HEADER MEMBRANE PROTEIN 03-JAN-17 5UEN TITLE CRYSTAL STRUCTURE OF THE HUMAN ADENOSINE A1 RECEPTOR A1AR-BRIL IN TITLE 2 COMPLEX WITH THE COVALENT ANTAGONIST DU172 AT 3.2A RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A1,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A1; COMPND 4 CHAIN: A, B; COMPND 5 FRAGMENT: UNP P30542 REISUES 2-210, UNP P0ABE7 RESIDUES 23-127, UNP COMPND 6 P30542 RESIDUES 228-31,UNP P30542 REISUES 2-210, UNP P0ABE7 RESIDUES COMPND 7 23-127, UNP P30542 RESIDUES 228-31,UNP P30542 REISUES 2-210, UNP COMPND 8 P0ABE7 RESIDUES 23-127, UNP P30542 RESIDUES 228-31; COMPND 9 SYNONYM: CYTOCHROME B-562; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA1, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS KEYWDS GPCR, TRANSMEMBRANE, RECEPTOR, ADENOSINE, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.GLUKHOVA,D.M.THAL,A.T.NGUYEN,E.A.VECCHIO,M.JORG,P.J.SCAMMELLS, AUTHOR 2 L.T.MAY,P.M.SEXTON,A.CHRISTOPOULOS REVDAT 4 08-JAN-20 5UEN 1 REMARK REVDAT 3 27-SEP-17 5UEN 1 REMARK REVDAT 2 15-MAR-17 5UEN 1 JRNL REVDAT 1 01-MAR-17 5UEN 0 JRNL AUTH A.GLUKHOVA,D.M.THAL,A.T.NGUYEN,E.A.VECCHIO,M.JORG, JRNL AUTH 2 P.J.SCAMMELLS,L.T.MAY,P.M.SEXTON,A.CHRISTOPOULOS JRNL TITL STRUCTURE OF THE ADENOSINE A1 RECEPTOR REVEALS THE BASIS FOR JRNL TITL 2 SUBTYPE SELECTIVITY. JRNL REF CELL V. 168 867 2017 JRNL REFN ISSN 1097-4172 JRNL PMID 28235198 JRNL DOI 10.1016/J.CELL.2017.01.042 REMARK 2 REMARK 2 RESOLUTION. 3.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0155 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 21759 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.288 REMARK 3 R VALUE (WORKING SET) : 0.286 REMARK 3 FREE R VALUE : 0.316 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800 REMARK 3 FREE R VALUE TEST SET COUNT : 1105 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1598 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.17 REMARK 3 BIN R VALUE (WORKING SET) : 0.3660 REMARK 3 BIN FREE R VALUE SET COUNT : 69 REMARK 3 BIN FREE R VALUE : 0.4240 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6061 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 189 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 92.83 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -6.32000 REMARK 3 B22 (A**2) : 6.09000 REMARK 3 B33 (A**2) : 0.23000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.553 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.482 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 59.391 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : NULL REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 5UEN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-17. REMARK 100 THE DEPOSITION ID IS D_1000224321. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-MAR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0-8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON REMARK 200 BEAMLINE : MX2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537 REMARK 200 MONOCHROMATOR : SILICON DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.15 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23000 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 14.10 REMARK 200 R MERGE (I) : 0.32800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 14.40 REMARK 200 R MERGE FOR SHELL (I) : 2.76700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.5.6 REMARK 200 STARTING MODEL: 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.15 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 7.0-8.0, 28-38% PEG REMARK 280 300 AND 500-700 MM NH4F, LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 X,-Y,-Z REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 -X,-Y+1/2,Z+1/2 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.48000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.08550 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.48000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 62.08550 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 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 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 GLY A 0 REMARK 465 PRO A 1 REMARK 465 PRO A 2 REMARK 465 PRO A 3 REMARK 465 LEU A 1014 REMARK 465 LYS A 1015 REMARK 465 VAL A 1016 REMARK 465 ILE A 1017 REMARK 465 GLU A 1018 REMARK 465 LYS A 1019 REMARK 465 ALA A 1020 REMARK 465 ASP A 1021 REMARK 465 ASN A 1022 REMARK 465 ALA A 1023 REMARK 465 ALA A 1024 REMARK 465 GLN A 1025 REMARK 465 GLN A 1041 REMARK 465 LYS A 1042 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 GLN A 317 REMARK 465 GLY B 0 REMARK 465 PRO B 1 REMARK 465 PRO B 2 REMARK 465 PRO B 3 REMARK 465 SER B 4 REMARK 465 ILE B 5 REMARK 465 ALA B 1043 REMARK 465 THR B 1044 REMARK 465 PRO B 1045 REMARK 465 PRO B 1046 REMARK 465 LYS B 1047 REMARK 465 LEU B 1048 REMARK 465 GLU B 1049 REMARK 465 ASP B 1050 REMARK 465 LYS B 1051 REMARK 465 SER B 1052 REMARK 465 PRO B 1053 REMARK 465 ASP B 1054 REMARK 465 SER B 1055 REMARK 465 PRO B 1056 REMARK 465 GLU B 1057 REMARK 465 MET B 1058 REMARK 465 LYS B 1059 REMARK 465 ASP B 1060 REMARK 465 PHE B 1061 REMARK 465 GLN B 310 REMARK 465 PRO B 311 REMARK 465 LEU B 312 REMARK 465 GLU B 313 REMARK 465 VAL B 314 REMARK 465 LEU B 315 REMARK 465 PHE B 316 REMARK 465 GLN B 317 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 ARG A 41 56.18 -99.57 REMARK 500 VAL A 189 -61.70 -108.85 REMARK 500 ARG B 41 56.07 -99.62 REMARK 500 VAL B 189 -62.29 -109.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 1204 REMARK 610 OLA A 1205 REMARK 610 OLA B 1204 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue DU1 A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue DU1 B 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA B 1204 DBREF 5UEN A 2 211 UNP P30542 AA1R_HUMAN 2 211 DBREF 5UEN A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127 DBREF 5UEN A 228 311 UNP P30542 AA1R_HUMAN 228 311 DBREF 5UEN B 2 211 UNP P30542 AA1R_HUMAN 2 211 DBREF 5UEN B 1001 1105 UNP P0ABE7 C562_ECOLX 23 127 DBREF 5UEN B 228 311 UNP P30542 AA1R_HUMAN 228 311 SEQADV 5UEN GLY A 0 UNP P30542 EXPRESSION TAG SEQADV 5UEN PRO A 1 UNP P30542 EXPRESSION TAG SEQADV 5UEN ALA A 159 UNP P30542 ASN 159 ENGINEERED MUTATION SEQADV 5UEN TRP A 1007 UNP P0ABE7 MET 29 CONFLICT SEQADV 5UEN ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT SEQADV 5UEN LEU A 1106 UNP P0ABE7 LINKER SEQADV 5UEN GLU A 220 UNP P0ABE7 LINKER SEQADV 5UEN ARG A 221 UNP P0ABE7 LINKER SEQADV 5UEN ALA A 222 UNP P0ABE7 LINKER SEQADV 5UEN ARG A 223 UNP P0ABE7 LINKER SEQADV 5UEN SER A 224 UNP P0ABE7 LINKER SEQADV 5UEN THR A 225 UNP P0ABE7 LINKER SEQADV 5UEN LEU A 226 UNP P0ABE7 LINKER SEQADV 5UEN GLN A 227 UNP P0ABE7 LINKER SEQADV 5UEN LEU A 312 UNP P30542 EXPRESSION TAG SEQADV 5UEN GLU A 313 UNP P30542 EXPRESSION TAG SEQADV 5UEN VAL A 314 UNP P30542 EXPRESSION TAG SEQADV 5UEN LEU A 315 UNP P30542 EXPRESSION TAG SEQADV 5UEN PHE A 316 UNP P30542 EXPRESSION TAG SEQADV 5UEN GLN A 317 UNP P30542 EXPRESSION TAG SEQADV 5UEN GLY B 0 UNP P30542 EXPRESSION TAG SEQADV 5UEN PRO B 1 UNP P30542 EXPRESSION TAG SEQADV 5UEN ALA B 159 UNP P30542 ASN 159 ENGINEERED MUTATION SEQADV 5UEN TRP B 1007 UNP P0ABE7 MET 29 CONFLICT SEQADV 5UEN ILE B 1102 UNP P0ABE7 HIS 124 CONFLICT SEQADV 5UEN LEU B 1106 UNP P0ABE7 LINKER SEQADV 5UEN GLU B 220 UNP P0ABE7 LINKER SEQADV 5UEN ARG B 221 UNP P0ABE7 LINKER SEQADV 5UEN ALA B 222 UNP P0ABE7 LINKER SEQADV 5UEN ARG B 223 UNP P0ABE7 LINKER SEQADV 5UEN SER B 224 UNP P0ABE7 LINKER SEQADV 5UEN THR B 225 UNP P0ABE7 LINKER SEQADV 5UEN LEU B 226 UNP P0ABE7 LINKER SEQADV 5UEN GLN B 227 UNP P0ABE7 LINKER SEQADV 5UEN LEU B 312 UNP P30542 EXPRESSION TAG SEQADV 5UEN GLU B 313 UNP P30542 EXPRESSION TAG SEQADV 5UEN VAL B 314 UNP P30542 EXPRESSION TAG SEQADV 5UEN LEU B 315 UNP P30542 EXPRESSION TAG SEQADV 5UEN PHE B 316 UNP P30542 EXPRESSION TAG SEQADV 5UEN GLN B 317 UNP P30542 EXPRESSION TAG SEQRES 1 A 416 GLY PRO PRO PRO SER ILE SER ALA PHE GLN ALA ALA TYR SEQRES 2 A 416 ILE GLY ILE GLU VAL LEU ILE ALA LEU VAL SER VAL PRO SEQRES 3 A 416 GLY ASN VAL LEU VAL ILE TRP ALA VAL LYS VAL ASN GLN SEQRES 4 A 416 ALA LEU ARG ASP ALA THR PHE CYS PHE ILE VAL SER LEU SEQRES 5 A 416 ALA VAL ALA ASP VAL ALA VAL GLY ALA LEU VAL ILE PRO SEQRES 6 A 416 LEU ALA ILE LEU ILE ASN ILE GLY PRO GLN THR TYR PHE SEQRES 7 A 416 HIS THR CYS LEU MET VAL ALA CYS PRO VAL LEU ILE LEU SEQRES 8 A 416 THR GLN SER SER ILE LEU ALA LEU LEU ALA ILE ALA VAL SEQRES 9 A 416 ASP ARG TYR LEU ARG VAL LYS ILE PRO LEU ARG TYR LYS SEQRES 10 A 416 MET VAL VAL THR PRO ARG ARG ALA ALA VAL ALA ILE ALA SEQRES 11 A 416 GLY CYS TRP ILE LEU SER PHE VAL VAL GLY LEU THR PRO SEQRES 12 A 416 MET PHE GLY TRP ASN ASN LEU SER ALA VAL GLU ARG ALA SEQRES 13 A 416 TRP ALA ALA ALA GLY SER MET GLY GLU PRO VAL ILE LYS SEQRES 14 A 416 CYS GLU PHE GLU LYS VAL ILE SER MET GLU TYR MET VAL SEQRES 15 A 416 TYR PHE ASN PHE PHE VAL TRP VAL LEU PRO PRO LEU LEU SEQRES 16 A 416 LEU MET VAL LEU ILE TYR LEU GLU VAL PHE TYR LEU ILE SEQRES 17 A 416 ARG LYS GLN LEU ALA ASP LEU GLU ASP ASN TRP GLU THR SEQRES 18 A 416 LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN SEQRES 19 A 416 ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA SEQRES 20 A 416 ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU SEQRES 21 A 416 GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE SEQRES 22 A 416 ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP SEQRES 23 A 416 ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA SEQRES 24 A 416 GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA SEQRES 25 A 416 TYR ILE GLN LYS TYR LEU GLU ARG ALA ARG SER THR LEU SEQRES 26 A 416 GLN LYS GLU LEU LYS ILE ALA LYS SER LEU ALA LEU ILE SEQRES 27 A 416 LEU PHE LEU PHE ALA LEU SER TRP LEU PRO LEU HIS ILE SEQRES 28 A 416 LEU ASN CYS ILE THR LEU PHE CYS PRO SER CYS HIS LYS SEQRES 29 A 416 PRO SER ILE LEU THR TYR ILE ALA ILE PHE LEU THR HIS SEQRES 30 A 416 GLY ASN SER ALA MET ASN PRO ILE VAL TYR ALA PHE ARG SEQRES 31 A 416 ILE GLN LYS PHE ARG VAL THR PHE LEU LYS ILE TRP ASN SEQRES 32 A 416 ASP HIS PHE ARG CYS GLN PRO LEU GLU VAL LEU PHE GLN SEQRES 1 B 416 GLY PRO PRO PRO SER ILE SER ALA PHE GLN ALA ALA TYR SEQRES 2 B 416 ILE GLY ILE GLU VAL LEU ILE ALA LEU VAL SER VAL PRO SEQRES 3 B 416 GLY ASN VAL LEU VAL ILE TRP ALA VAL LYS VAL ASN GLN SEQRES 4 B 416 ALA LEU ARG ASP ALA THR PHE CYS PHE ILE VAL SER LEU SEQRES 5 B 416 ALA VAL ALA ASP VAL ALA VAL GLY ALA LEU VAL ILE PRO SEQRES 6 B 416 LEU ALA ILE LEU ILE ASN ILE GLY PRO GLN THR TYR PHE SEQRES 7 B 416 HIS THR CYS LEU MET VAL ALA CYS PRO VAL LEU ILE LEU SEQRES 8 B 416 THR GLN SER SER ILE LEU ALA LEU LEU ALA ILE ALA VAL SEQRES 9 B 416 ASP ARG TYR LEU ARG VAL LYS ILE PRO LEU ARG TYR LYS SEQRES 10 B 416 MET VAL VAL THR PRO ARG ARG ALA ALA VAL ALA ILE ALA SEQRES 11 B 416 GLY CYS TRP ILE LEU SER PHE VAL VAL GLY LEU THR PRO SEQRES 12 B 416 MET PHE GLY TRP ASN ASN LEU SER ALA VAL GLU ARG ALA SEQRES 13 B 416 TRP ALA ALA ALA GLY SER MET GLY GLU PRO VAL ILE LYS SEQRES 14 B 416 CYS GLU PHE GLU LYS VAL ILE SER MET GLU TYR MET VAL SEQRES 15 B 416 TYR PHE ASN PHE PHE VAL TRP VAL LEU PRO PRO LEU LEU SEQRES 16 B 416 LEU MET VAL LEU ILE TYR LEU GLU VAL PHE TYR LEU ILE SEQRES 17 B 416 ARG LYS GLN LEU ALA ASP LEU GLU ASP ASN TRP GLU THR SEQRES 18 B 416 LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN SEQRES 19 B 416 ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA SEQRES 20 B 416 ALA ALA LEU ASP ALA GLN LYS ALA THR PRO PRO LYS LEU SEQRES 21 B 416 GLU ASP LYS SER PRO ASP SER PRO GLU MET LYS ASP PHE SEQRES 22 B 416 ARG HIS GLY PHE ASP ILE LEU VAL GLY GLN ILE ASP ASP SEQRES 23 B 416 ALA LEU LYS LEU ALA ASN GLU GLY LYS VAL LYS GLU ALA SEQRES 24 B 416 GLN ALA ALA ALA GLU GLN LEU LYS THR THR ARG ASN ALA SEQRES 25 B 416 TYR ILE GLN LYS TYR LEU GLU ARG ALA ARG SER THR LEU SEQRES 26 B 416 GLN LYS GLU LEU LYS ILE ALA LYS SER LEU ALA LEU ILE SEQRES 27 B 416 LEU PHE LEU PHE ALA LEU SER TRP LEU PRO LEU HIS ILE SEQRES 28 B 416 LEU ASN CYS ILE THR LEU PHE CYS PRO SER CYS HIS LYS SEQRES 29 B 416 PRO SER ILE LEU THR TYR ILE ALA ILE PHE LEU THR HIS SEQRES 30 B 416 GLY ASN SER ALA MET ASN PRO ILE VAL TYR ALA PHE ARG SEQRES 31 B 416 ILE GLN LYS PHE ARG VAL THR PHE LEU LYS ILE TRP ASN SEQRES 32 B 416 ASP HIS PHE ARG CYS GLN PRO LEU GLU VAL LEU PHE GLN HET DU1 A1201 35 HET OLA A1202 20 HET OLA A1203 20 HET OLA A1204 14 HET OLA A1205 12 HET DU1 B1201 35 HET OLA B1202 20 HET OLA B1203 20 HET OLA B1204 13 HETNAM DU1 4-{[3-(8-CYCLOHEXYL-2,6-DIOXO-1-PROPYL-1,2,6,7- HETNAM 2 DU1 TETRAHYDRO-3H-PURIN-3-YL)PROPYL]CARBAMOYL}BENZENE-1- HETNAM 3 DU1 SULFONYL FLUORIDE HETNAM OLA OLEIC ACID FORMUL 3 DU1 2(C24 H30 F N5 O5 S) FORMUL 4 OLA 7(C18 H34 O2) HELIX 1 AA1 SER A 6 ASN A 37 1 32 HELIX 2 AA2 GLN A 38 ARG A 41 5 4 HELIX 3 AA3 ASP A 42 LEU A 61 1 20 HELIX 4 AA4 LEU A 61 GLY A 72 1 12 HELIX 5 AA5 PHE A 77 ILE A 111 1 35 HELIX 6 AA6 ARG A 114 VAL A 119 1 6 HELIX 7 AA7 THR A 120 THR A 141 1 22 HELIX 8 AA8 PRO A 142 GLY A 145 5 4 HELIX 9 AA9 ASN A 148 GLY A 160 1 13 HELIX 10 AB1 GLU A 170 ILE A 175 1 6 HELIX 11 AB2 SER A 176 PHE A 183 1 8 HELIX 12 AB3 PHE A 183 VAL A 189 1 7 HELIX 13 AB4 VAL A 189 ASN A 1013 1 36 HELIX 14 AB5 LYS A 1027 ALA A 1040 1 14 HELIX 15 AB6 GLU A 1057 GLY A 1082 1 26 HELIX 16 AB7 LYS A 1083 TYR A 1101 1 19 HELIX 17 AB8 TYR A 1101 CYS A 260 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 PHE A 307 1 16 HELIX 20 AC2 CYS A 309 PHE A 316 1 8 HELIX 21 AC3 ALA B 7 ASN B 37 1 31 HELIX 22 AC4 GLN B 38 ARG B 41 5 4 HELIX 23 AC5 ASP B 42 LEU B 61 1 20 HELIX 24 AC6 LEU B 61 GLY B 72 1 12 HELIX 25 AC7 PHE B 77 ILE B 111 1 35 HELIX 26 AC8 ARG B 114 VAL B 119 1 6 HELIX 27 AC9 THR B 120 THR B 141 1 22 HELIX 28 AD1 PRO B 142 GLY B 145 5 4 HELIX 29 AD2 ASN B 148 GLY B 160 1 13 HELIX 30 AD3 GLU B 170 ILE B 175 1 6 HELIX 31 AD4 SER B 176 PHE B 183 1 8 HELIX 32 AD5 PHE B 183 VAL B 189 1 7 HELIX 33 AD6 VAL B 189 LYS B 1019 1 42 HELIX 34 AD7 ASN B 1022 LYS B 1042 1 21 HELIX 35 AD8 HIS B 1063 GLY B 1082 1 20 HELIX 36 AD9 LYS B 1083 TYR B 1101 1 19 HELIX 37 AE1 TYR B 1101 CYS B 260 1 47 HELIX 38 AE2 PRO B 266 ILE B 292 1 27 HELIX 39 AE3 ILE B 292 PHE B 307 1 16 SHEET 1 AA1 2 THR A 75 TYR A 76 0 SHEET 2 AA1 2 VAL A 166 ILE A 167 -1 O ILE A 167 N THR A 75 SHEET 1 AA2 2 THR B 75 TYR B 76 0 SHEET 2 AA2 2 VAL B 166 ILE B 167 -1 O ILE B 167 N THR B 75 SSBOND 1 CYS A 80 CYS A 169 1555 1555 2.02 SSBOND 2 CYS A 260 CYS A 263 1555 1555 2.04 SSBOND 3 CYS B 80 CYS B 169 1555 1555 2.04 SSBOND 4 CYS B 260 CYS B 263 1555 1555 2.04 LINK OH TYR A 271 S DU1 A1201 1555 1555 1.61 LINK OH TYR B 271 S DU1 B1201 1555 1555 1.61 SITE 1 AC1 13 TYR A 12 ASN A 70 VAL A 87 LEU A 88 SITE 2 AC1 13 THR A 91 PHE A 171 GLU A 172 MET A 180 SITE 3 AC1 13 TRP A 247 LEU A 250 ASN A 254 TYR A 271 SITE 4 AC1 13 ILE A 274 SITE 1 AC2 4 ALA A 125 VAL A 137 PHE A 144 OLA A1203 SITE 1 AC3 4 CYS A 46 VAL A 49 ILE A 89 OLA A1202 SITE 1 AC4 3 ILE A 5 ALA A 7 LEU A 18 SITE 1 AC5 4 PHE A 8 ASN A 70 ILE A 268 TYR A 271 SITE 1 AC6 11 TYR B 12 VAL B 87 LEU B 88 THR B 91 SITE 2 AC6 11 PHE B 171 MET B 180 TRP B 247 LEU B 250 SITE 3 AC6 11 ASN B 254 TYR B 271 ILE B 274 SITE 1 AC7 4 ALA B 125 PHE B 136 VAL B 137 OLA B1203 SITE 1 AC8 4 VAL B 49 ILE B 89 TRP B 132 OLA B1202 SITE 1 AC9 2 ALA B 10 VAL B 17 CRYST1 96.492 112.960 124.171 90.00 90.00 90.00 P 2 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.010364 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008853 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008053 0.00000 ATOM 1 N SER A 4 68.894 48.668 161.549 1.00 96.89 N ANISOU 1 N SER A 4 14529 11500 10785 577 -992 87 N ATOM 2 CA SER A 4 69.423 49.799 160.724 1.00 96.11 C ANISOU 2 CA SER A 4 14372 11400 10743 541 -948 35 C ATOM 3 C SER A 4 68.352 50.375 159.779 1.00 94.30 C ANISOU 3 C SER A 4 14159 11154 10516 511 -857 59 C ATOM 4 O SER A 4 68.614 50.614 158.596 1.00 94.66 O ANISOU 4 O SER A 4 14157 11191 10618 492 -812 45 O ATOM 5 CB SER A 4 70.675 49.345 159.947 1.00 96.80 C ANISOU 5 CB SER A 4 14380 11490 10909 553 -972 1 C ATOM 6 OG SER A 4 70.420 48.175 159.183 1.00 96.12 O ANISOU 6 OG SER A 4 14293 11387 10841 578 -960 36 O ATOM 7 N ILE A 5 67.147 50.593 160.316 1.00 92.50 N ANISOU 7 N ILE A 5 13997 10926 10222 508 -829 98 N ATOM 8 CA ILE A 5 66.043 51.231 159.579 1.00 90.40 C ANISOU 8 CA ILE A 5 13749 10647 9950 482 -746 124 C ATOM 9 C ILE A 5 65.687 52.561 160.264 1.00 89.01 C ANISOU 9 C ILE A 5 13602 10475 9740 465 -725 100 C ATOM 10 O ILE A 5 65.637 52.661 161.495 1.00 88.13 O ANISOU 10 O ILE A 5 13530 10379 9573 479 -764 92 O ATOM 11 CB ILE A 5 64.816 50.292 159.437 1.00 89.90 C ANISOU 11 CB ILE A 5 13731 10580 9845 495 -722 197 C ATOM 12 CG1 ILE A 5 65.165 49.130 158.494 1.00 90.31 C ANISOU 12 CG1 ILE A 5 13752 10618 9941 506 -732 212 C ATOM 13 CG2 ILE A 5 63.592 51.043 158.908 1.00 88.74 C ANISOU 13 CG2 ILE A 5 13606 10430 9681 471 -642 227 C ATOM 14 CD1 ILE A 5 64.157 47.996 158.469 1.00 90.30 C ANISOU 14 CD1 ILE A 5 13797 10609 9903 517 -729 280 C ATOM 15 N SER A 6 65.448 53.572 159.434 1.00 87.07 N ANISOU 15 N SER A 6 13338 10214 9528 435 -662 87 N ATOM 16 CA SER A 6 65.250 54.952 159.877 1.00 85.42 C ANISOU 16 CA SER A 6 13151 9997 9306 416 -638 55 C ATOM 17 C SER A 6 63.825 55.184 160.390 1.00 83.35 C ANISOU 17 C SER A 6 12954 9738 8975 430 -597 97 C ATOM 18 O SER A 6 62.853 54.666 159.823 1.00 83.25 O ANISOU 18 O SER A 6 12953 9728 8950 435 -554 154 O ATOM 19 CB SER A 6 65.553 55.908 158.714 1.00 85.60 C ANISOU 19 CB SER A 6 13129 9997 9396 379 -586 32 C ATOM 20 OG SER A 6 65.316 57.258 159.059 1.00 86.72 O ANISOU 20 OG SER A 6 13296 10121 9531 361 -561 2 O ATOM 21 N ALA A 7 63.705 55.981 161.454 1.00 81.22 N ANISOU 21 N ALA A 7 12725 9474 8661 435 -608 66 N ATOM 22 CA ALA A 7 62.403 56.336 162.051 1.00 79.61 C ANISOU 22 CA ALA A 7 12580 9278 8388 452 -567 96 C ATOM 23 C ALA A 7 61.428 56.948 161.035 1.00 77.12 C ANISOU 23 C ALA A 7 12261 8943 8096 440 -483 129 C ATOM 24 O ALA A 7 60.212 56.716 161.109 1.00 76.31 O ANISOU 24 O ALA A 7 12190 8856 7947 456 -443 183 O ATOM 25 CB ALA A 7 62.607 57.294 163.219 1.00 80.71 C ANISOU 25 CB ALA A 7 12758 9419 8487 456 -590 41 C ATOM 26 N PHE A 8 61.975 57.727 160.101 1.00 74.92 N ANISOU 26 N PHE A 8 11942 8635 7887 410 -459 99 N ATOM 27 CA PHE A 8 61.215 58.259 158.973 1.00 73.17 C ANISOU 27 CA PHE A 8 11709 8394 7697 395 -386 132 C ATOM 28 C PHE A 8 60.685 57.142 158.071 1.00 71.17 C ANISOU 28 C PHE A 8 11435 8156 7449 397 -366 197 C ATOM 29 O PHE A 8 59.519 57.160 157.675 1.00 69.73 O ANISOU 29 O PHE A 8 11268 7978 7246 402 -314 249 O ATOM 30 CB PHE A 8 62.078 59.229 158.136 1.00 73.47 C ANISOU 30 CB PHE A 8 11705 8399 7811 358 -373 89 C ATOM 31 CG PHE A 8 62.277 60.617 158.720 1.00 74.07 C ANISOU 31 CG PHE A 8 11806 8445 7890 348 -370 35 C ATOM 32 CD1 PHE A 8 61.668 61.063 159.903 1.00 74.58 C ANISOU 32 CD1 PHE A 8 11931 8513 7892 376 -373 20 C ATOM 33 CD2 PHE A 8 63.074 61.518 158.017 1.00 74.05 C ANISOU 33 CD2 PHE A 8 11767 8410 7957 308 -361 0 C ATOM 34 CE1 PHE A 8 61.885 62.347 160.366 1.00 75.25 C ANISOU 34 CE1 PHE A 8 12042 8564 7984 366 -370 -34 C ATOM 35 CE2 PHE A 8 63.290 62.808 158.480 1.00 74.41 C ANISOU 35 CE2 PHE A 8 11837 8419 8013 293 -360 -51 C ATOM 36 CZ PHE A 8 62.695 63.223 159.656 1.00 75.09 C ANISOU 36 CZ PHE A 8 11987 8503 8037 323 -366 -70 C ATOM 37 N GLN A 9 61.540 56.178 157.752 1.00 70.48 N ANISOU 37 N GLN A 9 11313 8075 7390 393 -409 191 N ATOM 38 CA GLN A 9 61.151 55.009 156.953 1.00 69.72 C ANISOU 38 CA GLN A 9 11202 7988 7298 395 -399 243 C ATOM 39 C GLN A 9 60.074 54.186 157.663 1.00 68.54 C ANISOU 39 C GLN A 9 11100 7861 7079 419 -404 300 C ATOM 40 O GLN A 9 59.071 53.776 157.047 1.00 68.68 O ANISOU 40 O GLN A 9 11125 7886 7085 415 -364 357 O ATOM 41 CB GLN A 9 62.368 54.131 156.632 1.00 70.40 C ANISOU 41 CB GLN A 9 11246 8076 7426 394 -450 217 C ATOM 42 CG GLN A 9 62.156 53.221 155.432 1.00 70.50 C ANISOU 42 CG GLN A 9 11233 8086 7464 388 -429 254 C ATOM 43 CD GLN A 9 63.340 52.314 155.146 1.00 71.34 C ANISOU 43 CD GLN A 9 11299 8194 7612 396 -477 225 C ATOM 44 OE1 GLN A 9 64.425 52.474 155.712 1.00 72.41 O ANISOU 44 OE1 GLN A 9 11412 8331 7766 403 -525 175 O ATOM 45 NE2 GLN A 9 63.133 51.350 154.251 1.00 71.41 N ANISOU 45 NE2 GLN A 9 11297 8200 7634 398 -467 254 N ATOM 46 N ALA A 10 60.285 53.960 158.958 1.00 67.10 N ANISOU 46 N ALA A 10 10950 7694 6849 441 -453 285 N ATOM 47 CA ALA A 10 59.281 53.332 159.814 1.00 66.08 C ANISOU 47 CA ALA A 10 10870 7591 6646 462 -457 337 C ATOM 48 C ALA A 10 57.961 54.107 159.825 1.00 65.01 C ANISOU 48 C ALA A 10 10760 7465 6475 464 -389 370 C ATOM 49 O ALA A 10 56.892 53.501 159.787 1.00 64.12 O ANISOU 49 O ALA A 10 10665 7372 6324 468 -365 434 O ATOM 50 CB ALA A 10 59.812 53.181 161.232 1.00 66.85 C ANISOU 50 CB ALA A 10 10998 7705 6695 483 -519 308 C ATOM 51 N ALA A 11 58.045 55.438 159.875 1.00 64.86 N ANISOU 51 N ALA A 11 10742 7431 6470 461 -359 327 N ATOM 52 CA ALA A 11 56.852 56.296 159.802 1.00 64.26 C ANISOU 52 CA ALA A 11 10686 7358 6370 469 -291 353 C ATOM 53 C ALA A 11 56.128 56.185 158.452 1.00 62.67 C ANISOU 53 C ALA A 11 10455 7151 6203 451 -238 406 C ATOM 54 O ALA A 11 54.900 56.055 158.411 1.00 62.12 O ANISOU 54 O ALA A 11 10399 7104 6098 460 -197 464 O ATOM 55 CB ALA A 11 57.217 57.744 160.089 1.00 64.86 C ANISOU 55 CB ALA A 11 10771 7407 6463 469 -277 290 C ATOM 56 N TYR A 12 56.893 56.241 157.362 1.00 61.49 N ANISOU 56 N TYR A 12 10264 6977 6123 424 -238 386 N ATOM 57 CA TYR A 12 56.355 56.009 156.016 1.00 60.86 C ANISOU 57 CA TYR A 12 10154 6894 6075 403 -196 433 C ATOM 58 C TYR A 12 55.641 54.657 155.939 1.00 60.47 C ANISOU 58 C TYR A 12 10112 6871 5990 405 -205 497 C ATOM 59 O TYR A 12 54.446 54.589 155.582 1.00 60.50 O ANISOU 59 O TYR A 12 10122 6892 5971 404 -163 556 O ATOM 60 CB TYR A 12 57.468 56.093 154.954 1.00 60.65 C ANISOU 60 CB TYR A 12 10080 6844 6120 375 -204 398 C ATOM 61 CG TYR A 12 57.074 55.529 153.605 1.00 60.24 C ANISOU 61 CG TYR A 12 10000 6796 6092 353 -174 443 C ATOM 62 CD1 TYR A 12 56.199 56.220 152.768 1.00 59.92 C ANISOU 62 CD1 TYR A 12 9951 6753 6060 341 -114 480 C ATOM 63 CD2 TYR A 12 57.565 54.292 153.170 1.00 60.17 C ANISOU 63 CD2 TYR A 12 9973 6791 6096 347 -208 448 C ATOM 64 CE1 TYR A 12 55.826 55.700 151.535 1.00 59.55 C ANISOU 64 CE1 TYR A 12 9879 6714 6030 319 -89 521 C ATOM 65 CE2 TYR A 12 57.195 53.766 151.939 1.00 59.52 C ANISOU 65 CE2 TYR A 12 9869 6713 6031 327 -182 484 C ATOM 66 CZ TYR A 12 56.332 54.471 151.127 1.00 59.23 C ANISOU 66 CZ TYR A 12 9825 6680 5999 311 -123 520 C ATOM 67 OH TYR A 12 55.965 53.946 149.915 1.00 58.85 O ANISOU 67 OH TYR A 12 9757 6639 5963 288 -101 556 O ATOM 68 N ILE A 13 56.374 53.600 156.305 1.00 60.14 N ANISOU 68 N ILE A 13 10073 6832 5946 409 -264 485 N ATOM 69 CA ILE A 13 55.836 52.228 156.303 1.00 59.76 C ANISOU 69 CA ILE A 13 10038 6798 5867 409 -285 541 C ATOM 70 C ILE A 13 54.570 52.120 157.168 1.00 60.04 C ANISOU 70 C ILE A 13 10112 6866 5831 423 -266 596 C ATOM 71 O ILE A 13 53.575 51.521 156.743 1.00 59.72 O ANISOU 71 O ILE A 13 10075 6843 5773 411 -243 660 O ATOM 72 CB ILE A 13 56.902 51.197 156.757 1.00 59.79 C ANISOU 72 CB ILE A 13 10043 6793 5879 419 -357 515 C ATOM 73 CG1 ILE A 13 58.015 51.083 155.703 1.00 59.60 C ANISOU 73 CG1 ILE A 13 9973 6745 5927 405 -368 472 C ATOM 74 CG2 ILE A 13 56.284 49.816 157.001 1.00 59.50 C ANISOU 74 CG2 ILE A 13 10034 6768 5806 421 -383 576 C ATOM 75 CD1 ILE A 13 59.325 50.560 156.254 1.00 59.91 C ANISOU 75 CD1 ILE A 13 10002 6775 5984 422 -437 424 C ATOM 76 N GLY A 14 54.613 52.720 158.361 1.00 60.53 N ANISOU 76 N GLY A 14 10203 6942 5854 446 -275 570 N ATOM 77 CA GLY A 14 53.479 52.734 159.286 1.00 60.77 C ANISOU 77 CA GLY A 14 10268 7010 5810 464 -253 615 C ATOM 78 C GLY A 14 52.258 53.465 158.755 1.00 60.67 C ANISOU 78 C GLY A 14 10246 7012 5791 463 -180 654 C ATOM 79 O GLY A 14 51.134 52.959 158.844 1.00 60.53 O ANISOU 79 O GLY A 14 10237 7028 5732 462 -157 722 O ATOM 80 N ILE A 15 52.482 54.656 158.201 1.00 60.80 N ANISOU 80 N ILE A 15 10246 7004 5852 463 -145 615 N ATOM 81 CA ILE A 15 51.402 55.450 157.600 1.00 60.76 C ANISOU 81 CA ILE A 15 10229 7007 5851 466 -77 651 C ATOM 82 C ILE A 15 50.805 54.716 156.394 1.00 60.27 C ANISOU 82 C ILE A 15 10137 6952 5810 436 -59 713 C ATOM 83 O ILE A 15 49.571 54.631 156.264 1.00 60.26 O ANISOU 83 O ILE A 15 10132 6983 5779 438 -20 777 O ATOM 84 CB ILE A 15 51.885 56.877 157.236 1.00 61.01 C ANISOU 84 CB ILE A 15 10250 6999 5930 470 -50 594 C ATOM 85 CG1 ILE A 15 52.157 57.673 158.524 1.00 61.54 C ANISOU 85 CG1 ILE A 15 10355 7064 5962 501 -60 539 C ATOM 86 CG2 ILE A 15 50.864 57.620 156.374 1.00 60.95 C ANISOU 86 CG2 ILE A 15 10225 6994 5940 470 15 637 C ATOM 87 CD1 ILE A 15 53.092 58.850 158.346 1.00 61.90 C ANISOU 87 CD1 ILE A 15 10397 7061 6061 495 -62 466 C ATOM 88 N GLU A 16 51.673 54.177 155.535 1.00 60.02 N ANISOU 88 N GLU A 16 10081 6894 5828 410 -88 695 N ATOM 89 CA GLU A 16 51.222 53.354 154.394 1.00 59.55 C ANISOU 89 CA GLU A 16 9999 6840 5786 380 -79 746 C ATOM 90 C GLU A 16 50.386 52.155 154.846 1.00 58.91 C ANISOU 90 C GLU A 16 9938 6791 5654 375 -96 810 C ATOM 91 O GLU A 16 49.259 51.941 154.355 1.00 58.47 O ANISOU 91 O GLU A 16 9873 6762 5582 360 -64 874 O ATOM 92 CB GLU A 16 52.417 52.868 153.569 1.00 59.87 C ANISOU 92 CB GLU A 16 10016 6848 5881 358 -113 706 C ATOM 93 CG GLU A 16 53.062 53.941 152.699 1.00 60.13 C ANISOU 93 CG GLU A 16 10019 6856 5971 348 -85 663 C ATOM 94 CD GLU A 16 52.379 54.121 151.352 1.00 60.27 C ANISOU 94 CD GLU A 16 10009 6879 6010 322 -40 706 C ATOM 95 OE1 GLU A 16 51.134 54.092 151.288 1.00 60.35 O ANISOU 95 OE1 GLU A 16 10025 6916 5988 322 -9 767 O ATOM 96 OE2 GLU A 16 53.097 54.296 150.344 1.00 60.85 O ANISOU 96 OE2 GLU A 16 10054 6934 6131 301 -34 680 O ATOM 97 N VAL A 17 50.942 51.400 155.797 1.00 58.77 N ANISOU 97 N VAL A 17 9947 6772 5611 385 -149 795 N ATOM 98 CA VAL A 17 50.252 50.257 156.408 1.00 58.94 C ANISOU 98 CA VAL A 17 9992 6820 5580 380 -173 855 C ATOM 99 C VAL A 17 48.903 50.663 157.012 1.00 59.35 C ANISOU 99 C VAL A 17 10055 6920 5574 391 -126 910 C ATOM 100 O VAL A 17 47.924 49.938 156.855 1.00 59.09 O ANISOU 100 O VAL A 17 10020 6915 5514 371 -117 980 O ATOM 101 CB VAL A 17 51.144 49.550 157.466 1.00 59.00 C ANISOU 101 CB VAL A 17 10030 6818 5567 396 -239 827 C ATOM 102 CG1 VAL A 17 50.342 48.600 158.352 1.00 59.31 C ANISOU 102 CG1 VAL A 17 10103 6890 5542 393 -257 893 C ATOM 103 CG2 VAL A 17 52.270 48.785 156.785 1.00 58.91 C ANISOU 103 CG2 VAL A 17 10006 6765 5611 384 -287 792 C ATOM 104 N LEU A 18 48.855 51.815 157.685 1.00 60.04 N ANISOU 104 N LEU A 18 10149 7017 5643 423 -98 876 N ATOM 105 CA LEU A 18 47.611 52.314 158.293 1.00 60.66 C ANISOU 105 CA LEU A 18 10235 7145 5668 444 -48 920 C ATOM 106 C LEU A 18 46.582 52.686 157.223 1.00 60.48 C ANISOU 106 C LEU A 18 10176 7136 5665 430 7 970 C ATOM 107 O LEU A 18 45.412 52.268 157.298 1.00 60.35 O ANISOU 107 O LEU A 18 10152 7166 5610 422 32 1042 O ATOM 108 CB LEU A 18 47.904 53.510 159.209 1.00 61.32 C ANISOU 108 CB LEU A 18 10338 7227 5731 485 -32 859 C ATOM 109 CG LEU A 18 46.843 53.939 160.234 1.00 61.98 C ANISOU 109 CG LEU A 18 10441 7365 5743 518 8 888 C ATOM 110 CD1 LEU A 18 47.529 54.646 161.398 1.00 62.48 C ANISOU 110 CD1 LEU A 18 10540 7420 5776 553 -7 815 C ATOM 111 CD2 LEU A 18 45.751 54.822 159.636 1.00 62.01 C ANISOU 111 CD2 LEU A 18 10417 7386 5757 532 80 920 C ATOM 112 N ILE A 19 47.029 53.451 156.223 1.00 60.92 N ANISOU 112 N ILE A 19 10208 7156 5782 425 26 935 N ATOM 113 CA ILE A 19 46.170 53.816 155.080 1.00 61.11 C ANISOU 113 CA ILE A 19 10196 7190 5830 409 73 981 C ATOM 114 C ILE A 19 45.611 52.564 154.396 1.00 60.92 C ANISOU 114 C ILE A 19 10159 7186 5801 367 57 1047 C ATOM 115 O ILE A 19 44.410 52.491 154.121 1.00 60.70 O ANISOU 115 O ILE A 19 10111 7199 5751 358 91 1115 O ATOM 116 CB ILE A 19 46.913 54.694 154.041 1.00 60.76 C ANISOU 116 CB ILE A 19 10131 7101 5854 402 86 934 C ATOM 117 CG1 ILE A 19 47.222 56.076 154.627 1.00 61.37 C ANISOU 117 CG1 ILE A 19 10221 7156 5938 441 110 879 C ATOM 118 CG2 ILE A 19 46.081 54.867 152.772 1.00 60.23 C ANISOU 118 CG2 ILE A 19 10028 7046 5810 380 125 989 C ATOM 119 CD1 ILE A 19 48.404 56.768 153.973 1.00 61.45 C ANISOU 119 CD1 ILE A 19 10222 7113 6012 429 100 815 C ATOM 120 N ALA A 20 46.485 51.592 154.130 1.00 61.10 N ANISOU 120 N ALA A 20 10190 7178 5845 342 5 1026 N ATOM 121 CA ALA A 20 46.046 50.305 153.576 1.00 61.01 C ANISOU 121 CA ALA A 20 10176 7176 5827 301 -18 1081 C ATOM 122 C ALA A 20 45.065 49.567 154.505 1.00 61.38 C ANISOU 122 C ALA A 20 10241 7269 5811 297 -23 1147 C ATOM 123 O ALA A 20 44.063 49.018 154.037 1.00 60.89 O ANISOU 123 O ALA A 20 10163 7235 5734 265 -11 1216 O ATOM 124 CB ALA A 20 47.242 49.426 153.267 1.00 60.90 C ANISOU 124 CB ALA A 20 10175 7117 5847 285 -75 1037 C ATOM 125 N LEU A 21 45.355 49.571 155.808 1.00 62.10 N ANISOU 125 N LEU A 21 10363 7368 5863 326 -41 1128 N ATOM 126 CA LEU A 21 44.482 48.947 156.819 1.00 62.98 C ANISOU 126 CA LEU A 21 10492 7528 5908 324 -44 1190 C ATOM 127 C LEU A 21 43.113 49.619 156.959 1.00 63.64 C ANISOU 127 C LEU A 21 10552 7672 5955 336 20 1245 C ATOM 128 O LEU A 21 42.149 48.956 157.345 1.00 63.90 O ANISOU 128 O LEU A 21 10584 7752 5943 317 25 1317 O ATOM 129 CB LEU A 21 45.156 48.892 158.203 1.00 63.28 C ANISOU 129 CB LEU A 21 10570 7565 5906 355 -77 1153 C ATOM 130 CG LEU A 21 46.158 47.763 158.464 1.00 63.40 C ANISOU 130 CG LEU A 21 10615 7542 5931 342 -150 1135 C ATOM 131 CD1 LEU A 21 46.900 48.016 159.772 1.00 63.56 C ANISOU 131 CD1 LEU A 21 10669 7564 5917 379 -179 1088 C ATOM 132 CD2 LEU A 21 45.482 46.397 158.472 1.00 63.44 C ANISOU 132 CD2 LEU A 21 10632 7560 5910 302 -177 1214 C ATOM 133 N VAL A 22 43.028 50.924 156.684 1.00 63.99 N ANISOU 133 N VAL A 22 10575 7715 6020 368 68 1213 N ATOM 134 CA VAL A 22 41.716 51.598 156.615 1.00 64.19 C ANISOU 134 CA VAL A 22 10570 7794 6022 383 131 1265 C ATOM 135 C VAL A 22 41.044 51.389 155.244 1.00 63.87 C ANISOU 135 C VAL A 22 10488 7760 6017 344 147 1318 C ATOM 136 O VAL A 22 39.824 51.226 155.170 1.00 63.89 O ANISOU 136 O VAL A 22 10464 7819 5992 333 177 1392 O ATOM 137 CB VAL A 22 41.821 53.105 156.955 1.00 64.55 C ANISOU 137 CB VAL A 22 10617 7834 6075 439 176 1212 C ATOM 138 CG1 VAL A 22 40.460 53.789 156.863 1.00 64.80 C ANISOU 138 CG1 VAL A 22 10614 7920 6086 463 242 1267 C ATOM 139 CG2 VAL A 22 42.391 53.296 158.359 1.00 64.95 C ANISOU 139 CG2 VAL A 22 10710 7885 6082 476 159 1161 C ATOM 140 N SER A 23 41.839 51.383 154.174 1.00 63.45 N ANISOU 140 N SER A 23 10430 7656 6022 322 127 1281 N ATOM 141 CA SER A 23 41.321 51.272 152.799 1.00 63.10 C ANISOU 141 CA SER A 23 10348 7615 6009 285 140 1322 C ATOM 142 C SER A 23 40.633 49.937 152.469 1.00 63.04 C ANISOU 142 C SER A 23 10335 7633 5982 231 113 1392 C ATOM 143 O SER A 23 39.483 49.929 152.026 1.00 63.36 O ANISOU 143 O SER A 23 10342 7721 6009 212 141 1460 O ATOM 144 CB SER A 23 42.452 51.522 151.791 1.00 62.88 C ANISOU 144 CB SER A 23 10319 7528 6043 274 122 1260 C ATOM 145 OG SER A 23 41.991 51.443 150.457 1.00 62.70 O ANISOU 145 OG SER A 23 10264 7512 6046 238 135 1296 O ATOM 146 N VAL A 24 41.336 48.825 152.686 1.00 62.62 N ANISOU 146 N VAL A 24 10315 7548 5928 206 57 1376 N ATOM 147 CA VAL A 24 40.875 47.498 152.231 1.00 62.13 C ANISOU 147 CA VAL A 24 10256 7492 5858 148 22 1431 C ATOM 148 C VAL A 24 39.537 47.070 152.865 1.00 62.86 C ANISOU 148 C VAL A 24 10338 7650 5896 130 38 1520 C ATOM 149 O VAL A 24 38.611 46.698 152.133 1.00 62.98 O ANISOU 149 O VAL A 24 10324 7695 5909 87 46 1582 O ATOM 150 CB VAL A 24 41.963 46.403 152.416 1.00 61.60 C ANISOU 150 CB VAL A 24 10232 7368 5805 133 -42 1392 C ATOM 151 CG1 VAL A 24 41.411 45.006 152.140 1.00 61.54 C ANISOU 151 CG1 VAL A 24 10236 7361 5783 75 -80 1453 C ATOM 152 CG2 VAL A 24 43.146 46.682 151.505 1.00 61.31 C ANISOU 152 CG2 VAL A 24 10193 7275 5825 139 -56 1316 C ATOM 153 N PRO A 25 39.424 47.130 154.213 1.00 63.61 N ANISOU 153 N PRO A 25 10453 7772 5944 160 43 1527 N ATOM 154 CA PRO A 25 38.156 46.718 154.830 1.00 63.98 C ANISOU 154 CA PRO A 25 10483 7888 5935 142 63 1614 C ATOM 155 C PRO A 25 36.957 47.587 154.431 1.00 64.15 C ANISOU 155 C PRO A 25 10450 7974 5950 153 126 1662 C ATOM 156 O PRO A 25 35.881 47.047 154.180 1.00 64.02 O ANISOU 156 O PRO A 25 10403 8006 5913 111 133 1742 O ATOM 157 CB PRO A 25 38.434 46.839 156.336 1.00 64.23 C ANISOU 157 CB PRO A 25 10549 7937 5917 183 62 1596 C ATOM 158 CG PRO A 25 39.916 46.834 156.461 1.00 64.01 C ANISOU 158 CG PRO A 25 10561 7837 5921 204 18 1509 C ATOM 159 CD PRO A 25 40.398 47.551 155.240 1.00 63.64 C ANISOU 159 CD PRO A 25 10491 7751 5938 209 32 1459 C ATOM 160 N GLY A 26 37.153 48.906 154.366 1.00 64.13 N ANISOU 160 N GLY A 26 10433 7967 5965 208 170 1614 N ATOM 161 CA GLY A 26 36.091 49.842 153.994 1.00 64.26 C ANISOU 161 CA GLY A 26 10397 8037 5981 231 231 1654 C ATOM 162 C GLY A 26 35.469 49.555 152.644 1.00 63.93 C ANISOU 162 C GLY A 26 10315 8006 5969 181 229 1705 C ATOM 163 O GLY A 26 34.246 49.471 152.521 1.00 63.37 O ANISOU 163 O GLY A 26 10199 8002 5874 164 255 1783 O ATOM 164 N ASN A 27 36.321 49.379 151.637 1.00 64.35 N ANISOU 164 N ASN A 27 10380 7998 6070 155 196 1661 N ATOM 165 CA ASN A 27 35.863 49.111 150.271 1.00 65.12 C ANISOU 165 CA ASN A 27 10445 8101 6194 106 190 1699 C ATOM 166 C ASN A 27 35.308 47.696 150.100 1.00 65.97 C ANISOU 166 C ASN A 27 10555 8227 6280 34 149 1762 C ATOM 167 O ASN A 27 34.322 47.501 149.373 1.00 66.49 O ANISOU 167 O ASN A 27 10581 8338 6342 -5 157 1827 O ATOM 168 CB ASN A 27 36.977 49.399 149.265 1.00 64.72 C ANISOU 168 CB ASN A 27 10409 7983 6196 103 173 1630 C ATOM 169 CG ASN A 27 37.277 50.884 149.144 1.00 64.70 C ANISOU 169 CG ASN A 27 10392 7967 6221 161 217 1587 C ATOM 170 OD1 ASN A 27 36.448 51.657 148.659 1.00 64.59 O ANISOU 170 OD1 ASN A 27 10337 7990 6212 175 258 1627 O ATOM 171 ND2 ASN A 27 38.462 51.291 149.586 1.00 64.65 N ANISOU 171 ND2 ASN A 27 10421 7908 6235 195 208 1507 N ATOM 172 N VAL A 28 35.913 46.717 150.779 1.00 67.11 N ANISOU 172 N VAL A 28 10748 8339 6411 17 103 1744 N ATOM 173 CA VAL A 28 35.320 45.370 150.866 1.00 67.96 C ANISOU 173 CA VAL A 28 10864 8462 6492 -48 64 1809 C ATOM 174 C VAL A 28 33.909 45.466 151.470 1.00 69.40 C ANISOU 174 C VAL A 28 11004 8735 6628 -54 102 1898 C ATOM 175 O VAL A 28 32.978 44.830 150.976 1.00 69.77 O ANISOU 175 O VAL A 28 11023 8820 6665 -114 93 1970 O ATOM 176 CB VAL A 28 36.202 44.383 151.677 1.00 67.72 C ANISOU 176 CB VAL A 28 10896 8381 6453 -56 10 1779 C ATOM 177 CG1 VAL A 28 35.453 43.085 151.984 1.00 68.21 C ANISOU 177 CG1 VAL A 28 10968 8464 6483 -121 -23 1857 C ATOM 178 CG2 VAL A 28 37.488 44.064 150.926 1.00 67.13 C ANISOU 178 CG2 VAL A 28 10855 8222 6427 -60 -31 1701 C ATOM 179 N LEU A 29 33.765 46.277 152.518 1.00 70.47 N ANISOU 179 N LEU A 29 11133 8906 6734 6 146 1891 N ATOM 180 CA LEU A 29 32.468 46.522 153.154 1.00 71.61 C ANISOU 180 CA LEU A 29 11233 9144 6832 14 192 1968 C ATOM 181 C LEU A 29 31.493 47.254 152.216 1.00 72.14 C ANISOU 181 C LEU A 29 11231 9261 6916 16 235 2012 C ATOM 182 O LEU A 29 30.294 46.956 152.220 1.00 73.56 O ANISOU 182 O LEU A 29 11363 9515 7068 -16 251 2097 O ATOM 183 CB LEU A 29 32.647 47.309 154.461 1.00 71.86 C ANISOU 183 CB LEU A 29 11279 9197 6828 89 231 1936 C ATOM 184 CG LEU A 29 31.521 47.217 155.486 1.00 72.74 C ANISOU 184 CG LEU A 29 11360 9401 6874 95 269 2010 C ATOM 185 CD1 LEU A 29 31.535 45.868 156.196 1.00 73.39 C ANISOU 185 CD1 LEU A 29 11479 9486 6918 39 222 2053 C ATOM 186 CD2 LEU A 29 31.632 48.353 156.496 1.00 72.88 C ANISOU 186 CD2 LEU A 29 11383 9442 6863 182 322 1965 C ATOM 187 N VAL A 30 32.003 48.201 151.422 1.00 71.55 N ANISOU 187 N VAL A 30 11150 9148 6885 51 251 1957 N ATOM 188 CA VAL A 30 31.197 48.853 150.373 1.00 71.74 C ANISOU 188 CA VAL A 30 11113 9210 6932 49 282 1997 C ATOM 189 C VAL A 30 30.710 47.840 149.334 1.00 72.04 C ANISOU 189 C VAL A 30 11133 9258 6977 -37 240 2052 C ATOM 190 O VAL A 30 29.525 47.844 148.978 1.00 71.91 O ANISOU 190 O VAL A 30 11059 9314 6949 -62 259 2131 O ATOM 191 CB VAL A 30 31.965 50.007 149.671 1.00 71.44 C ANISOU 191 CB VAL A 30 11081 9119 6942 97 300 1927 C ATOM 192 CG1 VAL A 30 31.260 50.472 148.401 1.00 71.39 C ANISOU 192 CG1 VAL A 30 11020 9141 6962 81 317 1971 C ATOM 193 CG2 VAL A 30 32.131 51.188 150.616 1.00 71.85 C ANISOU 193 CG2 VAL A 30 11139 9174 6987 184 350 1886 C ATOM 194 N ILE A 31 31.617 46.986 148.853 1.00 72.68 N ANISOU 194 N ILE A 31 11264 9270 7081 -82 184 2010 N ATOM 195 CA ILE A 31 31.261 45.957 147.855 1.00 73.04 C ANISOU 195 CA ILE A 31 11304 9314 7133 -167 139 2050 C ATOM 196 C ILE A 31 30.265 44.948 148.446 1.00 74.30 C ANISOU 196 C ILE A 31 11450 9528 7251 -224 123 2135 C ATOM 197 O ILE A 31 29.315 44.541 147.770 1.00 75.19 O ANISOU 197 O ILE A 31 11522 9687 7358 -283 113 2204 O ATOM 198 CB ILE A 31 32.506 45.217 147.300 1.00 72.30 C ANISOU 198 CB ILE A 31 11271 9129 7069 -196 83 1979 C ATOM 199 CG1 ILE A 31 33.408 46.183 146.528 1.00 71.69 C ANISOU 199 CG1 ILE A 31 11197 9006 7034 -153 100 1904 C ATOM 200 CG2 ILE A 31 32.100 44.073 146.371 1.00 72.55 C ANISOU 200 CG2 ILE A 31 11305 9156 7102 -284 34 2017 C ATOM 201 CD1 ILE A 31 34.843 45.722 146.408 1.00 71.32 C ANISOU 201 CD1 ILE A 31 11210 8874 7015 -151 60 1818 C ATOM 202 N TRP A 32 30.500 44.559 149.701 1.00 74.87 N ANISOU 202 N TRP A 32 11556 9596 7293 -208 118 2133 N ATOM 203 CA TRP A 32 29.569 43.725 150.484 1.00 75.64 C ANISOU 203 CA TRP A 32 11641 9753 7346 -254 111 2217 C ATOM 204 C TRP A 32 28.184 44.375 150.543 1.00 75.64 C ANISOU 204 C TRP A 32 11559 9859 7322 -243 168 2297 C ATOM 205 O TRP A 32 27.183 43.757 150.168 1.00 75.79 O ANISOU 205 O TRP A 32 11537 9931 7328 -311 155 2378 O ATOM 206 CB TRP A 32 30.115 43.540 151.909 1.00 76.34 C ANISOU 206 CB TRP A 32 11776 9826 7402 -217 111 2194 C ATOM 207 CG TRP A 32 29.596 42.375 152.691 1.00 77.67 C ANISOU 207 CG TRP A 32 11959 10021 7529 -276 82 2265 C ATOM 208 CD1 TRP A 32 28.319 41.885 152.724 1.00 78.75 C ANISOU 208 CD1 TRP A 32 12048 10236 7637 -335 90 2365 C ATOM 209 CD2 TRP A 32 30.355 41.577 153.605 1.00 78.23 C ANISOU 209 CD2 TRP A 32 12098 10042 7582 -281 41 2244 C ATOM 210 NE1 TRP A 32 28.246 40.813 153.587 1.00 79.50 N ANISOU 210 NE1 TRP A 32 12179 10329 7698 -381 56 2409 N ATOM 211 CE2 TRP A 32 29.482 40.604 154.139 1.00 79.00 C ANISOU 211 CE2 TRP A 32 12189 10186 7640 -347 25 2337 C ATOM 212 CE3 TRP A 32 31.696 41.583 154.015 1.00 77.86 C ANISOU 212 CE3 TRP A 32 12115 9916 7550 -238 14 2159 C ATOM 213 CZ2 TRP A 32 29.909 39.644 155.059 1.00 79.34 C ANISOU 213 CZ2 TRP A 32 12291 10196 7658 -370 -17 2349 C ATOM 214 CZ3 TRP A 32 32.120 40.627 154.929 1.00 77.95 C ANISOU 214 CZ3 TRP A 32 12183 9897 7537 -257 -29 2169 C ATOM 215 CH2 TRP A 32 31.227 39.673 155.444 1.00 78.93 C ANISOU 215 CH2 TRP A 32 12302 10065 7620 -322 -44 2265 C ATOM 216 N ALA A 33 28.153 45.632 150.989 1.00 75.72 N ANISOU 216 N ALA A 33 11544 9897 7328 -157 228 2271 N ATOM 217 CA ALA A 33 26.906 46.382 151.191 1.00 76.48 C ANISOU 217 CA ALA A 33 11563 10094 7401 -126 289 2338 C ATOM 218 C ALA A 33 25.990 46.426 149.970 1.00 76.80 C ANISOU 218 C ALA A 33 11537 10179 7461 -171 288 2399 C ATOM 219 O ALA A 33 24.773 46.334 150.110 1.00 77.53 O ANISOU 219 O ALA A 33 11565 10365 7529 -192 311 2485 O ATOM 220 CB ALA A 33 27.214 47.801 151.657 1.00 76.45 C ANISOU 220 CB ALA A 33 11554 10089 7402 -21 348 2281 C ATOM 221 N VAL A 34 26.574 46.567 148.782 1.00 76.66 N ANISOU 221 N VAL A 34 11535 10103 7489 -186 261 2355 N ATOM 222 CA VAL A 34 25.793 46.600 147.540 1.00 76.84 C ANISOU 222 CA VAL A 34 11501 10164 7528 -231 253 2408 C ATOM 223 C VAL A 34 25.261 45.209 147.186 1.00 77.44 C ANISOU 223 C VAL A 34 11576 10258 7590 -340 196 2470 C ATOM 224 O VAL A 34 24.127 45.090 146.722 1.00 77.23 O ANISOU 224 O VAL A 34 11483 10307 7553 -383 199 2551 O ATOM 225 CB VAL A 34 26.608 47.188 146.363 1.00 76.12 C ANISOU 225 CB VAL A 34 11430 10008 7484 -215 241 2342 C ATOM 226 CG1 VAL A 34 25.835 47.106 145.047 1.00 76.23 C ANISOU 226 CG1 VAL A 34 11392 10063 7509 -270 225 2398 C ATOM 227 CG2 VAL A 34 26.987 48.635 146.654 1.00 75.96 C ANISOU 227 CG2 VAL A 34 11404 9975 7481 -113 298 2293 C ATOM 228 N LYS A 35 26.067 44.169 147.406 1.00 78.68 N ANISOU 228 N LYS A 35 11805 10341 7746 -384 144 2432 N ATOM 229 CA LYS A 35 25.675 42.803 147.045 1.00 80.41 C ANISOU 229 CA LYS A 35 12037 10558 7957 -489 84 2482 C ATOM 230 C LYS A 35 24.480 42.307 147.863 1.00 81.95 C ANISOU 230 C LYS A 35 12186 10842 8110 -530 96 2583 C ATOM 231 O LYS A 35 23.544 41.727 147.306 1.00 82.50 O ANISOU 231 O LYS A 35 12212 10961 8172 -609 73 2656 O ATOM 232 CB LYS A 35 26.851 41.831 147.194 1.00 80.73 C ANISOU 232 CB LYS A 35 12169 10494 8009 -516 26 2417 C ATOM 233 CG LYS A 35 26.510 40.407 146.774 1.00 82.24 C ANISOU 233 CG LYS A 35 12384 10667 8196 -624 -39 2460 C ATOM 234 CD LYS A 35 27.729 39.512 146.674 1.00 82.96 C ANISOU 234 CD LYS A 35 12566 10645 8309 -643 -97 2387 C ATOM 235 CE LYS A 35 27.305 38.055 146.527 1.00 84.19 C ANISOU 235 CE LYS A 35 12751 10781 8456 -748 -162 2437 C ATOM 236 NZ LYS A 35 28.431 37.163 146.131 1.00 84.54 N ANISOU 236 NZ LYS A 35 12880 10711 8528 -769 -223 2363 N ATOM 237 N VAL A 36 24.528 42.525 149.177 1.00 82.95 N ANISOU 237 N VAL A 36 12320 10991 8205 -478 132 2585 N ATOM 238 CA VAL A 36 23.451 42.095 150.081 1.00 83.74 C ANISOU 238 CA VAL A 36 12376 11182 8259 -511 151 2680 C ATOM 239 C VAL A 36 22.163 42.923 149.938 1.00 84.50 C ANISOU 239 C VAL A 36 12367 11395 8342 -487 210 2752 C ATOM 240 O VAL A 36 21.071 42.361 149.935 1.00 85.61 O ANISOU 240 O VAL A 36 12451 11614 8461 -555 204 2846 O ATOM 241 CB VAL A 36 23.923 42.047 151.563 1.00 84.11 C ANISOU 241 CB VAL A 36 12467 11221 8270 -463 171 2659 C ATOM 242 CG1 VAL A 36 24.163 43.441 152.141 1.00 83.87 C ANISOU 242 CG1 VAL A 36 12420 11211 8232 -346 241 2609 C ATOM 243 CG2 VAL A 36 22.927 41.273 152.423 1.00 85.56 C ANISOU 243 CG2 VAL A 36 12619 11484 8403 -521 175 2761 C ATOM 244 N ASN A 37 22.296 44.241 149.797 1.00 85.18 N ANISOU 244 N ASN A 37 12426 11492 8444 -392 263 2710 N ATOM 245 CA ASN A 37 21.151 45.161 149.793 1.00 86.56 C ANISOU 245 CA ASN A 37 12504 11774 8609 -347 326 2771 C ATOM 246 C ASN A 37 20.574 45.339 148.382 1.00 88.30 C ANISOU 246 C ASN A 37 12668 12020 8862 -386 308 2806 C ATOM 247 O ASN A 37 21.261 45.828 147.485 1.00 88.09 O ANISOU 247 O ASN A 37 12668 11928 8873 -363 294 2745 O ATOM 248 CB ASN A 37 21.583 46.521 150.363 1.00 85.71 C ANISOU 248 CB ASN A 37 12401 11659 8506 -222 391 2707 C ATOM 249 CG ASN A 37 20.411 47.397 150.784 1.00 85.81 C ANISOU 249 CG ASN A 37 12322 11786 8497 -161 464 2768 C ATOM 250 OD1 ASN A 37 19.251 47.105 150.490 1.00 86.10 O ANISOU 250 OD1 ASN A 37 12279 11913 8522 -208 468 2861 O ATOM 251 ND2 ASN A 37 20.715 48.488 151.479 1.00 85.41 N ANISOU 251 ND2 ASN A 37 12279 11729 8441 -53 522 2715 N ATOM 252 N GLN A 38 19.314 44.948 148.199 1.00 91.23 N ANISOU 252 N GLN A 38 12959 12488 9214 -445 307 2908 N ATOM 253 CA GLN A 38 18.617 45.123 146.913 1.00 93.11 C ANISOU 253 CA GLN A 38 13134 12767 9476 -484 290 2953 C ATOM 254 C GLN A 38 18.214 46.579 146.632 1.00 94.17 C ANISOU 254 C GLN A 38 13202 12950 9628 -384 352 2955 C ATOM 255 O GLN A 38 18.030 46.950 145.470 1.00 95.25 O ANISOU 255 O GLN A 38 13307 13089 9792 -394 336 2964 O ATOM 256 CB GLN A 38 17.387 44.214 146.819 1.00 94.96 C ANISOU 256 CB GLN A 38 13300 13094 9686 -586 265 3064 C ATOM 257 CG GLN A 38 17.732 42.745 146.603 1.00 95.88 C ANISOU 257 CG GLN A 38 13482 13148 9798 -704 185 3066 C ATOM 258 CD GLN A 38 16.508 41.853 146.470 1.00 97.54 C ANISOU 258 CD GLN A 38 13625 13445 9987 -813 156 3177 C ATOM 259 OE1 GLN A 38 15.466 42.274 145.964 1.00 98.44 O ANISOU 259 OE1 GLN A 38 13643 13657 10102 -821 174 3246 O ATOM 260 NE2 GLN A 38 16.634 40.602 146.917 1.00 98.12 N ANISOU 260 NE2 GLN A 38 13751 13485 10044 -901 108 3196 N ATOM 261 N ALA A 39 18.082 47.397 147.678 1.00 95.65 N ANISOU 261 N ALA A 39 13370 13174 9799 -288 421 2946 N ATOM 262 CA ALA A 39 17.823 48.842 147.530 1.00 96.75 C ANISOU 262 CA ALA A 39 13460 13341 9958 -178 482 2935 C ATOM 263 C ALA A 39 18.978 49.606 146.867 1.00 97.53 C ANISOU 263 C ALA A 39 13623 13332 10100 -126 474 2839 C ATOM 264 O ALA A 39 18.773 50.708 146.353 1.00 98.32 O ANISOU 264 O ALA A 39 13684 13442 10227 -58 507 2837 O ATOM 265 CB ALA A 39 17.499 49.467 148.879 1.00 97.14 C ANISOU 265 CB ALA A 39 13487 13446 9976 -88 556 2937 C ATOM 266 N LEU A 40 20.179 49.024 146.894 1.00 98.16 N ANISOU 266 N LEU A 40 13798 13310 10188 -158 431 2763 N ATOM 267 CA LEU A 40 21.348 49.552 146.184 1.00 97.57 C ANISOU 267 CA LEU A 40 13786 13132 10154 -128 415 2673 C ATOM 268 C LEU A 40 21.625 48.811 144.860 1.00 97.63 C ANISOU 268 C LEU A 40 13813 13099 10181 -220 347 2672 C ATOM 269 O LEU A 40 22.785 48.688 144.456 1.00 96.77 O ANISOU 269 O LEU A 40 13776 12895 10094 -227 316 2593 O ATOM 270 CB LEU A 40 22.584 49.450 147.092 1.00 97.03 C ANISOU 270 CB LEU A 40 13808 12977 10081 -95 413 2582 C ATOM 271 CG LEU A 40 22.461 50.002 148.513 1.00 97.17 C ANISOU 271 CG LEU A 40 13824 13025 10068 -13 471 2570 C ATOM 272 CD1 LEU A 40 23.701 49.672 149.327 1.00 96.46 C ANISOU 272 CD1 LEU A 40 13826 12851 9970 -1 453 2486 C ATOM 273 CD2 LEU A 40 22.229 51.500 148.475 1.00 97.37 C ANISOU 273 CD2 LEU A 40 13812 13067 10115 90 534 2555 C ATOM 274 N ARG A 41 20.579 48.332 144.179 1.00 98.51 N ANISOU 274 N ARG A 41 13860 13285 10284 -290 323 2758 N ATOM 275 CA ARG A 41 20.739 47.597 142.918 1.00 98.96 C ANISOU 275 CA ARG A 41 13935 13313 10353 -382 258 2759 C ATOM 276 C ARG A 41 20.470 48.529 141.734 1.00 98.26 C ANISOU 276 C ARG A 41 13799 13244 10290 -356 267 2774 C ATOM 277 O ARG A 41 19.635 48.256 140.868 1.00 99.58 O ANISOU 277 O ARG A 41 13911 13471 10452 -417 239 2841 O ATOM 278 CB ARG A 41 19.825 46.360 142.903 1.00100.87 C ANISOU 278 CB ARG A 41 14144 13615 10566 -490 215 2841 C ATOM 279 CG ARG A 41 20.201 45.300 141.869 1.00102.18 C ANISOU 279 CG ARG A 41 14357 13728 10738 -594 138 2823 C ATOM 280 CD ARG A 41 19.915 43.873 142.346 1.00103.33 C ANISOU 280 CD ARG A 41 14525 13876 10858 -692 91 2860 C ATOM 281 NE ARG A 41 20.785 43.485 143.461 1.00103.85 N ANISOU 281 NE ARG A 41 14666 13873 10917 -665 95 2805 N ATOM 282 CZ ARG A 41 20.681 42.353 144.161 1.00106.17 C ANISOU 282 CZ ARG A 41 14990 14159 11189 -731 63 2832 C ATOM 283 NH1 ARG A 41 19.739 41.450 143.879 1.00107.42 N ANISOU 283 NH1 ARG A 41 15112 14369 11330 -833 24 2913 N ATOM 284 NH2 ARG A 41 21.530 42.117 145.160 1.00106.56 N ANISOU 284 NH2 ARG A 41 15108 14146 11232 -696 68 2780 N ATOM 285 N ASP A 42 21.225 49.626 141.708 1.00 96.24 N ANISOU 285 N ASP A 42 13570 12933 10061 -268 303 2709 N ATOM 286 CA ASP A 42 21.027 50.729 140.774 1.00 94.34 C ANISOU 286 CA ASP A 42 13289 12706 9847 -222 323 2722 C ATOM 287 C ASP A 42 22.348 51.032 140.068 1.00 91.65 C ANISOU 287 C ASP A 42 13022 12263 9536 -212 306 2631 C ATOM 288 O ASP A 42 23.430 50.691 140.569 1.00 92.32 O ANISOU 288 O ASP A 42 13183 12269 9625 -208 296 2552 O ATOM 289 CB ASP A 42 20.533 51.962 141.544 1.00 95.34 C ANISOU 289 CB ASP A 42 13368 12874 9982 -111 396 2740 C ATOM 290 CG ASP A 42 19.619 52.850 140.726 1.00 96.91 C ANISOU 290 CG ASP A 42 13484 13138 10196 -78 415 2808 C ATOM 291 OD1 ASP A 42 19.897 53.071 139.529 1.00 97.72 O ANISOU 291 OD1 ASP A 42 13594 13215 10319 -103 387 2802 O ATOM 292 OD2 ASP A 42 18.620 53.337 141.295 1.00 98.14 O ANISOU 292 OD2 ASP A 42 13567 13376 10345 -26 460 2869 O ATOM 293 N ALA A 43 22.247 51.677 138.906 1.00 88.80 N ANISOU 293 N ALA A 43 12636 11908 9194 -208 302 2647 N ATOM 294 CA ALA A 43 23.407 51.967 138.054 1.00 85.77 C ANISOU 294 CA ALA A 43 12312 11441 8835 -209 285 2573 C ATOM 295 C ALA A 43 24.520 52.683 138.814 1.00 82.88 C ANISOU 295 C ALA A 43 12004 10992 8493 -129 322 2486 C ATOM 296 O ALA A 43 25.678 52.273 138.735 1.00 82.01 O ANISOU 296 O ALA A 43 11964 10804 8391 -150 298 2408 O ATOM 297 CB ALA A 43 22.984 52.785 136.843 1.00 86.24 C ANISOU 297 CB ALA A 43 12324 11532 8908 -199 288 2617 C ATOM 298 N THR A 44 24.157 53.728 139.560 1.00 80.59 N ANISOU 298 N THR A 44 11684 10721 8214 -39 378 2499 N ATOM 299 CA THR A 44 25.108 54.504 140.369 1.00 78.68 C ANISOU 299 CA THR A 44 11493 10406 7994 39 414 2419 C ATOM 300 C THR A 44 25.954 53.607 141.272 1.00 77.75 C ANISOU 300 C THR A 44 11442 10238 7861 15 393 2353 C ATOM 301 O THR A 44 27.178 53.744 141.320 1.00 76.58 O ANISOU 301 O THR A 44 11357 10007 7732 28 386 2270 O ATOM 302 CB THR A 44 24.383 55.558 141.242 1.00 78.54 C ANISOU 302 CB THR A 44 11432 10429 7981 135 476 2448 C ATOM 303 OG1 THR A 44 23.664 56.471 140.404 1.00 78.57 O ANISOU 303 OG1 THR A 44 11376 10471 8005 167 495 2506 O ATOM 304 CG2 THR A 44 25.373 56.347 142.103 1.00 78.14 C ANISOU 304 CG2 THR A 44 11439 10299 7949 212 510 2360 C ATOM 305 N PHE A 45 25.295 52.681 141.964 1.00 78.14 N ANISOU 305 N PHE A 45 11475 10340 7875 -21 382 2396 N ATOM 306 CA PHE A 45 25.967 51.807 142.924 1.00 77.72 C ANISOU 306 CA PHE A 45 11480 10247 7803 -41 362 2347 C ATOM 307 C PHE A 45 26.855 50.781 142.226 1.00 76.58 C ANISOU 307 C PHE A 45 11393 10040 7664 -118 301 2302 C ATOM 308 O PHE A 45 27.981 50.538 142.674 1.00 76.71 O ANISOU 308 O PHE A 45 11474 9983 7688 -108 287 2224 O ATOM 309 CB PHE A 45 24.954 51.141 143.855 1.00 79.00 C ANISOU 309 CB PHE A 45 11605 10485 7923 -60 369 2415 C ATOM 310 CG PHE A 45 24.108 52.125 144.611 1.00 80.35 C ANISOU 310 CG PHE A 45 11720 10721 8086 21 434 2453 C ATOM 311 CD1 PHE A 45 24.684 52.976 145.547 1.00 80.65 C ANISOU 311 CD1 PHE A 45 11792 10721 8130 110 477 2391 C ATOM 312 CD2 PHE A 45 22.745 52.232 144.362 1.00 81.89 C ANISOU 312 CD2 PHE A 45 11829 11016 8269 14 452 2549 C ATOM 313 CE1 PHE A 45 23.914 53.901 146.237 1.00 81.73 C ANISOU 313 CE1 PHE A 45 11880 10913 8257 192 538 2420 C ATOM 314 CE2 PHE A 45 21.966 53.153 145.052 1.00 82.88 C ANISOU 314 CE2 PHE A 45 11900 11203 8388 98 515 2582 C ATOM 315 CZ PHE A 45 22.552 53.990 145.991 1.00 82.69 C ANISOU 315 CZ PHE A 45 11914 11136 8367 189 559 2516 C ATOM 316 N CYS A 46 26.380 50.232 141.106 1.00 75.54 N ANISOU 316 N CYS A 46 11235 9936 7528 -190 265 2346 N ATOM 317 CA CYS A 46 27.199 49.341 140.265 1.00 74.32 C ANISOU 317 CA CYS A 46 11134 9724 7379 -260 209 2299 C ATOM 318 C CYS A 46 28.541 49.958 139.829 1.00 72.24 C ANISOU 318 C CYS A 46 10920 9377 7149 -222 215 2208 C ATOM 319 O CYS A 46 29.532 49.241 139.676 1.00 70.44 O ANISOU 319 O CYS A 46 10751 9085 6926 -253 180 2144 O ATOM 320 CB CYS A 46 26.406 48.886 139.038 1.00 75.28 C ANISOU 320 CB CYS A 46 11216 9895 7489 -335 175 2360 C ATOM 321 SG CYS A 46 24.877 48.015 139.456 1.00 77.55 S ANISOU 321 SG CYS A 46 11443 10280 7740 -398 159 2468 S ATOM 322 N PHE A 47 28.568 51.279 139.642 1.00 71.38 N ANISOU 322 N PHE A 47 10787 9270 7063 -156 259 2205 N ATOM 323 CA PHE A 47 29.821 52.006 139.406 1.00 70.63 C ANISOU 323 CA PHE A 47 10734 9098 7001 -114 272 2123 C ATOM 324 C PHE A 47 30.604 52.220 140.707 1.00 70.14 C ANISOU 324 C PHE A 47 10716 8986 6946 -58 291 2058 C ATOM 325 O PHE A 47 31.840 52.240 140.686 1.00 70.44 O ANISOU 325 O PHE A 47 10804 8953 7005 -50 280 1979 O ATOM 326 CB PHE A 47 29.568 53.359 138.730 1.00 70.42 C ANISOU 326 CB PHE A 47 10671 9085 6999 -67 309 2146 C ATOM 327 CG PHE A 47 28.804 53.271 137.432 1.00 70.63 C ANISOU 327 CG PHE A 47 10653 9165 7017 -118 291 2212 C ATOM 328 CD1 PHE A 47 29.217 52.421 136.411 1.00 70.57 C ANISOU 328 CD1 PHE A 47 10670 9143 6999 -193 245 2194 C ATOM 329 CD2 PHE A 47 27.676 54.061 137.220 1.00 71.12 C ANISOU 329 CD2 PHE A 47 10648 9293 7080 -86 319 2292 C ATOM 330 CE1 PHE A 47 28.506 52.346 135.218 1.00 70.94 C ANISOU 330 CE1 PHE A 47 10677 9242 7032 -242 225 2253 C ATOM 331 CE2 PHE A 47 26.965 53.987 136.031 1.00 71.31 C ANISOU 331 CE2 PHE A 47 10630 9371 7094 -133 298 2356 C ATOM 332 CZ PHE A 47 27.381 53.132 135.028 1.00 71.23 C ANISOU 332 CZ PHE A 47 10646 9348 7069 -213 250 2336 C ATOM 333 N ILE A 48 29.895 52.401 141.824 1.00 69.91 N ANISOU 333 N ILE A 48 10665 8999 6899 -18 319 2092 N ATOM 334 CA ILE A 48 30.538 52.514 143.147 1.00 69.86 C ANISOU 334 CA ILE A 48 10700 8955 6888 31 334 2036 C ATOM 335 C ILE A 48 31.246 51.209 143.556 1.00 68.84 C ANISOU 335 C ILE A 48 10624 8787 6744 -18 285 1997 C ATOM 336 O ILE A 48 32.276 51.248 144.237 1.00 68.02 O ANISOU 336 O ILE A 48 10569 8625 6648 10 280 1926 O ATOM 337 CB ILE A 48 29.530 52.999 144.228 1.00 71.08 C ANISOU 337 CB ILE A 48 10816 9172 7019 85 379 2085 C ATOM 338 CG1 ILE A 48 29.167 54.471 143.969 1.00 71.31 C ANISOU 338 CG1 ILE A 48 10809 9212 7073 157 430 2097 C ATOM 339 CG2 ILE A 48 30.080 52.837 145.647 1.00 71.20 C ANISOU 339 CG2 ILE A 48 10876 9161 7014 121 386 2035 C ATOM 340 CD1 ILE A 48 27.929 54.949 144.699 1.00 71.84 C ANISOU 340 CD1 ILE A 48 10821 9357 7118 207 477 2161 C ATOM 341 N VAL A 49 30.704 50.071 143.126 1.00 68.75 N ANISOU 341 N VAL A 49 10604 8805 6712 -94 246 2045 N ATOM 342 CA VAL A 49 31.359 48.771 143.314 1.00 68.26 C ANISOU 342 CA VAL A 49 10595 8699 6641 -146 193 2011 C ATOM 343 C VAL A 49 32.669 48.736 142.512 1.00 67.71 C ANISOU 343 C VAL A 49 10569 8552 6603 -154 169 1929 C ATOM 344 O VAL A 49 33.719 48.374 143.051 1.00 67.68 O ANISOU 344 O VAL A 49 10617 8489 6609 -141 149 1862 O ATOM 345 CB VAL A 49 30.439 47.590 142.898 1.00 68.17 C ANISOU 345 CB VAL A 49 10566 8732 6604 -231 154 2082 C ATOM 346 CG1 VAL A 49 31.187 46.258 142.934 1.00 67.91 C ANISOU 346 CG1 VAL A 49 10594 8638 6569 -285 95 2042 C ATOM 347 CG2 VAL A 49 29.207 47.521 143.789 1.00 68.62 C ANISOU 347 CG2 VAL A 49 10576 8867 6626 -229 177 2164 C ATOM 348 N SER A 50 32.600 49.122 141.235 1.00 67.01 N ANISOU 348 N SER A 50 10458 8470 6531 -173 171 1936 N ATOM 349 CA SER A 50 33.787 49.189 140.370 1.00 65.95 C ANISOU 349 CA SER A 50 10357 8274 6425 -180 155 1863 C ATOM 350 C SER A 50 34.837 50.142 140.942 1.00 65.00 C ANISOU 350 C SER A 50 10260 8103 6333 -110 184 1792 C ATOM 351 O SER A 50 36.031 49.822 140.964 1.00 64.54 O ANISOU 351 O SER A 50 10244 7984 6292 -109 163 1718 O ATOM 352 CB SER A 50 33.398 49.620 138.954 1.00 66.16 C ANISOU 352 CB SER A 50 10349 8329 6457 -207 161 1893 C ATOM 353 OG SER A 50 34.542 49.789 138.132 1.00 66.00 O ANISOU 353 OG SER A 50 10357 8257 6460 -210 154 1824 O ATOM 354 N LEU A 51 34.378 51.302 141.412 1.00 64.50 N ANISOU 354 N LEU A 51 10166 8063 6275 -52 231 1815 N ATOM 355 CA LEU A 51 35.250 52.280 142.066 1.00 63.86 C ANISOU 355 CA LEU A 51 10108 7936 6220 12 259 1751 C ATOM 356 C LEU A 51 35.855 51.744 143.374 1.00 63.66 C ANISOU 356 C LEU A 51 10124 7880 6182 31 243 1705 C ATOM 357 O LEU A 51 37.024 52.005 143.668 1.00 63.03 O ANISOU 357 O LEU A 51 10079 7744 6125 57 238 1630 O ATOM 358 CB LEU A 51 34.485 53.587 142.312 1.00 63.94 C ANISOU 358 CB LEU A 51 10079 7979 6236 71 312 1790 C ATOM 359 CG LEU A 51 35.214 54.768 142.959 1.00 63.91 C ANISOU 359 CG LEU A 51 10095 7928 6258 140 345 1731 C ATOM 360 CD1 LEU A 51 36.511 55.095 142.246 1.00 63.54 C ANISOU 360 CD1 LEU A 51 10075 7815 6249 132 334 1661 C ATOM 361 CD2 LEU A 51 34.304 55.984 142.977 1.00 64.27 C ANISOU 361 CD2 LEU A 51 10100 8006 6311 194 394 1778 C ATOM 362 N ALA A 52 35.062 50.995 144.144 1.00 63.94 N ANISOU 362 N ALA A 52 10156 7957 6181 17 233 1754 N ATOM 363 CA ALA A 52 35.544 50.343 145.374 1.00 63.94 C ANISOU 363 CA ALA A 52 10196 7934 6161 27 211 1722 C ATOM 364 C ALA A 52 36.597 49.277 145.079 1.00 63.43 C ANISOU 364 C ALA A 52 10177 7812 6109 -12 157 1669 C ATOM 365 O ALA A 52 37.640 49.248 145.731 1.00 63.12 O ANISOU 365 O ALA A 52 10176 7724 6080 14 143 1604 O ATOM 366 CB ALA A 52 34.385 49.733 146.151 1.00 64.44 C ANISOU 366 CB ALA A 52 10242 8061 6181 11 213 1797 C ATOM 367 N VAL A 53 36.321 48.428 144.085 1.00 63.37 N ANISOU 367 N VAL A 53 10166 7811 6101 -75 127 1696 N ATOM 368 CA VAL A 53 37.264 47.387 143.618 1.00 63.14 C ANISOU 368 CA VAL A 53 10178 7725 6085 -113 76 1645 C ATOM 369 C VAL A 53 38.650 47.973 143.311 1.00 63.09 C ANISOU 369 C VAL A 53 10191 7662 6117 -79 81 1557 C ATOM 370 O VAL A 53 39.679 47.424 143.736 1.00 62.57 O ANISOU 370 O VAL A 53 10164 7545 6062 -71 50 1498 O ATOM 371 CB VAL A 53 36.709 46.646 142.368 1.00 62.80 C ANISOU 371 CB VAL A 53 10123 7700 6037 -183 51 1683 C ATOM 372 CG1 VAL A 53 37.779 45.786 141.689 1.00 62.40 C ANISOU 372 CG1 VAL A 53 10114 7588 6005 -211 8 1617 C ATOM 373 CG2 VAL A 53 35.495 45.797 142.738 1.00 63.23 C ANISOU 373 CG2 VAL A 53 10166 7803 6056 -229 33 1764 C ATOM 374 N ALA A 54 38.660 49.089 142.580 1.00 63.60 N ANISOU 374 N ALA A 54 10226 7736 6203 -60 118 1553 N ATOM 375 CA ALA A 54 39.894 49.826 142.290 1.00 63.50 C ANISOU 375 CA ALA A 54 10224 7676 6227 -30 129 1478 C ATOM 376 C ALA A 54 40.628 50.270 143.565 1.00 63.44 C ANISOU 376 C ALA A 54 10239 7636 6227 23 135 1427 C ATOM 377 O ALA A 54 41.853 50.153 143.653 1.00 63.36 O ANISOU 377 O ALA A 54 10254 7579 6241 34 115 1356 O ATOM 378 CB ALA A 54 39.601 51.030 141.400 1.00 63.54 C ANISOU 378 CB ALA A 54 10192 7701 6250 -19 171 1497 C ATOM 379 N ASP A 55 39.875 50.766 144.546 1.00 63.47 N ANISOU 379 N ASP A 55 10234 7672 6208 57 160 1463 N ATOM 380 CA ASP A 55 40.459 51.200 145.822 1.00 63.59 C ANISOU 380 CA ASP A 55 10274 7665 6223 108 165 1418 C ATOM 381 C ASP A 55 40.972 50.022 146.669 1.00 62.53 C ANISOU 381 C ASP A 55 10179 7509 6070 98 117 1395 C ATOM 382 O ASP A 55 42.023 50.143 147.311 1.00 63.05 O ANISOU 382 O ASP A 55 10271 7535 6148 126 102 1331 O ATOM 383 CB ASP A 55 39.466 52.065 146.621 1.00 64.82 C ANISOU 383 CB ASP A 55 10410 7864 6355 151 209 1460 C ATOM 384 CG ASP A 55 39.157 53.416 145.944 1.00 65.53 C ANISOU 384 CG ASP A 55 10468 7960 6471 177 257 1471 C ATOM 385 OD1 ASP A 55 39.997 53.937 145.166 1.00 65.34 O ANISOU 385 OD1 ASP A 55 10444 7894 6485 174 258 1426 O ATOM 386 OD2 ASP A 55 38.061 53.963 146.213 1.00 66.34 O ANISOU 386 OD2 ASP A 55 10542 8108 6555 202 293 1525 O ATOM 387 N VAL A 56 40.261 48.890 146.648 1.00 61.28 N ANISOU 387 N VAL A 56 10023 7374 5883 55 91 1449 N ATOM 388 CA VAL A 56 40.740 47.653 147.305 1.00 60.20 C ANISOU 388 CA VAL A 56 9928 7211 5733 38 39 1435 C ATOM 389 C VAL A 56 42.091 47.251 146.711 1.00 58.81 C ANISOU 389 C VAL A 56 9775 6973 5595 32 5 1360 C ATOM 390 O VAL A 56 43.013 46.882 147.447 1.00 58.20 O ANISOU 390 O VAL A 56 9729 6859 5523 53 -25 1312 O ATOM 391 CB VAL A 56 39.762 46.452 147.161 1.00 60.18 C ANISOU 391 CB VAL A 56 9926 7236 5700 -18 13 1507 C ATOM 392 CG1 VAL A 56 40.371 45.177 147.748 1.00 60.08 C ANISOU 392 CG1 VAL A 56 9963 7182 5682 -34 -44 1489 C ATOM 393 CG2 VAL A 56 38.434 46.728 147.841 1.00 60.52 C ANISOU 393 CG2 VAL A 56 9942 7347 5703 -13 45 1585 C ATOM 394 N ALA A 57 42.191 47.330 145.383 1.00 57.53 N ANISOU 394 N ALA A 57 9595 6806 5458 5 11 1352 N ATOM 395 CA ALA A 57 43.433 47.011 144.680 1.00 56.62 C ANISOU 395 CA ALA A 57 9493 6640 5377 0 -13 1281 C ATOM 396 C ALA A 57 44.607 47.918 145.063 1.00 55.76 C ANISOU 396 C ALA A 57 9385 6501 5299 47 0 1209 C ATOM 397 O ALA A 57 45.742 47.452 145.096 1.00 55.55 O ANISOU 397 O ALA A 57 9377 6433 5296 55 -31 1148 O ATOM 398 CB ALA A 57 43.215 47.037 143.175 1.00 56.52 C ANISOU 398 CB ALA A 57 9458 6639 5377 -38 -1 1291 C ATOM 399 N VAL A 58 44.340 49.194 145.358 1.00 54.89 N ANISOU 399 N VAL A 58 9254 6410 5192 78 43 1215 N ATOM 400 CA VAL A 58 45.397 50.126 145.791 1.00 54.15 C ANISOU 400 CA VAL A 58 9162 6286 5126 119 53 1149 C ATOM 401 C VAL A 58 45.980 49.669 147.138 1.00 53.83 C ANISOU 401 C VAL A 58 9155 6225 5073 147 18 1116 C ATOM 402 O VAL A 58 47.204 49.444 147.269 1.00 53.62 O ANISOU 402 O VAL A 58 9140 6161 5072 158 -10 1052 O ATOM 403 CB VAL A 58 44.876 51.585 145.882 1.00 54.23 C ANISOU 403 CB VAL A 58 9149 6314 5140 147 106 1166 C ATOM 404 CG1 VAL A 58 45.912 52.525 146.500 1.00 54.20 C ANISOU 404 CG1 VAL A 58 9154 6276 5163 186 112 1097 C ATOM 405 CG2 VAL A 58 44.463 52.096 144.507 1.00 54.36 C ANISOU 405 CG2 VAL A 58 9134 6347 5174 122 137 1195 C ATOM 406 N GLY A 59 45.083 49.509 148.114 1.00 53.61 N ANISOU 406 N GLY A 59 9138 6228 5003 157 21 1164 N ATOM 407 CA GLY A 59 45.436 49.066 149.467 1.00 53.54 C ANISOU 407 CA GLY A 59 9161 6211 4968 181 -10 1148 C ATOM 408 C GLY A 59 46.007 47.660 149.558 1.00 53.25 C ANISOU 408 C GLY A 59 9154 6146 4933 161 -69 1137 C ATOM 409 O GLY A 59 46.897 47.411 150.367 1.00 53.20 O ANISOU 409 O GLY A 59 9171 6113 4928 185 -103 1093 O ATOM 410 N ALA A 60 45.499 46.746 148.730 1.00 52.95 N ANISOU 410 N ALA A 60 9114 6109 4893 117 -82 1176 N ATOM 411 CA ALA A 60 45.956 45.348 148.719 1.00 52.76 C ANISOU 411 CA ALA A 60 9122 6051 4873 96 -139 1168 C ATOM 412 C ALA A 60 47.169 45.072 147.818 1.00 52.31 C ANISOU 412 C ALA A 60 9064 5948 4863 96 -161 1099 C ATOM 413 O ALA A 60 47.919 44.138 148.098 1.00 52.57 O ANISOU 413 O ALA A 60 9124 5942 4907 102 -210 1070 O ATOM 414 CB ALA A 60 44.809 44.427 148.331 1.00 53.02 C ANISOU 414 CB ALA A 60 9159 6105 4880 46 -149 1242 C ATOM 415 N LEU A 61 47.343 45.848 146.739 1.00 51.54 N ANISOU 415 N LEU A 61 8933 5855 4792 90 -125 1076 N ATOM 416 CA LEU A 61 48.463 45.661 145.793 1.00 51.15 C ANISOU 416 CA LEU A 61 8876 5772 4785 88 -136 1011 C ATOM 417 C LEU A 61 49.434 46.844 145.722 1.00 50.74 C ANISOU 417 C LEU A 61 8798 5714 4767 118 -110 952 C ATOM 418 O LEU A 61 50.651 46.643 145.839 1.00 50.53 O ANISOU 418 O LEU A 61 8773 5657 4769 139 -136 889 O ATOM 419 CB LEU A 61 47.942 45.333 144.384 1.00 51.08 C ANISOU 419 CB LEU A 61 8854 5774 4777 44 -123 1034 C ATOM 420 CG LEU A 61 48.953 45.089 143.249 1.00 50.86 C ANISOU 420 CG LEU A 61 8817 5721 4784 38 -128 972 C ATOM 421 CD1 LEU A 61 49.924 43.970 143.580 1.00 50.92 C ANISOU 421 CD1 LEU A 61 8854 5684 4810 55 -181 923 C ATOM 422 CD2 LEU A 61 48.220 44.793 141.954 1.00 50.74 C ANISOU 422 CD2 LEU A 61 8793 5726 4757 -8 -114 1004 C ATOM 423 N VAL A 62 48.914 48.060 145.530 1.00 50.59 N ANISOU 423 N VAL A 62 8754 5722 4746 120 -61 972 N ATOM 424 CA VAL A 62 49.775 49.226 145.267 1.00 50.51 C ANISOU 424 CA VAL A 62 8718 5701 4771 138 -34 921 C ATOM 425 C VAL A 62 50.607 49.601 146.494 1.00 50.54 C ANISOU 425 C VAL A 62 8734 5686 4783 177 -53 874 C ATOM 426 O VAL A 62 51.812 49.826 146.371 1.00 50.21 O ANISOU 426 O VAL A 62 8679 5620 4776 188 -64 811 O ATOM 427 CB VAL A 62 48.970 50.454 144.760 1.00 50.55 C ANISOU 427 CB VAL A 62 8697 5732 4774 132 21 959 C ATOM 428 CG1 VAL A 62 49.843 51.708 144.660 1.00 50.64 C ANISOU 428 CG1 VAL A 62 8689 5726 4823 150 46 910 C ATOM 429 CG2 VAL A 62 48.325 50.141 143.414 1.00 50.51 C ANISOU 429 CG2 VAL A 62 8676 5749 4765 92 37 999 C ATOM 430 N ILE A 63 49.970 49.658 147.665 1.00 50.68 N ANISOU 430 N ILE A 63 8773 5716 4764 196 -58 904 N ATOM 431 CA ILE A 63 50.667 50.066 148.893 1.00 50.89 C ANISOU 431 CA ILE A 63 8814 5729 4789 232 -77 861 C ATOM 432 C ILE A 63 51.737 49.057 149.365 1.00 50.76 C ANISOU 432 C ILE A 63 8816 5686 4783 243 -136 817 C ATOM 433 O ILE A 63 52.838 49.475 149.748 1.00 50.84 O ANISOU 433 O ILE A 63 8819 5677 4819 264 -153 757 O ATOM 434 CB ILE A 63 49.671 50.469 150.011 1.00 51.32 C ANISOU 434 CB ILE A 63 8889 5813 4797 252 -60 903 C ATOM 435 CG1 ILE A 63 48.978 51.785 149.620 1.00 51.45 C ANISOU 435 CG1 ILE A 63 8883 5846 4817 257 -1 922 C ATOM 436 CG2 ILE A 63 50.386 50.646 151.349 1.00 51.69 C ANISOU 436 CG2 ILE A 63 8959 5849 4831 287 -90 859 C ATOM 437 CD1 ILE A 63 47.804 52.176 150.496 1.00 51.79 C ANISOU 437 CD1 ILE A 63 8937 5924 4813 278 25 971 C ATOM 438 N PRO A 64 51.427 47.743 149.345 1.00 50.61 N ANISOU 438 N PRO A 64 8818 5663 4747 229 -171 849 N ATOM 439 CA PRO A 64 52.450 46.714 149.586 1.00 50.66 C ANISOU 439 CA PRO A 64 8840 5637 4771 241 -228 809 C ATOM 440 C PRO A 64 53.657 46.766 148.644 1.00 50.71 C ANISOU 440 C PRO A 64 8816 5620 4831 242 -231 744 C ATOM 441 O PRO A 64 54.796 46.674 149.112 1.00 50.54 O ANISOU 441 O PRO A 64 8790 5578 4832 268 -265 691 O ATOM 442 CB PRO A 64 51.679 45.417 149.382 1.00 50.71 C ANISOU 442 CB PRO A 64 8872 5639 4753 216 -252 863 C ATOM 443 CG PRO A 64 50.318 45.748 149.860 1.00 50.73 C ANISOU 443 CG PRO A 64 8883 5680 4709 203 -222 933 C ATOM 444 CD PRO A 64 50.071 47.167 149.428 1.00 50.57 C ANISOU 444 CD PRO A 64 8830 5683 4699 206 -164 926 C ATOM 445 N LEU A 65 53.407 46.910 147.341 1.00 50.80 N ANISOU 445 N LEU A 65 8805 5638 4858 214 -197 751 N ATOM 446 CA LEU A 65 54.485 47.057 146.353 1.00 51.13 C ANISOU 446 CA LEU A 65 8813 5667 4945 213 -189 693 C ATOM 447 C LEU A 65 55.407 48.239 146.667 1.00 51.45 C ANISOU 447 C LEU A 65 8824 5707 5015 231 -175 642 C ATOM 448 O LEU A 65 56.630 48.123 146.552 1.00 51.79 O ANISOU 448 O LEU A 65 8847 5736 5095 245 -195 584 O ATOM 449 CB LEU A 65 53.912 47.219 144.943 1.00 51.09 C ANISOU 449 CB LEU A 65 8790 5679 4943 176 -147 716 C ATOM 450 CG LEU A 65 53.412 45.952 144.241 1.00 51.19 C ANISOU 450 CG LEU A 65 8823 5685 4941 152 -166 741 C ATOM 451 CD1 LEU A 65 52.551 46.298 143.034 1.00 50.98 C ANISOU 451 CD1 LEU A 65 8781 5686 4902 113 -122 779 C ATOM 452 CD2 LEU A 65 54.572 45.061 143.831 1.00 51.44 C ANISOU 452 CD2 LEU A 65 8852 5687 5003 167 -199 680 C ATOM 453 N ALA A 66 54.812 49.362 147.068 1.00 51.52 N ANISOU 453 N ALA A 66 8833 5731 5010 231 -141 665 N ATOM 454 CA ALA A 66 55.561 50.563 147.450 1.00 51.76 C ANISOU 454 CA ALA A 66 8844 5757 5066 243 -128 620 C ATOM 455 C ALA A 66 56.453 50.302 148.655 1.00 52.13 C ANISOU 455 C ALA A 66 8903 5790 5115 274 -180 577 C ATOM 456 O ALA A 66 57.625 50.686 148.657 1.00 52.31 O ANISOU 456 O ALA A 66 8898 5801 5174 281 -192 519 O ATOM 457 CB ALA A 66 54.613 51.720 147.740 1.00 51.75 C ANISOU 457 CB ALA A 66 8848 5768 5044 243 -85 656 C ATOM 458 N ILE A 67 55.896 49.634 149.664 1.00 52.52 N ANISOU 458 N ILE A 67 8990 5842 5122 290 -210 608 N ATOM 459 CA ILE A 67 56.655 49.252 150.864 1.00 53.21 C ANISOU 459 CA ILE A 67 9094 5919 5202 320 -266 575 C ATOM 460 C ILE A 67 57.796 48.288 150.496 1.00 53.74 C ANISOU 460 C ILE A 67 9145 5967 5306 329 -310 534 C ATOM 461 O ILE A 67 58.954 48.515 150.883 1.00 54.17 O ANISOU 461 O ILE A 67 9179 6014 5389 347 -339 479 O ATOM 462 CB ILE A 67 55.732 48.632 151.951 1.00 53.14 C ANISOU 462 CB ILE A 67 9133 5923 5136 331 -288 628 C ATOM 463 CG1 ILE A 67 54.755 49.687 152.481 1.00 53.06 C ANISOU 463 CG1 ILE A 67 9134 5936 5089 332 -244 657 C ATOM 464 CG2 ILE A 67 56.544 48.067 153.113 1.00 53.43 C ANISOU 464 CG2 ILE A 67 9189 5950 5162 360 -352 600 C ATOM 465 CD1 ILE A 67 53.510 49.115 153.121 1.00 53.12 C ANISOU 465 CD1 ILE A 67 9176 5967 5038 332 -243 726 C ATOM 466 N LEU A 68 57.466 47.238 149.739 1.00 53.84 N ANISOU 466 N LEU A 68 9165 5971 5320 318 -315 559 N ATOM 467 CA LEU A 68 58.465 46.266 149.280 1.00 54.37 C ANISOU 467 CA LEU A 68 9219 6017 5422 331 -352 519 C ATOM 468 C LEU A 68 59.584 46.911 148.465 1.00 54.70 C ANISOU 468 C LEU A 68 9205 6061 5515 330 -331 458 C ATOM 469 O LEU A 68 60.751 46.587 148.668 1.00 54.93 O ANISOU 469 O LEU A 68 9213 6081 5576 355 -368 408 O ATOM 470 CB LEU A 68 57.811 45.133 148.473 1.00 54.42 C ANISOU 470 CB LEU A 68 9245 6010 5419 314 -353 555 C ATOM 471 CG LEU A 68 57.008 44.077 149.252 1.00 54.60 C ANISOU 471 CG LEU A 68 9322 6021 5402 316 -392 609 C ATOM 472 CD1 LEU A 68 56.382 43.094 148.270 1.00 54.61 C ANISOU 472 CD1 LEU A 68 9340 6008 5400 290 -390 638 C ATOM 473 CD2 LEU A 68 57.858 43.345 150.288 1.00 54.84 C ANISOU 473 CD2 LEU A 68 9369 6027 5437 355 -459 586 C ATOM 474 N ILE A 69 59.228 47.819 147.557 1.00 55.27 N ANISOU 474 N ILE A 69 9254 6150 5596 300 -273 466 N ATOM 475 CA ILE A 69 60.228 48.594 146.801 1.00 56.04 C ANISOU 475 CA ILE A 69 9298 6254 5738 291 -247 415 C ATOM 476 C ILE A 69 61.037 49.521 147.725 1.00 57.02 C ANISOU 476 C ILE A 69 9405 6379 5880 304 -263 375 C ATOM 477 O ILE A 69 62.252 49.663 147.546 1.00 57.13 O ANISOU 477 O ILE A 69 9376 6394 5935 311 -275 322 O ATOM 478 CB ILE A 69 59.575 49.390 145.634 1.00 55.51 C ANISOU 478 CB ILE A 69 9214 6203 5671 253 -182 442 C ATOM 479 CG1 ILE A 69 59.045 48.425 144.552 1.00 55.57 C ANISOU 479 CG1 ILE A 69 9231 6214 5667 238 -171 466 C ATOM 480 CG2 ILE A 69 60.542 50.394 145.011 1.00 55.42 C ANISOU 480 CG2 ILE A 69 9151 6201 5703 239 -152 398 C ATOM 481 CD1 ILE A 69 60.094 47.773 143.668 1.00 55.73 C ANISOU 481 CD1 ILE A 69 9219 6234 5721 244 -177 415 C ATOM 482 N ASN A 70 60.371 50.134 148.705 1.00 58.07 N ANISOU 482 N ASN A 70 9569 6512 5980 307 -262 400 N ATOM 483 CA ASN A 70 61.037 51.022 149.665 1.00 59.43 C ANISOU 483 CA ASN A 70 9734 6682 6162 318 -281 361 C ATOM 484 C ASN A 70 62.079 50.285 150.508 1.00 60.41 C ANISOU 484 C ASN A 70 9855 6801 6296 349 -348 322 C ATOM 485 O ASN A 70 63.234 50.716 150.588 1.00 60.79 O ANISOU 485 O ASN A 70 9863 6851 6382 351 -366 269 O ATOM 486 CB ASN A 70 60.010 51.696 150.583 1.00 59.95 C ANISOU 486 CB ASN A 70 9844 6752 6183 321 -267 396 C ATOM 487 CG ASN A 70 60.640 52.713 151.523 1.00 60.57 C ANISOU 487 CG ASN A 70 9920 6825 6268 328 -283 352 C ATOM 488 OD1 ASN A 70 60.802 52.455 152.716 1.00 60.95 O ANISOU 488 OD1 ASN A 70 9995 6875 6288 352 -328 341 O ATOM 489 ND2 ASN A 70 61.006 53.868 150.986 1.00 60.77 N ANISOU 489 ND2 ASN A 70 9916 6844 6329 305 -248 326 N ATOM 490 N ILE A 71 61.665 49.179 151.126 1.00 61.28 N ANISOU 490 N ILE A 71 10004 6906 6372 371 -388 351 N ATOM 491 CA ILE A 71 62.580 48.371 151.957 1.00 62.16 C ANISOU 491 CA ILE A 71 10117 7011 6490 405 -457 322 C ATOM 492 C ILE A 71 63.549 47.497 151.140 1.00 63.24 C ANISOU 492 C ILE A 71 10214 7138 6673 419 -477 289 C ATOM 493 O ILE A 71 64.603 47.112 151.646 1.00 63.83 O ANISOU 493 O ILE A 71 10269 7211 6770 448 -529 251 O ATOM 494 CB ILE A 71 61.818 47.505 152.998 1.00 61.94 C ANISOU 494 CB ILE A 71 10148 6978 6407 425 -496 370 C ATOM 495 CG1 ILE A 71 61.094 46.315 152.333 1.00 61.90 C ANISOU 495 CG1 ILE A 71 10167 6958 6392 420 -493 416 C ATOM 496 CG2 ILE A 71 60.873 48.381 153.813 1.00 61.69 C ANISOU 496 CG2 ILE A 71 10151 6961 6326 415 -472 400 C ATOM 497 CD1 ILE A 71 60.096 45.604 153.227 1.00 61.97 C ANISOU 497 CD1 ILE A 71 10234 6965 6344 425 -518 477 C ATOM 498 N GLY A 72 63.195 47.194 149.890 1.00 64.21 N ANISOU 498 N GLY A 72 10327 7259 6809 401 -436 302 N ATOM 499 CA GLY A 72 63.969 46.278 149.049 1.00 65.55 C ANISOU 499 CA GLY A 72 10467 7420 7017 418 -449 270 C ATOM 500 C GLY A 72 65.242 46.853 148.445 1.00 67.00 C ANISOU 500 C GLY A 72 10580 7621 7254 417 -435 209 C ATOM 501 O GLY A 72 65.605 47.996 148.735 1.00 67.25 O ANISOU 501 O GLY A 72 10586 7667 7297 400 -421 190 O ATOM 502 N PRO A 73 65.928 46.062 147.592 1.00 68.98 N ANISOU 502 N PRO A 73 10800 7870 7537 435 -437 178 N ATOM 503 CA PRO A 73 67.174 46.465 146.944 1.00 70.20 C ANISOU 503 CA PRO A 73 10881 8048 7743 436 -422 121 C ATOM 504 C PRO A 73 66.939 47.208 145.625 1.00 70.78 C ANISOU 504 C PRO A 73 10925 8143 7824 393 -348 123 C ATOM 505 O PRO A 73 65.793 47.530 145.285 1.00 70.91 O ANISOU 505 O PRO A 73 10979 8156 7808 361 -310 170 O ATOM 506 CB PRO A 73 67.846 45.118 146.668 1.00 70.56 C ANISOU 506 CB PRO A 73 10916 8080 7811 483 -458 93 C ATOM 507 CG PRO A 73 66.700 44.222 146.336 1.00 70.05 C ANISOU 507 CG PRO A 73 10915 7987 7710 479 -453 138 C ATOM 508 CD PRO A 73 65.538 44.697 147.180 1.00 69.52 C ANISOU 508 CD PRO A 73 10904 7914 7596 454 -454 195 C ATOM 509 N GLN A 74 68.026 47.476 144.898 1.00 71.45 N ANISOU 509 N GLN A 74 10941 8253 7951 391 -327 76 N ATOM 510 CA GLN A 74 67.938 47.941 143.512 1.00 71.69 C ANISOU 510 CA GLN A 74 10941 8308 7989 354 -259 76 C ATOM 511 C GLN A 74 67.322 46.845 142.651 1.00 71.08 C ANISOU 511 C GLN A 74 10896 8221 7889 364 -246 90 C ATOM 512 O GLN A 74 67.448 45.659 142.967 1.00 72.42 O ANISOU 512 O GLN A 74 11090 8366 8058 406 -291 79 O ATOM 513 CB GLN A 74 69.316 48.303 142.957 1.00 73.00 C ANISOU 513 CB GLN A 74 11023 8508 8203 354 -243 21 C ATOM 514 CG GLN A 74 69.911 49.577 143.536 1.00 73.86 C ANISOU 514 CG GLN A 74 11094 8631 8337 327 -244 8 C ATOM 515 CD GLN A 74 71.247 49.941 142.906 1.00 75.26 C ANISOU 515 CD GLN A 74 11182 8849 8564 318 -225 -40 C ATOM 516 OE1 GLN A 74 71.458 49.760 141.702 1.00 75.76 O ANISOU 516 OE1 GLN A 74 11212 8939 8634 309 -178 -50 O ATOM 517 NE2 GLN A 74 72.157 50.465 143.720 1.00 76.21 N ANISOU 517 NE2 GLN A 74 11262 8978 8715 319 -261 -70 N ATOM 518 N THR A 75 66.665 47.249 141.566 1.00 69.71 N ANISOU 518 N THR A 75 10725 8062 7697 323 -188 115 N ATOM 519 CA THR A 75 65.960 46.315 140.687 1.00 68.88 C ANISOU 519 CA THR A 75 10656 7951 7565 322 -174 131 C ATOM 520 C THR A 75 66.345 46.530 139.234 1.00 68.35 C ANISOU 520 C THR A 75 10543 7920 7505 299 -116 108 C ATOM 521 O THR A 75 66.887 47.575 138.878 1.00 68.17 O ANISOU 521 O THR A 75 10469 7928 7502 273 -78 97 O ATOM 522 CB THR A 75 64.435 46.493 140.800 1.00 68.37 C ANISOU 522 CB THR A 75 10651 7871 7453 291 -162 200 C ATOM 523 OG1 THR A 75 64.070 47.822 140.410 1.00 67.86 O ANISOU 523 OG1 THR A 75 10568 7831 7385 246 -111 227 O ATOM 524 CG2 THR A 75 63.966 46.239 142.221 1.00 68.47 C ANISOU 524 CG2 THR A 75 10710 7853 7450 312 -214 227 C ATOM 525 N TYR A 76 66.044 45.538 138.399 1.00 67.47 N ANISOU 525 N TYR A 76 10455 7804 7375 307 -109 101 N ATOM 526 CA TYR A 76 66.114 45.705 136.949 1.00 67.24 C ANISOU 526 CA TYR A 76 10398 7813 7336 279 -50 89 C ATOM 527 C TYR A 76 65.182 46.838 136.517 1.00 66.61 C ANISOU 527 C TYR A 76 10326 7752 7228 221 -4 147 C ATOM 528 O TYR A 76 64.233 47.169 137.235 1.00 66.48 O ANISOU 528 O TYR A 76 10352 7714 7193 207 -19 198 O ATOM 529 CB TYR A 76 65.678 44.426 136.227 1.00 67.30 C ANISOU 529 CB TYR A 76 10447 7804 7316 293 -57 79 C ATOM 530 CG TYR A 76 66.625 43.254 136.344 1.00 67.42 C ANISOU 530 CG TYR A 76 10454 7800 7360 355 -94 16 C ATOM 531 CD1 TYR A 76 67.914 43.312 135.811 1.00 67.62 C ANISOU 531 CD1 TYR A 76 10409 7862 7418 380 -71 -45 C ATOM 532 CD2 TYR A 76 66.220 42.070 136.955 1.00 67.51 C ANISOU 532 CD2 TYR A 76 10525 7758 7364 388 -151 21 C ATOM 533 CE1 TYR A 76 68.779 42.232 135.905 1.00 68.34 C ANISOU 533 CE1 TYR A 76 10490 7936 7538 443 -104 -103 C ATOM 534 CE2 TYR A 76 67.074 40.981 137.052 1.00 68.16 C ANISOU 534 CE2 TYR A 76 10603 7816 7475 449 -187 -34 C ATOM 535 CZ TYR A 76 68.352 41.063 136.527 1.00 68.57 C ANISOU 535 CZ TYR A 76 10585 7905 7563 480 -163 -98 C ATOM 536 OH TYR A 76 69.193 39.979 136.630 1.00 68.62 O ANISOU 536 OH TYR A 76 10584 7887 7600 547 -199 -153 O ATOM 537 N PHE A 77 65.440 47.431 135.352 1.00 66.19 N ANISOU 537 N PHE A 77 10233 7741 7172 188 52 141 N ATOM 538 CA PHE A 77 64.505 48.423 134.797 1.00 65.52 C ANISOU 538 CA PHE A 77 10159 7674 7060 134 96 201 C ATOM 539 C PHE A 77 63.070 47.868 134.633 1.00 65.16 C ANISOU 539 C PHE A 77 10179 7610 6966 120 87 253 C ATOM 540 O PHE A 77 62.091 48.530 135.021 1.00 64.64 O ANISOU 540 O PHE A 77 10140 7536 6884 96 91 312 O ATOM 541 CB PHE A 77 65.014 48.968 133.460 1.00 65.67 C ANISOU 541 CB PHE A 77 10129 7745 7077 101 157 188 C ATOM 542 CG PHE A 77 64.213 50.129 132.939 1.00 65.09 C ANISOU 542 CG PHE A 77 10058 7688 6982 47 201 251 C ATOM 543 CD1 PHE A 77 64.499 51.424 133.352 1.00 64.92 C ANISOU 543 CD1 PHE A 77 10008 7666 6990 25 216 269 C ATOM 544 CD2 PHE A 77 63.160 49.928 132.048 1.00 64.61 C ANISOU 544 CD2 PHE A 77 10032 7642 6874 19 223 294 C ATOM 545 CE1 PHE A 77 63.760 52.498 132.882 1.00 64.66 C ANISOU 545 CE1 PHE A 77 9982 7642 6942 -19 254 329 C ATOM 546 CE2 PHE A 77 62.415 50.997 131.574 1.00 64.36 C ANISOU 546 CE2 PHE A 77 10002 7626 6824 -26 260 356 C ATOM 547 CZ PHE A 77 62.716 52.286 131.992 1.00 64.55 C ANISOU 547 CZ PHE A 77 9999 7645 6881 -43 276 374 C ATOM 548 N HIS A 78 62.960 46.656 134.084 1.00 65.59 N ANISOU 548 N HIS A 78 10259 7660 7000 135 74 230 N ATOM 549 CA HIS A 78 61.652 46.030 133.804 1.00 65.38 C ANISOU 549 CA HIS A 78 10291 7620 6928 115 63 275 C ATOM 550 C HIS A 78 60.825 45.799 135.074 1.00 64.57 C ANISOU 550 C HIS A 78 10237 7476 6820 126 16 318 C ATOM 551 O HIS A 78 59.606 46.000 135.064 1.00 64.25 O ANISOU 551 O HIS A 78 10228 7436 6746 95 21 380 O ATOM 552 CB HIS A 78 61.808 44.714 132.997 1.00 66.22 C ANISOU 552 CB HIS A 78 10419 7722 7017 130 53 232 C ATOM 553 CG HIS A 78 62.051 43.495 133.837 1.00 66.87 C ANISOU 553 CG HIS A 78 10536 7753 7116 178 -7 201 C ATOM 554 ND1 HIS A 78 63.311 42.990 134.080 1.00 67.44 N ANISOU 554 ND1 HIS A 78 10579 7815 7228 230 -25 134 N ATOM 555 CD2 HIS A 78 61.188 42.678 134.490 1.00 67.43 C ANISOU 555 CD2 HIS A 78 10667 7779 7171 182 -54 234 C ATOM 556 CE1 HIS A 78 63.212 41.920 134.851 1.00 68.01 C ANISOU 556 CE1 HIS A 78 10696 7836 7308 266 -83 126 C ATOM 557 NE2 HIS A 78 61.934 41.710 135.115 1.00 67.63 N ANISOU 557 NE2 HIS A 78 10704 7765 7225 235 -101 187 N ATOM 558 N THR A 79 61.499 45.381 136.150 1.00 64.18 N ANISOU 558 N THR A 79 10188 7395 6800 170 -27 286 N ATOM 559 CA THR A 79 60.863 45.120 137.444 1.00 63.78 C ANISOU 559 CA THR A 79 10181 7309 6743 184 -73 323 C ATOM 560 C THR A 79 60.212 46.386 137.986 1.00 63.21 C ANISOU 560 C THR A 79 10105 7248 6662 160 -52 375 C ATOM 561 O THR A 79 59.051 46.375 138.390 1.00 62.31 O ANISOU 561 O THR A 79 10029 7125 6518 145 -60 432 O ATOM 562 CB THR A 79 61.892 44.626 138.485 1.00 64.02 C ANISOU 562 CB THR A 79 10203 7311 6809 236 -123 276 C ATOM 563 OG1 THR A 79 62.610 43.500 137.966 1.00 64.55 O ANISOU 563 OG1 THR A 79 10268 7365 6890 268 -141 222 O ATOM 564 CG2 THR A 79 61.210 44.239 139.805 1.00 63.73 C ANISOU 564 CG2 THR A 79 10216 7239 6757 250 -173 317 C ATOM 565 N CYS A 80 60.981 47.471 137.983 1.00 63.30 N ANISOU 565 N CYS A 80 10069 7278 6703 156 -25 353 N ATOM 566 CA CYS A 80 60.500 48.766 138.437 1.00 63.04 C ANISOU 566 CA CYS A 80 10031 7250 6668 136 -2 393 C ATOM 567 C CYS A 80 59.426 49.312 137.501 1.00 62.51 C ANISOU 567 C CYS A 80 9972 7207 6571 93 42 450 C ATOM 568 O CYS A 80 58.428 49.871 137.966 1.00 62.57 O ANISOU 568 O CYS A 80 10002 7210 6559 83 48 504 O ATOM 569 CB CYS A 80 61.660 49.755 138.551 1.00 63.56 C ANISOU 569 CB CYS A 80 10044 7326 6776 137 13 353 C ATOM 570 SG CYS A 80 61.237 51.298 139.389 1.00 63.93 S ANISOU 570 SG CYS A 80 10095 7364 6830 121 28 388 S ATOM 571 N LEU A 81 59.620 49.140 136.193 1.00 62.10 N ANISOU 571 N LEU A 81 9899 7181 6511 71 74 438 N ATOM 572 CA LEU A 81 58.600 49.537 135.218 1.00 61.80 C ANISOU 572 CA LEU A 81 9869 7170 6440 30 112 493 C ATOM 573 C LEU A 81 57.265 48.810 135.438 1.00 61.15 C ANISOU 573 C LEU A 81 9837 7077 6317 24 88 545 C ATOM 574 O LEU A 81 56.208 49.442 135.395 1.00 60.64 O ANISOU 574 O LEU A 81 9783 7025 6232 1 106 607 O ATOM 575 CB LEU A 81 59.095 49.312 133.784 1.00 62.53 C ANISOU 575 CB LEU A 81 9936 7297 6524 9 145 466 C ATOM 576 CG LEU A 81 58.175 49.765 132.634 1.00 62.49 C ANISOU 576 CG LEU A 81 9934 7327 6482 -36 184 521 C ATOM 577 CD1 LEU A 81 57.787 51.235 132.763 1.00 62.45 C ANISOU 577 CD1 LEU A 81 9911 7328 6486 -56 217 572 C ATOM 578 CD2 LEU A 81 58.823 49.489 131.283 1.00 62.85 C ANISOU 578 CD2 LEU A 81 9952 7410 6515 -53 216 484 C ATOM 579 N MET A 82 57.317 47.496 135.671 1.00 60.98 N ANISOU 579 N MET A 82 9845 7034 6288 43 46 521 N ATOM 580 CA MET A 82 56.102 46.698 135.932 1.00 60.60 C ANISOU 580 CA MET A 82 9845 6973 6204 32 18 569 C ATOM 581 C MET A 82 55.356 47.114 137.191 1.00 58.82 C ANISOU 581 C MET A 82 9640 6735 5974 42 2 618 C ATOM 582 O MET A 82 54.129 47.206 137.184 1.00 58.09 O ANISOU 582 O MET A 82 9566 6655 5850 19 8 681 O ATOM 583 CB MET A 82 56.433 45.206 136.034 1.00 62.19 C ANISOU 583 CB MET A 82 10078 7143 6406 53 -28 530 C ATOM 584 CG MET A 82 56.610 44.518 134.692 1.00 63.64 C ANISOU 584 CG MET A 82 10264 7341 6575 35 -16 499 C ATOM 585 SD MET A 82 57.267 42.847 134.908 1.00 65.67 S ANISOU 585 SD MET A 82 10557 7549 6845 73 -71 437 S ATOM 586 CE MET A 82 55.876 42.041 135.708 1.00 65.52 C ANISOU 586 CE MET A 82 10601 7498 6796 55 -119 506 C ATOM 587 N VAL A 83 56.108 47.356 138.261 1.00 57.80 N ANISOU 587 N VAL A 83 9503 6583 5872 77 -17 586 N ATOM 588 CA VAL A 83 55.547 47.745 139.564 1.00 56.85 C ANISOU 588 CA VAL A 83 9404 6452 5745 92 -32 622 C ATOM 589 C VAL A 83 54.911 49.146 139.527 1.00 55.65 C ANISOU 589 C VAL A 83 9234 6321 5588 76 11 665 C ATOM 590 O VAL A 83 53.974 49.417 140.276 1.00 55.45 O ANISOU 590 O VAL A 83 9229 6297 5540 80 10 713 O ATOM 591 CB VAL A 83 56.627 47.647 140.680 1.00 57.15 C ANISOU 591 CB VAL A 83 9438 6464 5812 134 -68 570 C ATOM 592 CG1 VAL A 83 56.139 48.216 142.004 1.00 57.22 C ANISOU 592 CG1 VAL A 83 9466 6467 5809 149 -79 600 C ATOM 593 CG2 VAL A 83 57.071 46.202 140.869 1.00 57.34 C ANISOU 593 CG2 VAL A 83 9485 6461 5838 156 -118 540 C ATOM 594 N ALA A 84 55.406 50.019 138.649 1.00 54.72 N ANISOU 594 N ALA A 84 9081 6220 5490 60 51 649 N ATOM 595 CA ALA A 84 54.861 51.370 138.513 1.00 54.06 C ANISOU 595 CA ALA A 84 8983 6149 5407 46 93 690 C ATOM 596 C ALA A 84 53.457 51.454 137.888 1.00 53.53 C ANISOU 596 C ALA A 84 8926 6108 5303 18 115 764 C ATOM 597 O ALA A 84 52.764 52.440 138.098 1.00 53.69 O ANISOU 597 O ALA A 84 8944 6135 5321 18 140 807 O ATOM 598 CB ALA A 84 55.828 52.238 137.724 1.00 54.18 C ANISOU 598 CB ALA A 84 8957 6173 5455 31 127 657 C ATOM 599 N CYS A 85 53.040 50.440 137.126 1.00 53.08 N ANISOU 599 N CYS A 85 8881 6066 5220 -2 104 776 N ATOM 600 CA CYS A 85 51.812 50.517 136.303 1.00 52.83 C ANISOU 600 CA CYS A 85 8851 6066 5154 -36 124 843 C ATOM 601 C CYS A 85 50.434 50.290 136.978 1.00 52.45 C ANISOU 601 C CYS A 85 8827 6026 5075 -36 111 910 C ATOM 602 O CYS A 85 49.461 50.981 136.622 1.00 52.26 O ANISOU 602 O CYS A 85 8791 6029 5035 -51 138 971 O ATOM 603 CB CYS A 85 51.947 49.599 135.084 1.00 53.20 C ANISOU 603 CB CYS A 85 8900 6129 5182 -65 119 826 C ATOM 604 SG CYS A 85 53.317 50.060 133.981 1.00 53.67 S ANISOU 604 SG CYS A 85 8922 6200 5267 -74 152 765 S ATOM 605 N PRO A 86 50.321 49.317 137.916 1.00 52.23 N ANISOU 605 N PRO A 86 8828 5977 5037 -21 69 903 N ATOM 606 CA PRO A 86 49.025 49.056 138.573 1.00 51.86 C ANISOU 606 CA PRO A 86 8800 5945 4959 -25 59 969 C ATOM 607 C PRO A 86 48.290 50.298 139.084 1.00 51.37 C ANISOU 607 C PRO A 86 8722 5900 4894 -9 93 1016 C ATOM 608 O PRO A 86 47.078 50.443 138.856 1.00 51.23 O ANISOU 608 O PRO A 86 8698 5914 4850 -26 107 1084 O ATOM 609 CB PRO A 86 49.413 48.147 139.741 1.00 52.10 C ANISOU 609 CB PRO A 86 8861 5943 4990 0 13 942 C ATOM 610 CG PRO A 86 50.584 47.382 139.238 1.00 52.25 C ANISOU 610 CG PRO A 86 8884 5936 5030 1 -9 874 C ATOM 611 CD PRO A 86 51.309 48.273 138.261 1.00 52.35 C ANISOU 611 CD PRO A 86 8861 5961 5067 -4 29 841 C ATOM 612 N VAL A 87 49.024 51.185 139.753 1.00 51.16 N ANISOU 612 N VAL A 87 8689 5852 4896 23 105 980 N ATOM 613 CA VAL A 87 48.474 52.458 140.225 1.00 51.07 C ANISOU 613 CA VAL A 87 8667 5848 4887 43 140 1012 C ATOM 614 C VAL A 87 47.940 53.325 139.071 1.00 50.79 C ANISOU 614 C VAL A 87 8604 5837 4855 21 181 1055 C ATOM 615 O VAL A 87 46.886 53.949 139.214 1.00 50.70 O ANISOU 615 O VAL A 87 8586 5847 4830 29 204 1113 O ATOM 616 CB VAL A 87 49.497 53.240 141.092 1.00 51.40 C ANISOU 616 CB VAL A 87 8711 5856 4962 78 141 954 C ATOM 617 CG1 VAL A 87 50.647 53.794 140.260 1.00 51.50 C ANISOU 617 CG1 VAL A 87 8700 5854 5013 65 156 906 C ATOM 618 CG2 VAL A 87 48.810 54.353 141.869 1.00 51.64 C ANISOU 618 CG2 VAL A 87 8743 5887 4988 107 168 984 C ATOM 619 N LEU A 88 48.642 53.319 137.930 1.00 50.58 N ANISOU 619 N LEU A 88 8562 5812 4843 -4 189 1029 N ATOM 620 CA LEU A 88 48.211 54.060 136.730 1.00 50.35 C ANISOU 620 CA LEU A 88 8509 5809 4813 -30 225 1071 C ATOM 621 C LEU A 88 46.893 53.520 136.193 1.00 50.32 C ANISOU 621 C LEU A 88 8504 5846 4769 -56 221 1141 C ATOM 622 O LEU A 88 45.993 54.299 135.848 1.00 50.42 O ANISOU 622 O LEU A 88 8499 5883 4774 -59 247 1202 O ATOM 623 CB LEU A 88 49.266 54.009 135.619 1.00 50.16 C ANISOU 623 CB LEU A 88 8469 5785 4804 -56 233 1027 C ATOM 624 CG LEU A 88 50.682 54.468 135.968 1.00 50.20 C ANISOU 624 CG LEU A 88 8466 5756 4851 -39 236 956 C ATOM 625 CD1 LEU A 88 51.589 54.342 134.758 1.00 50.33 C ANISOU 625 CD1 LEU A 88 8460 5785 4875 -68 249 922 C ATOM 626 CD2 LEU A 88 50.666 55.891 136.499 1.00 50.27 C ANISOU 626 CD2 LEU A 88 8468 5744 4888 -18 263 969 C ATOM 627 N ILE A 89 46.780 52.192 136.148 1.00 50.29 N ANISOU 627 N ILE A 89 8518 5848 4741 -76 185 1132 N ATOM 628 CA ILE A 89 45.531 51.533 135.737 1.00 50.57 C ANISOU 628 CA ILE A 89 8555 5921 4737 -107 173 1196 C ATOM 629 C ILE A 89 44.414 51.897 136.717 1.00 51.03 C ANISOU 629 C ILE A 89 8610 5994 4783 -84 180 1255 C ATOM 630 O ILE A 89 43.345 52.426 136.325 1.00 51.60 O ANISOU 630 O ILE A 89 8659 6105 4840 -93 201 1324 O ATOM 631 CB ILE A 89 45.673 49.988 135.689 1.00 50.59 C ANISOU 631 CB ILE A 89 8586 5914 4721 -131 128 1170 C ATOM 632 CG1 ILE A 89 46.720 49.562 134.650 1.00 50.79 C ANISOU 632 CG1 ILE A 89 8613 5929 4754 -150 124 1108 C ATOM 633 CG2 ILE A 89 44.328 49.319 135.381 1.00 50.63 C ANISOU 633 CG2 ILE A 89 8593 5957 4687 -169 111 1239 C ATOM 634 CD1 ILE A 89 47.311 48.189 134.893 1.00 50.89 C ANISOU 634 CD1 ILE A 89 8659 5911 4766 -151 80 1055 C ATOM 635 N LEU A 90 44.683 51.631 137.995 1.00 51.30 N ANISOU 635 N LEU A 90 8665 6003 4822 -52 163 1229 N ATOM 636 CA LEU A 90 43.657 51.752 139.025 1.00 51.49 C ANISOU 636 CA LEU A 90 8690 6046 4826 -31 166 1280 C ATOM 637 C LEU A 90 43.161 53.187 139.177 1.00 51.89 C ANISOU 637 C LEU A 90 8717 6109 4889 0 211 1314 C ATOM 638 O LEU A 90 41.947 53.417 139.270 1.00 52.00 O ANISOU 638 O LEU A 90 8712 6161 4881 3 226 1382 O ATOM 639 CB LEU A 90 44.163 51.201 140.356 1.00 51.37 C ANISOU 639 CB LEU A 90 8705 6000 4811 -3 138 1241 C ATOM 640 CG LEU A 90 44.437 49.695 140.367 1.00 51.19 C ANISOU 640 CG LEU A 90 8709 5963 4774 -31 90 1222 C ATOM 641 CD1 LEU A 90 45.176 49.317 141.648 1.00 51.35 C ANISOU 641 CD1 LEU A 90 8759 5949 4801 2 63 1176 C ATOM 642 CD2 LEU A 90 43.164 48.886 140.187 1.00 51.27 C ANISOU 642 CD2 LEU A 90 8719 6010 4748 -69 75 1293 C ATOM 643 N THR A 91 44.093 54.142 139.175 1.00 52.42 N ANISOU 643 N THR A 91 8783 6142 4992 24 231 1266 N ATOM 644 CA THR A 91 43.739 55.569 139.220 1.00 53.08 C ANISOU 644 CA THR A 91 8848 6224 5093 54 272 1292 C ATOM 645 C THR A 91 42.899 55.973 138.007 1.00 53.59 C ANISOU 645 C THR A 91 8884 6327 5151 29 294 1358 C ATOM 646 O THR A 91 41.925 56.718 138.157 1.00 54.02 O ANISOU 646 O THR A 91 8921 6403 5201 53 320 1415 O ATOM 647 CB THR A 91 44.978 56.486 139.316 1.00 52.98 C ANISOU 647 CB THR A 91 8842 6163 5123 73 286 1227 C ATOM 648 OG1 THR A 91 45.787 56.087 140.428 1.00 53.05 O ANISOU 648 OG1 THR A 91 8877 6141 5138 95 260 1165 O ATOM 649 CG2 THR A 91 44.573 57.940 139.508 1.00 53.15 C ANISOU 649 CG2 THR A 91 8855 6173 5166 108 325 1252 C ATOM 650 N GLN A 92 43.262 55.477 136.821 1.00 53.94 N ANISOU 650 N GLN A 92 8922 6381 5190 -15 284 1352 N ATOM 651 CA GLN A 92 42.474 55.758 135.616 1.00 54.40 C ANISOU 651 CA GLN A 92 8953 6481 5235 -44 298 1416 C ATOM 652 C GLN A 92 41.070 55.157 135.700 1.00 55.07 C ANISOU 652 C GLN A 92 9025 6617 5282 -57 286 1489 C ATOM 653 O GLN A 92 40.084 55.819 135.323 1.00 55.57 O ANISOU 653 O GLN A 92 9059 6715 5338 -52 308 1558 O ATOM 654 CB GLN A 92 43.185 55.282 134.347 1.00 54.16 C ANISOU 654 CB GLN A 92 8923 6456 5200 -91 289 1389 C ATOM 655 CG GLN A 92 42.585 55.832 133.055 1.00 54.31 C ANISOU 655 CG GLN A 92 8915 6514 5207 -119 308 1450 C ATOM 656 CD GLN A 92 42.534 57.354 133.017 1.00 54.35 C ANISOU 656 CD GLN A 92 8903 6503 5242 -88 347 1477 C ATOM 657 OE1 GLN A 92 43.546 58.022 133.198 1.00 53.91 O ANISOU 657 OE1 GLN A 92 8855 6404 5222 -72 362 1429 O ATOM 658 NE2 GLN A 92 41.348 57.903 132.793 1.00 54.71 N ANISOU 658 NE2 GLN A 92 8926 6583 5278 -79 361 1557 N ATOM 659 N SER A 93 40.974 53.923 136.206 1.00 55.71 N ANISOU 659 N SER A 93 9124 6701 5339 -74 252 1476 N ATOM 660 CA SER A 93 39.653 53.303 136.434 1.00 56.47 C ANISOU 660 CA SER A 93 9208 6846 5401 -91 238 1545 C ATOM 661 C SER A 93 38.728 54.176 137.292 1.00 57.35 C ANISOU 661 C SER A 93 9297 6978 5513 -43 269 1596 C ATOM 662 O SER A 93 37.543 54.356 136.964 1.00 57.66 O ANISOU 662 O SER A 93 9303 7070 5535 -51 279 1672 O ATOM 663 CB SER A 93 39.795 51.913 137.062 1.00 56.32 C ANISOU 663 CB SER A 93 9219 6816 5363 -112 196 1520 C ATOM 664 OG SER A 93 38.544 51.247 137.108 1.00 56.59 O ANISOU 664 OG SER A 93 9239 6898 5363 -142 180 1590 O ATOM 665 N SER A 94 39.284 54.728 138.372 1.00 58.10 N ANISOU 665 N SER A 94 9411 7036 5629 6 284 1552 N ATOM 666 CA SER A 94 38.522 55.591 139.282 1.00 58.85 C ANISOU 666 CA SER A 94 9491 7145 5724 60 316 1587 C ATOM 667 C SER A 94 37.855 56.773 138.573 1.00 59.42 C ANISOU 667 C SER A 94 9527 7237 5811 79 352 1641 C ATOM 668 O SER A 94 36.661 57.047 138.786 1.00 59.58 O ANISOU 668 O SER A 94 9517 7304 5816 100 370 1708 O ATOM 669 CB SER A 94 39.420 56.112 140.406 1.00 58.92 C ANISOU 669 CB SER A 94 9530 7101 5754 109 325 1518 C ATOM 670 OG SER A 94 40.054 55.047 141.093 1.00 59.21 O ANISOU 670 OG SER A 94 9599 7120 5778 96 289 1471 O ATOM 671 N ILE A 95 38.627 57.437 137.711 1.00 59.81 N ANISOU 671 N ILE A 95 9580 7254 5890 72 362 1614 N ATOM 672 CA ILE A 95 38.181 58.652 137.018 1.00 60.18 C ANISOU 672 CA ILE A 95 9601 7308 5957 91 395 1661 C ATOM 673 C ILE A 95 36.995 58.314 136.113 1.00 60.47 C ANISOU 673 C ILE A 95 9598 7412 5965 58 389 1747 C ATOM 674 O ILE A 95 35.939 58.978 136.171 1.00 60.61 O ANISOU 674 O ILE A 95 9582 7462 5981 91 412 1813 O ATOM 675 CB ILE A 95 39.330 59.288 136.190 1.00 60.35 C ANISOU 675 CB ILE A 95 9634 7282 6012 77 402 1618 C ATOM 676 CG1 ILE A 95 40.485 59.719 137.107 1.00 60.36 C ANISOU 676 CG1 ILE A 95 9668 7218 6045 108 407 1536 C ATOM 677 CG2 ILE A 95 38.830 60.497 135.390 1.00 60.94 C ANISOU 677 CG2 ILE A 95 9684 7364 6107 91 433 1677 C ATOM 678 CD1 ILE A 95 41.817 59.845 136.399 1.00 60.39 C ANISOU 678 CD1 ILE A 95 9685 7185 6075 77 403 1479 C ATOM 679 N LEU A 96 37.171 57.262 135.310 1.00 60.52 N ANISOU 679 N LEU A 96 9608 7439 5947 -4 356 1743 N ATOM 680 CA LEU A 96 36.130 56.801 134.381 1.00 61.07 C ANISOU 680 CA LEU A 96 9643 7574 5984 -47 341 1818 C ATOM 681 C LEU A 96 34.882 56.284 135.120 1.00 61.63 C ANISOU 681 C LEU A 96 9689 7697 6028 -41 334 1876 C ATOM 682 O LEU A 96 33.730 56.573 134.718 1.00 61.85 O ANISOU 682 O LEU A 96 9673 7782 6043 -42 342 1956 O ATOM 683 CB LEU A 96 36.695 55.731 133.442 1.00 60.81 C ANISOU 683 CB LEU A 96 9628 7544 5929 -116 305 1787 C ATOM 684 CG LEU A 96 37.845 56.183 132.530 1.00 60.71 C ANISOU 684 CG LEU A 96 9632 7497 5938 -129 314 1739 C ATOM 685 CD1 LEU A 96 38.516 54.995 131.858 1.00 60.61 C ANISOU 685 CD1 LEU A 96 9643 7482 5902 -186 280 1690 C ATOM 686 CD2 LEU A 96 37.363 57.190 131.491 1.00 61.00 C ANISOU 686 CD2 LEU A 96 9637 7562 5977 -131 336 1802 C ATOM 687 N ALA A 97 35.120 55.548 136.211 1.00 61.94 N ANISOU 687 N ALA A 97 9756 7720 6059 -35 320 1837 N ATOM 688 CA ALA A 97 34.039 55.131 137.115 1.00 62.25 C ANISOU 688 CA ALA A 97 9773 7805 6073 -24 320 1888 C ATOM 689 C ALA A 97 33.254 56.329 137.668 1.00 62.55 C ANISOU 689 C ALA A 97 9777 7864 6123 45 366 1932 C ATOM 690 O ALA A 97 32.023 56.303 137.690 1.00 62.89 O ANISOU 690 O ALA A 97 9775 7972 6147 46 373 2009 O ATOM 691 CB ALA A 97 34.588 54.281 138.254 1.00 62.14 C ANISOU 691 CB ALA A 97 9799 7760 6049 -22 301 1834 C ATOM 692 N LEU A 98 33.964 