HEADER TRANSFERASE 30-APR-15 5A1G TITLE THE STRUCTURE OF HUMAN MAT2A IN COMPLEX WITH S-ADENOSYLETHIONINE TITLE 2 AND PPNP. COMPND MOL_ID: 1; COMPND 2 MOLECULE: S-ADENOSYLMETHIONINE SYNTHASE ISOFORM TYPE-2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADOMET SYNTHASE 2, METHIONINE ADENOSYLTRANSFERASE 2, MAT COMPND 5 2, METHIONINE ADENOSYLTRANSFERASE II, MAT-II, METHIONINE COMPND 6 ADENOSYLTRANSFERASE 2A; COMPND 7 EC: 2.5.1.6; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4 KEYWDS TRANSFERASE, METHIONINE ADENOSYLTRANSFERASE, CELL GROWTH, LIVER KEYWDS 2 CANCER, METHYLATION EXPDTA X-RAY DIFFRACTION AUTHOR B.MURRAY,S.V.ANTONYUK,A.MARINA,S.C.LU,J.M.MATO,S.S.HASNAIN,A.L.ROJAS REVDAT 2 09-MAR-16 5A1G 1 JRNL REVDAT 1 17-FEB-16 5A1G 0 JRNL AUTH B.MURRAY,S.V.ANTONYUK,A.MARINA,S.C.LU,J.M.MATO,S.S.HASNAIN, JRNL AUTH 2 A.L.ROJAS JRNL TITL CRYSTALLOGRAPHY CAPTURES CATALYTIC STEPS IN HUMAN JRNL TITL 2 METHIONINE ADENOSYLTRANSFERASE ENZYMES. JRNL REF PROC.NATL.ACAD.SCI.USA V. 113 2104 2016 JRNL REFN ISSN 0027-8424 JRNL PMID 26858410 JRNL DOI 10.1073/PNAS.1510959113 REMARK 2 REMARK 2 RESOLUTION. 1.83 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0135 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU, REMARK 3 STEINER,NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.69 REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE REMARK 3 COMPLETENESS FOR RANGE (%) : 99.37 REMARK 3 NUMBER OF REFLECTIONS : 32055 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) : 0.12248 REMARK 3 R VALUE (WORKING SET) : 0.11982 REMARK 3 FREE R VALUE : 0.17490 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.8 REMARK 3 FREE R VALUE TEST SET COUNT : 1633 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) : 1.830 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.878 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2356 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72 REMARK 3 BIN R VALUE (WORKING SET) : 0.177 REMARK 3 BIN FREE R VALUE SET COUNT : 133 REMARK 3 BIN FREE R VALUE : 0.264 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2954 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 65 REMARK 3 SOLVENT ATOMS : 277 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.783 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.06 REMARK 3 B22 (A**2) : -0.38 REMARK 3 B33 (A**2) : -2.68 REMARK 3 B12 (A**2) : 0.00 REMARK 3 B13 (A**2) : 0.00 REMARK 3 B23 (A**2) : 0.00 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.297 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.105 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.260 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.979 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3134 ; 0.008 ; 0.019 REMARK 3 BOND LENGTHS OTHERS (A): 3033 ; 0.002 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4254 ; 1.376 ; 1.984 REMARK 3 BOND ANGLES OTHERS (DEGREES): 6975 ; 0.913 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 391 ; 6.268 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 139 ;36.702 ;23.453 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 540 ;12.279 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;20.264 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 471 ; 0.081 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3524 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 710 ; 0.002 ; 0.020 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): 1540 ; 1.592 ; 1.847 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1539 ; 1.591 ; 1.846 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1930 ; 1.966 ; 2.772 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1931 ; 1.966 ; 2.774 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1594 ; 2.178 ; 2.139 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1595 ; 2.178 ; 2.140 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2322 ; 2.664 ; 3.111 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3571 ; 3.773 ;15.829 REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3572 ; 3.772 ;15.831 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 6164 ; 1.150 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 88 ;35.870 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6296 ; 9.726 ; 5.000 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 : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY REMARK 4 REMARK 4 5A1G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-16. REMARK 100 THE PDBE ID CODE IS EBI-63718. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-AUG-14 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.92 REMARK 200 MONOCHROMATOR : SI111 REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL (PILATUS 6M) REMARK 200 DETECTOR MANUFACTURER : DECTRIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32401 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.83 REMARK 200 RESOLUTION RANGE LOW (A) : 29.34 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 13.3 REMARK 200 R MERGE (I) : 0.10 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 21.50 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5 REMARK 200 DATA REDUNDANCY IN SHELL : 12.5 REMARK 200 R MERGE FOR SHELL (I) : 0.81 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.40 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 2P02 REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE PH 7.0, 50 % MPD REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 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,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-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 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 34.19500 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.19500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 58.69500 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.19500 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.19500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.69500 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 34.19500 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.19500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.69500 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 34.19500 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.19500 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.69500 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 23850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 45230 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -230.1 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 117.39000 REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 117.39000 REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A2207 LIES ON A SPECIAL POSITION. REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 ASN A 2 REMARK 465 GLY A 3 REMARK 465 GLN A 4 REMARK 465 LEU A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 PHE A 8 REMARK 465 HIS A 9 REMARK 465 GLU A 10 REMARK 465 ALA A 11 REMARK 465 PHE A 12 REMARK 465 ILE A 13 REMARK 465 GLU A 14 REMARK 465 GLU A 15 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 2076 O HOH A 2076 3556 0.58 REMARK 500 REMARK 500 REMARK: NULL 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 THR A 62 115.19 -38.70 REMARK 500 VAL A 226 -68.15 -107.33 REMARK 500 PHE A 250 61.03 -157.60 REMARK 500 THR A 270 -100.45 -119.15 REMARK 500 ARG A 292 -64.47 -90.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 K A 405 K REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 57 OE2 REMARK 620 2 HOH A2014 O 66.5 REMARK 620 3 ASP A 258 OD1 157.8 135.7 REMARK 620 4 PPK A 402 O1B 95.6 64.4 97.2 REMARK 620 5 HOH A2015 O 120.5 54.1 81.6 61.3 REMARK 620 6 ALA A 259 O 104.5 71.2 85.5 117.6 57.5 REMARK 620 7 HOH A2035 O 81.3 141.6 77.5 142.8 149.7 98.8 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 406 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PPK A 402 O2G REMARK 620 2 HOH A2014 O 101.4 REMARK 620 3 PPK A 402 O2A 90.7 167.5 REMARK 620 4 PPK A 402 O1B 88.2 93.7 89.8 REMARK 620 5 HOH A2015 O 176.8 81.7 86.3 90.7 REMARK 620 6 ASP A 31 OD2 92.2 92.7 83.5 173.3 88.5 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 407 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 PPK A 402 O4A REMARK 620 2 PPK A 402 O1G 88.5 REMARK 620 3 HOH A2006 O 84.3 155.0 REMARK 620 4 HOH A2008 O 82.0 78.0 77.3 REMARK 620 5 HOH A2273 O 90.7 119.9 84.1 160.6 REMARK 620 6 HOH A2276 O 160.6 96.7 83.2 80.8 102.7 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PPK A 402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S7M A 404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 407 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5A19 RELATED DB: PDB REMARK 900 THE STRUCTURE OF MAT2A IN COMPLEX WITH PPNP. REMARK 900 RELATED ID: 5A1I RELATED DB: PDB REMARK 900 THE STRUCTURE OF HUMAB MAT2A IN COMPLEX WITH SAME, REMARK 900 ADENOSINE, METHIONINE AND PPNP. DBREF 5A1G A 1 395 UNP P31153 METK2_HUMAN 1 395 SEQRES 1 A 395 MET ASN GLY GLN LEU ASN GLY PHE HIS GLU ALA PHE ILE SEQRES 2 A 395 GLU GLU GLY THR PHE LEU PHE THR SER GLU SER VAL GLY SEQRES 3 A 395 GLU GLY HIS PRO ASP LYS ILE CYS ASP GLN ILE SER ASP SEQRES 4 A 395 ALA VAL LEU ASP ALA HIS LEU GLN GLN ASP PRO ASP ALA SEQRES 5 A 395 LYS VAL ALA CYS GLU THR VAL ALA LYS THR GLY MET ILE SEQRES 6 A 395 LEU LEU ALA GLY GLU ILE THR SER ARG ALA ALA VAL ASP SEQRES 7 A 395 TYR GLN LYS VAL VAL ARG GLU ALA VAL LYS HIS ILE GLY SEQRES 8 A 395 TYR ASP ASP SER SER LYS GLY PHE ASP TYR LYS THR CYS SEQRES 9 A 395 ASN VAL LEU VAL ALA LEU GLU GLN GLN SER PRO ASP ILE SEQRES 10 A 395 ALA GLN GLY VAL HIS LEU ASP ARG ASN GLU GLU ASP ILE SEQRES 11 A 395 GLY ALA GLY ASP GLN GLY LEU MET PHE GLY TYR ALA THR SEQRES 12 A 395 ASP GLU THR GLU GLU CYS MET PRO LEU THR ILE VAL LEU SEQRES 13 A 395 ALA HIS LYS LEU ASN ALA LYS LEU ALA GLU LEU ARG ARG SEQRES 14 A 395 ASN GLY THR LEU PRO TRP LEU ARG PRO ASP SER LYS THR SEQRES 15 A 395 GLN VAL THR VAL GLN TYR MET GLN ASP ARG GLY ALA VAL SEQRES 16 A 395 LEU PRO ILE ARG VAL HIS THR ILE VAL ILE SER VAL GLN SEQRES 17 A 395 HIS ASP GLU GLU VAL CYS LEU ASP GLU MET ARG ASP ALA SEQRES 18 A 395 LEU LYS GLU LYS VAL ILE LYS ALA VAL VAL PRO ALA LYS SEQRES 19 A 395 TYR LEU ASP GLU ASP THR ILE TYR HIS LEU GLN PRO SER SEQRES 20 A 395 GLY ARG PHE VAL ILE GLY GLY PRO GLN GLY ASP ALA GLY SEQRES 21 A 395 LEU THR GLY ARG LYS ILE ILE VAL ASP THR TYR GLY GLY SEQRES 22 A 395 TRP GLY ALA HIS GLY GLY GLY ALA PHE SER GLY LYS ASP SEQRES 23 A 395 TYR THR LYS VAL ASP ARG SER ALA ALA TYR ALA ALA ARG SEQRES 24 A 395 TRP VAL ALA LYS SER LEU VAL LYS GLY GLY LEU CYS ARG SEQRES 25 A 395 ARG VAL LEU VAL GLN VAL SER TYR ALA ILE GLY VAL SER SEQRES 26 A 395 HIS PRO LEU SER ILE SER ILE PHE HIS TYR GLY THR SER SEQRES 27 A 395 GLN LYS SER GLU ARG GLU LEU LEU GLU ILE VAL LYS LYS SEQRES 28 A 395 ASN PHE ASP LEU ARG PRO GLY VAL ILE VAL ARG ASP LEU SEQRES 29 A 395 ASP LEU LYS LYS PRO ILE TYR GLN ARG THR ALA ALA TYR SEQRES 30 A 395 GLY HIS PHE GLY ARG ASP SER PHE PRO TRP GLU VAL PRO SEQRES 31 A 395 LYS LYS LEU LYS TYR HET MPD A 400 8 HET MPD A 401 8 HET PPK A 402 13 HET IMD A 403 5 HET S7M A 404 28 HET K A 405 1 HET MG A 406 1 HET MG A 407 1 HETNAM IMD IMIDAZOLE HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL HETNAM K POTASSIUM ION HETNAM PPK (DIPHOSPHONO)AMINOPHOSPHONIC ACID HETNAM S7M [(3S)-3-AMINO-3-CARBOXYPROPYL]{[(2S,3S,4R,5R) HETNAM 2 S7M -5-(6-AMINO-9H-PURIN-9-YL)-3,4- HETNAM 3 S7M DIHYDROXYTETRAHYDROFURAN-2-YL]METHYL} HETNAM 4 S7M ETHYLSULFONIUM HETNAM MG MAGNESIUM ION HETSYN S7M S-ADENOSYL ETHIONINE FORMUL 2 IMD C3 H5 N2 1+ FORMUL 3 MPD 2(C6 H14 O2) FORMUL 4 PPK H6 N O9 P3 FORMUL 5 S7M C16 H25 N6 O5 S 1+ FORMUL 6 MG 2(MG 2+) FORMUL 7 K K 1+ FORMUL 8 HOH *277(H2 O) HELIX 1 1 HIS A 29 ASP A 49 1 21 HELIX 2 2 ASP A 78 GLY A 91 1 14 HELIX 3 3 SER A 95 GLY A 98 5 4 HELIX 4 4 SER A 114 HIS A 122 1 9 HELIX 5 5 ASN A 126 ILE A 130 5 5 HELIX 6 6 PRO A 151 ASN A 170 1 20 HELIX 7 7 CYS A 214 LYS A 225 1 12 HELIX 8 8 VAL A 226 VAL A 231 1 6 HELIX 9 9 PRO A 232 LEU A 236 5 5 HELIX 10 10 GLY A 253 GLY A 257 5 5 HELIX 11 11 LYS A 289 GLY A 308 1 20 HELIX 12 12 SER A 341 PHE A 353 1 13 HELIX 13 13 ARG A 356 LEU A 364 1 9 HELIX 14 14 TYR A 371 ALA A 375 5 5 HELIX 15 15 PHE A 385 VAL A 389 5 5 SHEET 1 AA 4 THR A 17 VAL A 25 0 SHEET 2 AA 4 LEU A 176 ASP A 191 -1 O THR A 182 N SER A 24 SHEET 3 AA 4 ALA A 194 HIS A 209 -1 O ALA A 194 N ASP A 191 SHEET 4 AA 4 ILE A 241 LEU A 244 1 O ILE A 241 N ILE A 203 SHEET 1 AB 4 ASN A 105 GLU A 111 0 SHEET 2 AB 4 MET A 64 THR A 72 1 O ILE A 65 N LEU A 107 SHEET 3 AB 4 LYS A 53 LYS A 61 -1 O LYS A 53 N THR A 72 SHEET 4 AB 4 GLY A 260 LEU A 261 -1 O GLY A 260 N ALA A 60 SHEET 1 AC 2 ASP A 93 ASP A 94 0 SHEET 2 AC 2 PHE A 99 ASP A 100 -1 O PHE A 99 N ASP A 94 SHEET 1 AD 3 GLY A 136 THR A 143 0 SHEET 2 AD 3 ARG A 313 TYR A 320 -1 O VAL A 314 N ALA A 142 SHEET 3 AD 3 SER A 329 PHE A 333 -1 O SER A 329 N SER A 319 LINK O2A PPK A 402 MG MG A 406 1555 1555 2.04 LINK O4A PPK A 402 MG MG A 407 1555 1555 2.02 LINK O1B PPK A 402 MG MG A 406 1555 1555 2.08 LINK O1G PPK A 402 MG MG A 407 1555 1555 2.29 LINK O2G PPK A 402 MG MG A 406 1555 1555 2.01 LINK K K A 405 O ALA A 259 1555 1555 2.89 LINK K K A 405 O HOH A2035 1555 2555 2.97 LINK K K A 405 OE2 GLU A 57 1555 2555 2.89 LINK K K A 405 O HOH A2014 1555 1555 3.09 LINK K K A 405 OD1 ASP A 258 1555 1555 2.76 LINK K K A 405 O1B PPK A 402 1555 1555 2.73 LINK K K A 405 O HOH A2015 1555 1555 3.12 LINK MG MG A 406 O HOH A2015 1555 1555 2.13 LINK MG MG A 406 OD2 ASP A 31 1555 1555 2.14 LINK MG MG A 406 O HOH A2014 1555 1555 2.18 LINK MG MG A 407 O HOH A2008 1555 1555 2.40 LINK MG MG A 407 O HOH A2273 1555 1555 2.00 LINK MG MG A 407 O HOH A2276 1555 1555 1.90 LINK MG MG A 407 O HOH A2006 1555 1555 2.66 SITE 1 AC1 4 GLY A 273 GLY A 275 ARG A 313 TYR A 335 SITE 1 AC2 21 HIS A 29 ASP A 31 ASP A 134 LYS A 181 SITE 2 AC2 21 ARG A 264 LYS A 265 GLY A 280 ALA A 281 SITE 3 AC2 21 LYS A 285 ASP A 291 S7M A 404 K A 405 SITE 4 AC2 21 MG A 406 MG A 407 HOH A2008 HOH A2015 SITE 5 AC2 21 HOH A2208 HOH A2209 HOH A2273 HOH A2274 SITE 6 AC2 21 HOH A2275 SITE 1 AC3 4 PHE A 18 GLN A 190 GLU A 342 HOH A2154 SITE 1 AC4 24 HIS A 29 PRO A 30 ALA A 55 GLU A 70 SITE 2 AC4 24 GLN A 113 ASP A 116 ILE A 117 GLY A 133 SITE 3 AC4 24 ASP A 134 ASP A 179 LYS A 181 SER A 247 SITE 4 AC4 24 ARG A 249 PHE A 250 ASP A 258 LYS A 289 SITE 5 AC4 24 ILE A 322 PPK A 402 HOH A2040 HOH A2106 SITE 6 AC4 24 HOH A2204 HOH A2206 HOH A2274 HOH A2277 SITE 1 AC5 7 GLU A 57 ASP A 258 ALA A 259 PPK A 402 SITE 2 AC5 7 MG A 406 HOH A2014 HOH A2035 SITE 1 AC6 6 ASP A 31 LYS A 265 PPK A 402 K A 405 SITE 2 AC6 6 HOH A2014 HOH A2015 SITE 1 AC7 6 ASP A 291 PPK A 402 HOH A2006 HOH A2008 SITE 2 AC7 6 HOH A2273 HOH A2276 CRYST1 68.390 94.390 117.390 90.00 90.00 90.00 I 2 2 2 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 0.014622 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010594 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008519 0.00000 ATOM 1 N GLY A 16 -7.748 11.739 5.464 1.00 29.13 N ANISOU 1 N GLY A 16 2905 4377 3785 262 -658 -239 N ATOM 2 CA GLY A 16 -6.301 11.783 5.842 1.00 29.09 C ANISOU 2 CA GLY A 16 3272 4314 3466 40 -1178 -486 C ATOM 3 C GLY A 16 -5.934 12.260 7.237 1.00 31.89 C ANISOU 3 C GLY A 16 4190 4532 3394 507 -1478 -413 C ATOM 4 O GLY A 16 -4.790 12.061 7.650 1.00 40.15 O ANISOU 4 O GLY A 16 4443 5926 4884 1527 -1567 -586 O ATOM 5 N THR A 17 -6.855 12.903 7.962 1.00 29.92 N ANISOU 5 N THR A 17 3729 4003 3634 336 -1261 167 N ATOM 6 CA THR A 17 -6.558 13.388 9.320 1.00 27.06 C ANISOU 6 CA THR A 17 3349 3541 3389 58 -593 344 C ATOM 7 C THR A 17 -7.244 12.580 10.410 1.00 23.97 C ANISOU 7 C THR A 17 2941 2976 3188 86 -744 166 C ATOM 8 O THR A 17 -8.272 11.945 10.181 1.00 23.31 O ANISOU 8 O THR A 17 2777 3315 2762 -137 -433 662 O ATOM 9 CB THR A 17 -6.938 14.871 9.527 1.00 27.91 C ANISOU 9 CB THR A 17 2669 3862 4070 504 -693 360 C ATOM 10 OG1 THR A 17 -8.358 15.030 9.437 1.00 27.16 O ANISOU 10 OG1 THR A 17 2506 3428 4386 150 -539 1118 O ATOM 11 CG2 THR A 17 -6.245 15.767 8.508 1.00 34.48 C ANISOU 11 CG2 THR A 17 4272 4272 4555 357 -352 835 C ATOM 12 N PHE A 18 -6.657 12.623 11.599 1.00 20.07 N ANISOU 12 N PHE A 18 2584 2323 2718 9 -184 111 N ATOM 13 CA PHE A 18 -7.190 11.920 12.764 1.00 19.04 C ANISOU 13 CA PHE A 18 2371 2178 2684 115 -215 137 C ATOM 14 C PHE A 18 -6.770 12.624 14.052 1.00 17.91 C ANISOU 14 C PHE A 18 2065 1941 2796 48 -295 190 C ATOM 15 O PHE A 18 -5.812 13.411 14.058 1.00 18.49 O ANISOU 15 O PHE A 18 2179 1956 2887 -45 -266 255 O ATOM 16 CB PHE A 18 -6.719 10.458 12.775 1.00 16.80 C ANISOU 16 CB PHE A 18 1830 2120 2432 -46 -169 52 C ATOM 17 CG PHE A 18 -5.222 10.288 12.918 1.00 17.41 C ANISOU 17 CG PHE A 18 1785 2112 2716 -153 -77 85 C ATOM 18 CD1 PHE A 18 -4.389 10.382 11.807 1.00 18.75 C ANISOU 18 CD1 PHE A 18 1854 2480 2790 46 -17 -77 C ATOM 19 CD2 PHE A 18 -4.651 10.018 14.161 1.00 15.43 C ANISOU 19 CD2 PHE A 18 1414 1899 2549 -277 118 15 C ATOM 20 CE1 PHE A 18 -3.015 10.218 11.929 1.00 19.40 C ANISOU 20 CE1 PHE A 18 1793 2431 3146 53 216 -59 C ATOM 21 CE2 PHE A 18 -3.277 9.852 14.290 1.00 16.05 C ANISOU 21 CE2 PHE A 18 1581 1861 2657 129 -98 161 C ATOM 22 CZ PHE A 18 -2.461 9.958 13.174 1.00 19.63 C ANISOU 22 CZ PHE A 18 2142 2330 2985 207 345 -25 C ATOM 23 N LEU A 19 -7.486 12.323 15.134 1.00 17.19 N ANISOU 23 N LEU A 19 1891 1926 2714 127 -370 173 N ATOM 24 CA LEU A 19 -7.150 12.825 16.469 1.00 17.41 C ANISOU 24 CA LEU A 19 2115 1892 2605 39 -364 306 C ATOM 25 C LEU A 19 -6.372 11.781 17.273 1.00 16.83 C ANISOU 25 C LEU A 19 2174 1524 2694 -123 -348 301 C ATOM 26 O LEU A 19 -6.610 10.586 17.133 1.00 16.52 O ANISOU 26 O LEU A 19 2137 1417 2722 65 -375 263 O ATOM 27 CB LEU A 19 -8.423 13.201 17.221 1.00 17.91 C ANISOU 27 CB LEU A 19 2350 1987 2465 -24 -228 201 C ATOM 28 CG LEU A 19 -9.294 14.259 16.545 1.00 19.07 C ANISOU 28 CG LEU A 19 2435 2137 2671 132 -325 175 C ATOM 29 CD1 LEU A 19 -10.540 14.552 17.372 1.00 18.80 C ANISOU 29 CD1 LEU A 19 2284 1934 2925 1235 -657 1050 C ATOM 30 CD2 LEU A 19 -8.510 15.538 16.304 1.00 17.93 C ANISOU 30 CD2 LEU A 19 2320 2020 2469 274 0 116 C ATOM 31 N PHE A 20 -5.439 12.244 18.106 1.00 14.79 N ANISOU 31 N PHE A 20 1559 1761 2299 267 -113 368 N ATOM 32 CA PHE A 20 -4.808 11.390 19.109 1.00 14.55 C ANISOU 32 CA PHE A 20 1608 1793 2128 82 -80 430 C ATOM 33 C PHE A 20 -4.654 12.206 20.382 1.00 13.89 C ANISOU 33 C PHE A 20 1593 1489 2194 123 115 434 C ATOM 34 O PHE A 20 -4.274 13.384 20.328 1.00 15.53 O ANISOU 34 O PHE A 20 1876 1496 2527 36 -85 477 O ATOM 35 CB PHE A 20 -3.431 10.892 18.633 1.00 14.86 C ANISOU 35 CB PHE A 20 1708 1944 1993 78 51 297 C ATOM 36 CG PHE A 20 -3.016 9.572 19.238 1.00 16.18 C ANISOU 36 CG PHE A 20 1802 1951 2394 119 79 385 C ATOM 37 CD1 PHE A 20 -2.456 9.507 20.516 1.00 16.65 C ANISOU 37 CD1 PHE A 20 1967 1945 2411 -51 93 313 C ATOM 38 CD2 PHE A 20 -3.201 8.383 18.531 1.00 15.35 C ANISOU 38 CD2 PHE A 20 1748 1924 2160 135 14 485 C ATOM 39 CE1 PHE A 20 -2.075 8.282 21.067 1.00 17.04 C ANISOU 39 CE1 PHE A 20 2139 2173 2161 50 260 484 C ATOM 40 CE2 PHE A 20 -2.824 7.153 19.074 1.00 16.10 C ANISOU 40 CE2 PHE A 20 1863 1676 2578 -54 33 436 C ATOM 41 CZ PHE A 20 -2.269 7.102 20.347 1.00 16.97 C ANISOU 41 CZ PHE A 20 1965 2046 2436 -43 179 549 C ATOM 42 N THR A 21 -4.915 11.567 21.516 1.00 14.19 N ANISOU 42 N THR A 21 1617 1575 2199 27 67 455 N ATOM 43 CA THR A 21 -4.871 12.207 22.826 1.00 15.12 C ANISOU 43 CA THR A 21 1852 1549 2343 68 210 244 C ATOM 44 C THR A 21 -3.850 11.516 23.744 1.00 14.01 C ANISOU 44 C THR A 21 1852 1028 2441 4 220 208 C ATOM 45 O THR A 21 -3.796 10.295 23.781 1.00 15.37 O ANISOU 45 O THR A 21 2049 1006 2783 18 193 19 O ATOM 46 CB THR A 21 -6.273 12.150 23.450 1.00 15.97 C ANISOU 46 CB THR A 21 1889 1794 2383 -47 205 143 C ATOM 47 OG1 THR A 21 -7.195 12.836 22.587 1.00 16.72 O ANISOU 47 OG1 THR A 21 2033 1642 2675 -33 106 203 O ATOM 48 CG2 THR A 21 -6.293 12.771 24.851 1.00 17.81 C ANISOU 48 CG2 THR A 21 2392 2008 2364 50 133 95 C ATOM 49 N SER A 22 -3.040 12.311 24.458 1.00 15.92 N ANISOU 49 N SER A 22 1938 1625 2483 116 45 -102 N ATOM 50 CA SER A 22 -2.166 11.842 25.545 1.00 15.67 C ANISOU 50 CA SER A 22 1687 1823 2441 48 132 -86 C ATOM 51 C SER A 22 -2.312 12.733 26.789 1.00 15.80 C ANISOU 51 C SER A 22 1685 1898 2420 29 212 -80 C ATOM 52 O SER A 22 -2.718 13.904 26.683 1.00 16.14 O ANISOU 52 O SER A 22 1722 1799 2611 -59 211 -177 O ATOM 53 CB SER A 22 -0.684 11.860 25.127 1.00 15.20 C ANISOU 53 CB SER A 22 1721 1769 2283 9 207 -124 C ATOM 54 OG SER A 22 -0.456 11.152 23.929 1.00 15.57 O ANISOU 54 OG SER A 22 1968 1701 2247 -27 180 -79 O ATOM 55 N GLU A 23 -1.954 12.182 27.953 1.00 14.79 N ANISOU 55 N GLU A 23 1452 1878 2286 -66 290 -117 N ATOM 56 CA GLU A 23 -1.982 12.927 29.217 1.00 15.03 C ANISOU 56 CA GLU A 23 1830 1564 2316 -76 74 -59 C ATOM 57 C GLU A 23 -0.631 12.906 29.914 1.00 15.43 C ANISOU 57 C GLU A 23 1916 1679 2266 38 50 -67 C ATOM 58 O GLU A 23 0.271 12.134 29.556 1.00 15.06 O ANISOU 58 O GLU A 23 1560 1661 2501 -39 -30 96 O ATOM 59 CB GLU A 23 -3.062 12.376 30.162 1.00 15.86 C ANISOU 59 CB GLU A 23 1921 1674 2429 103 157 99 C ATOM 60 CG GLU A 23 -2.761 10.993 30.715 1.00 18.36 C ANISOU 60 CG GLU A 23 2472 1722 2782 -168 -10 374 C ATOM 61 CD GLU A 23 -3.768 10.482 31.730 1.00 18.62 C ANISOU 61 CD GLU A 23 2391 1692 2990 340 170 657 C ATOM 62 OE1 GLU A 23 -4.650 11.230 32.210 1.00 18.70 O ANISOU 62 OE1 GLU A 23 2472 1435 3195 -10 461 381 O ATOM 63 OE2 GLU A 23 -3.656 9.294 32.050 1.00 18.08 O ANISOU 63 OE2 GLU A 23 1934 1573 3360 91 86 598 O ATOM 64 N SER A 24 -0.510 13.771 30.914 1.00 16.05 N ANISOU 64 N SER A 24 2265 1500 2332 80 125 -44 N ATOM 65 CA SER A 24 0.625 13.766 31.830 1.00 16.90 C ANISOU 65 CA SER A 24 2132 1638 2649 172 73 -186 C ATOM 66 C SER A 24 0.125 14.244 33.183 1.00 15.22 C ANISOU 66 C SER A 24 1917 1449 2415 206 -53 117 C ATOM 67 O SER A 24 -0.975 14.798 33.289 1.00 15.21 O ANISOU 67 O SER A 24 2196 1209 2371 450 -44 251 O ATOM 68 CB SER A 24 1.742 14.665 31.290 1.00 17.59 C ANISOU 68 CB SER A 24 1909 2054 2718 165 16 -205 C ATOM 69 OG SER A 24 2.855 14.728 32.168 1.00 19.13 O ANISOU 69 OG SER A 24 1826 2189 3253 -74 -153 -183 O ATOM 70 N VAL A 25 0.926 14.034 34.217 1.00 15.28 N ANISOU 70 N VAL A 25 1843 1432 2528 438 -58 192 N ATOM 71 CA VAL A 25 0.589 14.505 35.559 1.00 13.83 C ANISOU 71 CA VAL A 25 1061 1644 2549 652 -15 168 C ATOM 72 C VAL A 25 1.777 15.220 36.185 1.00 15.82 C ANISOU 72 C VAL A 25 1976 1563 2471 159 -146 80 C ATOM 73 O VAL A 25 2.924 15.020 35.781 1.00 18.37 O ANISOU 73 O VAL A 25 1969 2034 2973 203 -120 95 O ATOM 74 CB VAL A 25 0.089 13.369 36.486 1.00 14.00 C ANISOU 74 CB VAL A 25 1604 1660 2055 355 -231 -6 C ATOM 75 CG1 VAL A 25 -1.090 12.625 35.865 1.00 14.39 C ANISOU 75 CG1 VAL A 25 1698 1755 2012 89 -25 16 C ATOM 76 CG2 VAL A 25 1.208 12.396 36.832 1.00 13.89 C ANISOU 76 CG2 VAL A 25 1404 1665 2208 313 31 96 C ATOM 77 N GLY A 26 1.490 16.032 37.192 1.00 15.62 N ANISOU 77 N GLY A 26 1951 1539 2444 86 -25 106 N ATOM 78 CA GLY A 26 2.516 16.815 37.875 1.00 16.86 C ANISOU 78 CA GLY A 26 1963 1940 2500 31 -96 43 C ATOM 79 C GLY A 26 3.261 16.032 38.938 1.00 16.89 C ANISOU 79 C GLY A 26 2212 1608 2597 -99 -165 120 C ATOM 80 O GLY A 26 2.898 14.898 39.269 1.00 16.10 O ANISOU 80 O GLY A 26 1902 1470 2742 -28 -352 51 O ATOM 81 N GLU A 27 4.291 16.660 39.498 1.00 17.23 N ANISOU 81 N GLU A 27 2045 1833 2666 17 -199 12 N ATOM 82 CA GLU A 27 5.122 16.021 40.519 1.00 17.06 C ANISOU 82 CA GLU A 27 2089 1744 2648 -146 -374 -75 C ATOM 83 C GLU A 27 4.369 15.672 41.807 1.00 17.60 C ANISOU 83 C GLU A 27 2493 1648 2546 85 -322 45 C ATOM 84 O GLU A 27 4.773 14.763 42.529 1.00 17.64 O ANISOU 84 O GLU A 27 2488 1687 2526 229 -241 -7 O ATOM 85 CB GLU A 27 6.306 16.911 40.893 1.00 18.83 C ANISOU 85 CB GLU A 27 2179 2149 2823 -315 -329 -335 C ATOM 86 CG GLU A 27 7.301 17.174 39.795 1.00 19.73 C ANISOU 86 CG GLU A 27 2013 2520 2964 -406 -327 -512 C ATOM 87 CD GLU A 27 8.262 18.292 40.171 1.00 21.46 C ANISOU 87 CD GLU A 27 2103 2633 3418 -574 -145 -581 C ATOM 88 OE1 GLU A 27 8.847 18.238 41.267 1.00 25.91 O ANISOU 88 OE1 GLU A 27 2622 3534 3687 -654 -519 -719 O ATOM 89 OE2 GLU A 27 8.419 19.245 39.393 1.00 23.69 O ANISOU 89 OE2 GLU A 27 2372 2157 4471 -788 -123 -504 O ATOM 90 N GLY A 28 3.300 16.409 42.105 1.00 15.79 N ANISOU 90 N GLY A 28 2631 787 2579 182 -508 956 N ATOM 91 CA GLY A 28 2.487 16.152 43.288 1.00 16.28 C ANISOU 91 CA GLY A 28 2289 1485 2412 -19 -441 172 C ATOM 92 C GLY A 28 1.252 15.301 43.075 1.00 15.82 C ANISOU 92 C GLY A 28 2033 1513 2465 125 -382 63 C ATOM 93 O GLY A 28 0.485 15.103 44.012 1.00 16.68 O ANISOU 93 O GLY A 28 2103 1939 2295 57 -468 -87 O ATOM 94 N HIS A 29 1.044 14.798 41.861 1.00 14.32 N ANISOU 94 N HIS A 29 1778 1386 2275 45 -102 214 N ATOM 95 CA HIS A 29 0.027 13.765 41.630 1.00 14.41 C ANISOU 95 CA HIS A 29 1635 1519 2319 78 -121 87 C ATOM 96 C HIS A 29 0.374 12.542 42.504 1.00 14.56 C ANISOU 96 C HIS A 29 1649 1389 2493 144 19 86 C ATOM 97 O HIS A 29 1.543 12.136 42.540 1.00 14.18 O ANISOU 97 O HIS A 29 1689 1050 2649 155 -145 -44 O ATOM 98 CB HIS A 29 -0.038 13.363 40.154 1.00 15.94 C ANISOU 98 CB HIS A 29 1825 1873 2358 119 -144 -6 C ATOM 99 CG HIS A 29 -1.115 12.367 39.865 1.00 16.98 C ANISOU 99 CG HIS A 29 1744 2334 2371 12 -243 -13 C ATOM 100 ND1 HIS A 29 -0.956 11.021 40.092 1.00 17.64 N ANISOU 100 ND1 HIS A 29 1035 2619 3047 295 -452 385 N ATOM 101 CD2 HIS A 29 -2.380 12.523 39.421 1.00 17.32 C ANISOU 101 CD2 HIS A 29 1835 2147 2597 271 -270 235 C ATOM 102 CE1 HIS A 29 -2.072 10.386 39.786 1.00 17.47 C ANISOU 102 CE1 HIS A 29 1749 2317 2570 -113 -446 216 C ATOM 103 NE2 HIS A 29 -2.951 11.276 39.368 1.00 18.81 N ANISOU 103 NE2 HIS A 29 2100 2224 2821 185 -207 194 N ATOM 104 N PRO A 30 -0.619 11.971 43.222 1.00 14.53 N ANISOU 104 N PRO A 30 1446 1544 2531 192 -67 147 N ATOM 105 CA PRO A 30 -0.328 10.915 44.214 1.00 14.42 C ANISOU 105 CA PRO A 30 1534 1691 2252 179 -166 95 C ATOM 106 C PRO A 30 0.432 9.688 43.682 1.00 13.93 C ANISOU 106 C PRO A 30 1356 1728 2207 173 -138 143 C ATOM 107 O PRO A 30 1.322 9.176 44.371 1.00 14.91 O ANISOU 107 O PRO A 30 1568 1766 2330 521 -122 87 O ATOM 108 CB PRO A 30 -1.710 10.504 44.743 1.00 16.05 C ANISOU 108 CB PRO A 30 1773 1979 2346 135 72 182 C ATOM 109 CG PRO A 30 -2.708 11.413 44.127 1.00 16.55 C ANISOU 109 CG PRO A 30 1813 1892 2583 47 -53 246 C ATOM 110 CD PRO A 30 -2.021 12.427 43.279 1.00 14.71 C ANISOU 110 CD PRO A 30 1454 1860 2274 222 75 72 C ATOM 111 N ASP A 31 0.059 9.192 42.501 1.00 13.03 N ANISOU 111 N ASP A 31 969 1868 2111 352 -116 220 N ATOM 112 CA ASP A 31 0.833 8.120 41.835 1.00 13.39 C ANISOU 112 CA ASP A 31 1213 1749 2126 129 209 158 C ATOM 113 C ASP A 31 2.305 8.533 41.550 1.00 13.83 C ANISOU 113 C ASP A 31 1233 1652 2369 -40 -3 247 C ATOM 114 O ASP A 31 3.251 7.763 41.807 1.00 14.05 O ANISOU 114 O ASP A 31 1443 1516 2378 51 -107 9 O ATOM 115 CB ASP A 31 0.156 7.669 40.537 1.00 13.74 C ANISOU 115 CB ASP A 31 1326 1712 2180 250 73 218 C ATOM 116 CG ASP A 31 -1.150 6.920 40.762 1.00 15.18 C ANISOU 116 CG ASP A 31 1631 1686 2449 -25 -97 149 C ATOM 117 OD1 ASP A 31 -1.349 6.282 41.819 1.00 15.54 O ANISOU 117 OD1 ASP A 31 1783 1719 2401 140 -57 127 O ATOM 118 OD2 ASP A 31 -1.996 6.949 39.844 1.00 15.42 O ANISOU 118 OD2 ASP A 31 1532 1532 2793 -129 -249 -24 O ATOM 119 N LYS A 32 2.494 9.738 41.031 1.00 14.17 N ANISOU 119 N LYS A 32 1559 1462 2360 48 -64 107 N ATOM 120 CA LYS A 32 3.847 10.253 40.752 1.00 15.55 C ANISOU 120 CA LYS A 32 1607 1684 2615 54 87 185 C ATOM 121 C LYS A 32 4.675 10.535 42.004 1.00 16.12 C ANISOU 121 C LYS A 32 2110 1558 2457 -1 57 195 C ATOM 122 O LYS A 32 5.907 10.398 41.965 1.00 16.69 O ANISOU 122 O LYS A 32 2221 1730 2389 430 59 20 O ATOM 123 CB LYS A 32 3.815 11.474 39.818 1.00 17.27 C ANISOU 123 CB LYS A 32 2039 2023 2498 25 -45 337 C ATOM 124 CG LYS A 32 4.532 11.249 38.489 1.00 18.09 C ANISOU 124 CG LYS A 32 1990 2293 2590 102 -60 190 C ATOM 125 CD LYS A 32 3.951 10.110 37.657 1.00 15.79 C ANISOU 125 CD LYS A 32 1011 2267 2721 332 -186 209 C ATOM 126 CE LYS A 32 4.885 9.705 36.528 1.00 16.74 C ANISOU 126 CE LYS A 32 1472 2316 2572 171 -90 112 C ATOM 127 NZ LYS A 32 5.994 8.830 37.012 1.00 16.42 N ANISOU 127 NZ LYS A 32 1773 2200 2265 143 -175 305 N ATOM 128 N ILE A 33 4.026 10.928 43.100 1.00 15.77 N ANISOU 128 N ILE A 33 1996 1513 2483 121 -77 101 N ATOM 129 CA ILE A 33 4.702 10.999 44.407 1.00 16.25 C ANISOU 129 CA ILE A 33 2250 1497 2425 138 -110 86 C ATOM 130 C ILE A 33 5.334 9.630 44.722 1.00 15.05 C ANISOU 130 C ILE A 33 1825 1625 2266 171 -257 23 C ATOM 131 O ILE A 33 6.508 9.551 45.080 1.00 14.21 O ANISOU 131 O ILE A 33 1758 1253 2387 108 -262 -44 O ATOM 132 CB ILE A 33 3.747 11.419 45.554 1.00 16.24 C ANISOU 132 CB ILE A 33 2329 1633 2209 -18 -164 37 C ATOM 133 CG1 ILE A 33 3.279 12.871 45.364 1.00 17.28 C ANISOU 133 CG1 ILE A 33 2576 1606 2383 -1 -86 -15 C ATOM 134 CG2 ILE A 33 4.428 11.279 46.918 1.00 17.08 C ANISOU 134 CG2 ILE A 33 2493 1903 2092 -88 -124 -32 C ATOM 135 CD1 ILE A 33 2.168 13.304 46.296 1.00 19.27 C ANISOU 135 CD1 ILE A 33 3070 1547 2702 270 180 -25 C ATOM 136 N CYS A 34 4.555 8.560 44.560 1.00 14.79 N ANISOU 136 N CYS A 34 1955 1529 2135 114 18 77 N ATOM 137 CA CYS A 34 5.042 7.205 44.850 1.00 14.46 C ANISOU 137 CA CYS A 34 1646 1645 2202 194 -111 73 C ATOM 138 C CYS A 34 6.213 6.774 43.949 1.00 14.65 C ANISOU 138 C CYS A 34 1709 1579 2278 12 58 89 C ATOM 139 O CYS A 34 7.181 6.189 44.442 1.00 14.64 O ANISOU 139 O CYS A 34 1820 1378 2364 -145 -93 260 O ATOM 140 CB CYS A 34 3.900 6.190 44.770 1.00 15.78 C ANISOU 140 CB CYS A 34 1935 1763 2295 -34 -30 84 C ATOM 141 SG CYS A 34 2.644 6.439 46.043 1.00 17.29 S ANISOU 141 SG CYS A 34 2032 1852 2684 125 141 -39 S ATOM 142 N ASP A 35 6.122 7.066 42.650 1.00 13.20 N ANISOU 142 N ASP A 35 1406 1388 2218 -79 287 -14 N ATOM 143 CA ASP A 35 7.213 6.772 41.700 1.00 13.21 C ANISOU 143 CA ASP A 35 1449 1573 1995 -270 279 -34 C ATOM 144 C ASP A 35 8.505 7.493 42.113 1.00 14.11 C ANISOU 144 C ASP A 35 1458 1748 2154 -194 109 -166 C ATOM 145 O ASP A 35 9.588 6.891 42.115 1.00 13.44 O ANISOU 145 O ASP A 35 1463 1562 2080 -197 64 -232 O ATOM 146 CB ASP A 35 6.842 7.191 40.263 1.00 13.17 C ANISOU 146 CB ASP A 35 1354 1546 2101 -50 201 44 C ATOM 147 CG ASP A 35 5.791 6.288 39.617 1.00 13.69 C ANISOU 147 CG ASP A 35 1593 1326 2280 -34 78 68 C ATOM 148 OD1 ASP A 35 5.791 5.059 39.866 1.00 14.65 O ANISOU 148 OD1 ASP A 35 1487 1373 2703 78 136 223 O ATOM 149 OD2 ASP A 35 4.973 6.816 38.817 1.00 14.23 O ANISOU 149 OD2 ASP A 35 1431 1525 2450 142 165 69 O ATOM 150 N GLN A 36 8.384 8.771 42.469 1.00 14.69 N ANISOU 150 N GLN A 36 1659 1719 2201 -85 86 -128 N ATOM 151 CA GLN A 36 9.557 9.561 42.891 1.00 15.13 C ANISOU 151 CA GLN A 36 1929 1659 2157 -170 20 -201 C ATOM 152 C GLN A 36 10.173 9.041 44.185 1.00 16.01 C ANISOU 152 C GLN A 36 2175 1620 2288 -88 -69 -164 C ATOM 153 O GLN A 36 11.401 8.958 44.295 1.00 16.41 O ANISOU 153 O GLN A 36 2184 1584 2465 -3 -119 -108 O ATOM 154 CB GLN A 36 9.195 11.028 43.039 1.00 16.23 C ANISOU 154 CB GLN A 36 2006 1793 2368 113 -48 -108 C ATOM 155 CG GLN A 36 8.988 11.731 41.713 1.00 16.87 C ANISOU 155 CG GLN A 36 2058 1822 2529 314 -112 -16 C ATOM 156 CD GLN A 36 8.270 13.055 41.883 1.00 17.96 C ANISOU 156 CD GLN A 36 2402 1601 2818 233 -94 49 C ATOM 157 OE1 GLN A 36 8.905 14.085 42.090 1.00 17.89 O ANISOU 157 OE1 GLN A 36 2128 1480 3189 307 21 217 O ATOM 158 NE2 GLN A 36 6.939 13.029 41.835 1.00 18.84 N ANISOU 158 NE2 GLN A 36 2390 1999 2769 2 -10 198 N ATOM 159 N ILE A 37 9.327 8.674 45.150 1.00 16.29 N ANISOU 159 N ILE A 37 2095 1730 2362 21 9 -183 N ATOM 160 CA ILE A 37 9.803 8.097 46.418 1.00 16.25 C ANISOU 160 CA ILE A 37 2140 1612 2419 -69 -33 -136 C ATOM 161 C ILE A 37 10.508 6.759 46.175 1.00 16.15 C ANISOU 161 C ILE A 37 2060 1664 2410 -88 19 -236 C ATOM 162 O ILE A 37 11.612 6.542 46.686 1.00 16.57 O ANISOU 162 O ILE A 37 2237 1620 2435 129 -125 -471 O ATOM 163 CB ILE A 37 8.671 7.973 47.472 1.00 16.14 C ANISOU 163 CB ILE A 37 2028 1697 2404 36 -64 -108 C ATOM 164 CG1 ILE A 37 8.274 9.371 47.973 1.00 16.61 C ANISOU 164 CG1 ILE A 37 2134 1685 2492 -15 -71 -128 C ATOM 165 CG2 ILE A 37 9.105 7.130 48.674 1.00 16.06 C ANISOU 165 CG2 ILE A 37 1841 1848 2410 39 -118 -103 C ATOM 166 CD1 ILE A 37 6.944 9.432 48.704 1.00 17.66 C ANISOU 166 CD1 ILE A 37 2203 2058 2449 130 -35 -150 C ATOM 167 N SER A 38 9.875 5.875 45.397 1.00 16.14 N ANISOU 167 N SER A 38 2194 1630 2309 -67 87 -268 N ATOM 168 CA SER A 38 10.466 4.578 45.062 1.00 14.52 C ANISOU 168 CA SER A 38 1844 1551 2120 -152 171 -52 C ATOM 169 C SER A 38 11.846 4.733 44.424 1.00 14.76 C ANISOU 169 C SER A 38 1710 1668 2228 -34 70 -154 C ATOM 170 O SER A 38 12.769 3.981 44.761 1.00 14.63 O ANISOU 170 O SER A 38 1334 1946 2278 -101 167 -62 O ATOM 171 CB SER A 38 9.534 3.767 44.143 1.00 14.84 C ANISOU 171 CB SER A 38 1669 1698 2269 -333 285 -35 C ATOM 172 OG SER A 38 8.384 3.291 44.840 1.00 15.55 O ANISOU 172 OG SER A 38 1708 1510 2690 13 595 169 O ATOM 173 N ASP A 39 11.997 5.719 43.537 1.00 16.27 N ANISOU 173 N ASP A 39 2090 1630 2460 62 187 -105 N ATOM 174 CA ASP A 39 13.297 5.981 42.896 1.00 16.72 C ANISOU 174 CA ASP A 39 2001 1619 2729 -135 98 -77 C ATOM 175 C ASP A 39 14.295 6.741 43.776 1.00 16.32 C ANISOU 175 C ASP A 39 1703 1968 2529 -90 256 -153 C ATOM 176 O ASP A 39 15.517 6.560 43.615 1.00 16.17 O ANISOU 176 O ASP A 39 1572 1893 2679 -196 61 -68 O ATOM 177 CB ASP A 39 13.122 6.658 41.524 1.00 17.23 C ANISOU 177 CB ASP A 39 2087 1660 2797 -55 135 -39 C ATOM 178 CG ASP A 39 12.768 5.669 40.420 1.00 16.99 C ANISOU 178 CG ASP A 39 2061 1666 2726 61 129 -12 C ATOM 179 OD1 ASP A 39 13.070 4.455 40.554 1.00 16.13 O ANISOU 179 OD1 ASP A 39 2163 1411 2554 -247 122 -336 O ATOM 180 OD2 ASP A 39 12.204 6.106 39.394 1.00 16.92 O ANISOU 180 OD2 ASP A 39 1757 1655 3016 255 261 310 O ATOM 181 N ALA A 40 13.802 7.574 44.694 1.00 17.39 N ANISOU 181 N ALA A 40 1865 1898 2842 18 205 -287 N ATOM 182 CA ALA A 40 14.658 8.146 45.752 1.00 16.95 C ANISOU 182 CA ALA A 40 2110 1883 2445 149 157 -119 C ATOM 183 C ALA A 40 15.286 7.043 46.614 1.00 15.70 C ANISOU 183 C ALA A 40 1550 1974 2442 96 29 -190 C ATOM 184 O ALA A 40 16.493 7.083 46.915 1.00 15.35 O ANISOU 184 O ALA A 40 1614 1742 2474 25 -165 -232 O ATOM 185 CB ALA A 40 13.877 9.123 46.621 1.00 16.79 C ANISOU 185 CB ALA A 40 2082 1721 2575 128 79 -144 C ATOM 186 N VAL A 41 14.477 6.050 46.982 1.00 14.92 N ANISOU 186 N VAL A 41 1443 2020 2205 104 133 -290 N ATOM 187 CA VAL A 41 14.964 4.908 47.756 1.00 16.72 C ANISOU 187 CA VAL A 41 1834 2174 2344 131 -43 -155 C ATOM 188 C VAL A 41 15.996 4.104 46.958 1.00 16.78 C ANISOU 188 C VAL A 41 1834 2107 2434 161 -6 -47 C ATOM 189 O VAL A 41 17.047 3.758 47.498 1.00 17.41 O ANISOU 189 O VAL A 41 1953 2046 2615 116 -222 -21 O ATOM 190 CB VAL A 41 13.817 3.989 48.237 1.00 17.08 C ANISOU 190 CB VAL A 41 1986 2179 2322 192 -36 97 C ATOM 191 CG1 VAL A 41 14.363 2.684 48.827 1.00 18.56 C ANISOU 191 CG1 VAL A 41 2225 2107 2720 150 -32 204 C ATOM 192 CG2 VAL A 41 12.973 4.716 49.279 1.00 17.13 C ANISOU 192 CG2 VAL A 41 1733 2191 2584 184 -27 9 C ATOM 193 N LEU A 42 15.687 3.815 45.689 1.00 15.94 N ANISOU 193 N LEU A 42 1678 1838 2538 -118 118 -288 N ATOM 194 CA LEU A 42 16.634 3.150 44.785 1.00 16.54 C ANISOU 194 CA LEU A 42 1741 1875 2666 98 82 -217 C ATOM 195 C LEU A 42 17.965 3.908 44.715 1.00 15.94 C ANISOU 195 C LEU A 42 1476 1808 2772 335 -77 -206 C ATOM 196 O LEU A 42 19.025 3.316 44.905 1.00 16.31 O ANISOU 196 O LEU A 42 1603 1831 2761 501 -130 -412 O ATOM 197 CB LEU A 42 16.031 3.009 43.382 1.00 18.35 C ANISOU 197 CB LEU A 42 2061 2047 2861 -113 -166 -151 C ATOM 198 CG LEU A 42 16.922 2.463 42.258 1.00 19.02 C ANISOU 198 CG LEU A 42 2204 1978 3044 244 -236 -202 C ATOM 199 CD1 LEU A 42 17.422 1.057 42.573 1.00 19.69 C ANISOU 199 CD1 LEU A 42 2313 2208 2957 467 -273 -40 C ATOM 200 CD2 LEU A 42 16.185 2.478 40.935 1.00 19.76 C ANISOU 200 CD2 LEU A 42 2209 2195 3104 324 -284 -378 C ATOM 201 N ASP A 43 17.905 5.211 44.445 1.00 17.97 N ANISOU 201 N ASP A 43 2112 1822 2894 134 -27 -165 N ATOM 202 CA ASP A 43 19.125 6.041 44.373 1.00 18.32 C ANISOU 202 CA ASP A 43 2301 1840 2819 6 169 -119 C ATOM 203 C ASP A 43 19.947 6.018 45.670 1.00 17.90 C ANISOU 203 C ASP A 43 1828 1979 2995 173 165 -91 C ATOM 204 O ASP A 43 21.193 5.928 45.636 1.00 17.40 O ANISOU 204 O ASP A 43 1777 1774 3059 128 33 -335 O ATOM 205 CB ASP A 43 18.782 7.503 44.019 1.00 18.81 C ANISOU 205 CB ASP A 43 2572 1919 2655 59 -11 -39 C ATOM 206 CG ASP A 43 18.465 7.708 42.547 1.00 18.21 C ANISOU 206 CG ASP A 43 2269 1926 2722 -108 -177 -20 C ATOM 207 OD1 ASP A 43 18.710 6.809 41.704 1.00 17.90 O ANISOU 207 OD1 ASP A 43 2196 1786 2818 -105 -374 -36 O ATOM 208 OD2 ASP A 43 17.968 8.805 42.222 1.00 17.29 O ANISOU 208 OD2 ASP A 43 1873 1962 2731 -412 -739 95 O ATOM 209 N ALA A 44 19.252 6.107 46.803 1.00 18.44 N ANISOU 209 N ALA A 44 2121 2013 2871 227 126 -127 N ATOM 210 CA ALA A 44 19.901 6.069 48.124 1.00 18.49 C ANISOU 210 CA ALA A 44 2151 1984 2889 244 56 -174 C ATOM 211 C ALA A 44 20.726 4.791 48.312 1.00 17.58 C ANISOU 211 C ALA A 44 1610 2188 2881 192 -397 -204 C ATOM 212 O ALA A 44 21.876 4.842 48.782 1.00 16.57 O ANISOU 212 O ALA A 44 1287 1676 3330 356 -167 -325 O ATOM 213 CB ALA A 44 18.866 6.225 49.236 1.00 19.94 C ANISOU 213 CB ALA A 44 2584 2423 2569 194 71 -239 C ATOM 214 N HIS A 45 20.163 3.656 47.904 1.00 18.90 N ANISOU 214 N HIS A 45 2261 2039 2878 111 -300 -142 N ATOM 215 CA HIS A 45 20.897 2.379 47.938 1.00 18.68 C ANISOU 215 CA HIS A 45 2130 2229 2739 235 -155 -156 C ATOM 216 C HIS A 45 22.076 2.353 46.955 1.00 18.90 C ANISOU 216 C HIS A 45 2176 2178 2823 372 -131 -248 C ATOM 217 O HIS A 45 23.191 1.970 47.335 1.00 19.42 O ANISOU 217 O HIS A 45 2336 2465 2575 520 -309 -299 O ATOM 218 CB HIS A 45 19.954 1.189 47.713 1.00 18.44 C ANISOU 218 CB HIS A 45 2137 2234 2633 162 17 -98 C ATOM 219 CG HIS A 45 19.180 0.804 48.939 1.00 19.30 C ANISOU 219 CG HIS A 45 2194 2322 2814 66 127 -34 C ATOM 220 ND1 HIS A 45 19.707 -0.004 49.923 1.00 19.37 N ANISOU 220 ND1 HIS A 45 2077 2350 2932 -138 49 86 N ATOM 221 CD2 HIS A 45 17.931 1.134 49.353 1.00 18.89 C ANISOU 221 CD2 HIS A 45 2004 2262 2910 -64 48 95 C ATOM 222 CE1 HIS A 45 18.815 -0.163 50.886 1.00 19.45 C ANISOU 222 CE1 HIS A 45 2180 2303 2906 32 122 76 C ATOM 223 NE2 HIS A 45 17.729 0.518 50.564 1.00 18.41 N ANISOU 223 NE2 HIS A 45 1865 2353 2775 -171 31 -23 N ATOM 224 N LEU A 46 21.843 2.783 45.714 1.00 19.02 N ANISOU 224 N LEU A 46 2349 2054 2823 242 -213 -261 N ATOM 225 CA LEU A 46 22.907 2.771 44.692 1.00 19.90 C ANISOU 225 CA LEU A 46 2228 2364 2968 -106 -219 -238 C ATOM 226 C LEU A 46 24.112 3.659 45.022 1.00 20.09 C ANISOU 226 C LEU A 46 1944 2475 3214 -60 -19 -178 C ATOM 227 O LEU A 46 25.228 3.313 44.656 1.00 20.62 O ANISOU 227 O LEU A 46 1608 2811 3414 -483 25 -151 O ATOM 228 CB LEU A 46 22.364 3.133 43.314 1.00 20.02 C ANISOU 228 CB LEU A 46 2225 2433 2946 -52 -107 -96 C ATOM 229 CG LEU A 46 21.345 2.162 42.711 1.00 20.01 C ANISOU 229 CG LEU A 46 2234 2487 2881 -91 -79 -112 C ATOM 230 CD1 LEU A 46 20.788 2.756 41.426 1.00 19.05 C ANISOU 230 CD1 LEU A 46 2215 2098 2923 -124 -10 -57 C ATOM 231 CD2 LEU A 46 21.917 0.772 42.458 1.00 19.91 C ANISOU 231 CD2 LEU A 46 2188 2696 2678 108 -71 -140 C ATOM 232 N GLN A 47 23.878 4.780 45.709 1.00 19.70 N ANISOU 232 N GLN A 47 2082 2370 3031 -132 -234 -138 N ATOM 233 CA GLN A 47 24.958 5.662 46.189 1.00 21.36 C ANISOU 233 CA GLN A 47 2243 2864 3006 -283 -454 -116 C ATOM 234 C GLN A 47 26.000 4.939 47.046 1.00 18.83 C ANISOU 234 C GLN A 47 965 2527 3660 -448 -192 -311 C ATOM 235 O GLN A 47 27.171 5.306 47.025 1.00 21.59 O ANISOU 235 O GLN A 47 1210 2672 4321 -870 -186 46 O ATOM 236 CB GLN A 47 24.387 6.842 46.988 1.00 25.25 C ANISOU 236 CB GLN A 47 3054 3065 3473 -22 -208 -221 C ATOM 237 CG GLN A 47 23.914 7.993 46.123 1.00 31.25 C ANISOU 237 CG GLN A 47 4126 3369 4376 531 -534 -109 C ATOM 238 CD GLN A 47 22.937 8.918 46.832 1.00 35.20 C ANISOU 238 CD GLN A 47 4286 3559 5530 883 -478 -78 C ATOM 239 OE1 GLN A 47 22.938 9.031 48.062 0.36 32.01 O ANISOU 239 OE1 GLN A 47 4179 2512 5470 360 -705 209 O ATOM 240 NE2 GLN A 47 22.096 9.595 46.051 0.90 41.11 N ANISOU 240 NE2 GLN A 47 6098 3737 5784 664 -1563 278 N ATOM 241 N GLN A 48 25.558 3.944 47.810 1.00 20.17 N ANISOU 241 N GLN A 48 2084 2236 3344 -317 -278 -357 N ATOM 242 CA GLN A 48 26.423 3.155 48.691 1.00 21.28 C ANISOU 242 CA GLN A 48 2547 2146 3393 -53 -239 -323 C ATOM 243 C GLN A 48 26.773 1.773 48.135 1.00 20.18 C ANISOU 243 C GLN A 48 1784 2451 3431 707 -549 -236 C ATOM 244 O GLN A 48 27.893 1.295 48.340 1.00 20.98 O ANISOU 244 O GLN A 48 1111 2918 3943 -21 -841 -294 O ATOM 245 CB GLN A 48 25.744 2.980 50.047 1.00 21.42 C ANISOU 245 CB GLN A 48 2254 2607 3278 239 -306 -443 C ATOM 246 CG GLN A 48 25.566 4.265 50.833 1.00 23.08 C ANISOU 246 CG GLN A 48 2618 2819 3330 352 -208 -565 C ATOM 247 CD GLN A 48 24.895 4.022 52.173 1.00 24.55 C ANISOU 247 CD GLN A 48 2872 3325 3128 744 -288 -491 C ATOM 248 OE1 GLN A 48 25.320 3.157 52.935 1.00 24.06 O ANISOU 248 OE1 GLN A 48 2105 3520 3516 552 -604 -427 O ATOM 249 NE2 GLN A 48 23.835 4.772 52.464 1.00 25.62 N ANISOU 249 NE2 GLN A 48 2900 3549 3283 818 -177 -390 N ATOM 250 N ASP A 49 25.814 1.123 47.475 1.00 21.52 N ANISOU 250 N ASP A 49 2202 2681 3292 150 -391 -200 N ATOM 251 CA ASP A 49 25.993 -0.229 46.940 1.00 21.27 C ANISOU 251 CA ASP A 49 2318 2510 3252 24 -253 8 C ATOM 252 C ASP A 49 25.491 -0.301 45.492 1.00 18.09 C ANISOU 252 C ASP A 49 1131 2379 3363 -70 -215 6 C ATOM 253 O ASP A 49 24.295 -0.524 45.264 1.00 18.41 O ANISOU 253 O ASP A 49 985 2146 3862 166 -154 -1 O ATOM 254 CB ASP A 49 25.244 -1.247 47.817 1.00 21.61 C ANISOU 254 CB ASP A 49 2353 2864 2992 0 -75 11 C ATOM 255 CG ASP A 49 25.404 -2.691 47.331 1.00 20.88 C ANISOU 255 CG ASP A 49 2078 2886 2969 88 -43 33 C ATOM 256 OD1 ASP A 49 26.041 -2.940 46.288 1.00 19.29 O ANISOU 256 OD1 ASP A 49 1960 2238 3131 316 3 78 O ATOM 257 OD2 ASP A 49 24.887 -3.599 48.009 1.00 24.51 O ANISOU 257 OD2 ASP A 49 3409 2360 3542 157 27 168 O ATOM 258 N PRO A 50 26.403 -0.159 44.509 1.00 17.54 N ANISOU 258 N PRO A 50 746 2236 3681 -285 -192 0 N ATOM 259 CA PRO A 50 26.036 -0.257 43.092 1.00 18.19 C ANISOU 259 CA PRO A 50 873 2421 3616 -254 -69 14 C ATOM 260 C PRO A 50 25.315 -1.549 42.680 1.00 18.51 C ANISOU 260 C PRO A 50 1587 2100 3345 -64 -150 -80 C ATOM 261 O PRO A 50 24.582 -1.533 41.693 1.00 19.61 O ANISOU 261 O PRO A 50 1590 2322 3536 -80 -275 -252 O ATOM 262 CB PRO A 50 27.387 -0.160 42.378 1.00 20.61 C ANISOU 262 CB PRO A 50 1545 2764 3521 -213 518 159 C ATOM 263 CG PRO A 50 28.224 0.643 43.305 1.00 23.01 C ANISOU 263 CG PRO A 50 2269 2893 3578 -235 131 154 C ATOM 264 CD PRO A 50 27.838 0.149 44.663 1.00 18.02 C ANISOU 264 CD PRO A 50 695 2633 3517 -312 46 -64 C ATOM 265 N ASP A 51 25.515 -2.641 43.422 1.00 17.51 N ANISOU 265 N ASP A 51 1739 1887 3027 26 -266 -343 N ATOM 266 CA ASP A 51 24.855 -3.922 43.131 1.00 18.04 C ANISOU 266 CA ASP A 51 2048 1855 2950 -58 -144 -281 C ATOM 267 C ASP A 51 23.621 -4.226 43.994 1.00 17.43 C ANISOU 267 C ASP A 51 2236 1422 2963 174 63 -166 C ATOM 268 O ASP A 51 23.164 -5.374 44.053 1.00 17.86 O ANISOU 268 O ASP A 51 2047 1421 3316 207 -87 -72 O ATOM 269 CB ASP A 51 25.886 -5.054 43.213 1.00 20.57 C ANISOU 269 CB ASP A 51 2147 2304 3362 222 -198 -281 C ATOM 270 CG ASP A 51 26.957 -4.931 42.147 0.87 24.57 C ANISOU 270 CG ASP A 51 2565 2862 3908 22 211 -238 C ATOM 271 OD1 ASP A 51 26.603 -4.842 40.951 0.89 26.96 O ANISOU 271 OD1 ASP A 51 3449 2994 3798 -45 339 -587 O ATOM 272 OD2 ASP A 51 28.150 -4.915 42.500 0.90 27.37 O ANISOU 272 OD2 ASP A 51 2592 3550 4257 27 139 -390 O ATOM 273 N ALA A 52 23.053 -3.198 44.623 1.00 17.36 N ANISOU 273 N ALA A 52 1939 1841 2816 188 361 -182 N ATOM 274 CA ALA A 52 21.828 -3.354 45.400 1.00 16.81 C ANISOU 274 CA ALA A 52 1770 2191 2422 45 56 10 C ATOM 275 C ALA A 52 20.709 -3.932 44.540 1.00 15.78 C ANISOU 275 C ALA A 52 1887 1833 2275 93 126 -111 C ATOM 276 O ALA A 52 20.552 -3.563 43.372 1.00 15.32 O ANISOU 276 O ALA A 52 1646 1908 2264 43 159 -146 O ATOM 277 CB ALA A 52 21.400 -2.017 45.977 1.00 19.59 C ANISOU 277 CB ALA A 52 2224 2500 2718 276 -28 -254 C ATOM 278 N LYS A 53 19.962 -4.864 45.122 1.00 14.93 N ANISOU 278 N LYS A 53 1609 1882 2182 101 -53 -105 N ATOM 279 CA LYS A 53 18.809 -5.460 44.472 1.00 15.18 C ANISOU 279 CA LYS A 53 1730 1923 2113 162 -167 -165 C ATOM 280 C LYS A 53 17.628 -4.797 45.125 1.00 15.59 C ANISOU 280 C LYS A 53 1597 2000 2325 95 -114 -167 C ATOM 281 O LYS A 53 17.445 -4.944 46.331 1.00 15.84 O ANISOU 281 O LYS A 53 1724 2000 2292 353 -200 -334 O ATOM 282 CB LYS A 53 18.781 -6.969 44.699 1.00 16.89 C ANISOU 282 CB LYS A 53 2044 2024 2347 203 -97 120 C ATOM 283 CG LYS A 53 20.028 -7.690 44.210 1.00 19.22 C ANISOU 283 CG LYS A 53 2055 2428 2817 160 86 -124 C ATOM 284 CD LYS A 53 20.063 -7.778 42.695 1.00 20.73 C ANISOU 284 CD LYS A 53 2502 2495 2880 18 108 -186 C ATOM 285 CE LYS A 53 21.356 -8.411 42.204 1.00 22.19 C ANISOU 285 CE LYS A 53 2350 2795 3283 -66 119 -273 C ATOM 286 NZ LYS A 53 22.479 -7.441 42.210 1.00 24.33 N ANISOU 286 NZ LYS A 53 2633 2858 3754 -240 322 -598 N ATOM 287 N VAL A 54 16.841 -4.063 44.339 1.00 15.94 N ANISOU 287 N VAL A 54 1967 1935 2153 267 51 -93 N ATOM 288 CA VAL A 54 15.788 -3.182 44.864 1.00 14.86 C ANISOU 288 CA VAL A 54 1553 2001 2089 91 10 -81 C ATOM 289 C VAL A 54 14.471 -3.381 44.108 1.00 15.58 C ANISOU 289 C VAL A 54 1744 1959 2217 79 -187 -86 C ATOM 290 O VAL A 54 14.440 -3.357 42.873 1.00 14.73 O ANISOU 290 O VAL A 54 1373 1948 2275 27 -5 15 O ATOM 291 CB VAL A 54 16.206 -1.695 44.753 1.00 17.10 C ANISOU 291 CB VAL A 54 2150 1993 2352 99 -83 167 C ATOM 292 CG1 VAL A 54 15.186 -0.780 45.420 1.00 18.53 C ANISOU 292 CG1 VAL A 54 2400 2129 2512 246 -37 152 C ATOM 293 CG2 VAL A 54 17.574 -1.466 45.385 1.00 17.77 C ANISOU 293 CG2 VAL A 54 2229 1996 2524 250 -246 151 C ATOM 294 N ALA A 55 13.394 -3.560 44.872 1.00 14.21 N ANISOU 294 N ALA A 55 1531 1953 1913 38 -435 -104 N ATOM 295 CA ALA A 55 12.032 -3.702 44.350 1.00 15.58 C ANISOU 295 CA ALA A 55 1592 2042 2286 79 -549 -61 C ATOM 296 C ALA A 55 11.099 -3.003 45.334 1.00 17.30 C ANISOU 296 C ALA A 55 1865 2224 2484 24 -205 -68 C ATOM 297 O ALA A 55 10.377 -3.652 46.097 1.00 17.41 O ANISOU 297 O ALA A 55 2242 1660 2711 431 28 122 O ATOM 298 CB ALA A 55 11.667 -5.174 44.202 1.00 18.34 C ANISOU 298 CB ALA A 55 2286 2121 2562 -56 -491 -235 C ATOM 299 N CYS A 56 11.139 -1.669 45.317 1.00 16.98 N ANISOU 299 N CYS A 56 1834 2237 2381 -46 48 -50 N ATOM 300 CA CYS A 56 10.467 -0.845 46.317 1.00 17.44 C ANISOU 300 CA CYS A 56 1936 2182 2507 95 -55 -120 C ATOM 301 C CYS A 56 9.180 -0.227 45.788 1.00 18.89 C ANISOU 301 C CYS A 56 2056 2402 2719 203 -146 -3 C ATOM 302 O CYS A 56 9.224 0.657 44.929 1.00 20.02 O ANISOU 302 O CYS A 56 2195 2348 3063 392 -214 92 O ATOM 303 CB CYS A 56 11.401 0.270 46.797 1.00 19.41 C ANISOU 303 CB CYS A 56 2287 2243 2845 -146 249 -307 C ATOM 304 SG CYS A 56 10.692 1.282 48.121 1.00 22.66 S ANISOU 304 SG CYS A 56 2728 2217 3664 92 402 -694 S ATOM 305 N GLU A 57 8.047 -0.689 46.317 1.00 16.42 N ANISOU 305 N GLU A 57 1847 1842 2548 447 -289 48 N ATOM 306 CA GLU A 57 6.740 -0.107 46.023 1.00 15.33 C ANISOU 306 CA GLU A 57 1507 1905 2413 85 -236 44 C ATOM 307 C GLU A 57 6.406 0.921 47.091 1.00 16.47 C ANISOU 307 C GLU A 57 1680 2112 2465 312 -195 -7 C ATOM 308 O GLU A 57 6.715 0.724 48.277 1.00 18.94 O ANISOU 308 O GLU A 57 2457 2249 2488 346 -233 94 O ATOM 309 CB GLU A 57 5.632 -1.177 46.002 1.00 16.78 C ANISOU 309 CB GLU A 57 1745 2125 2506 -148 -209 61 C ATOM 310 CG GLU A 57 5.958 -2.435 45.215 1.00 18.14 C ANISOU 310 CG GLU A 57 1889 2201 2802 2 -141 -1 C ATOM 311 CD GLU A 57 6.007 -2.223 43.708 1.00 18.75 C ANISOU 311 CD GLU A 57 2224 2070 2828 140 -296 -53 C ATOM 312 OE1 GLU A 57 5.955 -1.069 43.225 0.86 18.72 O ANISOU 312 OE1 GLU A 57 2020 1810 3282 164 -762 -244 O ATOM 313 OE2 GLU A 57 6.085 -3.245 42.989 0.97 21.99 O ANISOU 313 OE2 GLU A 57 3077 1772 3505 426 -230 -56 O ATOM 314 N THR A 58 5.765 2.005 46.662 1.00 16.24 N ANISOU 314 N THR A 58 1803 2051 2317 273 -161 11 N ATOM 315 CA THR