516 822 O ATOM 2437 CB THR A 268 124.928 67.140 -16.545 1.00 39.22 C ANISOU 2437 CB THR A 268 4482 4625 5796 -1078 390 471 C ATOM 2438 OG1 THR A 268 124.163 67.553 -15.404 1.00 45.34 O ANISOU 2438 OG1 THR A 268 5313 5197 6717 -1103 328 394 O ATOM 2439 CG2 THR A 268 125.840 68.274 -16.970 1.00 43.13 C ANISOU 2439 CG2 THR A 268 5014 5093 6282 -1356 601 539 C ATOM 2440 N VAL A 269 125.376 65.130 -18.850 1.00 47.01 N ANISOU 2440 N VAL A 269 5392 6028 6440 -710 354 532 N ATOM 2441 CA VAL A 269 126.193 64.658 -19.968 1.00 53.85 C ANISOU 2441 CA VAL A 269 6198 7139 7124 -672 464 540 C ATOM 2442 C VAL A 269 125.349 64.493 -21.231 1.00 57.86 C ANISOU 2442 C VAL A 269 6925 7600 7461 -506 419 645 C ATOM 2443 O VAL A 269 125.781 64.845 -22.337 1.00 59.08 O ANISOU 2443 O VAL A 269 7166 7860 7423 -559 565 748 O ATOM 2444 CB VAL A 269 126.911 63.350 -19.595 1.00 58.62 C ANISOU 2444 CB VAL A 269 6549 7987 7739 -540 410 367 C ATOM 2445 CG1 VAL A 269 127.679 62.824 -20.797 1.00 45.64 C ANISOU 2445 CG1 VAL A 269 4844 6589 5910 -467 545 340 C ATOM 2446 CG2 VAL A 269 127.840 63.580 -18.413 1.00 51.81 C ANISOU 2446 CG2 VAL A 269 5449 7232 7004 -708 435 283 C ATOM 2447 N HIS A 270 124.132 63.965 -21.088 1.00 48.14 N ANISOU 2447 N HIS A 270 5780 6233 6279 -319 215 621 N ATOM 2448 CA HIS A 270 123.253 63.788 -22.238 1.00 41.95 C ANISOU 2448 CA HIS A 270 5178 5433 5327 -165 123 699 C ATOM 2449 C HIS A 270 122.879 65.126 -22.865 1.00 44.88 C ANISOU 2449 C HIS A 270 5772 5653 5627 -244 188 939 C ATOM 2450 O HIS A 270 122.831 65.253 -24.095 1.00 47.74 O ANISOU 2450 O HIS A 270 6283 6111 5744 -198 218 1059 O ATOM 2451 CB HIS A 270 122.004 63.021 -21.803 1.00 50.10 C ANISOU 2451 CB HIS A 270 6212 6348 6475 9 -110 611 C ATOM 2452 CG HIS A 270 121.033 62.754 -22.910 1.00 51.67 C ANISOU 2452 CG HIS A 270 6557 6564 6513 161 -251 653 C ATOM 2453 ND1 HIS A 270 121.245 61.790 -23.872 1.00 60.81 N ANISOU 2453 ND1 HIS A 270 7724 7920 7463 262 -274 542 N ATOM 2454 CD2 HIS A 270 119.835 63.315 -23.196 1.00 54.77 C ANISOU 2454 CD2 HIS A 270 7075 6816 6916 238 -391 776 C ATOM 2455 CE1 HIS A 270 120.220 61.771 -24.706 1.00 55.58 C ANISOU 2455 CE1 HIS A 270 7194 7256 6666 368 -435 589 C ATOM 2456 NE2 HIS A 270 119.351 62.688 -24.319 1.00 61.91 N ANISOU 2456 NE2 HIS A 270 8055 7864 7603 366 -518 744 N ATOM 2457 N LEU A 271 122.609 66.139 -22.037 1.00 61.91 N ANISOU 2457 N LEU A 271 7974 7566 7986 -357 214 1014 N ATOM 2458 CA LEU A 271 122.239 67.441 -22.581 1.00 44.13 C ANISOU 2458 CA LEU A 271 5957 5103 5708 -410 280 1259 C ATOM 2459 C LEU A 271 123.404 68.133 -23.275 1.00 64.36 C ANISOU 2459 C LEU A 271 8586 7750 8119 -626 535 1392 C ATOM 2460 O LEU A 271 123.199 68.787 -24.304 1.00 59.65 O ANISOU 2460 O LEU A 271 8217 7097 7349 -614 587 1629 O ATOM 2461 CB LEU A 271 121.685 68.345 -21.484 1.00 55.72 C ANISOU 2461 CB LEU A 271 7461 6253 7456 -470 271 1267 C ATOM 2462 CG LEU A 271 120.275 68.047 -20.996 1.00 63.16 C ANISOU 2462 CG LEU A 271 8395 7058 8546 -254 53 1215 C ATOM 2463 CD1 LEU A 271 120.005 68.894 -19.786 1.00 41.48 C ANISOU 2463 CD1 LEU A 271 5652 4042 6066 -348 109 1163 C ATOM 2464 CD2 LEU A 271 119.281 68.363 -22.101 1.00 43.59 C ANISOU 2464 CD2 LEU A 271 6098 4512 5952 -53 -74 1421 C ATOM 2465 N THR A 272 124.626 68.015 -22.744 1.00 71.34 N ANISOU 2465 N THR A 272 9269 8782 9055 -830 697 1257 N ATOM 2466 CA THR A 272 125.724 68.753 -23.367 1.00 75.56 C ANISOU 2466 CA THR A 272 9840 9396 9472 -1080 968 1381 C ATOM 2467 C THR A 272 126.089 68.195 -24.741 1.00 88.95 C ANISOU 2467 C THR A 272 11580 11381 10837 -999 1049 1445 C ATOM 2468 O THR A 272 126.578 68.940 -25.598 1.00114.89 O ANISOU 2468 O THR A 272 15014 14686 13952 -1158 1260 1647 O ATOM 2469 CB THR A 272 126.964 68.762 -22.472 1.00 65.45 C ANISOU 2469 CB THR A 272 8279 8254 8334 -1329 1110 1201 C ATOM 2470 OG1 THR A 272 127.452 67.427 -22.300 1.00 89.93 O ANISOU 2470 OG1 THR A 272 11108 11673 11388 -1189 1037 986 O ATOM 2471 CG2 THR A 272 126.656 69.378 -21.116 1.00 70.94 C ANISOU 2471 CG2 THR A 272 8954 8688 9311 -1443 1045 1115 C ATOM 2472 N THR A 273 125.864 66.903 -24.974 1.00 84.88 N ANISOU 2472 N THR A 273 10953 11080 10217 -767 902 1274 N ATOM 2473 CA THR A 273 126.272 66.258 -26.217 1.00 99.19 C ANISOU 2473 CA THR A 273 12790 13193 11706 -686 991 1261 C ATOM 2474 C THR A 273 125.146 66.133 -27.233 1.00110.09 C ANISOU 2474 C THR A 273 14433 14551 12847 -479 817 1388 C ATOM 2475 O THR A 273 125.376 65.582 -28.315 1.00108.75 O ANISOU 2475 O THR A 273 14317 14641 12363 -405 872 1359 O ATOM 2476 CB THR A 273 126.821 64.855 -25.941 1.00 94.65 C ANISOU 2476 CB THR A 273 11937 12870 11155 -554 957 961 C ATOM 2477 OG1 THR A 273 125.773 64.026 -25.428 1.00 82.33 O ANISOU 2477 OG1 THR A 273 10376 11187 9720 -330 672 834 O ATOM 2478 CG2 THR A 273 127.963 64.903 -24.941 1.00 93.22 C ANISOU 2478 CG2 THR A 273 11457 12772 11192 -725 1088 836 C ATOM 2479 N TRP A 274 123.945 66.610 -26.920 1.00116.52 N ANISOU 2479 N TRP A 274 15393 15087 13790 -378 606 1509 N ATOM 2480 CA TRP A 274 122.789 66.266 -27.735 1.00116.14 C ANISOU 2480 CA TRP A 274 15511 15066 13550 -147 368 1568 C ATOM 2481 C TRP A 274 122.920 66.876 -29.123 1.00122.79 C ANISOU 2481 C TRP A 274 16615 16029 14009 -173 473 1834 C ATOM 2482 O TRP A 274 123.232 68.061 -29.271 1.00121.32 O ANISOU 2482 O TRP A 274 16592 15686 13819 -331 645 2106 O ATOM 2483 CB TRP A 274 121.499 66.755 -27.076 1.00110.54 C ANISOU 2483 CB TRP A 274 14861 14049 13088 -30 137 1653 C ATOM 2484 CG TRP A 274 120.261 66.099 -27.629 1.00124.85 C ANISOU 2484 CG TRP A 274 16720 15932 14783 214 -162 1614 C ATOM 2485 CD1 TRP A 274 119.876 64.808 -27.429 1.00129.64 C ANISOU 2485 CD1 TRP A 274 17166 16664 15425 329 -328 1335 C ATOM 2486 CD2 TRP A 274 119.265 66.684 -28.484 1.00137.33 C ANISOU 2486 CD2 TRP A 274 18512 17472 16194 364 -339 1858 C ATOM 2487 NE1 TRP A 274 118.698 64.554 -28.086 1.00129.49 N ANISOU 2487 NE1 TRP A 274 17226 16696 15280 507 -594 1359 N ATOM 2488 CE2 TRP A 274 118.304 65.688 -28.744 1.00136.44 C ANISOU 2488 CE2 TRP A 274 18319 17500 16022 547 -621 1681 C ATOM 2489 CE3 TRP A 274 119.093 67.948 -29.053 1.00144.59 C ANISOU 2489 CE3 TRP A 274 19683 18244 17012 364 -294 2219 C ATOM 2490 CZ2 TRP A 274 117.186 65.917 -29.543 1.00134.37 C ANISOU 2490 CZ2 TRP A 274 18181 17283 15592 730 -880 1836 C ATOM 2491 CZ3 TRP A 274 117.978 68.176 -29.843 1.00141.39 C ANISOU 2491 CZ3 TRP A 274 19424 17861 16438 582 -553 2406 C ATOM 2492 CH2 TRP A 274 117.042 67.164 -30.082 1.00131.40 C ANISOU 2492 CH2 TRP A 274 18037 16786 15105 763 -853 2206 C ATOM 2493 N LYS A 275 122.699 66.052 -30.142 1.00139.86 N ANISOU 2493 N LYS A 275 18835 18466 15838 -32 381 1750 N ATOM 2494 CA LYS A 275 122.565 66.512 -31.515 1.00150.19 C ANISOU 2494 CA LYS A 275 20422 19928 16715 -8 409 2004 C ATOM 2495 C LYS A 275 121.180 66.131 -32.014 1.00156.58 C ANISOU 2495 C LYS A 275 21336 20769 17390 242 40 2008 C ATOM 2496 O LYS A 275 120.627 65.106 -31.602 1.00147.92 O ANISOU 2496 O LYS A 275 20067 19705 16432 367 -168 1717 O ATOM 2497 CB LYS A 275 123.646 65.911 -32.421 1.00140.07 C ANISOU 2497 CB LYS A 275 19122 19025 15075 -89 659 1879 C ATOM 2498 N VAL A 276 120.618 66.967 -32.890 1.00167.38 