57.372 138.098 1.00 62.63 N ANISOU 692 N LEU A 98 9809 7820 6167 101 395 1884 N ATOM 693 CA LEU A 98 33.307 58.611 138.558 1.00 63.15 C ANISOU 693 CA LEU A 98 9849 7893 6250 173 440 1918 C ATOM 694 C LEU A 98 32.541 59.326 137.433 1.00 63.22 C ANISOU 694 C LEU A 98 9813 7938 6270 173 453 1992 C ATOM 695 O LEU A 98 31.395 59.785 137.634 1.00 63.66 O ANISOU 695 O LEU A 98 9824 8043 6320 212 477 2059 O ATOM 696 CB LEU A 98 34.321 59.566 139.204 1.00 63.12 C ANISOU 696 CB LEU A 98 9886 7814 6283 227 463 1843 C ATOM 697 CG LEU A 98 34.826 59.116 140.588 1.00 63.01 C ANISOU 697 CG LEU A 98 9909 7775 6256 249 458 1781 C ATOM 698 CD1 LEU A 98 36.159 59.770 140.925 1.00 62.88 C ANISOU 698 CD1 LEU A 98 9938 7678 6275 273 463 1694 C ATOM 699 CD2 LEU A 98 33.804 59.402 141.680 1.00 63.29 C ANISOU 699 CD2 LEU A 98 9924 7851 6270 305 488 1817 C ATOM 700 N LEU A 99 33.171 59.411 136.259 1.00 62.93 N ANISOU 700 N LEU A 99 9786 7880 6245 132 439 1981 N ATOM 701 CA LEU A 99 32.510 59.987 135.077 1.00 63.38 C ANISOU 701 CA LEU A 99 9803 7973 6306 122 444 2054 C ATOM 702 C LEU A 99 31.218 59.239 134.713 1.00 63.76 C ANISOU 702 C LEU A 99 9800 8109 6314 86 424 2137 C ATOM 703 O LEU A 99 30.198 59.875 134.390 1.00 63.87 O ANISOU 703 O LEU A 99 9766 8170 6332 113 440 2214 O ATOM 704 CB LEU A 99 33.462 60.032 133.877 1.00 63.19 C ANISOU 704 CB LEU A 99 9799 7917 6290 74 429 2026 C ATOM 705 CG LEU A 99 32.942 60.678 132.584 1.00 63.64 C ANISOU 705 CG LEU A 99 9822 8007 6349 60 433 2098 C ATOM 706 CD1 LEU A 99 32.567 62.145 132.743 1.00 64.04 C ANISOU 706 CD1 LEU A 99 9857 8036 6438 133 472 2135 C ATOM 707 CD2 LEU A 99 33.991 60.550 131.491 1.00 63.49 C ANISOU 707 CD2 LEU A 99 9831 7962 6331 6 418 2060 C ATOM 708 N ALA A 100 31.260 57.903 134.778 1.00 63.93 N ANISOU 708 N ALA A 100 9834 8152 6303 25 387 2122 N ATOM 709 CA ALA A 100 30.036 57.092 134.610 1.00 64.40 C ANISOU 709 CA ALA A 100 9849 8294 6326 -15 364 2196 C ATOM 710 C ALA A 100 28.933 57.488 135.614 1.00 65.29 C ANISOU 710 C ALA A 100 9917 8452 6435 43 395 2251 C ATOM 711 O ALA A 100 27.761 57.688 135.233 1.00 65.87 O ANISOU 711 O ALA A 100 9931 8597 6499 44 398 2336 O ATOM 712 CB ALA A 100 30.353 55.607 134.727 1.00 63.97 C ANISOU 712 CB ALA A 100 9824 8238 6241 -84 320 2162 C ATOM 713 N ILE A 101 29.326 57.620 136.885 1.00 65.71 N ANISOU 713 N ILE A 101 9999 8468 6498 92 417 2200 N ATOM 714 CA ILE A 101 28.414 58.055 137.954 1.00 66.78 C ANISOU 714 CA ILE A 101 10100 8643 6628 157 454 2237 C ATOM 715 C ILE A 101 27.828 59.433 137.649 1.00 67.73 C ANISOU 715 C ILE A 101 10181 8774 6778 226 493 2284 C ATOM 716 O ILE A 101 26.614 59.631 137.795 1.00 69.01 O ANISOU 716 O ILE A 101 10282 9007 6929 253 511 2359 O ATOM 717 CB ILE A 101 29.101 58.080 139.344 1.00 66.94 C ANISOU 717 CB ILE A 101 10167 8613 6651 202 472 2163 C ATOM 718 CG1 ILE A 101 29.408 56.654 139.815 1.00 66.75 C ANISOU 718 CG1 ILE A 101 10173 8593 6595 140 433 2137 C ATOM 719 CG2 ILE A 101 28.225 58.774 140.383 1.00 67.55 C ANISOU 719 CG2 ILE A 101 10212 8727 6725 281 519 2195 C ATOM 720 CD1 ILE A 101 30.346 56.568 141.006 1.00 66.64 C ANISOU 720 CD1 ILE A 101 10215 8520 6582 172 439 2055 C ATOM 721 N ALA A 102 28.682 60.374 137.236 1.00 67.85 N ANISOU 721 N ALA A 102 10229 8719 6831 254 507 2242 N ATOM 722 CA ALA A 102 28.213 61.727 136.865 1.00 68.48 C ANISOU 722 CA ALA A 102 10279 8794 6944 320 541 2285 C ATOM 723 C ALA A 102 27.164 61.716 135.742 1.00 68.64 C ANISOU 723 C ALA A 102 10236 8890 6953 291 526 2384 C ATOM 724 O ALA A 102 26.089 62.328 135.883 1.00 68.63 O ANISOU 724 O ALA A 102 10179 8938 6958 347 552 2453 O ATOM 725 CB ALA A 102 29.384 62.615 136.473 1.00 68.60 C ANISOU 725 CB ALA A 102 10345 8719 7001 336 550 2226 C ATOM 726 N VAL A 103 27.465 61.012 134.647 1.00 68.79 N ANISOU 726 N VAL A 103 10260 8921 6954 208 484 2391 N ATOM 727 CA VAL A 103 26.501 60.909 133.535 1.00 69.87 C ANISOU 727 CA VAL A 103 10339 9134 7073 171 462 2484 C ATOM 728 C VAL A 103 25.238 60.126 133.924 1.00 70.65 C ANISOU 728 C VAL A 103 10378 9328 7137 152 451 2550 C ATOM 729 O VAL A 103 24.137 60.458 133.455 1.00 71.16 O ANISOU 729 O VAL A 103 10375 9462 7198 165 452 2639 O ATOM 730 CB VAL A 103 27.117 60.366 132.211 1.00 69.48 C ANISOU 730 CB VAL A 103 10312 9079 7006 85 420 2473 C ATOM 731 CG1 VAL A 103 28.282 61.237 131.769 1.00 69.21 C ANISOU 731 CG1 VAL A 103 10326 8962 7007 104 436 2420 C ATOM 732 CG2 VAL A 103 27.555 58.914 132.315 1.00 69.12 C ANISOU 732 CG2 VAL A 103 10298 9036 6925 6 381 2425 C ATOM 733 N ASP A 104 25.384 59.109 134.783 1.00 71.51 N ANISOU 733 N ASP A 104 10508 9440 7222 122 440 2512 N ATOM 734 CA ASP A 104 24.201 58.420 135.330 1.00 73.04 C ANISOU 734 CA ASP A 104 10646 9721 7385 108 435 2575 C ATOM 735 C ASP A 104 23.328 59.371 136.163 1.00 74.62 C ANISOU 735 C ASP A 104 10794 9955 7600 205 488 2618 C ATOM 736 O ASP A 104 22.101 59.390 136.003 1.00 75.38 O ANISOU 736 O ASP A 104 10815 10140 7685 210 491 2706 O ATOM 737 CB ASP A 104 24.582 57.201 136.174 1.00 72.53 C ANISOU 737 CB ASP A 104 10619 9644 7292 61 415 2527 C ATOM 738 CG ASP A 104 23.365 56.394 136.607 1.00 72.72 C ANISOU 738 CG ASP A 104 10585 9763 7283 28 404 2599 C ATOM 739 OD1 ASP A 104 22.669 55.845 135.727 1.00 72.72 O ANISOU 739 OD1 ASP A 104 10543 9824 7263 -38 368 2663 O ATOM 740 OD2 ASP A 104 23.095 56.316 137.824 1.00 73.01 O ANISOU 740 OD2 ASP A 104 10615 9813 7310 67 433 2595 O ATOM 741 N ARG A 105 23.965 60.147 137.043 1.00 75.52 N ANISOU 741 N ARG A 105 10951 10001 7741 282 529 2554 N ATOM 742 CA ARG A 105 23.266 61.203 137.793 1.00 76.99 C ANISOU 742 CA ARG A 105 11100 10206 7946 387 583 2581 C ATOM 743 C ARG A 105 22.609 62.239 136.872 1.00 78.49 C ANISOU 743 C ARG A 105 11238 10417 8164 429 595 2653 C ATOM 744 O ARG A 105 21.492 62.687 137.147 1.00 79.60 O ANISOU 744 O ARG A 105 11311 10625 8308 487 624 2720 O ATOM 745 CB ARG A 105 24.213 61.921 138.766 1.00 77.05 C ANISOU 745 CB ARG A 105 11173 10122 7978 457 619 2489 C ATOM 746 CG ARG A 105 24.514 61.172 140.056 1.00 76.91 C ANISOU 746 CG ARG A 105 11189 10102 7931 452 625 2435 C ATOM 747 CD ARG A 105 23.267 60.960 140.910 1.00 77.59 C ANISOU 747 CD ARG A 105 11212 10282 7987 486 654 2495 C ATOM 748 NE ARG A 105 22.785 59.581 140.877 1.00 77.55 N ANISOU 748 NE ARG A 105 11180 10347 7939 398 616 2537 N ATOM 749 CZ ARG A 105 21.724 59.134 141.548 1.00 78.24 C ANISOU 749 CZ ARG A 105 11209 10524 7992 401 633 2596 C ATOM 750 NH1 ARG A 105 20.995 59.948 142.313 1.00 79.27 N ANISOU 750 NH1 ARG A 105 11298 10695 8126 495 689 2619 N ATOM 751 NH2 ARG A 105 21.386 57.850 141.451 1.00 78.30 N ANISOU 751 NH2 ARG A 105 11200 10584 7965 310 593 2632 N ATOM 752 N TYR A 106 23.303 62.622 135.797 1.00 79.13 N ANISOU 752 N TYR A 106 11350 10446 8267 402 574 2640 N ATOM 753 CA TYR A 106 22.718 63.513 134.784 1.00 80.49 C ANISOU 753 CA TYR A 106 11478 10641 8464 430 576 2715 C ATOM 754 C TYR A 106 21.476 62.912 134.124 1.00 81.72 C ANISOU 754 C TYR A 106 11550 10911 8589 383 547 2817 C ATOM 755 O TYR A 106 20.402 63.525 134.143 1.00 82.26 O ANISOU 755 O TYR A 106 11548 11038 8668 443 568 2893 O ATOM 756 CB TYR A 106 23.753 63.864 133.713 1.00 80.51 C ANISOU 756 CB TYR A 106 11532 10572 8486 393 554 2683 C ATOM 757 CG TYR A 106 23.224 64.744 132.600 1.00 81.37 C ANISOU 757 CG TYR A 106 11600 10700 8615 413 551 2764 C ATOM 758 CD1 TYR A 106 22.955 66.097 132.823 1.00 82.06 C ANISOU 758 CD1 TYR A 106 11677 10753 8749 514 592 2786 C ATOM 759 CD2 TYR A 106 22.993 64.227 131.322 1.00 81.45 C ANISOU 759 CD2 TYR A 106 11586 10764 8598 332 505 2818 C ATOM 760 CE1 TYR A 106 22.470 66.909 131.808 1.00 82.64 C ANISOU 760 CE1 TYR A 106 11715 10841 8843 536 586 2865 C ATOM 761 CE2 TYR A 106 22.512 65.033 130.299 1.00 82.13 C ANISOU 761 CE2 TYR A 106 11634 10870 8698 350 499 2896 C ATOM 762 CZ TYR A 106 22.252 66.372 130.547 1.00 82.78 C ANISOU 762 CZ TYR A 106 11706 10916 8830 453 539 2922 C ATOM 763 OH TYR A 106 21.773 67.176 129.542 1.00 83.71 O ANISOU 763 OH TYR A 106 11788 11052 8964 473 531 3004 O ATOM 764 N LEU A 107 21.632 61.712 133.556 1.00 82.78 N ANISOU 764 N LEU A 107 11692 11075 8685 277 496 2816 N ATOM 765 CA LEU A 107 20.543 61.055 132.806 1.00 84.08 C ANISOU 765 CA LEU A 107 11784 11345 8817 214 458 2908 C ATOM 766 C LEU A 107 19.231 60.887 133.588 1.00 86.20 C ANISOU 766 C LEU A 107 11970 11709 9073 247 478 2976 C ATOM 767 O LEU A 107 18.150 61.053 133.017 1.00 86.95 O ANISOU 767 O LEU A 107 11985 11889 9163 248 467 3070 O ATOM 768 CB LEU A 107 20.997 59.694 132.269 1.00 83.19 C ANISOU 768 CB LEU A 107 11705 11237 8663 95 402 2879 C ATOM 769 CG LEU A 107 21.990 59.729 131.104 1.00 82.57 C ANISOU 769 CG LEU A 107 11683 11103 8587 44 372 2840 C ATOM 770 CD1 LEU A 107 22.652 58.370 130.930 1.00 82.21 C ANISOU 770 CD1 LEU A 107 11688 11041 8506 -54 328 2782 C ATOM 771 CD2 LEU A 107 21.309 60.164 129.814 1.00 83.03 C ANISOU 771 CD2 LEU A 107 11688 11219 8638 26 349 2926 C ATOM 772 N ARG A 108 19.329 60.566 134.881 1.00 87.85 N ANISOU 772 N ARG A 108 12197 11907 9274 274 507 2932 N ATOM 773 CA ARG A 108 18.141 60.381 135.735 1.00 89.80 C ANISOU 773 CA ARG A 108 12367 12247 9504 306 533 2992 C ATOM 774 C ARG A 108 17.262 61.625 135.765 1.00 91.58 C ANISOU 774 C ARG A 108 12524 12510 9761 414 578 3055 C ATOM 775 O ARG A 108 16.067 61.563 135.461 1.00 92.77 O ANISOU 775 O ARG A 108 12582 12764 9902 411 572 3150 O ATOM 776 CB ARG A 108 18.548 60.021 137.169 1.00 89.93 C ANISOU 776 CB ARG A 108 12426 12233 9508 332 565 2924 C ATOM 777 CG ARG A 108 19.109 58.623 137.320 1.00 89.63 C ANISOU 777 CG ARG A 108 12437 12182 9435 228 521 2882 C ATOM 778 CD ARG A 108 19.816 58.455 138.649 1.00 89.60 C ANISOU 778 CD ARG A 108 12494 12122 9424 261 550 2801 C ATOM 779 NE ARG A 108 18.889 58.505 139.781 1.00 90.36 N ANISOU 779 NE ARG A 108 12536 12292 9503 314 594 2840 N ATOM 780 CZ ARG A 108 18.112 57.493 140.183 1.00 91.35 C ANISOU 780 CZ ARG A 108 12616 12501 9589 256 580 2892 C ATOM 781 NH1 ARG A 108 18.110 56.315 139.557 1.00 91.61 N ANISOU 781 NH1 ARG A 108 12655 12553 9600 141 519 2913 N ATOM 782 NH2 ARG A 108 17.315 57.659 141.234 1.00 91.96 N ANISOU 782 NH2 ARG A 108 12643 12646 9650 312 628 2925 N ATOM 783 N VAL A 109 17.873 62.748 136.133 1.00 92.48 N ANISOU 783 N VAL A 109 12684 12539 9914 507 620 3002 N ATOM 784 CA VAL A 109 17.181 64.037 136.178 1.00 94.10 C ANISOU 784 CA VAL A 109 12839 12758 10157 620 664 3049 C ATOM 785 C VAL A 109 16.881 64.609 134.777 1.00 94.74 C ANISOU 785 C VAL A 109 12885 12851 10260 613 635 3121 C ATOM 786 O VAL A 109 15.874 65.301 134.599 1.00 95.69 O ANISOU 786 O VAL A 109 12928 13029 10398 680 653 3200 O ATOM 787 CB VAL A 109 17.935 65.065 137.069 1.00 94.49 C ANISOU 787 CB VAL A 109 12954 12703 10242 722 718 2965 C ATOM 788 CG1 VAL A 109 19.272 65.504 136.463 1.00 93.84 C ANISOU 788 CG1 VAL A 109 12964 12502 10189 702 700 2895 C ATOM 789 CG2 VAL A 109 17.049 66.267 137.360 1.00 95.71 C ANISOU 789 CG2 VAL A 109 13052 12882 10431 848 769 3013 C ATOM 790 N LYS A 110 17.738 64.320 133.794 1.00 94.63 N ANISOU 790 N LYS A 110 12926 12786 10241 533 590 3094 N ATOM 791 CA LYS A 110 17.555 64.851 132.435 1.00 95.30 C ANISOU 791 CA LYS A 110 12987 12880 10340 519 560 3158 C ATOM 792 C LYS A 110 16.438 64.144 131.658 1.00 96.02 C ANISOU 792 C LYS A 110 12990 13095 10397 452 515 3259 C ATOM 793 O LYS A 110 15.623 64.811 131.023 1.00 96.78 O ANISOU 793 O LYS A 110 13020 13242 10508 491 511 3346 O ATOM 794 CB LYS A 110 18.873 64.794 131.646 1.00 94.75 C ANISOU 794 CB LYS A 110 13005 12720 10273 457 531 3094 C ATOM 795 CG LYS A 110 18.834 65.406 130.248 1.00 94.88 C ANISOU 795 CG LYS A 110 13011 12738 10302 443 503 3154 C ATOM 796 CD LYS A 110 18.600 66.907 130.264 1.00 95.52 C ANISOU 796 CD LYS A 110 13078 12777 10437 558 543 3188 C ATOM 797 CE LYS A 110 18.512 67.450 128.846 1.00 96.20 C ANISOU 797 CE LYS A 110 13150 12871 10530 537 510 3259 C ATOM 798 NZ LYS A 110 18.288 68.921 128.817 1.00 97.05 N ANISOU 798 NZ LYS A 110 13249 12930 10694 648 545 3297 N ATOM 799 N ILE A 111 16.413 62.810 131.698 1.00 96.37 N ANISOU 799 N ILE A 111 13035 13184 10394 349 477 3248 N ATOM 800 CA ILE A 111 15.418 62.014 130.954 1.00 97.37 C ANISOU 800 CA ILE A 111 13085 13426 10484 267 427 3337 C ATOM 801 C ILE A 111 14.740 60.967 131.859 1.00 98.04 C ANISOU 801 C ILE A 111 13127 13586 10537 228 427 3350 C ATOM 802 O ILE A 111 14.882 59.755 131.644 1.00 98.22 O ANISOU 802 O ILE A 111 13168 13629 10522 118 380 3336 O ATOM 803 CB ILE A 111 16.028 61.369 129.677 1.00 96.99 C ANISOU 803 CB ILE A 111 13081 13362 10407 155 363 3324 C ATOM 804 CG1 ILE A 111 17.314 60.583 129.982 1.00 96.35 C ANISOU 804 CG1 ILE A 111 13102 13193 10311 95 353 3212 C ATOM 805 CG2 ILE A 111 16.325 62.447 128.641 1.00 96.99 C ANISOU 805 CG2 ILE A 111 13093 13323 10433 191 360 3348 C ATOM 806 CD1 ILE A 111 17.716 59.616 128.882 1.00 96.25 C ANISOU 806 CD1 ILE A 111 13123 13188 10259 -25 289 3199 C ATOM 807 N PRO A 112 13.982 61.437 132.873 1.00 99.23 N ANISOU 807 N PRO A 112 13219 13780 10702 318 480 3380 N ATOM 808 CA PRO A 112 13.370 60.522 133.850 1.00100.41 C ANISOU 808 CA PRO A 112 13327 14000 10820 288 489 3393 C ATOM 809 C PRO A 112 12.339 59.541 133.272 1.00102.04 C ANISOU 809 C PRO A 112 13452 14327 10991 187 436 3483 C ATOM 810 O PRO A 112 12.228 58.418 133.771 1.00102.16 O ANISOU 810 O PRO A 112 13469 14373 10971 110 417 3474 O ATOM 811 CB PRO A 112 12.716 61.471 134.866 1.00100.58 C ANISOU 811 CB PRO A 112 13296 14050 10868 420 562 3414 C ATOM 812 CG PRO A 112 12.485 62.732 134.119 1.00101.14 C ANISOU 812 CG PRO A 112 13338 14108 10980 502 573 3457 C ATOM 813 CD PRO A 112 13.604 62.840 133.128 1.00100.08 C ANISOU 813 CD PRO A 112 13292 13877 10855 453 534 3407 C ATOM 814 N LEU A 113 11.608 59.951 132.235 1.00103.88 N ANISOU 814 N LEU A 113 13614 14624 11229 185 408 3568 N ATOM 815 CA LEU A 113 10.600 59.084 131.606 1.00105.42 C ANISOU 815 CA LEU A 113 13727 14936 11390 87 351 3657 C ATOM 816 C LEU A 113 11.230 57.910 130.849 1.00105.72 C ANISOU 816 C LEU A 113 13831 14945 11391 -53 280 3619 C ATOM 817 O LEU A 113 10.757 56.777 130.964 1.00106.77 O ANISOU 817 O LEU A 113 13938 15140 11490 -150 244 3644 O ATOM 818 CB LEU A 113 9.699 59.892 130.668 1.00106.56 C ANISOU 818 CB LEU A 113 13780 15156 11551 126 337 3758 C ATOM 819 CG LEU A 113 8.838 60.971 131.341 1.00107.55 C ANISOU 819 CG LEU A 113 13819 15330 11712 264 402 3814 C ATOM 820 CD1 LEU A 113 8.265 61.932 130.306 1.00108.43 C ANISOU 820 CD1 LEU A 113 13869 15480 11850 316 386 3897 C ATOM 821 CD2 LEU A 113 7.725 60.353 132.177 1.00108.05 C ANISOU 821 CD2 LEU A 113 13784 15513 11755 252 419 3873 C ATOM 822 N ARG A 114 12.295 58.188 130.096 1.00105.17 N ANISOU 822 N ARG A 114 13848 14781 11328 -64 263 3557 N ATOM 823 CA ARG A 114 13.012 57.166 129.313 1.00104.67 C ANISOU 823 CA ARG A 114 13856 14681 11230 -187 200 3509 C ATOM 824 C ARG A 114 14.245 56.553 130.023 1.00103.32 C ANISOU 824 C ARG A 114 13795 14404 11056 -209 211 3392 C ATOM 825 O ARG A 114 14.904 55.661 129.460 1.00102.23 O ANISOU 825 O ARG A 114 13721 14228 10892 -304 163 3343 O ATOM 826 CB ARG A 114 13.422 57.752 127.952 1.00104.97 C ANISOU 826 CB ARG A 114 13919 14693 11270 -196 170 3516 C ATOM 827 CG ARG A 114 12.251 58.070 127.034 1.00105.70 C ANISOU 827 CG ARG A 114 13911 14896 11353 -206 137 3632 C ATOM 828 CD ARG A 114 12.649 58.980 125.880 1.00106.09 C ANISOU 828 CD ARG A 114 13981 14913 11412 -180 125 3645 C ATOM 829 NE ARG A 114 13.631 58.373 124.973 1.00105.59 N ANISOU 829 NE ARG A 114 14006 14794 11316 -273 80 3581 N ATOM 830 CZ ARG A 114 14.942 58.648 124.917 1.00105.28 C ANISOU 830 CZ ARG A 114 14067 14644 11290 -256 101 3488 C ATOM 831 NH1 ARG A 114 15.522 59.544 125.723 1.00105.25 N ANISOU 831 NH1 ARG A 114 14096 14560 11333 -153 164 3442 N ATOM 832 NH2 ARG A 114 15.698 58.013 124.023 1.00104.92 N ANISOU 832 NH2 ARG A 114 14087 14567 11208 -346 57 3439 N ATOM 833 N TYR A 115 14.545 57.003 131.249 1.00102.76 N ANISOU 833 N TYR A 115 13744 14288 11011 -121 273 3348 N ATOM 834 CA TYR A 115 15.735 56.536 131.980 1.00101.98 C ANISOU 834 CA TYR A 115 13746 14088 10912 -130 285 3240 C ATOM 835 C TYR A 115 15.844 55.013 132.064 1.00102.78 C ANISOU 835 C TYR A 115 13878 14197 10975 -248 235 3218 C ATOM 836 O TYR A 115 16.879 54.453 131.707 1.00102.24 O ANISOU 836 O TYR A 115 13895 14052 10897 -303 205 3142 O ATOM 837 CB TYR A 115 15.791 57.117 133.401 1.00101.35 C ANISOU 837 CB TYR A 115 13669 13984 10855 -27 355 3209 C ATOM 838 CG TYR A 115 16.950 56.584 134.228 1.00 99.95 C ANISOU 838 CG TYR A 115 13589 13713 10674 -38 363 3104 C ATOM 839 CD1 TYR A 115 18.268 56.919 133.911 1.00 98.92 C ANISOU 839 CD1 TYR A 115 13549 13473 10563 -27 363 3016 C ATOM 840 CD2 TYR A 115 16.734 55.732 135.314 1.00 99.03 C ANISOU 840 CD2 TYR A 115 13471 13619 10534 -63 370 3096 C ATOM 841 CE1 TYR A 115 19.335 56.430 134.655 1.00 97.60 C ANISOU 841 CE1 TYR A 115 13465 13224 10394 -36 367 2921 C ATOM 842 CE2 TYR A 115 17.796 55.238 136.061 1.00 98.15 C ANISOU 842 CE2 TYR A 115 13449 13423 10419 -72 373 3004 C ATOM 843 CZ TYR A 115 19.094 55.592 135.729 1.00 97.25 C ANISOU 843 CZ TYR A 115 13421 13203 10326 -57 371 2916 C ATOM 844 OH TYR A 115 20.153 55.111 136.464 1.00 96.12 O ANISOU 844 OH TYR A 115 13360 12980 10181 -64 372 2826 O ATOM 845 N LYS A 116 14.783 54.357 132.534 1.00104.98 N ANISOU 845 N LYS A 116 14087 14568 11232 -287 226 3286 N ATOM 846 CA LYS A 116 14.806 52.903 132.744 1.00105.75 C ANISOU 846 CA LYS A 116 14212 14671 11297 -398 179 3272 C ATOM 847 C LYS A 116 14.982 52.101 131.453 1.00105.58 C ANISOU 847 C LYS A 116 14219 14646 11249 -513 103 3269 C ATOM 848 O LYS A 116 15.668 51.078 131.456 1.00105.32 O ANISOU 848 O LYS A 116 14261 14556 11199 -588 67 3208 O ATOM 849 CB LYS A 116 13.558 52.423 133.502 1.00107.38 C ANISOU 849 CB LYS A 116 14329 14984 11486 -419 186 3356 C ATOM 850 CG LYS A 116 13.587 52.727 134.994 1.00108.52 C ANISOU 850 CG LYS A 116 14473 15120 11640 -335 254 3335 C ATOM 851 CD LYS A 116 12.695 51.777 135.791 1.00110.19 C ANISOU 851 CD LYS A 116 14630 15413 11822 -394 248 3394 C ATOM 852 CE LYS A 116 12.936 51.899 137.288 1.00110.78 C ANISOU 852 CE LYS A 116 14726 15466 11896 -324 309 3357 C ATOM 853 NZ LYS A 116 12.498 53.220 137.822 1.00111.75 N ANISOU 853 NZ LYS A 116 14792 15626 12042 -189 384 3379 N ATOM 854 N MET A 117 14.376 52.561 130.359 1.00105.93 N ANISOU 854 N MET A 117 14206 14752 11290 -524 79 3334 N ATOM 855 CA MET A 117 14.598 51.935 129.049 1.00105.68 C ANISOU 855 CA MET A 117 14206 14717 11229 -625 10 3326 C ATOM 856 C MET A 117 15.973 52.280 128.453 1.00101.96 C ANISOU 856 C MET A 117 13833 14139 10766 -606 13 3232 C ATOM 857 O MET A 117 16.542 51.460 127.728 1.00101.83 O ANISOU 857 O MET A 117 13878 14087 10724 -692 -36 3183 O ATOM 858 CB MET A 117 13.455 52.237 128.059 1.00109.05 C ANISOU 858 CB MET A 117 14537 15254 11641 -652 -23 3431 C ATOM 859 CG MET A 117 13.306 53.680 127.592 1.00111.63 C ANISOU 859 CG MET A 117 14822 15596 11996 -551 12 3471 C ATOM 860 SD MET A 117 12.115 53.863 126.238 1.00116.10 S ANISOU 860 SD MET A 117 15289 16286 12537 -601 -44 3589 S ATOM 861 CE MET A 117 10.563 53.561 127.088 1.00116.79 C ANISOU 861 CE MET A 117 15248 16501 12624 -604 -37 3694 C ATOM 862 N VAL A 118 16.505 53.470 128.754 1.00 98.33 N ANISOU 862 N VAL A 118 13387 13628 10343 -497 71 3204 N ATOM 863 CA VAL A 118 17.853 53.855 128.274 1.00 94.91 C ANISOU 863 CA VAL A 118 13043 13094 9922 -477 79 3115 C ATOM 864 C VAL A 118 18.974 53.138 129.045 1.00 91.09 C ANISOU 864 C VAL A 118 12652 12516 9442 -491 85 3010 C ATOM 865 O VAL A 118 19.718 52.353 128.461 1.00 89.50 O ANISOU 865 O VAL A 118 12516 12270 9220 -562 46 2950 O ATOM 866 CB VAL A 118 18.066 55.398 128.311 1.00 94.75 C ANISOU 866 CB VAL A 118 13011 13046 9944 -361 135 3123 C ATOM 867 CG1 VAL A 118 19.520 55.777 128.031 1.00 93.40 C ANISOU 867 CG1 VAL A 118 12933 12766 9789 -340 150 3027 C ATOM 868 CG2 VAL A 118 17.146 56.095 127.311 1.00 95.41 C ANISOU 868 CG2 VAL A 118 13017 13209 10023 -352 120 3221 C ATOM 869 N VAL A 119 19.095 53.425 130.341 1.00 88.47 N ANISOU 869 N VAL A 119 12324 12156 9135 -419 135 2987 N ATOM 870 CA VAL A 119 20.189 52.904 131.180 1.00 86.22 C ANISOU 870 CA VAL A 119 12123 11780 8857 -416 145 2889 C ATOM 871 C VAL A 119 19.834 51.528 131.759 1.00 85.55 C ANISOU 871 C VAL A 119 12044 11717 8744 -495 110 2894 C ATOM 872 O VAL A 119 19.203 51.434 132.814 1.00 84.78 O ANISOU 872 O VAL A 119 11908 11658 8646 -470 135 2930 O ATOM 873 CB VAL A 119 20.540 53.889 132.323 1.00 85.55 C ANISOU 873 CB VAL A 119 12046 11651 8807 -302 213 2858 C ATOM 874 CG1 VAL A 119 21.683 53.347 133.180 1.00 84.90 C ANISOU 874 CG1 VAL A 119 12049 11480 8730 -301 218 2759 C ATOM 875 CG2 VAL A 119 20.889 55.262 131.758 1.00 85.32 C ANISOU 875 CG2 VAL A 119 12015 11591 8809 -228 245 2855 C ATOM 876 N THR A 120 20.251 50.471 131.061 1.00 85.16 N ANISOU 876 N THR A 120 12044 11642 8670 -590 53 2859 N ATOM 877 CA THR A 120 19.956 49.090 131.456 1.00 84.40 C ANISOU 877 CA THR A 120 11962 11556 8549 -677 10 2863 C ATOM 878 C THR A 120 21.185 48.410 132.071 1.00 83.39 C ANISOU 878 C THR A 120 11931 11325 8427 -681 5 2762 C ATOM 879 O THR A 120 22.326 48.799 131.769 1.00 82.59 O ANISOU 879 O THR A 120 11889 11147 8342 -646 18 2683 O ATOM 880 CB THR A 120 19.480 48.254 130.251 1.00 84.68 C ANISOU 880 CB THR A 120 11988 11634 8550 -788 -59 2895 C ATOM 881 OG1 THR A 120 20.486 48.248 129.230 1.00 84.31 O ANISOU 881 OG1 THR A 120 12009 11526 8499 -806 -79 2823 O ATOM 882 CG2 THR A 120 18.190 48.824 129.683 1.00 85.29 C ANISOU 882 CG2 THR A 120 11964 11823 8618 -790 -62 3003 C ATOM 883 N PRO A 121 20.959 47.382 132.923 1.00 83.43 N ANISOU 883 N PRO A 121 11949 11327 8420 -726 -13 2767 N ATOM 884 CA PRO A 121 22.047 46.631 133.562 1.00 83.17 C ANISOU 884 CA PRO A 121 12006 11201 8393 -733 -24 2680 C ATOM 885 C PRO A 121 23.167 46.197 132.613 1.00 83.28 C ANISOU 885 C PRO A 121 12098 11137 8407 -769 -59 2593 C ATOM 886 O PRO A 121 24.345 46.388 132.931 1.00 83.20 O ANISOU 886 O PRO A 121 12150 11045 8417 -720 -40 2509 O ATOM 887 CB PRO A 121 21.329 45.407 134.135 1.00 83.34 C ANISOU 887 CB PRO A 121 12019 11252 8392 -812 -61 2726 C ATOM 888 CG PRO A 121 19.967 45.900 134.451 1.00 83.75 C ANISOU 888 CG PRO A 121 11969 11413 8436 -798 -35 2831 C ATOM 889 CD PRO A 121 19.639 46.928 133.408 1.00 84.04 C ANISOU 889 CD PRO A 121 11954 11496 8479 -767 -22 2862 C ATOM 890 N ARG A 122 22.794 45.627 131.466 1.00 84.05 N ANISOU 890 N ARG A 122 12191 11263 8480 -852 -111 2614 N ATOM 891 CA ARG A 122 23.772 45.187 130.458 1.00 84.10 C ANISOU 891 CA ARG A 122 12268 11206 8478 -890 -144 2534 C ATOM 892 C ARG A 122 24.607 46.350 129.909 1.00 82.50 C ANISOU 892 C ARG A 122 12075 10975 8294 -818 -103 2489 C ATOM 893 O ARG A 122 25.836 46.231 129.767 1.00 82.22 O ANISOU 893 O ARG A 122 12107 10861 8270 -801 -101 2398 O ATOM 894 CB ARG A 122 23.097 44.403 129.320 1.00 85.84 C ANISOU 894 CB ARG A 122 12478 11473 8663 -995 -207 2569 C ATOM 895 CG ARG A 122 22.059 45.149 128.488 1.00 87.58 C ANISOU 895 CG ARG A 122 12615 11793 8867 -1004 -207 2656 C ATOM 896 CD ARG A 122 21.443 44.232 127.445 1.00 89.28 C ANISOU 896 CD ARG A 122 12829 12050 9043 -1116 -277 2684 C ATOM 897 NE ARG A 122 20.272 44.834 126.803 1.00 90.66 N ANISOU 897 NE ARG A 122 12912 12332 9201 -1131 -283 2783 N ATOM 898 CZ ARG A 122 20.301 45.780 125.858 1.00 91.47 C ANISOU 898 CZ ARG A 122 12988 12467 9297 -1101 -269 2798 C ATOM 899 NH1 ARG A 122 21.452 46.282 125.402 1.00 91.02 N ANISOU 899 NH1 ARG A 122 12988 12347 9248 -1055 -245 2721 N ATOM 900 NH2 ARG A 122 19.153 46.237 125.358 1.00 92.53 N ANISOU 900 NH2 ARG A 122 13036 12703 9416 -1116 -281 2896 N ATOM 901 N ARG A 123 23.942 47.472 129.631 1.00 81.31 N ANISOU 901 N ARG A 123 11856 10889 8149 -774 -71 2555 N ATOM 902 CA ARG A 123 24.627 48.682 129.156 1.00 79.77 C ANISOU 902 CA ARG A 123 11664 10669 7974 -705 -30 2526 C ATOM 903 C ARG A 123 25.554 49.253 130.230 1.00 77.71 C ANISOU 903 C ARG A 123 11438 10336 7751 -618 19 2463 C ATOM 904 O ARG A 123 26.685 49.661 129.924 1.00 77.19 O ANISOU 904 O ARG A 123 11419 10207 7702 -587 35 2391 O ATOM 905 CB ARG A 123 23.622 49.739 128.684 1.00 80.70 C ANISOU 905 CB ARG A 123 11700 10869 8092 -675 -10 2618 C ATOM 906 CG ARG A 123 23.058 49.449 127.308 1.00 82.07 C ANISOU 906 CG ARG A 123 11849 11103 8228 -751 -58 2662 C ATOM 907 CD ARG A 123 21.846 50.314 126.986 1.00 83.23 C ANISOU 907 CD ARG A 123 11904 11344 8374 -728 -47 2770 C ATOM 908 NE ARG A 123 21.108 49.777 125.845 1.00 84.08 N ANISOU 908 NE ARG A 123 11982 11522 8439 -817 -105 2822 N ATOM 909 CZ ARG A 123 19.904 50.191 125.438 1.00 84.90 C ANISOU 909 CZ ARG A 123 12000 11723 8532 -825 -116 2924 C ATOM 910 NH1 ARG A 123 19.260 51.172 126.071 1.00 85.05 N ANISOU 910 NH1 ARG A 123 11951 11780 8581 -742 -69 2988 N ATOM 911 NH2 ARG A 123 19.338 49.611 124.383 1.00 85.91 N ANISOU 911 NH2 ARG A 123 12111 11911 8618 -915 -175 2962 N ATOM 912 N ALA A 124 25.074 49.263 131.477 1.00 75.94 N ANISOU 912 N ALA A 124 11190 10125 7537 -582 42 2491 N ATOM 913 CA ALA A 124 25.906 49.646 132.621 1.00 74.23 C ANISOU 913 CA ALA A 124 11010 9842 7348 -508 82 2430 C ATOM 914 C ALA A 124 27.132 48.734 132.756 1.00 72.82 C ANISOU 914 C ALA A 124 10916 9579 7172 -536 55 2334 C ATOM 915 O ALA A 124 28.246 49.212 133.001 1.00 72.25 O ANISOU 915 O ALA A 124 10885 9439 7125 -484 80 2261 O ATOM 916 CB ALA A 124 25.088 49.627 133.901 1.00 74.55 C ANISOU 916 CB ALA A 124 11012 9923 7389 -478 105 2481 C ATOM 917 N ALA A 125 26.921 47.430 132.579 1.00 71.75 N ANISOU 917 N ALA A 125 10804 9446 7013 -618 2 2336 N ATOM 918 CA ALA A 125 28.015 46.450 132.600 1.00 70.47 C ANISOU 918 CA ALA A 125 10720 9202 6851 -648 -29 2248 C ATOM 919 C ALA A 125 29.024 46.685 131.469 1.00 68.98 C ANISOU 919 C ALA A 125 10568 8973 6667 -650 -33 2180 C ATOM 920 O ALA A 125 30.246 46.674 131.703 1.00 68.36 O ANISOU 920 O ALA A 125 10541 8821 6608 -617 -23 2095 O ATOM 921 CB ALA A 125 27.462 45.033 132.536 1.00 71.08 C ANISOU 921 CB ALA A 125 10813 9290 6902 -739 -88 2271 C ATOM 922 N VAL A 126 28.511 46.908 130.255 1.00 68.21 N ANISOU 922 N VAL A 126 10440 8926 6548 -689 -46 2219 N ATOM 923 CA VAL A 126 29.369 47.244 129.102 1.00 67.44 C ANISOU 923 CA VAL A 126 10369 8805 6448 -692 -43 2165 C ATOM 924 C VAL A 126 30.182 48.510 129.408 1.00 66.47 C ANISOU 924 C VAL A 126 10246 8647 6361 -605 12 2132 C ATOM 925 O VAL A 126 31.416 48.529 129.236 1.00 65.72 O ANISOU 925 O VAL A 126 10197 8491 6281 -587 21 2049 O ATOM 926 CB VAL A 126 28.549 47.415 127.795 1.00 67.70 C ANISOU 926 CB VAL A 126 10362 8913 6447 -744 -65 2227 C ATOM 927 CG1 VAL A 126 29.398 48.005 126.668 1.00 67.58 C ANISOU 927 CG1 VAL A 126 10367 8882 6427 -735 -50 2182 C ATOM 928 CG2 VAL A 126 27.952 46.079 127.353 1.00 68.03 C ANISOU 928 CG2 VAL A 126 10418 8977 6452 -840 -128 2241 C ATOM 929 N ALA A 127 29.484 49.545 129.882 1.00 66.14 N ANISOU 929 N ALA A 127 10150 8644 6335 -551 50 2196 N ATOM 930 CA ALA A 127 30.128 50.792 130.307 1.00 65.59 C ANISOU 930 CA ALA A 127 10079 8538 6303 -467 103 2170 C ATOM 931 C ALA A 127 31.228 50.543 131.343 1.00 65.11 C ANISOU 931 C ALA A 127 10071 8400 6268 -430 114 2085 C ATOM 932 O ALA A 127 32.341 51.057 131.190 1.00 65.16 O ANISOU 932 O ALA A 127 10107 8353 6297 -398 134 2021 O ATOM 933 CB ALA A 127 29.102 51.776 130.851 1.00 65.71 C ANISOU 933 CB ALA A 127 10031 8603 6331 -413 138 2250 C ATOM 934 N ILE A 128 30.923 49.742 132.370 1.00 64.53 N ANISOU 934 N ILE A 128 10007 8322 6188 -438 98 2089 N ATOM 935 CA ILE A 128 31.927 49.372 133.378 1.00 63.76 C ANISOU 935 CA ILE A 128 9961 8154 6109 -408 99 2013 C ATOM 936 C ILE A 128 33.123 48.718 132.685 1.00 62.65 C ANISOU 936 C ILE A 128 9876 7957 5971 -439 73 1928 C ATOM 937 O ILE A 128 34.240 49.235 132.765 1.00 61.51 O ANISOU 937 O ILE A 128 9756 7761 5852 -398 95 1862 O ATOM 938 CB ILE A 128 31.347 48.443 134.483 1.00 64.68 C ANISOU 938 CB ILE A 128 10083 8281 6212 -425 78 2038 C ATOM 939 CG1 ILE A 128 30.393 49.228 135.392 1.00 65.22 C ANISOU 939 CG1 ILE A 128 10099 8398 6282 -374 117 2105 C ATOM 940 CG2 ILE A 128 32.453 47.820 135.342 1.00 64.39 C ANISOU 940 CG2 ILE A 128 10106 8169 6188 -408 66 1958 C ATOM 941 CD1 ILE A 128 29.396 48.367 136.144 1.00 65.72 C ANISOU 941 CD1 ILE A 128 10143 8506 6319 -409 98 2164 C ATOM 942 N ALA A 129 32.873 47.614 131.978 1.00 62.62 N ANISOU 942 N ALA A 129 9888 7965 5939 -512 27 1931 N ATOM 943 CA ALA A 129 33.942 46.887 131.268 1.00 62.31 C ANISOU 943 CA ALA A 129 9902 7876 5897 -542 0 1849 C ATOM 944 C ALA A 129 34.826 47.817 130.421 1.00 62.03 C ANISOU 944 C ALA A 129 9866 7827 5875 -514 32 1807 C ATOM 945 O ALA A 129 36.068 47.716 130.453 1.00 62.05 O ANISOU 945 O ALA A 129 9906 7773 5897 -492 38 1725 O ATOM 946 CB ALA A 129 33.348 45.790 130.400 1.00 62.67 C ANISOU 946 CB ALA A 129 9958 7947 5905 -626 -49 1869 C ATOM 947 N GLY A 130 34.175 48.730 129.691 1.00 61.55 N ANISOU 947 N GLY A 130 9759 7820 5804 -514 54 1868 N ATOM 948 CA GLY A 130 34.873 49.769 128.930 1.00 60.81 C ANISOU 948 CA GLY A 130 9658 7720 5724 -488 88 1846 C ATOM 949 C GLY A 130 35.857 50.579 129.759 1.00 60.12 C ANISOU 949 C GLY A 130 9583 7577 5681 -418 127 1795 C ATOM 950 O GLY A 130 37.013 50.791 129.338 1.00 59.94 O ANISOU 950 O GLY A 130 9583 7517 5673 -409 140 1729 O ATOM 951 N CYS A 131 35.409 51.013 130.941 1.00 59.76 N ANISOU 951 N CYS A 131 9521 7528 5655 -371 145 1824 N ATOM 952 CA CYS A 131 36.266 51.777 131.858 1.00 59.07 C ANISOU 952 CA CYS A 131 9447 7389 5608 -305 178 1775 C ATOM 953 C CYS A 131 37.537 51.011 132.168 1.00 57.51 C ANISOU 953 C CYS A 131 9298 7129 5421 -307 160 1682 C ATOM 954 O CYS A 131 38.628 51.546 132.026 1.00 56.95 O ANISOU 954 O CYS A 131 9240 7020 5376 -283 180 1624 O ATOM 955 CB CYS A 131 35.555 52.117 133.168 1.00 59.82 C ANISOU 955 CB CYS A 131 9525 7492 5713 -259 195 1813 C ATOM 956 SG CYS A 131 34.054 53.097 132.953 1.00 61.60 S ANISOU 956 SG CYS A 131 9685 7788 5930 -240 222 1923 S ATOM 957 N TRP A 132 37.382 49.751 132.561 1.00 56.32 N ANISOU 957 N TRP A 132 9173 6972 5253 -338 121 1670 N ATOM 958 CA TRP A 132 38.530 48.897 132.858 1.00 55.45 C ANISOU 958 CA TRP A 132 9110 6803 5154 -338 97 1585 C ATOM 959 C TRP A 132 39.407 48.640 131.633 1.00 55.12 C ANISOU 959 C TRP A 132 9085 6749 5109 -367 91 1529 C ATOM 960 O TRP A 132 40.631 48.717 131.733 1.00 54.90 O ANISOU 960 O TRP A 132 9077 6676 5106 -341 99 1456 O ATOM 961 CB TRP A 132 38.088 47.579 133.500 1.00 55.09 C ANISOU 961 CB TRP A 132 9090 6750 5090 -368 53 1593 C ATOM 962 CG TRP A 132 37.705 47.740 134.938 1.00 54.52 C ANISOU 962 CG TRP A 132 9013 6674 5026 -329 61 1619 C ATOM 963 CD1 TRP A 132 36.442 47.805 135.445 1.00 54.63 C ANISOU 963 CD1 TRP A 132 8997 6737 5021 -335 65 1699 C ATOM 964 CD2 TRP A 132 38.594 47.873 136.049 1.00 53.93 C ANISOU 964 CD2 TRP A 132 8963 6550 4976 -278 68 1565 C ATOM 965 NE1 TRP A 132 36.489 47.963 136.810 1.00 54.44 N ANISOU 965 NE1 TRP A 132 8980 6697 5006 -289 76 1696 N ATOM 966 CE2 TRP A 132 37.799 48.007 137.206 1.00 54.00 C ANISOU 966 CE2 TRP A 132 8960 6581 4976 -255 76 1614 C ATOM 967 CE3 TRP A 132 39.987 47.886 136.181 1.00 53.67 C ANISOU 967 CE3 TRP A 132 8959 6461 4972 -250 67 1479 C ATOM 968 CZ2 TRP A 132 38.349 48.151 138.483 1.00 53.76 C ANISOU 968 CZ2 TRP A 132 8949 6517 4959 -206 82 1580 C ATOM 969 CZ3 TRP A 132 40.536 48.032 137.459 1.00 53.54 C ANISOU 969 CZ3 TRP A 132 8959 6410 4972 -202 69 1447 C ATOM 970 CH2 TRP A 132 39.714 48.164 138.589 1.00 53.45 C ANISOU 970 CH2 TRP A 132 8940 6420 4947 -181 76 1496 C ATOM 971 N ILE A 133 38.795 48.363 130.483 1.00 55.10 N ANISOU 971 N ILE A 133 9071 6789 5072 -419 78 1564 N ATOM 972 CA ILE A 133 39.575 48.152 129.248 1.00 54.91 C ANISOU 972 CA ILE A 133 9063 6763 5036 -447 76 1513 C ATOM 973 C ILE A 133 40.431 49.391 128.953 1.00 54.28 C ANISOU 973 C ILE A 133 8965 6674 4983 -409 122 1488 C ATOM 974 O ILE A 133 41.668 49.294 128.826 1.00 53.86 O ANISOU 974 O ILE A 133 8932 6584 4948 -395 130 1411 O ATOM 975 CB ILE A 133 38.670 47.805 128.040 1.00 55.30 C ANISOU 975 CB ILE A 133 9100 6870 5038 -511 55 1562 C ATOM 976 CG1 ILE A 133 38.001 46.437 128.245 1.00 55.65 C ANISOU 976 CG1 ILE A 133 9171 6914 5058 -558 3 1572 C ATOM 977 CG2 ILE A 133 39.464 47.786 126.733 1.00 55.31 C ANISOU 977 CG2 ILE A 133 9114 6877 5021 -534 62 1512 C ATOM 978 CD1 ILE A 133 36.680 46.297 127.521 1.00 56.18 C ANISOU 978 CD1 ILE A 133 9211 7048 5085 -616 -17 1652 C ATOM 979 N LEU A 134 39.770 50.549 128.891 1.00 53.99 N ANISOU 979 N LEU A 134 8891 6670 4952 -392 153 1555 N ATOM 980 CA LEU A 134 40.462 51.819 128.628 1.00 53.74 C ANISOU 980 CA LEU A 134 8841 6626 4948 -359 196 1545 C ATOM 981 C LEU A 134 41.516 52.132 129.705 1.00 53.45 C ANISOU 981 C LEU A 134 8821 6530 4958 -308 211 1480 C ATOM 982 O LEU A 134 42.591 52.656 129.393 1.00 52.98 O ANISOU 982 O LEU A 134 8763 6446 4920 -296 234 1432 O ATOM 983 CB LEU A 134 39.450 52.965 128.500 1.00 53.88 C ANISOU 983 CB LEU A 134 8819 6682 4968 -344 221 1634 C ATOM 984 CG LEU A 134 39.937 54.335 127.978 1.00 53.93 C ANISOU 984 CG LEU A 134 8809 6684 4999 -322 263 1643 C ATOM 985 CD1 LEU A 134 40.525 54.238 126.571 1.00 54.06 C ANISOU 985 CD1 LEU A 134 8828 6721 4989 -366 266 1623 C ATOM 986 CD2 LEU A 134 38.798 55.344 128.016 1.00 54.00 C ANISOU 986 CD2 LEU A 134 8781 6724 5012 -300 282 1736 C ATOM 987 N SER A 135 41.206 51.785 130.960 1.00 53.55 N ANISOU 987 N SER A 135 8843 6521 4980 -281 197 1482 N ATOM 988 CA SER A 135 42.141 51.928 132.090 1.00 53.21 C ANISOU 988 CA SER A 135 8819 6424 4974 -235 202 1421 C ATOM 989 C SER A 135 43.389 51.081 131.926 1.00 53.16 C ANISOU 989 C SER A 135 8841 6382 4975 -243 182 1334 C ATOM 990 O SER A 135 44.500 51.563 132.158 1.00 53.00 O ANISOU 990 O SER A 135 8823 6327 4988 -216 199 1278 O ATOM 991 CB SER A 135 41.478 51.541 133.404 1.00 53.16 C ANISOU 991 CB SER A 135 8821 6412 4965 -212 186 1444 C ATOM 992 OG SER A 135 40.287 52.267 133.590 1.00 53.60 O ANISOU 992 OG SER A 135 8846 6505 5012 -199 206 1523 O ATOM 993 N PHE A 136 43.200 49.816 131.553 1.00 53.34 N ANISOU 993 N PHE A 136 8886 6411 4969 -281 146 1323 N ATOM 994 CA PHE A 136 44.324 48.945 131.201 1.00 53.36 C ANISOU 994 CA PHE A 136 8915 6383 4976 -289 127 1241 C ATOM 995 C PHE A 136 45.092 49.500 129.995 1.00 53.47 C ANISOU 995 C PHE A 136 8913 6411 4990 -301 157 1211 C ATOM 996 O PHE A 136 46.327 49.500 130.006 1.00 53.19 O ANISOU 996 O PHE A 136 8881 6347 4980 -281 165 1141 O ATOM 997 CB PHE A 136 43.873 47.494 130.953 1.00 53.45 C ANISOU 997 CB PHE A 136 8957 6394 4955 -329 81 1239 C ATOM 998 CG PHE A 136 43.840 46.648 132.200 1.00 53.27 C ANISOU 998 CG PHE A 136 8963 6332 4943 -311 46 1226 C ATOM 999 CD1 PHE A 136 45.019 46.178 132.766 1.00 53.17 C ANISOU 999 CD1 PHE A 136 8974 6267 4958 -278 32 1151 C ATOM 1000 CD2 PHE A 136 42.633 46.310 132.807 1.00 53.38 C ANISOU 1000 CD2 PHE A 136 8978 6364 4937 -328 26 1294 C ATOM 1001 CE1 PHE A 136 44.994 45.395 133.912 1.00 53.15 C ANISOU 1001 CE1 PHE A 136 9000 6229 4963 -262 -2 1144 C ATOM 1002 CE2 PHE A 136 42.603 45.523 133.953 1.00 53.20 C ANISOU 1002 CE2 PHE A 136 8983 6308 4921 -315 -5 1289 C ATOM 1003 CZ PHE A 136 43.785 45.066 134.506 1.00 53.09 C ANISOU 1003 CZ PHE A 136 8998 6239 4934 -282 -21 1214 C ATOM 1004 N VAL A 137 44.376 50.000 128.981 1.00 53.59 N ANISOU 1004 N VAL A 137 8907 6475 4978 -334 173 1268 N ATOM 1005 CA VAL A 137 45.043 50.625 127.824 1.00 53.94 C ANISOU 1005 CA VAL A 137 8935 6541 5018 -348 205 1250 C ATOM 1006 C VAL A 137 45.934 51.797 128.256 1.00 53.65 C ANISOU 1006 C VAL A 137 8878 6476 5027 -309 242 1228 C ATOM 1007 O VAL A 137 47.123 51.835 127.909 1.00 54.05 O ANISOU 1007 O VAL A 137 8928 6513 5094 -305 257 1165 O ATOM 1008 CB VAL A 137 44.037 51.071 126.724 1.00 54.53 C ANISOU 1008 CB VAL A 137 8988 6675 5053 -388 214 1326 C ATOM 1009 CG1 VAL A 137 44.689 51.993 125.692 1.00 54.56 C ANISOU 1009 CG1 VAL A 137 8971 6700 5057 -397 254 1323 C ATOM 1010 CG2 VAL A 137 43.440 49.856 126.025 1.00 55.00 C ANISOU 1010 CG2 VAL A 137 9069 6763 5063 -437 176 1329 C ATOM 1011 N VAL A 138 45.366 52.732 129.019 1.00 53.12 N ANISOU 1011 N VAL A 138 8797 6401 4983 -280 257 1278 N ATOM 1012 CA VAL A 138 46.108 53.925 129.452 1.00 52.83 C ANISOU 1012 CA VAL A 138 8746 6334 4991 -246 290 1261 C ATOM 1013 C VAL A 138 47.243 53.554 130.416 1.00 52.76 C ANISOU 1013 C VAL A 138 8753 6276 5016 -215 278 1180 C ATOM 1014 O VAL A 138 48.368 54.020 130.269 1.00 52.48 O ANISOU 1014 O VAL A 138 8707 6222 5009 -208 297 1132 O ATOM 1015 CB VAL A 138 45.168 54.969 130.103 1.00 52.59 C ANISOU 1015 CB VAL A 138 8702 6302 4975 -218 307 1330 C ATOM 1016 CG1 VAL A 138 45.956 56.119 130.723 1.00 52.55 C ANISOU 1016 CG1 VAL A 138 8691 6253 5019 -181 334 1303 C ATOM 1017 CG2 VAL A 138 44.170 55.512 129.078 1.00 52.72 C ANISOU 1017 CG2 VAL A 138 8697 6368 4965 -244 321 1412 C ATOM 1018 N GLY A 139 46.936 52.709 131.390 1.00 52.99 N ANISOU 1018 N GLY A 139 8803 6286 5041 -198 245 1170 N ATOM 1019 CA GLY A 139 47.904 52.290 132.396 1.00 53.18 C ANISOU 1019 CA GLY A 139 8844 6266 5094 -166 226 1100 C ATOM 1020 C GLY A 139 49.038 51.400 131.917 1.00 53.68 C ANISOU 1020 C GLY A 139 8916 6318 5160 -175 211 1025 C ATOM 1021 O GLY A 139 50.159 51.513 132.435 1.00 53.67 O ANISOU 1021 O GLY A 139 8911 6286 5193 -149 211 964 O ATOM 1022 N LEU A 140 48.761 50.510 130.956 1.00 54.27 N ANISOU 1022 N LEU A 140 9000 6418 5199 -210 198 1025 N ATOM 1023 CA LEU A 140 49.806 49.632 130.391 1.00 54.46 C ANISOU 1023 CA LEU A 140 9034 6434 5223 -215 187 950 C ATOM 1024 C LEU A 140 50.628 50.266 129.265 1.00 54.96 C ANISOU 1024 C LEU A 140 9069 6523 5289 -231 226 924 C ATOM 1025 O LEU A 140 51.626 49.676 128.857 1.00 54.85 O ANISOU 1025 O LEU A 140 9055 6505 5280 -227 225 856 O ATOM 1026 CB LEU A 140 49.218 48.303 129.899 1.00 54.49 C ANISOU 1026 CB LEU A 140 9069 6446 5188 -245 152 950 C ATOM 1027 CG LEU A 140 48.610 47.371 130.943 1.00 54.37 C ANISOU 1027 CG LEU A 140 9087 6401 5170 -235 106 964 C ATOM 1028 CD1 LEU A 140 47.958 46.180 130.258 1.00 54.45 C ANISOU 1028 CD1 LEU A 140 9127 6421 5139 -277 74 971 C ATOM 1029 CD2 LEU A 140 49.665 46.907 131.934 1.00 54.40 C ANISOU 1029 CD2 LEU A 140 9104 6354 5210 -192 85 897 C ATOM 1030 N THR A 141 50.241 51.449 128.775 1.00 55.60 N ANISOU 1030 N THR A 141 9125 6631 5368 -246 262 979 N ATOM 1031 CA THR A 141 51.016 52.137 127.723 1.00 56.21 C ANISOU 1031 CA THR A 141 9174 6734 5447 -265 302 963 C ATOM 1032 C THR A 141 52.544 52.153 128.004 1.00 56.62 C ANISOU 1032 C THR A 141 9210 6762 5539 -241 312 882 C ATOM 1033 O THR A 141 53.322 51.728 127.136 1.00 56.79 O ANISOU 1033 O THR A 141 9222 6806 5547 -254 324 834 O ATOM 1034 CB THR A 141 50.448 53.551 127.422 1.00 56.14 C ANISOU 1034 CB THR A 141 9143 6743 5443 -277 337 1038 C ATOM 1035 OG1 THR A 141 49.140 53.428 126.850 1.00 55.88 O ANISOU 1035 OG1 THR A 141 9117 6747 5366 -304 329 1109 O ATOM 1036 CG2 THR A 141 51.342 54.323 126.453 1.00 56.26 C ANISOU 1036 CG2 THR A 141 9129 6780 5464 -298 378 1024 C ATOM 1037 N PRO A 142 52.969 52.582 129.217 1.00 56.81 N ANISOU 1037 N PRO A 142 9231 6744 5608 -205 304 864 N ATOM 1038 CA PRO A 142 54.388 52.482 129.594 1.00 57.54 C ANISOU 1038 CA PRO A 142 9307 6816 5740 -181 304 787 C ATOM 1039 C PRO A 142 55.032 51.102 129.375 1.00 58.73 C ANISOU 1039 C PRO A 142 9468 6964 5879 -171 279 718 C ATOM 1040 O PRO A 142 56.193 51.037 128.953 1.00 58.73 O ANISOU 1040 O PRO A 142 9443 6975 5897 -166 295 660 O ATOM 1041 CB PRO A 142 54.379 52.829 131.086 1.00 57.07 C ANISOU 1041 CB PRO A 142 9256 6710 5716 -145 282 785 C ATOM 1042 CG PRO A 142 53.225 53.741 131.241 1.00 56.66 C ANISOU 1042 CG PRO A 142 9210 6661 5655 -153 296 863 C ATOM 1043 CD PRO A 142 52.193 53.306 130.240 1.00 56.44 C ANISOU 1043 CD PRO A 142 9192 6673 5578 -186 299 914 C ATOM 1044 N MET A 143 54.288 50.026 129.652 1.00 60.04 N ANISOU 1044 N MET A 143 9673 7118 6020 -167 240 725 N ATOM 1045 CA MET A 143 54.756 48.660 129.371 1.00 61.26 C ANISOU 1045 CA MET A 143 9847 7264 6162 -157 213 664 C ATOM 1046 C MET A 143 54.966 48.402 127.873 1.00 61.85 C ANISOU 1046 C MET A 143 9913 7384 6201 -189 240 645 C ATOM 1047 O MET A 143 55.827 47.595 127.517 1.00 62.80 O ANISOU 1047 O MET A 143 10034 7502 6323 -173 236 575 O ATOM 1048 CB MET A 143 53.791 47.605 129.924 1.00 62.24 C ANISOU 1048 CB MET A 143 10018 7363 6265 -156 166 687 C ATOM 1049 CG MET A 143 53.730 47.528 131.440 1.00 62.86 C ANISOU 1049 CG MET A 143 10111 7398 6373 -120 133 692 C ATOM 1050 SD MET A 143 54.977 46.443 132.160 1.00 64.56 S ANISOU 1050 SD MET A 143 10338 7567 6622 -72 93 605 S ATOM 1051 CE MET A 143 54.417 44.842 131.591 1.00 64.92 C ANISOU 1051 CE MET A 143 10434 7600 6631 -89 55 594 C ATOM 1052 N PHE A 144 54.192 49.065 127.004 1.00 61.74 N ANISOU 1052 N PHE A 144 9891 7411 6152 -229 268 705 N ATOM 1053 CA PHE A 144 54.355 48.879 125.553 1.00 61.88 C ANISOU 1053 CA PHE A 144 9903 7480 6128 -263 295 691 C ATOM 1054 C PHE A 144 55.629 49.528 124.994 1.00 61.15 C ANISOU 1054 C PHE A 144 9765 7412 6054 -260 341 649 C ATOM 1055 O PHE A 144 56.091 49.120 123.927 1.00 61.58 O ANISOU 1055 O PHE A 144 9814 7505 6077 -274 361 611 O ATOM 1056 CB PHE A 144 53.140 49.394 124.756 1.00 62.72 C ANISOU 1056 CB PHE A 144 10013 7627 6188 -309 307 774 C ATOM 1057 CG PHE A 144 51.809 48.793 125.163 1.00 63.28 C ANISOU 1057 CG PHE A 144 10121 7686 6236 -321 265 823 C ATOM 1058 CD1 PHE A 144 51.700 47.469 125.623 1.00 63.37 C ANISOU 1058 CD1 PHE A 144 10171 7663 6244 -308 219 785 C ATOM 1059 CD2 PHE A 144 50.638 49.560 125.048 1.00 63.16 C ANISOU 1059 CD2 PHE A 144 10098 7695 6203 -346 272 913 C ATOM 1060 CE1 PHE A 144 50.460 46.946 125.977 1.00 63.41 C ANISOU 1060 CE1 PHE A 144 10205 7660 6227 -327 182 836 C ATOM 1061 CE2 PHE A 144 49.400 49.034 125.398 1.00 62.94 C ANISOU 1061 CE2 PHE A 144 10095 7664 6153 -359 235 963 C ATOM 1062 CZ PHE A 144 49.310 47.725 125.853 1.00 63.20 C ANISOU 1062 CZ PHE A 144 10165 7664 6181 -353 191 925 C ATOM 1063 N GLY A 145 56.191 50.518 125.694 1.00 59.75 N ANISOU 1063 N GLY A 145 9557 7217 5926 -243 357 654 N ATOM 1064 CA GLY A 145 57.399 51.206 125.217 1.00 59.22 C ANISOU 1064 CA GLY A 145 9442 7176 5882 -247 400 620 C ATOM 1065 C GLY A 145 57.650 52.627 125.696 1.00 58.15 C ANISOU 1065 C GLY A 145 9275 7028 5788 -252 424 657 C ATOM 1066 O GLY A 145 58.809 53.040 125.785 1.00 57.86 O ANISOU 1066 O GLY A 145 9200 6994 5789 -245 444 616 O ATOM 1067 N TRP A 146 56.588 53.379 125.987 1.00 57.09 N ANISOU 1067 N TRP A 146 9157 6881 5652 -265 421 733 N ATOM 1068 CA TRP A 146 56.718 54.794 126.369 1.00 56.86 C ANISOU 1068 CA TRP A 146 9106 6836 5663 -271 444 772 C ATOM 1069 C TRP A 146 57.316 54.947 127.783 1.00 57.28 C ANISOU 1069 C TRP A 146 9156 6835 5771 -232 420 732 C ATOM 1070 O TRP A 146 56.595 55.087 128.778 1.00 56.88 O ANISOU 1070 O TRP A 146 9131 6748 5731 -210 394 760 O ATOM 1071 CB TRP A 146 55.363 55.519 126.248 1.00 55.96 C ANISOU 1071 CB TRP A 146 9010 6723 5528 -288 449 863 C ATOM 1072 CG TRP A 146 55.450 57.021 126.086 1.00 55.45 C ANISOU 1072 CG TRP A 146 8923 6652 5491 -307 484 912 C ATOM 1073 CD1 TRP A 146 56.564 57.807 126.210 1.00 55.47 C ANISOU 1073 CD1 TRP A 146 8894 6641 5538 -312 507 884 C ATOM 1074 CD2 TRP A 146 54.368 57.912 125.791 1.00 54.95 C ANISOU 1074 CD2 TRP A 146 8869 6593 5416 -323 496 1000 C ATOM 1075 NE1 TRP A 146 56.239 59.124 126.002 1.00 55.42 N ANISOU 1075 NE1 TRP A 146 8882 6625 5548 -333 532 949 N ATOM 1076 CE2 TRP A 146 54.899 59.218 125.746 1.00 55.08 C ANISOU 1076 CE2 TRP A 146 8862 6591 5471 -336 527 1020 C ATOM 1077 CE3 TRP A 146 53.000 57.734 125.559 1.00 54.73 C ANISOU 1077 CE3 TRP A 146 8862 6583 5349 -327 483 1065 C ATOM 1078 CZ2 TRP A 146 54.110 60.341 125.470 1.00 55.05 C ANISOU 1078 CZ2 TRP A 146 8863 6581 5471 -349 545 1103 C ATOM 1079 CZ3 TRP A 146 52.211 58.857 125.295 1.00 54.69 C ANISOU 1079 CZ3 TRP A 146 8855 6578 5347 -338 502 1148 C ATOM 1080 CH2 TRP A 146 52.773 60.138 125.249 1.00 54.86 C ANISOU 1080 CH2 TRP A 146 8858 6575 5409 -346 532 1165 C ATOM 1081 N ASN A 147 58.646 54.926 127.845 1.00 58.24 N ANISOU 1081 N ASN A 147 9243 6958 5925 -224 429 668 N ATOM 1082 CA ASN A 147 59.387 54.980 129.113 1.00 58.78 C ANISOU 1082 CA ASN A 147 9305 6984 6045 -189 402 622 C ATOM 1083 C ASN A 147 60.820 55.505 128.896 1.00 60.30 C ANISOU 1083 C ASN A 147 9443 7191 6276 -199 427 575 C ATOM 1084 O ASN A 147 61.165 55.906 127.783 1.00 61.17 O ANISOU 1084 O ASN A 147 9523 7343 6372 -235 469 586 O ATOM 1085 CB ASN A 147 59.369 53.592 129.780 1.00 58.24 C ANISOU 1085 CB ASN A 147 9264 6896 5969 -148 355 576 C ATOM 1086 CG ASN A 147 59.790 52.475 128.841 1.00 58.09 C ANISOU 1086 CG ASN A 147 9239 6911 5920 -148 359 530 C ATOM 1087 OD1 ASN A 147 60.934 52.424 128.387 1.00 58.34 O ANISOU 1087 OD1 ASN A 147 9230 6967 5967 -147 379 478 O ATOM 1088 ND2 ASN A 147 58.870 51.559 128.566 1.00 57.71 N ANISOU 1088 ND2 ASN A 147 9232 6865 5828 -149 338 547 N ATOM 1089 N ASN A 148 61.639 55.516 129.952 1.00 61.61 N ANISOU 1089 N ASN A 148 9595 7326 6487 -170 401 527 N ATOM 1090 CA ASN A 148 63.029 55.998 129.883 1.00 63.19 C ANISOU 1090 CA ASN A 148 9738 7540 6729 -180 419 482 C ATOM 1091 C ASN A 148 64.083 54.899 129.652 1.00 64.17 C ANISOU 1091 C ASN A 148 9830 7692 6856 -154 411 406 C ATOM 1092 O ASN A 148 65.273 55.124 129.922 1.00 65.23 O ANISOU 1092 O ASN A 148 9916 7834 7033 -150 413 360 O ATOM 1093 CB ASN A 148 63.385 56.744 131.178 1.00 63.56 C ANISOU 1093 CB ASN A 148 9783 7539 6827 -167 393 471 C ATOM 1094 CG ASN A 148 62.424 57.869 131.499 1.00 64.02 C ANISOU 1094 CG ASN A 148 9873 7563 6888 -185 400 537 C ATOM 1095 OD1 ASN A 148 61.955 58.581 130.608 1.00 65.07 O ANISOU 1095 OD1 ASN A 148 10005 7713 7006 -222 438 591 O ATOM 1096 ND2 ASN A 148 62.137 58.045 132.782 1.00 63.91 N ANISOU 1096 ND2 ASN A 148 9888 7502 6893 -156 364 533 N ATOM 1097 N LEU A 149 63.681 53.727 129.154 1.00 64.67 N ANISOU 1097 N LEU A 149 9920 7772 6879 -136 403 392 N ATOM 1098 CA LEU A 149 64.622 52.616 128.975 1.00 66.27 C ANISOU 1098 CA LEU A 149 10099 7993 7086 -102 393 317 C ATOM 1099 C LEU A 149 65.872 53.054 128.198 1.00 68.22 C ANISOU 1099 C LEU A 149 10275 8293 7352 -122 439 283 C ATOM 1100 O LEU A 149 66.999 52.878 128.668 1.00 68.45 O ANISOU 1100 O LEU A 149 10260 8325 7422 -96 427 227 O ATOM 1101 CB LEU A 149 63.943 51.432 128.276 1.00 66.15 C ANISOU 1101 CB LEU A 149 10124 7990 7018 -92 387 311 C ATOM 1102 CG LEU A 149 64.795 50.199 127.936 1.00 66.61 C ANISOU 1102 CG LEU A 149 10168 8065 7074 -53 379 233 C ATOM 1103 CD1 LEU A 149 65.525 49.668 129.161 1.00 66.77 C ANISOU 1103 CD1 LEU A 149 10181 8046 7144 0 330 182 C ATOM 1104 CD2 LEU A 149 63.926 49.116 127.319 1.00 66.84 C ANISOU 1104 CD2 LEU A 149 10251 8093 7050 -50 367 234 C ATOM 1105 N SER A 150 65.652 53.647 127.028 1.00 70.31 N ANISOU 1105 N SER A 150 10526 8601 7584 -170 490 321 N ATOM 1106 CA SER A 150 66.738 54.155 126.176 1.00 72.34 C ANISOU 1106 CA SER A 150 10716 8917 7852 -198 541 301 C ATOM 1107 C SER A 150 67.595 55.215 126.879 1.00 73.10 C ANISOU 1107 C SER A 150 10765 8999 8011 -214 542 299 C ATOM 1108 O SER A 150 68.818 55.235 126.716 1.00 74.52 O ANISOU 1108 O SER A 150 10879 9214 8218 -214 560 253 O ATOM 1109 CB SER A 150 66.168 54.737 124.880 1.00 72.86 C ANISOU 1109 CB SER A 150 10786 9029 7869 -253 593 359 C ATOM 1110 OG SER A 150 65.187 55.724 125.167 1.00 73.96 O ANISOU 1110 OG SER A 150 10960 9132 8010 -283 588 437 O ATOM 1111 N ALA A 151 66.945 56.088 127.650 1.00 72.52 N ANISOU 1111 N ALA A 151 10722 8874 7957 -229 522 349 N ATOM 1112 CA ALA A 151 67.642 57.100 128.448 1.00 72.36 C ANISOU 1112 CA ALA A 151 10669 8827 7996 -245 514 346 C ATOM 1113 C ALA A 151 68.528 56.479 129.531 1.00 72.30 C ANISOU 1113 C ALA A 151 10638 8800 8030 -197 467 276 C ATOM 1114 O ALA A 151 69.628 56.964 129.778 1.00 72.69 O ANISOU 1114 O ALA A 151 10630 8862 8124 -210 470 247 O ATOM 1115 CB ALA A 151 66.646 58.071 129.069 1.00 71.97 C ANISOU 1115 CB ALA A 151 10669 8721 7955 -262 500 409 C ATOM 1116 N VAL A 152 68.050 55.407 130.166 1.00 72.26 N ANISOU 1116 N VAL A 152 10678 8767 8010 -145 422 254 N ATOM 1117 CA VAL A 152 68.828 54.715 131.210 1.00 72.51 C ANISOU 1117 CA VAL A 152 10693 8780 8077 -94 372 192 C ATOM 1118 C VAL A 152 69.948 53.851 130.607 1.00 73.32 C ANISOU 1118 C VAL A 152 10739 8934 8186 -68 385 127 C ATOM 1119 O VAL A 152 71.050 53.774 131.171 1.00 73.79 O ANISOU 1119 O VAL A 152 10746 9001 8290 -46 364 78 O ATOM 1120 CB VAL A 152 67.921 53.875 132.141 1.00 71.98 C ANISOU 1120 CB VAL A 152 10696 8662 7991 -48 317 196 C ATOM 1121 CG1 VAL A 152 68.743 53.152 133.195 1.00 72.36 C ANISOU 1121 CG1 VAL A 152 10729 8691 8073 4 263 137 C ATOM 1122 CG2 VAL A 152 66.901 54.766 132.838 1.00 71.53 C ANISOU 1122 CG2 VAL A 152 10688 8559 7931 -67 305 255 C ATOM 1123 N GLU A 153 69.661 53.200 129.478 1.00 74.23 N ANISOU 1123 N GLU A 153 10862 9085 8255 -67 419 125 N ATOM 1124 CA GLU A 153 70.668 52.407 128.746 1.00 75.48 C ANISOU 1124 CA GLU A 153 10966 9298 8412 -41 442 62 C ATOM 1125 C GLU A 153 71.895 53.228 128.327 1.00 76.41 C ANISOU 1125 C GLU A 153 10994 9471 8564 -75 485 46 C ATOM 1126 O GLU A 153 73.023 52.725 128.371 1.00 76.52 O ANISOU 1126 O GLU A 153 10948 9517 8607 -41 483 -14 O ATOM 1127 CB GLU A 153 70.046 51.745 127.510 1.00 76.06 C ANISOU 1127 CB GLU A 153 11071 9403 8423 -46 477 68 C ATOM 1128 CG GLU A 153 69.179 50.535 127.832 1.00 76.16 C ANISOU 1128 CG GLU A 153 11158 9372 8407 -2 432 58 C ATOM 1129 CD GLU A 153 68.405 49.995 126.641 1.00 76.90 C ANISOU 1129 CD GLU A 153 11290 9491 8435 -18 461 71 C ATOM 1130 OE1 GLU A 153 68.368 50.644 125.572 1.00 77.82 O ANISOU 1130 OE1 GLU A 153 11384 9660 8521 -66 517 98 O ATOM 1131 OE2 GLU A 153 67.820 48.902 126.784 1.00 77.74 O ANISOU 1131 OE2 GLU A 153 11453 9565 8518 15 425 54 O ATOM 1132 N ARG A 154 71.663 54.478 127.915 1.00 76.91 N ANISOU 1132 N ARG A 154 11049 9545 8627 -141 522 103 N ATOM 1133 CA ARG A 154 72.744 55.423 127.614 1.00 77.83 C ANISOU 1133 CA ARG A 154 11085 9707 8780 -186 559 101 C ATOM 1134 C ARG A 154 73.650 55.641 128.820 1.00 77.56 C ANISOU 1134 C ARG A 154 11009 9648 8811 -168 514 64 C ATOM 1135 O ARG A 154 74.866 55.547 128.700 1.00 78.55 O ANISOU 1135 O ARG A 154 11054 9821 8968 -162 526 19 O ATOM 1136 CB ARG A 154 72.193 56.780 127.152 1.00 78.51 C ANISOU 1136 CB ARG A 154 11184 9788 8858 -260 596 178 C ATOM 1137 CG ARG A 154 71.762 56.825 125.706 1.00 79.43 C ANISOU 1137 CG ARG A 154 11305 9958 8916 -296 656 214 C ATOM 1138 CD ARG A 154 71.199 58.188 125.319 1.00 79.92 C ANISOU 1138 CD ARG A 154 11382 10008 8974 -366 686 297 C ATOM 1139 NE ARG A 154 72.231 59.113 124.841 1.00 80.84 N ANISOU 1139 NE ARG A 154 11424 10169 9120 -423 729 306 N ATOM 1140 CZ ARG A 154 71.996 60.310 124.299 1.00 81.01 C ANISOU 1140 CZ ARG A 154 11444 10192 9141 -491 765 376 C ATOM 1141 NH1 ARG A 154 70.751 60.771 124.154 1.00 80.45 N ANISOU 1141 NH1 ARG A 154 11442 10081 9042 -507 762 444 N ATOM 1142 NH2 ARG A 154 73.020 61.061 123.896 1.00 81.63 N ANISOU 1142 NH2 ARG A 154 11452 10314 9250 -544 802 381 N ATOM 1143 N ALA A 155 73.048 55.934 129.971 1.00 76.47 N ANISOU 1143 N ALA A 155 10923 9439 8690 -159 462 84 N ATOM 1144 CA ALA A 155 73.792 56.139 131.215 1.00 76.86 C ANISOU 1144 CA ALA A 155 10945 9461 8795 -142 410 50 C ATOM 1145 C ALA A 155 74.469 54.860 131.726 1.00 77.27 C ANISOU 1145 C ALA A 155 10974 9521 8860 -68 368 -17 C ATOM 1146 O ALA A 155 75.553 54.929 132.312 1.00 77.98 O ANISOU 1146 O ALA A 155 11002 9627 8998 -57 343 -58 O ATOM 1147 CB ALA A 155 72.878 56.715 132.286 1.00 76.60 C ANISOU 1147 CB ALA A 155 10983 9353 8766 -147 367 88 C ATOM 1148 N TRP A 156 73.832 53.707 131.504 1.00 77.30 N ANISOU 1148 N TRP A 156 11029 9515 8824 -19 358 -28 N ATOM 1149 CA TRP A 156 74.403 52.402 131.892 1.00 77.37 C ANISOU 1149 CA TRP A 156 11025 9526 8845 55 319 -90 C ATOM 1150 C TRP A 156 75.675 52.073 131.079 1.00 78.51 C ANISOU 1150 C TRP A 156 11077 9746 9007 68 358 -144 C ATOM 1151 O TRP A 156 76.702 51.633 131.635 1.00 79.07 O ANISOU 1151 O TRP A 156 11091 9830 9119 112 326 -195 O ATOM 1152 CB TRP A 156 73.338 51.307 131.725 1.00 76.77 C ANISOU 1152 CB TRP A 156 11031 9417 8720 93 303 -84 C ATOM 1153 CG TRP A 156 73.570 50.048 132.511 1.00 76.80 C ANISOU 1153 CG TRP A 156 11054 9389 8737 170 243 -130 C ATOM 1154 CD1 TRP A 156 73.675 48.782 132.011 1.00 76.93 C ANISOU 1154 CD1 TRP A 156 11080 9412 8735 222 241 -172 C ATOM 1155 CD2 TRP A 156 73.697 49.927 133.936 1.00 76.77 C ANISOU 1155 CD2 TRP A 156 11066 9338 8764 202 173 -137 C ATOM 1156 NE1 TRP A 156 73.870 47.882 133.030 1.00 77.00 N ANISOU 1156 NE1 TRP A 156 11110 9378 8767 286 174 -202 N ATOM 1157 CE2 TRP A 156 73.887 48.555 134.223 1.00 76.80 C ANISOU 1157 CE2 TRP A 156 11088 9322 8770 274 131 -179 C ATOM 1158 CE3 TRP A 156 73.682 50.846 134.997 1.00 76.60 C ANISOU 1158 CE3 TRP A 156 11047 9288 8768 177 141 -114 C ATOM 1159 CZ2 TRP A 156 74.064 48.076 135.530 1.00 76.44 C ANISOU 1159 CZ2 TRP A 156 11061 9233 8748 321 58 -192 C ATOM 1160 CZ3 TRP A 156 73.861 50.369 136.299 1.00 76.49 C ANISOU 1160 CZ3 TRP A 156 11052 9235 8774 223 69 -132 C ATOM 1161 CH2 TRP A 156 74.041 48.993 136.551 1.00 76.37 C ANISOU 1161 CH2 TRP A 156 11053 9204 8758 294 28 -168 C ATOM 1162 N ALA A 157 75.597 52.303 129.767 1.00 79.43 N ANISOU 1162 N ALA A 157 11174 9913 9089 31 427 -129 N ATOM 1163 CA ALA A 157 76.746 52.160 128.863 1.00 80.79 C ANISOU 1163 CA ALA A 157 11255 10168 9270 34 478 -172 C ATOM 1164 C ALA A 157 77.814 53.232 129.113 1.00 81.93 C ANISOU 1164 C ALA A 157 11310 10349 9468 -11 490 -170 C ATOM 1165 O ALA A 157 79.005 52.923 129.148 1.00 82.46 O ANISOU 1165 O ALA A 157 11293 10465 9572 16 492 -221 O ATOM 1166 CB ALA A 157 76.287 52.205 127.413 1.00 80.93 C ANISOU 1166 CB ALA A 157 11285 10234 9230 0 549 -149 C ATOM 1167 N ALA A 158 77.381 54.478 129.304 1.00 82.42 N ANISOU 1167 N ALA A 158 11391 10385 9538 -82 496 -111 N ATOM 1168 CA ALA A 158 78.274 55.597 129.649 1.00 83.43 C ANISOU 1168 CA ALA A 158 11447 10531 9719 -136 499 -103 C ATOM 1169 C ALA A 158 79.026 55.346 130.955 1.00 84.04 C ANISOU 1169 C ALA A 158 11492 10585 9851 -95 428 -148 C ATOM 1170 O ALA A 158 80.214 55.651 131.057 1.00 85.60 O ANISOU 1170 O ALA A 158 11598 10830 10095 -109 431 -176 O ATOM 1171 CB ALA A 158 77.492 56.901 129.741 1.00 83.07 C ANISOU 1171 CB ALA A 158 11449 10441 9671 -211 507 -32 C ATOM 1172 N ALA A 159 78.327 54.800 131.948 1.00 83.77 N ANISOU 1172 N ALA A 159 11534 10482 9811 -47 365 -151 N ATOM 1173 CA ALA A 159 78.970 54.280 133.159 1.00 84.30 C ANISOU 1173 CA ALA A 159 11581 10529 9919 6 293 -197 C ATOM 1174 C ALA A 159 79.855 53.073 132.830 1.00 84.99 C ANISOU 1174 C ALA A 159 11608 10667 10016 78 294 -259 C ATOM 1175 O ALA A 159 80.883 52.869 133.473 1.00 85.71 O ANISOU 1175 O ALA A 159 11632 10778 10153 108 256 -301 O ATOM 1176 CB ALA A 159 77.930 53.904 134.204 1.00 83.73 C ANISOU 1176 CB ALA A 159 11610 10376 9828 41 231 -180 C ATOM 1177 N GLY A 160 79.439 52.276 131.842 1.00 84.91 N ANISOU 1177 N GLY A 160 11623 10676 9961 106 336 -267 N ATOM 1178 CA GLY A 160 80.244 51.165 131.330 1.00 85.06 C ANISOU 1178 CA GLY A 160 11587 10745 9984 174 349 -329 C ATOM 1179 C GLY A 160 79.875 49.865 132.000 1.00 84.65 C ANISOU 1179 C GLY A 160 11597 10638 9926 260 288 -360 C ATOM 1180 O GLY A 160 80.754 49.129 132.450 1.00 85.04 O ANISOU 1180 O GLY A 160 11598 10700 10012 326 252 -411 O ATOM 1181 N SER A 161 78.572 49.587 132.055 1.00 83.90 N ANISOU 1181 N SER A 161 11609 10482 9786 258 275 -324 N ATOM 1182 CA SER A 161 78.045 48.388 132.709 1.00 83.01 C ANISOU 1182 CA SER A 161 11568 10306 9662 329 215 -341 C ATOM 1183 C SER A 161 77.270 47.539 131.705 1.00 82.49 C ANISOU 1183 C SER A 161 11562 10235 9542 347 248 -345 C ATOM 1184 O SER A 161 76.572 48.070 130.841 1.00 81.55 O ANISOU 1184 O SER A 161 11470 10133 9382 290 300 -307 O ATOM 1185 CB SER A 161 77.144 48.789 133.868 1.00 82.19 C ANISOU 1185 CB SER A 161 11541 10131 9555 310 158 -293 C ATOM 1186 OG SER A 161 77.875 49.470 134.871 1.00 82.57 O ANISOU 1186 OG SER A 161 11540 10180 9650 299 119 -297 O ATOM 1187 N MET A 162 77.402 46.220 131.830 1.00 82.96 N ANISOU 1187 N MET A 162 11646 10271 9604 425 215 -390 N ATOM 1188 CA MET A 162 76.818 45.271 130.876 1.00 83.05 C ANISOU 1188 CA MET A 162 11711 10276 9568 449 241 -408 C ATOM 1189 C MET A 162 75.392 44.886 131.272 1.00 80.86 C ANISOU 1189 C MET A 162 11547 9922 9251 440 202 -363 C ATOM 1190 O MET A 162 74.984 45.060 132.423 1.00 80.48 O ANISOU 1190 O MET A 162 11537 9821 9219 438 146 -330 O ATOM 1191 CB MET A 162 77.674 44.000 130.794 1.00 84.98 C ANISOU 1191 CB MET A 162 11926 10525 9836 541 223 -483 C ATOM 1192 CG MET A 162 79.154 44.219 130.498 1.00 86.67 C ANISOU 1192 CG MET A 162 12018 10817 10093 565 256 -534 C ATOM 1193 SD MET A 162 79.482 44.986 128.895 1.00 88.80 S ANISOU 1193 SD MET A 162 12222 11190 10328 504 365 -537 S ATOM 1194 CE MET A 162 79.432 46.739 129.276 1.00 87.89 C ANISOU 1194 CE MET A 162 12069 11095 10228 401 379 -466 C ATOM 1195 N GLY A 163 74.643 44.359 130.305 1.00 78.86 N ANISOU 1195 N GLY A 163 11348 9667 8946 432 233 -362 N ATOM 1196 CA GLY A 163 73.304 43.823 130.552 1.00 76.95 C ANISOU 1196 CA GLY A 163 11212 9358 8667 425 197 -323 C ATOM 1197 C GLY A 163 72.251 44.883 130.800 1.00 74.83 C ANISOU 1197 C GLY A 163 10981 9075 8373 352 203 -244 C ATOM 1198 O GLY A 163 72.475 46.064 130.524 1.00 75.06 O ANISOU 1198 O GLY A 163 10962 9148 8408 299 245 -218 O ATOM 1199 N GLU A 164 71.103 44.454 131.325 1.00 72.71 N ANISOU 1199 N GLU A 164 10798 8746 8081 349 161 -204 N ATOM 1200 CA GLU A 164 69.983 45.357 131.601 1.00 70.95 C ANISOU 1200 CA GLU A 164 10618 8507 7833 288 164 -128 C ATOM 1201 C GLU A 164 70.335 46.302 132.754 1.00 70.08 C ANISOU 1201 C GLU A 164 10477 8385 7763 279 138 -107 C ATOM 1202 O GLU A 164 71.016 45.890 133.696 1.00 70.66 O ANISOU 1202 O GLU A 164 10535 8436 7875 327 90 -138 O ATOM 1203 CB GLU A 164 68.717 44.574 131.962 1.00 70.34 C ANISOU 1203 CB GLU A 164 10633 8370 7722 292 121 -93 C ATOM 1204 CG GLU A 164 67.440 45.411 131.956 1.00 69.73 C ANISOU 1204 CG GLU A 164 10598 8287 7609 231 136 -15 C ATOM 1205 CD GLU A 164 66.239 44.702 132.559 1.00 69.06 C ANISOU 1205 CD GLU A 164 10595 8145 7498 235 88 24 C ATOM 1206 OE1 GLU A 164 66.346 43.506 132.906 1.00 69.52 O ANISOU 1206 OE1 GLU A 164 10686 8164 7562 281 43 -7 O ATOM 1207 OE2 GLU A 164 65.178 45.349 132.696 1.00 67.90 O ANISOU 1207 OE2 GLU A 164 10480 7993 7325 192 95 89 O ATOM 1208 N PRO A 165 69.885 47.570 132.677 1.00 68.88 N ANISOU 1208 N PRO A 165 10319 8247 7603 218 170 -54 N ATOM 1209 CA PRO A 165 70.067 48.485 133.802 1.00 68.04 C ANISOU 1209 CA PRO A 165 10198 8121 7530 206 143 -34 C ATOM 1210 C PRO A 165 69.438 48.037 135.125 1.00 66.85 C ANISOU 1210 C PRO A 165 10110 7910 7378 236 76 -14 C ATOM 1211 O PRO A 165 68.210 47.845 135.215 1.00 66.12 O ANISOU 1211 O PRO A 165 10085 7787 7248 223 68 31 O ATOM 1212 CB PRO A 165 69.409 49.776 133.313 1.00 67.93 C ANISOU 1212 CB PRO A 165 10188 8124 7498 138 191 24 C ATOM 1213 CG PRO A 165 69.551 49.732 131.837 1.00 68.34 C ANISOU 1213 CG PRO A 165 10212 8228 7523 113 252 16 C ATOM 1214 CD PRO A 165 69.443 48.285 131.461 1.00 68.64 C ANISOU 1214 CD PRO A 165 10281 8260 7538 160 235 -21 C ATOM 1215 N VAL A 166 70.307 47.846 136.117 1.00 66.85 N ANISOU 1215 N VAL A 166 10082 7898 7418 275 29 -49 N ATOM 1216 CA VAL A 166 69.923 47.713 137.517 1.00 66.75 C ANISOU 1216 CA VAL A 166 10115 7837 7409 297 -32 -30 C ATOM 1217 C VAL A 166 69.991 49.106 138.150 1.00 66.78 C ANISOU 1217 C VAL A 166 10099 7844 7429 257 -27 -7 C ATOM 1218 O VAL A 166 71.010 49.792 138.033 1.00 67.12 O ANISOU 1218 O VAL A 166 10073 7919 7509 242 -12 -36 O ATOM 1219 CB VAL A 166 70.869 46.768 138.284 1.00 67.26 C ANISOU 1219 CB VAL A 166 10160 7888 7506 363 -91 -80 C ATOM 1220 CG1 VAL A 166 70.450 46.653 139.751 1.00 67.04 C ANISOU 1220 CG1 VAL A 166 10182 7815 7474 382 -156 -56 C ATOM 1221 CG2 VAL A 166 70.918 45.403 137.607 1.00 67.69 C ANISOU 1221 CG2 VAL A 166 10231 7934 7551 407 -95 -111 C ATOM 1222 N ILE A 167 68.913 49.507 138.823 1.00 66.18 N ANISOU 1222 N ILE A 167 10083 7733 7326 240 -41 42 N ATOM 1223 CA ILE A 167 68.776 50.861 139.376 1.00 65.96 C ANISOU 1223 CA ILE A 167 10051 7700 7308 202 -32 66 C ATOM 1224 C ILE A 167 67.957 50.880 140.663 1.00 65.65 C ANISOU 1224 C ILE A 167 10076 7619 7247 216 -77 97 C ATOM 1225 O ILE A 167 67.225 49.927 140.963 1.00 65.84 O ANISOU 1225 O ILE A 167 10153 7620 7241 243 -104 116 O ATOM 1226 CB ILE A 167 68.141 51.851 138.354 1.00 65.66 C ANISOU 1226 CB ILE A 167 10013 7679 7254 144 33 109 C ATOM 1227 CG1 ILE A 167 66.827 51.311 137.753 1.00 65.02 C ANISOU 1227 CG1 ILE A 167 9991 7590 7124 139 51 155 C ATOM 1228 CG2 ILE A 167 69.129 52.192 137.246 1.00 66.18 C ANISOU 1228 CG2 ILE A 167 10006 7793 7346 120 79 80 C ATOM 1229 CD1 ILE A 167 65.568 51.757 138.465 1.00 64.54 C ANISOU 1229 CD1 ILE A 167 9990 7496 7034 129 41 211 C ATOM 1230 N LYS A 168 68.104 51.970 141.421 1.00 65.52 N ANISOU 1230 N LYS A 168 10054 7594 7247 196 -84 100 N ATOM 1231 CA LYS A 168 67.194 52.278 142.522 1.00 65.05 C ANISOU 1231 CA LYS A 168 10054 7500 7158 201 -111 134 C ATOM 1232 C LYS A 168 65.842 52.611 141.907 1.00 64.32 C ANISOU 1232 C LYS A 168 10005 7402 7030 173 -65 193 C ATOM 1233 O LYS A 168 65.726 53.571 141.141 1.00 63.81 O ANISOU 1233 O LYS A 168 9921 7349 6974 133 -16 211 O ATOM 1234 CB LYS A 168 67.695 53.457 143.372 1.00 65.45 C ANISOU 1234 CB LYS A 168 10090 7543 7235 183 -124 117 C ATOM 1235 CG LYS A 168 66.659 53.976 144.366 1.00 65.33 C ANISOU 1235 CG LYS A 168 10138 7496 7186 184 -137 152 C ATOM 1236 CD LYS A 168 67.278 54.650 145.574 1.00 65.81 C ANISOU 1236 CD LYS A 168 10196 7545 7264 187 -178 120 C ATOM 1237 CE LYS A 168 66.188 55.177 146.499 1.00 65.84 C ANISOU 1237 CE LYS A 168 10266 7521 7229 191 -182 152 C ATOM 1238 NZ LYS A 168 66.718 55.605 147.824 1.00 66.48 N ANISOU 1238 NZ LYS A 168 10355 7590 7313 202 -232 117 N ATOM 1239 N CYS A 169 64.833 51.813 142.249 1.00 64.12 N ANISOU 1239 N CYS A 169 10036 7360 6965 194 -84 227 N ATOM 1240 CA CYS A 169 63.513 51.925 141.639 1.00 63.85 C ANISOU 1240 CA CYS A 169 10038 7326 6893 171 -47 286 C ATOM 1241 C CYS A 169 62.811 53.221 142.045 1.00 64.13 C ANISOU 1241 C CYS A 169 10094 7351 6922 149 -23 322 C ATOM 1242 O CYS A 169 62.340 53.360 143.175 1.00 64.07 O ANISOU 1242 O CYS A 169 10122 7323 6896 167 -49 335 O ATOM 1243 CB CYS A 169 62.650 50.719 142.009 1.00 63.58 C ANISOU 1243 CB CYS A 169 10057 7277 6820 196 -78 313 C ATOM 1244 SG CYS A 169 60.982 50.739 141.317 1.00 63.42 S ANISOU 1244 SG CYS A 169 10079 7263 6754 167 -40 388 S ATOM 1245 N GLU A 170 62.767 54.163 141.106 1.00 64.71 N ANISOU 1245 N GLU A 170 10142 7436 7008 111 28 339 N ATOM 1246 CA GLU A 170 62.105 55.448 141.286 1.00 65.15 C ANISOU 1246 CA GLU A 170 10214 7477 7063 90 56 375 C ATOM 1247 C GLU A 170 61.128 55.656 140.144 1.00 64.03 C ANISOU 1247 C GLU A 170 10080 7351 6898 62 105 431 C ATOM 1248 O GLU A 170 61.405 55.264 139.016 1.00 64.05 O ANISOU 1248 O GLU A 170 10055 7379 6900 44 127 428 O ATOM 1249 CB GLU A 170 63.140 56.569 141.295 1.00 66.84 C ANISOU 1249 CB GLU A 170 10386 7685 7322 65 67 340 C ATOM 1250 CG GLU A 170 64.070 56.539 142.502 1.00 68.48 C ANISOU 1250 CG GLU A 170 10587 7879 7552 88 16 286 C ATOM 1251 CD GLU A 170 65.331 57.364 142.303 1.00 70.25 C ANISOU 1251 CD GLU A 170 10755 8107 7827 58 22 245 C ATOM 1252 OE1 GLU A 170 66.034 57.142 141.286 1.00 71.76 O ANISOU 1252 OE1 GLU A 170 10896 8328 8038 39 45 230 O ATOM 1253 OE2 GLU A 170 65.629 58.222 143.172 1.00 70.80 O ANISOU 1253 OE2 GLU A 170 10831 8152 7914 52 3 225 O ATOM 1254 N PHE A 171 59.995 56.287 140.437 1.00 63.37 N ANISOU 1254 N PHE A 171 10030 7253 6792 61 121 482 N ATOM 1255 CA PHE A 171 58.936 56.506 139.446 1.00 62.75 C ANISOU 1255 CA PHE A 171 9960 7190 6689 39 162 544 C ATOM 1256 C PHE A 171 59.434 57.342 138.269 1.00 63.45 C ANISOU 1256 C PHE A 171 10011 7294 6804 0 206 548 C ATOM 1257 O PHE A 171 59.295 56.943 137.110 1.00 63.68 O ANISOU 1257 O PHE A 171 10025 7353 6817 -22 229 567 O ATOM 1258 CB PHE A 171 57.737 57.190 140.102 1.00 61.98 C ANISOU 1258 CB PHE A 171 9900 7076 6572 51 171 593 C ATOM 1259 CG PHE A 171 56.538 57.308 139.210 1.00 61.08 C ANISOU 1259 CG PHE A 171 9794 6981 6430 34 206 662 C ATOM 1260 CD1 PHE A 171 55.611 56.280 139.135 1.00 60.50 C ANISOU 1260 CD1 PHE A 171 9743 6928 6315 41 193 696 C ATOM 1261 CD2 PHE A 171 56.325 58.457 138.458 1.00 60.93 C ANISOU 1261 CD2 PHE A 171 9761 6960 6426 9 248 696 C ATOM 1262 CE1 PHE A 171 54.496 56.391 138.320 1.00 60.33 C ANISOU 1262 CE1 PHE A 171 9725 6929 6267 23 221 761 C ATOM 1263 CE2 PHE A 171 55.215 58.573 137.638 1.00 60.79 C ANISOU 1263 CE2 PHE A 171 9750 6965 6383 -5 276 763 C ATOM 1264 CZ PHE A 171 54.300 57.539 137.568 1.00 60.55 C ANISOU 1264 CZ PHE A 171 9736 6959 6309 2 262 795 C ATOM 1265 N GLU A 172 60.029 58.490 138.581 1.00 64.33 N ANISOU 1265 N GLU A 172 10107 7382 6952 -13 215 532 N ATOM 1266 CA GLU A 172 60.584 59.387 137.558 1.00 64.81 C ANISOU 1266 CA GLU A 172 10130 7452 7041 -56 255 539 C ATOM 1267 C GLU A 172 61.760 58.807 136.762 1.00 64.87 C ANISOU 1267 C GLU A 172 10088 7495 7064 -74 260 495 C ATOM 1268 O GLU A 172 62.080 59.323 135.689 1.00 65.95 O ANISOU 1268 O GLU A 172 10193 7653 7211 -112 299 511 O ATOM 1269 CB GLU A 172 60.966 60.757 138.148 1.00 65.72 C ANISOU 1269 CB GLU A 172 10246 7527 7197 -69 259 529 C ATOM 1270 CG GLU A 172 62.103 60.774 139.166 1.00 66.68 C ANISOU 1270 CG GLU A 172 10353 7631 7352 -58 220 461 C ATOM 1271 CD GLU A 172 61.610 60.849 140.602 1.00 67.23 C ANISOU 1271 CD GLU A 172 10468 7666 7409 -19 184 451 C ATOM 1272 OE1 GLU A 172 60.862 59.928 141.011 1.00 67.43 O ANISOU 1272 OE1 GLU A 172 10523 7701 7394 14 166 465 O ATOM 1273 OE2 GLU A 172 61.972 61.819 141.318 1.00 67.95 O ANISOU 1273 OE2 GLU A 172 10567 7721 7527 -25 175 428 O ATOM 1274 N LYS A 173 62.403 57.759 137.282 1.00 64.40 N ANISOU 1274 N LYS A 173 10020 7443 7006 -44 222 443 N ATOM 1275 CA LYS A 173 63.488 57.069 136.567 1.00 64.46 C ANISOU 1275 CA LYS A 173 9979 7486 7025 -49 225 398 C ATOM 1276 C LYS A 173 62.977 56.128 135.470 1.00 63.30 C ANISOU 1276 C LYS A 173 9838 7373 6838 -52 244 417 C ATOM 1277 O LYS A 173 63.653 55.966 134.456 1.00 63.41 O ANISOU 1277 O LYS A 173 9811 7425 6856 -71 272 398 O ATOM 1278 CB LYS A 173 64.364 56.296 137.559 1.00 65.37 C ANISOU 1278 CB LYS A 173 10084 7594 7160 -11 173 336 C ATOM 1279 CG LYS A 173 65.656 55.712 136.998 1.00 66.33 C ANISOU 1279 CG LYS A 173 10147 7750 7305 -9 174 281 C ATOM 1280 CD LYS A 173 66.636 56.779 136.547 1.00 67.26 C ANISOU 1280 CD LYS A 173 10206 7885 7463 -51 205 267 C ATOM 1281 CE LYS A 173 68.023 56.176 136.333 1.00 68.29 C ANISOU 1281 CE LYS A 173 10273 8051 7622 -38 196 205 C ATOM 1282 NZ LYS A 173 69.018 57.161 135.828 1.00 69.31 N ANISOU 1282 NZ LYS A 173 10337 8205 7791 -85 229 193 N ATOM 1283 N VAL A 174 61.809 55.511 135.676 1.00 62.09 N ANISOU 1283 N VAL A 174 9733 7210 6645 -34 230 453 N ATOM 1284 CA VAL A 174 61.246 54.548 134.705 1.00 61.78 C ANISOU 1284 CA VAL A 174 9708 7200 6566 -39 240 469 C ATOM 1285 C VAL A 174 60.050 55.081 133.902 1.00 61.38 C ANISOU 1285 C VAL A 174 9676 7163 6482 -70 275 542 C ATOM 1286 O VAL A 174 59.951 54.804 132.707 1.00 61.28 O ANISOU 1286 O VAL A 174 9652 7186 6444 -94 303 553 O ATOM 1287 CB VAL A 174 60.892 53.177 135.352 1.00 61.39 C ANISOU 1287 CB VAL A 174 9695 7134 6494 0 192 453 C ATOM 1288 CG1 VAL A 174 62.100 52.608 136.085 1.00 61.57 C ANISOU 1288 CG1 VAL A 174 9697 7145 6550 34 155 385 C ATOM 1289 CG2 VAL A 174 59.681 53.260 136.277 1.00 60.83 C ANISOU 1289 CG2 VAL A 174 9673 7036 6401 12 171 502 C ATOM 1290 N ILE A 175 59.152 55.830 134.545 1.00 60.80 N ANISOU 1290 N ILE A 175 9630 7063 6406 -68 275 589 N ATOM 1291 CA ILE A 175 57.979 56.390 133.862 1.00 60.32 C ANISOU 1291 CA ILE A 175 9585 7015 6318 -92 305 663 C ATOM 1292 C ILE A 175 58.344 57.747 133.256 1.00 60.51 C ANISOU 1292 C ILE A 175 9580 7041 6368 -125 347 684 C ATOM 1293 O ILE A 175 58.953 58.588 133.927 1.00 61.02 O ANISOU 1293 O ILE A 175 9635 7075 6473 -122 345 663 O ATOM 1294 CB ILE A 175 56.768 56.543 134.815 1.00 59.85 C ANISOU 1294 CB ILE A 175 9566 6930 6242 -68 288 708 C ATOM 1295 CG1 ILE A 175 56.385 55.191 135.449 1.00 59.62 C ANISOU 1295 CG1 ILE A 175 9567 6899 6186 -41 245 694 C ATOM 1296 CG2 ILE A 175 55.569 57.146 134.083 1.00 59.88 C ANISOU 1296 CG2 ILE A 175 9578 6951 6221 -90 319 786 C ATOM 1297 CD1 ILE A 175 55.782 54.164 134.499 1.00 59.65 C ANISOU 1297 CD1 ILE A 175 9580 6934 6149 -58 244 715 C ATOM 1298 N SER A 176 57.970 57.947 131.991 1.00 60.19 N ANISOU 1298 N SER A 176 9530 7036 6304 -160 382 726 N ATOM 1299 CA SER A 176 58.232 59.200 131.277 1.00 59.77 C ANISOU 1299 CA SER A 176 9452 6986 6270 -196 423 758 C ATOM 1300 C SER A 176 57.311 60.306 131.790 1.00 58.92 C ANISOU 1300 C SER A 176 9370 6841 6174 -190 429 816 C ATOM 1301 O SER A 176 56.096 60.120 131.855 1.00 58.27 O ANISOU 1301 O SER A 176 9316 6762 6062 -176 423 865 O ATOM 1302 CB SER A 176 58.024 59.008 129.769 1.00 59.96 C ANISOU 1302 CB SER A 176 9462 7064 6256 -233 455 791 C ATOM 1303 OG SER A 176 58.217 60.214 129.046 1.00 60.49 O ANISOU 1303 OG SER A 176 9507 7136 6338 -272 495 831 O ATOM 1304 N MET A 177 57.889 61.450 132.157 1.00 58.62 N ANISOU 1304 N MET A 177 9322 6767 6183 -199 440 809 N ATOM 1305 CA MET A 177 57.095 62.604 132.597 1.00 58.42 C ANISOU 1305 CA MET A 177 9322 6699 6173 -191 449 859 C ATOM 1306 C MET A 177 56.230 63.176 131.479 1.00 58.09 C ANISOU 1306 C MET A 177 9281 6678 6110 -216 483 941 C ATOM 1307 O MET A 177 55.103 63.608 131.731 1.00 57.46 O ANISOU 1307 O MET A 177 9228 6581 6022 -195 485 994 O ATOM 1308 CB MET A 177 57.983 63.692 133.204 1.00 58.93 C ANISOU 1308 CB MET A 177 9379 6715 6294 -200 450 828 C ATOM 1309 CG MET A 177 58.488 63.340 134.595 1.00 59.16 C ANISOU 1309 CG MET A 177 9421 6715 6343 -165 410 762 C ATOM 1310 SD MET A 177 57.165 63.194 135.821 1.00 58.94 S ANISOU 1310 SD MET A 177 9445 6658 6289 -109 386 782 S ATOM 1311 CE MET A 177 57.715 61.756 136.707 1.00 59.01 C ANISOU 1311 CE MET A 177 9454 6682 6281 -78 338 714 C ATOM 1312 N GLU A 178 56.751 63.142 130.252 1.00 58.24 N ANISOU 1312 N GLU A 178 9270 6738 6118 -259 509 950 N ATOM 1313 CA GLU A 178 55.985 63.513 129.055 1.00 58.24 C ANISOU 1313 CA GLU A 178 9268 6770 6088 -287 538 1027 C ATOM 1314 C GLU A 178 54.677 62.719 128.955 1.00 57.46 C ANISOU 1314 C GLU A 178 9192 6699 5938 -266 523 1067 C ATOM 1315 O GLU A 178 53.598 63.300 128.741 1.00 57.15 O ANISOU 1315 O GLU A 178 9168 6658 5889 -261 532 1139 O ATOM 1316 CB GLU A 178 56.830 63.308 127.799 1.00 58.77 C ANISOU 1316 CB GLU A 178 9299 6890 6138 -334 566 1018 C ATOM 1317 CG GLU A 178 57.972 64.306 127.673 1.00 59.77 C ANISOU 1317 CG GLU A 178 9398 6996 6314 -368 588 1003 C ATOM 1318 CD GLU A 178 58.981 63.918 126.610 1.00 60.66 C ANISOU 1318 CD GLU A 178 9468 7169 6411 -409 615 976 C ATOM 1319 OE1 GLU A 178 59.512 62.787 126.692 1.00 60.98 O ANISOU 1319 OE1 GLU A 178 9494 7240 6434 -394 601 912 O ATOM 1320 OE2 GLU A 178 59.255 64.745 125.704 1.00 61.51 O ANISOU 1320 OE2 GLU A 178 9556 7292 6522 -455 650 1020 O ATOM 1321 N TYR A 179 54.789 61.399 129.137 1.00 56.90 N ANISOU 1321 N TYR A 179 9125 6654 5839 -252 498 1020 N ATOM 1322 CA TYR A 179 53.622 60.517 129.233 1.00 56.33 C ANISOU 1322 CA TYR A 179 9076 6603 5723 -234 476 1048 C ATOM 1323 C TYR A 179 52.651 60.964 130.342 1.00 55.85 C ANISOU 1323 C TYR A 179 9041 6504 5675 -194 462 1081 C ATOM 1324 O TYR A 179 51.446 61.102 130.104 1.00 55.72 O ANISOU 1324 O TYR A 179 9034 6504 5633 -190 465 1148 O ATOM 1325 CB TYR A 179 54.057 59.050 129.441 1.00 56.15 C ANISOU 1325 CB TYR A 179 9056 6597 5679 -223 447 983 C ATOM 1326 CG TYR A 179 52.972 58.157 130.003 1.00 55.90 C ANISOU 1326 CG TYR A 179 9054 6569 5616 -199 415 1001 C ATOM 1327 CD1 TYR A 179 51.968 57.646 129.184 1.00 55.96 C ANISOU 1327 CD1 TYR A 179 9068 6618 5574 -220 413 1052 C ATOM 1328 CD2 TYR A 179 52.942 57.835 131.363 1.00 55.81 C ANISOU 1328 CD2 TYR A 179 9062 6520 5621 -160 384 971 C ATOM 1329 CE1 TYR A 179 50.971 56.834 129.693 1.00 55.91 C ANISOU 1329 CE1 TYR A 179 9085 6615 5540 -204 383 1072 C ATOM 1330 CE2 TYR A 179 51.944 57.030 131.887 1.00 55.64 C ANISOU 1330 CE2 TYR A 179 9065 6504 5570 -142 357 993 C ATOM 1331 CZ TYR A 179 50.960 56.535 131.055 1.00 55.83 C ANISOU 1331 CZ TYR A 179 9093 6568 5549 -166 356 1045 C ATOM 1332 OH TYR A 179 49.970 55.736 131.581 1.00 56.12 O ANISOU 1332 OH TYR A 179 9152 6611 5558 -154 328 1070 O ATOM 1333 N MET A 180 53.185 61.201 131.537 1.00 55.31 N ANISOU 1333 N MET A 180 8982 6389 5644 -165 447 1033 N ATOM 1334 CA MET A 180 52.351 61.567 132.687 1.00 54.91 C ANISOU 1334 CA MET A 180 8957 6304 5601 -122 435 1052 C ATOM 1335 C MET A 180 51.627 62.906 132.512 1.00 54.83 C ANISOU 1335 C MET A 180 8951 6271 5608 -117 463 1119 C ATOM 1336 O MET A 180 50.450 63.030 132.864 1.00 54.66 O ANISOU 1336 O MET A 180 8945 6252 5570 -89 462 1168 O ATOM 1337 CB MET A 180 53.179 61.578 133.980 1.00 54.98 C ANISOU 1337 CB MET A 180 8977 6270 5643 -95 412 982 C ATOM 1338 CG MET A 180 53.291 60.220 134.662 1.00 54.46 C ANISOU 1338 CG MET A 180 8921 6215 5553 -74 375 937 C ATOM 1339 SD MET A 180 51.852 59.852 135.689 1.00 54.09 S ANISOU 1339 SD MET A 180 8908 6168 5474 -33 356 978 S ATOM 1340 CE MET A 180 50.933 58.722 134.656 1.00 54.11 C ANISOU 1340 CE MET A 180 8906 6228 5424 -58 352 1026 C ATOM 1341 N VAL A 181 52.328 63.892 131.958 1.00 54.90 N ANISOU 1341 N VAL A 181 8947 6261 5651 -145 487 1122 N ATOM 1342 CA VAL A 181 51.773 65.233 131.763 1.00 55.38 C ANISOU 1342 CA VAL A 181 9015 6289 5736 -141 512 1183 C ATOM 1343 C VAL A 181 50.869 65.294 130.528 1.00 55.29 C ANISOU 1343 C VAL A 181 8992 6323 5690 -162 530 1267 C ATOM 1344 O VAL A 181 49.674 65.621 130.643 1.00 55.30 O ANISOU 1344 O VAL A 181 9004 6326 5681 -134 533 1328 O ATOM 1345 CB VAL A 181 52.898 66.292 131.675 1.00 56.00 C ANISOU 1345 CB VAL A 181 9086 6322 5867 -167 528 1158 C ATOM 1346 CG1 VAL A 181 52.357 67.667 131.289 1.00 56.52 C ANISOU 1346 CG1 VAL A 181 9162 6352 5960 -169 554 1227 C ATOM 1347 CG2 VAL A 181 53.629 66.368 133.006 1.00 56.05 C ANISOU 1347 CG2 VAL A 181 9107 6281 5908 -142 505 1081 C ATOM 1348 N TYR A 182 51.434 64.971 129.360 1.00 55.05 N ANISOU 1348 N TYR A 182 8940 6336 5641 -210 542 1268 N ATOM 1349 CA TYR A 182 50.706 65.141 128.097 1.00 55.05 C ANISOU 1349 CA TYR A 182 8928 6381 5606 -238 560 1348 C ATOM 1350 C TYR A 182 49.628 64.073 127.919 1.00 54.71 C ANISOU 1350 C TYR A 182 8887 6390 5507 -229 540 1375 C ATOM 1351 O TYR A 182 48.463 64.398 127.656 1.00 54.76 O ANISOU 1351 O TYR A 182 8896 6413 5497 -217 542 1450 O ATOM 1352 CB TYR A 182 51.652 65.135 126.888 1.00 55.27 C ANISOU 1352 CB TYR A 182 8932 6445 5623 -294 581 1340 C ATOM 1353 CG TYR A 182 52.785 66.154 126.940 1.00 55.51 C ANISOU 1353 CG TYR A 182 8952 6430 5707 -316 601 1317 C ATOM 1354 CD1 TYR A 182 52.546 67.487 127.294 1.00 55.76 C ANISOU 1354 CD1 TYR A 182 8999 6400 5785 -303 612 1358 C ATOM 1355 CD2 TYR A 182 54.095 65.789 126.605 1.00 55.41 C ANISOU 1355 CD2 TYR A 182 8915 6437 5700 -350 609 1256 C ATOM 1356 CE1 TYR A 182 53.578 68.420 127.322 1.00 55.99 C ANISOU 1356 CE1 TYR A 182 9022 6385 5865 -330 628 1338 C ATOM 1357 CE2 TYR A 182 55.132 66.710 126.643 1.00 55.69 C ANISOU 1357 CE2 TYR A 182 8936 6436 5785 -376 626 1238 C ATOM 1358 CZ TYR A 182 54.869 68.025 126.995 1.00 55.99 C ANISOU 1358 CZ TYR A 182 8993 6410 5869 -370 634 1280 C ATOM 1359 OH TYR A 182 55.896 68.940 127.028 1.00 56.12 O ANISOU 1359 OH TYR A 182 8998 6387 5937 -403 649 1264 O ATOM 1360 N PHE A 183 50.006 62.806 128.086 1.00 54.53 N ANISOU 1360 N PHE A 183 8865 6393 5459 -233 518 1316 N ATOM 1361 CA PHE A 183 49.081 61.704 127.836 1.00 54.58 C ANISOU 1361 CA PHE A 183 8876 6449 5413 -235 496 1338 C ATOM 1362 C PHE A 183 48.123 61.512 129.014 1.00 54.56 C ANISOU 1362 C PHE A 183 8890 6427 5412 -189 475 1351 C ATOM 1363 O PHE A 183 46.920 61.739 128.875 1.00 54.90 O ANISOU 1363 O PHE A 183 8931 6490 5437 -179 476 1423 O ATOM 1364 CB PHE A 183 49.843 60.411 127.503 1.00 54.29 C ANISOU 1364 CB PHE A 183 8838 6442 5348 -257 480 1270 C ATOM 1365 CG PHE A 183 48.997 59.354 126.866 1.00 54.01 C ANISOU 1365 CG PHE A 183 8807 6459 5255 -276 461 1295 C ATOM 1366 CD1 PHE A 183 48.640 59.453 125.531 1.00 54.31 C ANISOU 1366 CD1 PHE A 183 8834 6549 5253 -317 475 1345 C ATOM 1367 CD2 PHE A 183 48.557 58.254 127.597 1.00 53.57 C ANISOU 1367 CD2 PHE A 183 8769 6402 5182 -258 426 1271 C ATOM 1368 CE1 PHE A 183 47.863 58.472 124.930 1.00 54.38 C ANISOU 1368 CE1 PHE A 183 8848 6606 5205 -339 453 1366 C ATOM 1369 CE2 PHE A 183 47.773 57.278 127.008 1.00 53.68 C ANISOU 1369 CE2 PHE A 183 8789 6461 5144 -282 405 1295 C ATOM 1370 CZ PHE A 183 47.427 57.385 125.669 1.00 53.97 C ANISOU 1370 CZ PHE A 183 8814 6548 5141 -323 418 1340 C ATOM 1371 N ASN A 184 48.646 61.129 130.174 1.00 54.55 N ANISOU 1371 N ASN A 184 8904 6391 5432 -160 458 1287 N ATOM 1372 CA ASN A 184 47.790 60.794 131.313 1.00 54.87 C ANISOU 1372 CA ASN A 184 8961 6421 5467 -119 438 1295 C ATOM 1373 C ASN A 184 47.003 62.013 131.845 1.00 55.40 C ANISOU 1373 C ASN A 184 9031 6459 5557 -82 457 1347 C ATOM 1374 O ASN A 184 45.757 61.993 131.892 1.00 55.68 O ANISOU 1374 O ASN A 184 9063 6521 5571 -65 456 1410 O ATOM 1375 CB ASN A 184 48.630 60.147 132.422 1.00 54.89 C ANISOU 1375 CB ASN A 184 8978 6391 5484 -98 413 1214 C ATOM 1376 CG ASN A 184 47.812 59.776 133.641 1.00 55.03 C ANISOU 1376 CG ASN A 184 9015 6402 5491 -58 394 1222 C ATOM 1377 OD1 ASN A 184 48.074 60.245 134.746 1.00 55.14 O ANISOU 1377 OD1 ASN A 184 9042 6375 5530 -23 392 1191 O ATOM 1378 ND2 ASN A 184 46.815 58.935 133.444 1.00 55.25 N ANISOU 1378 ND2 ASN A 184 9043 6471 5477 -67 379 1263 N ATOM 1379 N PHE A 185 47.725 63.074 132.213 1.00 55.59 N ANISOU 1379 N PHE A 185 9061 6431 5629 -69 474 1322 N ATOM 1380 CA PHE A 185 47.105 64.214 132.898 1.00 55.66 C ANISOU 1380 CA PHE A 185 9082 6400 5667 -25 490 1354 C ATOM 1381 C PHE A 185 46.262 65.102 131.967 1.00 55.61 C ANISOU 1381 C PHE A 185 9062 6406 5661 -29 514 1442 C ATOM 1382 O PHE A 185 45.057 65.321 132.228 1.00 55.43 O ANISOU 1382 O PHE A 185 9036 6396 5626 5 518 1499 O ATOM 1383 CB PHE A 185 48.175 65.022 133.648 1.00 56.02 C ANISOU 1383 CB PHE A 185 9143 6378 5763 -13 494 1292 C ATOM 1384 CG PHE A 185 47.638 66.206 134.412 1.00 56.50 C ANISOU 1384 CG PHE A 185 9223 6388 5855 34 510 1312 C ATOM 1385 CD1 PHE A 185 46.540 66.079 135.257 1.00 56.56 C ANISOU 1385 CD1 PHE A 185 9241 6405 5844 84 507 1335 C ATOM 1386 CD2 PHE A 185 48.256 67.449 134.306 1.00 57.08 C ANISOU 1386 CD2 PHE A 185 9304 6403 5978 28 527 1305 C ATOM 1387 CE1 PHE A 185 46.054 67.171 135.961 1.00 57.08 C ANISOU 1387 CE1 PHE A 185 9325 6424 5936 134 524 1348 C ATOM 1388 CE2 PHE A 185 47.776 68.543 135.010 1.00 57.44 C ANISOU 1388 CE2 PHE A 185 9374 6394 6054 75 541 1318 C ATOM 1389 CZ PHE A 185 46.672 68.404 135.838 1.00 57.44 C ANISOU 1389 CZ PHE A 185 9384 6405 6033 131 540 1337 C ATOM 1390 N PHE A 186 46.881 65.598 130.891 1.00 55.65 N ANISOU 1390 N PHE A 186 9055 6411 5678 -71 530 1456 N ATOM 1391 CA PHE A 186 46.184 66.512 129.959 1.00 55.86 C ANISOU 1391 CA PHE A 186 9070 6445 5706 -77 551 1544 C ATOM 1392 C PHE A 186 45.080 65.858 129.117 1.00 55.83 C ANISOU 1392 C PHE A 186 9047 6515 5649 -92 543 1613 C ATOM 1393 O PHE A 186 44.070 66.510 128.835 1.00 55.65 O ANISOU 1393 O PHE A 186 9016 6501 5627 -71 553 1691 O ATOM 1394 CB PHE A 186 47.161 67.249 129.023 1.00 55.91 C ANISOU 1394 CB PHE A 186 9071 6434 5738 -123 571 1546 C ATOM 1395 CG PHE A 186 48.087 68.234 129.707 1.00 56.05 C ANISOU 1395 CG PHE A 186 9106 6373 5816 -113 581 1500 C ATOM 1396 CD1 PHE A 186 47.789 68.819 130.949 1.00 56.06 C ANISOU 1396 CD1 PHE A 186 9132 6316 5851 -58 579 1480 C ATOM 1397 CD2 PHE A 186 49.262 68.617 129.066 1.00 56.28 C ANISOU 1397 CD2 PHE A 186 9125 6389 5867 -163 594 1478 C ATOM 1398 CE1 PHE A 186 48.660 69.726 131.534 1.00 56.26 C ANISOU 1398 CE1 PHE A 186 9176 6268 5931 -55 585 1434 C ATOM 1399 CE2 PHE A 186 50.131 69.529 129.646 1.00 56.54 C ANISOU 1399 CE2 PHE A 186 9172 6351 5957 -162 601 1437 C ATOM 1400 CZ PHE A 186 49.831 70.082 130.884 1.00 56.56 C ANISOU 1400 CZ PHE A 186 9203 6291 5993 -109 594 1414 C ATOM 1401 N VAL A 187 45.264 64.598 128.709 1.00 55.84 N ANISOU 1401 N VAL A 187 9040 6567 5606 -127 524 1586 N ATOM 1402 CA VAL A 187 44.234 63.897 127.916 1.00 55.97 C ANISOU 1402 CA VAL A 187 9040 6655 5569 -148 511 1646 C ATOM 1403 C VAL A 187 43.275 63.058 128.772 1.00 55.85 C ANISOU 1403 C VAL A 187 9027 6662 5531 -119 488 1651 C ATOM 1404 O VAL A 187 42.061 63.102 128.560 1.00 55.91 O ANISOU 1404 O VAL A 187 9018 6707 5516 -109 484 1724 O ATOM 1405 CB VAL A 187 44.848 63.021 126.800 1.00 55.78 C ANISOU 1405 CB VAL A 187 9010 6679 5504 -208 503 1623 C ATOM 1406 CG1 VAL A 187 43.768 62.265 126.035 1.00 55.82 C ANISOU 1406 CG1 VAL A 187 9002 6755 5451 -233 484 1680 C ATOM 1407 CG2 VAL A 187 45.662 63.877 125.838 1.00 56.13 C ANISOU 1407 CG2 VAL A 187 9047 6715 5563 -241 530 1633 C ATOM 1408 N TRP A 188 43.810 62.295 129.723 1.00 55.88 N ANISOU 1408 N TRP A 188 9048 6645 5539 -108 471 1578 N ATOM 1409 CA TRP A 188 43.005 61.293 130.439 1.00 56.06 C ANISOU 1409 CA TRP A 188 9073 6694 5531 -93 446 1580 C ATOM 1410 C TRP A 188 42.598 61.652 131.880 1.00 56.32 C ANISOU 1410 C TRP A 188 9117 6694 5587 -34 449 1572 C ATOM 1411 O TRP A 188 41.820 60.913 132.494 1.00 55.87 O ANISOU 1411 O TRP A 188 9060 6664 5505 -22 432 1586 O ATOM 1412 CB TRP A 188 43.707 59.931 130.382 1.00 55.72 C ANISOU 1412 CB TRP A 188 9042 6663 5463 -126 418 1515 C ATOM 1413 CG TRP A 188 43.780 59.399 128.990 1.00 55.67 C ANISOU 1413 CG TRP A 188 9026 6704 5420 -181 412 1529 C ATOM 1414 CD1 TRP A 188 44.896 59.268 128.212 1.00 55.55 C ANISOU 1414 CD1 TRP A 188 9012 6687 5405 -215 419 1482 C ATOM 1415 CD2 TRP A 188 42.684 58.956 128.195 1.00 55.88 C ANISOU 1415 CD2 TRP A 188 9038 6791 5401 -210 399 1596 C ATOM 1416 NE1 TRP A 188 44.561 58.758 126.983 1.00 55.56 N ANISOU 1416 NE1 TRP A 188 9005 6743 5359 -260 412 1512 N ATOM 1417 CE2 TRP A 188 43.208 58.557 126.945 1.00 55.78 C ANISOU 1417 CE2 TRP A 188 9024 6810 5360 -261 397 1582 C ATOM 1418 CE3 TRP A 188 41.303 58.872 128.410 1.00 56.19 C ANISOU 1418 CE3 TRP A 188 9062 6865 5420 -199 388 1668 C ATOM 1419 CZ2 TRP A 188 42.399 58.075 125.912 1.00 56.08 C ANISOU 1419 CZ2 TRP A 188 9051 6908 5346 -302 382 1634 C ATOM 1420 CZ3 TRP A 188 40.496 58.385 127.383 1.00 56.46 C ANISOU 1420 CZ3 TRP A 188 9081 6962 5408 -242 372 1723 C ATOM 1421 CH2 TRP A 188 41.049 57.988 126.152 1.00 56.37 C ANISOU 1421 CH2 TRP A 188 9073 6978 5366 -293 367 1704 C ATOM 1422 N VAL A 189 43.111 62.762 132.420 1.00 56.97 N ANISOU 1422 N VAL A 189 9211 6718 5715 0 471 1550 N ATOM 1423 CA VAL A 189 42.605 63.280 133.707 1.00 57.69 C ANISOU 1423 CA VAL A 189 9313 6779 5824 60 480 1548 C ATOM 1424 C VAL A 189 41.787 64.578 133.555 1.00 58.67 C ANISOU 1424 C VAL A 189 9427 6891 5972 98 509 1616 C ATOM 1425 O VAL A 189 40.599 64.588 133.894 1.00 59.21 O ANISOU 1425 O VAL A 189 9480 6990 6023 131 513 1669 O ATOM 1426 CB VAL A 189 43.733 63.464 134.754 1.00 57.65 C ANISOU 1426 CB VAL A 189 9337 6714 5851 79 476 1460 C ATOM 1427 CG1 VAL A 189 43.183 64.014 136.071 1.00 57.61 C ANISOU 1427 CG1 VAL A 189 9348 6682 5857 143 486 1456 C ATOM 1428 CG2 VAL A 189 44.467 62.145 134.996 1.00 57.34 C ANISOU 1428 CG2 VAL A 189 9307 6688 5790 52 445 1397 C ATOM 1429 N LEU A 190 42.397 65.658 133.056 1.00 59.31 N ANISOU 1429 N LEU A 190 9514 6926 6092 93 528 1616 N ATOM 1430 CA LEU A 190 41.717 66.982 133.093 1.00 59.99 C ANISOU 1430 CA LEU A 190 9599 6982 6210 139 554 1671 C ATOM 1431 C LEU A 190 40.335 67.071 132.393 1.00 60.75 C ANISOU 1431 C LEU A 190 9662 7135 6282 149 560 1772 C ATOM 1432 O LEU A 190 39.373 67.619 132.976 1.00 61.14 O ANISOU 1432 O LEU A 190 9705 7182 6340 208 574 1811 O ATOM 1433 CB LEU A 190 42.634 68.101 132.584 1.00 60.09 C ANISOU 1433 CB LEU A 190 9626 6933 6270 123 571 1661 C ATOM 1434 CG LEU A 190 43.741 68.581 133.531 1.00 60.00 C ANISOU 1434 CG LEU A 190 9648 6847 6301 136 573 1575 C ATOM 1435 CD1 LEU A 190 44.619 69.609 132.823 1.00 60.22 C ANISOU 1435 CD1 LEU A 190 9683 6822 6373 105 587 1576 C ATOM 1436 CD2 LEU A 190 43.173 69.154 134.824 1.00 60.14 C ANISOU 1436 CD2 LEU A 190 9688 6826 6337 209 582 1560 C ATOM 1437 N PRO A 191 40.224 66.541 131.155 1.00 61.37 N ANISOU 1437 N PRO A 191 9719 7269 6329 94 548 1814 N ATOM 1438 CA PRO A 191 38.921 66.624 130.477 1.00 62.30 C ANISOU 1438 CA PRO A 191 9802 7445 6421 100 548 1911 C ATOM 1439 C PRO A 191 37.783 65.856 131.173 1.00 63.36 C ANISOU 1439 C PRO A 191 9916 7634 6523 127 536 1936 C ATOM 1440 O PRO A 191 36.677 66.424 131.312 1.00 64.27 O ANISOU 1440 O PRO A 191 10007 7767 6644 174 549 2003 O ATOM 1441 CB PRO A 191 39.207 66.106 129.057 1.00 61.97 C ANISOU 1441 CB PRO A 191 9747 7452 6346 28 534 1936 C ATOM 1442 CG PRO A 191 40.690 66.171 128.900 1.00 61.60 C ANISOU 1442 CG PRO A 191 9726 7359 6320 -5 538 1861 C ATOM 1443 CD PRO A 191 41.273 66.005 130.265 1.00 61.25 C ANISOU 1443 CD PRO A 191 9707 7264 6299 27 537 1778 C ATOM 1444 N PRO A 192 38.035 64.601 131.626 1.00 64.02 N ANISOU 1444 N PRO A 192 10007 7741 6575 99 513 1885 N ATOM 1445 CA PRO A 192 37.029 63.972 132.488 1.00 64.64 C ANISOU 1445 CA PRO A 192 10070 7861 6628 127 505 1904 C ATOM 1446 C PRO A 192 36.637 64.817 133.699 1.00 66.07 C ANISOU 1446 C PRO A 192 10258 8006 6839 206 532 1899 C ATOM 1447 O PRO A 192 35.440 64.973 133.964 1.00 66.70 O ANISOU 1447 O PRO A 192 10307 8127 6908 245 542 1961 O ATOM 1448 CB PRO A 192 37.710 62.677 132.937 1.00 63.90 C ANISOU 1448 CB PRO A 192 9999 7771 6510 90 478 1833 C ATOM 1449 CG PRO A 192 38.574 62.318 131.788 1.00 63.74 C ANISOU 1449 CG PRO A 192 9985 7752 6481 28 464 1811 C ATOM 1450 CD PRO A 192 39.053 63.618 131.195 1.00 63.73 C ANISOU 1450 CD PRO A 192 9986 7708 6517 38 490 1824 C ATOM 1451 N LEU A 193 37.631 65.366 134.404 1.00 67.33 N ANISOU 1451 N LEU A 193 10456 8092 7034 230 544 1826 N ATOM 1452 CA LEU A 193 37.378 66.193 135.593 1.00 68.70 C ANISOU 1452 CA LEU A 193 10644 8223 7233 305 569 1807 C ATOM 1453 C LEU A 193 36.517 67.405 135.263 1.00 69.91 C ANISOU 1453 C LEU A 193 10778 8370 7414 356 597 1878 C ATOM 1454 O LEU A 193 35.489 67.637 135.920 1.00 70.48 O ANISOU 1454 O LEU A 193 10832 8466 7481 415 614 1913 O ATOM 1455 CB LEU A 193 38.684 66.656 136.246 1.00 68.91 C ANISOU 1455 CB LEU A 193 10717 8169 7296 312 572 1715 C ATOM 1456 CG LEU A 193 39.550 65.592 136.923 1.00 69.14 C ANISOU 1456 CG LEU A 193 10769 8196 7304 284 546 1636 C ATOM 1457 CD1 LEU A 193 40.881 66.204 137.335 1.00 69.43 C ANISOU 1457 CD1 LEU A 193 10843 8154 7381 285 547 1555 C ATOM 1458 CD2 LEU A 193 38.847 64.972 138.124 1.00 69.40 C ANISOU 1458 CD2 LEU A 193 10802 8262 7305 321 543 1630 C ATOM 1459 N LEU A 194 36.926 68.157 134.240 1.00 70.85 N ANISOU 1459 N LEU A 194 10899 8457 7561 334 601 1903 N ATOM 1460 CA LEU A 194 36.163 69.345 133.835 1.00 72.33 C ANISOU 1460 CA LEU A 194 11071 8630 7779 382 625 1976 C ATOM 1461 C LEU A 194 34.739 68.983 133.357 1.00 72.92 C ANISOU 1461 C LEU A 194 11091 8792 7820 391 621 2071 C ATOM 1462 O LEU A 194 33.740 69.639 133.754 1.00 73.58 O ANISOU 1462 O LEU A 194 11154 8884 7918 461 642 2119 O ATOM 1463 CB LEU A 194 36.921 70.137 132.768 1.00 72.94 C ANISOU 1463 CB LEU A 194 11163 8660 7891 347 627 1990 C ATOM 1464 CG LEU A 194 38.263 70.744 133.215 1.00 73.30 C ANISOU 1464 CG LEU A 194 11257 8613 7979 341 634 1906 C ATOM 1465 CD1 LEU A 194 38.965 71.408 132.037 1.00 73.84 C ANISOU 1465 CD1 LEU A 194 11332 8649 8074 294 636 1931 C ATOM 1466 CD2 LEU A 194 38.097 71.727 134.368 1.00 73.66 C ANISOU 1466 CD2 LEU A 194 11332 8589 8065 421 657 1875 C ATOM 1467 N LEU A 195 34.651 67.922 132.545 1.00 72.63 N ANISOU 1467 N LEU A 195 11031 8824 7739 322 593 2095 N ATOM 1468 CA LEU A 195 33.350 67.418 132.082 1.00 72.65 C ANISOU 1468 CA LEU A 195 10980 8917 7705 317 581 2182 C ATOM 1469 C LEU A 195 32.423 67.027 133.254 1.00 73.07 C ANISOU 1469 C LEU A 195 11012 9010 7741 367 590 2186 C ATOM 1470 O LEU A 195 31.236 67.399 133.274 1.00 73.93 O ANISOU 1470 O LEU A 195 11076 9162 7848 413 603 2260 O ATOM 1471 CB LEU A 195 33.546 66.230 131.134 1.00 72.07 C ANISOU 1471 CB LEU A 195 10896 8903 7584 227 546 2188 C ATOM 1472 CG LEU A 195 32.305 65.617 130.465 1.00 72.14 C ANISOU 1472 CG LEU A 195 10851 9008 7549 202 524 2275 C ATOM 1473 CD1 LEU A 195 31.462 66.662 129.753 1.00 72.88 C ANISOU 1473 CD1 LEU A 195 10908 9120 7661 237 536 2371 C ATOM 1474 CD2 LEU A 195 32.722 64.526 129.492 1.00 71.74 C ANISOU 1474 CD2 LEU A 195 10803 8998 7454 111 489 2264 C ATOM 1475 N MET A 196 32.983 66.293 134.220 1.00 72.56 N ANISOU 1475 N MET A 196 10976 8930 7662 359 584 2109 N ATOM 1476 CA MET A 196 32.263 65.922 135.447 1.00 72.61 C ANISOU 1476 CA MET A 196 10970 8968 7650 404 595 2104 C ATOM 1477 C MET A 196 31.833 67.143 136.261 1.00 73.54 C ANISOU 1477 C MET A 196 11090 9047 7802 500 636 2108 C ATOM 1478 O MET A 196 30.672 67.230 136.691 1.00 74.18 O ANISOU 1478 O MET A 196 11130 9182 7871 550 654 2160 O ATOM 1479 CB MET A 196 33.119 65.017 136.336 1.00 71.85 C ANISOU 1479 CB MET A 196 10913 8850 7534 378 580 2016 C ATOM 1480 CG MET A 196 33.135 63.563 135.928 1.00 71.13 C ANISOU 1480 CG MET A 196 10813 8814 7399 300 541 2019 C ATOM 1481 SD MET A 196 34.015 62.566 137.139 1.00 70.81 S ANISOU 1481 SD MET A 196 10817 8745 7340 286 524 1925 S ATOM 1482 CE MET A 196 35.716 62.867 136.673 1.00 70.03 C ANISOU 1482 CE MET A 196 10768 8562 7276 256 514 1840 C ATOM 1483 N VAL A 197 32.775 68.069 136.468 1.00 74.00 N ANISOU 1483 N VAL A 197 11196 9014 7904 525 651 2050 N ATOM 1484 CA VAL A 197 32.480 69.355 137.127 1.00 75.08 C ANISOU 1484 CA VAL A 197 11346 9097 8081 616 688 2046 C ATOM 1485 C VAL A 197 31.327 70.091 136.429 1.00 76.35 C ANISOU 1485 C VAL A 197 11458 9291 8258 659 704 2146 C ATOM 1486 O VAL A 197 30.459 70.649 137.103 1.00 77.08 O ANISOU 1486 O VAL A 197 11533 9394 8360 740 734 2169 O ATOM 1487 CB VAL A 197 33.735 70.266 137.215 1.00 74.62 C ANISOU 1487 CB VAL A 197 11347 8930 8072 620 694 1974 C ATOM 1488 CG1 VAL A 197 33.375 71.702 137.598 1.00 75.09 C ANISOU 1488 CG1 VAL A 197 11422 8927 8180 708 728 1983 C ATOM 1489 CG2 VAL A 197 34.735 69.699 138.214 1.00 74.00 C ANISOU 1489 CG2 VAL A 197 11314 8820 7982 601 683 1873 C ATOM 1490 N LEU A 198 31.315 70.080 135.095 1.00 77.31 N ANISOU 1490 N LEU A 198 11559 9433 8380 607 684 2206 N ATOM 1491 CA LEU A 198 30.195 70.686 134.358 1.00 79.21 C ANISOU 1491 CA LEU A 198 11748 9714 8631 642 692 2309 C ATOM 1492 C LEU A 198 28.863 69.913 134.551 1.00 79.85 C ANISOU 1492 C LEU A 198 11763 9906 8669 653 689 2374 C ATOM 1493 O LEU A 198 27.795 70.510 134.864 1.00 81.00 O ANISOU 1493 O LEU A 198 11869 10080 8828 730 714 2429 O ATOM 1494 CB LEU A 198 30.537 70.795 132.871 1.00 79.97 C ANISOU 1494 CB LEU A 198 11840 9812 8731 577 668 2358 C ATOM 