A 58 5.282 3.046 47.552 1.00 15.47 C ANISOU 315 CA THR A 58 1668 1994 2213 289 -270 31 C ATOM 316 C THR A 58 3.765 3.191 47.393 1.00 15.18 C ANISOU 316 C THR A 58 1648 2046 2071 304 -158 -88 C ATOM 317 O THR A 58 3.234 3.061 46.288 1.00 14.54 O ANISOU 317 O THR A 58 1235 2046 2243 482 -275 -21 O ATOM 318 CB THR A 58 6.005 4.382 47.278 1.00 16.16 C ANISOU 318 CB THR A 58 1897 1977 2264 238 -290 43 C ATOM 319 OG1 THR A 58 7.421 4.180 47.382 1.00 16.28 O ANISOU 319 OG1 THR A 58 1932 1775 2476 249 -507 311 O ATOM 320 CG2 THR A 58 5.586 5.446 48.276 1.00 16.42 C ANISOU 320 CG2 THR A 58 2114 1845 2276 151 -158 116 C ATOM 321 N VAL A 59 3.094 3.442 48.516 1.00 14.22 N ANISOU 321 N VAL A 59 1306 1985 2110 332 -183 -107 N ATOM 322 CA VAL A 59 1.656 3.691 48.572 1.00 14.76 C ANISOU 322 CA VAL A 59 1397 2011 2197 522 -105 -18 C ATOM 323 C VAL A 59 1.441 4.997 49.329 1.00 15.86 C ANISOU 323 C VAL A 59 1739 2031 2256 414 63 -81 C ATOM 324 O VAL A 59 2.048 5.212 50.372 1.00 16.76 O ANISOU 324 O VAL A 59 2205 1830 2331 826 -113 -204 O ATOM 325 CB VAL A 59 0.924 2.564 49.321 1.00 16.65 C ANISOU 325 CB VAL A 59 1639 2153 2534 260 -57 -28 C ATOM 326 CG1 VAL A 59 -0.587 2.805 49.350 1.00 17.02 C ANISOU 326 CG1 VAL A 59 1655 2223 2586 273 32 53 C ATOM 327 CG2 VAL A 59 1.242 1.227 48.684 1.00 19.99 C ANISOU 327 CG2 VAL A 59 2527 2195 2872 316 -63 -147 C ATOM 328 N ALA A 60 0.558 5.849 48.817 1.00 17.06 N ANISOU 328 N ALA A 60 2121 2041 2319 469 34 109 N ATOM 329 CA ALA A 60 0.283 7.143 49.432 1.00 17.14 C ANISOU 329 CA ALA A 60 1793 2328 2388 516 222 -115 C ATOM 330 C ALA A 60 -1.212 7.298 49.634 1.00 16.27 C ANISOU 330 C ALA A 60 1730 2107 2343 351 170 -12 C ATOM 331 O ALA A 60 -1.992 7.039 48.721 1.00 17.15 O ANISOU 331 O ALA A 60 2026 2166 2325 559 32 -31 O ATOM 332 CB ALA A 60 0.821 8.278 48.571 1.00 18.88 C ANISOU 332 CB ALA A 60 2109 2306 2756 325 -38 37 C ATOM 333 N LYS A 61 -1.599 7.682 50.846 1.00 14.15 N ANISOU 333 N LYS A 61 1297 1767 2310 204 64 -38 N ATOM 334 CA LYS A 61 -2.974 8.102 51.144 1.00 14.93 C ANISOU 334 CA LYS A 61 1318 2005 2348 294 44 -5 C ATOM 335 C LYS A 61 -2.869 9.218 52.189 1.00 15.29 C ANISOU 335 C LYS A 61 1436 2029 2342 245 113 -28 C ATOM 336 O LYS A 61 -1.762 9.583 52.576 1.00 16.34 O ANISOU 336 O LYS A 61 1756 2164 2286 193 -199 -222 O ATOM 337 CB LYS A 61 -3.810 6.886 51.600 1.00 17.76 C ANISOU 337 CB LYS A 61 1950 1982 2814 47 31 -104 C ATOM 338 CG LYS A 61 -5.311 7.102 51.797 1.00 20.25 C ANISOU 338 CG LYS A 61 2025 2320 3346 212 -83 -4 C ATOM 339 CD LYS A 61 -6.017 7.740 50.600 1.00 24.72 C ANISOU 339 CD LYS A 61 3058 2859 3475 259 -252 311 C ATOM 340 CE LYS A 61 -7.359 8.349 50.975 1.00 27.34 C ANISOU 340 CE LYS A 61 3267 3333 3788 325 0 -4 C ATOM 341 NZ LYS A 61 -7.743 9.446 50.036 1.00 27.50 N ANISOU 341 NZ LYS A 61 3749 3000 3697 315 160 -167 N ATOM 342 N THR A 62 -3.976 9.833 52.583 1.00 15.08 N ANISOU 342 N THR A 62 1448 1962 2316 104 217 -171 N ATOM 343 CA THR A 62 -3.956 10.884 53.608 1.00 15.40 C ANISOU 343 CA THR A 62 1546 1852 2452 -46 82 -172 C ATOM 344 C THR A 62 -2.981 10.607 54.747 1.00 14.45 C ANISOU 344 C THR A 62 1571 1577 2341 0 170 -110 C ATOM 345 O THR A 62 -3.125 9.638 55.476 1.00 14.70 O ANISOU 345 O THR A 62 1600 1462 2520 -52 160 -131 O ATOM 346 CB THR A 62 -5.350 11.099 54.207 1.00 15.91 C ANISOU 346 CB THR A 62 1438 2113 2492 -66 -17 -150 C ATOM 347 OG1 THR A 62 -6.289 11.217 53.141 1.00 16.79 O ANISOU 347 OG1 THR A 62 1756 2280 2341 62 -94 -130 O ATOM 348 CG2 THR A 62 -5.402 12.364 55.063 1.00 18.08 C ANISOU 348 CG2 THR A 62 1895 2090 2882 -63 -224 -257 C ATOM 349 N GLY A 63 -1.966 11.454 54.857 1.00 15.25 N ANISOU 349 N GLY A 63 2019 1321 2453 -155 62 -72 N ATOM 350 CA GLY A 63 -1.033 11.406 55.962 1.00 15.69 C ANISOU 350 CA GLY A 63 1881 1466 2614 -55 14 -127 C ATOM 351 C GLY A 63 -0.090 10.218 56.010 1.00 16.05 C ANISOU 351 C GLY A 63 1917 1391 2791 -69 -30 -318 C ATOM 352 O GLY A 63 0.567 10.021 57.034 1.00 17.29 O ANISOU 352 O GLY A 63 2053 1522 2992 154 -133 -169 O ATOM 353 N MET A 64 -0.003 9.442 54.926 1.00 15.83 N ANISOU 353 N MET A 64 1893 1610 2510 130 -141 -213 N ATOM 354 CA MET A 64 0.725 8.155 54.932 1.00 16.33 C ANISOU 354 CA MET A 64 2047 1521 2633 94 -243 10 C ATOM 355 C MET A 64 1.579 7.933 53.691 1.00 17.06 C ANISOU 355 C MET A 64 2299 1651 2530 162 -274 64 C ATOM 356 O MET A 64 1.088 8.045 52.570 1.00 16.66 O ANISOU 356 O MET A 64 2164 1518 2648 161 -375 37 O ATOM 357 CB MET A 64 -0.259 6.981 55.028 1.00 16.12 C ANISOU 357 CB MET A 64 2084 1627 2411 22 -61 -41 C ATOM 358 CG MET A 64 0.415 5.625 55.226 1.00 17.59 C ANISOU 358 CG MET A 64 2243 1890 2549 276 0 73 C ATOM 359 SD MET A 64 -0.678 4.217 54.997 1.00 21.65 S ANISOU 359 SD MET A 64 3044 1821 3358 69 207 -116 S ATOM 360 CE MET A 64 -0.683 4.109 53.206 1.00 23.75 C ANISOU 360 CE MET A 64 3182 2441 3401 63 114 -46 C ATOM 361 N ILE A 65 2.847 7.589 53.916 1.00 17.92 N ANISOU 361 N ILE A 65 2318 1880 2609 142 -354 83 N ATOM 362 CA ILE A 65 3.687 6.939 52.922 1.00 17.29 C ANISOU 362 CA ILE A 65 2368 1814 2384 67 -381 162 C ATOM 363 C ILE A 65 4.054 5.563 53.479 1.00 17.18 C ANISOU 363 C ILE A 65 2349 1827 2349 87 -622 103 C ATOM 364 O ILE A 65 4.628 5.468 54.559 1.00 17.82 O ANISOU 364 O ILE A 65 2748 1568 2455 213 -776 115 O ATOM 365 CB ILE A 65 4.982 7.728 52.640 1.00 19.23 C ANISOU 365 CB ILE A 65 2437 2222 2644 -26 -119 112 C ATOM 366 CG1 ILE A 65 4.671 9.154 52.158 1.00 19.73 C ANISOU 366 CG1 ILE A 65 2494 2185 2817 102 -60 9 C ATOM 367 CG2 ILE A 65 5.853 6.990 51.623 1.00 19.64 C ANISOU 367 CG2 ILE A 65 2364 2374 2721 98 -115 121 C ATOM 368 CD1 ILE A 65 3.930 9.250 50.841 1.00 20.83 C ANISOU 368 CD1 ILE A 65 2714 2541 2656 -15 34 -2 C ATOM 369 N LEU A 66 3.699 4.512 52.742 1.00 18.41 N ANISOU 369 N LEU A 66 2958 2522 1514 -265 -1643 375 N ATOM 370 CA LEU A 66 4.093 3.139 53.053 1.00 17.78 C ANISOU 370 CA LEU A 66 2263 2283 2208 26 -348 -131 C ATOM 371 C LEU A 66 5.078 2.642 51.993 1.00 17.43 C ANISOU 371 C LEU A 66 2397 1982 2241 275 -383 -14 C ATOM 372 O LEU A 66 4.819 2.769 50.793 1.00 16.23 O ANISOU 372 O LEU A 66 1890 1902 2375 461 -731 -292 O ATOM 373 CB LEU A 66 2.868 2.223 53.105 1.00 19.19 C ANISOU 373 CB LEU A 66 2539 1985 2766 -58 -253 -129 C ATOM 374 CG LEU A 66 3.126 0.707 53.147 1.00 21.93 C ANISOU 374 CG LEU A 66 2943 1898 3491 -390 -106 -6 C ATOM 375 CD1 LEU A 66 3.659 0.307 54.510 1.00 24.33 C ANISOU 375 CD1 LEU A 66 3132 2578 3533 -175 -154 1 C ATOM 376 CD2 LEU A 66 1.866 -0.074 52.807 1.00 25.14 C ANISOU 376 CD2 LEU A 66 3653 2404 3492 -1036 -232 -119 C ATOM 377 N LEU A 67 6.199 2.084 52.452 1.00 17.41 N ANISOU 377 N LEU A 67 2339 1958 2318 390 -215 -6 N ATOM 378 CA LEU A 67 7.143 1.374 51.601 1.00 17.76 C ANISOU 378 CA LEU A 67 2569 2147 2032 186 -28 -51 C ATOM 379 C LEU A 67 6.928 -0.132 51.774 1.00 17.43 C ANISOU 379 C LEU A 67 2520 2113 1988 254 -137 -83 C ATOM 380 O LEU A 67 6.920 -0.634 52.902 1.00 19.21 O ANISOU 380 O LEU A 67 3202 1698 2398 102 -305 252 O ATOM 381 CB LEU A 67 8.586 1.740 51.970 1.00 20.21 C ANISOU 381 CB LEU A 67 2676 2443 2559 225 -345 -3 C ATOM 382 CG LEU A 67 9.024 3.212 51.921 1.00 20.16 C ANISOU 382 CG LEU A 67 2451 2513 2694 148 -269 -34 C ATOM 383 CD1 LEU A 67 10.531 3.306 52.144 1.00 20.05 C ANISOU 383 CD1 LEU A 67 2418 2471 2728 213 -180 12 C ATOM 384 CD2 LEU A 67 8.646 3.896 50.611 1.00 20.83 C ANISOU 384 CD2 LEU A 67 2816 2430 2667 232 -187 -45 C ATOM 385 N ALA A 68 6.737 -0.842 50.665 1.00 15.14 N ANISOU 385 N ALA A 68 2095 1797 1859 297 -103 88 N ATOM 386 CA ALA A 68 6.534 -2.292 50.681 1.00 15.89 C ANISOU 386 CA ALA A 68 2167 1817 2051 336 -61 15 C ATOM 387 C ALA A 68 7.312 -2.929 49.540 1.00 17.36 C ANISOU 387 C ALA A 68 2397 2043 2155 446 23 -44 C ATOM 388 O ALA A 68 7.322 -2.416 48.421 1.00 19.90 O ANISOU 388 O ALA A 68 3171 2328 2063 342 247 -106 O ATOM 389 CB ALA A 68 5.057 -2.632 50.571 1.00 18.08 C ANISOU 389 CB ALA A 68 2190 2217 2460 239 51 -96 C ATOM 390 N GLY A 69 7.981 -4.037 49.820 1.00 15.70 N ANISOU 390 N GLY A 69 1994 1908 2062 194 0 -24 N ATOM 391 CA GLY A 69 8.750 -4.716 48.789 1.00 14.30 C ANISOU 391 CA GLY A 69 1038 2036 2357 120 38 93 C ATOM 392 C GLY A 69 9.987 -5.391 49.319 1.00 15.62 C ANISOU 392 C GLY A 69 1431 2066 2435 349 -134 119 C ATOM 393 O GLY A 69 10.055 -5.750 50.500 1.00 14.81 O ANISOU 393 O GLY A 69 1195 2018 2411 428 17 142 O ATOM 394 N GLU A 70 10.966 -5.555 48.430 1.00 16.27 N ANISOU 394 N GLU A 70 1740 2159 2282 442 -69 10 N ATOM 395 CA GLU A 70 12.139 -6.386 48.700 1.00 15.85 C ANISOU 395 CA GLU A 70 1400 2299 2322 216 -202 -20 C ATOM 396 C GLU A 70 13.424 -5.662 48.335 1.00 16.15 C ANISOU 396 C GLU A 70 1707 2202 2228 26 -60 -70 C ATOM 397 O GLU A 70 13.582 -5.187 47.204 1.00 17.20 O ANISOU 397 O GLU A 70 1770 2513 2251 42 -387 59 O ATOM 398 CB GLU A 70 12.058 -7.708 47.936 1.00 16.64 C ANISOU 398 CB GLU A 70 1601 2222 2500 203 -75 20 C ATOM 399 CG GLU A 70 10.760 -8.476 48.172 1.00 18.78 C ANISOU 399 CG GLU A 70 1928 2395 2811 -25 221 31 C ATOM 400 CD GLU A 70 9.598 -7.960 47.344 1.00 19.60 C ANISOU 400 CD GLU A 70 1932 2333 3179 34 204 50 C ATOM 401 OE1 GLU A 70 9.810 -7.597 46.167 1.00 22.03 O ANISOU 401 OE1 GLU A 70 2837 2042 3488 -532 184 345 O ATOM 402 OE2 GLU A 70 8.465 -7.919 47.875 1.00 21.92 O ANISOU 402 OE2 GLU A 70 2216 2532 3580 -116 613 17 O ATOM 403 N ILE A 71 14.335 -5.575 49.304 1.00 15.83 N ANISOU 403 N ILE A 71 1629 2237 2146 -117 9 149 N ATOM 404 CA ILE A 71 15.661 -4.982 49.097 1.00 15.05 C ANISOU 404 CA ILE A 71 1540 1965 2212 -2 -114 154 C ATOM 405 C ILE A 71 16.721 -5.823 49.791 1.00 17.30 C ANISOU 405 C ILE A 71 1821 2070 2680 126 -351 170 C ATOM 406 O ILE A 71 16.604 -6.109 50.983 1.00 19.08 O ANISOU 406 O ILE A 71 2191 2208 2850 132 -361 321 O ATOM 407 CB ILE A 71 15.757 -3.529 49.623 1.00 15.68 C ANISOU 407 CB ILE A 71 1669 2054 2233 -158 -140 68 C ATOM 408 CG1 ILE A 71 14.653 -2.657 49.001 1.00 15.19 C ANISOU 408 CG1 ILE A 71 1537 2067 2167 -37 20 -55 C ATOM 409 CG2 ILE A 71 17.139 -2.954 49.313 1.00 16.03 C ANISOU 409 CG2 ILE A 71 1632 2050 2409 -38 73 -18 C ATOM 410 CD1 ILE A 71 14.658 -1.206 49.431 1.00 15.90 C ANISOU 410 CD1 ILE A 71 1645 2199 2197 -76 9 -223 C ATOM 411 N THR A 72 17.742 -6.208 49.025 1.00 16.66 N ANISOU 411 N THR A 72 1789 2110 2429 232 -414 340 N ATOM 412 CA THR A 72 18.953 -6.841 49.545 1.00 16.03 C ANISOU 412 CA THR A 72 1576 2102 2411 173 -309 158 C ATOM 413 C THR A 72 20.106 -5.951 49.114 1.00 17.40 C ANISOU 413 C THR A 72 1476 2306 2825 234 -67 157 C ATOM 414 O THR A 72 20.369 -5.797 47.917 1.00 18.18 O ANISOU 414 O THR A 72 2057 2219 2628 549 -396 -121 O ATOM 415 CB THR A 72 19.133 -8.266 49.008 1.00 16.31 C ANISOU 415 CB THR A 72 1684 2162 2350 508 -199 201 C ATOM 416 OG1 THR A 72 18.072 -9.081 49.509 1.00 17.77 O ANISOU 416 OG1 THR A 72 1671 2128 2953 640 -52 341 O ATOM 417 CG2 THR A 72 20.480 -8.868 49.459 1.00 15.80 C ANISOU 417 CG2 THR A 72 1446 2195 2360 359 -121 40 C ATOM 418 N SER A 73 20.777 -5.360 50.099 1.00 17.46 N ANISOU 418 N SER A 73 1680 2178 2775 -4 -7 232 N ATOM 419 CA SER A 73 21.773 -4.318 49.849 1.00 17.44 C ANISOU 419 CA SER A 73 1523 2199 2903 130 250 223 C ATOM 420 C SER A 73 22.736 -4.203 51.018 1.00 18.93 C ANISOU 420 C SER A 73 1515 2695 2982 68 235 177 C ATOM 421 O SER A 73 22.355 -4.451 52.160 1.00 20.18 O ANISOU 421 O SER A 73 2154 2893 2619 196 -74 130 O ATOM 422 CB SER A 73 21.040 -2.983 49.659 1.00 18.74 C ANISOU 422 CB SER A 73 2143 2166 2810 260 -72 190 C ATOM 423 OG SER A 73 21.903 -1.863 49.753 1.00 19.52 O ANISOU 423 OG SER A 73 1967 2438 3010 176 -222 -130 O ATOM 424 N ARG A 74 23.977 -3.810 50.730 1.00 19.37 N ANISOU 424 N ARG A 74 1428 2953 2976 53 190 -101 N ATOM 425 CA ARG A 74 24.948 -3.500 51.784 1.00 20.84 C ANISOU 425 CA ARG A 74 1694 3184 3040 209 -31 -116 C ATOM 426 C ARG A 74 24.828 -2.070 52.326 1.00 22.00 C ANISOU 426 C ARG A 74 2204 3147 3007 -15 -608 -183 C ATOM 427 O ARG A 74 25.514 -1.722 53.294 1.00 25.53 O ANISOU 427 O ARG A 74 2404 3518 3776 -15 -1062 -623 O ATOM 428 CB ARG A 74 26.376 -3.745 51.290 1.00 22.14 C ANISOU 428 CB ARG A 74 1536 3516 3359 -219 61 -47 C ATOM 429 CG ARG A 74 26.683 -5.209 51.033 1.00 28.67 C ANISOU 429 CG ARG A 74 3385 3516 3992 -96 88 -36 C ATOM 430 CD ARG A 74 27.968 -5.410 50.240 1.00 34.26 C ANISOU 430 CD ARG A 74 4071 4465 4478 -84 691 -54 C ATOM 431 NE ARG A 74 27.798 -4.956 48.857 0.75 37.28 N ANISOU 431 NE ARG A 74 4816 4626 4721 427 462 28 N ATOM 432 CZ ARG A 74 28.509 -5.354 47.802 0.75 39.00 C ANISOU 432 CZ ARG A 74 4197 4696 5922 1183 690 -286 C ATOM 433 NH1 ARG A 74 29.491 -6.250 47.912 0.75 38.30 N ANISOU 433 NH1 ARG A 74 4727 4069 5753 1125 154 -152 N ATOM 434 NH2 ARG A 74 28.221 -4.842 46.604 0.75 35.21 N ANISOU 434 NH2 ARG A 74 3443 4294 5640 2576 1296 -793 N ATOM 435 N ALA A 75 23.961 -1.258 51.723 1.00 24.03 N ANISOU 435 N ALA A 75 2294 3121 3715 219 -594 -184 N ATOM 436 CA ALA A 75 23.786 0.142 52.108 1.00 24.83 C ANISOU 436 CA ALA A 75 2894 3073 3464 -33 -185 -130 C ATOM 437 C ALA A 75 23.048 0.287 53.440 1.00 25.14 C ANISOU 437 C ALA A 75 2778 3355 3419 -346 -183 89 C ATOM 438 O ALA A 75 22.257 -0.569 53.811 1.00 24.70 O ANISOU 438 O ALA A 75 1952 4060 3372 -23 640 140 O ATOM 439 CB ALA A 75 23.027 0.884 51.016 1.00 23.16 C ANISOU 439 CB ALA A 75 2707 2809 3281 -37 20 -198 C ATOM 440 N ALA A 76 23.337 1.371 54.154 1.00 26.10 N ANISOU 440 N ALA A 76 3044 3268 3603 221 -415 -65 N ATOM 441 CA ALA A 76 22.606 1.753 55.359 1.00 26.48 C ANISOU 441 CA ALA A 76 3355 3063 3641 890 -483 153 C ATOM 442 C ALA A 76 21.786 2.984 55.002 1.00 25.81 C ANISOU 442 C ALA A 76 3508 2761 3536 822 -463 -24 C ATOM 443 O ALA A 76 22.336 4.079 54.864 1.00 26.72 O ANISOU 443 O ALA A 76 4021 2816 3315 598 -558 -258 O ATOM 444 CB ALA A 76 23.573 2.059 56.493 1.00 31.00 C ANISOU 444 CB ALA A 76 3687 3993 4098 626 -701 -242 C ATOM 445 N VAL A 77 20.480 2.793 54.828 1.00 23.69 N ANISOU 445 N VAL A 77 3457 2045 3498 775 -379 88 N ATOM 446 CA VAL A 77 19.592 3.851 54.338 1.00 23.16 C ANISOU 446 CA VAL A 77 3085 2549 3164 719 -353 350 C ATOM 447 C VAL A 77 18.607 4.284 55.424 1.00 26.03 C ANISOU 447 C VAL A 77 3009 3497 3383 626 -160 310 C ATOM 448 O VAL A 77 17.964 3.450 56.063 1.00 25.39 O ANISOU 448 O VAL A 77 2737 3186 3724 978 -20 340 O ATOM 449 CB VAL A 77 18.843 3.392 53.068 1.00 24.07 C ANISOU 449 CB VAL A 77 3175 2695 3272 464 -155 -20 C ATOM 450 CG1 VAL A 77 17.807 4.422 52.629 1.00 24.70 C ANISOU 450 CG1 VAL A 77 3185 2962 3238 483 -240 135 C ATOM 451 CG2 VAL A 77 19.843 3.150 51.949 1.00 24.48 C ANISOU 451 CG2 VAL A 77 3087 2984 3230 153 -183 -128 C ATOM 452 N ASP A 78 18.509 5.597 55.617 1.00 25.34 N ANISOU 452 N ASP A 78 2465 3680 3482 533 -207 -60 N ATOM 453 CA ASP A 78 17.567 6.194 56.553 1.00 26.73 C ANISOU 453 CA ASP A 78 3081 3523 3551 879 -94 -2 C ATOM 454 C ASP A 78 16.289 6.474 55.774 1.00 23.37 C ANISOU 454 C ASP A 78 3039 2880 2958 810 61 -68 C ATOM 455 O ASP A 78 16.188 7.498 55.100 1.00 23.91 O ANISOU 455 O ASP A 78 2987 3344 2753 975 -415 114 O ATOM 456 CB ASP A 78 18.166 7.476 57.142 1.00 29.05 C ANISOU 456 CB ASP A 78 3206 3650 4180 1000 -238 -291 C ATOM 457 CG ASP A 78 17.235 8.183 58.117 1.00 31.99 C ANISOU 457 CG ASP A 78 4466 3537 4152 1275 -249 -773 C ATOM 458 OD1 ASP A 78 16.053 7.793 58.259 1.00 30.43 O ANISOU 458 OD1 ASP A 78 4475 3488 3596 1223 -786 -725 O ATOM 459 OD2 ASP A 78 17.705 9.151 58.744 1.00 38.71 O ANISOU 459 OD2 ASP A 78 5430 3419 5856 1414 -618 -1353 O ATOM 460 N TYR A 79 15.318 5.564 55.872 1.00 24.52 N ANISOU 460 N TYR A 79 3974 2807 2533 528 -273 1394 N ATOM 461 CA TYR A 79 14.105 5.656 55.045 1.00 24.51 C ANISOU 461 CA TYR A 79 3389 3145 2777 922 1 146 C ATOM 462 C TYR A 79 13.241 6.871 55.377 1.00 23.03 C ANISOU 462 C TYR A 79 3074 3454 2223 1073 -243 117 C ATOM 463 O TYR A 79 12.607 7.424 54.489 1.00 23.94 O ANISOU 463 O TYR A 79 2885 3311 2900 1425 -215 295 O ATOM 464 CB TYR A 79 13.279 4.370 55.116 1.00 24.58 C ANISOU 464 CB TYR A 79 3349 3211 2779 829 144 100 C ATOM 465 CG TYR A 79 13.992 3.200 54.484 1.00 23.14 C ANISOU 465 CG TYR A 79 3007 3326 2458 613 103 -82 C ATOM 466 CD1 TYR A 79 14.066 3.073 53.098 1.00 20.56 C ANISOU 466 CD1 TYR A 79 2566 2882 2361 343 -32 151 C ATOM 467 CD2 TYR A 79 14.622 2.234 55.268 1.00 24.06 C ANISOU 467 CD2 TYR A 79 3031 3068 3041 854 112 -243 C ATOM 468 CE1 TYR A 79 14.737 2.014 52.512 1.00 20.80 C ANISOU 468 CE1 TYR A 79 2423 2999 2479 302 -200 -54 C ATOM 469 CE2 TYR A 79 15.289 1.163 54.689 1.00 23.85 C ANISOU 469 CE2 TYR A 79 2643 3483 2935 1093 45 -239 C ATOM 470 CZ TYR A 79 15.344 1.058 53.310 1.00 21.80 C ANISOU 470 CZ TYR A 79 2565 2847 2869 449 -164 -75 C ATOM 471 OH TYR A 79 16.014 0.009 52.724 1.00 20.97 O ANISOU 471 OH TYR A 79 2498 2326 3141 24 -20 -96 O ATOM 472 N GLN A 80 13.237 7.283 56.646 1.00 23.45 N ANISOU 472 N GLN A 80 3009 3910 1989 2524 -844 356 N ATOM 473 CA GLN A 80 12.513 8.485 57.081 1.00 24.02 C ANISOU 473 CA GLN A 80 2951 3323 2851 1533 -391 -262 C ATOM 474 C GLN A 80 13.021 9.738 56.369 1.00 21.98 C ANISOU 474 C GLN A 80 2068 3962 2319 958 -396 -362 C ATOM 475 O GLN A 80 12.237 10.533 55.848 1.00 24.46 O ANISOU 475 O GLN A 80 2881 3978 2432 1163 -444 -130 O ATOM 476 CB GLN A 80 12.655 8.678 58.597 1.00 28.65 C ANISOU 476 CB GLN A 80 3914 4044 2926 999 -649 -284 C ATOM 477 CG GLN A 80 11.973 7.612 59.442 1.00 32.56 C ANISOU 477 CG GLN A 80 4675 4123 3571 924 -424 -61 C ATOM 478 CD GLN A 80 10.462 7.733 59.463 1.00 34.67 C ANISOU 478 CD GLN A 80 4860 4304 4009 1338 -1099 -209 C ATOM 479 OE1 GLN A 80 9.906 8.792 59.184 1.00 33.86 O ANISOU 479 OE1 GLN A 80 4649 4559 3654 1710 -944 -576 O ATOM 480 NE2 GLN A 80 9.788 6.642 59.816 1.00 43.33 N ANISOU 480 NE2 GLN A 80 7667 2412 6382 2535 -1508 997 N ATOM 481 N LYS A 81 14.340 9.897 56.352 1.00 21.13 N ANISOU 481 N LYS A 81 2127 3240 2659 552 -650 -565 N ATOM 482 CA LYS A 81 14.994 11.026 55.701 1.00 23.62 C ANISOU 482 CA LYS A 81 2257 3311 3404 502 -501 -443 C ATOM 483 C LYS A 81 14.755 11.047 54.190 1.00 21.62 C ANISOU 483 C LYS A 81 2223 2482 3508 370 -681 -454 C ATOM 484 O LYS A 81 14.375 12.079 53.634 1.00 22.59 O ANISOU 484 O LYS A 81 2546 2393 3643 845 -491 -683 O ATOM 485 CB LYS A 81 16.501 10.981 55.992 1.00 25.20 C ANISOU 485 CB LYS A 81 2268 3888 3418 432 -536 -556 C ATOM 486 CG LYS A 81 17.297 12.164 55.476 1.00 29.74 C ANISOU 486 CG LYS A 81 3480 3808 4012 289 -439 -274 C ATOM 487 CD LYS A 81 18.653 12.229 56.165 0.50 31.75 C ANISOU 487 CD LYS A 81 3608 4305 4150 390 -564 102 C ATOM 488 CE LYS A 81 19.508 13.366 55.637 0.50 36.44 C ANISOU 488 CE LYS A 81 4072 4785 4988 125 -81 261 C ATOM 489 NZ LYS A 81 20.087 13.050 54.303 0.50 37.96 N ANISOU 489 NZ LYS A 81 4455 4944 5023 440 -124 190 N ATOM 490 N VAL A 82 14.963 9.906 53.539 1.00 21.97 N ANISOU 490 N VAL A 82 2137 2653 3558 697 -437 -463 N ATOM 491 CA VAL A 82 14.813 9.808 52.082 1.00 21.60 C ANISOU 491 CA VAL A 82 1703 2995 3507 397 -327 -228 C ATOM 492 C VAL A 82 13.378 10.135 51.648 1.00 19.83 C ANISOU 492 C VAL A 82 1782 2512 3237 259 -463 -197 C ATOM 493 O VAL A 82 13.167 10.941 50.738 1.00 19.96 O ANISOU 493 O VAL A 82 1778 2269 3535 431 -755 -271 O ATOM 494 CB VAL A 82 15.237 8.419 51.553 1.00 21.27 C ANISOU 494 CB VAL A 82 1819 2958 3303 227 -284 -258 C ATOM 495 CG1 VAL A 82 14.926 8.281 50.067 1.00 24.68 C ANISOU 495 CG1 VAL A 82 2824 3391 3159 194 1 -263 C ATOM 496 CG2 VAL A 82 16.730 8.193 51.787 1.00 20.70 C ANISOU 496 CG2 VAL A 82 1785 3135 2944 301 -128 -288 C ATOM 497 N VAL A 83 12.406 9.525 52.314 1.00 19.11 N ANISOU 497 N VAL A 83 2034 2411 2815 408 -296 -128 N ATOM 498 CA VAL A 83 10.998 9.760 51.999 1.00 19.35 C ANISOU 498 CA VAL A 83 2054 2659 2639 233 -480 -75 C ATOM 499 C VAL A 83 10.613 11.225 52.235 1.00 20.62 C ANISOU 499 C VAL A 83 2166 2669 2997 94 -178 -292 C ATOM 500 O VAL A 83 10.009 11.858 51.357 1.00 18.97 O ANISOU 500 O VAL A 83 1959 2509 2738 -292 -106 -316 O ATOM 501 CB VAL A 83 10.069 8.827 52.806 1.00 20.50 C ANISOU 501 CB VAL A 83 2440 2678 2669 207 -324 -51 C ATOM 502 CG1 VAL A 83 8.600 9.232 52.642 1.00 21.66 C ANISOU 502 CG1 VAL A 83 2457 2796 2976 242 -298 9 C ATOM 503 CG2 VAL A 83 10.261 7.380 52.366 1.00 21.12 C ANISOU 503 CG2 VAL A 83 2673 2625 2726 326 -277 92 C ATOM 504 N ARG A 84 10.963 11.763 53.405 1.00 19.10 N ANISOU 504 N ARG A 84 2125 2385 2748 303 -18 -76 N ATOM 505 CA ARG A 84 10.550 13.128 53.777 1.00 19.97 C ANISOU 505 CA ARG A 84 2275 2344 2966 343 101 -21 C ATOM 506 C ARG A 84 11.195 14.199 52.889 1.00 18.08 C ANISOU 506 C ARG A 84 1752 2311 2803 387 12 -125 C ATOM 507 O ARG A 84 10.536 15.164 52.511 1.00 16.50 O ANISOU 507 O ARG A 84 1612 2134 2522 196 16 -89 O ATOM 508 CB ARG A 84 10.795 13.398 55.271 1.00 19.95 C ANISOU 508 CB ARG A 84 2107 2394 3077 401 55 -149 C ATOM 509 CG ARG A 84 9.862 12.599 56.168 1.00 20.82 C ANISOU 509 CG ARG A 84 2362 2372 3173 680 256 97 C ATOM 510 CD ARG A 84 10.128 12.762 57.658 1.00 21.01 C ANISOU 510 CD ARG A 84 2616 1832 3535 1044 -239 -405 C ATOM 511 NE ARG A 84 9.440 11.714 58.430 1.00 28.90 N ANISOU 511 NE ARG A 84 3776 1729 5474 1822 -53 1116 N ATOM 512 CZ ARG A 84 8.137 11.707 58.747 1.00 22.71 C ANISOU 512 CZ ARG A 84 3714 2116 2798 960 -370 473 C ATOM 513 NH1 ARG A 84 7.333 12.697 58.384 1.00 19.60 N ANISOU 513 NH1 ARG A 84 2474 2408 2566 817 -215 145 N ATOM 514 NH2 ARG A 84 7.623 10.690 59.439 1.00 27.93 N ANISOU 514 NH2 ARG A 84 4272 1655 4683 1913 234 1388 N ATOM 515 N GLU A 85 12.468 14.014 52.534 1.00 18.83 N ANISOU 515 N GLU A 85 1833 2686 2635 272 192 -168 N ATOM 516 CA GLU A 85 13.144 14.930 51.601 1.00 19.39 C ANISOU 516 CA GLU A 85 1904 2571 2893 79 107 -145 C ATOM 517 C GLU A 85 12.534 14.946 50.192 1.00 19.39 C ANISOU 517 C GLU A 85 1982 2499 2887 87 119 -190 C ATOM 518 O GLU A 85 12.455 16.002 49.554 1.00 19.01 O ANISOU 518 O GLU A 85 1302 2390 3531 -15 -99 -92 O ATOM 519 CB GLU A 85 14.637 14.617 51.533 1.00 19.88 C ANISOU 519 CB GLU A 85 2019 2558 2975 258 149 -293 C ATOM 520 CG GLU A 85 15.349 15.071 52.789 0.75 23.68 C ANISOU 520 CG GLU A 85 2545 3291 3161 161 -102 -414 C ATOM 521 CD GLU A 85 16.830 14.773 52.799 0.50 25.40 C ANISOU 521 CD GLU A 85 2503 3661 3487 150 158 -639 C ATOM 522 OE1 GLU A 85 17.372 14.261 51.796 0.50 24.62 O ANISOU 522 OE1 GLU A 85 1739 3739 3874 265 265 -656 O ATOM 523 OE2 GLU A 85 17.448 15.063 53.836 0.50 28.72 O ANISOU 523 OE2 GLU A 85 1404 4348 5159 -570 -617 -901 O ATOM 524 N ALA A 86 12.090 13.781 49.721 1.00 18.08 N ANISOU 524 N ALA A 86 1948 2472 2450 364 -79 -264 N ATOM 525 CA ALA A 86 11.440 13.684 48.426 1.00 17.35 C ANISOU 525 CA ALA A 86 1810 2283 2497 156 -96 -150 C ATOM 526 C ALA A 86 10.118 14.449 48.432 1.00 17.83 C ANISOU 526 C ALA A 86 1915 2257 2599 260 34 -112 C ATOM 527 O ALA A 86 9.817 15.174 47.485 1.00 18.30 O ANISOU 527 O ALA A 86 1804 2352 2797 -121 -281 -32 O ATOM 528 CB ALA A 86 11.212 12.227 48.051 1.00 16.55 C ANISOU 528 CB ALA A 86 1741 2272 2274 -107 4 -44 C ATOM 529 N VAL A 87 9.347 14.305 49.507 1.00 16.86 N ANISOU 529 N VAL A 87 1771 2203 2433 442 -156 210 N ATOM 530 CA VAL A 87 8.043 14.980 49.625 1.00 16.00 C ANISOU 530 CA VAL A 87 1795 1991 2294 416 -116 185 C ATOM 531 C VAL A 87 8.224 16.497 49.773 1.00 15.83 C ANISOU 531 C VAL A 87 1566 1979 2469 330 -110 392 C ATOM 532 O VAL A 87 7.443 17.268 49.222 1.00 16.09 O ANISOU 532 O VAL A 87 1727 1429 2955 341 66 459 O ATOM 533 CB VAL A 87 7.191 14.401 50.779 1.00 15.50 C ANISOU 533 CB VAL A 87 1843 1801 2244 292 -56 -18 C ATOM 534 CG1 VAL A 87 5.891 15.184 50.963 1.00 15.44 C ANISOU 534 CG1 VAL A 87 2038 1669 2159 431 -22 94 C ATOM 535 CG2 VAL A 87 6.859 12.936 50.517 1.00 14.94 C ANISOU 535 CG2 VAL A 87 1710 1880 2084 125 12 -24 C ATOM 536 N LYS A 88 9.251 16.914 50.513 1.00 16.63 N ANISOU 536 N LYS A 88 1666 1652 3000 758 -838 1005 N ATOM 537 CA LYS A 88 9.624 18.330 50.602 1.00 18.31 C ANISOU 537 CA LYS A 88 1836 2093 3028 64 -231 386 C ATOM 538 C LYS A 88 9.914 18.919 49.220 1.00 18.67 C ANISOU 538 C LYS A 88 2253 1862 2977 234 -385 388 C ATOM 539 O LYS A 88 9.381 19.975 48.878 1.00 18.97 O ANISOU 539 O LYS A 88 2408 1177 3622 -51 -236 95 O ATOM 540 CB LYS A 88 10.850 18.514 51.503 1.00 19.22 C ANISOU 540 CB LYS A 88 1817 2586 2898 -177 -112 184 C ATOM 541 CG LYS A 88 11.264 19.967 51.691 1.00 21.03 C ANISOU 541 CG LYS A 88 1499 2992 3498 -698 46 35 C ATOM 542 CD LYS A 88 12.576 20.055 52.440 1.00 25.64 C ANISOU 542 CD LYS A 88 1914 3880 3947 -886 -383 -49 C ATOM 543 CE LYS A 88 12.948 21.499 52.719 1.00 29.41 C ANISOU 543 CE LYS A 88 2441 3967 4766 -1215 -480 101 C ATOM 544 NZ LYS A 88 14.167 21.515 53.565 1.00 35.73 N ANISOU 544 NZ LYS A 88 2801 5150 5623 -1155 -1008 219 N ATOM 545 N HIS A 89 10.749 18.234 48.438 1.00 18.77 N ANISOU 545 N HIS A 89 1901 2098 3132 -302 -268 33 N ATOM 546 CA HIS A 89 11.087 18.674 47.069 1.00 22.27 C ANISOU 546 CA HIS A 89 2554 2761 3144 -260 -172 81 C ATOM 547 C HIS A 89 9.851 18.894 46.188 1.00 20.20 C ANISOU 547 C HIS A 89 2370 2196 3107 -407 -74 245 C ATOM 548 O HIS A 89 9.772 19.858 45.426 1.00 20.41 O ANISOU 548 O HIS A 89 2189 2377 3187 -681 0 407 O ATOM 549 CB HIS A 89 12.023 17.663 46.392 1.00 26.59 C ANISOU 549 CB HIS A 89 3174 3204 3722 55 7 -158 C ATOM 550 CG HIS A 89 12.540 18.119 45.063 1.00 34.64 C ANISOU 550 CG HIS A 89 4505 4031 4624 -613 924 201 C ATOM 551 ND1 HIS A 89 11.964 17.738 43.871 1.00 38.29 N ANISOU 551 ND1 HIS A 89 5123 4815 4609 -1060 1307 -163 N ATOM 552 CD2 HIS A 89 13.567 18.942 44.740 1.00 35.53 C ANISOU 552 CD2 HIS A 89 5788 4823 2889 -1657 795 196 C ATOM 553 CE1 HIS A 89 12.619 18.298 42.870 1.00 41.13 C ANISOU 553 CE1 HIS A 89 6165 3916 5546 -4367 606 -510 C ATOM 554 NE2 HIS A 89 13.596 19.034 43.369 1.00 33.78 N ANISOU 554 NE2 HIS A 89 5482 4511 2841 -4371 1057 183 N ATOM 555 N ILE A 90 8.891 17.988 46.308 1.00 17.27 N ANISOU 555 N ILE A 90 1999 2072 2488 -162 -185 245 N ATOM 556 CA ILE A 90 7.641 18.071 45.561 1.00 16.46 C ANISOU 556 CA ILE A 90 2058 1803 2392 -76 -221 99 C ATOM 557 C ILE A 90 6.826 19.332 45.922 1.00 17.81 C ANISOU 557 C ILE A 90 2086 1869 2809 -95 -52 10 C ATOM 558 O ILE A 90 6.183 19.926 45.045 1.00 19.23 O ANISOU 558 O ILE A 90 2566 1810 2929 -251 -142 260 O ATOM 559 CB ILE A 90 6.825 16.769 45.743 1.00 16.74 C ANISOU 559 CB ILE A 90 2205 1749 2404 -68 -235 71 C ATOM 560 CG1 ILE A 90 7.543 15.617 45.024 1.00 17.15 C ANISOU 560 CG1 ILE A 90 2265 1947 2303 -44 -150 7 C ATOM 561 CG2 ILE A 90 5.413 16.917 45.193 1.00 17.46 C ANISOU 561 CG2 ILE A 90 2221 2001 2412 5 -265 -64 C ATOM 562 CD1 ILE A 90 7.095 14.233 45.444 1.00 17.22 C ANISOU 562 CD1 ILE A 90 2195 1978 2367 -311 -41 -282 C ATOM 563 N GLY A 91 6.869 19.737 47.194 1.00 17.42 N ANISOU 563 N GLY A 91 1985 1853 2778 -195 -43 118 N ATOM 564 CA GLY A 91 6.227 20.973 47.669 1.00 17.75 C ANISOU 564 CA GLY A 91 2488 1766 2487 -245 26 82 C ATOM 565 C GLY A 91 5.153 20.814 48.732 1.00 18.83 C ANISOU 565 C GLY A 91 2814 1914 2425 -151 158 181 C ATOM 566 O GLY A 91 4.541 21.805 49.139 1.00 20.72 O ANISOU 566 O GLY A 91 3760 1321 2790 -196 54 288 O ATOM 567 N TYR A 92 4.914 19.578 49.176 1.00 18.31 N ANISOU 567 N TYR A 92 2640 1876 2441 -161 238 111 N ATOM 568 CA TYR A 92 3.955 19.303 50.240 1.00 16.96 C ANISOU 568 CA TYR A 92 2382 1649 2412 80 172 80 C ATOM 569 C TYR A 92 4.600 19.523 51.621 1.00 17.27 C ANISOU 569 C TYR A 92 2186 1847 2529 64 49 217 C ATOM 570 O TYR A 92 5.201 18.622 52.204 1.00 15.92 O ANISOU 570 O TYR A 92 1917 1718 2410 -185 -108 139 O ATOM 571 CB TYR A 92 3.347 17.899 50.072 1.00 16.62 C ANISOU 571 CB TYR A 92 2127 1906 2282 -133 170 31 C ATOM 572 CG TYR A 92 2.228 17.874 49.047 1.00 16.79 C ANISOU 572 CG TYR A 92 2131 1912 2336 -77 118 15 C ATOM 573 CD1 TYR A 92 1.060 18.628 49.244 1.00 18.01 C ANISOU 573 CD1 TYR A 92 2266 2056 2518 44 28 -139 C ATOM 574 CD2 TYR A 92 2.320 17.106 47.885 1.00 17.00 C ANISOU 574 CD2 TYR A 92 2158 1786 2514 -40 175 -37 C ATOM 575 CE1 TYR A 92 0.031 18.619 48.314 1.00 16.63 C ANISOU 575 CE1 TYR A 92 1686 1850 2781 -301 209 -92 C ATOM 576 CE2 TYR A 92 1.291 17.089 46.949 1.00 17.05 C ANISOU 576 CE2 TYR A 92 2219 1716 2542 -297 117 -226 C ATOM 577 CZ TYR A 92 0.152 17.848 47.167 1.00 17.97 C ANISOU 577 CZ TYR A 92 2109 1778 2938 -354 106 -215 C ATOM 578 OH TYR A 92 -0.875 17.844 46.247 1.00 19.13 O ANISOU 578 OH TYR A 92 2082 2030 3155 31 72 -237 O ATOM 579 N ASP A 93 4.456 20.747 52.124 1.00 17.28 N ANISOU 579 N ASP A 93 2456 1653 2453 -69 17 414 N ATOM 580 CA ASP A 93 5.153 21.209 53.329 1.00 19.67 C ANISOU 580 CA ASP A 93 2502 2211 2761 -73 -161 269 C ATOM 581 C ASP A 93 4.248 21.920 54.342 1.00 18.39 C ANISOU 581 C ASP A 93 2328 2000 2657 -174 -198 314 C ATOM 582 O ASP A 93 4.726 22.686 55.183 1.00 17.82 O ANISOU 582 O ASP A 93 2307 1583 2878 -35 82 116 O ATOM 583 CB ASP A 93 6.332 22.116 52.925 1.00 21.28 C ANISOU 583 CB ASP A 93 2908 2245 2932 -303 -70 346 C ATOM 584 CG ASP A 93 5.899 23.367 52.153 1.00 22.22 C ANISOU 584 CG ASP A 93 2330 2693 3417 -749 -536 874 C ATOM 585 OD1 ASP A 93 4.688 23.595 51.930 1.00 20.40 O ANISOU 585 OD1 ASP A 93 2466 1713 3571 -432 -572 457 O ATOM 586 OD2 ASP A 93 6.792 24.130 51.747 1.00 26.61 O ANISOU 586 OD2 ASP A 93 2587 3237 4284 -1487 -1284 1235 O ATOM 587 N ASP A 94 2.943 21.668 54.268 1.00 17.46 N ANISOU 587 N ASP A 94 2272 1868 2493 -31 -156 243 N ATOM 588 CA ASP A 94 2.007 22.298 55.178 1.00 18.95 C ANISOU 588 CA ASP A 94 2397 2285 2518 -88 0 109 C ATOM 589 C ASP A 94 0.668 21.598 55.131 1.00 19.39 C ANISOU 589 C ASP A 94 2448 2167 2750 -49 -235 37 C ATOM 590 O ASP A 94 0.196 21.215 54.056 1.00 18.71 O ANISOU 590 O ASP A 94 2521 1879 2706 163 -347 186 O ATOM 591 CB ASP A 94 1.801 23.776 54.846 1.00 19.51 C ANISOU 591 CB ASP A 94 2264 2182 2966 34 194 -191 C ATOM 592 CG ASP A 94 1.193 24.538 56.005 1.00 22.32 C ANISOU 592 CG ASP A 94 2155 2560 3764 50 617 -532 C ATOM 593 OD1 ASP A 94 1.947 24.928 56.919 1.00 26.59 O ANISOU 593 OD1 ASP A 94 2235 3302 4564 -28 645 -1454 O ATOM 594 OD2 ASP A 94 -0.037 24.721 56.025 1.00 22.46 O ANISOU 594 OD2 ASP A 94 2039 2725 3769 -202 207 -282 O ATOM 595 N SER A 95 0.046 21.465 56.298 1.00 20.48 N ANISOU 595 N SER A 95 2692 2317 2772 22 -138 35 N ATOM 596 CA SER A 95 -1.259 20.824 56.395 1.00 23.43 C ANISOU 596 CA SER A 95 2917 2871 3113 -240 -148 25 C ATOM 597 C SER A 95 -2.326 21.560 55.572 1.00 22.35 C ANISOU 597 C SER A 95 3063 2322 3104 -65 -42 -78 C ATOM 598 O SER A 95 -3.249 20.924 55.079 1.00 20.57 O ANISOU 598 O SER A 95 2770 2184 2860 -143 464 -88 O ATOM 599 CB SER A 95 -1.691 20.656 57.861 1.00 25.60 C ANISOU 599 CB SER A 95 3453 3111 3163 -315 17 -64 C ATOM 600 OG SER A 95 -1.632 21.871 58.576 1.00 25.15 O ANISOU 600 OG SER A 95 2983 3651 2921 -69 236 -465 O ATOM 601 N SER A 96 -2.168 22.872 55.369 1.00 23.15 N ANISOU 601 N SER A 96 3235 2257 3302 134 -22 -154 N ATOM 602 CA SER A 96 -3.084 23.650 54.513 1.00 23.51 C ANISOU 602 CA SER A 96 3265 2413 3255 328 95 -154 C ATOM 603 C SER A 96 -3.101 23.216 53.031 1.00 20.73 C ANISOU 603 C SER A 96 2366 2400 3107 430 -35 16 C ATOM 604 O SER A 96 -4.076 23.475 52.322 1.00 20.95 O ANISOU 604 O SER A 96 2408 2842 2708 542 6 -301 O ATOM 605 CB SER A 96 -2.780 25.152 54.616 1.00 25.93 C ANISOU 605 CB SER A 96 3707 2449 3693 196 134 49 C ATOM 606 OG SER A 96 -1.572 25.489 53.956 1.00 27.47 O ANISOU 606 OG SER A 96 4057 2162 4218 225 429 340 O ATOM 607 N LYS A 97 -2.025 22.567 52.578 1.00 15.83 N ANISOU 607 N LYS A 97 1994 1663 2357 -76 -126 39 N ATOM 608 CA LYS A 97 -1.938 21.991 51.228 1.00 15.23 C ANISOU 608 CA LYS A 97 1708 1738 2338 -62 -163 29 C ATOM 609 C LYS A 97 -2.447 20.547 51.144 1.00 16.44 C ANISOU 609 C LYS A 97 1952 1774 2518 -112 -264 -166 C ATOM 610 O LYS A 97 -2.534 19.990 50.048 1.00 17.87 O ANISOU 610 O LYS A 97 2476 1960 2354 132 -317 -31 O ATOM 611 CB LYS A 97 -0.495 22.046 50.743 1.00 13.79 C ANISOU 611 CB LYS A 97 1838 1438 1962 -30 16 -8 C ATOM 612 CG LYS A 97 0.085 23.457 50.751 1.00 14.98 C ANISOU 612 CG LYS A 97 2085 1457 2148 -98 -50 15 C ATOM 613 CD LYS A 97 1.546 23.485 50.336 1.00 18.30 C ANISOU 613 CD LYS A 97 2123 2314 2515 -231 8 47 C ATOM 614 CE LYS A 97 2.044 24.923 50.254 1.00 22.23 C ANISOU 614 CE LYS A 97 2879 2467 3099 -457 1 218 C ATOM 615 NZ LYS A 97 3.475 24.976 49.874 1.00 24.22 N ANISOU 615 NZ LYS A 97 2955 3021 3226 -444 13 477 N ATOM 616 N GLY A 98 -2.761 19.945 52.293 1.00 15.78 N ANISOU 616 N GLY A 98 1930 1519 2544 -32 -265 -192 N ATOM 617 CA GLY A 98 -3.307 18.585 52.373 1.00 15.62 C ANISOU 617 CA GLY A 98 1680 1697 2557 -175 -155 -156 C ATOM 618 C GLY A 98 -2.314 17.491 52.724 1.00 15.32 C ANISOU 618 C GLY A 98 1547 1685 2587 -223 -167 -129 C ATOM 619 O GLY A 98 -2.719 16.348 52.934 1.00 14.76 O ANISOU 619 O GLY A 98 1007 1701 2900 -119 -228 -72 O ATOM 620 N PHE A 99 -1.023 17.833 52.785 1.00 15.36 N ANISOU 620 N PHE A 99 1363 1774 2699 91 -27 -21 N ATOM 621 CA PHE A 99 0.041 16.873 53.054 1.00 15.14 C ANISOU 621 CA PHE A 99 1604 1575 2571 97 22 135 C ATOM 622 C PHE A 99 1.297 17.646 53.471 1.00 16.12 C ANISOU 622 C PHE A 99 1658 1827 2639 59 -55 45 C ATOM 623 O PHE A 99 1.577 18.722 52.925 1.00 16.73 O ANISOU 623 O PHE A 99 1930 1946 2480 94 -149 188 O ATOM 624 CB PHE A 99 0.320 16.034 51.803 1.00 15.48 C ANISOU 624 CB PHE A 99 1803 1521 2558 -83 -32 109 C ATOM 625 CG PHE A 99 0.896 14.669 52.088 1.00 15.21 C ANISOU 625 CG PHE A 99 1688 1505 2584 -5 229 2 C ATOM 626 CD1 PHE A 99 2.263 14.492 52.257 1.00 17.02 C ANISOU 626 CD1 PHE A 99 1700 1978 2788 -1 199 107 C ATOM 627 CD2 PHE A 99 0.067 13.556 52.170 1.00 15.63 C ANISOU 627 CD2 PHE A 99 1824 1476 2638 -39 81 67 C ATOM 628 CE1 PHE A 99 2.793 13.234 52.510 1.00 17.07 C ANISOU 628 CE1 PHE A 99 1895 1816 2774 -141 324 109 C ATOM 629 CE2 PHE A 99 0.590 12.294 52.426 1.00 15.69 C ANISOU 629 CE2 PHE A 99 1731 1566 2664 50 230 105 C ATOM 630 CZ PHE A 99 1.956 12.134 52.597 1.00 16.38 C ANISOU 630 CZ PHE A 99 1729 1783 2711 -66 113 129 C ATOM 631 N ASP A 100 2.041 17.104 54.433 1.00 17.00 N ANISOU 631 N ASP A 100 2051 1717 2690 195 -155 -3 N ATOM 632 CA ASP A 100 3.246 17.758 54.954 1.00 16.46 C ANISOU 632 CA ASP A 100 1911 1791 2550 280 -73 -35 C ATOM 633 C ASP A 100 4.352 16.738 55.251 1.00 17.34 C ANISOU 633 C ASP A 100 1971 1993 2624 356 -61 148 C ATOM 634 O ASP A 100 4.169 15.853 56.093 1.00 17.43 O ANISOU 634 O ASP A 100 2077 1721 2823 332 -204 151 O ATOM 635 CB ASP A 100 2.887 18.530 56.226 1.00 16.51 C ANISOU 635 CB ASP A 100 1960 1812 2499 -28 57 -48 C ATOM 636 CG ASP A 100 4.093 19.147 56.910 1.00 17.49 C ANISOU 636 CG ASP A 100 1700 2148 2796 135 116 -293 C ATOM 637 OD1 ASP A 100 5.108 19.424 56.245 1.00 17.28 O ANISOU 637 OD1 ASP A 100 1962 1583 3018 -53 269 -133 O ATOM 638 OD2 ASP A 100 4.032 19.351 58.137 1.00 22.96 O ANISOU 638 OD2 ASP A 100 2260 3424 3039 -241 55 -898 O ATOM 639 N TYR A 101 5.506 16.898 54.596 1.00 17.61 N ANISOU 639 N TYR A 101 1888 2209 2591 128 -185 176 N ATOM 640 CA TYR A 101 6.668 16.017 54.830 1.00 17.33 C ANISOU 640 CA TYR A 101 1740 2211 2633 73 -215 -94 C ATOM 641 C TYR A 101 7.146 15.972 56.290 1.00 16.89 C ANISOU 641 C TYR A 101 1746 2090 2581 332 -94 -113 C ATOM 642 O TYR A 101 7.712 14.967 56.720 1.00 17.54 O ANISOU 642 O TYR A 101 1909 1798 2956 324 27 -219 O ATOM 643 CB TYR A 101 7.842 16.404 53.922 1.00 17.18 C ANISOU 643 CB TYR A 101 1664 2389 2474 -160 -450 -90 C ATOM 644 CG TYR A 101 8.612 17.627 54.373 1.00 18.09 C ANISOU 644 CG TYR A 101 1856 2223 2792 -232 -419 68 C ATOM 645 CD1 TYR A 101 8.213 18.915 54.007 1.00 18.72 C ANISOU 645 CD1 TYR A 101 1749 2185 3178 -47 -241 -90 C ATOM 646 CD2 TYR A 101 9.749 17.492 55.166 1.00 18.34 C ANISOU 646 CD2 TYR A 101 1669 2273 3024 -197 -379 105 C ATOM 647 CE1 TYR A 101 8.925 20.031 54.432 1.00 18.82 C ANISOU 647 CE1 TYR A 101 1656 2226 3266 -166 -285 103 C ATOM 648 CE2 TYR A 101 10.464 18.597 55.593 1.00 19.76 C ANISOU 648 CE2 TYR A 101 1926 2349 3232 -367 -291 53 C ATOM 649 CZ TYR A 101 10.055 19.862 55.228 1.00 18.17 C ANISOU 649 CZ TYR A 101 1407 2310 3187 -437 -144 15 C ATOM 650 OH TYR A 101 10.784 20.948 55.661 1.00 21.58 O ANISOU 650 OH TYR A 101 2299 2393 3505 -576 -468 -219 O ATOM 651 N LYS A 102 6.956 17.065 57.029 1.00 17.14 N ANISOU 651 N LYS A 102 1732 1991 2789 -5 -39 -211 N ATOM 652 CA LYS A 102 7.372 17.144 58.438 1.00 18.63 C ANISOU 652 CA LYS A 102 1954 2289 2835 12 -139 -91 C ATOM 653 C LYS A 102 6.568 16.256 59.377 1.00 17.34 C ANISOU 653 C LYS A 102 1785 1940 2863 19 -348 -86 C ATOM 654 O LYS A 102 7.115 15.754 60.359 1.00 17.57 O ANISOU 654 O LYS A 102 1434 2158 3084 153 -280 92 O ATOM 655 CB LYS A 102 7.284 18.586 58.963 1.00 19.48 C ANISOU 655 CB LYS A 102 2465 2335 2599 -147 -185 -115 C ATOM 656 CG LYS A 102 8.169 19.589 58.236 1.00 19.00 C ANISOU 656 CG LYS A 102 2182 2328 2707 -180 -198 -215 C ATOM 657 CD LYS A 102 8.113 20.979 58.868 1.00 20.87 C ANISOU 657 CD LYS A 102 2717 2293 2919 -102 -233 -214 C ATOM 658 CE LYS A 102 6.738 21.646 58.832 1.00 22.02 C ANISOU 658 CE LYS A 102 2756 2533 3076 -40 -279 26 C ATOM 659 NZ LYS A 102 6.200 21.838 57.459 1.00 22.03 N ANISOU 659 NZ LYS A 102 3003 2235 3129 156 -246 288 N ATOM 660 N THR A 103 5.279 16.078 59.085 1.00 16.30 N ANISOU 660 N THR A 103 1664 1851 2677 -42 -70 82 N ATOM 661 CA THR A 103 4.336 15.472 60.032 1.00 16.33 C ANISOU 661 CA THR A 103 1884 1687 2631 -79 -71 140 C ATOM 662 C THR A 103 3.564 14.243 59.522 1.00 16.48 C ANISOU 662 C THR A 103 2009 1659 2592 -167 88 168 C ATOM 663 O THR A 103 2.766 13.683 60.273 1.00 18.52 O ANISOU 663 O THR A 103 2197 2223 2615 -515 88 196 O ATOM 664 CB THR A 103 3.322 16.539 60.507 1.00 16.51 C ANISOU 664 CB THR A 103 1907 1715 2649 -104 -52 20 C ATOM 665 OG1 THR A 103 2.688 17.140 59.369 1.00 17.21 O ANISOU 665 OG1 THR A 103 1993 1833 2713 -203 -69 125 O ATOM 666 CG2 THR A 103 4.029 17.621 61.322 1.00 17.37 C ANISOU 666 CG2 THR A 103 2519 1591 2490 148 -241 -54 C ATOM 667 N CYS A 104 3.796 13.809 58.279 1.00 16.91 N ANISOU 667 N CYS A 104 2152 1698 2574 -23 -22 173 N ATOM 668 CA CYS A 104 3.142 12.604 57.751 1.00 17.05 C ANISOU 668 CA CYS A 104 2227 1670 2578 205 -184 -26 C ATOM 669 C CYS A 104 3.718 11.338 58.399 1.00 17.44 C ANISOU 669 C CYS A 104 2399 1722 2504 84 -342 82 C ATOM 670 O CYS A 104 4.806 11.358 58.971 1.00 17.14 O ANISOU 670 O CYS A 104 2221 1757 2534 494 -225 262 O ATOM 671 CB CYS A 104 3.272 12.523 56.215 1.00 16.39 C ANISOU 671 CB CYS A 104 1816 1792 2619 38 -89 -238 C ATOM 672 SG CYS A 104 4.952 12.249 55.599 1.00 17.95 S ANISOU 672 SG CYS A 104 1856 2219 2745 326 -84 -79 S ATOM 673 N ASN A 105 2.960 10.252 58.308 1.00 17.77 N ANISOU 673 N ASN A 105 2401 1697 2651 60 -122 281 N ATOM 674 CA ASN A 105 3.389 8.927 58.760 1.00 17.76 C ANISOU 674 CA ASN A 105 2459 1809 2478 146 -265 266 C ATOM 675 C ASN A 105 4.210 8.278 57.654 1.00 18.36 C ANISOU 675 C ASN A 105 2629 2077 2268 243 -316 270 C ATOM 676 O ASN A 105 3.817 8.319 56.495 1.00 19.27 O ANISOU 676 O ASN A 105 2861 2493 1967 466 50 -250 O ATOM 677 CB ASN A 105 2.144 8.080 59.108 1.00 17.79 C ANISOU 677 CB ASN A 105 2667 1809 2280 22 -119 186 C ATOM 678 CG ASN A 105 2.460 6.622 59.435 1.00 19.76 C ANISOU 678 CG ASN A 105 2920 1840 2749 163 -188 119 C ATOM 679 OD1 ASN A 105 3.562 6.268 59.870 1.00 21.37 O ANISOU 679 OD1 ASN A 105 3254 1823 3040 442 -517 50 O ATOM 680 ND2 ASN A 105 1.465 5.765 59.244 1.00 19.56 N ANISOU 680 ND2 ASN A 105 3013 1697 2722 132 45 -50 N ATOM 681 N VAL A 106 5.360 7.713 58.016 1.00 18.76 N ANISOU 681 N VAL A 106 2800 2046 2282 497 -268 120 N ATOM 682 CA VAL A 106 6.150 6.874 57.113 1.00 21.45 C ANISOU 682 CA VAL A 106 3502 2179 2468 696 -148 -33 C ATOM 683 C VAL A 106 6.237 5.486 57.749 1.00 20.94 C ANISOU 683 C VAL A 106 3272 1876 2806 895 -624 -291 C ATOM 684 O VAL A 106 6.789 5.353 58.842 1.00 21.65 O ANISOU 684 O VAL A 106 3713 1814 2698 988 -650 -411 O ATOM 685 CB VAL A 106 7.565 7.437 56.853 1.00 22.31 C ANISOU 685 CB VAL A 106 3125 2770 2580 983 -242 -281 C ATOM 686 CG1 VAL A 106 8.337 6.538 55.896 1.00 24.66 C ANISOU 686 CG1 VAL A 106 3026 2981 3362 1145 -20 -400 C ATOM 687 CG2 VAL A 106 7.480 8.828 56.256 1.00 20.55 C ANISOU 687 CG2 VAL A 106 3454 2582 1772 2256 245 -843 C ATOM 688 N LEU A 107 5.660 4.488 57.071 1.00 22.07 N ANISOU 688 N LEU A 107 3730 1924 2730 672 -333 -448 N ATOM 689 CA LEU A 107 5.657 3.071 57.489 1.00 21.51 C ANISOU 689 CA LEU A 107 3334 2021 2816 388 -265 -326 C ATOM 690 C LEU A 107 6.505 2.247 56.524 1.00 19.64 C ANISOU 690 C LEU A 107 2764 2013 2682 229 -58 42 C ATOM 691 O LEU A 107 6.456 2.459 55.313 1.00 18.11 O ANISOU 691 O LEU A 107 2465 1819 2595 390 -38 -210 O ATOM 692 CB LEU A 107 4.239 2.486 57.441 1.00 23.92 C ANISOU 692 CB LEU A 107 3444 3055 2588 17 -301 -276 C ATOM 693 CG LEU A 107 3.202 2.868 58.484 1.00 24.93 C ANISOU 693 CG LEU A 107 3242 3429 2800 -59 -336 -255 C ATOM 694 CD1 LEU A 107 1.803 2.484 58.017 1.00 26.59 C ANISOU 694 CD1 LEU A 107 3360 3524 3218 -306 -422 -201 C ATOM 695 CD2 LEU A 107 3.513 2.195 59.807 1.00 28.20 C ANISOU 695 CD2 LEU A 107 3827 3832 3053 -294 -374 206 C ATOM 696 N VAL A 108 7.238 1.274 57.050 1.00 19.72 N ANISOU 696 N VAL A 108 2888 2116 2487 264 79 207 N ATOM 697 CA VAL A 108 8.148 0.475 56.236 1.00 19.90 C ANISOU 697 CA VAL A 108 2766 2234 2560 391 169 400 C ATOM 698 C VAL A 108 7.877 -1.022 56.432 1.00 17.91 C ANISOU 698 C VAL A 108 2302 2222 2280 542 190 563 C ATOM 699 O VAL A 108 7.892 -1.511 57.556 1.00 16.52 O ANISOU 699 O VAL A 108 2336 1842 2099 656 340 300 O ATOM 700 CB VAL A 108 9.610 0.820 56.570 1.00 23.51 C ANISOU 700 CB VAL A 108 2904 3014 3012 105 271 133 C ATOM 701 CG1 VAL A 108 10.563 0.012 55.708 1.00 25.71 C ANISOU 701 CG1 VAL A 108 3137 3224 3407 161 384 -149 C ATOM 702 CG2 VAL A 108 9.862 2.314 56.376 1.00 26.46 C ANISOU 702 CG2 VAL A 108 3396 3038 3618 279 158 428 C ATOM 703 N ALA A 109 7.616 -1.722 55.324 1.00 17.45 N ANISOU 703 N ALA A 109 1788 2271 2569 430 115 409 N ATOM 704 CA ALA A 109 7.419 -3.171 55.300 1.00 18.75 C ANISOU 704 CA ALA A 109 2040 2321 2763 344 -61 272 C ATOM 705 C ALA A 109 8.314 -3.770 54.224 1.00 18.82 C ANISOU 705 C ALA A 109 1890 2258 3001 345 -107 129 C ATOM 706 O ALA A 109 7.842 -4.333 53.235 1.00 21.10 O ANISOU 706 O ALA A 109 2475 2087 3455 644 -120 -337 O ATOM 707 CB ALA A 109 5.954 -3.505 55.036 1.00 19.90 C ANISOU 707 CB ALA A 109 2077 2604 2878 239 -23 156 C ATOM 708 N LEU A 110 9.616 -3.625 54.424 1.00 17.63 N ANISOU 708 N LEU A 110 1917 2292 2486 270 -168 -155 N ATOM 709 CA LEU A 110 10.618 -4.087 53.466 1.00 18.00 C ANISOU 709 CA LEU A 110 2332 2101 2407 108 22 -203 C ATOM 710 C LEU A 110 11.301 -5.339 54.012 1.00 17.36 C ANISOU 710 C LEU A 110 2162 2549 1882 219 -214 -150 C ATOM 711 O LEU A 110 11.642 -5.405 55.195 1.00 18.78 O ANISOU 711 O LEU A 110 2566 2697 1869 279 -306 -261 O ATOM 712 CB LEU A 110 11.653 -2.988 53.193 1.00 17.73 C ANISOU 712 CB LEU A 110 2089 2043 2605 151 -238 -182 C ATOM 713 CG LEU A 110 11.169 -1.742 52.428 1.00 17.47 C ANISOU 713 CG LEU A 110 2095 1682 2859 -34 -21 -193 C ATOM 714 CD1 LEU A 110 12.195 -0.620 52.529 1.00 18.32 C ANISOU 714 CD1 LEU A 110 2178 1930 2850 -198 -64 -245 C ATOM 715 CD2 LEU A 110 10.869 -2.040 50.966 1.00 18.14 C ANISOU 715 CD2 LEU A 110 1934 2084 2872 168 -130 -44 C ATOM 716 N GLU A 111 11.470 -6.331 53.144 1.00 17.45 N ANISOU 716 N GLU A 111 2069 2197 2363 228 -2 -115 N ATOM 717 CA GLU A 111 12.169 -7.575 53.468 1.00 19.44 C ANISOU 717 CA GLU A 111 2341 2245 2800 218 -188 75 C ATOM 718 C GLU A 111 13.286 -7.772 52.459 1.00 18.72 C ANISOU 718 C GLU A 111 2032 1902 3176 567 -265 104 C ATOM 719 O GLU A 111 13.420 -6.989 51.522 1.00 19.36 O ANISOU 719 O GLU A 111 2009 2217 3129 325 -405 153 O ATOM 720 CB GLU A 111 11.185 -8.743 53.418 1.00 21.75 C ANISOU 720 CB GLU A 111 2609 2298 3357 81 -205 -32 C ATOM 721 CG GLU A 111 10.025 -8.584 54.398 1.00 26.10 C ANISOU 721 CG GLU A 111 2738 3358 3822 -555 68 -97 C ATOM 722 CD GLU A 111 9.127 -9.805 54.480 1.00 31.95 C ANISOU 722 CD GLU A 111 2627 4534 4977 -1387 -1045 -65 C ATOM 723 OE1 GLU A 111 9.407 -10.723 55.266 0.75 33.99 O ANISOU 723 OE1 GLU A 111 3821 3981 5111 -1159 -68 -217 O ATOM 724 OE2 GLU A 111 8.115 -9.834 53.783 0.75 31.74 O ANISOU 724 OE2 GLU A 111 4001 3610 4446 -1761 -1855 455 O ATOM 725 N GLN A 112 14.093 -8.809 52.657 1.00 20.69 N ANISOU 725 N GLN A 112 2672 1934 3253 770 -392 285 N ATOM 726 CA GLN A 112 15.150 -9.169 51.705 1.00 22.04 C ANISOU 726 CA GLN A 112 2564 2534 3274 -85 -292 -229 C ATOM 727 C GLN A 112 14.522 -9.752 50.448 1.00 19.79 C ANISOU 727 C GLN A 112 2444 2201 2874 234 -149 -46 C ATOM 728 O GLN A 112 13.433 -10.325 50.504 1.00 18.71 O ANISOU 728 O GLN A 112 2312 1626 3168 461 -65 -197 O ATOM 729 CB GLN A 112 16.094 -10.239 52.280 1.00 25.64 C ANISOU 729 CB GLN A 112 3108 2950 3683 387 2 21 C ATOM 730 CG GLN A 112 16.757 -9.925 53.610 1.00 31.71 C ANISOU 730 CG GLN A 112 3866 4236 3945 -192 5 -439 C ATOM 731 CD GLN A 112 17.702 -8.749 53.545 1.00 36.16 C ANISOU 731 CD GLN A 112 3855 5131 4752 -641 1142 43 C ATOM 732 OE1 GLN A 112 17.502 -7.744 54.230 1.00 45.12 O ANISOU 732 OE1 GLN A 112 5461 5984 5696 -733 992 -843 O ATOM 733 NE2 GLN A 112 18.746 -8.867 52.732 1.00 36.32 N ANISOU 733 NE2 GLN A 112 3760 5109 4931 -585 1127 -272 N ATOM 734 N GLN A 113 15.221 -9.640 49.326 1.00 18.81 N ANISOU 734 N GLN A 113 2496 1818 2832 173 -157 96 N ATOM 735 CA GLN A 113 14.852 -10.394 48.125 1.00 18.08 C ANISOU 735 CA GLN A 113 2292 2087 2488 207 107 167 C ATOM 736 C GLN A 113 14.749 -11.902 48.412 1.00 18.75 C ANISOU 736 C GLN A 113 2437 1940 2744 396 -210 -103 C ATOM 737 O GLN A 113 15.575 -12.471 49.131 1.00 19.41 O ANISOU 737 O GLN A 113 2457 1901 3014 -35 -592 80 O ATOM 738 CB GLN A 113 15.862 -10.153 47.002 1.00 18.56 C ANISOU 738 CB GLN A 113 2191 2201 2659 313 260 14 C ATOM 739 CG GLN A 113 15.466 -10.777 45.665 1.00 18.75 C ANISOU 739 CG GLN A 113 2012 2286 2823 143 140 -69 C ATOM 740 CD GLN A 113 16.473 -10.493 44.568 1.00 19.10 C ANISOU 740 CD GLN A 113 1859 2613 2783 67 30 -144 C ATOM 741 OE1 GLN A 113 16.119 -10.076 43.459 1.00 20.92 O ANISOU 741 OE1 GLN A 113 2206 2806 2936 247 -348 -295 O ATOM 742 NE2 GLN A 113 17.739 -10.685 44.884 1.00 18.11 N ANISOU 742 NE2 GLN A 113 1941 2151 2788 333 6 -15 N ATOM 743 N SER A 114 13.723 -12.536 47.850 1.00 18.41 N ANISOU 743 N SER A 114 2103 1948 2944 407 72 -206 N ATOM 744 CA SER A 114 13.544 -13.978 47.976 1.00 18.12 C ANISOU 744 CA SER A 114 2259 1908 2715 584 108 -186 C ATOM 745 C SER A 114 14.831 -14.705 47.571 1.00 18.73 C ANISOU 745 C SER A 114 1941 1937 3235 419 -59 -344 C ATOM 746 O SER A 114 15.355 -14.446 46.495 1.00 18.68 O ANISOU 746 O SER A 114 2174 1671 3250 350 -200 -292 O ATOM 747 CB SER A 114 12.407 -14.455 47.084 1.00 17.54 C ANISOU 747 CB SER A 114 2204 1695 2763 337 192 1 C ATOM 748 OG SER A 114 12.489 -15.851 46.865 1.00 18.01 O ANISOU 748 OG SER A 114 1867 1731 3242 677 487 9 O ATOM 749 N PRO A 115 15.345 -15.607 48.427 1.00 19.80 N ANISOU 749 N PRO A 115 2034 2385 3104 312 -61 -143 N ATOM 750 CA PRO A 115 16.532 -16.385 48.009 1.00 19.56 C ANISOU 750 CA PRO A 115 2041 2186 3203 292 -59 -90 C ATOM 751 C PRO A 115 16.302 -17.268 46.775 1.00 17.62 C ANISOU 751 C PRO A 115 1489 2218 2986 20 -9 101 C ATOM 752 O PRO A 115 17.255 -17.546 46.046 1.00 17.70 O ANISOU 752 O PRO A 115 1551 2280 2891 136 -84 84 O ATOM 753 CB PRO A 115 16.846 -17.257 49.226 1.00 23.11 C ANISOU 753 CB PRO A 115 2848 2677 3254 536 -150 28 C ATOM 754 CG PRO A 115 16.146 -16.631 50.377 1.00 25.31 C ANISOU 754 CG PRO A 115 2974 2877 3764 1303 6 133 C ATOM 755 CD PRO A 115 15.000 -15.824 49.846 1.00 21.08 C ANISOU 755 CD PRO A 115 2393 2479 3135 643 -83 73 C ATOM 756 N ASP A 116 15.055 -17.713 46.564 1.00 17.00 N ANISOU 756 N ASP A 116 1508 2050 2899 48 -117 84 N ATOM 757 CA ASP A 116 14.681 -18.500 45.382 1.00 17.53 C ANISOU 757 CA ASP A 116 1895 1917 2846 -45 -25 123 C ATOM 758 C ASP A 116 14.826 -17.687 44.091 1.00 17.84 C ANISOU 758 C ASP A 116 2092 1862 2825 152 -38 81 C ATOM 759 O ASP A 116 15.252 -18.227 43.067 1.00 20.92 O ANISOU 759 O ASP A 116 2758 1990 3199 529 273 11 O ATOM 760 CB ASP A 116 13.237 -19.038 45.501 1.00 17.54 C ANISOU 760 CB ASP A 116 2029 1956 2677 -217 -95 263 C ATOM 761 CG ASP A 116 13.072 -20.106 46.583 1.00 16.60 C ANISOU 761 CG ASP A 116 1239 2142 2925 -412 -134 442 C ATOM 762 OD1 ASP A 116 14.072 -20.550 47.193 1.00 21.07 O ANISOU 762 OD1 ASP A 116 2209 2487 3308 74 -638 671 O ATOM 763 OD2 ASP A 116 11.917 -20.517 46.814 1.00 15.87 O ANISOU 763 OD2 ASP A 116 