HEADER LYASE 16-JUN-15 5C2X TITLE CRYSTAL STRUCTURE OF DEOXYRIBOSE-PHOSPHATE ALDOLASE FROM COLWELLIA TITLE 2 PSYCHRERYTHRAEA (TETRAGONAL FORM) COMPND MOL_ID: 1; COMPND 2 MOLECULE: DEOXYRIBOSE-PHOSPHATE ALDOLASE; COMPND 3 CHAIN: A, B; COMPND 4 EC: 4.1.2.4; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: COLWELLIA PSYCHRERYTHRAEA; SOURCE 3 ORGANISM_TAXID: 28229; SOURCE 4 GENE: DEOC, CPS_1972; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET21A KEYWDS DERA, TIM BARREL, PSYCHROPHILIC, LYASE EXPDTA X-RAY DIFFRACTION AUTHOR M.DICK,O.H.WEIERGRAEBER,J.PIETRUSZKA REVDAT 1 03-FEB-16 5C2X 0 JRNL AUTH M.DICK,O.H.WEIERGRABER,T.CLASSEN,C.BISTERFELD,J.BRAMSKI, JRNL AUTH 2 H.GOHLKE,J.PIETRUSZKA JRNL TITL TRADING OFF STABILITY AGAINST ACTIVITY IN EXTREMOPHILIC JRNL TITL 2 ALDOLASES. JRNL REF SCI REP V. 6 17908 2016 JRNL REFN ESSN 2045-2322 JRNL PMID 26783049 JRNL DOI 10.1038/SREP17908 REMARK 2 REMARK 2 RESOLUTION. 2.11 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.11 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.15 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 82.3 REMARK 3 NUMBER OF REFLECTIONS : 29929 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.163 REMARK 3 R VALUE (WORKING SET) : 0.161 REMARK 3 FREE R VALUE : 0.201 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1497 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 47.1587 - 4.6803 0.76 2566 136 0.1587 0.1652 REMARK 3 2 4.6803 - 3.7154 0.79 2526 133 0.1176 0.1677 REMARK 3 3 3.7154 - 3.2459 0.81 2536 133 0.1432 0.1750 REMARK 3 4 3.2459 - 2.9491 0.82 2557 135 0.1592 0.2291 REMARK 3 5 2.9491 - 2.7378 0.83 2603 137 0.1659 0.1860 REMARK 3 6 2.7378 - 2.5764 0.83 2586 136 0.1744 0.2496 REMARK 3 7 2.5764 - 2.4474 0.84 2618 137 0.1858 0.2346 REMARK 3 8 2.4474 - 2.3408 0.85 2622 139 0.1951 0.2586 REMARK 3 9 2.3408 - 2.2507 0.85 2614 137 0.1916 0.2434 REMARK 3 10 2.2507 - 2.1730 0.86 2650 140 0.2091 0.2428 REMARK 3 11 2.1730 - 2.1051 0.83 2554 134 0.2365 0.2847 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.800 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 30.43 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.08 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 : 0.005 3683 REMARK 3 ANGLE : 0.813 5011 REMARK 3 CHIRALITY : 0.030 614 REMARK 3 PLANARITY : 0.004 652 REMARK 3 DIHEDRAL : 11.015 1300 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A AND RESID 2:301 REMARK 3 ORIGIN FOR THE GROUP (A): 8.6825 1.9870 14.1512 REMARK 3 T TENSOR REMARK 3 T11: 0.2599 T22: 0.2606 REMARK 3 T33: 0.1596 T12: -0.0192 REMARK 3 T13: -0.0055 T23: 0.0120 REMARK 3 L TENSOR REMARK 3 L11: 1.8823 L22: 1.8882 REMARK 3 L33: 0.8050 L12: 0.2251 REMARK 3 L13: -0.2088 L23: -0.1149 REMARK 3 S TENSOR REMARK 3 S11: -0.0124 S12: -0.0434 S13: -0.0720 REMARK 3 S21: 0.0313 S22: 0.0257 S23: 0.0252 REMARK 3 S31: 0.0613 S32: -0.1263 S33: -0.0168 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN B AND RESID 2:301 REMARK 3 ORIGIN FOR THE GROUP (A): 44.5250 13.3589 18.0876 REMARK 3 T TENSOR REMARK 3 T11: 0.2275 T22: 0.2138 REMARK 3 T33: 0.2105 T12: -0.0339 REMARK 3 T13: -0.0034 T23: 0.0300 REMARK 3 L TENSOR REMARK 3 L11: 2.9468 L22: 1.4537 REMARK 3 L33: 1.4469 L12: 0.1287 REMARK 3 L13: -0.9558 L23: -0.3327 REMARK 3 S TENSOR REMARK 3 S11: 0.0591 S12: -0.3077 S13: 0.0869 REMARK 3 S21: 0.0609 S22: -0.0868 S23: -0.1758 REMARK 3 S31: -0.1015 S32: 0.2224 S33: 0.0274 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 5C2X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-15. REMARK 100 THE DEPOSITION ID IS D_1000210938. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 08-FEB-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID29 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.969 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29931 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.110 REMARK 200 RESOLUTION RANGE LOW (A) : 47.150 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 82.3 REMARK 200 DATA REDUNDANCY : 6.900 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.1500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 82.2 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 0.91000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.020 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1JCL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 57.49 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LITHIUM SULFATE, TRIS REMARK 280 BUFFER, TRIETHANOLAMINE, PH 8.5, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 56.49000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.88000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.88000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 28.24500 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.88000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.88000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 84.73500 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.88000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.88000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 28.24500 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.88000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.88000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 84.73500 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.49000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19090 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 502 LIES ON A SPECIAL POSITION. 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 1 REMARK 465 LYS A 248 REMARK 465 SER A 249 REMARK 465 ASN A 250 REMARK 465 THR A 251 REMARK 465 LYS A 252 REMARK 465 SER A 253 REMARK 465 SER A 254 REMARK 465 SER A 255 REMARK 465 ASN A 256 REMARK 465 TYR A 257 REMARK 465 HIS A 258 REMARK 465 HIS A 259 REMARK 465 HIS A 260 REMARK 465 HIS A 261 REMARK 465 HIS A 262 REMARK 465 HIS A 263 REMARK 465 MET B 1 REMARK 465 LYS B 248 REMARK 465 SER B 249 REMARK 465 ASN B 250 REMARK 465 THR B 251 REMARK 465 LYS B 252 REMARK 465 SER B 253 REMARK 465 SER B 254 REMARK 465 SER B 255 REMARK 465 ASN B 256 REMARK 465 TYR B 257 REMARK 465 HIS B 258 REMARK 465 HIS B 259 REMARK 465 HIS B 260 REMARK 465 HIS B 261 REMARK 465 HIS B 262 REMARK 465 HIS B 263 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 58 CE NZ REMARK 470 LYS A 61 CG CD CE NZ REMARK 470 LYS A 69 CE NZ REMARK 470 LYS A 145 CD CE NZ REMARK 470 LYS A 152 CD CE NZ REMARK 470 LYS A 171 CE NZ REMARK 470 LYS A 182 CE NZ REMARK 470 SER B 2 OG REMARK 470 ASP B 3 CG OD1 OD2 REMARK 470 LYS B 5 CE NZ REMARK 470 ARG B 34 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 37 CG CD CE NZ REMARK 470 LYS B 57 CE NZ REMARK 470 LYS B 61 CE NZ REMARK 470 GLN B 112 CG CD OE1 NE2 REMARK 470 LYS B 123 CE NZ REMARK 470 LYS B 134 CE NZ REMARK 470 LYS B 145 CG CD CE NZ REMARK 470 GLU B 148 CD OE1 OE2 REMARK 470 LYS B 152 CD CE NZ REMARK 470 LYS B 171 CE NZ REMARK 470 GLU B 179 CG CD OE1 OE2 REMARK 470 LYS B 182 CG CD CE NZ REMARK 470 LYS B 189 CD CE NZ REMARK 470 ARG B 204 CG CD NE CZ NH1 NH2 REMARK 470 GLU B 223 CD OE1 OE2 REMARK 470 ILE B 239 CG1 CG2 CD1 REMARK 470 ASP B 243 CG OD1 OD2 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 ASN A 132 -38.66 -138.77 REMARK 500 GLU A 140 66.27 61.15 REMARK 500 LYS A 145 -72.97 65.24 REMARK 500 ASN A 175 -128.61 -113.96 REMARK 500 ASN A 192 105.40 -163.07 REMARK 500 SER A 235 -77.49 -118.48 REMARK 500 ASN B 132 -34.13 -130.50 REMARK 500 GLU B 140 70.79 56.99 REMARK 500 LYS B 145 -63.02 69.58 REMARK 500 ASN B 175 -132.46 -106.09 REMARK 500 ASN B 192 104.21 -163.04 REMARK 500 SER B 235 -74.97 -124.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 564 DISTANCE = 6.25 ANGSTROMS REMARK 525 HOH B 539 DISTANCE = 6.26 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CO3 B 303 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue LYS B 166 DBREF 5C2X A 1 257 UNP Q483R4 Q483R4_COLP3 1 257 DBREF 5C2X B 1 257 UNP Q483R4 Q483R4_COLP3 1 257 SEQADV 5C2X HIS A 258 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS A 259 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS A 260 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS A 261 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS A 262 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS A 263 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS B 258 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS B 259 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS B 260 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS B 261 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS B 262 UNP Q483R4 EXPRESSION TAG SEQADV 5C2X HIS B 263 UNP Q483R4 EXPRESSION TAG SEQRES 1 A 263 MET SER ASP ILE LYS ALA VAL ALA GLN ARG ALA LEU SER SEQRES 2 A 263 LEU MET ASP LEU THR SER LEU THR ASN THR GLU THR ASP SEQRES 3 A 263 GLN GLU ILE ILE ASP LEU CYS ARG GLN ALA LYS SER PRO SEQRES 4 A 263 ALA GLY GLU THR ALA ALA ILE CYS ILE PHE PRO ARG PHE SEQRES 5 A 263 ILE PRO VAL ALA LYS LYS ALA LEU LYS ALA GLN GLN THR SEQRES 6 A 263 PRO HIS ILE LYS ILE ALA THR VAL THR ASN PHE PRO GLN SEQRES 7 A 263 GLY ASN ASP ASP LEU ASP ILE ALA LEU ALA GLU THR ARG SEQRES 8 A 263 ALA ALA VAL ALA TYR GLY ALA ASP GLU VAL ASP LEU VAL SEQRES 9 A 263 PHE PRO TYR ARG ALA LEU ILE GLN GLY ASN GLU THR ILE SEQRES 10 A 263 GLY PHE ASP MET VAL LYS VAL CYS LYS GLN ALA CYS SER SEQRES 11 A 263 GLY ASN ALA LYS LEU LYS VAL ILE ILE GLU THR GLY GLU SEQRES 12 A 263 LEU LYS SER GLU GLU LEU ILE ARG LYS ALA SER GLU ILE SEQRES 13 A 263 ALA ILE ASN ALA GLY ALA ASP PHE ILE LYS THR SER THR SEQRES 14 A 263 GLY LYS VAL ALA ILE ASN ALA THR PRO GLU ALA ALA LYS SEQRES 15 A 263 VAL MET LEU THR VAL ILE LYS ASN LYS ASN THR ALA VAL SEQRES 16 A 263 GLY PHE LYS PRO ALA GLY GLY VAL ARG ASN ALA ASP ASP SEQRES 17 A 263 ALA ALA ILE TYR LEU ASP LEU ALA ASP ASN ILE LEU GLY SEQRES 18 A 263 ASN GLU TRP ALA ASP ALA ASN HIS PHE ARG PHE GLY ALA SEQRES 19 A 263 SER SER LEU LEU ILE SER LEU LEU ASP THR LEU GLY HIS SEQRES 20 A 263 LYS SER ASN THR LYS SER SER SER ASN TYR HIS HIS HIS SEQRES 21 A 263 HIS HIS HIS SEQRES 1 B 263 MET SER ASP ILE LYS ALA VAL ALA GLN ARG ALA LEU SER SEQRES 2 B 263 LEU MET ASP LEU THR SER LEU THR ASN THR GLU THR ASP SEQRES 3 B 263 GLN GLU ILE ILE ASP LEU CYS ARG GLN ALA LYS SER PRO SEQRES 4 B 263 ALA GLY GLU THR ALA ALA ILE CYS ILE PHE PRO ARG PHE SEQRES 5 B 263 ILE PRO VAL ALA LYS LYS ALA LEU LYS ALA GLN GLN THR SEQRES 6 B 263 PRO HIS ILE LYS ILE ALA THR VAL THR ASN PHE PRO GLN SEQRES 7 B 263 GLY ASN ASP ASP LEU ASP ILE ALA LEU ALA GLU THR ARG SEQRES 8 B 263 ALA ALA VAL ALA TYR GLY ALA ASP GLU VAL ASP LEU VAL SEQRES 9 B 263 PHE PRO TYR ARG ALA LEU ILE GLN GLY ASN GLU THR ILE SEQRES 10 B 263 GLY PHE ASP MET VAL LYS VAL CYS LYS GLN ALA CYS SER SEQRES 11 B 263 GLY ASN ALA LYS LEU LYS VAL ILE ILE GLU THR GLY GLU SEQRES 12 B 263 LEU LYS SER GLU GLU LEU ILE ARG LYS ALA SER GLU ILE SEQRES 13 B 263 ALA ILE ASN ALA GLY ALA ASP PHE ILE LYS THR SER THR SEQRES 14 B 263 GLY LYS VAL ALA ILE ASN ALA THR PRO GLU ALA ALA LYS SEQRES 15 B 263 VAL MET LEU THR VAL ILE LYS ASN LYS ASN THR ALA VAL SEQRES 16 B 263 GLY PHE LYS PRO ALA GLY GLY VAL ARG ASN ALA ASP ASP SEQRES 17 B 263 ALA ALA ILE TYR LEU ASP LEU ALA ASP ASN ILE LEU GLY SEQRES 18 B 263 ASN GLU TRP ALA ASP ALA ASN HIS PHE ARG PHE GLY ALA SEQRES 19 B 263 SER SER LEU LEU ILE SER LEU LEU ASP THR LEU GLY HIS SEQRES 20 B 263 LYS SER ASN THR LYS SER SER SER ASN TYR HIS HIS HIS SEQRES 21 B 263 HIS HIS HIS HET UNL A 301 6 HET SO4 A 302 5 HET UNL B 301 6 HET SO4 B 302 5 HET CO3 B 303 4 HETNAM UNL UNKNOWN LIGAND HETNAM SO4 SULFATE ION HETNAM CO3 CARBONATE ION FORMUL 4 SO4 2(O4 S 2-) FORMUL 7 CO3 C O3 2- FORMUL 8 HOH *303(H2 O) HELIX 1 AA1 ASP A 3 LEU A 14 1 12 HELIX 2 AA2 THR A 25 ALA A 36 1 12 HELIX 3 AA3 PHE A 49 ARG A 51 5 3 HELIX 4 AA4 PHE A 52 GLN A 63 1 12 HELIX 5 AA5 ASP A 82 GLY A 97 1 16 HELIX 6 AA6 PRO A 106 GLN A 112 1 7 HELIX 7 AA7 GLU A 115 SER A 130 1 16 HELIX 8 AA8 GLU A 140 LYS A 145 1 6 HELIX 9 AA9 SER A 146 GLY A 161 1 16 HELIX 10 AB1 THR A 177 ASN A 192 1 16 HELIX 11 AB2 ASN A 205 GLY A 221 1 17 HELIX 12 AB3 SER A 236 LEU A 245 1 10 HELIX 13 AB4 ASP B 3 LEU B 14 1 12 HELIX 14 AB5 THR B 25 ALA B 36 1 12 HELIX 15 AB6 PHE B 49 ARG B 51 5 3 HELIX 16 AB7 PHE B 52 GLN B 63 1 12 HELIX 17 AB8 ASP B 82 GLY B 97 1 16 HELIX 18 AB9 PRO B 106 GLN B 112 1 7 HELIX 19 AC1 GLU B 115 SER B 130 1 16 HELIX 20 AC2 GLU B 140 LYS B 145 1 6 HELIX 21 AC3 SER B 146 GLY B 161 1 16 HELIX 22 AC4 THR B 177 ASN B 192 1 16 HELIX 23 AC5 ASN B 205 GLY B 221 1 17 HELIX 24 AC6 SER B 236 LEU B 245 1 10 SHEET 1 AA1 8 GLY A 196 LYS A 198 0 SHEET 2 AA1 8 PHE A 164 LYS A 166 1 N ILE A 165 O GLY A 196 SHEET 3 AA1 8 LYS A 134 ILE A 138 1 N VAL A 137 O LYS A 166 SHEET 4 AA1 8 GLU A 100 VAL A 104 1 N LEU A 103 O ILE A 138 SHEET 5 AA1 8 LYS A 69 THR A 74 1 N THR A 72 O ASP A 102 SHEET 6 AA1 8 ALA A 45 CYS A 47 1 N ILE A 46 O ALA A 71 SHEET 7 AA1 8 MET A 15 THR A 18 1 N LEU A 17 O ALA A 45 SHEET 8 AA1 8 PHE A 232 ALA A 234 1 O PHE A 232 N ASP A 16 SHEET 1 AA2 2 LYS A 37 SER A 38 0 SHEET 2 AA2 2 GLY A 41 GLU A 42 -1 O GLY A 41 N SER A 38 SHEET 1 AA3 8 GLY B 196 LYS B 198 0 SHEET 2 AA3 8 PHE B 164 LYS B 166 1 N ILE B 165 O GLY B 196 SHEET 3 AA3 8 LYS B 134 ILE B 138 1 N VAL B 137 O LYS B 166 SHEET 4 AA3 8 GLU B 100 VAL B 104 1 N LEU B 103 O ILE B 138 SHEET 5 AA3 8 LYS B 69 THR B 74 1 N THR B 72 O ASP B 102 SHEET 6 AA3 8 ALA B 45 CYS B 47 1 N ILE B 46 O ALA B 71 SHEET 7 AA3 8 MET B 15 THR B 18 1 N LEU B 17 O ALA B 45 SHEET 8 AA3 8 PHE B 232 ALA B 234 1 O PHE B 232 N ASP B 16 SHEET 1 AA4 2 LYS B 37 SER B 38 0 SHEET 2 AA4 2 GLY B 41 GLU B 42 -1 O GLY B 41 N SER B 38 LINK NZ LYS A 166 C1 UNL A 301 1555 1555 1.38 LINK NZ LYS B 166 C1 UNL B 301 1555 1555 1.38 CISPEP 1 PHE A 76 PRO A 77 0 -3.25 CISPEP 2 PHE B 76 PRO B 77 0 -2.32 SITE 1 AC1 7 GLY A 201 GLY A 202 ARG A 204 ALA A 234 SITE 2 AC1 7 SER A 235 HOH A 460 HOH A 490 SITE 1 AC2 5 LYS B 191 GLY B 202 ALA B 234 SER B 235 SITE 2 AC2 5 HOH B 414 SITE 1 AC3 4 ARG B 91 ALA B 128 HOH B 403 HOH B 461 SITE 1 AC4 9 ASP B 102 VAL B 137 ILE B 138 ILE B 139 SITE 2 AC4 9 ILE B 165 THR B 167 SER B 168 LYS B 198 SITE 3 AC4 9 ALA B 200 CRYST1 103.760 103.760 112.980 90.00 90.00 90.00 P 41 21 2 16 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 0.009638 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009638 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008851 0.00000 ATOM 1 N SER A 2 -8.585 -21.127 18.515 1.00 73.35 N ANISOU 1 N SER A 2 8705 8392 10774 -1758 620 844 N ATOM 2 CA SER A 2 -8.637 -19.698 18.228 1.00 71.78 C ANISOU 2 CA SER A 2 8497 8375 10403 -1680 568 778 C ATOM 3 C SER A 2 -7.788 -19.350 17.008 1.00 69.07 C ANISOU 3 C SER A 2 8222 8042 9981 -1632 440 618 C ATOM 4 O SER A 2 -7.195 -20.229 16.379 1.00 69.71 O ANISOU 4 O SER A 2 8354 7992 10141 -1661 398 547 O ATOM 5 CB SER A 2 -8.171 -18.888 19.441 1.00 71.06 C ANISOU 5 CB SER A 2 8474 8390 10137 -1578 648 907 C ATOM 6 OG SER A 2 -6.839 -19.219 19.791 1.00 68.47 O ANISOU 6 OG SER A 2 8278 7999 9740 -1510 644 958 O ATOM 7 N ASP A 3 -7.730 -18.062 16.688 1.00 63.73 N ANISOU 7 N ASP A 3 7547 7516 9151 -1557 388 563 N ATOM 8 CA ASP A 3 -7.023 -17.582 15.506 1.00 59.31 C ANISOU 8 CA ASP A 3 7045 6988 8500 -1513 274 420 C ATOM 9 C ASP A 3 -5.648 -17.026 15.885 1.00 51.20 C ANISOU 9 C ASP A 3 6144 5991 7318 -1393 283 454 C ATOM 10 O ASP A 3 -4.984 -16.353 15.091 1.00 48.64 O ANISOU 10 O ASP A 3 5871 5721 6888 -1336 209 359 O ATOM 11 CB ASP A 3 -7.862 -16.512 14.805 1.00 64.23 C ANISOU 11 CB ASP A 3 7583 7752 9071 -1512 200 344 C ATOM 12 CG ASP A 3 -7.424 -16.265 13.378 1.00 68.93 C ANISOU 12 CG ASP A 3 8219 8367 9603 -1506 74 189 C ATOM 13 OD1 ASP A 3 -7.118 -17.248 12.669 1.00 70.82 O ANISOU 13 OD1 ASP A 3 8494 8494 9919 -1568 36 101 O ATOM 14 OD2 ASP A 3 -7.383 -15.085 12.968 1.00 70.49 O ANISOU 14 OD2 ASP A 3 8418 8690 9675 -1441 19 157 O ATOM 15 N ILE A 4 -5.222 -17.332 17.103 1.00 45.88 N ANISOU 15 N ILE A 4 5517 5282 6634 -1361 371 593 N ATOM 16 CA ILE A 4 -4.092 -16.653 17.714 1.00 40.71 C ANISOU 16 CA ILE A 4 4960 4682 5825 -1250 382 648 C ATOM 17 C ILE A 4 -2.745 -16.994 17.067 1.00 37.84 C ANISOU 17 C ILE A 4 4688 4238 5451 -1204 324 580 C ATOM 18 O ILE A 4 -1.811 -16.192 17.118 1.00 34.25 O ANISOU 18 O ILE A 4 4298 3849 4866 -1114 298 571 O ATOM 19 CB ILE A 4 -4.030 -16.962 19.231 1.00 39.18 C ANISOU 19 CB ILE A 4 4794 4477 5614 -1236 484 825 C ATOM 20 CG1 ILE A 4 -3.248 -15.873 19.965 1.00 40.05 C ANISOU 20 CG1 ILE A 4 4979 4704 5535 -1130 489 871 C ATOM 21 CG2 ILE A 4 -3.453 -18.352 19.491 1.00 37.54 C ANISOU 21 CG2 ILE A 4 4632 4101 5532 -1268 507 896 C ATOM 22 CD1 ILE A 4 -3.769 -14.469 19.691 1.00 41.33 C ANISOU 22 CD1 ILE A 4 5097 5016 5591 -1092 470 798 C ATOM 23 N LYS A 5 -2.640 -18.167 16.449 1.00 37.02 N ANISOU 23 N LYS A 5 4586 3987 5492 -1267 310 526 N ATOM 24 CA LYS A 5 -1.366 -18.581 15.870 1.00 35.91 C ANISOU 24 CA LYS A 5 4526 3756 5363 -1222 276 460 C ATOM 25 C LYS A 5 -1.126 -17.899 14.528 1.00 35.45 C ANISOU 25 C LYS A 5 4482 3764 5223 -1205 197 292 C ATOM 26 O LYS A 5 0.002 -17.495 14.219 1.00 34.22 O ANISOU 26 O LYS A 5 4394 3621 4987 -1128 175 253 O ATOM 27 CB LYS A 5 -1.302 -20.105 15.730 1.00 36.62 C ANISOU 27 CB LYS A 5 4617 3649 5649 -1290 303 459 C ATOM 28 CG LYS A 5 -1.147 -20.812 17.072 1.00 38.64 C ANISOU 28 CG LYS A 5 4885 3822 5973 -1283 380 649 C ATOM 29 CD LYS A 5 -0.680 -22.248 16.922 1.00 40.11 C ANISOU 29 CD LYS A 5 5092 3793 6355 -1318 402 655 C ATOM 30 CE LYS A 5 -1.781 -23.128 16.387 1.00 42.05 C ANISOU 30 CE LYS A 5 5266 3937 6774 -1447 414 586 C ATOM 31 NZ LYS A 5 -1.330 -24.531 16.163 1.00 43.82 N ANISOU 31 NZ LYS A 5 5510 3932 7206 -1483 438 572 N ATOM 32 N ALA A 6 -2.187 -17.751 13.742 1.00 33.41 N ANISOU 32 N ALA A 6 4156 3552 4984 -1279 152 200 N ATOM 33 CA ALA A 6 -2.104 -17.002 12.493 1.00 35.18 C ANISOU 33 CA ALA A 6 4394 3864 5108 -1268 70 58 C ATOM 34 C ALA A 6 -1.735 -15.541 12.768 1.00 35.90 C ANISOU 34 C ALA A 6 4506 4105 5029 -1169 59 99 C ATOM 35 O ALA A 6 -0.937 -14.945 12.040 1.00 34.25 O ANISOU 35 O ALA A 6 4354 3938 4720 -1115 19 25 O ATOM 36 CB ALA A 6 -3.421 -17.090 11.726 1.00 34.07 C ANISOU 36 CB ALA A 6 4165 3758 5020 -1368 11 -25 C ATOM 37 N VAL A 7 -2.318 -14.973 13.824 1.00 37.54 N ANISOU 37 N VAL A 7 4668 4387 5208 -1148 102 213 N ATOM 38 CA VAL A 7 -1.987 -13.611 14.255 1.00 33.64 C ANISOU 38 CA VAL A 7 4195 4020 4568 -1056 103 254 C ATOM 39 C VAL A 7 -0.520 -13.512 14.659 1.00 30.41 C ANISOU 39 C VAL A 7 3880 3580 4093 -972 120 287 C ATOM 40 O VAL A 7 0.170 -12.564 14.298 1.00 33.94 O ANISOU 40 O VAL A 7 4366 4095 4433 -905 87 248 O ATOM 41 CB VAL A 7 -2.868 -13.151 15.440 1.00 32.78 C ANISOU 41 CB VAL A 7 4025 3982 4449 -1053 168 366 C ATOM 42 CG1 VAL A 7 -2.299 -11.875 16.081 1.00 32.30 C ANISOU 42 CG1 VAL A 7 4006 4024 4242 -954 184 408 C ATOM 43 CG2 VAL A 7 -4.308 -12.936 14.987 1.00 31.39 C ANISOU 43 CG2 VAL A 7 3734 3860 4332 -1119 145 331 C ATOM 44 N ALA A 8 -0.047 -14.506 15.403 1.00 31.29 N ANISOU 44 N ALA A 8 4022 3586 4282 -978 167 366 N ATOM 45 CA ALA A 8 1.330 -14.524 15.876 1.00 29.35 C ANISOU 45 CA ALA A 8 3852 3304 3998 -900 175 413 C ATOM 46 C ALA A 8 2.312 -14.594 14.709 1.00 28.06 C ANISOU 46 C ALA A 8 3732 3095 3836 -874 132 293 C ATOM 47 O ALA A 8 3.336 -13.922 14.710 1.00 29.35 O ANISOU 47 O ALA A 8 3939 3295 3919 -798 117 288 O ATOM 48 CB ALA A 8 1.547 -15.688 16.820 1.00 28.68 C ANISOU 48 CB ALA A 8 3781 3102 4014 -918 225 531 C ATOM 49 N GLN A 9 1.983 -15.413 13.718 1.00 31.50 N ANISOU 49 N GLN A 9 4155 3448 4365 -942 117 192 N ATOM 50 CA GLN A 9 2.816 -15.576 12.537 1.00 34.40 C ANISOU 50 CA GLN A 9 4567 3770 4732 -929 92 63 C ATOM 51 C GLN A 9 2.920 -14.261 11.761 1.00 34.13 C ANISOU 51 C GLN A 9 4546 3873 4549 -891 46 -9 C ATOM 52 O GLN A 9 4.004 -13.855 11.333 1.00 30.90 O ANISOU 52 O GLN A 9 4185 3471 4084 -830 44 -50 O ATOM 53 CB GLN A 9 2.248 -16.681 11.643 1.00 39.88 C ANISOU 53 CB GLN A 9 5247 4362 5545 -1023 85 -46 C ATOM 54 CG GLN A 9 3.230 -17.210 10.623 1.00 49.52 C ANISOU 54 CG GLN A 9 6525 5492 6798 -1012 90 -173 C ATOM 55 CD GLN A 9 4.336 -18.023 11.264 1.00 55.92 C ANISOU 55 CD GLN A 9 7364 6162 7720 -959 145 -107 C ATOM 56 OE1 GLN A 9 4.078 -18.872 12.122 1.00 61.43 O ANISOU 56 OE1 GLN A 9 8039 6761 8541 -983 177 -6 O ATOM 57 NE2 GLN A 9 5.573 -17.768 10.858 1.00 52.58 N ANISOU 57 NE2 GLN A 9 6986 5727 7264 -886 157 -153 N ATOM 58 N ARG A 10 1.782 -13.597 11.596 1.00 31.67 N ANISOU 58 N ARG A 10 4184 3666 4185 -926 12 -15 N ATOM 59 CA ARG A 10 1.726 -12.339 10.872 1.00 31.87 C ANISOU 59 CA ARG A 10 4213 3817 4081 -894 -37 -66 C ATOM 60 C ARG A 10 2.484 -11.245 11.622 1.00 27.33 C ANISOU 60 C ARG A 10 3662 3310 3413 -799 -19 10 C ATOM 61 O ARG A 10 3.271 -10.504 11.031 1.00 26.40 O ANISOU 61 O ARG A 10 3584 3232 3213 -749 -36 -33 O ATOM 62 CB ARG A 10 0.269 -11.930 10.648 1.00 36.45 C ANISOU 62 CB ARG A 10 4715 4481 4653 -949 -80 -71 C ATOM 63 CG ARG A 10 0.077 -10.775 9.693 1.00 37.92 C ANISOU 63 CG ARG A 10 4899 4784 4723 -928 -146 -125 C ATOM 64 CD ARG A 10 -1.400 -10.458 9.515 1.00 39.93 C ANISOU 64 CD ARG A 10 5060 5113 5000 -981 -197 -119 C ATOM 65 NE ARG A 10 -1.605 -9.450 8.483 1.00 41.71 N ANISOU 65 NE ARG A 10 5284 5442 5122 -964 -274 -164 N ATOM 66 CZ ARG A 10 -2.740 -8.783 8.299 1.00 41.02 C ANISOU 66 CZ ARG A 10 5111 5442 5034 -979 -331 -143 C ATOM 67 NH1 ARG A 10 -3.780 -9.007 9.090 1.00 40.82 N ANISOU 67 NH1 ARG A 10 4990 5414 5108 -1012 -307 -84 N ATOM 68 NH2 ARG A 10 -2.827 -7.884 7.328 1.00 40.80 N ANISOU 68 NH2 ARG A 10 5090 5502 4911 -959 -407 -171 N ATOM 69 N ALA A 11 2.254 -11.157 12.928 1.00 27.39 N ANISOU 69 N ALA A 11 3648 3328 3433 -780 19 122 N ATOM 70 CA ALA A 11 2.922 -10.157 13.759 1.00 26.24 C ANISOU 70 CA ALA A 11 3526 3245 3198 -699 33 187 C ATOM 71 C ALA A 11 4.443 -10.277 13.676 1.00 28.64 C ANISOU 71 C ALA A 11 3892 3495 3497 -643 34 177 C ATOM 72 O ALA A 11 5.154 -9.276 13.484 1.00 27.38 O ANISOU 72 O ALA A 11 3755 3391 3258 -586 18 158 O ATOM 73 CB ALA A 11 2.463 -10.283 15.201 1.00 27.21 C ANISOU 73 CB ALA A 11 3630 3379 3330 -700 80 303 C ATOM 74 N LEU A 12 4.936 -11.505 13.813 1.00 27.33 N ANISOU 74 N LEU A 12 3743 3211 3431 -659 56 191 N ATOM 75 CA LEU A 12 6.373 -11.760 13.803 1.00 26.40 C ANISOU 75 CA LEU A 12 3665 3025 3340 -603 62 190 C ATOM 76 C LEU A 12 7.026 -11.226 12.524 1.00 29.71 C ANISOU 76 C LEU A 12 4108 3465 3714 -582 48 76 C ATOM 77 O LEU A 12 8.092 -10.597 12.576 1.00 29.37 O ANISOU 77 O LEU A 12 4085 3441 3634 -519 46 82 O ATOM 78 CB LEU A 12 6.653 -13.259 13.967 1.00 26.43 C ANISOU 78 CB LEU A 12 3673 2881 3488 -629 90 213 C ATOM 79 CG LEU A 12 8.107 -13.665 14.234 1.00 28.70 C ANISOU 79 CG LEU A 12 3984 3082 3837 -564 98 245 C ATOM 80 CD1 LEU A 12 8.171 -14.954 15.043 1.00 32.86 C ANISOU 80 CD1 LEU A 12 4506 3483 4498 -577 121 344 C ATOM 81 CD2 LEU A 12 8.886 -13.827 12.937 1.00 29.23 C ANISOU 81 CD2 LEU A 12 4069 3097 3940 -552 111 115 C ATOM 82 N SER A 13 6.385 -11.465 11.381 1.00 28.65 N ANISOU 82 N SER A 13 3973 3332 3582 -639 37 -25 N ATOM 83 CA SER A 13 6.930 -11.029 10.094 1.00 30.51 C ANISOU 83 CA SER A 13 4241 3593 3757 -628 30 -132 C ATOM 84 C SER A 13 6.889 -9.504 9.925 1.00 28.44 C ANISOU 84 C SER A 13 3979 3460 3367 -589 1 -119 C ATOM 85 O SER A 13 7.507 -8.956 9.010 1.00 28.64 O ANISOU 85 O SER A 13 4035 3515 3331 -568 3 -180 O ATOM 86 CB SER A 13 6.176 -11.692 8.943 1.00 33.02 C ANISOU 86 CB SER A 13 4566 3891 4090 -708 15 -244 C ATOM 87 OG SER A 13 4.912 -11.082 8.752 1.00 37.29 O ANISOU 87 OG SER A 13 5070 4533 4566 -749 -37 -241 O ATOM 88 N LEU A 14 6.161 -8.828 10.811 1.00 26.54 N ANISOU 88 N LEU A 14 3702 3288 3091 -580 -16 -40 N ATOM 89 CA LEU A 14 6.029 -7.377 10.758 1.00 27.01 C ANISOU 89 CA LEU A 14 3755 3455 3053 -542 -40 -23 C ATOM 90 C LEU A 14 6.846 -6.684 11.849 1.00 26.55 C ANISOU 90 C LEU A 14 3703 3410 2973 -475 -25 48 C ATOM 91 O LEU A 14 6.816 -5.462 11.966 1.00 23.62 O ANISOU 91 O LEU A 14 3326 3113 2535 -440 -37 63 O ATOM 92 CB LEU A 14 4.554 -6.974 10.882 1.00 26.76 C ANISOU 92 CB LEU A 14 3670 3495 3001 -577 -68 -2 C ATOM 93 CG LEU A 14 3.597 -7.528 9.821 1.00 26.50 C ANISOU 93 CG LEU A 14 3618 3467 2985 -651 -105 -71 C ATOM 94 CD1 LEU A 14 2.151 -7.176 10.137 1.00 26.53 C ANISOU 94 CD1 LEU A 14 3547 3535 3000 -681 -131 -33 C ATOM 95 CD2 LEU A 14 3.971 -7.031 8.439 1.00 23.84 C ANISOU 95 CD2 LEU A 14 3320 3170 2567 -648 -138 -148 C ATOM 96 N MET A 15 7.575 -7.462 12.643 1.00 24.56 N ANISOU 96 N MET A 15 3463 3086 2783 -459 -4 93 N ATOM 97 CA MET A 15 8.318 -6.907 13.770 1.00 25.77 C ANISOU 97 CA MET A 15 3622 3257 2912 -405 -5 163 C ATOM 98 C MET A 15 9.550 -6.101 13.370 1.00 27.53 C ANISOU 98 C MET A 15 3862 3490 3110 -353 -12 133 C ATOM 99 O MET A 15 10.318 -6.491 12.485 1.00 28.02 O ANISOU 99 O MET A 15 3935 3498 3212 -349 3 79 O ATOM 100 CB MET A 15 8.764 -8.021 14.726 1.00 27.58 C ANISOU 100 CB MET A 15 3857 3407 3216 -403 5 236 C ATOM 101 CG MET A 15 7.783 -8.345 15.831 1.00 31.96 C ANISOU 101 CG MET A 15 4399 3982 3762 -431 17 318 C ATOM 102 SD MET A 15 8.523 -9.427 17.075 1.00 41.68 S ANISOU 102 SD MET A 15 5647 5132 5055 -415 19 434 S ATOM 103 CE MET A 15 9.792 -8.339 17.713 1.00 21.95 C ANISOU 103 CE MET A 15 3168 2692 2480 -343 -23 456 C ATOM 104 N ASP A 16 9.725 -4.971 14.042 1.00 26.64 N ANISOU 104 N ASP A 16 3746 3440 2935 -318 -28 164 N ATOM 105 CA ASP A 16 11.025 -4.332 14.140 1.00 27.12 C ANISOU 105 CA ASP A 16 3813 3496 2995 -270 -38 162 C ATOM 106 C ASP A 16 11.646 -4.818 15.446 1.00 24.67 C ANISOU 106 C ASP A 16 3503 3158 2711 -249 -58 236 C ATOM 107 O ASP A 16 11.361 -4.267 16.507 1.00 24.13 O ANISOU 107 O ASP A 16 3441 3145 2582 -241 -76 280 O ATOM 108 CB ASP A 16 10.909 -2.804 14.127 1.00 27.45 C ANISOU 108 CB ASP A 16 3852 3614 2966 -248 -49 148 C ATOM 109 CG ASP A 16 10.563 -2.246 12.756 1.00 29.55 C ANISOU 109 CG ASP A 16 4120 3904 3205 -259 -39 92 C ATOM 110 OD1 ASP A 16 10.307 -3.037 11.824 1.00 30.77 O ANISOU 110 OD1 ASP A 16 4282 4031 3378 -291 -26 54 O ATOM 111 OD2 ASP A 16 10.544 -1.004 12.613 1.00 31.80 O ANISOU 111 OD2 ASP A 16 4400 4234 3448 -238 -45 87 O ATOM 112 N LEU A 17 12.467 -5.863 15.374 1.00 26.57 N ANISOU 112 N LEU A 17 3739 3313 3042 -240 -55 251 N ATOM 113 CA LEU A 17 13.060 -6.458 16.575 1.00 24.20 C ANISOU 113 CA LEU A 17 3438 2981 2777 -219 -86 339 C ATOM 114 C LEU A 17 14.027 -5.476 17.222 1.00 25.83 C ANISOU 114 C LEU A 17 3637 3232 2945 -179 -132 357 C ATOM 115 O LEU A 17 15.098 -5.187 16.672 1.00 22.66 O ANISOU 115 O LEU A 17 3212 2801 2596 -151 -137 321 O ATOM 116 CB LEU A 17 13.776 -7.761 16.236 1.00 25.56 C ANISOU 116 CB LEU A 17 3596 3037 3080 -211 -72 350 C ATOM 117 CG LEU A 17 14.397 -8.487 17.427 1.00 29.42 C ANISOU 117 CG LEU A 17 4078 3481 3620 -185 -114 460 C ATOM 118 CD1 LEU A 17 13.340 -8.792 18.479 1.00 28.31 C ANISOU 118 CD1 LEU A 17 3964 3379 3412 -218 -119 545 C ATOM 119 CD2 LEU A 17 15.083 -9.766 16.963 1.00 33.12 C ANISOU 119 CD2 LEU A 17 4523 3816 4246 -170 -91 465 C ATOM 120 N THR A 18 13.656 -4.975 18.397 1.00 24.18 N ANISOU 120 N THR A 18 3448 3094 2646 -180 -163 407 N ATOM 121 CA THR A 18 14.299 -3.783 18.942 1.00 24.16 C ANISOU 121 CA THR A 18 3445 3150 2584 -155 -207 394 C ATOM 122 C THR A 18 15.188 -4.018 20.167 1.00 28.47 C ANISOU 122 C THR A 18 3994 3700 3122 -135 -278 470 C ATOM 123 O THR A 18 14.823 -4.734 21.103 1.00 28.53 O ANISOU 123 O THR A 18 4027 3717 3095 -145 -293 553 O ATOM 124 CB THR A 18 13.234 -2.732 19.307 1.00 25.37 C ANISOU 124 CB THR A 18 3623 3392 2626 -171 -188 366 C ATOM 125 OG1 THR A 18 12.445 -2.436 18.144 1.00 26.81 O ANISOU 125 OG1 THR A 18 3794 3575 2819 -187 -139 305 O ATOM 126 CG2 THR A 18 13.885 -1.447 19.820 1.00 20.76 C ANISOU 126 CG2 THR A 18 3041 2857 1990 -151 -228 334 C ATOM 127 N SER A 19 16.368 -3.408 20.144 1.00 26.72 N ANISOU 127 N SER A 19 3743 3475 2935 -107 -325 448 N ATOM 128 CA SER A 19 17.200 -3.307 21.335 1.00 27.97 C ANISOU 128 CA SER A 19 3901 3662 3065 -92 -415 506 C ATOM 129 C SER A 19 17.740 -1.886 21.435 1.00 26.02 C ANISOU 129 C SER A 19 3643 3466 2778 -88 -450 437 C ATOM 130 O SER A 19 18.550 -1.455 20.611 1.00 23.09 O ANISOU 130 O SER A 19 3223 3054 2496 -73 -443 387 O ATOM 131 CB SER A 19 18.345 -4.323 21.307 1.00 28.20 C ANISOU 131 CB SER A 19 3881 3607 3226 -61 -459 569 C ATOM 132 OG SER A 19 19.107 -4.262 22.504 1.00 29.20 O ANISOU 132 OG SER A 19 4005 3770 3319 -48 -565 640 O ATOM 133 N LEU A 20 17.281 -1.154 22.441 1.00 27.57 N ANISOU 133 N LEU A 20 3886 3746 2845 -103 -478 430 N ATOM 134 CA LEU A 20 17.700 0.229 22.617 1.00 27.59 C ANISOU 134 CA LEU A 20 3883 3788 2812 -106 -509 354 C ATOM 135 C LEU A 20 18.040 0.521 24.070 1.00 29.00 C ANISOU 135 C LEU A 20 4098 4039 2883 -115 -600 378 C ATOM 136 O LEU A 20 17.501 1.453 24.660 1.00 29.85 O ANISOU 136 O LEU A 20 4250 4211 2880 -133 -592 322 O ATOM 137 CB LEU A 20 16.604 1.183 22.122 1.00 27.33 C ANISOU 137 CB LEU A 20 3874 3784 2727 -118 -428 278 C ATOM 138 CG LEU A 20 16.373 1.195 20.607 1.00 24.99 C ANISOU 138 CG LEU A 20 3543 3431 2519 -112 -355 242 C ATOM 139 CD1 LEU A 20 15.082 1.938 20.224 1.00 24.02 C ANISOU 139 CD1 LEU A 20 3443 3342 2341 -122 -287 196 C ATOM 140 CD2 LEU A 20 17.580 1.783 19.884 1.00 21.34 C ANISOU 140 CD2 LEU A 20 3029 2923 2155 -99 -372 203 C ATOM 141 N THR A 21 18.936 -0.281 24.641 1.00 29.46 N ANISOU 141 N THR A 21 4136 4084 2974 -104 -689 461 N ATOM 142 CA THR A 21 19.385 -0.073 26.012 1.00 30.91 C ANISOU 142 CA THR A 21 4356 4343 3047 -115 -798 493 C ATOM 143 C THR A 21 20.480 0.985 26.081 1.00 32.56 C ANISOU 143 C THR A 21 4519 4558 3295 -119 -880 418 C ATOM 144 O THR A 21 20.691 1.593 27.135 1.00 33.39 O ANISOU 144 O THR A 21 4664 4740 3285 -141 -962 394 O ATOM 145 CB THR A 21 19.936 -1.374 26.654 1.00 29.31 C ANISOU 145 CB THR A 21 4145 4125 2866 -100 -880 632 C ATOM 146 OG1 THR A 21 21.242 -1.663 26.130 1.00 27.03 O ANISOU 146 OG1 THR A 21 3761 3760 2748 -69 -942 651 O ATOM 147 CG2 THR A 21 18.996 -2.552 26.411 1.00 27.25 C ANISOU 147 CG2 THR A 21 3911 3826 2618 -97 -794 711 C ATOM 148 N ASN A 22 21.180 1.167 24.958 1.00 30.96 N ANISOU 148 N ASN A 22 4234 4275 3255 -101 -855 381 N ATOM 149 CA ASN A 22 22.302 2.102 24.825 1.00 30.38 C ANISOU 149 CA ASN A 22 4095 4186 3263 -106 -918 317 C ATOM 150 C ASN A 22 23.561 1.592 25.533 1.00 35.47 C ANISOU 150 C ASN A 22 4682 4831 3964 -97 -1061 388 C ATOM 151 O ASN A 22 24.542 2.322 25.688 1.00 36.94 O ANISOU 151 O ASN A 22 4809 5017 4210 -109 -1142 342 O ATOM 152 CB ASN A 22 21.923 3.496 25.346 1.00 30.29 C ANISOU 152 CB ASN A 22 4133 4235 3141 -140 -924 212 C ATOM 153 CG ASN A 22 22.746 4.605 24.714 1.00 34.53 C ANISOU 153 CG ASN A 22 4600 4723 3796 -150 -929 126 C ATOM 154 OD1 ASN A 22 23.201 4.491 23.572 1.00 34.96 O ANISOU 154 OD1 ASN A 22 4584 4701 3996 -132 -872 130 O ATOM 155 ND2 ASN A 22 22.946 5.687 25.460 1.00 35.51 N ANISOU 155 ND2 ASN A 22 4745 4889 3857 -183 -992 45 N ATOM 156 N THR A 23 23.534 0.331 25.953 1.00 37.28 N ANISOU 156 N THR A 23 4921 5056 4188 -75 -1096 505 N ATOM 157 CA THR A 23 24.708 -0.301 26.546 1.00 39.59 C ANISOU 157 CA THR A 23 5147 5338 4557 -56 -1234 596 C ATOM 158 C THR A 23 24.988 -1.644 25.885 1.00 40.15 C ANISOU 158 C THR A 23 5158 5309 4788 -9 -1194 690 C ATOM 159 O THR A 23 25.635 -2.508 26.475 1.00 44.45 O ANISOU 159 O THR A 23 5667 5839 5385 17 -1294 803 O ATOM 160 CB THR A 23 24.546 -0.513 28.069 1.00 42.90 C ANISOU 160 CB THR A 23 5646 5862 4793 -76 -1357 670 C ATOM 161 OG1 THR A 23 23.368 -1.286 28.332 1.00 41.57 O ANISOU 161 OG1 THR A 23 5568 5714 4510 -76 -1279 738 O ATOM 162 CG2 THR A 23 24.445 0.824 28.792 1.00 47.35 C ANISOU 162 CG2 THR A 23 6265 6521 5205 -124 -1409 560 C ATOM 163 N GLU A 24 24.499 -1.819 24.661 1.00 37.30 N ANISOU 163 N GLU A 24 4789 4877 4507 2 -1049 642 N ATOM 164 CA GLU A 24 24.717 -3.066 23.931 1.00 35.71 C ANISOU 164 CA GLU A 24 4537 4570 4462 43 -992 704 C ATOM 165 C GLU A 24 26.188 -3.256 23.564 1.00 36.79 C ANISOU 165 C GLU A 24 4543 4632 4805 80 -1042 720 C ATOM 166 O GLU A 24 26.903 -2.287 23.306 1.00 35.82 O ANISOU 166 O GLU A 24 4360 4518 4734 70 -1062 648 O ATOM 167 CB GLU A 24 23.861 -3.114 22.660 1.00 33.26 C ANISOU 167 CB GLU A 24 4253 4212 4172 37 -830 629 C ATOM 168 CG GLU A 24 22.364 -3.245 22.903 1.00 33.78 C ANISOU 168 CG GLU A 24 4425 4329 4081 7 -770 632 C ATOM 169 CD GLU A 24 21.670 -1.903 23.063 1.00 33.41 C ANISOU 169 CD GLU A 24 4435 4370 3891 -29 -749 542 C ATOM 170 OE1 GLU A 24 22.359 -0.879 23.262 1.00 31.29 O ANISOU 170 OE1 GLU A 24 4136 4131 3621 -36 -806 488 O ATOM 171 OE2 GLU A 24 20.428 -1.874 22.977 1.00 34.73 O ANISOU 171 OE2 GLU A 24 4668 4568 3960 -50 -675 524 O ATOM 172 N THR A 25 26.633 -4.509 23.559 1.00 38.28 N ANISOU 172 N THR A 25 4680 4739 5125 124 -1058 818 N ATOM 173 CA THR A 25 27.951 -4.862 23.050 1.00 37.74 C ANISOU 173 CA THR A 25 4475 4578 5288 170 -1074 833 C ATOM 174 C THR A 25 27.804 -5.342 21.609 1.00 37.59 C ANISOU 174 C THR A 25 4433 4455 5397 191 -902 767 C ATOM 175 O THR A 25 26.689 -5.584 21.152 1.00 34.74 O ANISOU 175 O THR A 25 4161 4093 4946 171 -801 733 O ATOM 176 CB THR A 25 28.617 -5.958 23.901 1.00 41.85 C ANISOU 176 CB THR A 25 4940 5059 5902 215 -1198 984 C ATOM 177 OG1 THR A 25 27.796 -7.132 23.893 1.00 41.44 O ANISOU 177 OG1 THR A 25 4954 4954 5839 230 -1136 1057 O ATOM 178 CG2 THR A 25 28.797 -5.485 25.335 1.00 43.39 C ANISOU 178 CG2 THR A 25 5166 5372 5947 190 -1380 1051 C ATOM 179 N ASP A 26 28.919 -5.477 20.894 1.00 40.86 N ANISOU 179 N ASP A 26 4724 4784 6016 228 -868 745 N ATOM 180 CA ASP A 26 28.880 -5.963 19.515 1.00 41.11 C ANISOU 180 CA ASP A 26 4737 4719 6165 248 -699 674 C ATOM 181 C ASP A 26 28.277 -7.365 19.451 1.00 38.62 C ANISOU 181 C ASP A 26 4465 4324 5886 272 -652 730 C ATOM 182 O ASP A 26 27.529 -7.687 18.531 1.00 37.82 O ANISOU 182 O ASP A 26 4423 4186 5761 257 -521 660 O ATOM 183 CB ASP A 26 30.280 -5.972 18.892 1.00 45.33 C ANISOU 183 CB ASP A 26 5123 5172 6931 289 -668 652 C ATOM 184 CG ASP A 26 30.827 -4.574 18.641 1.00 49.08 C ANISOU 184 CG ASP A 26 5551 5704 7394 256 -671 576 C ATOM 185 OD1 ASP A 26 30.036 -3.605 18.605 1.00 48.43 O ANISOU 185 OD1 ASP A 26 5561 5706 7134 204 -655 516 O ATOM 186 OD2 ASP A 26 32.057 -4.450 18.465 1.00 54.50 O ANISOU 186 OD2 ASP A 26 6100 6343 8265 283 -685 579 O ATOM 187 N GLN A 27 28.609 -8.190 20.438 1.00 39.84 N ANISOU 187 N GLN A 27 4589 4449 6098 306 -765 861 N ATOM 188 CA GLN A 27 28.099 -9.553 20.506 1.00 40.93 C ANISOU 188 CA GLN A 27 4761 4498 6292 329 -732 935 C ATOM 189 C GLN A 27 26.579 -9.567 20.642 1.00 39.30 C ANISOU 189 C GLN A 27 4697 4352 5882 273 -688 920 C ATOM 190 O GLN A 27 25.894 -10.337 19.971 1.00 34.61 O ANISOU 190 O GLN A 27 4145 3685 5321 267 -580 888 O ATOM 191 CB GLN A 27 28.742 -10.306 21.670 1.00 45.08 C ANISOU 191 CB GLN A 27 5231 4994 6903 374 -882 1102 C ATOM 192 CG GLN A 27 28.384 -11.779 21.708 1.00 52.17 C ANISOU 192 CG GLN A 27 6145 5769 7908 406 -844 1192 C ATOM 193 CD GLN A 27 28.663 -12.475 20.387 1.00 56.76 C ANISOU 193 CD GLN A 27 6671 6201 8696 440 -683 1098 C ATOM 194 OE1 GLN A 27 29.765 -12.378 19.841 1.00 58.66 O ANISOU 194 OE1 GLN A 27 6793 6380 9115 485 -656 1056 O ATOM 195 NE2 GLN A 27 27.659 -13.174 19.861 1.00 56.45 N ANISOU 195 NE2 GLN A 27 6714 6102 8631 415 -571 1057 N ATOM 196 N GLU A 28 26.057 -8.700 21.501 1.00 41.70 N ANISOU 196 N GLU A 28 5070 4790 5983 231 -770 937 N ATOM 197 CA GLU A 28 24.613 -8.602 21.699 1.00 41.96 C ANISOU 197 CA GLU A 28 5226 4891 5827 178 -726 923 C ATOM 198 C GLU A 28 23.887 -8.140 20.432 1.00 38.71 C ANISOU 198 C GLU A 28 4852 4479 5379 147 -586 781 C ATOM 199 O GLU A 28 22.769 -8.580 20.157 1.00 38.99 O ANISOU 199 O GLU A 28 4956 4505 5351 117 -514 765 O ATOM 200 CB GLU A 28 24.303 -7.663 22.865 1.00 44.41 C ANISOU 200 CB GLU A 28 5596 5345 5933 144 -832 953 C ATOM 201 CG GLU A 28 24.780 -8.204 24.207 1.00 50.89 C ANISOU 201 CG GLU A 28 6410 6188 6739 164 -978 1107 C ATOM 202 CD GLU A 28 24.466 -7.276 25.364 1.00 57.62 C ANISOU 202 CD GLU A 28 7334 7191 7368 124 -1077 1121 C ATOM 203 OE1 GLU A 28 23.902 -6.188 25.118 1.00 57.87 O ANISOU 203 OE1 GLU A 28 7412 7296 7278 85 -1026 1005 O ATOM 204 OE2 GLU A 28 24.783 -7.635 26.521 1.00 61.72 O ANISOU 204 OE2 GLU A 28 7866 7752 7832 131 -1204 1247 O ATOM 205 N ILE A 29 24.524 -7.261 19.662 1.00 34.60 N ANISOU 205 N ILE A 29 4282 3967 4899 150 -550 684 N ATOM 206 CA ILE A 29 23.985 -6.839 18.371 1.00 30.12 C ANISOU 206 CA ILE A 29 3743 3396 4303 125 -421 561 C ATOM 207 C ILE A 29 23.954 -8.008 17.379 1.00 30.89 C ANISOU 207 C ILE A 29 3829 3375 4535 143 -314 530 C ATOM 208 O ILE A 29 22.970 -8.204 16.664 1.00 28.99 O ANISOU 208 O ILE A 29 3653 3132 4231 109 -230 467 O ATOM 209 CB ILE A 29 24.806 -5.675 17.764 1.00 30.35 C ANISOU 209 CB ILE A 29 3717 3451 4362 127 -402 482 C ATOM 210 CG1 ILE A 29 24.723 -4.440 18.663 1.00 30.11 C ANISOU 210 CG1 ILE A 29 3709 3532 4199 100 -497 488 C ATOM 211 CG2 ILE A 29 24.303 -5.332 16.362 1.00 24.80 C ANISOU 211 CG2 ILE A 29 3050 2743 3631 104 -267 371 C ATOM 212 CD1 ILE A 29 23.322 -3.871 18.779 1.00 28.07 C ANISOU 212 CD1 ILE A 29 3556 3358 3753 55 -472 454 C ATOM 213 N ILE A 30 25.034 -8.784 17.342 1.00 30.04 N ANISOU 213 N ILE A 30 3634 3164 4617 195 -320 569 N ATOM 214 CA ILE A 30 25.102 -9.944 16.459 1.00 31.38 C ANISOU 214 CA ILE A 30 3787 3204 4933 217 -214 530 C ATOM 215 C ILE A 30 24.038 -10.976 16.844 1.00 32.62 C ANISOU 215 C ILE A 30 4014 3321 5058 195 -214 585 C ATOM 216 O ILE A 30 23.366 -11.530 15.974 1.00 33.18 O ANISOU 216 O ILE A 30 4130 3340 5138 170 -114 506 O ATOM 217 CB ILE A 30 26.504 -10.584 16.482 1.00 30.39 C ANISOU 217 CB ILE A 30 3539 2966 5042 287 -224 573 C ATOM 218 CG1 ILE A 30 27.529 -9.613 15.892 1.00 29.70 C ANISOU 218 CG1 ILE A 30 3373 2905 5009 301 -192 503 C ATOM 219 CG2 ILE A 30 26.514 -11.903 15.713 1.00 30.00 C ANISOU 219 CG2 ILE A 30 3479 2766 5156 313 -113 536 C ATOM 220 CD1 ILE A 30 28.968 -10.057 16.060 1.00 29.77 C ANISOU 220 CD1 ILE A 30 3238 2820 5254 370 -220 555 C ATOM 221 N ASP A 31 23.876 -11.214 18.144 1.00 32.72 N ANISOU 221 N ASP A 31 4040 3364 5029 199 -326 719 N ATOM 222 CA ASP A 31 22.836 -12.116 18.638 1.00 35.20 C ANISOU 222 CA ASP A 31 4422 3650 5304 172 -327 790 C ATOM 223 C ASP A 31 21.433 -11.635 18.250 1.00 32.74 C ANISOU 223 C ASP A 31 4202 3422 4817 103 -269 711 C ATOM 224 O ASP A 31 20.552 -12.442 17.965 1.00 29.83 O ANISOU 224 O ASP A 31 3875 2997 4462 71 -211 701 O ATOM 225 CB ASP A 31 22.921 -12.266 20.159 1.00 43.98 C ANISOU 225 CB ASP A 31 5540 4807 6362 183 -459 956 C ATOM 226 CG ASP A 31 24.187 -12.973 20.612 1.00 56.50 C ANISOU 226 CG ASP A 31 7031 6297 8139 254 -532 1063 C ATOM 227 OD1 ASP A 31 24.797 -13.700 19.797 1.00 61.57 O ANISOU 227 OD1 ASP A 31 7607 6802 8985 295 -459 1022 O ATOM 228 OD2 ASP A 31 24.569 -12.810 21.792 1.00 60.29 O ANISOU 228 OD2 ASP A 31 7502 6838 8566 268 -664 1189 O ATOM 229 N LEU A 32 21.231 -10.320 18.246 1.00 28.96 N ANISOU 229 N LEU A 32 3747 3070 4188 79 -287 657 N ATOM 230 CA LEU A 32 19.944 -9.758 17.859 1.00 29.42 C ANISOU 230 CA LEU A 32 3877 3208 4093 22 -238 586 C ATOM 231 C LEU A 32 19.668 -10.067 16.389 1.00 30.80 C ANISOU 231 C LEU A 32 4058 3322 4321 4 -128 462 C ATOM 232 O LEU A 32 18.543 -10.417 16.021 1.00 29.73 O ANISOU 232 O LEU A 32 3973 3188 4136 -42 -84 428 O ATOM 233 CB LEU A 32 19.902 -8.245 18.109 1.00 28.96 C ANISOU 233 CB LEU A 32 3834 3280 3890 10 -277 550 C ATOM 234 CG LEU A 32 18.516 -7.595 18.029 1.00 28.59 C ANISOU 234 CG LEU A 32 3854 3325 3684 -41 -246 507 C ATOM 235 CD1 LEU A 32 17.662 -8.028 19.203 1.00 31.75 C ANISOU 235 CD1 LEU A 32 4299 3762 4004 -64 -284 605 C ATOM 236 CD2 LEU A 32 18.612 -6.079 17.971 1.00 24.66 C ANISOU 236 CD2 LEU A 32 3360 2924 3086 -46 -263 449 C ATOM 237 N CYS A 33 20.701 -9.956 15.555 1.00 29.10 N ANISOU 237 N CYS A 33 3792 3057 4208 38 -84 396 N ATOM 238 CA CYS A 33 20.565 -10.285 14.140 1.00 29.92 C ANISOU 238 CA CYS A 33 3909 3106 4353 22 26 273 C ATOM 239 C CYS A 33 20.221 -11.767 13.952 1.00 30.81 C ANISOU 239 C CYS A 33 4031 3092 4582 15 70 273 C ATOM 240 O CYS A 33 19.409 -12.121 13.092 1.00 27.01 O ANISOU 240 O CYS A 33 3597 2594 4069 -31 135 183 O ATOM 241 CB CYS A 33 21.846 -9.930 13.378 1.00 30.43 C ANISOU 241 CB CYS A 33 3911 3137 4513 63 78 211 C ATOM 242 SG CYS A 33 22.177 -8.152 13.249 1.00 30.77 S ANISOU 242 SG CYS A 33 3948 3311 4434 56 55 183 S ATOM 243 N AARG A 34 20.846 -12.622 14.758 0.54 31.46 N ANISOU 243 N AARG A 34 4067 3083 4804 59 29 376 N ATOM 244 N BARG A 34 20.833 -12.620 14.768 0.46 31.56 N ANISOU 244 N BARG A 34 4080 3096 4814 58 28 377 N ATOM 245 CA AARG A 34 20.580 -14.057 14.727 0.54 33.40 C ANISOU 245 CA AARG A 34 4316 3188 5187 57 65 396 C ATOM 246 CA BARG A 34 20.586 -14.056 14.714 0.46 33.41 C ANISOU 246 CA BARG A 34 4317 3189 5188 57 66 395 C ATOM 247 C AARG A 34 19.138 -14.355 15.118 0.54 32.23 C ANISOU 247 C AARG A 34 4236 3073 4936 -9 50 429 C ATOM 248 C BARG A 34 19.157 -14.386 15.148 0.46 32.31 C ANISOU 248 C BARG A 34 4245 3080 4951 -8 49 433 C ATOM 249 O AARG A 34 18.476 -15.194 14.508 0.54 31.86 O ANISOU 249 O AARG A 34 4217 2946 4942 -48 113 366 O ATOM 250 O BARG A 34 18.519 -15.275 14.586 0.46 32.02 O ANISOU 250 O BARG A 34 4234 2956 4975 -45 110 377 O ATOM 251 CB AARG A 34 21.533 -14.808 15.663 0.54 36.55 C ANISOU 251 CB AARG A 34 4647 3490 5752 122 5 533 C ATOM 252 CB BARG A 34 21.598 -14.805 15.589 0.46 36.56 C ANISOU 252 CB BARG A 34 4644 3487 5761 125 10 525 C ATOM 253 CG AARG A 34 21.293 -16.316 15.712 0.54 40.19 C ANISOU 253 CG AARG A 34 5106 3785 6379 125 41 572 C ATOM 254 CG BARG A 34 21.532 -16.323 15.470 0.46 39.96 C ANISOU 254 CG BARG A 34 5063 3739 6380 136 60 545 C ATOM 255 CD AARG A 34 21.896 -16.961 16.964 0.54 43.50 C ANISOU 255 CD AARG A 34 5475 4138 6913 180 -52 760 C ATOM 256 CD BARG A 34 22.621 -17.017 16.296 0.46 43.08 C ANISOU 256 CD BARG A 34 5375 4028 6965 214 -2 687 C ATOM 257 NE AARG A 34 21.212 -16.538 18.186 0.54 44.24 N ANISOU 257 NE AARG A 34 5619 4354 6837 148 -151 891 N ATOM 258 NE BARG A 34 22.488 -16.759 17.728 0.46 43.99 N ANISOU 258 NE BARG A 34 5502 4229 6985 217 -133 862 N ATOM 259 CZ AARG A 34 20.208 -17.200 18.755 0.54 45.72 C ANISOU 259 CZ AARG A 34 5860 4519 6991 104 -155 975 C ATOM 260 CZ BARG A 34 23.298 -15.970 18.426 0.46 43.26 C ANISOU 260 CZ BARG A 34 5363 4226 6847 255 -234 935 C ATOM 261 NH1AARG A 34 19.762 -18.331 18.220 0.54 47.74 N ANISOU 261 NH1AARG A 34 6124 4629 7387 83 -75 940 N ATOM 262 NH1BARG A 34 24.315 -15.364 17.828 0.46 40.89 N ANISOU 262 NH1BARG A 34 4994 3934 6610 294 -215 854 N ATOM 263 NH2AARG A 34 19.650 -16.733 19.865 0.54 45.18 N ANISOU 263 NH2AARG A 34 5837 4574 6755 78 -231 1088 N ATOM 264 NH2BARG A 34 23.097 -15.791 19.725 0.46 44.09 N ANISOU 264 NH2BARG A 34 5494 4414 6843 249 -351 1085 N ATOM 265 N GLN A 35 18.658 -13.660 16.143 1.00 33.15 N ANISOU 265 N GLN A 35 4377 3309 4912 -24 -28 522 N ATOM 266 CA GLN A 35 17.302 -13.861 16.637 1.00 34.42 C ANISOU 266 CA GLN A 35 4592 3511 4975 -84 -36 566 C ATOM 267 C GLN A 35 16.247 -13.388 15.645 1.00 31.19 C ANISOU 267 C GLN A 35 4224 3166 4463 -146 18 437 C ATOM 268 O GLN A 35 15.172 -13.978 15.553 1.00 29.81 O ANISOU 268 O GLN A 35 4076 2966 4285 -201 44 429 O ATOM 269 CB GLN A 35 17.110 -13.144 17.968 1.00 40.01 C ANISOU 269 CB GLN A 35 5317 4339 5546 -82 -121 684 C ATOM 270 CG GLN A 35 17.867 -13.770 19.118 1.00 49.60 C ANISOU 270 CG GLN A 35 6506 5502 6838 -36 -193 841 C ATOM 271 CD GLN A 35 17.792 -12.924 20.371 1.00 57.65 C ANISOU 271 CD GLN A 35 7553 6660 7693 -36 -280 935 C ATOM 272 OE1 GLN A 35 17.025 -11.960 20.436 1.00 56.84 O ANISOU 272 OE1 GLN A 35 7489 6677 7428 -73 -272 885 O ATOM 273 NE2 GLN A 35 18.594 -13.273 21.373 1.00 64.07 N ANISOU 273 NE2 GLN A 35 8344 7455 8545 6 -366 1070 N ATOM 274 N ALA A 36 16.552 -12.322 14.909 1.00 29.20 N ANISOU 274 N ALA A 36 3971 2992 4130 -138 31 344 N ATOM 275 CA ALA A 36 15.637 -11.821 13.887 1.00 28.14 C ANISOU 275 CA ALA A 36 3873 2923 3895 -190 72 230 C ATOM 276 C ALA A 36 15.365 -12.901 12.842 1.00 28.74 C ANISOU 276 C ALA A 36 3961 2891 4066 -224 140 132 C ATOM 277 O ALA A 36 14.289 -12.945 12.252 1.00 30.84 O ANISOU 277 O ALA A 36 4259 3188 4270 -285 156 65 O ATOM 278 CB ALA A 36 16.195 -10.571 13.227 1.00 23.31 C ANISOU 278 CB ALA A 36 3258 2395 3204 -169 79 161 C ATOM 279 N LYS A 37 16.350 -13.763 12.615 1.00 26.19 N ANISOU 279 N LYS A 37 3610 2439 3902 -184 178 118 N ATOM 280 CA LYS A 37 16.148 -14.952 11.795 1.00 30.83 C ANISOU 280 CA LYS A 37 4210 2898 4606 -214 247 27 C ATOM 281 C LYS A 37 15.647 -16.090 12.682 1.00 31.26 C ANISOU 281 C LYS A 37 4257 2850 4769 -232 227 129 C ATOM 282 O LYS A 37 16.429 -16.918 13.152 1.00 33.59 O ANISOU 282 O LYS A 37 4516 3020 5225 -183 232 198 O ATOM 283 CB LYS A 37 17.441 -15.342 11.085 1.00 31.44 C ANISOU 283 CB LYS A 37 4256 2873 4817 -159 316 -47 C ATOM 284 CG LYS A 37 17.280 -16.435 10.047 1.00 35.76 C ANISOU 284 CG LYS A 37 4826 3293 5467 -192 403 -182 C ATOM 285 CD LYS A 37 18.613 -16.698 9.368 1.00 41.61 C ANISOU 285 CD LYS A 37 5531 3942 6336 -130 488 -259 C ATOM 286 CE LYS A 37 18.441 -17.460 8.065 1.00 45.25 C ANISOU 286 CE LYS A 37 6036 4317 6839 -171 592 -441 C ATOM 287 NZ LYS A 37 19.717 -17.469 7.298 1.00 44.70 N ANISOU 287 NZ LYS A 37 5936 4191 6857 -113 694 -531 N ATOM 288 N SER A 38 14.338 -16.112 12.911 1.00 32.00 N ANISOU 288 N SER A 38 4380 2995 4783 -301 206 146 N ATOM 289 CA SER A 38 13.725 -17.005 13.896 1.00 32.74 C ANISOU 289 CA SER A 38 4469 3019 4952 -326 187 267 C ATOM 290 C SER A 38 13.215 -18.306 13.275 1.00 32.32 C ANISOU 290 C SER A 38 4423 2815 5044 -382 243 193 C ATOM 291 O SER A 38 12.979 -18.359 12.067 1.00 33.48 O ANISOU 291 O SER A 38 4590 2952 5177 -421 284 31 O ATOM 292 CB SER A 38 12.566 -16.282 14.590 1.00 33.91 C ANISOU 292 CB SER A 38 4634 3306 4943 -372 145 335 C ATOM 293 OG SER A 38 11.344 -16.521 13.909 1.00 32.30 O ANISOU 293 OG SER A 38 4444 3110 4718 -455 169 246 O ATOM 294 N PRO A 39 13.013 -19.351 14.104 1.00 32.90 N ANISOU 294 N PRO A 39 4482 2769 5248 -390 242 311 N ATOM 295 CA PRO A 39 12.451 -20.627 13.642 1.00 34.57 C ANISOU 295 CA PRO A 39 4697 2822 5618 -451 293 251 C ATOM 296 C PRO A 39 11.089 -20.493 12.964 1.00 37.67 C ANISOU 296 C PRO A 39 5112 3279 5923 -554 298 140 C ATOM 297 O PRO A 39 10.674 -21.412 12.252 1.00 38.57 O ANISOU 297 O PRO A 39 5231 3273 6150 -614 339 33 O ATOM 298 CB PRO A 39 12.308 -21.439 14.934 1.00 34.73 C ANISOU 298 CB PRO A 39 4700 2752 5746 -446 275 448 C ATOM 299 CG PRO A 39 13.294 -20.868 15.855 1.00 36.24 C ANISOU 299 CG PRO A 39 4875 3005 5889 -357 221 586 C ATOM 300 CD PRO A 39 13.396 -19.411 15.527 1.00 34.22 C ANISOU 300 CD PRO A 39 4632 2939 5430 -342 191 512 C ATOM 301 N ALA A 40 10.399 -19.380 13.196 1.00 34.79 N ANISOU 301 N ALA A 40 4754 3095 5371 -574 255 164 N ATOM 302 CA ALA A 40 9.077 -19.171 12.612 1.00 35.20 C ANISOU 302 CA ALA A 40 4811 3220 5345 -666 246 76 C ATOM 303 C ALA A 40 9.117 -18.119 11.506 1.00 33.11 C ANISOU 303 C ALA A 40 4568 3084 4927 -665 231 -64 C ATOM 304 O ALA A 40 8.081 -17.595 11.102 1.00 34.86 O ANISOU 304 O ALA A 40 4788 3411 5046 -724 202 -115 O ATOM 305 CB ALA A 40 8.078 -18.774 13.688 1.00 31.82 C ANISOU 305 CB ALA A 40 4363 2888 4839 -696 218 212 C ATOM 306 N GLY A 41 10.314 -17.816 11.018 1.00 29.79 N ANISOU 306 N GLY A 41 4163 2656 4501 -597 252 -119 N ATOM 307 CA GLY A 41 10.466 -16.874 9.927 1.00 29.68 C ANISOU 307 CA GLY A 41 4177 2753 4348 -595 250 -242 C ATOM 308 C GLY A 41 11.235 -15.634 10.333 1.00 29.18 C ANISOU 308 C GLY A 41 4107 2803 4176 -518 227 -174 C ATOM 309 O GLY A 41 11.578 -15.457 11.500 1.00 34.82 O ANISOU 309 O GLY A 41 4799 3525 4907 -471 202 -37 O ATOM 310 N GLU A 42 11.504 -14.770 9.364 1.00 27.23 N ANISOU 310 N GLU A 42 3884 2645 3815 -509 234 -269 N ATOM 311 CA GLU A 42 12.277 -13.560 9.617 1.00 30.29 C ANISOU 311 CA GLU A 42 4265 3130 4114 -443 219 -219 C ATOM 312 C GLU A 42 11.395 -12.387 10.030 1.00 28.45 C ANISOU 312 C GLU A 42 4029 3046 3735 -457 160 -162 C ATOM 313 O GLU A 42 10.282 -12.223 9.530 1.00 27.16 O ANISOU 313 O GLU A 42 3875 2943 3501 -517 138 -208 O ATOM 314 CB GLU A 42 13.088 -13.187 8.375 1.00 34.11 C ANISOU 314 CB GLU A 42 4775 3627 4558 -424 270 -339 C ATOM 315 CG GLU A 42 13.847 -14.368 7.788 1.00 43.02 C ANISOU 315 CG GLU A 42 5909 4606 5832 -415 346 -428 C ATOM 316 CD GLU A 42 14.645 -14.003 6.554 1.00 49.64 C ANISOU 316 CD GLU A 42 6777 5463 6621 -399 416 -550 C ATOM 317 OE1 GLU A 42 14.625 -12.820 6.157 1.00 51.82 O ANISOU 317 OE1 GLU A 42 7071 5869 6750 -395 400 -552 O ATOM 318 OE2 GLU A 42 15.296 -14.902 5.983 1.00 53.76 O ANISOU 318 OE2 GLU A 42 7304 5865 7255 -389 496 -642 O ATOM 319 N THR A 43 11.897 -11.573 10.951 1.00 28.59 N ANISOU 319 N THR A 43 4028 3120 3715 -402 133 -64 N ATOM 320 CA THR A 43 11.233 -10.319 11.267 1.00 27.14 C ANISOU 320 CA THR A 43 3843 3072 3399 -404 91 -27 C ATOM 321 C THR A 43 11.451 -9.381 10.089 1.00 27.68 C ANISOU 321 C THR A 43 3931 3210 3374 -400 100 -114 C ATOM 322 O THR A 43 12.294 -9.648 9.232 1.00 26.26 O ANISOU 322 O THR A 43 3768 2983 3228 -386 144 -188 O ATOM 323 CB THR A 43 11.761 -9.681 12.571 1.00 26.57 C ANISOU 323 CB THR A 43 3753 3038 3306 -351 59 84 C ATOM 324 OG1 THR A 43 13.156 -9.371 12.437 1.00 26.49 O ANISOU 324 OG1 THR A 43 3734 3003 3330 -293 69 76 O ATOM 325 CG2 THR A 43 11.554 -10.626 13.752 1.00 28.36 C ANISOU 325 CG2 THR A 43 3968 3201 3605 -356 50 187 C ATOM 326 N ALA A 44 10.677 -8.300 10.033 1.00 29.32 N ANISOU 326 N ALA A 44 4138 3529 3472 -410 65 -102 N ATOM 327 CA ALA A 44 10.838 -7.291 8.984 1.00 28.41 C ANISOU 327 CA ALA A 44 4045 3488 3263 -404 68 -158 C ATOM 328 C ALA A 44 12.178 -6.576 9.100 1.00 28.42 C ANISOU 328 C ALA A 44 4041 3486 3269 -343 91 -140 C ATOM 329 O ALA A 44 12.812 -6.236 8.095 1.00 29.72 O ANISOU 329 O ALA A 44 4227 3659 3405 -334 127 -197 O ATOM 330 CB ALA A 44 9.705 -6.277 9.045 1.00 20.79 C ANISOU 330 CB ALA A 44 3067 2629 2204 -420 21 -129 C ATOM 331 N ALA A 45 12.599 -6.348 10.338 1.00 26.42 N ANISOU 331 N ALA A 45 3761 3227 3051 -304 69 -58 N ATOM 332 CA ALA A 45 13.764 -5.521 10.605 1.00 28.07 C ANISOU 332 CA ALA A 45 3953 3444 3267 -253 72 -34 C ATOM 333 C ALA A 45 14.258 -5.675 12.037 1.00 25.05 C ANISOU 333 C ALA A 45 3544 3037 2936 -220 35 50 C ATOM 334 O ALA A 45 13.619 -6.325 12.866 1.00 24.43 O ANISOU 334 O ALA A 45 3465 2946 2870 -236 13 102 O ATOM 335 CB ALA A 45 13.436 -4.045 10.321 1.00 29.23 C ANISOU 335 CB ALA A 45 4106 3685 3313 -248 55 -34 C ATOM 336 N ILE A 46 15.410 -5.076 12.308 1.00 23.63 N ANISOU 336 N ILE A 46 3340 2855 2784 -178 28 67 N ATOM 337 CA ILE A 46 15.877 -4.857 13.669 1.00 25.11 C ANISOU 337 CA ILE A 46 3504 3051 2984 -150 -28 145 C ATOM 338 C ILE A 46 15.934 -3.348 13.913 1.00 26.10 C ANISOU 338 C ILE A 46 3628 3256 3031 -139 -54 142 C ATOM 339 O ILE A 46 15.953 -2.569 12.963 1.00 27.96 O ANISOU 339 O ILE A 46 3869 3516 3237 -143 -22 92 O ATOM 340 CB ILE A 46 17.261 -5.477 13.917 1.00 26.42 C ANISOU 340 CB ILE A 46 3629 3137 3273 -110 -33 170 C ATOM 341 CG1 ILE A 46 18.297 -4.822 13.002 1.00 26.39 C ANISOU 341 CG1 ILE A 46 3597 3123 3307 -89 8 113 C ATOM 342 CG2 ILE A 46 17.222 -6.994 13.708 1.00 26.68 C ANISOU 342 CG2 ILE A 46 3661 3070 3406 -115 -2 173 C ATOM 343 CD1 ILE A 46 19.716 -5.193 13.328 1.00 30.52 C ANISOU 343 CD1 ILE A 46 4057 3577 3962 -45 -3 142 C ATOM 344 N CYS A 47 15.952 -2.930 15.173 1.00 23.70 N ANISOU 344 N CYS A 47 3322 2990 2691 -128 -109 195 N ATOM 345 CA CYS A 47 16.056 -1.510 15.483 1.00 22.99 C ANISOU 345 CA CYS A 47 3230 2962 2542 -120 -133 182 C ATOM 346 C CYS A 47 17.037 -1.308 16.627 1.00 22.96 C ANISOU 346 C CYS A 47 3206 2960 2559 -98 -198 222 C ATOM 347 O CYS A 47 16.862 -1.859 17.719 1.00 25.24 O ANISOU 347 O CYS A 47 3509 3262 2821 -99 -241 280 O ATOM 348 CB CYS A 47 14.693 -0.909 15.832 1.00 20.49 C ANISOU 348 CB CYS A 47 2944 2715 2126 -140 -131 180 C ATOM 349 SG CYS A 47 14.744 0.882 16.109 1.00 25.71 S ANISOU 349 SG CYS A 47 3603 3431 2733 -128 -146 149 S ATOM 350 N ILE A 48 18.076 -0.524 16.356 1.00 21.23 N ANISOU 350 N ILE A 48 2950 2729 2385 -82 -208 194 N ATOM 351 CA ILE A 48 19.208 -0.364 17.259 1.00 21.18 C ANISOU 351 CA ILE A 48 2907 2717 2424 -63 -280 224 C ATOM 352 C ILE A 48 19.726 1.070 17.208 1.00 21.12 C ANISOU 352 C ILE A 48 2878 2733 2414 -66 -294 178 C ATOM 353 O ILE A 48 19.325 1.839 16.346 1.00 21.74 O ANISOU 353 O ILE A 48 2968 2819 2473 -74 -238 135 O ATOM 354 CB ILE A 48 20.358 -1.327 16.887 1.00 24.11 C ANISOU 354 CB ILE A 48 3221 3008 2933 -38 -277 246 C ATOM 355 CG1 ILE A 48 20.845 -1.043 15.462 1.00 23.65 C ANISOU 355 CG1 ILE A 48 3133 2908 2944 -34 -192 185 C ATOM 356 CG2 ILE A 48 19.914 -2.785 17.012 1.00 23.37 C ANISOU 356 CG2 ILE A 48 3145 2870 2865 -35 -265 294 C ATOM 357 CD1 ILE A 48 21.865 -2.042 14.932 1.00 21.30 C ANISOU 357 CD1 ILE A 48 2779 2523 2790 -7 -157 190 C ATOM 358 N PHE A 49 20.621 1.434 18.123 1.00 23.44 N ANISOU 358 N PHE A 49 3140 3036 2731 -60 -375 192 N ATOM 359 CA PHE A 49 21.218 2.768 18.088 1.00 22.71 C ANISOU 359 CA PHE A 49 3018 2950 2660 -69 -391 143 C ATOM 360 C PHE A 49 22.223 2.848 16.933 1.00 22.85 C ANISOU 360 C PHE A 49 2970 2903 2808 -58 -335 125 C ATOM 361 O PHE A 49 22.813 1.835 16.553 1.00 20.99 O ANISOU 361 O PHE A 49 2695 2619 2660 -39 -316 152 O ATOM 362 CB PHE A 49 21.865 3.116 19.441 1.00 25.11 C ANISOU 362 CB PHE A 49 3308 3287 2944 -75 -505 153 C ATOM 363 CG PHE A 49 20.867 3.576 20.479 1.00 26.13 C ANISOU 363 CG PHE A 49 3513 3491 2925 -93 -535 139 C ATOM 364 CD1 PHE A 49 20.097 4.712 20.260 1.00 24.71 C ANISOU 364 CD1 PHE A 49 3366 3331 2690 -106 -486 76 C ATOM 365 CD2 PHE A 49 20.682 2.867 21.658 1.00 25.71 C ANISOU 365 CD2 PHE A 49 3496 3485 2789 -95 -604 193 C ATOM 366 CE1 PHE A 49 19.158 5.142 21.206 1.00 24.54 C ANISOU 366 CE1 PHE A 49 3409 3374 2541 -119 -496 54 C ATOM 367 CE2 PHE A 49 19.744 3.292 22.605 1.00 26.48 C ANISOU 367 CE2 PHE A 49 3667 3656 2740 -113 -612 175 C ATOM 368 CZ PHE A 49 18.986 4.433 22.377 1.00 23.10 C ANISOU 368 CZ PHE A 49 3267 3245 2266 -124 -553 98 C ATOM 369 N PRO A 50 22.391 4.051 16.350 1.00 24.32 N ANISOU 369 N PRO A 50 3143 3085 3012 -72 -297 81 N ATOM 370 CA PRO A 50 