1495 CG LEU A 198 29.763 71.861 132.087 1.00 81.46 C ANISOU 1495 CG LEU A 198 11998 10000 8950 622 677 2453 C ATOM 1496 CD1 LEU A 198 30.220 73.269 132.461 1.00 81.83 C ANISOU 1496 CD1 LEU A 198 12091 9936 9062 690 707 2426 C ATOM 1497 CD2 LEU A 198 29.909 71.627 130.588 1.00 81.51 C ANISOU 1497 CD2 LEU A 198 11988 10043 8937 544 647 2512 C ATOM 1498 N ILE A 199 28.946 68.589 134.371 1.00 80.06 N ANISOU 1498 N ILE A 199 11777 9993 8646 574 657 2366 N ATOM 1499 CA ILE A 199 27.776 67.707 134.518 1.00 80.31 C ANISOU 1499 CA ILE A 199 11747 10131 8634 564 648 2425 C ATOM 1500 C ILE A 199 27.055 67.927 135.857 1.00 81.28 C ANISOU 1500 C ILE A 199 11853 10272 8757 648 684 2417 C ATOM 1501 O ILE A 199 25.819 68.027 135.889 1.00 81.64 O ANISOU 1501 O ILE A 199 11835 10390 8794 689 697 2494 O ATOM 1502 CB ILE A 199 28.160 66.213 134.353 1.00 79.34 C ANISOU 1502 CB ILE A 199 11632 10050 8462 468 608 2396 C ATOM 1503 CG1 ILE A 199 28.456 65.895 132.884 1.00 78.84 C ANISOU 1503 CG1 ILE A 199 11564 10004 8385 387 572 2428 C ATOM 1504 CG2 ILE A 199 27.059 65.283 134.857 1.00 79.69 C ANISOU 1504 CG2 ILE A 199 11623 10189 8463 460 601 2440 C ATOM 1505 CD1 ILE A 199 29.372 64.704 132.686 1.00 78.13 C ANISOU 1505 CD1 ILE A 199 11511 9910 8265 300 539 2365 C ATOM 1506 N TYR A 200 27.825 67.998 136.951 1.00 82.01 N ANISOU 1506 N TYR A 200 12000 10302 8856 674 701 2325 N ATOM 1507 CA TYR A 200 27.222 68.178 138.276 1.00 83.60 C ANISOU 1507 CA TYR A 200 12193 10521 9051 753 738 2309 C ATOM 1508 C TYR A 200 26.530 69.535 138.413 1.00 85.19 C ANISOU 1508 C TYR A 200 12375 10700 9293 857 779 2345 C ATOM 1509 O TYR A 200 25.367 69.577 138.811 1.00 86.71 O ANISOU 1509 O TYR A 200 12510 10963 9471 912 803 2400 O ATOM 1510 CB TYR A 200 28.231 67.926 139.412 1.00 83.12 C ANISOU 1510 CB TYR A 200 12198 10401 8982 754 742 2201 C ATOM 1511 CG TYR A 200 28.429 66.451 139.699 1.00 82.39 C ANISOU 1511 CG TYR A 200 12105 10359 8838 678 711 2181 C ATOM 1512 CD1 TYR A 200 27.385 65.675 140.202 1.00 82.68 C ANISOU 1512 CD1 TYR A 200 12091 10489 8831 678 715 2229 C ATOM 1513 CD2 TYR A 200 29.649 65.828 139.459 1.00 81.78 C ANISOU 1513 CD2 TYR A 200 12077 10235 8758 607 677 2116 C ATOM 1514 CE1 TYR A 200 27.551 64.321 140.463 1.00 82.21 C ANISOU 1514 CE1 TYR A 200 12036 10469 8727 607 683 2214 C ATOM 1515 CE2 TYR A 200 29.829 64.476 139.718 1.00 81.46 C ANISOU 1515 CE2 TYR A 200 12041 10233 8674 542 646 2098 C ATOM 1516 CZ TYR A 200 28.777 63.722 140.221 1.00 81.71 C ANISOU 1516 CZ TYR A 200 12028 10351 8664 541 648 2148 C ATOM 1517 OH TYR A 200 28.953 62.379 140.467 1.00 81.63 O ANISOU 1517 OH TYR A 200 12026 10373 8614 473 614 2134 O ATOM 1518 N LEU A 201 27.208 70.622 138.031 1.00 85.57 N ANISOU 1518 N LEU A 201 12467 10652 9393 883 786 2321 N ATOM 1519 CA LEU A 201 26.573 71.948 137.968 1.00 87.11 C ANISOU 1519 CA LEU A 201 12648 10816 9634 979 819 2363 C ATOM 1520 C LEU A 201 25.212 71.876 137.261 1.00 88.59 C ANISOU 1520 C LEU A 201 12747 11101 9810 995 818 2480 C ATOM 1521 O LEU A 201 24.186 72.366 137.794 1.00 90.00 O ANISOU 1521 O LEU A 201 12883 11316 9996 1085 853 2518 O ATOM 1522 CB LEU A 201 27.476 72.971 137.260 1.00 86.80 C ANISOU 1522 CB LEU A 201 12660 10667 9649 975 814 2345 C ATOM 1523 CG LEU A 201 28.698 73.481 138.024 1.00 86.64 C ANISOU 1523 CG LEU A 201 12724 10536 9658 987 824 2235 C ATOM 1524 CD1 LEU A 201 29.730 74.073 137.071 1.00 86.09 C ANISOU 1524 CD1 LEU A 201 12697 10381 9630 938 804 2225 C ATOM 1525 CD2 LEU A 201 28.288 74.497 139.080 1.00 87.51 C ANISOU 1525 CD2 LEU A 201 12854 10598 9797 1102 868 2204 C ATOM 1526 N GLU A 202 25.201 71.227 136.092 1.00 89.14 N ANISOU 1526 N GLU A 202 12790 11219 9860 908 777 2535 N ATOM 1527 CA GLU A 202 23.938 71.000 135.379 1.00 90.69 C ANISOU 1527 CA GLU A 202 12900 11519 10038 906 765 2647 C ATOM 1528 C GLU A 202 22.919 70.174 136.208 1.00 91.19 C ANISOU 1528 C GLU A 202 12902 11686 10057 921 778 2671 C ATOM 1529 O GLU A 202 21.709 70.529 136.279 1.00 92.17 O ANISOU 1529 O GLU A 202 12955 11878 10185 986 799 2746 O ATOM 1530 CB GLU A 202 24.197 70.328 134.025 1.00 91.29 C ANISOU 1530 CB GLU A 202 12965 11629 10090 799 715 2689 C ATOM 1531 CG GLU A 202 23.015 70.377 133.045 1.00 92.63 C ANISOU 1531 CG GLU A 202 13053 11890 10252 798 697 2810 C ATOM 1532 CD GLU A 202 22.620 71.789 132.616 1.00 93.90 C ANISOU 1532 CD GLU A 202 13201 12008 10466 883 717 2868 C ATOM 1533 OE1 GLU A 202 23.506 72.661 132.508 1.00 94.71 O ANISOU 1533 OE1 GLU A 202 13368 12004 10612 904 728 2825 O ATOM 1534 OE2 GLU A 202 21.421 72.018 132.373 1.00 94.50 O ANISOU 1534 OE2 GLU A 202 13202 12159 10543 929 721 2960 O ATOM 1535 N VAL A 203 23.410 69.099 136.840 1.00 90.81 N ANISOU 1535 N VAL A 203 12881 11653 9969 862 765 2609 N ATOM 1536 CA VAL A 203 22.549 68.238 137.667 1.00 90.93 C ANISOU 1536 CA VAL A 203 12846 11764 9939 863 775 2629 C ATOM 1537 C VAL A 203 21.884 69.035 138.794 1.00 91.72 C ANISOU 1537 C VAL A 203 12927 11868 10053 983 833 2623 C ATOM 1538 O VAL A 203 20.679 68.887 139.034 1.00 92.71 O ANISOU 1538 O VAL A 203 12974 12090 10160 1018 851 2692 O ATOM 1539 CB VAL A 203 23.313 67.013 138.243 1.00 90.24 C ANISOU 1539 CB VAL A 203 12802 11674 9809 785 752 2558 C ATOM 1540 CG1 VAL A 203 22.481 66.270 139.299 1.00 90.56 C ANISOU 1540 CG1 VAL A 203 12800 11800 9806 797 770 2573 C ATOM 1541 CG2 VAL A 203 23.730 66.060 137.122 1.00 89.53 C ANISOU 1541 CG2 VAL A 203 12717 11602 9698 668 696 2574 C ATOM 1542 N PHE A 204 22.664 69.880 139.468 1.00 92.08 N ANISOU 1542 N PHE A 204 13042 11811 10130 1044 861 2540 N ATOM 1543 CA PHE A 204 22.137 70.765 140.508 1.00 93.22 C ANISOU 1543 CA PHE A 204 13182 11945 10291 1164 918 2522 C ATOM 1544 C PHE A 204 21.155 71.763 139.915 1.00 94.72 C ANISOU 1544 C PHE A 204 13314 12154 10521 1244 938 2607 C ATOM 1545 O PHE A 204 20.021 71.890 140.419 1.00 96.44 O ANISOU 1545 O PHE A 204 13464 12450 10727 1316 973 2655 O ATOM 1546 CB PHE A 204 23.270 71.512 141.234 1.00 92.80 C ANISOU 1546 CB PHE A 204 13224 11766 10266 1204 936 2411 C ATOM 1547 CG PHE A 204 24.150 70.616 142.069 1.00 91.77 C ANISOU 1547 CG PHE A 204 13149 11623 10097 1147 923 2324 C ATOM 1548 CD1 PHE A 204 23.615 69.914 143.153 1.00 91.71 C ANISOU 1548 CD1 PHE A 204 13116 11691 10036 1162 944 2315 C ATOM 1549 CD2 PHE A 204 25.509 70.481 141.785 1.00 90.84 C ANISOU 1549 CD2 PHE A 204 13103 11418 9992 1080 890 2254 C ATOM 1550 CE1 PHE A 204 24.415 69.087 143.922 1.00 91.02 C ANISOU 1550 CE1 PHE A 204 13080 11591 9913 1111 928 2240 C ATOM 1551 CE2 PHE A 204 26.309 69.654 142.555 1.00 90.24 C ANISOU 1551 CE2 PHE A 204 13073 11331 9881 1033 875 2177 C ATOM 1552 CZ PHE A 204 25.764 68.965 143.633 1.00 90.30 C ANISOU 1552 CZ PHE A 204 13060 11411 9837 1049 893 2170 C ATOM 1553 N TYR A 205 21.585 72.442 138.841 1.00103.60 N ANISOU 1553 N TYR A 205 11362 11058 16940 2457 88 153 N ATOM 1554 CA TYR A 205 20.720 73.410 138.146 1.00103.64 C ANISOU 1554 CA TYR A 205 11412 11060 16906 2497 82 147 C ATOM 1555 C TYR A 205 19.332 72.830 137.838 1.00103.93 C ANISOU 1555 C TYR A 205 11428 11105 16954 2530 38 123 C ATOM 1556 O TYR A 205 18.310 73.470 138.155 1.00104.05 O ANISOU 1556 O TYR A 205 11449 11121 16961 2545 27 122 O ATOM 1557 CB TYR A 205 21.369 73.928 136.851 1.00103.94 C ANISOU 1557 CB TYR A 205 11502 11089 16900 2523 101 146 C ATOM 1558 CG TYR A 205 20.382 74.645 135.941 1.00104.28 C ANISOU 1558 CG TYR A 205 11585 11129 16905 2572 87 135 C ATOM 1559 CD1 TYR A 205 19.845 75.884 136.298 1.00104.49 C ANISOU 1559 CD1 TYR A 205 11641 11151 16908 2579 97 145 C ATOM 1560 CD2 TYR A 205 19.966 74.069 134.738 1.00104.53 C ANISOU 1560 CD2 TYR A 205 11625 11165 16926 2611 62 112 C ATOM 1561 CE1 TYR A 205 18.929 76.531 135.478 1.00104.83 C ANISOU 1561 CE1 TYR A 205 11721 11193 16917 2624 84 134 C ATOM 1562 CE2 TYR A 205 19.050 74.707 133.912 1.00104.79 C ANISOU 1562 CE2 TYR A 205 11694 11196 16924 2656 48 101 C ATOM 1563 CZ TYR A 205 18.529 75.936 134.288 1.00105.04 C ANISOU 1563 CZ TYR A 205 11754 11222 16932 2663 59 112 C ATOM 1564 OH TYR A 205 17.626 76.585 133.477 1.00105.83 O ANISOU 1564 OH TYR A 205 11891 11320 16997 2708 45 101 O ATOM 1565 N LEU A 206 19.307 71.632 137.233 1.00104.62 N ANISOU 1565 N LEU A 206 11491 11200 17060 2541 15 105 N ATOM 1566 CA LEU A 206 18.022 70.983 136.917 1.00105.37 C ANISOU 1566 CA LEU A 206 11563 11303 17168 2571 -27 80 C ATOM 1567 C LEU A 206 17.127 70.766 138.167 1.00105.88 C ANISOU 1567 C LEU A 206 11586 11375 17269 2553 -45 81 C ATOM 1568 O LEU A 206 15.928 71.141 138.187 1.00106.11 O ANISOU 1568 O LEU A 206 11617 11406 17290 2577 -67 72 O ATOM 1569 CB LEU A 206 18.246 69.653 136.191 1.00105.25 C ANISOU 1569 CB LEU A 206 11524 11294 17172 2580 -47 61 C ATOM 1570 CG LEU A 206 18.184 69.631 134.655 1.00105.51 C ANISOU 1570 CG LEU A 206 11592 11325 17170 2624 -56 44 C ATOM 1571 CD1 LEU A 206 19.063 70.686 134.003 1.00105.67 C ANISOU 1571 CD1 LEU A 206 11669 11334 17146 2631 -20 59 C ATOM 1572 CD2 LEU A 206 18.543 68.244 134.140 1.00105.72 C ANISOU 1572 CD2 LEU A 206 11588 11358 17222 2624 -73 28 C ATOM 1573 N ILE A 207 17.737 70.181 139.200 1.00106.32 N ANISOU 1573 N ILE A 207 11602 11433 17362 2509 -36 93 N ATOM 1574 CA ILE A 207 17.016 69.821 140.423 1.00106.87 C ANISOU 1574 CA ILE A 207 11626 11508 17469 2488 -53 94 C ATOM 1575 C ILE A 207 16.504 71.069 141.145 1.00107.34 C ANISOU 1575 C ILE A 207 11706 11564 17513 2484 -41 108 C ATOM 1576 O ILE A 207 15.336 71.112 141.560 1.00108.10 O ANISOU 1576 O ILE A 207 11786 11665 17620 2495 -64 100 O ATOM 1577 CB ILE A 207 17.868 68.949 141.383 1.00106.70 C ANISOU 1577 CB ILE A 207 11560 11490 17490 2441 -43 104 C ATOM 1578 CG1 ILE A 207 18.180 67.586 140.741 1.00106.62 C ANISOU 1578 CG1 ILE A 207 11524 11486 17501 2445 -61 87 C ATOM 1579 CG2 ILE A 207 17.120 68.705 142.698 1.00106.58 C ANISOU 1579 CG2 ILE A 207 11502 11480 17511 2418 -57 107 C ATOM 1580 CD1 ILE A 207 19.261 66.803 141.469 1.00106.47 C ANISOU 1580 CD1 ILE A 207 11470 11467 17514 2402 -46 98 C ATOM 1581 N ARG A 208 17.358 72.083 141.271 1.00108.02 N ANISOU 1581 N ARG A 208 11828 11642 17573 2470 -4 130 N ATOM 1582 CA ARG A 208 16.950 73.337 141.934 1.00108.94 C ANISOU 1582 CA ARG A 208 11966 11753 17671 2466 9 145 C ATOM 1583 C ARG A 208 15.796 74.022 141.177 1.00110.00 C ANISOU 1583 C ARG A 208 12133 11886 17773 2513 -8 132 C ATOM 1584 O ARG A 208 14.840 74.515 141.807 1.00109.50 O ANISOU 1584 O ARG A 208 12064 11825 17713 2517 -19 133 O ATOM 1585 CB ARG A 208 18.132 74.312 142.110 1.00108.83 C ANISOU 1585 CB ARG A 208 11987 11729 17633 2444 53 169 C ATOM 1586 CG ARG A 208 19.333 73.787 142.883 1.00108.64 C ANISOU 1586 CG ARG A 208 11935 11704 17637 2397 75 184 C ATOM 1587 CD ARG A 208 19.318 74.057 144.384 1.00108.30 C ANISOU 1587 CD ARG A 208 11865 11663 17620 2359 85 202 C ATOM 1588 NE ARG A 208 20.568 73.598 145.004 1.00107.90 N ANISOU 1588 NE ARG A 208 11793 11612 17592 2317 108 216 N ATOM 1589 CZ ARG A 208 20.778 73.439 146.314 1.00107.70 C ANISOU 1589 CZ ARG A 208 11734 11589 17598 2278 115 229 C ATOM 1590 NH1 ARG A 208 19.821 73.695 147.208 1.00107.82 N ANISOU 1590 NH1 ARG A 208 11730 11606 17627 2273 102 231 N ATOM 1591 NH2 ARG A 208 21.966 73.012 146.740 1.00107.25 N ANISOU 1591 NH2 ARG A 208 11660 11531 17559 2242 136 240 N ATOM 1592 N LYS A 209 15.858 74.010 139.839 1.00111.44 N ANISOU 1592 N LYS A 209 12347 12067 17926 2549 -13 118 N ATOM 1593 CA LYS A 209 14.769 74.551 139.018 1.00112.79 C ANISOU 1593 CA LYS A 209 12548 12238 18067 2596 -33 103 C ATOM 1594 C LYS A 209 13.474 73.736 139.161 1.00112.86 C ANISOU 1594 C LYS A 209 12518 12258 18104 2613 -76 81 C ATOM 1595 O LYS A 209 12.384 74.318 139.327 1.00112.93 O ANISOU 1595 O LYS A 209 12534 12269 18104 2633 -91 76 O ATOM 1596 CB LYS A 209 15.174 74.639 137.543 1.00114.18 C ANISOU 1596 CB LYS A 209 12765 12409 18206 2630 -29 94 C ATOM 1597 CG LYS A 209 14.264 75.542 136.715 1.00115.32 C ANISOU 1597 CG LYS A 209 12954 12551 18309 2677 -39 84 C ATOM 1598 CD LYS A 209 14.853 75.825 135.330 1.00116.53 C ANISOU 1598 CD LYS A 209 13156 12698 18421 2707 -26 80 C ATOM 1599 CE LYS A 209 14.614 74.670 134.364 1.00117.59 C ANISOU 1599 CE LYS A 209 13273 12840 18565 2733 -56 54 C ATOM 1600 NZ LYS A 209 13.175 74.487 134.009 1.00118.22 N ANISOU 1600 NZ LYS A 209 13344 12927 18644 2771 -96 31 N ATOM 1601 N GLN A 210 13.595 72.404 139.107 1.00113.18 N ANISOU 1601 N GLN A 210 12516 12306 18179 2604 -95 68 N ATOM 1602 CA GLN A 210 12.416 71.537 139.304 1.00113.76 C ANISOU 1602 CA GLN A 210 12548 12390 18284 2616 -135 46 C ATOM 1603 C GLN A 210 11.779 71.693 140.701 1.00115.02 C ANISOU 1603 C GLN A 210 12675 12552 18472 2590 -140 55 C ATOM 1604 O GLN A 210 10.535 71.722 140.833 1.00115.17 O ANISOU 1604 O GLN A 210 12683 12578 18498 2610 -167 41 O ATOM 1605 CB GLN A 210 12.747 70.071 139.019 1.00112.93 C ANISOU 1605 CB GLN A 210 12404 12291 18211 2609 -153 31 C ATOM 1606 CG GLN A 210 12.889 69.780 137.530 1.00112.82 C ANISOU 1606 CG GLN A 210 12417 12277 18172 2647 -162 14 C ATOM 1607 CD GLN A 210 13.338 68.362 137.238 1.00112.38 C ANISOU 1607 CD GLN A 210 12324 12226 18146 2638 -176 1 C ATOM 1608 OE1 GLN A 210 12.799 67.416 137.800 1.00112.35 O ANISOU 1608 OE1 GLN A 210 12273 12231 18184 2626 -200 -9 O ATOM 1609 NE2 GLN A 210 14.316 68.205 136.344 1.00112.26 N ANISOU 1609 NE2 GLN A 210 12332 12207 18112 2643 -161 1 N ATOM 1610 N LEU A 211 12.627 71.809 141.728 1.00116.31 N ANISOU 1610 N LEU A 211 12826 12713 18654 2546 -114 78 N ATOM 1611 CA LEU A 211 12.153 72.157 143.076 1.00116.98 C ANISOU 1611 CA LEU A 211 12887 12799 18760 2520 -112 90 C ATOM 1612 C LEU A 211 11.473 73.526 143.091 1.00118.56 C ANISOU 1612 C LEU A 211 13126 12995 18925 2540 -106 97 C ATOM 1613 O LEU A 211 10.382 73.672 143.658 1.00118.89 O ANISOU 1613 O LEU A 211 13151 13041 18979 2546 -125 91 O ATOM 1614 CB LEU A 211 13.302 72.140 144.099 1.00116.82 C ANISOU 1614 CB LEU A 211 12850 12775 18759 2470 -81 115 C ATOM 1615 CG LEU A 211 13.837 70.772 144.536 1.00116.97 C ANISOU 1615 CG LEU A 211 12820 12800 18823 2440 -88 111 C ATOM 1616 CD1 LEU A 211 15.155 70.932 145.279 1.00116.87 C ANISOU 1616 CD1 LEU A 211 12804 12782 18817 2397 -53 136 C ATOM 1617 CD2 LEU A 211 12.820 70.044 145.406 1.00116.56 C ANISOU 1617 CD2 LEU A 211 12718 12756 18812 2432 -118 101 C ATOM 1618 N ALA A1001 12.114 74.513 142.458 1.00120.62 N ANISOU 1618 N ALA A1001 13439 13247 19144 2551 -79 108 N ATOM 1619 CA ALA A1001 11.543 75.866 142.350 1.00121.71 C ANISOU 1619 CA ALA A1001 13619 13379 19244 2573 -70 114 C ATOM 1620 C ALA A1001 10.165 75.881 141.674 1.00123.49 C ANISOU 1620 C ALA A1001 13852 13611 19458 2619 -105 91 C ATOM 1621 O ALA A1001 9.257 76.588 142.141 1.00124.42 O ANISOU 1621 O ALA A1001 13974 13729 19569 2628 -113 92 O ATOM 1622 CB ALA A1001 12.499 76.797 141.614 1.00121.79 C ANISOU 1622 CB ALA A1001 13684 13378 19210 2580 -37 128 C ATOM 1623 N ASP A1002 10.010 75.096 140.602 1.00125.48 N ANISOU 1623 N ASP A1002 14101 13866 19707 2648 -127 69 N ATOM 1624 CA ASP A1002 8.726 75.022 139.875 1.00126.92 C ANISOU 1624 CA ASP A1002 14288 14054 19879 2693 -162 44 C ATOM 1625 C ASP A1002 7.558 74.479 140.725 1.00127.15 C ANISOU 1625 C ASP A1002 14270 14093 19946 2688 -193 32 C ATOM 1626 O ASP A1002 6.431 74.998 140.654 1.00127.23 O ANISOU 1626 O ASP A1002 14290 14106 19944 2715 -211 22 O ATOM 1627 CB ASP A1002 8.869 74.177 138.599 1.00127.85 C ANISOU 1627 CB ASP A1002 14409 14175 19990 2722 -179 23 C ATOM 1628 CG ASP A1002 9.729 74.845 137.531 1.00128.75 C ANISOU 1628 CG ASP A1002 14578 14280 20059 2740 -154 29 C ATOM 1629 OD1 ASP A1002 10.369 75.885 137.807 1.00129.73 O ANISOU 1629 OD1 ASP A1002 14736 14395 20159 2726 -120 52 O ATOM 1630 OD2 ASP A1002 9.767 74.317 136.399 1.00129.35 O ANISOU 1630 OD2 ASP A1002 14664 14358 20124 2769 -168 12 O ATOM 1631 N LEU A1003 7.828 73.447 141.522 1.00127.51 N ANISOU 1631 N LEU A1003 14266 14144 20038 2653 -198 33 N ATOM 1632 CA LEU A1003 6.807 72.897 142.427 1.00127.92 C ANISOU 1632 CA LEU A1003 14269 14203 20128 2644 -225 24 C ATOM 1633 C LEU A1003 6.362 73.899 143.494 1.00128.66 C ANISOU 1633 C LEU A1003 14368 14295 20220 2628 -213 41 C ATOM 1634 O LEU A1003 5.159 74.024 143.769 1.00128.84 O ANISOU 1634 O LEU A1003 14379 14323 20250 2644 -237 30 O ATOM 1635 CB LEU A1003 7.306 71.615 143.095 1.00127.77 C ANISOU 1635 CB LEU A1003 14197 14189 20157 2607 -229 24 C ATOM 1636 CG LEU A1003 7.478 70.405 142.167 1.00128.19 C ANISOU 1636 CG LEU A1003 14234 14248 20223 2622 -249 3 C ATOM 1637 CD1 LEU A1003 8.114 69.274 142.943 1.00128.42 C ANISOU 1637 CD1 LEU A1003 14214 14280 20298 2582 -247 8 C ATOM 1638 CD2 LEU A1003 6.153 69.934 141.574 1.00128.19 C ANISOU 1638 CD2 LEU A1003 14220 14256 20228 2661 -289 -26 C ATOM 1639 N GLU A1004 7.323 74.610 144.088 1.00130.23 N ANISOU 1639 N GLU A1004 14584 14486 20409 2598 -177 68 N ATOM 1640 CA GLU A1004 7.001 75.684 145.048 1.00132.04 C ANISOU 1640 CA GLU A1004 14824 14712 20631 2584 -163 86 C ATOM 1641 C GLU A1004 6.302 76.866 144.357 1.00134.01 C ANISOU 1641 C GLU A1004 15123 14957 20835 2624 -164 82 C ATOM 1642 O GLU A1004 5.428 77.507 144.957 1.00133.35 O ANISOU 1642 O GLU A1004 15040 14875 20750 2628 -171 84 O ATOM 1643 CB GLU A1004 8.252 76.178 145.792 1.00131.88 C ANISOU 1643 CB GLU A1004 14813 14684 20610 2542 -123 115 C ATOM 1644 CG GLU A1004 7.935 76.957 147.069 1.00131.75 C ANISOU 1644 CG GLU A1004 14789 14666 20601 2517 -111 133 C ATOM 1645 CD GLU A1004 9.125 77.715 147.636 1.00131.59 C ANISOU 1645 CD GLU A1004 14789 14636 20569 2483 -69 162 C ATOM 1646 OE1 GLU A1004 10.265 77.213 147.545 1.00132.34 O ANISOU 1646 OE1 GLU A1004 14879 14729 20673 2461 -52 169 O ATOM 1647 OE2 GLU A1004 8.917 78.817 148.189 1.00131.36 O ANISOU 1647 OE2 GLU A1004 14782 14603 20523 2479 -54 176 O ATOM 1648 N ASP A1005 6.687 77.145 143.107 1.00136.05 N ANISOU 1648 N ASP A1005 15423 15211 21056 2654 -158 76 N ATOM 1649 CA ASP A1005 5.998 78.147 142.282 1.00137.73 C ANISOU 1649 CA ASP A1005 15683 15421 21225 2697 -163 69 C ATOM 1650 C ASP A1005 4.527 77.760 142.066 1.00139.78 C ANISOU 1650 C ASP A1005 15923 15691 21495 2730 -204 43 C ATOM 1651 O ASP A1005 3.629 78.576 142.317 1.00141.22 O ANISOU 1651 O ASP A1005 16120 15873 21663 2746 -211 43 O ATOM 1652 CB ASP A1005 6.714 78.332 140.933 1.00137.94 C ANISOU 1652 CB ASP A1005 15754 15442 21213 2724 -151 66 C ATOM 1653 CG ASP A1005 6.177 79.511 140.132 1.00138.45 C ANISOU 1653 CG ASP A1005 15874 15501 21228 2765 -149 63 C ATOM 1654 OD1 ASP A1005 6.111 80.633 140.678 1.00139.01 O ANISOU 1654 OD1 ASP A1005 15969 15566 21280 2758 -129 81 O ATOM 1655 OD2 ASP A1005 5.833 79.317 138.946 1.00138.43 O ANISOU 1655 OD2 ASP A1005 15891 15501 21204 2806 -166 44 O ATOM 1656 N ASN A1006 4.287 76.521 141.626 1.00140.84 N ANISOU 1656 N ASN A1006 16024 15832 21654 2739 -232 21 N ATOM 1657 CA ASN A1006 2.910 76.010 141.467 1.00141.91 C ANISOU 1657 CA ASN A1006 16135 15978 21806 2767 -273 -4 C ATOM 1658 C ASN A1006 2.129 75.968 142.788 1.00142.88 C ANISOU 1658 C ASN A1006 16218 16105 21962 2744 -283 -1 C ATOM 1659 O ASN A1006 0.943 76.318 142.818 1.00142.78 O ANISOU 1659 O ASN A1006 16206 16098 21946 2768 -305 -13 O ATOM 1660 CB ASN A1006 2.903 74.607 140.843 1.00142.86 C ANISOU 1660 CB ASN A1006 16222 16106 21951 2776 -298 -27 C ATOM 1661 CG ASN A1006 3.273 74.607 139.376 1.00144.30 C ANISOU 1661 CG ASN A1006 16442 16285 22098 2812 -299 -39 C ATOM 1662 OD1 ASN A1006 2.862 75.482 138.614 1.00145.24 O ANISOU 1662 OD1 ASN A1006 16605 16401 22176 2849 -299 -43 O ATOM 1663 ND2 ASN A1006 4.035 73.598 138.964 1.00144.87 N ANISOU 1663 ND2 ASN A1006 16497 16359 22187 2802 -299 -44 N ATOM 1664 N TRP A1007 2.795 75.528 143.860 1.00145.28 N ANISOU 1664 N TRP A1007 16488 16409 22301 2697 -268 15 N ATOM 1665 CA TRP A1007 2.185 75.480 145.196 1.00146.87 C ANISOU 1665 CA TRP A1007 16653 16615 22536 2670 -274 21 C ATOM 1666 C TRP A1007 1.807 76.871 145.710 1.00148.60 C ANISOU 1666 C TRP A1007 16902 16828 22728 2672 -259 37 C ATOM 1667 O TRP A1007 0.715 77.057 146.254 1.00149.54 O ANISOU 1667 O TRP A1007 17006 16952 22859 2678 -277 30 O ATOM 1668 CB TRP A1007 3.122 74.797 146.196 1.00147.35 C ANISOU 1668 CB TRP A1007 16676 16674 22634 2619 -257 38 C ATOM 1669 CG TRP A1007 2.562 74.668 147.604 1.00147.61 C ANISOU 1669 CG TRP A1007 16669 16711 22705 2589 -262 45 C ATOM 1670 CD1 TRP A1007 3.066 75.246 148.733 1.00147.63 C ANISOU 1670 CD1 TRP A1007 16669 16709 22714 2552 -236 71 C ATOM 1671 CD2 TRP A1007 1.411 73.915 148.019 1.00147.86 C ANISOU 1671 CD2 TRP A1007 16656 16751 22770 2594 -296 26 C ATOM 1672 NE1 TRP A1007 2.308 74.900 149.824 1.00147.08 N ANISOU 1672 NE1 TRP A1007 16558 16645 22681 2533 -251 70 N ATOM 1673 CE2 TRP A1007 1.284 74.087 149.416 1.00147.53 C ANISOU 1673 CE2 TRP A1007 16588 16709 22755 2558 -287 42 C ATOM 1674 CE3 TRP A1007 0.476 73.112 147.347 1.00148.23 C ANISOU 1674 CE3 TRP A1007 16684 16807 22830 2624 -332 -3 C ATOM 1675 CZ2 TRP A1007 0.262 73.485 150.161 1.00147.65 C ANISOU 1675 CZ2 TRP A1007 16559 16732 22808 2552 -313 30 C ATOM 1676 CZ3 TRP A1007 -0.555 72.514 148.091 1.00148.25 C ANISOU 1676 CZ3 TRP A1007 16641 16816 22869 2618 -358 -15 C ATOM 1677 CH2 TRP A1007 -0.638 72.695 149.488 1.00147.96 C ANISOU 1677 CH2 TRP A1007 16579 16778 22858 2582 -348 1 C ATOM 1678 N GLU A1008 2.708 77.837 145.537 1.00150.21 N ANISOU 1678 N GLU A1008 17151 17023 22899 2666 -225 58 N ATOM 1679 CA GLU A1008 2.429 79.226 145.929 1.00150.78 C ANISOU 1679 CA GLU A1008 17257 17089 22942 2669 -208 74 C ATOM 1680 C GLU A1008 1.387 79.893 145.017 1.00151.63 C ANISOU 1680 C GLU A1008 17399 17197 23014 2721 -227 57 C ATOM 1681 O GLU A1008 0.564 80.672 145.500 1.00152.43 O ANISOU 1681 O GLU A1008 17509 17299 23108 2728 -232 60 O ATOM 1682 CB GLU A1008 3.713 80.061 145.982 1.00150.64 C ANISOU 1682 CB GLU A1008 17276 17060 22898 2649 -165 101 C ATOM 1683 CG GLU A1008 3.542 81.383 146.728 1.00150.50 C ANISOU 1683 CG GLU A1008 17284 17036 22861 2639 -145 121 C ATOM 1684 CD GLU A1008 4.855 82.057 147.096 1.00150.56 C ANISOU 1684 CD GLU A1008 17316 17034 22855 2607 -102 149 C ATOM 1685 OE1 GLU A1008 5.899 81.713 146.503 1.00151.47 O ANISOU 1685 OE1 GLU A1008 17442 17145 22963 2602 -86 152 O ATOM 1686 OE2 GLU A1008 4.839 82.941 147.983 1.00149.91 O ANISOU 1686 OE2 GLU A1008 17242 16947 22768 2588 -83 168 O ATOM 1687 N THR A1009 1.423 79.586 143.716 1.00151.65 N ANISOU 1687 N THR A1009 17423 17201 22995 2756 -239 40 N ATOM 1688 CA THR A1009 0.390 80.056 142.775 1.00151.96 C ANISOU 1688 CA THR A1009 17491 17242 23003 2807 -262 20 C ATOM 1689 C THR A1009 -1.016 79.608 143.197 1.00152.18 C ANISOU 1689 C THR A1009 17481 17281 23059 2819 -299 0 C ATOM 1690 O THR A1009 -1.957 80.413 143.217 1.00152.62 O ANISOU 1690 O THR A1009 17555 17338 23095 2843 -308 -4 O ATOM 1691 CB THR A1009 0.663 79.559 141.336 1.00151.98 C ANISOU 1691 CB THR A1009 17513 17245 22985 2841 -272 2 C ATOM 1692 OG1 THR A1009 1.955 80.005 140.911 1.00152.29 O ANISOU 1692 OG1 THR A1009 17590 17275 22998 2831 -237 20 O ATOM 1693 CG2 THR A1009 -0.394 80.078 140.354 1.00152.21 C ANISOU 1693 CG2 THR A1009 17575 17278 22981 2895 -295 -18 C ATOM 1694 N LEU A1010 -1.141 78.329 143.543 1.00151.46 N ANISOU 1694 N LEU A1010 17337 17197 23011 2802 -319 -12 N ATOM 1695 CA LEU A1010 -2.428 77.746 143.946 1.00150.77 C ANISOU 1695 CA LEU A1010 17209 17120 22956 2811 -354 -33 C ATOM 1696 C LEU A1010 -2.975 78.353 145.252 1.00151.03 C ANISOU 1696 C LEU A1010 17226 17153 23003 2788 -349 -19 C ATOM 1697 O LEU A1010 -4.182 78.553 145.376 1.00150.44 O ANISOU 1697 O LEU A1010 17145 17084 22931 2809 -373 -33 O ATOM 1698 CB LEU A1010 -2.298 76.224 144.090 1.00149.48 C ANISOU 1698 CB LEU A1010 16992 16964 22838 2793 -372 -47 C ATOM 1699 CG LEU A1010 -3.580 75.398 144.112 1.00148.76 C ANISOU 1699 CG LEU A1010 16860 16883 22777 2811 -413 -75 C ATOM 1700 CD1 LEU A1010 -4.211 75.348 142.733 1.00148.71 C ANISOU 1700 CD1 LEU A1010 16877 16881 22743 2863 -438 -102 C ATOM 1701 CD2 LEU A1010 -3.283 73.985 144.588 1.00148.44 C ANISOU 1701 CD2 LEU A1010 16765 16848 22786 2780 -423 -81 C ATOM 1702 N ASN A1011 -2.081 78.634 146.207 1.00151.91 N ANISOU 1702 N ASN A1011 17334 17258 23125 2744 -318 8 N ATOM 1703 CA ASN A1011 -2.458 79.169 147.538 1.00152.56 C ANISOU 1703 CA ASN A1011 17400 17340 23223 2717 -310 24 C ATOM 1704 C ASN A1011 -2.749 80.677 147.564 1.00153.90 C ANISOU 1704 C ASN A1011 17618 17504 23353 2733 -295 37 C ATOM 1705 O ASN A1011 -3.555 81.132 148.384 1.00154.38 O ANISOU 1705 O ASN A1011 17667 17567 23422 2728 -301 39 O ATOM 1706 CB ASN A1011 -1.374 78.862 148.586 1.00152.33 C ANISOU 1706 CB ASN A1011 17347 17307 23222 2664 -283 48 C ATOM 1707 CG ASN A1011 -1.293 77.386 148.946 1.00152.74 C ANISOU 1707 CG ASN A1011 17342 17366 23323 2642 -300 37 C ATOM 1708 OD1 ASN A1011 -1.971 76.546 148.356 1.00153.56 O ANISOU 1708 OD1 ASN A1011 17427 17478 23441 2665 -331 11 O ATOM 1709 ND2 ASN A1011 -0.459 77.069 149.928 1.00152.61 N ANISOU 1709 ND2 ASN A1011 17302 17348 23335 2596 -280 57 N ATOM 1710 N ASP A1012 -2.063 81.446 146.717 1.00155.04 N ANISOU 1710 N ASP A1012 17814 17641 23454 2750 -273 45 N ATOM 1711 CA ASP A1012 -2.375 82.868 146.546 1.00155.64 C ANISOU 1711 CA ASP A1012 17939 17710 23486 2771 -260 55 C ATOM 1712 C ASP A1012 -3.780 83.050 145.969 1.00157.17 C ANISOU 1712 C ASP A1012 18139 17910 23666 2817 -294 30 C ATOM 1713 O ASP A1012 -4.601 83.762 146.555 1.00157.32 O ANISOU 1713 O ASP A1012 18161 17930 23681 2821 -299 33 O ATOM 1714 CB ASP A1012 -1.346 83.545 145.635 1.00155.54 C ANISOU 1714 CB ASP A1012 17979 17687 23429 2782 -231 67 C ATOM 1715 CG ASP A1012 0.025 83.684 146.289 1.00155.35 C ANISOU 1715 CG ASP A1012 17957 17655 23412 2737 -193 95 C ATOM 1716 OD1 ASP A1012 0.255 83.106 147.374 1.00155.14 O ANISOU 1716 OD1 ASP A1012 17887 17632 23426 2697 -190 104 O ATOM 1717 OD2 ASP A1012 0.886 84.383 145.711 1.00155.63 O ANISOU 1717 OD2 ASP A1012 18037 17682 23412 2741 -165 108 O ATOM 1718 N ASN A1013 -4.038 82.387 144.846 1.00159.07 N ANISOU 1718 N ASN A1013 18381 18155 23900 2851 -317 6 N ATOM 1719 CA ASN A1013 -5.339 82.459 144.174 1.00160.19 C ANISOU 1719 CA ASN A1013 18530 18305 24030 2897 -351 -20 C ATOM 1720 C ASN A1013 -6.464 81.900 145.033 1.00159.98 C ANISOU 1720 C ASN A1013 18452 18288 24044 2890 -380 -34 C ATOM 1721 O ASN A1013 -7.531 82.493 145.104 1.00159.13 O ANISOU 1721 O ASN A1013 18352 18183 23924 2913 -396 -43 O ATOM 1722 CB ASN A1013 -5.294 81.690 142.865 1.00161.03 C ANISOU 1722 CB ASN A1013 18641 18415 24127 2930 -370 -44 C ATOM 1723 CG ASN A1013 -4.338 82.296 141.841 1.00161.41 C ANISOU 1723 CG ASN A1013 18743 18453 24130 2947 -345 -34 C ATOM 1724 OD1 ASN A1013 -3.624 83.267 142.112 1.00161.34 O ANISOU 1724 OD1 ASN A1013 18769 18435 24098 2931 -312 -9 O ATOM 1725 ND2 ASN A1013 -4.314 81.706 140.654 1.00161.81 N ANISOU 1725 ND2 ASN A1013 18802 18507 24170 2978 -362 -54 N ATOM 1726 N VAL A1026 -11.875 86.581 139.498 1.00187.28 N ANISOU 1726 N VAL A1026 22152 21754 27251 3211 -480 -131 N ATOM 1727 CA VAL A1026 -12.111 85.141 139.595 1.00187.33 C ANISOU 1727 CA VAL A1026 22101 21770 27304 3200 -507 -152 C ATOM 1728 C VAL A1026 -11.541 84.411 138.371 1.00188.99 C ANISOU 1728 C VAL A1026 22321 21980 27503 3221 -512 -166 C ATOM 1729 O VAL A1026 -10.884 83.378 138.519 1.00189.57 O ANISOU 1729 O VAL A1026 22362 22055 27609 3193 -511 -166 O ATOM 1730 CB VAL A1026 -13.618 84.817 139.773 1.00186.58 C ANISOU 1730 CB VAL A1026 21974 21687 27229 3223 -547 -180 C ATOM 1731 CG1 VAL A1026 -13.856 83.308 139.812 1.00185.91 C ANISOU 1731 CG1 VAL A1026 21831 21612 27192 3213 -574 -202 C ATOM 1732 CG2 VAL A1026 -14.167 85.482 141.032 1.00186.26 C ANISOU 1732 CG2 VAL A1026 21921 21646 27201 3200 -541 -166 C ATOM 1733 N LYS A1027 -11.789 84.952 137.175 1.00190.17 N ANISOU 1733 N LYS A1027 22518 22129 27608 3270 -519 -178 N ATOM 1734 CA LYS A1027 -11.298 84.363 135.913 1.00190.06 C ANISOU 1734 CA LYS A1027 22519 22115 27579 3295 -525 -192 C ATOM 1735 C LYS A1027 -9.765 84.323 135.847 1.00189.99 C ANISOU 1735 C LYS A1027 22526 22095 27563 3264 -488 -167 C ATOM 1736 O LYS A1027 -9.173 83.293 135.479 1.00190.12 O ANISOU 1736 O LYS A1027 22522 22115 27600 3254 -492 -174 O ATOM 1737 CB LYS A1027 -11.853 85.139 134.712 1.00189.51 C ANISOU 1737 CB LYS A1027 22502 22045 27457 3353 -536 -207 C ATOM 1738 CG LYS A1027 -11.615 84.472 133.365 1.00189.06 C ANISOU 1738 CG LYS A1027 22457 21990 27386 3386 -550 -227 C ATOM 1739 CD LYS A1027 -12.393 85.160 132.260 1.00188.91 C ANISOU 1739 CD LYS A1027 22483 21973 27320 3446 -568 -246 C ATOM 1740 CE LYS A1027 -12.195 84.461 130.926 1.00188.69 C ANISOU 1740 CE LYS A1027 22465 21948 27279 3479 -583 -267 C ATOM 1741 NZ LYS A1027 -13.031 85.069 129.857 1.00189.23 N ANISOU 1741 NZ LYS A1027 22574 22019 27304 3539 -604 -288 N ATOM 1742 N ASP A1028 -9.142 85.447 136.211 1.00189.24 N ANISOU 1742 N ASP A1028 22471 21990 27442 3249 -453 -139 N ATOM 1743 CA ASP A1028 -7.679 85.568 136.300 1.00188.76 C ANISOU 1743 CA ASP A1028 22427 21917 27375 3216 -413 -112 C ATOM 1744 C ASP A1028 -7.056 84.581 137.300 1.00189.70 C ANISOU 1744 C ASP A1028 22491 22038 27546 3162 -407 -102 C ATOM 1745 O ASP A1028 -5.931 84.124 137.093 1.00189.89 O ANISOU 1745 O ASP A1028 22516 22058 27575 3142 -387 -92 O ATOM 1746 CB ASP A1028 -7.281 87.007 136.675 1.00187.39 C ANISOU 1746 CB ASP A1028 22300 21732 27167 3208 -378 -83 C ATOM 1747 CG ASP A1028 -5.797 87.283 136.481 1.00186.64 C ANISOU 1747 CG ASP A1028 22235 21625 27054 3184 -338 -59 C ATOM 1748 OD1 ASP A1028 -5.240 86.854 135.451 1.00186.22 O ANISOU 1748 OD1 ASP A1028 22197 21569 26986 3202 -337 -67 O ATOM 1749 OD2 ASP A1028 -5.190 87.943 137.353 1.00186.07 O ANISOU 1749 OD2 ASP A1028 22170 21545 26983 3149 -306 -31 O ATOM 1750 N ALA A1029 -7.779 84.271 138.378 1.00190.33 N ANISOU 1750 N ALA A1029 22527 22126 27664 3141 -422 -105 N ATOM 1751 CA ALA A1029 -7.363 83.226 139.322 1.00190.73 C ANISOU 1751 CA ALA A1029 22521 22180 27767 3094 -421 -100 C ATOM 1752 C ALA A1029 -7.558 81.828 138.723 1.00192.13 C ANISOU 1752 C ALA A1029 22661 22367 27972 3105 -451 -127 C ATOM 1753 O ALA A1029 -6.625 81.013 138.714 1.00191.96 O ANISOU 1753 O ALA A1029 22620 22343 27970 3079 -441 -122 O ATOM 1754 CB ALA A1029 -8.130 83.353 140.632 1.00190.05 C ANISOU 1754 CB ALA A1029 22399 22098 27711 3070 -429 -95 C ATOM 1755 N LEU A1030 -8.767 81.570 138.218 1.00193.24 N ANISOU 1755 N LEU A1030 22792 22517 28112 3143 -488 -156 N ATOM 1756 CA LEU A1030 -9.133 80.266 137.637 1.00193.22 C ANISOU 1756 CA LEU A1030 22754 22524 28137 3158 -520 -185 C ATOM 1757 C LEU A1030 -8.244 79.840 136.464 1.00192.64 C ANISOU 1757 C LEU A1030 22703 22447 28043 3173 -514 -190 C ATOM 1758 O LEU A1030 -7.839 78.675 136.393 1.00192.43 O ANISOU 1758 O LEU A1030 22641 22424 28048 3157 -522 -198 O ATOM 1759 CB LEU A1030 -10.603 80.258 137.186 1.00193.75 C ANISOU 1759 CB LEU A1030 22815 22601 28198 3202 -560 -216 C ATOM 1760 CG LEU A1030 -11.672 80.214 138.284 1.00193.91 C ANISOU 1760 CG LEU A1030 22796 22628 28251 3189 -578 -222 C ATOM 1761 CD1 LEU A1030 -13.036 80.570 137.712 1.00193.99 C ANISOU 1761 CD1 LEU A1030 22817 22646 28243 3238 -610 -248 C ATOM 1762 CD2 LEU A1030 -11.721 78.852 138.957 1.00194.05 C ANISOU 1762 CD2 LEU A1030 22749 22653 28327 3157 -593 -231 C ATOM 1763 N THR A1031 -7.949 80.774 135.556 1.00191.11 N ANISOU 1763 N THR A1031 22567 22246 27798 3204 -499 -184 N ATOM 1764 CA THR A1031 -7.071 80.483 134.408 1.00189.48 C ANISOU 1764 CA THR A1031 22389 22036 27569 3220 -490 -187 C ATOM 1765 C THR A1031 -5.639 80.113 134.840 1.00187.47 C ANISOU 1765 C THR A1031 22125 21774 27330 3173 -458 -163 C ATOM 1766 O THR A1031 -5.041 79.176 134.293 1.00187.66 O ANISOU 1766 O THR A1031 22135 21799 27367 3170 -461 -171 O ATOM 1767 CB THR A1031 -7.026 81.658 133.405 1.00189.45 C ANISOU 1767 CB THR A1031 22452 22024 27505 3261 -478 -184 C ATOM 1768 OG1 THR A1031 -6.740 82.878 134.098 1.00189.79 O ANISOU 1768 OG1 THR A1031 22525 22058 27527 3244 -447 -155 O ATOM 1769 CG2 THR A1031 -8.357 81.794 132.673 1.00189.34 C ANISOU 1769 CG2 THR A1031 22447 22019 27473 3315 -515 -213 C ATOM 1770 N LYS A1032 -5.111 80.842 135.827 1.00184.82 N ANISOU 1770 N LYS A1032 21796 21430 26995 3137 -427 -134 N ATOM 1771 CA LYS A1032 -3.798 80.538 136.418 1.00182.50 C ANISOU 1771 CA LYS A1032 21489 21129 26720 3089 -395 -109 C ATOM 1772 C LYS A1032 -3.801 79.220 137.202 1.00183.19 C ANISOU 1772 C LYS A1032 21512 21225 26865 3054 -410 -116 C ATOM 1773 O LYS A1032 -2.826 78.460 137.139 1.00183.05 O ANISOU 1773 O LYS A1032 21479 21206 26865 3030 -399 -111 O ATOM 1774 CB LYS A1032 -3.325 81.686 137.319 1.00180.13 C ANISOU 1774 CB LYS A1032 21212 20819 26406 3060 -360 -78 C ATOM 1775 CG LYS A1032 -2.952 82.950 136.564 1.00178.75 C ANISOU 1775 CG LYS A1032 21105 20634 26175 3086 -336 -66 C ATOM 1776 CD LYS A1032 -2.690 84.106 137.517 1.00177.01 C ANISOU 1776 CD LYS A1032 20905 20406 25944 3060 -305 -37 C ATOM 1777 CE LYS A1032 -2.422 85.398 136.764 1.00176.14 C ANISOU 1777 CE LYS A1032 20862 20285 25777 3088 -282 -26 C ATOM 1778 NZ LYS A1032 -2.482 86.580 137.664 1.00175.66 N ANISOU 1778 NZ LYS A1032 20820 20218 25705 3071 -259 -3 N ATOM 1779 N MET A1033 -4.886 78.958 137.939 1.00183.97 N ANISOU 1779 N MET A1033 21573 21332 26993 3051 -435 -128 N ATOM 1780 CA MET A1033 -5.092 77.648 138.589 1.00183.92 C ANISOU 1780 CA MET A1033 21503 21334 27042 3024 -455 -139 C ATOM 1781 C MET A1033 -5.120 76.505 137.569 1.00184.61 C ANISOU 1781 C MET A1033 21574 21428 27138 3047 -480 -165 C ATOM 1782 O MET A1033 -4.516 75.448 137.792 1.00184.84 O ANISOU 1782 O MET A1033 21569 21460 27202 3020 -480 -166 O ATOM 1783 CB MET A1033 -6.387 77.630 139.413 1.00183.12 C ANISOU 1783 CB MET A1033 21369 21241 26966 3025 -480 -150 C ATOM 1784 CG MET A1033 -6.279 78.335 140.755 1.00182.23 C ANISOU 1784 CG MET A1033 21249 21123 26864 2987 -458 -124 C ATOM 1785 SD MET A1033 -7.738 78.110 141.791 1.00180.95 S ANISOU 1785 SD MET A1033 21041 20972 26740 2983 -488 -138 S ATOM 1786 CE MET A1033 -7.190 78.865 143.321 1.00179.59 C ANISOU 1786 CE MET A1033 20864 20791 26578 2931 -453 -101 C ATOM 1787 N ARG A1034 -5.822 76.732 136.456 1.00185.63 N ANISOU 1787 N ARG A1034 21731 21560 27237 3098 -501 -188 N ATOM 1788 CA ARG A1034 -5.888 75.763 135.357 1.00186.39 C ANISOU 1788 CA ARG A1034 21820 21664 27337 3125 -525 -214 C ATOM 1789 C ARG A1034 -4.499 75.543 134.755 1.00187.65 C ANISOU 1789 C ARG A1034 22000 21815 27482 3114 -500 -201 C ATOM 1790 O ARG A1034 -4.008 74.407 134.712 1.00187.80 O ANISOU 1790 O ARG A1034 21984 21837 27531 3096 -505 -207 O ATOM 1791 CB ARG A1034 -6.872 76.224 134.280 1.00186.00 C ANISOU 1791 CB ARG A1034 21801 21617 27251 3183 -550 -238 C ATOM 1792 CG ARG A1034 -7.374 75.096 133.391 1.00185.39 C ANISOU 1792 CG ARG A1034 21700 21551 27189 3212 -586 -271 C ATOM 1793 CD ARG A1034 -8.416 75.579 132.394 1.00185.49 C ANISOU 1793 CD ARG A1034 21742 21568 27166 3269 -612 -296 C ATOM 1794 NE ARG A1034 -9.413 74.549 132.081 1.00185.91 N ANISOU 1794 NE ARG A1034 21754 21633 27247 3291 -653 -330 N ATOM 1795 CZ ARG A1034 -10.416 74.183 132.882 1.00185.71 C ANISOU 1795 CZ ARG A1034 21686 21616 27258 3282 -677 -343 C ATOM 1796 NH1 ARG A1034 -10.595 74.745 134.080 1.00185.41 N ANISOU 1796 NH1 ARG A1034 21637 21575 27232 3252 -663 -324 N ATOM 1797 NH2 ARG A1034 -11.259 73.233 132.486 1.00185.71 N ANISOU 1797 NH2 ARG A1034 21652 21627 27282 3303 -714 -375 N ATOM 1798 N ALA A1035 -3.856 76.638 134.344 1.00189.00 N ANISOU 1798 N ALA A1035 22225 21976 27608 3123 -471 -182 N ATOM 1799 CA ALA A1035 -2.478 76.600 133.817 1.00189.48 C ANISOU 1799 CA ALA A1035 22311 22028 27652 3111 -441 -167 C ATOM 1800 C ALA A1035 -1.504 75.892 134.767 1.00190.09 C ANISOU 1800 C ALA A1035 22351 22104 27770 3056 -422 -149 C ATOM 1801 O ALA A1035 -0.651 75.117 134.323 1.00189.30 O ANISOU 1801 O ALA A1035 22242 22002 27678 3046 -416 -150 O ATOM 1802 CB ALA A1035 -1.985 78.009 133.515 1.00189.33 C ANISOU 1802 CB ALA A1035 22355 21998 27582 3122 -409 -145 C ATOM 1803 N ALA A1036 -1.648 76.157 136.067 1.00190.95 N ANISOU 1803 N ALA A1036 22436 22212 27902 3021 -413 -132 N ATOM 1804 CA ALA A1036 -0.892 75.445 137.104 1.00190.89 C ANISOU 1804 CA ALA A1036 22386 22204 27937 2968 -399 -117 C ATOM 1805 C ALA A1036 -1.253 73.956 137.165 1.00191.28 C ANISOU 1805 C ALA A1036 22380 22264 28033 2962 -429 -139 C ATOM 1806 O ALA A1036 -0.371 73.118 137.389 1.00190.75 O ANISOU 1806 O ALA A1036 22288 22197 27992 2932 -419 -133 O ATOM 1807 CB ALA A1036 -1.109 76.094 138.463 1.00190.30 C ANISOU 1807 CB ALA A1036 22300 22127 27876 2936 -385 -97 C ATOM 1808 N ALA A1037 -2.536 73.630 136.971 1.00192.14 N ANISOU 1808 N ALA A1037 22469 22382 28152 2991 -465 -166 N ATOM 1809 CA ALA A1037 -2.982 72.226 136.946 1.00192.67 C ANISOU 1809 CA ALA A1037 22484 22458 28261 2989 -496 -190 C ATOM 1810 C ALA A1037 -2.424 71.456 135.740 1.00193.55 C ANISOU 1810 C ALA A1037 22603 22571 28365 3009 -503 -205 C ATOM 1811 O ALA A1037 -2.003 70.303 135.876 1.00193.19 O ANISOU 1811 O ALA A1037 22520 22529 28354 2987 -509 -210 O ATOM 1812 CB ALA A1037 -4.504 72.140 136.977 1.00192.67 C ANISOU 1812 CB ALA A1037 22465 22468 28271 3017 -533 -215 C ATOM 1813 N LEU A1038 -2.428 72.099 134.570 1.00194.63 N ANISOU 1813 N LEU A1038 22789 22705 28454 3050 -502 -211 N ATOM 1814 CA LEU A1038 -1.846 71.519 133.349 1.00194.55 C ANISOU 1814 CA LEU A1038 22794 22695 28430 3072 -506 -224 C ATOM 1815 C LEU A1038 -0.327 71.328 133.458 1.00193.65 C ANISOU 1815 C LEU A1038 22686 22572 28317 3036 -472 -200 C ATOM 1816 O LEU A1038 0.210 70.348 132.936 1.00193.22 O ANISOU 1816 O LEU A1038 22616 22521 28278 3034 -478 -210 O ATOM 1817 CB LEU A1038 -2.169 72.383 132.122 1.00194.92 C ANISOU 1817 CB LEU A1038 22897 22740 28424 3123 -510 -233 C ATOM 1818 CG LEU A1038 -3.642 72.492 131.716 1.00194.75 C ANISOU 1818 CG LEU A1038 22874 22727 28395 3167 -547 -261 C ATOM 1819 CD1 LEU A1038 -3.822 73.571 130.658 1.00194.71 C ANISOU 1819 CD1 LEU A1038 22931 22717 28333 3213 -542 -263 C ATOM 1820 CD2 LEU A1038 -4.175 71.157 131.217 1.00194.36 C ANISOU 1820 CD2 LEU A1038 22784 22688 28376 3182 -583 -293 C ATOM 1821 N ASP A1039 0.351 72.267 134.122 1.00192.21 N ANISOU 1821 N ASP A1039 22527 22381 28121 3010 -437 -171 N ATOM 1822 CA ASP A1039 1.781 72.127 134.437 1.00190.69 C ANISOU 1822 CA ASP A1039 22336 22181 27935 2971 -403 -147 C ATOM 1823 C ASP A1039 2.015 71.004 135.451 1.00190.99 C ANISOU 1823 C ASP A1039 22313 22224 28027 2927 -408 -144 C ATOM 1824 O ASP A1039 2.934 70.195 135.285 1.00191.23 O ANISOU 1824 O ASP A1039 22330 22254 28074 2908 -400 -142 O ATOM 1825 CB ASP A1039 2.350 73.444 134.986 1.00188.79 C ANISOU 1825 CB ASP A1039 22133 21931 27667 2953 -366 -116 C ATOM 1826 CG ASP A1039 3.863 73.416 135.133 1.00187.28 C ANISOU 1826 CG ASP A1039 21951 21730 27474 2918 -329 -93 C ATOM 1827 OD1 ASP A1039 4.563 73.223 134.117 1.00186.41 O ANISOU 1827 OD1 ASP A1039 21865 21617 27343 2933 -322 -96 O ATOM 1828 OD2 ASP A1039 4.353 73.599 136.257 1.00185.61 O ANISOU 1828 OD2 ASP A1039 21723 21516 27283 2876 -308 -71 O ATOM 1829 N ALA A1040 1.183 70.968 136.492 1.00191.04 N ANISOU 1829 N ALA A1040 22286 22235 28062 2912 -421 -145 N ATOM 1830 CA ALA A1040 1.266 69.931 137.527 1.00190.44 C ANISOU 1830 CA ALA A1040 22152 22163 28040 2872 -427 -144 C ATOM 1831 C ALA A1040 0.978 68.518 136.987 1.00190.59 C ANISOU 1831 C ALA A1040 22134 22191 28089 2883 -458 -171 C ATOM 1832 O ALA A1040 0.032 68.274 136.224 1.00190.99 O ANISOU 1832 O ALA A1040 22185 22249 28134 2922 -489 -198 O ATOM 1833 CB ALA A1040 0.334 70.262 138.690 1.00189.50 C ANISOU 1833 CB ALA A1040 22009 22047 27942 2857 -436 -140 C ATOM 1834 N PRO A1056 -1.293 52.525 142.038 1.00155.38 N ANISOU 1834 N PRO A1056 17028 17793 24216 2658 -675 -328 N ATOM 1835 CA PRO A1056 -1.744 52.640 143.425 1.00155.93 C ANISOU 1835 CA PRO A1056 17069 17862 24314 2627 -670 -316 C ATOM 1836 C PRO A1056 -1.830 54.090 143.901 1.00157.26 C ANISOU 1836 C PRO A1056 17272 18026 24451 2626 -651 -294 C ATOM 1837 O PRO A1056 -2.886 54.515 144.374 1.00156.13 O ANISOU 1837 O PRO A1056 17121 17886 24313 2634 -663 -301 O ATOM 1838 CB PRO A1056 -0.694 51.847 144.217 1.00154.85 C ANISOU 1838 CB PRO A1056 16904 17721 24210 2582 -651 -297 C ATOM 1839 CG PRO A1056 0.501 51.737 143.331 1.00154.66 C ANISOU 1839 CG PRO A1056 16906 17694 24161 2586 -636 -291 C ATOM 1840 CD PRO A1056 0.109 52.090 141.925 1.00154.73 C ANISOU 1840 CD PRO A1056 16949 17706 24134 2634 -652 -312 C ATOM 1841 N GLU A1057 -0.730 54.830 143.772 1.00159.87 N ANISOU 1841 N GLU A1057 17639 18351 24750 2617 -621 -270 N ATOM 1842 CA GLU A1057 -0.687 56.256 144.111 1.00162.37 C ANISOU 1842 CA GLU A1057 17994 18663 25033 2617 -600 -249 C ATOM 1843 C GLU A1057 -1.149 57.115 142.933 1.00166.04 C ANISOU 1843 C GLU A1057 18505 19130 25452 2664 -610 -262 C ATOM 1844 O GLU A1057 -1.938 58.062 143.110 1.00167.41 O ANISOU 1844 O GLU A1057 18696 19304 25607 2680 -613 -261 O ATOM 1845 CB GLU A1057 0.728 56.672 144.516 1.00162.09 C ANISOU 1845 CB GLU A1057 17978 18620 24986 2585 -563 -216 C ATOM 1846 CG GLU A1057 1.266 55.944 145.738 1.00162.04 C ANISOU 1846 CG GLU A1057 17931 18613 25023 2537 -551 -201 C ATOM 1847 CD GLU A1057 2.572 56.533 146.245 1.00162.09 C ANISOU 1847 CD GLU A1057 17958 18612 25014 2506 -513 -168 C ATOM 1848 OE1 GLU A1057 2.626 57.755 146.499 1.00160.98 O ANISOU 1848 OE1 GLU A1057 17850 18467 24844 2506 -495 -150 O ATOM 1849 OE2 GLU A1057 3.548 55.770 146.402 1.00162.95 O ANISOU 1849 OE2 GLU A1057 18051 18720 25143 2480 -502 -160 O ATOM 1850 N MET A1058 -0.654 56.776 141.737 1.00168.61 N ANISOU 1850 N MET A1058 18848 19455 25758 2687 -613 -273 N ATOM 1851 CA MET A1058 -1.029 57.470 140.489 1.00169.59 C ANISOU 1851 CA MET A1058 19016 19581 25837 2734 -623 -287 C ATOM 1852 C MET A1058 -2.545 57.609 140.302 1.00170.37 C ANISOU 1852 C MET A1058 19107 19686 25937 2767 -655 -313 C ATOM 1853 O MET A1058 -3.006 58.621 139.783 1.00170.78 O ANISOU 1853 O MET A1058 19197 19738 25951 2798 -657 -316 O ATOM 1854 CB MET A1058 -0.407 56.787 139.256 1.00169.60 C ANISOU 1854 CB MET A1058 19028 19583 25828 2754 -629 -301 C ATOM 1855 CG MET A1058 -0.904 55.371 138.971 1.00169.70 C ANISOU 1855 CG MET A1058 18996 19603 25878 2760 -659 -329 C ATOM 1856 SD MET A1058 -0.022 54.556 137.626 1.00170.22 S ANISOU 1856 SD MET A1058 19072 19669 25932 2777 -662 -342 S ATOM 1857 CE MET A1058 -0.643 55.442 136.198 1.00169.78 C ANISOU 1857 CE MET A1058 19068 19615 25823 2836 -676 -360 C ATOM 1858 N LYS A1059 -3.307 56.602 140.740 1.00170.09 N ANISOU 1858 N LYS A1059 19022 19656 25945 2760 -680 -332 N ATOM 1859 CA LYS A1059 -4.777 56.659 140.725 1.00169.26 C ANISOU 1859 CA LYS A1059 18903 19558 25849 2786 -710 -356 C ATOM 1860 C LYS A1059 -5.318 57.695 141.709 1.00169.12 C ANISOU 1860 C LYS A1059 18892 19538 25825 2775 -700 -340 C ATOM 1861 O LYS A1059 -6.259 58.408 141.385 1.00168.32 O ANISOU 1861 O LYS A1059 18810 19441 25703 2807 -715 -352 O ATOM 1862 CB LYS A1059 -5.383 55.292 141.058 1.00168.04 C ANISOU 1862 CB LYS A1059 18692 19410 25746 2776 -735 -378 C ATOM 1863 CG LYS A1059 -5.091 54.201 140.035 1.00167.15 C ANISOU 1863 CG LYS A1059 18568 19300 25640 2792 -751 -400 C ATOM 1864 CD LYS A1059 -5.409 52.821 140.584 1.00166.09 C ANISOU 1864 CD LYS A1059 18375 19169 25561 2770 -769 -415 C ATOM 1865 CE LYS A1059 -5.044 51.740 139.582 1.00165.88 C ANISOU 1865 CE LYS A1059 18339 19146 25543 2784 -783 -435 C ATOM 1866 NZ LYS A1059 -5.326 50.375 140.105 1.00166.10 N ANISOU 1866 NZ LYS A1059 18309 19175 25623 2763 -799 -449 N ATOM 1867 N ASP A1060 -4.715 57.763 142.898 1.00168.79 N ANISOU 1867 N ASP A1060 18836 19492 25804 2731 -676 -313 N ATOM 1868 CA ASP A1060 -5.094 58.751 143.914 1.00168.11 C ANISOU 1868 CA ASP A1060 18756 19403 25713 2716 -664 -295 C ATOM 1869 C ASP A1060 -4.704 60.176 143.517 1.00169.25 C ANISOU 1869 C ASP A1060 18958 19542 25804 2732 -642 -277 C ATOM 1870 O ASP A1060 -5.449 61.117 143.811 1.00169.57 O ANISOU 1870 O ASP A1060 19014 19583 25829 2744 -644 -275 O ATOM 1871 CB ASP A1060 -4.496 58.396 145.282 1.00166.50 C ANISOU 1871 CB ASP A1060 18520 19195 25544 2664 -643 -271 C ATOM 1872 CG ASP A1060 -5.073 57.113 145.861 1.00164.87 C ANISOU 1872 CG ASP A1060 18256 18993 25391 2648 -665 -287 C ATOM 1873 OD1 ASP A1060 -5.618 56.290 145.094 1.00164.07 O ANISOU 1873 OD1 ASP A1060 18138 18897 25301 2673 -692 -316 O ATOM 1874 OD2 ASP A1060 -4.973 56.924 147.091 1.00163.23 O ANISOU 1874 OD2 ASP A1060 18020 18784 25215 2611 -654 -271 O ATOM 1875 N PHE A1061 -3.554 60.338 142.855 1.00170.41 N ANISOU 1875 N PHE A1061 19136 19684 25925 2732 -621 -265 N ATOM 1876 CA PHE A1061 -3.172 61.648 142.296 1.00171.64 C ANISOU 1876 CA PHE A1061 19350 19836 26029 2752 -602 -250 C ATOM 1877 C PHE A1061 -4.101 62.026 141.145 1.00171.84 C ANISOU 1877 C PHE A1061 19402 19865 26023 2804 -626 -276 C ATOM 1878 O PHE A1061 -4.701 63.112 141.147 1.00171.25 O ANISOU 1878 O PHE A1061 19356 19790 25921 2824 -626 -273 O ATOM 1879 CB PHE A1061 -1.718 61.661 141.807 1.00172.13 C ANISOU 1879 CB PHE A1061 19438 19891 26071 2740 -574 -233 C ATOM 1880 CG PHE A1061 -0.701 61.437 142.895 1.00172.67 C ANISOU 1880 CG PHE A1061 19486 19954 26163 2689 -547 -206 C ATOM 1881 CD1 PHE A1061 -0.718 62.204 144.061 1.00172.33 C ANISOU 1881 CD1 PHE A1061 19443 19907 26124 2662 -528 -182 C ATOM 1882 CD2 PHE A1061 0.293 60.471 142.749 1.00173.36 C ANISOU 1882 CD2 PHE A1061 19556 20040 26270 2669 -539 -203 C ATOM 1883 CE1 PHE A1061 0.222 62.000 145.060 1.00172.44 C ANISOU 1883 CE1 PHE A1061 19440 19917 26160 2616 -503 -158 C ATOM 1884 CE2 PHE A1061 1.237 60.265 143.745 1.00173.39 C ANISOU 1884 CE2 PHE A1061 19543 20041 26296 2623 -514 -178 C ATOM 1885 CZ PHE A1061 1.202 61.031 144.902 1.00173.16 C ANISOU 1885 CZ PHE A1061 19513 20008 26270 2597 -496 -156 C ATOM 1886 N ARG A1062 -4.218 61.114 140.177 1.00172.45 N ANISOU 1886 N ARG A1062 19468 19947 26106 2828 -649 -301 N ATOM 1887 CA ARG A1062 -5.161 61.248 139.060 1.00173.17 C ANISOU 1887 CA ARG A1062 19577 20045 26175 2879 -677 -330 C ATOM 1888 C ARG A1062 -6.532 61.678 139.559 1.00175.88 C ANISOU 1888 C ARG A1062 19909 20393 26525 2892 -697 -342 C ATOM 1889 O ARG A1062 -7.101 62.644 139.047 1.00176.85 O ANISOU 1889 O ARG A1062 20067 20515 26610 2926 -702 -347 O ATOM 1890 CB ARG A1062 -5.288 59.925 138.290 1.00171.55 C ANISOU 1890 CB ARG A1062 19343 19845 25991 2893 -703 -358 C ATOM 1891 CG ARG A1062 -6.140 59.980 137.027 1.00170.15 C ANISOU 1891 CG ARG A1062 19184 19674 25789 2946 -732 -389 C ATOM 1892 CD ARG A1062 -6.531 58.586 136.559 1.00168.89 C ANISOU 1892 CD ARG A1062 18984 19521 25663 2956 -762 -419 C ATOM 1893 NE ARG A1062 -5.383 57.683 136.441 1.00167.62 N ANISOU 1893 NE ARG A1062 18810 19358 25520 2931 -749 -412 N ATOM 1894 CZ ARG A1062 -4.497 57.676 135.441 1.00167.39 C ANISOU 1894 CZ ARG A1062 18812 19326 25463 2945 -739 -410 C ATOM 1895 NH1 ARG A1062 -4.587 58.535 134.424 1.00167.60 N ANISOU 1895 NH1 ARG A1062 18886 19352 25440 2985 -739 -414 N ATOM 1896 NH2 ARG A1062 -3.497 56.798 135.459 1.00167.13 N ANISOU 1896 NH2 ARG A1062 18761 19291 25450 2919 -727 -402 N ATOM 1897 N HIS A1063 -7.054 60.962 140.555 1.00178.84 N ANISOU 1897 N HIS A1063 20232 20770 26945 2866 -708 -347 N ATOM 1898 CA HIS A1063 -8.413 61.204 141.047 1.00181.61 C ANISOU 1898 CA HIS A1063 20566 21127 27309 2878 -730 -361 C ATOM 1899 C HIS A1063 -8.533 62.415 141.985 1.00182.88 C ANISOU 1899 C HIS A1063 20746 21284 27456 2862 -710 -336 C ATOM 1900 O HIS A1063 -9.589 63.056 142.033 1.00184.51 O ANISOU 1900 O HIS A1063 20959 21492 27651 2885 -724 -347 O ATOM 1901 CB HIS A1063 -8.992 59.956 141.707 1.00182.03 C ANISOU 1901 CB HIS A1063 20559 21186 27419 2858 -751 -378 C ATOM 1902 CG HIS A1063 -10.478 59.997 141.833 1.00182.60 C ANISOU 1902 CG HIS A1063 20611 21264 27502 2881 -781 -402 C ATOM 1903 ND1 HIS A1063 -11.322 59.763 140.768 1.00182.83 N ANISOU 1903 ND1 HIS A1063 20645 21301 27521 2925 -812 -435 N ATOM 1904 CD2 HIS A1063 -11.271 60.291 142.888 1.00182.41 C ANISOU 1904 CD2 HIS A1063 20566 21241 27498 2866 -785 -399 C ATOM 1905 CE1 HIS A1063 -12.574 59.886 141.171 1.00182.49 C ANISOU 1905 CE1 HIS A1063 20582 21264 27492 2936 -833 -451 C ATOM 1906 NE2 HIS A1063 -12.570 60.208 142.452 1.00182.43 N ANISOU 1906 NE2 HIS A1063 20559 21252 27503 2901 -817 -430 N ATOM 1907 N GLY A1064 -7.470 62.724 142.727 1.00183.26 N ANISOU 1907 N GLY A1064 20801 21324 27505 2824 -677 -304 N ATOM 1908 CA GLY A1064 -7.372 64.004 143.434 1.00184.25 C ANISOU 1908 CA GLY A1064 20954 21444 27608 2812 -653 -278 C ATOM 1909 C GLY A1064 -7.460 65.171 142.467 1.00185.93 C ANISOU 1909 C GLY A1064 21224 21654 27764 2851 -649 -278 C ATOM 1910 O GLY A1064 -8.187 66.153 142.711 1.00185.77 O ANISOU 1910 O GLY A1064 21223 21634 27725 2865 -650 -276 O ATOM 1911 N PHE A1065 -6.722 65.043 141.358 1.00188.24 N ANISOU 1911 N PHE A1065 21544 21945 28032 2870 -644 -282 N ATOM 1912 CA PHE A1065 -6.794 66.004 140.252 1.00190.05 C ANISOU 1912 CA PHE A1065 21828 22172 28208 2912 -642 -286 C ATOM 1913 C PHE A1065 -8.160 66.004 139.539 1.00190.86 C ANISOU 1913 C PHE A1065 21931 22283 28303 2958 -679 -319 C ATOM 1914 O PHE A1065 -8.608 67.064 139.106 1.00191.04 O ANISOU 1914 O PHE A1065 21994 22305 28287 2989 -679 -319 O ATOM 1915 CB PHE A1065 -5.654 65.763 139.253 1.00190.64 C ANISOU 1915 CB PHE A1065 21929 22243 28261 2918 -628 -282 C ATOM 1916 CG PHE A1065 -4.348 66.413 139.644 1.00191.37 C ANISOU 1916 CG PHE A1065 22048 22325 28336 2888 -587 -248 C ATOM 1917 CD1 PHE A1065 -3.722 66.139 140.864 1.00191.60 C ANISOU 1917 CD1 PHE A1065 22048 22351 28397 2838 -567 -225 C ATOM 1918 CD2 PHE A1065 -3.735 67.311 138.772 1.00191.98 C ANISOU 1918 CD2 PHE A1065 22182 22397 28364 2909 -569 -238 C ATOM 1919 CE1 PHE A1065 -2.514 66.738 141.188 1.00191.85 C ANISOU 1919 CE1 PHE A1065 22106 22375 28413 2811 -530 -195 C ATOM 1920 CE2 PHE A1065 -2.531 67.919 139.102 1.00192.12 C ANISOU 1920 CE2 PHE A1065 22225 22406 28366 2882 -531 -207 C ATOM 1921 CZ PHE A1065 -1.921 67.635 140.311 1.00192.16 C ANISOU 1921 CZ PHE A1065 22200 22408 28403 2832 -512 -186 C ATOM 1922 N ASP A1066 -8.802 64.837 139.410 1.00190.84 N ANISOU 1922 N ASP A1066 21885 22289 28336 2964 -709 -346 N ATOM 1923 CA ASP A1066 -10.195 64.765 138.922 1.00190.39 C ANISOU 1923 CA ASP A1066 21820 22241 28278 3004 -745 -378 C ATOM 1924 C ASP A1066 -11.122 65.564 139.835 1.00190.94 C ANISOU 1924 C ASP A1066 21886 22312 28351 3000 -747 -373 C ATOM 1925 O ASP A1066 -11.846 66.450 139.364 1.00190.24 O ANISOU 1925 O ASP A1066 21828 22224 28228 3036 -757 -381 O ATOM 1926 CB ASP A1066 -10.725 63.315 138.844 1.00189.27 C ANISOU 1926 CB ASP A1066 21625 22107 28182 3004 -775 -407 C ATOM 1927 CG ASP A1066 -10.036 62.467 137.778 1.00188.45 C ANISOU 1927 CG ASP A1066 21523 22003 28074 3016 -780 -419 C ATOM 1928 OD1 ASP A1066 -9.385 63.023 136.866 1.00188.04 O ANISOU 1928 OD1 ASP A1066 21517 21948 27981 3037 -767 -412 O ATOM 1929 OD2 ASP A1066 -10.167 61.225 137.861 1.00187.72 O ANISOU 1929 OD2 ASP A1066 21386 21915 28022 3005 -797 -435 O ATOM 1930 N ILE A1067 -11.083 65.249 141.135 1.00192.27 N ANISOU 1930 N ILE A1067 22016 22478 28557 2957 -739 -359 N ATOM 1931 CA ILE A1067 -11.912 65.934 142.145 1.00193.23 C ANISOU 1931 CA ILE A1067 22130 22601 28688 2948 -739 -352 C ATOM 1932 C ILE A1067 -11.625 67.442 142.174 1.00195.44 C ANISOU 1932 C ILE A1067 22462 22874 28921 2955 -714 -328 C ATOM 1933 O ILE A1067 -12.563 68.239 142.282 1.00196.16 O ANISOU 1933 O ILE A1067 22567 22967 28996 2976 -724 -334 O ATOM 1934 CB ILE A1067 -11.742 65.319 143.566 1.00191.88 C ANISOU 1934 CB ILE A1067 21911 22429 28566 2897 -730 -337 C ATOM 1935 CG1 ILE A1067 -12.345 63.910 143.620 1.00191.18 C ANISOU 1935 CG1 ILE A1067 21768 22347 28525 2894 -759 -364 C ATOM 1936 CG2 ILE A1067 -12.407 66.186 144.635 1.00190.85 C ANISOU 1936 CG2 ILE A1067 21778 22296 28437 2885 -724 -324 C ATOM 1937 CD1 ILE A1067 -11.837 63.053 144.767 1.00190.47 C ANISOU 1937 CD1 ILE A1067 21632 22255 28482 2844 -747 -350 C ATOM 1938 N LEU A1068 -10.347 67.819 142.071 1.00198.03 N ANISOU 1938 N LEU A1068 22821 23194 29228 2938 -682 -302 N ATOM 1939 CA LEU A1068 -9.960 69.235 142.045 1.00200.47 C ANISOU 1939 CA LEU A1068 23181 23495 29491 2943 -656 -278 C ATOM 1940 C LEU A1068 -10.441 69.940 140.767 1.00203.97 C ANISOU 1940 C LEU A1068 23670 23940 29886 2997 -669 -295 C ATOM 1941 O LEU A1068 -11.253 70.881 140.837 1.00204.46 O ANISOU 1941 O LEU A1068 23754 24003 29927 3019 -674 -297 O ATOM 1942 CB LEU A1068 -8.441 69.376 142.213 1.00199.86 C ANISOU 1942 CB LEU A1068 23122 23408 29405 2911 -619 -248 C ATOM 1943 CG LEU A1068 -7.858 70.802 142.219 1.00199.52 C ANISOU 1943 CG LEU A1068 23134 23357 29318 2912 -587 -221 C ATOM 1944 CD1 LEU A1068 -6.877 71.018 143.362 1.00198.83 C ANISOU 1944 CD1 LEU A1068 23038 23262 29244 2861 -553 -188 C ATOM 1945 CD2 LEU A1068 -7.209 71.137 140.882 1.00199.91 C ANISOU 1945 CD2 LEU A1068 23231 23403 29323 2943 -579 -223 C ATOM 1946 N VAL A1069 -9.976 69.454 139.614 1.00207.41 N ANISOU 1946 N VAL A1069 24121 24376 30308 3020 -674 -308 N ATOM 1947 CA VAL A1069 -10.321 70.049 138.307 1.00209.24 C ANISOU 1947 CA VAL A1069 24397 24609 30493 3072 -686 -323 C ATOM 1948 C VAL A1069 -11.841 70.076 138.091 1.00211.33 C ANISOU 1948 C VAL A1069 24650 24883 30760 3108 -722 -353 C ATOM 1949 O VAL A1069 -12.363 71.028 137.507 1.00212.17 O ANISOU 1949 O VAL A1069 24796 24990 30827 3145 -727 -358 O ATOM 1950 CB VAL A1069 -9.599 69.334 137.125 1.00208.89 C ANISOU 1950 CB VAL A1069 24363 24564 30438 3088 -688 -335 C ATOM 1951 CG1 VAL A1069 -10.108 69.817 135.770 1.00208.71 C ANISOU 1951 CG1 VAL A1069 24382 24544 30371 3145 -705 -355 C ATOM 1952 CG2 VAL A1069 -8.089 69.543 137.206 1.00208.23 C ANISOU 1952 CG2 VAL A1069 24303 24472 30343 3058 -650 -304 C ATOM 1953 N GLY A1070 -12.538 69.044 138.569 1.00213.30 N ANISOU 1953 N GLY A1070 24846 25141 31057 3097 -747 -373 N ATOM 1954 CA GLY A1070 -14.006 69.036 138.603 1.00215.18 C ANISOU 1954 CA GLY A1070 25065 25387 31304 3124 -780 -399 C ATOM 1955 C GLY A1070 -14.597 70.192 139.392 1.00217.54 C ANISOU 1955 C GLY A1070 25379 25685 31590 3121 -772 -385 C ATOM 1956 O GLY A1070 -15.565 70.821 138.944 1.00218.42 O ANISOU 1956 O GLY A1070 25511 25801 31678 3159 -790 -402 O ATOM 1957 N GLN A1071 -14.013 70.480 140.558 1.00220.23 N ANISOU 1957 N GLN A1071 25711 26019 31946 3076 -744 -355 N ATOM 1958 CA GLN A1071 -14.449 71.617 141.386 1.00222.80 C ANISOU 1958 CA GLN A1071 26052 26341 32259 3069 -733 -338 C ATOM 1959 C GLN A1071 -14.061 72.969 140.775 1.00226.62 C ANISOU 1959 C GLN A1071 26601 26818 32685 3093 -712 -323 C ATOM 1960 O GLN A1071 -14.797 73.956 140.931 1.00227.63 O ANISOU 1960 O GLN A1071 26751 26947 32791 3111 -715 -322 O ATOM 1961 CB GLN A1071 -13.905 71.495 142.811 1.00221.22 C ANISOU 1961 CB GLN A1071 25823 26137 32092 3014 -709 -311 C ATOM 1962 CG GLN A1071 -14.575 70.393 143.620 1.00220.28 C ANISOU 1962 CG GLN A1071 25642 26025 32030 2992 -731 -326 C ATOM 1963 CD GLN A1071 -13.792 69.995 144.860 1.00219.59 C ANISOU 1963 CD GLN A1071 25524 25932 31977 2936 -707 -300 C ATOM 1964 OE1 GLN A1071 -12.812 70.640 145.225 1.00219.49 O ANISOU 1964 OE1 GLN A1071 25536 25910 31947 2913 -674 -270 O ATOM 1965 NE2 GLN A1071 -14.216 68.917 145.509 1.00219.31 N ANISOU 1965 NE2 GLN A1071 25433 25901 31991 2915 -723 -312 N ATOM 1966 N ILE A1072 -12.911 73.011 140.092 1.00229.82 N ANISOU 1966 N ILE A1072 27036 27218 33067 3092 -691 -310 N ATOM 1967 CA ILE A1072 -12.512 74.185 139.298 1.00231.29 C ANISOU 1967 CA ILE A1072 27285 27396 33196 3120 -673 -299 C ATOM 1968 C ILE A1072 -13.490 74.415 138.137 1.00233.35 C ANISOU 1968 C ILE A1072 27569 27663 33427 3178 -703 -328 C ATOM 1969 O ILE A1072 -13.818 75.562 137.837 1.00235.06 O ANISOU 1969 O ILE A1072 27829 27877 33604 3204 -697 -324 O ATOM 1970 CB ILE A1072 -11.046 74.081 138.792 1.00230.73 C ANISOU 1970 CB ILE A1072 27240 27318 33109 3106 -644 -280 C ATOM 1971 CG1 ILE A1072 -10.085 74.208 139.983 1.00229.87 C ANISOU 1971 CG1 ILE A1072 27119 27201 33020 3051 -611 -247 C ATOM 1972 CG2 ILE A1072 -10.735 75.158 137.749 1.00230.59 C ANISOU 1972 CG2 ILE A1072 27286 27293 33032 3142 -631 -275 C ATOM 1973 CD1 ILE A1072 -8.629 73.947 139.664 1.00229.23 C ANISOU 1973 CD1 ILE A1072 27051 27112 32931 3031 -583 -229 C ATOM 1974 N ASP A1073 -13.948 73.336 137.497 1.00233.32 N ANISOU 1974 N ASP A1073 27538 27669 33444 3197 -733 -359 N ATOM 1975 CA ASP A1073 -15.001 73.426 136.472 1.00231.81 C ANISOU 1975 CA ASP A1073 27359 27485 33230 3251 -766 -391 C ATOM 1976 C ASP A1073 -16.353 73.843 137.068 1.00229.80 C ANISOU 1976 C ASP A1073 27090 27238 32986 3263 -787 -403 C ATOM 1977 O ASP A1073 -17.061 74.665 136.473 1.00229.74 O ANISOU 1977 O ASP A1073 27115 27231 32941 3304 -798 -414 O ATOM 1978 CB ASP A1073 -15.150 72.100 135.703 1.00231.75 C ANISOU 1978 CB ASP A1073 27321 27485 33246 3267 -794 -421 C ATOM 1979 CG ASP A1073 -13.957 71.795 134.806 1.00231.59 C ANISOU 1979 CG ASP A1073 27325 27459 33207 3269 -778 -414 C ATOM 1980 OD1 ASP A1073 -13.464 72.711 134.119 1.00231.31 O ANISOU 1980 OD1 ASP A1073 27344 27418 33124 3290 -760 -402 O ATOM 1981 OD2 ASP A1073 -13.524 70.626 134.771 1.00230.68 O ANISOU 1981 OD2 ASP A1073 27175 27347 33124 3250 -783 -421 O ATOM 1982 N ASP A1074 -16.705 73.278 138.229 1.00226.45 N ANISOU 1982 N ASP A1074 26615 26816 32609 3227 -792 -402 N ATOM 1983 CA ASP A1074 -17.918 73.690 138.966 1.00223.46 C ANISOU 1983 CA ASP A1074 26219 26443 32242 3231 -808 -410 C ATOM 1984 C ASP A1074 -17.879 75.155 139.413 1.00222.62 C ANISOU 1984 C ASP A1074 26154 26329 32101 3230 -784 -385 C ATOM 1985 O ASP A1074 -18.925 75.808 139.464 1.00223.49 O ANISOU 1985 O ASP A1074 26272 26443 32198 3256 -800 -396 O ATOM 1986 CB ASP A1074 -18.168 72.791 140.189 1.00221.56 C ANISOU 1986 CB ASP A1074 25916 26205 32060 3189 -814 -410 C ATOM 1987 CG ASP A1074 -18.792 71.452 139.820 1.00220.32 C ANISOU 1987 CG ASP A1074 25712 26057 31939 3200 -848 -444 C ATOM 1988 OD1 ASP A1074 -18.584 70.972 138.686 1.00220.02 O ANISOU 1988 OD1 ASP A1074 25685 26022 31887 3227 -860 -462 O ATOM 1989 OD2 ASP A1074 -19.496 70.875 140.676 1.00218.58 O ANISOU 1989 OD2 ASP A1074 25444 25842 31761 3180 -863 -454 O ATOM 1990 N ALA A1075 -16.686 75.654 139.751 1.00220.92 N ANISOU 1990 N ALA A1075 25963 26103 31872 3201 -747 -351 N ATOM 1991 CA ALA A1075 -16.494 77.082 140.029 1.00219.79 C ANISOU 1991 CA ALA A1075 25866 25952 31690 3202 -721 -326 C ATOM 1992 C ALA A1075 -16.616 77.897 138.739 1.00220.00 C ANISOU 1992 C ALA A1075 25950 25978 31662 3253 -725 -334 C ATOM 1993 O ALA A1075 -17.454 78.805 138.648 1.00220.78 O ANISOU 1993 O ALA A1075 26073 26078 31734 3282 -733 -340 O ATOM 1994 CB ALA A1075 -15.143 77.325 140.686 1.00218.51 C ANISOU 1994 CB ALA A1075 25714 25779 31530 3156 -681 -289 C ATOM 1995 N LEU A1076 -15.798 77.539 137.745 1.00218.26 N ANISOU 1995 N LEU A1076 25749 25754 31423 3265 -719 -337 N ATOM 1996 CA LEU A1076 -15.783 78.186 136.418 1.00216.41 C ANISOU 1996 CA LEU A1076 25570 25518 31137 3314 -721 -345 C ATOM 1997 C LEU A1076 -17.186 78.325 135.825 1.00214.11 C ANISOU 1997 C LEU A1076 25281 25237 30834 3364 -758 -378 C ATOM 1998 O LEU A1076 -17.542 79.394 135.318 1.00214.38 O ANISOU 1998 O LEU A1076 25361 25268 30824 3398 -756 -377 O ATOM 1999 CB LEU A1076 -14.881 77.401 135.448 1.00216.35 C ANISOU 1999 CB LEU A1076 25568 25509 31125 3320 -718 -351 C ATOM 2000 CG LEU A1076 -14.546 78.017 134.085 1.00216.61 C ANISOU 2000 CG LEU A1076 25660 25538 31103 3363 -713 -354 C ATOM 2001 CD1 LEU A1076 -13.656 79.243 134.242 1.00216.59 C ANISOU 2001 CD1 LEU A1076 25708 25522 31063 3351 -672 -320 C ATOM 2002 CD2 LEU A1076 -13.871 76.986 133.193 1.00215.75 C ANISOU 2002 CD2 LEU A1076 25543 25430 31000 3369 -718 -366 C ATOM 2003 N LYS A1077 -17.979 77.254 135.928 1.00209.91 N ANISOU 2003 N LYS A1077 24697 24715 30341 3366 -791 -405 N ATOM 2004 CA LYS A1077 -19.405 77.250 135.542 1.00206.59 C ANISOU 2004 CA LYS A1077 24269 24306 29920 3408 -829 -439 C ATOM 2005 C LYS A1077 -20.182 78.488 136.022 1.00206.01 C ANISOU 2005 C LYS A1077 24218 24231 29823 3420 -827 -431 C ATOM 2006 O LYS A1077 -21.060 78.980 135.309 1.00206.25 O ANISOU 2006 O LYS A1077 24272 24267 29825 3467 -848 -452 O ATOM 2007 CB LYS A1077 -20.088 75.972 136.061 1.00204.37 C ANISOU 2007 CB LYS A1077 23920 24035 29695 3391 -857 -462 C ATOM 2008 CG LYS A1077 -21.540 75.792 135.636 1.00202.82 C ANISOU 2008 CG LYS A1077 23708 23850 29502 3433 -898 -499 C ATOM 2009 CD LYS A1077 -22.052 74.409 136.006 1.00200.76 C ANISOU 2009 CD LYS A1077 23382 23598 29297 3417 -924 -523 C ATOM 2010 CE LYS A1077 -23.550 74.288 135.778 1.00199.53 C ANISOU 2010 CE LYS A1077 23207 23454 29149 3453 -964 -559 C ATOM 2011 NZ LYS A1077 -23.929 74.465 134.348 1.00199.05 N ANISOU 2011 NZ LYS A1077 23181 23399 29050 3510 -985 -584 N ATOM 2012 N LEU A1078 -19.859 78.979 137.220 1.00205.21 N ANISOU 2012 N LEU A1078 24110 24123 29734 3379 -801 -403 N ATOM 2013 CA LEU A1078 -20.461 80.216 137.741 1.00204.95 C ANISOU 2013 CA LEU A1078 24103 24089 29680 3386 -795 -391 C ATOM 2014 C LEU A1078 -19.923 81.454 137.020 1.00205.38 C ANISOU 2014 C LEU A1078 24225 24133 29674 3411 -771 -374 C ATOM 2015 O LEU A1078 -20.699 82.332 136.634 1.00207.43 O ANISOU 2015 O LEU A1078 24516 24395 29900 3449 -782 -383 O ATOM 2016 CB LEU A1078 -20.218 80.354 139.248 1.00204.06 C ANISOU 2016 CB LEU A1078 23962 23971 29598 3333 -773 -365 C ATOM 2017 CG LEU A1078 -20.732 79.214 140.138 1.00203.49 C ANISOU 2017 CG LEU A1078 23823 23908 29587 3303 -793 -378 C ATOM 2018 CD1 LEU A1078 -20.056 79.251 141.497 1.00203.16 C ANISOU 2018 CD1 LEU A1078 23759 23859 29573 3246 -764 -346 C ATOM 2019 CD2 LEU A1078 -22.249 79.268 140.280 1.00203.04 C ANISOU 2019 CD2 LEU A1078 23744 23861 29540 3330 -827 -405 C ATOM 2020 N ALA A1079 -18.601 81.506 136.825 1.00204.14 N ANISOU 2020 N ALA A1079 24092 23967 29505 3391 -740 -350 N ATOM 2021 CA ALA A1079 -17.919 82.679 136.237 1.00202.44 C ANISOU 2021 CA ALA A1079 23941 23740 29234 3408 -712 -330 C ATOM 2022 C ALA A1079 -18.435 83.098 134.852 1.00201.22 C ANISOU 2022 C ALA A1079 23829 23589 29034 3469 -730 -352 C ATOM 2023 O ALA A1079 -18.338 84.273 134.488 1.00201.23 O ANISOU 2023 O ALA A1079 23884 23583 28989 3491 -714 -339 O ATOM 2024 CB ALA A1079 -16.414 82.447 136.184 1.00202.05 C ANISOU 2024 CB ALA A1079 23903 23681 29183 3376 -678 -305 C ATOM 2025 N ASN A1080 -18.966 82.139 134.092 1.00198.84 N ANISOU 2025 N ASN A1080 23506 23298 28747 3496 -764 -385 N ATOM 2026 CA ASN A1080 -19.636 82.426 132.818 1.00196.27 C ANISOU 2026 CA ASN A1080 23213 22977 28382 3556 -787 -410 C ATOM 2027 C ASN A1080 -20.925 83.229 133.023 1.00194.00 C ANISOU 2027 C ASN A1080 22934 22695 28080 3585 -807 -423 C ATOM 2028 O ASN A1080 -21.222 84.129 132.234 1.00194.03 O ANISOU 2028 O ASN A1080 22986 22696 28036 3628 -808 -427 O ATOM 2029 CB ASN A1080 -19.944 81.129 132.056 1.00195.91 C ANISOU 2029 CB ASN A1080 23134 22942 28360 3575 -820 -444 C ATOM 2030 CG ASN A1080 -18.690 80.403 131.601 1.00195.04 C ANISOU 2030 CG ASN A1080 23024 22826 28254 3556 -803 -435 C ATOM 2031 OD1 ASN A1080 -17.618 80.552 132.188 1.00194.02 O ANISOU 2031 OD1 ASN A1080 22900 22687 28130 3515 -769 -404 O ATOM 2032 ND2 ASN A1080 -18.824 79.602 130.551 1.00194.93 N ANISOU 2032 ND2 ASN A1080 23004 22819 28239 3587 -827 -462 N ATOM 2033 N GLU A1081 -21.682 82.901 134.073 1.00190.87 N ANISOU 2033 N GLU A1081 22490 22305 27725 3562 -821 -428 N ATOM 2034 CA GLU A1081 -22.883 83.667 134.437 1.00188.58 C ANISOU 2034 CA GLU A1081 22203 22020 27426 3583 -837 -437 C ATOM 2035 C GLU A1081 -22.503 84.993 135.099 1.00188.64 C ANISOU 2035 C GLU A1081 22249 22017 27407 3566 -803 -403 C ATOM 2036 O GLU A1081 -23.005 86.051 134.710 1.00190.10 O ANISOU 2036 O GLU A1081 22477 22201 27551 3601 -805 -404 O ATOM 2037 CB GLU A1081 -23.794 82.865 135.370 1.00185.28 C ANISOU 2037 CB GLU A1081 21722 21613 27063 3562 -863 -454 C ATOM 2038 CG GLU A1081 -24.370 81.599 134.750 1.00182.69 C ANISOU 2038 CG GLU A1081 21354 21297 26762 3582 -900 -492 C ATOM 2039 CD GLU A1081 -24.904 80.624 135.780 1.00180.23 C ANISOU 2039 CD GLU A1081 20975 20993 26511 3548 -916 -502 C ATOM 2040 OE1 GLU A1081 -25.416 81.071 136.829 1.00178.39 O ANISOU 2040 OE1 GLU A1081 20727 20760 26294 3527 -913 -492 O ATOM 2041 OE2 GLU A1081 -24.822 79.400 135.539 1.00178.60 O ANISOU 2041 OE2 GLU A1081 20729 20791 26336 3541 -932 -520 O ATOM 2042 N GLY A1082 -21.621 84.921 136.098 1.00186.87 N ANISOU 2042 N GLY A1082 22009 21785 27207 3513 -773 -374 N ATOM 2043 CA GLY A1082 -21.125 86.094 136.821 1.00184.96 C ANISOU 2043 CA GLY A1082 21799 21532 26944 3490 -738 -339 C ATOM 2044 C GLY A1082 -21.743 86.215 138.200 1.00183.79 C ANISOU 2044 C GLY A1082 21614 21387 26830 3458 -740 -332 C ATOM 2045 O GLY A1082 -22.500 87.153 138.465 1.00183.45 O ANISOU 2045 O GLY A1082 21589 21344 26768 3475 -744 -331 O ATOM 2046 N LYS A1083 -21.428 85.252 139.067 1.00182.24 N ANISOU 2046 N LYS A1083 21365 21193 26684 3413 -738 -327 N ATOM 2047 CA LYS A1083 -21.914 85.230 140.449 1.00180.74 C ANISOU 2047 CA LYS A1083 21135 21005 26532 3377 -738 -319 C ATOM 2048 C LYS A1083 -20.776 84.853 141.399 1.00179.30 C ANISOU 2048 C LYS A1083 20930 20815 26378 3319 -708 -290 C ATOM 2049 O LYS A1083 -20.330 83.703 141.418 1.00178.34 O ANISOU 2049 O LYS A1083 20772 20696 26291 3298 -712 -296 O ATOM 2050 CB LYS A1083 -23.087 84.256 140.592 1.00180.65 C ANISOU 2050 CB LYS A1083 21070 21007 26560 3387 -779 -353 C ATOM 2051 CG LYS A1083 -24.329 84.703 139.836 1.00180.56 C ANISOU 2051 CG LYS A1083 21076 21003 26522 3442 -810 -381 C ATOM 2052 CD LYS A1083 -25.496 83.751 140.026 1.00180.36 C ANISOU 2052 CD LYS A1083 20997 20992 26538 3450 -849 -415 C ATOM 2053 CE LYS A1083 -26.738 84.271 139.322 1.00180.40 C ANISOU 2053 CE LYS A1083 21021 21005 26516 3505 -879 -443 C ATOM 2054 NZ LYS A1083 -27.888 83.332 139.436 1.00180.63 N ANISOU 2054 NZ LYS A1083 20998 21048 26585 3515 -918 -478 N ATOM 2055 N VAL A1084 -20.314 85.835 142.174 1.00178.47 N ANISOU 2055 N VAL A1084 20847 20700 26260 3294 -676 -258 N ATOM 2056 CA VAL A1084 -19.162 85.672 143.067 1.00178.04 C ANISOU 2056 CA VAL A1084 20780 20638 26227 3239 -643 -228 C ATOM 2057 C VAL A1084 -19.550 84.890 144.324 1.00177.09 C ANISOU 2057 C VAL A1084 20597 20523 26163 3200 -653 -229 C ATOM 2058 O VAL A1084 -18.853 83.944 144.700 1.00178.17 O ANISOU 2058 O VAL A1084 20701 20660 26335 3165 -646 -223 O ATOM 2059 CB VAL A1084 -18.546 87.043 143.463 1.00178.16 C ANISOU 2059 CB VAL A1084 20842 20641 26207 3227 -606 -194 C ATOM 2060 CG1 VAL A1084 -17.382 86.868 144.440 1.00177.75 C ANISOU 2060 CG1 VAL A1084 20774 20581 26179 3170 -572 -163 C ATOM 2061 CG2 VAL A1084 -18.089 87.804 142.222 1.00178.10 C ANISOU 2061 CG2 VAL A1084 20898 20628 26144 3265 -594 -192 C ATOM 2062 N LYS A1085 -20.663 85.279 144.946 1.00175.28 N ANISOU 2062 N LYS A1085 20354 20300 25943 3206 -669 -236 N ATOM 2063 CA LYS A1085 -21.116 84.708 146.234 1.00173.62 C ANISOU 2063 CA LYS A1085 20089 20094 25784 3168 -676 -235 C ATOM 2064 C LYS A1085 -20.975 83.181 146.251 1.00173.34 C ANISOU 2064 C LYS A1085 20000 20065 25794 3151 -692 -252 C ATOM 2065 O LYS A1085 -20.277 82.617 147.101 1.00172.77 O ANISOU 2065 O LYS A1085 19898 19989 25756 3105 -676 -235 O ATOM 2066 CB LYS A1085 -22.583 85.068 146.535 1.00172.44 C ANISOU 2066 CB LYS A1085 19927 19953 25639 3192 -703 -255 C ATOM 2067 CG LYS A1085 -22.925 86.545 146.674 1.00171.33 C ANISOU 2067 CG LYS A1085 19831 19807 25457 3208 -691 -241 C ATOM 2068 CD LYS A1085 -22.154 87.245 147.782 1.00170.22 C ANISOU 2068 CD LYS A1085 19700 19658 25319 3164 -653 -203 C ATOM 2069 CE LYS A1085 -22.490 88.728 147.801 1.00169.91 C ANISOU 2069 CE LYS A1085 19708 19613 25235 3185 -642 -190 C ATOM 2070 NZ LYS A1085 -21.571 89.519 148.666 1.00169.59 N ANISOU 2070 NZ LYS A1085 19687 19562 25188 3146 -602 -153 N ATOM 2071 N GLU A1086 -21.609 82.532 145.276 1.00173.02 N ANISOU 2071 N GLU A1086 19952 20033 25755 3188 -724 -285 N ATOM 2072 CA GLU A1086 -21.591 81.071 145.153 1.00172.87 C ANISOU 2072 CA GLU A1086 19885 20020 25777 3177 -743 -304 C ATOM 2073 C GLU A1086 -20.172 80.516 144.946 1.00174.06 C ANISOU 2073 C GLU A1086 20038 20164 25932 3151 -719 -287 C ATOM 2074 O GLU A1086 -19.832 79.466 145.508 1.00174.57 O ANISOU 2074 O GLU A1086 20057 20230 26040 3116 -720 -286 O ATOM 2075 CB GLU A1086 -22.514 80.614 144.013 1.00171.71 C ANISOU 2075 CB GLU A1086 19736 19883 25622 3228 -781 -343 C ATOM 2076 CG GLU A1086 -23.998 80.897 144.239 1.00169.89 C ANISOU 2076 CG GLU A1086 19491 19661 25397 3252 -810 -366 C ATOM 2077 CD GLU A1086 -24.829 80.814 142.965 1.00168.10 C ANISOU 2077 CD GLU A1086 19279 19443 25146 3309 -843 -400 C ATOM 2078 OE1 GLU A1086 -24.433 81.415 141.944 1.00166.24 O ANISOU 2078 OE1 GLU A1086 19094 19204 24865 3341 -836 -398 O ATOM 2079 OE2 GLU A1086 -25.895 80.162 142.988 1.00166.59 O ANISOU 2079 OE2 GLU A1086 19050 19262 24983 3323 -876 -430 O ATOM 2080 N ALA A1087 -19.341 81.235 144.182 1.00175.21 N ANISOU 2080 N ALA A1087 20237 20302 26033 3165 -697 -272 N ATOM 2081 CA ALA A1087 -17.948 80.816 143.930 1.00175.47 C ANISOU 2081 CA ALA A1087 20277 20328 26065 3142 -672 -255 C ATOM 2082 C ALA A1087 -17.117 80.625 145.209 1.00176.07 C ANISOU 2082 C ALA A1087 20328 20398 26173 3083 -645 -226 C ATOM 2083 O ALA A1087 -16.156 79.845 145.206 1.00177.83 O ANISOU 2083 O ALA A1087 20534 20618 26414 3058 -633 -218 O ATOM 2084 CB ALA A1087 -17.245 81.784 142.982 1.00175.08 C ANISOU 2084 CB ALA A1087 20291 20269 25959 3167 -651 -242 C ATOM 2085 N GLN A1088 -17.486 81.324 146.288 1.00174.80 N ANISOU 2085 N GLN A1088 20162 20235 26018 3063 -635 -210 N ATOM 2086 CA GLN A1088 -16.859 81.111 147.602 1.00173.11 C ANISOU 2086 CA GLN A1088 19918 20017 25838 3009 -612 -185 C ATOM 2087 C GLN A1088 -17.160 79.721 148.190 1.00172.64 C ANISOU 2087 C GLN A1088 19794 19964 25835 2984 -632 -199 C ATOM 2088 O GLN A1088 -16.343 79.188 148.951 1.00172.46 O ANISOU 2088 O GLN A1088 19746 19938 25842 2940 -614 -181 O ATOM 2089 CB GLN A1088 -17.272 82.209 148.590 1.00171.65 C ANISOU 2089 CB GLN A1088 19744 19829 25646 2996 -599 -166 C ATOM 2090 CG GLN A1088 -16.767 83.600 148.218 1.00170.90 C ANISOU 2090 CG GLN A1088 19711 19725 25498 3010 -572 -145 C ATOM 2091 CD GLN A1088 -17.504 84.719 148.934 1.00170.78 C ANISOU 2091 CD GLN A1088 19709 19708 25469 3012 -568 -135 C ATOM 2092 OE1 GLN A1088 -18.072 84.525 150.009 1.00170.54 O ANISOU 2092 OE1 GLN A1088 19641 19681 25472 2988 -575 -134 O ATOM 2093 NE2 GLN A1088 -17.496 85.905 148.334 1.00171.00 N ANISOU 2093 NE2 GLN A1088 19793 19731 25448 3041 -557 -128 N ATOM 2094 N ALA A1089 -18.316 79.143 147.843 1.00171.99 N ANISOU 2094 N ALA A1089 19686 19892 25769 3011 -668 -232 N ATOM 2095 CA ALA A1089 -18.649 77.764 148.245 1.00170.59 C ANISOU 2095 CA ALA A1089 19448 19721 25644 2993 -689 -249 C ATOM 2096 C ALA A1089 -17.712 76.730 147.611 1.00169.69 C ANISOU 2096 C ALA A1089 19325 19607 25542 2985 -687 -253 C ATOM 2097 O ALA A1089 -17.349 75.742 148.260 1.00169.17 O ANISOU 2097 O ALA A1089 19215 19541 25518 2950 -685 -250 O ATOM 2098 CB ALA A1089 -20.099 77.433 147.913 1.00170.33 C ANISOU 2098 CB ALA A1089 19394 19700 25623 3028 -729 -285 C ATOM 2099 N ALA A1090 -17.330 76.960 146.353 1.00168.75 N ANISOU 2099 N ALA A1090 19245 19486 25384 3019 -687 -260 N ATOM 2100 CA ALA A1090 -16.346 76.114 145.663 1.00167.72 C ANISOU 2100 CA ALA A1090 19113 19353 25257 3014 -681 -261 C ATOM 2101 C ALA A1090 -14.937 76.279 146.246 1.00166.59 C ANISOU 2101 C ALA A1090 18980 19201 25115 2970 -642 -226 C ATOM 2102 O ALA A1090 -14.209 75.291 146.407 1.00166.71 O ANISOU 2102 O ALA A1090 18966 19216 25160 2943 -637 -223 O ATOM 2103 CB ALA A1090 -16.338 76.418 144.170 1.00167.61 C ANISOU 2103 CB ALA A1090 19142 19340 25199 3062 -690 -277 C ATOM 2104 N ALA A1091 -14.570 77.525 146.563 1.00165.15 N ANISOU 2104 N ALA A1091 18837 19011 24901 2965 -615 -201 N ATOM 2105 CA ALA A1091 -13.265 77.847 147.165 1.00163.87 C ANISOU 2105 CA ALA A1091 18687 18839 24736 2924 -576 -167 C ATOM 2106 C ALA A1091 -12.994 77.088 148.469 1.00163.37 C ANISOU 2106 C ALA A1091 18572 18776 24723 2873 -569 -154 C ATOM 2107 O ALA A1091 -11.881 76.597 148.679 1.00163.17 O ANISOU 2107 O ALA A1091 18538 18746 24712 2842 -549 -139 O ATOM 2108 CB ALA A1091 -13.145 79.348 147.398 1.00162.82 C ANISOU 2108 CB ALA A1091 18601 18699 24563 2928 -552 -144 C ATOM 2109 N GLU A1092 -14.010 76.996 149.331 1.00162.66 N ANISOU 2109 N GLU A1092 18449 18691 24661 2866 -586 -162 N ATOM 2110 CA GLU A1092 -13.916 76.210 150.573 1.00161.64 C ANISOU 2110 CA GLU A1092 18267 18563 24583 2821 -583 -154 C ATOM 2111 C GLU A1092 -13.699 74.713 150.317 1.00161.04 C ANISOU 2111 C GLU A1092 18150 18492 24544 2812 -599 -171 C ATOM 2112 O GLU A1092 -12.963 74.056 151.057 1.00159.77 O ANISOU 2112 O GLU A1092 17960 18329 24415 2771 -585 -156 O ATOM 2113 CB GLU A1092 -15.169 76.393 151.436 1.00161.54 C ANISOU 2113 CB GLU A1092 18228 18556 24591 2820 -601 -162 C ATOM 2114 CG GLU A1092 -15.315 77.779 152.042 1.00161.86 C ANISOU 2114 CG GLU A1092 18301 18592 24606 2816 -582 -140 C ATOM 2115 CD GLU A1092 -16.590 77.933 152.853 1.00162.53 C ANISOU 2115 CD GLU A1092 18359 18682 24712 2817 -601 -150 C ATOM 2116 OE1 GLU A1092 -16.906 77.027 153.655 1.00162.24 O ANISOU 2116 OE1 GLU A1092 18272 18650 24722 2791 -612 -156 O ATOM 2117 OE2 GLU A1092 -17.275 78.966 152.693 1.00163.38 O ANISOU 2117 OE2 GLU A1092 18496 18790 24789 2843 -605 -152 O ATOM 2118 N GLN A1093 -14.350 74.187 149.276 1.00161.09 N ANISOU 2118 N GLN A1093 18154 18505 24547 2850 -629 -202 N ATOM 2119 CA GLN A1093 -14.206 72.778 148.886 1.00160.79 C ANISOU 2119 CA GLN A1093 18079 18472 24541 2847 -646 -221 C ATOM 2120 C GLN A1093 -12.833 72.505 148.251 1.00160.80 C ANISOU 2120 C GLN A1093 18101 18468 24528 2838 -625 -209 C ATOM 2121 O GLN A1093 -12.214 71.459 148.516 1.00161.06 O ANISOU 2121 O GLN A1093 18100 18500 24594 2811 -622 -207 O ATOM 2122 CB GLN A1093 -15.328 72.365 147.921 1.00160.69 C ANISOU 2122 CB GLN A1093 18060 18468 24526 2893 -684 -259 C ATOM 2123 CG GLN A1093 -16.747 72.482 148.479 1.00160.01 C ANISOU 2123 CG GLN A1093 17949 18389 24458 2903 -709 -276 C ATOM 2124 CD GLN A1093 -17.175 71.292 149.324 1.00159.03 C ANISOU 2124 CD GLN A1093 17762 18269 24391 2875 -724 -286 C ATOM 2125 OE1 GLN A1093 -16.355 70.635 149.965 1.00158.14 O ANISOU 2125 OE1 GLN A1093 17625 18153 24307 2835 -708 -271 O ATOM 2126 NE2 GLN A1093 -18.474 71.014 149.333 1.00158.44 N ANISOU 2126 NE2 GLN A1093 17663 18203 24333 2896 -755 -314 N ATOM 2127 N LEU A1094 -12.365 73.440 147.417 1.00160.32 N ANISOU 2127 N LEU A1094 18094 18402 24418 2862 -611 -200 N ATOM 2128 CA LEU A1094 -11.023 73.353 146.812 1.00158.96 C ANISOU 2128 CA LEU A1094 17946 18223 24227 2855 -587 -186 C ATOM 2129 C LEU A1094 -9.899 73.286 147.859 1.00157.32 C ANISOU 2129 C LEU A1094 17726 18008 24038 2803 -554 -155 C ATOM 2130 O LEU A1094 -8.922 72.551 147.669 1.00157.60 O ANISOU 2130 O LEU A1094 17752 18041 24085 2784 -544 -149 O ATOM 2131 CB LEU A1094 -10.775 74.523 145.848 1.00159.25 C ANISOU 2131 CB LEU A1094 18046 18254 24206 2889 -574 -180 C ATOM 2132 CG LEU A1094 -11.561 74.492 144.527 1.00159.72 C ANISOU 2132 CG LEU A1094 18126 18320 24241 2943 -603 -211 C ATOM 2133 CD1 LEU A1094 -11.505 75.847 143.836 1.00159.77 C ANISOU 2133 CD1 LEU A1094 18194 18321 24190 2975 -590 -203 C ATOM 2134 CD2 LEU A1094 -11.059 73.393 143.587 1.00159.73 C ANISOU 2134 CD2 LEU A1094 18116 18324 24250 2953 -614 -228 C ATOM 2135 N LYS A1095 -10.041 74.047 148.948 1.00155.35 N ANISOU 2135 N LYS A1095 17477 17755 23792 2779 -539 -134 N ATOM 2136 CA LYS A1095 -9.108 73.964 150.086 1.00153.95 C ANISOU 2136 CA LYS A1095 17283 17573 23637 2728 -511 -106 C ATOM 2137 C LYS A1095 -9.149 72.599 150.790 1.00153.57 C ANISOU 2137 C LYS A1095 17175 17530 23644 2698 -523 -113 C ATOM 2138 O LYS A1095 -8.111 72.098 151.233 1.00152.84 O ANISOU 2138 O LYS A1095 17068 17433 23570 2663 -503 -96 O ATOM 2139 CB LYS A1095 -9.377 75.083 151.100 1.00152.99 C ANISOU 2139 CB LYS A1095 17173 17448 23507 2713 -494 -84 C ATOM 2140 CG LYS A1095 -9.025 76.473 150.601 1.00152.35 C ANISOU 2140 CG LYS A1095 17152 17360 23373 2732 -472 -69 C ATOM 2141 CD LYS A1095 -9.429 77.537 151.607 1.00151.61 C ANISOU 2141 CD LYS A1095 17068 17263 23273 2718 -459 -51 C ATOM 2142 CE LYS A1095 -8.923 78.912 151.204 1.00151.04 C ANISOU 2142 CE LYS A1095 17054 17182 23149 2731 -433 -32 C ATOM 2143 NZ LYS A1095 -9.180 79.919 152.269 1.00150.61 N ANISOU 2143 NZ LYS A1095 17007 17124 23091 2713 -417 -12 N ATOM 2144 N THR A1096 -10.343 72.012 150.895 1.00154.10 N ANISOU 2144 N THR A1096 17208 17605 23738 2712 -555 -138 N ATOM 2145 CA THR A1096 -10.509 70.649 151.423 1.00154.62 C ANISOU 2145 CA THR A1096 17216 17675 23855 2689 -571 -150 C ATOM 2146 C THR A1096 -9.849 69.622 150.498 1.00155.44 C ANISOU 2146 C THR A1096 17313 17780 23965 2696 -577 -162 C ATOM 2147 O THR A1096 -9.133 68.736 150.969 1.00155.30 O ANISOU 2147 O THR A1096 17266 17761 23979 2663 -568 -155 O ATOM 2148 CB THR A1096 -11.998 70.270 151.611 1.00154.83 C ANISOU 2148 CB THR A1096 17210 17709 23906 2707 -605 -177 C ATOM 2149 OG1 THR A1096 -12.706 71.355 152.226 1.00155.73 O ANISOU 2149 OG1 THR A1096 17339 17823 24006 2710 -602 -168 O ATOM 2150 CG2 THR A1096 -12.141 69.015 152.475 1.00154.48 C ANISOU 2150 CG2 THR A1096 17107 17669 23919 2674 -615 -182 C ATOM 2151 N THR A1097 -10.095 69.752 149.191 1.00157.30 N ANISOU 2151 N THR A1097 17578 18018 24170 2739 -592 -182 N ATOM 2152 CA THR A1097 -9.451 68.894 148.179 1.00158.58 C ANISOU 2152 CA THR A1097 17740 18181 24331 2750 -597 -194 C ATOM 2153 C THR A1097 -7.919 69.016 148.205 1.00159.40 C ANISOU 2153 C THR A1097 17864 18277 24423 2723 -562 -167 C ATOM 2154 O THR A1097 -7.207 68.002 148.161 1.00160.02 O ANISOU 2154 O THR A1097 17918 18355 24525 2703 -560 -168 O ATOM 2155 CB THR A1097 -9.971 69.211 146.759 1.00158.98 C ANISOU 2155 CB THR A1097 17825 18234 24343 2803 -616 -218 C ATOM 2156 OG1 THR A1097 -11.380 68.971 146.704 1.00159.94 O ANISOU 2156 OG1 THR A1097 17924 18364 24480 2828 -650 -246 O ATOM 2157 CG2 THR A1097 -9.287 68.322 145.705 1.00158.91 C ANISOU 2157 CG2 THR A1097 17816 18226 24333 2814 -622 -230 C ATOM 2158 N ARG A1098 -7.435 70.257 148.277 1.00160.33 N ANISOU 2158 N ARG A1098 18026 18388 24504 2721 -536 -144 N ATOM 2159 CA ARG A1098 -5.998 70.559 148.373 1.00160.62 C ANISOU 2159 CA ARG A1098 18085 18416 24525 2695 -500 -116 C ATOM 2160 C ARG A1098 -5.336 69.814 149.534 1.00160.80 C ANISOU 2160 C ARG A1098 18066 18438 24592 2645 -486 -100 C ATOM 2161 O ARG A1098 -4.377 69.050 149.331 1.00161.07 O ANISOU 2161 O ARG A1098 18090 18470 24638 2628 -477 -96 O ATOM 2162 CB ARG A1098 -5.782 72.073 148.528 1.00160.49 C ANISOU 2162 CB ARG A1098 18117 18393 24468 2698 -475 -94 C ATOM 2163 CG ARG A1098 -4.326 72.519 148.618 1.00160.75 C ANISOU 2163 CG ARG A1098 18177 18417 24483 2672 -437 -65 C ATOM 2164 CD ARG A1098 -4.207 74.031 148.509 1.00160.97 C ANISOU 2164 CD ARG A1098 18257 18438 24464 2684 -415 -48 C ATOM 2165 NE ARG A1098 -4.930 74.737 149.571 1.00160.77 N ANISOU 2165 NE ARG A1098 18225 18413 24446 2673 -413 -38 N ATOM 2166 CZ ARG A1098 -4.514 74.884 150.832 1.00160.43 C ANISOU 2166 CZ ARG A1098 18164 18367 24425 2630 -393 -14 C ATOM 2167 NH1 ARG A1098 -3.361 74.373 151.252 1.00160.20 N ANISOU 2167 NH1 ARG A1098 18120 18334 24413 2594 -372 1 N ATOM 2168 NH2 ARG A1098 -5.267 75.551 151.700 1.00160.65 N ANISOU 2168 NH2 ARG A1098 18188 18396 24457 2624 -394 -8 N ATOM 2169 N ASN A1099 -5.876 70.029 150.733 1.00161.28 N ANISOU 2169 N ASN A1099 18104 18499 24675 2622 -486 -91 N ATOM 2170 CA ASN A1099 -5.363 69.399 151.957 1.00161.30 C ANISOU 2170 CA ASN A1099 18066 18501 24719 2574 -473 -74 C ATOM 2171 C ASN A1099 -5.607 67.890 151.994 1.00160.98 C ANISOU 2171 C ASN A1099 17975 18466 24724 2566 -497 -94 C ATOM 2172 O ASN A1099 -4.830 67.159 152.612 1.00161.18 O ANISOU 2172 O ASN A1099 17972 18489 24778 2530 -484 -83 O ATOM 2173 CB ASN A1099 -5.982 70.043 153.206 1.00162.36 C ANISOU 2173 CB ASN A1099 18188 18634 24865 2555 -468 -61 C ATOM 2174 CG ASN A1099 -5.608 71.504 153.361 1.00164.22 C ANISOU 2174 CG ASN A1099 18471 18863 25060 2554 -441 -37 C ATOM 2175 OD1 ASN A1099 -5.318 72.192 152.381 1.00166.28 O ANISOU 2175 OD1 ASN A1099 18777 19121 25279 2581 -434 -37 O ATOM 2176 ND2 ASN A1099 -5.612 71.986 154.600 1.00164.61 N ANISOU 2176 ND2 ASN A1099 18509 18910 25122 2523 -426 -17 N ATOM 2177 N ALA A1100 -6.684 67.431 151.348 1.00160.63 N ANISOU 2177 N ALA A1100 17918 18428 24685 2599 -530 -125 N ATOM 2178 CA ALA A1100 -6.975 65.998 151.247 1.00159.53 C ANISOU 2178 CA ALA A1100 17731 18294 24586 2597 -554 -147 C ATOM 2179 C ALA A1100 -5.980 65.270 150.341 1.00158.60 C ANISOU 2179 C ALA A1100 17620 18176 24464 2599 -549 -151 C ATOM 2180 O ALA A1100 -5.364 64.291 150.764 1.00159.30 O ANISOU 2180 O ALA A1100 17676 18264 24586 2570 -545 -146 O ATOM 2181 CB ALA A1100 -8.398 65.772 150.758 1.00159.68 C ANISOU 2181 CB ALA A1100 17739 18322 24611 2633 -590 -179 C ATOM 2182 N TYR A1101 -5.829 65.754 149.107 1.00157.33 N ANISOU 2182 N TYR A1101 17500 18014 24261 2635 -551 -159 N ATOM 2183 CA TYR A1101 -5.032 65.058 148.080 1.00156.49 C ANISOU 2183 CA TYR A1101 17401 17907 24148 2645 -551 -167 C ATOM 2184 C TYR A1101 -3.691 65.715 147.725 1.00154.55 C ANISOU 2184 C TYR A1101 17198 17654 23868 2636 -518 -143 C ATOM 2185 O TYR A1101 -2.661 65.031 147.663 1.00153.28 O ANISOU 2185 O TYR A1101 17027 17491 23720 2615 -505 -135 O ATOM 2186 CB TYR A1101 -5.864 64.881 146.803 1.00157.73 C ANISOU 2186 CB TYR A1101 17570 18070 24288 2694 -581 -199 C ATOM 2187 CG TYR A1101 -7.084 64.000 146.985 1.00159.51 C ANISOU 2187 CG TYR A1101 17750 18304 24550 2704 -616 -227 C ATOM 2188 CD1 TYR A1101 -8.304 64.541 147.406 1.00160.63 C ANISOU 2188 CD1 TYR A1101 17888 18449 24693 2717 -632 -236 C ATOM 2189 CD2 TYR A1101 -7.021 62.616 146.759 1.00159.76 C ANISOU 2189 CD2 TYR A1101 17743 18339 24617 2698 -633 -245 C ATOM 2190 CE1 TYR A1101 -9.425 63.739 147.573 1.00160.96 C ANISOU 2190 CE1 TYR A1101 17888 18499 24770 2725 -663 -262 C ATOM 2191 CE2 TYR A1101 -8.139 61.812 146.927 1.00160.33 C ANISOU 2191 CE2 TYR A1101 17774 18418 24723 2706 -664 -271 C ATOM 2192 CZ TYR A1101 -9.342 62.378 147.327 1.00160.90 C ANISOU 2192 CZ TYR A1101 17843 18494 24796 2720 -679 -279 C ATOM 2193 OH TYR A1101 -10.447 61.579 147.514 1.00160.99 O ANISOU 2193 OH TYR A1101 17813 18513 24843 2727 -709 -306 O ATOM 2194 N ILE A1102 -3.694 67.031 147.509 1.00153.41 N ANISOU 2194 N ILE A1102 17100 17506 23682 2652 -503 -131 N ATOM 2195 CA ILE A1102 -2.581 67.692 146.798 1.00152.52 C ANISOU 2195 CA ILE A1102 17034 17386 23528 2657 -476 -115 C ATOM 2196 C ILE A1102 -1.281 67.769 147.619 1.00151.56 C ANISOU 2196 C ILE A1102 16911 17258 23416 2611 -441 -84 C ATOM 2197 O ILE A1102 -0.182 67.696 147.046 1.00153.13 O ANISOU 2197 O ILE A1102 17130 17452 23599 2607 -423 -76 O ATOM 2198 CB ILE A1102 -2.995 69.090 146.257 1.00152.48 C ANISOU 2198 CB ILE A1102 17082 17377 23474 2690 -471 -112 C ATOM 2199 CG1 ILE A1102 -4.251 68.984 145.366 1.00152.36 C ANISOU 2199 CG1 ILE A1102 17070 17370 23449 2738 -506 -144 C ATOM 2200 CG2 ILE A1102 -1.852 69.760 145.498 1.00152.71 C ANISOU 2200 CG2 ILE A1102 17160 17399 23461 2696 -443 -97 C ATOM 2201 CD1 ILE A1102 -4.147 68.003 144.213 1.00152.35 C ANISOU 2201 CD1 ILE A1102 17063 17373 23450 2762 -526 -168 C ATOM 2202 N GLN A1103 -1.398 67.901 148.944 1.00149.17 N ANISOU 2202 N GLN A1103 16584 16954 23139 2577 -432 -68 N ATOM 2203 CA GLN A1103 -0.223 67.865 149.837 1.00147.37 C ANISOU 2203 CA GLN A1103 16347 16721 22925 2532 -401 -40 C ATOM 2204 C GLN A1103 0.670 66.633 149.633 1.00147.31 C ANISOU 2204 C GLN A1103 16313 16714 22942 2513 -400 -43 C ATOM 2205 O GLN A1103 1.895 66.744 149.694 1.00147.35 O ANISOU 2205 O GLN A1103 16332 16714 22939 2491 -372 -24 O ATOM 2206 CB GLN A1103 -0.637 67.958 151.313 1.00145.54 C ANISOU 2206 CB GLN A1103 16084 16490 22724 2499 -397 -27 C ATOM 2207 CG GLN A1103 -0.916 69.381 151.797 1.00144.14 C ANISOU 2207 CG GLN A1103 15939 16309 22519 2500 -381 -10 C ATOM 2208 CD GLN A1103 -0.957 69.483 153.317 1.00142.96 C ANISOU 2208 CD GLN A1103 15760 16158 22398 2460 -370 8 C ATOM 2209 OE1 GLN A1103 -0.057 69.009 154.010 1.00141.63 O ANISOU 2209 OE1 GLN A1103 15571 15988 22253 2423 -352 24 O ATOM 2210 NE2 GLN A1103 -1.998 70.109 153.839 1.00142.68 N ANISOU 2210 NE2 GLN A1103 15724 16125 22362 2468 -380 6 N ATOM 2211 N LYS A1104 0.053 65.478 149.389 1.00153.13 N ANISOU 2211 N LYS A1104 19948 21713 16522 3176 2441 1464 N ATOM 2212 CA LYS A1104 0.782 64.223 149.155 1.00151.08 C ANISOU 2212 CA LYS A1104 19714 21394 16294 2970 2401 1569 C ATOM 2213 C LYS A1104 1.740 64.333 147.960 1.00147.39 C ANISOU 2213 C LYS A1104 19374 20642 15984 2896 2351 1567 C ATOM 2214 O LYS A1104 2.939 64.051 148.094 1.00146.32 O ANISOU 2214 O LYS A1104 19335 20361 15896 2804 2315 1535 O ATOM 2215 CB LYS A1104 -0.207 63.075 148.940 1.00152.16 C ANISOU 2215 CB LYS A1104 19714 21731 16366 2867 2410 1738 C ATOM 2216 CG LYS A1104 0.409 61.692 148.794 1.00151.87 C ANISOU 2216 CG LYS A1104 19692 21661 16350 2658 2364 1854 C ATOM 2217 CD LYS A1104 -0.661 60.691 148.359 1.00152.26 C ANISOU 2217 CD LYS A1104 19613 21881 16357 2565 2365 2022 C ATOM 2218 CE LYS A1104 -0.089 59.409 147.769 1.00151.17 C ANISOU 2218 CE LYS A1104 19505 21650 16281 2363 2304 2139 C ATOM 2219 NZ LYS A1104 -1.017 58.824 146.759 1.00151.17 N ANISOU 2219 NZ LYS A1104 19423 21709 16305 2300 2294 2275 N ATOM 2220 N TYR A1105 1.205 64.758 146.813 1.00144.17 N ANISOU 2220 N TYR A1105 18961 20164 15652 2938 2349 1601 N ATOM 2221 CA TYR A1105 2.005 64.925 145.588 1.00141.56 C ANISOU 2221 CA TYR A1105 18740 19579 15467 2876 2304 1606 C ATOM 2222 C TYR A1105 3.166 65.893 145.829 1.00139.97 C ANISOU 2222 C TYR A1105 18678 19171 15331 2933 2284 1459 C ATOM 2223 O TYR A1105 4.331 65.572 145.524 1.00139.67 O ANISOU 2223 O TYR A1105 18736 18964 15367 2822 2243 1452 O ATOM 2224 CB TYR A1105 1.131 65.425 144.428 1.00141.77 C ANISOU 2224 CB TYR A1105 18732 19583 15550 2944 2310 1652 C ATOM 2225 CG TYR A1105 1.804 65.412 143.064 1.00139.93 C ANISOU 2225 CG TYR A1105 18588 19124 15455 2861 2265 1687 C ATOM 2226 CD1 TYR A1105 1.831 64.252 142.284 1.00138.65 C ANISOU 2226 CD1 TYR A1105 18396 18962 15323 2702 2236 1817 C ATOM 2227 CD2 TYR A1105 2.399 66.565 142.542 1.00139.19 C ANISOU 2227 CD2 TYR A1105 18606 18820 15458 2940 2248 1592 C ATOM 2228 CE1 TYR A1105 2.440 64.238 141.033 1.00137.32 C ANISOU 2228 CE1 TYR A1105 18302 18601 15272 2630 2195 1846 C ATOM 2229 CE2 TYR A1105 3.009 66.562 141.292 1.00137.72 C ANISOU 2229 CE2 TYR A1105 18494 18441 15390 2862 2208 1629 C ATOM 2230 CZ TYR A1105 3.028 65.398 140.541 1.00136.99 C ANISOU 2230 CZ TYR A1105 18365 18364 15320 2710 2184 1753 C ATOM 2231 OH TYR A1105 3.631 65.390 139.302 1.00135.18 O ANISOU 2231 OH TYR A1105 18204 17956 15200 2636 2144 1786 O ATOM 2232 N LEU A1106 2.841 67.056 146.402 1.00139.12 N ANISOU 2232 N LEU A1106 18581 19085 15193 3107 2312 1340 N ATOM 2233 CA LEU A1106 3.841 68.065 146.749 1.00138.83 C ANISOU 2233 CA LEU A1106 18673 18867 15210 3176 2293 1192 C ATOM 2234 C LEU A1106 4.938 67.497 147.652 1.00137.73 C ANISOU 2234 C LEU A1106 18584 18708 15039 3078 2276 1153 C ATOM 2235 O LEU A1106 6.120 67.594 147.322 1.00136.79 O ANISOU 2235 O LEU A1106 18578 18387 15009 3006 2236 1114 O ATOM 2236 CB LEU A1106 3.182 69.263 147.445 1.00140.76 C ANISOU 2236 CB LEU A1106 18899 19181 15400 3383 2324 1070 C ATOM 2237 CG LEU A1106 4.100 70.446 147.828 1.00141.29 C ANISOU 2237 CG LEU A1106 19099 19060 15523 3475 2300 906 C ATOM 2238 CD1 LEU A1106 4.548 71.221 146.583 1.00140.70 C ANISOU 2238 CD1 LEU A1106 19131 18731 15597 3481 2260 895 C ATOM 2239 CD2 LEU A1106 3.396 71.335 148.838 1.00143.01 C ANISOU 2239 CD2 LEU A1106 19275 19409 15650 3670 2333 787 C ATOM 2240 N GLU A 220 4.536 66.912 148.780 1.00137.85 N ANISOU 2240 N GLU A 220 18512 18939 14926 3076 2306 1166 N ATOM 2241 CA GLU A 220 5.484 66.358 149.762 1.00137.14 C ANISOU 2241 CA GLU A 220 18459 18857 14789 2992 2293 1130 C ATOM 2242 C GLU A 220 6.340 65.215 149.193 1.00134.29 C ANISOU 2242 C GLU A 220 18137 18396 14489 2795 2248 1227 C ATOM 2243 O GLU A 220 7.560 65.184 149.417 1.00134.23 O ANISOU 2243 O GLU A 220 18228 18248 14525 2734 2215 1167 O ATOM 2244 CB GLU A 220 4.754 65.893 151.032 1.00138.60 C ANISOU 2244 CB GLU A 220 18528 19318 14815 3024 2334 1145 C ATOM 2245 CG GLU A 220 4.213 67.024 151.897 1.00141.00 C ANISOU 2245 CG GLU A 220 18809 19719 15044 3222 2373 1011 C ATOM 2246 CD GLU A 220 3.278 66.539 153.000 1.00143.25 C ANISOU 2246 CD GLU A 220 18954 20311 15163 3256 2421 1046 C ATOM 2247 OE1 GLU A 220 3.377 65.365 153.412 1.00144.58 O ANISOU 2247 OE1 GLU A 220 19068 20594 15268 3118 2417 1146 O ATOM 2248 OE2 GLU A 220 2.442 67.335 153.472 1.00144.38 O ANISOU 2248 OE2 GLU A 220 19037 20585 15235 3423 2459 971 O ATOM 2249 N ARG A 221 5.708 64.298 148.453 1.00131.38 N ANISOU 2249 N ARG A 221 17692 18098 14125 2702 2243 1372 N ATOM 2250 CA ARG A 221 6.435 63.178 147.836 1.00128.40 C ANISOU 2250 CA ARG A 221 17347 17630 13808 2522 2195 1466 C ATOM 2251 C ARG A 221 7.399 63.654 146.731 1.00125.65 C ANISOU 2251 C ARG A 221 17118 17019 13602 2491 2155 1427 C ATOM 2252 O ARG A 221 8.550 63.175 146.653 1.00124.59 O ANISOU 2252 O ARG A 221 17061 16761 13517 2382 2113 1418 O ATOM 2253 CB ARG A 221 5.462 62.118 147.291 1.00128.26 C ANISOU 2253 CB ARG A 221 17218 17752 13763 2435 2195 1628 C ATOM 2254 CG ARG A 221 5.959 60.687 147.384 1.00127.46 C ANISOU 2254 CG ARG A 221 17108 17669 13650 2257 2153 1726 C ATOM 2255 CD ARG A 221 5.996 60.212 148.832 1.00128.58 C ANISOU 2255 CD ARG A 221 17207 17976 13670 2241 2167 1717 C ATOM 2256 NE ARG A 221 5.924 58.758 148.952 1.00129.21 N ANISOU 2256 NE ARG A 221 17232 18147 13712 2083 2133 1851 N ATOM 2257 CZ ARG A 221 6.003 58.082 150.103 1.00131.19 C ANISOU 2257 CZ ARG A 221 17446 18538 13863 2031 2131 1876 C ATOM 2258 NH1 ARG A 221 6.169 58.713 151.268 1.00132.34 N ANISOU 2258 NH1 ARG A 221 17596 18757 13928 2125 2166 1772 N ATOM 2259 NH2 ARG A 221 5.918 56.754 150.086 1.00131.23 N ANISOU 2259 NH2 ARG A 221 17407 18606 13848 1882 2091 2007 N ATOM 2260 N ALA A 222 6.935 64.599 145.903 1.00123.40 N ANISOU 2260 N ALA A 222 16847 16658 13379 2588 2166 1405 N ATOM 2261 CA ALA A 222 7.804 65.227 144.901 1.00121.08 C ANISOU 2261 CA ALA A 222 16666 16123 13215 2575 2131 1361 C ATOM 2262 C ALA A 222 8.987 65.945 145.562 1.00120.14 C ANISOU 2262 C ALA A 222 16660 15867 13121 2604 2115 1223 C ATOM 2263 O ALA A 222 10.149 65.759 145.151 1.00119.27 O ANISOU 2263 O ALA A 222 16635 15595 13084 2507 2074 1208 O ATOM 2264 CB ALA A 222 7.015 66.200 144.039 1.00121.47 C ANISOU 2264 CB ALA A 222 16707 16129 13315 2689 2147 1359 C ATOM 2265 N ARG A 223 8.684 66.750 146.586 1.00120.42 N ANISOU 2265 N ARG A 223 16690 15973 13089 2738 2146 1120 N ATOM 2266 CA ARG A 223 9.710 67.386 147.423 1.00120.27 C ANISOU 2266 CA ARG A 223 16766 15856 13073 2772 2133 984 C ATOM 2267 C ARG A 223 10.719 66.365 147.915 1.00118.90 C ANISOU 2267 C ARG A 223 16617 15679 12880 2629 2107 1002 C ATOM 2268 O ARG A 223 11.914 66.519 147.671 1.00118.94 O ANISOU 