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*** 3ZXF ***elNémo ID: 2403281306111137963Job options:ID = 2403281306111137963 JOBID = 3ZXF USERID = Angela PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER 3ZXF HEADER SUGAR BINDING PROTEIN 10-AUG-11 3ZXF TITLE HIGH RESOLUTION STRUCTURE OF HUMAN GALECTIN-7 COMPND MOL_ID: 1; COMPND 2 MOLECULE: GALECTIN-7; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: GAL-7, HKL-14, PI7, P53-INDUCED GENE 1 PROTEIN; COMPND 5 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: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) KEYWDS SUGAR BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.MASUYER,C.T.OBERG,H.LEFFLER,U.J.NILSSON,K.R.ACHARYA REVDAT 3 20-DEC-23 3ZXF 1 REMARK LINK REVDAT 2 25-JAN-12 3ZXF 1 JRNL REVDAT 1 30-NOV-11 3ZXF 0 JRNL AUTH G.MASUYER,T.JABEEN,C.T.OBERG,H.LEFFLER,U.J.NILSSON, JRNL AUTH 2 K.R.ACHARYA JRNL TITL INHIBITION MECHANISM OF HUMAN GALECTIN-7 BY A NOVEL JRNL TITL 2 GALACTOSE-BENZYLPHOSPHATE INHIBITOR. JRNL REF FEBS J. V. 279 193 2012 JRNL REFN ISSN 1742-464X JRNL PMID 22059385 JRNL DOI 10.1111/J.1742-4658.2011.08414.X REMARK 2 REMARK 2 RESOLUTION. 1.38 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : 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) : 1.38 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.94 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8 REMARK 3 NUMBER OF REFLECTIONS : 49835 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) : 0.182 REMARK 3 R VALUE (WORKING SET) : 0.181 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600 REMARK 3 FREE R VALUE TEST SET COUNT : 1322 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) : 1.38 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.42 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3657 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.53 REMARK 3 BIN R VALUE (WORKING SET) : 0.2920 REMARK 3 BIN FREE R VALUE SET COUNT : 91 REMARK 3 BIN FREE R VALUE : 0.3590 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2137 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 333 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.18 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.85000 REMARK 3 B22 (A**2) : -0.27000 REMARK 3 B33 (A**2) : 1.12000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.078 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.072 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.039 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.115 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2267 ; 0.009 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3079 ; 1.263 ; 1.955 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 7.511 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 117 ;28.287 ;22.137 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;13.847 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.236 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.104 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1822 ; 0.014 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1403 ; 2.835 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2269 ; 4.009 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 864 ; 5.835 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 810 ; 8.116 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2267 ; 3.068 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 1136 REMARK 3 ORIGIN FOR THE GROUP (A): -6.4844 -21.3304 6.9811 REMARK 3 T TENSOR REMARK 3 T11: 0.0198 T22: 0.0304 REMARK 3 T33: 0.0263 T12: 0.0058 REMARK 3 T13: 0.0016 T23: -0.0182 REMARK 3 L TENSOR REMARK 3 L11: 0.4543 L22: 0.3834 REMARK 3 L33: 0.1573 L12: 0.1789 REMARK 3 L13: -0.0146 L23: -0.2155 REMARK 3 S TENSOR REMARK 3 S11: 0.0261 S12: -0.0560 S13: 0.0527 REMARK 3 S21: -0.0222 S22: -0.0223 S23: 0.0216 REMARK 3 S31: 0.0300 S32: 0.0196 S33: -0.0038 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B -2 B 135 REMARK 3 ORIGIN FOR THE GROUP (A): 13.1046 -19.5110 27.8701 REMARK 3 T TENSOR REMARK 3 T11: 0.0373 T22: 0.0112 REMARK 3 T33: 0.0296 T12: -0.0116 REMARK 3 T13: -0.0133 T23: 0.0170 REMARK 3 L TENSOR REMARK 3 L11: 0.8292 L22: 0.7420 REMARK 3 L33: 0.9165 L12: 0.3145 REMARK 3 L13: -0.5669 L23: 0.1603 REMARK 3 S TENSOR REMARK 3 S11: -0.0158 S12: -0.0248 S13: -0.0759 REMARK 3 S21: 0.1015 S22: -0.0443 S23: -0.0931 REMARK 3 S31: 0.0568 S32: 0.0322 S33: 0.0601 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 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. REMARK 4 REMARK 4 3ZXF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-11. REMARK 100 THE DEPOSITION ID IS D_1290049301. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 23-JUN-08 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.1 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I04 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.972 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52544 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5 REMARK 200 DATA REDUNDANCY : 5.300 REMARK 200 R MERGE (I) : 0.06000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 25.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2 REMARK 200 DATA REDUNDANCY IN SHELL : 4.30 REMARK 200 R MERGE FOR SHELL (I) : 0.32000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 1BKZ REMARK 200 REMARK 200 REMARK: NONE REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM SODIUM PHOSPHATE, 300 MM NACL, REMARK 280 15% PEG3350, 20MM IMIDAZOLE, PH 8.1 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 27.15050 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.41600 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.55500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 35.41600 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.15050 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.55500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA 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 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 PRO A -2 REMARK 465 ALA A -1 REMARK 465 MET A 0 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 CSX B 38 OD REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH B 2082 O HOH B 2083 0.56 REMARK 500 OD1 ASP B 45 O GLU B 65 1.76 REMARK 500 CG2 ILE B 13 O HOH B 2012 1.94 REMARK 500 O HOH A 2036 O HOH A 2037 2.06 REMARK 500 O HOH B 2012 O HOH B 2013 2.09 REMARK 500 O HOH A 2159 O HOH A 2160 2.15 REMARK 500 O HOH A 2196 O HOH A 2197 2.18 REMARK 500 REMARK 500 REMARK: NULL 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 NH2 ARG B 110 O HOH A 2169 3545 1.77 REMARK 500 O HOH A 2083 O HOH B 2054 4445 2.12 REMARK 500 O HOH A 2094 O HOH A 2123 4445 2.15 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 ARG B 117 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 ARG B 117 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES 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 PRO A 79 41.35 -84.39 REMARK 500 GLU B 65 -70.42 -108.61 REMARK 500 PRO B 79 37.47 -88.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A2098 DISTANCE = 6.16 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1136 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3ZXE RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN GALECTIN-7 IN COMPLEX WITH A GALACTOSE- REMARK 900 BENZYLPHOSPHATE INHIBITOR REMARK 900 RELATED ID: 4GAL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN GALECTIN-7 IN COMPLEX WITH LACTOSE REMARK 900 RELATED ID: 5GAL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN GALECTIN-7 IN COMPLEX WITH N- REMARK 900 ACETYLLACTOSAMINE REMARK 900 RELATED ID: 1BKZ RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN GALECTIN-7 REMARK 900 RELATED ID: 2GAL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN GALECTIN-7 IN COMPLEX WITH GALACTOSE REMARK 900 RELATED ID: 3GAL RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF HUMAN GALECTIN-7 IN COMPLEX WITH GALACTOSAMINE DBREF 3ZXF A 0 135 UNP P47929 LEG7_HUMAN 1 136 DBREF 3ZXF B 0 135 UNP P47929 LEG7_HUMAN 1 136 SEQADV 3ZXF PRO A -2 UNP P47929 EXPRESSION TAG SEQADV 3ZXF ALA A -1 UNP P47929 EXPRESSION TAG SEQADV 3ZXF PRO B -2 UNP P47929 EXPRESSION TAG SEQADV 3ZXF ALA B -1 UNP P47929 EXPRESSION TAG SEQRES 1 A 138 PRO ALA MET SER ASN VAL PRO HIS LYS SER SER LEU PRO SEQRES 2 A 138 GLU GLY ILE ARG PRO GLY THR VAL LEU ARG ILE ARG GLY SEQRES 3 A 138 LEU VAL PRO PRO ASN ALA SER ARG PHE HIS VAL ASN LEU SEQRES 4 A 138 LEU CSX GLY GLU GLU GLN GLY SER ASP ALA ALA LEU HIS SEQRES 5 A 138 PHE ASN PRO ARG LEU ASP THR SER GLU VAL VAL PHE ASN SEQRES 6 A 138 SER LYS GLU GLN GLY SER TRP GLY ARG GLU GLU ARG GLY SEQRES 7 A 138 PRO GLY VAL PRO PHE GLN ARG GLY GLN PRO PHE GLU VAL SEQRES 8 A 138 LEU ILE ILE ALA SER ASP ASP GLY PHE LYS ALA VAL VAL SEQRES 9 A 138 GLY ASP ALA GLN TYR HIS HIS PHE ARG HIS ARG LEU PRO SEQRES 10 A 138 LEU ALA ARG VAL ARG LEU VAL GLU VAL GLY GLY ASP VAL SEQRES 11 A 138 GLN LEU ASP SER VAL ARG ILE PHE SEQRES 1 B 138 PRO ALA MET SER ASN VAL PRO HIS LYS SER SER LEU PRO SEQRES 2 B 138 GLU GLY ILE ARG PRO GLY THR VAL LEU ARG ILE ARG GLY SEQRES 3 B 138 LEU VAL PRO PRO ASN ALA SER ARG PHE HIS VAL ASN LEU SEQRES 4 B 138 LEU CSX GLY GLU GLU GLN GLY SER ASP ALA ALA LEU HIS SEQRES 5 B 138 PHE ASN PRO ARG LEU ASP THR SER GLU VAL VAL PHE ASN SEQRES 6 B 138 SER LYS GLU GLN GLY SER TRP GLY ARG GLU GLU ARG GLY SEQRES 7 B 138 PRO GLY VAL PRO PHE GLN ARG GLY GLN PRO PHE GLU VAL SEQRES 8 B 138 LEU ILE ILE ALA SER ASP ASP GLY PHE LYS ALA VAL VAL SEQRES 9 B 138 GLY ASP ALA GLN TYR HIS HIS PHE ARG HIS ARG LEU PRO SEQRES 10 B 138 LEU ALA ARG VAL ARG LEU VAL GLU VAL GLY GLY ASP VAL SEQRES 11 B 138 GLN LEU ASP SER VAL ARG ILE PHE MODRES 3ZXF CSX A 38 CYS S-OXY CYSTEINE MODRES 3ZXF CSX B 38 CYS S-OXY CYSTEINE HET CSX A 38 7 HET CSX B 38 6 HET ACT A1136 4 HETNAM CSX S-OXY CYSTEINE HETNAM ACT ACETATE ION FORMUL 1 CSX 2(C3 H7 N O3 S) FORMUL 3 ACT C2 H3 O2 1- FORMUL 4 HOH *333(H2 O) HELIX 1 1 PRO A 114 VAL A 118 5 5 HELIX 2 2 PRO B 114 VAL B 118 5 5 SHEET 1 AA 6 HIS A 5 SER A 8 0 SHEET 2 AA 6 LEU A 120 GLY A 125 -1 O VAL A 121 N SER A 7 SHEET 3 AA 6 PHE A 32 LEU A 37 -1 O HIS A 33 N GLY A 124 SHEET 4 AA 6 ALA A 46 ARG A 53 -1 N ALA A 47 O LEU A 36 SHEET 5 AA 6 GLU A 58 GLU A 65 -1 O GLU A 58 N ARG A 53 SHEET 6 AA 6 SER A 68 TRP A 69 -1 O SER A 68 N GLU A 65 SHEET 1 AB 6 HIS A 5 SER A 8 0 SHEET 2 AB 6 LEU A 120 GLY A 125 -1 O VAL A 121 N SER A 7 SHEET 3 AB 6 PHE A 32 LEU A 37 -1 O HIS A 33 N GLY A 124 SHEET 4 AB 6 ALA A 46 ARG A 53 -1 N ALA A 47 O LEU A 36 SHEET 5 AB 6 GLU A 58 GLU A 65 -1 O GLU A 58 N ARG A 53 SHEET 6 AB 6 GLU A 73 ARG A 74 -1 O GLU A 73 N PHE A 61 SHEET 1 AC 2 SER A 68 TRP A 69 0 SHEET 2 AC 2 GLU A 58 GLU A 65 -1 O GLU A 65 N SER A 68 SHEET 1 AD 5 ALA A 104 ARG A 110 0 SHEET 2 AD 5 GLY A 96 VAL A 101 -1 O PHE A 97 N PHE A 109 SHEET 3 AD 5 GLN A 84 ALA A 92 -1 O LEU A 89 N VAL A 100 SHEET 4 AD 5 THR A 17 VAL A 25 -1 O THR A 17 N ALA A 92 SHEET 5 AD 5 GLN A 128 ILE A 134 -1 O GLN A 128 N LEU A 24 SHEET 1 BA 6 HIS B 5 SER B 8 0 SHEET 2 BA 6 LEU B 120 GLY B 125 -1 O VAL B 121 N SER B 7 SHEET 3 BA 6 PHE B 32 LEU B 37 -1 O HIS B 33 N GLY B 124 SHEET 4 BA 6 ALA B 46 ARG B 53 -1 N ALA B 47 O LEU B 36 SHEET 5 BA 6 GLU B 58 LYS B 64 -1 O GLU B 58 N ARG B 53 SHEET 6 BA 6 GLU B 73 PRO B 76 -1 O GLU B 73 N PHE B 61 SHEET 1 BB 5 ALA B 104 ARG B 110 0 SHEET 2 BB 5 GLY B 96 VAL B 101 -1 O PHE B 97 N PHE B 109 SHEET 3 BB 5 PRO B 85 ALA B 92 -1 O LEU B 89 N VAL B 100 SHEET 4 BB 5 VAL B 18 LEU B 24 -1 O LEU B 19 N ILE B 90 SHEET 5 BB 5 GLN B 128 PHE B 135 -1 O GLN B 128 N LEU B 24 LINK C LEU A 37 N CSX A 38 1555 1555 1.33 LINK C CSX A 38 N GLY A 39 1555 1555 1.33 LINK C LEU B 37 N CSX B 38 1555 1555 1.34 LINK C CSX B 38 N GLY B 39 1555 1555 1.32 SITE 1 AC1 6 GLN A 81 HOH A2167 ALA B -1 ASP B 95 SITE 2 AC1 6 ARG B 110 HIS B 111 CRYST1 54.301 65.110 70.832 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.018416 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015359 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014118 0.00000 ATOM 1 N SER A 1 0.710 -21.197 -12.324 1.00 37.85 N ANISOU 1 N SER A 1 4500 4786 5095 -11 -128 90 N ATOM 2 CA SER A 1 -0.091 -22.354 -11.823 1.00 33.45 C ANISOU 2 CA SER A 1 4273 4275 4160 358 364 57 C ATOM 3 C SER A 1 -0.242 -22.316 -10.299 1.00 29.98 C ANISOU 3 C SER A 1 3581 4099 3709 228 41 81 C ATOM 4 O SER A 1 0.747 -22.238 -9.552 1.00 28.84 O ANISOU 4 O SER A 1 3243 4207 3505 152 -73 65 O ATOM 5 CB SER A 1 0.532 -23.680 -12.269 1.00 37.91 C ANISOU 5 CB SER A 1 4838 4726 4837 148 334 -223 C ATOM 6 OG SER A 1 -0.307 -24.774 -11.931 1.00 38.44 O ANISOU 6 OG SER A 1 5923 4206 4477 -19 733 -856 O ATOM 7 N ASN A 2 -1.479 -22.436 -9.836 1.00 24.50 N ANISOU 7 N ASN A 2 3228 3138 2941 307 65 205 N ATOM 8 CA ASN A 2 -1.734 -22.704 -8.427 1.00 23.71 C ANISOU 8 CA ASN A 2 3218 2865 2925 300 -132 285 C ATOM 9 C ASN A 2 -1.712 -24.209 -8.162 1.00 24.43 C ANISOU 9 C ASN A 2 3422 2556 3304 354 -233 84 C ATOM 10 O ASN A 2 -2.469 -24.969 -8.773 1.00 29.25 O ANISOU 10 O ASN A 2 3936 3111 4068 166 -601 173 O ATOM 11 CB ASN A 2 -3.081 -22.126 -7.979 1.00 22.70 C ANISOU 11 CB ASN A 2 3078 2700 2847 345 12 407 C ATOM 12 CG ASN A 2 -3.139 -20.617 -8.070 1.00 23.40 C ANISOU 12 CG ASN A 2 2752 2829 3310 -1 -25 -42 C ATOM 13 OD1 ASN A 2 -2.114 -19.934 -8.133 1.00 23.03 O ANISOU 13 OD1 ASN A 2 2427 3035 3285 66 101 -89 O ATOM 14 ND2 ASN A 2 -4.358 -20.075 -8.041 1.00 23.27 N ANISOU 14 ND2 ASN A 2 3160 3191 2490 372 -37 -160 N ATOM 15 N VAL A 3 -0.797 -24.630 -7.294 1.00 23.14 N ANISOU 15 N VAL A 3 3420 2555 2815 377 -29 -37 N ATOM 16 CA VAL A 3 -0.640 -26.035 -6.911 1.00 23.96 C ANISOU 16 CA VAL A 3 3474 2699 2930 349 197 -84 C ATOM 17 C VAL A 3 -0.835 -26.130 -5.393 1.00 22.33 C ANISOU 17 C VAL A 3 3049 2785 2650 517 158 -292 C ATOM 18 O VAL A 3 -0.077 -25.526 -4.625 1.00 23.00 O ANISOU 18 O VAL A 3 3472 2837 2427 416 161 -93 O ATOM 19 CB VAL A 3 0.767 -26.592 -7.315 1.00 24.75 C ANISOU 19 CB VAL A 3 3938 2687 2777 553 369 -100 C ATOM 20 CG1 VAL A 3 0.906 -28.057 -6.897 1.00 25.73 C ANISOU 20 CG1 VAL A 3 3888 2471 3415 310 174 -224 C ATOM 21 CG2 VAL A 3 0.996 -26.464 -8.834 1.00 27.65 C ANISOU 21 CG2 VAL A 3 4144 3456 2906 382 644 -256 C ATOM 22 N PRO A 4 -1.841 -26.909 -4.949 1.00 22.90 N ANISOU 22 N PRO A 4 3242 2954 2504 361 -18 -152 N ATOM 23 CA PRO A 4 -2.109 -26.982 -3.505 1.00 23.41 C ANISOU 23 CA PRO A 4 3298 2742 2853 329 104 52 C ATOM 24 C PRO A 4 -0.912 -27.536 -2.722 1.00 21.49 C ANISOU 24 C PRO A 4 2850 2479 2835 510 368 -117 C ATOM 25 O PRO A 4 -0.183 -28.407 -3.215 1.00 24.24 O ANISOU 25 O PRO A 4 3676 2756 2775 550 550 -492 O ATOM 26 CB PRO A 4 -3.290 -27.949 -3.420 1.00 24.72 C ANISOU 26 CB PRO A 4 2992 3200 3201 405 -263 146 C ATOM 27 CG PRO A 4 -3.951 -27.867 -4.748 1.00 25.75 C ANISOU 27 CG PRO A 4 3609 3408 2766 212 138 187 C ATOM 28 CD PRO A 4 -2.897 -27.556 -5.752 1.00 24.81 C ANISOU 28 CD PRO A 4 3336 3071 3018 113 350 -286 C ATOM 29 N HIS A 5 -0.684 -27.002 -1.526 1.00 17.20 N ANISOU 29 N HIS A 5 2307 2148 2079 359 363 124 N ATOM 30 CA HIS A 5 0.320 -27.520 -0.619 1.00 16.26 C ANISOU 30 CA HIS A 5 2015 2239 1924 91 403 55 C ATOM 31 C HIS A 5 -0.350 -28.330 0.479 1.00 14.02 C ANISOU 31 C HIS A 5 1914 1518 1894 327 482 -116 C ATOM 32 O HIS A 5 -1.214 -27.823 1.169 1.00 15.75 O ANISOU 32 O HIS A 5 2168 1779 2035 480 685 36 O ATOM 33 CB HIS A 5 1.109 -26.362 0.001 1.00 19.92 C ANISOU 33 CB HIS A 5 2298 2369 2901 147 327 30 C ATOM 34 CG HIS A 5 2.272 -26.801 0.838 1.00 20.95 C ANISOU 34 CG HIS A 5 2511 2333 3115 -146 306 -167 C ATOM 35 ND1 HIS A 5 2.131 -27.251 2.132 1.00 23.17 N ANISOU 35 ND1 HIS A 5 3481 2061 3259 267 -158 -869 N ATOM 36 CD2 HIS A 5 3.599 -26.831 0.571 1.00 29.32 C ANISOU 36 CD2 HIS A 5 3074 4082 3984 201 322 109 C ATOM 37 CE1 HIS A 5 3.320 -27.548 2.625 1.00 25.91 C ANISOU 37 CE1 HIS A 5 3492 3303 3047 458 350 -364 C ATOM 38 NE2 HIS A 5 4.230 -27.284 1.704 1.00 30.34 N ANISOU 38 NE2 HIS A 5 3460 4175 3891 822 348 12 N ATOM 39 N LYS A 6 0.031 -29.593 0.624 1.00 15.90 N ANISOU 39 N LYS A 6 2217 1643 2179 307 494 51 N ATOM 40 CA LYS A 6 -0.621 -30.494 1.553 1.00 15.58 C ANISOU 40 CA LYS A 6 2419 1711 1787 289 312 -164 C ATOM 41 C LYS A 6 0.366 -30.976 2.611 1.00 17.15 C ANISOU 41 C LYS A 6 2130 2071 2312 448 440 76 C ATOM 42 O LYS A 6 1.486 -31.398 2.296 1.00 20.94 O ANISOU 42 O LYS A 6 2522 2780 2655 785 496 355 O ATOM 43 CB LYS A 6 -1.203 -31.688 0.798 1.00 17.45 C ANISOU 43 CB LYS A 6 2364 2108 2159 25 299 -204 C ATOM 44 CG LYS A 6 -2.272 -31.295 -0.213 1.00 22.14 C ANISOU 44 CG LYS A 6 2986 2577 2848 -258 -209 -76 C ATOM 45 CD LYS A 6 -2.923 -32.512 -0.850 1.00 31.99 C ANISOU 45 CD LYS A 6 4710 3637 3807 -229 -409 -441 C ATOM 46 CE LYS A 6 -3.874 -32.093 -1.957 1.00 34.63 C ANISOU 46 CE LYS A 6 5117 3794 4247 -534 -820 -221 C ATOM 47 NZ LYS A 6 -4.718 -33.219 -2.470 1.00 38.50 N ANISOU 47 NZ LYS A 6 5400 4619 4608 -831 -805 -718 N ATOM 48 N SER A 7 -0.062 -30.923 3.864 1.00 15.21 N ANISOU 48 N SER A 7 2051 2045 1681 411 226 178 N ATOM 49 CA SER A 7 0.710 -31.418 5.007 1.00 18.01 C ANISOU 49 CA SER A 7 2035 2385 2421 526 156 128 C ATOM 50 C SER A 7 -0.138 -32.469 5.735 1.00 17.90 C ANISOU 50 C SER A 7 2179 2307 2312 661 282 240 C ATOM 51 O SER A 7 -1.133 -32.132 6.379 1.00 16.75 O ANISOU 51 O SER A 7 2173 2048 2142 769 290 136 O ATOM 52 CB SER A 7 1.077 -30.269 5.959 1.00 20.87 C ANISOU 52 CB SER A 7 2421 3028 2479 101 -253 399 C ATOM 53 OG SER A 7 1.808 -29.237 5.299 1.00 23.87 O ANISOU 53 OG SER A 7 2600 3148 3321 -52 -160 200 O ATOM 54 N SER A 8 0.261 -33.738 5.649 1.00 19.55 N ANISOU 54 N SER A 8 2907 2269 2252 649 255 150 N ATOM 55 CA SER A 8 -0.442 -34.816 6.342 1.00 18.88 C ANISOU 55 CA SER A 8 2582 1946 2646 964 129 -67 C ATOM 56 C SER A 8 -0.133 -34.780 7.837 1.00 18.76 C ANISOU 56 C SER A 8 2396 2346 2384 511 -152 5 C ATOM 57 O SER A 8 1.014 -34.559 8.227 1.00 20.94 O ANISOU 57 O SER A 8 2578 2426 2952 531 -216 250 O ATOM 58 CB SER A 8 0.000 -36.173 5.796 1.00 24.09 C ANISOU 58 CB SER A 8 3803 2407 2940 1211 294 -369 C ATOM 59 OG SER A 8 -0.668 -36.430 4.576 1.00 33.85 O ANISOU 59 OG SER A 8 5044 3671 4146 756 -370 -290 O ATOM 60 N LEU A 9 -1.162 -35.010 8.653 1.00 17.05 N ANISOU 60 N LEU A 9 2307 2006 2165 341 -44 5 N ATOM 61 CA LEU A 9 -1.060 -35.021 10.106 1.00 17.38 C ANISOU 61 CA LEU A 9 2562 2185 1856 119 -64 40 C ATOM 