23.143 4.244 15.104 1.00 22.02 C ANISOU 370 CA PRO A 50 2803 2741 2821 -68 -215 66 C ATOM 371 C PRO A 50 24.551 3.644 15.080 1.00 23.08 C ANISOU 371 C PRO A 50 2846 2821 3101 -51 -229 84 C ATOM 372 O PRO A 50 24.954 3.117 14.044 1.00 24.36 O ANISOU 372 O PRO A 50 2983 2940 3335 -38 -140 80 O ATOM 373 CB PRO A 50 23.220 5.773 14.982 1.00 23.45 C ANISOU 373 CB PRO A 50 2979 2926 3005 -89 -208 32 C ATOM 374 CG PRO A 50 21.965 6.259 15.652 1.00 25.13 C ANISOU 374 CG PRO A 50 3264 3192 3091 -98 -239 18 C ATOM 375 CD PRO A 50 21.741 5.300 16.802 1.00 24.62 C ANISOU 375 CD PRO A 50 3220 3162 2971 -90 -315 45 C ATOM 376 N ARG A 51 25.288 3.722 16.182 1.00 22.34 N ANISOU 376 N ARG A 51 2703 2732 3054 -50 -336 100 N ATOM 377 CA ARG A 51 26.683 3.295 16.162 1.00 22.95 C ANISOU 377 CA ARG A 51 2671 2755 3294 -32 -358 121 C ATOM 378 C ARG A 51 26.832 1.783 15.971 1.00 25.70 C ANISOU 378 C ARG A 51 3002 3062 3701 5 -335 163 C ATOM 379 O ARG A 51 27.916 1.300 15.652 1.00 26.79 O ANISOU 379 O ARG A 51 3046 3140 3994 30 -315 177 O ATOM 380 CB ARG A 51 27.394 3.737 17.441 1.00 23.36 C ANISOU 380 CB ARG A 51 2672 2830 3374 -44 -502 131 C ATOM 381 CG ARG A 51 26.970 3.023 18.725 1.00 26.65 C ANISOU 381 CG ARG A 51 3135 3297 3694 -36 -618 180 C ATOM 382 CD ARG A 51 27.644 3.718 19.908 1.00 29.46 C ANISOU 382 CD ARG A 51 3453 3691 4049 -61 -764 173 C ATOM 383 NE ARG A 51 27.299 3.156 21.209 1.00 31.03 N ANISOU 383 NE ARG A 51 3705 3953 4132 -59 -882 223 N ATOM 384 CZ ARG A 51 26.181 3.434 21.875 1.00 31.75 C ANISOU 384 CZ ARG A 51 3907 4115 4042 -79 -894 206 C ATOM 385 NH1 ARG A 51 25.276 4.256 21.356 1.00 26.01 N ANISOU 385 NH1 ARG A 51 3241 3397 3243 -97 -800 141 N ATOM 386 NH2 ARG A 51 25.961 2.874 23.061 1.00 33.63 N ANISOU 386 NH2 ARG A 51 4192 4413 4172 -79 -995 262 N ATOM 387 N PHE A 52 25.741 1.044 16.150 1.00 26.45 N ANISOU 387 N PHE A 52 3182 3181 3687 9 -331 182 N ATOM 388 CA PHE A 52 25.765 -0.411 16.009 1.00 25.36 C ANISOU 388 CA PHE A 52 3036 2992 3608 40 -308 221 C ATOM 389 C PHE A 52 25.453 -0.881 14.590 1.00 26.41 C ANISOU 389 C PHE A 52 3194 3082 3760 43 -166 174 C ATOM 390 O PHE A 52 25.594 -2.067 14.277 1.00 27.69 O ANISOU 390 O PHE A 52 3342 3182 3997 68 -126 185 O ATOM 391 CB PHE A 52 24.784 -1.050 16.996 1.00 24.13 C ANISOU 391 CB PHE A 52 2955 2876 3338 36 -377 272 C ATOM 392 CG PHE A 52 25.112 -0.759 18.431 1.00 24.06 C ANISOU 392 CG PHE A 52 2934 2916 3291 32 -518 321 C ATOM 393 CD1 PHE A 52 26.270 -1.260 19.004 1.00 25.22 C ANISOU 393 CD1 PHE A 52 2993 3028 3561 61 -605 379 C ATOM 394 CD2 PHE A 52 24.282 0.040 19.198 1.00 23.80 C ANISOU 394 CD2 PHE A 52 2975 2968 3101 1 -565 307 C ATOM 395 CE1 PHE A 52 26.589 -0.981 20.326 1.00 27.62 C ANISOU 395 CE1 PHE A 52 3292 3390 3814 52 -750 425 C ATOM 396 CE2 PHE A 52 24.591 0.320 20.517 1.00 23.99 C ANISOU 396 CE2 PHE A 52 3000 3046 3068 -8 -693 340 C ATOM 397 CZ PHE A 52 25.743 -0.192 21.084 1.00 24.61 C ANISOU 397 CZ PHE A 52 2999 3099 3253 15 -793 401 C ATOM 398 N ILE A 53 25.061 0.049 13.727 1.00 25.97 N ANISOU 398 N ILE A 53 3176 3056 3637 17 -93 122 N ATOM 399 CA ILE A 53 24.648 -0.297 12.367 1.00 28.06 C ANISOU 399 CA ILE A 53 3482 3302 3878 11 32 76 C ATOM 400 C ILE A 53 25.736 -1.011 11.529 1.00 28.96 C ANISOU 400 C ILE A 53 3527 3335 4140 38 126 52 C ATOM 401 O ILE A 53 25.429 -1.991 10.843 1.00 28.96 O ANISOU 401 O ILE A 53 3560 3298 4144 44 199 21 O ATOM 402 CB ILE A 53 24.138 0.969 11.613 1.00 26.91 C ANISOU 402 CB ILE A 53 3383 3207 3635 -20 83 42 C ATOM 403 CG1 ILE A 53 22.861 1.496 12.279 1.00 26.77 C ANISOU 403 CG1 ILE A 53 3437 3259 3477 -40 15 55 C ATOM 404 CG2 ILE A 53 23.855 0.657 10.145 1.00 26.41 C ANISOU 404 CG2 ILE A 53 3363 3135 3536 -29 206 -3 C ATOM 405 CD1 ILE A 53 22.371 2.835 11.733 1.00 25.48 C ANISOU 405 CD1 ILE A 53 3308 3136 3239 -63 45 37 C ATOM 406 N PRO A 54 27.003 -0.545 11.579 1.00 28.99 N ANISOU 406 N PRO A 54 3431 3307 4276 52 129 59 N ATOM 407 CA PRO A 54 27.995 -1.271 10.773 1.00 29.55 C ANISOU 407 CA PRO A 54 3429 3299 4498 82 236 33 C ATOM 408 C PRO A 54 28.204 -2.727 11.202 1.00 30.85 C ANISOU 408 C PRO A 54 3562 3392 4768 124 212 58 C ATOM 409 O PRO A 54 28.339 -3.591 10.332 1.00 25.22 O ANISOU 409 O PRO A 54 2852 2617 4114 141 325 12 O ATOM 410 CB PRO A 54 29.273 -0.456 10.983 1.00 30.04 C ANISOU 410 CB PRO A 54 3374 3344 4696 88 220 50 C ATOM 411 CG PRO A 54 28.780 0.919 11.285 1.00 30.25 C ANISOU 411 CG PRO A 54 3444 3443 4606 45 164 53 C ATOM 412 CD PRO A 54 27.569 0.699 12.131 1.00 27.28 C ANISOU 412 CD PRO A 54 3162 3120 4084 37 64 75 C ATOM 413 N VAL A 55 28.229 -2.991 12.508 1.00 29.83 N ANISOU 413 N VAL A 55 3407 3268 4658 139 70 131 N ATOM 414 CA VAL A 55 28.327 -4.362 13.018 1.00 30.60 C ANISOU 414 CA VAL A 55 3481 3296 4851 179 34 178 C ATOM 415 C VAL A 55 27.112 -5.209 12.600 1.00 31.37 C ANISOU 415 C VAL A 55 3688 3383 4850 163 88 149 C ATOM 416 O VAL A 55 27.254 -6.373 12.201 1.00 29.77 O ANISOU 416 O VAL A 55 3472 3089 4750 190 152 133 O ATOM 417 CB VAL A 55 28.460 -4.376 14.562 1.00 32.24 C ANISOU 417 CB VAL A 55 3659 3532 5057 189 -141 276 C ATOM 418 CG1 VAL A 55 28.157 -5.764 15.131 1.00 34.73 C ANISOU 418 CG1 VAL A 55 3989 3788 5417 220 -182 344 C ATOM 419 CG2 VAL A 55 29.847 -3.919 14.982 1.00 33.79 C ANISOU 419 CG2 VAL A 55 3722 3712 5407 213 -206 307 C ATOM 420 N ALA A 56 25.924 -4.617 12.691 1.00 30.82 N ANISOU 420 N ALA A 56 3717 3400 4592 117 62 138 N ATOM 421 CA ALA A 56 24.693 -5.297 12.303 1.00 30.44 C ANISOU 421 CA ALA A 56 3765 3354 4447 92 102 109 C ATOM 422 C ALA A 56 24.668 -5.594 10.808 1.00 31.05 C ANISOU 422 C ALA A 56 3870 3395 4533 82 246 11 C ATOM 423 O ALA A 56 24.238 -6.670 10.396 1.00 31.21 O ANISOU 423 O ALA A 56 3925 3357 4577 79 295 -24 O ATOM 424 CB ALA A 56 23.471 -4.460 12.691 1.00 25.89 C ANISOU 424 CB ALA A 56 3271 2882 3683 48 47 118 C ATOM 425 N LYS A 57 25.125 -4.638 10.002 1.00 29.52 N ANISOU 425 N LYS A 57 3664 3236 4316 72 313 -35 N ATOM 426 CA LYS A 57 25.123 -4.806 8.553 1.00 32.57 C ANISOU 426 CA LYS A 57 4088 3607 4679 57 453 -127 C ATOM 427 C LYS A 57 25.981 -6.006 8.155 1.00 31.28 C ANISOU 427 C LYS A 57 3869 3328 4688 97 541 -166 C ATOM 428 O LYS A 57 25.590 -6.811 7.309 1.00 30.83 O ANISOU 428 O LYS A 57 3868 3233 4614 84 629 -244 O ATOM 429 CB LYS A 57 25.620 -3.539 7.855 1.00 36.73 C ANISOU 429 CB LYS A 57 4603 4187 5166 43 513 -145 C ATOM 430 CG LYS A 57 24.937 -3.268 6.523 1.00 42.00 C ANISOU 430 CG LYS A 57 5366 4905 5687 3 610 -215 C ATOM 431 CD LYS A 57 24.893 -1.772 6.215 1.00 48.35 C ANISOU 431 CD LYS A 57 6185 5787 6398 -22 612 -190 C ATOM 432 CE LYS A 57 23.780 -1.434 5.227 1.00 51.49 C ANISOU 432 CE LYS A 57 6694 6260 6609 -66 644 -224 C ATOM 433 NZ LYS A 57 23.934 -2.174 3.936 1.00 55.78 N ANISOU 433 NZ LYS A 57 7284 6785 7125 -77 775 -310 N ATOM 434 N LYS A 58 27.139 -6.126 8.791 1.00 29.92 N ANISOU 434 N LYS A 58 3582 3096 4690 145 513 -114 N ATOM 435 CA LYS A 58 28.042 -7.244 8.549 1.00 30.09 C ANISOU 435 CA LYS A 58 3526 2994 4912 196 589 -138 C ATOM 436 C LYS A 58 27.411 -8.576 8.986 1.00 30.96 C ANISOU 436 C LYS A 58 3671 3029 5062 207 552 -123 C ATOM 437 O LYS A 58 27.457 -9.571 8.257 1.00 33.43 O ANISOU 437 O LYS A 58 3998 3253 5452 218 659 -200 O ATOM 438 CB LYS A 58 29.370 -7.005 9.276 1.00 31.15 C ANISOU 438 CB LYS A 58 3515 3089 5231 246 536 -67 C ATOM 439 CG LYS A 58 30.421 -8.079 9.039 1.00 35.52 C ANISOU 439 CG LYS A 58 3963 3507 6025 309 618 -83 C ATOM 440 CD LYS A 58 31.795 -7.620 9.523 1.00 38.24 C ANISOU 440 CD LYS A 58 4148 3827 6553 352 579 -23 C ATOM 441 N ALA A 59 26.806 -8.584 10.168 1.00 29.85 N ANISOU 441 N ALA A 59 3549 2924 4867 200 409 -28 N ATOM 442 CA ALA A 59 26.171 -9.784 10.698 1.00 31.43 C ANISOU 442 CA ALA A 59 3782 3056 5105 204 368 10 C ATOM 443 C ALA A 59 25.011 -10.255 9.809 1.00 34.36 C ANISOU 443 C ALA A 59 4264 3429 5363 152 444 -86 C ATOM 444 O ALA A 59 24.874 -11.453 9.533 1.00 34.12 O ANISOU 444 O ALA A 59 4243 3290 5431 160 498 -124 O ATOM 445 CB ALA A 59 25.685 -9.535 12.119 1.00 30.11 C ANISOU 445 CB ALA A 59 3625 2950 4864 197 209 134 C ATOM 446 N LEU A 60 24.188 -9.312 9.356 1.00 30.23 N ANISOU 446 N LEU A 60 3818 3023 4644 98 445 -126 N ATOM 447 CA LEU A 60 23.044 -9.637 8.511 1.00 32.13 C ANISOU 447 CA LEU A 60 4159 3285 4764 42 495 -214 C ATOM 448 C LEU A 60 23.463 -10.170 7.142 1.00 33.50 C ANISOU 448 C LEU A 60 4350 3396 4984 40 643 -346 C ATOM 449 O LEU A 60 22.807 -11.051 6.583 1.00 33.55 O ANISOU 449 O LEU A 60 4415 3355 4978 8 688 -425 O ATOM 450 CB LEU A 60 22.143 -8.417 8.342 1.00 31.44 C ANISOU 450 CB LEU A 60 4137 3339 4470 -7 453 -214 C ATOM 451 CG LEU A 60 21.354 -8.090 9.609 1.00 32.83 C ANISOU 451 CG LEU A 60 4322 3575 4576 -19 326 -112 C ATOM 452 CD1 LEU A 60 20.564 -6.801 9.449 1.00 30.82 C ANISOU 452 CD1 LEU A 60 4117 3448 4145 -56 293 -113 C ATOM 453 CD2 LEU A 60 20.436 -9.258 9.967 1.00 34.53 C ANISOU 453 CD2 LEU A 60 4573 3736 4811 -43 303 -99 C ATOM 454 N LYS A 61 24.557 -9.638 6.610 1.00 33.45 N ANISOU 454 N LYS A 61 4290 3388 5030 71 723 -374 N ATOM 455 CA LYS A 61 25.080 -10.099 5.332 1.00 34.55 C ANISOU 455 CA LYS A 61 4443 3472 5212 74 882 -501 C ATOM 456 C LYS A 61 25.609 -11.523 5.448 1.00 36.52 C ANISOU 456 C LYS A 61 4640 3559 5675 119 936 -532 C ATOM 457 O LYS A 61 25.368 -12.358 4.574 1.00 39.04 O ANISOU 457 O LYS A 61 5014 3815 6003 99 1038 -653 O ATOM 458 CB LYS A 61 26.187 -9.163 4.833 1.00 36.22 C ANISOU 458 CB LYS A 61 4596 3718 5448 97 964 -508 C ATOM 459 N ALA A 62 26.324 -11.790 6.538 1.00 37.12 N ANISOU 459 N ALA A 62 4612 3566 5927 179 863 -422 N ATOM 460 CA ALA A 62 26.936 -13.096 6.782 1.00 39.54 C ANISOU 460 CA ALA A 62 4848 3706 6471 236 902 -421 C ATOM 461 C ALA A 62 25.911 -14.229 6.887 1.00 40.61 C ANISOU 461 C ALA A 62 5056 3766 6608 204 882 -446 C ATOM 462 O ALA A 62 26.174 -15.349 6.459 1.00 41.28 O ANISOU 462 O ALA A 62 5129 3709 6848 227 976 -522 O ATOM 463 CB ALA A 62 27.783 -13.044 8.044 1.00 31.35 C ANISOU 463 CB ALA A 62 3687 2632 5593 301 790 -269 C ATOM 464 N GLN A 63 24.748 -13.938 7.464 1.00 40.44 N ANISOU 464 N GLN A 63 5104 3832 6427 151 767 -384 N ATOM 465 CA GLN A 63 23.692 -14.940 7.597 1.00 40.47 C ANISOU 465 CA GLN A 63 5172 3774 6431 109 745 -400 C ATOM 466 C GLN A 63 22.731 -14.886 6.410 1.00 43.18 C ANISOU 466 C GLN A 63 5626 4175 6605 30 811 -549 C ATOM 467 O GLN A 63 21.683 -15.538 6.413 1.00 42.99 O ANISOU 467 O GLN A 63 5661 4125 6547 -24 784 -576 O ATOM 468 CB GLN A 63 22.922 -14.743 8.908 1.00 36.16 C ANISOU 468 CB GLN A 63 4634 3287 5817 92 593 -248 C ATOM 469 CG GLN A 63 22.171 -13.426 8.997 1.00 33.67 C ANISOU 469 CG GLN A 63 4373 3153 5268 44 525 -227 C ATOM 470 CD GLN A 63 21.357 -13.303 10.274 1.00 33.12 C ANISOU 470 CD GLN A 63 4317 3138 5130 25 396 -94 C ATOM 471 OE1 GLN A 63 21.788 -13.740 11.342 1.00 36.52 O ANISOU 471 OE1 GLN A 63 4694 3512 5671 68 330 27 O ATOM 472 NE2 GLN A 63 20.173 -12.709 10.169 1.00 27.26 N ANISOU 472 NE2 GLN A 63 3645 2508 4206 -38 362 -110 N ATOM 473 N GLN A 64 23.099 -14.088 5.410 1.00 45.95 N ANISOU 473 N GLN A 64 6001 4607 6849 20 892 -638 N ATOM 474 CA GLN A 64 22.341 -13.950 4.168 1.00 44.54 C ANISOU 474 CA GLN A 64 5930 4499 6495 -52 955 -780 C ATOM 475 C GLN A 64 20.877 -13.583 4.391 1.00 41.21 C ANISOU 475 C GLN A 64 5581 4186 5891 -125 843 -748 C ATOM 476 O GLN A 64 19.984 -14.214 3.827 1.00 41.12 O ANISOU 476 O GLN A 64 5638 4159 5826 -187 852 -842 O ATOM 477 CB GLN A 64 22.430 -15.240 3.346 1.00 47.55 C ANISOU 477 CB GLN A 64 6342 4743 6984 -62 1074 -931 C ATOM 478 CG GLN A 64 23.848 -15.602 2.919 1.00 53.47 C ANISOU 478 CG GLN A 64 7021 5384 7913 9 1216 -991 C ATOM 479 CD GLN A 64 23.941 -16.973 2.258 1.00 60.98 C ANISOU 479 CD GLN A 64 7996 6172 9003 7 1335 -1142 C ATOM 480 OE1 GLN A 64 22.925 -17.604 1.950 1.00 62.79 O ANISOU 480 OE1 GLN A 64 8307 6381 9170 -62 1316 -1223 O ATOM 481 NE2 GLN A 64 25.168 -17.443 2.045 1.00 63.87 N ANISOU 481 NE2 GLN A 64 8281 6414 9571 81 1460 -1184 N ATOM 482 N THR A 65 20.624 -12.565 5.206 1.00 39.29 N ANISOU 482 N THR A 65 5316 4049 5562 -119 737 -623 N ATOM 483 CA THR A 65 19.264 -12.057 5.348 1.00 42.60 C ANISOU 483 CA THR A 65 5795 4582 5810 -182 644 -596 C ATOM 484 C THR A 65 19.188 -10.585 4.950 1.00 44.67 C ANISOU 484 C THR A 65 6081 4994 5899 -192 627 -579 C ATOM 485 O THR A 65 19.093 -9.710 5.807 1.00 45.14 O ANISOU 485 O THR A 65 6110 5122 5920 -175 546 -471 O ATOM 486 CB THR A 65 18.724 -12.236 6.786 1.00 39.97 C ANISOU 486 CB THR A 65 5426 4237 5522 -175 532 -459 C ATOM 487 OG1 THR A 65 19.560 -11.538 7.716 1.00 37.65 O ANISOU 487 OG1 THR A 65 5066 3968 5271 -115 485 -345 O ATOM 488 CG2 THR A 65 18.675 -13.711 7.161 1.00 39.09 C ANISOU 488 CG2 THR A 65 5298 3972 5581 -172 546 -460 C ATOM 489 N PRO A 66 19.215 -10.314 3.636 1.00 47.93 N ANISOU 489 N PRO A 66 6552 5455 6203 -222 707 -687 N ATOM 490 CA PRO A 66 19.176 -8.945 3.114 1.00 47.85 C ANISOU 490 CA PRO A 66 6570 5577 6034 -233 703 -667 C ATOM 491 C PRO A 66 17.808 -8.300 3.300 1.00 50.36 C ANISOU 491 C PRO A 66 6928 6005 6201 -280 592 -620 C ATOM 492 O PRO A 66 17.708 -7.074 3.281 1.00 52.77 O ANISOU 492 O PRO A 66 7236 6408 6407 -276 559 -561 O ATOM 493 CB PRO A 66 19.489 -9.134 1.631 1.00 49.66 C ANISOU 493 CB PRO A 66 6865 5815 6188 -259 824 -801 C ATOM 494 CG PRO A 66 18.919 -10.479 1.317 1.00 50.52 C ANISOU 494 CG PRO A 66 7015 5844 6337 -299 840 -906 C ATOM 495 CD PRO A 66 19.160 -11.313 2.552 1.00 50.83 C ANISOU 495 CD PRO A 66 6976 5758 6578 -257 801 -837 C ATOM 496 N HIS A 67 16.772 -9.117 3.477 1.00 50.51 N ANISOU 496 N HIS A 67 6971 6001 6220 -324 540 -644 N ATOM 497 CA HIS A 67 15.416 -8.605 3.628 1.00 52.47 C ANISOU 497 CA HIS A 67 7243 6348 6346 -371 441 -605 C ATOM 498 C HIS A 67 15.120 -8.156 5.055 1.00 45.71 C ANISOU 498 C HIS A 67 6330 5506 5532 -342 357 -475 C ATOM 499 O HIS A 67 14.076 -7.565 5.317 1.00 46.96 O ANISOU 499 O HIS A 67 6492 5746 5603 -368 283 -429 O ATOM 500 CB HIS A 67 14.392 -9.654 3.194 1.00 60.54 C ANISOU 500 CB HIS A 67 8305 7341 7358 -439 421 -689 C ATOM 501 CG HIS A 67 14.344 -9.871 1.714 1.00 70.73 C ANISOU 501 CG HIS A 67 9671 8660 8543 -486 477 -825 C ATOM 502 ND1 HIS A 67 15.029 -9.074 0.823 1.00 75.12 N ANISOU 502 ND1 HIS A 67 10263 9282 8996 -471 540 -852 N ATOM 503 CD2 HIS A 67 13.690 -10.794 0.968 1.00 74.72 C ANISOU 503 CD2 HIS A 67 10228 9140 9022 -554 479 -945 C ATOM 504 CE1 HIS A 67 14.801 -9.497 -0.409 1.00 77.51 C ANISOU 504 CE1 HIS A 67 10645 9609 9197 -525 581 -980 C ATOM 505 NE2 HIS A 67 13.992 -10.539 -0.347 1.00 77.74 N ANISOU 505 NE2 HIS A 67 10684 9583 9271 -578 541 -1046 N ATOM 506 N ILE A 68 16.026 -8.444 5.980 1.00 39.69 N ANISOU 506 N ILE A 68 5513 4666 4902 -289 367 -416 N ATOM 507 CA ILE A 68 15.900 -7.885 7.317 1.00 34.40 C ANISOU 507 CA ILE A 68 4799 4025 4245 -261 291 -298 C ATOM 508 C ILE A 68 16.588 -6.524 7.316 1.00 32.18 C ANISOU 508 C ILE A 68 4500 3812 3913 -226 291 -261 C ATOM 509 O ILE A 68 17.811 -6.431 7.211 1.00 31.78 O ANISOU 509 O ILE A 68 4416 3719 3939 -186 340 -266 O ATOM 510 CB ILE A 68 16.500 -8.800 8.396 1.00 31.36 C ANISOU 510 CB ILE A 68 4367 3537 4012 -224 280 -236 C ATOM 511 CG1 ILE A 68 15.900 -10.205 8.285 1.00 33.48 C ANISOU 511 CG1 ILE A 68 4652 3714 4355 -261 296 -276 C ATOM 512 CG2 ILE A 68 16.245 -8.222 9.780 1.00 28.42 C ANISOU 512 CG2 ILE A 68 3966 3214 3618 -206 197 -119 C ATOM 513 CD1 ILE A 68 16.390 -11.170 9.343 1.00 36.59 C ANISOU 513 CD1 ILE A 68 5002 3997 4904 -226 282 -196 C ATOM 514 N LYS A 69 15.788 -5.468 7.401 1.00 29.14 N ANISOU 514 N LYS A 69 4131 3527 3415 -242 240 -227 N ATOM 515 CA LYS A 69 16.307 -4.112 7.292 1.00 28.32 C ANISOU 515 CA LYS A 69 4016 3482 3264 -217 242 -198 C ATOM 516 C LYS A 69 16.867 -3.624 8.627 1.00 24.69 C ANISOU 516 C LYS A 69 3503 3013 2863 -177 193 -119 C ATOM 517 O LYS A 69 16.546 -4.159 9.684 1.00 23.10 O ANISOU 517 O LYS A 69 3287 2792 2698 -174 143 -73 O ATOM 518 CB LYS A 69 15.215 -3.162 6.797 1.00 31.11 C ANISOU 518 CB LYS A 69 4404 3933 3484 -247 207 -192 C ATOM 519 CG LYS A 69 14.572 -3.581 5.480 1.00 34.86 C ANISOU 519 CG LYS A 69 4935 4435 3875 -294 232 -266 C ATOM 520 CD LYS A 69 15.606 -3.752 4.374 1.00 36.80 C ANISOU 520 CD LYS A 69 5208 4655 4121 -290 326 -333 C ATOM 521 N ILE A 70 17.710 -2.605 8.577 1.00 23.34 N ANISOU 521 N ILE A 70 3307 2860 2700 -152 205 -103 N ATOM 522 CA ILE A 70 18.220 -2.010 9.802 1.00 22.77 C ANISOU 522 CA ILE A 70 3190 2791 2671 -123 147 -42 C ATOM 523 C ILE A 70 17.551 -0.665 10.056 1.00 22.54 C ANISOU 523 C ILE A 70 3175 2838 2551 -131 107 -17 C ATOM 524 O ILE A 70 17.758 0.297 9.308 1.00 23.76 O ANISOU 524 O ILE A 70 3336 3019 2675 -133 139 -29 O ATOM 525 CB ILE A 70 19.743 -1.822 9.752 1.00 23.33 C ANISOU 525 CB ILE A 70 3202 2812 2849 -91 180 -42 C ATOM 526 CG1 ILE A 70 20.432 -3.167 9.520 1.00 24.64 C ANISOU 526 CG1 ILE A 70 3343 2889 3130 -73 227 -67 C ATOM 527 CG2 ILE A 70 20.240 -1.173 11.039 1.00 19.89 C ANISOU 527 CG2 ILE A 70 2720 2387 2449 -70 100 15 C ATOM 528 CD1 ILE A 70 21.902 -3.040 9.173 1.00 30.00 C ANISOU 528 CD1 ILE A 70 3955 3515 3927 -42 285 -80 C ATOM 529 N ALA A 71 16.741 -0.608 11.107 1.00 21.44 N ANISOU 529 N ALA A 71 3041 2730 2375 -135 45 20 N ATOM 530 CA ALA A 71 16.145 0.646 11.541 1.00 22.13 C ANISOU 530 CA ALA A 71 3134 2877 2397 -135 12 39 C ATOM 531 C ALA A 71 16.956 1.230 12.693 1.00 21.63 C ANISOU 531 C ALA A 71 3038 2808 2372 -113 -34 64 C ATOM 532 O ALA A 71 17.674 0.509 13.387 1.00 21.74 O ANISOU 532 O ALA A 71 3028 2786 2445 -100 -61 86 O ATOM 533 CB ALA A 71 14.687 0.438 11.953 1.00 21.08 C ANISOU 533 CB ALA A 71 3025 2788 2197 -155 -15 53 C ATOM 534 N THR A 72 16.852 2.541 12.879 1.00 23.90 N ANISOU 534 N THR A 72 3323 3127 2630 -109 -47 61 N ATOM 535 CA THR A 72 17.504 3.217 13.996 1.00 24.79 C ANISOU 535 CA THR A 72 3413 3242 2766 -98 -99 69 C ATOM 536 C THR A 72 16.653 4.414 14.418 1.00 24.29 C ANISOU 536 C THR A 72 3369 3221 2641 -100 -112 58 C ATOM 537 O THR A 72 15.613 4.689 13.807 1.00 24.26 O ANISOU 537 O THR A 72 3386 3241 2589 -105 -83 56 O ATOM 538 CB THR A 72 18.943 3.674 13.631 1.00 21.98 C ANISOU 538 CB THR A 72 3008 2841 2503 -89 -87 58 C ATOM 539 OG1 THR A 72 19.666 4.014 14.823 1.00 22.05 O ANISOU 539 OG1 THR A 72 2985 2848 2543 -84 -158 63 O ATOM 540 CG2 THR A 72 18.911 4.862 12.700 1.00 21.39 C ANISOU 540 CG2 THR A 72 2934 2766 2425 -95 -39 42 C ATOM 541 N VAL A 73 17.084 5.117 15.463 1.00 23.24 N ANISOU 541 N VAL A 73 3225 3094 2511 -97 -158 47 N ATOM 542 CA VAL A 73 16.315 6.235 16.007 1.00 21.87 C ANISOU 542 CA VAL A 73 3070 2950 2288 -96 -164 23 C ATOM 543 C VAL A 73 17.125 7.535 16.049 1.00 23.55 C ANISOU 543 C VAL A 73 3258 3132 2558 -97 -174 -10 C ATOM 544 O VAL A 73 18.346 7.511 16.218 1.00 21.97 O ANISOU 544 O VAL A 73 3023 2902 2422 -101 -204 -15 O ATOM 545 CB VAL A 73 15.807 5.919 17.430 1.00 21.65 C ANISOU 545 CB VAL A 73 3070 2968 2187 -100 -204 25 C ATOM 546 CG1 VAL A 73 14.826 4.756 17.401 1.00 19.67 C ANISOU 546 CG1 VAL A 73 2841 2743 1889 -105 -184 62 C ATOM 547 CG2 VAL A 73 16.985 5.607 18.370 1.00 22.63 C ANISOU 547 CG2 VAL A 73 3181 3087 2330 -103 -274 30 C ATOM 548 N THR A 74 16.438 8.663 15.880 1.00 23.31 N ANISOU 548 N THR A 74 3238 3100 2518 -92 -148 -31 N ATOM 549 CA THR A 74 17.059 9.984 16.003 1.00 27.08 C ANISOU 549 CA THR A 74 3695 3536 3059 -95 -153 -67 C ATOM 550 C THR A 74 16.132 10.932 16.762 1.00 25.82 C ANISOU 550 C THR A 74 3560 3389 2864 -88 -151 -109 C ATOM 551 O THR A 74 14.917 10.700 16.829 1.00 24.56 O ANISOU 551 O THR A 74 3422 3266 2643 -74 -127 -98 O ATOM 552 CB THR A 74 17.400 10.602 14.627 1.00 29.38 C ANISOU 552 CB THR A 74 3964 3779 3419 -94 -99 -41 C ATOM 553 OG1 THR A 74 16.215 10.662 13.823 1.00 27.77 O ANISOU 553 OG1 THR A 74 3785 3597 3171 -80 -59 -8 O ATOM 554 CG2 THR A 74 18.457 9.770 13.902 1.00 29.48 C ANISOU 554 CG2 THR A 74 3950 3775 3479 -102 -84 -14 C ATOM 555 N ASN A 75 16.714 11.997 17.316 1.00 22.63 N ANISOU 555 N ASN A 75 3144 2947 2508 -98 -172 -164 N ATOM 556 CA ASN A 75 16.008 12.927 18.201 1.00 23.91 C ANISOU 556 CA ASN A 75 3331 3111 2644 -92 -168 -228 C ATOM 557 C ASN A 75 15.301 12.168 19.321 1.00 24.42 C ANISOU 557 C ASN A 75 3437 3251 2590 -92 -185 -243 C ATOM 558 O ASN A 75 14.232 12.568 19.787 1.00 24.50 O ANISOU 558 O ASN A 75 3470 3281 2556 -77 -147 -274 O ATOM 559 CB ASN A 75 15.001 13.785 17.418 1.00 21.50 C ANISOU 559 CB ASN A 75 3020 2770 2377 -65 -103 -212 C ATOM 560 CG ASN A 75 14.687 15.097 18.121 1.00 24.32 C ANISOU 560 CG ASN A 75 3384 3084 2772 -58 -88 -290 C ATOM 561 OD1 ASN A 75 15.542 15.661 18.801 1.00 25.04 O ANISOU 561 OD1 ASN A 75 3475 3144 2896 -83 -124 -358 O ATOM 562 ND2 ASN A 75 13.455 15.581 17.970 1.00 24.93 N ANISOU 562 ND2 ASN A 75 3463 3155 2853 -25 -37 -286 N ATOM 563 N PHE A 76 15.934 11.083 19.757 1.00 24.93 N ANISOU 563 N PHE A 76 3506 3353 2611 -107 -238 -216 N ATOM 564 CA PHE A 76 15.298 10.060 20.578 1.00 23.65 C ANISOU 564 CA PHE A 76 3383 3262 2339 -108 -248 -193 C ATOM 565 C PHE A 76 15.851 10.054 22.001 1.00 26.68 C ANISOU 565 C PHE A 76 3800 3689 2649 -129 -318 -235 C ATOM 566 O PHE A 76 17.061 10.166 22.199 1.00 28.11 O ANISOU 566 O PHE A 76 3957 3850 2872 -147 -388 -248 O ATOM 567 CB PHE A 76 15.501 8.696 19.910 1.00 21.10 C ANISOU 567 CB PHE A 76 3044 2944 2027 -106 -253 -113 C ATOM 568 CG PHE A 76 14.817 7.551 20.607 1.00 21.53 C ANISOU 568 CG PHE A 76 3133 3056 1990 -110 -255 -70 C ATOM 569 CD1 PHE A 76 15.437 6.885 21.659 1.00 25.74 C ANISOU 569 CD1 PHE A 76 3687 3624 2470 -123 -321 -50 C ATOM 570 CD2 PHE A 76 13.575 7.112 20.181 1.00 21.73 C ANISOU 570 CD2 PHE A 76 3164 3100 1991 -103 -195 -41 C ATOM 571 CE1 PHE A 76 14.814 5.816 22.292 1.00 26.61 C ANISOU 571 CE1 PHE A 76 3831 3780 2499 -128 -317 5 C ATOM 572 CE2 PHE A 76 12.942 6.044 20.806 1.00 25.38 C ANISOU 572 CE2 PHE A 76 3653 3607 2385 -113 -189 4 C ATOM 573 CZ PHE A 76 13.558 5.394 21.860 1.00 25.55 C ANISOU 573 CZ PHE A 76 3701 3656 2349 -125 -244 31 C ATOM 574 N PRO A 77 14.966 9.923 23.002 1.00 27.31 N ANISOU 574 N PRO A 77 3932 3832 2613 -131 -298 -254 N ATOM 575 CA PRO A 77 13.508 9.852 22.857 1.00 27.07 C ANISOU 575 CA PRO A 77 3915 3824 2546 -113 -211 -243 C ATOM 576 C PRO A 77 12.781 11.164 23.142 1.00 27.97 C ANISOU 576 C PRO A 77 4039 3922 2665 -99 -152 -331 C ATOM 577 O PRO A 77 11.556 11.208 23.010 1.00 28.29 O ANISOU 577 O PRO A 77 4076 3976 2697 -79 -76 -323 O ATOM 578 CB PRO A 77 13.124 8.817 23.907 1.00 28.52 C ANISOU 578 CB PRO A 77 4148 4087 2604 -126 -220 -204 C ATOM 579 CG PRO A 77 14.088 9.113 25.025 1.00 30.91 C ANISOU 579 CG PRO A 77 4487 4419 2838 -150 -302 -253 C ATOM 580 CD PRO A 77 15.394 9.513 24.353 1.00 29.22 C ANISOU 580 CD PRO A 77 4221 4139 2742 -155 -369 -264 C ATOM 581 N GLN A 78 13.515 12.205 23.524 1.00 28.44 N ANISOU 581 N GLN A 78 4105 3947 2755 -111 -184 -414 N ATOM 582 CA GLN A 78 12.910 13.414 24.074 1.00 29.94 C ANISOU 582 CA GLN A 78 4315 4118 2943 -102 -130 -517 C ATOM 583 C GLN A 78 12.022 14.158 23.085 1.00 30.43 C ANISOU 583 C GLN A 78 4332 4114 3115 -63 -49 -508 C ATOM 584 O GLN A 78 11.074 14.825 23.487 1.00 31.02 O ANISOU 584 O GLN A 78 4415 4183 3187 -41 23 -566 O ATOM 585 CB GLN A 78 13.990 14.366 24.589 1.00 33.78 C ANISOU 585 CB GLN A 78 4811 4564 3458 -130 -192 -614 C ATOM 586 CG GLN A 78 15.074 13.699 25.421 1.00 40.70 C ANISOU 586 CG GLN A 78 5716 5500 4249 -170 -301 -612 C ATOM 587 CD GLN A 78 16.296 13.325 24.593 1.00 44.13 C ANISOU 587 CD GLN A 78 6088 5889 4788 -181 -374 -546 C ATOM 588 OE1 GLN A 78 16.175 12.814 23.480 1.00 38.79 O ANISOU 588 OE1 GLN A 78 5370 5184 4183 -159 -340 -459 O ATOM 589 NE2 GLN A 78 17.484 13.600 25.130 1.00 50.92 N ANISOU 589 NE2 GLN A 78 6940 6745 5662 -217 -472 -593 N ATOM 590 N GLY A 79 12.327 14.043 21.797 1.00 28.23 N ANISOU 590 N GLY A 79 4005 3787 2933 -53 -60 -433 N ATOM 591 CA GLY A 79 11.601 14.782 20.782 1.00 26.64 C ANISOU 591 CA GLY A 79 3761 3525 2834 -17 -2 -408 C ATOM 592 C GLY A 79 11.736 16.289 20.937 1.00 28.74 C ANISOU 592 C GLY A 79 4020 3706 3195 -7 22 -491 C ATOM 593 O GLY A 79 10.750 17.018 20.820 1.00 29.04 O ANISOU 593 O GLY A 79 4039 3707 3286 30 87 -508 O ATOM 594 N ASN A 80 12.956 16.752 21.203 1.00 27.10 N ANISOU 594 N ASN A 80 3819 3458 3021 -40 -31 -543 N ATOM 595 CA ASN A 80 13.238 18.180 21.346 1.00 30.99 C ANISOU 595 CA ASN A 80 4303 3853 3619 -41 -14 -629 C ATOM 596 C ASN A 80 12.965 18.932 20.045 1.00 30.20 C ANISOU 596 C ASN A 80 4152 3660 3662 -8 30 -559 C ATOM 597 O ASN A 80 12.842 18.324 18.986 1.00 25.95 O ANISOU 597 O ASN A 80 3590 3141 3128 5 30 -448 O ATOM 598 CB ASN A 80 14.690 18.404 21.788 1.00 30.90 C ANISOU 598 CB ASN A 80 4295 3818 3627 -93 -93 -687 C ATOM 599 CG ASN A 80 14.961 17.902 23.201 1.00 34.87 C ANISOU 599 CG ASN A 80 4855 4409 3986 -127 -149 -766 C ATOM 600 OD1 ASN A 80 14.086 17.942 24.065 1.00 38.56 O ANISOU 600 OD1 ASN A 80 5369 4923 4358 -115 -107 -828 O ATOM 601 ND2 ASN A 80 16.180 17.438 23.441 1.00 35.66 N ANISOU 601 ND2 ASN A 80 4947 4532 4069 -169 -244 -761 N ATOM 602 N ASP A 81 12.875 20.256 20.121 1.00 32.66 N ANISOU 602 N ASP A 81 4452 3869 4088 5 67 -623 N ATOM 603 CA ASP A 81 12.495 21.037 18.945 1.00 35.75 C ANISOU 603 CA ASP A 81 4798 4169 4616 42 111 -543 C ATOM 604 C ASP A 81 13.688 21.664 18.224 1.00 35.57 C ANISOU 604 C ASP A 81 4749 4054 4711 11 88 -512 C ATOM 605 O ASP A 81 13.536 22.668 17.532 1.00 33.68 O ANISOU 605 O ASP A 81 4481 3711 4607 34 127 -473 O ATOM 606 CB ASP A 81 11.491 22.130 19.329 1.00 36.23 C ANISOU 606 CB ASP A 81 4850 4155 4762 88 181 -608 C ATOM 607 CG ASP A 81 12.036 23.108 20.363 1.00 39.04 C ANISOU 607 CG ASP A 81 5230 4435 5168 60 186 -764 C ATOM 608 OD1 ASP A 81 13.246 23.070 20.684 1.00 39.75 O ANISOU 608 OD1 ASP A 81 5335 4521 5246 1 124 -812 O ATOM 609 OD2 ASP A 81 11.242 23.938 20.848 1.00 41.01 O ANISOU 609 OD2 ASP A 81 5480 4624 5479 95 253 -844 O ATOM 610 N ASP A 82 14.869 21.071 18.391 1.00 33.80 N ANISOU 610 N ASP A 82 4530 3867 4447 -40 27 -521 N ATOM 611 CA ASP A 82 16.081 21.579 17.755 1.00 30.05 C ANISOU 611 CA ASP A 82 4018 3311 4089 -76 12 -493 C ATOM 612 C ASP A 82 16.302 20.870 16.417 1.00 28.47 C ANISOU 612 C ASP A 82 3798 3142 3879 -69 22 -351 C ATOM 613 O ASP A 82 16.681 19.696 16.379 1.00 24.43 O ANISOU 613 O ASP A 82 3291 2717 3274 -84 -12 -323 O ATOM 614 CB ASP A 82 17.283 21.392 18.681 1.00 29.11 C ANISOU 614 CB ASP A 82 3901 3208 3952 -135 -62 -586 C ATOM 615 CG ASP A 82 18.521 22.113 18.189 1.00 35.32 C ANISOU 615 CG ASP A 82 4636 3894 4890 -179 -73 -580 C ATOM 616 OD1 ASP A 82 18.951 21.848 17.048 1.00 37.73 O ANISOU 616 OD1 ASP A 82 4908 4188 5241 -178 -48 -466 O ATOM 617 OD2 ASP A 82 19.068 22.951 18.942 1.00 36.91 O ANISOU 617 OD2 ASP A 82 4831 4028 5167 -218 -102 -692 O ATOM 618 N LEU A 83 16.065 21.587 15.323 1.00 28.27 N ANISOU 618 N LEU A 83 3751 3043 3948 -47 72 -263 N ATOM 619 CA LEU A 83 16.110 20.984 13.992 1.00 28.78 C ANISOU 619 CA LEU A 83 3809 3145 3980 -39 91 -131 C ATOM 620 C LEU A 83 17.524 20.582 13.562 1.00 25.88 C ANISOU 620 C LEU A 83 3419 2776 3639 -86 81 -107 C ATOM 621 O LEU A 83 17.711 19.535 12.941 1.00 26.23 O ANISOU 621 O LEU A 83 3469 2894 3602 -89 81 -48 O ATOM 622 CB LEU A 83 15.503 21.940 12.962 1.00 30.82 C ANISOU 622 CB LEU A 83 4056 3328 4326 -4 141 -33 C ATOM 623 CG LEU A 83 15.445 21.496 11.498 1.00 31.67 C ANISOU 623 CG LEU A 83 4169 3476 4389 3 163 109 C ATOM 624 CD1 LEU A 83 14.192 22.041 10.836 1.00 30.33 C ANISOU 624 CD1 LEU A 83 4000 3290 4235 57 180 198 C ATOM 625 CD2 LEU A 83 16.683 21.954 10.729 1.00 32.55 C ANISOU 625 CD2 LEU A 83 4261 3520 4587 -36 197 165 C ATOM 626 N ASP A 84 18.512 21.418 13.866 1.00 23.65 N ANISOU 626 N ASP A 84 3103 2402 3480 -125 78 -156 N ATOM 627 CA ASP A 84 19.889 21.122 13.477 1.00 26.40 C ANISOU 627 CA ASP A 84 3411 2739 3880 -170 76 -134 C ATOM 628 C ASP A 84 20.370 19.807 14.098 1.00 26.47 C ANISOU 628 C ASP A 84 3420 2848 3790 -185 15 -175 C ATOM 629 O ASP A 84 21.049 19.015 13.449 1.00 26.35 O ANISOU 629 O ASP A 84 3383 2867 3763 -195 29 -120 O ATOM 630 CB ASP A 84 20.825 22.261 13.877 1.00 30.64 C ANISOU 630 CB ASP A 84 3901 3159 4581 -216 71 -195 C ATOM 631 CG ASP A 84 20.522 23.555 13.142 1.00 40.61 C ANISOU 631 CG ASP A 84 5157 4302 5971 -206 139 -134 C ATOM 632 OD1 ASP A 84 19.969 23.497 12.022 1.00 44.84 O ANISOU 632 OD1 ASP A 84 5712 4851 6476 -173 193 -10 O ATOM 633 OD2 ASP A 84 20.839 24.633 13.686 1.00 42.66 O ANISOU 633 OD2 ASP A 84 5393 4452 6365 -233 135 -207 O ATOM 634 N ILE A 85 19.999 19.568 15.350 1.00 25.60 N ANISOU 634 N ILE A 85 3336 2783 3609 -183 -46 -269 N ATOM 635 CA ILE A 85 20.389 18.338 16.015 1.00 26.53 C ANISOU 635 CA ILE A 85 3457 2993 3631 -193 -110 -294 C ATOM 636 C ILE A 85 19.695 17.137 15.374 1.00 27.66 C ANISOU 636 C ILE A 85 3630 3219 3660 -159 -85 -215 C ATOM 637 O ILE A 85 20.360 16.163 15.010 1.00 25.64 O ANISOU 637 O ILE A 85 3354 2999 3389 -167 -93 -177 O ATOM 638 CB ILE A 85 20.090 18.392 17.520 1.00 27.41 C ANISOU 638 CB ILE A 85 3602 3140 3671 -202 -178 -404 C ATOM 639 CG1 ILE A 85 21.065 19.369 18.189 1.00 30.65 C ANISOU 639 CG1 ILE A 85 3977 3476 4191 -251 -225 -497 C ATOM 640 CG2 ILE A 85 20.205 16.995 18.150 1.00 27.29 C ANISOU 640 CG2 ILE A 85 3605 3231 3532 -201 -239 -398 C ATOM 641 CD1 ILE A 85 21.073 19.318 19.697 1.00 33.77 C ANISOU 641 CD1 ILE A 85 4409 3923 4501 -274 -309 -613 C ATOM 642 N ALA A 86 18.374 17.215 15.214 1.00 24.87 N ANISOU 642 N ALA A 86 3317 2891 3241 -122 -53 -195 N ATOM 643 CA ALA A 86 17.624 16.127 14.591 1.00 23.41 C ANISOU 643 CA ALA A 86 3158 2782 2955 -98 -35 -128 C ATOM 644 C ALA A 86 18.148 15.823 13.186 1.00 24.23 C ANISOU 644 C ALA A 86 3246 2875 3086 -103 10 -43 C ATOM 645 O ALA A 86 18.288 14.656 12.802 1.00 26.79 O ANISOU 645 O ALA A 86 3577 3254 3348 -103 11 -15 O ATOM 646 CB ALA A 86 16.137 16.457 14.543 1.00 20.76 C ANISOU 646 CB ALA A 86 2850 2462 2576 -60 -10 -115 C ATOM 647 N LEU A 87 18.454 16.869 12.428 1.00 23.25 N ANISOU 647 N LEU A 87 3103 2678 3054 -108 55 -5 N ATOM 648 CA LEU A 87 18.979 16.693 11.079 1.00 24.32 C ANISOU 648 CA LEU A 87 3231 2806 3205 -116 113 78 C ATOM 649 C LEU A 87 20.365 16.037 11.068 1.00 24.04 C ANISOU 649 C LEU A 87 3154 2769 3212 -147 115 62 C ATOM 650 O LEU A 87 20.611 15.132 10.275 1.00 25.38 O ANISOU 650 O LEU A 87 3330 2978 3334 -147 151 101 O ATOM 651 CB LEU A 87 19.043 18.037 10.341 1.00 23.59 C ANISOU 651 CB LEU A 87 3127 2629 3208 -118 165 135 C ATOM 652 CG LEU A 87 19.552 17.968 8.895 1.00 23.89 C ANISOU 652 CG LEU A 87 3168 2664 3245 -130 237 232 C ATOM 653 CD1 LEU A 87 18.816 16.895 8.093 1.00 21.45 C ANISOU 653 CD1 LEU A 87 2907 2452 2790 -112 245 277 C ATOM 654 CD2 LEU A 87 19.445 19.337 8.207 1.00 22.85 C ANISOU 654 CD2 LEU A 87 3032 2447 3201 -128 286 310 C ATOM 655 N ALA A 88 21.268 16.502 11.929 1.00 22.75 N ANISOU 655 N ALA A 88 2943 2555 3145 -174 77 1 N ATOM 656 CA ALA A 88 22.619 15.943 11.991 1.00 22.03 C ANISOU 656 CA ALA A 88 2793 2456 3122 -200 70 -11 C ATOM 657 C ALA A 88 22.596 14.453 12.366 1.00 22.73 C ANISOU 657 C ALA A 88 2892 2622 3122 -185 29 -24 C ATOM 658 O ALA A 88 23.343 13.651 11.802 1.00 22.49 O ANISOU 658 O ALA A 88 2831 2600 3116 -188 62 2 O ATOM 659 CB ALA A 88 23.471 16.724 12.980 1.00 22.52 C ANISOU 659 CB ALA A 88 2800 2459 3299 -235 11 -82 C ATOM 660 N GLU A 89 21.735 14.091 13.313 1.00 23.47 N ANISOU 660 N GLU A 89 3029 2767 3121 -169 -34 -61 N ATOM 661 CA GLU A 89 21.617 12.706 13.755 1.00 24.53 C ANISOU 661 CA GLU A 89 3177 2966 3175 -156 -75 -63 C ATOM 662 C GLU A 89 21.075 11.821 12.641 1.00 23.84 C ANISOU 662 C GLU A 89 3123 2914 3021 -137 -12 -9 C ATOM 663 O GLU A 89 21.533 10.697 12.455 1.00 22.95 O ANISOU 663 O GLU A 89 2997 2818 2905 -133 -7 1 O ATOM 664 CB GLU A 89 20.719 12.603 14.992 1.00 26.28 C ANISOU 664 CB GLU A 89 3445 3237 3304 -147 -141 -107 C ATOM 665 CG GLU A 89 21.306 13.239 16.253 1.00 28.78 C ANISOU 665 CG GLU A 89 3741 3538 3656 -171 -219 -177 C ATOM 666 CD GLU A 89 20.455 12.977 17.488 1.00 31.86 C ANISOU 666 CD GLU A 89 4186 3991 3928 -164 -272 -219 C ATOM 667 OE1 GLU A 89 19.299 12.540 17.327 1.00 32.49 O ANISOU 667 OE1 GLU A 89 4312 4112 3919 -140 -237 -193 O ATOM 668 OE2 GLU A 89 20.941 13.200 18.621 1.00 30.49 O ANISOU 668 OE2 GLU A 89 4010 3830 3746 -186 -350 -277 O ATOM 669 N THR A 90 20.103 12.338 11.900 1.00 24.21 N ANISOU 669 N THR A 90 3211 2967 3020 -126 33 22 N ATOM 670 CA THR A 90 19.487 11.596 10.808 1.00 22.80 C ANISOU 670 CA THR A 90 3071 2829 2763 -116 81 66 C ATOM 671 C THR A 90 20.480 11.385 9.665 1.00 25.60 C ANISOU 671 C THR A 90 3404 3159 3163 -129 155 96 C ATOM 672 O THR A 90 20.579 10.283 9.120 1.00 23.98 O ANISOU 672 O THR A 90 3213 2982 2916 -127 184 98 O ATOM 673 CB THR A 90 18.228 12.318 10.294 1.00 24.60 C ANISOU 673 CB THR A 90 3339 3072 2936 -102 95 100 C ATOM 674 OG1 THR A 90 17.238 12.329 11.331 1.00 27.04 O ANISOU 674 OG1 THR A 90 3663 3409 3202 -87 43 68 O ATOM 675 CG2 THR A 90 17.659 11.614 9.073 1.00 22.04 C ANISOU 675 CG2 THR A 90 3053 2795 2525 -100 132 144 C ATOM 676 N ARG A 91 21.228 12.434 9.321 1.00 24.74 N ANISOU 676 N ARG A 91 3261 2994 3145 -144 194 114 N ATOM 677 CA ARG A 91 22.297 12.311 8.334 1.00 24.93 C ANISOU 677 CA ARG A 91 3254 2991 3226 -160 279 141 C ATOM 678 C ARG A 91 23.341 11.273 8.768 1.00 25.58 C ANISOU 678 C ARG A 91 3280 3066 3372 -161 269 103 C ATOM 679 O ARG A 91 23.810 10.476 7.957 1.00 22.55 O ANISOU 679 O ARG A 91 2893 2690 2985 -159 340 110 O ATOM 680 CB ARG A 91 22.978 13.663 8.097 1.00 25.74 C ANISOU 680 CB ARG A 91 3316 3022 3441 -181 319 169 C ATOM 681 CG ARG A 91 22.176 14.647 7.254 1.00 28.37 C ANISOU 681 CG ARG A 91 3700 3349 3732 -178 360 237 C ATOM 682 CD ARG A 91 22.911 15.978 7.135 1.00 32.84 C ANISOU 682 CD ARG A 91 4218 3825 4433 -203 400 267 C ATOM 683 NE ARG A 91 22.173 16.925 6.308 1.00 35.86 N ANISOU 683 NE ARG A 91 4647 4191 4786 -196 438 351 N ATOM 684 CZ ARG A 91 22.380 18.237 6.302 1.00 36.11 C ANISOU 684 CZ ARG A 91 4655 4136 4931 -209 459 387 C ATOM 685 NH1 ARG A 91 23.306 18.774 7.087 1.00 36.13 N ANISOU 685 NH1 ARG A 91 4585 4061 5081 -237 443 332 N ATOM 686 NH2 ARG A 91 21.654 19.014 5.513 1.00 37.13 N ANISOU 686 NH2 ARG A 91 4827 4251 5030 -196 489 479 N ATOM 687 N ALA A 92 23.711 11.298 10.045 1.00 24.10 N ANISOU 687 N ALA A 92 3048 2864 3244 -162 181 62 N ATOM 688 CA ALA A 92 24.674 10.334 10.571 1.00 24.11 C ANISOU 688 CA ALA A 92 2988 2858 3315 -158 149 39 C ATOM 689 C ALA A 92 24.127 8.919 10.454 1.00 23.80 C ANISOU 689 C ALA A 92 2991 2862 3188 -134 149 39 C ATOM 690 O ALA A 92 24.840 8.000 10.051 1.00 24.30 O ANISOU 690 O ALA A 92 3020 2910 3304 -125 193 38 O ATOM 691 CB ALA A 92 25.020 10.652 12.017 1.00 23.37 C ANISOU 691 CB ALA A 92 2853 2755 3270 -167 34 2 C ATOM 692 N ALA A 93 22.857 8.751 10.807 1.00 23.59 N ANISOU 692 N ALA A 93 3035 2883 3044 -126 106 37 N ATOM 693 CA ALA A 93 22.210 7.445 10.739 1.00 22.65 C ANISOU 693 CA ALA A 93 2958 2800 2847 -111 103 36 C ATOM 694 C ALA A 93 22.285 6.893 9.321 1.00 23.57 C ANISOU 694 C ALA A 93 3097 2916 2942 -112 204 42 C ATOM 695 O ALA A 93 22.647 5.734 9.113 1.00 19.97 O ANISOU 695 O ALA A 93 2631 2448 2509 -103 229 28 O ATOM 696 CB ALA A 93 20.765 7.541 11.197 1.00 22.21 C ANISOU 696 CB ALA A 93 2967 2795 2678 -108 57 36 C ATOM 697 N VAL A 94 21.951 7.744 8.353 1.00 22.90 N ANISOU 697 N VAL A 94 3046 2842 2814 -124 262 65 N ATOM 698 CA VAL A 94 22.027 7.385 6.945 1.00 23.43 C ANISOU 698 CA VAL A 94 3147 2920 2834 -132 361 71 C ATOM 699 C VAL A 94 23.462 7.047 6.543 1.00 26.62 C ANISOU 699 C VAL A 94 3488 3275 3350 -132 442 58 C ATOM 700 O VAL A 94 23.696 6.067 5.833 1.00 26.93 O ANISOU 700 O VAL A 94 3543 3315 3375 -129 511 31 O ATOM 701 CB VAL A 94 21.482 8.521 6.053 1.00 24.34 C ANISOU 701 CB VAL A 94 3308 3057 2884 -145 398 118 C ATOM 702 CG1 VAL A 94 21.818 8.273 4.591 1.00 24.51 C ANISOU 702 CG1 VAL A 94 3366 3094 2852 -160 509 129 C ATOM 703 CG2 VAL A 94 19.974 8.658 6.243 1.00 22.21 C ANISOU 703 CG2 VAL A 94 3094 2838 2506 -140 329 131 C ATOM 704 N ALA A 95 24.421 7.842 7.016 1.00 23.63 N ANISOU 704 N ALA A 95 3034 2851 3095 -137 435 69 N ATOM 705 CA ALA A 95 25.831 7.617 6.707 1.00 24.86 C ANISOU 705 CA ALA A 95 3106 2955 3385 -138 511 61 C ATOM 706 C ALA A 95 26.351 6.317 7.326 1.00 24.72 C ANISOU 706 C ALA A 95 3036 2914 3441 -112 477 28 C ATOM 707 O ALA A 95 27.256 5.683 6.783 1.00 24.81 O ANISOU 707 O ALA A 95 2997 2890 3539 -101 565 12 O ATOM 708 CB ALA A 95 26.678 8.806 7.178 1.00 28.07 C ANISOU 708 CB ALA A 95 3431 3314 3920 -156 493 80 C ATOM 709 N TYR A 96 25.778 5.919 8.458 1.00 24.81 N ANISOU 709 N TYR A 96 3060 2943 3422 -99 358 23 N ATOM 710 CA TYR A 96 26.155 4.658 9.092 1.00 25.91 C ANISOU 710 CA TYR A 96 3159 3059 3625 -73 315 11 C ATOM 711 C TYR A 96 25.726 3.465 8.243 1.00 26.84 C ANISOU 711 C TYR A 96 3332 3179 3686 -62 392 -15 C ATOM 712 O TYR A 96 26.348 2.404 8.293 1.00 27.51 O ANISOU 712 O TYR A 96 3371 3217 3864 -37 414 -30 O ATOM 713 CB TYR A 96 25.534 4.527 10.478 1.00 24.44 C ANISOU 713 CB TYR A 96 2990 2901 3394 -67 176 23 C ATOM 714 CG TYR A 96 26.348 5.051 11.646 1.00 25.80 C ANISOU 714 CG TYR A 96 3083 3057 3661 -69 74 33 C ATOM 715 CD1 TYR A 96 27.620 4.554 11.928 1.00 25.64 C ANISOU 715 CD1 TYR A 96 2957 2988 3795 -52 58 42 C ATOM 716 CD2 TYR A 96 25.810 6.000 12.510 1.00 24.82 C ANISOU 716 CD2 TYR A 96 2989 2968 3473 -88 -12 30 C ATOM 717 CE1 TYR A 96 28.345 5.017 13.022 1.00 24.71 C ANISOU 717 CE1 TYR A 96 2766 2866 3757 -60 -57 51 C ATOM 718 CE2 TYR A 96 26.521 6.463 13.600 1.00 23.95 C ANISOU 718 CE2 TYR A 96 2817 2852 3432 -97 -115 26 C ATOM 719 CZ TYR A 96 27.783 5.971 13.853 1.00 23.93 C ANISOU 719 CZ TYR A 96 2711 2809 3574 -86 -145 38 C ATOM 720 OH TYR A 96 28.476 6.445 14.941 1.00 25.21 O ANISOU 720 OH TYR A 96 2810 2972 3798 -101 -265 33 O ATOM 721 N GLY A 97 24.649 3.645 7.482 1.00 26.15 N ANISOU 721 N GLY A 97 3340 3141 3454 -80 426 -22 N ATOM 722 CA GLY A 97 24.107 2.583 6.653 1.00 28.93 C ANISOU 722 CA GLY A 97 3757 3502 3734 -82 487 -60 C ATOM 723 C GLY A 97 22.688 2.163 7.010 1.00 28.07 C ANISOU 723 C GLY A 97 3721 3438 3504 -91 411 -61 C ATOM 724 O GLY A 97 22.244 1.092 6.611 1.00 30.44 O ANISOU 724 O GLY A 97 4062 3733 3770 -95 435 -97 O ATOM 725 N ALA A 98 21.972 3.001 7.757 1.00 26.72 N ANISOU 725 N ALA A 98 3564 3306 3280 -97 325 -27 N ATOM 726 CA ALA A 98 20.602 2.678 8.166 1.00 25.30 C ANISOU 726 CA ALA A 98 3441 3171 3000 -106 259 -23 C ATOM 727 C ALA A 98 19.669 2.503 6.969 1.00 25.20 C ANISOU 727 C ALA A 98 3502 3202 2872 -130 303 -43 C ATOM 728 O ALA A 98 19.752 3.245 5.991 1.00 26.14 O ANISOU 728 O ALA A 98 3645 3344 2943 -142 357 -37 O ATOM 729 CB ALA A 98 20.057 3.759 9.101 1.00 24.97 C ANISOU 729 CB ALA A 98 3397 3161 2928 -106 180 10 C ATOM 730 N ASP A 99 18.791 1.507 7.048 1.00 25.31 N ANISOU 730 N ASP A 99 3551 3227 2840 -142 276 -65 N ATOM 731 CA ASP A 99 17.741 1.327 6.049 1.00 25.64 C ANISOU 731 CA ASP A 99 3657 3318 2765 -172 288 -87 C ATOM 732 C ASP A 99 16.522 2.176 6.381 1.00 24.69 C ANISOU 732 C ASP A 99 3553 3258 2570 -179 217 -45 C ATOM 733 O ASP A 99 15.754 2.545 5.497 1.00 25.90 O ANISOU 733 O ASP A 99 3748 3464 2630 -198 216 -41 O ATOM 734 CB ASP A 99 17.328 -0.143 5.949 1.00 25.63 C ANISOU 734 CB ASP A 99 3679 3293 2768 -189 290 -137 C ATOM 735 CG ASP A 99 18.441 -1.017 5.416 1.00 31.25 C ANISOU 735 CG ASP A 99 4379 3937 3556 -179 377 -191 C ATOM 736 OD1 ASP A 99 18.996 -0.673 4.350 1.00 33.28 O ANISOU 736 OD1 ASP A 99 4657 4206 3782 -186 458 -218 O ATOM 737 OD2 ASP A 99 18.776 -2.028 6.073 1.00 28.91 O ANISOU 737 OD2 ASP A 99 4050 3575 3358 -164 369 -201 O ATOM 738 N GLU A 100 16.338 2.457 7.667 1.00 21.93 N ANISOU 738 N GLU A 100 3169 2903 2261 -161 157 -16 N ATOM 739 CA GLU A 100 15.165 3.178 8.148 1.00 20.69 C ANISOU 739 CA GLU A 100 3017 2792 2051 -162 100 15 C ATOM 740 C GLU A 100 15.549 4.007 9.359 1.00 21.31 C ANISOU 740 C GLU A 100 3060 2857 2181 -138 67 38 C ATOM 741 O GLU A 100 16.358 3.569 10.173 1.00 23.18 O ANISOU 741 O GLU A 100 3269 3058 2479 -128 54 34 O ATOM 742 CB GLU A 100 14.026 2.205 8.511 1.00 21.91 C ANISOU 742 CB GLU A 100 3183 2967 2174 -181 63 6 C ATOM 743 CG GLU A 100 13.561 1.320 7.354 1.00 26.16 C ANISOU 743 CG GLU A 100 3759 3519 2663 -215 84 -32 C ATOM 744 CD GLU A 100 12.663 0.170 7.786 1.00 29.28 C ANISOU 744 CD GLU A 100 4154 3909 3062 -241 53 -47 C ATOM 745 OE1 GLU A 100 12.271 0.112 8.971 1.00 31.25 O ANISOU 745 OE1 GLU A 100 4378 4156 3340 -231 20 -15 O ATOM 746 OE2 GLU A 100 12.348 -0.681 6.932 1.00 29.29 O ANISOU 746 OE2 GLU A 100 4183 3908 3037 -275 66 -93 O ATOM 747 N VAL A 101 14.961 5.195 9.476 1.00 18.76 N ANISOU 747 N VAL A 101 2736 2559 1834 -130 49 61 N ATOM 748 CA VAL A 101 15.203 6.077 10.605 1.00 18.95 C ANISOU 748 CA VAL A 101 2734 2569 1897 -113 19 65 C ATOM 749 C VAL A 101 13.884 6.415 11.300 1.00 21.04 C ANISOU 749 C VAL A 101 3003 2871 2119 -107 -14 72 C ATOM 750 O VAL A 101 12.990 7.000 10.688 1.00 22.95 O ANISOU 750 O VAL A 101 3251 3137 2332 -104 -11 91 O ATOM 751 CB VAL A 101 15.897 7.399 10.169 1.00 24.40 C ANISOU 751 CB VAL A 101 3409 3230 2631 -105 44 77 C ATOM 752 CG1 VAL A 101 16.045 8.350 11.349 1.00 22.98 C ANISOU 752 CG1 VAL A 101 3206 3032 2492 -94 9 63 C ATOM 753 CG2 VAL A 101 17.248 7.125 9.523 1.00 23.05 C ANISOU 753 CG2 VAL A 101 3221 3021 2515 -112 92 71 C ATOM 754 N ASP A 102 13.758 6.034 12.566 1.00 22.13 N ANISOU 754 N ASP A 102 3137 3017 2255 -104 -44 62 N ATOM 755 CA ASP A 102 12.585 6.403 13.355 1.00 22.72 C ANISOU 755 CA ASP A 102 3213 3127 2294 -98 -57 62 C ATOM 756 C ASP A 102 12.874 7.715 14.091 1.00 24.65 C ANISOU 756 C ASP A 102 3448 3355 2563 -80 -64 40 C ATOM 757 O ASP A 102 13.556 7.727 15.114 1.00 27.00 O ANISOU 757 O ASP A 102 3747 3645 2866 -82 -89 17 O ATOM 758 CB ASP A 102 12.212 5.301 14.353 1.00 24.42 C ANISOU 758 CB ASP A 102 3436 3363 2478 -109 -74 67 C ATOM 759 CG ASP A 102 11.726 4.014 13.678 1.00 26.44 C ANISOU 759 CG ASP A 102 3698 3624 2723 -132 -65 82 C ATOM 760 OD1 ASP A 102 12.030 3.780 12.490 1.00 26.63 O ANISOU 760 OD1 ASP A 102 3728 3633 2759 -141 -51 76 O ATOM 761 OD2 ASP A 102 11.040 3.224 14.355 1.00 24.98 O ANISOU 761 OD2 ASP A 102 3517 3457 2518 -146 -69 96 O ATOM 762 N LEU A 103 12.355 8.813 13.554 1.00 23.21 N ANISOU 762 N LEU A 103 3256 3163 2398 -65 -46 46 N ATOM 763 CA LEU A 103 12.576 10.146 14.106 1.00 22.13 C ANISOU 763 CA LEU A 103 3110 2993 2304 -49 -43 18 C ATOM 764 C LEU A 103 11.492 10.541 15.102 1.00 21.77 C ANISOU 764 C LEU A 103 3064 2972 2235 -33 -37 -10 C ATOM 765 O LEU A 103 10.307 10.350 14.839 1.00 22.29 O ANISOU 765 O LEU A 103 3119 3069 2282 -24 -22 14 O ATOM 766 CB LEU A 103 12.626 11.169 12.973 1.00 25.17 C ANISOU 766 CB LEU A 103 3483 3341 2740 -37 -20 50 C ATOM 767 CG LEU A 103 12.411 12.645 13.309 1.00 25.90 C ANISOU 767 CG LEU A 103 3561 3385 2894 -14 -7 32 C ATOM 768 CD1 LEU A 103 13.654 13.239 13.964 1.00 23.54 C ANISOU 768 CD1 LEU A 103 3258 3036 2653 -28 -17 -17 C ATOM 769 CD2 LEU A 103 12.026 13.414 12.042 1.00 26.80 C ANISOU 769 CD2 LEU A 103 3664 3474 3043 2 13 97 C ATOM 770 N VAL A 104 11.880 11.106 16.240 1.00 20.51 N ANISOU 770 N VAL A 104 2914 2800 2079 -32 -45 -64 N ATOM 771 CA VAL A 104 10.869 11.581 17.172 1.00 23.33 C ANISOU 771 CA VAL A 104 3275 3177 2411 -16 -19 -103 C ATOM 772 C VAL A 104 10.425 12.997 16.813 1.00 24.31 C ANISOU 772 C VAL A 104 3375 3247 2614 15 12 -118 C ATOM 773 O VAL A 104 11.230 13.933 16.764 1.00 24.20 O ANISOU 773 O VAL A 104 3359 3172 2662 14 7 -147 O ATOM 774 CB VAL A 104 11.347 11.557 18.632 1.00 27.10 C ANISOU 774 CB VAL A 104 3785 3676 2834 -31 -38 -166 C ATOM 775 CG1 VAL A 104 10.161 11.844 19.563 1.00 26.17 C ANISOU 775 CG1 VAL A 104 3678 3593 2671 -16 9 -206 C ATOM 776 CG2 VAL A 104 11.966 10.208 18.966 1.00 28.04 C ANISOU 776 CG2 VAL A 104 3924 3835 2894 -57 -81 -134 C ATOM 777 N PHE A 105 9.128 13.117 16.547 1.00 24.16 N ANISOU 777 N PHE A 105 3331 3246 2605 40 44 -93 N ATOM 778 CA PHE A 105 8.455 14.376 16.257 1.00 23.49 C ANISOU 778 CA PHE A 105 3212 3108 2606 80 76 -94 C ATOM 779 C PHE A 105 8.516 15.304 17.469 1.00 26.19 C ANISOU 779 C PHE A 105 3567 3413 2970 92 109 -191 C ATOM 780 O PHE A 105 8.378 14.845 18.606 1.00 28.39 O ANISOU 780 O PHE A 105 3874 3741 3171 78 122 -247 O ATOM 781 CB PHE A 105 7.000 14.079 15.862 1.00 27.09 C ANISOU 781 CB PHE A 105 3625 3602 3065 103 94 -46 C ATOM 782 CG PHE A 105 6.223 15.266 15.380 1.00 29.72 C ANISOU 782 CG PHE A 105 3910 3881 3503 152 118 -21 C ATOM 783 CD1 PHE A 105 6.209 15.603 14.036 1.00 31.20 C ANISOU 783 CD1 PHE A 105 4076 4044 3735 164 87 65 C ATOM 784 CD2 PHE A 105 5.466 16.019 16.262 1.00 31.99 C ANISOU 784 CD2 PHE A 105 4172 4142 3842 188 174 -80 C ATOM 785 CE1 PHE A 105 5.469 16.687 13.586 1.00 32.49 C ANISOU 785 CE1 PHE A 105 4189 4153 4002 214 100 106 C ATOM 786 CE2 PHE A 105 4.727 17.103 15.815 1.00 32.92 C ANISOU 786 CE2 PHE A 105 4233 4196 4078 241 197 -52 C ATOM 787 CZ PHE A 105 4.730 17.434 14.478 1.00 31.21 C ANISOU 787 CZ PHE A 105 3992 3953 3914 255 154 48 C ATOM 788 N PRO A 106 8.717 16.614 17.237 1.00 23.12 N ANISOU 788 N PRO A 106 3162 2937 2685 115 127 -212 N ATOM 789 CA PRO A 106 8.715 17.535 18.378 1.00 24.68 C ANISOU 789 CA PRO A 106 3375 3091 2910 124 163 -322 C ATOM 790 C PRO A 106 7.293 17.754 18.894 1.00 28.21 C ANISOU 790 C PRO A 106 3796 3555 3369 165 231 -349 C ATOM 791 O PRO A 106 6.645 18.749 18.552 1.00 29.84 O ANISOU 791 O PRO A 106 3958 3689 3691 211 271 -344 O ATOM 792 CB PRO A 106 9.311 18.819 17.795 1.00 22.60 C ANISOU 792 CB PRO A 106 3093 2714 2779 135 165 -323 C ATOM 793 CG PRO A 106 8.911 18.791 16.357 1.00 26.27 C ANISOU 793 CG PRO A 106 3520 3168 3295 159 157 -196 C ATOM 794 CD PRO A 106 8.887 17.319 15.954 1.00 25.08 C ANISOU 794 CD PRO A 106 3381 3119 3028 132 119 -135 C ATOM 795 N TYR A 107 6.823 16.821 19.719 1.00 27.74 N ANISOU 795 N TYR A 107 3758 3585 3198 149 247 -372 N ATOM 796 CA TYR A 107 5.429 16.802 20.142 1.00 27.53 C ANISOU 796 CA TYR A 107 3695 3587 3177 183 321 -383 C ATOM 797 C TYR A 107 5.103 17.861 21.190 1.00 27.65 C ANISOU 797 C TYR A 107 3721 3558 3228 209 399 -505 C ATOM 798 O TYR A 107 3.976 18.355 21.229 1.00 29.90 O ANISOU 798 O TYR A 107 3950 3818 3593 258 473 -514 O ATOM 799 CB TYR A 107 5.043 15.409 20.665 1.00 27.40 C ANISOU 799 CB TYR A 107 3698 3678 3034 151 323 -357 C ATOM 800 CG TYR A 107 5.869 14.886 21.828 1.00 28.42 C ANISOU 800 CG TYR A 107 3908 3861 3030 106 307 -419 C ATOM 801 CD1 TYR A 107 5.525 15.186 23.144 1.00 30.64 C ANISOU 801 CD1 TYR A 107 4228 4171 3242 106 374 -516 C ATOM 802 CD2 TYR A 107 6.976 14.067 21.610 1.00 29.75 C ANISOU 802 CD2 TYR A 107 4112 4053 3138 65 224 -378 C ATOM 803 CE1 TYR A 107 6.269 14.703 24.211 1.00 31.93 C ANISOU 803 CE1 TYR A 107 4472 4395 3267 62 345 -562 C ATOM 804 CE2 TYR A 107 7.726 13.574 22.673 1.00 32.66 C ANISOU 804 CE2 TYR A 107 4547 4472 3390 27 193 -419 C ATOM 805 CZ TYR A 107 7.366 13.898 23.972 1.00 34.23 C ANISOU 805 CZ TYR A 107 4791 4709 3508 24 247 -507 C ATOM 806 OH TYR A 107 8.102 13.415 25.032 1.00 34.88 O ANISOU 806 OH TYR A 107 4945 4851 3457 -16 205 -539 O ATOM 807 N ARG A 108 6.066 18.211 22.041 1.00 25.58 N ANISOU 807 N ARG A 108 3525 3282 2911 177 385 -605 N ATOM 808 CA ARG A 108 5.805 19.246 23.037 1.00 28.77 C ANISOU 808 CA ARG A 108 3950 3639 3342 196 461 -742 C ATOM 809 C ARG A 108 5.623 20.596 22.351 1.00 31.08 C ANISOU 809 C ARG A 108 4187 3795 3826 245 489 -750 C ATOM 810 O ARG A 108 4.790 21.401 22.769 1.00 29.87 O ANISOU 810 O ARG A 108 4007 3589 3754 291 581 -822 O ATOM 811 CB ARG A 108 6.923 19.321 24.082 1.00 29.28 C ANISOU 811 CB ARG A 108 4102 3726 3299 141 421 -853 C ATOM 812 CG ARG A 108 6.938 18.143 25.048 1.00 34.16 C ANISOU 812 CG ARG A 108 4782 4475 3721 100 411 -857 C ATOM 813 CD ARG A 108 8.007 18.297 26.123 1.00 40.45 C ANISOU 813 CD ARG A 108 5665 5300 4405 47 357 -967 C ATOM 814 NE ARG A 108 9.342 18.498 25.564 1.00 43.72 N ANISOU 814 NE ARG A 108 6074 5661 4879 16 249 -949 N ATOM 815 CZ ARG A 108 10.215 17.523 25.332 1.00 46.47 C ANISOU 815 CZ ARG A 108 6430 6060 5165 -20 154 -866 C ATOM 816 NH1 ARG A 108 9.903 16.262 25.613 1.00 49.14 N ANISOU 816 NH1 ARG A 108 6789 6501 5380 -30 146 -792 N ATOM 817 NH2 ARG A 108 11.404 17.809 24.818 1.00 46.24 N ANISOU 817 NH2 ARG A 108 6382 5974 5212 -44 72 -857 N ATOM 818 N ALA A 109 6.394 20.839 21.293 1.00 28.95 N ANISOU 818 N ALA A 109 3900 3466 3636 237 419 -672 N ATOM 819 CA ALA A 109 6.269 22.095 20.559 1.00 32.42 C ANISOU 819 CA ALA A 109 4287 3770 4260 282 441 -652 C ATOM 820 C ALA A 109 4.886 22.202 19.911 1.00 32.56 C ANISOU 820 C ALA A 109 4223 3778 4372 350 486 -564 C ATOM 821 O ALA A 109 4.286 23.281 19.870 1.00 32.83 O ANISOU 821 O ALA A 109 4209 3707 4556 407 546 -589 O ATOM 822 CB ALA A 109 7.364 22.219 19.514 1.00 31.76 C ANISOU 822 CB ALA A 109 4203 3638 4225 254 363 -567 C ATOM 823 N LEU A 110 4.377 21.077 19.420 1.00 30.79 N ANISOU 823 N LEU A 110 3976 3655 4067 344 454 -463 N ATOM 824 CA LEU A 110 3.039 21.046 18.838 1.00 29.35 C ANISOU 824 CA LEU A 110 3707 3481 3964 400 481 -378 C ATOM 825 C LEU A 110 1.987 21.335 19.907 1.00 33.21 C ANISOU 825 C LEU A 110 4166 3971 4482 438 591 -476 C ATOM 826 O LEU A 110 1.068 22.127 19.689 1.00 34.78 O ANISOU 826 O LEU A 110 4285 4097 4833 506 644 -462 O ATOM 827 CB LEU A 110 2.769 19.696 18.174 1.00 27.20 C ANISOU 827 CB LEU A 110 3422 3321 3591 370 419 -270 C ATOM 828 CG LEU A 110 1.377 19.521 17.558 1.00 28.53 C ANISOU 828 CG LEU A 110 3493 3514 3834 416 427 -180 C ATOM 829 CD1 LEU A 110 1.131 20.563 16.475 1.00 29.16 C ANISOU 829 CD1 LEU A 110 3510 3498 4070 471 398 -91 C ATOM 830 CD2 LEU A 110 1.195 18.117 17.004 1.00 26.63 C ANISOU 830 CD2 LEU A 110 3250 3383 3483 371 363 -98 C ATOM 831 N ILE A 111 2.134 20.692 21.063 1.00 32.79 N ANISOU 831 N ILE A 111 4176 3999 4282 397 628 -570 N ATOM 832 CA ILE A 111 1.252 20.918 22.206 1.00 33.62 C ANISOU 832 CA ILE A 111 4273 4119 4383 424 750 -679 C ATOM 833 C ILE A 111 1.190 22.404 22.589 1.00 34.35 C ANISOU 833 C ILE A 111 4355 4078 4620 473 826 -792 C ATOM 834 O ILE A 111 0.115 22.936 22.875 1.00 31.89 O ANISOU 834 O ILE A 111 3976 3725 4417 534 930 -830 O ATOM 835 CB ILE A 111 1.705 20.079 23.427 1.00 32.83 C ANISOU 835 CB ILE A 111 4272 4127 4075 360 766 -763 C ATOM 836 CG1 ILE A 111 1.487 18.589 23.155 1.00 32.38 C ANISOU 836 CG1 ILE A 111 4209 4189 3903 322 718 -651 C ATOM 837 CG2 ILE A 111 0.964 20.502 24.694 1.00 30.66 C ANISOU 837 CG2 ILE A 111 4010 3861 3777 382 906 -899 C ATOM 838 CD1 ILE A 111 1.980 17.682 24.267 1.00 33.44 C ANISOU 838 CD1 ILE A 111 4440 4428 3838 260 721 -701 C ATOM 839 N GLN A 112 2.339 23.073 22.564 1.00 34.00 N ANISOU 839 N GLN A 112 4368 3956 4593 446 778 -846 N ATOM 840 CA GLN A 112 2.403 24.500 22.870 1.00 40.75 C ANISOU 840 CA GLN A 112 5218 4666 5600 484 842 -958 C ATOM 841 C GLN A 112 1.909 25.375 21.717 1.00 40.99 C ANISOU 841 C GLN A 112 5149 4568 5858 556 838 -849 C ATOM 842 O GLN A 112 1.837 26.593 21.850 1.00 43.11 O ANISOU 842 O GLN A 112 5397 4694 6291 598 897 -922 O ATOM 843 CB GLN A 112 3.831 24.900 23.238 1.00 45.26 C ANISOU 843 CB GLN A 112 5879 5196 6124 420 784 -1052 C ATOM 844 CG GLN A 112 4.382 24.182 24.451 1.00 51.93 C ANISOU 844 CG GLN A 112 6825 6158 6747 351 775 -1164 C ATOM 845 CD GLN A 112 5.892 24.293 24.545 1.00 60.18 C ANISOU 845 CD GLN A 112 7938 7187 7742 280 673 -1207 C ATOM 846 OE1 GLN A 112 6.502 25.163 23.919 1.00 62.21 O ANISOU 846 OE1 GLN A 112 8172 7320 8147 282 640 -1197 O ATOM 847 NE2 GLN A 112 6.505 23.400 25.316 1.00 63.22 N ANISOU 847 NE2 GLN A 112 8400 7695 7925 216 621 -1244 N ATOM 848 N GLY A 113 1.591 24.760 20.582 1.00 41.59 N ANISOU 848 N GLY A 113 5168 4692 5943 567 764 -674 N ATOM 849 CA GLY A 113 0.984 25.483 19.476 1.00 42.67 C ANISOU 849 CA GLY A 113 5208 4730 6276 638 750 -549 C ATOM 850 C GLY A 113 1.867 25.760 18.269 1.00 43.45 C ANISOU 850 C GLY A 113 5317 4773 6417 619 648 -424 C ATOM 851 O GLY A 113 1.451 26.466 17.351 1.00 46.67 O ANISOU 851 O GLY A 113 5655 5092 6984 677 632 -310 O ATOM 852 N ASN A 114 3.078 25.209 18.263 1.00 38.79 N ANISOU 852 N ASN A 114 4811 4237 5689 542 583 -436 N ATOM 853 CA ASN A 114 4.006 25.394 17.151 1.00 34.48 C ANISOU 853 CA ASN A 114 4280 3649 5170 516 503 -323 C ATOM 854 C ASN A 114 3.936 24.208 16.183 1.00 34.77 C ANISOU 854 C ASN A 114 4313 3813 5085 491 420 -181 C ATOM 855 O ASN A 114 4.492 23.139 16.450 1.00 31.01 O ANISOU 855 O ASN A 114 3892 3445 4447 431 385 -206 O ATOM 856 CB ASN A 114 5.432 25.579 17.684 1.00 35.47 C ANISOU 856 CB ASN A 114 4486 3743 5246 447 486 -426 C ATOM 857 CG ASN A 114 6.441 25.928 16.592 1.00 38.51 C ANISOU 857 CG ASN A 114 4879 4066 5688 420 426 -319 C ATOM 858 OD1 ASN A 114 6.174 25.784 15.400 1.00 39.91 O ANISOU 858 OD1 ASN A 114 5022 4256 5885 441 387 -160 O ATOM 859 ND2 ASN A 114 7.620 26.375 17.008 1.00 38.43 N ANISOU 859 ND2 ASN A 114 4914 3993 5696 368 419 -407 N ATOM 860 N GLU A 115 3.249 24.407 15.061 1.00 37.35 N ANISOU 860 N GLU A 115 4575 4124 5493 537 387 -34 N ATOM 861 CA GLU A 115 3.065 23.355 14.063 1.00 40.07 C ANISOU 861 CA GLU A 115 4914 4585 5727 513 307 93 C ATOM 862 C GLU A 115 4.166 23.377 13.004 1.00 39.31 C ANISOU 862 C GLU A 115 4866 4476 5595 473 246 187 C ATOM 863 O GLU A 115 4.357 22.405 12.272 1.00 41.41 O ANISOU 863 O GLU A 115 5156 4843 5738 435 186 259 O ATOM 864 CB GLU A 115 1.694 23.490 13.384 1.00 43.17 C ANISOU 864 CB GLU A 115 5210 4985 6208 578 287 206 C ATOM 865 CG GLU A 115 0.510 23.449 14.344 1.00 48.31 C ANISOU 865 CG GLU A 115 5793 5649 6912 623 360 125 C ATOM 866 CD GLU A 115 -0.834 23.401 13.630 1.00 53.83 C ANISOU 866 CD GLU A 115 6381 6375 7698 679 324 244 C ATOM 867 OE1 GLU A 115 -0.856 23.454 12.381 1.00 55.25 O ANISOU 867 OE1 GLU A 115 6542 6562 7887 685 234 391 O ATOM 868 OE2 GLU A 115 -1.873 23.308 14.322 1.00 56.72 O ANISOU 868 OE2 GLU A 115 6674 6757 8120 716 387 192 O ATOM 869 N THR A 116 4.884 24.492 12.929 1.00 36.26 N ANISOU 869 N THR A 116 4492 3961 5324 479 270 180 N ATOM 870 CA THR A 116 5.877 24.696 11.883 1.00 34.23 C ANISOU 870 CA THR A 116 4270 3675 5062 446 232 281 C ATOM 871 C THR A 116 7.136 23.869 12.111 1.00 32.49 C ANISOU 871 C THR A 116 4118 3519 4707 367 215 219 C ATOM 872 O THR A 116 7.629 23.222 11.183 1.00 33.63 O ANISOU 872 O THR