2268 O ARG A 223 16722 15509 12959 2567 2069 952 O ATOM 2269 CB ARG A 223 9.098 68.089 148.647 1.00121.77 C ANISOU 2269 CB ARG A 223 16919 16185 13163 2927 2173 884 C ATOM 2270 CG ARG A 223 8.596 69.503 148.414 1.00123.26 C ANISOU 2270 CG ARG A 223 17138 16304 13389 3097 2183 793 C ATOM 2271 CD ARG A 223 8.005 70.047 149.707 1.00125.48 C ANISOU 2271 CD ARG A 223 17372 16745 13557 3246 2220 693 C ATOM 2272 NE ARG A 223 7.265 71.294 149.515 1.00127.62 N ANISOU 2272 NE ARG A 223 17649 16990 13848 3424 2231 617 N ATOM 2273 CZ ARG A 223 6.552 71.916 150.458 1.00129.34 C ANISOU 2273 CZ ARG A 223 17818 17349 13974 3585 2262 525 C ATOM 2274 NH1 ARG A 223 6.463 71.428 151.696 1.00130.08 N ANISOU 2274 NH1 ARG A 223 17849 17632 13941 3589 2291 498 N ATOM 2275 NH2 ARG A 223 5.906 73.035 150.154 1.00130.40 N ANISOU 2275 NH2 ARG A 223 17965 17440 14141 3745 2263 459 N ATOM 2276 N SER A 224 10.232 65.318 148.585 1.00118.08 N ANISOU 2276 N SER A 224 16420 15768 12675 2575 2123 1078 N ATOM 2277 CA SER A 224 11.120 64.304 149.173 1.00116.30 C ANISOU 2277 CA SER A 224 16213 15555 12420 2445 2095 1098 C ATOM 2278 C SER A 224 11.965 63.598 148.112 1.00113.17 C ANISOU 2278 C SER A 224 15870 15006 12124 2300 2044 1165 C ATOM 2279 O SER A 224 13.186 63.497 148.275 1.00112.70 O ANISOU 2279 O SER A 224 15892 14825 12101 2234 2010 1110 O ATOM 2280 CB SER A 224 10.339 63.280 150.014 1.00117.12 C ANISOU 2280 CB SER A 224 16201 15901 12398 2408 2118 1186 C ATOM 2281 OG SER A 224 9.594 62.385 149.204 1.00117.66 O ANISOU 2281 OG SER A 224 16191 16037 12475 2327 2112 1333 O ATOM 2282 N THR A 225 11.329 63.144 147.025 1.00110.82 N ANISOU 2282 N THR A 225 15524 14715 11867 2254 2039 1276 N ATOM 2283 CA THR A 225 12.058 62.431 145.959 1.00108.40 C ANISOU 2283 CA THR A 225 15258 14276 11650 2121 1989 1341 C ATOM 2284 C THR A 225 13.061 63.324 145.203 1.00106.38 C ANISOU 2284 C THR A 225 15115 13796 11506 2131 1964 1259 C ATOM 2285 O THR A 225 14.162 62.859 144.852 1.00105.66 O ANISOU 2285 O THR A 225 15085 13589 11470 2026 1920 1256 O ATOM 2286 CB THR A 225 11.107 61.745 144.959 1.00108.16 C ANISOU 2286 CB THR A 225 15147 14311 11636 2072 1987 1477 C ATOM 2287 OG1 THR A 225 10.144 62.692 144.479 1.00110.54 O ANISOU 2287 OG1 THR A 225 15417 14630 11950 2193 2024 1470 O ATOM 2288 CG2 THR A 225 10.378 60.584 145.624 1.00108.40 C ANISOU 2288 CG2 THR A 225 15075 14543 11567 2012 1993 1577 C ATOM 2289 N LEU A 226 12.693 64.592 144.967 1.00105.36 N ANISOU 2289 N LEU A 226 15012 13609 11409 2255 1988 1194 N ATOM 2290 CA LEU A 226 13.641 65.561 144.389 1.00103.60 C ANISOU 2290 CA LEU A 226 14900 13176 11286 2270 1963 1111 C ATOM 2291 C LEU A 226 14.800 65.885 145.337 1.00102.46 C ANISOU 2291 C LEU A 226 14836 12959 11132 2265 1948 994 C ATOM 2292 O LEU A 226 15.970 65.907 144.924 1.00102.21 O ANISOU 2292 O LEU A 226 14885 12777 11171 2188 1909 963 O ATOM 2293 CB LEU A 226 12.935 66.860 143.984 1.00104.56 C ANISOU 2293 CB LEU A 226 15033 13250 11443 2409 1986 1070 C ATOM 2294 CG LEU A 226 12.119 66.845 142.690 1.00104.26 C ANISOU 2294 CG LEU A 226 14950 13205 11456 2410 1989 1169 C ATOM 2295 CD1 LEU A 226 11.235 68.071 142.655 1.00105.43 C ANISOU 2295 CD1 LEU A 226 15093 13355 11609 2570 2017 1122 C ATOM 2296 CD2 LEU A 226 13.015 66.812 141.462 1.00102.92 C ANISOU 2296 CD2 LEU A 226 14849 12859 11395 2312 1947 1197 C ATOM 2297 N GLN A 227 14.473 66.140 146.604 1.00102.07 N ANISOU 2297 N GLN A 227 14764 13024 10993 2349 1977 927 N ATOM 2298 CA GLN A 227 15.493 66.404 147.627 1.00101.59 C ANISOU 2298 CA GLN A 227 14772 12918 10909 2350 1964 815 C ATOM 2299 C GLN A 227 16.398 65.202 147.887 1.00 99.77 C ANISOU 2299 C GLN A 227 14548 12698 10662 2206 1931 853 C ATOM 2300 O GLN A 227 17.556 65.388 148.248 1.00 99.52 O ANISOU 2300 O GLN A 227 14594 12564 10654 2171 1904 772 O ATOM 2301 CB GLN A 227 14.860 66.897 148.934 1.00103.23 C ANISOU 2301 CB GLN A 227 14942 13267 11013 2476 2003 737 C ATOM 2302 CG GLN A 227 14.354 68.330 148.845 1.00104.58 C ANISOU 2302 CG GLN A 227 15144 13378 11212 2633 2021 648 C ATOM 2303 CD GLN A 227 13.516 68.746 150.042 1.00106.07 C ANISOU 2303 CD GLN A 227 15275 13736 11289 2770 2063 581 C ATOM 2304 OE1 GLN A 227 13.599 68.149 151.116 1.00106.27 O ANISOU 2304 OE1 GLN A 227 15261 13898 11217 2749 2076 570 O ATOM 2305 NE2 GLN A 227 12.701 69.781 149.861 1.00107.36 N ANISOU 2305 NE2 GLN A 227 15430 13895 11463 2914 2082 535 N ATOM 2306 N LYS A 228 15.882 63.984 147.700 1.00 98.13 N ANISOU 2306 N LYS A 228 14260 12608 10417 2124 1929 975 N ATOM 2307 CA LYS A 228 16.718 62.774 147.732 1.00 96.08 C ANISOU 2307 CA LYS A 228 14009 12339 10158 1982 1887 1024 C ATOM 2308 C LYS A 228 17.699 62.727 146.557 1.00 93.32 C ANISOU 2308 C LYS A 228 13730 11806 9921 1896 1842 1030 C ATOM 2309 O LYS A 228 18.871 62.364 146.747 1.00 92.19 O ANISOU 2309 O LYS A 228 13643 11587 9797 1818 1804 992 O ATOM 2310 CB LYS A 228 15.859 61.503 147.783 1.00 96.72 C ANISOU 2310 CB LYS A 228 13988 12585 10175 1916 1889 1158 C ATOM 2311 CG LYS A 228 15.281 61.219 149.163 1.00 98.22 C ANISOU 2311 CG LYS A 228 14113 12966 10239 1956 1919 1156 C ATOM 2312 CD LYS A 228 14.107 60.251 149.097 1.00 98.69 C ANISOU 2312 CD LYS A 228 14059 13200 10236 1916 1931 1294 C ATOM 2313 CE LYS A 228 13.446 60.081 150.456 1.00100.51 C ANISOU 2313 CE LYS A 228 14216 13638 10334 1964 1967 1295 C ATOM 2314 NZ LYS A 228 12.159 59.337 150.355 1.00101.28 N ANISOU 2314 NZ LYS A 228 14195 13915 10369 1940 1986 1428 N ATOM 2315 N GLU A 229 17.227 63.098 145.360 1.00 91.93 N ANISOU 2315 N GLU A 229 13547 11568 9814 1912 1846 1076 N ATOM 2316 CA GLU A 229 18.122 63.286 144.198 1.00 89.49 C ANISOU 2316 CA GLU A 229 13305 11085 9611 1848 1808 1072 C ATOM 2317 C GLU A 229 19.197 64.348 144.470 1.00 88.26 C ANISOU 2317 C GLU A 229 13250 10785 9499 1880 1797 946 C ATOM 2318 O GLU A 229 20.380 64.149 144.133 1.00 87.57 O ANISOU 2318 O GLU A 229 13221 10587 9461 1794 1757 920 O ATOM 2319 CB GLU A 229 17.341 63.643 142.921 1.00 89.08 C ANISOU 2319 CB GLU A 229 13227 11000 9618 1875 1818 1140 C ATOM 2320 CG GLU A 229 16.820 62.436 142.151 1.00 88.87 C ANISOU 2320 CG GLU A 229 13128 11045 9591 1788 1802 1269 C ATOM 2321 CD GLU A 229 17.933 61.611 141.503 1.00 88.68 C ANISOU 2321 CD GLU A 229 13141 10932 9621 1658 1747 1289 C ATOM 2322 OE1 GLU A 229 18.906 62.181 140.962 1.00 89.16 O ANISOU 2322 OE1 GLU A 229 13275 10848 9750 1638 1726 1233 O ATOM 2323 OE2 GLU A 229 17.838 60.371 141.524 1.00 88.55 O ANISOU 2323 OE2 GLU A 229 13077 10990 9574 1575 1722 1363 O ATOM 2324 N LEU A 230 18.783 65.456 145.087 1.00 87.82 N ANISOU 2324 N LEU A 230 13213 10732 9422 2003 1828 865 N ATOM 2325 CA LEU A 230 19.724 66.502 145.506 1.00 87.48 C ANISOU 2325 CA LEU A 230 13265 10559 9412 2041 1815 739 C ATOM 2326 C LEU A 230 20.736 65.999 146.544 1.00 86.60 C ANISOU 2326 C LEU A 230 13184 10465 9255 1983 1795 677 C ATOM 2327 O LEU A 230 21.926 66.286 146.435 1.00 85.62 O ANISOU 2327 O LEU A 230 13136 10211 9182 1932 1762 614 O ATOM 2328 CB LEU A 230 18.981 67.716 146.084 1.00 88.81 C ANISOU 2328 CB LEU A 230 13442 10744 9557 2194 1849 660 C ATOM 2329 CG LEU A 230 19.818 68.989 146.297 1.00 89.37 C ANISOU 2329 CG LEU A 230 13618 10654 9682 2244 1829 533 C ATOM 2330 CD1 LEU A 230 20.272 69.626 144.978 1.00 88.89 C ANISOU 2330 CD1 LEU A 230 13620 10416 9738 2209 1799 551 C ATOM 2331 CD2 LEU A 230 19.031 69.997 147.124 1.00 90.91 C ANISOU 2331 CD2 LEU A 230 13811 10896 9831 2404 1859 447 C ATOM 2332 N LYS A 231 20.258 65.250 147.537 1.00 86.61 N ANISOU 2332 N LYS A 231 13121 10628 9157 1989 1815 699 N ATOM 2333 CA LYS A 231 21.101 64.758 148.645 1.00 86.14 C ANISOU 2333 CA LYS A 231 13082 10604 9040 1945 1798 644 C ATOM 2334 C LYS A 231 22.238 63.865 148.173 1.00 84.75 C ANISOU 2334 C LYS A 231 12937 10353 8908 1807 1748 675 C ATOM 2335 O LYS A 231 23.362 64.023 148.644 1.00 84.38 O ANISOU 2335 O LYS A 231 12954 10235 8871 1775 1722 592 O ATOM 2336 CB LYS A 231 20.267 64.004 149.694 1.00 86.26 C ANISOU 2336 CB LYS A 231 13013 10825 8938 1966 1826 687 C ATOM 2337 CG LYS A 231 20.988 63.759 151.010 1.00 86.17 C ANISOU 2337 CG LYS A 231 13021 10863 8853 1952 1817 614 C ATOM 2338 CD LYS A 231 20.172 62.846 151.911 1.00 86.61 C ANISOU 2338 CD LYS A 231 12985 11127 8793 1949 1839 684 C ATOM 2339 CE LYS A 231 20.904 62.500 153.199 1.00 86.77 C ANISOU 2339 CE LYS A 231 13023 11206 8738 1926 1826 624 C ATOM 2340 NZ LYS A 231 20.394 61.234 153.803 1.00 86.87 N ANISOU 2340 NZ LYS A 231 12953 11394 8658 1864 1825 728 N ATOM 2341 N ILE A 232 21.951 62.946 147.247 1.00 84.10 N ANISOU 2341 N ILE A 232 12809 10289 8853 1729 1732 788 N ATOM 2342 CA ILE A 232 22.980 62.025 146.732 1.00 83.09 C ANISOU 2342 CA ILE A 232 12705 10098 8766 1603 1680 818 C ATOM 2343 C ILE A 232 23.998 62.794 145.883 1.00 82.15 C ANISOU 2343 C ILE A 232 12666 9804 8743 1580 1655 758 C ATOM 2344 O ILE A 232 25.221 62.661 146.084 1.00 81.50 O ANISOU 2344 O ILE A 232 12636 9651 8678 1519 1620 700 O ATOM 2345 CB ILE A 232 22.366 60.857 145.921 1.00 83.01 C ANISOU 2345 CB ILE A 232 12626 10150 8761 1531 1663 951 C ATOM 2346 CG1 ILE A 232 21.437 60.008 146.801 1.00 84.19 C ANISOU 2346 CG1 ILE A 232 12696 10477 8813 1536 1680 1019 C ATOM 2347 CG2 ILE A 232 23.457 59.966 145.337 1.00 82.19 C ANISOU 2347 CG2 ILE A 232 12550 9973 8705 1413 1604 970 C ATOM 2348 CD1 ILE A 232 20.566 59.033 146.023 1.00 84.18 C ANISOU 2348 CD1 ILE A 232 12620 10546 8816 1482 1669 1152 C ATOM 2349 N ALA A 233 23.478 63.609 144.957 1.00 81.98 N ANISOU 2349 N ALA A 233 12649 9717 8780 1627 1673 775 N ATOM 2350 CA ALA A 233 24.302 64.447 144.072 1.00 81.08 C ANISOU 2350 CA ALA A 233 12606 9442 8758 1608 1652 732 C ATOM 2351 C ALA A 233 25.432 65.172 144.808 1.00 80.80 C ANISOU 2351 C ALA A 233 12652 9319 8730 1613 1636 609 C ATOM 2352 O ALA A 233 26.577 65.165 144.353 1.00 79.72 O ANISOU 2352 O ALA A 233 12562 9082 8644 1536 1600 582 O ATOM 2353 CB ALA A 233 23.430 65.455 143.333 1.00 81.60 C ANISOU 2353 CB ALA A 233 12670 9463 8868 1690 1679 751 C ATOM 2354 N LYS A 234 25.103 65.783 145.947 1.00 81.49 N ANISOU 2354 N LYS A 234 12750 9449 8763 1705 1663 535 N ATOM 2355 CA LYS A 234 26.101 66.452 146.787 1.00 81.55 C ANISOU 2355 CA LYS A 234 12831 9386 8768 1716 1647 412 C ATOM 2356 C LYS A 234 27.161 65.479 147.302 1.00 79.86 C ANISOU 2356 C LYS A 234 12623 9196 8522 1620 1614 398 C ATOM 2357 O LYS A 234 28.356 65.789 147.249 1.00 79.84 O ANISOU 2357 O LYS A 234 12683 9090 8560 1569 1582 332 O ATOM 2358 CB LYS A 234 25.436 67.171 147.966 1.00 83.38 C ANISOU 2358 CB LYS A 234 13061 9683 8934 1840 1682 336 C ATOM 2359 CG LYS A 234 24.606 68.385 147.574 1.00 84.78 C ANISOU 2359 CG LYS A 234 13254 9806 9149 1951 1705 316 C ATOM 2360 CD LYS A 234 24.164 69.160 148.812 1.00 86.43 C ANISOU 2360 CD LYS A 234 13475 10069 9296 2076 1730 214 C ATOM 2361 CE LYS A 234 23.167 70.261 148.484 1.00 87.58 C ANISOU 2361 CE LYS A 234 13624 10183 9469 2202 1752 198 C ATOM 2362 NZ LYS A 234 22.494 70.788 149.706 1.00 88.66 N ANISOU 2362 NZ LYS A 234 13745 10419 9524 2335 1782 113 N ATOM 2363 N SER A 235 26.725 64.310 147.778 1.00 78.29 N ANISOU 2363 N SER A 235 12358 9133 8253 1593 1618 462 N ATOM 2364 CA SER A 235 27.644 63.268 148.266 1.00 76.54 C ANISOU 2364 CA SER A 235 12138 8943 8000 1502 1581 460 C ATOM 2365 C SER A 235 28.592 62.822 147.153 1.00 74.15 C ANISOU 2365 C SER A 235 11857 8542 7772 1399 1536 488 C ATOM 2366 O SER A 235 29.811 62.766 147.346 1.00 73.19 O ANISOU 2366 O SER A 235 11783 8360 7666 1343 1502 426 O ATOM 2367 CB SER A 235 26.878 62.043 148.789 1.00 76.46 C ANISOU 2367 CB SER A 235 12050 9090 7910 1485 1588 547 C ATOM 2368 OG SER A 235 25.844 62.416 149.672 1.00 77.22 O ANISOU 2368 OG SER A 235 12108 9298 7931 1581 1634 538 O ATOM 2369 N LEU A 236 28.018 62.527 145.990 1.00 72.42 N ANISOU 2369 N LEU A 236 11602 8316 7597 1376 1537 580 N ATOM 2370 CA LEU A 236 28.807 62.108 144.831 1.00 71.04 C ANISOU 2370 CA LEU A 236 11439 8062 7490 1285 1497 611 C ATOM 2371 C LEU A 236 29.736 63.217 144.325 1.00 70.57 C ANISOU 2371 C LEU A 236 11450 7862 7500 1277 1486 536 C ATOM 2372 O LEU A 236 30.845 62.927 143.870 1.00 70.15 O ANISOU 2372 O LEU A 236 11420 7750 7482 1197 1447 517 O ATOM 2373 CB LEU A 236 27.899 61.617 143.698 1.00 70.66 C ANISOU 2373 CB LEU A 236 11334 8044 7470 1271 1502 723 C ATOM 2374 CG LEU A 236 27.089 60.355 144.016 1.00 70.49 C ANISOU 2374 CG LEU A 236 11240 8152 7388 1252 1499 812 C ATOM 2375 CD1 LEU A 236 26.027 60.154 142.945 1.00 70.51 C ANISOU 2375 CD1 LEU A 236 11188 8181 7418 1258 1512 913 C ATOM 2376 CD2 LEU A 236 27.984 59.130 144.159 1.00 69.62 C ANISOU 2376 CD2 LEU A 236 11129 8057 7266 1158 1443 821 C ATOM 2377 N ALA A 237 29.289 64.472 144.417 1.00 70.30 N ANISOU 2377 N ALA A 237 11447 7776 7486 1360 1517 494 N ATOM 2378 CA ALA A 237 30.133 65.625 144.090 1.00 69.70 C ANISOU 2378 CA ALA A 237 11445 7563 7474 1355 1504 420 C ATOM 2379 C ALA A 237 31.307 65.739 145.059 1.00 69.20 C ANISOU 2379 C ALA A 237 11432 7471 7388 1328 1479 317 C ATOM 2380 O ALA A 237 32.462 65.858 144.631 1.00 68.61 O ANISOU 2380 O ALA A 237 11395 7315 7356 1253 1445 284 O ATOM 2381 CB ALA A 237 29.315 66.905 144.101 1.00 70.87 C ANISOU 2381 CB ALA A 237 11618 7663 7644 1459 1536 395 C ATOM 2382 N LEU A 238 31.010 65.676 146.360 1.00 69.16 N ANISOU 2382 N LEU A 238 11423 7544 7310 1385 1497 268 N ATOM 2383 CA LEU A 238 32.046 65.685 147.413 1.00 68.99 C ANISOU 2383 CA LEU A 238 11443 7516 7254 1364 1475 171 C ATOM 2384 C LEU A 238 33.150 64.659 147.158 1.00 68.03 C ANISOU 2384 C LEU A 238 11314 7396 7136 1254 1431 186 C ATOM 2385 O LEU A 238 34.330 64.947 147.362 1.00 68.02 O ANISOU 2385 O LEU A 238 11361 7328 7152 1209 1401 110 O ATOM 2386 CB LEU A 238 31.425 65.430 148.794 1.00 69.35 C ANISOU 2386 CB LEU A 238 11461 7682 7203 1434 1501 144 C ATOM 2387 CG LEU A 238 32.372 65.324 149.989 1.00 69.30 C ANISOU 2387 CG LEU A 238 11488 7693 7147 1419 1481 50 C ATOM 2388 CD1 LEU A 238 33.187 66.600 150.124 1.00 69.81 C ANISOU 2388 CD1 LEU A 238 11634 7629 7258 1435 1467 -61 C ATOM 2389 CD2 LEU A 238 31.587 65.032 151.256 1.00 69.90 C ANISOU 2389 CD2 LEU A 238 11526 7908 7122 1490 1511 40 C ATOM 2390 N ILE A 239 32.756 63.466 146.720 1.00 67.22 N ANISOU 2390 N ILE A 239 11152 7371 7018 1212 1423 280 N ATOM 2391 CA ILE A 239 33.718 62.436 146.324 1.00 66.41 C ANISOU 2391 CA ILE A 239 11038 7268 6925 1113 1376 300 C ATOM 2392 C ILE A 239 34.615 62.927 145.179 1.00 66.08 C ANISOU 2392 C ILE A 239 11028 7114 6963 1054 1351 285 C ATOM 2393 O ILE A 239 35.833 62.731 145.227 1.00 66.34 O ANISOU 2393 O ILE A 239 11086 7114 7005 991 1314 234 O ATOM 2394 CB ILE A 239 32.997 61.108 145.988 1.00 66.05 C ANISOU 2394 CB ILE A 239 10924 7318 6854 1086 1367 408 C ATOM 2395 CG1 ILE A 239 32.457 60.486 147.288 1.00 66.58 C ANISOU 2395 CG1 ILE A 239 10962 7501 6832 1119 1378 416 C ATOM 2396 CG2 ILE A 239 33.922 60.122 145.279 1.00 65.28 C ANISOU 2396 CG2 ILE A 239 10816 7203 6783 991 1313 432 C ATOM 2397 CD1 ILE A 239 31.298 59.539 147.082 1.00 66.51 C ANISOU 2397 CD1 ILE A 239 10884 7592 6793 1120 1386 530 C ATOM 2398 N LEU A 240 34.024 63.577 144.175 1.00 65.68 N ANISOU 2398 N LEU A 240 10975 7012 6966 1075 1372 330 N ATOM 2399 CA LEU A 240 34.798 64.155 143.064 1.00 65.10 C ANISOU 2399 CA LEU A 240 10931 6838 6966 1019 1352 324 C ATOM 2400 C LEU A 240 35.758 65.236 143.563 1.00 65.02 C ANISOU 2400 C LEU A 240 10991 6737 6976 1016 1341 220 C ATOM 2401 O LEU A 240 36.947 65.237 143.206 1.00 64.84 O ANISOU 2401 O LEU A 240 10989 6667 6980 940 1307 186 O ATOM 2402 CB LEU A 240 33.872 64.721 141.981 1.00 65.54 C ANISOU 2402 CB LEU A 240 10972 6859 7072 1050 1377 396 C ATOM 2403 CG LEU A 240 34.522 65.321 140.728 1.00 65.48 C ANISOU 2403 CG LEU A 240 10985 6756 7136 992 1358 408 C ATOM 2404 CD1 LEU A 240 35.369 64.285 140.001 1.00 64.63 C ANISOU 2404 CD1 LEU A 240 10843 6677 7034 898 1320 436 C ATOM 2405 CD2 LEU A 240 33.460 65.906 139.798 1.00 65.83 C ANISOU 2405 CD2 LEU A 240 11015 6773 7222 1037 1386 482 C ATOM 2406 N PHE A 241 35.238 66.143 144.390 1.00 65.16 N ANISOU 2406 N PHE A 241 11043 6734 6979 1099 1369 167 N ATOM 2407 CA PHE A 241 36.058 67.189 145.004 1.00 65.45 C ANISOU 2407 CA PHE A 241 11152 6685 7031 1105 1355 61 C ATOM 2408 C PHE A 241 37.235 66.584 145.765 1.00 64.91 C ANISOU 2408 C PHE A 241 11093 6645 6925 1046 1323 -3 C ATOM 2409 O PHE A 241 38.379 67.009 145.583 1.00 65.18 O ANISOU 2409 O PHE A 241 11165 6606 6992 984 1292 -56 O ATOM 2410 CB PHE A 241 35.225 68.067 145.942 1.00 66.55 C ANISOU 2410 CB PHE A 241 11319 6820 7145 1217 1387 8 C ATOM 2411 CG PHE A 241 36.023 69.136 146.636 1.00 67.63 C ANISOU 2411 CG PHE A 241 11531 6866 7296 1228 1368 -106 C ATOM 2412 CD1 PHE A 241 36.413 70.279 145.954 1.00 68.35 C ANISOU 2412 CD1 PHE A 241 11680 6822 7466 1210 1350 -127 C ATOM 2413 CD2 PHE A 241 36.395 68.997 147.967 1.00 68.28 C ANISOU 2413 CD2 PHE A 241 11630 6998 7316 1252 1365 -191 C ATOM 2414 CE1 PHE A 241 37.154 71.269 146.588 1.00 69.16 C ANISOU 2414 CE1 PHE A 241 11856 6835 7587 1215 1326 -233 C ATOM 2415 CE2 PHE A 241 37.139 69.980 148.605 1.00 69.08 C ANISOU 2415 CE2 PHE A 241 11801 7014 7431 1261 1343 -302 C ATOM 2416 CZ PHE A 241 37.520 71.117 147.915 1.00 69.39 C ANISOU 2416 CZ PHE A 241 11900 6913 7552 1241 1323 -323 C ATOM 2417 N LEU A 242 36.948 65.585 146.601 1.00 64.07 N ANISOU 2417 N LEU A 242 10947 6648 6745 1062 1328 6 N ATOM 2418 CA LEU A 242 37.989 64.896 147.373 1.00 63.13 C ANISOU 2418 CA LEU A 242 10833 6567 6583 1012 1295 -48 C ATOM 2419 C LEU A 242 38.996 64.185 146.471 1.00 61.59 C ANISOU 2419 C LEU A 242 10621 6358 6421 912 1253 -22 C ATOM 2420 O LEU A 242 40.201 64.248 146.724 1.00 61.51 O ANISOU 2420 O LEU A 242 10638 6318 6413 859 1220 -91 O ATOM 2421 CB LEU A 242 37.370 63.918 148.378 1.00 63.07 C ANISOU 2421 CB LEU A 242 10784 6685 6492 1048 1306 -25 C ATOM 2422 CG LEU A 242 36.659 64.591 149.563 1.00 63.98 C ANISOU 2422 CG LEU A 242 10917 6835 6555 1145 1342 -80 C ATOM 2423 CD1 LEU A 242 35.697 63.624 150.239 1.00 63.96 C ANISOU 2423 CD1 LEU A 242 10856 6971 6475 1182 1362 -18 C ATOM 2424 CD2 LEU A 242 37.654 65.149 150.572 1.00 64.41 C ANISOU 2424 CD2 LEU A 242 11027 6856 6588 1145 1323 -199 C ATOM 2425 N PHE A 243 38.509 63.534 145.415 1.00 60.24 N ANISOU 2425 N PHE A 243 10403 6211 6274 888 1253 71 N ATOM 2426 CA PHE A 243 39.381 62.889 144.427 1.00 58.97 C ANISOU 2426 CA PHE A 243 10219 6040 6144 801 1214 96 C ATOM 2427 C PHE A 243 40.320 63.905 143.789 1.00 58.64 C ANISOU 2427 C PHE A 243 10218 5901 6161 754 1201 50 C ATOM 2428 O PHE A 243 41.545 63.718 143.796 1.00 58.10 O ANISOU 2428 O PHE A 243 10158 5823 6093 689 1164 0 O ATOM 2429 CB PHE A 243 38.552 62.194 143.342 1.00 58.51 C ANISOU 2429 CB PHE A 243 10106 6019 6106 794 1219 203 C ATOM 2430 CG PHE A 243 39.376 61.425 142.350 1.00 57.94 C ANISOU 2430 CG PHE A 243 10004 5953 6057 715 1176 226 C ATOM 2431 CD1 PHE A 243 39.714 60.100 142.589 1.00 57.52 C ANISOU 2431 CD1 PHE A 243 9918 5968 5967 684 1137 236 C ATOM 2432 CD2 PHE A 243 39.820 62.026 141.175 1.00 57.93 C ANISOU 2432 CD2 PHE A 243 10007 5890 6113 672 1171 237 C ATOM 2433 CE1 PHE A 243 40.479 59.389 141.676 1.00 56.95 C ANISOU 2433 CE1 PHE A 243 9817 5904 5915 621 1093 248 C ATOM 2434 CE2 PHE A 243 40.589 61.321 140.261 1.00 57.27 C ANISOU 2434 CE2 PHE A 243 9890 5826 6044 603 1132 252 C ATOM 2435 CZ PHE A 243 40.919 60.004 140.511 1.00 56.68 C ANISOU 2435 CZ PHE A 243 9782 5820 5933 582 1093 253 C ATOM 2436 N ALA A 244 39.736 64.979 143.253 1.00 58.77 N ANISOU 2436 N ALA A 244 10258 5847 6224 785 1228 70 N ATOM 2437 CA ALA A 244 40.507 66.052 142.600 1.00 58.65 C ANISOU 2437 CA ALA A 244 10284 5730 6268 739 1215 40 C ATOM 2438 C ALA A 244 41.517 66.692 143.549 1.00 58.83 C ANISOU 2438 C ALA A 244 10363 5707 6282 722 1195 -67 C ATOM 2439 O ALA A 244 42.687 66.894 143.188 1.00 58.24 O ANISOU 2439 O ALA A 244 10301 5595 6230 644 1163 -101 O ATOM 2440 CB ALA A 244 39.571 67.113 142.041 1.00 59.02 C ANISOU 2440 CB ALA A 244 10353 5706 6363 789 1245 80 C ATOM 2441 N LEU A 245 41.058 66.983 144.766 1.00 59.33 N ANISOU 2441 N LEU A 245 10455 5781 6306 797 1214 -121 N ATOM 2442 CA LEU A 245 41.897 67.606 145.788 1.00 60.09 C ANISOU 2442 CA LEU A 245 10605 5837 6387 794 1196 -230 C ATOM 2443 C LEU A 245 43.038 66.679 146.213 1.00 59.46 C ANISOU 2443 C LEU A 245 10506 5817 6267 728 1160 -270 C ATOM 2444 O LEU A 245 44.174 67.134 146.375 1.00 59.83 O ANISOU 2444 O LEU A 245 10587 5817 6328 673 1131 -339 O ATOM 2445 CB LEU A 245 41.058 68.018 147.005 1.00 61.13 C ANISOU 2445 CB LEU A 245 10763 5986 6476 897 1225 -278 C ATOM 2446 CG LEU A 245 41.671 69.037 147.972 1.00 62.33 C ANISOU 2446 CG LEU A 245 10984 6071 6626 916 1211 -395 C ATOM 2447 CD1 LEU A 245 41.738 70.422 147.338 1.00 63.17 C ANISOU 2447 CD1 LEU A 245 11148 6041 6811 912 1202 -410 C ATOM 2448 CD2 LEU A 245 40.869 69.082 149.264 1.00 63.04 C ANISOU 2448 CD2 LEU A 245 11079 6221 6650 1019 1238 -441 C ATOM 2449 N SER A 246 42.735 65.390 146.378 1.00 58.58 N ANISOU 2449 N SER A 246 10342 5807 6108 733 1160 -225 N ATOM 2450 CA SER A 246 43.756 64.379 146.678 1.00 57.68 C ANISOU 2450 CA SER A 246 10204 5752 5957 675 1120 -253 C ATOM 2451 C SER A 246 44.763 64.206 145.537 1.00 56.78 C ANISOU 2451 C SER A 246 10072 5615 5886 585 1086 -239 C ATOM 2452 O SER A 246 45.972 64.115 145.783 1.00 56.48 O ANISOU 2452 O SER A 246 10042 5578 5839 530 1051 -303 O ATOM 2453 CB SER A 246 43.100 63.025 146.986 1.00 57.29 C ANISOU 2453 CB SER A 246 10104 5807 5855 700 1120 -193 C ATOM 2454 OG SER A 246 42.249 63.101 148.125 1.00 57.89 O ANISOU 2454 OG SER A 246 10189 5926 5879 777 1149 -206 O ATOM 2455 N TRP A 247 44.264 64.176 144.296 1.00 56.17 N ANISOU 2455 N TRP A 247 9964 5524 5851 571 1097 -158 N ATOM 2456 CA TRP A 247 45.104 63.835 143.125 1.00 55.12 C ANISOU 2456 CA TRP A 247 9799 5395 5749 490 1067 -133 C ATOM 2457 C TRP A 247 45.856 64.980 142.441 1.00 55.16 C ANISOU 2457 C TRP A 247 9832 5317 5807 431 1060 -156 C ATOM 2458 O TRP A 247 46.951 64.747 141.925 1.00 54.67 O ANISOU 2458 O TRP A 247 9748 5271 5749 357 1027 -175 O ATOM 2459 CB TRP A 247 44.290 63.052 142.086 1.00 54.47 C ANISOU 2459 CB TRP A 247 9660 5355 5678 496 1074 -33 C ATOM 2460 CG TRP A 247 44.211 61.600 142.417 1.00 53.89 C ANISOU 2460 CG TRP A 247 9545 5372 5558 503 1049 -15 C ATOM 2461 CD1 TRP A 247 43.140 60.920 142.918 1.00 53.73 C ANISOU 2461 CD1 TRP A 247 9507 5402 5505 559 1065 31 C ATOM 2462 CD2 TRP A 247 45.270 60.655 142.300 1.00 53.30 C ANISOU 2462 CD2 TRP A 247 9441 5345 5463 450 999 -44 C ATOM 2463 NE1 TRP A 247 43.464 59.598 143.105 1.00 53.10 N ANISOU 2463 NE1 TRP A 247 9393 5391 5390 540 1024 38 N ATOM 2464 CE2 TRP A 247 44.770 59.410 142.735 1.00 52.97 C ANISOU 2464 CE2 TRP A 247 9370 5372 5381 478 982 -11 C ATOM 2465 CE3 TRP A 247 46.595 60.737 141.858 1.00 53.27 C ANISOU 2465 CE3 TRP A 247 9431 5337 5471 382 965 -95 C ATOM 2466 CZ2 TRP A 247 45.552 58.250 142.737 1.00 52.78 C ANISOU 2466 CZ2 TRP A 247 9317 5402 5333 445 927 -29 C ATOM 2467 CZ3 TRP A 247 47.369 59.594 141.863 1.00 52.98 C ANISOU 2467 CZ3 TRP A 247 9360 5365 5406 354 915 -117 C ATOM 2468 CH2 TRP A 247 46.847 58.361 142.297 1.00 52.72 C ANISOU 2468 CH2 TRP A 247 9303 5389 5337 388 895 -86 C ATOM 2469 N LEU A 248 45.292 66.192 142.430 1.00 55.64 N ANISOU 2469 N LEU A 248 9940 5293 5905 463 1086 -154 N ATOM 2470 CA LEU A 248 45.905 67.323 141.688 1.00 55.97 C ANISOU 2470 CA LEU A 248 10013 5247 6005 403 1076 -159 C ATOM 2471 C LEU A 248 47.349 67.707 142.076 1.00 55.90 C ANISOU 2471 C LEU A 248 10029 5216 5994 329 1039 -244 C ATOM 2472 O LEU A 248 48.156 68.026 141.187 1.00 55.99 O ANISOU 2472 O LEU A 248 10028 5208 6035 246 1018 -230 O ATOM 2473 CB LEU A 248 45.000 68.565 141.714 1.00 56.94 C ANISOU 2473 CB LEU A 248 10190 5273 6171 460 1103 -146 C ATOM 2474 CG LEU A 248 43.826 68.530 140.722 1.00 56.95 C ANISOU 2474 CG LEU A 248 10162 5274 6200 496 1132 -43 C ATOM 2475 CD1 LEU A 248 42.801 69.610 141.054 1.00 57.80 C ANISOU 2475 CD1 LEU A 248 10323 5301 6337 580 1159 -43 C ATOM 2476 CD2 LEU A 248 44.303 68.656 139.276 1.00 56.74 C ANISOU 2476 CD2 LEU A 248 10106 5234 6217 412 1117 19 C ATOM 2477 N PRO A 249 47.682 67.686 143.384 1.00 55.98 N ANISOU 2477 N PRO A 249 10071 5233 5964 357 1031 -330 N ATOM 2478 CA PRO A 249 49.062 67.972 143.810 1.00 56.37 C ANISOU 2478 CA PRO A 249 10140 5271 6006 287 994 -413 C ATOM 2479 C PRO A 249 50.150 67.132 143.111 1.00 55.74 C ANISOU 2479 C PRO A 249 10000 5265 5913 203 961 -406 C ATOM 2480 O PRO A 249 51.101 67.700 142.551 1.00 55.74 O ANISOU 2480 O PRO A 249 10001 5237 5940 119 938 -420 O ATOM 2481 CB PRO A 249 49.021 67.681 145.314 1.00 56.52 C ANISOU 2481 CB PRO A 249 10184 5321 5969 347 994 -491 C ATOM 2482 CG PRO A 249 47.629 68.018 145.706 1.00 56.72 C ANISOU 2482 CG PRO A 249 10234 5321 5995 445 1035 -465 C ATOM 2483 CD PRO A 249 46.769 67.606 144.544 1.00 56.16 C ANISOU 2483 CD PRO A 249 10118 5270 5950 454 1057 -356 C ATOM 2484 N LEU A 250 49.988 65.807 143.126 1.00 55.07 N ANISOU 2484 N LEU A 250 9862 5276 5786 225 956 -382 N ATOM 2485 CA LEU A 250 50.948 64.891 142.486 1.00 54.53 C ANISOU 2485 CA LEU A 250 9733 5287 5699 161 921 -380 C ATOM 2486 C LEU A 250 51.089 65.142 140.973 1.00 54.45 C ANISOU 2486 C LEU A 250 9685 5271 5731 101 921 -314 C ATOM 2487 O LEU A 250 52.171 64.943 140.410 1.00 54.04 O ANISOU 2487 O LEU A 250 9596 5263 5674 28 891 -332 O ATOM 2488 CB LEU A 250 50.562 63.428 142.746 1.00 53.77 C ANISOU 2488 CB LEU A 250 9592 5279 5556 206 912 -359 C ATOM 2489 CG LEU A 250 51.593 62.346 142.394 1.00 53.22 C ANISOU 2489 CG LEU A 250 9466 5295 5458 160 865 -380 C ATOM 2490 CD1 LEU A 250 52.798 62.390 143.321 1.00 53.47 C ANISOU 2490 CD1 LEU A 250 9514 5343 5457 129 833 -478 C ATOM 2491 CD2 LEU A 250 50.947 60.974 142.446 1.00 52.68 C ANISOU 2491 CD2 LEU A 250 9361 5294 5360 209 854 -337 C ATOM 2492 N HIS A 251 50.000 65.573 140.330 1.00 54.55 N ANISOU 2492 N HIS A 251 9706 5239 5781 133 954 -237 N ATOM 2493 CA HIS A 251 50.043 66.014 138.931 1.00 54.64 C ANISOU 2493 CA HIS A 251 9691 5234 5834 78 957 -170 C ATOM 2494 C HIS A 251 50.806 67.330 138.790 1.00 55.48 C ANISOU 2494 C HIS A 251 9839 5261 5978 8 947 -197 C ATOM 2495 O HIS A 251 51.737 67.425 137.980 1.00 55.46 O ANISOU 2495 O HIS A 251 9801 5289 5982 -77 924 -189 O ATOM 2496 CB HIS A 251 48.636 66.145 138.340 1.00 54.46 C ANISOU 2496 CB HIS A 251 9667 5183 5840 136 994 -81 C ATOM 2497 CG HIS A 251 47.957 64.831 138.121 1.00 53.53 C ANISOU 2497 CG HIS A 251 9496 5149 5692 182 998 -35 C ATOM 2498 ND1 HIS A 251 48.475 63.859 137.293 1.00 52.88 N ANISOU 2498 ND1 HIS A 251 9348 5151 5593 141 971 -16 N ATOM 2499 CD2 HIS A 251 46.803 64.329 138.618 1.00 53.16 C ANISOU 2499 CD2 HIS A 251 9452 5117 5630 263 1021 -6 C ATOM 2500 CE1 HIS A 251 47.670 62.812 137.295 1.00 52.28 C ANISOU 2500 CE1 HIS A 251 9240 5126 5496 195 974 22 C ATOM 2501 NE2 HIS A 251 46.646 63.072 138.087 1.00 52.42 N ANISOU 2501 NE2 HIS A 251 9297 5105 5513 264 1005 33 N ATOM 2502 N ILE A 252 50.448 68.325 139.600 1.00 56.35 N ANISOU 2502 N ILE A 252 10023 5275 6111 42 958 -231 N ATOM 2503 CA ILE A 252 51.182 69.603 139.587 1.00 57.57 C ANISOU 2503 CA ILE A 252 10227 5341 6305 -25 939 -263 C ATOM 2504 C ILE A 252 52.693 69.346 139.743 1.00 58.05 C ANISOU 2504 C ILE A 252 10260 5458 6336 -112 901 -327 C ATOM 2505 O ILE A 252 53.510 69.921 139.003 1.00 58.19 O ANISOU 2505 O ILE A 252 10267 5464 6378 -208 880 -312 O ATOM 2506 CB ILE A 252 50.662 70.591 140.662 1.00 58.15 C ANISOU 2506 CB ILE A 252 10387 5307 6398 36 949 -315 C ATOM 2507 CG1 ILE A 252 49.249 71.076 140.297 1.00 58.20 C ANISOU 2507 CG1 ILE A 252 10419 5250 6443 112 983 -246 C ATOM 2508 CG2 ILE A 252 51.593 71.798 140.807 1.00 59.00 C ANISOU 2508 CG2 ILE A 252 10549 5324 6542 -41 916 -364 C ATOM 2509 CD1 ILE A 252 48.471 71.645 141.467 1.00 58.89 C ANISOU 2509 CD1 ILE A 252 10573 5272 6530 209 999 -301 C ATOM 2510 N LEU A 253 53.044 68.463 140.683 1.00 58.26 N ANISOU 2510 N LEU A 253 10273 5553 6309 -81 890 -394 N ATOM 2511 CA LEU A 253 54.433 68.021 140.864 1.00 58.69 C ANISOU 2511 CA LEU A 253 10292 5680 6327 -151 852 -458 C ATOM 2512 C LEU A 253 55.046 67.396 139.593 1.00 58.89 C ANISOU 2512 C LEU A 253 10235 5797 6344 -218 837 -411 C ATOM 2513 O LEU A 253 56.217 67.639 139.294 1.00 59.18 O ANISOU 2513 O LEU A 253 10245 5863 6374 -306 809 -440 O ATOM 2514 CB LEU A 253 54.552 67.045 142.041 1.00 58.29 C ANISOU 2514 CB LEU A 253 10236 5691 6218 -93 843 -525 C ATOM 2515 CG LEU A 253 54.436 67.645 143.450 1.00 58.86 C ANISOU 2515 CG LEU A 253 10381 5700 6281 -48 846 -602 C ATOM 2516 CD1 LEU A 253 54.266 66.568 144.513 1.00 58.34 C ANISOU 2516 CD1 LEU A 253 10305 5706 6154 20 843 -644 C ATOM 2517 CD2 LEU A 253 55.648 68.500 143.785 1.00 59.70 C ANISOU 2517 CD2 LEU A 253 10517 5769 6397 -128 814 -676 C ATOM 2518 N ASN A 254 54.266 66.597 138.860 1.00 58.85 N ANISOU 2518 N ASN A 254 10185 5841 6335 -176 854 -341 N ATOM 2519 CA ASN A 254 54.738 66.004 137.595 1.00 58.95 C ANISOU 2519 CA ASN A 254 10117 5943 6338 -229 840 -297 C ATOM 2520 C ASN A 254 54.917 67.039 136.495 1.00 59.72 C ANISOU 2520 C ASN A 254 10210 6001 6478 -308 845 -237 C ATOM 2521 O ASN A 254 55.858 66.945 135.700 1.00 59.17 O ANISOU 2521 O ASN A 254 10082 6004 6394 -387 824 -232 O ATOM 2522 CB ASN A 254 53.796 64.896 137.103 1.00 58.54 C ANISOU 2522 CB ASN A 254 10022 5947 6272 -162 853 -239 C ATOM 2523 CG ASN A 254 53.863 63.647 137.958 1.00 57.97 C ANISOU 2523 CG ASN A 254 9933 5939 6151 -105 833 -290 C ATOM 2524 OD1 ASN A 254 54.649 63.563 138.901 1.00 57.99 O ANISOU 2524 OD1 ASN A 254 9952 5953 6126 -114 810 -370 O ATOM 2525 ND2 ASN A 254 53.032 62.667 137.627 1.00 57.48 N ANISOU 2525 ND2 ASN A 254 9840 5919 6080 -49 837 -241 N ATOM 2526 N CYS A 255 54.007 68.011 136.448 1.00 61.25 N ANISOU 2526 N CYS A 255 10464 6086 6722 -284 872 -189 N ATOM 2527 CA CYS A 255 54.106 69.130 135.503 1.00 62.65 C ANISOU 2527 CA CYS A 255 10652 6204 6947 -359 873 -127 C ATOM 2528 C CYS A 255 55.316 70.011 135.800 1.00 64.03 C ANISOU 2528 C CYS A 255 10852 6345 7130 -455 842 -179 C ATOM 2529 O CYS A 255 56.117 70.288 134.894 1.00 64.04 O ANISOU 2529 O CYS A 255 10808 6389 7132 -553 824 -147 O ATOM 2530 CB CYS A 255 52.825 69.966 135.505 1.00 62.95 C ANISOU 2530 CB CYS A 255 10755 6124 7038 -299 903 -72 C ATOM 2531 SG CYS A 255 51.391 69.091 134.842 1.00 62.50 S ANISOU 2531 SG CYS A 255 10658 6109 6977 -208 939 12 S ATOM 2532 N ILE A 256 55.464 70.432 137.059 1.00 65.62 N ANISOU 2532 N ILE A 256 11120 6478 7334 -429 833 -258 N ATOM 2533 CA ILE A 256 56.606 71.292 137.416 1.00 67.75 C ANISOU 2533 CA ILE A 256 11418 6709 7613 -522 799 -313 C ATOM 2534 C ILE A 256 57.963 70.588 137.269 1.00 67.90 C ANISOU 2534 C ILE A 256 11361 6858 7579 -596 770 -358 C ATOM 2535 O ILE A 256 58.931 71.238 136.903 1.00 69.10 O ANISOU 2535 O ILE A 256 11501 7013 7739 -703 744 -359 O ATOM 2536 CB ILE A 256 56.472 71.996 138.802 1.00 68.89 C ANISOU 2536 CB ILE A 256 11656 6745 7773 -478 792 -394 C ATOM 2537 CG1 ILE A 256 56.556 71.001 139.962 1.00 68.46 C ANISOU 2537 CG1 ILE A 256 11594 6757 7661 -405 794 -478 C ATOM 2538 CG2 ILE A 256 55.203 72.855 138.847 1.00 69.52 C ANISOU 2538 CG2 ILE A 256 11809 6694 7909 -410 816 -351 C ATOM 2539 CD1 ILE A 256 56.101 71.571 141.292 1.00 69.12 C ANISOU 2539 CD1 ILE A 256 11762 6746 7752 -334 798 -548 C ATOM 2540 N THR A 257 58.035 69.279 137.511 1.00 67.46 N ANISOU 2540 N THR A 257 11252 6910 7470 -541 771 -391 N ATOM 2541 CA THR A 257 59.273 68.518 137.245 1.00 67.62 C ANISOU 2541 CA THR A 257 11190 7063 7436 -600 741 -432 C ATOM 2542 C THR A 257 59.588 68.425 135.745 1.00 67.70 C ANISOU 2542 C THR A 257 11121 7155 7444 -671 739 -358 C ATOM 2543 O THR A 257 60.752 68.561 135.348 1.00 68.08 O ANISOU 2543 O THR A 257 11118 7278 7470 -764 713 -376 O ATOM 2544 CB THR A 257 59.239 67.092 137.840 1.00 66.80 C ANISOU 2544 CB THR A 257 11051 7049 7278 -518 734 -484 C ATOM 2545 OG1 THR A 257 58.033 66.435 137.450 1.00 66.23 O ANISOU 2545 OG1 THR A 257 10970 6979 7213 -436 761 -422 O ATOM 2546 CG2 THR A 257 59.328 67.135 139.362 1.00 67.10 C ANISOU 2546 CG2 THR A 257 11151 7040 7302 -472 726 -571 C ATOM 2547 N LEU A 258 58.555 68.197 134.927 1.00 67.38 N ANISOU 2547 N LEU A 258 11067 7109 7423 -626 767 -275 N ATOM 2548 CA LEU A 258 58.703 68.170 133.464 1.00 67.07 C ANISOU 2548 CA LEU A 258 10955 7144 7382 -686 769 -196 C ATOM 2549 C LEU A 258 59.130 69.525 132.921 1.00 68.38 C ANISOU 2549 C LEU A 258 11143 7250 7587 -796 762 -148 C ATOM 2550 O LEU A 258 60.167 69.626 132.266 1.00 68.66 O ANISOU 2550 O LEU A 258 11115 7376 7597 -894 741 -143 O ATOM 2551 CB LEU A 258 57.396 67.754 132.774 1.00 65.85 C ANISOU 2551 CB LEU A 258 10792 6980 7245 -612 800 -116 C ATOM 2552 CG LEU A 258 57.372 67.771 131.236 1.00 65.12 C ANISOU 2552 CG LEU A 258 10630 6958 7153 -665 806 -27 C ATOM 2553 CD1 LEU A 258 58.456 66.880 130.655 1.00 64.74 C ANISOU 2553 CD1 LEU A 258 10480 7075 7043 -707 779 -62 C ATOM 2554 CD2 LEU A 258 56.009 67.365 130.712 1.00 64.18 C ANISOU 2554 CD2 LEU A 258 10511 6819 7052 -583 836 44 C ATOM 2555 N PHE A 259 58.328 70.555 133.193 1.00 69.71 N ANISOU 2555 N PHE A 259 11400 7271 7816 -780 777 -112 N ATOM 2556 CA PHE A 259 58.565 71.886 132.618 1.00 71.75 C ANISOU 2556 CA PHE A 259 11688 7449 8122 -880 766 -51 C ATOM 2557 C PHE A 259 59.759 72.598 133.256 1.00 74.63 C ANISOU 2557 C PHE A 259 12079 7789 8487 -974 729 -115 C ATOM 2558 O PHE A 259 60.532 73.254 132.554 1.00 75.06 O ANISOU 2558 O PHE A 259 12105 7864 8547 -1094 707 -74 O ATOM 2559 CB PHE A 259 57.311 72.763 132.714 1.00 71.32 C ANISOU 2559 CB PHE A 259 11725 7237 8136 -824 786 3 C ATOM 2560 CG PHE A 259 56.104 72.184 132.024 1.00 70.19 C ANISOU 2560 CG PHE A 259 11557 7115 7997 -741 821 75 C ATOM 2561 CD1 PHE A 259 56.172 71.761 130.699 1.00 69.88 C ANISOU 2561 CD1 PHE A 259 11433 7181 7937 -782 827 151 C ATOM 2562 CD2 PHE A 259 54.888 72.073 132.693 1.00 69.87 C ANISOU 2562 CD2 PHE A 259 11574 6995 7977 -622 848 68 C ATOM 2563 CE1 PHE A 259 55.060 71.226 130.062 1.00 69.18 C ANISOU 2563 CE1 PHE A 259 11321 7112 7852 -707 857 216 C ATOM 2564 CE2 PHE A 259 53.772 71.541 132.059 1.00 69.27 C ANISOU 2564 CE2 PHE A 259 11473 6942 7905 -549 879 136 C ATOM 2565 CZ PHE A 259 53.859 71.117 130.742 1.00 68.91 C ANISOU 2565 CZ PHE A 259 11345 6994 7841 -592 883 210 C ATOM 2566 N CYS A 260 59.898 72.463 134.577 1.00 77.85 N ANISOU 2566 N CYS A 260 12537 8157 8886 -922 721 -214 N ATOM 2567 CA CYS A 260 61.021 73.032 135.329 1.00 80.91 C ANISOU 2567 CA CYS A 260 12949 8524 9268 -1000 684 -289 C ATOM 2568 C CYS A 260 61.848 71.934 136.035 1.00 81.62 C ANISOU 2568 C CYS A 260 12985 8738 9288 -976 671 -387 C ATOM 2569 O CYS A 260 61.660 71.681 137.228 1.00 81.36 O ANISOU 2569 O CYS A 260 13001 8666 9245 -901 671 -466 O ATOM 2570 CB CYS A 260 60.501 74.064 136.337 1.00 82.55 C ANISOU 2570 CB CYS A 260 13276 8557 9531 -965 678 -324 C ATOM 2571 SG CYS A 260 61.816 74.981 137.159 1.00 86.15 S ANISOU 2571 SG CYS A 260 13773 8963 9993 -1073 626 -406 S ATOM 2572 N PRO A 261 62.764 71.265 135.297 1.00 83.05 N ANISOU 2572 N PRO A 261 13063 9074 9417 -1036 658 -384 N ATOM 2573 CA PRO A 261 63.687 70.322 135.957 1.00 83.58 C ANISOU 2573 CA PRO A 261 13079 9255 9420 -1022 637 -482 C ATOM 2574 C PRO A 261 64.709 71.011 136.880 1.00 85.59 C ANISOU 2574 C PRO A 261 13370 9476 9673 -1094 603 -561 C ATOM 2575 O PRO A 261 65.251 70.369 137.787 1.00 85.64 O ANISOU 2575 O PRO A 261 13367 9535 9636 -1058 586 -653 O ATOM 2576 CB PRO A 261 64.385 69.629 134.782 1.00 82.99 C ANISOU 2576 CB PRO A 261 12886 9350 9297 -1075 629 -451 C ATOM 2577 CG PRO A 261 64.314 70.614 133.668 1.00 83.48 C ANISOU 2577 CG PRO A 261 12940 9381 9395 -1171 635 -350 C ATOM 2578 CD PRO A 261 63.022 71.360 133.846 1.00 83.31 C ANISOU 2578 CD PRO A 261 13020 9190 9445 -1118 660 -295 C ATOM 2579 N SER A 262 64.961 72.299 136.640 1.00 87.95 N ANISOU 2579 N SER A 262 13711 9686 10019 -1194 588 -523 N ATOM 2580 CA SER A 262 65.818 73.122 137.499 1.00 89.61 C ANISOU 2580 CA SER A 262 13968 9838 10239 -1267 552 -591 C ATOM 2581 C SER A 262 65.212 73.401 138.889 1.00 89.90 C ANISOU 2581 C SER A 262 14112 9742 10302 -1177 554 -664 C ATOM 2582 O SER A 262 65.954 73.557 139.862 1.00 90.60 O ANISOU 2582 O SER A 262 14224 9827 10373 -1198 526 -754 O ATOM 2583 CB SER A 262 66.134 74.447 136.791 1.00 90.97 C ANISOU 2583 CB SER A 262 14163 9937 10463 -1401 531 -517 C ATOM 2584 OG SER A 262 67.138 75.173 137.474 1.00 92.83 O ANISOU 2584 OG SER A 262 14427 10140 10702 -1492 489 -579 O ATOM 2585 N CYS A 263 63.881 73.472 138.971 1.00 89.61 N ANISOU 2585 N CYS A 263 14135 9608 10303 -1076 587 -627 N ATOM 2586 CA CYS A 263 63.166 73.748 140.229 1.00 90.07 C ANISOU 2586 CA CYS A 263 14290 9550 10382 -980 593 -691 C ATOM 2587 C CYS A 263 63.400 72.684 141.308 1.00 90.67 C ANISOU 2587 C CYS A 263 14348 9707 10395 -900 594 -787 C ATOM 2588 O CYS A 263 63.323 71.486 141.029 1.00 89.73 O ANISOU 2588 O CYS A 263 14160 9704 10230 -851 609 -778 O ATOM 2589 CB CYS A 263 61.653 73.853 139.983 1.00 88.97 C ANISOU 2589 CB CYS A 263 14197 9322 10282 -880 633 -625 C ATOM 2590 SG CYS A 263 61.108 75.300 139.042 1.00 89.73 S ANISOU 2590 SG CYS A 263 14351 9273 10466 -944 628 -523 S ATOM 2591 N HIS A 264 63.681 73.144 142.530 1.00 92.70 N ANISOU 2591 N HIS A 264 14671 9899 10652 -888 573 -877 N ATOM 2592 CA HIS A 264 63.743 72.289 143.715 1.00 92.87 C ANISOU 2592 CA HIS A 264 14693 9973 10618 -802 574 -966 C ATOM 2593 C HIS A 264 62.361 72.259 144.367 1.00 92.00 C ANISOU 2593 C HIS A 264 14651 9781 10523 -673 608 -965 C ATOM 2594 O HIS A 264 61.685 73.291 144.446 1.00 91.42 O ANISOU 2594 O HIS A 264 14654 9576 10505 -659 615 -947 O ATOM 2595 CB HIS A 264 64.770 72.826 144.721 1.00 94.86 C ANISOU 2595 CB HIS A 264 14979 10206 10857 -857 533 -1067 C ATOM 2596 CG HIS A 264 66.164 72.931 144.180 1.00 96.86 C ANISOU 2596 CG HIS A 264 15165 10544 11092 -989 497 -1074 C ATOM 2597 ND1 HIS A 264 66.970 71.831 143.977 1.00 97.16 N ANISOU 2597 ND1 HIS A 264 15108 10742 11066 -1001 488 -1096 N ATOM 2598 CD2 HIS A 264 66.901 74.009 143.816 1.00 98.44 C ANISOU 2598 CD2 HIS A 264 15379 10695 11328 -1115 465 -1063 C ATOM 2599 CE1 HIS A 264 68.140 72.225 143.503 1.00 97.84 C ANISOU 2599 CE1 HIS A 264 15145 10882 11144 -1126 456 -1099 C ATOM 2600 NE2 HIS A 264 68.124 73.542 143.396 1.00 98.67 N ANISOU 2600 NE2 HIS A 264 15315 10865 11310 -1202 441 -1075 N ATOM 2601 N LYS A 265 61.945 71.075 144.821 1.00 91.61 N ANISOU 2601 N LYS A 265 14571 9811 10423 -579 627 -982 N ATOM 2602 CA LYS A 265 60.679 70.903 145.541 1.00 91.18 C ANISOU 2602 CA LYS A 265 14569 9706 10369 -455 660 -983 C ATOM 2603 C LYS A 265 60.875 70.035 146.784 1.00 89.46 C ANISOU 2603 C LYS A 265 14347 9556 10085 -389 653 -1065 C ATOM 2604 O LYS A 265 61.209 68.859 146.648 1.00 88.10 O ANISOU 2604 O LYS A 265 14108 9498 9866 -379 647 -1062 O ATOM 2605 CB LYS A 265 59.619 70.294 144.620 1.00 91.26 C ANISOU 2605 CB LYS A 265 14543 9740 10390 -402 698 -884 C ATOM 2606 CG LYS A 265 58.912 71.337 143.763 1.00 92.49 C ANISOU 2606 CG LYS A 265 14737 9789 10616 -421 715 -807 C ATOM 2607 CD LYS A 265 57.830 72.076 144.547 1.00 92.52 C ANISOU 2607 CD LYS A 265 14828 9676 10649 -333 735 -825 C ATOM 2608 CE LYS A 265 57.655 73.519 144.101 1.00 93.16 C ANISOU 2608 CE LYS A 265 14973 9618 10803 -379 725 -796 C ATOM 2609 NZ LYS A 265 56.424 74.108 144.701 1.00 93.51 N ANISOU 2609 NZ LYS A 265 15092 9560 10875 -272 748 -804 N ATOM 2610 N PRO A 266 60.672 70.612 147.994 1.00 88.91 N ANISOU 2610 N PRO A 266 14350 9419 10012 -343 650 -1139 N ATOM 2611 CA PRO A 266 60.860 69.890 149.263 1.00 87.76 C ANISOU 2611 CA PRO A 266 14207 9337 9801 -283 642 -1218 C ATOM 2612 C PRO A 266 60.204 68.510 149.335 1.00 85.12 C ANISOU 2612 C PRO A 266 13826 9096 9420 -200 663 -1179 C ATOM 2613 O PRO A 266 59.117 68.304 148.785 1.00 83.87 O ANISOU 2613 O PRO A 266 13663 8921 9282 -149 698 -1101 O ATOM 2614 CB PRO A 266 60.219 70.826 150.291 1.00 88.82 C ANISOU 2614 CB PRO A 266 14430 9368 9949 -222 652 -1273 C ATOM 2615 CG PRO A 266 60.441 72.182 149.734 1.00 89.96 C ANISOU 2615 CG PRO A 266 14620 9396 10163 -296 636 -1264 C ATOM 2616 CD PRO A 266 60.361 72.037 148.238 1.00 89.74 C ANISOU 2616 CD PRO A 266 14541 9384 10173 -352 647 -1159 C ATOM 2617 N SER A 267 60.878 67.591 150.022 1.00 83.39 N ANISOU 2617 N SER A 267 13573 8970 9139 -191 638 -1232 N ATOM 2618 CA SER A 267 60.446 66.199 150.103 1.00 81.55 C ANISOU 2618 CA SER A 267 13294 8829 8862 -126 644 -1198 C ATOM 2619 C SER A 267 59.107 66.023 150.824 1.00 80.99 C ANISOU 2619 C SER A 267 13262 8734 8775 -21 680 -1176 C ATOM 2620 O SER A 267 58.331 65.153 150.454 1.00 80.29 O ANISOU 2620 O SER A 267 13141 8686 8678 26 697 -1106 O ATOM 2621 CB SER A 267 61.514 65.337 150.786 1.00 80.89 C ANISOU 2621 CB SER A 267 13175 8841 8716 -139 601 -1267 C ATOM 2622 OG SER A 267 62.773 65.470 150.155 1.00 80.76 O ANISOU 2622 OG SER A 267 13115 8862 8706 -233 568 -1292 O ATOM 2623 N ILE A 268 58.829 66.851 151.838 1.00 81.57 N ANISOU 2623 N ILE A 268 13401 8747 8845 14 690 -1235 N ATOM 2624 CA ILE A 268 57.570 66.745 152.593 1.00 81.57 C ANISOU 2624 CA ILE A 268 13433 8737 8822 117 726 -1221 C ATOM 2625 C ILE A 268 56.363 66.982 151.680 1.00 80.92 C ANISOU 2625 C ILE A 268 13351 8605 8787 150 767 -1127 C ATOM 2626 O ILE A 268 55.365 66.255 151.765 1.00 80.31 O ANISOU 2626 O ILE A 268 13256 8570 8688 219 793 -1070 O ATOM 2627 CB ILE A 268 57.546 67.686 153.836 1.00 83.09 C ANISOU 2627 CB ILE A 268 13695 8877 8998 152 726 -1314 C ATOM 2628 CG1 ILE A 268 56.431 67.299 154.825 1.00 83.58 C ANISOU 2628 CG1 ILE A 268 13772 8975 9009 261 757 -1312 C ATOM 2629 CG2 ILE A 268 57.422 69.152 153.441 1.00 83.87 C ANISOU 2629 CG2 ILE A 268 13850 8849 9166 125 732 -1328 C ATOM 2630 CD1 ILE A 268 56.695 66.026 155.606 1.00 83.24 C ANISOU 2630 CD1 ILE A 268 13690 9046 8888 285 740 -1323 C ATOM 2631 N LEU A 269 56.479 67.961 150.783 1.00 80.94 N ANISOU 2631 N LEU A 269 13372 8524 8856 96 769 -1105 N ATOM 2632 CA LEU A 269 55.418 68.267 149.820 1.00 80.78 C ANISOU 2632 CA LEU A 269 13353 8453 8886 120 804 -1014 C ATOM 2633 C LEU A 269 55.212 67.107 148.842 1.00 79.90 C ANISOU 2633 C LEU A 269 13169 8420 8769 112 810 -926 C ATOM 2634 O LEU A 269 54.073 66.799 148.480 1.00 79.48 O ANISOU 2634 O LEU A 269 13105 8370 8724 169 842 -853 O ATOM 2635 CB LEU A 269 55.707 69.573 149.062 1.00 81.84 C ANISOU 2635 CB LEU A 269 13523 8479 9092 53 797 -1007 C ATOM 2636 CG LEU A 269 55.571 70.894 149.844 1.00 82.91 C ANISOU 2636 CG LEU A 269 13743 8504 9254 76 792 -1078 C ATOM 2637 CD1 LEU A 269 56.028 72.083 149.008 1.00 83.55 C ANISOU 2637 CD1 LEU A 269 13857 8479 9409 -9 771 -1064 C ATOM 2638 CD2 LEU A 269 54.148 71.106 150.340 1.00 83.04 C ANISOU 2638 CD2 LEU A 269 13795 8488 9267 193 832 -1065 C ATOM 2639 N THR A 270 56.307 66.460 148.431 1.00 79.79 N ANISOU 2639 N THR A 270 13102 8473 8738 43 775 -937 N ATOM 2640 CA THR A 270 56.239 65.238 147.616 1.00 78.68 C ANISOU 2640 CA THR A 270 12892 8417 8584 41 769 -872 C ATOM 2641 C THR A 270 55.567 64.095 148.381 1.00 78.98 C ANISOU 2641 C THR A 270 12917 8521 8569 121 773 -861 C ATOM 2642 O THR A 270 54.724 63.390 147.827 1.00 78.60 O ANISOU 2642 O THR A 270 12838 8501 8525 157 789 -783 O ATOM 2643 CB THR A 270 57.645 64.777 147.165 1.00 77.68 C ANISOU 2643 CB THR A 270 12712 8359 8442 -39 724 -905 C ATOM 2644 OG1 THR A 270 58.269 65.817 146.401 1.00 77.42 O ANISOU 2644 OG1 THR A 270 12684 8276 8454 -124 719 -905 O ATOM 2645 CG2 THR A 270 57.572 63.501 146.323 1.00 76.68 C ANISOU 2645 CG2 THR A 270 12515 8319 8301 -33 712 -848 C ATOM 2646 N TYR A 271 55.946 63.930 149.649 1.00 80.41 N ANISOU 2646 N TYR A 271 13121 8728 8701 145 757 -935 N ATOM 2647 CA TYR A 271 55.456 62.835 150.489 1.00 80.99 C ANISOU 2647 CA TYR A 271 13183 8871 8718 211 753 -926 C ATOM 2648 C TYR A 271 53.974 62.982 150.866 1.00 79.45 C ANISOU 2648 C TYR A 271 13014 8654 8520 292 800 -876 C ATOM 2649 O TYR A 271 53.230 62.002 150.781 1.00 78.64 O ANISOU 2649 O TYR A 271 12880 8603 8396 332 805 -810 O ATOM 2650 CB TYR A 271 56.335 62.651 151.744 1.00 83.87 C ANISOU 2650 CB TYR A 271 13562 9275 9026 209 720 -1019 C ATOM 2651 CG TYR A 271 57.495 61.680 151.567 1.00 86.69 C ANISOU 2651 CG TYR A 271 13871 9709 9358 164 667 -1045 C ATOM 2652 CD1 TYR A 271 57.268 60.308 151.524 1.00 88.77 C ANISOU 2652 CD1 TYR A 271 14094 10044 9590 195 644 -1000 C ATOM 2653 CD2 TYR A 271 58.817 62.127 151.460 1.00 88.94 C ANISOU 2653 CD2 TYR A 271 14149 9995 9648 93 635 -1115 C ATOM 2654 CE1 TYR A 271 58.315 59.405 151.376 1.00 91.11 C ANISOU 2654 CE1 TYR A 271 14347 10408 9863 164 589 -1028 C ATOM 2655 CE2 TYR A 271 59.874 61.234 151.305 1.00 90.90 C ANISOU 2655 CE2 TYR A 271 14347 10321 9868 60 586 -1143 C ATOM 2656 CZ TYR A 271 59.619 59.871 151.251 1.00 93.44 C ANISOU 2656 CZ TYR A 271 14631 10710 10161 99 562 -1102 C ATOM 2657 OH TYR A 271 60.654 58.956 151.126 1.00100.76 O ANISOU 2657 OH TYR A 271 15510 11712 11060 77 506 -1135 O ATOM 2658 N ILE A 272 53.544 64.183 151.268 1.00 78.96 N ANISOU 2658 N ILE A 272 13005 8517 8477 318 830 -908 N ATOM 2659 CA ILE A 272 52.110 64.406 151.579 1.00 78.26 C ANISOU 2659 CA ILE A 272 12937 8413 8384 401 876 -864 C ATOM 2660 C ILE A 272 51.204 64.246 150.349 1.00 76.43 C ANISOU 2660 C ILE A 272 12676 8165 8198 408 903 -759 C ATOM 2661 O ILE A 272 50.075 63.751 150.462 1.00 75.54 O ANISOU 2661 O ILE A 272 12547 8087 8066 469 930 -698 O ATOM 2662 CB ILE A 272 51.821 65.767 152.280 1.00 79.46 C ANISOU 2662 CB ILE A 272 13156 8486 8549 439 898 -930 C ATOM 2663 CG1 ILE A 272 52.075 66.960 151.347 1.00 80.26 C ANISOU 2663 CG1 ILE A 272 13287 8480 8728 389 899 -929 C ATOM 2664 CG2 ILE A 272 52.597 65.877 153.594 1.00 80.04 C ANISOU 2664 CG2 ILE A 272 13258 8584 8569 443 874 -1035 C ATOM 2665 CD1 ILE A 272 52.000 68.308 152.036 1.00 81.93 C ANISOU 2665 CD1 ILE A 272 13571 8601 8957 418 904 -1007 C ATOM 2666 N ALA A 273 51.706 64.663 149.187 1.00 75.38 N ANISOU 2666 N ALA A 273 12532 7987 8121 342 893 -737 N ATOM 2667 CA ALA A 273 51.019 64.442 147.910 1.00 73.99 C ANISOU 2667 CA ALA A 273 12321 7804 7986 337 912 -639 C ATOM 2668 C ALA A 273 50.798 62.954 147.655 1.00 72.29 C ANISOU 2668 C ALA A 273 12046 7680 7738 347 897 -582 C ATOM 2669 O ALA A 273 49.702 62.546 147.275 1.00 72.63 O ANISOU 2669 O ALA A 273 12069 7739 7787 390 921 -504 O ATOM 2670 CB ALA A 273 51.802 65.062 146.758 1.00 73.84 C ANISOU 2670 CB ALA A 273 12294 7739 8022 254 897 -631 C ATOM 2671 N ILE A 274 51.840 62.156 147.884 1.00 70.74 N ANISOU 2671 N ILE A 274 11824 7542 7509 309 852 -624 N ATOM 2672 CA ILE A 274 51.772 60.700 147.711 1.00 68.96 C ANISOU 2672 CA ILE A 274 11549 7398 7255 318 823 -581 C ATOM 2673 C ILE A 274 50.892 60.040 148.780 1.00 67.66 C ANISOU 2673 C ILE A 274 11392 7276 7039 386 833 -561 C ATOM 2674 O ILE A 274 50.133 59.115 148.468 1.00 66.76 O ANISOU 2674 O ILE A 274 11245 7201 6917 410 831 -486 O ATOM 2675 CB ILE A 274 53.191 60.082 147.662 1.00 69.00 C ANISOU 2675 CB ILE A 274 11525 7452 7240 262 767 -638 C ATOM 2676 CG1 ILE A 274 53.886 60.526 146.364 1.00 69.17 C ANISOU 2676 CG1 ILE A 274 11518 7454 7306 194 759 -632 C ATOM 2677 CG2 ILE A 274 53.148 58.554 147.729 1.00 68.64 C ANISOU 2677 CG2 ILE A 274 11438 7482 7159 282 726 -608 C ATOM 2678 CD1 ILE A 274 55.389 60.390 146.383 1.00 69.40 C ANISOU 2678 CD1 ILE A 274 11527 7522 7320 133 713 -707 C ATOM 2679 N PHE A 275 50.984 60.510 150.025 1.00 67.25 N ANISOU 2679 N PHE A 275 11381 7220 6951 415 842 -626 N ATOM 2680 CA PHE A 275 50.082 60.043 151.082 1.00 66.76 C ANISOU 2680 CA PHE A 275 11325 7205 6835 480 858 -605 C ATOM 2681 C PHE A 275 48.618 60.374 150.788 1.00 65.58 C ANISOU 2681 C PHE A 275 11176 7038 6703 534 910 -530 C ATOM 2682 O PHE A 275 47.737 59.567 151.096 1.00 64.96 O ANISOU 2682 O PHE A 275 11074 7017 6590 573 917 -467 O ATOM 2683 CB PHE A 275 50.470 60.609 152.462 1.00 68.08 C ANISOU 2683 CB PHE A 275 11536 7376 6956 504 860 -697 C ATOM 2684 CG PHE A 275 51.736 60.022 153.046 1.00 68.78 C ANISOU 2684 CG PHE A 275 11618 7506 7006 466 806 -763 C ATOM 2685 CD1 PHE A 275 51.957 58.639 153.065 1.00 68.75 C ANISOU 2685 CD1 PHE A 275 11577 7573 6973 457 762 -727 C ATOM 2686 CD2 PHE A 275 52.696 60.855 153.620 1.00 69.61 C ANISOU 2686 CD2 PHE A 275 11759 7581 7106 442 795 -864 C ATOM 2687 CE1 PHE A 275 53.119 58.113 153.610 1.00 68.89 C ANISOU 2687 CE1 PHE A 275 11590 7629 6956 428 710 -791 C ATOM 2688 CE2 PHE A 275 53.856 60.331 154.170 1.00 69.76 C ANISOU 2688 CE2 PHE A 275 11770 7644 7088 409 746 -926 C ATOM 2689 CZ PHE A 275 54.066 58.960 154.168 1.00 69.36 C ANISOU 2689 CZ PHE A 275 11680 7665 7008 405 704 -890 C ATOM 2690 N LEU A 276 48.363 61.549 150.203 1.00 64.80 N ANISOU 2690 N LEU A 276 11102 6862 6656 535 944 -534 N ATOM 2691 CA LEU A 276 46.998 61.936 149.804 1.00 64.27 C ANISOU 2691 CA LEU A 276 11034 6774 6612 588 992 -463 C ATOM 2692 C LEU A 276 46.371 60.986 148.773 1.00 63.13 C ANISOU 2692 C LEU A 276 10836 6664 6485 579 989 -359 C ATOM 2693 O LEU A 276 45.191 60.633 148.893 1.00 63.24 O ANISOU 2693 O LEU A 276 10831 6715 6481 629 1016 -292 O ATOM 2694 CB LEU A 276 46.970 63.370 149.258 1.00 64.72 C ANISOU 2694 CB LEU A 276 11130 6731 6729 584 1017 -486 C ATOM 2695 CG LEU A 276 46.792 64.493 150.276 1.00 65.53 C ANISOU 2695 CG LEU A 276 11290 6789 6819 636 1039 -564 C ATOM 2696 CD1 LEU A 276 47.241 65.830 149.707 1.00 65.80 C ANISOU 2696 CD1 LEU A 276 11369 6710 6919 604 1038 -602 C ATOM 2697 CD2 LEU A 276 45.337 64.565 150.716 1.00 65.84 C ANISOU 2697 CD2 LEU A 276 11325 6857 6831 728 1084 -522 C ATOM 2698 N THR A 277 47.165 60.575 147.782 1.00 61.96 N ANISOU 2698 N THR A 277 10661 6512 6369 515 955 -348 N ATOM 2699 CA THR A 277 46.687 59.712 146.698 1.00 60.99 C ANISOU 2699 CA THR A 277 10488 6416 6267 502 945 -259 C ATOM 2700 C THR A 277 46.342 58.312 147.184 1.00 60.38 C ANISOU 2700 C THR A 277 10381 6418 6143 519 917 -218 C ATOM 2701 O THR A 277 45.292 57.776 146.829 1.00 60.40 O ANISOU 2701 O THR A 277 10355 6446 6146 545 929 -134 O ATOM 2702 CB THR A 277 47.717 59.570 145.559 1.00 60.74 C ANISOU 2702 CB THR A 277 10431 6374 6273 432 910 -268 C ATOM 2703 OG1 THR A 277 48.953 59.067 146.074 1.00 60.61 O ANISOU 2703 OG1 THR A 277 10413 6390 6226 397 862 -339 O ATOM 2704 CG2 THR A 277 47.953 60.897 144.880 1.00 61.33 C ANISOU 2704 CG2 THR A 277 10530 6372 6400 404 936 -283 C ATOM 2705 N HIS A 278 47.233 57.724 147.983 1.00 60.10 N ANISOU 2705 N HIS A 278 10349 6418 6066 503 874 -275 N ATOM 2706 CA HIS A 278 46.961 56.426 148.613 1.00 59.62 C ANISOU 2706 CA HIS A 278 10267 6427 5957 518 839 -239 C ATOM 2707 C HIS A 278 45.826 56.546 149.630 1.00 59.70 C ANISOU 2707 C HIS A 278 10290 6470 5923 577 879 -208 C ATOM 2708 O HIS A 278 44.971 55.659 149.719 1.00 59.41 O ANISOU 2708 O HIS A 278 10225 6482 5864 594 873 -129 O ATOM 2709 CB HIS A 278 48.213 55.854 149.281 1.00 59.69 C ANISOU 2709 CB HIS A 278 10282 6465 5931 490 782 -311 C ATOM 2710 CG HIS A 278 49.347 55.609 148.333 1.00 59.53 C ANISOU 2710 CG HIS A 278 10240 6433 5944 437 738 -345 C ATOM 2711 ND1 HIS A 278 50.663 55.827 148.679 1.00 59.94 N ANISOU 2711 ND1 HIS A 278 10303 6485 5984 404 708 -436 N ATOM 2712 CD2 HIS A 278 49.360 55.192 147.045 1.00 59.22 C ANISOU 2712 CD2 HIS A 278 10163 6390 5945 412 720 -301 C ATOM 2713 CE1 HIS A 278 51.440 55.537 147.651 1.00 59.72 C ANISOU 2713 CE1 HIS A 278 10244 6460 5986 362 674 -446 C ATOM 2714 NE2 HIS A 278 50.674 55.151 146.645 1.00 59.32 N ANISOU 2714 NE2 HIS A 278 10163 6408 5967 367 680 -367 N ATOM 2715 N GLY A 279 45.827 57.653 150.377 1.00 60.17 N ANISOU 2715 N GLY A 279 10388 6504 5969 606 918 -270 N ATOM 2716 CA GLY A 279 44.759 57.985 151.320 1.00 60.80 C ANISOU 2716 CA GLY A 279 10478 6617 6004 671 963 -255 C ATOM 2717 C GLY A 279 43.379 58.113 150.698 1.00 61.07 C ANISOU 2717 C GLY A 279 10488 6653 6059 707 1008 -165 C ATOM 2718 O GLY A 279 42.382 57.724 151.319 1.00 61.57 O ANISOU 2718 O GLY A 279 10534 6783 6077 749 1028 -113 O ATOM 2719 N ASN A 280 43.315 58.634 149.470 1.00 60.93 N ANISOU 2719 N ASN A 280 10468 6573 6109 689 1021 -142 N ATOM 2720 CA ASN A 280 42.046 58.746 148.727 1.00 60.76 C ANISOU 2720 CA ASN A 280 10420 6550 6114 721 1060 -54 C ATOM 2721 C ASN A 280 41.260 57.422 148.637 1.00 60.86 C ANISOU 2721 C ASN A 280 10384 6639 6100 720 1042 42 C ATOM 2722 O ASN A 280 40.026 57.437 148.616 1.00 60.81 O ANISOU 2722 O ASN A 280 10355 6666 6084 762 1079 110 O ATOM 2723 CB ASN A 280 42.293 59.304 147.321 1.00 60.01 C ANISOU 2723 CB ASN A 280 10324 6381 6094 687 1063 -40 C ATOM 2724 CG ASN A 280 41.013 59.696 146.612 1.00 59.79 C ANISOU 2724 CG ASN A 280 10278 6342 6096 727 1108 37 C ATOM 2725 OD1 ASN A 280 40.641 59.095 145.602 1.00 59.17 O ANISOU 2725 OD1 ASN A 280 10161 6274 6044 705 1098 112 O ATOM 2726 ND2 ASN A 280 40.329 60.702 147.139 1.00 60.31 N ANISOU 2726 ND2 ASN A 280 10371 6387 6155 789 1154 16 N ATOM 2727 N SER A 281 41.973 56.293 148.603 1.00 60.96 N ANISOU 2727 N SER A 281 10380 6679 6101 673 982 48 N ATOM 2728 CA SER A 281 41.335 54.967 148.637 1.00 61.36 C ANISOU 2728 CA SER A 281 10391 6795 6125 665 950 135 C ATOM 2729 C SER A 281 40.580 54.657 149.940 1.00 62.41 C ANISOU 2729 C SER A 281 10520 7007 6186 703 966 162 C ATOM 2730 O SER A 281 39.700 53.790 149.942 1.00 62.68 O ANISOU 2730 O SER A 281 10518 7096 6199 703 957 253 O ATOM 2731 CB SER A 281 42.360 53.859 148.369 1.00 61.23 C ANISOU 2731 CB SER A 281 10365 6783 6115 612 873 123 C ATOM 2732 OG SER A 281 42.944 53.999 147.083 1.00 61.49 O ANISOU 2732 OG SER A 281 10389 6764 6208 577 857 111 O ATOM 2733 N ALA A 282 40.923 55.348 151.033 1.00 63.44 N ANISOU 2733 N ALA A 282 10682 7145 6273 732 988 84 N ATOM 2734 CA ALA A 282 40.230 55.180 152.321 1.00 64.14 C ANISOU 2734 CA ALA A 282 10764 7319 6284 773 1009 101 C ATOM 2735 C ALA A 282 38.962 56.036 152.494 1.00 65.17 C ANISOU 2735 C ALA A 282 10884 7475 6399 840 1082 126 C ATOM 2736 O ALA A 282 38.101 55.693 153.308 1.00 65.35 O ANISOU 2736 O ALA A 282 10882 7590 6358 872 1100 173 O ATOM 2737 CB ALA A 282 41.195 55.457 153.462 1.00 64.38 C ANISOU 2737 CB ALA A 282 10832 7360 6269 776 995 2 C ATOM 2738 N MET A 283 38.836 57.118 151.724 1.00 66.30 N ANISOU 2738 N MET A 283 11046 7544 6601 863 1119 99 N ATOM 2739 CA MET A 283 37.823 58.152 151.991 1.00 67.98 C ANISOU 2739 CA MET A 283 11261 7767 6801 939 1185 93 C ATOM 2740 C MET A 283 36.399 57.710 151.629 1.00 68.77 C ANISOU 2740 C MET A 283 11306 7931 6889 965 1213 206 C ATOM 2741 O MET A 283 35.468 57.840 152.451 1.00 69.43 O ANISOU 2741 O MET A 283 11368 8100 6911 1022 1251 224 O ATOM 2742 CB MET A 283 38.170 59.453 151.244 1.00 68.13 C ANISOU 2742 CB MET A 283 11321 7674 6892 952 1207 32 C ATOM 2743 CG MET A 283 39.550 60.022 151.560 1.00 68.40 C ANISOU 2743 CG MET A 283 11407 7639 6940 923 1181 -78 C ATOM 2744 SD MET A 283 39.895 61.625 150.783 1.00 69.02 S ANISOU 2744 SD MET A 283 11538 7585 7100 933 1203 -143 S ATOM 2745 CE MET A 283 41.642 61.832 151.136 1.00 68.50 C ANISOU 2745 CE MET A 283 11517 7466 7043 870 1155 -253 C ATOM 2746 N ASN A 284 36.243 57.176 150.412 1.00 69.12 N ANISOU 2746 N ASN A 284 11326 7945 6990 922 1193 279 N ATOM 2747 CA ASN A 284 34.925 56.824 149.852 1.00 69.74 C ANISOU 2747 CA ASN A 284 11353 8072 7071 940 1217 386 C ATOM 2748 C ASN A 284 34.020 56.027 150.824 1.00 70.47 C ANISOU 2748 C ASN A 284 11402 8292 7081 956 1223 454 C ATOM 2749 O ASN A 284 32.905 56.489 151.140 1.00 71.41 O ANISOU 2749 O ASN A 284 11493 8471 7165 1018 1276 483 O ATOM 2750 CB ASN A 284 35.068 56.127 148.480 1.00 69.18 C ANISOU 2750 CB ASN A 284 11261 7957 7065 880 1179 451 C ATOM 2751 CG ASN A 284 35.420 57.089 147.353 1.00 69.32 C ANISOU 2751 CG ASN A 284 11303 7874 7160 879 1195 417 C ATOM 2752 OD1 ASN A 284 35.303 58.308 147.480 1.00 69.93 O ANISOU 2752 OD1 ASN A 284 11410 7908 7250 928 1238 364 O ATOM 2753 ND2 ASN A 284 35.851 56.531 146.228 1.00 68.96 N ANISOU 2753 ND2 ASN A 284 11244 7790 7165 823 1156 449 N ATOM 2754 N PRO A 285 34.501 54.868 151.337 1.00 70.38 N ANISOU 2754 N PRO A 285 11382 8324 7033 903 1168 478 N ATOM 2755 CA PRO A 285 33.736 54.143 152.364 1.00 70.63 C ANISOU 2755 CA PRO A 285 11375 8479 6980 910 1169 543 C ATOM 2756 C PRO A 285 33.323 55.001 153.557 1.00 70.92 C ANISOU 2756 C PRO A 285 11416 8585 6945 985 1226 488 C ATOM 2757 O PRO A 285 32.196 54.867 154.030 1.00 70.57 O ANISOU 2757 O PRO A 285 11323 8646 6841 1018 1260 552 O ATOM 2758 CB PRO A 285 34.705 53.052 152.825 1.00 70.66 C ANISOU 2758 CB PRO A 285 11393 8489 6964 845 1095 540 C ATOM 2759 CG PRO A 285 35.585 52.821 151.659 1.00 70.02 C ANISOU 2759 CG PRO A 285 11334 8304 6966 796 1049 520 C ATOM 2760 CD PRO A 285 35.753 54.160 151.006 1.00 70.01 C ANISOU 2760 CD PRO A 285 11359 8221 7019 834 1098 450 C ATOM 2761 N ILE A 286 34.224 55.877 154.017 1.00 71.32 N ANISOU 2761 N ILE A 286 11519 8580 6998 1010 1234 369 N ATOM 2762 CA ILE A 286 33.944 56.731 155.177 1.00 72.53 C ANISOU 2762 CA ILE A 286 11682 8793 7083 1085 1282 298 C ATOM 2763 C ILE A 286 32.882 57.774 154.834 1.00 73.31 C ANISOU 2763 C ILE A 286 11767 8891 7196 1166 1347 298 C ATOM 2764 O ILE A 286 31.940 57.960 155.613 1.00 74.20 O ANISOU 2764 O ILE A 286 11844 9113 7235 1228 1389 313 O ATOM 2765 CB ILE A 286 35.219 57.405 155.748 1.00 72.41 C ANISOU 2765 CB ILE A 286 11730 8711 7071 1089 1267 166 C ATOM 2766 CG1 ILE A 286 36.169 56.335 156.309 1.00 72.14 C ANISOU 2766 CG1 ILE A 286 11703 8703 7004 1021 1204 167 C ATOM 2767 CG2 ILE A 286 34.864 58.404 156.848 1.00 73.19 C ANISOU 2767 CG2 ILE A 286 11841 8862 7105 1177 1316 84 C ATOM 2768 CD1 ILE A 286 37.566 56.829 156.614 1.00 72.14 C ANISOU 2768 CD1 ILE A 286 11761 8626 7021 1005 1177 46 C ATOM 2769 N VAL A 287 33.025 58.441 153.685 1.00 73.19 N ANISOU 2769 N VAL A 287 11777 8761 7270 1167 1354 282 N ATOM 2770 CA VAL A 287 32.019 59.437 153.258 1.00 73.82 C ANISOU 2770 CA VAL A 287 11846 8829 7372 1245 1410 286 C ATOM 2771 C VAL A 287 30.647 58.803 152.950 1.00 73.70 C ANISOU 2771 C VAL A 287 11757 8915 7331 1256 1434 410 C ATOM 2772 O VAL A 287 29.608 59.398 153.288 1.00 74.56 O ANISOU 2772 O VAL A 287 11836 9090 7401 1338 1485 414 O ATOM 2773 CB VAL A 287 32.520 60.366 152.107 1.00 73.65 C ANISOU 2773 CB VAL A 287 11872 8658 7453 1241 1409 242 C ATOM 2774 CG1 VAL A 287 32.818 59.608 150.825 1.00 72.62 C ANISOU 2774 CG1 VAL A 287 11728 8474 7391 1159 1372 318 C ATOM 2775 CG2 VAL A 287 31.522 61.481 151.830 1.00 74.53 C ANISOU 2775 CG2 VAL A 287 11981 8753 7583 1332 1463 235 C ATOM 2776 N TYR A 288 30.637 57.602 152.356 1.00 72.96 N ANISOU 2776 N TYR A 288 11630 8836 7254 1177 1393 507 N ATOM 2777 CA TYR A 288 29.371 56.867 152.166 1.00 73.41 C ANISOU 2777 CA TYR A 288 11615 8998 7280 1174 1406 631 C ATOM 2778 C TYR A 288 28.656 56.630 153.501 1.00 74.90 C ANISOU 2778 C TYR A 288 11760 9340 7356 1213 1433 650 C ATOM 2779 O TYR A 288 27.447 56.847 153.607 1.00 75.45 O ANISOU 2779 O TYR A 288 11776 9502 7387 1268 1480 700 O ATOM 2780 CB TYR A 288 29.573 55.506 151.477 1.00 72.42 C ANISOU 2780 CB TYR A 288 11466 8864 7183 1077 1345 725 C ATOM 2781 CG TYR A 288 30.137 55.532 150.068 1.00 71.34 C ANISOU 2781 CG TYR A 288 11355 8603 7147 1033 1316 725 C ATOM 2782 CD1 TYR A 288 29.722 56.476 149.129 1.00 71.48 C ANISOU 2782 CD1 TYR A 288 11377 8556 7223 1076 1355 718 C ATOM 2783 CD2 TYR A 288 31.072 54.580 149.664 1.00 70.68 C ANISOU 2783 CD2 TYR A 288 11287 8472 7096 951 1247 736 C ATOM 2784 CE1 TYR A 288 30.240 56.483 147.842 1.00 70.69 C ANISOU 2784 CE1 TYR A 288 11294 8354 7208 1033 1329 723 C ATOM 2785 CE2 TYR A 288 31.596 54.583 148.381 1.00 70.18 C ANISOU 2785 CE2 TYR A 288 11239 8308 7115 914 1221 733 C ATOM 2786 CZ TYR A 288 31.177 55.532 147.475 1.00 70.09 C ANISOU 2786 CZ TYR A 288 11230 8242 7158 952 1263 729 C ATOM 2787 OH TYR A 288 31.699 55.528 146.204 1.00 69.84 O ANISOU 2787 OH TYR A 288 11210 8124 7202 912 1237 731 O ATOM 2788 N ALA A 289 29.409 56.190 154.508 1.00 75.80 N ANISOU 2788 N ALA A 289 11893 9488 7416 1184 1403 612 N ATOM 2789 CA ALA A 289 28.859 55.906 155.838 1.00 77.14 C ANISOU 2789 CA ALA A 289 12023 9813 7473 1212 1423 630 C ATOM 2790 C ALA A 289 28.268 57.146 156.494 1.00 79.04 C ANISOU 2790 C ALA A 289 12259 10104 7665 1326 1491 551 C ATOM 2791 O ALA A 289 27.173 57.091 157.051 1.00 79.94 O ANISOU 2791 O ALA A 289 12311 10360 7702 1372 1531 601 O ATOM 2792 CB ALA A 289 29.929 55.303 156.735 1.00 77.02 C ANISOU 2792 CB ALA A 289 12039 9806 7416 1162 1373 591 C ATOM 2793 N PHE A 290 28.994 58.259 156.418 1.00 80.60 N ANISOU 2793 N PHE A 290 12523 10189 7909 1372 1501 427 N ATOM 2794 CA PHE A 290 28.522 59.531 156.976 1.00 82.80 C ANISOU 2794 CA PHE A 290 12810 10492 8155 1487 1557 336 C ATOM 2795 C PHE A 290 27.334 60.111 156.203 1.00 84.27 C ANISOU 2795 C PHE A 290 12960 10684 8372 1553 1603 379 C ATOM 2796 O PHE A 290 26.344 60.504 156.823 1.00 85.60 O ANISOU 2796 O PHE A 290 13083 10971 8469 1638 1651 376 O ATOM 2797 CB PHE A 290 29.660 60.562 157.039 1.00 83.21 C ANISOU 2797 CB PHE A 290 12949 10405 8259 1509 1545 194 C ATOM 2798 CG PHE A 290 30.486 60.476 158.293 1.00 84.09 C ANISOU 2798 CG PHE A 290 13088 10559 8302 1505 1526 113 C ATOM 2799 CD1 PHE A 290 31.266 59.356 158.563 1.00 83.83 C ANISOU 2799 CD1 PHE A 290 13056 10545 8250 1411 1475 150 C ATOM 2800 CD2 PHE A 290 30.481 61.523 159.215 1.00 85.65 C ANISOU 2800 CD2 PHE A 290 13312 10778 8452 1599 1556 -5 C ATOM 2801 CE1 PHE A 290 32.020 59.279 159.724 1.00 84.58 C ANISOU 2801 CE1 PHE A 290 13175 10682 8279 1408 1456 77 C ATOM 2802 CE2 PHE A 290 31.239 61.454 160.376 1.00 86.02 C ANISOU 2802 CE2 PHE A 290 13382 10869 8432 1596 1538 -83 C ATOM 2803 CZ PHE A 290 32.009 60.330 160.631 1.00 85.60 C ANISOU 2803 CZ PHE A 290 13327 10837 8359 1499 1490 -39 C ATOM 2804 N ARG A 291 27.419 60.152 154.870 1.00 85.06 N ANISOU 2804 N ARG A 291 13077 10668 8573 1515 1588 419 N ATOM 2805 CA ARG A 291 26.397 60.848 154.062 1.00 86.41 C ANISOU 2805 CA ARG A 291 13223 10822 8783 1582 1629 448 C ATOM 2806 C ARG A 291 25.246 59.972 153.549 1.00 86.46 C ANISOU 2806 C ARG A 291 13146 10932 8772 1556 1640 591 C ATOM 2807 O ARG A 291 24.080 60.354 153.681 1.00 87.35 O ANISOU 2807 O ARG A 291 13205 11138 8843 1635 1687 617 O ATOM 2808 CB ARG A 291 27.056 61.578 152.894 1.00 86.91 C ANISOU 2808 CB ARG A 291 13352 10704 8964 1568 1613 407 C ATOM 2809 CG ARG A 291 27.947 62.727 153.336 1.00 88.06 C ANISOU 2809 CG ARG A 291 13578 10746 9132 1612 1610 265 C ATOM 2810 CD ARG A 291 28.386 63.579 152.153 1.00 88.49 C ANISOU 2810 CD ARG A 291 13689 10631 9299 1606 1599 236 C ATOM 2811 NE ARG A 291 27.268 64.314 151.555 1.00 89.38 N ANISOU 2811 NE ARG A 291 13780 10740 9439 1688 1638 265 N ATOM 2812 CZ ARG A 291 26.720 65.426 152.055 1.00 90.62 C ANISOU 2812 CZ ARG A 291 13953 10900 9577 1803 1671 190 C ATOM 2813 NH1 ARG A 291 27.159 65.974 153.192 1.00 91.13 N ANISOU 2813 NH1 ARG A 291 14055 10974 9593 1854 1672 76 N ATOM 2814 NH2 ARG A 291 25.703 65.989 151.410 1.00 91.27 N ANISOU 2814 NH2 ARG A 291 14012 10978 9688 1873 1701 226 N ATOM 2815 N ILE A 292 25.566 58.818 152.962 1.00 86.13 N ANISOU 2815 N ILE A 292 13092 10874 8760 1449 1593 680 N ATOM 2816 CA ILE A 292 24.552 57.955 152.335 1.00 86.56 C ANISOU 2816 CA ILE A 292 13072 11005 8811 1411 1593 817 C ATOM 2817 C ILE A 292 23.882 57.044 153.375 1.00 88.62 C ANISOU 2817 C ILE A 292 13263 11444 8961 1393 1596 892 C ATOM 2818 O ILE A 292 24.515 56.142 153.935 1.00 88.03 O ANISOU 2818 O ILE A 292 13197 11394 8856 1320 1551 910 O ATOM 2819 CB ILE A 292 25.122 57.113 151.170 1.00 84.90 C ANISOU 2819 CB ILE A 292 12877 10696 8685 1307 1536 879 C ATOM 2820 CG1 ILE A 292 25.823 58.026 150.151 1.00 84.10 C ANISOU 2820 CG1 ILE A 292 12840 10428 8684 1319 1533 808 C ATOM 2821 CG2 ILE A 292 24.004 56.316 150.495 1.00 84.79 C ANISOU 2821 CG2 ILE A 292 12788 10756 8670 1275 1535 1015 C ATOM 2822 CD1 ILE A 292 26.324 57.331 148.901 1.00 82.95 C ANISOU 2822 CD1 ILE A 292 12703 10193 8620 1230 1483 862 C ATOM 2823 N GLN A 293 22.594 57.304 153.603 1.00 91.38 N ANISOU 2823 N GLN A 293 13543 11920 9254 1461 1648 937 N ATOM 2824 CA GLN A 293 21.742 56.576 154.565 1.00 93.67 C ANISOU 2824 CA GLN A 293 13752 12405 9430 1454 1662 1017 C ATOM 2825 C GLN A 293 21.688 55.044 154.413 1.00 93.13 C ANISOU 2825 C GLN A 293 13647 12385 9353 1329 1606 1150 C ATOM 2826 O GLN A 293 21.715 54.319 155.412 1.00 93.53 O ANISOU 2826 O GLN A 293 13670 12546 9319 1290 1588 1188 O ATOM 2827 CB GLN A 293 20.308 57.142 154.509 1.00 95.95 C ANISOU 2827 CB GLN A 293 13966 12811 9677 1546 1726 1052 C ATOM 2828 CG GLN A 293 19.606 56.977 153.159 1.00 96.41 C ANISOU 2828 CG GLN A 293 13993 12827 9810 1524 1726 1142 C ATOM 2829 CD GLN A 293 18.578 58.052 152.837 1.00 98.11 C ANISOU 2829 CD GLN A 293 14175 13076 10026 1643 1788 1119 C ATOM 2830 OE1 GLN A 293 18.527 59.121 153.456 1.00 99.73 O ANISOU 2830 OE1 GLN A 293 14399 13294 10199 1753 1828 1013 O ATOM 2831 NE2 GLN A 293 17.753 57.768 151.843 1.00 98.01 N ANISOU 2831 NE2 GLN A 293 14113 13074 10052 1624 1791 1216 N ATOM 2832 N LYS A 294 21.605 54.565 153.173 1.00 91.76 N ANISOU 2832 N LYS A 294 13472 12128 9264 1270 1574 1221 N ATOM 2833 CA LYS A 294 21.418 53.135 152.893 1.00 90.51 C ANISOU 2833 CA LYS A 294 13277 12006 9106 1157 1515 1352 C ATOM 2834 C LYS A 294 22.680 52.307 153.150 1.00 88.64 C ANISOU 2834 C LYS A 294 13098 11693 8888 1070 1441 1334 C ATOM 2835 O LYS A 294 22.583 51.126 153.482 1.00 88.10 O ANISOU 2835 O LYS A 294 13001 11688 8784 987 1390 1428 O ATOM 2836 CB LYS A 294 20.941 52.934 151.452 1.00 90.72 C ANISOU 2836 CB LYS A 294 13285 11964 9218 1128 1503 1422 C ATOM 2837 CG LYS A 294 19.539 53.464 151.178 1.00 92.25 C ANISOU 2837 CG LYS A 294 13407 12257 9387 1199 1566 1472 C ATOM 2838 CD LYS A 294 19.358 53.903 149.730 1.00 92.23 C ANISOU 2838 CD LYS A 294 13416 12142 9484 1213 1571 1477 C ATOM 2839 CE LYS A 294 18.003 54.561 149.503 1.00 93.17 C ANISOU 2839 CE LYS A 294 13466 12356 9577 1298 1636 1513 C ATOM 2840 NZ LYS A 294 17.711 54.768 148.055 1.00 92.62 N ANISOU 2840 NZ LYS A 294 13396 12194 9599 1296 1633 1546 N ATOM 2841 N PHE A 295 23.853 52.916 152.979 1.00 87.39 N ANISOU 2841 N PHE A 295 13019 11398 8785 1086 1430 1217 N ATOM 2842 CA PHE A 295 25.129 52.273 153.329 1.00 86.61 C ANISOU 2842 CA PHE A 295 12976 11233 8698 1019 1364 1180 C ATOM 2843 C PHE A 295 25.327 52.196 154.850 1.00 87.21 C ANISOU 2843 C PHE A 295 13049 11417 8670 1033 1371 1149 C ATOM 2844 O PHE A 295 25.818 51.182 155.365 1.00 88.07 O ANISOU 2844 O PHE A 295 13163 11547 8749 959 1312 1189 O ATOM 2845 CB PHE A 295 26.319 53.006 152.682 1.00 85.89 C ANISOU 2845 CB PHE A 295 12965 10975 8695 1032 1354 1063 C ATOM 2846 CG PHE A 295 26.545 52.658 151.230 1.00 84.95 C ANISOU 2846 CG PHE A 295 12857 10742 8675 981 1316 1099 C ATOM 2847 CD1 PHE A 295 26.915 51.365 150.860 1.00 84.66 C ANISOU 2847 CD1 PHE A 295 12819 10683 8664 887 1238 1168 C ATOM 2848 CD2 PHE A 295 26.421 53.622 150.233 1.00 84.25 C ANISOU 2848 CD2 PHE A 295 12785 10569 8657 1027 1352 1061 C ATOM 2849 CE1 PHE A 295 27.134 51.039 149.527 1.00 83.49 C ANISOU 2849 CE1 PHE A 295 12679 10438 8602 846 1201 1193 C ATOM 2850 CE2 PHE A 295 26.644 53.302 148.901 1.00 83.49 C ANISOU 2850 CE2 PHE A 295 12696 10379 8647 980 1317 1093 C ATOM 2851 CZ PHE A 295 26.998 52.007 148.547 1.00 82.95 C ANISOU 2851 CZ PHE A 295 12622 10298 8598 891 1243 1156 C ATOM 2852 N ARG A 296 24.956 53.271 155.551 1.00 87.19 N ANISOU 2852 N ARG A 296 13038 11478 8612 1131 1440 1074 N ATOM 2853 CA ARG A 296 25.028 53.338 157.018 1.00 87.03 C ANISOU 2853 CA ARG A 296 13007 11578 8483 1160 1457 1037 C ATOM 2854 C ARG A 296 24.250 52.204 157.695 1.00 86.29 C ANISOU 2854 C ARG A 296 12838 11649 8298 1102 1439 1170 C ATOM 2855 O ARG A 296 24.776 51.534 158.587 1.00 85.52 O ANISOU 2855 O ARG A 296 12749 11601 8144 1053 1400 1182 O ATOM 2856 CB ARG A 296 24.524 54.705 157.513 1.00 88.75 C ANISOU 2856 CB ARG A 296 13216 11845 8657 1286 1536 942 C ATOM 2857 CG ARG A 296 24.358 54.821 159.023 1.00 90.88 C ANISOU 2857 CG ARG A 296 13458 12271 8801 1330 1564 908 C ATOM 2858 CD ARG A 296 24.372 56.258 159.522 1.00 92.33 C ANISOU 2858 CD ARG A 296 13667 12450 8961 1456 1622 765 C ATOM 2859 NE ARG A 296 25.733 56.745 159.754 1.00 92.87 N ANISOU 2859 NE ARG A 296 13827 12390 9070 1456 1595 637 N ATOM 2860 CZ ARG A 296 26.052 57.894 160.355 1.00 94.27 C ANISOU 2860 CZ ARG A 296 14043 12546 9227 1549 1627 499 C ATOM 2861 NH1 ARG A 296 25.109 58.716 160.816 1.00 95.53 N ANISOU 2861 NH1 ARG A 296 14163 12808 9325 1660 1688 461 N ATOM 2862 NH2 ARG A 296 27.336 58.226 160.504 1.00 94.15 N ANISOU 2862 NH2 ARG A 296 14108 12409 9252 1532 1594 394 N ATOM 2863 N VAL A 297 23.008 52.000 157.263 1.00 85.52 N ANISOU 2863 N VAL A 297 12667 11637 8186 1104 1466 1274 N ATOM 2864 CA VAL A 297 22.145 50.936 157.803 1.00 85.46 C ANISOU 2864 CA VAL A 297 12581 11793 8096 1041 1449 1416 C ATOM 2865 C VAL A 297 22.712 49.535 157.494 1.00 84.24 C ANISOU 2865 C VAL A 297 12449 11576 7983 911 1352 1507 C ATOM 2866 O VAL A 297 22.605 48.624 158.315 1.00 85.37 O ANISOU 2866 O VAL A 297 12562 11822 8052 847 1315 1589 O ATOM 2867 CB VAL A 297 20.676 51.071 157.289 1.00 85.79 C ANISOU 2867 CB VAL A 297 12536 11936 8122 1070 1498 1506 C ATOM 2868 CG1 VAL A 297 19.801 49.885 157.702 1.00 86.23 C ANISOU 2868 CG1 VAL A 297 12509 12150 8102 986 1470 1668 C ATOM 2869 CG2 VAL A 297 20.051 52.373 157.781 1.00 86.90 C ANISOU 2869 CG2 VAL A 297 12649 12165 8205 1205 1588 1419 C ATOM 2870 N THR A 298 23.315 49.377 156.319 1.00 82.44 N ANISOU 2870 N THR A 298 12272 11181 7870 876 1309 1491 N ATOM 2871 CA THR A 298 23.916 48.108 155.910 1.00 81.36 C ANISOU 2871 CA THR A 298 12162 10966 7784 766 1212 1559 C ATOM 2872 C THR A 298 25.207 47.796 156.680 1.00 81.39 C ANISOU 2872 C THR A 298 12229 10922 7773 738 1160 1491 C ATOM 2873 O THR A 298 25.331 46.697 157.246 1.00 82.34 O ANISOU 2873 O THR A 298 12341 11089 7853 660 1095 1571 O ATOM 2874 CB THR A 298 24.196 48.085 154.397 1.00 79.78 C ANISOU 2874 CB THR A 298 11994 10610 7707 747 1183 1550 C ATOM 2875 OG1 THR A 298 23.012 48.461 153.687 1.00 79.37 O ANISOU 2875 OG1 THR A 298 11884 10603 7668 780 1234 1607 O ATOM 2876 CG2 THR A 298 24.634 46.694 153.949 1.00 79.09 C ANISOU 2876 CG2 THR A 298 11924 10459 7667 638 1079 1630 C ATOM 2877 N PHE A 299 26.144 48.753 156.724 1.00 80.88 N ANISOU 2877 N PHE A 299 12226 10766 7738 798 1186 1347 N ATOM 2878 CA PHE A 299 27.432 48.550 157.433 1.00 80.54 C ANISOU 2878 CA PHE A 299 12244 10674 7683 777 1139 1270 C ATOM 2879 C PHE A 299 27.229 48.101 158.891 1.00 82.05 C ANISOU 2879 C PHE A 299 12403 11017 7752 763 1135 1312 C ATOM 2880 O PHE A 299 27.930 47.201 159.378 1.00 82.01 O ANISOU 2880 O PHE A 299 12423 11003 7731 697 1062 1337 O ATOM 2881 CB PHE A 299 28.320 49.811 157.420 1.00 79.67 C ANISOU 2881 CB PHE A 299 12194 10469 7605 852 1180 1109 C ATOM 2882 CG PHE A 299 28.734 50.297 156.043 1.00 78.38 C ANISOU 2882 CG PHE A 299 12070 10151 7559 859 1179 1058 C ATOM 2883 CD1 PHE A 299 28.852 49.435 154.943 1.00 77.43 C ANISOU 2883 CD1 PHE A 299 11951 9950 7516 789 1117 1127 C ATOM 2884 CD2 PHE A 299 29.042 51.644 155.857 1.00 78.08 C ANISOU 2884 CD2 PHE A 299 12067 10046 7551 937 1235 939 C ATOM 2885 CE1 PHE A 299 29.244 49.919 153.698 1.00 76.13 C ANISOU 2885 CE1 PHE A 299 11817 9656 7450 798 1119 1079 C ATOM 2886 CE2 PHE A 299 29.437 52.125 154.613 1.00 76.94 C ANISOU 2886 CE2 PHE A 299 11957 9766 7510 940 1234 898 C ATOM 2887 CZ PHE A 299 29.537 51.262 153.535 1.00 75.86 C ANISOU 2887 CZ PHE A 299 11815 9563 7442 871 1178 969 C ATOM 2888 N LEU A 300 26.271 48.731 159.571 1.00 83.26 N ANISOU 2888 N LEU A 300 12500 11314 7819 827 1212 1319 N ATOM 2889 CA LEU A 300 25.839 48.301 160.905 1.00 84.68 C ANISOU 2889 CA LEU A 300 12632 11671 7872 814 1217 1378 C ATOM 2890 C LEU A 300 25.372 46.846 160.915 1.00 84.66 C ANISOU 2890 C LEU A 300 12588 11728 7849 703 1145 1545 C ATOM 2891 O LEU A 300 25.754 46.083 161.802 1.00 85.20 O ANISOU 2891 O LEU A 300 12660 11852 7857 647 1094 1587 O ATOM 2892 CB LEU A 300 24.709 49.197 161.428 1.00 86.17 C ANISOU 2892 CB LEU A 300 12751 12013 7973 906 1313 1367 C ATOM 2893 CG LEU A 300 25.091 50.628 161.814 1.00 86.87 C ANISOU 2893 CG LEU A 300 12875 12079 8049 1023 1380 1202 C ATOM 2894 CD1 LEU A 300 23.847 51.496 161.948 1.00 87.91 C ANISOU 2894 CD1 LEU A 300 12939 12336 8124 1120 1468 1197 C ATOM 2895 CD2 LEU A 300 25.899 50.643 163.105 1.00 87.33 C ANISOU 2895 CD2 LEU A 300 12963 12191 8028 1030 1367 1131 C ATOM 2896 N LYS A 301 24.556 46.470 159.929 1.00 84.23 N ANISOU 2896 N LYS A 301 12497 11659 7848 669 1138 1641 N ATOM 2897 CA LYS A 301 24.033 45.097 159.838 1.00 84.25 C ANISOU 2897 CA LYS A 301 12460 11708 7841 559 1065 1805 C ATOM 2898 C LYS A 301 25.154 44.084 159.598 1.00 83.75 C ANISOU 2898 C LYS A 301 12466 11509 7844 475 954 1813 C ATOM 2899 O LYS A 301 25.191 43.039 160.248 1.00 84.18 O ANISOU 2899 O LYS A 301 12511 11619 7851 395 885 1908 O ATOM 2900 CB LYS A 301 22.958 44.973 158.753 1.00 83.54 C ANISOU 2900 CB LYS A 301 12318 11619 7801 545 1079 1894 C ATOM 2901 CG LYS A 301 22.174 43.666 158.821 1.00 83.40 C ANISOU 2901 CG LYS A 301 12245 11688 7753 435 1015 2073 C ATOM 2902 CD LYS A 301 20.964 43.678 157.914 1.00 83.00 C ANISOU 2902 CD LYS A 301 12130 11674 7731 431 1045 2159 C ATOM 2903 CE LYS A 301 19.796 44.440 158.519 1.00 83.81 C ANISOU 2903 CE LYS A 301 12143 11968 7730 501 1146 2178 C ATOM 2904 NZ LYS A 301 18.557 44.258 157.719 1.00 83.84 N ANISOU 2904 NZ LYS A 301 12074 12028 7751 481 1163 2285 N ATOM 2905 N ILE A 302 26.067 44.407 158.683 1.00 83.39 N ANISOU 2905 N ILE A 302 12487 11291 7904 495 935 1713 N ATOM 2906 CA ILE A 302 27.226 43.546 158.411 1.00 83.15 C ANISOU 2906 CA ILE A 302 12525 11129 7939 431 831 1698 C ATOM 2907 C ILE A 302 28.117 43.449 159.658 1.00 83.92 C ANISOU 2907 C ILE A 302 12656 11260 7967 431 808 1644 C ATOM 2908 O ILE A 302 28.545 42.346 160.029 1.00 84.10 O ANISOU 2908 O ILE A 302 12698 11273 7981 355 715 1708 O ATOM 2909 CB ILE A 302 28.036 44.032 157.180 1.00 82.09 C ANISOU 2909 CB ILE A 302 12446 10819 7922 461 826 1591 C ATOM 2910 CG1 ILE A 302 27.190 43.904 155.906 1.00 81.90 C ANISOU 2910 CG1 ILE A 302 12389 10760 7968 447 831 1660 C ATOM 2911 CG2 ILE A 302 29.329 43.232 157.018 1.00 81.65 C ANISOU 2911 CG2 ILE A 302 12458 10643 7922 409 724 1555 C ATOM 2912 CD1 ILE A 302 27.663 44.766 154.758 1.00 81.41 C ANISOU 2912 CD1 ILE A 302 12363 10569 8000 499 863 1556 C ATOM 2913 N TRP A 303 28.372 44.593 160.301 1.00 84.77 N ANISOU 2913 N TRP A 303 12773 11408 8027 515 887 1528 N ATOM 2914 CA TRP A 303 29.149 44.638 161.552 1.00 85.75 C ANISOU 2914 CA TRP A 303 12924 11581 8075 525 876 1469 C ATOM 2915 C TRP A 303 28.526 43.749 162.627 1.00 87.55 C ANISOU 2915 C TRP A 303 13100 11968 8194 466 847 1600 C ATOM 2916 O TRP A 303 29.189 42.844 163.145 1.00 87.70 O ANISOU 2916 O TRP A 303 13149 11974 8199 403 763 1636 O ATOM 2917 CB TRP A 303 29.268 46.081 162.064 1.00 85.95 C ANISOU 2917 CB TRP A 303 12956 11643 8059 631 973 1332 C ATOM 2918 CG TRP A 303 29.999 46.229 163.379 1.00 86.34 C ANISOU 2918 CG TRP A 303 13027 11754 8022 649 970 1263 C ATOM 2919 CD1 TRP A 303 31.256 45.784 163.676 1.00 85.88 C ANISOU 2919 CD1 TRP A 303 13030 11617 7983 614 899 1211 C ATOM 2920 CD2 TRP A 303 29.518 46.887 164.560 1.00 87.20 C ANISOU 2920 CD2 TRP A 303 13096 12023 8011 711 1040 1233 C ATOM 2921 NE1 TRP A 303 31.584 46.112 164.974 1.00 86.28 N ANISOU 2921 NE1 TRP A 303 13082 11767 7933 647 920 1155 N ATOM 2922 CE2 TRP A 303 30.536 46.793 165.537 1.00 87.31 C ANISOU 2922 CE2 TRP A 303 13151 12045 7976 707 1007 1165 C ATOM 2923 CE3 TRP A 303 28.321 47.543 164.890 1.00 87.86 C ANISOU 2923 CE3 TRP A 303 13110 12250 8021 774 1127 1253 C ATOM 2924 CZ2 TRP A 303 30.393 47.328 166.826 1.00 88.37 C ANISOU 2924 CZ2 TRP A 303 13261 12326 7990 761 1057 1118 C ATOM 2925 CZ3 TRP A 303 28.179 48.078 166.173 1.00 88.81 C ANISOU 2925 CZ3 TRP A 303 13204 12519 8020 832 1177 1202 C ATOM 2926 CH2 TRP A 303 29.212 47.965 167.123 1.00 89.13 C ANISOU 2926 CH2 TRP A 303 13288 12563 8013 824 1142 1135 C ATOM 2927 N ASN A 304 27.251 44.000 162.923 1.00 89.37 N ANISOU 2927 N ASN A 304 13252 12350 8351 486 913 1675 N ATOM 2928 CA ASN A 304 26.497 43.233 163.926 1.00 91.32 C ANISOU 2928 CA ASN A 304 13436 12775 8486 428 896 1811 C ATOM 2929 C ASN A 304 26.435 41.740 163.598 1.00 91.45 C ANISOU 2929 C ASN A 304 13456 12750 8540 305 783 1960 C ATOM 2930 O ASN A 304 26.736 40.902 164.452 1.00 92.42 O ANISOU 2930 O ASN A 304 13584 12924 8605 240 716 2027 O ATOM 2931 CB ASN A 304 25.070 43.781 164.078 1.00 92.64 C ANISOU 2931 CB ASN A 304 13510 13108 8578 472 988 1867 C ATOM 2932 CG ASN A 304 25.025 45.128 164.772 1.00 93.98 C ANISOU 2932 CG ASN A 304 13667 13362 8677 592 1091 1735 C ATOM 2933 OD1 ASN A 304 25.609 45.312 165.843 1.00 95.29 O ANISOU 2933 OD1 ASN A 304 13850 13587 8767 615 1095 1673 O ATOM 2934 ND2 ASN A 304 24.313 46.077 164.170 1.00 94.32 N ANISOU 2934 ND2 ASN A 304 13681 13413 8744 673 1172 1690 N ATOM 2935 N ASP A 305 26.057 41.416 162.361 1.00 90.87 N ANISOU 2935 N ASP A 305 13380 12581 8563 274 757 2009 N ATOM 2936 CA ASP A 305 25.872 40.017 161.955 1.00 90.92 C ANISOU 2936 CA ASP A 305 13388 12545 8612 160 646 2152 C ATOM 2937 C ASP A 305 27.174 39.235 161.742 1.00 90.60 C ANISOU 2937 C ASP A 305 13433 12343 8647 114 533 2115 C ATOM 2938 O ASP A 305 27.167 38.012 161.893 1.00 91.66 O ANISOU 2938 O ASP A 305 13575 12468 8784 20 429 2231 O ATOM 2939 CB ASP A 305 25.000 39.922 160.695 1.00 90.59 C ANISOU 2939 CB ASP A 305 13312 12459 8646 144 653 2215 C ATOM 2940 CG ASP A 305 23.583 40.434 160.919 1.00 91.70 C ANISOU 2940 CG ASP A 305 13357 12775 8707 172 747 2285 C ATOM 2941 OD1 ASP A 305 23.325 41.087 161.952 1.00 92.51 O ANISOU 2941 OD1 ASP A 305 13422 13024 8703 226 822 2254 O ATOM 2942 OD2 ASP A 305 22.721 40.186 160.052 1.00 92.43 O ANISOU 2942 OD2 ASP A 305 13410 12865 8844 143 745 2366 O ATOM 2943 N HIS A 306 28.273 39.912 161.392 1.00 90.12 N ANISOU 2943 N HIS A 306 13437 12158 8646 179 547 1958 N ATOM 2944 CA HIS A 306 29.536 39.207 161.096 1.00 89.69 C ANISOU 2944 CA HIS A 306 13459 11951 8665 143 441 1913 C ATOM 2945 C HIS A 306 30.768 39.643 161.912 1.00 89.63 C ANISOU 2945 C HIS A 306 13505 11924 8627 187 443 1785 C ATOM 2946 O HIS A 306 31.525 38.782 162.358 1.00 89.48 O ANISOU 2946 O HIS A 306 13524 11867 8604 138 348 1804 O ATOM 2947 CB HIS A 306 29.829 39.265 159.590 1.00 89.08 C ANISOU 2947 CB HIS A 306 13414 11715 8718 154 420 1861 C ATOM 2948 CG HIS A 306 28.795 38.579 158.749 1.00 89.42 C ANISOU 2948 CG HIS A 306 13416 11756 8802 97 387 1990 C ATOM 2949 ND1 HIS A 306 28.966 37.307 158.247 1.00 89.51 N ANISOU 2949 ND1 HIS A 306 13453 11681 8876 16 263 2070 N ATOM 2950 CD2 HIS A 306 27.572 38.986 158.329 1.00 89.97 C ANISOU 2950 CD2 HIS A 306 13421 11901 8861 109 459 2051 C ATOM 2951 CE1 HIS A 306 27.897 36.961 157.551 1.00 89.79 C ANISOU 2951 CE1 HIS A 306 13442 11736 8937 -22 260 2175 C ATOM 2952 NE2 HIS A 306 27.035 37.961 157.587 1.00 90.08 N ANISOU 2952 NE2 HIS A 306 13422 11875 8929 32 379 2167 N ATOM 2953 N PHE A 307 30.973 40.949 162.109 1.00 90.27 N ANISOU 2953 N PHE A 307 13587 12025 8685 277 544 1657 N ATOM 2954 CA PHE A 307 32.204 41.467 162.749 1.00 90.76 C ANISOU 2954 CA PHE A 307 13702 12052 8729 322 547 1520 C ATOM 2955 C PHE A 307 32.011 41.995 164.178 1.00 93.39 C ANISOU 2955 C PHE A 307 14008 12543 8933 358 608 1501 C ATOM 2956 O PHE A 307 32.813 42.799 164.664 1.00 93.55 O ANISOU 2956 O PHE A 307 14062 12549 8933 418 644 1368 O ATOM 2957 CB PHE A 307 32.837 42.542 161.847 1.00 89.22 C ANISOU 2957 CB PHE A 307 13545 11735 8618 392 599 1370 C ATOM 2958 CG PHE A 307 33.469 41.980 160.606 1.00 87.43 C ANISOU 2958 CG PHE A 307 13359 11349 8510 358 524 1358 C ATOM 2959 CD1 PHE A 307 32.723 41.803 159.446 1.00 86.40 C ANISOU 2959 CD1 PHE A 307 13204 11175 8448 341 525 1421 C ATOM 2960 CD2 PHE A 307 34.807 41.595 160.607 1.00 86.56 C ANISOU 2960 CD2 PHE A 307 13309 11141 8439 344 448 1283 C ATOM 2961 CE1 PHE A 307 33.302 41.265 158.310 1.00 85.56 C ANISOU 2961 CE1 PHE A 307 13131 10931 8445 313 454 1406 C ATOM 2962 CE2 PHE A 307 35.392 41.059 159.471 1.00 85.52 C ANISOU 2962 CE2 PHE A 307 13209 10875 8410 318 376 1266 C ATOM 2963 CZ PHE A 307 34.638 40.891 158.320 1.00 85.09 C ANISOU 2963 CZ PHE A 307 13129 10779 8421 303 379 1327 C ATOM 2964 N ARG A 308 30.968 41.522 164.857 1.00 96.67 N ANISOU 2964 N ARG A 308 14360 13110 9258 321 616 1633 N ATOM 2965 CA ARG A 308 30.667 41.957 166.221 1.00 99.14 C ANISOU 2965 CA ARG A 308 14634 13596 9436 354 674 1627 C ATOM 2966 C ARG A 308 31.453 41.119 167.233 1.00101.03 C ANISOU 2966 C ARG A 308 14903 13862 9619 299 590 1657 C ATOM 2967 O ARG A 308 31.652 39.917 167.041 1.00100.85 O ANISOU 2967 O ARG A 308 14900 13784 9633 213 484 1757 O ATOM 2968 CB ARG A 308 29.163 41.838 166.492 1.00100.17 C ANISOU 2968 CB ARG A 308 14673 13898 9487 337 723 1761 C ATOM 2969 CG ARG A 308 28.640 42.708 167.627 1.00100.98 C ANISOU 2969 CG ARG A 308 14723 14188 9458 408 820 1721 C ATOM 2970 CD ARG A 308 28.689 44.193 167.286 1.00100.46 C ANISOU 2970 CD ARG A 308 14667 14085 9417 526 921 1562 C ATOM 2971 NE ARG A 308 27.764 44.983 168.097 1.00101.37 N ANISOU 2971 NE ARG A 308 14711 14389 9415 598 1018 1550 N ATOM 2972 CZ ARG A 308 27.940 45.310 169.377 1.00102.63 C ANISOU 2972 CZ ARG A 308 14855 14682 9456 636 1047 1503 C ATOM 2973 NH1 ARG A 308 29.015 44.909 170.060 1.00102.82 N ANISOU 2973 NH1 ARG A 308 14931 14675 9460 605 986 1467 N ATOM 2974 NH2 ARG A 308 27.013 46.042 169.995 1.00103.70 N ANISOU 2974 NH2 ARG A 308 14919 14993 9488 709 1136 1490 N ATOM 2975 N CYS A 309 31.897 41.777 168.301 1.00128.03 N ANISOU 2975 N CYS A 309 14505 21972 12167 -4848 1539 -3139 N ATOM 2976 CA CYS A 309 32.625 41.147 169.401 1.00126.19 C ANISOU 2976 CA CYS A 309 13883 21636 12425 -4390 1852 -3271 C ATOM 2977 C CYS A 309 32.046 41.709 170.701 1.00122.11 C ANISOU 2977 C CYS A 309 12950 21287 12158 -4036 1460 -3055 C ATOM 2978 O CYS A 309 32.749 42.316 171.513 1.00119.34 O ANISOU 2978 O CYS A 309 12397 20906 12038 -3796 1447 -3001 O ATOM 2979 CB CYS A 309 34.123 41.440 169.271 1.00127.99 C ANISOU 2979 CB CYS A 309 14003 21635 12991 -4256 2320 -3372 C ATOM 2980 SG CYS A 309 34.476 43.171 168.885 1.00128.59 S ANISOU 2980 SG CYS A 309 14068 21870 12919 -4267 2103 -3238 S ATOM 2981 N GLN A 310 30.743 41.484 170.880 1.00122.49 N ANISOU 2981 N GLN A 310 12954 21411 12173 -4090 1188 -2900 N ATOM 2982 CA GLN A 310 29.971 42.061 171.995 1.00121.52 C ANISOU 2982 CA GLN A 310 12563 21272 12337 -3827 1073 -2704 C ATOM 2983 C GLN A 310 30.474 41.677 173.396 1.00120.17 C ANISOU 2983 C GLN A 310 12389 20977 12290 -3586 1233 -2825 C ATOM 2984 O GLN A 310 30.412 42.509 174.310 1.00119.55 O ANISOU 2984 O GLN A 310 12378 20778 12266 -3485 1292 -2750 O ATOM 2985 CB GLN A 310 28.475 41.723 171.863 1.00122.89 C ANISOU 2985 CB GLN A 310 12578 21404 12707 -3937 861 -2430 C ATOM 2986 CG GLN A 310 27.568 42.502 172.813 1.00123.00 C ANISOU 2986 CG GLN A 310 12295 21203 13234 -3688 1008 -2172 C ATOM 2987 CD GLN A 310 26.102 42.138 172.679 1.00125.80 C ANISOU 2987 CD GLN A 310 12297 21388 14111 -3769 846 -1764 C ATOM 2988 OE1 GLN A 310 25.662 41.629 171.647 1.00128.27 O ANISOU 2988 OE1 GLN A 310 12603 21801 14333 -4143 359 -1535 O ATOM 2989 NE2 GLN A 310 25.333 42.405 173.730 1.00126.77 N ANISOU 2989 NE2 GLN A 310 12196 21153 14815 -3499 1286 -1628 N ATOM 2990 N PRO A 311 30.963 40.427 173.575 1.00120.18 N ANISOU 2990 N PRO A 311 12403 20929 12329 -3586 1309 -2971 N ATOM 2991 CA PRO A 311 31.541 40.076 174.877 1.00119.91 C ANISOU 2991 CA PRO A 311 12392 20734 12431 -3501 1262 -2949 C ATOM 2992 C PRO A 311 32.727 40.939 175.341 1.00120.29 C ANISOU 2992 C PRO A 311 12475 20682 12548 -3542 1103 -2814 C ATOM 2993 O PRO A 311 32.954 41.020 176.544 1.00120.90 O ANISOU 2993 O PRO A 311 12784 20581 12572 -3659 894 -2684 O ATOM 2994 CB PRO A 311 31.967 38.619 174.686 1.00120.57 C ANISOU 2994 CB PRO A 311 12344 20737 12728 -3509 1369 -3039 C ATOM 2995 CG PRO A 311 31.016 38.094 173.673 1.00120.84 C ANISOU 2995 CG PRO A 311 12465 20890 12556 -3613 1496 -3168 C ATOM 2996 CD PRO A 311 30.820 39.234 172.718 1.00121.35 C ANISOU 2996 CD PRO A 311 12623 21082 12401 -3746 1427 -3108 C ATOM 2997 N LEU A 312 33.457 41.575 174.419 1.00120.74 N ANISOU 2997 N LEU A 312 12400 20798 12675 -3543 1167 -2810 N ATOM 2998 CA LEU A 312 34.450 42.605 174.784 1.00121.27 C ANISOU 2998 CA LEU A 312 12477 20778 12819 -3599 966 -2626 C ATOM 2999 C LEU A 312 33.785 43.874 175.330 1.00120.41 C ANISOU 2999 C LEU A 312 12715 20697 12337 -3643 920 -2608 C ATOM 3000 O LEU A 312 34.282 44.470 176.286 1.00122.08 O ANISOU 3000 O LEU A 312 13236 20727 12420 -3829 700 -2456 O ATOM 3001 CB LEU A 312 35.348 42.982 173.597 1.00122.21 C ANISOU 3001 CB LEU A 312 12371 20902 13159 -3573 1174 -2645 C ATOM 3002 CG LEU A 312 36.364 41.944 173.117 1.00125.16 C ANISOU 3002 CG LEU A 312 12404 20989 14160 -3546 1494 -2608 C ATOM 3003 CD1 LEU A 312 37.034 42.418 171.833 1.00127.05 C ANISOU 3003 CD1 LEU A 312 12622 21131 14518 -3571 1967 -2720 C ATOM 3004 CD2 LEU A 312 37.401 41.650 174.195 1.00127.72 C ANISOU 3004 CD2 LEU A 312 12379 20999 15149 -3589 1105 -2169 C ATOM 3005 N GLU A 313 32.683 44.294 174.706 1.00119.16 N ANISOU 3005 N GLU A 313 12532 20671 12072 -3550 1131 -2692 N ATOM 3006 CA GLU A 313 31.904 45.446 175.188 1.00119.42 C ANISOU 3006 CA GLU A 313 12774 20572 12026 -3538 1313 -2628 C ATOM 3007 C GLU A 313 31.226 45.157 176.534 1.00120.02 C ANISOU 3007 C GLU A 313 13256 20321 12025 -3608 1557 -2657 C ATOM 3008 O GLU A 313 31.163 46.036 177.399 1.00121.99 O ANISOU 3008 O GLU A 313 14008 20253 12090 -3754 1814 -2652 O ATOM 3009 CB GLU A 313 30.873 45.900 174.140 1.00120.07 C ANISOU 3009 CB GLU A 313 12541 20763 12317 -3460 1394 -2514 C ATOM 3010 CG GLU A 313 31.501 46.565 172.918 1.00120.21 C ANISOU 3010 CG GLU A 313 12426 21001 12244 -3532 1204 -2478 C ATOM 3011 CD GLU A 313 30.487 47.153 171.947 1.00122.01 C ANISOU 3011 CD GLU A 313 12411 21271 12675 -3620 1076 -2206 C ATOM 3012 OE1 GLU A 313 29.287 46.817 172.049 1.00123.55 O ANISOU 3012 OE1 GLU A 313 12389 21331 13222 -3616 1074 -1984 O ATOM 3013 OE2 GLU A 313 30.892 47.941 171.062 1.00122.33 O ANISOU 3013 OE2 GLU A 313 12444 21433 12600 -3743 918 -2133 O ATOM 3014 N VAL A 314 30.735 43.926 176.704 1.00118.44 N ANISOU 3014 N VAL A 314 12956 20132 11911 -3566 1558 -2714 N ATOM 3015 CA VAL A 314 30.191 43.460 177.993 1.00118.93 C ANISOU 3015 CA VAL A 314 13487 19852 11849 -3688 1807 -2769 C ATOM 3016 C VAL A 314 31.311 43.349 179.042 1.00119.11 C ANISOU 3016 C VAL A 314 14085 19697 11474 -4065 1445 -2719 C ATOM 3017 O VAL A 314 31.117 43.699 180.209 1.00121.96 O ANISOU 3017 O VAL A 314 15251 19636 11451 -4408 1666 -2742 O ATOM 3018 CB VAL A 314 29.450 42.103 177.844 1.00118.11 C ANISOU 3018 CB VAL A 314 13087 19835 11952 -3559 1819 -2816 C ATOM 3019 CG1 VAL A 314 29.021 41.549 179.200 1.00120.39 C ANISOU 3019 CG1 VAL A 314 13929 19751 12062 -3729 2073 -2889 C ATOM 3020 CG2 VAL A 314 28.231 42.249 176.938 1.00118.40 C ANISOU 3020 CG2 VAL A 314 12626 19930 12429 -3361 2004 -2687 C ATOM 3021 N LEU A 315 32.470 42.854 178.604 1.00116.71 N ANISOU 3021 N LEU A 315 13407 19608 11330 -4084 915 -2586 N ATOM 3022 CA LEU A 315 33.686 42.747 179.431 1.00118.24 C ANISOU 3022 CA LEU A 315 13889 19596 11440 -4498 318 -2293 C ATOM 3023 C LEU A 315 34.131 44.081 180.054 1.00119.81 C ANISOU 3023 C LEU A 315 14767 19552 11200 -4896 183 -2168 C ATOM 3024 O LEU A 315 34.658 44.092 181.163 1.00123.41 O ANISOU 3024 O LEU A 315 15930 19665 11292 -5495 -289 -1911 O ATOM 3025 CB LEU A 315 34.815 42.105 178.600 1.00117.76 C ANISOU 3025 CB LEU A 315 13033 19682 12026 -4335 -9 -2083 C ATOM 3026 CG LEU A 315 36.292 42.130 178.977 1.00121.52 C ANISOU 3026 CG LEU A 315 13320 19919 12934 -4654 -679 -1562 C ATOM 3027 CD1 LEU A 315 36.543 41.509 180.344 1.00126.21 C ANISOU 3027 CD1 LEU A 315 14373 20166 13413 -5205 -1332 -1175 C ATOM 3028 CD2 LEU A 315 37.107 41.422 177.901 1.00121.51 C ANISOU 3028 CD2 LEU A 315 12393 19928 13846 -4321 -509 -1451 C ATOM 3029 N PHE A 316 33.912 45.192 179.348 1.00117.55 N ANISOU 3029 N PHE A 316 14354 19401 10908 -4661 541 -2306 N ATOM 3030 CA PHE A 316 34.119 46.533 179.924 1.00119.52 C ANISOU 3030 CA PHE A 316 15343 19368 10698 -5019 616 -2267 C ATOM 3031 C PHE A 316 32.986 46.888 180.889 1.00122.01 C ANISOU 3031 C PHE A 316 16587 19204 10568 -5244 1364 -2501 C ATOM 3032 O PHE A 316 31.893 47.271 180.472 1.00120.40 O ANISOU 3032 O PHE A 316 16137 18950 10658 -4856 2129 -2694 O ATOM 3033 CB PHE A 316 34.247 47.609 178.831 1.00116.66 C ANISOU 3033 CB PHE A 316 14498 19268 10560 -4679 804 -2318 C ATOM 3034 CG PHE A 316 35.651 47.801 178.330 1.00116.18 C ANISOU 3034 CG PHE A 316 14020 19380 10743 -4738 184 -2044 C ATOM 3035 CD1 PHE A 316 36.543 48.614 179.025 1.00119.64 C ANISOU 3035 CD1 PHE A 316 15013 19564 10880 -5240 -271 -1769 C ATOM 3036 CD2 PHE A 316 36.084 47.178 177.163 1.00113.53 C ANISOU 3036 CD2 PHE A 316 12812 19354 10970 -4363 128 -2032 C ATOM 3037 CE1 PHE A 316 37.841 48.799 178.568 1.00120.39 C ANISOU 3037 CE1 PHE A 316 14588 19737 11416 -5282 -840 -1410 C ATOM 3038 CE2 PHE A 316 37.380 47.358 176.699 1.00114.76 C ANISOU 3038 CE2 PHE A 316 12537 19513 11553 -4391 -223 -1757 C ATOM 3039 CZ PHE A 316 38.261 48.170 177.403 1.00118.00 C ANISOU 3039 CZ PHE A 316 13293 19693 11846 -4808 -742 -1406 C TER 3040 PHE A 316 ATOM 3041 N SER B 6 61.723 24.440 111.833 1.00122.86 N ANISOU 3041 N SER B 6 17156 15588 13936 -884 2062 -463 N ATOM 3042 CA SER B 6 60.785 25.485 111.340 1.00122.70 C ANISOU 3042 CA SER B 6 17179 15750 13691 -989 1923 -243 C ATOM 3043 C SER B 6 59.357 24.929 111.271 1.00122.22 C ANISOU 3043 C SER B 6 17150 15712 13574 -1031 1866 -243 C ATOM 3044 O SER B 6 58.535 25.245 112.139 1.00122.40 O ANISOU 3044 O SER B 6 17219 15604 13681 -908 1742 -70 O ATOM 3045 CB SER B 6 61.270 26.032 109.990 1.00124.64 C ANISOU 3045 CB SER B 6 17384 16287 13684 -1205 1971 -261 C ATOM 3046 OG SER B 6 60.303 26.865 109.382 1.00125.56 O ANISOU 3046 OG SER B 6 17518 16602 13585 -1327 1845 -45 O ATOM 3047 N ALA B 7 59.085 24.082 110.274 1.00122.73 N ANISOU 3047 N ALA B 7 17187 15942 13502 -1211 1967 -452 N ATOM 3048 CA ALA B 7 57.756 23.481 110.070 1.00122.21 C ANISOU 3048 CA ALA B 7 17143 15937 13353 -1290 1928 -480 C ATOM 3049 C ALA B 7 57.234 22.735 111.302 1.00119.96 C ANISOU 3049 C ALA B 7 16898 15362 13318 -1096 1903 -500 C ATOM 3050 O ALA B 7 56.031 22.743 111.584 1.00119.35 O ANISOU 3050 O ALA B 7 16854 15283 13210 -1084 1796 -386 O ATOM 3051 CB ALA B 7 57.778 22.548 108.866 1.00124.63 C ANISOU 3051 CB ALA B 7 17408 16448 13496 -1529 2085 -768 C ATOM 3052 N PHE B 8 58.151 22.102 112.028 1.00118.32 N ANISOU 3052 N PHE B 8 16674 14921 13359 -948 2001 -630 N ATOM 3053 CA PHE B 8 57.850 21.467 113.322 1.00115.70 C ANISOU 3053 CA PHE B 8 16367 14307 13285 -751 1970 -613 C ATOM 3054 C PHE B 8 57.419 22.509 114.359 1.00111.31 C ANISOU 3054 C PHE B 8 15858 13661 12773 -605 1792 -324 C ATOM 3055 O PHE B 