930 2162 2938 -85 -195 343 O ATOM 764 N ILE A 117 14.470 -16.397 44.140 1.00 17.15 N ANISOU 764 N ILE A 117 1942 1851 2721 94 46 -61 N ATOM 765 CA ILE A 117 14.723 -15.483 43.018 1.00 15.81 C ANISOU 765 CA ILE A 117 1517 1986 2502 132 -46 -122 C ATOM 766 C ILE A 117 16.234 -15.270 42.857 1.00 16.78 C ANISOU 766 C ILE A 117 1503 1980 2893 177 -7 -138 C ATOM 767 O ILE A 117 16.764 -15.408 41.760 1.00 16.56 O ANISOU 767 O ILE A 117 885 2055 3351 501 173 -234 O ATOM 768 CB ILE A 117 14.000 -14.125 43.190 1.00 14.83 C ANISOU 768 CB ILE A 117 1434 2076 2123 192 -92 -103 C ATOM 769 CG1 ILE A 117 12.480 -14.337 43.106 1.00 16.86 C ANISOU 769 CG1 ILE A 117 1443 2431 2530 182 -133 2 C ATOM 770 CG2 ILE A 117 14.454 -13.124 42.127 1.00 15.74 C ANISOU 770 CG2 ILE A 117 1725 2025 2229 92 -69 -99 C ATOM 771 CD1 ILE A 117 11.648 -13.151 43.566 1.00 20.95 C ANISOU 771 CD1 ILE A 117 2439 2533 2987 424 88 -143 C ATOM 772 N ALA A 118 16.915 -14.943 43.947 1.00 16.93 N ANISOU 772 N ALA A 118 1551 2096 2783 220 100 -158 N ATOM 773 CA ALA A 118 18.352 -14.633 43.893 1.00 17.70 C ANISOU 773 CA ALA A 118 1595 2088 3040 167 136 -260 C ATOM 774 C ALA A 118 19.156 -15.773 43.266 1.00 17.71 C ANISOU 774 C ALA A 118 1637 2170 2923 269 132 -212 C ATOM 775 O ALA A 118 20.002 -15.528 42.398 1.00 19.34 O ANISOU 775 O ALA A 118 2177 2199 2972 382 448 -262 O ATOM 776 CB ALA A 118 18.884 -14.305 45.281 1.00 21.36 C ANISOU 776 CB ALA A 118 2618 2404 3090 115 -119 -141 C ATOM 777 N GLN A 119 18.881 -17.006 43.689 1.00 17.70 N ANISOU 777 N GLN A 119 1598 2274 2850 29 272 -250 N ATOM 778 CA GLN A 119 19.606 -18.177 43.164 1.00 18.83 C ANISOU 778 CA GLN A 119 2014 2340 2800 85 454 -249 C ATOM 779 C GLN A 119 19.326 -18.421 41.681 1.00 17.42 C ANISOU 779 C GLN A 119 1441 2386 2791 238 692 -501 C ATOM 780 O GLN A 119 20.208 -18.860 40.961 1.00 20.34 O ANISOU 780 O GLN A 119 1637 2912 3177 110 1038 -716 O ATOM 781 CB GLN A 119 19.361 -19.450 44.002 1.00 21.35 C ANISOU 781 CB GLN A 119 2574 2440 3096 -88 252 -80 C ATOM 782 CG GLN A 119 17.947 -20.033 43.957 1.00 22.32 C ANISOU 782 CG GLN A 119 2495 2758 3224 12 282 -225 C ATOM 783 CD GLN A 119 17.643 -20.842 42.696 1.00 24.32 C ANISOU 783 CD GLN A 119 3010 2751 3477 473 237 -514 C ATOM 784 OE1 GLN A 119 18.515 -21.530 42.161 1.00 27.47 O ANISOU 784 OE1 GLN A 119 3620 2889 3929 1160 36 -580 O ATOM 785 NE2 GLN A 119 16.405 -20.757 42.217 1.00 24.08 N ANISOU 785 NE2 GLN A 119 3354 2366 3428 906 -126 -260 N ATOM 786 N GLY A 120 18.104 -18.136 41.229 1.00 18.00 N ANISOU 786 N GLY A 120 1885 2245 2707 238 192 -159 N ATOM 787 CA GLY A 120 17.754 -18.292 39.819 1.00 19.37 C ANISOU 787 CA GLY A 120 2269 2484 2605 199 310 -122 C ATOM 788 C GLY A 120 18.222 -17.181 38.880 1.00 18.46 C ANISOU 788 C GLY A 120 2187 2298 2529 43 287 -287 C ATOM 789 O GLY A 120 18.336 -17.407 37.677 1.00 18.93 O ANISOU 789 O GLY A 120 2214 2446 2530 175 216 -257 O ATOM 790 N VAL A 121 18.488 -15.990 39.418 1.00 15.63 N ANISOU 790 N VAL A 121 1903 2100 1933 79 238 24 N ATOM 791 CA VAL A 121 18.758 -14.800 38.605 1.00 15.84 C ANISOU 791 CA VAL A 121 1602 2146 2270 -146 147 105 C ATOM 792 C VAL A 121 20.229 -14.412 38.584 1.00 16.29 C ANISOU 792 C VAL A 121 1533 2114 2542 4 401 137 C ATOM 793 O VAL A 121 20.801 -14.232 37.508 1.00 16.95 O ANISOU 793 O VAL A 121 1655 2234 2551 -248 400 268 O ATOM 794 CB VAL A 121 17.911 -13.599 39.090 1.00 18.56 C ANISOU 794 CB VAL A 121 2144 2344 2562 75 207 0 C ATOM 795 CG1 VAL A 121 18.357 -12.286 38.446 1.00 22.19 C ANISOU 795 CG1 VAL A 121 2876 2516 3038 109 154 375 C ATOM 796 CG2 VAL A 121 16.437 -13.852 38.792 1.00 18.46 C ANISOU 796 CG2 VAL A 121 2218 2409 2387 33 33 87 C ATOM 797 N HIS A 122 20.827 -14.236 39.758 1.00 17.52 N ANISOU 797 N HIS A 122 1680 2293 2682 6 265 185 N ATOM 798 CA HIS A 122 22.178 -13.648 39.819 1.00 19.12 C ANISOU 798 CA HIS A 122 1875 2391 2996 -246 324 187 C ATOM 799 C HIS A 122 23.239 -14.303 40.700 1.00 19.87 C ANISOU 799 C HIS A 122 2100 2356 3093 52 388 168 C ATOM 800 O HIS A 122 24.416 -14.004 40.510 1.00 21.03 O ANISOU 800 O HIS A 122 1805 2683 3500 236 -73 235 O ATOM 801 CB HIS A 122 22.088 -12.155 40.158 1.00 20.43 C ANISOU 801 CB HIS A 122 2057 2517 3186 110 476 -16 C ATOM 802 CG HIS A 122 21.394 -11.876 41.443 1.00 21.20 C ANISOU 802 CG HIS A 122 2155 2519 3381 21 653 -126 C ATOM 803 ND1 HIS A 122 22.023 -11.970 42.665 1.00 21.39 N ANISOU 803 ND1 HIS A 122 2065 2667 3394 275 764 -196 N ATOM 804 CD2 HIS A 122 20.112 -11.532 41.700 1.00 20.84 C ANISOU 804 CD2 HIS A 122 2358 2581 2977 373 679 -84 C ATOM 805 CE1 HIS A 122 21.159 -11.687 43.622 1.00 21.45 C ANISOU 805 CE1 HIS A 122 2208 2921 3020 360 667 -33 C ATOM 806 NE2 HIS A 122 19.996 -11.411 43.060 1.00 20.46 N ANISOU 806 NE2 HIS A 122 1685 3033 3055 276 1062 -212 N ATOM 807 N LEU A 123 22.877 -15.169 41.643 1.00 20.96 N ANISOU 807 N LEU A 123 2470 2537 2955 84 353 214 N ATOM 808 CA LEU A 123 23.906 -15.785 42.485 1.00 23.97 C ANISOU 808 CA LEU A 123 2438 3136 3534 192 -83 -154 C ATOM 809 C LEU A 123 24.764 -16.741 41.663 1.00 25.27 C ANISOU 809 C LEU A 123 2884 3342 3373 504 67 52 C ATOM 810 O LEU A 123 24.248 -17.507 40.836 1.00 23.77 O ANISOU 810 O LEU A 123 1874 2986 4168 851 197 -291 O ATOM 811 CB LEU A 123 23.313 -16.482 43.711 1.00 26.95 C ANISOU 811 CB LEU A 123 2832 3793 3615 -217 50 -247 C ATOM 812 CG LEU A 123 22.616 -15.540 44.706 1.00 31.32 C ANISOU 812 CG LEU A 123 3803 4174 3921 111 99 -534 C ATOM 813 CD1 LEU A 123 21.906 -16.330 45.795 1.00 34.04 C ANISOU 813 CD1 LEU A 123 4676 4231 4025 -243 -216 -163 C ATOM 814 CD2 LEU A 123 23.590 -14.540 45.324 1.00 34.10 C ANISOU 814 CD2 LEU A 123 4346 4442 4168 -234 -188 -313 C ATOM 815 N ASP A 124 26.077 -16.641 41.871 1.00 25.35 N ANISOU 815 N ASP A 124 2749 3375 3506 872 310 52 N ATOM 816 CA ASP A 124 27.079 -17.453 41.180 1.00 28.45 C ANISOU 816 CA ASP A 124 3232 3601 3974 1492 432 301 C ATOM 817 C ASP A 124 27.076 -17.314 39.644 1.00 29.95 C ANISOU 817 C ASP A 124 3381 3936 4060 1730 206 601 C ATOM 818 O ASP A 124 27.478 -18.243 38.936 1.00 34.49 O ANISOU 818 O ASP A 124 3845 4873 4383 2606 545 490 O ATOM 819 CB ASP A 124 26.968 -18.922 41.629 0.75 23.75 C ANISOU 819 CB ASP A 124 2905 3267 2850 2418 1174 -178 C ATOM 820 CG ASP A 124 27.192 -19.094 43.124 0.75 26.83 C ANISOU 820 CG ASP A 124 3604 3466 3122 1241 688 326 C ATOM 821 OD1 ASP A 124 27.979 -18.323 43.718 0.75 34.30 O ANISOU 821 OD1 ASP A 124 4275 4159 4595 923 238 -59 O ATOM 822 OD2 ASP A 124 26.580 -20.006 43.713 0.75 32.58 O ANISOU 822 OD2 ASP A 124 4313 3564 4499 814 667 655 O ATOM 823 N ARG A 125 26.660 -16.137 39.160 1.00 24.11 N ANISOU 823 N ARG A 125 2147 3254 3758 1030 290 220 N ATOM 824 C ARG A 125 27.545 -14.649 37.410 1.00 25.72 C ANISOU 824 C ARG A 125 2910 2979 3881 472 85 -32 C ATOM 825 O ARG A 125 27.634 -13.697 38.186 1.00 28.89 O ANISOU 825 O ARG A 125 3474 3222 4278 904 72 -378 O ATOM 826 CA AARG A 125 26.643 -15.847 37.728 0.50 23.47 C ANISOU 826 CA AARG A 125 2007 3269 3641 650 128 32 C ATOM 827 CB AARG A 125 25.205 -15.633 37.231 0.50 20.87 C ANISOU 827 CB AARG A 125 2022 2831 3076 370 85 119 C ATOM 828 CG AARG A 125 24.391 -16.922 37.244 0.50 20.94 C ANISOU 828 CG AARG A 125 1605 3384 2966 22 53 79 C ATOM 829 CD AARG A 125 22.927 -16.734 36.857 0.50 19.88 C ANISOU 829 CD AARG A 125 1523 3332 2696 -393 61 137 C ATOM 830 NE AARG A 125 22.733 -16.601 35.417 0.50 22.02 N ANISOU 830 NE AARG A 125 1933 3862 2572 -2190 502 544 N ATOM 831 CZ AARG A 125 21.642 -16.999 34.769 0.50 17.34 C ANISOU 831 CZ AARG A 125 1555 2969 2063 -819 318 249 C ATOM 832 NH1AARG A 125 20.651 -17.577 35.433 0.50 17.23 N ANISOU 832 NH1AARG A 125 930 3121 2495 -194 532 326 N ATOM 833 NH2AARG A 125 21.547 -16.838 33.456 0.50 18.74 N ANISOU 833 NH2AARG A 125 1247 3917 1955 -1832 114 26 N ATOM 834 CA BARG A 125 26.597 -15.803 37.733 0.50 24.17 C ANISOU 834 CA BARG A 125 2338 3183 3660 689 275 20 C ATOM 835 CB BARG A 125 25.191 -15.335 37.373 0.50 22.71 C ANISOU 835 CB BARG A 125 2486 2888 3252 697 165 98 C ATOM 836 CG BARG A 125 24.092 -16.336 37.647 0.50 26.53 C ANISOU 836 CG BARG A 125 3175 3036 3867 204 301 -122 C ATOM 837 CD BARG A 125 23.596 -16.953 36.358 0.50 29.21 C ANISOU 837 CD BARG A 125 3566 3641 3891 -33 270 -179 C ATOM 838 NE BARG A 125 22.208 -17.362 36.484 0.50 30.32 N ANISOU 838 NE BARG A 125 3909 3271 4338 -541 486 -91 N ATOM 839 CZ BARG A 125 21.334 -17.364 35.487 0.50 31.15 C ANISOU 839 CZ BARG A 125 3939 3269 4627 -512 374 -70 C ATOM 840 NH1BARG A 125 21.691 -16.970 34.271 0.50 30.30 N ANISOU 840 NH1BARG A 125 3825 3044 4644 -285 393 -56 N ATOM 841 NH2BARG A 125 20.093 -17.756 35.715 0.50 32.33 N ANISOU 841 NH2BARG A 125 4061 3513 4710 -769 317 -18 N ATOM 842 N ASN A 126 28.230 -14.741 36.266 1.00 26.11 N ANISOU 842 N ASN A 126 3136 2658 4126 220 411 263 N ATOM 843 CA ASN A 126 29.086 -13.681 35.693 1.00 24.84 C ANISOU 843 CA ASN A 126 3392 1694 4348 412 219 22 C ATOM 844 C ASN A 126 28.194 -12.494 35.360 1.00 23.52 C ANISOU 844 C ASN A 126 3044 1279 4613 -90 -65 154 C ATOM 845 O ASN A 126 27.097 -12.701 34.848 1.00 25.58 O ANISOU 845 O ASN A 126 2677 1993 5049 361 -6 279 O ATOM 846 CB ASN A 126 29.708 -14.241 34.404 1.00 23.79 C ANISOU 846 CB ASN A 126 2762 1272 5003 790 240 -194 C ATOM 847 CG ASN A 126 30.708 -13.311 33.751 1.00 26.42 C ANISOU 847 CG ASN A 126 2997 2430 4610 300 -5 37 C ATOM 848 OD1 ASN A 126 31.588 -12.752 34.414 1.00 31.87 O ANISOU 848 OD1 ASN A 126 3004 3408 5696 418 -891 -87 O ATOM 849 ND2 ASN A 126 30.606 -13.171 32.427 1.00 30.94 N ANISOU 849 ND2 ASN A 126 3675 3361 4719 146 -490 -154 N ATOM 850 N GLU A 127 28.638 -11.268 35.632 1.00 23.60 N ANISOU 850 N GLU A 127 2999 1698 4269 -405 -108 -159 N ATOM 851 CA GLU A 127 27.766 -10.097 35.451 1.00 24.92 C ANISOU 851 CA GLU A 127 2790 2301 4377 -126 -71 30 C ATOM 852 C GLU A 127 27.122 -10.016 34.057 1.00 23.07 C ANISOU 852 C GLU A 127 2548 2122 4092 -56 307 31 C ATOM 853 O GLU A 127 25.914 -9.780 33.949 1.00 23.40 O ANISOU 853 O GLU A 127 2395 2232 4263 -101 529 153 O ATOM 854 CB GLU A 127 28.470 -8.774 35.773 1.00 27.72 C ANISOU 854 CB GLU A 127 3908 2385 4238 -375 -277 -7 C ATOM 855 CG GLU A 127 27.495 -7.598 35.807 0.40 26.06 C ANISOU 855 CG GLU A 127 3978 2332 3592 -353 -172 -117 C ATOM 856 CD GLU A 127 28.147 -6.300 36.209 0.40 24.82 C ANISOU 856 CD GLU A 127 4032 1805 3590 149 -162 -144 C ATOM 857 OE1 GLU A 127 28.571 -6.188 37.375 0.40 25.26 O ANISOU 857 OE1 GLU A 127 4189 1963 3445 134 11 -87 O ATOM 858 OE2 GLU A 127 28.221 -5.389 35.362 0.40 26.73 O ANISOU 858 OE2 GLU A 127 3833 2316 4005 203 -230 325 O ATOM 859 N GLU A 128 27.910 -10.226 33.006 1.00 24.29 N ANISOU 859 N GLU A 128 2487 2085 4657 -173 740 50 N ATOM 860 CA GLU A 128 27.375 -10.241 31.625 1.00 26.31 C ANISOU 860 CA GLU A 128 2801 2567 4626 -43 721 78 C ATOM 861 C GLU A 128 26.286 -11.305 31.385 1.00 23.69 C ANISOU 861 C GLU A 128 2004 2867 4129 276 221 358 C ATOM 862 O GLU A 128 25.427 -11.133 30.515 1.00 23.87 O ANISOU 862 O GLU A 128 2253 3042 3772 320 330 640 O ATOM 863 CB GLU A 128 28.503 -10.436 30.597 1.00 30.27 C ANISOU 863 CB GLU A 128 3042 3493 4964 75 872 -274 C ATOM 864 CG GLU A 128 29.315 -9.183 30.299 0.50 32.24 C ANISOU 864 CG GLU A 128 3100 3406 5743 -11 569 -187 C ATOM 865 CD GLU A 128 30.196 -9.311 29.065 0.50 32.76 C ANISOU 865 CD GLU A 128 3223 2364 6858 -250 1384 4 C ATOM 866 OE1 GLU A 128 30.428 -10.439 28.575 0.50 34.93 O ANISOU 866 OE1 GLU A 128 2608 2958 7706 -385 1255 -917 O ATOM 867 OE2 GLU A 128 30.667 -8.267 28.576 0.50 39.19 O ANISOU 867 OE2 GLU A 128 3749 3317 7823 45 1616 1563 O ATOM 868 N ASP A 129 26.350 -12.395 32.153 1.00 21.05 N ANISOU 868 N ASP A 129 1821 2550 3625 -77 196 50 N ATOM 869 CA ASP A 129 25.466 -13.553 32.007 1.00 19.45 C ANISOU 869 CA ASP A 129 2238 1886 3266 309 163 -313 C ATOM 870 C ASP A 129 24.414 -13.695 33.096 1.00 20.44 C ANISOU 870 C ASP A 129 2554 2186 3024 339 253 -692 C ATOM 871 O ASP A 129 23.834 -14.773 33.275 1.00 19.14 O ANISOU 871 O ASP A 129 2149 2045 3077 640 27 -498 O ATOM 872 CB ASP A 129 26.351 -14.788 31.936 1.00 21.19 C ANISOU 872 CB ASP A 129 2175 2224 3650 531 34 -284 C ATOM 873 CG ASP A 129 27.321 -14.690 30.799 1.00 25.02 C ANISOU 873 CG ASP A 129 2540 2859 4104 187 401 -224 C ATOM 874 OD1 ASP A 129 26.839 -14.834 29.663 1.00 27.99 O ANISOU 874 OD1 ASP A 129 2914 3518 4201 2 318 -439 O ATOM 875 OD2 ASP A 129 28.527 -14.399 31.027 1.00 25.81 O ANISOU 875 OD2 ASP A 129 2450 2351 5004 444 143 -111 O ATOM 876 N ILE A 130 24.150 -12.592 33.794 1.00 20.16 N ANISOU 876 N ILE A 130 2572 1907 3178 347 235 -521 N ATOM 877 C ILE A 130 21.766 -12.806 34.031 1.00 20.67 C ANISOU 877 C ILE A 130 2387 2295 3169 146 222 -323 C ATOM 878 O ILE A 130 21.563 -12.338 32.912 1.00 19.92 O ANISOU 878 O ILE A 130 1990 2375 3201 -15 241 -359 O ATOM 879 CA ILE A 130 23.071 -12.505 34.767 0.75 19.88 C ANISOU 879 CA ILE A 130 2659 2027 2867 121 154 -438 C ATOM 880 CB ILE A 130 23.041 -11.093 35.418 0.75 23.88 C ANISOU 880 CB ILE A 130 3304 2623 3146 -183 52 -1148 C ATOM 881 CG1 ILE A 130 24.281 -10.890 36.294 0.75 27.74 C ANISOU 881 CG1 ILE A 130 3514 3398 3625 108 -336 -611 C ATOM 882 CG2 ILE A 130 21.773 -10.854 36.230 0.75 28.00 C ANISOU 882 CG2 ILE A 130 3543 3970 3125 -162 257 -804 C ATOM 883 CD1 ILE A 130 24.256 -11.594 37.623 0.75 31.46 C ANISOU 883 CD1 ILE A 130 4121 3912 3919 -132 305 -336 C ATOM 884 N GLY A 131 20.908 -13.622 34.636 1.00 20.06 N ANISOU 884 N GLY A 131 2263 2388 2969 316 -51 114 N ATOM 885 CA GLY A 131 19.588 -13.874 34.079 1.00 18.87 C ANISOU 885 CA GLY A 131 2010 2351 2807 410 284 -96 C ATOM 886 C GLY A 131 18.685 -12.655 34.223 1.00 18.03 C ANISOU 886 C GLY A 131 2200 2108 2539 345 142 -97 C ATOM 887 O GLY A 131 18.870 -11.824 35.123 1.00 17.51 O ANISOU 887 O GLY A 131 2328 1688 2634 334 82 -1 O ATOM 888 N ALA A 132 17.704 -12.537 33.333 1.00 17.40 N ANISOU 888 N ALA A 132 2083 2138 2387 289 241 -60 N ATOM 889 CA ALA A 132 16.634 -11.548 33.517 1.00 16.70 C ANISOU 889 CA ALA A 132 1938 1930 2477 158 -1 -37 C ATOM 890 C ALA A 132 16.013 -11.749 34.896 1.00 16.22 C ANISOU 890 C ALA A 132 1917 1709 2535 132 87 -317 C ATOM 891 O ALA A 132 15.818 -12.895 35.336 1.00 16.92 O ANISOU 891 O ALA A 132 1721 1750 2956 325 8 -25 O ATOM 892 CB ALA A 132 15.579 -11.699 32.438 1.00 17.09 C ANISOU 892 CB ALA A 132 1951 2132 2409 83 -3 65 C ATOM 893 N GLY A 133 15.701 -10.646 35.576 1.00 14.95 N ANISOU 893 N GLY A 133 1586 1467 2624 23 -126 -257 N ATOM 894 CA GLY A 133 15.139 -10.716 36.929 1.00 15.55 C ANISOU 894 CA GLY A 133 1426 1808 2673 -28 -111 -234 C ATOM 895 C GLY A 133 13.693 -11.182 36.989 1.00 14.15 C ANISOU 895 C GLY A 133 1413 1560 2400 15 -159 -212 C ATOM 896 O GLY A 133 13.165 -11.424 38.071 1.00 14.58 O ANISOU 896 O GLY A 133 1197 1741 2601 277 -42 -113 O ATOM 897 N ASP A 134 13.051 -11.295 35.832 1.00 13.91 N ANISOU 897 N ASP A 134 1654 1559 2070 -20 13 -61 N ATOM 898 CA ASP A 134 11.658 -11.732 35.734 1.00 14.92 C ANISOU 898 CA ASP A 134 1655 1586 2425 -35 77 -154 C ATOM 899 C ASP A 134 11.391 -12.080 34.275 1.00 14.98 C ANISOU 899 C ASP A 134 1699 1555 2437 -78 99 -92 C ATOM 900 O ASP A 134 12.187 -11.737 33.398 1.00 16.58 O ANISOU 900 O ASP A 134 1807 1555 2935 -133 334 71 O ATOM 901 CB ASP A 134 10.736 -10.577 36.169 1.00 14.80 C ANISOU 901 CB ASP A 134 1617 1770 2236 84 53 -115 C ATOM 902 CG ASP A 134 9.299 -11.020 36.486 1.00 17.30 C ANISOU 902 CG ASP A 134 1707 2075 2790 -36 178 -183 C ATOM 903 OD1 ASP A 134 8.939 -12.218 36.353 1.00 16.81 O ANISOU 903 OD1 ASP A 134 1690 1880 2816 188 83 -25 O ATOM 904 OD2 ASP A 134 8.518 -10.144 36.916 1.00 19.32 O ANISOU 904 OD2 ASP A 134 2417 1576 3346 25 380 -91 O ATOM 905 N GLN A 135 10.274 -12.756 34.008 1.00 14.97 N ANISOU 905 N GLN A 135 1710 1459 2517 -107 103 18 N ATOM 906 CA GLN A 135 9.738 -12.794 32.655 1.00 14.70 C ANISOU 906 CA GLN A 135 1665 1378 2542 -73 43 39 C ATOM 907 C GLN A 135 9.095 -11.444 32.336 1.00 15.10 C ANISOU 907 C GLN A 135 1679 1452 2606 18 80 54 C ATOM 908 O GLN A 135 8.850 -10.635 33.235 1.00 16.22 O ANISOU 908 O GLN A 135 1987 1303 2869 13 4 -40 O ATOM 909 CB GLN A 135 8.703 -13.915 32.482 1.00 14.66 C ANISOU 909 CB GLN A 135 1806 1541 2220 -185 -34 -26 C ATOM 910 CG GLN A 135 7.407 -13.734 33.257 1.00 15.53 C ANISOU 910 CG GLN A 135 1830 1688 2383 -150 34 10 C ATOM 911 CD GLN A 135 6.322 -14.692 32.794 1.00 16.08 C ANISOU 911 CD GLN A 135 1565 1857 2685 -62 -56 0 C ATOM 912 OE1 GLN A 135 6.508 -15.906 32.825 1.00 16.10 O ANISOU 912 OE1 GLN A 135 1083 1918 3116 130 -63 51 O ATOM 913 NE2 GLN A 135 5.182 -14.150 32.364 1.00 16.62 N ANISOU 913 NE2 GLN A 135 1513 1929 2873 120 222 120 N ATOM 914 N GLY A 136 8.812 -11.225 31.057 1.00 14.08 N ANISOU 914 N GLY A 136 1604 1101 2643 246 144 173 N ATOM 915 CA GLY A 136 7.987 -10.102 30.623 1.00 15.35 C ANISOU 915 CA GLY A 136 1971 1239 2621 402 50 218 C ATOM 916 C GLY A 136 8.250 -9.659 29.197 1.00 16.15 C ANISOU 916 C GLY A 136 2131 1424 2578 196 168 63 C ATOM 917 O GLY A 136 9.186 -10.128 28.547 1.00 16.93 O ANISOU 917 O GLY A 136 2262 1698 2471 74 394 129 O ATOM 918 N LEU A 137 7.418 -8.730 28.736 1.00 14.49 N ANISOU 918 N LEU A 137 1396 1825 2284 -10 -38 2 N ATOM 919 CA LEU A 137 7.575 -8.100 27.428 1.00 15.69 C ANISOU 919 CA LEU A 137 1913 1792 2256 23 47 -64 C ATOM 920 C LEU A 137 7.732 -6.600 27.608 1.00 15.16 C ANISOU 920 C LEU A 137 1754 1820 2183 83 155 -239 C ATOM 921 O LEU A 137 7.271 -6.049 28.600 1.00 15.33 O ANISOU 921 O LEU A 137 1946 1582 2295 1 304 -236 O ATOM 922 CB LEU A 137 6.393 -8.412 26.511 1.00 16.36 C ANISOU 922 CB LEU A 137 1942 2030 2241 47 10 -23 C ATOM 923 CG LEU A 137 4.985 -8.247 27.096 1.00 17.50 C ANISOU 923 CG LEU A 137 2079 2135 2435 28 191 -57 C ATOM 924 CD1 LEU A 137 4.012 -7.718 26.049 1.00 17.42 C ANISOU 924 CD1 LEU A 137 2233 1998 2385 -59 62 -139 C ATOM 925 CD2 LEU A 137 4.488 -9.558 27.684 1.00 18.53 C ANISOU 925 CD2 LEU A 137 2390 2112 2537 53 205 17 C ATOM 926 N MET A 138 8.421 -5.963 26.658 1.00 14.64 N ANISOU 926 N MET A 138 1540 1648 2372 87 128 -204 N ATOM 927 CA MET A 138 8.718 -4.530 26.706 1.00 14.66 C ANISOU 927 CA MET A 138 1529 1612 2428 163 30 -149 C ATOM 928 C MET A 138 8.716 -3.964 25.290 1.00 14.44 C ANISOU 928 C MET A 138 1565 1573 2346 137 238 -282 C ATOM 929 O MET A 138 9.054 -4.666 24.344 1.00 14.41 O ANISOU 929 O MET A 138 1843 998 2633 448 199 -230 O ATOM 930 CB MET A 138 10.095 -4.267 27.327 1.00 15.66 C ANISOU 930 CB MET A 138 1781 1747 2419 110 -222 -244 C ATOM 931 CG MET A 138 10.302 -4.838 28.724 1.00 16.66 C ANISOU 931 CG MET A 138 2128 1694 2505 65 -117 -166 C ATOM 932 SD MET A 138 10.870 -6.551 28.699 1.00 17.40 S ANISOU 932 SD MET A 138 1885 1808 2917 205 -31 -72 S ATOM 933 CE MET A 138 10.485 -7.101 30.354 1.00 17.55 C ANISOU 933 CE MET A 138 2000 1993 2675 177 -125 -215 C ATOM 934 N PHE A 139 8.343 -2.694 25.157 1.00 14.40 N ANISOU 934 N PHE A 139 1429 1485 2557 -55 330 -130 N ATOM 935 CA PHE A 139 8.378 -2.002 23.870 1.00 15.42 C ANISOU 935 CA PHE A 139 1403 1820 2634 -161 376 34 C ATOM 936 C PHE A 139 9.155 -0.699 23.959 1.00 16.57 C ANISOU 936 C PHE A 139 1591 1835 2867 -264 653 255 C ATOM 937 O PHE A 139 9.072 0.018 24.964 1.00 15.37 O ANISOU 937 O PHE A 139 1056 1679 3101 -100 236 195 O ATOM 938 CB PHE A 139 6.988 -1.630 23.400 1.00 14.67 C ANISOU 938 CB PHE A 139 1544 1662 2368 -226 222 81 C ATOM 939 CG PHE A 139 6.101 -2.793 23.103 1.00 13.85 C ANISOU 939 CG PHE A 139 1402 1506 2353 -75 290 3 C ATOM 940 CD1 PHE A 139 5.274 -3.311 24.093 1.00 14.54 C ANISOU 940 CD1 PHE A 139 1774 1550 2199 -5 354 64 C ATOM 941 CD2 PHE A 139 6.027 -3.321 21.819 1.00 14.45 C ANISOU 941 CD2 PHE A 139 1462 1646 2378 -126 210 -44 C ATOM 942 CE1 PHE A 139 4.408 -4.364 23.814 1.00 15.70 C ANISOU 942 CE1 PHE A 139 2034 1535 2395 -47 309 -131 C ATOM 943 CE2 PHE A 139 5.160 -4.372 21.533 1.00 14.42 C ANISOU 943 CE2 PHE A 139 1971 1403 2104 -135 190 -137 C ATOM 944 CZ PHE A 139 4.357 -4.896 22.531 1.00 15.61 C ANISOU 944 CZ PHE A 139 1767 1884 2277 -92 276 -68 C ATOM 945 N GLY A 140 9.884 -0.405 22.889 1.00 15.01 N ANISOU 945 N GLY A 140 1550 1615 2535 -88 574 -58 N ATOM 946 CA GLY A 140 10.441 0.916 22.634 1.00 15.04 C ANISOU 946 CA GLY A 140 1867 1559 2288 -65 495 35 C ATOM 947 C GLY A 140 9.798 1.527 21.406 1.00 14.47 C ANISOU 947 C GLY A 140 1381 1626 2488 -168 408 66 C ATOM 948 O GLY A 140 9.381 0.815 20.486 1.00 15.57 O ANISOU 948 O GLY A 140 1639 1681 2595 -95 348 -24 O ATOM 949 N TYR A 141 9.757 2.854 21.374 1.00 14.24 N ANISOU 949 N TYR A 141 1382 1619 2410 -110 197 -119 N ATOM 950 CA TYR A 141 9.113 3.590 20.295 1.00 14.05 C ANISOU 950 CA TYR A 141 1692 1384 2262 -347 273 13 C ATOM 951 C TYR A 141 9.863 4.887 20.010 1.00 14.39 C ANISOU 951 C TYR A 141 2082 1174 2212 -285 252 5 C ATOM 952 O TYR A 141 10.439 5.495 20.921 1.00 15.97 O ANISOU 952 O TYR A 141 2255 1410 2399 -245 68 -84 O ATOM 953 CB TYR A 141 7.665 3.883 20.685 1.00 14.19 C ANISOU 953 CB TYR A 141 1677 1217 2496 -244 158 -72 C ATOM 954 CG TYR A 141 6.867 4.669 19.672 1.00 16.27 C ANISOU 954 CG TYR A 141 1795 1727 2659 -196 -25 40 C ATOM 955 CD1 TYR A 141 6.310 4.045 18.557 1.00 18.61 C ANISOU 955 CD1 TYR A 141 2286 2093 2690 -215 -205 30 C ATOM 956 CD2 TYR A 141 6.647 6.040 19.838 1.00 16.73 C ANISOU 956 CD2 TYR A 141 1999 1764 2593 -116 -221 -48 C ATOM 957 CE1 TYR A 141 5.557 4.758 17.637 1.00 19.43 C ANISOU 957 CE1 TYR A 141 2390 2350 2642 -160 -271 51 C ATOM 958 CE2 TYR A 141 5.903 6.758 18.919 1.00 16.79 C ANISOU 958 CE2 TYR A 141 1932 2043 2404 8 -94 -39 C ATOM 959 CZ TYR A 141 5.358 6.112 17.825 1.00 17.65 C ANISOU 959 CZ TYR A 141 1995 2360 2348 -59 -293 100 C ATOM 960 OH TYR A 141 4.621 6.818 16.918 1.00 17.73 O ANISOU 960 OH TYR A 141 1542 2614 2579 -159 -381 145 O ATOM 961 N ALA A 142 9.863 5.297 18.747 1.00 14.20 N ANISOU 961 N ALA A 142 2063 1275 2056 -82 275 -156 N ATOM 962 CA ALA A 142 10.397 6.602 18.355 1.00 15.53 C ANISOU 962 CA ALA A 142 2204 1273 2421 -110 310 -173 C ATOM 963 C ALA A 142 9.648 7.135 17.136 1.00 16.42 C ANISOU 963 C ALA A 142 2165 1339 2735 187 296 -91 C ATOM 964 O ALA A 142 9.177 6.362 16.296 1.00 17.43 O ANISOU 964 O ALA A 142 1938 1729 2952 492 317 -475 O ATOM 965 CB ALA A 142 11.892 6.506 18.071 1.00 17.05 C ANISOU 965 CB ALA A 142 2177 2005 2295 -171 188 -88 C ATOM 966 N THR A 143 9.530 8.457 17.060 1.00 16.17 N ANISOU 966 N THR A 143 2141 1345 2655 113 159 68 N ATOM 967 CA THR A 143 8.842 9.124 15.958 1.00 15.35 C ANISOU 967 CA THR A 143 2002 1493 2334 -58 213 15 C ATOM 968 C THR A 143 9.590 10.397 15.588 1.00 15.32 C ANISOU 968 C THR A 143 1839 1472 2510 101 287 194 C ATOM 969 O THR A 143 9.978 11.144 16.462 1.00 17.03 O ANISOU 969 O THR A 143 2047 1495 2926 41 80 121 O ATOM 970 CB THR A 143 7.385 9.483 16.324 1.00 15.84 C ANISOU 970 CB THR A 143 2059 1634 2323 60 200 -27 C ATOM 971 OG1 THR A 143 6.871 10.438 15.390 1.00 16.96 O ANISOU 971 OG1 THR A 143 2079 1706 2655 -103 106 207 O ATOM 972 CG2 THR A 143 7.277 10.058 17.728 1.00 16.49 C ANISOU 972 CG2 THR A 143 2188 1821 2254 11 174 26 C ATOM 973 N ASP A 144 9.731 10.663 14.293 1.00 15.24 N ANISOU 973 N ASP A 144 1862 1415 2513 0 259 208 N ATOM 974 CA ASP A 144 10.477 11.841 13.814 1.00 16.77 C ANISOU 974 CA ASP A 144 1742 1744 2883 -143 316 352 C ATOM 975 C ASP A 144 9.687 13.157 13.887 1.00 16.80 C ANISOU 975 C ASP A 144 1875 1588 2917 -225 467 316 C ATOM 976 O ASP A 144 10.166 14.187 13.436 1.00 17.42 O ANISOU 976 O ASP A 144 1660 1722 3235 -46 664 593 O ATOM 977 CB ASP A 144 10.995 11.619 12.383 1.00 19.43 C ANISOU 977 CB ASP A 144 2081 2268 3030 -22 513 234 C ATOM 978 CG ASP A 144 9.893 11.593 11.337 1.00 20.80 C ANISOU 978 CG ASP A 144 2146 2214 3539 -216 353 491 C ATOM 979 OD1 ASP A 144 8.699 11.471 11.695 1.00 21.68 O ANISOU 979 OD1 ASP A 144 1786 2407 4042 -154 -57 463 O ATOM 980 OD2 ASP A 144 10.232 11.674 10.135 1.00 22.07 O ANISOU 980 OD2 ASP A 144 2296 2210 3879 -420 894 428 O ATOM 981 N GLU A 145 8.477 13.116 14.432 1.00 17.84 N ANISOU 981 N GLU A 145 1805 2027 2947 239 425 139 N ATOM 982 CA GLU A 145 7.619 14.299 14.504 1.00 16.74 C ANISOU 982 CA GLU A 145 1926 1721 2712 90 104 50 C ATOM 983 C GLU A 145 8.131 15.412 15.431 1.00 17.34 C ANISOU 983 C GLU A 145 2111 1416 3062 307 -89 7 C ATOM 984 O GLU A 145 7.668 16.542 15.315 1.00 16.79 O ANISOU 984 O GLU A 145 1741 1405 3230 232 31 102 O ATOM 985 CB GLU A 145 6.197 13.900 14.911 1.00 18.26 C ANISOU 985 CB GLU A 145 1995 2062 2878 62 255 9 C ATOM 986 CG GLU A 145 6.022 13.597 16.385 1.00 18.60 C ANISOU 986 CG GLU A 145 2141 2112 2812 219 119 -53 C ATOM 987 CD GLU A 145 4.729 12.864 16.660 1.00 19.22 C ANISOU 987 CD GLU A 145 2283 1972 3044 108 42 -88 C ATOM 988 OE1 GLU A 145 4.656 11.661 16.323 1.00 18.31 O ANISOU 988 OE1 GLU A 145 2210 1790 2955 312 -326 184 O ATOM 989 OE2 GLU A 145 3.797 13.497 17.220 1.00 19.54 O ANISOU 989 OE2 GLU A 145 2503 1896 3022 340 -98 -126 O ATOM 990 N THR A 146 9.050 15.088 16.349 1.00 18.80 N ANISOU 990 N THR A 146 2245 2024 2875 109 -104 163 N ATOM 991 CA THR A 146 9.759 16.086 17.166 1.00 17.42 C ANISOU 991 CA THR A 146 1869 1627 3120 10 53 335 C ATOM 992 C THR A 146 11.249 15.778 17.165 1.00 16.86 C ANISOU 992 C THR A 146 1888 1373 3145 22 0 237 C ATOM 993 O THR A 146 11.645 14.645 16.882 1.00 15.42 O ANISOU 993 O THR A 146 1554 1102 3202 -228 -95 368 O ATOM 994 CB THR A 146 9.277 16.101 18.637 1.00 19.80 C ANISOU 994 CB THR A 146 2236 2241 3045 -76 -10 314 C ATOM 995 OG1 THR A 146 9.435 14.801 19.221 1.00 19.72 O ANISOU 995 OG1 THR A 146 2143 2289 3061 -136 346 423 O ATOM 996 CG2 THR A 146 7.823 16.521 18.731 1.00 19.50 C ANISOU 996 CG2 THR A 146 2337 2401 2672 38 104 22 C ATOM 997 N GLU A 147 12.072 16.771 17.500 1.00 19.56 N ANISOU 997 N GLU A 147 2113 1789 3528 -428 75 401 N ATOM 998 CA GLU A 147 13.537 16.569 17.570 1.00 21.04 C ANISOU 998 CA GLU A 147 2129 2259 3603 -332 -15 439 C ATOM 999 C GLU A 147 13.947 15.513 18.603 1.00 22.76 C ANISOU 999 C GLU A 147 2598 1991 4056 -374 52 580 C ATOM 1000 O GLU A 147 14.881 14.735 18.370 1.00 25.37 O ANISOU 1000 O GLU A 147 3029 2281 4329 67 -52 624 O ATOM 1001 CB GLU A 147 14.270 17.890 17.861 1.00 24.18 C ANISOU 1001 CB GLU A 147 3066 2206 3915 -453 -74 301 C ATOM 1002 CG GLU A 147 15.783 17.852 17.611 1.00 26.65 C ANISOU 1002 CG GLU A 147 2961 2956 4208 -263 -377 316 C ATOM 1003 CD GLU A 147 16.571 17.113 18.682 0.75 27.04 C ANISOU 1003 CD GLU A 147 3038 2993 4243 -430 -447 362 C ATOM 1004 OE1 GLU A 147 16.250 17.266 19.880 0.75 27.64 O ANISOU 1004 OE1 GLU A 147 2878 3054 4569 -1165 -165 -368 O ATOM 1005 OE2 GLU A 147 17.504 16.355 18.326 0.75 25.79 O ANISOU 1005 OE2 GLU A 147 2603 3023 4171 -600 -509 369 O ATOM 1006 N GLU A 148 13.248 15.493 19.737 1.00 22.87 N ANISOU 1006 N GLU A 148 2975 1855 3860 -196 21 380 N ATOM 1007 CA GLU A 148 13.481 14.497 20.795 1.00 23.00 C ANISOU 1007 CA GLU A 148 2910 2009 3817 -399 -104 424 C ATOM 1008 C GLU A 148 12.905 13.106 20.474 1.00 21.16 C ANISOU 1008 C GLU A 148 2701 1917 3421 -256 -51 451 C ATOM 1009 O GLU A 148 13.006 12.199 21.291 1.00 22.80 O ANISOU 1009 O GLU A 148 2839 1588 4236 -476 222 660 O ATOM 1010 CB GLU A 148 12.952 14.995 22.150 1.00 25.95 C ANISOU 1010 CB GLU A 148 3137 2799 3921 -185 46 363 C ATOM 1011 CG GLU A 148 11.476 15.391 22.193 1.00 28.49 C ANISOU 1011 CG GLU A 148 3081 3440 4303 -213 17 209 C ATOM 1012 CD GLU A 148 11.250 16.899 22.093 1.00 32.78 C ANISOU 1012 CD GLU A 148 4137 3467 4849 -295 419 445 C ATOM 1013 OE1 GLU A 148 11.544 17.499 21.025 1.00 29.26 O ANISOU 1013 OE1 GLU A 148 4401 2299 4415 -13 -128 167 O ATOM 1014 OE2 GLU A 148 10.769 17.490 23.084 1.00 39.65 O ANISOU 1014 OE2 GLU A 148 4231 4868 5967 -422 1033 -470 O ATOM 1015 N CYS A 149 12.302 12.957 19.293 1.00 18.06 N ANISOU 1015 N CYS A 149 2333 1326 3202 72 -2 1040 N ATOM 1016 CA CYS A 149 11.794 11.691 18.778 1.00 18.21 C ANISOU 1016 CA CYS A 149 1923 2006 2988 39 67 338 C ATOM 1017 C CYS A 149 10.635 11.135 19.607 1.00 17.51 C ANISOU 1017 C CYS A 149 1803 1708 3143 157 156 217 C ATOM 1018 O CYS A 149 10.498 9.922 19.739 1.00 15.70 O ANISOU 1018 O CYS A 149 1153 1724 3089 301 175 429 O ATOM 1019 CB CYS A 149 12.916 10.647 18.576 1.00 21.51 C ANISOU 1019 CB CYS A 149 2022 2544 3607 360 -63 413 C ATOM 1020 SG CYS A 149 13.997 11.025 17.182 1.00 25.72 S ANISOU 1020 SG CYS A 149 2459 3393 3920 631 494 51 S ATOM 1021 N MET A 150 9.787 12.033 20.119 1.00 18.25 N ANISOU 1021 N MET A 150 2127 1906 2900 42 391 -109 N ATOM 1022 CA MET A 150 8.620 11.669 20.931 1.00 16.42 C ANISOU 1022 CA MET A 150 1783 1889 2563 101 12 27 C ATOM 1023 C MET A 150 7.344 12.232 20.336 1.00 16.00 C ANISOU 1023 C MET A 150 1780 1884 2414 219 195 19 C ATOM 1024 O MET A 150 7.388 13.215 19.571 1.00 17.48 O ANISOU 1024 O MET A 150 1994 1912 2736 -19 227 164 O ATOM 1025 CB MET A 150 8.754 12.208 22.353 1.00 17.63 C ANISOU 1025 CB MET A 150 2058 2024 2617 155 39 -44 C ATOM 1026 CG MET A 150 9.860 11.570 23.177 1.00 18.51 C ANISOU 1026 CG MET A 150 2285 2080 2665 67 -167 10 C ATOM 1027 SD MET A 150 9.467 9.868 23.620 1.00 20.90 S ANISOU 1027 SD MET A 150 2391 2173 3377 4 -88 258 S ATOM 1028 CE MET A 150 8.234 10.141 24.885 1.00 23.01 C ANISOU 1028 CE MET A 150 2962 2464 3315 -261 180 168 C ATOM 1029 N PRO A 151 6.192 11.626 20.694 1.00 16.64 N ANISOU 1029 N PRO A 151 1794 2166 2363 88 117 130 N ATOM 1030 CA PRO A 151 4.915 12.173 20.227 1.00 16.61 C ANISOU 1030 CA PRO A 151 2052 1909 2349 221 35 126 C ATOM 1031 C PRO A 151 4.641 13.580 20.763 1.00 16.08 C ANISOU 1031 C PRO A 151 2038 1733 2337 -73 32 142 C ATOM 1032 O PRO A 151 4.791 13.816 21.960 1.00 15.85 O ANISOU 1032 O PRO A 151 2002 1629 2391 -228 66 28 O ATOM 1033 CB PRO A 151 3.872 11.187 20.770 1.00 18.35 C ANISOU 1033 CB PRO A 151 2509 2038 2422 -121 -3 92 C ATOM 1034 CG PRO A 151 4.616 9.949 21.105 1.00 17.95 C ANISOU 1034 CG PRO A 151 2094 2300 2423 20 -16 -15 C ATOM 1035 CD PRO A 151 6.016 10.368 21.441 1.00 16.98 C ANISOU 1035 CD PRO A 151 1967 2143 2341 187 47 90 C ATOM 1036 N LEU A 152 4.219 14.491 19.886 1.00 14.58 N ANISOU 1036 N LEU A 152 2103 1218 2219 -110 98 -118 N ATOM 1037 CA LEU A 152 3.906 15.871 20.294 1.00 14.98 C ANISOU 1037 CA LEU A 152 1990 1221 2479 -73 76 -113 C ATOM 1038 C LEU A 152 2.852 15.929 21.401 1.00 14.61 C ANISOU 1038 C LEU A 152 1759 1283 2508 -216 3 -123 C ATOM 1039 O LEU A 152 2.944 16.765 22.304 1.00 14.70 O ANISOU 1039 O LEU A 152 1689 1274 2619 -157 58 -186 O ATOM 1040 CB LEU A 152 3.450 16.715 19.093 1.00 16.66 C ANISOU 1040 CB LEU A 152 2087 1630 2611 8 -4 42 C ATOM 1041 CG LEU A 152 3.183 18.201 19.373 1.00 17.32 C ANISOU 1041 CG LEU A 152 2379 1709 2491 55 45 -60 C ATOM 1042 CD1 LEU A 152 4.465 18.908 19.764 1.00 18.08 C ANISOU 1042 CD1 LEU A 152 2421 1980 2467 -4 0 -43 C ATOM 1043 CD2 LEU A 152 2.553 18.870 18.169 1.00 19.07 C ANISOU 1043 CD2 LEU A 152 2710 2136 2398 -122 -13 71 C ATOM 1044 N THR A 153 1.867 15.036 21.334 1.00 15.57 N ANISOU 1044 N THR A 153 1826 1630 2458 -428 89 -44 N ATOM 1045 CA THR A 153 0.782 15.022 22.311 1.00 15.94 C ANISOU 1045 CA THR A 153 1633 1767 2657 -260 42 -49 C ATOM 1046 C THR A 153 1.323 14.929 23.741 1.00 15.40 C ANISOU 1046 C THR A 153 1649 1481 2719 -248 -61 -73 C ATOM 1047 O THR A 153 0.937 15.733 24.598 1.00 16.46 O ANISOU 1047 O THR A 153 1667 1834 2750 61 207 7 O ATOM 1048 CB THR A 153 -0.205 13.856 22.067 1.00 15.93 C ANISOU 1048 CB THR A 153 1662 1635 2756 -189 -58 -45 C ATOM 1049 OG1 THR A 153 0.515 12.618 21.963 1.00 17.00 O ANISOU 1049 OG1 THR A 153 1819 1785 2854 -54 111 -236 O ATOM 1050 CG2 THR A 153 -1.001 14.082 20.798 1.00 18.09 C ANISOU 1050 CG2 THR A 153 2359 2075 2436 -159 -4 -52 C ATOM 1051 N ILE A 154 2.227 13.977 23.986 1.00 15.30 N ANISOU 1051 N ILE A 154 1519 1329 2965 -284 50 -189 N ATOM 1052 CA ILE A 154 2.773 13.788 25.341 1.00 18.82 C ANISOU 1052 CA ILE A 154 1811 2123 3216 -249 -236 -251 C ATOM 1053 C ILE A 154 3.838 14.820 25.714 1.00 16.82 C ANISOU 1053 C ILE A 154 1679 1530 3179 76 -238 -99 C ATOM 1054 O ILE A 154 3.904 15.222 26.881 1.00 16.94 O ANISOU 1054 O ILE A 154 1364 1846 3224 -63 -250 -202 O ATOM 1055 CB ILE A 154 3.278 12.339 25.624 1.00 25.67 C ANISOU 1055 CB ILE A 154 1287 1807 6658 -688 -1395 -811 C ATOM 1056 CG1 ILE A 154 3.452 12.144 27.137 1.00 33.91 C ANISOU 1056 CG1 ILE A 154 2425 4130 6329 -1365 -1123 -516 C ATOM 1057 CG2 ILE A 154 4.573 12.017 24.884 1.00 23.92 C ANISOU 1057 CG2 ILE A 154 2901 2294 3893 -367 -762 -198 C ATOM 1058 CD1 ILE A 154 3.465 10.709 27.595 1.00 32.31 C ANISOU 1058 CD1 ILE A 154 3654 4498 4124 -821 -869 -502 C ATOM 1059 N VAL A 155 4.652 15.250 24.740 1.00 16.33 N ANISOU 1059 N VAL A 155 1890 1560 2754 81 -307 -95 N ATOM 1060 CA VAL A 155 5.650 16.312 24.970 1.00 15.70 C ANISOU 1060 CA VAL A 155 1844 1398 2721 108 -125 162 C ATOM 1061 C VAL A 155 4.947 17.567 25.500 1.00 16.55 C ANISOU 1061 C VAL A 155 1983 1663 2640 233 -76 66 C ATOM 1062 O VAL A 155 5.343 18.116 26.526 1.00 17.98 O ANISOU 1062 O VAL A 155 2280 1606 2943 -24 -57 -103 O ATOM 1063 CB VAL A 155 6.475 16.633 23.698 1.00 16.31 C ANISOU 1063 CB VAL A 155 1952 1529 2712 76 -92 137 C ATOM 1064 CG1 VAL A 155 7.350 17.880 23.896 1.00 16.56 C ANISOU 1064 CG1 VAL A 155 2150 1491 2648 49 -12 128 C ATOM 1065 CG2 VAL A 155 7.358 15.449 23.328 1.00 16.57 C ANISOU 1065 CG2 VAL A 155 1922 1705 2666 70 105 79 C ATOM 1066 N LEU A 156 3.889 17.992 24.816 1.00 16.52 N ANISOU 1066 N LEU A 156 1880 1923 2473 149 -77 25 N ATOM 1067 CA LEU A 156 3.113 19.155 25.260 1.00 17.19 C ANISOU 1067 CA LEU A 156 2037 1839 2655 109 -62 25 C ATOM 1068 C LEU A 156 2.458 18.942 26.623 1.00 17.48 C ANISOU 1068 C LEU A 156 1895 1991 2754 -13 -77 247 C ATOM 1069 O LEU A 156 2.494 19.840 27.462 1.00 17.48 O ANISOU 1069 O LEU A 156 2191 1587 2863 -207 83 434 O ATOM 1070 CB LEU A 156 2.073 19.556 24.217 1.00 16.91 C ANISOU 1070 CB LEU A 156 1875 1761 2788 144 -6 117 C ATOM 1071 CG LEU A 156 2.611 20.086 22.885 1.00 19.22 C ANISOU 1071 CG LEU A 156 2431 2079 2790 69 160 72 C ATOM 1072 CD1 LEU A 156 1.456 20.356 21.934 1.00 20.34 C ANISOU 1072 CD1 LEU A 156 2704 2182 2839 172 63 312 C ATOM 1073 CD2 LEU A 156 3.454 21.340 23.061 1.00 20.23 C ANISOU 1073 CD2 LEU A 156 2440 2228 3017 -50 254 164 C ATOM 1074 N ALA A 157 1.887 17.759 26.849 1.00 17.83 N ANISOU 1074 N ALA A 157 2165 2047 2561 -166 -133 157 N ATOM 1075 CA ALA A 157 1.256 17.438 28.139 1.00 17.57 C ANISOU 1075 CA ALA A 157 2272 1776 2628 -38 50 12 C ATOM 1076 C ALA A 157 2.254 17.543 29.299 1.00 17.19 C ANISOU 1076 C ALA A 157 2252 1636 2644 -1 53 13 C ATOM 1077 O ALA A 157 1.944 18.146 30.327 1.00 16.11 O ANISOU 1077 O ALA A 157 1760 1505 2854 393 170 118 O ATOM 1078 CB ALA A 157 0.620 16.052 28.103 1.00 17.13 C ANISOU 1078 CB ALA A 157 2196 1866 2444 -129 96 -4 C ATOM 1079 N HIS A 158 3.448 16.970 29.124 1.00 16.40 N ANISOU 1079 N HIS A 158 2254 1484 2490 -87 232 39 N ATOM 1080 CA HIS A 158 4.514 17.077 30.123 1.00 16.71 C ANISOU 1080 CA HIS A 158 2411 1461 2477 -415 192 -97 C ATOM 1081 C HIS A 158 4.868 18.543 30.374 1.00 16.44 C ANISOU 1081 C HIS A 158 2201 1289 2756 -82 192 -49 C ATOM 1082 O HIS A 158 4.974 18.976 31.525 1.00 16.41 O ANISOU 1082 O HIS A 158 2373 1099 2763 231 209 -1 O ATOM 1083 CB HIS A 158 5.801 16.355 29.678 1.00 17.13 C ANISOU 1083 CB HIS A 158 2594 1388 2527 -271 88 -83 C ATOM 1084 CG HIS A 158 5.729 14.858 29.699 1.00 16.89 C ANISOU 1084 CG HIS A 158 2526 1376 2512 -248 -13 -133 C ATOM 1085 ND1 HIS A 158 5.067 14.146 30.676 1.00 17.54 N ANISOU 1085 ND1 HIS A 158 2522 1300 2841 -294 179 -180 N ATOM 1086 CD2 HIS A 158 6.306 13.935 28.892 1.00 15.78 C ANISOU 1086 CD2 HIS A 158 2502 1030 2463 -516 70 -30 C ATOM 1087 CE1 HIS A 158 5.206 12.852 30.447 1.00 16.95 C ANISOU 1087 CE1 HIS A 158 2571 1367 2502 -160 35 -265 C ATOM 1088 NE2 HIS A 158 5.962 12.697 29.376 1.00 15.21 N ANISOU 1088 NE2 HIS A 158 2339 1027 2411 -386 -6 68 N ATOM 1089 N LYS A 159 5.070 19.294 29.294 1.00 16.65 N ANISOU 1089 N LYS A 159 2043 1775 2508 -129 -35 -21 N ATOM 1090 CA LYS A 159 5.523 20.692 29.407 1.00 17.24 C ANISOU 1090 CA LYS A 159 2051 1823 2675 -116 99 -219 C ATOM 1091 C LYS A 159 4.505 21.583 30.120 1.00 14.74 C ANISOU 1091 C LYS A 159 1431 1727 2440 -92 -292 -79 C ATOM 1092 O LYS A 159 4.889 22.512 30.816 1.00 13.71 O ANISOU 1092 O LYS A 159 1368 1446 2394 -26 -62 17 O ATOM 1093 CB LYS A 159 5.879 21.281 28.036 1.00 20.06 C ANISOU 1093 CB LYS A 159 2487 2214 2918 -348 132 62 C ATOM 1094 CG LYS A 159 7.202 20.774 27.477 1.00 23.30 C ANISOU 1094 CG LYS A 159 2758 2636 3458 -272 366 -290 C ATOM 1095 CD LYS A 159 7.435 21.301 26.072 1.00 27.22 C ANISOU 1095 CD LYS A 159 3567 3124 3649 -388 519 -166 C ATOM 1096 CE LYS A 159 8.859 21.057 25.595 1.00 31.01 C ANISOU 1096 CE LYS A 159 3871 3962 3948 -361 925 -228 C ATOM 1097 NZ LYS A 159 9.111 21.785 24.319 0.50 31.80 N ANISOU 1097 NZ LYS A 159 4182 4044 3857 -332 827 -248 N ATOM 1098 N LEU A 160 3.213 21.302 29.948 1.00 14.25 N ANISOU 1098 N LEU A 160 1371 1672 2370 -121 -45 -162 N ATOM 1099 CA LEU A 160 2.184 22.042 30.671 1.00 13.26 C ANISOU 1099 CA LEU A 160 1142 1495 2400 -37 -285 -86 C ATOM 1100 C LEU A 160 2.279 21.807 32.190 1.00 13.41 C ANISOU 1100 C LEU A 160 1422 1281 2389 -84 -167 -180 C ATOM 1101 O LEU A 160 2.138 22.746 32.966 1.00 13.91 O ANISOU 1101 O LEU A 160 1714 1175 2396 -27 -76 -126 O ATOM 1102 CB LEU A 160 0.793 21.688 30.146 1.00 13.03 C ANISOU 1102 CB LEU A 160 1203 1550 2195 -132 -279 -10 C ATOM 1103 CG LEU A 160 0.486 22.145 28.715 1.00 15.01 C ANISOU 1103 CG LEU A 160 1697 1898 2106 -218 -169 61 C ATOM 1104 CD1 LEU A 160 -0.787 21.455 28.251 1.00 15.30 C ANISOU 1104 CD1 LEU A 160 1507 1981 2326 -177 -130 278 C ATOM 1105 CD2 LEU A 160 0.335 23.660 28.570 1.00 15.82 C ANISOU 1105 CD2 LEU A 160 1769 1949 2291 -288 -117 182 C ATOM 1106 N ASN A 161 2.536 20.567 32.613 1.00 14.71 N ANISOU 1106 N ASN A 161 1450 1432 2707 -65 -280 32 N ATOM 1107 CA ASN A 161 2.751 20.291 34.041 1.00 15.18 C ANISOU 1107 CA ASN A 161 1326 1811 2630 -86 -266 -96 C ATOM 1108 C ASN A 161 4.020 20.934 34.593 1.00 14.92 C ANISOU 1108 C ASN A 161 1625 1434 2607 -212 -329 -129 C ATOM 1109 O ASN A 161 4.023 21.424 35.726 1.00 14.10 O ANISOU 1109 O ASN A 161 1299 1342 2713 -366 -255 -208 O ATOM 1110 CB ASN A 161 2.774 18.790 34.327 1.00 15.38 C ANISOU 1110 CB ASN A 161 1458 1909 2474 -96 -198 17 C ATOM 1111 CG ASN A 161 1.394 18.172 34.255 1.00 16.17 C ANISOU 1111 CG ASN A 161 1562 1915 2664 -206 -127 53 C ATOM 1112 OD1 ASN A 161 0.484 18.562 34.997 1.00 17.40 O ANISOU 1112 OD1 ASN A 161 2149 1876 2587 -39 101 -1 O ATOM 1113 ND2 ASN A 161 1.224 17.223 33.356 1.00 18.19 N ANISOU 1113 ND2 ASN A 161 2176 1920 2815 236 -310 -70 N ATOM 1114 N ALA A 162 5.083 20.938 33.798 1.00 15.78 N ANISOU 1114 N ALA A 162 2080 1634 2280 -61 -162 -311 N ATOM 1115 CA ALA A 162 6.357 21.540 34.222 1.00 17.47 C ANISOU 1115 CA ALA A 162 2267 1832 2539 -327 -198 -189 C ATOM 1116 C ALA A 162 6.230 23.061 34.362 1.00 18.02 C ANISOU 1116 C ALA A 162 2405 1831 2610 -295 -74 -119 C ATOM 1117 O ALA A 162 6.815 23.649 35.266 1.00 18.62 O ANISOU 1117 O ALA A 162 2560 1942 2571 -166 -177 -127 O ATOM 1118 CB ALA A 162 7.470 21.175 33.252 1.00 19.03 C ANISOU 1118 CB ALA A 162 2473 2245 2512 -236 -122 -124 C ATOM 1119 N LYS A 163 5.452 23.682 33.473 1.00 18.68 N ANISOU 1119 N LYS A 163 2386 2060 2649 -116 -30 -167 N ATOM 1120 CA LYS A 163 5.168 25.120 33.538 1.00 18.31 C ANISOU 1120 CA LYS A 163 2265 1963 2727 -301 45 -145 C ATOM 1121 C LYS A 163 4.406 25.477 34.814 1.00 17.93 C ANISOU 1121 C LYS A 163 2208 1751 2851 -266 176 -42 C ATOM 1122 O LYS A 163 4.723 26.470 35.469 1.00 15.84 O ANISOU 1122 O LYS A 163 1559 1806 2651 -404 335 54 O ATOM 1123 CB LYS A 163 4.391 25.584 32.295 1.00 17.84 C ANISOU 1123 CB LYS A 163 2415 1693 2669 -84 112 -227 C ATOM 1124 CG LYS A 163 4.083 27.086 32.210 1.00 16.26 C ANISOU 1124 CG LYS A 163 2110 1695 2371 -138 -63 -198 C ATOM 1125 CD LYS A 163 5.312 27.988 32.261 1.00 18.84 C ANISOU 1125 CD LYS A 163 2546 2167 2444 -597 177 -79 C ATOM 1126 CE LYS A 163 6.265 27.753 31.104 1.00 20.02 C ANISOU 1126 CE LYS A 163 2604 2428 2575 -612 218 -247 C ATOM 1127 NZ LYS A 163 7.462 28.638 31.185 1.00 19.95 N ANISOU 1127 NZ LYS A 163 2694 2348 2537 -679 210 -156 N ATOM 1128 N LEU A 164 3.411 24.666 35.169 1.00 18.14 N ANISOU 1128 N LEU A 164 2302 1700 2887 -286 277 -154 N ATOM 1129 CA LEU A 164 2.695 24.849 36.435 1.00 16.44 C ANISOU 1129 CA LEU A 164 2049 1489 2707 -488 113 20 C ATOM 1130 C LEU A 164 3.626 24.813 37.646 1.00 15.83 C ANISOU 1130 C LEU A 164 2120 1289 2603 -185 130 -131 C ATOM 1131 O LEU A 164 3.550 25.696 38.499 1.00 16.84 O ANISOU 1131 O LEU A 164 2081 1494 2822 -54 -9 -357 O ATOM 1132 CB LEU A 164 1.587 23.806 36.598 1.00 15.79 C ANISOU 1132 CB LEU A 164 1919 1511 2566 -450 41 -18 C ATOM 1133 CG LEU A 164 0.404 23.996 35.646 1.00 16.18 C ANISOU 1133 CG LEU A 164 2214 1415 2518 -144 -46 45 C ATOM 1134 CD1 LEU A 164 -0.450 22.743 35.649 1.00 17.14 C ANISOU 1134 CD1 LEU A 164 2284 1738 2490 -421 15 138 C ATOM 1135 CD2 LEU A 164 -0.438 25.215 36.022 1.00 17.63 C ANISOU 1135 CD2 LEU A 164 2538 1695 2465 169 94 107 C ATOM 1136 N ALA A 165 4.509 23.811 37.703 1.00 14.86 N ANISOU 1136 N ALA A 165 2113 1239 2291 -196 -20 -28 N ATOM 1137 CA ALA A 165 5.496 23.706 38.784 1.00 16.48 C ANISOU 1137 CA ALA A 165 2050 1744 2466 -157 -102 -230 C ATOM 1138 C ALA A 165 6.420 24.923 38.845 1.00 16.66 C ANISOU 1138 C ALA A 165 2180 1560 2589 -67 -263 -360 C ATOM 1139 O ALA A 165 6.725 25.415 39.933 1.00 16.29 O ANISOU 1139 O ALA A 165 1947 1538 2705 -15 -436 -427 O ATOM 1140 CB ALA A 165 6.320 22.425 38.649 1.00 15.07 C ANISOU 1140 CB ALA A 165 1577 1952 2193 -162 -153 -331 C ATOM 1141 N GLU A 166 6.858 25.393 37.677 1.00 17.88 N ANISOU 1141 N GLU A 166 2530 1750 2511 13 -349 -326 N ATOM 1142 CA GLU A 166 7.716 26.585 37.571 1.00 21.71 C ANISOU 1142 CA GLU A 166 2588 1610 4049 74 -339 -474 C ATOM 1143 C GLU A 166 7.054 27.832 38.156 1.00 18.71 C ANISOU 1143 C GLU A 166 2245 1946 2915 85 4 -231 C ATOM 1144 O GLU A 166 7.674 28.566 38.934 1.00 18.43 O ANISOU 1144 O GLU A 166 2287 1986 2729 -88 142 -128 O ATOM 1145 CB GLU A 166 8.099 26.838 36.104 1.00 27.10 C ANISOU 1145 CB GLU A 166 4470 1318 4507 1259 554 -1285 C ATOM 1146 CG GLU A 166 8.976 28.072 35.881 1.00 26.27 C ANISOU 1146 CG GLU A 166 3697 1811 4470 1567 490 -926 C ATOM 1147 CD GLU A 166 9.283 28.344 34.420 1.00 29.23 C ANISOU 1147 CD GLU A 166 3602 3162 4340 -172 208 -669 C ATOM 1148 OE1 GLU A 166 8.609 27.785 33.531 1.00 27.48 O ANISOU 1148 OE1 GLU A 166 3370 3543 3529 -689 624 -88 O ATOM 1149 OE2 GLU A 166 10.198 29.140 34.155 1.00 33.88 O ANISOU 1149 OE2 GLU A 166 4244 4739 3888 -1201 178 -648 O ATOM 1150 N LEU A 167 5.806 28.076 37.756 1.00 17.35 N ANISOU 1150 N LEU A 167 2091 1646 2854 -48 179 -127 N ATOM 1151 CA LEU A 167 5.056 29.250 38.204 1.00 18.44 C ANISOU 1151 CA LEU A 167 2569 1746 2690 148 235 -126 C ATOM 1152 C LEU A 167 4.629 29.162 39.672 1.00 18.41 C ANISOU 1152 C LEU A 167 2487 1826 2681 8 176 95 C ATOM 1153 O LEU A 167 4.496 30.195 40.342 1.00 19.12 O ANISOU 1153 O LEU A 167 2492 1771 2998 -39 18 26 O ATOM 1154 CB LEU A 167 3.841 29.487 37.298 1.00 17.14 C ANISOU 1154 CB LEU A 167 1928 1103 3481 728 481 -520 C ATOM 1155 CG LEU A 167 4.168 29.733 35.813 1.00 20.99 C ANISOU 1155 CG LEU A 167 2496 2211 3267 183 135 -243 C ATOM 1156 CD1 LEU A 167 2.910 30.011 35.013 1.00 22.51 C ANISOU 1156 CD1 LEU A 167 2628 2888 3037 -9 118 -52 C ATOM 1157 CD2 LEU A 167 5.167 30.870 35.633 1.00 22.49 C ANISOU 1157 CD2 LEU A 167 3098 2489 2959 -191 63 -25 C ATOM 1158 N ARG A 168 4.415 27.934 40.154 1.00 17.86 N ANISOU 1158 N ARG A 168 2304 1998 2484 -145 20 225 N ATOM 1159 CA ARG A 168 4.193 27.669 41.573 1.00 17.28 C ANISOU 1159 CA ARG A 168 2026 2030 2509 -84 -65 328 C ATOM 1160 C ARG A 168 5.443 28.018 42.372 1.00 19.36 C ANISOU 1160 C ARG A 168 2084 2312 2959 -271 -165 300 C ATOM 1161 O ARG A 168 5.365 28.722 43.374 1.00 21.71 O ANISOU 1161 O ARG A 168 2407 2876 2963 -531 -604 99 O ATOM 1162 CB ARG A 168 3.812 26.191 41.797 1.00 18.34 C ANISOU 1162 CB ARG A 168 2282 2044 2642 -188 27 229 C ATOM 1163 CG ARG A 168 3.746 25.742 43.253 1.00 18.43 C ANISOU 1163 CG ARG A 168 2408 1944 2649 -212 -28 235 C ATOM 1164 CD ARG A 168 3.089 24.374 43.393 1.00 18.91 C ANISOU 1164 CD ARG A 168 2453 1997 2732 -249 65 366 C ATOM 1165 NE ARG A 168 3.796 23.309 42.675 1.00 19.24 N ANISOU 1165 NE ARG A 168 2582 2055 2672 -376 166 268 N ATOM 1166 CZ ARG A 168 4.892 22.678 43.102 1.00 21.58 C ANISOU 1166 CZ ARG A 168 2509 2678 3012 -151 352 297 C ATOM 1167 NH1 ARG A 168 5.468 22.996 44.260 1.00 22.61 N ANISOU 1167 NH1 ARG A 168 2768 2905 2918 -251 482 259 N ATOM 1168 NH2 ARG A 168 5.427 21.712 42.357 1.00 23.23 N ANISOU 1168 NH2 ARG A 168 2796 3209 2818 -54 583 172 N ATOM 1169 N ARG A 169 6.588 27.519 41.917 1.00 18.60 N ANISOU 1169 N ARG A 169 2177 2274 2614 -203 -225 118 N ATOM 1170 CA ARG A 169 7.832 27.672 42.658 1.00 19.91 C ANISOU 1170 CA ARG A 169 2489 2196 2880 -270 -513 90 C ATOM 1171 C ARG A 169 8.439 29.075 42.607 1.00 21.32 C ANISOU 1171 C ARG A 169 2624 2321 3156 -437 -727 116 C ATOM 1172 O ARG A 169 9.099 29.473 43.560 1.00 22.12 O ANISOU 1172 O ARG A 169 2479 2473 3453 -560 -799 -42 O ATOM 1173 CB ARG A 169 8.857 26.631 42.207 1.00 19.51 C ANISOU 1173 CB ARG A 169 2770 1954 2689 -344 -262 80 C ATOM 1174 CG ARG A 169 8.500 25.227 42.661 1.00 19.82 C ANISOU 1174 CG ARG A 169 2889 1950 2689 -213 -364 200 C ATOM 1175 CD ARG A 169 9.469 24.213 42.093 1.00 21.42 C ANISOU 1175 CD ARG A 169 3166 2113 2861 -293 -127 -115 C ATOM 1176 NE ARG A 169 9.266 22.886 42.688 1.00 23.26 N ANISOU 1176 NE ARG A 169 3344 2249 3245 -34 -14 137 N ATOM 1177 CZ ARG A 169 9.120 21.740 42.022 1.00 24.23 C ANISOU 1177 CZ ARG A 169 3129 2794 3281 -194 -62 -269 C ATOM 1178 NH1 ARG A 169 9.167 21.693 40.688 1.00 22.87 N ANISOU 1178 NH1 ARG A 169 2602 2862 3226 -265 -236 87 N ATOM 1179 NH2 ARG A 169 8.937 20.611 42.709 1.00 27.83 N ANISOU 1179 NH2 ARG A 169 3487 3556 3529 -102 94 368 N ATOM 1180 N ASN A 170 8.222 29.824 41.525 1.00 22.27 N ANISOU 1180 N ASN A 170 2515 2750 3193 -361 -396 353 N ATOM 1181 CA ASN A 170 8.731 31.205 41.452 1.00 23.87 C ANISOU 1181 CA ASN A 170 2794 2525 3751 -214 -398 -146 C ATOM 1182 C ASN A 170 7.775 32.289 41.975 1.00 23.33 C ANISOU 1182 C ASN A 170 2951 2123 3788 -418 -378 -210 C ATOM 1183 O ASN A 170 8.107 33.467 41.923 1.00 25.23 O ANISOU 1183 O ASN A 170 3540 1924 4120 -294 -1010 -707 O ATOM 1184 CB ASN A 170 9.299 31.541 40.052 1.00 25.52 C ANISOU 1184 CB ASN A 170 2849 2648 4198 -162 -34 40 C ATOM 1185 CG ASN A 170 8.242 31.723 38.970 1.00 27.31 C ANISOU 1185 CG ASN A 170 3240 2596 4538 -171 -371 -104 C ATOM 1186 OD1 ASN A 170 7.065 31.993 39.232 1.00 26.66 O ANISOU 1186 OD1 ASN A 170 3282 2378 4468 171 -748 -589 O ATOM 1187 ND2 ASN A 170 8.681 31.598 37.722 1.00 27.24 N ANISOU 1187 ND2 ASN A 170 3357 2289 4703 -107 -232 152 N ATOM 1188 N GLY A 171 6.602 31.895 42.474 1.00 23.39 N ANISOU 1188 N GLY A 171 2828 2428 3629 -41 -222 -269 N ATOM 1189 CA GLY A 171 5.659 32.838 43.078 1.00 24.70 C ANISOU 1189 CA GLY A 171 3167 2751 3466 0 33 -411 C ATOM 1190 C GLY A 171 4.797 33.641 42.117 1.00 24.21 C ANISOU 1190 C GLY A 171 2720 2383 4094 -122 -13 -351 C ATOM 1191 O GLY A 171 4.069 34.528 42.555 1.00 26.87 O ANISOU 1191 O GLY A 171 3214 2302 4693 1 -217 -644 O ATOM 1192 N THR A 172 4.862 33.336 40.817 1.00 23.64 N ANISOU 1192 N THR A 172 2670 2391 3920 -42 57 50 N ATOM 1193 CA THR A 172 4.001 33.973 39.813 1.00 23.25 C ANISOU 1193 CA THR A 172 2389 2751 3693 -223 161 138 C ATOM 1194 C THR A 172 2.525 33.646 40.075 1.00 21.27 C ANISOU 1194 C THR A 172 2320 2133 3625 92 264 127 C ATOM 1195 O THR A 172 1.684 34.533 40.023 1.00 22.21 O ANISOU 1195 O THR A 172 3163 1337 3937 41 -42 204 O ATOM 1196 CB THR A 172 4.386 33.540 38.374 1.00 22.63 C ANISOU 1196 CB THR A 172 2357 2665 3574 -308 107 195 C ATOM 1197 OG1 THR A 172 5.730 33.940 38.092 1.00 24.91 O ANISOU 1197 OG1 THR A 172 2034 3215 4216 417 391 366 O ATOM 1198 CG2 THR A 172 3.473 34.177 37.331 1.00 22.53 C ANISOU 1198 CG2 THR A 172 2611 2686 3262 2 467 324 C ATOM 1199 N LEU A 173 2.226 32.375 40.345 1.00 20.59 N ANISOU 1199 N LEU A 173 2236 2182 3406 -60 190 131 N ATOM 1200 CA LEU A 173 0.866 31.937 40.686 1.00 20.85 C ANISOU 1200 CA LEU A 173 2231 2558 3130 4 282 -127 C ATOM 1201 C LEU A 173 0.899 31.221 42.049 1.00 21.85 C ANISOU 1201 C LEU A 173 2545 2582 3173 -333 184 -132 C ATOM 1202 O LEU A 173 0.879 29.993 42.109 1.00 20.41 O ANISOU 1202 O LEU A 173 1936 2605 3214 -499 -128 -116 O ATOM 1203 CB LEU A 173 0.311 31.025 39.582 1.00 22.18 C ANISOU 1203 CB LEU A 173 2779 2477 3171 77 160 -125 C ATOM 1204 CG LEU A 173 0.214 31.605 38.161 1.00 23.71 C ANISOU 1204 CG LEU A 173 2964 2915 3126 279 98 -133 C ATOM 1205 CD1 LEU A 173 -0.217 30.528 37.174 1.00 23.88 C ANISOU 1205 CD1 LEU A 173 2918 2949 3207 104 226 -107 C ATOM 1206 CD2 LEU A 173 -0.739 32.792 38.096 1.00 23.20 C ANISOU 1206 CD2 LEU A 173 3258 2435 3119 67 -36 160 C ATOM 1207 N PRO A 174 0.954 31.989 43.157 1.00 24.95 N ANISOU 1207 N PRO A 174 3436 2659 3382 -510 258 -300 N ATOM 1208 CA PRO A 174 1.156 31.376 44.484 1.00 25.61 C ANISOU 1208 CA PRO A 174 3517 2635 3578 -887 44 -165 C ATOM 1209 C PRO A 174 -0.023 30.534 44.998 1.00 23.98 C ANISOU 1209 C PRO A 174 3044 2787 3278 -546 11 16 C ATOM 1210 O PRO A 174 0.133 29.796 45.965 1.00 23.97 O ANISOU 1210 O PRO A 174 2821 2914 3370 -1499 -76 269 O ATOM 1211 CB PRO A 174 1.390 32.585 45.394 1.00 30.33 C ANISOU 1211 CB PRO A 174 4393 3093 4036 -870 -285 -608 C ATOM 1212 CG PRO A 174 0.658 33.698 44.735 1.00 32.36 C ANISOU 1212 CG PRO A 174 5710 1789 4797 -1204 -43 -369 C ATOM 1213 CD PRO A 174 0.741 33.446 43.256 1.00 30.53 C ANISOU 1213 CD PRO A 174 4264 2638 4698 -486 149 -229 C ATOM 1214 N TRP A 175 -1.180 30.659 44.355 1.00 21.79 N ANISOU 1214 N TRP A 175 2627 2126 3527 -392 262 -177 N ATOM 1215 CA TRP A 175 -2.337 29.801 44.624 1.00 19.89 C ANISOU 1215 CA TRP A 175 2236 2255 3065 -120 320 -105 C ATOM 1216 C TRP A 175 -2.206 28.357 44.116 1.00 20.12 C ANISOU 1216 C TRP A 175 2219 2087 3338 -333 204 -12 C ATOM 1217 O TRP A 175 -2.992 27.510 44.517 1.00 17.95 O ANISOU 1217 O TRP A 175 1745 1630 3445 100 388 -265 O ATOM 1218 CB TRP A 175 -3.629 30.427 44.075 1.00 21.53 C ANISOU 1218 CB TRP A 175 2431 2481 3265 36 148 -69 C ATOM 1219 CG TRP A 175 -3.602 30.849 42.627 1.00 20.02 C ANISOU 1219 CG TRP A 175 2241 2117 3245 72 108 -122 C ATOM 1220 CD1 TRP A 175 -3.362 32.109 42.149 1.00 20.42 C ANISOU 1220 CD1 TRP A 175 2260 2368 3130 -68 214 81 C ATOM 1221 CD2 TRP A 175 -3.858 30.031 41.479 1.00 19.81 C ANISOU 1221 CD2 TRP A 175 2210 2285 3032 21 59 23 C ATOM 1222 NE1 TRP A 175 -3.440 32.125 40.782 1.00 19.48 N ANISOU 1222 NE1 TRP A 175 2176 2043 3181 128 -76 97 N ATOM 1223 CE2 TRP A 175 -3.743 30.865 40.340 1.00 19.33 C ANISOU 1223 CE2 TRP A 175 2154 2225 2963 34 -89 -29 C ATOM 1224 CE3 TRP A 175 -4.167 28.677 41.298 1.00 19.59 C ANISOU 1224 CE3 TRP A 175 2475 2187 2778 239 -60 31 C ATOM 1225 CZ2 TRP A 175 -3.923 30.388 39.040 1.00 19.27 C ANISOU 1225 CZ2 TRP A 175 2150 2605 2564 63 173 294 C ATOM 1226 CZ3 TRP A 175 -4.352 28.203 39.999 1.00 20.15 C ANISOU 1226 CZ3 TRP A 175 2544 2526 2584 153 -42 244 C ATOM 1227 CH2 TRP A 175 -4.224 29.060 38.887 1.00 18.91 C ANISOU 1227 CH2 TRP A 175 2181 2569 2431 204 -35 179 C ATOM 1228 N LEU A 176 -1.238 28.076 43.244 1.00 19.92 N ANISOU 1228 N LEU A 176 1683 1622 4260 -1156 740 529 N ATOM 1229 CA LEU A 176 -1.016 26.703 42.770 1.00 19.30 C ANISOU 1229 CA LEU A 176 2165 2144 3024 -428 -38 131 C ATOM 1230 C LEU A 176 -0.500 25.763 43.855 1.00 19.80 C ANISOU 1230 C LEU A 176 2328 1926 3266 -320 -163 72 C ATOM 1231 O LEU A 176 0.292 26.171 44.715 1.00 19.63 O ANISOU 1231 O LEU A 176 2268 1567 3620 -131 -449 233 O ATOM 1232 CB LEU A 176 0.001 26.670 41.626 1.00 19.92 C ANISOU 1232 CB LEU A 176 2285 2425 2857 -282 -67 51 C ATOM 1233 CG LEU A 176 -0.418 27.222 40.269 1.00 18.97 C ANISOU 1233 CG LEU A 176 2182 2230 2796 -224 -172 -135 C ATOM 1234 CD1 LEU A 176 0.795 27.335 39.363 1.00 20.45 C ANISOU 1234 CD1 LEU A 176 2507 2495 2766 -37 57 8 C ATOM 1235 CD2 LEU A 176 -1.485 26.345 39.628 1.00 20.53 C ANISOU 1235 CD2 LEU A 176 2880 2388 2530 -413 -314 -383 C ATOM 1236 N AARG A 177 -0.984 24.517 43.824 0.50 18.82 N ANISOU 1236 N AARG A 177 1930 2054 3166 -409 -75 136 N ATOM 1237 CA AARG A 177 -0.473 23.425 44.662 0.50 18.92 C ANISOU 1237 CA AARG A 177 2102 2164 2920 -245 -68 46 C ATOM 1238 C AARG A 177 0.163 22.353 43.769 0.50 18.29 C ANISOU 1238 C AARG A 177 1907 1920 3121 -91 -286 104 C ATOM 1239 O AARG A 177 0.023 22.421 42.549 0.50 17.21 O ANISOU 1239 O AARG A 177 1539 1902 3098 -201 -286 -12 O ATOM 1240 CB AARG A 177 -1.583 22.832 45.526 0.50 20.22 C ANISOU 1240 CB AARG A 177 2605 2440 2635 -456 24 139 C ATOM 1241 CG AARG A 177 -1.639 23.420 46.925 0.50 18.40 C ANISOU 1241 CG AARG A 177 2616 2315 2059 -1455 790 824 C ATOM 1242 CD AARG A 177 -2.237 24.813 46.913 0.50 16.54 C ANISOU 1242 CD AARG A 177 2934 2015 1335 -1794 579 317 C ATOM 1243 NE AARG A 177 -2.208 25.451 48.225 0.50 16.79 N ANISOU 1243 NE AARG A 177 2215 3131 1033 -1727 608 315 N ATOM 1244 CZ AARG A 177 -1.535 26.560 48.499 0.50 19.11 C ANISOU 1244 CZ AARG A 177 2614 2239 2407 -852 225 -157 C ATOM 1245 NH1AARG A 177 -0.832 27.164 47.550 0.50 22.36 N ANISOU 1245 NH1AARG A 177 4099 1249 3146 -1215 528 54 N ATOM 1246 NH2AARG A 177 -1.576 27.072 49.718 0.50 22.10 N ANISOU 1246 NH2AARG A 177 2919 2637 2840 -100 385 -629 N ATOM 1247 N BARG A 177 -0.924 24.505 43.772 0.50 19.03 N ANISOU 1247 N BARG A 177 2031 1952 3245 -285 -231 17 N ATOM 1248 CA BARG A 177 -0.434 23.443 44.640 0.50 19.61 C ANISOU 1248 CA BARG A 177 2281 2017 3149 14 -310 -159 C ATOM 1249 C BARG A 177 0.127 22.319 43.767 0.50 18.13 C ANISOU 1249 C BARG A 177 1936 1757 3195 -81 -352 -52 C ATOM 1250 O BARG A 177 -0.088 22.327 42.556 0.50 17.59 O ANISOU 1250 O BARG A 177 1665 1802 3213 -176 -406 -143 O ATOM 1251 CB BARG A 177 -1.555 22.979 45.553 0.50 20.81 C ANISOU 1251 CB BARG A 177 2542 2266 3096 43 -236 -96 C ATOM 1252 CG BARG A 177 -1.970 24.064 46.529 0.50 23.58 C ANISOU 1252 CG BARG A 177 3046 2229 3683 136 -343 -345 C ATOM 1253 CD BARG A 177 -3.152 23.622 47.356 0.50 30.54 C ANISOU 1253 CD BARG A 177 2896 3278 5426 -319 -242 167 C ATOM 1254 NE BARG A 177 -3.346 24.453 48.533 0.50 28.56 N ANISOU 1254 NE BARG A 177 796 983 9072 -133 -796 -1427 N ATOM 1255 CZ BARG A 177 -4.464 24.452 49.245 0.50 25.27 C ANISOU 1255 CZ BARG A 177 2769 1998 4832 -308 -534 -292 C ATOM 1256 NH1BARG A 177 -5.473 23.669 48.876 0.50 19.98 N ANISOU 1256 NH1BARG A 177 1953 1641 3994 -109 280 39 N ATOM 1257 NH2BARG A 177 -4.575 25.232 50.308 0.50 26.64 N ANISOU 1257 NH2BARG A 177 3013 2445 4661 -349 -10 -226 N ATOM 1258 N PRO A 178 0.884 21.377 44.366 1.00 17.44 N ANISOU 1258 N PRO A 178 1928 1660 3037 -58 -117 -7 N ATOM 1259 CA PRO A 178 1.676 20.430 43.545 1.00 16.65 C ANISOU 1259 CA PRO A 178 1831 1550 2943 -28 -130 95 C ATOM 1260 C PRO A 178 0.960 19.386 42.680 1.00 16.61 C ANISOU 1260 C PRO A 178 1633 1548 3128 -55 -18 17 C ATOM 1261 O PRO A 178 1.576 18.867 41.749 1.00 17.25 O ANISOU 1261 O PRO A 178 1522 1736 3295 -102 -100 -238 O ATOM 1262 CB PRO A 178 2.558 19.730 44.585 1.00 16.80 C ANISOU 1262 CB PRO A 178 2080 1734 2568 114 -31 51 C ATOM 1263 CG PRO A 178 2.605 20.658 45.737 1.00 16.42 C ANISOU 1263 CG PRO A 178 1990 1615 2632 84 -7 53 C ATOM 1264 CD PRO A 178 1.211 21.200 45.796 1.00 17.60 C ANISOU 1264 CD PRO A 178 1951 1736 2997 31 -85 92 C ATOM 1265 N ASP A 179 -0.295 19.071 42.990 1.00 15.15 N ANISOU 1265 N ASP A 179 1421 1277 3055 266 -66 -20 N ATOM 1266 CA ASP A 179 -1.068 18.041 42.270 1.00 15.74 C ANISOU 1266 CA ASP A 179 1646 1558 2776 48 -26 27 C ATOM 1267 C ASP A 179 -1.732 18.637 41.026 1.00 14.29 C ANISOU 1267 C ASP A 179 1480 1271 2676 148 105 -68 C ATOM 1268 O ASP A 179 -2.545 19.555 41.141 1.00 17.38 O ANISOU 1268 O ASP A 179 2482 1348 2774 689 -58 42 O ATOM 1269 CB ASP A 179 -2.114 17.462 43.234 1.00 16.67 C ANISOU 1269 CB ASP A 179 1825 1712 2796 -87 -2 133 C ATOM 1270 CG ASP A 179 -2.938 16.321 42.644 1.00 16.68 C ANISOU 1270 CG ASP A 179 1691 1634 3010 -31 -19 186 C ATOM 1271 OD1 ASP A 179 -2.718 15.892 41.489 1.00 16.74 O ANISOU 1271 OD1 ASP A 179 1697 1577 3082 -42 136 186 O ATOM 1272 OD2 ASP A 179 -3.825 15.846 43.392 1.00 17.41 O ANISOU 1272 OD2 ASP A 179 1914 1722 2977 -102 212 -43 O ATOM 1273 N SER A 180 -1.379 18.104 39.853 1.00 14.49 N ANISOU 1273 N SER A 180 1580 1182 2742 352 51 -95 N ATOM 1274 CA SER A 180 -1.891 18.576 38.557 1.00 15.49 C ANISOU 1274 CA SER A 180 1779 1480 2628 207 92 0 C ATOM 1275 C SER A 180 -1.995 17.453 37.529 1.00 13.57 C ANISOU 1275 C SER A 180 1500 1225 2430 556 26 198 C ATOM 1276 O SER A 180 -1.282 16.438 37.612 1.00 15.36 O ANISOU 1276 O SER A 180 1813 1299 2723 778 117 -103 O ATOM 1277 CB SER A 180 -1.016 19.709 37.986 1.00 14.96 C ANISOU 1277 CB SER A 180 1515 1971 2196 31 62 -51 C ATOM 1278 OG SER A 180 0.291 19.264 37.618 1.00 15.52 O ANISOU 1278 OG SER A 180 1364 1904 2626 -1 -59 61 O ATOM 1279 N LYS A 181 -2.884 17.648 36.562 1.00 13.42 N ANISOU 1279 N LYS A 181 1211 1394 2492 495 86 169 N ATOM 1280 CA LYS A 181 -3.032 16.758 35.408 1.00 13.66 C ANISOU 1280 CA LYS A 181 1206 1554 2429 6 32 207 C ATOM 1281 C LYS A 181 -3.292 17.598 34.178 1.00 14.47 C ANISOU 1281 C LYS A 181 1516 1742 2238 -99 -13 132 C ATOM 1282 O LYS A 181 -3.976 18.634 34.258 1.00 16.41 O ANISOU 1282 O LYS A 181 1779 1957 2499 120 199 162 O ATOM 1283 CB LYS A 181 -4.204 15.777 35.595 1.00 13.38 C ANISOU 1283 CB LYS A 181 1412 1584 2087 -179 -50 7 C ATOM 1284 CG LYS A 181 -4.125 14.932 36.857 1.00 14.00 C ANISOU 1284 CG LYS A 181 1471 1657 2189 -311 -8 83 C ATOM 1285 CD LYS A 181 -5.253 13.910 36.929 1.00 14.20 C ANISOU 1285 CD LYS A 181 1420 1763 2210 -332 -45 139 C ATOM 1286 CE LYS A 181 -5.049 12.728 36.001 1.00 15.33 C ANISOU 1286 CE LYS A 181 1724 1831 2268 -283 -1 98 C ATOM 1287 NZ LYS A 181 -6.125 11.693 36.174 1.00 15.65 N ANISOU 1287 NZ LYS A 181 1756 1757 2431 -261 -44 75 N ATOM 1288 N THR A 182 -2.756 17.147 33.045 1.00 14.46 N ANISOU 1288 N THR A 182 1411 1617 2466 -152 67 -5 N ATOM 1289 CA THR A 182 -3.008 17.772 31.748 1.00 15.18 C ANISOU 1289 CA THR A 182 1581 1820 2364 131 41 -69 C ATOM 1290 C THR A 182 -3.295 16.724 30.689 1.00 14.77 C ANISOU 1290 C THR A 182 1416 1871 2322 6 75 -15 C ATOM 1291 O THR A 182 -2.940 15.562 30.844 1.00 15.15 O ANISOU 1291 O THR A 182 1281 1971 2504 45 -200 11 O ATOM 1292 CB THR A 182 -1.811 18.616 31.282 1.00 14.81 C ANISOU 1292 CB THR A 182 1673 1691 2261 247 164 -50 C ATOM 1293 OG1 THR A 182 -0.682 17.765 31.027 1.00 15.29 O ANISOU 1293 OG1 THR A 182 1450 1877 2481 348 -105 136 O ATOM 1294 CG2 THR A 182 -1.443 19.663 32.337 1.00 16.33 C ANISOU 1294 CG2 THR A 182 1967 1843 2394 92 31 -121 C ATOM 1295 N GLN A 183 -3.934 17.154 29.605 1.00 14.87 N ANISOU 1295 N GLN A 183 1503 1661 2486 25 -6 20 N ATOM 1296 CA GLN A 183 -4.280 16.275 28.495 1.00 13.55 C ANISOU 1296 CA GLN A 183 1247 1597 2302 163 118 81 C ATOM 1297 C GLN A 183 -4.388 17.076 27.213 1.00 13.08 C ANISOU 1297 C GLN A 183 1272 1428 2269 14 177 22 C ATOM 1298 O GLN A 183 -5.052 18.121 27.182 1.00 14.40 O ANISOU 1298 O GLN A 183 1529 1570 2372 211 209 -38 O ATOM 1299 CB GLN A 183 -5.606 15.560 28.777 1.00 13.36 C ANISOU 1299 CB GLN A 183 1537 1397 2141 12 208 189 C ATOM 1300 CG GLN A 183 -5.926 14.414 27.845 1.00 14.15 C ANISOU 1300 CG GLN A 183 1689 1512 2173 16 116 128 C ATOM 1301 CD GLN A 183 -7.186 13.698 28.275 1.00 15.64 C ANISOU 1301 CD GLN A 183 1697 1665 2579 -52 127 72 C ATOM 1302 OE1 GLN A 183 -7.147 12.813 29.142 1.00 18.53 O ANISOU 1302 OE1 GLN A 183 2739 1394 2907 -243 55 79 O ATOM 1303 NE2 GLN A 183 -8.320 14.095 27.700 1.00 16.90 N ANISOU 1303 NE2 GLN A 183 1752 1739 2927 0 15 116 N ATOM 1304 N VAL A 184 -3.766 16.560 26.157 1.00 13.65 N ANISOU 1304 N VAL A 184 1291 1571 2323 225 75 -83 N ATOM 1305 CA VAL A 184 -3.639 17.256 24.885 1.00 14.81 C ANISOU 1305 CA VAL A 184 1453 1832 2340 236 72 -7 C ATOM 1306 C VAL A 184 -4.085 16.335 23.752 1.00 16.50 C ANISOU 1306 C VAL A 184 1568 2123 2577 197 -104 -169 C ATOM 1307 O VAL A 184 -3.540 15.235 23.591 1.00 16.54 O ANISOU 1307 O VAL A 184 1782 1721 2779 -106 -240 30 O ATOM 1308 CB VAL A 184 -2.183 17.738 24.642 1.00 15.40 C ANISOU 1308 CB VAL A 184 1513 2146 2189 100 32 -70 C ATOM 1309 CG1 VAL A 184 -2.066 18.460 23.307 1.00 16.72 C ANISOU 1309 CG1 VAL A 184 1790 2242 2320 45 172 28 C ATOM 1310 CG2 VAL A 184 -1.725 18.660 25.766 1.00 15.81 C ANISOU 1310 CG2 VAL A 184 1883 1859 2263 -39 15 26 C ATOM 1311 N THR A 185 -5.075 16.805 22.985 1.00 16.10 N ANISOU 1311 N THR A 185 1502 2067 2546 412 151 -42 N ATOM 1312 CA THR A 185 -5.556 16.158 21.764 1.00 15.94 C ANISOU 1312 CA THR A 185 1425 1996 2634 321 48 33 C ATOM 1313 C THR A 185 -5.004 16.953 20.574 1.00 16.30 C ANISOU 1313 C THR A 185 1675 1778 2737 337 -111 212 C ATOM 1314 O THR A 185 -5.234 18.158 20.485 1.00 17.00 O ANISOU 1314 O THR A 185 1971 1596 2890 -39 129 48 O ATOM 1315 CB THR A 185 -7.104 16.154 21.700 1.00 15.79 C ANISOU 1315 CB THR A 185 1441 1893 2666 33 23 107 C ATOM 1316 OG1 THR A 185 -7.632 15.522 22.869 1.00 17.37 O ANISOU 1316 OG1 THR A 185 1909 1904 2785 254 210 217 O ATOM 1317 CG2 THR A 185 -7.603 15.409 20.483 1.00 16.86 C ANISOU 1317 CG2 THR A 185 2056 1721 2628 -85 -58 222 C ATOM 1318 N VAL A 186 -4.265 16.277 19.690 1.00 16.28 N ANISOU 1318 N VAL A 186 1901 1774 2511 83 -58 111 N ATOM 1319 CA VAL A 186 -3.710 16.874 18.477 1.00 16.55 C ANISOU 1319 CA VAL A 186 1795 1878 2612 27 12 55 C ATOM 1320 C VAL A 186 -4.388 16.253 17.262 1.00 17.11 C ANISOU 1320 C VAL A 186 2108 1762 2628 -38 61 -21 C ATOM 1321 O VAL A 186 -4.670 15.041 17.252 1.00 15.87 O ANISOU 1321 O VAL A 186 1690 1759 2579 -49 99 349 O ATOM 1322 CB VAL A 186 -2.170 16.682 18.417 1.00 16.70 C ANISOU 1322 CB VAL A 186 1803 2037 2505 17 -67 71 C ATOM 1323 CG1 VAL A 186 -1.591 17.069 17.056 1.00 18.41 C ANISOU 1323 CG1 VAL A 186 2220 2250 2524 -65 -34 138 C ATOM 1324 CG2 VAL A 186 -1.518 17.496 19.523 1.00 16.86 C ANISOU 1324 CG2 VAL A 186 2013 1922 2470 -109 -88 189 C ATOM 1325 N GLN A 187 -4.681 17.097 16.269 1.00 18.39 N ANISOU 1325 N GLN A 187 2366 2007 2612 -123 154 122 N ATOM 1326 CA GLN A 187 -5.086 16.650 14.940 1.00 20.25 C ANISOU 1326 CA GLN A 187 2796 2273 2625 -288 -67 278 C ATOM 1327 C GLN A 187 -3.841 16.441 14.087 1.00 18.96 C ANISOU 1327 C GLN A 187 2737 1807 2657 -354 -100 73 C ATOM 1328 O GLN A 187 -3.031 17.368 13.902 1.00 18.82 O ANISOU 1328 O GLN A 187 2731 1702 2717 -354 4 -222 O ATOM 1329 CB GLN A 187 -6.014 17.655 14.256 1.00 22.63 C ANISOU 1329 CB GLN A 187 3235 2388 2975 -241 -212 499 C ATOM 1330 CG GLN A 187 -6.615 17.128 12.949 1.00 24.96 C ANISOU 1330 CG GLN A 187 3555 2817 3111 -483 -310 451 C ATOM 1331 CD GLN A 187 -7.241 18.201 12.083 1.00 28.70 C ANISOU 1331 CD GLN A 187 3841 3473 3587 41 -592 626 C ATOM 1332 OE1 GLN A 187 -6.800 19.351 12.076 1.00 30.56 O ANISOU 1332 OE1 GLN A 187 4435 3477 3699 -52 -1261 1110 O ATOM 1333 NE2 GLN A 187 -8.273 17.829 11.333 1.00 27.99 N ANISOU 1333 NE2 GLN A 187 5031 2535 3067 1509 -2031 1218 N ATOM 1334 N TYR A 188 -3.713 15.225 13.562 1.00 18.57 N ANISOU 1334 N TYR A 188 2431 1757 2866 -561 -151 12 N ATOM 1335 CA TYR A 188 -2.569 14.806 12.755 1.00 19.08 C ANISOU 1335 CA TYR A 188 2611 1595 3043 -103 -94 211 C ATOM 1336 C TYR A 188 -2.991 14.535 11.322 1.00 21.42 C ANISOU 1336 C TYR A 188 2795 2384 2960 -1 -9 324 C ATOM 1337 O TYR A 188 -4.144 14.197 11.073 1.00 22.12 O ANISOU 1337 O TYR A 188 2598 2715 3089 398 -198 389 O ATOM 1338 CB TYR A 188 -2.014 13.490 13.291 1.00 18.24 C ANISOU 1338 CB TYR A 188 2199 1866 2865 142 -134 142 C ATOM 1339 CG TYR A 188 -1.163 13.584 14.523 1.00 16.59 C ANISOU 1339 CG TYR A 188 1714 1829 2759 -50 89 142 C ATOM 1340 CD1 TYR A 188 -1.722 13.479 15.795 1.00 17.36 C ANISOU 1340 CD1 TYR A 188 2198 1770 2625 -38 47 5 C ATOM 1341 CD2 TYR A 188 0.217 13.729 14.419 1.00 16.75 C ANISOU 1341 CD2 TYR A 188 1720 1972 2671 22 292 32 C ATOM 1342 CE1 TYR A 188 -0.932 13.546 16.931 1.00 16.32 C ANISOU 1342 CE1 TYR A 188 1903 1699 2597 -157 164 184 C ATOM 1343 CE2 TYR A 188 1.014 13.783 15.545 1.00 18.31 C ANISOU 1343 CE2 TYR A 188 1898 2072 2987 -89 39 -83 C ATOM 1344 CZ TYR A 188 0.443 13.688 16.801 1.00 17.65 C ANISOU 1344 CZ TYR A 188 1885 1824 2995 -260 24 105 C ATOM 1345 OH TYR A 188 1.235 13.746 17.922 1.00 17.19 O ANISOU 1345 OH TYR A 188 1408 2089 3032 -395 145 233 O ATOM 1346 N MET A 189 -2.037 14.641 10.398 1.00 21.69 N ANISOU 1346 N MET A 189 2767 2638 2836 169 -58 389 N ATOM 1347 CA MET A 189 -2.189 14.128 9.036 1.00 23.13 C ANISOU 1347 CA MET A 189 2934 2799 3056 364 -93 120 C ATOM 1348 C MET A 189 -1.303 12.899 8.864 1.00 21.78 C ANISOU 1348 C MET A 189 2539 3000 2733 400 -526 10 C ATOM 1349 O MET A 189 -0.190 12.856 9.389 1.00 22.18 O ANISOU 1349 O MET A 189 2569 2439 3418 487 -793 28 O ATOM 1350 CB MET A 189 -1.765 15.192 8.029 1.00 27.52 C ANISOU 1350 CB MET A 189 3708 3421 3326 503 104 584 C ATOM 1351 CG MET A 189 -2.158 14.893 6.594 0.50 31.00 C ANISOU 1351 CG MET A 189 4287 4048 3440 342 41 473 C ATOM 1352 SD MET A 189 -1.964 16.339 5.537 0.50 41.13 S ANISOU 1352 SD MET A 189 6185 5068 4373 235 52 1448 S ATOM 1353 CE MET A 189 -0.240 16.744 5.810 1.00 43.23 C ANISOU 1353 CE MET A 189 6067 5017 5341 733 55 590 C ATOM 1354 N GLN A 190 -1.785 11.915 8.111 1.00 22.47 N ANISOU 1354 N GLN A 190 2630 2660 3248 43 -378 157 N ATOM 1355 CA GLN A 190 -0.956 10.758 7.729 1.00 25.77 C ANISOU 1355 CA GLN A 190 3246 3065 3479 297 -165 -142 C ATOM 1356 C GLN A 190 0.074 11.136 6.661 1.00 25.46 C ANISOU 1356 C GLN A 190 2897 3272 3503 501 -288 1 C ATOM 1357 O GLN A 190 -0.212 11.934 5.773 1.00 24.59 O ANISOU 1357 O GLN A 190 2878 3552 2911 704 -305 -293 O ATOM 1358 CB GLN A 190 -1.834 9.628 7.203 1.00 28.76 C ANISOU 1358 CB GLN A 190 3915 3134 3876 -72 -65 -190 C ATOM 1359 CG GLN A 190 -2.794 9.072 8.233 1.00 30.13 C ANISOU 1359 CG GLN A 190 3949 3427 4071 -246 14 -226 C ATOM 1360 CD GLN A 190 -3.768 8.088 7.628 1.00 33.93 C ANISOU 1360 CD GLN A 190 4514 3707 4671 -127 -485 -863 C ATOM 1361 OE1 GLN A 190 -4.965 8.359 7.556 1.00 37.06 O ANISOU 1361 OE1 GLN A 190 4113 5192 4773 -771 -129 6 O ATOM 1362 NE2 GLN A 190 -3.256 6.949 7.160 1.00 37.89 N ANISOU 1362 NE2 GLN A 190 4432 2529 7433 -1117 -2686 -2306 N ATOM 1363 N ASP A 191 1.271 10.561 6.747 1.00 25.57 N ANISOU 1363 N ASP A 191 2857 3215 3644 402 -292 -23 N ATOM 1364 CA ASP A 191 2.317 10.818 5.760 1.00 27.33 C ANISOU 1364 CA ASP A 191 3156 3378 3849 664 -34 270 C ATOM 1365 C ASP A 191 3.150 9.555 5.569 1.00 27.52 C ANISOU 1365 C ASP A 191 3472 3314 3669 705 -195 97 C ATOM 1366 O ASP A 191 4.215 9.410 6.165 1.00 25.36 O ANISOU 1366 O ASP A 191 2827 3000 3806 718 277 351 O ATOM 1367 CB ASP A 191 3.184 12.017 6.192 1.00 31.50 C ANISOU 1367 CB ASP A 191 3676 4020 4271 -95 -164 644 C ATOM 1368 CG ASP A 191 4.285 12.360 5.181 1.00 34.72 C ANISOU 1368 CG ASP A 191 3481 4627 5083 -405 -144 966 C ATOM 1369 OD1 ASP A 191 4.166 12.005 3.989 1.00 35.86 O ANISOU 1369 OD1 ASP A 191 3849 4507 5267 145 -826 1077 O ATOM 1370 OD2 ASP A 191 5.286 12.989 5.585 1.00 40.30 O ANISOU 1370 OD2 ASP A 191 3600 6034 5676 -908 -600 1354 O ATOM 1371 N ARG A 192 2.628 8.648 4.741 1.00 26.94 N ANISOU 1371 N ARG A 192 3476 2819 3938 421 145 155 N ATOM 1372 CA ARG A 192 3.310 7.403 4.356 1.00 27.38 C ANISOU 1372 CA ARG A 192 3836 3094 3472 640 212 71 C ATOM 1373 C ARG A 192 3.753 6.578 5.584 1.00 27.47 C ANISOU 1373 C ARG A 192 4028 3342 3068 411 363 75 C ATOM 1374 O ARG A 192 4.886 6.089 5.661 1.00 26.60 O ANISOU 1374 O ARG A 192 4339 3070 2698 616 59 323 O ATOM 1375 CB ARG A 192 4.485 7.712 3.412 1.00 30.09 C ANISOU 1375 CB ARG A 192 4122 3645 3665 214 278 297 C ATOM 1376 CG ARG A 192 4.066 8.331 2.079 0.50 29.00 C ANISOU 1376 CG ARG A 192 3728 3833 3458 503 267 0 C ATOM 1377 CD ARG A 192 5.225 9.039 1.389 0.50 29.23 C ANISOU 1377 CD ARG A 192 3579 4139 3387 751 335 257 C ATOM 1378 NE ARG A 192 5.550 10.297 2.056 0.50 22.77 N ANISOU 1378 NE ARG A 192 2464 4200 1987 2070 1164 -96 N ATOM 1379 CZ ARG A 192 6.707 10.939 1.931 0.50 29.45 C ANISOU 1379 CZ ARG A 192 3736 3988 3463 826 312 253 C ATOM 1380 NH1 ARG A 192 7.664 10.443 1.162 0.50 34.69 N ANISOU 1380 NH1 ARG A 192 3958 5031 4189 1257 441 -13 N ATOM 1381 NH2 ARG A 192 6.910 12.076 2.580 0.50 32.93 N ANISOU 1381 NH2 ARG A 192 4341 4135 4036 396 -78 214 N ATOM 1382 N GLY A 193 2.844 6.447 6.552 1.00 25.10 N ANISOU 1382 N GLY A 193 3763 3040 2734 507 98 8 N ATOM 1383 CA GLY A 193 3.131 5.739 7.804 1.00 23.25 C ANISOU 1383 CA GLY A 193 3451 2785 2597 242 362 -4 C ATOM 1384 C GLY A 193 3.670 6.583 8.949 1.00 20.03 C ANISOU 1384 C GLY A 193 2260 2360 2989 365 245 16 C ATOM 1385 O GLY A 193 3.566 6.181 10.106 1.00 19.34 O ANISOU 1385 O GLY A 193 2381 1871 3096 4 57 -29 O ATOM 1386 N ALA A 194 4.267 7.731 8.631 1.00 18.13 N ANISOU 1386 N ALA A 194 2029 2479 2378 447 323 133 N ATOM 1387 CA ALA A 194 4.643 8.729 9.625 1.00 18.95 C ANISOU 1387 CA ALA A 194 2207 2622 2372 417 281 106 C ATOM 1388 C ALA A 194 3.440 9.607 9.913 1.00 19.97 C ANISOU 1388 C ALA A 194 2843 2388 2357 757 275 104 C ATOM 1389 O ALA A 194 2.420 9.524 9.221 1.00 22.07 O ANISOU 1389 O ALA A 194 2846 2893 2646 471 272 133 O ATOM 1390 CB ALA A 194 5.804 9.580 9.127 1.00 20.72 C ANISOU 1390 CB ALA A 194 2439 2819 2614 191 360 77 C ATOM 1391 N VAL A 195 3.567 10.449 10.932 1.00 19.93 N ANISOU 1391 N VAL A 195 2413 2531 2628 236 -10 -8 N ATOM 1392 CA VAL A 195 2.481 11.340 11.338 1.00 20.17 C ANISOU 1392 CA VAL A 195 3092 2125 2447 483 -97 12 C ATOM 1393 C VAL A 195 2.993 12.777 11.409 1.00 21.16 C ANISOU 1393 C VAL A 195 2833 2441 2764 2 -213 34 C ATOM 1394 O VAL A 195 4.133 13.005 11.808 1.00 21.31 O ANISOU 1394 O VAL A 195 2796 2270 3029 49 -250 187 O ATOM 1395 CB VAL A 195 1.815 10.871 12.654 1.00 27.71 C ANISOU 1395 CB VAL A 195 3646 4163 2719 755 396 357 C ATOM 1396 CG1 VAL A 195 1.265 9.460 12.476 1.00 28.60 C ANISOU 1396 CG1 VAL A 195 5328 3671 1868 1150 2187 1092 C ATOM 1397 CG2 VAL A 195 2.774 10.928 13.847 1.00 24.72 C ANISOU 1397 CG2 VAL A 195 3412 3051 2929 368 337 124 C ATOM 1398 N LEU A 196 2.153 13.724 10.981 1.00 21.49 N ANISOU 1398 N LEU A 196 2899 2278 2986 19 -170 -29 N ATOM 1399 CA LEU A 196 2.493 15.150 10.938 1.00 21.12 C ANISOU 1399 CA LEU A 196 2747 2116 3161 424 -184 9 C ATOM 1400 C LEU A 196 1.463 15.926 11.765 1.00 20.28 C ANISOU 1400 C LEU A 196 2423 2379 2901 257 -167 111 C ATOM 1401 O LEU A 196 0.275 15.922 11.413 1.00 19.25 O ANISOU 1401 O LEU A 196 2296 2090 2925 226 -22 72 O ATOM 1402 CB LEU A 196 2.484 15.667 9.498 1.00 24.20 C ANISOU 1402 CB LEU A 196 3220 2745 3230 626 82 115 C ATOM 1403 CG LEU A 196 3.362 14.972 8.454 1.00 29.71 C ANISOU 1403 CG LEU A 196 4058 3394 3835 767 488 -217 C ATOM 1404 CD1 LEU A 196 3.135 15.594 7.082 1.00 34.59 C ANISOU 1404 CD1 LEU A 196 4729 4100 4310 675 293 404 C ATOM 1405 CD2 LEU A 196 4.838 15.029 8.825 1.00 33.13 C ANISOU 1405 CD2 LEU A 196 4418 3873 4294 572 -130 118 C ATOM 1406 N PRO A 197 1.897 16.583 12.868 1.00 19.11 N ANISOU 1406 N PRO A 197 1910 2356 2995 2 31 79 N ATOM 1407 CA PRO A 197 0.942 17.385 13.652 1.00 18.33 C ANISOU 1407 CA PRO A 197 2145 2031 2789 -255 236 139 C ATOM 1408 C PRO A 197 0.462 18.631 12.883 1.00 18.48 C ANISOU 1408 C PRO A 197 2257 1889 2875 -761 636 569 C ATOM 1409 O PRO A 197 1.290 19.341 12.307 1.00 21.25 O ANISOU 1409 O PRO A 197 1977 2518 3579 -750 1010 630 O ATOM 1410 CB PRO A 197 1.742 17.789 14.905 0.75 19.65 C ANISOU 1410 CB PRO A 197 2285 2533 2646 59 173 71 C ATOM 1411 CG PRO A 197 3.043 17.063 14.843 0.75 20.01 C ANISOU 1411 CG PRO A 197 2335 2607 2661 108 35 -132 C ATOM 1412 CD PRO A 197 3.261 16.640 13.429 0.75 18.90 C ANISOU 1412 CD PRO A 197 1925 2658 2596 45 104 2 C ATOM 1413 N ILE A 198 -0.854 18.866 12.888 1.00 19.06 N ANISOU 1413 N ILE A 198 2409 1956 2875 -414 328 485 N ATOM 1414 C ILE A 198 -1.892 21.099 13.207 1.00 21.95 C ANISOU 1414 C ILE A 198 3093 1950 3294 2 173 273 C ATOM 1415 O ILE A 198 -1.529 22.267 13.045 1.00 20.91 O ANISOU 1415 O ILE A 198 3036 1578 3327 671 450 397 O ATOM 1416 CA AILE A 198 -1.453 20.019 12.207 0.50 21.92 C ANISOU 1416 CA AILE A 198 3169 2062 3098 -4 179 349 C ATOM 1417 CB AILE A 198 -2.622 19.578 11.294 0.50 24.29 C ANISOU 1417 CB AILE A 198 3361 2689 3177 -15 7 251 C ATOM 1418 CG1AILE A 198 -2.089 18.685 10.169 0.50 26.28 C ANISOU 1418 CG1AILE A 198 3584 2977 3424 67 46 47 C ATOM 1419 CG2AILE A 198 -3.349 20.772 10.688 0.50 23.73 C ANISOU 1419 CG2AILE A 198 3242 2701 3069 -33 91 242 C ATOM 1420 CD1AILE A 198 -0.886 19.254 9.448 0.50 26.87 C ANISOU 1420 CD1AILE A 198 3371 3168 3667 61 -3 -57 C ATOM 1421 CA BILE A 198 -1.498 20.009 12.208 0.50 21.70 C ANISOU 1421 CA BILE A 198 3109 2068 3067 -24 149 335 C ATOM 1422 CB BILE A 198 -2.798 19.591 11.469 0.50 23.28 C ANISOU 1422 CB BILE A 198 3219 2617 3010 25 5 238 C ATOM 1423 CG1BILE A 198 -2.542 18.494 10.439 0.50 23.99 C ANISOU 1423 CG1BILE A 198 3265 2816 3033 123 -42 145 C ATOM 1424 CG2BILE A 198 -3.445 20.775 10.757 0.50 22.79 C ANISOU 1424 CG2BILE A 198 3100 2596 2963 -3 51 210 C ATOM 1425 CD1BILE A 198 -3.829 17.984 9.826 0.50 24.10 C ANISOU 1425 CD1BILE A 198 3283 2942 2929 82 13 -43 C ATOM 1426 N ARG A 199 -2.665 20.712 14.224 1.00 20.55 N ANISOU 1426 N ARG A 199 2747 2000 3058 238 1 243 N ATOM 1427 CA ARG A 199 -3.187 21.657 15.231 1.00 19.93 C ANISOU 1427 CA ARG A 199 2360 2483 2726 37 78 174 C ATOM 1428 C ARG A 199 -3.522 20.978 16.560 1.00 18.22 C ANISOU 1428 C ARG A 199 2130 2196 2594 149 -53 82 C ATOM 1429 O ARG A 199 -3.700 19.760 16.609 1.00 16.84 O ANISOU 1429 O ARG A 199 1701 2228 2469 81 155 189 O ATOM 1430 CB ARG A 199 -4.441 22.375 14.696 1.00 21.00 C ANISOU 1430 CB ARG A 199 2696 2444 2839 182 -78 226 C ATOM 1431 CG ARG A 199 -5.582 21.454 14.284 1.00 21.91 C ANISOU 1431 CG ARG A 199 2554 2758 3012 238 -308 296 C ATOM 1432 CD ARG A 199 -6.823 22.212 13.798 1.00 24.16 C ANISOU 1432 CD ARG A 199 2526 2841 3811 433 -9 482 C ATOM 1433 NE ARG A 199 -7.413 23.049 14.851 1.00 29.21 N ANISOU 1433 NE ARG A 199 3626 3247 4222 111 480 140 N ATOM 1434 CZ ARG A 199 -8.364 22.686 15.725 1.00 30.29 C ANISOU 1434 CZ ARG A 199 4280 2760 4469 -184 631 421 C ATOM 1435 NH1 ARG A 199 -8.911 21.460 15.733 1.00 29.45 N ANISOU 1435 NH1 ARG A 199 4580 2762 3847 -294 -8 217 N ATOM 1436 NH2 ARG A 199 -8.782 23.573 16.625 1.00 33.06 N ANISOU 1436 NH2 ARG A 199 5445 2677 4440 -2 509 368 N ATOM 1437 N VAL A 200 -3.617 21.779 17.624 1.00 17.48 N ANISOU 1437 N VAL A 200 2136 1873 2631 264 -20 177 N ATOM 1438 CA VAL A 200 -4.157 21.320 18.910 1.00 17.59 C ANISOU 1438 CA VAL A 200 2103 2052 2528 227 -45 59 C ATOM 1439 C VAL A 200 -5.680 21.485 18.900 1.00 16.75 C ANISOU 1439 C VAL A 200 2139 1655 2569 322 -88 220 C ATOM 1440 O VAL A 200 -6.207 22.591 18.721 1.00 19.39 O ANISOU 1440 O VAL A 200 2589 1822 2956 557 -94 417 O ATOM 1441 CB VAL A 200 -3.540 22.058 20.121 1.00 18.34 C ANISOU 1441 CB VAL A 200 2203 2121 2644 125 -40 -34 C ATOM 1442 CG1 VAL A 200 -4.283 21.722 21.409 1.00 18.38 C ANISOU 1442 CG1 VAL A 200 2320 2147 2515 97 -101 -106 C ATOM 1443 CG2 VAL A 200 -2.075 21.684 20.276 1.00 17.98 C ANISOU 1443 CG2 VAL A 200 2144 2094 2592 61 117 -20 C ATOM 1444 N HIS A 201 -6.363 20.366 19.120 1.00 16.41 N ANISOU 1444 N HIS A 201 1964 1883 2385 120 -165 97 N ATOM 1445 CA HIS A 201 -7.815 20.264 19.049 1.00 17.33 C ANISOU 1445 CA HIS A 201 1961 1940 2682 97 -223 120 C ATOM 1446 C HIS A 201 -8.457 20.559 20.423 1.00 17.08 C ANISOU 1446 C HIS A 201 2020 1786 2683 179 -250 168 C ATOM 1447 O HIS A 201 -9.450 21.294 20.507 1.00 17.81 O ANISOU 1447 O HIS A 201 2399 1421 2944 302 -125 233 O ATOM 1448 CB HIS A 201 -8.157 18.856 18.527 1.00 15.48 C ANISOU 1448 CB HIS A 201 1356 2176 2349 97 -191 -59 C ATOM 1449 CG HIS A 201 -9.620 18.544 18.463 1.00 17.32 C ANISOU 1449 CG HIS A 201 1344 2376 2860 159 -503 -119 C ATOM 1450 ND1 HIS A 201 -10.367 18.245 19.581 1.00 19.20 N ANISOU 1450 ND1 HIS A 201 1919 2505 2869 165 -429 -51 N ATOM 1451 CD2 HIS A 201 -10.454 18.411 17.407 1.00 18.54 C ANISOU 1451 CD2 HIS A 201 1871 2643 2527 82 -476 -192 C ATOM 1452 CE1 HIS A 201 -11.609 17.978 19.221 1.00 22.94 C ANISOU 1452 CE1 HIS A 201 2065 3049 3600 51 -721 -132 C ATOM 1453 NE2 HIS A 201 -11.687 18.068 17.905 1.00 21.29 N ANISOU 1453 NE2 HIS A 201 1122 3295 3673 334 -932 -127 N ATOM 1454 N THR A 202 -7.894 19.982 21.486 1.00 16.04 N ANISOU 1454 N THR A 202 1804 1527 2763 10 -296 191 N ATOM 1455 CA THR A 202 -8.417 20.132 22.853 1.00 17.07 C ANISOU 1455 CA THR A 202 2053 1586 2845 0 -209 26 C ATOM 1456 C THR A 202 -7.270 20.094 23.859 1.00 16.25 C ANISOU 1456 C THR A 202 1885 1700 2586 86 14 18 C ATOM 1457 O THR A 202 -6.339 19.284 23.703 1.00 18.38 O ANISOU 1457 O THR A 202 2392 1864 2727 484 171 265 O ATOM 1458 CB THR A 202 -9.422 19.007 23.217 1.00 17.70 C ANISOU 1458 CB THR A 202 1719 1998 3007 -28 -129 106 C ATOM 1459 OG1 THR A 202 -10.505 18.993 22.281 1.00 18.57 O ANISOU 1459 OG1 THR A 202 2216 1767 3072 -68 -417 -12 O ATOM 1460 CG2 THR A 202 -9.997 19.193 24.624 1.00 19.05 C ANISOU 1460 CG2 THR A 202 2120 2080 3038 126 -124 12 C ATOM 1461 N ILE A 203 -7.339 20.971 24.869 1.00 16.70 N ANISOU 1461 N ILE A 203 1966 1886 2492 60 71 -21 N ATOM 1462 CA ILE A 203 -6.473 20.914 26.062 1.00 16.94 C ANISOU 1462 CA ILE A 203 1902 1870 2662 17 -45 50 C ATOM 1463 C ILE A 203 -7.315 20.866 27.343 1.00 15.67 C ANISOU 1463 C ILE A 203 2213 1484 2257 -9 -272 156 C ATOM 1464 O ILE A 203 -8.278 21.644 27.510 1.00 15.39 O ANISOU 1464 O ILE A 203 2061 1326 2459 -148 -107 331 O ATOM 1465 CB ILE A 203 -5.512 22.122 26.155 1.00 18.17 C ANISOU 1465 CB ILE A 203 2426 1795 2682 -98 -68 -95 C ATOM 1466 CG1 ILE A 203 -4.586 22.160 24.936 1.00 19.36 C ANISOU 1466 CG1 ILE A 203 2447 2080 2830 192 69 -164 C ATOM 1467 CG2 ILE A 203 -4.688 22.062 27.445 1.00 19.00 C ANISOU 1467 CG2 ILE A 203 2651 1919 2650 -136 -96 5 C ATOM 1468 CD1 ILE A 203 -3.787 23.441 24.795 1.00 21.00 C ANISOU 1468 CD1 ILE A 203 2461 2382 3135 -9 93 -128 C ATOM 1469 N VAL A 204 -6.943 19.946 28.236 1.00 15.08 N ANISOU 1469 N VAL A 204 1919 1448 2361 92 -401 86 N ATOM 1470 CA VAL A 204 -7.484 19.867 29.598 1.00 15.93 C ANISOU 1470 CA VAL A 204 1977 1558 2518 219 -184 130 C ATOM 1471 C VAL A 204 -6.372 20.214 30.576 1.00 16.08 C ANISOU 1471 C VAL A 204 2160 1567 2381 165 -186 92 C ATOM 1472 O VAL A 204 -5.267 19.708 30.429 1.00 15.35 O ANISOU 1472 O VAL A 204 1834 1477 2519 -144 -324 157 O ATOM 1473 CB VAL A 204 -7.980 18.447 29.948 1.00 16.22 C ANISOU 1473 CB VAL A 204 2090 1683 2386 169 -89 236 C ATOM 1474 CG1 VAL A 204 -8.657 18.427 31.318 1.00 17.18 C ANISOU 1474 CG1 VAL A 204 2203 1922 2400 333 -51 141 C ATOM 1475 CG2 VAL A 204 -8.924 17.913 28.875 1.00 17.18 C ANISOU 1475 CG2 VAL A 204 2192 1998 2338 282 -200 180 C ATOM 1476 N ILE A 205 -6.666 21.066 31.561 1.00 16.87 N ANISOU 1476 N ILE A 205 2262 1572 2576 -63 -132 -59 N ATOM 1477 CA ILE A 205 -5.788 21.258 32.726 1.00 16.91 C ANISOU 1477 CA ILE A 205 2103 1605 2714 83 -183 -14 C ATOM 1478 C ILE A 205 -6.627 21.245 34.001 1.00 15.63 C ANISOU 1478 C ILE A 205 2000 1209 2726 69 -209 -37 C ATOM 1479 O ILE A 205 -7.594 22.005 34.115 1.00 15.45 O ANISOU 1479 O ILE A 205 1899 1193 2777 13 -137 -80 O ATOM 1480 CB ILE A 205 -4.974 22.581 32.660 1.00 16.18 C ANISOU 1480 CB ILE A 205 1939 1611 2597 132 -131 -116 C ATOM 1481 CG1 ILE A 205 -4.137 22.622 31.384 1.00 16.56 C ANISOU 1481 CG1 ILE A 205 2017 1709 2565 96 -83 -8 C ATOM 1482 CG2 ILE A 205 -4.092 22.747 33.906 1.00 15.95 C ANISOU 1482 CG2 ILE A 205 1711 1446 2903 -364 -198 -94 C ATOM 1483 CD1 ILE A 205 -3.218 23.821 31.262 1.00 17.34 C ANISOU 1483 CD1 ILE A 205 1943 2041 2603 -79 33 -137 C ATOM 1484 N SER A 206 -6.241 20.387 34.947 1.00 15.22 N ANISOU 1484 N SER A 206 1983 1117 2679 -108 -180 -10 N ATOM 1485 CA SER A 206 -6.770 20.403 36.313 1.00 16.06 C ANISOU 1485 CA SER A 206 2117 1353 2630 -80 -157 23 C ATOM 1486 C SER A 206 -5.606 20.536 37.288 1.00 15.81 C ANISOU 1486 C SER A 206 2030 1562 2413 93 -17 115 C ATOM 1487 O SER A 206 -4.652 19.752 37.231 1.00 15.43 O ANISOU 1487 O SER A 206 2276 1361 2225 164 10 -43 O ATOM 1488 CB SER A 206 -7.556 19.128 36.609 1.00 14.97 C ANISOU 1488 CB SER A 206 1971 1475 2239 -121 -269 57 C ATOM 1489 OG SER A 206 -8.731 19.077 35.819 1.00 14.93 O ANISOU 1489 OG SER A 206 1573 1309 2788 -249 -169 -124 O ATOM 1490 N VAL A 207 -5.675 21.521 38.181 1.00 15.82 N ANISOU 1490 N VAL A 207 1832 1727 2452 -81 238 31 N ATOM 1491 CA VAL A 207 -4.611 21.720 39.158 1.00 17.56 C ANISOU 1491 CA VAL A 207 2254 1813 2604 -96 2 15 C ATOM 1492 C VAL A 207 -5.176 22.106 40.525 1.00 16.88 C ANISOU 1492 C VAL A 207 2071 1724 2618 -19 83 196 C ATOM 1493 O VAL A 207 -6.080 22.933 40.619 1.00 16.83 O ANISOU 1493 O VAL A 207 2390 1305 2697 -48 283 345 O ATOM 1494 CB VAL A 207 -3.569 22.744 38.648 1.00 19.32 C ANISOU 1494 CB VAL A 207 2346 2057 2935 -154 278 61 C ATOM 1495 CG1 VAL A 207 -4.195 24.114 38.372 1.00 17.42 C ANISOU 1495 CG1 VAL A 207 1912 1872 2836 -310 32 -306 C ATOM 1496 CG2 VAL A 207 -2.394 22.846 39.617 1.00 18.65 C ANISOU 1496 CG2 VAL A 207 1385 1903 3798 -1064 704 559 C ATOM 1497 N GLN A 208 -4.647 21.474 41.572 1.00 15.58 N ANISOU 1497 N GLN A 208 1936 1364 2619 -18 148 142 N ATOM 1498 CA GLN A 208 -4.987 21.805 42.961 1.00 15.57 C ANISOU 1498 CA GLN A 208 1962 1398 2556 8 47 85 C ATOM 1499 C GLN A 208 -4.674 23.279 43.287 1.00 15.34 C ANISOU 1499 C GLN A 208 1992 1339 2497 99 159 109 C ATOM 1500 O GLN A 208 -3.652 23.820 42.850 1.00 15.23 O ANISOU 1500 O GLN A 208 1926 1247 2613 36 -46 288 O ATOM 1501 CB GLN A 208 -4.236 20.880 43.928 1.00 15.43 C ANISOU 1501 CB GLN A 208 1781 1697 2383 203 46 -67 C ATOM 1502 CG GLN A 208 -4.707 20.953 45.380 1.00 16.28 C ANISOU 1502 CG GLN A 208 2110 1809 2266 189 -88 29 C ATOM 1503 CD GLN A 208 -3.779 20.253 46.365 1.00 17.32 C ANISOU 1503 CD GLN A 208 2353 1989 2238 377 -78 48 C ATOM 1504 OE1 GLN A 208 -2.714 19.734 46.000 1.00 16.96 O ANISOU 1504 OE1 GLN A 208 2549 1394 2499 442 0 41 O ATOM 1505 NE2 GLN A 208 -4.186 20.235 47.628 1.00 17.93 N ANISOU 1505 NE2 GLN A 208 2417 2161 2231 272 -45 103 N ATOM 1506 N HIS A 209 -5.547 23.913 44.070 1.00 15.77 N ANISOU 1506 N HIS A 209 1895 1493 2602 73 257 164 N ATOM 1507 CA HIS A 209 -5.448 25.348 44.315 1.00 15.62 C ANISOU 1507 CA HIS A 209 1800 1624 2510 -177 -57 -43 C ATOM 1508 C HIS A 209 -5.898 25.741 45.716 1.00 17.03 C ANISOU 1508 C HIS A 209 2024 1967 2477 -204 30 104 C ATOM 1509 O HIS A 209 -6.619 25.001 46.377 1.00 16.67 O ANISOU 1509 O HIS A 209 2466 1394 2472 -299 282 -289 O ATOM 1510 CB HIS A 209 -6.265 26.109 43.265 1.00 15.98 C ANISOU 1510 CB HIS A 209 1872 1987 2212 -296 90 122 C ATOM 1511 CG HIS A 209 -7.734 25.815 43.309 1.00 16.77 C ANISOU 1511 CG HIS A 209 1860 2240 2272 -342 -6 159 C ATOM 1512 ND1 HIS A 209 -8.600 26.483 44.144 1.00 17.57 N ANISOU 1512 ND1 HIS A 209 2000 2384 2291 -509 50 17 N ATOM 1513 CD2 HIS A 209 -8.490 24.937 42.610 1.00 16.83 C ANISOU 1513 CD2 HIS A 209 2000 2110 2282 -183 63 1 C ATOM 1514 CE1 HIS A 209 -9.825 26.018 43.972 1.00 17.79 C ANISOU 1514 CE1 HIS A 209 1909 2590 2257 -388 10 -153 C ATOM 1515 NE2 HIS A 209 -9.784 25.081 43.045 1.00 16.97 N ANISOU 1515 NE2 HIS A 209 1915 2262 2268 -539 53 0 N ATOM 1516 N ASP A 210 -5.481 26.926 46.165 1.00 19.56 N ANISOU 1516 N ASP A 210 2429 2188 2812 -312 -267 -27 N ATOM 1517 C ASP A 210 -7.343 27.896 47.438 1.00 21.61 C ANISOU 1517 C ASP A 210 2469 2335 3405 203 -318 -173 C ATOM 1518 O ASP A 210 -7.890 28.151 46.361 1.00 19.47 O ANISOU 1518 O ASP A 210 2075 2242 3079 560 89 -334 O ATOM 1519 CA ASP A 210 -5.897 27.401 47.482 0.75 21.09 C ANISOU 1519 CA ASP A 210 2581 2345 3087 402 -274 -276 C ATOM 1520 CB ASP A 210 -4.896 28.414 48.069 0.75 25.89 C ANISOU 1520 CB ASP A 210 3228 3215 3394 22 -399 -785 C ATOM 1521 CG ASP A 210 -5.042 29.823 47.526 0.75 29.00 C ANISOU 1521 CG ASP A 210 4651 2985 3383 -456 -805 -1101 C ATOM 1522 OD1 ASP A 210 -5.748 30.074 46.531 0.75 30.02 O ANISOU 1522 OD1 ASP A 210 4706 4061 2638 -307 -145 -880 O ATOM 1523 OD2 ASP A 210 -4.416 30.712 48.126 0.75 42.05 O ANISOU 1523 OD2 ASP A 210 7996 2982 4997 512 -2356 -2777 O ATOM 1524 N GLU A 211 -7.939 28.011 48.619 1.00 23.56 N ANISOU 1524 N GLU A 211 2686 2572 3694 933 3 67 N ATOM 1525 CA GLU A 211 -9.355 28.369 48.781 1.00 31.51 C ANISOU 1525 CA GLU A 211 3017 3505 5449 1410 247 -257 C ATOM 1526 C GLU A 211 -9.708 29.748 48.247 1.00 31.90 C ANISOU 1526 C GLU A 211 4358 3427 4333 926 512 -60 C ATOM 1527 O GLU A 211 -10.844 29.982 47.835 1.00 39.99 O ANISOU 1527 O GLU A 211 5027 5317 4849 1213 -8 877 O ATOM 1528 CB GLU A 211 -9.749 28.306 50.266 1.00 35.74 C ANISOU 1528 CB GLU A 211 4466 3401 5711 2914 701 -232 C ATOM 1529 CG GLU A 211 -10.263 26.949 50.705 0.50 28.55 C ANISOU 1529 CG GLU A 211 4666 2885 3295 2901 623 -1002 C ATOM 1530 CD GLU A 211 -11.753 26.776 50.464 0.50 28.35 C ANISOU 1530 CD GLU A 211 4801 2935 3034 814 724 13 C ATOM 1531 OE1 GLU A 211 -12.300 27.348 49.495 0.50 28.41 O ANISOU 1531 OE1 GLU A 211 4583 3085 3126 53 188 -7 O ATOM 1532 OE2 GLU A 211 -12.386 26.057 51.259 0.50 30.99 O ANISOU 1532 OE2 GLU A 211 4889 2806 4077 -808 243 -300 O ATOM 1533 N GLU A 212 -8.728 30.645 48.245 1.00 29.90 N ANISOU 1533 N GLU A 212 3798 4181 3380 791 -152 -384 N ATOM 1534 CA GLU A 212 -8.965 32.072 48.081 1.00 31.98 C ANISOU 1534 CA GLU A 212 4845 4189 3114 1097 -33 -584 C ATOM 1535 C GLU A 212 -9.133 32.522 46.623 1.00 27.47 C ANISOU 1535 C GLU A 212 4225 3216 2995 1529 251 -820 C ATOM 1536 O GLU A 212 -9.830 33.495 46.366 1.00 32.28 O ANISOU 1536 O GLU A 212 5072 3209 3981 1372 -87 274 O ATOM 1537 CB GLU A 212 -7.824 32.864 48.736 1.00 36.63 C ANISOU 1537 CB GLU A 212 5235 4736 3947 837 -469 -684 C ATOM 1538 CG GLU A 212 -7.493 32.472 50.178 1.00 42.68 C ANISOU 1538 CG GLU A 212 6664 5674 3878 239 -430 -605 C ATOM 1539 CD GLU A 212 -8.525 32.938 51.186 0.50 41.68 C ANISOU 1539 CD GLU A 212 7332 4814 3687 -967 -314 -1878 C ATOM 1540 OE1 GLU A 212 -9.686 32.482 51.125 0.50 45.23 O ANISOU 1540 OE1 GLU A 212 7757 4527 4901 -1460 -615 -1451 O ATOM 1541 OE2 GLU A 212 -8.164 33.764 52.045 0.50 44.50 O ANISOU 1541 OE2 GLU A 212 7915 5008 3984 -231 -526 -2444 O ATOM 1542 N VAL A 213 -8.492 31.834 45.682 1.00 26.08 N ANISOU 1542 N VAL A 213 3874 2335 3700 2551 -66 -501 N ATOM 1543 CA VAL A 213 -8.569 32.221 44.259 1.00 26.94 C ANISOU 1543 CA VAL A 213 3499 3040 3696 783 -128 -248 C ATOM 1544 C VAL A 213 -9.880 31.738 43.615 1.00 25.99 C ANISOU 1544 C VAL A 213 3296 2812 3765 1022 -134 -187 C ATOM 1545 O VAL A 213 -10.323 30.616 43.873 1.00 24.79 O ANISOU 1545 O VAL A 213 2275 3031 4112 977 -494 18 O ATOM 1546 CB VAL A 213 -7.328 31.731 43.466 1.00 23.59 C ANISOU 1546 CB VAL A 213 3175 2418 3367 295 -161 -225 C ATOM 1547 CG1 VAL A 213 -7.288 30.203 43.338 1.00 21.59 C ANISOU 1547 CG1 VAL A 213 3024 2385 2792 59 20 -66 C ATOM 1548 CG2 VAL A 213 -7.269 32.385 42.092 1.00 23.18 C ANISOU 1548 CG2 VAL A 213 2483 2722 3601 64 61 16 C ATOM 1549 N CYS A 214 -10.503 32.578 42.785 1.00 24.79 N ANISOU 1549 N CYS A 214 2996 2721 3700 876 8 -167 N ATOM 1550 CA CYS A 214 -11.740 32.176 42.107 1.00 22.87 C ANISOU 1550 CA CYS A 214 2492 2683 3513 1699 21 122 C ATOM 1551 C CYS A 214 -11.452 31.509 40.765 1.00 22.02 C ANISOU 1551 C CYS A 214 2301 2473 3590 1116 134 74 C ATOM 1552 O CYS A 214 -10.352 31.616 40.212 1.00 23.48 O ANISOU 1552 O CYS A 214 2754 2460 3707 1109 586 149 O ATOM 1553 CB CYS A 214 -12.702 33.356 41.929 1.00 20.22 C ANISOU 1553 CB CYS A 214 1946 2546 3189 1396 158 178 C ATOM 1554 SG CYS A 214 -12.271 34.491 40.597 0.75 22.14 S ANISOU 1554 SG CYS A 214 2689 2117 3605 1130 404 202 S ATOM 1555 N LEU A 215 -12.481 30.842 40.252 1.00 21.79 N ANISOU 1555 N LEU A 215 2561 2164 3551 865 223 91 N ATOM 1556 CA LEU A 215 -12.397 30.030 39.054 1.00 19.30 C ANISOU 1556 CA LEU A 215 1882 1715 3736 1070 145 119 C ATOM 1557 C LEU A 215 -12.033 30.825 37.795 1.00 19.61 C ANISOU 1557 C LEU A 215 1860 2030 3560 218 330 -210 C ATOM 1558 O LEU A 215 -11.233 30.372 36.988 1.00 19.24 O ANISOU 1558 O LEU A 215 1933 1731 3646 467 404 151 O ATOM 1559 CB LEU A 215 -13.732 29.307 38.858 1.00 25.34 C ANISOU 1559 CB LEU A 215 2763 2541 4324 154 -230 438 C ATOM 1560 CG LEU A 215 -13.835 28.206 37.818 1.00 28.85 C ANISOU 1560 CG LEU A 215 3485 3002 4473 755 -424 160 C ATOM 1561 CD1 LEU A 215 -12.890 27.054 38.123 1.00 26.84 C ANISOU 1561 CD1 LEU A 215 3321 2598 4279 321 -300 555 C ATOM 1562 CD2 LEU A 215 -15.279 27.724 37.794 1.00 36.02 C ANISOU 1562 CD2 LEU A 215 3016 2175 8494 1783 -1101 1147 C ATOM 1563 N ASP A 216 -12.623 32.005 37.633 1.00 17.62 N ANISOU 1563 N ASP A 216 1398 2287 3009 546 1388 -579 N ATOM 1564 CA ASP A 216 -12.319 32.868 36.492 1.00 18.15 C ANISOU 1564 CA ASP A 216 1928 2055 2913 318 386 -378 C ATOM 1565 C ASP A 216 -10.853 33.342 36.476 1.00 17.58 C ANISOU 1565 C ASP A 216 1822 1909 2949 478 272 -185 C ATOM 1566 O ASP A 216 -10.225 33.352 35.423 1.00 17.25 O ANISOU 1566 O ASP A 216 1771 2010 2770 349 100 -45 O ATOM 1567 CB ASP A 216 -13.286 34.056 36.447 1.00 19.96 C ANISOU 1567 CB ASP A 216 2362 2335 2883 656 377 -239 C ATOM 1568 CG ASP A 216 -14.696 33.645 36.041 1.00 22.79 C ANISOU 1568 CG ASP A 216 2741 2380 3538 249 287 -567 C ATOM 1569 OD1 ASP A 216 -14.893 33.285 34.868 1.00 26.56 O ANISOU 1569 OD1 ASP A 216 3419 2891 3779 173 -16 -762 O ATOM 1570 OD2 ASP A 216 -15.617 33.700 36.875 1.00 26.59 O ANISOU 1570 OD2 ASP A 216 2591 3065 4446 -206 657 -11 O ATOM 1571 N GLU A 217 -10.305 33.713 37.631 1.00 17.30 N ANISOU 1571 N GLU A 217 1693 1788 3090 241 196 -135 N ATOM 1572 CA GLU A 217 -8.872 34.067 37.708 1.00 17.35 C ANISOU 1572 CA GLU A 217 1709 1837 3043 190 202 101 C ATOM 1573 C GLU A 217 -7.986 32.864 37.334 1.00 17.24 C ANISOU 1573 C GLU A 217 2102 1503 2944 56 204 -30 C ATOM 1574 O GLU A 217 -7.029 33.004 36.565 1.00 18.31 O ANISOU 1574 O GLU A 217 2584 1387 2984 170 486 221 O ATOM 1575 CB GLU A 217 -8.497 34.609 39.094 1.00 21.09 C ANISOU 1575 CB GLU A 217 2481 2230 3300 31 84 -194 C ATOM 1576 CG GLU A 217 -7.061 35.138 39.179 1.00 24.63 C ANISOU 1576 CG GLU A 217 2475 2978 3906 28 -63 -517 C ATOM 1577 CD GLU A 217 -6.735 35.860 40.481 0.25 21.13 C ANISOU 1577 CD GLU A 217 1838 2352 3837 103 164 -421 C ATOM 1578 OE1 GLU A 217 -7.636 36.461 41.104 0.25 19.10 O ANISOU 1578 OE1 GLU A 217 1090 2106 4058 -220 -45 -412 O ATOM 1579 OE2 GLU A 217 -5.552 35.842 40.877 0.25 19.45 O ANISOU 1579 OE2 GLU A 217 1669 1919 3799 106 388 -455 O ATOM 1580 N MET A 218 -8.315 31.685 37.858 1.00 16.77 N ANISOU 1580 N MET A 218 2078 1205 3088 437 380 -123 N ATOM 1581 CA MET A 218 -7.564 30.469 37.516 1.00 17.99 C ANISOU 1581 CA MET A 218 2316 1309 3208 481 211 -489 C ATOM 1582 C MET A 218 -7.598 30.168 36.016 1.00 16.60 C ANISOU 1582 C MET A 218 1705 1672 2927 126 86 -3 C ATOM 1583 O MET A 218 -6.551 29.934 35.418 1.00 16.52 O ANISOU 1583 O MET A 218 1814 1620 2842 -32 270 5 O ATOM 1584 CB MET A 218 -8.057 29.253 38.317 1.00 23.29 C ANISOU 1584 CB MET A 218 3189 831 4826 871 997 -399 C ATOM 1585 CG MET A 218 -7.715 29.338 39.796 1.00 22.50 C ANISOU 1585 CG MET A 218 2671 1095 4781 858 1810 -578 C ATOM 1586 SD MET A 218 -8.003 27.794 40.680 1.00 19.73 S ANISOU 1586 SD MET A 218 2208 1988 3298 630 201 199 S ATOM 1587 CE MET A 218 -9.784 27.839 40.822 1.00 20.30 C ANISOU 1587 CE MET A 218 2182 2720 2809 258 77 126 C ATOM 1588 N AARG A 219 -8.785 30.189 35.414 0.50 15.82 N ANISOU 1588 N AARG A 219 1766 1591 2654 58 39 137 N ATOM 1589 CA AARG A 219 -8.921 29.862 33.993 0.50 16.23 C ANISOU 1589 CA AARG A 219 1723 1766 2675 -42 -155 90 C ATOM 1590 C AARG A 219 -8.227 30.879 33.078 0.50 17.21 C ANISOU 1590 C AARG A 219 1920 1786 2831 -81 -112 131 C ATOM 1591 O AARG A 219 -7.617 30.499 32.071 0.50 16.74 O ANISOU 1591 O AARG A 219 1951 1696 2711 -32 -359 14 O ATOM 1592 CB AARG A 219 -10.396 29.692 33.631 0.50 14.39 C ANISOU 1592 CB AARG A 219 1726 1650 2090 -43 -75 129 C ATOM 1593 CG AARG A 219 -10.997 28.470 34.300 0.50 13.62 C ANISOU 1593 CG AARG A 219 1846 1456 1872 103 -146 106 C ATOM 1594 CD AARG A 219 -12.504 28.419 34.184 0.50 13.19 C ANISOU 1594 CD AARG A 219 1827 1192 1992 106 -51 225 C ATOM 1595 NE AARG A 219 -12.986 27.102 34.559 0.50 13.46 N ANISOU 1595 NE AARG A 219 1823 924 2365 469 -51 294 N ATOM 1596 CZ AARG A 219 -14.261 26.787 34.734 0.50 14.51 C ANISOU 1596 CZ AARG A 219 1758 1096 2660 519 -98 452 C ATOM 1597 NH1AARG A 219 -15.201 27.711 34.578 0.50 13.79 N ANISOU 1597 NH1AARG A 219 1674 791 2772 454 243 112 N ATOM 1598 NH2AARG A 219 -14.596 25.548 35.076 0.50 14.82 N ANISOU 1598 NH2AARG A 219 1686 1217 2725 439 -95 601 N ATOM 1599 N BARG A 219 -8.795 30.173 35.424 0.50 17.08 N ANISOU 1599 N BARG A 219 1751 1812 2926 130 18 135 N ATOM 1600 CA BARG A 219 -8.956 29.869 33.996 0.50 18.67 C ANISOU 1600 CA BARG A 219 1960 2152 2982 53 -77 29 C ATOM 1601 C BARG A 219 -8.208 30.871 33.103 0.50 18.87 C ANISOU 1601 C BARG A 219 2126 1884 3159 71 -33 -11 C ATOM 1602 O BARG A 219 -7.552 30.472 32.133 0.50 18.94 O ANISOU 1602 O BARG A 219 2193 1761 3243 183 -143 -184 O ATOM 1603 CB BARG A 219 -10.438 29.822 33.604 0.50 19.44 C ANISOU 1603 CB BARG A 219 2012 2632 2742 155 -104 8 C ATOM 1604 CG BARG A 219 -11.176 28.549 34.004 0.50 20.54 C ANISOU 1604 CG BARG A 219 2534 2612 2655 76 -26 -34 C ATOM 1605 CD BARG A 219 -12.600 28.606 33.476 0.50 23.12 C ANISOU 1605 CD BARG A 219 2558 3225 2999 0 -75 -27 C ATOM 1606 NE BARG A 219 -13.108 29.954 33.689 0.50 26.31 N ANISOU 1606 NE BARG A 219 3125 3466 3402 439 27 158 N ATOM 1607 CZ BARG A 219 -12.943 30.973 32.848 0.50 23.58 C ANISOU 1607 CZ BARG A 219 2821 2799 3339 522 115 -233 C ATOM 1608 NH1BARG A 219 -12.324 30.812 31.693 0.50 28.17 N ANISOU 1608 NH1BARG A 219 3500 4271 2931 259 62 390 N ATOM 1609 NH2BARG A 219 -13.428 32.152 33.166 0.50 19.36 N ANISOU 1609 NH2BARG A 219 2102 2435 2816 485 -104 389 N ATOM 1610 N ASP A 220 -8.295 32.159 33.451 1.00 17.65 N ANISOU 1610 N ASP A 220 1821 1883 3002 101 59 -16 N ATOM 1611 CA ASP A 220 -7.557 33.221 32.758 1.00 17.39 C ANISOU 1611 CA ASP A 220 1550 2236 2821 11 -23 42 C ATOM 1612 C ASP A 220 -6.035 32.987 32.815 1.00 17.57 C ANISOU 1612 C ASP A 220 1531 1997 3148 -21 95 151 C ATOM 1613 O ASP A 220 -5.380 33.053 31.791 1.00 17.32 O ANISOU 1613 O ASP A 220 1390 2064 3124 152 22 280 O ATOM 1614 CB ASP A 220 -7.891 34.593 33.357 1.00 19.05 C ANISOU 1614 CB ASP A 220 2087 2272 2879 -60 83 23 C ATOM 1615 CG ASP A 220 -7.220 35.734 32.616 1.00 23.02 C ANISOU 1615 CG ASP A 220 2444 2620 3680 -278 0 456 C ATOM 1616 OD1 ASP A 220 -7.513 35.930 31.422 1.00 27.05 O ANISOU 1616 OD1 ASP A 220 3346 3016 3912 -266 -280 815 O ATOM 1617 OD2 ASP A 220 -6.382 36.428 33.221 1.00 28.79 O ANISOU 1617 OD2 ASP A 220 3217 2714 5006 -1347 80 542 O ATOM 1618 N ALA A 221 -5.505 32.688 34.005 1.00 19.22 N ANISOU 1618 N ALA A 221 2378 1835 3087 -266 98 307 N ATOM 1619 CA ALA A 221 -4.064 32.387 34.188 1.00 18.27 C ANISOU 1619 CA ALA A 221 2079 1389 3473 -1103 466 681 C ATOM 1620 C ALA A 221 -3.617 31.125 33.460 1.00 17.78 C ANISOU 1620 C ALA A 221 1937 1997 2820 -343 91 519 C ATOM 1621 O ALA A 221 -2.530 31.099 32.868 1.00 17.26 O ANISOU 1621 O ALA A 221 2089 1807 2661 -6 142 73 O ATOM 1622 CB ALA A 221 -3.725 32.251 35.666 1.00 20.32 C ANISOU 1622 CB ALA A 221 2315 2079 3326 -294 176 79 C ATOM 1623 N LEU A 222 -4.442 30.078 33.515 1.00 16.80 N ANISOU 1623 N LEU A 222 1824 1648 2909 -71 137 266 N ATOM 1624 CA LEU A 222 -4.121 28.831 32.828 1.00 17.93 C ANISOU 1624 CA LEU A 222 2207 1855 2749 18 68 139 C ATOM 1625 C LEU A 222 -4.001 29.032 31.308 1.00 16.52 C ANISOU 1625 C LEU A 222 1845 1687 2743 187 219 53 C ATOM 1626 O LEU A 222 -3.121 28.453 30.680 1.00 18.80 O ANISOU 1626 O LEU A 222 2274 2084 2783 480 362 12 O ATOM 1627 CB LEU A 222 -5.132 27.725 33.181 1.00 19.12 C ANISOU 1627 CB LEU A 222 2422 1909 2933 25 344 199 C ATOM 1628 CG LEU A 222 -5.074 27.183 34.617 1.00 20.76 C ANISOU 1628 CG LEU A 222 2753 2237 2897 322 195 161 C ATOM 1629 CD1 LEU A 222 -6.211 26.191 34.863 1.00 21.08 C ANISOU 1629 CD1 LEU A 222 2719 2378 2913 260 110 58 C ATOM 1630 CD2 LEU A 222 -3.727 26.556 34.945 1.00 20.67 C ANISOU 1630 CD2 LEU A 222 2563 2463 2826 186 241 163 C ATOM 1631 N LYS A 223 -4.846 29.883 30.730 1.00 16.86 N ANISOU 1631 N LYS A 223 1706 1665 3034 164 150 22 N ATOM 1632 CA LYS A 223 -4.765 30.180 29.299 1.00 18.53 C ANISOU 1632 CA LYS A 223 2074 1832 3133 208 248 126 C ATOM 1633 C LYS A 223 -3.550 31.067 28.979 1.00 19.29 C ANISOU 1633 C LYS A 223 2249 1853 3226 185 486 161 C ATOM 1634 O LYS A 223 -2.719 30.709 28.138 1.00 20.52 O ANISOU 1634 O LYS A 223 2533 1750 3512 722 591 235 O ATOM 1635 CB LYS A 223 -6.062 30.814 28.788 1.00 22.74 C ANISOU 1635 