62 C LEU A 9 -1.611 -36.326 10.648 1.00 19.58 C ANISOU 62 C LEU A 9 2541 2712 2187 -26 -136 -36 C ATOM 63 O LEU A 9 -2.680 -36.374 11.245 1.00 21.07 O ANISOU 63 O LEU A 9 2242 3398 2365 -216 -274 263 O ATOM 64 CB LEU A 9 -1.843 -33.841 10.701 1.00 17.88 C ANISOU 64 CB LEU A 9 2581 2467 1743 198 -279 -47 C ATOM 65 CG LEU A 9 -1.278 -32.478 10.302 1.00 20.63 C ANISOU 65 CG LEU A 9 3257 2423 2158 838 -477 366 C ATOM 66 CD1 LEU A 9 -2.214 -31.350 10.707 1.00 26.40 C ANISOU 66 CD1 LEU A 9 3696 2651 3683 1296 -94 -654 C ATOM 67 CD2 LEU A 9 0.116 -32.261 10.897 1.00 27.88 C ANISOU 67 CD2 LEU A 9 3275 3300 4016 201 -551 -232 C ATOM 68 N PRO A 10 -0.831 -37.388 10.537 1.00 22.12 N ANISOU 68 N PRO A 10 3386 2202 2813 -87 298 169 N ATOM 69 CA PRO A 10 -1.442 -38.689 10.823 1.00 23.27 C ANISOU 69 CA PRO A 10 3618 2289 2933 -81 479 154 C ATOM 70 C PRO A 10 -1.655 -38.963 12.316 1.00 24.79 C ANISOU 70 C PRO A 10 3903 2756 2760 1 394 -192 C ATOM 71 O PRO A 10 -2.460 -39.838 12.648 1.00 26.26 O ANISOU 71 O PRO A 10 4500 2765 2709 -430 107 -304 O ATOM 72 CB PRO A 10 -0.467 -39.696 10.217 1.00 28.41 C ANISOU 72 CB PRO A 10 4107 2995 3690 226 437 273 C ATOM 73 CG PRO A 10 0.733 -38.928 9.785 1.00 27.32 C ANISOU 73 CG PRO A 10 3675 2525 4178 380 527 0 C ATOM 74 CD PRO A 10 0.562 -37.473 10.092 1.00 23.09 C ANISOU 74 CD PRO A 10 3208 2104 3461 678 58 430 C ATOM 75 N GLU A 11 -0.986 -38.219 13.202 1.00 19.68 N ANISOU 75 N GLU A 11 2754 1941 2781 367 -46 300 N ATOM 76 CA GLU A 11 -1.344 -38.271 14.619 1.00 21.20 C ANISOU 76 CA GLU A 11 2683 2646 2724 441 -54 36 C ATOM 77 C GLU A 11 -2.148 -37.042 15.029 1.00 18.72 C ANISOU 77 C GLU A 11 2478 2480 2155 341 -204 78 C ATOM 78 O GLU A 11 -2.346 -36.760 16.208 1.00 22.31 O ANISOU 78 O GLU A 11 2801 3411 2265 587 -505 65 O ATOM 79 CB GLU A 11 -0.100 -38.450 15.513 1.00 22.90 C ANISOU 79 CB GLU A 11 3083 2937 2678 471 160 137 C ATOM 80 CG GLU A 11 0.590 -39.806 15.290 1.00 27.94 C ANISOU 80 CG GLU A 11 3795 3742 3076 1029 273 376 C ATOM 81 CD GLU A 11 1.725 -40.111 16.268 1.00 38.33 C ANISOU 81 CD GLU A 11 4632 5418 4512 827 321 223 C ATOM 82 OE1 GLU A 11 2.216 -39.184 16.948 1.00 33.05 O ANISOU 82 OE1 GLU A 11 3405 4853 4299 918 448 1294 O ATOM 83 OE2 GLU A 11 2.173 -41.285 16.298 1.00 34.71 O ANISOU 83 OE2 GLU A 11 4672 5376 3137 1400 1881 673 O ATOM 84 N GLY A 12 -2.775 -36.403 14.056 1.00 15.62 N ANISOU 84 N GLY A 12 1969 1990 1974 483 -467 22 N ATOM 85 CA GLY A 12 -3.654 -35.298 14.371 1.00 15.97 C ANISOU 85 CA GLY A 12 2049 1901 2117 140 -297 -217 C ATOM 86 C GLY A 12 -2.927 -34.100 14.929 1.00 16.83 C ANISOU 86 C GLY A 12 1815 2318 2261 109 -319 -207 C ATOM 87 O GLY A 12 -1.710 -33.979 14.816 1.00 20.37 O ANISOU 87 O GLY A 12 2404 2552 2782 42 -271 -731 O ATOM 88 N ILE A 13 -3.704 -33.191 15.495 1.00 16.32 N ANISOU 88 N ILE A 13 2190 1922 2087 -22 -237 -218 N ATOM 89 CA ILE A 13 -3.154 -32.048 16.202 1.00 17.81 C ANISOU 89 CA ILE A 13 2417 2225 2125 -45 145 -236 C ATOM 90 C ILE A 13 -3.825 -31.853 17.547 1.00 16.60 C ANISOU 90 C ILE A 13 2144 2266 1895 -92 -52 -153 C ATOM 91 O ILE A 13 -5.016 -32.113 17.702 1.00 19.65 O ANISOU 91 O ILE A 13 2311 2895 2260 168 -65 -308 O ATOM 92 CB ILE A 13 -3.170 -30.782 15.358 1.00 20.76 C ANISOU 92 CB ILE A 13 2986 2591 2309 47 289 -160 C ATOM 93 CG1 ILE A 13 -4.560 -30.464 14.840 1.00 22.91 C ANISOU 93 CG1 ILE A 13 3584 2394 2724 48 -152 -110 C ATOM 94 CG2 ILE A 13 -2.154 -30.909 14.238 1.00 25.27 C ANISOU 94 CG2 ILE A 13 3629 3463 2509 -169 588 -227 C ATOM 95 CD1 ILE A 13 -4.595 -29.165 14.041 1.00 26.15 C ANISOU 95 CD1 ILE A 13 3577 1958 4399 433 -598 626 C ATOM 96 N ARG A 14 -3.009 -31.554 18.551 1.00 18.39 N ANISOU 96 N ARG A 14 2354 2670 1964 -104 -52 -348 N ATOM 97 CA ARG A 14 -3.479 -31.429 19.928 1.00 19.69 C ANISOU 97 CA ARG A 14 2839 2636 2005 23 -185 -4 C ATOM 98 C ARG A 14 -3.472 -29.935 20.326 1.00 17.16 C ANISOU 98 C ARG A 14 2211 2351 1955 -443 -29 -26 C ATOM 99 O ARG A 14 -2.822 -29.112 19.680 1.00 17.25 O ANISOU 99 O ARG A 14 2315 2363 1874 -350 -90 -71 O ATOM 100 CB ARG A 14 -2.552 -32.237 20.831 1.00 22.31 C ANISOU 100 CB ARG A 14 3314 2769 2391 -313 -477 165 C ATOM 101 CG ARG A 14 -2.491 -33.720 20.463 1.00 30.25 C ANISOU 101 CG ARG A 14 4606 3717 3169 324 -663 116 C ATOM 102 CD ARG A 14 -2.486 -34.605 21.697 1.00 43.10 C ANISOU 102 CD ARG A 14 6308 5694 4374 171 -936 813 C ATOM 103 NE ARG A 14 -1.164 -34.671 22.312 1.00 55.82 N ANISOU 103 NE ARG A 14 6514 7826 6869 381 -659 341 N ATOM 104 CZ ARG A 14 -0.949 -34.805 23.618 1.00 59.66 C ANISOU 104 CZ ARG A 14 7197 8458 7011 158 -536 386 C ATOM 105 NH1 ARG A 14 -1.970 -34.869 24.465 1.00 60.93 N ANISOU 105 NH1 ARG A 14 7165 8464 7522 -55 -393 377 N ATOM 106 NH2 ARG A 14 0.293 -34.854 24.079 1.00 62.92 N ANISOU 106 NH2 ARG A 14 7358 9011 7537 437 -651 268 N ATOM 107 N PRO A 15 -4.240 -29.571 21.358 1.00 16.24 N ANISOU 107 N PRO A 15 2040 2444 1685 -413 -104 -59 N ATOM 108 CA PRO A 15 -4.145 -28.220 21.893 1.00 17.09 C ANISOU 108 CA PRO A 15 2104 2583 1805 -208 145 -40 C ATOM 109 C PRO A 15 -2.676 -27.860 22.152 1.00 15.64 C ANISOU 109 C PRO A 15 1791 2546 1605 -140 112 29 C ATOM 110 O PRO A 15 -1.882 -28.690 22.625 1.00 18.81 O ANISOU 110 O PRO A 15 2195 2731 2217 -313 -264 144 O ATOM 111 CB PRO A 15 -4.930 -28.314 23.200 1.00 17.54 C ANISOU 111 CB PRO A 15 2091 2817 1756 -380 132 -44 C ATOM 112 CG PRO A 15 -5.963 -29.393 22.898 1.00 19.07 C ANISOU 112 CG PRO A 15 2444 2817 1982 -272 -220 103 C ATOM 113 CD PRO A 15 -5.174 -30.410 22.130 1.00 17.13 C ANISOU 113 CD PRO A 15 2249 2505 1754 -334 26 332 C ATOM 114 N GLY A 16 -2.291 -26.670 21.714 1.00 16.98 N ANISOU 114 N GLY A 16 2125 2445 1881 -498 31 -184 N ATOM 115 CA GLY A 16 -0.897 -26.270 21.778 1.00 18.87 C ANISOU 115 CA GLY A 16 2315 2601 2252 -528 177 -81 C ATOM 116 C GLY A 16 -0.101 -26.622 20.544 1.00 17.10 C ANISOU 116 C GLY A 16 1852 2228 2416 -520 -81 -255 C ATOM 117 O GLY A 16 1.006 -27.140 20.655 1.00 22.89 O ANISOU 117 O GLY A 16 2500 2893 3303 -233 -138 -830 O ATOM 118 N THR A 17 -0.742 -26.495 19.389 1.00 19.04 N ANISOU 118 N THR A 17 2042 3167 2024 -428 263 -42 N ATOM 119 CA THR A 17 -0.098 -26.679 18.099 1.00 18.74 C ANISOU 119 CA THR A 17 2243 2825 2053 -200 491 93 C ATOM 120 C THR A 17 -0.164 -25.399 17.299 1.00 17.50 C ANISOU 120 C THR A 17 2002 2663 1983 -8 156 -67 C ATOM 121 O THR A 17 -1.194 -24.726 17.259 1.00 16.98 O ANISOU 121 O THR A 17 1874 2812 1766 -84 198 -73 O ATOM 122 CB THR A 17 -0.825 -27.765 17.303 1.00 20.41 C ANISOU 122 CB THR A 17 3026 2742 1985 -309 569 -66 C ATOM 123 OG1 THR A 17 -0.650 -29.026 17.964 1.00 28.51 O ANISOU 123 OG1 THR A 17 3948 2978 3905 175 1506 545 O ATOM 124 CG2 THR A 17 -0.294 -27.869 15.867 1.00 26.33 C ANISOU 124 CG2 THR A 17 4247 3059 2698 -749 1106 -543 C ATOM 125 N VAL A 18 0.921 -25.088 16.607 1.00 16.85 N ANISOU 125 N VAL A 18 1978 2484 1939 -83 152 114 N ATOM 126 CA VAL A 18 1.004 -23.864 15.823 1.00 15.28 C ANISOU 126 CA VAL A 18 1754 2181 1869 -104 -54 -174 C ATOM 127 C VAL A 18 1.229 -24.199 14.348 1.00 14.24 C ANISOU 127 C VAL A 18 1804 1820 1786 72 -233 -312 C ATOM 128 O VAL A 18 2.179 -24.910 14.014 1.00 15.47 O ANISOU 128 O VAL A 18 1742 2257 1876 98 110 -119 O ATOM 129 CB VAL A 18 2.152 -22.980 16.318 1.00 16.29 C ANISOU 129 CB VAL A 18 1864 2622 1702 -321 127 -287 C ATOM 130 CG1 VAL A 18 2.352 -21.822 15.377 1.00 18.43 C ANISOU 130 CG1 VAL A 18 2438 2334 2230 -372 -496 -619 C ATOM 131 CG2 VAL A 18 1.853 -22.482 17.713 1.00 20.45 C ANISOU 131 CG2 VAL A 18 2233 3762 1775 186 -289 -717 C ATOM 132 N LEU A 19 0.349 -23.709 13.469 1.00 14.13 N ANISOU 132 N LEU A 19 1715 2028 1623 -57 -76 -124 N ATOM 133 CA LEU A 19 0.555 -23.793 12.030 1.00 13.18 C ANISOU 133 CA LEU A 19 1537 1962 1508 -73 -148 -165 C ATOM 134 C LEU A 19 1.074 -22.427 11.592 1.00 14.23 C ANISOU 134 C LEU A 19 1747 2026 1632 3 -45 -209 C ATOM 135 O LEU A 19 0.402 -21.411 11.806 1.00 14.49 O ANISOU 135 O LEU A 19 1640 2032 1832 86 15 -210 O ATOM 136 CB LEU A 19 -0.781 -24.117 11.341 1.00 14.82 C ANISOU 136 CB LEU A 19 1843 2399 1387 25 27 -259 C ATOM 137 CG LEU A 19 -0.934 -23.970 9.842 1.00 18.50 C ANISOU 137 CG LEU A 19 2236 2808 1984 -99 -82 -272 C ATOM 138 CD1 LEU A 19 0.069 -24.759 9.050 1.00 22.61 C ANISOU 138 CD1 LEU A 19 2533 3083 2974 26 264 -742 C ATOM 139 CD2 LEU A 19 -2.370 -24.359 9.472 1.00 19.52 C ANISOU 139 CD2 LEU A 19 2228 2614 2572 -165 -366 -437 C ATOM 140 N ARG A 20 2.291 -22.399 11.045 1.00 12.87 N ANISOU 140 N ARG A 20 1475 1815 1599 -212 28 -93 N ATOM 141 CA ARG A 20 2.936 -21.149 10.662 1.00 12.97 C ANISOU 141 CA ARG A 20 1719 1688 1519 48 -102 -195 C ATOM 142 C ARG A 20 3.003 -21.101 9.143 1.00 12.36 C ANISOU 142 C ARG A 20 1328 1731 1635 -47 173 -187 C ATOM 143 O ARG A 20 3.645 -21.963 8.518 1.00 12.81 O ANISOU 143 O ARG A 20 1460 1728 1675 185 37 -122 O ATOM 144 CB ARG A 20 4.346 -21.092 11.252 1.00 13.78 C ANISOU 144 CB ARG A 20 1649 1868 1719 -305 -66 -260 C ATOM 145 CG ARG A 20 5.058 -19.758 11.026 1.00 14.12 C ANISOU 145 CG ARG A 20 1941 1809 1615 -305 52 -90 C ATOM 146 CD ARG A 20 6.508 -19.776 11.485 1.00 16.87 C ANISOU 146 CD ARG A 20 1636 2492 2280 -245 -154 -355 C ATOM 147 NE ARG A 20 7.307 -20.548 10.543 1.00 16.51 N ANISOU 147 NE ARG A 20 1682 2235 2354 -80 -143 -149 N ATOM 148 CZ ARG A 20 8.577 -20.912 10.726 1.00 17.07 C ANISOU 148 CZ ARG A 20 1877 2409 2197 -159 140 -37 C ATOM 149 NH1 ARG A 20 9.203 -20.633 11.857 1.00 18.39 N ANISOU 149 NH1 ARG A 20 1866 2522 2596 -415 -108 -338 N ATOM 150 NH2 ARG A 20 9.213 -21.578 9.770 1.00 20.72 N ANISOU 150 NH2 ARG A 20 2264 2498 3108 -62 58 -350 N ATOM 151 N ILE A 21 2.356 -20.104 8.548 1.00 12.62 N ANISOU 151 N ILE A 21 1600 1600 1595 -92 63 -23 N ATOM 152 CA ILE A 21 2.288 -19.995 7.089 1.00 12.95 C ANISOU 152 CA ILE A 21 1612 1715 1593 5 28 -214 C ATOM 153 C ILE A 21 2.901 -18.684 6.653 1.00 12.36 C ANISOU 153 C ILE A 21 1477 1604 1615 151 96 -145 C ATOM 154 O ILE A 21 2.445 -17.623 7.079 1.00 13.67 O ANISOU 154 O ILE A 21 1592 1719 1883 21 238 -190 O ATOM 155 CB ILE A 21 0.838 -20.086 6.580 1.00 13.96 C ANISOU 155 CB ILE A 21 1758 1652 1893 -124 -83 -164 C ATOM 156 CG1 ILE A 21 0.228 -21.390 7.087 1.00 17.17 C ANISOU 156 CG1 ILE A 21 2211 2342 1971 -371 7 -169 C ATOM 157 CG2 ILE A 21 0.798 -20.022 5.045 1.00 14.40 C ANISOU 157 CG2 ILE A 21 1999 1722 1747 114 -98 -144 C ATOM 158 CD1 ILE A 21 -1.190 -21.559 6.735 1.00 24.36 C ANISOU 158 CD1 ILE A 21 2873 2963 3417 31 -202 -28 C ATOM 159 N ARG A 22 3.926 -18.750 5.805 1.00 12.03 N ANISOU 159 N ARG A 22 1481 1670 1417 -141 93 -253 N ATOM 160 CA ARG A 22 4.576 -17.543 5.281 1.00 11.77 C ANISOU 160 CA ARG A 22 1436 1663 1373 71 146 -35 C ATOM 161 C ARG A 22 4.494 -17.559 3.764 1.00 10.89 C ANISOU 161 C ARG A 22 1327 1406 1402 133 128 -37 C ATOM 162 O ARG A 22 4.734 -18.575 3.152 1.00 11.98 O ANISOU 162 O ARG A 22 1416 1583 1552 263 40 -269 O ATOM 163 CB ARG A 22 6.041 -17.471 5.737 1.00 12.37 C ANISOU 163 CB ARG A 22 1499 1699 1501 -4 49 -26 C ATOM 164 CG ARG A 22 6.177 -17.320 7.235 1.00 14.13 C ANISOU 164 CG ARG A 22 1659 1947 1760 42 -207 -92 C ATOM 165 CD ARG A 22 7.601 -17.621 7.695 1.00 15.76 C ANISOU 165 CD ARG A 22 1518 2522 1946 230 -280 -371 C ATOM 166 NE ARG A 22 7.763 -17.272 9.102 1.00 14.99 N ANISOU 166 NE ARG A 22 1697 2079 1919 66 -446 19 N ATOM 167 CZ ARG A 22 8.887 -17.464 9.784 1.00 17.14 C ANISOU 167 CZ ARG A 22 1792 2264 2454 81 -151 -62 C ATOM 168 NH1 ARG A 22 9.856 -18.184 9.242 1.00 19.86 N ANISOU 168 NH1 ARG A 22 1664 3000 2880 191 -410 52 N ATOM 169 NH2 ARG A 22 8.993 -17.047 11.037 1.00 20.16 N ANISOU 169 NH2 ARG A 22 2017 3051 2590 -517 -162 -51 N ATOM 170 N GLY A 23 4.230 -16.417 3.157 1.00 11.23 N ANISOU 170 N GLY A 23 1428 1609 1230 158 22 33 N ATOM 171 CA GLY A 23 4.198 -16.388 1.692 1.00 12.67 C ANISOU 171 CA GLY A 23 1796 1569 1447 290 -146 76 C ATOM 172 C GLY A 23 3.934 -15.007 1.159 1.00 11.81 C ANISOU 172 C GLY A 23 1278 1524 1685 157 -73 -128 C ATOM 173 O GLY A 23 3.988 -14.021 1.897 1.00 13.48 O ANISOU 173 O GLY A 23 1744 1664 1713 331 -42 -118 O ATOM 174 N LEU A 24 3.663 -14.965 -0.146 1.00 12.02 N ANISOU 174 N LEU A 24 1475 1470 1620 108 -212 59 N ATOM 175 CA LEU A 24 3.405 -13.716 -0.837 1.00 12.28 C ANISOU 175 CA LEU A 24 1386 1701 1576 141 -212 65 C ATOM 176 C LEU A 24 1.980 -13.786 -1.401 1.00 11.69 C ANISOU 176 C LEU A 24 1386 1498 1557 -99 -146 -76 C ATOM 177 O LEU A 24 1.589 -14.789 -2.008 1.00 12.42 O ANISOU 177 O LEU A 24 1413 1495 1811 -34 -89 -152 O ATOM 178 CB LEU A 24 4.399 -13.565 -2.011 1.00 12.22 C ANISOU 178 CB LEU A 24 1451 1521 1670 9 -39 -17 C ATOM 179 CG LEU A 24 4.169 -12.395 -2.965 1.00 12.41 C ANISOU 179 CG LEU A 24 1518 1581 1616 118 336 43 C ATOM 180 CD1 LEU A 24 4.321 -11.069 -2.235 1.00 14.22 C ANISOU 180 CD1 LEU A 24 1764 1652 1984 95 143 -167 C ATOM 181 CD2 LEU A 24 5.073 -12.440 -4.166 1.00 14.59 C ANISOU 181 CD2 LEU A 24 1449 2045 2046 186 459 188 C ATOM 182 N VAL A 25 1.204 -12.711 -1.245 1.00 11.56 N ANISOU 182 N VAL A 25 1088 1560 1744 68 -149 -38 N ATOM 183 CA VAL A 25 -0.027 -12.559 -2.041 1.00 11.82 C ANISOU 183 CA VAL A 25 1187 1611 1693 112 -119 -51 C ATOM 184 C VAL A 25 0.381 -11.950 -3.372 1.00 11.16 C ANISOU 184 C VAL A 25 1282 1360 1596 38 -47 30 C ATOM 185 O VAL A 25 0.868 -10.832 -3.385 1.00 12.60 O ANISOU 185 O VAL A 25 1309 1605 1872 -21 -67 24 O ATOM 186 CB VAL A 25 -1.048 -11.662 -1.338 1.00 11.62 C ANISOU 186 CB VAL A 25 1210 1574 1628 21 -53 -98 C ATOM 187 CG1 VAL A 25 -2.280 -11.518 -2.213 1.00 13.68 C ANISOU 187 CG1 VAL A 25 1248 1772 2176 102 -144 7 C ATOM 188 CG2 VAL A 25 -1.451 -12.275 -0.002 1.00 14.70 C ANISOU 188 CG2 VAL A 25 1658 1893 2032 335 23 -91 C ATOM 189 N PRO A 26 0.270 -12.708 -4.476 1.00 11.90 N ANISOU 189 N PRO A 26 1361 1468 1692 8 41 31 N ATOM 190 CA PRO A 26 0.812 -12.198 -5.732 1.00 12.78 C ANISOU 190 CA PRO A 26 1464 1720 1672 198 -16 68 C ATOM 191 C PRO A 26 -0.079 -11.094 -6.329 1.00 13.10 C ANISOU 191 C PRO A 26 1340 1735 1899 51 -74 84 C ATOM 192 O PRO A 26 -1.189 -10.824 -5.847 1.00 13.00 O ANISOU 192 O PRO A 26 1386 1755 1795 46 -130 121 O ATOM 193 CB PRO A 26 0.850 -13.438 -6.633 1.00 13.83 C ANISOU 193 CB PRO A 26 1664 1778 1809 135 60 8 C ATOM 194 CG PRO A 26 -0.312 -14.268 -6.112 1.00 13.24 C ANISOU 194 CG PRO A 26 1953 1651 1425 -97 31 -85 C ATOM 195 CD PRO A 26 -0.285 -14.072 -4.613 1.00 12.11 C ANISOU 195 CD PRO A 26 1634 1560 1407 -247 -146 83 C ATOM 196 N PRO A 27 0.448 -10.385 -7.327 1.00 13.38 N ANISOU 196 N PRO A 27 1485 1718 1878 126 42 209 N ATOM 197 CA PRO A 27 -0.193 -9.145 -7.771 1.00 15.37 C ANISOU 197 CA PRO A 27 1453 1933 2452 6 67 528 C ATOM 198 C PRO A 27 -1.626 -9.295 -8.250 1.00 17.56 C ANISOU 198 C PRO A 27 1999 2416 2255 -65 83 300 C ATOM 199 O PRO A 27 -2.412 -8.341 -8.128 1.00 18.91 O ANISOU 199 O PRO A 27 2034 2328 2822 304 203 228 O ATOM 200 CB PRO A 27 0.675 -8.696 -8.944 1.00 17.37 C ANISOU 200 CB PRO A 27 1779 2372 2446 127 361 636 C ATOM 201 CG PRO A 27 1.961 -9.336 -8.740 1.00 17.03 C ANISOU 201 CG PRO A 27 1952 2245 2272 353 -4 582 C ATOM 202 CD PRO A 27 1.798 -10.542 -7.899 1.00 15.67 C ANISOU 202 CD PRO A 27 1798 2049 2104 47 448 234 C ATOM 203 N ASN A 28 -1.976 -10.433 -8.848 1.00 16.14 N ANISOU 203 N ASN A 28 1847 2259 2024 -540 -176 334 N ATOM 204 CA ASN A 28 -3.332 -10.539 -9.406 1.00 18.20 C ANISOU 204 CA ASN A 28 2092 2671 2149 -165 -204 250 C ATOM 205 C ASN A 28 -4.266 -11.441 -8.592 1.00 17.19 C ANISOU 205 C ASN A 28 2001 2390 2141 -179 -323 398 C ATOM 206 O ASN A 28 -5.308 -11.880 -9.073 1.00 19.42 O ANISOU 206 O ASN A 28 2290 2848 2240 -588 -414 96 O ATOM 207 CB ASN A 28 -3.298 -10.897 -10.891 1.00 20.69 C ANISOU 207 CB ASN A 28 2849 2670 2339 -213 -87 218 C ATOM 208 CG ASN A 28 -2.807 -9.742 -11.742 1.00 21.88 C ANISOU 208 CG ASN A 28 2802 3150 2358 -84 -380 232 C ATOM 209 OD1 ASN A 28 -3.429 -8.686 -11.784 1.00 25.34 O ANISOU 209 OD1 ASN A 28 3090 2981 3557 -78 301 1030 O ATOM 210 ND2 ASN A 28 -1.660 -9.915 -12.371 1.00 25.41 N ANISOU 210 ND2 ASN A 28 2721 3916 3016 -156 -507 -65 N ATOM 211 N ALA A 29 -3.895 -11.662 -7.333 1.00 15.44 N ANISOU 211 N ALA A 29 1918 2071 1877 -156 -143 452 N ATOM 212 CA ALA A 29 -4.607 -12.588 -6.467 1.00 13.33 C ANISOU 212 CA ALA A 29 1436 1934 1692 -218 94 221 C ATOM 213 C ALA A 29 -6.068 -12.218 -6.263 1.00 13.00 C ANISOU 213 C ALA A 29 1658 1521 1758 208 -102 25 C ATOM 214 O ALA A 29 -6.414 -11.058 -5.998 1.00 15.87 O ANISOU 214 O ALA A 29 1756 1777 2494 -41 -375 -42 O ATOM 215 CB ALA A 29 -3.925 -12.685 -5.103 1.00 12.83 C ANISOU 215 CB ALA A 29 1409 1954 1510 -37 -179 -115 C ATOM 216 N SER A 30 -6.921 -13.233 -6.328 1.00 13.34 N ANISOU 216 N SER A 30 1514 1995 1557 -78 96 85 N ATOM 217 CA SER A 30 -8.316 -13.058 -5.932 1.00 13.26 C ANISOU 217 CA SER A 30 1293 1863 1880 -60 58 -78 C ATOM 218 C SER A 30 -8.557 -13.499 -4.495 1.00 12.64 C ANISOU 218 C SER A 30 1413 1617 1773 -3 -133 -39 C ATOM 219 O SER A 30 -9.157 -12.773 -3.719 1.00 13.49 O ANISOU 219 O SER A 30 1520 1525 2078 42 -144 -80 O ATOM 220 CB SER A 30 -9.235 -13.784 -6.898 1.00 16.73 C ANISOU 220 CB SER A 30 1945 2383 2027 -316 -317 83 C ATOM 221 OG SER A 30 -9.191 -13.118 -8.154 1.00 23.97 O ANISOU 221 OG SER A 30 2568 3891 2646 -113 -177 302 O ATOM 222 N ARG A 31 -8.179 -14.724 -4.163 1.00 11.82 N ANISOU 222 N ARG A 31 1415 1378 1694 27 120 134 N ATOM 223 CA ARG A 31 -8.402 -15.242 -2.809 1.00 12.04 C ANISOU 223 CA ARG A 31 1314 1445 1815 49 57 191 C ATOM 224 C ARG A 31 -7.538 -16.493 -2.626 1.00 10.65 C ANISOU 224 C ARG A 31 1311 1291 1445 29 -3 0 C ATOM 225 O ARG A 31 -7.105 -17.094 -3.623 1.00 11.66 O ANISOU 225 O ARG A 31 1462 1500 1467 120 31 -208 O ATOM 226 CB ARG A 31 -9.891 -15.570 -2.580 1.00 13.41 C ANISOU 226 CB ARG A 31 1255 1847 1993 -141 231 20 C ATOM 227 CG ARG A 31 -10.537 -16.390 -3.690 1.00 14.05 C ANISOU 227 CG ARG A 31 1158 1904 2275 -326 -175 -183 C ATOM 228 CD ARG A 31 -12.027 -16.573 -3.403 1.00 14.72 C ANISOU 228 CD ARG A 31 1483 1518 2589 143 81 16 C ATOM 229 NE ARG A 31 -12.723 -15.288 -3.463 1.00 14.57 N ANISOU 229 NE ARG A 31 1157 1767 2611 13 -60 -237 N ATOM 230 CZ ARG A 31 -14.018 -15.129 -3.186 1.00 13.15 C ANISOU 230 CZ ARG A 31 1165 1615 2217 72 25 -263 C ATOM 231 NH1 ARG A 31 -14.780 -16.171 -2.833 1.00 14.28 N ANISOU 231 NH1 ARG A 31 1649 1611 2163 -144 -149 -156 N ATOM 232 NH2 ARG A 31 -14.557 -13.922 -3.300 1.00 13.57 N ANISOU 232 NH2 ARG A 31 