8 56.432 22.299 115.075 1.00109.60 O ANISOU 3055 O PHE B 8 15680 13341 12621 -530 1707 -245 O ATOM 3056 CB PHE B 8 59.064 20.683 113.822 1.00116.32 C ANISOU 3056 CB PHE B 8 16391 14182 13620 -631 2108 -769 C ATOM 3057 CG PHE B 8 59.630 19.757 112.775 1.00118.64 C ANISOU 3057 CG PHE B 8 16628 14550 13899 -773 2316 -1070 C ATOM 3058 CD1 PHE B 8 58.810 18.812 112.170 1.00119.61 C ANISOU 3058 CD1 PHE B 8 16763 14721 13962 -910 2399 -1262 C ATOM 3059 CD2 PHE B 8 60.947 19.883 112.330 1.00119.82 C ANISOU 3059 CD2 PHE B 8 16710 14740 14074 -794 2436 -1171 C ATOM 3060 CE1 PHE B 8 59.306 17.969 111.176 1.00122.07 C ANISOU 3060 CE1 PHE B 8 17021 15103 14255 -1066 2614 -1571 C ATOM 3061 CE2 PHE B 8 61.443 19.051 111.340 1.00122.03 C ANISOU 3061 CE2 PHE B 8 16932 15090 14341 -937 2647 -1469 C ATOM 3062 CZ PHE B 8 60.625 18.090 110.763 1.00123.44 C ANISOU 3062 CZ PHE B 8 17125 15304 14471 -1078 2743 -1678 C ATOM 3063 N GLN B 9 58.144 23.634 114.415 1.00108.63 N ANISOU 3063 N GLN B 9 15512 13363 12396 -578 1747 -179 N ATOM 3064 CA GLN B 9 57.794 24.723 115.343 1.00105.66 C ANISOU 3064 CA GLN B 9 15178 12901 12063 -463 1605 73 C ATOM 3065 C GLN B 9 56.428 25.324 114.987 1.00104.75 C ANISOU 3065 C GLN B 9 15096 12907 11795 -533 1489 239 C ATOM 3066 O GLN B 9 55.584 25.570 115.865 1.00103.81 O ANISOU 3066 O GLN B 9 15013 12670 11758 -431 1393 372 O ATOM 3067 CB GLN B 9 58.873 25.809 115.326 1.00105.20 C ANISOU 3067 CB GLN B 9 15105 12877 11987 -453 1603 173 C ATOM 3068 CG GLN B 9 58.854 26.710 116.547 1.00103.75 C ANISOU 3068 CG GLN B 9 14957 12541 11921 -316 1506 364 C ATOM 3069 CD GLN B 9 59.862 27.846 116.478 1.00103.62 C ANISOU 3069 CD GLN B 9 14931 12565 11874 -331 1509 460 C ATOM 3070 OE1 GLN B 9 60.726 27.883 115.601 1.00105.00 O ANISOU 3070 OE1 GLN B 9 15065 12870 11959 -425 1586 379 O ATOM 3071 NE2 GLN B 9 59.753 28.781 117.410 1.00102.31 N ANISOU 3071 NE2 GLN B 9 14799 12288 11783 -250 1436 622 N ATOM 3072 N ALA B 10 56.222 25.539 113.688 1.00105.52 N ANISOU 3072 N ALA B 10 15169 13254 11669 -715 1502 233 N ATOM 3073 CA ALA B 10 54.925 25.955 113.158 1.00105.87 C ANISOU 3073 CA ALA B 10 15215 13459 11551 -810 1399 390 C ATOM 3074 C ALA B 10 53.819 24.956 113.500 1.00105.11 C ANISOU 3074 C ALA B 10 15136 13302 11496 -794 1382 308 C ATOM 3075 O ALA B 10 52.715 25.364 113.838 1.00104.00 O ANISOU 3075 O ALA B 10 15008 13155 11349 -756 1270 484 O ATOM 3076 CB ALA B 10 55.007 26.156 111.651 1.00107.94 C ANISOU 3076 CB ALA B 10 15428 14036 11547 -1042 1429 373 C ATOM 3077 N ALA B 11 54.118 23.660 113.412 1.00105.16 N ANISOU 3077 N ALA B 11 15138 13257 11560 -823 1503 43 N ATOM 3078 CA ALA B 11 53.166 22.607 113.800 1.00104.20 C ANISOU 3078 CA ALA B 11 15036 13047 11505 -807 1505 -56 C ATOM 3079 C ALA B 11 52.843 22.637 115.297 1.00101.99 C ANISOU 3079 C ALA B 11 14797 12504 11450 -593 1427 54 C ATOM 3080 O ALA B 11 51.671 22.552 115.681 1.00101.73 O ANISOU 3080 O ALA B 11 14785 12452 11415 -570 1342 140 O ATOM 3081 CB ALA B 11 53.686 21.236 113.398 1.00105.06 C ANISOU 3081 CB ALA B 11 15127 13122 11668 -881 1677 -372 C ATOM 3082 N TYR B 12 53.878 22.754 116.131 1.00100.40 N ANISOU 3082 N TYR B 12 14598 12121 11429 -450 1457 53 N ATOM 3083 CA TYR B 12 53.697 22.935 117.581 1.00 97.74 C ANISOU 3083 CA TYR B 12 14290 11566 11278 -270 1381 173 C ATOM 3084 C TYR B 12 52.801 24.150 117.868 1.00 96.12 C ANISOU 3084 C TYR B 12 14111 11400 11007 -244 1247 416 C ATOM 3085 O TYR B 12 51.756 24.026 118.541 1.00 94.65 O ANISOU 3085 O TYR B 12 13948 11140 10871 -188 1176 487 O ATOM 3086 CB TYR B 12 55.054 23.091 118.290 1.00 97.13 C ANISOU 3086 CB TYR B 12 14194 11354 11356 -159 1425 164 C ATOM 3087 CG TYR B 12 54.950 23.633 119.703 1.00 95.93 C ANISOU 3087 CG TYR B 12 14066 11043 11337 -16 1336 320 C ATOM 3088 CD1 TYR B 12 54.467 22.839 120.746 1.00 95.39 C ANISOU 3088 CD1 TYR B 12 14008 10818 11416 75 1311 307 C ATOM 3089 CD2 TYR B 12 55.320 24.946 119.996 1.00 95.64 C ANISOU 3089 CD2 TYR B 12 14042 11020 11276 9 1284 474 C ATOM 3090 CE1 TYR B 12 54.364 23.337 122.037 1.00 94.06 C ANISOU 3090 CE1 TYR B 12 13857 10534 11344 177 1235 438 C ATOM 3091 CE2 TYR B 12 55.222 25.454 121.284 1.00 94.58 C ANISOU 3091 CE2 TYR B 12 13929 10754 11251 111 1221 588 C ATOM 3092 CZ TYR B 12 54.742 24.645 122.299 1.00 93.92 C ANISOU 3092 CZ TYR B 12 13852 10541 11291 188 1196 567 C ATOM 3093 OH TYR B 12 54.637 25.145 123.571 1.00 93.55 O ANISOU 3093 OH TYR B 12 13822 10393 11330 262 1139 669 O ATOM 3094 N ILE B 13 53.206 25.302 117.326 1.00 95.73 N ANISOU 3094 N ILE B 13 14051 11463 10858 -289 1225 540 N ATOM 3095 CA ILE B 13 52.457 26.560 117.493 1.00 94.67 C ANISOU 3095 CA ILE B 13 13927 11352 10692 -265 1121 782 C ATOM 3096 C ILE B 13 51.003 26.417 117.011 1.00 95.04 C ANISOU 3096 C ILE B 13 13960 11520 10630 -336 1051 860 C ATOM 3097 O ILE B 13 50.075 26.853 117.692 1.00 95.15 O ANISOU 3097 O ILE B 13 13984 11452 10715 -256 975 1002 O ATOM 3098 CB ILE B 13 53.163 27.742 116.778 1.00 94.97 C ANISOU 3098 CB ILE B 13 13944 11503 10636 -328 1124 902 C ATOM 3099 CG1 ILE B 13 54.475 28.087 117.499 1.00 94.24 C ANISOU 3099 CG1 ILE B 13 13865 11273 10669 -242 1174 866 C ATOM 3100 CG2 ILE B 13 52.275 28.984 116.734 1.00 95.17 C ANISOU 3100 CG2 ILE B 13 13961 11558 10640 -319 1031 1165 C ATOM 3101 CD1 ILE B 13 55.490 28.808 116.642 1.00 95.26 C ANISOU 3101 CD1 ILE B 13 13969 11528 10696 -330 1216 891 C ATOM 3102 N GLY B 14 50.821 25.789 115.852 1.00 95.31 N ANISOU 3102 N GLY B 14 13963 11758 10492 -495 1085 757 N ATOM 3103 CA GLY B 14 49.498 25.545 115.272 1.00 95.10 C ANISOU 3103 CA GLY B 14 13909 11894 10329 -598 1023 815 C ATOM 3104 C GLY B 14 48.623 24.629 116.105 1.00 93.18 C ANISOU 3104 C GLY B 14 13695 11515 10193 -526 1006 738 C ATOM 3105 O GLY B 14 47.449 24.927 116.328 1.00 92.95 O ANISOU 3105 O GLY B 14 13652 11509 10154 -506 915 889 O ATOM 3106 N ILE B 15 49.195 23.517 116.565 1.00 91.80 N ANISOU 3106 N ILE B 15 13550 11196 10134 -486 1096 515 N ATOM 3107 CA ILE B 15 48.478 22.572 117.430 1.00 90.50 C ANISOU 3107 CA ILE B 15 13413 10879 10092 -415 1088 439 C ATOM 3108 C ILE B 15 48.110 23.243 118.763 1.00 88.23 C ANISOU 3108 C ILE B 15 13152 10410 9960 -243 1003 610 C ATOM 3109 O ILE B 15 46.961 23.123 119.226 1.00 86.76 O ANISOU 3109 O ILE B 15 12971 10201 9793 -216 936 679 O ATOM 3110 CB ILE B 15 49.289 21.268 117.647 1.00 90.51 C ANISOU 3110 CB ILE B 15 13427 10741 10221 -399 1214 188 C ATOM 3111 CG1 ILE B 15 49.362 20.470 116.340 1.00 92.42 C ANISOU 3111 CG1 ILE B 15 13644 11161 10311 -595 1319 -18 C ATOM 3112 CG2 ILE B 15 48.671 20.397 118.740 1.00 89.52 C ANISOU 3112 CG2 ILE B 15 13330 10423 10260 -301 1198 151 C ATOM 3113 CD1 ILE B 15 50.515 19.487 116.275 1.00 93.16 C ANISOU 3113 CD1 ILE B 15 13727 11130 10536 -588 1479 -260 C ATOM 3114 N GLU B 16 49.073 23.959 119.354 1.00 87.55 N ANISOU 3114 N GLU B 16 13078 10212 9975 -145 1013 667 N ATOM 3115 CA GLU B 16 48.813 24.739 120.577 1.00 86.82 C ANISOU 3115 CA GLU B 16 13006 9967 10012 -12 950 813 C ATOM 3116 C GLU B 16 47.683 25.756 120.379 1.00 86.01 C ANISOU 3116 C GLU B 16 12885 9943 9851 -21 866 1018 C ATOM 3117 O GLU B 16 46.715 25.797 121.160 1.00 85.94 O ANISOU 3117 O GLU B 16 12882 9854 9916 42 815 1086 O ATOM 3118 CB GLU B 16 50.086 25.462 121.043 1.00 87.69 C ANISOU 3118 CB GLU B 16 13123 9990 10202 51 984 837 C ATOM 3119 CG GLU B 16 51.124 24.558 121.695 1.00 88.55 C ANISOU 3119 CG GLU B 16 13234 9975 10434 107 1048 691 C ATOM 3120 CD GLU B 16 50.875 24.314 123.177 1.00 88.45 C ANISOU 3120 CD GLU B 16 13240 9795 10571 213 1012 719 C ATOM 3121 OE1 GLU B 16 49.701 24.133 123.576 1.00 89.61 O ANISOU 3121 OE1 GLU B 16 13402 9918 10726 227 959 761 O ATOM 3122 OE2 GLU B 16 51.862 24.293 123.950 1.00 88.46 O ANISOU 3122 OE2 GLU B 16 13230 9705 10673 271 1036 703 O ATOM 3123 N VAL B 17 47.816 26.557 119.322 1.00 85.58 N ANISOU 3123 N VAL B 17 12795 10049 9672 -104 855 1123 N ATOM 3124 CA VAL B 17 46.797 27.539 118.930 1.00 85.06 C ANISOU 3124 CA VAL B 17 12684 10077 9556 -121 779 1352 C ATOM 3125 C VAL B 17 45.428 26.882 118.710 1.00 85.34 C ANISOU 3125 C VAL B 17 12689 10212 9522 -172 722 1367 C ATOM 3126 O VAL B 17 44.417 27.435 119.127 1.00 84.88 O ANISOU 3126 O VAL B 17 12602 10118 9528 -111 661 1528 O ATOM 3127 CB VAL B 17 47.235 28.344 117.675 1.00 85.76 C ANISOU 3127 CB VAL B 17 12726 10357 9502 -230 775 1470 C ATOM 3128 CG1 VAL B 17 46.071 29.099 117.037 1.00 86.69 C ANISOU 3128 CG1 VAL B 17 12767 10623 9547 -277 688 1723 C ATOM 3129 CG2 VAL B 17 48.350 29.321 118.039 1.00 85.26 C ANISOU 3129 CG2 VAL B 17 12686 10174 9534 -164 816 1519 C ATOM 3130 N LEU B 18 45.404 25.712 118.072 1.00 86.15 N ANISOU 3130 N LEU B 18 12792 10434 9504 -287 754 1191 N ATOM 3131 CA LEU B 18 44.149 24.982 117.823 1.00 86.53 C ANISOU 3131 CA LEU B 18 12814 10593 9468 -362 710 1177 C ATOM 3132 C LEU B 18 43.531 24.484 119.133 1.00 84.36 C ANISOU 3132 C LEU B 18 12579 10114 9359 -237 694 1137 C ATOM 3133 O LEU B 18 42.330 24.689 119.386 1.00 84.01 O ANISOU 3133 O LEU B 18 12500 10094 9323 -215 623 1264 O ATOM 3134 CB LEU B 18 44.389 23.813 116.854 1.00 88.34 C ANISOU 3134 CB LEU B 18 13042 10982 9539 -534 777 955 C ATOM 3135 CG LEU B 18 43.167 23.194 116.151 1.00 89.90 C ANISOU 3135 CG LEU B 18 13194 11394 9569 -689 736 946 C ATOM 3136 CD1 LEU B 18 43.567 22.611 114.801 1.00 91.82 C ANISOU 3136 CD1 LEU B 18 13411 11883 9593 -914 807 785 C ATOM 3137 CD2 LEU B 18 42.467 22.146 117.014 1.00 89.24 C ANISOU 3137 CD2 LEU B 18 13150 11162 9592 -637 744 821 C ATOM 3138 N ILE B 19 44.358 23.851 119.967 1.00 82.84 N ANISOU 3138 N ILE B 19 12445 9730 9298 -157 758 977 N ATOM 3139 CA ILE B 19 43.918 23.395 121.300 1.00 81.44 C ANISOU 3139 CA ILE B 19 12303 9361 9278 -45 743 949 C ATOM 3140 C ILE B 19 43.363 24.559 122.121 1.00 80.60 C ANISOU 3140 C ILE B 19 12185 9170 9267 61 685 1140 C ATOM 3141 O ILE B 19 42.289 24.438 122.720 1.00 79.70 O ANISOU 3141 O ILE B 19 12062 9020 9198 96 640 1190 O ATOM 3142 CB ILE B 19 45.056 22.692 122.079 1.00 80.40 C ANISOU 3142 CB ILE B 19 12215 9050 9281 23 813 796 C ATOM 3143 CG1 ILE B 19 45.399 21.350 121.414 1.00 81.32 C ANISOU 3143 CG1 ILE B 19 12335 9201 9359 -70 892 587 C ATOM 3144 CG2 ILE B 19 44.669 22.455 123.540 1.00 79.07 C ANISOU 3144 CG2 ILE B 19 12072 8704 9264 131 784 815 C ATOM 3145 CD1 ILE B 19 46.803 20.873 121.698 1.00 81.34 C ANISOU 3145 CD1 ILE B 19 12348 9076 9478 -20 979 463 C ATOM 3146 N ALA B 20 44.091 25.677 122.139 1.00 81.00 N ANISOU 3146 N ALA B 20 12234 9186 9356 105 698 1236 N ATOM 3147 CA ALA B 20 43.602 26.896 122.796 1.00 81.00 C ANISOU 3147 CA ALA B 20 12216 9097 9462 193 671 1409 C ATOM 3148 C ALA B 20 42.293 27.410 122.178 1.00 82.61 C ANISOU 3148 C ALA B 20 12347 9426 9613 165 607 1591 C ATOM 3149 O ALA B 20 41.380 27.802 122.901 1.00 82.31 O ANISOU 3149 O ALA B 20 12287 9306 9679 237 584 1680 O ATOM 3150 CB ALA B 20 44.667 27.983 122.762 1.00 80.89 C ANISOU 3150 CB ALA B 20 12210 9030 9491 221 712 1469 C ATOM 3151 N LEU B 21 42.210 27.396 120.848 1.00 85.26 N ANISOU 3151 N LEU B 21 12634 9974 9785 51 580 1648 N ATOM 3152 CA LEU B 21 40.996 27.817 120.120 1.00 87.67 C ANISOU 3152 CA LEU B 21 12846 10449 10015 1 506 1849 C ATOM 3153 C LEU B 21 39.785 26.913 120.357 1.00 88.54 C ANISOU 3153 C LEU B 21 12937 10609 10093 -23 462 1805 C ATOM 3154 O LEU B 21 38.654 27.383 120.247 1.00 89.04 O ANISOU 3154 O LEU B 21 12918 10743 10170 -11 401 1989 O ATOM 3155 CB LEU B 21 41.252 27.937 118.605 1.00 89.50 C ANISOU 3155 CB LEU B 21 13021 10943 10042 -151 483 1919 C ATOM 3156 CG LEU B 21 41.922 29.230 118.111 1.00 90.42 C ANISOU 3156 CG LEU B 21 13104 11073 10178 -140 489 2101 C ATOM 3157 CD1 LEU B 21 42.324 29.087 116.649 1.00 91.93 C ANISOU 3157 CD1 LEU B 21 13251 11546 10133 -321 475 2116 C ATOM 3158 CD2 LEU B 21 41.021 30.447 118.306 1.00 90.94 C ANISOU 3158 CD2 LEU B 21 13084 11086 10381 -50 442 2392 C ATOM 3159 N VAL B 22 40.008 25.629 120.645 1.00 88.98 N ANISOU 3159 N VAL B 22 13058 10631 10118 -60 495 1574 N ATOM 3160 CA VAL B 22 38.904 24.746 121.072 1.00 89.16 C ANISOU 3160 CA VAL B 22 13076 10660 10138 -74 463 1518 C ATOM 3161 C VAL B 22 38.604 24.907 122.577 1.00 88.75 C ANISOU 3161 C VAL B 22 13060 10378 10283 72 470 1518 C ATOM 3162 O VAL B 22 37.438 24.871 122.986 1.00 88.50 O ANISOU 3162 O VAL B 22 12988 10352 10285 95 427 1589 O ATOM 3163 CB VAL B 22 39.174 23.262 120.721 1.00 88.90 C ANISOU 3163 CB VAL B 22 13092 10679 10007 -188 507 1275 C ATOM 3164 CG1 VAL B 22 38.015 22.377 121.170 1.00 88.52 C ANISOU 3164 CG1 VAL B 22 13040 10631 9961 -211 477 1223 C ATOM 3165 CG2 VAL B 22 39.385 23.093 119.221 1.00 90.40 C ANISOU 3165 CG2 VAL B 22 13240 11123 9982 -365 515 1250 C ATOM 3166 N SER B 23 39.648 25.094 123.386 1.00 89.00 N ANISOU 3166 N SER B 23 13155 10227 10431 155 525 1441 N ATOM 3167 CA SER B 23 39.512 25.186 124.848 1.00 88.50 C ANISOU 3167 CA SER B 23 13126 9969 10527 261 541 1417 C ATOM 3168 C SER B 23 38.719 26.407 125.353 1.00 89.00 C ANISOU 3168 C SER B 23 13137 9973 10703 343 529 1589 C ATOM 3169 O SER B 23 37.748 26.249 126.102 1.00 89.39 O ANISOU 3169 O SER B 23 13170 9976 10816 378 513 1602 O ATOM 3170 CB SER B 23 40.898 25.177 125.503 1.00 87.90 C ANISOU 3170 CB SER B 23 13114 9754 10527 306 599 1312 C ATOM 3171 OG SER B 23 40.809 25.260 126.917 1.00 87.36 O ANISOU 3171 OG SER B 23 13073 9534 10586 379 613 1290 O ATOM 3172 N VAL B 24 39.137 27.608 124.946 1.00 89.36 N ANISOU 3172 N VAL B 24 13154 10011 10786 370 549 1718 N ATOM 3173 CA VAL B 24 38.596 28.860 125.506 1.00 89.79 C ANISOU 3173 CA VAL B 24 13161 9953 11000 458 575 1864 C ATOM 3174 C VAL B 24 37.086 29.032 125.261 1.00 90.88 C ANISOU 3174 C VAL B 24 13200 10171 11157 470 524 2019 C ATOM 3175 O VAL B 24 36.346 29.289 126.217 1.00 91.35 O ANISOU 3175 O VAL B 24 13241 10117 11351 539 549 2028 O ATOM 3176 CB VAL B 24 39.395 30.109 125.027 1.00 90.27 C ANISOU 3176 CB VAL B 24 13206 9977 11112 478 616 1980 C ATOM 3177 CG1 VAL B 24 38.706 31.412 125.430 1.00 90.54 C ANISOU 3177 CG1 VAL B 24 13173 9888 11338 564 658 2147 C ATOM 3178 CG2 VAL B 24 40.819 30.075 125.582 1.00 89.41 C ANISOU 3178 CG2 VAL B 24 13188 9762 11021 480 677 1828 C ATOM 3179 N PRO B 25 36.619 28.882 124.002 1.00 91.58 N ANISOU 3179 N PRO B 25 13217 10471 11107 393 455 2139 N ATOM 3180 CA PRO B 25 35.178 29.041 123.758 1.00 91.90 C ANISOU 3180 CA PRO B 25 13142 10611 11161 399 397 2308 C ATOM 3181 C PRO B 25 34.302 28.014 124.482 1.00 90.31 C ANISOU 3181 C PRO B 25 12959 10407 10947 391 375 2187 C ATOM 3182 O PRO B 25 33.259 28.387 125.017 1.00 91.36 O ANISOU 3182 O PRO B 25 13021 10492 11197 457 374 2282 O ATOM 3183 CB PRO B 25 35.050 28.878 122.234 1.00 93.53 C ANISOU 3183 CB PRO B 25 13278 11092 11168 274 321 2430 C ATOM 3184 CG PRO B 25 36.412 29.136 121.704 1.00 93.60 C ANISOU 3184 CG PRO B 25 13346 11100 11115 236 357 2380 C ATOM 3185 CD PRO B 25 37.331 28.580 122.750 1.00 92.10 C ANISOU 3185 CD PRO B 25 13287 10715 10989 282 428 2130 C ATOM 3186 N GLY B 26 34.730 26.751 124.501 1.00 87.81 N ANISOU 3186 N GLY B 26 12729 10130 10505 312 369 1981 N ATOM 3187 CA GLY B 26 33.986 25.675 125.168 1.00 86.07 C ANISOU 3187 CA GLY B 26 12533 9900 10268 290 351 1859 C ATOM 3188 C GLY B 26 33.713 25.945 126.639 1.00 83.64 C ANISOU 3188 C GLY B 26 12250 9393 10136 394 396 1819 C ATOM 3189 O GLY B 26 32.572 25.845 127.102 1.00 83.29 O ANISOU 3189 O GLY B 26 12153 9358 10136 413 375 1861 O ATOM 3190 N ASN B 27 34.766 26.311 127.362 1.00 81.89 N ANISOU 3190 N ASN B 27 12101 9008 10003 448 460 1738 N ATOM 3191 CA ASN B 27 34.663 26.585 128.799 1.00 80.94 C ANISOU 3191 CA ASN B 27 12008 8718 10026 515 515 1678 C ATOM 3192 C ASN B 27 33.948 27.906 129.103 1.00 81.80 C ANISOU 3192 C ASN B 27 12033 8752 10296 596 560 1822 C ATOM 3193 O ASN B 27 33.187 27.988 130.075 1.00 81.76 O ANISOU 3193 O ASN B 27 12006 8672 10387 630 592 1796 O ATOM 3194 CB ASN B 27 36.042 26.536 129.457 1.00 79.51 C ANISOU 3194 CB ASN B 27 11918 8420 9871 521 567 1550 C ATOM 3195 CG ASN B 27 36.609 25.134 129.503 1.00 78.26 C ANISOU 3195 CG ASN B 27 11828 8288 9618 462 539 1405 C ATOM 3196 OD1 ASN B 27 36.091 24.268 130.213 1.00 77.97 O ANISOU 3196 OD1 ASN B 27 11807 8235 9582 443 520 1335 O ATOM 3197 ND2 ASN B 27 37.679 24.902 128.751 1.00 77.70 N ANISOU 3197 ND2 ASN B 27 11790 8251 9479 431 545 1363 N ATOM 3198 N VAL B 28 34.170 28.924 128.269 1.00 82.91 N ANISOU 3198 N VAL B 28 12119 8907 10475 625 572 1974 N ATOM 3199 CA VAL B 28 33.357 30.152 128.330 1.00 84.56 C ANISOU 3199 CA VAL B 28 12220 9045 10862 707 616 2150 C ATOM 3200 C VAL B 28 31.874 29.802 128.148 1.00 85.59 C ANISOU 3200 C VAL B 28 12245 9288 10984 709 556 2253 C ATOM 3201 O VAL B 28 31.023 30.316 128.874 1.00 86.71 O ANISOU 3201 O VAL B 28 12321 9333 11291 777 610 2292 O ATOM 3202 CB VAL B 28 33.807 31.216 127.288 1.00 85.21 C ANISOU 3202 CB VAL B 28 12245 9146 10983 728 623 2339 C ATOM 3203 CG1 VAL B 28 32.793 32.353 127.162 1.00 86.35 C ANISOU 3203 CG1 VAL B 28 12246 9234 11329 816 656 2568 C ATOM 3204 CG2 VAL B 28 35.174 31.784 127.660 1.00 84.60 C ANISOU 3204 CG2 VAL B 28 12260 8925 10958 737 705 2242 C ATOM 3205 N LEU B 29 31.584 28.914 127.197 1.00 85.76 N ANISOU 3205 N LEU B 29 12248 9520 10813 622 454 2281 N ATOM 3206 CA LEU B 29 30.220 28.434 126.956 1.00 86.80 C ANISOU 3206 CA LEU B 29 12282 9798 10897 594 385 2366 C ATOM 3207 C LEU B 29 29.679 27.620 128.143 1.00 85.87 C ANISOU 3207 C LEU B 29 12214 9610 10800 593 403 2196 C ATOM 3208 O LEU B 29 28.491 27.729 128.474 1.00 86.45 O ANISOU 3208 O LEU B 29 12194 9703 10949 625 397 2272 O ATOM 3209 CB LEU B 29 30.159 27.607 125.665 1.00 87.88 C ANISOU 3209 CB LEU B 29 12401 10193 10794 464 284 2397 C ATOM 3210 CG LEU B 29 28.788 27.462 125.001 1.00 89.80 C ANISOU 3210 CG LEU B 29 12499 10651 10970 416 199 2573 C ATOM 3211 CD1 LEU B 29 28.381 28.753 124.298 1.00 91.57 C ANISOU 3211 CD1 LEU B 29 12565 10927 11300 478 182 2881 C ATOM 3212 CD2 LEU B 29 28.801 26.299 124.019 1.00 90.28 C ANISOU 3212 CD2 LEU B 29 12583 10957 10761 243 121 2494 C ATOM 3213 N VAL B 30 30.540 26.813 128.772 1.00 84.54 N ANISOU 3213 N VAL B 30 12180 9368 10571 554 423 1984 N ATOM 3214 CA VAL B 30 30.177 26.110 130.017 1.00 83.50 C ANISOU 3214 CA VAL B 30 12099 9156 10469 548 444 1835 C ATOM 3215 C VAL B 30 29.834 27.098 131.137 1.00 83.68 C ANISOU 3215 C VAL B 30 12086 9017 10689 635 538 1845 C ATOM 3216 O VAL B 30 28.813 26.932 131.812 1.00 83.63 O ANISOU 3216 O VAL B 30 12031 9007 10734 643 548 1834 O ATOM 3217 CB VAL B 30 31.289 25.135 130.492 1.00 82.63 C ANISOU 3217 CB VAL B 30 12123 8990 10281 496 449 1643 C ATOM 3218 CG1 VAL B 30 31.050 24.644 131.922 1.00 82.31 C ANISOU 3218 CG1 VAL B 30 12125 8853 10293 492 478 1523 C ATOM 3219 CG2 VAL B 30 31.378 23.939 129.557 1.00 83.16 C ANISOU 3219 CG2 VAL B 30 12220 9198 10178 398 381 1590 C ATOM 3220 N ILE B 31 30.684 28.111 131.328 1.00 83.61 N ANISOU 3220 N ILE B 31 12100 8878 10790 686 618 1852 N ATOM 3221 CA ILE B 31 30.452 29.131 132.370 1.00 84.16 C ANISOU 3221 CA ILE B 31 12137 8779 11058 750 738 1833 C ATOM 3222 C ILE B 31 29.180 29.935 132.069 1.00 86.54 C ANISOU 3222 C ILE B 31 12287 9081 11513 826 763 2012 C ATOM 3223 O ILE B 31 28.404 30.233 132.981 1.00 87.26 O ANISOU 3223 O ILE B 31 12327 9089 11737 858 841 1972 O ATOM 3224 CB ILE B 31 31.664 30.080 132.540 1.00 83.73 C ANISOU 3224 CB ILE B 31 12137 8587 11088 772 828 1800 C ATOM 3225 CG1 ILE B 31 32.887 29.306 133.054 1.00 82.45 C ANISOU 3225 CG1 ILE B 31 12105 8422 10798 700 812 1626 C ATOM 3226 CG2 ILE B 31 31.349 31.214 133.518 1.00 84.45 C ANISOU 3226 CG2 ILE B 31 12185 8502 11399 822 976 1770 C ATOM 3227 CD1 ILE B 31 34.209 29.987 132.760 1.00 82.49 C ANISOU 3227 CD1 ILE B 31 12162 8362 10817 703 856 1620 C ATOM 3228 N TRP B 32 28.987 30.278 130.794 1.00 88.41 N ANISOU 3228 N TRP B 32 12440 9420 11732 849 700 2214 N ATOM 3229 CA TRP B 32 27.750 30.908 130.297 1.00 91.00 C ANISOU 3229 CA TRP B 32 12594 9793 12187 917 692 2440 C ATOM 3230 C TRP B 32 26.533 30.046 130.646 1.00 91.54 C ANISOU 3230 C TRP B 32 12611 9973 12196 886 638 2412 C ATOM 3231 O TRP B 32 25.588 30.524 131.283 1.00 93.10 O ANISOU 3231 O TRP B 32 12710 10093 12570 952 710 2447 O ATOM 3232 CB TRP B 32 27.837 31.091 128.770 1.00 92.56 C ANISOU 3232 CB TRP B 32 12718 10159 12290 899 592 2665 C ATOM 3233 CG TRP B 32 26.922 32.114 128.157 1.00 94.48 C ANISOU 3233 CG TRP B 32 12766 10418 12711 986 596 2962 C ATOM 3234 CD1 TRP B 32 25.620 32.384 128.485 1.00 95.53 C ANISOU 3234 CD1 TRP B 32 12754 10542 13002 1054 620 3074 C ATOM 3235 CD2 TRP B 32 27.244 32.975 127.062 1.00 95.70 C ANISOU 3235 CD2 TRP B 32 12837 10614 12908 1011 571 3208 C ATOM 3236 NE1 TRP B 32 25.124 33.374 127.675 1.00 97.82 N ANISOU 3236 NE1 TRP B 32 12865 10852 13450 1130 613 3387 N ATOM 3237 CE2 TRP B 32 26.098 33.753 126.790 1.00 97.89 C ANISOU 3237 CE2 TRP B 32 12908 10895 13387 1102 579 3482 C ATOM 3238 CE3 TRP B 32 28.396 33.170 126.288 1.00 95.59 C ANISOU 3238 CE3 TRP B 32 12894 10638 12788 963 544 3233 C ATOM 3239 CZ2 TRP B 32 26.068 34.715 125.772 1.00 99.92 C ANISOU 3239 CZ2 TRP B 32 13025 11193 13746 1146 554 3801 C ATOM 3240 CZ3 TRP B 32 28.370 34.128 125.280 1.00 97.54 C ANISOU 3240 CZ3 TRP B 32 13011 10930 13116 996 521 3531 C ATOM 3241 CH2 TRP B 32 27.211 34.887 125.031 1.00 99.69 C ANISOU 3241 CH2 TRP B 32 13076 11207 13594 1087 522 3822 C ATOM 3242 N ALA B 33 26.588 28.775 130.243 1.00 90.78 N ANISOU 3242 N ALA B 33 12581 10049 11861 781 526 2336 N ATOM 3243 CA ALA B 33 25.475 27.829 130.415 1.00 90.61 C ANISOU 3243 CA ALA B 33 12517 10161 11750 726 461 2311 C ATOM 3244 C ALA B 33 24.960 27.717 131.851 1.00 89.64 C ANISOU 3244 C ALA B 33 12411 9913 11735 749 542 2167 C ATOM 3245 O ALA B 33 23.754 27.610 132.061 1.00 89.26 O ANISOU 3245 O ALA B 33 12258 9926 11731 759 533 2224 O ATOM 3246 CB ALA B 33 25.869 26.452 129.898 1.00 90.00 C ANISOU 3246 CB ALA B 33 12541 10235 11419 597 362 2196 C ATOM 3247 N VAL B 34 25.869 27.743 132.824 1.00 89.40 N ANISOU 3247 N VAL B 34 12502 9728 11735 742 620 1986 N ATOM 3248 CA VAL B 34 25.486 27.666 134.237 1.00 90.33 C ANISOU 3248 CA VAL B 34 12639 9748 11932 735 704 1838 C ATOM 3249 C VAL B 34 24.849 28.975 134.710 1.00 92.99 C ANISOU 3249 C VAL B 34 12857 9949 12525 834 839 1903 C ATOM 3250 O VAL B 34 23.887 28.944 135.479 1.00 94.48 O ANISOU 3250 O VAL B 34 12980 10126 12790 837 891 1860 O ATOM 3251 CB VAL B 34 26.685 27.287 135.145 1.00 88.80 C ANISOU 3251 CB VAL B 34 12598 9465 11676 675 741 1640 C ATOM 3252 CG1 VAL B 34 26.298 27.314 136.622 1.00 88.43 C ANISOU 3252 CG1 VAL B 34 12557 9343 11697 644 832 1498 C ATOM 3253 CG2 VAL B 34 27.209 25.907 134.779 1.00 88.20 C ANISOU 3253 CG2 VAL B 34 12622 9496 11392 588 625 1575 C ATOM 3254 N LYS B 35 25.376 30.113 134.255 1.00 94.41 N ANISOU 3254 N LYS B 35 13004 10019 12847 910 907 2002 N ATOM 3255 CA LYS B 35 24.875 31.419 134.693 1.00 96.59 C ANISOU 3255 CA LYS B 35 13166 10122 13409 1008 1064 2055 C ATOM 3256 C LYS B 35 23.435 31.673 134.242 1.00 98.82 C ANISOU 3256 C LYS B 35 13258 10471 13818 1084 1047 2256 C ATOM 3257 O LYS B 35 22.610 32.132 135.036 1.00100.07 O ANISOU 3257 O LYS B 35 13325 10530 14165 1129 1168 2217 O ATOM 3258 CB LYS B 35 25.782 32.554 134.201 1.00 97.83 C ANISOU 3258 CB LYS B 35 13328 10140 13702 1069 1137 2138 C ATOM 3259 CG LYS B 35 25.341 33.933 134.676 1.00100.20 C ANISOU 3259 CG LYS B 35 13515 10221 14336 1168 1329 2177 C ATOM 3260 CD LYS B 35 26.435 34.978 134.539 1.00100.99 C ANISOU 3260 CD LYS B 35 13662 10145 14561 1195 1433 2178 C ATOM 3261 CE LYS B 35 25.980 36.302 135.128 1.00103.46 C ANISOU 3261 CE LYS B 35 13868 10208 15232 1281 1655 2177 C ATOM 3262 NZ LYS B 35 26.922 37.412 134.817 1.00104.76 N ANISOU 3262 NZ LYS B 35 14056 10194 15554 1316 1759 2223 N ATOM 3263 N VAL B 36 23.150 31.384 132.973 1.00100.20 N ANISOU 3263 N VAL B 36 13362 10823 13885 1087 904 2468 N ATOM 3264 CA VAL B 36 21.807 31.587 132.407 1.00102.28 C ANISOU 3264 CA VAL B 36 13423 11196 14243 1147 861 2702 C ATOM 3265 C VAL B 36 20.767 30.579 132.926 1.00101.53 C ANISOU 3265 C VAL B 36 13302 11234 14037 1085 809 2615 C ATOM 3266 O VAL B 36 19.639 30.964 133.231 1.00102.75 O ANISOU 3266 O VAL B 36 13301 11372 14367 1151 867 2700 O ATOM 3267 CB VAL B 36 21.829 31.613 130.850 1.00103.52 C ANISOU 3267 CB VAL B 36 13497 11544 14290 1140 716 2972 C ATOM 3268 CG1 VAL B 36 22.126 30.240 130.248 1.00102.30 C ANISOU 3268 CG1 VAL B 36 13452 11628 13786 993 554 2893 C ATOM 3269 CG2 VAL B 36 20.519 32.170 130.300 1.00106.21 C ANISOU 3269 CG2 VAL B 36 13591 11970 14794 1223 695 3268 C ATOM 3270 N ASN B 37 21.153 29.308 133.043 1.00 99.68 N ANISOU 3270 N ASN B 37 13216 11121 13535 959 711 2449 N ATOM 3271 CA ASN B 37 20.227 28.225 133.391 1.00 99.20 C ANISOU 3271 CA ASN B 37 13143 11206 13340 879 642 2379 C ATOM 3272 C ASN B 37 20.107 28.049 134.910 1.00 98.52 C ANISOU 3272 C ASN B 37 13124 10992 13316 856 753 2149 C ATOM 3273 O ASN B 37 21.088 27.729 135.581 1.00 97.06 O ANISOU 3273 O ASN B 37 13098 10722 13057 799 783 1960 O ATOM 3274 CB ASN B 37 20.701 26.917 132.739 1.00 97.83 C ANISOU 3274 CB ASN B 37 13092 11210 12869 746 495 2315 C ATOM 3275 CG ASN B 37 19.623 25.845 132.689 1.00 98.22 C ANISOU 3275 CG ASN B 37 13095 11449 12774 654 404 2308 C ATOM 3276 OD1 ASN B 37 18.562 25.968 133.304 1.00 99.26 O ANISOU 3276 OD1 ASN B 37 13122 11582 13008 683 446 2324 O ATOM 3277 ND2 ASN B 37 19.898 24.779 131.944 1.00 97.97 N ANISOU 3277 ND2 ASN B 37 13140 11576 12505 534 290 2272 N ATOM 3278 N GLN B 38 18.900 28.253 135.439 1.00100.23 N ANISOU 3278 N GLN B 38 13206 11213 13662 892 812 2175 N ATOM 3279 CA GLN B 38 18.629 28.061 136.873 1.00100.38 C ANISOU 3279 CA GLN B 38 13267 11149 13723 848 918 1961 C ATOM 3280 C GLN B 38 18.572 26.584 137.291 1.00 99.06 C ANISOU 3280 C GLN B 38 13217 11118 13303 706 813 1819 C ATOM 3281 O GLN B 38 18.782 26.270 138.463 1.00 98.74 O ANISOU 3281 O GLN B 38 13261 11018 13234 636 876 1628 O ATOM 3282 CB GLN B 38 17.330 28.777 137.277 1.00102.75 C ANISOU 3282 CB GLN B 38 13371 11408 14259 932 1031 2031 C ATOM 3283 CG GLN B 38 16.046 28.122 136.777 1.00103.93 C ANISOU 3283 CG GLN B 38 13387 11768 14332 913 917 2170 C ATOM 3284 CD GLN B 38 14.872 29.087 136.668 1.00106.44 C ANISOU 3284 CD GLN B 38 13461 12051 14929 1043 1009 2350 C ATOM 3285 OE1 GLN B 38 14.799 30.097 137.374 1.00107.36 O ANISOU 3285 OE1 GLN B 38 13514 11963 15313 1129 1197 2293 O ATOM 3286 NE2 GLN B 38 13.944 28.774 135.777 1.00107.67 N ANISOU 3286 NE2 GLN B 38 13468 12410 15029 1049 883 2568 N ATOM 3287 N ALA B 39 18.283 25.689 136.340 1.00 99.05 N ANISOU 3287 N ALA B 39 13212 11301 13120 650 658 1915 N ATOM 3288 CA ALA B 39 18.315 24.234 136.583 1.00 97.40 C ANISOU 3288 CA ALA B 39 13119 11201 12684 512 560 1790 C ATOM 3289 C ALA B 39 19.715 23.697 136.906 1.00 95.63 C ANISOU 3289 C ALA B 39 13088 10894 12352 451 548 1640 C ATOM 3290 O ALA B 39 19.842 22.612 137.474 1.00 94.65 O ANISOU 3290 O ALA B 39 13062 10799 12099 348 506 1518 O ATOM 3291 CB ALA B 39 17.737 23.483 135.391 1.00 97.73 C ANISOU 3291 CB ALA B 39 13109 11454 12569 453 419 1915 C ATOM 3292 N LEU B 40 20.751 24.452 136.527 1.00 95.93 N ANISOU 3292 N LEU B 40 13168 10829 12449 515 585 1665 N ATOM 3293 CA LEU B 40 22.139 24.154 136.881 1.00 95.30 C ANISOU 3293 CA LEU B 40 13247 10659 12300 474 591 1538 C ATOM 3294 C LEU B 40 22.650 25.007 138.062 1.00 95.73 C ANISOU 3294 C LEU B 40 13329 10554 12487 497 729 1427 C ATOM 3295 O LEU B 40 23.839 25.331 138.118 1.00 95.20 O ANISOU 3295 O LEU B 40 13349 10400 12422 503 759 1379 O ATOM 3296 CB LEU B 40 23.038 24.385 135.657 1.00 95.31 C ANISOU 3296 CB LEU B 40 13282 10672 12260 507 540 1626 C ATOM 3297 CG LEU B 40 22.612 23.736 134.337 1.00 95.98 C ANISOU 3297 CG LEU B 40 13327 10935 12206 465 420 1737 C ATOM 3298 CD1 LEU B 40 23.507 24.205 133.198 1.00 96.25 C ANISOU 3298 CD1 LEU B 40 13376 10980 12212 494 395 1825 C ATOM 3299 CD2 LEU B 40 22.635 22.220 134.456 1.00 95.38 C ANISOU 3299 CD2 LEU B 40 13346 10934 11958 343 345 1617 C ATOM 3300 N ARG B 41 21.773 25.351 139.011 1.00 97.52 N ANISOU 3300 N ARG B 41 13481 10756 12815 495 821 1373 N ATOM 3301 CA ARG B 41 22.155 26.178 140.168 1.00 98.78 C ANISOU 3301 CA ARG B 41 13656 10783 13092 486 975 1241 C ATOM 3302 C ARG B 41 22.393 25.278 141.389 1.00 97.58 C ANISOU 3302 C ARG B 41 13596 10675 12803 348 965 1081 C ATOM 3303 O ARG B 41 21.802 25.467 142.454 1.00 97.54 O ANISOU 3303 O ARG B 41 13548 10667 12843 293 1060 979 O ATOM 3304 CB ARG B 41 21.090 27.248 140.433 1.00101.78 C ANISOU 3304 CB ARG B 41 13881 11095 13696 566 1114 1272 C ATOM 3305 CG ARG B 41 21.577 28.408 141.292 1.00103.26 C ANISOU 3305 CG ARG B 41 14068 11113 14051 574 1306 1145 C ATOM 3306 CD ARG B 41 20.529 29.497 141.370 1.00105.91 C ANISOU 3306 CD ARG B 41 14234 11349 14655 675 1459 1192 C ATOM 3307 NE ARG B 41 20.386 30.237 140.114 1.00107.93 N ANISOU 3307 NE ARG B 41 14389 11553 15063 822 1439 1417 N ATOM 3308 CZ ARG B 41 19.532 31.246 139.908 1.00110.78 C ANISOU 3308 CZ ARG B 41 14578 11813 15699 943 1558 1529 C ATOM 3309 NH1 ARG B 41 18.714 31.666 140.876 1.00112.04 N ANISOU 3309 NH1 ARG B 41 14645 11899 16025 940 1725 1411 N ATOM 3310 NH2 ARG B 41 19.495 31.847 138.719 1.00111.75 N ANISOU 3310 NH2 ARG B 41 14608 11910 15939 1066 1516 1770 N ATOM 3311 N ASP B 42 23.296 24.316 141.212 1.00 96.58 N ANISOU 3311 N ASP B 42 13587 10590 12517 287 854 1067 N ATOM 3312 CA ASP B 42 23.553 23.252 142.181 1.00 95.19 C ANISOU 3312 CA ASP B 42 13491 10471 12204 158 807 972 C ATOM 3313 C ASP B 42 25.051 23.196 142.492 1.00 92.95 C ANISOU 3313 C ASP B 42 13313 10137 11864 117 802 922 C ATOM 3314 O ASP B 42 25.876 23.668 141.698 1.00 92.99 O ANISOU 3314 O ASP B 42 13347 10081 11902 189 799 966 O ATOM 3315 CB ASP B 42 23.068 21.909 141.616 1.00 95.56 C ANISOU 3315 CB ASP B 42 13558 10620 12129 121 669 1031 C ATOM 3316 CG ASP B 42 22.567 20.959 142.695 1.00 96.88 C ANISOU 3316 CG ASP B 42 13741 10858 12210 -1 644 964 C ATOM 3317 OD1 ASP B 42 23.205 20.860 143.770 1.00 98.19 O ANISOU 3317 OD1 ASP B 42 13957 11012 12338 -86 675 887 O ATOM 3318 OD2 ASP B 42 21.533 20.298 142.465 1.00 97.70 O ANISOU 3318 OD2 ASP B 42 13802 11046 12274 -26 589 998 O ATOM 3319 N ALA B 43 25.388 22.612 143.641 1.00 90.92 N ANISOU 3319 N ALA B 43 13103 9922 11521 -4 797 842 N ATOM 3320 CA ALA B 43 26.773 22.545 144.126 1.00 88.94 C ANISOU 3320 CA ALA B 43 12929 9650 11212 -62 792 806 C ATOM 3321 C ALA B 43 27.728 21.968 143.084 1.00 87.35 C ANISOU 3321 C ALA B 43 12795 9418 10975 -2 692 884 C ATOM 3322 O ALA B 43 28.778 22.553 142.823 1.00 87.32 O ANISOU 3322 O ALA B 43 12824 9357 10996 31 720 881 O ATOM 3323 CB ALA B 43 26.853 21.736 145.418 1.00 88.59 C ANISOU 3323 CB ALA B 43 12905 9695 11058 -214 764 760 C ATOM 3324 N THR B 44 27.344 20.837 142.486 1.00 85.73 N ANISOU 3324 N THR B 44 12606 9251 10716 0 589 940 N ATOM 3325 CA THR B 44 28.142 20.176 141.441 1.00 84.25 C ANISOU 3325 CA THR B 44 12475 9036 10500 43 511 990 C ATOM 3326 C THR B 44 28.535 21.140 140.322 1.00 82.89 C ANISOU 3326 C THR B 44 12293 8817 10383 147 543 1025 C ATOM 3327 O THR B 44 29.699 21.189 139.923 1.00 81.92 O ANISOU 3327 O THR B 44 12220 8651 10254 170 534 1030 O ATOM 3328 CB THR B 44 27.387 18.972 140.830 1.00 84.32 C ANISOU 3328 CB THR B 44 12487 9092 10457 22 427 1021 C ATOM 3329 OG1 THR B 44 27.126 18.006 141.853 1.00 84.72 O ANISOU 3329 OG1 THR B 44 12550 9173 10463 -77 393 1004 O ATOM 3330 CG2 THR B 44 28.194 18.298 139.711 1.00 83.77 C ANISOU 3330 CG2 THR B 44 12472 8990 10366 51 374 1041 C ATOM 3331 N PHE B 45 27.565 21.913 139.843 1.00 82.33 N ANISOU 3331 N PHE B 45 12148 8760 10373 206 580 1063 N ATOM 3332 CA PHE B 45 27.788 22.826 138.719 1.00 81.74 C ANISOU 3332 CA PHE B 45 12044 8655 10357 301 601 1135 C ATOM 3333 C PHE B 45 28.660 24.012 139.124 1.00 81.02 C ANISOU 3333 C PHE B 45 11964 8467 10350 332 699 1102 C ATOM 3334 O PHE B 45 29.557 24.400 138.369 1.00 81.48 O ANISOU 3334 O PHE B 45 12052 8489 10415 377 696 1137 O ATOM 3335 CB PHE B 45 26.460 23.278 138.112 1.00 82.58 C ANISOU 3335 CB PHE B 45 12043 8812 10518 355 605 1222 C ATOM 3336 CG PHE B 45 25.608 22.134 137.640 1.00 82.91 C ANISOU 3336 CG PHE B 45 12071 8969 10461 306 510 1249 C ATOM 3337 CD1 PHE B 45 26.025 21.335 136.582 1.00 83.18 C ANISOU 3337 CD1 PHE B 45 12151 9058 10394 281 428 1271 C ATOM 3338 CD2 PHE B 45 24.405 21.833 138.271 1.00 83.64 C ANISOU 3338 CD2 PHE B 45 12104 9117 10557 268 512 1236 C ATOM 3339 CE1 PHE B 45 25.256 20.261 136.157 1.00 83.78 C ANISOU 3339 CE1 PHE B 45 12218 9237 10375 213 355 1273 C ATOM 3340 CE2 PHE B 45 23.625 20.768 137.844 1.00 84.01 C ANISOU 3340 CE2 PHE B 45 12139 9272 10507 208 428 1255 C ATOM 3341 CZ PHE B 45 24.051 19.978 136.788 1.00 84.08 C ANISOU 3341 CZ PHE B 45 12198 9330 10416 176 351 1269 C ATOM 3342 N CYS B 46 28.438 24.543 140.328 1.00 79.84 N ANISOU 3342 N CYS B 46 11793 8285 10254 289 792 1021 N ATOM 3343 CA CYS B 46 29.305 25.592 140.890 1.00 79.04 C ANISOU 3343 CA CYS B 46 11710 8099 10219 279 901 955 C ATOM 3344 C CYS B 46 30.798 25.212 140.925 1.00 77.45 C ANISOU 3344 C CYS B 46 11598 7897 9933 239 856 934 C ATOM 3345 O CYS B 46 31.662 26.078 140.781 1.00 77.26 O ANISOU 3345 O CYS B 46 11591 7808 9956 260 918 921 O ATOM 3346 CB CYS B 46 28.828 25.986 142.289 1.00 79.63 C ANISOU 3346 CB CYS B 46 11754 8172 10328 193 1010 838 C ATOM 3347 SG CYS B 46 27.127 26.594 142.324 1.00 81.01 S ANISOU 3347 SG CYS B 46 11805 8327 10646 250 1097 852 S ATOM 3348 N PHE B 47 31.091 23.924 141.109 1.00 76.16 N ANISOU 3348 N PHE B 47 11479 7799 9659 183 753 938 N ATOM 3349 CA PHE B 47 32.461 23.411 140.978 1.00 74.87 C ANISOU 3349 CA PHE B 47 11379 7632 9435 164 700 946 C ATOM 3350 C PHE B 47 32.867 23.243 139.508 1.00 73.67 C ANISOU 3350 C PHE B 47 11248 7460 9284 251 649 1012 C ATOM 3351 O PHE B 47 34.043 23.410 139.170 1.00 73.10 O ANISOU 3351 O PHE B 47 11211 7359 9205 266 650 1015 O ATOM 3352 CB PHE B 47 32.630 22.076 141.710 1.00 74.68 C ANISOU 3352 CB PHE B 47 11378 7665 9329 79 620 947 C ATOM 3353 CG PHE B 47 32.265 22.121 143.173 1.00 75.28 C ANISOU 3353 CG PHE B 47 11430 7800 9371 -35 657 893 C ATOM 3354 CD1 PHE B 47 32.810 23.083 144.024 1.00 75.59 C ANISOU 3354 CD1 PHE B 47 11461 7847 9412 -102 748 824 C ATOM 3355 CD2 PHE B 47 31.388 21.180 143.709 1.00 75.57 C ANISOU 3355 CD2 PHE B 47 11451 7898 9365 -96 606 903 C ATOM 3356 CE1 PHE B 47 32.470 23.112 145.372 1.00 75.92 C ANISOU 3356 CE1 PHE B 47 11475 7972 9400 -238 789 759 C ATOM 3357 CE2 PHE B 47 31.046 21.210 145.054 1.00 76.04 C ANISOU 3357 CE2 PHE B 47 11482 8034 9375 -221 639 855 C ATOM 3358 CZ PHE B 47 31.588 22.177 145.886 1.00 76.03 C ANISOU 3358 CZ PHE B 47 11469 8055 9362 -297 733 779 C ATOM 3359 N ILE B 48 31.909 22.897 138.644 1.00 73.51 N ANISOU 3359 N ILE B 48 11199 7472 9258 291 606 1061 N ATOM 3360 CA ILE B 48 32.160 22.810 137.193 1.00 73.71 C ANISOU 3360 CA ILE B 48 11231 7513 9262 346 565 1118 C ATOM 3361 C ILE B 48 32.502 24.185 136.586 1.00 74.01 C ANISOU 3361 C ILE B 48 11243 7508 9370 415 627 1168 C ATOM 3362 O ILE B 48 33.292 24.268 135.634 1.00 74.22 O ANISOU 3362 O ILE B 48 11292 7537 9369 440 609 1198 O ATOM 3363 CB ILE B 48 30.980 22.120 136.451 1.00 74.26 C ANISOU 3363 CB ILE B 48 11264 7665 9287 340 504 1159 C ATOM 3364 CG1 ILE B 48 30.944 20.631 136.817 1.00 73.94 C ANISOU 3364 CG1 ILE B 48 11267 7644 9183 268 444 1108 C ATOM 3365 CG2 ILE B 48 31.086 22.281 134.931 1.00 75.17 C ANISOU 3365 CG2 ILE B 48 11362 7832 9364 373 474 1225 C ATOM 3366 CD1 ILE B 48 29.647 19.928 136.478 1.00 74.63 C ANISOU 3366 CD1 ILE B 48 11318 7813 9225 232 398 1123 C ATOM 3367 N VAL B 49 31.927 25.250 137.147 1.00 73.48 N ANISOU 3367 N VAL B 49 11123 7392 9402 439 711 1172 N ATOM 3368 CA VAL B 49 32.283 26.620 136.768 1.00 73.69 C ANISOU 3368 CA VAL B 49 11123 7341 9532 500 793 1217 C ATOM 3369 C VAL B 49 33.740 26.898 137.158 1.00 72.63 C ANISOU 3369 C VAL B 49 11057 7155 9382 467 830 1149 C ATOM 3370 O VAL B 49 34.520 27.388 136.334 1.00 73.41 O ANISOU 3370 O VAL B 49 11171 7232 9488 504 834 1196 O ATOM 3371 CB VAL B 49 31.338 27.668 137.417 1.00 74.90 C ANISOU 3371 CB VAL B 49 11199 7424 9834 528 904 1214 C ATOM 3372 CG1 VAL B 49 31.823 29.097 137.159 1.00 75.29 C ANISOU 3372 CG1 VAL B 49 11226 7356 10024 584 1012 1249 C ATOM 3373 CG2 VAL B 49 29.909 27.499 136.905 1.00 75.87 C ANISOU 3373 CG2 VAL B 49 11231 7607 9987 573 865 1312 C ATOM 3374 N SER B 50 34.098 26.576 138.404 1.00 71.14 N ANISOU 3374 N SER B 50 10901 6968 9160 386 852 1048 N ATOM 3375 CA SER B 50 35.474 26.735 138.892 1.00 70.32 C ANISOU 3375 CA SER B 50 10847 6847 9021 334 876 991 C ATOM 3376 C SER B 50 36.460 25.928 138.051 1.00 69.56 C ANISOU 3376 C SER B 50 10795 6784 8849 353 787 1030 C ATOM 3377 O SER B 50 37.531 26.427 137.689 1.00 69.39 O ANISOU 3377 O SER B 50 10796 6736 8830 364 811 1033 O ATOM 3378 CB SER B 50 35.580 26.327 140.366 1.00 69.99 C ANISOU 3378 CB SER B 50 10814 6849 8927 221 890 904 C ATOM 3379 OG SER B 50 36.922 26.384 140.823 1.00 70.06 O ANISOU 3379 OG SER B 50 10857 6875 8886 158 896 872 O ATOM 3380 N LEU B 51 36.083 24.689 137.739 1.00 69.49 N ANISOU 3380 N LEU B 51 10794 6828 8780 352 698 1050 N ATOM 3381 CA LEU B 51 36.883 23.822 136.869 1.00 68.95 C ANISOU 3381 CA LEU B 51 10758 6780 8660 368 634 1066 C ATOM 3382 C LEU B 51 37.002 24.378 135.440 1.00 69.12 C ANISOU 3382 C LEU B 51 10772 6807 8682 427 639 1119 C ATOM 3383 O LEU B 51 38.072 24.288 134.829 1.00 69.17 O ANISOU 3383 O LEU B 51 10805 6812 8663 435 634 1115 O ATOM 3384 CB LEU B 51 36.301 22.402 136.855 1.00 68.48 C ANISOU 3384 CB LEU B 51 10704 6756 8558 342 562 1060 C ATOM 3385 CG LEU B 51 37.010 21.318 136.038 1.00 68.34 C ANISOU 3385 CG LEU B 51 10714 6739 8511 346 519 1050 C ATOM 3386 CD1 LEU B 51 38.498 21.238 136.340 1.00 67.91 C ANISOU 3386 CD1 LEU B 51 10677 6648 8474 344 531 1039 C ATOM 3387 CD2 LEU B 51 36.346 19.975 136.299 1.00 68.50 C ANISOU 3387 CD2 LEU B 51 10738 6768 8520 306 470 1034 C ATOM 3388 N ALA B 52 35.913 24.953 134.923 1.00 69.43 N ANISOU 3388 N ALA B 52 10764 6863 8750 462 647 1180 N ATOM 3389 CA ALA B 52 35.920 25.603 133.603 1.00 69.73 C ANISOU 3389 CA ALA B 52 10776 6932 8787 506 646 1267 C ATOM 3390 C ALA B 52 36.828 26.835 133.579 1.00 69.88 C ANISOU 3390 C ALA B 52 10801 6878 8870 533 718 1287 C ATOM 3391 O ALA B 52 37.633 26.991 132.659 1.00 69.78 O ANISOU 3391 O ALA B 52 10804 6890 8819 540 708 1317 O ATOM 3392 CB ALA B 52 34.509 25.981 133.182 1.00 70.26 C ANISOU 3392 CB ALA B 52 10766 7042 8887 536 635 1362 C ATOM 3393 N VAL B 53 36.702 27.683 134.604 1.00 70.03 N ANISOU 3393 N VAL B 53 10810 6813 8985 534 799 1256 N ATOM 3394 CA VAL B 53 37.551 28.880 134.779 1.00 70.26 C ANISOU 3394 CA VAL B 53 10850 6756 9089 539 890 1248 C ATOM 3395 C VAL B 53 39.045 28.534 134.692 1.00 70.20 C ANISOU 3395 C VAL B 53 10901 6769 9003 503 870 1197 C ATOM 3396 O VAL B 53 39.811 29.214 133.996 1.00 69.89 O ANISOU 3396 O VAL B 53 10869 6710 8975 521 896 1236 O ATOM 3397 CB VAL B 53 37.246 29.594 136.127 1.00 70.22 C ANISOU 3397 CB VAL B 53 10834 6667 9180 505 996 1165 C ATOM 3398 CG1 VAL B 53 38.301 30.646 136.473 1.00 70.44 C ANISOU 3398 CG1 VAL B 53 10886 6614 9261 473 1096 1115 C ATOM 3399 CG2 VAL B 53 35.856 30.226 136.097 1.00 71.21 C ANISOU 3399 CG2 VAL B 53 10882 6743 9431 559 1048 1225 C ATOM 3400 N ALA B 54 39.442 27.475 135.398 1.00 70.29 N ANISOU 3400 N ALA B 54 10942 6819 8944 454 824 1125 N ATOM 3401 CA ALA B 54 40.816 26.958 135.333 1.00 70.32 C ANISOU 3401 CA ALA B 54 10981 6848 8888 428 798 1093 C ATOM 3402 C ALA B 54 41.231 26.564 133.908 1.00 70.53 C ANISOU 3402 C ALA B 54 11014 6916 8867 465 755 1133 C ATOM 3403 O ALA B 54 42.351 26.867 133.480 1.00 70.39 O ANISOU 3403 O ALA B 54 11010 6898 8834 463 774 1130 O ATOM 3404 CB ALA B 54 40.984 25.774 136.279 1.00 70.02 C ANISOU 3404 CB ALA B 54 10950 6843 8809 379 748 1048 C ATOM 3405 N ASP B 55 40.328 25.906 133.180 1.00 70.81 N ANISOU 3405 N ASP B 55 11035 7000 8868 481 704 1162 N ATOM 3406 CA ASP B 55 40.600 25.504 131.794 1.00 71.61 C ANISOU 3406 CA ASP B 55 11137 7168 8901 485 673 1182 C ATOM 3407 C ASP B 55 40.660 26.706 130.828 1.00 71.82 C ANISOU 3407 C ASP B 55 11139 7214 8934 507 700 1274 C ATOM 3408 O ASP B 55 41.500 26.725 129.917 1.00 71.35 O ANISOU 3408 O ASP B 55 11089 7200 8820 494 701 1276 O ATOM 3409 CB ASP B 55 39.581 24.455 131.312 1.00 72.15 C ANISOU 3409 CB ASP B 55 11192 7303 8915 465 617 1175 C ATOM 3410 CG ASP B 55 39.696 23.109 132.056 1.00 71.72 C ANISOU 3410 CG ASP B 55 11163 7221 8864 438 592 1091 C ATOM 3411 OD1 ASP B 55 40.789 22.768 132.566 1.00 71.11 O ANISOU 3411 OD1 ASP B 55 11106 7098 8815 437 606 1049 O ATOM 3412 OD2 ASP B 55 38.679 22.376 132.116 1.00 71.68 O ANISOU 3412 OD2 ASP B 55 11149 7244 8842 417 556 1082 O ATOM 3413 N VAL B 56 39.803 27.710 131.043 1.00 72.18 N ANISOU 3413 N VAL B 56 11145 7220 9057 539 729 1354 N ATOM 3414 CA VAL B 56 39.872 28.971 130.275 1.00 73.42 C ANISOU 3414 CA VAL B 56 11268 7366 9262 568 765 1471 C ATOM 3415 C VAL B 56 41.244 29.614 130.470 1.00 73.37 C ANISOU 3415 C VAL B 56 11302 7297 9278 557 824 1431 C ATOM 3416 O VAL B 56 41.852 30.092 129.511 1.00 73.78 O ANISOU 3416 O VAL B 56 11349 7385 9300 553 828 1493 O ATOM 3417 CB VAL B 56 38.776 30.002 130.678 1.00 74.26 C ANISOU 3417 CB VAL B 56 11313 7392 9507 617 815 1562 C ATOM 3418 CG1 VAL B 56 38.984 31.343 129.969 1.00 74.95 C ANISOU 3418 CG1 VAL B 56 11360 7434 9683 652 865 1699 C ATOM 3419 CG2 VAL B 56 37.378 29.474 130.374 1.00 74.64 C ANISOU 3419 CG2 VAL B 56 11303 7522 9535 629 753 1630 C ATOM 3420 N ALA B 57 41.717 29.620 131.716 1.00 73.22 N ANISOU 3420 N ALA B 57 11316 7203 9299 537 868 1330 N ATOM 3421 CA ALA B 57 43.034 30.170 132.048 1.00 73.03 C ANISOU 3421 CA ALA B 57 11324 7138 9284 507 923 1281 C ATOM 3422 C ALA B 57 44.190 29.443 131.357 1.00 72.85 C ANISOU 3422 C ALA B 57 11325 7192 9163 488 881 1251 C ATOM 3423 O ALA B 57 45.177 30.082 131.011 1.00 72.82 O ANISOU 3423 O ALA B 57 11330 7181 9155 474 918 1259 O ATOM 3424 CB ALA B 57 43.247 30.184 133.556 1.00 72.46 C ANISOU 3424 CB ALA B 57 11270 7017 9244 460 967 1181 C ATOM 3425 N VAL B 58 44.071 28.129 131.151 1.00 72.40 N ANISOU 3425 N VAL B 58 11270 7197 9038 485 817 1209 N ATOM 3426 CA VAL B 58 45.109 27.358 130.440 1.00 72.24 C ANISOU 3426 CA VAL B 58 11261 7236 8950 470 798 1164 C ATOM 3427 C VAL B 58 45.216 27.844 128.985 1.00 73.40 C ANISOU 3427 C VAL B 58 11395 7454 9039 464 800 1227 C ATOM 3428 O VAL B 58 46.303 28.260 128.523 1.00 73.57 O ANISOU 3428 O VAL B 58 11422 7492 9038 448 831 1224 O ATOM 3429 CB VAL B 58 44.833 25.831 130.497 1.00 71.54 C ANISOU 3429 CB VAL B 58 11173 7173 8834 464 750 1100 C ATOM 3430 CG1 VAL B 58 45.797 25.043 129.612 1.00 71.57 C ANISOU 3430 CG1 VAL B 58 11177 7222 8794 450 757 1041 C ATOM 3431 CG2 VAL B 58 44.913 25.327 131.933 1.00 71.14 C ANISOU 3431 CG2 VAL B 58 11125 7069 8834 459 741 1064 C ATOM 3432 N GLY B 59 44.075 27.812 128.294 1.00 74.05 N ANISOU 3432 N GLY B 59 11450 7593 9089 465 765 1296 N ATOM 3433 CA GLY B 59 43.970 28.246 126.900 1.00 74.53 C ANISOU 3433 CA GLY B 59 11480 7760 9074 438 751 1386 C ATOM 3434 C GLY B 59 44.243 29.720 126.652 1.00 74.72 C ANISOU 3434 C GLY B 59 11487 7747 9155 455 791 1506 C ATOM 3435 O GLY B 59 44.823 30.074 125.629 1.00 74.83 O ANISOU 3435 O GLY B 59 11488 7841 9101 419 794 1558 O ATOM 3436 N ALA B 60 43.831 30.574 127.588 1.00 74.90 N ANISOU 3436 N ALA B 60 11505 7644 9307 500 833 1545 N ATOM 3437 CA ALA B 60 44.031 32.029 127.480 1.00 75.40 C ANISOU 3437 CA ALA B 60 11550 7627 9469 518 894 1654 C ATOM 3438 C ALA B 60 45.379 32.540 128.011 1.00 74.52 C ANISOU 3438 C ALA B 60 11484 7441 9386 495 963 1573 C ATOM 3439 O ALA B 60 45.853 33.570 127.538 1.00 75.44 O ANISOU 3439 O ALA B 60 11592 7526 9542 487 1008 1655 O ATOM 3440 CB ALA B 60 42.895 32.766 128.174 1.00 76.07 C ANISOU 3440 CB ALA B 60 11597 7597 9707 571 934 1723 C ATOM 3441 N LEU B 61 45.971 31.853 128.995 1.00 72.80 N ANISOU 3441 N LEU B 61 11307 7202 9151 476 969 1430 N ATOM 3442 CA LEU B 61 47.259 32.265 129.597 1.00 71.96 C ANISOU 3442 CA LEU B 61 11230 7053 9055 438 1026 1355 C ATOM 3443 C LEU B 61 48.398 31.256 129.402 1.00 71.09 C ANISOU 3443 C LEU B 61 11132 7030 8845 412 990 1271 C ATOM 3444 O LEU B 61 49.487 31.642 128.970 1.00 70.65 O ANISOU 3444 O LEU B 61 11081 7000 8759 384 1019 1268 O ATOM 3445 CB LEU B 61 47.089 32.569 131.096 1.00 71.60 C ANISOU 3445 CB LEU B 61 11200 6914 9091 418 1080 1278 C ATOM 3446 CG LEU B 61 48.307 33.026 131.911 1.00 71.46 C ANISOU 3446 CG LEU B 61 11203 6875 9074 349 1141 1195 C ATOM 3447 CD1 LEU B 61 48.961 34.269 131.321 1.00 72.17 C ANISOU 3447 CD1 LEU B 61 11299 6916 9206 329 1214 1246 C ATOM 3448 CD2 LEU B 61 47.892 33.270 133.354 1.00 71.40 C ANISOU 3448 CD2 LEU B 61 11200 6806 9122 303 1195 1115 C ATOM 3449 N VAL B 62 48.160 29.981 129.726 1.00 70.60 N ANISOU 3449 N VAL B 62 11069 7003 8750 422 938 1207 N ATOM 3450 CA VAL B 62 49.243 28.978 129.740 1.00 69.95 C ANISOU 3450 CA VAL B 62 10983 6970 8624 410 921 1129 C ATOM 3451 C VAL B 62 49.764 28.690 128.333 1.00 70.07 C ANISOU 3451 C VAL B 62 10987 7068 8565 401 920 1128 C ATOM 3452 O VAL B 62 50.977 28.667 128.121 1.00 69.69 O ANISOU 3452 O VAL B 62 10931 7049 8498 382 947 1091 O ATOM 3453 CB VAL B 62 48.827 27.658 130.445 1.00 69.37 C ANISOU 3453 CB VAL B 62 10902 6889 8564 425 875 1077 C ATOM 3454 CG1 VAL B 62 49.900 26.582 130.305 1.00 69.19 C ANISOU 3454 CG1 VAL B 62 10857 6896 8536 428 869 1018 C ATOM 3455 CG2 VAL B 62 48.541 27.920 131.914 1.00 69.11 C ANISOU 3455 CG2 VAL B 62 10872 6805 8580 407 880 1070 C ATOM 3456 N ILE B 63 48.853 28.481 127.383 1.00 70.16 N ANISOU 3456 N ILE B 63 10993 7137 8526 399 891 1165 N ATOM 3457 CA ILE B 63 49.250 28.136 126.008 1.00 70.74 C ANISOU 3457 CA ILE B 63 11052 7323 8503 359 894 1148 C ATOM 3458 C ILE B 63 49.967 29.289 125.267 1.00 70.52 C ANISOU 3458 C ILE B 63 11018 7337 8438 327 927 1220 C ATOM 3459 O ILE B 63 50.976 29.044 124.597 1.00 71.24 O ANISOU 3459 O ILE B 63 11100 7497 8470 290 956 1163 O ATOM 3460 CB ILE B 63 48.067 27.532 125.208 1.00 71.94 C ANISOU 3460 CB ILE B 63 11190 7561 8583 334 851 1163 C ATOM 3461 CG1 ILE B 63 47.734 26.139 125.772 1.00 72.07 C ANISOU 3461 CG1 ILE B 63 11214 7539 8629 349 836 1054 C ATOM 3462 CG2 ILE B 63 48.398 27.421 123.725 1.00 73.01 C ANISOU 3462 CG2 ILE B 63 11304 7846 8590 258 862 1155 C ATOM 3463 CD1 ILE B 63 46.447 25.519 125.260 1.00 72.63 C ANISOU 3463 CD1 ILE B 63 11275 7680 8641 318 795 1058 C ATOM 3464 N PRO B 64 49.458 30.535 125.378 1.00 69.67 N ANISOU 3464 N PRO B 64 10910 7182 8380 339 934 1345 N ATOM 3465 CA PRO B 64 50.192 31.706 124.880 1.00 69.53 C ANISOU 3465 CA PRO B 64 10889 7170 8360 310 975 1424 C ATOM 3466 C PRO B 64 51.596 31.892 125.463 1.00 68.75 C ANISOU 3466 C PRO B 64 10808 7029 8283 296 1026 1340 C ATOM 3467 O PRO B 64 52.529 32.158 124.712 1.00 69.45 O ANISOU 3467 O PRO B 64 10889 7188 8311 252 1050 1342 O ATOM 3468 CB PRO B 64 49.293 32.866 125.289 1.00 69.85 C ANISOU 3468 CB PRO B 64 10921 7103 8513 345 991 1553 C ATOM 3469 CG PRO B 64 47.931 32.295 125.192 1.00 70.02 C ANISOU 3469 CG PRO B 64 10919 7156 8529 373 933 1592 C ATOM 3470 CD PRO B 64 48.051 30.877 125.667 1.00 69.50 C ANISOU 3470 CD PRO B 64 10875 7115 8416 375 906 1438 C ATOM 3471 N LEU B 65 51.736 31.763 126.779 1.00 67.78 N ANISOU 3471 N LEU B 65 10702 6815 8237 318 1040 1274 N ATOM 3472 CA LEU B 65 53.055 31.830 127.437 1.00 67.64 C ANISOU 3472 CA LEU B 65 10685 6786 8228 291 1077 1202 C ATOM 3473 C LEU B 65 54.041 30.807 126.872 1.00 67.91 C ANISOU 3473 C LEU B 65 10692 6912 8198 284 1069 1124 C ATOM 3474 O LEU B 65 55.213 31.125 126.653 1.00 68.14 O ANISOU 3474 O LEU B 65 10706 6979 8203 250 1106 1105 O ATOM 3475 CB LEU B 65 52.928 31.626 128.955 1.00 66.91 C ANISOU 3475 CB LEU B 65 10599 6624 8200 295 1077 1149 C ATOM 3476 CG LEU B 65 52.431 32.826 129.766 1.00 66.99 C ANISOU 3476 CG LEU B 65 10631 6532 8288 272 1131 1177 C ATOM 3477 CD1 LEU B 65 51.981 32.402 131.157 1.00 66.51 C ANISOU 3477 CD1 LEU B 65 10571 6436 8262 262 1121 1118 C ATOM 3478 CD2 LEU B 65 53.508 33.900 129.856 1.00 67.48 C ANISOU 3478 CD2 LEU B 65 10702 6579 8359 208 1202 1172 C ATOM 3479 N ALA B 66 53.556 29.589 126.638 1.00 68.27 N ANISOU 3479 N ALA B 66 10726 6985 8229 312 1034 1074 N ATOM 3480 CA ALA B 66 54.365 28.515 126.055 1.00 69.40 C ANISOU 3480 CA ALA B 66 10835 7190 8343 309 1049 983 C ATOM 3481 C ALA B 66 54.839 28.878 124.652 1.00 70.90 C ANISOU 3481 C ALA B 66 11015 7485 8437 255 1082 985 C ATOM 3482 O ALA B 66 56.012 28.694 124.324 1.00 71.49 O ANISOU 3482 O ALA B 66 11059 7604 8498 235 1127 925 O ATOM 3483 CB ALA B 66 53.583 27.208 126.030 1.00 69.25 C ANISOU 3483 CB ALA B 66 10811 7160 8342 338 1022 923 C ATOM 3484 N ILE B 67 53.925 29.408 123.843 1.00 72.34 N ANISOU 3484 N ILE B 67 11214 7721 8552 224 1060 1065 N ATOM 3485 CA ILE B 67 54.250 29.875 122.487 1.00 74.23 C ANISOU 3485 CA ILE B 67 11437 8088 8677 150 1080 1100 C ATOM 3486 C ILE B 67 55.265 31.031 122.539 1.00 74.89 C ANISOU 3486 C ILE B 67 11522 8159 8770 127 1118 1157 C ATOM 3487 O ILE B 67 56.291 30.991 121.850 1.00 75.18 O ANISOU 3487 O ILE B 67 11536 8284 8742 76 1159 1107 O ATOM 3488 CB ILE B 67 52.973 30.277 121.703 1.00 74.96 C ANISOU 3488 CB ILE B 67 11526 8255 8699 117 1032 1223 C ATOM 3489 CG1 ILE B 67 52.099 29.033 121.446 1.00 75.40 C ANISOU 3489 CG1 ILE B 67 11574 8361 8711 107 1003 1141 C ATOM 3490 CG2 ILE B 67 53.318 30.950 120.376 1.00 75.96 C ANISOU 3490 CG2 ILE B 67 11627 8532 8701 23 1042 1304 C ATOM 3491 CD1 ILE B 67 50.645 29.350 121.169 1.00 75.92 C ANISOU 3491 CD1 ILE B 67 11630 8469 8747 100 940 1273 C ATOM 3492 N LEU B 68 54.983 32.035 123.369 1.00 75.12 N ANISOU 3492 N LEU B 68 11577 8078 8885 155 1116 1246 N ATOM 3493 CA LEU B 68 55.889 33.177 123.560 1.00 75.95 C ANISOU 3493 CA LEU B 68 11690 8149 9016 122 1163 1290 C ATOM 3494 C LEU B 68 57.285 32.750 124.024 1.00 75.92 C ANISOU 3494 C LEU B 68 11667 8163 9014 111 1199 1176 C ATOM 3495 O LEU B 68 58.284 33.256 123.514 1.00 76.93 O ANISOU 3495 O LEU B 68 11782 8351 9097 59 1238 1179 O ATOM 3496 CB LEU B 68 55.303 34.204 124.543 1.00 76.03 C ANISOU 3496 CB LEU B 68 11731 8013 9144 147 1179 1363 C ATOM 3497 CG LEU B 68 54.145 35.084 124.052 1.00 77.06 C ANISOU 3497 CG LEU B 68 11860 8101 9316 158 1169 1521 C ATOM 3498 CD1 LEU B 68 53.641 35.970 125.183 1.00 76.84 C ANISOU 3498 CD1 LEU B 68 11856 7900 9438 186 1215 1548 C ATOM 3499 CD2 LEU B 68 54.541 35.933 122.851 1.00 78.10 C ANISOU 3499 CD2 LEU B 68 11973 8308 9391 99 1184 1644 C ATOM 3500 N ILE B 69 57.349 31.821 124.979 1.00 75.17 N ANISOU 3500 N ILE B 69 11560 8025 8975 158 1182 1093 N ATOM 3501 CA ILE B 69 58.635 31.250 125.418 1.00 74.75 C ANISOU 3501 CA ILE B 69 11461 8001 8939 158 1206 1012 C ATOM 3502 C ILE B 69 59.302 30.438 124.293 1.00 75.44 C ANISOU 3502 C ILE B 69 11504 8189 8971 147 1236 935 C ATOM 3503 O ILE B 69 60.522 30.497 124.128 1.00 75.53 O ANISOU 3503 O ILE B 69 11472 8253 8971 121 1279 899 O ATOM 3504 CB ILE B 69 58.472 30.399 126.708 1.00 74.05 C ANISOU 3504 CB ILE B 69 11351 7850 8931 209 1173 976 C ATOM 3505 CG1 ILE B 69 58.105 31.301 127.902 1.00 73.99 C ANISOU 3505 CG1 ILE B 69 11377 7770 8963 184 1167 1022 C ATOM 3506 CG2 ILE B 69 59.727 29.585 127.026 1.00 73.88 C ANISOU 3506 CG2 ILE B 69 11254 7870 8947 222 1188 922 C ATOM 3507 CD1 ILE B 69 59.238 32.135 128.475 1.00 74.61 C ANISOU 3507 CD1 ILE B 69 11439 7872 9035 116 1208 1023 C ATOM 3508 N ASN B 70 58.503 29.694 123.526 1.00 75.85 N ANISOU 3508 N ASN B 70 11561 8272 8985 154 1224 901 N ATOM 3509 CA ASN B 70 59.017 28.898 122.402 1.00 76.95 C ANISOU 3509 CA ASN B 70 11660 8510 9065 120 1274 798 C ATOM 3510 C ASN B 70 59.645 29.772 121.314 1.00 78.05 C ANISOU 3510 C ASN B 70 11794 8770 9090 32 1311 828 C ATOM 3511 O ASN B 70 60.781 29.533 120.905 1.00 78.02 O ANISOU 3511 O ASN B 70 11742 8828 9071 4 1372 748 O ATOM 3512 CB ASN B 70 57.903 28.032 121.799 1.00 77.15 C ANISOU 3512 CB ASN B 70 11698 8561 9052 113 1258 750 C ATOM 3513 CG ASN B 70 58.399 27.112 120.705 1.00 78.06 C ANISOU 3513 CG ASN B 70 11771 8772 9115 58 1333 604 C ATOM 3514 OD1 ASN B 70 58.161 27.358 119.525 1.00 78.83 O ANISOU 3514 OD1 ASN B 70 11871 9007 9072 -38 1348 599 O ATOM 3515 ND2 ASN B 70 59.100 26.051 121.091 1.00 78.48 N ANISOU 3515 ND2 ASN B 70 11774 8757 9287 112 1389 488 N ATOM 3516 N ILE B 71 58.902 30.777 120.857 1.00 78.98 N ANISOU 3516 N ILE B 71 11951 8918 9137 -11 1275 954 N ATOM 3517 CA ILE B 71 59.403 31.703 119.820 1.00 80.17 C ANISOU 3517 CA ILE B 71 12095 9187 9179 -105 1300 1022 C ATOM 3518 C ILE B 71 60.402 32.745 120.352 1.00 80.34 C ANISOU 3518 C ILE B 71 12120 9159 9243 -114 1328 1073 C ATOM 3519 O ILE B 71 61.195 33.289 119.579 1.00 81.48 O ANISOU 3519 O ILE B 71 12246 9402 9308 -191 1366 1090 O ATOM 3520 CB ILE B 71 58.250 32.403 119.048 1.00 80.78 C ANISOU 3520 CB ILE B 71 12191 9326 9176 -154 1249 1176 C ATOM 3521 CG1 ILE B 71 57.554 33.476 119.907 1.00 80.35 C ANISOU 3521 CG1 ILE B 71 12174 9123 9232 -98 1214 1328 C ATOM 3522 CG2 ILE B 71 57.268 31.362 118.512 1.00 81.26 C ANISOU 3522 CG2 ILE B 71 12241 9463 9171 -169 1221 1119 C ATOM 3523 CD1 ILE B 71 56.244 33.991 119.343 1.00 80.90 C ANISOU 3523 CD1 ILE B 71 12241 9222 9275 -112 1158 1497 C ATOM 3524 N GLY B 72 60.367 33.018 121.659 1.00 79.30 N ANISOU 3524 N GLY B 72 12011 8891 9227 -53 1315 1090 N ATOM 3525 CA GLY B 72 61.197 34.060 122.273 1.00 79.10 C ANISOU 3525 CA GLY B 72 11995 8818 9241 -83 1347 1129 C ATOM 3526 C GLY B 72 62.665 33.703 122.473 1.00 79.02 C ANISOU 3526 C GLY B 72 11929 8867 9226 -101 1390 1035 C ATOM 3527 O GLY B 72 63.103 32.625 122.074 1.00 79.28 O ANISOU 3527 O GLY B 72 11910 8967 9244 -81 1407 936 O ATOM 3528 N PRO B 73 63.439 34.617 123.097 1.00 79.08 N ANISOU 3528 N PRO B 73 11941 8848 9258 -145 1419 1063 N ATOM 3529 CA PRO B 73 64.865 34.425 123.358 1.00 79.24 C ANISOU 3529 CA PRO B 73 11895 8938 9273 -173 1456 997 C ATOM 3530 C PRO B 73 65.129 33.712 124.685 1.00 78.88 C ANISOU 3530 C PRO B 73 11805 8854 9310 -121 1430 954 C ATOM 3531 O PRO B 73 64.190 33.237 125.334 1.00 78.28 O ANISOU 3531 O PRO B 73 11753 8700 9290 -63 1386 960 O ATOM 3532 CB PRO B 73 65.378 35.865 123.431 1.00 79.88 C ANISOU 3532 CB PRO B 73 12009 9009 9332 -265 1494 1062 C ATOM 3533 CG PRO B 73 64.252 36.601 124.071 1.00 79.51 C ANISOU 3533 CG PRO B 73 12035 8822 9352 -255 1479 1132 C ATOM 3534 CD PRO B 73 62.983 35.929 123.604 1.00 79.28 C ANISOU 3534 CD PRO B 73 12025 8768 9326 -180 1429 1156 C ATOM 3535 N GLN B 74 66.402 33.640 125.074 1.00 79.40 N ANISOU 3535 N GLN B 74 11796 8990 9380 -151 1455 926 N ATOM 3536 CA GLN B 74 66.784 33.231 126.429 1.00 78.85 C ANISOU 3536 CA GLN B 74 11668 8917 9373 -136 1424 928 C ATOM 3537 C GLN B 74 66.264 34.251 127.434 1.00 77.50 C ANISOU 3537 C GLN B 74 11566 8678 9200 -203 1415 967 C ATOM 3538 O GLN B 74 66.100 35.426 127.103 1.00 77.58 O ANISOU 3538 O GLN B 74 11646 8651 9177 -272 1455 990 O ATOM 3539 CB GLN B 74 68.306 33.114 126.572 1.00 80.21 C ANISOU 3539 CB GLN B 74 11731 9205 9540 -173 1452 915 C ATOM 3540 CG GLN B 74 68.915 31.933 125.836 1.00 81.20 C ANISOU 3540 CG GLN B 74 11757 9380 9712 -96 1478 861 C ATOM 3541 CD GLN B 74 70.411 31.798 126.064 1.00 82.46 C ANISOU 3541 CD GLN B 74 11787 9652 9891 -121 1507 864 C ATOM 3542 OE1 GLN B 74 70.917 32.042 127.164 1.00 82.48 O ANISOU 3542 OE1 GLN B 74 11736 9700 9900 -165 1473 922 O ATOM 3543 NE2 GLN B 74 71.129 31.397 125.018 1.00 83.64 N ANISOU 3543 NE2 GLN B 74 11872 9862 10043 -104 1573 801 N ATOM 3544 N THR B 75 66.014 33.790 128.656 1.00 76.40 N ANISOU 3544 N THR B 75 11400 8523 9103 -191 1372 973 N ATOM 3545 CA THR B 75 65.441 34.629 129.710 1.00 75.22 C ANISOU 3545 CA THR B 75 11311 8315 8954 -266 1377 980 C ATOM 3546 C THR B 75 66.245 34.526 130.992 1.00 74.46 C ANISOU 3546 C THR B 75 11134 8319 8837 -349 1358 982 C ATOM 3547 O THR B 75 67.026 33.594 131.170 1.00 75.05 O ANISOU 3547 O THR B 75 11098 8490 8927 -312 1319 1008 O ATOM 3548 CB THR B 75 63.993 34.205 130.027 1.00 74.91 C ANISOU 3548 CB THR B 75 11327 8170 8965 -194 1337 986 C ATOM 3549 OG1 THR B 75 63.971 32.846 130.487 1.00 73.93 O ANISOU 3549 OG1 THR B 75 11131 8079 8879 -119 1273 992 O ATOM 3550 CG2 THR B 75 63.110 34.338 128.796 1.00 75.34 C ANISOU 3550 CG2 THR B 75 11449 8149 9026 -129 1346 1003 C ATOM 3551 N TYR B 76 66.026 35.482 131.892 1.00 73.57 N ANISOU 3551 N TYR B 76 11068 8187 8698 -468 1392 959 N ATOM 3552 CA TYR B 76 66.527 35.383 133.265 1.00 73.47 C ANISOU 3552 CA TYR B 76 10983 8289 8642 -577 1368 960 C ATOM 3553 C TYR B 76 65.946 34.131 133.925 1.00 73.27 C ANISOU 3553 C TYR B 76 10905 8276 8655 -494 1281 1004 C ATOM 3554 O TYR B 76 64.899 33.631 133.497 1.00 72.83 O ANISOU 3554 O TYR B 76 10905 8107 8661 -378 1259 1004 O ATOM 3555 CB TYR B 76 66.102 36.600 134.089 1.00 73.12 C ANISOU 3555 CB TYR B 76 11016 8197 8568 -729 1442 893 C ATOM 3556 CG TYR B 76 66.769 37.906 133.719 1.00 73.22 C ANISOU 3556 CG TYR B 76 11070 8198 8550 -847 1540 849 C ATOM 3557 CD1 TYR B 76 68.144 38.081 133.870 1.00 73.75 C ANISOU 3557 CD1 TYR B 76 11055 8427 8539 -955 1547 853 C ATOM 3558 CD2 TYR B 76 66.018 38.985 133.248 1.00 72.86 C ANISOU 3558 CD2 TYR B 76 11138 7975 8568 -857 1631 816 C ATOM 3559 CE1 TYR B 76 68.753 39.286 133.541 1.00 74.21 C ANISOU 3559 CE1 TYR B 76 11155 8471 8569 -1076 1642 809 C ATOM 3560 CE2 TYR B 76 66.617 40.190 132.917 1.00 73.35 C ANISOU 3560 CE2 TYR B 76 11238 8006 8623 -968 1729 786 C ATOM 3561 CZ TYR B 76 67.982 40.339 133.065 1.00 73.95 C ANISOU 3561 CZ TYR B 76 11243 8244 8608 -1082 1736 774 C ATOM 3562 OH TYR B 76 68.571 41.535 132.736 1.00 74.55 O ANISOU 3562 OH TYR B 76 11360 8286 8678 -1203 1837 742 O ATOM 3563 N PHE B 77 66.610 33.629 134.964 1.00 73.98 N ANISOU 3563 N PHE B 77 10882 8515 8710 -562 1228 1054 N ATOM 3564 CA PHE B 77 66.037 32.523 135.750 1.00 74.00 C ANISOU 3564 CA PHE B 77 10830 8534 8751 -508 1144 1116 C ATOM 3565 C PHE B 77 64.635 32.846 136.313 1.00 73.47 C ANISOU 3565 C PHE B 77 10869 8363 8681 -534 1156 1062 C ATOM 3566 O PHE B 77 63.707 32.022 136.205 1.00 73.06 O ANISOU 3566 O PHE B 77 10838 8224 8696 -418 1110 1084 O ATOM 3567 CB PHE B 77 66.979 32.116 136.887 1.00 75.15 C ANISOU 3567 CB PHE B 77 10825 8885 8842 -613 1082 1206 C ATOM 3568 CG PHE B 77 66.564 30.859 137.591 1.00 75.38 C ANISOU 3568 CG PHE B 77 10772 8941 8929 -546 987 1311 C ATOM 3569 CD1 PHE B 77 66.944 29.616 137.098 1.00 75.59 C ANISOU 3569 CD1 PHE B 77 10696 8945 9080 -387 939 1404 C ATOM 3570 CD2 PHE B 77 65.779 30.913 138.741 1.00 75.65 C ANISOU 3570 CD2 PHE B 77 10826 9015 8902 -649 956 1312 C ATOM 3571 CE1 PHE B 77 66.554 28.449 137.743 1.00 76.11 C ANISOU 3571 CE1 PHE B 77 10682 9013 9222 -323 858 1515 C ATOM 3572 CE2 PHE B 77 65.385 29.752 139.389 1.00 75.77 C ANISOU 3572 CE2 PHE B 77 10762 9057 8968 -595 865 1425 C ATOM 3573 CZ PHE B 77 65.775 28.519 138.892 1.00 76.05 C ANISOU 3573 CZ PHE B 77 10696 9056 9140 -428 813 1535 C ATOM 3574 N HIS B 78 64.486 34.044 136.885 1.00 73.76 N ANISOU 3574 N HIS B 78 10969 8402 8652 -690 1229 982 N ATOM 3575 CA HIS B 78 63.223 34.465 137.524 1.00 73.56 C ANISOU 3575 CA HIS B 78 11030 8282 8635 -735 1266 914 C ATOM 3576 C HIS B 78 62.049 34.517 136.537 1.00 72.65 C ANISOU 3576 C HIS B 78 11019 7964 8619 -582 1289 896 C ATOM 3577 O HIS B 78 60.929 34.127 136.882 1.00 72.32 O ANISOU 3577 O HIS B 78 11009 7854 8613 -535 1265 891 O ATOM 3578 CB HIS B 78 63.381 35.816 138.268 1.00 74.64 C ANISOU 3578 CB HIS B 78 11209 8444 8704 -945 1375 805 C ATOM 3579 CG HIS B 78 63.182 37.028 137.405 1.00 74.85 C ANISOU 3579 CG HIS B 78 11341 8302 8794 -938 1492 735 C ATOM 3580 ND1 HIS B 78 64.225 37.717 136.824 1.00 75.21 N ANISOU 3580 ND1 HIS B 78 11383 8379 8815 -993 1542 728 N ATOM 3581 CD2 HIS B 78 62.052 37.675 137.028 1.00 74.93 C ANISOU 3581 CD2 HIS B 78 11452 8112 8903 -883 1567 689 C ATOM 3582 CE1 HIS B 78 63.745 38.731 136.124 1.00 75.30 C ANISOU 3582 CE1 HIS B 78 11491 8210 8908 -973 1642 687 C ATOM 3583 NE2 HIS B 78 62.429 38.726 136.230 1.00 74.67 N ANISOU 3583 NE2 HIS B 78 11471 7987 8912 -902 1658 670 N ATOM 3584 N THR B 79 62.321 34.997 135.320 1.00 72.43 N ANISOU 3584 N THR B 79 11033 7862 8624 -519 1331 897 N ATOM 3585 CA THR B 79 61.317 35.109 134.258 1.00 71.81 C ANISOU 3585 CA THR B 79 11034 7628 8621 -392 1346 906 C ATOM 3586 C THR B 79 60.756 33.739 133.904 1.00 71.69 C ANISOU 3586 C THR B 79 10993 7606 8639 -250 1255 954 C ATOM 3587 O THR B 79 59.538 33.554 133.838 1.00 70.74 O ANISOU 3587 O THR B 79 10922 7392 8564 -185 1243 954 O ATOM 3588 CB THR B 79 61.920 35.725 132.977 1.00 71.63 C ANISOU 3588 CB THR B 79 11034 7579 8599 -369 1390 924 C ATOM 3589 OG1 THR B 79 62.560 36.966 133.288 1.00 72.23 O ANISOU 3589 OG1 THR B 79 11132 7659 8653 -509 1480 880 O ATOM 3590 CG2 THR B 79 60.849 35.957 131.909 1.00 71.06 C ANISOU 3590 CG2 THR B 79 11033 7377 8590 -267 1402 958 C ATOM 3591 N CYS B 80 61.662 32.791 133.681 1.00 73.01 N ANISOU 3591 N CYS B 80 11075 7869 8796 -205 1202 992 N ATOM 3592 CA CYS B 80 61.289 31.419 133.365 1.00 73.74 C ANISOU 3592 CA CYS B 80 11130 7946 8940 -80 1135 1025 C ATOM 3593 C CYS B 80 60.618 30.746 134.557 1.00 73.56 C ANISOU 3593 C CYS B 80 11083 7932 8932 -91 1077 1049 C ATOM 3594 O CYS B 80 59.633 30.023 134.382 1.00 72.76 O ANISOU 3594 O CYS B 80 11009 7757 8879 -5 1042 1055 O ATOM 3595 CB CYS B 80 62.516 30.619 132.924 1.00 75.54 C ANISOU 3595 CB CYS B 80 11257 8258 9188 -36 1117 1054 C ATOM 3596 SG CYS B 80 62.127 28.999 132.222 1.00 76.56 S ANISOU 3596 SG CYS B 80 11346 8326 9415 117 1080 1062 S ATOM 3597 N LEU B 81 61.138 30.993 135.761 1.00 74.59 N ANISOU 3597 N LEU B 81 11160 8169 9010 -212 1066 1066 N ATOM 3598 CA LEU B 81 60.505 30.476 136.978 1.00 75.08 C ANISOU 3598 CA LEU B 81 11195 8268 9061 -257 1013 1094 C ATOM 3599 C LEU B 81 59.060 30.974 137.148 1.00 74.69 C ANISOU 3599 C LEU B 81 11251 8105 9023 -261 1048 1028 C ATOM 3600 O LEU B 81 58.175 30.183 137.474 1.00 74.28 O ANISOU 3600 O LEU B 81 11200 8020 9002 -208 997 1052 O ATOM 3601 CB LEU B 81 61.335 30.827 138.220 1.00 76.40 C ANISOU 3601 CB LEU B 81 11284 8608 9135 -430 1004 1117 C ATOM 3602 CG LEU B 81 60.864 30.281 139.577 1.00 76.98 C ANISOU 3602 CG LEU B 81 11305 8776 9165 -515 942 1165 C ATOM 3603 CD1 LEU B 81 60.720 28.767 139.537 1.00 77.10 C ANISOU 3603 CD1 LEU B 81 11244 8780 9269 -383 844 1284 C ATOM 3604 CD2 LEU B 81 61.822 30.689 140.688 1.00 78.03 C ANISOU 3604 CD2 LEU B 81 11346 9125 9177 -716 934 1193 C ATOM 3605 N MET B 82 58.833 32.270 136.925 1.00 74.87 N ANISOU 3605 N MET B 82 11351 8059 9034 -320 1140 953 N ATOM 3606 CA MET B 82 57.481 32.860 137.029 1.00 74.67 C ANISOU 3606 CA MET B 82 11411 7908 9052 -314 1193 898 C ATOM 3607 C MET B 82 56.492 32.280 136.018 1.00 73.96 C ANISOU 3607 C MET B 82 11361 7709 9032 -154 1156 932 C ATOM 3608 O MET B 82 55.342 31.998 136.358 1.00 72.96 O ANISOU 3608 O MET B 82 11258 7527 8935 -124 1141 925 O ATOM 3609 CB MET B 82 57.525 34.378 136.841 1.00 75.78 C ANISOU 3609 CB MET B 82 11614 7968 9212 -391 1315 828 C ATOM 3610 CG MET B 82 57.955 35.133 138.078 1.00 77.45 C ANISOU 3610 CG MET B 82 11810 8256 9360 -586 1386 745 C ATOM 3611 SD MET B 82 58.270 36.876 137.787 1.00 79.15 S ANISOU 3611 SD MET B 82 12090 8362 9620 -688 1549 657 S ATOM 3612 CE MET B 82 58.732 37.405 139.439 1.00 80.10 C ANISOU 3612 CE MET B 82 12177 8620 9634 -950 1623 532 C ATOM 3613 N VAL B 83 56.948 32.128 134.775 1.00 73.91 N ANISOU 3613 N VAL B 83 11355 7687 9038 -70 1148 964 N ATOM 3614 CA VAL B 83 56.116 31.616 133.677 1.00 73.01 C ANISOU 3614 CA VAL B 83 11273 7504 8964 51 1118 991 C ATOM 3615 C VAL B 83 55.756 30.131 133.866 1.00 71.97 C ANISOU 3615 C VAL B 83 11102 7393 8848 121 1037 1011 C ATOM 3616 O VAL B 83 54.706 29.684 133.399 1.00 71.04 O ANISOU 3616 O VAL B 83 11014 7219 8756 190 1013 1016 O ATOM 3617 CB VAL B 83 56.799 31.861 132.305 1.00 73.49 C ANISOU 3617 CB VAL B 83 11336 7575 9008 87 1140 1007 C ATOM 3618 CG1 VAL B 83 56.047 31.179 131.161 1.00 73.51 C ANISOU 3618 CG1 VAL B 83 11356 7554 9021 182 1106 1027 C ATOM 3619 CG2 VAL B 83 56.903 33.361 132.030 1.00 73.83 C ANISOU 3619 CG2 VAL B 83 11425 7567 9058 28 1222 1009 C ATOM 3620 N ALA B 84 56.608 29.380 134.561 1.00 71.57 N ANISOU 3620 N ALA B 84 10977 7423 8790 97 997 1034 N ATOM 3621 CA ALA B 84 56.347 27.964 134.829 1.00 71.39 C ANISOU 3621 CA ALA B 84 10906 7404 8814 160 928 1070 C ATOM 3622 C ALA B 84 55.203 27.679 135.817 1.00 71.13 C ANISOU 3622 C ALA B 84 10891 7350 8784 137 892 1077 C ATOM 3623 O ALA B 84 54.648 26.585 135.785 1.00 72.02 O ANISOU 3623 O ALA B 84 10989 7429 8944 201 844 1101 O ATOM 3624 CB ALA B 84 57.619 27.285 135.308 1.00 72.14 C ANISOU 3624 CB ALA B 84 10894 7588 8927 146 896 1127 C ATOM 3625 N CYS B 85 54.845 28.640 136.668 1.00 70.96 N ANISOU 3625 N CYS B 85 10899 7344 8718 38 927 1046 N ATOM 3626 CA CYS B 85 53.904 28.399 137.787 1.00 70.56 C ANISOU 3626 CA CYS B 85 10850 7304 8655 -14 901 1044 C ATOM 3627 C CYS B 85 52.381 28.382 137.497 1.00 69.01 C ANISOU 3627 C CYS B 85 10717 7006 8496 46 908 1015 C ATOM 3628 O CYS B 85 51.674 27.561 138.087 1.00 69.43 O ANISOU 3628 O CYS B 85 10755 7068 8557 51 856 1037 O ATOM 3629 CB CYS B 85 54.192 29.390 138.927 1.00 71.88 C ANISOU 3629 CB CYS B 85 11009 7548 8751 -174 953 999 C ATOM 3630 SG CYS B 85 55.867 29.288 139.600 1.00 73.68 S ANISOU 3630 SG CYS B 85 11136 7952 8907 -286 924 1054 S ATOM 3631 N PRO B 86 51.864 29.287 136.632 1.00 68.06 N ANISOU 3631 N PRO B 86 10655 6798 8403 87 969 983 N ATOM 3632 CA PRO B 86 50.414 29.317 136.348 1.00 66.98 C ANISOU 3632 CA PRO B 86 10559 6582 8308 143 972 977 C ATOM 3633 C PRO B 86 49.774 27.957 136.050 1.00 65.78 C ANISOU 3633 C PRO B 86 10395 6429 8167 219 891 1009 C ATOM 3634 O PRO B 86 48.711 27.634 136.600 1.00 65.61 O ANISOU 3634 O PRO B 86 10379 6391 8156 216 871 1004 O ATOM 3635 CB PRO B 86 50.325 30.231 135.126 1.00 67.23 C ANISOU 3635 CB PRO B 86 10625 6547 8370 194 1023 991 C ATOM 3636 CG PRO B 86 51.438 31.199 135.326 1.00 67.93 C ANISOU 3636 CG PRO B 86 10713 6652 8442 118 1089 966 C ATOM 3637 CD PRO B 86 52.536 30.468 136.055 1.00 68.27 C ANISOU 3637 CD PRO B 86 10707 6804 8429 62 1043 963 C ATOM 3638 N VAL B 87 50.438 27.168 135.207 1.00 64.84 N ANISOU 3638 N VAL B 87 10258 6326 8051 276 857 1030 N ATOM 3639 CA VAL B 87 49.989 25.801 134.901 1.00 63.38 C ANISOU 3639 CA VAL B 87 10059 6128 7893 335 800 1041 C ATOM 3640 C VAL B 87 49.935 24.915 136.156 1.00 62.38 C ANISOU 3640 C VAL B 87 9890 6028 7783 301 749 1073 C ATOM 3641 O VAL B 87 48.995 24.129 136.309 1.00 62.35 O ANISOU 3641 O VAL B 87 9893 5997 7801 322 712 1079 O ATOM 3642 CB VAL B 87 50.847 25.150 133.786 1.00 63.44 C ANISOU 3642 CB VAL B 87 10047 6140 7917 388 804 1031 C ATOM 3643 CG1 VAL B 87 52.259 24.829 134.268 1.00 63.74 C ANISOU 3643 CG1 VAL B 87 10019 6218 7979 371 802 1057 C ATOM 3644 CG2 VAL B 87 50.161 23.905 133.233 1.00 63.62 C ANISOU 3644 CG2 VAL B 87 10070 6127 7973 437 777 1011 C ATOM 3645 N LEU B 88 50.912 25.073 137.056 1.00 61.31 N ANISOU 3645 N LEU B 88 9705 5960 7629 234 743 1105 N ATOM 3646 CA LEU B 88 50.953 24.327 138.327 1.00 60.57 C ANISOU 3646 CA LEU B 88 9552 5926 7534 177 686 1168 C ATOM 3647 C LEU B 88 49.765 24.685 139.209 1.00 59.96 C ANISOU 3647 C LEU B 88 9507 5861 7414 108 688 1140 C ATOM 3648 O LEU B 88 49.131 23.800 139.790 1.00 60.14 O ANISOU 3648 O LEU B 88 9508 5889 7450 101 635 1180 O ATOM 3649 CB LEU B 88 52.252 24.581 139.103 1.00 60.42 C ANISOU 3649 CB LEU B 88 9460 6017 7478 93 678 1220 C ATOM 3650 CG LEU B 88 53.572 24.332 138.379 1.00 60.67 C ANISOU 3650 CG LEU B 88 9440 6055 7555 148 684 1252 C ATOM 3651 CD1 LEU B 88 54.748 24.634 139.293 1.00 61.46 C ANISOU 3651 CD1 LEU B 88 9454 6293 7604 45 667 1319 C ATOM 3652 CD2 LEU B 88 53.638 22.907 137.858 1.00 61.01 C ANISOU 3652 CD2 LEU B 88 9440 6026 7714 256 650 1300 C ATOM 3653 N ILE B 89 49.460 25.979 139.283 1.00 59.75 N ANISOU 3653 N ILE B 89 9525 5826 7351 58 760 1068 N ATOM 3654 CA ILE B 89 48.284 26.462 140.024 1.00 59.86 C ANISOU 3654 CA ILE B 89 9566 5832 7346 -1 793 1017 C ATOM 3655 C ILE B 89 47.014 25.889 139.394 1.00 59.56 C ANISOU 3655 C ILE B 89 9559 5714 7354 93 766 1020 C ATOM 3656 O ILE B 89 46.196 25.228 140.064 1.00 59.70 O ANISOU 3656 O ILE B 89 9566 5752 7366 69 727 1032 O ATOM 3657 CB ILE B 89 48.194 28.016 140.029 1.00 59.77 C ANISOU 3657 CB ILE B 89 9592 5782 7333 -52 904 932 C ATOM 3658 CG1 ILE B 89 49.412 28.630 140.742 1.00 60.45 C ANISOU 3658 CG1 ILE B 89 9648 5963 7355 -179 941 909 C ATOM 3659 CG2 ILE B 89 46.902 28.493 140.689 1.00 59.68 C ANISOU 3659 CG2 ILE B 89 9600 5738 7339 -97 960 867 C ATOM 3660 CD1 ILE B 89 49.705 30.060 140.360 1.00 61.01 C ANISOU 3660 CD1 ILE B 89 9759 5970 7452 -207 1055 836 C ATOM 3661 N LEU B 90 46.872 26.133 138.094 1.00 59.78 N ANISOU 3661 N LEU B 90 9621 5672 7419 188 785 1015 N ATOM 3662 CA LEU B 90 45.633 25.805 137.391 1.00 59.91 C ANISOU 3662 CA LEU B 90 9661 5636 7463 259 767 1017 C ATOM 3663 C LEU B 90 45.351 24.308 137.382 1.00 60.27 C ANISOU 3663 C LEU B 90 9691 5689 7517 287 691 1046 C ATOM 3664 O LEU B 90 44.211 23.895 137.634 1.00 60.38 O ANISOU 3664 O LEU B 90 9710 5695 7534 287 668 1044 O ATOM 3665 CB LEU B 90 45.657 26.367 135.967 1.00 59.80 C ANISOU 3665 CB LEU B 90 9672 5585 7464 329 795 1025 C ATOM 3666 CG LEU B 90 45.663 27.898 135.891 1.00 60.03 C ANISOU 3666 CG LEU B 90 9714 5573 7518 313 879 1016 C ATOM 3667 CD1 LEU B 90 45.927 28.335 134.468 1.00 60.25 C ANISOU 3667 CD1 LEU B 90 9753 5588 7549 370 890 1056 C ATOM 3668 CD2 LEU B 90 44.363 28.489 136.410 1.00 60.35 C ANISOU 3668 CD2 LEU B 90 9754 5568 7608 306 921 1003 C ATOM 3669 N THR B 91 46.389 23.507 137.125 1.00 61.09 N ANISOU 3669 N THR B 91 9769 5801 7639 308 663 1072 N ATOM 3670 CA THR B 91 46.269 22.042 137.187 1.00 61.30 C ANISOU 3670 CA THR B 91 9771 5807 7711 333 609 1101 C ATOM 3671 C THR B 91 45.870 21.577 138.589 1.00 61.49 C ANISOU 3671 C THR B 91 9763 5870 7728 264 564 1149 C ATOM 3672 O THR B 91 45.028 20.688 138.721 1.00 61.31 O ANISOU 3672 O THR B 91 9743 5821 7730 272 528 1162 O ATOM 3673 CB THR B 91 47.572 21.324 136.766 1.00 61.71 C ANISOU 3673 CB THR B 91 9781 5844 7822 371 607 1126 C ATOM 3674 OG1 THR B 91 47.979 21.783 135.474 1.00 62.23 O ANISOU 3674 OG1 THR B 91 9873 5894 7876 414 654 1073 O ATOM 3675 CG2 THR B 91 47.371 19.809 136.706 1.00 62.09 C ANISOU 3675 CG2 THR B 91 9802 5831 7958 405 577 1149 C ATOM 3676 N GLN B 92 46.462 22.178 139.624 1.00 61.80 N ANISOU 3676 N GLN B 92 9771 5987 7722 181 568 1174 N ATOM 3677 CA GLN B 92 46.095 21.842 141.003 1.00 62.24 C ANISOU 3677 CA GLN B 92 9789 6119 7740 83 528 1221 C ATOM 3678 C GLN B 92 44.651 22.223 141.317 1.00 61.94 C ANISOU 3678 C GLN B 92 9791 6073 7668 52 550 1159 C ATOM 3679 O GLN B 92 43.934 21.447 141.960 1.00 62.33 O ANISOU 3679 O GLN B 92 9824 6145 7714 17 503 1195 O ATOM 3680 CB GLN B 92 47.050 22.485 142.021 1.00 62.78 C ANISOU 3680 CB GLN B 92 9808 6307 7738 -32 535 1247 C ATOM 3681 CG GLN B 92 46.928 21.910 143.429 1.00 63.41 C ANISOU 3681 CG GLN B 92 9823 6505 7764 -154 475 1330 C ATOM 3682 CD GLN B 92 47.146 20.401 143.473 1.00 63.74 C ANISOU 3682 CD GLN B 92 9804 6519 7891 -100 389 1468 C ATOM 3683 OE1 GLN B 92 48.166 19.889 142.994 1.00 63.79 O ANISOU 3683 OE1 GLN B 92 9765 6492 7980 -30 371 1539 O ATOM 3684 NE2 GLN B 92 46.177 19.682 144.033 1.00 63.67 N ANISOU 3684 NE2 GLN B 92 9792 6515 7883 -132 346 1504 N ATOM 3685 N SER B 93 44.222 23.399 140.854 1.00 61.97 N ANISOU 3685 N SER B 93 9838 6042 7663 68 623 1078 N ATOM 3686 CA SER B 93 42.809 23.804 141.003 1.00 62.03 C ANISOU 3686 CA SER B 93 9869 6026 7671 62 657 1026 C ATOM 3687 C SER B 93 41.837 22.761 140.443 1.00 61.64 C ANISOU 3687 C SER B 93 9830 5936 7651 129 601 1051 C ATOM 3688 O SER B 93 40.836 22.419 141.093 1.00 61.71 O ANISOU 3688 O SER B 93 9830 5969 7646 87 585 1046 O ATOM 3689 CB SER B 93 42.549 25.171 140.355 1.00 62.10 C ANISOU 3689 CB SER B 93 9908 5974 7712 100 747 967 C ATOM 3690 OG SER B 93 41.244 25.633 140.663 1.00 62.29 O ANISOU 3690 OG SER B 93 9931 5974 7760 91 793 925 O ATOM 3691 N SER B 94 42.148 22.247 139.255 1.00 61.73 N ANISOU 3691 N SER B 94 9858 5898 7698 216 579 1067 N ATOM 3692 CA SER B 94 41.313 21.230 138.603 1.00 62.03 C ANISOU 3692 CA SER B 94 9907 5903 7757 260 538 1072 C ATOM 3693 C SER B 94 41.073 19.998 139.481 1.00 62.31 C ANISOU 3693 C SER B 94 9918 5949 7806 215 480 1116 C ATOM 3694 O SER B 94 39.929 19.534 139.623 1.00 62.88 O ANISOU 3694 O SER B 94 9996 6023 7872 200 458 1109 O ATOM 3695 CB SER B 94 41.937 20.789 137.272 1.00 62.19 C ANISOU 3695 CB SER B 94 9941 5883 7803 327 540 1062 C ATOM 3696 OG SER B 94 42.169 21.905 136.429 1.00 62.42 O ANISOU 3696 OG SER B 94 9987 5916 7812 359 585 1043 O ATOM 3697 N ILE B 95 42.153 19.504 140.089 1.00 61.86 N ANISOU 3697 N ILE B 95 9824 5907 7773 188 453 1177 N ATOM 3698 CA ILE B 95 42.124 18.276 140.890 1.00 61.70 C ANISOU 3698 CA ILE B 95 9763 5889 7790 150 393 1259 C ATOM 3699 C ILE B 95 41.203 18.478 142.096 1.00 61.66 C ANISOU 3699 C ILE B 95 9746 5967 7713 50 375 1268 C ATOM 3700 O ILE B 95 40.297 17.664 142.345 1.00 62.48 O ANISOU 3700 O ILE B 95 9851 6059 7829 30 340 1288 O ATOM 3701 CB ILE B 95 43.545 17.867 141.356 1.00 62.14 C ANISOU 3701 CB ILE B 95 9754 5962 7891 140 367 1357 C ATOM 3702 CG1 ILE B 95 44.447 17.560 140.152 1.00 62.14 C ANISOU 3702 CG1 ILE B 95 9757 5873 7979 239 398 1335 C ATOM 3703 CG2 ILE B 95 43.502 16.654 142.276 1.00 62.91 C ANISOU 3703 CG2 ILE B 95 9792 6067 8042 95 300 1482 C ATOM 3704 CD1 ILE B 95 45.933 17.664 140.432 1.00 62.64 C ANISOU 3704 CD1 ILE B 95 9754 5969 8074 240 395 1410 C ATOM 3705 N LEU B 96 41.423 19.584 142.809 1.00 60.87 N ANISOU 3705 N LEU B 96 9637 5951 7538 -23 411 1239 N ATOM 3706 CA LEU B 96 40.623 19.930 143.995 1.00 60.65 C ANISOU 3706 CA LEU B 96 9593 6018 7433 -141 420 1217 C ATOM 3707 C LEU B 96 39.155 20.211 143.637 1.00 59.75 C ANISOU 3707 C LEU B 96 9515 5864 7322 -110 455 1137 C ATOM 3708 O LEU B 96 38.228 19.773 144.353 1.00 59.52 O ANISOU 3708 O LEU B 96 9470 5881 7262 -176 433 1143 O ATOM 3709 CB LEU B 96 41.244 21.125 144.729 1.00 61.14 C ANISOU 3709 CB LEU B 96 9637 6170 7420 -240 479 1169 C ATOM 3710 CG LEU B 96 42.665 20.888 145.280 1.00 61.98 C ANISOU 3710 CG LEU B 96 9687 6364 7497 -304 436 1264 C ATOM 3711 CD1 LEU B 96 43.303 22.197 145.729 1.00 62.09 C ANISOU 3711 CD1 LEU B 96 9697 6457 7436 -400 513 1185 C ATOM 3712 CD2 LEU B 96 42.664 19.866 146.415 1.00 62.84 C ANISOU 3712 CD2 LEU B 96 9726 6584 7565 -411 349 1392 C ATOM 3713 N ALA B 97 38.952 20.914 142.520 1.00 59.03 N ANISOU 3713 N ALA B 97 9460 5698 7269 -14 505 1078 N ATOM 3714 CA ALA B 97 37.609 21.115 141.963 1.00 58.91 C ANISOU 3714 CA ALA B 97 9459 5649 7273 33 527 1036 C ATOM 3715 C ALA B 97 36.903 19.785 141.666 1.00 58.97 C ANISOU 3715 C ALA B 97 9471 5641 7292 50 457 1073 C ATOM 3716 O ALA B 97 35.726 19.618 142.003 1.00 58.85 O ANISOU 3716 O ALA B 97 9444 5652 7260 19 453 1058 O ATOM 3717 CB ALA B 97 37.671 21.975 140.709 1.00 58.74 C ANISOU 3717 CB ALA B 97 9460 5567 7290 130 573 1012 C ATOM 3718 N LEU B 98 37.621 18.841 141.053 1.00 59.15 N ANISOU 3718 N LEU B 98 9504 5615 7352 92 414 1113 N ATOM 3719 CA LEU B 98 37.069 17.499 140.809 1.00 59.50 C ANISOU 3719 CA LEU B 98 9554 5625 7428 94 364 1137 C ATOM 3720 C LEU B 98 36.781 16.734 142.110 1.00 59.83 C ANISOU 3720 C LEU B 98 9565 5709 7459 2 317 1200 C ATOM 3721 O LEU B 98 35.715 16.093 142.252 1.00 59.49 O ANISOU 3721 O LEU B 98 9523 5671 7409 -28 293 1199 O ATOM 3722 CB LEU B 98 38.001 16.682 139.908 1.00 60.00 C ANISOU 3722 CB LEU B 98 9628 5607 7562 152 358 1148 C ATOM 3723 CG LEU B 98 38.048 17.102 138.440 1.00 59.98 C ANISOU 3723 CG LEU B 98 9656 5579 7552 220 396 1082 C ATOM 3724 CD1 LEU B 98 39.333 16.615 137.778 1.00 60.41 C ANISOU 3724 CD1 LEU B 98 9711 5569 7673 264 414 1079 C ATOM 3725 CD2 LEU B 98 36.824 16.590 137.692 1.00 60.02 C ANISOU 3725 CD2 LEU B 98 9678 5592 7535 212 388 1038 C ATOM 3726 N LEU B 99 37.724 16.807 143.055 1.00 60.19 N ANISOU 3726 N LEU B 99 9574 5802 7493 -52 301 1266 N ATOM 3727 CA LEU B 99 37.534 16.197 144.378 1.00 60.90 C ANISOU 3727 CA LEU B 99 9619 5969 7550 -163 250 1351 C ATOM 3728 C LEU B 99 36.299 16.754 145.096 1.00 61.18 C ANISOU 3728 C LEU B 99 9652 6093 7497 -247 274 1287 C ATOM 3729 O LEU B 99 35.535 15.983 145.702 1.00 61.74 O ANISOU 3729 O LEU B 99 9707 6199 7552 -314 233 1329 O ATOM 3730 CB LEU B 99 38.784 16.363 145.251 1.00 61.30 C ANISOU 3730 CB LEU B 99 9615 6100 7576 -228 227 1440 C ATOM 3731 CG LEU B 99 38.763 15.734 146.653 1.00 62.46 C ANISOU 3731 CG LEU B 99 9695 6364 7672 -366 162 1565 C ATOM 3732 CD1 LEU B 99 38.640 14.214 146.600 1.00 62.89 C ANISOU 3732 CD1 LEU B 99 9726 6332 7836 -339 95 1691 C ATOM 3733 CD2 LEU B 99 40.005 16.151 147.423 1.00 63.26 C ANISOU 3733 CD2 LEU B 99 9732 6584 7718 -447 144 1646 C ATOM 3734 N ALA B 100 36.097 18.075 145.017 1.00 60.98 N ANISOU 3734 N ALA B 100 9641 6095 7433 -243 350 1187 N ATOM 3735 CA ALA B 100 34.859 18.694 145.529 1.00 61.28 C ANISOU 3735 CA ALA B 100 9669 6189 7424 -300 402 1106 C ATOM 3736 C ALA B 100 33.596 18.080 144.892 1.00 61.36 C ANISOU 3736 C ALA B 100 9692 6155 7464 -247 379 1096 C ATOM 3737 O ALA B 100 32.635 17.719 145.602 1.00 61.55 O ANISOU 3737 O ALA B 100 9694 6241 7450 -326 367 1093 O ATOM 3738 CB ALA B 100 34.883 20.201 145.319 1.00 61.12 C ANISOU 3738 CB ALA B 100 9655 6154 7411 -274 506 1005 C ATOM 3739 N ILE B 101 33.622 17.942 143.562 1.00 61.19 N ANISOU 3739 N ILE B 101 9703 6047 7500 -133 373 1091 N ATOM 3740 CA ILE B 101 32.525 17.313 142.809 1.00 61.02 C ANISOU 3740 CA ILE B 101 9690 6002 7493 -97 348 1082 C ATOM 3741 C ILE B 101 32.286 15.881 143.279 1.00 60.98 C ANISOU 3741 C ILE B 101 9684 5995 7489 -161 280 1139 C ATOM 3742 O ILE B 101 31.133 15.491 143.498 1.00 60.64 O ANISOU 3742 O ILE B 101 9629 5989 7421 -206 266 1128 O ATOM 3743 CB ILE B 101 32.778 17.320 141.276 1.00 60.88 C ANISOU 3743 CB ILE B 101 9701 5919 7511 3 350 1068 C ATOM 3744 CG1 ILE B 101 32.709 18.751 140.729 1.00 60.30 C ANISOU 3744 CG1 ILE B 101 9617 5850 7443 67 413 1036 C ATOM 3745 CG2 ILE B 101 31.765 16.433 140.537 1.00 61.14 C ANISOU 3745 CG2 ILE B 101 9741 5952 7538 2 317 1059 C ATOM 3746 CD1 ILE B 101 33.247 18.908 139.321 1.00 59.86 C ANISOU 3746 CD1 ILE B 101 9584 5756 7404 146 415 1038 C ATOM 3747 N ALA B 102 33.366 15.109 143.428 1.00 61.57 N ANISOU 3747 N ALA B 102 9763 6021 7608 -164 243 1209 N ATOM 3748 CA ALA B 102 33.256 13.719 143.925 1.00 62.52 C ANISOU 3748 CA ALA B 102 9872 6114 7767 -222 185 1291 C ATOM 3749 C ALA B 102 32.590 13.624 145.305 1.00 63.17 C ANISOU 3749 C ALA B 102 9916 6308 7778 -346 158 1335 C ATOM 3750 O ALA B 102 31.639 12.845 145.491 1.00 63.09 O ANISOU 3750 O ALA B 102 9904 6302 7763 -396 131 1349 O ATOM 3751 CB ALA B 102 34.621 13.045 143.952 1.00 62.84 C ANISOU 3751 CB ALA B 102 9898 6079 7898 -195 161 1384 C ATOM 3752 N VAL B 103 33.076 14.422 146.261 1.00 63.67 N ANISOU 3752 N VAL B 103 9946 6471 7771 -414 172 1348 N ATOM 3753 CA VAL B 103 32.473 14.433 147.609 1.00 64.54 C ANISOU 3753 CA VAL B 103 10014 6720 7787 -561 159 1371 C ATOM 3754 C VAL B 103 31.041 14.992 147.606 1.00 64.82 C ANISOU 3754 C VAL B 103 10052 6801 7774 -579 212 1256 C ATOM 3755 O VAL B 103 30.197 14.522 148.377 1.00 64.59 O ANISOU 3755 O VAL B 103 9996 6851 7692 -682 191 1274 O ATOM 3756 CB VAL B 103 33.349 15.128 148.688 1.00 65.05 C ANISOU 3756 CB VAL B 103 10035 6913 7768 -668 171 1398 C ATOM 3757 CG1 VAL B 103 34.718 14.463 148.769 1.00 65.48 C ANISOU 3757 CG1 VAL B 103 10062 6941 7876 -655 105 1548 C ATOM 3758 CG2 VAL B 103 33.494 16.625 148.457 1.00 65.08 C ANISOU 3758 CG2 VAL B 103 10054 6929 7742 -639 270 1259 C ATOM 3759 N ASP B 104 30.761 15.970 146.738 1.00 65.49 N ANISOU 3759 N ASP B 104 10157 6839 7886 -480 280 1153 N ATOM 3760 CA ASP B 104 29.371 16.440 146.561 1.00 66.17 C ANISOU 3760 CA ASP B 104 10227 6951 7962 -470 329 1070 C ATOM 3761 C ASP B 104 28.466 15.323 146.024 1.00 66.80 C ANISOU 3761 C ASP B 104 10318 7004 8059 -458 270 1102 C ATOM 3762 O ASP B 104 27.363 15.123 146.533 1.00 66.52 O ANISOU 3762 O ASP B 104 10251 7038 7983 -528 272 1083 O ATOM 3763 CB ASP B 104 29.291 17.659 145.638 1.00 65.96 C ANISOU 3763 CB ASP B 104 10203 6870 7988 -355 406 996 C ATOM 3764 CG ASP B 104 27.888 18.247 145.572 1.00 66.30 C ANISOU 3764 CG ASP B 104 10201 6945 8045 -342 464 934 C ATOM 3765 OD1 ASP B 104 27.391 18.726 146.614 1.00 67.15 O ANISOU 3765 OD1 ASP B 104 10267 7125 8122 -432 527 875 O ATOM 3766 OD2 ASP B 104 27.278 18.220 144.484 1.00 65.91 O ANISOU 3766 OD2 ASP B 104 10147 6860 8035 -251 451 946 O ATOM 3767 N ARG B 105 28.940 14.608 145.001 1.00 67.75 N ANISOU 3767 N ARG B 105 10478 7027 8237 -382 230 1136 N ATOM 3768 CA ARG B 105 28.239 13.415 144.496 1.00 69.03 C ANISOU 3768 CA ARG B 105 10656 7152 8418 -395 183 1155 C ATOM 3769 C ARG B 105 28.058 12.339 145.576 1.00 70.39 C ANISOU 3769 C ARG B 105 10814 7351 8577 -512 131 1234 C ATOM 3770 O ARG B 105 27.000 11.705 145.648 1.00 70.65 O ANISOU 3770 O ARG B 105 10840 7411 8590 -568 111 1229 O ATOM 3771 CB ARG B 105 28.972 12.801 143.292 1.00 69.27 C ANISOU 3771 CB ARG B 105 10731 7066 8519 -317 172 1157 C ATOM 3772 CG ARG B 105 28.767 13.516 141.963 1.00 69.09 C ANISOU 3772 CG ARG B 105 10719 7041 8491 -228 207 1090 C ATOM 3773 CD ARG B 105 27.311 13.496 141.512 1.00 69.36 C ANISOU 3773 CD ARG B 105 10728 7147 8478 -250 203 1054 C ATOM 3774 NE ARG B 105 26.647 14.790 141.676 1.00 68.69 N ANISOU 3774 NE ARG B 105 10590 7140 8366 -218 243 1037 N ATOM 3775 CZ ARG B 105 25.383 15.038 141.339 1.00 68.95 C ANISOU 3775 CZ ARG B 105 10574 7251 8372 -220 248 1026 C ATOM 3776 NH1 ARG B 105 24.604 14.084 140.832 1.00 69.53 N ANISOU 3776 NH1 ARG B 105 10648 7356 8411 -272 207 1021 N ATOM 3777 NH2 ARG B 105 24.883 16.250 141.527 1.00 69.36 N ANISOU 3777 NH2 ARG B 105 10565 7345 8442 -176 300 1021 N ATOM 3778 N TYR B 106 29.086 12.130 146.402 1.00 71.17 N ANISOU 3778 N TYR B 106 10901 7454 8686 -555 104 1322 N ATOM 3779 CA TYR B 106 28.977 11.215 147.550 1.00 72.01 C ANISOU 3779 CA TYR B 106 10975 7611 8773 -680 47 1434 C ATOM 3780 C TYR B 106 27.900 11.659 148.544 1.00 72.96 C ANISOU 3780 C TYR B 106 11056 7887 8777 -799 63 1393 C ATOM 3781 O TYR B 106 26.988 10.889 148.853 1.00 73.22 O ANISOU 3781 O TYR B 106 11079 7948 8791 -873 33 1419 O ATOM 3782 CB TYR B 106 30.325 11.089 148.266 1.00 72.14 C ANISOU 3782 CB TYR B 106 10961 7640 8809 -711 12 1559 C ATOM 3783 CG TYR B 106 30.299 10.221 149.502 1.00 72.80 C ANISOU 3783 CG TYR B 106 10992 7803 8866 -852 -56 1714 C ATOM 3784 CD1 TYR B 106 30.207 8.835 149.396 1.00 73.59 C ANISOU 3784 CD1 TYR B 106 11091 7792 9076 -857 -106 1829 C ATOM 3785 CD2 TYR B 106 30.372 10.782 150.781 1.00 73.03 C ANISOU 3785 CD2 TYR B 106 10964 8022 8759 -995 -65 1748 C ATOM 3786 CE1 TYR B 106 30.185 8.028 150.527 1.00 74.86 C ANISOU 3786 CE1 TYR B 106 11194 8026 9224 -988 -175 2002 C ATOM 3787 CE2 TYR B 106 30.351 9.984 151.916 1.00 74.48 C ANISOU 3787 CE2 TYR B 106 11089 8309 8900 -1143 -137 1912 C ATOM 3788 CZ TYR B 106 30.258 8.607 151.783 1.00 75.24 C ANISOU 3788 CZ TYR B 106 11182 8288 9118 -1133 -198 2054 C ATOM 3789 OH TYR B 106 30.233 7.801 152.894 1.00 76.42 O ANISOU 3789 OH TYR B 106 11263 8536 9237 -1280 -275 2247 O ATOM 3790 N LEU B 107 28.010 12.897 149.029 1.00 73.76 N ANISOU 3790 N LEU B 107 11133 8083 8807 -822 123 1318 N ATOM 3791 CA LEU B 107 27.093 13.423 150.061 1.00 74.66 C ANISOU 3791 CA LEU B 107 11200 8349 8816 -949 166 1254 C ATOM 3792 C LEU B 107 25.603 13.344 149.696 1.00 74.97 C ANISOU 3792 C LEU B 107 11230 8398 8854 -936 190 1179 C ATOM 3793 O LEU B 107 24.778 13.051 150.563 1.00 75.50 O ANISOU 3793 O LEU B 107 11260 8575 8849 -1062 187 1179 O ATOM 3794 CB LEU B 107 27.451 14.870 150.427 1.00 74.66 C ANISOU 3794 CB LEU B 107 11179 8412 8774 -961 262 1145 C ATOM 3795 CG LEU B 107 28.734 15.060 151.240 1.00 75.05 C ANISOU 3795 CG LEU B 107 11212 8536 8766 -1052 247 1207 C ATOM 3796 CD1 LEU B 107 29.180 16.514 151.199 1.00 74.78 C ANISOU 3796 CD1 LEU B 107 11177 8509 8726 -1028 356 1077 C ATOM 3797 CD2 LEU B 107 28.561 14.591 152.676 1.00 76.23 C ANISOU 3797 CD2 LEU B 107 11306 8869 8789 -1264 210 1274 C ATOM 3798 N ARG B 108 25.268 13.598 148.430 1.00 75.08 N ANISOU 3798 N ARG B 108 11269 8316 8939 -797 211 1125 N ATOM 3799 CA ARG B 108 23.870 13.543 147.961 1.00 75.60 C ANISOU 3799 CA ARG B 108 11310 8407 9004 -780 227 1072 C ATOM 3800 C ARG B 108 23.239 12.174 148.211 1.00 76.18 C ANISOU 3800 C ARG B 108 11391 8498 9054 -873 154 1137 C ATOM 3801 O ARG B 108 22.191 12.068 148.858 1.00 76.28 O ANISOU 3801 O ARG B 108 11360 8613 9008 -966 164 1114 O ATOM 3802 CB ARG B 108 23.779 13.880 146.468 1.00 74.96 C ANISOU 3802 CB ARG B 108 11249 8242 8990 -633 238 1042 C ATOM 3803 CG ARG B 108 24.031 15.346 146.155 1.00 74.79 C ANISOU 3803 CG ARG B 108 11203 8206 9006 -539 321 982 C ATOM 3804 CD ARG B 108 24.306 15.563 144.677 1.00 74.54 C ANISOU 3804 CD ARG B 108 11195 8095 9028 -408 312 992 C ATOM 3805 NE ARG B 108 23.120 15.313 143.867 1.00 74.94 N ANISOU 3805 NE ARG B 108 11210 8187 9075 -386 293 994 N ATOM 3806 CZ ARG B 108 22.100 16.157 143.694 1.00 75.40 C ANISOU 3806 CZ ARG B 108 11189 8303 9156 -347 343 976 C ATOM 3807 NH1 ARG B 108 22.080 17.362 144.274 1.00 75.56 N ANISOU 3807 NH1 ARG B 108 11160 8321 9226 -318 435 935 N ATOM 3808 NH2 ARG B 108 21.081 15.784 142.920 1.00 75.85 N ANISOU 3808 NH2 ARG B 108 11205 8419 9194 -341 307 999 N ATOM 3809 N VAL B 109 23.893 11.138 147.695 1.00 76.65 N ANISOU 3809 N VAL B 109 11501 8449 9172 -848 93 1212 N ATOM 3810 CA VAL B 109 23.445 9.757 147.884 1.00 77.95 C ANISOU 3810 CA VAL B 109 11679 8590 9348 -934 34 1282 C ATOM 3811 C VAL B 109 23.670 9.239 149.322 1.00 79.23 C ANISOU 3811 C VAL B 109 11810 8828 9463 -1077 -7 1391 C ATOM 3812 O VAL B 109 22.891 8.410 149.804 1.00 80.56 O ANISOU 3812 O VAL B 109 11965 9038 9605 -1183 -41 1436 O ATOM 3813 CB VAL B 109 24.067 8.794 146.827 1.00 78.17 C ANISOU 3813 CB VAL B 109 11765 8451 9485 -866 9 1311 C ATOM 3814 CG1 VAL B 109 25.574 8.625 147.002 1.00 78.27 C ANISOU 3814 CG1 VAL B 109 11793 8368 9575 -824 -6 1399 C ATOM 3815 CG2 VAL B 109 23.388 7.432 146.869 1.00 79.37 C ANISOU 3815 CG2 VAL B 109 11930 8559 9666 -956 -25 1353 C ATOM 3816 N LYS B 110 24.715 9.721 150.000 1.00 78.84 N ANISOU 3816 N LYS B 110 11744 8814 9395 -1095 -8 1443 N ATOM 3817 CA LYS B 110 25.031 9.254 151.358 1.00 79.65 C ANISOU 3817 CA LYS B 110 11803 9024 9435 -1249 -59 1573 C ATOM 3818 C LYS B 110 24.086 9.825 152.422 1.00 80.55 C ANISOU 3818 C LYS B 110 11862 9338 9403 -1395 -22 1506 C ATOM 3819 O LYS B 110 23.617 9.082 153.284 1.00 82.19 O ANISOU 3819 O LYS B 110 12038 9638 9551 -1540 -69 1594 O ATOM 3820 CB LYS B 110 26.491 9.568 151.716 1.00 79.52 C ANISOU 3820 CB LYS B 110 11772 9009 9430 -1239 -76 1659 C ATOM 3821 CG LYS B 110 26.965 9.050 153.072 1.00 80.77 C ANISOU 3821 CG LYS B 110 11866 9301 9518 -1408 -145 1835 C ATOM 3822 CD LYS B 110 26.990 7.530 153.150 1.00 81.83 C ANISOU 3822 CD LYS B 110 11994 9339 9758 -1436 -229 2023 C ATOM 3823 CE LYS B 110 27.406 7.061 154.532 1.00 83.30 C ANISOU 3823 CE LYS B 110 12098 9686 9867 -1615 -307 2233 C ATOM 3824 NZ LYS B 110 27.441 5.577 154.619 1.00 84.51 N ANISOU 3824 NZ LYS B 110 12233 9720 10157 -1636 -383 2443 N ATOM 3825 N ILE B 111 23.825 11.134 152.370 1.00 80.58 N ANISOU 3825 N ILE B 111 11852 9402 9363 -1361 69 1352 N ATOM 3826 CA ILE B 111 22.972 11.810 153.364 1.00 81.75 C ANISOU 3826 CA ILE B 111 11940 9727 9393 -1497 139 1252 C ATOM 3827 C ILE B 111 21.894 12.672 152.682 1.00 82.78 C ANISOU 3827 C ILE B 111 12055 9834 9563 -1398 234 1090 C ATOM 3828 O ILE B 111 21.884 13.899 152.829 1.00 82.55 O ANISOU 3828 O ILE B 111 11996 9835 9532 -1378 341 965 O ATOM 3829 CB ILE B 111 23.811 12.626 154.389 1.00 81.60 C ANISOU 3829 CB ILE B 111 11886 9841 9277 -1613 183 1230 C ATOM 3830 CG1 ILE B 111 24.802 13.578 153.699 1.00 80.67 C ANISOU 3830 CG1 ILE B 111 11800 9620 9231 -1475 234 1170 C ATOM 3831 CG2 ILE B 111 24.575 11.683 155.306 1.00 82.22 C ANISOU 3831 CG2 ILE B 111 11940 10011 9286 -1761 76 1425 C ATOM 3832 CD1 ILE B 111 25.349 14.666 154.594 1.00 81.25 C ANISOU 3832 CD1 ILE B 111 11836 9824 9209 -1591 322 1077 C ATOM 3833 N PRO B 112 20.963 12.025 151.948 1.00 84.57 N ANISOU 3833 N PRO B 112 12291 10007 9833 -1344 201 1098 N ATOM 3834 CA PRO B 112 19.944 12.768 151.190 1.00 86.02 C ANISOU 3834 CA PRO B 112 12441 10176 10064 -1240 274 986 C ATOM 3835 C PRO B 112 18.974 13.603 152.043 1.00 88.93 C ANISOU 3835 C PRO B 112 12725 10680 10384 -1325 381 868 C ATOM 3836 O PRO B 112 18.532 14.664 151.592 1.00 89.73 O ANISOU 3836 O PRO B 112 12781 10754 10558 -1223 477 772 O ATOM 3837 CB PRO B 112 19.195 11.666 150.426 1.00 85.42 C ANISOU 3837 CB PRO B 112 12385 10057 10010 -1222 199 1039 C ATOM 3838 CG PRO B 112 19.412 10.431 151.221 1.00 85.59 C ANISOU 3838 CG PRO B 112 12431 10107 9982 -1364 117 1151 C ATOM 3839 CD PRO B 112 20.769 10.566 151.843 1.00 85.04 C ANISOU 3839 CD PRO B 112 12380 10026 9902 -1393 100 1219 C ATOM 3840 N LEU B 113 18.661 13.141 153.254 1.00 92.07 N ANISOU 3840 N LEU B 113 13092 11218 10670 -1512 371 880 N ATOM 3841 CA LEU B 113 17.754 13.864 154.154 1.00 94.73 C ANISOU 3841 CA LEU B 113 13344 11696 10952 -1620 488 749 C ATOM 3842 C LEU B 113 18.365 15.168 154.675 1.00 96.39 C ANISOU 3842 C LEU B 113 13529 11926 11166 -1638 618 624 C ATOM 3843 O LEU B 113 17.692 16.197 154.704 1.00 97.80 O ANISOU 3843 O LEU B 113 13642 12108 11409 -1601 759 480 O ATOM 3844 CB LEU B 113 17.340 12.974 155.332 1.00 96.31 C ANISOU 3844 CB LEU B 113 13519 12062 11010 -1843 439 801 C ATOM 3845 CG LEU B 113 16.521 11.729 154.973 1.00 96.80 C ANISOU 3845 CG LEU B 113 13594 12116 11069 -1858 337 899 C ATOM 3846 CD1 LEU B 113 16.480 10.751 156.140 1.00 97.87 C ANISOU 3846 CD1 LEU B 113 13719 12394 11072 -2081 265 1002 C ATOM 3847 CD2 LEU B 113 15.113 12.113 154.537 1.00 96.98 C ANISOU 3847 CD2 LEU B 113 13547 12164 11134 -1801 408 795 C ATOM 3848 N ARG B 114 19.635 15.113 155.075 1.00 97.75 N ANISOU 3848 N ARG B 114 13747 12109 11284 -1696 577 681 N ATOM 3849 CA ARG B 114 20.367 16.276 155.599 1.00 99.52 C ANISOU 3849 CA ARG B 114 13957 12364 11492 -1742 695 563 C ATOM 3850 C ARG B 114 21.212 17.036 154.550 1.00 99.01 C ANISOU 3850 C ARG B 114 13939 12120 11560 -1544 721 552 C ATOM 3851 O ARG B 114 21.845 18.049 154.887 1.00 99.29 O ANISOU 3851 O ARG B 114 13967 12159 11599 -1574 828 448 O ATOM 3852 CB ARG B 114 21.249 15.831 156.779 1.00101.52 C ANISOU 3852 CB ARG B 114 14211 12783 11578 -1962 637 636 C ATOM 3853 CG ARG B 114 20.450 15.416 158.015 1.00103.95 C ANISOU 3853 CG ARG B 114 14455 13309 11730 -2202 651 612 C ATOM 3854 CD ARG B 114 21.203 14.458 158.939 1.00105.24 C ANISOU 3854 CD ARG B 114 14616 13633 11735 -2400 519 794 C ATOM 3855 NE ARG B 114 22.466 15.016 159.443 1.00106.16 N ANISOU 3855 NE ARG B 114 14732 13828 11776 -2490 536 795 N ATOM 3856 CZ ARG B 114 23.697 14.708 159.015 1.00105.63 C ANISOU 3856 CZ ARG B 114 14707 13676 11752 -2405 434 949 C ATOM 3857 NH1 ARG B 114 23.909 13.817 158.043 1.00104.50 N ANISOU 3857 NH1 ARG B 114 14618 13348 11739 -2222 312 