N ANISOU 2498 N VAL A 276 22980 22124 18494 309 -47 2351 N ATOM 2499 CA VAL A 276 119.245 66.756 -33.342 1.00169.66 C ANISOU 2499 CA VAL A 276 23341 22454 18669 552 -433 2389 C ATOM 2500 C VAL A 276 119.128 65.440 -34.100 1.00164.51 C ANISOU 2500 C VAL A 276 22635 22176 17695 634 -565 2073 C ATOM 2501 O VAL A 276 118.204 64.650 -33.872 1.00157.09 O ANISOU 2501 O VAL A 276 21558 21257 16871 771 -859 1842 O ATOM 2502 CB VAL A 276 118.772 67.946 -34.196 1.00175.01 C ANISOU 2502 CB VAL A 276 24337 23067 19090 627 -500 2860 C ATOM 2503 N GLY A 277 120.074 65.175 -34.999 1.00165.93 N ANISOU 2503 N GLY A 277 22918 22652 17477 536 -330 2036 N ATOM 2504 CA GLY A 277 119.988 64.002 -35.847 1.00166.71 C ANISOU 2504 CA GLY A 277 23015 23106 17220 613 -430 1728 C ATOM 2505 C GLY A 277 120.743 62.787 -35.347 1.00160.58 C ANISOU 2505 C GLY A 277 21994 22398 16621 569 -276 1282 C ATOM 2506 O GLY A 277 120.481 61.666 -35.794 1.00156.23 O ANISOU 2506 O GLY A 277 21409 22042 15908 655 -405 949 O ATOM 2507 N LEU A 278 121.675 62.988 -34.420 1.00166.45 N ANISOU 2507 N LEU A 278 22567 22976 17700 440 -11 1265 N ATOM 2508 CA LEU A 278 122.528 61.901 -33.957 1.00168.10 C ANISOU 2508 CA LEU A 278 22539 23259 18072 424 153 889 C ATOM 2509 C LEU A 278 121.798 61.007 -32.961 1.00162.98 C ANISOU 2509 C LEU A 278 21699 22405 17820 535 -101 625 C ATOM 2510 O LEU A 278 121.073 61.486 -32.083 1.00149.48 O ANISOU 2510 O LEU A 278 19938 20425 16432 544 -267 756 O ATOM 2511 CB LEU A 278 123.798 62.458 -33.314 1.00168.33 C ANISOU 2511 CB LEU A 278 22424 23227 18308 245 500 974 C ATOM 2512 N CYS A 279 121.990 59.695 -33.110 1.00161.75 N ANISOU 2512 N CYS A 279 21449 22370 17640 616 -110 250 N ATOM 2513 CA CYS A 279 121.567 58.717 -32.111 1.00158.65 C ANISOU 2513 CA CYS A 279 20871 21769 17640 692 -271 -9 C ATOM 2514 C CYS A 279 122.734 58.488 -31.153 1.00145.08 C ANISOU 2514 C CYS A 279 18930 19971 16221 648 -28 -91 C ATOM 2515 O CYS A 279 123.780 57.965 -31.553 1.00147.40 O ANISOU 2515 O CYS A 279 19161 20455 16391 666 205 -263 O ATOM 2516 CB CYS A 279 121.142 57.394 -32.754 1.00166.20 C ANISOU 2516 CB CYS A 279 21864 22842 18444 800 -414 -375 C ATOM 2517 SG CYS A 279 119.651 57.376 -33.806 1.00165.65 S ANISOU 2517 SG CYS A 279 21992 22908 18039 852 -785 -379 S ATOM 2518 N LYS A 280 122.564 58.888 -29.898 1.00127.51 N ANISOU 2518 N LYS A 280 16577 17493 14377 601 -82 23 N ATOM 2519 CA LYS A 280 123.494 58.537 -28.831 1.00 98.47 C ANISOU 2519 CA LYS A 280 12668 13740 11004 580 64 -74 C ATOM 2520 C LYS A 280 122.837 57.462 -27.970 1.00 76.66 C ANISOU 2520 C LYS A 280 9811 10776 8539 687 -141 -275 C ATOM 2521 O LYS A 280 122.497 57.683 -26.804 1.00 75.55 O ANISOU 2521 O LYS A 280 9580 10427 8700 650 -227 -194 O ATOM 2522 CB LYS A 280 123.871 59.771 -28.011 1.00 91.94 C ANISOU 2522 CB LYS A 280 11778 12798 10358 418 168 184 C ATOM 2523 N ASP A 281 122.672 56.277 -28.570 1.00 71.83 N ANISOU 2523 N ASP A 281 9240 10224 7828 809 -199 -547 N ATOM 2524 CA ASP A 281 121.809 55.244 -28.001 1.00 66.22 C ANISOU 2524 CA ASP A 281 8506 9300 7356 884 -412 -730 C ATOM 2525 C ASP A 281 122.225 54.866 -26.585 1.00 66.05 C ANISOU 2525 C ASP A 281 8304 9083 7710 901 -381 -730 C ATOM 2526 O ASP A 281 121.387 54.806 -25.677 1.00 70.50 O ANISOU 2526 O ASP A 281 8839 9433 8515 870 -541 -677 O ATOM 2527 CB ASP A 281 121.804 54.011 -28.907 1.00 92.64 C ANISOU 2527 CB ASP A 281 11932 12727 10540 993 -425 -1059 C ATOM 2528 CG ASP A 281 120.944 54.199 -30.144 1.00117.84 C ANISOU 2528 CG ASP A 281 15315 16083 13378 969 -574 -1092 C ATOM 2529 OD1 ASP A 281 119.943 54.945 -30.061 1.00123.94 O ANISOU 2529 OD1 ASP A 281 16132 16808 14151 907 -768 -893 O ATOM 2530 OD2 ASP A 281 121.261 53.602 -31.196 1.00124.36 O ANISOU 2530 OD2 ASP A 281 16241 17096 13915 1025 -502 -1323 O ATOM 2531 N ARG A 282 123.518 54.613 -26.371 1.00 47.14 N ANISOU 2531 N ARG A 282 5772 6784 5356 953 -178 -785 N ATOM 2532 CA ARG A 282 123.946 54.010 -25.111 1.00 46.53 C ANISOU 2532 CA ARG A 282 5529 6551 5600 1016 -183 -813 C ATOM 2533 C ARG A 282 123.818 54.998 -23.952 1.00 55.76 C ANISOU 2533 C ARG A 282 6614 7631 6942 878 -220 -572 C ATOM 2534 O ARG A 282 123.313 54.645 -22.873 1.00 61.37 O ANISOU 2534 O ARG A 282 7288 8142 7889 882 -345 -549 O ATOM 2535 CB ARG A 282 125.380 53.495 -25.251 1.00 46.48 C ANISOU 2535 CB ARG A 282 5362 6710 5586 1140 28 -938 C ATOM 2536 CG ARG A 282 125.558 52.516 -26.419 1.00 49.04 C ANISOU 2536 CG ARG A 282 5778 7121 5734 1291 103 -1219 C ATOM 2537 CD ARG A 282 126.942 51.866 -26.454 1.00 60.38 C ANISOU 2537 CD ARG A 282 7023 8693 7226 1469 315 -1373 C ATOM 2538 NE ARG A 282 127.204 51.197 -27.733 1.00 69.97 N ANISOU 2538 NE ARG A 282 8333 10047 8204 1590 450 -1650 N ATOM 2539 CZ ARG A 282 126.799 49.968 -28.041 1.00 75.90 C ANISOU 2539 CZ ARG A 282 9209 10619 9013 1745 381 -1927 C ATOM 2540 NH1 ARG A 282 127.089 49.442 -29.228 1.00 66.24 N ANISOU 2540 NH1 ARG A 282 8078 9547 7543 1841 526 -2207 N ATOM 2541 NH2 ARG A 282 126.087 49.270 -27.167 1.00 59.07 N ANISOU 2541 NH2 ARG A 282 7122 8146 7176 1785 180 -1932 N ATOM 2542 N LEU A 283 124.245 56.246 -24.164 1.00 56.89 N ANISOU 2542 N LEU A 283 6746 7910 6961 739 -101 -398 N ATOM 2543 CA LEU A 283 124.111 57.260 -23.121 1.00 46.99 C ANISOU 2543 CA LEU A 283 5439 6554 5862 591 -122 -205 C ATOM 2544 C LEU A 283 122.641 57.501 -22.802 1.00 42.25 C ANISOU 2544 C LEU A 283 4963 5739 5350 565 -321 -134 C ATOM 2545 O LEU A 283 122.254 57.621 -21.635 1.00 49.95 O ANISOU 2545 O LEU A 283 5881 6560 6536 520 -394 -84 O ATOM 2546 CB LEU A 283 124.759 58.575 -23.562 1.00 53.58 C ANISOU 2546 CB LEU A 283 6282 7527 6550 425 55 -40 C ATOM 2547 CG LEU A 283 125.259 59.573 -22.496 1.00 57.25 C ANISOU 2547 CG LEU A 283 6631 7949 7174 245 125 90 C ATOM 2548 CD1 LEU A 283 125.987 60.754 -23.147 1.00 81.12 C ANISOU 2548 CD1 LEU A 283 9682 11099 10043 60 338 230 C ATOM 2549 CD2 LEU A 283 124.233 60.049 -21.473 1.00 64.96 C ANISOU 2549 CD2 LEU A 283 7667 8678 8339 189 -28 174 C ATOM 2550 N HIS A 284 121.811 57.600 -23.844 1.00 39.41 N ANISOU 2550 N HIS A 284 4761 5397 4814 594 -407 -130 N ATOM 2551 CA HIS A 284 120.386 57.869 -23.663 1.00 51.83 C ANISOU 2551 CA HIS A 284 6413 6811 6470 586 -603 -67 C ATOM 2552 C HIS A 284 119.713 56.737 -22.893 1.00 38.90 C ANISOU 2552 C HIS A 284 4713 5014 5054 639 -740 -216 C ATOM 2553 O HIS A 284 118.844 56.973 -22.043 1.00 41.87 O ANISOU 2553 O HIS A 284 5057 5234 5618 595 -834 -155 O ATOM 2554 CB HIS A 284 119.746 58.083 -25.042 1.00 40.55 C ANISOU 2554 CB HIS A 284 5141 5497 4769 627 -693 -47 C ATOM 2555 CG HIS A 284 118.323 58.547 -25.008 1.00 51.59 C ANISOU 2555 CG HIS A 284 6586 6783 6231 638 -901 47 C ATOM 2556 ND1 HIS A 284 117.556 58.652 -26.148 1.00 50.00 N ANISOU 2556 ND1 HIS A 284 6501 6697 5800 696 -1054 64 N ATOM 2557 CD2 HIS A 284 117.522 58.917 -23.981 1.00 45.99 C ANISOU 2557 CD2 HIS A 284 5804 5886 5785 611 -983 117 C ATOM 2558 CE1 HIS A 284 116.348 59.078 -25.828 1.00 57.68 C ANISOU 2558 CE1 HIS A 284 7445 7557 6915 718 -1233 150 C ATOM 2559 NE2 HIS A 284 116.300 59.244 -24.518 1.00 62.61 N ANISOU 2559 NE2 HIS A 284 7954 7990 7844 667 -1176 175 N ATOM 2560 N LYS A 285 120.138 55.501 -23.155 