A 116 4289 3729 4758 333 174 307 O ATOM 873 CB THR A 116 6.265 26.184 11.768 1.00 33.19 C ANISOU 873 CB THR A 116 4122 3370 5119 473 271 297 C ATOM 874 OG1 THR A 116 5.082 26.967 11.579 1.00 35.82 O ANISOU 874 OG1 THR A 116 4382 3629 5597 556 288 359 O ATOM 875 CG2 THR A 116 7.195 26.403 10.592 1.00 33.24 C ANISOU 875 CG2 THR A 116 4159 3349 5123 440 243 426 C ATOM 876 N ILE A 117 7.650 23.885 13.340 1.00 29.28 N ANISOU 876 N ILE A 117 3739 3096 4291 340 246 68 N ATOM 877 CA ILE A 117 8.906 23.205 13.649 1.00 27.71 C ANISOU 877 CA ILE A 117 3593 2945 3991 269 223 9 C ATOM 878 C ILE A 117 8.780 21.700 13.388 1.00 29.44 C ANISOU 878 C ILE A 117 3832 3311 4042 243 180 45 C ATOM 879 O ILE A 117 9.730 21.063 12.940 1.00 30.90 O ANISOU 879 O ILE A 117 4048 3536 4158 196 152 72 O ATOM 880 CB ILE A 117 9.357 23.468 15.114 1.00 29.91 C ANISOU 880 CB ILE A 117 3897 3194 4274 245 247 -163 C ATOM 881 CG1 ILE A 117 10.718 22.822 15.397 1.00 30.10 C ANISOU 881 CG1 ILE A 117 3962 3261 4212 175 207 -209 C ATOM 882 CG2 ILE A 117 8.315 22.978 16.110 1.00 29.00 C ANISOU 882 CG2 ILE A 117 3780 3151 4087 270 274 -244 C ATOM 883 CD1 ILE A 117 11.829 23.291 14.479 1.00 32.46 C ANISOU 883 CD1 ILE A 117 4256 3488 4590 144 196 -138 C ATOM 884 N GLY A 118 7.591 21.151 13.627 1.00 30.20 N ANISOU 884 N GLY A 118 3905 3478 4091 272 182 47 N ATOM 885 CA GLY A 118 7.323 19.753 13.349 1.00 28.39 C ANISOU 885 CA GLY A 118 3689 3374 3725 247 145 83 C ATOM 886 C GLY A 118 7.382 19.442 11.868 1.00 27.81 C ANISOU 886 C GLY A 118 3615 3331 3621 240 102 213 C ATOM 887 O GLY A 118 7.978 18.443 11.456 1.00 26.75 O ANISOU 887 O GLY A 118 3516 3265 3384 196 74 229 O ATOM 888 N PHE A 119 6.764 20.303 11.064 1.00 28.09 N ANISOU 888 N PHE A 119 3612 3316 3746 284 97 307 N ATOM 889 CA PHE A 119 6.785 20.139 9.615 1.00 27.58 C ANISOU 889 CA PHE A 119 3556 3285 3639 277 54 439 C ATOM 890 C PHE A 119 8.201 20.255 9.050 1.00 26.90 C ANISOU 890 C PHE A 119 3520 3167 3532 233 65 462 C ATOM 891 O PHE A 119 8.644 19.393 8.291 1.00 28.36 O ANISOU 891 O PHE A 119 3743 3427 3607 195 44 500 O ATOM 892 CB PHE A 119 5.874 21.167 8.939 1.00 28.80 C ANISOU 892 CB PHE A 119 3657 3381 3904 338 40 548 C ATOM 893 CG PHE A 119 5.821 21.030 7.446 1.00 28.69 C ANISOU 893 CG PHE A 119 3660 3415 3826 329 -14 693 C ATOM 894 CD1 PHE A 119 6.746 21.677 6.639 1.00 31.35 C ANISOU 894 CD1 PHE A 119 4034 3695 4181 315 0 773 C ATOM 895 CD2 PHE A 119 4.854 20.240 6.847 1.00 28.87 C ANISOU 895 CD2 PHE A 119 3662 3544 3764 330 -80 749 C ATOM 896 CE1 PHE A 119 6.701 21.540 5.259 1.00 33.13 C ANISOU 896 CE1 PHE A 119 4287 3977 4322 303 -44 908 C ATOM 897 CE2 PHE A 119 4.806 20.097 5.473 1.00 28.22 C ANISOU 897 CE2 PHE A 119 3606 3518 3599 316 -138 874 C ATOM 898 CZ PHE A 119 5.726 20.744 4.679 1.00 29.69 C ANISOU 898 CZ PHE A 119 3840 3656 3785 304 -118 955 C ATOM 899 N ASP A 120 8.899 21.328 9.411 1.00 26.61 N ANISOU 899 N ASP A 120 3481 3017 3612 238 105 434 N ATOM 900 CA ASP A 120 10.242 21.578 8.886 1.00 27.03 C ANISOU 900 CA ASP A 120 3566 3027 3677 196 126 462 C ATOM 901 C ASP A 120 11.216 20.458 9.249 1.00 24.04 C ANISOU 901 C ASP A 120 3220 2716 3196 140 122 384 C ATOM 902 O ASP A 120 12.045 20.063 8.438 1.00 24.83 O ANISOU 902 O ASP A 120 3347 2842 3247 105 130 432 O ATOM 903 CB ASP A 120 10.786 22.914 9.398 1.00 29.32 C ANISOU 903 CB ASP A 120 3837 3172 4131 203 168 424 C ATOM 904 CG ASP A 120 9.986 24.101 8.900 1.00 34.65 C ANISOU 904 CG ASP A 120 4477 3754 4934 261 179 521 C ATOM 905 OD1 ASP A 120 9.124 23.913 8.014 1.00 34.88 O ANISOU 905 OD1 ASP A 120 4497 3839 4918 292 144 637 O ATOM 906 OD2 ASP A 120 10.229 25.225 9.392 1.00 36.46 O ANISOU 906 OD2 ASP A 120 4686 3850 5317 274 216 480 O ATOM 907 N MET A 121 11.102 19.941 10.464 1.00 26.40 N ANISOU 907 N MET A 121 3519 3046 3467 134 114 269 N ATOM 908 CA MET A 121 12.013 18.898 10.922 1.00 27.29 C ANISOU 908 CA MET A 121 3656 3214 3498 88 102 202 C ATOM 909 C MET A 121 11.808 17.592 10.149 1.00 27.67 C ANISOU 909 C MET A 121 3726 3366 3420 72 79 252 C ATOM 910 O MET A 121 12.770 16.983 9.688 1.00 28.58 O ANISOU 910 O MET A 121 3861 3502 3497 37 86 260 O ATOM 911 CB MET A 121 11.845 18.656 12.425 1.00 25.57 C ANISOU 911 CB MET A 121 3439 3012 3265 86 92 81 C ATOM 912 CG MET A 121 12.833 17.636 12.972 1.00 28.20 C ANISOU 912 CG MET A 121 3794 3396 3527 42 68 25 C ATOM 913 SD MET A 121 12.661 17.289 14.732 1.00 33.06 S ANISOU 913 SD MET A 121 4425 4047 4091 35 48 -99 S ATOM 914 CE MET A 121 13.128 18.869 15.453 1.00 26.56 C ANISOU 914 CE MET A 121 3590 3109 3391 35 66 -185 C ATOM 915 N VAL A 122 10.560 17.162 10.009 1.00 28.31 N ANISOU 915 N VAL A 122 3799 3508 3449 96 57 278 N ATOM 916 CA VAL A 122 10.272 15.945 9.254 1.00 27.22 C ANISOU 916 CA VAL A 122 3681 3462 3198 75 31 315 C ATOM 917 C VAL A 122 10.700 16.120 7.795 1.00 24.52 C ANISOU 917 C VAL A 122 3364 3123 2829 63 37 409 C ATOM 918 O VAL A 122 11.303 15.222 7.209 1.00 24.88 O ANISOU 918 O VAL A 122 3442 3215 2796 28 43 409 O ATOM 919 CB VAL A 122 8.770 15.559 9.329 1.00 24.13 C ANISOU 919 CB VAL A 122 3263 3129 2775 99 -1 330 C ATOM 920 CG1 VAL A 122 8.438 14.459 8.321 1.00 20.27 C ANISOU 920 CG1 VAL A 122 2795 2725 2181 71 -36 373 C ATOM 921 CG2 VAL A 122 8.407 15.112 10.736 1.00 20.10 C ANISOU 921 CG2 VAL A 122 2739 2635 2261 100 8 239 C ATOM 922 N LYS A 123 10.411 17.287 7.223 1.00 23.65 N ANISOU 922 N LYS A 123 3239 2959 2786 91 43 489 N ATOM 923 CA LYS A 123 10.767 17.557 5.835 1.00 22.13 C ANISOU 923 CA LYS A 123 3077 2773 2557 79 53 594 C ATOM 924 C LYS A 123 12.272 17.452 5.582 1.00 23.11 C ANISOU 924 C LYS A 123 3229 2870 2683 39 109 578 C ATOM 925 O LYS A 123 12.681 16.749 4.664 1.00 22.39 O ANISOU 925 O LYS A 123 3178 2837 2494 9 124 606 O ATOM 926 CB LYS A 123 10.273 18.940 5.399 1.00 25.05 C ANISOU 926 CB LYS A 123 3423 3072 3022 121 52 695 C ATOM 927 CG LYS A 123 10.661 19.292 3.968 1.00 27.25 C ANISOU 927 CG LYS A 123 3742 3360 3253 107 65 823 C ATOM 928 CD LYS A 123 10.198 20.687 3.578 1.00 33.46 C ANISOU 928 CD LYS A 123 4503 4062 4149 151 62 940 C ATOM 929 CE LYS A 123 10.924 21.178 2.332 1.00 39.20 C ANISOU 929 CE LYS A 123 5275 4775 4843 128 99 1067 C ATOM 930 NZ LYS A 123 10.437 22.513 1.888 1.00 45.32 N ANISOU 930 NZ LYS A 123 6027 5464 5727 173 91 1205 N ATOM 931 N VAL A 124 13.101 18.138 6.374 1.00 23.39 N ANISOU 931 N VAL A 124 3240 2816 2833 35 141 528 N ATOM 932 CA VAL A 124 14.545 18.081 6.120 1.00 22.73 C ANISOU 932 CA VAL A 124 3162 2700 2773 -5 194 518 C ATOM 933 C VAL A 124 15.083 16.670 6.388 1.00 21.31 C ANISOU 933 C VAL A 124 2996 2589 2513 -34 190 441 C ATOM 934 O VAL A 124 15.995 16.206 5.701 1.00 24.14 O ANISOU 934 O VAL A 124 3368 2961 2841 -63 235 455 O ATOM 935 CB VAL A 124 15.360 19.124 6.958 1.00 23.71 C ANISOU 935 CB VAL A 124 3247 2709 3051 -12 218 471 C ATOM 936 CG1 VAL A 124 15.034 20.541 6.515 1.00 26.87 C ANISOU 936 CG1 VAL A 124 3636 3018 3554 12 239 558 C ATOM 937 CG2 VAL A 124 15.128 18.953 8.450 1.00 25.40 C ANISOU 937 CG2 VAL A 124 3440 2918 3293 -3 177 350 C ATOM 938 N CYS A 125 14.515 15.979 7.368 1.00 20.65 N ANISOU 938 N CYS A 125 2904 2543 2399 -24 144 366 N ATOM 939 CA CYS A 125 14.965 14.623 7.653 1.00 24.90 C ANISOU 939 CA CYS A 125 3453 3136 2874 -47 136 306 C ATOM 940 C CYS A 125 14.544 13.662 6.529 1.00 26.79 C ANISOU 940 C CYS A 125 3732 3452 2995 -58 140 344 C ATOM 941 O CYS A 125 15.258 12.705 6.227 1.00 25.43 O ANISOU 941 O CYS A 125 3573 3302 2786 -82 166 316 O ATOM 942 CB CYS A 125 14.438 14.151 9.014 1.00 26.35 C ANISOU 942 CB CYS A 125 3622 3338 3051 -36 89 229 C ATOM 943 SG CYS A 125 15.246 14.964 10.450 1.00 27.96 S ANISOU 943 SG CYS A 125 3793 3467 3362 -40 79 150 S ATOM 944 N LYS A 126 13.406 13.931 5.891 1.00 25.33 N ANISOU 944 N LYS A 126 3562 3304 2758 -42 112 404 N ATOM 945 CA LYS A 126 12.996 13.136 4.730 1.00 24.73 C ANISOU 945 CA LYS A 126 3530 3306 2562 -61 105 438 C ATOM 946 C LYS A 126 13.955 13.347 3.561 1.00 25.01 C ANISOU 946 C LYS A 126 3602 3337 2565 -84 171 488 C ATOM 947 O LYS A 126 14.331 12.395 2.866 1.00 24.58 O ANISOU 947 O LYS A 126 3585 3329 2424 -112 200 464 O ATOM 948 CB LYS A 126 11.569 13.484 4.299 1.00 25.39 C ANISOU 948 CB LYS A 126 3611 3433 2604 -39 46 501 C ATOM 949 CG LYS A 126 11.084 12.703 3.085 1.00 23.03 C ANISOU 949 CG LYS A 126 3359 3222 2169 -66 20 530 C ATOM 950 CD LYS A 126 11.137 11.199 3.330 1.00 22.36 C ANISOU 950 CD LYS A 126 3290 3180 2027 -98 16 438 C ATOM 951 CE LYS A 126 10.478 10.424 2.193 1.00 23.90 C ANISOU 951 CE LYS A 126 3529 3461 2089 -130 -22 449 C ATOM 952 NZ LYS A 126 9.043 10.802 1.980 1.00 25.86 N ANISOU 952 NZ LYS A 126 3751 3756 2319 -115 -109 508 N ATOM 953 N GLN A 127 14.343 14.599 3.344 1.00 25.00 N ANISOU 953 N GLN A 127 3588 3273 2637 -73 203 555 N ATOM 954 CA GLN A 127 15.304 14.932 2.295 1.00 25.49 C ANISOU 954 CA GLN A 127 3680 3324 2683 -97 281 615 C ATOM 955 C GLN A 127 16.625 14.199 2.515 1.00 25.72 C ANISOU 955 C GLN A 127 3696 3333 2744 -124 347 539 C ATOM 956 O GLN A 127 17.207 13.658 1.574 1.00 26.44 O ANISOU 956 O GLN A 127 3825 3460 2761 -149 413 546 O ATOM 957 CB GLN A 127 15.537 16.444 2.238 1.00 24.44 C ANISOU 957 CB GLN A 127 3522 3103 2659 -82 307 699 C ATOM 958 CG GLN A 127 14.292 17.230 1.878 1.00 31.46 C ANISOU 958 CG GLN A 127 4419 4001 3534 -48 248 794 C ATOM 959 CD GLN A 127 14.507 18.728 1.907 1.00 39.28 C ANISOU 959 CD GLN A 127 5382 4884 4660 -29 275 876 C ATOM 960 OE1 GLN A 127 15.106 19.263 2.840 1.00 43.70 O ANISOU 960 OE1 GLN A 127 5894 5351 5359 -28 297 817 O ATOM 961 NE2 GLN A 127 14.017 19.414 0.882 1.00 38.99 N ANISOU 961 NE2 GLN A 127 5374 4856 4585 -16 269 1013 N ATOM 962 N ALA A 128 17.082 14.176 3.764 1.00 24.34 N ANISOU 962 N ALA A 128 3466 3104 2678 -117 329 465 N ATOM 963 CA ALA A 128 18.335 13.519 4.116 1.00 27.08 C ANISOU 963 CA ALA A 128 3782 3426 3081 -136 373 400 C ATOM 964 C ALA A 128 18.272 12.005 3.891 1.00 28.82 C ANISOU 964 C ALA A 128 4031 3710 3210 -145 374 343 C ATOM 965 O ALA A 128 19.287 11.374 3.585 1.00 31.66 O ANISOU 965 O ALA A 128 4380 4060 3590 -161 440 312 O ATOM 966 CB ALA A 128 18.697 13.823 5.565 1.00 26.01 C ANISOU 966 CB ALA A 128 3586 3231 3065 -128 327 337 C ATOM 967 N CYS A 129 17.079 11.434 4.039 1.00 27.92 N ANISOU 967 N CYS A 129 3945 3652 3011 -136 308 328 N ATOM 968 CA CYS A 129 16.880 9.989 3.905 1.00 28.54 C ANISOU 968 CA CYS A 129 4049 3779 3016 -148 301 269 C ATOM 969 C CYS A 129 16.743 9.532 2.464 1.00 32.80 C ANISOU 969 C CYS A 129 4654 4377 3433 -171 347 286 C ATOM 970 O CYS A 129 16.940 8.353 2.162 1.00 36.33 O ANISOU 970 O CYS A 129 5124 4845 3835 -188 372 225 O ATOM 971 CB CYS A 129 15.630 9.547 4.665 1.00 25.64 C ANISOU 971 CB CYS A 129 3680 3445 2616 -136 214 245 C ATOM 972 SG CYS A 129 15.817 9.413 6.437 1.00 27.19 S ANISOU 972 SG CYS A 129 3822 3599 2911 -119 167 193 S ATOM 973 N SER A 130 16.381 10.460 1.583 1.00 32.16 N ANISOU 973 N SER A 130 4607 4320 3294 -173 355 369 N ATOM 974 CA SER A 130 15.993 10.107 0.222 1.00 33.49 C ANISOU 974 CA SER A 130 4851 4566 3310 -199 374 393 C ATOM 975 C SER A 130 17.105 9.378 -0.525 1.00 33.61 C ANISOU 975 C SER A 130 4897 4583 3291 -225 485 344 C ATOM 976 O SER A 130 18.252 9.824 -0.557 1.00 32.73 O ANISOU 976 O SER A 130 4756 4418 3261 -225 572 359 O ATOM 977 CB SER A 130 15.559 11.360 -0.547 1.00 38.75 C ANISOU 977 CB SER A 130 5543 5250 3931 -193 364 513 C ATOM 978 OG SER A 130 14.296 11.827 -0.075 1.00 38.52 O ANISOU 978 OG SER A 130 5490 5232 3912 -167 259 552 O ATOM 979 N GLY A 131 16.756 8.233 -1.103 1.00 32.52 N ANISOU 979 N GLY A 131 4812 4502 3043 -249 485 278 N ATOM 980 CA GLY A 131 17.709 7.444 -1.862 1.00 33.01 C ANISOU 980 CA GLY A 131 4910 4567 3066 -272 599 215 C ATOM 981 C GLY A 131 18.540 6.524 -0.987 1.00 31.84 C ANISOU 981 C GLY A 131 4699 4347 3052 -258 634 125 C ATOM 982 O GLY A 131 19.437 5.841 -1.474 1.00 32.19 O ANISOU 982 O GLY A 131 4752 4372 3105 -268 738 65 O ATOM 983 N ASN A 132 18.249 6.505 0.310 1.00 29.68 N ANISOU 983 N ASN A 132 4362 4031 2884 -234 549 119 N ATOM 984 CA ASN A 132 18.999 5.658 1.230 1.00 30.70 C ANISOU 984 CA ASN A 132 4430 4095 3141 -217 562 53 C ATOM 985 C ASN A 132 18.130 4.964 2.268 1.00 30.55 C ANISOU 985 C ASN A 132 4393 4073 3141 -209 459 23 C ATOM 986 O ASN A 132 18.374 3.808 2.610 1.00 30.69 O ANISOU 986 O ASN A 132 4397 4059 3203 -207 466 -40 O ATOM 987 CB ASN A 132 20.080 6.474 1.947 1.00 29.66 C ANISOU 987 CB ASN A 132 4218 3895 3156 -197 587 86 C ATOM 988 CG ASN A 132 21.311 6.689 1.089 1.00 30.11 C ANISOU 988 CG ASN A 132 4266 3928 3246 -206 719 91 C ATOM 989 OD1 ASN A 132 22.034 5.740 0.768 1.00 31.48 O ANISOU 989 OD1 ASN A 132 4431 4080 3450 -207 798 28 O ATOM 990 ND2 ASN A 132 21.560 7.936 0.719 1.00 28.12 N ANISOU 990 ND2 ASN A 132 4011 3673 3002 -213 752 167 N ATOM 991 N ALA A 133 17.121 5.664 2.778 1.00 26.34 N ANISOU 991 N ALA A 133 3855 3567 2585 -201 370 71 N ATOM 992 CA ALA A 133 16.361 5.128 3.898 1.00 25.85 C ANISOU 992 CA ALA A 133 3767 3500 2553 -192 287 51 C ATOM 993 C ALA A 133 14.913 5.589 3.920 1.00 28.66 C ANISOU 993 C ALA A 133 4140 3912 2838 -195 208 88 C ATOM 994 O ALA A 133 14.564 6.612 3.333 1.00 30.18 O ANISOU 994 O ALA A 133 4347 4132 2986 -192 202 147 O ATOM 995 CB ALA A 133 17.035 5.504 5.207 1.00 24.23 C ANISOU 995 CB ALA A 133 3497 3240 2468 -166 266 59 C ATOM 996 N LYS A 134 14.073 4.826 4.615 1.00 24.49 N ANISOU 996 N LYS A 134 3601 3394 2312 -200 151 62 N ATOM 997 CA LYS A 134 12.710 5.254 4.878 1.00 27.60 C ANISOU 997 CA LYS A 134 3985 3830 2671 -198 79 96 C ATOM 998 C LYS A 134 12.635 6.028 6.190 1.00 25.97 C ANISOU 998 C LYS A 134 3730 3595 2543 -165 53 120 C ATOM 999 O LYS A 134 13.397 5.779 7.126 1.00 26.23 O ANISOU 999 O LYS A 134 3739 3584 2642 -154 64 97 O ATOM 1000 CB LYS A 134 11.763 4.053 4.906 1.00 29.32 C ANISOU 1000 CB LYS A 134 4211 4075 2855 -227 39 56 C ATOM 1001 CG LYS A 134 11.697 3.338 3.580 1.00 33.90 C ANISOU 1001 CG LYS A 134 4845 4688 3345 -267 55 17 C ATOM 1002 CD LYS A 134 10.673 2.233 3.584 1.00 38.12 C ANISOU 1002 CD LYS A 134 5382 5244 3857 -305 7 -27 C ATOM 1003 CE LYS A 134 10.740 1.466 2.278 1.00 41.99 C ANISOU 1003 CE LYS A 134 5935 5761 4256 -350 27 -90 C ATOM 1004 NZ LYS A 134 12.144 1.066 1.966 1.00 42.97 N ANISOU 1004 NZ LYS A 134 6088 5834 4405 -343 124 -137 N ATOM 1005 N LEU A 135 11.709 6.975 6.249 1.00 25.93 N ANISOU 1005 N LEU A 135 3710 3614 2529 -149 15 165 N ATOM 1006 CA LEU A 135 11.539 7.796 7.439 1.00 21.17 C ANISOU 1006 CA LEU A 135 3067 2983 1993 -118 0 175 C ATOM 1007 C LEU A 135 10.263 7.441 8.193 1.00 21.54 C ANISOU 1007 C LEU A 135 3088 3060 2034 -116 -41 168 C ATOM 1008 O LEU A 135 9.158 7.622 7.682 1.00 23.13 O ANISOU 1008 O LEU A 135 3279 3302 2208 -117 -73 198 O ATOM 1009 CB LEU A 135 11.516 9.278 7.062 1.00 22.06 C ANISOU 1009 CB LEU A 135 3171 3078 2132 -94 6 228 C ATOM 1010 CG LEU A 135 11.488 10.254 8.242 1.00 20.74 C ANISOU 1010 CG LEU A 135 2968 2867 2045 -63 2 220 C ATOM 1011 CD1 LEU A 135 12.786 10.173 9.030 1.00 18.31 C ANISOU 1011 CD1 LEU A 135 2654 2512 1789 -68 24 176 C ATOM 1012 CD2 LEU A 135 11.223 11.678 7.766 1.00 21.03 C ANISOU 1012 CD2 LEU A 135 2993 2876 2121 -37 6 279 C ATOM 1013 N LYS A 136 10.422 6.934 9.410 1.00 21.39 N ANISOU 1013 N LYS A 136 3056 3025 2044 -115 -41 135 N ATOM 1014 CA LYS A 136 9.293 6.755 10.312 1.00 21.14 C ANISOU 1014 CA LYS A 136 2999 3019 2015 -111 -60 133 C ATOM 1015 C LYS A 136 9.271 7.926 11.281 1.00 22.10 C ANISOU 1015 C LYS A 136 3100 3120 2178 -77 -51 129 C ATOM 1016 O LYS A 136 10.322 8.384 11.725 1.00 24.88 O ANISOU 1016 O LYS A 136 3462 3435 2559 -68 -39 110 O ATOM 1017 CB LYS A 136 9.383 5.434 11.086 1.00 21.97 C ANISOU 1017 CB LYS A 136 3111 3124 2114 -134 -60 108 C ATOM 1018 CG LYS A 136 9.683 4.188 10.259 1.00 22.39 C ANISOU 1018 CG LYS A 136 3187 3172 2147 -168 -59 93 C ATOM 1019 CD LYS A 136 9.096 2.942 10.924 1.00 20.78 C ANISOU 1019 CD LYS A 136 2977 2970 1947 -194 -65 86 C ATOM 1020 CE LYS A 136 9.704 1.658 10.376 1.00 24.68 C ANISOU 1020 CE LYS A 136 3496 3431 2450 -222 -54 59 C ATOM 1021 NZ LYS A 136 11.048 1.375 10.965 1.00 24.90 N ANISOU 1021 NZ LYS A 136 3532 3409 2520 -204 -37 55 N ATOM 1022 N VAL A 137 8.080 8.411 11.615 1.00 24.23 N ANISOU 1022 N VAL A 137 3337 3410 2459 -59 -54 140 N ATOM 1023 CA VAL A 137 7.960 9.539 12.535 1.00 23.57 C ANISOU 1023 CA VAL A 137 3236 3301 2419 -25 -34 122 C ATOM 1024 C VAL A 137 7.162 9.171 13.782 1.00 24.93 C ANISOU 1024 C VAL A 137 3394 3501 2579 -24 -16 94 C ATOM 1025 O VAL A 137 5.975 8.843 13.705 1.00 26.68 O ANISOU 1025 O VAL A 137 3579 3757 2802 -26 -14 113 O ATOM 1026 CB VAL A 137 7.304 10.752 11.852 1.00 21.25 C ANISOU 1026 CB VAL A 137 2910 2990 2175 9 -35 160 C ATOM 1027 CG1 VAL A 137 7.139 11.883 12.842 1.00 23.13 C ANISOU 1027 CG1 VAL A 137 3129 3187 2472 44 -4 125 C ATOM 1028 CG2 VAL A 137 8.137 11.197 10.659 1.00 20.05 C ANISOU 1028 CG2 VAL A 137 2781 2811 2025 5 -43 199 C ATOM 1029 N ILE A 138 7.827 9.230 14.930 1.00 25.00 N ANISOU 1029 N ILE A 138 3427 3498 2573 -25 -3 52 N ATOM 1030 CA ILE A 138 7.196 8.970 16.222 1.00 24.44 C ANISOU 1030 CA ILE A 138 3357 3459 2470 -26 25 25 C ATOM 1031 C ILE A 138 6.508 10.220 16.758 1.00 28.30 C ANISOU 1031 C ILE A 138 3822 3934 2998 11 66 -9 C ATOM 1032 O ILE A 138 7.176 11.224 17.022 1.00 26.96 O ANISOU 1032 O ILE A 138 3666 3721 2856 27 69 -49 O ATOM 1033 CB ILE A 138 8.229 8.503 17.264 1.00 22.94 C ANISOU 1033 CB ILE A 138 3214 3273 2231 -45 12 -3 C ATOM 1034 CG1 ILE A 138 8.948 7.244 16.781 1.00 20.70 C ANISOU 1034 CG1 ILE A 138 2946 2988 1931 -73 -22 31 C ATOM 1035 CG2 ILE A 138 7.566 8.279 18.611 1.00 23.99 C ANISOU 1035 CG2 ILE A 138 3360 3449 2306 -48 47 -24 C ATOM 1036 CD1 ILE A 138 10.163 6.884 17.615 1.00 22.59 C ANISOU 1036 CD1 ILE A 138 3218 3219 2145 -84 -52 18 C ATOM 1037 N ILE A 139 5.189 10.174 16.938 1.00 28.16 N ANISOU 1037 N ILE A 139 3760 3944 2995 23 102 1 N ATOM 1038 CA ILE A 139 4.491 11.369 17.413 1.00 29.21 C ANISOU 1038 CA ILE A 139 3861 4055 3184 66 153 -36 C ATOM 1039 C ILE A 139 4.225 11.362 18.926 1.00 29.07 C ANISOU 1039 C ILE A 139 3866 4065 3112 64 215 -99 C ATOM 1040 O ILE A 139 3.850 12.394 19.494 1.00 30.92 O ANISOU 1040 O ILE A 139 4088 4273 3386 98 269 -156 O ATOM 1041 CB ILE A 139 3.158 11.586 16.658 1.00 29.47 C ANISOU 1041 CB ILE A 139 3813 4093 3292 92 161 13 C ATOM 1042 CG1 ILE A 139 2.236 10.373 16.781 1.00 30.69 C ANISOU 1042 CG1 ILE A 139 3935 4309 3417 61 169 44 C ATOM 1043 CG2 ILE A 139 3.425 11.907 15.191 1.00 28.25 C ANISOU 1043 CG2 ILE A 139 3644 3911 3178 100 99 73 C ATOM 1044 CD1 ILE A 139 0.868 10.612 16.165 1.00 30.68 C ANISOU 1044 CD1 ILE A 139 3838 4318 3502 85 171 87 C ATOM 1045 N GLU A 140 4.445 10.213 19.568 1.00 26.77 N ANISOU 1045 N GLU A 140 3615 3824 2732 25 211 -89 N ATOM 1046 CA GLU A 140 4.285 10.051 21.020 1.00 24.73 C ANISOU 1046 CA GLU A 140 3397 3609 2390 14 266 -134 C ATOM 1047 C GLU A 140 2.846 10.325 21.471 1.00 26.03 C ANISOU 1047 C GLU A 140 3509 3797 2586 37 359 -148 C ATOM 1048 O GLU A 140 2.573 11.281 22.204 1.00 25.95 O ANISOU 1048 O GLU A 140 3503 3775 2581 65 424 -222 O ATOM 1049 CB GLU A 140 5.260 10.952 21.782 1.00 24.52 C ANISOU 1049 CB GLU A 140 3428 3559 2328 21 257 -216 C ATOM 1050 CG GLU A 140 5.567 10.481 23.201 1.00 26.58 C ANISOU 1050 CG GLU A 140 3761 3881 2458 -8 273 -250 C ATOM 1051 CD GLU A 140 6.482 9.269 23.230 1.00 27.82 C ANISOU 1051 CD GLU A 140 3957 4063 2550 -47 198 -187 C ATOM 1052 OE1 GLU A 140 6.016 8.148 22.931 1.00 25.01 O ANISOU 1052 OE1 GLU A 140 3583 3731 2190 -65 201 -112 O ATOM 1053 OE2 GLU A 140 7.676 9.442 23.553 1.00 28.82 O ANISOU 1053 OE2 GLU A 140 4128 4181 2643 -60 133 -215 O ATOM 1054 N THR A 141 1.937 9.460 21.037 1.00 27.48 N ANISOU 1054 N THR A 141 3637 4008 2795 21 369 -83 N ATOM 1055 CA THR A 141 0.512 9.622 21.298 1.00 27.56 C ANISOU 1055 CA THR A 141 3571 4038 2861 40 454 -83 C ATOM 1056 C THR A 141 0.183 9.619 22.792 1.00 27.92 C ANISOU 1056 C THR A 141 3655 4129 2823 34 558 -134 C ATOM 1057 O THR A 141 -0.770 10.264 23.226 1.00 27.88 O ANISOU 1057 O THR A 141 3600 4126 2869 67 654 -173 O ATOM 1058 CB THR A 141 -0.289 8.516 20.601 1.00 27.38 C ANISOU 1058 CB THR A 141 3484 4042 2878 7 433 -3 C ATOM 1059 OG1 THR A 141 0.181 7.239 21.046 1.00 26.49 O ANISOU 1059 OG1 THR A 141 3429 3961 2674 -47 418 30 O ATOM 1060 CG2 THR A 141 -0.109 8.610 19.097 1.00 25.68 C ANISOU 1060 CG2 THR A 141 3233 3793 2733 13 337 38 C ATOM 1061 N GLY A 142 0.980 8.895 23.572 1.00 27.42 N ANISOU 1061 N GLY A 142 3682 4105 2633 -6 540 -130 N ATOM 1062 CA GLY A 142 0.819 8.873 25.013 1.00 30.58 C ANISOU 1062 CA GLY A 142 4142 4560 2918 -18 628 -174 C ATOM 1063 C GLY A 142 0.994 10.240 25.660 1.00 34.32 C ANISOU 1063 C GLY A 142 4647 5015 3377 19 678 -290 C ATOM 1064 O GLY A 142 0.444 10.499 26.732 1.00 32.31 O ANISOU 1064 O GLY A 142 4418 4802 3057 23 787 -347 O ATOM 1065 N GLU A 143 1.768 11.115 25.021 1.00 31.74 N ANISOU 1065 N GLU A 143 4323 4621 3113 44 607 -329 N ATOM 1066 CA GLU A 143 1.953 12.472 25.534 1.00 33.16 C ANISOU 1066 CA GLU A 143 4528 4762 3309 78 650 -447 C ATOM 1067 C GLU A 143 1.002 13.459 24.865 1.00 32.81 C ANISOU 1067 C GLU A 143 4383 4648 3433 138 708 -465 C ATOM 1068 O GLU A 143 0.596 14.446 25.475 1.00 35.65 O ANISOU 1068 O GLU A 143 4741 4980 3826 173 798 -562 O ATOM 1069 CB GLU A 143 3.396 12.938 25.339 1.00 32.88 C ANISOU 1069 CB GLU A 143 4551 4683 3258 66 545 -483 C ATOM 1070 CG GLU A 143 4.419 12.173 26.165 1.00 36.69 C ANISOU 1070 CG GLU A 143 5129 5229 3583 14 482 -480 C ATOM 1071 CD GLU A 143 4.213 12.336 27.654 1.00 38.22 C ANISOU 1071 CD GLU A 143 5400 5490 3633 -1 557 -565 C ATOM 1072 OE1 GLU A 143 3.732 13.404 28.088 1.00 42.76 O ANISOU 1072 OE1 GLU A 143 5972 6038 4235 28 644 -673 O ATOM 1073 OE2 GLU A 143 4.530 11.390 28.394 1.00 41.52 O ANISOU 1073 OE2 GLU A 143 5883 5986 3907 -42 534 -522 O ATOM 1074 N LEU A 144 0.652 13.192 23.611 1.00 30.22 N ANISOU 1074 N LEU A 144 3974 4292 3214 150 653 -372 N ATOM 1075 CA LEU A 144 -0.295 14.039 22.890 1.00 29.91 C ANISOU 1075 CA LEU A 144 3830 4194 3341 209 688 -361 C ATOM 1076 C LEU A 144 -1.691 13.940 23.498 1.00 31.26 C ANISOU 1076 C LEU A 144 3930 4399 3548 230 813 -373 C ATOM 1077 O LEU A 144 -2.434 14.922 23.516 1.00 34.21 O ANISOU 1077 O LEU A 144 4234 4721 4045 288 887 -416 O ATOM 1078 CB LEU A 144 -0.335 13.663 21.407 1.00 27.80 C ANISOU 1078 CB LEU A 144 3502 3908 3152 208 586 -251 C ATOM 1079 CG LEU A 144 0.925 14.017 20.612 1.00 26.88 C ANISOU 1079 CG LEU A 144 3435 3742 3038 201 484 -237 C ATOM 1080 CD1 LEU A 144 0.797 13.562 19.174 1.00 26.15 C ANISOU 1080 CD1 LEU A 144 3292 3647 2996 195 397 -132 C ATOM 1081 CD2 LEU A 144 1.197 15.516 20.679 1.00 27.02 C ANISOU 1081 CD2 LEU A 144 3451 3668 3146 249 510 -306 C ATOM 1082 N LYS A 145 -2.026 12.741 23.974 1.00 30.35 N ANISOU 1082 N LYS A 145 3828 4366 3339 182 839 -330 N ATOM 1083 CA LYS A 145 -3.281 12.442 24.668 1.00 33.31 C ANISOU 1083 CA LYS A 145 4141 4787 3729 185 970 -333 C ATOM 1084 C LYS A 145 -4.532 12.583 23.793 1.00 37.43 C ANISOU 1084 C LYS A 145 4507 5282 4434 223 984 -273 C ATOM 1085 O LYS A 145 -5.131 11.577 23.407 1.00 39.68 O ANISOU 1085 O LYS A 145 4732 5607 4739 187 964 -188 O ATOM 1086 CB LYS A 145 -3.421 13.315 25.923 1.00 36.30 C ANISOU 1086 CB LYS A 145 4567 5167 4060 213 1105 -460 C ATOM 1087 CG LYS A 145 -2.442 12.948 27.038 1.00 35.67 C ANISOU 1087 CG LYS A 145 4637 5147 3768 162 1104 -513 C ATOM 1088 N SER A 146 -4.928 13.813 23.476 1.00 36.42 N ANISOU 1088 N SER A 146 4310 5080 4448 294 1013 -312 N ATOM 1089 CA SER A 146 -6.200 14.039 22.782 1.00 37.49 C ANISOU 1089 CA SER A 146 4285 5191 4768 339 1031 -255 C ATOM 1090 C SER A 146 -6.221 13.493 21.350 1.00 37.01 C ANISOU 1090 C SER A 146 4167 5132 4764 320 878 -137 C ATOM 1091 O SER A 146 -5.190 13.437 20.682 1.00 34.83 O ANISOU 1091 O SER A 146 3966 4839 4428 300 762 -113 O ATOM 1092 CB SER A 146 -6.532 15.530 22.757 1.00 37.41 C ANISOU 1092 CB SER A 146 4216 5088 4910 427 1090 -317 C ATOM 1093 OG SER A 146 -5.735 16.215 21.808 1.00 38.71 O ANISOU 1093 OG SER A 146 4407 5181 5121 450 970 -291 O ATOM 1094 N GLU A 147 -7.407 13.098 20.890 1.00 37.83 N ANISOU 1094 N GLU A 147 4134 5257 4982 323 880 -70 N ATOM 1095 CA GLU A 147 -7.605 12.670 19.509 1.00 39.10 C ANISOU 1095 CA GLU A 147 4229 5423 5204 306 734 32 C ATOM 1096 C GLU A 147 -7.239 13.782 18.525 1.00 37.47 C ANISOU 1096 C GLU A 147 4011 5145 5081 365 643 58 C ATOM 1097 O GLU A 147 -6.684 13.527 17.454 1.00 34.33 O ANISOU 1097 O GLU A 147 3645 4751 4646 341 510 120 O ATOM 1098 CB GLU A 147 -9.055 12.232 19.286 1.00 45.12 C ANISOU 1098 CB GLU A 147 4826 6217 6099 304 756 89 C ATOM 1099 CG GLU A 147 -9.453 12.142 17.820 1.00 52.73 C ANISOU 1099 CG GLU A 147 5698 7180 7156 304 600 185 C ATOM 1100 CD GLU A 147 -10.878 11.658 17.615 1.00 62.65 C ANISOU 1100 CD GLU A 147 6782 8472 8551 293 607 239 C ATOM 1101 OE1 GLU A 147 -11.361 10.831 18.422 1.00 65.81 O ANISOU 1101 OE1 GLU A 147 7159 8914 8931 245 705 221 O ATOM 1102 OE2 GLU A 147 -11.516 12.107 16.639 1.00 67.32 O ANISOU 1102 OE2 GLU A 147 7256 9048 9275 330 511 306 O ATOM 1103 N GLU A 148 -7.549 15.017 18.903 1.00 37.49 N ANISOU 1103 N GLU A 148 3970 5079 5198 444 724 10 N ATOM 1104 CA GLU A 148 -7.260 16.173 18.070 1.00 37.68 C ANISOU 1104 CA GLU A 148 3977 5017 5323 507 656 41 C ATOM 1105 C GLU A 148 -5.766 16.332 17.763 1.00 32.48 C ANISOU 1105 C GLU A 148 3463 4334 4543 478 581 27 C ATOM 1106 O GLU A 148 -5.382 16.501 16.612 1.00 32.04 O ANISOU 1106 O GLU A 148 3412 4259 4501 479 464 107 O ATOM 1107 CB GLU A 148 -7.787 17.438 18.742 1.00 45.19 C ANISOU 1107 CB GLU A 148 4867 5883 6422 594 782 -29 C ATOM 1108 CG GLU A 148 -7.553 18.687 17.930 1.00 55.21 C ANISOU 1108 CG GLU A 148 6110 7045 7822 664 721 12 C ATOM 1109 CD GLU A 148 -7.742 19.944 18.744 1.00 64.64 C ANISOU 1109 CD GLU A 148 7284 8134 9142 741 856 -90 C ATOM 1110 OE1 GLU A 148 -7.932 19.829 19.976 1.00 69.80 O ANISOU 1110 OE1 GLU A 148 7964 8809 9748 733 998 -206 O ATOM 1111 OE2 GLU A 148 -7.700 21.044 18.153 1.00 65.87 O ANISOU 1111 OE2 GLU A 148 7399 8183 9443 808 824 -53 O ATOM 1112 N LEU A 149 -4.932 16.275 18.796 1.00 30.43 N ANISOU 1112 N LEU A 149 3319 4078 4164 450 649 -73 N ATOM 1113 CA LEU A 149 -3.491 16.450 18.631 1.00 29.20 C ANISOU 1113 CA LEU A 149 3289 3896 3909 422 586 -96 C ATOM 1114 C LEU A 149 -2.860 15.267 17.915 1.00 30.05 C ANISOU 1114 C LEU A 149 3451 4070 3897 352 476 -27 C ATOM 1115 O LEU A 149 -1.942 15.424 17.114 1.00 28.55 O ANISOU 1115 O LEU A 149 3314 3855 3680 340 391 8 O ATOM 1116 CB LEU A 149 -2.820 16.654 19.988 1.00 31.82 C ANISOU 1116 CB LEU A 149 3722 4225 4143 406 676 -223 C ATOM 1117 CG LEU A 149 -2.957 18.056 20.578 1.00 35.24 C ANISOU 1117 CG LEU A 149 4143 4564 4684 471 770 -319 C ATOM 1118 CD1 LEU A 149 -2.569 18.066 22.047 1.00 35.02 C ANISOU 1118 CD1 LEU A 149 4209 4562 4535 446 869 -456 C ATOM 1119 CD2 LEU A 149 -2.094 19.028 19.791 1.00 36.17 C ANISOU 1119 CD2 LEU A 149 4286 4583 4874 494 695 -301 C ATOM 1120 N ILE A 150 -3.358 14.077 18.212 1.00 31.47 N ANISOU 1120 N ILE A 150 3615 4328 4012 304 489 -11 N ATOM 1121 CA ILE A 150 -2.861 12.875 17.567 1.00 31.37 C ANISOU 1121 CA ILE A 150 3647 4370 3902 237 396 45 C ATOM 1122 C ILE A 150 -3.148 12.928 16.067 1.00 29.05 C ANISOU 1122 C ILE A 150 3295 4071 3673 245 286 137 C ATOM 1123 O ILE A 150 -2.292 12.604 15.244 1.00 28.91 O ANISOU 1123 O ILE A 150 3339 4056 3588 213 201 169 O ATOM 1124 CB ILE A 150 -3.488 11.621 18.203 1.00 29.02 C ANISOU 1124 CB ILE A 150 3331 4143 3550 186 441 49 C ATOM 1125 CG1 ILE A 150 -2.952 11.446 19.629 1.00 26.66 C ANISOU 1125 CG1 ILE A 150 3124 3864 3142 167 531 -27 C ATOM 1126 CG2 ILE A 150 -3.206 10.391 17.361 1.00 25.26 C ANISOU 1126 CG2 ILE A 150 2876 3706 3015 121 343 109 C ATOM 1127 CD1 ILE A 150 -3.710 10.412 20.460 1.00 25.29 C ANISOU 1127 CD1 ILE A 150 2928 3753 2927 125 609 -19 C ATOM 1128 N ARG A 151 -4.355 13.357 15.720 1.00 29.46 N ANISOU 1128 N ARG A 151 3223 4116 3854 287 289 179 N ATOM 1129 CA ARG A 151 -4.731 13.526 14.325 1.00 31.32 C ANISOU 1129 CA ARG A 151 3398 4354 4150 299 174 274 C ATOM 1130 C ARG A 151 -3.854 14.589 13.670 1.00 30.92 C ANISOU 1130 C ARG A 151 3401 4236 4111 337 131 298 C ATOM 1131 O ARG A 151 -3.267 14.356 12.609 1.00 29.93 O ANISOU 1131 O ARG A 151 3324 4127 3922 309 35 354 O ATOM 1132 CB ARG A 151 -6.211 13.908 14.213 1.00 36.01 C ANISOU 1132 CB ARG A 151 3834 4946 4901 347 187 317 C ATOM 1133 CG ARG A 151 -6.693 14.134 12.791 1.00 41.44 C ANISOU 1133 CG ARG A 151 4450 5644 5652 362 52 426 C ATOM 1134 CD ARG A 151 -8.203 14.360 12.740 1.00 47.40 C ANISOU 1134 CD ARG A 151 5030 6406 6574 404 54 472 C ATOM 1135 NE ARG A 151 -8.607 15.618 13.372 1.00 54.96 N ANISOU 1135 NE ARG A 151 5920 7279 7682 498 154 449 N ATOM 1136 CZ ARG A 151 -9.316 15.704 14.497 1.00 57.86 C ANISOU 1136 CZ ARG A 151 6217 7634 8132 524 292 381 C ATOM 1137 NH1 ARG A 151 -9.636 16.896 14.991 1.00 57.66 N ANISOU 1137 NH1 ARG A 151 6136 7522 8250 613 385 351 N ATOM 1138 NH2 ARG A 151 -9.708 14.599 15.126 1.00 57.40 N ANISOU 1138 NH2 ARG A 151 6147 7646 8018 462 345 345 N ATOM 1139 N LYS A 152 -3.763 15.749 14.322 1.00 28.18 N ANISOU 1139 N LYS A 152 3049 3810 3847 398 210 250 N ATOM 1140 CA LYS A 152 -2.962 16.864 13.829 1.00 31.20 C ANISOU 1140 CA LYS A 152 3475 4110 4269 435 186 270 C ATOM 1141 C LYS A 152 -1.515 16.448 13.548 1.00 30.13 C ANISOU 1141 C LYS A 152 3466 3985 3996 378 143 256 C ATOM 1142 O LYS A 152 -0.996 16.661 12.448 1.00 31.27 O ANISOU 1142 O LYS A 152 3639 4119 4125 373 67 331 O ATOM 1143 CB LYS A 152 -2.990 18.020 14.837 1.00 33.38 C ANISOU 1143 CB LYS A 152 3742 4295 4647 495 297 184 C ATOM 1144 CG LYS A 152 -2.379 19.317 14.319 1.00 33.74 C ANISOU 1144 CG LYS A 152 3806 4231 4784 541 279 213 C ATOM 1145 N ALA A 153 -0.872 15.847 14.542 1.00 27.92 N ANISOU 1145 N ALA A 153 3260 3730 3617 336 195 167 N ATOM 1146 CA ALA A 153 0.513 15.420 14.406 1.00 27.32 C ANISOU 1146 CA ALA A 153 3290 3662 3429 286 160 149 C ATOM 1147 C ALA A 153 0.666 14.426 13.257 1.00 28.20 C ANISOU 1147 C ALA A 153 3417 3835 3465 239 71 223 C ATOM 1148 O ALA A 153 1.647 14.469 12.515 1.00 28.66 O ANISOU 1148 O ALA A 153 3534 3879 3478 219 28 251 O ATOM 1149 CB ALA A 153 1.011 14.809 15.710 1.00 24.15 C ANISOU 1149 CB ALA A 153 2952 3290 2936 250 217 55 C ATOM 1150 N SER A 154 -0.310 13.535 13.113 1.00 27.26 N ANISOU 1150 N SER A 154 3243 3780 3334 217 50 250 N ATOM 1151 CA SER A 154 -0.276 12.540 12.049 1.00 28.42 C ANISOU 1151 CA SER A 154 3404 3986 3410 167 -33 303 C ATOM 1152 C SER A 154 -0.349 13.199 10.682 1.00 27.63 C ANISOU 1152 C SER A 154 3286 3875 3337 189 -111 390 C ATOM 1153 O SER A 154 0.372 12.813 9.760 1.00 27.17 O ANISOU 1153 O SER A 154 3291 3838 3196 153 -164 418 O ATOM 1154 CB SER A 154 -1.425 11.542 12.204 1.00 30.90 C ANISOU 1154 CB SER A 154 3649 4362 3731 136 -41 309 C ATOM 1155 OG SER A 154 -1.248 10.748 13.360 1.00 31.92 O ANISOU 1155 OG SER A 154 3810 4507 3809 104 26 246 O ATOM 1156 N GLU A 155 -1.224 14.195 10.561 1.00 23.73 N ANISOU 1156 N GLU A 155 2708 3348 2961 250 -113 436 N ATOM 1157 CA GLU A 155 -1.411 14.910 9.303 1.00 26.49 C ANISOU 1157 CA GLU A 155 3034 3687 3345 279 -192 541 C ATOM 1158 C GLU A 155 -0.170 15.720 8.940 1.00 27.86 C ANISOU 1158 C GLU A 155 3289 3796 3500 290 -180 557 C ATOM 1159 O GLU A 155 0.272 15.697 7.792 1.00 28.88 O ANISOU 1159 O GLU A 155 3463 3947 3562 269 -243 628 O ATOM 1160 CB GLU A 155 -2.646 15.818 9.375 1.00 27.15 C ANISOU 1160 CB GLU A 155 2994 3736 3586 351 -192 592 C ATOM 1161 CG GLU A 155 -3.945 15.033 9.469 1.00 33.77 C ANISOU 1161 CG GLU A 155 3729 4643 4458 336 -221 599 C ATOM 1162 CD GLU A 155 -5.171 15.914 9.583 1.00 40.14 C ANISOU 1162 CD GLU A 155 4397 5412 5443 413 -214 649 C ATOM 1163 OE1 GLU A 155 -5.030 17.091 9.975 1.00 42.64 O ANISOU 1163 OE1 GLU A 155 4700 5635 5864 482 -151 644 O ATOM 1164 OE2 GLU A 155 -6.281 15.424 9.281 1.00 42.40 O ANISOU 1164 OE2 GLU A 155 4578 5756 5775 404 -272 690 O ATOM 1165 N ILE A 156 0.397 16.417 9.920 1.00 27.21 N ANISOU 1165 N ILE A 156 3229 3636 3472 316 -96 488 N ATOM 1166 CA ILE A 156 1.612 17.198 9.695 1.00 28.90 C ANISOU 1166 CA ILE A 156 3512 3780 3690 320 -77 493 C ATOM 1167 C ILE A 156 2.764 16.293 9.258 1.00 30.28 C ANISOU 1167 C ILE A 156 3777 4000 3726 253 -97 477 C ATOM 1168 O ILE A 156 3.439 16.576 8.269 1.00 31.92 O ANISOU 1168 O ILE A 156 4028 4197 3903 242 -124 542 O ATOM 1169 CB ILE A 156 2.028 17.986 10.954 1.00 29.22 C ANISOU 1169 CB ILE A 156 3561 3733 3809 347 12 395 C ATOM 1170 CG1 ILE A 156 0.943 19.000 11.330 1.00 29.60 C ANISOU 1170 CG1 ILE A 156 3519 3717 4013 421 49 403 C ATOM 1171 CG2 ILE A 156 3.354 18.696 10.720 1.00 30.32 C ANISOU 1171 CG2 ILE A 156 3765 3798 3957 336 26 394 C ATOM 1172 CD1 ILE A 156 1.225 19.764 12.609 1.00 29.76 C ANISOU 1172 CD1 ILE A 156 3549 3654 4106 446 144 285 C ATOM 1173 N ALA A 157 2.965 15.196 9.983 1.00 27.26 N ANISOU 1173 N ALA A 157 3422 3666 3268 210 -78 398 N ATOM 1174 CA ALA A 157 4.041 14.260 9.673 1.00 26.24 C ANISOU 1174 CA ALA A 157 3369 3572 3028 152 -89 375 C ATOM 1175 C ALA A 157 3.925 13.738 8.239 1.00 24.70 C ANISOU 1175 C ALA A 157 3191 3435 2758 124 -155 450 C ATOM 1176 O ALA A 157 4.906 13.724 7.492 1.00 26.27 O ANISOU 1176 O ALA A 157 3450 3629 2903 101 -157 471 O ATOM 1177 CB ALA A 157 4.042 13.107 10.667 1.00 24.62 C ANISOU 1177 CB ALA A 157 3177 3408 2769 117 -66 297 C ATOM 1178 N ILE A 158 2.719 13.341 7.847 1.00 23.60 N ANISOU 1178 N ILE A 158 2999 3353 2616 123 -208 487 N ATOM 1179 CA ILE A 158 2.493 12.842 6.494 1.00 22.29 C ANISOU 1179 CA ILE A 158 2851 3253 2366 91 -285 549 C ATOM 1180 C ILE A 158 2.702 13.928 5.434 1.00 24.15 C ANISOU 1180 C ILE A 158 3102 3467 2609 120 -315 651 C ATOM 1181 O ILE A 158 3.367 13.692 4.426 1.00 24.56 O ANISOU 1181 O ILE A 158 3222 3549 2561 86 -334 683 O ATOM 1182 CB ILE A 158 1.088 12.250 6.358 1.00 26.90 C ANISOU 1182 CB ILE A 158 3360 3901 2961 80 -347 565 C ATOM 1183 CG1 ILE A 158 1.017 10.919 7.112 1.00 28.49 C ANISOU 1183 CG1 ILE A 158 3566 4132 3126 31 -322 477 C ATOM 1184 CG2 ILE A 158 0.721 12.047 4.893 1.00 23.64 C ANISOU 1184 CG2 ILE A 158 2959 3557 2468 54 -446 639 C ATOM 1185 CD1 ILE A 158 -0.337 10.249 7.024 1.00 28.58 C ANISOU 1185 CD1 ILE A 158 3496 4201 3162 9 -377 486 C ATOM 1186 N ASN A 159 2.141 15.112 5.670 1.00 25.62 N ANISOU 1186 N ASN A 159 3225 3594 2916 183 -311 704 N ATOM 1187 CA ASN A 159 2.347 16.261 4.787 1.00 26.54 C ANISOU 1187 CA ASN A 159 3350 3668 3064 218 -331 816 C ATOM 1188 C ASN A 159 3.823 16.568 4.562 1.00 26.51 C ANISOU 1188 C ASN A 159 3433 3618 3022 197 -273 809 C ATOM 1189 O ASN A 159 4.231 16.921 3.455 1.00 26.78 O ANISOU 1189 O ASN A 159 3513 3663 3001 188 -294 900 O ATOM 1190 CB ASN A 159 1.658 17.505 5.351 1.00 25.32 C ANISOU 1190 CB ASN A 159 3112 3426 3082 295 -311 851 C ATOM 1191 CG ASN A 159 0.163 17.489 5.131 1.00 35.77 C ANISOU 1191 CG ASN A 159 4335 4794 4464 328 -385 911 C ATOM 1192 OD1 ASN A 159 -0.340 16.738 4.293 1.00 39.19 O ANISOU 1192 OD1 ASN A 159 4766 5324 4802 292 -473 953 O ATOM 1193 ND2 ASN A 159 -0.562 18.328 5.874 1.00 34.63 N ANISOU 1193 ND2 ASN A 159 4100 4575 4483 397 -349 909 N ATOM 1194 N ALA A 160 4.617 16.417 5.619 1.00 24.15 N ANISOU 1194 N ALA A 160 3154 3272 2752 186 -199 704 N ATOM 1195 CA ALA A 160 6.030 16.769 5.579 1.00 25.02 C ANISOU 1195 CA ALA A 160 3323 3324 2858 166 -141 688 C ATOM 1196 C ALA A 160 6.913 15.673 4.969 1.00 25.96 C ANISOU 1196 C ALA A 160 3513 3507 2843 105 -136 661 C ATOM 1197 O ALA A 160 8.087 15.915 4.679 1.00 25.52 O ANISOU 1197 O ALA A 160 3501 3415 2781 86 -88 665 O ATOM 1198 CB ALA A 160 6.516 17.116 6.982 1.00 25.71 C ANISOU 1198 CB ALA A 160 3395 3336 3036 179 -79 585 C ATOM 1199 N GLY A 161 6.363 14.473 4.790 1.00 23.51 N ANISOU 1199 N GLY A 161 3209 3284 2441 73 -178 629 N ATOM 1200 CA GLY A 161 7.053 13.441 4.036 1.00 23.33 C ANISOU 1200 CA GLY A 161 3251 3317 2294 19 -173 605 C ATOM 1201 C GLY A 161 7.329 12.124 4.743 1.00 27.10 C ANISOU 1201 C GLY A 161 3740 3818 2738 -17 -156 499 C ATOM 1202 O GLY A 161 8.138 11.324 4.272 1.00 27.76 O ANISOU 1202 O GLY A 161 3877 3922 2749 -56 -131 464 O ATOM 1203 N ALA A 162 6.658 11.887 5.865 1.00 24.98 N ANISOU 1203 N ALA A 162 3423 3543 2526 -2 -162 450 N ATOM 1204 CA ALA A 162 6.829 10.639 6.603 1.00 22.69 C ANISOU 1204 CA ALA A 162 3141 3270 2209 -35 -149 367 C ATOM 1205 C ALA A 162 6.461 9.425 5.748 1.00 23.85 C ANISOU 1205 C ALA A 162 3313 3484 2263 -83 -188 356 C ATOM 1206 O ALA A 162 5.453 9.442 5.037 1.00 22.61 O ANISOU 1206 O ALA A 162 3135 3378 2077 -88 -249 399 O ATOM 1207 CB ALA A 162 5.992 10.657 7.870 1.00 21.02 C ANISOU 1207 CB ALA A 162 2874 3050 2062 -13 -145 335 C ATOM 1208 N ASP A 163 7.284 8.381 5.815 1.00 23.04 N ANISOU 1208 N ASP A 163 3252 3377 2123 -118 -158 296 N ATOM 1209 CA ASP A 163 6.997 7.130 5.112 1.00 24.02 C ANISOU 1209 CA ASP A 163 3404 3549 2172 -168 -185 262 C ATOM 1210 C ASP A 163 6.180 6.212 6.008 1.00 21.78 C ANISOU 1210 C ASP A 163 3079 3273 1923 -185 -202 222 C ATOM 1211 O ASP A 163 5.432 5.361 5.524 1.00 22.39 O ANISOU 1211 O ASP A 163 3152 3391 1965 -225 -245 205 O ATOM 1212 CB ASP A 163 8.288 6.433 4.675 1.00 24.07 C ANISOU 1212 CB ASP A 163 3471 3535 2139 -193 -131 215 C ATOM 1213 CG ASP A 163 9.071 7.241 3.653 1.00 26.84 C ANISOU 1213 CG ASP A 163 3865 3887 2447 -186 -100 258 C ATOM 1214 OD1 ASP A 163 8.464 7.695 2.659 1.00 25.73 O ANISOU 1214 OD1 ASP A 163 3740 3797 2238 -192 -142 312 O ATOM 1215 OD2 ASP A 163 10.293 7.428 3.852 1.00 26.13 O ANISOU 1215 OD2 ASP A 163 3788 3747 2392 -176 -36 243 O ATOM 1216 N PHE A 164 6.352 6.396 7.315 1.00 22.63 N ANISOU 1216 N PHE A 164 3160 3341 2096 -159 -168 208 N ATOM 1217 CA PHE A 164 5.571 5.725 8.355 1.00 22.50 C ANISOU 1217 CA PHE A 164 3103 3329 2116 -169 -169 187 C ATOM 1218 C PHE A 164 5.201 6.736 9.424 1.00 26.12 C ANISOU 1218 C PHE A 164 3520 3772 2634 -123 -146 203 C ATOM 1219 O PHE A 164 5.957 7.682 9.670 1.00 30.07 O ANISOU 1219 O PHE A 164 4034 4236 3155 -89 -121 206 O ATOM 1220 CB PHE A 164 6.360 4.594 9.022 1.00 21.81 C ANISOU 1220 CB PHE A 164 3047 3211 2030 -193 -136 142 C ATOM 1221 CG PHE A 164 6.300 3.282 8.304 1.00 24.35 C ANISOU 1221 CG PHE A 164 3393 3540 2320 -244 -151 109 C ATOM 1222 CD1 PHE A 164 6.980 3.091 7.112 1.00 27.55 C ANISOU 1222 CD1 PHE A 164 3847 3947 2675 -262 -149 89 C ATOM 1223 CD2 PHE A 164 5.600 2.217 8.850 1.00 24.51 C ANISOU 1223 CD2 PHE A 164 3389 3558 2365 -278 -156 94 C ATOM 1224 CE1 PHE A 164 6.932 1.869 6.460 1.00 29.31 C ANISOU 1224 CE1 PHE A 164 4097 4169 2870 -311 -156 41 C ATOM 1225 CE2 PHE A 164 5.548 0.996 8.202 1.00 26.00 C ANISOU 1225 CE2 PHE A 164 3599 3739 2540 -329 -168 54 C ATOM 1226 CZ PHE A 164 6.216 0.821 7.008 1.00 27.12 C ANISOU 1226 CZ PHE A 164 3793 3880 2630 -345 -169 20 C ATOM 1227 N ILE A 165 4.063 6.533 10.078 1.00 24.79 N ANISOU 1227 N ILE A 165 3297 3625 2498 -123 -148 205 N ATOM 1228 CA ILE A 165 3.814 7.218 11.339 1.00 24.66 C ANISOU 1228 CA ILE A 165 3252 3591 2528 -86 -103 196 C ATOM 1229 C ILE A 165 3.761 6.188 12.467 1.00 24.95 C ANISOU 1229 C ILE A 165 3295 3633 2551 -113 -69 168 C ATOM 1230 O ILE A 165 3.200 5.093 12.317 1.00 26.40 O ANISOU 1230 O ILE A 165 3464 3838 2730 -155 -82 171 O ATOM 1231 CB ILE A 165 2.524 8.069 11.311 1.00 24.67 C ANISOU 1231 CB ILE A 165 3176 3608 2591 -52 -109 228 C ATOM 1232 CG1 ILE A 165 1.328 7.255 10.819 1.00 24.43 C ANISOU 1232 CG1 ILE A 165 3088 3625 2570 -87 -151 249 C ATOM 1233 CG2 ILE A 165 2.725 9.296 10.434 1.00 22.47 C ANISOU 1233 CG2 ILE A 165 2895 3308 2336 -13 -135 269 C ATOM 1234 CD1 ILE A 165 0.008 7.996 10.955 1.00 25.38 C ANISOU 1234 CD1 ILE A 165 3111 3759 2774 -51 -152 282 C ATOM 1235 N LYS A 166 4.368 6.546 13.593 1.00 23.25 N ANISOU 1235 N LYS A 166 3106 3397 2331 -93 -29 143 N ATOM 1236 CA LYS A 166 4.614 5.610 14.683 1.00 24.14 C ANISOU 1236 CA LYS A 166 3244 3514 2413 -117 -3 129 C ATOM 1237 C LYS A 166 4.069 6.171 15.990 1.00 25.67 C ANISOU 1237 C LYS A 166 3424 3724 2607 -94 51 112 C ATOM 1238 O LYS A 166 4.144 7.377 16.216 1.00 26.54 O ANISOU 1238 O LYS A 166 3528 3818 2737 -55 68 88 O ATOM 1239 CB LYS A 166 6.121 5.334 14.788 1.00 22.96 C ANISOU 1239 CB LYS A 166 3154 3333 2236 -122 -17 114 C ATOM 1240 CG LYS A 166 6.551 4.530 15.993 1.00 19.11 C ANISOU 1240 CG LYS A 166 2698 2848 1715 -137 -3 114 C ATOM 1241 CD LYS A 166 7.989 4.088 15.825 1.00 23.61 C ANISOU 1241 CD LYS A 166 3306 3382 2283 -142 -31 110 C ATOM 1242 CE LYS A 166 8.559 3.607 17.128 1.00 25.12 C ANISOU 1242 CE LYS A 166 3528 3577 2441 -147 -34 118 C ATOM 1243 NZ LYS A 166 9.993 3.243 17.028 1.00 28.02 N ANISOU 1243 NZ LYS A 166 3915 3905 2827 -145 -68 119 N ATOM 1244 N THR A 167 3.529 5.313 16.855 1.00 24.82 N ANISOU 1244 N THR A 167 3312 3642 2476 -120 85 123 N ATOM 1245 CA THR A 167 2.834 5.817 18.034 1.00 25.31 C ANISOU 1245 CA THR A 167 3359 3730 2528 -101 153 105 C ATOM 1246 C THR A 167 3.772 6.381 19.089 1.00 27.39 C ANISOU 1246 C THR A 167 3686 3989 2731 -84 168 63 C ATOM 1247 O THR A 167 3.527 7.466 19.614 1.00 25.89 O ANISOU 1247 O THR A 167 3490 3798 2549 -51 209 18 O ATOM 1248 CB THR A 167 1.965 4.730 18.718 1.00 24.26 C ANISOU 1248 CB THR A 167 3206 3630 2382 -140 198 137 C ATOM 1249 OG1 THR A 167 2.803 3.681 19.222 1.00 24.71 O ANISOU 1249 OG1 THR A 167 3326 3683 2381 -172 182 159 O ATOM 1250 CG2 THR A 167 0.942 4.160 17.748 1.00 25.05 C ANISOU 1250 CG2 THR A 167 3231 3735 2552 -166 178 169 C ATOM 1251 N SER A 168 4.836 5.641 19.406 1.00 24.65 N ANISOU 1251 N SER A 168 3397 3637 2332 -107 132 74 N ATOM 1252 CA SER A 168 5.532 5.854 20.675 1.00 26.34 C ANISOU 1252 CA SER A 168 3670 3869 2469 -105 141 46 C ATOM 1253 C SER A 168 7.016 5.525 20.656 1.00 23.59 C ANISOU 1253 C SER A 168 3367 3496 2100 -114 71 51 C ATOM 1254 O SER A 168 7.477 4.742 19.836 1.00 22.28 O ANISOU 1254 O SER A 168 3194 3301 1969 -128 33 87 O ATOM 1255 CB SER A 168 4.867 5.010 21.774 1.00 23.69 C ANISOU 1255 CB SER A 168 3351 3582 2066 -132 193 79 C ATOM 1256 OG SER A 168 3.454 5.023 21.648 1.00 24.37 O ANISOU 1256 OG SER A 168 3377 3688 2196 -132 259 89 O ATOM 1257 N THR A 169 7.748 6.105 21.600 1.00 24.99 N ANISOU 1257 N THR A 169 3589 3686 2222 -108 57 11 N ATOM 1258 CA THR A 169 9.162 5.795 21.791 1.00 25.46 C ANISOU 1258 CA THR A 169 3680 3728 2265 -117 -16 18 C ATOM 1259 C THR A 169 9.368 4.603 22.718 1.00 27.65 C ANISOU 1259 C THR A 169 3997 4040 2469 -141 -35 77 C ATOM 1260 O THR A 169 10.464 4.056 22.805 1.00 29.18 O ANISOU 1260 O THR A 169 4204 4216 2667 -147 -101 107 O ATOM 1261 CB THR A 169 9.928 6.994 22.383 1.00 24.17 C ANISOU 1261 CB THR A 169 3542 3561 2082 -105 -42 -56 C ATOM 1262 OG1 THR A 169 9.394 7.310 23.678 1.00 24.80 O ANISOU 1262 OG1 THR A 169 3663 3696 2062 -110 -4 -94 O ATOM 1263 CG2 THR A 169 9.820 8.202 21.474 1.00 20.05 C ANISOU 1263 CG2 THR A 169 2981 2988 1649 -80 -23 -102 C ATOM 1264 N GLY A 170 8.317 4.218 23.435 1.00 28.12 N ANISOU 1264 N GLY A 170 4070 4147 2467 -154 25 101 N ATOM 1265 CA GLY A 170 8.444 3.196 24.458 1.00 25.55 C ANISOU 1265 CA GLY A 170 3791 3860 2058 -179 16 169 C ATOM 1266 C GLY A 170 8.996 3.736 25.769 1.00 27.30 C ANISOU 1266 C GLY A 170 4078 4138 2157 -181 -11 136 C ATOM 1267 O GLY A 170 9.068 3.008 26.763 1.00 28.70 O ANISOU 1267 O GLY A 170 4306 4363 2237 -201 -20 197 O ATOM 1268 N LYS A 171 9.374 5.014 25.786 1.00 25.38 N ANISOU 1268 N LYS A 171 3838 3890 1916 -164 -24 41 N ATOM 1269 CA LYS A 171 10.092 5.571 26.928 1.00 27.62 C ANISOU 1269 CA LYS A 171 4184 4220 2090 -173 -72 -9 C ATOM 1270 C LYS A 171 9.252 6.503 27.806 1.00 32.47 C ANISOU 1270 C LYS A 171 4837 4887 2612 -172 12 -97 C ATOM 1271 O LYS A 171 9.783 7.150 28.711 1.00 34.17 O ANISOU 1271 O LYS A 171 5109 5141 2732 -182 -22 -167 O ATOM 1272 CB LYS A 171 11.340 6.318 26.448 1.00 28.55 C ANISOU 1272 CB LYS A 171 4280 4287 2282 -164 -158 -64 C ATOM 1273 CG LYS A 171 12.367 5.449 25.724 1.00 26.50 C ANISOU 1273 CG LYS A 171 3982 3977 2109 -163 -238 10 C ATOM 1274 CD LYS A 171 12.982 4.421 26.662 1.00 30.56 C ANISOU 1274 CD LYS A 171 4537 4534 2539 -180 -312 91 C ATOM 1275 N VAL A 172 7.949 6.582 27.545 1.00 30.05 N ANISOU 1275 N VAL A 172 4498 4582 2339 -160 122 -99 N ATOM 1276 CA VAL A 172 7.070 7.367 28.406 1.00 29.32 C ANISOU 1276 CA VAL A 172 4435 4537 2169 -155 224 -180 C ATOM 1277 C VAL A 172 6.036 6.457 29.081 1.00 27.91 C ANISOU 1277 C VAL A 172 4274 4424 1908 -175 316 -108 C ATOM 1278 O VAL A 172 6.019 5.244 28.852 1.00 26.35 O ANISOU 1278 O VAL A 172 4064 4225 1723 -195 292 5 O ATOM 1279 CB VAL A 172 6.367 8.501 27.623 1.00 28.68 C ANISOU 1279 CB VAL A 172 4286 4396 2217 -116 290 -258 C ATOM 1280 CG1 VAL A 172 7.385 9.542 27.174 1.00 26.42 C ANISOU 1280 CG1 VAL A 172 3994 4046 1998 -102 215 -334 C ATOM 1281 CG2 VAL A 172 5.609 7.947 26.427 1.00 27.29 C ANISOU 1281 CG2 VAL A 172 4023 4179 2168 -104 313 -181 C ATOM 1282 N ALA A 173 5.193 7.042 29.927 1.00 27.21 N ANISOU 1282 N ALA A 173 4213 4386 1740 -172 428 -176 N ATOM 1283 CA ALA A 173 4.239 6.271 30.722 1.00 32.67 C ANISOU 1283 CA ALA A 173 4928 5148 2338 -196 533 -113 C ATOM 1284 C ALA A 173 3.229 5.520 29.854 1.00 33.90 C ANISOU 1284 C ALA A 173 4987 5266 2628 -195 590 -27 C ATOM 1285 O ALA A 173 2.957 4.337 30.066 1.00 32.32 O ANISOU 1285 O ALA A 173 4792 5089 2399 -228 605 84 O ATOM 1286 CB ALA A 173 3.511 7.187 31.697 1.00 33.93 C ANISOU 1286 CB ALA A 173 5128 5362 2403 -187 662 -223 C ATOM 1287 N ILE A 174 2.667 6.226 28.882 1.00 34.20 N ANISOU 1287 N ILE A 174 4934 5244 2817 -160 616 -76 N ATOM 1288 CA ILE A 174 1.684 5.646 27.988 1.00 31.94 C ANISOU 1288 CA ILE A 174 4547 4924 2664 -161 654 -10 C ATOM 1289 C ILE A 174 2.269 5.540 26.596 1.00 31.19 C ANISOU 1289 C ILE A 174 4403 4755 2694 -150 541 13 C ATOM 1290 O ILE A 174 2.737 6.526 26.033 1.00 31.53 O ANISOU 1290 O ILE A 174 4433 4755 2793 -117 496 -53 O ATOM 1291 CB ILE A 174 0.397 6.479 27.949 1.00 33.23 C ANISOU 1291 CB ILE A 174 4632 5085 2908 -129 777 -71 C ATOM 1292 CG1 ILE A 174 -0.160 6.640 29.362 1.00 37.40 C ANISOU 1292 CG1 ILE A 174 5217 5691 3304 -139 911 -109 C ATOM 1293 CG2 ILE A 174 -0.632 5.841 27.020 1.00 31.26 C ANISOU 1293 CG2 ILE A 174 4269 4809 2802 -136 798 2 C ATOM 1294 CD1 ILE A 174 -1.419 7.465 29.426 1.00 43.64 C ANISOU 1294 CD1 ILE A 174 5924 6475 4183 -101 1051 -176 C ATOM 1295 N ASN A 175 2.259 4.334 26.050 1.00 29.39 N ANISOU 1295 N ASN A 175 4150 4509 2507 -181 500 107 N ATOM 1296 CA ASN A 175 2.759 4.133 24.709 1.00 27.70 C ANISOU 1296 CA ASN A 175 3896 4231 2398 -176 407 124 C ATOM 1297 C ASN A 175 1.609 3.721 23.795 1.00 26.28 C ANISOU 1297 C ASN A 175 3619 4030 2334 -186 436 159 C ATOM 1298 O ASN A 175 0.588 4.399 23.778 1.00 29.18 O ANISOU 1298 O ASN A 175 3925 4410 2752 -165 507 126 O ATOM 1299 CB ASN A 175 3.906 3.125 24.739 1.00 27.84 C ANISOU 1299 CB ASN A 175 3969 4233 2377 -201 320 184 C ATOM 1300 CG ASN A 175 5.083 3.635 25.571 1.00 30.09 C ANISOU 1300 CG ASN A 175 4333 4540 2559 -191 268 147 C ATOM 1301 OD1 ASN A 175 5.807 4.536 25.146 1.00 28.27 O ANISOU 1301 OD1 ASN A 175 4103 4280 2359 -165 217 83 O ATOM 1302 ND2 ASN A 175 5.244 3.097 26.775 1.00 29.07 N ANISOU 1302 ND2 ASN A 175 4273 4466 2308 -214 281 190 N ATOM 1303 N ALA A 176 1.750 2.637 23.044 1.00 26.20 N ANISOU 1303 N ALA A 176 3592 3989 2375 -218 382 218 N ATOM 1304 CA ALA A 176 0.706 2.259 22.089 1.00 27.70 C ANISOU 1304 CA ALA A 176 3690 4160 2674 -236 390 240 C ATOM 1305 C ALA A 176 -0.646 1.982 22.766 1.00 27.67 C ANISOU 1305 C ALA A 176 3630 4194 2688 -258 496 267 C ATOM 1306 O ALA A 176 -0.725 1.238 23.747 1.00 26.18 O ANISOU 1306 O ALA A 176 3481 4031 2435 -290 551 316 O ATOM 1307 CB ALA A 176 1.148 1.043 21.279 1.00 26.38 C ANISOU 1307 CB ALA A 176 3527 3948 2548 -275 320 285 C ATOM 1308 N THR A 177 -1.701 2.605 22.244 1.00 28.49 N ANISOU 1308 N THR A 177 3639 4302 2886 -239 527 243 N ATOM 1309 CA THR A 177 -3.070 2.334 22.690 1.00 30.31 C ANISOU 1309 CA THR A 177 3786 4561 3170 -260 628 269 C ATOM 1310 C THR A 177 -3.991 2.118 21.491 1.00 31.42 C ANISOU 1310 C THR A 177 3807 4680 3450 -277 583 285 C ATOM 1311 O THR A 177 -3.746 2.666 20.411 1.00 28.53 O ANISOU 1311 O THR A 177 3420 4290 3128 -250 494 259 O ATOM 1312 CB THR A 177 -3.643 3.481 23.557 1.00 33.94 C ANISOU 1312 CB THR A 177 4227 5057 3611 -212 738 215 C ATOM 1313 OG1 THR A 177 -3.698 4.693 22.790 1.00 36.96 O ANISOU 1313 OG1 THR A 177 4561 5412 4068 -154 699 160 O ATOM 1314 CG2 THR A 177 -2.798 3.694 24.802 1.00 34.01 C ANISOU 1314 CG2 THR A 177 4359 5099 3463 -205 779 189 C ATOM 1315 N PRO A 178 -5.056 1.315 21.675 1.00 31.66 N ANISOU 1315 N PRO A 178 3760 4722 3550 -326 641 331 N ATOM 1316 CA PRO A 178 -6.014 1.076 20.588 1.00 33.07 C ANISOU 1316 CA PRO A 178 3814 4886 3865 -351 589 343 C ATOM 1317 C PRO A 178 -6.649 2.363 20.052 1.00 33.25 C ANISOU 1317 C PRO A 178 3745 4919 3969 -288 579 306 C ATOM 1318 O PRO A 178 -6.830 2.503 18.843 1.00 33.14 O ANISOU 1318 O PRO A 178 3675 4891 4023 -287 474 306 O ATOM 1319 CB PRO A 178 -7.076 0.179 21.247 1.00 33.45 C ANISOU 1319 CB PRO A 178 3789 4948 3973 -410 688 395 C ATOM 1320 CG PRO A 178 -6.358 -0.497 22.360 1.00 33.50 C ANISOU 1320 CG PRO A 178 3912 4959 3857 -435 750 432 C ATOM 1321 CD PRO A 178 -5.392 0.534 22.881 1.00 32.99 C ANISOU 1321 CD PRO A 178 3951 4915 3670 -368 752 381 C ATOM 1322 N GLU A 179 -6.975 3.298 20.937 1.00 32.58 N ANISOU 1322 N GLU A 179 3648 4856 3876 -235 686 277 N ATOM 1323 CA GLU A 179 -7.657 4.505 20.499 1.00 36.91 C ANISOU 1323 CA GLU A 179 4097 5400 4529 -170 688 248 C ATOM 1324 C GLU A 179 -6.735 5.406 19.690 1.00 33.03 C ANISOU 1324 C GLU A 179 3663 4877 4010 -119 584 218 C ATOM 1325 O GLU A 179 -7.159 6.002 18.705 1.00 32.83 O ANISOU 1325 O GLU A 179 3557 4838 4079 -87 512 228 O ATOM 1326 CB GLU A 179 -8.230 5.274 21.687 1.00 44.92 C ANISOU 1326 CB GLU A 179 5085 6434 5549 -124 847 211 C ATOM 1327 CG GLU A 179 -9.028 6.499 21.271 1.00 53.64 C ANISOU 1327 CG GLU A 179 6069 7518 6793 -50 862 185 C ATOM 1328 CD GLU A 179 -10.182 6.164 20.332 1.00 60.16 C ANISOU 1328 CD GLU A 179 6729 8345 7782 -69 803 241 C ATOM 1329 OE1 GLU A 179 -10.782 5.070 20.471 1.00 61.62 O ANISOU 1329 OE1 GLU A 179 6861 8553 7998 -140 827 283 O ATOM 1330 OE2 GLU A 179 -10.490 7.000 19.453 1.00 60.98 O ANISOU 1330 OE2 GLU A 179 6753 8426 7990 -16 726 246 O ATOM 1331 N ALA A 180 -5.475 5.502 20.101 1.00 31.54 N ANISOU 1331 N ALA A 180 3610 4679 3696 -113 573 188 N ATOM 1332 CA ALA A 180 -4.497 6.262 19.330 1.00 31.87 C ANISOU 1332 CA ALA A 180 3708 4688 3715 -75 479 165 C ATOM 1333 C ALA A 180 -4.269 5.614 17.967 1.00 28.31 C ANISOU 1333 C ALA A 180 3248 4225 3282 -112 352 204 C ATOM 1334 O ALA A 180 -4.136 6.305 16.960 1.00 27.28 O ANISOU 1334 O ALA A 180 3099 4078 3190 -80 275 208 O ATOM 1335 CB ALA A 180 -3.187 6.378 20.087 1.00 30.23 C ANISOU 1335 CB ALA A 180 3635 4474 3379 -71 490 126 C ATOM 1336 N ALA A 181 -4.236 4.284 17.944 1.00 26.79 N ANISOU 1336 N ALA A 181 3074 4043 3063 -180 334 232 N ATOM 1337 CA ALA A 181 -4.022 3.536 16.708 1.00 25.95 C ANISOU 1337 CA ALA A 181 2969 3925 2966 -224 224 251 C ATOM 1338 C ALA A 181 -5.137 3.793 15.694 1.00 28.70 C ANISOU 1338 C ALA A 181 3197 4289 3419 -225 163 272 C ATOM 1339 O ALA A 181 -4.884 3.941 14.495 1.00 27.22 O ANISOU 1339 O ALA A 181 3016 4100 3227 -226 60 276 O ATOM 1340 CB ALA A 181 -3.913 2.052 17.006 1.00 25.96 C ANISOU 1340 CB ALA A 181 3001 3919 2944 -298 234 271 C ATOM 1341 N LYS A 182 -6.369 3.855 16.185 1.00 30.61 N ANISOU 1341 N LYS A 182 3326 4550 3753 -224 227 288 N ATOM 1342 CA LYS A 182 -7.529 4.074 15.330 1.00 30.68 C ANISOU 1342 CA LYS A 182 3199 4577 3880 -225 165 315 C ATOM 1343 C LYS A 182 -7.478 5.450 14.667 1.00 31.63 C ANISOU 1343 C LYS A 182 3296 4690 4032 -146 112 321 C ATOM 1344 O LYS A 182 -7.793 5.590 13.484 1.00 31.18 O ANISOU 1344 O LYS A 182 3191 4647 4010 -151 -3 350 O ATOM 1345 CB LYS A 182 -8.819 3.920 16.139 1.00 31.11 C ANISOU 1345 CB LYS A 182 3127 4650 4043 -234 267 332 C ATOM 1346 CG LYS A 182 -10.097 4.132 15.341 1.00 33.00 C ANISOU 1346 CG LYS A 182 3200 4909 4430 -234 200 365 C ATOM 1347 CD LYS A 182 -11.339 3.834 16.181 1.00 33.44 C ANISOU 1347 CD LYS A 182 3121 4978 4605 -252 315 382 C ATOM 1348 N VAL A 183 -7.080 6.462 15.430 1.00 30.22 N ANISOU 1348 N VAL A 183 3155 4488 3838 -78 195 294 N ATOM 1349 CA VAL A 183 -6.985 7.817 14.900 1.00 31.11 C ANISOU 1349 CA VAL A 183 3250 4576 3997 -1 159 302 C ATOM 1350 C VAL A 183 -5.914 7.898 13.803 1.00 28.99 C ANISOU 1350 C VAL A 183 3077 4296 3643 -9 46 315 C ATOM 1351 O VAL A 183 -6.146 8.460 12.734 1.00 25.92 O ANISOU 1351 O VAL A 183 2647 3909 3294 15 -46 359 O ATOM 1352 CB VAL A 183 -6.677 8.834 16.025 1.00 31.78 C ANISOU 1352 CB VAL A 183 3369 4625 4081 64 279 252 C ATOM 1353 CG1 VAL A 183 -6.376 10.206 15.449 1.00 29.81 C ANISOU 1353 CG1 VAL A 183 3118 4328 3881 139 240 260 C ATOM 1354 CG2 VAL A 183 -7.847 8.902 17.004 1.00 31.67 C ANISOU 1354 CG2 VAL A 183 3249 4623 4159 81 404 238 C ATOM 1355 N MET A 184 -4.753 7.306 14.062 1.00 27.65 N ANISOU 1355 N MET A 184 3031 4118 3356 -44 54 282 N ATOM 1356 CA MET A 184 -3.652 7.337 13.102 1.00 26.91 C ANISOU 1356 CA MET A 184 3029 4012 3182 -53 -29 286 C ATOM 1357 C MET A 184 -3.953 6.534 11.829 1.00 27.62 C ANISOU 1357 C MET A 184 3101 4137 3258 -109 -138 315 C ATOM 1358 O MET A 184 -3.708 7.018 10.723 1.00 30.43 O ANISOU 1358 O MET A 184 3473 4499 3593 -96 -220 344 O ATOM 1359 CB MET A 184 -2.370 6.831 13.764 1.00 25.04 C ANISOU 1359 CB MET A 184 2912 3757 2846 -75 12 244 C ATOM 1360 CG MET A 184 -1.978 7.660 14.976 1.00 27.08 C ANISOU 1360 CG MET A 184 3202 3989 3097 -28 103 205 C ATOM 1361 SD MET A 184 -0.511 7.068 15.826 1.00 27.69 S ANISOU 1361 SD MET A 184 3407 4053 3060 -55 130 165 S ATOM 1362 CE MET A 184 0.745 7.332 14.567 1.00 24.37 C ANISOU 1362 CE MET A 184 3051 3602 2605 -53 44 172 C ATOM 1363 N LEU A 185 -4.490 5.324 11.978 1.00 26.50 N ANISOU 1363 N LEU A 185 2927 4016 3124 -175 -139 307 N ATOM 1364 CA LEU A 185 -4.905 4.528 10.820 1.00 28.41 C ANISOU 1364 CA LEU A 185 3144 4290 3360 -237 -245 317 C ATOM 1365 C LEU A 185 -5.977 5.247 10.002 1.00 30.79 C ANISOU 1365 C LEU A 185 3333 4626 3739 -212 -328 367 C ATOM 1366 O LEU A 185 -5.988 5.161 8.771 1.00 32.04 