1415 1601 2139 -53 -103 52 N ATOM 233 N PHE A 32 -7.244 -16.850 -1.369 1.00 10.52 N ANISOU 233 N PHE A 32 1262 1280 1454 -57 15 62 N ATOM 234 CA PHE A 32 -6.534 -18.084 -1.083 1.00 10.64 C ANISOU 234 CA PHE A 32 1236 1477 1328 0 -113 -95 C ATOM 235 C PHE A 32 -7.092 -18.661 0.207 1.00 10.82 C ANISOU 235 C PHE A 32 1364 1302 1441 50 -34 -122 C ATOM 236 O PHE A 32 -7.920 -18.034 0.889 1.00 11.07 O ANISOU 236 O PHE A 32 1287 1389 1527 50 49 -82 O ATOM 237 CB PHE A 32 -4.998 -17.837 -1.058 1.00 12.20 C ANISOU 237 CB PHE A 32 1500 1568 1568 0 -8 -114 C ATOM 238 CG PHE A 32 -4.482 -17.126 0.172 1.00 11.34 C ANISOU 238 CG PHE A 32 1303 1454 1548 -179 95 -108 C ATOM 239 CD1 PHE A 32 -4.442 -15.728 0.224 1.00 13.90 C ANISOU 239 CD1 PHE A 32 1455 1828 1996 -165 313 -386 C ATOM 240 CD2 PHE A 32 -4.038 -17.846 1.282 1.00 14.27 C ANISOU 240 CD2 PHE A 32 1374 2282 1765 -76 98 -256 C ATOM 241 CE1 PHE A 32 -3.901 -15.078 1.353 1.00 15.14 C ANISOU 241 CE1 PHE A 32 1368 2135 2248 -71 358 -651 C ATOM 242 CE2 PHE A 32 -3.480 -17.185 2.403 1.00 16.63 C ANISOU 242 CE2 PHE A 32 1501 2635 2182 -181 40 -433 C ATOM 243 CZ PHE A 32 -3.405 -15.810 2.409 1.00 15.97 C ANISOU 243 CZ PHE A 32 1495 2270 2302 -186 248 -673 C ATOM 244 N HIS A 33 -6.684 -19.873 0.533 1.00 11.61 N ANISOU 244 N HIS A 33 1584 1298 1529 67 76 -34 N ATOM 245 CA HIS A 33 -7.258 -20.530 1.692 1.00 12.06 C ANISOU 245 CA HIS A 33 1435 1509 1638 -32 4 109 C ATOM 246 C HIS A 33 -6.244 -21.379 2.456 1.00 12.33 C ANISOU 246 C HIS A 33 1638 1287 1759 188 92 26 C ATOM 247 O HIS A 33 -5.257 -21.902 1.876 1.00 13.22 O ANISOU 247 O HIS A 33 1736 1407 1880 105 179 -58 O ATOM 248 CB HIS A 33 -8.443 -21.424 1.278 1.00 15.34 C ANISOU 248 CB HIS A 33 1764 2018 2044 -140 114 -43 C ATOM 249 CG HIS A 33 -8.100 -22.401 0.199 1.00 16.54 C ANISOU 249 CG HIS A 33 2270 1865 2146 -553 -367 -21 C ATOM 250 ND1 HIS A 33 -8.312 -22.139 -1.137 1.00 18.63 N ANISOU 250 ND1 HIS A 33 2626 2360 2090 -371 -431 -156 N ATOM 251 CD2 HIS A 33 -7.446 -23.586 0.251 1.00 19.08 C ANISOU 251 CD2 HIS A 33 2860 1749 2640 -429 283 -401 C ATOM 252 CE1 HIS A 33 -7.870 -23.160 -1.857 1.00 22.44 C ANISOU 252 CE1 HIS A 33 3399 2713 2411 -473 -659 -104 C ATOM 253 NE2 HIS A 33 -7.305 -24.033 -1.042 1.00 22.46 N ANISOU 253 NE2 HIS A 33 2827 2447 3256 -313 -318 -709 N ATOM 254 N VAL A 34 -6.541 -21.549 3.744 1.00 11.67 N ANISOU 254 N VAL A 34 1519 1421 1494 190 -22 -68 N ATOM 255 CA VAL A 34 -5.858 -22.522 4.600 1.00 11.74 C ANISOU 255 CA VAL A 34 1367 1440 1651 214 -34 -10 C ATOM 256 C VAL A 34 -6.953 -23.388 5.181 1.00 11.43 C ANISOU 256 C VAL A 34 1435 1270 1636 143 136 -72 C ATOM 257 O VAL A 34 -7.831 -22.866 5.875 1.00 13.62 O ANISOU 257 O VAL A 34 1621 1754 1799 260 230 -92 O ATOM 258 CB VAL A 34 -5.059 -21.838 5.743 1.00 13.45 C ANISOU 258 CB VAL A 34 1525 1727 1856 8 -41 -55 C ATOM 259 CG1 VAL A 34 -4.412 -22.889 6.659 1.00 14.45 C ANISOU 259 CG1 VAL A 34 1822 2081 1585 164 -146 -39 C ATOM 260 CG2 VAL A 34 -4.015 -20.885 5.165 1.00 14.46 C ANISOU 260 CG2 VAL A 34 1627 1657 2206 33 214 -40 C ATOM 261 N ASN A 35 -6.934 -24.691 4.880 1.00 11.13 N ANISOU 261 N ASN A 35 1519 1229 1479 78 122 -9 N ATOM 262 CA ASN A 35 -7.974 -25.600 5.339 1.00 11.69 C ANISOU 262 CA ASN A 35 1429 1500 1511 115 -117 85 C ATOM 263 C ASN A 35 -7.388 -26.638 6.293 1.00 10.27 C ANISOU 263 C ASN A 35 1149 1443 1311 196 -47 37 C ATOM 264 O ASN A 35 -6.342 -27.235 5.973 1.00 12.51 O ANISOU 264 O ASN A 35 1547 1649 1555 345 270 29 O ATOM 265 CB ASN A 35 -8.623 -26.332 4.157 1.00 12.90 C ANISOU 265 CB ASN A 35 1599 1738 1562 231 -194 21 C ATOM 266 CG ASN A 35 -9.371 -25.404 3.258 1.00 13.69 C ANISOU 266 CG ASN A 35 2086 1481 1630 472 -93 -239 C ATOM 267 OD1 ASN A 35 -9.762 -24.310 3.686 1.00 15.67 O ANISOU 267 OD1 ASN A 35 2103 1890 1959 604 -119 -41 O ATOM 268 ND2 ASN A 35 -9.473 -25.756 1.982 1.00 16.76 N ANISOU 268 ND2 ASN A 35 2582 1938 1847 277 -96 -293 N ATOM 269 N LEU A 36 -8.087 -26.908 7.394 1.00 9.93 N ANISOU 269 N LEU A 36 1278 1201 1293 39 65 81 N ATOM 270 CA LEU A 36 -7.782 -28.032 8.279 1.00 10.87 C ANISOU 270 CA LEU A 36 1387 1416 1324 127 10 -91 C ATOM 271 C LEU A 36 -8.877 -29.063 8.045 1.00 11.05 C ANISOU 271 C LEU A 36 1340 1366 1490 158 -45 -153 C ATOM 272 O LEU A 36 -10.049 -28.797 8.336 1.00 12.28 O ANISOU 272 O LEU A 36 1468 1462 1735 56 84 7 O ATOM 273 CB LEU A 36 -7.751 -27.586 9.759 1.00 12.63 C ANISOU 273 CB LEU A 36 1637 1826 1335 35 -71 -195 C ATOM 274 CG LEU A 36 -6.529 -26.784 10.215 1.00 13.08 C ANISOU 274 CG LEU A 36 1827 1785 1358 -52 -62 -348 C ATOM 275 CD1 LEU A 36 -6.213 -25.604 9.360 1.00 18.31 C ANISOU 275 CD1 LEU A 36 2222 2743 1991 -263 -286 -252 C ATOM 276 CD2 LEU A 36 -6.675 -26.397 11.664 1.00 14.36 C ANISOU 276 CD2 LEU A 36 1781 2290 1383 -211 -171 -164 C ATOM 277 N LEU A 37 -8.473 -30.207 7.516 1.00 12.40 N ANISOU 277 N LEU A 37 1686 1334 1689 53 -71 -75 N ATOM 278 CA LEU A 37 -9.380 -31.175 6.912 1.00 12.09 C ANISOU 278 CA LEU A 37 1923 1375 1295 132 -89 -192 C ATOM 279 C LEU A 37 -9.323 -32.512 7.649 1.00 11.92 C ANISOU 279 C LEU A 37 1748 1236 1542 138 14 -53 C ATOM 280 O LEU A 37 -8.327 -32.873 8.280 1.00 13.96 O ANISOU 280 O LEU A 37 1604 1801 1899 285 -301 203 O ATOM 281 CB LEU A 37 -9.023 -31.423 5.429 1.00 13.32 C ANISOU 281 CB LEU A 37 2248 1469 1344 216 41 -139 C ATOM 282 CG LEU A 37 -9.067 -30.164 4.561 1.00 14.81 C ANISOU 282 CG LEU A 37 2309 1602 1716 166 -98 165 C ATOM 283 CD1 LEU A 37 -8.449 -30.401 3.216 1.00 21.91 C ANISOU 283 CD1 LEU A 37 3578 2680 2065 80 524 265 C ATOM 284 CD2 LEU A 37 -10.473 -29.600 4.450 1.00 19.46 C ANISOU 284 CD2 LEU A 37 2405 2447 2539 -211 -620 431 C HETATM 285 N CSX A 38 -10.427 -33.251 7.538 1.00 13.09 N ANISOU 285 N CSX A 38 1862 1533 1576 48 -93 30 N HETATM 286 CA CSX A 38 -10.574 -34.539 8.236 1.00 15.00 C ANISOU 286 CA CSX A 38 2374 1350 1974 188 26 174 C HETATM 287 CB CSX A 38 -12.061 -34.806 8.497 1.00 17.06 C ANISOU 287 CB CSX A 38 2555 1602 2322 267 117 363 C HETATM 288 SG CSX A 38 -12.794 -33.690 9.638 1.00 23.07 S ANISOU 288 SG CSX A 38 2825 2799 3141 427 44 106 S HETATM 289 C CSX A 38 -9.986 -35.708 7.475 1.00 15.05 C ANISOU 289 C CSX A 38 2328 1877 1512 356 -80 244 C HETATM 290 O CSX A 38 -9.673 -36.736 8.058 1.00 15.97 O ANISOU 290 O CSX A 38 2469 1612 1985 211 -175 149 O HETATM 291 OD CSX A 38 -11.881 -32.486 10.117 1.00 26.48 O ANISOU 291 OD CSX A 38 3403 3634 3023 1323 682 975 O ATOM 292 N GLY A 39 -9.743 -35.534 6.178 1.00 15.55 N ANISOU 292 N GLY A 39 2705 1354 1847 373 238 -17 N ATOM 293 CA GLY A 39 -9.212 -36.619 5.342 1.00 17.78 C ANISOU 293 CA GLY A 39 2990 2066 1697 361 200 72 C ATOM 294 C GLY A 39 -8.706 -36.127 3.996 1.00 17.24 C ANISOU 294 C GLY A 39 2873 1848 1829 437 212 -105 C ATOM 295 O GLY A 39 -8.848 -34.938 3.687 1.00 18.73 O ANISOU 295 O GLY A 39 3306 1655 2156 190 202 103 O ATOM 296 N GLU A 40 -8.094 -37.025 3.220 1.00 18.12 N ANISOU 296 N GLU A 40 2829 2240 1815 394 284 -65 N ATOM 297 CA GLU A 40 -7.464 -36.676 1.942 1.00 19.14 C ANISOU 297 CA GLU A 40 2929 2310 2032 281 254 -57 C ATOM 298 C GLU A 40 -8.466 -36.558 0.790 1.00 20.05 C ANISOU 298 C GLU A 40 3259 2108 2250 218 82 0 C ATOM 299 O GLU A 40 -8.106 -36.153 -0.332 1.00 23.49 O ANISOU 299 O GLU A 40 3833 2714 2377 392 343 -24 O ATOM 300 CB GLU A 40 -6.385 -37.693 1.573 1.00 20.71 C ANISOU 300 CB GLU A 40 3132 2333 2403 361 289 -133 C ATOM 301 CG GLU A 40 -5.188 -37.714 2.485 1.00 25.28 C ANISOU 301 CG GLU A 40 3487 2835 3283 377 395 145 C ATOM 302 CD GLU A 40 -4.377 -38.992 2.292 1.00 25.80 C ANISOU 302 CD GLU A 40 3611 3045 3145 854 -201 -49 C ATOM 303 OE1 GLU A 40 -4.508 -39.621 1.215 1.00 31.59 O ANISOU 303 OE1 GLU A 40 4836 3419 3747 686 627 73 O ATOM 304 OE2 GLU A 40 -3.772 -39.466 3.274 1.00 29.84 O ANISOU 304 OE2 GLU A 40 4774 3222 3340 370 -637 -200 O ATOM 305 N GLU A 41 -9.672 -37.056 1.011 1.00 21.01 N ANISOU 305 N GLU A 41 3330 2323 2327 140 -31 -429 N ATOM 306 CA GLU A 41 -10.707 -37.081 -0.019 1.00 21.86 C ANISOU 306 CA GLU A 41 3702 2230 2373 18 -171 -273 C ATOM 307 C GLU A 41 -11.061 -35.671 -0.504 1.00 21.04 C ANISOU 307 C GLU A 41 3625 2552 1817 316 -432 -148 C ATOM 308 O GLU A 41 -11.066 -34.723 0.285 1.00 20.60 O ANISOU 308 O GLU A 41 3566 2249 2011 118 33 -248 O ATOM 309 CB GLU A 41 -11.956 -37.787 0.538 1.00 22.84 C ANISOU 309 CB GLU A 41 3537 2367 2772 -128 13 -524 C ATOM 310 CG GLU A 41 -12.708 -37.027 1.664 1.00 24.51 C ANISOU 310 CG GLU A 41 3747 2712 2854 23 115 -50 C ATOM 311 CD GLU A 41 -12.174 -37.294 3.080 1.00 22.11 C ANISOU 311 CD GLU A 41 3551 1982 2865 393 54 273 C ATOM 312 OE1 GLU A 41 -11.107 -37.947 3.243 1.00 21.67 O ANISOU 312 OE1 GLU A 41 3490 1553 3190 22 -133 4 O ATOM 313 OE2 GLU A 41 -12.811 -36.806 4.048 1.00 23.14 O ANISOU 313 OE2 GLU A 41 3379 2008 3404 259 226 303 O ATOM 314 N GLN A 42 -11.386 -35.516 -1.786 1.00 23.26 N ANISOU 314 N GLN A 42 4166 2984 1686 323 -40 -127 N ATOM 315 CA GLN A 42 -11.845 -34.215 -2.258 1.00 24.46 C ANISOU 315 CA GLN A 42 4011 3222 2062 263 -249 -5 C ATOM 316 C GLN A 42 -13.184 -33.859 -1.610 1.00 23.29 C ANISOU 316 C GLN A 42 3762 2938 2147 199 -602 269 C ATOM 317 O GLN A 42 -14.030 -34.715 -1.446 1.00 25.77 O ANISOU 317 O GLN A 42 3730 3100 2961 -201 -856 99 O ATOM 318 CB GLN A 42 -11.936 -34.202 -3.787 1.00 28.44 C ANISOU 318 CB GLN A 42 4644 3739 2420 332 -353 102 C ATOM 319 CG GLN A 42 -10.608 -33.859 -4.471 1.00 38.33 C ANISOU 319 CG GLN A 42 5540 4889 4133 -135 -150 222 C ATOM 320 CD GLN A 42 -10.098 -32.478 -4.077 1.00 46.12 C ANISOU 320 CD GLN A 42 6416 5388 5719 -615 -151 610 C ATOM 321 OE1 GLN A 42 -9.021 -32.344 -3.487 1.00 49.38 O ANISOU 321 OE1 GLN A 42 6186 6268 6305 -1106 -142 731 O ATOM 322 NE2 GLN A 42 -10.932 -31.466 -4.280 1.00 44.70 N ANISOU 322 NE2 GLN A 42 6599 5442 4941 -464 -229 1601 N ATOM 323 N GLY A 43 -13.320 -32.637 -1.105 1.00 22.76 N ANISOU 323 N GLY A 43 3701 3001 1946 325 -422 111 N ATOM 324 CA GLY A 43 -14.553 -32.254 -0.426 1.00 21.73 C ANISOU 324 CA GLY A 43 3227 2937 2091 327 -488 150 C ATOM 325 C GLY A 43 -14.669 -32.696 1.033 1.00 19.27 C ANISOU 325 C GLY A 43 2765 2581 1976 220 -526 47 C ATOM 326 O GLY A 43 -15.762 -32.644 1.608 1.00 20.29 O ANISOU 326 O GLY A 43 2629 2813 2265 159 -812 -193 O ATOM 327 N SER A 44 -13.545 -33.104 1.633 1.00 17.36 N ANISOU 327 N SER A 44 2638 2257 1699 304 -303 -8 N ATOM 328 CA SER A 44 -13.496 -33.530 3.032 1.00 15.52 C ANISOU 328 CA SER A 44 2259 1959 1678 143 -92 -159 C ATOM 329 C SER A 44 -14.160 -32.501 3.975 1.00 14.66 C ANISOU 329 C SER A 44 2150 1604 1816 53 -400 -157 C ATOM 330 O SER A 44 -14.040 -31.295 3.787 1.00 15.77 O ANISOU 330 O SER A 44 2165 1842 1982 128 -488 87 O ATOM 331 CB SER A 44 -12.031 -33.718 3.416 1.00 16.84 C ANISOU 331 CB SER A 44 2526 2244 1626 272 -90 -108 C ATOM 332 OG SER A 44 -11.886 -34.151 4.756 1.00 16.47 O ANISOU 332 OG SER A 44 2383 2112 1762 15 -217 27 O ATOM 333 N ASP A 45 -14.769 -32.974 5.054 1.00 13.75 N ANISOU 333 N ASP A 45 1752 1785 1686 79 -229 -93 N ATOM 334 CA ASP A 45 -15.142 -32.100 6.166 1.00 13.29 C ANISOU 334 CA ASP A 45 1731 1775 1542 12 -274 -66 C ATOM 335 C ASP A 45 -13.935 -31.287 6.647 1.00 12.45 C ANISOU 335 C ASP A 45 1558 1349 1821 105 -239 -39 C ATOM 336 O ASP A 45 -12.780 -31.695 6.496 1.00 13.00 O ANISOU 336 O ASP A 45 1775 1356 1807 53 -158 83 O ATOM 337 CB ASP A 45 -15.733 -32.891 7.338 1.00 13.37 C ANISOU 337 CB ASP A 45 1589 1911 1579 -121 -247 108 C ATOM 338 CG ASP A 45 -17.174 -33.358 7.101 1.00 17.24 C ANISOU 338 CG ASP A 45 2257 2156 2138 96 -580 499 C ATOM 339 OD1 ASP A 45 -17.775 -32.996 6.066 1.00 18.79 O ANISOU 339 OD1 ASP A 45 2319 2314 2505 -453 -238 -198 O ATOM 340 OD2 ASP A 45 -17.775 -33.871 8.076 1.00 18.85 O ANISOU 340 OD2 ASP A 45 2181 2336 2645 -231 -189 335 O ATOM 341 N ALA A 46 -14.228 -30.082 7.104 1.00 11.91 N ANISOU 341 N ALA A 46 1569 1436 1520 -45 -368 -270 N ATOM 342 CA ALA A 46 -13.181 -29.130 7.463 1.00 12.40 C ANISOU 342 CA ALA A 46 1560 1506 1644 -330 -96 -335 C ATOM 343 C ALA A 46 -13.462 -28.544 8.843 1.00 11.88 C ANISOU 343 C ALA A 46 1410 1523 1580 -157 -141 -185 C ATOM 344 O ALA A 46 -14.492 -27.890 9.033 1.00 12.05 O ANISOU 344 O ALA A 46 1468 1591 1517 -66 -116 -67 O ATOM 345 CB ALA A 46 -13.110 -27.982 6.432 1.00 15.41 C ANISOU 345 CB ALA A 46 2146 1875 1832 -371 158 -121 C ATOM 346 N ALA A 47 -12.536 -28.732 9.781 1.00 11.56 N ANISOU 346 N ALA A 47 1537 1470 1385 -62 -179 -24 N ATOM 347 CA ALA A 47 -12.628 -28.066 11.073 1.00 12.26 C ANISOU 347 CA ALA A 47 1553 1493 1612 92 -132 -51 C ATOM 348 C ALA A 47 -12.482 -26.542 10.918 1.00 10.46 C ANISOU 348 C ALA A 47 1419 1353 1201 62 37 -177 C ATOM 349 O ALA A 47 -13.041 -25.753 11.693 1.00 12.21 O ANISOU 349 O ALA A 47 1603 1499 1537 25 76 -256 O ATOM 350 CB ALA A 47 -11.575 -28.589 11.998 1.00 13.36 C ANISOU 350 CB ALA A 47 1699 1776 1599 225 -270 45 C ATOM 351 N LEU A 48 -11.655 -26.133 9.961 1.00 10.41 N ANISOU 351 N LEU A 48 1216 1323 1415 -166 -49 -31 N ATOM 352 CA LEU A 48 -11.433 -24.712 9.707 1.00 10.40 C ANISOU 352 CA LEU A 48 1339 1366 1247 -78 -121 -194 C ATOM 353 C LEU A 48 -11.145 -24.497 8.242 1.00 10.26 C ANISOU 353 C LEU A 48 1073 1418 1406 -1 51 -210 C ATOM 354 O LEU A 48 -10.309 -25.176 7.646 1.00 11.70 O ANISOU 354 O LEU A 48 1357 1540 1547 203 125 -78 O ATOM 355 CB LEU A 48 -10.272 -24.174 10.555 1.00 13.19 C ANISOU 355 CB LEU A 48 1661 1832 1517 -293 38 -140 C ATOM 356 CG LEU A 48 -9.859 -22.724 10.290 1.00 12.71 C ANISOU 356 CG LEU A 48 1673 1621 1532 -167 -143 -271 C ATOM 357 CD1 LEU A 48 -10.981 -21.732 10.695 1.00 18.20 C ANISOU 357 CD1 LEU A 48 2372 1991 2552 -141 29 -325 C ATOM 358 CD2 LEU A 48 -8.549 -22.411 11.022 1.00 15.72 C ANISOU 358 CD2 LEU A 48 1685 2237 2051 -138 -522 -256 C ATOM 359 N HIS A 49 -11.827 -23.502 7.677 1.00 10.87 N ANISOU 359 N HIS A 49 1292 1393 1445 85 83 88 N ATOM 360 CA HIS A 49 -11.553 -22.980 6.340 1.00 10.45 C ANISOU 360 CA HIS A 49 1338 1279 1351 -142 -103 -113 C ATOM 361 C HIS A 49 -11.281 -21.490 6.559 1.00 10.43 C ANISOU 361 C HIS A 49 1200 1258 1503 81 187 -177 C ATOM 362 O HIS A 49 -12.168 -20.761 7.021 1.00 12.00 O ANISOU 362 O HIS A 49 1193 1476 1890 66 94 -200 O ATOM 363 CB HIS A 49 -12.786 -23.199 5.443 1.00 12.71 C ANISOU 363 CB HIS A 49 1619 1666 1543 -206 -198 -76 C ATOM 364 CG HIS A 49 -12.796 -22.424 4.164 1.00 11.88 C ANISOU 364 CG HIS A 49 1332 1460 1721 56 -215 -150 C ATOM 365 ND1 HIS A 49 -11.931 -22.663 3.122 1.00 13.32 N ANISOU 365 ND1 HIS A 49 1682 1724 1653 72 -231 113 N ATOM 366 CD2 HIS A 49 -13.685 -21.505 3.705 1.00 14.03 C ANISOU 366 CD2 HIS A 49 1643 1724 1962 112 -290 136 C ATOM 367 CE1 HIS A 49 -12.254 -21.887 2.094 1.00 13.38 C ANISOU 367 CE1 HIS A 49 1616 1579 1885 -161 -248 104 C ATOM 368 NE2 HIS A 49 -13.313 -21.176 2.429 1.00 16.54 N ANISOU 368 NE2 HIS A 49 2131 1883 2269 -333 -255 -82 N ATOM 369 N PHE A 50 -10.032 -21.062 6.335 1.00 10.61 N ANISOU 369 N PHE A 50 1307 1339 1385 -179 111 36 N ATOM 370 CA PHE A 50 -9.598 -19.670 6.548 1.00 10.33 C ANISOU 370 CA PHE A 50 1270 1247 1405 -93 -78 7 C ATOM 371 C PHE A 50 -9.355 -19.096 5.162 1.00 10.58 C ANISOU 371 C PHE A 50 1227 1381 1412 129 144 -181 C ATOM 372 O PHE A 50 -8.522 -19.602 4.414 1.00 11.42 O ANISOU 372 O PHE A 50 1347 1425 1565 292 123 9 O ATOM 373 CB PHE A 50 -8.299 -19.706 7.360 1.00 11.65 C ANISOU 373 CB PHE A 50 1311 1471 1643 -100 -150 -300 C ATOM 374 CG PHE A 50 -7.584 -18.389 7.452 1.00 11.47 C ANISOU 374 CG PHE A 50 1243 1406 1708 93 -9 -322 C ATOM 375 CD1 PHE A 50 -8.060 -17.386 8.279 1.00 14.15 C ANISOU 375 CD1 PHE A 50 1440 1708 2229 -210 -24 -498 C ATOM 376 CD2 PHE A 50 -6.418 -18.152 6.713 1.00 13.32 C ANISOU 376 CD2 PHE A 50 1292 1744 2024 -265 -262 -240 C ATOM 377 CE1 PHE A 50 -7.331 -16.210 8.441 1.00 14.83 C ANISOU 377 CE1 PHE A 50 1466 1732 2433 -54 264 -453 C ATOM 378 CE2 PHE A 50 -5.714 -16.966 6.859 1.00 12.16 C ANISOU 378 CE2 PHE A 50 1354 1579 1687 0 -52 -329 C ATOM 379 CZ PHE A 50 -6.184 -16.001 7.718 1.00 12.82 C ANISOU 379 CZ PHE A 50 1432 1629 1809 116 57 -263 C ATOM 380 N ASN A 51 -10.112 -18.051 4.810 1.00 10.89 N ANISOU 380 N ASN A 51 1355 1273 1510 64 118 -71 N ATOM 381 CA ASN A 51 -10.204 -17.641 3.398 1.00 10.72 C ANISOU 381 CA ASN A 51 1460 1128 1481 -60 -200 -163 C ATOM 382 C ASN A 51 -10.084 -16.128 3.243 1.00 11.11 C ANISOU 382 C ASN A 51 1243 1264 1713 14 49 -236 C ATOM 383 O ASN A 51 -11.095 -15.422 3.166 1.00 11.66 O ANISOU 383 O ASN A 51 1351 1368 1710 63 93 -180 O ATOM 384 CB ASN A 51 -11.558 -18.145 2.881 1.00 11.35 C ANISOU 384 CB ASN A 51 1273 1419 1621 -193 -54 -243 C ATOM 385 CG ASN A 51 -11.798 -17.926 1.379 1.00 11.56 C ANISOU 385 CG ASN A 51 1212 1314 1866 -40 -241 14 C ATOM 386 OD1 ASN A 51 -12.963 -17.787 0.944 1.00 13.73 O ANISOU 386 OD1 ASN A 51 1414 1563 2238 14 -288 45 O ATOM 387 ND2 ASN A 51 -10.741 -17.957 0.570 1.00 13.19 N ANISOU 387 ND2 ASN A 51 1358 1898 1755 -13 101 -83 N ATOM 388 N PRO A 52 -8.839 -15.621 3.138 1.00 10.57 N ANISOU 388 N PRO A 52 1120 1226 1668 11 3 -137 N ATOM 389 CA PRO A 52 -8.658 -14.226 2.737 1.00 11.17 C ANISOU 389 CA PRO A 52 1305 1243 1696 39 -86 -206 C ATOM 390 C PRO A 52 -9.134 -14.004 1.303 1.00 10.31 C ANISOU 390 C PRO A 52 1298 1027 1591 79 -50 -99 C ATOM 391 O PRO A 52 -8.644 -14.655 0.351 1.00 11.83 O ANISOU 391 O PRO A 52 1383 1407 1703 119 -15 -155 O ATOM 392 CB PRO A 52 -7.143 -13.998 2.885 1.00 12.84 C ANISOU 392 CB PRO A 52 1197 1631 2049 -129 -225 -165 C ATOM 393 CG PRO A 52 -6.732 -15.043 3.918 1.00 12.57 C ANISOU 393 CG PRO A 52 1379 1413 1981 -152 -102 -90 C ATOM 394 CD PRO A 52 -7.569 -16.264 3.501 1.00 11.14 C ANISOU 394 CD PRO A 52 1038 1493 1702 0 -215 1 C ATOM 395 N ARG A 53 -10.012 -13.020 1.152 1.00 11.48 N ANISOU 395 N ARG A 53 1286 1257 1816 11 -186 -124 N ATOM 396 CA ARG A 53 -10.607 -12.698 -0.144 1.00 11.78 C ANISOU 396 CA ARG A 53 1252 1445 1780 0 -57 -70 C ATOM 397 C ARG A 53 -10.143 -11.285 -0.536 1.00 11.58 C ANISOU 397 C ARG A 53 1353 1271 1775 60 156 -125 C ATOM 398 O ARG A 53 -10.705 -10.288 -0.077 1.00 13.91 O ANISOU 398 O ARG A 53 1569 1572 2142 123 100 -140 O ATOM 399 CB ARG A 53 -12.148 -12.792 -0.098 1.00 12.59 C ANISOU 399 CB ARG A 53 1386 1266 2131 -114 98 -128 C ATOM 400 CG ARG A 53 -12.650 -14.202 0.264 1.00 11.68 C ANISOU 400 CG ARG A 53 1216 1285 1937 -137 59 -121 C ATOM 401 CD ARG A 53 -14.168 -14.200 0.387 1.00 12.69 C ANISOU 401 CD ARG A 53 1359 1427 2037 -180 -91 -28 C ATOM 402 NE ARG A 53 -14.708 -15.519 0.700 1.00 12.76 N ANISOU 402 NE ARG A 53 1500 1518 1830 -118 -95 -161 N ATOM 403 CZ ARG A 53 -16.000 -15.755 0.913 1.00 13.21 C ANISOU 403 CZ ARG A 53 1526 1599 1891 -116 -282 -252 C ATOM 404 NH1 ARG A 53 -16.902 -14.783 0.808 1.00 14.89 N ANISOU 404 NH1 ARG A 53 1601 1763 2292 58 -395 108 N ATOM 405 NH2 ARG A 53 -16.400 -16.963 1.278 1.00 15.95 N ANISOU 405 NH2 ARG A 53 2021 1690 2347 -87 -430 69 N ATOM 406 N LEU A 54 -9.109 -11.191 -1.381 1.00 12.37 N ANISOU 406 N LEU A 54 1427 1469 1801 -184 -90 21 N ATOM 407 CA LEU A 54 -8.571 -9.902 -1.805 1.00 13.25 C ANISOU 407 CA LEU A 54 1321 1558 2155 -61 -26 65 C ATOM 408 C LEU A 54 -9.563 -9.240 -2.745 1.00 13.34 C ANISOU 408 C LEU A 54 1476 1394 2196 38 4 2 C ATOM 409 O LEU A 54 -9.701 -8.022 -2.749 1.00 15.78 O ANISOU 409 O LEU A 54 1742 1534 2719 -19 -588 -32 O ATOM 410 CB LEU A 54 -7.232 -10.073 -2.541 1.00 14.68 C ANISOU 410 CB LEU A 54 1453 1989 2135 177 -45 310 C ATOM 411 CG LEU A 54 -5.999 -10.418 -1.712 1.00 16.76 C ANISOU 411 CG LEU A 54 1642 2264 2461 96 -238 51 C ATOM 412 CD1 LEU A 54 -5.795 -9.430 -0.580 1.00 18.47 C ANISOU 412 CD1 LEU A 54 1760 2334 2921 21 -459 -87 C ATOM 413 CD2 LEU A 54 -6.061 -11.878 -1.216 1.00 18.93 C ANISOU 413 CD2 LEU A 54 1857 2537 2797 292 47 536 C ATOM 414 N ASP A 55 -10.271 -10.057 -3.527 1.00 12.07 N ANISOU 414 N ASP A 55 1196 1621 1768 32 -251 0 N ATOM 415 CA ASP A 55 -11.224 -9.524 -4.477 1.00 13.63 C ANISOU 415 CA ASP A 55 1589 1658 1930 116 -165 2 C ATOM 416 C ASP A 55 -12.398 -8.764 -3.830 1.00 12.83 C ANISOU 416 C ASP A 55 1432 1400 2041 151 -85 17 C ATOM 417 O ASP A 55 -12.851 -7.753 -4.376 1.00 17.51 O ANISOU 417 O ASP A 55 2221 2088 2344 433 -95 223 O ATOM 418 CB ASP A 55 -11.661 -10.587 -5.506 1.00 14.39 C ANISOU 418 CB ASP A 55 1781 1794 1892 -200 -195 -44 C ATOM 419 CG ASP A 55 -12.151 -11.887 -4.884 1.00 16.28 C ANISOU 419 CG ASP A 55 1751 2131 2303 -125 -229 -345 C ATOM 420 OD1 ASP A 55 -12.323 -11.980 -3.648 1.00 14.43 O ANISOU 420 OD1 ASP A 55 1627 1552 2303 -58 -158 -180 O ATOM 421 OD2 ASP A 55 -12.403 -12.819 -5.681 1.00 19.23 O ANISOU 421 OD2 ASP A 55 1996 2422 2887 -278 83 -386 O ATOM 422 N THR A 56 -12.883 -9.241 -2.690 1.00 12.69 N ANISOU 422 N THR A 56 1325 1352 2144 44 -80 -73 N ATOM 423 CA THR A 56 -14.026 -8.621 -2.023 1.00 12.94 C ANISOU 423 CA THR A 56 1485 1390 2042 79 -126 -111 C ATOM 424 C THR A 56 -13.618 -7.909 -0.715 1.00 13.77 C ANISOU 424 C THR A 56 1597 1400 2234 66 -262 -190 C ATOM 425 O THR A 56 -14.472 -7.390 0.009 1.00 15.39 O ANISOU 425 O THR A 56 1565 1677 2603 229 -12 -384 O ATOM 426 CB THR A 56 -15.089 -9.676 -1.694 1.00 12.50 C ANISOU 426 CB THR A 56 1565 1185 1998 -73 -272 91 C ATOM 427 OG1 THR A 56 -14.457 -10.685 -0.907 1.00 13.97 O ANISOU 427 OG1 THR A 56 1383 1539 2383 20 -37 57 O ATOM 428 CG2 THR A 56 -15.650 -10.321 -2.992 1.00 14.80 C ANISOU 428 CG2 THR A 56 1453 1921 2248 -42 63 -293 C ATOM 429 N SER A 57 -12.321 -7.897 -0.395 1.00 12.33 N ANISOU 429 N SER A 57 1496 1234 1953 43 -131 -64 N ATOM 430 CA SER A 57 -11.803 -7.234 0.824 1.00 12.48 C ANISOU 430 CA SER A 57 1589 1222 1930 -8 -112 -230 C ATOM 431 C SER A 57 -12.445 -7.770 2.102 1.00 13.80 C ANISOU 431 C SER A 57 1752 1249 2242 -43 44 -206 C ATOM 432 O SER A 57 -12.870 -7.014 2.967 1.00 16.54 O ANISOU 432 O SER A 57 2071 1659 2555 60 148 -433 O ATOM 433 CB SER A 57 -11.921 -5.712 0.732 1.00 15.42 C ANISOU 433 CB SER A 57 1888 1441 2529 142 147 -4 C ATOM 434 OG SER A 57 -11.199 -5.241 -0.389 1.00 17.96 O ANISOU 434 OG SER A 57 2491 1524 2807 -162 144 -214 O ATOM 435 N GLU A 58 -12.435 -9.096 2.249 1.00 13.56 N ANISOU 435 N GLU A 58 1733 1222 2196 -144 64 -178 N ATOM 436 CA GLU A 58 -12.940 -9.740 3.471 1.00 13.66 C ANISOU 436 CA GLU A 58 1531 1543 2115 -63 128 -103 C ATOM 437 C GLU A 58 -12.063 -10.934 3.826 1.00 12.60 C ANISOU 437 C GLU A 58 1534 1315 1936 128 159 -156 C ATOM 438 O GLU A 58 -11.377 -11.464 2.968 1.00 15.20 O ANISOU 438 O GLU A 58 2220 1695 1858 353 282 -102 O ATOM 439 CB GLU A 58 -14.375 -10.253 3.265 1.00 16.11 C ANISOU 439 CB GLU A 58 1679 1685 2756 217 388 469 C ATOM 440 CG GLU A 58 -15.378 -9.211 2.839 1.00 17.69 C ANISOU 440 CG GLU A 58 1910 1874 2937 269 158 82 C ATOM 441 CD GLU A 58 -16.793 -9.645 3.153 1.00 18.97 C ANISOU 441 CD GLU A 58 2039 1710 3458 7 100 -93 C ATOM 442 OE1 GLU A 58 -17.295 -10.576 2.463 1.00 20.99 O ANISOU 442 OE1 GLU A 58 2541 2430 3003 -254 666 -392 O ATOM 443 OE2 GLU A 58 -17.336 -9.178 4.198 1.00 25.71 O ANISOU 443 OE2 GLU A 58 2663 3259 3846 -223 407 -587 O ATOM 444 N VAL A 59 -12.066 -11.345 5.094 1.00 12.50 N ANISOU 444 N VAL A 59 1690 1336 1721 24 33 -283 N ATOM 445 CA VAL A 59 -11.476 -12.629 5.474 1.00 11.33 C ANISOU 445 CA VAL A 59 1261 1322 1721 -18 41 -137 C ATOM 446 C VAL A 59 -12.576 -13.458 6.117 1.00 12.21 C ANISOU 446 C VAL A 59 1393 1430 1815 28 172 -414 C ATOM 447 O VAL A 59 -13.101 -13.109 7.156 1.00 13.38 O ANISOU 447 O VAL A 59 1707 1652 1724 -120 164 -293 O ATOM 448 CB VAL A 59 -10.274 -12.464 6.446 1.00 13.16 C ANISOU 448 CB VAL A 59 1420 1653 1926 -136 -40 -209 C ATOM 449 CG1 VAL A 59 -9.706 -13.831 6.788 1.00 14.12 C ANISOU 449 CG1 VAL A 59 1771 1939 1655 211 199 21 C ATOM 450 CG2 VAL A 59 -9.198 -11.547 5.835 1.00 14.95 C ANISOU 450 CG2 VAL A 59 1679 1887 2114 -469 161 -203 C ATOM 451 N VAL A 60 -12.863 -14.599 5.512 1.00 11.63 N ANISOU 451 N VAL A 60 1346 1230 1842 -85 9 -218 N ATOM 452 CA VAL A 60 -13.949 -15.467 5.961 1.00 11.41 C ANISOU 452 CA VAL A 60 1464 1150 1719 -136 -44 10 C ATOM 453 C VAL A 60 -13.395 -16.694 6.681 1.00 10.39 C ANISOU 453 C VAL A 60 1212 1192 1542 -2 126 -347 C ATOM 454 O VAL A 60 -12.383 -17.251 6.279 1.00 11.82 O ANISOU 454 O VAL A 60 1280 1511 1698 77 193 -191 O ATOM 455 CB VAL A 60 -14.808 -15.882 4.745 1.00 11.69 C ANISOU 455 CB VAL A 60 1161 1289 1991 -156 -196 -29 C ATOM 456 CG1 VAL A 60 -15.665 -17.115 5.037 1.00 14.03 C ANISOU 456 CG1 VAL A 60 1715 1828 1787 -474 -187 25 C ATOM 457 CG2 VAL A 60 -15.640 -14.699 4.282 1.00 16.13 C ANISOU 457 CG2 VAL A 60 1592 2102 2433 283 -97 -116 C ATOM 458 N PHE A 61 -14.087 -17.096 7.748 1.00 10.43 N ANISOU 458 N PHE A 61 1274 1208 1478 -79 37 -146 N ATOM 459 CA PHE A 61 -13.799 -18.321 8.484 1.00 11.78 C ANISOU 459 CA PHE A 61 1560 1262 1653 -155 -53 -189 C ATOM 460 C PHE A 61 -15.048 -19.195 8.436 1.00 11.04 C ANISOU 460 C PHE A 61 1237 1333 1622 -5 -58 -304 C ATOM 461 O PHE A 61 -16.143 -18.704 8.676 1.00 12.76 O ANISOU 461 O PHE A 61 1518 1399 1931 74 63 -274 O ATOM 462 CB PHE A 61 -13.499 -18.032 9.965 1.00 12.56 C ANISOU 462 CB PHE A 61 1482 1512 1779 -53 113 -463 C ATOM 463 CG PHE A 61 -12.293 -17.179 10.190 1.00 12.16 C ANISOU 463 CG PHE A 61 1452 1575 1590 -118 166 -332 C ATOM 464 CD1 PHE A 61 -12.339 -15.809 9.967 1.00 13.27 C ANISOU 464 CD1 PHE A 61 1617 1622 1803 -244 87 -363 C ATOM 465 CD2 PHE A 61 -11.161 -17.725 10.758 1.00 15.16 C ANISOU 465 CD2 PHE A 61 1594 2153 2011 -66 -442 -582 C ATOM 466 CE1 PHE A 61 -11.186 -15.029 10.179 1.00 14.96 C ANISOU 466 CE1 PHE A 61 1552 1971 2160 -344 -64 -393 C ATOM 467 CE2 PHE A 61 -10.079 -16.929 11.082 1.00 15.32 C ANISOU 467 CE2 PHE A 61 1762 1892 2165 -185 -200 -330 C ATOM 468 CZ PHE A 61 -10.074 -15.609 10.744 1.00 14.39 C ANISOU 468 CZ PHE A 61 1545 1754 2165 -159 -22 -703 C ATOM 469 N ASN A 62 -14.901 -20.485 8.173 1.00 10.72 N ANISOU 469 N ASN A 62 1360 1267 1443 -65 58 -127 N ATOM 470 CA ASN A 62 -16.053 -21.383 8.205 1.00 10.23 C ANISOU 470 CA ASN A 62 1094 1401 1392 -87 -34 -87 C ATOM 471 C ASN A 62 -15.603 -22.800 8.517 1.00 11.09 C ANISOU 471 C ASN A 62 1204 1420 1589 58 136 -244 C ATOM 472 O ASN A 62 -14.386 -23.063 8.614 1.00 12.05 O ANISOU 472 O ASN A 62 1277 1434 1867 -96 121 -25 O ATOM 473 CB ASN A 62 -16.851 -21.313 6.888 1.00 11.82 C ANISOU 473 CB ASN A 62 1217 1662 1608 61 -136 -150 C ATOM 474 CG ASN A 62 -18.344 -21.588 7.088 1.00 9.90 C ANISOU 474 CG ASN A 62 1115 1268 1375 -28 -3 -136 C ATOM 475 OD1 ASN A 62 -18.772 -22.036 8.161 1.00 11.33 O ANISOU 475 OD1 ASN A 62 1267 1426 1609 -18 -16 -27 O ATOM 476 ND2 ASN A 62 -19.146 -21.343 6.035 1.00 11.30 N ANISOU 476 ND2 ASN A 62 1352 1366 1573 -18 -141 -136 N ATOM 477 N SER A 63 -16.554 -23.716 8.629 1.00 10.94 N ANISOU 477 N SER A 63 1241 1277 1638 -80 15 -176 N ATOM 478 CA SER A 63 -16.315 -25.162 8.816 1.00 11.42 C ANISOU 478 CA SER A 63 1554 1197 1584 -134 -30 -146 C ATOM 479 C SER A 63 -17.232 -25.876 7.841 1.00 11.63 C ANISOU 479 C SER A 63 1297 1439 1680 -4 -44 105 C ATOM 480 O SER A 63 -18.198 -25.296 7.333 1.00 13.91 O ANISOU 480 O SER A 63 1420 1640 2225 83 -407 -135 O ATOM 481 CB SER A 63 -16.704 -25.555 10.228 1.00 13.06 C ANISOU 481 CB SER A 63 1459 1657 1846 -79 165 -112 C ATOM 482 OG SER A 63 -18.037 -25.125 10.475 1.00 15.85 O ANISOU 482 OG SER A 63 1990 1962 2069 24 298 21 O ATOM 483 N LYS A 64 -16.928 -27.138 7.581 1.00 12.07 N ANISOU 483 N LYS A 64 1433 1433 1719 -140 -135 -160 N ATOM 484 CA LYS A 64 -17.796 -27.962 6.747 1.00 13.55 C ANISOU 484 CA LYS A 64 1661 1505 1982 -242 -170 -74 C ATOM 485 C LYS A 64 -17.967 -29.291 7.487 1.00 13.99 C ANISOU 485 C LYS A 64 1343 1643 2326 0 -311 242 C ATOM 486 O LYS A 64 -16.976 -29.918 7.880 1.00 13.60 O ANISOU 486 O LYS A 64 1469 1542 2156 -97 -155 23 O ATOM 487 CB LYS A 64 -17.168 -28.189 5.355 1.00 13.73 C ANISOU 487 CB LYS A 64 1468 1829 1920 -173 -326 -357 C ATOM 488 CG LYS A 64 -18.082 -28.968 4.393 1.00 18.09 C ANISOU 488 CG LYS A 64 2173 2469 2229 -155 -514 -438 C ATOM 489 CD LYS A 64 -17.362 -29.268 3.089 1.00 21.60 C ANISOU 489 CD LYS A 64 2718 3371 2115 -321 -694 -784 C ATOM 490 CE LYS A 64 -18.343 -29.631 1.997 1.00 31.35 C ANISOU 490 CE LYS A 64 3817 4791 3303 -161 -1038 -97 C ATOM 491 NZ LYS A 64 -17.669 -30.260 0.828 1.00 35.60 N ANISOU 491 NZ LYS A 64 4203 5362 3959 1117 -982 172 N ATOM 492 N GLU A 65 -19.210 -29.692 7.757 1.00 15.87 N ANISOU 492 N GLU A 65 1816 1621 2590 -302 64 140 N ATOM 493 CA GLU A 65 -19.446 -30.911 8.535 1.00 18.75 C ANISOU 493 CA GLU A 65 2379 1791 2952 -211 -229 244 C ATOM 494 C GLU A 65 -20.609 -31.666 7.946 1.00 18.27 C ANISOU 494 C GLU A 65 1948 1738 3254 1 -354 308 C ATOM 495 O GLU A 65 -21.619 -31.058 7.545 1.00 18.01 O ANISOU 495 O GLU A 65 1961 1896 2983 -198 -321 652 O ATOM 496 CB GLU A 65 -19.714 -30.610 10.013 1.00 21.26 C ANISOU 496 CB GLU A 65 2673 2161 3243 -142 -86 536 C ATOM 497 CG GLU A 65 -19.757 -31.871 10.882 1.00 28.10 C ANISOU 497 CG GLU A 65 3877 3194 3604 3 35 518 C ATOM 498 CD GLU A 65 -20.104 -31.583 12.327 1.00 33.44 C ANISOU 498 CD GLU A 65 4268 4438 3997 628 260 738 C ATOM 499 OE1 GLU A 65 -21.057 -30.815 12.574 1.00 42.98 O ANISOU 499 OE1 GLU A 65 4993 5493 5844 922 516 597 O ATOM 500 OE2 GLU A 65 -19.469 -32.178 13.223 1.00 35.98 O ANISOU 500 OE2 GLU A 65 3822 5145 4701 1238 -104 819 O ATOM 501 N GLN A 66 -20.469 -32.994 7.859 1.00 18.09 N ANISOU 501 N GLN A 66 2298 1790 2782 -232 -203 118 N ATOM 502 CA GLN A 66 -21.475 -33.799 7.175 1.00 20.90 C ANISOU 502 CA GLN A 66 2332 2525 3084 -583 -315 67 C ATOM 503 C GLN A 66 -21.730 -33.280 5.755 1.00 20.48 C ANISOU 503 C GLN A 66 2595 2151 3033 -97 -483 222 C ATOM 504 O GLN A 66 -22.860 -33.317 5.256 1.00 20.29 O ANISOU 504 O GLN A 66 2314 2083 3313 -273 -679 -250 O ATOM 505 CB GLN A 66 -22.791 -33.848 7.966 1.00 24.26 C ANISOU 505 CB GLN A 66 2546 3015 3654 -154 -247 459 C ATOM 506 CG GLN A 66 -22.633 -34.125 9.451 1.00 31.59 C ANISOU 506 CG GLN A 66 3287 4684 4028 -770 -213 -48 C ATOM 507 CD GLN A 66 -21.920 -35.424 9.729 1.00 45.47 C ANISOU 507 CD GLN A 66 5378 5842 6056 -349 -394 457 C ATOM 508 OE1 GLN A 66 -21.718 -36.242 8.829 1.00 51.53 O ANISOU 508 OE1 GLN A 66 6056 7213 6309 -443 -103 -2 O ATOM 509 NE2 GLN A 66 -21.534 -35.628 10.984 1.00 51.83 N ANISOU 509 NE2 GLN A 66 6339 7276 6079 -509 -431 190 N ATOM 510 N GLY A 67 -20.683 -32.768 5.119 1.00 18.71 N ANISOU 510 N GLY A 67 2748 1786 2573 6 56 -86 N ATOM 511 CA GLY A 67 -20.785 -32.212 3.750 1.00 17.04 C ANISOU 511 CA GLY A 67 2524 1603 2345 447 -463 -192 C ATOM 512 C GLY A 67 -21.498 -30.870 3.575 1.00 19.17 C ANISOU 512 C GLY A 67 2509 2115 2659 192 -155 -358 C ATOM 513 O GLY A 67 -21.726 -30.447 2.454 1.00 21.40 O ANISOU 513 O GLY A 67 2735 2717 2679 523 -452 -44 O ATOM 514 N SER A 68 -21.794 -30.162 4.659 1.00 16.55 N ANISOU 514 N SER A 68 2029 1672 2585 23 -395 -101 N ATOM 515 CA SER A 68 -22.513 -28.881 4.558 1.00 16.12 C ANISOU 515 CA SER A 68 1679 1614 2831 -212 -443 -340 C ATOM 516 C SER A 68 -21.666 -27.796 5.217 1.00 15.28 C ANISOU 516 C SER A 68 1697 1794 2313 -136 -417 -221 C ATOM 517 O SER A 68 -21.111 -28.026 6.293 1.00 15.08 O ANISOU 517 O SER A 68 1737 1662 2331 -88 -191 62 O ATOM 518 CB SER A 68 -23.831 -29.018 5.319 1.00 17.92 C ANISOU 518 CB SER A 68 1671 1890 3247 -457 -301 -590 C ATOM 519 OG SER A 68 -24.742 -29.841 4.602 1.00 19.95 O ANISOU 519 OG SER A 68 2150 2150 3278 -349 -621 -95 O ATOM 520 N TRP A 69 -21.642 -26.600 4.627 1.00 13.50 N ANISOU 520 N TRP A 69 1420 1626 2084 -178 -173 -216 N ATOM 521 CA TRP A 69 -20.918 -25.480 5.261 1.00 12.80 C ANISOU 521 CA TRP A 69 1437 1494 1931 -164 -163 -207 C ATOM 522 C TRP A 69 -21.686 -24.935 6.446 1.00 12.62 C ANISOU 522 C TRP A 69 1352 1573 1867 -71 -212 -287 C ATOM 523 O TRP A 69 -22.934 -24.937 6.446 1.00 14.94 O ANISOU 523 O TRP A 69 1498 1910 2269 -7 -74 -256 O ATOM 524 CB TRP A 69 -20.697 -24.361 4.263 1.00 12.52 C ANISOU 524 CB TRP A 69 1303 1605 1850 -11 -163 -175 C ATOM 525 CG TRP A 69 -19.730 -24.769 3.204 1.00 12.86 C ANISOU 525 CG TRP A 69 1548 1715 1620 -159 -199 -362 C ATOM 526 CD1 TRP A 69 -20.004 -25.277 1.962 1.00 16.17 C ANISOU 526 CD1 TRP A 69 1822 2122 2200 32 -56 -281 C ATOM 527 CD2 TRP A 69 -18.309 -24.714 3.313 1.00 14.75 C ANISOU 527 CD2 TRP A 69 1511 1789 2303 -189 -32 -268 C ATOM 528 NE1 TRP A 69 -18.829 -25.519 1.283 1.00 20.08 N ANISOU 528 NE1 TRP A 69 1914 2924 2789 3 204 -666 N ATOM 529 CE2 TRP A 69 -17.775 -25.179 2.095 1.00 17.05 C ANISOU 529 CE2 TRP A 69 1500 2812 2165 -253 -43 -573 C ATOM 530 CE3 TRP A 69 -17.434 -24.297 4.321 1.00 15.40 C ANISOU 530 CE3 TRP A 69 1590 1756 2503 -21 -191 -455 C ATOM 531 CZ2 TRP A 69 -16.393 -25.282 1.878 1.00 20.57 C ANISOU 531 CZ2 TRP A 69 1585 3109 3120 -353 266 -1285 C ATOM 532 CZ3 TRP A 69 -16.055 -24.351 4.089 1.00 18.78 C ANISOU 532 CZ3 TRP A 69 2093 2173 2868 64 -59 -480 C ATOM 533 CH2 TRP A 69 -15.555 -24.850 2.882 1.00 21.35 C ANISOU 533 CH2 TRP A 69 2153 2979 2978 -413 73 -899 C ATOM 534 N GLY A 70 -20.949 -24.458 7.446 1.00 12.62 N ANISOU 534 N GLY A 70 1451 1458 1885 -8 -323 -208 N ATOM 535 CA GLY A 70 -21.538 -23.725 8.555 1.00 13.42 C ANISOU 535 CA GLY A 70 1708 1366 2021 -125 0 -47 C ATOM 536 C GLY A 70 -21.845 -22.269 8.255 1.00 12.65 C ANISOU 536 C GLY A 70 1477 1424 1903 -123 18 -38 C ATOM 537 O GLY A 70 -21.806 -21.842 7.096 1.00 12.62 O ANISOU 537 O GLY A 70 1312 1586 1897 -36 85 -35 O ATOM 538 N ARG A 71 -22.129 -21.500 9.300 1.00 12.67 N ANISOU 538 N ARG A 71 1464 1535 1812 -113 -7 -103 N ATOM 539 CA ARG A 71 -22.311 -20.056 9.116 1.00 11.71 C ANISOU 539 CA ARG A 71 1399 1300 1748 -59 285 -196 C ATOM 540 C ARG A 71 -20.940 -19.346 9.068 1.00 11.92 C ANISOU 540 C ARG A 71 1343 1446 1738 -31 -194 -47 C ATOM 541 O ARG A 71 -20.087 -19.598 9.920 1.00 13.77 O ANISOU 541 O ARG A 71 1530 1621 2078 -22 -244 -36 O ATOM 542 CB ARG A 71 -23.148 -19.495 10.254 1.00 13.45 C ANISOU 542 CB ARG A 71 1692 1652 1764 -70 444 -161 C ATOM 543 CG ARG A 71 -23.496 -18.038 10.050 1.00 15.14 C ANISOU 543 CG ARG A 71 2143 1691 1917 218 163 -164 C ATOM 544 CD ARG A 71 -24.425 -17.482 11.095 1.00 17.26 C ANISOU 544 CD ARG A 71 1927 2205 2423 507 441 -315 C ATOM 545 NE ARG A 71 -24.626 -16.070 10.823 1.00 19.30 N ANISOU 545 NE ARG A 71 1883 2700 2747 227 210 -492 N ATOM 546 CZ ARG A 71 -25.525 -15.601 9.964 1.00 19.89 C ANISOU 546 CZ ARG A 71 2395 2085 3075 41 -198 -910 C ATOM 547 NH1 ARG A 71 -26.349 -16.443 9.350 1.00 21.99 N ANISOU 547 NH1 ARG A 71 2405 2179 3770 556 -189 -1043 N ATOM 548 NH2 ARG A 71 -25.539 -14.309 9.651 1.00 23.76 N ANISOU 548 NH2 ARG A 71 3131 1852 4042 230 59 -335 N ATOM 549 N GLU A 72 -20.705 -18.514 8.055 1.00 12.19 N ANISOU 549 N GLU A 72 1291 1531 1810 -143 74 -96 N ATOM 550 CA GLU A 72 -19.431 -17.788 7.961 1.00 12.76 C ANISOU 550 CA GLU A 72 1339 1631 1879 -91 -38 -180 C ATOM 551 C GLU A 72 -19.277 -16.819 9.118 1.00 12.20 C ANISOU 551 C GLU A 72 1309 1444 1879 71 -96 -330 C ATOM 552 O GLU A 72 -20.239 -16.147 9.493 1.00 13.61 O ANISOU 552 O GLU A 72 1447 1773 1949 143 -98 -287 O ATOM 553 CB GLU A 72 -19.344 -17.012 6.650 1.00 13.53 C ANISOU 553 CB GLU A 72 1614 1492 2033 -92 73 -162 C ATOM 554 CG GLU A 72 -19.201 -17.927 5.452 1.00 14.36 C ANISOU 554 CG GLU A 72 1710 1620 2124 -263 -108 -298 C ATOM 555 CD GLU A 72 -19.292 -17.215 4.113 1.00 14.69 C ANISOU 555 CD GLU A 72 1367 2025 2190 215 17 -176 C ATOM 556 OE1 GLU A 72 -19.747 -16.054 4.073 1.00 15.48 O ANISOU 556 OE1 GLU A 72 1642 1796 2441 27 -132 -73 O ATOM 557 OE2 GLU A 72 -18.862 -17.817 3.100 1.00 15.11 O ANISOU 557 OE2 GLU A 72 1887 1843 2011 -101 106 -81 O ATOM 558 N GLU A 73 -18.051 -16.708 9.616 1.00 12.86 N ANISOU 558 N GLU A 73 1454 1443 1986 14 -12 -342 N ATOM 559 CA GLU A 73 -17.610 -15.597 10.453 1.00 13.39 C ANISOU 559 CA GLU A 73 1581 1533 1971 -72 139 -523 C ATOM 560 C GLU A 73 -16.623 -14.755 9.653 1.00 13.48 C ANISOU 560 C GLU A 73 1365 1703 2052 -37 278 -622 C ATOM 561 O GLU A 73 -15.982 -15.245 8.751 1.00 15.44 O ANISOU 561 O GLU A 73 1730 1711 2423 98 491 -636 O ATOM 562 CB GLU A 73 -16.886 -16.117 11.713 1.00 14.91 C ANISOU 562 CB GLU A 73 1779 2035 1851 -99 248 -388 C ATOM 563 CG GLU A 73 -17.723 -17.035 12.584 1.00 18.10 C ANISOU 563 CG GLU A 73 2277 2362 2237 -308 119 212 C ATOM 564 CD GLU A 73 -16.986 -17.604 13.811 1.00 21.46 C ANISOU 564 CD GLU A 73 2308 2857 2987 -215 -16 -239 C ATOM 565 OE1 GLU A 73 -15.942 -17.063 14.230 1.00 21.43 O ANISOU 565 OE1 GLU A 73 2428 2915 2798 -139 183 -139 O ATOM 566 OE2 GLU A 73 -17.494 -18.601 14.377 1.00 23.16 O ANISOU 566 OE2 GLU A 73 2696 3267 2837 101 140 22 O ATOM 567 N ARG A 74 -16.529 -13.476 9.965 1.00 14.30 N ANISOU 567 N ARG A 74 1794 1513 2126 -125 336 -553 N ATOM 568 CA ARG A 74 -15.596 -12.594 9.294 1.00 14.86 C ANISOU 568 CA ARG A 74 1648 1790 2208 -186 170 -488 C ATOM 569 C ARG A 74 -14.683 -11.931 10.290 1.00 15.20 C ANISOU 569 C ARG A 74 1751 1743 2279 -218 304 -524 C ATOM 570 O ARG A 74 -15.132 -11.516 11.354 1.00 16.54 O ANISOU 570 O ARG A 74 1928 2083 2272 -230 332 -653 O ATOM 571 CB ARG A 74 -16.355 -11.552 8.485 1.00 17.27 C ANISOU 571 CB ARG A 74 2058 1927 2574 -119 0 -369 C ATOM 572 CG ARG A 74 -16.904 -12.138 7.205 1.00 17.87 C ANISOU 572 CG ARG A 74 2087 2166 2536 20 117 -591 C ATOM 573 CD ARG A 74 -18.091 -11.356 6.683 1.00 19.30 C ANISOU 573 CD ARG A 74 2663 1769 2901 135 52 -74 C ATOM 574 NE ARG A 74 -18.306 -11.633 5.266 1.00 18.10 N ANISOU 574 NE ARG A 74 2066 2238 2574 -174 66 -210 N ATOM 575 CZ ARG A 74 -18.870 -12.742 4.778 1.00 16.83 C ANISOU 575 CZ ARG A 74 1922 1764 2706 59 -91 -230 C ATOM 576 NH1 ARG A 74 -19.389 -13.658 5.596 1.00 17.37 N ANISOU 576 NH1 ARG A 74 1461 1966 3169 119 -166 -36 N ATOM 577 NH2 ARG A 74 -18.883 -12.946 3.459 1.00 17.68 N ANISOU 577 NH2 ARG A 74 1556 2459 2701 168 60 -247 N ATOM 578 N GLY A 75 -13.407 -11.815 9.948 1.00 15.43 N ANISOU 578 N GLY A 75 1624 1908 2328 -253 311 -499 N ATOM 579 CA GLY A 75 -12.515 -10.978 10.747 1.00 15.40 C ANISOU 579 CA GLY A 75 1519 2136 2195 -26 50 -330 C ATOM 580 C GLY A 75 -12.713 -9.499 10.396 1.00 18.02 C ANISOU 580 C GLY A 75 1802 2258 2787 -117 374 -787 C ATOM 581 O GLY A 75 -13.408 -9.145 9.455 1.00 17.79 O ANISOU 581 O GLY A 75 2018 1976 2764 63 376 -593 O ATOM 582 N PRO A 76 -12.033 -8.598 11.104 1.00 21.22 N ANISOU 582 N PRO A 76 2357 2603 3102 -343 374 -832 N ATOM 583 CA PRO A 76 -12.165 -7.170 10.757 1.00 21.89 C ANISOU 583 CA PRO A 76 2738 2557 3021 -87 478 -1169 C ATOM 584 C PRO A 76 -11.306 -6.797 9.539 1.00 20.75 C ANISOU 584 C PRO A 76 2363 2056 3463 -322 328 -410 C ATOM 585 O PRO A 76 -10.186 -7.278 9.424 1.00 25.89 O ANISOU 585 O PRO A 76 3217 3118 3502 -302 121 -262 O ATOM 586 CB PRO A 76 -11.675 -6.460 12.022 1.00 25.94 C ANISOU 586 CB PRO A 76 3227 3162 3465 -325 286 -1092 C ATOM 587 CG PRO A 76 -10.758 -7.468 12.683 1.00 26.39 C ANISOU 587 CG PRO A 76 3559 3031 3436 -35 222 -1405 C ATOM 588 CD PRO A 76 -11.341 -8.824 12.379 1.00 23.61 C ANISOU 588 CD PRO A 76 2800 3421 2747 -244 573 -1078 C ATOM 589 N GLY A 77 -11.935 -6.249 8.503 1.00 21.62 N ANISOU 589 N GLY A 77 2386 2564 3265 -280 591 -333 N ATOM 590 CA GLY A 77 -11.211 -5.765 7.321 1.00 22.24 C ANISOU 590 CA GLY A 77 2281 2494 3672 92 665 -303 C ATOM 591 C GLY A 77 -10.456 -6.861 6.599 1.00 21.05 C ANISOU 591 C GLY A 77 2438 2175 3383 -127 770 -176 C ATOM 592 O GLY A 77 -10.964 -7.963 6.395 1.00 23.28 O ANISOU 592 O GLY A 77 2713 2378 3754 -350 771 -442 O ATOM 593 N VAL A 78 -9.247 -6.547 6.178 1.00 19.55 N ANISOU 593 N VAL A 78 2119 1830 3478 -19 760 -220 N ATOM 594 CA VAL A 78 -8.426 -7.494 5.442 1.00 16.84 C ANISOU 594 CA VAL A 78 1842 1739 2817 90 305 -572 C ATOM 595 C VAL A 78 -6.938 -7.181 5.600 1.00 14.69 C ANISOU 595 C VAL A 78 1805 1372 2404 -70 142 -321 C ATOM 596 O VAL A 78 -6.429 -6.287 4.929 1.00 16.53 O ANISOU 596 O VAL A 78 1935 1782 2562 -63 290 -311 O ATOM 597 CB VAL A 78 -8.861 -7.573 3.940 1.00 18.04 C ANISOU 597 CB VAL A 78 2285 1800 2768 72 103 1 C ATOM 598 CG1 VAL A 78 -8.840 -6.218 3.209 1.00 23.51 C ANISOU 598 CG1 VAL A 78 3166 2312 3453 21 -276 10 C ATOM 599 CG2 VAL A 78 -8.096 -8.645 3.183 1.00 19.01 C ANISOU 599 CG2 VAL A 78 2290 2382 2548 237 -111 -295 C ATOM 600 N PRO A 79 -6.219 -7.906 6.489 1.00 15.53 N ANISOU 600 N PRO A 79 1687 1696 2516 -233 324 -296 N ATOM 601 CA PRO A 79 -4.814 -7.605 6.758 1.00 15.58 C ANISOU 601 CA PRO A 79 1788 1936 2195 -71 145 -520 C ATOM 602 C PRO A 79 -3.855 -8.257 5.748 1.00 15.64 C ANISOU 602 C PRO A 79 1678 1869 2395 -128 121 -566 C ATOM 603 O PRO A 79 -2.908 -8.919 6.155 1.00 17.87 O ANISOU 603 O PRO A 79 1903 2481 2406 -92 131 -511 O ATOM 604 CB PRO A 79 -4.589 -8.196 8.155 1.00 18.46 C ANISOU 604 CB PRO A 79 2427 2113 2471 -199 277 -582 C ATOM 605 CG PRO A 79 -5.542 -9.326 8.230 1.00 19.79 C ANISOU 605 CG PRO A 79 2047 2441 3029 -164 29 -127 C ATOM 606 CD PRO A 79 -6.759 -8.891 7.449 1.00 19.64 C ANISOU 606 CD PRO A 79 2036 2427 2998 -34 368 232 C ATOM 607 N PHE A 80 -4.219 -8.238 4.472 1.00 15.35 N ANISOU 607 N PHE A 80 1548 2140 2141 212 281 -198 N ATOM 608 CA PHE A 80 -3.400 -8.810 3.401 1.00 15.62 C ANISOU 608 CA PHE A 80 1671 2233 2029 231 327 -128 C ATOM 609 C PHE A 80 -3.480 -7.830 2.253 1.00 15.98 C ANISOU 609 C PHE A 80 1540 2203 2328 360 354 1 C ATOM 610 O PHE A 80 -4.479 -7.115 2.116 1.00 20.50 O ANISOU 610 O PHE A 80 1844 3062 2880 879 477 193 O ATOM 611 CB PHE A 80 -3.966 -10.156 2.919 1.00 16.02 C ANISOU 611 CB PHE A 80 1833 2050 2203 20 -83 -36 C ATOM 612 CG PHE A 80 -3.986 -11.240 3.970 1.00 13.89 C ANISOU 612 CG PHE A 80 1479 2050 1749 23 -25 -174 C ATOM 613 CD1 PHE A 80 -2.865 -12.032 4.177 1.00 14.10 C ANISOU 613 CD1 PHE A 80 1528 1941 1887 230 -236 -385 C ATOM 614 CD2 PHE A 80 -5.082 -11.400 4.818 1.00 14.11 C ANISOU 614 CD2 PHE A 80 1418 1921 2019 -160 -206 -331 C ATOM 615 CE1 PHE A 80 -2.842 -12.998 5.161 1.00 14.61 C ANISOU 615 CE1 PHE A 80 1531 2021 1997 -39 6 -232 C ATOM 616 CE2 PHE A 80 -5.075 -12.376 5.797 1.00 15.44 C ANISOU 616 CE2 PHE A 80 1563 1967 2333 -195 -98 -190 C ATOM 617 CZ PHE A 80 -3.944 -13.184 5.978 1.00 14.04 C ANISOU 617 CZ PHE A 80 1551 1690 2093 -42 -70 -327 C ATOM 618 N GLN A 81 -2.448 -7.802 1.416 1.00 16.48 N ANISOU 618 N GLN A 81 1619 2266 2377 316 199 -167 N ATOM 619 CA GLN A 81 -2.445 -6.909 0.258 1.00 16.58 C ANISOU 619 CA GLN A 81 1724 2250 2324 239 270 -56 C ATOM 620 C GLN A 81 -1.776 -7.619 -0.924 1.00 16.03 C ANISOU 620 C GLN A 81 1710 2133 2245 168 101 -60 C ATOM 621 O GLN A 81 -0.725 -8.265 -0.764 1.00 15.18 O ANISOU 621 O GLN A 81 1702 1762 2301 237 92 110 O ATOM 622 CB GLN A 81 -1.631 -5.645 0.528 1.00 19.89 C ANISOU 622 CB GLN A 81 2156 2620 2781 232 436 -280 C ATOM 623 CG GLN A 81 -1.993 -4.855 1.755 1.00 27.46 C ANISOU 623 CG GLN A 81 3354 3561 3518 -18 611 -253 C ATOM 624 CD GLN A 81 -1.240 -3.537 1.802 1.00 39.76 C ANISOU 624 CD GLN A 81 5673 4307 5125 -402 77 -481 C ATOM 625 OE1 GLN A 81 -0.836 -3.077 2.874 1.00 48.54 O ANISOU 625 OE1 GLN A 81 6769 5500 6173 -619 -539 -443 O ATOM 626 NE2 GLN A 81 -0.937 -2.989 0.623 1.00 41.68 N ANISOU 626 NE2 GLN A 81 6369 3847 5617 -117 -725 443 N ATOM 627 N ARG A 82 -2.347 -7.459 -2.110 1.00 15.21 N ANISOU 627 N ARG A 82 1639 2084 2056 65 177 93 N ATOM 628 CA ARG A 82 -1.676 -7.887 -3.334 1.00 15.03 C ANISOU 628 CA ARG A 82 1620 1951 2139 136 86 29 C ATOM 629 C ARG A 82 -0.292 -7.262 -3.404 1.00 14.13 C ANISOU 629 C ARG A 82 1603 1813 1951 170 16 -47 C ATOM 630 O ARG A 82 -0.140 -6.072 -3.174 1.00 15.88 O ANISOU 630 O ARG A 82 1678 1829 2526 259 6 -14 O ATOM 631 CB ARG A 82 -2.507 -7.473 -4.541 1.00 15.15 C ANISOU 631 CB ARG A 82 1606 2000 2147 -60 -236 116 C ATOM 632 CG ARG A 82 -3.829 -8.201 -4.641 1.00 16.75 C ANISOU 632 CG ARG A 82 1782 1918 2661 50 -69 300 C ATOM 633 CD ARG A 82 -4.706 -7.564 -5.725 1.00 18.08 C ANISOU 633 CD ARG A 82 1963 2031 2874 -443 -66 298 C ATOM 634 NE ARG A 82 -5.953 -8.308 -5.915 1.00 16.47 N ANISOU 634 NE ARG A 82 1965 1959 2332 -80 3 186 N ATOM 635 CZ ARG A 82 -7.163 -7.773 -6.077 1.00 23.06 C ANISOU 635 CZ ARG A 82 2231 2299 4230 4 -134 531 C ATOM 636 NH1 ARG A 82 -7.345 -6.474 -5.937 1.00 26.26 N ANISOU 636 NH1 ARG A 82 2583 2352 5043 154 602 581 N ATOM 637 NH2 ARG A 82 -8.212 -8.562 -6.262 1.00 21.40 N ANISOU 637 NH2 ARG A 82 1848 2683 3600 -237 -11 387 N ATOM 638 N GLY A 83 0.707 -8.085 -3.701 1.00 13.46 N ANISOU 638 N GLY A 83 1366 1860 1887 224 -100 149 N ATOM 639 CA GLY A 83 2.076 -7.608 -3.839 1.00 13.70 C ANISOU 639 CA GLY A 83 1436 1725 2041 195 11 200 C ATOM 640 C GLY A 83 2.831 -7.526 -2.524 1.00 14.16 C ANISOU 640 C GLY A 83 1626 1638 2114 -111 -4 -185 C ATOM 641 O GLY A 83 3.919 -6.951 -2.492 1.00 15.10 O ANISOU 641 O GLY A 83 1599 1798 2338 -157 278 -88 O ATOM 642 N GLN A 84 2.248 -8.030 -1.431 1.00 13.90 N ANISOU 642 N GLN A 84 1658 1480 2144 190 71 28 N ATOM 643 CA GLN A 84 2.949 -8.003 -0.146 1.00 13.92 C ANISOU 643 CA GLN A 84 1779 1415 2093 253 59 -153 C ATOM 644 C GLN A 84 3.051 -9.370 0.519 1.00 13.27 C ANISOU 644 C GLN A 84 1495 1618 1928 -61 -15 -61 C ATOM 645 O GLN A 84 2.104 -10.157 0.454 1.00 12.82 O ANISOU 645 O GLN A 84 1420 1530 1918 4 109 -204 O ATOM 646 CB GLN A 84 2.288 -7.011 0.831 1.00 17.25 C ANISOU 646 CB GLN A 84 2155 1875 2521 198 123 -135 C ATOM 647 CG GLN A 84 2.212 -5.562 0.333 1.00 18.85 C ANISOU 647 CG GLN A 84 2185 1642 3335 185 301 -357 C ATOM 648 CD GLN A 84 3.558 -4.909 0.077 1.00 18.85 C ANISOU 648 CD GLN A 84 2454 2003 2703 192 -86 -119 C ATOM 649 OE1 GLN A 84 4.548 -5.226 0.727 1.00 24.36 O ANISOU 649 OE1 GLN A 84 3002 2221 4031 -150 -363 -268 O ATOM 650 NE2 GLN A 84 3.602 -4.022 -0.904 1.00 19.14 N ANISOU 650 NE2 GLN A 84 2706 1601 2964 147 326 -300 N ATOM 651 N PRO A 85 4.194 -9.647 1.173 1.00 13.26 N ANISOU 651 N PRO A 85 1438 1636 1961 8 72 -39 N ATOM 652 CA PRO A 85 4.351 -10.890 1.933 1.00 12.67 C ANISOU 652 CA PRO A 85 1306 1638 1869 51 70 -61 C ATOM 653 C PRO A 85 3.584 -10.845 3.249 1.00 11.99 C ANISOU 653 C PRO A 85 1348 1601 1605 15 -110 -157 C ATOM 654 O PRO A 85 3.269 -9.772 3.757 1.00 14.99 O ANISOU 654 O PRO A 85 1902 1765 2028 32 -7 -110 O ATOM 655 CB PRO A 85 5.865 -10.962 2.184 1.00 15.69 C ANISOU 655 CB PRO A 85 1506 2091 2365 157 17 -56 C ATOM 656 CG PRO A 85 6.297 -9.509 2.210 1.00 17.46 C ANISOU 656 CG PRO A 85 1923 1992 2717 99 -493 149 C ATOM 657 CD PRO A 85 5.409 -8.803 1.217 1.00 14.35 C ANISOU 657 CD PRO A 85 1457 1739 2256 -282 -202 88 C ATOM 658 N PHE A 86 3.308 -12.019 3.796 1.00 11.93 N ANISOU 658 N PHE A 86 1475 1523 1532 -64 -69 -51 N ATOM 659 CA PHE A 86 2.569 -12.112 5.042 1.00 11.00 C ANISOU 659 CA PHE A 86 1180 1568 1430 -78 -145 -242 C ATOM 660 C PHE A 86 3.096 -13.255 5.886 1.00 11.85 C ANISOU 660 C PHE A 86 1206 1598 1698 13 16 -369 C ATOM 661 O PHE A 86 3.779 -14.159 5.381 1.00 11.93 O ANISOU 661 O PHE A 86 1273 1682 1577 83 -70 -241 O ATOM 662 CB PHE A 86 1.071 -12.355 4.768 1.00 13.55 C ANISOU 662 CB PHE A 86 1460 1677 2011 193 -219 -201 C ATOM 663 CG PHE A 86 0.778 -13.683 4.086 1.00 12.27 C ANISOU 663 CG PHE A 86 1244 1849 1567 -74 -94 -314 C ATOM 664 CD1 PHE A 86 0.599 -14.844 4.826 1.00 12.82 C ANISOU 664 CD1 PHE A 86 1533 1582 1756 -57 -34 -62 C ATOM 665 CD2 PHE A 86 0.761 -13.772 2.708 1.00 13.95 C ANISOU 665 CD2 PHE A 86 1610 1903 1786 43 -210 -300 C ATOM 666 CE1 PHE A 86 0.401 -16.072 4.213 1.00 13.54 C ANISOU 666 CE1 PHE A 86 1536 1955 1653 -10 -362 -299 C ATOM 667 CE2 PHE A 86 0.578 -14.983 2.095 1.00 14.78 C ANISOU 667 CE2 PHE A 86 1857 2033 1725 -371 -179 -127 C ATOM 668 CZ PHE A 86 0.379 -16.136 2.841 1.00 13.84 C ANISOU 668 CZ PHE A 86 1695 1955 1607 -118 -158 -215 C ATOM 669 N GLU A 87 2.687 -13.246 7.158 1.00 13.05 N ANISOU 669 N GLU A 87 1748 1686 1522 -46 -173 -254 N ATOM 670 CA GLU A 87 2.836 -14.389 8.027 1.00 13.14 C ANISOU 670 CA GLU A 87 1663 1843 1484 -1 -93 -226 C ATOM 671 C GLU A 87 1.559 -14.597 8.825 1.00 13.84 C ANISOU 671 C GLU A 87 1714 1767 1776 129 196 -279 C ATOM 672 O GLU A 87 1.044 -13.678 9.474 1.00 16.26 O ANISOU 672 O GLU A 87 2135 1750 2291 202 199 -489 O ATOM 673 CB GLU A 87 4.008 -14.212 8.981 1.00 15.10 C ANISOU 673 CB GLU A 87 1868 1967 1899 -24 -213 -326 C ATOM 674 CG GLU A 87 4.154 -15.387 9.954 1.00 16.79 C ANISOU 674 CG GLU A 87 2066 2584 1730 -18 -408 -152 C ATOM 675 CD GLU A 87 5.308 -15.167 10.912 1.00 24.36 C ANISOU 675 CD GLU A 87 3103 3375 2776 603 -855 -551 C ATOM 676 OE1 GLU A 87 5.458 -14.025 11.404 1.00 35.54 O ANISOU 676 OE1 GLU A 87 5094 3767 4641 889 -1480 -844 O ATOM 677 OE2 GLU A 87 6.133 -16.082 11.090 1.00 21.50 O ANISOU 677 OE2 GLU A 87 2554 3271 2343 748 -408 -331 O ATOM 678 N VAL A 88 1.026 -15.813 8.766 1.00 13.53 N ANISOU 678 N VAL A 88 1314 1940 1885 -10 55 -216 N ATOM 679 CA VAL A 88 -0.128 -16.201 9.565 1.00 12.56 C ANISOU 679 CA VAL A 88 1431 1735 1606 53 67 -137 C ATOM 680 C VAL A 88 0.248 -17.322 10.522 1.00 13.71 C ANISOU 680 C VAL A 88 1489 2043 1674 12 187 -296 C ATOM 681 O VAL A 88 0.912 -18.280 10.125 1.00 14.12 O ANISOU 681 O VAL A 88 1576 2016 1771 12 166 -326 O ATOM 682 CB VAL A 88 -1.269 -16.699 8.638 1.00 14.97 C ANISOU 682 CB VAL A 88 1520 2176 1990 -74 152 3 C ATOM 683 CG1 VAL A 88 -2.395 -17.317 9.428 1.00 19.18 C ANISOU 683 CG1 VAL A 88 2151 2810 2325 -225 85 38 C ATOM 684 CG2 VAL A 88 -1.773 -15.585 7.754 1.00 17.45 C ANISOU 684 CG2 VAL A 88 1965 2059 2604 102 324 7 C ATOM 685 N ALEU A 89 -0.166 -17.185 11.782 0.50 12.76 N ANISOU 685 N ALEU A 89 1388 2086 1373 -209 24 -287 N ATOM 686 N BLEU A 89 -0.208 -17.218 11.770 0.50 13.89 N ANISOU 686 N BLEU A 89 1545 2230 1500 -210 0 -302 N ATOM 687 CA ALEU A 89 -0.249 -18.321 12.701 0.50 12.25 C ANISOU 687 CA ALEU A 89 1268 1909 1476 -169 -95 -297 C ATOM 688 CA BLEU A 89 -0.226 -18.367 12.673 0.50 15.03 C ANISOU 688 CA BLEU A 89 1679 2162 1869 -192 -152 -339 C ATOM 689 C ALEU A 89 -1.704 -18.734 12.763 0.50 11.46 C ANISOU 689 C ALEU A 89 1301 1794 1259 -33 -53 -269 C ATOM 690 C BLEU A 89 -1.655 -18.775 12.992 0.50 14.12 C ANISOU 690 C BLEU A 89 1609 1967 1788 -124 -66 -352 C ATOM 691 O ALEU A 89 -2.587 -17.862 12.847 0.50 9.31 O ANISOU 691 O ALEU A 89 1139 1672 725 11 -227 -255 O ATOM 692 O BLEU A 89 -2.466 -17.979 13.493 0.50 14.26 O ANISOU 692 O BLEU A 89 1852 1808 1757 -75 87 -539 O ATOM 693 CB ALEU A 89 0.199 -17.920 14.112 0.50 11.83 C ANISOU 693 CB ALEU A 89 1264 1971 1258 -189 69 -409 C ATOM 694 CB BLEU A 89 0.530 -18.082 13.973 0.50 16.90 C ANISOU 694 CB BLEU A 89 2086 2341 1993 -139 -207 -619 C ATOM 695 CG ALEU A 89 1.582 -17.259 14.214 0.50 10.61 C ANISOU 695 CG ALEU A 89 1056 1752 1220 -385 -10 -668 C ATOM 696 CG BLEU A 89 1.906 -17.423 13.848 0.50 22.21 C ANISOU 696 CG BLEU A 89 2184 3368 2884 -235 -255 -442 C ATOM 697 CD1ALEU A 89 2.051 -17.179 15.665 0.50 12.19 C ANISOU 697 CD1ALEU A 89 1635 1627 1368 -372 -511 -476 C ATOM 698 CD1BLEU A 89 2.072 -16.366 14.921 0.50 29.69 C ANISOU 698 CD1BLEU A 89 3202 3932 4145 -73 62 -846 C ATOM 699 CD2ALEU A 89 2.620 -17.997 13.332 0.50 11.88 C ANISOU 699 CD2ALEU A 89 968 2042 1505 395 -630 -415 C ATOM 700 CD2BLEU A 89 3.017 -18.462 13.948 0.50 24.06 C ANISOU 700 CD2BLEU A 89 1953 3488 3697 61 524 -261 C ATOM 701 N ILE A 90 -1.929 -20.053 12.773 1.00 13.56 N ANISOU 701 N ILE A 90 1562 1894 1697 -55 -8 -303 N ATOM 702 CA ILE A 90 -3.178 -20.653 13.247 1.00 14.43 C ANISOU 702 CA ILE A 90 1777 2043 1661 -223 215 -175 C ATOM 703 C ILE A 90 -2.812 -21.506 14.452 1.00 12.79 C ANISOU 703 C ILE A 90 1291 1823 1745 -30 -75 -370 C ATOM 704 O ILE A 90 -2.056 -22.461 14.335 1.00 14.40 O ANISOU 704 O ILE A 90 1677 2066 1729 -9 61 -400 O ATOM 705 CB ILE A 90 -3.850 -21.512 12.150 1.00 14.56 C ANISOU 705 CB ILE A 90 1674 2009 1848 -258 69 -199 C ATOM 706 CG1 ILE A 90 -4.112 -20.697 10.886 1.00 17.01 C ANISOU 706 CG1 ILE A 90 1825 2340 2296 10 -258 -213 C ATOM 707 CG2 ILE A 90 -5.092 -22.188 12.677 1.00 15.61 C ANISOU 707 CG2 ILE A 90 1831 2350 1747 -305 -128 -122 C ATOM 708 CD1 ILE A 90 -5.118 -19.605 10.995 1.00 21.03 C ANISOU 708 CD1 ILE A 90 2933 2501 2553 -192 -180 -787 C ATOM 709 N ILE A 91 -3.352 -21.143 15.617 1.00 13.35 N ANISOU 709 N ILE A 91 1408 2218 1446 -141 -101 -213 N ATOM 710 CA ILE A 91 -2.933 -21.765 16.866 1.00 14.52 C ANISOU 710 CA ILE A 91 1820 2186 1509 -225 45 -286 C ATOM 711 C ILE A 91 -4.135 -22.550 17.399 1.00 14.33 C ANISOU 711 C ILE A 91 1642 2239 1560 -25 198 -224 C ATOM 712 O ILE A 91 -5.188 -21.969 17.633 1.00 16.56 O ANISOU 712 O ILE A 91 1768 2337 2187 -25 239 -195 O ATOM 713 CB ILE A 91 -2.499 -20.704 17.911 1.00 15.43 C ANISOU 713 CB ILE A 91 1839 2123 1899 -83 15 -201 C ATOM 714 CG1 ILE A 91 -1.428 -19.774 17.339 1.00 17.04 C ANISOU 714 CG1 ILE A 91 1888 2768 1816 -638 -30 -414 C ATOM 715 CG2 ILE A 91 -2.069 -21.373 19.198 1.00 18.88 C ANISOU 715 CG2 ILE A 91 2414 2692 2065 -440 -281 -241 C ATOM 716 CD1 ILE A 91 -1.136 -18.569 18.227 1.00 18.89 C ANISOU 716 CD1 ILE A 91 2823 1833 2522 -114 -317 -425 C ATOM 717 N ALA A 92 -3.955 -23.837 17.683 1.00 15.97 N ANISOU 717 N ALA A 92 1854 2403 1811 -209 129 -259 N ATOM 718 CA ALA A 92 -5.027 -24.659 18.258 1.00 15.84 C ANISOU 718 CA ALA A 92 1921 2315 1779 -155 167 -345 C ATOM 719 C ALA A 92 -4.967 -24.659 19.781 1.00 16.10 C ANISOU 719 C ALA A 92 1736 2611 1769 -177 -142 -391 C ATOM 720 O ALA A 92 -3.926 -24.942 20.361 1.00 17.21 O ANISOU 720 O ALA A 92 1897 2617 2025 -212 -244 -52 O ATOM 721 CB ALA A 92 -4.938 -26.091 17.737 1.00 17.82 C ANISOU 721 CB ALA A 92 2126 2232 2413 -198 -57 -551 C ATOM 722 N SER A 93 -6.101 -24.420 20.422 1.00 17.84 N ANISOU 722 N SER A 93 2035 3025 1715 -261 78 -294 N ATOM 723 CA SER A 93 -6.233 -24.572 21.875 1.00 17.99 C ANISOU 723 CA SER A 93 2286 2946 1601 72 76 -280 C ATOM 724 C SER A 93 -7.350 -25.584 22.132 1.00 20.01 C ANISOU 724 C SER A 93 2336 3276 1991 1 200 -310 C ATOM 725 O SER A 93 -7.917 -26.129 21.182 1.00 18.45 O ANISOU 725 O SER A 93 2565 2774 1668 -105 162 -147 O ATOM 726 CB SER A 93 -6.579 -23.228 22.499 1.00 19.55 C ANISOU 726 CB SER A 93 2322 3215 1891 96 -232 -463 C ATOM 727 OG SER A 93 -7.922 -22.861 22.194 1.00 21.39 O ANISOU 727 OG SER A 93 2296 3577 2252 -198 -208 -343 O ATOM 728 N ASP A 94 -7.744 -25.764 23.395 1.00 19.77 N ANISOU 728 N ASP A 94 2429 3343 1740 3 172 48 N ATOM 729 CA ASP A 94 -8.902 -26.608 23.703 1.00 22.44 C ANISOU 729 CA ASP A 94 2790 3672 2063 -59 128 325 C ATOM 730 C ASP A 94 -10.202 -25.981 23.209 1.00 20.45 C ANISOU 730 C ASP A 94 2392 3349 2026 -233 276 -30 C ATOM 731 O ASP A 94 -11.206 -26.675 23.052 1.00 22.68 O ANISOU 731 O ASP A 94 2735 3585 2295 -165 306 91 O ATOM 732 CB ASP A 94 -9.034 -26.859 25.216 1.00 23.49 C ANISOU 732 CB ASP A 94 2961 4198 1764 -360 55 798 C ATOM 733 CG ASP A 94 -7.913 -27.715 25.779 1.00 32.85 C ANISOU 733 CG ASP A 94 3927 4986 3566 -1 -62 211 C ATOM 734 OD1 ASP A 94 -7.829 -28.898 25.394 1.00 41.15 O ANISOU 734 OD1 ASP A 94 5592 5724 4318 650 561 -531 O ATOM 735 OD2 ASP A 94 -7.248 -27.271 26.746 1.00 42.64 O ANISOU 735 OD2 ASP A 94 4627 6188 5384 -691 -299 -219 O ATOM 736 N ASP A 95 -10.206 -24.660 23.047 1.00 20.38 N ANISOU 736 N ASP A 95 2541 3426 1775 21 262 -221 N ATOM 737 CA ASP A 95 -11.452 -23.940 22.797 1.00 21.26 C ANISOU 737 CA ASP A 95 2693 3375 2010 27 201 -392 C ATOM 738 C ASP A 95 -11.663 -23.572 21.338 1.00 18.74 C ANISOU 738 C ASP A 95 2045 3055 2018 -63 155 -182 C ATOM 739 O ASP A 95 -12.789 -23.369 20.901 1.00 19.01 O ANISOU 739 