1.00 38.01 N ANISOU 2560 N LYS A 285 4586 4924 4932 731 -726 -414 N ATOM 2561 CA LYS A 285 119.632 54.346 -22.419 1.00 48.46 C ANISOU 2561 CA LYS A 285 5877 6057 6480 770 -824 -541 C ATOM 2562 C LYS A 285 120.032 54.414 -20.948 1.00 35.49 C ANISOU 2562 C LYS A 285 4121 4308 5056 737 -776 -435 C ATOM 2563 O LYS A 285 119.226 54.126 -20.047 1.00 60.47 O ANISOU 2563 O LYS A 285 7270 7301 8406 693 -863 -412 O ATOM 2564 CB LYS A 285 120.169 53.076 -23.076 1.00 43.38 C ANISOU 2564 CB LYS A 285 5269 5431 5782 893 -787 -774 C ATOM 2565 CG LYS A 285 119.646 51.765 -22.540 1.00 62.13 C ANISOU 2565 CG LYS A 285 7662 7565 8380 932 -878 -920 C ATOM 2566 CD LYS A 285 120.250 50.622 -23.353 1.00 80.63 C ANISOU 2566 CD LYS A 285 10069 9909 10657 1071 -816 -1174 C ATOM 2567 CE LYS A 285 119.768 49.259 -22.892 1.00 85.47 C ANISOU 2567 CE LYS A 285 10739 10223 11512 1105 -888 -1326 C ATOM 2568 NZ LYS A 285 120.366 48.158 -23.708 1.00102.86 N ANISOU 2568 NZ LYS A 285 13024 12386 13671 1257 -812 -1605 N ATOM 2569 N ALA A 286 121.289 54.786 -20.689 1.00 37.81 N ANISOU 2569 N ALA A 286 4322 4729 5313 745 -634 -377 N ATOM 2570 CA ALA A 286 121.738 54.984 -19.314 1.00 44.20 C ANISOU 2570 CA ALA A 286 5017 5498 6280 699 -608 -275 C ATOM 2571 C ALA A 286 120.890 56.038 -18.611 1.00 39.75 C ANISOU 2571 C ALA A 286 4474 4848 5782 554 -651 -141 C ATOM 2572 O ALA A 286 120.499 55.876 -17.444 1.00 50.89 O ANISOU 2572 O ALA A 286 5852 6144 7339 514 -696 -101 O ATOM 2573 CB ALA A 286 123.214 55.388 -19.301 1.00 35.14 C ANISOU 2573 CB ALA A 286 3733 4558 5061 701 -461 -248 C ATOM 2574 N LEU A 287 120.599 57.131 -19.317 1.00 43.42 N ANISOU 2574 N LEU A 287 5004 5361 6132 485 -626 -64 N ATOM 2575 CA LEU A 287 119.774 58.196 -18.758 1.00 32.94 C ANISOU 2575 CA LEU A 287 3705 3925 4884 384 -652 51 C ATOM 2576 C LEU A 287 118.375 57.699 -18.440 1.00 52.83 C ANISOU 2576 C LEU A 287 6243 6294 7534 409 -792 11 C ATOM 2577 O LEU A 287 117.800 58.069 -17.413 1.00 53.56 O ANISOU 2577 O LEU A 287 6301 6283 7767 344 -797 55 O ATOM 2578 CB LEU A 287 119.714 59.385 -19.723 1.00 37.08 C ANISOU 2578 CB LEU A 287 4327 4497 5266 345 -605 164 C ATOM 2579 CG LEU A 287 118.746 60.510 -19.323 1.00 37.44 C ANISOU 2579 CG LEU A 287 4423 4390 5414 291 -638 281 C ATOM 2580 CD1 LEU A 287 119.088 61.115 -17.967 1.00 31.65 C ANISOU 2580 CD1 LEU A 287 3623 3577 4826 170 -549 302 C ATOM 2581 CD2 LEU A 287 118.692 61.591 -20.384 1.00 44.85 C ANISOU 2581 CD2 LEU A 287 5492 5344 6205 289 -604 429 C ATOM 2582 N VAL A 288 117.812 56.862 -19.314 1.00 43.70 N ANISOU 2582 N VAL A 288 5132 5141 6330 486 -895 -93 N ATOM 2583 CA VAL A 288 116.496 56.282 -19.055 1.00 44.37 C ANISOU 2583 CA VAL A 288 5201 5102 6556 479 -1026 -157 C ATOM 2584 C VAL A 288 116.516 55.458 -17.773 1.00 49.13 C ANISOU 2584 C VAL A 288 5749 5579 7338 442 -1000 -182 C ATOM 2585 O VAL A 288 115.622 55.570 -16.920 1.00 54.60 O ANISOU 2585 O VAL A 288 6396 6172 8176 371 -1019 -150 O ATOM 2586 CB VAL A 288 116.039 55.444 -20.261 1.00 35.01 C ANISOU 2586 CB VAL A 288 4071 3959 5270 539 -1145 -307 C ATOM 2587 CG1 VAL A 288 114.851 54.589 -19.887 1.00 33.98 C ANISOU 2587 CG1 VAL A 288 3895 3695 5320 491 -1262 -411 C ATOM 2588 CG2 VAL A 288 115.686 56.362 -21.424 1.00 34.99 C ANISOU 2588 CG2 VAL A 288 4131 4092 5071 571 -1212 -240 C ATOM 2589 N ILE A 289 117.543 54.618 -17.617 1.00 41.57 N ANISOU 2589 N ILE A 289 4795 4632 6368 501 -947 -228 N ATOM 2590 CA ILE A 289 117.622 53.758 -16.436 1.00 34.80 C ANISOU 2590 CA ILE A 289 3916 3649 5657 492 -935 -211 C ATOM 2591 C ILE A 289 117.719 54.597 -15.161 1.00 40.59 C ANISOU 2591 C ILE A 289 4592 4402 6428 399 -875 -80 C ATOM 2592 O ILE A 289 117.032 54.331 -14.162 1.00 49.26 O ANISOU 2592 O ILE A 289 5684 5396 7637 328 -879 -42 O ATOM 2593 CB ILE A 289 118.803 52.777 -16.577 1.00 43.64 C ANISOU 2593 CB ILE A 289 5043 4782 6757 626 -899 -267 C ATOM 2594 CG1 ILE A 289 118.571 51.837 -17.761 1.00 39.15 C ANISOU 2594 CG1 ILE A 289 4556 4154 6165 707 -946 -447 C ATOM 2595 CG2 ILE A 289 119.032 51.996 -15.291 1.00 32.98 C ANISOU 2595 CG2 ILE A 289 3685 3311 5536 644 -895 -188 C ATOM 2596 CD1 ILE A 289 119.771 50.993 -18.116 1.00 40.36 C ANISOU 2596 CD1 ILE A 289 4712 4329 6293 877 -883 -536 C ATOM 2597 N THR A 290 118.547 55.643 -15.178 1.00 36.39 N ANISOU 2597 N THR A 290 4022 4009 5795 375 -804 -22 N ATOM 2598 CA THR A 290 118.688 56.446 -13.966 1.00 38.95 C ANISOU 2598 CA THR A 290 4303 4355 6142 267 -747 58 C ATOM 2599 C THR A 290 117.492 57.362 -13.728 1.00 52.49 C ANISOU 2599 C THR A 290 6036 5983 7924 180 -739 77 C ATOM 2600 O THR A 290 117.220 57.715 -12.578 1.00 55.62 O ANISOU 2600 O THR A 290 6413 6352 8368 93 -694 103 O ATOM 2601 CB THR A 290 119.978 57.258 -14.016 1.00 40.26 C ANISOU 2601 CB THR A 290 4409 4684 6203 231 -668 86 C ATOM 2602 OG1 THR A 290 119.989 58.065 -15.199 1.00 41.88 O ANISOU 2602 OG1 THR A 290 4658 4926 6330 224 -631 90 O ATOM 2603 CG2 THR A 290 121.177 56.336 -14.006 1.00 31.83 C ANISOU 2603 CG2 THR A 290 3266 3728 5098 338 -673 66 C ATOM 2604 N LEU A 291 116.761 57.738 -14.779 1.00 39.54 N ANISOU 2604 N LEU A 291 4429 4314 6280 218 -786 62 N ATOM 2605 CA LEU A 291 115.494 58.439 -14.592 1.00 40.40 C ANISOU 2605 CA LEU A 291 4524 4335 6492 188 -800 75 C ATOM 2606 C LEU A 291 114.478 57.540 -13.904 1.00 51.32 C ANISOU 2606 C LEU A 291 5855 5634 8011 156 -836 26 C ATOM 2607 O LEU A 291 113.720 57.995 -13.037 1.00 60.22 O ANISOU 2607 O LEU A 291 6933 6710 9236 95 -780 32 O ATOM 2608 CB LEU A 291 114.961 58.934 -15.942 1.00 29.59 C ANISOU 2608 CB LEU A 291 3190 2983 5071 268 -882 91 C ATOM 2609 CG LEU A 291 113.598 59.627 -15.940 1.00 39.75 C ANISOU 2609 CG LEU A 291 4429 4195 6478 296 -932 111 C ATOM 2610 CD1 LEU A 291 113.606 60.850 -15.052 1.00 45.42 C ANISOU 2610 CD1 LEU A 291 5152 4831 7273 247 -805 165 C ATOM 2611 CD2 LEU A 291 113.208 60.016 -17.343 1.00 45.02 C ANISOU 2611 CD2 LEU A 291 5141 4917 7050 402 -1051 156 C ATOM 2612 N ALA A 292 114.459 56.256 -14.270 1.00 41.60 N ANISOU 2612 N ALA A 292 4638 4377 6792 186 -906 -33 N ATOM 2613 CA ALA A 292 113.624 55.302 -13.549 1.00 40.51 C ANISOU 2613 CA ALA A 292 4468 4132 6790 117 -912 -64 C ATOM 2614 C ALA A 292 114.044 55.197 -12.084 1.00 44.80 C ANISOU 2614 C ALA A 292 5023 4661 7337 45 -808 16 C ATOM 2615 O ALA A 292 113.193 55.152 -11.188 1.00 34.68 O ANISOU 2615 O ALA A 292 3703 3330 6143 -51 -748 30 O ATOM 2616 CB ALA A 292 113.687 53.937 -14.229 1.00 39.98 C ANISOU 2616 CB ALA A 292 4451 3994 6744 153 -993 -151 C ATOM 2617 N LEU A 293 115.352 55.150 -11.821 1.00 37.52 N ANISOU 2617 N LEU A 293 4141 3810 6304 89 -785 67 N ATOM 2618 CA LEU A 293 115.816 55.143 -10.432 1.00 43.25 C ANISOU 2618 CA LEU A 293 4875 4575 6985 27 -719 149 C ATOM 2619 C LEU A 293 115.380 56.399 -9.683 1.00 45.66 C ANISOU 2619 C LEU A 293 5145 4928 7275 -78 -628 145 C ATOM 2620 O LEU A 293 114.978 56.325 -8.517 1.00 51.37 O ANISOU 2620 O LEU A 293 5875 5650 7995 -169 -558 174 O ATOM 2621 CB LEU A 293 117.336 54.996 -10.365 1.00 50.99 C ANISOU 2621 CB LEU A 293 5854 5674 7848 105 -738 192 C ATOM 2622 CG LEU A 293 117.937 53.619 -10.603 1.00 71.68 C ANISOU 2622 CG LEU A 293 8512 8233 10491 235 -799 214 C ATOM 2623 