O ANISOU 1366 O LEU A 185 3503 4816 3856 -237 -441 385 O ATOM 1367 CB LEU A 185 -5.419 3.149 11.255 1.00 28.34 C ANISOU 1367 CB LEU A 185 3105 4285 3378 -314 -221 298 C ATOM 1368 CG LEU A 185 -4.378 2.155 11.783 1.00 28.31 C ANISOU 1368 CG LEU A 185 3211 4245 3300 -353 -171 262 C ATOM 1369 CD1 LEU A 185 -5.066 1.004 12.512 1.00 29.89 C ANISOU 1369 CD1 LEU A 185 3363 4436 3557 -416 -120 264 C ATOM 1370 CD2 LEU A 185 -3.509 1.629 10.657 1.00 23.11 C ANISOU 1370 CD2 LEU A 185 2640 3579 2562 -389 -249 233 C ATOM 1371 N THR A 186 -6.871 5.962 10.685 1.00 30.69 N ANISOU 1371 N THR A 186 3214 4609 3839 -161 -273 392 N ATOM 1372 CA THR A 186 -7.911 6.733 10.005 1.00 29.15 C ANISOU 1372 CA THR A 186 2894 4437 3745 -123 -349 451 C ATOM 1373 C THR A 186 -7.301 7.869 9.187 1.00 27.56 C ANISOU 1373 C THR A 186 2744 4223 3504 -62 -410 492 C ATOM 1374 O THR A 186 -7.745 8.144 8.068 1.00 30.12 O ANISOU 1374 O THR A 186 3025 4583 3838 -61 -532 550 O ATOM 1375 CB THR A 186 -8.943 7.312 11.001 1.00 31.38 C ANISOU 1375 CB THR A 186 3045 4704 4175 -70 -252 462 C ATOM 1376 OG1 THR A 186 -9.533 6.245 11.750 1.00 30.19 O ANISOU 1376 OG1 THR A 186 2845 4567 4060 -132 -185 435 O ATOM 1377 CG2 THR A 186 -10.053 8.070 10.264 1.00 32.34 C ANISOU 1377 CG2 THR A 186 3019 4844 4426 -26 -341 533 C ATOM 1378 N VAL A 187 -6.283 8.529 9.736 1.00 26.43 N ANISOU 1378 N VAL A 187 2695 4031 3318 -16 -330 468 N ATOM 1379 CA VAL A 187 -5.600 9.587 8.995 1.00 28.69 C ANISOU 1379 CA VAL A 187 3037 4293 3573 35 -374 510 C ATOM 1380 C VAL A 187 -4.911 8.999 7.758 1.00 31.26 C ANISOU 1380 C VAL A 187 3455 4657 3766 -22 -474 521 C ATOM 1381 O VAL A 187 -4.953 9.590 6.679 1.00 31.64 O ANISOU 1381 O VAL A 187 3504 4725 3794 -4 -564 588 O ATOM 1382 CB VAL A 187 -4.558 10.337 9.864 1.00 29.59 C ANISOU 1382 CB VAL A 187 3233 4340 3670 83 -268 468 C ATOM 1383 CG1 VAL A 187 -3.777 11.340 9.021 1.00 27.53 C ANISOU 1383 CG1 VAL A 187 3033 4047 3382 122 -312 516 C ATOM 1384 CG2 VAL A 187 -5.235 11.043 11.020 1.00 32.05 C ANISOU 1384 CG2 VAL A 187 3463 4612 4101 143 -165 447 C ATOM 1385 N ILE A 188 -4.287 7.831 7.918 1.00 29.36 N ANISOU 1385 N ILE A 188 3293 4426 3435 -90 -453 457 N ATOM 1386 CA ILE A 188 -3.645 7.156 6.792 1.00 28.87 C ANISOU 1386 CA ILE A 188 3320 4398 3250 -148 -528 446 C ATOM 1387 C ILE A 188 -4.667 6.853 5.691 1.00 29.91 C ANISOU 1387 C ILE A 188 3384 4598 3382 -187 -659 484 C ATOM 1388 O ILE A 188 -4.430 7.148 4.515 1.00 28.14 O ANISOU 1388 O ILE A 188 3206 4411 3074 -193 -745 524 O ATOM 1389 CB ILE A 188 -2.946 5.849 7.239 1.00 29.42 C ANISOU 1389 CB ILE A 188 3466 4453 3258 -211 -477 367 C ATOM 1390 CG1 ILE A 188 -1.620 6.165 7.936 1.00 26.43 C ANISOU 1390 CG1 ILE A 188 3180 4020 2842 -179 -385 337 C ATOM 1391 CG2 ILE A 188 -2.707 4.931 6.047 1.00 29.43 C ANISOU 1391 CG2 ILE A 188 3527 4494 3161 -283 -558 340 C ATOM 1392 CD1 ILE A 188 -1.020 4.996 8.704 1.00 24.56 C ANISOU 1392 CD1 ILE A 188 2996 3758 2578 -223 -325 276 C ATOM 1393 N LYS A 189 -5.810 6.285 6.075 1.00 29.71 N ANISOU 1393 N LYS A 189 3248 4593 3448 -217 -674 477 N ATOM 1394 CA LYS A 189 -6.854 5.961 5.105 1.00 32.16 C ANISOU 1394 CA LYS A 189 3476 4970 3773 -262 -811 508 C ATOM 1395 C LYS A 189 -7.324 7.205 4.362 1.00 32.66 C ANISOU 1395 C LYS A 189 3481 5058 3868 -197 -900 609 C ATOM 1396 O LYS A 189 -7.575 7.153 3.160 1.00 29.51 O ANISOU 1396 O LYS A 189 3089 4724 3397 -229 -1034 647 O ATOM 1397 CB LYS A 189 -8.050 5.289 5.786 1.00 36.52 C ANISOU 1397 CB LYS A 189 3893 5529 4455 -298 -798 491 C ATOM 1398 CG LYS A 189 -9.153 4.844 4.825 1.00 38.25 C ANISOU 1398 CG LYS A 189 4014 5817 4703 -358 -950 513 C ATOM 1399 CD LYS A 189 -8.626 3.811 3.836 1.00 41.69 C ANISOU 1399 CD LYS A 189 4559 6289 4992 -452 -1032 449 C ATOM 1400 CE LYS A 189 -9.729 3.244 2.944 1.00 44.99 C ANISOU 1400 CE LYS A 189 4882 6778 5433 -529 -1191 450 C ATOM 1401 NZ LYS A 189 -9.179 2.243 1.978 1.00 43.23 N ANISOU 1401 NZ LYS A 189 4780 6586 5057 -623 -1262 368 N ATOM 1402 N ASN A 190 -7.427 8.324 5.078 1.00 29.53 N ANISOU 1402 N ASN A 190 3033 4610 3578 -106 -825 653 N ATOM 1403 CA ASN A 190 -7.961 9.547 4.485 1.00 32.06 C ANISOU 1403 CA ASN A 190 3280 4934 3967 -33 -901 760 C ATOM 1404 C ASN A 190 -6.939 10.339 3.664 1.00 32.51 C ANISOU 1404 C ASN A 190 3457 4981 3914 -2 -927 814 C ATOM 1405 O ASN A 190 -7.312 11.040 2.729 1.00 35.25 O ANISOU 1405 O ASN A 190 3772 5358 4261 28 -1036 916 O ATOM 1406 CB ASN A 190 -8.552 10.452 5.570 1.00 32.68 C ANISOU 1406 CB ASN A 190 3245 4946 4226 55 -801 780 C ATOM 1407 CG ASN A 190 -9.889 9.945 6.098 1.00 37.34 C ANISOU 1407 CG ASN A 190 3672 5558 4957 37 -800 769 C ATOM 1408 OD1 ASN A 190 -10.642 9.264 5.392 1.00 38.20 O ANISOU 1408 OD1 ASN A 190 3714 5735 5067 -23 -921 788 O ATOM 1409 ND2 ASN A 190 -10.193 10.286 7.344 1.00 37.97 N ANISOU 1409 ND2 ASN A 190 3688 5582 5157 87 -660 736 N ATOM 1410 N LYS A 191 -5.658 10.223 3.997 1.00 30.54 N ANISOU 1410 N LYS A 191 3339 4690 3574 -11 -831 754 N ATOM 1411 CA LYS A 191 -4.635 11.042 3.336 1.00 32.62 C ANISOU 1411 CA LYS A 191 3707 4932 3756 20 -830 805 C ATOM 1412 C LYS A 191 -3.741 10.269 2.368 1.00 30.22 C ANISOU 1412 C LYS A 191 3537 4681 3265 -53 -867 773 C ATOM 1413 O LYS A 191 -3.536 10.703 1.237 1.00 29.26 O ANISOU 1413 O LYS A 191 3465 4599 3052 -54 -943 848 O ATOM 1414 CB LYS A 191 -3.754 11.739 4.376 1.00 34.27 C ANISOU 1414 CB LYS A 191 3957 5044 4018 75 -690 769 C ATOM 1415 CG LYS A 191 -4.431 12.892 5.102 1.00 39.11 C ANISOU 1415 CG LYS A 191 4462 5590 4806 163 -646 811 C ATOM 1416 CD LYS A 191 -3.430 13.623 5.994 1.00 42.87 C ANISOU 1416 CD LYS A 191 5001 5975 5315 206 -521 764 C ATOM 1417 CE LYS A 191 -2.458 14.474 5.175 1.00 45.14 C ANISOU 1417 CE LYS A 191 5373 6226 5550 226 -536 831 C ATOM 1418 NZ LYS A 191 -3.159 15.553 4.409 1.00 47.40 N ANISOU 1418 NZ LYS A 191 5590 6497 5923 288 -612 963 N ATOM 1419 N ASN A 192 -3.195 9.141 2.812 1.00 26.54 N ANISOU 1419 N ASN A 192 3131 4212 2742 -112 -807 665 N ATOM 1420 CA ASN A 192 -2.247 8.393 1.989 1.00 27.92 C ANISOU 1420 CA ASN A 192 3432 4420 2756 -176 -815 617 C ATOM 1421 C ASN A 192 -2.059 6.961 2.479 1.00 25.63 C ANISOU 1421 C ASN A 192 3169 4126 2444 -245 -774 502 C ATOM 1422 O ASN A 192 -1.378 6.716 3.478 1.00 24.54 O ANISOU 1422 O ASN A 192 3056 3926 2341 -234 -668 447 O ATOM 1423 CB ASN A 192 -0.893 9.113 1.955 1.00 30.58 C ANISOU 1423 CB ASN A 192 3868 4704 3048 -139 -731 631 C ATOM 1424 CG ASN A 192 0.056 8.539 0.912 1.00 32.28 C ANISOU 1424 CG ASN A 192 4207 4958 3098 -195 -735 600 C ATOM 1425 OD1 ASN A 192 -0.156 7.446 0.395 1.00 35.74 O ANISOU 1425 OD1 ASN A 192 4674 5451 3455 -264 -782 537 O ATOM 1426 ND2 ASN A 192 1.108 9.281 0.601 1.00 31.79 N ANISOU 1426 ND2 ASN A 192 4219 4864 2996 -166 -677 638 N ATOM 1427 N THR A 193 -2.644 6.015 1.751 1.00 26.44 N ANISOU 1427 N THR A 193 3267 4292 2488 -318 -863 467 N ATOM 1428 CA THR A 193 -2.584 4.608 2.133 1.00 27.69 C ANISOU 1428 CA THR A 193 3442 4437 2644 -389 -832 362 C ATOM 1429 C THR A 193 -1.203 3.991 1.886 1.00 29.47 C ANISOU 1429 C THR A 193 3800 4632 2764 -417 -760 288 C ATOM 1430 O THR A 193 -0.954 2.840 2.260 1.00 29.10 O ANISOU 1430 O THR A 193 3777 4552 2726 -466 -717 204 O ATOM 1431 CB THR A 193 -3.647 3.788 1.379 1.00 27.37 C ANISOU 1431 CB THR A 193 3351 4464 2582 -467 -955 337 C ATOM 1432 OG1 THR A 193 -3.467 3.951 -0.032 1.00 30.40 O ANISOU 1432 OG1 THR A 193 3811 4923 2819 -495 -1050 354 O ATOM 1433 CG2 THR A 193 -5.049 4.256 1.750 1.00 28.14 C ANISOU 1433 CG2 THR A 193 3293 4584 2816 -442 -1019 404 C ATOM 1434 N ALA A 194 -0.310 4.757 1.261 1.00 26.69 N ANISOU 1434 N ALA A 194 3528 4284 2327 -384 -740 326 N ATOM 1435 CA ALA A 194 1.058 4.312 1.028 1.00 27.38 C ANISOU 1435 CA ALA A 194 3728 4340 2334 -400 -658 264 C ATOM 1436 C ALA A 194 1.985 4.785 2.146 1.00 32.17 C ANISOU 1436 C ALA A 194 4340 4865 3020 -342 -545 268 C ATOM 1437 O ALA A 194 3.208 4.664 2.048 1.00 32.86 O ANISOU 1437 O ALA A 194 4502 4917 3065 -339 -472 236 O ATOM 1438 CB ALA A 194 1.554 4.804 -0.322 1.00 25.79 C ANISOU 1438 CB ALA A 194 3613 4195 1990 -407 -689 300 C ATOM 1439 N VAL A 195 1.394 5.353 3.194 1.00 30.53 N ANISOU 1439 N VAL A 195 4047 4628 2926 -296 -532 306 N ATOM 1440 CA VAL A 195 2.121 5.650 4.426 1.00 26.16 C ANISOU 1440 CA VAL A 195 3493 4003 2445 -252 -436 293 C ATOM 1441 C VAL A 195 1.847 4.535 5.424 1.00 26.65 C ANISOU 1441 C VAL A 195 3526 4040 2559 -284 -404 233 C ATOM 1442 O VAL A 195 0.696 4.145 5.620 1.00 26.03 O ANISOU 1442 O VAL A 195 3375 3987 2527 -307 -444 236 O ATOM 1443 CB VAL A 195 1.707 7.004 5.038 1.00 24.70 C ANISOU 1443 CB VAL A 195 3243 3795 2347 -181 -425 360 C ATOM 1444 CG1 VAL A 195 2.387 7.209 6.388 1.00 24.24 C ANISOU 1444 CG1 VAL A 195 3189 3672 2350 -148 -334 326 C ATOM 1445 CG2 VAL A 195 2.042 8.141 4.086 1.00 24.23 C ANISOU 1445 CG2 VAL A 195 3214 3744 2250 -148 -451 434 C ATOM 1446 N GLY A 196 2.901 4.013 6.041 1.00 24.20 N ANISOU 1446 N GLY A 196 3266 3678 2249 -286 -333 187 N ATOM 1447 CA GLY A 196 2.764 2.899 6.956 1.00 24.53 C ANISOU 1447 CA GLY A 196 3293 3692 2336 -316 -301 145 C ATOM 1448 C GLY A 196 2.457 3.288 8.392 1.00 25.67 C ANISOU 1448 C GLY A 196 3388 3814 2552 -279 -254 166 C ATOM 1449 O GLY A 196 2.592 4.454 8.793 1.00 23.17 O ANISOU 1449 O GLY A 196 3058 3490 2255 -225 -233 196 O ATOM 1450 N PHE A 197 2.043 2.293 9.170 1.00 24.26 N ANISOU 1450 N PHE A 197 3186 3622 2410 -312 -231 148 N ATOM 1451 CA PHE A 197 1.709 2.489 10.572 1.00 23.53 C ANISOU 1451 CA PHE A 197 3057 3518 2365 -287 -176 165 C ATOM 1452 C PHE A 197 2.545 1.578 11.478 1.00 24.48 C ANISOU 1452 C PHE A 197 3226 3595 2479 -302 -128 147 C ATOM 1453 O PHE A 197 2.695 0.385 11.202 1.00 23.75 O ANISOU 1453 O PHE A 197 3155 3479 2390 -350 -136 127 O ATOM 1454 CB PHE A 197 0.218 2.228 10.798 1.00 23.83 C ANISOU 1454 CB PHE A 197 3004 3587 2462 -312 -187 184 C ATOM 1455 CG PHE A 197 -0.195 2.297 12.236 1.00 25.32 C ANISOU 1455 CG PHE A 197 3159 3771 2690 -294 -112 198 C ATOM 1456 CD1 PHE A 197 -0.022 3.471 12.963 1.00 25.04 C ANISOU 1456 CD1 PHE A 197 3123 3734 2657 -232 -67 205 C ATOM 1457 CD2 PHE A 197 -0.759 1.194 12.866 1.00 24.72 C ANISOU 1457 CD2 PHE A 197 3057 3689 2648 -344 -81 203 C ATOM 1458 CE1 PHE A 197 -0.400 3.546 14.294 1.00 25.21 C ANISOU 1458 CE1 PHE A 197 3124 3760 2695 -219 10 207 C ATOM 1459 CE2 PHE A 197 -1.148 1.260 14.192 1.00 25.50 C ANISOU 1459 CE2 PHE A 197 3132 3792 2765 -330 -1 222 C ATOM 1460 CZ PHE A 197 -0.962 2.438 14.912 1.00 25.10 C ANISOU 1460 CZ PHE A 197 3088 3750 2697 -268 45 220 C ATOM 1461 N LYS A 198 3.079 2.137 12.559 1.00 24.60 N ANISOU 1461 N LYS A 198 3259 3598 2489 -262 -83 156 N ATOM 1462 CA LYS A 198 3.892 1.356 13.488 1.00 23.72 C ANISOU 1462 CA LYS A 198 3192 3453 2367 -271 -51 155 C ATOM 1463 C LYS A 198 3.493 1.587 14.950 1.00 21.76 C ANISOU 1463 C LYS A 198 2930 3221 2114 -255 0 175 C ATOM 1464 O LYS A 198 3.959 2.529 15.589 1.00 23.28 O ANISOU 1464 O LYS A 198 3142 3419 2283 -214 18 166 O ATOM 1465 CB LYS A 198 5.388 1.668 13.288 1.00 21.85 C ANISOU 1465 CB LYS A 198 3013 3184 2106 -244 -57 137 C ATOM 1466 CG LYS A 198 6.324 0.920 14.253 1.00 22.44 C ANISOU 1466 CG LYS A 198 3125 3224 2177 -246 -41 146 C ATOM 1467 CD LYS A 198 7.806 1.052 13.873 1.00 21.92 C ANISOU 1467 CD LYS A 198 3096 3120 2113 -226 -53 128 C ATOM 1468 CE LYS A 198 8.698 0.592 15.034 1.00 23.08 C ANISOU 1468 CE LYS A 198 3266 3242 2261 -217 -51 148 C ATOM 1469 NZ LYS A 198 10.151 0.561 14.715 1.00 21.60 N ANISOU 1469 NZ LYS A 198 3096 3011 2099 -199 -64 135 N ATOM 1470 N PRO A 199 2.624 0.719 15.485 1.00 22.93 N ANISOU 1470 N PRO A 199 3049 3378 2286 -292 27 199 N ATOM 1471 CA PRO A 199 2.358 0.729 16.928 1.00 24.37 C ANISOU 1471 CA PRO A 199 3236 3580 2445 -286 88 224 C ATOM 1472 C PRO A 199 3.577 0.207 17.686 1.00 22.54 C ANISOU 1472 C PRO A 199 3077 3323 2167 -283 86 239 C ATOM 1473 O PRO A 199 4.136 -0.809 17.285 1.00 21.66 O ANISOU 1473 O PRO A 199 2987 3167 2077 -309 60 251 O ATOM 1474 CB PRO A 199 1.164 -0.219 17.072 1.00 25.45 C ANISOU 1474 CB PRO A 199 3316 3723 2629 -337 118 255 C ATOM 1475 CG PRO A 199 1.306 -1.159 15.923 1.00 25.37 C ANISOU 1475 CG PRO A 199 3306 3675 2660 -380 62 243 C ATOM 1476 CD PRO A 199 1.850 -0.324 14.789 1.00 23.21 C ANISOU 1476 CD PRO A 199 3046 3404 2368 -348 7 203 C ATOM 1477 N ALA A 200 3.989 0.885 18.752 1.00 22.96 N ANISOU 1477 N ALA A 200 3164 3400 2161 -252 110 236 N ATOM 1478 CA ALA A 200 5.200 0.486 19.463 1.00 24.23 C ANISOU 1478 CA ALA A 200 3388 3544 2276 -248 88 255 C ATOM 1479 C ALA A 200 5.127 0.790 20.957 1.00 27.85 C ANISOU 1479 C ALA A 200 3881 4050 2650 -240 127 270 C ATOM 1480 O ALA A 200 4.491 1.765 21.371 1.00 25.41 O ANISOU 1480 O ALA A 200 3558 3780 2315 -220 172 235 O ATOM 1481 CB ALA A 200 6.412 1.168 18.851 1.00 23.21 C ANISOU 1481 CB ALA A 200 3280 3388 2153 -217 36 216 C ATOM 1482 N GLY A 201 5.791 -0.046 21.757 1.00 26.41 N ANISOU 1482 N GLY A 201 3748 3863 2426 -254 110 323 N ATOM 1483 CA GLY A 201 5.806 0.115 23.201 1.00 25.09 C ANISOU 1483 CA GLY A 201 3631 3751 2153 -253 139 346 C ATOM 1484 C GLY A 201 4.625 -0.547 23.892 1.00 29.97 C ANISOU 1484 C GLY A 201 4239 4401 2747 -287 221 403 C ATOM 1485 O GLY A 201 3.477 -0.099 23.766 1.00 29.79 O ANISOU 1485 O GLY A 201 4167 4403 2749 -290 289 375 O ATOM 1486 N GLY A 202 4.900 -1.622 24.625 1.00 29.85 N ANISOU 1486 N GLY A 202 4264 4382 2695 -313 217 490 N ATOM 1487 CA GLY A 202 3.865 -2.290 25.394 1.00 29.78 C ANISOU 1487 CA GLY A 202 4253 4403 2657 -351 303 560 C ATOM 1488 C GLY A 202 3.116 -3.366 24.629 1.00 28.37 C ANISOU 1488 C GLY A 202 4013 4164 2603 -392 326 603 C ATOM 1489 O GLY A 202 2.142 -3.921 25.134 1.00 25.50 O ANISOU 1489 O GLY A 202 3630 3816 2245 -430 406 660 O ATOM 1490 N VAL A 203 3.562 -3.657 23.409 1.00 27.30 N ANISOU 1490 N VAL A 203 3846 3958 2567 -389 260 572 N ATOM 1491 CA VAL A 203 3.015 -4.783 22.656 1.00 28.81 C ANISOU 1491 CA VAL A 203 3990 4081 2875 -436 266 600 C ATOM 1492 C VAL A 203 3.687 -6.068 23.143 1.00 29.81 C ANISOU 1492 C VAL A 203 4160 4147 3020 -456 247 695 C ATOM 1493 O VAL A 203 4.770 -6.436 22.669 1.00 28.49 O ANISOU 1493 O VAL A 203 4014 3919 2892 -436 179 690 O ATOM 1494 CB VAL A 203 3.216 -4.622 21.132 1.00 29.10 C ANISOU 1494 CB VAL A 203 3988 4072 2998 -429 208 521 C ATOM 1495 CG1 VAL A 203 2.566 -5.792 20.385 1.00 31.00 C ANISOU 1495 CG1 VAL A 203 4181 4245 3351 -487 213 533 C ATOM 1496 CG2 VAL A 203 2.638 -3.289 20.651 1.00 25.99 C ANISOU 1496 CG2 VAL A 203 3552 3735 2590 -401 215 445 C ATOM 1497 N ARG A 204 3.037 -6.739 24.093 1.00 27.67 N ANISOU 1497 N ARG A 204 3899 3889 2727 -492 313 788 N ATOM 1498 CA ARG A 204 3.654 -7.832 24.842 1.00 30.89 C ANISOU 1498 CA ARG A 204 4359 4251 3129 -505 299 905 C ATOM 1499 C ARG A 204 3.549 -9.199 24.167 1.00 34.82 C ANISOU 1499 C ARG A 204 4822 4627 3781 -547 294 945 C ATOM 1500 O ARG A 204 4.467 -10.019 24.257 1.00 33.30 O ANISOU 1500 O ARG A 204 4661 4358 3632 -537 247 1007 O ATOM 1501 CB ARG A 204 3.020 -7.939 26.236 1.00 32.05 C ANISOU 1501 CB ARG A 204 4542 4468 3168 -529 382 1002 C ATOM 1502 CG ARG A 204 3.076 -6.682 27.088 1.00 30.22 C ANISOU 1502 CG ARG A 204 4356 4355 2770 -494 402 960 C ATOM 1503 CD ARG A 204 2.044 -6.780 28.206 1.00 28.69 C ANISOU 1503 CD ARG A 204 4179 4234 2489 -530 523 1029 C ATOM 1504 NE ARG A 204 0.702 -6.932 27.656 1.00 30.17 N ANISOU 1504 NE ARG A 204 4272 4401 2789 -569 610 1005 N ATOM 1505 CZ ARG A 204 -0.331 -7.461 28.308 1.00 34.84 C ANISOU 1505 CZ ARG A 204 4842 5011 3383 -619 724 1084 C ATOM 1506 NH1 ARG A 204 -0.191 -7.897 29.555 1.00 31.33 N ANISOU 1506 NH1 ARG A 204 4477 4610 2815 -635 773 1200 N ATOM 1507 NH2 ARG A 204 -1.510 -7.556 27.707 1.00 34.29 N ANISOU 1507 NH2 ARG A 204 4668 4920 3439 -655 789 1053 N ATOM 1508 N ASN A 205 2.416 -9.451 23.519 1.00 35.05 N ANISOU 1508 N ASN A 205 4782 4634 3901 -596 341 909 N ATOM 1509 CA ASN A 205 2.102 -10.788 23.034 1.00 30.08 C ANISOU 1509 CA ASN A 205 4120 3890 3420 -653 351 945 C ATOM 1510 C ASN A 205 1.185 -10.776 21.815 1.00 30.43 C ANISOU 1510 C ASN A 205 4083 3912 3566 -695 351 844 C ATOM 1511 O ASN A 205 0.898 -9.719 21.239 1.00 27.15 O ANISOU 1511 O ASN A 205 3638 3567 3112 -672 333 752 O ATOM 1512 CB ASN A 205 1.470 -11.612 24.158 1.00 30.19 C ANISOU 1512 CB ASN A 205 4143 3894 3435 -700 432 1084 C ATOM 1513 CG ASN A 205 0.262 -10.921 24.789 1.00 31.27 C ANISOU 1513 CG ASN A 205 4245 4137 3498 -721 525 1090 C ATOM 1514 OD1 ASN A 205 -0.592 -10.373 24.094 1.00 30.78 O ANISOU 1514 OD1 ASN A 205 4109 4105 3481 -736 541 1000 O ATOM 1515 ND2 ASN A 205 0.195 -10.943 26.114 1.00 30.18 N ANISOU 1515 ND2 ASN A 205 4161 4059 3247 -722 588 1198 N ATOM 1516 N ALA A 206 0.717 -11.959 21.436 1.00 27.60 N ANISOU 1516 N ALA A 206 3688 3453 3344 -760 367 865 N ATOM 1517 CA ALA A 206 -0.117 -12.102 20.255 1.00 29.06 C ANISOU 1517 CA ALA A 206 3798 3611 3631 -812 351 768 C ATOM 1518 C ALA A 206 -1.473 -11.423 20.439 1.00 27.82 C ANISOU 1518 C ALA A 206 3564 3547 3460 -840 402 759 C ATOM 1519 O ALA A 206 -2.015 -10.865 19.489 1.00 31.34 O ANISOU 1519 O ALA A 206 3951 4027 3928 -847 363 664 O ATOM 1520 CB ALA A 206 -0.296 -13.570 19.912 1.00 28.57 C ANISOU 1520 CB ALA A 206 3717 3411 3726 -883 358 789 C ATOM 1521 N ASP A 207 -2.008 -11.465 21.659 1.00 30.07 N ANISOU 1521 N ASP A 207 3846 3872 3706 -852 492 861 N ATOM 1522 CA ASP A 207 -3.270 -10.790 21.971 1.00 34.31 C ANISOU 1522 CA ASP A 207 4304 4497 4235 -870 562 858 C ATOM 1523 C ASP A 207 -3.192 -9.288 21.699 1.00 33.22 C ANISOU 1523 C ASP A 207 4161 4461 3999 -799 533 771 C ATOM 1524 O ASP A 207 -4.098 -8.715 21.091 1.00 34.71 O ANISOU 1524 O ASP A 207 4261 4689 4237 -809 528 710 O ATOM 1525 CB ASP A 207 -3.669 -11.018 23.432 1.00 39.34 C ANISOU 1525 CB ASP A 207 4961 5170 4815 -885 679 984 C ATOM 1526 CG ASP A 207 -4.140 -12.431 23.702 1.00 47.32 C ANISOU 1526 CG ASP A 207 5947 6083 5952 -969 732 1082 C ATOM 1527 OD1 ASP A 207 -4.573 -13.112 22.749 1.00 50.28 O ANISOU 1527 OD1 ASP A 207 6253 6373 6479 -1028 695 1033 O ATOM 1528 OD2 ASP A 207 -4.082 -12.857 24.876 1.00 48.49 O ANISOU 1528 OD2 ASP A 207 6145 6236 6042 -979 812 1209 O ATOM 1529 N ASP A 208 -2.116 -8.652 22.159 1.00 28.91 N ANISOU 1529 N ASP A 208 3706 3952 3325 -730 508 771 N ATOM 1530 CA ASP A 208 -1.918 -7.230 21.902 1.00 30.10 C ANISOU 1530 CA ASP A 208 3860 4181 3395 -664 479 690 C ATOM 1531 C ASP A 208 -1.789 -6.990 20.408 1.00 30.97 C ANISOU 1531 C ASP A 208 3934 4263 3569 -659 385 593 C ATOM 1532 O ASP A 208 -2.422 -6.087 19.858 1.00 29.35 O ANISOU 1532 O ASP A 208 3668 4109 3375 -642 373 535 O ATOM 1533 CB ASP A 208 -0.674 -6.695 22.615 1.00 33.20 C ANISOU 1533 CB ASP A 208 4356 4604 3654 -601 457 702 C ATOM 1534 CG ASP A 208 -0.771 -6.793 24.123 1.00 36.53 C ANISOU 1534 CG ASP A 208 4829 5076 3975 -603 541 792 C ATOM 1535 OD1 ASP A 208 -1.896 -6.950 24.647 1.00 36.06 O ANISOU 1535 OD1 ASP A 208 4719 5046 3935 -641 640 832 O ATOM 1536 OD2 ASP A 208 0.288 -6.701 24.782 1.00 35.92 O ANISOU 1536 OD2 ASP A 208 4840 5013 3795 -569 509 823 O ATOM 1537 N ALA A 209 -0.958 -7.807 19.764 1.00 28.57 N ANISOU 1537 N ALA A 209 3671 3879 3305 -673 322 581 N ATOM 1538 CA ALA A 209 -0.710 -7.700 18.331 1.00 26.79 C ANISOU 1538 CA ALA A 209 3432 3628 3121 -674 239 488 C ATOM 1539 C ALA A 209 -2.016 -7.738 17.548 1.00 28.67 C ANISOU 1539 C ALA A 209 3571 3881 3443 -728 227 447 C ATOM 1540 O ALA A 209 -2.214 -6.954 16.611 1.00 29.32 O ANISOU 1540 O ALA A 209 3622 4004 3513 -709 170 380 O ATOM 1541 CB ALA A 209 0.218 -8.814 17.872 1.00 26.19 C ANISOU 1541 CB ALA A 209 3406 3448 3095 -693 202 482 C ATOM 1542 N ALA A 210 -2.906 -8.639 17.961 1.00 26.27 N ANISOU 1542 N ALA A 210 3212 3542 3227 -796 278 497 N ATOM 1543 CA ALA A 210 -4.214 -8.808 17.337 1.00 28.37 C ANISOU 1543 CA ALA A 210 3367 3818 3596 -859 266 468 C ATOM 1544 C ALA A 210 -5.045 -7.530 17.379 1.00 31.26 C ANISOU 1544 C ALA A 210 3656 4283 3938 -820 278 454 C ATOM 1545 O ALA A 210 -5.800 -7.252 16.452 1.00 32.37 O ANISOU 1545 O ALA A 210 3715 4449 4136 -842 217 404 O ATOM 1546 CB ALA A 210 -4.983 -9.952 18.013 1.00 28.23 C ANISOU 1546 CB ALA A 210 3300 3743 3684 -938 340 541 C ATOM 1547 N ILE A 211 -4.920 -6.771 18.464 1.00 30.64 N ANISOU 1547 N ILE A 211 3604 4259 3778 -762 356 498 N ATOM 1548 CA ILE A 211 -5.653 -5.521 18.608 1.00 33.15 C ANISOU 1548 CA ILE A 211 3854 4658 4084 -715 385 482 C ATOM 1549 C ILE A 211 -5.361 -4.604 17.429 1.00 31.43 C ANISOU 1549 C ILE A 211 3632 4464 3844 -670 280 409 C ATOM 1550 O ILE A 211 -6.269 -4.121 16.759 1.00 31.71 O ANISOU 1550 O ILE A 211 3568 4532 3946 -674 242 385 O ATOM 1551 CB ILE A 211 -5.289 -4.793 19.922 1.00 35.83 C ANISOU 1551 CB ILE A 211 4254 5046 4315 -655 479 516 C ATOM 1552 CG1 ILE A 211 -5.752 -5.601 21.134 1.00 37.01 C ANISOU 1552 CG1 ILE A 211 4402 5190 4472 -700 595 601 C ATOM 1553 CG2 ILE A 211 -5.905 -3.401 19.960 1.00 37.10 C ANISOU 1553 CG2 ILE A 211 4351 5274 4472 -595 506 479 C ATOM 1554 CD1 ILE A 211 -5.083 -5.176 22.418 1.00 35.93 C ANISOU 1554 CD1 ILE A 211 4366 5096 4192 -653 668 637 C ATOM 1555 N TYR A 212 -4.079 -4.393 17.163 1.00 30.51 N ANISOU 1555 N TYR A 212 3621 4330 3641 -629 232 382 N ATOM 1556 CA TYR A 212 -3.672 -3.419 16.162 1.00 30.06 C ANISOU 1556 CA TYR A 212 3576 4298 3546 -581 151 326 C ATOM 1557 C TYR A 212 -3.839 -3.940 14.737 1.00 29.12 C ANISOU 1557 C TYR A 212 3434 4160 3472 -630 51 280 C ATOM 1558 O TYR A 212 -4.195 -3.178 13.837 1.00 28.95 O ANISOU 1558 O TYR A 212 3370 4177 3451 -611 -15 252 O ATOM 1559 CB TYR A 212 -2.233 -2.979 16.442 1.00 27.44 C ANISOU 1559 CB TYR A 212 3357 3956 3112 -524 147 316 C ATOM 1560 CG TYR A 212 -2.135 -2.383 17.824 1.00 27.35 C ANISOU 1560 CG TYR A 212 3372 3978 3044 -481 233 348 C ATOM 1561 CD1 TYR A 212 -2.502 -1.062 18.054 1.00 29.54 C ANISOU 1561 CD1 TYR A 212 3616 4303 3303 -424 260 328 C ATOM 1562 CD2 TYR A 212 -1.741 -3.153 18.911 1.00 27.40 C ANISOU 1562 CD2 TYR A 212 3433 3964 3013 -499 289 400 C ATOM 1563 CE1 TYR A 212 -2.448 -0.513 19.319 1.00 30.21 C ANISOU 1563 CE1 TYR A 212 3730 4420 3328 -390 344 340 C ATOM 1564 CE2 TYR A 212 -1.681 -2.610 20.185 1.00 30.16 C ANISOU 1564 CE2 TYR A 212 3816 4358 3287 -466 365 424 C ATOM 1565 CZ TYR A 212 -2.038 -1.289 20.382 1.00 31.98 C ANISOU 1565 CZ TYR A 212 4020 4639 3494 -414 395 385 C ATOM 1566 OH TYR A 212 -1.986 -0.736 21.644 1.00 33.60 O ANISOU 1566 OH TYR A 212 4264 4887 3614 -385 476 391 O ATOM 1567 N LEU A 213 -3.621 -5.236 14.535 1.00 28.88 N ANISOU 1567 N LEU A 213 3429 4064 3478 -695 40 272 N ATOM 1568 CA LEU A 213 -3.861 -5.832 13.225 1.00 30.64 C ANISOU 1568 CA LEU A 213 3634 4268 3741 -755 -49 212 C ATOM 1569 C LEU A 213 -5.358 -5.827 12.880 1.00 31.27 C ANISOU 1569 C LEU A 213 3582 4384 3913 -806 -80 213 C ATOM 1570 O LEU A 213 -5.735 -5.577 11.735 1.00 31.66 O ANISOU 1570 O LEU A 213 3597 4468 3963 -824 -178 167 O ATOM 1571 CB LEU A 213 -3.295 -7.253 13.167 1.00 27.78 C ANISOU 1571 CB LEU A 213 3327 3811 3416 -812 -41 195 C ATOM 1572 CG LEU A 213 -1.766 -7.331 13.052 1.00 27.19 C ANISOU 1572 CG LEU A 213 3368 3693 3269 -767 -42 173 C ATOM 1573 CD1 LEU A 213 -1.283 -8.761 13.196 1.00 29.38 C ANISOU 1573 CD1 LEU A 213 3687 3864 3613 -815 -18 171 C ATOM 1574 CD2 LEU A 213 -1.277 -6.743 11.737 1.00 25.24 C ANISOU 1574 CD2 LEU A 213 3157 3478 2954 -746 -118 98 C ATOM 1575 N ASP A 214 -6.207 -6.082 13.871 1.00 32.52 N ANISOU 1575 N ASP A 214 3665 4542 4148 -829 1 270 N ATOM 1576 CA ASP A 214 -7.653 -6.046 13.655 1.00 31.66 C ANISOU 1576 CA ASP A 214 3412 4468 4150 -875 -18 278 C ATOM 1577 C ASP A 214 -8.108 -4.645 13.241 1.00 31.46 C ANISOU 1577 C ASP A 214 3323 4523 4106 -807 -63 276 C ATOM 1578 O ASP A 214 -8.941 -4.499 12.346 1.00 34.50 O ANISOU 1578 O ASP A 214 3615 4942 4551 -837 -156 257 O ATOM 1579 CB ASP A 214 -8.412 -6.499 14.909 1.00 33.76 C ANISOU 1579 CB ASP A 214 3609 4719 4499 -905 106 348 C ATOM 1580 CG ASP A 214 -8.341 -8.008 15.130 1.00 40.25 C ANISOU 1580 CG ASP A 214 4453 5451 5389 -994 134 361 C ATOM 1581 OD1 ASP A 214 -7.927 -8.734 14.197 1.00 42.73 O ANISOU 1581 OD1 ASP A 214 4810 5713 5712 -1042 49 300 O ATOM 1582 OD2 ASP A 214 -8.707 -8.473 16.236 1.00 39.43 O ANISOU 1582 OD2 ASP A 214 4325 5325 5330 -1017 247 434 O ATOM 1583 N LEU A 215 -7.563 -3.622 13.895 1.00 27.68 N ANISOU 1583 N LEU A 215 2894 4070 3552 -717 -3 298 N ATOM 1584 CA LEU A 215 -7.846 -2.228 13.535 1.00 30.87 C ANISOU 1584 CA LEU A 215 3252 4532 3947 -642 -38 300 C ATOM 1585 C LEU A 215 -7.443 -1.909 12.096 1.00 31.92 C ANISOU 1585 C LEU A 215 3421 4683 4025 -638 -174 261 C ATOM 1586 O LEU A 215 -8.216 -1.308 11.350 1.00 30.90 O ANISOU 1586 O LEU A 215 3203 4599 3941 -629 -254 268 O ATOM 1587 CB LEU A 215 -7.131 -1.270 14.491 1.00 28.16 C ANISOU 1587 CB LEU A 215 2979 4195 3525 -555 51 314 C ATOM 1588 CG LEU A 215 -7.825 -1.080 15.843 1.00 31.69 C ANISOU 1588 CG LEU A 215 3367 4656 4018 -538 187 350 C ATOM 1589 CD1 LEU A 215 -6.902 -0.415 16.856 1.00 31.19 C ANISOU 1589 CD1 LEU A 215 3409 4594 3849 -472 270 347 C ATOM 1590 CD2 LEU A 215 -9.086 -0.260 15.661 1.00 32.83 C ANISOU 1590 CD2 LEU A 215 3362 4840 4273 -510 190 363 C ATOM 1591 N ALA A 216 -6.232 -2.309 11.713 1.00 30.94 N ANISOU 1591 N ALA A 216 3425 4525 3806 -643 -198 225 N ATOM 1592 CA ALA A 216 -5.744 -2.080 10.353 1.00 30.66 C ANISOU 1592 CA ALA A 216 3441 4509 3698 -644 -308 185 C ATOM 1593 C ALA A 216 -6.622 -2.807 9.341 1.00 34.17 C ANISOU 1593 C ALA A 216 3818 4971 4192 -730 -412 153 C ATOM 1594 O ALA A 216 -6.971 -2.254 8.293 1.00 34.76 O ANISOU 1594 O ALA A 216 3865 5101 4241 -726 -518 149 O ATOM 1595 CB ALA A 216 -4.288 -2.527 10.217 1.00 26.82 C ANISOU 1595 CB ALA A 216 3095 3975 3119 -640 -291 147 C ATOM 1596 N ASP A 217 -6.983 -4.045 9.668 1.00 34.39 N ANISOU 1596 N ASP A 217 3821 4952 4293 -810 -385 134 N ATOM 1597 CA ASP A 217 -7.859 -4.836 8.816 1.00 33.27 C ANISOU 1597 CA ASP A 217 3608 4818 4216 -905 -482 93 C ATOM 1598 C ASP A 217 -9.213 -4.154 8.621 1.00 33.69 C ANISOU 1598 C ASP A 217 3505 4940 4358 -902 -543 134 C ATOM 1599 O ASP A 217 -9.681 -4.028 7.495 1.00 30.22 O ANISOU 1599 O ASP A 217 3027 4551 3904 -935 -676 108 O ATOM 1600 CB ASP A 217 -8.053 -6.244 9.392 1.00 32.60 C ANISOU 1600 CB ASP A 217 3511 4653 4224 -990 -422 76 C ATOM 1601 CG ASP A 217 -6.805 -7.112 9.261 1.00 35.00 C ANISOU 1601 CG ASP A 217 3955 4879 4465 -1008 -395 24 C ATOM 1602 OD1 ASP A 217 -5.858 -6.701 8.555 1.00 37.34 O ANISOU 1602 OD1 ASP A 217 4350 5191 4645 -967 -432 -15 O ATOM 1603 OD2 ASP A 217 -6.771 -8.211 9.857 1.00 33.98 O ANISOU 1603 OD2 ASP A 217 3832 4667 4411 -1061 -332 26 O ATOM 1604 N ASN A 218 -9.831 -3.710 9.712 1.00 33.16 N ANISOU 1604 N ASN A 218 3346 4876 4378 -862 -446 197 N ATOM 1605 CA ASN A 218 -11.137 -3.057 9.635 1.00 37.47 C ANISOU 1605 CA ASN A 218 3725 5477 5037 -850 -485 241 C ATOM 1606 C ASN A 218 -11.096 -1.757 8.846 1.00 36.75 C ANISOU 1606 C ASN A 218 3628 5448 4889 -772 -578 264 C ATOM 1607 O ASN A 218 -11.989 -1.473 8.054 1.00 36.06 O ANISOU 1607 O ASN A 218 3430 5412 4859 -789 -697 279 O ATOM 1608 CB ASN A 218 -11.689 -2.760 11.032 1.00 43.34 C ANISOU 1608 CB ASN A 218 4386 6208 5875 -811 -333 297 C ATOM 1609 CG ASN A 218 -11.965 -4.011 11.834 1.00 52.72 C ANISOU 1609 CG ASN A 218 5553 7340 7139 -894 -239 300 C ATOM 1610 OD1 ASN A 218 -12.217 -5.082 11.278 1.00 58.21 O ANISOU 1610 OD1 ASN A 218 6231 8005 7881 -993 -306 263 O ATOM 1611 ND2 ASN A 218 -11.928 -3.881 13.155 1.00 54.39 N ANISOU 1611 ND2 ASN A 218 5770 7534 7361 -857 -82 344 N ATOM 1612 N ILE A 219 -10.055 -0.964 9.072 1.00 33.65 N ANISOU 1612 N ILE A 219 3349 5047 4391 -688 -526 273 N ATOM 1613 CA ILE A 219 -10.007 0.382 8.520 1.00 32.48 C ANISOU 1613 CA ILE A 219 3192 4941 4208 -603 -586 312 C ATOM 1614 C ILE A 219 -9.464 0.418 7.090 1.00 32.94 C ANISOU 1614 C ILE A 219 3337 5036 4145 -624 -725 288 C ATOM 1615 O ILE A 219 -9.965 1.159 6.254 1.00 29.91 O ANISOU 1615 O ILE A 219 2896 4706 3764 -599 -836 329 O ATOM 1616 CB ILE A 219 -9.175 1.304 9.431 1.00 30.87 C ANISOU 1616 CB ILE A 219 3063 4707 3959 -506 -465 330 C ATOM 1617 CG1 ILE A 219 -9.855 1.410 10.800 1.00 31.15 C ANISOU 1617 CG1 ILE A 219 3007 4724 4103 -482 -328 353 C ATOM 1618 CG2 ILE A 219 -9.018 2.688 8.807 1.00 27.90 C ANISOU 1618 CG2 ILE A 219 2689 4357 3556 -422 -524 371 C ATOM 1619 CD1 ILE A 219 -8.989 1.998 11.884 1.00 33.15 C ANISOU 1619 CD1 ILE A 219 3353 4945 4296 -413 -199 348 C ATOM 1620 N LEU A 220 -8.460 -0.394 6.790 1.00 32.73 N ANISOU 1620 N LEU A 220 3445 4979 4011 -670 -719 225 N ATOM 1621 CA LEU A 220 -7.838 -0.306 5.474 1.00 32.24 C ANISOU 1621 CA LEU A 220 3481 4954 3815 -685 -824 196 C ATOM 1622 C LEU A 220 -7.984 -1.565 4.623 1.00 36.31 C ANISOU 1622 C LEU A 220 4024 5476 4297 -797 -909 115 C ATOM 1623 O LEU A 220 -7.608 -1.573 3.449 1.00 39.69 O ANISOU 1623 O LEU A 220 4531 5946 4604 -822 -1003 80 O ATOM 1624 CB LEU A 220 -6.363 0.052 5.635 1.00 28.07 C ANISOU 1624 CB LEU A 220 3100 4389 3175 -629 -744 184 C ATOM 1625 CG LEU A 220 -6.159 1.472 6.165 1.00 32.37 C ANISOU 1625 CG LEU A 220 3631 4934 3735 -522 -691 254 C ATOM 1626 CD1 LEU A 220 -5.309 1.481 7.424 1.00 30.12 C ANISOU 1626 CD1 LEU A 220 3405 4585 3454 -481 -550 243 C ATOM 1627 CD2 LEU A 220 -5.543 2.349 5.088 1.00 34.33 C ANISOU 1627 CD2 LEU A 220 3953 5217 3874 -483 -759 281 C ATOM 1628 N GLY A 221 -8.540 -2.624 5.204 1.00 36.62 N ANISOU 1628 N GLY A 221 4002 5472 4442 -867 -873 82 N ATOM 1629 CA GLY A 221 -8.715 -3.874 4.483 1.00 35.94 C ANISOU 1629 CA GLY A 221 3934 5372 4348 -981 -946 -8 C ATOM 1630 C GLY A 221 -7.745 -4.949 4.946 1.00 34.41 C ANISOU 1630 C GLY A 221 3850 5083 4139 -1013 -842 -72 C ATOM 1631 O GLY A 221 -6.651 -4.644 5.413 1.00 31.05 O ANISOU 1631 O GLY A 221 3522 4623 3651 -946 -749 -58 O ATOM 1632 N ASN A 222 -8.150 -6.208 4.802 1.00 36.51 N ANISOU 1632 N ASN A 222 4093 5302 4475 -1117 -864 -141 N ATOM 1633 CA ASN A 222 -7.357 -7.351 5.251 1.00 36.66 C ANISOU 1633 CA ASN A 222 4199 5214 4516 -1153 -769 -196 C ATOM 1634 C ASN A 222 -5.967 -7.440 4.633 1.00 34.99 C ANISOU 1634 C ASN A 222 4149 4980 4166 -1127 -751 -261 C ATOM 1635 O ASN A 222 -5.053 -7.987 5.241 1.00 36.99 O ANISOU 1635 O ASN A 222 4475 5147 4432 -1108 -648 -270 O ATOM 1636 CB ASN A 222 -8.103 -8.660 4.957 1.00 40.26 C ANISOU 1636 CB ASN A 222 4600 5619 5077 -1280 -816 -272 C ATOM 1637 CG ASN A 222 -9.281 -8.886 5.882 1.00 48.35 C ANISOU 1637 CG ASN A 222 5469 6626 6275 -1314 -781 -205 C ATOM 1638 OD1 ASN A 222 -9.774 -7.958 6.523 1.00 50.79 O ANISOU 1638 OD1 ASN A 222 5693 6986 6617 -1247 -748 -111 O ATOM 1639 ND2 ASN A 222 -9.745 -10.128 5.952 1.00 53.40 N ANISOU 1639 ND2 ASN A 222 6068 7187 7034 -1420 -778 -255 N ATOM 1640 N GLU A 223 -5.809 -6.914 3.423 1.00 34.02 N ANISOU 1640 N GLU A 223 4077 4936 3913 -1125 -848 -299 N ATOM 1641 CA GLU A 223 -4.574 -7.107 2.669 1.00 32.60 C ANISOU 1641 CA GLU A 223 4045 4739 3603 -1117 -828 -375 C ATOM 1642 C GLU A 223 -3.565 -5.982 2.855 1.00 33.61 C ANISOU 1642 C GLU A 223 4241 4892 3639 -1007 -767 -310 C ATOM 1643 O GLU A 223 -2.406 -6.114 2.463 1.00 33.48 O ANISOU 1643 O GLU A 223 4337 4846 3536 -987 -717 -359 O ATOM 1644 CB GLU A 223 -4.893 -7.265 1.181 1.00 33.16 C ANISOU 1644 CB GLU A 223 4153 4884 3563 -1189 -959 -464 C ATOM 1645 CG GLU A 223 -5.744 -8.480 0.862 1.00 33.11 C ANISOU 1645 CG GLU A 223 4096 4844 3641 -1313 -1027 -559 C ATOM 1646 CD GLU A 223 -6.088 -8.590 -0.612 1.00 36.71 C ANISOU 1646 CD GLU A 223 4595 5388 3967 -1390 -1172 -654 C ATOM 1647 OE1 GLU A 223 -5.632 -7.738 -1.402 1.00 38.13 O ANISOU 1647 OE1 GLU A 223 4851 5658 3980 -1345 -1212 -636 O ATOM 1648 OE2 GLU A 223 -6.819 -9.530 -0.982 1.00 37.14 O ANISOU 1648 OE2 GLU A 223 4607 5423 4082 -1500 -1247 -746 O ATOM 1649 N TRP A 224 -4.001 -4.883 3.462 1.00 33.09 N ANISOU 1649 N TRP A 224 4100 4871 3603 -937 -764 -204 N ATOM 1650 CA TRP A 224 -3.188 -3.672 3.511 1.00 31.55 C ANISOU 1650 CA TRP A 224 3957 4705 3326 -840 -726 -143 C ATOM 1651 C TRP A 224 -1.891 -3.821 4.310 1.00 30.75 C ANISOU 1651 C TRP A 224 3934 4523 3225 -789 -601 -144 C ATOM 1652 O TRP A 224 -0.813 -3.462 3.834 1.00 30.08 O ANISOU 1652 O TRP A 224 3942 4438 3048 -752 -574 -161 O ATOM 1653 CB TRP A 224 -3.997 -2.517 4.093 1.00 28.22 C ANISOU 1653 CB TRP A 224 3429 4329 2963 -777 -740 -39 C ATOM 1654 CG TRP A 224 -3.218 -1.235 4.148 1.00 27.92 C ANISOU 1654 CG TRP A 224 3440 4308 2860 -682 -704 21 C ATOM 1655 CD1 TRP A 224 -2.976 -0.381 3.111 1.00 29.93 C ANISOU 1655 CD1 TRP A 224 3738 4624 3009 -656 -769 46 C ATOM 1656 CD2 TRP A 224 -2.589 -0.657 5.301 1.00 26.13 C ANISOU 1656 CD2 TRP A 224 3222 4035 2670 -607 -597 65 C ATOM 1657 NE1 TRP A 224 -2.232 0.691 3.545 1.00 29.58 N ANISOU 1657 NE1 TRP A 224 3724 4562 2952 -569 -703 104 N ATOM 1658 CE2 TRP A 224 -1.981 0.547 4.884 1.00 27.83 C ANISOU 1658 CE2 TRP A 224 3482 4277 2816 -539 -601 108 C ATOM 1659 CE3 TRP A 224 -2.477 -1.041 6.642 1.00 26.41 C ANISOU 1659 CE3 TRP A 224 3238 4012 2786 -594 -500 73 C ATOM 1660 CZ2 TRP A 224 -1.273 1.374 5.763 1.00 25.83 C ANISOU 1660 CZ2 TRP A 224 3247 3988 2580 -464 -516 145 C ATOM 1661 CZ3 TRP A 224 -1.771 -0.219 7.514 1.00 26.04 C ANISOU 1661 CZ3 TRP A 224 3217 3942 2735 -517 -421 111 C ATOM 1662 CH2 TRP A 224 -1.181 0.975 7.070 1.00 24.20 C ANISOU 1662 CH2 TRP A 224 3022 3731 2442 -455 -432 140 C ATOM 1663 N ALA A 225 -2.002 -4.344 5.525 1.00 29.10 N ANISOU 1663 N ALA A 225 3684 4249 3122 -787 -526 -121 N ATOM 1664 CA ALA A 225 -0.864 -4.389 6.433 1.00 31.44 C ANISOU 1664 CA ALA A 225 4040 4481 3426 -733 -423 -103 C ATOM 1665 C ALA A 225 0.163 -5.457 6.056 1.00 34.42 C ANISOU 1665 C ALA A 225 4507 4782 3788 -764 -388 -181 C ATOM 1666 O ALA A 225 0.099 -6.581 6.541 1.00 39.34 O ANISOU 1666 O ALA A 225 5123 5330 4496 -808 -353 -203 O ATOM 1667 CB ALA A 225 -1.348 -4.608 7.864 1.00 29.20 C ANISOU 1667 CB ALA A 225 3690 4161 3242 -724 -359 -43 C ATOM 1668 N ASP A 226 1.108 -5.103 5.189 1.00 34.53 N ANISOU 1668 N ASP A 226 4603 4812 3705 -740 -388 -220 N ATOM 1669 CA ASP A 226 2.278 -5.944 4.965 1.00 30.79 C ANISOU 1669 CA ASP A 226 4210 4259 3229 -746 -328 -288 C ATOM 1670 C ASP A 226 3.515 -5.230 5.521 1.00 28.30 C ANISOU 1670 C ASP A 226 3931 3924 2896 -662 -260 -240 C ATOM 1671 O ASP A 226 3.404 -4.143 6.094 1.00 28.35 O ANISOU 1671 O ASP A 226 3906 3975 2891 -608 -261 -164 O ATOM 1672 CB ASP A 226 2.448 -6.298 3.475 1.00 29.15 C ANISOU 1672 CB ASP A 226 4070 4076 2929 -797 -366 -390 C ATOM 1673 CG ASP A 226 2.580 -5.070 2.564 1.00 29.50 C ANISOU 1673 CG ASP A 226 4147 4222 2839 -765 -408 -366 C ATOM 1674 OD1 ASP A 226 2.960 -3.974 3.026 1.00 27.09 O ANISOU 1674 OD1 ASP A 226 3831 3941 2522 -692 -384 -283 O ATOM 1675 OD2 ASP A 226 2.308 -5.212 1.355 1.00 30.70 O ANISOU 1675 OD2 ASP A 226 4340 4429 2894 -816 -467 -431 O ATOM 1676 N ALA A 227 4.686 -5.835 5.354 1.00 26.63 N ANISOU 1676 N ALA A 227 3781 3644 2695 -652 -200 -289 N ATOM 1677 CA ALA A 227 5.917 -5.287 5.927 1.00 27.96 C ANISOU 1677 CA ALA A 227 3972 3785 2869 -579 -140 -247 C ATOM 1678 C ALA A 227 6.221 -3.860 5.443 1.00 27.25 C ANISOU 1678 C ALA A 227 3896 3770 2686 -533 -152 -213 C ATOM 1679 O ALA A 227 6.948 -3.117 6.098 1.00 26.94 O ANISOU 1679 O ALA A 227 3853 3724 2660 -474 -120 -162 O ATOM 1680 CB ALA A 227 7.088 -6.211 5.621 1.00 25.08 C ANISOU 1680 CB ALA A 227 3657 3331 2541 -578 -77 -314 C ATOM 1681 N ASN A 228 5.656 -3.471 4.305 1.00 27.82 N ANISOU 1681 N ASN A 228 3986 3916 2670 -562 -204 -237 N ATOM 1682 CA ASN A 228 5.888 -2.130 3.778 1.00 28.22 C ANISOU 1682 CA ASN A 228 4052 4033 2638 -521 -217 -190 C ATOM 1683 C ASN A 228 4.821 -1.123 4.225 1.00 29.04 C ANISOU 1683 C ASN A 228 4087 4194 2751 -498 -275 -108 C ATOM 1684 O ASN A 228 4.882 0.055 3.868 1.00 29.88 O ANISOU 1684 O ASN A 228 4197 4347 2810 -461 -291 -56 O ATOM 1685 CB ASN A 228 5.964 -2.169 2.249 1.00 28.03 C ANISOU 1685 CB ASN A 228 4095 4061 2495 -560 -238 -246 C ATOM 1686 CG ASN A 228 7.111 -3.031 1.744 1.00 30.45 C ANISOU 1686 CG ASN A 228 4470 4309 2792 -573 -158 -335 C ATOM 1687 OD1 ASN A 228 6.904 -4.000 1.012 1.00 29.24 O ANISOU 1687 OD1 ASN A 228 4356 4148 2607 -633 -165 -429 O ATOM 1688 ND2 ASN A 228 8.331 -2.674 2.129 1.00 29.79 N ANISOU 1688 ND2 ASN A 228 4396 4178 2744 -519 -79 -313 N ATOM 1689 N HIS A 229 3.855 -1.581 5.014 1.00 28.48 N ANISOU 1689 N HIS A 229 3952 4115 2754 -519 -299 -95 N ATOM 1690 CA HIS A 229 2.783 -0.702 5.482 1.00 26.12 C ANISOU 1690 CA HIS A 229 3577 3864 2484 -495 -341 -25 C ATOM 1691 C HIS A 229 2.531 -0.795 6.985 1.00 24.77 C ANISOU 1691 C HIS A 229 3353 3656 2402 -472 -294 11 C ATOM 1692 O HIS A 229 1.750 -0.020 7.537 1.00 24.85 O ANISOU 1692 O HIS A 229 3300 3697 2447 -443 -304 62 O ATOM 1693 CB HIS A 229 1.481 -1.014 4.742 1.00 26.77 C ANISOU 1693 CB HIS A 229 3612 4002 2556 -553 -430 -38 C ATOM 1694 CG HIS A 229 1.512 -0.670 3.285 1.00 29.65 C ANISOU 1694 CG HIS A 229 4026 4432 2808 -573 -495 -54 C ATOM 1695 ND1 HIS A 229 2.028 -1.520 2.329 1.00 27.83 N ANISOU 1695 ND1 HIS A 229 3875 4197 2503 -626 -496 -140 N ATOM 1696 CD2 HIS A 229 1.086 0.431 2.621 1.00 27.79 C ANISOU 1696 CD2 HIS A 229 3775 4267 2517 -547 -559 8 C ATOM 1697 CE1 HIS A 229 1.917 -0.957 1.139 1.00 28.39 C ANISOU 1697 CE1 HIS A 229 3985 4345 2458 -636 -557 -132 C ATOM 1698 NE2 HIS A 229 1.350 0.228 1.289 1.00 28.81 N ANISOU 1698 NE2 HIS A 229 3981 4444 2523 -587 -601 -33 N ATOM 1699 N PHE A 230 3.184 -1.742 7.647 1.00 24.50 N ANISOU 1699 N PHE A 230 3346 3555 2407 -484 -242 -13 N ATOM 1700 CA PHE A 230 2.877 -2.029 9.046 1.00 23.71 C ANISOU 1700 CA PHE A 230 3207 3428 2376 -475 -201 25 C ATOM 1701 C PHE A 230 4.076 -2.657 9.753 1.00 24.80 C ANISOU 1701 C PHE A 230 3394 3496 2534 -459 -146 22 C ATOM 1702 O PHE A 230 4.685 -3.598 9.240 1.00 22.07 O ANISOU 1702 O PHE A 230 3088 3099 2200 -486 -138 -25 O ATOM 1703 CB PHE A 230 1.662 -2.958 9.129 1.00 23.91 C ANISOU 1703 CB PHE A 230 3174 3451 2459 -540 -222 19 C ATOM 1704 CG PHE A 230 1.045 -3.062 10.504 1.00 23.02 C ANISOU 1704 CG PHE A 230 3008 3331 2407 -535 -175 73 C ATOM 1705 CD1 PHE A 230 1.676 -3.764 11.522 1.00 22.76 C ANISOU 1705 CD1 PHE A 230 3007 3240 2400 -531 -118 95 C ATOM 1706 CD2 PHE A 230 -0.198 -2.496 10.761 1.00 23.82 C ANISOU 1706 CD2 PHE A 230 3024 3484 2541 -534 -186 107 C ATOM 1707 CE1 PHE A 230 1.090 -3.871 12.784 1.00 24.14 C ANISOU 1707 CE1 PHE A 230 3143 3418 2610 -531 -68 152 C ATOM 1708 CE2 PHE A 230 -0.790 -2.601 12.016 1.00 24.27 C ANISOU 1708 CE2 PHE A 230 3035 3539 2648 -532 -125 153 C ATOM 1709 CZ PHE A 230 -0.144 -3.289 13.028 1.00 23.02 C ANISOU 1709 CZ PHE A 230 2922 3331 2492 -533 -64 176 C ATOM 1710 N ARG A 231 4.412 -2.133 10.929 1.00 26.32 N ANISOU 1710 N ARG A 231 3581 3685 2733 -414 -112 68 N ATOM 1711 CA ARG A 231 5.466 -2.716 11.754 1.00 25.56 C ANISOU 1711 CA ARG A 231 3520 3531 2659 -397 -77 82 C ATOM 1712 C ARG A 231 5.049 -2.735 13.213 1.00 27.18 C ANISOU 1712 C ARG A 231 3704 3745 2878 -388 -48 139 C ATOM 1713 O ARG A 231 4.346 -1.839 13.669 1.00 31.71 O ANISOU 1713 O ARG A 231 4245 4371 3430 -369 -41 159 O ATOM 1714 CB ARG A 231 6.783 -1.939 11.614 1.00 23.32 C ANISOU 1714 CB ARG A 231 3274 3240 2347 -347 -70 73 C ATOM 1715 CG ARG A 231 7.317 -1.827 10.206 1.00 23.57 C ANISOU 1715 CG ARG A 231 3335 3269 2352 -352 -79 23 C ATOM 1716 CD ARG A 231 7.838 -3.151 9.670 1.00 23.62 C ANISOU 1716 CD ARG A 231 3370 3210 2395 -385 -62 -24 C ATOM 1717 NE ARG A 231 8.392 -2.960 8.332 1.00 27.92 N ANISOU 1717 NE ARG A 231 3950 3761 2895 -389 -55 -79 N ATOM 1718 CZ ARG A 231 9.581 -2.411 8.086 1.00 28.50 C ANISOU 1718 CZ ARG A 231 4047 3822 2961 -350 -24 -83 C ATOM 1719 NH1 ARG A 231 10.359 -2.021 9.089 1.00 24.95 N ANISOU 1719 NH1 ARG A 231 3581 3349 2549 -307 -12 -42 N ATOM 1720 NH2 ARG A 231 9.998 -2.262 6.837 1.00 29.82 N ANISOU 1720 NH2 ARG A 231 4251 4002 3079 -360 -5 -130 N ATOM 1721 N PHE A 232 5.481 -3.754 13.946 1.00 23.15 N ANISOU 1721 N PHE A 232 3213 3182 2403 -400 -28 168 N ATOM 1722 CA PHE A 232 5.404 -3.708 15.402 1.00 24.53 C ANISOU 1722 CA PHE A 232 3390 3371 2561 -385 0 231 C ATOM 1723 C PHE A 232 6.764 -3.303 15.960 1.00 27.65 C ANISOU 1723 C PHE A 232 3825 3753 2925 -337 -10 243 C ATOM 1724 O PHE A 232 7.764 -3.972 15.708 1.00 26.50 O ANISOU 1724 O PHE A 232 3702 3548 2818 -332 -21 240 O ATOM 1725 CB PHE A 232 4.989 -5.058 15.996 1.00 20.73 C ANISOU 1725 CB PHE A 232 2902 2841 2133 -430 25 279 C ATOM 1726 CG PHE A 232 3.530 -5.378 15.840 1.00 25.24 C ANISOU 1726 CG PHE A 232 3418 3431 2740 -482 42 282 C ATOM 1727 CD1 PHE A 232 2.574 -4.719 16.600 1.00 28.70 C ANISOU 1727 CD1 PHE A 232 3819 3935 3150 -478 77 314 C ATOM 1728 CD2 PHE A 232 3.114 -6.359 14.954 1.00 24.07 C ANISOU 1728 CD2 PHE A 232 3250 3231 2662 -539 27 248 C ATOM 1729 CE1 PHE A 232 1.222 -5.027 16.463 1.00 30.24 C ANISOU 1729 CE1 PHE A 232 3946 4146 3399 -527 96 320 C ATOM 1730 CE2 PHE A 232 1.771 -6.669 14.814 1.00 22.38 C ANISOU 1730 CE2 PHE A 232 2974 3034 2497 -594 34 249 C ATOM 1731 CZ PHE A 232 0.827 -6.004 15.569 1.00 29.66 C ANISOU 1731 CZ PHE A 232 3846 4023 3401 -587 68 290 C ATOM 1732 N GLY A 233 6.808 -2.207 16.709 1.00 29.28 N ANISOU 1732 N GLY A 233 4037 4014 3075 -303 -5 251 N ATOM 1733 CA GLY A 233 8.024 -1.841 17.408 1.00 29.53 C ANISOU 1733 CA GLY A 233 4102 4041 3078 -267 -25 263 C ATOM 1734 C GLY A 233 8.059 -2.520 18.762 1.00 30.00 C ANISOU 1734 C GLY A 233 4185 4104 3111 -275 -18 332 C ATOM 1735 O GLY A 233 7.328 -2.127 19.669 1.00 27.59 O ANISOU 1735 O GLY A 233 3884 3854 2747 -278 12 352 O ATOM 1736 N ALA A 234 8.902 -3.541 18.905 1.00 29.90 N ANISOU 1736 N ALA A 234 4187 4031 3141 -276 -40 372 N ATOM 1737 CA ALA A 234 8.902 -4.338 20.126 1.00 31.62 C ANISOU 1737 CA ALA A 234 4430 4247 3338 -287 -38 460 C ATOM 1738 C ALA A 234 10.220 -5.075 20.372 1.00 34.62 C ANISOU 1738 C ALA A 234 4824 4564 3766 -265 -87 507 C ATOM 1739 O ALA A 234 11.056 -5.199 19.480 1.00 33.88 O ANISOU 1739 O ALA A 234 4714 4414 3747 -247 -106 466 O ATOM 1740 CB ALA A 234 7.749 -5.334 20.087 1.00 30.64 C ANISOU 1740 CB ALA A 234 4289 4098 3255 -335 9 497 C ATOM 1741 N SER A 235 10.392 -5.567 21.596 1.00 39.03 N ANISOU 1741 N SER A 235 5412 5135 4283 -266 -104 599 N ATOM 1742 CA SER A 235 11.547 -6.388 21.942 1.00 41.85 C ANISOU 1742 CA SER A 235 5774 5429 4698 -243 -158 669 C ATOM 1743 C SER A 235 11.126 -7.796 22.388 1.00 42.95 C ANISOU 1743 C SER A 235 5921 5506 4890 -270 -135 774 C ATOM 1744 O SER A 235 11.218 -8.759 21.620 1.00 42.78 O ANISOU 1744 O SER A 235 5875 5384 4997 -279 -118 770 O ATOM 1745 CB SER A 235 12.375 -5.707 23.035 1.00 45.58 C ANISOU 1745 CB SER A 235 6275 5968 5076 -216 -225 702 C ATOM 1746 OG SER A 235 11.597 -5.439 24.188 1.00 48.46 O ANISOU 1746 OG SER A 235 6685 6420 5306 -237 -205 746 O ATOM 1747 N SER A 236 10.648 -7.911 23.624 1.00 41.13 N ANISOU 1747 N SER A 236 5730 5335 4563 -287 -128 864 N ATOM 1748 CA SER A 236 10.334 -9.218 24.194 1.00 41.03 C ANISOU 1748 CA SER A 236 5730 5264 4596 -313 -108 989 C ATOM 1749 C SER A 236 9.069 -9.845 23.604 1.00 37.21 C ANISOU 1749 C SER A 236 5219 4734 4184 -366 -24 972 C ATOM 1750 O SER A 236 8.728 -10.977 23.942 1.00 38.29 O ANISOU 1750 O SER A 236 5358 4803 4386 -396 3 1069 O ATOM 1751 CB SER A 236 10.206 -9.117 25.715 1.00 43.17 C ANISOU 1751 CB SER A 236 6060 5624 4720 -318 -119 1099 C ATOM 1752 OG SER A 236 9.549 -7.924 26.096 1.00 45.40 O ANISOU 1752 OG SER A 236 6364 6026 4860 -327 -84 1031 O ATOM 1753 N LEU A 237 8.387 -9.116 22.723 1.00 30.98 N ANISOU 1753 N LEU A 237 4400 3978 3392 -380 9 855 N ATOM 1754 CA LEU A 237 7.274 -9.672 21.961 1.00 27.97 C ANISOU 1754 CA LEU A 237 3979 3552 3095 -432 67 821 C ATOM 1755 C LEU A 237 7.680 -10.940 21.203 1.00 29.94 C ANISOU 1755 C LEU A 237 4212 3662 3502 -446 60 823 C ATOM 1756 O LEU A 237 6.912 -11.892 21.130 1.00 29.94 O ANISOU 1756 O LEU A 237 4193 3597 3585 -498 102 857 O ATOM 1757 CB LEU A 237 6.725 -8.635 20.974 1.00 24.83 C ANISOU 1757 CB LEU A 237 3550 3210 2675 -434 76 694 C ATOM 1758 CG LEU A 237 5.697 -9.097 19.929 1.00 26.00 C ANISOU 1758 CG LEU A 237 3649 3318 2912 -487 107 634 C ATOM 1759 CD1 LEU A 237 4.425 -9.634 20.587 1.00 24.50 C ANISOU 1759 CD1 LEU A 237 3435 3138 2736 -544 170 703 C ATOM 1760 CD2 LEU A 237 5.359 -7.978 18.958 1.00 23.77 C ANISOU 1760 CD2 LEU A 237 3340 3097 2595 -476 93 525 C ATOM 1761 N LEU A 238 8.890 -10.945 20.648 1.00 32.07 N ANISOU 1761 N LEU A 238 4482 3880 3823 -401 13 782 N ATOM 1762 CA LEU A 238 9.360 -12.052 19.815 1.00 31.77 C ANISOU 1762 CA LEU A 238 4426 3704 3941 -406 16 757 C ATOM 1763 C LEU A 238 9.338 -13.386 20.555 1.00 31.65 C ANISOU 1763 C LEU A 238 4418 3589 4021 -424 30 886 C ATOM 1764 O LEU A 238 8.891 -14.397 20.013 1.00 32.38 O ANISOU 1764 O LEU A 238 4492 3574 4239 -466 66 870 O ATOM 1765 CB LEU A 238 10.776 -11.774 19.301 1.00 33.97 C ANISOU 1765 CB LEU A 238 4700 3950 4256 -345 -26 708 C ATOM 1766 CG LEU A 238 11.395 -12.900 18.465 1.00 37.29 C ANISOU 1766 CG LEU A 238 5101 4222 4845 -339 -9 673 C ATOM 1767 CD1 LEU A 238 10.584 -13.148 17.194 1.00 36.48 C ANISOU 1767 CD1 LEU A 238 4989 4088 4783 -394 37 547 C ATOM 1768 CD2 LEU A 238 12.845 -12.599 18.124 1.00 38.30 C ANISOU 1768 CD2 LEU A 238 5214 4324 5015 -273 -41 640 C ATOM 1769 N ILE A 239 9.814 -13.380 21.795 1.00 31.03 N ANISOU 1769 N ILE A 239 4366 3543 3879 -394 -4 1015 N ATOM 1770 CA ILE A 239 9.851 -14.585 22.616 1.00 33.03 C ANISOU 1770 CA ILE A 239 4632 3708 4210 -404 2 1168 C ATOM 1771 C ILE A 239 8.440 -15.100 22.862 1.00 32.20 C ANISOU 1771 C ILE A 239 4525 3598 4113 -480 77 1210 C ATOM 1772 O ILE A 239 8.187 -16.306 22.825 1.00 31.39 O ANISOU 1772 O ILE A 239 4410 3368 4150 -514 109 1272 O ATOM 1773 CB ILE A 239 10.549 -14.322 23.971 1.00 35.82 C ANISOU 1773 CB ILE A 239 5026 4133 4452 -362 -60 1305 C ATOM 1774 CG1 ILE A 239 11.995 -13.884 23.743 1.00 40.20 C ANISOU 1774 CG1 ILE A 239 5566 4682 5027 -291 -142 1270 C ATOM 1775 CG2 ILE A 239 10.508 -15.561 24.859 1.00 30.54 C ANISOU 1775 CG2 ILE A 239 4375 3378 3850 -375 -55 1487 C ATOM 1776 CD1 ILE A 239 12.672 -13.339 24.988 1.00 43.94 C ANISOU 1776 CD1 ILE A 239 6076 5257 5363 -255 -223 1371 C ATOM 1777 N SER A 240 7.526 -14.169 23.108 1.00 29.57 N ANISOU 1777 N SER A 240 4196 3396 3644 -506 108 1174 N ATOM 1778 CA SER A 240 6.125 -14.505 23.312 1.00 32.01 C ANISOU 1778 CA SER A 240 4486 3715 3962 -579 186 1203 C ATOM 1779 C SER A 240 5.517 -15.154 22.068 1.00 28.89 C ANISOU 1779 C SER A 240 4039 3218 3723 -632 214 1100 C ATOM 1780 O SER A 240 4.882 -16.205 22.153 1.00 29.96 O ANISOU 1780 O SER A 240 4154 3259 3972 -691 260 1159 O ATOM 1781 CB SER A 240 5.329 -13.254 23.695 1.00 34.08 C ANISOU 1781 CB SER A 240 4750 4136 4063 -584 217 1161 C ATOM 1782 OG SER A 240 3.967 -13.577 23.913 1.00 36.39 O ANISOU 1782 OG SER A 240 5010 4439 4380 -653 300 1193 O ATOM 1783 N LEU A 241 5.705 -14.513 20.918 1.00 29.10 N ANISOU 1783 N LEU A 241 4045 3265 3748 -616 184 948 N ATOM 1784 CA LEU A 241 5.193 -15.032 19.653 1.00 29.27 C ANISOU 1784 CA LEU A 241 4026 3206 3887 -668 195 832 C ATOM 1785 C LEU A 241 5.734 -16.425 19.359 1.00 35.57 C ANISOU 1785 C LEU A 241 4826 3828 4860 -680 201 852 C ATOM 1786 O LEU A 241 4.986 -17.322 18.966 1.00 39.65 O ANISOU 1786 O LEU A 241 5315 4253 5499 -751 234 832 O ATOM 1787 CB LEU A 241 5.542 -14.084 18.508 1.00 28.26 C ANISOU 1787 CB LEU A 241 3895 3136 3706 -638 156 681 C ATOM 1788 CG LEU A 241 4.902 -12.697 18.609 1.00 28.22 C ANISOU 1788 CG LEU A 241 3878 3286 3559 -629 153 646 C ATOM 1789 CD1 LEU A 241 5.095 -11.917 17.319 1.00 24.77 C ANISOU 1789 CD1 LEU A 241 3432 2887 3091 -613 117 507 C ATOM 1790 CD2 LEU A 241 3.417 -12.819 18.967 1.00 28.87 C ANISOU 1790 CD2 LEU A 241 3915 3405 3650 -696 202 680 C ATOM 1791 N LEU A 242 7.035 -16.603 19.553 1.00 35.71 N ANISOU 1791 N LEU A 242 4872 3794 4904 -612 167 891 N ATOM 1792 CA LEU A 242 7.653 -17.906 19.348 1.00 35.65 C ANISOU 1792 CA LEU A 242 4861 3607 5078 -608 175 919 C ATOM 1793 C LEU A 242 7.000 -18.963 20.240 1.00 36.29 C ANISOU 1793 C LEU A 242 4939 3604 5247 -658 216 1069 C ATOM 1794 O LEU A 242 6.690 -20.063 19.781 1.00 38.65 O ANISOU 1794 O LEU A 242 5217 3753 5715 -708 251 1049 O ATOM 1795 CB LEU A 242 9.159 -17.829 19.609 1.00 32.18 C ANISOU 1795 CB LEU A 242 4437 3138 4651 -517 128 963 C ATOM 1796 CG LEU A 242 9.912 -17.027 18.545 1.00 32.94 C ANISOU 1796 CG LEU A 242 4528 3275 4712 -473 105 809 C ATOM 1797 CD1 LEU A 242 11.363 -16.789 18.950 1.00 28.66 C ANISOU 1797 CD1 LEU A 242 3987 2727 4176 -385 55 864 C ATOM 1798 CD2 LEU A 242 9.824 -17.742 17.200 1.00 33.39 C ANISOU 1798 CD2 LEU A 242 4571 3214 4903 -509 144 662 C ATOM 1799 N ASP A 243 6.771 -18.621 21.504 1.00 35.20 N ANISOU 1799 N ASP A 243 4825 3560 4991 -650 218 1217 N ATOM 1800 CA ASP A 243 6.126 -19.549 22.432 1.00 39.23 C ANISOU 1800 CA ASP A 243 5338 4007 5562 -700 268 1380 C ATOM 1801 C ASP A 243 4.704 -19.902 21.987 1.00 39.60 C ANISOU 1801 C ASP A 243 5339 4029 5678 -801 334 1323 C ATOM 1802 O ASP A 243 4.298 -21.059 22.058 1.00 40.94 O ANISOU 1802 O ASP A 243 5490 4057 6008 -857 377 1387 O ATOM 1803 CB ASP A 243 6.097 -18.972 23.847 1.00 45.12 C ANISOU 1803 CB ASP A 243 6128 4889 6127 -676 264 1534 C ATOM 1804 CG ASP A 243 5.542 -19.956 24.862 1.00 55.80 C ANISOU 1804 CG ASP A 243 7493 6177 7530 -724 321 1726 C ATOM 1805 OD1 ASP A 243 6.052 -21.099 24.926 1.00 58.84 O ANISOU 1805 OD1 ASP A 243 7879 6399 8079 -718 314 1819 O ATOM 1806 OD2 ASP A 243 4.583 -19.595 25.585 1.00 60.40 O ANISOU 1806 OD2 ASP A 243 8084 6867 7997 -769 380 1787 O ATOM 1807 N THR A 244 3.953 -18.907 21.522 1.00 38.54 N ANISOU 1807 N THR A 244 5180 4026 5437 -824 338 1207 N ATOM 1808 CA THR A 244 2.606 -19.149 21.007 1.00 39.00 C ANISOU 1808 CA THR A 244 5179 4073 5566 -918 385 1141 C ATOM 1809 C THR A 244 2.653 -20.107 19.815 1.00 38.23 C ANISOU 1809 C THR A 244 5055 3814 5657 -963 374 1021 C ATOM 1810 O THR A 244 1.764 -20.935 19.631 1.00 35.92 O ANISOU 1810 O THR A 244 4718 3430 5498 -1051 414 1019 O ATOM 1811 CB THR A 244 1.912 -17.835 20.581 1.00 36.41 C ANISOU 1811 CB THR A 244 4821 3911 5102 -920 373 1028 C ATOM 1812 OG1 THR A 244 1.859 -16.932 21.694 1.00 36.73 O ANISOU 1812 OG1 THR A 244 4889 4094 4972 -879 393 1121 O ATOM 1813 CG2 THR A 244 0.499 -18.106 20.081 1.00 33.11 C ANISOU 1813 CG2 THR A 244 4326 3483 4770 -1018 410 971 C ATOM 1814 N LEU A 245 3.714 -19.993 19.020 1.00 39.05 N ANISOU 1814 N LEU A 245 5185 3881 5771 -905 325 917 N ATOM 1815 CA LEU A 245 3.875 -20.802 17.818 1.00 37.48 C ANISOU 1815 CA LEU A 245 4974 3540 5726 -940 320 777 C ATOM 1816 C LEU A 245 4.540 -22.157 18.096 1.00 38.72 C ANISOU 1816 C LEU A 245 5144 3491 6075 -932 346 858 C ATOM 1817 O LEU A 245 4.743 -22.956 17.180 1.00 40.56 O ANISOU 1817 O LEU A 245 5371 3581 6459 -959 354 741 O ATOM 1818 CB LEU A 245 4.681 -20.022 16.774 1.00 37.68 C ANISOU 1818 CB LEU A 245 5022 3624 5669 -883 273 620 C ATOM 1819 CG LEU A 245 3.984 -18.776 16.225 1.00 34.31 C ANISOU 1819 CG LEU A 245 4579 3372 5086 -898 243 521 C ATOM 1820 CD1 LEU A 245 4.908 -17.984 15.327 1.00 32.56 C ANISOU 1820 CD1 LEU A 245 4389 3207 4777 -834 205 400 C ATOM 1821 CD2 LEU A 245 2.723 -19.176 15.475 1.00 34.29 C ANISOU 1821 CD2 LEU A 245 4528 3348 5152 -1003 247 425 C ATOM 1822 N GLY A 246 4.878 -22.409 19.357 1.00 39.16 N ANISOU 1822 N GLY A 246 5220 3534 6126 -894 358 1056 N ATOM 1823 CA GLY A 246 5.440 -23.687 19.760 1.00 40.92 C ANISOU 1823 CA GLY A 246 5450 3560 6539 -883 380 1171 C ATOM 1824 C GLY A 246 6.921 -23.887 19.478 1.00 45.04 C ANISOU 1824 C GLY A 246 5991 3994 7127 -786 344 1151 C ATOM 1825 O GLY A 246 7.368 -25.017 19.277 1.00 49.42 O ANISOU 1825 O GLY A 246 6538 4350 7891 -782 366 1165 O ATOM 1826 N HIS A 247 7.689 -22.803 19.470 1.00 44.04 N ANISOU 1826 N HIS A 247 5884 4007 6842 -708 293 1118 N ATOM 1827 CA HIS A 247 9.132 -22.895 19.266 1.00 44.58 C ANISOU 1827 CA HIS A 247 5957 4007 6974 -612 259 1108 C ATOM 1828 C HIS A 247 9.883 -22.568 20.548 1.00 48.58 C ANISOU 1828 C HIS A 247 6482 4582 7392 -536 205 1303 C ATOM 1829 O HIS A 247 9.910 -21.417 20.982 1.00 49.66 O ANISOU 1829 O HIS A 247 6639 4902 7327 -512 166 1316 O ATOM 1830 CB HIS A 247 9.586 -21.961 18.142 1.00 42.54 C ANISOU 1830 CB HIS A 247 5700 3838 6626 -582 240 910 C ATOM 1831 CG HIS A 247 9.105 -22.371 16.785 1.00 46.11 C ANISOU 1831 CG HIS A 247 6143 4213 7165 -646 281 710 C ATOM 1832 ND1 HIS A 247 9.565 -23.502 16.145 1.00 49.25 N ANISOU 1832 ND1 HIS A 247 6531 4408 7773 -647 321 639 N ATOM 1833 CD2 HIS A 247 8.202 -21.807 15.949 1.00 45.92 C ANISOU 1833 CD2 HIS A 247 6118 4286 7043 -712 284 563 C ATOM 1834 CE1 HIS A 247 8.965 -23.617 14.973 1.00 50.32 C ANISOU 1834 CE1 HIS A 247 6670 4527 7923 -717 347 448 C ATOM 1835 NE2 HIS A 247 8.134 -22.600 14.829 1.00 47.21 N ANISOU 1835 NE2 HIS A 247 6279 4316 7341 -758 318 405 N TER 1836 HIS A 247 ATOM 1837 N SER B 2 57.564 32.497 34.988 1.00 83.68 N ANISOU 1837 N SER B 2 9737 11935 10122 -3290 -467 -3274 N ATOM 1838 CA SER B 2 58.145 31.160 34.970 1.00 81.23 C ANISOU 1838 CA SER B 2 9309 11906 9648 -3219 -641 -3041 C ATOM 1839 C SER B 2 58.216 30.620 33.547 1.00 76.73 C ANISOU 1839 C SER B 2 8727 11156 9269 -3108 -620 -2802 C ATOM 1840 O SER B 2 57.325 30.877 32.737 1.00 75.54 O ANISOU 1840 O SER B 2 8700 10722 9279 -3025 -481 -2773 O ATOM 1841 CB SER B 2 57.334 30.210 35.854 1.00 80.21 C ANISOU 1841 CB SER B 2 9225 12026 9225 -3120 -701 -2982 C ATOM 1842 N ASP B 3 59.277 29.876 33.245 1.00 73.41 N ANISOU 1842 N ASP B 3 8152 10906 8834 -3103 -754 -2626 N ATOM 1843 CA ASP B 3 59.409 29.240 31.939 1.00 67.69 C ANISOU 1843 CA ASP B 3 7399 10052 8268 -2997 -739 -2390 C ATOM 1844 C ASP B 3 58.363 28.139 31.785 1.00 65.59 C ANISOU 1844 C ASP B 3 7216 9833 7874 -2829 -742 -2228 C ATOM 1845 O ASP B 3 57.841 27.901 30.692 1.00 63.29 O ANISOU 1845 O ASP B 3 6988 9332 7728 -2735 -658 -2104 O ATOM 1846 CB ASP B 3 60.815 28.668 31.753 1.00 66.50 C ANISOU 1846 CB ASP B 3 7046 10095 8125 -3026 -878 -2241 C ATOM 1847 N ILE B 4 58.049 27.477 32.892 1.00 63.04 N ANISOU 1847 N ILE B 4 6890 9787 7276 -2796 -834 -2226 N ATOM 1848 CA ILE B 4 57.115 26.366 32.863 1.00 57.52 C ANISOU 1848 CA ILE B 4 6255 9162 6439 -2642 -848 -2061 C ATOM 1849 C ILE B 4 55.678 26.874 32.730 1.00 55.70 C ANISOU 1849 C ILE B 4 6214 8692 6256 -2598 -695 -2177 C ATOM 1850 O ILE B 4 54.826 26.196 32.159 1.00 52.79 O