O ASP A 95 2313 3006 1901 53 23 -304 O ATOM 740 CB ASP A 95 -11.540 -22.698 23.675 1.00 23.28 C ANISOU 740 CB ASP A 95 3292 3417 2137 -115 237 -359 C ATOM 741 CG ASP A 95 -11.351 -23.025 25.146 1.00 31.81 C ANISOU 741 CG ASP A 95 4466 4999 2619 -169 270 -661 C ATOM 742 OD1 ASP A 95 -12.025 -23.959 25.638 1.00 41.21 O ANISOU 742 OD1 ASP A 95 5793 5918 3945 -418 343 -108 O ATOM 743 OD2 ASP A 95 -10.420 -22.464 25.763 1.00 41.26 O ANISOU 743 OD2 ASP A 95 4916 6666 4093 -466 -730 -1062 O ATOM 744 N GLY A 96 -10.583 -23.433 20.585 1.00 16.93 N ANISOU 744 N GLY A 96 2020 2594 1818 -9 243 -245 N ATOM 745 CA GLY A 96 -10.747 -22.986 19.205 1.00 18.41 C ANISOU 745 CA GLY A 96 2099 2762 2133 135 103 -154 C ATOM 746 C GLY A 96 -9.410 -22.738 18.558 1.00 15.57 C ANISOU 746 C GLY A 96 1750 2410 1755 84 129 -225 C ATOM 747 O GLY A 96 -8.376 -23.258 19.012 1.00 17.61 O ANISOU 747 O GLY A 96 2035 2897 1759 107 189 -92 O ATOM 748 N PHE A 97 -9.443 -22.009 17.454 1.00 16.01 N ANISOU 748 N PHE A 97 1937 2535 1610 -5 237 -106 N ATOM 749 CA PHE A 97 -8.259 -21.638 16.698 1.00 15.81 C ANISOU 749 CA PHE A 97 1624 2482 1900 -193 231 -289 C ATOM 750 C PHE A 97 -8.096 -20.134 16.778 1.00 17.13 C ANISOU 750 C PHE A 97 1961 2397 2151 4 -65 -174 C ATOM 751 O PHE A 97 -9.032 -19.381 16.475 1.00 19.40 O ANISOU 751 O PHE A 97 1945 2384 3042 -141 -361 -282 O ATOM 752 CB PHE A 97 -8.414 -22.008 15.214 1.00 14.95 C ANISOU 752 CB PHE A 97 1920 2166 1591 -187 150 -40 C ATOM 753 CG PHE A 97 -8.612 -23.473 14.966 1.00 13.66 C ANISOU 753 CG PHE A 97 1667 2028 1493 -63 23 -240 C ATOM 754 CD1 PHE A 97 -7.553 -24.373 15.063 1.00 14.69 C ANISOU 754 CD1 PHE A 97 1872 2374 1335 78 240 -198 C ATOM 755 CD2 PHE A 97 -9.880 -23.968 14.630 1.00 16.22 C ANISOU 755 CD2 PHE A 97 1945 2332 1885 -408 -355 -253 C ATOM 756 CE1 PHE A 97 -7.751 -25.729 14.862 1.00 16.31 C ANISOU 756 CE1 PHE A 97 1970 2369 1858 -290 188 -184 C ATOM 757 CE2 PHE A 97 -10.086 -25.329 14.396 1.00 16.34 C ANISOU 757 CE2 PHE A 97 2196 2359 1651 -9 -84 -11 C ATOM 758 CZ PHE A 97 -9.034 -26.220 14.552 1.00 16.10 C ANISOU 758 CZ PHE A 97 2038 2634 1444 -105 128 -462 C ATOM 759 N LYS A 98 -6.896 -19.685 17.115 1.00 15.69 N ANISOU 759 N LYS A 98 1715 2334 1913 -140 138 -284 N ATOM 760 CA LYS A 98 -6.541 -18.267 17.071 1.00 15.62 C ANISOU 760 CA LYS A 98 1740 2219 1977 -34 59 -353 C ATOM 761 C LYS A 98 -5.770 -17.973 15.797 1.00 16.14 C ANISOU 761 C LYS A 98 1756 2360 2013 -51 159 -437 C ATOM 762 O LYS A 98 -4.797 -18.680 15.480 1.00 19.01 O ANISOU 762 O LYS A 98 2060 2525 2635 304 337 -303 O ATOM 763 CB LYS A 98 -5.668 -17.908 18.268 1.00 19.18 C ANISOU 763 CB LYS A 98 2207 2837 2241 -283 -30 -268 C ATOM 764 CG LYS A 98 -6.435 -17.941 19.569 1.00 25.01 C ANISOU 764 CG LYS A 98 2666 4243 2594 -1007 125 -792 C ATOM 765 CD LYS A 98 -5.477 -17.776 20.739 1.00 27.59 C ANISOU 765 CD LYS A 98 3612 5050 1818 -548 270 -941 C ATOM 766 CE LYS A 98 -4.543 -18.983 20.830 1.00 36.96 C ANISOU 766 CE LYS A 98 3434 5515 5093 -423 -534 -280 C ATOM 767 NZ LYS A 98 -3.568 -18.888 21.950 1.00 36.21 N ANISOU 767 NZ LYS A 98 3758 5387 4611 205 -317 121 N ATOM 768 N ALA A 99 -6.242 -16.997 15.024 1.00 14.16 N ANISOU 768 N ALA A 99 1540 2084 1753 -157 -41 -362 N ATOM 769 CA ALA A 99 -5.501 -16.524 13.851 1.00 14.24 C ANISOU 769 CA ALA A 99 1545 2101 1763 -205 72 -529 C ATOM 770 C ALA A 99 -4.734 -15.275 14.177 1.00 15.44 C ANISOU 770 C ALA A 99 1772 2153 1938 19 138 -760 C ATOM 771 O ALA A 99 -5.306 -14.330 14.721 1.00 16.01 O ANISOU 771 O ALA A 99 1761 2265 2053 126 86 -799 O ATOM 772 CB ALA A 99 -6.447 -16.265 12.683 1.00 14.62 C ANISOU 772 CB ALA A 99 1705 2044 1802 39 -196 -496 C ATOM 773 N VAL A 100 -3.424 -15.324 13.946 1.00 13.69 N ANISOU 773 N VAL A 100 1558 2016 1626 -137 113 -445 N ATOM 774 CA VAL A 100 -2.540 -14.172 14.149 1.00 14.67 C ANISOU 774 CA VAL A 100 1560 2038 1976 -61 -3 -412 C ATOM 775 C VAL A 100 -2.024 -13.787 12.770 1.00 15.16 C ANISOU 775 C VAL A 100 1766 2131 1860 -32 119 -426 C ATOM 776 O VAL A 100 -1.595 -14.656 12.013 1.00 15.73 O ANISOU 776 O VAL A 100 2027 1811 2137 143 158 -436 O ATOM 777 CB VAL A 100 -1.344 -14.542 15.089 1.00 15.48 C ANISOU 777 CB VAL A 100 1634 2318 1929 -135 -36 -368 C ATOM 778 CG1 VAL A 100 -0.381 -13.386 15.238 1.00 18.17 C ANISOU 778 CG1 VAL A 100 2080 2608 2213 -615 -147 -685 C ATOM 779 CG2 VAL A 100 -1.865 -14.968 16.436 1.00 17.20 C ANISOU 779 CG2 VAL A 100 2084 2666 1785 -346 279 -374 C ATOM 780 N VAL A 101 -2.158 -12.515 12.394 1.00 14.97 N ANISOU 780 N VAL A 101 1770 1996 1922 -141 12 -434 N ATOM 781 CA VAL A 101 -1.618 -12.044 11.113 1.00 15.60 C ANISOU 781 CA VAL A 101 1668 2106 2152 -33 5 -405 C ATOM 782 C VAL A 101 -0.632 -10.916 11.386 1.00 16.39 C ANISOU 782 C VAL A 101 1991 2073 2161 6 -52 -581 C ATOM 783 O VAL A 101 -0.928 -9.991 12.139 1.00 17.70 O ANISOU 783 O VAL A 101 2248 2378 2099 37 -11 -674 O ATOM 784 CB VAL A 101 -2.740 -11.557 10.148 1.00 16.04 C ANISOU 784 CB VAL A 101 1870 2193 2030 3 69 -439 C ATOM 785 CG1 VAL A 101 -2.155 -11.216 8.785 1.00 16.77 C ANISOU 785 CG1 VAL A 101 2062 2667 1640 -202 -67 -252 C ATOM 786 CG2 VAL A 101 -3.848 -12.611 10.014 1.00 16.49 C ANISOU 786 CG2 VAL A 101 1711 2301 2253 0 -66 -619 C ATOM 787 N GLY A 102 0.576 -11.054 10.856 1.00 17.76 N ANISOU 787 N GLY A 102 2103 2499 2146 -334 66 -587 N ATOM 788 CA GLY A 102 1.659 -10.153 11.201 1.00 21.59 C ANISOU 788 CA GLY A 102 2335 3218 2647 -482 20 -578 C ATOM 789 C GLY A 102 1.932 -10.218 12.698 1.00 20.54 C ANISOU 789 C GLY A 102 2031 2752 3020 -84 -281 -441 C ATOM 790 O GLY A 102 2.133 -11.289 13.274 1.00 24.46 O ANISOU 790 O GLY A 102 2961 3587 2746 -304 -658 -532 O ATOM 791 N ASP A 103 1.932 -9.084 13.358 1.00 25.24 N ANISOU 791 N ASP A 103 2755 3960 2875 -330 -201 -572 N ATOM 792 CA ASP A 103 2.246 -9.144 14.765 1.00 26.56 C ANISOU 792 CA ASP A 103 3190 3724 3176 -416 -359 -536 C ATOM 793 C ASP A 103 0.992 -9.012 15.602 1.00 26.05 C ANISOU 793 C ASP A 103 3099 3645 3152 -719 -132 -613 C ATOM 794 O ASP A 103 1.056 -8.691 16.775 1.00 28.29 O ANISOU 794 O ASP A 103 3799 3769 3180 -968 -117 -655 O ATOM 795 CB ASP A 103 3.299 -8.098 15.138 1.00 29.89 C ANISOU 795 CB ASP A 103 3096 4417 3844 -560 -779 -510 C ATOM 796 CG ASP A 103 4.462 -8.690 15.921 1.00 33.59 C ANISOU 796 CG ASP A 103 3874 4391 4495 -413 -834 -454 C ATOM 797 OD1 ASP A 103 4.527 -9.931 16.062 1.00 39.43 O ANISOU 797 OD1 ASP A 103 4779 4748 5455 -88 -1090 -233 O ATOM 798 OD2 ASP A 103 5.279 -7.907 16.449 1.00 38.24 O ANISOU 798 OD2 ASP A 103 5021 3618 5888 -791 -1017 -315 O ATOM 799 N ALA A 104 -0.163 -9.325 15.025 1.00 22.32 N ANISOU 799 N ALA A 104 2298 3285 2897 -505 200 -882 N ATOM 800 CA ALA A 104 -1.390 -9.010 15.724 1.00 22.26 C ANISOU 800 CA ALA A 104 2725 2843 2889 -369 415 -1043 C ATOM 801 C ALA A 104 -2.373 -10.176 15.817 1.00 19.35 C ANISOU 801 C ALA A 104 2241 2646 2462 -345 482 -918 C ATOM 802 O ALA A 104 -2.721 -10.805 14.809 1.00 18.43 O ANISOU 802 O ALA A 104 2234 2692 2074 -213 226 -930 O ATOM 803 CB ALA A 104 -2.035 -7.810 15.090 1.00 25.32 C ANISOU 803 CB ALA A 104 3103 2743 3774 -239 744 -866 C ATOM 804 N GLN A 105 -2.959 -10.354 16.995 1.00 19.05 N ANISOU 804 N GLN A 105 2076 2708 2453 -346 345 -856 N ATOM 805 CA GLN A 105 -4.073 -11.264 17.124 1.00 16.83 C ANISOU 805 CA GLN A 105 2257 2101 2035 -303 175 -706 C ATOM 806 C GLN A 105 -5.223 -10.777 16.267 1.00 19.32 C ANISOU 806 C GLN A 105 2485 2482 2370 -22 255 -884 C ATOM 807 O GLN A 105 -5.545 -9.595 16.283 1.00 21.10 O ANISOU 807 O GLN A 105 2543 2414 3060 -19 -221 -1058 O ATOM 808 CB GLN A 105 -4.494 -11.375 18.592 1.00 19.57 C ANISOU 808 CB GLN A 105 2412 2912 2111 -618 71 -958 C ATOM 809 CG GLN A 105 -5.868 -12.026 18.828 1.00 23.06 C ANISOU 809 CG GLN A 105 2726 2728 3307 -482 172 -571 C ATOM 810 CD GLN A 105 -5.948 -13.485 18.367 1.00 24.04 C ANISOU 810 CD GLN A 105 2659 3032 3440 202 80 -644 C ATOM 811 OE1 GLN A 105 -4.947 -14.198 18.323 1.00 24.77 O ANISOU 811 OE1 GLN A 105 2793 2789 3827 203 118 -315 O ATOM 812 NE2 GLN A 105 -7.143 -13.915 17.973 1.00 25.31 N ANISOU 812 NE2 GLN A 105 2832 3740 3044 -603 -224 -283 N ATOM 813 N TYR A 106 -5.761 -11.661 15.434 1.00 16.64 N ANISOU 813 N TYR A 106 2135 2214 1973 -75 66 -587 N ATOM 814 CA TYR A 106 -6.719 -11.242 14.425 1.00 15.49 C ANISOU 814 CA TYR A 106 1896 2129 1858 -32 63 -407 C ATOM 815 C TYR A 106 -8.163 -11.750 14.640 1.00 15.83 C ANISOU 815 C TYR A 106 1802 2014 2197 16 354 -622 C ATOM 816 O TYR A 106 -9.128 -10.989 14.514 1.00 18.50 O ANISOU 816 O TYR A 106 1839 2439 2749 -23 344 -512 O ATOM 817 CB TYR A 106 -6.222 -11.625 13.030 1.00 16.15 C ANISOU 817 CB TYR A 106 2032 2195 1908 60 177 -625 C ATOM 818 CG TYR A 106 -7.164 -11.235 11.913 1.00 15.22 C ANISOU 818 CG TYR A 106 1825 1807 2151 85 237 -502 C ATOM 819 CD1 TYR A 106 -7.404 -9.897 11.604 1.00 15.84 C ANISOU 819 CD1 TYR A 106 1980 1808 2228 266 22 -461 C ATOM 820 CD2 TYR A 106 -7.804 -12.208 11.157 1.00 16.11 C ANISOU 820 CD2 TYR A 106 1719 2153 2248 -316 252 -518 C ATOM 821 CE1 TYR A 106 -8.285 -9.536 10.589 1.00 16.51 C ANISOU 821 CE1 TYR A 106 1835 1914 2523 -74 129 -171 C ATOM 822 CE2 TYR A 106 -8.680 -11.856 10.148 1.00 15.94 C ANISOU 822 CE2 TYR A 106 1871 2059 2123 -108 307 -572 C ATOM 823 CZ TYR A 106 -8.955 -10.528 9.904 1.00 17.17 C ANISOU 823 CZ TYR A 106 1893 2375 2255 216 115 -294 C ATOM 824 OH TYR A 106 -9.836 -10.161 8.908 1.00 18.97 O ANISOU 824 OH TYR A 106 2035 2844 2328 -202 28 -150 O ATOM 825 N HIS A 107 -8.324 -13.033 14.944 1.00 15.88 N ANISOU 825 N HIS A 107 1860 2136 2036 -132 142 -619 N ATOM 826 CA HIS A 107 -9.662 -13.634 15.113 1.00 15.96 C ANISOU 826 CA HIS A 107 1914 2202 1946 -27 130 -680 C ATOM 827 C HIS A 107 -9.557 -14.902 15.945 1.00 15.90 C ANISOU 827 C HIS A 107 1866 2070 2105 -130 156 -748 C ATOM 828 O HIS A 107 -8.571 -15.638 15.841 1.00 17.48 O ANISOU 828 O HIS A 107 1809 2450 2380 75 259 -478 O ATOM 829 CB HIS A 107 -10.284 -13.944 13.736 1.00 18.08 C ANISOU 829 CB HIS A 107 1689 2934 2246 -204 -165 -409 C ATOM 830 CG HIS A 107 -11.738 -14.295 13.779 1.00 17.50 C ANISOU 830 CG HIS A 107 1948 2356 2345 -93 195 -312 C ATOM 831 ND1 HIS A 107 -12.720 -13.336 13.873 1.00 22.75 N ANISOU 831 ND1 HIS A 107 1973 2708 3962 -45 -11 -253 N ATOM 832 CD2 HIS A 107 -12.379 -15.482 13.655 1.00 18.17 C ANISOU 832 CD2 HIS A 107 1876 2394 2630 38 -105 -385 C ATOM 833 CE1 HIS A 107 -13.905 -13.923 13.870 1.00 21.83 C ANISOU 833 CE1 HIS A 107 1649 2706 3938 -61 -81 -506 C ATOM 834 NE2 HIS A 107 -13.730 -15.223 13.724 1.00 18.67 N ANISOU 834 NE2 HIS A 107 1756 2775 2562 147 -28 -365 N ATOM 835 N HIS A 108 -10.595 -15.182 16.732 1.00 16.32 N ANISOU 835 N HIS A 108 2068 2148 1985 -17 218 -543 N ATOM 836 CA HIS A 108 -10.751 -16.474 17.394 1.00 16.87 C ANISOU 836 CA HIS A 108 2073 2330 2005 -236 324 -599 C ATOM 837 C HIS A 108 -11.958 -17.187 16.808 1.00 17.48 C ANISOU 837 C HIS A 108 2003 2460 2179 -9 323 -652 C ATOM 838 O HIS A 108 -13.078 -16.675 16.832 1.00 18.01 O ANISOU 838 O HIS A 108 1987 2391 2465 96 167 -702 O ATOM 839 CB HIS A 108 -10.971 -16.313 18.902 1.00 20.16 C ANISOU 839 CB HIS A 108 2729 2799 2131 -72 177 -670 C ATOM 840 CG HIS A 108 -10.990 -17.623 19.632 1.00 24.57 C ANISOU 840 CG HIS A 108 3047 3311 2977 -295 458 -417 C ATOM 841 ND1 HIS A 108 -12.158 -18.193 20.097 1.00 33.17 N ANISOU 841 ND1 HIS A 108 3923 4465 4215 -115 406 -250 N ATOM 842 CD2 HIS A 108 -10.033 -18.570 19.776 1.00 27.44 C ANISOU 842 CD2 HIS A 108 2806 4168 3451 -324 31 -21 C ATOM 843 CE1 HIS A 108 -11.888 -19.376 20.623 1.00 34.38 C ANISOU 843 CE1 HIS A 108 4500 4182 4378 549 654 -45 C ATOM 844 NE2 HIS A 108 -10.598 -19.618 20.461 1.00 30.49 N ANISOU 844 NE2 HIS A 108 3985 3534 4063 226 -558 380 N ATOM 845 N PHE A 109 -11.730 -18.401 16.330 1.00 16.69 N ANISOU 845 N PHE A 109 1997 2165 2179 -226 -39 -624 N ATOM 846 CA PHE A 109 -12.787 -19.240 15.756 1.00 15.29 C ANISOU 846 CA PHE A 109 1869 2115 1826 -270 -187 -456 C ATOM 847 C PHE A 109 -13.019 -20.422 16.701 1.00 15.23 C ANISOU 847 C PHE A 109 1762 2174 1850 -27 87 -330 C ATOM 848 O PHE A 109 -12.141 -21.300 16.830 1.00 16.34 O ANISOU 848 O PHE A 109 1810 2404 1994 -6 -58 -236 O ATOM 849 CB PHE A 109 -12.324 -19.725 14.370 1.00 14.69 C ANISOU 849 CB PHE A 109 1622 2296 1661 -219 66 -625 C ATOM 850 CG PHE A 109 -13.365 -20.496 13.577 1.00 13.69 C ANISOU 850 CG PHE A 109 1672 1853 1675 -69 23 -337 C ATOM 851 CD1 PHE A 109 -14.323 -19.822 12.862 1.00 15.47 C ANISOU 851 CD1 PHE A 109 1470 2387 2022 -194 234 -271 C ATOM 852 CD2 PHE A 109 -13.385 -21.887 13.568 1.00 16.24 C ANISOU 852 CD2 PHE A 109 1770 2046 2351 -125 -149 -494 C ATOM 853 CE1 PHE A 109 -15.264 -20.501 12.114 1.00 15.81 C ANISOU 853 CE1 PHE A 109 1927 2351 1729 -213 196 -95 C ATOM 854 CE2 PHE A 109 -14.343 -22.579 12.845 1.00 15.56 C ANISOU 854 CE2 PHE A 109 1606 2204 2100 110 35 -306 C ATOM 855 CZ PHE A 109 -15.278 -21.883 12.104 1.00 14.96 C ANISOU 855 CZ PHE A 109 1709 2104 1868 -21 111 -228 C ATOM 856 N AARG A 110 -14.151 -20.407 17.408 0.50 15.31 N ANISOU 856 N AARG A 110 1720 2397 1699 -228 88 -427 N ATOM 857 N BARG A 110 -14.137 -20.408 17.431 0.50 15.57 N ANISOU 857 N BARG A 110 1765 2411 1739 -236 70 -417 N ATOM 858 CA AARG A 110 -14.494 -21.487 18.342 0.50 15.75 C ANISOU 858 CA AARG A 110 1596 2408 1977 -173 220 -292 C ATOM 859 CA BARG A 110 -14.422 -21.503 18.365 0.50 16.75 C ANISOU 859 CA BARG A 110 1808 2481 2074 -181 149 -239 C ATOM 860 C AARG A 110 -14.605 -22.830 17.615 0.50 15.38 C ANISOU 860 C AARG A 110 1718 2418 1707 -308 215 -240 C ATOM 861 C BARG A 110 -14.569 -22.821 17.615 0.50 15.47 C ANISOU 861 C BARG A 110 1734 2421 1720 -330 190 -212 C ATOM 862 O AARG A 110 -15.175 -22.899 16.525 0.50 16.39 O ANISOU 862 O AARG A 110 1743 2531 1953 -168 14 -303 O ATOM 863 O BARG A 110 -15.125 -22.864 16.516 0.50 16.42 O ANISOU 863 O BARG A 110 1701 2551 1987 -204 19 -243 O ATOM 864 CB AARG A 110 -15.807 -21.161 19.067 0.50 17.25 C ANISOU 864 CB AARG A 110 1890 2727 1935 -132 514 -279 C ATOM 865 CB BARG A 110 -15.674 -21.224 19.207 0.50 18.30 C ANISOU 865 CB BARG A 110 1995 2843 2113 -194 262 -196 C ATOM 866 CG AARG A 110 -16.257 -22.199 20.099 0.50 16.29 C ANISOU 866 CG AARG A 110 1567 2868 1751 -433 433 -278 C ATOM 867 CG BARG A 110 -15.644 -21.818 20.628 0.50 23.46 C ANISOU 867 CG BARG A 110 2777 3586 2549 -236 -9 -41 C ATOM 868 CD AARG A 110 -17.210 -21.578 21.116 0.50 25.28 C ANISOU 868 CD AARG A 110 2681 4099 2823 -199 1024 -662 C ATOM 869 CD BARG A 110 -15.679 -23.353 20.641 0.50 27.33 C ANISOU 869 CD BARG A 110 3661 3912 2809 -522 -155 -46 C ATOM 870 NE AARG A 110 -17.489 -22.474 22.236 0.50 32.74 N ANISOU 870 NE AARG A 110 3765 5136 3538 108 744 -99 N ATOM 871 NE BARG A 110 -15.107 -23.928 21.867 0.50 30.48 N ANISOU 871 NE BARG A 110 4133 4225 3222 -655 328 551 N ATOM 872 CZ AARG A 110 -16.934 -22.370 23.443 0.50 33.21 C ANISOU 872 CZ AARG A 110 3868 5489 3259 -93 1097 -379 C ATOM 873 CZ BARG A 110 -14.995 -25.235 22.095 0.50 27.74 C ANISOU 873 CZ BARG A 110 3739 4001 2797 -891 369 661 C ATOM 874 NH1AARG A 110 -16.052 -21.410 23.696 0.50 35.49 N ANISOU 874 NH1AARG A 110 4332 5547 3604 103 372 -609 N ATOM 875 NH1BARG A 110 -15.472 -26.103 21.213 0.50 34.05 N ANISOU 875 NH1BARG A 110 5262 4261 3412 -922 1143 143 N ATOM 876 NH2AARG A 110 -17.260 -23.231 24.398 0.50 39.54 N ANISOU 876 NH2AARG A 110 5446 5603 3972 16 577 65 N ATOM 877 NH2BARG A 110 -14.425 -25.676 23.206 0.50 36.66 N ANISOU 877 NH2BARG A 110 4757 5104 4066 -763 65 511 N ATOM 878 N HIS A 111 -14.122 -23.909 18.230 1.00 15.77 N ANISOU 878 N HIS A 111 1836 2275 1878 -41 260 -275 N ATOM 879 CA HIS A 111 -14.257 -25.218 17.612 1.00 15.44 C ANISOU 879 CA HIS A 111 1873 2317 1676 -157 136 -245 C ATOM 880 C HIS A 111 -15.714 -25.502 17.305 1.00 16.21 C ANISOU 880 C HIS A 111 1765 2355 2036 -203 364 -192 C ATOM 881 O HIS A 111 -16.597 -25.334 18.161 1.00 18.81 O ANISOU 881 O HIS A 111 1982 2762 2403 -181 566 -437 O ATOM 882 CB HIS A 111 -13.707 -26.364 18.470 1.00 16.02 C ANISOU 882 CB HIS A 111 1901 2302 1883 -72 273 78 C ATOM 883 CG HIS A 111 -12.225 -26.344 18.642 1.00 15.39 C ANISOU 883 CG HIS A 111 1860 2193 1793 -22 176 -139 C ATOM 884 ND1 HIS A 111 -11.345 -26.215 17.586 1.00 15.98 N ANISOU 884 ND1 HIS A 111 1882 2262 1926 -67 90 -246 N ATOM 885 CD2 HIS A 111 -11.468 -26.413 19.761 1.00 19.67 C ANISOU 885 CD2 HIS A 111 2348 2995 2128 32 -49 -157 C ATOM 886 CE1 HIS A 111 -10.109 -26.210 18.051 1.00 17.36 C ANISOU 886 CE1 HIS A 111 2121 2582 1890 -104 -169 -510 C ATOM 887 NE2 HIS A 111 -10.154 -26.353 19.365 1.00 17.60 N ANISOU 887 NE2 HIS A 111 2309 2443 1935 132 227 -363 N ATOM 888 N ARG A 112 -15.946 -26.032 16.118 1.00 15.26 N ANISOU 888 N ARG A 112 1840 2162 1796 -114 125 -300 N ATOM 889 CA ARG A 112 -17.248 -26.587 15.765 1.00 14.96 C ANISOU 889 CA ARG A 112 1684 2192 1808 -64 20 -96 C ATOM 890 C ARG A 112 -17.168 -28.111 15.629 1.00 15.52 C ANISOU 890 C ARG A 112 1660 2166 2070 -275 204 -275 C ATOM 891 O ARG A 112 -18.019 -28.822 16.149 1.00 23.19 O ANISOU 891 O ARG A 112 2732 2568 3511 -587 951 -360 O ATOM 892 CB ARG A 112 -17.771 -25.931 14.485 1.00 16.76 C ANISOU 892 CB ARG A 112 1974 2249 2142 46 17 15 C ATOM 893 CG ARG A 112 -17.931 -24.431 14.633 1.00 17.49 C ANISOU 893 CG ARG A 112 2104 2149 2389 206 280 164 C ATOM 894 CD ARG A 112 -18.146 -23.815 13.292 1.00 18.53 C ANISOU 894 CD ARG A 112 2931 1975 2134 109 -52 -188 C ATOM 895 NE ARG A 112 -18.356 -22.380 13.324 1.00 14.75 N ANISOU 895 NE ARG A 112 1730 2046 1829 175 -33 -195 N ATOM 896 CZ ARG A 112 -18.765 -21.686 12.269 1.00 13.84 C ANISOU 896 CZ ARG A 112 1556 1831 1868 119 -259 -129 C ATOM 897 NH1 ARG A 112 -18.959 -22.303 11.117 1.00 14.68 N ANISOU 897 NH1 ARG A 112 1890 1804 1881 -165 -120 -209 N ATOM 898 NH2 ARG A 112 -18.939 -20.379 12.345 1.00 15.14 N ANISOU 898 NH2 ARG A 112 1990 1778 1982 106 -206 -113 N ATOM 899 N LEU A 113 -16.191 -28.610 14.881 1.00 16.18 N ANISOU 899 N LEU A 113 1971 1867 2307 -48 105 -116 N ATOM 900 CA LEU A 113 -15.875 -30.048 14.835 1.00 16.84 C ANISOU 900 CA LEU A 113 2073 2059 2264 21 113 115 C ATOM 901 C LEU A 113 -14.902 -30.306 15.989 1.00 15.67 C ANISOU 901 C LEU A 113 2061 1957 1934 -141 -31 -145 C ATOM 902 O LEU A 113 -14.123 -29.420 16.355 1.00 17.44 O ANISOU 902 O LEU A 113 2190 2282 2154 -222 -148 -57 O ATOM 903 CB LEU A 113 -15.192 -30.402 13.492 1.00 16.70 C ANISOU 903 CB LEU A 113 