CB LYS A 223 2364 2628 3647 622 118 124 C ATOM 1636 CG LYS A 223 -6.351 30.516 27.322 1.00 30.12 C ANISOU 1636 CG LYS A 223 3595 3710 4136 296 -561 -178 C ATOM 1637 CD LYS A 223 -7.676 31.126 26.866 1.00 32.07 C ANISOU 1637 CD LYS A 223 3673 3517 4992 518 -582 -503 C ATOM 1638 CE LYS A 223 -8.550 30.131 26.113 0.50 33.23 C ANISOU 1638 CE LYS A 223 3966 3820 4838 485 -487 -828 C ATOM 1639 NZ LYS A 223 -9.946 30.626 25.968 0.50 31.96 N ANISOU 1639 NZ LYS A 223 4173 3299 4670 749 -372 -756 N ATOM 1640 N GLU A 224 -3.428 32.193 29.683 1.00 19.55 N ANISOU 1640 N GLU A 224 2420 1835 3172 269 315 218 N ATOM 1641 CA GLU A 224 -2.438 33.226 29.324 1.00 19.59 C ANISOU 1641 CA GLU A 224 2342 2265 2833 186 223 449 C ATOM 1642 C GLU A 224 -1.002 32.941 29.762 1.00 20.10 C ANISOU 1642 C GLU A 224 2221 2347 3068 27 233 280 C ATOM 1643 O GLU A 224 -0.074 33.206 29.000 1.00 23.54 O ANISOU 1643 O GLU A 224 2995 3162 2787 -322 401 512 O ATOM 1644 CB GLU A 224 -2.897 34.605 29.826 1.00 23.04 C ANISOU 1644 CB GLU A 224 2968 2592 3192 562 427 325 C ATOM 1645 CG GLU A 224 -4.219 35.051 29.208 1.00 28.49 C ANISOU 1645 CG GLU A 224 3313 3449 4062 785 77 502 C ATOM 1646 CD GLU A 224 -4.176 35.149 27.686 0.75 31.96 C ANISOU 1646 CD GLU A 224 4409 3651 4080 633 114 553 C ATOM 1647 OE1 GLU A 224 -3.298 35.863 27.159 0.75 35.81 O ANISOU 1647 OE1 GLU A 224 5626 3728 4251 553 657 1008 O ATOM 1648 OE2 GLU A 224 -5.018 34.512 27.016 0.75 30.39 O ANISOU 1648 OE2 GLU A 224 4513 3408 3624 559 42 990 O ATOM 1649 N LYS A 225 -0.823 32.407 30.968 1.00 20.12 N ANISOU 1649 N LYS A 225 2724 1796 3121 -141 104 214 N ATOM 1650 CA LYS A 225 0.507 32.180 31.541 1.00 21.18 C ANISOU 1650 CA LYS A 225 2643 1819 3583 -244 48 67 C ATOM 1651 C LYS A 225 1.020 30.738 31.434 1.00 19.40 C ANISOU 1651 C LYS A 225 2231 1962 3178 -166 5 -108 C ATOM 1652 O LYS A 225 2.218 30.514 31.570 1.00 20.51 O ANISOU 1652 O LYS A 225 1931 2279 3583 -727 158 105 O ATOM 1653 CB LYS A 225 0.530 32.643 33.001 1.00 24.51 C ANISOU 1653 CB LYS A 225 2697 2807 3806 -124 75 -332 C ATOM 1654 CG LYS A 225 0.339 34.147 33.141 1.00 30.53 C ANISOU 1654 CG LYS A 225 3762 2978 4860 149 -4 -578 C ATOM 1655 CD LYS A 225 0.428 34.609 34.589 1.00 37.08 C ANISOU 1655 CD LYS A 225 4893 4254 4939 279 35 -692 C ATOM 1656 CE LYS A 225 0.107 36.091 34.733 0.50 39.55 C ANISOU 1656 CE LYS A 225 5083 4138 5803 217 -136 -530 C ATOM 1657 NZ LYS A 225 0.967 36.953 33.876 0.50 39.16 N ANISOU 1657 NZ LYS A 225 4904 4166 5809 193 -240 -604 N ATOM 1658 N VAL A 226 0.137 29.768 31.193 1.00 19.54 N ANISOU 1658 N VAL A 226 2432 1898 3091 -318 147 71 N ATOM 1659 CA VAL A 226 0.556 28.366 31.081 1.00 19.62 C ANISOU 1659 CA VAL A 226 2385 2031 3037 -55 -54 129 C ATOM 1660 C VAL A 226 0.495 27.891 29.624 1.00 18.90 C ANISOU 1660 C VAL A 226 2140 2044 2997 164 -85 216 C ATOM 1661 O VAL A 226 1.536 27.650 29.015 1.00 19.52 O ANISOU 1661 O VAL A 226 2401 2048 2966 -59 345 481 O ATOM 1662 CB VAL A 226 -0.261 27.452 32.022 1.00 18.63 C ANISOU 1662 CB VAL A 226 2281 1971 2823 31 -95 66 C ATOM 1663 CG1 VAL A 226 0.218 26.007 31.932 1.00 18.92 C ANISOU 1663 CG1 VAL A 226 2628 1788 2772 -169 -215 -26 C ATOM 1664 CG2 VAL A 226 -0.176 27.967 33.457 1.00 17.60 C ANISOU 1664 CG2 VAL A 226 2063 1810 2815 -318 -140 133 C ATOM 1665 N ILE A 227 -0.714 27.777 29.066 1.00 18.82 N ANISOU 1665 N ILE A 227 1924 2146 3080 199 60 274 N ATOM 1666 CA ILE A 227 -0.898 27.285 27.683 1.00 18.04 C ANISOU 1666 CA ILE A 227 1752 2087 3013 170 232 277 C ATOM 1667 C ILE A 227 -0.160 28.153 26.645 1.00 18.85 C ANISOU 1667 C ILE A 227 2122 2205 2833 216 319 310 C ATOM 1668 O ILE A 227 0.640 27.644 25.848 1.00 17.60 O ANISOU 1668 O ILE A 227 2157 1735 2793 9 314 243 O ATOM 1669 CB ILE A 227 -2.393 27.147 27.302 1.00 16.84 C ANISOU 1669 CB ILE A 227 1788 1986 2621 70 193 210 C ATOM 1670 CG1 ILE A 227 -3.044 26.032 28.133 1.00 17.12 C ANISOU 1670 CG1 ILE A 227 1774 2247 2483 -35 218 217 C ATOM 1671 CG2 ILE A 227 -2.548 26.843 25.812 1.00 17.35 C ANISOU 1671 CG2 ILE A 227 1849 2140 2601 25 308 188 C ATOM 1672 CD1 ILE A 227 -4.557 25.944 28.030 1.00 16.98 C ANISOU 1672 CD1 ILE A 227 1793 2147 2510 -26 109 101 C ATOM 1673 N LYS A 228 -0.408 29.458 26.660 1.00 18.95 N ANISOU 1673 N LYS A 228 2200 2291 2710 354 270 371 N ATOM 1674 CA LYS A 228 0.256 30.344 25.696 1.00 20.36 C ANISOU 1674 CA LYS A 228 2434 2500 2799 177 361 335 C ATOM 1675 C LYS A 228 1.777 30.396 25.898 1.00 19.77 C ANISOU 1675 C LYS A 228 2374 2277 2860 -224 610 144 C ATOM 1676 O LYS A 228 2.486 30.646 24.947 1.00 20.94 O ANISOU 1676 O LYS A 228 2509 2908 2537 -334 413 262 O ATOM 1677 CB LYS A 228 -0.382 31.735 25.665 1.00 23.78 C ANISOU 1677 CB LYS A 228 3168 2597 3268 438 417 179 C ATOM 1678 CG LYS A 228 -1.763 31.716 25.021 0.50 26.79 C ANISOU 1678 CG LYS A 228 3294 3323 3561 203 270 45 C ATOM 1679 CD LYS A 228 -2.167 33.059 24.439 0.50 30.92 C ANISOU 1679 CD LYS A 228 4197 3483 4067 266 294 292 C ATOM 1680 CE LYS A 228 -3.655 33.072 24.125 0.50 34.50 C ANISOU 1680 CE LYS A 228 4258 4417 4432 141 222 25 C ATOM 1681 NZ LYS A 228 -4.227 31.696 24.117 0.50 34.61 N ANISOU 1681 NZ LYS A 228 4283 4381 4484 178 226 83 N ATOM 1682 N ALA A 229 2.269 30.108 27.107 1.00 20.97 N ANISOU 1682 N ALA A 229 2853 2044 3069 -469 479 449 N ATOM 1683 CA ALA A 229 3.721 30.032 27.359 1.00 21.93 C ANISOU 1683 CA ALA A 229 2948 1322 4062 -1035 589 1264 C ATOM 1684 C ALA A 229 4.381 28.727 26.883 1.00 19.12 C ANISOU 1684 C ALA A 229 1689 2571 3002 -458 178 559 C ATOM 1685 O ALA A 229 5.607 28.674 26.780 1.00 22.42 O ANISOU 1685 O ALA A 229 1739 2441 4338 -293 623 27 O ATOM 1686 CB ALA A 229 4.008 30.237 28.843 1.00 27.39 C ANISOU 1686 CB ALA A 229 4332 2230 3843 -1980 757 1388 C ATOM 1687 N VAL A 230 3.587 27.683 26.629 1.00 18.65 N ANISOU 1687 N VAL A 230 1837 2274 2973 -233 81 423 N ATOM 1688 CA VAL A 230 4.094 26.337 26.277 1.00 19.60 C ANISOU 1688 CA VAL A 230 2360 2374 2712 -274 200 133 C ATOM 1689 C VAL A 230 3.833 25.941 24.814 1.00 18.32 C ANISOU 1689 C VAL A 230 1939 2412 2606 -83 336 134 C ATOM 1690 O VAL A 230 4.725 25.419 24.140 1.00 19.70 O ANISOU 1690 O VAL A 230 1750 2635 3098 -23 317 -56 O ATOM 1691 CB VAL A 230 3.486 25.270 27.225 1.00 20.72 C ANISOU 1691 CB VAL A 230 2601 2237 3032 -109 195 393 C ATOM 1692 CG1 VAL A 230 3.743 23.845 26.738 1.00 22.03 C ANISOU 1692 CG1 VAL A 230 2893 2304 3171 -218 -134 163 C ATOM 1693 CG2 VAL A 230 4.035 25.452 28.634 1.00 22.31 C ANISOU 1693 CG2 VAL A 230 3954 1890 2634 -1508 528 1254 C ATOM 1694 N VAL A 231 2.611 26.160 24.340 1.00 16.96 N ANISOU 1694 N VAL A 231 1902 2016 2522 -218 308 34 N ATOM 1695 CA VAL A 231 2.174 25.664 23.038 1.00 17.65 C ANISOU 1695 CA VAL A 231 2048 1946 2711 -222 124 -4 C ATOM 1696 C VAL A 231 2.392 26.731 21.970 1.00 18.88 C ANISOU 1696 C VAL A 231 2424 1911 2838 -136 52 79 C ATOM 1697 O VAL A 231 1.863 27.834 22.106 1.00 18.49 O ANISOU 1697 O VAL A 231 2509 1486 3028 -443 -219 111 O ATOM 1698 CB VAL A 231 0.675 25.287 23.064 1.00 18.32 C ANISOU 1698 CB VAL A 231 2057 2077 2826 -267 105 119 C ATOM 1699 CG1 VAL A 231 0.258 24.655 21.740 1.00 19.30 C ANISOU 1699 CG1 VAL A 231 2192 2372 2769 -148 137 87 C ATOM 1700 CG2 VAL A 231 0.392 24.338 24.223 1.00 18.89 C ANISOU 1700 CG2 VAL A 231 2416 2164 2598 -164 20 90 C ATOM 1701 N PRO A 232 3.161 26.411 20.904 1.00 20.81 N ANISOU 1701 N PRO A 232 2632 2421 2852 -92 137 81 N ATOM 1702 CA PRO A 232 3.289 27.359 19.790 1.00 22.32 C ANISOU 1702 CA PRO A 232 2846 2763 2868 76 -184 261 C ATOM 1703 C PRO A 232 1.941 27.834 19.246 1.00 20.57 C ANISOU 1703 C PRO A 232 2783 2102 2930 -292 -286 257 C ATOM 1704 O PRO A 232 1.027 27.020 19.042 1.00 20.59 O ANISOU 1704 O PRO A 232 2636 2208 2979 -384 -76 394 O ATOM 1705 CB PRO A 232 4.038 26.550 18.734 1.00 22.18 C ANISOU 1705 CB PRO A 232 2842 3077 2506 90 -259 322 C ATOM 1706 CG PRO A 232 4.883 25.606 19.530 1.00 21.04 C ANISOU 1706 CG PRO A 232 2447 2999 2548 180 -111 161 C ATOM 1707 CD PRO A 232 4.036 25.236 20.716 1.00 20.85 C ANISOU 1707 CD PRO A 232 2619 2730 2570 157 -82 258 C ATOM 1708 N ALA A 233 1.837 29.143 19.023 1.00 21.53 N ANISOU 1708 N ALA A 233 3171 2054 2953 -454 -199 287 N ATOM 1709 CA ALA A 233 0.608 29.781 18.551 1.00 22.69 C ANISOU 1709 CA ALA A 233 3378 2097 3145 -95 15 346 C ATOM 1710 C ALA A 233 0.107 29.186 17.237 1.00 22.36 C ANISOU 1710 C ALA A 233 3322 2045 3129 -129 -60 454 C ATOM 1711 O ALA A 233 -1.101 29.110 17.020 1.00 21.19 O ANISOU 1711 O ALA A 233 3186 1803 3063 353 190 428 O ATOM 1712 CB ALA A 233 0.816 31.285 18.402 1.00 24.22 C ANISOU 1712 CB ALA A 233 3622 2062 3518 -40 66 189 C ATOM 1713 N LYS A 234 1.025 28.725 16.385 1.00 21.25 N ANISOU 1713 N LYS A 234 2845 2331 2898 -568 -99 461 N ATOM 1714 CA LYS A 234 0.646 28.081 15.123 1.00 21.46 C ANISOU 1714 CA LYS A 234 2666 2565 2920 -709 -141 496 C ATOM 1715 C LYS A 234 -0.290 26.874 15.289 1.00 20.36 C ANISOU 1715 C LYS A 234 2619 2118 2997 -486 -453 398 C ATOM 1716 O LYS A 234 -1.007 26.538 14.348 1.00 21.27 O ANISOU 1716 O LYS A 234 2073 2550 3458 -870 -515 460 O ATOM 1717 CB LYS A 234 1.882 27.664 14.318 1.00 24.44 C ANISOU 1717 CB LYS A 234 2980 3216 3089 -312 -81 372 C ATOM 1718 CG LYS A 234 2.679 26.537 14.934 1.00 24.67 C ANISOU 1718 CG LYS A 234 3150 3023 3199 -259 -41 244 C ATOM 1719 CD LYS A 234 3.910 26.222 14.121 1.00 25.97 C ANISOU 1719 CD LYS A 234 2676 3608 3581 -700 -99 146 C ATOM 1720 CE LYS A 234 4.738 25.182 14.841 1.00 26.24 C ANISOU 1720 CE LYS A 234 2836 3155 3979 -716 -95 19 C ATOM 1721 NZ LYS A 234 5.938 24.825 14.048 1.00 24.83 N ANISOU 1721 NZ LYS A 234 3446 1694 4292 -951 361 -12 N ATOM 1722 N TYR A 235 -0.262 26.223 16.460 1.00 19.26 N ANISOU 1722 N TYR A 235 2562 2036 2718 -449 -439 159 N ATOM 1723 CA TYR A 235 -1.154 25.091 16.761 1.00 18.16 C ANISOU 1723 CA TYR A 235 2157 2028 2714 -256 -299 112 C ATOM 1724 C TYR A 235 -2.520 25.464 17.355 1.00 20.37 C ANISOU 1724 C TYR A 235 2493 2369 2877 -307 64 -28 C ATOM 1725 O TYR A 235 -3.420 24.613 17.402 1.00 19.38 O ANISOU 1725 O TYR A 235 1904 2002 3458 164 111 89 O ATOM 1726 CB TYR A 235 -0.459 24.109 17.709 1.00 19.26 C ANISOU 1726 CB TYR A 235 2557 2169 2591 -143 -272 140 C ATOM 1727 CG TYR A 235 0.780 23.432 17.141 1.00 21.53 C ANISOU 1727 CG TYR A 235 2626 2541 3012 -154 26 128 C ATOM 1728 CD1 TYR A 235 0.746 22.776 15.909 1.00 24.19 C ANISOU 1728 CD1 TYR A 235 3029 2942 3218 -150 -54 -116 C ATOM 1729 CD2 TYR A 235 1.978 23.409 17.856 1.00 23.64 C ANISOU 1729 CD2 TYR A 235 2958 2750 3271 -370 -288 94 C ATOM 1730 CE1 TYR A 235 1.874 22.146 15.391 1.00 24.41 C ANISOU 1730 CE1 TYR A 235 2988 3116 3169 -84 85 251 C ATOM 1731 CE2 TYR A 235 3.112 22.779 17.345 1.00 28.28 C ANISOU 1731 CE2 TYR A 235 3522 3174 4046 -66 268 83 C ATOM 1732 CZ TYR A 235 3.053 22.143 16.115 1.00 24.87 C ANISOU 1732 CZ TYR A 235 2274 3255 3918 -302 473 227 C ATOM 1733 OH TYR A 235 4.172 21.514 15.598 1.00 27.66 O ANISOU 1733 OH TYR A 235 2064 3288 5155 -375 969 649 O ATOM 1734 N LEU A 236 -2.681 26.705 17.812 1.00 22.29 N ANISOU 1734 N LEU A 236 3096 2452 2918 -201 89 -85 N ATOM 1735 CA LEU A 236 -3.907 27.138 18.472 1.00 22.45 C ANISOU 1735 CA LEU A 236 3247 2613 2668 -6 93 277 C ATOM 1736 C LEU A 236 -4.723 28.016 17.537 1.00 25.01 C ANISOU 1736 C LEU A 236 4004 2657 2839 -164 -160 549 C ATOM 1737 O LEU A 236 -4.179 28.825 16.800 1.00 23.33 O ANISOU 1737 O LEU A 236 3606 2429 2828 254 -447 804 O ATOM 1738 CB LEU A 236 -3.574 27.900 19.753 1.00 22.06 C ANISOU 1738 CB LEU A 236 3173 2690 2517 141 47 341 C ATOM 1739 CG LEU A 236 -2.709 27.161 20.776 1.00 21.60 C ANISOU 1739 CG LEU A 236 2992 2588 2625 456 94 193 C ATOM 1740 CD1 LEU A 236 -2.321 28.095 21.910 1.00 19.61 C ANISOU 1740 CD1 LEU A 236 2918 2960 1571 1811 -764 644 C ATOM 1741 CD2 LEU A 236 -3.430 25.932 21.329 1.00 21.22 C ANISOU 1741 CD2 LEU A 236 2994 2562 2504 447 -34 261 C ATOM 1742 N ASP A 237 -6.037 27.852 17.556 1.00 23.74 N ANISOU 1742 N ASP A 237 4549 2165 2303 -1714 54 1527 N ATOM 1743 CA ASP A 237 -6.893 28.663 16.693 1.00 24.19 C ANISOU 1743 CA ASP A 237 2756 2981 3454 -762 -65 716 C ATOM 1744 C ASP A 237 -8.264 28.822 17.333 1.00 22.32 C ANISOU 1744 C ASP A 237 2414 2446 3619 -154 -511 1074 C ATOM 1745 O ASP A 237 -8.503 28.313 18.436 1.00 22.96 O ANISOU 1745 O ASP A 237 2511 2485 3726 -238 78 901 O ATOM 1746 CB ASP A 237 -6.949 28.056 15.275 1.00 24.80 C ANISOU 1746 CB ASP A 237 3385 2485 3551 -549 -57 756 C ATOM 1747 CG ASP A 237 -7.532 26.644 15.242 1.00 27.59 C ANISOU 1747 CG ASP A 237 4036 2246 4201 -378 -18 618 C ATOM 1748 OD1 ASP A 237 -8.454 26.329 16.022 1.00 26.29 O ANISOU 1748 OD1 ASP A 237 3597 2268 4123 -78 -227 697 O ATOM 1749 OD2 ASP A 237 -7.071 25.832 14.410 1.00 33.12 O ANISOU 1749 OD2 ASP A 237 5272 2527 4784 -291 164 176 O ATOM 1750 N GLU A 238 -9.153 29.517 16.633 1.00 22.50 N ANISOU 1750 N GLU A 238 1843 2500 4205 -29 -274 1180 N ATOM 1751 CA GLU A 238 -10.507 29.796 17.120 1.00 25.09 C ANISOU 1751 CA GLU A 238 1891 3260 4379 251 -424 769 C ATOM 1752 C GLU A 238 -11.332 28.559 17.505 1.00 27.15 C ANISOU 1752 C GLU A 238 2881 3045 4390 543 146 1227 C ATOM 1753 O GLU A 238 -12.278 28.672 18.294 1.00 31.02 O ANISOU 1753 O GLU A 238 2626 4258 4900 658 224 1102 O ATOM 1754 CB GLU A 238 -11.282 30.631 16.080 1.00 30.84 C ANISOU 1754 CB GLU A 238 3219 3828 4669 271 -668 1406 C ATOM 1755 CG GLU A 238 -11.585 29.925 14.754 0.50 32.39 C ANISOU 1755 CG GLU A 238 3875 3603 4828 395 -348 1141 C ATOM 1756 CD GLU A 238 -12.416 30.766 13.790 0.50 37.65 C ANISOU 1756 CD GLU A 238 4269 4759 5276 -70 -1148 1675 C ATOM 1757 OE1 GLU A 238 -12.746 31.931 14.109 0.50 39.22 O ANISOU 1757 OE1 GLU A 238 4577 4591 5733 31 -966 1986 O ATOM 1758 OE2 GLU A 238 -12.744 30.253 12.698 0.50 36.50 O ANISOU 1758 OE2 GLU A 238 3954 5188 4724 -608 -310 1794 O ATOM 1759 N ASP A 239 -10.994 27.400 16.926 1.00 28.66 N ANISOU 1759 N ASP A 239 3116 3305 4468 1065 -207 1094 N ATOM 1760 CA ASP A 239 -11.725 26.152 17.164 1.00 28.68 C ANISOU 1760 CA ASP A 239 3548 2909 4439 1078 -89 595 C ATOM 1761 C ASP A 239 -11.171 25.300 18.304 1.00 24.57 C ANISOU 1761 C ASP A 239 2490 3081 3764 423 -213 288 C ATOM 1762 O ASP A 239 -11.854 24.382 18.755 1.00 25.36 O ANISOU 1762 O ASP A 239 2004 3501 4128 694 370 433 O ATOM 1763 CB ASP A 239 -11.755 25.306 15.888 1.00 30.97 C ANISOU 1763 CB ASP A 239 3841 3910 4014 148 -146 633 C ATOM 1764 CG ASP A 239 -12.500 25.978 14.752 1.00 36.03 C ANISOU 1764 CG ASP A 239 4272 4834 4582 635 -359 925 C ATOM 1765 OD1 ASP A 239 -13.479 26.718 15.011 1.00 35.53 O ANISOU 1765 OD1 ASP A 239 3382 5353 4763 463 -593 1240 O ATOM 1766 OD2 ASP A 239 -12.108 25.750 13.588 1.00 41.62 O ANISOU 1766 OD2 ASP A 239 5067 6360 4387 9 -273 944 O ATOM 1767 N THR A 240 -9.945 25.575 18.754 1.00 20.50 N ANISOU 1767 N THR A 240 2243 2445 3102 600 2 453 N ATOM 1768 CA THR A 240 -9.354 24.834 19.867 1.00 19.52 C ANISOU 1768 CA THR A 240 2492 2074 2848 256 -85 272 C ATOM 1769 C THR A 240 -10.278 24.870 21.085 1.00 17.47 C ANISOU 1769 C THR A 240 2186 1515 2937 289 -126 74 C ATOM 1770 O THR A 240 -10.797 25.934 21.453 1.00 20.07 O ANISOU 1770 O THR A 240 2297 1811 3518 697 -391 -52 O ATOM 1771 CB THR A 240 -7.966 25.388 20.257 1.00 19.13 C ANISOU 1771 CB THR A 240 2470 2120 2676 248 -106 214 C ATOM 1772 OG1 THR A 240 -7.080 25.287 19.137 1.00 19.54 O ANISOU 1772 OG1 THR A 240 2786 1674 2963 215 144 191 O ATOM 1773 CG2 THR A 240 -7.373 24.615 21.434 1.00 18.59 C ANISOU 1773 CG2 THR A 240 2522 2112 2429 88 110 264 C ATOM 1774 N ILE A 241 -10.477 23.701 21.689 1.00 17.27 N ANISOU 1774 N ILE A 241 2098 1479 2984 290 -203 95 N ATOM 1775 CA ILE A 241 -11.334 23.541 22.867 1.00 18.30 C ANISOU 1775 CA ILE A 241 2151 1784 3015 64 -164 6 C ATOM 1776 C ILE A 241 -10.488 23.544 24.151 1.00 17.24 C ANISOU 1776 C ILE A 241 1842 1720 2985 83 -84 -5 C ATOM 1777 O ILE A 241 -9.447 22.864 24.232 1.00 18.22 O ANISOU 1777 O ILE A 241 2206 1857 2859 393 -20 224 O ATOM 1778 CB ILE A 241 -12.186 22.248 22.750 1.00 19.11 C ANISOU 1778 CB ILE A 241 2159 2046 3054 -137 -128 -77 C ATOM 1779 CG1 ILE A 241 -13.149 22.371 21.562 1.00 19.97 C ANISOU 1779 CG1 ILE A 241 2416 2236 2935 -106 -119 -75 C ATOM 1780 CG2 ILE A 241 -12.970 21.976 24.034 1.00 15.74 C ANISOU 1780 CG2 ILE A 241 1520 1357 3102 -358 -302 -118 C ATOM 1781 CD1 ILE A 241 -13.662 21.054 21.031 1.00 20.17 C ANISOU 1781 CD1 ILE A 241 2474 2222 2965 -53 50 -169 C ATOM 1782 N TYR A 242 -10.939 24.313 25.144 1.00 16.81 N ANISOU 1782 N TYR A 242 1906 1641 2839 102 -82 110 N ATOM 1783 CA TYR A 242 -10.261 24.428 26.439 1.00 18.43 C ANISOU 1783 CA TYR A 242 2110 2055 2837 198 -128 48 C ATOM 1784 C TYR A 242 -11.148 23.971 27.582 1.00 17.09 C ANISOU 1784 C TYR A 242 1592 1940 2959 701 -25 -38 C ATOM 1785 O TYR A 242 -12.223 24.537 27.820 1.00 17.74 O ANISOU 1785 O TYR A 242 1537 2012 3189 723 148 296 O ATOM 1786 CB TYR A 242 -9.825 25.867 26.700 1.00 20.37 C ANISOU 1786 CB TYR A 242 2887 2095 2756 74 -288 83 C ATOM 1787 CG TYR A 242 -8.874 26.397 25.660 1.00 23.41 C ANISOU 1787 CG TYR A 242 3884 2465 2544 -193 -98 178 C ATOM 1788 CD1 TYR A 242 -7.500 26.195 25.772 1.00 26.29 C ANISOU 1788 CD1 TYR A 242 4461 3531 1996 57 -932 1944 C ATOM 1789 CD2 TYR A 242 -9.348 27.093 24.555 1.00 22.89 C ANISOU 1789 CD2 TYR A 242 3003 2602 3089 -145 113 599 C ATOM 1790 CE1 TYR A 242 -6.628 26.680 24.812 1.00 21.66 C ANISOU 1790 CE1 TYR A 242 2617 2533 3077 440 -354 664 C ATOM 1791 CE2 TYR A 242 -8.488 27.576 23.587 1.00 20.69 C ANISOU 1791 CE2 TYR A 242 2163 2266 3432 -432 -190 546 C ATOM 1792 CZ TYR A 242 -7.125 27.365 23.722 1.00 20.28 C ANISOU 1792 CZ TYR A 242 2302 2348 3055 -46 -310 750 C ATOM 1793 OH TYR A 242 -6.267 27.841 22.770 1.00 23.45 O ANISOU 1793 OH TYR A 242 3214 2125 3570 -452 124 820 O ATOM 1794 N HIS A 243 -10.696 22.939 28.286 1.00 17.32 N ANISOU 1794 N HIS A 243 2404 1339 2837 457 -25 -242 N ATOM 1795 CA HIS A 243 -11.346 22.483 29.512 1.00 18.22 C ANISOU 1795 CA HIS A 243 1917 1897 3108 352 -45 67 C ATOM 1796 C HIS A 243 -10.397 22.781 30.666 1.00 18.53 C ANISOU 1796 C HIS A 243 2103 1972 2964 360 -89 213 C ATOM 1797 O HIS A 243 -9.515 21.969 30.978 1.00 16.47 O ANISOU 1797 O HIS A 243 1366 1828 3064 29 31 104 O ATOM 1798 CB HIS A 243 -11.669 20.993 29.423 1.00 18.02 C ANISOU 1798 CB HIS A 243 2188 1969 2689 129 90 125 C ATOM 1799 CG HIS A 243 -12.756 20.666 28.448 1.00 18.72 C ANISOU 1799 CG HIS A 243 2266 1930 2916 183 -31 23 C ATOM 1800 ND1 HIS A 243 -14.073 21.003 28.664 1.00 19.91 N ANISOU 1800 ND1 HIS A 243 2397 1833 3332 191 172 -178 N ATOM 1801 CD2 HIS A 243 -12.723 20.014 27.261 1.00 18.00 C ANISOU 1801 CD2 HIS A 243 1873 2006 2957 209 -245 -29 C ATOM 1802 CE1 HIS A 243 -14.804 20.580 27.647 1.00 20.02 C ANISOU 1802 CE1 HIS A 243 2313 2014 3277 127 161 -84 C ATOM 1803 NE2 HIS A 243 -14.011 19.970 26.786 1.00 17.35 N ANISOU 1803 NE2 HIS A 243 1894 1705 2993 121 -244 -106 N ATOM 1804 N LEU A 244 -10.569 23.954 31.281 1.00 18.79 N ANISOU 1804 N LEU A 244 963 2388 3788 1142 -173 -181 N ATOM 1805 CA LEU A 244 -9.646 24.442 32.319 1.00 18.74 C ANISOU 1805 CA LEU A 244 2541 1424 3155 228 -51 -37 C ATOM 1806 C LEU A 244 -10.368 24.458 33.660 1.00 15.99 C ANISOU 1806 C LEU A 244 1700 1131 3243 305 -237 -2 C ATOM 1807 O LEU A 244 -11.439 25.061 33.787 1.00 16.20 O ANISOU 1807 O LEU A 244 1626 1219 3309 310 -350 -67 O ATOM 1808 CB LEU A 244 -9.123 25.837 31.949 1.00 18.16 C ANISOU 1808 CB LEU A 244 2534 1546 2821 -65 -196 -228 C ATOM 1809 CG LEU A 244 -8.593 25.988 30.517 1.00 19.60 C ANISOU 1809 CG LEU A 244 2781 1921 2744 36 -191 -189 C ATOM 1810 CD1 LEU A 244 -8.254 27.435 30.196 1.00 20.52 C ANISOU 1810 CD1 LEU A 244 3213 1896 2687 22 -247 -249 C ATOM 1811 CD2 LEU A 244 -7.383 25.101 30.266 1.00 20.36 C ANISOU 1811 CD2 LEU A 244 2663 2322 2751 64 -155 -231 C ATOM 1812 N GLN A 245 -9.787 23.780 34.648 1.00 18.04 N ANISOU 1812 N GLN A 245 1787 1531 3535 144 -809 3 N ATOM 1813 CA GLN A 245 -10.464 23.459 35.914 1.00 21.60 C ANISOU 1813 CA GLN A 245 2486 1524 4197 880 -845 1272 C ATOM 1814 C GLN A 245 -11.894 22.978 35.658 1.00 17.34 C ANISOU 1814 C GLN A 245 2304 1602 2682 619 68 61 C ATOM 1815 O GLN A 245 -12.856 23.548 36.194 1.00 16.45 O ANISOU 1815 O GLN A 245 2397 1067 2786 596 132 116 O ATOM 1816 CB GLN A 245 -10.447 24.663 36.864 1.00 23.32 C ANISOU 1816 CB GLN A 245 2365 1769 4725 1316 -901 972 C ATOM 1817 CG GLN A 245 -9.062 25.239 37.157 1.00 22.28 C ANISOU 1817 CG GLN A 245 2576 2855 3033 864 -403 188 C ATOM 1818 CD GLN A 245 -8.211 24.319 38.014 1.00 20.95 C ANISOU 1818 CD GLN A 245 2525 2766 2666 997 -467 -220 C ATOM 1819 OE1 GLN A 245 -7.991 23.157 37.664 1.00 22.92 O ANISOU 1819 OE1 GLN A 245 2809 2890 3008 1164 -763 -428 O ATOM 1820 NE2 GLN A 245 -7.708 24.831 39.133 1.00 19.44 N ANISOU 1820 NE2 GLN A 245 2224 2910 2250 1685 -1011 408 N ATOM 1821 N PRO A 246 -12.044 21.946 34.808 1.00 15.98 N ANISOU 1821 N PRO A 246 1699 1559 2814 104 -121 126 N ATOM 1822 CA PRO A 246 -13.411 21.530 34.419 1.00 16.74 C ANISOU 1822 CA PRO A 246 1681 1864 2815 112 -141 -33 C ATOM 1823 C PRO A 246 -14.277 20.973 35.553 1.00 16.21 C ANISOU 1823 C PRO A 246 1216 1823 3118 -4 -139 -100 C ATOM 1824 O PRO A 246 -15.515 20.985 35.432 1.00 17.28 O ANISOU 1824 O PRO A 246 1144 2130 3291 -119 65 87 O ATOM 1825 CB PRO A 246 -13.157 20.473 33.340 1.00 17.09 C ANISOU 1825 CB PRO A 246 1957 2032 2503 243 -323 34 C ATOM 1826 CG PRO A 246 -11.791 19.942 33.652 1.00 16.19 C ANISOU 1826 CG PRO A 246 1809 2038 2304 200 -121 -23 C ATOM 1827 CD PRO A 246 -11.026 21.152 34.100 1.00 16.47 C ANISOU 1827 CD PRO A 246 1701 1953 2602 166 -107 103 C ATOM 1828 N SER A 247 -13.672 20.512 36.647 1.00 16.69 N ANISOU 1828 N SER A 247 1844 1524 2972 166 -48 -114 N ATOM 1829 CA SER A 247 -14.466 20.096 37.811 1.00 18.98 C ANISOU 1829 CA SER A 247 2260 2070 2881 191 75 -202 C ATOM 1830 C SER A 247 -15.069 21.280 38.580 1.00 19.67 C ANISOU 1830 C SER A 247 2105 2055 3312 202 265 -204 C ATOM 1831 O SER A 247 -16.018 21.088 39.335 1.00 21.05 O ANISOU 1831 O SER A 247 2215 2286 3497 279 403 58 O ATOM 1832 CB SER A 247 -13.639 19.242 38.770 1.00 20.78 C ANISOU 1832 CB SER A 247 2613 2210 3071 238 -87 -56 C ATOM 1833 OG SER A 247 -12.754 20.048 39.532 1.00 21.58 O ANISOU 1833 OG SER A 247 2926 2337 2935 240 -294 -47 O ATOM 1834 N GLY A 248 -14.487 22.475 38.428 1.00 20.55 N ANISOU 1834 N GLY A 248 2371 2139 3299 76 494 -222 N ATOM 1835 CA GLY A 248 -14.962 23.693 39.101 1.00 21.67 C ANISOU 1835 CA GLY A 248 2500 2244 3488 464 186 -229 C ATOM 1836 C GLY A 248 -14.330 23.995 40.456 1.00 22.42 C ANISOU 1836 C GLY A 248 2811 2268 3438 893 8 -125 C ATOM 1837 O GLY A 248 -14.392 25.136 40.929 1.00 22.41 O ANISOU 1837 O GLY A 248 2767 2828 2918 1061 43 -638 O ATOM 1838 N ARG A 249 -13.719 22.987 41.081 1.00 20.58 N ANISOU 1838 N ARG A 249 2906 1146 3764 550 -122 -533 N ATOM 1839 CA ARG A 249 -13.134 23.117 42.414 1.00 21.76 C ANISOU 1839 CA ARG A 249 2984 1830 3452 653 50 -242 C ATOM 1840 C ARG A 249 -12.209 21.924 42.678 1.00 19.00 C ANISOU 1840 C ARG A 249 2599 2088 2532 606 -223 -284 C ATOM 1841 O ARG A 249 -12.592 20.777 42.463 1.00 20.19 O ANISOU 1841 O ARG A 249 2674 2257 2740 161 -170 -3 O ATOM 1842 CB ARG A 249 -14.224 23.176 43.489 1.00 24.50 C ANISOU 1842 CB ARG A 249 3383 2517 3409 451 168 -256 C ATOM 1843 CG ARG A 249 -13.701 23.452 44.893 1.00 23.89 C ANISOU 1843 CG ARG A 249 3133 2433 3509 206 114 -239 C ATOM 1844 CD ARG A 249 -14.823 23.512 45.915 1.00 26.55 C ANISOU 1844 CD ARG A 249 3311 2941 3835 189 315 -377 C ATOM 1845 NE ARG A 249 -14.304 23.363 47.277 1.00 28.21 N ANISOU 1845 NE ARG A 249 3447 3368 3901 507 383 -358 N ATOM 1846 CZ ARG A 249 -13.877 24.351 48.068 1.00 29.25 C ANISOU 1846 CZ ARG A 249 3547 4057 3508 175 369 -415 C ATOM 1847 NH1 ARG A 249 -13.897 25.628 47.676 1.00 30.02 N ANISOU 1847 NH1 ARG A 249 3490 4042 3874 425 904 -472 N ATOM 1848 NH2 ARG A 249 -13.422 24.052 49.279 1.00 28.69 N ANISOU 1848 NH2 ARG A 249 3484 3746 3670 204 496 174 N ATOM 1849 N PHE A 250 -11.028 22.217 43.208 1.00 17.46 N ANISOU 1849 N PHE A 250 2431 1728 2472 585 -58 -254 N ATOM 1850 CA PHE A 250 -9.912 21.268 43.343 1.00 17.05 C ANISOU 1850 CA PHE A 250 1963 1909 2605 358 -119 -94 C ATOM 1851 C PHE A 250 -9.031 21.840 44.473 1.00 17.12 C ANISOU 1851 C PHE A 250 2058 1846 2598 375 -103 -127 C ATOM 1852 O PHE A 250 -7.871 22.198 44.274 1.00 17.45 O ANISOU 1852 O PHE A 250 2267 1647 2716 70 -18 -212 O ATOM 1853 CB PHE A 250 -9.179 21.123 41.985 1.00 16.49 C ANISOU 1853 CB PHE A 250 2190 1643 2431 423 -249 -94 C ATOM 1854 CG PHE A 250 -8.133 20.004 41.902 1.00 16.05 C ANISOU 1854 CG PHE A 250 2119 1479 2497 286 -168 -66 C ATOM 1855 CD1 PHE A 250 -7.758 19.219 42.995 1.00 17.55 C ANISOU 1855 CD1 PHE A 250 2460 1735 2471 319 -185 -7 C ATOM 1856 CD2 PHE A 250 -7.488 19.781 40.689 1.00 15.81 C ANISOU 1856 CD2 PHE A 250 2309 1182 2515 370 -114 -125 C ATOM 1857 CE1 PHE A 250 -6.783 18.233 42.864 1.00 16.18 C ANISOU 1857 CE1 PHE A 250 2037 1863 2245 160 -175 -133 C ATOM 1858 CE2 PHE A 250 -6.506 18.811 40.557 1.00 14.40 C ANISOU 1858 CE2 PHE A 250 1809 1338 2324 127 139 -221 C ATOM 1859 CZ PHE A 250 -6.160 18.029 41.646 1.00 16.95 C ANISOU 1859 CZ PHE A 250 2260 1817 2361 224 -22 -111 C ATOM 1860 N VAL A 251 -9.626 21.951 45.661 1.00 17.13 N ANISOU 1860 N VAL A 251 1991 1838 2677 420 -31 34 N ATOM 1861 CA VAL A 251 -8.919 22.406 46.867 1.00 17.51 C ANISOU 1861 CA VAL A 251 2072 1747 2833 258 -87 30 C ATOM 1862 C VAL A 251 -8.295 21.200 47.567 1.00 17.22 C ANISOU 1862 C VAL A 251 2191 1635 2716 45 -24 154 C ATOM 1863 O VAL A 251 -7.101 21.210 47.904 1.00 17.15 O ANISOU 1863 O VAL A 251 2147 1546 2822 -230 20 -166 O ATOM 1864 CB VAL A 251 -9.859 23.199 47.796 1.00 17.84 C ANISOU 1864 CB VAL A 251 2199 1752 2827 235 12 82 C ATOM 1865 CG1 VAL A 251 -9.211 23.502 49.142 1.00 20.62 C ANISOU 1865 CG1 VAL A 251 2459 2275 3099 157 -153 -87 C ATOM 1866 CG2 VAL A 251 -10.261 24.497 47.104 1.00 18.01 C ANISOU 1866 CG2 VAL A 251 2048 1965 2829 355 -74 168 C ATOM 1867 N ILE A 252 -9.113 20.168 47.772 1.00 16.72 N ANISOU 1867 N ILE A 252 1960 1673 2719 117 205 107 N ATOM 1868 CA ILE A 252 -8.638 18.889 48.298 1.00 16.97 C ANISOU 1868 CA ILE A 252 2076 1774 2595 -187 -63 362 C ATOM 1869 C ILE A 252 -7.817 18.205 47.199 1.00 16.66 C ANISOU 1869 C ILE A 252 1781 1762 2786 -52 -228 261 C ATOM 1870 O ILE A 252 -8.288 18.060 46.082 1.00 16.49 O ANISOU 1870 O ILE A 252 1914 1750 2600 -57 -70 428 O ATOM 1871 CB ILE A 252 -9.818 17.998 48.751 1.00 16.84 C ANISOU 1871 CB ILE A 252 1801 2147 2447 -155 68 114 C ATOM 1872 CG1 ILE A 252 -10.528 18.639 49.947 1.00 16.27 C ANISOU 1872 CG1 ILE A 252 1100 2154 2926 92 102 54 C ATOM 1873 CG2 ILE A 252 -9.328 16.599 49.138 1.00 19.39 C ANISOU 1873 CG2 ILE A 252 2434 2187 2744 9 -153 30 C ATOM 1874 CD1 ILE A 252 -11.948 18.147 50.158 1.00 17.94 C ANISOU 1874 CD1 ILE A 252 1234 2614 2967 -104 268 50 C ATOM 1875 N GLY A 253 -6.584 17.810 47.505 1.00 17.03 N ANISOU 1875 N GLY A 253 2015 1869 2584 -36 -637 303 N ATOM 1876 CA GLY A 253 -5.694 17.249 46.488 1.00 18.19 C ANISOU 1876 CA GLY A 253 1913 2109 2890 -98 -457 177 C ATOM 1877 C GLY A 253 -4.566 16.453 47.098 1.00 17.23 C ANISOU 1877 C GLY A 253 1881 1827 2837 33 -176 59 C ATOM 1878 O GLY A 253 -4.526 16.258 48.308 1.00 17.94 O ANISOU 1878 O GLY A 253 1942 2058 2814 698 -93 -75 O ATOM 1879 N GLY A 254 -3.650 15.980 46.256 1.00 17.32 N ANISOU 1879 N GLY A 254 2344 1746 2488 45 -129 -16 N ATOM 1880 CA GLY A 254 -2.585 15.079 46.710 1.00 16.37 C ANISOU 1880 CA GLY A 254 2159 1640 2419 58 71 -76 C ATOM 1881 C GLY A 254 -3.175 13.765 47.214 1.00 16.64 C ANISOU 1881 C GLY A 254 2111 1841 2371 -24 -86 111 C ATOM 1882 O GLY A 254 -4.316 13.434 46.884 1.00 16.35 O ANISOU 1882 O GLY A 254 2046 1697 2467 71 -62 180 O ATOM 1883 N PRO A 255 -2.418 13.010 48.033 1.00 16.77 N ANISOU 1883 N PRO A 255 1846 1860 2664 31 0 195 N ATOM 1884 CA PRO A 255 -2.937 11.759 48.594 1.00 16.93 C ANISOU 1884 CA PRO A 255 1957 1880 2595 -36 17 113 C ATOM 1885 C PRO A 255 -4.278 11.877 49.343 1.00 17.99 C ANISOU 1885 C PRO A 255 2059 1952 2823 155 127 105 C ATOM 1886 O PRO A 255 -5.050 10.920 49.352 1.00 18.64 O ANISOU 1886 O PRO A 255 2038 1817 3227 252 -83 104 O ATOM 1887 CB PRO A 255 -1.824 11.316 49.536 1.00 17.24 C ANISOU 1887 CB PRO A 255 2064 2075 2410 44 115 273 C ATOM 1888 CG PRO A 255 -0.584 11.854 48.907 1.00 17.41 C ANISOU 1888 CG PRO A 255 2093 2221 2298 159 246 289 C ATOM 1889 CD PRO A 255 -0.986 13.188 48.344 1.00 17.28 C ANISOU 1889 CD PRO A 255 1835 2172 2557 148 -6 182 C ATOM 1890 N GLN A 256 -4.565 13.032 49.943 1.00 17.77 N ANISOU 1890 N GLN A 256 2021 2129 2600 273 185 94 N ATOM 1891 CA GLN A 256 -5.864 13.229 50.591 1.00 18.76 C ANISOU 1891 CA GLN A 256 2043 2322 2763 284 225 140 C ATOM 1892 C GLN A 256 -7.043 13.103 49.630 1.00 18.95 C ANISOU 1892 C GLN A 256 2041 2366 2794 -11 256 -2 C ATOM 1893 O GLN A 256 -8.085 12.579 50.001 1.00 20.90 O ANISOU 1893 O GLN A 256 2150 2636 3154 -238 266 -16 O ATOM 1894 CB GLN A 256 -5.928 14.570 51.307 1.00 20.47 C ANISOU 1894 CB GLN A 256 2641 2601 2535 298 80 -43 C ATOM 1895 CG GLN A 256 -7.184 14.739 52.147 1.00 22.08 C ANISOU 1895 CG GLN A 256 2861 2857 2672 474 265 213 C ATOM 1896 CD GLN A 256 -7.109 15.967 53.013 1.00 24.47 C ANISOU 1896 CD GLN A 256 2825 3324 3146 687 102 -259 C ATOM 1897 OE1 GLN A 256 -6.801 17.046 52.521 1.00 25.69 O ANISOU 1897 OE1 GLN A 256 2329 3581 3847 557 -62 -21 O ATOM 1898 NE2 GLN A 256 -7.380 15.815 54.308 1.00 27.16 N ANISOU 1898 NE2 GLN A 256 3324 3681 3315 709 225 5 N ATOM 1899 N GLY A 257 -6.883 13.586 48.406 1.00 18.99 N ANISOU 1899 N GLY A 257 2005 2249 2959 48 180 173 N ATOM 1900 CA GLY A 257 -7.946 13.498 47.411 1.00 19.75 C ANISOU 1900 CA GLY A 257 2291 2239 2971 37 68 44 C ATOM 1901 C GLY A 257 -8.073 12.154 46.711 1.00 18.60 C ANISOU 1901 C GLY A 257 1743 2102 3220 495 55 35 C ATOM 1902 O GLY A 257 -9.149 11.816 46.228 1.00 19.88 O ANISOU 1902 O GLY A 257 1974 2374 3205 141 -59 239 O ATOM 1903 N ASP A 258 -6.977 11.399 46.637 1.00 16.85 N ANISOU 1903 N ASP A 258 1525 2066 2810 384 -131 299 N ATOM 1904 CA ASP A 258 -6.902 10.222 45.787 1.00 17.43 C ANISOU 1904 CA ASP A 258 1766 1944 2911 253 -108 275 C ATOM 1905 C ASP A 258 -5.664 9.400 46.163 1.00 16.66 C ANISOU 1905 C ASP A 258 1996 1652 2682 263 -215 195 C ATOM 1906 O ASP A 258 -4.573 9.940 46.196 1.00 17.42 O ANISOU 1906 O ASP A 258 2258 1394 2965 38 -69 -31 O ATOM 1907 CB ASP A 258 -6.809 10.708 44.339 1.00 17.86 C ANISOU 1907 CB ASP A 258 1857 2004 2925 -140 31 198 C ATOM 1908 CG ASP A 258 -6.696 9.592 43.342 1.00 20.03 C ANISOU 1908 CG ASP A 258 2182 2129 3299 238 -6 58 C ATOM 1909 OD1 ASP A 258 -7.457 8.596 43.446 1.00 19.61 O ANISOU 1909 OD1 ASP A 258 1869 2109 3472 351 -9 -60 O ATOM 1910 OD2 ASP A 258 -5.837 9.699 42.438 1.00 22.36 O ANISOU 1910 OD2 ASP A 258 2478 2390 3626 97 292 -13 O ATOM 1911 N ALA A 259 -5.830 8.114 46.467 1.00 17.34 N ANISOU 1911 N ALA A 259 2306 1651 2630 -14 -283 61 N ATOM 1912 CA ALA A 259 -4.686 7.260 46.841 1.00 18.20 C ANISOU 1912 CA ALA A 259 2395 2113 2405 234 -210 45 C ATOM 1913 C ALA A 259 -3.703 7.126 45.692 1.00 18.82 C ANISOU 1913 C ALA A 259 2551 2069 2529 336 -103 64 C ATOM 1914 O ALA A 259 -4.119 7.069 44.542 1.00 18.69 O ANISOU 1914 O ALA A 259 2056 2386 2658 484 -139 -84 O ATOM 1915 CB ALA A 259 -5.154 5.877 47.274 1.00 18.14 C ANISOU 1915 CB ALA A 259 2368 2273 2248 76 -74 18 C ATOM 1916 N GLY A 260 -2.412 7.065 46.006 1.00 18.45 N ANISOU 1916 N GLY A 260 2460 2017 2532 205 135 -52 N ATOM 1917 CA GLY A 260 -1.376 6.848 45.012 1.00 16.84 C ANISOU 1917 CA GLY A 260 1990 1870 2537 309 -29 214 C ATOM 1918 C GLY A 260 -0.649 5.525 45.195 1.00 15.63 C ANISOU 1918 C GLY A 260 1905 1736 2297 163 -75 278 C ATOM 1919 O GLY A 260 -0.550 5.016 46.311 1.00 13.86 O ANISOU 1919 O GLY A 260 1371 1614 2282 174 26 222 O ATOM 1920 N LEU A 261 -0.141 4.978 44.092 1.00 13.62 N ANISOU 1920 N LEU A 261 1306 1716 2153 324 -249 422 N ATOM 1921 CA LEU A 261 0.694 3.779 44.113 1.00 14.46 C ANISOU 1921 CA LEU A 261 1681 1573 2239 333 -304 217 C ATOM 1922 C LEU A 261 1.816 3.904 43.086 1.00 14.89 C ANISOU 1922 C LEU A 261 1490 1627 2538 120 -246 155 C ATOM 1923 O LEU A 261 1.637 4.520 42.037 1.00 14.15 O ANISOU 1923 O LEU A 261 983 1912 2481 98 -131 148 O ATOM 1924 CB LEU A 261 -0.118 2.527 43.773 1.00 18.09 C ANISOU 1924 CB LEU A 261 2169 2107 2594 -135 -372 82 C ATOM 1925 CG LEU A 261 -1.468 2.235 44.431 1.00 21.62 C ANISOU 1925 CG LEU A 261 2456 2637 3120 -485 -110 -186 C ATOM 1926 CD1 LEU A 261 -2.118 1.058 43.724 1.00 25.48 C ANISOU 1926 CD1 LEU A 261 3018 3107 3554 -748 -398 -421 C ATOM 1927 CD2 LEU A 261 -1.312 1.917 45.902 1.00 24.82 C ANISOU 1927 CD2 LEU A 261 3048 3151 3230 -352 -193 -54 C ATOM 1928 N THR A 262 2.960 3.295 43.372 1.00 14.54 N ANISOU 1928 N THR A 262 1468 1824 2232 92 -234 259 N ATOM 1929 CA THR A 262 4.025 3.164 42.377 1.00 15.71 C ANISOU 1929 CA THR A 262 1619 1988 2361 5 -87 170 C ATOM 1930 C THR A 262 3.556 2.369 41.154 1.00 14.80 C ANISOU 1930 C THR A 262 1596 1917 2110 111 114 233 C ATOM 1931 O THR A 262 2.851 1.372 41.285 1.00 15.24 O ANISOU 1931 O THR A 262 1861 1778 2148 64 87 89 O ATOM 1932 CB THR A 262 5.249 2.447 42.983 1.00 16.85 C ANISOU 1932 CB THR A 262 1826 2046 2531 104 -187 237 C ATOM 1933 OG1 THR A 262 5.713 3.182 44.117 1.00 17.27 O ANISOU 1933 OG1 THR A 262 1945 2196 2421 20 219 76 O ATOM 1934 CG2 THR A 262 6.385 2.301 41.978 1.00 17.94 C ANISOU 1934 CG2 THR A 262 2194 2107 2514 -27 -13 85 C ATOM 1935 N GLY A 263 3.958 2.820 39.969 1.00 14.59 N ANISOU 1935 N GLY A 263 1650 1961 1931 151 42 112 N ATOM 1936 CA GLY A 263 3.707 2.073 38.735 1.00 14.34 C ANISOU 1936 CA GLY A 263 1660 1665 2121 113 67 42 C ATOM 1937 C GLY A 263 2.276 2.119 38.235 1.00 14.17 C ANISOU 1937 C GLY A 263 1657 1566 2159 -55 62 -78 C ATOM 1938 O GLY A 263 1.839 1.195 37.559 1.00 14.64 O ANISOU 1938 O GLY A 263 1487 1604 2470 -132 -25 -89 O ATOM 1939 N ARG A 264 1.554 3.191 38.560 1.00 14.03 N ANISOU 1939 N ARG A 264 1603 1575 2151 -41 97 -38 N ATOM 1940 CA ARG A 264 0.208 3.421 38.047 1.00 14.94 C ANISOU 1940 CA ARG A 264 1642 1830 2204 10 126 41 C ATOM 1941 C ARG A 264 0.130 4.587 37.040 1.00 15.54 C ANISOU 1941 C ARG A 264 1785 1820 2300 248 54 51 C ATOM 1942 O ARG A 264 -0.965 5.081 36.740 1.00 16.64 O ANISOU 1942 O ARG A 264 1757 1860 2703 262 66 174 O ATOM 1943 CB ARG A 264 -0.747 3.641 39.232 1.00 16.12 C ANISOU 1943 CB ARG A 264 1849 2133 2139 7 146 -108 C ATOM 1944 CG ARG A 264 -1.062 2.355 39.982 1.00 16.94 C ANISOU 1944 CG ARG A 264 1927 2349 2159 -33 -42 113 C ATOM 1945 CD ARG A 264 -2.099 1.523 39.245 1.00 17.61 C ANISOU 1945 CD ARG A 264 2165 2207 2317 -90 -68 62 C ATOM 1946 NE ARG A 264 -3.392 2.211 39.263 1.00 17.96 N ANISOU 1946 NE ARG A 264 1917 2327 2578 -251 -169 342 N ATOM 1947 CZ ARG A 264 -4.365 2.028 40.153 1.00 18.53 C ANISOU 1947 CZ ARG A 264 2055 2416 2567 -467 -111 219 C ATOM 1948 NH1 ARG A 264 -4.256 1.129 41.123 1.00 19.74 N ANISOU 1948 NH1 ARG A 264 2130 2318 3051 -187 146 392 N ATOM 1949 NH2 ARG A 264 -5.473 2.754 40.062 1.00 19.37 N ANISOU 1949 NH2 ARG A 264 1885 2604 2869 -574 -6 318 N ATOM 1950 N LYS A 265 1.286 5.005 36.519 1.00 14.97 N ANISOU 1950 N LYS A 265 2130 1426 2129 -46 134 -58 N ATOM 1951 CA LYS A 265 1.374 5.989 35.438 1.00 15.06 C ANISOU 1951 CA LYS A 265 2107 1579 2035 51 126 -37 C ATOM 1952 C LYS A 265 2.323 5.519 34.322 1.00 14.25 C ANISOU 1952 C LYS A 265 2062 1324 2027 -120 143 -76 C ATOM 1953 O LYS A 265 3.160 6.282 33.830 1.00 14.56 O ANISOU 1953 O LYS A 265 2367 1439 1726 -316 167 -139 O ATOM 1954 CB LYS A 265 1.800 7.345 36.019 1.00 14.80 C ANISOU 1954 CB LYS A 265 2001 1579 2043 116 302 -95 C ATOM 1955 CG LYS A 265 0.690 8.019 36.823 1.00 15.84 C ANISOU 1955 CG LYS A 265 2027 1875 2116 152 403 -103 C ATOM 1956 CD LYS A 265 -0.421 8.550 35.929 1.00 16.69 C ANISOU 1956 CD LYS A 265 2228 2019 2092 166 328 -85 C ATOM 1957 CE LYS A 265 -1.709 8.774 36.702 1.00 15.21 C ANISOU 1957 CE LYS A 265 2311 1590 1876 265 329 -21 C ATOM 1958 NZ LYS A 265 -2.455 7.513 36.967 1.00 17.45 N ANISOU 1958 NZ LYS A 265 2768 1637 2223 107 315 -30 N ATOM 1959 N ILE A 266 2.172 4.260 33.910 1.00 14.31 N ANISOU 1959 N ILE A 266 1893 1468 2075 -288 11 -214 N ATOM 1960 CA ILE A 266 3.154 3.636 33.001 1.00 15.02 C ANISOU 1960 CA ILE A 266 1897 1675 2134 -84 -11 -142 C ATOM 1961 C ILE A 266 3.098 4.179 31.565 1.00 14.72 C ANISOU 1961 C ILE A 266 1920 1482 2190 18 -49 -96 C ATOM 1962 O ILE A 266 4.087 4.112 30.840 1.00 16.12 O ANISOU 1962 O ILE A 266 1646 1910 2566 137 -110 79 O ATOM 1963 CB ILE A 266 3.095 2.081 33.011 1.00 15.88 C ANISOU 1963 CB ILE A 266 2007 1702 2325 -15 4 -47 C ATOM 1964 CG1 ILE A 266 1.832 1.543 32.322 1.00 17.22 C ANISOU 1964 CG1 ILE A 266 2176 2017 2346 -62 -158 -34 C ATOM 1965 CG2 ILE A 266 3.254 1.554 34.437 1.00 16.22 C ANISOU 1965 CG2 ILE A 266 1744 2054 2362 -28 67 68 C ATOM 1966 CD1 ILE A 266 1.745 0.030 32.316 1.00 18.86 C ANISOU 1966 CD1 ILE A 266 2539 2031 2593 -63 -78 23 C ATOM 1967 N ILE A 267 1.945 4.715 31.166 1.00 13.88 N ANISOU 1967 N ILE A 267 1651 1570 2052 -116 108 -125 N ATOM 1968 CA ILE A 267 1.767 5.317 29.840 1.00 14.00 C ANISOU 1968 CA ILE A 267 1746 1508 2065 2 126 -100 C ATOM 1969 C ILE A 267 2.252 6.776 29.821 1.00 13.70 C ANISOU 1969 C ILE A 267 1706 1523 1974 9 125 89 C ATOM 1970 O ILE A 267 2.873 7.214 28.849 1.00 14.60 O ANISOU 1970 O ILE A 267 1928 1598 2018 -32 179 201 O ATOM 1971 CB ILE A 267 0.303 5.163 29.373 1.00 14.75 C ANISOU 1971 CB ILE A 267 1800 1801 2003 -75 88 -35 C ATOM 1972 CG1 ILE A 267 -0.061 3.672 29.254 1.00 15.45 C ANISOU 1972 CG1 ILE A 267 1883 1858 2126 -172 109 -2 C ATOM 1973 CG2 ILE A 267 0.052 5.883 28.056 1.00 16.57 C ANISOU 1973 CG2 ILE A 267 2222 2046 2026 -137 -27 19 C ATOM 1974 CD1 ILE A 267 0.748 2.874 28.247 1.00 15.88 C ANISOU 1974 CD1 ILE A 267 1921 1956 2154 -253 141 -90 C ATOM 1975 N VAL A 268 1.995 7.509 30.902 1.00 13.52 N ANISOU 1975 N VAL A 268 1568 1480 2089 131 -31 6 N ATOM 1976 CA VAL A 268 2.605 8.829 31.133 1.00 13.39 C ANISOU 1976 CA VAL A 268 1438 1425 2223 145 -102 166 C ATOM 1977 C VAL A 268 4.142 8.725 31.161 1.00 13.38 C ANISOU 1977 C VAL A 268 1446 1333 2305 106 -62 154 C ATOM 1978 O VAL A 268 4.837 9.603 30.654 1.00 13.65 O ANISOU 1978 O VAL A 268 1560 1163 2460 282 180 205 O ATOM 1979 CB VAL A 268 2.075 9.454 32.448 1.00 15.27 C ANISOU 1979 CB VAL A 268 1885 1599 2318 -14 -19 11 C ATOM 1980 CG1 VAL A 268 2.897 10.660 32.899 1.00 16.28 C ANISOU 1980 CG1 VAL A 268 2166 1593 2426 -66 -35 -41 C ATOM 1981 CG2 VAL A 268 0.606 9.840 32.293 1.00 14.90 C ANISOU 1981 CG2 VAL A 268 2064 1324 2271 287 -118 -1 C ATOM 1982 N ASP A 269 4.655 7.639 31.744 1.00 14.19 N ANISOU 1982 N ASP A 269 1813 1292 2284 208 -77 98 N ATOM 1983 CA ASP A 269 6.108 7.397 31.805 1.00 15.23 C ANISOU 1983 CA ASP A 269 1703 1807 2275 -81 -20 -4 C ATOM 1984 C ASP A 269 6.775 7.104 30.457 1.00 15.83 C ANISOU 1984 C ASP A 269 2195 1620 2196 -174 10 -68 C ATOM 1985 O ASP A 269 8.005 7.244 30.332 1.00 16.00 O ANISOU 1985 O ASP A 269 2278 1487 2311 -360 207 -78 O ATOM 1986 CB ASP A 269 6.424 6.230 32.752 1.00 15.87 C ANISOU 1986 CB ASP A 269 1810 1658 2562 -35 -62 -7 C ATOM 1987 CG ASP A 269 6.385 6.623 34.220 1.00 16.51 C ANISOU 1987 CG ASP A 269 1987 1647 2640 -97 20 -84 C ATOM 1988 OD1 ASP A 269 6.514 7.823 34.550 1.00 16.56 O ANISOU 1988 OD1 ASP A 269 2076 1814 2402 -232 -42 -334 O ATOM 1989 OD2 ASP A 269 6.235 5.709 35.057 1.00 16.96 O ANISOU 1989 OD2 ASP A 269 1549 1705 3189 -75 49 178 O ATOM 1990 N THR A 270 5.979 6.688 29.472 1.00 14.49 N ANISOU 1990 N THR A 270 1806 1439 2257 -282 124 26 N ATOM 1991 CA THR A 270 6.483 6.192 28.197 1.00 15.32 C ANISOU 1991 CA THR A 270 1962 1601 2255 -188 81 -31 C ATOM 1992 C THR A 270 5.996 7.051 27.013 1.00 15.02 C ANISOU 1992 C THR A 270 1847 1532 2327 -192 18 -57 C ATOM 1993 O THR A 270 6.556 8.106 26.788 1.00 16.49 O ANISOU 1993 O THR A 270 2313 1569 2384 -167 223 296 O ATOM 1994 CB THR A 270 6.171 4.687 28.027 1.00 14.36 C ANISOU 1994 CB THR A 270 1607 1621 2227 -126 230 -186 C ATOM 1995 OG1 THR A 270 4.768 4.442 28.204 1.00 14.02 O ANISOU 1995 OG1 THR A 270 1328 1632 2367 238 -280 15 O ATOM 1996 CG2 THR A 270 6.955 3.866 29.050 1.00 16.97 C ANISOU 1996 CG2 THR A 270 2115 2007 2324 -84 66 -21 C ATOM 1997 N TYR A 271 4.971 6.623 26.271 1.00 14.17 N ANISOU 1997 N TYR A 271 1311 1583 2488 -45 133 106 N ATOM 1998 CA TYR A 271 4.679 7.219 24.960 1.00 13.39 C ANISOU 1998 CA TYR A 271 814 1805 2467 125 80 38 C ATOM 1999 C TYR A 271 3.255 7.765 24.807 1.00 14.68 C ANISOU 1999 C TYR A 271 1204 1847 2526 585 -61 77 C ATOM 2000 O TYR A 271 2.834 8.074 23.693 1.00 16.48 O ANISOU 2000 O TYR A 271 1404 2172 2683 176 -333 176 O ATOM 2001 CB TYR A 271 4.986 6.212 23.851 1.00 13.90 C ANISOU 2001 CB TYR A 271 1185 1822 2274 -4 50 89 C ATOM 2002 CG TYR A 271 6.388 5.646 23.938 1.00 14.64 C ANISOU 2002 CG TYR A 271 1377 1863 2320 214 -76 -68 C ATOM 2003 CD1 TYR A 271 7.501 6.445 23.683 1.00 15.52 C ANISOU 2003 CD1 TYR A 271 1665 1910 2321 55 -11 -25 C ATOM 2004 CD2 TYR A 271 6.605 4.320 24.293 1.00 16.04 C ANISOU 2004 CD2 TYR A 271 1839 1821 2431 29 -79 -45 C ATOM 2005 CE1 TYR A 271 8.788 5.935 23.772 1.00 14.27 C ANISOU 2005 CE1 TYR A 271 1529 1838 2053 -112 -101 -48 C ATOM 2006 CE2 TYR A 271 7.888 3.800 24.384 1.00 14.57 C ANISOU 2006 CE2 TYR A 271 1536 1824 2176 -304 -95 -152 C ATOM 2007 CZ TYR A 271 8.977 4.612 24.125 1.00 14.38 C ANISOU 2007 CZ TYR A 271 1648 1712 2102 -358 -153 -143 C ATOM 2008 OH TYR A 271 10.255 4.078 24.207 1.00 15.21 O ANISOU 2008 OH TYR A 271 1743 1907 2128 -166 144 -106 O ATOM 2009 N GLY A 272 2.541 7.912 25.922 1.00 14.06 N ANISOU 2009 N GLY A 272 1250 1642 2448 228 19 190 N ATOM 2010 CA GLY A 272 1.218 8.538 25.921 1.00 14.79 C ANISOU 2010 CA GLY A 272 1514 1737 2368 509 86 83 C ATOM 2011 C GLY A 272 0.158 7.882 25.064 1.00 15.04 C ANISOU 2011 C GLY A 272 1539 1706 2469 350 25 266 C ATOM 2012 O GLY A 272 -0.718 8.572 24.533 1.00 15.02 O ANISOU 2012 O GLY A 272 1077 1595 3033 321 88 96 O ATOM 2013 N GLY A 273 0.248 6.558 24.918 1.00 15.79 N ANISOU 2013 N GLY A 273 1799 1703 2496 164 154 164 N ATOM 2014 CA GLY A 273 -0.719 5.775 24.135 1.00 17.10 C ANISOU 2014 CA GLY A 273 2134 1795 2568 71 -65 228 C ATOM 2015 C GLY A 273 -0.203 5.344 22.771 1.00 16.70 C ANISOU 2015 C GLY A 273 2082 1684 2579 106 36 376 C ATOM 2016 O GLY A 273 -0.711 4.383 22.188 1.00 17.13 O ANISOU 2016 O GLY A 273 1773 1939 2794 -25 63 323 O ATOM 2017 N TRP A 274 0.791 6.059 22.245 1.00 16.60 N ANISOU 2017 N TRP A 274 2144 1753 2408 101 104 330 N ATOM 2018 CA TRP A 274 1.424 5.688 20.978 1.00 16.67 C ANISOU 2018 CA TRP A 274 2230 1752 2353 -150 98 266 C ATOM 2019 C TRP A 274 2.283 4.445 21.187 1.00 16.30 C ANISOU 2019 C TRP A 274 2079 1536 2577 -287 228 118 C ATOM 2020 O TRP A 274 2.710 4.160 22.304 1.00 16.42 O ANISOU 2020 O TRP A 274 2258 1408 2570 -204 242 66 O ATOM 2021 CB TRP A 274 2.309 6.824 20.451 1.00 14.41 C ANISOU 2021 CB TRP A 274 1671 1646 2157 55 -48 227 C ATOM 2022 CG TRP A 274 1.589 8.081 20.080 1.00 15.37 C ANISOU 2022 CG TRP A 274 1718 1702 2418 139 -130 219 C ATOM 2023 CD1 TRP A 274 1.281 9.119 20.904 1.00 16.30 C ANISOU 2023 CD1 TRP A 274 1983 1927 2284 327 -240 199 C ATOM 2024 CD2 TRP A 274 1.100 8.444 18.780 1.00 15.59 C ANISOU 2024 CD2 TRP A 274 1696 1866 2361 321 6 216 C ATOM 2025 NE1 TRP A 274 0.639 10.112 20.201 1.00 15.79 N ANISOU 2025 NE1 TRP A 274 1759 1677 2561 293 -49 219 N ATOM 2026 CE2 TRP A 274 0.518 9.724 18.895 1.00 15.61 C ANISOU 2026 CE2 TRP A 274 1445 1917 2569 308 22 114 C ATOM 2027 CE3 TRP A 274 1.104 7.814 17.526 1.00 16.83 C ANISOU 2027 CE3 TRP A 274 1796 2155 2442 525 -272 94 C ATOM 2028 CZ2 TRP A 274 -0.062 10.388 17.809 1.00 17.56 C ANISOU 2028 CZ2 TRP A 274 2052 2253 2364 350 9 91 C ATOM 2029 CZ3 TRP A 274 0.541 8.481 16.436 1.00 17.34 C ANISOU 2029 CZ3 TRP A 274 1915 2048 2624 613 -376 108 C ATOM 2030 CH2 TRP A 274 -0.051 9.753 16.592 1.00 17.93 C ANISOU 2030 CH2 TRP A 274 2170 2103 2539 627 -30 -51 C ATOM 2031 N GLY A 275 2.537 3.709 20.112 1.00 16.50 N ANISOU 2031 N GLY A 275 2165 1680 2422 -359 7 75 N ATOM 2032 CA GLY A 275 3.382 2.516 20.195 1.00 18.00 C ANISOU 2032 CA GLY A 275 2440 1634 2764 -305 75 12 C ATOM 2033 C GLY A 275 2.651 1.412 20.936 1.00 19.01 C ANISOU 2033 C GLY A 275 2459 1714 3047 -485 6 8 C ATOM 2034 O GLY A 275 1.597 0.993 20.506 1.00 22.07 O ANISOU 2034 O GLY A 275 2218 2359 3807 -224 -347 189 O ATOM 2035 N ALA A 276 3.209 0.957 22.056 1.00 19.63 N ANISOU 2035 N ALA A 276 2512 2111 2836 -220 145 -181 N ATOM 2036 CA ALA A 276 2.612 -0.131 22.840 1.00 18.90 C ANISOU 2036 CA ALA A 276 2359 1994 2824 -155 43 -244 C ATOM 2037 C ALA A 276 3.292 -0.189 24.194 1.00 17.91 C ANISOU 2037 C ALA A 276 2215 1829 2761 -91 142 -113 C ATOM 2038 O ALA A 276 4.322 0.463 24.398 1.00 18.84 O ANISOU 2038 O ALA A 276 2339 1905 2912 -308 258 -99 O ATOM 2039 CB ALA A 276 2.765 -1.461 22.114 1.00 18.60 C ANISOU 2039 CB ALA A 276 2367 1873 2826 -257 -47 -161 C ATOM 2040 N HIS A 277 2.727 -0.971 25.107 1.00 17.39 N ANISOU 2040 N HIS A 277 1997 1742 2866 -207 180 -181 N ATOM 2041 CA HIS A 277 3.327 -1.187 26.425 1.00 18.15 C ANISOU 2041 CA HIS A 277 2370 1652 2871 53 198 73 C ATOM 2042 C HIS A 277 3.186 -2.663 26.833 1.00 17.34 C ANISOU 2042 C HIS A 277 2271 1598 2717 276 238 41 C ATOM 2043 O HIS A 277 2.160 -3.299 26.558 1.00 15.88 O ANISOU 2043 O HIS A 277 1932 1274 2826 575 302 117 O ATOM 2044 CB HIS A 277 2.709 -0.230 27.468 1.00 19.19 C ANISOU 2044 CB HIS A 277 2701 1840 2748 43 281 36 C ATOM 2045 CG HIS A 277 3.637 0.119 28.591 1.00 20.07 C ANISOU 2045 CG HIS A 277 2711 2039 2872 268 191 -124 C ATOM 2046 ND1 HIS A 277 4.057 -0.809 29.511 1.00 19.83 N ANISOU 2046 ND1 HIS A 277 2898 1845 2791 252 264 -243 N ATOM 2047 CD2 HIS A 277 4.234 1.281 28.943 1.00 21.45 C ANISOU 2047 CD2 HIS A 277 3123 2021 3004 235 -44 -104 C ATOM 2048 CE1 HIS A 277 4.877 -0.248 30.378 1.00 19.87 C ANISOU 2048 CE1 HIS A 277 3333 1677 2537 365 17 -31 C ATOM 2049 NE2 HIS A 277 5.003 1.025 30.056 1.00 21.24 N ANISOU 2049 NE2 HIS A 277 3598 1631 2842 243 -32 -40 N ATOM 2050 N GLY A 278 4.246 -3.211 27.437 1.00 17.51 N ANISOU 2050 N GLY A 278 2332 1849 2472 242 227 112 N ATOM 2051 CA GLY A 278 4.262 -4.604 27.908 1.00 18.25 C ANISOU 2051 CA GLY A 278 2504 1712 2717 234 276 -63 C ATOM 2052 C GLY A 278 3.734 -4.847 29.322 1.00 19.19 C ANISOU 2052 C GLY A 278 2378 2189 2724 -1 341 -281 C ATOM 2053 O GLY A 278 3.569 -5.990 29.737 1.00 20.42 O ANISOU 2053 O GLY A 278 2282 2178 3298 182 465 -184 O ATOM 2054 N GLY A 279 3.540 -3.771 30.076 1.00 16.95 N ANISOU 2054 N GLY A 279 2210 1239 2990 -366 356 168 N ATOM 2055 CA GLY A 279 2.849 -3.770 31.371 1.00 18.15 C ANISOU 2055 CA GLY A 279 2106 1965 2824 -51 182 -186 C ATOM 2056 C GLY A 279 3.697 -3.456 32.593 1.00 17.84 C ANISOU 2056 C GLY A 279 2335 1774 2667 52 146 -85 C ATOM 2057 O GLY A 279 3.155 -3.156 33.645 1.00 17.74 O ANISOU 2057 O GLY A 279 1665 2253 2823 328 -90 -326 O ATOM 2058 N GLY A 280 5.021 -3.507 32.462 1.00 17.29 N ANISOU 2058 N GLY A 280 2339 1865 2364 261 -90 -67 N ATOM 2059 CA GLY A 280 5.917 -3.386 33.604 1.00 18.20 C ANISOU 2059 CA GLY A 280 2488 1767 2658 168 -323 -37 C ATOM 2060 C GLY A 280 6.197 -1.961 34.049 1.00 17.59 C ANISOU 2060 C GLY A 280 2315 1552 2816 332 -319 167 C ATOM 2061 O GLY A 280 6.436 -1.092 33.226 1.00 19.24 O ANISOU 2061 O GLY A 280 2667 1888 2753 -164 -344 140 O ATOM 2062 N ALA A 281 6.181 -1.725 35.358 1.00 17.20 N ANISOU 2062 N ALA A 281 2294 1429 2811 329 -226 207 N ATOM 2063 CA ALA A 281 6.462 -0.400 35.916 1.00 14.89 C ANISOU 2063 CA ALA A 281 2298 1015 2343 661 -568 728 C ATOM 2064 C ALA A 281 7.970 -0.200 35.951 1.00 15.02 C ANISOU 2064 C ALA A 281 2277 1354 2074 101 -200 80 C ATOM 2065 O ALA A 281 8.715 -1.179 36.000 1.00 14.83 O ANISOU 2065 O ALA A 281 1831 1100 2702 -220 -26 28 O ATOM 2066 CB ALA A 281 5.890 -0.297 37.316 1.00 15.51 C ANISOU 2066 CB ALA A 281 1691 1712 2487 313 -335 -3 C ATOM 2067 N PHE A 282 8.425 1.052 35.937 1.00 14.52 N ANISOU 2067 N PHE A 282 1592 1554 2369 -55 -147 -52 N ATOM 2068 CA PHE A 282 9.874 1.338 36.020 1.00 14.87 C ANISOU 2068 CA PHE A 282 1536 1742 2369 4 -75 -62 C ATOM 2069 C PHE A 282 10.401 1.603 37.436 1.00 15.63 C ANISOU 2069 C PHE A 282 1655 1890 2391 244 -203 83 C ATOM 2070 O PHE A 282 11.490 1.115 37.808 1.00 16.17 O ANISOU 2070 O PHE A 282 1386 2247 2511 144 -91 58 O ATOM 2071 CB PHE A 282 