ANISOU 1850 O ILE B 4 5920 8246 5893 -2475 -658 -2044 O ATOM 1851 CB ILE B 4 57.266 25.474 34.118 1.00 57.59 C ANISOU 1851 CB ILE B 4 6193 9547 6140 -2610 -987 -1990 C ATOM 1852 CG1 ILE B 4 56.590 24.117 33.897 1.00 53.42 C ANISOU 1852 CG1 ILE B 4 5688 9104 5504 -2438 -1020 -1745 C ATOM 1853 CG2 ILE B 4 56.757 26.186 35.372 1.00 59.24 C ANISOU 1853 CG2 ILE B 4 6478 9840 6190 -2693 -955 -2227 C ATOM 1854 CD1 ILE B 4 57.161 23.341 32.728 1.00 50.91 C ANISOU 1854 CD1 ILE B 4 5279 8735 5331 -2356 -1054 -1508 C ATOM 1855 N LYS B 5 55.414 28.076 33.236 1.00 56.93 N ANISOU 1855 N LYS B 5 6443 8728 6459 -2697 -601 -2422 N ATOM 1856 CA LYS B 5 54.104 28.691 33.051 1.00 56.12 C ANISOU 1856 CA LYS B 5 6508 8368 6446 -2650 -436 -2530 C ATOM 1857 C LYS B 5 53.903 29.043 31.581 1.00 54.51 C ANISOU 1857 C LYS B 5 6356 7823 6534 -2599 -320 -2446 C ATOM 1858 O LYS B 5 52.782 29.011 31.073 1.00 51.78 O ANISOU 1858 O LYS B 5 6129 7288 6257 -2498 -213 -2411 O ATOM 1859 CB LYS B 5 53.950 29.936 33.928 1.00 58.22 C ANISOU 1859 CB LYS B 5 6825 8579 6716 -2766 -350 -2808 C ATOM 1860 CG LYS B 5 53.726 29.638 35.404 1.00 60.94 C ANISOU 1860 CG LYS B 5 7163 9230 6761 -2795 -421 -2906 C ATOM 1861 CD LYS B 5 53.583 30.918 36.217 1.00 57.90 C ANISOU 1861 CD LYS B 5 6826 8778 6395 -2922 -322 -3198 C ATOM 1862 N ALA B 6 55.000 29.378 30.905 1.00 55.37 N ANISOU 1862 N ALA B 6 6367 7859 6811 -2668 -339 -2406 N ATOM 1863 CA ALA B 6 54.971 29.634 29.471 1.00 52.39 C ANISOU 1863 CA ALA B 6 6018 7188 6701 -2619 -235 -2289 C ATOM 1864 C ALA B 6 54.622 28.355 28.720 1.00 51.76 C ANISOU 1864 C ALA B 6 5934 7156 6575 -2488 -280 -2053 C ATOM 1865 O ALA B 6 53.955 28.393 27.684 1.00 52.59 O ANISOU 1865 O ALA B 6 6124 7022 6837 -2403 -171 -1962 O ATOM 1866 CB ALA B 6 56.304 30.182 28.998 1.00 52.22 C ANISOU 1866 CB ALA B 6 5876 7118 6847 -2725 -252 -2282 C ATOM 1867 N VAL B 7 55.076 27.226 29.257 1.00 50.65 N ANISOU 1867 N VAL B 7 5693 7331 6222 -2467 -438 -1946 N ATOM 1868 CA VAL B 7 54.782 25.913 28.688 1.00 50.11 C ANISOU 1868 CA VAL B 7 5607 7347 6087 -2345 -492 -1720 C ATOM 1869 C VAL B 7 53.338 25.490 28.959 1.00 50.64 C ANISOU 1869 C VAL B 7 5815 7391 6035 -2241 -447 -1719 C ATOM 1870 O VAL B 7 52.641 25.008 28.062 1.00 47.87 O ANISOU 1870 O VAL B 7 5551 6871 5769 -2065 -376 -1535 O ATOM 1871 CB VAL B 7 55.734 24.839 29.248 1.00 49.67 C ANISOU 1871 CB VAL B 7 5388 7637 5847 -2334 -670 -1577 C ATOM 1872 CG1 VAL B 7 55.305 23.449 28.795 1.00 43.48 C ANISOU 1872 CG1 VAL B 7 4613 6916 4993 -2150 -705 -1313 C ATOM 1873 CG2 VAL B 7 57.167 25.132 28.828 1.00 52.27 C ANISOU 1873 CG2 VAL B 7 5564 7981 6315 -2415 -710 -1541 C ATOM 1874 N ALA B 8 52.899 25.672 30.201 1.00 51.86 N ANISOU 1874 N ALA B 8 6011 7690 6004 -2269 -468 -1862 N ATOM 1875 CA ALA B 8 51.534 25.345 30.591 1.00 50.07 C ANISOU 1875 CA ALA B 8 5911 7457 5658 -2181 -417 -1880 C ATOM 1876 C ALA B 8 50.530 26.089 29.718 1.00 48.37 C ANISOU 1876 C ALA B 8 5834 6881 5662 -2127 -242 -1928 C ATOM 1877 O ALA B 8 49.519 25.527 29.302 1.00 45.74 O ANISOU 1877 O ALA B 8 5590 6455 5332 -1956 -190 -1779 O ATOM 1878 CB ALA B 8 51.309 25.675 32.056 1.00 52.56 C ANISOU 1878 CB ALA B 8 6245 7954 5773 -2230 -434 -2044 C ATOM 1879 N GLN B 9 50.827 27.354 29.437 1.00 49.85 N ANISOU 1879 N GLN B 9 6039 6851 6052 -2212 -141 -2071 N ATOM 1880 CA GLN B 9 49.965 28.183 28.605 1.00 50.93 C ANISOU 1880 CA GLN B 9 6293 6637 6421 -2157 33 -2098 C ATOM 1881 C GLN B 9 49.924 27.689 27.162 1.00 48.38 C ANISOU 1881 C GLN B 9 5978 6154 6252 -2023 62 -1844 C ATOM 1882 O GLN B 9 48.865 27.664 26.527 1.00 45.88 O ANISOU 1882 O GLN B 9 5762 5656 6016 -1876 157 -1741 O ATOM 1883 CB GLN B 9 50.439 29.634 28.634 1.00 57.94 C ANISOU 1883 CB GLN B 9 7180 7339 7497 -2250 132 -2253 C ATOM 1884 CG GLN B 9 49.396 30.616 28.154 1.00 61.39 C ANISOU 1884 CG GLN B 9 7738 7448 8140 -2180 321 -2300 C ATOM 1885 CD GLN B 9 48.272 30.780 29.153 1.00 64.38 C ANISOU 1885 CD GLN B 9 8203 7865 8393 -2145 377 -2441 C ATOM 1886 OE1 GLN B 9 48.507 30.837 30.361 1.00 68.13 O ANISOU 1886 OE1 GLN B 9 8650 8550 8686 -2229 319 -2593 O ATOM 1887 NE2 GLN B 9 47.043 30.849 28.657 1.00 64.04 N ANISOU 1887 NE2 GLN B 9 8260 7627 8446 -2018 494 -2383 N ATOM 1888 N ARG B 10 51.089 27.307 26.649 1.00 47.43 N ANISOU 1888 N ARG B 10 5745 6112 6166 -2051 -18 -1721 N ATOM 1889 CA ARG B 10 51.215 26.847 25.272 1.00 45.11 C ANISOU 1889 CA ARG B 10 5451 5688 6003 -1912 12 -1468 C ATOM 1890 C ARG B 10 50.512 25.504 25.070 1.00 41.69 C ANISOU 1890 C ARG B 10 5055 5355 5430 -1723 -41 -1259 C ATOM 1891 O ARG B 10 49.745 25.328 24.124 1.00 40.11 O ANISOU 1891 O ARG B 10 4935 4991 5315 -1581 33 -1121 O ATOM 1892 CB ARG B 10 52.692 26.737 24.889 1.00 44.08 C ANISOU 1892 CB ARG B 10 5176 5640 5933 -1997 -56 -1404 C ATOM 1893 CG ARG B 10 52.939 26.458 23.418 1.00 41.53 C ANISOU 1893 CG ARG B 10 4852 5168 5762 -1878 1 -1175 C ATOM 1894 CD ARG B 10 54.425 26.292 23.131 1.00 41.89 C ANISOU 1894 CD ARG B 10 4741 5318 5858 -1959 -61 -1113 C ATOM 1895 NE ARG B 10 54.690 26.123 21.704 1.00 41.91 N ANISOU 1895 NE ARG B 10 4745 5174 6006 -1855 15 -911 N ATOM 1896 CZ ARG B 10 55.858 25.738 21.198 1.00 42.61 C ANISOU 1896 CZ ARG B 10 4706 5341 6141 -1869 -19 -796 C ATOM 1897 NH1 ARG B 10 56.881 25.473 22.000 1.00 39.34 N ANISOU 1897 NH1 ARG B 10 4143 5154 5651 -1980 -139 -851 N ATOM 1898 NH2 ARG B 10 56.002 25.611 19.886 1.00 45.49 N ANISOU 1898 NH2 ARG B 10 5088 5573 6622 -1769 68 -622 N ATOM 1899 N ALA B 11 50.784 24.565 25.969 1.00 41.25 N ANISOU 1899 N ALA B 11 4934 5575 5162 -1726 -170 -1235 N ATOM 1900 CA ALA B 11 50.219 23.225 25.898 1.00 39.11 C ANISOU 1900 CA ALA B 11 4685 5408 4766 -1562 -220 -1040 C ATOM 1901 C ALA B 11 48.698 23.254 26.023 1.00 39.18 C ANISOU 1901 C ALA B 11 4827 5312 4748 -1468 -140 -1063 C ATOM 1902 O ALA B 11 47.997 22.496 25.353 1.00 35.55 O ANISOU 1902 O ALA B 11 4417 4789 4301 -1319 -119 -898 O ATOM 1903 CB ALA B 11 50.822 22.345 26.981 1.00 38.91 C ANISOU 1903 CB ALA B 11 4557 5700 4527 -1595 -364 -1012 C ATOM 1904 N LEU B 12 48.199 24.134 26.888 1.00 42.46 N ANISOU 1904 N LEU B 12 5292 5713 5129 -1560 -92 -1279 N ATOM 1905 CA LEU B 12 46.764 24.287 27.101 1.00 42.06 C ANISOU 1905 CA LEU B 12 5354 5563 5063 -1479 -2 -1322 C ATOM 1906 C LEU B 12 46.067 24.663 25.796 1.00 38.52 C ANISOU 1906 C LEU B 12 4979 4835 4823 -1367 111 -1219 C ATOM 1907 O LEU B 12 45.027 24.102 25.455 1.00 39.00 O ANISOU 1907 O LEU B 12 5096 4852 4869 -1231 139 -1104 O ATOM 1908 CB LEU B 12 46.491 25.345 28.183 1.00 46.24 C ANISOU 1908 CB LEU B 12 5919 6097 5552 -1612 55 -1601 C ATOM 1909 CG LEU B 12 45.071 25.473 28.746 1.00 47.75 C ANISOU 1909 CG LEU B 12 6209 6247 5686 -1546 145 -1677 C ATOM 1910 CD1 LEU B 12 45.116 25.945 30.189 1.00 49.23 C ANISOU 1910 CD1 LEU B 12 6397 6605 5704 -1687 139 -1934 C ATOM 1911 CD2 LEU B 12 44.216 26.420 27.911 1.00 48.81 C ANISOU 1911 CD2 LEU B 12 6428 6060 6059 -1481 304 -1698 C ATOM 1912 N SER B 13 46.659 25.601 25.059 1.00 38.10 N ANISOU 1912 N SER B 13 4914 4604 4960 -1427 174 -1253 N ATOM 1913 CA SER B 13 46.072 26.088 23.815 1.00 37.78 C ANISOU 1913 CA SER B 13 4933 4308 5114 -1327 285 -1146 C ATOM 1914 C SER B 13 46.147 25.045 22.694 1.00 35.09 C ANISOU 1914 C SER B 13 4577 3990 4767 -1194 238 -898 C ATOM 1915 O SER B 13 45.519 25.200 21.644 1.00 34.24 O ANISOU 1915 O SER B 13 4517 3724 4767 -1089 308 -780 O ATOM 1916 CB SER B 13 46.758 27.384 23.374 1.00 40.75 C ANISOU 1916 CB SER B 13 5294 4489 5699 -1434 375 -1236 C ATOM 1917 OG SER B 13 48.024 27.125 22.789 1.00 44.85 O ANISOU 1917 OG SER B 13 5726 5062 6254 -1481 315 -1143 O ATOM 1918 N LEU B 14 46.907 23.981 22.921 1.00 35.49 N ANISOU 1918 N LEU B 14 4556 4241 4688 -1198 123 -821 N ATOM 1919 CA LEU B 14 47.049 22.930 21.922 1.00 33.03 C ANISOU 1919 CA LEU B 14 4228 3951 4371 -1081 88 -612 C ATOM 1920 C LEU B 14 46.326 21.653 22.339 1.00 34.25 C ANISOU 1920 C LEU B 14 4400 4241 4373 -984 27 -528 C ATOM 1921 O LEU B 14 46.465 20.618 21.694 1.00 32.17 O ANISOU 1921 O LEU B 14 4117 4016 4088 -897 -7 -376 O ATOM 1922 CB LEU B 14 48.529 22.630 21.669 1.00 28.87 C ANISOU 1922 CB LEU B 14 3595 3516 3858 -1140 26 -557 C ATOM 1923 CG LEU B 14 49.420 23.800 21.238 1.00 31.53 C ANISOU 1923 CG LEU B 14 3893 3731 4357 -1251 85 -625 C ATOM 1924 CD1 LEU B 14 50.880 23.361 21.128 1.00 30.21 C ANISOU 1924 CD1 LEU B 14 3598 3692 4186 -1309 13 -566 C ATOM 1925 CD2 LEU B 14 48.934 24.403 19.923 1.00 30.65 C ANISOU 1925 CD2 LEU B 14 3850 3391 4404 -1175 201 -534 C ATOM 1926 N MET B 15 45.553 21.718 23.417 1.00 36.51 N ANISOU 1926 N MET B 15 4720 4594 4558 -1001 25 -631 N ATOM 1927 CA MET B 15 44.895 20.517 23.930 1.00 37.21 C ANISOU 1927 CA MET B 15 4816 4816 4505 -921 -25 -548 C ATOM 1928 C MET B 15 43.647 20.106 23.155 1.00 34.67 C ANISOU 1928 C MET B 15 4563 4379 4230 -793 28 -448 C ATOM 1929 O MET B 15 42.848 20.946 22.751 1.00 33.10 O ANISOU 1929 O MET B 15 4422 4028 4128 -770 111 -493 O ATOM 1930 CB MET B 15 44.515 20.700 25.399 1.00 39.71 C ANISOU 1930 CB MET B 15 5141 5269 4678 -986 -40 -687 C ATOM 1931 CG MET B 15 45.601 20.313 26.383 1.00 44.00 C ANISOU 1931 CG MET B 15 5594 6049 5077 -1076 -146 -713 C ATOM 1932 SD MET B 15 44.931 20.127 28.049 1.00 52.05 S ANISOU 1932 SD MET B 15 6629 7279 5869 -1114 -168 -818 S ATOM 1933 CE MET B 15 43.778 18.776 27.781 1.00 30.43 C ANISOU 1933 CE MET B 15 3932 4532 3099 -947 -152 -615 C ATOM 1934 N ASP B 16 43.516 18.797 22.941 1.00 34.15 N ANISOU 1934 N ASP B 16 4482 4391 4105 -712 -19 -308 N ATOM 1935 CA ASP B 16 42.244 18.159 22.611 1.00 32.00 C ANISOU 1935 CA ASP B 16 4257 4073 3828 -612 10 -234 C ATOM 1936 C ASP B 16 41.670 17.611 23.911 1.00 32.30 C ANISOU 1936 C ASP B 16 4294 4249 3731 -616 -11 -259 C ATOM 1937 O ASP B 16 41.990 16.483 24.306 1.00 31.66 O ANISOU 1937 O ASP B 16 4171 4292 3566 -594 -67 -164 O ATOM 1938 CB ASP B 16 42.420 17.023 21.593 1.00 31.81 C ANISOU 1938 CB ASP B 16 4218 4037 3832 -534 -15 -84 C ATOM 1939 CG ASP B 16 42.673 17.524 20.177 1.00 32.54 C ANISOU 1939 CG ASP B 16 4327 3997 4041 -510 23 -47 C ATOM 1940 OD1 ASP B 16 42.798 18.753 19.978 1.00 33.50 O ANISOU 1940 OD1 ASP B 16 4465 4027 4238 -552 68 -116 O ATOM 1941 OD2 ASP B 16 42.753 16.679 19.258 1.00 31.74 O ANISOU 1941 OD2 ASP B 16 4222 3882 3956 -450 16 53 O ATOM 1942 N LEU B 17 40.858 18.414 24.595 1.00 31.42 N ANISOU 1942 N LEU B 17 4222 4115 3599 -642 45 -381 N ATOM 1943 CA LEU B 17 40.299 18.010 25.881 1.00 29.40 C ANISOU 1943 CA LEU B 17 3967 4003 3199 -652 40 -416 C ATOM 1944 C LEU B 17 39.360 16.826 25.672 1.00 29.86 C ANISOU 1944 C LEU B 17 4032 4069 3244 -555 44 -277 C ATOM 1945 O LEU B 17 38.330 16.950 25.011 1.00 25.48 O ANISOU 1945 O LEU B 17 3511 3393 2779 -494 99 -258 O ATOM 1946 CB LEU B 17 39.570 19.175 26.549 1.00 30.64 C ANISOU 1946 CB LEU B 17 4172 4114 3357 -694 124 -590 C ATOM 1947 CG LEU B 17 38.934 18.868 27.905 1.00 31.20 C ANISOU 1947 CG LEU B 17 4249 4341 3263 -707 138 -643 C ATOM 1948 CD1 LEU B 17 39.993 18.410 28.901 1.00 32.66 C ANISOU 1948 CD1 LEU B 17 4379 4757 3272 -784 46 -648 C ATOM 1949 CD2 LEU B 17 38.167 20.077 28.430 1.00 29.79 C ANISOU 1949 CD2 LEU B 17 4121 4085 3111 -740 246 -829 C ATOM 1950 N THR B 18 39.720 15.678 26.242 1.00 30.07 N ANISOU 1950 N THR B 18 4017 4241 3169 -544 -13 -174 N ATOM 1951 CA THR B 18 39.127 14.409 25.827 1.00 26.89 C ANISOU 1951 CA THR B 18 3608 3817 2793 -461 -11 -25 C ATOM 1952 C THR B 18 38.298 13.711 26.913 1.00 29.30 C ANISOU 1952 C THR B 18 3908 4234 2989 -441 10 19 C ATOM 1953 O THR B 18 38.716 13.609 28.069 1.00 29.86 O ANISOU 1953 O THR B 18 3954 4475 2918 -481 -18 12 O ATOM 1954 CB THR B 18 40.237 13.439 25.346 1.00 26.36 C ANISOU 1954 CB THR B 18 3489 3780 2748 -440 -72 102 C ATOM 1955 OG1 THR B 18 40.994 14.056 24.296 1.00 27.52 O ANISOU 1955 OG1 THR B 18 3637 3827 2994 -456 -81 70 O ATOM 1956 CG2 THR B 18 39.642 12.144 24.834 1.00 23.96 C ANISOU 1956 CG2 THR B 18 3183 3422 2499 -364 -55 232 C ATOM 1957 N SER B 19 37.113 13.242 26.531 1.00 28.01 N ANISOU 1957 N SER B 19 3766 3988 2890 -383 61 67 N ATOM 1958 CA SER B 19 36.327 12.348 27.374 1.00 26.87 C ANISOU 1958 CA SER B 19 3607 3928 2674 -357 91 147 C ATOM 1959 C SER B 19 35.752 11.224 26.523 1.00 27.40 C ANISOU 1959 C SER B 19 3662 3894 2853 -298 104 267 C ATOM 1960 O SER B 19 34.917 11.463 25.652 1.00 24.86 O ANISOU 1960 O SER B 19 3359 3452 2635 -275 134 235 O ATOM 1961 CB SER B 19 35.203 13.099 28.088 1.00 28.10 C ANISOU 1961 CB SER B 19 3792 4101 2783 -366 166 43 C ATOM 1962 OG SER B 19 34.432 12.208 28.873 1.00 28.23 O ANISOU 1962 OG SER B 19 3789 4202 2734 -340 205 134 O ATOM 1963 N LEU B 20 36.207 10.001 26.782 1.00 27.68 N ANISOU 1963 N LEU B 20 3661 3983 2872 -277 82 404 N ATOM 1964 CA LEU B 20 35.786 8.840 26.008 1.00 25.75 C ANISOU 1964 CA LEU B 20 3404 3632 2747 -234 103 504 C ATOM 1965 C LEU B 20 35.460 7.657 26.915 1.00 24.52 C ANISOU 1965 C LEU B 20 3214 3545 2557 -212 137 644 C ATOM 1966 O LEU B 20 36.017 6.574 26.748 1.00 25.75 O ANISOU 1966 O LEU B 20 3340 3675 2770 -183 132 766 O ATOM 1967 CB LEU B 20 36.877 8.442 25.000 1.00 24.00 C ANISOU 1967 CB LEU B 20 3172 3340 2607 -220 61 540 C ATOM 1968 CG LEU B 20 37.247 9.458 23.910 1.00 24.73 C ANISOU 1968 CG LEU B 20 3294 3351 2750 -236 37 434 C ATOM 1969 CD1 LEU B 20 38.512 9.029 23.167 1.00 23.20 C ANISOU 1969 CD1 LEU B 20 3079 3127 2609 -223 5 481 C ATOM 1970 CD2 LEU B 20 36.092 9.664 22.928 1.00 23.47 C ANISOU 1970 CD2 LEU B 20 3163 3077 2676 -222 69 382 C ATOM 1971 N THR B 21 34.567 7.864 27.880 1.00 23.46 N ANISOU 1971 N THR B 21 3083 3492 2339 -222 184 633 N ATOM 1972 CA THR B 21 34.141 6.775 28.750 1.00 25.36 C ANISOU 1972 CA THR B 21 3289 3796 2549 -200 233 781 C ATOM 1973 C THR B 21 33.081 5.914 28.071 1.00 27.87 C ANISOU 1973 C THR B 21 3598 3967 3026 -184 292 826 C ATOM 1974 O THR B 21 32.894 4.753 28.444 1.00 25.10 O ANISOU 1974 O THR B 21 3213 3606 2717 -164 337 971 O ATOM 1975 CB THR B 21 33.571 7.288 30.084 1.00 27.33 C ANISOU 1975 CB THR B 21 3543 4207 2633 -219 274 755 C ATOM 1976 OG1 THR B 21 32.269 7.855 29.873 1.00 26.88 O ANISOU 1976 OG1 THR B 21 3506 4078 2628 -225 338 653 O ATOM 1977 CG2 THR B 21 34.496 8.321 30.704 1.00 27.05 C ANISOU 1977 CG2 THR B 21 3521 4318 2438 -259 216 654 C ATOM 1978 N ASN B 22 32.393 6.508 27.093 1.00 27.13 N ANISOU 1978 N ASN B 22 3525 3764 3020 -195 293 706 N ATOM 1979 CA ASN B 22 31.275 5.892 26.365 1.00 29.05 C ANISOU 1979 CA ASN B 22 3748 3886 3403 -197 335 712 C ATOM 1980 C ASN B 22 30.007 5.759 27.218 1.00 30.50 C ANISOU 1980 C ASN B 22 3903 4117 3568 -202 415 742 C ATOM 1981 O ASN B 22 29.044 5.102 26.814 1.00 28.74 O ANISOU 1981 O ASN B 22 3646 3812 3463 -213 456 766 O ATOM 1982 CB ASN B 22 31.672 4.518 25.799 1.00 29.04 C ANISOU 1982 CB ASN B 22 3727 3785 3523 -189 342 810 C ATOM 1983 CG ASN B 22 30.835 4.114 24.596 1.00 32.55 C ANISOU 1983 CG ASN B 22 4161 4094 4114 -212 353 750 C ATOM 1984 OD1 ASN B 22 30.268 4.964 23.910 1.00 31.47 O ANISOU 1984 OD1 ASN B 22 4032 3942 3982 -223 325 641 O ATOM 1985 ND2 ASN B 22 30.756 2.808 24.335 1.00 34.14 N ANISOU 1985 ND2 ASN B 22 4337 4198 4437 -221 395 823 N ATOM 1986 N THR B 23 29.998 6.389 28.391 1.00 31.53 N ANISOU 1986 N THR B 23 4044 4386 3551 -200 439 732 N ATOM 1987 CA THR B 23 28.785 6.440 29.209 1.00 30.72 C ANISOU 1987 CA THR B 23 3916 4340 3417 -202 528 744 C ATOM 1988 C THR B 23 28.419 7.873 29.566 1.00 29.06 C ANISOU 1988 C THR B 23 3734 4190 3119 -203 547 596 C ATOM 1989 O THR B 23 27.658 8.110 30.503 1.00 30.62 O ANISOU 1989 O THR B 23 3919 4474 3242 -201 628 589 O ATOM 1990 CB THR B 23 28.918 5.637 30.520 1.00 30.43 C ANISOU 1990 CB THR B 23 3858 4432 3271 -195 581 895 C ATOM 1991 OG1 THR B 23 30.065 6.093 31.247 1.00 32.66 O ANISOU 1991 OG1 THR B 23 4168 4862 3379 -195 528 891 O ATOM 1992 CG2 THR B 23 29.046 4.144 30.237 1.00 30.11 C ANISOU 1992 CG2 THR B 23 3782 4301 3360 -186 599 1059 C ATOM 1993 N GLU B 24 28.963 8.824 28.819 1.00 26.98 N ANISOU 1993 N GLU B 24 3505 3871 2874 -206 486 481 N ATOM 1994 CA GLU B 24 28.735 10.235 29.106 1.00 28.79 C ANISOU 1994 CA GLU B 24 3765 4126 3049 -207 514 334 C ATOM 1995 C GLU B 24 27.251 10.597 29.023 1.00 32.42 C ANISOU 1995 C GLU B 24 4190 4538 3591 -182 597 297 C ATOM 1996 O GLU B 24 26.515 10.058 28.192 1.00 31.48 O ANISOU 1996 O GLU B 24 4025 4331 3606 -169 593 347 O ATOM 1997 CB GLU B 24 29.551 11.114 28.151 1.00 25.04 C ANISOU 1997 CB GLU B 24 3326 3567 2620 -212 443 241 C ATOM 1998 CG GLU B 24 31.054 11.165 28.465 1.00 26.80 C ANISOU 1998 CG GLU B 24 3576 3865 2741 -244 373 238 C ATOM 1999 CD GLU B 24 31.877 10.124 27.712 1.00 30.20 C ANISOU 1999 CD GLU B 24 3991 4250 3233 -237 303 349 C ATOM 2000 OE1 GLU B 24 31.285 9.289 26.993 1.00 29.01 O ANISOU 2000 OE1 GLU B 24 3816 4009 3196 -217 313 418 O ATOM 2001 OE2 GLU B 24 33.127 10.149 27.834 1.00 28.11 O ANISOU 2001 OE2 GLU B 24 3733 4040 2908 -255 243 359 O ATOM 2002 N THR B 25 26.817 11.478 29.922 1.00 33.14 N ANISOU 2002 N THR B 25 4295 4698 3599 -178 677 206 N ATOM 2003 CA THR B 25 25.504 12.104 29.832 1.00 34.78 C ANISOU 2003 CA THR B 25 4467 4853 3896 -142 765 150 C ATOM 2004 C THR B 25 25.638 13.405 29.059 1.00 35.87 C ANISOU 2004 C THR B 25 4632 4883 4115 -120 749 31 C ATOM 2005 O THR B 25 26.746 13.916 28.888 1.00 36.58 O ANISOU 2005 O THR B 25 4776 4961 4162 -145 690 -30 O ATOM 2006 CB THR B 25 24.898 12.410 31.222 1.00 37.54 C ANISOU 2006 CB THR B 25 4817 5324 4124 -141 887 106 C ATOM 2007 OG1 THR B 25 25.604 13.501 31.827 1.00 38.89 O ANISOU 2007 OG1 THR B 25 5055 5546 4178 -163 901 -44 O ATOM 2008 CG2 THR B 25 24.967 11.191 32.132 1.00 37.13 C ANISOU 2008 CG2 THR B 25 4747 5402 3959 -163 906 242 C ATOM 2009 N ASP B 26 24.514 13.950 28.604 1.00 34.98 N ANISOU 2009 N ASP B 26 4471 4694 4128 -71 807 10 N ATOM 2010 CA ASP B 26 24.523 15.236 27.918 1.00 30.35 C ANISOU 2010 CA ASP B 26 3901 3996 3636 -35 814 -78 C ATOM 2011 C ASP B 26 25.088 16.330 28.822 1.00 29.95 C ANISOU 2011 C ASP B 26 3919 3963 3496 -55 880 -228 C ATOM 2012 O ASP B 26 25.819 17.206 28.366 1.00 30.93 O ANISOU 2012 O ASP B 26 4089 4006 3658 -63 853 -303 O ATOM 2013 CB ASP B 26 23.117 15.613 27.450 1.00 30.62 C ANISOU 2013 CB ASP B 26 3852 3965 3816 35 878 -54 C ATOM 2014 CG ASP B 26 22.656 14.791 26.265 1.00 37.39 C ANISOU 2014 CG ASP B 26 4637 4794 4775 44 790 62 C ATOM 2015 OD1 ASP B 26 23.488 14.065 25.675 1.00 41.09 O ANISOU 2015 OD1 ASP B 26 5135 5263 5216 2 686 107 O ATOM 2016 OD2 ASP B 26 21.461 14.879 25.911 1.00 43.00 O ANISOU 2016 OD2 ASP B 26 5257 5487 5595 90 825 102 O ATOM 2017 N GLN B 27 24.749 16.270 30.104 1.00 30.68 N ANISOU 2017 N GLN B 27 4020 4168 3471 -71 972 -278 N ATOM 2018 CA GLN B 27 25.258 17.232 31.071 1.00 33.09 C ANISOU 2018 CA GLN B 27 4390 4517 3664 -109 1040 -447 C ATOM 2019 C GLN B 27 26.781 17.131 31.187 1.00 35.57 C ANISOU 2019 C GLN B 27 4763 4895 3858 -185 931 -477 C ATOM 2020 O GLN B 27 27.465 18.149 31.301 1.00 35.79 O ANISOU 2020 O GLN B 27 4841 4882 3874 -223 941 -623 O ATOM 2021 CB GLN B 27 24.602 17.024 32.438 1.00 35.56 C ANISOU 2021 CB GLN B 27 4698 4976 3839 -116 1157 -483 C ATOM 2022 CG GLN B 27 25.127 17.946 33.531 1.00 40.81 C ANISOU 2022 CG GLN B 27 5433 5720 4353 -171 1229 -682 C ATOM 2023 CD GLN B 27 24.928 19.415 33.207 1.00 46.46 C ANISOU 2023 CD GLN B 27 6175 6264 5213 -145 1319 -850 C ATOM 2024 OE1 GLN B 27 23.919 19.804 32.616 1.00 49.62 O ANISOU 2024 OE1 GLN B 27 6526 6527 5799 -61 1393 -820 O ATOM 2025 NE2 GLN B 27 25.897 20.242 33.589 1.00 46.81 N ANISOU 2025 NE2 GLN B 27 6289 6312 5183 -218 1314 -1024 N ATOM 2026 N GLU B 28 27.310 15.910 31.139 1.00 32.02 N ANISOU 2026 N GLU B 28 4297 4534 3335 -208 834 -338 N ATOM 2027 CA GLU B 28 28.755 15.713 31.207 1.00 32.10 C ANISOU 2027 CA GLU B 28 4341 4614 3243 -269 726 -339 C ATOM 2028 C GLU B 28 29.452 16.251 29.957 1.00 29.37 C ANISOU 2028 C GLU B 28 4011 4117 3033 -268 652 -358 C ATOM 2029 O GLU B 28 30.566 16.761 30.037 1.00 26.60 O ANISOU 2029 O GLU B 28 3692 3783 2631 -324 603 -438 O ATOM 2030 CB GLU B 28 29.091 14.235 31.406 1.00 35.18 C ANISOU 2030 CB GLU B 28 4700 5113 3554 -274 657 -163 C ATOM 2031 CG GLU B 28 28.757 13.719 32.795 1.00 42.70 C ANISOU 2031 CG GLU B 28 5643 6254 4328 -288 719 -128 C ATOM 2032 CD GLU B 28 28.883 12.207 32.915 1.00 46.84 C ANISOU 2032 CD GLU B 28 6125 6848 4822 -275 677 82 C ATOM 2033 OE1 GLU B 28 29.312 11.556 31.940 1.00 46.14 O ANISOU 2033 OE1 GLU B 28 6020 6661 4849 -262 598 178 O ATOM 2034 OE2 GLU B 28 28.549 11.669 33.991 1.00 51.53 O ANISOU 2034 OE2 GLU B 28 6705 7595 5281 -278 734 151 O ATOM 2035 N ILE B 29 28.795 16.138 28.805 1.00 29.77 N ANISOU 2035 N ILE B 29 4030 4033 3248 -209 645 -282 N ATOM 2036 CA ILE B 29 29.321 16.721 27.574 1.00 28.60 C ANISOU 2036 CA ILE B 29 3894 3748 3224 -198 591 -289 C ATOM 2037 C ILE B 29 29.324 18.248 27.670 1.00 30.23 C ANISOU 2037 C ILE B 29 4136 3858 3493 -200 669 -439 C ATOM 2038 O ILE B 29 30.303 18.903 27.304 1.00 27.20 O ANISOU 2038 O ILE B 29 3784 3416 3135 -238 635 -498 O ATOM 2039 CB ILE B 29 28.505 16.289 26.338 1.00 26.08 C ANISOU 2039 CB ILE B 29 3528 3338 3046 -135 566 -175 C ATOM 2040 CG1 ILE B 29 28.570 14.773 26.157 1.00 24.89 C ANISOU 2040 CG1 ILE B 29 3346 3251 2860 -145 499 -47 C ATOM 2041 CG2 ILE B 29 29.005 16.996 25.085 1.00 22.32 C ANISOU 2041 CG2 ILE B 29 3065 2739 2678 -118 523 -175 C ATOM 2042 CD1 ILE B 29 29.970 14.236 25.987 1.00 27.83 C ANISOU 2042 CD1 ILE B 29 3745 3658 3170 -188 410 -14 C ATOM 2043 N ILE B 30 28.225 18.806 28.167 1.00 29.00 N ANISOU 2043 N ILE B 30 3968 3675 3376 -160 785 -501 N ATOM 2044 CA ILE B 30 28.121 20.246 28.345 1.00 31.25 C ANISOU 2044 CA ILE B 30 4285 3846 3743 -155 889 -652 C ATOM 2045 C ILE B 30 29.191 20.720 29.331 1.00 33.65 C ANISOU 2045 C ILE B 30 4647 4228 3909 -258 892 -816 C ATOM 2046 O ILE B 30 29.847 21.741 29.099 1.00 31.75 O ANISOU 2046 O ILE B 30 4443 3881 3742 -295 911 -926 O ATOM 2047 CB ILE B 30 26.708 20.658 28.828 1.00 30.95 C ANISOU 2047 CB ILE B 30 4215 3777 3767 -86 1031 -690 C ATOM 2048 CG1 ILE B 30 25.668 20.346 27.748 1.00 30.51 C ANISOU 2048 CG1 ILE B 30 4083 3645 3865 10 1017 -532 C ATOM 2049 CG2 ILE B 30 26.652 22.141 29.153 1.00 33.47 C ANISOU 2049 CG2 ILE B 30 4573 3967 4177 -84 1162 -866 C ATOM 2050 CD1 ILE B 30 24.229 20.533 28.203 1.00 32.38 C ANISOU 2050 CD1 ILE B 30 4260 3876 4166 83 1146 -535 C ATOM 2051 N ASP B 31 29.383 19.960 30.409 1.00 34.00 N ANISOU 2051 N ASP B 31 4695 4467 3755 -307 871 -824 N ATOM 2052 CA ASP B 31 30.413 20.273 31.400 1.00 36.99 C ANISOU 2052 CA ASP B 31 5114 4975 3964 -413 851 -970 C ATOM 2053 C ASP B 31 31.810 20.247 30.788 1.00 35.80 C ANISOU 2053 C ASP B 31 4968 4813 3822 -473 725 -947 C ATOM 2054 O ASP B 31 32.685 21.016 31.183 1.00 37.84 O ANISOU 2054 O ASP B 31 5253 5087 4036 -562 720 -1102 O ATOM 2055 CB ASP B 31 30.359 19.294 32.579 1.00 42.04 C ANISOU 2055 CB ASP B 31 5741 5857 4374 -441 835 -927 C ATOM 2056 CG ASP B 31 29.145 19.511 33.469 1.00 50.90 C ANISOU 2056 CG ASP B 31 6866 7024 5449 -408 982 -999 C ATOM 2057 OD1 ASP B 31 28.660 20.659 33.548 1.00 54.79 O ANISOU 2057 OD1 ASP B 31 7386 7394 6037 -398 1103 -1161 O ATOM 2058 OD2 ASP B 31 28.677 18.532 34.093 1.00 53.33 O ANISOU 2058 OD2 ASP B 31 7146 7483 5633 -390 988 -887 O ATOM 2059 N LEU B 32 32.023 19.347 29.834 1.00 33.81 N ANISOU 2059 N LEU B 32 4683 4536 3626 -429 629 -763 N ATOM 2060 CA LEU B 32 33.323 19.238 29.185 1.00 31.26 C ANISOU 2060 CA LEU B 32 4357 4202 3320 -473 520 -724 C ATOM 2061 C LEU B 32 33.597 20.477 28.337 1.00 30.81 C ANISOU 2061 C LEU B 32 4322 3948 3435 -480 558 -808 C ATOM 2062 O LEU B 32 34.717 20.984 28.316 1.00 31.46 O ANISOU 2062 O LEU B 32 4413 4027 3514 -558 518 -885 O ATOM 2063 CB LEU B 32 33.400 17.976 28.325 1.00 25.13 C ANISOU 2063 CB LEU B 32 3543 3430 2575 -418 432 -520 C ATOM 2064 CG LEU B 32 34.786 17.650 27.763 1.00 25.63 C ANISOU 2064 CG LEU B 32 3592 3510 2635 -457 326 -464 C ATOM 2065 CD1 LEU B 32 35.729 17.170 28.867 1.00 25.20 C ANISOU 2065 CD1 LEU B 32 3517 3661 2396 -527 262 -474 C ATOM 2066 CD2 LEU B 32 34.688 16.624 26.640 1.00 24.88 C ANISOU 2066 CD2 LEU B 32 3472 3358 2622 -392 273 -294 C ATOM 2067 N CYS B 33 32.567 20.957 27.643 1.00 30.49 N ANISOU 2067 N CYS B 33 4283 3750 3553 -396 636 -780 N ATOM 2068 CA CYS B 33 32.675 22.169 26.837 1.00 27.79 C ANISOU 2068 CA CYS B 33 3959 3208 3393 -383 693 -829 C ATOM 2069 C CYS B 33 32.957 23.375 27.724 1.00 31.78 C ANISOU 2069 C CYS B 33 4503 3669 3902 -462 789 -1053 C ATOM 2070 O CYS B 33 33.771 24.239 27.383 1.00 33.67 O ANISOU 2070 O CYS B 33 4761 3798 4234 -519 800 -1130 O ATOM 2071 CB CYS B 33 31.399 22.397 26.026 1.00 25.87 C ANISOU 2071 CB CYS B 33 3691 2832 3305 -264 759 -733 C ATOM 2072 SG CYS B 33 31.070 21.113 24.794 1.00 33.08 S ANISOU 2072 SG CYS B 33 4556 3784 4231 -190 647 -502 S ATOM 2073 N ARG B 34 32.283 23.421 28.868 1.00 32.85 N ANISOU 2073 N ARG B 34 4651 3891 3938 -472 867 -1164 N ATOM 2074 CA ARG B 34 32.476 24.498 29.827 1.00 36.89 C ANISOU 2074 CA ARG B 34 5206 4381 4429 -557 970 -1409 C ATOM 2075 C ARG B 34 33.907 24.488 30.354 1.00 39.41 C ANISOU 2075 C ARG B 34 5533 4834 4608 -699 874 -1515 C ATOM 2076 O ARG B 34 34.473 25.539 30.640 1.00 39.11 O ANISOU 2076 O ARG B 34 5523 4718 4620 -793 929 -1709 O ATOM 2077 CB ARG B 34 31.478 24.380 30.981 1.00 34.71 C ANISOU 2077 CB ARG B 34 4940 4214 4036 -538 1069 -1499 C ATOM 2078 N GLN B 35 34.494 23.299 30.465 1.00 41.44 N ANISOU 2078 N GLN B 35 5756 5287 4704 -715 734 -1383 N ATOM 2079 CA GLN B 35 35.870 23.181 30.942 1.00 44.43 C ANISOU 2079 CA GLN B 35 6118 5821 4944 -839 627 -1449 C ATOM 2080 C GLN B 35 36.876 23.563 29.858 1.00 40.87 C ANISOU 2080 C GLN B 35 5649 5232 4647 -868 570 -1407 C ATOM 2081 O GLN B 35 37.965 24.058 30.161 1.00 43.54 O ANISOU 2081 O GLN B 35 5976 5615 4953 -989 530 -1532 O ATOM 2082 CB GLN B 35 36.149 21.764 31.444 1.00 48.10 C ANISOU 2082 CB GLN B 35 6540 6535 5200 -830 508 -1297 C ATOM 2083 CG GLN B 35 35.491 21.446 32.780 1.00 55.21 C ANISOU 2083 CG GLN B 35 7452 7632 5895 -841 554 -1361 C ATOM 2084 CD GLN B 35 35.662 19.993 33.187 1.00 62.55 C ANISOU 2084 CD GLN B 35 8336 8783 6649 -810 453 -1164 C ATOM 2085 OE1 GLN B 35 36.480 19.266 32.618 1.00 62.54 O ANISOU 2085 OE1 GLN B 35 8292 8809 6663 -800 339 -1011 O ATOM 2086 NE2 GLN B 35 34.883 19.559 34.176 1.00 66.80 N ANISOU 2086 NE2 GLN B 35 8879 9472 7029 -790 507 -1158 N ATOM 2087 N ALA B 36 36.507 23.344 28.599 1.00 34.42 N ANISOU 2087 N ALA B 36 4827 4262 3991 -763 569 -1233 N ATOM 2088 CA ALA B 36 37.363 23.720 27.478 1.00 32.57 C ANISOU 2088 CA ALA B 36 4578 3892 3904 -776 534 -1174 C ATOM 2089 C ALA B 36 37.551 25.237 27.436 1.00 37.37 C ANISOU 2089 C ALA B 36 5217 4308 4672 -841 645 -1351 C ATOM 2090 O ALA B 36 38.602 25.732 27.023 1.00 39.13 O ANISOU 2090 O ALA B 36 5425 4470 4973 -918 620 -1383 O ATOM 2091 CB ALA B 36 36.784 23.210 26.168 1.00 29.78 C ANISOU 2091 CB ALA B 36 4216 3433 3667 -648 522 -963 C ATOM 2092 N LYS B 37 36.530 25.970 27.871 1.00 38.67 N ANISOU 2092 N LYS B 37 5421 4369 4902 -809 780 -1466 N ATOM 2093 CA LYS B 37 36.648 27.409 28.050 1.00 39.72 C ANISOU 2093 CA LYS B 37 5587 4313 5190 -877 910 -1666 C ATOM 2094 C LYS B 37 37.237 27.694 29.430 1.00 41.57 C ANISOU 2094 C LYS B 37 5833 4702 5259 -1035 908 -1922 C ATOM 2095 O LYS B 37 36.515 28.033 30.365 1.00 38.95 O ANISOU 2095 O LYS B 37 5537 4397 4867 -1045 1007 -2083 O ATOM 2096 CB LYS B 37 35.288 28.093 27.891 1.00 42.54 C ANISOU 2096 CB LYS B 37 5974 4478 5711 -763 1072 -1674 C ATOM 2097 N SER B 38 38.554 27.543 29.545 1.00 42.38 N ANISOU 2097 N SER B 38 5899 4923 5280 -1157 794 -1958 N ATOM 2098 CA SER B 38 39.241 27.635 30.830 1.00 46.24 C ANISOU 2098 CA SER B 38 6379 5626 5567 -1316 749 -2177 C ATOM 2099 C SER B 38 39.539 29.087 31.214 1.00 48.05 C ANISOU 2099 C SER B 38 6640 5693 5925 -1452 873 -2469 C ATOM 2100 O SER B 38 39.456 29.982 30.372 1.00 46.31 O ANISOU 2100 O SER B 38 6433 5191 5972 -1415 974 -2445 O ATOM 2101 CB SER B 38 40.540 26.820 30.788 1.00 45.74 C ANISOU 2101 CB SER B 38 6239 5773 5365 -1387 566 -2078 C ATOM 2102 OG SER B 38 41.566 27.528 30.116 1.00 47.63 O ANISOU 2102 OG SER B 38 6449 5876 5773 -1475 557 -2116 O ATOM 2103 N PRO B 39 39.877 29.326 32.493 1.00 52.32 N ANISOU 2103 N PRO B 39 7159 6433 6288 -1552 845 -2632 N ATOM 2104 CA PRO B 39 40.309 30.661 32.927 1.00 57.32 C ANISOU 2104 CA PRO B 39 7782 6956 7039 -1648 925 -2819 C ATOM 2105 C PRO B 39 41.616 31.110 32.272 1.00 58.65 C ANISOU 2105 C PRO B 39 7895 7047 7342 -1744 863 -2806 C ATOM 2106 O PRO B 39 41.970 32.286 32.357 1.00 60.86 O ANISOU 2106 O PRO B 39 8170 7178 7778 -1814 948 -2936 O ATOM 2107 CB PRO B 39 40.499 30.499 34.439 1.00 59.74 C ANISOU 2107 CB PRO B 39 8069 7560 7069 -1741 869 -2970 C ATOM 2108 CG PRO B 39 39.650 29.346 34.810 1.00 59.62 C ANISOU 2108 CG PRO B 39 8077 7730 6848 -1647 836 -2864 C ATOM 2109 CD PRO B 39 39.690 28.414 33.636 1.00 54.67 C ANISOU 2109 CD PRO B 39 7445 7056 6272 -1566 763 -2646 C ATOM 2110 N ALA B 40 42.324 30.184 31.634 1.00 56.86 N ANISOU 2110 N ALA B 40 7624 6921 7060 -1748 724 -2649 N ATOM 2111 CA ALA B 40 43.585 30.507 30.977 1.00 53.55 C ANISOU 2111 CA ALA B 40 7141 6444 6763 -1834 663 -2615 C ATOM 2112 C ALA B 40 43.447 30.489 29.455 1.00 50.38 C ANISOU 2112 C ALA B 40 6758 5788 6597 -1740 710 -2428 C ATOM 2113 O ALA B 40 44.444 30.524 28.735 1.00 50.32 O ANISOU 2113 O ALA B 40 6695 5741 6685 -1789 656 -2349 O ATOM 2114 CB ALA B 40 44.674 29.542 31.420 1.00 52.13 C ANISOU 2114 CB ALA B 40 6872 6584 6352 -1920 468 -2572 C ATOM 2115 N GLY B 41 42.209 30.431 28.972 1.00 46.31 N ANISOU 2115 N GLY B 41 6313 5109 6173 -1600 814 -2347 N ATOM 2116 CA GLY B 41 41.946 30.430 27.543 1.00 42.88 C ANISOU 2116 CA GLY B 41 5894 4448 5950 -1483 861 -2136 C ATOM 2117 C GLY B 41 41.269 29.161 27.058 1.00 41.20 C ANISOU 2117 C GLY B 41 5678 4356 5622 -1311 776 -1874 C ATOM 2118 O GLY B 41 41.084 28.212 27.819 1.00 41.01 O ANISOU 2118 O GLY B 41 5642 4572 5366 -1301 684 -1864 O ATOM 2119 N GLU B 42 40.904 29.141 25.781 1.00 40.38 N ANISOU 2119 N GLU B 42 5580 4086 5676 -1180 809 -1658 N ATOM 2120 CA GLU B 42 40.237 27.986 25.186 1.00 37.90 C ANISOU 2120 CA GLU B 42 5261 3863 5276 -1026 736 -1422 C ATOM 2121 C GLU B 42 41.228 26.917 24.742 1.00 36.56 C ANISOU 2121 C GLU B 42 5034 3862 4995 -1037 584 -1273 C ATOM 2122 O GLU B 42 42.302 27.234 24.236 1.00 39.12 O ANISOU 2122 O GLU B 42 5322 4143 5399 -1108 563 -1260 O ATOM 2123 CB GLU B 42 39.394 28.422 23.989 1.00 42.88 C ANISOU 2123 CB GLU B 42 5914 4271 6106 -884 830 -1260 C ATOM 2124 CG GLU B 42 38.333 29.461 24.319 1.00 51.94 C ANISOU 2124 CG GLU B 42 7107 5230 7399 -842 995 -1370 C ATOM 2125 CD GLU B 42 37.663 30.026 23.079 1.00 57.53 C ANISOU 2125 CD GLU B 42 7818 5716 8325 -704 1086 -1188 C ATOM 2126 OE1 GLU B 42 37.847 29.444 21.986 1.00 57.97 O ANISOU 2126 OE1 GLU B 42 7849 5806 8373 -633 1008 -972 O ATOM 2127 OE2 GLU B 42 36.961 31.055 23.196 1.00 61.12 O ANISOU 2127 OE2 GLU B 42 8298 5969 8955 -666 1241 -1258 O ATOM 2128 N THR B 43 40.869 25.648 24.922 1.00 32.65 N ANISOU 2128 N THR B 43 4526 3548 4331 -965 491 -1156 N ATOM 2129 CA THR B 43 41.680 24.570 24.376 1.00 32.86 C ANISOU 2129 CA THR B 43 4501 3702 4283 -946 370 -994 C ATOM 2130 C THR B 43 41.475 24.556 22.872 1.00 32.46 C ANISOU 2130 C THR B 43 4460 3500 4374 -841 398 -813 C ATOM 2131 O THR B 43 40.574 25.217 22.364 1.00 32.59 O ANISOU 2131 O THR B 43 4515 3351 4516 -769 493 -791 O ATOM 2132 CB THR B 43 41.326 23.186 24.977 1.00 32.39 C ANISOU 2132 CB THR B 43 4426 3855 4026 -894 280 -911 C ATOM 2133 OG1 THR B 43 39.947 22.876 24.728 1.00 29.39 O ANISOU 2133 OG1 THR B 43 4086 3417 3663 -775 330 -835 O ATOM 2134 CG2 THR B 43 41.595 23.172 26.478 1.00 34.67 C ANISOU 2134 CG2 THR B 43 4699 4333 4142 -997 244 -1070 C ATOM 2135 N ALA B 44 42.315 23.813 22.161 1.00 30.21 N ANISOU 2135 N ALA B 44 4132 3281 4066 -829 320 -681 N ATOM 2136 CA ALA B 44 42.209 23.732 20.710 1.00 29.46 C ANISOU 2136 CA ALA B 44 4045 3076 4072 -737 342 -515 C ATOM 2137 C ALA B 44 40.916 23.030 20.298 1.00 29.54 C ANISOU 2137 C ALA B 44 4086 3094 4045 -609 341 -406 C ATOM 2138 O ALA B 44 40.288 23.379 19.296 1.00 26.99 O ANISOU 2138 O ALA B 44 3783 2656 3817 -527 392 -310 O ATOM 2139 CB ALA B 44 43.420 22.998 20.129 1.00 26.34 C ANISOU 2139 CB ALA B 44 3595 2768 3644 -755 267 -416 C ATOM 2140 N ALA B 45 40.523 22.037 21.085 1.00 28.24 N ANISOU 2140 N ALA B 45 3914 3074 3740 -595 282 -413 N ATOM 2141 CA ALA B 45 39.410 21.176 20.715 1.00 27.49 C ANISOU 2141 CA ALA B 45 3833 3005 3607 -491 269 -309 C ATOM 2142 C ALA B 45 38.895 20.385 21.903 1.00 27.62 C ANISOU 2142 C ALA B 45 3844 3159 3490 -496 237 -350 C ATOM 2143 O ALA B 45 39.497 20.390 22.979 1.00 31.06 O ANISOU 2143 O ALA B 45 4265 3699 3836 -576 210 -443 O ATOM 2144 CB ALA B 45 39.831 20.216 19.596 1.00 20.68 C ANISOU 2144 CB ALA B 45 2951 2175 2732 -442 212 -165 C ATOM 2145 N ILE B 46 37.767 19.719 21.702 1.00 23.25 N ANISOU 2145 N ILE B 46 3298 2616 2920 -416 240 -276 N ATOM 2146 CA ILE B 46 37.357 18.651 22.595 1.00 27.45 C ANISOU 2146 CA ILE B 46 3816 3283 3330 -409 205 -261 C ATOM 2147 C ILE B 46 37.317 17.370 21.779 1.00 27.67 C ANISOU 2147 C ILE B 46 3825 3339 3349 -355 151 -122 C ATOM 2148 O ILE B 46 37.239 17.419 20.550 1.00 27.28 O ANISOU 2148 O ILE B 46 3780 3210 3376 -313 151 -58 O ATOM 2149 CB ILE B 46 35.983 18.907 23.255 1.00 27.75 C ANISOU 2149 CB ILE B 46 3870 3311 3362 -375 273 -310 C ATOM 2150 CG1 ILE B 46 34.863 18.868 22.214 1.00 28.24 C ANISOU 2150 CG1 ILE B 46 3928 3278 3522 -284 300 -222 C ATOM 2151 CG2 ILE B 46 35.999 20.222 24.030 1.00 27.23 C ANISOU 2151 CG2 ILE B 46 3830 3195 3319 -429 349 -471 C ATOM 2152 CD1 ILE B 46 33.474 18.902 22.819 1.00 30.58 C ANISOU 2152 CD1 ILE B 46 4218 3581 3818 -241 362 -245 C ATOM 2153 N CYS B 47 37.391 16.230 22.452 1.00 26.85 N ANISOU 2153 N CYS B 47 3698 3350 3152 -357 111 -77 N ATOM 2154 CA CYS B 47 37.329 14.949 21.763 1.00 23.11 C ANISOU 2154 CA CYS B 47 3208 2885 2687 -312 77 38 C ATOM 2155 C CYS B 47 36.368 14.023 22.490 1.00 23.72 C ANISOU 2155 C CYS B 47 3274 3024 2715 -288 88 77 C ATOM 2156 O CYS B 47 36.575 13.694 23.660 1.00 26.88 O ANISOU 2156 O CYS B 47 3660 3531 3023 -314 81 76 O ATOM 2157 CB CYS B 47 38.716 14.316 21.657 1.00 23.17 C ANISOU 2157 CB CYS B 47 3185 2946 2672 -333 25 89 C ATOM 2158 SG CYS B 47 38.730 12.781 20.703 1.00 27.55 S ANISOU 2158 SG CYS B 47 3725 3476 3267 -278 8 207 S ATOM 2159 N ILE B 48 35.317 13.613 21.782 1.00 20.33 N ANISOU 2159 N ILE B 48 2844 2537 2344 -243 105 117 N ATOM 2160 CA ILE B 48 34.210 12.850 22.350 1.00 21.78 C ANISOU 2160 CA ILE B 48 3010 2756 2510 -224 131 151 C ATOM 2161 C ILE B 48 33.726 11.825 21.327 1.00 22.69 C ANISOU 2161 C ILE B 48 3107 2823 2691 -197 116 218 C ATOM 2162 O ILE B 48 34.059 11.927 20.146 1.00 23.54 O ANISOU 2162 O ILE B 48 3224 2875 2844 -187 91 221 O ATOM 2163 CB ILE B 48 33.013 13.764 22.740 1.00 23.52 C ANISOU 2163 CB ILE B 48 3234 2955 2747 -208 191 87 C ATOM 2164 CG1 ILE B 48 32.527 14.543 21.519 1.00 24.86 C ANISOU 2164 CG1 ILE B 48 3406 3025 3015 -172 197 79 C ATOM 2165 CG2 ILE B 48 33.385 14.732 23.859 1.00 24.48 C ANISOU 2165 CG2 ILE B 48 3377 3123 2800 -245 224 -10 C ATOM 2166 CD1 ILE B 48 31.562 15.674 21.855 1.00 28.12 C ANISOU 2166 CD1 ILE B 48 3818 3396 3472 -144 267 19 C ATOM 2167 N PHE B 49 32.940 10.847 21.771 1.00 19.07 N ANISOU 2167 N PHE B 49 2623 2389 2235 -193 137 265 N ATOM 2168 CA PHE B 49 32.364 9.869 20.854 1.00 21.01 C ANISOU 2168 CA PHE B 49 2847 2584 2552 -186 129 302 C ATOM 2169 C PHE B 49 31.343 10.554 19.936 1.00 20.52 C ANISOU 2169 C PHE B 49 2771 2485 2539 -168 125 264 C ATOM 2170 O PHE B 49 30.730 11.542 20.332 1.00 22.90 O ANISOU 2170 O PHE B 49 3069 2793 2837 -150 153 232 O ATOM 2171 CB PHE B 49 31.730 8.706 21.632 1.00 20.20 C ANISOU 2171 CB PHE B 49 2712 2504 2459 -195 165 363 C ATOM 2172 CG PHE B 49 32.737 7.697 22.144 1.00 21.52 C ANISOU 2172 CG PHE B 49 2878 2689 2609 -199 164 440 C ATOM 2173 CD1 PHE B 49 33.452 6.899 21.257 1.00 23.78 C ANISOU 2173 CD1 PHE B 49 3167 2912 2957 -196 147 463 C ATOM 2174 CD2 PHE B 49 32.958 7.539 23.501 1.00 20.26 C ANISOU 2174 CD2 PHE B 49 2709 2619 2371 -199 186 497 C ATOM 2175 CE1 PHE B 49 34.382 5.966 21.715 1.00 23.91 C ANISOU 2175 CE1 PHE B 49 3171 2933 2981 -185 157 551 C ATOM 2176 CE2 PHE B 49 33.884 6.611 23.967 1.00 24.44 C ANISOU 2176 CE2 PHE B 49 3222 3176 2888 -189 183 597 C ATOM 2177 CZ PHE B 49 34.598 5.824 23.071 1.00 25.16 C ANISOU 2177 CZ PHE B 49 3310 3183 3065 -177 171 630 C ATOM 2178 N PRO B 50 31.177 10.042 18.702 1.00 22.22 N ANISOU 2178 N PRO B 50 2977 2669 2798 -170 93 268 N ATOM 2179 CA PRO B 50 30.415 10.731 17.650 1.00 22.95 C ANISOU 2179 CA PRO B 50 3050 2754 2917 -149 71 251 C ATOM 2180 C PRO B 50 28.988 11.144 18.018 1.00 21.79 C ANISOU 2180 C PRO B 50 2849 2626 2802 -129 96 253 C ATOM 2181 O PRO B 50 28.583 12.236 17.624 1.00 21.51 O ANISOU 2181 O PRO B 50 2802 2585 2784 -89 97 252 O ATOM 2182 CB PRO B 50 30.385 9.703 16.515 1.00 24.82 C ANISOU 2182 CB PRO B 50 3274 2985 3171 -174 35 246 C ATOM 2183 CG PRO B 50 31.632 8.880 16.726 1.00 24.18 C ANISOU 2183 CG PRO B 50 3230 2876 3082 -192 45 256 C ATOM 2184 CD PRO B 50 31.769 8.778 18.211 1.00 24.38 C ANISOU 2184 CD PRO B 50 3254 2917 3093 -192 81 288 C ATOM 2185 N ARG B 51 28.247 10.312 18.750 1.00 22.72 N ANISOU 2185 N ARG B 51 2929 2764 2940 -151 126 266 N ATOM 2186 CA ARG B 51 26.844 10.610 19.032 1.00 21.54 C ANISOU 2186 CA ARG B 51 2713 2639 2834 -133 156 272 C ATOM 2187 C ARG B 51 26.686 11.865 19.896 1.00 21.62 C ANISOU 2187 C ARG B 51 2736 2648 2829 -89 213 252 C ATOM 2188 O ARG B 51 25.600 12.436 19.968 1.00 22.90 O ANISOU 2188 O ARG B 51 2843 2819 3040 -53 246 256 O ATOM 2189 CB ARG B 51 26.150 9.416 19.707 1.00 22.02 C ANISOU 2189 CB ARG B 51 2727 2714 2925 -173 191 296 C ATOM 2190 CG ARG B 51 26.577 9.114 21.147 1.00 25.03 C ANISOU 2190 CG ARG B 51 3139 3112 3258 -180 253 322 C ATOM 2191 CD ARG B 51 25.911 7.815 21.630 1.00 27.21 C ANISOU 2191 CD ARG B 51 3365 3389 3583 -220 294 373 C ATOM 2192 NE ARG B 51 26.284 7.425 22.991 1.00 28.03 N ANISOU 2192 NE ARG B 51 3491 3529 3629 -221 354 427 N ATOM 2193 CZ ARG B 51 27.389 6.746 23.304 1.00 29.12 C ANISOU 2193 CZ ARG B 51 3671 3662 3732 -230 347 475 C ATOM 2194 NH1 ARG B 51 28.253 6.393 22.358 1.00 23.98 N ANISOU 2194 NH1 ARG B 51 3048 2954 3108 -238 292 462 N ATOM 2195 NH2 ARG B 51 27.635 6.425 24.569 1.00 30.24 N ANISOU 2195 NH2 ARG B 51 3819 3865 3806 -226 397 545 N ATOM 2196 N PHE B 52 27.766 12.305 20.533 1.00 19.76 N ANISOU 2196 N PHE B 52 2567 2404 2535 -94 229 224 N ATOM 2197 CA PHE B 52 27.694 13.483 21.397 1.00 23.03 C ANISOU 2197 CA PHE B 52 3003 2813 2935 -69 293 174 C ATOM 2198 C PHE B 52 27.976 14.788 20.644 1.00 22.88 C ANISOU 2198 C PHE B 52 3005 2727 2961 -32 290 150 C ATOM 2199 O PHE B 52 27.818 15.873 21.198 1.00 26.26 O ANISOU 2199 O PHE B 52 3447 3120 3412 -8 356 98 O ATOM 2200 CB PHE B 52 28.658 13.334 22.580 1.00 21.72 C ANISOU 2200 CB PHE B 52 2887 2693 2673 -108 312 143 C ATOM 2201 CG PHE B 52 28.357 12.144 23.451 1.00 21.44 C ANISOU 2201 CG PHE B 52 2828 2725 2592 -133 332 192 C ATOM 2202 CD1 PHE B 52 27.183 12.088 24.189 1.00 22.15 C ANISOU 2202 CD1 PHE B 52 2876 2850 2691 -119 404 197 C ATOM 2203 CD2 PHE B 52 29.240 11.080 23.523 1.00 21.43 C ANISOU 2203 CD2 PHE B 52 2841 2749 2554 -163 292 248 C ATOM 2204 CE1 PHE B 52 26.890 10.983 24.988 1.00 26.30 C ANISOU 2204 CE1 PHE B 52 3376 3435 3181 -142 435 263 C ATOM 2205 CE2 PHE B 52 28.962 9.976 24.319 1.00 22.75 C ANISOU 2205 CE2 PHE B 52 2982 2965 2696 -178 323 319 C ATOM 2206 CZ PHE B 52 27.786 9.925 25.051 1.00 24.60 C ANISOU 2206 CZ PHE B 52 3178 3236 2933 -171 394 329 C ATOM 2207 N ILE B 53 28.370 14.682 19.380 1.00 21.24 N ANISOU 2207 N ILE B 53 2800 2498 2773 -27 225 189 N ATOM 2208 CA ILE B 53 28.762 15.859 18.597 1.00 22.29 C ANISOU 2208 CA ILE B 53 2953 2567 2948 9 226 194 C ATOM 2209 C ILE B 53 27.669 16.952 18.465 1.00 25.44 C ANISOU 2209 C ILE B 53 3307 2923 3437 80 281 214 C ATOM 2210 O ILE B 53 27.973 18.132 18.637 1.00 26.63 O ANISOU 2210 O ILE B 53 3487 2994 3638 105 339 185 O ATOM 2211 CB ILE B 53 29.241 15.430 17.191 1.00 23.31 C ANISOU 2211 CB ILE B 53 3085 2708 3064 5 150 247 C ATOM 2212 CG1 ILE B 53 30.582 14.696 17.302 1.00 24.18 C ANISOU 2212 CG1 ILE B 53 3246 2829 3113 -50 121 226 C ATOM 2213 CG2 ILE B 53 29.365 16.627 16.270 1.00 22.58 C ANISOU 2213 CG2 ILE B 53 2996 2563 3020 56 158 290 C ATOM 2214 CD1 ILE B 53 31.069 14.091 16.003 1.00 21.35 C ANISOU 2214 CD1 ILE B 53 2892 2487 2732 -58 64 260 C ATOM 2215 N PRO B 54 26.400 16.577 18.181 1.00 26.59 N ANISOU 2215 N PRO B 54 3372 3113 3618 113 270 262 N ATOM 2216 CA PRO B 54 25.395 17.642 18.057 1.00 25.38 C ANISOU 2216 CA PRO B 54 3161 2920 3564 196 328 299 C ATOM 2217 C PRO B 54 25.167 18.434 19.349 1.00 28.59 C ANISOU 2217 C PRO B 54 3587 3266 4010 214 446 220 C ATOM 2218 O PRO B 54 25.044 19.661 19.297 1.00 26.21 O ANISOU 2218 O PRO B 54 3288 2871 3801 273 518 218 O ATOM 2219 CB PRO B 54 24.123 16.877 17.666 1.00 26.33 C ANISOU 2219 CB PRO B 54 3175 3127 3702 209 285 357 C ATOM 2220 CG PRO B 54 24.620 15.646 17.005 1.00 27.72 C ANISOU 2220 CG PRO B 54 3366 3368 3799 138 188 360 C ATOM 2221 CD PRO B 54 25.849 15.271 17.770 1.00 24.28 C ANISOU 2221 CD PRO B 54 3026 2901 3296 79 205 294 C ATOM 2222 N VAL B 55 25.101 17.742 20.484 1.00 29.21 N ANISOU 2222 N VAL B 55 3679 3397 4022 164 475 157 N ATOM 2223 CA VAL B 55 24.911 18.409 21.770 1.00 29.48 C ANISOU 2223 CA VAL B 55 3738 3403 4060 169 591 64 C ATOM 2224 C VAL B 55 26.097 19.320 22.093 1.00 27.85 C ANISOU 2224 C VAL B 55 3622 3123 3838 138 623 -29 C ATOM 2225 O VAL B 55 25.918 20.464 22.521 1.00 26.73 O ANISOU 2225 O VAL B 55 3494 2892 3768 169 725 -100 O ATOM 2226 CB VAL B 55 24.711 17.382 22.907 1.00 33.28 C ANISOU 2226 CB VAL B 55 4219 3985 4442 116 609 33 C ATOM 2227 CG1 VAL B 55 25.014 17.999 24.271 1.00 32.46 C ANISOU 2227 CG1 VAL B 55 4172 3884 4276 92 709 -89 C ATOM 2228 CG2 VAL B 55 23.293 16.830 22.868 1.00 33.55 C ANISOU 2228 CG2 VAL B 55 4150 4066 4531 151 630 99 C ATOM 2229 N ALA B 56 27.306 18.815 21.866 1.00 25.58 N ANISOU 2229 N ALA B 56 3386 2865 3469 73 541 -31 N ATOM 2230 CA ALA B 56 28.518 19.596 22.092 1.00 24.90 C ANISOU 2230 CA ALA B 56 3370 2721 3369 27 556 -115 C ATOM 2231 C ALA B 56 28.540 20.844 21.217 1.00 28.15 C ANISOU 2231 C ALA B 56 3783 2994 3917 80 596 -92 C ATOM 2232 O ALA B 56 28.908 21.927 21.671 1.00 29.12 O ANISOU 2232 O ALA B 56 3944 3021 4097 66 678 -188 O ATOM 2233 CB ALA B 56 29.750 18.750 21.830 1.00 21.66 C ANISOU 2233 CB ALA B 56 2991 2373 2866 -39 456 -92 C ATOM 2234 N LYS B 57 28.142 20.682 19.959 1.00 30.35 N ANISOU 2234 N LYS B 57 4017 3266 4248 138 542 37 N ATOM 2235 CA LYS B 57 28.125 21.793 19.018 1.00 31.78 C ANISOU 2235 CA LYS B 57 4190 3332 4555 203 576 104 C ATOM 2236 C LYS B 57 27.157 22.874 19.499 1.00 31.87 C ANISOU 2236 C LYS B 57 4171 3240 4700 277 704 77 C ATOM 2237 O LYS B 57 27.458 24.069 19.423 1.00 32.17 O ANISOU 2237 O LYS B 57 4235 3134 4855 300 791 53 O ATOM 2238 CB LYS B 57 27.747 21.304 17.618 1.00 35.40 C ANISOU 2238 CB LYS B 57 4593 3848 5008 252 485 255 C ATOM 2239 CG LYS B 57 28.045 22.297 16.503 1.00 40.86 C ANISOU 2239 CG LYS B 57 5284 4451 5791 310 500 356 C ATOM 2240 CD LYS B 57 27.996 21.631 15.130 1.00 43.70 C ANISOU 2240 CD LYS B 57 5606 4914 6082 329 390 484 C ATOM 2241 N LYS B 58 26.009 22.450 20.021 1.00 30.60 N ANISOU 2241 N LYS B 58 3951 3141 4533 313 730 78 N ATOM 2242 CA LYS B 58 25.037 23.390 20.569 1.00 31.92 C ANISOU 2242 CA LYS B 58 4082 3216 4829 390 867 45 C ATOM 2243 C LYS B 58 25.579 24.069 21.823 1.00 32.57 C ANISOU 2243 C LYS B 58 4244 3225 4907 330 980 -143 C ATOM 2244 O LYS B 58 25.364 25.261 22.026 1.00 32.89 O ANISOU 2244 O LYS B 58 4292 3115 5090 377 1110 -197 O ATOM 2245 CB LYS B 58 23.716 22.687 20.884 1.00 30.06 C ANISOU 2245 CB LYS B 58 3757 3083 4582 432 871 87 C ATOM 2246 CG LYS B 58 22.627 23.620 21.366 1.00 31.30 C ANISOU 2246 CG LYS B 58 3857 3150 4885 528 1020 71 C ATOM 2247 CD LYS B 58 21.298 22.902 21.503 1.00 35.66 C ANISOU 2247 CD LYS B 58 4296 3813 5440 573 1014 139 C ATOM 2248 CE LYS B 58 20.177 23.878 21.855 1.00 38.00 C ANISOU 2248 CE LYS B 58 4516 4015 5906 689 1170 146 C ATOM 2249 NZ LYS B 58 18.834 23.227 21.790 1.00 39.29 N ANISOU 2249 NZ LYS B 58 4540 4292 6096 741 1156 242 N ATOM 2250 N ALA B 59 26.291 23.308 22.653 1.00 33.68 N ANISOU 2250 N ALA B 59 4439 3474 4884 225 933 -244 N ATOM 2251 CA ALA B 59 26.824 23.828 23.910 1.00 32.81 C ANISOU 2251 CA ALA B 59 4397 3345 4723 151 1020 -435 C ATOM 2252 C ALA B 59 27.934 24.855 23.687 1.00 34.56 C ANISOU 2252 C ALA B 59 4680 3432 5017 101 1048 -514 C ATOM 2253 O ALA B 59 28.030 25.848 24.413 1.00 37.57 O ANISOU 2253 O ALA B 59 5101 3712 5462 76 1172 -671 O ATOM 2254 CB ALA B 59 27.333 22.685 24.780 1.00 31.09 C ANISOU 2254 CB ALA B 59 4207 3307 4298 57 944 -485 C ATOM 2255 N LEU B 60 28.774 24.612 22.689 1.00 32.83 N ANISOU 2255 N LEU B 60 4468 3211 4794 82 944 -415 N ATOM 2256 CA LEU B 60 29.890 25.504 22.407 1.00 33.70 C ANISOU 2256 CA LEU B 60 4627 3199 4977 27 966 -472 C ATOM 2257 C LEU B 60 29.395 26.813 21.798 1.00 37.41 C ANISOU 2257 C LEU B 60 5082 3459 5674 116 1088 -427 C ATOM 2258 O LEU B 60 29.898 27.890 22.128 1.00 36.86 O ANISOU 2258 O LEU B 60 5053 3237 5713 73 1192 -549 O ATOM 2259 CB LEU B 60 30.900 24.825 21.481 1.00 31.25 C ANISOU 2259 CB LEU B 60 4320 2954 4598 -11 831 -364 C ATOM 2260 CG LEU B 60 31.695 23.678 22.110 1.00 31.38 C ANISOU 2260 CG LEU B 60 4354 3147 4421 -106 725 -413 C ATOM 2261 CD1 LEU B 60 32.416 22.865 21.042 1.00 32.82 C ANISOU 2261 CD1 LEU B 60 4525 3388 4557 -110 605 -280 C ATOM 2262 CD2 LEU B 60 32.692 24.208 23.135 1.00 30.45 C ANISOU 2262 CD2 LEU B 60 4281 3031 4257 -222 755 -595 C ATOM 2263 N LYS B 61 28.402 26.720 20.918 1.00 38.37 N ANISOU 2263 N LYS B 61 5137 3571 5872 239 1079 -250 N ATOM 2264 CA LYS B 61 27.778 27.914 20.359 1.00 40.85 C ANISOU 2264 CA LYS B 61 5417 3697 6407 350 1199 -169 C ATOM 2265 C LYS B 61 27.041 28.679 21.452 1.00 40.09 C ANISOU 2265 C LYS B 61 5325 3495 6414 376 1368 -320 C ATOM 2266 O LYS B 61 27.080 29.906 21.492 1.00 39.40 O ANISOU 2266 O LYS B 61 5255 3198 6518 405 1513 -369 O ATOM 2267 CB LYS B 61 26.825 27.551 19.217 1.00 44.37 C ANISOU 2267 CB LYS B 61 5770 4203 6884 475 1133 64 C ATOM 2268 CG LYS B 61 27.531 27.001 17.977 1.00 47.41 C ANISOU 2268 CG LYS B 61 6154 4671 7187 460 993 211 C ATOM 2269 CD LYS B 61 26.538 26.495 16.934 1.00 48.43 C ANISOU 2269 CD LYS B 61 6188 4913 7303 563 909 412 C ATOM 2270 N ALA B 62 26.385 27.941 22.346 1.00 41.14 N ANISOU 2270 N ALA B 62 5442 3767 6424 364 1362 -395 N ATOM 2271 CA ALA B 62 25.668 28.536 23.471 1.00 40.11 C ANISOU 2271 CA ALA B 62 5317 3569 6355 384 1527 -554 C ATOM 2272 C ALA B 62 26.593 29.364 24.367 1.00 38.47 C ANISOU 2272 C ALA B 62 5203 3255 6158 269 1626 -798 C ATOM 2273 O ALA B 62 26.211 30.437 24.824 1.00 41.35 O ANISOU 2273 O ALA B 62 5581 3445 6686 302 1805 -916 O ATOM 2274 CB ALA B 62 24.978 27.457 24.289 1.00 39.29 C ANISOU 2274 CB ALA B 62 5185 3665 6080 370 1490 -585 C ATOM 2275 N GLN B 63 27.802 28.865 24.612 1.00 33.88 N ANISOU 2275 N GLN B 63 4678 2782 5411 132 1514 -879 N ATOM 2276 CA GLN B 63 28.775 29.581 25.435 1.00 37.15 C ANISOU 2276 CA GLN B 63 5169 3131 5814 -1 1581 -1118 C ATOM 2277 C GLN B 63 29.647 30.491 24.565 1.00 39.97 C ANISOU 2277 C GLN B 63 5546 3292 6348 -24 1603 -1084 C ATOM 2278 O GLN B 63 30.653 31.042 25.028 1.00 39.67 O ANISOU 2278 O GLN B 63 5561 3198 6313 -154 1631 -1263 O ATOM 2279 CB GLN B 63 29.646 28.600 26.233 1.00 36.72 C ANISOU 2279 CB GLN B 63 5149 3314 5489 -139 1449 -1217 C ATOM 2280 CG GLN B 63 30.582 27.732 25.388 1.00 34.04 C ANISOU 2280 CG GLN B 63 4797 3080 5056 -176 1266 -1063 C ATOM 2281 CD GLN B 63 31.447 26.799 26.233 1.00 34.09 C ANISOU 2281 CD GLN B 63 4824 3315 4815 -298 1148 -1147 C ATOM 2282 OE1 GLN B 63 31.088 26.449 27.357 1.00 34.02 O ANISOU 2282 OE1 GLN B 63 4826 3441 4661 -330 1172 -1256 O ATOM 2283 NE2 GLN B 63 32.595 26.397 25.691 1.00 32.28 N ANISOU 2283 NE2 GLN B 63 4594 3136 4536 -361 1024 -1083 N ATOM 2284 N GLN B 64 29.241 30.639 23.305 1.00 39.05 N ANISOU 2284 N GLN B 64 5379 3083 6375 100 1589 -848 N ATOM 2285 CA GLN B 64 29.884 31.542 22.352 1.00 40.05 C ANISOU 2285 CA GLN B 64 5513 3012 6692 110 1630 -762 C ATOM 2286 C GLN B 64 31.371 31.252 22.176 1.00 37.91 C ANISOU 2286 C GLN B 64 5281 2807 6317 -32 1516 -803 C ATOM 2287 O GLN B 64 32.187 32.171 22.140 1.00 36.77 O ANISOU 2287 O GLN B 64 5169 2497 6305 -108 1593 -893 O ATOM 2288 CB GLN B 64 29.683 33.002 22.774 1.00 43.82 C ANISOU 2288 CB GLN B 64 6016 3213 7419 121 1851 -905 C ATOM 2289 CG GLN B 64 28.222 33.416 22.929 1.00 47.85 C ANISOU 2289 CG GLN B 64 6469 3666 8048 270 1969 -844 C ATOM 2290 CD GLN B 64 27.426 33.288 21.641 1.00 48.69 C ANISOU 2290 CD GLN B 64 6490 3752 8260 446 1934 -531 C ATOM 2291 OE1 GLN B 64 27.925 33.585 20.555 1.00 48.75 O ANISOU 2291 OE1 GLN B 64 6480 3706 8336 469 1885 -354 O ATOM 2292 NE2 GLN B 64 26.179 32.841 21.757 1.00 49.48 N ANISOU 2292 NE2 GLN B 64 6524 3923 8351 567 1949 -455 N ATOM 2293 N THR B 65 31.711 29.970 22.073 1.00 33.79 N ANISOU 2293 N THR B 65 4747 2519 5572 -67 1342 -737 N ATOM 2294 CA THR B 65 33.058 29.556 21.700 1.00 34.94 C ANISOU 2294 CA THR B 65 4909 2742 5626 -171 1224 -722 C ATOM 2295 C THR B 65 33.002 28.661 20.468 1.00 33.03 C ANISOU 2295 C THR B 65 4627 2604 5319 -92 1096 -478 C ATOM 2296 O THR B 65 33.225 27.455 20.562 1.00 32.38 O ANISOU 2296 O THR B 65 4536 2717 5048 -122 965 -452 O ATOM 2297 CB THR B 65 33.774 28.809 22.839 1.00 36.36 C ANISOU 2297 CB THR B 65 5113 3117 5587 -308 1138 -895 C ATOM 2298 OG1 THR B 65 32.994 27.670 23.230 1.00 34.38 O ANISOU 2298 OG1 THR B 65 4841 3054 5169 -258 1064 -846 O ATOM 2299 CG2 THR B 65 33.981 29.726 24.038 1.00 36.76 C ANISOU 2299 CG2 THR B 65 5204 3088 5674 -412 1256 -1164 C ATOM 2300 N PRO B 66 32.709 29.255 19.300 1.00 36.21 N ANISOU 2300 N PRO B 66 5005 2877 5877 8 1139 -299 N ATOM 2301 CA PRO B 66 32.512 28.478 18.072 1.00 36.69 C ANISOU 2301 CA PRO B 66 5025 3048 5867 89 1026 -75 C ATOM 2302 C PRO B 66 33.810 27.925 17.477 1.00 34.64 C ANISOU 2302 C PRO B 66 4781 2872 5508 8 922 -34 C ATOM 2303 O PRO B 66 33.762 27.065 16.599 1.00 32.41 O ANISOU 2303 O PRO B 66 4474 2715 5124 50 819 107 O ATOM 2304 CB PRO B 66 31.878 29.496 17.124 1.00 39.67 C ANISOU 2304 CB PRO B 66 5369 3259 6446 216 1124 96 C ATOM 2305 CG PRO B 66 32.450 30.800 17.556 1.00 41.64 C ANISOU 2305 CG PRO B 66 5656 3278 6886 160 1273 -24 C ATOM 2306 CD PRO B 66 32.583 30.705 19.057 1.00 40.40 C ANISOU 2306 CD PRO B 66 5541 3151 6660 50 1302 -293 C ATOM 2307 N HIS B 67 34.954 28.402 17.952 1.00 33.32 N ANISOU 2307 N HIS B 67 4647 2641 5373 -110 953 -167 N ATOM 2308 CA HIS B 67 36.221 28.027 17.341 1.00 33.29 C ANISOU 2308 CA HIS B 67 4644 2695 5309 -180 876 -117 C ATOM 2309 C HIS B 67 36.947 26.936 18.117 1.00 30.51 C ANISOU 2309 C HIS B 67 4296 2531 4767 -280 762 -227 C ATOM 2310 O HIS B 67 38.075 26.574 17.793 1.00 32.22 O ANISOU 2310 O HIS B 67 4504 2806 4934 -345 701 -208 O ATOM 2311 CB HIS B 67 37.099 29.263 17.195 1.00 33.05 C ANISOU 2311 CB HIS B 67 4627 2472 5457 -247 981 -160 C ATOM 2312 CG HIS B 67 36.449 30.359 16.408 1.00 36.46 C ANISOU 2312 CG HIS B 67 5051 2704 6097 -139 1106 -22 C ATOM 2313 ND1 HIS B 67 35.895 30.150 15.165 1.00 35.39 N ANISOU 2313 ND1 HIS B 67 4886 2603 5956 -10 1076 218 N ATOM 2314 CD2 HIS B 67 36.256 31.669 16.694 1.00 39.14 C ANISOU 2314 CD2 HIS B 67 5405 2808 6660 -138 1266 -84 C ATOM 2315 CE1 HIS B 67 35.394 31.288 14.713 1.00 39.02 C ANISOU 2315 CE1 HIS B 67 5335 2868 6624 75 1207 322 C ATOM 2316 NE2 HIS B 67 35.598 32.223 15.621 1.00 40.24 N ANISOU 2316 NE2 HIS B 67 5517 2839 6933 3 1331 143 N ATOM 2317 N ILE B 68 36.298 26.403 19.141 1.00 31.70 N ANISOU 2317 N ILE B 68 4451 2779 4815 -285 741 -327 N ATOM 2318 CA ILE B 68 36.805 25.196 19.772 1.00 30.71 C ANISOU 2318 CA ILE B 68 4318 2849 4500 -347 627 -374 C ATOM 2319 C ILE B 68 36.354 24.015 18.925 1.00 31.72 C ANISOU 2319 C ILE B 68 4424 3087 4542 -264 538 -210 C ATOM 2320 O ILE B 68 35.158 23.746 18.808 1.00 33.81 O ANISOU 2320 O ILE B 68 4677 3366 4804 -181 546 -154 O ATOM 2321 CB ILE B 68 36.320 25.047 21.218 1.00 31.88 C ANISOU 2321 CB ILE B 68 4478 3075 4558 -388 644 -531 C ATOM 2322 CG1 ILE B 68 36.807 26.234 22.054 1.00 34.20 C ANISOU 2322 CG1 ILE B 68 4797 3268 4929 -489 736 -727 C ATOM 2323 CG2 ILE B 68 36.815 23.725 21.809 1.00 30.76 C ANISOU 2323 CG2 ILE B 68 4320 3144 4222 -436 527 -532 C ATOM 2324 CD1 ILE B 68 36.312 26.233 23.485 1.00 36.86 C ANISOU 2324 CD1 ILE B 68 5152 3687 5167 -533 772 -903 C ATOM 2325 N LYS B 69 37.316 23.331 18.313 1.00 31.04 N ANISOU 2325 N LYS B 69 4326 3073 4394 -292 461 -142 N ATOM 2326 CA LYS B 69 37.013 22.251 17.380 1.00 31.89 C ANISOU 2326 CA LYS B 69 4418 3268 4431 -226 388 -7 C ATOM 2327 C LYS B 69 36.401 21.044 18.079 1.00 28.75 C ANISOU 2327 C LYS B 69 4010 3000 3913 -218 330 -26 C ATOM 2328 O LYS B 69 36.652 20.798 19.258 1.00 28.70 O ANISOU 2328 O LYS B 69 4006 3059 3840 -276 319 -123 O ATOM 2329 CB LYS B 69 38.273 21.818 16.629 1.00 35.17 C ANISOU 2329 CB LYS B 69 4825 3722 4816 -260 340 50 C ATOM 2330 CG LYS B 69 38.929 22.924 15.829 1.00 43.38 C ANISOU 2330 CG LYS B 69 5868 4639 5974 -269 403 95 C ATOM 2331 CD LYS B 69 38.054 23.382 14.674 1.00 47.60 C ANISOU 2331 CD LYS B 69 6404 5109 6572 -168 442 231 C ATOM 2332 CE LYS B 69 38.718 24.529 13.924 1.00 51.11 C ANISOU 2332 CE LYS B 69 6852 5422 7144 -173 520 297 C ATOM 2333 NZ LYS B 69 40.124 24.189 13.566 1.00 52.22 N ANISOU 2333 NZ LYS B 69 6983 5608 7252 -241 493 304 N ATOM 2334 N ILE B 70 35.594 20.293 17.342 1.00 24.85 N ANISOU 2334 N ILE B 70 3500 2551 3391 -150 293 70 N ATOM 2335 CA ILE B 70 35.052 19.050 17.859 1.00 25.20 C ANISOU 2335 CA ILE B 70 3529 2703 3343 -147 244 69 C ATOM 2336 C ILE B 70 35.704 17.879 17.138 1.00 26.31 C ANISOU 2336 C ILE B 70 3662 2912 3421 -154 175 132 C ATOM 2337 O ILE B 70 35.465 17.667 15.944 1.00 26.76 O ANISOU 2337 O ILE B 70 3713 2968 3488 -113 156 207 O ATOM 2338 CB ILE B 70 33.528 18.969 17.694 1.00 26.33 C ANISOU 2338 CB ILE B 70 3646 2847 