CD1 LEU A 293 119.450 53.726 -10.611 1.00 76.09 C ANISOU 2623 CD1 LEU A 293 9004 8962 10944 332 -813 239 C ATOM 2624 CD2 LEU A 293 117.470 52.666 -9.514 1.00 63.72 C ANISOU 2624 CD2 LEU A 293 7573 7101 9537 197 -794 312 C ATOM 2625 N ALA A 294 115.467 57.563 -10.327 1.00 40.83 N ANISOU 2625 N ALA A 294 4516 4349 6649 -66 -614 108 N ATOM 2626 CA ALA A 294 115.057 58.807 -9.681 1.00 35.50 C ANISOU 2626 CA ALA A 294 3828 3668 5991 -147 -515 80 C ATOM 2627 C ALA A 294 113.562 58.815 -9.394 1.00 50.00 C ANISOU 2627 C ALA A 294 5613 5417 7969 -166 -475 41 C ATOM 2628 O ALA A 294 113.127 59.328 -8.357 1.00 47.27 O ANISOU 2628 O ALA A 294 5252 5072 7636 -246 -360 6 O ATOM 2629 CB ALA A 294 115.440 60.002 -10.554 1.00 28.09 C ANISOU 2629 CB ALA A 294 2911 2725 5036 -118 -504 74 C ATOM 2630 N ALA A 295 112.758 58.252 -10.299 1.00 48.25 N ANISOU 2630 N ALA A 295 5345 5140 7847 -101 -564 25 N ATOM 2631 CA ALA A 295 111.319 58.190 -10.058 1.00 37.12 C ANISOU 2631 CA ALA A 295 3830 3681 6593 -129 -533 -23 C ATOM 2632 C ALA A 295 110.970 57.199 -8.951 1.00 48.19 C ANISOU 2632 C ALA A 295 5224 5071 8014 -251 -453 -8 C ATOM 2633 O ALA A 295 110.006 57.420 -8.208 1.00 57.67 O ANISOU 2633 O ALA A 295 6339 6271 9301 -323 -338 -46 O ATOM 2634 CB ALA A 295 110.581 57.833 -11.348 1.00 35.05 C ANISOU 2634 CB ALA A 295 3498 3402 6419 -49 -679 -59 C ATOM 2635 N ALA A 296 111.739 56.112 -8.820 1.00 51.88 N ANISOU 2635 N ALA A 296 5783 5524 8405 -266 -497 56 N ATOM 2636 CA ALA A 296 111.532 55.115 -7.769 1.00 50.57 C ANISOU 2636 CA ALA A 296 5658 5319 8236 -375 -422 124 C ATOM 2637 C ALA A 296 111.709 55.674 -6.358 1.00 51.07 C ANISOU 2637 C ALA A 296 5754 5476 8173 -465 -281 163 C ATOM 2638 O ALA A 296 111.423 54.964 -5.384 1.00 49.55 O ANISOU 2638 O ALA A 296 5608 5275 7945 -570 -194 240 O ATOM 2639 CB ALA A 296 112.486 53.937 -7.986 1.00 39.04 C ANISOU 2639 CB ALA A 296 4313 3798 6722 -318 -513 203 C ATOM 2640 N ASN A 297 112.175 56.916 -6.221 1.00 44.74 N ANISOU 2640 N ASN A 297 4948 4761 7291 -441 -248 109 N ATOM 2641 CA ASN A 297 112.342 57.494 -4.910 1.00 45.23 C ANISOU 2641 CA ASN A 297 5049 4926 7213 -541 -118 97 C ATOM 2642 C ASN A 297 111.017 57.583 -4.158 1.00 52.53 C ANISOU 2642 C ASN A 297 5904 5840 8214 -640 53 42 C ATOM 2643 O ASN A 297 110.966 57.373 -2.961 1.00 56.91 O ANISOU 2643 O ASN A 297 6515 6478 8631 -753 172 77 O ATOM 2644 CB ASN A 297 113.002 58.858 -5.057 1.00 42.23 C ANISOU 2644 CB ASN A 297 4676 4593 6777 -519 -109 9 C ATOM 2645 CG ASN A 297 112.918 59.687 -3.809 1.00 53.44 C ANISOU 2645 CG ASN A 297 6126 6097 8084 -634 44 -81 C ATOM 2646 OD1 ASN A 297 112.081 60.568 -3.697 1.00 55.91 O ANISOU 2646 OD1 ASN A 297 6390 6350 8502 -637 168 -201 O ATOM 2647 ND2 ASN A 297 113.793 59.421 -2.871 1.00 48.24 N ANISOU 2647 ND2 ASN A 297 5542 5585 7203 -715 31 -35 N ATOM 2648 N ALA A 298 109.928 57.835 -4.895 1.00 50.57 N ANISOU 2648 N ALA A 298 5519 5513 8181 -592 62 -38 N ATOM 2649 CA ALA A 298 108.599 57.996 -4.318 1.00 56.77 C ANISOU 2649 CA ALA A 298 6174 6310 9085 -666 233 -116 C ATOM 2650 C ALA A 298 108.083 56.719 -3.666 1.00 65.79 C ANISOU 2650 C ALA A 298 7322 7453 10224 -816 313 -26 C ATOM 2651 O ALA A 298 107.189 56.790 -2.815 1.00 72.87 O ANISOU 2651 O ALA A 298 8139 8407 11143 -928 514 -71 O ATOM 2652 CB ALA A 298 107.617 58.462 -5.395 1.00 39.25 C ANISOU 2652 CB ALA A 298 3772 4031 7110 -550 171 -206 C ATOM 2653 N CYS A 299 108.601 55.553 -4.053 1.00 57.26 N ANISOU 2653 N CYS A 299 6338 6294 9125 -824 183 97 N ATOM 2654 CA CYS A 299 108.280 54.326 -3.342 1.00 62.74 C ANISOU 2654 CA CYS A 299 7099 6940 9800 -977 269 222 C ATOM 2655 C CYS A 299 109.421 53.846 -2.457 1.00 49.62 C ANISOU 2655 C CYS A 299 5652 5318 7881 -989 256 394 C ATOM 2656 O CYS A 299 109.216 52.930 -1.656 1.00 71.03 O ANISOU 2656 O CYS A 299 8464 7996 10529 -1115 351 542 O ATOM 2657 CB CYS A 299 107.878 53.213 -4.322 1.00 67.43 C ANISOU 2657 CB CYS A 299 7658 7367 10595 -993 152 233 C ATOM 2658 SG CYS A 299 109.191 52.593 -5.378 1.00 60.70 S ANISOU 2658 SG CYS A 299 6954 6404 9703 -822 -94 288 S ATOM 2659 N PHE A 300 110.609 54.440 -2.579 1.00 51.33 N ANISOU 2659 N PHE A 300 5936 5617 7949 -868 138 391 N ATOM 2660 CA PHE A 300 111.695 54.109 -1.660 1.00 41.76 C ANISOU 2660 CA PHE A 300 4883 4506 6477 -868 104 543 C ATOM 2661 C PHE A 300 111.591 54.844 -0.329 1.00 56.41 C ANISOU 2661 C PHE A 300 6774 6556 8103 -988 264 512 C ATOM 2662 O PHE A 300 112.023 54.309 0.699 1.00 51.04 O ANISOU 2662 O PHE A 300 6231 5974 7189 -1047 282 672 O ATOM 2663 CB PHE A 300 113.042 54.410 -2.311 1.00 52.46 C ANISOU 2663 CB PHE A 300 6253 5909 7770 -711 -86 535 C ATOM 2664 CG PHE A 300 113.398 53.463 -3.416 1.00 69.39 C ANISOU 2664 CG PHE A 300 8412 7892 10063 -582 -233 588 C ATOM 2665 CD1 PHE A 300 112.785 52.224 -3.508 1.00 61.33 C ANISOU 2665 CD1 PHE A 300 7449 6681 9172 -621 -217 680 C ATOM 2666 CD2 PHE A 300 114.331 53.814 -4.376 1.00 63.60 C ANISOU 2666 CD2 PHE A 300 7638 7188 9341 -440 -368 527 C ATOM 2667 CE1 PHE A 300 113.111 51.353 -4.528 1.00 69.16 C ANISOU 2667 CE1 PHE A 300 8472 7505 10302 -505 -341 685 C ATOM 2668 CE2 PHE A 300 114.657 52.941 -5.398 1.00 67.99 C ANISOU 2668 CE2 PHE A 300 8213 7609 10014 -316 -480 542 C ATOM 2669 CZ PHE A 300 114.043 51.711 -5.472 1.00 73.04 C ANISOU 2669 CZ PHE A 300 8922 8048 10782 -342 -471 608 C ATOM 2670 N ASN A 301 111.028 56.052 -0.322 1.00 53.72 N ANISOU 2670 N ASN A 301 6325 6270 7815 -1014 380 308 N ATOM 2671 CA ASN A 301 111.020 56.846 0.904 1.00 51.77 C ANISOU 2671 CA ASN A 301 6125 6208 7338 -1122 539 221 C ATOM 2672 C ASN A 301 110.231 56.249 2.075 1.00 54.05 C ANISOU 2672 C ASN A 301 6472 6576 7490 -1287 750 308 C ATOM 2673 O ASN A 301 110.560 56.600 3.222 1.00 48.11 O ANISOU 2673 O ASN A 301 5824 6021 6435 -1380 838 294 O ATOM 2674 CB ASN A 301 110.506 58.263 0.607 1.00 42.51 C ANISOU 2674 CB ASN A 301 4833 5017 6301 -1092 642 -32 C ATOM 2675 CG ASN A 301 111.508 59.097 -0.167 1.00 47.83 C ANISOU 2675 CG ASN A 301 5513 5663 7000 -985 481 -107 C ATOM 2676 OD1 ASN A 301 112.716 58.997 0.048 1.00 56.50 O ANISOU 2676 OD1 ASN A 301 6697 6865 7906 -990 351 -42 O ATOM 2677 ND2 ASN A 301 111.007 59.950 -1.050 1.00 41.27 N ANISOU 2677 ND2 ASN A 301 4579 4701 6401 -892 494 -236 N ATOM 2678 N PRO A 302 109.206 55.407 1.894 1.00 55.54 N ANISOU 2678 N PRO A 302 6599 6643 7862 -1355 849 384 N ATOM 2679 CA PRO A 302 108.558 54.811 3.077 1.00 60.81 C ANISOU 2679 CA PRO A 302 7344 7398 8363 -1544 1076 499 C ATOM 2680 C PRO A 302 109.485 54.004 3.980 1.00 60.28 C ANISOU 2680 C PRO A 302 7523 7421 7960 -1583 1003 765 C ATOM 2681 O PRO A 302 109.112 53.754 5.131 1.00 51.78 O ANISOU 2681 O PRO A 302 6551 6479 6642 -1742 1199 861 O ATOM 2682 CB PRO A 302 107.461 53.930 2.472 1.00 46.75 C ANISOU 2682 CB PRO A 302 5441 5430 6892 -1618 1145 546 C ATOM 2683 CG PRO A 302 107.100 54.625 1.220 1.00 44.48 C ANISOU 2683 CG PRO A 302 4939 5051 6911 -1480 1041 338 C ATOM 2684 CD PRO A 302 108.390 55.189 0.681 1.00 50.22 C ANISOU 2684 CD PRO A 302 5750 5784 7549 -1300 805 316 C ATOM 2685 N LEU A 303 110.662 53.581 3.511 1.00 59.06 N ANISOU 2685 N LEU A 303 7458 7211 7772 -1433 735 896 N ATOM 2686 CA LEU A 303 111.642 52.980 4.416 