1109 N ATOM 3858 NH2 ARG B 114 24.747 15.309 159.576 1.00106.20 N ANISOU 3858 NH2 ARG B 114 14762 13855 11734 -2516 463 932 N ATOM 3859 N TYR B 115 21.208 16.577 153.293 1.00 98.77 N ANISOU 3859 N TYR B 115 13953 11945 11630 -1361 635 647 N ATOM 3860 CA TYR B 115 22.042 17.182 152.234 1.00 98.16 C ANISOU 3860 CA TYR B 115 13920 11711 11662 -1183 643 658 C ATOM 3861 C TYR B 115 21.871 18.694 152.114 1.00 98.87 C ANISOU 3861 C TYR B 115 13966 11748 11851 -1113 809 511 C ATOM 3862 O TYR B 115 22.856 19.426 152.148 1.00 98.76 O ANISOU 3862 O TYR B 115 13977 11689 11856 -1100 861 473 O ATOM 3863 CB TYR B 115 21.774 16.542 150.862 1.00 96.97 C ANISOU 3863 CB TYR B 115 13805 11443 11593 -1020 550 751 C ATOM 3864 CG TYR B 115 22.546 17.202 149.728 1.00 95.69 C ANISOU 3864 CG TYR B 115 13681 11143 11534 -848 564 759 C ATOM 3865 CD1 TYR B 115 23.935 17.086 149.645 1.00 95.17 C ANISOU 3865 CD1 TYR B 115 13675 11027 11457 -836 519 813 C ATOM 3866 CD2 TYR B 115 21.892 17.953 148.749 1.00 95.19 C ANISOU 3866 CD2 TYR B 115 13580 11010 11577 -704 620 729 C ATOM 3867 CE1 TYR B 115 24.649 17.694 148.619 1.00 93.87 C ANISOU 3867 CE1 TYR B 115 13543 10746 11376 -691 534 818 C ATOM 3868 CE2 TYR B 115 22.598 18.558 147.715 1.00 94.27 C ANISOU 3868 CE2 TYR B 115 13492 10783 11543 -562 628 752 C ATOM 3869 CZ TYR B 115 23.976 18.429 147.656 1.00 93.36 C ANISOU 3869 CZ TYR B 115 13447 10618 11406 -558 588 786 C ATOM 3870 OH TYR B 115 24.683 19.028 146.637 1.00 92.48 O ANISOU 3870 OH TYR B 115 13362 10405 11368 -428 598 806 O ATOM 3871 N LYS B 116 20.628 19.149 151.977 1.00100.16 N ANISOU 3871 N LYS B 116 14056 11910 12090 -1070 896 437 N ATOM 3872 CA LYS B 116 20.346 20.577 151.755 1.00101.39 C ANISOU 3872 CA LYS B 116 14152 11978 12394 -976 1067 318 C ATOM 3873 C LYS B 116 20.752 21.463 152.935 1.00102.52 C ANISOU 3873 C LYS B 116 14272 12177 12503 -1129 1224 152 C ATOM 3874 O LYS B 116 21.228 22.580 152.724 1.00102.51 O ANISOU 3874 O LYS B 116 14265 12069 12613 -1063 1346 71 O ATOM 3875 CB LYS B 116 18.877 20.811 151.383 1.00102.62 C ANISOU 3875 CB LYS B 116 14209 12124 12656 -895 1126 298 C ATOM 3876 CG LYS B 116 18.557 20.424 149.945 1.00102.36 C ANISOU 3876 CG LYS B 116 14181 12015 12693 -717 1013 441 C ATOM 3877 CD LYS B 116 17.148 20.822 149.554 1.00103.53 C ANISOU 3877 CD LYS B 116 14207 12169 12960 -632 1078 440 C ATOM 3878 CE LYS B 116 16.846 20.458 148.107 1.00102.89 C ANISOU 3878 CE LYS B 116 14120 12052 12920 -485 960 590 C ATOM 3879 NZ LYS B 116 16.816 18.986 147.878 1.00102.12 N ANISOU 3879 NZ LYS B 116 14095 12033 12673 -557 792 671 N ATOM 3880 N MET B 117 20.571 20.974 154.161 1.00103.91 N ANISOU 3880 N MET B 117 14431 12527 12520 -1346 1227 100 N ATOM 3881 CA MET B 117 21.056 21.699 155.343 1.00105.87 C ANISOU 3881 CA MET B 117 14660 12874 12689 -1541 1368 -62 C ATOM 3882 C MET B 117 22.583 21.606 155.511 1.00104.27 C ANISOU 3882 C MET B 117 14531 12698 12385 -1606 1293 0 C ATOM 3883 O MET B 117 23.194 22.540 156.033 1.00105.45 O ANISOU 3883 O MET B 117 14675 12864 12525 -1700 1427 -138 O ATOM 3884 CB MET B 117 20.317 21.277 156.629 1.00108.63 C ANISOU 3884 CB MET B 117 14952 13437 12884 -1781 1406 -144 C ATOM 3885 CG MET B 117 20.550 19.854 157.127 1.00109.50 C ANISOU 3885 CG MET B 117 15098 13709 12798 -1921 1210 23 C ATOM 3886 SD MET B 117 20.195 19.673 158.890 1.00113.02 S ANISOU 3886 SD MET B 117 15477 14453 13012 -2276 1279 -88 S ATOM 3887 CE MET B 117 21.594 20.532 159.612 1.00113.78 C ANISOU 3887 CE MET B 117 15590 14633 13007 -2442 1368 -190 C ATOM 3888 N VAL B 118 23.194 20.499 155.074 1.00101.55 N ANISOU 3888 N VAL B 118 14249 12355 11978 -1561 1093 198 N ATOM 3889 CA VAL B 118 24.665 20.351 155.139 1.00 99.62 C ANISOU 3889 CA VAL B 118 14060 12127 11661 -1598 1012 284 C ATOM 3890 C VAL B 118 25.385 21.193 154.071 1.00 97.59 C ANISOU 3890 C VAL B 118 13845 11680 11552 -1404 1055 271 C ATOM 3891 O VAL B 118 26.126 22.116 154.410 1.00 97.07 O ANISOU 3891 O VAL B 118 13781 11618 11481 -1467 1160 167 O ATOM 3892 CB VAL B 118 25.110 18.865 155.054 1.00 98.97 C ANISOU 3892 CB VAL B 118 14016 12090 11497 -1610 801 508 C ATOM 3893 CG1 VAL B 118 26.626 18.732 154.893 1.00 98.40 C ANISOU 3893 CG1 VAL B 118 13986 11998 11401 -1596 720 618 C ATOM 3894 CG2 VAL B 118 24.651 18.099 156.293 1.00100.20 C ANISOU 3894 CG2 VAL B 118 14125 12460 11485 -1843 757 543 C ATOM 3895 N VAL B 119 25.172 20.858 152.797 1.00 95.99 N ANISOU 3895 N VAL B 119 13674 11328 11467 -1191 975 374 N ATOM 3896 CA VAL B 119 25.872 21.497 151.671 1.00 94.63 C ANISOU 3896 CA VAL B 119 13543 10991 11421 -1009 987 396 C ATOM 3897 C VAL B 119 25.139 22.764 151.215 1.00 94.17 C ANISOU 3897 C VAL B 119 13435 10813 11529 -897 1151 279 C ATOM 3898 O VAL B 119 24.225 22.701 150.389 1.00 93.63 O ANISOU 3898 O VAL B 119 13337 10673 11562 -758 1137 325 O ATOM 3899 CB VAL B 119 26.034 20.518 150.478 1.00 93.93 C ANISOU 3899 CB VAL B 119 13505 10816 11368 -854 828 560 C ATOM 3900 CG1 VAL B 119 26.773 21.187 149.315 1.00 93.53 C ANISOU 3900 CG1 VAL B 119 13491 10619 11427 -686 842 582 C ATOM 3901 CG2 VAL B 119 26.754 19.249 150.923 1.00 93.84 C ANISOU 3901 CG2 VAL B 119 13528 10886 11240 -950 683 687 C ATOM 3902 N THR B 120 25.556 23.909 151.754 1.00 94.27 N ANISOU 3902 N THR B 120 13431 10807 11577 -965 1312 134 N ATOM 3903 CA THR B 120 24.937 25.203 151.458 1.00 94.50 C ANISOU 3903 CA THR B 120 13402 10701 11801 -870 1499 17 C ATOM 3904 C THR B 120 25.802 26.033 150.503 1.00 93.78 C ANISOU 3904 C THR B 120 13348 10447 11837 -723 1529 51 C ATOM 3905 O THR B 120 27.026 25.843 150.456 1.00 93.34 O ANISOU 3905 O THR B 120 13360 10412 11690 -758 1455 95 O ATOM 3906 CB THR B 120 24.703 26.017 152.747 1.00 96.14 C ANISOU 3906 CB THR B 120 13558 10977 11994 -1062 1704 -204 C ATOM 3907 OG1 THR B 120 25.947 26.226 153.428 1.00 95.90 O ANISOU 3907 OG1 THR B 120 13576 11028 11833 -1225 1721 -266 O ATOM 3908 CG2 THR B 120 23.744 25.289 153.670 1.00 97.01 C ANISOU 3908 CG2 THR B 120 13620 11255 11984 -1213 1690 -245 C ATOM 3909 N PRO B 121 25.173 26.965 149.751 1.00 93.74 N ANISOU 3909 N PRO B 121 13286 10282 12046 -562 1639 44 N ATOM 3910 CA PRO B 121 25.889 27.846 148.818 1.00 93.64 C ANISOU 3910 CA PRO B 121 13296 10109 12173 -423 1680 88 C ATOM 3911 C PRO B 121 27.149 28.499 149.394 1.00 94.37 C ANISOU 3911 C PRO B 121 13442 10193 12220 -541 1768 -25 C ATOM 3912 O PRO B 121 28.200 28.481 148.746 1.00 94.26 O ANISOU 3912 O PRO B 121 13492 10141 12179 -483 1686 60 O ATOM 3913 CB PRO B 121 24.845 28.910 148.481 1.00 94.73 C ANISOU 3913 CB PRO B 121 13328 10099 12563 -301 1848 54 C ATOM 3914 CG PRO B 121 23.549 28.195 148.584 1.00 94.60 C ANISOU 3914 CG PRO B 121 13245 10171 12528 -291 1794 93 C ATOM 3915 CD PRO B 121 23.713 27.180 149.676 1.00 94.15 C ANISOU 3915 CD PRO B 121 13236 10302 12232 -494 1718 26 C ATOM 3916 N ARG B 122 27.038 29.056 150.601 1.00 95.97 N ANISOU 3916 N ARG B 122 13615 10446 12403 -720 1937 -223 N ATOM 3917 CA ARG B 122 28.177 29.699 151.274 1.00 96.85 C ANISOU 3917 CA ARG B 122 13767 10583 12448 -878 2037 -357 C ATOM 3918 C ARG B 122 29.313 28.705 151.558 1.00 94.00 C ANISOU 3918 C ARG B 122 13478 10396 11841 -989 1848 -262 C ATOM 3919 O ARG B 122 30.492 29.017 151.336 1.00 93.47 O ANISOU 3919 O ARG B 122 13459 10307 11745 -999 1832 -245 O ATOM 3920 CB ARG B 122 27.725 30.390 152.575 1.00100.78 C ANISOU 3920 CB ARG B 122 14209 11135 12947 -1087 2264 -610 C ATOM 3921 CG ARG B 122 28.730 31.384 153.143 1.00103.48 C ANISOU 3921 CG ARG B 122 14577 11462 13279 -1244 2431 -788 C ATOM 3922 CD ARG B 122 28.221 32.030 154.426 1.00106.78 C ANISOU 3922 CD ARG B 122 14935 11945 13689 -1477 2675 -1067 C ATOM 3923 NE ARG B 122 28.125 31.063 155.524 1.00108.26 N ANISOU 3923 NE ARG B 122 15115 12421 13594 -1711 2581 -1092 N ATOM 3924 CZ ARG B 122 29.152 30.594 156.242 1.00109.12 C ANISOU 3924 CZ ARG B 122 15263 12758 13437 -1929 2484 -1083 C ATOM 3925 NH1 ARG B 122 30.408 30.987 156.009 1.00109.41 N ANISOU 3925 NH1 ARG B 122 15352 12775 13440 -1950 2468 -1065 N ATOM 3926 NH2 ARG B 122 28.920 29.711 157.213 1.00109.48 N ANISOU 3926 NH2 ARG B 122 15283 13065 13246 -2135 2397 -1075 N ATOM 3927 N ARG B 123 28.953 27.507 152.021 1.00 91.63 N ANISOU 3927 N ARG B 123 13174 10259 11381 -1066 1705 -186 N ATOM 3928 CA ARG B 123 29.935 26.447 152.273 1.00 89.42 C ANISOU 3928 CA ARG B 123 12940 10131 10903 -1153 1518 -56 C ATOM 3929 C ARG B 123 30.583 25.966 150.976 1.00 86.40 C ANISOU 3929 C ARG B 123 12613 9640 10573 -951 1364 127 C ATOM 3930 O ARG B 123 31.796 25.742 150.934 1.00 85.91 O ANISOU 3930 O ARG B 123 12589 9620 10431 -982 1286 194 O ATOM 3931 CB ARG B 123 29.299 25.278 153.028 1.00 89.45 C ANISOU 3931 CB ARG B 123 12918 10310 10758 -1273 1410 0 C ATOM 3932 CG ARG B 123 29.131 25.548 154.519 1.00 91.18 C ANISOU 3932 CG ARG B 123 13089 10720 10835 -1550 1525 -162 C ATOM 3933 CD ARG B 123 28.236 24.520 155.186 1.00 91.69 C ANISOU 3933 CD ARG B 123 13116 10939 10782 -1654 1442 -112 C ATOM 3934 NE ARG B 123 28.613 24.248 156.578 1.00 92.83 N ANISOU 3934 NE ARG B 123 13228 11344 10698 -1952 1441 -156 N ATOM 3935 CZ ARG B 123 28.014 23.358 157.367 1.00 93.06 C ANISOU 3935 CZ ARG B 123 13218 11553 10585 -2099 1366 -104 C ATOM 3936 NH1 ARG B 123 26.981 22.637 156.935 1.00 92.25 N ANISOU 3936 NH1 ARG B 123 13110 11390 10548 -1978 1293 -23 N ATOM 3937 NH2 ARG B 123 28.447 23.188 158.614 1.00 94.55 N ANISOU 3937 NH2 ARG B 123 13368 12002 10553 -2387 1363 -128 N ATOM 3938 N ALA B 124 29.775 25.825 149.924 1.00 83.83 N ANISOU 3938 N ALA B 124 12282 9191 10376 -757 1328 204 N ATOM 3939 CA ALA B 124 30.288 25.521 148.583 1.00 81.03 C ANISOU 3939 CA ALA B 124 11973 8734 10081 -574 1213 349 C ATOM 3940 C ALA B 124 31.259 26.603 148.098 1.00 80.00 C ANISOU 3940 C ALA B 124 11868 8495 10031 -520 1297 315 C ATOM 3941 O ALA B 124 32.318 26.289 147.540 1.00 79.17 O ANISOU 3941 O ALA B 124 11812 8382 9887 -475 1203 404 O ATOM 3942 CB ALA B 124 29.142 25.356 147.597 1.00 80.45 C ANISOU 3942 CB ALA B 124 11870 8577 10118 -410 1183 421 C ATOM 3943 N ALA B 125 30.901 27.867 148.330 1.00 87.49 N ANISOU 3943 N ALA B 125 12548 9365 11329 -342 2322 368 N ATOM 3944 CA ALA B 125 31.773 28.999 147.993 1.00 86.57 C ANISOU 3944 CA ALA B 125 12396 9173 11323 -252 2342 433 C ATOM 3945 C ALA B 125 33.088 28.973 148.786 1.00 85.12 C ANISOU 3945 C ALA B 125 12449 9049 10843 -419 2326 378 C ATOM 3946 O ALA B 125 34.173 29.160 148.207 1.00 84.09 O ANISOU 3946 O ALA B 125 12360 8960 10628 -316 2171 516 O ATOM 3947 CB ALA B 125 31.044 30.316 148.213 1.00 88.65 C ANISOU 3947 CB ALA B 125 12464 9228 11989 -241 2623 316 C ATOM 3948 N VAL B 126 32.988 28.728 150.096 1.00 84.70 N ANISOU 3948 N VAL B 126 12548 9004 10628 -691 2480 182 N ATOM 3949 CA VAL B 126 34.180 28.574 150.954 1.00 83.23 C ANISOU 3949 CA VAL B 126 12598 8892 10131 -892 2436 142 C ATOM 3950 C VAL B 126 35.060 27.438 150.423 1.00 80.23 C ANISOU 3950 C VAL B 126 12332 8666 9486 -813 2104 337 C ATOM 3951 O VAL B 126 36.274 27.616 150.233 1.00 78.73 O ANISOU 3951 O VAL B 126 12213 8509 9190 -780 1974 430 O ATOM 3952 CB VAL B 126 33.801 28.326 152.444 1.00 84.69 C ANISOU 3952 CB VAL B 126 12945 9086 10146 -1237 2632 -85 C ATOM 3953 CG1 VAL B 126 35.013 27.910 153.278 1.00 84.20 C ANISOU 3953 CG1 VAL B 126 13138 9135 9717 -1460 2507 -74 C ATOM 3954 CG2 VAL B 126 33.149 29.565 153.051 1.00 87.13 C ANISOU 3954 CG2 VAL B 126 13154 9227 10723 -1350 3001 -315 C ATOM 3955 N ALA B 127 34.434 26.289 150.165 1.00 79.11 N ANISOU 3955 N ALA B 127 12189 8604 9263 -783 1980 389 N ATOM 3956 CA ALA B 127 35.120 25.135 149.571 1.00 76.74 C ANISOU 3956 CA ALA B 127 11964 8428 8764 -697 1686 562 C ATOM 3957 C ALA B 127 35.821 25.506 148.265 1.00 74.93 C ANISOU 3957 C ALA B 127 11630 8202 8637 -443 1539 735 C ATOM 3958 O ALA B 127 36.995 25.176 148.086 1.00 73.03 O ANISOU 3958 O ALA B 127 11481 8017 8250 -428 1370 830 O ATOM 3959 CB ALA B 127 34.150 23.982 149.345 1.00 76.36 C ANISOU 3959 CB ALA B 127 11889 8443 8680 -678 1615 578 C ATOM 3960 N ILE B 128 35.113 26.204 147.372 1.00 75.05 N ANISOU 3960 N ILE B 128 11450 8151 8913 -260 1603 777 N ATOM 3961 CA ILE B 128 35.715 26.680 146.118 1.00 74.66 C ANISOU 3961 CA ILE B 128 11305 8102 8959 -45 1481 942 C ATOM 3962 C ILE B 128 36.938 27.540 146.437 1.00 74.89 C ANISOU 3962 C ILE B 128 11410 8085 8959 -84 1519 931 C ATOM 3963 O ILE B 128 38.058 27.196 146.041 1.00 74.06 O ANISOU 3963 O ILE B 128 11381 8043 8714 -42 1353 1028 O ATOM 3964 CB ILE B 128 34.705 27.450 145.226 1.00 75.58 C ANISOU 3964 CB ILE B 128 11196 8139 9382 124 1548 1003 C ATOM 3965 CG1 ILE B 128 33.673 26.479 144.634 1.00 75.47 C ANISOU 3965 CG1 ILE B 128 11102 8201 9370 187 1444 1058 C ATOM 3966 CG2 ILE B 128 35.411 28.173 144.076 1.00 75.10 C ANISOU 3966 CG2 ILE B 128 11058 8064 9410 302 1451 1169 C ATOM 3967 CD1 ILE B 128 32.378 27.127 144.195 1.00 76.85 C ANISOU 3967 CD1 ILE B 128 11051 8282 9864 284 1542 1074 C ATOM 3968 N ALA B 129 36.725 28.623 147.185 1.00 76.42 N ANISOU 3968 N ALA B 129 11579 8162 9292 -177 1749 796 N ATOM 3969 CA ALA B 129 37.822 29.536 147.564 1.00 76.61 C ANISOU 3969 CA ALA B 129 11670 8135 9300 -233 1815 763 C ATOM 3970 C ALA B 129 39.045 28.791 148.119 1.00 75.62 C ANISOU 3970 C ALA B 129 11744 8113 8875 -366 1656 780 C ATOM 3971 O ALA B 129 40.194 29.078 147.733 1.00 74.20 O ANISOU 3971 O ALA B 129 11593 7942 8656 -304 1557 863 O ATOM 3972 CB ALA B 129 37.331 30.567 148.570 1.00 78.55 C ANISOU 3972 CB ALA B 129 11895 8252 9696 -388 2113 564 C ATOM 3973 N GLY B 130 38.782 27.824 149.002 1.00 75.86 N ANISOU 3973 N GLY B 130 11901 8212 8709 -551 1624 711 N ATOM 3974 CA GLY B 130 39.819 26.937 149.537 1.00 74.97 C ANISOU 3974 CA GLY B 130 11961 8193 8330 -684 1435 760 C ATOM 3975 C GLY B 130 40.642 26.249 148.465 1.00 73.23 C ANISOU 3975 C GLY B 130 11714 8031 8076 -499 1187 939 C ATOM 3976 O GLY B 130 41.884 26.239 148.543 1.00 72.86 O ANISOU 3976 O GLY B 130 11737 8000 7944 -523 1070 996 O ATOM 3977 N CYS B 131 39.955 25.696 147.457 1.00 72.31 N ANISOU 3977 N CYS B 131 11491 7945 8037 -327 1118 1017 N ATOM 3978 CA CYS B 131 40.634 25.026 146.338 1.00 71.21 C ANISOU 3978 CA CYS B 131 11319 7861 7875 -164 916 1162 C ATOM 3979 C CYS B 131 41.629 25.962 145.684 1.00 70.21 C ANISOU 3979 C CYS B 131 11149 7693 7835 -52 912 1222 C ATOM 3980 O CYS B 131 42.787 25.606 145.515 1.00 69.78 O ANISOU 3980 O CYS B 131 11145 7660 7706 -45 778 1282 O ATOM 3981 CB CYS B 131 39.650 24.533 145.273 1.00 71.40 C ANISOU 3981 CB CYS B 131 11224 7925 7980 -11 877 1223 C ATOM 3982 SG CYS B 131 38.421 23.363 145.874 1.00 73.02 S ANISOU 3982 SG CYS B 131 11461 8180 8100 -121 880 1157 S ATOM 3983 N TRP B 132 41.175 27.164 145.346 1.00 69.86 N ANISOU 3983 N TRP B 132 11001 7574 7968 29 1065 1203 N ATOM 3984 CA TRP B 132 42.041 28.163 144.728 1.00 69.23 C ANISOU 3984 CA TRP B 132 10877 7443 7983 131 1083 1259 C ATOM 3985 C TRP B 132 43.174 28.612 145.654 1.00 69.32 C ANISOU 3985 C TRP B 132 10999 7424 7913 -7 1111 1193 C ATOM 3986 O TRP B 132 44.320 28.711 145.212 1.00 68.17 O ANISOU 3986 O TRP B 132 10870 7284 7745 46 1018 1258 O ATOM 3987 CB TRP B 132 41.228 29.361 144.233 1.00 69.88 C ANISOU 3987 CB TRP B 132 10815 7433 8302 239 1239 1266 C ATOM 3988 CG TRP B 132 40.481 29.067 142.969 1.00 69.44 C ANISOU 3988 CG TRP B 132 10637 7416 8329 402 1152 1394 C ATOM 3989 CD1 TRP B 132 39.153 28.780 142.841 1.00 69.96 C ANISOU 3989 CD1 TRP B 132 10610 7487 8481 428 1180 1392 C ATOM 3990 CD2 TRP B 132 41.027 29.021 141.648 1.00 68.34 C ANISOU 3990 CD2 TRP B 132 10458 7325 8181 540 1020 1539 C ATOM 3991 NE1 TRP B 132 38.836 28.563 141.521 1.00 69.27 N ANISOU 3991 NE1 TRP B 132 10428 7456 8434 570 1056 1540 N ATOM 3992 CE2 TRP B 132 39.969 28.704 140.767 1.00 68.35 C ANISOU 3992 CE2 TRP B 132 10350 7370 8248 631 962 1629 C ATOM 3993 CE3 TRP B 132 42.309 29.220 141.122 1.00 67.70 C ANISOU 3993 CE3 TRP B 132 10423 7255 8043 579 951 1596 C ATOM 3994 CZ2 TRP B 132 40.152 28.583 139.390 1.00 68.28 C ANISOU 3994 CZ2 TRP B 132 10293 7428 8220 739 836 1776 C ATOM 3995 CZ3 TRP B 132 42.494 29.099 139.752 1.00 67.49 C ANISOU 3995 CZ3 TRP B 132 10346 7285 8011 692 845 1728 C ATOM 3996 CH2 TRP B 132 41.419 28.784 138.901 1.00 67.87 C ANISOU 3996 CH2 TRP B 132 10302 7388 8098 761 787 1818 C ATOM 3997 N ILE B 133 42.869 28.855 146.930 1.00 70.58 N ANISOU 3997 N ILE B 133 11236 7556 8022 -202 1239 1059 N ATOM 3998 CA ILE B 133 43.916 29.245 147.893 1.00 71.33 C ANISOU 3998 CA ILE B 133 11449 7640 8010 -375 1254 995 C ATOM 3999 C ILE B 133 45.006 28.164 147.943 1.00 70.68 C ANISOU 3999 C ILE B 133 11457 7636 7759 -413 1008 1089 C ATOM 4000 O ILE B 133 46.199 28.449 147.718 1.00 70.85 O ANISOU 4000 O ILE B 133 11488 7646 7783 -382 930 1139 O ATOM 4001 CB ILE B 133 43.340 29.502 149.310 1.00 72.97 C ANISOU 4001 CB ILE B 133 11750 7831 8143 -631 1426 826 C ATOM 4002 CG1 ILE B 133 42.433 30.739 149.305 1.00 74.30 C ANISOU 4002 CG1 ILE B 133 11806 7883 8540 -600 1704 710 C ATOM 4003 CG2 ILE B 133 44.453 29.704 150.341 1.00 73.58 C ANISOU 4003 CG2 ILE B 133 11972 7930 8055 -853 1397 776 C ATOM 4004 CD1 ILE B 133 41.365 30.706 150.377 1.00 75.77 C ANISOU 4004 CD1 ILE B 133 12035 8049 8704 -808 1896 536 C ATOM 4005 N LEU B 134 44.580 26.926 148.197 1.00 70.11 N ANISOU 4005 N LEU B 134 11436 7631 7571 -472 889 1116 N ATOM 4006 CA LEU B 134 45.507 25.792 148.266 1.00 69.15 C ANISOU 4006 CA LEU B 134 11379 7561 7334 -508 652 1215 C ATOM 4007 C LEU B 134 46.253 25.576 146.941 1.00 67.59 C ANISOU 4007 C LEU B 134 11085 7358 7238 -291 536 1323 C ATOM 4008 O LEU B 134 47.440 25.231 146.945 1.00 66.94 O ANISOU 4008 O LEU B 134 11025 7270 7138 -305 393 1384 O ATOM 4009 CB LEU B 134 44.759 24.520 148.689 1.00 69.46 C ANISOU 4009 CB LEU B 134 11473 7656 7261 -597 565 1226 C ATOM 4010 CG LEU B 134 45.560 23.275 149.080 1.00 69.59 C ANISOU 4010 CG LEU B 134 11566 7705 7167 -688 327 1325 C ATOM 4011 CD1 LEU B 134 46.486 23.535 150.262 1.00 70.49 C ANISOU 4011 CD1 LEU B 134 11800 7818 7162 -916 262 1325 C ATOM 4012 CD2 LEU B 134 44.603 22.119 149.374 1.00 69.67 C ANISOU 4012 CD2 LEU B 134 11617 7761 7094 -754 279 1330 C ATOM 4013 N SER B 135 45.561 25.808 145.821 1.00 67.22 N ANISOU 4013 N SER B 135 10929 7308 7302 -109 602 1346 N ATOM 4014 CA SER B 135 46.158 25.744 144.475 1.00 66.68 C ANISOU 4014 CA SER B 135 10776 7243 7315 72 531 1432 C ATOM 4015 C SER B 135 47.254 26.775 144.276 1.00 67.02 C ANISOU 4015 C SER B 135 10807 7230 7425 105 571 1437 C ATOM 4016 O SER B 135 48.317 26.448 143.747 1.00 67.00 O ANISOU 4016 O SER B 135 10792 7225 7440 155 466 1488 O ATOM 4017 CB SER B 135 45.105 25.961 143.392 1.00 66.26 C ANISOU 4017 CB SER B 135 10618 7207 7348 221 598 1464 C ATOM 4018 OG SER B 135 44.037 25.063 143.549 1.00 66.21 O ANISOU 4018 OG SER B 135 10612 7251 7291 192 573 1451 O ATOM 4019 N PHE B 136 46.980 28.017 144.678 1.00 67.39 N ANISOU 4019 N PHE B 136 10848 7224 7533 76 736 1375 N ATOM 4020 CA PHE B 136 48.008 29.060 144.692 1.00 67.60 C ANISOU 4020 CA PHE B 136 10875 7191 7616 77 792 1362 C ATOM 4021 C PHE B 136 49.159 28.684 145.636 1.00 67.84 C ANISOU 4021 C PHE B 136 11001 7230 7545 -77 679 1345 C ATOM 4022 O PHE B 136 50.329 28.862 145.280 1.00 67.03 O ANISOU 4022 O PHE B 136 10883 7103 7481 -38 615 1381 O ATOM 4023 CB PHE B 136 47.421 30.438 145.048 1.00 68.85 C ANISOU 4023 CB PHE B 136 11005 7274 7879 57 1011 1283 C ATOM 4024 CG PHE B 136 46.911 31.209 143.856 1.00 69.05 C ANISOU 4024 CG PHE B 136 10909 7255 8072 242 1094 1350 C ATOM 4025 CD1 PHE B 136 47.800 31.832 142.993 1.00 68.77 C ANISOU 4025 CD1 PHE B 136 10835 7187 8104 347 1084 1415 C ATOM 4026 CD2 PHE B 136 45.546 31.317 143.591 1.00 69.74 C ANISOU 4026 CD2 PHE B 136 10914 7328 8253 301 1172 1358 C ATOM 4027 CE1 PHE B 136 47.340 32.543 141.889 1.00 68.93 C ANISOU 4027 CE1 PHE B 136 10754 7170 8264 495 1141 1503 C ATOM 4028 CE2 PHE B 136 45.082 32.024 142.491 1.00 69.75 C ANISOU 4028 CE2 PHE B 136 10796 7287 8416 459 1216 1453 C ATOM 4029 CZ PHE B 136 45.981 32.638 141.638 1.00 69.37 C ANISOU 4029 CZ PHE B 136 10727 7215 8415 551 1194 1533 C ATOM 4030 N VAL B 137 48.836 28.140 146.813 1.00 69.12 N ANISOU 4030 N VAL B 137 11257 7425 7580 -263 644 1300 N ATOM 4031 CA VAL B 137 49.886 27.678 147.744 1.00 70.14 C ANISOU 4031 CA VAL B 137 11476 7570 7602 -435 493 1319 C ATOM 4032 C VAL B 137 50.793 26.619 147.090 1.00 69.88 C ANISOU 4032 C VAL B 137 11398 7542 7609 -342 280 1431 C ATOM 4033 O VAL B 137 52.019 26.762 147.093 1.00 70.40 O ANISOU 4033 O VAL B 137 11452 7576 7719 -353 193 1464 O ATOM 4034 CB VAL B 137 49.303 27.154 149.085 1.00 70.80 C ANISOU 4034 CB VAL B 137 11682 7701 7515 -676 472 1273 C ATOM 4035 CG1 VAL B 137 50.354 26.410 149.906 1.00 71.31 C ANISOU 4035 CG1 VAL B 137 11830 7792 7473 -848 248 1350 C ATOM 4036 CG2 VAL B 137 48.741 28.306 149.904 1.00 71.86 C ANISOU 4036 CG2 VAL B 137 11869 7815 7619 -823 702 1130 C ATOM 4037 N VAL B 138 50.188 25.578 146.524 1.00 69.36 N ANISOU 4037 N VAL B 138 11298 7507 7548 -256 210 1477 N ATOM 4038 CA VAL B 138 50.952 24.485 145.903 1.00 69.26 C ANISOU 4038 CA VAL B 138 11230 7483 7599 -179 35 1561 C ATOM 4039 C VAL B 138 51.709 24.966 144.658 1.00 68.44 C ANISOU 4039 C VAL B 138 11030 7340 7631 -8 76 1572 C ATOM 4040 O VAL B 138 52.895 24.665 144.485 1.00 68.31 O ANISOU 4040 O VAL B 138 10976 7278 7698 1 -28 1607 O ATOM 4041 CB VAL B 138 50.045 23.287 145.537 1.00 69.30 C ANISOU 4041 CB VAL B 138 11219 7528 7581 -134 -18 1588 C ATOM 4042 CG1 VAL B 138 50.804 22.238 144.719 1.00 69.08 C ANISOU 4042 CG1 VAL B 138 11114 7471 7661 -40 -151 1648 C ATOM 4043 CG2 VAL B 138 49.462 22.658 146.793 1.00 70.17 C ANISOU 4043 CG2 VAL B 138 11433 7672 7556 -322 -81 1588 C ATOM 4044 N GLY B 139 51.018 25.715 143.806 1.00 68.09 N ANISOU 4044 N GLY B 139 10943 7309 7619 112 226 1546 N ATOM 4045 CA GLY B 139 51.597 26.219 142.566 1.00 68.07 C ANISOU 4045 CA GLY B 139 10865 7281 7715 253 278 1562 C ATOM 4046 C GLY B 139 52.677 27.282 142.717 1.00 68.69 C ANISOU 4046 C GLY B 139 10944 7301 7854 238 327 1542 C ATOM 4047 O GLY B 139 53.613 27.307 141.918 1.00 68.32 O ANISOU 4047 O GLY B 139 10844 7221 7890 310 311 1555 O ATOM 4048 N LEU B 140 52.548 28.163 143.718 1.00 69.50 N ANISOU 4048 N LEU B 140 11103 7386 7917 134 406 1494 N ATOM 4049 CA LEU B 140 53.565 29.202 143.976 1.00 69.91 C ANISOU 4049 CA LEU B 140 11161 7383 8019 98 460 1462 C ATOM 4050 C LEU B 140 54.749 28.740 144.835 1.00 70.79 C ANISOU 4050 C LEU B 140 11305 7478 8114 -33 304 1473 C ATOM 4051 O LEU B 140 55.715 29.487 144.981 1.00 71.61 O ANISOU 4051 O LEU B 140 11402 7538 8268 -62 326 1451 O ATOM 4052 CB LEU B 140 52.942 30.458 144.607 1.00 70.13 C ANISOU 4052 CB LEU B 140 11224 7387 8033 35 642 1389 C ATOM 4053 CG LEU B 140 51.948 31.241 143.740 1.00 69.65 C ANISOU 4053 CG LEU B 140 11100 7305 8056 173 803 1396 C ATOM 4054 CD1 LEU B 140 51.310 32.360 144.548 1.00 70.52 C ANISOU 4054 CD1 LEU B 140 11231 7366 8195 89 990 1307 C ATOM 4055 CD2 LEU B 140 52.614 31.791 142.486 1.00 69.21 C ANISOU 4055 CD2 LEU B 140 10978 7215 8104 319 832 1449 C ATOM 4056 N THR B 141 54.694 27.534 145.403 1.00 71.11 N ANISOU 4056 N THR B 141 11373 7546 8096 -118 137 1518 N ATOM 4057 CA THR B 141 55.819 27.004 146.206 1.00 71.96 C ANISOU 4057 CA THR B 141 11495 7631 8214 -249 -52 1566 C ATOM 4058 C THR B 141 57.199 27.199 145.528 1.00 72.38 C ANISOU 4058 C THR B 141 11454 7612 8434 -164 -92 1581 C ATOM 4059 O THR B 141 58.111 27.755 146.158 1.00 73.06 O ANISOU 4059 O THR B 141 11552 7671 8535 -265 -132 1575 O ATOM 4060 CB THR B 141 55.568 25.540 146.648 1.00 71.69 C ANISOU 4060 CB THR B 141 11478 7618 8142 -317 -241 1644 C ATOM 4061 OG1 THR B 141 54.465 25.516 147.564 1.00 71.79 O ANISOU 4061 OG1 THR B 141 11600 7696 7981 -455 -202 1617 O ATOM 4062 CG2 THR B 141 56.799 24.930 147.329 1.00 72.66 C ANISOU 4062 CG2 THR B 141 11582 7695 8329 -434 -470 1731 C ATOM 4063 N PRO B 142 57.343 26.804 144.242 1.00 72.35 N ANISOU 4063 N PRO B 142 11358 7581 8550 5 -64 1587 N ATOM 4064 CA PRO B 142 58.574 27.106 143.495 1.00 73.06 C ANISOU 4064 CA PRO B 142 11359 7599 8802 82 -50 1572 C ATOM 4065 C PRO B 142 59.035 28.575 143.553 1.00 73.89 C ANISOU 4065 C PRO B 142 11483 7683 8908 73 86 1518 C ATOM 4066 O PRO B 142 60.238 28.830 143.644 1.00 74.26 O ANISOU 4066 O PRO B 142 11482 7669 9061 47 40 1512 O ATOM 4067 CB PRO B 142 58.213 26.717 142.061 1.00 72.18 C ANISOU 4067 CB PRO B 142 11186 7492 8745 238 35 1558 C ATOM 4068 CG PRO B 142 57.202 25.642 142.208 1.00 71.66 C ANISOU 4068 CG PRO B 142 11143 7478 8604 228 -35 1591 C ATOM 4069 CD PRO B 142 56.434 25.946 143.458 1.00 71.72 C ANISOU 4069 CD PRO B 142 11253 7536 8458 104 -51 1601 C ATOM 4070 N MET B 143 58.092 29.518 143.502 1.00 74.61 N ANISOU 4070 N MET B 143 11631 7811 8907 95 253 1480 N ATOM 4071 CA MET B 143 58.405 30.946 143.682 1.00 75.84 C ANISOU 4071 CA MET B 143 11807 7935 9071 72 398 1425 C ATOM 4072 C MET B 143 58.966 31.273 145.068 1.00 76.91 C ANISOU 4072 C MET B 143 12003 8070 9149 -120 334 1398 C ATOM 4073 O MET B 143 59.756 32.211 145.192 1.00 77.61 O ANISOU 4073 O MET B 143 12085 8117 9286 -151 400 1354 O ATOM 4074 CB MET B 143 57.179 31.833 143.421 1.00 76.18 C ANISOU 4074 CB MET B 143 11879 7995 9070 128 588 1398 C ATOM 4075 CG MET B 143 56.724 31.876 141.973 1.00 75.99 C ANISOU 4075 CG MET B 143 11798 7974 9101 301 664 1438 C ATOM 4076 SD MET B 143 57.614 33.095 140.982 1.00 77.25 S ANISOU 4076 SD MET B 143 11912 8064 9374 391 799 1429 S ATOM 4077 CE MET B 143 57.069 34.633 141.735 1.00 78.42 C ANISOU 4077 CE MET B 143 12097 8166 9532 339 982 1378 C ATOM 4078 N PHE B 144 58.565 30.521 146.099 1.00 77.22 N ANISOU 4078 N PHE B 144 12108 8159 9072 -265 205 1425 N ATOM 4079 CA PHE B 144 59.079 30.761 147.459 1.00 78.03 C ANISOU 4079 CA PHE B 144 12285 8280 9081 -493 122 1412 C ATOM 4080 C PHE B 144 60.539 30.335 147.644 1.00 78.13 C ANISOU 4080 C PHE B 144 12236 8251 9198 -543 -80 1477 C ATOM 4081 O PHE B 144 61.199 30.834 148.558 1.00 79.25 O ANISOU 4081 O PHE B 144 12420 8401 9288 -718 -131 1463 O ATOM 4082 CB PHE B 144 58.213 30.085 148.540 1.00 78.89 C ANISOU 4082 CB PHE B 144 12499 8462 9011 -669 40 1430 C ATOM 4083 CG PHE B 144 56.745 30.468 148.511 1.00 78.77 C ANISOU 4083 CG PHE B 144 12536 8480 8913 -646 240 1355 C ATOM 4084 CD1 PHE B 144 56.320 31.749 148.126 1.00 78.89 C ANISOU 4084 CD1 PHE B 144 12535 8458 8979 -571 488 1261 C ATOM 4085 CD2 PHE B 144 55.779 29.544 148.920 1.00 78.57 C ANISOU 4085 CD2 PHE B 144 12564 8509 8778 -707 178 1383 C ATOM 4086 CE1 PHE B 144 54.968 32.075 148.119 1.00 79.17 C ANISOU 4086 CE1 PHE B 144 12590 8502 8987 -549 662 1201 C ATOM 4087 CE2 PHE B 144 54.427 29.866 148.913 1.00 78.64 C ANISOU 4087 CE2 PHE B 144 12602 8537 8737 -689 360 1309 C ATOM 4088 CZ PHE B 144 54.020 31.131 148.508 1.00 79.15 C ANISOU 4088 CZ PHE B 144 12634 8557 8882 -607 600 1219 C ATOM 4089 N GLY B 145 61.045 29.434 146.793 1.00 77.01 N ANISOU 4089 N GLY B 145 11985 8059 9215 -404 -188 1540 N ATOM 4090 CA GLY B 145 62.441 28.980 146.896 1.00 77.52 C ANISOU 4090 CA GLY B 145 11954 8055 9444 -435 -376 1600 C ATOM 4091 C GLY B 145 62.777 27.600 146.347 1.00 77.31 C ANISOU 4091 C GLY B 145 11815 7969 9590 -343 -536 1680 C ATOM 4092 O GLY B 145 63.917 27.369 145.934 1.00 77.76 O ANISOU 4092 O GLY B 145 11746 7933 9865 -293 -609 1695 O ATOM 4093 N TRP B 146 61.807 26.680 146.349 1.00 76.26 N ANISOU 4093 N TRP B 146 11716 7875 9382 -328 -579 1721 N ATOM 4094 CA TRP B 146 62.051 25.298 145.926 1.00 76.24 C ANISOU 4094 CA TRP B 146 11608 7807 9551 -260 -726 1792 C ATOM 4095 C TRP B 146 62.248 25.192 144.401 1.00 76.22 C ANISOU 4095 C TRP B 146 11498 7747 9715 -59 -576 1717 C ATOM 4096 O TRP B 146 61.310 24.909 143.643 1.00 75.46 O ANISOU 4096 O TRP B 146 11421 7694 9555 38 -462 1682 O ATOM 4097 CB TRP B 146 60.916 24.380 146.409 1.00 75.71 C ANISOU 4097 CB TRP B 146 11620 7803 9341 -317 -803 1850 C ATOM 4098 CG TRP B 146 61.285 22.918 146.529 1.00 75.83 C ANISOU 4098 CG TRP B 146 11544 7742 9523 -329 -1023 1960 C ATOM 4099 CD1 TRP B 146 62.426 22.306 146.084 1.00 76.43 C ANISOU 4099 CD1 TRP B 146 11456 7688 9896 -266 -1129 1996 C ATOM 4100 CD2 TRP B 146 60.481 21.888 147.107 1.00 75.69 C ANISOU 4100 CD2 TRP B 146 11585 7759 9414 -407 -1148 2043 C ATOM 4101 NE1 TRP B 146 62.388 20.968 146.366 1.00 77.28 N ANISOU 4101 NE1 TRP B 146 11507 7736 10120 -296 -1318 2104 N ATOM 4102 CE2 TRP B 146 61.205 20.680 146.993 1.00 76.75 C ANISOU 4102 CE2 TRP B 146 11581 7772 9806 -384 -1338 2140 C ATOM 4103 CE3 TRP B 146 59.219 21.867 147.715 1.00 75.32 C ANISOU 4103 CE3 TRP B 146 11686 7822 9109 -498 -1109 2039 C ATOM 4104 CZ2 TRP B 146 60.709 19.458 147.465 1.00 76.96 C ANISOU 4104 CZ2 TRP B 146 11621 7786 9833 -447 -1499 2247 C ATOM 4105 CZ3 TRP B 146 58.729 20.655 148.190 1.00 75.84 C ANISOU 4105 CZ3 TRP B 146 11774 7886 9153 -569 -1265 2136 C ATOM 4106 CH2 TRP B 146 59.476 19.464 148.060 1.00 76.54 C ANISOU 4106 CH2 TRP B 146 11729 7854 9495 -542 -1463 2246 C ATOM 4107 N ASN B 147 63.489 25.416 143.972 1.00 77.61 N ANISOU 4107 N ASN B 147 11558 7827 10101 -19 -578 1691 N ATOM 4108 CA ASN B 147 63.849 25.438 142.548 1.00 77.85 C ANISOU 4108 CA ASN B 147 11495 7801 10284 131 -416 1601 C ATOM 4109 C ASN B 147 65.350 25.150 142.352 1.00 79.97 C ANISOU 4109 C ASN B 147 11599 7927 10858 137 -493 1593 C ATOM 4110 O ASN B 147 66.049 24.845 143.321 1.00 81.47 O ANISOU 4110 O ASN B 147 11739 8063 11152 35 -702 1681 O ATOM 4111 CB ASN B 147 63.427 26.785 141.929 1.00 76.77 C ANISOU 4111 CB ASN B 147 11439 7729 10002 192 -182 1519 C ATOM 4112 CG ASN B 147 63.904 27.983 142.731 1.00 76.99 C ANISOU 4112 CG ASN B 147 11518 7764 9969 103 -168 1510 C ATOM 4113 OD1 ASN B 147 65.102 28.226 142.849 1.00 77.29 O ANISOU 4113 OD1 ASN B 147 11477 7725 10164 74 -216 1499 O ATOM 4114 ND2 ASN B 147 62.963 28.754 143.264 1.00 76.78 N ANISOU 4114 ND2 ASN B 147 11616 7824 9729 54 -88 1504 N ATOM 4115 N ASN B 148 65.835 25.233 141.111 1.00 81.13 N ANISOU 4115 N ASN B 148 11660 8012 11153 242 -329 1490 N ATOM 4116 CA ASN B 148 67.252 24.982 140.787 1.00 83.20 C ANISOU 4116 CA ASN B 148 11748 8122 11740 255 -357 1450 C ATOM 4117 C ASN B 148 68.136 26.243 140.737 1.00 83.90 C ANISOU 4117 C ASN B 148 11830 8189 11859 242 -263 1391 C ATOM 4118 O ASN B 148 69.229 26.196 140.169 1.00 85.25 O ANISOU 4118 O ASN B 148 11862 8239 12290 271 -213 1319 O ATOM 4119 CB ASN B 148 67.359 24.257 139.436 1.00 83.63 C ANISOU 4119 CB ASN B 148 11705 8108 11962 347 -206 1343 C ATOM 4120 CG ASN B 148 66.534 22.984 139.378 1.00 83.73 C ANISOU 4120 CG ASN B 148 11712 8132 11969 360 -275 1381 C ATOM 4121 OD1 ASN B 148 66.452 22.236 140.354 1.00 85.07 O ANISOU 4121 OD1 ASN B 148 11859 8273 12191 303 -494 1499 O ATOM 4122 ND2 ASN B 148 65.929 22.723 138.222 1.00 82.89 N ANISOU 4122 ND2 ASN B 148 11629 8069 11795 420 -93 1287 N ATOM 4123 N LEU B 149 67.698 27.354 141.333 1.00 83.50 N ANISOU 4123 N LEU B 149 11918 8240 11567 192 -227 1408 N ATOM 4124 CA LEU B 149 68.458 28.610 141.261 1.00 83.89 C ANISOU 4124 CA LEU B 149 11970 8270 11633 179 -116 1344 C ATOM 4125 C LEU B 149 69.918 28.408 141.674 1.00 85.72 C ANISOU 4125 C LEU B 149 12044 8374 12149 124 -259 1355 C ATOM 4126 O LEU B 149 70.831 28.743 140.915 1.00 85.70 O ANISOU 4126 O LEU B 149 11943 8282 12335 173 -138 1262 O ATOM 4127 CB LEU B 149 67.807 29.695 142.131 1.00 83.39 C ANISOU 4127 CB LEU B 149 12063 8315 11304 100 -90 1368 C ATOM 4128 CG LEU B 149 68.493 31.062 142.231 1.00 83.29 C ANISOU 4128 CG LEU B 149 12069 8288 11288 67 24 1304 C ATOM 4129 CD1 LEU B 149 68.772 31.656 140.860 1.00 82.76 C ANISOU 4129 CD1 LEU B 149 11972 8179 11292 186 258 1207 C ATOM 4130 CD2 LEU B 149 67.640 32.015 143.055 1.00 82.91 C ANISOU 4130 CD2 LEU B 149 12175 8341 10985 -15 82 1311 C ATOM 4131 N SER B 150 70.119 27.832 142.860 1.00 87.19 N ANISOU 4131 N SER B 150 12204 8551 12372 13 -522 1477 N ATOM 4132 CA SER B 150 71.464 27.541 143.379 1.00 89.42 C ANISOU 4132 CA SER B 150 12320 8710 12945 -54 -716 1528 C ATOM 4133 C SER B 150 72.264 26.605 142.467 1.00 90.16 C ANISOU 4133 C SER B 150 12200 8633 13423 44 -699 1477 C ATOM 4134 O SER B 150 73.472 26.791 142.290 1.00 90.87 O ANISOU 4134 O SER B 150 12135 8600 13791 44 -704 1432 O ATOM 4135 CB SER B 150 71.373 26.938 144.781 1.00 90.85 C ANISOU 4135 CB SER B 150 12522 8921 13073 -209 -1030 1702 C ATOM 4136 OG SER B 150 70.674 27.808 145.650 1.00 90.99 O ANISOU 4136 OG SER B 150 12737 9091 12741 -332 -1019 1720 O ATOM 4137 N ALA B 151 71.585 25.608 141.899 1.00 89.85 N ANISOU 4137 N ALA B 151 12148 8582 13408 117 -666 1472 N ATOM 4138 CA ALA B 151 72.197 24.687 140.936 1.00 90.38 C ANISOU 4138 CA ALA B 151 12023 8487 13830 201 -596 1389 C ATOM 4139 C ALA B 151 72.645 25.399 139.656 1.00 90.27 C ANISOU 4139 C ALA B 151 11986 8442 13870 275 -292 1200 C ATOM 4140 O ALA B 151 73.713 25.086 139.125 1.00 91.40 O ANISOU 4140 O ALA B 151 11939 8421 14366 297 -239 1111 O ATOM 4141 CB ALA B 151 71.243 23.547 140.601 1.00 89.56 C ANISOU 4141 CB ALA B 151 11937 8398 13690 246 -597 1409 C ATOM 4142 N VAL B 152 71.844 26.354 139.176 1.00 88.97 N ANISOU 4142 N VAL B 152 12007 8423 13372 302 -96 1143 N ATOM 4143 CA VAL B 152 72.185 27.114 137.963 1.00 88.69 C ANISOU 4143 CA VAL B 152 11982 8378 13338 349 184 987 C ATOM 4144 C VAL B 152 73.265 28.171 138.242 1.00 89.92 C ANISOU 4144 C VAL B 152 12092 8479 13591 313 207 951 C ATOM 4145 O VAL B 152 74.147 28.398 137.402 1.00 91.22 O ANISOU 4145 O VAL B 152 12159 8545 13954 332 374 819 O ATOM 4146 CB VAL B 152 70.936 27.763 137.314 1.00 86.72 C ANISOU 4146 CB VAL B 152 11934 8292 12720 387 365 968 C ATOM 4147 CG1 VAL B 152 71.319 28.556 136.070 1.00 86.56 C ANISOU 4147 CG1 VAL B 152 11934 8263 12691 412 634 834 C ATOM 4148 CG2 VAL B 152 69.912 26.703 136.930 1.00 86.19 C ANISOU 4148 CG2 VAL B 152 11900 8277 12569 418 355 988 C ATOM 4149 N GLU B 153 73.188 28.818 139.407 1.00 90.33 N ANISOU 4149 N GLU B 153 12222 8601 13498 245 55 1054 N ATOM 4150 CA GLU B 153 74.206 29.793 139.842 1.00 91.87 C ANISOU 4150 CA GLU B 153 12374 8752 13777 189 48 1029 C ATOM 4151 C GLU B 153 75.619 29.201 139.909 1.00 94.50 C ANISOU 4151 C GLU B 153 12463 8901 14540 170 -64 1007 C ATOM 4152 O GLU B 153 76.594 29.876 139.562 1.00 95.42 O ANISOU 4152 O GLU B 153 12500 8940 14813 167 47 909 O ATOM 4153 CB GLU B 153 73.838 30.400 141.202 1.00 91.49 C ANISOU 4153 CB GLU B 153 12449 8814 13499 82 -117 1143 C ATOM 4154 CG GLU B 153 72.733 31.443 141.136 1.00 89.77 C ANISOU 4154 CG GLU B 153 12444 8741 12921 92 53 1123 C ATOM 4155 CD GLU B 153 72.234 31.891 142.505 1.00 89.72 C ANISOU 4155 CD GLU B 153 12561 8840 12686 -36 -86 1212 C ATOM 4156 OE1 GLU B 153 72.608 31.286 143.534 1.00 90.63 O ANISOU 4156 OE1 GLU B 153 12623 8942 12867 -147 -344 1313 O ATOM 4157 OE2 GLU B 153 71.454 32.865 142.554 1.00 88.99 O ANISOU 4157 OE2 GLU B 153 12620 8840 12352 -40 66 1182 O ATOM 4158 N ARG B 154 75.718 27.952 140.366 1.00 95.93 N ANISOU 4158 N ARG B 154 12517 9002 14928 157 -286 1105 N ATOM 4159 CA ARG B 154 76.987 27.212 140.364 1.00 98.32 C ANISOU 4159 CA ARG B 154 12549 9097 15707 153 -401 1097 C ATOM 4160 C ARG B 154 77.560 27.082 138.959 1.00 98.93 C ANISOU 4160 C ARG B 154 12506 9048 16034 233 -115 892 C ATOM 4161 O ARG B 154 78.729 27.378 138.743 1.00100.10 O ANISOU 4161 O ARG B 154 12493 9062 16475 223 -63 805 O ATOM 4162 CB ARG B 154 76.823 25.822 140.992 1.00 99.33 C ANISOU 4162 CB ARG B 154 12567 9153 16021 135 -674 1249 C ATOM 4163 CG ARG B 154 76.854 25.855 142.516 1.00100.02 C ANISOU 4163 CG ARG B 154 12689 9300 16013 5 -1019 1463 C ATOM 4164 CD ARG B 154 76.672 24.478 143.138 1.00101.36 C ANISOU 4164 CD ARG B 154 12758 9395 16359 -24 -1303 1639 C ATOM 4165 NE ARG B 154 75.262 24.145 143.353 1.00100.07 N ANISOU 4165 NE ARG B 154 12801 9387 15832 -28 -1309 1701 N ATOM 4166 CZ ARG B 154 74.817 23.038 143.953 1.00100.83 C ANISOU 4166 CZ ARG B 154 12876 9462 15972 -67 -1539 1861 C ATOM 4167 NH1 ARG B 154 75.663 22.115 144.414 1.00102.95 N ANISOU 4167 NH1 ARG B 154 12917 9551 16649 -102 -1802 1998 N ATOM 4168 NH2 ARG B 154 73.505 22.850 144.094 1.00 99.61 N ANISOU 4168 NH2 ARG B 154 12920 9458 15466 -72 -1508 1892 N ATOM 4169 N ALA B 155 76.730 26.642 138.019 1.00 98.47 N ANISOU 4169 N ALA B 155 12528 9035 15848 293 71 811 N ATOM 4170 CA ALA B 155 77.134 26.506 136.614 1.00 99.49 C ANISOU 4170 CA ALA B 155 12581 9072 16148 332 371 602 C ATOM 4171 C ALA B 155 77.424 27.853 135.940 1.00 99.70 C ANISOU 4171 C ALA B 155 12714 9157 16008 324 621 478 C ATOM 4172 O ALA B 155 78.306 27.934 135.083 1.00101.59 O ANISOU 4172 O ALA B 155 12835 9274 16489 318 824 309 O ATOM 4173 CB ALA B 155 76.076 25.743 135.829 1.00 98.48 C ANISOU 4173 CB ALA B 155 12541 9012 15864 367 494 558 C ATOM 4174 N TRP B 156 76.687 28.896 136.327 1.00 98.41 N ANISOU 4174 N TRP B 156 12767 9169 15454 317 617 558 N ATOM 4175 CA TRP B 156 76.899 30.259 135.798 1.00 97.61 C ANISOU 4175 CA TRP B 156 12775 9121 15189 308 834 471 C ATOM 4176 C TRP B 156 78.266 30.829 136.235 1.00 98.98 C ANISOU 4176 C TRP B 156 12803 9174 15630 267 796 428 C ATOM 4177 O TRP B 156 79.016 31.401 135.418 1.00 99.41 O ANISOU 4177 O TRP B 156 12816 9159 15796 259 1019 280 O ATOM 4178 CB TRP B 156 75.747 31.173 136.254 1.00 95.81 C ANISOU 4178 CB TRP B 156 12785 9084 14534 311 818 581 C ATOM 4179 CG TRP B 156 75.537 32.411 135.435 1.00 94.97 C ANISOU 4179 CG TRP B 156 12823 9048 14213 321 1070 512 C ATOM 4180 CD1 TRP B 156 75.559 33.699 135.885 1.00 94.38 C ANISOU 4180 CD1 TRP B 156 12847 9025 13986 300 1105 540 C ATOM 4181 CD2 TRP B 156 75.244 32.480 134.032 1.00 94.73 C ANISOU 4181 CD2 TRP B 156 12859 9042 14092 337 1317 416 C ATOM 4182 NE1 TRP B 156 75.314 34.568 134.849 1.00 94.02 N ANISOU 4182 NE1 TRP B 156 12914 9020 13786 317 1350 481 N ATOM 4183 CE2 TRP B 156 75.112 33.849 133.701 1.00 93.99 C ANISOU 4183 CE2 TRP B 156 12901 9010 13800 332 1474 413 C ATOM 4184 CE3 TRP B 156 75.086 31.520 133.021 1.00 95.22 C ANISOU 4184 CE3 TRP B 156 12881 9080 14218 338 1424 331 C ATOM 4185 CZ2 TRP B 156 74.840 34.285 132.397 1.00 93.95 C ANISOU 4185 CZ2 TRP B 156 12996 9048 13652 323 1710 352 C ATOM 4186 CZ3 TRP B 156 74.802 31.956 131.721 1.00 95.26 C ANISOU 4186 CZ3 TRP B 156 12997 9143 14055 313 1671 251 C ATOM 4187 CH2 TRP B 156 74.688 33.328 131.425 1.00 94.66 C ANISOU 4187 CH2 TRP B 156 13059 9132 13775 304 1798 275 C ATOM 4188 N ALA B 157 78.584 30.649 137.519 1.00 99.89 N ANISOU 4188 N ALA B 157 12842 9268 15842 224 510 561 N ATOM 4189 CA ALA B 157 79.893 31.018 138.076 1.00101.76 C ANISOU 4189 CA ALA B 157 12914 9387 16363 170 411 549 C ATOM 4190 C ALA B 157 81.020 30.127 137.544 1.00104.05 C ANISOU 4190 C ALA B 157 12922 9452 17158 188 435 444 C ATOM 4191 O ALA B 157 82.088 30.625 137.189 1.00104.47 O ANISOU 4191 O ALA B 157 12853 9393 17444 171 557 321 O ATOM 4192 CB ALA B 157 79.855 30.963 139.598 1.00102.05 C ANISOU 4192 CB ALA B 157 12952 9476 16343 88 72 739 C ATOM 4193 N ALA B 158 80.769 28.818 137.478 1.00105.61 N ANISOU 4193 N ALA B 158 13011 9574 17540 219 335 484 N ATOM 4194 CA ALA B 158 81.716 27.847 136.904 1.00107.78 C ANISOU 4194 CA ALA B 158 13005 9612 18332 240 388 370 C ATOM 4195 C ALA B 158 82.037 28.158 135.442 1.00108.19 C ANISOU 4195 C ALA B 158 13057 9610 18438 254 784 114 C ATOM 4196 O ALA B 158 83.190 28.052 135.022 1.00110.51 O ANISOU 4196 O ALA B 158 13133 9713 19142 239 895 -29 O ATOM 4197 CB ALA B 158 81.171 26.430 137.028 1.00108.14 C ANISOU 4197 CB ALA B 158 12971 9602 18514 272 246 453 C ATOM 4198 N ALA B 159 81.011 28.532 134.677 1.00106.36 N ANISOU 4198 N ALA B 159 13069 9546 17797 267 991 64 N ATOM 4199 CA ALA B 159 81.204 29.087 133.334 1.00105.93 C ANISOU 4199 CA ALA B 159 13081 9493 17672 243 1357 -147 C ATOM 4200 C ALA B 159 81.920 30.437 133.406 1.00105.95 C ANISOU 4200 C ALA B 159 13123 9506 17626 213 1445 -190 C ATOM 4201 O ALA B 159 82.687 30.776 132.504 1.00107.33 O ANISOU 4201 O ALA B 159 13238 9589 17953 174 1706 -381 O ATOM 4202 CB ALA B 159 79.872 29.233 132.613 1.00104.07 C ANISOU 4202 CB ALA B 159 13106 9453 16982 251 1501 -138 C ATOM 4203 N GLY B 160 81.647 31.205 134.466 1.00104.89 N ANISOU 4203 N GLY B 160 13095 9484 17272 214 1246 -26 N ATOM 4204 CA GLY B 160 82.365 32.455 134.738 1.00105.00 C ANISOU 4204 CA GLY B 160 13128 9499 17268 178 1293 -55 C ATOM 4205 C GLY B 160 81.615 33.644 134.184 1.00103.27 C ANISOU 4205 C GLY B 160 13174 9443 16620 178 1502 -69 C ATOM 4206 O GLY B 160 82.199 34.490 133.504 1.00103.73 O ANISOU 4206 O GLY B 160 13254 9467 16691 149 1730 -196 O ATOM 4207 N SER B 161 80.318 33.702 134.490 1.00101.33 N ANISOU 4207 N SER B 161 13122 9364 16014 207 1419 68 N ATOM 4208 CA SER B 161 79.437 34.760 134.000 1.00 99.51 C ANISOU 4208 CA SER B 161 13133 9281 15395 217 1588 90 C ATOM 4209 C SER B 161 78.834 35.524 135.175 1.00 98.19 C ANISOU 4209 C SER B 161 13089 9227 14990 213 1425 238 C ATOM 4210 O SER B 161 78.498 34.932 136.204 1.00 97.97 O ANISOU 4210 O SER B 161 13034 9230 14957 206 1177 355 O ATOM 4211 CB SER B 161 78.335 34.157 133.138 1.00 98.52 C ANISOU 4211 CB SER B 161 13123 9246 15063 246 1678 102 C ATOM 4212 OG SER B 161 78.869 33.552 131.977 1.00 99.66 O ANISOU 4212 OG SER B 161 13177 9296 15391 217 1874 -62 O ATOM 4213 N MET B 162 78.704 36.839 135.007 1.00 97.43 N ANISOU 4213 N MET B 162 13128 9186 14705 203 1577 228 N ATOM 4214 CA MET B 162 78.252 37.733 136.075 1.00 96.67 C ANISOU 4214 CA MET B 162 13140 9174 14413 179 1482 326 C ATOM 4215 C MET B 162 76.731 37.859 136.096 1.00 93.75 C ANISOU 4215 C MET B 162 12952 8943 13722 221 1483 437 C ATOM 4216 O MET B 162 76.055 37.560 135.108 1.00 92.66 O ANISOU 4216 O MET B 162 12882 8846 13478 269 1595 439 O ATOM 4217 CB MET B 162 78.870 39.127 135.898 1.00 98.44 C ANISOU 4217 CB MET B 162 13405 9366 14629 148 1663 253 C ATOM 4218 CG MET B 162 80.391 39.162 135.791 1.00100.92 C ANISOU 4218 CG MET B 162 13540 9541 15264 104 1697 127 C ATOM 4219 SD MET B 162 81.261 38.547 137.252 1.00103.55 S ANISOU 4219 SD MET B 162 13682 9814 15847 34 1370 176 S ATOM 4220 CE MET B 162 81.404 36.789 136.910 1.00104.12 C ANISOU 4220 CE MET B 162 13577 9798 16185 77 1237 181 C ATOM 4221 N GLY B 163 76.206 38.305 137.235 1.00 91.87 N ANISOU 4221 N GLY B 163 12790 8777 13337 185 1362 523 N ATOM 4222 CA GLY B 163 74.783 38.607 137.379 1.00 89.81 C ANISOU 4222 CA GLY B 163 12690 8632 12800 217 1381 615 C ATOM 4223 C GLY B 163 73.900 37.376 137.443 1.00 88.18 C ANISOU 4223 C GLY B 163 12490 8486 12525 251 1239 693 C ATOM 4224 O GLY B 163 74.385 36.259 137.644 1.00 88.69 O ANISOU 4224 O GLY B 163 12434 8504 12758 239 1086 692 O ATOM 4225 N GLU B 164 72.596 37.592 137.263 1.00 85.82 N ANISOU 4225 N GLU B 164 12323 8282 12003 294 1291 763 N ATOM 4226 CA GLU B 164 71.611 36.511 137.306 1.00 83.77 C ANISOU 4226 CA GLU B 164 12086 8091 11649 326 1174 837 C ATOM 4227 C GLU B 164 71.783 35.588 136.099 1.00 83.47 C ANISOU 4227 C GLU B 164 11986 8024 11703 373 1230 792 C ATOM 4228 O GLU B 164 72.104 36.063 135.006 1.00 83.51 O ANISOU 4228 O GLU B 164 12004 8002 11723 390 1416 729 O ATOM 4229 CB GLU B 164 70.186 37.070 137.313 1.00 82.24 C ANISOU 4229 CB GLU B 164 12033 7994 11219 361 1239 914 C ATOM 4230 CG GLU B 164 69.113 36.047 137.675 1.00 81.36 C ANISOU 4230 CG GLU B 164 11950 7961 10999 375 1099 991 C ATOM 4231 CD GLU B 164 67.697 36.546 137.446 1.00 80.35 C ANISOU 4231 CD GLU B 164 11936 7915 10678 423 1183 1061 C ATOM 4232 OE1 GLU B 164 67.510 37.730 137.093 1.00 80.32 O ANISOU 4232 OE1 GLU B 164 11986 7898 10633 445 1339 1065 O ATOM 4233 OE2 GLU B 164 66.757 35.738 137.611 1.00 79.32 O ANISOU 4233 OE2 GLU B 164 11831 7850 10456 439 1090 1117 O ATOM 4234 N PRO B 165 71.584 34.268 136.291 1.00 83.35 N ANISOU 4234 N PRO B 165 11906 8011 11750 378 1079 817 N ATOM 4235 CA PRO B 165 71.597 33.346 135.155 1.00 83.41 C ANISOU 4235 CA PRO B 165 11863 7996 11831 408 1153 759 C ATOM 4236 C PRO B 165 70.560 33.644 134.063 1.00 82.91 C ANISOU 4236 C PRO B 165 11929 8032 11540 442 1308 781 C ATOM 4237 O PRO B 165 69.339 33.640 134.319 1.00 81.74 O ANISOU 4237 O PRO B 165 11877 7985 11194 470 1253 880 O ATOM 4238 CB PRO B 165 71.311 31.993 135.802 1.00 83.47 C ANISOU 4238 CB PRO B 165 11800 7999 11913 406 946 811 C ATOM 4239 CG PRO B 165 71.857 32.117 137.178 1.00 83.86 C ANISOU 4239 CG PRO B 165 11799 8012 12051 352 754 866 C ATOM 4240 CD PRO B 165 71.618 33.543 137.578 1.00 83.55 C ANISOU 4240 CD PRO B 165 11880 8034 11831 331 835 885 C ATOM 4241 N VAL B 166 71.079 33.931 132.868 1.00 84.33 N ANISOU 4241 N VAL B 166 12107 8180 11755 425 1498 692 N ATOM 4242 CA VAL B 166 70.304 33.960 131.634 1.00 84.93 C ANISOU 4242 CA VAL B 166 12283 8342 11643 421 1633 705 C ATOM 4243 C VAL B 166 70.411 32.577 130.992 1.00 86.23 C ANISOU 4243 C VAL B 166 12371 8489 11901 391 1640 617 C ATOM 4244 O VAL B 166 71.521 32.058 130.813 1.00 87.85 O ANISOU 4244 O VAL B 166 12446 8575 12357 356 1686 486 O ATOM 4245 CB VAL B 166 70.839 35.017 130.646 1.00 85.54 C ANISOU 4245 CB VAL B 166 12416 8400 11686 380 1843 655 C ATOM 4246 CG1 VAL B 166 70.021 35.017 129.353 1.00 85.58 C ANISOU 4246 CG1 VAL B 166 12535 8509 11473 344 1955 694 C ATOM 4247 CG2 VAL B 166 70.834 36.395 131.298 1.00 85.61 C ANISOU 4247 CG2 VAL B 166 12481 8399 11646 408 1853 727 C ATOM 4248 N ILE B 167 69.264 31.995 130.642 1.00 86.09 N ANISOU 4248 N ILE B 167 12424 8579 11705 401 1604 682 N ATOM 4249 CA ILE B 167 69.195 30.617 130.135 1.00 86.89 C ANISOU 4249 CA ILE B 167 12459 8672 11883 369 1605 601 C ATOM 4250 C ILE B 167 68.065 30.434 129.126 1.00 86.66 C ANISOU 4250 C ILE B 167 12550 8785 11592 334 1672 643 C ATOM 4251 O ILE B 167 67.141 31.255 129.052 1.00 85.83 O ANISOU 4251 O ILE B 167 12567 8787 11258 360 1657 776 O ATOM 4252 CB ILE B 167 69.029 29.576 131.282 1.00 86.90 C ANISOU 4252 CB ILE B 167 12365 8631 12018 414 1390 644 C ATOM 4253 CG1 ILE B 167 67.861 29.929 132.229 1.00 85.95 C ANISOU 4253 CG1 ILE B 167 12346 8618 11690 468 1235 807 C ATOM 4254 CG2 ILE B 167 70.317 29.436 132.088 1.00 87.73 C ANISOU 4254 CG2 ILE B 167 12316 8580 12435 415 1311 590 C ATOM 4255 CD1 ILE B 167 66.539 29.273 131.888 1.00 85.56 C ANISOU 4255 CD1 ILE B 167 12371 8689 11449 479 1200 869 C ATOM 4256 N LYS B 168 68.161 29.357 128.342 1.00 87.50 N ANISOU 4256 N LYS B 168 12610 8884 11752 267 1749 526 N ATOM 4257 CA LYS B 168 67.037 28.889 127.532 1.00 87.14 C ANISOU 4257 CA LYS B 168 12661 8980 11468 219 1772 563 C ATOM 4258 C LYS B 168 65.981 28.368 128.495 1.00 85.59 C ANISOU 4258 C LYS B 168 12469 8841 11210 307 1567 690 C ATOM 4259 O LYS B 168 66.241 27.424 129.247 1.00 85.52 O ANISOU 4259 O LYS B 168 12350 8747 11394 341 1460 655 O ATOM 4260 CB LYS B 168 67.449 27.782 126.543 1.00 88.13 C ANISOU 4260 CB LYS B 168 12726 9072 11685 104 1919 378 C ATOM 4261 CG LYS B 168 66.263 27.079 125.881 1.00 87.82 C ANISOU 4261 CG LYS B 168 12770 9181 11416 46 1912 409 C ATOM 4262 CD LYS B 168 66.528 26.630 124.451 1.00 89.33 C ANISOU 4262 CD LYS B 168 12992 9407 11540 -133 2134 240 C ATOM 4263 CE LYS B 168 65.226 26.256 123.756 1.00 89.31 C ANISOU 4263 CE LYS B 168 13109 9593 11231 -208 2108 314 C ATOM 4264 NZ LYS B 168 65.371 26.152 122.278 1.00 90.98 N ANISOU 4264 NZ LYS B 168 13405 9886 11276 -425 2324 186 N ATOM 4265 N CYS B 169 64.802 28.989 128.464 1.00 84.26 N ANISOU 4265 N CYS B 169 12420 8804 10788 338 1513 842 N ATOM 4266 CA CYS B 169 63.737 28.678 129.408 1.00 82.62 C ANISOU 4266 CA CYS B 169 12227 8653 10510 415 1338 962 C ATOM 4267 C CYS B 169 63.175 27.272 129.191 1.00 83.29 C ANISOU 4267 C CYS B 169 12280 8778 10587 388 1292 918 C ATOM 4268 O CYS B 169 62.442 27.023 128.232 1.00 83.40 O ANISOU 4268 O CYS B 169 12359 8905 10424 328 1348 926 O ATOM 4269 CB CYS B 169 62.614 29.715 129.312 1.00 81.22 C ANISOU 4269 CB CYS B 169 12163 8588 10106 450 1318 1123 C ATOM 4270 SG CYS B 169 61.232 29.434 130.446 1.00 79.12 S ANISOU 4270 SG CYS B 169 11916 8388 9758 531 1139 1250 S ATOM 4271 N GLU B 170 63.549 26.366 130.092 1.00 83.85 N ANISOU 4271 N GLU B 170 12249 8754 10857 420 1185 879 N ATOM 4272 CA GLU B 170 63.082 24.987 130.090 1.00 84.16 C ANISOU 4272 CA GLU B 170 12240 8800 10936 404 1128 842 C ATOM 4273 C GLU B 170 62.518 24.675 131.465 1.00 83.36 C ANISOU 4273 C GLU B 170 12128 8693 10849 473 926 953 C ATOM 4274 O GLU B 170 63.047 25.142 132.477 1.00 83.21 O ANISOU 4274 O GLU B 170 12082 8602 10930 506 835 999 O ATOM 4275 CB GLU B 170 64.245 24.048 129.784 1.00 85.88 C ANISOU 4275 CB GLU B 170 12316 8868 11446 356 1205 675 C ATOM 4276 CG GLU B 170 64.786 24.184 128.367 1.00 87.97 C ANISOU 4276 CG GLU B 170 12592 9137 11693 251 1437 527 C ATOM 4277 CD GLU B 170 66.171 23.586 128.194 1.00 90.07 C ANISOU 4277 CD GLU B 170 12697 9214 12311 209 1543 347 C ATOM 4278 OE1 GLU B 170 67.081 23.951 128.972 1.00 90.36 O ANISOU 4278 OE1 GLU B 170 12645 9125 12564 264 1476 360 O ATOM 4279 OE2 GLU B 170 66.356 22.762 127.269 1.00 91.88 O ANISOU 4279 OE2 GLU B 170 12881 9416 12610 111 1700 186 O ATOM 4280 N PHE B 171 61.459 23.870 131.497 1.00 83.20 N ANISOU 4280 N PHE B 171 12136 8753 10722 474 860 991 N ATOM 4281 CA PHE B 171 60.778 23.516 132.745 1.00 82.42 C ANISOU 4281 CA PHE B 171 12047 8665 10602 516 681 1094 C ATOM 4282 C PHE B 171 61.716 22.812 133.724 1.00 83.22 C ANISOU 4282 C PHE B 171 12035 8617 10966 515 558 1081 C ATOM 4283 O PHE B 171 61.847 23.224 134.877 1.00 82.67 O ANISOU 4283 O PHE B 171 11978 8522 10909 526 431 1164 O ATOM 4284 CB PHE B 171 59.573 22.623 132.445 1.00 81.80 C ANISOU 4284 CB PHE B 171 12003 8687 10390 505 654 1111 C ATOM 4285 CG PHE B 171 58.707 22.347 133.638 1.00 80.72 C ANISOU 4285 CG PHE B 171 11899 8581 10189 534 495 1214 C ATOM 4286 CD1 PHE B 171 57.685 23.222 133.985 1.00 79.94 C ANISOU 4286 CD1 PHE B 171 11894 8585 9892 563 476 1311 C ATOM 4287 CD2 PHE B 171 58.906 21.207 134.408 1.00 81.14 C ANISOU 4287 CD2 PHE B 171 11883 8551 10395 522 371 1214 C ATOM 4288 CE1 PHE B 171 56.878 22.969 135.080 1.00 79.64 C ANISOU 4288 CE1 PHE B 171 11891 8574 9794 567 356 1384 C ATOM 4289 CE2 PHE B 171 58.108 20.949 135.504 1.00 80.91 C ANISOU 4289 CE2 PHE B 171 11900 8557 10284 522 231 1308 C ATOM 4290 CZ PHE B 171 57.088 21.832 135.843 1.00 80.13 C ANISOU 4290 CZ PHE B 171 11905 8570 9971 539 234 1382 C ATOM 4291 N GLU B 172 62.375 21.762 133.240 1.00 85.10 N ANISOU 4291 N GLU B 172 12158 8752 11423 488 598 976 N ATOM 4292 CA GLU B 172 63.323 20.989 134.051 1.00 86.97 C ANISOU 4292 CA GLU B 172 12253 8820 11970 486 470 976 C ATOM 4293 C GLU B 172 64.573 21.775 134.496 1.00 87.58 C ANISOU 4293 C GLU B 172 12266 8790 12219 488 449 975 C ATOM 4294 O GLU B 172 65.259 21.350 135.426 1.00 88.90 O ANISOU 4294 O GLU B 172 12331 8837 12610 482 287 1029 O ATOM 4295 CB GLU B 172 63.737 19.682 133.343 1.00 88.58 C ANISOU 4295 CB GLU B 172 12323 8910 12421 457 547 848 C ATOM 4296 CG GLU B 172 64.545 19.828 132.053 1.00 90.23 C ANISOU 4296 CG GLU B 172 12474 9064 12742 412 784 669 C ATOM 4297 CD GLU B 172 63.707 19.682 130.794 1.00 90.78 C ANISOU 4297 CD GLU B 172 12640 9275 12576 355 961 580 C ATOM 4298 OE1 GLU B 172 62.683 20.390 130.657 1.00 89.77 O ANISOU 4298 OE1 GLU B 172 12665 9325 12119 365 949 672 O ATOM 4299 OE2 GLU B 172 64.079 18.855 129.941 1.00 92.38 O ANISOU 4299 OE2 GLU B 172 12757 9405 12935 288 1112 418 O ATOM 4300 N LYS B 173 64.869 22.895 133.831 1.00 87.11 N ANISOU 4300 N LYS B 173 12263 8773 12062 488 602 923 N ATOM 4301 CA LYS B 173 65.983 23.763 134.220 1.00 87.32 C ANISOU 4301 CA LYS B 173 12241 8714 12222 488 598 916 C ATOM 4302 C LYS B 173 65.667 24.651 135.429 1.00 85.76 C ANISOU 4302 C LYS B 173 12133 8576 11872 496 458 1049 C ATOM 4303 O LYS B 173 66.569 24.951 136.217 1.00 85.46 O ANISOU 4303 O LYS B 173 12031 8452 11988 476 360 1076 O ATOM 4304 CB LYS B 173 66.426 24.633 133.032 1.00 88.16 C ANISOU 4304 CB LYS B 173 12380 8837 12279 472 828 807 C ATOM 4305 CG LYS B 173 67.748 25.373 133.225 1.00 89.41 C ANISOU 4305 CG LYS B 173 12459 8880 12632 464 862 759 C ATOM 4306 CD LYS B 173 68.931 24.423 133.370 1.00 91.41 C ANISOU 4306 CD LYS B 173 12506 8939 13285 448 821 675 C ATOM 4307 CE LYS B 173 70.254 25.161 133.328 1.00 93.01 C ANISOU 4307 CE LYS B 173 12619 9027 13693 433 891 601 C ATOM 4308 NZ LYS B 173 71.402 24.251 133.604 1.00 95.00 N ANISOU 4308 NZ LYS B 173 12641 9070 14384 423 821 542 N ATOM 4309 N VAL B 174 64.407 25.075 135.566 1.00 83.89 N ANISOU 4309 N VAL B 174 12038 8484 11350 511 457 1124 N ATOM 4310 CA VAL B 174 63.992 25.968 136.670 1.00 82.50 C ANISOU 4310 CA VAL B 174 11955 8367 11022 500 369 1222 C ATOM 4311 C VAL B 174 63.167 25.285 137.768 1.00 81.73 C ANISOU 4311 C VAL B 174 11898 8314 10841 470 192 1318 C ATOM 4312 O VAL B 174 63.360 25.582 138.945 1.00 81.34 O ANISOU 4312 O VAL B 174 11872 8255 10779 413 66 1382 O ATOM 4313 CB VAL B 174 63.259 27.245 136.165 1.00 81.86 C ANISOU 4313 CB VAL B 174 11994 8390 10717 531 517 1235 C ATOM 4314 CG1 VAL B 174 64.109 27.971 135.128 1.00 82.60 C ANISOU 4314 CG1 VAL B 174 12063 8441 10878 540 686 1154 C ATOM 4315 CG2 VAL B 174 61.862 26.944 135.619 1.00 81.07 C ANISOU 4315 CG2 VAL B 174 11970 8409 10424 559 551 1272 C ATOM 4316 N ILE B 175 62.257 24.383 137.393 1.00 81.17 N ANISOU 4316 N ILE B 175 11842 8296 10700 488 186 1325 N ATOM 4317 CA ILE B 175 61.426 23.671 138.371 1.00 80.80 C ANISOU 4317 CA ILE B 175 11839 8291 10569 452 31 1410 C ATOM 4318 C ILE B 175 62.156 22.407 138.827 1.00 81.84 C ANISOU 4318 C ILE B 175 11851 8301 10941 418 -129 1433 C ATOM 4319 O ILE B 175 62.677 21.652 138.003 1.00 82.68 O ANISOU 4319 O ILE B 175 11846 8323 11242 447 -75 1359 O ATOM 4320 CB ILE B 175 60.035 23.300 137.796 1.00 79.91 C ANISOU 4320 CB ILE B 175 11795 8292 10273 485 94 1412 C ATOM 4321 CG1 ILE B 175 59.281 24.551 137.306 1.00 79.24 C ANISOU 4321 CG1 ILE B 175 11804 8309 9991 522 235 1415 C ATOM 4322 CG2 ILE B 175 59.200 22.541 138.826 1.00 79.43 C ANISOU 4322 CG2 ILE B 175 11778 8267 10132 439 -54 1489 C ATOM 4323 CD1 ILE B 175 58.816 25.505 138.386 1.00 78.87 C ANISOU 4323 CD1 ILE B 175 11843 8301 9823 492 208 1471 C ATOM 4324 N SER B 176 62.189 22.189 140.143 1.00 81.79 N ANISOU 4324 N SER B 176 11865 8281 10928 342 -322 1536 N ATOM 4325 CA SER B 176 62.837 21.017 140.738 1.00 81.99 C ANISOU 4325 CA SER B 176 11777 8186 11189 296 -520 1605 C ATOM 4326 C SER B 176 61.993 19.767 140.491 1.00 81.10 C ANISOU 4326 C SER B 176 11655 8082 11075 314 -545 1615 C ATOM 4327 O SER B 176 60.795 19.766 140.776 1.00 79.51 O ANISOU 4327 O SER B 176 11576 8001 10630 297 -541 1647 O ATOM 4328 CB SER B 176 63.028 21.232 142.246 1.00 82.92 C ANISOU 4328 CB SER B 176 11948 8312 11243 175 -733 1734 C ATOM 4329 OG SER B 176 63.606 20.099 142.871 1.00 84.57 O ANISOU 4329 OG SER B 176 12048 8403 11679 118 -959 1840 O ATOM 4330 N MET B 177 62.613 18.713 139.960 1.00 81.51 N ANISOU 4330 N MET B 177 11554 7997 11416 343 -558 1578 N ATOM 4331 CA MET B 177 61.916 17.433 139.755 1.00 81.25 C ANISOU 4331 CA MET B 177 11495 7950 11425 351 -583 1582 C ATOM 4332 C MET B 177 61.509 16.780 141.073 1.00 81.34 C ANISOU 4332 C MET B 177 11549 7960 11395 268 -824 1744 C ATOM 4333 O MET B 177 60.445 16.168 141.153 1.00 81.32 O ANISOU 4333 O MET B 177 11618 8028 11249 258 -831 1764 O ATOM 4334 CB MET B 177 62.755 16.460 138.916 1.00 82.20 C ANISOU 4334 CB MET B 177 11424 7897 11911 387 -520 1488 C ATOM 4335 CG MET B 177 62.811 16.838 137.446 1.00 81.89 C ANISOU 4335 CG MET B 177 11374 7891 11847 437 -247 1305 C ATOM 4336 SD MET B 177 61.206 16.698 136.633 1.00 80.74 S ANISOU 4336 SD MET B 177 11375 7941 11360 450 -100 1246 S ATOM 4337 CE MET B 177 61.229 18.193 135.629 1.00 80.47 C ANISOU 4337 CE MET B 177 11434 8028 11110 473 113 1158 C ATOM 4338 N GLU B 178 62.343 16.938 142.099 1.00 81.65 N ANISOU 4338 N GLU B 178 11552 7925 11543 192 -1022 1863 N ATOM 4339 CA GLU B 178 62.011 16.504 143.465 1.00 81.82 C ANISOU 4339 CA GLU B 178 11645 7967 11473 69 -1267 2036 C ATOM 4340 C GLU B 178 60.679 17.099 143.939 1.00 79.63 C ANISOU 4340 C GLU B 178 11582 7885 10788 16 -1211 2038 C ATOM 4341 O GLU B 178 59.812 16.376 144.449 1.00 79.62 O ANISOU 4341 O GLU B 178 11651 7927 10672 -41 -1293 2105 O ATOM 4342 CB GLU B 178 63.142 16.880 144.426 1.00 83.55 C ANISOU 4342 CB GLU B 178 11814 8112 11818 -28 -1475 2157 C ATOM 4343 CG GLU B 178 64.407 16.058 144.205 1.00 85.65 C ANISOU 4343 CG GLU B 178 11842 8155 12546 4 -1591 2198 C ATOM 4344 CD GLU B 178 65.628 16.633 144.891 1.00 87.34 C ANISOU 4344 CD GLU B 178 11979 8297 12906 -70 -1759 2288 C ATOM 4345 OE1 GLU B 178 65.934 17.823 144.666 1.00 86.95 O ANISOU 4345 OE1 GLU B 178 11980 8316 12739 -54 -1627 2195 O ATOM 4346 OE2 GLU B 178 66.295 15.884 145.637 1.00 89.29 O ANISOU 4346 OE2 GLU B 178 12109 8413 13403 -148 -2029 2460 O ATOM 4347 N TYR B 179 60.518 18.406 143.736 1.00 77.48 N ANISOU 4347 N TYR B 179 11399 7714 10324 36 -1058 1958 N ATOM 4348 CA TYR B 179 59.243 19.098 143.983 1.00 75.85 C ANISOU 4348 CA TYR B 179 11364 7671 9783 9 -949 1927 C ATOM 4349 C TYR B 179 58.091 18.465 143.191 1.00 74.05 C ANISOU 4349 C TYR B 179 11154 7501 9477 90 -832 1867 C ATOM 4350 O TYR B 179 57.040 18.155 143.755 1.00 73.78 O ANISOU 4350 O TYR B 179 11220 7548 9264 30 -863 1903 O ATOM 4351 CB TYR B 179 59.359 20.607 143.671 1.00 75.30 C ANISOU 4351 CB TYR B 179 11347 7663 9599 45 -778 1843 C ATOM 4352 CG TYR B 179 58.028 21.298 143.442 1.00 74.40 C ANISOU 4352 CG TYR B 179 11353 7682 9233 75 -607 1782 C ATOM 4353 CD1 TYR B 179 57.224 21.681 144.516 1.00 74.56 C ANISOU 4353 CD1 TYR B 179 11504 7786 9037 -43 -630 1812 C ATOM 4354 CD2 TYR B 179 57.565 21.554 142.149 1.00 73.62 C ANISOU 4354 CD2 TYR B 179 11230 7619 9122 205 -424 1697 C ATOM 4355 CE1 TYR B 179 55.992 22.296 144.304 1.00 73.91 C ANISOU 4355 CE1 TYR B 179 11503 7800 8778 -10 -467 1753 C ATOM 4356 CE2 TYR B 179 56.340 22.169 141.933 1.00 72.73 C ANISOU 4356 CE2 TYR B 179 11203 7613 8816 235 -292 1666 C ATOM 4357 CZ TYR B 179 55.556 22.540 143.013 1.00 73.04 C ANISOU 4357 CZ TYR B 179 11349 7714 8688 137 -310 1691 C ATOM 4358 OH TYR B 179 54.341 23.156 142.805 1.00 72.23 O ANISOU 4358 OH TYR B 179 11304 7694 8446 170 -171 1656 O ATOM 4359 N MET B 180 58.301 18.265 141.893 1.00 73.09 N ANISOU 4359 N MET B 180 10940 7345 9486 207 -694 1771 N ATOM 4360 CA MET B 180 57.250 17.728 141.018 1.00 72.16 C ANISOU 4360 CA MET B 180 10837 7296 9283 271 -574 1705 C ATOM 4361 C MET B 180 56.824 16.306 141.385 1.00 72.82 C ANISOU 4361 C MET B 180 10894 7338 9436 232 -696 1759 C ATOM 4362 O MET B 180 55.632 15.994 141.375 1.00 72.44 O ANISOU 4362 O MET B 180 10921 7384 9215 226 -662 1753 O ATOM 4363 CB MET B 180 57.679 17.790 139.546 1.00 71.94 C ANISOU 4363 CB MET B 180 10722 7241 9370 363 -401 1584 C ATOM 4364 CG MET B 180 57.380 19.117 138.868 1.00 70.99 C ANISOU 4364 CG MET B 180 10670 7223 9077 411 -234 1529 C ATOM 4365 SD MET B 180 55.676 19.210 138.286 1.00 69.83 S ANISOU 4365 SD MET B 180 10620 7244 8668 441 -128 1513 S ATOM 4366 CE MET B 180 54.916 20.245 139.524 1.00 69.45 C ANISOU 4366 CE MET B 180 10694 7271 8421 397 -167 1587 C ATOM 4367 N VAL B 181 57.797 15.460 141.717 1.00 74.07 N ANISOU 4367 N VAL B 181 10936 7343 9864 204 -842 1819 N ATOM 4368 CA VAL B 181 57.539 14.062 142.064 1.00 74.69 C ANISOU 4368 CA VAL B 181 10967 7346 10064 167 -969 1886 C ATOM 4369 C VAL B 181 57.039 13.926 143.505 1.00 74.77 C ANISOU 4369 C VAL B 181 11096 7403 9909 36 -1162 2035 C ATOM 4370 O VAL B 181 55.929 13.421 143.736 1.00 74.25 O ANISOU 4370 O VAL B 181 11116 7414 9681 3 -1160 2047 O ATOM 4371 CB VAL B 181 58.791 13.188 141.821 1.00 76.13 C ANISOU 4371 CB VAL B 181 10951 7317 10656 189 -1047 1899 C ATOM 4372 CG1 VAL B 181 58.595 11.765 142.343 1.00 77.34 C ANISOU 4372 CG1 VAL B 181 11047 7365 10972 141 -1208 2002 C ATOM 4373 CG2 VAL B 181 59.126 13.167 140.330 1.00 75.98 C ANISOU 4373 CG2 VAL B 181 10829 7259 10780 288 -816 1718 C ATOM 4374 N TYR B 182 57.847 14.378 144.464 1.00 75.39 N ANISOU 4374 N TYR B 182 11184 7441 10018 -54 -1323 2143 N ATOM 4375 CA TYR B 182 57.537 14.161 145.886 1.00 76.05 C ANISOU 4375 CA TYR B 182 11382 7561 9952 -224 -1529 2297 C ATOM 4376 C TYR B 182 56.397 15.060 146.365 1.00 74.95 C ANISOU 4376 C TYR B 182 11437 7604 9436 -294 -1421 2249 C ATOM 4377 O TYR B 182 55.424 14.579 146.949 1.00 74.55 O ANISOU 4377 O TYR B 182 11490 7619 9215 -382 -1458 2288 O ATOM 4378 CB TYR B 182 58.772 14.360 146.779 1.00 77.35 C ANISOU 4378 CB TYR B 182 11499 7637 10253 -333 -1752 2437 C ATOM 4379 CG TYR B 182 59.990 13.525 146.404 1.00 78.37 C ANISOU 4379 CG TYR B 182 11406 7556 10815 -270 -1873 2495 C ATOM 4380 CD1 TYR B 182 59.878 12.163 146.107 1.00 78.88 C ANISOU 4380 CD1 TYR B 182 11359 7497 11114 -229 -1929 2533 C ATOM 4381 CD2 TYR B 182 61.265 14.096 146.371 1.00 78.91 C ANISOU 4381 CD2 TYR B 182 11362 7535 11083 -258 -1924 2507 C ATOM 4382 CE1 TYR B 182 60.991 11.406 145.766 1.00 80.17 C ANISOU 4382 CE1 TYR B 182 11295 7441 11723 -172 -2019 2575 C ATOM 4383 CE2 TYR B 182 62.385 13.339 146.042 1.00 80.23 C ANISOU 4383 CE2 TYR B 182 11303 7490 11689 -202 -2025 2553 C ATOM 4384 CZ TYR B 182 62.243 11.999 145.738 1.00 80.81 C ANISOU 4384 CZ TYR B 182 11258 7431 12013 -158 -2067 2584 C ATOM 4385 OH TYR B 182 63.350 11.254 145.412 1.00 82.29 O ANISOU 4385 OH TYR B 182 11199 7382 12684 -104 -2148 2618 O ATOM 4386 N PHE B 183 56.508 16.358 146.102 1.00 74.54 N ANISOU 4386 N PHE B 183 11424 7619 9276 -257 -1275 2159 N ATOM 4387 CA PHE B 183 55.516 17.313 146.599 1.00 74.31 C ANISOU 4387 CA PHE B 183 11556 7734 8945 -327 -1158 2106 C ATOM 4388 C PHE B 183 54.252 17.312 145.736 1.00 73.12 C ANISOU 4388 C PHE B 183 11428 7667 8686 -214 -961 1998 C ATOM 4389 O PHE B 183 53.190 16.918 146.199 1.00 72.70 O ANISOU 4389 O PHE B 183 11461 7680 8479 -281 -959 2005 O ATOM 4390 CB PHE B 183 56.118 18.715 146.712 1.00 74.23 C ANISOU 4390 CB PHE B 183 11569 7747 8886 -339 -1079 2057 C ATOM 4391 CG PHE B 183 55.325 19.647 147.580 1.00 74.19 C ANISOU 4391 CG PHE B 183 11723 7854 8612 -470 -995 2020 C ATOM 4392 CD1 PHE B 183 55.364 19.532 148.964 1.00 75.28 C ANISOU 4392 CD1 PHE B 183 11971 8021 8609 -699 -1147 2105 C ATOM 4393 CD2 PHE B 183 54.540 20.644 147.013 1.00 73.38 C ANISOU 4393 CD2 PHE B 183 11652 7820 8407 -380 -761 1899 C ATOM 4394 CE1 PHE B 183 54.631 20.393 149.766 1.00 75.64 C ANISOU 4394 CE1 PHE B 183 12163 8164 8412 -845 -1035 2039 C ATOM 4395 CE2 PHE B 183 53.808 21.508 147.810 1.00 73.61 C ANISOU 4395 CE2 PHE B 183 11805 7926 8236 -502 -657 1845 C ATOM 4396 CZ PHE B 183 53.859 21.388 149.191 1.00 74.68 C ANISOU 4396 CZ PHE B 183 12056 8091 8228 -740 -779 1899 C ATOM 4397 N ASN B 184 54.370 17.719 144.477 1.00 72.59 N ANISOU 4397 N ASN B 184 11282 7598 8701 -56 -805 1904 N ATOM 4398 CA ASN B 184 53.194 17.874 143.616 1.00 71.87 C ANISOU 4398 CA ASN B 184 11209 7598 8498 38 -632 1819 C ATOM 4399 C ASN B 184 52.496 16.530 143.322 1.00 71.63 C ANISOU 4399 C ASN B 184 11153 7569 8493 52 -669 1825 C ATOM 4400 O ASN B 184 51.303 16.357 143.628 1.00 72.48 O ANISOU 4400 O ASN B 184 11336 7758 8444 15 -636 1816 O ATOM 4401 CB ASN B 184 53.580 18.593 142.317 1.00 71.65 C ANISOU 4401 CB ASN B 184 11111 7571 8542 173 -480 1739 C ATOM 4402 CG ASN B 184 52.403 18.789 141.382 1.00 71.34 C ANISOU 4402 CG ASN B 184 11084 7632 8388 255 -331 1679 C ATOM 4403 OD1 ASN B 184 52.416 18.316 140.245 1.00 71.40 O ANISOU 4403 OD1 ASN B 184 11024 7641 8461 330 -272 1634 O ATOM 4404 ND2 ASN B 184 51.369 19.475 141.861 1.00 71.78 N ANISOU 4404 ND2 ASN B 184 11222 7768 8281 226 -269 1676 N ATOM 4405 N PHE B 185 53.239 15.575 142.767 1.00 70.72 N ANISOU 4405 N PHE B 185 10923 7351 8594 98 -727 1830 N ATOM 4406 CA PHE B 185 52.645 14.322 142.287 1.00 69.49 C ANISOU 4406 CA PHE B 185 10724 7185 8492 122 -726 1810 C ATOM 4407 C PHE B 185 52.250 13.363 143.422 1.00 69.22 C ANISOU 4407 C PHE B 185 10744 7124 8433 5 -891 1913 C ATOM 4408 O PHE B 185 51.075 12.957 143.512 1.00 68.32 O ANISOU 4408 O PHE B 185 10693 7089 8174 -16 -854 1895 O ATOM 4409 CB PHE B 185 53.578 13.649 141.269 1.00 70.05 C ANISOU 4409 CB PHE B 185 10646 7139 8829 198 -695 1755 C ATOM 4410 CG PHE B 185 53.047 12.361 140.693 1.00 70.19 C ANISOU 4410 CG PHE B 185 10607 7133 8926 214 -668 1710 C ATOM 4411 CD1 PHE B 185 51.749 12.281 140.188 1.00 69.33 C ANISOU 4411 CD1 PHE B 185 10561 7159 8622 232 -561 1648 C ATOM 4412 CD2 PHE B 185 53.858 11.230 140.627 1.00 70.75 C ANISOU 4412 CD2 PHE B 185 10549 7038 9293 209 -744 1725 C ATOM 4413 CE1 PHE B 185 51.268 11.095 139.652 1.00 69.36 C ANISOU 4413 CE1 PHE B 185 10514 7146 8693 234 -529 1596 C ATOM 4414 CE2 PHE B 185 53.382 10.048 140.088 1.00 71.02 C ANISOU 4414 CE2 PHE B 185 10527 7039 9416 217 -698 1668 C ATOM 4415 CZ PHE B 185 52.087 9.979 139.601 1.00 70.27 C ANISOU 4415 CZ PHE B 185 10509 7094 9094 225 -589 1599 C ATOM 4416 N PHE B 186 53.211 13.016 144.284 1.00 69.75 N ANISOU 4416 N PHE B 186 10783 7081 8637 -77 -1079 2029 N ATOM 4417 CA PHE B 186 52.955 12.054 145.377 1.00 70.14 C ANISOU 4417 CA PHE B 186 10883 7092 8672 -211 -1265 2158 C ATOM 4418 C PHE B 186 52.045 12.577 146.496 1.00 69.68 C ANISOU 4418 C PHE B 186 11006 7159 8308 -358 -1283 2192 C ATOM 4419 O PHE B 186 51.278 11.796 147.055 1.00 69.84 O ANISOU 4419 O PHE B 186 11094 7201 8240 -448 -1344 2240 O ATOM 4420 CB PHE B 186 54.257 11.513 146.002 1.00 71.28 C ANISOU 4420 CB PHE B 186 10937 7077 9068 -276 -1495 2306 C ATOM 4421 CG PHE B 186 55.097 10.646 145.088 1.00 71.69 C ANISOU 4421 CG PHE B 186 10790 6961 9487 -162 -1494 2280 C ATOM 4422 CD1 PHE B 186 54.560 9.966 143.985 1.00 71.03 C ANISOU 4422 CD1 PHE B 186 10638 6870 9479 -57 -1334 2154 C ATOM 4423 CD2 PHE B 186 56.448 10.472 145.372 1.00 72.89 C ANISOU 4423 CD2 PHE B 186 10813 6951 9928 -179 -1656 2381 C ATOM 4424 CE1 PHE B 186 55.364 9.169 143.182 1.00 71.81 C ANISOU 4424 CE1 PHE B 186 10551 6802 9929 20 -1306 2107 C ATOM 4425 CE2 PHE B 186 57.252 9.672 144.572 1.00 73.67 C ANISOU 4425 CE2 PHE B 186 10708 6869 10410 -83 -1637 2343 C ATOM 4426 CZ PHE B 186 56.711 9.020 143.477 1.00 73.15 C ANISOU 4426 CZ PHE B 186 10584 6796 10414 12 -1449 2195 C ATOM 4427 N VAL B 187 52.124 13.865 146.831 1.00 69.03 N ANISOU 4427 N VAL B 187 11000 7152 8076 -394 -1215 2157 N ATOM 4428 CA VAL B 187 51.255 14.440 147.878 1.00 69.17 C ANISOU 4428 CA VAL B 187 11185 7280 7815 -552 -1187 2153 C ATOM 4429 C VAL B 187 49.981 15.087 147.321 1.00 67.86 C ANISOU 4429 C VAL B 187 11059 7225 7496 -472 -954 2013 C ATOM 4430 O VAL B 187 48.901 14.874 147.863 1.00 67.71 O ANISOU 4430 O VAL B 187 11134 7273 7316 -564 -916 1992 O ATOM 4431 CB VAL B 187 52.011 15.453 148.778 1.00 69.86 C ANISOU 4431 CB VAL B 187 11343 7380 7820 -686 -1247 2192 C ATOM 4432 CG1 VAL B 187 51.074 16.088 149.807 1.00 70.05 C ANISOU 4432 CG1 VAL B 187 11540 7516 7560 -869 -1169 2149 C ATOM 4433 CG2 VAL B 187 53.182 14.774 149.477 1.00 71.43 C ANISOU 4433 CG2 VAL B 187 11504 7475 8160 -798 -1517 2363 C ATOM 4434 N TRP B 188 50.103 15.871 146.255 1.00 67.26 N ANISOU 4434 N TRP B 188 10909 7164 7482 -312 -805 1925 N ATOM 4435 CA TRP B 188 48.985 16.706 145.783 1.00 67.06 C ANISOU 4435 CA TRP B 188 10909 7233 7335 -244 -604 1819 C ATOM 4436 C TRP B 188 48.262 16.226 144.520 1.00 66.59 C ANISOU 4436 C TRP B 188 10769 7208 7321 -96 -511 1763 C ATOM 4437 O TRP B 188 47.235 16.807 144.156 1.00 66.48 O ANISOU 4437 O TRP B 188 10766 7272 7222 -49 -374 1701 O ATOM 4438 CB TRP B 188 49.452 18.164 145.630 1.00 66.83 C ANISOU 4438 CB TRP B 188 10879 7212 7301 -205 -497 1774 C ATOM 4439 CG TRP B 188 49.804 18.768 146.944 1.00 67.71 C ANISOU 4439 CG TRP B 188 11093 7322 7309 -383 -544 1797 C ATOM 4440 CD1 TRP B 188 51.047 19.096 147.401 1.00 68.51 C ANISOU 4440 CD1 TRP B 188 11194 7370 7466 -448 -649 1851 C ATOM 4441 CD2 TRP B 188 48.892 19.077 147.995 1.00 68.21 C ANISOU 4441 CD2 TRP B 188 11279 7446 7191 -547 -483 1759 C ATOM 4442 NE1 TRP B 188 50.960 19.614 148.671 1.00 69.45 N ANISOU 4442 NE1 TRP B 188 11438 7525 7425 -653 -663 1852 N ATOM 4443 CE2 TRP B 188 49.648 19.608 149.062 1.00 69.55 C ANISOU 4443 CE2 TRP B 188 11531 7605 7288 -724 -552 1788 C ATOM 4444 CE3 TRP B 188 47.499 18.985 148.128 1.00 68.13 C ANISOU 4444 CE3 TRP B 188 11312 7495 7077 -572 -365 1692 C ATOM 4445 CZ2 TRP B 188 49.060 20.047 150.251 1.00 70.89 C ANISOU 4445 CZ2 TRP B 188 11839 7828 7268 -942 -491 1739 C ATOM 4446 CZ3 TRP B 188 46.912 19.405 149.313 1.00 69.42 C ANISOU 4446 CZ3 TRP B 188 11599 7697 7078 -774 -299 1640 C ATOM 4447 CH2 TRP B 188 47.697 19.928 150.365 1.00 70.87 C ANISOU 4447 CH2 TRP B 188 11877 7874 7174 -967 -355 1659 C ATOM 4448 N VAL B 189 48.770 15.181 143.862 1.00 66.89 N ANISOU 4448 N VAL B 189 10721 7186 7505 -36 -582 1783 N ATOM 4449 CA VAL B 189 48.021 14.538 142.759 1.00 66.20 C ANISOU 4449 CA VAL B 189 10573 7143 7436 57 -502 1724 C ATOM 4450 C VAL B 189 47.496 13.142 143.135 1.00 66.48 C ANISOU 4450 C VAL B 189 10618 7158 7480 -6 -588 1751 C ATOM 4451 O VAL B 189 46.280 12.941 143.152 1.00 66.03 O ANISOU 4451 O VAL B 189 10601 7182 7305 -21 -529 1716 O ATOM 4452 CB VAL B 189 48.830 14.486 141.442 1.00 65.83 C ANISOU 4452 CB VAL B 189 10416 7058 7538 171 -449 1678 C ATOM 4453 CG1 VAL B 189 48.029 13.811 140.333 1.00 65.45 C ANISOU 4453 CG1 VAL B 189 10319 7072 7474 228 -366 1611 C ATOM 4454 CG2 VAL B 189 49.237 15.890 141.005 1.00 65.55 C ANISOU 4454 CG2 VAL B 189 10379 7049 7478 231 -354 1655 C ATOM 4455 N LEU B 190 48.381 12.188 143.437 1.00 66.91 N ANISOU 4455 N LEU B 190 10629 7097 7696 -44 -727 1819 N ATOM 4456 CA LEU B 190 47.944 10.779 143.604 1.00 67.55 C ANISOU 4456 CA LEU B 190 10696 7136 7830 -88 -799 1846 C ATOM 4457 C LEU B 190 46.853 10.522 144.663 1.00 67.55 C ANISOU 4457 C LEU B 190 10820 7200 7642 -215 -835 1882 C ATOM 4458 O LEU B 190 45.867 9.814 144.369 1.00 68.04 O ANISOU 4458 O LEU B 190 10883 7307 7659 -208 -783 1836 O ATOM 4459 CB LEU B 190 49.136 9.836 143.849 1.00 68.99 C ANISOU 4459 CB LEU B 190 10793 7152 8266 -113 -957 1936 C ATOM 4460 CG LEU B 190 49.995 9.467 142.642 1.00 69.67 C ANISOU 4460 CG LEU B 190 10724 7143 8601 0 -894 1864 C ATOM 4461 CD1 LEU B 190 51.174 8.612 143.078 1.00 71.19 C ANISOU 4461 CD1 LEU B 190 10814 7144 9089 -32 -1061 1968 C ATOM 4462 CD2 LEU B 190 49.185 8.746 141.571 1.00 69.44 C ANISOU 4462 CD2 LEU B 190 10649 7163 8572 58 -758 1747 C ATOM 4463 N PRO B 191 47.010 11.084 145.883 1.00 67.27 N ANISOU 4463 N PRO B 191 10893 7174 7491 -349 -913 1953 N ATOM 4464 CA PRO B 191 45.981 10.828 146.901 1.00 67.46 C ANISOU 4464 CA PRO B 191 11046 7259 7326 -500 -926 1969 C ATOM 4465 C PRO B 191 44.588 11.381 146.557 1.00 66.50 C ANISOU 4465 C PRO B 191 10955 7258 7053 -460 -734 1845 C ATOM 4466 O PRO B 191 43.607 10.649 146.729 1.00 66.94 O ANISOU 4466 O PRO B 191 11044 7347 7042 -509 -714 1823 O ATOM 4467 CB PRO B 191 46.564 11.443 148.186 1.00 68.36 C ANISOU 4467 CB PRO B 191 11270 7365 7337 -674 -1031 2054 C ATOM 4468 CG PRO B 191 48.014 11.613 147.920 1.00 68.64 C ANISOU 4468 CG PRO B 191 11215 7304 7559 -613 -1138 2122 C ATOM 4469 CD PRO B 191 48.159 11.812 146.441 1.00 67.52 C ANISOU 4469 CD PRO B 191 10938 7156 7559 -398 -1003 2021 C ATOM 4470 N PRO B 192 44.495 12.639 146.058 1.00 65.45 N ANISOU 4470 N PRO B 192 10798 7179 6888 -372 -599 1770 N ATOM 4471 CA PRO B 192 43.203 13.070 145.520 1.00 64.43 C ANISOU 4471 CA PRO B 192 10652 7143 6684 -307 -435 1671 C ATOM 4472 C PRO B 192 42.629 12.130 144.462 1.00 63.46 C ANISOU 4472 C PRO B 192 10443 7045 6621 -206 -413 1637 C ATOM 4473 O PRO B 192 41.455 11.780 144.548 1.00 62.82 O ANISOU 4473 O PRO B 192 10380 7022 6465 -236 -356 1592 O ATOM 4474 CB PRO B 192 43.520 14.433 144.913 1.00 64.07 C ANISOU 4474 CB PRO B 192 10559 7116 6667 -201 -332 1634 C ATOM 4475 CG PRO B 192 44.597 14.965 145.776 1.00 64.63 C ANISOU 4475 CG PRO B 192 10690 7131 6734 -292 -405 1686 C ATOM 4476 CD PRO B 192 45.421 13.783 146.185 1.00 65.31 C ANISOU 4476 CD PRO B 192 10783 7140 6889 -361 -591 1781 C ATOM 4477 N LEU B 193 43.457 11.714 143.501 1.00 62.99 N ANISOU 4477 N LEU B 193 10292 6942 6699 -107 -449 1647 N ATOM 4478 CA LEU B 193 43.013 10.809 142.427 1.00 62.79 C ANISOU 4478 CA LEU B 193 10186 6942 6728 -35 -414 1597 C ATOM 4479 C LEU B 193 42.491 9.493 142.980 1.00 62.49 C ANISOU 4479 C LEU B 193 10179 6876 6688 -122 -480 1614 C ATOM 4480 O LEU B 193 41.368 9.081 142.648 1.00 62.36 O ANISOU 4480 O LEU B 193 10154 6934 6606 -119 -415 1556 O ATOM 4481 CB LEU B 193 44.138 10.528 141.424 1.00 63.35 C ANISOU 4481 CB LEU B 193 10159 6948 6960 47 -425 1586 C ATOM 4482 CG LEU B 193 44.588 11.688 140.532 1.00 63.53 C ANISOU 4482 CG LEU B 193 10140 7010 6985 140 -340 1556 C ATOM 4483 CD1 LEU B 193 45.828 11.267 139.754 1.00 64.11 C ANISOU 4483 CD1 LEU B 193 10128 6995 7235 184 -349 1535 C ATOM 4484 CD2 LEU B 193 43.479 12.150 139.591 1.00 63.18 C ANISOU 4484 CD2 LEU B 193 10073 7097 6833 197 -229 1502 C ATOM 4485 N LEU B 194 43.290 8.853 143.835 1.00 62.20 N ANISOU 4485 N LEU B 194 10174 6731 6728 -208 -618 1703 N ATOM 4486 CA LEU B 194 42.881 7.579 144.438 1.00 62.25 C ANISOU 4486 CA LEU B 194 10214 6691 6747 -304 -699 1746 C ATOM 4487 C LEU B 194 41.628 7.736 145.312 1.00 61.69 C ANISOU 4487 C LEU B 194 10258 6706 6473 -417 -655 1726 C ATOM 4488 O LEU B 194 40.687 6.927 145.223 1.00 61.42 O ANISOU 4488 O LEU B 194 10228 6703 6406 -442 -620 1685 O ATOM 4489 CB LEU B 194 44.038 6.961 145.235 1.00 63.41 C ANISOU 4489 CB LEU B 194 10367 6693 7032 -385 -884 1882 C ATOM 4490 CG LEU B 194 45.274 6.548 144.421 1.00 63.74 C ANISOU 4490 CG LEU B 194 10267 6610 7339 -284 -925 1893 C ATOM 4491 CD1 LEU B 194 46.374 6.050 145.346 1.00 64.88 C ANISOU 4491 CD1 LEU B 194 10405 6603 7642 -373 -1132 2054 C ATOM 4492 CD2 LEU B 194 44.932 5.496 143.375 1.00 63.79 C ANISOU 4492 CD2 LEU B 194 10171 6592 7473 -213 -843 1802 C ATOM 4493 N LEU B 195 41.600 8.795 146.117 1.00 61.50 N ANISOU 4493 N LEU B 195 10324 6720 6324 -492 -635 1736 N ATOM 4494 CA LEU B 195 40.431 9.117 146.951 1.00 61.79 C ANISOU 4494 CA LEU B 195 10464 6830 6180 -614 -551 1686 C ATOM 4495 C LEU B 195 39.167 9.319 146.112 1.00 60.67 C ANISOU 4495 C LEU B 195 10256 6782 6013 -515 -393 1568 C ATOM 4496 O LEU B 195 38.113 8.780 146.442 1.00 60.49 O ANISOU 4496 O LEU B 195 10269 6795 5918 -587 -348 1524 O ATOM 4497 CB LEU B 195 40.714 10.361 147.810 1.00 62.21 C ANISOU 4497 CB LEU B 195 10606 6901 6130 -708 -519 1686 C ATOM 4498 CG LEU B 195 39.660 10.828 148.812 1.00 63.04 C ANISOU 4498 CG LEU B 195 10826 7065 6062 -872 -406 1613 C ATOM 4499 CD1 LEU B 195 39.251 9.697 149.746 1.00 64.01 C ANISOU 4499 CD1 LEU B 195 11058 7174 6088 -1059 -490 1662 C ATOM 4500 CD2 LEU B 195 40.191 12.015 149.602 1.00 63.70 C ANISOU 4500 CD2 LEU B 195 10988 7148 6066 -977 -375 1608 C ATOM 4501 N MET B 196 39.284 10.082 145.027 1.00 59.91 N ANISOU 4501 N MET B 196 10060 6722 5978 -359 -319 1527 N ATOM 4502 CA MET B 196 38.183 10.286 144.070 1.00 59.42 C ANISOU 4502 CA MET B 196 9912 6750 5912 -261 -204 1446 C ATOM 4503 C MET B 196 37.745 8.984 143.414 1.00 59.30 C ANISOU 4503 C MET B 196 9846 6751 5931 -239 -228 1423 C ATOM 4504 O MET B 196 36.543 8.700 143.338 1.00 59.08 O ANISOU 4504 O MET B 196 9804 6788 5853 -258 -163 1364 O ATOM 4505 CB MET B 196 38.581 11.278 142.978 1.00 58.96 C ANISOU 4505 CB MET B 196 9765 6723 5913 -117 -155 1441 C ATOM 4506 CG MET B 196 38.475 12.731 143.386 1.00 59.13 C ANISOU 4506 CG MET B 196 9804 6751 5910 -114 -72 1431 C ATOM 4507 SD MET B 196 38.793 13.791 141.966 1.00 59.07 S ANISOU 4507 SD MET B 196 9685 6782 5976 53 -24 1444 S ATOM 4508 CE MET B 196 40.586 13.783 141.898 1.00 58.65 C ANISOU 4508 CE MET B 196 9652 6646 5985 70 -113 1498 C ATOM 4509 N VAL B 197 38.722 8.206 142.934 1.00 59.28 N ANISOU 4509 N VAL B 197 9805 6683 6033 -205 -310 1458 N ATOM 4510 CA VAL B 197 38.462 6.866 142.377 1.00 59.13 C ANISOU 4510 CA VAL B 197 9737 6653 6074 -204 -325 1427 C ATOM 4511 C VAL B 197 37.707 5.992 143.381 1.00 59.57 C ANISOU 4511 C VAL B 197 9872 6691 6071 -330 -355 1438 C ATOM 4512 O VAL B 197 36.786 5.278 142.998 1.00 59.32 O ANISOU 4512 O VAL B 197 9810 6707 6020 -336 -306 1375 O ATOM 4513 CB VAL B 197 39.766 6.165 141.911 1.00 59.42 C ANISOU 4513 CB VAL B 197 9714 6578 6282 -169 -396 1459 C ATOM 4514 CG1 VAL B 197 39.554 4.673 141.646 1.00 59.84 C ANISOU 4514 CG1 VAL B 197 9726 6581 6427 -201 -411 1429 C ATOM 4515 CG2 VAL B 197 40.313 6.844 140.659 1.00 59.25 C ANISOU 4515 CG2 VAL B 197 9608 6596 6305 -58 -331 1413 C ATOM 4516 N LEU B 198 38.083 6.059 144.657 1.00 60.30 N ANISOU 4516 N LEU B 198 10070 6718 6120 -448 -434 1517 N ATOM 4517 CA LEU B 198 37.353 5.324 145.699 1.00 61.26 C ANISOU 4517 CA LEU B 198 10291 6828 6154 -601 -459 1534 C ATOM 4518 C LEU B 198 35.938 5.877 145.925 1.00 60.99 C ANISOU 4518 C LEU B 198 10288 6900 5983 -639 -319 1434 C ATOM 4519 O LEU B 198 34.956 5.118 145.952 1.00 61.35 O ANISOU 4519 O LEU B 198 10337 6977 5997 -685 -276 1382 O ATOM 4520 CB LEU B 198 38.149 5.332 147.011 1.00 62.55 C ANISOU 4520 CB LEU B 198 10575 6910 6279 -752 -591 1658 C ATOM 4521 CG LEU B 198 37.840 4.191 147.982 1.00 63.94 C ANISOU 4521 CG LEU B 198 10848 7033 6411 -923 -682 1730 C ATOM 4522 CD1 LEU B 198 38.406 2.870 147.461 1.00 64.45 C ANISOU 4522 CD1 LEU B 198 10825 6986 6675 -868 -784 1793 C ATOM 4523 CD2 LEU B 198 38.381 4.517 149.370 1.00 65.02 C ANISOU 4523 CD2 LEU B 198 11133 7136 6433 -1118 -796 1845 C ATOM 4524 N ILE B 199 35.837 7.195 146.074 1.00 60.81 N ANISOU 4524 N ILE B 199 10274 6921 5907 -620 -240 1402 N ATOM 4525 CA ILE B 199 34.551 7.884 146.282 1.00 61.17 C ANISOU 4525 CA ILE B 199 10318 7041 5880 -648 -91 1300 C ATOM 4526 C ILE B 199 33.525 7.502 145.222 1.00 60.85 C ANISOU 4526 C ILE B 199 10159 7074 5885 -545 -24 1227 C ATOM 4527 O ILE B 199 32.381 7.216 145.564 1.00 61.39 O ANISOU 4527 O ILE B 199 10237 7176 5909 -615 52 1157 O ATOM 4528 CB ILE B 199 34.717 9.431 146.335 1.00 61.08 C ANISOU 4528 CB ILE B 199 10292 7044 5872 -604 -6 1276 C ATOM 4529 CG1 ILE B 199 35.369 9.851 147.659 1.00 61.74 C ANISOU 4529 CG1 ILE B 199 10518 7076 5864 -772 -35 1313 C ATOM 4530 CG2 ILE B 199 33.370 10.148 146.209 1.00 61.22 C ANISOU 4530 CG2 ILE B 199 10243 7117 5899 -582 155 1170 C ATOM 4531 CD1 ILE B 199 36.095 11.176 147.584 1.00 61.45 C ANISOU 4531 CD1 ILE B 199 10462 7025 5858 -714 -2 1321 C ATOM 4532 N TYR B 200 33.923 7.484 143.954 1.00 60.50 N ANISOU 4532 N TYR B 200 10007 7058 5921 -399 -52 1240 N ATOM 4533 CA TYR B 200 32.989 7.125 142.870 1.00 60.22 C ANISOU 4533 CA TYR B 200 9861 7110 5909 -324 -6 1180 C ATOM 4534 C TYR B 200 32.529 5.672 142.971 1.00 60.61 C ANISOU 4534 C TYR B 200 9929 7152 5948 -397 -29 1149 C ATOM 4535 O TYR B 200 31.323 5.418 142.966 1.00 60.97 O ANISOU 4535 O TYR B 200 9945 7255 5962 -428 36 1081 O ATOM 4536 CB TYR B 200 33.545 7.464 141.477 1.00 59.54 C ANISOU 4536 CB TYR B 200 9673 7069 5878 -191 -25 1198 C ATOM 4537 CG TYR B 200 33.405 8.935 141.144 1.00 59.10 C ANISOU 4537 CG TYR B 200 9565 7055 5836 -110 24 1215 C ATOM 4538 CD1 TYR B 200 32.142 9.520 140.993 1.00 59.26 C ANISOU 4538 CD1 TYR B 200 9511 7140 5862 -91 98 1180 C ATOM 4539 CD2 TYR B 200 34.524 9.752 141.000 1.00 58.94 C ANISOU 4539 CD2 TYR B 200 9554 6993 5845 -54 0 1269 C ATOM 4540 CE1 TYR B 200 32.004 10.870 140.710 1.00 59.30 C ANISOU 4540 CE1 TYR B 200 9451 7158 5921 -15 141 1210 C ATOM 4541 CE2 TYR B 200 34.393 11.106 140.710 1.00 58.99 C ANISOU 4541 CE2 TYR B 200 9510 7022 5878 16 49 1291 C ATOM 4542 CZ TYR B 200 33.135 11.656 140.567 1.00 59.15 C ANISOU 4542 CZ TYR B 200 9454 7097 5921 37 118 1267 C ATOM 4543 OH TYR B 200 33.012 12.996 140.271 1.00 59.66 O ANISOU 4543 OH TYR B 200 9452 7163 6053 112 163 1303 O ATOM 4544 N LEU B 201 33.463 4.737 143.128 1.00 61.01 N ANISOU 4544 N LEU B 201 10020 7116 6044 -429 -119 1201 N ATOM 4545 CA LEU B 201 33.110 3.326 143.395 1.00 62.23 C ANISOU 4545 CA LEU B 201 10201 7230 6210 -513 -145 1187 C ATOM 4546 C LEU B 201 32.061 3.225 144.506 1.00 62.84 C ANISOU 4546 C LEU B 201 10369 7321 6184 -646 -96 1157 C ATOM 4547 O LEU B 201 31.029 2.551 144.346 1.00 62.69 O ANISOU 4547 O LEU B 201 10324 7347 6146 -679 -40 1085 O ATOM 4548 CB LEU B 201 34.356 2.500 143.759 1.00 63.05 C ANISOU 4548 CB LEU B 201 10342 7196 6414 -549 -265 1280 C ATOM 4549 CG LEU B 201 35.311 2.167 142.592 1.00 62.79 C ANISOU 4549 CG LEU B 201 10203 7125 6528 -440 -285 1273 C ATOM 4550 CD1 LEU B 201 36.699 1.788 143.085 1.00 63.23 C ANISOU 4550 CD1 LEU B 201 10276 7023 6723 -461 -407 1382 C ATOM 4551 CD2 LEU B 201 34.753 1.056 141.712 1.00 63.14 C ANISOU 4551 CD2 LEU B 201 10169 7194 6625 -432 -229 1181 C ATOM 4552 N GLU B 202 32.307 3.935 145.608 1.00 63.71 N ANISOU 4552 N GLU B 202 10586 7399 6223 -737 -102 1199 N ATOM 4553 CA GLU B 202 31.315 4.030 146.696 1.00 65.32 C ANISOU 4553 CA GLU B 202 10884 7619 6313 -891 -21 1146 C ATOM 4554 C GLU B 202 29.978 4.633 146.228 1.00 65.73 C ANISOU 4554 C GLU B 202 10840 7765 6370 -837 128 1022 C ATOM 4555 O GLU B 202 28.909 4.108 146.561 1.00 66.57 O ANISOU 4555 O GLU B 202 10959 7894 6440 -923 201 947 O ATOM 4556 CB GLU B 202 31.883 4.830 147.879 1.00 66.02 C ANISOU 4556 CB GLU B 202 11104 7667 6314 -1018 -35 1196 C ATOM 4557 CG GLU B 202 31.126 4.697 149.189 1.00 67.36 C ANISOU 4557 CG GLU B 202 11414 7834 6343 -1243 34 1152 C ATOM 4558 CD GLU B 202 31.138 3.298 149.767 1.00 68.12 C ANISOU 4558 CD GLU B 202 11608 7880 6395 -1383 -64 1222 C ATOM 4559 OE1 GLU B 202 32.134 2.558 149.590 1.00 67.92 O ANISOU 4559 OE1 GLU B 202 11579 7780 6444 -1351 -226 1349 O ATOM 4560 OE2 GLU B 202 30.133 2.930 150.413 1.00 69.44 O ANISOU 4560 OE2 GLU B 202 11846 8067 6469 -1530 26 1148 O ATOM 4561 N VAL B 203 30.037 5.711 145.444 1.00 65.88 N ANISOU 4561 N VAL B 203 10753 7828 6449 -698 165 1010 N ATOM 4562 CA VAL B 203 28.820 6.370 144.924 1.00 66.64 C ANISOU 4562 CA VAL B 203 10726 7998 6593 -633 280 924 C ATOM 4563 C VAL B 203 27.992 5.395 144.087 1.00 67.27 C ANISOU 4563 C VAL B 203 10715 8145 6697 -598 275 879 C ATOM 4564 O VAL B 203 26.785 5.339 144.241 1.00 68.09 O ANISOU 4564 O VAL B 203 10773 8284 6813 -639 365 796 O ATOM 4565 CB VAL B 203 29.144 7.658 144.113 1.00 66.41 C ANISOU 4565 CB VAL B 203 10592 7997 6643 -484 289 957 C ATOM 4566 CG1 VAL B 203 27.924 8.178 143.356 1.00 66.77 C ANISOU 4566 CG1 VAL B 203 10478 8114 6775 -403 361 907 C ATOM 4567 CG2 VAL B 203 29.706 8.743 145.028 1.00 66.62 C ANISOU 4567 CG2 VAL B 203 10697 7959 6655 -535 335 969 C ATOM 4568 N PHE B 204 28.648 4.633 143.217 1.00 67.65 N ANISOU 4568 N PHE B 204 10735 8206 6762 -534 183 921 N ATOM 4569 CA PHE B 204 27.979 3.599 142.422 1.00 68.73 C ANISOU 4569 CA PHE B 204 10798 8404 6909 -526 182 868 C ATOM 4570 C PHE B 204 27.421 2.504 143.342 1.00 70.27 C ANISOU 4570 C PHE B 204 11082 8555 7062 -666 208 824 C ATOM 4571 O PHE B 204 26.219 2.151 143.259 1.00 70.64 O ANISOU 4571 O PHE B 204 11076 8657 7104 -703 277 740 O ATOM 4572 CB PHE B 204 28.932 2.987 141.384 1.00 68.30 C ANISOU 4572 CB PHE B 204 10707 8353 6890 -460 105 900 C ATOM 4573 CG PHE B 204 29.367 3.947 140.298 1.00 67.67 C ANISOU 4573 CG PHE B 204 10539 8338 6831 -342 87 934 C ATOM 4574 CD1 PHE B 204 28.443 4.504 139.424 1.00 67.88 C ANISOU 4574 CD1 PHE B 204 10451 8485 6855 -290 112 912 C ATOM 4575 CD2 PHE B 204 30.708 4.277 140.134 1.00 66.98 C ANISOU 4575 CD2 PHE B 204 10482 8191 6776 -293 35 997 C ATOM 4576 CE1 PHE B 204 28.837 5.382 138.418 1.00 67.39 C ANISOU 4576 CE1 PHE B 204 10318 8485 6801 -201 82 965 C ATOM 4577 CE2 PHE B 204 31.114 5.155 139.133 1.00 66.63 C ANISOU 4577 CE2 PHE B 204 10368 8207 6740 -199 25 1028 C ATOM 4578 CZ PHE B 204 30.177 5.714 138.281 1.00 66.92 C ANISOU 4578 CZ PHE B 204 10304 8367 6755 -158 46 1017 C ATOM 4579 N TYR B 205 28.284 1.993 144.228 1.00 75.06 N ANISOU 4579 N TYR B 205 8230 9242 11046 -822 288 -1523 N ATOM 4580 CA TYR B 205 27.873 0.969 145.204 1.00 76.94 C ANISOU 4580 CA TYR B 205 8415 9279 11540 -816 239 -1396 C ATOM 4581 C TYR B 205 26.600 1.359 145.959 1.00 75.80 C ANISOU 4581 C TYR B 205 8453 9098 11248 -868 237 -1301 C ATOM 4582 O TYR B 205 25.664 0.567 146.046 1.00 75.94 O ANISOU 4582 O TYR B 205 8432 8990 11432 -826 247 -1347 O ATOM 4583 CB TYR B 205 28.995 0.650 146.206 1.00 79.04 C ANISOU 4583 CB TYR B 205 8603 9484 11945 -869 145 -1144 C ATOM 4584 CG TYR B 205 28.514 -0.131 147.415 1.00 80.80 C ANISOU 4584 CG TYR B 205 8802 9548 12349 -911 71 -929 C ATOM 4585 CD1 TYR B 205 28.107 -1.461 147.290 1.00 82.47 C ANISOU 4585 CD1 TYR B 205 8830 9564 12938 -823 80 -990 C ATOM 4586 CD2 TYR B 205 28.435 0.466 148.678 1.00 80.86 C ANISOU 4586 CD2 TYR B 205 8964 9611 12146 -1060 2 -674 C ATOM 4587 CE1 TYR B 205 27.654 -2.181 148.386 1.00 83.67 C ANISOU 4587 CE1 TYR B 205 8947 9579 13265 -866 4 -768 C ATOM 4588 CE2 TYR B 205 27.982 -0.247 149.781 1.00 82.11 C ANISOU 4588 CE2 TYR B 205 9093 9661 12444 -1126 -70 -466 C ATOM 4589 CZ TYR B 205 27.600 -1.571 149.632 1.00 83.62 C ANISOU 4589 CZ TYR B 205 9093 9657 13020 -1021 -79 -496 C ATOM 4590 OH TYR B 205 27.145 -2.278 150.725 1.00 84.97 O ANISOU 4590 OH TYR B 205 9221 9728 13335 -1092 -160 -263 O ATOM 4591 N LEU B 206 26.566 2.575 146.493 1.00 74.80 N ANISOU 4591 N LEU B 206 8518 9073 10830 -963 241 -1181 N ATOM 4592 CA LEU B 206 25.371 3.077 147.208 1.00 74.08 C ANISOU 4592 CA LEU B 206 8601 8943 10603 -1026 276 -1112 C ATOM 4593 C LEU B 206 24.120 3.079 146.338 1.00 73.78 C ANISOU 4593 C LEU B 206 8571 8894 10566 -945 347 -1282 C ATOM 4594 O LEU B 206 23.075 2.569 146.753 1.00 73.63 O ANISOU 4594 O LEU B 206 8573 8761 10643 -935 355 -1268 O ATOM 4595 CB LEU B 206 25.608 4.489 147.772 1.00 73.36 C ANISOU 4595 CB LEU B 206 8698 8956 10220 -1152 313 -1008 C ATOM 4596 CG LEU B 206 26.554 4.519 148.972 1.00 73.93 C ANISOU 4596 CG LEU B 206 8797 9051 10241 -1296 239 -800 C ATOM 4597 CD1 LEU B 206 27.234 5.872 149.094 1.00 73.55 C ANISOU 4597 CD1 LEU B 206 8881 9140 9924 -1406 281 -766 C ATOM 4598 CD2 LEU B 206 25.827 4.168 150.260 1.00 74.39 C ANISOU 4598 CD2 LEU B 206 8928 9025 10309 -1411 223 -658 C ATOM 4599 N ILE B 207 24.231 3.628 145.128 1.00 74.21 N ANISOU 4599 N ILE B 207 8597 9087 10513 -901 391 -1424 N ATOM 4600 CA ILE B 207 23.088 3.761 144.210 1.00 74.45 C ANISOU 4600 CA ILE B 207 8618 9163 10506 -856 445 -1551 C ATOM 4601 C ILE B 207 22.582 2.383 143.790 1.00 76.18 C ANISOU 4601 C ILE B 207 8690 9292 10962 -789 435 -1698 C ATOM 4602 O ILE B 207 21.368 2.144 143.818 1.00 75.75 O ANISOU 4602 O ILE B 207 8659 9174 10946 -775 456 -1715 O ATOM 4603 CB ILE B 207 23.431 4.625 142.964 1.00 74.10 C ANISOU 4603 CB ILE B 207 8542 9331 10281 -856 476 -1640 C ATOM 4604 CG1 ILE B 207 23.685 6.075 143.379 1.00 73.10 C ANISOU 4604 CG1 ILE B 207 8563 9261 9949 -921 508 -1491 C ATOM 4605 CG2 ILE B 207 22.321 4.582 141.919 1.00 74.43 C ANISOU 4605 CG2 ILE B 207 8524 9461 10296 -835 508 -1751 C ATOM 4606 CD1 ILE B 207 24.363 6.932 142.340 1.00 73.25 C ANISOU 4606 CD1 ILE B 207 8541 9484 9806 -932 518 -1527 C ATOM 4607 N ARG B 208 23.499 1.480 143.419 1.00 78.48 N ANISOU 4607 N ARG B 208 8820 9563 11434 -753 416 -1808 N ATOM 4608 CA ARG B 208 23.085 0.122 143.031 1.00 80.67 C ANISOU 4608 CA ARG B 208 8939 9725 11985 -699 433 -1975 C ATOM 4609 C ARG B 208 22.386 -0.626 144.188 1.00 80.89 C ANISOU 4609 C ARG B 208 8991 9535 12209 -687 394 -1834 C ATOM 4610 O ARG B 208 21.368 -1.305 143.978 1.00 80.86 O ANISOU 4610 O ARG B 208 8946 9452 12325 -659 416 -1931 O ATOM 4611 CB ARG B 208 24.267 -0.658 142.454 1.00 83.18 C ANISOU 4611 CB ARG B 208 9062 10031 12512 -668 454 -2127 C ATOM 4612 CG ARG B 208 24.656 -0.131 141.066 1.00 84.51 C ANISOU 4612 CG ARG B 208 9180 10440 12489 -695 514 -2338 C ATOM 4613 CD ARG B 208 26.112 -0.345 140.711 1.00 86.59 C ANISOU 4613 CD ARG B 208 9310 10731 12858 -685 537 -2416 C ATOM 4614 NE ARG B 208 26.404 0.145 139.358 1.00 87.64 N ANISOU 4614 NE ARG B 208 9392 11122 12783 -734 600 -2629 N ATOM 4615 CZ ARG B 208 27.624 0.272 138.824 1.00 89.45 C ANISOU 4615 CZ ARG B 208 9527 11450 13008 -745 634 -2718 C ATOM 4616 NH1 ARG B 208 28.723 -0.055 139.512 1.00 90.25 N ANISOU 4616 NH1 ARG B 208 9562 11403 13323 -702 609 -2602 N ATOM 4617 NH2 ARG B 208 27.751 0.735 137.580 1.00 90.12 N ANISOU 4617 NH2 ARG B 208 9569 11802 12868 -815 689 -2907 N ATOM 4618 N LYS B 209 22.907 -0.458 145.403 1.00 81.50 N ANISOU 4618 N LYS B 209 9134 9539 12290 -731 332 -1598 N ATOM 4619 CA LYS B 209 22.279 -1.033 146.605 1.00 82.23 C ANISOU 4619 CA LYS B 209 9259 9468 12515 -757 284 -1422 C ATOM 4620 C LYS B 209 20.911 -0.409 146.891 1.00 81.74 C ANISOU 4620 C LYS B 209 9368 9415 12273 -788 324 -1395 C ATOM 4621 O LYS B 209 19.951 -1.131 147.170 1.00 82.16 O ANISOU 4621 O LYS B 209 9399 9345 12473 -764 323 -1397 O ATOM 4622 CB LYS B 209 23.190 -0.896 147.834 1.00 82.55 C ANISOU 4622 CB LYS B 209 9327 9492 12545 -847 203 -1156 C ATOM 4623 CG LYS B 209 22.779 -1.789 148.999 1.00 83.71 C ANISOU 4623 CG LYS B 209 9431 9483 12889 -887 133 -960 C ATOM 4624 CD LYS B 209 23.826 -1.872 150.094 1.00 84.84 C ANISOU 4624 CD LYS B 209 9532 9641 13060 -998 30 -676 C ATOM 4625 CE LYS B 209 23.844 -0.643 150.991 1.00 84.04 C ANISOU 4625 CE LYS B 209 9654 9691 12584 -1168 30 -530 C ATOM 4626 NZ LYS B 209 22.618 -0.521 151.834 1.00 83.65 N ANISOU 4626 NZ LYS B 209 9746 9607 12428 -1253 57 -467 N ATOM 4627 N GLN B 210 20.814 0.918 146.815 1.00 81.73 N ANISOU 4627 N GLN B 210 9521 9544 11987 -839 370 -1366 N ATOM 4628 CA GLN B 210 19.523 1.607 147.003 1.00 81.50 C ANISOU 4628 CA GLN B 210 9630 9505 11828 -863 436 -1341 C ATOM 4629 C GLN B 210 18.488 1.219 145.942 1.00 81.80 C ANISOU 4629 C GLN B 210 9591 9554 11934 -785 468 -1502 C ATOM 4630 O GLN B 210 17.316 1.036 146.266 1.00 81.23 O ANISOU 4630 O GLN B 210 9560 9392 11909 -780 492 -1474 O ATOM 4631 CB GLN B 210 19.701 3.129 147.057 1.00 81.26 C ANISOU 4631 CB GLN B 210 9746 9586 11540 -930 502 -1281 C ATOM 4632 CG GLN B 210 20.278 3.618 148.373 1.00 82.12 C ANISOU 4632 CG GLN B 210 9978 9677 11543 -1059 499 -1118 C ATOM 4633 CD GLN B 210 20.221 5.129 148.525 1.00 82.63 C ANISOU 4633 CD GLN B 210 10195 9808 11392 -1140 605 -1085 C ATOM 4634 OE1 GLN B 210 19.228 5.776 148.168 1.00 83.26 O ANISOU 4634 OE1 GLN B 210 10323 9864 11446 -1115 699 -1116 O ATOM 4635 NE2 GLN B 210 21.288 5.702 149.067 1.00 83.19 N ANISOU 4635 NE2 GLN B 210 10328 9951 11329 -1245 595 -1010 N ATOM 4636 N LEU B 211 18.925 1.087 144.689 1.00 83.04 N ANISOU 4636 N LEU B 211 9629 9835 12084 -744 470 -1670 N ATOM 4637 CA LEU B 211 18.069 0.532 143.625 1.00 84.15 C ANISOU 4637 CA LEU B 211 9664 10023 12285 -709 491 -1845 C ATOM 4638 C LEU B 211 17.655 -0.905 143.957 1.00 85.80 C ANISOU 4638 C LEU B 211 9773 10050 12775 -670 470 -1912 C ATOM 4639 O LEU B 211 16.472 -1.252 143.845 1.00 85.94 O ANISOU 4639 O LEU B 211 9787 10021 12843 -660 484 -1944 O ATOM 4640 CB LEU B 211 18.766 0.573 142.258 1.00 84.42 C ANISOU 4640 CB LEU B 211 9574 10256 12243 -716 505 -2036 C ATOM 4641 CG LEU B 211 18.902 1.944 141.579 1.00 83.35 C ANISOU 4641 CG LEU B 211 9495 10339 11832 -760 523 -1984 C ATOM 4642 CD1 LEU B 211 19.885 1.873 140.417 1.00 84.24 C ANISOU 4642 CD1 LEU B 211 9481 10651 11876 -784 529 -2162 C ATOM 4643 CD2 LEU B 211 17.560 2.492 141.112 1.00 82.77 C ANISOU 4643 CD2 LEU B 211 9443 10345 11658 -782 544 -1930 C ATOM 4644 N ALA B1001 18.624 -1.725 144.375 1.00 87.58 N ANISOU 4644 N ALA B1001 9904 10163 13207 -649 436 -1911 N ATOM 4645 CA ALA B1001 18.344 -3.109 144.783 1.00 