3512 -78 260 108 C ATOM 2339 CG1 ILE B 70 32.845 20.127 18.428 1.00 27.28 C ANISOU 2339 CG1 ILE B 70 3769 2887 3711 -57 349 44 C ATOM 2340 CG2 ILE B 70 33.020 17.640 18.220 1.00 25.56 C ANISOU 2340 CG2 ILE B 70 3527 2849 3333 -87 218 110 C ATOM 2341 CD1 ILE B 70 31.337 20.107 18.319 1.00 27.17 C ANISOU 2341 CD1 ILE B 70 3711 2876 3736 18 373 90 C ATOM 2342 N ALA B 71 36.551 17.150 17.860 1.00 19.51 N ANISOU 2342 N ALA B 71 2798 2118 2497 -205 143 101 N ATOM 2343 CA ALA B 71 37.155 15.938 17.334 1.00 23.48 C ANISOU 2343 CA ALA B 71 3290 2674 2958 -205 95 155 C ATOM 2344 C ALA B 71 36.412 14.729 17.873 1.00 22.79 C ANISOU 2344 C ALA B 71 3187 2646 2825 -195 75 169 C ATOM 2345 O ALA B 71 35.701 14.818 18.874 1.00 23.97 O ANISOU 2345 O ALA B 71 3332 2819 2955 -199 94 136 O ATOM 2346 CB ALA B 71 38.638 15.861 17.692 1.00 22.34 C ANISOU 2346 CB ALA B 71 3135 2560 2794 -256 77 141 C ATOM 2347 N THR B 72 36.564 13.604 17.193 1.00 22.15 N ANISOU 2347 N THR B 72 3098 2582 2736 -183 50 216 N ATOM 2348 CA THR B 72 35.913 12.372 17.605 1.00 23.97 C ANISOU 2348 CA THR B 72 3310 2845 2951 -179 43 236 C ATOM 2349 C THR B 72 36.780 11.206 17.156 1.00 24.66 C ANISOU 2349 C THR B 72 3391 2935 3042 -181 30 272 C ATOM 2350 O THR B 72 37.840 11.418 16.569 1.00 28.55 O ANISOU 2350 O THR B 72 3891 3417 3541 -183 27 278 O ATOM 2351 CB THR B 72 34.473 12.261 17.027 1.00 22.36 C ANISOU 2351 CB THR B 72 3094 2629 2772 -154 45 238 C ATOM 2352 OG1 THR B 72 33.771 11.188 17.668 1.00 22.03 O ANISOU 2352 OG1 THR B 72 3028 2611 2730 -163 52 250 O ATOM 2353 CG2 THR B 72 34.489 12.044 15.526 1.00 23.47 C ANISOU 2353 CG2 THR B 72 3238 2757 2921 -141 23 252 C ATOM 2354 N VAL B 73 36.348 9.982 17.438 1.00 24.65 N ANISOU 2354 N VAL B 73 3374 2939 3053 -180 37 297 N ATOM 2355 CA VAL B 73 37.155 8.807 17.115 1.00 26.40 C ANISOU 2355 CA VAL B 73 3586 3140 3303 -175 45 332 C ATOM 2356 C VAL B 73 36.375 7.786 16.293 1.00 26.79 C ANISOU 2356 C VAL B 73 3637 3145 3398 -178 61 314 C ATOM 2357 O VAL B 73 35.158 7.649 16.457 1.00 25.07 O ANISOU 2357 O VAL B 73 3407 2930 3190 -189 61 299 O ATOM 2358 CB VAL B 73 37.684 8.113 18.398 1.00 21.03 C ANISOU 2358 CB VAL B 73 2877 2498 2614 -173 53 397 C ATOM 2359 CG1 VAL B 73 38.685 9.010 19.122 1.00 20.17 C ANISOU 2359 CG1 VAL B 73 2758 2456 2451 -186 27 399 C ATOM 2360 CG2 VAL B 73 36.523 7.736 19.328 1.00 23.72 C ANISOU 2360 CG2 VAL B 73 3206 2859 2946 -179 70 415 C ATOM 2361 N THR B 74 37.081 7.079 15.407 1.00 25.13 N ANISOU 2361 N THR B 74 3434 2896 3218 -173 79 305 N ATOM 2362 CA THR B 74 36.498 5.983 14.620 1.00 23.15 C ANISOU 2362 CA THR B 74 3185 2597 3016 -190 102 262 C ATOM 2363 C THR B 74 37.481 4.816 14.511 1.00 23.34 C ANISOU 2363 C THR B 74 3205 2556 3109 -176 156 282 C ATOM 2364 O THR B 74 38.689 5.008 14.663 1.00 20.83 O ANISOU 2364 O THR B 74 2880 2245 2788 -147 164 327 O ATOM 2365 CB THR B 74 36.105 6.427 13.196 1.00 21.69 C ANISOU 2365 CB THR B 74 3021 2435 2786 -203 79 191 C ATOM 2366 OG1 THR B 74 37.272 6.882 12.497 1.00 21.63 O ANISOU 2366 OG1 THR B 74 3035 2435 2748 -182 88 195 O ATOM 2367 CG2 THR B 74 35.048 7.532 13.238 1.00 19.73 C ANISOU 2367 CG2 THR B 74 2763 2242 2492 -202 34 191 C ATOM 2368 N ASN B 75 36.950 3.620 14.234 1.00 24.72 N ANISOU 2368 N ASN B 75 3374 2659 3358 -198 198 248 N ATOM 2369 CA ASN B 75 37.720 2.376 14.254 1.00 24.03 C ANISOU 2369 CA ASN B 75 3279 2478 3375 -178 272 273 C ATOM 2370 C ASN B 75 38.417 2.222 15.606 1.00 27.84 C ANISOU 2370 C ASN B 75 3724 2971 3883 -133 282 411 C ATOM 2371 O ASN B 75 39.504 1.649 15.709 1.00 27.13 O ANISOU 2371 O ASN B 75 3613 2841 3855 -89 326 473 O ATOM 2372 CB ASN B 75 38.736 2.337 13.103 1.00 22.18 C ANISOU 2372 CB ASN B 75 3068 2224 3136 -161 303 218 C ATOM 2373 CG ASN B 75 39.085 0.910 12.670 1.00 26.75 C ANISOU 2373 CG ASN B 75 3647 2677 3840 -157 400 180 C ATOM 2374 OD1 ASN B 75 38.253 -0.004 12.744 1.00 26.60 O ANISOU 2374 OD1 ASN B 75 3624 2579 3903 -195 438 141 O ATOM 2375 ND2 ASN B 75 40.322 0.715 12.219 1.00 25.47 N ANISOU 2375 ND2 ASN B 75 3484 2486 3708 -113 453 190 N ATOM 2376 N PHE B 76 37.750 2.722 16.643 1.00 27.33 N ANISOU 2376 N PHE B 76 3645 2973 3767 -142 243 460 N ATOM 2377 CA PHE B 76 38.348 2.947 17.957 1.00 26.34 C ANISOU 2377 CA PHE B 76 3486 2919 3603 -110 226 577 C ATOM 2378 C PHE B 76 37.771 1.995 19.008 1.00 25.63 C ANISOU 2378 C PHE B 76 3365 2806 3567 -103 269 675 C ATOM 2379 O PHE B 76 36.568 1.760 19.029 1.00 25.20 O ANISOU 2379 O PHE B 76 3317 2722 3537 -139 285 640 O ATOM 2380 CB PHE B 76 38.116 4.411 18.359 1.00 25.82 C ANISOU 2380 CB PHE B 76 3433 2962 3417 -129 158 544 C ATOM 2381 CG PHE B 76 38.765 4.815 19.656 1.00 26.49 C ANISOU 2381 CG PHE B 76 3486 3150 3430 -114 130 627 C ATOM 2382 CD1 PHE B 76 38.126 4.589 20.871 1.00 25.81 C ANISOU 2382 CD1 PHE B 76 3380 3119 3306 -117 137 691 C ATOM 2383 CD2 PHE B 76 39.996 5.456 19.657 1.00 26.46 C ANISOU 2383 CD2 PHE B 76 3465 3201 3386 -107 95 635 C ATOM 2384 CE1 PHE B 76 38.713 4.975 22.064 1.00 26.40 C ANISOU 2384 CE1 PHE B 76 3425 3320 3286 -112 104 756 C ATOM 2385 CE2 PHE B 76 40.590 5.845 20.850 1.00 26.80 C ANISOU 2385 CE2 PHE B 76 3470 3364 3349 -109 56 694 C ATOM 2386 CZ PHE B 76 39.946 5.602 22.055 1.00 25.97 C ANISOU 2386 CZ PHE B 76 3351 3330 3187 -112 58 751 C ATOM 2387 N PRO B 77 38.628 1.451 19.892 1.00 25.55 N ANISOU 2387 N PRO B 77 3312 2819 3577 -55 288 813 N ATOM 2388 CA PRO B 77 40.085 1.632 19.937 1.00 27.88 C ANISOU 2388 CA PRO B 77 3575 3161 3856 -11 268 872 C ATOM 2389 C PRO B 77 40.890 0.521 19.256 1.00 29.15 C ANISOU 2389 C PRO B 77 3716 3196 4162 36 344 909 C ATOM 2390 O PRO B 77 42.113 0.632 19.160 1.00 31.74 O ANISOU 2390 O PRO B 77 4008 3556 4496 78 335 957 O ATOM 2391 CB PRO B 77 40.372 1.630 21.437 1.00 27.94 C ANISOU 2391 CB PRO B 77 3530 3294 3790 14 240 1018 C ATOM 2392 CG PRO B 77 39.368 0.651 21.975 1.00 27.37 C ANISOU 2392 CG PRO B 77 3454 3159 3786 16 305 1092 C ATOM 2393 CD PRO B 77 38.120 0.843 21.137 1.00 27.02 C ANISOU 2393 CD PRO B 77 3464 3032 3770 -43 318 940 C ATOM 2394 N GLN B 78 40.212 -0.522 18.790 1.00 27.77 N ANISOU 2394 N GLN B 78 3560 2877 4114 26 424 879 N ATOM 2395 CA GLN B 78 40.877 -1.757 18.382 1.00 32.85 C ANISOU 2395 CA GLN B 78 4181 3376 4925 76 525 926 C ATOM 2396 C GLN B 78 41.747 -1.623 17.134 1.00 31.71 C ANISOU 2396 C GLN B 78 4056 3187 4805 89 548 822 C ATOM 2397 O GLN B 78 42.758 -2.309 17.004 1.00 32.10 O ANISOU 2397 O GLN B 78 4066 3167 4964 155 617 893 O ATOM 2398 CB GLN B 78 39.837 -2.859 18.154 1.00 35.22 C ANISOU 2398 CB GLN B 78 4500 3517 5364 41 614 886 C ATOM 2399 CG GLN B 78 38.922 -3.118 19.341 1.00 39.72 C ANISOU 2399 CG GLN B 78 5046 4115 5930 28 616 999 C ATOM 2400 CD GLN B 78 37.651 -2.269 19.321 1.00 45.33 C ANISOU 2400 CD GLN B 78 5790 4907 6524 -51 548 887 C ATOM 2401 OE1 GLN B 78 37.585 -1.220 18.667 1.00 43.11 O ANISOU 2401 OE1 GLN B 78 5545 4706 6131 -82 473 763 O ATOM 2402 NE2 GLN B 78 36.629 -2.731 20.038 1.00 49.32 N ANISOU 2402 NE2 GLN B 78 6279 5391 7070 -78 583 945 N ATOM 2403 N GLY B 79 41.357 -0.745 16.218 1.00 30.67 N ANISOU 2403 N GLY B 79 3979 3099 4575 32 498 668 N ATOM 2404 CA GLY B 79 42.059 -0.620 14.953 1.00 30.42 C ANISOU 2404 CA GLY B 79 3973 3036 4549 36 529 564 C ATOM 2405 C GLY B 79 41.947 -1.876 14.105 1.00 33.40 C ANISOU 2405 C GLY B 79 4372 3247 5071 34 646 478 C ATOM 2406 O GLY B 79 42.945 -2.355 13.555 1.00 33.12 O ANISOU 2406 O GLY B 79 4323 3143 5116 83 726 474 O ATOM 2407 N ASN B 80 40.733 -2.417 14.006 1.00 30.76 N ANISOU 2407 N ASN B 80 4065 2843 4779 -28 666 401 N ATOM 2408 CA ASN B 80 40.482 -3.576 13.156 1.00 33.12 C ANISOU 2408 CA ASN B 80 4390 2979 5214 -59 777 278 C ATOM 2409 C ASN B 80 40.724 -3.237 11.690 1.00 32.70 C ANISOU 2409 C ASN B 80 4388 2955 5081 -92 784 99 C ATOM 2410 O ASN B 80 40.853 -2.067 11.330 1.00 30.52 O ANISOU 2410 O ASN B 80 4129 2823 4644 -99 694 80 O ATOM 2411 CB ASN B 80 39.058 -4.096 13.352 1.00 36.02 C ANISOU 2411 CB ASN B 80 4766 3288 5632 -140 782 220 C ATOM 2412 CG ASN B 80 38.819 -4.608 14.757 1.00 38.70 C ANISOU 2412 CG ASN B 80 5055 3585 6064 -105 806 406 C ATOM 2413 OD1 ASN B 80 39.726 -5.149 15.394 1.00 40.35 O ANISOU 2413 OD1 ASN B 80 5222 3735 6373 -19 868 561 O ATOM 2414 ND2 ASN B 80 37.602 -4.433 15.252 1.00 36.29 N ANISOU 2414 ND2 ASN B 80 4744 3320 5723 -166 759 404 N ATOM 2415 N ASP B 81 40.795 -4.263 10.850 1.00 33.19 N ANISOU 2415 N ASP B 81 4475 2879 5257 -113 899 -30 N ATOM 2416 CA ASP B 81 41.148 -4.065 9.452 1.00 35.27 C ANISOU 2416 CA ASP B 81 4787 3177 5437 -139 925 -200 C ATOM 2417 C ASP B 81 39.936 -4.132 8.527 1.00 37.77 C ANISOU 2417 C ASP B 81 5149 3528 5674 -256 893 -404 C ATOM 2418 O ASP B 81 40.073 -4.452 7.343 1.00 38.97 O ANISOU 2418 O ASP B 81 5343 3671 5794 -295 952 -580 O ATOM 2419 CB ASP B 81 42.197 -5.098 9.017 1.00 38.92 C ANISOU 2419 CB ASP B 81 5245 3480 6061 -80 1088 -232 C ATOM 2420 CG ASP B 81 41.704 -6.530 9.145 1.00 42.04 C ANISOU 2420 CG ASP B 81 5640 3660 6672 -111 1214 -295 C ATOM 2421 OD1 ASP B 81 40.677 -6.760 9.818 1.00 42.00 O ANISOU 2421 OD1 ASP B 81 5622 3627 6708 -163 1175 -263 O ATOM 2422 OD2 ASP B 81 42.356 -7.428 8.577 1.00 44.92 O ANISOU 2422 OD2 ASP B 81 6016 3875 7179 -82 1365 -376 O ATOM 2423 N ASP B 82 38.754 -3.831 9.060 1.00 33.47 N ANISOU 2423 N ASP B 82 4589 3039 5088 -313 800 -383 N ATOM 2424 CA ASP B 82 37.551 -3.799 8.238 1.00 32.48 C ANISOU 2424 CA ASP B 82 4485 2981 4877 -425 746 -558 C ATOM 2425 C ASP B 82 37.332 -2.386 7.703 1.00 31.37 C ANISOU 2425 C ASP B 82 4357 3054 4510 -429 615 -557 C ATOM 2426 O ASP B 82 36.914 -1.483 8.434 1.00 30.80 O ANISOU 2426 O ASP B 82 4259 3071 4373 -408 519 -437 O ATOM 2427 CB ASP B 82 36.331 -4.274 9.027 1.00 35.08 C ANISOU 2427 CB ASP B 82 4775 3253 5301 -487 727 -538 C ATOM 2428 CG ASP B 82 35.136 -4.580 8.132 1.00 40.41 C ANISOU 2428 CG ASP B 82 5452 3967 5936 -618 695 -741 C ATOM 2429 OD1 ASP B 82 34.820 -3.768 7.238 1.00 43.04 O ANISOU 2429 OD1 ASP B 82 5799 4474 6079 -652 600 -825 O ATOM 2430 OD2 ASP B 82 34.502 -5.636 8.325 1.00 43.50 O ANISOU 2430 OD2 ASP B 82 5823 4219 6487 -691 765 -811 O ATOM 2431 N LEU B 83 37.617 -2.211 6.418 1.00 31.92 N ANISOU 2431 N LEU B 83 4466 3201 4462 -453 623 -690 N ATOM 2432 CA LEU B 83 37.537 -0.910 5.770 1.00 33.54 C ANISOU 2432 CA LEU B 83 4683 3601 4458 -445 519 -672 C ATOM 2433 C LEU B 83 36.101 -0.388 5.754 1.00 31.17 C ANISOU 2433 C LEU B 83 4354 3420 4068 -510 398 -690 C ATOM 2434 O LEU B 83 35.860 0.787 6.033 1.00 30.09 O ANISOU 2434 O LEU B 83 4201 3395 3838 -474 306 -576 O ATOM 2435 CB LEU B 83 38.104 -0.995 4.345 1.00 34.67 C ANISOU 2435 CB LEU B 83 4874 3810 4490 -462 570 -812 C ATOM 2436 CG LEU B 83 38.153 0.276 3.487 1.00 35.09 C ANISOU 2436 CG LEU B 83 4943 4066 4324 -447 487 -784 C ATOM 2437 CD1 LEU B 83 39.399 0.287 2.616 1.00 34.90 C ANISOU 2437 CD1 LEU B 83 4959 4057 4244 -405 581 -819 C ATOM 2438 CD2 LEU B 83 36.908 0.402 2.616 1.00 37.23 C ANISOU 2438 CD2 LEU B 83 5209 4491 4446 -538 396 -904 C ATOM 2439 N ASP B 84 35.153 -1.266 5.440 1.00 31.29 N ANISOU 2439 N ASP B 84 4354 3405 4127 -608 405 -835 N ATOM 2440 CA ASP B 84 33.752 -0.873 5.326 1.00 33.01 C ANISOU 2440 CA ASP B 84 4526 3749 4268 -678 291 -863 C ATOM 2441 C ASP B 84 33.198 -0.326 6.635 1.00 31.19 C ANISOU 2441 C ASP B 84 4247 3503 4099 -637 238 -696 C ATOM 2442 O ASP B 84 32.428 0.631 6.632 1.00 30.87 O ANISOU 2442 O ASP B 84 4172 3599 3958 -633 135 -639 O ATOM 2443 CB ASP B 84 32.901 -2.054 4.856 1.00 36.67 C ANISOU 2443 CB ASP B 84 4970 4164 4800 -805 320 -1059 C ATOM 2444 CG ASP B 84 33.168 -2.420 3.413 1.00 42.28 C ANISOU 2444 CG ASP B 84 5722 4950 5392 -868 347 -1262 C ATOM 2445 OD1 ASP B 84 33.536 -1.514 2.632 1.00 43.81 O ANISOU 2445 OD1 ASP B 84 5940 5312 5393 -828 292 -1237 O ATOM 2446 OD2 ASP B 84 33.012 -3.610 3.059 1.00 46.04 O ANISOU 2446 OD2 ASP B 84 6208 5317 5969 -961 431 -1447 O ATOM 2447 N ILE B 85 33.585 -0.940 7.748 1.00 31.69 N ANISOU 2447 N ILE B 85 4307 3408 4326 -603 315 -611 N ATOM 2448 CA ILE B 85 33.180 -0.457 9.065 1.00 29.70 C ANISOU 2448 CA ILE B 85 4017 3151 4118 -561 280 -453 C ATOM 2449 C ILE B 85 33.785 0.921 9.330 1.00 25.14 C ANISOU 2449 C ILE B 85 3455 2672 3427 -474 222 -327 C ATOM 2450 O ILE B 85 33.073 1.860 9.681 1.00 28.54 O ANISOU 2450 O ILE B 85 3856 3194 3793 -462 146 -265 O ATOM 2451 CB ILE B 85 33.610 -1.426 10.190 1.00 32.32 C ANISOU 2451 CB ILE B 85 4340 3310 4630 -533 380 -368 C ATOM 2452 CG1 ILE B 85 33.033 -2.828 9.959 1.00 33.32 C ANISOU 2452 CG1 ILE B 85 4452 3301 4908 -623 461 -490 C ATOM 2453 CG2 ILE B 85 33.222 -0.873 11.563 1.00 28.29 C ANISOU 2453 CG2 ILE B 85 3794 2827 4129 -490 345 -207 C ATOM 2454 CD1 ILE B 85 31.726 -3.082 10.614 1.00 34.18 C ANISOU 2454 CD1 ILE B 85 4500 3401 5086 -687 440 -472 C ATOM 2455 N ALA B 86 35.098 1.034 9.149 1.00 22.04 N ANISOU 2455 N ALA B 86 3100 2250 3023 -415 267 -296 N ATOM 2456 CA ALA B 86 35.813 2.279 9.427 1.00 24.20 C ANISOU 2456 CA ALA B 86 3384 2596 3214 -344 227 -184 C ATOM 2457 C ALA B 86 35.316 3.425 8.550 1.00 24.02 C ANISOU 2457 C ALA B 86 3366 2716 3044 -351 145 -203 C ATOM 2458 O ALA B 86 35.204 4.564 9.010 1.00 23.89 O ANISOU 2458 O ALA B 86 3340 2756 2982 -313 94 -111 O ATOM 2459 CB ALA B 86 37.325 2.086 9.240 1.00 24.97 C ANISOU 2459 CB ALA B 86 3507 2641 3338 -291 297 -159 C ATOM 2460 N LEU B 87 35.022 3.119 7.288 1.00 23.01 N ANISOU 2460 N LEU B 87 3251 2649 2841 -398 138 -321 N ATOM 2461 CA LEU B 87 34.492 4.114 6.366 1.00 22.22 C ANISOU 2461 CA LEU B 87 3147 2705 2592 -401 58 -321 C ATOM 2462 C LEU B 87 33.110 4.597 6.825 1.00 23.13 C ANISOU 2462 C LEU B 87 3203 2881 2703 -418 -24 -282 C ATOM 2463 O LEU B 87 32.845 5.800 6.856 1.00 21.89 O ANISOU 2463 O LEU B 87 3030 2801 2485 -371 -77 -187 O ATOM 2464 CB LEU B 87 34.413 3.546 4.945 1.00 26.28 C ANISOU 2464 CB LEU B 87 3681 3298 3008 -459 65 -467 C ATOM 2465 CG LEU B 87 33.907 4.491 3.853 1.00 28.27 C ANISOU 2465 CG LEU B 87 3921 3743 3078 -459 -19 -454 C ATOM 2466 CD1 LEU B 87 34.696 5.801 3.837 1.00 26.10 C ANISOU 2466 CD1 LEU B 87 3667 3503 2748 -371 -21 -305 C ATOM 2467 CD2 LEU B 87 33.963 3.813 2.490 1.00 30.80 C ANISOU 2467 CD2 LEU B 87 4266 4158 3280 -524 -3 -615 C ATOM 2468 N ALA B 88 32.238 3.659 7.191 1.00 24.49 N ANISOU 2468 N ALA B 88 3338 3008 2959 -482 -21 -350 N ATOM 2469 CA ALA B 88 30.882 4.020 7.592 1.00 25.62 C ANISOU 2469 CA ALA B 88 3411 3214 3110 -502 -89 -318 C ATOM 2470 C ALA B 88 30.914 4.910 8.840 1.00 25.69 C ANISOU 2470 C ALA B 88 3411 3186 3164 -429 -87 -178 C ATOM 2471 O ALA B 88 30.261 5.948 8.879 1.00 26.82 O ANISOU 2471 O ALA B 88 3519 3411 3262 -395 -143 -111 O ATOM 2472 CB ALA B 88 30.034 2.768 7.831 1.00 22.33 C ANISOU 2472 CB ALA B 88 2950 2735 2798 -594 -68 -417 C ATOM 2473 N GLU B 89 31.697 4.511 9.838 1.00 23.97 N ANISOU 2473 N GLU B 89 3223 2851 3034 -404 -20 -134 N ATOM 2474 CA GLU B 89 31.858 5.297 11.056 1.00 20.61 C ANISOU 2474 CA GLU B 89 2795 2404 2631 -347 -14 -23 C ATOM 2475 C GLU B 89 32.431 6.696 10.777 1.00 23.70 C ANISOU 2475 C GLU B 89 3213 2851 2941 -287 -43 38 C ATOM 2476 O GLU B 89 32.041 7.673 11.425 1.00 22.90 O ANISOU 2476 O GLU B 89 3095 2770 2837 -252 -59 100 O ATOM 2477 CB GLU B 89 32.755 4.558 12.055 1.00 21.08 C ANISOU 2477 CB GLU B 89 2876 2358 2774 -332 55 18 C ATOM 2478 CG GLU B 89 32.133 3.305 12.654 1.00 22.56 C ANISOU 2478 CG GLU B 89 3032 2468 3070 -378 101 3 C ATOM 2479 CD GLU B 89 33.037 2.624 13.675 1.00 30.19 C ANISOU 2479 CD GLU B 89 4011 3344 4116 -346 169 83 C ATOM 2480 OE1 GLU B 89 34.147 3.132 13.954 1.00 31.84 O ANISOU 2480 OE1 GLU B 89 4245 3564 4288 -293 171 141 O ATOM 2481 OE2 GLU B 89 32.630 1.575 14.210 1.00 31.90 O ANISOU 2481 OE2 GLU B 89 4203 3482 4437 -375 223 97 O ATOM 2482 N THR B 90 33.349 6.795 9.817 1.00 23.18 N ANISOU 2482 N THR B 90 3187 2802 2819 -277 -34 16 N ATOM 2483 CA THR B 90 33.947 8.091 9.489 1.00 23.18 C ANISOU 2483 CA THR B 90 3208 2841 2758 -226 -47 82 C ATOM 2484 C THR B 90 32.926 8.990 8.781 1.00 23.02 C ANISOU 2484 C THR B 90 3156 2920 2671 -212 -107 110 C ATOM 2485 O THR B 90 32.796 10.163 9.117 1.00 24.95 O ANISOU 2485 O THR B 90 3392 3167 2921 -165 -115 187 O ATOM 2486 CB THR B 90 35.218 7.929 8.625 1.00 24.70 C ANISOU 2486 CB THR B 90 3445 3031 2910 -219 -10 63 C ATOM 2487 OG1 THR B 90 36.200 7.187 9.361 1.00 24.37 O ANISOU 2487 OG1 THR B 90 3417 2898 2947 -216 47 63 O ATOM 2488 CG2 THR B 90 35.805 9.284 8.262 1.00 21.31 C ANISOU 2488 CG2 THR B 90 3032 2634 2432 -173 -14 141 C ATOM 2489 N ARG B 91 32.186 8.429 7.826 1.00 21.87 N ANISOU 2489 N ARG B 91 2984 2857 2468 -252 -147 46 N ATOM 2490 CA ARG B 91 31.105 9.157 7.168 1.00 23.62 C ANISOU 2490 CA ARG B 91 3151 3199 2624 -237 -216 87 C ATOM 2491 C ARG B 91 30.064 9.674 8.168 1.00 23.68 C ANISOU 2491 C ARG B 91 3100 3187 2708 -212 -231 144 C ATOM 2492 O ARG B 91 29.540 10.783 8.014 1.00 22.43 O ANISOU 2492 O ARG B 91 2907 3079 2537 -155 -258 233 O ATOM 2493 CB ARG B 91 30.417 8.271 6.124 1.00 26.62 C ANISOU 2493 CB ARG B 91 3498 3689 2928 -307 -266 -15 C ATOM 2494 CG ARG B 91 31.267 7.966 4.901 1.00 29.52 C ANISOU 2494 CG ARG B 91 3917 4117 3182 -326 -252 -76 C ATOM 2495 CD ARG B 91 30.554 6.998 3.968 1.00 30.77 C ANISOU 2495 CD ARG B 91 4043 4386 3263 -416 -298 -214 C ATOM 2496 NE ARG B 91 31.180 6.947 2.649 1.00 32.29 N ANISOU 2496 NE ARG B 91 4278 4689 3303 -428 -294 -265 N ATOM 2497 CZ ARG B 91 31.007 5.959 1.777 1.00 35.04 C ANISOU 2497 CZ ARG B 91 4629 5113 3572 -516 -301 -429 C ATOM 2498 NH1 ARG B 91 30.233 4.925 2.085 1.00 34.81 N ANISOU 2498 NH1 ARG B 91 4560 5043 3623 -607 -312 -556 N ATOM 2499 NH2 ARG B 91 31.615 5.999 0.598 1.00 37.04 N ANISOU 2499 NH2 ARG B 91 4925 5481 3667 -521 -288 -473 N ATOM 2500 N ALA B 92 29.766 8.866 9.185 1.00 21.17 N ANISOU 2500 N ALA B 92 2770 2795 2478 -249 -203 101 N ATOM 2501 CA ALA B 92 28.794 9.244 10.209 1.00 21.60 C ANISOU 2501 CA ALA B 92 2769 2832 2604 -229 -200 146 C ATOM 2502 C ALA B 92 29.328 10.376 11.083 1.00 24.08 C ANISOU 2502 C ALA B 92 3118 3083 2947 -163 -157 219 C ATOM 2503 O ALA B 92 28.622 11.353 11.360 1.00 25.18 O ANISOU 2503 O ALA B 92 3219 3237 3111 -114 -159 276 O ATOM 2504 CB ALA B 92 28.429 8.035 11.067 1.00 19.70 C ANISOU 2504 CB ALA B 92 2510 2531 2444 -288 -167 92 C ATOM 2505 N ALA B 93 30.578 10.234 11.512 1.00 22.87 N ANISOU 2505 N ALA B 93 3031 2859 2799 -165 -115 210 N ATOM 2506 CA ALA B 93 31.261 11.278 12.268 1.00 22.21 C ANISOU 2506 CA ALA B 93 2982 2723 2735 -123 -78 254 C ATOM 2507 C ALA B 93 31.190 12.627 11.539 1.00 25.37 C ANISOU 2507 C ALA B 93 3379 3144 3116 -69 -88 315 C ATOM 2508 O ALA B 93 30.878 13.658 12.140 1.00 28.98 O ANISOU 2508 O ALA B 93 3826 3565 3619 -30 -61 349 O ATOM 2509 CB ALA B 93 32.708 10.882 12.516 1.00 19.55 C ANISOU 2509 CB ALA B 93 2699 2337 2392 -139 -49 239 C ATOM 2510 N VAL B 94 31.472 12.617 10.243 1.00 23.31 N ANISOU 2510 N VAL B 94 3127 2940 2791 -66 -118 330 N ATOM 2511 CA VAL B 94 31.389 13.837 9.446 1.00 23.18 C ANISOU 2511 CA VAL B 94 3102 2952 2754 -9 -124 417 C ATOM 2512 C VAL B 94 29.947 14.362 9.426 1.00 25.68 C ANISOU 2512 C VAL B 94 3341 3317 3098 34 -153 471 C ATOM 2513 O VAL B 94 29.699 15.537 9.693 1.00 26.30 O ANISOU 2513 O VAL B 94 3406 3348 3238 95 -119 543 O ATOM 2514 CB VAL B 94 31.893 13.595 7.999 1.00 24.00 C ANISOU 2514 CB VAL B 94 3224 3141 2754 -16 -151 429 C ATOM 2515 CG1 VAL B 94 31.604 14.792 7.112 1.00 19.29 C ANISOU 2515 CG1 VAL B 94 2603 2599 2127 51 -161 551 C ATOM 2516 CG2 VAL B 94 33.387 13.266 8.001 1.00 21.25 C ANISOU 2516 CG2 VAL B 94 2941 2736 2398 -42 -105 393 C ATOM 2517 N ALA B 95 28.997 13.477 9.145 1.00 23.65 N ANISOU 2517 N ALA B 95 3028 3148 2811 -1 -207 432 N ATOM 2518 CA ALA B 95 27.592 13.867 9.066 1.00 25.66 C ANISOU 2518 CA ALA B 95 3187 3471 3093 36 -243 487 C ATOM 2519 C ALA B 95 27.059 14.414 10.396 1.00 28.28 C ANISOU 2519 C ALA B 95 3497 3711 3538 71 -183 499 C ATOM 2520 O ALA B 95 26.206 15.299 10.406 1.00 28.76 O ANISOU 2520 O ALA B 95 3492 3783 3651 141 -175 578 O ATOM 2521 CB ALA B 95 26.747 12.687 8.602 1.00 21.94 C ANISOU 2521 CB ALA B 95 2651 3110 2576 -33 -313 419 C ATOM 2522 N TYR B 96 27.555 13.880 11.510 1.00 28.08 N ANISOU 2522 N TYR B 96 3521 3603 3545 28 -135 424 N ATOM 2523 CA TYR B 96 27.217 14.393 12.840 1.00 24.89 C ANISOU 2523 CA TYR B 96 3112 3123 3220 53 -66 418 C ATOM 2524 C TYR B 96 27.651 15.854 13.014 1.00 26.61 C ANISOU 2524 C TYR B 96 3364 3260 3487 118 -9 464 C ATOM 2525 O TYR B 96 27.041 16.607 13.773 1.00 29.33 O ANISOU 2525 O TYR B 96 3683 3555 3907 162 51 472 O ATOM 2526 CB TYR B 96 27.886 13.551 13.922 1.00 22.88 C ANISOU 2526 CB TYR B 96 2911 2821 2960 -6 -32 344 C ATOM 2527 CG TYR B 96 27.095 12.375 14.454 1.00 23.36 C ANISOU 2527 CG TYR B 96 2925 2913 3038 -54 -36 310 C ATOM 2528 CD1 TYR B 96 25.802 12.530 14.956 1.00 23.76 C ANISOU 2528 CD1 TYR B 96 2897 2989 3143 -34 -16 327 C ATOM 2529 CD2 TYR B 96 27.664 11.108 14.488 1.00 24.27 C ANISOU 2529 CD2 TYR B 96 3070 3020 3131 -118 -46 267 C ATOM 2530 CE1 TYR B 96 25.092 11.437 15.460 1.00 22.58 C ANISOU 2530 CE1 TYR B 96 2698 2861 3020 -87 -9 303 C ATOM 2531 CE2 TYR B 96 26.972 10.020 14.981 1.00 23.09 C ANISOU 2531 CE2 TYR B 96 2877 2877 3018 -167 -35 245 C ATOM 2532 CZ TYR B 96 25.692 10.185 15.467 1.00 23.10 C ANISOU 2532 CZ TYR B 96 2800 2908 3068 -155 -17 263 C ATOM 2533 OH TYR B 96 25.029 9.084 15.962 1.00 23.34 O ANISOU 2533 OH TYR B 96 2783 2939 3146 -211 4 249 O ATOM 2534 N GLY B 97 28.724 16.231 12.327 1.00 22.88 N ANISOU 2534 N GLY B 97 2948 2765 2981 119 -13 486 N ATOM 2535 CA GLY B 97 29.258 17.579 12.397 1.00 22.73 C ANISOU 2535 CA GLY B 97 2962 2651 3024 166 49 528 C ATOM 2536 C GLY B 97 30.683 17.651 12.930 1.00 24.77 C ANISOU 2536 C GLY B 97 3300 2837 3275 115 84 465 C ATOM 2537 O GLY B 97 31.110 18.701 13.393 1.00 26.97 O ANISOU 2537 O GLY B 97 3606 3019 3622 128 149 457 O ATOM 2538 N ALA B 98 31.421 16.543 12.878 1.00 22.64 N ANISOU 2538 N ALA B 98 3059 2610 2932 55 46 417 N ATOM 2539 CA ALA B 98 32.796 16.532 13.383 1.00 23.97 C ANISOU 2539 CA ALA B 98 3282 2731 3093 9 69 370 C ATOM 2540 C ALA B 98 33.683 17.508 12.615 1.00 25.99 C ANISOU 2540 C ALA B 98 3564 2937 3372 24 96 420 C ATOM 2541 O ALA B 98 33.613 17.586 11.385 1.00 27.52 O ANISOU 2541 O ALA B 98 3750 3173 3535 55 75 494 O ATOM 2542 CB ALA B 98 33.387 15.128 13.309 1.00 22.91 C ANISOU 2542 CB ALA B 98 3161 2649 2895 -40 31 334 C ATOM 2543 N ASP B 99 34.509 18.254 13.343 1.00 23.11 N ANISOU 2543 N ASP B 99 3228 2494 3059 -4 145 380 N ATOM 2544 CA ASP B 99 35.538 19.072 12.714 1.00 25.05 C ANISOU 2544 CA ASP B 99 3496 2683 3341 -9 179 421 C ATOM 2545 C ASP B 99 36.769 18.221 12.422 1.00 24.77 C ANISOU 2545 C ASP B 99 3475 2694 3242 -56 151 405 C ATOM 2546 O ASP B 99 37.513 18.505 11.490 1.00 25.49 O ANISOU 2546 O ASP B 99 3574 2778 3331 -52 167 461 O ATOM 2547 CB ASP B 99 35.913 20.259 13.602 1.00 25.15 C ANISOU 2547 CB ASP B 99 3522 2582 3450 -35 249 366 C ATOM 2548 CG ASP B 99 34.739 21.182 13.856 1.00 31.15 C ANISOU 2548 CG ASP B 99 4266 3270 4297 24 302 381 C ATOM 2549 OD1 ASP B 99 34.098 21.620 12.876 1.00 34.76 O ANISOU 2549 OD1 ASP B 99 4701 3719 4788 97 311 495 O ATOM 2550 OD2 ASP B 99 34.452 21.459 15.036 1.00 31.03 O ANISOU 2550 OD2 ASP B 99 4258 3218 4315 0 339 284 O ATOM 2551 N GLU B 100 36.975 17.180 13.228 1.00 24.92 N ANISOU 2551 N GLU B 100 3492 2760 3217 -95 118 340 N ATOM 2552 CA GLU B 100 38.155 16.316 13.111 1.00 25.49 C ANISOU 2552 CA GLU B 100 3566 2869 3250 -130 101 329 C ATOM 2553 C GLU B 100 37.797 14.871 13.454 1.00 22.50 C ANISOU 2553 C GLU B 100 3178 2548 2823 -135 64 305 C ATOM 2554 O GLU B 100 36.999 14.619 14.346 1.00 24.91 O ANISOU 2554 O GLU B 100 3473 2864 3127 -137 55 277 O ATOM 2555 CB GLU B 100 39.292 16.811 14.025 1.00 26.55 C ANISOU 2555 CB GLU B 100 3695 2975 3417 -184 119 286 C ATOM 2556 CG GLU B 100 39.803 18.200 13.668 1.00 29.62 C ANISOU 2556 CG GLU B 100 4091 3284 3881 -196 169 302 C ATOM 2557 CD GLU B 100 40.722 18.805 14.710 1.00 34.02 C ANISOU 2557 CD GLU B 100 4634 3815 4477 -269 183 227 C ATOM 2558 OE1 GLU B 100 40.942 18.169 15.763 1.00 30.55 O ANISOU 2558 OE1 GLU B 100 4178 3443 3988 -305 145 172 O ATOM 2559 OE2 GLU B 100 41.228 19.927 14.465 1.00 37.31 O ANISOU 2559 OE2 GLU B 100 5052 4150 4975 -295 234 228 O ATOM 2560 N VAL B 101 38.388 13.925 12.736 1.00 22.30 N ANISOU 2560 N VAL B 101 3153 2551 2768 -136 56 316 N ATOM 2561 CA VAL B 101 38.187 12.518 13.030 1.00 20.66 C ANISOU 2561 CA VAL B 101 2937 2370 2544 -143 40 294 C ATOM 2562 C VAL B 101 39.527 11.858 13.335 1.00 23.27 C ANISOU 2562 C VAL B 101 3255 2700 2887 -157 53 301 C ATOM 2563 O VAL B 101 40.440 11.887 12.512 1.00 23.49 O ANISOU 2563 O VAL B 101 3285 2725 2915 -153 75 316 O ATOM 2564 CB VAL B 101 37.493 11.775 11.860 1.00 19.72 C ANISOU 2564 CB VAL B 101 2823 2278 2392 -131 29 285 C ATOM 2565 CG1 VAL B 101 37.350 10.282 12.176 1.00 19.67 C ANISOU 2565 CG1 VAL B 101 2808 2267 2400 -148 31 252 C ATOM 2566 CG2 VAL B 101 36.137 12.402 11.551 1.00 20.03 C ANISOU 2566 CG2 VAL B 101 2852 2341 2418 -112 5 296 C ATOM 2567 N ASP B 102 39.635 11.277 14.526 1.00 23.16 N ANISOU 2567 N ASP B 102 3218 2699 2881 -169 44 303 N ATOM 2568 CA ASP B 102 40.812 10.511 14.910 1.00 24.24 C ANISOU 2568 CA ASP B 102 3326 2849 3036 -170 52 333 C ATOM 2569 C ASP B 102 40.583 9.022 14.595 1.00 23.70 C ANISOU 2569 C ASP B 102 3255 2755 2995 -150 74 342 C ATOM 2570 O ASP B 102 39.942 8.294 15.363 1.00 19.55 O ANISOU 2570 O ASP B 102 2718 2228 2481 -149 72 356 O ATOM 2571 CB ASP B 102 41.137 10.711 16.399 1.00 22.78 C ANISOU 2571 CB ASP B 102 3108 2713 2833 -192 27 347 C ATOM 2572 CG ASP B 102 41.563 12.140 16.730 1.00 26.99 C ANISOU 2572 CG ASP B 102 3640 3260 3355 -230 16 312 C ATOM 2573 OD1 ASP B 102 41.227 13.075 15.968 1.00 29.91 O ANISOU 2573 OD1 ASP B 102 4040 3582 3741 -230 33 287 O ATOM 2574 OD2 ASP B 102 42.224 12.332 17.774 1.00 26.73 O ANISOU 2574 OD2 ASP B 102 3571 3287 3296 -262 -8 309 O ATOM 2575 N LEU B 103 41.100 8.589 13.449 1.00 21.79 N ANISOU 2575 N LEU B 103 3024 2487 2769 -135 107 330 N ATOM 2576 CA LEU B 103 40.932 7.215 12.982 1.00 25.43 C ANISOU 2576 CA LEU B 103 3488 2902 3270 -124 146 310 C ATOM 2577 C LEU B 103 42.033 6.308 13.531 1.00 23.76 C ANISOU 2577 C LEU B 103 3234 2665 3127 -95 183 369 C ATOM 2578 O LEU B 103 43.204 6.685 13.519 1.00 24.55 O ANISOU 2578 O LEU B 103 3306 2789 3235 -82 190 406 O ATOM 2579 CB LEU B 103 40.936 7.179 11.449 1.00 25.89 C ANISOU 2579 CB LEU B 103 3581 2957 3299 -125 173 250 C ATOM 2580 CG LEU B 103 41.068 5.819 10.758 1.00 26.21 C ANISOU 2580 CG LEU B 103 3631 2943 3385 -120 235 197 C ATOM 2581 CD1 LEU B 103 39.757 5.024 10.850 1.00 23.53 C ANISOU 2581 CD1 LEU B 103 3300 2575 3065 -152 226 141 C ATOM 2582 CD2 LEU B 103 41.497 6.000 9.309 1.00 21.59 C ANISOU 2582 CD2 LEU B 103 3076 2384 2742 -119 270 142 C ATOM 2583 N VAL B 104 41.679 5.122 14.017 1.00 21.30 N ANISOU 2583 N VAL B 104 2910 2304 2879 -84 212 390 N ATOM 2584 CA VAL B 104 42.730 4.191 14.421 1.00 23.87 C ANISOU 2584 CA VAL B 104 3187 2594 3288 -40 259 468 C ATOM 2585 C VAL B 104 43.176 3.355 13.215 1.00 23.54 C ANISOU 2585 C VAL B 104 3161 2468 3313 -20 343 411 C ATOM 2586 O VAL B 104 42.378 2.655 12.588 1.00 22.97 O ANISOU 2586 O VAL B 104 3127 2331 3269 -41 380 329 O ATOM 2587 CB VAL B 104 42.303 3.247 15.583 1.00 23.82 C ANISOU 2587 CB VAL B 104 3149 2562 3339 -24 271 551 C ATOM 2588 CG1 VAL B 104 43.511 2.454 16.085 1.00 18.70 C ANISOU 2588 CG1 VAL B 104 2432 1897 2775 38 313 669 C ATOM 2589 CG2 VAL B 104 41.706 4.036 16.732 1.00 23.19 C ANISOU 2589 CG2 VAL B 104 3062 2576 3172 -49 201 584 C ATOM 2590 N PHE B 105 44.460 3.479 12.892 1.00 21.88 N ANISOU 2590 N PHE B 105 2919 2269 3127 15 374 445 N ATOM 2591 CA PHE B 105 45.129 2.699 11.857 1.00 26.15 C ANISOU 2591 CA PHE B 105 3464 2736 3737 47 472 400 C ATOM 2592 C PHE B 105 45.054 1.201 12.163 1.00 27.68 C ANISOU 2592 C PHE B 105 3639 2808 4069 83 554 424 C ATOM 2593 O PHE B 105 45.124 0.809 13.327 1.00 30.04 O ANISOU 2593 O PHE B 105 3887 3104 4424 113 539 542 O ATOM 2594 CB PHE B 105 46.589 3.157 11.767 1.00 28.14 C ANISOU 2594 CB PHE B 105 3656 3032 4002 85 489 466 C ATOM 2595 CG PHE B 105 47.315 2.700 10.542 1.00 28.35 C ANISOU 2595 CG PHE B 105 3694 3008 4071 114 595 406 C ATOM 2596 CD1 PHE B 105 47.194 3.397 9.347 1.00 27.09 C ANISOU 2596 CD1 PHE B 105 3591 2891 3812 81 604 314 C ATOM 2597 CD2 PHE B 105 48.164 1.605 10.595 1.00 27.93 C ANISOU 2597 CD2 PHE B 105 3587 2871 4155 182 694 454 C ATOM 2598 CE1 PHE B 105 47.888 2.990 8.219 1.00 28.73 C ANISOU 2598 CE1 PHE B 105 3809 3069 4038 107 712 255 C ATOM 2599 CE2 PHE B 105 48.862 1.194 9.471 1.00 29.04 C ANISOU 2599 CE2 PHE B 105 3736 2962 4336 213 808 387 C ATOM 2600 CZ PHE B 105 48.723 1.882 8.283 1.00 29.10 C ANISOU 2600 CZ PHE B 105 3807 3025 4225 171 818 280 C ATOM 2601 N PRO B 106 44.898 0.359 11.125 1.00 27.35 N ANISOU 2601 N PRO B 106 3638 2669 4083 78 648 311 N ATOM 2602 CA PRO B 106 44.953 -1.096 11.345 1.00 28.66 C ANISOU 2602 CA PRO B 106 3785 2685 4419 115 755 329 C ATOM 2603 C PRO B 106 46.385 -1.582 11.583 1.00 27.88 C ANISOU 2603 C PRO B 106 3610 2542 4440 209 834 445 C ATOM 2604 O PRO B 106 46.994 -2.190 10.701 1.00 28.34 O ANISOU 2604 O PRO B 106 3675 2515 4580 241 950 376 O ATOM 2605 CB PRO B 106 44.380 -1.674 10.047 1.00 28.17 C ANISOU 2605 CB PRO B 106 3795 2546 4363 64 830 135 C ATOM 2606 CG PRO B 106 44.585 -0.605 9.025 1.00 23.48 C ANISOU 2606 CG PRO B 106 3238 2075 3607 37 787 54 C ATOM 2607 CD PRO B 106 44.515 0.705 9.745 1.00 24.31 C ANISOU 2607 CD PRO B 106 3322 2311 3602 30 660 157 C ATOM 2608 N TYR B 107 46.912 -1.313 12.772 1.00 27.72 N ANISOU 2608 N TYR B 107 3511 2594 4428 253 772 618 N ATOM 2609 CA TYR B 107 48.317 -1.571 13.050 1.00 28.71 C ANISOU 2609 CA TYR B 107 3539 2724 4646 342 819 750 C ATOM 2610 C TYR B 107 48.631 -3.067 13.154 1.00 33.12 C ANISOU 2610 C TYR B 107 4058 3110 5416 424 959 817 C ATOM 2611 O TYR B 107 49.727 -3.492 12.782 1.00 35.74 O ANISOU 2611 O TYR B 107 4331 3391 5858 502 1054 858 O ATOM 2612 CB TYR B 107 48.758 -0.839 14.325 1.00 25.52 C ANISOU 2612 CB TYR B 107 3052 2476 4170 354 698 911 C ATOM 2613 CG TYR B 107 47.953 -1.169 15.566 1.00 29.10 C ANISOU 2613 CG TYR B 107 3495 2948 4616 348 645 1011 C ATOM 2614 CD1 TYR B 107 46.815 -0.440 15.894 1.00 29.08 C ANISOU 2614 CD1 TYR B 107 3557 3012 4479 267 554 943 C ATOM 2615 CD2 TYR B 107 48.340 -2.194 16.417 1.00 31.24 C ANISOU 2615 CD2 TYR B 107 3685 3172 5014 432 694 1188 C ATOM 2616 CE1 TYR B 107 46.084 -0.729 17.026 1.00 31.20 C ANISOU 2616 CE1 TYR B 107 3814 3307 4733 262 518 1035 C ATOM 2617 CE2 TYR B 107 47.613 -2.494 17.553 1.00 32.19 C ANISOU 2617 CE2 TYR B 107 3794 3321 5116 429 654 1296 C ATOM 2618 CZ TYR B 107 46.486 -1.759 17.852 1.00 32.81 C ANISOU 2618 CZ TYR B 107 3942 3472 5051 340 568 1212 C ATOM 2619 OH TYR B 107 45.761 -2.051 18.981 1.00 31.95 O ANISOU 2619 OH TYR B 107 3821 3401 4917 338 541 1319 O ATOM 2620 N ARG B 108 47.686 -3.868 13.640 1.00 31.41 N ANISOU 2620 N ARG B 108 3869 2793 5274 411 986 831 N ATOM 2621 CA ARG B 108 47.920 -5.312 13.721 1.00 34.24 C ANISOU 2621 CA ARG B 108 4193 2954 5862 487 1138 895 C ATOM 2622 C ARG B 108 48.096 -5.904 12.326 1.00 34.46 C ANISOU 2622 C ARG B 108 4279 2832 5982 481 1284 702 C ATOM 2623 O ARG B 108 48.910 -6.804 12.124 1.00 36.14 O ANISOU 2623 O ARG B 108 4444 2906 6383 571 1428 748 O ATOM 2624 CB ARG B 108 46.780 -6.025 14.459 1.00 35.74 C ANISOU 2624 CB ARG B 108 4405 3053 6121 458 1149 938 C ATOM 2625 CG ARG B 108 46.802 -5.824 15.966 1.00 40.78 C ANISOU 2625 CG ARG B 108 4967 3814 6715 497 1055 1173 C ATOM 2626 CD ARG B 108 45.755 -6.682 16.677 1.00 47.89 C ANISOU 2626 CD ARG B 108 5880 4605 7712 481 1099 1241 C ATOM 2627 NE ARG B 108 44.433 -6.593 16.056 1.00 50.68 N ANISOU 2627 NE ARG B 108 6333 4904 8019 362 1092 1031 N ATOM 2628 CZ ARG B 108 43.547 -5.637 16.316 1.00 48.57 C ANISOU 2628 CZ ARG B 108 6106 4783 7566 279 964 972 C ATOM 2629 NH1 ARG B 108 43.837 -4.681 17.186 1.00 47.54 N ANISOU 2629 NH1 ARG B 108 5936 4849 7277 294 840 1087 N ATOM 2630 NH2 ARG B 108 42.371 -5.636 15.704 1.00 47.90 N ANISOU 2630 NH2 ARG B 108 6093 4650 7458 178 962 794 N ATOM 2631 N ALA B 109 47.337 -5.385 11.366 1.00 33.50 N ANISOU 2631 N ALA B 109 4256 2749 5723 378 1249 487 N ATOM 2632 CA ALA B 109 47.469 -5.808 9.978 1.00 35.27 C ANISOU 2632 CA ALA B 109 4543 2879 5978 355 1372 279 C ATOM 2633 C ALA B 109 48.853 -5.434 9.428 1.00 36.97 C ANISOU 2633 C ALA B 109 4712 3149 6185 428 1423 307 C ATOM 2634 O ALA B 109 49.485 -6.219 8.714 1.00 38.30 O ANISOU 2634 O ALA B 109 4878 3188 6486 479 1586 234 O ATOM 2635 CB ALA B 109 46.366 -5.188 9.130 1.00 33.89 C ANISOU 2635 CB ALA B 109 4468 2790 5617 229 1294 73 C ATOM 2636 N LEU B 110 49.324 -4.236 9.772 1.00 34.29 N ANISOU 2636 N LEU B 110 4331 2996 5701 431 1295 407 N ATOM 2637 CA LEU B 110 50.639 -3.785 9.332 1.00 32.74 C ANISOU 2637 CA LEU B 110 4074 2867 5499 491 1333 450 C ATOM 2638 C LEU B 110 51.727 -4.681 9.891 1.00 34.12 C ANISOU 2638 C LEU B 110 4132 2943 5890 619 1441 617 C ATOM 2639 O LEU B 110 52.644 -5.076 9.175 1.00 36.37 O ANISOU 2639 O LEU B 110 4384 3162 6272 684 1578 586 O ATOM 2640 CB LEU B 110 50.901 -2.338 9.755 1.00 31.89 C ANISOU 2640 CB LEU B 110 3932 2963 5221 457 1173 534 C ATOM 2641 CG LEU B 110 52.304 -1.826 9.414 1.00 33.42 C ANISOU 2641 CG LEU B 110 4042 3233 5425 510 1208 599 C ATOM 2642 CD1 LEU B 110 52.558 -1.929 7.918 1.00 34.50 C ANISOU 2642 CD1 LEU B 110 4242 3329 5536 503 1336 431 C ATOM 2643 CD2 LEU B 110 52.515 -0.398 9.904 1.00 33.77 C ANISOU 2643 CD2 LEU B 110 4050 3459 5323 459 1053 671 C ATOM 2644 N ILE B 111 51.617 -4.988 11.179 1.00 34.80 N ANISOU 2644 N ILE B 111 4148 3029 6047 660 1380 804 N ATOM 2645 CA ILE B 111 52.567 -5.866 11.855 1.00 38.77 C ANISOU 2645 CA ILE B 111 4522 3451 6757 792 1468 1008 C ATOM 2646 C ILE B 111 52.594 -7.239 11.182 1.00 41.87 C ANISOU 2646 C ILE B 111 4944 3589 7377 850 1685 923 C ATOM 2647 O ILE B 111 53.644 -7.881 11.102 1.00 45.60 O ANISOU 2647 O ILE B 111 5322 3972 8032 970 1817 1020 O ATOM 2648 CB ILE B 111 52.216 -6.006 13.357 1.00 38.70 C ANISOU 2648 CB ILE B 111 4449 3499 6757 815 1363 1222 C ATOM 2649 CG1 ILE B 111 52.374 -4.657 14.065 1.00 35.06 C ANISOU 2649 CG1 ILE B 111 3946 3293 6082 762 1164 1296 C ATOM 2650 CG2 ILE B 111 53.077 -7.066 14.033 1.00 40.44 C ANISOU 2650 CG2 ILE B 111 4535 3624 7205 964 1465 1454 C ATOM 2651 CD1 ILE B 111 51.876 -4.659 15.500 1.00 35.86 C ANISOU 2651 CD1 ILE B 111 4004 3486 6134 761 1050 1468 C ATOM 2652 N GLN B 112 51.440 -7.668 10.674 1.00 39.66 N ANISOU 2652 N GLN B 112 4787 3191 7092 762 1727 732 N ATOM 2653 CA GLN B 112 51.319 -8.952 9.993 1.00 42.30 C ANISOU 2653 CA GLN B 112 5165 3270 7638 786 1937 602 C ATOM 2654 C GLN B 112 51.816 -8.888 8.545 1.00 43.41 C ANISOU 2654 C GLN B 112 5361 3388 7745 771 2056 378 C ATOM 2655 O GLN B 112 51.818 -9.896 7.843 1.00 47.08 O ANISOU 2655 O GLN B 112 5861 3700 8327 758 2214 232 O ATOM 2656 CB GLN B 112 49.865 -9.442 10.032 1.00 41.00 C ANISOU 2656 CB GLN B 112 5099 3004 7477 675 1928 470 C ATOM 2657 N GLY B 113 52.231 -7.705 8.100 1.00 41.40 N ANISOU 2657 N GLY B 113 5109 3341 7280 739 1955 350 N ATOM 2658 CA GLY B 113 52.821 -7.558 6.780 1.00 41.95 C ANISOU 2658 CA GLY B 113 5218 3423 7298 736 2068 175 C ATOM 2659 C GLY B 113 51.917 -6.925 5.736 1.00 44.69 C ANISOU 2659 C GLY B 113 5700 3873 7405 597 2008 -69 C ATOM 2660 O GLY B 113 52.325 -6.745 4.587 1.00 42.81 O ANISOU 2660 O GLY B 113 5505 3675 7084 584 2095 -220 O ATOM 2661 N ASN B 114 50.692 -6.582 6.130 1.00 44.48 N ANISOU 2661 N ASN B 114 5734 3905 7263 498 1860 -98 N ATOM 2662 CA ASN B 114 49.740 -5.971 5.207 1.00 43.76 C ANISOU 2662 CA ASN B 114 5755 3930 6944 370 1785 -303 C ATOM 2663 C ASN B 114 49.806 -4.448 5.270 1.00 41.41 C ANISOU 2663 C ASN B 114 5448 3864 6421 340 1613 -218 C ATOM 2664 O ASN B 114 49.307 -3.832 6.214 1.00 40.91 O ANISOU 2664 O ASN B 114 5363 3878 6304 317 1460 -94 O ATOM 2665 CB ASN B 114 48.314 -6.451 5.507 1.00 44.81 C ANISOU 2665 CB ASN B 114 5946 3992 7086 275 1731 -393 C ATOM 2666 CG ASN B 114 47.326 -6.116 4.391 1.00 46.28 C ANISOU 2666 CG ASN B 114 6238 4280 7068 146 1684 -634 C ATOM 2667 OD1 ASN B 114 47.593 -5.274 3.529 1.00 45.52 O ANISOU 2667 OD1 ASN B 114 6172 4344 6778 126 1651 -694 O ATOM 2668 ND2 ASN B 114 46.173 -6.775 4.410 1.00 47.73 N ANISOU 2668 ND2 ASN B 114 6465 4377 7292 56 1679 -760 N ATOM 2669 N GLU B 115 50.415 -3.846 4.254 1.00 41.45 N ANISOU 2669 N GLU B 115 5474 3974 6302 339 1652 -287 N ATOM 2670 CA GLU B 115 50.560 -2.395 4.197 1.00 41.51 C ANISOU 2670 CA GLU B 115 5473 4178 6120 311 1518 -207 C ATOM 2671 C GLU B 115 49.388 -1.738 3.472 1.00 35.98 C ANISOU 2671 C GLU B 115 4873 3599 5199 203 1419 -342 C ATOM 2672 O GLU B 115 48.972 -0.632 3.813 1.00 33.12 O ANISOU 2672 O GLU B 115 4511 3362 4712 167 1272 -260 O ATOM 2673 CB GLU B 115 51.873 -2.028 3.507 1.00 49.24 C ANISOU 2673 CB GLU B 115 6407 5213 7089 371 1617 -178 C ATOM 2674 CG GLU B 115 53.066 -2.814 4.017 1.00 59.09 C ANISOU 2674 CG GLU B 115 7544 6339 8568 487 1741 -62 C ATOM 2675 CD GLU B 115 54.348 -2.457 3.291 1.00 68.18 C ANISOU 2675 CD GLU B 115 8640 7549 9716 543 1850 -38 C ATOM 2676 OE1 GLU B 115 54.261 -1.874 2.189 1.00 71.99 O ANISOU 2676 OE1 GLU B 115 9194 8136 10023 492 1873 -153 O ATOM 2677 OE2 GLU B 115 55.440 -2.753 3.823 1.00 70.42 O ANISOU 2677 OE2 GLU B 115 8801 7787 10170 641 1913 108 O ATOM 2678 N THR B 116 48.860 -2.442 2.476 1.00 35.63 N ANISOU 2678 N THR B 116 4907 3519 5113 153 1505 -551 N ATOM 2679 CA THR B 116 47.813 -1.921 1.602 1.00 33.86 C ANISOU 2679 CA THR B 116 4766 3434 4666 53 1423 -689 C ATOM 2680 C THR B 116 46.497 -1.581 2.324 1.00 31.14 C ANISOU 2680 C THR B 116 4432 3124 4276 -14 1257 -656 C ATOM 2681 O THR B 116 45.870 -0.565 2.018 1.00 31.84 O ANISOU 2681 O THR B 116 4545 3370 4181 -61 1135 -643 O ATOM 2682 CB THR B 116 47.512 -2.926 0.464 1.00 36.17 C ANISOU 2682 CB THR B 116 5131 3679 4933 0 1553 -945 C ATOM 2683 OG1 THR B 116 48.719 -3.233 -0.242 1.00 37.00 O ANISOU 2683 OG1 THR B 116 5228 3754 5075 66 1725 -987 O ATOM 2684 CG2 THR B 116 46.497 -2.353 -0.513 1.00 39.77 C ANISOU 2684 CG2 THR B 116 5657 4325 5128 -102 1457 -1079 C ATOM 2685 N ILE B 117 46.075 -2.414 3.274 1.00 30.33 N ANISOU 2685 N ILE B 117 4303 2874 4344 -12 1260 -631 N ATOM 2686 CA ILE B 117 44.787 -2.188 3.943 1.00 31.07 C ANISOU 2686 CA ILE B 117 4403 2996 4405 -76 1122 -609 C ATOM 2687 C ILE B 117 44.823 -0.897 4.758 1.00 28.84 C ANISOU 2687 C ILE B 117 4082 2829 4046 -51 982 -422 C ATOM 2688 O ILE B 117 43.837 -0.162 4.814 1.00 29.12 O ANISOU 2688 O ILE B 117 4136 2968 3961 -105 859 -421 O ATOM 2689 CB ILE B 117 44.377 -3.384 4.856 1.00 38.22 C ANISOU 2689 CB ILE B 117 5284 3712 5525 -75 1174 -599 C ATOM 2690 CG1 ILE B 117 43.027 -3.121 5.534 1.00 40.36 C ANISOU 2690 CG1 ILE B 117 5554 4023 5757 -144 1040 -574 C ATOM 2691 CG2 ILE B 117 45.438 -3.662 5.912 1.00 37.49 C ANISOU 2691 CG2 ILE B 117 5115 3519 5609 35 1226 -402 C ATOM 2692 CD1 ILE B 117 41.869 -2.879 4.575 1.00 39.84 C ANISOU 2692 CD1 ILE B 117 5540 4072 5525 -254 971 -751 C ATOM 2693 N GLY B 118 45.968 -0.608 5.367 1.00 29.31 N ANISOU 2693 N GLY B 118 4081 2873 4180 29 1004 -270 N ATOM 2694 CA GLY B 118 46.123 0.614 6.135 1.00 29.63 C ANISOU 2694 CA GLY B 118 4083 3017 4158 42 884 -116 C ATOM 2695 C GLY B 118 46.103 1.841 5.246 1.00 28.92 C ANISOU 2695 C GLY B 118 4028 3074 3888 13 832 -136 C ATOM 2696 O GLY B 118 45.476 2.855 5.578 1.00 29.64 O ANISOU 2696 O GLY B 118 4124 3250 3888 -17 718 -82 O ATOM 2697 N PHE B 119 46.793 1.749 4.114 1.00 26.95 N ANISOU 2697 N PHE B 119 3800 2850 3591 27 930 -207 N ATOM 2698 CA PHE B 119 46.822 2.838 3.144 1.00 27.51 C ANISOU 2698 CA PHE B 119 3904 3063 3486 6 903 -212 C ATOM 2699 C PHE B 119 45.415 3.113 2.632 1.00 27.79 C ANISOU 2699 C PHE B 119 3997 3187 3373 -63 812 -298 C ATOM 2700 O PHE B 119 44.964 4.262 2.599 1.00 26.50 O ANISOU 2700 O PHE B 119 3838 3125 3104 -78 717 -224 O ATOM 2701 CB PHE B 119 47.751 2.501 1.976 1.00 29.04 C ANISOU 2701 CB PHE B 119 4114 3274 3647 32 1044 -287 C ATOM 2702 CG PHE B 119 47.960 3.641 1.015 1.00 31.22 C ANISOU 2702 CG PHE B 119 4413 3700 3749 22 1034 -254 C ATOM 2703 CD1 PHE B 119 47.002 3.953 0.058 1.00 30.34 C ANISOU 2703 CD1 PHE B 119 4367 3715 3447 -31 987 -338 C ATOM 2704 CD2 PHE B 119 49.124 4.397 1.061 1.00 34.37 C ANISOU 2704 CD2 PHE B 119 4759 4123 4178 65 1073 -128 C ATOM 2705 CE1 PHE B 119 47.195 5.005 -0.826 1.00 30.77 C ANISOU 2705 CE1 PHE B 119 4438 3912 3340 -30 984 -278 C ATOM 2706 CE2 PHE B 119 49.328 5.446 0.174 1.00 33.27 C ANISOU 2706 CE2 PHE B 119 4639 4109 3894 56 1079 -80 C ATOM 2707 CZ PHE B 119 48.358 5.750 -0.770 1.00 30.92 C ANISOU 2707 CZ PHE B 119 4413 3934 3404 14 1037 -146 C ATOM 2708 N ASP B 120 44.733 2.048 2.222 1.00 26.90 N ANISOU 2708 N ASP B 120 3921 3033 3267 -106 848 -453 N ATOM 2709 CA ASP B 120 43.401 2.167 1.652 1.00 29.63 C ANISOU 2709 CA ASP B 120 4307 3480 3473 -181 763 -552 C ATOM 2710 C ASP B 120 42.400 2.728 2.657 1.00 28.04 C ANISOU 2710 C ASP B 120 4077 3286 3290 -199 629 -459 C ATOM 2711 O ASP B 120 41.551 3.543 2.297 1.00 30.05 O ANISOU 2711 O ASP B 120 4339 3667 3410 -228 532 -442 O ATOM 2712 CB ASP B 120 42.914 0.810 1.136 1.00 32.13 C ANISOU 2712 CB ASP B 120 4656 3730 3822 -240 835 -757 C ATOM 2713 CG ASP B 120 43.594 0.397 -0.155 1.00 37.11 C ANISOU 2713 CG ASP B 120 5330 4405 4365 -243 959 -896 C ATOM 2714 OD1 ASP B 120 44.161 1.273 -0.843 1.00 37.75 O ANISOU 2714 OD1 ASP B 120 5421 4616 4306 -214 965 -835 O ATOM 2715 OD2 ASP B 120 43.550 -0.805 -0.489 1.00 40.45 O ANISOU 2715 OD2 ASP B 120 5778 4728 4863 -279 1062 -1072 O ATOM 2716 N MET B 121 42.500 2.291 3.911 1.00 26.69 N ANISOU 2716 N MET B 121 3870 2988 3285 -175 630 -390 N ATOM 2717 CA MET B 121 41.572 2.746 4.941 1.00 26.90 C ANISOU 2717 CA MET B 121 3870 3019 3333 -191 522 -310 C ATOM 2718 C MET B 121 41.705 4.249 5.155 1.00 28.84 C ANISOU 2718 C MET B 121 4103 3360 3496 -164 443 -181 C ATOM 2719 O MET B 121 40.707 4.973 5.155 1.00 26.96 O ANISOU 2719 O MET B 121 3866 3198 3179 -188 354 -163 O ATOM 2720 CB MET B 121 41.800 2.001 6.258 1.00 26.88 C ANISOU 2720 CB MET B 121 3828 2879 3505 -163 550 -242 C ATOM 2721 CG MET B 121 40.710 2.254 7.303 1.00 27.70 C ANISOU 2721 CG MET B 121 3910 2988 3628 -188 457 -184 C ATOM 2722 SD MET B 121 40.916 1.309 8.830 1.00 37.15 S ANISOU 2722 SD MET B 121 5060 4048 5007 -155 497 -87 S ATOM 2723 CE MET B 121 40.681 -0.377 8.234 1.00 22.67 C ANISOU 2723 CE MET B 121 3245 2068 3299 -189 615 -229 C ATOM 2724 N VAL B 122 42.941 4.712 5.324 1.00 28.69 N ANISOU 2724 N VAL B 122 4064 3327 3508 -116 485 -94 N ATOM 2725 CA VAL B 122 43.200 6.133 5.539 1.00 27.73 C ANISOU 2725 CA VAL B 122 3928 3270 3337 -100 430 18 C ATOM 2726 C VAL B 122 42.716 6.952 4.347 1.00 27.23 C ANISOU 2726 C VAL B 122 3900 3324 3121 -114 404 5 C ATOM 2727 O VAL B 122 42.124 8.014 4.525 1.00 25.87 O ANISOU 2727 O VAL B 122 3724 3201 2906 -116 333 75 O ATOM 2728 CB VAL B 122 44.703 6.412 5.780 1.00 26.70 C ANISOU 2728 CB VAL B 122 3759 3113 3275 -59 489 98 C ATOM 2729 CG1 VAL B 122 44.980 7.921 5.827 1.00 23.88 C ANISOU 2729 CG1 VAL B 122 3390 2811 2873 -60 447 193 C ATOM 2730 CG2 VAL B 122 45.170 5.733 7.067 1.00 23.89 C ANISOU 2730 CG2 VAL B 122 3351 2671 3057 -37 494 147 C ATOM 2731 N LYS B 123 42.945 6.444 3.138 1.00 26.72 N ANISOU 2731 N LYS B 123 3868 3310 2976 -122 468 -82 N ATOM 2732 CA LYS B 123 42.600 7.184 1.930 1.00 26.84 C ANISOU 2732 CA LYS B 123 3911 3466 2821 -130 449 -76 C ATOM 2733 C LYS B 123 41.091 7.402 1.779 1.00 27.61 C ANISOU 2733 C LYS B 123 4011 3648 2831 -165 343 -99 C ATOM 2734 O LYS B 123 40.651 8.525 1.514 1.00 23.56 O ANISOU 2734 O LYS B 123 3491 3220 2239 -149 285 0 O ATOM 2735 CB LYS B 123 43.146 6.477 0.688 1.00 28.94 C ANISOU 2735 CB LYS B 123 4213 3787 2997 -137 546 -186 C ATOM 2736 CG LYS B 123 42.977 7.301 -0.588 1.00 33.36 C ANISOU 2736 CG LYS B 123 4798 4521 3358 -137 536 -152 C ATOM 2737 CD LYS B 123 43.696 6.677 -1.769 1.00 36.15 C ANISOU 2737 CD LYS B 123 5187 4939 3610 -141 651 -257 C ATOM 2738 N VAL B 124 40.298 6.345 1.955 1.00 28.97 N ANISOU 2738 N VAL B 124 4184 3792 3032 -212 323 -221 N ATOM 2739 CA VAL B 124 38.854 6.479 1.778 1.00 29.54 C ANISOU 2739 CA VAL B 124 4240 3956 3026 -252 222 -249 C ATOM 2740 C VAL B 124 38.258 7.305 2.915 1.00 26.67 C ANISOU 2740 C VAL B 124 3840 3550 2744 -227 148 -128 C ATOM 2741 O VAL B 124 37.340 8.094 2.689 1.00 26.44 O ANISOU 2741 O VAL B 124 3787 3616 2641 -223 70 -70 O ATOM 2742 CB VAL B 124 38.128 5.105 1.681 1.00 25.31 C ANISOU 2742 CB VAL B 124 3706 3392 2518 -326 225 -423 C ATOM 2743 CG1 VAL B 124 38.563 4.363 0.430 1.00 26.88 C ANISOU 2743 CG1 VAL B 124 3946 3653 2613 -362 299 -573 C ATOM 2744 CG2 VAL B 124 38.359 4.260 2.928 1.00 23.88 C ANISOU 2744 CG2 VAL B 124 3511 3025 2536 -324 271 -431 C ATOM 2745 N CYS B 125 38.800 7.152 4.122 1.00 25.24 N ANISOU 2745 N CYS B 125 3647 3234 2708 -207 177 -87 N ATOM 2746 CA CYS B 125 38.336 7.928 5.268 1.00 25.02 C ANISOU 2746 CA CYS B 125 3590 3168 2749 -187 123 9 C ATOM 2747 C CYS B 125 38.701 9.409 5.111 1.00 28.86 C ANISOU 2747 C CYS B 125 4076 3692 3198 -145 112 129 C ATOM 2748 O CYS B 125 37.943 10.298 5.521 1.00 24.38 O ANISOU 2748 O CYS B 125 3488 3138 2638 -130 60 195 O ATOM 2749 CB CYS B 125 38.911 7.360 6.573 1.00 24.76 C ANISOU 2749 CB CYS B 125 3543 3010 2853 -180 158 23 C ATOM 2750 SG CYS B 125 38.109 5.813 7.137 1.00 27.47 S ANISOU 2750 SG CYS B 125 3872 3279 3285 -225 167 -71 S ATOM 2751 N LYS B 126 39.859 9.669 4.511 1.00 27.50 N ANISOU 2751 N LYS B 126 3922 3526 3000 -125 173 158 N ATOM 2752 CA LYS B 126 40.260 11.039 4.204 1.00 27.80 C ANISOU 2752 CA LYS B 126 3959 3590 3013 -92 181 273 C ATOM 2753 C LYS B 126 39.300 11.647 3.189 1.00 28.92 C ANISOU 2753 C LYS B 126 4103 3856 3030 -80 134 316 C ATOM 2754 O LYS B 126 38.809 12.762 3.378 1.00 30.48 O ANISOU 2754 O LYS B 126 4282 4054 3244 -50 104 418 O ATOM 2755 CB LYS B 126 41.691 11.087 3.671 1.00 24.42 C ANISOU 2755 CB LYS B 126 3542 3153 2583 -80 266 295 C ATOM 2756 CG LYS B 126 42.106 12.452 3.156 1.00 26.20 C ANISOU 2756 CG LYS B 126 3765 3406 2782 -53 290 419 C ATOM 2757 CD LYS B 126 42.013 13.519 4.244 1.00 28.37 C ANISOU 2757 CD LYS B 126 4017 3593 3170 -50 264 492 C ATOM 2758 CE LYS B 126 42.237 14.907 3.677 1.00 31.90 C ANISOU 2758 CE LYS B 126 4463 4046 3613 -25 297 618 C ATOM 2759 NZ LYS B 126 41.984 15.960 4.699 1.00 35.47 N ANISOU 2759 NZ LYS B 126 4895 4398 4182 -28 280 664 N ATOM 2760 N GLN B 127 39.031 10.901 2.120 1.00 28.43 N ANISOU 2760 N GLN B 127 4057 3902 2844 -102 132 237 N ATOM 2761 CA GLN B 127 38.062 11.310 1.104 1.00 28.34 C ANISOU 2761 CA GLN B 127 4034 4051 2684 -96 71 273 C ATOM 2762 C GLN B 127 36.682 11.559 1.712 1.00 28.35 C ANISOU 2762 C GLN B 127 3988 4060 2722 -96 -20 295 C ATOM 2763 O GLN B 127 35.953 12.443 1.272 1.00 30.31 O ANISOU 2763 O GLN B 127 4205 4401 2911 -59 -70 402 O ATOM 2764 CB GLN B 127 37.972 10.253 -0.002 1.00 31.44 C ANISOU 2764 CB GLN B 127 4448 4566 2932 -143 78 136 C ATOM 2765 CG GLN B 127 39.204 10.213 -0.914 1.00 42.95 C ANISOU 2765 CG GLN B 127 5947 6063 4308 -130 176 133 C ATOM 2766 CD GLN B 127 39.222 9.012 -1.855 1.00 51.80 C ANISOU 2766 CD GLN B 127 7100 7277 5306 -185 208 -46 C ATOM 2767 OE1 GLN B 127 38.430 8.078 -1.706 1.00 56.54 O ANISOU 2767 OE1 GLN B 127 7691 7877 5914 -243 165 -185 O ATOM 2768 NE2 GLN B 127 40.127 9.037 -2.831 1.00 51.23 N ANISOU 2768 NE2 GLN B 127 7062 7280 5123 -172 294 -50 N ATOM 2769 N ALA B 128 36.330 10.779 2.728 1.00 27.74 N ANISOU 2769 N ALA B 128 3900 3887 2752 -131 -34 207 N ATOM 2770 CA ALA B 128 35.061 10.958 3.428 1.00 29.43 C ANISOU 2770 CA ALA B 128 4064 4098 3019 -132 -104 225 C ATOM 2771 C ALA B 128 35.045 12.270 4.210 1.00 29.56 C ANISOU 2771 C ALA B 128 4066 4038 3126 -73 -97 356 C ATOM 2772 O ALA B 128 33.987 12.833 4.476 1.00 29.18 O ANISOU 2772 O ALA B 128 3972 4014 3100 -48 -144 412 O ATOM 2773 CB ALA B 128 34.801 9.784 4.360 1.00 26.84 C ANISOU 2773 CB ALA B 128 3731 3679 2790 -183 -99 112 C ATOM 2774 N CYS B 129 36.228 12.741 4.591 1.00 27.28 N ANISOU 2774 N CYS B 129 3811 3654 2900 -56 -32 396 N ATOM 2775 CA CYS B 129 36.347 13.969 5.359 1.00 26.90 C ANISOU 2775 CA CYS B 129 3754 3516 2950 -18 -11 489 C ATOM 2776 C CYS B 129 36.407 15.199 4.455 1.00 30.73 C ANISOU 2776 C CYS B 129 4236 4045 3394 35 6 624 C ATOM 2777 O CYS B 129 36.175 16.318 4.912 1.00 28.97 O ANISOU 2777 O CYS B 129 3998 3751 3259 73 23 709 O ATOM 2778 CB CYS B 129 37.594 13.927 6.247 1.00 24.09 C ANISOU 2778 CB CYS B 129 3422 3046 2685 -37 45 463 C ATOM 2779 SG CYS B 129 37.520 12.759 7.614 1.00 29.35 S ANISOU 2779 SG CYS B 129 4081 3648 3424 -79 33 361 S ATOM 2780 N SER B 130 36.708 14.975 3.179 1.00 36.07 N ANISOU 2780 N SER B 130 4926 4837 3942 38 10 643 N ATOM 2781 CA SER B 130 37.047 16.047 2.241 1.00 41.58 C ANISOU 2781 CA SER B 130 5626 5581 4591 87 46 790 C ATOM 2782 C SER B 130 36.057 17.204 2.230 1.00 43.82 C ANISOU 2782 C SER B 130 5866 5870 4915 152 21 932 C ATOM 2783 O SER B 130 34.890 17.041 1.883 1.00 47.87 O ANISOU 2783 O SER B 130 6334 6497 5358 171 -53 949 O ATOM 2784 CB SER B 130 37.174 15.489 0.823 1.00 45.24 C ANISOU 2784 CB SER B 130 6103 6221 4865 79 38 780 C ATOM 2785 OG SER B 130 37.957 16.356 0.017 1.00 50.10 O ANISOU 2785 OG SER B 130 6734 6861 5440 118 106 915 O ATOM 2786 N GLY B 131 36.543 18.378 2.620 1.00 43.92 N ANISOU 2786 N GLY B 131 5884 5751 5053 186 90 1032 N ATOM 2787 CA GLY B 131 35.741 19.586 2.592 1.00 42.58 C ANISOU 2787 CA GLY B 131 5674 5549 4957 260 97 1182 C ATOM 2788 C GLY B 131 34.954 19.824 3.865 1.00 38.46 C ANISOU 2788 C GLY B 131 5127 4912 4575 265 85 1129 C ATOM 2789 O GLY B 131 34.260 20.832 3.988 1.00 38.59 O ANISOU 2789 O GLY B 131 5106 4872 4683 333 107 1240 O ATOM 2790 N ASN B 132 35.056 18.902 4.816 1.00 35.39 N ANISOU 2790 N ASN B 132 4755 4485 4205 201 62 967 N ATOM 2791 CA ASN B 132 34.297 19.028 6.055 1.00 34.20 C ANISOU 2791 CA ASN B 132 4583 4247 4165 202 56 909 C ATOM 2792 C ASN B 132 35.128 18.846 7.321 1.00 35.14 C ANISOU 2792 C ASN B 132 4739 4243 4368 140 95 790 C ATOM 2793 O ASN B 132 34.864 19.495 8.332 1.00 39.76 O ANISOU 2793 O ASN B 132 5319 4723 5064 146 131 766 O ATOM 2794 CB ASN B 132 33.131 18.036 6.061 1.00 35.15 C ANISOU 2794 CB ASN B 132 4660 4483 4213 191 -29 849 C ATOM 2795 CG ASN B 132 31.983 18.479 5.167 1.00 39.15 C ANISOU 2795 CG ASN B 132 5099 5109 4669 260 -78 974 C ATOM 2796 OD1 ASN B 132 31.211 19.368 5.524 1.00 38.00 O ANISOU 2796 OD1 ASN B 132 4907 4908 4623 325 -58 1057 O ATOM 2797 ND2 ASN B 132 31.868 17.860 3.999 1.00 40.80 N ANISOU 2797 ND2 ASN B 132 5294 5488 4720 247 -140 986 N ATOM 2798 N ALA B 133 36.133 17.979 7.275 1.00 32.52 N ANISOU 2798 N ALA B 133 4440 3934 3984 85 92 716 N ATOM 2799 CA ALA B 133 36.895 17.669 8.481 1.00 31.70 C ANISOU 2799 CA ALA B 133 4354 3749 3941 29 112 617 C ATOM 2800 C ALA B 133 38.347 17.321 8.195 1.00 31.74 C ANISOU 2800 C ALA B 133 4381 3752 3928 -9 141 599 C ATOM 2801 O ALA B 133 38.693 16.938 7.079 1.00 35.57 O ANISOU 2801 O ALA B 133 4875 4309 4332 0 144 632 O ATOM 2802 CB ALA B 133 36.230 16.519 9.241 1.00 31.18 C ANISOU 2802 CB ALA B 133 4277 3721 3850 3 63 524 C ATOM 2803 N LYS B 134 39.189 17.458 9.216 1.00 28.65 N ANISOU 2803 N LYS B 134 3991 3289 3606 -54 165 545 N ATOM 2804 CA LYS B 134 40.565 16.975 9.157 1.00 27.96 C ANISOU 2804 CA LYS B 134 3903 3207 3514 -91 185 523 C ATOM 2805 C LYS B 134 40.630 15.542 9.686 1.00 25.44 C ANISOU 2805 C LYS B 134 3577 2932 3156 -110 148 450 C ATOM 2806 O LYS B 134 39.856 15.162 10.568 1.00 22.70 O ANISOU 2806 O LYS B 134 3226 2586 2815 -115 113 406 O ATOM 2807 CB LYS B 134 41.508 17.880 9.966 1.00 31.55 C ANISOU 2807 CB LYS B 134 4344 3580 4065 -137 223 508 C ATOM 2808 CG LYS B 134 41.502 19.355 9.565 1.00 32.54 C ANISOU 2808 CG LYS B 134 4473 3621 4269 -127 281 577 C ATOM 2809 CD LYS B 134 41.884 19.540 8.110 1.00 34.19 C ANISOU 2809 CD LYS B 134 4688 3861 4439 -92 321 685 C ATOM 2810 N LEU B 135 41.557 14.752 9.153 1.00 25.19 N ANISOU 2810 N LEU B 135 3544 2930 3097 -116 167 444 N ATOM 2811 CA LEU B 135 41.716 13.365 9.585 1.00 23.79 C ANISOU 2811 CA LEU B 135 3357 2773 2910 -125 151 390 C ATOM 2812 C LEU B 135 42.994 13.170 10.396 1.00 22.61 C ANISOU 2812 C LEU B 135 3171 2604 2817 -149 165 389 C ATOM 2813 O LEU B 135 44.092 13.389 9.885 1.00 23.24 O ANISOU 2813 O LEU B 135 3234 2684 2914 -152 207 418 O ATOM 2814 CB LEU B 135 41.731 12.419 8.376 1.00 20.89 C ANISOU 2814 CB LEU B 135 3009 2451 2479 -108 172 370 C ATOM 2815 CG LEU B 135 41.855 10.921 8.683 1.00 22.75 C ANISOU 2815 CG LEU B 135 3237 2676 2730 -113 178 312 C ATOM 2816 CD1 LEU B 135 40.567 10.375 9.292 1.00 21.20 C ANISOU 2816 CD1 LEU B 135 3042 2477 2536 -123 132 274 C ATOM 2817 CD2 LEU B 135 42.255 10.112 7.440 1.00 23.46 C ANISOU 2817 CD2 LEU B 135 3347 2794 2774 -103 229 273 C ATOM 2818 N LYS B 136 42.855 12.758 11.654 1.00 21.31 N ANISOU 2818 N LYS B 136 2984 2438 2673 -165 132 365 N ATOM 2819 CA LYS B 136 44.018 12.326 12.421 1.00 22.38 C ANISOU 2819 CA LYS B 136 3070 2589 2846 -180 132 378 C ATOM 2820 C LYS B 136 44.096 10.801 12.351 1.00 24.55 C ANISOU 2820 C LYS B 136 3334 2867 3127 -148 145 382 C ATOM 2821 O LYS B 136 43.066 10.117 12.416 1.00 24.03 O ANISOU 2821 O LYS B 136 3295 2791 3046 -138 134 357 O ATOM 2822 CB LYS B 136 43.947 12.797 13.878 1.00 23.58 C ANISOU 2822 CB LYS B 136 3196 2762 3002 -217 89 361 C ATOM 2823 CG LYS B 136 43.651 14.281 14.084 1.00 23.61 C ANISOU 2823 CG LYS B 136 3217 2735 3018 -252 90 331 C ATOM 2824 CD LYS B 136 44.241 14.763 15.410 1.00 23.42 C ANISOU 2824 CD LYS B 136 3151 2748 2999 -311 60 294 C ATOM 2825 CE LYS B 136 43.574 16.045 15.909 1.00 23.92 C ANISOU 2825 CE LYS B 136 3244 2768 3077 -346 70 231 C ATOM 2826 NZ LYS B 136 42.179 15.805 16.419 1.00 22.44 N ANISOU 2826 NZ LYS B 136 3090 2583 2851 -317 60 207 N ATOM 2827 N VAL B 137 45.304 10.267 12.196 1.00 22.15 N ANISOU 2827 N VAL B 137 2986 2567 2862 -134 179 413 N ATOM 2828 CA VAL B 137 45.485 8.817 12.164 1.00 23.51 C ANISOU 2828 CA VAL B 137 3144 2717 3073 -95 213 422 C ATOM 2829 C VAL B 137 46.292 8.328 13.365 1.00 25.39 C ANISOU 2829 C VAL B 137 3304 2983 3358 -84 193 489 C