1.00 62.65 C ANISOU 2686 CA LEU A 303 8121 7796 7889 -1420 631 1144 C ATOM 2687 C LEU A 303 112.060 53.960 5.507 1.00 73.65 C ANISOU 2687 C LEU A 303 9561 9511 8910 -1493 685 1032 C ATOM 2688 O LEU A 303 112.174 53.592 6.683 1.00 94.71 O ANISOU 2688 O LEU A 303 12395 12359 11232 -1593 750 1202 O ATOM 2689 CB LEU A 303 112.864 52.504 3.634 1.00 74.73 C ANISOU 2689 CB LEU A 303 9674 9235 9486 -1207 332 1253 C ATOM 2690 CG LEU A 303 112.878 51.077 3.088 1.00 98.70 C ANISOU 2690 CG LEU A 303 12800 11985 12716 -1127 247 1485 C ATOM 2691 CD1 LEU A 303 111.836 50.880 2.012 1.00109.51 C ANISOU 2691 CD1 LEU A 303 14039 13101 14467 -1169 326 1345 C ATOM 2692 CD2 LEU A 303 114.267 50.751 2.547 1.00 97.30 C ANISOU 2692 CD2 LEU A 303 12641 11796 12534 -886 -31 1570 C ATOM 2693 N LEU A 304 112.320 55.212 5.128 1.00 59.26 N ANISOU 2693 N LEU A 304 7614 7763 7141 -1453 655 747 N ATOM 2694 CA LEU A 304 112.599 56.237 6.127 1.00 48.74 C ANISOU 2694 CA LEU A 304 6323 6706 5489 -1556 736 567 C ATOM 2695 C LEU A 304 111.429 56.379 7.090 1.00 51.36 C ANISOU 2695 C LEU A 304 6690 7131 5692 -1736 1063 497 C ATOM 2696 O LEU A 304 111.623 56.552 8.299 1.00 67.44 O ANISOU 2696 O LEU A 304 8862 9434 7327 -1857 1147 498 O ATOM 2697 CB LEU A 304 112.906 57.568 5.436 1.00 46.57 C ANISOU 2697 CB LEU A 304 5916 6402 5377 -1500 691 260 C ATOM 2698 CG LEU A 304 114.207 57.585 4.631 1.00 70.69 C ANISOU 2698 CG LEU A 304 8931 9439 8489 -1361 398 304 C ATOM 2699 CD1 LEU A 304 114.345 58.847 3.806 1.00 70.36 C ANISOU 2699 CD1 LEU A 304 8772 9304 8658 -1327 396 35 C ATOM 2700 CD2 LEU A 304 115.381 57.452 5.576 1.00 91.55 C ANISOU 2700 CD2 LEU A 304 11671 12375 10739 -1396 235 398 C ATOM 2701 N TYR A 305 110.206 56.267 6.569 1.00 54.66 N ANISOU 2701 N TYR A 305 6974 7361 6433 -1758 1251 435 N ATOM 2702 CA TYR A 305 109.022 56.364 7.413 1.00 61.01 C ANISOU 2702 CA TYR A 305 7760 8261 7159 -1928 1596 358 C ATOM 2703 C TYR A 305 108.944 55.167 8.347 1.00 67.03 C ANISOU 2703 C TYR A 305 8718 9113 7639 -2068 1677 686 C ATOM 2704 O TYR A 305 108.503 55.294 9.496 1.00 81.90 O ANISOU 2704 O TYR A 305 10691 11216 9211 -2233 1928 669 O ATOM 2705 CB TYR A 305 107.758 56.437 6.554 1.00 59.63 C ANISOU 2705 CB TYR A 305 7344 7882 7431 -1909 1745 230 C ATOM 2706 CG TYR A 305 107.732 57.534 5.508 1.00 67.50 C ANISOU 2706 CG TYR A 305 8159 8752 8736 -1741 1653 -35 C ATOM 2707 CD1 TYR A 305 108.621 58.602 5.543 1.00 56.98 C ANISOU 2707 CD1 TYR A 305 6882 7487 7281 -1668 1546 -209 C ATOM 2708 CD2 TYR A 305 106.829 57.475 4.460 1.00 67.48 C ANISOU 2708 CD2 TYR A 305 7936 8560 9145 -1665 1660 -95 C ATOM 2709 CE1 TYR A 305 108.593 59.579 4.564 1.00 60.14 C ANISOU 2709 CE1 TYR A 305 7150 7732 7969 -1522 1475 -407 C ATOM 2710 CE2 TYR A 305 106.791 58.443 3.488 1.00 53.10 C ANISOU 2710 CE2 TYR A 305 5971 6620 7583 -1495 1563 -288 C ATOM 2711 CZ TYR A 305 107.673 59.491 3.541 1.00 65.83 C ANISOU 2711 CZ TYR A 305 7672 8266 9075 -1421 1481 -428 C ATOM 2712 OH TYR A 305 107.624 60.453 2.561 1.00 69.96 O ANISOU 2712 OH TYR A 305 8084 8638 9860 -1258 1400 -583 O ATOM 2713 N TYR A 306 109.349 53.989 7.861 1.00 70.40 N ANISOU 2713 N TYR A 306 9226 9353 8168 -2002 1484 991 N ATOM 2714 CA TYR A 306 109.480 52.816 8.711 1.00 86.37 C ANISOU 2714 CA TYR A 306 11486 11411 9920 -2099 1514 1361 C ATOM 2715 C TYR A 306 110.380 53.168 9.883 1.00 96.16 C ANISOU 2715 C TYR A 306 12914 12995 10626 -2118 1442 1418 C ATOM 2716 O TYR A 306 109.922 53.306 11.022 1.00106.64 O ANISOU 2716 O TYR A 306 14352 14559 11609 -2297 1685 1425 O ATOM 2717 CB TYR A 306 110.124 51.635 7.980 1.00 87.63 C ANISOU 2717 CB TYR A 306 11734 11300 10261 -1955 1251 1654 C ATOM 2718 CG TYR A 306 109.905 50.293 8.652 1.00 95.75 C ANISOU 2718 CG TYR A 306 12998 12226 11155 -2066 1340 2055 C ATOM 2719 CD1 TYR A 306 109.148 49.308 8.036 1.00104.32 C ANISOU 2719 CD1 TYR A 306 14069 12971 12597 -2140 1427 2177 C ATOM 2720 CD2 TYR A 306 110.313 50.072 9.970 1.00110.30 C ANISOU 2720 CD2 TYR A 306 15085 14324 12499 -2137 1375 2296 C ATOM 2721 CE1 TYR A 306 108.923 48.090 8.656 1.00117.13 C ANISOU 2721 CE1 TYR A 306 15934 14450 14120 -2267 1535 2554 C ATOM 2722 CE2 TYR A 306 110.070 48.872 10.608 1.00113.47 C ANISOU 2722 CE2 TYR A 306 15735 14614 12766 -2245 1478 2700 C ATOM 2723 CZ TYR A 306 109.375 47.884 9.949 1.00117.57 C ANISOU 2723 CZ TYR A 306 16251 14740 13680 -2315 1569 2833 C ATOM 2724 OH TYR A 306 109.138 46.689 10.590 1.00127.65 O ANISOU 2724 OH TYR A 306 17802 15857 14840 -2443 1691 3250 O ATOM 2725 N PHE A 307 111.674 53.324 9.589 1.00 91.26 N ANISOU 2725 N PHE A 307 12315 12430 9927 -1941 1108 1443 N ATOM 2726 CA PHE A 307 112.679 53.286 10.647 1.00 87.35 C ANISOU 2726 CA PHE A 307 12007 12258 8925 -1938 951 1596 C ATOM 2727 C PHE A 307 112.590 54.517 11.542 1.00111.57 C ANISOU 2727 C PHE A 307 15071 15668 11654 -2087 1102 1274 C ATOM 2728 O PHE A 307 112.520 54.397 12.772 1.00143.15 O ANISOU 2728 O PHE A 307 19255 19951 15185 -2228 1216 1377 O ATOM 2729 CB PHE A 307 114.091 53.165 10.065 1.00 72.30 C ANISOU 2729 CB PHE A 307 10062 10353 7057 -1710 554 1674 C ATOM 2730 CG PHE A 307 114.353 51.893 9.288 1.00 82.87 C ANISOU 2730 CG PHE A 307 11438 11371 8676 -1531 390 1990 C ATOM 2731 CD1 PHE A 307 113.376 50.921 9.114 1.00108.53 C ANISOU 2731 CD1 PHE A 307 14769 14326 12142 -1603 577 2184 C ATOM 2732 CD2 PHE A 307 115.620 51.649 8.787 1.00104.57 C ANISOU 2732 CD2 PHE A 307 14142 14125 11466 -1299 56 2082 C ATOM 2733 CE1 PHE A 307 113.643 49.762 8.403 1.00119.48 C ANISOU 2733 CE1 PHE A 307 16215 15386 13797 -1447 432 2437 C ATOM 2734 CE2 PHE A 307 115.898 50.490 8.091 1.00118.81 C ANISOU 2734 CE2 PHE A 307 15990 15625 13529 -1112 -80 2340 C ATOM 2735 CZ PHE A 307 114.908 49.546 7.898 1.00119.59 C ANISOU 2735 CZ PHE A 307 16199 15392 13849 -1186 106 2512 C ATOM 2736 N ALA A 308 112.601 55.714 10.946 1.00 90.37 N ANISOU 2736 N ALA A 308 12200 12952 9186 -2061 1110 880 N ATOM 2737 CA ALA A 308 112.589 56.923 11.761 1.00 98.40 C ANISOU 2737 CA ALA A 308 13231 14248 9909 -2196 1249 533 C ATOM 2738 C ALA A 308 111.207 57.207 12.333 1.00128.39 C ANISOU 2738 C ALA A 308 17025 18070 13687 -2361 1677 372 C ATOM 2739 O ALA A 308 111.091 57.892 13.356 1.00142.18 O ANISOU 2739 O ALA A 308 18860 20100 15062 -2505 1853 155 O ATOM 2740 CB ALA A 308 113.079 58.117 10.943 1.00 74.56 C ANISOU 2740 CB ALA A 308 10042 11139 7150 -2119 1132 181 C ATOM 2741 N GLY A 309 110.156 56.686 11.703 1.00138.28 N ANISOU 2741 N GLY A 309 18162 19054 15326 -2349 1854 453 N ATOM 2742 CA GLY A 309 108.801 57.040 12.080 1.00156.41 C ANISOU 2742 CA GLY A 309 20369 21368 17694 -2483 2267 258 C ATOM 2743 C GLY A 309 108.319 56.391 13.360 1.00167.00 C ANISOU 2743 C GLY A 309 21899 22952 18601 -2691 2529 455 C ATOM 2744 O GLY A 309 108.045 57.078 14.350 1.00181.68 O ANISOU 2744 O GLY A 309 23823 25091 20114 -2822 2774 227 O ATOM 2745 N GLU A 310 108.207 55.065 13.355 1.00164.50 N ANISOU 2745 N GLU A 310 21691 22521 18290 -2729 2497 878 N ATOM 2746 CA GLU A 310 107.676 54.320 14.489 1.00169.49 C ANISOU 2746 CA GLU A 310 22522 23336 18539 -2944 2769 1137 C ATOM 2747 C GLU A 310 108.747 53.898 15.489 1.00173.61 C ANISOU 2747 C GLU A 310 23364 24141 18458 -2958 2563 