10.235 2.562 35.171 1.00 14.59 C ANISOU 2071 CB PHE A 282 1700 1582 2259 -13 -129 -167 C ATOM 2072 CG PHE A 282 9.994 2.415 33.682 1.00 14.43 C ANISOU 2072 CG PHE A 282 1722 1516 2244 48 -93 -149 C ATOM 2073 CD1 PHE A 282 10.059 1.183 33.016 1.00 14.19 C ANISOU 2073 CD1 PHE A 282 1912 1229 2249 43 -176 78 C ATOM 2074 CD2 PHE A 282 9.745 3.554 32.927 1.00 14.62 C ANISOU 2074 CD2 PHE A 282 1764 1636 2155 -101 -61 -18 C ATOM 2075 CE1 PHE A 282 9.861 1.111 31.647 1.00 14.77 C ANISOU 2075 CE1 PHE A 282 1807 1501 2301 97 -220 -211 C ATOM 2076 CE2 PHE A 282 9.546 3.487 31.556 1.00 14.97 C ANISOU 2076 CE2 PHE A 282 1831 1650 2206 -60 -202 -139 C ATOM 2077 CZ PHE A 282 9.607 2.262 30.912 1.00 15.13 C ANISOU 2077 CZ PHE A 282 1940 1674 2132 42 -206 -139 C ATOM 2078 N SER A 283 9.670 2.406 38.208 1.00 15.42 N ANISOU 2078 N SER A 283 1184 2029 2645 -56 6 4 N ATOM 2079 CA SER A 283 10.239 3.028 39.408 1.00 16.43 C ANISOU 2079 CA SER A 283 1848 2003 2391 130 33 23 C ATOM 2080 C SER A 283 10.390 2.050 40.561 1.00 15.84 C ANISOU 2080 C SER A 283 1613 2225 2177 14 91 -20 C ATOM 2081 O SER A 283 9.548 1.167 40.757 1.00 16.34 O ANISOU 2081 O SER A 283 920 2331 2956 175 -240 24 O ATOM 2082 CB SER A 283 9.431 4.260 39.843 1.00 15.76 C ANISOU 2082 CB SER A 283 2002 1852 2133 -25 76 -30 C ATOM 2083 OG SER A 283 9.641 5.357 38.960 1.00 16.07 O ANISOU 2083 OG SER A 283 2174 1583 2348 30 -59 -38 O ATOM 2084 N GLY A 284 11.476 2.215 41.313 1.00 15.94 N ANISOU 2084 N GLY A 284 1563 2140 2350 186 1 69 N ATOM 2085 CA GLY A 284 11.774 1.372 42.468 1.00 14.98 C ANISOU 2085 CA GLY A 284 1747 1761 2183 202 36 -159 C ATOM 2086 C GLY A 284 12.523 0.092 42.145 1.00 16.25 C ANISOU 2086 C GLY A 284 1945 1860 2366 336 56 -236 C ATOM 2087 O GLY A 284 12.677 -0.754 43.029 1.00 18.61 O ANISOU 2087 O GLY A 284 2322 2109 2640 256 -90 -23 O ATOM 2088 N LYS A 285 12.994 -0.043 40.901 1.00 14.72 N ANISOU 2088 N LYS A 285 1509 1652 2430 378 143 -27 N ATOM 2089 CA LYS A 285 13.628 -1.276 40.401 1.00 14.04 C ANISOU 2089 CA LYS A 285 1693 1596 2044 267 172 -91 C ATOM 2090 C LYS A 285 15.062 -1.055 39.911 1.00 15.30 C ANISOU 2090 C LYS A 285 1691 1793 2327 214 170 -104 C ATOM 2091 O LYS A 285 15.308 -0.160 39.109 1.00 15.90 O ANISOU 2091 O LYS A 285 1804 1545 2690 201 173 -98 O ATOM 2092 CB LYS A 285 12.816 -1.838 39.244 1.00 13.86 C ANISOU 2092 CB LYS A 285 1431 1695 2140 231 195 -99 C ATOM 2093 CG LYS A 285 11.387 -2.209 39.612 1.00 15.08 C ANISOU 2093 CG LYS A 285 1655 1865 2211 -48 319 -91 C ATOM 2094 CD LYS A 285 10.658 -2.771 38.409 1.00 16.38 C ANISOU 2094 CD LYS A 285 2083 1863 2277 13 154 -124 C ATOM 2095 CE LYS A 285 9.226 -3.136 38.749 1.00 15.69 C ANISOU 2095 CE LYS A 285 2074 1368 2517 447 457 -338 C ATOM 2096 NZ LYS A 285 8.514 -3.548 37.518 1.00 18.34 N ANISOU 2096 NZ LYS A 285 2324 2043 2599 -79 289 -33 N ATOM 2097 N ASP A 286 15.993 -1.898 40.365 1.00 16.08 N ANISOU 2097 N ASP A 286 1872 1923 2313 288 76 -92 N ATOM 2098 CA ASP A 286 17.366 -1.919 39.833 1.00 16.24 C ANISOU 2098 CA ASP A 286 1731 2003 2434 161 -44 -27 C ATOM 2099 C ASP A 286 17.446 -2.567 38.435 1.00 16.17 C ANISOU 2099 C ASP A 286 1521 2152 2468 165 -112 -61 C ATOM 2100 O ASP A 286 16.461 -3.137 37.925 1.00 14.33 O ANISOU 2100 O ASP A 286 980 1897 2566 602 -134 35 O ATOM 2101 CB ASP A 286 18.315 -2.646 40.802 1.00 16.42 C ANISOU 2101 CB ASP A 286 1696 2232 2310 311 -69 -222 C ATOM 2102 CG ASP A 286 18.087 -4.144 40.834 1.00 16.53 C ANISOU 2102 CG ASP A 286 1773 2166 2340 618 11 -185 C ATOM 2103 OD1 ASP A 286 17.217 -4.580 41.618 1.00 17.66 O ANISOU 2103 OD1 ASP A 286 1957 2095 2654 401 12 -15 O ATOM 2104 OD2 ASP A 286 18.767 -4.882 40.078 1.00 17.40 O ANISOU 2104 OD2 ASP A 286 1413 2407 2789 951 103 -21 O ATOM 2105 N TYR A 287 18.644 -2.518 37.843 1.00 16.34 N ANISOU 2105 N TYR A 287 1428 2071 2707 128 -127 27 N ATOM 2106 CA TYR A 287 18.842 -2.894 36.435 1.00 17.04 C ANISOU 2106 CA TYR A 287 1695 2074 2703 -63 -57 78 C ATOM 2107 C TYR A 287 18.539 -4.359 36.084 1.00 17.04 C ANISOU 2107 C TYR A 287 1778 2040 2654 5 -6 58 C ATOM 2108 O TYR A 287 18.272 -4.651 34.915 1.00 18.91 O ANISOU 2108 O TYR A 287 2407 2052 2724 -581 -36 70 O ATOM 2109 CB TYR A 287 20.258 -2.543 35.966 1.00 17.65 C ANISOU 2109 CB TYR A 287 1776 2277 2652 14 88 133 C ATOM 2110 CG TYR A 287 21.295 -3.566 36.352 1.00 19.23 C ANISOU 2110 CG TYR A 287 2266 2095 2944 325 245 -55 C ATOM 2111 CD1 TYR A 287 21.956 -3.491 37.571 1.00 21.03 C ANISOU 2111 CD1 TYR A 287 2372 2565 3050 450 128 16 C ATOM 2112 CD2 TYR A 287 21.596 -4.632 35.500 1.00 20.40 C ANISOU 2112 CD2 TYR A 287 2157 2508 3086 478 326 -276 C ATOM 2113 CE1 TYR A 287 22.899 -4.437 37.930 1.00 21.42 C ANISOU 2113 CE1 TYR A 287 2345 2683 3108 574 526 254 C ATOM 2114 CE2 TYR A 287 22.531 -5.583 35.854 1.00 22.07 C ANISOU 2114 CE2 TYR A 287 2389 2505 3492 538 487 113 C ATOM 2115 CZ TYR A 287 23.178 -5.481 37.069 1.00 21.58 C ANISOU 2115 CZ TYR A 287 2441 2227 3531 393 438 288 C ATOM 2116 OH TYR A 287 24.117 -6.421 37.412 1.00 27.41 O ANISOU 2116 OH TYR A 287 2981 2505 4929 611 344 1013 O ATOM 2117 N THR A 288 18.582 -5.267 37.066 1.00 15.45 N ANISOU 2117 N THR A 288 1522 1935 2414 45 -120 -67 N ATOM 2118 CA THR A 288 18.267 -6.684 36.807 1.00 16.77 C ANISOU 2118 CA THR A 288 1933 1869 2568 66 32 8 C ATOM 2119 C THR A 288 16.786 -6.903 36.495 1.00 16.60 C ANISOU 2119 C THR A 288 1899 1734 2673 160 43 32 C ATOM 2120 O THR A 288 16.421 -7.928 35.915 1.00 15.50 O ANISOU 2120 O THR A 288 1133 1498 3255 93 95 155 O ATOM 2121 CB THR A 288 18.686 -7.626 37.957 1.00 18.80 C ANISOU 2121 CB THR A 288 2297 2313 2530 49 -167 86 C ATOM 2122 OG1 THR A 288 17.917 -7.349 39.142 1.00 18.95 O ANISOU 2122 OG1 THR A 288 1921 2331 2947 249 -62 15 O ATOM 2123 CG2 THR A 288 20.181 -7.492 38.245 1.00 19.11 C ANISOU 2123 CG2 THR A 288 2237 2312 2710 121 -57 20 C ATOM 2124 N LYS A 289 15.945 -5.945 36.884 1.00 16.11 N ANISOU 2124 N LYS A 289 2014 1621 2486 143 113 94 N ATOM 2125 CA LYS A 289 14.539 -5.944 36.490 1.00 17.80 C ANISOU 2125 CA LYS A 289 2135 2041 2587 43 -73 11 C ATOM 2126 C LYS A 289 14.441 -5.381 35.063 1.00 16.79 C ANISOU 2126 C LYS A 289 2099 1810 2470 49 -118 -245 C ATOM 2127 O LYS A 289 14.483 -4.151 34.851 1.00 16.37 O ANISOU 2127 O LYS A 289 1739 1813 2664 167 -395 -104 O ATOM 2128 CB LYS A 289 13.687 -5.121 37.464 1.00 17.46 C ANISOU 2128 CB LYS A 289 2016 1888 2730 -69 39 34 C ATOM 2129 CG LYS A 289 13.390 -5.797 38.804 1.00 18.31 C ANISOU 2129 CG LYS A 289 2320 1870 2766 -115 -31 59 C ATOM 2130 CD LYS A 289 14.618 -5.960 39.681 1.00 18.92 C ANISOU 2130 CD LYS A 289 2453 1868 2865 -18 -125 120 C ATOM 2131 CE LYS A 289 14.256 -6.292 41.118 1.00 20.64 C ANISOU 2131 CE LYS A 289 2746 2127 2968 -21 64 140 C ATOM 2132 NZ LYS A 289 15.458 -6.686 41.905 1.00 20.60 N ANISOU 2132 NZ LYS A 289 2847 2254 2725 -349 -63 189 N ATOM 2133 N VAL A 290 14.341 -6.302 34.104 1.00 15.66 N ANISOU 2133 N VAL A 290 1730 1630 2589 146 -31 -286 N ATOM 2134 CA VAL A 290 14.218 -5.990 32.675 1.00 15.38 C ANISOU 2134 CA VAL A 290 1550 1648 2644 324 -43 -155 C ATOM 2135 C VAL A 290 13.012 -5.108 32.293 1.00 15.97 C ANISOU 2135 C VAL A 290 1640 1730 2697 322 -176 -63 C ATOM 2136 O VAL A 290 13.038 -4.468 31.245 1.00 15.90 O ANISOU 2136 O VAL A 290 1748 1526 2766 284 -36 -99 O ATOM 2137 CB VAL A 290 14.252 -7.260 31.772 1.00 15.11 C ANISOU 2137 CB VAL A 290 1605 1879 2255 40 -47 -183 C ATOM 2138 CG1 VAL A 290 15.668 -7.832 31.708 1.00 15.00 C ANISOU 2138 CG1 VAL A 290 1471 1921 2308 -107 -26 -172 C ATOM 2139 CG2 VAL A 290 13.258 -8.327 32.220 1.00 15.85 C ANISOU 2139 CG2 VAL A 290 2036 1683 2300 1 -6 -128 C ATOM 2140 N ASP A 291 11.967 -5.068 33.117 1.00 15.85 N ANISOU 2140 N ASP A 291 2120 1589 2311 175 -45 -219 N ATOM 2141 CA ASP A 291 10.903 -4.058 32.940 1.00 15.62 C ANISOU 2141 CA ASP A 291 2031 1496 2407 16 -113 -38 C ATOM 2142 C ASP A 291 11.478 -2.670 32.693 1.00 16.73 C ANISOU 2142 C ASP A 291 2391 1537 2427 -30 84 60 C ATOM 2143 O ASP A 291 10.968 -1.926 31.861 1.00 18.78 O ANISOU 2143 O ASP A 291 2297 1853 2984 54 42 366 O ATOM 2144 CB ASP A 291 10.028 -3.967 34.182 1.00 16.34 C ANISOU 2144 CB ASP A 291 2060 1666 2481 -343 -12 -1 C ATOM 2145 CG ASP A 291 9.041 -5.108 34.295 1.00 17.52 C ANISOU 2145 CG ASP A 291 2107 2078 2472 -609 -37 -33 C ATOM 2146 OD1 ASP A 291 8.663 -5.721 33.276 1.00 17.15 O ANISOU 2146 OD1 ASP A 291 2162 1644 2708 -692 -179 12 O ATOM 2147 OD2 ASP A 291 8.641 -5.376 35.431 1.00 20.49 O ANISOU 2147 OD2 ASP A 291 2489 2409 2886 -198 646 54 O ATOM 2148 N ARG A 292 12.526 -2.330 33.439 1.00 16.91 N ANISOU 2148 N ARG A 292 2397 1528 2498 -137 99 55 N ATOM 2149 CA ARG A 292 13.216 -1.057 33.281 1.00 17.98 C ANISOU 2149 CA ARG A 292 2693 1611 2525 -249 50 211 C ATOM 2150 C ARG A 292 14.362 -1.137 32.265 1.00 17.28 C ANISOU 2150 C ARG A 292 2385 1392 2788 104 -41 120 C ATOM 2151 O ARG A 292 14.298 -0.483 31.223 1.00 16.84 O ANISOU 2151 O ARG A 292 2441 1340 2613 68 129 -36 O ATOM 2152 CB ARG A 292 13.713 -0.556 34.636 1.00 18.89 C ANISOU 2152 CB ARG A 292 2619 1975 2582 -223 41 86 C ATOM 2153 CG ARG A 292 14.211 0.872 34.592 1.00 21.10 C ANISOU 2153 CG ARG A 292 3140 2032 2843 -335 120 84 C ATOM 2154 CD ARG A 292 14.511 1.408 35.982 1.00 22.62 C ANISOU 2154 CD ARG A 292 3257 2491 2845 -193 243 -71 C ATOM 2155 NE ARG A 292 14.100 2.798 36.091 1.00 19.88 N ANISOU 2155 NE ARG A 292 2423 2524 2606 -227 290 -307 N ATOM 2156 CZ ARG A 292 13.838 3.439 37.224 1.00 18.40 C ANISOU 2156 CZ ARG A 292 2412 2140 2439 -203 302 -50 C ATOM 2157 NH1 ARG A 292 13.976 2.847 38.405 1.00 18.17 N ANISOU 2157 NH1 ARG A 292 2477 1694 2733 -379 159 132 N ATOM 2158 NH2 ARG A 292 13.463 4.716 37.166 1.00 20.34 N ANISOU 2158 NH2 ARG A 292 2557 2285 2886 77 282 76 N ATOM 2159 N SER A 293 15.399 -1.930 32.553 1.00 17.05 N ANISOU 2159 N SER A 293 2425 1344 2708 112 -34 145 N ATOM 2160 CA SER A 293 16.597 -1.953 31.704 1.00 17.91 C ANISOU 2160 CA SER A 293 2530 1605 2669 323 25 208 C ATOM 2161 C SER A 293 16.293 -2.272 30.240 1.00 14.98 C ANISOU 2161 C SER A 293 1910 1149 2630 55 165 342 C ATOM 2162 O SER A 293 16.836 -1.618 29.345 1.00 15.58 O ANISOU 2162 O SER A 293 1603 1405 2908 -46 235 481 O ATOM 2163 CB SER A 293 17.675 -2.904 32.251 1.00 16.76 C ANISOU 2163 CB SER A 293 1901 2038 2429 123 -85 101 C ATOM 2164 OG SER A 293 17.175 -4.217 32.458 1.00 18.12 O ANISOU 2164 OG SER A 293 1091 2748 3046 -621 -48 161 O ATOM 2165 N ALA A 294 15.424 -3.251 29.989 1.00 14.54 N ANISOU 2165 N ALA A 294 1572 1201 2750 188 208 140 N ATOM 2166 CA ALA A 294 15.117 -3.631 28.602 1.00 15.73 C ANISOU 2166 CA ALA A 294 1923 1312 2740 -157 259 107 C ATOM 2167 C ALA A 294 14.211 -2.629 27.902 1.00 15.10 C ANISOU 2167 C ALA A 294 1781 1120 2833 -148 356 -9 C ATOM 2168 O ALA A 294 14.349 -2.458 26.693 1.00 14.56 O ANISOU 2168 O ALA A 294 1475 1143 2912 -152 293 108 O ATOM 2169 CB ALA A 294 14.531 -5.040 28.502 1.00 14.30 C ANISOU 2169 CB ALA A 294 1828 1350 2253 -142 185 -100 C ATOM 2170 N ALA A 295 13.280 -1.993 28.629 1.00 14.48 N ANISOU 2170 N ALA A 295 1637 1415 2448 -298 323 -3 N ATOM 2171 CA ALA A 295 12.474 -0.906 28.038 1.00 15.15 C ANISOU 2171 CA ALA A 295 1845 1587 2323 -174 185 -26 C ATOM 2172 C ALA A 295 13.351 0.288 27.657 1.00 14.83 C ANISOU 2172 C ALA A 295 1627 1559 2447 -159 105 -120 C ATOM 2173 O ALA A 295 13.179 0.871 26.579 1.00 15.60 O ANISOU 2173 O ALA A 295 1992 1322 2611 -270 234 40 O ATOM 2174 CB ALA A 295 11.354 -0.463 28.967 1.00 16.14 C ANISOU 2174 CB ALA A 295 1976 1804 2352 -91 173 -149 C ATOM 2175 N TYR A 296 14.288 0.640 28.535 1.00 13.86 N ANISOU 2175 N TYR A 296 1499 1406 2360 -314 194 52 N ATOM 2176 CA TYR A 296 15.285 1.689 28.237 1.00 15.09 C ANISOU 2176 CA TYR A 296 1542 1511 2677 -368 276 130 C ATOM 2177 C TYR A 296 16.142 1.329 27.000 1.00 15.16 C ANISOU 2177 C TYR A 296 1713 1485 2562 -355 209 125 C ATOM 2178 O TYR A 296 16.337 2.160 26.111 1.00 14.50 O ANISOU 2178 O TYR A 296 1698 1337 2473 -97 132 97 O ATOM 2179 CB TYR A 296 16.181 1.948 29.461 1.00 15.28 C ANISOU 2179 CB TYR A 296 822 1856 3127 -782 285 49 C ATOM 2180 CG TYR A 296 15.558 2.720 30.635 1.00 16.47 C ANISOU 2180 CG TYR A 296 1633 1772 2852 -163 57 210 C ATOM 2181 CD1 TYR A 296 14.179 2.996 30.710 1.00 15.78 C ANISOU 2181 CD1 TYR A 296 1736 1711 2549 48 25 -181 C ATOM 2182 CD2 TYR A 296 16.365 3.161 31.688 1.00 17.61 C ANISOU 2182 CD2 TYR A 296 2090 1887 2712 11 64 -86 C ATOM 2183 CE1 TYR A 296 13.643 3.695 31.788 1.00 16.41 C ANISOU 2183 CE1 TYR A 296 1814 1834 2585 253 239 -1 C ATOM 2184 CE2 TYR A 296 15.836 3.858 32.767 1.00 17.20 C ANISOU 2184 CE2 TYR A 296 1730 2190 2613 313 -14 70 C ATOM 2185 CZ TYR A 296 14.474 4.124 32.814 1.00 17.11 C ANISOU 2185 CZ TYR A 296 1744 2093 2662 323 187 -40 C ATOM 2186 OH TYR A 296 13.957 4.810 33.897 1.00 14.89 O ANISOU 2186 OH TYR A 296 787 2187 2681 -21 68 -137 O ATOM 2187 N ALA A 297 16.647 0.099 26.943 1.00 16.77 N ANISOU 2187 N ALA A 297 1882 1626 2864 -164 136 100 N ATOM 2188 CA ALA A 297 17.379 -0.371 25.752 1.00 16.81 C ANISOU 2188 CA ALA A 297 2006 1601 2778 -113 77 166 C ATOM 2189 C ALA A 297 16.526 -0.353 24.480 1.00 16.81 C ANISOU 2189 C ALA A 297 2069 1542 2773 -180 40 183 C ATOM 2190 O ALA A 297 17.016 -0.003 23.414 1.00 14.95 O ANISOU 2190 O ALA A 297 1610 1198 2869 -298 32 90 O ATOM 2191 CB ALA A 297 17.951 -1.761 25.973 1.00 17.65 C ANISOU 2191 CB ALA A 297 2402 1738 2565 134 27 187 C ATOM 2192 N ALA A 298 15.255 -0.731 24.592 1.00 16.16 N ANISOU 2192 N ALA A 298 2025 1676 2439 -155 -90 136 N ATOM 2193 CA ALA A 298 14.363 -0.733 23.432 1.00 15.36 C ANISOU 2193 CA ALA A 298 1806 1635 2393 -39 -9 130 C ATOM 2194 C ALA A 298 14.098 0.683 22.893 1.00 14.77 C ANISOU 2194 C ALA A 298 1694 1502 2416 -194 153 79 C ATOM 2195 O ALA A 298 13.999 0.879 21.675 1.00 13.60 O ANISOU 2195 O ALA A 298 1153 1591 2423 113 311 176 O ATOM 2196 CB ALA A 298 13.055 -1.436 23.766 1.00 15.20 C ANISOU 2196 CB ALA A 298 1955 1665 2155 -217 -83 84 C ATOM 2197 N ARG A 299 13.963 1.658 23.794 1.00 14.53 N ANISOU 2197 N ARG A 299 1862 1297 2362 -211 238 210 N ATOM 2198 CA ARG A 299 13.898 3.084 23.410 1.00 14.38 C ANISOU 2198 CA ARG A 299 1815 1230 2418 -165 225 104 C ATOM 2199 C ARG A 299 15.169 3.493 22.655 1.00 15.42 C ANISOU 2199 C ARG A 299 1804 1540 2513 -250 282 -57 C ATOM 2200 O ARG A 299 15.123 4.162 21.611 1.00 14.36 O ANISOU 2200 O ARG A 299 1441 1323 2689 -539 0 -12 O ATOM 2201 CB ARG A 299 13.742 3.965 24.664 1.00 15.68 C ANISOU 2201 CB ARG A 299 2112 1409 2436 87 118 67 C ATOM 2202 CG ARG A 299 14.042 5.453 24.473 1.00 16.01 C ANISOU 2202 CG ARG A 299 2265 1474 2344 -80 163 0 C ATOM 2203 CD ARG A 299 13.103 6.096 23.465 1.00 17.03 C ANISOU 2203 CD ARG A 299 2283 1801 2387 58 84 -54 C ATOM 2204 NE ARG A 299 13.336 7.532 23.366 1.00 15.92 N ANISOU 2204 NE ARG A 299 1960 1808 2281 125 -258 126 N ATOM 2205 CZ ARG A 299 12.778 8.354 22.476 1.00 16.44 C ANISOU 2205 CZ ARG A 299 2256 2007 1982 280 -284 45 C ATOM 2206 NH1 ARG A 299 11.922 7.910 21.561 1.00 18.87 N ANISOU 2206 NH1 ARG A 299 2996 2060 2112 117 -1273 1339 N ATOM 2207 NH2 ARG A 299 13.089 9.651 22.504 1.00 14.77 N ANISOU 2207 NH2 ARG A 299 1527 2156 1927 96 -1365 -442 N ATOM 2208 N TRP A 300 16.301 3.102 23.227 1.00 15.54 N ANISOU 2208 N TRP A 300 1805 1732 2366 -314 274 2 N ATOM 2209 CA TRP A 300 17.622 3.346 22.638 1.00 16.58 C ANISOU 2209 CA TRP A 300 1646 1994 2659 -574 137 -127 C ATOM 2210 C TRP A 300 17.731 2.795 21.208 1.00 16.08 C ANISOU 2210 C TRP A 300 1655 1656 2798 -546 119 -225 C ATOM 2211 O TRP A 300 18.240 3.473 20.313 1.00 17.05 O ANISOU 2211 O TRP A 300 1963 1461 3052 -609 219 -211 O ATOM 2212 CB TRP A 300 18.678 2.725 23.543 1.00 16.11 C ANISOU 2212 CB TRP A 300 1638 2084 2399 -628 214 -158 C ATOM 2213 CG TRP A 300 20.109 3.067 23.251 1.00 16.48 C ANISOU 2213 CG TRP A 300 1576 1946 2737 -570 222 -222 C ATOM 2214 CD1 TRP A 300 20.612 4.259 22.816 1.00 16.86 C ANISOU 2214 CD1 TRP A 300 1930 1720 2756 -320 274 -201 C ATOM 2215 CD2 TRP A 300 21.227 2.196 23.435 1.00 17.73 C ANISOU 2215 CD2 TRP A 300 1644 2130 2961 -457 312 -197 C ATOM 2216 NE1 TRP A 300 21.990 4.178 22.701 1.00 17.73 N ANISOU 2216 NE1 TRP A 300 1968 1809 2957 -120 381 -227 N ATOM 2217 CE2 TRP A 300 22.390 2.922 23.082 1.00 17.55 C ANISOU 2217 CE2 TRP A 300 1927 1741 2999 -453 410 -36 C ATOM 2218 CE3 TRP A 300 21.359 0.872 23.872 1.00 17.22 C ANISOU 2218 CE3 TRP A 300 962 2222 3356 -776 447 65 C ATOM 2219 CZ2 TRP A 300 23.675 2.356 23.141 1.00 19.03 C ANISOU 2219 CZ2 TRP A 300 2304 1933 2992 -36 181 -52 C ATOM 2220 CZ3 TRP A 300 22.637 0.305 23.928 1.00 19.07 C ANISOU 2220 CZ3 TRP A 300 1933 2134 3177 244 311 33 C ATOM 2221 CH2 TRP A 300 23.777 1.051 23.567 1.00 19.62 C ANISOU 2221 CH2 TRP A 300 2237 2057 3159 31 221 97 C ATOM 2222 N VAL A 301 17.221 1.584 20.992 1.00 15.34 N ANISOU 2222 N VAL A 301 1602 1572 2655 -552 36 82 N ATOM 2223 CA VAL A 301 17.198 0.969 19.661 1.00 15.57 C ANISOU 2223 CA VAL A 301 1549 1719 2647 -472 -44 78 C ATOM 2224 C VAL A 301 16.298 1.780 18.733 1.00 15.03 C ANISOU 2224 C VAL A 301 1286 1710 2712 -370 121 98 C ATOM 2225 O VAL A 301 16.699 2.129 17.628 1.00 15.37 O ANISOU 2225 O VAL A 301 1250 1684 2906 -265 163 278 O ATOM 2226 CB VAL A 301 16.701 -0.507 19.700 1.00 17.39 C ANISOU 2226 CB VAL A 301 2112 1767 2727 -622 -28 21 C ATOM 2227 CG1 VAL A 301 16.519 -1.070 18.295 1.00 17.97 C ANISOU 2227 CG1 VAL A 301 1961 2238 2627 -406 -167 59 C ATOM 2228 CG2 VAL A 301 17.680 -1.390 20.460 1.00 18.91 C ANISOU 2228 CG2 VAL A 301 2539 1905 2738 -278 8 -45 C ATOM 2229 N ALA A 302 15.073 2.053 19.184 1.00 14.59 N ANISOU 2229 N ALA A 302 1361 1884 2297 -193 90 185 N ATOM 2230 CA ALA A 302 14.107 2.816 18.387 1.00 14.35 C ANISOU 2230 CA ALA A 302 1458 1876 2115 -303 26 220 C ATOM 2231 C ALA A 302 14.646 4.195 17.995 1.00 15.68 C ANISOU 2231 C ALA A 302 1734 1862 2360 -310 128 251 C ATOM 2232 O ALA A 302 14.591 4.584 16.824 1.00 15.60 O ANISOU 2232 O ALA A 302 1905 1627 2394 -250 101 245 O ATOM 2233 CB ALA A 302 12.788 2.952 19.137 1.00 15.03 C ANISOU 2233 CB ALA A 302 1774 1961 1975 18 216 260 C ATOM 2234 N LYS A 303 15.189 4.918 18.966 1.00 15.44 N ANISOU 2234 N LYS A 303 1782 1677 2406 -361 197 260 N ATOM 2235 CA LYS A 303 15.761 6.233 18.683 1.00 17.28 C ANISOU 2235 CA LYS A 303 1920 1890 2753 -594 338 310 C ATOM 2236 C LYS A 303 17.001 6.159 17.762 1.00 18.41 C ANISOU 2236 C LYS A 303 2202 1918 2871 -293 527 45 C ATOM 2237 O LYS A 303 17.203 7.044 16.920 1.00 18.04 O ANISOU 2237 O LYS A 303 1882 1642 3330 -223 375 137 O ATOM 2238 CB LYS A 303 16.089 6.980 19.973 1.00 19.11 C ANISOU 2238 CB LYS A 303 2526 1928 2805 -628 255 316 C ATOM 2239 CG LYS A 303 16.355 8.462 19.734 1.00 20.32 C ANISOU 2239 CG LYS A 303 2825 1855 3039 -619 -10 220 C ATOM 2240 CD LYS A 303 16.351 9.243 21.025 1.00 21.62 C ANISOU 2240 CD LYS A 303 2692 2341 3179 -384 -37 4 C ATOM 2241 CE LYS A 303 16.612 10.718 20.761 1.00 22.55 C ANISOU 2241 CE LYS A 303 2614 2420 3535 -448 -102 159 C ATOM 2242 NZ LYS A 303 16.856 11.440 22.033 1.00 21.94 N ANISOU 2242 NZ LYS A 303 2554 2322 3459 -375 -49 217 N ATOM 2243 N SER A 304 17.808 5.108 17.909 1.00 19.17 N ANISOU 2243 N SER A 304 2457 1865 2961 -263 354 128 N ATOM 2244 CA SER A 304 18.954 4.886 17.022 1.00 17.50 C ANISOU 2244 CA SER A 304 2159 1427 3060 -398 224 53 C ATOM 2245 C SER A 304 18.530 4.622 15.571 1.00 18.10 C ANISOU 2245 C SER A 304 2091 1767 3018 -498 213 114 C ATOM 2246 O SER A 304 19.187 5.077 14.644 1.00 17.42 O ANISOU 2246 O SER A 304 1960 1650 3006 -600 88 141 O ATOM 2247 CB SER A 304 19.831 3.738 17.532 1.00 19.48 C ANISOU 2247 CB SER A 304 2296 1855 3249 -86 321 198 C ATOM 2248 OG SER A 304 20.385 4.044 18.799 1.00 17.95 O ANISOU 2248 OG SER A 304 1741 1438 3637 -191 247 -40 O ATOM 2249 N LEU A 305 17.428 3.898 15.375 1.00 16.54 N ANISOU 2249 N LEU A 305 1921 1590 2772 -289 172 72 N ATOM 2250 CA LEU A 305 16.919 3.640 14.018 1.00 17.84 C ANISOU 2250 CA LEU A 305 2254 1874 2648 -260 197 104 C ATOM 2251 C LEU A 305 16.409 4.920 13.333 1.00 18.45 C ANISOU 2251 C LEU A 305 2559 2099 2351 -194 177 197 C ATOM 2252 O LEU A 305 16.663 5.141 12.143 1.00 19.71 O ANISOU 2252 O LEU A 305 3130 1959 2401 -134 446 139 O ATOM 2253 CB LEU A 305 15.823 2.569 14.049 1.00 17.28 C ANISOU 2253 CB LEU A 305 2101 2012 2452 -244 12 11 C ATOM 2254 CG LEU A 305 16.272 1.141 14.378 1.00 16.87 C ANISOU 2254 CG LEU A 305 1949 2032 2426 -236 106 -4 C ATOM 2255 CD1 LEU A 305 15.064 0.250 14.649 1.00 16.85 C ANISOU 2255 CD1 LEU A 305 2034 1777 2589 -196 158 -31 C ATOM 2256 CD2 LEU A 305 17.122 0.567 13.250 1.00 19.12 C ANISOU 2256 CD2 LEU A 305 2207 2359 2696 5 223 -87 C ATOM 2257 N VAL A 306 15.716 5.769 14.094 1.00 17.67 N ANISOU 2257 N VAL A 306 2383 1883 2448 -181 44 261 N ATOM 2258 CA VAL A 306 15.156 7.014 13.558 1.00 16.50 C ANISOU 2258 CA VAL A 306 2118 1875 2274 -303 -15 303 C ATOM 2259 C VAL A 306 16.248 8.067 13.325 1.00 16.83 C ANISOU 2259 C VAL A 306 2283 1968 2144 -433 -72 396 C ATOM 2260 O VAL A 306 16.397 8.569 12.211 1.00 16.36 O ANISOU 2260 O VAL A 306 1971 1893 2350 -280 252 529 O ATOM 2261 CB VAL A 306 14.011 7.538 14.446 1.00 15.83 C ANISOU 2261 CB VAL A 306 2240 1492 2280 -68 -139 334 C ATOM 2262 CG1 VAL A 306 13.516 8.898 13.965 1.00 16.41 C ANISOU 2262 CG1 VAL A 306 2160 1580 2494 150 -151 263 C ATOM 2263 CG2 VAL A 306 12.868 6.532 14.437 1.00 15.50 C ANISOU 2263 CG2 VAL A 306 1954 1676 2259 0 -40 239 C ATOM 2264 N LYS A 307 17.028 8.373 14.355 1.00 16.49 N ANISOU 2264 N LYS A 307 1589 2228 2446 -828 64 456 N ATOM 2265 CA LYS A 307 18.168 9.296 14.204 1.00 19.64 C ANISOU 2265 CA LYS A 307 2274 2261 2925 -1231 275 468 C ATOM 2266 C LYS A 307 19.225 8.810 13.204 1.00 19.41 C ANISOU 2266 C LYS A 307 2228 2190 2956 -1660 479 553 C ATOM 2267 O LYS A 307 19.955 9.628 12.636 1.00 19.91 O ANISOU 2267 O LYS A 307 2096 1827 3638 -1358 849 608 O ATOM 2268 CB LYS A 307 18.832 9.592 15.556 1.00 21.23 C ANISOU 2268 CB LYS A 307 2661 2467 2938 -711 100 339 C ATOM 2269 CG LYS A 307 17.989 10.421 16.515 1.00 23.13 C ANISOU 2269 CG LYS A 307 2721 2892 3173 -241 -102 230 C ATOM 2270 CD LYS A 307 17.660 11.790 15.934 1.00 26.51 C ANISOU 2270 CD LYS A 307 3606 3058 3405 -301 -239 465 C ATOM 2271 CE LYS A 307 17.236 12.787 16.995 1.00 30.90 C ANISOU 2271 CE LYS A 307 4088 3953 3696 -298 -84 1 C ATOM 2272 NZ LYS A 307 16.807 14.079 16.389 1.00 34.08 N ANISOU 2272 NZ LYS A 307 4891 3700 4358 -700 -257 160 N ATOM 2273 N GLY A 308 19.308 7.496 12.990 1.00 21.53 N ANISOU 2273 N GLY A 308 2685 2383 3110 -533 271 400 N ATOM 2274 CA GLY A 308 20.162 6.930 11.941 1.00 24.09 C ANISOU 2274 CA GLY A 308 2797 3008 3344 -265 408 331 C ATOM 2275 C GLY A 308 19.600 6.987 10.525 1.00 21.97 C ANISOU 2275 C GLY A 308 2695 2896 2753 -376 1193 -1 C ATOM 2276 O GLY A 308 20.264 6.552 9.586 1.00 22.53 O ANISOU 2276 O GLY A 308 2349 3225 2984 -603 1483 60 O ATOM 2277 N GLY A 309 18.374 7.491 10.364 1.00 21.57 N ANISOU 2277 N GLY A 309 2527 2711 2957 -749 855 349 N ATOM 2278 CA GLY A 309 17.759 7.650 9.055 1.00 24.07 C ANISOU 2278 CA GLY A 309 2052 4681 2410 -1160 1554 618 C ATOM 2279 C GLY A 309 17.219 6.379 8.417 1.00 25.71 C ANISOU 2279 C GLY A 309 3146 3706 2915 -334 764 669 C ATOM 2280 O GLY A 309 16.932 6.378 7.220 1.00 25.28 O ANISOU 2280 O GLY A 309 3833 2906 2866 -160 754 314 O ATOM 2281 N LEU A 310 17.075 5.307 9.196 1.00 23.18 N ANISOU 2281 N LEU A 310 3034 3051 2721 -235 682 185 N ATOM 2282 CA LEU A 310 16.559 4.035 8.673 1.00 23.48 C ANISOU 2282 CA LEU A 310 2630 3156 3135 -78 440 -6 C ATOM 2283 C LEU A 310 15.045 3.990 8.626 1.00 21.96 C ANISOU 2283 C LEU A 310 2677 2950 2714 -26 -183 -153 C ATOM 2284 O LEU A 310 14.481 3.236 7.831 1.00 22.49 O ANISOU 2284 O LEU A 310 2248 3211 3084 -202 -165 -286 O ATOM 2285 CB LEU A 310 17.092 2.852 9.485 1.00 25.16 C ANISOU 2285 CB LEU A 310 2987 3381 3189 -18 188 52 C ATOM 2286 CG LEU A 310 18.584 2.572 9.259 1.00 28.95 C ANISOU 2286 CG LEU A 310 3186 4156 3657 82 690 36 C ATOM 2287 CD1 LEU A 310 19.148 1.680 10.355 1.00 31.54 C ANISOU 2287 CD1 LEU A 310 3735 4194 4053 179 424 163 C ATOM 2288 CD2 LEU A 310 18.832 1.952 7.886 1.00 34.29 C ANISOU 2288 CD2 LEU A 310 4272 4717 4038 63 668 -447 C ATOM 2289 N CYS A 311 14.390 4.765 9.490 1.00 20.73 N ANISOU 2289 N CYS A 311 2198 2915 2761 -100 -162 -64 N ATOM 2290 CA CYS A 311 12.938 4.930 9.429 1.00 20.96 C ANISOU 2290 CA CYS A 311 2211 2726 3025 -164 -175 104 C ATOM 2291 C CYS A 311 12.498 6.227 10.097 1.00 20.66 C ANISOU 2291 C CYS A 311 2474 2523 2853 -198 -90 224 C ATOM 2292 O CYS A 311 13.305 6.916 10.713 1.00 20.67 O ANISOU 2292 O CYS A 311 2409 2442 3000 155 -133 -195 O ATOM 2293 CB CYS A 311 12.236 3.729 10.061 1.00 26.35 C ANISOU 2293 CB CYS A 311 2895 3396 3718 -434 -57 707 C ATOM 2294 SG CYS A 311 12.868 3.270 11.674 1.00 32.98 S ANISOU 2294 SG CYS A 311 1991 6144 4396 -497 154 2160 S ATOM 2295 N ARG A 312 11.221 6.558 9.934 1.00 18.23 N ANISOU 2295 N ARG A 312 2476 1815 2634 -198 25 166 N ATOM 2296 CA ARG A 312 10.622 7.768 10.501 1.00 20.25 C ANISOU 2296 CA ARG A 312 2798 2134 2761 -8 221 8 C ATOM 2297 C ARG A 312 9.831 7.508 11.777 1.00 19.03 C ANISOU 2297 C ARG A 312 3014 1698 2519 109 160 -148 C ATOM 2298 O ARG A 312 9.723 8.387 12.625 1.00 19.55 O ANISOU 2298 O ARG A 312 3394 1786 2245 -53 198 -77 O ATOM 2299 CB ARG A 312 9.716 8.437 9.467 1.00 20.72 C ANISOU 2299 CB ARG A 312 2647 2449 2776 -14 267 107 C ATOM 2300 CG ARG A 312 10.483 8.946 8.262 1.00 22.88 C ANISOU 2300 CG ARG A 312 2767 2705 3219 -59 488 365 C ATOM 2301 CD ARG A 312 9.577 9.555 7.213 1.00 24.60 C ANISOU 2301 CD ARG A 312 2834 3205 3306 -5 262 251 C ATOM 2302 NE ARG A 312 8.858 10.733 7.705 1.00 26.94 N ANISOU 2302 NE ARG A 312 3918 3005 3312 81 263 192 N ATOM 2303 CZ ARG A 312 7.881 11.361 7.046 1.00 27.71 C ANISOU 2303 CZ ARG A 312 3338 3284 3907 -33 300 114 C ATOM 2304 NH1 ARG A 312 7.481 10.941 5.847 1.00 30.52 N ANISOU 2304 NH1 ARG A 312 3898 4087 3611 224 211 301 N ATOM 2305 NH2 ARG A 312 7.294 12.422 7.592 1.00 27.91 N ANISOU 2305 NH2 ARG A 312 3681 2849 4074 -91 283 356 N ATOM 2306 N ARG A 313 9.272 6.306 11.889 1.00 17.78 N ANISOU 2306 N ARG A 313 2656 1820 2278 -54 363 -876 N ATOM 2307 CA ARG A 313 8.488 5.893 13.039 1.00 18.42 C ANISOU 2307 CA ARG A 313 2507 1909 2581 326 240 -111 C ATOM 2308 C ARG A 313 8.704 4.390 13.231 1.00 17.12 C ANISOU 2308 C ARG A 313 2121 1868 2513 189 210 8 C ATOM 2309 O ARG A 313 8.658 3.646 12.251 1.00 16.39 O ANISOU 2309 O ARG A 313 1883 2089 2257 14 337 103 O ATOM 2310 CB ARG A 313 7.016 6.187 12.745 1.00 21.42 C ANISOU 2310 CB ARG A 313 2593 2439 3104 444 32 -40 C ATOM 2311 CG ARG A 313 6.133 6.309 13.968 1.00 21.96 C ANISOU 2311 CG ARG A 313 2877 2390 3076 620 44 -125 C ATOM 2312 CD ARG A 313 4.911 7.169 13.674 1.00 21.30 C ANISOU 2312 CD ARG A 313 2804 2309 2979 493 -160 -78 C ATOM 2313 NE ARG A 313 3.860 6.451 12.961 1.00 22.24 N ANISOU 2313 NE ARG A 313 2968 2499 2982 196 39 -101 N ATOM 2314 CZ ARG A 313 2.897 5.727 13.525 1.00 23.21 C ANISOU 2314 CZ ARG A 313 3116 2639 3061 103 64 -97 C ATOM 2315 NH1 ARG A 313 2.824 5.569 14.850 1.00 23.71 N ANISOU 2315 NH1 ARG A 313 3204 2783 3019 217 -366 -226 N ATOM 2316 NH2 ARG A 313 1.996 5.144 12.744 1.00 24.92 N ANISOU 2316 NH2 ARG A 313 3126 3187 3155 -82 6 -47 N ATOM 2317 N VAL A 314 8.956 3.944 14.462 1.00 16.75 N ANISOU 2317 N VAL A 314 2073 1739 2552 150 138 -28 N ATOM 2318 CA VAL A 314 9.274 2.517 14.709 1.00 17.34 C ANISOU 2318 CA VAL A 314 2284 1702 2601 21 60 89 C ATOM 2319 C VAL A 314 8.888 2.044 16.113 1.00 14.93 C ANISOU 2319 C VAL A 314 1801 1367 2503 19 129 -218 C ATOM 2320 O VAL A 314 9.023 2.786 17.080 1.00 15.08 O ANISOU 2320 O VAL A 314 2075 1419 2233 -163 205 -56 O ATOM 2321 CB VAL A 314 10.775 2.217 14.433 1.00 19.67 C ANISOU 2321 CB VAL A 314 2470 2092 2910 196 261 184 C ATOM 2322 CG1 VAL A 314 11.681 2.883 15.459 1.00 21.63 C ANISOU 2322 CG1 VAL A 314 2802 2360 3054 -83 179 158 C ATOM 2323 CG2 VAL A 314 11.046 0.712 14.355 1.00 20.62 C ANISOU 2323 CG2 VAL A 314 2659 2065 3107 131 158 224 C ATOM 2324 N LEU A 315 8.399 0.806 16.187 1.00 14.59 N ANISOU 2324 N LEU A 315 1736 1340 2468 66 161 -91 N ATOM 2325 CA LEU A 315 8.075 0.116 17.429 1.00 13.88 C ANISOU 2325 CA LEU A 315 1298 1633 2344 -59 31 -129 C ATOM 2326 C LEU A 315 8.951 -1.139 17.529 1.00 14.60 C ANISOU 2326 C LEU A 315 1668 1435 2442 -102 -34 22 C ATOM 2327 O LEU A 315 9.103 -1.879 16.551 1.00 16.11 O ANISOU 2327 O LEU A 315 1778 1740 2600 258 -44 -133 O ATOM 2328 CB LEU A 315 6.590 -0.274 17.435 1.00 14.80 C ANISOU 2328 CB LEU A 315 1416 1667 2538 -298 -18 -92 C ATOM 2329 CG LEU A 315 6.032 -1.004 18.659 1.00 15.47 C ANISOU 2329 CG LEU A 315 1510 2003 2363 -131 0 -58 C ATOM 2330 CD1 LEU A 315 6.036 -0.106 19.883 1.00 17.90 C ANISOU 2330 CD1 LEU A 315 2311 1808 2681 -255 43 -174 C ATOM 2331 CD2 LEU A 315 4.619 -1.525 18.384 1.00 15.20 C ANISOU 2331 CD2 LEU A 315 1497 1881 2397 -139 72 -65 C ATOM 2332 N VAL A 316 9.522 -1.362 18.710 1.00 15.38 N ANISOU 2332 N VAL A 316 2030 1496 2316 -64 38 107 N ATOM 2333 CA VAL A 316 10.426 -2.484 18.974 1.00 15.50 C ANISOU 2333 CA VAL A 316 1925 1715 2247 74 217 95 C ATOM 2334 C VAL A 316 9.875 -3.278 20.144 1.00 15.55 C ANISOU 2334 C VAL A 316 2118 1552 2239 -97 100 75 C ATOM 2335 O VAL A 316 9.655 -2.695 21.202 1.00 17.42 O ANISOU 2335 O VAL A 316 2767 1767 2085 -280 66 116 O ATOM 2336 CB VAL A 316 11.845 -1.984 19.354 1.00 17.71 C ANISOU 2336 CB VAL A 316 2174 2079 2474 -199 63 50 C ATOM 2337 CG1 VAL A 316 12.771 -3.155 19.695 1.00 17.59 C ANISOU 2337 CG1 VAL A 316 1939 2347 2395 -161 233 227 C ATOM 2338 CG2 VAL A 316 12.436 -1.151 18.223 1.00 19.15 C ANISOU 2338 CG2 VAL A 316 2439 2326 2507 1 230 138 C ATOM 2339 N GLN A 317 9.645 -4.583 19.971 1.00 14.90 N ANISOU 2339 N GLN A 317 2147 1561 1951 -6 107 -42 N ATOM 2340 CA GLN A 317 9.305 -5.461 21.102 1.00 13.79 C ANISOU 2340 CA GLN A 317 1831 1266 2141 13 -18 3 C ATOM 2341 C GLN A 317 10.486 -6.354 21.444 1.00 14.55 C ANISOU 2341 C GLN A 317 1618 1565 2342 42 50 -42 C ATOM 2342 O GLN A 317 11.173 -6.847 20.550 1.00 14.74 O ANISOU 2342 O GLN A 317 1533 1589 2476 96 49 -85 O ATOM 2343 CB GLN A 317 8.074 -6.360 20.839 1.00 15.66 C ANISOU 2343 CB GLN A 317 2066 1573 2309 -202 -184 -96 C ATOM 2344 CG GLN A 317 7.567 -7.025 22.131 1.00 16.05 C ANISOU 2344 CG GLN A 317 1999 1549 2550 -372 -134 -23 C ATOM 2345 CD GLN A 317 6.486 -8.089 21.949 1.00 16.30 C ANISOU 2345 CD GLN A 317 1849 1511 2832 -323 17 7 C ATOM 2346 OE1 GLN A 317 6.634 -9.029 21.162 1.00 15.86 O ANISOU 2346 OE1 GLN A 317 1319 1611 3095 -17 -185 -93 O ATOM 2347 NE2 GLN A 317 5.411 -7.977 22.726 1.00 16.34 N ANISOU 2347 NE2 GLN A 317 1705 1566 2935 177 -138 -205 N ATOM 2348 N VAL A 318 10.684 -6.560 22.747 1.00 15.12 N ANISOU 2348 N VAL A 318 1634 1681 2428 262 -95 23 N ATOM 2349 CA VAL A 318 11.575 -7.590 23.284 1.00 15.23 C ANISOU 2349 CA VAL A 318 1888 1631 2267 292 -112 30 C ATOM 2350 C VAL A 318 10.840 -8.353 24.397 1.00 15.60 C ANISOU 2350 C VAL A 318 1742 1823 2359 173 -32 -31 C ATOM 2351 O VAL A 318 9.856 -7.849 24.962 1.00 16.76 O ANISOU 2351 O VAL A 318 2475 1329 2563 397 260 -269 O ATOM 2352 CB VAL A 318 12.902 -6.990 23.817 1.00 18.11 C ANISOU 2352 CB VAL A 318 1928 2368 2585 165 -204 -46 C ATOM 2353 CG1 VAL A 318 13.657 -6.315 22.696 1.00 22.67 C ANISOU 2353 CG1 VAL A 318 2691 3006 2916 119 65 197 C ATOM 2354 CG2 VAL A 318 12.670 -5.987 24.944 1.00 17.24 C ANISOU 2354 CG2 VAL A 318 1847 2058 2642 239 -183 75 C ATOM 2355 N SER A 319 11.305 -9.564 24.697 1.00 14.82 N ANISOU 2355 N SER A 319 1634 1671 2324 15 152 -63 N ATOM 2356 CA SER A 319 10.777 -10.340 25.821 1.00 15.72 C ANISOU 2356 CA SER A 319 1977 1668 2325 64 134 9 C ATOM 2357 C SER A 319 11.832 -11.217 26.472 1.00 14.73 C ANISOU 2357 C SER A 319 1650 1726 2218 -75 76 -144 C ATOM 2358 O SER A 319 12.858 -11.522 25.853 1.00 16.03 O ANISOU 2358 O SER A 319 2015 1566 2509 -101 480 -59 O ATOM 2359 CB SER A 319 9.576 -11.194 25.385 1.00 16.79 C ANISOU 2359 CB SER A 319 2132 1812 2432 -83 -36 130 C ATOM 2360 OG SER A 319 9.972 -12.228 24.492 1.00 17.11 O ANISOU 2360 OG SER A 319 1778 2017 2704 174 131 112 O ATOM 2361 N TYR A 320 11.563 -11.611 27.721 1.00 15.17 N ANISOU 2361 N TYR A 320 1763 1728 2273 11 163 -69 N ATOM 2362 CA TYR A 320 12.495 -12.366 28.559 1.00 16.14 C ANISOU 2362 CA TYR A 320 1928 1815 2387 187 69 -169 C ATOM 2363 C TYR A 320 11.802 -13.451 29.379 1.00 15.49 C ANISOU 2363 C TYR A 320 1667 1869 2346 325 223 -219 C ATOM 2364 O TYR A 320 10.586 -13.399 29.604 1.00 15.98 O ANISOU 2364 O TYR A 320 1548 1888 2632 97 22 -210 O ATOM 2365 CB TYR A 320 13.230 -11.425 29.524 1.00 15.54 C ANISOU 2365 CB TYR A 320 1864 1843 2197 125 226 -128 C ATOM 2366 CG TYR A 320 14.082 -10.388 28.823 1.00 14.73 C ANISOU 2366 CG TYR A 320 1500 1883 2211 198 203 -120 C ATOM 2367 CD1 TYR A 320 13.511 -9.218 28.324 1.00 15.53 C ANISOU 2367 CD1 TYR A 320 1753 1794 2354 232 124 -167 C ATOM 2368 CD2 TYR A 320 15.452 -10.577 28.643 1.00 13.84 C ANISOU 2368 CD2 TYR A 320 1421 1735 2099 172 10 21 C ATOM 2369 CE1 TYR A 320 14.269 -8.271 27.660 1.00 15.12 C ANISOU 2369 CE1 TYR A 320 1589 1711 2446 236 147 -285 C ATOM 2370 CE2 TYR A 320 16.224 -9.626 27.982 1.00 13.76 C ANISOU 2370 CE2 TYR A 320 1608 1424 2196 117 41 -152 C ATOM 2371 CZ TYR A 320 15.626 -8.475 27.493 1.00 14.71 C ANISOU 2371 CZ TYR A 320 1584 1582 2420 151 235 90 C ATOM 2372 OH TYR A 320 16.375 -7.517 26.844 1.00 15.85 O ANISOU 2372 OH TYR A 320 1445 1680 2894 -1 279 89 O ATOM 2373 N ALA A 321 12.595 -14.432 29.813 1.00 17.03 N ANISOU 2373 N ALA A 321 2262 1703 2504 403 83 -202 N ATOM 2374 CA ALA A 321 12.197 -15.397 30.845 1.00 17.77 C ANISOU 2374 CA ALA A 321 2288 1709 2752 166 105 -172 C ATOM 2375 C ALA A 321 13.104 -15.214 32.054 1.00 18.29 C ANISOU 2375 C ALA A 321 2569 1658 2721 217 63 -159 C ATOM 2376 O ALA A 321 14.306 -14.958 31.895 1.00 17.18 O ANISOU 2376 O ALA A 321 2729 1494 2305 -181 102 -54 O ATOM 2377 CB ALA A 321 12.320 -16.817 30.323 1.00 18.43 C ANISOU 2377 CB ALA A 321 2550 1808 2643 125 24 -302 C ATOM 2378 N ILE A 322 12.540 -15.366 33.255 1.00 17.89 N ANISOU 2378 N ILE A 322 2208 1688 2901 307 123 14 N ATOM 2379 CA ILE A 322 13.323 -15.256 34.491 1.00 16.80 C ANISOU 2379 CA ILE A 322 1846 1435 3103 592 30 -14 C ATOM 2380 C ILE A 322 14.472 -16.267 34.479 1.00 15.57 C ANISOU 2380 C ILE A 322 1469 1390 3056 368 -94 117 C ATOM 2381 O ILE A 322 14.280 -17.432 34.156 1.00 17.29 O ANISOU 2381 O ILE A 322 1862 1459 3245 101 244 66 O ATOM 2382 CB ILE A 322 12.470 -15.411 35.777 1.00 18.06 C ANISOU 2382 CB ILE A 322 2366 1706 2788 282 -71 -40 C ATOM 2383 CG1 ILE A 322 13.316 -15.082 37.013 1.00 20.21 C ANISOU 2383 CG1 ILE A 322 2774 1855 3049 129 -243 -302 C ATOM 2384 CG2 ILE A 322 11.851 -16.804 35.907 1.00 17.56 C ANISOU 2384 CG2 ILE A 322 2504 1715 2453 233 -58 -71 C ATOM 2385 CD1 ILE A 322 12.529 -15.044 38.302 1.00 22.38 C ANISOU 2385 CD1 ILE A 322 2965 2595 2940 -16 -274 -69 C ATOM 2386 N GLY A 323 15.670 -15.786 34.795 1.00 16.21 N ANISOU 2386 N GLY A 323 1419 1706 3034 212 -47 387 N ATOM 2387 CA GLY A 323 16.856 -16.632 34.840 1.00 15.92 C ANISOU 2387 CA GLY A 323 1365 1750 2933 200 -60 187 C ATOM 2388 C GLY A 323 17.568 -16.877 33.521 1.00 16.49 C ANISOU 2388 C GLY A 323 1740 1622 2903 102 -10 182 C ATOM 2389 O GLY A 323 18.597 -17.553 33.508 1.00 19.49 O ANISOU 2389 O GLY A 323 2232 1682 3490 512 67 180 O ATOM 2390 N VAL A 324 17.047 -16.329 32.427 1.00 16.32 N ANISOU 2390 N VAL A 324 1966 1419 2813 -34 96 247 N ATOM 2391 CA VAL A 324 17.622 -16.495 31.098 1.00 16.49 C ANISOU 2391 CA VAL A 324 1816 1504 2944 149 194 53 C ATOM 2392 C VAL A 324 18.191 -15.131 30.662 1.00 15.23 C ANISOU 2392 C VAL A 324 1479 1438 2868 270 107 55 C ATOM 2393 O VAL A 324 17.500 -14.113 30.720 1.00 15.53 O ANISOU 2393 O VAL A 324 1358 1562 2977 325 73 -163 O ATOM 2394 CB VAL A 324 16.547 -17.006 30.124 1.00 16.35 C ANISOU 2394 CB VAL A 324 1833 1564 2814 13 279 72 C ATOM 2395 CG1 VAL A 324 17.109 -17.204 28.723 1.00 17.70 C ANISOU 2395 CG1 VAL A 324 2093 1737 2896 32 322 -60 C ATOM 2396 CG2 VAL A 324 15.942 -18.310 30.650 1.00 15.95 C ANISOU 2396 CG2 VAL A 324 2147 1226 2688 107 119 -124 C ATOM 2397 N SER A 325 19.454 -15.094 30.248 1.00 17.46 N ANISOU 2397 N SER A 325 1560 2175 2897 124 198 -14 N ATOM 2398 CA SER A 325 20.098 -13.803 29.958 1.00 17.24 C ANISOU 2398 CA SER A 325 1189 2312 3049 4 141 -110 C ATOM 2399 C SER A 325 19.660 -13.180 28.618 1.00 17.97 C ANISOU 2399 C SER A 325 1708 1971 3146 135 179 -53 C ATOM 2400 O SER A 325 19.387 -11.985 28.577 1.00 18.49 O ANISOU 2400 O SER A 325 1858 2073 3094 513 -90 -166 O ATOM 2401 CB SER A 325 21.621 -13.914 30.034 1.00 17.53 C ANISOU 2401 CB SER A 325 1111 2312 3237 -104 635 -207 C ATOM 2402 OG SER A 325 22.088 -14.701 28.972 1.00 23.73 O ANISOU 2402 OG SER A 325 2046 2800 4167 215 619 -903 O ATOM 2403 N HIS A 326 19.598 -13.976 27.543 1.00 18.10 N ANISOU 2403 N HIS A 326 1413 2342 3121 -7 254 -174 N ATOM 2404 CA HIS A 326 19.244 -13.461 26.203 1.00 18.30 C ANISOU 2404 CA HIS A 326 1606 2349 2996 -92 289 -162 C ATOM 2405 C HIS A 326 17.736 -13.293 26.060 1.00 16.96 C ANISOU 2405 C HIS A 326 1655 2117 2670 111 343 -207 C ATOM 2406 O HIS A 326 16.982 -14.088 26.616 1.00 19.12 O ANISOU 2406 O HIS A 326 2364 2148 2750 -84 475 -172 O ATOM 2407 CB HIS A 326 19.722 -14.401 25.094 1.00 18.49 C ANISOU 2407 CB HIS A 326 1721 2440 2862 -230 293 -127 C ATOM 2408 CG HIS A 326 21.205 -14.411 24.903 1.00 22.34 C ANISOU 2408 CG HIS A 326 1799 3002 3688 -200 530 -275 C ATOM 2409 ND1 HIS A 326 21.872 -13.424 24.209 1.00 28.24 N ANISOU 2409 ND1 HIS A 326 3289 3303 4138 -777 668 -142 N ATOM 2410 CD2 HIS A 326 22.151 -15.291 25.303 1.00 25.82 C ANISOU 2410 CD2 HIS A 326 2478 3198 4134 -49 321 117 C ATOM 2411 CE1 HIS A 326 23.166 -13.694 24.193 1.00 28.75 C ANISOU 2411 CE1 HIS A 326 3063 2963 4896 -1777 2001 674 C ATOM 2412 NE2 HIS A 326 23.361 -14.822 24.853 1.00 28.41 N ANISOU 2412 NE2 HIS A 326 3050 3175 4566 -639 527 139 N ATOM 2413 N PRO A 327 17.283 -12.282 25.287 1.00 16.74 N ANISOU 2413 N PRO A 327 1256 2343 2758 107 378 -65 N ATOM 2414 CA PRO A 327 15.838 -12.153 25.040 1.00 15.52 C ANISOU 2414 CA PRO A 327 1338 1981 2577 219 250 -212 C ATOM 2415 C PRO A 327 15.284 -13.368 24.302 1.00 16.96 C ANISOU 2415 C PRO A 327 2427 1683 2333 564 298 -353 C ATOM 2416 O PRO A 327 16.009 -14.016 23.552 1.00 17.17 O ANISOU 2416 O PRO A 327 1750 2558 2214 -378 709 -780 O ATOM 2417 CB PRO A 327 15.727 -10.898 24.155 1.00 17.87 C ANISOU 2417 CB PRO A 327 1688 2259 2842 128 174 42 C ATOM 2418 CG PRO A 327 17.096 -10.669 23.617 1.00 19.88 C ANISOU 2418 CG PRO A 327 1983 2664 2906 4 438 281 C ATOM 2419 CD PRO A 327 18.043 -11.196 24.645 1.00 18.89 C ANISOU 2419 CD PRO A 327 1931 2380 2866 -214 227 -7 C ATOM 2420 N LEU A 328 14.020 -13.678 24.556 1.00 16.15 N ANISOU 2420 N LEU A 328 2841 1678 1618 719 1104 -710 N ATOM 2421 CA LEU A 328 13.322 -14.779 23.892 1.00 17.34 C ANISOU 2421 CA LEU A 328 2219 1974 2396 273 513 -194 C ATOM 2422 C LEU A 328 12.828 -14.401 22.509 1.00 17.02 C ANISOU 2422 C LEU A 328 2102 1745 2617 322 359 -166 C ATOM 2423 O LEU A 328 12.671 -15.266 21.654 1.00 16.95 O ANISOU 2423 O LEU A 328 1982 1581 2874 327 91 -123 O ATOM 2424 CB LEU A 328 12.101 -15.215 24.708 1.00 18.62 C ANISOU 2424 CB LEU A 328 2062 2426 2587 50 369 -92 C ATOM 2425 CG LEU A 328 12.260 -15.490 26.201 1.00 19.31 C ANISOU 2425 CG LEU A 328 1851 2890 2594 -161 334 -29 C ATOM 2426 CD1 LEU A 328 10.973 -16.104 26.740 1.00 19.84 C ANISOU 2426 CD1 LEU A 328 2039 2862 2636 -422 262 6 C ATOM 2427 CD2 LEU A 328 13.448 -16.385 26.504 1.00 20.62 C ANISOU 2427 CD2 LEU A 328 2443 2730 2661 259 522 7 C ATOM 2428 N SER A 329 12.514 -13.121 22.314 1.00 17.53 N ANISOU 2428 N SER A 329 2152 1704 2802 81 20 -35 N ATOM 2429 CA SER A 329 12.023 -12.631 21.039 1.00 16.34 C ANISOU 2429 CA SER A 329 1812 1726 2668 -37 36 -103 C ATOM 2430 C SER A 329 12.377 -11.163 20.869 1.00 15.54 C ANISOU 2430 C SER A 329 1907 1701 2296 -27 24 -171 C ATOM 2431 O SER A 329 12.487 -10.419 21.855 1.00 14.56 O ANISOU 2431 O SER A 329 1490 1293 2747 147 113 -345 O ATOM 2432 CB SER A 329 10.501 -12.823 20.945 1.00 15.68 C ANISOU 2432 CB SER A 329 1778 1853 2326 21 153 -167 C ATOM 2433 OG SER A 329 9.804 -11.923 21.791 1.00 15.63 O ANISOU 2433 OG SER A 329 1512 1809 2618 -11 177 -257 O ATOM 2434 N ILE A 330 12.591 -10.769 19.618 1.00 16.01 N ANISOU 2434 N ILE A 330 2044 1656 2380 -100 209 -105 N ATOM 2435 CA ILE A 330 12.788 -9.366 19.244 1.00 16.77 C ANISOU 2435 CA ILE A 330 2257 1644 2471 66 212 -20 C ATOM 2436 C ILE A 330 11.983 -9.134 17.971 1.00 16.12 C ANISOU 2436 C ILE A 330 2308 1573 2242 239 351 -257 C ATOM 2437 O ILE A 330 12.040 -9.949 17.051 1.00 15.94 O ANISOU 2437 O ILE A 330 1966 1449 2642 108 282 -471 O ATOM 2438 CB ILE A 330 14.276 -9.002 18.987 1.00 18.59 C ANISOU 2438 CB ILE A 330 2269 2216 2575 -9 221 13 C ATOM 2439 CG1 ILE A 330 15.167 -9.395 20.172 1.00 19.01 C ANISOU 2439 CG1 ILE A 330 2263 2452 2505 43 306 28 C ATOM 2440 CG2 ILE A 330 14.417 -7.500 18.709 1.00 19.07 C ANISOU 2440 CG2 ILE A 330 2354 2234 2656 -12 114 53 C ATOM 2441 CD1 ILE A 330 16.654 -9.334 19.880 1.00 18.98 C ANISOU 2441 CD1 ILE A 330 2268 2276 2667 -188 265 89 C ATOM 2442 N SER A 331 11.235 -8.027 17.923 1.00 16.62 N ANISOU 2442 N SER A 331 2418 1296 2601 60 329 -53 N ATOM 2443 CA SER A 331 10.409 -7.695 16.761 1.00 17.56 C ANISOU 2443 CA SER A 331 2300 1777 2595 -26 273 -44 C ATOM 2444 C SER A 331 10.484 -6.209 16.419 1.00 16.60 C ANISOU 2444 C SER A 331 2194 1802 2308 -63 158 -43 C ATOM 2445 O SER A 331 10.546 -5.368 17.314 1.00 17.03 O ANISOU 2445 O SER A 331 2414 1693 2362 -255 -107 34 O ATOM 2446 CB SER A 331 8.952 -8.121 17.012 1.00 17.22 C ANISOU 2446 CB SER A 331 2353 1732 2457 46 366 333 C ATOM 2447 OG SER A 331 8.889 -9.442 17.543 1.00 15.45 O ANISOU 2447 OG SER A 331 1766 1530 2573 492 255 226 O ATOM 2448 N ILE A 332 10.472 -5.897 15.122 1.00 16.60 N ANISOU 2448 N ILE A 332 2253 1799 2252 -16 105 -203 N ATOM 2449 CA ILE A 332 10.553 -4.516 14.622 1.00 18.20 C ANISOU 2449 CA ILE A 332 2402 1874 2637 188 47 -17 C ATOM 2450 C ILE A 332 9.343 -4.224 13.742 1.00 16.87 C ANISOU 2450 C ILE A 332 2408 1604 2396 173 118 -75 C ATOM 2451 O ILE A 332 9.071 -4.964 12.792 1.00 18.78 O ANISOU 2451 O ILE A 332 2567 1874 2692 -75 -263 -159 O ATOM 2452 CB ILE A 332 11.830 -4.284 13.781 1.00 21.83 C ANISOU 2452 CB ILE A 332 2708 2432 3153 264 391 101 C ATOM 2453 CG1 ILE A 332 13.090 -4.693 14.555 1.00 29.48 C ANISOU 2453 CG1 ILE A 332 2912 3620 4667 902 212 866 C ATOM 2454 CG2 ILE A 332 11.936 -2.824 13.331 1.00 23.67 C ANISOU 2454 CG2 ILE A 332 3006 2349 3636 452 142 132 C ATOM 2455 CD1 ILE A 332 13.384 -3.868 15.793 1.00 38.43 C ANISOU 2455 CD1 ILE A 332 1627 6857 6117 1718 -1842 1 C ATOM 2456 N PHE A 333 8.642 -3.134 14.042 1.00 15.99 N ANISOU 2456 N PHE A 333 1718 1974 2382 236 27 -202 N ATOM 2457 CA PHE A 333 7.494 -2.688 13.237 1.00 18.23 C ANISOU 2457 CA PHE A 333 2330 2027 2567 217 -357 66 C ATOM 2458 C PHE A 333 7.714 -1.246 12.809 1.00 17.12 C ANISOU 2458 C PHE A 333 1786 1861 2857 277 -170 -143 C ATOM 2459 O PHE A 333 7.727 -0.363 13.668 1.00 16.22 O ANISOU 2459 O PHE A 333 1468 2008 2686 225 -305 -126 O ATOM 2460 CB PHE A 333 6.192 -2.803 14.035 1.00 19.22 C ANISOU 2460 CB PHE A 333 2584 2186 2531 114 -206 125 C ATOM 2461 CG PHE A 333 6.013 -4.124 14.718 1.00 19.69 C ANISOU 2461 CG PHE A 333 2440 2135 2905 128 -391 211 C ATOM 2462 CD1 PHE A 333 5.577 -5.233 14.004 1.00 20.95 C ANISOU 2462 CD1 PHE A 333 2937 2273 2748 87 -552 221 C ATOM 2463 CD2 PHE A 333 6.263 -4.260 16.079 1.00 18.59 C ANISOU 2463 CD2 PHE A 333 2181 1989 2893 218 -330 208 C ATOM 2464 CE1 PHE A 333 5.402 -6.456 14.628 1.00 20.99 C ANISOU 2464 CE1 PHE A 333 2812 1919 3243 286 -531 90 C ATOM 2465 CE2 PHE A 333 6.098 -5.481 16.709 1.00 18.68 C ANISOU 2465 CE2 PHE A 333 2417 1999 2678 241 -287 154 C ATOM 2466 CZ PHE A 333 5.662 -6.580 15.986 1.00 21.27 C ANISOU 2466 CZ PHE A 333 2775 2114 3192 369 -500 -124 C ATOM 2467 N HIS A 334 7.891 -1.007 11.500 1.00 18.09 N ANISOU 2467 N HIS A 334 2091 1872 2908 268 -179 -28 N ATOM 2468 CA HIS A 334 8.264 0.337 11.002 1.00 17.83 C ANISOU 2468 CA HIS A 334 2151 2020 2601 136 27 -59 C ATOM 2469 C HIS A 334 7.135 1.164 10.358 1.00 17.98 C ANISOU 2469 C HIS A 334 2070 2212 2549 -40 -94 83 C ATOM 2470 O HIS A 334 7.390 2.258 9.845 1.00 17.30 O ANISOU 2470 O HIS A 334 1904 2173 2496 -186 100 -72 O ATOM 2471 CB HIS A 334 9.551 0.323 10.135 1.00 19.10 C ANISOU 2471 CB HIS A 334 2149 2378 2730 186 56 -264 C ATOM 2472 CG HIS A 334 9.479 -0.467 8.858 1.00 19.90 C ANISOU 2472 CG HIS A 334 2495 2374 2689 456 571 -295 C ATOM 2473 ND1 HIS A 334 8.361 -0.534 8.063 1.00 20.97 N ANISOU 2473 ND1 HIS A 334 2930 2344 2692 180 321 -215 N ATOM 2474 CD2 HIS A 334 10.433 -1.172 8.208 1.00 22.38 C ANISOU 2474 CD2 HIS A 334 2998 2681 2824 356 1056 -593 C ATOM 2475 CE1 HIS A 334 8.613 -1.262 6.994 1.00 23.98 C ANISOU 2475 CE1 HIS A 334 3596 2602 2912 252 559 -387 C ATOM 2476 NE2 HIS A 334 9.868 -1.661 7.055 1.00 25.03 N ANISOU 2476 NE2 HIS A 334 4379 2650 2479 1477 1261 -1189 N ATOM 2477 N TYR A 335 5.904 0.644 10.393 1.00 17.82 N ANISOU 2477 N TYR A 335 2072 2128 2570 -34 176 -51 N ATOM 2478 CA TYR A 335 4.717 1.340 9.866 1.00 20.86 C ANISOU 2478 CA TYR A 335 2405 2674 2843 203 -116 -74 C ATOM 2479 C TYR A 335 4.797 1.702 8.370 1.00 21.39 C ANISOU 2479 C TYR A 335 2538 2681 2907 -134 -121 26 C ATOM 2480 O TYR A 335 4.079 2.576 7.901 1.00 24.02 O ANISOU 2480 O TYR A 335 3043 2973 3108 -214 -427 535 O ATOM 2481 CB TYR A 335 4.413 2.600 10.703 1.00 22.01 C ANISOU 2481 CB TYR A 335 2705 2860 2797 470 -17 -83 C ATOM 2482 CG TYR A 335 4.276 2.354 12.194 1.00 20.68 C ANISOU 2482 CG TYR A 335 2299 2713 2845 518 111 23 C ATOM 2483 CD1 TYR A 335 3.074 1.908 12.740 1.00 21.20 C ANISOU 2483 CD1 TYR A 335 2378 2863 2811 649 211 358 C ATOM 2484 CD2 TYR A 335 5.346 2.583 13.063 1.00 20.36 C ANISOU 2484 CD2 TYR A 335 2630 2523 2582 404 48 24 C ATOM 2485 CE1 TYR A 335 2.943 1.695 14.104 1.00 21.11 C ANISOU 2485 CE1 TYR A 335 2202 2963 2857 302 369 370 C ATOM 2486 CE2 TYR A 335 5.222 2.371 14.432 1.00 19.37 C ANISOU 2486 CE2 TYR A 335 2305 2347 2707 354 164 261 C ATOM 2487 CZ TYR A 335 4.016 1.927 14.950 1.00 21.19 C ANISOU 2487 CZ TYR A 335 2398 2629 3022 188 219 375 C ATOM 2488 OH TYR A 335 3.877 1.718 16.309 1.00 18.78 O ANISOU 2488 OH TYR A 335 1954 2268 2914 -27 -100 72 O ATOM 2489 N GLY A 336 5.603 0.962 7.617 1.00 22.89 N ANISOU 2489 N GLY A 336 2981 2657 3059 -184 8 -116 N ATOM 2490 CA GLY A 336 5.997 1.318 6.252 1.00 21.89 C ANISOU 2490 CA GLY A 336 2636 2503 3178 -672 34 -106 C ATOM 2491 C GLY A 336 6.898 2.530 6.029 1.00 20.49 C ANISOU 2491 C GLY A 336 2874 2385 2524 -529 107 363 C ATOM 2492 O GLY A 336 6.978 3.019 4.898 1.00 21.29 O ANISOU 2492 O GLY A 336 3300 2606 2182 -529 -18 120 O ATOM 2493 N THR A 337 7.595 2.998 7.070 1.00 19.53 N ANISOU 2493 N THR A 337 2398 2222 2799 -188 -90 344 N ATOM 2494 CA THR A 337 8.429 4.226 6.987 1.00 19.33 C ANISOU 2494 CA THR A 337 2229 2221 2893 -147 98 173 C ATOM 2495 C THR A 337 9.928 4.008 6.679 1.00 19.54 C ANISOU 2495 C THR A 337 2310 2253 2860 -150 233 126 C ATOM 2496 O THR A 337 10.755 4.906 6.902 1.00 19.54 O ANISOU 2496 O THR A 337 3094 1941 2389 -328 200 127 O ATOM 2497 CB THR A 337 8.314 5.087 8.267 1.00 19.16 C ANISOU 2497 CB THR A 337 2123 2457 2697 -285 178 246 C ATOM 2498 OG1 THR A 337 8.937 4.423 9.377 1.00 18.57 O ANISOU 2498 OG1 THR A 337 1975 2541 2537 64 230 -75 O ATOM 2499 CG2 THR A 337 6.862 5.412 8.597 1.00 16.87 C ANISOU 2499 CG2 THR A 337 1884 1877 2648 -835 125 77 C ATOM 2500 N SER A 338 10.269 2.833 6.153 1.00 21.45 N ANISOU 2500 N SER A 338 2765 2341 3043 -49 168 -17 N ATOM 2501 CA SER A 338 11.640 2.503 5.763 1.00 22.86 C ANISOU 2501 CA SER A 338 2906 2782 2994 34 359 -5 C ATOM 2502 C SER A 338 11.628 1.873 4.382 1.00 23.98 C ANISOU 2502 C SER A 338 3236 2761 3113 12 191 -104 C ATOM 2503 O SER A 338 10.667 1.191 4.017 1.00 23.19 O ANISOU 2503 O SER A 338 2928 2579 3302 574 -455 -94 O ATOM 2504 CB SER A 338 12.237 1.495 6.740 1.00 22.88 C ANISOU 2504 CB SER A 338 2742 2852 3098 -32 268 1 C ATOM 2505 OG SER A 338 13.588 1.199 6.423 1.00 22.38 O ANISOU 2505 OG SER A 338 2773 2812 2915 104 272 85 O ATOM 2506 N GLN A 339 12.703 2.092 3.627 1.00 25.28 N ANISOU 2506 N GLN A 339 3331 3112 3160 104 324 -125 N ATOM 2507 CA GLN A 339 12.921 1.346 