ATOM 2830 O VAL B 137 47.448 8.714 13.552 1.00 25.93 O ANISOU 2830 O VAL B 137 3310 3090 3452 -91 192 530 O ATOM 2831 CB VAL B 137 46.178 8.355 10.867 1.00 22.20 C ANISOU 2831 CB VAL B 137 2984 2527 2923 -67 291 409 C ATOM 2832 CG1 VAL B 137 46.476 6.865 10.927 1.00 21.36 C ANISOU 2832 CG1 VAL B 137 2855 2371 2888 -24 345 414 C ATOM 2833 CG2 VAL B 137 45.309 8.669 9.658 1.00 22.44 C ANISOU 2833 CG2 VAL B 137 3087 2561 2879 -76 303 349 C ATOM 2834 N ILE B 138 45.669 7.475 14.175 1.00 23.95 N ANISOU 2834 N ILE B 138 3120 2793 3187 -70 178 510 N ATOM 2835 CA ILE B 138 46.324 6.874 15.331 1.00 25.11 C ANISOU 2835 CA ILE B 138 3190 2983 3367 -47 159 600 C ATOM 2836 C ILE B 138 47.055 5.602 14.915 1.00 28.23 C ANISOU 2836 C ILE B 138 3546 3319 3862 18 234 654 C ATOM 2837 O ILE B 138 46.415 4.619 14.541 1.00 26.73 O ANISOU 2837 O ILE B 138 3394 3042 3719 42 288 631 O ATOM 2838 CB ILE B 138 45.311 6.520 16.435 1.00 29.19 C ANISOU 2838 CB ILE B 138 3718 3521 3852 -54 123 622 C ATOM 2839 CG1 ILE B 138 44.402 7.712 16.743 1.00 28.28 C ANISOU 2839 CG1 ILE B 138 3651 3442 3652 -109 72 551 C ATOM 2840 CG2 ILE B 138 46.027 6.007 17.685 1.00 30.35 C ANISOU 2840 CG2 ILE B 138 3778 3747 4005 -29 94 738 C ATOM 2841 CD1 ILE B 138 43.344 7.423 17.807 1.00 27.55 C ANISOU 2841 CD1 ILE B 138 3569 3377 3521 -116 49 565 C ATOM 2842 N ILE B 139 48.384 5.606 14.991 1.00 26.25 N ANISOU 2842 N ILE B 139 3210 3107 3655 43 245 722 N ATOM 2843 CA ILE B 139 49.147 4.451 14.537 1.00 27.47 C ANISOU 2843 CA ILE B 139 3320 3194 3924 117 335 775 C ATOM 2844 C ILE B 139 49.461 3.453 15.661 1.00 27.75 C ANISOU 2844 C ILE B 139 3272 3243 4026 176 331 914 C ATOM 2845 O ILE B 139 49.918 2.345 15.391 1.00 29.17 O ANISOU 2845 O ILE B 139 3418 3339 4329 249 420 970 O ATOM 2846 CB ILE B 139 50.459 4.891 13.847 1.00 28.39 C ANISOU 2846 CB ILE B 139 3376 3336 4073 129 372 787 C ATOM 2847 CG1 ILE B 139 51.408 5.578 14.833 1.00 26.77 C ANISOU 2847 CG1 ILE B 139 3059 3261 3851 105 290 872 C ATOM 2848 CG2 ILE B 139 50.151 5.823 12.678 1.00 27.60 C ANISOU 2848 CG2 ILE B 139 3359 3222 3908 80 390 676 C ATOM 2849 CD1 ILE B 139 52.741 5.965 14.213 1.00 23.84 C ANISOU 2849 CD1 ILE B 139 2607 2918 3533 112 330 895 C ATOM 2850 N GLU B 140 49.188 3.843 16.905 1.00 27.75 N ANISOU 2850 N GLU B 140 3244 3352 3949 146 238 970 N ATOM 2851 CA GLU B 140 49.438 3.007 18.089 1.00 28.00 C ANISOU 2851 CA GLU B 140 3191 3436 4011 201 220 1126 C ATOM 2852 C GLU B 140 50.908 2.583 18.188 1.00 31.99 C ANISOU 2852 C GLU B 140 3564 3987 4605 270 240 1256 C ATOM 2853 O GLU B 140 51.256 1.413 17.991 1.00 31.32 O ANISOU 2853 O GLU B 140 3439 3804 4658 360 332 1346 O ATOM 2854 CB GLU B 140 48.531 1.773 18.089 1.00 28.25 C ANISOU 2854 CB GLU B 140 3271 3335 4126 245 298 1153 C ATOM 2855 CG GLU B 140 48.275 1.185 19.473 1.00 29.80 C ANISOU 2855 CG GLU B 140 3415 3601 4308 277 265 1308 C ATOM 2856 CD GLU B 140 47.334 2.041 20.311 1.00 33.95 C ANISOU 2856 CD GLU B 140 3986 4240 4673 200 173 1259 C ATOM 2857 OE1 GLU B 140 47.768 3.092 20.829 1.00 34.31 O ANISOU 2857 OE1 GLU B 140 3999 4438 4600 150 81 1238 O ATOM 2858 OE2 GLU B 140 46.154 1.661 20.453 1.00 35.36 O ANISOU 2858 OE2 GLU B 140 4231 4351 4853 185 202 1232 O ATOM 2859 N THR B 141 51.761 3.554 18.501 1.00 29.96 N ANISOU 2859 N THR B 141 3230 3872 4279 225 159 1262 N ATOM 2860 CA THR B 141 53.199 3.337 18.598 1.00 32.56 C ANISOU 2860 CA THR B 141 3412 4274 4684 277 162 1380 C ATOM 2861 C THR B 141 53.579 2.351 19.696 1.00 34.03 C ANISOU 2861 C THR B 141 3483 4537 4909 363 142 1585 C ATOM 2862 O THR B 141 54.620 1.693 19.620 1.00 35.42 O ANISOU 2862 O THR B 141 3537 4715 5204 451 188 1717 O ATOM 2863 CB THR B 141 53.935 4.665 18.852 1.00 33.19 C ANISOU 2863 CB THR B 141 3427 4509 4674 185 63 1333 C ATOM 2864 OG1 THR B 141 53.410 5.284 20.034 1.00 35.12 O ANISOU 2864 OG1 THR B 141 3678 4895 4771 111 -53 1318 O ATOM 2865 CG2 THR B 141 53.744 5.604 17.674 1.00 25.93 C ANISOU 2865 CG2 THR B 141 2603 3502 3746 119 104 1171 C ATOM 2866 N GLY B 142 52.737 2.262 20.720 1.00 33.31 N ANISOU 2866 N GLY B 142 3423 4515 4719 342 81 1624 N ATOM 2867 CA GLY B 142 52.977 1.354 21.823 1.00 35.29 C ANISOU 2867 CA GLY B 142 3570 4854 4983 423 61 1839 C ATOM 2868 C GLY B 142 52.919 -0.090 21.373 1.00 38.40 C ANISOU 2868 C GLY B 142 3964 5051 5576 545 204 1947 C ATOM 2869 O GLY B 142 53.599 -0.943 21.937 1.00 42.79 O ANISOU 2869 O GLY B 142 4394 5644 6219 649 224 2160 O ATOM 2870 N GLU B 143 52.114 -0.362 20.349 1.00 35.83 N ANISOU 2870 N GLU B 143 3772 4515 5326 532 306 1801 N ATOM 2871 CA GLU B 143 51.984 -1.714 19.811 1.00 34.94 C ANISOU 2871 CA GLU B 143 3676 4186 5416 628 459 1854 C ATOM 2872 C GLU B 143 52.923 -1.958 18.628 1.00 34.75 C ANISOU 2872 C GLU B 143 3623 4048 5535 680 566 1804 C ATOM 2873 O GLU B 143 53.385 -3.081 18.418 1.00 39.62 O ANISOU 2873 O GLU B 143 4184 4529 6341 789 691 1908 O ATOM 2874 CB GLU B 143 50.537 -1.984 19.395 1.00 33.73 C ANISOU 2874 CB GLU B 143 3674 3876 5264 574 514 1712 C ATOM 2875 CG GLU B 143 49.561 -2.024 20.560 1.00 36.87 C ANISOU 2875 CG GLU B 143 4094 4352 5563 544 450 1786 C ATOM 2876 CD GLU B 143 49.854 -3.163 21.523 1.00 44.72 C ANISOU 2876 CD GLU B 143 4988 5343 6660 651 494 2043 C ATOM 2877 OE1 GLU B 143 49.804 -4.337 21.096 1.00 45.25 O ANISOU 2877 OE1 GLU B 143 5058 5201 6933 725 636 2094 O ATOM 2878 OE2 GLU B 143 50.146 -2.883 22.707 1.00 47.74 O ANISOU 2878 OE2 GLU B 143 5286 5935 6919 661 391 2196 O ATOM 2879 N LEU B 144 53.203 -0.911 17.857 1.00 31.33 N ANISOU 2879 N LEU B 144 3224 3663 5018 606 531 1649 N ATOM 2880 CA LEU B 144 54.159 -1.020 16.758 1.00 34.37 C ANISOU 2880 CA LEU B 144 3574 3972 5514 650 632 1605 C ATOM 2881 C LEU B 144 55.562 -1.254 17.298 1.00 37.58 C ANISOU 2881 C LEU B 144 3790 4484 6003 739 621 1803 C ATOM 2882 O LEU B 144 56.309 -2.074 16.769 1.00 39.87 O ANISOU 2882 O LEU B 144 4014 4663 6470 843 751 1865 O ATOM 2883 CB LEU B 144 54.131 0.234 15.890 1.00 31.10 C ANISOU 2883 CB LEU B 144 3233 3605 4980 548 593 1423 C ATOM 2884 CG LEU B 144 52.829 0.471 15.130 1.00 29.22 C ANISOU 2884 CG LEU B 144 3167 3268 4667 472 613 1232 C ATOM 2885 CD1 LEU B 144 52.883 1.807 14.423 1.00 25.75 C ANISOU 2885 CD1 LEU B 144 2778 2900 4107 383 565 1102 C ATOM 2886 CD2 LEU B 144 52.580 -0.664 14.145 1.00 28.87 C ANISOU 2886 CD2 LEU B 144 3186 3025 4759 527 774 1159 C ATOM 2887 N LYS B 145 55.902 -0.499 18.341 1.00 38.10 N ANISOU 2887 N LYS B 145 3765 4772 5939 694 466 1890 N ATOM 2888 CA LYS B 145 57.122 -0.683 19.129 1.00 38.29 C ANISOU 2888 CA LYS B 145 3587 4956 6006 766 412 2102 C ATOM 2889 C LYS B 145 58.412 -0.323 18.388 1.00 38.95 C ANISOU 2889 C LYS B 145 3559 5069 6170 784 451 2094 C ATOM 2890 O LYS B 145 59.126 0.588 18.803 1.00 38.90 O ANISOU 2890 O LYS B 145 3447 5260 6074 718 333 2111 O ATOM 2891 CB LYS B 145 57.204 -2.125 19.649 1.00 37.54 C ANISOU 2891 CB LYS B 145 3418 4775 6070 913 498 2320 C ATOM 2892 N SER B 146 58.721 -1.036 17.309 1.00 39.59 N ANISOU 2892 N SER B 146 3660 4959 6425 868 624 2062 N ATOM 2893 CA SER B 146 59.983 -0.810 16.603 1.00 41.54 C ANISOU 2893 CA SER B 146 3789 5228 6765 902 686 2074 C ATOM 2894 C SER B 146 59.963 0.502 15.826 1.00 39.79 C ANISOU 2894 C SER B 146 3646 5051 6421 768 649 1878 C ATOM 2895 O SER B 146 58.910 0.955 15.395 1.00 38.30 O ANISOU 2895 O SER B 146 3632 4793 6125 683 641 1708 O ATOM 2896 CB SER B 146 60.292 -1.971 15.653 1.00 40.18 C ANISOU 2896 CB SER B 146 3623 4831 6812 1033 903 2080 C ATOM 2897 OG SER B 146 59.438 -1.943 14.525 1.00 41.50 O ANISOU 2897 OG SER B 146 3987 4829 6952 978 1002 1853 O ATOM 2898 N GLU B 147 61.139 1.099 15.645 1.00 43.73 N ANISOU 2898 N GLU B 147 4003 5664 6948 755 632 1915 N ATOM 2899 CA GLU B 147 61.272 2.339 14.885 1.00 43.33 C ANISOU 2899 CA GLU B 147 4005 5646 6811 635 618 1758 C ATOM 2900 C GLU B 147 60.872 2.135 13.428 1.00 41.75 C ANISOU 2900 C GLU B 147 3958 5258 6648 652 784 1605 C ATOM 2901 O GLU B 147 60.241 3.003 12.824 1.00 38.83 O ANISOU 2901 O GLU B 147 3724 4870 6161 551 768 1452 O ATOM 2902 CB GLU B 147 62.707 2.876 14.968 1.00 45.36 C ANISOU 2902 CB GLU B 147 4055 6053 7127 625 588 1847 C ATOM 2903 CG GLU B 147 62.974 4.063 14.051 1.00 49.63 C ANISOU 2903 CG GLU B 147 4638 6599 7622 514 613 1707 C ATOM 2904 CD GLU B 147 64.324 4.714 14.298 1.00 57.21 C ANISOU 2904 CD GLU B 147 5381 7722 8632 472 560 1789 C ATOM 2905 OE1 GLU B 147 64.982 4.372 15.305 1.00 60.36 O ANISOU 2905 OE1 GLU B 147 5596 8268 9068 511 468 1946 O ATOM 2906 OE2 GLU B 147 64.726 5.573 13.482 1.00 58.82 O ANISOU 2906 OE2 GLU B 147 5592 7916 8840 398 612 1704 O ATOM 2907 N GLU B 148 61.237 0.983 12.871 1.00 41.81 N ANISOU 2907 N GLU B 148 3939 5130 6816 780 947 1649 N ATOM 2908 CA GLU B 148 60.881 0.647 11.495 1.00 41.52 C ANISOU 2908 CA GLU B 148 4044 4926 6806 798 1116 1491 C ATOM 2909 C GLU B 148 59.365 0.667 11.274 1.00 38.22 C ANISOU 2909 C GLU B 148 3836 4422 6264 728 1089 1337 C ATOM 2910 O GLU B 148 58.882 1.244 10.300 1.00 35.03 O ANISOU 2910 O GLU B 148 3560 3991 5758 657 1122 1180 O ATOM 2911 CB GLU B 148 61.444 -0.727 11.119 1.00 44.03 C ANISOU 2911 CB GLU B 148 4299 5097 7334 951 1302 1556 C ATOM 2912 CG GLU B 148 61.022 -1.213 9.741 1.00 44.83 C ANISOU 2912 CG GLU B 148 4552 5026 7455 965 1486 1368 C ATOM 2913 N LEU B 149 58.618 0.040 12.180 1.00 36.57 N ANISOU 2913 N LEU B 149 3653 4181 6064 748 1031 1395 N ATOM 2914 CA LEU B 149 57.168 -0.030 12.040 1.00 36.67 C ANISOU 2914 CA LEU B 149 3842 4112 5978 685 1007 1261 C ATOM 2915 C LEU B 149 56.524 1.325 12.284 1.00 34.97 C ANISOU 2915 C LEU B 149 3697 4021 5570 555 854 1186 C ATOM 2916 O LEU B 149 55.602 1.714 11.572 1.00 35.86 O ANISOU 2916 O LEU B 149 3953 4089 5582 488 859 1036 O ATOM 2917 CB LEU B 149 56.579 -1.074 12.993 1.00 38.30 C ANISOU 2917 CB LEU B 149 4043 4248 6262 743 999 1362 C ATOM 2918 CG LEU B 149 56.834 -2.515 12.547 1.00 43.68 C ANISOU 2918 CG LEU B 149 4708 4734 7153 863 1186 1388 C ATOM 2919 CD1 LEU B 149 56.344 -3.503 13.591 1.00 44.11 C ANISOU 2919 CD1 LEU B 149 4737 4719 7304 925 1181 1530 C ATOM 2920 CD2 LEU B 149 56.169 -2.771 11.197 1.00 43.65 C ANISOU 2920 CD2 LEU B 149 4864 4583 7137 824 1312 1158 C ATOM 2921 N ILE B 150 57.020 2.042 13.288 1.00 35.58 N ANISOU 2921 N ILE B 150 3665 4255 5597 519 721 1289 N ATOM 2922 CA ILE B 150 56.517 3.373 13.594 1.00 33.72 C ANISOU 2922 CA ILE B 150 3484 4126 5202 395 589 1214 C ATOM 2923 C ILE B 150 56.758 4.312 12.412 1.00 32.43 C ANISOU 2923 C ILE B 150 3372 3953 4996 337 638 1102 C ATOM 2924 O ILE B 150 55.887 5.108 12.054 1.00 32.08 O ANISOU 2924 O ILE B 150 3448 3901 4840 258 601 991 O ATOM 2925 CB ILE B 150 57.169 3.943 14.876 1.00 35.38 C ANISOU 2925 CB ILE B 150 3552 4516 5373 359 449 1328 C ATOM 2926 CG1 ILE B 150 56.708 3.146 16.099 1.00 36.74 C ANISOU 2926 CG1 ILE B 150 3695 4725 5540 405 386 1443 C ATOM 2927 CG2 ILE B 150 56.814 5.413 15.065 1.00 31.65 C ANISOU 2927 CG2 ILE B 150 3130 4132 4763 224 341 1225 C ATOM 2928 CD1 ILE B 150 57.351 3.576 17.406 1.00 36.12 C ANISOU 2928 CD1 ILE B 150 3468 4856 5398 374 244 1560 C ATOM 2929 N ARG B 151 57.931 4.206 11.796 1.00 31.76 N ANISOU 2929 N ARG B 151 3190 3871 5005 383 731 1144 N ATOM 2930 CA ARG B 151 58.238 5.020 10.625 1.00 32.26 C ANISOU 2930 CA ARG B 151 3294 3928 5034 337 799 1059 C ATOM 2931 C ARG B 151 57.329 4.624 9.463 1.00 33.33 C ANISOU 2931 C ARG B 151 3596 3948 5119 350 901 928 C ATOM 2932 O ARG B 151 56.791 5.482 8.759 1.00 31.34 O ANISOU 2932 O ARG B 151 3445 3706 4757 281 893 839 O ATOM 2933 CB ARG B 151 59.714 4.881 10.229 1.00 31.53 C ANISOU 2933 CB ARG B 151 3049 3866 5064 392 894 1141 C ATOM 2934 CG ARG B 151 60.084 5.619 8.955 1.00 34.25 C ANISOU 2934 CG ARG B 151 3432 4202 5378 355 992 1070 C ATOM 2935 CD ARG B 151 61.594 5.715 8.758 1.00 41.70 C ANISOU 2935 CD ARG B 151 4198 5204 6442 388 1064 1165 C ATOM 2936 NE ARG B 151 62.207 4.406 8.556 1.00 51.91 N ANISOU 2936 NE ARG B 151 5415 6431 7878 523 1195 1224 N ATOM 2937 CZ ARG B 151 63.010 3.810 9.435 1.00 58.21 C ANISOU 2937 CZ ARG B 151 6038 7275 8804 595 1168 1369 C ATOM 2938 NH1 ARG B 151 63.310 4.417 10.578 1.00 60.84 N ANISOU 2938 NH1 ARG B 151 6253 7747 9115 533 1002 1458 N ATOM 2939 NH2 ARG B 151 63.519 2.611 9.171 1.00 57.91 N ANISOU 2939 NH2 ARG B 151 5937 7149 8916 731 1309 1425 N ATOM 2940 N LYS B 152 57.146 3.317 9.290 1.00 35.56 N ANISOU 2940 N LYS B 152 3900 4125 5486 436 995 918 N ATOM 2941 CA LYS B 152 56.338 2.785 8.196 1.00 37.18 C ANISOU 2941 CA LYS B 152 4249 4227 5649 441 1096 774 C ATOM 2942 C LYS B 152 54.869 3.222 8.297 1.00 31.81 C ANISOU 2942 C LYS B 152 3705 3551 4829 360 994 682 C ATOM 2943 O LYS B 152 54.290 3.711 7.325 1.00 28.13 O ANISOU 2943 O LYS B 152 3344 3095 4249 311 1012 574 O ATOM 2944 CB LYS B 152 56.437 1.257 8.163 1.00 38.55 C ANISOU 2944 CB LYS B 152 4408 4266 5972 540 1221 777 C ATOM 2945 CG LYS B 152 56.050 0.639 6.830 1.00 41.84 C ANISOU 2945 CG LYS B 152 4941 4583 6373 549 1369 609 C ATOM 2946 N ALA B 153 54.271 3.044 9.470 1.00 29.93 N ANISOU 2946 N ALA B 153 3457 3318 4597 349 889 737 N ATOM 2947 CA ALA B 153 52.885 3.459 9.675 1.00 28.78 C ANISOU 2947 CA ALA B 153 3422 3179 4334 278 794 663 C ATOM 2948 C ALA B 153 52.729 4.958 9.412 1.00 28.43 C ANISOU 2948 C ALA B 153 3411 3227 4165 198 718 633 C ATOM 2949 O ALA B 153 51.767 5.391 8.776 1.00 28.17 O ANISOU 2949 O ALA B 153 3483 3191 4029 152 702 542 O ATOM 2950 CB ALA B 153 52.422 3.113 11.083 1.00 25.49 C ANISOU 2950 CB ALA B 153 2970 2773 3942 282 701 747 C ATOM 2951 N SER B 154 53.693 5.740 9.890 1.00 26.93 N ANISOU 2951 N SER B 154 3122 3116 3995 180 675 715 N ATOM 2952 CA SER B 154 53.673 7.186 9.695 1.00 28.07 C ANISOU 2952 CA SER B 154 3285 3323 4058 101 621 695 C ATOM 2953 C SER B 154 53.709 7.553 8.212 1.00 28.64 C ANISOU 2953 C SER B 154 3424 3378 4078 98 716 635 C ATOM 2954 O SER B 154 52.951 8.412 7.766 1.00 27.27 O ANISOU 2954 O SER B 154 3334 3217 3809 49 685 591 O ATOM 2955 CB SER B 154 54.851 7.845 10.420 1.00 28.65 C ANISOU 2955 CB SER B 154 3221 3478 4186 73 575 782 C ATOM 2956 OG SER B 154 54.755 7.662 11.819 1.00 27.92 O ANISOU 2956 OG SER B 154 3069 3439 4100 64 470 835 O ATOM 2957 N GLU B 155 54.592 6.901 7.457 1.00 28.07 N ANISOU 2957 N GLU B 155 3313 3285 4070 156 838 643 N ATOM 2958 CA GLU B 155 54.727 7.184 6.033 1.00 28.38 C ANISOU 2958 CA GLU B 155 3410 3330 4043 156 942 590 C ATOM 2959 C GLU B 155 53.463 6.809 5.272 1.00 25.10 C ANISOU 2959 C GLU B 155 3132 2890 3515 149 953 477 C ATOM 2960 O GLU B 155 53.014 7.552 4.402 1.00 23.92 O ANISOU 2960 O GLU B 155 3054 2786 3246 115 958 446 O ATOM 2961 CB GLU B 155 55.936 6.451 5.449 1.00 32.05 C ANISOU 2961 CB GLU B 155 3798 3776 4604 226 1086 612 C ATOM 2962 CG GLU B 155 57.255 7.024 5.924 1.00 40.06 C ANISOU 2962 CG GLU B 155 4662 4843 5717 222 1084 725 C ATOM 2963 CD GLU B 155 58.458 6.338 5.311 1.00 47.20 C ANISOU 2963 CD GLU B 155 5476 5731 6725 299 1238 755 C ATOM 2964 OE1 GLU B 155 58.270 5.321 4.607 1.00 49.28 O ANISOU 2964 OE1 GLU B 155 5800 5929 6994 362 1353 678 O ATOM 2965 OE2 GLU B 155 59.591 6.820 5.533 1.00 49.82 O ANISOU 2965 OE2 GLU B 155 5673 6117 7141 293 1249 848 O ATOM 2966 N ILE B 156 52.895 5.656 5.604 1.00 25.74 N ANISOU 2966 N ILE B 156 3240 2904 3635 179 956 424 N ATOM 2967 CA ILE B 156 51.674 5.192 4.964 1.00 27.18 C ANISOU 2967 CA ILE B 156 3538 3066 3724 159 959 303 C ATOM 2968 C ILE B 156 50.541 6.187 5.197 1.00 30.14 C ANISOU 2968 C ILE B 156 3972 3495 3987 96 831 302 C ATOM 2969 O ILE B 156 49.864 6.603 4.255 1.00 31.91 O ANISOU 2969 O ILE B 156 4271 3772 4083 68 830 245 O ATOM 2970 CB ILE B 156 51.263 3.808 5.485 1.00 28.23 C ANISOU 2970 CB ILE B 156 3675 3096 3956 191 983 258 C ATOM 2971 CG1 ILE B 156 52.272 2.750 5.036 1.00 33.00 C ANISOU 2971 CG1 ILE B 156 4235 3625 4681 263 1139 240 C ATOM 2972 CG2 ILE B 156 49.884 3.437 4.989 1.00 28.12 C ANISOU 2972 CG2 ILE B 156 3766 3069 3849 145 959 128 C ATOM 2973 CD1 ILE B 156 52.101 1.415 5.742 1.00 35.52 C ANISOU 2973 CD1 ILE B 156 4530 3815 5151 310 1178 241 C ATOM 2974 N ALA B 157 50.354 6.573 6.456 1.00 27.98 N ANISOU 2974 N ALA B 157 3657 3218 3759 78 729 371 N ATOM 2975 CA ALA B 157 49.315 7.525 6.829 1.00 26.24 C ANISOU 2975 CA ALA B 157 3480 3032 3457 27 621 373 C ATOM 2976 C ALA B 157 49.452 8.815 6.033 1.00 27.56 C ANISOU 2976 C ALA B 157 3669 3257 3545 0 626 400 C ATOM 2977 O ALA B 157 48.477 9.302 5.457 1.00 27.78 O ANISOU 2977 O ALA B 157 3765 3318 3473 -20 595 371 O ATOM 2978 CB ALA B 157 49.370 7.810 8.317 1.00 23.21 C ANISOU 2978 CB ALA B 157 3037 2647 3133 11 532 439 C ATOM 2979 N ILE B 158 50.671 9.349 5.979 1.00 28.96 N ANISOU 2979 N ILE B 158 3779 3449 3776 2 671 466 N ATOM 2980 CA ILE B 158 50.926 10.612 5.288 1.00 25.64 C ANISOU 2980 CA ILE B 158 3367 3066 3309 -25 692 514 C ATOM 2981 C ILE B 158 50.672 10.494 3.784 1.00 27.27 C ANISOU 2981 C ILE B 158 3643 3319 3399 -5 771 481 C ATOM 2982 O ILE B 158 50.026 11.354 3.190 1.00 29.29 O ANISOU 2982 O ILE B 158 3950 3615 3562 -21 751 506 O ATOM 2983 CB ILE B 158 52.368 11.105 5.535 1.00 25.97 C ANISOU 2983 CB ILE B 158 3306 3111 3450 -37 735 589 C ATOM 2984 CG1 ILE B 158 52.545 11.502 7.003 1.00 24.67 C ANISOU 2984 CG1 ILE B 158 3072 2937 3366 -78 638 617 C ATOM 2985 CG2 ILE B 158 52.709 12.296 4.626 1.00 23.61 C ANISOU 2985 CG2 ILE B 158 3016 2837 3117 -62 792 646 C ATOM 2986 CD1 ILE B 158 53.972 11.912 7.356 1.00 28.97 C ANISOU 2986 CD1 ILE B 158 3492 3502 4012 -104 662 680 C ATOM 2987 N ASN B 159 51.169 9.425 3.174 1.00 27.93 N ANISOU 2987 N ASN B 159 3727 3402 3484 34 865 425 N ATOM 2988 CA ASN B 159 50.959 9.203 1.747 1.00 30.06 C ANISOU 2988 CA ASN B 159 4063 3737 3620 47 946 368 C ATOM 2989 C ASN B 159 49.489 9.023 1.381 1.00 28.04 C ANISOU 2989 C ASN B 159 3895 3524 3236 26 874 290 C ATOM 2990 O ASN B 159 49.073 9.373 0.279 1.00 28.50 O ANISOU 2990 O ASN B 159 4007 3678 3144 20 893 279 O ATOM 2991 CB ASN B 159 51.750 7.983 1.275 1.00 31.26 C ANISOU 2991 CB ASN B 159 4199 3863 3815 91 1072 295 C ATOM 2992 CG ASN B 159 53.219 8.287 1.067 1.00 33.09 C ANISOU 2992 CG ASN B 159 4347 4099 4127 117 1177 376 C ATOM 2993 OD1 ASN B 159 53.598 9.427 0.800 1.00 32.98 O ANISOU 2993 OD1 ASN B 159 4312 4132 4088 95 1181 470 O ATOM 2994 ND2 ASN B 159 54.055 7.259 1.175 1.00 32.51 N ANISOU 2994 ND2 ASN B 159 4217 3969 4165 167 1272 346 N ATOM 2995 N ALA B 160 48.709 8.473 2.307 1.00 27.57 N ANISOU 2995 N ALA B 160 3839 3405 3230 14 792 244 N ATOM 2996 CA ALA B 160 47.297 8.206 2.051 1.00 28.44 C ANISOU 2996 CA ALA B 160 4013 3552 3240 -12 721 165 C ATOM 2997 C ALA B 160 46.409 9.418 2.370 1.00 30.29 C ANISOU 2997 C ALA B 160 4257 3825 3429 -33 615 245 C ATOM 2998 O ALA B 160 45.208 9.406 2.086 1.00 28.65 O ANISOU 2998 O ALA B 160 4086 3669 3131 -51 550 204 O ATOM 2999 CB ALA B 160 46.839 6.985 2.843 1.00 25.94 C ANISOU 2999 CB ALA B 160 3693 3148 3016 -17 702 82 C ATOM 3000 N GLY B 161 46.998 10.452 2.968 1.00 30.31 N ANISOU 3000 N GLY B 161 4217 3795 3504 -32 602 352 N ATOM 3001 CA GLY B 161 46.312 11.724 3.120 1.00 28.18 C ANISOU 3001 CA GLY B 161 3956 3543 3209 -45 536 432 C ATOM 3002 C GLY B 161 46.031 12.239 4.522 1.00 26.48 C ANISOU 3002 C GLY B 161 3710 3253 3098 -64 462 458 C ATOM 3003 O GLY B 161 45.255 13.182 4.679 1.00 28.08 O ANISOU 3003 O GLY B 161 3926 3455 3288 -70 413 503 O ATOM 3004 N ALA B 162 46.650 11.639 5.535 1.00 24.95 N ANISOU 3004 N ALA B 162 3472 3004 3003 -71 458 436 N ATOM 3005 CA ALA B 162 46.453 12.069 6.922 1.00 26.88 C ANISOU 3005 CA ALA B 162 3686 3205 3323 -96 389 450 C ATOM 3006 C ALA B 162 46.799 13.544 7.139 1.00 27.75 C ANISOU 3006 C ALA B 162 3776 3293 3473 -125 388 514 C ATOM 3007 O ALA B 162 47.763 14.054 6.568 1.00 29.45 O ANISOU 3007 O ALA B 162 3966 3511 3712 -130 450 563 O ATOM 3008 CB ALA B 162 47.277 11.205 7.862 1.00 24.30 C ANISOU 3008 CB ALA B 162 3301 2853 3080 -94 391 442 C ATOM 3009 N ASP B 163 46.008 14.224 7.968 1.00 26.66 N ANISOU 3009 N ASP B 163 3647 3126 3355 -146 329 507 N ATOM 3010 CA ASP B 163 46.288 15.615 8.328 1.00 28.16 C ANISOU 3010 CA ASP B 163 3820 3268 3611 -182 337 544 C ATOM 3011 C ASP B 163 47.131 15.696 9.593 1.00 27.19 C ANISOU 3011 C ASP B 163 3636 3132 3565 -234 312 514 C ATOM 3012 O ASP B 163 47.898 16.646 9.786 1.00 26.38 O ANISOU 3012 O ASP B 163 3494 2996 3532 -282 336 530 O ATOM 3013 CB ASP B 163 44.988 16.397 8.524 1.00 29.00 C ANISOU 3013 CB ASP B 163 3967 3343 3708 -174 305 546 C ATOM 3014 CG ASP B 163 44.199 16.532 7.246 1.00 31.04 C ANISOU 3014 CG ASP B 163 4267 3639 3888 -125 321 600 C ATOM 3015 OD1 ASP B 163 44.697 17.212 6.324 1.00 31.91 O ANISOU 3015 OD1 ASP B 163 4379 3750 3996 -115 380 679 O ATOM 3016 OD2 ASP B 163 43.091 15.959 7.169 1.00 27.90 O ANISOU 3016 OD2 ASP B 163 3893 3282 3426 -99 274 571 O ATOM 3017 N PHE B 164 46.940 14.706 10.461 1.00 24.07 N ANISOU 3017 N PHE B 164 3226 2768 3154 -228 261 473 N ATOM 3018 CA PHE B 164 47.761 14.497 11.646 1.00 23.98 C ANISOU 3018 CA PHE B 164 3143 2785 3183 -266 225 458 C ATOM 3019 C PHE B 164 48.143 13.031 11.703 1.00 25.57 C ANISOU 3019 C PHE B 164 3314 3024 3378 -221 226 475 C ATOM 3020 O PHE B 164 47.405 12.168 11.207 1.00 21.87 O ANISOU 3020 O PHE B 164 2893 2543 2872 -175 239 463 O ATOM 3021 CB PHE B 164 47.021 14.847 12.941 1.00 23.44 C ANISOU 3021 CB PHE B 164 3083 2722 3100 -301 162 407 C ATOM 3022 CG PHE B 164 46.836 16.317 13.180 1.00 28.07 C ANISOU 3022 CG PHE B 164 3684 3257 3726 -355 171 373 C ATOM 3023 CD1 PHE B 164 45.818 17.016 12.549 1.00 27.92 C ANISOU 3023 CD1 PHE B 164 3728 3172 3706 -329 200 380 C ATOM 3024 CD2 PHE B 164 47.651 16.990 14.079 1.00 28.22 C ANISOU 3024 CD2 PHE B 164 3645 3291 3786 -434 152 330 C ATOM 3025 CE1 PHE B 164 45.641 18.372 12.785 1.00 31.28 C ANISOU 3025 CE1 PHE B 164 4165 3523 4196 -370 228 354 C ATOM 3026 CE2 PHE B 164 47.480 18.342 14.316 1.00 27.32 C ANISOU 3026 CE2 PHE B 164 3547 3105 3729 -493 177 279 C ATOM 3027 CZ PHE B 164 46.474 19.034 13.670 1.00 28.59 C ANISOU 3027 CZ PHE B 164 3777 3174 3912 -456 223 294 C ATOM 3028 N ILE B 165 49.278 12.747 12.328 1.00 23.72 N ANISOU 3028 N ILE B 165 2992 2832 3189 -235 215 504 N ATOM 3029 CA ILE B 165 49.546 11.396 12.766 1.00 25.84 C ANISOU 3029 CA ILE B 165 3218 3129 3470 -187 209 536 C ATOM 3030 C ILE B 165 49.634 11.432 14.289 1.00 26.75 C ANISOU 3030 C ILE B 165 3277 3314 3573 -221 127 545 C ATOM 3031 O ILE B 165 50.241 12.339 14.861 1.00 28.67 O ANISOU 3031 O ILE B 165 3467 3604 3822 -287 90 531 O ATOM 3032 CB ILE B 165 50.819 10.809 12.117 1.00 26.99 C ANISOU 3032 CB ILE B 165 3295 3281 3679 -148 276 588 C ATOM 3033 CG1 ILE B 165 52.022 11.739 12.288 1.00 25.93 C ANISOU 3033 CG1 ILE B 165 3069 3189 3593 -204 271 615 C ATOM 3034 CG2 ILE B 165 50.575 10.568 10.634 1.00 26.59 C ANISOU 3034 CG2 ILE B 165 3314 3179 3611 -110 363 565 C ATOM 3035 CD1 ILE B 165 53.297 11.200 11.651 1.00 24.32 C ANISOU 3035 CD1 ILE B 165 2781 2997 3462 -162 347 675 C ATOM 3036 N LYS B 166 48.982 10.466 14.933 1.00 24.69 N ANISOU 3036 N LYS B 166 3029 3064 3287 -184 103 562 N ATOM 3037 CA LYS B 166 48.782 10.478 16.378 1.00 24.68 C ANISOU 3037 CA LYS B 166 2993 3145 3240 -213 28 572 C ATOM 3038 C LYS B 166 49.370 9.222 17.012 1.00 24.77 C ANISOU 3038 C LYS B 166 2923 3210 3277 -156 20 675 C ATOM 3039 O LYS B 166 49.255 8.136 16.449 1.00 28.13 O ANISOU 3039 O LYS B 166 3364 3566 3759 -87 79 714 O ATOM 3040 CB LYS B 166 47.285 10.604 16.689 1.00 25.72 C ANISOU 3040 CB LYS B 166 3213 3246 3313 -219 13 518 C ATOM 3041 CG LYS B 166 46.900 10.440 18.149 1.00 25.99 C ANISOU 3041 CG LYS B 166 3224 3368 3282 -238 -46 530 C ATOM 3042 CD LYS B 166 45.411 10.669 18.327 1.00 26.98 C ANISOU 3042 CD LYS B 166 3432 3454 3364 -244 -43 472 C ATOM 3043 CE LYS B 166 44.968 10.322 19.726 1.00 28.96 C ANISOU 3043 CE LYS B 166 3664 3797 3544 -252 -83 496 C ATOM 3044 NZ LYS B 166 43.509 10.521 19.936 1.00 31.37 N ANISOU 3044 NZ LYS B 166 4038 4066 3815 -254 -69 443 N ATOM 3045 N THR B 167 50.003 9.363 18.175 1.00 26.87 N ANISOU 3045 N THR B 167 3100 3603 3508 -186 -51 720 N ATOM 3046 CA THR B 167 50.750 8.246 18.754 1.00 25.89 C ANISOU 3046 CA THR B 167 2872 3546 3417 -121 -60 853 C ATOM 3047 C THR B 167 49.870 7.092 19.223 1.00 26.28 C ANISOU 3047 C THR B 167 2957 3564 3464 -57 -42 918 C ATOM 3048 O THR B 167 50.137 5.950 18.871 1.00 25.23 O ANISOU 3048 O THR B 167 2797 3363 3424 25 22 1004 O ATOM 3049 CB THR B 167 51.631 8.683 19.958 1.00 28.35 C ANISOU 3049 CB THR B 167 3064 4043 3666 -173 -158 896 C ATOM 3050 OG1 THR B 167 50.805 9.037 21.075 1.00 26.37 O ANISOU 3050 OG1 THR B 167 2850 3879 3292 -223 -223 854 O ATOM 3051 CG2 THR B 167 52.537 9.855 19.575 1.00 31.32 C ANISOU 3051 CG2 THR B 167 3391 4447 4062 -256 -175 824 C ATOM 3052 N SER B 168 48.825 7.384 19.999 1.00 23.37 N ANISOU 3052 N SER B 168 2646 3231 3001 -95 -82 877 N ATOM 3053 CA SER B 168 48.163 6.342 20.789 1.00 25.25 C ANISOU 3053 CA SER B 168 2885 3482 3226 -44 -76 970 C ATOM 3054 C SER B 168 46.666 6.548 21.028 1.00 24.11 C ANISOU 3054 C SER B 168 2842 3298 3022 -74 -70 893 C ATOM 3055 O SER B 168 46.164 7.669 20.949 1.00 21.37 O ANISOU 3055 O SER B 168 2551 2956 2613 -139 -94 772 O ATOM 3056 CB SER B 168 48.859 6.224 22.145 1.00 26.78 C ANISOU 3056 CB SER B 168 2969 3865 3340 -45 -154 1084 C ATOM 3057 OG SER B 168 50.269 6.274 21.997 1.00 27.85 O ANISOU 3057 OG SER B 168 2991 4068 3522 -34 -177 1145 O ATOM 3058 N THR B 169 45.972 5.447 21.326 1.00 24.62 N ANISOU 3058 N THR B 169 2920 3315 3120 -23 -29 971 N ATOM 3059 CA THR B 169 44.563 5.462 21.725 1.00 25.20 C ANISOU 3059 CA THR B 169 3064 3367 3144 -46 -19 928 C ATOM 3060 C THR B 169 44.376 5.776 23.204 1.00 28.62 C ANISOU 3060 C THR B 169 3467 3967 3442 -73 -77 971 C ATOM 3061 O THR B 169 43.296 6.182 23.623 1.00 28.62 O ANISOU 3061 O THR B 169 3520 3979 3373 -107 -75 906 O ATOM 3062 CB THR B 169 43.868 4.103 21.479 1.00 25.41 C ANISOU 3062 CB THR B 169 3110 3269 3275 8 59 996 C ATOM 3063 OG1 THR B 169 44.577 3.076 22.186 1.00 28.47 O ANISOU 3063 OG1 THR B 169 3415 3696 3707 74 74 1171 O ATOM 3064 CG2 THR B 169 43.810 3.762 20.001 1.00 25.69 C ANISOU 3064 CG2 THR B 169 3191 3145 3423 21 122 916 C ATOM 3065 N GLY B 170 45.417 5.545 23.998 1.00 29.45 N ANISOU 3065 N GLY B 170 3477 4212 3502 -55 -124 1085 N ATOM 3066 CA GLY B 170 45.308 5.633 25.444 1.00 29.01 C ANISOU 3066 CA GLY B 170 3380 4346 3296 -75 -178 1149 C ATOM 3067 C GLY B 170 44.817 4.331 26.066 1.00 35.58 C ANISOU 3067 C GLY B 170 4191 5174 4154 -2 -130 1324 C ATOM 3068 O GLY B 170 44.698 4.224 27.290 1.00 37.61 O ANISOU 3068 O GLY B 170 4410 5600 4279 -4 -164 1414 O ATOM 3069 N LYS B 171 44.547 3.331 25.227 1.00 32.99 N ANISOU 3069 N LYS B 171 3886 4655 3995 58 -44 1374 N ATOM 3070 CA LYS B 171 43.902 2.102 25.689 1.00 32.86 C ANISOU 3070 CA LYS B 171 3862 4582 4042 116 27 1522 C ATOM 3071 C LYS B 171 44.845 0.903 25.778 1.00 36.23 C ANISOU 3071 C LYS B 171 4196 4981 4590 214 65 1731 C ATOM 3072 O LYS B 171 44.423 -0.187 26.163 1.00 38.42 O ANISOU 3072 O LYS B 171 4458 5193 4949 271 138 1880 O ATOM 3073 CB LYS B 171 42.723 1.747 24.773 1.00 31.11 C ANISOU 3073 CB LYS B 171 3730 4151 3939 102 110 1420 C ATOM 3074 CG LYS B 171 41.612 2.791 24.738 1.00 31.95 C ANISOU 3074 CG LYS B 171 3915 4275 3949 25 87 1250 C ATOM 3075 CD LYS B 171 40.977 2.980 26.108 1.00 33.04 C ANISOU 3075 CD LYS B 171 4044 4566 3941 7 70 1306 C ATOM 3076 N VAL B 172 46.114 1.087 25.427 1.00 36.68 N ANISOU 3076 N VAL B 172 4183 5079 4675 238 28 1751 N ATOM 3077 CA VAL B 172 47.069 -0.017 25.519 1.00 37.05 C ANISOU 3077 CA VAL B 172 4125 5102 4851 345 70 1961 C ATOM 3078 C VAL B 172 48.090 0.213 26.631 1.00 39.37 C ANISOU 3078 C VAL B 172 4288 5660 5009 365 -35 2117 C ATOM 3079 O VAL B 172 48.006 1.199 27.365 1.00 40.04 O ANISOU 3079 O VAL B 172 4374 5947 4892 284 -136 2042 O ATOM 3080 CB VAL B 172 47.806 -0.250 24.186 1.00 37.18 C ANISOU 3080 CB VAL B 172 4138 4948 5041 380 133 1897 C ATOM 3081 CG1 VAL B 172 46.819 -0.730 23.118 1.00 35.55 C ANISOU 3081 CG1 VAL B 172 4046 4494 4968 367 242 1766 C ATOM 3082 CG2 VAL B 172 48.536 1.019 23.737 1.00 34.68 C ANISOU 3082 CG2 VAL B 172 3812 4728 4636 311 48 1752 C ATOM 3083 N ALA B 173 49.034 -0.716 26.765 1.00 38.06 N ANISOU 3083 N ALA B 173 4005 5498 4957 473 -6 2331 N ATOM 3084 CA ALA B 173 50.025 -0.649 27.830 1.00 42.22 C ANISOU 3084 CA ALA B 173 4384 6296 5362 503 -109 2509 C ATOM 3085 C ALA B 173 50.861 0.619 27.721 1.00 43.21 C ANISOU 3085 C ALA B 173 4466 6589 5364 413 -231 2365 C ATOM 3086 O ALA B 173 50.940 1.411 28.662 1.00 44.49 O ANISOU 3086 O ALA B 173 4594 7001 5309 335 -349 2335 O ATOM 3087 CB ALA B 173 50.924 -1.881 27.801 1.00 41.58 C ANISOU 3087 CB ALA B 173 4185 6142 5473 621 -24 2676 C ATOM 3088 N ILE B 174 51.473 0.806 26.558 1.00 42.12 N ANISOU 3088 N ILE B 174 4328 6308 5368 416 -192 2264 N ATOM 3089 CA ILE B 174 52.347 1.942 26.321 1.00 41.14 C ANISOU 3089 CA ILE B 174 4154 6306 5173 332 -285 2135 C ATOM 3090 C ILE B 174 51.712 2.938 25.364 1.00 39.58 C ANISOU 3090 C ILE B 174 4101 5965 4972 231 -260 1864 C ATOM 3091 O ILE B 174 51.348 2.590 24.241 1.00 37.91 O ANISOU 3091 O ILE B 174 3974 5524 4907 261 -154 1793 O ATOM 3092 CB ILE B 174 53.697 1.491 25.748 1.00 38.14 C ANISOU 3092 CB ILE B 174 3637 5903 4953 415 -258 2250 C ATOM 3093 CG1 ILE B 174 54.399 0.556 26.731 1.00 36.07 C ANISOU 3093 CG1 ILE B 174 3206 5802 4697 527 -291 2547 C ATOM 3094 CG2 ILE B 174 54.558 2.697 25.403 1.00 36.63 C ANISOU 3094 CG2 ILE B 174 3394 5815 4708 315 -340 2104 C ATOM 3095 CD1 ILE B 174 55.579 -0.165 26.134 1.00 37.69 C ANISOU 3095 CD1 ILE B 174 3278 5934 5110 644 -224 2692 C ATOM 3096 N ASN B 175 51.577 4.178 25.813 1.00 38.36 N ANISOU 3096 N ASN B 175 3971 5952 4651 109 -355 1713 N ATOM 3097 CA ASN B 175 51.038 5.226 24.961 1.00 35.85 C ANISOU 3097 CA ASN B 175 3776 5509 4336 19 -333 1479 C ATOM 3098 C ASN B 175 52.144 6.174 24.501 1.00 35.03 C ANISOU 3098 C ASN B 175 3603 5458 4248 -48 -380 1391 C ATOM 3099 O ASN B 175 53.199 5.720 24.054 1.00 33.67 O ANISOU 3099 O ASN B 175 3327 5278 4188 11 -361 1491 O ATOM 3100 CB ASN B 175 49.927 5.967 25.695 1.00 38.87 C ANISOU 3100 CB ASN B 175 4253 5957 4558 -66 -370 1356 C ATOM 3101 CG ASN B 175 48.780 5.044 26.078 1.00 43.38 C ANISOU 3101 CG ASN B 175 4890 6464 5128 -5 -310 1441 C ATOM 3102 OD1 ASN B 175 48.242 4.316 25.236 1.00 41.49 O ANISOU 3102 OD1 ASN B 175 4714 6020 5031 54 -213 1454 O ATOM 3103 ND2 ASN B 175 48.418 5.049 27.356 1.00 46.86 N ANISOU 3103 ND2 ASN B 175 5310 7087 5407 -24 -362 1498 N ATOM 3104 N ALA B 176 51.915 7.477 24.609 1.00 33.61 N ANISOU 3104 N ALA B 176 3475 5322 3973 -169 -429 1209 N ATOM 3105 CA ALA B 176 52.899 8.457 24.146 1.00 33.02 C ANISOU 3105 CA ALA B 176 3341 5275 3930 -249 -461 1115 C ATOM 3106 C ALA B 176 54.259 8.291 24.832 1.00 36.13 C ANISOU 3106 C ALA B 176 3544 5886 4297 -253 -552 1236 C ATOM 3107 O ALA B 176 54.347 8.248 26.060 1.00 37.88 O ANISOU 3107 O ALA B 176 3695 6326 4371 -282 -647 1290 O ATOM 3108 CB ALA B 176 52.377 9.868 24.358 1.00 31.71 C ANISOU 3108 CB ALA B 176 3256 5120 3672 -383 -493 907 C ATOM 3109 N THR B 177 55.311 8.174 24.024 1.00 34.77 N ANISOU 3109 N THR B 177 3282 5667 4262 -222 -520 1286 N ATOM 3110 CA THR B 177 56.683 8.169 24.518 1.00 35.62 C ANISOU 3110 CA THR B 177 3189 5978 4366 -236 -606 1387 C ATOM 3111 C THR B 177 57.521 9.163 23.719 1.00 35.44 C ANISOU 3111 C THR B 177 3123 5913 4430 -327 -595 1270 C ATOM 3112 O THR B 177 57.233 9.417 22.549 1.00 34.54 O ANISOU 3112 O THR B 177 3114 5588 4422 -317 -490 1187 O ATOM 3113 CB THR B 177 57.338 6.774 24.423 1.00 35.33 C ANISOU 3113 CB THR B 177 3034 5943 4447 -76 -565 1632 C ATOM 3114 OG1 THR B 177 57.454 6.393 23.048 1.00 33.55 O ANISOU 3114 OG1 THR B 177 2861 5480 4407 0 -427 1624 O ATOM 3115 CG2 THR B 177 56.521 5.734 25.179 1.00 32.96 C ANISOU 3115 CG2 THR B 177 2773 5660 4088 19 -557 1772 C ATOM 3116 N PRO B 178 58.560 9.730 24.351 1.00 36.06 N ANISOU 3116 N PRO B 178 3037 6205 4458 -420 -704 1266 N ATOM 3117 CA PRO B 178 59.492 10.618 23.649 1.00 37.09 C ANISOU 3117 CA PRO B 178 3095 6307 4691 -510 -690 1177 C ATOM 3118 C PRO B 178 60.131 9.953 22.430 1.00 39.25 C ANISOU 3118 C PRO B 178 3327 6429 5159 -392 -570 1289 C ATOM 3119 O PRO B 178 60.231 10.588 21.383 1.00 40.16 O ANISOU 3119 O PRO B 178 3501 6388 5371 -431 -484 1191 O ATOM 3120 CB PRO B 178 60.547 10.932 24.714 1.00 37.95 C ANISOU 3120 CB PRO B 178 2995 6714 4712 -603 -841 1209 C ATOM 3121 CG PRO B 178 59.837 10.752 26.010 1.00 40.04 C ANISOU 3121 CG PRO B 178 3290 7154 4769 -622 -939 1212 C ATOM 3122 CD PRO B 178 58.871 9.626 25.789 1.00 38.23 C ANISOU 3122 CD PRO B 178 3186 6776 4564 -459 -849 1336 C ATOM 3123 N GLU B 179 60.544 8.695 22.563 1.00 40.36 N ANISOU 3123 N GLU B 179 3367 6610 5356 -246 -554 1495 N ATOM 3124 CA GLU B 179 61.199 7.986 21.462 1.00 41.25 C ANISOU 3124 CA GLU B 179 3431 6584 5660 -125 -426 1598 C ATOM 3125 C GLU B 179 60.291 7.840 20.236 1.00 38.06 C ANISOU 3125 C GLU B 179 3233 5904 5324 -76 -276 1503 C ATOM 3126 O GLU B 179 60.742 7.986 19.098 1.00 35.85 O ANISOU 3126 O GLU B 179 2958 5501 5161 -60 -169 1472 O ATOM 3127 CB GLU B 179 61.675 6.606 21.924 1.00 44.17 C ANISOU 3127 CB GLU B 179 3666 7028 6090 36 -423 1840 C ATOM 3128 N ALA B 180 59.013 7.553 20.463 1.00 32.88 N ANISOU 3128 N ALA B 180 2738 5167 4588 -56 -267 1460 N ATOM 3129 CA ALA B 180 58.082 7.400 19.351 1.00 33.24 C ANISOU 3129 CA ALA B 180 2968 4980 4681 -19 -143 1367 C ATOM 3130 C ALA B 180 57.815 8.750 18.690 1.00 35.04 C ANISOU 3130 C ALA B 180 3292 5141 4879 -140 -132 1189 C ATOM 3131 O ALA B 180 57.650 8.835 17.469 1.00 32.71 O ANISOU 3131 O ALA B 180 3085 4692 4652 -118 -23 1133 O ATOM 3132 CB ALA B 180 56.781 6.768 19.822 1.00 33.06 C ANISOU 3132 CB ALA B 180 3073 4902 4588 23 -144 1371 C ATOM 3133 N ALA B 181 57.783 9.801 19.506 1.00 35.60 N ANISOU 3133 N ALA B 181 3344 5332 4850 -269 -239 1102 N ATOM 3134 CA ALA B 181 57.570 11.158 19.018 1.00 32.54 C ANISOU 3134 CA ALA B 181 3034 4875 4454 -388 -225 944 C ATOM 3135 C ALA B 181 58.687 11.587 18.076 1.00 32.67 C ANISOU 3135 C ALA B 181 2963 4857 4594 -410 -159 954 C ATOM 3136 O ALA B 181 58.431 12.173 17.022 1.00 32.41 O ANISOU 3136 O ALA B 181 3027 4682 4607 -428 -69 884 O ATOM 3137 CB ALA B 181 57.464 12.129 20.182 1.00 33.88 C ANISOU 3137 CB ALA B 181 3178 5184 4511 -525 -343 842 C ATOM 3138 N LYS B 182 59.926 11.298 18.468 1.00 32.69 N ANISOU 3138 N LYS B 182 2774 5001 4647 -405 -203 1054 N ATOM 3139 CA LYS B 182 61.089 11.658 17.666 1.00 35.63 C ANISOU 3139 CA LYS B 182 3033 5361 5145 -426 -138 1079 C ATOM 3140 C LYS B 182 61.006 11.035 16.278 1.00 35.44 C ANISOU 3140 C LYS B 182 3088 5163 5214 -309 22 1119 C ATOM 3141 O LYS B 182 61.242 11.709 15.276 1.00 37.38 O ANISOU 3141 O LYS B 182 3368 5318 5519 -346 111 1068 O ATOM 3142 CB LYS B 182 62.386 11.227 18.360 1.00 36.40 C ANISOU 3142 CB LYS B 182 2890 5654 5285 -414 -214 1208 C ATOM 3143 N VAL B 183 60.661 9.754 16.225 1.00 33.80 N ANISOU 3143 N VAL B 183 2912 4912 5019 -171 64 1205 N ATOM 3144 CA VAL B 183 60.525 9.055 14.953 1.00 33.65 C ANISOU 3144 CA VAL B 183 2975 4735 5077 -64 219 1217 C ATOM 3145 C VAL B 183 59.461 9.710 14.078 1.00 31.07 C ANISOU 3145 C VAL B 183 2847 4272 4687 -107 275 1085 C ATOM 3146 O VAL B 183 59.712 10.025 12.915 1.00 32.97 O ANISOU 3146 O VAL B 183 3123 4435 4970 -104 383 1056 O ATOM 3147 CB VAL B 183 60.173 7.565 15.155 1.00 33.36 C ANISOU 3147 CB VAL B 183 2953 4652 5071 77 257 1310 C ATOM 3148 CG1 VAL B 183 59.865 6.906 13.818 1.00 33.83 C ANISOU 3148 CG1 VAL B 183 3124 4538 5192 164 421 1271 C ATOM 3149 CG2 VAL B 183 61.317 6.841 15.855 1.00 34.82 C ANISOU 3149 CG2 VAL B 183 2926 4962 5344 150 226 1478 C ATOM 3150 N MET B 184 58.281 9.931 14.649 1.00 29.66 N ANISOU 3150 N MET B 184 2787 4080 4404 -145 202 1015 N ATOM 3151 CA MET B 184 57.155 10.477 13.893 1.00 27.74 C ANISOU 3151 CA MET B 184 2720 3718 4100 -171 245 909 C ATOM 3152 C MET B 184 57.397 11.902 13.393 1.00 28.46 C ANISOU 3152 C MET B 184 2825 3790 4199 -275 261 844 C ATOM 3153 O MET B 184 57.121 12.205 12.233 1.00 27.28 O ANISOU 3153 O MET B 184 2764 3548 4052 -262 353 816 O ATOM 3154 CB MET B 184 55.890 10.420 14.743 1.00 24.91 C ANISOU 3154 CB MET B 184 2460 3363 3642 -188 163 860 C ATOM 3155 CG MET B 184 55.468 8.984 15.054 1.00 25.28 C ANISOU 3155 CG MET B 184 2520 3391 3696 -83 175 928 C ATOM 3156 SD MET B 184 54.099 8.855 16.202 1.00 30.44 S ANISOU 3156 SD MET B 184 3258 4070 4238 -103 83 897 S ATOM 3157 CE MET B 184 52.806 9.678 15.267 1.00 24.86 C ANISOU 3157 CE MET B 184 2727 3243 3477 -146 122 761 C ATOM 3158 N LEU B 185 57.918 12.768 14.259 1.00 31.26 N ANISOU 3158 N LEU B 185 3088 4235 4557 -381 175 821 N ATOM 3159 CA LEU B 185 58.259 14.138 13.863 1.00 32.83 C ANISOU 3159 CA LEU B 185 3280 4397 4796 -490 200 763 C ATOM 3160 C LEU B 185 59.318 14.171 12.765 1.00 33.40 C ANISOU 3160 C LEU B 185 3278 4443 4971 -468 313 827 C ATOM 3161 O LEU B 185 59.339 15.086 11.939 1.00 38.24 O ANISOU 3161 O LEU B 185 3936 4976 5616 -516 389 804 O ATOM 3162 CB LEU B 185 58.749 14.951 15.067 1.00 32.94 C ANISOU 3162 CB LEU B 185 3188 4521 4806 -621 89 710 C ATOM 3163 CG LEU B 185 57.738 15.309 16.163 1.00 30.03 C ANISOU 3163 CG LEU B 185 2898 4181 4331 -678 -9 614 C ATOM 3164 CD1 LEU B 185 58.465 15.781 17.409 1.00 29.26 C ANISOU 3164 CD1 LEU B 185 2661 4244 4211 -797 -124 568 C ATOM 3165 CD2 LEU B 185 56.749 16.367 15.681 1.00 26.86 C ANISOU 3165 CD2 LEU B 185 2647 3634 3926 -724 43 517 C ATOM 3166 N THR B 186 60.202 13.181 12.756 1.00 33.10 N ANISOU 3166 N THR B 186 3119 4470 4988 -390 335 919 N ATOM 3167 CA THR B 186 61.263 13.133 11.752 1.00 31.47 C ANISOU 3167 CA THR B 186 2827 4249 4883 -361 455 983 C ATOM 3168 C THR B 186 60.692 12.770 10.386 1.00 29.05 C ANISOU 3168 C THR B 186 2664 3825 4547 -274 591 974 C ATOM 3169 O THR B 186 61.091 13.342 9.369 1.00 27.11 O ANISOU 3169 O THR B 186 2426 3539 4337 -292 697 985 O ATOM 3170 CB THR B 186 62.372 12.131 12.135 1.00 34.48 C ANISOU 3170 CB THR B 186 3026 4730 5347 -286 452 1092 C ATOM 3171 OG1 THR B 186 63.000 12.558 13.351 1.00 35.18 O ANISOU 3171 OG1 THR B 186 2959 4963 5446 -380 316 1104 O ATOM 3172 CG2 THR B 186 63.424 12.053 11.036 1.00 29.63 C ANISOU 3172 CG2 THR B 186 2325 4093 4841 -245 598 1153 C ATOM 3173 N VAL B 187 59.751 11.826 10.371 1.00 27.45 N ANISOU 3173 N VAL B 187 2572 3581 4276 -188 588 954 N ATOM 3174 CA VAL B 187 59.054 11.460 9.140 1.00 28.47 C ANISOU 3174 CA VAL B 187 2846 3621 4351 -122 696 918 C ATOM 3175 C VAL B 187 58.323 12.671 8.566 1.00 29.75 C ANISOU 3175 C VAL B 187 3124 3734 4445 -193 703 867 C ATOM 3176 O VAL B 187 58.402 12.941 7.370 1.00 32.96 O ANISOU 3176 O VAL B 187 3581 4108 4833 -177 812 875 O ATOM 3177 CB VAL B 187 58.047 10.311 9.371 1.00 28.27 C ANISOU 3177 CB VAL B 187 2916 3556 4270 -44 674 886 C ATOM 3178 CG1 VAL B 187 57.217 10.063 8.114 1.00 28.42 C ANISOU 3178 CG1 VAL B 187 3085 3502 4211 -3 766 822 C ATOM 3179 CG2 VAL B 187 58.780 9.041 9.789 1.00 29.54 C ANISOU 3179 CG2 VAL B 187 2964 3737 4522 48 700 959 C ATOM 3180 N ILE B 188 57.623 13.399 9.433 1.00 28.10 N ANISOU 3180 N ILE B 188 2953 3523 4199 -267 594 822 N ATOM 3181 CA ILE B 188 56.932 14.627 9.054 1.00 27.35 C ANISOU 3181 CA ILE B 188 2953 3369 4068 -332 599 786 C ATOM 3182 C ILE B 188 57.889 15.624 8.407 1.00 29.31 C ANISOU 3182 C ILE B 188 3134 3603 4399 -392 682 831 C ATOM 3183 O ILE B 188 57.605 16.174 7.338 1.00 27.96 O ANISOU 3183 O ILE B 188 3041 3381 4202 -383 769 856 O ATOM 3184 CB ILE B 188 56.258 15.292 10.282 1.00 27.10 C ANISOU 3184 CB ILE B 188 2941 3339 4017 -410 479 722 C ATOM 3185 CG1 ILE B 188 55.096 14.437 10.786 1.00 26.27 C ANISOU 3185 CG1 ILE B 188 2922 3235 3822 -352 414 684 C ATOM 3186 CG2 ILE B 188 55.783 16.697 9.946 1.00 24.29 C ANISOU 3186 CG2 ILE B 188 2653 2903 3674 -480 504 696 C ATOM 3187 CD1 ILE B 188 54.455 14.955 12.067 1.00 26.88 C ANISOU 3187 CD1 ILE B 188 3014 3333 3868 -418 306 620 C ATOM 3188 N LYS B 189 59.028 15.850 9.058 1.00 31.33 N ANISOU 3188 N LYS B 189 3237 3914 4753 -455 655 851 N ATOM 3189 CA LYS B 189 60.028 16.782 8.547 1.00 33.44 C ANISOU 3189 CA LYS B 189 3416 4166 5122 -528 735 895 C ATOM 3190 C LYS B 189 60.543 16.324 7.185 1.00 34.80 C ANISOU 3190 C LYS B 189 3590 4334 5298 -444 885 969 C ATOM 3191 O LYS B 189 60.716 17.128 6.273 1.00 35.33 O ANISOU 3191 O LYS B 189 3682 4355 5388 -471 986 1013 O ATOM 3192 CB LYS B 189 61.192 16.924 9.535 1.00 33.90 C ANISOU 3192 CB LYS B 189 3285 4312 5281 -612 667 897 C ATOM 3193 CG LYS B 189 62.245 17.960 9.128 1.00 33.18 C ANISOU 3193 CG LYS B 189 3084 4203 5320 -713 744 931 C ATOM 3194 N ASN B 190 60.758 15.021 7.051 1.00 33.93 N ANISOU 3194 N ASN B 190 3458 4269 5166 -341 908 985 N ATOM 3195 CA ASN B 190 61.333 14.447 5.839 1.00 36.71 C ANISOU 3195 CA ASN B 190 3801 4626 5522 -258 1060 1035 C ATOM 3196 C ASN B 190 60.352 14.327 4.662 1.00 33.10 C ANISOU 3196 C ASN B 190 3519 4129 4930 -199 1138 1010 C ATOM 3197 O ASN B 190 60.769 14.324 3.503 1.00 32.68 O ANISOU 3197 O ASN B 190 3477 4086 4856 -164 1277 1049 O ATOM 3198 CB ASN B 190 61.922 13.072 6.172 1.00 42.71 C ANISOU 3198 CB ASN B 190 4468 5431 6329 -165 1070 1053 C ATOM 3199 CG ASN B 190 62.671 12.452 5.012 1.00 51.32 C ANISOU 3199 CG ASN B 190 5528 6525 7448 -80 1244 1091 C ATOM 3200 OD1 ASN B 190 62.338 11.351 4.562 1.00 55.75 O ANISOU 3200 OD1 ASN B 190 6155 7062 7963 20 1306 1056 O ATOM 3201 ND2 ASN B 190 63.693 13.150 4.522 1.00 52.42 N ANISOU 3201 ND2 ASN B 190 5562 6688 7667 -123 1334 1156 N ATOM 3202 N LYS B 191 59.054 14.252 4.959 1.00 32.03 N ANISOU 3202 N LYS B 191 3511 3964 4696 -193 1049 948 N ATOM 3203 CA LYS B 191 58.047 13.921 3.944 1.00 33.34 C ANISOU 3203 CA LYS B 191 3828 4120 4721 -134 1096 914 C ATOM 3204 C LYS B 191 57.014 15.015 3.643 1.00 34.07 C ANISOU 3204 C LYS B 191 4029 4181 4735 -176 1062 921 C ATOM 3205 O LYS B 191 56.741 15.308 2.481 1.00 34.73 O ANISOU 3205 O LYS B 191 4184 4283 4728 -152 1145 956 O ATOM 3206 CB LYS B 191 57.301 12.649 4.357 1.00 32.70 C ANISOU 3206 CB LYS B 191 3802 4033 4589 -72 1039 837 C ATOM 3207 CG LYS B 191 58.192 11.423 4.480 1.00 33.90 C ANISOU 3207 CG LYS B 191 3863 4196 4822 -3 1099 840 C ATOM 3208 CD LYS B 191 58.775 11.026 3.136 1.00 38.78 C ANISOU 3208 CD LYS B 191 4490 4831 5414 54 1267 842 C ATOM 3209 CE LYS B 191 59.496 9.686 3.225 1.00 42.36 C ANISOU 3209 CE LYS B 191 4867 5269 5959 140 1344 831 C ATOM 3210 NZ LYS B 191 59.912 9.208 1.880 1.00 45.84 N ANISOU 3210 NZ LYS B 191 5339 5721 6356 198 1523 800 N ATOM 3211 N ASN B 192 56.421 15.594 4.685 1.00 33.71 N ANISOU 3211 N ASN B 192 3992 4096 4720 -233 945 893 N ATOM 3212 CA ASN B 192 55.341 16.564 4.515 1.00 31.01 C ANISOU 3212 CA ASN B 192 3748 3709 4324 -258 913 900 C ATOM 3213 C ASN B 192 55.137 17.362 5.795 1.00 29.38 C ANISOU 3213 C ASN B 192 3511 3451 4203 -340 814 864 C ATOM 3214 O ASN B 192 54.558 16.861 6.764 1.00 26.19 O ANISOU 3214 O ASN B 192 3121 3055 3776 -338 714 795 O ATOM 3215 CB ASN B 192 54.044 15.853 4.119 1.00 30.71 C ANISOU 3215 CB ASN B 192 3829 3695 4145 -193 876 851 C ATOM 3216 CG ASN B 192 52.947 16.813 3.699 1.00 30.77 C ANISOU 3216 CG ASN B 192 3925 3677 4090 -197 859 887 C ATOM 3217 OD1 ASN B 192 52.996 18.010 3.985 1.00 32.20 O ANISOU 3217 OD1 ASN B 192 4089 3793 4352 -249 861 933 O ATOM 3218 ND2 ASN B 192 51.940 16.284 3.014 1.00 31.34 N ANISOU 3218 ND2 ASN B 192 4085 3798 4024 -142 846 864 N ATOM 3219 N THR B 193 55.608 18.606 5.787 1.00 30.76 N ANISOU 3219 N THR B 193 3644 3568 4474 -415 854 907 N ATOM 3220 CA THR B 193 55.600 19.439 6.984 1.00 32.49 C ANISOU 3220 CA THR B 193 3823 3733 4788 -512 780 849 C ATOM 3221 C THR B 193 54.229 20.040 7.285 1.00 32.98 C ANISOU 3221 C THR B 193 3992 3726 4813 -510 731 812 C ATOM 3222 O THR B 193 54.059 20.731 8.288 1.00 33.19 O ANISOU 3222 O THR B 193 4003 3701 4905 -586 678 742 O ATOM 3223 CB THR B 193 56.629 20.579 6.867 1.00 33.75 C ANISOU 3223 CB THR B 193 3894 3837 5094 -608 854 892 C ATOM 3224 OG1 THR B 193 56.349 21.359 5.697 1.00 35.59 O ANISOU 3224 OG1 THR B 193 4192 4002 5328 -583 965 993 O ATOM 3225 CG2 THR B 193 58.042 20.007 6.774 1.00 30.87 C ANISOU 3225 CG2 THR B 193 3394 3551 4786 -620 891 923 C ATOM 3226 N ALA B 194 53.256 19.773 6.418 1.00 32.00 N ANISOU 3226 N ALA B 194 3968 3609 4580 -424 751 853 N ATOM 3227 CA ALA B 194 51.895 20.244 6.633 1.00 30.04 C ANISOU 3227 CA ALA B 194 3809 3309 4296 -404 706 833 C ATOM 3228 C ALA B 194 51.119 19.258 7.496 1.00 32.86 C ANISOU 3228 C ALA B 194 4194 3716 4574 -377 600 740 C ATOM 3229 O ALA B 194 50.021 19.559 7.959 1.00 31.55 O ANISOU 3229 O ALA B 194 4083 3514 4390 -370 552 703 O ATOM 3230 CB ALA B 194 51.185 20.462 5.305 1.00 28.51 C ANISOU 3230 CB ALA B 194 3692 3124 4016 -329 767 934 C ATOM 3231 N VAL B 195 51.696 18.076 7.707 1.00 31.83 N ANISOU 3231 N VAL B 195 4020 3663 4411 -358 575 711 N ATOM 3232 CA VAL B 195 51.067 17.057 8.540 1.00 29.45 C ANISOU 3232 CA VAL B 195 3735 3404 4051 -331 488 642 C ATOM 3233 C VAL B 195 51.369 17.298 10.019 1.00 30.16 C ANISOU 3233 C VAL B 195 3762 3499 4197 -403 412 580 C ATOM 3234 O VAL B 195 52.529 17.457 10.408 1.00 31.26 O ANISOU 3234 O VAL B 195 3805 3665 4406 -457 415 584 O ATOM 3235 CB VAL B 195 51.534 15.641 8.146 1.00 28.94 C ANISOU 3235 CB VAL B 195 3648 3402 3945 -271 508 647 C ATOM 3236 CG1 VAL B 195 51.003 14.608 9.129 1.00 27.78 C ANISOU 3236 CG1 VAL B 195 3504 3282 3769 -249 428 595 C ATOM 3237 CG2 VAL B 195 51.093 15.308 6.727 1.00 28.15 C ANISOU 3237 CG2 VAL B 195 3621 3317 3757 -208 575 674 C ATOM 3238 N GLY B 196 50.324 17.321 10.842 1.00 25.69 N ANISOU 3238 N GLY B 196 3245 2925 3593 -406 346 521 N ATOM 3239 CA GLY B 196 50.475 17.617 12.255 1.00 21.90 C ANISOU 3239 CA GLY B 196 2717 2468 3134 -478 276 450 C ATOM 3240 C GLY B 196 50.836 16.411 13.105 1.00 23.76 C ANISOU 3240 C GLY B 196 2894 2805 3327 -460 209 446 C ATOM 3241 O GLY B 196 50.797 15.274 12.637 1.00 23.31 O ANISOU 3241 O GLY B 196 2846 2773 3238 -385 223 490 O ATOM 3242 N PHE B 197 51.177 16.668 14.365 1.00 27.47 N ANISOU 3242 N PHE B 197 3304 3336 3797 -531 142 393 N ATOM 3243 CA PHE B 197 51.568 15.619 15.305 1.00 28.33 C ANISOU 3243 CA PHE B 197 3341 3561 3860 -515 72 414 C ATOM 3244 C PHE B 197 50.759 15.693 16.606 1.00 27.92 C ANISOU 3244 C PHE B 197 3315 3562 3730 -547 -1 346 C ATOM 3245 O PHE B 197 50.602 16.768 17.187 1.00 29.67 O ANISOU 3245 O PHE B 197 3547 3773 3954 -633 -16 254 O ATOM 3246 CB PHE B 197 53.068 15.721 15.605 1.00 26.89 C ANISOU 3246 CB PHE B 197 3020 3463 3733 -571 52 441 C ATOM 3247 CG PHE B 197 53.554 14.743 16.638 1.00 27.29 C ANISOU 3247 CG PHE B 197 2976 3654 3738 -552 -28 487 C ATOM 3248 CD1 PHE B 197 53.449 13.375 16.424 1.00 31.17 C ANISOU 3248 CD1 PHE B 197 3467 4157 4220 -441 -12 577 C ATOM 3249 CD2 PHE B 197 54.135 15.190 17.814 1.00 27.08 C ANISOU 3249 CD2 PHE B 197 2854 3753 3681 -646 -114 443 C ATOM 3250 CE1 PHE B 197 53.905 12.470 17.375 1.00 32.15 C ANISOU 3250 CE1 PHE B 197 3495 4403 4316 -410 -76 651 C ATOM 3251 CE2 PHE B 197 54.596 14.295 18.765 1.00 30.27 C ANISOU 3251 CE2 PHE B 197 3158 4312 4029 -621 -194 513 C ATOM 3252 CZ PHE B 197 54.479 12.933 18.549 1.00 30.34 C ANISOU 3252 CZ PHE B 197 3165 4320 4041 -495 -172 631 C ATOM 3253 N LYS B 198 50.255 14.551 17.067 1.00 26.74 N ANISOU 3253 N LYS B 198 3176 3465 3518 -481 -35 388 N ATOM 3254 CA LYS B 198 49.479 14.505 18.305 1.00 25.54 C ANISOU 3254 CA LYS B 198 3046 3380 3278 -503 -94 340 C ATOM 3255 C LYS B 198 49.940 13.380 19.241 1.00 25.90 C ANISOU 3255 C LYS B 198 3008 3562 3270 -472 -155 421 C ATOM 3256 O LYS B 198 49.559 12.224 19.066 1.00 26.14 O ANISOU 3256 O LYS B 198 3056 3576 3301 -385 -137 500 O ATOM 3257 CB LYS B 198 47.985 14.348 17.990 1.00 26.96 C ANISOU 3257 CB LYS B 198 3338 3473 3432 -450 -62 320 C ATOM 3258 CG LYS B 198 47.079 14.228 19.216 1.00 27.18 C ANISOU 3258 CG LYS B 198 3391 3565 3372 -462 -104 279 C ATOM 3259 CD LYS B 198 45.598 14.324 18.839 1.00 28.14 C ANISOU 3259 CD LYS B 198 3609 3593 3489 -422 -65 250 C ATOM 3260 CE LYS B 198 44.696 14.022 20.038 1.00 29.75 C ANISOU 3260 CE LYS B 198 3830 3865 3608 -423 -92 226 C ATOM 3261 NZ LYS B 198 43.233 14.108 19.747 1.00 26.30 N ANISOU 3261 NZ LYS B 198 3468 3350 3176 -385 -55 201 N ATOM 3262 N PRO B 199 50.782 13.717 20.231 1.00 25.66 N ANISOU 3262 N PRO B 199 2881 3671 3198 -545 -225 404 N ATOM 3263 CA PRO B 199 51.071 12.747 21.289 1.00 27.63 C ANISOU 3263 CA PRO B 199 3050 4079 3370 -514 -294 496 C ATOM 3264 C PRO B 199 49.853 12.610 22.190 1.00 32.41 C ANISOU 3264 C PRO B 199 3730 4719 3866 -511 -313 461 C ATOM 3265 O PRO B 199 49.253 13.626 22.546 1.00 34.15 O ANISOU 3265 O PRO B 199 4011 4924 4042 -584 -314 329 O ATOM 3266 CB PRO B 199 52.254 13.370 22.032 1.00 26.09 C ANISOU 3266 CB PRO B 199 2728 4042 3144 -614 -372 465 C ATOM 3267 CG PRO B 199 52.095 14.841 21.813 1.00 26.17 C ANISOU 3267 CG PRO B 199 2791 3969 3181 -725 -348 302 C ATOM 3268 CD PRO B 199 51.519 14.980 20.423 1.00 26.25 C ANISOU 3268 CD PRO B 199 2907 3773 3295 -664 -246 306 C ATOM 3269 N ALA B 200 49.477 11.384 22.534 1.00 33.17 N ANISOU 3269 N ALA B 200 3821 4848 3934 -424 -314 578 N ATOM 3270 CA ALA B 200 48.288 11.168 23.348 1.00 33.46 C ANISOU 3270 CA ALA B 200 3924 4915 3876 -415 -317 562 C ATOM 3271 C ALA B 200 48.499 10.064 24.375 1.00 36.51 C ANISOU 3271 C ALA B 200 4233 5452 4186 -364 -361 710 C ATOM 3272 O ALA B 200 49.216 9.096 24.122 1.00 35.19 O ANISOU 3272 O ALA B 200 3991 5289 4089 -290 -355 853 O ATOM 3273 CB ALA B 200 47.102 10.841 22.463 1.00 31.17 C ANISOU 3273 CB ALA B 200 3743 4449 3652 -356 -239 549 C ATOM 3274 N GLY B 201 47.860 10.216 25.533 1.00 38.64 N ANISOU 3274 N GLY B 201 4520 5844 4316 -398 -395 684 N ATOM 3275 CA GLY B 201 47.924 9.212 26.580 1.00 39.89 C ANISOU 3275 CA GLY B 201 4613 6161 4384 -347 -431 842 C ATOM 3276 C GLY B 201 49.185 9.297 27.422 1.00 42.70 C ANISOU 3276 C GLY B 201 4829 6752 4645 -386 -533 904 C ATOM 3277 O GLY B 201 50.287 9.053 26.930 1.00 43.23 O ANISOU 3277 O GLY B 201 4802 6821 4802 -361 -552 979 O ATOM 3278 N GLY B 202 49.019 9.650 28.695 1.00 42.75 N ANISOU 3278 N GLY B 202 4815 6969 4460 -449 -597 868 N ATOM 3279 CA GLY B 202 50.127 9.688 29.633 1.00 45.67 C ANISOU 3279 CA GLY B 202 5041 7611 4700 -493 -711 931 C ATOM 3280 C GLY B 202 50.746 11.057 29.860 1.00 48.06 C ANISOU 3280 C GLY B 202 5313 8013 4934 -646 -779 722 C ATOM 3281 O GLY B 202 51.628 11.214 30.708 1.00 50.37 O ANISOU 3281 O GLY B 202 5482 8562 5096 -710 -887 739 O ATOM 3282 N VAL B 203 50.300 12.056 29.106 1.00 45.03 N ANISOU 3282 N VAL B 203 5034 7432 4644 -708 -716 527 N ATOM 3283 CA VAL B 203 50.819 13.407 29.292 1.00 45.84 C ANISOU 3283 CA VAL B 203 5117 7587 4713 -861 -757 315 C ATOM 3284 C VAL B 203 50.113 14.060 30.481 1.00 45.65 C ANISOU 3284 C VAL B 203 5147 7707 4493 -953 -776 155 C ATOM 3285 O VAL B 203 49.035 14.635 30.335 1.00 43.20 O ANISOU 3285 O VAL B 203 4967 7244 4203 -966 -690 21 O ATOM 3286 CB VAL B 203 50.640 14.266 28.026 1.00 45.54 C ANISOU 3286 CB VAL B 203 5166 7274 4864 -886 -668 187 C ATOM 3287 CG1 VAL B 203 51.385 15.592 28.176 1.00 48.42 C ANISOU 3287 CG1 VAL B 203 5487 7678 5234 -1047 -703 -8 C ATOM 3288 CG2 VAL B 203 51.134 13.510 26.797 1.00 42.06 C ANISOU 3288 CG2 VAL B 203 4696 6687 4599 -780 -626 344 C ATOM 3289 N ARG B 204 50.728 13.968 31.658 1.00 47.33 N ANISOU 3289 N ARG B 204 5252 8223 4507 -1016 -885 172 N ATOM 3290 CA ARG B 204 50.058 14.352 32.900 1.00 47.44 C ANISOU 3290 CA ARG B 204 5311 8420 4295 -1089 -902 47 C ATOM 3291 C ARG B 204 50.191 15.836 33.249 1.00 47.69 C ANISOU 3291 C ARG B 204 5369 8474 4276 -1270 -908 -262 C ATOM 3292 O ARG B 204 49.269 16.424 33.820 1.00 49.75 O ANISOU 3292 O ARG B 204 5732 8731 4440 -1320 -850 -432 O ATOM 3293 CB ARG B 204 50.586 13.505 34.064 1.00 51.31 C ANISOU 3293 CB ARG B 204 5674 9260 4562 -1067 -1017 222 C ATOM 3294 N ASN B 205 51.323 16.446 32.910 1.00 45.73 N ANISOU 3294 N ASN B 205 5027 8240 4109 -1370 -966 -341 N ATOM 3295 CA ASN B 205 51.570 17.831 33.305 1.00 46.70 C ANISOU 3295 CA ASN B 205 5158 8390 4196 -1561 -973 -641 C ATOM 3296 C ASN B 205 52.479 18.608 32.353 1.00 46.43 C ANISOU 3296 C ASN B 205 5073 8188 4381 -1643 -963 -725 C ATOM 3297 O ASN B 205 52.903 18.091 31.318 1.00 44.47 O ANISOU 3297 O ASN B 205 4790 7801 4308 -1546 -945 -551 O ATOM 3298 CB ASN B 205 52.163 17.864 34.713 1.00 49.81 C ANISOU 3298 CB ASN B 205 5458 9105 4362 -1636 -1070 -683 C ATOM 3299 CG ASN B 205 53.328 16.914 34.868 1.00 50.86 C ANISOU 3299 CG ASN B 205 5421 9436 4468 -1570 -1184 -437 C ATOM 3300 OD1 ASN B 205 54.240 16.889 34.040 1.00 47.78 O ANISOU 3300 OD1 ASN B 205 4934 8988 4232 -1580 -1222 -371 O ATOM 3301 ND2 ASN B 205 53.296 16.107 35.923 1.00 54.93 N ANISOU 3301 ND2 ASN B 205 5894 10177 4802 -1496 -1226 -286 N ATOM 3302 N ALA B 206 52.778 19.850 32.727 1.00 47.49 N ANISOU 3302 N ALA B 206 5202 8337 4505 -1829 -965 -999 N ATOM 3303 CA ALA B 206 53.571 20.756 31.898 1.00 46.13 C ANISOU 3303 CA ALA B 206 4988 7988 4550 -1932 -935 -1106 C ATOM 3304 C ALA B 206 54.961 20.200 31.587 1.00 49.55 C ANISOU 3304 C ALA B 206 5235 8564 5029 -1931 -1046 -935 C ATOM 3305 O ALA B 206 55.474 20.392 30.483 1.00 50.93 O ANISOU 3305 O ALA B 206 5384 8539 5426 -1912 -993 -879 O ATOM 3306 CB ALA B 206 53.688 22.114 32.572 1.00 43.86 C ANISOU 3306 CB ALA B 206 4737 7663 4263 -2084 -890 -1396 C ATOM 3307 N ASP B 207 55.567 19.520 32.559 1.00 49.48 N ANISOU 3307 N ASP B 207 5117 8839 4843 -1894 -1155 -818 N ATOM 3308 CA ASP B 207 56.864 18.883 32.350 1.00 49.36 C ANISOU 3308 CA ASP B 207 4920 8962 4872 -1859 -1250 -625 C ATOM 3309 C ASP B 207 56.774 17.828 31.255 1.00 48.44 C ANISOU 3309 C ASP B 207 4776 8748 4881 -1708 -1232 -368 C ATOM 3310 O ASP B 207 57.638 17.758 30.384 1.00 47.66 O ANISOU 3310 O ASP B 207 4586 8560 4962 -1689 -1222 -277 O ATOM 3311 CB ASP B 207 57.382 18.256 33.646 1.00 51.99 C ANISOU 3311 CB ASP B 207 5155 9612 4987 -1825 -1356 -520 C ATOM 3312 CG ASP B 207 58.011 19.276 34.577 1.00 59.20 C ANISOU 3312 CG ASP B 207 6027 10650 5816 -1987 -1398 -746 C ATOM 3313 OD1 ASP B 207 58.370 20.377 34.107 1.00 59.07 O ANISOU 3313 OD1 ASP B 207 6019 10474 5951 -2118 -1357 -945 O ATOM 3314 OD2 ASP B 207 58.158 18.974 35.779 1.00 64.99 O ANISOU 3314 OD2 ASP B 207 6717 11639 6338 -1985 -1467 -720 O ATOM 