1430 C ATOM 2748 O GLU A 310 108.502 52.987 16.288 1.00162.67 O ANISOU 2748 O GLU A 310 22202 22845 16761 -3098 2702 1792 O ATOM 2749 CB GLU A 310 106.928 53.080 13.995 1.00170.42 C ANISOU 2749 CB GLU A 310 22612 23146 18992 -3011 2870 1458 C ATOM 2750 N ASN A 311 109.917 54.541 15.477 1.00181.40 N ANISOU 2750 N ASN A 311 24372 25285 19266 -2825 2235 1293 N ATOM 2751 CA ASN A 311 111.028 54.055 16.289 1.00182.15 C ANISOU 2751 CA ASN A 311 24724 25653 18831 -2795 1956 1600 C ATOM 2752 C ASN A 311 110.778 54.255 17.780 1.00181.73 C ANISOU 2752 C ASN A 311 24893 26038 18116 -3014 2196 1593 C ATOM 2753 O ASN A 311 111.337 53.521 18.604 1.00192.11 O ANISOU 2753 O ASN A 311 26472 27574 18948 -3030 2054 1980 O ATOM 2754 CB ASN A 311 112.325 54.747 15.867 1.00172.95 C ANISOU 2754 CB ASN A 311 23466 24578 17669 -2623 1550 1412 C ATOM 2755 N PHE A 312 109.950 55.233 18.147 1.00156.55 N ANISOU 2755 N PHE A 312 21612 22986 14883 -3167 2559 1164 N ATOM 2756 CA PHE A 312 109.696 55.524 19.553 1.00150.76 C ANISOU 2756 CA PHE A 312 21087 22698 13497 -3383 2821 1084 C ATOM 2757 C PHE A 312 109.042 54.331 20.241 1.00148.22 C ANISOU 2757 C PHE A 312 20982 22411 12923 -3534 3068 1559 C ATOM 2758 O PHE A 312 107.986 53.855 19.809 1.00151.74 O ANISOU 2758 O PHE A 312 21309 22577 13770 -3602 3362 1640 O ATOM 2759 CB PHE A 312 108.814 56.765 19.679 1.00146.43 C ANISOU 2759 CB PHE A 312 20368 22214 13057 -3487 3213 504 C ATOM 2760 N LYS A 313 109.677 53.858 21.311 1.00146.96 N ANISOU 2760 N LYS A 313 21087 22515 12236 -3497 2884 1845 N ATOM 2761 CA LYS A 313 109.217 52.695 22.073 1.00143.98 C ANISOU 2761 CA LYS A 313 20924 22097 11684 -3527 3029 2320 C ATOM 2762 C LYS A 313 109.052 51.464 21.185 1.00136.54 C ANISOU 2762 C LYS A 313 19989 20703 11186 -3471 2967 2776 C ATOM 2763 O LYS A 313 109.813 50.501 21.295 1.00139.46 O ANISOU 2763 O LYS A 313 20568 20989 11432 -3324 2666 3247 O ATOM 2764 CB LYS A 313 107.901 53.003 22.793 1.00144.40 C ANISOU 2764 CB LYS A 313 20923 22245 11697 -3704 3550 2095 C TER 2765 LYS A 313 HETATM 2766 C4 KNZ A2001 114.194 62.656 -21.953 1.00 60.56 C HETATM 2767 C14 KNZ A2001 115.635 69.351 -16.910 1.00 41.50 C HETATM 2768 C5 KNZ A2001 114.490 61.525 -20.978 1.00 54.26 C HETATM 2769 C6 KNZ A2001 114.796 60.221 -21.696 1.00 63.15 C HETATM 2770 C11 KNZ A2001 116.995 66.347 -19.900 1.00 59.72 C HETATM 2771 C7 KNZ A2001 113.677 59.763 -22.613 1.00 60.44 C HETATM 2772 C8 KNZ A2001 114.935 64.752 -20.863 1.00 57.24 C HETATM 2773 C9 KNZ A2001 116.270 64.474 -21.176 1.00 41.16 C HETATM 2774 C10 KNZ A2001 117.282 65.273 -20.704 1.00 47.88 C HETATM 2775 C12 KNZ A2001 115.684 66.645 -19.569 1.00 51.19 C HETATM 2776 C13 KNZ A2001 116.239 68.509 -18.007 1.00 52.47 C HETATM 2777 N1 KNZ A2001 113.910 63.948 -21.303 1.00 53.69 N HETATM 2778 N2 KNZ A2001 115.379 67.752 -18.733 1.00 48.49 N HETATM 2779 C3 KNZ A2001 112.507 64.298 -21.065 1.00 56.16 C HETATM 2780 C1 KNZ A2001 112.365 65.759 -20.641 1.00 59.15 C HETATM 2781 C15 KNZ A2001 114.289 69.568 -16.689 1.00 44.68 C HETATM 2782 C16 KNZ A2001 113.807 70.348 -15.663 1.00 37.88 C HETATM 2783 C17 KNZ A2001 114.731 70.944 -14.808 1.00 53.00 C HETATM 2784 C18 KNZ A2001 112.974 71.820 -13.410 1.00 43.95 C HETATM 2785 C19 KNZ A2001 112.898 72.604 -12.127 1.00 56.68 C HETATM 2786 C2 KNZ A2001 110.965 66.038 -20.098 1.00 68.13 C HETATM 2787 C20 KNZ A2001 113.427 74.024 -12.230 1.00 57.00 C HETATM 2788 C21 KNZ A2001 113.591 74.705 -10.896 1.00 54.46 C HETATM 2789 C22 KNZ A2001 114.850 74.302 -8.856 1.00 79.03 C HETATM 2790 C23 KNZ A2001 115.109 73.236 -8.009 1.00 80.94 C HETATM 2791 C24 KNZ A2001 115.360 73.447 -6.666 1.00 79.33 C HETATM 2792 C25 KNZ A2001 115.386 74.718 -6.136 1.00 76.76 C HETATM 2793 C26 KNZ A2001 115.151 75.778 -6.973 1.00 88.94 C HETATM 2794 C27 KNZ A2001 114.891 75.586 -8.319 1.00 88.12 C HETATM 2795 C28 KNZ A2001 116.088 70.755 -14.996 1.00 42.87 C HETATM 2796 C29 KNZ A2001 116.529 69.966 -16.038 1.00 55.19 C HETATM 2797 C30 KNZ A2001 114.643 65.845 -20.045 1.00 52.04 C HETATM 2798 F1 KNZ A2001 115.169 77.043 -6.498 1.00106.05 F HETATM 2799 F2 KNZ A2001 114.671 76.655 -9.105 1.00 91.56 F HETATM 2800 F3 KNZ A2001 113.397 68.989 -17.525 1.00 57.81 F HETATM 2801 O1 KNZ A2001 110.012 65.920 -20.833 1.00 71.99 O HETATM 2802 O2 KNZ A2001 110.818 66.361 -18.945 1.00 76.82 O1- HETATM 2803 O3 KNZ A2001 113.901 59.720 -23.839 1.00 50.77 O HETATM 2804 O4 KNZ A2001 112.584 59.455 -22.096 1.00 70.84 O1- HETATM 2805 O5 KNZ A2001 117.454 68.505 -18.158 1.00 59.23 O HETATM 2806 O6 KNZ A2001 114.360 71.735 -13.755 1.00 63.22 O HETATM 2807 O7 KNZ A2001 113.355 66.159 -19.696 1.00 54.22 O HETATM 2808 O8 KNZ A2001 114.619 74.010 -10.177 1.00 60.88 O HETATM 2809 C18 OLC A2002 104.269 67.162 -6.399 1.00 52.43 C HETATM 2810 C10 OLC A2002 97.403 64.352 -10.912 1.00 71.36 C HETATM 2811 C9 OLC A2002 96.896 63.808 -11.997 1.00 66.68 C HETATM 2812 C17 OLC A2002 103.380 67.147 -7.638 1.00 78.56 C HETATM 2813 C11 OLC A2002 98.005 65.752 -10.947 1.00 66.18 C HETATM 2814 C8 OLC A2002 96.902 64.573 -13.317 1.00 74.44 C HETATM 2815 C24 OLC A2002 91.365 65.340 -23.573 1.00104.03 C HETATM 2816 C16 OLC A2002 102.633 68.476 -7.745 1.00 75.37 C HETATM 2817 C12 OLC A2002 98.929 65.899 -9.743 1.00 61.49 C HETATM 2818 C7 OLC A2002 96.515 63.615 -14.441 1.00 65.50 C HETATM 2819 C15 OLC A2002 101.671 68.411 -8.928 1.00 97.36 C HETATM 2820 C13 OLC A2002 99.844 67.094 -9.970 1.00 61.55 C HETATM 2821 C6 OLC A2002 95.855 64.407 -15.568 1.00 70.32 C HETATM 2822 C14 OLC A2002 100.814 67.156 -8.798 1.00 99.58 C HETATM 2823 C5 OLC A2002 95.065 63.471 -16.480 1.00 72.39 C HETATM 2824 C4 OLC A2002 93.762 64.155 -16.890 1.00 81.15 C HETATM 2825 C3 OLC A2002 92.899 63.220 -17.737 1.00 81.65 C HETATM 2826 C2 OLC A2002 92.754 63.798 -19.145 1.00101.84 C HETATM 2827 C21 OLC A2002 90.554 64.521 -21.388 1.00117.70 C HETATM 2828 C1 OLC A2002 91.591 63.113 -19.856 1.00111.02 C HETATM 2829 C22 OLC A2002 90.211 64.639 -22.867 1.00111.03 C HETATM 2830 O19 OLC A2002 90.888 62.368 -19.258 1.00126.92 O HETATM 2831 O25 OLC A2002 91.170 66.726 -23.520 1.00102.91 O HETATM 2832 O23 OLC A2002 90.038 63.354 -23.397 1.00103.77 O HETATM 2833 O20 OLC A2002 91.356 63.361 -21.182 1.00108.20 O HETATM 2834 C10 OLC A2003 105.085 44.553 -8.256 1.00 70.83 C HETATM 2835 C9 OLC A2003 104.086 45.298 -8.680 1.00 43.74 C HETATM 2836 C11 OLC A2003 105.383 43.206 -8.907 1.00 90.79 C HETATM 2837 C8 OLC A2003 103.215 44.823 -9.844 1.00 48.19 C HETATM 2838 C24 OLC A2003 106.011 46.615 -22.737 1.00 94.64 C HETATM 2839 C12 OLC A2003 106.837 42.839 -8.631 1.00 71.60 C HETATM 2840 C7 OLC A2003 103.514 45.667 -11.085 1.00 36.63 C HETATM 2841 C15 OLC A2003 108.177 42.232 -12.163 1.00 60.03 C HETATM 2842 C13 OLC A2003 107.640 43.135 -9.894 1.00 81.09 C HETATM 2843 C6 OLC A2003 103.811 44.742 -12.261 1.00 46.53 C HETATM 2844 C14 OLC A2003 107.229 42.134 -10.972 1.00 72.36 C HETATM 2845 C5 OLC A2003 103.669 45.515 -13.572 1.00 34.60 C HETATM 2846 C4 OLC A2003 104.009 44.600 -14.748 1.00 37.51 C HETATM 2847 C3 OLC A2003 103.992 45.406 -16.049 1.00 63.38 C HETATM 2848 C2 OLC A2003 104.573 44.550 -17.172 1.00 57.35 C HETATM 2849 C21 OLC A2003 105.078 45.442 -20.749 1.00 76.99 C HETATM 2850 C1 OLC A2003 104.767 45.380 -18.436 1.00 64.88 C HETATM 2851 C22 OLC A2003 106.290 45.559 -21.672 1.00 87.93 C HETATM 2852 O19 OLC A2003 104.331 46.481 -18.500 1.00 75.98 O HETATM 2853 O25 OLC A2003 106.287 46.081 -23.999 1.00100.50 O HETATM 2854 O23 OLC A2003 107.412 45.933 -20.926 1.00100.00 O HETATM 2855 O20 OLC A2003 105.452 44.854 -19.504 1.00 66.48 O HETATM 2856 C10 OLC A2004 129.854 58.718 -16.361 1.00 55.65 C HETATM 2857 C9 OLC A2004 129.950 58.628 -17.674 1.00 53.28 C HETATM 2858 C11 OLC A2004 129.847 60.039 -15.601 1.00 68.65 C HETATM 2859 C8 OLC A2004 130.063 59.841 -18.597 1.00 56.56 C HETATM 2860 C24 OLC A2004 127.536 58.714 -31.779 1.00118.70 C HETATM 2861 C12 OLC A2004 129.821 59.726 -14.105 1.00 65.14 C HETATM 2862 C7 OLC A2004 129.266 59.533 -19.869 1.00 60.16 C HETATM 2863 C13 OLC A2004 130.796 60.644 -13.372 1.00 62.51 C HETATM 2864 C6 OLC A2004 129.958 60.035 -21.141 1.00 58.21 C HETATM 2865 C14 OLC A2004 130.230 61.038 -12.008 1.00 70.04 C HETATM 2866 C5 OLC A2004 129.321 59.351 -22.355 1.00 63.59 C HETATM 2867 C4 OLC A2004 129.482 60.170 -23.638 1.00 57.51 C HETATM 2868 C3 OLC A2004 128.789 59.418 -24.781 1.00 64.29 C HETATM 2869 C2 OLC A2004 128.836 60.212 -26.090 1.00 77.12 C HETATM 2870 C21 OLC A2004 128.224 59.627 -29.555 1.00 99.87 C HETATM 2871 C1 OLC A2004 128.357 59.313 -27.232 1.00102.09 C HETATM 2872 C22 OLC A2004 127.858 58.360 -30.331 1.00112.17 C HETATM 2873 O19 OLC A2004 127.396 58.636 -27.080 1.00110.03 O HETATM 2874 O25 OLC A2004 126.673 57.745 -32.303 1.00108.54 O HETATM 2875 O23 OLC A2004 128.926 57.454 -30.294 1.00106.95 O HETATM 2876 O20 OLC A2004 129.028 59.271 -28.431 1.00101.96 O HETATM 2877 C24 OLC A2005 115.007 45.540 -23.794 1.00107.05 C HETATM 2878 C7 OLC A2005 113.059 45.835 -11.838 1.00 85.88 C HETATM 2879 C6 OLC A2005 112.690 45.158 -13.156 1.00 79.65 C HETATM 2880 C5 OLC A2005 113.487 45.782 -14.300 1.00 74.29 C HETATM 2881 C4 OLC A2005 112.783 45.474 -15.620 1.00 74.30 C HETATM 2882 C3 OLC A2005 113.802 45.423 -16.756 1.00 80.23 C HETATM 2883 C2 OLC A2005 113.125 44.850 -17.998 1.00 90.42 C HETATM 2884 C21 OLC A2005 113.941 45.736 -21.547 1.00105.43 C HETATM 2885 C1 OLC A2005 113.875 45.298 -19.248 1.00108.35 C HETATM 2886 C22 OLC A2005 114.671 44.798 -22.503 1.00109.63 C HETATM 2887 O19 OLC A2005 114.869 45.939 -19.150 1.00133.59 O HETATM 2888 O25 OLC A2005 114.100 45.170 -24.796 1.00104.58 O HETATM 2889 O23 OLC A2005 115.848 44.338 -21.898 1.00117.02 O HETATM 2890 O20 OLC A2005 113.396 44.958 -20.486 1.00101.49 O HETATM 2891 C10 OLC A2006 97.176 63.577 -2.310 1.00 99.69 C HETATM 2892 C9 OLC A2006 96.824 64.229 -1.219 1.00106.13 C HETATM 2893 C17 OLC A2006 94.724 62.039 -9.855 1.00 87.16 C HETATM 2894 C11 OLC A2006 96.548 62.227 -2.646 1.00 89.24 C HETATM 2895 C8 OLC A2006 95.778 63.649 -0.270 1.00 98.23 C HETATM 2896 C16 OLC A2006 94.455 61.588 -8.419 1.00 91.38 C HETATM 2897 C12 OLC A2006 96.823 61.906 -4.114 1.00 76.30 C HETATM 2898 C7 OLC A2006 96.278 63.822 1.164 1.00 93.50 C HETATM 2899 C15 OLC A2006 95.304 62.403 -7.441 1.00 70.13 C HETATM 2900 C13 OLC A2006 95.777 62.595 -4.992 1.00 68.39 C HETATM 2901 C6 OLC A2006 95.121 64.274 2.053 1.00 86.59 C HETATM 2902 C14 OLC A2006 95.391 61.640 -6.120 1.00 72.09 C HETATM 2903 C5 OLC A2006 95.665 65.181 3.154 1.00 77.92 C HETATM 2904 C10 OLC A2007 129.368 65.890 -15.196 1.00 68.77 C HETATM 2905 C9 OLC A2007 129.946 65.967 -16.377 1.00 78.11 C HETATM 2906 C11 OLC A2007 128.632 67.097 -14.622 1.00 71.14 C HETATM 2907 C8 OLC A2007 129.882 67.262 -17.179 1.00 87.58 C HETATM 2908 C12 OLC A2007 127.711 66.624 -13.500 1.00 75.66 C HETATM 2909 C7 OLC A2007 130.704 67.107 -18.457 1.00 98.52 C HETATM 2910 C13 OLC A2007 128.514 66.415 -12.218 1.00 81.87 C HETATM 2911 C6 OLC A2007 129.876 67.609 -19.637 1.00 87.90 C HETATM 2912 C5 OLC A2007 130.695 67.523 -20.922 1.00 89.00 C HETATM 2913 C16 OLC A2008 120.548 74.736 4.161 1.00 76.69 C HETATM 2914 C12 OLC A2008 121.772 76.579 8.009 1.00 85.18 C HETATM 2915 C15 OLC A2008 121.744 75.678 4.271 1.00 80.46 C HETATM 2916 C13 OLC A2008 121.868 75.712 6.755 1.00 85.15 C HETATM 2917 C14 OLC A2008 121.583 76.553 5.512 1.00 92.03 C HETATM 2918 C18 OLC A2009 116.445 49.294 -12.821 1.00 56.78 C HETATM 2919 C10 OLC A2009 110.325 48.911 -5.907 1.00 93.78 C HETATM 2920 C9 OLC A2009 110.311 48.621 -4.610 1.00101.66 C HETATM 2921 C17 OLC A2009 115.369 50.373 -12.710 1.00 63.32 C HETATM 2922 C11 OLC A2009 111.609 48.950 -6.744 1.00 74.15 C HETATM 2923 C8 OLC A2009 111.580 48.291 -3.821 1.00100.53 C HETATM 2924 C16 OLC A2009 114.962 50.551 -11.246 1.00 62.77 C HETATM 2925 C12 OLC A2009 111.409 49.937 -7.900 1.00 69.78 C HETATM 2926 C7 OLC A2009 111.547 48.963 -2.443 1.00 96.58 C HETATM 2927 C15 OLC A2009 113.457 50.323 -11.086 1.00 52.30 C HETATM 2928 C13 OLC A2009 112.115 49.468 -9.171 1.00 64.36 C HETATM 2929 C6 OLC A2009 110.170 48.821 -1.789 1.00102.71 C HETATM 2930 C14 OLC A2009 113.065 50.573 -9.631 1.00 48.61 C HETATM 2931 C5 OLC A2009 109.980 49.958 -0.782 1.00 90.09 C HETATM 2932 C4 OLC A2009 108.846 49.639 0.193 1.00 66.35 C HETATM 2933 C18 OLC A2010 129.495 62.557 -8.724 1.00 70.26 C HETATM 2934 C17 OLC A2010 130.512 62.323 -7.605 1.00 72.48 C HETATM 2935 C16 OLC A2010 129.783 62.085 -6.284 1.00 66.92 C HETATM 2936 C15 OLC A2010 130.791 62.107 -5.137 1.00 67.35 C HETATM 2937 C10 OLC A2011 107.399 44.609 -1.395 1.00 90.05 C HETATM 2938 C9 OLC A2011 107.033 45.323 -0.341 1.00 91.71 C HETATM 2939 C11 OLC A2011 107.256 45.126 -2.825 1.00 92.94 C HETATM 2940 C8 OLC A2011 106.432 46.725 -0.451 1.00 93.75 C HETATM 2941 C24 OLC A2011 104.543 55.333 9.273 1.00119.42 C HETATM 2942 C12 OLC A2011 107.919 44.137 -3.788 1.00 97.26 C HETATM 2943 C7 OLC A2011 106.204 47.258 0.969 1.00 90.50 C HETATM 2944 C13 OLC A2011 108.979 44.855 -4.625 1.00101.49 C HETATM 2945 C6 OLC A2011 105.450 48.589 0.946 1.00 81.39 C HETATM 2946 C14 OLC A2011 108.994 44.298 -6.049 1.00 90.02 C HETATM 2947 C5 OLC A2011 104.791 48.818 2.308 1.00 99.28 C HETATM 2948 C4 OLC A2011 105.612 49.780 3.173 1.00111.34 C HETATM 2949 C3 OLC A2011 104.678 50.521 4.133 1.00102.23 C HETATM 2950 C2 OLC A2011 105.203 50.444 5.568 1.00106.36 C HETATM 2951 C21 OLC A2011 104.595 53.425 7.646 1.00124.68 C HETATM 2952 C1 OLC A2011 105.435 51.858 6.094 1.00123.90 C HETATM 2953 C22 OLC A2011 105.404 54.222 8.669 1.00124.30 C HETATM 2954 O19 OLC A2011 105.815 52.706 5.349 1.00125.98 O HETATM 2955 O25 OLC A2011 105.125 55.829 10.452 1.00112.95 O HETATM 2956 O23 OLC A2011 105.864 53.365 9.678 1.00130.92 O HETATM 2957 O20 OLC A2011 105.213 52.157 7.418 1.00131.81 O HETATM 2958 C1 OLA A2012 93.642 54.045 -20.683 1.00 93.06 C HETATM 2959 C2 OLA A2012 93.485 53.802 -19.201 1.00 96.67 C HETATM 2960 C3 OLA A2012 94.358 54.781 -18.425 1.00 93.21 C HETATM 2961 C4 OLA A2012 94.066 54.698 -16.931 1.00100.36 C HETATM 2962 C5 OLA A2012 94.529 55.965 -16.220 1.00 95.17 C HETATM 2963 C6 OLA A2012 93.739 56.218 -14.938 1.00100.87 C HETATM 2964 C7 OLA A2012 94.104 55.208 -13.856 1.00105.22 C HETATM 2965 C8 OLA A2012 93.916 55.762 -12.445 1.00104.15 C HETATM 2966 C9 OLA A2012 94.647 57.078 -12.307 1.00 90.73 C HETATM 2967 C10 OLA