2.390 1.00 27.91 C ANISOU 2507 CA GLN A 339 4042 2980 3581 256 396 -314 C ATOM 2508 C GLN A 339 13.365 -0.087 2.688 1.00 27.48 C ANISOU 2508 C GLN A 339 4081 3128 3232 183 324 167 C ATOM 2509 O GLN A 339 13.161 -0.976 1.862 1.00 30.74 O ANISOU 2509 O GLN A 339 4884 3312 3480 677 405 -212 O ATOM 2510 CB GLN A 339 13.938 2.048 1.481 1.00 29.79 C ANISOU 2510 CB GLN A 339 4443 3063 3811 30 253 122 C ATOM 2511 CG GLN A 339 13.400 3.316 0.840 1.00 33.23 C ANISOU 2511 CG GLN A 339 4925 2836 4863 -160 48 289 C ATOM 2512 CD GLN A 339 14.258 3.793 -0.320 0.75 35.07 C ANISOU 2512 CD GLN A 339 4962 3630 4730 -151 -236 858 C ATOM 2513 OE1 GLN A 339 15.484 3.699 -0.278 0.75 42.33 O ANISOU 2513 OE1 GLN A 339 5012 4862 6208 -620 -270 1562 O ATOM 2514 NE2 GLN A 339 13.621 4.308 -1.360 0.75 35.17 N ANISOU 2514 NE2 GLN A 339 4424 3848 5091 -84 -513 718 N ATOM 2515 N LYS A 340 13.965 -0.314 3.856 1.00 25.28 N ANISOU 2515 N LYS A 340 3656 2853 3094 43 552 155 N ATOM 2516 CA LYS A 340 14.351 -1.663 4.258 1.00 24.33 C ANISOU 2516 CA LYS A 340 3339 2964 2942 -146 579 451 C ATOM 2517 C LYS A 340 13.149 -2.403 4.829 1.00 22.99 C ANISOU 2517 C LYS A 340 3216 2508 3008 76 687 221 C ATOM 2518 O LYS A 340 12.220 -1.785 5.380 1.00 21.73 O ANISOU 2518 O LYS A 340 2701 2493 3062 -259 509 -61 O ATOM 2519 CB LYS A 340 15.468 -1.621 5.290 1.00 26.04 C ANISOU 2519 CB LYS A 340 3471 3165 3256 -147 391 428 C ATOM 2520 CG LYS A 340 16.734 -0.937 4.797 1.00 30.05 C ANISOU 2520 CG LYS A 340 3689 3755 3970 -618 367 290 C ATOM 2521 CD LYS A 340 17.864 -1.148 5.782 1.00 34.08 C ANISOU 2521 CD LYS A 340 3947 4374 4625 -474 -18 62 C ATOM 2522 CE LYS A 340 19.140 -0.465 5.324 1.00 36.69 C ANISOU 2522 CE LYS A 340 4165 4690 5084 -313 627 164 C ATOM 2523 NZ LYS A 340 19.794 -1.203 4.212 1.00 38.45 N ANISOU 2523 NZ LYS A 340 4827 5341 4440 -101 461 297 N ATOM 2524 N SER A 341 13.168 -3.725 4.684 1.00 22.70 N ANISOU 2524 N SER A 341 3251 2517 2858 370 448 107 N ATOM 2525 CA SER A 341 12.154 -4.581 5.295 1.00 22.27 C ANISOU 2525 CA SER A 341 2797 3050 2612 301 380 -146 C ATOM 2526 C SER A 341 12.337 -4.613 6.809 1.00 20.46 C ANISOU 2526 C SER A 341 2394 2786 2592 82 357 110 C ATOM 2527 O SER A 341 13.424 -4.324 7.331 1.00 19.85 O ANISOU 2527 O SER A 341 2558 2894 2090 15 232 200 O ATOM 2528 CB SER A 341 12.220 -6.010 4.747 1.00 20.00 C ANISOU 2528 CB SER A 341 1642 3255 2702 872 381 -364 C ATOM 2529 OG SER A 341 13.442 -6.654 5.088 1.00 22.13 O ANISOU 2529 OG SER A 341 2250 3142 3014 1097 -88 -31 O ATOM 2530 N GLU A 342 11.268 -4.978 7.504 1.00 20.02 N ANISOU 2530 N GLU A 342 2062 2831 2712 89 235 -120 N ATOM 2531 CA GLU A 342 11.323 -5.175 8.954 1.00 19.77 C ANISOU 2531 CA GLU A 342 2306 2465 2737 -136 -15 -30 C ATOM 2532 C GLU A 342 12.332 -6.280 9.323 1.00 20.50 C ANISOU 2532 C GLU A 342 2554 2378 2854 -71 20 -17 C ATOM 2533 O GLU A 342 13.069 -6.153 10.306 1.00 21.32 O ANISOU 2533 O GLU A 342 1996 2939 3162 184 -2 96 O ATOM 2534 CB GLU A 342 9.917 -5.434 9.507 1.00 20.43 C ANISOU 2534 CB GLU A 342 2346 2741 2674 -83 -13 -137 C ATOM 2535 CG GLU A 342 9.069 -4.164 9.520 1.00 21.54 C ANISOU 2535 CG GLU A 342 2470 2823 2889 5 -74 -106 C ATOM 2536 CD GLU A 342 7.587 -4.391 9.763 1.00 22.81 C ANISOU 2536 CD GLU A 342 2603 2818 3243 -204 -10 -204 C ATOM 2537 OE1 GLU A 342 7.099 -5.532 9.630 1.00 26.13 O ANISOU 2537 OE1 GLU A 342 3266 2651 4009 -131 -133 -366 O ATOM 2538 OE2 GLU A 342 6.881 -3.409 10.079 1.00 23.53 O ANISOU 2538 OE2 GLU A 342 2690 2941 3307 -106 -1 -279 O ATOM 2539 N ARG A 343 12.412 -7.324 8.500 1.00 20.57 N ANISOU 2539 N ARG A 343 2343 2428 3044 54 19 -95 N ATOM 2540 CA ARG A 343 13.418 -8.380 8.682 1.00 18.63 C ANISOU 2540 CA ARG A 343 1640 2668 2767 -94 125 -50 C ATOM 2541 C ARG A 343 14.847 -7.820 8.595 1.00 18.70 C ANISOU 2541 C ARG A 343 1730 2743 2629 -171 386 -8 C ATOM 2542 O ARG A 343 15.706 -8.173 9.412 1.00 20.59 O ANISOU 2542 O ARG A 343 2357 2439 3025 -339 -168 -31 O ATOM 2543 CB ARG A 343 13.227 -9.493 7.651 1.00 21.38 C ANISOU 2543 CB ARG A 343 2239 2711 3169 306 -26 -264 C ATOM 2544 CG ARG A 343 14.108 -10.727 7.875 1.00 26.31 C ANISOU 2544 CG ARG A 343 3011 2655 4330 550 -136 -363 C ATOM 2545 CD ARG A 343 14.797 -11.190 6.600 0.40 28.47 C ANISOU 2545 CD ARG A 343 3173 3517 4124 402 -10 -98 C ATOM 2546 NE ARG A 343 16.111 -10.573 6.443 0.40 31.52 N ANISOU 2546 NE ARG A 343 3836 3696 4443 -218 207 100 N ATOM 2547 CZ ARG A 343 16.635 -10.226 5.274 0.40 30.34 C ANISOU 2547 CZ ARG A 343 3160 3800 4564 -345 292 -65 C ATOM 2548 NH1 ARG A 343 15.948 -10.415 4.157 0.40 32.39 N ANISOU 2548 NH1 ARG A 343 4049 3879 4378 -354 179 -96 N ATOM 2549 NH2 ARG A 343 17.840 -9.676 5.226 0.40 30.84 N ANISOU 2549 NH2 ARG A 343 3552 3618 4547 -776 2 -192 N ATOM 2550 N GLU A 344 15.082 -6.949 7.616 1.00 19.16 N ANISOU 2550 N GLU A 344 1943 2761 2574 -61 448 20 N ATOM 2551 CA GLU A 344 16.372 -6.271 7.461 1.00 19.69 C ANISOU 2551 CA GLU A 344 2017 2868 2595 -222 308 -310 C ATOM 2552 C GLU A 344 16.716 -5.401 8.669 1.00 18.98 C ANISOU 2552 C GLU A 344 1940 2927 2344 35 392 -274 C ATOM 2553 O GLU A 344 17.857 -5.392 9.114 1.00 19.92 O ANISOU 2553 O GLU A 344 1837 3099 2629 -14 416 -121 O ATOM 2554 CB GLU A 344 16.407 -5.412 6.188 1.00 23.72 C ANISOU 2554 CB GLU A 344 2917 3331 2763 26 173 -21 C ATOM 2555 CG GLU A 344 16.613 -6.203 4.910 1.00 25.93 C ANISOU 2555 CG GLU A 344 3240 4113 2499 55 319 98 C ATOM 2556 CD GLU A 344 16.575 -5.328 3.670 0.75 25.65 C ANISOU 2556 CD GLU A 344 1898 4792 3055 371 -209 742 C ATOM 2557 OE1 GLU A 344 15.489 -4.839 3.299 0.75 25.15 O ANISOU 2557 OE1 GLU A 344 2108 4597 2848 1238 633 692 O ATOM 2558 OE2 GLU A 344 17.649 -5.135 3.065 0.75 33.61 O ANISOU 2558 OE2 GLU A 344 3268 5531 3971 156 1137 1054 O ATOM 2559 N LEU A 345 15.734 -4.665 9.184 1.00 18.78 N ANISOU 2559 N LEU A 345 1904 2657 2574 -61 395 -329 N ATOM 2560 CA LEU A 345 15.943 -3.866 10.390 1.00 18.39 C ANISOU 2560 CA LEU A 345 2099 2484 2402 190 411 -214 C ATOM 2561 C LEU A 345 16.224 -4.760 11.603 1.00 18.34 C ANISOU 2561 C LEU A 345 2027 2286 2653 -48 215 -149 C ATOM 2562 O LEU A 345 17.119 -4.460 12.391 1.00 17.08 O ANISOU 2562 O LEU A 345 1385 1862 3242 -348 392 -103 O ATOM 2563 CB LEU A 345 14.752 -2.924 10.661 1.00 19.21 C ANISOU 2563 CB LEU A 345 2106 2460 2733 234 168 -350 C ATOM 2564 CG LEU A 345 14.523 -1.795 9.647 1.00 20.20 C ANISOU 2564 CG LEU A 345 2400 2448 2825 212 267 -285 C ATOM 2565 CD1 LEU A 345 13.446 -0.833 10.135 1.00 20.21 C ANISOU 2565 CD1 LEU A 345 2342 2492 2843 173 378 -220 C ATOM 2566 CD2 LEU A 345 15.796 -1.012 9.352 1.00 21.33 C ANISOU 2566 CD2 LEU A 345 2863 2307 2932 -124 242 -195 C ATOM 2567 N LEU A 346 15.486 -5.865 11.734 1.00 17.30 N ANISOU 2567 N LEU A 346 1635 2356 2579 5 373 -154 N ATOM 2568 CA LEU A 346 15.732 -6.815 12.826 1.00 19.34 C ANISOU 2568 CA LEU A 346 2302 2325 2721 19 153 -138 C ATOM 2569 C LEU A 346 17.180 -7.323 12.802 1.00 19.30 C ANISOU 2569 C LEU A 346 2275 2154 2904 -68 -22 -141 C ATOM 2570 O LEU A 346 17.825 -7.401 13.846 1.00 18.33 O ANISOU 2570 O LEU A 346 2039 2143 2780 -315 53 -569 O ATOM 2571 CB LEU A 346 14.753 -7.998 12.778 1.00 20.83 C ANISOU 2571 CB LEU A 346 2520 2466 2926 -129 131 -169 C ATOM 2572 CG LEU A 346 14.868 -9.064 13.881 1.00 22.58 C ANISOU 2572 CG LEU A 346 2749 2672 3157 -116 -90 -3 C ATOM 2573 CD1 LEU A 346 14.730 -8.449 15.263 1.00 23.66 C ANISOU 2573 CD1 LEU A 346 3078 2558 3354 48 -10 -146 C ATOM 2574 CD2 LEU A 346 13.828 -10.162 13.692 1.00 23.63 C ANISOU 2574 CD2 LEU A 346 2900 2795 3283 -227 -41 -131 C ATOM 2575 N GLU A 347 17.684 -7.661 11.616 1.00 20.66 N ANISOU 2575 N GLU A 347 2592 2360 2895 -69 30 -127 N ATOM 2576 CA GLU A 347 19.059 -8.150 11.496 1.00 21.52 C ANISOU 2576 CA GLU A 347 2729 2313 3134 73 64 -27 C ATOM 2577 C GLU A 347 20.090 -7.068 11.832 1.00 21.10 C ANISOU 2577 C GLU A 347 2727 2290 2998 126 59 -199 C ATOM 2578 O GLU A 347 21.101 -7.368 12.469 1.00 23.11 O ANISOU 2578 O GLU A 347 3128 2412 3238 572 -113 -327 O ATOM 2579 CB GLU A 347 19.321 -8.771 10.118 1.00 25.63 C ANISOU 2579 CB GLU A 347 3638 2806 3292 -80 109 -259 C ATOM 2580 CG GLU A 347 18.496 -10.021 9.803 1.00 29.51 C ANISOU 2580 CG GLU A 347 3937 3043 4230 -270 168 -460 C ATOM 2581 CD GLU A 347 18.486 -11.070 10.909 0.30 28.89 C ANISOU 2581 CD GLU A 347 3943 2904 4128 516 548 -572 C ATOM 2582 OE1 GLU A 347 19.535 -11.699 11.149 0.30 30.55 O ANISOU 2582 OE1 GLU A 347 4709 2644 4252 1342 928 -974 O ATOM 2583 OE2 GLU A 347 17.419 -11.277 11.529 0.30 30.00 O ANISOU 2583 OE2 GLU A 347 4445 2656 4296 673 1109 -757 O ATOM 2584 N ILE A 348 19.827 -5.820 11.441 1.00 19.47 N ANISOU 2584 N ILE A 348 2245 2406 2746 90 -92 -94 N ATOM 2585 CA ILE A 348 20.683 -4.679 11.838 1.00 19.23 C ANISOU 2585 CA ILE A 348 2000 2499 2806 123 -138 -88 C ATOM 2586 C ILE A 348 20.704 -4.517 13.374 1.00 17.14 C ANISOU 2586 C ILE A 348 1487 2204 2818 214 -242 -105 C ATOM 2587 O ILE A 348 21.769 -4.331 13.973 1.00 17.89 O ANISOU 2587 O ILE A 348 1019 2492 3285 224 31 -276 O ATOM 2588 CB ILE A 348 20.251 -3.361 11.132 1.00 20.12 C ANISOU 2588 CB ILE A 348 2356 2620 2668 -19 -95 64 C ATOM 2589 CG1 ILE A 348 20.571 -3.445 9.630 1.00 21.58 C ANISOU 2589 CG1 ILE A 348 2515 2952 2731 -239 104 280 C ATOM 2590 CG2 ILE A 348 20.929 -2.143 11.758 1.00 20.85 C ANISOU 2590 CG2 ILE A 348 2480 2290 3150 224 21 -98 C ATOM 2591 CD1 ILE A 348 19.967 -2.343 8.782 1.00 22.86 C ANISOU 2591 CD1 ILE A 348 2888 3127 2669 71 150 231 C ATOM 2592 N VAL A 349 19.533 -4.614 14.001 1.00 18.13 N ANISOU 2592 N VAL A 349 1858 2107 2923 473 142 171 N ATOM 2593 CA VAL A 349 19.415 -4.523 15.464 1.00 18.83 C ANISOU 2593 CA VAL A 349 2116 2097 2940 490 110 132 C ATOM 2594 C VAL A 349 20.201 -5.672 16.130 1.00 19.97 C ANISOU 2594 C VAL A 349 2355 2028 3202 486 205 288 C ATOM 2595 O VAL A 349 20.980 -5.433 17.053 1.00 21.29 O ANISOU 2595 O VAL A 349 2586 2005 3498 353 129 83 O ATOM 2596 CB VAL A 349 17.925 -4.502 15.915 1.00 18.25 C ANISOU 2596 CB VAL A 349 2133 1962 2837 113 91 134 C ATOM 2597 CG1 VAL A 349 17.786 -4.637 17.427 1.00 20.39 C ANISOU 2597 CG1 VAL A 349 2617 2305 2824 -85 217 -51 C ATOM 2598 CG2 VAL A 349 17.251 -3.210 15.467 1.00 19.03 C ANISOU 2598 CG2 VAL A 349 2236 2297 2695 356 -58 170 C ATOM 2599 N LYS A 350 20.027 -6.897 15.638 1.00 21.08 N ANISOU 2599 N LYS A 350 2527 2396 3084 283 104 -59 N ATOM 2600 CA LYS A 350 20.762 -8.056 16.176 1.00 20.38 C ANISOU 2600 CA LYS A 350 2280 2507 2955 323 80 -205 C ATOM 2601 C LYS A 350 22.290 -7.919 16.056 1.00 20.78 C ANISOU 2601 C LYS A 350 2292 2651 2951 284 -58 -274 C ATOM 2602 O LYS A 350 23.009 -8.284 16.977 1.00 21.34 O ANISOU 2602 O LYS A 350 2184 2814 3110 199 -146 -187 O ATOM 2603 CB LYS A 350 20.278 -9.366 15.541 1.00 22.20 C ANISOU 2603 CB LYS A 350 2506 2716 3213 -9 45 -220 C ATOM 2604 CG LYS A 350 18.910 -9.799 16.048 1.00 23.40 C ANISOU 2604 CG LYS A 350 2529 2975 3385 -217 -89 -122 C ATOM 2605 CD LYS A 350 18.413 -11.080 15.391 1.00 30.10 C ANISOU 2605 CD LYS A 350 4348 2932 4156 -253 -564 -244 C ATOM 2606 CE LYS A 350 17.035 -11.452 15.925 0.75 36.44 C ANISOU 2606 CE LYS A 350 4610 4206 5029 556 167 350 C ATOM 2607 NZ LYS A 350 16.451 -12.662 15.278 0.75 42.74 N ANISOU 2607 NZ LYS A 350 6940 2640 6655 1715 -604 483 N ATOM 2608 N LYS A 351 22.770 -7.381 14.940 1.00 22.68 N ANISOU 2608 N LYS A 351 2874 2839 2903 364 44 -216 N ATOM 2609 CA LYS A 351 24.214 -7.146 14.745 1.00 27.07 C ANISOU 2609 CA LYS A 351 2809 3693 3783 476 -186 -290 C ATOM 2610 C LYS A 351 24.787 -6.042 15.645 1.00 24.90 C ANISOU 2610 C LYS A 351 2383 3634 3444 622 -335 -135 C ATOM 2611 O LYS A 351 25.963 -6.087 16.009 1.00 24.60 O ANISOU 2611 O LYS A 351 2217 3332 3798 705 -199 -304 O ATOM 2612 CB LYS A 351 24.516 -6.793 13.281 1.00 33.49 C ANISOU 2612 CB LYS A 351 4018 4989 3717 894 -28 -254 C ATOM 2613 CG LYS A 351 24.286 -7.931 12.298 1.00 38.64 C ANISOU 2613 CG LYS A 351 4579 5403 4700 524 -218 -666 C ATOM 2614 CD LYS A 351 24.325 -7.448 10.854 0.25 38.17 C ANISOU 2614 CD LYS A 351 4603 5304 4593 368 -254 -704 C ATOM 2615 CE LYS A 351 23.914 -8.546 9.887 0.25 32.79 C ANISOU 2615 CE LYS A 351 4313 4932 3212 294 4 37 C ATOM 2616 NZ LYS A 351 23.941 -8.089 8.468 0.25 31.13 N ANISOU 2616 NZ LYS A 351 4130 4506 3191 151 -52 -14 N ATOM 2617 N ASN A 352 23.957 -5.062 15.995 1.00 21.26 N ANISOU 2617 N ASN A 352 2393 2706 2977 -19 107 73 N ATOM 2618 CA ASN A 352 24.408 -3.832 16.655 1.00 19.45 C ANISOU 2618 CA ASN A 352 2128 2679 2583 -189 204 256 C ATOM 2619 C ASN A 352 24.128 -3.708 18.169 1.00 17.52 C ANISOU 2619 C ASN A 352 1668 2319 2667 -801 425 285 C ATOM 2620 O ASN A 352 24.763 -2.891 18.844 1.00 19.51 O ANISOU 2620 O ASN A 352 1332 3225 2856 -545 37 -170 O ATOM 2621 CB ASN A 352 23.829 -2.621 15.906 1.00 19.92 C ANISOU 2621 CB ASN A 352 2028 2515 3023 -39 302 196 C ATOM 2622 CG ASN A 352 24.595 -2.303 14.625 1.00 19.24 C ANISOU 2622 CG ASN A 352 1934 2555 2820 48 168 33 C ATOM 2623 OD1 ASN A 352 25.629 -1.637 14.661 1.00 21.46 O ANISOU 2623 OD1 ASN A 352 1595 3098 3460 94 175 121 O ATOM 2624 ND2 ASN A 352 24.095 -2.767 13.499 1.00 19.99 N ANISOU 2624 ND2 ASN A 352 2044 2776 2776 179 -14 120 N ATOM 2625 N PHE A 353 23.196 -4.504 18.701 1.00 17.36 N ANISOU 2625 N PHE A 353 1545 2270 2781 -689 516 260 N ATOM 2626 CA PHE A 353 22.836 -4.433 20.118 1.00 17.92 C ANISOU 2626 CA PHE A 353 1888 2172 2748 -206 323 -60 C ATOM 2627 C PHE A 353 22.961 -5.780 20.814 1.00 17.19 C ANISOU 2627 C PHE A 353 1810 1785 2935 -219 131 -376 C ATOM 2628 O PHE A 353 22.696 -6.821 20.216 1.00 19.43 O ANISOU 2628 O PHE A 353 2516 1512 3352 -174 102 -329 O ATOM 2629 CB PHE A 353 21.409 -3.899 20.275 1.00 18.39 C ANISOU 2629 CB PHE A 353 1947 2246 2794 -143 418 -93 C ATOM 2630 CG PHE A 353 21.252 -2.476 19.823 1.00 17.94 C ANISOU 2630 CG PHE A 353 1958 2206 2652 -64 521 -118 C ATOM 2631 CD1 PHE A 353 20.949 -2.184 18.501 1.00 17.20 C ANISOU 2631 CD1 PHE A 353 1876 2021 2636 -110 474 -187 C ATOM 2632 CD2 PHE A 353 21.444 -1.421 20.714 1.00 18.25 C ANISOU 2632 CD2 PHE A 353 2276 2094 2564 -96 448 12 C ATOM 2633 CE1 PHE A 353 20.820 -0.864 18.072 1.00 17.19 C ANISOU 2633 CE1 PHE A 353 2130 2023 2377 99 478 -304 C ATOM 2634 CE2 PHE A 353 21.306 -0.099 20.295 1.00 17.21 C ANISOU 2634 CE2 PHE A 353 1867 2033 2637 72 386 -108 C ATOM 2635 CZ PHE A 353 21.001 0.180 18.972 1.00 15.82 C ANISOU 2635 CZ PHE A 353 1691 1812 2508 -59 537 -218 C ATOM 2636 N ASP A 354 23.357 -5.738 22.082 1.00 17.78 N ANISOU 2636 N ASP A 354 1567 2171 3013 -39 40 -69 N ATOM 2637 CA ASP A 354 23.390 -6.909 22.957 1.00 18.84 C ANISOU 2637 CA ASP A 354 1926 2365 2867 -27 10 -26 C ATOM 2638 C ASP A 354 22.411 -6.612 24.093 1.00 17.70 C ANISOU 2638 C ASP A 354 1653 2227 2843 -278 -31 -46 C ATOM 2639 O ASP A 354 22.707 -5.819 24.984 1.00 18.50 O ANISOU 2639 O ASP A 354 1366 2528 3133 -205 -256 -237 O ATOM 2640 CB ASP A 354 24.821 -7.126 23.468 1.00 19.28 C ANISOU 2640 CB ASP A 354 1956 2402 2964 163 37 67 C ATOM 2641 CG ASP A 354 24.982 -8.405 24.281 1.00 20.06 C ANISOU 2641 CG ASP A 354 1576 2653 3393 532 325 339 C ATOM 2642 OD1 ASP A 354 24.004 -8.901 24.892 1.00 21.27 O ANISOU 2642 OD1 ASP A 354 2025 2300 3756 -244 141 381 O ATOM 2643 OD2 ASP A 354 26.119 -8.916 24.323 1.00 25.00 O ANISOU 2643 OD2 ASP A 354 2199 3486 3813 1418 151 288 O ATOM 2644 N LEU A 355 21.241 -7.251 24.050 1.00 17.01 N ANISOU 2644 N LEU A 355 1693 1937 2833 -225 14 -237 N ATOM 2645 CA LEU A 355 20.139 -6.928 24.958 1.00 18.11 C ANISOU 2645 CA LEU A 355 2168 1966 2746 12 219 -105 C ATOM 2646 C LEU A 355 20.036 -7.821 26.208 1.00 18.23 C ANISOU 2646 C LEU A 355 2231 1851 2842 245 161 -105 C ATOM 2647 O LEU A 355 18.956 -7.955 26.803 1.00 18.67 O ANISOU 2647 O LEU A 355 1813 1873 3405 140 -50 -21 O ATOM 2648 CB LEU A 355 18.826 -6.926 24.167 1.00 19.19 C ANISOU 2648 CB LEU A 355 2413 2253 2622 -7 105 -26 C ATOM 2649 CG LEU A 355 18.811 -5.984 22.955 1.00 20.65 C ANISOU 2649 CG LEU A 355 2616 2484 2743 86 22 150 C ATOM 2650 CD1 LEU A 355 17.480 -6.075 22.232 1.00 23.42 C ANISOU 2650 CD1 LEU A 355 2658 3053 3188 -83 -72 200 C ATOM 2651 CD2 LEU A 355 19.086 -4.546 23.362 1.00 20.59 C ANISOU 2651 CD2 LEU A 355 2381 2473 2967 39 148 192 C ATOM 2652 N ARG A 356 21.159 -8.419 26.602 1.00 18.39 N ANISOU 2652 N ARG A 356 2129 1892 2964 126 -78 -264 N ATOM 2653 CA ARG A 356 21.282 -9.089 27.885 1.00 19.04 C ANISOU 2653 CA ARG A 356 2134 1826 3273 169 33 22 C ATOM 2654 C ARG A 356 21.346 -8.012 28.969 1.00 18.57 C ANISOU 2654 C ARG A 356 1986 1728 3339 110 88 44 C ATOM 2655 O ARG A 356 22.076 -7.023 28.795 1.00 18.75 O ANISOU 2655 O ARG A 356 2162 1138 3823 491 73 306 O ATOM 2656 CB ARG A 356 22.572 -9.923 27.939 1.00 20.25 C ANISOU 2656 CB ARG A 356 2466 2036 3190 512 90 172 C ATOM 2657 CG ARG A 356 22.605 -11.131 27.021 1.00 20.36 C ANISOU 2657 CG ARG A 356 2301 2399 3034 254 13 58 C ATOM 2658 CD ARG A 356 23.918 -11.898 27.188 1.00 18.51 C ANISOU 2658 CD ARG A 356 2384 1942 2707 260 298 159 C ATOM 2659 NE ARG A 356 25.035 -11.208 26.538 1.00 21.44 N ANISOU 2659 NE ARG A 356 2560 2433 3152 111 426 367 N ATOM 2660 CZ ARG A 356 26.327 -11.523 26.667 1.00 21.94 C ANISOU 2660 CZ ARG A 356 2622 2389 3322 226 710 379 C ATOM 2661 NH1 ARG A 356 26.725 -12.517 27.460 1.00 23.05 N ANISOU 2661 NH1 ARG A 356 2640 2101 4014 -126 2424 1383 N ATOM 2662 NH2 ARG A 356 27.238 -10.812 26.012 1.00 23.68 N ANISOU 2662 NH2 ARG A 356 2657 2882 3455 260 1170 45 N ATOM 2663 N PRO A 357 20.620 -8.196 30.096 1.00 18.87 N ANISOU 2663 N PRO A 357 1901 1922 3346 -180 65 23 N ATOM 2664 CA PRO A 357 20.639 -7.162 31.146 1.00 18.79 C ANISOU 2664 CA PRO A 357 1981 2122 3033 -124 1 89 C ATOM 2665 C PRO A 357 22.041 -6.828 31.701 1.00 17.46 C ANISOU 2665 C PRO A 357 1689 1801 3143 72 221 38 C ATOM 2666 O PRO A 357 22.322 -5.667 32.020 1.00 17.26 O ANISOU 2666 O PRO A 357 1975 1536 3047 507 107 74 O ATOM 2667 CB PRO A 357 19.723 -7.733 32.238 1.00 20.01 C ANISOU 2667 CB PRO A 357 2460 2320 2821 46 187 112 C ATOM 2668 CG PRO A 357 19.545 -9.174 31.914 1.00 22.37 C ANISOU 2668 CG PRO A 357 2850 2412 3236 -153 94 4 C ATOM 2669 CD PRO A 357 19.708 -9.305 30.433 1.00 19.75 C ANISOU 2669 CD PRO A 357 2205 2048 3249 -240 268 162 C ATOM 2670 N GLY A 358 22.907 -7.834 31.785 1.00 18.45 N ANISOU 2670 N GLY A 358 1949 1996 3064 255 -106 221 N ATOM 2671 CA GLY A 358 24.293 -7.644 32.200 1.00 19.44 C ANISOU 2671 CA GLY A 358 1991 2349 3047 217 -119 42 C ATOM 2672 C GLY A 358 25.209 -6.897 31.247 1.00 19.28 C ANISOU 2672 C GLY A 358 2210 2058 3056 328 -55 88 C ATOM 2673 O GLY A 358 26.338 -6.565 31.621 1.00 21.14 O ANISOU 2673 O GLY A 358 2418 2093 3519 262 -277 -45 O ATOM 2674 N VAL A 359 24.758 -6.679 30.012 1.00 16.44 N ANISOU 2674 N VAL A 359 1173 1841 3231 560 -89 64 N ATOM 2675 CA VAL A 359 25.452 -5.832 29.042 1.00 17.68 C ANISOU 2675 CA VAL A 359 1972 1910 2835 649 -14 90 C ATOM 2676 C VAL A 359 24.771 -4.451 28.964 1.00 16.74 C ANISOU 2676 C VAL A 359 1690 1721 2947 405 215 31 C ATOM 2677 O VAL A 359 25.451 -3.420 28.964 1.00 17.95 O ANISOU 2677 O VAL A 359 1760 1849 3211 260 511 -12 O ATOM 2678 CB VAL A 359 25.524 -6.522 27.662 1.00 18.66 C ANISOU 2678 CB VAL A 359 2187 2109 2791 425 -17 89 C ATOM 2679 CG1 VAL A 359 26.148 -5.602 26.612 1.00 17.63 C ANISOU 2679 CG1 VAL A 359 2027 1735 2937 559 -41 81 C ATOM 2680 CG2 VAL A 359 26.321 -7.818 27.771 1.00 20.04 C ANISOU 2680 CG2 VAL A 359 2603 2089 2919 479 -122 95 C ATOM 2681 N ILE A 360 23.438 -4.431 28.945 1.00 16.18 N ANISOU 2681 N ILE A 360 1672 1737 2739 149 143 -41 N ATOM 2682 CA ILE A 360 22.688 -3.163 28.963 1.00 15.23 C ANISOU 2682 CA ILE A 360 1471 1705 2611 80 361 209 C ATOM 2683 C ILE A 360 23.151 -2.267 30.124 1.00 16.04 C ANISOU 2683 C ILE A 360 1410 1442 3241 -39 426 8 C ATOM 2684 O ILE A 360 23.310 -1.060 29.947 1.00 16.90 O ANISOU 2684 O ILE A 360 1784 1506 3129 -213 258 164 O ATOM 2685 CB ILE A 360 21.155 -3.380 29.051 1.00 15.16 C ANISOU 2685 CB ILE A 360 1610 1307 2842 -286 299 119 C ATOM 2686 CG1 ILE A 360 20.622 -4.067 27.793 1.00 18.06 C ANISOU 2686 CG1 ILE A 360 2454 1648 2759 -68 145 36 C ATOM 2687 CG2 ILE A 360 20.429 -2.042 29.206 1.00 16.67 C ANISOU 2687 CG2 ILE A 360 2167 1231 2933 -235 138 -62 C ATOM 2688 CD1 ILE A 360 19.243 -4.686 27.973 1.00 17.79 C ANISOU 2688 CD1 ILE A 360 2222 1725 2809 223 277 -69 C ATOM 2689 N VAL A 361 23.378 -2.864 31.296 1.00 17.93 N ANISOU 2689 N VAL A 361 1380 2052 3380 119 613 227 N ATOM 2690 CA VAL A 361 23.854 -2.128 32.473 1.00 18.33 C ANISOU 2690 CA VAL A 361 1325 1533 4106 967 530 -267 C ATOM 2691 C VAL A 361 25.148 -1.342 32.211 1.00 18.68 C ANISOU 2691 C VAL A 361 1937 1739 3421 474 575 -57 C ATOM 2692 O VAL A 361 25.273 -0.203 32.675 1.00 19.50 O ANISOU 2692 O VAL A 361 1847 1853 3709 414 211 -157 O ATOM 2693 CB VAL A 361 24.000 -3.050 33.717 1.00 19.14 C ANISOU 2693 CB VAL A 361 1865 1783 3622 512 243 -278 C ATOM 2694 CG1 VAL A 361 25.094 -4.101 33.544 1.00 17.04 C ANISOU 2694 CG1 VAL A 361 1738 1777 2957 507 22 45 C ATOM 2695 CG2 VAL A 361 24.241 -2.234 34.983 1.00 17.75 C ANISOU 2695 CG2 VAL A 361 1819 1845 3080 1098 -140 222 C ATOM 2696 N ARG A 362 26.077 -1.942 31.467 1.00 20.69 N ANISOU 2696 N ARG A 362 2221 1912 3727 1026 613 162 N ATOM 2697 CA ARG A 362 27.336 -1.287 31.078 1.00 24.93 C ANISOU 2697 CA ARG A 362 2824 2833 3813 93 335 233 C ATOM 2698 C ARG A 362 27.079 -0.165 30.085 1.00 22.52 C ANISOU 2698 C ARG A 362 2368 2291 3895 157 229 -66 C ATOM 2699 O ARG A 362 27.537 0.959 30.275 1.00 25.31 O ANISOU 2699 O ARG A 362 2706 2675 4233 -629 169 433 O ATOM 2700 CB ARG A 362 28.323 -2.270 30.415 1.00 31.53 C ANISOU 2700 CB ARG A 362 3536 3872 4572 415 692 -399 C ATOM 2701 CG ARG A 362 29.038 -3.231 31.347 1.00 38.73 C ANISOU 2701 CG ARG A 362 4850 5013 4852 349 424 231 C ATOM 2702 CD ARG A 362 30.313 -3.800 30.719 0.90 47.84 C ANISOU 2702 CD ARG A 362 5887 6344 5946 650 1161 -683 C ATOM 2703 NE ARG A 362 30.079 -4.873 29.738 0.90 56.81 N ANISOU 2703 NE ARG A 362 7216 7296 7072 207 470 -1396 N ATOM 2704 CZ ARG A 362 29.989 -4.735 28.407 0.90 52.93 C ANISOU 2704 CZ ARG A 362 7248 5726 7135 -291 794 -1328 C ATOM 2705 NH1 ARG A 362 30.086 -3.546 27.806 0.90 52.91 N ANISOU 2705 NH1 ARG A 362 6474 6286 7342 -676 1452 -783 N ATOM 2706 NH2 ARG A 362 29.785 -5.816 27.655 0.90 56.85 N ANISOU 2706 NH2 ARG A 362 7923 6155 7521 369 956 -2016 N ATOM 2707 N ASP A 363 26.368 -0.492 29.011 1.00 23.30 N ANISOU 2707 N ASP A 363 2271 2748 3831 -169 252 92 N ATOM 2708 CA ASP A 363 26.097 0.467 27.930 1.00 22.10 C ANISOU 2708 CA ASP A 363 2464 2263 3667 200 270 -266 C ATOM 2709 C ASP A 363 25.343 1.708 28.394 1.00 20.48 C ANISOU 2709 C ASP A 363 2428 1690 3661 -61 485 189 C ATOM 2710 O ASP A 363 25.658 2.825 27.961 1.00 19.94 O ANISOU 2710 O ASP A 363 1823 1775 3977 -714 636 -116 O ATOM 2711 CB ASP A 363 25.344 -0.213 26.777 1.00 21.19 C ANISOU 2711 CB ASP A 363 1824 2744 3482 403 172 -27 C ATOM 2712 CG ASP A 363 26.215 -1.206 26.014 1.00 22.16 C ANISOU 2712 CG ASP A 363 1828 2770 3819 26 249 -533 C ATOM 2713 OD1 ASP A 363 27.452 -1.095 26.069 1.00 26.56 O ANISOU 2713 OD1 ASP A 363 1773 3636 4682 -77 761 -180 O ATOM 2714 OD2 ASP A 363 25.672 -2.098 25.352 1.00 26.04 O ANISOU 2714 OD2 ASP A 363 2685 3154 4052 -482 392 -781 O ATOM 2715 N LEU A 364 24.385 1.519 29.297 1.00 18.46 N ANISOU 2715 N LEU A 364 2058 1522 3431 126 340 -185 N ATOM 2716 CA LEU A 364 23.511 2.606 29.729 1.00 20.60 C ANISOU 2716 CA LEU A 364 2771 1620 3434 460 444 -176 C ATOM 2717 C LEU A 364 23.780 3.117 31.158 1.00 19.28 C ANISOU 2717 C LEU A 364 2413 1617 3293 548 519 -88 C ATOM 2718 O LEU A 364 23.009 3.930 31.669 1.00 16.49 O ANISOU 2718 O LEU A 364 1268 1926 3071 30 492 -300 O ATOM 2719 CB LEU A 364 22.054 2.160 29.558 1.00 23.78 C ANISOU 2719 CB LEU A 364 2457 1328 5250 1272 605 -575 C ATOM 2720 CG LEU A 364 21.639 1.785 28.125 1.00 28.13 C ANISOU 2720 CG LEU A 364 3967 2284 4437 588 812 147 C ATOM 2721 CD1 LEU A 364 20.159 1.436 28.088 1.00 27.57 C ANISOU 2721 CD1 LEU A 364 3840 1831 4802 1829 512 -224 C ATOM 2722 CD2 LEU A 364 21.931 2.896 27.113 1.00 23.76 C ANISOU 2722 CD2 LEU A 364 2911 2877 3239 230 273 -54 C ATOM 2723 N ASP A 365 24.875 2.666 31.777 1.00 19.03 N ANISOU 2723 N ASP A 365 2059 1746 3424 -65 389 118 N ATOM 2724 CA ASP A 365 25.300 3.122 33.116 1.00 22.53 C ANISOU 2724 CA ASP A 365 2756 2081 3720 -278 214 -101 C ATOM 2725 C ASP A 365 24.193 2.998 34.164 1.00 21.24 C ANISOU 2725 C ASP A 365 2212 2023 3835 -623 -54 -159 C ATOM 2726 O ASP A 365 23.939 3.934 34.929 1.00 20.07 O ANISOU 2726 O ASP A 365 1675 1613 4335 -814 -216 -204 O ATOM 2727 CB ASP A 365 25.796 4.578 33.068 1.00 25.24 C ANISOU 2727 CB ASP A 365 3061 2229 4298 -515 211 -176 C ATOM 2728 CG ASP A 365 26.899 4.790 32.054 1.00 30.64 C ANISOU 2728 CG ASP A 365 3184 3022 5433 -129 827 -209 C ATOM 2729 OD1 ASP A 365 27.858 4.005 32.057 1.00 34.64 O ANISOU 2729 OD1 ASP A 365 3824 3415 5921 483 688 -209 O ATOM 2730 OD2 ASP A 365 26.817 5.752 31.262 1.00 40.26 O ANISOU 2730 OD2 ASP A 365 4355 3514 7429 -1096 628 956 O ATOM 2731 N LEU A 366 23.544 1.835 34.203 1.00 19.15 N ANISOU 2731 N LEU A 366 1680 1835 3760 -313 -445 13 N ATOM 2732 CA LEU A 366 22.342 1.662 35.014 1.00 20.22 C ANISOU 2732 CA LEU A 366 2215 2113 3355 -236 -206 -86 C ATOM 2733 C LEU A 366 22.564 1.383 36.512 1.00 20.68 C ANISOU 2733 C LEU A 366 2506 1937 3411 -16 -368 -132 C ATOM 2734 O LEU A 366 21.588 1.194 37.242 1.00 21.25 O ANISOU 2734 O LEU A 366 2153 2106 3812 192 -410 -245 O ATOM 2735 CB LEU A 366 21.418 0.619 34.361 1.00 19.24 C ANISOU 2735 CB LEU A 366 2052 1939 3318 -192 -160 51 C ATOM 2736 CG LEU A 366 20.919 0.990 32.959 1.00 20.00 C ANISOU 2736 CG LEU A 366 2310 2103 3186 -85 -11 119 C ATOM 2737 CD1 LEU A 366 19.980 -0.083 32.419 1.00 19.44 C ANISOU 2737 CD1 LEU A 366 2178 2200 3009 1 -108 125 C ATOM 2738 CD2 LEU A 366 20.211 2.347 32.936 1.00 19.21 C ANISOU 2738 CD2 LEU A 366 2302 2073 2922 -142 29 219 C ATOM 2739 N LYS A 367 23.818 1.386 36.976 1.00 19.12 N ANISOU 2739 N LYS A 367 2377 1852 3034 50 -150 -215 N ATOM 2740 CA LYS A 367 24.107 1.395 38.419 1.00 20.25 C ANISOU 2740 CA LYS A 367 2246 2337 3109 82 -235 -183 C ATOM 2741 C LYS A 367 24.267 2.805 39.007 1.00 19.85 C ANISOU 2741 C LYS A 367 1861 2421 3257 -71 -121 -273 C ATOM 2742 O LYS A 367 24.411 2.943 40.220 1.00 20.33 O ANISOU 2742 O LYS A 367 1429 2884 3409 -162 -263 -575 O ATOM 2743 CB LYS A 367 25.358 0.569 38.738 1.00 20.66 C ANISOU 2743 CB LYS A 367 1905 3083 2860 130 -129 -212 C ATOM 2744 CG LYS A 367 25.359 -0.823 38.135 1.00 20.17 C ANISOU 2744 CG LYS A 367 1891 2940 2830 118 -286 -39 C ATOM 2745 CD LYS A 367 26.493 -1.666 38.691 1.00 21.79 C ANISOU 2745 CD LYS A 367 2374 3127 2778 346 -299 185 C ATOM 2746 CE LYS A 367 26.470 -3.064 38.102 1.00 25.35 C ANISOU 2746 CE LYS A 367 3170 3165 3295 263 -214 98 C ATOM 2747 NZ LYS A 367 27.638 -3.873 38.553 1.00 24.95 N ANISOU 2747 NZ LYS A 367 3075 3326 3077 361 -116 -109 N ATOM 2748 N LYS A 368 24.228 3.841 38.168 1.00 18.45 N ANISOU 2748 N LYS A 368 1679 2503 2829 -191 119 -376 N ATOM 2749 CA LYS A 368 24.353 5.226 38.639 1.00 20.11 C ANISOU 2749 CA LYS A 368 1792 2558 3289 -19 20 -561 C ATOM 2750 C LYS A 368 23.047 5.682 39.302 1.00 20.15 C ANISOU 2750 C LYS A 368 1795 2741 3119 -73 68 -485 C ATOM 2751 O LYS A 368 21.967 5.405 38.778 1.00 20.89 O ANISOU 2751 O LYS A 368 2044 2665 3226 -94 -187 -708 O ATOM 2752 CB LYS A 368 24.684 6.171 37.482 1.00 24.05 C ANISOU 2752 CB LYS A 368 2818 3023 3297 -238 299 -538 C ATOM 2753 CG LYS A 368 26.079 5.997 36.901 1.00 26.86 C ANISOU 2753 CG LYS A 368 2904 3441 3861 -163 418 -494 C ATOM 2754 CD LYS A 368 26.363 7.070 35.860 0.25 27.44 C ANISOU 2754 CD LYS A 368 3213 3562 3651 -227 223 -457 C ATOM 2755 CE LYS A 368 27.844 7.176 35.538 0.25 26.25 C ANISOU 2755 CE LYS A 368 3228 3331 3416 -228 203 -243 C ATOM 2756 NZ LYS A 368 28.090 8.251 34.537 0.25 26.77 N ANISOU 2756 NZ LYS A 368 3409 3277 3484 -247 150 -223 N ATOM 2757 N PRO A 369 23.136 6.397 40.440 1.00 20.38 N ANISOU 2757 N PRO A 369 2351 2332 3059 97 133 -342 N ATOM 2758 CA PRO A 369 21.924 6.839 41.130 1.00 21.82 C ANISOU 2758 CA PRO A 369 2437 2543 3311 177 249 -326 C ATOM 2759 C PRO A 369 21.285 8.077 40.472 1.00 21.57 C ANISOU 2759 C PRO A 369 2050 2674 3471 248 66 -403 C ATOM 2760 O PRO A 369 21.301 9.162 41.049 1.00 21.16 O ANISOU 2760 O PRO A 369 2495 2431 3111 290 -16 -83 O ATOM 2761 CB PRO A 369 22.436 7.141 42.543 1.00 18.39 C ANISOU 2761 CB PRO A 369 1801 1798 3387 1218 436 -813 C ATOM 2762 CG PRO A 369 23.830 7.632 42.311 1.00 21.24 C ANISOU 2762 CG PRO A 369 2346 2784 2940 269 130 -179 C ATOM 2763 CD PRO A 369 24.354 6.830 41.151 1.00 21.44 C ANISOU 2763 CD PRO A 369 2516 2711 2918 161 -9 -211 C ATOM 2764 N ILE A 370 20.718 7.901 39.279 1.00 21.82 N ANISOU 2764 N ILE A 370 2046 2774 3471 -314 60 11 N ATOM 2765 CA ILE A 370 20.084 9.008 38.532 1.00 24.20 C ANISOU 2765 CA ILE A 370 2500 2856 3838 -147 -62 81 C ATOM 2766 C ILE A 370 18.585 8.790 38.301 1.00 21.11 C ANISOU 2766 C ILE A 370 2501 2479 3041 -100 -126 431 C ATOM 2767 O ILE A 370 17.961 9.499 37.513 1.00 21.85 O ANISOU 2767 O ILE A 370 1274 2995 4030 -228 -67 983 O ATOM 2768 CB ILE A 370 20.823 9.314 37.199 1.00 28.28 C ANISOU 2768 CB ILE A 370 3274 3508 3960 -37 31 414 C ATOM 2769 CG1 ILE A 370 21.054 8.058 36.336 1.00 30.08 C ANISOU 2769 CG1 ILE A 370 3366 3716 4345 -302 286 82 C ATOM 2770 CG2 ILE A 370 22.160 9.985 37.503 1.00 30.71 C ANISOU 2770 CG2 ILE A 370 3421 3658 4586 -228 93 333 C ATOM 2771 CD1 ILE A 370 19.810 7.449 35.722 1.00 33.87 C ANISOU 2771 CD1 ILE A 370 3729 4393 4744 -315 -150 -148 C ATOM 2772 N TYR A 371 18.000 7.839 39.019 1.00 18.13 N ANISOU 2772 N TYR A 371 2216 2317 2352 -159 -170 9 N ATOM 2773 CA TYR A 371 16.622 7.421 38.751 1.00 17.06 C ANISOU 2773 CA TYR A 371 2090 2033 2359 -12 11 -60 C ATOM 2774 C TYR A 371 15.520 8.353 39.261 1.00 17.57 C ANISOU 2774 C TYR A 371 2036 1914 2724 37 25 132 C ATOM 2775 O TYR A 371 14.467 8.455 38.623 1.00 17.86 O ANISOU 2775 O TYR A 371 2048 1957 2777 110 33 184 O ATOM 2776 CB TYR A 371 16.403 6.016 39.276 1.00 16.07 C ANISOU 2776 CB TYR A 371 1882 1956 2266 -94 -4 -208 C ATOM 2777 CG TYR A 371 17.189 4.983 38.515 1.00 17.07 C ANISOU 2777 CG TYR A 371 1723 2007 2753 112 82 -137 C ATOM 2778 CD1 TYR A 371 16.816 4.615 37.221 1.00 18.34 C ANISOU 2778 CD1 TYR A 371 1953 2277 2736 291 380 -359 C ATOM 2779 CD2 TYR A 371 18.308 4.367 39.078 1.00 16.42 C ANISOU 2779 CD2 TYR A 371 1553 2219 2465 -46 134 -82 C ATOM 2780 CE1 TYR A 371 17.521 3.644 36.514 1.00 18.56 C ANISOU 2780 CE1 TYR A 371 2128 2225 2696 95 455 -511 C ATOM 2781 CE2 TYR A 371 19.019 3.398 38.376 1.00 18.31 C ANISOU 2781 CE2 TYR A 371 1744 2368 2845 151 210 -137 C ATOM 2782 CZ TYR A 371 18.625 3.045 37.100 1.00 19.31 C ANISOU 2782 CZ TYR A 371 1930 2632 2773 -6 469 -285 C ATOM 2783 OH TYR A 371 19.321 2.083 36.413 1.00 20.01 O ANISOU 2783 OH TYR A 371 1948 2797 2857 97 190 -487 O ATOM 2784 N GLN A 372 15.735 9.031 40.387 1.00 16.12 N ANISOU 2784 N GLN A 372 1717 1684 2723 233 118 183 N ATOM 2785 CA GLN A 372 14.726 9.986 40.871 1.00 17.57 C ANISOU 2785 CA GLN A 372 2257 1653 2764 361 75 -71 C ATOM 2786 C GLN A 372 14.400 11.044 39.792 1.00 18.20 C ANISOU 2786 C GLN A 372 2452 1679 2782 160 -95 -30 C ATOM 2787 O GLN A 372 13.241 11.452 39.664 1.00 18.48 O ANISOU 2787 O GLN A 372 2571 1602 2847 233 -384 -259 O ATOM 2788 CB GLN A 372 15.138 10.636 42.194 1.00 18.71 C ANISOU 2788 CB GLN A 372 2355 1930 2821 182 -30 -92 C ATOM 2789 CG GLN A 372 13.991 11.378 42.876 1.00 20.07 C ANISOU 2789 CG GLN A 372 2291 2366 2965 106 50 -245 C ATOM 2790 CD GLN A 372 14.380 12.017 44.192 1.00 20.35 C ANISOU 2790 CD GLN A 372 2386 2299 3044 274 73 -384 C ATOM 2791 OE1 GLN A 372 15.443 11.741 44.744 1.00 21.38 O ANISOU 2791 OE1 GLN A 372 2440 2677 3004 -81 -145 -201 O ATOM 2792 NE2 GLN A 372 13.512 12.886 44.703 1.00 21.41 N ANISOU 2792 NE2 GLN A 372 2190 2460 3484 91 246 -644 N ATOM 2793 N AARG A 373 15.422 11.460 39.026 0.50 18.96 N ANISOU 2793 N AARG A 373 2322 1940 2939 61 -135 -53 N ATOM 2794 CA AARG A 373 15.265 12.378 37.875 0.50 20.58 C ANISOU 2794 CA AARG A 373 2647 2241 2930 -2 -314 13 C ATOM 2795 C AARG A 373 14.251 11.906 36.825 0.50 18.87 C ANISOU 2795 C AARG A 373 2238 1844 3087 155 -342 142 C ATOM 2796 O AARG A 373 13.594 12.727 36.182 0.50 17.57 O ANISOU 2796 O AARG A 373 1844 1597 3233 7 -438 -19 O ATOM 2797 CB AARG A 373 16.601 12.592 37.140 0.50 24.27 C ANISOU 2797 CB AARG A 373 3182 2747 3291 -235 147 259 C ATOM 2798 CG AARG A 373 17.661 13.403 37.871 0.50 27.77 C ANISOU 2798 CG AARG A 373 3699 3504 3346 -398 -115 37 C ATOM 2799 CD AARG A 373 18.663 14.011 36.888 0.50 32.99 C ANISOU 2799 CD AARG A 373 3774 4414 4345 -339 459 227 C ATOM 2800 NE AARG A 373 19.686 13.073 36.419 0.50 37.15 N ANISOU 2800 NE AARG A 373 3878 5122 5114 240 162 297 N ATOM 2801 CZ AARG A 373 20.312 13.173 35.245 0.50 34.92 C ANISOU 2801 CZ AARG A 373 3867 4336 5065 354 63 796 C ATOM 2802 NH1AARG A 373 20.001 14.153 34.407 0.50 38.12 N ANISOU 2802 NH1AARG A 373 4485 4820 5178 95 -375 1119 N ATOM 2803 NH2AARG A 373 21.237 12.289 34.895 0.50 25.88 N ANISOU 2803 NH2AARG A 373 2334 3794 3706 -549 73 1240 N ATOM 2804 N BARG A 373 15.400 11.451 39.019 0.50 18.60 N ANISOU 2804 N BARG A 373 2271 1882 2910 113 -136 -60 N ATOM 2805 CA BARG A 373 15.176 12.407 37.947 0.50 19.54 C ANISOU 2805 CA BARG A 373 2380 2123 2918 74 -195 27 C ATOM 2806 C BARG A 373 14.237 11.910 36.829 0.50 18.83 C ANISOU 2806 C BARG A 373 2339 1784 3031 298 -463 243 C ATOM 2807 O BARG A 373 13.590 12.722 36.164 0.50 20.62 O ANISOU 2807 O BARG A 373 3073 1655 3106 249 -740 339 O ATOM 2808 CB BARG A 373 16.505 12.845 37.351 0.50 22.25 C ANISOU 2808 CB BARG A 373 2510 2735 3210 1 111 -70 C ATOM 2809 CG BARG A 373 16.337 14.063 36.480 0.50 22.76 C ANISOU 2809 CG BARG A 373 2277 3044 3327 -61 242 145 C ATOM 2810 CD BARG A 373 17.648 14.599 35.945 0.50 25.33 C ANISOU 2810 CD BARG A 373 2602 3316 3705 -490 329 202 C ATOM 2811 NE BARG A 373 17.377 15.210 34.659 0.50 26.54 N ANISOU 2811 NE BARG A 373 2807 3469 3805 -472 237 189 N ATOM 2812 CZ BARG A 373 17.863 14.775 33.509 0.50 26.13 C ANISOU 2812 CZ BARG A 373 2712 3275 3941 -617 326 11 C ATOM 2813 NH1BARG A 373 18.709 13.753 33.477 0.50 24.20 N ANISOU 2813 NH1BARG A 373 3101 2823 3268 -768 60 116 N ATOM 2814 NH2BARG A 373 17.524 15.394 32.396 0.50 24.79 N ANISOU 2814 NH2BARG A 373 2270 3182 3965 -245 347 -204 N ATOM 2815 N THR A 374 14.147 10.591 36.647 1.00 17.57 N ANISOU 2815 N THR A 374 1981 1925 2767 167 -381 -149 N ATOM 2816 CA THR A 374 13.273 9.988 35.615 1.00 15.85 C ANISOU 2816 CA THR A 374 1575 1879 2566 -27 -165 114 C ATOM 2817 C THR A 374 11.794 9.906 36.003 1.00 15.48 C ANISOU 2817 C THR A 374 1576 1717 2589 36 -139 92 C ATOM 2818 O THR A 374 10.953 9.680 35.132 1.00 16.92 O ANISOU 2818 O THR A 374 2036 1722 2671 -148 -314 -4 O ATOM 2819 CB THR A 374 13.716 8.552 35.252 1.00 15.29 C ANISOU 2819 CB THR A 374 1588 1900 2321 -74 -169 52 C ATOM 2820 OG1 THR A 374 13.421 7.652 36.333 1.00 15.55 O ANISOU 2820 OG1 THR A 374 1691 1627 2587 -342 -116 17 O ATOM 2821 CG2 THR A 374 15.225 8.500 34.912 1.00 15.66 C ANISOU 2821 CG2 THR A 374 1652 1871 2425 -33 -48 -64 C ATOM 2822 N ALA A 375 11.490 10.074 37.292 1.00 15.39 N ANISOU 2822 N ALA A 375 1704 1551 2592 64 -80 0 N ATOM 2823 CA ALA A 375 10.221 9.623 37.872 1.00 15.54 C ANISOU 2823 CA ALA A 375 1749 1813 2340 -45 -122 -54 C ATOM 2824 C ALA A 375 9.070 10.630 37.785 1.00 16.55 C ANISOU 2824 C ALA A 375 1950 1732 2606 10 -108 87 C ATOM 2825 O ALA A 375 7.971 10.352 38.280 1.00 16.90 O ANISOU 2825 O ALA A 375 1855 1602 2961 70 -82 193 O ATOM 2826 CB ALA A 375 10.437 9.184 39.317 1.00 15.76 C ANISOU 2826 CB ALA A 375 2046 1787 2151 -150 -37 -298 C ATOM 2827 N ALA A 376 9.316 11.784 37.167 1.00 18.05 N ANISOU 2827 N ALA A 376 1982 1799 3075 -335 -280 183 N ATOM 2828 CA ALA A 376 8.238 12.681 36.723 1.00 21.03 C ANISOU 2828 CA ALA A 376 2106 2400 3484 16 -200 380 C ATOM 2829 C ALA A 376 8.609 13.263 35.368 1.00 18.17 C ANISOU 2829 C ALA A 376 1898 1822 3183 211 -142 -55 C ATOM 2830 O ALA A 376 9.798 13.315 35.023 1.00 19.18 O ANISOU 2830 O ALA A 376 1670 2172 3444 331 -355 -133 O ATOM 2831 CB ALA A 376 8.008 13.789 37.733 1.00 21.53 C ANISOU 2831 CB ALA A 376 1495 1702 4982 1094 -838 406 C ATOM 2832 N TYR A 377 7.591 13.677 34.611 1.00 16.61 N ANISOU 2832 N TYR A 377 1822 1695 2794 354 5 -263 N ATOM 2833 CA TYR A 377 7.749 14.256 33.254 1.00 17.84 C ANISOU 2833 CA TYR A 377 1815 2064 2897 183 64 -124 C ATOM 2834 C TYR A 377 8.233 13.271 32.162 1.00 16.86 C ANISOU 2834 C TYR A 377 1480 2241 2683 -19 44 -118 C ATOM 2835 O TYR A 377 8.667 13.702 31.086 1.00 17.90 O ANISOU 2835 O TYR A 377 2168 1973 2660 167 -47 75 O ATOM 2836 CB TYR A 377 8.618 15.533 33.281 1.00 17.40 C ANISOU 2836 CB TYR A 377 2129 1811 2671 273 74 96 C ATOM 2837 CG TYR A 377 8.213 16.529 34.350 1.00 17.18 C ANISOU 2837 CG TYR A 377 1898 1829 2797 115 40 -39 C ATOM 2838 CD1 TYR A 377 6.996 17.203 34.273 1.00 18.48 C ANISOU 2838 CD1 TYR A 377 2306 1861 2852 483 -90 -138 C ATOM 2839 CD2 TYR A 377 9.040 16.800 35.437 1.00 19.23 C ANISOU 2839 CD2 TYR A 377 2474 2161 2669 221 -54 -140 C ATOM 2840 CE1 TYR A 377 6.611 18.114 35.249 1.00 20.04 C ANISOU 2840 CE1 TYR A 377 2657 1719 3235 163 -100 -439 C ATOM 2841 CE2 TYR A 377 8.666 17.716 36.419 1.00 19.95 C ANISOU 2841 CE2 TYR A 377 2548 1902 3129 391 -69 -224 C ATOM 2842 CZ TYR A 377 7.450 18.367 36.318 1.00 19.78 C ANISOU 2842 CZ TYR A 377 2610 1804 3100 416 -61 -369 C ATOM 2843 OH TYR A 377 7.077 19.276 37.280 1.00 20.77 O ANISOU 2843 OH TYR A 377 2419 1713 3760 350 -36 -681 O ATOM 2844 N GLY A 378 8.124 11.964 32.421 1.00 16.28 N ANISOU 2844 N GLY A 378 1518 2244 2420 136 88 -65 N ATOM 2845 CA GLY A 378 8.446 10.925 31.434 1.00 12.52 C ANISOU 2845 CA GLY A 378 771 1822 2164 145 -85 220 C ATOM 2846 C GLY A 378 9.892 10.485 31.502 1.00 13.00 C ANISOU 2846 C GLY A 378 844 1689 2404 264 20 139 C ATOM 2847 O GLY A 378 10.758 11.260 31.882 1.00 16.45 O ANISOU 2847 O GLY A 378 1520 1971 2757 -290 -2 214 O ATOM 2848 N HIS A 379 10.141 9.224 31.144 1.00 14.58 N ANISOU 2848 N HIS A 379 1284 1744 2511 348 -82 60 N ATOM 2849 CA HIS A 379 11.502 8.646 31.168 1.00 14.19 C ANISOU 2849 CA HIS A 379 1291 1652 2446 330 -188 13 C ATOM 2850 C HIS A 379 12.234 8.847 29.852 1.00 15.78 C ANISOU 2850 C HIS A 379 1634 1884 2478 320 -86 -49 C ATOM 2851 O HIS A 379 13.472 8.662 29.787 1.00 15.86 O ANISOU 2851 O HIS A 379 1604 1619 2800 296 -52 -216 O ATOM 2852 CB HIS A 379 11.434 7.149 31.489 1.00 16.47 C ANISOU 2852 CB HIS A 379 1910 1706 2640 129 -299 83 C ATOM 2853 CG HIS A 379 10.930 6.866 32.867 1.00 17.14 C ANISOU 2853 CG HIS A 379 2117 1795 2600 85 -321 -14 C ATOM 2854 ND1 HIS A 379 11.690 6.236 33.826 1.00 15.22 N ANISOU 2854 ND1 HIS A 379 1599 1708 2474 -162 -153 -72 N ATOM 2855 CD2 HIS A 379 9.744 7.155 33.454 1.00 21.61 C ANISOU 2855 CD2 HIS A 379 1377 2879 3955 1010 -1088 664 C ATOM 2856 CE1 HIS A 379 11.000 6.158 34.948 1.00 15.96 C ANISOU 2856 CE1 HIS A 379 1765 1719 2577 -293 -49 29 C ATOM 2857 NE2 HIS A 379 9.813 6.705 34.746 1.00 17.96 N ANISOU 2857 NE2 HIS A 379 1938 1634 3252 -77 -165 -154 N ATOM 2858 N PHE A 380 11.473 9.214 28.814 1.00 16.43 N ANISOU 2858 N PHE A 380 1957 1794 2491 501 -136 -31 N ATOM 2859 CA PHE A 380 11.985 9.336 27.457 1.00 18.28 C ANISOU 2859 CA PHE A 380 2288 2108 2548 413 -40 -34 C ATOM 2860 C PHE A 380 11.789 10.722 26.873 1.00 19.24 C ANISOU 2860 C PHE A 380 2341 2147 2818 535 84 13 C ATOM 2861 O PHE A 380 10.880 11.466 27.252 1.00 21.28 O ANISOU 2861 O PHE A 380 2604 2123 3357 709 193 114 O ATOM 2862 CB PHE A 380 11.344 8.280 26.545 1.00 18.14 C ANISOU 2862 CB PHE A 380 2330 2112 2449 282 -75 114 C ATOM 2863 CG PHE A 380 11.428 6.877 27.091 1.00 17.92 C ANISOU 2863 CG PHE A 380 2334 2100 2374 182 -161 92 C ATOM 2864 CD1 PHE A 380 12.616 6.393 27.638 1.00 16.61 C ANISOU 2864 CD1 PHE A 380 1835 2097 2377 -18 -11 -240 C ATOM 2865 CD2 PHE A 380 10.316 6.033 27.060 1.00 18.65 C ANISOU 2865 CD2 PHE A 380 2420 2372 2291 -3 69 67 C ATOM 2866 CE1 PHE A 380 12.691 5.102 28.144 1.00 17.66 C ANISOU 2866 CE1 PHE A 380 1952 2264 2493 86 -100 -83 C ATOM 2867 CE2 PHE A 380 10.390 4.741 27.566 1.00 18.66 C ANISOU 2867 CE2 PHE A 380 2257 2255 2578 123 128 -64 C ATOM 2868 CZ PHE A 380 11.577 4.276 28.112 1.00 18.12 C ANISOU 2868 CZ PHE A 380 2364 1897 2623 -38 -86 -110 C ATOM 2869 N GLY A 381 12.663 11.038 25.923 1.00 17.12 N ANISOU 2869 N GLY A 381 1327 1870 3307 1210 175 -238 N ATOM 2870 CA GLY A 381 12.726 12.341 25.287 1.00 20.17 C ANISOU 2870 CA GLY A 381 2206 2029 3426 116 368 -183 C ATOM 2871 C GLY A 381 13.321 13.432 26.148 1.00 23.07 C ANISOU 2871 C GLY A 381 2854 2068 3841 -185 369 -272 C ATOM 2872 O GLY A 381 13.200 14.607 25.794 1.00 24.07 O ANISOU 2872 O GLY A 381 2778 1813 4553 -886 493 -271 O ATOM 2873 N ARG A 382 13.976 13.041 27.248 1.00 26.12 N ANISOU 2873 N ARG A 382 3002 3065 3856 -321 208 -355 N ATOM 2874 C ARG A 382 16.036 14.118 28.108 1.00 29.50 C ANISOU 2874 C ARG A 382 3815 3667 3727 -182 374 -801 C ATOM 2875 O ARG A 382 16.720 13.236 27.572 1.00 29.75 O ANISOU 2875 O ARG A 382 3287 3542 4473 -449 434 -825 O ATOM 2876 CA AARG A 382 14.530 13.926 28.288 0.50 28.73 C ANISOU 2876 CA AARG A 382 3912 3365 3636 -368 431 -569 C ATOM 2877 CB AARG A 382 14.339 13.307 29.692 0.50 29.93 C ANISOU 2877 CB AARG A 382 4311 3106 3953 -569 388 -289 C ATOM 2878 CG AARG A 382 12.917 12.991 30.135 0.50 27.06 C ANISOU 2878 CG AARG A 382 4380 2406 3495 -799 255 -222 C ATOM 2879 CD AARG A 382 12.255 14.150 30.870 0.50 23.10 C ANISOU 2879 CD AARG A 382 3638 1994 3141 -1217 65 -134 C ATOM 2880 NE AARG A 382 13.094 14.729 31.924 0.50 21.85 N ANISOU 2880 NE AARG A 382 4290 794 3217 -1253 83 -322 N ATOM 2881 CZ AARG A 382 13.184 14.253 33.159 0.50 25.80 C ANISOU 2881 CZ AARG A 382 4582 2007 3211 -1630 26 -129 C ATOM 2882 NH1AARG A 382 12.490 13.177 33.505 0.50 27.91 N ANISOU 2882 NH1AARG A 382 4358 2835 3411 -1877 416 298 N ATOM 2883 NH2AARG A 382 13.969 14.854 34.050 0.50 31.77 N ANISOU 2883 NH2AARG A 382 6222 1490 4356 -2362 -414 -553 N ATOM 2884 CA BARG A 382 14.520 14.050 28.140 0.50 29.28 C ANISOU 2884 CA BARG A 382 3779 3393 3950 -213 253 -712 C ATOM 2885 CB BARG A 382 13.945 13.900 29.539 0.50 29.96 C ANISOU 2885 CB BARG A 382 3242 3885 4254 -156 369 -547 C ATOM 2886 CG BARG A 382 12.634 14.652 29.648 0.50 32.07 C ANISOU 2886 CG BARG A 382 3877 3489 4816 358 -193 -459 C ATOM 2887 CD BARG A 382 12.352 15.016 31.081 0.50 30.82 C ANISOU 2887 CD BARG A 382 4238 2736 4735 12 -378 -292 C ATOM 2888 NE BARG A 382 12.057 13.854 31.877 0.50 18.79 N ANISOU 2888 NE BARG A 382 924 542 5672 290 -1644 -1120 N ATOM 2889 CZ BARG A 382 12.400 13.757 33.145 0.50 20.08 C ANISOU 2889 CZ BARG A 382 1715 1468 4444 -937 -720 -246 C ATOM 2890 NH1BARG A 382 13.074 14.748 33.713 0.50 19.03 N ANISOU 2890 NH1BARG A 382 2624 2316 2290 -2153 -1202 1053 N ATOM 2891 NH2BARG A 382 12.091 12.670 33.823 0.50 15.81 N ANISOU 2891 NH2BARG A 382 1169 646 4192 -169 -1254 -489 N ATOM 2892 N ASP A 383 16.544 15.222 28.634 1.00 22.40 N ANISOU 2892 N ASP A 383 3186 2266 3058 1418 1307 -1042 N ATOM 2893 CA ASP A 383 17.943 15.578 28.503 1.00 30.60 C ANISOU 2893 CA ASP A 383 4107 2851 4666 -135 715 219 C ATOM 2894 C ASP A 383 18.829 14.625 29.276 1.00 35.30 C ANISOU 2894 C ASP A 383 4981 2507 5921 -180 355 517 C ATOM 2895 O ASP A 383 18.493 14.204 30.387 1.00 39.17 O ANISOU 2895 O ASP A 383 5353 3844 5684 -646 122 380 O ATOM 2896 CB ASP A 383 18.203 17.004 29.023 1.00 35.86 C ANISOU 2896 CB ASP A 383 5230 2870 5522 -491 66 266 C ATOM 2897 CG ASP A 383 17.403 18.078 28.278 0.50 34.17 C ANISOU 2897 CG ASP A 383 4970 2011 6001 -866 -134 90 C ATOM 2898 OD1 ASP A 383 16.892 17.825 27.167 0.50 32.14 O ANISOU 2898 OD1 ASP A 383 4905 1299 6008 -1200 -356 629 O ATOM 2899 OD2 ASP A 383 17.294 19.194 28.822 0.50 32.68 O ANISOU 2899 OD2 ASP A 383 4871 994 6552 -896 -134 969 O ATOM 2900 N SER A 384 19.933 14.253 28.648 1.00 33.01 N ANISOU 2900 N SER A 384 5277 1760 5502 -822 817 616 N ATOM 2901 CA SER A 384 21.122 13.750 29.324 1.00 43.58 C ANISOU 2901 CA SER A 384 5395 4018 7144 -899 37 995 C ATOM 2902 C SER A 384 20.930 12.370 29.946 1.00 39.92 C ANISOU 2902 C SER A 384 4427 2373 8365 -793 -1172 -323 C ATOM 2903 O SER A 384 21.389 12.137 31.074 1.00 50.38 O ANISOU 2903 O SER A 384 4568 4146 10426 -424 -2744 1391 O ATOM 2904 CB SER A 384 21.611 14.768 30.376 1.00 54.51 C ANISOU 2904 CB SER A 384 6879 6075 7757 -781 24 -468 C ATOM 2905 OG SER A 384 22.908 14.442 30.852 1.00 53.02 O ANISOU 2905 OG SER A 384 7608 5886 6648 -1147 -1026 -1090 O ATOM 2906 N PHE A 385 20.247 11.470 29.223 1.00 27.68 N ANISOU 2906 N PHE A 385 3653 1351 5510 97 -344 34 N ATOM 2907 CA PHE A 385 20.241 10.047 29.583 1.00 20.48 C ANISOU 2907 CA PHE A 385 2548 1496 3736 -86 -214 66 C ATOM 2908 C PHE A 385 20.874 9.208 28.457 1.00 19.78 C ANISOU 2908 C PHE A 385 2029 1884 3599 73 -102 254 C ATOM 2909 O PHE A 385 20.664 9.501 27.272 1.00 19.40 O ANISOU 2909 O PHE A 385 2398 1298 3672 -29 -463 -6 O ATOM 2910 CB PHE A 385 18.829 9.533 29.899 1.00 22.61 C ANISOU 2910 CB PHE A 385 3021 2021 3548 -448 365 97 C ATOM 2911 CG PHE A 385 18.185 10.186 31.097 1.00 26.00 C ANISOU 2911 CG PHE A 385 3764 2471 3642 -74 579 149 C ATOM 2912 CD1 PHE A 385 18.733 10.051 32.374 1.00 29.38 C ANISOU 2912 CD1 PHE A 385 4376 3048 3736 118 306 -548 C ATOM 2913 CD2 PHE A 385 16.999 10.900 30.959 1.00 28.62 C ANISOU 2913 CD2 PHE A 385 4762 2666 3446 876 687 -20 C ATOM 2914 CE1 PHE A 385 18.119 10.634 33.478 1.00 30.77 C ANISOU 2914 CE1 PHE A 385 4260 3481 3948 -107 444 -839 C ATOM 2915 CE2 PHE A 385 16.384 11.495 32.058 1.00 29.76 C ANISOU 2915 CE2 PHE A 385 4473 3239 3593 685 751 -319 C ATOM 2916 CZ PHE A 385 16.942 11.365 33.320 1.00 29.07 C ANISOU 2916 CZ PHE A 385 5160 3201 2684 865 1516 -1637 C ATOM 2917 N PRO A 386 21.658 8.167 28.817 1.00 17.80 N ANISOU 2917 N PRO A 386 2051 1732 2980 33 -69 87 N ATOM 2918 CA PRO A 386 22.338 7.319 27.826 1.00 18.50 C ANISOU 2918 CA PRO A 386 2042 1889 3098 93 64 61 C ATOM 2919 C PRO A 386 21.429 6.670 26.778 1.00 17.84 C ANISOU 2919 C PRO A 386 1675 1846 3255 9 99 206 C ATOM 2920 O PRO A 386 21.825 6.537 25.624 1.00 17.35 O ANISOU 2920 O PRO A 386 1536 1853 3203 -271 -83 242 O ATOM 2921 CB PRO A 386 23.017 6.245 28.688 1.00 18.24 C ANISOU 2921 CB PRO A 386 2275 2057 2598 275 -9 -177 C ATOM 2922 CG PRO A 386 23.241 6.901 29.994 1.00 18.00 C ANISOU 2922 CG PRO A 386 2027 2199 2611 262 -53 -198 C ATOM 2923 CD PRO A 386 22.065 7.817 30.194 1.00 18.51 C ANISOU 2923 CD PRO A 386 2079 2028 2924 258 -58 31 C ATOM 2924 N TRP A 387 20.216 6.292 27.178 1.00 17.11 N ANISOU 2924 N TRP A 387 1928 1796 2774 -201 175 284 N ATOM 2925 CA TRP A 387 19.241 5.704 26.248 1.00 17.29 C ANISOU 2925 CA TRP A 387 2005 1697 2867 -271 206 228 C ATOM 2926 C TRP A 387 18.670 6.690 25.213 1.00 17.85 C ANISOU 2926 C TRP A 387 1916 1782 3084 -69 62 164 C ATOM 2927 O TRP A 387 18.022 6.265 24.255 1.00 18.47 O ANISOU 2927 O TRP A 387 1922 1826 3270 -135 -50 241 O ATOM 2928 CB TRP A 387 18.104 4.980 26.996 1.00 16.31 C ANISOU 2928 CB TRP A 387 1892 1677 2628 -218 205 80 C ATOM 2929 CG TRP A 387 17.386 5.779 28.061 1.00 15.93 C ANISOU 2929 CG TRP A 387 1762 1760 2528 -180 268 213 C ATOM 2930 CD1 TRP A 387 16.249 6.518 27.903 1.00 15.78 C ANISOU 2930 CD1 TRP A 387 1792 1859 2344 -198 149 377 C ATOM 2931 CD2 TRP A 387 17.748 5.888 29.445 1.00 16.19 C ANISOU 2931 CD2 TRP A 387 1931 1694 2523 -35 265 239 C ATOM 2932 NE1 TRP A 387 15.888 7.093 29.098 1.00 17.39 N ANISOU 2932 NE1 TRP A 387 2038 2039 2531 -190 196 178 N ATOM 2933 CE2 TRP A 387 16.788 6.717 30.063 1.00 16.48 C ANISOU 2933 CE2 TRP A 387 1926 1753 2582 -63 255 153 C ATOM 2934 CE3 TRP A 387 18.803 5.372 30.223 1.00 15.66 C ANISOU 2934 CE3 TRP A 387 1936 1649 2363 -72 299 167 C ATOM 2935 CZ2 TRP A 387 16.840 7.041 31.421 1.00 17.24 C ANISOU 2935 CZ2 TRP A 387 2201 1757 2592 27 -7 206 C ATOM 2936 CZ3 TRP A 387 18.860 5.700 31.572 1.00 15.44 C ANISOU 2936 CZ3 TRP A 387 1733 1721 2411 -18 216 108 C ATOM 2937 CH2 TRP A 387 17.876 6.525 32.160 1.00 16.09 C ANISOU 2937 CH2 TRP A 387 2107 1658 2346 173 192 88 C ATOM 2938 N GLU A 388 18.921 7.985 25.405 1.00 16.48 N ANISOU 2938 N GLU A 388 1572 1858 2830 -99 -7 -8 N ATOM 2939 CA GLU A 388 18.535 9.033 24.461 1.00 17.83 C ANISOU 2939 CA GLU A 388 2045 2028 2702 -227 -147 53 C ATOM 2940 C GLU A 388 