2309 2138 1895 -212 -269 130 C ATOM 904 CG LEU A 113 -16.009 -30.404 12.203 1.00 18.95 C ANISOU 904 CG LEU A 113 2252 2296 2650 -171 -19 -2 C ATOM 905 CD1 LEU A 113 -16.511 -28.993 11.920 1.00 19.57 C ANISOU 905 CD1 LEU A 113 2500 2405 2529 54 -54 -211 C ATOM 906 CD2 LEU A 113 -15.191 -30.946 11.035 1.00 21.71 C ANISOU 906 CD2 LEU A 113 2971 2771 2507 -18 -179 164 C ATOM 907 N PRO A 114 -14.844 -31.543 16.494 1.00 15.24 N ANISOU 907 N PRO A 114 1745 2148 1898 79 86 -67 N ATOM 908 CA PRO A 114 -13.763 -31.875 17.443 1.00 17.06 C ANISOU 908 CA PRO A 114 1966 2567 1945 -62 -42 26 C ATOM 909 C PRO A 114 -12.380 -31.772 16.797 1.00 15.78 C ANISOU 909 C PRO A 114 1892 2288 1816 -89 -81 -55 C ATOM 910 O PRO A 114 -12.158 -32.258 15.679 1.00 16.58 O ANISOU 910 O PRO A 114 1932 2566 1798 408 -237 -148 O ATOM 911 CB PRO A 114 -14.086 -33.322 17.867 1.00 18.14 C ANISOU 911 CB PRO A 114 2313 2376 2202 120 -155 416 C ATOM 912 CG PRO A 114 -15.542 -33.498 17.504 1.00 18.43 C ANISOU 912 CG PRO A 114 2621 2268 2112 275 -83 343 C ATOM 913 CD PRO A 114 -15.775 -32.664 16.284 1.00 17.08 C ANISOU 913 CD PRO A 114 2223 2281 1985 -246 -25 210 C ATOM 914 N LEU A 115 -11.479 -31.089 17.487 1.00 18.04 N ANISOU 914 N LEU A 115 1956 2953 1945 -48 -45 -196 N ATOM 915 CA LEU A 115 -10.107 -30.913 17.024 1.00 16.04 C ANISOU 915 CA LEU A 115 1835 2635 1624 -97 -244 -109 C ATOM 916 C LEU A 115 -9.459 -32.258 16.667 1.00 15.51 C ANISOU 916 C LEU A 115 1986 2366 1540 -118 -319 -12 C ATOM 917 O LEU A 115 -8.666 -32.351 15.715 1.00 16.07 O ANISOU 917 O LEU A 115 1806 2707 1590 145 -427 94 O ATOM 918 CB LEU A 115 -9.281 -30.172 18.090 1.00 18.17 C ANISOU 918 CB LEU A 115 2314 3052 1537 -125 -225 -169 C ATOM 919 CG LEU A 115 -7.802 -29.972 17.809 1.00 18.31 C ANISOU 919 CG LEU A 115 2376 3030 1548 -245 -419 -211 C ATOM 920 CD1 LEU A 115 -7.665 -29.037 16.640 1.00 19.21 C ANISOU 920 CD1 LEU A 115 2255 2871 2173 130 215 359 C ATOM 921 CD2 LEU A 115 -7.147 -29.366 19.025 1.00 20.82 C ANISOU 921 CD2 LEU A 115 2301 3361 2249 -265 -600 -701 C ATOM 922 N ALA A 116 -9.825 -33.320 17.379 1.00 17.57 N ANISOU 922 N ALA A 116 2092 2725 1857 -60 -354 191 N ATOM 923 CA ALA A 116 -9.232 -34.632 17.097 1.00 17.46 C ANISOU 923 CA ALA A 116 2366 2591 1676 -279 -211 314 C ATOM 924 C ALA A 116 -9.521 -35.217 15.697 1.00 16.13 C ANISOU 924 C ALA A 116 1965 2379 1785 2 -249 143 C ATOM 925 O ALA A 116 -8.870 -36.191 15.278 1.00 18.78 O ANISOU 925 O ALA A 116 2314 2423 2396 44 -334 380 O ATOM 926 CB ALA A 116 -9.608 -35.629 18.181 1.00 21.82 C ANISOU 926 CB ALA A 116 2785 3318 2185 -463 -309 494 C ATOM 927 N AARG A 117 -10.490 -34.662 14.970 0.50 14.36 N ANISOU 927 N AARG A 117 1810 2277 1367 75 -253 313 N ATOM 928 N BARG A 117 -10.501 -34.632 14.999 0.50 14.57 N ANISOU 928 N BARG A 117 1856 2325 1354 107 -242 254 N ATOM 929 CA AARG A 117 -10.753 -35.173 13.631 0.50 13.60 C ANISOU 929 CA AARG A 117 1834 1793 1541 53 -284 321 C ATOM 930 CA BARG A 117 -10.848 -35.054 13.646 0.50 14.93 C ANISOU 930 CA BARG A 117 1977 2061 1633 43 -269 125 C ATOM 931 C AARG A 117 -9.774 -34.631 12.581 0.50 14.28 C ANISOU 931 C AARG A 117 1745 1997 1683 131 -209 297 C ATOM 932 C BARG A 117 -9.782 -34.638 12.620 0.50 14.68 C ANISOU 932 C BARG A 117 1786 2083 1708 177 -218 246 C ATOM 933 O AARG A 117 -9.699 -35.161 11.483 0.50 15.25 O ANISOU 933 O AARG A 117 2203 1878 1713 23 -288 54 O ATOM 934 O BARG A 117 -9.678 -35.246 11.565 0.50 15.48 O ANISOU 934 O BARG A 117 2222 1952 1705 164 -412 104 O ATOM 935 CB AARG A 117 -12.180 -34.854 13.183 0.50 14.71 C ANISOU 935 CB AARG A 117 1756 1731 2100 46 -159 273 C ATOM 936 CB BARG A 117 -12.190 -34.444 13.210 0.50 15.70 C ANISOU 936 CB BARG A 117 2049 2132 1783 305 -181 202 C ATOM 937 CG AARG A 117 -13.271 -35.498 14.011 0.50 10.65 C ANISOU 937 CG AARG A 117 1319 1465 1262 230 -301 589 C ATOM 938 CG BARG A 117 -13.446 -35.026 13.857 0.50 18.11 C ANISOU 938 CG BARG A 117 2210 2290 2378 -106 -150 45 C ATOM 939 CD AARG A 117 -14.629 -35.330 13.281 0.50 12.11 C ANISOU 939 CD AARG A 117 1484 1355 1763 -58 -294 643 C ATOM 940 CD BARG A 117 -14.694 -34.745 12.968 0.50 19.12 C ANISOU 940 CD BARG A 117 2481 2859 1922 267 -359 655 C ATOM 941 NE AARG A 117 -15.749 -35.533 14.192 0.50 11.44 N ANISOU 941 NE AARG A 117 957 1604 1787 236 81 144 N ATOM 942 NE BARG A 117 -14.647 -35.552 11.745 0.50 22.70 N ANISOU 942 NE BARG A 117 3183 3098 2342 -61 -28 73 N ATOM 943 CZ AARG A 117 -16.970 -35.014 14.063 0.50 10.10 C ANISOU 943 CZ AARG A 117 1343 1325 1170 67 -176 465 C ATOM 944 CZ BARG A 117 -15.359 -35.375 10.622 0.50 22.47 C ANISOU 944 CZ BARG A 117 2470 3007 3057 538 -399 -105 C ATOM 945 NH1AARG A 117 -17.275 -34.202 13.057 0.50 12.03 N ANISOU 945 NH1AARG A 117 1516 1425 1629 34 -519 137 N ATOM 946 NH1BARG A 117 -16.300 -34.423 10.483 0.50 12.75 N ANISOU 946 NH1BARG A 117 1658 1693 1491 62 -379 325 N ATOM 947 NH2AARG A 117 -17.861 -35.236 15.025 0.50 12.89 N ANISOU 947 NH2AARG A 117 1399 1995 1501 -126 198 114 N ATOM 948 NH2BARG A 117 -15.144 -36.224 9.621 0.50 23.31 N ANISOU 948 NH2BARG A 117 3570 3408 1876 -314 -151 581 N ATOM 949 N VAL A 118 -9.024 -33.582 12.896 1.00 13.21 N ANISOU 949 N VAL A 118 1689 1937 1390 146 -142 194 N ATOM 950 CA VAL A 118 -8.142 -32.996 11.867 1.00 13.57 C ANISOU 950 CA VAL A 118 1813 1903 1436 277 -61 240 C ATOM 951 C VAL A 118 -7.030 -33.995 11.495 1.00 14.25 C ANISOU 951 C VAL A 118 1657 2240 1517 448 -336 265 C ATOM 952 O VAL A 118 -6.353 -34.557 12.382 1.00 15.03 O ANISOU 952 O VAL A 118 1859 2197 1653 517 -416 173 O ATOM 953 CB VAL A 118 -7.530 -31.653 12.320 1.00 14.20 C ANISOU 953 CB VAL A 118 2001 1740 1654 431 -25 300 C ATOM 954 CG1 VAL A 118 -6.534 -31.104 11.279 1.00 18.28 C ANISOU 954 CG1 VAL A 118 2134 2788 2024 232 142 402 C ATOM 955 CG2 VAL A 118 -8.619 -30.618 12.570 1.00 15.99 C ANISOU 955 CG2 VAL A 118 1940 2142 1992 523 -267 -318 C ATOM 956 N ARG A 119 -6.788 -34.154 10.188 1.00 14.57 N ANISOU 956 N ARG A 119 1958 1950 1628 356 0 92 N ATOM 957 CA ARG A 119 -5.780 -35.081 9.698 1.00 13.72 C ANISOU 957 CA ARG A 119 1782 1855 1574 216 101 -128 C ATOM 958 C ARG A 119 -4.905 -34.500 8.572 1.00 13.30 C ANISOU 958 C ARG A 119 1829 1807 1415 444 -50 -3 C ATOM 959 O ARG A 119 -3.980 -35.147 8.101 1.00 14.66 O ANISOU 959 O ARG A 119 1858 1697 2016 257 37 -226 O ATOM 960 CB ARG A 119 -6.396 -36.409 9.275 1.00 17.42 C ANISOU 960 CB ARG A 119 1881 1972 2764 412 -299 -130 C ATOM 961 CG ARG A 119 -5.652 -37.615 9.836 1.00 21.68 C ANISOU 961 CG ARG A 119 2751 2334 3152 778 58 -568 C ATOM 962 CD ARG A 119 -6.177 -38.877 9.172 1.00 20.55 C ANISOU 962 CD ARG A 119 3053 2027 2727 283 -247 -379 C ATOM 963 NE ARG A 119 -5.560 -40.113 9.666 1.00 21.72 N ANISOU 963 NE ARG A 119 3242 2110 2900 765 16 22 N ATOM 964 CZ ARG A 119 -4.447 -40.640 9.187 1.00 21.38 C ANISOU 964 CZ ARG A 119 2961 2624 2537 535 9 398 C ATOM 965 NH1 ARG A 119 -3.830 -40.077 8.158 1.00 20.23 N ANISOU 965 NH1 ARG A 119 2861 2378 2446 330 -40 608 N ATOM 966 NH2 ARG A 119 -3.944 -41.745 9.744 1.00 24.14 N ANISOU 966 NH2 ARG A 119 3016 2648 3505 660 -765 1009 N ATOM 967 N LEU A 120 -5.226 -33.297 8.100 1.00 13.59 N ANISOU 967 N LEU A 120 1915 1511 1735 246 -20 195 N ATOM 968 CA LEU A 120 -4.545 -32.754 6.917 1.00 14.06 C ANISOU 968 CA LEU A 120 2070 1451 1819 398 8 -59 C ATOM 969 C LEU A 120 -4.654 -31.234 6.921 1.00 12.21 C ANISOU 969 C LEU A 120 1592 1393 1651 158 -26 -27 C ATOM 970 O LEU A 120 -5.700 -30.697 7.300 1.00 13.98 O ANISOU 970 O LEU A 120 1580 1636 2097 243 166 -20 O ATOM 971 CB LEU A 120 -5.249 -33.276 5.666 1.00 15.84 C ANISOU 971 CB LEU A 120 2579 1373 2066 -39 3 67 C ATOM 972 CG LEU A 120 -4.794 -32.788 4.311 1.00 18.26 C ANISOU 972 CG LEU A 120 2550 2240 2146 198 104 -611 C ATOM 973 CD1 LEU A 120 -3.358 -33.156 4.054 1.00 24.32 C ANISOU 973 CD1 LEU A 120 2928 3603 2708 230 492 -508 C ATOM 974 CD2 LEU A 120 -5.717 -33.314 3.219 1.00 23.70 C ANISOU 974 CD2 LEU A 120 3444 3126 2435 239 -150 -755 C ATOM 975 N VAL A 121 -3.579 -30.550 6.533 1.00 13.58 N ANISOU 975 N VAL A 121 1814 1638 1704 261 189 170 N ATOM 976 CA VAL A 121 -3.623 -29.115 6.263 1.00 12.53 C ANISOU 976 CA VAL A 121 1674 1509 1577 74 55 15 C ATOM 977 C VAL A 121 -3.382 -28.870 4.783 1.00 11.27 C ANISOU 977 C VAL A 121 1360 1584 1337 235 233 -65 C ATOM 978 O VAL A 121 -2.433 -29.398 4.211 1.00 14.37 O ANISOU 978 O VAL A 121 1751 1782 1924 489 312 -120 O ATOM 979 CB VAL A 121 -2.561 -28.363 7.094 1.00 15.03 C ANISOU 979 CB VAL A 121 1903 1954 1853 58 41 -13 C ATOM 980 CG1 VAL A 121 -2.450 -26.903 6.677 1.00 16.78 C ANISOU 980 CG1 VAL A 121 1918 1984 2471 -23 -272 -205 C ATOM 981 CG2 VAL A 121 -2.885 -28.465 8.575 1.00 20.04 C ANISOU 981 CG2 VAL A 121 2954 2625 2033 72 -30 -167 C ATOM 982 N GLU A 122 -4.262 -28.095 4.146 1.00 12.03 N ANISOU 982 N GLU A 122 1659 1403 1507 231 -58 -56 N ATOM 983 CA GLU A 122 -4.094 -27.782 2.717 1.00 12.32 C ANISOU 983 CA GLU A 122 1655 1416 1610 171 84 -27 C ATOM 984 C GLU A 122 -4.083 -26.261 2.542 1.00 12.04 C ANISOU 984 C GLU A 122 1522 1351 1700 188 135 -183 C ATOM 985 O GLU A 122 -4.966 -25.572 3.065 1.00 13.99 O ANISOU 985 O GLU A 122 1827 1574 1913 280 381 41 O ATOM 986 CB GLU A 122 -5.219 -28.388 1.885 1.00 14.84 C ANISOU 986 CB GLU A 122 2076 1888 1672 -86 188 -63 C ATOM 987 CG GLU A 122 -5.046 -28.198 0.378 1.00 19.25 C ANISOU 987 CG GLU A 122 3072 2365 1876 -433 51 -122 C ATOM 988 CD GLU A 122 -6.081 -28.937 -0.475 1.00 27.94 C ANISOU 988 CD GLU A 122 4418 3061 3134 -305 -307 -684 C ATOM 989 OE1 GLU A 122 -6.764 -29.856 0.033 1.00 34.41 O ANISOU 989 OE1 GLU A 122 4901 4360 3811 -1059 -165 -97 O ATOM 990 OE2 GLU A 122 -6.231 -28.572 -1.660 1.00 38.55 O ANISOU 990 OE2 GLU A 122 5662 4774 4210 -100 -165 -223 O ATOM 991 N VAL A 123 -3.096 -25.738 1.819 1.00 12.75 N ANISOU 991 N VAL A 123 1674 1247 1922 157 369 -32 N ATOM 992 CA VAL A 123 -3.001 -24.299 1.592 1.00 14.12 C ANISOU 992 CA VAL A 123 1922 1610 1830 181 -8 -119 C ATOM 993 C VAL A 123 -2.989 -24.139 0.101 1.00 14.19 C ANISOU 993 C VAL A 123 1974 1660 1755 346 273 -126 C ATOM 994 O VAL A 123 -2.152 -24.733 -0.579 1.00 14.94 O ANISOU 994 O VAL A 123 2128 1530 2017 312 510 -112 O ATOM 995 CB VAL A 123 -1.708 -23.701 2.181 1.00 13.03 C ANISOU 995 CB VAL A 123 1807 1218 1923 66 161 -89 C ATOM 996 CG1 VAL A 123 -1.673 -22.177 1.974 1.00 18.36 C ANISOU 996 CG1 VAL A 123 2591 1352 3030 39 -75 -311 C ATOM 997 CG2 VAL A 123 -1.605 -24.012 3.650 1.00 16.30 C ANISOU 997 CG2 VAL A 123 2099 2025 2069 117 -391 -116 C ATOM 998 N GLY A 124 -3.889 -23.325 -0.420 1.00 15.09 N ANISOU 998 N GLY A 124 2309 1543 1879 236 24 108 N ATOM 999 CA GLY A 124 -3.985 -23.203 -1.865 1.00 16.84 C ANISOU 999 CA GLY A 124 2608 1880 1908 302 52 203 C ATOM 1000 C GLY A 124 -4.673 -21.935 -2.305 1.00 12.67 C ANISOU 1000 C GLY A 124 2011 1359 1441 36 240 -147 C ATOM 1001 O GLY A 124 -4.946 -21.067 -1.485 1.00 13.56 O ANISOU 1001 O GLY A 124 1924 1469 1757 133 97 -163 O ATOM 1002 N GLY A 125 -5.023 -21.878 -3.590 1.00 14.19 N ANISOU 1002 N GLY A 125 2093 1654 1645 -131 -33 -120 N ATOM 1003 CA GLY A 125 -5.528 -20.651 -4.181 1.00 13.50 C ANISOU 1003 CA GLY A 125 2020 1479 1629 -11 -62 -68 C ATOM 1004 C GLY A 125 -4.427 -19.699 -4.622 1.00 12.75 C ANISOU 1004 C GLY A 125 1702 1552 1591 -51 16 -380 C ATOM 1005 O GLY A 125 -3.315 -20.123 -4.946 1.00 14.37 O ANISOU 1005 O GLY A 125 1965 1626 1868 54 70 -246 O ATOM 1006 N ASP A 126 -4.743 -18.404 -4.650 1.00 12.30 N ANISOU 1006 N ASP A 126 1502 1478 1690 -73 -85 -125 N ATOM 1007 CA ASP A 126 -3.836 -17.401 -5.231 1.00 12.38 C ANISOU 1007 CA ASP A 126 1458 1408 1838 -22 -54 -44 C ATOM 1008 C ASP A 126 -2.840 -16.918 -4.173 1.00 12.24 C ANISOU 1008 C ASP A 126 1630 1365 1656 28 -64 -112 C ATOM 1009 O ASP A 126 -3.010 -15.852 -3.563 1.00 13.13 O ANISOU 1009 O ASP A 126 1531 1616 1841 27 146 -108 O ATOM 1010 CB ASP A 126 -4.643 -16.215 -5.742 1.00 13.74 C ANISOU 1010 CB ASP A 126 1630 1859 1730 -31 -112 5 C ATOM 1011 CG ASP A 126 -5.611 -16.587 -6.824 1.00 15.55 C ANISOU 1011 CG ASP A 126 2052 1985 1870 329 -271 -190 C ATOM 1012 OD1 ASP A 126 -5.334 -17.523 -7.604 1.00 20.72 O ANISOU 1012 OD1 ASP A 126 2703 2587 2581 413 -372 -580 O ATOM 1013 OD2 ASP A 126 -6.658 -15.923 -6.910 1.00 18.15 O ANISOU 1013 OD2 ASP A 126 2173 1857 2865 380 -463 -284 O ATOM 1014 N VAL A 127 -1.826 -17.734 -3.952 1.00 11.70 N ANISOU 1014 N VAL A 127 1351 1454 1640 -22 -113 -161 N ATOM 1015 CA VAL A 127 -0.805 -17.465 -2.950 1.00 11.68 C ANISOU 1015 CA VAL A 127 1428 1628 1382 6 90 -366 C ATOM 1016 C VAL A 127 0.482 -18.103 -3.471 1.00 12.46 C ANISOU 1016 C VAL A 127 1490 1473 1769 -1 141 -280 C ATOM 1017 O VAL A 127 0.437 -19.183 -4.057 1.00 13.68 O ANISOU 1017 O VAL A 127 1534 1574 2090 1 -21 -349 O ATOM 1018 CB VAL A 127 -1.228 -18.040 -1.571 1.00 12.65 C ANISOU 1018 CB VAL A 127 1685 1498 1621 -245 -24 -261 C ATOM 1019 CG1 VAL A 127 -1.464 -19.525 -1.617 1.00 13.97 C ANISOU 1019 CG1 VAL A 127 1737 1451 2117 -302 -32 188 C ATOM 1020 CG2 VAL A 127 -0.224 -17.677 -0.473 1.00 16.91 C ANISOU 1020 CG2 VAL A 127 1925 2327 2173 -593 -26 -370 C ATOM 1021 N GLN A 128 1.620 -17.466 -3.202 1.00 12.21 N ANISOU 1021 N GLN A 128 1232 1734 1673 -19 -112 -191 N ATOM 1022 CA GLN A 128 2.927 -18.069 -3.478 1.00 11.20 C ANISOU 1022 CA GLN A 128 1399 1541 1313 173 -228 -7 C ATOM 1023 C GLN A 128 3.621 -18.359 -2.155 1.00 12.09 C ANISOU 1023 C GLN A 128 1466 1560 1564 55 -88 -193 C ATOM 1024 O GLN A 128 4.198 -17.482 -1.518 1.00 15.05 O ANISOU 1024 O GLN A 128 1928 1824 1966 7 -147 -297 O ATOM 1025 CB GLN A 128 3.743 -17.160 -4.395 1.00 11.58 C ANISOU 1025 CB GLN A 128 1383 1691 1326 24 129 34 C ATOM 1026 CG GLN A 128 3.069 -16.979 -5.753 1.00 12.28 C ANISOU 1026 CG GLN A 128 1361 1718 1585 -59 116 271 C ATOM 1027 CD GLN A 128 3.987 -16.270 -6.714 1.00 11.59 C ANISOU 1027 CD GLN A 128 1181 1586 1637 256 49 9 C ATOM 1028 OE1 GLN A 128 4.250 -15.062 -6.552 1.00 13.07 O ANISOU 1028 OE1 GLN A 128 1546 1635 1782 -93 113 -65 O ATOM 1029 NE2 GLN A 128 4.574 -17.026 -7.646 1.00 14.78 N ANISOU 1029 NE2 GLN A 128 1578 2123 1913 40 -100 -447 N ATOM 1030 N LEU A 129 3.649 -19.624 -1.787 1.00 12.60 N ANISOU 1030 N LEU A 129 1506 1672 1609 197 202 53 N ATOM 1031 CA LEU A 129 4.096 -19.979 -0.447 1.00 12.79 C ANISOU 1031 CA LEU A 129 1539 1614 1706 -8 169 -23 C ATOM 1032 C LEU A 129 5.605 -19.916 -0.322 1.00 12.99 C ANISOU 1032 C LEU A 129 1497 1653 1783 260 74 -215 C ATOM 1033 O LEU A 129 6.349 -20.389 -1.201 1.00 15.45 O ANISOU 1033 O LEU A 129 1507 2426 1934 320 208 -349 O ATOM 1034 CB LEU A 129 3.625 -21.375 -0.096 1.00 13.76 C ANISOU 1034 CB LEU A 129 1637 1746 1842 -17 46 131 C ATOM 1035 CG LEU A 129 2.118 -21.422 0.152 1.00 15.65 C ANISOU 1035 CG LEU A 129 1858 1799 2289 4 310 -238 C ATOM 1036 CD1 LEU A 129 1.706 -22.884 0.265 1.00 18.68 C ANISOU 1036 CD1 LEU A 129 2511 1922 2663 -579 -54 321 C ATOM 1037 CD2 LEU A 129 1.739 -20.661 1.435 1.00 17.31 C ANISOU 1037 CD2 LEU A 129 1992 2270 2312 -316 581 -450 C ATOM 1038 N ASP A 130 6.043 -19.326 0.794 1.00 12.29 N ANISOU 1038 N ASP A 130 1327 1791 1552 99 -18 -59 N ATOM 1039 CA ASP A 130 7.428 -19.387 1.245 1.00 12.38 C ANISOU 1039 CA ASP A 130 1358 1525 1820 70 -56 10 C ATOM 1040 C ASP A 130 7.647 -20.668 2.067 1.00 12.55 C ANISOU 1040 C ASP A 130 1208 1767 1792 184 224 41 C ATOM 1041 O ASP A 130 8.439 -21.545 1.676 1.00 12.51 O ANISOU 1041 O ASP A 130 1401 1649 1702 135 194 -147 O ATOM 1042 CB ASP A 130 7.751 -18.075 1.995 1.00 12.27 C ANISOU 1042 CB ASP A 130 1090 1591 1980 83 -80 -17 C ATOM 1043 CG ASP A 130 9.156 -18.015 2.569 1.00 14.99 C ANISOU 1043 CG ASP A 130 1539 1622 2533 172 -56 -304 C ATOM 1044 OD1 ASP A 130 9.892 -19.022 2.596 1.00 16.07 O ANISOU 1044 OD1 ASP A 130 1271 2116 2716 227 -89 -65 O ATOM 1045 OD2 ASP A 130 9.514 -16.891 2.996 1.00 18.01 O ANISOU 1045 OD2 ASP A 130 1570 1983 3289 11 -42 -322 O ATOM 1046 N SER A 131 6.871 -20.839 3.134 1.00 12.40 N ANISOU 1046 N SER A 131 1395 1769 1547 -15 246 117 N ATOM 1047 CA SER A 131 6.953 -22.060 3.926 1.00 12.91 C ANISOU 1047 CA SER A 131 1481 1584 1837 197 268 57 C ATOM 1048 C SER A 131 5.655 -22.317 4.701 1.00 12.44 C ANISOU 1048 C SER A 131 1555 1677 1492 193 164 -62 C ATOM 1049 O SER A 131 4.936 -21.369 5.051 1.00 12.35 O ANISOU 1049 O SER A 131 1406 1408 1878 13 169 -89 O ATOM 1050 CB SER A 131 8.115 -21.974 4.929 1.00 16.84 C ANISOU 1050 CB SER A 131 1806 2363 2227 503 50 -118 C ATOM 1051 OG SER A 131 7.907 -20.939 5.872 1.00 16.66 O ANISOU 1051 OG SER A 131 1510 2729 2092 172 -98 -189 O ATOM 1052 N VAL A 132 5.393 -23.590 4.985 1.00 14.00 N ANISOU 1052 N VAL A 132 1864 1697 1759 62 309 -90 N ATOM 1053 CA VAL A 132 4.333 -24.030 5.892 1.00 13.76 C ANISOU 1053 CA VAL A 132 1669 1734 1824 81 195 -120 C ATOM 1054 C VAL A 132 4.986 -24.980 6.905 1.00 15.02 C ANISOU 1054 C VAL A 132 1910 2089 1707 287 224 -49 C ATOM 1055 O VAL A 132 5.685 -25.921 6.504 1.00 18.78 O ANISOU 1055 O VAL A 132 2694 2194 2247 485 402 241 O ATOM 1056 CB VAL A 132 3.229 -24.800 5.114 1.00 16.78 C ANISOU 1056 CB VAL A 132 1913 2111 2351 -160 179 -117 C ATOM 1057 CG1 VAL A 132 2.172 -25.332 6.085 1.00 18.98 C ANISOU 1057 CG1 VAL A 132 2325 2260 2623 -509 345 -102 C ATOM 1058 CG2 VAL A 132 2.575 -23.892 4.080 1.00 18.35 C ANISOU 1058 CG2 VAL A 132 2150 2433 2388 87 -71 -389 C ATOM 1059 N ARG A 133 4.841 -24.693 8.198 1.00 13.95 N ANISOU 1059 N ARG A 133 1858 1708 1735 45 123 155 N ATOM 1060 CA ARG A 133 5.367 -25.580 9.238 1.00 15.54 C ANISOU 1060 CA ARG A 133 1942 2143 1819 187 26 61 C ATOM 1061 C ARG A 133 4.301 -25.804 10.272 1.00 15.40 C ANISOU 1061 C ARG A 133 2057 2037 1758 81 230 -134 C ATOM 1062 O ARG A 133 3.504 -24.914 10.560 1.00 15.98 O ANISOU 1062 O ARG A 133 2246 2023 1801 110 276 62 O ATOM 1063 CB ARG A 133 6.575 -24.939 9.915 1.00 17.53 C ANISOU 1063 CB ARG A 133 2192 2301 2165 -156 -126 -81 C ATOM 1064 CG ARG A 133 7.765 -24.868 9.020 1.00 20.14 C ANISOU 1064 CG ARG A 133 2477 2290 2884 -75 199 12 C ATOM 1065 CD ARG A 133 8.363 -26.251 8.790 1.00 22.74 C ANISOU 1065 CD ARG A 133 2455 2932 3250 241 -69 -535 C ATOM 1066 NE ARG A 133 9.649 -26.145 8.120 1.00 28.12 N ANISOU 1066 NE ARG A 133 2718 3395 4569 230 534 -374 N ATOM 1067 CZ ARG A 133 9.776 -25.888 6.822 1.00 29.24 C ANISOU 1067 CZ ARG A 133 2821 4195 4094 541 529 -217 C ATOM 1068 NH1 ARG A 133 8.683 -25.792 6.068 1.00 27.04 N ANISOU 1068 NH1 ARG A 133 2706 3622 3945 355 712 