89.73 C ANISOU 4645 CA ALA B1001 10055 10228 13807 -610 418 -1938 C ATOM 4646 C ALA B1001 17.314 -3.208 145.922 1.00 90.71 C ANISOU 4646 C ALA B1001 10286 10219 13958 -625 387 -1749 C ATOM 4647 O ALA B1001 16.422 -4.063 145.888 1.00 91.53 O ANISOU 4647 O ALA B1001 10327 10208 14239 -596 393 -1812 O ATOM 4648 CB ALA B1001 19.630 -3.826 145.168 1.00 90.79 C ANISOU 4648 CB ALA B1001 10052 10252 14189 -589 383 -1892 C ATOM 4649 N ASP B1002 17.432 -2.327 146.916 1.00 91.80 N ANISOU 4649 N ASP B1002 10583 10381 13915 -688 367 -1535 N ATOM 4650 CA ASP B1002 16.502 -2.302 148.065 1.00 92.90 C ANISOU 4650 CA ASP B1002 10835 10419 14041 -736 359 -1364 C ATOM 4651 C ASP B1002 15.052 -1.994 147.678 1.00 93.28 C ANISOU 4651 C ASP B1002 10951 10473 14015 -716 421 -1431 C ATOM 4652 O ASP B1002 14.123 -2.622 148.206 1.00 93.61 O ANISOU 4652 O ASP B1002 10992 10391 14184 -712 414 -1385 O ATOM 4653 CB ASP B1002 16.976 -1.307 149.136 1.00 93.02 C ANISOU 4653 CB ASP B1002 11009 10493 13840 -849 357 -1167 C ATOM 4654 CG ASP B1002 18.245 -1.767 149.855 1.00 94.49 C ANISOU 4654 CG ASP B1002 11119 10662 14120 -902 267 -1017 C ATOM 4655 OD1 ASP B1002 18.876 -2.759 149.426 1.00 95.15 O ANISOU 4655 OD1 ASP B1002 11015 10676 14462 -829 219 -1069 O ATOM 4656 OD2 ASP B1002 18.612 -1.125 150.862 1.00 95.60 O ANISOU 4656 OD2 ASP B1002 11375 10862 14087 -1032 254 -845 O ATOM 4657 N LEU B1003 14.857 -1.039 146.765 1.00 94.81 N ANISOU 4657 N LEU B1003 11188 10814 14019 -709 476 -1514 N ATOM 4658 CA LEU B1003 13.511 -0.721 146.261 1.00 96.60 C ANISOU 4658 CA LEU B1003 11441 11066 14196 -694 526 -1548 C ATOM 4659 C LEU B1003 12.869 -1.901 145.528 1.00 98.92 C ANISOU 4659 C LEU B1003 11590 11324 14672 -647 504 -1708 C ATOM 4660 O LEU B1003 11.692 -2.192 145.750 1.00 98.39 O ANISOU 4660 O LEU B1003 11537 11175 14672 -638 516 -1678 O ATOM 4661 CB LEU B1003 13.532 0.497 145.334 1.00 96.79 C ANISOU 4661 CB LEU B1003 11491 11273 14010 -707 573 -1567 C ATOM 4662 CG LEU B1003 13.867 1.841 145.969 1.00 96.41 C ANISOU 4662 CG LEU B1003 11590 11245 13794 -760 631 -1422 C ATOM 4663 CD1 LEU B1003 14.068 2.886 144.876 1.00 96.84 C ANISOU 4663 CD1 LEU B1003 11618 11482 13692 -763 660 -1439 C ATOM 4664 CD2 LEU B1003 12.795 2.271 146.959 1.00 95.87 C ANISOU 4664 CD2 LEU B1003 11643 11043 13740 -795 709 -1295 C ATOM 4665 N GLU B1004 13.642 -2.574 144.672 1.00102.66 N ANISOU 4665 N GLU B1004 11920 11854 15232 -627 486 -1891 N ATOM 4666 CA GLU B1004 13.163 -3.787 143.988 1.00105.63 C ANISOU 4666 CA GLU B1004 12143 12184 15807 -607 490 -2089 C ATOM 4667 C GLU B1004 12.942 -4.942 144.979 1.00106.58 C ANISOU 4667 C GLU B1004 12219 12054 16221 -572 458 -2025 C ATOM 4668 O GLU B1004 12.013 -5.744 144.804 1.00107.11 O ANISOU 4668 O GLU B1004 12221 12039 16437 -561 466 -2108 O ATOM 4669 CB GLU B1004 14.119 -4.233 142.868 1.00108.29 C ANISOU 4669 CB GLU B1004 12327 12631 16187 -618 515 -2336 C ATOM 4670 CG GLU B1004 14.431 -3.197 141.788 1.00109.20 C ANISOU 4670 CG GLU B1004 12453 13025 16010 -672 537 -2404 C ATOM 4671 CD GLU B1004 13.202 -2.626 141.101 1.00110.00 C ANISOU 4671 CD GLU B1004 12577 13291 15924 -724 542 -2387 C ATOM 4672 OE1 GLU B1004 12.205 -3.361 140.925 1.00111.48 O ANISOU 4672 OE1 GLU B1004 12708 13430 16218 -736 546 -2463 O ATOM 4673 OE2 GLU B1004 13.240 -1.434 140.728 1.00109.66 O ANISOU 4673 OE2 GLU B1004 12593 13427 15644 -757 540 -2279 O ATOM 4674 N ASP B1005 13.792 -5.019 146.009 1.00107.18 N ANISOU 4674 N ASP B1005 12320 12025 16379 -571 416 -1859 N ATOM 4675 CA ASP B1005 13.606 -5.980 147.105 1.00108.45 C ANISOU 4675 CA ASP B1005 12435 11971 16797 -561 367 -1715 C ATOM 4676 C ASP B1005 12.274 -5.736 147.831 1.00107.88 C ANISOU 4676 C ASP B1005 12493 11852 16645 -586 370 -1582 C ATOM 4677 O ASP B1005 11.477 -6.665 147.998 1.00108.54 O ANISOU 4677 O ASP B1005 12506 11799 16934 -561 358 -1598 O ATOM 4678 CB ASP B1005 14.783 -5.917 148.092 1.00109.13 C ANISOU 4678 CB ASP B1005 12523 12017 16922 -595 305 -1507 C ATOM 4679 CG ASP B1005 14.756 -7.038 149.123 1.00111.57 C ANISOU 4679 CG ASP B1005 12726 12124 17538 -599 235 -1330 C ATOM 4680 OD1 ASP B1005 14.664 -8.220 148.726 1.00114.36 O ANISOU 4680 OD1 ASP B1005 12895 12325 18229 -536 243 -1446 O ATOM 4681 OD2 ASP B1005 14.843 -6.737 150.333 1.00111.75 O ANISOU 4681 OD2 ASP B1005 12840 12150 17469 -682 178 -1072 O ATOM 4682 N ASN B1006 12.031 -4.487 148.234 1.00107.85 N ANISOU 4682 N ASN B1006 12666 11948 16363 -637 401 -1463 N ATOM 4683 CA ASN B1006 10.750 -4.112 148.870 1.00107.63 C ANISOU 4683 CA ASN B1006 12758 11874 16260 -667 439 -1356 C ATOM 4684 C ASN B1006 9.545 -4.304 147.946 1.00108.12 C ANISOU 4684 C ASN B1006 12773 11951 16353 -620 473 -1488 C ATOM 4685 O ASN B1006 8.494 -4.776 148.386 1.00108.02 O ANISOU 4685 O ASN B1006 12768 11831 16444 -616 476 -1439 O ATOM 4686 CB ASN B1006 10.779 -2.659 149.366 1.00107.25 C ANISOU 4686 CB ASN B1006 12889 11916 15944 -738 507 -1243 C ATOM 4687 CG ASN B1006 11.667 -2.470 150.589 1.00107.69 C ANISOU 4687 CG ASN B1006 13017 11961 15936 -837 479 -1081 C ATOM 4688 OD1 ASN B1006 11.706 -3.314 151.488 1.00109.41 O ANISOU 4688 OD1 ASN B1006 13196 12085 16290 -878 415 -964 O ATOM 4689 ND2 ASN B1006 12.379 -1.350 150.632 1.00107.15 N ANISOU 4689 ND2 ASN B1006 13048 12006 15658 -894 523 -1057 N ATOM 4690 N TRP B1007 9.704 -3.933 146.675 1.00109.36 N ANISOU 4690 N TRP B1007 12876 12265 16410 -604 493 -1640 N ATOM 4691 CA TRP B1007 8.652 -4.104 145.656 1.00110.38 C ANISOU 4691 CA TRP B1007 12933 12469 16536 -595 510 -1759 C ATOM 4692 C TRP B1007 8.315 -5.574 145.427 1.00112.93 C ANISOU 4692 C TRP B1007 13115 12677 17114 -573 483 -1906 C ATOM 4693 O TRP B1007 7.135 -5.927 145.346 1.00113.47 O ANISOU 4693 O TRP B1007 13166 12705 17241 -573 487 -1910 O ATOM 4694 CB TRP B1007 9.080 -3.450 144.334 1.00110.13 C ANISOU 4694 CB TRP B1007 12848 12675 16321 -621 524 -1880 C ATOM 4695 CG TRP B1007 8.094 -3.565 143.203 1.00110.15 C ANISOU 4695 CG TRP B1007 12757 12820 16274 -657 527 -1982 C ATOM 4696 CD1 TRP B1007 8.270 -4.232 142.022 1.00111.21 C ANISOU 4696 CD1 TRP B1007 12743 13096 16413 -706 521 -2220 C ATOM 4697 CD2 TRP B1007 6.785 -2.989 143.144 1.00109.81 C ANISOU 4697 CD2 TRP B1007 12747 12809 16166 -672 543 -1843 C ATOM 4698 NE1 TRP B1007 7.150 -4.105 141.230 1.00111.65 N ANISOU 4698 NE1 TRP B1007 12741 13302 16376 -769 515 -2227 N ATOM 4699 CE2 TRP B1007 6.224 -3.343 141.892 1.00110.53 C ANISOU 4699 CE2 TRP B1007 12701 13087 16206 -737 521 -1978 C ATOM 4700 CE3 TRP B1007 6.031 -2.195 144.021 1.00108.75 C ANISOU 4700 CE3 TRP B1007 12732 12566 16022 -650 586 -1621 C ATOM 4701 CZ2 TRP B1007 4.937 -2.942 141.506 1.00110.34 C ANISOU 4701 CZ2 TRP B1007 12647 13149 16128 -774 517 -1857 C ATOM 4702 CZ3 TRP B1007 4.759 -1.791 143.631 1.00108.61 C ANISOU 4702 CZ3 TRP B1007 12682 12600 15986 -667 604 -1518 C ATOM 4703 CH2 TRP B1007 4.221 -2.177 142.392 1.00109.57 C ANISOU 4703 CH2 TRP B1007 12656 12911 16063 -724 557 -1615 C ATOM 4704 N GLU B1008 9.345 -6.420 145.328 1.00115.68 N ANISOU 4704 N GLU B1008 13350 12960 17640 -555 464 -2024 N ATOM 4705 CA GLU B1008 9.140 -7.864 145.166 1.00118.08 C ANISOU 4705 CA GLU B1008 13497 13110 18257 -533 462 -2174 C ATOM 4706 C GLU B1008 8.608 -8.517 146.448 1.00117.39 C ANISOU 4706 C GLU B1008 13432 12795 18376 -507 420 -1982 C ATOM 4707 O GLU B1008 7.782 -9.429 146.370 1.00118.36 O ANISOU 4707 O GLU B1008 13473 12805 18694 -496 423 -2053 O ATOM 4708 CB GLU B1008 10.420 -8.564 144.696 1.00120.65 C ANISOU 4708 CB GLU B1008 13668 13398 18775 -520 483 -2351 C ATOM 4709 CG GLU B1008 10.174 -9.971 144.162 1.00123.91 C ANISOU 4709 CG GLU B1008 13888 13672 19518 -517 529 -2593 C ATOM 4710 CD GLU B1008 11.401 -10.621 143.548 1.00126.85 C ANISOU 4710 CD GLU B1008 14084 14000 20111 -513 593 -2816 C ATOM 4711 OE1 GLU B1008 12.479 -9.985 143.480 1.00127.37 O ANISOU 4711 OE1 GLU B1008 14174 14160 20057 -509 589 -2780 O ATOM 4712 OE2 GLU B1008 11.281 -11.792 143.123 1.00128.91 O ANISOU 4712 OE2 GLU B1008 14170 14117 20690 -519 662 -3042 O ATOM 4713 N THR B1009 9.076 -8.058 147.613 1.00116.11 N ANISOU 4713 N THR B1009 13372 12585 18159 -518 383 -1741 N ATOM 4714 CA THR B1009 8.542 -8.520 148.907 1.00116.17 C ANISOU 4714 CA THR B1009 13414 12430 18295 -531 339 -1524 C ATOM 4715 C THR B1009 7.032 -8.276 149.021 1.00116.07 C ANISOU 4715 C THR B1009 13492 12415 18193 -540 370 -1492 C ATOM 4716 O THR B1009 6.278 -9.175 149.422 1.00117.14 O ANISOU 4716 O THR B1009 13568 12405 18532 -528 347 -1457 O ATOM 4717 CB THR B1009 9.252 -7.829 150.094 1.00115.34 C ANISOU 4717 CB THR B1009 13425 12352 18044 -597 305 -1278 C ATOM 4718 OG1 THR B1009 10.659 -8.091 150.028 1.00115.75 O ANISOU 4718 OG1 THR B1009 13376 12404 18200 -591 265 -1273 O ATOM 4719 CG2 THR B1009 8.715 -8.327 151.441 1.00115.53 C ANISOU 4719 CG2 THR B1009 13472 12252 18170 -652 258 -1048 C ATOM 4720 N LEU B1010 6.606 -7.069 148.651 1.00115.74 N ANISOU 4720 N LEU B1010 13574 12522 17877 -560 426 -1491 N ATOM 4721 CA LEU B1010 5.194 -6.681 148.722 1.00115.81 C ANISOU 4721 CA LEU B1010 13657 12531 17815 -567 470 -1436 C ATOM 4722 C LEU B1010 4.294 -7.499 147.787 1.00117.63 C ANISOU 4722 C LEU B1010 13762 12753 18177 -539 461 -1596 C ATOM 4723 O LEU B1010 3.168 -7.843 148.162 1.00117.33 O ANISOU 4723 O LEU B1010 13733 12624 18221 -535 465 -1532 O ATOM 4724 CB LEU B1010 5.030 -5.180 148.440 1.00114.63 C ANISOU 4724 CB LEU B1010 13625 12526 17401 -591 542 -1385 C ATOM 4725 CG LEU B1010 3.720 -4.541 148.931 1.00114.27 C ANISOU 4725 CG LEU B1010 13674 12435 17308 -608 617 -1255 C ATOM 4726 CD1 LEU B1010 3.700 -4.418 150.452 1.00114.09 C ANISOU 4726 CD1 LEU B1010 13771 12294 17283 -667 652 -1098 C ATOM 4727 CD2 LEU B1010 3.498 -3.186 148.274 1.00113.92 C ANISOU 4727 CD2 LEU B1010 13672 12521 17089 -615 692 -1224 C ATOM 4728 N ASN B1011 4.783 -7.820 146.588 1.00120.15 N ANISOU 4728 N ASN B1011 13963 13178 18507 -538 457 -1812 N ATOM 4729 CA ASN B1011 4.046 -8.700 145.665 1.00122.78 C ANISOU 4729 CA ASN B1011 14163 13527 18960 -551 458 -2006 C ATOM 4730 C ASN B1011 4.092 -10.177 146.092 1.00124.72 C ANISOU 4730 C ASN B1011 14289 13545 19553 -522 436 -2076 C ATOM 4731 O ASN B1011 3.066 -10.863 146.046 1.00125.28 O ANISOU 4731 O ASN B1011 14308 13537 19753 -527 434 -2112 O ATOM 4732 CB ASN B1011 4.558 -8.547 144.222 1.00124.22 C ANISOU 4732 CB ASN B1011 14251 13932 19015 -603 480 -2241 C ATOM 4733 CG ASN B1011 4.184 -7.207 143.596 1.00123.68 C ANISOU 4733 CG ASN B1011 14252 14104 18636 -647 489 -2153 C ATOM 4734 OD1 ASN B1011 3.166 -6.600 143.940 1.00122.82 O ANISOU 4734 OD1 ASN B1011 14217 13989 18456 -641 494 -1969 O ATOM 4735 ND2 ASN B1011 5.002 -6.748 142.653 1.00124.31 N ANISOU 4735 ND2 ASN B1011 14288 14391 18553 -694 499 -2274 N ATOM 4736 N ASP B1012 5.269 -10.656 146.502 1.00126.00 N ANISOU 4736 N ASP B1012 14390 13595 19888 -495 421 -2076 N ATOM 4737 CA ASP B1012 5.445 -12.059 146.926 1.00127.92 C ANISOU 4737 CA ASP B1012 14481 13594 20528 -463 405 -2107 C ATOM 4738 C ASP B1012 4.533 -12.469 148.091 1.00128.23 C ANISOU 4738 C ASP B1012 14562 13467 20691 -450 356 -1878 C ATOM 4739 O ASP B1012 3.966 -13.564 148.073 1.00130.13 O ANISOU 4739 O ASP B1012 14681 13548 21212 -437 356 -1946 O ATOM 4740 CB ASP B1012 6.913 -12.353 147.291 1.00128.82 C ANISOU 4740 CB ASP B1012 14509 13616 20818 -437 388 -2064 C ATOM 4741 CG ASP B1012 7.826 -12.458 146.067 1.00130.48 C ANISOU 4741 CG ASP B1012 14603 13918 21052 -446 458 -2358 C ATOM 4742 OD1 ASP B1012 7.388 -12.139 144.939 1.00130.81 O ANISOU 4742 OD1 ASP B1012 14653 14149 20900 -496 511 -2583 O ATOM 4743 OD2 ASP B1012 9.000 -12.853 146.240 1.00131.40 O ANISOU 4743 OD2 ASP B1012 14610 13933 21383 -418 461 -2353 O ATOM 4744 N ASN B1013 4.384 -11.595 149.085 1.00127.19 N ANISOU 4744 N ASN B1013 14596 13377 20353 -470 329 -1623 N ATOM 4745 CA ASN B1013 3.532 -11.891 150.248 1.00127.40 C ANISOU 4745 CA ASN B1013 14673 13279 20455 -486 294 -1402 C ATOM 4746 C ASN B1013 2.021 -11.812 149.969 1.00127.38 C ANISOU 4746 C ASN B1013 14716 13291 20389 -486 328 -1440 C ATOM 4747 O ASN B1013 1.227 -12.435 150.692 1.00127.49 O ANISOU 4747 O ASN B1013 14715 13171 20553 -489 303 -1324 O ATOM 4748 CB ASN B1013 3.928 -11.005 151.437 1.00126.53 C ANISOU 4748 CB ASN B1013 14716 13223 20137 -547 278 -1148 C ATOM 4749 CG ASN B1013 5.254 -11.419 152.061 1.00127.54 C ANISOU 4749 CG ASN B1013 14759 13295 20402 -569 209 -1019 C ATOM 4750 OD1 ASN B1013 5.961 -12.289 151.545 1.00128.96 O ANISOU 4750 OD1 ASN B1013 14762 13380 20856 -518 187 -1125 O ATOM 4751 ND2 ASN B1013 5.603 -10.788 153.177 1.00127.13 N ANISOU 4751 ND2 ASN B1013 14824 13309 20171 -661 185 -789 N ATOM 4752 N LEU B1014 1.620 -11.088 148.919 1.00127.88 N ANISOU 4752 N LEU B1014 14817 13524 20246 -491 376 -1580 N ATOM 4753 CA LEU B1014 0.221 -11.125 148.447 1.00128.99 C ANISOU 4753 CA LEU B1014 14953 13695 20360 -498 397 -1621 C ATOM 4754 C LEU B1014 -0.180 -12.505 147.904 1.00131.42 C ANISOU 4754 C LEU B1014 15093 13896 20945 -494 380 -1805 C ATOM 4755 O LEU B1014 -1.351 -12.882 147.989 1.00132.21 O ANISOU 4755 O LEU B1014 15179 13940 21112 -500 375 -1776 O ATOM 4756 CB LEU B1014 -0.048 -10.052 147.381 1.00128.58 C ANISOU 4756 CB LEU B1014 14939 13875 20040 -526 436 -1690 C ATOM 4757 CG LEU B1014 -0.174 -8.604 147.864 1.00127.26 C ANISOU 4757 CG LEU B1014 14929 13785 19637 -532 485 -1496 C ATOM 4758 CD1 LEU B1014 -0.099 -7.650 146.681 1.00126.98 C ANISOU 4758 CD1 LEU B1014 14878 13978 19387 -558 507 -1558 C ATOM 4759 CD2 LEU B1014 -1.460 -8.388 148.651 1.00126.96 C ANISOU 4759 CD2 LEU B1014 14963 13650 19623 -532 522 -1321 C ATOM 4760 N LYS B1015 0.784 -13.244 147.350 1.00133.54 N ANISOU 4760 N LYS B1015 15227 14125 21388 -491 385 -2002 N ATOM 4761 CA LYS B1015 0.560 -14.635 146.930 1.00135.53 C ANISOU 4761 CA LYS B1015 15299 14227 21969 -496 399 -2203 C ATOM 4762 C LYS B1015 0.431 -15.556 148.148 1.00136.73 C ANISOU 4762 C LYS B1015 15400 14107 22445 -450 352 -2012 C ATOM 4763 O LYS B1015 -0.366 -16.496 148.137 1.00136.46 O ANISOU 4763 O LYS B1015 15270 13935 22641 -452 352 -2068 O ATOM 4764 CB LYS B1015 1.696 -15.128 146.025 1.00136.49 C ANISOU 4764 CB LYS B1015 15275 14359 22225 -513 454 -2485 C ATOM 4765 CG LYS B1015 1.871 -14.343 144.731 1.00136.06 C ANISOU 4765 CG LYS B1015 15242 14602 21853 -588 498 -2693 C ATOM 4766 CD LYS B1015 3.246 -14.571 144.123 1.00137.09 C ANISOU 4766 CD LYS B1015 15264 14748 22074 -599 557 -2912 C ATOM 4767 CE LYS B1015 3.508 -13.626 142.962 1.00136.71 C ANISOU 4767 CE LYS B1015 15253 15029 21659 -684 587 -3062 C ATOM 4768 NZ LYS B1015 4.915 -13.716 142.487 1.00137.34 N ANISOU 4768 NZ LYS B1015 15247 15130 21803 -690 647 -3246 N ATOM 4769 N VAL B1016 1.222 -15.277 149.187 1.00138.56 N ANISOU 4769 N VAL B1016 15683 14280 22682 -428 306 -1774 N ATOM 4770 CA VAL B1016 1.161 -16.010 150.459 1.00141.43 C ANISOU 4770 CA VAL B1016 15998 14437 23302 -415 239 -1519 C ATOM 4771 C VAL B1016 -0.171 -15.755 151.172 1.00143.34 C ANISOU 4771 C VAL B1016 16361 14683 23416 -439 221 -1343 C ATOM 4772 O VAL B1016 -0.797 -16.702 151.653 1.00145.42 O ANISOU 4772 O VAL B1016 16535 14777 23939 -432 188 -1266 O ATOM 4773 CB VAL B1016 2.349 -15.654 151.397 1.00140.82 C ANISOU 4773 CB VAL B1016 15947 14360 23195 -430 184 -1281 C ATOM 4774 CG1 VAL B1016 2.194 -16.313 152.769 1.00141.35 C ANISOU 4774 CG1 VAL B1016 15963 14275 23468 -459 98 -964 C ATOM 4775 CG2 VAL B1016 3.676 -16.061 150.765 1.00142.02 C ANISOU 4775 CG2 VAL B1016 15943 14465 23552 -397 204 -1432 C ATOM 4776 N ILE B1017 -0.599 -14.490 151.238 1.00144.71 N ANISOU 4776 N ILE B1017 16723 15036 23223 -466 253 -1279 N ATOM 4777 CA ILE B1017 -1.895 -14.150 151.864 1.00145.97 C ANISOU 4777 CA ILE B1017 16993 15197 23271 -490 267 -1131 C ATOM 4778 C ILE B1017 -3.087 -14.752 151.100 1.00147.81 C ANISOU 4778 C ILE B1017 17149 15394 23618 -471 282 -1278 C ATOM 4779 O ILE B1017 -4.003 -15.299 151.722 1.00149.92 O ANISOU 4779 O ILE B1017 17402 15545 24015 -475 262 -1165 O ATOM 4780 CB ILE B1017 -2.078 -12.617 152.035 1.00145.40 C ANISOU 4780 CB ILE B1017 17114 15294 22836 -523 334 -1048 C ATOM 4781 CG1 ILE B1017 -1.079 -12.085 153.070 1.00145.92 C ANISOU 4781 CG1 ILE B1017 17270 15389 22785 -579 323 -875 C ATOM 4782 CG2 ILE B1017 -3.503 -12.266 152.470 1.00144.50 C ANISOU 4782 CG2 ILE B1017 17085 15166 22652 -541 382 -940 C ATOM 4783 CD1 ILE B1017 -0.882 -10.584 153.039 1.00144.94 C ANISOU 4783 CD1 ILE B1017 17308 15422 22339 -613 407 -859 C ATOM 4784 N GLU B1018 -3.071 -14.650 149.769 1.00148.42 N ANISOU 4784 N GLU B1018 17170 15591 23629 -471 314 -1522 N ATOM 4785 CA GLU B1018 -4.168 -15.171 148.929 1.00148.56 C ANISOU 4785 CA GLU B1018 17107 15627 23711 -492 325 -1676 C ATOM 4786 C GLU B1018 -4.318 -16.701 148.954 1.00149.39 C ANISOU 4786 C GLU B1018 17042 15518 24199 -484 305 -1786 C ATOM 4787 O GLU B1018 -5.423 -17.209 148.753 1.00149.76 O ANISOU 4787 O GLU B1018 17044 15527 24328 -504 303 -1824 O ATOM 4788 CB GLU B1018 -4.029 -14.688 147.474 1.00148.95 C ANISOU 4788 CB GLU B1018 17122 15907 23562 -540 359 -1906 C ATOM 4789 CG GLU B1018 -4.419 -13.228 147.252 1.00147.87 C ANISOU 4789 CG GLU B1018 17114 15980 23087 -556 380 -1777 C ATOM 4790 CD GLU B1018 -5.918 -12.962 147.343 1.00147.36 C ANISOU 4790 CD GLU B1018 17080 15935 22974 -570 383 -1640 C ATOM 4791 OE1 GLU B1018 -6.717 -13.923 147.390 1.00147.59 O ANISOU 4791 OE1 GLU B1018 17030 15857 23190 -580 361 -1681 O ATOM 4792 OE2 GLU B1018 -6.299 -11.773 147.367 1.00146.17 O ANISOU 4792 OE2 GLU B1018 17019 15895 22622 -570 417 -1485 O ATOM 4793 N LYS B1019 -3.218 -17.419 149.192 1.00149.47 N ANISOU 4793 N LYS B1019 16943 15380 24465 -457 295 -1825 N ATOM 4794 CA LYS B1019 -3.229 -18.883 149.279 1.00150.53 C ANISOU 4794 CA LYS B1019 16885 15265 25041 -443 293 -1910 C ATOM 4795 C LYS B1019 -2.584 -19.351 150.591 1.00151.98 C ANISOU 4795 C LYS B1019 17022 15249 25473 -403 227 -1625 C ATOM 4796 O LYS B1019 -1.558 -20.038 150.587 1.00153.12 O ANISOU 4796 O LYS B1019 17008 15245 25922 -379 232 -1667 O ATOM 4797 CB LYS B1019 -2.516 -19.491 148.064 1.00150.61 C ANISOU 4797 CB LYS B1019 16735 15268 25222 -470 372 -2276 C ATOM 4798 CG LYS B1019 -3.191 -19.195 146.730 1.00149.49 C ANISOU 4798 CG LYS B1019 16604 15356 24839 -558 428 -2560 C ATOM 4799 CD LYS B1019 -2.336 -19.626 145.546 1.00150.36 C ANISOU 4799 CD LYS B1019 16571 15512 25044 -622 527 -2941 C ATOM 4800 CE LYS B1019 -2.283 -21.139 145.394 1.00152.54 C ANISOU 4800 CE LYS B1019 16627 15509 25821 -635 603 -3164 C ATOM 4801 NZ LYS B1019 -1.444 -21.547 144.235 1.00154.26 N ANISOU 4801 NZ LYS B1019 16699 15767 26146 -718 738 -3578 N ATOM 4802 N ALA B1020 -3.204 -18.964 151.707 1.00152.48 N ANISOU 4802 N ALA B1020 17207 15321 25406 -414 170 -1327 N ATOM 4803 CA ALA B1020 -2.766 -19.352 153.057 1.00154.19 C ANISOU 4803 CA ALA B1020 17383 15406 25794 -423 90 -1005 C ATOM 4804 C ALA B1020 -3.839 -20.196 153.748 1.00154.93 C ANISOU 4804 C ALA B1020 17416 15343 26106 -432 47 -852 C ATOM 4805 O ALA B1020 -5.033 -19.905 153.632 1.00154.87 O ANISOU 4805 O ALA B1020 17508 15399 25934 -443 73 -882 O ATOM 4806 CB ALA B1020 -2.448 -18.115 153.891 1.00153.59 C ANISOU 4806 CB ALA B1020 17507 15511 25338 -475 71 -781 C ATOM 4807 N ASP B1021 -3.407 -21.225 154.478 1.00155.90 N ANISOU 4807 N ASP B1021 17360 15261 26611 -430 -21 -664 N ATOM 4808 CA ASP B1021 -4.326 -22.115 155.200 1.00156.19 C ANISOU 4808 CA ASP B1021 17310 15137 26896 -443 -74 -484 C ATOM 4809 C ASP B1021 -4.666 -21.529 156.564 1.00156.34 C ANISOU 4809 C ASP B1021 17472 15274 26655 -530 -140 -129 C ATOM 4810 O ASP B1021 -5.838 -21.333 156.890 1.00155.92 O ANISOU 4810 O ASP B1021 17524 15264 26454 -558 -126 -78 O ATOM 4811 CB ASP B1021 -3.726 -23.521 155.374 1.00157.17 C ANISOU 4811 CB ASP B1021 17142 14973 27599 -411 -115 -410 C ATOM 4812 CG ASP B1021 -3.521 -24.255 154.055 1.00156.81 C ANISOU 4812 CG ASP B1021 16932 14775 27871 -350 -10 -807 C ATOM 4813 OD1 ASP B1021 -3.872 -23.708 152.986 1.00154.25 O ANISOU 4813 OD1 ASP B1021 16720 14602 27283 -351 75 -1132 O ATOM 4814 OD2 ASP B1021 -2.996 -25.385 154.094 1.00157.54 O ANISOU 4814 OD2 ASP B1021 16767 14600 28491 -318 -7 -790 O ATOM 4815 N ASN B1022 -3.627 -21.257 157.363 1.00157.84 N ANISOU 4815 N ASN B1022 17656 15527 26787 -591 -205 111 N ATOM 4816 CA ASN B1022 -3.779 -20.791 158.753 1.00158.22 C ANISOU 4816 CA ASN B1022 17812 15710 26593 -726 -267 455 C ATOM 4817 C ASN B1022 -3.442 -19.294 158.892 1.00157.21 C ANISOU 4817 C ASN B1022 17929 15841 25961 -795 -204 425 C ATOM 4818 O ASN B1022 -2.521 -18.773 158.235 1.00155.85 O ANISOU 4818 O ASN B1022 17783 15734 25696 -754 -174 276 O ATOM 4819 CB ASN B1022 -2.897 -21.626 159.720 1.00159.98 C ANISOU 4819 CB ASN B1022 17824 15846 27115 -798 -403 814 C ATOM 4820 CG ASN B1022 -3.243 -21.398 161.181 1.00160.12 C ANISOU 4820 CG ASN B1022 17912 16012 26912 -979 -477 1180 C ATOM 4821 OD1 ASN B1022 -4.348 -20.969 161.511 1.00159.02 O ANISOU 4821 OD1 ASN B1022 17933 15958 26526 -1029 -421 1160 O ATOM 4822 ND2 ASN B1022 -2.295 -21.690 162.066 1.00161.50 N ANISOU 4822 ND2 ASN B1022 17952 16231 27176 -1095 -601 1523 N ATOM 4823 N ALA B1023 -4.175 -18.622 159.784 1.00157.82 N ANISOU 4823 N ALA B1023 18175 16055 25732 -911 -173 565 N ATOM 4824 CA ALA B1023 -3.979 -17.192 160.079 1.00157.81 C ANISOU 4824 CA ALA B1023 18403 16278 25278 -1004 -84 544 C ATOM 4825 C ALA B1023 -2.527 -16.820 160.422 1.00159.57 C ANISOU 4825 C ALA B1023 18618 16616 25394 -1084 -138 659 C ATOM 4826 O ALA B1023 -2.082 -15.708 160.114 1.00159.64 O ANISOU 4826 O ALA B1023 18779 16765 25111 -1097 -57 530 O ATOM 4827 CB ALA B1023 -4.910 -16.756 161.204 1.00157.30 C ANISOU 4827 CB ALA B1023 18473 16314 24979 -1155 -33 704 C ATOM 4828 N ALA B1024 -1.802 -17.750 161.050 1.00161.58 N ANISOU 4828 N ALA B1024 18678 16808 25905 -1140 -278 921 N ATOM 4829 CA ALA B1024 -0.363 -17.600 161.312 1.00162.21 C ANISOU 4829 CA ALA B1024 18692 16975 25964 -1208 -355 1065 C ATOM 4830 C ALA B1024 0.476 -17.380 160.045 1.00161.35 C ANISOU 4830 C ALA B1024 18556 16814 25935 -1051 -310 791 C ATOM 4831 O ALA B1024 1.469 -16.651 160.089 1.00160.02 O ANISOU 4831 O ALA B1024 18452 16787 25560 -1105 -310 808 O ATOM 4832 CB ALA B1024 0.164 -18.804 162.082 1.00164.89 C ANISOU 4832 CB ALA B1024 18765 17214 26669 -1274 -522 1424 C ATOM 4833 N GLN B1025 0.083 -18.004 158.930 1.00161.38 N ANISOU 4833 N GLN B1025 18463 16633 26220 -879 -268 534 N ATOM 4834 CA GLN B1025 0.751 -17.771 157.636 1.00160.77 C ANISOU 4834 CA GLN B1025 18367 16536 26182 -753 -203 229 C ATOM 4835 C GLN B1025 0.463 -16.359 157.104 1.00159.94 C ANISOU 4835 C GLN B1025 18513 16629 25626 -753 -90 20 C ATOM 4836 O GLN B1025 1.356 -15.689 156.565 1.00160.12 O ANISOU 4836 O GLN B1025 18584 16752 25502 -734 -59 -95 O ATOM 4837 CB GLN B1025 0.329 -18.817 156.596 1.00159.61 C ANISOU 4837 CB GLN B1025 18048 16169 26426 -617 -169 -15 C ATOM 4838 CG GLN B1025 0.693 -20.250 156.962 1.00160.97 C ANISOU 4838 CG GLN B1025 17931 16091 27137 -595 -253 159 C ATOM 4839 CD GLN B1025 0.292 -21.259 155.899 1.00161.16 C ANISOU 4839 CD GLN B1025 17785 15888 27560 -480 -183 -137 C ATOM 4840 OE1 GLN B1025 -0.679 -21.063 155.167 1.00159.00 O ANISOU 4840 OE1 GLN B1025 17613 15651 27145 -447 -105 -396 O ATOM 4841 NE2 GLN B1025 1.038 -22.353 155.818 1.00162.94 N ANISOU 4841 NE2 GLN B1025 17732 15873 28303 -433 -204 -94 N ATOM 4842 N VAL B1026 -0.783 -15.917 157.282 1.00159.30 N ANISOU 4842 N VAL B1026 18577 16595 25355 -777 -25 -6 N ATOM 4843 CA VAL B1026 -1.229 -14.589 156.855 1.00156.90 C ANISOU 4843 CA VAL B1026 18483 16447 24684 -779 92 -160 C ATOM 4844 C VAL B1026 -0.558 -13.489 157.691 1.00156.02 C ANISOU 4844 C VAL B1026 18528 16510 24241 -912 121 -24 C ATOM 4845 O VAL B1026 -0.105 -12.487 157.138 1.00154.67 O ANISOU 4845 O VAL B1026 18462 16452 23852 -895 191 -157 O ATOM 4846 CB VAL B1026 -2.775 -14.470 156.922 1.00156.55 C ANISOU 4846 CB VAL B1026 18518 16376 24586 -773 161 -187 C ATOM 4847 CG1 VAL B1026 -3.246 -13.057 156.580 1.00155.97 C ANISOU 4847 CG1 VAL B1026 18633 16440 24188 -781 293 -293 C ATOM 4848 CG2 VAL B1026 -3.426 -15.483 155.984 1.00156.42 C ANISOU 4848 CG2 VAL B1026 18354 16214 24864 -660 139 -351 C ATOM 4849 N LYS B1027 -0.487 -13.689 159.009 1.00156.88 N ANISOU 4849 N LYS B1027 18641 16655 24311 -1063 66 240 N ATOM 4850 CA LYS B1027 0.151 -12.729 159.930 1.00157.37 C ANISOU 4850 CA LYS B1027 18841 16906 24045 -1243 95 372 C ATOM 4851 C LYS B1027 1.644 -12.529 159.631 1.00157.98 C ANISOU 4851 C LYS B1027 18870 17052 24103 -1239 35 378 C ATOM 4852 O LYS B1027 2.133 -11.386 159.577 1.00157.74 O ANISOU 4852 O LYS B1027 18988 17166 23781 -1296 115 302 O ATOM 4853 CB LYS B1027 -0.036 -13.185 161.383 1.00158.18 C ANISOU 4853 CB LYS B1027 18915 17062 24121 -1442 26 673 C ATOM 4854 CG LYS B1027 0.358 -12.152 162.428 1.00158.36 C ANISOU 4854 CG LYS B1027 19101 17313 23752 -1687 89 780 C ATOM 4855 CD LYS B1027 -0.215 -12.497 163.797 1.00158.93 C ANISOU 4855 CD LYS B1027 19174 17471 23740 -1912 62 1025 C ATOM 4856 CE LYS B1027 -0.032 -11.363 164.790 1.00158.77 C ANISOU 4856 CE LYS B1027 19340 17694 23288 -2190 181 1054 C ATOM 4857 NZ LYS B1027 -0.820 -11.596 166.031 1.00159.62 N ANISOU 4857 NZ LYS B1027 19470 17901 23276 -2425 202 1228 N ATOM 4858 N ASP B1028 2.346 -13.649 159.438 1.00158.61 N ANISOU 4858 N ASP B1028 18728 17011 24524 -1171 -94 468 N ATOM 4859 CA ASP B1028 3.765 -13.654 159.047 1.00157.87 C ANISOU 4859 CA ASP B1028 18539 16939 24502 -1141 -153 472 C ATOM 4860 C ASP B1028 4.024 -12.942 157.713 1.00155.80 C ANISOU 4860 C ASP B1028 18352 16701 24140 -1002 -55 148 C ATOM 4861 O ASP B1028 5.085 -12.342 157.531 1.00156.84 O ANISOU 4861 O ASP B1028 18514 16939 24138 -1023 -56 131 O ATOM 4862 CB ASP B1028 4.307 -15.092 158.979 1.00159.52 C ANISOU 4862 CB ASP B1028 18459 16954 25198 -1069 -279 606 C ATOM 4863 CG ASP B1028 4.592 -15.684 160.353 1.00161.04 C ANISOU 4863 CG ASP B1028 18531 17178 25479 -1242 -418 1022 C ATOM 4864 OD1 ASP B1028 3.824 -15.430 161.307 1.00160.85 O ANISOU 4864 OD1 ASP B1028 18621 17264 25231 -1394 -415 1168 O ATOM 4865 OD2 ASP B1028 5.594 -16.416 160.475 1.00161.88 O ANISOU 4865 OD2 ASP B1028 18411 17204 25891 -1236 -529 1215 O ATOM 4866 N ALA B1029 3.066 -13.021 156.786 1.00153.36 N ANISOU 4866 N ALA B1029 18061 16314 23891 -878 21 -88 N ATOM 4867 CA ALA B1029 3.126 -12.253 155.535 1.00150.12 C ANISOU 4867 CA ALA B1029 17726 15974 23335 -782 112 -369 C ATOM 4868 C ALA B1029 2.844 -10.765 155.782 1.00147.46 C ANISOU 4868 C ALA B1029 17620 15806 22600 -859 217 -378 C ATOM 4869 O ALA B1029 3.626 -9.900 155.365 1.00147.29 O ANISOU 4869 O ALA B1029 17667 15899 22394 -861 254 -455 O ATOM 4870 CB ALA B1029 2.147 -12.817 154.517 1.00149.92 C ANISOU 4870 CB ALA B1029 17631 15849 23482 -667 150 -585 C ATOM 4871 N LEU B1030 1.734 -10.485 156.468 1.00145.38 N ANISOU 4871 N LEU B1030 17462 15540 22234 -925 277 -302 N ATOM 4872 CA LEU B1030 1.298 -9.108 156.760 1.00143.18 C ANISOU 4872 CA LEU B1030 17383 15374 21645 -1003 417 -322 C ATOM 4873 C LEU B1030 2.323 -8.288 157.546 1.00141.99 C ANISOU 4873 C LEU B1030 17336 15362 21249 -1154 437 -222 C ATOM 4874 O LEU B1030 2.554 -7.118 157.220 1.00142.10 O ANISOU 4874 O LEU B1030 17469 15466 21057 -1165 543 -320 O ATOM 4875 CB LEU B1030 -0.041 -9.106 157.516 1.00143.61 C ANISOU 4875 CB LEU B1030 17505 15377 21681 -1066 490 -246 C ATOM 4876 CG LEU B1030 -1.295 -9.470 156.711 1.00143.42 C ANISOU 4876 CG LEU B1030 17429 15249 21815 -936 519 -358 C ATOM 4877 CD1 LEU B1030 -2.456 -9.772 157.646 1.00143.77 C ANISOU 4877 CD1 LEU B1030 17504 15225 21895 -1009 558 -239 C ATOM 4878 CD2 LEU B1030 -1.672 -8.365 155.732 1.00142.44 C ANISOU 4878 CD2 LEU B1030 17376 15182 21560 -865 635 -507 C ATOM 4879 N THR B1031 2.927 -8.893 158.572 1.00141.28 N ANISOU 4879 N THR B1031 17188 15299 21190 -1283 332 -13 N ATOM 4880 CA THR B1031 3.960 -8.207 159.373 1.00140.58 C ANISOU 4880 CA THR B1031 17181 15376 20857 -1465 331 103 C ATOM 4881 C THR B1031 5.207 -7.846 158.542 1.00138.30 C ANISOU 4881 C THR B1031 16861 15140 20546 -1385 296 12 C ATOM 4882 O THR B1031 5.754 -6.738 158.674 1.00138.70 O ANISOU 4882 O THR B1031 17043 15321 20335 -1476 376 -26 O ATOM 4883 CB THR B1031 4.376 -9.037 160.606 1.00142.64 C ANISOU 4883 CB THR B1031 17343 15684 21167 -1641 193 397 C ATOM 4884 OG1 THR B1031 4.700 -10.374 160.206 1.00145.13 O ANISOU 4884 OG1 THR B1031 17430 15854 21860 -1508 37 481 O ATOM 4885 CG2 THR B1031 3.250 -9.080 161.634 1.00142.90 C ANISOU 4885 CG2 THR B1031 17451 15737 21106 -1793 255 493 C ATOM 4886 N LYS B1032 5.633 -8.774 157.683 1.00136.13 N ANISOU 4886 N LYS B1032 16408 14756 20557 -1223 195 -39 N ATOM 4887 CA LYS B1032 6.744 -8.536 156.748 1.00134.93 C ANISOU 4887 CA LYS B1032 16205 14640 20420 -1131 175 -160 C ATOM 4888 C LYS B1032 6.388 -7.502 155.670 1.00133.04 C ANISOU 4888 C LYS B1032 16082 14453 20014 -1037 301 -404 C ATOM 4889 O LYS B1032 7.230 -6.671 155.308 1.00132.46 O ANISOU 4889 O LYS B1032 16066 14488 19773 -1047 331 -464 O ATOM 4890 CB LYS B1032 7.203 -9.848 156.098 1.00135.39 C ANISOU 4890 CB LYS B1032 16026 14548 20865 -997 72 -187 C ATOM 4891 CG LYS B1032 7.902 -10.790 157.066 1.00136.63 C ANISOU 4891 CG LYS B1032 16021 14656 21235 -1084 -67 101 C ATOM 4892 CD LYS B1032 8.162 -12.156 156.453 1.00137.22 C ANISOU 4892 CD LYS B1032 15836 14521 21780 -943 -132 65 C ATOM 4893 CE LYS B1032 8.743 -13.117 157.479 1.00138.57 C ANISOU 4893 CE LYS B1032 15810 14620 22220 -1031 -275 414 C ATOM 4894 NZ LYS B1032 8.623 -14.540 157.058 1.00139.41 N ANISOU 4894 NZ LYS B1032 15654 14464 22849 -902 -312 396 N ATOM 4895 N MET B1033 5.154 -7.561 155.161 1.00131.28 N ANISOU 4895 N MET B1033 15874 14159 19845 -955 366 -518 N ATOM 4896 CA MET B1033 4.628 -6.515 154.261 1.00128.58 C ANISOU 4896 CA MET B1033 15626 13878 19347 -894 483 -681 C ATOM 4897 C MET B1033 4.624 -5.138 154.929 1.00126.23 C ANISOU 4897 C MET B1033 15513 13674 18774 -1014 608 -630 C ATOM 4898 O MET B1033 5.001 -4.140 154.304 1.00125.81 O ANISOU 4898 O MET B1033 15518 13704 18579 -993 676 -716 O ATOM 4899 CB MET B1033 3.209 -6.850 153.780 1.00128.46 C ANISOU 4899 CB MET B1033 15582 13779 19448 -815 521 -753 C ATOM 4900 CG MET B1033 3.162 -7.885 152.673 1.00129.03 C ANISOU 4900 CG MET B1033 15484 13796 19744 -698 446 -902 C ATOM 4901 SD MET B1033 1.492 -8.213 152.082 1.00129.00 S ANISOU 4901 SD MET B1033 15444 13731 19838 -637 484 -977 S ATOM 4902 CE MET B1033 1.194 -6.780 151.050 1.00128.01 C ANISOU 4902 CE MET B1033 15391 13765 19481 -617 582 -1059 C ATOM 4903 N ARG B1034 4.201 -5.099 156.193 1.00124.55 N ANISOU 4903 N ARG B1034 15381 13447 18494 -1156 648 -496 N ATOM 4904 CA ARG B1034 4.208 -3.866 156.985 1.00123.30 C ANISOU 4904 CA ARG B1034 15393 13368 18086 -1315 798 -473 C ATOM 4905 C ARG B1034 5.637 -3.356 157.169 1.00122.44 C ANISOU 4905 C ARG B1034 15320 13391 17811 -1406 764 -446 C ATOM 4906 O ARG B1034 5.944 -2.212 156.801 1.00121.97 O ANISOU 4906 O ARG B1034 15350 13390 17603 -1414 873 -536 O ATOM 4907 CB ARG B1034 3.538 -4.087 158.349 1.00124.08 C ANISOU 4907 CB ARG B1034 15552 13455 18136 -1489 844 -350 C ATOM 4908 CG ARG B1034 3.069 -2.819 159.025 1.00124.29 C ANISOU 4908 CG ARG B1034 15748 13516 17958 -1644 1069 -399 C ATOM 4909 CD ARG B1034 2.212 -3.149 160.236 1.00125.58 C ANISOU 4909 CD ARG B1034 15954 13665 18094 -1811 1130 -312 C ATOM 4910 NE ARG B1034 1.885 -1.949 160.996 1.00125.83 N ANISOU 4910 NE ARG B1034 16143 13736 17931 -2003 1376 -388 N ATOM 4911 CZ ARG B1034 2.711 -1.312 161.830 1.00126.80 C ANISOU 4911 CZ ARG B1034 16364 14010 17803 -2244 1441 -381 C ATOM 4912 NH1 ARG B1034 3.962 -1.734 162.028 1.00126.97 N ANISOU 4912 NH1 ARG B1034 16340 14173 17728 -2318 1257 -264 N ATOM 4913 NH2 ARG B1034 2.289 -0.223 162.465 1.00128.27 N ANISOU 4913 NH2 ARG B1034 16685 14203 17847 -2423 1706 -498 N ATOM 4914 N ALA B1035 6.510 -4.225 157.689 1.00122.08 N ANISOU 4914 N ALA B1035 15183 13384 17818 -1470 607 -304 N ATOM 4915 CA ALA B1035 7.940 -3.906 157.851 1.00121.43 C ANISOU 4915 CA ALA B1035 15101 13429 17609 -1554 543 -245 C ATOM 4916 C ALA B1035 8.584 -3.411 156.546 1.00119.04 C ANISOU 4916 C ALA B1035 14773 13143 17311 -1396 552 -406 C ATOM 4917 O ALA B1035 9.380 -2.462 156.557 1.00117.70 O ANISOU 4917 O ALA B1035 14688 13083 16946 -1469 601 -429 O ATOM 4918 CB ALA B1035 8.695 -5.115 158.385 1.00122.88 C ANISOU 4918 CB ALA B1035 15121 13613 17951 -1600 352 -38 C ATOM 4919 N ALA B1036 8.228 -4.056 155.434 1.00118.07 N ANISOU 4919 N ALA B1036 14532 12926 17401 -1202 508 -521 N ATOM 4920 CA ALA B1036 8.641 -3.608 154.100 1.00116.67 C ANISOU 4920 CA ALA B1036 14323 12791 17214 -1069 527 -689 C ATOM 4921 C ALA B1036 8.050 -2.241 153.734 1.00115.24 C ANISOU 4921 C ALA B1036 14276 12656 16851 -1072 683 -774 C ATOM 4922 O ALA B1036 8.727 -1.430 153.099 1.00115.24 O ANISOU 4922 O ALA B1036 14302 12748 16736 -1051 714 -841 O ATOM 4923 CB ALA B1036 8.262 -4.643 153.048 1.00117.16 C ANISOU 4923 CB ALA B1036 14224 12765 17523 -910 463 -811 C ATOM 4924 N ALA B1037 6.796 -1.995 154.125 1.00114.61 N ANISOU 4924 N ALA B1037 14263 12503 16777 -1096 786 -760 N ATOM 4925 CA ALA B1037 6.152 -0.690 153.890 1.00114.10 C ANISOU 4925 CA ALA B1037 14300 12443 16609 -1104 958 -808 C ATOM 4926 C ALA B1037 6.810 0.445 154.684 1.00115.12 C ANISOU 4926 C ALA B1037 14570 12638 16532 -1263 1074 -783 C ATOM 4927 O ALA B1037 7.013 1.546 154.150 1.00115.04 O ANISOU 4927 O ALA B1037 14601 12663 16444 -1247 1174 -837 O ATOM 4928 CB ALA B1037 4.661 -0.758 154.198 1.00113.99 C ANISOU 4928 CB ALA B1037 14305 12313 16693 -1097 1052 -787 C ATOM 4929 N LEU B1038 7.141 0.171 155.948 1.00116.62 N ANISOU 4929 N LEU B1038 14822 12856 16632 -1436 1061 -694 N ATOM 4930 CA LEU B1038 7.857 1.135 156.799 1.00116.96 C ANISOU 4930 CA LEU B1038 14996 12994 16449 -1638 1165 -682 C ATOM 4931 C LEU B1038 9.273 1.427 156.291 1.00116.14 C ANISOU 4931 C LEU B1038 14868 13006 16250 -1621 1076 -690 C ATOM 4932 O LEU B1038 9.743 2.562 156.399 1.00116.37 O ANISOU 4932 O LEU B1038 14996 13094 16123 -1714 1196 -738 O ATOM 4933 CB LEU B1038 7.923 0.643 158.251 1.00118.81 C ANISOU 4933 CB LEU B1038 15275 13285 16580 -1865 1140 -562 C ATOM 4934 CG LEU B1038 6.595 0.520 159.006 1.00119.49 C ANISOU 4934 CG LEU B1038 15411 13283 16704 -1945 1264 -558 C ATOM 4935 CD1 LEU B1038 6.806 -0.213 160.325 1.00120.86 C ANISOU 4935 CD1 LEU B1038 15586 13558 16775 -2172 1178 -402 C ATOM 4936 CD2 LEU B1038 5.961 1.886 159.237 1.00119.27 C ANISOU 4936 CD2 LEU B1038 15516 13204 16595 -2035 1546 -688 C ATOM 4937 N ASP B1039 9.947 0.404 155.756 1.00114.79 N ANISOU 4937 N ASP B1039 14560 12856 16196 -1509 882 -649 N ATOM 4938 CA ASP B1039 11.244 0.584 155.082 1.00112.83 C ANISOU 4938 CA ASP B1039 14263 12704 15903 -1460 798 -672 C ATOM 4939 C ASP B1039 11.083 1.384 153.786 1.00110.72 C ANISOU 4939 C ASP B1039 13989 12440 15637 -1314 872 -809 C ATOM 4940 O ASP B1039 11.863 2.303 153.511 1.00110.21 O ANISOU 4940 O ASP B1039 13973 12462 15437 -1344 915 -840 O ATOM 4941 CB ASP B1039 11.895 -0.770 154.776 1.00112.63 C ANISOU 4941 CB ASP B1039 14063 12662 16068 -1367 605 -615 C ATOM 4942 CG ASP B1039 13.324 -0.633 154.250 1.00111.98 C ANISOU 4942 CG ASP B1039 13920 12677 15950 -1341 526 -624 C ATOM 4943 OD1 ASP B1039 14.180 -0.084 154.973 1.00112.31 O ANISOU 4943 OD1 ASP B1039 14032 12825 15813 -1497 524 -530 O ATOM 4944 OD2 ASP B1039 13.591 -1.073 153.105 1.00111.23 O ANISOU 4944 OD2 ASP B1039 13703 12561 15996 -1179 474 -733 O ATOM 4945 N ALA B1040 10.065 1.029 152.999 1.00109.40 N ANISOU 4945 N ALA B1040 13751 12194 15619 -1174 879 -873 N ATOM 4946 CA ALA B1040 9.787 1.699 151.727 1.00108.37 C ANISOU 4946 CA ALA B1040 13582 12097 15494 -1057 928 -962 C ATOM 4947 C ALA B1040 9.391 3.159 151.910 1.00107.58 C ANISOU 4947 C ALA B1040 13595 11983 15298 -1120 1113 -952 C ATOM 4948 O ALA B1040 9.723 3.983 151.070 1.00105.87 O ANISOU 4948 O ALA B1040 13357 11834 15032 -1075 1146 -979 O ATOM 4949 CB ALA B1040 8.707 0.957 150.954 1.00108.55 C ANISOU 4949 CB ALA B1040 13496 12063 15683 -935 890 -1008 C ATOM 4950 N GLN B1041 8.699 3.472 153.009 1.00108.49 N ANISOU 4950 N GLN B1041 13814 12005 15401 -1235 1245 -914 N ATOM 4951 CA GLN B1041 8.337 4.860 153.317 1.00108.78 C ANISOU 4951 CA GLN B1041 13950 11988 15393 -1317 1465 -927 C ATOM 4952 C GLN B1041 9.550 5.774 153.557 1.00109.34 C ANISOU 4952 C GLN B1041 14103 12151 15290 -1429 1514 -949 C ATOM 4953 O GLN B1041 9.489 6.962 153.228 1.00110.01 O ANISOU 4953 O GLN B1041 14212 12205 15380 -1432 1664 -972 O ATOM 4954 CB GLN B1041 7.387 4.924 154.519 1.00109.66 C ANISOU 4954 CB GLN B1041 14153 11982 15530 -1447 1621 -918 C ATOM 4955 CG GLN B1041 6.731 6.289 154.697 1.00110.11 C ANISOU 4955 CG GLN B1041 14272 11924 15639 -1504 1891 -956 C ATOM 4956 CD GLN B1041 5.668 6.301 155.781 1.00110.56 C ANISOU 4956 CD GLN B1041 14399 11854 15753 -1626 2070 -975 C ATOM 4957 OE1 GLN B1041 4.682 5.571 155.707 1.00109.65 O ANISOU 4957 OE1 GLN B1041 14224 11665 15773 -1542 2028 -936 O ATOM 4958 NE2 GLN B1041 5.861 7.141 156.792 1.00111.46 N ANISOU 4958 NE2 GLN B1041 14639 11950 15760 -1840 2283 -1052 N ATOM 4959 N LYS B1042 10.631 5.225 154.119 1.00110.13 N ANISOU 4959 N LYS B1042 14227 12357 15258 -1522 1389 -924 N ATOM 4960 CA LYS B1042 11.844 6.012 154.405 1.00110.73 C ANISOU 4960 CA LYS B1042 14378 12541 15152 -1648 1417 -934 C ATOM 4961 C LYS B1042 12.588 6.450 153.135 1.00108.66 C ANISOU 4961 C LYS B1042 14041 12355 14889 -1510 1353 -961 C ATOM 4962 O LYS B1042 12.712 5.710 152.150 1.00107.07 O ANISOU 4962 O LYS B1042 13714 12192 14773 -1351 1203 -966 O ATOM 4963 CB LYS B1042 12.795 5.246 155.338 1.00112.69 C ANISOU 4963 CB LYS B1042 14642 12901 15273 -1796 1277 -853 C ATOM 4964 CG LYS B1042 12.241 5.014 156.732 1.00114.79 C ANISOU 4964 CG LYS B1042 14993 13152 15467 -2005 1350 -810 C ATOM 4965 CD LYS B1042 13.154 4.107 157.540 1.00116.22 C ANISOU 4965 CD LYS B1042 15138 13467 15553 -2145 1165 -665 C ATOM 4966 CE LYS B1042 12.524 3.710 158.866 1.00117.87 C ANISOU 4966 CE LYS B1042 15402 13692 15689 -2361 1207 -593 C ATOM 4967 NZ LYS B1042 13.405 2.788 159.634 1.00119.15 N ANISOU 4967 NZ LYS B1042 15490 13999 15779 -2507 1002 -392 N ATOM 4968 N ARG B1062 3.873 9.156 151.195 1.00126.55 N ANISOU 4968 N ARG B1062 15929 13699 18454 -1063 2230 -688 N ATOM 4969 CA ARG B1062 3.578 9.145 152.625 1.00127.76 C ANISOU 4969 CA ARG B1062 16227 13717 18598 -1207 2410 -788 C ATOM 4970 C ARG B1062 2.154 8.655 152.880 1.00126.35 C ANISOU 4970 C ARG B1062 15997 13399 18608 -1167 2471 -742 C ATOM 4971 O ARG B1062 1.938 7.726 153.665 1.00127.22 O ANISOU 4971 O ARG B1062 16182 13513 18640 -1225 2419 -796 O ATOM 4972 CB ARG B1062 3.746 10.546 153.225 1.00130.73 C ANISOU 4972 CB ARG B1062 16672 13954 19043 -1332 2708 -847 C ATOM 4973 CG ARG B1062 5.109 11.185 152.989 1.00132.33 C ANISOU 4973 CG ARG B1062 16923 14278 19078 -1381 2676 -887 C ATOM 4974 CD ARG B1062 5.074 12.701 153.141 1.00135.59 C ANISOU 4974 CD ARG B1062 17333 14522 19662 -1451 2974 -907 C ATOM 4975 NE ARG B1062 6.250 13.327 152.532 1.00137.74 N ANISOU 4975 NE ARG B1062 17597 14915 19822 -1444 2905 -893 N ATOM 4976 CZ ARG B1062 6.433 14.641 152.369 1.00140.46 C ANISOU 4976 CZ ARG B1062 17905 15142 20321 -1475 3113 -880 C ATOM 4977 NH1 ARG B1062 5.516 15.525 152.770 1.00142.59 N ANISOU 4977 NH1 ARG B1062 18132 15144 20899 -1516 3428 -887 N ATOM 4978 NH2 ARG B1062 7.553 15.080 151.795 1.00140.06 N ANISOU 4978 NH2 ARG B1062 17847 15227 20139 -1465 3015 -859 N ATOM 4979 N HIS B1063 1.190 9.276 152.199 1.00123.57 N ANISOU 4979 N HIS B1063 15501 12930 18517 -1070 2570 -614 N ATOM 4980 CA HIS B1063 -0.222 8.966 152.409 1.00121.26 C ANISOU 4980 CA HIS B1063 15143 12488 18443 -1030 2654 -548 C ATOM 4981 C HIS B1063 -0.691 7.684 151.707 1.00118.64 C ANISOU 4981 C HIS B1063 14717 12278 18080 -917 2386 -480 C ATOM 4982 O HIS B1063 -1.613 7.012 152.188 1.00120.87 O ANISOU 4982 O HIS B1063 15003 12476 18445 -916 2401 -477 O ATOM 4983 CB HIS B1063 -1.111 10.145 152.017 1.00121.32 C ANISOU 4983 CB HIS B1063 15006 12301 18789 -980 2879 -407 C ATOM 4984 CG HIS B1063 -2.480 10.059 152.603 1.00120.85 C ANISOU 4984 CG HIS B1063 14909 12031 18975 -983 3058 -377 C ATOM 4985 ND1 HIS B1063 -2.741 10.362 153.922 1.00120.60 N ANISOU 4985 ND1 HIS B1063 15009 11825 18986 -1129 3334 -534 N ATOM 4986 CD2 HIS B1063 -3.653 9.652 152.067 1.00120.47 C ANISOU 4986 CD2 HIS B1063 14707 11938 19127 -876 2998 -215 C ATOM 4987 CE1 HIS B1063 -4.024 10.167 154.166 1.00122.07 C ANISOU 4987 CE1 HIS B1063 15122 11850 19407 -1098 3447 -472 C ATOM 4988 NE2 HIS B1063 -4.596 9.730 153.059 1.00121.50 N ANISOU 4988 NE2 HIS B1063 14876 11849 19438 -938 3239 -269 N ATOM 4989 N GLY B1064 -0.071 7.344 150.579 1.00115.01 N ANISOU 4989 N GLY B1064 14172 12020 17505 -838 2156 -440 N ATOM 4990 CA GLY B1064 -0.253 6.019 149.976 1.00112.56 C ANISOU 4990 CA GLY B1064 13795 11849 17122 -769 1907 -445 C ATOM 4991 C GLY B1064 0.206 4.931 150.943 1.00110.27 C ANISOU 4991 C GLY B1064 13641 11565 16690 -829 1828 -585 C ATOM 4992 O GLY B1064 -0.472 3.918 151.116 1.00109.60 O ANISOU 4992 O GLY B1064 13532 11452 16656 -804 1747 -588 O ATOM 4993 N PHE B1065 1.349 5.161 151.583 1.00108.53 N ANISOU 4993 N PHE B1065 13548 11384 16304 -918 1850 -675 N ATOM 4994 CA PHE B1065 1.856 4.291 152.653 1.00106.14 C ANISOU 4994 CA PHE B1065 13361 11092 15872 -1011 1790 -757 C ATOM 4995 C PHE B1065 0.977 4.310 153.912 1.00105.71 C ANISOU 4995 C PHE B1065 13395 10886 15884 -1118 1967 -763 C ATOM 4996 O PHE B1065 0.839 3.276 154.571 1.00106.22 O ANISOU 4996 O PHE B1065 13489 10954 15915 -1160 1877 -771 O ATOM 4997 CB PHE B1065 3.315 4.635 153.019 1.00105.34 C ANISOU 4997 CB PHE B1065 13359 11096 15570 -1106 1770 -820 C ATOM 4998 CG PHE B1065 4.314 4.275 151.950 1.00103.76 C ANISOU 4998 CG PHE B1065 13078 11058 15285 -1017 1570 -838 C ATOM 4999 CD1 PHE B1065 4.474 2.953 151.549 1.00103.03 C ANISOU 4999 CD1 PHE B1065 12907 11033 15207 -947 1365 -864 C ATOM 5000 CD2 PHE B1065 5.096 5.256 151.337 1.00103.01 C ANISOU 5000 CD2 PHE B1065 12976 11043 15117 -1010 1601 -840 C ATOM 5001 CE1 PHE B1065 5.372 2.615 150.543 1.00102.18 C ANISOU 5001 CE1 PHE B1065 12714 11067 15041 -878 1214 -914 C ATOM 5002 CE2 PHE B1065 6.008 4.922 150.347 1.00102.46 C ANISOU 5002 CE2 PHE B1065 12830 11136 14964 -941 1430 -870 C ATOM 5003 CZ PHE B1065 6.146 3.600 149.949 1.00102.08 C ANISOU 5003 CZ PHE B1065 12703 11153 14929 -879 1244 -918 C ATOM 5004 N ASP B1066 0.390 5.466 154.253 1.00104.36 N ANISOU 5004 N ASP B1066 13251 10575 15823 -1171 2227 -759 N ATOM 5005 CA ASP B1066 -0.633 5.535 155.319 1.00103.81 C ANISOU 5005 CA ASP B1066 13238 10347 15855 -1270 2432 -780 C ATOM 5006 C ASP B1066 -1.826 4.632 154.973 1.00103.94 C ANISOU 5006 C ASP B1066 13150 10307 16035 -1152 2337 -697 C ATOM 5007 O ASP B1066 -2.209 3.762 155.766 1.00103.52 O ANISOU 5007 O ASP B1066 13143 10238 15951 -1214 2302 -713 O ATOM 5008 CB ASP B1066 -1.154 6.968 155.546 1.00104.27 C ANISOU 5008 CB ASP B1066 13300 10226 16090 -1323 2761 -799 C ATOM 5009 CG ASP B1066 -0.104 7.922 156.122 1.00103.20 C ANISOU 5009 CG ASP B1066 13287 10119 15805 -1485 2915 -917 C ATOM 5010 OD1 ASP B1066 0.921 7.462 156.665 1.00102.24 O ANISOU 5010 OD1 ASP B1066 13274 10156 15416 -1602 2794 -982 O ATOM 5011 OD2 ASP B1066 -0.318 9.153 156.042 1.00100.79 O ANISOU 5011 OD2 ASP B1066 12955 9667 15672 -1504 3167 -933 O ATOM 5012 N ILE B1067 -2.395 4.845 153.783 1.00104.82 N ANISOU 5012 N ILE B1067 13109 10406 16311 -1000 2288 -592 N ATOM 5013 CA ILE B1067 -3.543 4.054 153.296 1.00105.65 C ANISOU 5013 CA ILE B1067 13092 10478 16568 -896 2189 -501 C ATOM 5014 C ILE B1067 -3.203 2.559 153.212 1.00106.19 C ANISOU 5014 C ILE B1067 13163 10670 16515 -869 1928 -546 C ATOM 5015 O ILE B1067 -4.031 1.718 153.554 1.00106.47 O ANISOU 5015 O ILE B1067 13179 10645 16630 -859 1890 -527 O ATOM 5016 CB ILE B1067 -4.077 4.575 151.928 1.00105.27 C ANISOU 5016 CB ILE B1067 12859 10458 16680 -772 2152 -353 C ATOM 5017 CG1 ILE B1067 -4.735 5.954 152.108 1.00106.25 C ANISOU 5017 CG1 ILE B1067 12936 10391 17043 -785 2438 -262 C ATOM 5018 CG2 ILE B1067 -5.090 3.601 151.311 1.00105.49 C ANISOU 5018 CG2 ILE B1067 12758 10517 16804 -688 1998 -270 C ATOM 5019 CD1 ILE B1067 -4.887 6.748 150.830 1.00106.70 C ANISOU 5019 CD1 ILE B1067 12805 10498 17238 -697 2410 -79 C ATOM 5020 N LEU B1068 -1.993 2.236 152.761 1.00107.90 N ANISOU 5020 N LEU B1068 13388 11040 16566 -858 1760 -606 N ATOM 5021 CA LEU B1068 -1.534 0.839 152.685 1.00109.42 C ANISOU 5021 CA LEU B1068 13560 11319 16694 -834 1537 -659 C ATOM 5022 C LEU B1068 -1.347 0.225 154.078 1.00110.71 C ANISOU 5022 C LEU B1068 13834 11430 16798 -951 1549 -678 C ATOM 5023 O LEU B1068 -2.027 -0.746 154.426 1.00111.47 O ANISOU 5023 O LEU B1068 13900 11469 16982 -942 1485 -652 O ATOM 5024 CB LEU B1068 -0.246 0.745 151.859 1.00109.77 C ANISOU 5024 CB LEU B1068 13571 11524 16610 -800 1389 -722 C ATOM 5025 CG LEU B1068 0.406 -0.634 151.682 1.00109.93 C ANISOU 5025 CG LEU B1068 13542 11612 16614 -772 1184 -793 C ATOM 5026 CD1 LEU B1068 0.832 -0.847 150.234 1.00110.00 C ANISOU 5026 CD1 LEU B1068 13424 11765 16603 -692 1058 -862 C ATOM 5027 CD2 LEU B1068 1.596 -0.819 152.618 1.00110.18 C ANISOU 5027 CD2 LEU B1068 13668 11665 16527 -865 1153 -811 C ATOM 5028 N VAL B1069 -0.463 0.816 154.882 1.00112.12 N ANISOU 5028 N VAL B1069 14132 11642 16823 -1079 1631 -709 N ATOM 5029 CA VAL B1069 -0.167 0.318 156.242 1.00113.90 C ANISOU 5029 CA VAL B1069 14455 11876 16945 -1241 1634 -699 C ATOM 5030 C VAL B1069 -1.445 0.246 157.102 1.00115.03 C ANISOU 5030 C VAL B1069 14632 11896 17178 -1312 1781 -671 C ATOM 5031 O VAL B1069 -1.597 -0.680 157.906 1.00116.82 O ANISOU 5031 O VAL B1069 14867 12129 17387 -1390 1704 -625 O ATOM 5032 CB VAL B1069 0.934 1.160 156.949 1.00115.24 C ANISOU 5032 CB VAL B1069 14747 12130 16906 -1409 1726 -738 C ATOM 5033 CG1 VAL B1069 1.085 0.777 158.425 1.00116.68 C ANISOU 5033 CG1 VAL B1069 15022 12356 16952 -1631 1751 -706 C ATOM 5034 CG2 VAL B1069 2.276 1.000 156.236 1.00114.33 C ANISOU 5034 CG2 VAL B1069 14593 12144 16702 -1348 1550 -749 C ATOM 5035 N GLY B1070 -2.351 1.212 156.919 1.00115.56 N ANISOU 5035 N GLY B1070 14697 11847 17363 -1286 1993 -684 N ATOM 5036 CA GLY B1070 -3.688 1.153 157.519 1.00116.04 C ANISOU 5036 CA GLY B1070 14757 11769 17561 -1319 2144 -660 C ATOM 5037 C GLY B1070 -4.476 -0.096 157.128 1.00115.60 C ANISOU 5037 C GLY B1070 14595 11687 17640 -1197 1964 -589 C ATOM 5038 O GLY B1070 -5.114 -0.730 157.977 1.00115.43 O ANISOU 5038 O GLY B1070 14595 11617 17643 -1272 1982 -561 O ATOM 5039 N GLN B1071 -4.427 -0.450 155.843 1.00115.28 N ANISOU 5039 N GLN B1071 14434 11691 17675 -1031 1796 -567 N ATOM 5040 CA GLN B1071 -5.084 -1.666 155.339 1.00115.43 C ANISOU 5040 CA GLN B1071 14341 11698 17817 -927 1621 -529 C ATOM 5041 C GLN B1071 -4.372 -2.949 155.792 1.00117.27 C ANISOU 5041 C GLN B1071 14576 11986 17992 -962 1428 -540 C ATOM 5042 O GLN B1071 -5.025 -3.977 156.014 1.00117.98 O ANISOU 5042 O GLN B1071 14612 12020 18194 -943 1344 -502 O ATOM 5043 CB GLN B1071 -5.212 -1.628 153.813 1.00114.02 C ANISOU 5043 CB GLN B1071 14026 11585 17708 -786 1515 -523 C ATOM 5044 CG GLN B1071 -6.250 -0.626 153.328 1.00113.67 C ANISOU 5044 CG GLN B1071 13917 11470 17802 -740 1671 -436 C ATOM 5045 CD GLN B1071 -6.124 -0.289 151.854 1.00113.15 C ANISOU 5045 CD GLN B1071 13718 11529 17743 -652 1575 -399 C ATOM 5046 OE1 GLN B1071 -5.379 -0.932 151.107 1.00112.99 O ANISOU 5046 OE1 GLN B1071 13652 11654 17624 -622 1392 -473 O ATOM 5047 NE2 GLN B1071 -6.873 0.720 151.422 1.00113.51 N ANISOU 5047 NE2 GLN B1071 13682 11523 17922 -622 1705 -275 N ATOM 5048 N ILE B1072 -3.045 -2.885 155.920 1.00118.42 N ANISOU 5048 N ILE B1072 14766 12232 17993 -1014 1359 -573 N ATOM 5049 CA ILE B1072 -2.261 -3.973 156.527 1.00118.95 C ANISOU 5049 CA ILE B1072 14820 12340 18033 -1073 1196 -538 C ATOM 5050 C ILE B1072 -2.632 -4.153 158.008 1.00120.65 C ANISOU 5050 C ILE B1072 15118 12529 18194 -1246 1269 -453 C ATOM 5051 O ILE B1072 -2.714 -5.285 158.486 1.00122.62 O ANISOU 5051 O ILE B1072 15307 12759 18522 -1269 1139 -370 O ATOM 5052 CB ILE B1072 -0.732 -3.765 156.350 1.00118.63 C ANISOU 5052 CB ILE B1072 14797 12417 17858 -1099 1116 -568 C ATOM 5053 CG1 ILE B1072 -0.357 -3.935 154.873 1.00117.81 C ANISOU 5053 CG1 ILE B1072 14583 12355 17823 -940 1012 -659 C ATOM 5054 CG2 ILE B1072 0.067 -4.749 157.204 1.00119.74 C ANISOU 5054 CG2 ILE B1072 14912 12592 17990 -1194 972 -474 C ATOM 5055 CD1 ILE B1072 1.065 -3.551 154.526 1.00117.60 C ANISOU 5055 CD1 ILE B1072 14568 12441 17671 -949 961 -704 C ATOM 5056 N ASP B1073 -2.855 -3.047 158.721 1.00121.62 N ANISOU 5056 N ASP B1073 15364 12654 18191 -1381 1486 -477 N ATOM 5057 CA ASP B1073 -3.366 -3.103 160.102 1.00123.34 C ANISOU 5057 CA ASP B1073 15661 12867 18334 -1580 1600 -428 C ATOM 5058 C ASP B1073 -4.816 -3.626 160.161 1.00124.25 C ANISOU 5058 C ASP B1073 15722 12853 18633 -1516 1638 -392 C ATOM 5059 O ASP B1073 -5.149 -4.427 161.043 1.00124.41 O ANISOU 5059 O ASP B1073 15736 12881 18652 -1620 1587 -305 O ATOM 5060 CB ASP B1073 -3.268 -1.734 160.788 1.00124.29 C ANISOU 5060 CB ASP B1073 15921 13012 18290 -1760 1867 -516 C ATOM 5061 CG ASP B1073 -1.825 -1.307 161.065 1.00124.44 C ANISOU 5061 CG ASP B1073 16009 13187 18084 -1891 1829 -533 C ATOM 5062 OD1 ASP B1073 -1.006 -2.145 161.510 1.00124.57 O ANISOU 5062 OD1 ASP B1073 15997 13323 18009 -1973 1633 -428 O ATOM 5063 OD2 ASP B1073 -1.510 -0.116 160.848 1.00124.06 O ANISOU 5063 OD2 ASP B1073 16031 13136 17971 -1917 1998 -637 O ATOM 5064 N ASP B1074 -5.662 -3.174 159.231 1.00124.53 N ANISOU 5064 N ASP B1074 15706 12782 18827 -1356 1719 -435 N ATOM 5065 CA ASP B1074 -7.038 -3.700 159.100 1.00125.69 C ANISOU 5065 CA ASP B1074 15778 12809 19169 -1272 1732 -389 C ATOM 5066 C ASP B1074 -7.080 -5.194 158.751 1.00128.28 C ANISOU 5066 C ASP B1074 15992 13137 19609 -1177 1478 -330 C ATOM 5067 O ASP B1074 -8.000 -5.900 159.170 1.00129.11 O ANISOU 5067 O ASP B1074 16061 13171 19824 -1185 1463 -268 O ATOM 5068 CB ASP B1074 -7.849 -2.916 158.055 1.00124.35 C ANISOU 5068 CB ASP B1074 15541 12550 19153 -1126 1840 -405 C ATOM 5069 CG ASP B1074 -8.355 -1.582 158.573 1.00124.25 C ANISOU 5069 CG ASP B1074 15601 12446 19162 -1213 2149 -439 C ATOM 5070 OD1 ASP B1074 -7.734 -1.005 159.486 1.00124.59 O ANISOU 5070 OD1 ASP B1074 15765 12530 19041 -1387 2286 -506 O ATOM 5071 OD2 ASP B1074 -9.386 -1.106 158.056 1.00124.18 O ANISOU 5071 OD2 ASP B1074 15511 12320 19349 -1119 2264 -397 O ATOM 5072 N ALA B1075 -6.103 -5.664 157.974 1.00130.92 N ANISOU 5072 N ALA B1075 16263 13541 19939 -1092 1296 -359 N ATOM 5073 CA ALA B1075 -5.934 -7.100 157.718 1.00132.72 C ANISOU 5073 CA ALA B1075 16371 13751 20303 -1024 1078 -328 C ATOM 5074 C ALA B1075 -5.442 -7.812 158.981 1.00134.22 C ANISOU 5074 C ALA B1075 16579 13967 20449 -1172 1004 -209 C ATOM 5075 O ALA B1075 -6.085 -8.749 159.464 1.00133.71 O ANISOU 5075 O ALA B1075 16455 13836 20513 -1189 939 -120 O ATOM 5076 CB ALA B1075 -4.967 -7.331 156.565 1.00133.18 C ANISOU 5076 CB ALA B1075 16348 13870 20382 -914 945 -419 C ATOM 5077 N LEU B1076 -4.319 -7.333 159.521 1.00136.27 N ANISOU 5077 N LEU B1076 16913 14339 20525 -1295 1011 -187 N ATOM 5078 CA LEU B1076 -3.709 -7.868 160.756 1.00139.19 C ANISOU 5078 CA LEU B1076 17289 14787 20808 -1482 932 -34 C ATOM 5079 C LEU B1076 -4.734 -8.025 161.889 1.00141.40 C ANISOU 5079 C LEU B1076 17614 15053 21058 -1633 1022 57 C ATOM 5080 O LEU B1076 -4.771 -9.066 162.556 1.00142.27 O ANISOU 5080 O LEU B1076 17640 15167 21246 -1704 888 219 O ATOM 5081 CB LEU B1076 -2.550 -6.969 161.214 1.00139.61 C ANISOU 5081 CB LEU B1076 17446 14993 20607 -1635 984 -39 C ATOM 5082 CG LEU B1076 -1.646 -7.448 162.357 1.00141.33 C ANISOU 5082 CG LEU B1076 17647 15349 20701 -1852 869 146 C ATOM 5083 CD1 LEU B1076 -0.805 -8.636 161.918 1.00141.73 C ANISOU 5083 CD1 LEU B1076 17520 15366 20966 -1739 625 258 C ATOM 5084 CD2 LEU B1076 -0.752 -6.312 162.833 1.00141.46 C ANISOU 5084 CD2 LEU B1076 17797 15529 20422 -2037 977 106 C ATOM 5085 N LYS B1077 -5.575 -7.001 162.064 1.00142.64 N ANISOU 5085 N LYS B1077 17883 15183 21131 -1678 1255 -39 N ATOM 5086 CA LYS B1077 -6.715 -7.032 163.002 1.00144.46 C ANISOU 5086 CA LYS B1077 18154 15379 21353 -1806 1390 2 C ATOM 5087 C LYS B1077 -7.531 -8.336 162.951 1.00145.79 C ANISOU 5087 C LYS B1077 18197 15448 21749 -1711 1242 111 C ATOM 5088 O LYS B1077 -8.004 -8.802 163.989 1.00146.98 O ANISOU 5088 O LYS B1077 18349 15629 21865 -1869 1249 226 O ATOM 5089 CB LYS B1077 -7.635 -5.827 162.750 1.00144.12 C ANISOU 5089 CB LYS B1077 18193 15243 21323 -1774 1666 -139 C ATOM 5090 CG LYS B1077 -8.812 -5.681 163.708 1.00144.78 C ANISOU 5090 CG LYS B1077 18324 15278 21407 -1915 1861 -133 C ATOM 5091 CD LYS B1077 -9.494 -4.331 163.538 1.00144.30 C ANISOU 5091 CD LYS B1077 18331 15112 21384 -1907 2171 -275 C ATOM 5092 CE LYS B1077 -10.858 -4.291 164.211 1.00144.67 C ANISOU 5092 CE LYS B1077 18383 15056 21527 -1981 2369 -279 C ATOM 5093 NZ LYS B1077 -10.782 -4.517 165.681 1.00145.84 N ANISOU 5093 NZ LYS B1077 18610 15341 21459 -2287 2440 -256 N ATOM 5094 N LEU B1078 -7.691 -8.911 161.755 1.00146.53 N ANISOU 5094 N LEU B1078 18177 15434 22060 -1478 1115 69 N ATOM 5095 CA LEU B1078 -8.358 -10.211 161.599 1.00148.05 C ANISOU 5095 CA LEU B1078 18236 15522 22492 -1385 967 151 C ATOM 5096 C LEU B1078 -7.485 -11.361 162.116 1.00150.79 C ANISOU 5096 C LEU B1078 18478 15905 22911 -1448 755 311 C ATOM 5097 O LEU B1078 -7.974 -12.236 162.844 1.00151.78 O ANISOU 5097 O LEU B1078 18535 15997 23135 -1519 683 463 O ATOM 5098 CB LEU B1078 -8.725 -10.477 160.135 1.00146.35 C ANISOU 5098 CB LEU B1078 17925 15209 22470 -1155 906 32 C ATOM 5099 CG LEU B1078 -9.626 -9.453 159.437 1.00144.88 C ANISOU 5099 CG LEU B1078 17786 14988 22273 -1073 1076 -70 C ATOM 5100 CD1 LEU B1078 -9.528 -9.585 157.922 1.00144.39 C ANISOU 5100 CD1 LEU B1078 17626 14920 22315 -900 986 -179 C ATOM 5101 CD2 LEU B1078 -11.062 -9.603 159.904 1.00144.71 C ANISOU 5101 CD2 LEU B1078 17759 14872 22350 -1091 1171 -10 C ATOM 5102 N ALA B1079 -6.198 -11.340 161.753 1.00152.44 N ANISOU 5102 N ALA B1079 18657 16175 23088 -1427 659 298 N ATOM 5103 CA ALA B1079 -5.256 -12.432 162.076 1.00153.13 C ANISOU 5103 CA ALA B1079 18600 16267 23314 -1460 455 466 C ATOM 5104 C ALA B1079 -5.129 -12.752 163.573 1.00153.76 C ANISOU 5104 C ALA B1079 18677 16460 23283 -1707 407 721 C ATOM 5105 O ALA B1079 -4.805 -13.884 163.937 1.00154.02 O ANISOU 5105 O ALA B1079 18545 16455 23518 -1729 232 924 O ATOM 5106 CB ALA B1079 -3.881 -12.136 161.488 1.00153.53 C ANISOU 5106 CB ALA B1079 18634 16377 23321 -1413 396 405 C ATOM 5107 N ASN B1080 -5.371 -11.754 164.425 1.00153.63 N ANISOU 5107 N ASN B1080 18825 16588 22957 -1910 571 711 N ATOM 5108 CA ASN B1080 -5.440 -11.956 165.875 1.00155.29 C ANISOU 5108 CA ASN B1080 19048 16953 23002 -2197 559 928 C ATOM 5109 C ASN B1080 -6.637 -12.824 166.273 1.00155.97 C ANISOU 5109 C ASN B1080 19057 16942 23260 -2192 532 1034 C ATOM 5110 O ASN B1080 -6.515 -13.664 167.168 1.00158.22 O ANISOU 5110 O ASN B1080 19234 17302 23580 -2350 393 1296 O ATOM 5111 CB ASN B1080 -5.498 -10.612 166.613 1.00155.44 C ANISOU 5111 CB ASN B1080 19268 17143 22646 -2432 793 820 C ATOM 5112 CG ASN B1080 -4.216 -9.809 166.469 1.00154.84 C ANISOU 5112 CG ASN B1080 19261 17198 22369 -2498 804 762 C ATOM 5113 OD1 ASN B1080 -3.471 -9.964 165.499 1.00152.89 O ANISOU 5113 OD1 ASN B1080 18947 16877 22265 -2298 693 716 O ATOM 5114 ND2 ASN B1080 -3.955 -8.941 167.439 1.00156.05 N ANISOU 5114 ND2 ASN B1080 19549 17557 22186 -2795 949 747 N ATOM 5115 N GLU B1081 -7.780 -12.620 165.613 1.00154.21 N ANISOU 5115 N GLU B1081 18876 16564 23150 -2023 656 857 N ATOM 5116 CA GLU B1081 -8.957 -13.472 165.824 1.00154.65 C ANISOU 5116 CA GLU B1081 18851 16504 23402 -1984 626 940 C ATOM 5117 C GLU B1081 -8.785 -14.831 165.148 1.00154.76 C ANISOU 5117 C GLU B1081 18660 16355 23784 -1794 403 1025 C ATOM 5118 O GLU B1081 -9.004 -15.871 165.775 1.00156.22 O ANISOU 5118 O GLU B1081 18715 16512 24129 -1859 273 1242 O ATOM 5119 CB GLU B1081 -10.235 -12.794 165.315 1.00153.56 C ANISOU 5119 CB GLU B1081 18808 16256 23282 -1871 830 741 C ATOM 5120 CG GLU B1081 -10.615 -11.534 166.082 1.00154.39 C ANISOU 5120 CG GLU B1081 19088 16469 23101 -2067 1096 650 C ATOM 5121 CD GLU B1081 -12.106 -11.224 166.029 1.00154.63 C ANISOU 5121 CD GLU B1081 19155 16377 23219 -2013 1283 562 C ATOM 5122 OE1 GLU B1081 -12.763 -11.557 165.020 1.00153.70 O ANISOU 5122 OE1 GLU B1081 18962 16098 23339 -1778 1238 507 O ATOM 5123 OE2 GLU B1081 -12.619 -10.646 167.008 1.00156.01 O ANISOU 5123 OE2 GLU B1081 19426 16626 23223 -2224 1484 545 O ATOM 5124 N GLY B1082 -8.401 -14.805 163.872 1.00153.49 N ANISOU 5124 N GLY B1082 18463 16090 23767 -1575 374 846 N ATOM 5125 CA GLY B1082 -8.156 -16.019 163.088 1.00153.15 C ANISOU 5125 CA GLY B1082 18223 15880 24087 -1401 206 853 C ATOM 5126 C GLY B1082 -9.268 -16.282 162.092 1.00151.97 C ANISOU 5126 C GLY B1082 18045 15575 24120 -1217 250 672 C ATOM 5127 O GLY B1082 -10.009 -17.258 162.217 1.00152.32 O ANISOU 5127 O GLY B1082 17977 15498 24398 -1186 183 751 O ATOM 5128 N LYS B1083 -9.376 -15.393 161.106 1.00150.49 N ANISOU 5128 N LYS B1083 17948 15407 23821 -1112 358 447 N ATOM 5129 CA LYS B1083 -10.300 -15.554 159.980 1.00149.41 C ANISOU 5129 CA LYS B1083 17769 15170 23827 -954 386 276 C ATOM 5130 C LYS B1083 -9.580 -15.207 158.675 1.00149.37 C ANISOU 5130 C LYS B1083 17746 15195 23812 -838 379 69 C ATOM 5131 O LYS B1083 -9.276 -14.039 158.411 1.00147.93 O ANISOU 5131 O LYS B1083 17682 15122 23403 -846 479 -7 O ATOM 5132 CB LYS B1083 -11.535 -14.668 160.167 1.00148.04 C ANISOU 5132 CB LYS B1083 17717 15019 23509 -978 553 257 C ATOM 5133 CG LYS B1083 -12.663 -14.979 159.194 1.00147.26 C ANISOU 5133 CG LYS B1083 17547 14830 23574 -850 558 155 C ATOM 5134 CD LYS B1083 -13.777 -13.949 159.258 1.00146.31 C ANISOU 5134 CD LYS B1083 17526 14727 23338 -860 735 150 C ATOM 5135 CE LYS B1083 -14.860 -14.263 158.239 1.00145.98 C ANISOU 5135 CE LYS B1083 17391 14621 23453 -747 717 83 C ATOM 5136 NZ LYS B1083 -15.977 -13.283 158.282 1.00145.89 N ANISOU 5136 NZ LYS B1083 17438 14605 23385 -748 889 118 N ATOM 5137 N VAL B1084 -9.318 -16.233 157.862 1.00150.96 N ANISOU 5137 N VAL B1084 17789 15297 24270 -743 273 -28 N ATOM 5138 CA VAL B1084 -8.600 -16.078 156.591 1.00151.33 C ANISOU 5138 CA VAL B1084 17793 15383 24322 -656 265 -245 C ATOM 5139 C VAL B1084 -9.517 -15.474 155.522 1.00151.24 C ANISOU 5139 C VAL B1084 17817 15435 24214 -598 342 -403 C ATOM 5140 O VAL B1084 -9.130 -14.518 154.843 1.00152.05 O ANISOU 5140 O VAL B1084 17983 15661 24126 -581 397 -502 O ATOM 5141 CB VAL B1084 -8.018 -17.426 156.089 1.00151.98 C ANISOU 5141 CB VAL B1084 17674 15327 24743 -599 159 -328 C ATOM 5142 CG1 VAL B1084 -7.323 -17.259 154.737 1.00151.55 C ANISOU 5142 CG1 VAL B1084 17573 15331 24674 -536 175 -591 C ATOM 5143 CG2 VAL B1084 -7.055 -18.008 157.120 1.00152.97 C ANISOU 5143 CG2 VAL B1084 17726 15389 25007 -658 70 -116 C ATOM 5144 N LYS B1085 -10.730 -16.028 155.398 1.00151.59 N ANISOU 5144 N LYS B1085 17804 15401 24392 -578 337 -398 N ATOM 5145 CA LYS B1085 -11.709 -15.607 154.383 1.00151.25 C ANISOU 5145 CA LYS B1085 17755 15425 24289 -541 386 -505 C ATOM 5146 C LYS B1085 -11.762 -14.093 154.219 1.00151.62 C ANISOU 5146 C LYS B1085 17928 15607 24072 -549 498 -478 C ATOM 5147 O LYS B1085 -11.520 -13.574 153.124 1.00152.68 O ANISOU 5147 O LYS B1085 18040 15861 24107 -524 505 -598 O ATOM 5148 CB LYS B1085 -13.118 -16.132 154.722 1.00150.81 C ANISOU 5148 CB LYS B1085 17661 15273 24363 -545 389 -414 C ATOM 5149 CG LYS B1085 -13.300 -17.650 154.659 1.00151.36 C ANISOU 5149 CG LYS B1085 17580 15196 24734 -532 288 -460 C ATOM 5150 CD LYS B1085 -13.002 -18.215 153.280 1.00151.68 C ANISOU 5150 CD LYS B1085 17493 15265 24873 -507 246 -716 C ATOM 5151 CE LYS B1085 -13.574 -19.613 153.105 1.00153.22 C ANISOU 5151 CE LYS B1085 17534 15305 25377 -507 187 -788 C ATOM 5152 NZ LYS B1085 -13.372 -20.110 151.717 1.00154.08 N ANISOU 5152 NZ LYS B1085 17521 15465 25556 -524 180 -1083 N ATOM 5153 N GLU B1086 -12.037 -13.399 155.322 1.00152.51 N ANISOU 5153 N GLU B1086 18161 15702 24082 -600 594 -324 N ATOM 5154 CA GLU B1086 -12.135 -11.932 155.325 1.00152.40 C ANISOU 5154 CA GLU B1086 18260 15772 23873 -615 739 -293 C ATOM 5155 C GLU B1086 -10.824 -11.251 154.911 1.00151.80 C ANISOU 5155 C GLU B1086 18231 15806 23640 -615 739 -377 C ATOM 5156 O GLU B1086 -10.853 -10.249 154.189 1.00152.07 O ANISOU 5156 O GLU B1086 18283 15927 23566 -590 809 -410 O ATOM 5157 CB GLU B1086 -12.598 -11.416 156.700 1.00152.60 C ANISOU 5157 CB GLU B1086 18401 15743 23835 -703 872 -154 C ATOM 5158 CG GLU B1086 -12.857 -9.910 156.788 1.00151.97 C ANISOU 5158 CG GLU B1086 18421 15699 23622 -727 1069 -136 C ATOM 5159 CD GLU B1086 -13.825 -9.391 155.737 1.00150.96 C ANISOU 5159 CD GLU B1086 18215 15574 23569 -643 1116 -132 C ATOM 5160 OE1 GLU B1086 -14.894 -10.009 155.543 1.00151.22 O ANISOU 5160 OE1 GLU B1086 18162 15548 23745 -611 1078 -86 O ATOM 5161 OE2 GLU B1086 -13.515 -8.358 155.106 1.00147.73 O ANISOU 5161 OE2 GLU B1086 17816 15234 23078 -619 1186 -153 O ATOM 5162 N ALA B1087 -9.686 -11.814 155.328 1.00151.08 N ANISOU 5162 N ALA B1087 18136 15709 23556 -643 654 -391 N ATOM 5163 CA ALA B1087 -8.363 -11.261 154.976 1.00150.26 C ANISOU 5163 CA ALA B1087 18068 15707 23316 -645 644 -466 C ATOM 5164 C ALA B1087 -8.121 -11.149 153.459 1.00150.29 C ANISOU 5164 C ALA B1087 17989 15805 23307 -572 605 -632 C ATOM 5165 O ALA B1087 -7.335 -10.301 153.020 1.00151.17 O ANISOU 5165 O ALA B1087 18146 16026 23263 -571 636 -683 O ATOM 5166 CB ALA B1087 -7.246 -12.063 155.635 1.00150.42 C ANISOU 5166 CB ALA B1087 18056 15693 23404 -685 540 -423 C ATOM 5167 N GLN B1088 -8.796 -11.989 152.669 1.00151.35 N ANISOU 5167 N GLN B1088 18000 15915 23590 -534 540 -719 N ATOM 5168 CA GLN B1088 -8.760 -11.875 151.202 1.00152.10 C ANISOU 5168 CA GLN B1088 18006 16144 23637 -512 512 -878 C ATOM 5169 C GLN B1088 -9.434 -10.590 150.686 1.00151.75 C ANISOU 5169 C GLN B1088 18000 16222 23435 -515 596 -801 C ATOM 5170 O GLN B1088 -9.053 -10.079 149.628 1.00152.60 O ANISOU 5170 O GLN B1088 18064 16492 23423 -521 583 -881 O ATOM 5171 CB GLN B1088 -9.392 -13.109 150.540 1.00153.63 C ANISOU 5171 CB GLN B1088 18054 16297 24019 -511 436 -1000 C ATOM 5172 CG GLN B1088 -8.619 -14.402 150.780 1.00154.97 C ANISOU 5172 CG GLN B1088 18136 16332 24411 -502 366 -1103 C ATOM 5173 CD GLN B1088 -9.436 -15.654 150.514 1.00156.14 C ANISOU 5173 CD GLN B1088 18153 16371 24799 -507 320 -1187 C ATOM 5174 OE1 GLN B1088 -10.396 -15.637 149.744 1.00156.92 O ANISOU 5174 OE1 GLN B1088 18204 16555 24861 -534 324 -1245 O ATOM 5175 NE2 GLN B1088 -9.050 -16.754 151.151 1.00156.78 N ANISOU 5175 NE2 GLN B1088 18160 16264 25143 -492 275 -1177 N ATOM 5176 N ALA B1089 -10.422 -10.074 151.425 1.00151.22 N ANISOU 5176 N ALA B1089 17994 16075 23387 -517 687 -636 N ATOM 5177 CA ALA B1089 -11.055 -8.786 151.092 1.00150.42 C ANISOU 5177 CA ALA B1089 17909 16039 23205 -513 795 -524 C ATOM 5178 C ALA B1089 -10.079 -7.611 151.233 1.00149.61 C ANISOU 5178 C ALA B1089 17903 15994 22946 -523 879 -513 C ATOM 5179 O ALA B1089 -10.125 -6.675 150.440 1.00149.67 O ANISOU 5179 O ALA B1089 17873 16111 22884 -515 917 -474 O ATOM 5180 CB ALA B1089 -12.295 -8.550 151.947 1.00150.33 C ANISOU 5180 CB ALA B1089 17929 15890 23297 -516 904 -367 C ATOM 5181 N ALA B1090 -9.210 -7.668 152.244 1.00148.77 N ANISOU 5181 N ALA B1090 17909 15824 22791 -553 903 -530 N ATOM 5182 CA ALA B1090 -8.145 -6.674 152.427 1.00148.00 C ANISOU 5182 CA ALA B1090 17908 15788 22537 -580 972 -542 C ATOM 5183 C ALA B1090 -7.068 -6.785 151.341 1.00147.76 C ANISOU 5183 C ALA B1090 17816 15904 22420 -554 863 -670 C ATOM 5184 O ALA B1090 -6.583 -5.765 150.841 1.00148.17 O ANISOU 5184 O ALA B1090 17888 16056 22353 -554 913 -668 O ATOM 5185 CB ALA B1090 -7.521 -6.812 153.809 1.00147.67 C ANISOU 5185 CB ALA B1090 17986 15675 22447 -654 1008 -513 C ATOM 5186 N ALA B1091 -6.704 -8.019 150.984 1.00147.29 N ANISOU 5186 N ALA B1091 17671 15847 22442 -540 730 -787 N ATOM 5187 CA ALA B1091 -5.712 -8.289 149.929 1.00147.59 C ANISOU 5187 CA ALA B1091 17633 16016 22429 -529 645 -949 C ATOM 5188 C ALA B1091 -6.073 -7.655 148.577 1.00148.34 C ANISOU 5188 C ALA B1091 17644 16294 22422 -535 643 -980 C ATOM 5189 O ALA B1091 -5.204 -7.095 147.898 1.00149.50 O ANISOU 5189 O ALA B1091 17784 16585 22433 -546 634 -1044 O ATOM 5190 CB ALA B1091 -5.510 -9.789 149.768 1.00148.68 C ANISOU 5190 CB ALA B1091 17663 16083 22744 -520 541 -1082 C ATOM 5191 N GLU B1092 -7.348 -7.746 148.198 1.00149.73 N ANISOU 5191 N GLU B1092 17747 16481 22661 -541 643 -913 N ATOM 5192 CA GLU B1092 -7.853 -7.088 146.979 1.00151.05 C ANISOU 5192 CA GLU B1092 17810 16846 22733 -574 631 -870 C ATOM 5193 C GLU B1092 -7.744 -5.560 147.038 1.00150.08 C ANISOU 5193 C GLU B1092 17742 16763 22519 -562 732 -703 C ATOM 5194 O GLU B1092 -7.453 -4.921 146.025 1.00150.12 O ANISOU 5194 O GLU B1092 17671 16964 22402 -595 705 -688 O ATOM 5195 CB GLU B1092 -9.310 -7.476 146.707 1.00153.14 C ANISOU 5195 CB GLU B1092 17977 17104 23104 -592 609 -783 C ATOM 5196 CG GLU B1092 -9.507 -8.928 146.300 1.00155.06 C ANISOU 5196 CG GLU B1092 18128 17353 23434 -629 510 -969 C ATOM 5197 CD GLU B1092 -10.967 -9.282 146.081 1.00156.94 C ANISOU 5197 CD GLU B1092 18273 17589 23767 -658 488 -872 C ATOM 5198 OE1 GLU B1092 -11.680 -8.504 145.411 1.00158.28 O ANISOU 5198 OE1 GLU B1092 18362 17907 23870 -697 490 -713 O ATOM 5199 OE2 GLU B1092 -11.402 -10.346 146.573 1.00158.22 O ANISOU 5199 OE2 GLU B1092 18427 17603 24085 -645 462 -933 O ATOM 5200 N GLN B1093 -7.987 -4.987 148.217 1.00149.12 N ANISOU 5200 N GLN B1093 17737 16459 22462 -533 857 -583 N ATOM 5201 CA GLN B1093 -7.874 -3.536 148.435 1.00148.20 C ANISOU 5201 CA GLN B1093 17675 16325 22309 -528 996 -449 C ATOM 5202 C GLN B1093 -6.408 -3.077 148.440 1.00146.01 C ANISOU 5202 C GLN B1093 17480 16119 21876 -539 996 -544 C ATOM 5203 O GLN B1093 -6.085 -2.017 147.888 1.00146.73 O ANISOU 5203 O GLN B1093 17546 16305 21897 -543 1041 -476 O ATOM 5204 CB GLN B1093 -8.557 -3.118 149.750 1.00148.00 C ANISOU 5204 CB GLN B1093 17752 16078 22403 -525 1165 -345 C ATOM 5205 CG GLN B1093 -10.054 -3.418 149.831 1.00147.93 C ANISOU 5205 CG GLN B1093 17661 15977 22568 -509 1193 -226 C ATOM 5206 CD GLN B1093 -10.932 -2.380 149.152 1.00148.39 C ANISOU 5206 CD GLN B1093 17591 16059 22729 -493 1273 -27 C ATOM 5207 OE1 GLN B1093 -10.520 -1.717 148.199 1.00149.03 O ANISOU 5207 OE1 GLN B1093 17591 16296 22738 -499 1235 24 O ATOM 5208 NE2 GLN B1093 -12.159 -2.246 149.638 1.00148.41 N ANISOU 5208 NE2 GLN B1093 17557 15909 22920 -478 1382 107 N ATOM 5209 N LEU B1094 -5.534 -3.876 149.059 1.00142.68 N ANISOU 5209 N LEU B1094 17139 15651 21421 -546 941 -677 N ATOM 5210 CA LEU B1094 -4.084 -3.611 149.051 1.00140.03 C ANISOU 5210 CA LEU B1094 16865 15390 20947 -560 919 -768 C ATOM 5211 C LEU B1094 -3.492 -3.549 147.636 1.00138.82 C ANISOU 5211 C LEU B1094 16602 15452 20689 -561 825 -859 C ATOM 5212 O LEU B1094 -2.622 -2.715 147.366 1.00139.28 O ANISOU 5212 O LEU B1094 16692 15602 20624 -570 851 -860 O ATOM 5213 CB LEU B1094 -3.329 -4.655 149.890 1.00139.34 C ANISOU 5213 CB LEU B1094 16834 15218 20890 -573 853 -856 C ATOM 5214 CG LEU B1094 -3.512 -4.589 151.408 1.00139.14 C ANISOU 5214 CG LEU B1094 16933 15040 20891 -621 940 -764 C ATOM 5215 CD1 LEU B1094 -3.020 -5.870 152.065 1.00139.32 C ANISOU 5215 CD1 LEU B1094 16944 14996 20995 -637 831 -797 C ATOM 5216 CD2 LEU B1094 -2.798 -3.387 151.986 1.00139.17 C ANISOU 5216 CD2 LEU B1094 17063 15062 20752 -679 1060 -726 C ATOM 5217 N LYS B1095 -3.962 -4.426 146.747 1.00137.14 N ANISOU 5217 N LYS B1095 16260 15331 20515 -571 725 -944 N ATOM 5218 CA LYS B1095 -3.578 -4.379 145.324 1.00135.47 C ANISOU 5218 CA LYS B1095 15926 15367 20179 -615 647 -1039 C ATOM 5219 C LYS B1095 -4.069 -3.103 144.619 1.00133.54 C ANISOU 5219 C LYS B1095 15618 15268 19852 -641 684 -850 C ATOM 5220 O LYS B1095 -3.363 -2.556 143.761 1.00132.87 O ANISOU 5220 O LYS B1095 15482 15382 19618 -680 653 -872 O ATOM 5221 CB LYS B1095 -4.078 -5.622 144.580 1.00136.54 C ANISOU 5221 CB LYS B1095 15932 15575 20370 -660 555 -1193 C ATOM 5222 CG LYS B1095 -3.345 -6.894 144.979 1.00137.15 C ANISOU 5222 CG LYS B1095 16019 15529 20561 -641 517 -1402 C ATOM 5223 CD LYS B1095 -3.938 -8.127 144.321 1.00138.60 C ANISOU 5223 CD LYS B1095 16071 15742 20846 -693 459 -1571 C ATOM 5224 CE LYS B1095 -3.264 -9.387 144.837 1.00138.90 C ANISOU 5224 CE LYS B1095 16097 15596 21083 -660 443 -1745 C ATOM 5225 NZ LYS B1095 -3.814 -10.618 144.209 1.00140.39 N ANISOU 5225 NZ LYS B1095 16148 15783 21408 -718 412 -1942 N ATOM 5226 N THR B1096 -5.270 -2.644 144.982 1.00131.33 N ANISOU 5226 N THR B1096 15322 14883 19691 -621 753 -651 N ATOM 5227 CA THR B1096 -5.806 -1.366 144.493 1.00130.02 C ANISOU 5227 CA THR B1096 15075 14793 19533 -632 811 -413 C ATOM 5228 C THR B1096 -4.969 -0.193 145.006 1.00127.74 C ANISOU 5228 C THR B1096 14892 14430 19212 -603 929 -358 C ATOM 5229 O THR B1096 -4.622 0.700 144.231 1.00128.21 O ANISOU 5229 O THR B1096 14874 14643 19195 -628 924 -259 O ATOM 5230 CB THR B1096 -7.282 -1.146 144.910 1.00130.04 C ANISOU 5230 CB THR B1096 15028 14645 19735 -607 889 -206 C ATOM 5231 OG1 THR B1096 -8.033 -2.346 144.700 1.00130.53 O ANISOU 5231 OG1 THR B1096 15025 14731 19838 -632 790 -280 O ATOM 5232 CG2 THR B1096 -7.918 -0.007 144.109 1.00130.47 C ANISOU 5232 CG2 THR B1096 14920 14811 19842 -632 915 69 C ATOM 5233 N THR B1097 -4.652 -0.206 146.303 1.00124.59 N ANISOU 5233 N THR B1097 14660 13812 18864 -570 1032 -416 N ATOM 5234 CA THR B1097 -3.772 0.805 146.916 1.00122.40 C ANISOU 5234 CA THR B1097 14504 13464 18537 -570 1153 -407 C ATOM 5235 C THR B1097 -2.382 0.823 146.270 1.00121.79 C ANISOU 5235 C THR B1097 14433 13572 18269 -589 1057 -532 C ATOM 5236 O THR B1097 -1.854 1.899 145.965 1.00121.40 O ANISOU 5236 O THR B1097 14379 13583 18162 -598 1112 -460 O ATOM 5237 CB THR B1097 -3.634 0.571 148.440 1.00120.61 C ANISOU 5237 CB THR B1097 14452 13025 18350 -581 1258 -474 C ATOM 5238 OG1 THR B1097 -4.917 0.721 149.060 1.00120.32 O ANISOU 5238 OG1 THR B1097 14409 12814 18490 -574 1382 -361 O ATOM 5239 CG2 THR B1097 -2.650 1.532 149.086 1.00119.98 C ANISOU 5239 CG2 THR B1097 14501 12903 18184 -619 1378 -496 C ATOM 5240 N ARG B1098 -1.811 -0.368 146.070 1.00121.65 N ANISOU 5240 N ARG B1098 14411 13626 18182 -594 927 -715 N ATOM 5241 CA ARG B1098 -0.502 -0.536 145.427 1.00121.20 C ANISOU 5241 CA ARG B1098 14341 13736 17971 -613 840 -862 C ATOM 5242 C ARG B1098 -0.456 0.147 144.060 1.00120.84 C ANISOU 5242 C ARG B1098 14160 13939 17813 -652 794 -801 C ATOM 5243 O ARG B1098 0.397 1.017 143.812 1.00121.16 O ANISOU 5243 O ARG B1098 14220 14065 17747 -662 819 -773 O ATOM 5244 CB ARG B1098 -0.176 -2.030 145.287 1.00122.28 C ANISOU 5244 CB ARG B1098 14441 13884 18135 -615 729 -1066 C ATOM 5245 CG ARG B1098 1.174 -2.335 144.657 1.00123.81 C ANISOU 5245 CG ARG B1098 14604 14221 18217 -634 661 -1243 C ATOM 5246 CD ARG B1098 1.548 -3.803 144.793 1.00124.83 C ANISOU 5246 CD ARG B1098 14694 14274 18461 -625 595 -1437 C ATOM 5247 NE ARG B1098 0.575 -4.686 144.146 1.00126.12 N ANISOU 5247 NE ARG B1098 14736 14476 18705 -653 550 -1520 N ATOM 5248 CZ ARG B1098 0.482 -4.918 142.832 1.00127.33 C ANISOU 5248 CZ ARG B1098 14754 14855 18768 -729 505 -1650 C ATOM 5249 NH1 ARG B1098 1.303 -4.326 141.956 1.00127.30 N ANISOU 5249 NH1 ARG B1098 14709 15072 18585 -781 494 -1708 N ATOM 5250 NH2 ARG B1098 -0.461 -5.749 142.389 1.00129.14 N ANISOU 5250 NH2 ARG B1098 14885 15110 19073 -776 471 -1725 N ATOM 5251 N ASN B1099 -1.395 -0.244 143.197 1.00120.63 N ANISOU 5251 N ASN B1099 13988 14042 17804 -691 724 -763 N ATOM 5252 CA ASN B1099 -1.497 0.305 141.840 1.00121.69 C ANISOU 5252 CA ASN B1099 13959 14464 17814 -770 658 -671 C ATOM 5253 C ASN B1099 -1.933 1.772 141.819 1.00121.17 C ANISOU 5253 C ASN B1099 13849 14376 17812 -756 744 -373 C ATOM 5254 O ASN B1099 -1.565 2.507 140.901 1.00120.95 O ANISOU 5254 O ASN B1099 13716 14567 17671 -812 704 -272 O ATOM 5255 CB ASN B1099 -2.460 -0.529 140.987 1.00123.48 C ANISOU 5255 CB ASN B1099 14031 14853 18031 -851 558 -694 C ATOM 5256 CG ASN B1099 -1.973 -1.954 140.774 1.00124.37 C ANISOU 5256 CG ASN B1099 14145 15007 18101 -888 490 -1015 C ATOM 5257 OD1 ASN B1099 -1.246 -2.509 141.600 1.00123.33 O ANISOU 5257 OD1 ASN B1099 14134 14685 18037 -817 520 -1172 O ATOM 5258 ND2 ASN B1099 -2.386 -2.559 139.669 1.00126.34 N ANISOU 5258 ND2 ASN B1099 14242 15504 18254 -1015 404 -1107 N ATOM 5259 N ALA B1100 -2.716 2.186 142.816 1.00120.73 N ANISOU 5259 N ALA B1100 13859 14053 17958 -690 872 -234 N ATOM 5260 CA ALA B1100 -3.141 3.587 142.948 1.00121.07 C ANISOU 5260 CA ALA B1100 13855 14000 18144 -667 1003 32 C ATOM 5261 C ALA B1100 -1.981 4.501 143.329 1.00120.21 C ANISOU 5261 C ALA B1100 13858 13838 17977 -651 1096 -2 C ATOM 5262 O ALA B1100 -1.726 5.490 142.638 1.00120.73 O ANISOU 5262 O ALA B1100 13821 14022 18029 -674 1103 157 O ATOM 5263 CB ALA B1100 -4.266 3.728 143.971 1.00121.08 C ANISOU 5263 CB ALA B1100 13897 13708 18397 -614 1152 141 C ATOM 5264 N TYR B1101 -1.286 4.165 144.419 1.00119.43 N ANISOU 5264 N TYR B1101 13957 13577 17844 -626 1159 -192 N ATOM 5265 CA TYR B1101 -0.247 5.041 144.984 1.00119.00 C ANISOU 5265 CA TYR B1101 14026 13447 17738 -629 1267 -228 C ATOM 5266 C TYR B1101 1.194 4.556 144.798 1.00118.13 C ANISOU 5266 C TYR B1101 13991 13485 17405 -648 1156 -428 C ATOM 5267 O TYR B1101 2.053 5.339 144.392 1.00118.85 O ANISOU 5267 O TYR B1101 14076 13678 17401 -665 1163 -406 O ATOM 5268 CB TYR B1101 -0.507 5.258 146.475 1.00119.13 C ANISOU 5268 CB TYR B1101 14205 13179 17877 -626 1453 -261 C ATOM 5269 CG TYR B1101 -1.796 5.984 146.779 1.00120.49 C ANISOU 5269 CG TYR B1101 14310 13160 18311 -610 1626 -76 C ATOM 5270 CD1 TYR B1101 -2.991 5.284 146.934 1.00120.54 C ANISOU 5270 CD1 TYR B1101 14264 13088 18446 -587 1612 -29 C ATOM 5271 CD2 TYR B1101 -1.817 7.367 146.940 1.00121.37 C ANISOU 5271 CD2 TYR B1101 14399 13144 18571 -617 1820 49 C ATOM 5272 CE1 TYR B1101 -4.182 5.944 147.215 1.00121.58 C ANISOU 5272 CE1 TYR B1101 14316 13029 18847 -568 1782 147 C ATOM 5273 CE2 TYR B1101 -3.000 8.043 147.225 1.00122.60 C ANISOU 5273 CE2 TYR B1101 14466 13087 19027 -598 2007 218 C ATOM 5274 CZ TYR B1101 -4.181 7.327 147.354 1.00122.78 C ANISOU 5274 CZ TYR B1101 14432 13044 19172 -572 1986 272 C ATOM 5275 OH TYR B1101 -5.357 7.974 147.656 1.00123.76 O ANISOU 5275 OH TYR B1101 14457 12945 19620 -550 2182 442 O ATOM 5276 N ILE B1102 1.456 3.280 145.080 1.00117.57 N ANISOU 5276 N ILE B1102 13972 13415 17281 -644 1060 -608 N ATOM 5277 CA ILE B1102 2.830 2.817 145.338 1.00117.59 C ANISOU 5277 CA ILE B1102 14067 13463 17149 -654 1000 -784 C ATOM 5278 C ILE B1102 3.714 2.779 144.081 1.00120.02 C ANISOU 5278 C ILE B1102 14272 14029 17299 -675 886 -864 C ATOM 5279 O ILE B1102 4.920 3.042 144.177 1.00120.69 O ANISOU 5279 O ILE B1102 14419 14160 17277 -684 882 -936 O ATOM 5280 CB ILE B1102 2.853 1.455 146.090 1.00116.25 C ANISOU 5280 CB ILE B1102 13954 13182 17032 -643 942 -919 C ATOM 5281 CG1 ILE B1102 2.035 1.528 147.395 1.00116.18 C ANISOU 5281 CG1 ILE B1102 14052 12945 17145 -649 1059 -838 C ATOM 5282 CG2 ILE B1102 4.287 1.026 146.404 1.00115.38 C ANISOU 5282 CG2 ILE B1102 13908 13100 16830 -655 885 -1050 C ATOM 5283 CD1 ILE B1102 2.411 2.651 148.345 1.00115.89 C ANISOU 5283 CD1 ILE B1102 14151 12803 17077 -696 1217 -779 C ATOM 5284 N GLN B1103 3.127 2.479 142.920 1.00122.56 N ANISOU 5284 N GLN B1103 14434 14538 17594 -704 801 -852 N ATOM 5285 CA GLN B1103 3.865 2.530 141.636 1.00124.24 C ANISOU 5285 CA GLN B1103 14532 15042 17631 -763 707 -926 C ATOM 5286 C GLN B1103 4.588 3.866 141.398 1.00123.72 C ANISOU 5286 C GLN B1103 14475 15057 17476 -774 752 -798 C ATOM 5287 O GLN B1103 5.719 3.884 140.887 1.00124.39 O ANISOU 5287 O GLN B1103 14551 15300 17410 -802 704 -913 O ATOM 5288 CB GLN B1103 2.941 2.254 140.439 1.00127.18 C ANISOU 5288 CB GLN B1103 14718 15641 17963 -840 623 -876 C ATOM 5289 CG GLN B1103 2.624 0.790 140.195 1.00128.69 C ANISOU 5289 CG GLN B1103 14861 15862 18173 -872 553 -1095 C ATOM 5290 CD GLN B1103 2.028 0.533 138.822 1.00131.17 C ANISOU 5290 CD GLN B1103 14982 16490 18365 -1005 462 -1100 C ATOM 5291 OE1 GLN B1103 2.569 0.976 137.803 1.00131.87 O ANISOU 5291 OE1 GLN B1103 14973 16865 18266 -1102 415 -1102 O ATOM 5292 NE2 GLN B1103 0.910 -0.200 138.788 1.00132.33 N ANISOU 5292 NE2 GLN B1103 15068 16606 18601 -1031 435 -1101 N ATOM 5293 N LYS B1104 3.933 4.969 141.772 1.00123.61 N ANISOU 5293 N LYS B1104 14467 14917 17579 -752 858 -567 N ATOM 5294 CA LYS B1104 4.493 6.313 141.608 1.00125.17 C ANISOU 5294 CA LYS B1104 14659 15147 17750 -760 926 -423 C ATOM 5295 C LYS B1104 5.821 6.467 142.356 1.00124.86 C ANISOU 5295 C LYS B1104 14787 15027 17624 -746 970 -567 C ATOM 5296 O LYS B1104 6.831 6.855 141.762 1.00125.25 O ANISOU 5296 O LYS B1104 14813 15246 17530 -773 925 -597 O ATOM 5297 CB LYS B1104 3.489 7.374 142.086 1.00126.45 C ANISOU 5297 CB LYS B1104 14797 15106 18140 -733 1076 -174 C ATOM 5298 CG LYS B1104 3.921 8.812 141.817 1.00127.16 C ANISOU 5298 CG LYS B1104 14838 15208 18267 -744 1160 4 C ATOM 5299 CD LYS B1104 2.787 9.803 141.972 1.00128.13 C ANISOU 5299 CD LYS B1104 14855 15149 18678 -723 1305 280 C ATOM 5300 CE LYS B1104 3.284 11.200 141.654 1.00129.15 C ANISOU 5300 CE LYS B1104 14911 15278 18880 -735 1391 460 C ATOM 5301 NZ LYS B1104 2.202 12.210 141.756 1.00130.86 N ANISOU 5301 NZ LYS B1104 14984 15288 19447 -711 1552 750 N ATOM 5302 N TYR B1105 5.811 6.142 143.649 1.00133.10 N ANISOU 5302 N TYR B1105 19341 16652 14579 -1813 -1140 1859 N ATOM 5303 CA TYR B1105 7.008 6.220 144.497 1.00132.96 C ANISOU 5303 CA TYR B1105 19351 16706 14458 -1860 -1106 1849 C ATOM 5304 C TYR B1105 8.137 5.368 143.922 1.00130.27 C ANISOU 5304 C TYR B1105 19176 16281 14037 -1769 -1224 1995 C ATOM 5305 O TYR B1105 9.254 5.853 143.745 1.00129.22 O ANISOU 5305 O TYR B1105 19065 16107 13925 -1679 -1204 1999 O ATOM 5306 CB TYR B1105 6.687 5.784 145.937 1.00135.66 C ANISOU 5306 CB TYR B1105 19659 17228 14658 -2086 -1070 1802 C ATOM 5307 CG TYR B1105 7.791 6.072 146.944 1.00137.63 C ANISOU 5307 CG TYR B1105 19904 17578 14809 -2170 -1020 1774 C ATOM 5308 CD1 TYR B1105 7.907 7.330 147.548 1.00137.95 C ANISOU 5308 CD1 TYR B1105 19804 17691 14919 -2206 -866 1608 C ATOM 5309 CD2 TYR B1105 8.714 5.084 147.305 1.00138.58 C ANISOU 5309 CD2 TYR B1105 20151 17718 14782 -2222 -1129 1913 C ATOM 5310 CE1 TYR B1105 8.911 7.596 148.472 1.00138.37 C ANISOU 5310 CE1 TYR B1105 19854 17847 14872 -2295 -820 1582 C ATOM 5311 CE2 TYR B1105 9.723 5.342 148.228 1.00138.59 C ANISOU 5311 CE2 TYR B1105 20146 17814 14695 -2310 -1096 1903 C ATOM 5312 CZ TYR B1105 9.817 6.598 148.811 1.00138.63 C ANISOU 5312 CZ TYR B1105 20022 17904 14746 -2350 -939 1738 C ATOM 5313 OH TYR B1105 10.814 6.856 149.726 1.00137.94 O ANISOU 5313 OH TYR B1105 19930 17919 14561 -2448 -905 1728 O ATOM 5314 N LEU B1106 7.820 4.114 143.606 1.00128.19 N ANISOU 5314 N LEU B1106 19018 15985 13700 -1792 -1343 2105 N ATOM 5315 CA LEU B1106 8.774 3.186 142.983 1.00126.82 C ANISOU 5315 CA LEU B1106 18988 15713 13484 -1708 -1457 2228 C ATOM 5316 C LEU B1106 9.372 3.757 141.696 1.00125.30 C ANISOU 5316 C LEU B1106 18825 15392 13392 -1521 -1451 2231 C ATOM 5317 O LEU B1106 10.596 3.841 141.568 1.00126.13 O ANISOU 5317 O LEU B1106 18978 15453 13491 -1450 -1456 2252 O ATOM 5318 CB LEU B1106 8.097 1.848 142.680 1.00127.52 C ANISOU 5318 CB LEU B1106 19160 15769 13520 -1753 -1575 2323 C ATOM 5319 CG LEU B1106 8.939 0.734 142.059 1.00127.30 C ANISOU 5319 CG LEU B1106 19265 15628 13473 -1684 -1696 2433 C ATOM 5320 CD1 LEU B1106 9.884 0.153 143.090 1.00127.46 C ANISOU 5320 CD1 LEU B1106 19316 15691 13420 -1777 -1748 2497 C ATOM 5321 CD2 LEU B1106 8.057 -0.361 141.457 1.00127.45 C ANISOU 5321 CD2 LEU B1106 19347 15594 13482 -1699 -1794 2498 C ATOM 5322 N GLU B 220 8.506 4.146 140.759 1.00123.43 N ANISOU 5322 N GLU B 220 18555 15099 13243 -1456 -1446 2215 N ATOM 5323 CA GLU B 220 8.950 4.667 139.453 1.00121.79 C ANISOU 5323 CA GLU B 220 18375 14783 13115 -1307 -1454 2233 C ATOM 5324 C GLU B 220 9.758 5.972 139.569 1.00119.90 C ANISOU 5324 C GLU B 220 18061 14545 12950 -1239 -1361 2167 C ATOM 5325 O GLU B 220 10.805 6.135 138.910 1.00119.07 O ANISOU 5325 O GLU B 220 18016 14376 12850 -1140 -1372 2193 O ATOM 5326 CB GLU B 220 7.751 4.859 138.512 1.00123.15 C ANISOU 5326 CB GLU B 220 18512 14910 13368 -1283 -1481 2246 C ATOM 5327 CG GLU B 220 7.136 3.550 138.018 1.00123.85 C ANISOU 5327 CG GLU B 220 18700 14971 13386 -1317 -1584 2323 C ATOM 5328 CD GLU B 220 5.807 3.737 137.298 1.00124.46 C ANISOU 5328 CD GLU B 220 18728 15023 13537 -1323 -1610 2337 C ATOM 5329 OE1 GLU B 220 5.573 4.836 136.748 1.00124.99 O ANISOU 5329 OE1 GLU B 220 18708 15056 13724 -1267 -1577 2317 O ATOM 5330 OE2 GLU B 220 4.995 2.781 137.272 1.00124.26 O ANISOU 5330 OE2 GLU B 220 18746 15006 13460 -1386 -1674 2377 O ATOM 5331 N ARG B 221 9.286 6.889 140.416 1.00118.83 N ANISOU 5331 N ARG B 221 17790 14482 12877 -1300 -1265 2070 N ATOM 5332 CA ARG B 221 9.986 8.166 140.639 1.00117.53 C ANISOU 5332 CA ARG B 221 17537 14320 12797 -1247 -1169 1993 C ATOM 5333 C ARG B 221 11.327 7.962 141.356 1.00114.36 C ANISOU 5333 C ARG B 221 17196 13961 12293 -1260 -1154 1999 C ATOM 5334 O ARG B 221 12.332 8.588 140.991 1.00114.48 O ANISOU 5334 O ARG B 221 17221 13930 12345 -1163 -1128 1996 O ATOM 5335 CB ARG B 221 9.105 9.169 141.405 1.00119.57 C ANISOU 5335 CB ARG B 221 17618 14642 13171 -1319 -1060 1863 C ATOM 5336 CG ARG B 221 7.850 9.641 140.659 1.00121.28 C ANISOU 5336 CG ARG B 221 17738 14791 13549 -1290 -1072 1852 C ATOM 5337 CD ARG B 221 8.100 10.371 139.340 1.00121.53 C ANISOU 5337 CD ARG B 221 17765 14699 13709 -1151 -1113 1914 C ATOM 5338 NE ARG B 221 8.251 11.819 139.487 1.00122.48 N ANISOU 5338 NE ARG B 221 17731 14791 14013 -1108 -1025 1825 N ATOM 5339 CZ ARG B 221 8.329 12.683 138.471 1.00122.90 C ANISOU 5339 CZ ARG B 221 17735 14740 14217 -1010 -1057 1873 C ATOM 5340 NH1 ARG B 221 8.273 12.271 137.202 1.00122.93 N ANISOU 5340 NH1 ARG B 221 17839 14675 14193 -955 -1171 2007 N ATOM 5341 NH2 ARG B 221 8.465 13.984 138.723 1.00123.33 N ANISOU 5341 NH2 ARG B 221 17637 14765 14458 -979 -978 1787 N ATOM 5342 N ALA B 222 11.350 7.081 142.355 1.00111.30 N ANISOU 5342 N ALA B 222 16847 13661 11780 -1386 -1179 2018 N ATOM 5343 CA ALA B 222 12.603 6.691 143.019 1.00109.10 C ANISOU 5343 CA ALA B 222 16633 13414 11405 -1415 -1199 2057 C ATOM 5344 C ALA B 222 13.578 6.052 142.029 1.00106.95 C ANISOU 5344 C ALA B 222 16487 13019 11131 -1289 -1287 2151 C ATOM 5345 O ALA B 222 14.750 6.433 141.981 1.00106.65 O ANISOU 5345 O ALA B 222 16467 12951 11103 -1220 -1266 2150 O ATOM 5346 CB ALA B 222 12.332 5.755 144.182 1.00109.53 C ANISOU 5346 CB ALA B 222 16706 13579 11330 -1594 -1241 2093 C ATOM 5347 N ARG B 223 13.080 5.097 141.240 1.00105.66 N ANISOU 5347 N ARG B 223 16401 12787 10958 -1265 -1378 2219 N ATOM 5348 CA ARG B 223 13.845 4.503 140.131 1.00104.45 C ANISOU 5348 CA ARG B 223 16353 12514 10818 -1152 -1448 2278 C ATOM 5349 C ARG B 223 14.448 5.595 139.242 1.00101.86 C ANISOU 5349 C ARG B 223 16004 12133 10565 -1023 -1386 2236 C ATOM 5350 O ARG B 223 15.674 5.640 139.043 1.00101.52 O ANISOU 5350 O ARG B 223 16003 12045 10524 -955 -1383 2241 O ATOM 5351 CB ARG B 223 12.973 3.585 139.263 1.00105.97 C ANISOU 5351 CB ARG B 223 16606 12650 11006 -1149 -1528 2325 C ATOM 5352 CG ARG B 223 12.806 2.157 139.757 1.00107.67 C ANISOU 5352 CG ARG B 223 16886 12863 11158 -1239 -1628 2396 C ATOM 5353 CD ARG B 223 11.869 1.383 138.836 1.00108.99 C ANISOU 5353 CD ARG B 223 17106 12976 11329 -1232 -1695 2428 C ATOM 5354 NE ARG B 223 11.409 0.113 139.404 1.00110.79 N ANISOU 5354 NE ARG B 223 17374 13214 11507 -1336 -1788 2494 N ATOM 5355 CZ ARG B 223 10.524 -0.708 138.830 1.00112.03 C ANISOU 5355 CZ ARG B 223 17574 13335 11657 -1356 -1854 2527 C ATOM 5356 NH1 ARG B 223 9.973 -0.410 137.649 1.00111.82 N ANISOU 5356 NH1 ARG B 223 17557 13266 11660 -1287 -1839 2502 N ATOM 5357 NH2 ARG B 223 10.189 -1.852 139.432 1.00112.99 N ANISOU 5357 NH2 ARG B 223 17726 13463 11739 -1457 -1944 2594 N ATOM 5358 N SER B 224 13.584 6.476 138.728 1.00 99.52 N ANISOU 5358 N SER B 224 15634 11838 10341 -998 -1344 2201 N ATOM 5359 CA SER B 224 14.038 7.528 137.807 1.00 97.54 C ANISOU 5359 CA SER B 224 15357 11535 10168 -892 -1305 2183 C ATOM 5360 C SER B 224 15.068 8.472 138.452 1.00 95.37 C ANISOU 5360 C SER B 224 15028 11288 9919 -861 -1223 2129 C ATOM 5361 O SER B 224 16.129 8.734 137.865 1.00 94.75 O ANISOU 5361 O SER B 224 14992 11160 9846 -775 -1218 2138 O ATOM 5362 CB SER B 224 12.859 8.322 137.231 1.00 98.00 C ANISOU 5362 CB SER B 224 15324 11581 10327 -887 -1294 2173 C ATOM 5363 OG SER B 224 12.297 9.199 138.187 1.00 98.77 O ANISOU 5363 OG SER B 224 15285 11738 10504 -938 -1213 2095 O ATOM 5364 N THR B 225 14.770 8.953 139.660 1.00 93.41 N ANISOU 5364 N THR B 225 14685 11124 9680 -941 -1155 2065 N ATOM 5365 CA THR B 225 15.682 9.874 140.363 1.00 91.76 C ANISOU 5365 CA THR B 225 14416 10953 9492 -929 -1069 2003 C ATOM 5366 C THR B 225 17.007 9.219 140.784 1.00 90.18 C ANISOU 5366 C THR B 225 14307 10756 9200 -927 -1099 2044 C ATOM 5367 O THR B 225 18.050 9.868 140.717 1.00 89.08 O ANISOU 5367 O THR B 225 14163 10598 9086 -858 -1058 2025 O ATOM 5368 CB THR B 225 15.015 10.544 141.583 1.00 92.01 C ANISOU 5368 CB THR B 225 14314 11090 9553 -1040 -976 1901 C ATOM 5369 OG1 THR B 225 14.455 9.546 142.435 1.00 93.24 O ANISOU 5369 OG1 THR B 225 14497 11329 9601 -1177 -1010 1918 O ATOM 5370 CG2 THR B 225 13.920 11.510 141.135 1.00 92.17 C ANISOU 5370 CG2 THR B 225 14209 11080 9731 -1015 -930 1840 C ATOM 5371 N LEU B 226 16.970 7.950 141.198 1.00 89.53 N ANISOU 5371 N LEU B 226 14300 10688 9029 -1002 -1179 2107 N ATOM 5372 CA LEU B 226 18.205 7.177 141.461 1.00 89.18 C ANISOU 5372 CA LEU B 226 14337 10613 8933 -995 -1237 2167 C ATOM 5373 C LEU B 226 19.016 6.938 140.176 1.00 89.27 C ANISOU 5373 C LEU B 226 14428 10503 8987 -858 -1272 2192 C ATOM 5374 O LEU B 226 20.238 7.135 140.160 1.00 89.09 O ANISOU 5374 O LEU B 226 14424 10446 8978 -799 -1258 2190 O ATOM 5375 CB LEU B 226 17.909 5.832 142.139 1.00 89.50 C ANISOU 5375 CB LEU B 226 14428 10678 8898 -1114 -1335 2244 C ATOM 5376 CG LEU B 226 17.583 5.878 143.640 1.00 90.10 C ANISOU 5376 CG LEU B 226 14443 10897 8893 -1287 -1313 2236 C ATOM 5377 CD1 LEU B 226 16.908 4.594 144.120 1.00 90.60 C ANISOU 5377 CD1 LEU B 226 14548 10989 8885 -1416 -1418 2320 C ATOM 5378 CD2 LEU B 226 18.827 6.158 144.475 1.00 90.06 C ANISOU 5378 CD2 LEU B 226 14429 10932 8857 -1319 -1297 2247 C ATOM 5379 N GLN B 227 18.336 6.516 139.110 1.00 89.75 N ANISOU 5379 N GLN B 227 14530 10505 9063 -821 -1314 2210 N ATOM 5380 CA GLN B 227 19.000 6.313 137.813 1.00 89.86 C ANISOU 5380 CA GLN B 227 14614 10424 9102 -717 -1335 2214 C ATOM 5381 C GLN B 227 19.554 7.616 137.205 1.00 89.68 C ANISOU 5381 C GLN B 227 14552 10396 9126 -629 -1259 2171 C ATOM 5382 O GLN B 227 20.560 7.591 136.476 1.00 90.13 O ANISOU 5382 O GLN B 227 14656 10396 9191 -556 -1256 2162 O ATOM 5383 CB GLN B 227 18.074 5.598 136.829 1.00 90.51 C ANISOU 5383 CB GLN B 227 14746 10466 9175 -723 -1394 2238 C ATOM 5384 CG GLN B 227 17.884 4.125 137.167 1.00 91.49 C ANISOU 5384 CG GLN B 227 14930 10562 9270 -785 -1483 2284 C ATOM 5385 CD GLN B 227 16.781 3.456 136.369 1.00 92.52 C ANISOU 5385 CD GLN B 227 15098 10669 9385 -810 -1536 2304 C ATOM 5386 OE1 GLN B 227 16.379 3.937 135.308 1.00 93.17 O ANISOU 5386 OE1 GLN B 227 15184 10741 9475 -772 -1518 2288 O ATOM 5387 NE2 GLN B 227 16.287 2.331 136.879 1.00 93.18 N ANISOU 5387 NE2 GLN B 227 15210 10746 9446 -885 -1611 2348 N ATOM 5388 N LYS B 228 18.910 8.743 137.510 1.00 89.83 N ANISOU 5388 N LYS B 228 14475 10468 9187 -642 -1199 2140 N ATOM 5389 CA LYS B 228 19.463 10.061 137.152 1.00 90.20 C ANISOU 5389 CA LYS B 228 14466 10509 9297 -569 -1131 2105 C ATOM 5390 C LYS B 228 20.752 10.384 137.931 1.00 89.05 C ANISOU 5390 C LYS B 228 14312 10379 9140 -547 -1082 2077 C ATOM 5391 O LYS B 228 21.717 10.915 137.358 1.00 88.87 O ANISOU 5391 O LYS B 228 14304 10321 9139 -468 -1055 2067 O ATOM 5392 CB LYS B 228 18.411 11.164 137.321 1.00 92.05 C ANISOU 5392 CB LYS B 228 14578 10775 9621 -591 -1084 2073 C ATOM 5393 CG LYS B 228 17.406 11.178 136.172 1.00 93.54 C ANISOU 5393 CG LYS B 228 14766 10923 9849 -584 -1138 2119 C ATOM 5394 CD LYS B 228 16.117 11.915 136.490 1.00 94.68 C ANISOU 5394 CD LYS B 228 14783 11087 10103 -627 -1115 2093 C ATOM 5395 CE LYS B 228 15.130 11.754 135.341 1.00 95.41 C ANISOU 5395 CE LYS B 228 14886 11135 10228 -631 -1192 2161 C ATOM 5396 NZ LYS B 228 13.928 12.623 135.472 1.00 96.39 N ANISOU 5396 NZ LYS B 228 14864 11251 10506 -659 -1178 2143 N ATOM 5397 N GLU B 229 20.764 10.056 139.226 1.00 88.21 N ANISOU 5397 N GLU B 229 14184 10336 8995 -631 -1075 2069 N ATOM 5398 CA GLU B 229 22.002 10.118 140.036 1.00 87.17 C ANISOU 5398 CA GLU B 229 14058 10225 8838 -634 -1052 2063 C ATOM 5399 C GLU B 229 23.100 9.213 139.471 1.00 86.06 C ANISOU 5399 C GLU B 229 14014 9997 8686 -572 -1115 2107 C ATOM 5400 O GLU B 229 24.269 9.607 139.417 1.00 86.14 O ANISOU 5400 O GLU B 229 14030 9981 8716 -510 -1085 2092 O ATOM 5401 CB GLU B 229 21.740 9.757 141.512 1.00 87.43 C ANISOU 5401 CB GLU B 229 14056 10354 8806 -772 -1055 2067 C ATOM 5402 CG GLU B 229 21.274 10.911 142.385 1.00 87.77 C ANISOU 5402 CG GLU B 229 13982 10499 8867 -837 -952 1981 C ATOM 5403 CD GLU B 229 22.331 11.974 142.600 1.00 87.57 C ANISOU 5403 CD GLU B 229 13912 10482 8877 -782 -873 1931 C ATOM 5404 OE1 GLU B 229 23.515 11.620 142.817 1.00 87.47 O ANISOU 5404 OE1 GLU B 229 13955 10450 8829 -763 -903 1974 O ATOM 5405 OE2 GLU B 229 21.968 13.173 142.556 1.00 87.55 O ANISOU 5405 OE2 GLU B 229 13810 10496 8956 -758 -785 1849 O ATOM 5406 N LEU B 230 22.715 8.009 139.043 1.00 84.87 N ANISOU 5406 N LEU B 230 13932 9797 8518 -591 -1198 2150 N ATOM 5407 CA LEU B 230 23.645 7.093 138.371 1.00 83.74 C ANISOU 5407 CA LEU B 230 13866 9554 8398 -533 -1252 2168 C ATOM 5408 C LEU B 230 24.175 7.663 137.053 1.00 82.66 C ANISOU 5408 C LEU B 230 13749 9367 8288 -430 -1206 2121 C ATOM 5409 O LEU B 230 25.381 7.573 136.785 1.00 82.22 O ANISOU 5409 O LEU B 230 13718 9258 8263 -371 -1195 2099 O ATOM 5410 CB LEU B 230 22.985 5.732 138.124 1.00 83.93 C ANISOU 5410 CB LEU B 230 13943 9530 8414 -580 -1344 2209 C ATOM 5411 CG LEU B 230 23.883 4.596 137.627 1.00 84.08 C ANISOU 5411 CG LEU B 230 14022 9433 8489 -541 -1406 2214 C ATOM 5412 CD1 LEU B 230 24.744 4.113 138.770 1.00 84.16 C ANISOU 5412 CD1 LEU B 230 14017 9426 8533 -583 -1459 2268 C ATOM 5413 CD2 LEU B 230 23.070 3.453 137.043 1.00 84.64 C ANISOU 5413 CD2 LEU B 230 14141 9454 8564 -572 -1477 2229 C ATOM 5414 N LYS B 231 23.278 8.242 136.247 1.00 82.24 N ANISOU 5414 N LYS B 231 13683 9336 8228 -421 -1184 2110 N ATOM 5415 CA LYS B 231 23.648 8.776 134.923 1.00 81.58 C ANISOU 5415 CA LYS B 231 13621 9224 8151 -356 -1155 2084 C ATOM 5416 C LYS B 231 24.717 9.880 134.992 1.00 80.94 C ANISOU 5416 C LYS B 231 13502 9153 8097 -293 -1086 2054 C ATOM 5417 O LYS B 231 25.658 9.888 134.191 1.00 80.89 O ANISOU 5417 O LYS B 231 13534 9111 8090 -242 -1068 2024 O ATOM 5418 CB LYS B 231 22.418 9.297 134.174 1.00 81.40 C ANISOU 5418 CB LYS B 231 13574 9230 8125 -379 -1164 2106 C ATOM 5419 CG LYS B 231 22.662 9.566 132.690 1.00 81.68 C ANISOU 5419 CG LYS B 231 13646 9246 8139 -352 -1164 2101 C ATOM 5420 CD LYS B 231 21.578 10.431 132.068 1.00 81.99 C ANISOU 5420 CD LYS B 231 13635 9315 8200 -378 -1179 2148 C ATOM 5421 CE LYS B 231 21.992 10.921 130.688 1.00 82.40 C ANISOU 5421 CE LYS B 231 13715 9370 8222 -372 -1180 2160 C ATOM 5422 NZ LYS B 231 21.096 12.005 130.200 1.00 82.84 N ANISOU 5422 NZ LYS B 231 13697 9446 8332 -397 -1207 2229 N ATOM 5423 N ILE B 232 24.567 10.804 135.940 1.00 80.40 N ANISOU 5423 N ILE B 232 13355 9138 8054 -304 -1041 2050 N ATOM 5424 CA ILE B 232 25.524 11.913 136.088 1.00 79.91 C ANISOU 5424 CA ILE B 232 13249 9087 8025 -248 -973 2021 C ATOM 5425 C ILE B 232 26.876 11.389 136.597 1.00 78.31 C ANISOU 5425 C ILE B 232 13084 8856 7815 -223 -971 2009 C ATOM 5426 O ILE B 232 27.943 11.713 136.035 1.00 77.60 O ANISOU 5426 O ILE B 232 13012 8733 7738 -157 -941 1984 O ATOM 5427 CB ILE B 232 24.986 13.027 137.024 1.00 81.04 C ANISOU 5427 CB ILE B 232 13285 9292 8213 -277 -916 2000 C ATOM 5428 CG1 ILE B 232 23.699 13.641 136.447 1.00 82.69 C ANISOU 5428 CG1 ILE B 232 13435 9507 8475 -292 -922 2011 C ATOM 5429 CG2 ILE B 232 26.031 14.129 137.211 1.00 80.41 C ANISOU 5429 CG2 ILE B 232 13160 9220 8172 -220 -847 1966 C ATOM 5430 CD1 ILE B 232 22.937 14.527 137.409 1.00 83.47 C ANISOU 5430 CD1 ILE B 232 13410 9655 8646 -337 -867 1967 C ATOM 5431 N ALA B 233 26.814 10.569 137.648 1.00 77.17 N ANISOU 5431 N ALA B 233 12945 8721 7652 -285 -1013 2035 N ATOM 5432 CA ALA B 233 28.005 9.940 138.246 1.00 75.88 C ANISOU 5432 CA ALA B 233 12806 8520 7503 -280 -1040 2049 C ATOM 5433 C ALA B 233 28.965 9.352 137.208 1.00 74.44 C ANISOU 5433 C ALA B 233 12682 8241 7360 -205 -1054 2023 C ATOM 5434 O ALA B 233 30.174 9.568 137.293 1.00 74.09 O ANISOU 5434 O ALA B 233 12633 8166 7352 -155 -1029 2003 O ATOM 5435 CB ALA B 233 27.591 8.868 139.244 1.00 76.47 C ANISOU 5435 CB ALA B 233 12891 8606 7558 -379 -1120 2109 C ATOM 5436 N LYS B 234 28.421 8.632 136.228 1.00 73.03 N ANISOU 5436 N LYS B 234 12551 8020 7176 -205 -1088 2012 N ATOM 5437 CA LYS B 234 29.225 8.082 135.130 1.00 72.11 C ANISOU 5437 CA LYS B 234 12481 7824 7094 -152 -1084 1955 C ATOM 5438 C LYS B 234 29.911 9.185 134.313 1.00 71.08 C ANISOU 5438 C LYS B 234 12342 7716 6949 -91 -1003 1904 C ATOM 5439 O LYS B 234 31.110 9.082 134.001 1.00 71.66 O ANISOU 5439 O LYS B 234 12423 7739 7063 -42 -975 1853 O ATOM 5440 CB LYS B 234 28.368 7.209 134.211 1.00 72.63 C ANISOU 5440 CB LYS B 234 12594 7862 7139 -185 -1125 1942 C ATOM 5441 CG LYS B 234 27.894 5.908 134.843 1.00 73.05 C ANISOU 5441 CG LYS B 234 12662 7866 7225 -239 -1214 1985 C ATOM 5442 CD LYS B 234 27.008 5.118 133.894 1.00 73.44 C ANISOU 5442 CD LYS B 234 12757 7894 7252 -272 -1246 1964 C ATOM 5443 CE LYS B 234 26.570 3.797 134.506 1.00 74.18 C ANISOU 5443 CE LYS B 234 12863 7929 7393 -325 -1342 2010 C ATOM 5444 NZ LYS B 234 25.695 3.006 133.599 1.00 74.70 N ANISOU 5444 NZ LYS B 234 12972 7972 7438 -359 -1372 1985 N ATOM 5445 N SER B 235 29.153 10.238 133.984 1.00 69.71 N ANISOU 5445 N SER B 235 12142 7612 6730 -99 -972 1923 N ATOM 5446 CA SER B 235 29.693 11.389 133.244 1.00 68.34 C ANISOU 5446 CA SER B 235 11951 7466 6546 -56 -910 1898 C ATOM 5447 C SER B 235 30.835 12.050 134.007 1.00 67.58 C ANISOU 5447 C SER B 235 11818 7370 6488 -5 -862 1884 C ATOM 5448 O SER B 235 31.927 12.301 133.456 1.00 67.04 O ANISOU 5448 O SER B 235 11761 7281 6428 41 -821 1839 O ATOM 5449 CB SER B 235 28.597 12.423 132.967 1.00 67.87 C ANISOU 5449 CB SER B 235 11847 7465 6472 -80 -907 1943 C ATOM 5450 OG SER B 235 27.439 11.818 132.416 1.00 68.30 O ANISOU 5450 OG SER B 235 11931 7524 6496 -135 -960 1970 O ATOM 5451 N LEU B 236 30.580 12.311 135.289 1.00 67.10 N ANISOU 5451 N LEU B 236 11710 7341 6444 -27 -864 1916 N ATOM 5452 CA LEU B 236 31.589 12.921 136.154 1.00 66.42 C ANISOU 5452 CA LEU B 236 11584 7266 6384 2 -823 1907 C ATOM 5453 C LEU B 236 32.807 12.013 136.368 1.00 66.55 C ANISOU 5453 C LEU B 236 11634 7212 6438 27 -848 1894 C ATOM 5454 O LEU B 236 33.933 12.502 136.474 1.00 66.86 O ANISOU 5454 O LEU B 236 11658 7240 6506 76 -807 1871 O ATOM 5455 CB LEU B 236 30.969 13.334 137.485 1.00 66.30 C ANISOU 5455 CB LEU B 236 11508 7318 6364 -56 -816 1932 C ATOM 5456 CG LEU B 236 29.910 14.441 137.409 1.00 66.12 C ANISOU 5456 CG LEU B 236 11418 7352 6353 -72 -775 1924 C ATOM 5457 CD1 LEU B 236 29.177 14.574 138.732 1.00 66.24 C ANISOU 5457 CD1 LEU B 236 11371 7436 6361 -156 -763 1922 C ATOM 5458 CD2 LEU B 236 30.525 15.773 136.997 1.00 65.62 C ANISOU 5458 CD2 LEU B 236 11309 7293 6329 -8 -710 1898 C ATOM 5459 N ALA B 237 32.581 10.700 136.419 1.00 66.77 N ANISOU 5459 N ALA B 237 11698 7184 6485 -6 -919 1911 N ATOM 5460 CA ALA B 237 33.673 9.720 136.484 1.00 67.05 C ANISOU 5460 CA ALA B 237 11750 7122 6601 17 -957 1896 C ATOM 5461 C ALA B 237 34.517 9.749 135.211 1.00 67.05 C ANISOU 5461 C ALA B 237 11774 7072 6631 83 -904 1806 C ATOM 5462 O ALA B 237 35.751 9.843 135.284 1.00 67.05 O ANISOU 5462 O ALA B 237 11756 7025 6693 132 -878 1772 O ATOM 5463 CB ALA B 237 33.126 8.320 136.721 1.00 67.63 C ANISOU 5463 CB ALA B 237 11847 7137 6712 -37 -1052 1934 C ATOM 5464 N LEU B 238 33.846 9.693 134.054 1.00 67.27 N ANISOU 5464 N LEU B 238 11836 7117 6606 72 -887 1766 N ATOM 5465 CA LEU B 238 34.524 9.801 132.745 1.00 67.34 C ANISOU 5465 CA LEU B 238 11867 7110 6608 101 -826 1671 C ATOM 5466 C LEU B 238 35.471 11.006 132.665 1.00 66.49 C ANISOU 5466 C LEU B 238 11733 7041 6488 152 -753 1652 C ATOM 5467 O LEU B 238 36.583 10.905 132.128 1.00 66.49 O ANISOU 5467 O LEU B 238 11733 7001 6526 187 -708 1571 O ATOM 5468 CB LEU B 238 33.503 9.881 131.605 1.00 67.68 C ANISOU 5468 CB LEU B 238 11946 7207 6558 52 -821 1660 C ATOM 5469 CG LEU B 238 34.064 10.061 130.185 1.00 68.55 C ANISOU 5469 CG LEU B 238 12082 7338 6622 42 -759 1566 C ATOM 5470 CD1 LEU B 238 35.026 8.935 129.828 1.00 69.50 C ANISOU 5470 CD1 LEU B 238 12210 7365 6830 55 -739 1447 C ATOM 5471 CD2 LEU B 238 32.939 10.141 129.168 1.00 69.09 C ANISOU 5471 CD2 LEU B 238 12186 7475 6588 -32 -775 1584 C ATOM 5472 N ILE B 239 35.018 12.138 133.197 1.00 65.53 N ANISOU 5472 N ILE B 239 11580 6993 6324 153 -739 1716 N ATOM 5473 CA ILE B 239 35.862 13.328 133.295 1.00 64.86 C ANISOU 5473 CA ILE B 239 11461 6941 6239 200 -677 1709 C ATOM 5474 C ILE B 239 37.132 13.051 134.125 1.00 64.16 C ANISOU 5474 C ILE B 239 11352 6796 6228 244 -672 1692 C ATOM 5475 O ILE B 239 38.241 13.441 133.722 1.00 64.07 O ANISOU 5475 O ILE B 239 11334 6770 6239 290 -619 1639 O ATOM 5476 CB ILE B 239 35.055 14.530 133.838 1.00 64.84 C ANISOU 5476 CB ILE B 239 11411 7013 6212 188 -667 1772 C ATOM 5477 CG1 ILE B 239 34.064 14.997 132.768 1.00 65.26 C ANISOU 5477 CG1 ILE B 239 11472 7109 6214 154 -674 1793 C ATOM 5478 CG2 ILE B 239 35.964 15.688 134.249 1.00 64.62 C ANISOU 5478 CG2 ILE B 239 11336 7008 6206 237 -608 1766 C ATOM 5479 CD1 ILE B 239 32.870 15.747 133.299 1.00 65.25 C ANISOU 5479 CD1 ILE B 239 11413 7150 6226 126 -690 1852 C ATOM 5480 N LEU B 240 36.970 12.365 135.258 1.00 63.68 N ANISOU 5480 N LEU B 240 11279 6706 6210 217 -733 1744 N ATOM 5481 CA LEU B 240 38.116 11.987 136.090 1.00 63.44 C ANISOU 5481 CA LEU B 240 11223 6614 6264 239 -754 1753 C ATOM 5482 C LEU B 240 39.064 11.044 135.346 1.00 63.67 C ANISOU 5482 C LEU B 240 11265 6533 6393 277 -758 1675 C ATOM 5483 O LEU B 240 40.289 11.247 135.346 1.00 63.43 O ANISOU 5483 O LEU B 240 11210 6461 6428 327 -724 1635 O ATOM 5484 CB LEU B 240 37.643 11.338 137.401 1.00 63.48 C ANISOU 5484 CB LEU B 240 11213 6618 6285 171 -840 1844 C ATOM 5485 CG LEU B 240 38.711 10.917 138.411 1.00 63.74 C ANISOU 5485 CG LEU B 240 11215 6595 6405 164 -893 1891 C ATOM 5486 CD1 LEU B 240 39.533 12.111 138.862 1.00 63.24 C ANISOU 5486 CD1 LEU B 240 11119 6589 6321 197 -826 1887 C ATOM 5487 CD2 LEU B 240 38.031 10.243 139.577 1.00 64.01 C ANISOU 5487 CD2 LEU B 240 11240 6651 6426 63 -990 1994 C ATOM 5488 N PHE B 241 38.488 10.025 134.709 1.00 64.17 N ANISOU 5488 N PHE B 241 11357 6547 6475 250 -793 1642 N ATOM 5489 CA PHE B 241 39.263 9.096 133.886 1.00 65.26 C ANISOU 5489 CA PHE B 241 11495 6579 6721 275 -781 1534 C ATOM 5490 C PHE B 241 40.057 9.840 132.816 1.00 65.08 C ANISOU 5490 C PHE B 241 11475 6589 6661 312 -675 1426 C ATOM 5491 O PHE B 241 41.261 9.609 132.664 1.00 65.42 O ANISOU 5491 O PHE B 241 11486 6558 6812 354 -643 1348 O ATOM 5492 CB PHE B 241 38.356 8.050 133.230 1.00 66.08 C ANISOU 5492 CB PHE B 241 11631 6649 6826 228 -818 1499 C ATOM 5493 CG PHE B 241 39.091 7.085 132.344 1.00 67.20 C ANISOU 5493 CG PHE B 241 11759 6682 7090 242 -792 1359 C ATOM 5494 CD1 PHE B 241 39.845 6.056 132.896 1.00 68.13 C ANISOU 5494 CD1 PHE B 241 11826 6651 7410 263 -855 1349 C ATOM 5495 CD2 PHE B 241 39.041 7.210 130.962 1.00 67.81 C ANISOU 5495 CD2 PHE B 241 11865 6805 7092 220 -706 1234 C ATOM 5496 CE1 PHE B 241 40.530 5.164 132.085 1.00 69.60 C ANISOU 5496 CE1 PHE B 241 11978 6720 7745 277 -822 1196 C ATOM 5497 CE2 PHE B 241 39.725 6.320 130.144 1.00 69.37 C ANISOU 5497 CE2 PHE B 241 12039 6910 7406 218 -664 1074 C ATOM 5498 CZ PHE B 241 40.468 5.292 130.707 1.00 70.11 C ANISOU 5498 CZ PHE B 241 12070 6840 7725 253 -717 1045 C ATOM 5499 N LEU B 242 39.379 10.737 132.095 1.00 64.46 N ANISOU 5499 N LEU B 242 11428 6622 6439 288 -627 1429 N ATOM 5500 CA LEU B 242 40.031 11.541 131.054 1.00 64.23 C ANISOU 5500 CA LEU B 242 11405 6649 6350 298 -536 1349 C ATOM 5501 C LEU B 242 41.131 12.443 131.626 1.00 63.52 C ANISOU 5501 C LEU B 242 11277 6563 6292 360 -496 1363 C ATOM 5502 O LEU B 242 42.214 12.550 131.033 1.00 63.85 O ANISOU 5502 O LEU B 242 11306 6586 6366 385 -431 1266 O ATOM 5503 CB LEU B 242 39.004 12.365 130.269 1.00 63.97 C ANISOU 5503 CB LEU B 242 11404 6731 6169 245 -523 1389 C ATOM 5504 CG LEU B 242 38.095 11.540 129.351 1.00 64.91 C ANISOU 5504 CG LEU B 242 11566 6860 6235 171 -544 1351 C ATOM 5505 CD1 LEU B 242 36.825 12.297 128.991 1.00 64.70 C ANISOU 5505 CD1 LEU B 242 11558 6931 6091 117 -573 1446 C ATOM 5506 CD2 LEU B 242 38.833 11.108 128.092 1.00 66.02 C ANISOU 5506 CD2 LEU B 242 11722 7001 6362 134 -473 1201 C ATOM 5507 N PHE B 243 40.854 13.065 132.778 1.00 62.43 N ANISOU 5507 N PHE B 243 11117 6455 6148 375 -530 1470 N ATOM 5508 CA PHE B 243 41.857 13.879 133.471 1.00 61.67 C ANISOU 5508 CA PHE B 243 10983 6364 6084 427 -498 1489 C ATOM 5509 C PHE B 243 43.099 13.055 133.812 1.00 61.85 C ANISOU 5509 C PHE B 243 10977 6274 6248 465 -511 1441 C ATOM 5510 O PHE B 243 44.226 13.428 133.452 1.00 61.44 O ANISOU 5510 O PHE B 243 10905 6205 6233 509 -450 1373 O ATOM 5511 CB PHE B 243 41.270 14.493 134.744 1.00 61.35 C ANISOU 5511 CB PHE B 243 10917 6375 6017 412 -533 1597 C ATOM 5512 CG PHE B 243 42.212 15.424 135.458 1.00 61.40 C ANISOU 5512 CG PHE B 243 10884 6402 6043 452 -495 1614 C ATOM 5513 CD1 PHE B 243 42.253 16.773 135.130 1.00 61.18 C ANISOU 5513 CD1 PHE B 243 10839 6447 5956 473 -431 1611 C ATOM 5514 CD2 PHE B 243 43.058 14.955 136.460 1.00 61.72 C ANISOU 5514 CD2 PHE B 243 10896 6385 6168 462 -533 1642 C ATOM 5515 CE1 PHE B 243 43.117 17.637 135.786 1.00 60.92 C ANISOU 5515 CE1 PHE B 243 10769 6434 5944 509 -393 1621 C ATOM 5516 CE2 PHE B 243 43.927 15.813 137.116 1.00 61.24 C ANISOU 5516 CE2 PHE B 243 10800 6349 6117 490 -499 1659 C ATOM 5517 CZ PHE B 243 43.957 17.155 136.777 1.00 60.87 C ANISOU 5517 CZ PHE B 243 10741 6379 6006 517 -423 1641 C ATOM 5518 N ALA B 244 42.872 11.932 134.497 1.00 62.45 N ANISOU 5518 N ALA B 244 11043 6268 6415 444 -597 1482 N ATOM 5519 CA ALA B 244 43.961 11.030 134.906 1.00 63.13 C ANISOU 5519 CA ALA B 244 11085 6221 6678 472 -639 1458 C ATOM 5520 C ALA B 244 44.754 10.502 133.710 1.00 63.85 C ANISOU 5520 C ALA B 244 11164 6236 6859 502 -574 1298 C ATOM 5521 O ALA B 244 45.996 10.501 133.718 1.00 63.80 O ANISOU 5521 O ALA B 244 11111 6161 6969 549 -544 1239 O ATOM 5522 CB ALA B 244 43.410 9.870 135.716 1.00 63.72 C ANISOU 5522 CB ALA B 244 11151 6221 6838 425 -760 1543 C ATOM 5523 N LEU B 245 44.021 10.083 132.680 1.00 64.38 N ANISOU 5523 N LEU B 245 11268 6324 6867 463 -547 1222 N ATOM 5524 CA LEU B 245 44.627 9.546 131.462 1.00 65.67 C ANISOU 5524 CA LEU B 245 11419 6438 7094 462 -470 1044 C ATOM 5525 C LEU B 245 45.436 10.613 130.718 1.00 65.23 C ANISOU 5525 C LEU B 245 11365 6466 6954 478 -357 963 C ATOM 5526 O LEU B 245 46.537 10.333 130.236 1.00 65.97 O ANISOU 5526 O LEU B 245 11414 6494 7156 501 -293 827 O ATOM 5527 CB LEU B 245 43.555 8.947 130.542 1.00 66.65 C ANISOU 5527 CB LEU B 245 11589 6594 7139 393 -466 988 C ATOM 5528 CG LEU B 245 44.032 7.962 129.469 1.00 68.43 C ANISOU 5528 CG LEU B 245 11788 6742 7468 367 -405 790 C ATOM 5529 CD1 LEU B 245 44.472 6.642 130.094 1.00 69.29 C ANISOU 5529 CD1 LEU B 245 11827 6659 7838 399 -481 766 C ATOM 5530 CD2 LEU B 245 42.933 7.721 128.441 1.00 68.89 C ANISOU 5530 CD2 LEU B 245 11906 6887 7382 280 -382 741 C ATOM 5531 N SER B 246 44.892 11.829 130.641 1.00 63.81 N ANISOU 5531 N SER B 246 11225 6422 6595 464 -335 1046 N ATOM 5532 CA SER B 246 45.614 12.969 130.059 1.00 63.15 C ANISOU 5532 CA SER B 246 11141 6424 6427 474 -246 1004 C ATOM 5533 C SER B 246 46.859 13.356 130.864 1.00 62.82 C ANISOU 5533 C SER B 246 11048 6326 6492 550 -234 1016 C ATOM 5534 O SER B 246 47.917 13.625 130.277 1.00 62.60 O ANISOU 5534 O SER B 246 10996 6297 6490 567 -154 910 O ATOM 5535 CB SER B 246 44.699 14.192 129.942 1.00 62.24 C ANISOU 5535 CB SER B 246 11063 6443 6139 444 -250 1115 C ATOM 5536 OG SER B 246 43.589 13.936 129.107 1.00 62.64 O ANISOU 5536 OG SER B 246 11159 6553 6088 366 -264 1113 O ATOM 5537 N TRP B 247 46.733 13.369 132.197 1.00 62.72 N ANISOU 5537 N TRP B 247 11017 6276 6536 582 -313 1143 N ATOM 5538 CA TRP B 247 47.804 13.891 133.075 1.00 62.81 C ANISOU 5538 CA TRP B 247 10984 6258 6622 639 -313 1184 C ATOM 5539 C TRP B 247 48.899 12.909 133.514 1.00 64.08 C ANISOU 5539 C TRP B 247 11083 6266 6998 676 -348 1140 C ATOM 5540 O TRP B 247 50.046 13.334 133.696 1.00 63.90 O ANISOU 5540 O TRP B 247 11019 6216 7042 723 -312 1114 O ATOM 5541 CB TRP B 247 47.206 14.583 134.310 1.00 61.79 C ANISOU 5541 CB TRP B 247 10858 6191 6427 632 -369 1337 C ATOM 5542 CG TRP B 247 46.806 15.989 134.021 1.00 60.94 C ANISOU 5542 CG TRP B 247 10770 6211 6173 629 -310 1365 C ATOM 5543 CD1 TRP B 247 45.542 16.474 133.850 1.00 60.58 C ANISOU 5543 CD1 TRP B 247 10752 6249 6014 587 -320 1419 C ATOM 5544 CD2 TRP B 247 47.688 17.092 133.838 1.00 60.49 C ANISOU 5544 CD2 TRP B 247 10695 6198 6089 668 -239 1343 C ATOM 5545 NE1 TRP B 247 45.585 17.819 133.580 1.00 60.01 N ANISOU 5545 NE1 TRP B 247 10672 6261 5865 599 -266 1436 N ATOM 5546 CE2 TRP B 247 46.892 18.226 133.569 1.00 59.97 C ANISOU 5546 CE2 TRP B 247 10643 6237 5903 647 -216 1391 C ATOM 5547 CE3 TRP B 247 49.078 17.237 133.885 1.00 60.77 C ANISOU 5547 CE3 TRP B 247 10696 6187 6205 719 -198 1289 C ATOM 5548 CZ2 TRP B 247 47.444 19.492 133.342 1.00 59.59 C ANISOU 5548 CZ2 TRP B 247 10578 6249 5814 673 -156 1392 C ATOM 5549 CZ3 TRP B 247 49.627 18.491 133.661 1.00 60.25 C ANISOU 5549 CZ3 TRP B 247 10622 6192 6078 745 -131 1285 C ATOM 5550 CH2 TRP B 247 48.813 19.604 133.396 1.00 59.61 C ANISOU 5550 CH2 TRP B 247 10557 6215 5877 721 -113 1339 C ATOM 5551 N LEU B 248 48.565 11.623 133.679 1.00 65.30 N ANISOU 5551 N LEU B 248 11220 6312 7276 655 -425 1137 N ATOM 5552 CA LEU B 248 49.539 10.639 134.207 1.00 66.55 C ANISOU 5552 CA LEU B 248 11301 6300 7683 686 -488 1122 C ATOM 5553 C LEU B 248 50.857 10.470 133.417 1.00 67.46 C ANISOU 5553 C LEU B 248 11355 6330 7945 732 -400 948 C ATOM 5554 O LEU B 248 51.922 10.318 134.037 1.00 67.85 O ANISOU 5554 O LEU B 248 11334 6275 8169 775 -435 967 O ATOM 5555 CB LEU B 248 48.875 9.272 134.438 1.00 67.72 C ANISOU 5555 CB LEU B 248 11436 6338 7955 649 -594 1150 C ATOM 5556 CG LEU B 248 48.050 9.170 135.733 1.00 67.57 C ANISOU 5556 CG LEU B 248 11437 6348 7888 601 -722 1351 C ATOM 5557 CD1 LEU B 248 47.154 7.938 135.722 1.00 68.51 C ANISOU 5557 CD1 LEU B 248 11561 6392 8077 552 -812 1372 C ATOM 5558 CD2 LEU B 248 48.941 9.171 136.973 1.00 67.87 C ANISOU 5558 CD2 LEU B 248 11416 6321 8050 608 -812 1472 C ATOM 5559 N PRO B 249 50.800 10.490 132.069 1.00 68.12 N ANISOU 5559 N PRO B 249 11460 6462 7960 711 -286 778 N ATOM 5560 CA PRO B 249 52.029 10.412 131.262 1.00 69.55 C ANISOU 5560 CA PRO B 249 11580 6588 8257 736 -180 588 C ATOM 5561 C PRO B 249 53.121 11.436 131.630 1.00 69.59 C ANISOU 5561 C PRO B 249 11560 6625 8256 790 -137 615 C ATOM 5562 O PRO B 249 54.273 11.047 131.892 1.00 70.54 O ANISOU 5562 O PRO B 249 11593 6613 8594 838 -140 557 O ATOM 5563 CB PRO B 249 51.519 10.647 129.834 1.00 69.60 C ANISOU 5563 CB PRO B 249 11641 6722 8081 666 -64 447 C ATOM 5564 CG PRO B 249 50.141 10.084 129.851 1.00 69.26 C ANISOU 5564 CG PRO B 249 11653 6699 7964 616 -136 517 C ATOM 5565 CD PRO B 249 49.595 10.372 131.222 1.00 68.10 C ANISOU 5565 CD PRO B 249 11526 6553 7794 645 -259 743 C ATOM 5566 N LEU B 250 52.750 12.718 131.677 1.00 68.73 N ANISOU 5566 N LEU B 250 11518 6677 7918 782 -106 706 N ATOM 5567 CA LEU B 250 53.693 13.796 132.015 1.00 68.36 C ANISOU 5567 CA LEU B 250 11454 6674 7844 829 -64 738 C ATOM 5568 C LEU B 250 54.298 13.630 133.420 1.00 68.47 C ANISOU 5568 C LEU B 250 11414 6586 8013 878 -165 866 C ATOM 5569 O LEU B 250 55.451 14.017 133.654 1.00 68.20 O ANISOU 5569 O LEU B 250 11331 6516 8065 925 -136 846 O ATOM 5570 CB LEU B 250 53.019 15.166 131.886 1.00 67.36 C ANISOU 5570 CB LEU B 250 11399 6725 7467 807 -30 827 C ATOM 5571 CG LEU B 250 53.915 16.413 131.937 1.00 66.78 C ANISOU 5571 CG LEU B 250 11316 6720 7336 844 33 837 C ATOM 5572 CD1 LEU B 250 54.803 16.517 130.707 1.00 67.54 C ANISOU 5572 CD1 LEU B 250 11393 6837 7430 830 152 658 C ATOM 5573 CD2 LEU B 250 53.067 17.665 132.066 1.00 65.68 C ANISOU 5573 CD2 LEU B 250 11230 6724 7000 824 32 956 C ATOM 5574 N HIS B 251 53.520 13.059 134.343 1.00 68.94 N ANISOU 5574 N HIS B 251 11483 6608 8102 854 -286 1004 N ATOM 5575 CA HIS B 251 54.025 12.689 135.670 1.00 69.49 C ANISOU 5575 CA HIS B 251 11499 6580 8324 865 -406 1138 C ATOM 5576 C HIS B 251 54.992 11.515 135.583 1.00 71.04 C ANISOU 5576 C HIS B 251 11597 6574 8821 895 -447 1056 C ATOM 5577 O HIS B 251 56.117 11.604 136.095 1.00 71.48 O ANISOU 5577 O HIS B 251 11583 6549 9024 933 -471 1078 O ATOM 5578 CB HIS B 251 52.879 12.381 136.638 1.00 69.35 C ANISOU 5578 CB HIS B 251 11517 6594 8238 804 -525 1305 C ATOM 5579 CG HIS B 251 52.102 13.593 137.043 1.00 68.37 C ANISOU 5579 CG HIS B 251 11457 6647 7872 776 -495 1396 C ATOM 5580 ND1 HIS B 251 52.684 14.664 137.687 1.00 67.82 N ANISOU 5580 ND1 HIS B 251 11379 6648 7740 793 -470 1454 N ATOM 5581 CD2 HIS B 251 50.794 13.907 136.893 1.00 68.22 C ANISOU 5581 CD2 HIS B 251 11501 6738 7680 733 -486 1429 C ATOM 5582 CE1 HIS B 251 51.768 15.587 137.916 1.00 67.25 C ANISOU 5582 CE1 HIS B 251 11355 6718 7479 761 -441 1509 C ATOM 5583 NE2 HIS B 251 50.614 15.155 137.439 1.00 67.40 N ANISOU 5583 NE2 HIS B 251 11414 6759 7432 726 -452 1497 N ATOM 5584 N ILE B 252 54.583 10.442 134.902 1.00 71.92 N ANISOU 5584 N ILE B 252 11690 6596 9037 877 -451 952 N ATOM 5585 CA ILE B 252 55.483 9.295 134.696 1.00 73.87 C ANISOU 5585 CA ILE B 252 11824 6632 9610 906 -478 840 C ATOM 5586 C ILE B 252 56.828 9.780 134.125 1.00 74.27 C ANISOU 5586 C ILE B 252 11813 6658 9747 961 -359 686 C ATOM 5587 O ILE B 252 57.899 9.369 134.607 1.00 75.24 O ANISOU 5587 O ILE B 252 11831 6623 10132 1002 -414 690 O ATOM 5588 CB ILE B 252 54.858 8.200 133.790 1.00 75.03 C ANISOU 5588 CB ILE B 252 11959 6706 9840 876 -457 694 C ATOM 5589 CG1 ILE B 252 53.687 7.511 134.500 1.00 74.91 C ANISOU 5589 CG1 ILE B 252 11981 6673 9808 826 -601 858 C ATOM 5590 CG2 ILE B 252 55.898 7.144 133.397 1.00 76.91 C ANISOU 5590 CG2 ILE B 252 12058 6723 10438 910 -447 524 C ATOM 5591 CD1 ILE B 252 52.734 6.792 133.563 1.00 75.33 C ANISOU 5591 CD1 ILE B 252 12067 6731 9824 784 -562 738 C ATOM 5592 N LEU B 253 56.759 10.667 133.128 1.00 73.36 N ANISOU 5592 N LEU B 253 11760 6698 9413 954 -207 564 N ATOM 5593 CA LEU B 253 57.956 11.306 132.569 1.00 73.73 C ANISOU 5593 CA LEU B 253 11765 6762 9487 991 -85 427 C ATOM 5594 C LEU B 253 58.794 12.067 133.612 1.00 73.15 C ANISOU 5594 C LEU B 253 11667 6684 9440 1041 -135 570 C ATOM 5595 O LEU B 253 60.027 12.012 133.566 1.00 73.63 O ANISOU 5595 O LEU B 253 11639 6647 9689 1086 -101 484 O ATOM 5596 CB LEU B 253 57.586 12.244 131.412 1.00 73.31 C ANISOU 5596 CB LEU B 253 11797 6908 9149 948 61 321 C ATOM 5597 CG LEU B 253 57.165 11.601 130.089 1.00 74.45 C ANISOU 5597 CG LEU B 253 11947 7073 9267 881 157 115 C ATOM 5598 CD1 LEU B 253 56.559 12.663 129.185 1.00 73.67 C ANISOU 5598 CD1 LEU B 253 11950 7197 8842 815 252 100 C ATOM 5599 CD2 LEU B 253 58.337 10.901 129.410 1.00 76.21 C ANISOU 5599 CD2 LEU B 253 12053 7166 9737 891 252 -130 C ATOM 5600 N ASN B 254 58.135 12.771 134.537 1.00 72.18 N ANISOU 5600 N ASN B 254 11617 6669 9138 1025 -210 775 N ATOM 5601 CA ASN B 254 58.847 13.482 135.617 1.00 71.76 C ANISOU 5601 CA ASN B 254 11544 6626 9096 1054 -264 918 C ATOM 5602 C ASN B 254 59.487 12.530 136.620 1.00 72.92 C ANISOU 5602 C ASN B 254 11593 6584 9527 1061 -412 1018 C ATOM 5603 O ASN B 254 60.586 12.796 137.113 1.00 72.58 O ANISOU 5603 O ASN B 254 11487 6483 9607 1096 -431 1050 O ATOM 5604 CB ASN B 254 57.919 14.452 136.361 1.00 70.44 C ANISOU 5604 CB ASN B 254 11466 6625 8669 1017 -296 1089 C ATOM 5605 CG ASN B 254 57.545 15.660 135.528 1.00 69.17 C ANISOU 5605 CG ASN B 254 11380 6638 8260 1017 -166 1025 C ATOM 5606 OD1 ASN B 254 58.006 15.820 134.400 1.00 69.56 O ANISOU 5606 OD1 ASN B 254 11423 6703 8301 1033 -53 865 O ATOM 5607 ND2 ASN B 254 56.703 16.522 136.087 1.00 67.84 N ANISOU 5607 ND2 ASN B 254 11274 6603 7899 988 -183 1149 N ATOM 5608 N CYS B 255 58.788 11.435 136.921 1.00 74.25 N ANISOU 5608 N CYS B 255 11748 6660 9803 1022 -526 1078 N ATOM 5609 CA CYS B 255 59.318 10.389 137.797 1.00 75.98 C ANISOU 5609 CA CYS B 255 11863 6681 10322 1013 -691 1186 C ATOM 5610 C CYS B 255 60.517 9.680 137.167 1.00 77.89 C ANISOU 5610 C CYS B 255 11973 6723 10897 1074 -654 1010 C ATOM 5611 O CYS B 255 61.569 9.561 137.809 1.00 78.58 O ANISOU 5611 O CYS B 255 11966 6688 11202 1098 -732 1077 O ATOM 5612 CB CYS B 255 58.231 9.372 138.159 1.00 76.35 C ANISOU 5612 CB CYS B 255 11925 6678 10406 949 -820 1285 C ATOM 5613 SG CYS B 255 56.927 10.055 139.209 1.00 74.66 S ANISOU 5613 SG CYS B 255 11832 6673 9862 859 -893 1512 S ATOM 5614 N ILE B 256 60.372 9.233 135.917 1.00 78.90 N ANISOU 5614 N ILE B 256 12088 6821 11069 1089 -533 779 N ATOM 5615 CA ILE B 256 61.485 8.535 135.248 1.00 81.23 C ANISOU 5615 CA ILE B 256 12243 6925 11695 1137 -475 569 C ATOM 5616 C ILE B 256 62.705 9.436 135.006 1.00 81.35 C ANISOU 5616 C ILE B 256 12223 6976 11709 1189 -361 477 C ATOM 5617 O ILE B 256 63.825 8.950 135.082 1.00 82.62 O ANISOU 5617 O ILE B 256 12245 6952 12191 1232 -381 406 O ATOM 5618 CB ILE B 256 61.078 7.761 133.958 1.00 82.38 C ANISOU 5618 CB ILE B 256 12368 7031 11902 1120 -361 313 C ATOM 5619 CG1 ILE B 256 60.680 8.711 132.823 1.00 81.46 C ANISOU 5619 CG1 ILE B 256 12363 7144 11442 1094 -167 162 C ATOM 5620 CG2 ILE B 256 59.992 6.728 134.268 1.00 82.89 C ANISOU 5620 CG2 ILE B 256 12445 7021 12029 1075 -492 407 C ATOM 5621 CD1 ILE B 256 59.964 8.038 131.669 1.00 82.30 C ANISOU 5621 CD1 ILE B 256 12484 7267 11517 1041 -74 -38 C ATOM 5622 N THR B 257 62.502 10.730 134.757 1.00 80.79 N ANISOU 5622 N THR B 257 12266 7128 11300 1185 -253 488 N ATOM 5623 CA THR B 257 63.633 11.674 134.662 1.00 81.35 C ANISOU 5623 CA THR B 257 12313 7245 11351 1230 -161 436 C ATOM 5624 C THR B 257 64.336 11.876 136.013 1.00 81.97 C ANISOU 5624 C THR B 257 12343 7250 11551 1254 -304 650 C ATOM 5625 O THR B 257 65.572 11.929 136.067 1.00 82.96 O ANISOU 5625 O THR B 257 12368 7272 11878 1302 -286 592 O ATOM 5626 CB THR B 257 63.215 13.052 134.103 1.00 79.65 C ANISOU 5626 CB THR B 257 12227 7283 10754 1213 -28 417 C ATOM 5627 OG1 THR B 257 62.080 13.544 134.823 1.00 78.50 O ANISOU 5627 OG1 THR B 257 12191 7267 10368 1177 -110 624 O ATOM 5628 CG2 THR B 257 62.881 12.956 132.616 1.00 80.21 C ANISOU 5628 CG2 THR B 257 12324 7430 10719 1175 129 181 C ATOM 5629 N LEU B 258 63.550 11.982 137.088 1.00 81.92 N ANISOU 5629 N LEU B 258 12402 7304 11418 1208 -443 890 N ATOM 5630 CA LEU B 258 64.093 12.095 138.449 1.00 82.47 C ANISOU 5630 CA LEU B 258 12431 7323 11579 1195 -596 1114 C ATOM 5631 C LEU B 258 64.858 10.843 138.853 1.00 85.33 C ANISOU 5631 C LEU B 258 12639 7419 12361 1204 -740 1143 C ATOM 5632 O LEU B 258 66.035 10.921 139.193 1.00 86.19 O ANISOU 5632 O LEU B 258 12652 7424 12670 1240 -772 1161 O ATOM 5633 CB LEU B 258 62.981 12.357 139.476 1.00 81.15 C ANISOU 5633 CB LEU B 258 12361 7288 11181 1113 -708 1343 C ATOM 5634 CG LEU B 258 63.388 12.402 140.957 1.00 81.19 C ANISOU 5634 CG LEU B 258 12332 7271 11245 1056 -880 1590 C ATOM 5635 CD1 LEU B 258 64.434 13.480 141.195 1.00 80.74 C ANISOU 5635 CD1 LEU B 258 12264 7276 11136 1095 -815 1593 C ATOM 5636 CD2 LEU B 258 62.177 12.633 141.844 1.00 80.38 C ANISOU 5636 CD2 LEU B 258 12325 7322 10891 954 -961 1774 C ATOM 5637 N PHE B 259 64.179 9.698 138.817 1.00 87.59 N ANISOU 5637 N PHE B 259 12896 7591 12793 1171 -833 1156 N ATOM 5638 CA PHE B 259 64.766 8.439 139.300 1.00 90.70 C ANISOU 5638 CA PHE B 259 13134 7714 13612 1168 -1005 1220 C ATOM 5639 C PHE B 259 65.823 7.878 138.351 1.00 94.08 C ANISOU 5639 C PHE B 259 13414 7944 14388 1247 -908 959 C ATOM 5640 O PHE B 259 66.849 7.369 138.807 1.00 95.57 O ANISOU 5640 O PHE B 259 13453 7924 14934 1270 -1017 1004 O ATOM 5641 CB PHE B 259 63.681 7.387 139.567 1.00 90.76 C ANISOU 5641 CB PHE B 259 13152 7657 13676 1102 -1142 1318 C ATOM 5642 CG PHE B 259 62.646 7.819 140.576 1.00 88.91 C ANISOU 5642 CG PHE B 259 13043 7605 13130 1007 -1246 1570 C ATOM 5643 CD1 PHE B 259 63.025 8.308 141.826 1.00 88.39 C ANISOU 5643 CD1 PHE B 259 12981 7594 13008 948 -1373 1809 C ATOM 5644 CD2 PHE B 259 61.289 7.728 140.283 1.00 87.87 C ANISOU 5644 CD2 PHE B 259 13023 7598 12766 965 -1213 1560 C ATOM 5645 CE1 PHE B 259 62.074 8.708 142.753 1.00 87.28 C ANISOU 5645 CE1 PHE B 259 12947 7635 12578 842 -1452 2013 C ATOM 5646 CE2 PHE B 259 60.333 8.125 141.207 1.00 86.82 C ANISOU 5646 CE2 PHE B 259 12993 7634 12359 872 -1297 1769 C ATOM 5647 CZ PHE B 259 60.725 8.614 142.445 1.00 86.53 C ANISOU 5647 CZ PHE B 259 12954 7657 12264 806 -1411 1987 C ATOM 5648 N CYS B 260 65.571 7.978 137.044 1.00 96.35 N ANISOU 5648 N CYS B 260 13735 8300 14574 1274 -707 688 N ATOM 5649 CA CYS B 260 66.519 7.552 136.008 1.00 99.45 C ANISOU 5649 CA CYS B 260 13992 8545 15246 1330 -570 390 C ATOM 5650 C CYS B 260 66.945 8.731 135.103 1.00 98.96 C ANISOU 5650 C CYS B 260 13999 8679 14922 1355 -340 201 C ATOM 5651 O CYS B 260 66.401 8.905 134.010 1.00 97.86 O ANISOU 5651 O CYS B 260 13930 8669 14583 1331 -177 8 O ATOM 5652 CB CYS B 260 65.912 6.415 135.176 1.00101.70 C ANISOU 5652 CB CYS B 260 14227 8720 15692 1311 -534 200 C ATOM 5653 SG CYS B 260 67.082 5.671 134.017 1.00105.94 S ANISOU 5653 SG CYS B 260 14559 9041 16650 1359 -377 -187 S ATOM 5654 N PRO B 261 67.914 9.555 135.562 1.00 99.69 N ANISOU 5654 N PRO B 261 14072 8798 15005 1393 -335 270 N ATOM 5655 CA PRO B 261 68.467 10.597 134.680 1.00 99.75 C ANISOU 5655 CA PRO B 261 14121 8963 14815 1415 -124 83 C ATOM 5656 C PRO B 261 69.296 10.033 133.511 1.00102.33 C ANISOU 5656 C PRO B 261 14312 9168 15401 1435 34 -256 C ATOM 5657 O PRO B 261 69.473 10.713 132.498 1.00101.34 O ANISOU 5657 O PRO B 261 14232 9199 15072 1419 230 -455 O ATOM 5658 CB PRO B 261 69.344 11.429 135.626 1.00 98.92 C ANISOU 5658 CB PRO B 261 14007 8875 14703 1449 -191 261 C ATOM 5659 CG PRO B 261 69.735 10.485 136.709 1.00 99.92 C ANISOU 5659 CG PRO B 261 14008 8764 15191 1455 -412 440 C ATOM 5660 CD PRO B 261 68.570 9.556 136.886 1.00 99.99 C ANISOU 5660 CD PRO B 261 14046 8727 15218 1404 -524 521 C ATOM 5661 N SER B 262 69.799 8.808 133.669 1.00105.70 N ANISOU 5661 N SER B 262 14562 9318 16280 1459 -51 -322 N ATOM 5662 CA SER B 262 70.515 8.092 132.608 1.00108.47 C ANISOU 5662 CA SER B 262 14755 9522 16936 1470 95 -670 C ATOM 5663 C SER B 262 69.608 7.668 131.437 1.00109.14 C ANISOU 5663 C SER B 262 14892 9699 16877 1403 238 -902 C ATOM 5664 O SER B 262 70.074 7.590 130.297 1.00111.05 O ANISOU 5664 O SER B 262 15069 9961 17164 1376 439 -1226 O ATOM 5665 CB SER B 262 71.216 6.859 133.196 1.00110.81 C ANISOU 5665 CB SER B 262 14832 9470 17797 1513 -62 -654 C ATOM 5666 OG SER B 262 72.101 6.270 132.262 1.00113.22 O ANISOU 5666 OG SER B 262 14955 9617 18443 1530 88 -1005 O ATOM 5667 N CYS B 263 68.331 7.393 131.722 1.00107.97 N ANISOU 5667 N CYS B 263 14857 9613 16552 1364 138 -742 N ATOM 5668 CA CYS B 263 67.353 6.971 130.702 1.00107.82 C ANISOU 5668 CA CYS B 263 14898 9686 16379 1293 248 -924 C ATOM 5669 C CYS B 263 67.120 8.025 129.615 1.00107.07 C ANISOU 5669 C CYS B 263 14936 9883 15861 1231 460 -1075 C ATOM 5670 O CYS B 263 66.936 9.205 129.922 1.00105.70 O ANISOU 5670 O CYS B 263 14897 9906 15354 1233 458 -901 O ATOM 5671 CB CYS B 263 65.998 6.645 131.350 1.00106.23 C ANISOU 5671 CB CYS B 263 14811 9520 16030 1265 85 -676 C ATOM 5672 SG CYS B 263 65.953 5.172 132.399 1.00107.11 S ANISOU 5672 SG CYS B 263 14775 9302 16617 1293 -170 -514 S ATOM 5673 N HIS B 264 67.133 7.586 128.355 1.00108.78 N ANISOU 5673 N HIS B 264 15105 10125 16099 1162 639 -1399 N ATOM 5674 CA HIS B 264 66.733 8.421 127.215 1.00108.16 C ANISOU 5674 CA HIS B 264 15153 10332 15608 1064 825 -1539 C ATOM 5675 C HIS B 264 65.247 8.202 126.956 1.00106.74 C ANISOU 5675 C HIS B 264 15107 10272 15175 993 788 -1461 C ATOM 5676 O HIS B 264 64.769 7.071 127.015 1.00107.45 O ANISOU 5676 O HIS B 264 15137 10209 15481 989 722 -1504 O ATOM 5677 CB HIS B 264 67.544 8.065 125.958 1.00111.02 C ANISOU 5677 CB HIS B 264 15390 10683 16106 995 1048 -1944 C ATOM 5678 CG HIS B 264 67.178 8.869 124.746 1.00111.10 C ANISOU 5678 CG HIS B 264 15522 10995 15693 862 1231 -2087 C ATOM 5679 ND1 HIS B 264 67.533 10.193 124.593 1.00109.90 N ANISOU 5679 ND1 HIS B 264 15464 11052 15240 845 1295 -2012 N ATOM 5680 CD2 HIS B 264 66.496 8.530 123.626 1.00112.10 C ANISOU 5680 CD2 HIS B 264 15687 11252 15651 726 1355 -2291 C ATOM 5681 CE1 HIS B 264 67.079 10.637 123.434 1.00110.22 C ANISOU 5681 CE1 HIS B 264 15594 11336 14947 700 1439 -2150 C ATOM 5682 NE2 HIS B 264 66.447 9.647 122.827 1.00111.60 N ANISOU 5682 NE2 HIS B 264 15740 11475 15186 621 1480 -2320 N ATOM 5683 N LYS B 265 64.526 9.288 126.677 1.00104.58 N ANISOU 5683 N LYS B 265 15006 10264 14462 939 822 -1341 N ATOM 5684 CA LYS B 265 63.094 9.238 126.367 1.00103.57 C ANISOU 5684 CA LYS B 265 15012 10275 14063 864 792 -1259 C ATOM 5685 C LYS B 265 62.788 10.137 125.167 1.00102.74 C ANISOU 5685 C LYS B 265 15014 10449 13572 742 951 -1369 C ATOM 5686 O LYS B 265 62.963 11.354 125.263 1.00100.32 O ANISOU 5686 O LYS B 265 14787 10297 13030 747 965 -1244 O ATOM 5687 CB LYS B 265 62.264 9.663 127.580 1.00101.88 C ANISOU 5687 CB LYS B 265 14906 10084 13719 924 603 -902 C ATOM 5688 CG LYS B 265 62.032 8.533 128.573 1.00102.83 C ANISOU 5688 CG LYS B 265 14951 9969 14148 984 428 -781 C ATOM 5689 CD LYS B 265 60.932 7.574 128.119 1.00103.32 C ANISOU 5689 CD LYS B 265 15036 10010 14209 921 409 -844 C ATOM 5690 CE LYS B 265 61.175 6.165 128.641 1.00104.59 C ANISOU 5690 CE LYS B 265 15050 9882 14806 965 296 -873 C ATOM 5691 NZ LYS B 265 60.159 5.201 128.146 1.00105.29 N ANISOU 5691 NZ LYS B 265 15151 9942 14911 903 287 -956 N ATOM 5692 N PRO B 266 62.342 9.543 124.032 1.00104.40 N ANISOU 5692 N PRO B 266 15221 10724 13721 619 1065 -1600 N ATOM 5693 CA PRO B 266 62.078 10.289 122.795 1.00104.19 C ANISOU 5693 CA PRO B 266 15284 10968 13335 467 1212 -1716 C ATOM 5694 C PRO B 266 61.235 11.553 122.961 1.00101.15 C ANISOU 5694 C PRO B 266 15068 10798 12566 447 1140 -1437 C ATOM 5695 O PRO B 266 60.320 11.591 123.785 1.00 99.38 O ANISOU 5695 O PRO B 266 14917 10546 12296 509 989 -1189 O ATOM 5696 CB PRO B 266 61.329 9.271 121.932 1.00106.02 C ANISOU 5696 CB PRO B 266 15505 11208 13569 350 1271 -1912 C ATOM 5697 CG PRO B 266 61.896 7.964 122.343 1.00107.77 C ANISOU 5697 CG PRO B 266 15559 11139 14249 432 1250 -2064 C ATOM 5698 CD PRO B 266 62.190 8.087 123.813 1.00106.49 C ANISOU 5698 CD PRO B 266 15375 10801 14283 605 1069 -1789 C ATOM 5699 N SER B 267 61.549 12.566 122.158 1.00100.67 N ANISOU 5699 N SER B 267 15057 10948 12244 350 1249 -1487 N ATOM 5700 CA SER B 267 60.855 13.847 122.203 1.00 98.80 C ANISOU 5700 CA SER B 267 14958 10909 11669 321 1189 -1240 C ATOM 5701 C SER B 267 59.372 13.759 121.836 1.00 98.40 C ANISOU 5701 C SER B 267 15016 10972 11397 230 1127 -1132 C ATOM 5702 O SER B 267 58.581 14.498 122.399 1.00 97.23 O ANISOU 5702 O SER B 267 14959 10884 11099 269 1011 -871 O ATOM 5703 CB SER B 267 61.562 14.866 121.310 1.00 99.14 C ANISOU 5703 CB SER B 267 15018 11148 11502 214 1317 -1331 C ATOM 5704 OG SER B 267 62.897 15.057 121.744 1.00 99.31 O ANISOU 5704 OG SER B 267 14946 11067 11720 310 1364 -1401 O ATOM 5705 N ILE B 268 58.993 12.854 120.934 1.00100.14 N ANISOU 5705 N ILE B 268 15219 11215 11614 108 1202 -1337 N ATOM 5706 CA ILE B 268 57.575 12.717 120.535 1.00100.08 C ANISOU 5706 CA ILE B 268 15311 11316 11398 12 1142 -1240 C ATOM 5707 C ILE B 268 56.711 12.318 121.744 1.00 98.54 C ANISOU 5707 C ILE B 268 15143 10971 11323 150 969 -1012 C ATOM 5708 O ILE B 268 55.615 12.866 121.933 1.00 97.42 O ANISOU 5708 O ILE B 268 15103 10926 10985 135 871 -793 O ATOM 5709 CB ILE B 268 57.355 11.726 119.353 1.00102.16 C ANISOU 5709 CB ILE B 268 15543 11627 11646 -153 1261 -1523 C ATOM 5710 CG1 ILE B 268 58.165 12.160 118.133 1.00104.06 C ANISOU 5710 CG1 ILE B 268 15759 12050 11729 -324 1440 -1754 C ATOM 5711 CG2 ILE B 268 55.868 11.646 118.979 1.00101.44 C ANISOU 5711 CG2 ILE B 268 15560 11652 11329 -253 1186 -1397 C ATOM 5712 CD1 ILE B 268 58.099 11.220 116.948 1.00106.99 C ANISOU 5712 CD1 ILE B 268 16082 12484 12083 -511 1585 -2073 C ATOM 5713 N LEU B 269 57.227 11.402 122.568 1.00 98.34 N ANISOU 5713 N LEU B 269 15022 10713 11630 274 927 -1057 N ATOM 5714 CA LEU B 269 56.530 10.968 123.778 1.00 97.12 C ANISOU 5714 CA LEU B 269 14881 10415 11602 389 759 -843 C ATOM 5715 C LEU B 269 56.394 12.119 124.784 1.00 95.27 C ANISOU 5715 C LEU B 269 14712 10229 11256 479 656 -559 C ATOM 5716 O LEU B 269 55.358 12.244 125.437 1.00 94.05 O ANISOU 5716 O LEU B 269 14626 10088 11021 505 537 -352 O ATOM 5717 CB LEU B 269 57.233 9.763 124.418 1.00 98.00 C ANISOU 5717 CB LEU B 269 14860 10262 12110 485 725 -943 C ATOM 5718 CG LEU B 269 56.993 8.388 123.779 1.00 99.59 C ANISOU 5718 CG LEU B 269 14991 10359 12487 422 772 -1170 C ATOM 5719 CD1 LEU B 269 57.192 8.337 122.270 1.00101.18 C ANISOU 5719 CD1 LEU B 269 15182 10705 12553 263 961 -1463 C ATOM 5720 CD2 LEU B 269 57.895 7.369 124.459 1.00100.60 C ANISOU 5720 CD2 LEU B 269 14964 10208 13052 527 729 -1256 C ATOM 5721 N THR B 270 57.432 12.954 124.888 1.00 95.21 N ANISOU 5721 N THR B 270 14677 10251 11246 519 709 -566 N ATOM 5722 CA THR B 270 57.375 14.182 125.693 1.00 93.67 C ANISOU 5722 CA THR B 270 14539 10125 10925 585 638 -329 C ATOM 5723 C THR B 270 56.336 15.162 125.149 1.00 93.61 C ANISOU 5723 C THR B 270 14642 10324 10600 497 629 -205 C ATOM 5724 O THR B 270 55.565 15.735 125.913 1.00 91.85 O ANISOU 5724 O THR B 270 14474 10127 10296 541 526 12 O ATOM 5725 CB THR B 270 58.748 14.891 125.754 1.00 93.22 C ANISOU 5725 CB THR B 270 14427 10067 10922 631 712 -385 C ATOM 5726 OG1 THR B 270 59.724 14.004 126.311 1.00 94.08 O ANISOU 5726 OG1 THR B 270 14420 9969 11356 717 704 -483 O ATOM 5727 CG2 THR B 270 58.685 16.158 126.604 1.00 91.38 C ANISOU 5727 CG2 THR B 270 14247 9903 10570 698 641 -150 C ATOM 5728 N TYR B 271 56.328 15.338 123.830 1.00 96.75 N ANISOU 5728 N TYR B 271 15063 10866 10829 360 735 -347 N ATOM 5729 CA TYR B 271 55.452 16.302 123.160 1.00 98.26 C ANISOU 5729 CA TYR B 271 15347 11257 10728 252 722 -230 C ATOM 5730 C TYR B 271 53.974 15.893 123.190 1.00 96.12 C ANISOU 5730 C TYR B 271 15138 11003 10377 214 629 -118 C ATOM 5731 O TYR B 271 53.122 16.736 123.477 1.00 95.11 O ANISOU 5731 O TYR B 271 15070 10951 10114 216 544 86 O ATOM 5732 CB TYR B 271 55.925 16.587 121.717 1.00103.23 C ANISOU 5732 CB TYR B 271 15980 12053 11189 86 855 -407 C ATOM 5733 CG TYR B 271 56.910 17.747 121.599 1.00106.59 C ANISOU 5733 CG TYR B 271 16394 12563 11542 88 909 -388 C ATOM 5734 CD1 TYR B 271 56.476 19.065 121.732 1.00107.76 C ANISOU 5734 CD1 TYR B 271 16601 12823 11516 82 838 -166 C ATOM 5735 CD2 TYR B 271 58.269 17.529 121.343 1.00110.10 C ANISOU 5735 CD2 TYR B 271 16757 12967 12106 94 1030 -597 C ATOM 5736 CE1 TYR B 271 57.362 20.129 121.622 1.00110.25 C ANISOU 5736 CE1 TYR B 271 16904 13213 11772 82 882 -142 C ATOM 5737 CE2 TYR B 271 59.163 18.591 121.231 1.00112.05 C ANISOU 5737 CE2 TYR B 271 16996 13296 12282 93 1079 -578 C ATOM 5738 CZ TYR B 271 58.708 19.892 121.377 1.00113.45 C ANISOU 5738 CZ TYR B 271 17240 13587 12277 88 1002 -345 C ATOM 5739 OH TYR B 271 59.579 20.963 121.262 1.00120.40 O ANISOU 5739 OH TYR B 271 18110 14546 13091 84 1044 -318 O ATOM 5740 N ILE B 272 53.664 14.623 122.910 1.00 95.30 N ANISOU 5740 N ILE B 272 15014 10823 10373 180 643 -256 N ATOM 5741 CA ILE B 272 52.257 14.152 122.990 1.00 93.77 C ANISOU 5741 CA ILE B 272 14877 10633 10117 148 551 -151 C ATOM 5742 C ILE B 272 51.700 14.205 124.422 1.00 90.98 C ANISOU 5742 C ILE B 272 14533 10171 9864 284 414 65 C ATOM 5743 O ILE B 272 50.514 14.501 124.624 1.00 90.16 O ANISOU 5743 O ILE B 272 14490 10123 9643 265 330 226 O ATOM 5744 CB ILE B 272 52.032 12.736 122.384 1.00 95.60 C ANISOU 5744 CB ILE B 272 15079 10799 10442 79 596 -353 C ATOM 5745 CG1 ILE B 272 52.728 11.637 123.208 1.00 96.16 C ANISOU 5745 CG1 ILE B 272 15055 10638 10843 201 580 -445 C ATOM 5746 CG2 ILE B 272 52.441 12.702 120.911 1.00 97.35 C ANISOU 5746 CG2 ILE B 272 15296 11164 10528 -92 740 -580 C ATOM 5747 CD1 ILE B 272 52.705 10.268 122.561 1.00 97.79 C ANISOU 5747 CD1 ILE B 272 15205 10760 11188 136 641 -680 C ATOM 5748 N ALA B 273 52.559 13.922 125.403 1.00 89.50 N ANISOU 5748 N ALA B 273 14280 9833 9891 405 393 65 N ATOM 5749 CA ALA B 273 52.207 14.074 126.818 1.00 87.60 C ANISOU 5749 CA ALA B 273 14042 9511 9729 511 272 267 C ATOM 5750 C ALA B 273 51.821 15.515 127.137 1.00 85.39 C ANISOU 5750 C ALA B 273 13812 9356 9273 521 242 448 C ATOM 5751 O ALA B 273 50.822 15.751 127.804 1.00 85.39 O ANISOU 5751 O ALA B 273 13848 9372 9222 536 154 608 O ATOM 5752 CB ALA B 273 53.357 13.628 127.710 1.00 87.74 C ANISOU 5752 CB ALA B 273 13975 9364 9996 614 256 238 C ATOM 5753 N ILE B 274 52.610 16.466 126.641 1.00 83.87 N ANISOU 5753 N ILE B 274 13615 9250 9000 507 319 411 N ATOM 5754 CA ILE B 274 52.345 17.897 126.834 1.00 81.88 C ANISOU 5754 CA ILE B 274 13396 9109 8604 512 296 567 C ATOM 5755 C ILE B 274 51.111 18.358 126.049 1.00 81.00 C ANISOU 5755 C ILE B 274 13347 9130 8299 407 268 645 C ATOM 5756 O ILE B 274 50.323 19.155 126.559 1.00 80.71 O ANISOU 5756 O ILE B 274 13329 9130 8205 426 199 811 O ATOM 5757 CB ILE B 274 53.599 18.744 126.499 1.00 82.03 C ANISOU 5757 CB ILE B 274 13387 9176 8604 521 381 506 C ATOM 5758 CG1 ILE B 274 54.673 18.484 127.560 1.00 81.93 C ANISOU 5758 CG1 ILE B 274 13311 9027 8792 640 377 490 C ATOM 5759 CG2 ILE B 274 53.286 20.237 126.440 1.00 81.15 C ANISOU 5759 CG2 ILE B 274 13304 9186 8341 503 361 654 C ATOM 5760 CD1 ILE B 274 56.076 18.862 127.152 1.00 82.60 C ANISOU 5760 CD1 ILE B 274 13350 9119 8913 651 475 369 C ATOM 5761 N PHE B 275 50.941 17.860 124.825 1.00 80.85 N ANISOU 5761 N PHE B 275 13350 9179 8189 288 321 522 N ATOM 5762 CA PHE B 275 49.720 18.131 124.056 1.00 80.04 C ANISOU 5762 CA PHE B 275 13303 9194 7911 172 279 602 C ATOM 5763 C PHE B 275 48.468 17.566 124.742 1.00 78.13 C ANISOU 5763 C PHE B 275 13083 8889 7712 206 180 708 C ATOM 5764 O PHE B 275 47.410 18.192 124.694 1.00 77.25 O ANISOU 5764 O PHE B 275 13002 8845 7502 169 110 854 O ATOM 5765 CB PHE B 275 49.816 17.592 122.619 1.00 82.14 C ANISOU 5765 CB PHE B 275 13588 9557 8063 14 359 434 C ATOM 5766 CG PHE B 275 50.770 18.355 121.723 1.00 83.53 C ANISOU 5766 CG PHE B 275 13756 9855 8126 -73 450 356 C ATOM 5767 CD1 PHE B 275 50.750 19.752 121.654 1.00 83.11 C ANISOU 5767 CD1 PHE B 275 13715 9898 7962 -91 413 516 C ATOM 5768 CD2 PHE B 275 51.662 17.669 120.899 1.00 85.49 C ANISOU 5768 CD2 PHE B 275 13974 10123 8382 -154 573 116 C ATOM 5769 CE1 PHE B 275 51.621 20.439 120.816 1.00 83.82 C ANISOU 5769 CE1 PHE B 275 13798 10107 7941 -187 488 454 C ATOM 5770 CE2 PHE B 275 52.533 18.354 120.059 1.00 86.30 C ANISOU 5770 CE2 PHE B 275 14068 10354 8366 -255 662 36 C ATOM 5771 CZ PHE B 275 52.513 19.740 120.018 1.00 85.31 C ANISOU 5771 CZ PHE B 275 13965 10330 8117 -273 615 214 C ATOM 5772 N LEU B 276 48.588 16.394 125.369 1.00 76.90 N ANISOU 5772 N LEU B 276 12903 8599 7713 271 168 637 N ATOM 5773 CA LEU B 276 47.472 15.801 126.131 1.00 75.35 C ANISOU 5773 CA LEU B 276 12724 8338 7566 303 71 739 C ATOM 5774 C LEU B 276 46.997 16.671 127.301 1.00 73.40 C ANISOU 5774 C LEU B 276 12474 8088 7328 379 -4 926 C ATOM 5775 O LEU B 276 45.787 16.811 127.526 1.00 72.92 O ANISOU 5775 O LEU B 276 12438 8056 7212 356 -73 1039 O ATOM 5776 CB LEU B 276 47.834 14.399 126.650 1.00 75.69 C ANISOU 5776 CB LEU B 276 12731 8227 7801 355 60 641 C ATOM 5777 CG LEU B 276 47.578 13.241 125.679 1.00 76.96 C ANISOU 5777 CG LEU B 276 12898 8372 7969 269 98 481 C ATOM 5778 CD1 LEU B 276 48.370 12.004 126.083 1.00 77.68 C ANISOU 5778 CD1 LEU B 276 12920 8290 8302 328 108 349 C ATOM 5779 CD2 LEU B 276 46.091 12.927 125.577 1.00 76.73 C ANISOU 5779 CD2 LEU B 276 12923 8383 7847 211 22 574 C ATOM 5780 N THR B 277 47.950 17.252 128.032 1.00 72.13 N ANISOU 5780 N THR B 277 12274 7891 7238 461 14 945 N ATOM 5781 CA THR B 277 47.648 18.073 129.211 1.00 70.33 C ANISOU 5781 CA THR B 277 12030 7662 7029 524 -39 1093 C ATOM 5782 C THR B 277 46.955 19.374 128.845 1.00 70.30 C ANISOU 5782 C THR B 277 12039 7769 6903 485 -49 1196 C ATOM 5783 O THR B 277 45.970 19.747 129.482 1.00 70.15 O ANISOU 5783 O THR B 277 12014 7759 6878 492 -108 1307 O ATOM 5784 CB THR B 277 48.910 18.420 130.019 1.00 69.40 C ANISOU 5784 CB THR B 277 11867 7490 7011 608 -11 1083 C ATOM 5785 OG1 THR B 277 49.853 19.113 129.189 1.00 68.92 O ANISOU 5785 OG1 THR B 277 11799 7486 6902 597 70 1011 O ATOM 5786 CG2 THR B 277 49.532 17.156 130.599 1.00 69.79 C ANISOU 5786 CG2 THR B 277 11886 7406 7224 650 -31 1018 C ATOM 5787 N HIS B 278 47.476 20.064 127.831 1.00 71.07 N ANISOU 5787 N HIS B 278 12141 7945 6914 437 4 1160 N ATOM 5788 CA HIS B 278 46.824 21.270 127.300 1.00 71.03 C ANISOU 5788 CA HIS B 278 12140 8039 6808 381 -22 1269 C ATOM 5789 C HIS B 278 45.489 20.912 126.644 1.00 70.89 C ANISOU 5789 C HIS B 278 12157 8065 6711 288 -81 1316 C ATOM 5790 O HIS B 278 44.508 21.641 126.786 1.00 69.99 O ANISOU 5790 O HIS B 278 12030 7979 6584 272 -144 1443 O ATOM 5791 CB HIS B 278 47.730 22.008 126.305 1.00 72.31 C ANISOU 5791 CB HIS B 278 12301 8283 6887 326 37 1227 C ATOM 5792 CG HIS B 278 49.020 22.480 126.902 1.00 73.04 C ANISOU 5792 CG HIS B 278 12357 8339 7054 415 92 1189 C ATOM 5793 ND1 HIS B 278 50.212 22.470 126.209 1.00 74.20 N ANISOU 5793 ND1 HIS B 278 12502 8517 7174 389 175 1073 N ATOM 5794 CD2 HIS B 278 49.309 22.956 128.137 1.00 72.98 C ANISOU 5794 CD2 HIS B 278 12311 8271 7145 519 80 1246 C ATOM 5795 CE1 HIS B 278 51.176 22.929 126.988 1.00 74.01 C ANISOU 5795 CE1 HIS B 278 12439 8444 7235 484 204 1070 C ATOM 5796 NE2 HIS B 278 50.654 23.231 128.163 1.00 73.22 N ANISOU 5796 NE2 HIS B 278 12319 8292 7208 561 146 1176 N ATOM 5797 N GLY B 279 45.469 19.786 125.931 1.00 71.52 N ANISOU 5797 N GLY B 279 12274 8145 6754 226 -57 1207 N ATOM 5798 CA GLY B 279 44.254 19.241 125.326 1.00 71.94 C ANISOU 5798 CA GLY B 279 12365 8234 6734 135 -109 1235 C ATOM 5799 C GLY B 279 43.144 18.915 126.314 1.00 71.23 C ANISOU 5799 C GLY B 279 12269 8078 6714 187 -186 1327 C ATOM 5800 O GLY B 279 41.960 19.103 126.002 1.00 71.65 O ANISOU 5800 O GLY B 279 12335 8174 6713 126 -249 1418 O ATOM 5801 N ASN B 280 43.515 18.450 127.509 1.00 70.43 N ANISOU 5801 N ASN B 280 12145 7881 6734 288 -186 1309 N ATOM 5802 CA ASN B 280 42.542 18.172 128.584 1.00 69.65 C ANISOU 5802 CA ASN B 280 12035 7732 6694 325 -254 1393 C ATOM 5803 C ASN B 280 41.607 19.355 128.894 1.00 69.05 C ANISOU 5803 C ASN B 280 11928 7705 6600 320 -299 1525 C ATOM 5804 O ASN B 280 40.452 19.149 129.270 1.00 68.42 O ANISOU 5804 O ASN B 280 11846 7618 6529 302 -355 1588 O ATOM 5805 CB ASN B 280 43.263 17.729 129.865 1.00 69.12 C ANISOU 5805 CB ASN B 280 11939 7575 6746 413 -251 1375 C ATOM 5806 CG ASN B 280 42.312 17.176 130.913 1.00 68.49 C ANISOU 5806 CG ASN B 280 11854 7455 6711 420 -321 1444 C ATOM 5807 OD1 ASN B 280 42.143 17.760 131.981 1.00 67.87 O ANISOU 5807 OD1 ASN B 280 11740 7381 6663 451 -338 1514 O ATOM 5808 ND2 ASN B 280 41.672 16.052 130.603 1.00 68.63 N ANISOU 5808 ND2 ASN B 280 11905 7442 6728 379 -357 1417 N ATOM 5809 N SER B 281 42.097 20.582 128.721 1.00 69.78 N ANISOU 5809 N SER B 281 11989 7839 6682 332 -274 1562 N ATOM 5810 CA SER B 281 41.263 21.784 128.866 1.00 70.34 C ANISOU 5810 CA SER B 281 12011 7942 6770 322 -316 1678 C ATOM 5811 C SER B 281 40.128 21.900 127.829 1.00 71.61 C ANISOU 5811 C SER B 281 12187 8155 6864 222 -380 1751 C ATOM 5812 O SER B 281 39.155 22.615 128.070 1.00 71.70 O ANISOU 5812 O SER B 281 12147 8165 6927 213 -434 1847 O ATOM 5813 CB SER B 281 42.126 23.052 128.831 1.00 69.92 C ANISOU 5813 CB SER B 281 11914 7913 6736 353 -281 1700 C ATOM 5814 OG SER B 281 43.066 23.079 129.895 1.00 68.90 O ANISOU 5814 OG SER B 281 11762 7738 6675 441 -231 1652 O ATOM 5815 N ALA B 282 40.253 21.214 126.691 1.00 73.03 N ANISOU 5815 N ALA B 282 12427 8380 6940 138 -373 1699 N ATOM 5816 CA ALA B 282 39.200 21.188 125.661 1.00 74.28 C ANISOU 5816 CA ALA B 282 12608 8599 7016 21 -439 1770 C ATOM 5817 C ALA B 282 38.100 20.133 125.876 1.00 74.47 C ANISOU 5817 C ALA B 282 12660 8590 7043 3 -483 1767 C ATOM 5818 O ALA B 282 37.003 20.273 125.338 1.00 74.64 O ANISOU 5818 O ALA B 282 12681 8645 7031 -75 -555 1856 O ATOM 5819 CB ALA B 282 39.827 20.997 124.285 1.00 75.51 C ANISOU 5819 CB ALA B 282 12813 8843 7032 -92 -406 1709 C ATOM 5820 N MET B 283 38.382 19.094 126.660 1.00 74.56 N ANISOU 5820 N MET B 283 12691 8535 7104 70 -451 1678 N ATOM 5821 CA MET B 283 37.527 17.891 126.706 1.00 74.90 C ANISOU 5821 CA MET B 283 12771 8548 7137 41 -486 1655 C ATOM 5822 C MET B 283 36.208 18.113 127.462 1.00 75.12 C ANISOU 5822 C MET B 283 12764 8555 7223 54 -555 1759 C ATOM 5823 O MET B 283 35.119 17.785 126.945 1.00 76.53 O ANISOU 5823 O MET B 283 12962 8756 7359 -16 -612 1805 O ATOM 5824 CB MET B 283 38.294 16.710 127.321 1.00 74.12 C ANISOU 5824 CB MET B 283 12691 8370 7099 102 -444 1539 C ATOM 5825 CG MET B 283 39.596 16.367 126.600 1.00 74.46 C ANISOU 5825 CG MET B 283 12754 8418 7119 91 -367 1408 C ATOM 5826 SD MET B 283 40.393 14.892 127.240 1.00 74.76 S ANISOU 5826 SD MET B 283 12791 8333 7280 155 -339 1278 S ATOM 5827 CE MET B 283 41.971 14.955 126.393 1.00 74.99 C ANISOU 5827 CE MET B 283 12812 8377 7303 146 -233 1124 C ATOM 5828 N ASN B 284 36.312 18.685 128.664 1.00 74.26 N ANISOU 5828 N ASN B 284 12599 8408 7207 135 -545 1787 N ATOM 5829 CA ASN B 284 35.159 18.856 129.570 1.00 73.93 C ANISOU 5829 CA ASN B 284 12509 8347 7232 145 -589 1852 C ATOM 5830 C ASN B 284 33.898 19.446 128.891 1.00 74.22 C ANISOU 5830 C ASN B 284 12517 8415 7267 77 -656 1949 C ATOM 5831 O ASN B 284 32.831 18.797 128.912 1.00 74.66 O ANISOU 5831 O ASN B 284 12585 8464 7315 38 -704 1973 O ATOM 5832 CB ASN B 284 35.555 19.634 130.844 1.00 73.70 C ANISOU 5832 CB ASN B 284 12411 8297 7293 217 -553 1854 C ATOM 5833 CG ASN B 284 36.363 18.794 131.826 1.00 73.64 C ANISOU 5833 CG ASN B 284 12425 8251 7301 263 -522 1790 C ATOM 5834 OD1 ASN B 284 36.381 17.564 131.749 1.00 73.44 O ANISOU 5834 OD1 ASN B 284 12455 8196 7253 248 -541 1753 O ATOM 5835 ND2 ASN B 284 37.037 19.462 132.759 1.00 73.61 N ANISOU 5835 ND2 ASN B 284 12374 8244 7350 313 -481 1781 N ATOM 5836 N PRO B 285 34.019 20.634 128.249 1.00 73.98 N ANISOU 5836 N PRO B 285 12443 8415 7250 55 -670 2015 N ATOM 5837 CA PRO B 285 32.892 21.168 127.469 1.00 74.49 C ANISOU 5837 CA PRO B 285 12474 8501 7326 -23 -754 2126 C ATOM 5838 C PRO B 285 32.313 20.183 126.456 1.00 75.14 C ANISOU 5838 C PRO B 285 12634 8623 7290 -121 -800 2133 C ATOM 5839 O PRO B 285 31.090 20.109 126.320 1.00 74.86 O ANISOU 5839 O PRO B 285 12578 8582 7282 -169 -871 2206 O ATOM 5840 CB PRO B 285 33.505 22.365 126.734 1.00 75.00 C ANISOU 5840 CB PRO B 285 12503 8599 7394 -49 -764 2189 C ATOM 5841 CG PRO B 285 34.627 22.801 127.604 1.00 74.32 C ANISOU 5841 CG PRO B 285 12391 8487 7360 49 -682 2119 C ATOM 5842 CD PRO B 285 35.180 21.547 128.206 1.00 73.71 C ANISOU 5842 CD PRO B 285 12383 8391 7230 96 -621 2002 C ATOM 5843 N ILE B 286 33.180 19.432 125.771 1.00 75.90 N ANISOU 5843 N ILE B 286 12813 8757 7267 -155 -755 2047 N ATOM 5844 CA ILE B 286 32.732 18.471 124.754 1.00 77.18 C ANISOU 5844 CA ILE B 286 13049 8965 7308 -262 -783 2027 C ATOM 5845 C ILE B 286 31.996 17.300 125.404 1.00 77.25 C ANISOU 5845 C ILE B 286 13084 8922 7344 -235 -795 1985 C ATOM 5846 O ILE B 286 30.922 16.921 124.931 1.00 77.88 O ANISOU 5846 O ILE B 286 13181 9020 7387 -310 -859 2037 O ATOM 5847 CB ILE B 286 33.892 17.965 123.856 1.00 77.84 C ANISOU 5847 CB ILE B 286 13198 9104 7271 -316 -713 1912 C ATOM 5848 CG1 ILE B 286 34.462 19.123 123.030 1.00 78.50 C ANISOU 5848 CG1 ILE B 286 13262 9264 7300 -382 -718 1974 C ATOM 5849 CG2 ILE B 286 33.419 16.848 122.923 1.00 78.71 C ANISOU 5849 CG2 ILE B 286 13379 9260 7266 -431 -725 1857 C ATOM 5850 CD1 ILE B 286 35.785 18.820 122.355 1.00 79.24 C ANISOU 5850 CD1 ILE B 286 13401 9413 7294 -421 -627 1842 C ATOM 5851 N VAL B 287 32.563 16.736 126.474 1.00 76.83 N ANISOU 5851 N VAL B 287 13032 8805 7353 -138 -743 1903 N ATOM 5852 CA VAL B 287 31.894 15.624 127.185 1.00 76.88 C ANISOU 5852 CA VAL B 287 13059 8760 7390 -119 -765 1877 C ATOM 5853 C VAL B 287 30.573 16.054 127.862 1.00 76.79 C ANISOU 5853 C VAL B 287 12991 8738 7448 -117 -824 1974 C ATOM 5854 O VAL B 287 29.592 15.284 127.848 1.00 77.38 O ANISOU 5854 O VAL B 287 13087 8804 7507 -158 -870 1990 O ATOM 5855 CB VAL B 287 32.839 14.854 128.155 1.00 76.24 C ANISOU 5855 CB VAL B 287 12988 8612 7365 -38 -715 1785 C ATOM 5856 CG1 VAL B 287 33.358 15.728 129.278 1.00 75.38 C ANISOU 5856 CG1 VAL B 287 12818 8485 7337 42 -686 1808 C ATOM 5857 CG2 VAL B 287 32.149 13.618 128.730 1.00 76.42 C ANISOU 5857 CG2 VAL B 287 13036 8586 7412 -44 -755 1772 C ATOM 5858 N TYR B 288 30.530 17.276 128.411 1.00 76.49 N ANISOU 5858 N TYR B 288 12870 8697 7493 -76 -819 2028 N ATOM 5859 CA TYR B 288 29.259 17.819 128.937 1.00 76.58 C ANISOU 5859 CA TYR B 288 12805 8696 7596 -84 -866 2103 C ATOM 5860 C TYR B 288 28.172 17.853 127.856 1.00 77.77 C ANISOU 5860 C TYR B 288 12959 8872 7715 -176 -949 2190 C ATOM 5861 O TYR B 288 27.034 17.446 128.099 1.00 77.40 O ANISOU 5861 O TYR B 288 12899 8812 7698 -203 -994 2220 O ATOM 5862 CB TYR B 288 29.414 19.237 129.517 1.00 76.34 C ANISOU 5862 CB TYR B 288 12667 8653 7684 -36 -842 2133 C ATOM 5863 CG TYR B 288 30.344 19.381 130.709 1.00 75.99 C ANISOU 5863 CG TYR B 288 12601 8592 7677 40 -765 2058 C ATOM 5864 CD1 TYR B 288 30.363 18.440 131.741 1.00 75.38 C ANISOU 5864 CD1 TYR B 288 12551 8503 7585 57 -742 2002 C ATOM 5865 CD2 TYR B 288 31.189 20.487 130.821 1.00 76.21 C ANISOU 5865 CD2 TYR B 288 12577 8620 7757 85 -723 2056 C ATOM 5866 CE1 TYR B 288 31.213 18.582 132.825 1.00 74.65 C ANISOU 5866 CE1 TYR B 288 12437 8406 7520 106 -684 1950 C ATOM 5867 CE2 TYR B 288 32.041 20.637 131.904 1.00 75.48 C ANISOU 5867 CE2 TYR B 288 12465 8520 7694 146 -654 1992 C ATOM 5868 CZ TYR B 288 32.051 19.678 132.902 1.00 74.90 C ANISOU 5868 CZ TYR B 288 12420 8441 7595 151 -637 1942 C ATOM 5869 OH TYR B 288 32.892 19.825 133.975 1.00 75.40 O ANISOU 5869 OH TYR B 288 12463 8506 7678 190 -582 1894 O ATOM 5870 N ALA B 289 28.535 18.337 126.670 1.00 79.32 N ANISOU 5870 N ALA B 289 13175 9113 7850 -236 -972 2237 N ATOM 5871 CA ALA B 289 27.602 18.450 125.546 1.00 80.98 C ANISOU 5871 CA ALA B 289 13389 9360 8017 -348 -1065 2341 C ATOM 5872 C ALA B 289 27.070 17.089 125.102 1.00 82.11 C ANISOU 5872 C ALA B 289 13621 9525 8051 -412 -1084 2302 C ATOM 5873 O ALA B 289 25.871 16.936 124.861 1.00 82.63 O ANISOU 5873 O ALA B 289 13671 9590 8132 -470 -1160 2377 O ATOM 5874 CB ALA B 289 28.266 19.158 124.376 1.00 81.47 C ANISOU 5874 CB ALA B 289 13464 9487 8004 -424 -1084 2395 C ATOM 5875 N PHE B 290 27.966 16.111 124.995 1.00 83.14 N ANISOU 5875 N PHE B 290 13834 9665 8089 -402 -1017 2180 N ATOM 5876 CA PHE B 290 27.583 14.747 124.622 1.00 84.86 C ANISOU 5876 CA PHE B 290 14130 9889 8222 -456 -1025 2119 C ATOM 5877 C PHE B 290 26.756 14.044 125.703 1.00 85.96 C ANISOU 5877 C PHE B 290 14257 9966 8437 -402 -1043 2113 C ATOM 5878 O PHE B 290 25.712 13.464 125.391 1.00 86.43 O ANISOU 5878 O PHE B 290 14337 10032 8468 -464 -1101 2149 O ATOM 5879 CB PHE B 290 28.812 13.897 124.261 1.00 85.03 C ANISOU 5879 CB PHE B 290 14220 9917 8168 -455 -943 1973 C ATOM 5880 CG PHE B 290 29.250 14.039 122.828 1.00 85.77 C ANISOU 5880 CG PHE B 290 14356 10105 8126 -578 -932 1952 C ATOM 5881 CD1 PHE B 290 28.454 13.554 121.797 1.00 86.58 C ANISOU 5881 CD1 PHE B 290 14503 10274 8119 -716 -982 1977 C ATOM 5882 CD2 PHE B 290 30.463 14.648 122.507 1.00 85.76 C ANISOU 5882 CD2 PHE B 290 14350 10139 8095 -572 -869 1906 C ATOM 5883 CE1 PHE B 290 28.854 13.678 120.472 1.00 87.82 C ANISOU 5883 CE1 PHE B 290 14699 10541 8127 -861 -969 1955 C ATOM 5884 CE2 PHE B 290 30.867 14.775 121.186 1.00 86.78 C ANISOU 5884 CE2 PHE B 290 14516 10374 8081 -710 -854 1881 C ATOM 5885 CZ PHE B 290 30.061 14.289 120.166 1.00 87.93 C ANISOU 5885 CZ PHE B 290 14705 10596 8106 -863 -903 1905 C ATOM 5886 N ARG B 291 27.208 14.103 126.960 1.00 86.77 N ANISOU 5886 N ARG B 291 14324 10015 8627 -301 -998 2073 N ATOM 5887 CA ARG B 291 26.573 13.311 128.033 1.00 87.53 C ANISOU 5887 CA ARG B 291 14415 10067 8773 -270 -1012 2059 C ATOM 5888 C ARG B 291 25.478 14.030 128.833 1.00 89.10 C ANISOU 5888 C ARG B 291 14527 10260 9066 -261 -1044 2133 C ATOM 5889 O ARG B 291 24.398 13.467 129.040 1.00 89.46 O ANISOU 5889 O ARG B 291 14573 10299 9118 -297 -1089 2159 O ATOM 5890 CB ARG B 291 27.634 12.750 128.981 1.00 86.77 C ANISOU 5890 CB ARG B 291 14333 9925 8708 -197 -958 1976 C ATOM 5891 CG ARG B 291 28.551 11.740 128.314 1.00 87.08 C ANISOU 5891 CG ARG B 291 14445 9944 8696 -207 -930 1881 C ATOM 5892 CD ARG B 291 29.431 11.036 129.321 1.00 86.92 C ANISOU 5892 CD ARG B 291 14426 9856 8742 -142 -904 1820 C ATOM 5893 NE ARG B 291 28.669 10.142 130.194 1.00 87.15 N ANISOU 5893 NE ARG B 291 14458 9848 8806 -152 -956 1847 N ATOM 5894 CZ ARG B 291 28.236 8.925 129.867 1.00 87.83 C ANISOU 5894 CZ ARG B 291 14590 9899 8881 -193 -996 1819 C ATOM 5895 NH1 ARG B 291 28.454 8.410 128.655 1.00 89.13 N ANISOU 5895 NH1 ARG B 291 14801 10064 8998 -233 -980 1748 N ATOM 5896 NH2 ARG B 291 27.565 8.207 130.771 1.00 87.49 N ANISOU 5896 NH2 ARG B 291 14542 9826 8872 -206 -1049 1859 N ATOM 5897 N ILE B 292 25.755 15.255 129.283 1.00 90.76 N ANISOU 5897 N ILE B 292 14655 10469 9358 -217 -1015 2155 N ATOM 5898 CA ILE B 292 24.826 15.992 130.157 1.00 92.12 C ANISOU 5898 CA ILE B 292 14721 10629 9650 -206 -1023 2189 C ATOM 5899 C ILE B 292 23.755 16.723 129.338 1.00 95.24 C ANISOU 5899 C ILE B 292 15055 11024 10105 -261 -1096 2288 C ATOM 5900 O ILE B 292 24.053 17.674 128.613 1.00 94.69 O ANISOU 5900 O ILE B 292 14950 10959 10065 -270 -1116 2345 O ATOM 5901 CB ILE B 292 25.552 16.981 131.102 1.00 90.84 C ANISOU 5901 CB ILE B 292 14481 10459 9574 -140 -954 2152 C ATOM 5902 CG1 ILE B 292 26.647 16.250 131.894 1.00 89.84 C ANISOU 5902 CG1 ILE B 292 14412 10331 9390 -99 -898 2075 C ATOM 5903 CG2 ILE B 292 24.549 17.633 132.056 1.00 90.79 C ANISOU 5903 CG2 ILE B 292 14355 10443 9698 -145 -945 2152 C ATOM 5904 CD1 ILE B 292 27.353 17.085 132.941 1.00 89.21 C ANISOU 5904 CD1 ILE B 292 14263 10254 9376 -48 -830 2034 C ATOM 5905 N GLN B 293 22.513 16.258 129.486 1.00 99.76 N ANISOU 5905 N GLN B 293 15610 11589 10702 -303 -1144 2316 N ATOM 5906 CA GLN B 293 21.325 16.796 128.786 1.00103.14 C ANISOU 5906 CA GLN B 293 15972 12005 11208 -363 -1229 2418 C ATOM 5907 C GLN B 293 21.065 18.305 128.932 1.00103.41 C ANISOU 5907 C GLN B 293 15859 12001 11430 -342 -1241 2469 C ATOM 5908 O GLN B 293 20.699 18.966 127.960 1.00104.87 O ANISOU 5908 O GLN B 293 16003 12175 11666 -391 -1323 2580 O ATOM 5909 CB GLN B 293 20.071 16.024 129.241 1.00105.54 C ANISOU 5909 CB GLN B 293 16269 12302 11530 -397 -1261 2416 C ATOM 5910 CG GLN B 293 19.738 16.157 130.739 1.00106.31 C ANISOU 5910 CG GLN B 293 16282 12386 11725 -360 -1196 2339 C ATOM 5911 CD GLN B 293 19.000 14.952 131.308 1.00107.38 C ANISOU 5911 CD GLN B 293 16465 12536 11798 -396 -1205 2307 C ATOM 5912 OE1 GLN B 293 18.249 14.276 130.602 1.00109.32 O ANISOU 5912 OE1 GLN B 293 16761 12783 11992 -448 -1274 2359 O ATOM 5913 NE2 GLN B 293 19.207 14.680 132.598 1.00107.56 N ANISOU 5913 NE2 GLN B 293 16470 12576 11819 -381 -1140 2227 N ATOM 5914 N LYS B 294 21.249 18.836 130.138 1.00103.37 N ANISOU 5914 N LYS B 294 15767 11974 11533 -281 -1163 2391 N ATOM 5915 CA LYS B 294 20.920 20.236 130.442 1.00103.94 C ANISOU 5915 CA LYS B 294 15675 11995 11822 -258 -1160 2409 C ATOM 5916 C LYS B 294 21.909 21.231 129.828 1.00103.91 C ANISOU 5916 C LYS B 294 15653 11981 11846 -232 -1166 2457 C ATOM 5917 O LYS B 294 21.534 22.360 129.520 1.00104.72 O ANISOU 5917 O LYS B 294 15629 12028 12128 -239 -1216 2529 O ATOM 5918 CB LYS B 294 20.837 20.445 131.959 1.00104.42 C ANISOU 5918 CB LYS B 294 15649 12052 11974 -220 -1059 2283 C ATOM 5919 CG LYS B 294 19.659 19.736 132.617 1.00105.48 C ANISOU 5919 CG LYS B 294 15758 12196 12123 -264 -1058 2242 C ATOM 5920 CD LYS B 294 19.954 19.338 134.059 1.00105.67 C ANISOU 5920 CD LYS B 294 15781 12267 12099 -259 -954 2114 C ATOM 5921 CE LYS B 294 20.720 18.023 134.124 1.00105.43 C ANISOU 5921 CE LYS B 294 15920 12288 11851 -261 -952 2106 C ATOM 5922 NZ LYS B 294 20.963 17.572 135.523 1.00105.33 N ANISOU 5922 NZ LYS B 294 15907 12326 11785 -282 -877 2012 N ATOM 5923 N PHE B 295 23.167 20.817 129.673 1.00103.61 N ANISOU 5923 N PHE B 295 15730 11988 11647 -206 -1118 2417 N ATOM 5924 CA PHE B 295 24.174 21.622 128.966 1.00104.13 C ANISOU 5924 CA PHE B 295 15801 12061 11702 -195 -1124 2463 C ATOM 5925 C PHE B 295 23.929 21.637 127.450 1.00105.37 C ANISOU 5925 C PHE B 295 16003 12244 11788 -287 -1233 2595 C ATOM 5926 O PHE B 295 24.084 22.679 126.801 1.00106.25 O ANISOU 5926 O PHE B 295 16049 12340 11979 -314 -1291 2693 O ATOM 5927 CB PHE B 295 25.598 21.120 129.266 1.00102.86 C ANISOU 5927 CB PHE B 295 15744 11941 11397 -143 -1034 2369 C ATOM 5928 CG PHE B 295 26.154 21.591 130.588 1.00101.86 C ANISOU 5928 CG PHE B 295 15551 11796 11352 -66 -938 2273 C ATOM 5929 CD1 PHE B 295 26.395 22.945 130.817 1.00101.92 C ANISOU 5929 CD1 PHE B 295 15439 11769 11515 -31 -919 2283 C ATOM 5930 CD2 PHE B 295 26.469 20.680 131.595 1.00101.18 C ANISOU 5930 CD2 PHE B 295 15521 11731 11190 -41 -872 2176 C ATOM 5931 CE1 PHE B 295 26.917 23.381 132.028 1.00101.01 C ANISOU 5931 CE1 PHE B 295 15264 11649 11465 25 -824 2184 C ATOM 5932 CE2 PHE B 295 26.990 21.110 132.809 1.00100.57 C ANISOU 5932 CE2 PHE B 295 15385 11655 11169 4 -789 2095 C ATOM 5933 CZ PHE B 295 27.217 22.461 133.026 1.00100.37 C ANISOU 5933 CZ PHE B 295 15245 11604 11285 37 -758 2091 C ATOM 5934 N ARG B 296 23.565 20.477 126.899 1.00105.81 N ANISOU 5934 N ARG B 296 16169 12343 11691 -348 -1265 2599 N ATOM 5935 CA ARG B 296 23.249 20.329 125.471 1.00107.20 C ANISOU 5935 CA ARG B 296 16398 12565 11766 -466 -1365 2713 C ATOM 5936 C ARG B 296 22.140 21.277 125.018 1.00108.59 C ANISOU 5936 C ARG B 296 16449 12695 12115 -526 -1488 2868 C ATOM 5937 O ARG B 296 22.287 21.958 123.999 1.00110.73 O ANISOU 5937 O ARG B 296 16703 12989 12379 -608 -1574 2995 O ATOM 5938 CB ARG B 296 22.860 18.874 125.163 1.00108.15 C ANISOU 5938 CB ARG B 296 16639 12729 11724 -518 -1369 2669 C ATOM 5939 CG ARG B 296 22.285 18.618 123.778 1.00110.04 C ANISOU 5939 CG ARG B 296 16927 13025 11856 -660 -1474 2780 C ATOM 5940 CD ARG B 296 22.297 17.132 123.463 1.00111.37 C ANISOU 5940 CD ARG B 296 17228 13243 11843 -703 -1444 2692 C ATOM 5941 NE ARG B 296 23.541 16.706 122.823 1.00112.80 N ANISOU 5941 NE ARG B 296 17508 13491 11858 -734 -1379 2606 N ATOM 5942 CZ ARG B 296 23.778 15.477 122.356 1.00113.93 C ANISOU 5942 CZ ARG B 296 17759 13677 11850 -785 -1343 2510 C ATOM 5943 NH1 ARG B 296 22.873 14.502 122.474 1.00114.24 N ANISOU 5943 NH1 ARG B 296 17832 13701 11870 -807 -1370 2495 N ATOM 5944 NH2 ARG B 296 24.944 15.215 121.771 1.00114.51 N ANISOU 5944 NH2 ARG B 296 17900 13807 11801 -816 -1274 2417 N ATOM 5945 N VAL B 297 21.043 21.317 125.777 1.00108.33 N ANISOU 5945 N VAL B 297 16320 12596 12242 -495 -1501 2860 N ATOM 5946 CA VAL B 297 19.906 22.193 125.456 1.00109.79 C ANISOU 5946 CA VAL B 297 16360 12711 12643 -542 -1620 2997 C ATOM 5947 C VAL B 297 20.283 23.680 125.584 1.00110.47 C ANISOU 5947 C VAL B 297 16302 12728 12942 -503 -1636 3048 C ATOM 5948 O VAL B 297 19.815 24.506 124.794 1.00112.21 O ANISOU 5948 O VAL B 297 16430 12906 13295 -575 -1767 3211 O ATOM 5949 CB VAL B 297 18.648 21.843 126.296 1.00109.23 C ANISOU 5949 CB VAL B 297 16211 12584 12706 -518 -1613 2949 C ATOM 5950 CG1 VAL B 297 18.767 22.330 127.731 1.00108.83 C ANISOU 5950 CG1 VAL B 297 16052 12481 12818 -414 -1496 2808 C ATOM 5951 CG2 VAL B 297 17.390 22.405 125.645 1.00110.57 C ANISOU 5951 CG2 VAL B 297 16261 12690 13060 -596 -1760 3107 C ATOM 5952 N THR B 298 21.146 24.004 126.547 1.00109.33 N ANISOU 5952 N THR B 298 16136 12571 12831 -400 -1512 2918 N ATOM 5953 CA THR B 298 21.617 25.375 126.745 1.00110.12 C ANISOU 5953 CA THR B 298 16104 12607 13129 -355 -1510 2942 C ATOM 5954 C THR B 298 22.580 25.834 125.639 1.00111.66 C ANISOU 5954 C THR B 298 16360 12851 13213 -411 -1569 3054 C ATOM 5955 O THR B 298 22.360 26.898 125.037 1.00113.08 O ANISOU 5955 O THR B 298 16428 12977 13561 -459 -1681 3201 O ATOM 5956 CB THR B 298 22.289 25.538 128.123 1.00108.68 C ANISOU 5956 CB THR B 298 15889 12411 12991 -242 -1354 2762 C ATOM 5957 OG1 THR B 298 21.410 25.041 129.143 1.00108.33 O ANISOU 5957 OG1 THR B 298 15797 12347 13015 -218 -1295 2654 O ATOM 5958 CG2 THR B 298 22.612 26.999 128.411 1.00109.06 C ANISOU 5958 CG2 THR B 298 15776 12379 13282 -195 -1348 2773 C ATOM 5959 N PHE B 299 23.618 25.035 125.357 1.00112.05 N ANISOU 5959 N PHE B 299 16576 13001 12995 -416 -1499 2987 N ATOM 5960 CA PHE B 299 24.617 25.390 124.317 1.00113.18 C ANISOU 5960 CA PHE B 299 16786 13214 13003 -483 -1534 3066 C ATOM 5961 C PHE B 299 23.964 25.709 122.964 1.00116.44 C ANISOU 5961 C PHE B 299 17183 13652 13407 -639 -1705 3272 C ATOM 5962 O PHE B 299 24.351 26.676 122.286 1.00117.03 O ANISOU 5962 O PHE B 299 17206 13730 13531 -701 -1785 3401 O ATOM 5963 CB PHE B 299 25.669 24.280 124.101 1.00111.71 C ANISOU 5963 CB PHE B 299 16779 13132 12533 -485 -1436 2947 C ATOM 5964 CG PHE B 299 26.518 23.951 125.313 1.00109.65 C ANISOU 5964 CG PHE B 299 16545 12855 12261 -351 -1286 2770 C ATOM 5965 CD1 PHE B 299 26.790 24.887 126.316 1.00108.95 C ANISOU 5965 CD1 PHE B 299 16341 12697 12355 -250 -1231 2725 C ATOM 5966 CD2 PHE B 299 27.078 22.681 125.429 1.00108.46 C ANISOU 5966 CD2 PHE B 299 16530 12759 11920 -336 -1205 2648 C ATOM 5967 CE1 PHE B 299 27.582 24.550 127.408 1.00107.54 C ANISOU 5967 CE1 PHE B 299 16194 12520 12146 -150 -1103 2575 C ATOM 5968 CE2 PHE B 299 27.871 22.343 126.516 1.00107.45 C ANISOU 5968 CE2 PHE B 299 16425 12615 11786 -229 -1089 2509 C ATOM 5969 CZ PHE B 299 28.123 23.278 127.509 1.00106.81 C ANISOU 5969 CZ PHE B 299 16239 12481 11864 -141 -1040 2478 C ATOM 5970 N LEU B 300 22.979 24.892 122.585 1.00118.49 N ANISOU 5970 N LEU B 300 17485 13933 13601 -713 -1766 3311 N ATOM 5971 CA LEU B 300 22.147 25.155 121.407 1.00121.08 C ANISOU 5971 CA LEU B 300 17783 14280 13941 -873 -1942 3519 C ATOM 5972 C LEU B 300 21.459 26.516 121.494 1.00122.71 C ANISOU 5972 C LEU B 300 17786 14357 14480 -870 -2066 3672 C ATOM 5973 O LEU B 300 21.460 27.271 120.517 1.00124.54 O ANISOU 5973 O LEU B 300 17972 14601 14745 -993 -2210 3866 O ATOM 5974 CB LEU B 300 21.087 24.061 121.232 1.00121.82 C ANISOU 5974 CB LEU B 300 17937 14397 13951 -930 -1976 3516 C ATOM 5975 CG LEU B 300 21.593 22.683 120.791 1.00121.59 C ANISOU 5975 CG LEU B 300 18100 14494 13603 -982 -1897 3404 C ATOM 5976 CD1 LEU B 300 20.521 21.625 121.012 1.00121.38 C ANISOU 5976 CD1 LEU B 300 18111 14458 13549 -989 -1905 3366 C ATOM 5977 CD2 LEU B 300 22.043 22.697 119.336 1.00122.78 C ANISOU 5977 CD2 LEU B 300 18335 14774 13540 -1168 -1975 3514 C ATOM 5978 N LYS B 301 20.880 26.823 122.659 1.00123.14 N ANISOU 5978 N LYS B 301 17710 14289 14786 -742 -2012 3582 N ATOM 5979 CA LYS B 301 20.178 28.096 122.854 1.00124.32 C ANISOU 5979 CA LYS B 301 17639 14292 15306 -726 -2113 3692 C ATOM 5980 C LYS B 301 21.126 29.288 122.767 1.00124.03 C ANISOU 5980 C LYS B 301 17527 14221 15378 -703 -2124 3742 C ATOM 5981 O LYS B 301 20.811 30.279 122.108 1.00125.32 O ANISOU 5981 O LYS B 301 17563 14313 15737 -781 -2285 3939 O ATOM 5982 CB LYS B 301 19.417 28.118 124.190 1.00124.13 C ANISOU 5982 CB LYS B 301 17487 14157 15517 -602 -2020 3538 C ATOM 5983 CG LYS B 301 18.430 29.273 124.326 1.00125.83 C ANISOU 5983 CG LYS B 301 17454 14205 16148 -600 -2131 3637 C ATOM 5984 CD LYS B 301 17.227 28.913 125.203 1.00126.03 C ANISOU 5984 CD LYS B 301 17380 14155 16348 -552 -2085 3525 C ATOM 5985 CE LYS B 301 16.208 28.075 124.438 1.00126.81 C ANISOU 5985 CE LYS B 301 17544 14291 16347 -659 -2204 3646 C ATOM 5986 NZ LYS B 301 15.341 27.261 125.337 1.00126.30 N ANISOU 5986 NZ LYS B 301 17472 14217 16297 -611 -2110 3491 N ATOM 5987 N ILE B 302 22.290 29.176 123.408 1.00122.21 N ANISOU 5987 N ILE B 302 17372 14037 15023 -603 -1963 3576 N ATOM 5988 CA ILE B 302 23.315 30.226 123.339 1.00121.95 C ANISOU 5988 CA ILE B 302 17288 13986 15060 -577 -1957 3608 C ATOM 5989 C ILE B 302 23.814 30.383 121.894 1.00123.14 C ANISOU 5989 C ILE B 302 17523 14238 15025 -738 -2086 3799 C ATOM 5990 O ILE B 302 23.930 31.514 121.400 1.00124.12 O ANISOU 5990 O ILE B 302 17534 14307 15316 -792 -2207 3963 O ATOM 5991 CB ILE B 302 24.493 29.957 124.311 1.00120.17 C ANISOU 5991 CB ILE B 302 17142 13803 14712 -446 -1757 3389 C ATOM 5992 CG1 ILE B 302 24.012 30.027 125.769 1.00119.07 C ANISOU 5992 CG1 ILE B 302 16892 13571 14776 -317 -1641 3215 C ATOM 5993 CG2 ILE B 302 25.626 30.964 124.100 1.00120.38 C ANISOU 5993 CG2 ILE B 302 17138 13829 14770 -433 -1755 3430 C ATOM 5994 CD1 ILE B 302 24.922 29.325 126.757 1.00117.13 C ANISOU 5994 CD1 ILE B 302 16757 13393 14351 -219 -1455 3004 C ATOM 5995 N TRP B 303 24.084 29.256 121.227 1.00123.86 N ANISOU 5995 N TRP B 303 17803 14477 14781 -825 -2061 3775 N ATOM 5996 CA TRP B 303 24.500 29.256 119.813 1.00125.60 C ANISOU 5996 CA TRP B 303 18115 14826 14781 -1013 -2169 3933 C ATOM 5997 C TRP B 303 23.475 29.965 118.930 1.00127.44 C ANISOU 5997 C TRP B 303 18229 15010 15180 -1166 -2401 4205 C ATOM 5998 O TRP B 303 23.813 30.934 118.235 1.00129.45 O ANISOU 5998 O TRP B 303 18420 15269 15495 -1266 -2525 4384 O ATOM 5999 CB TRP B 303 24.723 27.821 119.309 1.00125.81 C ANISOU 5999 CB TRP B 303 18342 15006 14453 -1088 -2095 3832 C ATOM 6000 CG TRP B 303 25.111 27.721 117.847 1.00127.32 C ANISOU 6000 CG TRP B 303 18631 15355 14388 -1309 -2187 3963 C ATOM 6001 CD1 TRP B 303 26.157 28.352 117.227 1.00127.84 C ANISOU 6001 CD1 TRP B 303 18719 15502 14352 -1390 -2198 4019 C ATOM 6002 CD2 TRP B 303 24.466 26.933 116.837 1.00128.59 C ANISOU 6002 CD2 TRP B 303 18880 15627 14349 -1494 -2273 4045 C ATOM 6003 NE1 TRP B 303 26.198 28.009 115.897 1.00129.17 N ANISOU 6003 NE1 TRP B 303 18982 15834 14261 -1625 -2282 4127 N ATOM 6004 CE2 TRP B 303 25.173 27.140 115.629 1.00129.71 C ANISOU 6004 CE2 TRP B 303 19093 15924 14265 -1695 -2329 4143 C ATOM 6005 CE3 TRP B 303 23.358 26.072 116.833 1.00128.85 C ANISOU 6005 CE3 TRP B 303 18938 15650 14366 -1520 -2306 4042 C ATOM 6006 CZ2 TRP B 303 24.810 26.515 114.428 1.00130.89 C ANISOU 6006 CZ2 TRP B 303 19337 16228 14166 -1931 -2412 4230 C ATOM 6007 CZ3 TRP B 303 22.995 25.448 115.634 1.00129.77 C ANISOU 6007 CZ3 TRP B 303 19150 15907 14246 -1740 -2393 4134 C ATOM 6008 CH2 TRP B 303 23.722 25.676 114.450 1.00130.89 C ANISOU 6008 CH2 TRP B 303 19361 16211 14159 -1948 -2443 4223 C ATOM 6009 N ASN B 304 22.229 29.491 118.993 1.00127.31 N ANISOU 6009 N ASN B 304 18176 14944 15250 -1185 -2465 4240 N ATOM 6010 CA ASN B 304 21.119 30.056 118.210 1.00128.60 C ANISOU 6010 CA ASN B 304 18218 15048 15596 -1329 -2697 4502 C ATOM 6011 C ASN B 304 20.886 31.540 118.521 1.00129.60 C ANISOU 6011 C ASN B 304 18111 14993 16136 -1278 -2806 4630 C ATOM 6012 O ASN B 304 20.799 32.359 117.605 1.00131.02 O ANISOU 6012 O ASN B 304 18214 15163 16403 -1428 -3001 4881 O ATOM 6013 CB ASN B 304 19.824 29.268 118.465 1.00128.17 C ANISOU 6013 CB ASN B 304 18151 14949 15598 -1320 -2718 4478 C ATOM 6014 CG ASN B 304 18.787 29.466 117.373 1.00130.40 C ANISOU 6014 CG ASN B 304 18375 15230 15940 -1518 -2957 4753 C ATOM 6015 OD1 ASN B 304 18.460 30.592 117.001 1.00131.59 O ANISOU 6015 OD1 ASN B 304 18360 15279 16357 -1584 -3135 4968 O ATOM 6016 ND2 ASN B 304 18.252 28.362 116.862 1.00130.88 N ANISOU 6016 ND2 ASN B 304 18564 15398 15765 -1620 -2971 4752 N ATOM 6017 N ASP B 305 20.794 31.876 119.807 1.00128.27 N ANISOU 6017 N ASP B 305 17825 14685 16224 -1081 -2681 4456 N ATOM 6018 CA ASP B 305 20.483 33.250 120.223 1.00128.39 C ANISOU 6018 CA ASP B 305 17595 14507 16679 -1019 -2764 4535 C ATOM 6019 C ASP B 305 21.640 34.247 120.064 1.00128.58 C ANISOU 6019 C ASP B 305 17588 14530 16736 -1013 -2769 4584 C ATOM 6020 O ASP B 305 21.382 35.442 119.898 1.00130.24 O ANISOU 6020 O ASP B 305 17602 14598 17285 -1036 -2916 4747 O ATOM 6021 CB ASP B 305 19.966 33.284 121.669 1.00126.56 C ANISOU 6021 CB ASP B 305 17238 14139 16711 -831 -2615 4307 C ATOM 6022 CG ASP B 305 18.653 32.535 121.845 1.00125.91 C ANISOU 6022 CG ASP B 305 17132 14022 16683 -843 -2640 4287 C ATOM 6023 OD1 ASP B 305 18.251 31.780 120.931 1.00125.69 O ANISOU 6023 OD1 ASP B 305 17226 14097 16433 -978 -2739 4413 O ATOM 6024 OD2 ASP B 305 18.024 32.697 122.911 1.00125.20 O ANISOU 6024 OD2 ASP B 305 16901 13811 16855 -725 -2552 4134 O ATOM 6025 N HIS B 306 22.893 33.781 120.119 1.00126.25 N ANISOU 6025 N HIS B 306 17471 14380 16118 -982 -2617 4447 N ATOM 6026 CA HIS B 306 24.047 34.699 120.056 1.00125.18 C ANISOU 6026 CA HIS B 306 17310 14247 16005 -964 -2602 4471 C ATOM 6027 C HIS B 306 25.083 34.420 118.951 1.00125.39 C ANISOU 6027 C HIS B 306 17517 14470 15655 -1116 -2626 4557 C ATOM 6028 O HIS B 306 25.537 35.367 118.305 1.00127.11 O ANISOU 6028 O HIS B 306 17673 14685 15935 -1211 -2750 4735 O ATOM 6029 CB HIS B 306 24.727 34.784 121.428 1.00122.93 C ANISOU 6029 CB HIS B 306 17007 13910 15791 -753 -2379 4201 C ATOM 6030 CG HIS B 306 23.844 35.344 122.504 1.00122.48 C ANISOU 6030 CG HIS B 306 16738 13661 16137 -626 -2352 4112 C ATOM 6031 ND1 HIS B 306 23.916 36.656 122.920 1.00122.96 N ANISOU 6031 ND1 HIS B 306 16588 13563 16565 -563 -2386 4137 N ATOM 6032 CD2 HIS B 306 22.866 34.769 123.243 1.00121.75 C ANISOU 6032 CD2 HIS B 306 16603 13514 16142 -561 -2288 3986 C ATOM 6033 CE1 HIS B 306 23.024 36.864 123.873 1.00122.75 C ANISOU 6033 CE1 HIS B 306 16394 13392 16850 -466 -2334 4014 C ATOM 6034 NE2 HIS B 306 22.373 35.735 124.088 1.00121.95 N ANISOU 6034 NE2 HIS B 306 16393 13357 16586 -466 -2275 3924 N ATOM 6035 N PHE B 307 25.451 33.154 118.726 1.00124.27 N ANISOU 6035 N PHE B 307 17584 14494 15138 -1148 -2511 4428 N ATOM 6036 CA PHE B 307 26.540 32.811 117.781 1.00123.77 C ANISOU 6036 CA PHE B 307 17690 14625 14710 -1284 -2488 4445 C ATOM 6037 C PHE B 307 26.064 32.175 116.461 1.00125.71 C ANISOU 6037 C PHE B 307 18038 15021 14702 -1527 -2619 4601 C ATOM 6038 O PHE B 307 26.832 31.490 115.779 1.00124.55 O ANISOU 6038 O PHE B 307 18057 15057 14206 -1639 -2550 4538 O ATOM 6039 CB PHE B 307 27.566 31.908 118.478 1.00120.82 C ANISOU 6039 CB PHE B 307 17468 14331 14107 -1148 -2243 4158 C ATOM 6040 CG PHE B 307 28.387 32.615 119.512 1.00118.30 C ANISOU 6040 CG PHE B 307 17076 13920 13952 -965 -2123 4031 C ATOM 6041 CD1 PHE B 307 29.584 33.228 119.165 1.00117.46 C ANISOU 6041 CD1 PHE B 307 16994 13875 13757 -995 -2103 4053 C ATOM 6042 CD2 PHE B 307 27.970 32.663 120.837 1.00117.09 C ANISOU 6042 CD2 PHE B 307 16829 13629 14029 -777 -2025 3884 C ATOM 6043 CE1 PHE B 307 30.351 33.881 120.121 1.00116.43 C ANISOU 6043 CE1 PHE B 307 16798 13662 13775 -830 -1991 3935 C ATOM 6044 CE2 PHE B 307 28.729 33.313 121.797 1.00115.90 C ANISOU 6044 CE2 PHE B 307 16611 13406 14016 -626 -1910 3760 C ATOM 6045 CZ PHE B 307 29.922 33.924 121.440 1.00115.61 C ANISOU 6045 CZ PHE B 307 16603 13424 13899 -647 -1895 3789 C ATOM 6046 N ARG B 308 24.810 32.431 116.090 1.00128.51 N ANISOU 6046 N ARG B 308 18287 15300 15242 -1620 -2807 4800 N ATOM 6047 CA ARG B 308 24.241 31.888 114.859 1.00131.91 C ANISOU 6047 CA ARG B 308 18799 15868 15451 -1866 -2950 4969 C ATOM 6048 C ARG B 308 24.564 32.804 113.678 1.00135.02 C ANISOU 6048 C ARG B 308 19156 16342 15801 -2102 -3149 5248 C ATOM 6049 O ARG B 308 24.580 34.034 113.822 1.00136.19 O ANISOU 6049 O ARG B 308 19139 16358 16250 -2075 -3266 5400 O ATOM 6050 CB ARG B 308 22.724 31.724 115.003 1.00133.24 C ANISOU 6050 CB ARG B 308 18865 15917 15840 -1866 -3072 5067 C ATOM 6051 CG ARG B 308 22.096 30.717 114.051 1.00134.57 C ANISOU 6051 CG ARG B 308 19161 16236 15734 -2066 -3143 5139 C ATOM 6052 CD ARG B 308 22.506 29.287 114.383 1.00133.31 C ANISOU 6052 CD ARG B 308 19193 16191 15267 -1990 -2918 4852 C ATOM 6053 NE ARG B 308 21.582 28.304 113.813 1.00134.28 N ANISOU 6053 NE ARG B 308 19394 16392 15231 -2121 -2975 4888 N ATOM 6054 CZ ARG B 308 21.519 27.954 112.524 1.00135.81 C ANISOU 6054 CZ ARG B 308 19683 16767 15149 -2390 -3081 5022 C ATOM 6055 NH1 ARG B 308 22.331 28.496 111.614 1.00137.50 N ANISOU 6055 NH1 ARG B 308 19931 17117 15196 -2576 -3144 5140 N ATOM 6056 NH2 ARG B 308 20.629 27.044 112.137 1.00135.93 N ANISOU 6056 NH2 ARG B 308 19762 16838 15045 -2488 -3121 5034 N ATOM 6057 N CYS B 309 24.811 32.196 112.518 1.00137.04 N ANISOU 6057 N CYS B 309 19560 16819 15688 -2346 -3187 5310 N ATOM 6058 CA CYS B 309 25.127 32.935 111.289 1.00139.92 C ANISOU 6058 CA CYS B 309 19913 17308 15941 -2623 -3378 5580 C ATOM 6059 C CYS B 309 23.842 33.504 110.669 1.00141.82 C ANISOU 6059 C CYS B 309 20014 17470 16401 -2793 -3672 5917 C ATOM 6060 O CYS B 309 23.425 33.112 109.580 1.00142.40 O ANISOU 6060 O CYS B 309 20157 17703 16245 -3064 -3805 6079 O ATOM 6061 CB CYS B 309 25.880 32.031 110.301 1.00140.95 C ANISOU 6061 CB CYS B 309 20251 17723 15579 -2841 -3290 5491 C ATOM 6062 SG CYS B 309 26.601 32.879 108.867 1.00144.22 S ANISOU 6062 SG CYS B 309 20679 18342 15775 -3195 -3467 5760 S TER 6063 CYS B 309 HETATM 6064 O4 DU1 A1201 52.632 56.381 141.281 1.00 60.89 O HETATM 6065 C3 DU1 A1201 53.092 57.489 141.071 1.00 58.99 C HETATM 6066 N1 DU1 A1201 54.241 57.935 141.723 1.00 60.21 N HETATM 6067 C14 DU1 A1201 54.739 59.205 141.449 1.00 58.78 C HETATM 6068 C22 DU1 A1201 54.124 60.036 140.552 1.00 57.54 C HETATM 6069 N4 DU1 A1201 54.897 61.167 140.563 1.00 56.77 N HETATM 6070 C15 DU1 A1201 55.910 60.971 141.444 1.00 56.90 C HETATM 6071 C16 DU1 A1201 56.974 61.968 141.733 1.00 56.94 C HETATM 6072 C21 DU1 A1201 56.419 63.357 142.071 1.00 56.59 C HETATM 6073 C20 DU1 A1201 57.523 64.320 142.504 1.00 56.46 C HETATM 6074 C19 DU1 A1201 58.880 63.915 141.946 1.00 56.42 C HETATM 6075 C18 DU1 A1201 58.749 63.350 140.542 1.00 56.71 C HETATM 6076 C17 DU1 A1201 57.917 62.069 140.527 1.00 56.73 C HETATM 6077 N3 DU1 A1201 55.847 59.780 142.000 1.00 57.84 N HETATM 6078 C23 DU1 A1201 52.955 59.668 139.845 1.00 57.21 C HETATM 6079 O3 DU1 A1201 52.364 60.373 139.033 1.00 56.07 O HETATM 6080 N DU1 A1201 52.492 58.368 140.164 1.00 57.32 N HETATM 6081 C2 DU1 A1201 51.292 57.890 139.453 1.00 55.89 C HETATM 6082 C1 DU1 A1201 50.003 58.368 140.053 1.00 55.32 C HETATM 6083 C DU1 A1201 48.813 57.763 139.327 1.00 54.88 C HETATM 6084 C4 DU1 A1201 54.903 57.018 142.666 1.00 61.90 C HETATM 6085 C5 DU1 A1201 54.273 57.020 144.043 1.00 64.75 C HETATM 6086 C6 DU1 A1201 54.879 55.986 144.968 1.00 67.52 C HETATM 6087 N2 DU1 A1201 56.038 56.504 145.684 1.00 70.55 N HETATM 6088 C7 DU1 A1201 56.350 56.105 146.923 1.00 73.59 C HETATM 6089 O2 DU1 A1201 55.669 55.283 147.534 1.00 76.81 O HETATM 6090 C8 DU1 A1201 57.554 56.719 147.568 1.00 73.81 C HETATM 6091 C13 DU1 A1201 57.962 58.025 147.299 1.00 74.48 C HETATM 6092 C12 DU1 A1201 59.067 58.571 147.928 1.00 76.49 C HETATM 6093 C11 DU1 A1201 59.769 57.813 148.852 1.00 76.85 C HETATM 6094 S DU1 A1201 61.183 58.480 149.680 1.00 79.44 S HETATM 6095 O1 DU1 A1201 61.626 59.622 148.910 1.00 82.41 O HETATM 6096 O DU1 A1201 62.126 57.392 149.841 1.00 79.67 O HETATM 6097 C10 DU1 A1201 59.375 56.519 149.147 1.00 75.20 C HETATM 6098 C9 DU1 A1201 58.270 55.981 148.511 1.00 74.78 C HETATM 6099 C1 OLA A1202 29.207 43.942 135.216 1.00 83.80 C HETATM 6100 O1 OLA A1202 28.631 42.972 134.676 1.00 84.55 O HETATM 6101 O2 OLA A1202 28.790 44.486 136.263 1.00 84.61 O HETATM 6102 C2 OLA A1202 30.459 44.490 134.571 1.00 82.45 C HETATM 6103 C3 OLA A1202 31.564 43.442 134.577 1.00 81.35 C HETATM 6104 C4 OLA A1202 32.892 44.068 134.175 1.00 80.37 C HETATM 6105 C5 OLA A1202 33.910 42.997 133.806 1.00 80.07 C HETATM 6106 C6 OLA A1202 35.282 43.613 133.543 1.00 80.62 C HETATM 6107 C7 OLA A1202 36.041 42.858 132.456 1.00 81.64 C HETATM 6108 C8 OLA A1202 37.312 43.584 132.022 1.00 82.50 C HETATM 6109 C9 OLA A1202 38.523 43.032 132.751 1.00 83.24 C HETATM 6110 C10 OLA A1202 39.754 43.040 132.225 1.00 84.73 C HETATM 6111 C11 OLA A1202 40.036 43.603 130.850 1.00 86.14 C HETATM 6112 C12 OLA A1202 41.526 43.571 130.539 1.00 86.32 C HETATM 6113 C13 OLA A1202 41.835 44.513 129.380 1.00 86.55 C HETATM 6114 C14 OLA A1202 43.114 44.100 128.665 1.00 87.34 C HETATM 6115 C15 OLA A1202 43.490 45.104 127.582 1.00 87.81 C HETATM 6116 C16 OLA A1202 44.943 44.916 127.159 1.00 88.54 C HETATM 6117 C17 OLA A1202 45.342 45.914 126.077 1.00 88.74 C HETATM 6118 C18 OLA A1202 45.744 47.242 126.679 1.00 87.90 C HETATM 6119 C1 OLA A1203 30.068 45.160 139.185 1.00 62.83 C HETATM 6120 O1 OLA A1203 29.890 46.282 139.700 1.00 64.92 O HETATM 6121 O2 OLA A1203 29.302 44.194 139.391 1.00 64.76 O HETATM 6122 C2 OLA A1203 31.248 44.964 138.266 1.00 61.18 C HETATM 6123 C3 OLA A1203 32.567 45.154 139.007 1.00 59.27 C HETATM 6124 C4 OLA A1203 33.718 45.065 138.011 1.00 58.36 C HETATM 6125 C5 OLA A1203 35.068 44.868 138.685 1.00 57.53 C HETATM 6126 C6 OLA A1203 36.096 44.384 137.668 1.00 57.19 C HETATM 6127 C7 OLA A1203 37.495 44.371 138.269 1.00 57.18 C HETATM 6128 C8 OLA A1203 38.557 44.066 137.218 1.00 57.57 C HETATM 6129 C9 OLA A1203 39.832 43.666 137.925 1.00 59.05 C HETATM 6130 C10 OLA A1203 40.960 44.357 137.757 1.00 60.42 C HETATM 6131 C11 OLA A1203 42.233 43.954 138.474 1.00 61.20 C HETATM 6132 C12 OLA A1203 42.710 45.092 139.374 1.00 61.44 C HETATM 6133 C13 OLA A1203 44.205 44.988 139.670 1.00 61.45 C HETATM 6134 C14 OLA A1203 45.045 45.647 138.577 1.00 61.19 C HETATM 6135 C15 OLA A1203 46.450 45.051 138.510 1.00 61.56 C HETATM 6136 C16 OLA A1203 47.208 45.536 137.279 1.00 61.82 C HETATM 6137 C17 OLA A1203 48.510 44.764 137.078 1.00 61.78 C HETATM 6138 C18 OLA A1203 49.409 45.440 136.062 1.00 61.25 C HETATM 6139 C1 OLA A1204 63.424 53.947 165.201 1.00 71.50 C HETATM 6140 O1 OLA A1204 63.640 53.288 164.161 1.00 72.34 O HETATM 6141 O2 OLA A1204 64.296 54.667 165.738 1.00 71.90 O HETATM 6142 C2 OLA A1204 62.052 53.865 165.833 1.00 70.01 C HETATM 6143 C3 OLA A1204 61.018 54.502 164.913 1.00 67.84 C HETATM 6144 C4 OLA A1204 59.612 54.411 165.488 1.00 66.99 C HETATM 6145 C5 OLA A1204 58.611 55.153 164.603 1.00 66.29 C HETATM 6146 C6 OLA A1204 57.269 54.431 164.548 1.00 66.62 C HETATM 6147 C7 OLA A1204 56.317 55.103 163.566 1.00 66.47 C HETATM 6148 C8 OLA A1204 54.938 54.447 163.588 1.00 66.16 C HETATM 6149 C9 OLA A1204 54.036 55.146 162.594 1.00 66.65 C HETATM 6150 C10 OLA A1204 52.774 54.764 162.386 1.00 66.67 C HETATM 6151 C11 OLA A1204 52.156 53.604 163.133 1.00 66.58 C HETATM 6152 C12 OLA A1204 50.711 53.417 162.686 1.00 65.71 C HETATM 6153 C1 OLA A1205 62.587 57.452 153.660 1.00 60.10 C HETATM 6154 O1 OLA A1205 61.850 56.457 153.471 1.00 60.00 O HETATM 6155 O2 OLA A1205 63.825 57.393 153.493 1.00 59.78 O HETATM 6156 C2 OLA A1205 61.995 58.780 154.103 1.00 60.12 C HETATM 6157 C3 OLA A1205 60.514 58.671 154.463 1.00 60.42 C HETATM 6158 C4 OLA A1205 59.925 60.019 154.873 1.00 61.15 C HETATM 6159 C5 OLA A1205 58.476 59.868 155.334 1.00 62.46 C HETATM 6160 C6 OLA A1205 57.968 61.103 156.075 1.00 63.68 C HETATM 6161 C7 OLA A1205 56.752 60.765 156.934 1.00 64.49 C HETATM 6162 C8 OLA A1205 56.219 62.004 157.649 1.00 65.77 C HETATM 6163 C9 OLA A1205 55.324 62.804 156.728 1.00 66.51 C HETATM 6164 C10 OLA A1205 54.071 63.085 157.082 1.00 66.30 C HETATM 6165 O4 DU1 B1201 54.338 22.563 132.835 1.00 85.23 O HETATM 6166 C3 DU1 B1201 55.002 21.542 132.877 1.00 82.53 C HETATM 6167 N1 DU1 B1201 55.977 21.269 131.918 1.00 82.84 N HETATM 6168 C14 DU1 B1201 56.722 20.095 132.010 1.00 81.80 C HETATM 6169 C22 DU1 B1201 56.516 19.197 133.020 1.00 80.44 C HETATM 6170 N4 DU1 B1201 57.417 18.197 132.770 1.00 79.34 N HETATM 6171 C15 DU1 B1201 58.105 18.528 131.648 1.00 79.21 C HETATM 6172 C16 DU1 B1201 59.176 17.671 131.072 1.00 77.97 C HETATM 6173 C21 DU1 B1201 58.617 16.319 130.607 1.00 77.85 C HETATM 6174 C20 DU1 B1201 59.699 15.249 130.478 1.00 77.14 C HETATM 6175 C19 DU1 B1201 61.075 15.863 130.311 1.00 76.98 C HETATM 6176 C18 DU1 B1201 61.467 16.664 131.541 1.00 77.20 C HETATM 6177 C17 DU1 B1201 60.286 17.452 132.107 1.00 76.99 C HETATM 6178 N3 DU1 B1201 57.707 19.685 131.158 1.00 81.74 N HETATM 6179 C23 DU1 B1201 55.551 19.392 134.030 1.00 80.60 C HETATM 6180 O3 DU1 B1201 55.328 18.617 134.952 1.00 82.30 O HETATM 6181 N DU1 B1201 54.824 20.596 133.890 1.00 80.96 N HETATM 6182 C2 DU1 B1201 53.811 20.892 134.921 1.00 80.22 C HETATM 6183 C1 DU1 B1201 52.473 20.248 134.672 1.00 79.90 C HETATM 6184 C DU1 B1201 51.465 20.706 135.712 1.00 78.79 C HETATM 6185 C4 DU1 B1201 56.195 22.263 130.854 1.00 83.04 C HETATM 6186 C5 DU1 B1201 55.140 22.221 129.764 1.00 83.48 C HETATM 6187 C6 DU1 B1201 55.304 23.333 128.747 1.00 83.97 C HETATM 6188 N2 DU1 B1201 56.291 22.985 127.733 1.00 84.94 N HETATM 6189 C7 DU1 B1201 56.126 23.266 126.436 1.00 86.51 C HETATM 6190 O2 DU1 B1201 55.120 23.829 126.010 1.00 87.18 O HETATM 6191 C8 DU1 B1201 57.205 22.828 125.494 1.00 87.68 C HETATM 6192 C13 DU1 B1201 57.868 21.615 125.677 1.00 88.32 C HETATM 6193 C12 DU1 B1201 58.848 21.199 124.793 1.00 89.43 C HETATM 6194 C11 DU1 B1201 59.163 21.992 123.700 1.00 89.31 C HETATM 6195 S DU1 B1201 60.402 21.478 122.547 1.00 90.08 S HETATM 6196 O1 DU1 B1201 61.104 20.363 123.146 1.00 91.02 O HETATM 6197 O DU1 B1201 61.182 22.651 122.221 1.00 90.31 O HETATM 6198 C10 DU1 B1201 58.505 23.194 123.487 1.00 88.78 C HETATM 6199 C9 DU1 B1201 57.528 23.603 124.380 1.00 88.85 C HETATM 6200 C1 OLA B1202 32.096 31.516 144.658 1.00 84.89 C HETATM 6201 O1 OLA B1202 31.712 31.079 143.551 1.00 84.27 O HETATM 6202 O2 OLA B1202 31.344 32.143 145.435 1.00 85.87 O HETATM 6203 C2 OLA B1202 33.529 31.275 145.073 1.00 84.82 C HETATM 6204 C3 OLA B1202 34.223 32.605 145.350 1.00 85.38 C HETATM 6205 C4 OLA B1202 35.716 32.422 145.618 1.00 85.94 C HETATM 6206 C5 OLA B1202 36.558 32.753 144.391 1.00 86.38 C HETATM 6207 C6 OLA B1202 38.051 32.633 144.681 1.00 87.03 C HETATM 6208 C7 OLA B1202 38.626 33.942 145.216 1.00 87.64 C HETATM 6209 C8 OLA B1202 40.029 33.757 145.788 1.00 87.97 C HETATM 6210 C9 OLA B1202 41.020 33.530 144.665 1.00 88.20 C HETATM 6211 C10 OLA B1202 42.334 33.438 144.884 1.00 88.04 C HETATM 6212 C11 OLA B1202 42.926 33.554 146.272 1.00 88.10 C HETATM 6213 C12 OLA B1202 44.446 33.431 146.205 1.00 88.54 C HETATM 6214 C13 OLA B1202 45.100 33.978 147.470 1.00 89.61 C HETATM 6215 C14 OLA B1202 46.624 33.897 147.400 1.00 90.58 C HETATM 6216 C15 OLA B1202 47.183 32.812 148.315 1.00 91.40 C HETATM 6217 C16 OLA B1202 48.708 32.825 148.303 1.00 92.07 C HETATM 6218 C17 OLA B1202 49.285 31.711 149.172 1.00 92.21 C HETATM 6219 C18 OLA B1202 50.610 32.116 149.784 1.00 92.48 C HETATM 6220 C1 OLA B1203 33.748 30.406 140.483 1.00 70.56 C HETATM 6221 O1 OLA B1203 33.126 31.235 139.788 1.00 71.37 O HETATM 6222 O2 OLA B1203 33.180 29.669 141.316 1.00 70.82 O HETATM 6223 C2 OLA B1203 35.244 30.281 140.305 1.00 70.61 C HETATM 6224 C3 OLA B1203 35.942 31.620 140.524 1.00 71.77 C HETATM 6225 C4 OLA B1203 37.434 31.408 140.771 1.00 72.97 C HETATM 6226 C5 OLA B1203 38.263 32.659 140.487 1.00 73.01 C HETATM 6227 C6 OLA B1203 39.758 32.363 140.617 1.00 73.60 C HETATM 6228 C7 OLA B1203 40.636 33.494 140.074 1.00 74.82 C HETATM 6229 C8 OLA B1203 41.860 32.985 139.311 1.00 74.81 C HETATM 6230 C9 OLA B1203 41.444 32.514 137.927 1.00 74.29 C HETATM 6231 C10 OLA B1203 42.186 32.639 136.818 1.00 72.57 C HETATM 6232 C11 OLA B1203 43.553 33.288 136.770 1.00 72.27 C HETATM 6233 C12 OLA B1203 44.615 32.442 137.470 1.00 71.93 C HETATM 6234 C13 OLA B1203 45.984 32.659 136.823 1.00 72.02 C HETATM 6235 C14 OLA B1203 47.162 32.313 137.737 1.00 72.10 C HETATM 6236 C15 OLA B1203 48.225 33.409 137.708 1.00 72.57 C HETATM 6237 C16 OLA B1203 49.512 32.967 138.399 1.00 73.07 C HETATM 6238 C17 OLA B1203 50.568 34.069 138.370 1.00 73.28 C HETATM 6239 C18 OLA B1203 51.908 33.565 138.865 1.00 72.69 C HETATM 6240 C1 OLA B1204 57.517 30.107 112.861 1.00 84.81 C HETATM 6241 O1 OLA B1204 58.209 29.103 112.580 1.00 83.92 O HETATM 6242 O2 OLA B1204 57.700 30.791 113.892 1.00 84.41 O HETATM 6243 C2 OLA B1204 56.409 30.512 111.912 1.00 84.65 C HETATM 6244 C3 OLA B1204 55.243 29.526 111.990 1.00 83.68 C HETATM 6245 C4 OLA B1204 53.917 30.207 112.318 1.00 83.25 C HETATM 6246 C5 OLA B1204 52.832 29.173 112.604 1.00 82.38 C HETATM 6247 C6 OLA B1204 51.480 29.828 112.870 1.00 82.53 C HETATM 6248 C7 OLA B1204 50.339 28.849 112.608 1.00 82.61 C HETATM 6249 C8 OLA B1204 49.013 29.341 113.184 1.00 82.68 C HETATM 6250 C9 OLA B1204 48.494 30.513 112.377 1.00 82.63 C HETATM 6251 C10 OLA B1204 47.302 31.065 112.617 1.00 82.27 C HETATM 6252 C11 OLA B1204 46.388 30.560 113.711 1.00 81.07 C CONECT 570 1244 CONECT 1244 570 CONECT 2571 2590 CONECT 2590 2571 CONECT 2657 6094 CONECT 3596 4270 CONECT 4270 3596 CONECT 5653 5672 CONECT 5672 5653 CONECT 5739 6195 CONECT 6064 6065 CONECT 6065 6064 6066 6080 CONECT 6066 6065 6067 6084 CONECT 6067 6066 6068 6077 CONECT 6068 6067 6069 6078 CONECT 6069 6068 6070 CONECT 6070 6069 6071 6077 CONECT 6071 6070 6072 6076 CONECT 6072 6071 6073 CONECT 6073 6072 6074 CONECT 6074 6073 6075 CONECT 6075 6074 6076 CONECT 6076 6071 6075 CONECT 6077 6067 6070 CONECT 6078 6068 6079 6080 CONECT 6079 6078 CONECT 6080 6065 6078 6081 CONECT 6081 6080 6082 CONECT 6082 6081 6083 CONECT 6083 6082 CONECT 6084 6066 6085 CONECT 6085 6084 6086 CONECT 6086 6085 6087 CONECT 6087 6086 6088 CONECT 6088 6087 6089 6090 CONECT 6089 6088 CONECT 6090 6088 6091 6098 CONECT 6091 6090 6092 CONECT 6092 6091 6093 CONECT 6093 6092 6094 6097 CONECT 6094 2657 6093 6095 6096 CONECT 6095 6094 CONECT 6096 6094 CONECT 6097 6093 6098 CONECT 6098 6090 6097 CONECT 6099 6100 6101 6102 CONECT 6100 6099 CONECT 6101 6099 CONECT 6102 6099 6103 CONECT 6103 6102 6104 CONECT 6104 6103 6105 CONECT 6105 6104 6106 CONECT 6106 6105 6107 CONECT 6107 6106 6108 CONECT 6108 6107 6109 CONECT 6109 6108 6110 CONECT 6110 6109 6111 CONECT 6111 6110 6112 CONECT 6112 6111 6113 CONECT 6113 6112 6114 CONECT 6114 6113 6115 CONECT 6115 6114 6116 CONECT 6116 6115 6117 CONECT 6117 6116 6118 CONECT 6118 6117 CONECT 6119 6120 6121 6122 CONECT 6120 6119 CONECT 6121 6119 CONECT 6122 6119 6123 CONECT 6123 6122 6124 CONECT 6124 6123 6125 CONECT 6125 6124 6126 CONECT 6126 6125 6127 CONECT 6127 6126 6128 CONECT 6128 6127 6129 CONECT 6129 6128 6130 CONECT 6130 6129 6131 CONECT 6131 6130 6132 CONECT 6132 6131 6133 CONECT 6133 6132 6134 CONECT 6134 6133 6135 CONECT 6135 6134 6136 CONECT 6136 6135 6137 CONECT 6137 6136 6138 CONECT 6138 6137 CONECT 6139 6140 6141 6142 CONECT 6140 6139 CONECT 6141 6139 CONECT 6142 6139 6143 CONECT 6143 6142 6144 CONECT 6144 6143 6145 CONECT 6145 6144 6146 CONECT 6146 6145 6147 CONECT 6147 6146 6148 CONECT 6148 6147 6149 CONECT 6149 6148 6150 CONECT 6150 6149 6151 CONECT 6151 6150 6152 CONECT 6152 6151 CONECT 6153 6154 6155 6156 CONECT 6154 6153 CONECT 6155 6153 CONECT 6156 6153 6157 CONECT 6157 6156 6158 CONECT 6158 6157 6159 CONECT 6159 6158 6160 CONECT 6160 6159 6161 CONECT 6161 6160 6162 CONECT 6162 6161 6163 CONECT 6163 6162 6164 CONECT 6164 6163 CONECT 6165 6166 CONECT 6166 6165 6167 6181 CONECT 6167 6166 6168 6185 CONECT 6168 6167 6169 6178 CONECT 6169 6168 6170 6179 CONECT 6170 6169 6171 CONECT 6171 6170 6172 6178 CONECT 6172 6171 6173 6177 CONECT 6173 6172 6174 CONECT 6174 6173 6175 CONECT 6175 6174 6176 CONECT 6176 6175 6177 CONECT 6177 6172 6176 CONECT 6178 6168 6171 CONECT 6179 6169 6180 6181 CONECT 6180 6179 CONECT 6181 6166 6179 6182 CONECT 6182 6181 6183 CONECT 6183 6182 6184 CONECT 6184 6183 CONECT 6185 6167 6186 CONECT 6186 6185 6187 CONECT 6187 6186 6188 CONECT 6188 6187 6189 CONECT 6189 6188 6190 6191 CONECT 6190 6189 CONECT 6191 6189 6192 6199 CONECT 6192 6191 6193 CONECT 6193 6192 6194 CONECT 6194 6193 6195 6198 CONECT 6195 5739 6194 6196 6197 CONECT 6196 6195 CONECT 6197 6195 CONECT 6198 6194 6199 CONECT 6199 6191 6198 CONECT 6200 6201 6202 6203 CONECT 6201 6200 CONECT 6202 6200 CONECT 6203 6200 6204 CONECT 6204 6203 6205 CONECT 6205 6204 6206 CONECT 6206 6205 6207 CONECT 6207 6206 6208 CONECT 6208 6207 6209 CONECT 6209 6208 6210 CONECT 6210 6209 6211 CONECT 6211 6210 6212 CONECT 6212 6211 6213 CONECT 6213 6212 6214 CONECT 6214 6213 6215 CONECT 6215 6214 6216 CONECT 6216 6215 6217 CONECT 6217 6216 6218 CONECT 6218 6217 6219 CONECT 6219 6218 CONECT 6220 6221 6222 6223 CONECT 6221 6220 CONECT 6222 6220 CONECT 6223 6220 6224 CONECT 6224 6223 6225 CONECT 6225 6224 6226 CONECT 6226 6225 6227 CONECT 6227 6226 6228 CONECT 6228 6227 6229 CONECT 6229 6228 6230 CONECT 6230 6229 6231 CONECT 6231 6230 6232 CONECT 6232 6231 6233 CONECT 6233 6232 6234 CONECT 6234 6233 6235 CONECT 6235 6234 6236 CONECT 6236 6235 6237 CONECT 6237 6236 6238 CONECT 6238 6237 6239 CONECT 6239 6238 CONECT 6240 6241 6242 6243 CONECT 6241 6240 CONECT 6242 6240 CONECT 6243 6240 6244 CONECT 6244 6243 6245 CONECT 6245 6244 6246 CONECT 6246 6245 6247 CONECT 6247 6246 6248 CONECT 6248 6247 6249 CONECT 6249 6248 6250 CONECT 6250 6249 6251 CONECT 6251 6250 6252 CONECT 6252 6251 MASTER 373 0 9 39 4 0 14 6 6250 2 199 64 END