3315 N ASP B 208 55.722 17.016 31.300 1.00 48.65 N ANISOU 3315 N ASP B 208 4920 8712 4851 -1555 -1177 -241 N ATOM 3316 CA ASP B 208 55.469 16.043 30.243 1.00 46.99 C ANISOU 3316 CA ASP B 208 4754 8295 4803 -1363 -1094 -15 C ATOM 3317 C ASP B 208 55.254 16.752 28.911 1.00 43.45 C ANISOU 3317 C ASP B 208 4410 7509 4591 -1367 -965 -106 C ATOM 3318 O ASP B 208 55.819 16.365 27.886 1.00 41.26 O ANISOU 3318 O ASP B 208 4087 7108 4481 -1290 -925 25 O ATOM 3319 CB ASP B 208 54.254 15.174 30.575 1.00 48.33 C ANISOU 3319 CB ASP B 208 5041 8444 4877 -1228 -1048 96 C ATOM 3320 CG ASP B 208 54.528 14.174 31.682 1.00 51.60 C ANISOU 3320 CG ASP B 208 5342 9172 5092 -1172 -1157 281 C ATOM 3321 OD1 ASP B 208 55.712 13.870 31.937 1.00 53.52 O ANISOU 3321 OD1 ASP B 208 5403 9620 5310 -1187 -1264 393 O ATOM 3322 OD2 ASP B 208 53.551 13.681 32.286 1.00 53.66 O ANISOU 3322 OD2 ASP B 208 5687 9475 5224 -1108 -1132 331 O ATOM 3323 N ALA B 209 54.427 17.793 28.937 1.00 40.32 N ANISOU 3323 N ALA B 209 4149 6967 4204 -1451 -892 -323 N ATOM 3324 CA ALA B 209 54.154 18.588 27.747 1.00 39.02 C ANISOU 3324 CA ALA B 209 4083 6492 4252 -1458 -768 -405 C ATOM 3325 C ALA B 209 55.434 19.146 27.129 1.00 39.73 C ANISOU 3325 C ALA B 209 4052 6552 4492 -1549 -779 -425 C ATOM 3326 O ALA B 209 55.628 19.075 25.912 1.00 38.00 O ANISOU 3326 O ALA B 209 3850 6139 4449 -1478 -697 -331 O ATOM 3327 CB ALA B 209 53.199 19.719 28.082 1.00 39.57 C ANISOU 3327 CB ALA B 209 4287 6442 4307 -1549 -695 -641 C ATOM 3328 N ALA B 210 56.307 19.688 27.978 1.00 40.47 N ANISOU 3328 N ALA B 210 4017 6854 4506 -1712 -879 -547 N ATOM 3329 CA ALA B 210 57.535 20.340 27.528 1.00 42.14 C ANISOU 3329 CA ALA B 210 4097 7054 4862 -1832 -892 -595 C ATOM 3330 C ALA B 210 58.436 19.396 26.734 1.00 43.12 C ANISOU 3330 C ALA B 210 4097 7198 5087 -1713 -905 -348 C ATOM 3331 O ALA B 210 59.161 19.829 25.841 1.00 41.35 O ANISOU 3331 O ALA B 210 3817 6847 5045 -1748 -849 -337 O ATOM 3332 CB ALA B 210 58.296 20.914 28.720 1.00 39.97 C ANISOU 3332 CB ALA B 210 3684 7052 4450 -2032 -1022 -767 C ATOM 3333 N ILE B 211 58.380 18.108 27.062 1.00 45.40 N ANISOU 3333 N ILE B 211 4344 7638 5267 -1569 -966 -146 N ATOM 3334 CA ILE B 211 59.180 17.099 26.375 1.00 46.75 C ANISOU 3334 CA ILE B 211 4400 7824 5539 -1436 -964 93 C ATOM 3335 C ILE B 211 58.832 17.000 24.890 1.00 42.79 C ANISOU 3335 C ILE B 211 4014 7015 5230 -1325 -810 158 C ATOM 3336 O ILE B 211 59.717 16.979 24.033 1.00 42.13 O ANISOU 3336 O ILE B 211 3841 6870 5297 -1310 -767 235 O ATOM 3337 CB ILE B 211 58.999 15.712 27.015 1.00 49.55 C ANISOU 3337 CB ILE B 211 4712 8355 5759 -1287 -1031 302 C ATOM 3338 CG1 ILE B 211 59.321 15.772 28.509 1.00 54.92 C ANISOU 3338 CG1 ILE B 211 5275 9379 6215 -1389 -1190 260 C ATOM 3339 CG2 ILE B 211 59.869 14.679 26.307 1.00 48.10 C ANISOU 3339 CG2 ILE B 211 4402 8167 5705 -1146 -1012 542 C ATOM 3340 CD1 ILE B 211 58.994 14.500 29.256 1.00 56.76 C ANISOU 3340 CD1 ILE B 211 5481 9789 6297 -1246 -1248 471 C ATOM 3341 N TYR B 212 57.540 16.945 24.587 1.00 37.22 N ANISOU 3341 N TYR B 212 3499 6133 4509 -1250 -728 128 N ATOM 3342 CA TYR B 212 57.106 16.773 23.206 1.00 38.09 C ANISOU 3342 CA TYR B 212 3721 5986 4766 -1140 -594 194 C ATOM 3343 C TYR B 212 57.215 18.076 22.417 1.00 39.17 C ANISOU 3343 C TYR B 212 3906 5935 5042 -1243 -507 61 C ATOM 3344 O TYR B 212 57.551 18.062 21.233 1.00 39.34 O ANISOU 3344 O TYR B 212 3932 5815 5201 -1190 -417 137 O ATOM 3345 CB TYR B 212 55.680 16.216 23.172 1.00 38.34 C ANISOU 3345 CB TYR B 212 3920 5916 4731 -1027 -547 217 C ATOM 3346 CG TYR B 212 55.616 14.845 23.811 1.00 38.74 C ANISOU 3346 CG TYR B 212 3920 6119 4681 -913 -608 380 C ATOM 3347 CD1 TYR B 212 56.046 13.717 23.119 1.00 37.07 C ANISOU 3347 CD1 TYR B 212 3659 5870 4556 -777 -569 563 C ATOM 3348 CD2 TYR B 212 55.175 14.684 25.117 1.00 38.64 C ANISOU 3348 CD2 TYR B 212 3904 6286 4493 -942 -693 354 C ATOM 3349 CE1 TYR B 212 56.015 12.467 23.702 1.00 38.00 C ANISOU 3349 CE1 TYR B 212 3724 6102 4611 -668 -608 726 C ATOM 3350 CE2 TYR B 212 55.139 13.435 25.709 1.00 38.85 C ANISOU 3350 CE2 TYR B 212 3877 6448 4436 -834 -739 530 C ATOM 3351 CZ TYR B 212 55.561 12.332 24.998 1.00 39.37 C ANISOU 3351 CZ TYR B 212 3893 6452 4614 -696 -695 720 C ATOM 3352 OH TYR B 212 55.530 11.089 25.587 1.00 42.12 O ANISOU 3352 OH TYR B 212 4185 6911 4908 -582 -726 908 O ATOM 3353 N LEU B 213 56.964 19.198 23.081 1.00 39.42 N ANISOU 3353 N LEU B 213 3969 5969 5041 -1390 -526 -133 N ATOM 3354 CA LEU B 213 57.085 20.501 22.438 1.00 39.66 C ANISOU 3354 CA LEU B 213 4037 5808 5223 -1498 -434 -258 C ATOM 3355 C LEU B 213 58.540 20.814 22.077 1.00 41.73 C ANISOU 3355 C LEU B 213 4130 6119 5608 -1588 -445 -231 C ATOM 3356 O LEU B 213 58.809 21.428 21.043 1.00 40.67 O ANISOU 3356 O LEU B 213 4012 5802 5638 -1604 -337 -219 O ATOM 3357 CB LEU B 213 56.503 21.592 23.338 1.00 38.34 C ANISOU 3357 CB LEU B 213 3935 5626 5005 -1639 -442 -488 C ATOM 3358 CG LEU B 213 54.972 21.543 23.432 1.00 36.60 C ANISOU 3358 CG LEU B 213 3895 5292 4718 -1549 -386 -521 C ATOM 3359 CD1 LEU B 213 54.444 22.441 24.548 1.00 39.55 C ANISOU 3359 CD1 LEU B 213 4318 5700 5011 -1681 -400 -752 C ATOM 3360 CD2 LEU B 213 54.350 21.932 22.101 1.00 33.00 C ANISOU 3360 CD2 LEU B 213 3559 4561 4419 -1465 -247 -466 C ATOM 3361 N ASP B 214 59.474 20.381 22.921 1.00 42.51 N ANISOU 3361 N ASP B 214 4055 6472 5624 -1643 -572 -208 N ATOM 3362 CA ASP B 214 60.893 20.598 22.654 1.00 45.15 C ANISOU 3362 CA ASP B 214 4199 6883 6073 -1728 -594 -172 C ATOM 3363 C ASP B 214 61.349 19.791 21.443 1.00 42.24 C ANISOU 3363 C ASP B 214 3798 6430 5820 -1573 -511 40 C ATOM 3364 O ASP B 214 62.154 20.262 20.637 1.00 41.51 O ANISOU 3364 O ASP B 214 3630 6253 5887 -1619 -439 63 O ATOM 3365 CB ASP B 214 61.742 20.235 23.877 1.00 50.70 C ANISOU 3365 CB ASP B 214 4707 7913 6643 -1810 -765 -176 C ATOM 3366 CG ASP B 214 61.628 21.260 24.992 1.00 56.01 C ANISOU 3366 CG ASP B 214 5374 8688 7220 -2017 -841 -428 C ATOM 3367 OD1 ASP B 214 60.982 22.310 24.776 1.00 56.50 O ANISOU 3367 OD1 ASP B 214 5573 8537 7356 -2101 -745 -602 O ATOM 3368 OD2 ASP B 214 62.192 21.019 26.083 1.00 58.95 O ANISOU 3368 OD2 ASP B 214 5599 9357 7441 -2095 -993 -452 O ATOM 3369 N LEU B 215 60.835 18.571 21.325 1.00 38.82 N ANISOU 3369 N LEU B 215 3421 6018 5311 -1394 -513 188 N ATOM 3370 CA LEU B 215 61.146 17.723 20.181 1.00 38.77 C ANISOU 3370 CA LEU B 215 3405 5922 5404 -1239 -420 366 C ATOM 3371 C LEU B 215 60.662 18.371 18.887 1.00 36.31 C ANISOU 3371 C LEU B 215 3237 5351 5209 -1221 -267 338 C ATOM 3372 O LEU B 215 61.408 18.454 17.912 1.00 36.76 O ANISOU 3372 O LEU B 215 3235 5339 5393 -1204 -179 411 O ATOM 3373 CB LEU B 215 60.517 16.336 20.347 1.00 34.25 C ANISOU 3373 CB LEU B 215 2887 5389 4735 -1063 -437 499 C ATOM 3374 CG LEU B 215 61.144 15.416 21.393 1.00 34.63 C ANISOU 3374 CG LEU B 215 2772 5692 4695 -1027 -564 612 C ATOM 3375 CD1 LEU B 215 60.269 14.192 21.613 1.00 33.70 C ANISOU 3375 CD1 LEU B 215 2745 5568 4491 -867 -561 724 C ATOM 3376 CD2 LEU B 215 62.539 15.005 20.959 1.00 33.69 C ANISOU 3376 CD2 LEU B 215 2452 5651 4698 -995 -554 748 C ATOM 3377 N ALA B 216 59.417 18.836 18.891 1.00 31.93 N ANISOU 3377 N ALA B 216 2862 4666 4604 -1220 -234 243 N ATOM 3378 CA ALA B 216 58.851 19.511 17.725 1.00 32.29 C ANISOU 3378 CA ALA B 216 3043 4482 4745 -1199 -99 230 C ATOM 3379 C ALA B 216 59.674 20.743 17.362 1.00 34.30 C ANISOU 3379 C ALA B 216 3224 4660 5148 -1341 -40 168 C ATOM 3380 O ALA B 216 60.046 20.921 16.202 1.00 35.22 O ANISOU 3380 O ALA B 216 3342 4664 5375 -1306 72 251 O ATOM 3381 CB ALA B 216 57.401 19.895 17.975 1.00 29.87 C ANISOU 3381 CB ALA B 216 2912 4069 4366 -1185 -86 137 C ATOM 3382 N ASP B 217 59.965 21.579 18.357 1.00 35.28 N ANISOU 3382 N ASP B 217 3282 4849 5272 -1508 -111 17 N ATOM 3383 CA ASP B 217 60.782 22.769 18.141 1.00 38.39 C ANISOU 3383 CA ASP B 217 3593 5168 5825 -1670 -58 -63 C ATOM 3384 C ASP B 217 62.157 22.415 17.574 1.00 40.22 C ANISOU 3384 C ASP B 217 3646 5480 6158 -1670 -41 62 C ATOM 3385 O ASP B 217 62.614 23.035 16.621 1.00 35.98 O ANISOU 3385 O ASP B 217 3092 4804 5773 -1701 79 103 O ATOM 3386 CB ASP B 217 60.959 23.562 19.441 1.00 41.85 C ANISOU 3386 CB ASP B 217 3968 5703 6230 -1863 -154 -270 C ATOM 3387 CG ASP B 217 59.654 24.142 19.963 1.00 41.97 C ANISOU 3387 CG ASP B 217 4156 5610 6180 -1881 -138 -419 C ATOM 3388 OD1 ASP B 217 58.611 24.011 19.284 1.00 40.22 O ANISOU 3388 OD1 ASP B 217 4095 5230 5957 -1748 -53 -353 O ATOM 3389 OD2 ASP B 217 59.678 24.737 21.059 1.00 42.87 O ANISOU 3389 OD2 ASP B 217 4239 5807 6243 -2032 -208 -609 O ATOM 3390 N ASN B 218 62.810 21.414 18.156 1.00 43.38 N ANISOU 3390 N ASN B 218 3905 6102 6475 -1629 -152 137 N ATOM 3391 CA ASN B 218 64.154 21.043 17.724 1.00 47.79 C ANISOU 3391 CA ASN B 218 4268 6754 7134 -1625 -140 258 C ATOM 3392 C ASN B 218 64.187 20.422 16.335 1.00 43.21 C ANISOU 3392 C ASN B 218 3742 6053 6622 -1459 2 425 C ATOM 3393 O ASN B 218 65.115 20.657 15.569 1.00 43.51 O ANISOU 3393 O ASN B 218 3676 6060 6798 -1481 90 494 O ATOM 3394 CB ASN B 218 64.793 20.079 18.724 1.00 54.78 C ANISOU 3394 CB ASN B 218 4982 7915 7916 -1601 -294 321 C ATOM 3395 CG ASN B 218 65.163 20.755 20.027 1.00 62.52 C ANISOU 3395 CG ASN B 218 5846 9074 8834 -1797 -440 160 C ATOM 3396 OD1 ASN B 218 65.543 21.925 20.046 1.00 65.15 O ANISOU 3396 OD1 ASN B 218 6137 9344 9271 -1979 -415 19 O ATOM 3397 ND2 ASN B 218 65.047 20.021 21.128 1.00 65.88 N ANISOU 3397 ND2 ASN B 218 6219 9726 9088 -1766 -587 177 N ATOM 3398 N ILE B 219 63.173 19.630 16.010 1.00 39.70 N ANISOU 3398 N ILE B 219 3458 5547 6079 -1299 28 481 N ATOM 3399 CA ILE B 219 63.176 18.894 14.752 1.00 37.90 C ANISOU 3399 CA ILE B 219 3281 5233 5886 -1141 153 619 C ATOM 3400 C ILE B 219 62.642 19.740 13.595 1.00 37.26 C ANISOU 3400 C ILE B 219 3345 4945 5868 -1144 297 609 C ATOM 3401 O ILE B 219 63.210 19.734 12.503 1.00 38.56 O ANISOU 3401 O ILE B 219 3481 5054 6116 -1102 419 701 O ATOM 3402 CB ILE B 219 62.362 17.584 14.880 1.00 34.80 C ANISOU 3402 CB ILE B 219 2984 4871 5369 -975 122 680 C ATOM 3403 CG1 ILE B 219 63.104 16.607 15.801 1.00 34.45 C ANISOU 3403 CG1 ILE B 219 2769 5029 5292 -939 11 755 C ATOM 3404 CG2 ILE B 219 62.124 16.952 13.514 1.00 31.59 C ANISOU 3404 CG2 ILE B 219 2672 4349 4983 -831 262 774 C ATOM 3405 CD1 ILE B 219 62.285 15.404 16.233 1.00 33.01 C ANISOU 3405 CD1 ILE B 219 2666 4880 4995 -802 -35 808 C ATOM 3406 N LEU B 220 61.572 20.490 13.838 1.00 36.17 N ANISOU 3406 N LEU B 220 3354 4700 5689 -1190 288 506 N ATOM 3407 CA LEU B 220 60.912 21.211 12.753 1.00 35.90 C ANISOU 3407 CA LEU B 220 3462 4477 5700 -1165 418 526 C ATOM 3408 C LEU B 220 61.007 22.729 12.853 1.00 39.15 C ANISOU 3408 C LEU B 220 3873 4765 6239 -1322 465 437 C ATOM 3409 O LEU B 220 60.637 23.432 11.913 1.00 39.76 O ANISOU 3409 O LEU B 220 4041 4684 6383 -1306 586 484 O ATOM 3410 CB LEU B 220 59.442 20.799 12.679 1.00 34.76 C ANISOU 3410 CB LEU B 220 3502 4276 5428 -1055 404 512 C ATOM 3411 CG LEU B 220 59.219 19.385 12.147 1.00 34.20 C ANISOU 3411 CG LEU B 220 3468 4263 5264 -893 414 608 C ATOM 3412 CD1 LEU B 220 58.390 18.571 13.119 1.00 32.80 C ANISOU 3412 CD1 LEU B 220 3341 4159 4963 -843 300 562 C ATOM 3413 CD2 LEU B 220 58.553 19.448 10.785 1.00 34.14 C ANISOU 3413 CD2 LEU B 220 3594 4141 5237 -801 532 673 C ATOM 3414 N GLY B 221 61.498 23.235 13.981 1.00 40.49 N ANISOU 3414 N GLY B 221 3936 5007 6443 -1475 373 311 N ATOM 3415 CA GLY B 221 61.609 24.671 14.175 1.00 42.34 C ANISOU 3415 CA GLY B 221 4163 5108 6815 -1642 422 197 C ATOM 3416 C GLY B 221 60.673 25.197 15.250 1.00 42.71 C ANISOU 3416 C GLY B 221 4302 5125 6801 -1713 350 21 C ATOM 3417 O GLY B 221 59.586 24.655 15.459 1.00 37.24 O ANISOU 3417 O GLY B 221 3736 4440 5972 -1603 311 19 O ATOM 3418 N ASN B 222 61.102 26.265 15.923 1.00 45.19 N ANISOU 3418 N ASN B 222 4548 5401 7222 -1905 343 -137 N ATOM 3419 CA ASN B 222 60.339 26.884 17.009 1.00 48.29 C ANISOU 3419 CA ASN B 222 5015 5765 7569 -2000 291 -339 C ATOM 3420 C ASN B 222 58.943 27.339 16.598 1.00 46.72 C ANISOU 3420 C ASN B 222 5016 5357 7379 -1906 387 -338 C ATOM 3421 O ASN B 222 58.047 27.449 17.430 1.00 46.96 O ANISOU 3421 O ASN B 222 5133 5390 7319 -1912 340 -467 O ATOM 3422 CB ASN B 222 61.101 28.089 17.572 1.00 51.17 C ANISOU 3422 CB ASN B 222 5274 6080 8088 -2236 305 -520 C ATOM 3423 CG ASN B 222 62.368 27.692 18.308 1.00 57.92 C ANISOU 3423 CG ASN B 222 5915 7189 8904 -2357 171 -566 C ATOM 3424 OD1 ASN B 222 62.665 26.507 18.464 1.00 58.71 O ANISOU 3424 OD1 ASN B 222 5944 7501 8861 -2252 67 -452 O ATOM 3425 ND2 ASN B 222 63.128 28.688 18.761 1.00 60.70 N ANISOU 3425 ND2 ASN B 222 6183 7520 9361 -2531 159 -700 N ATOM 3426 N GLU B 223 58.771 27.611 15.312 1.00 47.29 N ANISOU 3426 N GLU B 223 5151 5260 7555 -1816 523 -185 N ATOM 3427 CA GLU B 223 57.541 28.204 14.806 1.00 47.83 C ANISOU 3427 CA GLU B 223 5384 5124 7664 -1732 626 -158 C ATOM 3428 C GLU B 223 56.518 27.176 14.328 1.00 43.30 C ANISOU 3428 C GLU B 223 4925 4605 6923 -1531 597 -34 C ATOM 3429 O GLU B 223 55.354 27.503 14.121 1.00 43.14 O ANISOU 3429 O GLU B 223 5032 4463 6896 -1453 646 -24 O ATOM 3430 CB GLU B 223 57.879 29.165 13.664 1.00 51.60 C ANISOU 3430 CB GLU B 223 5864 5394 8348 -1751 794 -45 C ATOM 3431 CG GLU B 223 58.880 28.593 12.665 1.00 53.02 C ANISOU 3431 CG GLU B 223 5951 5655 8539 -1702 830 134 C ATOM 3432 N TRP B 224 56.950 25.931 14.168 1.00 39.40 N ANISOU 3432 N TRP B 224 4376 4291 6303 -1448 521 57 N ATOM 3433 CA TRP B 224 56.135 24.922 13.501 1.00 34.87 C ANISOU 3433 CA TRP B 224 3897 3755 5595 -1268 515 181 C ATOM 3434 C TRP B 224 54.881 24.522 14.285 1.00 35.97 C ANISOU 3434 C TRP B 224 4138 3928 5603 -1210 437 103 C ATOM 3435 O TRP B 224 53.794 24.398 13.715 1.00 34.00 O ANISOU 3435 O TRP B 224 4003 3608 5308 -1097 474 165 O ATOM 3436 CB TRP B 224 56.989 23.681 13.216 1.00 34.02 C ANISOU 3436 CB TRP B 224 3698 3815 5415 -1204 469 279 C ATOM 3437 CG TRP B 224 56.261 22.614 12.473 1.00 32.00 C ANISOU 3437 CG TRP B 224 3533 3590 5037 -1036 475 386 C ATOM 3438 CD1 TRP B 224 56.059 22.548 11.125 1.00 31.94 C ANISOU 3438 CD1 TRP B 224 3586 3517 5032 -941 576 511 C ATOM 3439 CD2 TRP B 224 55.632 21.455 13.032 1.00 30.91 C ANISOU 3439 CD2 TRP B 224 3431 3561 4754 -951 380 372 C ATOM 3440 NE1 TRP B 224 55.338 21.422 10.809 1.00 28.42 N ANISOU 3440 NE1 TRP B 224 3213 3134 4451 -812 545 554 N ATOM 3441 CE2 TRP B 224 55.064 20.732 11.962 1.00 29.74 C ANISOU 3441 CE2 TRP B 224 3365 3394 4539 -816 430 474 C ATOM 3442 CE3 TRP B 224 55.487 20.959 14.334 1.00 29.13 C ANISOU 3442 CE3 TRP B 224 3173 3452 4443 -980 261 287 C ATOM 3443 CZ2 TRP B 224 54.363 19.539 12.153 1.00 28.32 C ANISOU 3443 CZ2 TRP B 224 3236 3285 4238 -717 371 482 C ATOM 3444 CZ3 TRP B 224 54.793 19.769 14.520 1.00 29.00 C ANISOU 3444 CZ3 TRP B 224 3207 3508 4304 -870 208 321 C ATOM 3445 CH2 TRP B 224 54.245 19.071 13.434 1.00 26.30 C ANISOU 3445 CH2 TRP B 224 2947 3123 3925 -744 265 413 C ATOM 3446 N ALA B 225 55.035 24.329 15.591 1.00 38.41 N ANISOU 3446 N ALA B 225 4394 4357 5843 -1291 330 -30 N ATOM 3447 CA ALA B 225 53.991 23.718 16.410 1.00 39.67 C ANISOU 3447 CA ALA B 225 4627 4591 5854 -1232 250 -87 C ATOM 3448 C ALA B 225 52.875 24.678 16.820 1.00 46.90 C ANISOU 3448 C ALA B 225 5649 5368 6803 -1258 297 -202 C ATOM 3449 O ALA B 225 52.899 25.235 17.917 1.00 55.27 O ANISOU 3449 O ALA B 225 6690 6452 7858 -1375 263 -369 O ATOM 3450 CB ALA B 225 54.609 23.096 17.652 1.00 37.18 C ANISOU 3450 CB ALA B 225 4209 4487 5432 -1300 120 -162 C ATOM 3451 N ASP B 226 51.893 24.860 15.945 1.00 43.07 N ANISOU 3451 N ASP B 226 5270 4748 6347 -1148 376 -115 N ATOM 3452 CA ASP B 226 50.682 25.585 16.307 1.00 38.33 C ANISOU 3452 CA ASP B 226 4767 4025 5772 -1135 421 -197 C ATOM 3453 C ASP B 226 49.514 24.607 16.340 1.00 34.70 C ANISOU 3453 C ASP B 226 4380 3636 5166 -1002 371 -143 C ATOM 3454 O ASP B 226 49.689 23.420 16.064 1.00 34.40 O ANISOU 3454 O ASP B 226 4321 3725 5023 -930 309 -52 O ATOM 3455 CB ASP B 226 50.411 26.738 15.330 1.00 34.03 C ANISOU 3455 CB ASP B 226 4270 3257 5402 -1118 560 -129 C ATOM 3456 CG ASP B 226 50.395 26.289 13.875 1.00 32.57 C ANISOU 3456 CG ASP B 226 4104 3065 5207 -995 602 80 C ATOM 3457 OD1 ASP B 226 49.956 25.156 13.587 1.00 30.68 O ANISOU 3457 OD1 ASP B 226 3890 2943 4823 -889 539 153 O ATOM 3458 OD2 ASP B 226 50.818 27.076 13.011 1.00 34.95 O ANISOU 3458 OD2 ASP B 226 4395 3241 5644 -1009 705 167 O ATOM 3459 N ALA B 227 48.323 25.107 16.652 1.00 35.15 N ANISOU 3459 N ALA B 227 4518 3603 5236 -968 408 -200 N ATOM 3460 CA ALA B 227 47.143 24.251 16.767 1.00 32.28 C ANISOU 3460 CA ALA B 227 4213 3304 4748 -855 365 -161 C ATOM 3461 C ALA B 227 46.835 23.480 15.482 1.00 30.30 C ANISOU 3461 C ALA B 227 3986 3067 4458 -729 368 13 C ATOM 3462 O ALA B 227 46.153 22.459 15.526 1.00 29.91 O ANISOU 3462 O ALA B 227 3961 3107 4295 -651 313 49 O ATOM 3463 CB ALA B 227 45.936 25.076 17.183 1.00 33.91 C ANISOU 3463 CB ALA B 227 4489 3390 5006 -836 427 -239 C ATOM 3464 N ASN B 228 47.334 23.960 14.345 1.00 30.86 N ANISOU 3464 N ASN B 228 4049 3054 4620 -715 437 117 N ATOM 3465 CA ASN B 228 47.144 23.250 13.079 1.00 33.73 C ANISOU 3465 CA ASN B 228 4433 3455 4926 -608 443 268 C ATOM 3466 C ASN B 228 48.196 22.171 12.818 1.00 32.37 C ANISOU 3466 C ASN B 228 4203 3410 4685 -610 398 308 C ATOM 3467 O ASN B 228 48.103 21.442 11.831 1.00 29.49 O ANISOU 3467 O ASN B 228 3856 3090 4259 -529 404 406 O ATOM 3468 CB ASN B 228 47.144 24.231 11.907 1.00 37.78 C ANISOU 3468 CB ASN B 228 4966 3840 5548 -578 548 383 C ATOM 3469 CG ASN B 228 45.891 25.080 11.855 1.00 42.37 C ANISOU 3469 CG ASN B 228 5606 4301 6192 -523 600 400 C ATOM 3470 OD1 ASN B 228 44.813 24.641 12.251 1.00 44.17 O ANISOU 3470 OD1 ASN B 228 5868 4569 6345 -467 553 369 O ATOM 3471 ND2 ASN B 228 46.029 26.307 11.362 1.00 44.71 N ANISOU 3471 ND2 ASN B 228 5905 4441 6641 -536 706 460 N ATOM 3472 N HIS B 229 49.195 22.073 13.693 1.00 29.74 N ANISOU 3472 N HIS B 229 3795 3141 4364 -702 355 231 N ATOM 3473 CA HIS B 229 50.280 21.117 13.494 1.00 32.60 C ANISOU 3473 CA HIS B 229 4081 3616 4688 -699 321 281 C ATOM 3474 C HIS B 229 50.603 20.280 14.732 1.00 31.89 C ANISOU 3474 C HIS B 229 3933 3665 4519 -731 220 216 C ATOM 3475 O HIS B 229 51.414 19.355 14.668 1.00 30.72 O ANISOU 3475 O HIS B 229 3715 3615 4342 -709 190 270 O ATOM 3476 CB HIS B 229 51.547 21.844 13.044 1.00 36.59 C ANISOU 3476 CB HIS B 229 4511 4080 5310 -776 382 308 C ATOM 3477 CG HIS B 229 51.477 22.369 11.644 1.00 42.10 C ANISOU 3477 CG HIS B 229 5249 4679 6067 -725 488 423 C ATOM 3478 ND1 HIS B 229 51.242 23.694 11.359 1.00 47.25 N ANISOU 3478 ND1 HIS B 229 5932 5183 6839 -763 571 431 N ATOM 3479 CD2 HIS B 229 51.604 21.743 10.451 1.00 46.01 C ANISOU 3479 CD2 HIS B 229 5760 5209 6512 -638 530 538 C ATOM 3480 CE1 HIS B 229 51.234 23.866 10.049 1.00 50.27 C ANISOU 3480 CE1 HIS B 229 6342 5524 7235 -696 655 569 C ATOM 3481 NE2 HIS B 229 51.449 22.696 9.475 1.00 48.91 N ANISOU 3481 NE2 HIS B 229 6163 5471 6948 -624 629 626 N ATOM 3482 N PHE B 230 49.977 20.605 15.856 1.00 28.98 N ANISOU 3482 N PHE B 230 3587 3309 4113 -776 177 109 N ATOM 3483 CA PHE B 230 50.313 19.953 17.115 1.00 28.67 C ANISOU 3483 CA PHE B 230 3487 3423 3985 -816 81 54 C ATOM 3484 C PHE B 230 49.128 19.980 18.069 1.00 29.30 C ANISOU 3484 C PHE B 230 3634 3518 3983 -811 51 -30 C ATOM 3485 O PHE B 230 48.507 21.022 18.270 1.00 28.02 O ANISOU 3485 O PHE B 230 3525 3254 3868 -851 97 -120 O ATOM 3486 CB PHE B 230 51.530 20.635 17.758 1.00 29.90 C ANISOU 3486 CB PHE B 230 3537 3633 4191 -952 53 -24 C ATOM 3487 CG PHE B 230 52.167 19.844 18.873 1.00 30.95 C ANISOU 3487 CG PHE B 230 3572 3966 4220 -985 -56 -36 C ATOM 3488 CD1 PHE B 230 51.502 19.639 20.077 1.00 32.32 C ANISOU 3488 CD1 PHE B 230 3769 4237 4272 -1002 -121 -113 C ATOM 3489 CD2 PHE B 230 53.452 19.339 18.730 1.00 31.52 C ANISOU 3489 CD2 PHE B 230 3519 4139 4317 -998 -90 40 C ATOM 3490 CE1 PHE B 230 52.094 18.919 21.103 1.00 34.83 C ANISOU 3490 CE1 PHE B 230 3992 4762 4482 -1026 -224 -99 C ATOM 3491 CE2 PHE B 230 54.055 18.627 19.755 1.00 33.91 C ANISOU 3491 CE2 PHE B 230 3716 4641 4527 -1018 -195 55 C ATOM 3492 CZ PHE B 230 53.379 18.417 20.943 1.00 35.04 C ANISOU 3492 CZ PHE B 230 3886 4891 4537 -1033 -265 -9 C ATOM 3493 N ARG B 231 48.827 18.825 18.655 1.00 30.33 N ANISOU 3493 N ARG B 231 3756 3768 4002 -757 -14 7 N ATOM 3494 CA ARG B 231 47.777 18.711 19.657 1.00 29.48 C ANISOU 3494 CA ARG B 231 3697 3702 3802 -751 -41 -60 C ATOM 3495 C ARG B 231 48.221 17.816 20.806 1.00 30.13 C ANISOU 3495 C ARG B 231 3708 3975 3765 -767 -131 -46 C ATOM 3496 O ARG B 231 49.008 16.890 20.614 1.00 30.29 O ANISOU 3496 O ARG B 231 3658 4073 3779 -729 -166 60 O ATOM 3497 CB ARG B 231 46.490 18.149 19.044 1.00 27.23 C ANISOU 3497 CB ARG B 231 3497 3347 3503 -641 -7 3 C ATOM 3498 CG ARG B 231 45.918 18.966 17.909 1.00 27.65 C ANISOU 3498 CG ARG B 231 3613 3241 3651 -608 72 17 C ATOM 3499 CD ARG B 231 45.313 20.290 18.385 1.00 28.23 C ANISOU 3499 CD ARG B 231 3727 3220 3777 -659 121 -95 C ATOM 3500 NE ARG B 231 44.761 21.015 17.245 1.00 29.79 N ANISOU 3500 NE ARG B 231 3975 3270 4075 -608 198 -41 N ATOM 3501 CZ ARG B 231 43.611 20.703 16.652 1.00 27.65 C ANISOU 3501 CZ ARG B 231 3752 2965 3787 -513 214 24 C ATOM 3502 NH1 ARG B 231 42.877 19.696 17.110 1.00 25.39 N ANISOU 3502 NH1 ARG B 231 3477 2765 3407 -468 166 31 N ATOM 3503 NH2 ARG B 231 43.190 21.401 15.608 1.00 26.93 N ANISOU 3503 NH2 ARG B 231 3693 2764 3777 -464 277 92 N ATOM 3504 N PHE B 232 47.710 18.090 21.999 1.00 30.46 N ANISOU 3504 N PHE B 232 3764 4095 3713 -817 -160 -145 N ATOM 3505 CA PHE B 232 47.863 17.166 23.115 1.00 28.06 C ANISOU 3505 CA PHE B 232 3407 3986 3270 -812 -240 -105 C ATOM 3506 C PHE B 232 46.563 16.389 23.331 1.00 28.30 C ANISOU 3506 C PHE B 232 3508 4007 3238 -721 -221 -54 C ATOM 3507 O PHE B 232 45.519 16.974 23.639 1.00 25.36 O ANISOU 3507 O PHE B 232 3210 3578 2848 -730 -177 -146 O ATOM 3508 CB PHE B 232 48.252 17.905 24.399 1.00 26.73 C ANISOU 3508 CB PHE B 232 3194 3959 3003 -939 -292 -249 C ATOM 3509 CG PHE B 232 49.719 18.229 24.502 1.00 29.35 C ANISOU 3509 CG PHE B 232 3407 4386 3357 -1035 -351 -269 C ATOM 3510 CD1 PHE B 232 50.657 17.222 24.646 1.00 28.32 C ANISOU 3510 CD1 PHE B 232 3165 4411 3186 -1000 -428 -127 C ATOM 3511 CD2 PHE B 232 50.155 19.546 24.477 1.00 30.05 C ANISOU 3511 CD2 PHE B 232 3489 4406 3524 -1162 -324 -427 C ATOM 3512 CE1 PHE B 232 52.008 17.518 24.751 1.00 31.16 C ANISOU 3512 CE1 PHE B 232 3395 4873 3571 -1088 -486 -138 C ATOM 3513 CE2 PHE B 232 51.505 19.851 24.581 1.00 33.64 C ANISOU 3513 CE2 PHE B 232 3821 4954 4008 -1265 -379 -451 C ATOM 3514 CZ PHE B 232 52.431 18.835 24.719 1.00 33.53 C ANISOU 3514 CZ PHE B 232 3685 5114 3943 -1227 -466 -305 C ATOM 3515 N GLY B 233 46.628 15.072 23.162 1.00 29.77 N ANISOU 3515 N GLY B 233 3666 4237 3407 -634 -242 93 N ATOM 3516 CA GLY B 233 45.496 14.216 23.459 1.00 30.63 C ANISOU 3516 CA GLY B 233 3824 4348 3465 -560 -225 151 C ATOM 3517 C GLY B 233 45.520 13.836 24.924 1.00 30.34 C ANISOU 3517 C GLY B 233 3743 4505 3278 -586 -281 163 C ATOM 3518 O GLY B 233 46.269 12.947 25.325 1.00 33.43 O ANISOU 3518 O GLY B 233 4054 5020 3627 -559 -333 284 O ATOM 3519 N ALA B 234 44.709 14.512 25.730 1.00 27.64 N ANISOU 3519 N ALA B 234 3452 4197 2854 -632 -263 46 N ATOM 3520 CA ALA B 234 44.752 14.306 27.172 1.00 33.40 C ANISOU 3520 CA ALA B 234 4142 5138 3409 -671 -313 38 C ATOM 3521 C ALA B 234 43.435 14.650 27.846 1.00 37.00 C ANISOU 3521 C ALA B 234 4675 5592 3791 -675 -257 -52 C ATOM 3522 O ALA B 234 42.544 15.234 27.234 1.00 35.46 O ANISOU 3522 O ALA B 234 4555 5228 3691 -657 -182 -126 O ATOM 3523 CB ALA B 234 45.877 15.134 27.786 1.00 34.54 C ANISOU 3523 CB ALA B 234 4217 5421 3484 -789 -381 -70 C ATOM 3524 N SER B 235 43.328 14.291 29.120 1.00 43.31 N ANISOU 3524 N SER B 235 5447 6593 4415 -694 -289 -35 N ATOM 3525 CA SER B 235 42.174 14.667 29.926 1.00 44.67 C ANISOU 3525 CA SER B 235 5683 6798 4493 -708 -228 -133 C ATOM 3526 C SER B 235 42.625 15.415 31.177 1.00 44.65 C ANISOU 3526 C SER B 235 5656 7003 4305 -821 -267 -284 C ATOM 3527 O SER B 235 42.509 16.637 31.251 1.00 47.48 O ANISOU 3527 O SER B 235 6058 7298 4685 -903 -226 -491 O ATOM 3528 CB SER B 235 41.347 13.435 30.301 1.00 45.03 C ANISOU 3528 CB SER B 235 5730 6891 4487 -617 -202 34 C ATOM 3529 OG SER B 235 42.153 12.435 30.905 1.00 49.13 O ANISOU 3529 OG SER B 235 6166 7597 4906 -596 -277 201 O ATOM 3530 N SER B 236 43.168 14.681 32.145 1.00 44.93 N ANISOU 3530 N SER B 236 5618 7290 4164 -828 -345 -179 N ATOM 3531 CA SER B 236 43.535 15.256 33.438 1.00 48.31 C ANISOU 3531 CA SER B 236 6016 7970 4369 -939 -393 -316 C ATOM 3532 C SER B 236 44.604 16.348 33.334 1.00 47.35 C ANISOU 3532 C SER B 236 5856 7865 4270 -1071 -448 -500 C ATOM 3533 O SER B 236 44.782 17.136 34.264 1.00 49.56 O ANISOU 3533 O SER B 236 6132 8302 4396 -1191 -466 -693 O ATOM 3534 CB SER B 236 44.006 14.152 34.393 1.00 52.39 C ANISOU 3534 CB SER B 236 6443 8774 4690 -907 -480 -119 C ATOM 3535 OG SER B 236 45.012 13.347 33.803 1.00 54.99 O ANISOU 3535 OG SER B 236 6679 9103 5112 -851 -556 76 O ATOM 3536 N LEU B 237 45.298 16.398 32.199 1.00 44.42 N ANISOU 3536 N LEU B 237 5455 7330 4091 -1054 -466 -449 N ATOM 3537 CA LEU B 237 46.348 17.391 31.951 1.00 43.12 C ANISOU 3537 CA LEU B 237 5245 7151 3990 -1177 -507 -601 C ATOM 3538 C LEU B 237 45.877 18.835 32.140 1.00 41.96 C ANISOU 3538 C LEU B 237 5179 6892 3873 -1286 -424 -884 C ATOM 3539 O LEU B 237 46.643 19.690 32.583 1.00 42.24 O ANISOU 3539 O LEU B 237 5170 7014 3866 -1431 -464 -1064 O ATOM 3540 CB LEU B 237 46.905 17.212 30.533 1.00 38.43 C ANISOU 3540 CB LEU B 237 4628 6351 3622 -1118 -499 -488 C ATOM 3541 CG LEU B 237 47.848 18.269 29.944 1.00 37.93 C ANISOU 3541 CG LEU B 237 4529 6191 3692 -1227 -504 -621 C ATOM 3542 CD1 LEU B 237 49.151 18.364 30.727 1.00 36.67 C ANISOU 3542 CD1 LEU B 237 4233 6290 3408 -1345 -628 -659 C ATOM 3543 CD2 LEU B 237 48.121 17.965 28.475 1.00 36.07 C ANISOU 3543 CD2 LEU B 237 4294 5743 3667 -1138 -467 -483 C ATOM 3544 N LEU B 238 44.617 19.101 31.805 1.00 42.59 N ANISOU 3544 N LEU B 238 5368 6775 4040 -1219 -304 -923 N ATOM 3545 CA LEU B 238 44.075 20.457 31.874 1.00 44.61 C ANISOU 3545 CA LEU B 238 5704 6877 4370 -1296 -198 -1171 C ATOM 3546 C LEU B 238 44.055 21.001 33.299 1.00 44.63 C ANISOU 3546 C LEU B 238 5708 7093 4157 -1421 -203 -1387 C ATOM 3547 O LEU B 238 44.415 22.156 33.532 1.00 44.73 O ANISOU 3547 O LEU B 238 5731 7063 4203 -1555 -172 -1627 O ATOM 3548 CB LEU B 238 42.661 20.500 31.285 1.00 43.76 C ANISOU 3548 CB LEU B 238 5694 6545 4389 -1178 -72 -1135 C ATOM 3549 CG LEU B 238 41.991 21.877 31.277 1.00 44.39 C ANISOU 3549 CG LEU B 238 5853 6431 4582 -1227 60 -1361 C ATOM 3550 CD1 LEU B 238 42.814 22.886 30.478 1.00 43.87 C ANISOU 3550 CD1 LEU B 238 5776 6184 4710 -1304 77 -1452 C ATOM 3551 CD2 LEU B 238 40.577 21.781 30.732 1.00 42.72 C ANISOU 3551 CD2 LEU B 238 5713 6037 4484 -1093 169 -1286 C ATOM 3552 N ILE B 239 43.633 20.165 34.243 1.00 46.49 N ANISOU 3552 N ILE B 239 5934 7558 4172 -1380 -235 -1303 N ATOM 3553 CA ILE B 239 43.570 20.556 35.647 1.00 49.36 C ANISOU 3553 CA ILE B 239 6299 8170 4285 -1490 -242 -1492 C ATOM 3554 C ILE B 239 44.971 20.835 36.187 1.00 53.37 C ANISOU 3554 C ILE B 239 6701 8889 4690 -1626 -370 -1570 C ATOM 3555 O ILE B 239 45.167 21.748 36.993 1.00 56.48 O ANISOU 3555 O ILE B 239 7095 9321 5045 -1722 -340 -1773 O ATOM 3556 CB ILE B 239 42.887 19.474 36.509 1.00 45.85 C ANISOU 3556 CB ILE B 239 5854 7946 3620 -1403 -252 -1332 C ATOM 3557 N SER B 240 45.943 20.051 35.728 1.00 53.29 N ANISOU 3557 N SER B 240 6587 8976 4684 -1606 -497 -1374 N ATOM 3558 CA SER B 240 47.332 20.242 36.132 1.00 55.02 C ANISOU 3558 CA SER B 240 6681 9355 4868 -1695 -611 -1388 C ATOM 3559 C SER B 240 47.893 21.559 35.599 1.00 55.37 C ANISOU 3559 C SER B 240 6731 9200 5106 -1822 -570 -1614 C ATOM 3560 O SER B 240 48.523 22.316 36.341 1.00 58.84 O ANISOU 3560 O SER B 240 7128 9727 5502 -1932 -588 -1775 O ATOM 3561 CB SER B 240 48.199 19.077 35.654 1.00 51.79 C ANISOU 3561 CB SER B 240 6154 9065 4458 -1622 -738 -1106 C ATOM 3562 OG SER B 240 49.507 19.180 36.187 1.00 52.83 O ANISOU 3562 OG SER B 240 6152 9385 4537 -1696 -846 -1102 O ATOM 3563 N LEU B 241 47.666 21.827 34.315 1.00 52.31 N ANISOU 3563 N LEU B 241 6395 8542 4937 -1807 -509 -1618 N ATOM 3564 CA LEU B 241 48.142 23.061 33.695 1.00 53.07 C ANISOU 3564 CA LEU B 241 6502 8406 5257 -1911 -445 -1798 C ATOM 3565 C LEU B 241 47.535 24.280 34.378 1.00 56.34 C ANISOU 3565 C LEU B 241 7004 8710 5695 -1975 -318 -2058 C ATOM 3566 O LEU B 241 48.224 25.275 34.616 1.00 58.97 O ANISOU 3566 O LEU B 241 7304 8998 6104 -2090 -303 -2224 O ATOM 3567 CB LEU B 241 47.819 23.082 32.196 1.00 51.20 C ANISOU 3567 CB LEU B 241 6319 7837 5297 -1799 -358 -1666 C ATOM 3568 CG LEU B 241 48.508 22.023 31.326 1.00 49.75 C ANISOU 3568 CG LEU B 241 6053 7670 5180 -1691 -440 -1380 C ATOM 3569 CD1 LEU B 241 48.230 22.255 29.850 1.00 46.33 C ANISOU 3569 CD1 LEU B 241 5679 6911 5013 -1598 -341 -1287 C ATOM 3570 CD2 LEU B 241 50.007 21.988 31.595 1.00 52.98 C ANISOU 3570 CD2 LEU B 241 6310 8285 5537 -1809 -573 -1384 C ATOM 3571 N LEU B 242 46.246 24.195 34.699 1.00 55.59 N ANISOU 3571 N LEU B 242 7013 8570 5540 -1900 -221 -2088 N ATOM 3572 CA LEU B 242 45.568 25.276 35.405 1.00 54.84 C ANISOU 3572 CA LEU B 242 6995 8379 5464 -1943 -89 -2320 C ATOM 3573 C LEU B 242 46.195 25.501 36.778 1.00 56.49 C ANISOU 3573 C LEU B 242 7139 8855 5471 -2042 -156 -2433 C ATOM 3574 O LEU B 242 46.348 26.640 37.218 1.00 57.57 O ANISOU 3574 O LEU B 242 7292 8915 5669 -2142 -85 -2656 O ATOM 3575 CB LEU B 242 44.073 24.980 35.540 1.00 50.79 C ANISOU 3575 CB LEU B 242 6587 7803 4908 -1829 21 -2301 C ATOM 3576 CG LEU B 242 43.267 25.141 34.252 1.00 47.87 C ANISOU 3576 CG LEU B 242 6300 7116 4773 -1744 132 -2259 C ATOM 3577 CD1 LEU B 242 41.819 24.744 34.472 1.00 45.18 C ANISOU 3577 CD1 LEU B 242 6040 6746 4379 -1618 232 -2209 C ATOM 3578 CD2 LEU B 242 43.364 26.571 33.738 1.00 47.55 C ANISOU 3578 CD2 LEU B 242 6295 6770 5003 -1800 255 -2427 C ATOM 3579 N ASP B 243 46.567 24.410 37.441 1.00 56.48 N ANISOU 3579 N ASP B 243 7061 9165 5234 -2011 -289 -2270 N ATOM 3580 CA ASP B 243 47.216 24.489 38.744 1.00 58.21 C ANISOU 3580 CA ASP B 243 7205 9672 5242 -2098 -368 -2344 C ATOM 3581 C ASP B 243 48.605 25.108 38.621 1.00 58.42 C ANISOU 3581 C ASP B 243 7132 9720 5346 -2228 -447 -2430 C ATOM 3582 O ASP B 243 49.104 25.725 39.560 1.00 63.56 O ANISOU 3582 O ASP B 243 7743 10511 5897 -2343 -468 -2598 O ATOM 3583 CB ASP B 243 47.309 23.104 39.386 1.00 57.56 C ANISOU 3583 CB ASP B 243 7053 9900 4917 -2012 -486 -2100 C ATOM 3584 N THR B 244 49.226 24.938 37.459 1.00 54.58 N ANISOU 3584 N THR B 244 6601 9099 5039 -2214 -488 -2317 N ATOM 3585 CA THR B 244 50.532 25.531 37.200 1.00 55.39 C ANISOU 3585 CA THR B 244 6605 9192 5249 -2333 -551 -2385 C ATOM 3586 C THR B 244 50.393 27.028 36.954 1.00 56.39 C ANISOU 3586 C THR B 244 6803 9037 5587 -2433 -412 -2643 C ATOM 3587 O THR B 244 51.209 27.823 37.416 1.00 56.53 O ANISOU 3587 O THR B 244 6762 9100 5615 -2567 -431 -2806 O ATOM 3588 CB THR B 244 51.222 24.870 35.994 1.00 53.01 C ANISOU 3588 CB THR B 244 6229 8826 5086 -2281 -625 -2171 C ATOM 3589 OG1 THR B 244 51.511 23.503 36.304 1.00 54.20 O ANISOU 3589 OG1 THR B 244 6293 9249 5053 -2190 -756 -1923 O ATOM 3590 CG2 THR B 244 52.521 25.590 35.645 1.00 53.08 C ANISOU 3590 CG2 THR B 244 6138 8789 5240 -2405 -667 -2249 C ATOM 3591 N LEU B 245 49.340 27.405 36.238 1.00 56.62 N ANISOU 3591 N LEU B 245 6953 8774 5788 -2362 -266 -2672 N ATOM 3592 CA LEU B 245 49.089 28.803 35.914 1.00 58.79 C ANISOU 3592 CA LEU B 245 7299 8744 6296 -2425 -110 -2878 C ATOM 3593 C LEU B 245 48.395 29.534 37.062 1.00 62.72 C ANISOU 3593 C LEU B 245 7863 9273 6696 -2472 -12 -3103 C ATOM 3594 O LEU B 245 48.135 30.735 36.981 1.00 61.36 O ANISOU 3594 O LEU B 245 7747 8863 6704 -2524 129 -3287 O ATOM 3595 CB LEU B 245 48.255 28.902 34.638 1.00 55.18 C ANISOU 3595 CB LEU B 245 6932 7956 6075 -2315 11 -2789 C ATOM 3596 CG LEU B 245 48.942 28.292 33.416 1.00 51.67 C ANISOU 3596 CG LEU B 245 6427 7453 5752 -2280 -66 -2585 C ATOM 3597 CD1 LEU B 245 47.985 28.197 32.244 1.00 47.42 C ANISOU 3597 CD1 LEU B 245 5982 6635 5398 -2159 43 -2478 C ATOM 3598 CD2 LEU B 245 50.176 29.109 33.045 1.00 52.88 C ANISOU 3598 CD2 LEU B 245 6499 7520 6072 -2401 -80 -2652 C ATOM 3599 N GLY B 246 48.097 28.800 38.130 1.00 67.75 N ANISOU 3599 N GLY B 246 8488 10204 7051 -2449 -81 -3075 N ATOM 3600 CA GLY B 246 47.533 29.389 39.331 1.00 72.72 C ANISOU 3600 CA GLY B 246 9165 10916 7548 -2502 -3 -3283 C ATOM 3601 C GLY B 246 46.032 29.601 39.290 1.00 74.66 C ANISOU 3601 C GLY B 246 9537 10974 7855 -2399 163 -3324 C ATOM 3602 O GLY B 246 45.542 30.669 39.661 1.00 79.77 O ANISOU 3602 O GLY B 246 10246 11471 8592 -2446 305 -3539 O ATOM 3603 N HIS B 247 45.301 28.585 38.845 1.00 70.20 N ANISOU 3603 N HIS B 247 9006 10418 7249 -2256 150 -3117 N ATOM 3604 CA HIS B 247 43.843 28.639 38.823 1.00 71.02 C ANISOU 3604 CA HIS B 247 9217 10373 7394 -2146 298 -3130 C ATOM 3605 C HIS B 247 43.245 27.513 39.658 1.00 70.59 C ANISOU 3605 C HIS B 247 9165 10597 7060 -2068 244 -3005 C ATOM 3606 O HIS B 247 43.572 26.343 39.460 1.00 68.99 O ANISOU 3606 O HIS B 247 8908 10565 6739 -2011 115 -2782 O ATOM 3607 CB HIS B 247 43.320 28.563 37.388 1.00 69.04 C ANISOU 3607 CB HIS B 247 9018 9821 7393 -2037 368 -3002 C ATOM 3608 CG HIS B 247 43.649 29.765 36.560 1.00 70.88 C ANISOU 3608 CG HIS B 247 9266 9736 7928 -2087 465 -3107 C ATOM 3609 ND1 HIS B 247 43.000 30.972 36.710 1.00 73.20 N ANISOU 3609 ND1 HIS B 247 9625 9800 8389 -2098 641 -3289 N ATOM 3610 CD2 HIS B 247 44.557 29.947 35.572 1.00 69.97 C ANISOU 3610 CD2 HIS B 247 9104 9493 7988 -2123 417 -3040 C ATOM 3611 CE1 HIS B 247 43.495 31.845 35.851 1.00 72.59 C ANISOU 3611 CE1 HIS B 247 9540 9464 8576 -2135 698 -3318 C ATOM 3612 NE2 HIS B 247 44.441 31.248 35.148 1.00 71.27 N ANISOU 3612 NE2 HIS B 247 9308 9355 8416 -2153 565 -3171 N TER 3613 HIS B 247 HETATM 3614 C1 UNL A 301 10.536 2.484 18.039 1.00 30.18 C ANISOU 3614 C1 UNL A 301 4212 4179 3078 -152 -88 147 C HETATM 3615 C2 UNL A 301 9.690 2.460 19.303 1.00 25.11 C ANISOU 3615 C2 UNL A 301 3586 3587 2367 -159 -66 164 C HETATM 3616 O2 UNL A 301 11.002 0.535 19.893 1.00 31.96 O ANISOU 3616 O2 UNL A 301 4479 4407 3257 -175 -122 248 O HETATM 3617 C3 UNL A 301 10.267 1.628 20.431 1.00 26.87 C ANISOU 3617 C3 UNL A 301 3843 3818 2548 -169 -95 212 C HETATM 3618 O3 UNL A 301 11.910 2.782 18.332 1.00 35.01 O ANISOU 3618 O3 UNL A 301 4830 4768 3705 -137 -130 136 O HETATM 3619 C4 UNL A 301 9.144 1.105 21.320 1.00 25.42 C ANISOU 3619 C4 UNL A 301 3674 3678 2305 -190 -49 252 C HETATM 3620 S SO4 A 302 8.768 -2.934 24.753 1.00 40.75 S HETATM 3621 O1 SO4 A 302 7.624 -2.106 25.094 1.00 42.77 O HETATM 3622 O2 SO4 A 302 8.776 -3.188 23.320 1.00 42.99 O HETATM 3623 O3 SO4 A 302 10.008 -2.277 25.142 1.00 42.18 O HETATM 3624 O4 SO4 A 302 8.670 -4.198 25.472 1.00 47.96 O HETATM 3625 C1 UNL B 301 42.997 10.414 21.213 1.00 37.75 C ANISOU 3625 C1 UNL B 301 4837 4962 4543 -269 -92 450 C HETATM 3626 C2 UNL B 301 43.720 9.470 22.170 1.00 38.51 C ANISOU 3626 C2 UNL B 301 4859 5174 4600 -248 -123 563 C HETATM 3627 O2 UNL B 301 42.681 10.830 23.880 1.00 47.40 O ANISOU 3627 O2 UNL B 301 6022 6437 5550 -335 -151 428 O HETATM 3628 C3 UNL B 301 43.165 9.519 23.590 1.00 41.38 C ANISOU 3628 C3 UNL B 301 5216 5663 4845 -271 -147 568 C HETATM 3629 O3 UNL B 301 41.600 10.107 21.150 1.00 42.69 O ANISOU 3629 O3 UNL B 301 5515 5531 5173 -246 -58 436 O HETATM 3630 C4 UNL B 301 44.244 9.162 24.607 1.00 38.21 C ANISOU 3630 C4 UNL B 301 4721 5433 4363 -277 -207 662 C HETATM 3631 S SO4 B 302 45.152 10.658 29.854 1.00 55.89 S HETATM 3632 O1 SO4 B 302 46.492 10.105 30.006 1.00 55.22 O HETATM 3633 O2 SO4 B 302 44.651 10.326 28.525 1.00 55.50 O HETATM 3634 O3 SO4 B 302 44.273 10.083 30.867 1.00 57.36 O HETATM 3635 O4 SO4 B 302 45.191 12.109 30.028 1.00 58.02 O HETATM 3636 C CO3 B 303 32.441 9.551 0.606 1.00 61.74 C HETATM 3637 O1 CO3 B 303 32.072 10.281 -0.401 1.00 61.07 O HETATM 3638 O2 CO3 B 303 31.980 9.806 1.794 1.00 63.83 O HETATM 3639 O3 CO3 B 303 33.269 8.568 0.425 1.00 62.94 O HETATM 3640 O HOH A 401 1.509 -3.606 27.362 1.00 39.37 O HETATM 3641 O HOH A 402 6.190 -15.503 10.473 1.00 35.55 O HETATM 3642 O HOH A 403 9.185 11.164 24.336 1.00 20.99 O HETATM 3643 O HOH A 404 -6.742 -10.584 -3.175 1.00 40.16 O HETATM 3644 O HOH A 405 13.025 -0.540 4.575 1.00 34.68 O HETATM 3645 O HOH A 406 3.213 -10.342 7.123 1.00 43.69 O HETATM 3646 O HOH A 407 6.454 -17.975 8.561 1.00 51.27 O HETATM 3647 O HOH A 408 25.943 -14.756 22.495 1.00 57.37 O HETATM 3648 O HOH A 409 20.147 10.262 1.537 1.00 37.44 O HETATM 3649 O HOH A 410 12.097 25.840 10.983 1.00 47.61 O HETATM 3650 O HOH A 411 10.961 -0.554 17.330 1.00 26.08 O HETATM 3651 O HOH A 412 -10.369 9.426 20.298 1.00 48.19 O HETATM 3652 O HOH A 413 13.909 17.680 26.603 1.00 48.80 O HETATM 3653 O HOH A 414 -3.550 -6.288 -1.819 1.00 29.81 O HETATM 3654 O HOH A 415 21.902 14.972 20.239 1.00 48.99 O HETATM 3655 O HOH A 416 -1.197 6.150 22.950 1.00 23.35 O HETATM 3656 O HOH A 417 0.375 22.767 10.180 1.00 54.08 O HETATM 3657 O HOH A 418 28.905 -0.945 14.745 1.00 28.53 O HETATM 3658 O HOH A 419 12.431 7.993 2.445 1.00 27.38 O HETATM 3659 O HOH A 420 -4.123 -7.991 25.557 1.00 30.52 O HETATM 3660 O HOH A 421 2.134 -14.348 22.062 1.00 29.14 O HETATM 3661 O HOH A 422 -7.109 13.270 8.030 1.00 36.12 O HETATM 3662 O HOH A 423 16.158 18.214 18.816 1.00 25.89 O HETATM 3663 O HOH A 424 12.122 2.065 23.284 1.00 32.73 O HETATM 3664 O HOH A 425 0.932 -0.488 24.866 1.00 38.39 O HETATM 3665 O HOH A 426 11.648 22.762 -0.453 1.00 41.42 O HETATM 3666 O HOH A 427 4.290 11.401 3.472 1.00 22.45 O HETATM 3667 O HOH A 428 -7.038 0.690 2.142 1.00 49.90 O HETATM 3668 O HOH A 429 20.788 -9.568 21.614 1.00 40.12 O HETATM 3669 O HOH A 430 -4.616 -4.790 7.124 1.00 32.44 O HETATM 3670 O HOH A 431 -6.199 18.779 22.478 1.00 36.58 O HETATM 3671 O HOH A 432 30.760 5.273 15.747 1.00 33.80 O HETATM 3672 O HOH A 433 30.255 2.621 15.436 1.00 26.05 O HETATM 3673 O HOH A 434 3.350 -16.951 24.246 1.00 42.84 O HETATM 3674 O HOH A 435 3.509 7.372 23.587 1.00 28.11 O HETATM 3675 O HOH A 436 12.381 -9.593 6.522 1.00 38.54 O HETATM 3676 O HOH A 437 5.784 4.358 3.025 1.00 34.49 O HETATM 3677 O HOH A 438 -10.695 -7.103 12.269 1.00 46.55 O HETATM 3678 O HOH A 439 -0.463 -15.493 9.421 1.00 41.88 O HETATM 3679 O HOH A 440 26.817 7.125 16.984 1.00 26.23 O HETATM 3680 O HOH A 441 5.524 20.703 15.814 1.00 30.90 O HETATM 3681 O HOH A 442 24.888 -1.875 1.404 1.00 54.32 O HETATM 3682 O HOH A 443 -0.972 -2.412 23.537 1.00 45.46 O HETATM 3683 O HOH A 444 24.126 11.278 5.369 1.00 27.16 O HETATM 3684 O HOH A 445 29.604 -3.455 7.914 1.00 29.71 O HETATM 3685 O HOH A 446 25.544 -13.224 11.522 1.00 38.92 O HETATM 3686 O HOH A 447 10.925 -1.637 21.590 1.00 38.09 O HETATM 3687 O HOH A 448 21.853 4.494 4.516 1.00 22.79 O HETATM 3688 O HOH A 449 5.840 7.802 1.794 1.00 34.73 O HETATM 3689 O HOH A 450 25.029 -5.047 27.466 1.00 41.30 O HETATM 3690 O HOH A 451 -6.699 -9.441 21.691 1.00 39.96 O HETATM 3691 O HOH A 452 18.868 10.609 19.272 1.00 27.47 O HETATM 3692 O HOH A 453 15.515 -6.869 22.740 1.00 33.27 O HETATM 3693 O HOH A 454 7.018 25.328 6.873 1.00 52.44 O HETATM 3694 O HOH A 455 21.769 12.420 4.293 1.00 31.36 O HETATM 3695 O HOH A 456 10.908 23.867 5.868 1.00 51.54 O HETATM 3696 O HOH A 457 15.391 -2.103 24.271 1.00 35.65 O HETATM 3697 O HOH A 458 26.726 3.350 27.107 1.00 41.78 O HETATM 3698 O HOH A 459 14.586 -16.197 17.164 1.00 34.62 O HETATM 3699 O HOH A 460 6.223 -2.948 22.112 1.00 23.13 O HETATM 3700 O HOH A 461 21.062 -3.344 5.113 1.00 41.64 O HETATM 3701 O HOH A 462 15.427 15.127 21.559 1.00 35.67 O HETATM 3702 O HOH A 463 29.253 -8.286 12.723 1.00 40.28 O HETATM 3703 O HOH A 464 20.098 8.470 18.203 1.00 33.96 O HETATM 3704 O HOH A 465 29.275 1.337 22.109 1.00 27.34 O HETATM 3705 O HOH A 466 -8.964 -4.133 17.631 1.00 31.69 O HETATM 3706 O HOH A 467 3.891 1.017 28.151 1.00 37.92 O HETATM 3707 O HOH A 468 9.534 -10.501 7.385 1.00 51.13 O HETATM 3708 O HOH A 469 20.171 -5.804 5.722 1.00 54.38 O HETATM 3709 O HOH A 470 2.804 9.108 28.291 1.00 37.60 O HETATM 3710 O HOH A 471 8.392 -14.257 8.799 1.00 37.07 O HETATM 3711 O HOH A 472 20.506 1.889 2.857 1.00 44.08 O HETATM 3712 O HOH A 473 15.552 24.417 15.147 1.00 39.19 O HETATM 3713 O HOH A 474 21.188 -0.298 20.498 1.00 26.35 O HETATM 3714 O HOH A 475 2.128 11.547 2.079 1.00 48.74 O HETATM 3715 O HOH A 476 18.155 17.723 4.485 1.00 44.81 O HETATM 3716 O HOH A 477 8.101 -6.041 -0.682 1.00 40.16 O HETATM 3717 O HOH A 478 16.290 -12.014 3.898 1.00 43.43 O HETATM 3718 O HOH A 479 29.663 -10.145 6.426 1.00 35.21 O HETATM 3719 O HOH A 480 22.713 20.028 11.265 1.00 43.85 O HETATM 3720 O HOH A 481 8.479 16.650 22.639 1.00 26.73 O HETATM 3721 O HOH A 482 -3.756 15.145 1.564 1.00 51.25 O HETATM 3722 O HOH A 483 7.773 14.876 27.561 1.00 51.41 O HETATM 3723 O HOH A 484 22.221 7.025 22.445 1.00 41.73 O HETATM 3724 O HOH A 485 27.311 0.494 6.272 1.00 42.11 O HETATM 3725 O HOH A 486 7.290 1.497 2.980 1.00 41.94 O HETATM 3726 O HOH A 487 -1.564 11.041 -0.932 1.00 43.53 O HETATM 3727 O HOH A 488 8.894 12.907 -0.086 1.00 43.12 O HETATM 3728 O HOH A 489 5.810 9.787 30.827 1.00 53.99 O HETATM 3729 O HOH A 490 7.597 -6.304 23.528 1.00 30.23 O HETATM 3730 O HOH A 491 24.738 5.803 18.883 1.00 15.99 O HETATM 3731 O HOH A 492 14.982 1.384 2.861 1.00 50.34 O HETATM 3732 O HOH A 493 1.015 20.402 7.337 1.00 38.60 O HETATM 3733 O HOH A 494 18.120 3.920 26.232 1.00 37.39 O HETATM 3734 O HOH A 495 28.569 -9.380 25.714 1.00 49.73 O HETATM 3735 O HOH A 496 -9.454 -8.845 11.072 1.00 54.55 O HETATM 3736 O HOH A 497 19.300 -17.829 13.049 1.00 40.66 O HETATM 3737 O HOH A 498 21.827 23.146 17.741 1.00 42.13 O HETATM 3738 O HOH A 499 -7.416 3.129 23.916 1.00 33.53 O HETATM 3739 O HOH A 500 11.160 -10.389 -1.402 1.00 57.42 O HETATM 3740 O HOH A 501 -7.142 18.012 12.225 1.00 45.17 O HETATM 3741 O HOH A 502 5.341 5.341 0.000 1.00 45.45 O HETATM 3742 O HOH A 503 9.200 19.682 21.020 1.00 31.10 O HETATM 3743 O HOH A 504 -9.493 -6.506 18.428 1.00 41.24 O HETATM 3744 O HOH A 505 -0.116 -6.735 0.293 1.00 45.13 O HETATM 3745 O HOH A 506 17.465 -17.954 15.839 1.00 39.82 O HETATM 3746 O HOH A 507 -8.584 10.292 12.420 1.00 35.02 O HETATM 3747 O HOH A 508 1.004 1.955 27.524 1.00 35.62 O HETATM 3748 O HOH A 509 -0.858 -21.004 21.244 1.00 51.93 O HETATM 3749 O HOH A 510 8.016 24.374 1.460 1.00 50.56 O HETATM 3750 O HOH A 511 18.743 13.542 20.774 1.00 45.63 O HETATM 3751 O HOH A 512 3.938 28.057 14.247 1.00 46.51 O HETATM 3752 O HOH A 513 10.362 -15.287 6.523 1.00 41.13 O HETATM 3753 O HOH A 514 14.747 5.839 -0.958 1.00 47.20 O HETATM 3754 O HOH A 515 -4.094 -10.742 11.694 1.00 49.68 O HETATM 3755 O HOH A 516 9.192 6.661 -0.221 1.00 39.82 O HETATM 3756 O HOH A 517 0.668 2.270 30.743 1.00 45.69 O HETATM 3757 O HOH A 518 6.048 11.610 1.356 1.00 36.03 O HETATM 3758 O HOH A 519 -9.886 15.847 20.913 1.00 45.70 O HETATM 3759 O HOH A 520 2.016 27.060 13.778 1.00 45.57 O HETATM 3760 O HOH A 521 -4.601 13.529 0.181 1.00 54.78 O HETATM 3761 O HOH A 522 13.028 21.167 23.267 1.00 40.09 O HETATM 3762 O HOH A 523 15.583 21.722 22.450 1.00 55.11 O HETATM 3763 O HOH A 524 4.887 -8.866 4.269 1.00 32.26 O HETATM 3764 O HOH A 525 -6.734 19.598 8.831 1.00 58.67 O HETATM 3765 O HOH A 526 18.029 18.076 20.852 1.00 43.60 O HETATM 3766 O HOH A 527 23.848 19.722 14.974 1.00 37.19 O HETATM 3767 O HOH A 528 -2.777 7.969 24.395 1.00 38.01 O HETATM 3768 O HOH A 529 31.419 -7.787 22.161 1.00 35.50 O HETATM 3769 O HOH A 530 10.591 21.193 24.060 1.00 44.36 O HETATM 3770 O HOH A 531 3.732 8.122 -1.162 1.00 39.25 O HETATM 3771 O HOH A 532 -8.689 11.744 10.013 1.00 41.91 O HETATM 3772 O HOH A 533 14.806 22.348 -0.852 1.00 49.22 O HETATM 3773 O HOH A 534 30.579 -9.161 24.628 1.00 51.24 O HETATM 3774 O HOH A 535 -9.987 13.716 23.265 1.00 42.31 O HETATM 3775 O HOH A 536 -2.577 -4.378 -0.651 1.00 32.07 O HETATM 3776 O HOH A 537 7.594 -9.713 5.516 1.00 56.10 O HETATM 3777 O HOH A 538 19.489 7.968 23.770 1.00 45.18 O HETATM 3778 O HOH A 539 2.347 -13.747 27.163 1.00 45.68 O HETATM 3779 O HOH A 540 29.108 -12.101 4.184 1.00 60.97 O HETATM 3780 O HOH A 541 21.794 15.324 2.993 1.00 30.14 O HETATM 3781 O HOH A 542 20.032 16.631 3.169 1.00 43.89 O HETATM 3782 O HOH A 543 -12.787 -7.773 13.822 1.00 49.26 O HETATM 3783 O HOH A 544 14.234 3.725 0.338 1.00 60.45 O HETATM 3784 O HOH A 545 21.321 -17.467 11.542 1.00 48.58 O HETATM 3785 O HOH A 546 28.713 -4.602 5.477 1.00 50.09 O HETATM 3786 O HOH A 547 33.505 -3.202 14.950 1.00 48.07 O HETATM 3787 O HOH A 548 25.353 9.681 3.562 1.00 44.46 O HETATM 3788 O HOH A 549 8.622 12.887 28.988 1.00 54.67 O HETATM 3789 O HOH A 550 14.863 -0.782 26.776 1.00 58.84 O HETATM 3790 O HOH A 551 17.120 -0.021 28.710 1.00 42.15 O HETATM 3791 O HOH A 552 -5.023 -12.951 10.174 1.00 44.57 O HETATM 3792 O HOH A 553 25.375 14.262 5.431 1.00 49.58 O HETATM 3793 O HOH A 554 -6.650 4.544 25.989 1.00 42.61 O HETATM 3794 O HOH A 555 9.779 -8.339 5.124 1.00 44.63 O HETATM 3795 O HOH A 556 22.649 7.518 19.553 1.00 28.94 O HETATM 3796 O HOH A 557 4.349 24.655 7.684 1.00 40.29 O HETATM 3797 O HOH A 558 13.072 15.583 28.862 1.00 60.18 O HETATM 3798 O HOH A 559 17.305 6.297 24.868 1.00 44.58 O HETATM 3799 O HOH A 560 -4.186 6.828 26.962 1.00 56.89 O HETATM 3800 O HOH A 561 -8.438 20.641 10.475 1.00 52.40 O HETATM 3801 O HOH A 562 16.616 6.978 26.856 1.00 53.21 O HETATM 3802 O HOH A 563 14.515 25.762 12.691 1.00 54.80 O HETATM 3803 O HOH A 564 3.629 24.018 5.034 1.00 46.20 O HETATM 3804 O HOH B 401 31.122 8.781 31.684 1.00 48.56 O HETATM 3805 O HOH B 402 44.071 10.939 0.639 1.00 42.61 O HETATM 3806 O HOH B 403 35.486 7.538 0.466 1.00 37.77 O HETATM 3807 O HOH B 404 44.374 -0.290 20.011 1.00 20.67 O HETATM 3808 O HOH B 405 57.606 23.597 16.556 1.00 27.34 O HETATM 3809 O HOH B 406 39.548 -6.485 17.504 1.00 53.91 O HETATM 3810 O HOH B 407 42.571 13.189 22.548 1.00 26.37 O HETATM 3811 O HOH B 408 43.626 26.879 21.834 1.00 39.84 O HETATM 3812 O HOH B 409 29.338 11.967 5.761 1.00 25.07 O HETATM 3813 O HOH B 410 41.677 6.934 25.479 1.00 50.26 O HETATM 3814 O HOH B 411 61.549 24.405 22.799 1.00 46.09 O HETATM 3815 O HOH B 412 44.073 -1.204 -2.985 1.00 47.93 O HETATM 3816 O HOH B 413 24.702 14.005 34.200 1.00 51.93 O HETATM 3817 O HOH B 414 46.649 7.530 30.307 1.00 53.52 O HETATM 3818 O HOH B 415 23.944 21.426 23.915 1.00 39.40 O HETATM 3819 O HOH B 416 61.418 19.619 6.010 1.00 44.64 O HETATM 3820 O HOH B 417 30.140 33.442 19.193 1.00 39.42 O HETATM 3821 O HOH B 418 33.357 5.764 16.513 1.00 23.39 O HETATM 3822 O HOH B 419 32.048 4.417 31.498 1.00 31.43 O HETATM 3823 O HOH B 420 52.813 9.211 27.944 1.00 40.76 O HETATM 3824 O HOH B 421 24.457 14.661 20.730 1.00 26.15 O HETATM 3825 O HOH B 422 56.147 -7.128 11.200 1.00 44.83 O HETATM 3826 O HOH B 423 27.892 9.140 33.828 1.00 44.97 O HETATM 3827 O HOH B 424 22.895 9.315 17.488 1.00 35.37 O HETATM 3828 O HOH B 425 47.465 0.964 29.939 1.00 49.92 O HETATM 3829 O HOH B 426 31.592 17.628 9.679 1.00 32.86 O HETATM 3830 O HOH B 427 37.665 14.421 30.367 1.00 43.15 O HETATM 3831 O HOH B 428 49.796 5.813 29.518 1.00 42.04 O HETATM 3832 O HOH B 429 49.088 13.808 4.257 1.00 31.74 O HETATM 3833 O HOH B 430 23.244 11.691 18.941 1.00 26.05 O HETATM 3834 O HOH B 431 32.508 16.024 31.727 1.00 43.71 O HETATM 3835 O HOH B 432 57.914 13.735 0.652 1.00 51.75 O HETATM 3836 O HOH B 433 52.502 26.934 19.961 1.00 50.01 O HETATM 3837 O HOH B 434 37.349 -2.018 11.186 1.00 28.18 O HETATM 3838 O HOH B 435 25.827 17.486 8.831 1.00 51.54 O HETATM 3839 O HOH B 436 53.386 20.342 2.615 1.00 42.07 O HETATM 3840 O HOH B 437 63.418 15.445 3.053 1.00 33.78 O HETATM 3841 O HOH B 438 40.961 25.297 17.454 1.00 37.64 O HETATM 3842 O HOH B 439 33.094 13.498 30.899 1.00 40.50 O HETATM 3843 O HOH B 440 48.165 -1.665 7.467 1.00 39.11 O HETATM 3844 O HOH B 441 32.421 10.935 24.613 1.00 28.21 O HETATM 3845 O HOH B 442 54.645 10.915 28.203 1.00 39.61 O HETATM 3846 O HOH B 443 45.206 -3.125 14.959 1.00 34.27 O HETATM 3847 O HOH B 444 63.986 25.819 20.801 1.00 66.84 O HETATM 3848 O HOH B 445 24.155 8.394 24.485 1.00 37.84 O HETATM 3849 O HOH B 446 32.622 20.570 10.772 1.00 50.93 O HETATM 3850 O HOH B 447 48.361 21.786 8.023 1.00 34.03 O HETATM 3851 O HOH B 448 52.444 23.965 7.212 1.00 46.51 O HETATM 3852 O HOH B 449 50.390 3.434 21.691 1.00 29.18 O HETATM 3853 O HOH B 450 24.020 21.150 17.179 1.00 36.31 O HETATM 3854 O HOH B 451 46.629 0.956 -2.094 1.00 47.60 O HETATM 3855 O HOH B 452 25.955 19.174 13.984 1.00 29.85 O HETATM 3856 O HOH B 453 40.879 21.610 12.249 1.00 39.29 O HETATM 3857 O HOH B 454 38.073 -1.290 15.234 1.00 24.62 O HETATM 3858 O HOH B 455 47.122 18.435 5.589 1.00 49.77 O HETATM 3859 O HOH B 456 51.720 -0.935 24.355 1.00 33.11 O HETATM 3860 O HOH B 457 27.182 25.910 27.103 1.00 44.21 O HETATM 3861 O HOH B 458 44.242 29.127 25.058 1.00 40.82 O HETATM 3862 O HOH B 459 47.573 12.299 27.756 1.00 28.46 O HETATM 3863 O HOH B 460 35.806 30.209 20.173 1.00 23.01 O HETATM 3864 O HOH B 461 31.427 11.708 3.991 1.00 32.14 O HETATM 3865 O HOH B 462 33.796 28.019 31.843 1.00 45.17 O HETATM 3866 O HOH B 463 62.509 16.560 24.338 1.00 42.24 O HETATM 3867 O HOH B 464 55.202 4.879 22.210 1.00 35.45 O HETATM 3868 O HOH B 465 34.830 3.620 16.675 1.00 23.35 O HETATM 3869 O HOH B 466 43.736 23.143 39.023 1.00 58.53 O HETATM 3870 O HOH B 467 37.921 -3.011 22.572 1.00 54.90 O HETATM 3871 O HOH B 468 49.074 -5.801 18.739 1.00 43.65 O HETATM 3872 O HOH B 469 60.851 1.651 8.251 1.00 56.24 O HETATM 3873 O HOH B 470 40.158 27.229 20.359 1.00 35.31 O HETATM 3874 O HOH B 471 35.826 26.712 32.906 1.00 48.00 O HETATM 3875 O HOH B 472 54.157 23.226 5.462 1.00 42.12 O HETATM 3876 O HOH B 473 26.109 7.548 26.818 1.00 36.21 O HETATM 3877 O HOH B 474 57.959 -3.578 2.650 1.00 54.60 O HETATM 3878 O HOH B 475 49.041 -3.347 25.368 1.00 30.40 O HETATM 3879 O HOH B 476 44.421 -4.371 12.029 1.00 30.88 O HETATM 3880 O HOH B 477 41.274 -6.938 12.723 1.00 43.14 O HETATM 3881 O HOH B 478 60.815 9.360 6.480 1.00 40.05 O HETATM 3882 O HOH B 479 35.521 22.078 10.285 1.00 55.78 O HETATM 3883 O HOH B 480 29.869 -0.656 7.532 1.00 41.60 O HETATM 3884 O HOH B 481 32.367 0.825 1.145 1.00 58.64 O HETATM 3885 O HOH B 482 38.181 21.207 10.348 1.00 51.49 O HETATM 3886 O HOH B 483 23.176 26.938 20.821 1.00 41.02 O HETATM 3887 O HOH B 484 59.883 -4.371 12.788 1.00 56.56 O HETATM 3888 O HOH B 485 35.738 -3.489 13.067 1.00 34.21 O HETATM 3889 O HOH B 486 38.588 9.511 28.584 1.00 46.12 O HETATM 3890 O HOH B 487 56.454 2.567 21.884 1.00 36.05 O HETATM 3891 O HOH B 488 38.084 -7.558 11.233 1.00 57.55 O HETATM 3892 O HOH B 489 31.121 1.349 3.953 1.00 44.35 O HETATM 3893 O HOH B 490 49.716 27.872 20.330 1.00 45.68 O HETATM 3894 O HOH B 491 21.834 12.522 29.167 1.00 36.74 O HETATM 3895 O HOH B 492 48.151 28.086 17.471 1.00 29.11 O HETATM 3896 O HOH B 493 42.592 -4.966 20.017 1.00 55.02 O HETATM 3897 O HOH B 494 38.630 24.708 33.144 1.00 46.55 O HETATM 3898 O HOH B 495 60.962 6.796 25.010 1.00 47.28 O HETATM 3899 O HOH B 496 31.792 -5.092 6.855 1.00 39.39 O HETATM 3900 O HOH B 497 55.511 9.585 3.276 1.00 43.81 O HETATM 3901 O HOH B 498 45.538 -8.493 6.972 1.00 45.83 O HETATM 3902 O HOH B 499 35.422 25.380 14.519 1.00 63.69 O HETATM 3903 O HOH B 500 35.683 3.497 26.055 1.00 50.47 O HETATM 3904 O HOH B 501 54.598 16.507 0.422 1.00 34.82 O HETATM 3905 O HOH B 502 28.879 7.168 19.312 1.00 10.34 O HETATM 3906 O HOH B 503 34.894 0.223 16.064 1.00 42.63 O HETATM 3907 O HOH B 504 63.933 7.538 19.203 1.00 57.94 O HETATM 3908 O HOH B 505 63.587 -0.746 14.640 1.00 35.64 O HETATM 3909 O HOH B 506 38.279 -4.505 4.207 1.00 37.05 O HETATM 3910 O HOH B 507 39.987 18.390 1.549 1.00 50.16 O HETATM 3911 O HOH B 508 29.002 2.450 0.356 1.00 55.94 O HETATM 3912 O HOH B 509 30.360 9.615 35.806 1.00 56.26 O HETATM 3913 O HOH B 510 30.917 2.994 -0.722 1.00 53.14 O HETATM 3914 O HOH B 511 31.714 3.561 21.205 1.00 41.11 O HETATM 3915 O HOH B 512 22.072 14.655 31.370 1.00 43.43 O HETATM 3916 O HOH B 513 45.089 -8.515 10.238 1.00 46.68 O HETATM 3917 O HOH B 514 40.607 -6.645 4.782 1.00 45.29 O HETATM 3918 O HOH B 515 42.752 -6.909 3.520 1.00 38.96 O HETATM 3919 O HOH B 516 48.719 17.515 3.817 1.00 51.86 O HETATM 3920 O HOH B 517 52.319 -5.579 23.522 1.00 47.28 O HETATM 3921 O HOH B 518 23.130 11.286 23.472 1.00 54.97 O HETATM 3922 O HOH B 519 33.940 2.116 21.498 1.00 45.19 O HETATM 3923 O HOH B 520 39.402 20.382 3.729 1.00 57.49 O HETATM 3924 O HOH B 521 63.921 -0.748 17.158 1.00 41.26 O HETATM 3925 O HOH B 522 43.376 27.117 19.333 1.00 43.91 O HETATM 3926 O HOH B 523 43.524 -7.079 12.458 1.00 34.04 O HETATM 3927 O HOH B 524 60.969 10.987 -1.327 1.00 55.94 O HETATM 3928 O HOH B 525 25.570 4.758 28.600 1.00 53.36 O HETATM 3929 O HOH B 526 42.796 -1.979 22.076 1.00 51.03 O HETATM 3930 O HOH B 527 22.459 14.301 34.362 1.00 49.39 O HETATM 3931 O HOH B 528 23.501 23.829 25.701 1.00 43.33 O HETATM 3932 O HOH B 529 22.563 9.987 21.611 1.00 44.28 O HETATM 3933 O HOH B 530 21.765 25.706 24.438 1.00 47.07 O HETATM 3934 O HOH B 531 28.036 9.800 3.736 1.00 49.71 O HETATM 3935 O HOH B 532 31.038 5.175 18.933 1.00 32.50 O HETATM 3936 O HOH B 533 28.114 14.786 4.782 1.00 44.04 O HETATM 3937 O HOH B 534 38.598 22.807 34.942 1.00 55.97 O HETATM 3938 O HOH B 535 61.963 -3.940 11.047 1.00 57.69 O HETATM 3939 O HOH B 536 50.055 -7.782 16.763 1.00 42.08 O HETATM 3940 O HOH B 537 65.340 8.342 21.020 1.00 58.30 O HETATM 3941 O HOH B 538 24.347 25.028 27.760 1.00 56.96 O HETATM 3942 O HOH B 539 67.579 8.726 18.984 1.00 58.63 O CONECT 1243 3614 CONECT 3044 3625 CONECT 3614 1243 CONECT 3620 3621 3622 3623 3624 CONECT 3621 3620 CONECT 3622 3620 CONECT 3623 3620 CONECT 3624 3620 CONECT 3625 3044 CONECT 3631 3632 3633 3634 3635 CONECT 3632 3631 CONECT 3633 3631 CONECT 3634 3631 CONECT 3635 3631 CONECT 3636 3637 3638 3639 CONECT 3637 3636 CONECT 3638 3636 CONECT 3639 3636 MASTER 392 0 5 24 20 0 8 6 3929 2 18 42 END