19.662 9.460 23.510 1.00 19.09 C ANISOU 2940 C GLU A 388 2244 1984 3023 -348 -36 221 C ATOM 2941 O GLU A 388 19.423 10.293 22.619 1.00 17.55 O ANISOU 2941 O GLU A 388 1776 1827 3066 -368 30 192 O ATOM 2942 CB GLU A 388 18.013 10.250 25.238 1.00 18.42 C ANISOU 2942 CB GLU A 388 2096 2076 2827 -173 -70 41 C ATOM 2943 CG GLU A 388 16.759 9.960 26.051 1.00 17.85 C ANISOU 2943 CG GLU A 388 1864 2011 2904 -135 -210 5 C ATOM 2944 CD GLU A 388 15.542 9.692 25.184 1.00 17.77 C ANISOU 2944 CD GLU A 388 1903 1974 2874 -248 -203 102 C ATOM 2945 OE1 GLU A 388 15.422 10.304 24.094 1.00 20.28 O ANISOU 2945 OE1 GLU A 388 2380 2157 3167 -207 128 471 O ATOM 2946 OE2 GLU A 388 14.679 8.869 25.589 1.00 15.93 O ANISOU 2946 OE2 GLU A 388 1293 1787 2969 -5 -256 -80 O ATOM 2947 N VAL A 389 20.868 8.898 23.685 1.00 17.59 N ANISOU 2947 N VAL A 389 2053 1548 3079 -608 100 375 N ATOM 2948 CA VAL A 389 22.000 9.189 22.809 1.00 18.48 C ANISOU 2948 CA VAL A 389 2086 1951 2985 -69 308 168 C ATOM 2949 C VAL A 389 22.091 8.057 21.792 1.00 18.80 C ANISOU 2949 C VAL A 389 2025 1832 3284 -376 250 105 C ATOM 2950 O VAL A 389 22.398 6.931 22.176 1.00 18.42 O ANISOU 2950 O VAL A 389 1562 2091 3344 148 337 54 O ATOM 2951 CB VAL A 389 23.318 9.318 23.595 1.00 17.99 C ANISOU 2951 CB VAL A 389 2542 1420 2871 -8 -76 666 C ATOM 2952 CG1 VAL A 389 24.461 9.714 22.666 1.00 19.95 C ANISOU 2952 CG1 VAL A 389 2704 2191 2682 -227 -40 409 C ATOM 2953 CG2 VAL A 389 23.172 10.346 24.712 1.00 20.48 C ANISOU 2953 CG2 VAL A 389 2419 2364 2995 57 -6 245 C ATOM 2954 N PRO A 390 21.819 8.344 20.496 1.00 20.20 N ANISOU 2954 N PRO A 390 2219 2213 3242 -445 225 -39 N ATOM 2955 CA PRO A 390 21.809 7.270 19.493 1.00 18.69 C ANISOU 2955 CA PRO A 390 1395 2134 3573 -1205 271 -162 C ATOM 2956 C PRO A 390 23.124 6.498 19.381 1.00 19.90 C ANISOU 2956 C PRO A 390 1850 2389 3319 -744 346 -205 C ATOM 2957 O PRO A 390 24.201 7.083 19.532 1.00 21.27 O ANISOU 2957 O PRO A 390 2545 2091 3443 -1396 721 -312 O ATOM 2958 CB PRO A 390 21.531 8.009 18.178 1.00 22.53 C ANISOU 2958 CB PRO A 390 2163 2815 3579 -203 -11 -227 C ATOM 2959 CG PRO A 390 20.870 9.268 18.569 1.00 23.72 C ANISOU 2959 CG PRO A 390 2868 2866 3277 -21 -53 -179 C ATOM 2960 CD PRO A 390 21.439 9.642 19.901 1.00 22.25 C ANISOU 2960 CD PRO A 390 2806 2532 3114 -116 34 25 C ATOM 2961 N LYS A 391 23.022 5.194 19.143 1.00 20.53 N ANISOU 2961 N LYS A 391 2425 2346 3030 -166 227 -283 N ATOM 2962 CA LYS A 391 24.189 4.389 18.775 1.00 19.81 C ANISOU 2962 CA LYS A 391 2369 2479 2677 -192 187 -354 C ATOM 2963 C LYS A 391 24.388 4.491 17.264 1.00 19.55 C ANISOU 2963 C LYS A 391 1771 3007 2646 -340 -17 -223 C ATOM 2964 O LYS A 391 23.431 4.354 16.496 1.00 19.95 O ANISOU 2964 O LYS A 391 1571 2912 3095 -140 -162 -219 O ATOM 2965 CB LYS A 391 24.002 2.921 19.184 1.00 23.40 C ANISOU 2965 CB LYS A 391 3225 2542 3121 -419 32 -239 C ATOM 2966 CG LYS A 391 25.112 1.993 18.708 1.00 25.10 C ANISOU 2966 CG LYS A 391 3486 2706 3343 -393 190 -481 C ATOM 2967 CD LYS A 391 24.942 0.561 19.198 1.00 30.67 C ANISOU 2967 CD LYS A 391 4388 2936 4330 -317 19 -40 C ATOM 2968 CE LYS A 391 25.727 0.290 20.467 1.00 37.22 C ANISOU 2968 CE LYS A 391 5398 4112 4630 -123 -311 307 C ATOM 2969 NZ LYS A 391 25.730 -1.160 20.797 1.00 44.17 N ANISOU 2969 NZ LYS A 391 6258 4092 6430 306 -323 290 N ATOM 2970 N LYS A 392 25.631 4.713 16.841 1.00 23.10 N ANISOU 2970 N LYS A 392 2090 3496 3188 -691 347 -125 N ATOM 2971 CA LYS A 392 25.977 4.684 15.414 1.00 24.28 C ANISOU 2971 CA LYS A 392 2813 3289 3122 -812 235 14 C ATOM 2972 C LYS A 392 25.940 3.230 14.925 1.00 25.08 C ANISOU 2972 C LYS A 392 2736 3471 3319 -437 127 -320 C ATOM 2973 O LYS A 392 26.580 2.353 15.509 1.00 25.82 O ANISOU 2973 O LYS A 392 2416 3387 4004 -307 -7 -619 O ATOM 2974 CB LYS A 392 27.332 5.363 15.157 0.75 27.59 C ANISOU 2974 CB LYS A 392 2516 4096 3870 -759 176 -79 C ATOM 2975 CG LYS A 392 27.231 6.879 15.258 0.50 28.39 C ANISOU 2975 CG LYS A 392 2977 4102 3706 -830 -40 52 C ATOM 2976 CD LYS A 392 28.578 7.582 15.287 0.25 30.31 C ANISOU 2976 CD LYS A 392 2281 5128 4105 -393 -471 278 C ATOM 2977 CE LYS A 392 28.422 8.994 15.837 0.25 30.48 C ANISOU 2977 CE LYS A 392 1655 5393 4533 952 -1626 309 C ATOM 2978 NZ LYS A 392 29.551 9.895 15.477 0.25 33.27 N ANISOU 2978 NZ LYS A 392 1840 5939 4860 465 -1532 -48 N ATOM 2979 N LEU A 393 25.145 2.981 13.887 1.00 23.36 N ANISOU 2979 N LEU A 393 2628 3121 3124 -100 42 186 N ATOM 2980 CA LEU A 393 24.836 1.620 13.432 1.00 21.46 C ANISOU 2980 CA LEU A 393 2229 2983 2941 -16 96 343 C ATOM 2981 C LEU A 393 25.722 1.195 12.262 1.00 22.33 C ANISOU 2981 C LEU A 393 2919 2896 2667 -194 450 767 C ATOM 2982 O LEU A 393 25.908 1.963 11.323 1.00 24.34 O ANISOU 2982 O LEU A 393 3314 3007 2925 -369 928 852 O ATOM 2983 CB LEU A 393 23.362 1.540 13.017 1.00 21.38 C ANISOU 2983 CB LEU A 393 2289 2905 2928 -27 19 123 C ATOM 2984 CG LEU A 393 22.355 1.890 14.110 1.00 21.87 C ANISOU 2984 CG LEU A 393 2490 2889 2928 129 36 54 C ATOM 2985 CD1 LEU A 393 20.948 1.810 13.541 1.00 24.03 C ANISOU 2985 CD1 LEU A 393 2547 3329 3252 265 -44 -123 C ATOM 2986 CD2 LEU A 393 22.489 0.969 15.319 1.00 22.47 C ANISOU 2986 CD2 LEU A 393 2355 3003 3178 197 198 256 C ATOM 2987 N LYS A 394 26.270 -0.020 12.339 1.00 23.70 N ANISOU 2987 N LYS A 394 2715 3188 3099 100 461 420 N ATOM 2988 CA LYS A 394 27.033 -0.630 11.243 0.90 27.94 C ANISOU 2988 CA LYS A 394 3653 3499 3462 96 768 98 C ATOM 2989 C LYS A 394 26.156 -1.599 10.449 1.00 29.28 C ANISOU 2989 C LYS A 394 4094 3225 3802 -32 821 34 C ATOM 2990 O LYS A 394 25.515 -2.482 11.030 1.00 29.84 O ANISOU 2990 O LYS A 394 4591 3134 3611 -139 1134 -189 O ATOM 2991 CB LYS A 394 28.260 -1.381 11.776 0.90 33.74 C ANISOU 2991 CB LYS A 394 4156 4080 4581 397 403 445 C ATOM 2992 CG LYS A 394 29.458 -0.495 12.087 0.80 40.97 C ANISOU 2992 CG LYS A 394 4935 5247 5384 -298 51 273 C ATOM 2993 CD LYS A 394 30.748 -1.298 12.226 0.40 45.39 C ANISOU 2993 CD LYS A 394 5414 5965 5864 263 119 149 C ATOM 2994 CE LYS A 394 30.802 -2.115 13.510 0.40 48.37 C ANISOU 2994 CE LYS A 394 6074 6431 5873 38 8 257 C ATOM 2995 NZ LYS A 394 30.986 -1.267 14.720 0.40 50.53 N ANISOU 2995 NZ LYS A 394 6106 6819 6272 -52 81 -164 N ATOM 2996 N TYR A 395 26.133 -1.424 9.127 1.00 31.69 N ANISOU 2996 N TYR A 395 4588 3721 3732 -159 621 -332 N ATOM 2997 CA TYR A 395 25.379 -2.307 8.221 1.00 32.53 C ANISOU 2997 CA TYR A 395 4795 4109 3457 -446 821 -422 C ATOM 2998 C TYR A 395 25.763 -2.059 6.767 1.00 36.20 C ANISOU 2998 C TYR A 395 4872 5121 3761 -1152 1109 -17 C ATOM 2999 O TYR A 395 26.525 -1.142 6.449 1.00 33.80 O ANISOU 2999 O TYR A 395 4505 5135 3202 -927 1309 -76 O ATOM 3000 CB TYR A 395 23.864 -2.121 8.391 1.00 36.96 C ANISOU 3000 CB TYR A 395 4657 4938 4446 -787 578 -106 C ATOM 3001 CG TYR A 395 23.399 -0.699 8.213 1.00 36.21 C ANISOU 3001 CG TYR A 395 4402 5020 4335 -845 790 71 C ATOM 3002 CD1 TYR A 395 23.438 0.202 9.274 1.00 36.51 C ANISOU 3002 CD1 TYR A 395 4730 5023 4116 -847 910 197 C ATOM 3003 CD2 TYR A 395 22.930 -0.245 6.980 1.00 35.99 C ANISOU 3003 CD2 TYR A 395 3908 5214 4553 -1211 496 52 C ATOM 3004 CE1 TYR A 395 23.021 1.512 9.119 1.00 37.78 C ANISOU 3004 CE1 TYR A 395 4508 5198 4648 -440 951 -67 C ATOM 3005 CE2 TYR A 395 22.510 1.066 6.813 1.00 38.81 C ANISOU 3005 CE2 TYR A 395 4507 5368 4870 -706 579 -247 C ATOM 3006 CZ TYR A 395 22.561 1.940 7.887 1.00 38.46 C ANISOU 3006 CZ TYR A 395 4485 5595 4530 -283 1018 -193 C ATOM 3007 OH TYR A 395 22.150 3.239 7.737 1.00 40.56 O ANISOU 3007 OH TYR A 395 4566 5912 4933 104 921 216 O ATOM 3008 OXT TYR A 395 25.303 -2.774 5.875 1.00 39.05 O ANISOU 3008 OXT TYR A 395 5078 5852 3904 -2041 1081 104 O TER 3009 TYR A 395 HETATM 3010 C1 MPD A 400 -2.265 3.265 14.065 1.00 23.32 C ANISOU 3010 C1 MPD A 400 2810 2972 3076 -105 -4 48 C HETATM 3011 C2 MPD A 400 -1.225 3.902 14.972 1.00 22.74 C ANISOU 3011 C2 MPD A 400 2990 2796 2854 57 -31 -26 C HETATM 3012 O2 MPD A 400 -1.154 5.276 14.586 1.00 31.01 O ANISOU 3012 O2 MPD A 400 4473 2934 4375 -350 -198 258 O HETATM 3013 CM MPD A 400 0.055 3.152 14.675 1.00 21.92 C ANISOU 3013 CM MPD A 400 2749 2856 2721 -36 75 155 C HETATM 3014 C3 MPD A 400 -1.604 3.853 16.471 1.00 23.58 C ANISOU 3014 C3 MPD A 400 2960 3028 2971 37 126 106 C HETATM 3015 C4 MPD A 400 -0.558 3.380 17.522 1.00 22.83 C ANISOU 3015 C4 MPD A 400 2867 2883 2924 -144 90 84 C HETATM 3016 O4 MPD A 400 0.792 3.987 17.501 1.00 20.57 O ANISOU 3016 O4 MPD A 400 2893 2383 2537 -243 -413 -46 O HETATM 3017 C5 MPD A 400 -1.144 3.529 18.934 1.00 21.94 C ANISOU 3017 C5 MPD A 400 2632 2720 2983 12 104 -152 C HETATM 3018 C1 MPD A 401 10.570 17.503 29.753 1.00 24.23 C ANISOU 3018 C1 MPD A 401 2966 3144 3095 132 70 -88 C HETATM 3019 C2 MPD A 401 10.133 18.732 30.519 1.00 23.17 C ANISOU 3019 C2 MPD A 401 2870 2987 2945 -10 26 -15 C HETATM 3020 O2 MPD A 401 8.704 18.739 30.469 1.00 29.29 O ANISOU 3020 O2 MPD A 401 2786 4152 4190 -98 -80 -76 O HETATM 3021 CM MPD A 401 10.628 19.940 29.749 1.00 23.75 C ANISOU 3021 CM MPD A 401 2909 3003 3112 -93 -58 61 C HETATM 3022 C3 MPD A 401 10.555 18.606 32.002 1.00 24.14 C ANISOU 3022 C3 MPD A 401 3031 3085 3055 -91 -97 6 C HETATM 3023 C4 MPD A 401 11.595 19.578 32.568 1.00 23.87 C ANISOU 3023 C4 MPD A 401 2984 3053 3030 -57 25 -112 C HETATM 3024 O4 MPD A 401 11.703 19.398 33.990 1.00 32.63 O ANISOU 3024 O4 MPD A 401 4835 4283 3280 -162 18 622 O HETATM 3025 C5 MPD A 401 13.003 19.368 32.032 1.00 24.70 C ANISOU 3025 C5 MPD A 401 3102 3161 3122 106 110 -19 C HETATM 3026 O1G PPK A 402 -4.833 5.793 36.054 1.00 29.58 O ANISOU 3026 O1G PPK A 402 4379 2951 3909 200 -498 -67 O HETATM 3027 PG PPK A 402 -5.248 5.153 37.339 1.00 29.89 P ANISOU 3027 PG PPK A 402 3220 3683 4451 132 -440 347 P HETATM 3028 O2G PPK A 402 -4.143 5.368 38.493 1.00 25.53 O ANISOU 3028 O2G PPK A 402 3274 2824 3600 663 -204 758 O HETATM 3029 O3G PPK A 402 -5.510 3.593 37.125 1.00 32.11 O ANISOU 3029 O3G PPK A 402 4531 3392 4275 622 -574 638 O HETATM 3030 N3B PPK A 402 -6.759 5.949 37.684 1.00 27.34 N ANISOU 3030 N3B PPK A 402 3034 2833 4521 -327 -368 -287 N HETATM 3031 PB PPK A 402 -7.045 6.818 39.149 1.00 25.27 P ANISOU 3031 PB PPK A 402 3212 2826 3560 -620 -244 520 P HETATM 3032 O1B PPK A 402 -6.149 6.377 40.244 1.00 20.84 O ANISOU 3032 O1B PPK A 402 2943 2217 2756 -369 282 227 O HETATM 3033 O2B PPK A 402 -8.560 6.541 39.612 1.00 26.86 O ANISOU 3033 O2B PPK A 402 3720 2253 4232 -282 639 433 O HETATM 3034 O3A PPK A 402 -6.778 8.383 38.742 1.00 25.89 O ANISOU 3034 O3A PPK A 402 2668 2865 4302 -604 322 590 O HETATM 3035 PA PPK A 402 -5.348 8.954 38.163 1.00 21.34 P ANISOU 3035 PA PPK A 402 1956 2925 3225 -27 77 165 P HETATM 3036 O1A PPK A 402 -5.325 10.402 38.465 1.00 23.86 O ANISOU 3036 O1A PPK A 402 2249 2814 3999 -216 -1 390 O HETATM 3037 O2A PPK A 402 -4.305 8.207 38.939 1.00 24.81 O ANISOU 3037 O2A PPK A 402 2079 3115 4231 -85 -301 229 O HETATM 3038 O4A PPK A 402 -5.309 8.702 36.675 1.00 21.50 O ANISOU 3038 O4A PPK A 402 2127 2815 3224 259 601 707 O HETATM 3039 N1 IMD A 403 -2.303 5.577 10.316 1.00 26.56 N ANISOU 3039 N1 IMD A 403 3162 3033 3896 -239 83 -140 N HETATM 3040 C2 IMD A 403 -3.448 5.036 9.841 1.00 26.99 C ANISOU 3040 C2 IMD A 403 3336 2870 4046 -372 -7 -35 C HETATM 3041 N3 IMD A 403 -4.484 5.795 10.264 1.00 27.27 N ANISOU 3041 N3 IMD A 403 3170 3130 4058 -371 -23 -161 N HETATM 3042 C4 IMD A 403 -3.999 6.809 11.003 1.00 26.09 C ANISOU 3042 C4 IMD A 403 3114 2917 3878 -242 -62 -12 C HETATM 3043 C5 IMD A 403 -2.627 6.674 11.039 1.00 25.45 C ANISOU 3043 C5 IMD A 403 3076 2665 3927 -514 96 14 C HETATM 3044 C1 S7M A 404 -10.218 12.544 40.588 1.00 30.42 C ANISOU 3044 C1 S7M A 404 3284 3759 4514 156 -633 866 C HETATM 3045 S2 S7M A 404 -9.102 11.413 41.081 1.00 23.84 S ANISOU 3045 S2 S7M A 404 1905 3330 3820 -420 -395 702 S HETATM 3046 C3 S7M A 404 -9.627 9.826 40.813 1.00 30.36 C ANISOU 3046 C3 S7M A 404 3609 3494 4431 -743 -231 524 C HETATM 3047 C4 S7M A 404 -11.005 9.425 41.343 1.00 28.65 C ANISOU 3047 C4 S7M A 404 3440 3110 4336 -319 -55 409 C HETATM 3048 C5 S7M A 404 -11.041 9.354 42.870 1.00 24.75 C ANISOU 3048 C5 S7M A 404 2748 2382 4272 -144 102 584 C HETATM 3049 C6 S7M A 404 -12.445 9.188 43.397 1.00 21.82 C ANISOU 3049 C6 S7M A 404 2098 2416 3775 -97 -767 714 C HETATM 3050 O7 S7M A 404 -12.569 8.738 44.559 1.00 21.32 O ANISOU 3050 O7 S7M A 404 2269 1971 3859 -279 -651 694 O HETATM 3051 O8 S7M A 404 -13.433 9.510 42.698 1.00 20.38 O ANISOU 3051 O8 S7M A 404 1778 2422 3541 162 -386 678 O HETATM 3052 N9 S7M A 404 -10.190 8.240 43.342 1.00 23.96 N ANISOU 3052 N9 S7M A 404 2421 2640 4042 -1 73 286 N HETATM 3053 C10 S7M A 404 -7.675 11.314 40.211 1.00 21.50 C ANISOU 3053 C10 S7M A 404 2248 2681 3238 45 -319 234 C HETATM 3054 C11 S7M A 404 -6.790 12.543 40.157 1.00 19.62 C ANISOU 3054 C11 S7M A 404 2119 2310 3023 362 -250 37 C HETATM 3055 C12 S7M A 404 -6.145 12.951 41.471 1.00 16.39 C ANISOU 3055 C12 S7M A 404 1480 1791 2955 673 -174 83 C HETATM 3056 C13 S7M A 404 -5.856 14.399 41.144 1.00 16.91 C ANISOU 3056 C13 S7M A 404 1931 1874 2620 429 141 -24 C HETATM 3057 C14 S7M A 404 -7.054 14.812 40.308 1.00 18.25 C ANISOU 3057 C14 S7M A 404 2229 2001 2703 343 -114 68 C HETATM 3058 O15 S7M A 404 -7.531 13.650 39.650 1.00 19.67 O ANISOU 3058 O15 S7M A 404 2807 2013 2652 128 -240 272 O HETATM 3059 N16 S7M A 404 -8.102 15.421 41.156 1.00 17.02 N ANISOU 3059 N16 S7M A 404 2169 1927 2369 219 -140 213 N HETATM 3060 C17 S7M A 404 -8.343 15.261 42.475 1.00 15.69 C ANISOU 3060 C17 S7M A 404 2303 1387 2272 960 -617 711 C HETATM 3061 N18 S7M A 404 -9.372 16.036 42.862 1.00 15.32 N ANISOU 3061 N18 S7M A 404 1466 1709 2644 221 -295 140 N HETATM 3062 C19 S7M A 404 -9.804 16.708 41.793 1.00 16.45 C ANISOU 3062 C19 S7M A 404 1878 1880 2491 -34 -303 139 C HETATM 3063 C20 S7M A 404 -8.966 16.296 40.667 1.00 16.68 C ANISOU 3063 C20 S7M A 404 1674 2009 2653 33 -276 149 C HETATM 3064 N21 S7M A 404 -9.177 16.828 39.439 1.00 15.44 N ANISOU 3064 N21 S7M A 404 1370 1844 2650 75 -362 84 N HETATM 3065 C22 S7M A 404 -10.160 17.728 39.260 1.00 18.46 C ANISOU 3065 C22 S7M A 404 1942 2106 2966 452 -408 251 C HETATM 3066 N23 S7M A 404 -10.973 18.155 40.254 1.00 17.71 N ANISOU 3066 N23 S7M A 404 2040 1832 2854 -22 -327 7 N HETATM 3067 C24 S7M A 404 -10.868 17.698 41.521 1.00 18.59 C ANISOU 3067 C24 S7M A 404 2008 2165 2890 152 -411 38 C HETATM 3068 N25 S7M A 404 -11.688 18.114 42.518 1.00 20.99 N ANISOU 3068 N25 S7M A 404 2852 2142 2980 210 -81 -96 N HETATM 3069 O26 S7M A 404 -4.674 14.537 40.354 1.00 15.54 O ANISOU 3069 O26 S7M A 404 1681 1649 2575 190 -36 34 O HETATM 3070 O27 S7M A 404 -4.956 12.205 41.788 1.00 16.58 O ANISOU 3070 O27 S7M A 404 715 2346 3235 492 96 -269 O HETATM 3071 C28 S7M A 404 -10.345 12.581 39.102 1.00 36.39 C ANISOU 3071 C28 S7M A 404 4528 4779 4518 -515 -400 377 C HETATM 3072 K K A 405 -6.339 6.127 42.951 1.00 32.27 K ANISOU 3072 K K A 405 4139 4607 3514 1145 -386 -1366 K HETATM 3073 MG MG A 406 -4.079 6.556 40.111 1.00 18.57 MG ANISOU 3073 MG MG A 406 1487 2684 2884 226 420 -58 MG HETATM 3074 MG MG A 407 -6.008 7.551 35.172 0.90 26.89 MG ANISOU 3074 MG MG A 407 2974 3892 3350 1336 -468 -1926 MG HETATM 3075 O HOH A2001 -9.238 9.366 9.352 1.00 40.26 O ANISOU 3075 O HOH A2001 7724 3568 4002 -2943 1113 -799 O HETATM 3076 O HOH A2002 -9.424 14.817 12.430 1.00 14.41 O ANISOU 3076 O HOH A2002 1118 1702 2652 51 -186 236 O HETATM 3077 O HOH A2003 -10.016 10.787 14.977 1.00 18.06 O ANISOU 3077 O HOH A2003 2299 1598 2963 -162 -381 20 O HETATM 3078 O HOH A2004 -11.315 12.716 13.518 1.00 22.24 O ANISOU 3078 O HOH A2004 2047 2097 4303 -295 -614 185 O HETATM 3079 O HOH A2005 -0.532 9.608 28.612 1.00 16.27 O ANISOU 3079 O HOH A2005 1795 1620 2764 260 -285 160 O HETATM 3080 O HOH A2006 -6.286 9.864 33.883 1.00 18.91 O ANISOU 3080 O HOH A2006 2213 2243 2726 93 -76 3 O HETATM 3081 O HOH A2007 -1.789 7.887 30.490 1.00 14.80 O ANISOU 3081 O HOH A2007 456 1952 3213 381 -34 35 O HETATM 3082 O HOH A2008 -3.809 7.936 34.301 0.90 24.58 O ANISOU 3082 O HOH A2008 2902 2936 3498 -167 -958 184 O HETATM 3083 O HOH A2009 4.660 13.236 34.655 1.00 20.48 O ANISOU 3083 O HOH A2009 2436 2137 3207 700 185 2 O HETATM 3084 O HOH A2010 3.924 19.791 40.806 1.00 24.90 O ANISOU 3084 O HOH A2010 3104 2532 3824 -364 64 365 O HETATM 3085 O HOH A2011 4.693 19.112 38.177 1.00 27.81 O ANISOU 3085 O HOH A2011 2681 2458 5425 -1010 -191 402 O HETATM 3086 O HOH A2012 18.890 13.484 47.602 0.50 22.59 O ANISOU 3086 O HOH A2012 1804 1360 5418 -1041 695 -555 O HETATM 3087 O HOH A2013 2.580 5.677 39.661 1.00 15.50 O ANISOU 3087 O HOH A2013 2623 1203 2063 518 -196 -397 O HETATM 3088 O HOH A2014 -3.709 5.104 41.696 1.00 18.42 O ANISOU 3088 O HOH A2014 2408 1750 2838 -264 -471 160 O HETATM 3089 O HOH A2015 -4.064 7.902 41.767 1.00 24.37 O ANISOU 3089 O HOH A2015 3406 2767 3084 320 -104 -573 O HETATM 3090 O HOH A2016 8.130 10.152 34.642 1.00 18.50 O ANISOU 3090 O HOH A2016 2791 1968 2269 404 160 -355 O HETATM 3091 O HOH A2017 8.112 6.616 37.028 1.00 15.83 O ANISOU 3091 O HOH A2017 1586 1912 2515 -20 165 -252 O HETATM 3092 O HOH A2018 4.150 4.778 36.826 1.00 11.88 O ANISOU 3092 O HOH A2018 802 1566 2144 -110 -54 -133 O HETATM 3093 O HOH A2019 6.844 3.358 37.803 1.00 16.06 O ANISOU 3093 O HOH A2019 1726 1483 2890 510 11 -111 O HETATM 3094 O HOH A2020 17.901 9.529 47.115 1.00 24.76 O ANISOU 3094 O HOH A2020 1769 2929 4707 225 -398 -842 O HETATM 3095 O HOH A2021 14.204 -2.821 56.151 0.50 28.96 O ANISOU 3095 O HOH A2021 2625 3058 5317 -949 -611 561 O HETATM 3096 O HOH A2022 22.335 -9.637 46.389 0.50 22.81 O ANISOU 3096 O HOH A2022 1269 4143 3253 1544 -24 -1195 O HETATM 3097 O HOH A2023 18.204 11.097 40.394 1.00 31.56 O ANISOU 3097 O HOH A2023 2246 3508 6234 873 127 -184 O HETATM 3098 O HOH A2024 17.786 10.605 44.298 1.00 23.70 O ANISOU 3098 O HOH A2024 1013 3092 4899 -568 -710 -341 O HETATM 3099 O HOH A2025 22.848 6.748 50.558 1.00 22.18 O ANISOU 3099 O HOH A2025 2104 2124 4198 31 -678 -116 O HETATM 3100 O HOH A2026 13.682 20.800 48.435 1.00 38.01 O ANISOU 3100 O HOH A2026 2787 5401 6254 -3187 8 -34 O HETATM 3101 O HOH A2027 26.390 3.377 41.943 1.00 31.27 O ANISOU 3101 O HOH A2027 3006 3428 5444 150 -502 -869 O HETATM 3102 O HOH A2028 21.505 10.666 43.352 1.00 36.33 O ANISOU 3102 O HOH A2028 4959 3782 5060 -938 -489 211 O HETATM 3103 O HOH A2029 5.566 24.993 60.436 1.00 25.17 O ANISOU 3103 O HOH A2029 3636 2298 3629 63 -573 441 O HETATM 3104 O HOH A2030 1.912 27.255 53.405 1.00 34.69 O ANISOU 3104 O HOH A2030 7185 1661 4332 563 104 610 O HETATM 3105 O HOH A2031 24.678 -6.259 46.959 1.00 38.57 O ANISOU 3105 O HOH A2031 7574 4041 3038 1237 -720 958 O HETATM 3106 O HOH A2032 22.109 -2.274 41.025 1.00 27.56 O ANISOU 3106 O HOH A2032 2898 3175 4396 714 -950 -1690 O HETATM 3107 O HOH A2033 21.405 -4.951 40.832 1.00 26.45 O ANISOU 3107 O HOH A2033 2883 3360 3806 456 378 618 O HETATM 3108 O HOH A2034 24.825 -8.916 41.388 1.00 38.09 O ANISOU 3108 O HOH A2034 4719 2895 6855 -417 465 706 O HETATM 3109 O HOH A2035 8.250 -5.539 45.141 1.00 21.24 O ANISOU 3109 O HOH A2035 2344 2595 3130 -586 282 -150 O HETATM 3110 O HOH A2036 8.271 -1.091 41.593 1.00 23.24 O ANISOU 3110 O HOH A2036 2995 2187 3648 -92 -402 -477 O HETATM 3111 O HOH A2037 9.063 -3.467 42.569 1.00 26.16 O ANISOU 3111 O HOH A2037 3176 3249 3514 1309 -637 188 O HETATM 3112 O HOH A2038 -4.911 7.544 55.687 1.00 25.13 O ANISOU 3112 O HOH A2038 2399 2591 4557 -498 -930 1476 O HETATM 3113 O HOH A2039 -1.886 14.290 54.594 1.00 16.73 O ANISOU 3113 O HOH A2039 2482 1061 2810 -175 18 46 O HETATM 3114 O HOH A2040 14.720 -7.110 44.818 1.00 16.40 O ANISOU 3114 O HOH A2040 1496 1877 2856 942 161 -66 O HETATM 3115 O HOH A2041 15.340 -4.777 53.646 0.50 28.67 O ANISOU 3115 O HOH A2041 4911 2289 3692 -364 368 -169 O HETATM 3116 O HOH A2042 19.574 -5.706 52.685 1.00 47.12 O ANISOU 3116 O HOH A2042 6491 7764 3648 -5417 194 -574 O HETATM 3117 O HOH A2043 19.647 -10.949 46.869 1.00 22.13 O ANISOU 3117 O HOH A2043 2056 2821 3530 1213 -334 -275 O HETATM 3118 O HOH A2044 18.328 -12.012 49.413 1.00 32.33 O ANISOU 3118 O HOH A2044 3058 3740 5482 237 -374 21 O HETATM 3119 O HOH A2045 20.044 -2.542 53.243 1.00 34.71 O ANISOU 3119 O HOH A2045 4802 4176 4208 990 370 301 O HETATM 3120 O HOH A2046 7.746 25.073 27.761 1.00 30.44 O ANISOU 3120 O HOH A2046 4055 3249 4261 -217 -607 374 O HETATM 3121 O HOH A2047 20.367 7.500 53.451 1.00 33.88 O ANISOU 3121 O HOH A2047 1403 2841 8627 387 -683 -1466 O HETATM 3122 O HOH A2048 16.360 10.936 60.419 0.50 23.73 O ANISOU 3122 O HOH A2048 3230 1620 4166 978 -175 -1091 O HETATM 3123 O HOH A2049 -2.606 35.745 36.619 1.00 34.80 O ANISOU 3123 O HOH A2049 4489 1840 6891 386 535 -279 O HETATM 3124 O HOH A2050 18.281 -0.629 54.611 1.00 53.87 O ANISOU 3124 O HOH A2050 6482 8939 5045 4644 1375 3642 O HETATM 3125 O HOH A2051 7.353 7.911 60.838 1.00 44.50 O ANISOU 3125 O HOH A2051 1590 11278 4039 -1661 40 883 O HETATM 3126 O HOH A2052 15.071 11.964 49.038 1.00 29.40 O ANISOU 3126 O HOH A2052 2524 3375 5268 -437 -102 -1703 O HETATM 3127 O HOH A2053 9.480 5.065 3.158 1.00 45.30 O ANISOU 3127 O HOH A2053 6216 5696 5297 -854 -284 855 O HETATM 3128 O HOH A2054 14.687 14.595 47.178 1.00 22.28 O ANISOU 3128 O HOH A2054 1067 3724 3675 -1104 105 -880 O HETATM 3129 O HOH A2055 14.416 18.149 49.552 1.00 39.59 O ANISOU 3129 O HOH A2055 3651 4172 7218 771 -739 -279 O HETATM 3130 O BHOH A2056 17.412 12.428 51.197 0.50 24.80 O ANISOU 3130 O BHOH A2056 2237 4364 2819 -1132 -174 -1786 O HETATM 3131 O HOH A2057 9.322 22.736 51.183 1.00 52.22 O ANISOU 3131 O HOH A2057 3380 5091 11370 1598 3022 3090 O HETATM 3132 O HOH A2058 8.288 22.667 45.476 1.00 23.16 O ANISOU 3132 O HOH A2058 2637 3071 3088 -201 287 536 O HETATM 3133 O HOH A2059 -6.322 38.847 36.830 1.00 48.79 O ANISOU 3133 O HOH A2059 1742 6516 10278 -568 46 -4790 O HETATM 3134 O HOH A2060 3.942 23.538 58.521 1.00 28.24 O ANISOU 3134 O HOH A2060 1438 3139 6153 45 -21 -507 O HETATM 3135 O HOH A2061 5.908 25.211 55.822 1.00 54.14 O ANISOU 3135 O HOH A2061 8684 7208 4679 -3526 -875 711 O HETATM 3136 O HOH A2062 4.452 26.244 53.087 0.40 17.41 O ANISOU 3136 O HOH A2062 2414 924 3275 680 183 -388 O HETATM 3137 O HOH A2063 1.341 26.139 59.508 1.00 42.71 O ANISOU 3137 O HOH A2063 3697 6311 6219 -2813 -1078 566 O HETATM 3138 O HOH A2064 -5.991 20.762 55.274 1.00 35.73 O ANISOU 3138 O HOH A2064 3626 4806 5144 1250 1269 627 O HETATM 3139 O HOH A2065 -5.921 21.178 50.800 1.00 37.24 O ANISOU 3139 O HOH A2065 6348 3048 4753 -1535 -2715 554 O HETATM 3140 O HOH A2066 2.973 24.328 46.918 1.00 26.24 O ANISOU 3140 O HOH A2066 6227 1526 2214 -1513 490 -159 O HETATM 3141 O HOH A2067 4.209 27.713 50.082 1.00 46.58 O ANISOU 3141 O HOH A2067 7122 3400 7175 -1345 1024 377 O HETATM 3142 O HOH A2068 -6.138 31.452 18.762 1.00 59.95 O ANISOU 3142 O HOH A2068 6659 5520 10599 -3946 3340 -2819 O HETATM 3143 O HOH A2069 -2.193 31.958 20.738 1.00 29.18 O ANISOU 3143 O HOH A2069 2893 3013 5179 -354 591 1151 O HETATM 3144 O HOH A2070 0.092 30.144 12.026 1.00 49.57 O ANISOU 3144 O HOH A2070 7037 5865 5929 1000 -957 2673 O HETATM 3145 O HOH A2071 -2.895 15.264 50.314 1.00 19.26 O ANISOU 3145 O HOH A2071 2157 1656 3503 620 -486 -533 O HETATM 3146 O HOH A2072 -4.954 29.054 11.993 1.00 50.13 O ANISOU 3146 O HOH A2072 5398 9009 4639 -2776 -614 1432 O HETATM 3147 O HOH A2073 0.658 14.920 55.964 1.00 21.11 O ANISOU 3147 O HOH A2073 3006 1413 3601 -1092 -184 857 O HETATM 3148 O HOH A2074 8.481 23.464 55.983 1.00 23.26 O ANISOU 3148 O HOH A2074 2378 2280 4180 -1265 -1041 336 O HETATM 3149 O HOH A2075 -16.910 20.599 23.551 0.75 30.24 O ANISOU 3149 O HOH A2075 930 4992 5567 1758 333 889 O HETATM 3150 O HOH A2076 0.145 16.347 58.946 0.50 28.49 O ANISOU 3150 O HOH A2076 2320 4144 4360 812 13 3784 O HETATM 3151 O HOH A2077 -11.181 21.924 51.901 0.80 32.62 O ANISOU 3151 O HOH A2077 3444 3373 5574 316 1251 -685 O HETATM 3152 O HOH A2078 8.985 -13.467 55.497 1.00 42.42 O ANISOU 3152 O HOH A2078 4691 5184 6241 126 96 -2102 O HETATM 3153 O HOH A2079 11.580 -11.252 56.627 0.75 31.48 O ANISOU 3153 O HOH A2079 3909 4698 3352 -811 -157 131 O HETATM 3154 O HOH A2080 9.891 -10.779 51.098 0.75 39.48 O ANISOU 3154 O HOH A2080 5013 1945 8041 510 -2690 -27 O HETATM 3155 O HOH A2081 15.164 -7.500 56.075 1.00 60.30 O ANISOU 3155 O HOH A2081 3844 12809 6258 -2873 673 -4270 O HETATM 3156 O HOH A2082 13.872 -10.175 55.462 1.00 20.95 O ANISOU 3156 O HOH A2082 2626 2820 2513 195 -623 944 O HETATM 3157 O HOH A2083 16.892 -9.037 40.816 1.00 16.39 O ANISOU 3157 O HOH A2083 1364 1880 2983 -456 -199 -96 O HETATM 3158 O HOH A2084 16.806 -20.660 48.139 1.00 39.69 O ANISOU 3158 O HOH A2084 2746 2489 9842 99 -1680 374 O HETATM 3159 O HOH A2085 24.702 -11.772 42.954 1.00 34.67 O ANISOU 3159 O HOH A2085 1754 5694 5722 660 -230 -1148 O HETATM 3160 O HOH A2086 26.243 -12.011 40.239 1.00 40.82 O ANISOU 3160 O HOH A2086 2326 6661 6522 -904 55 -2763 O HETATM 3161 O HOH A2087 28.166 -19.264 36.211 1.00 50.97 O ANISOU 3161 O HOH A2087 6847 6231 6287 2325 2206 -1964 O HETATM 3162 O HOH A2088 30.063 -16.099 39.258 1.00 30.37 O ANISOU 3162 O HOH A2088 3127 2143 6267 -253 -1435 1104 O HETATM 3163 O HOH A2089 30.436 -17.504 42.272 1.00 24.80 O ANISOU 3163 O HOH A2089 2356 3092 3973 958 -342 319 O HETATM 3164 O HOH A2090 27.081 -14.369 43.660 1.00 42.55 O ANISOU 3164 O HOH A2090 3903 5887 6375 779 -267 1375 O HETATM 3165 O HOH A2091 24.882 -18.055 33.714 1.00 42.72 O ANISOU 3165 O HOH A2091 4320 4612 7299 -665 1515 164 O HETATM 3166 O HOH A2092 20.927 -17.939 30.340 1.00 17.07 O ANISOU 3166 O HOH A2092 673 2096 3715 161 183 476 O HETATM 3167 O HOH A2093 23.595 -17.459 31.282 1.00 37.46 O ANISOU 3167 O HOH A2093 5729 3736 4767 -1853 1098 868 O HETATM 3168 O HOH A2094 27.555 -17.086 34.537 1.00 32.50 O ANISOU 3168 O HOH A2094 3493 6448 2405 2900 495 239 O HETATM 3169 O HOH A2095 30.593 -9.929 33.356 1.00 40.87 O ANISOU 3169 O HOH A2095 2831 2909 9788 -645 569 -976 O HETATM 3170 O HOH A2096 31.090 -10.464 37.126 1.00 44.23 O ANISOU 3170 O HOH A2096 4047 4822 7934 -374 -929 281 O HETATM 3171 O HOH A2097 32.293 -12.138 30.105 0.75 47.37 O ANISOU 3171 O HOH A2097 1921 7602 8474 201 2378 -2660 O HETATM 3172 O HOH A2098 18.854 -18.372 25.690 1.00 30.98 O ANISOU 3172 O HOH A2098 1682 4197 5891 805 -470 -482 O HETATM 3173 O HOH A2099 22.810 -10.578 31.306 1.00 16.98 O ANISOU 3173 O HOH A2099 1123 2130 3195 -9 178 233 O HETATM 3174 O HOH A2100 29.687 -13.160 28.667 1.00 32.69 O ANISOU 3174 O HOH A2100 4265 3842 4311 -1060 622 558 O HETATM 3175 O HOH A2101 15.910 -13.807 19.486 1.00 56.82 O ANISOU 3175 O HOH A2101 6267 8703 6619 143 187 -212 O HETATM 3176 O HOH A2102 27.611 -15.821 27.241 1.00 23.34 O ANISOU 3176 O HOH A2102 3328 1647 3890 1048 694 4 O HETATM 3177 O HOH A2103 24.457 -15.311 28.763 1.00 38.57 O ANISOU 3177 O HOH A2103 3766 4264 6625 1631 178 -2171 O HETATM 3178 O HOH A2104 2.069 -1.657 10.206 0.50 40.69 O ANISOU 3178 O HOH A2104 534 2139 12786 -281 -131 -1361 O HETATM 3179 O HOH A2105 6.313 -1.503 3.995 1.00 46.93 O ANISOU 3179 O HOH A2105 5160 6339 6333 565 -513 -1679 O HETATM 3180 O HOH A2106 14.485 -10.077 40.116 1.00 20.21 O ANISOU 3180 O HOH A2106 2808 2030 2841 -685 309 -395 O HETATM 3181 O HOH A2107 12.196 -11.731 10.882 1.00 30.10 O ANISOU 3181 O HOH A2107 2195 4883 4357 -313 -194 166 O HETATM 3182 O HOH A2108 9.924 -8.125 33.507 1.00 18.00 O ANISOU 3182 O HOH A2108 1411 2174 3252 -862 -432 47 O HETATM 3183 O HOH A2109 5.585 -7.686 30.801 1.00 15.95 O ANISOU 3183 O HOH A2109 653 1585 3820 343 790 -231 O HETATM 3184 O HOH A2110 7.030 -4.304 30.641 1.00 39.60 O ANISOU 3184 O HOH A2110 2003 5433 7610 -1327 1633 -4168 O HETATM 3185 O HOH A2111 6.900 -1.686 27.699 1.00 13.85 O ANISOU 3185 O HOH A2111 1359 1526 2377 443 392 61 O HETATM 3186 O HOH A2112 10.700 1.993 25.907 1.00 15.84 O ANISOU 3186 O HOH A2112 1147 1903 2965 -445 257 -223 O HETATM 3187 O HOH A2113 6.697 0.908 26.490 1.00 25.83 O ANISOU 3187 O HOH A2113 3270 2561 3984 -396 1362 -206 O HETATM 3188 O HOH A2114 3.866 9.318 17.492 1.00 19.75 O ANISOU 3188 O HOH A2114 2471 1869 3161 -214 61 267 O HETATM 3189 O HOH A2115 27.373 1.970 23.584 1.00 29.66 O ANISOU 3189 O HOH A2115 1837 2748 6682 701 633 322 O HETATM 3190 O HOH A2116 29.654 6.311 28.004 1.00 53.07 O ANISOU 3190 O HOH A2116 3789 6670 9703 -94 953 1852 O HETATM 3191 O HOH A2117 23.501 8.306 33.390 1.00 39.98 O ANISOU 3191 O HOH A2117 5979 5660 3550 -1680 530 -985 O HETATM 3192 O HOH A2118 28.404 -1.080 34.934 1.00 31.32 O ANISOU 3192 O HOH A2118 2891 5431 3577 -1382 305 238 O HETATM 3193 O HOH A2119 6.371 10.092 12.442 1.00 19.03 O ANISOU 3193 O HOH A2119 2730 2054 2445 401 -354 31 O HETATM 3194 O HOH A2120 6.815 13.219 10.777 1.00 30.16 O ANISOU 3194 O HOH A2120 3728 2060 5672 -453 -837 126 O HETATM 3195 O HOH A2121 12.953 11.800 9.457 1.00 39.65 O ANISOU 3195 O HOH A2121 6581 3949 4532 -1763 411 537 O HETATM 3196 O HOH A2122 10.741 19.523 17.629 1.00 22.26 O ANISOU 3196 O HOH A2122 1428 1153 5876 279 -35 -183 O HETATM 3197 O HOH A2123 19.535 17.274 16.503 1.00 28.43 O ANISOU 3197 O HOH A2123 3880 3141 3779 -1275 -344 962 O HETATM 3198 O HOH A2124 27.079 3.946 21.457 1.00 30.99 O ANISOU 3198 O HOH A2124 1524 5998 4251 1593 -288 -765 O HETATM 3199 O HOH A2125 7.105 10.157 28.489 1.00 29.07 O ANISOU 3199 O HOH A2125 6505 988 3551 -740 -671 -263 O HETATM 3200 O HOH A2126 7.156 23.950 30.615 1.00 24.08 O ANISOU 3200 O HOH A2126 3222 2473 3454 211 678 -514 O HETATM 3201 O HOH A2127 2.445 20.664 38.147 1.00 20.17 O ANISOU 3201 O HOH A2127 2668 1653 3341 394 -183 292 O HETATM 3202 O HOH A2128 9.554 22.775 36.209 1.00 43.36 O ANISOU 3202 O HOH A2128 5287 6209 4978 490 1647 -1251 O HETATM 3203 O HOH A2129 8.873 24.959 32.660 1.00 34.10 O ANISOU 3203 O HOH A2129 4145 3196 5612 -138 -128 203 O HETATM 3204 O HOH A2130 8.024 28.177 28.275 1.00 36.28 O ANISOU 3204 O HOH A2130 1881 6438 5465 428 1075 702 O HETATM 3205 O HOH A2131 10.585 29.604 31.494 1.00 26.66 O ANISOU 3205 O HOH A2131 3042 2975 4111 -146 399 -168 O HETATM 3206 O HOH A2132 10.556 28.289 39.089 1.00 31.68 O ANISOU 3206 O HOH A2132 4500 2237 5300 -474 590 196 O HETATM 3207 O HOH A2133 11.441 30.533 36.893 1.00 41.37 O ANISOU 3207 O HOH A2133 3534 4207 7976 -1761 832 865 O HETATM 3208 O HOH A2134 4.356 30.263 45.583 0.40 28.65 O ANISOU 3208 O HOH A2134 339 7067 3478 -90 -367 1160 O HETATM 3209 O HOH A2135 6.359 28.211 46.540 1.00 50.82 O ANISOU 3209 O HOH A2135 8554 5767 4986 -89 1924 201 O HETATM 3210 O HOH A2136 1.964 22.755 40.407 1.00 19.16 O ANISOU 3210 O HOH A2136 2207 2119 2952 -361 162 10 O HETATM 3211 O HOH A2137 5.779 25.205 46.386 1.00 38.05 O ANISOU 3211 O HOH A2137 8324 3769 2363 2101 -1734 -220 O HETATM 3212 O HOH A2138 10.286 23.652 38.643 1.00 34.31 O ANISOU 3212 O HOH A2138 3749 3647 5638 -701 -50 1203 O HETATM 3213 O HOH A2139 6.965 33.824 35.450 0.50 19.18 O ANISOU 3213 O HOH A2139 2067 3075 2143 1864 368 -903 O HETATM 3214 O HOH A2140 4.334 35.349 45.180 1.00 43.10 O ANISOU 3214 O HOH A2140 6058 4786 5529 -2202 1101 -2181 O HETATM 3215 O HOH A2141 -1.586 30.129 48.407 0.50 25.86 O ANISOU 3215 O HOH A2141 3048 2406 4371 -300 -741 -1381 O HETATM 3216 O HOH A2142 2.314 27.882 46.019 1.00 44.20 O ANISOU 3216 O HOH A2142 5530 5150 6111 1155 -1104 -2064 O HETATM 3217 O HOH A2143 -3.347 34.669 39.376 1.00 28.58 O ANISOU 3217 O HOH A2143 2126 2931 5803 -980 -1853 2052 O HETATM 3218 O HOH A2144 -5.875 14.212 44.595 1.00 15.05 O ANISOU 3218 O HOH A2144 2124 1318 2274 600 -473 42 O HETATM 3219 O HOH A2145 -7.529 16.408 25.581 1.00 20.76 O ANISOU 3219 O HOH A2145 3381 1734 2772 532 292 -135 O HETATM 3220 O HOH A2146 -8.868 19.282 14.240 1.00 35.70 O ANISOU 3220 O HOH A2146 5098 3894 4573 959 -225 167 O HETATM 3221 O HOH A2147 -10.758 17.238 13.684 1.00 36.42 O ANISOU 3221 O HOH A2147 6206 3459 4172 1428 -660 -180 O HETATM 3222 O HOH A2148 -7.455 7.063 7.207 1.00 47.98 O ANISOU 3222 O HOH A2148 7318 5821 5091 -2295 699 -1293 O HETATM 3223 O HOH A2149 -6.686 8.449 9.742 1.00 46.98 O ANISOU 3223 O HOH A2149 6882 5576 5390 723 374 -1587 O HETATM 3224 O HOH A2150 -0.029 6.619 6.426 1.00 23.74 O ANISOU 3224 O HOH A2150 1961 2548 4509 354 -771 -446 O HETATM 3225 O HOH A2151 -0.014 8.848 3.276 1.00 39.95 O ANISOU 3225 O HOH A2151 4937 6334 3906 759 -1521 -769 O HETATM 3226 O HOH A2152 7.556 6.944 4.986 1.00 39.57 O ANISOU 3226 O HOH A2152 5661 5435 3936 -1781 -472 1173 O HETATM 3227 O HOH A2153 8.799 9.294 3.812 1.00 32.03 O ANISOU 3227 O HOH A2153 5741 3227 3203 -221 -335 70 O HETATM 3228 O HOH A2154 0.365 4.784 10.373 1.00 32.97 O ANISOU 3228 O HOH A2154 2864 6437 3224 1847 -19 850 O HETATM 3229 O HOH A2155 0.357 7.549 9.284 1.00 30.75 O ANISOU 3229 O HOH A2155 3428 3540 4712 -291 -375 -569 O HETATM 3230 O HOH A2156 1.089 23.816 11.376 1.00 48.30 O ANISOU 3230 O HOH A2156 5037 5770 7544 -77 229 -237 O HETATM 3231 O HOH A2157 -11.054 21.763 18.205 1.00 21.87 O ANISOU 3231 O HOH A2157 2842 2420 3045 575 -584 370 O HETATM 3232 O HOH A2158 -13.500 16.890 15.466 1.00 36.57 O ANISOU 3232 O HOH A2158 2584 3941 7368 -206 -1436 -32 O HETATM 3233 O HOH A2159 -8.611 16.699 34.492 1.00 18.93 O ANISOU 3233 O HOH A2159 2552 1453 3184 160 -390 117 O HETATM 3234 O HOH A2160 -10.871 20.324 37.193 1.00 17.55 O ANISOU 3234 O HOH A2160 1876 1457 3334 161 -33 172 O HETATM 3235 O HOH A2161 -5.856 18.412 50.235 1.00 22.21 O ANISOU 3235 O HOH A2161 1887 3204 3348 512 -849 -639 O HETATM 3236 O HOH A2162 -6.283 28.552 51.401 1.00 56.12 O ANISOU 3236 O HOH A2162 3482 15198 2642 907 380 2500 O HETATM 3237 O HOH A2163 -11.954 28.532 44.941 1.00 44.75 O ANISOU 3237 O HOH A2163 6880 2954 7167 974 1236 213 O HETATM 3238 O HOH A2164 -10.910 35.243 48.444 0.50 29.35 O ANISOU 3238 O HOH A2164 1097 3484 6568 1604 -1121 -1189 O HETATM 3239 O HOH A2165 -9.463 35.235 42.660 1.00 31.43 O ANISOU 3239 O HOH A2165 2437 4010 5493 138 23 -273 O HETATM 3240 O HOH A2166 -14.858 33.082 39.464 1.00 29.21 O ANISOU 3240 O HOH A2166 850 6121 4125 908 176 -300 O HETATM 3241 O HOH A2167 -17.475 31.649 36.766 1.00 52.43 O ANISOU 3241 O HOH A2167 3101 9234 7583 -1360 474 4137 O HETATM 3242 O HOH A2168 -17.732 33.575 34.161 1.00 48.75 O ANISOU 3242 O HOH A2168 5342 3981 9198 -1267 -4531 1166 O HETATM 3243 O HOH A2169 -15.681 30.353 33.487 1.00 38.47 O ANISOU 3243 O HOH A2169 5207 4021 5388 17 5 1264 O HETATM 3244 O HOH A2170 -7.763 38.896 39.470 1.00 46.08 O ANISOU 3244 O HOH A2170 1566 4321 11619 568 502 -687 O HETATM 3245 O HOH A2171 -9.475 31.046 29.759 1.00 43.66 O ANISOU 3245 O HOH A2171 4880 3942 7767 105 -788 1912 O HETATM 3246 O HOH A2172 -17.194 24.644 36.301 1.00 40.39 O ANISOU 3246 O HOH A2172 3742 6195 5409 -372 -726 914 O HETATM 3247 O HOH A2173 -14.066 24.718 31.970 1.00 35.44 O ANISOU 3247 O HOH A2173 3983 2968 6515 533 30 92 O HETATM 3248 O HOH A2174 -11.859 29.133 30.111 1.00 30.29 O ANISOU 3248 O HOH A2174 5630 2444 3431 -537 -1145 0 O HETATM 3249 O HOH A2175 -8.334 39.387 32.325 1.00 32.56 O ANISOU 3249 O HOH A2175 1852 4456 6063 -723 -423 -222 O HETATM 3250 O HOH A2176 -9.326 31.138 22.836 0.50 30.79 O ANISOU 3250 O HOH A2176 2068 1512 8117 379 9 1534 O HETATM 3251 O HOH A2177 -2.761 37.752 30.621 1.00 48.44 O ANISOU 3251 O HOH A2177 3580 3168 11655 -119 3182 -1015 O HETATM 3252 O HOH A2178 4.216 32.287 31.984 1.00 23.19 O ANISOU 3252 O HOH A2178 2639 3162 3009 291 526 295 O HETATM 3253 O HOH A2179 0.831 30.420 22.222 1.00 34.14 O ANISOU 3253 O HOH A2179 7133 2899 2938 626 841 -91 O HETATM 3254 O HOH A2180 -2.804 30.336 15.752 1.00 28.12 O ANISOU 3254 O HOH A2180 3279 1974 5428 -894 134 1244 O HETATM 3255 O HOH A2181 -3.255 31.752 17.979 1.00 36.38 O ANISOU 3255 O HOH A2181 3972 2927 6921 -537 449 -632 O HETATM 3256 O HOH A2182 -0.678 31.750 14.772 1.00 40.56 O ANISOU 3256 O HOH A2182 6164 3421 5824 -311 -1381 2131 O HETATM 3257 O HOH A2183 2.254 31.352 14.167 1.00 46.30 O ANISOU 3257 O HOH A2183 4734 4852 8006 117 -234 2875 O HETATM 3258 O HOH A2184 6.390 21.428 16.980 1.00 40.22 O ANISOU 3258 O HOH A2184 3934 5581 5766 -134 674 1152 O HETATM 3259 O HOH A2185 -5.046 31.431 14.541 0.50 24.80 O ANISOU 3259 O HOH A2185 2917 1486 5020 1090 1437 1556 O HETATM 3260 O HOH A2186 -10.998 28.630 21.033 1.00 39.19 O ANISOU 3260 O HOH A2186 6337 3107 5443 -842 -722 711 O HETATM 3261 O HOH A2187 -7.075 29.361 20.828 1.00 25.32 O ANISOU 3261 O HOH A2187 3427 2499 3695 5 156 648 O HETATM 3262 O HOH A2188 -4.727 26.332 13.209 1.00 47.15 O ANISOU 3262 O HOH A2188 5899 5627 6389 -1388 3848 -235 O HETATM 3263 O HOH A2189 -8.161 31.151 14.140 1.00 35.11 O ANISOU 3263 O HOH A2189 7433 2089 3818 2049 649 1082 O HETATM 3264 O HOH A2190 -12.958 33.874 12.066 0.50 37.44 O ANISOU 3264 O HOH A2190 2640 5262 6322 2061 -216 -149 O HETATM 3265 O HOH A2191 -14.546 34.681 14.368 1.00 41.86 O ANISOU 3265 O HOH A2191 4414 4993 6498 926 1807 107 O HETATM 3266 O HOH A2192 -14.600 24.076 18.357 1.00 41.84 O ANISOU 3266 O HOH A2192 4080 5470 6346 499 -884 3340 O HETATM 3267 O HOH A2193 -13.239 26.270 24.823 1.00 24.24 O ANISOU 3267 O HOH A2193 2255 2893 4062 787 483 518 O HETATM 3268 O HOH A2194 -13.456 27.116 27.597 1.00 52.22 O ANISOU 3268 O HOH A2194 4721 8122 6997 3863 -777 -991 O HETATM 3269 O HOH A2195 -15.130 24.165 27.143 1.00 37.96 O ANISOU 3269 O HOH A2195 4333 3693 6398 -845 -54 351 O HETATM 3270 O HOH A2196 -12.315 26.102 30.348 1.00 33.15 O ANISOU 3270 O HOH A2196 3824 4606 4165 486 -559 -208 O HETATM 3271 O HOH A2197 -15.243 22.361 30.811 1.00 24.71 O ANISOU 3271 O HOH A2197 2731 3411 3245 1503 -1 -629 O HETATM 3272 O HOH A2198 -14.982 18.842 24.371 1.00 18.29 O ANISOU 3272 O HOH A2198 1629 1996 3322 68 99 -711 O HETATM 3273 O HOH A2199 -18.271 20.911 27.072 1.00 38.78 O ANISOU 3273 O HOH A2199 3094 3474 8163 -734 -182 2120 O HETATM 3274 O HOH A2200 -16.704 21.401 32.948 1.00 29.69 O ANISOU 3274 O HOH A2200 3957 3221 4103 106 247 419 O HETATM 3275 O HOH A2201 -18.027 19.940 36.353 1.00 27.04 O ANISOU 3275 O HOH A2201 2743 2245 5285 738 208 -524 O HETATM 3276 O HOH A2202 -13.152 21.420 49.806 1.00 29.59 O ANISOU 3276 O HOH A2202 3510 3142 4589 454 -208 -783 O HETATM 3277 O HOH A2203 -14.645 26.990 45.169 1.00 44.76 O ANISOU 3277 O HOH A2203 9272 3267 4465 921 -373 -163 O HETATM 3278 O HOH A2204 -10.557 16.792 45.335 1.00 16.93 O ANISOU 3278 O HOH A2204 1245 1362 3825 -61 502 160 O HETATM 3279 O HOH A2205 -7.601 18.999 54.294 0.50 17.90 O ANISOU 3279 O HOH A2205 1305 1498 3996 -374 789 10 O HETATM 3280 O HOH A2206 -11.811 11.023 46.251 1.00 20.20 O ANISOU 3280 O HOH A2206 3080 1286 3309 1082 -161 227 O HETATM 3281 O HOH A2207 0.011 0.001 35.741 0.50 13.79 O ANISOU 3281 O HOH A2207 1777 761 2700 -588 4 -195 O HETATM 3282 O HOH A2208 -3.058 3.134 36.441 1.00 32.60 O ANISOU 3282 O HOH A2208 2102 5122 5162 -669 -1501 1041 O HETATM 3283 O HOH A2209 -2.317 5.733 34.423 1.00 24.54 O ANISOU 3283 O HOH A2209 2540 3810 2972 -203 544 -549 O HETATM 3284 O HOH A2210 -0.407 2.658 34.692 1.00 17.40 O ANISOU 3284 O HOH A2210 2397 1787 2425 -250 396 -264 O HETATM 3285 O HOH A2211 -0.351 6.360 32.540 1.00 12.62 O ANISOU 3285 O HOH A2211 1463 1131 2199 268 253 84 O HETATM 3286 O HOH A2212 6.544 2.985 34.858 1.00 14.52 O ANISOU 3286 O HOH A2212 1570 1253 2693 386 626 2 O HETATM 3287 O HOH A2213 4.019 2.792 26.047 1.00 28.98 O ANISOU 3287 O HOH A2213 5058 2708 3243 -1129 937 -83 O HETATM 3288 O HOH A2214 1.943 4.318 25.064 1.00 24.31 O ANISOU 3288 O HOH A2214 3196 2720 3321 1235 1191 1534 O HETATM 3289 O HOH A2215 -0.092 2.065 24.113 1.00 21.11 O ANISOU 3289 O HOH A2215 2203 2003 3814 205 -116 -96 O HETATM 3290 O HOH A2216 1.355 0.782 17.192 1.00 24.25 O ANISOU 3290 O HOH A2216 2267 4826 2120 1353 641 808 O HETATM 3291 O HOH A2217 6.755 1.590 32.343 1.00 20.08 O ANISOU 3291 O HOH A2217 2895 2375 2357 120 14 -329 O HETATM 3292 O HOH A2218 8.430 -2.087 30.708 1.00 24.39 O ANISOU 3292 O HOH A2218 941 1771 6556 -237 -259 865 O HETATM 3293 O HOH A2219 17.320 -0.110 36.834 0.50 17.58 O ANISOU 3293 O HOH A2219 1409 1901 3369 458 -414 -661 O HETATM 3294 O HOH A2220 20.458 -0.655 39.185 1.00 19.17 O ANISOU 3294 O HOH A2220 2610 1616 3054 311 -318 -1 O HETATM 3295 O HOH A2221 11.706 -7.031 35.371 1.00 16.21 O ANISOU 3295 O HOH A2221 2439 1081 2636 -507 265 227 O HETATM 3296 O HOH A2222 21.850 5.840 14.891 1.00 23.00 O ANISOU 3296 O HOH A2222 2730 2030 3977 29 768 821 O HETATM 3297 O HOH A2223 14.473 9.377 10.004 1.00 40.54 O ANISOU 3297 O HOH A2223 5456 4340 5607 -1894 -737 13 O HETATM 3298 O HOH A2224 19.285 15.245 14.370 1.00 33.60 O ANISOU 3298 O HOH A2224 2212 4349 6203 630 750 642 O HETATM 3299 O HOH A2225 22.388 4.712 9.925 0.50 22.36 O ANISOU 3299 O HOH A2225 377 5247 2872 780 -100 -1088 O HETATM 3300 O HOH A2226 14.953 3.859 4.616 1.00 32.19 O ANISOU 3300 O HOH A2226 3328 4554 4346 -1867 1008 -374 O HETATM 3301 O HOH A2227 8.975 -9.756 20.392 1.00 17.44 O ANISOU 3301 O HOH A2227 1357 2134 3133 -6 -89 402 O HETATM 3302 O HOH A2228 15.281 -14.005 28.908 1.00 14.82 O ANISOU 3302 O HOH A2228 1507 1649 2472 130 344 130 O HETATM 3303 O HOH A2229 19.289 -20.202 32.492 1.00 43.34 O ANISOU 3303 O HOH A2229 1949 2989 11529 701 -606 732 O HETATM 3304 O HOH A2230 20.462 -16.962 27.450 1.00 24.74 O ANISOU 3304 O HOH A2230 2099 1976 5322 -30 1385 353 O HETATM 3305 O HOH A2231 16.893 -16.671 24.946 1.00 24.32 O ANISOU 3305 O HOH A2231 2950 2522 3769 -252 683 -152 O HETATM 3306 O HOH A2232 25.848 -15.306 24.855 1.00 33.84 O ANISOU 3306 O HOH A2232 1421 3982 7454 -46 -470 -1290 O HETATM 3307 O HOH A2233 12.975 -17.914 22.502 1.00 18.04 O ANISOU 3307 O HOH A2233 2054 1680 3120 -185 399 -17 O HETATM 3308 O HOH A2234 13.675 -12.318 17.182 1.00 26.09 O ANISOU 3308 O HOH A2234 3439 3650 2821 -486 829 -876 O HETATM 3309 O HOH A2235 9.940 -8.378 13.428 1.00 21.61 O ANISOU 3309 O HOH A2235 3359 1731 3120 233 -203 -801 O HETATM 3310 O HOH A2236 7.724 -7.432 12.120 1.00 24.76 O ANISOU 3310 O HOH A2236 2362 1252 5791 -107 606 -377 O HETATM 3311 O HOH A2237 4.743 -1.996 11.001 1.00 29.77 O ANISOU 3311 O HOH A2237 4108 3139 4063 -757 -695 1256 O HETATM 3312 O AHOH A2238 1.203 2.943 8.706 0.90 32.56 O ANISOU 3312 O AHOH A2238 2177 3494 6698 -1096 -1329 1740 O HETATM 3313 O HOH A2239 9.500 -1.463 3.351 1.00 41.92 O ANISOU 3313 O HOH A2239 3510 6792 5627 93 -269 -2360 O HETATM 3314 O HOH A2240 16.239 -0.778 0.872 0.50 31.60 O ANISOU 3314 O HOH A2240 2267 4742 4996 -664 -1727 -1063 O HETATM 3315 O HOH A2241 18.098 -2.935 1.498 1.00 45.75 O ANISOU 3315 O HOH A2241 5642 7734 4007 -420 612 1096 O HETATM 3316 O HOH A2242 20.009 -4.088 5.286 1.00 40.90 O ANISOU 3316 O HOH A2242 7112 4309 4116 376 1398 692 O HETATM 3317 O HOH A2243 22.192 0.313 3.231 1.00 40.51 O ANISOU 3317 O HOH A2243 3826 7422 4144 -784 654 512 O HETATM 3318 O HOH A2244 10.109 -8.156 6.806 1.00 25.69 O ANISOU 3318 O HOH A2244 2731 2734 4297 -3 110 -98 O HETATM 3319 O HOH A2245 8.680 -5.025 5.738 1.00 27.67 O ANISOU 3319 O HOH A2245 2867 4016 3630 214 -1088 -1927 O HETATM 3320 O HOH A2246 11.323 -9.034 11.039 1.00 27.95 O ANISOU 3320 O HOH A2246 2637 3699 4283 588 551 268 O HETATM 3321 O HOH A2247 5.230 -2.766 7.750 1.00 39.03 O ANISOU 3321 O HOH A2247 3673 5007 6149 281 -2328 778 O HETATM 3322 O HOH A2248 21.808 -10.222 12.177 1.00 45.65 O ANISOU 3322 O HOH A2248 6257 5096 5989 2857 1915 854 O HETATM 3323 O HOH A2249 23.530 -9.441 19.712 1.00 44.71 O ANISOU 3323 O HOH A2249 6709 4828 5451 393 -280 -2055 O HETATM 3324 O HOH A2250 13.572 -14.083 14.830 1.00 25.21 O ANISOU 3324 O HOH A2250 2644 2806 4126 -203 -293 398 O HETATM 3325 O HOH A2251 20.212 -8.460 19.690 1.00 45.08 O ANISOU 3325 O HOH A2251 5963 6750 4415 -2852 -182 -262 O HETATM 3326 O HOH A2252 24.269 -3.184 22.912 1.00 32.71 O ANISOU 3326 O HOH A2252 5975 1754 4700 -407 0 -484 O HETATM 3327 O HOH A2253 23.227 -3.019 25.577 1.00 26.16 O ANISOU 3327 O HOH A2253 3696 2096 4145 139 143 144 O HETATM 3328 O HOH A2254 28.403 -7.118 23.861 1.00 43.27 O ANISOU 3328 O HOH A2254 2230 8904 5306 985 1127 -575 O HETATM 3329 O HOH A2255 20.467 -9.738 22.241 1.00 22.05 O ANISOU 3329 O HOH A2255 2060 1996 4322 -1401 1316 -1172 O HETATM 3330 O HOH A2256 29.620 -12.875 24.814 1.00 23.71 O ANISOU 3330 O HOH A2256 3069 1775 4161 -39 68 -108 O HETATM 3331 O HOH A2257 29.453 1.873 32.365 1.00 52.68 O ANISOU 3331 O HOH A2257 1580 5148 13286 -1153 -202 -1710 O HETATM 3332 O HOH A2258 26.165 3.847 25.428 1.00 26.81 O ANISOU 3332 O HOH A2258 2268 2801 5118 -636 -1 431 O HETATM 3333 O HOH A2259 26.879 5.621 28.473 1.00 46.32 O ANISOU 3333 O HOH A2259 4251 8135 5214 737 -65 -2006 O HETATM 3334 O HOH A2260 22.215 5.955 33.658 1.00 29.76 O ANISOU 3334 O HOH A2260 4468 2973 3864 -620 -217 27 O HETATM 3335 O HOH A2261 21.186 4.708 36.129 1.00 33.70 O ANISOU 3335 O HOH A2261 3002 4365 5437 606 -301 88 O HETATM 3336 O HOH A2262 26.619 1.843 35.959 1.00 21.61 O ANISOU 3336 O HOH A2262 1461 3281 3466 251 81 352 O HETATM 3337 O HOH A2263 26.161 8.200 32.373 1.00 47.08 O ANISOU 3337 O HOH A2263 5874 3433 8579 -1220 2479 1225 O HETATM 3338 O HOH A2264 20.498 12.943 39.632 1.00 55.26 O ANISOU 3338 O HOH A2264 5213 6444 9337 -3537 2885 -435 O HETATM 3339 O HOH A2265 15.075 16.820 30.771 1.00 30.42 O ANISOU 3339 O HOH A2265 5365 2441 3749 -1349 1060 -379 O HETATM 3340 O HOH A2266 9.492 13.442 28.467 1.00 28.32 O ANISOU 3340 O HOH A2266 3892 3301 3566 1793 297 317 O HETATM 3341 O HOH A2267 15.707 16.063 24.690 1.00 37.76 O ANISOU 3341 O HOH A2267 1620 4473 8251 674 200 1115 O HETATM 3342 O HOH A2268 24.429 5.997 24.821 1.00 19.07 O ANISOU 3342 O HOH A2268 328 2280 4636 156 -434 877 O HETATM 3343 O HOH A2269 25.159 5.989 22.149 1.00 28.29 O ANISOU 3343 O HOH A2269 2746 4282 3721 -153 -767 -72 O HETATM 3344 O HOH A2270 27.904 4.668 18.793 1.00 29.04 O ANISOU 3344 O HOH A2270 1263 5139 4629 -1536 815 -1227 O HETATM 3345 O HOH A2271 23.504 5.009 12.703 1.00 25.45 O ANISOU 3345 O HOH A2271 2671 2442 4555 -20 611 -163 O HETATM 3346 O HOH A2272 28.665 0.397 8.397 0.50 23.57 O ANISOU 3346 O HOH A2272 2925 4385 1643 -1410 425 -124 O HETATM 3347 O HOH A2273 -7.891 7.886 35.757 1.00 20.06 O ANISOU 3347 O HOH A2273 1598 1823 4201 -220 1058 -638 O HETATM 3348 O HOH A2274 -9.725 6.022 41.682 1.00 30.38 O ANISOU 3348 O HOH A2274 5484 1930 4128 -923 2036 -580 O HETATM 3349 O HOH A2275 -10.155 6.631 37.804 1.00 30.66 O ANISOU 3349 O HOH A2275 1970 5361 4315 -452 -463 997 O HETATM 3350 O HOH A2276 -6.236 6.816 33.438 0.90 23.51 O ANISOU 3350 O HOH A2276 3495 2160 3278 787 1152 1020 O HETATM 3351 O HOH A2277 -8.744 15.171 36.869 1.00 16.28 O ANISOU 3351 O HOH A2277 1931 1503 2751 16 -300 104 O HETATM 3352 O HOH A2278 13.187 -1.136 58.198 0.50 22.78 O ANISOU 3352 O HOH A2278 4014 2980 1660 -128 -507 315 O CONECT 118 3073 CONECT 1909 3072 CONECT 1914 3072 CONECT 3010 3011 CONECT 3011 3010 3012 3013 3014 CONECT 3012 3011 CONECT 3013 3011 CONECT 3014 3011 3015 CONECT 3015 3014 3016 3017 CONECT 3016 3015 CONECT 3017 3015 CONECT 3018 3019 CONECT 3019 3018 3020 3021 3022 CONECT 3020 3019 CONECT 3021 3019 CONECT 3022 3019 3023 CONECT 3023 3022 3024 3025 CONECT 3024 3023 CONECT 3025 3023 CONECT 3026 3027 3074 CONECT 3027 3026 3028 3029 3030 CONECT 3028 3027 3073 CONECT 3029 3027 CONECT 3030 3027 3031 CONECT 3031 3030 3032 3033 3034 CONECT 3032 3031 3072 3073 CONECT 3033 3031 CONECT 3034 3031 3035 CONECT 3035 3034 3036 3037 3038 CONECT 3036 3035 CONECT 3037 3035 3073 CONECT 3038 3035 3074 CONECT 3039 3040 3043 CONECT 3040 3039 3041 CONECT 3041 3040 3042 CONECT 3042 3041 3043 CONECT 3043 3039 3042 CONECT 3044 3045 3071 CONECT 3045 3044 3046 3053 CONECT 3046 3045 3047 CONECT 3047 3046 3048 CONECT 3048 3047 3049 3052 CONECT 3049 3048 3050 3051 CONECT 3050 3049 CONECT 3051 3049 CONECT 3052 3048 CONECT 3053 3045 3054 CONECT 3054 3053 3055 3058 CONECT 3055 3054 3056 3070 CONECT 3056 3055 3057 3069 CONECT 3057 3056 3058 3059 CONECT 3058 3054 3057 CONECT 3059 3057 3060 3063 CONECT 3060 3059 3061 CONECT 3061 3060 3062 CONECT 3062 3061 3063 3067 CONECT 3063 3059 3062 3064 CONECT 3064 3063 3065 CONECT 3065 3064 3066 CONECT 3066 3065 3067 CONECT 3067 3062 3066 3068 CONECT 3068 3067 CONECT 3069 3056 CONECT 3070 3055 CONECT 3071 3044 CONECT 3072 1909 1914 3032 3088 CONECT 3072 3089 CONECT 3073 118 3028 3032 3037 CONECT 3073 3088 3089 CONECT 3074 3026 3038 3080 3082 CONECT 3074 3347 3350 CONECT 3080 3074 CONECT 3082 3074 CONECT 3088 3072 3073 CONECT 3089 3072 3073 CONECT 3347 3074 CONECT 3350 3074 MASTER 407 0 8 15 13 0 20 6 3351 1 77 31 END