A2012 94.843 57.642 -11.115 1.00 87.88 C HETATM 2968 C11 OLA A2012 94.374 56.985 -9.836 1.00 85.54 C HETATM 2969 C12 OLA A2012 95.259 57.445 -8.680 1.00 90.38 C HETATM 2970 C13 OLA A2012 95.069 56.571 -7.443 1.00 91.07 C HETATM 2971 C14 OLA A2012 95.663 57.231 -6.205 1.00 88.79 C HETATM 2972 C1 OLA A2013 90.369 59.928 -24.322 1.00122.65 C HETATM 2973 O1 OLA A2013 90.573 59.213 -25.330 1.00112.11 O HETATM 2974 O2 OLA A2013 90.597 61.158 -24.304 1.00125.78 O HETATM 2975 C2 OLA A2013 89.824 59.284 -23.067 1.00115.89 C HETATM 2976 C3 OLA A2013 90.962 58.680 -22.251 1.00106.08 C HETATM 2977 C4 OLA A2013 90.452 58.079 -20.948 1.00 94.46 C HETATM 2978 C5 OLA A2013 90.255 59.157 -19.888 1.00 91.52 C HETATM 2979 C6 OLA A2013 91.225 58.942 -18.733 1.00 94.87 C HETATM 2980 C7 OLA A2013 90.608 59.318 -17.390 1.00 96.74 C HETATM 2981 C1 OLA A2014 119.501 45.967 -21.358 1.00 84.62 C HETATM 2982 O1 OLA A2014 119.123 45.397 -22.409 1.00 85.84 O HETATM 2983 O2 OLA A2014 120.558 46.634 -21.284 1.00 97.38 O HETATM 2984 C2 OLA A2014 118.655 45.840 -20.118 1.00 79.13 C HETATM 2985 C3 OLA A2014 119.156 46.782 -19.027 1.00 67.77 C HETATM 2986 C4 OLA A2014 118.728 46.294 -17.646 1.00 67.54 C HETATM 2987 C5 OLA A2014 118.512 47.467 -16.694 1.00 71.99 C HETATM 2988 O HOH A2101 125.898 56.947 -26.376 1.00 84.08 O HETATM 2989 O HOH A2102 110.377 61.453 -5.138 1.00 92.95 O HETATM 2990 O HOH A2103 107.380 59.242 0.386 1.00 62.68 O HETATM 2991 O HOH A2104 114.107 64.035 -16.975 1.00 64.86 O HETATM 2992 O HOH A2105 104.833 62.237 -13.965 1.00 48.85 O HETATM 2993 O HOH A2106 109.259 58.637 -18.952 1.00 53.44 O HETATM 2994 O HOH A2107 116.106 61.218 9.472 1.00 70.54 O HETATM 2995 O HOH A2108 110.071 59.620 -23.577 1.00 38.75 O HETATM 2996 O HOH A2109 98.641 58.047 -23.993 1.00 54.35 O HETATM 2997 O HOH A2110 110.462 77.372 -14.529 1.00 60.22 O HETATM 2998 O HOH A2111 108.071 64.869 -18.873 1.00 65.36 O HETATM 2999 O HOH A2112 113.767 62.000 -25.603 1.00 57.00 O HETATM 3000 O HOH A2113 110.954 60.887 -20.191 1.00 49.48 O HETATM 3001 O HOH A2114 96.614 63.860 -26.552 1.00 65.67 O HETATM 3002 O HOH A2115 94.700 67.641 -20.946 1.00 42.55 O HETATM 3003 O HOH A2116 109.595 62.784 -9.062 1.00 56.03 O HETATM 3004 O HOH A2117 107.397 65.973 -26.110 1.00 76.83 O CONECT 6 2517 CONECT 654 1183 CONECT 1183 654 CONECT 2517 6 CONECT 2766 2768 2777 CONECT 2767 2776 2781 2796 CONECT 2768 2766 2769 CONECT 2769 2768 2771 CONECT 2770 2774 2775 CONECT 2771 2769 2803 2804 CONECT 2772 2773 2777 2797 CONECT 2773 2772 2774 CONECT 2774 2770 2773 CONECT 2775 2770 2778 2797 CONECT 2776 2767 2778 2805 CONECT 2777 2766 2772 2779 CONECT 2778 2775 2776 CONECT 2779 2777 2780 CONECT 2780 2779 2786 2807 CONECT 2781 2767 2782 2800 CONECT 2782 2781 2783 CONECT 2783 2782 2795 2806 CONECT 2784 2785 2806 CONECT 2785 2784 2787 CONECT 2786 2780 2801 2802 CONECT 2787 2785 2788 CONECT 2788 2787 2808 CONECT 2789 2790 2794 2808 CONECT 2790 2789 2791 CONECT 2791 2790 2792 CONECT 2792 2791 2793 CONECT 2793 2792 2794 2798 CONECT 2794 2789 2793 2799 CONECT 2795 2783 2796 CONECT 2796 2767 2795 CONECT 2797 2772 2775 2807 CONECT 2798 2793 CONECT 2799 2794 CONECT 2800 2781 CONECT 2801 2786 CONECT 2802 2786 CONECT 2803 2771 CONECT 2804 2771 CONECT 2805 2776 CONECT 2806 2783 2784 CONECT 2807 2780 2797 CONECT 2808 2788 2789 CONECT 2809 2812 CONECT 2810 2811 2813 CONECT 2811 2810 2814 CONECT 2812 2809 2816 CONECT 2813 2810 2817 CONECT 2814 2811 2818 CONECT 2815 2829 2831 CONECT 2816 2812 2819 CONECT 2817 2813 2820 CONECT 2818 2814 2821 CONECT 2819 2816 2822 CONECT 2820 2817 2822 CONECT 2821 2818 2823 CONECT 2822 2819 2820 CONECT 2823 2821 2824 CONECT 2824 2823 2825 CONECT 2825 2824 2826 CONECT 2826 2825 2828 CONECT 2827 2829 2833 CONECT 2828 2826 2830 2833 CONECT 2829 2815 2827 2832 CONECT 2830 2828 CONECT 2831 2815 CONECT 2832 2829 CONECT 2833 2827 2828 CONECT 2834 2835 2836 CONECT 2835 2834 2837 CONECT 2836 2834 2839 CONECT 2837 2835 2840 CONECT 2838 2851 2853 CONECT 2839 2836 2842 CONECT 2840 2837 2843 CONECT 2841 2844 CONECT 2842 2839 2844 CONECT 2843 2840 2845 CONECT 2844 2841 2842 CONECT 2845 2843 2846 CONECT 2846 2845 2847 CONECT 2847 2846 2848 CONECT 2848 2847 2850 CONECT 2849 2851 2855 CONECT 2850 2848 2852 2855 CONECT 2851 2838 2849 2854 CONECT 2852 2850 CONECT 2853 2838 CONECT 2854 2851 CONECT 2855 2849 2850 CONECT 2856 2857 2858 CONECT 2857 2856 2859 CONECT 2858 2856 2861 CONECT 2859 2857 2862 CONECT 2860 2872 2874 CONECT 2861 2858 2863 CONECT 2862 2859 2864 CONECT 2863 2861 2865 CONECT 2864 2862 2866 CONECT 2865 2863 CONECT 2866 2864 2867 CONECT 2867 2866 2868 CONECT 2868 2867 2869 CONECT 2869 2868 2871 CONECT 2870 2872 2876 CONECT 2871 2869 2873 2876 CONECT 2872 2860 2870 2875 CONECT 2873 2871 CONECT 2874 2860 CONECT 2875 2872 CONECT 2876 2870 2871 CONECT 2877 2886 2888 CONECT 2878 2879 CONECT 2879 2878 2880 CONECT 2880 2879 2881 CONECT 2881 2880 2882 CONECT 2882 2881 2883 CONECT 2883 2882 2885 CONECT 2884 2886 2890 CONECT 2885 2883 2887 2890 CONECT 2886 2877 2884 2889 CONECT 2887 2885 CONECT 2888 2877 CONECT 2889 2886 CONECT 2890 2884 2885 CONECT 2891 2892 2894 CONECT 2892 2891 2895 CONECT 2893 2896 CONECT 2894 2891 2897 CONECT 2895 2892 2898 CONECT 2896 2893 2899 CONECT 2897 2894 2900 CONECT 2898 2895 2901 CONECT 2899 2896 2902 CONECT 2900 2897 2902 CONECT 2901 2898 2903 CONECT 2902 2899 2900 CONECT 2903 2901 CONECT 2904 2905 2906 CONECT 2905 2904 2907 CONECT 2906 2904 2908 CONECT 2907 2905 2909 CONECT 2908 2906 2910 CONECT 2909 2907 2911 CONECT 2910 2908 CONECT 2911 2909 2912 CONECT 2912 2911 CONECT 2913 2915 CONECT 2914 2916 CONECT 2915 2913 2917 CONECT 2916 2914 2917 CONECT 2917 2915 2916 CONECT 2918 2921 CONECT 2919 2920 2922 CONECT 2920 2919 2923 CONECT 2921 2918 2924 CONECT 2922 2919 2925 CONECT 2923 2920 2926 CONECT 2924 2921 2927 CONECT 2925 2922 2928 CONECT 2926 2923 2929 CONECT 2927 2924 2930 CONECT 2928 2925 2930 CONECT 2929 2926 2931 CONECT 2930 2927 2928 CONECT 2931 2929 2932 CONECT 2932 2931 CONECT 2933 2934 CONECT 2934 2933 2935 CONECT 2935 2934 2936 CONECT 2936 2935 CONECT 2937 2938 2939 CONECT 2938 2937 2940 CONECT 2939 2937 2942 CONECT 2940 2938 2943 CONECT 2941 2953 2955 CONECT 2942 2939 2944 CONECT 2943 2940 2945 CONECT 2944 2942 2946 CONECT 2945 2943 2947 CONECT 2946 2944 CONECT 2947 2945 2948 CONECT 2948 2947 2949 CONECT 2949 2948 2950 CONECT 2950 2949 2952 CONECT 2951 2953 2957 CONECT 2952 2950 2954 2957 CONECT 2953 2941 2951 2956 CONECT 2954 2952 CONECT 2955 2941 CONECT 2956 2953 CONECT 2957 2951 2952 CONECT 2958 2959 CONECT 2959 2958 2960 CONECT 2960 2959 2961 CONECT 2961 2960 2962 CONECT 2962 2961 2963 CONECT 2963 2962 2964 CONECT 2964 2963 2965 CONECT 2965 2964 2966 CONECT 2966 2965 2967 CONECT 2967 2966 2968 CONECT 2968 2967 2969 CONECT 2969 2968 2970 CONECT 2970 2969 2971 CONECT 2971 2970 CONECT 2972 2973 2974 2975 CONECT 2973 2972 CONECT 2974 2972 CONECT 2975 2972 2976 CONECT 2976 2975 2977 CONECT 2977 2976 2978 CONECT 2978 2977 2979 CONECT 2979 2978 2980 CONECT 2980 2979 CONECT 2981 2982 2983 2984 CONECT 2982 2981 CONECT 2983 2981 CONECT 2984 2981 2985 CONECT 2985 2984 2986 CONECT 2986 2985 2987 CONECT 2987 2986 MASTER 440 0 14 14 2 0 24 6 3003 1 226 32 END