25 N ATOM 1069 NH2 ARG A 133 10.982 -25.737 6.278 1.00 35.04 N ANISOU 1069 NH2 ARG A 133 3013 4668 5629 674 1079 -800 N ATOM 1070 N ILE A 134 4.295 -27.000 10.845 1.00 15.47 N ANISOU 1070 N ILE A 134 2304 1759 1812 -82 173 3 N ATOM 1071 CA ILE A 134 3.393 -27.320 11.927 1.00 16.94 C ANISOU 1071 CA ILE A 134 2322 2044 2067 -178 75 -66 C ATOM 1072 C ILE A 134 4.184 -27.770 13.136 1.00 18.03 C ANISOU 1072 C ILE A 134 2320 2138 2391 35 -21 -14 C ATOM 1073 O ILE A 134 4.974 -28.701 13.063 1.00 21.31 O ANISOU 1073 O ILE A 134 2932 2418 2745 409 96 173 O ATOM 1074 CB ILE A 134 2.378 -28.390 11.514 1.00 18.35 C ANISOU 1074 CB ILE A 134 2478 2659 1832 -188 32 -196 C ATOM 1075 CG1 ILE A 134 1.506 -27.858 10.376 1.00 23.84 C ANISOU 1075 CG1 ILE A 134 3092 3122 2844 -41 -233 -259 C ATOM 1076 CG2 ILE A 134 1.498 -28.753 12.701 1.00 21.19 C ANISOU 1076 CG2 ILE A 134 2775 3283 1993 -864 24 -179 C ATOM 1077 CD1 ILE A 134 1.191 -28.862 9.334 1.00 31.50 C ANISOU 1077 CD1 ILE A 134 4812 3971 3184 31 -759 -722 C ATOM 1078 N PHE A 135 4.014 -27.034 14.227 1.00 18.11 N ANISOU 1078 N PHE A 135 2210 2406 2262 -335 -51 94 N ATOM 1079 CA PHE A 135 4.730 -27.294 15.461 1.00 18.56 C ANISOU 1079 CA PHE A 135 2229 2369 2452 -303 60 -160 C ATOM 1080 C PHE A 135 3.720 -27.768 16.514 1.00 23.55 C ANISOU 1080 C PHE A 135 2966 2994 2985 -34 719 205 C ATOM 1081 O PHE A 135 3.686 -28.932 16.946 1.00 27.55 O ANISOU 1081 O PHE A 135 3448 3218 3802 211 535 291 O ATOM 1082 CB PHE A 135 5.459 -26.022 15.948 1.00 19.97 C ANISOU 1082 CB PHE A 135 2417 2563 2606 -368 245 -153 C ATOM 1083 CG PHE A 135 6.340 -25.365 14.896 1.00 18.32 C ANISOU 1083 CG PHE A 135 2297 2372 2290 -322 209 -187 C ATOM 1084 CD1 PHE A 135 7.423 -26.043 14.345 1.00 19.21 C ANISOU 1084 CD1 PHE A 135 2548 2434 2316 -257 272 -218 C ATOM 1085 CD2 PHE A 135 6.107 -24.058 14.489 1.00 17.78 C ANISOU 1085 CD2 PHE A 135 1996 2512 2245 -108 -250 -48 C ATOM 1086 CE1 PHE A 135 8.260 -25.423 13.429 1.00 20.06 C ANISOU 1086 CE1 PHE A 135 2453 2986 2181 -359 298 -342 C ATOM 1087 CE2 PHE A 135 6.943 -23.441 13.583 1.00 19.36 C ANISOU 1087 CE2 PHE A 135 1877 3159 2316 -136 -253 170 C ATOM 1088 CZ PHE A 135 8.004 -24.132 13.032 1.00 19.40 C ANISOU 1088 CZ PHE A 135 2557 2575 2237 -276 -281 -96 C ATOM 1089 OXT PHE A 135 2.946 -26.988 17.049 1.00 26.90 O ANISOU 1089 OXT PHE A 135 2623 3735 3862 400 474 720 O TER 1090 PHE A 135 ATOM 1091 N PRO B -2 31.739 1.104 30.129 1.00 45.89 N ANISOU 1091 N PRO B -2 5240 6243 5952 -1143 42 -486 N ATOM 1092 CA PRO B -2 30.316 1.223 30.448 1.00 43.55 C ANISOU 1092 CA PRO B -2 5183 5771 5593 -1100 41 -501 C ATOM 1093 C PRO B -2 29.783 -0.017 31.171 1.00 40.84 C ANISOU 1093 C PRO B -2 4661 5603 5250 -1149 -188 -493 C ATOM 1094 O PRO B -2 29.177 -0.893 30.547 1.00 42.96 O ANISOU 1094 O PRO B -2 5184 5690 5448 -1110 -259 -516 O ATOM 1095 CB PRO B -2 29.659 1.378 29.067 1.00 41.85 C ANISOU 1095 CB PRO B -2 4825 5573 5502 -1089 174 -354 C ATOM 1096 CG PRO B -2 30.764 1.052 28.026 1.00 45.54 C ANISOU 1096 CG PRO B -2 5271 5963 6067 -895 384 -460 C ATOM 1097 CD PRO B -2 31.951 0.540 28.787 1.00 44.84 C ANISOU 1097 CD PRO B -2 5150 6117 5769 -960 174 -501 C ATOM 1098 N ALA B -1 29.990 -0.075 32.483 1.00 39.54 N ANISOU 1098 N ALA B -1 4524 5363 5135 -992 -234 -323 N ATOM 1099 CA ALA B -1 29.815 -1.308 33.245 1.00 37.01 C ANISOU 1099 CA ALA B -1 4332 5017 4713 -971 -582 -351 C ATOM 1100 C ALA B -1 28.395 -1.437 33.781 1.00 37.25 C ANISOU 1100 C ALA B -1 4634 4827 4689 -788 -471 -236 C ATOM 1101 O ALA B -1 28.185 -1.534 34.989 1.00 39.36 O ANISOU 1101 O ALA B -1 4934 5210 4811 -567 -356 55 O ATOM 1102 CB ALA B -1 30.815 -1.361 34.394 1.00 38.01 C ANISOU 1102 CB ALA B -1 4469 5262 4711 -948 -861 -436 C ATOM 1103 N MET B 0 27.440 -1.524 32.860 1.00 34.53 N ANISOU 1103 N MET B 0 4327 4312 4479 -700 -501 -47 N ATOM 1104 CA MET B 0 26.021 -1.505 33.178 1.00 33.69 C ANISOU 1104 CA MET B 0 4289 3968 4543 -384 -478 -81 C ATOM 1105 C MET B 0 25.332 -2.343 32.108 1.00 31.52 C ANISOU 1105 C MET B 0 3724 3788 4463 -299 -516 -45 C ATOM 1106 O MET B 0 25.755 -2.330 30.957 1.00 28.47 O ANISOU 1106 O MET B 0 2931 3762 4121 119 -588 -164 O ATOM 1107 CB MET B 0 25.500 -0.063 33.106 1.00 37.06 C ANISOU 1107 CB MET B 0 4967 3963 5152 -248 -273 -114 C ATOM 1108 CG MET B 0 24.082 0.119 33.609 1.00 42.71 C ANISOU 1108 CG MET B 0 5365 4761 6101 -178 -155 359 C ATOM 1109 SD MET B 0 23.968 0.183 35.409 1.00 57.51 S ANISOU 1109 SD MET B 0 7296 7294 7259 631 363 632 S ATOM 1110 CE MET B 0 25.399 1.188 35.814 1.00 58.05 C ANISOU 1110 CE MET B 0 7441 6691 7923 542 -448 583 C ATOM 1111 N SER B 1 24.293 -3.084 32.481 1.00 28.44 N ANISOU 1111 N SER B 1 3321 3329 4155 -369 -1051 58 N ATOM 1112 CA SER B 1 23.433 -3.733 31.481 1.00 28.75 C ANISOU 1112 CA SER B 1 3828 2789 4305 -531 -711 -25 C ATOM 1113 C SER B 1 21.957 -3.474 31.807 1.00 29.34 C ANISOU 1113 C SER B 1 3837 3097 4215 -426 -611 25 C ATOM 1114 O SER B 1 21.630 -2.957 32.879 1.00 30.36 O ANISOU 1114 O SER B 1 3877 3276 4382 -350 -429 316 O ATOM 1115 CB SER B 1 23.733 -5.233 31.390 1.00 32.50 C ANISOU 1115 CB SER B 1 4215 3484 4649 -197 -926 -53 C ATOM 1116 OG SER B 1 23.730 -5.833 32.672 1.00 36.71 O ANISOU 1116 OG SER B 1 5309 3518 5118 -342 -799 380 O ATOM 1117 N ASN B 2 21.059 -3.809 30.885 1.00 27.37 N ANISOU 1117 N ASN B 2 3376 2718 4302 -217 -405 354 N ATOM 1118 CA ASN B 2 19.648 -3.617 31.177 1.00 29.95 C ANISOU 1118 CA ASN B 2 3741 3446 4191 -402 -202 124 C ATOM 1119 C ASN B 2 19.140 -4.569 32.254 1.00 29.81 C ANISOU 1119 C ASN B 2 3807 3368 4150 -236 -328 75 C ATOM 1120 O ASN B 2 19.639 -5.688 32.397 1.00 29.17 O ANISOU 1120 O ASN B 2 3736 3175 4170 14 -347 117 O ATOM 1121 CB ASN B 2 18.777 -3.665 29.913 1.00 27.23 C ANISOU 1121 CB ASN B 2 3517 2952 3875 -333 -681 247 C ATOM 1122 CG ASN B 2 19.201 -4.753 28.938 1.00 36.37 C ANISOU 1122 CG ASN B 2 4771 4691 4356 -264 -325 133 C ATOM 1123 OD1 ASN B 2 19.355 -5.909 29.317 1.00 37.91 O ANISOU 1123 OD1 ASN B 2 5218 4674 4509 300 -1403 -249 O ATOM 1124 ND2 ASN B 2 19.255 -4.407 27.652 1.00 41.95 N ANISOU 1124 ND2 ASN B 2 5915 6010 4014 2 -477 540 N ATOM 1125 N VAL B 3 18.217 -4.079 33.074 1.00 28.43 N ANISOU 1125 N VAL B 3 3943 3179 3677 -277 -248 -174 N ATOM 1126 CA VAL B 3 17.416 -4.940 33.929 1.00 29.33 C ANISOU 1126 CA VAL B 3 3891 3476 3775 -267 -450 -119 C ATOM 1127 C VAL B 3 16.688 -5.967 33.059 1.00 27.48 C ANISOU 1127 C VAL B 3 3673 3146 3619 -357 -516 -86 C ATOM 1128 O VAL B 3 16.202 -5.632 31.978 1.00 28.08 O ANISOU 1128 O VAL B 3 3708 3521 3440 -321 -495 182 O ATOM 1129 CB VAL B 3 16.400 -4.118 34.743 1.00 28.26 C ANISOU 1129 CB VAL B 3 3917 3431 3386 -352 -196 -294 C ATOM 1130 CG1 VAL B 3 15.678 -5.005 35.757 1.00 30.92 C ANISOU 1130 CG1 VAL B 3 4453 3203 4092 -314 14 -64 C ATOM 1131 CG2 VAL B 3 17.094 -2.963 35.435 1.00 29.36 C ANISOU 1131 CG2 VAL B 3 4463 3164 3526 -359 -965 250 C ATOM 1132 N PRO B 4 16.739 -7.247 33.456 1.00 25.08 N ANISOU 1132 N PRO B 4 3139 3090 3298 -225 -660 -84 N ATOM 1133 CA PRO B 4 16.126 -8.300 32.658 1.00 24.77 C ANISOU 1133 CA PRO B 4 3177 2931 3302 -290 -683 -141 C ATOM 1134 C PRO B 4 14.659 -7.995 32.386 1.00 22.24 C ANISOU 1134 C PRO B 4 2806 2616 3026 -85 -262 -170 C ATOM 1135 O PRO B 4 13.941 -7.480 33.262 1.00 23.81 O ANISOU 1135 O PRO B 4 3128 2811 3104 -245 -372 -329 O ATOM 1136 CB PRO B 4 16.225 -9.526 33.556 1.00 23.92 C ANISOU 1136 CB PRO B 4 2944 3060 3084 50 -652 3 C ATOM 1137 CG PRO B 4 17.378 -9.257 34.450 1.00 26.63 C ANISOU 1137 CG PRO B 4 3384 3200 3530 -342 -685 -472 C ATOM 1138 CD PRO B 4 17.525 -7.775 34.583 1.00 27.25 C ANISOU 1138 CD PRO B 4 3777 3285 3289 -112 -801 128 C ATOM 1139 N HIS B 5 14.230 -8.305 31.174 1.00 18.81 N ANISOU 1139 N HIS B 5 2433 1946 2766 -447 -338 225 N ATOM 1140 CA HIS B 5 12.871 -8.037 30.751 1.00 18.76 C ANISOU 1140 CA HIS B 5 2536 2065 2527 -87 -253 236 C ATOM 1141 C HIS B 5 11.888 -8.884 31.540 1.00 16.45 C ANISOU 1141 C HIS B 5 2425 1596 2227 -101 98 5 C ATOM 1142 O HIS B 5 12.112 -10.093 31.715 1.00 17.75 O ANISOU 1142 O HIS B 5 2515 1519 2710 -194 -11 58 O ATOM 1143 CB HIS B 5 12.730 -8.366 29.273 1.00 18.83 C ANISOU 1143 CB HIS B 5 2788 1966 2400 -155 -308 79 C ATOM 1144 CG HIS B 5 11.320 -8.291 28.777 1.00 16.98 C ANISOU 1144 CG HIS B 5 2382 1646 2422 -102 -270 30 C ATOM 1145 ND1 HIS B 5 10.740 -7.098 28.399 1.00 17.96 N ANISOU 1145 ND1 HIS B 5 2514 1831 2477 167 -40 264 N ATOM 1146 CD2 HIS B 5 10.335 -9.221 28.728 1.00 19.33 C ANISOU 1146 CD2 HIS B 5 2531 1940 2871 -309 -271 103 C ATOM 1147 CE1 HIS B 5 9.473 -7.310 28.091 1.00 17.51 C ANISOU 1147 CE1 HIS B 5 2692 1667 2294 -210 -422 59 C ATOM 1148 NE2 HIS B 5 9.202 -8.589 28.282 1.00 18.15 N ANISOU 1148 NE2 HIS B 5 2692 1785 2419 -276 -308 56 N ATOM 1149 N LYS B 6 10.792 -8.269 31.979 1.00 17.11 N ANISOU 1149 N LYS B 6 2442 1905 2151 -336 -23 -27 N ATOM 1150 CA LYS B 6 9.672 -8.996 32.558 1.00 17.06 C ANISOU 1150 CA LYS B 6 2472 1842 2167 -422 148 145 C ATOM 1151 C LYS B 6 8.370 -8.577 31.890 1.00 18.41 C ANISOU 1151 C LYS B 6 2524 1811 2659 -140 81 107 C ATOM 1152 O LYS B 6 8.107 -7.366 31.707 1.00 20.23 O ANISOU 1152 O LYS B 6 3080 1415 3191 -108 460 399 O ATOM 1153 CB LYS B 6 9.597 -8.730 34.066 1.00 21.71 C ANISOU 1153 CB LYS B 6 3339 2485 2424 -610 -230 59 C ATOM 1154 CG LYS B 6 10.806 -9.270 34.830 1.00 27.89 C ANISOU 1154 CG LYS B 6 4165 3265 3164 -384 -384 46 C ATOM 1155 CD LYS B 6 10.700 -9.046 36.342 1.00 34.80 C ANISOU 1155 CD LYS B 6 5487 4832 2904 -374 -950 -297 C ATOM 1156 CE LYS B 6 11.413 -7.773 36.771 1.00 41.49 C ANISOU 1156 CE LYS B 6 6251 5159 4353 -368 -896 58 C ATOM 1157 NZ LYS B 6 11.876 -7.814 38.192 1.00 47.08 N ANISOU 1157 NZ LYS B 6 7141 6275 4469 197 -867 -525 N ATOM 1158 N SER B 7 7.564 -9.565 31.504 1.00 17.53 N ANISOU 1158 N SER B 7 2339 1947 2372 -165 50 449 N ATOM 1159 CA SER B 7 6.203 -9.331 30.998 1.00 19.59 C ANISOU 1159 CA SER B 7 2326 2485 2632 -265 -8 513 C ATOM 1160 C SER B 7 5.253 -10.219 31.793 1.00 17.64 C ANISOU 1160 C SER B 7 2181 1936 2586 -123 40 485 C ATOM 1161 O SER B 7 5.469 -11.420 31.859 1.00 18.36 O ANISOU 1161 O SER B 7 2581 1852 2541 -83 -23 464 O ATOM 1162 CB SER B 7 6.120 -9.736 29.509 1.00 20.88 C ANISOU 1162 CB SER B 7 2662 2588 2682 -248 -109 537 C ATOM 1163 OG SER B 7 6.551 -8.710 28.638 1.00 23.03 O ANISOU 1163 OG SER B 7 2673 3180 2894 -30 -242 749 O ATOM 1164 N SER B 8 4.172 -9.658 32.329 1.00 20.76 N ANISOU 1164 N SER B 8 2633 2446 2809 -434 461 519 N ATOM 1165 CA SER B 8 3.113 -10.487 32.919 1.00 22.47 C ANISOU 1165 CA SER B 8 2776 2575 3187 -410 480 492 C ATOM 1166 C SER B 8 2.247 -11.132 31.845 1.00 23.70 C ANISOU 1166 C SER B 8 2974 3075 2955 -310 516 462 C ATOM 1167 O SER B 8 2.000 -10.524 30.813 1.00 25.79 O ANISOU 1167 O SER B 8 3082 3222 3494 -390 -27 699 O ATOM 1168 CB SER B 8 2.237 -9.642 33.838 1.00 26.15 C ANISOU 1168 CB SER B 8 3237 3253 3443 -620 750 266 C ATOM 1169 OG SER B 8 2.993 -9.170 34.930 1.00 31.78 O ANISOU 1169 OG SER B 8 3671 4385 4019 -333 409 15 O ATOM 1170 N LEU B 9 1.683 -12.306 32.135 1.00 24.07 N ANISOU 1170 N LEU B 9 3037 2769 3339 -176 324 276 N ATOM 1171 CA LEU B 9 0.694 -12.902 31.236 1.00 27.45 C ANISOU 1171 CA LEU B 9 3531 3303 3594 -241 422 216 C ATOM 1172 C LEU B 9 -0.694 -12.386 31.612 1.00 31.99 C ANISOU 1172 C LEU B 9 3940 4142 4072 -365 382 62 C ATOM 1173 O LEU B 9 -1.157 -12.618 32.724 1.00 34.52 O ANISOU 1173 O LEU B 9 3983 5134 3997 -200 737 -222 O ATOM 1174 CB LEU B 9 0.737 -14.443 31.296 1.00 25.13 C ANISOU 1174 CB LEU B 9 3449 3120 2979 -309 606 106 C ATOM 1175 CG LEU B 9 1.941 -15.148 30.647 1.00 31.09 C ANISOU 1175 CG LEU B 9 4429 3402 3980 102 577 379 C ATOM 1176 CD1 LEU B 9 3.225 -14.500 31.101 1.00 31.72 C ANISOU 1176 CD1 LEU B 9 3266 5229 3556 172 176 1049 C ATOM 1177 CD2 LEU B 9 1.964 -16.662 30.926 1.00 37.63 C ANISOU 1177 CD2 LEU B 9 5474 4181 4639 238 583 420 C ATOM 1178 N PRO B 10 -1.344 -11.654 30.693 1.00 36.01 N ANISOU 1178 N PRO B 10 4291 4665 4723 -84 326 162 N ATOM 1179 CA PRO B 10 -2.618 -10.997 30.968 1.00 39.47 C ANISOU 1179 CA PRO B 10 4748 5067 5180 -110 412 43 C ATOM 1180 C PRO B 10 -3.797 -11.972 30.962 1.00 40.87 C ANISOU 1180 C PRO B 10 4731 5322 5475 -171 407 -231 C ATOM 1181 O PRO B 10 -4.789 -11.743 31.662 1.00 42.21 O ANISOU 1181 O PRO B 10 4775 5616 5647 -191 693 -443 O ATOM 1182 CB PRO B 10 -2.749 -10.008 29.809 1.00 40.51 C ANISOU 1182 CB PRO B 10 4924 5073 5395 64 390 145 C ATOM 1183 CG PRO B 10 -2.061 -10.691 28.665 1.00 39.63 C ANISOU 1183 CG PRO B 10 4766 5213 5076 196 303 232 C ATOM 1184 CD PRO B 10 -0.969 -11.562 29.268 1.00 37.16 C ANISOU 1184 CD PRO B 10 4211 5063 4845 -45 298 151 C ATOM 1185 N GLU B 11 -3.686 -13.046 30.183 1.00 40.23 N ANISOU 1185 N GLU B 11 4575 5318 5392 -67 336 -298 N ATOM 1186 CA GLU B 11 -4.765 -14.022 30.069 1.00 41.34 C ANISOU 1186 CA GLU B 11 4898 5208 5600 -215 378 -158 C ATOM 1187 C GLU B 11 -4.446 -15.275 30.871 1.00 40.99 C ANISOU 1187 C GLU B 11 4886 5158 5531 -408 369 -299 C ATOM 1188 O GLU B 11 -5.249 -16.214 30.932 1.00 43.60 O ANISOU 1188 O GLU B 11 5159 5198 6208 -717 608 -135 O ATOM 1189 CB GLU B 11 -5.011 -14.383 28.601 1.00 42.68 C ANISOU 1189 CB GLU B 11 4955 5522 5737 2 218 -236 C ATOM 1190 CG GLU B 11 -5.448 -13.208 27.736 1.00 48.98 C ANISOU 1190 CG GLU B 11 5785 6288 6536 136 121 141 C ATOM 1191 CD GLU B 11 -5.661 -13.594 26.280 1.00 53.71 C ANISOU 1191 CD GLU B 11 6608 6748 7050 399 309 -75 C ATOM 1192 OE1 GLU B 11 -5.620 -14.806 25.970 1.00 56.40 O ANISOU 1192 OE1 GLU B 11 6973 6589 7866 339 517 -131 O ATOM 1193 OE2 GLU B 11 -5.872 -12.684 25.447 1.00 59.44 O ANISOU 1193 OE2 GLU B 11 7360 7458 7766 852 -1 395 O ATOM 1194 N GLY B 12 -3.278 -15.282 31.504 1.00 37.89 N ANISOU 1194 N GLY B 12 4825 4441 5129 -717 384 -1 N ATOM 1195 CA GLY B 12 -2.797 -16.471 32.182 1.00 38.69 C ANISOU 1195 CA GLY B 12 5204 4559 4936 -314 209 -398 C ATOM 1196 C GLY B 12 -2.319 -17.452 31.134 1.00 35.82 C ANISOU 1196 C GLY B 12 5111 4164 4335 -279 242 -207 C ATOM 1197 O GLY B 12 -1.879 -17.048 30.050 1.00 38.27 O ANISOU 1197 O GLY B 12 5235 4436 4867 -426 122 -135 O ATOM 1198 N ILE B 13 -2.476 -18.743 31.405 1.00 31.93 N ANISOU 1198 N ILE B 13 4765 3735 3629 -351 -33 -346 N ATOM 1199 CA ILE B 13 -1.788 -19.727 30.586 1.00 27.90 C ANISOU 1199 CA ILE B 13 4078 3640 2880 -200 -139 -326 C ATOM 1200 C ILE B 13 -2.546 -21.028 30.440 1.00 26.72 C ANISOU 1200 C ILE B 13 4118 3445 2587 -238 97 -478 C ATOM 1201 O ILE B 13 -3.113 -21.550 31.400 1.00 29.14 O ANISOU 1201 O ILE B 13 4536 3793 2740 -38 -48 -748 O ATOM 1202 CB ILE B 13 -0.387 -20.000 31.126 1.00 27.30 C ANISOU 1202 CB ILE B 13 3498 3437 3434 -750 -222 -95 C ATOM 1203 CG1 ILE B 13 0.509 -20.582 30.035 1.00 27.69 C ANISOU 1203 CG1 ILE B 13 3785 3958 2774 -148 -587 -470 C ATOM 1204 CG2 ILE B 13 -0.462 -20.877 32.351 1.00 28.23 C ANISOU 1204 CG2 ILE B 13 3940 3639 3144 -844 -280 -206 C ATOM 1205 CD1 ILE B 13 1.984 -20.376 30.275 1.00 27.23 C ANISOU 1205 CD1 ILE B 13 3493 3993 2858 505 -719 -484 C ATOM 1206 N ARG B 14 -2.648 -21.499 29.203 1.00 23.97 N ANISOU 1206 N ARG B 14 3743 3163 2201 -225 -62 -838 N ATOM 1207 CA ARG B 14 -3.394 -22.711 28.927 1.00 22.19 C ANISOU 1207 CA ARG B 14 3180 3251 1998 -344 -141 -697 C ATOM 1208 C ARG B 14 -2.675 -23.401 27.774 1.00 19.26 C ANISOU 1208 C ARG B 14 2508 2818 1993 -414 381 -281 C ATOM 1209 O ARG B 14 -1.882 -22.771 27.072 1.00 18.77 O ANISOU 1209 O ARG B 14 2617 2692 1823 -593 100 -400 O ATOM 1210 CB ARG B 14 -4.847 -22.365 28.532 1.00 24.33 C ANISOU 1210 CB ARG B 14 3280 3513 2451 -321 187 -1242 C ATOM 1211 CG ARG B 14 -5.661 -21.665 29.624 1.00 35.86 C ANISOU 1211 CG ARG B 14 4601 5097 3928 -84 448 -845 C ATOM 1212 CD ARG B 14 -7.078 -21.357 29.143 1.00 47.69 C ANISOU 1212 CD ARG B 14 5360 6774 5982 89 401 -684 C ATOM 1213 NE ARG B 14 -7.931 -20.854 30.220 1.00 58.18 N ANISOU 1213 NE ARG B 14 7292 7691 7121 48 914 -788 N ATOM 1214 CZ ARG B 14 -8.235 -21.538 31.320 1.00 61.84 C ANISOU 1214 CZ ARG B 14 7932 8074 7488 -137 933 -461 C ATOM 1215 NH1 ARG B 14 -7.734 -22.752 31.514 1.00 64.03 N ANISOU 1215 NH1 ARG B 14 8332 8058 7938 -209 811 -153 N ATOM 1216 NH2 ARG B 14 -9.028 -21.001 32.238 1.00 63.70 N ANISOU 1216 NH2 ARG B 14 8398 8080 7722 86 1171 -677 N ATOM 1217 N PRO B 15 -2.975 -24.682 27.538 1.00 19.06 N ANISOU 1217 N PRO B 15 2367 2865 2010 -336 381 -513 N ATOM 1218 CA PRO B 15 -2.474 -25.268 26.301 1.00 19.93 C ANISOU 1218 CA PRO B 15 2525 2863 2183 -366 234 -534 C ATOM 1219 C PRO B 15 -2.916 -24.429 25.104 1.00 19.10 C ANISOU 1219 C PRO B 15 2316 2815 2122 -566 225 -464 C ATOM 1220 O PRO B 15 -4.091 -24.113 24.954 1.00 20.63 O ANISOU 1220 O PRO B 15 2411 3471 1956 -399 238 -374 O ATOM 1221 CB PRO B 15 -3.117 -26.664 26.302 1.00 20.82 C ANISOU 1221 CB PRO B 15 2761 3059 2088 -515 662 -601 C ATOM 1222 CG PRO B 15 -3.245 -26.968 27.757 1.00 19.65 C ANISOU 1222 CG PRO B 15 2658 2535 2271 -461 647 -365 C ATOM 1223 CD PRO B 15 -3.709 -25.668 28.344 1.00 19.55 C ANISOU 1223 CD PRO B 15 2511 2580 2338 -438 710 -507 C ATOM 1224 N GLY B 16 -1.973 -24.048 24.260 1.00 17.89 N ANISOU 1224 N GLY B 16 2419 2728 1648 -337 153 -158 N ATOM 1225 CA GLY B 16 -2.283 -23.083 23.201 1.00 18.11 C ANISOU 1225 CA GLY B 16 2254 2759 1867 -248 -114 -277 C ATOM 1226 C GLY B 16 -1.693 -21.689 23.371 1.00 19.09 C ANISOU 1226 C GLY B 16 2148 3025 2077 -376 84 -225 C ATOM 1227 O GLY B 16 -1.673 -20.888 22.426 1.00 21.00 O ANISOU 1227 O GLY B 16 2562 3413 2004 -477 -126 -81 O ATOM 1228 N THR B 17 -1.241 -21.361 24.575 1.00 18.62 N ANISOU 1228 N THR B 17 2064 2759 2251 -309 23 -359 N ATOM 1229 CA THR B 17 -0.566 -20.091 24.772 1.00 17.35 C ANISOU 1229 CA THR B 17 2148 2557 1884 -354 231 -272 C ATOM 1230 C THR B 17 0.780 -20.158 24.031 1.00 16.34 C ANISOU 1230 C THR B 17 1848 2336 2022 -154 -19 -346 C ATOM 1231 O THR B 17 1.495 -21.148 24.145 1.00 16.88 O ANISOU 1231 O THR B 17 1951 2431 2030 -175 -78 -198 O ATOM 1232 CB THR B 17 -0.310 -19.844 26.257 1.00 16.97 C ANISOU 1232 CB THR B 17 2087 2540 1820 -373 102 -550 C ATOM 1233 OG1 THR B 17 -1.566 -19.695 26.927 1.00 21.61 O ANISOU 1233 OG1 THR B 17 2540 2935 2732 -492 490 -401 O ATOM 1234 CG2 THR B 17 0.525 -18.584 26.458 1.00 21.03 C ANISOU 1234 CG2 THR B 17 2613 2723 2653 -81 161 -534 C ATOM 1235 N AVAL B 18 1.087 -19.110 23.265 0.50 16.48 N ANISOU 1235 N AVAL B 18 1806 2695 1759 -131 21 -258 N ATOM 1236 N BVAL B 18 1.122 -19.123 23.272 0.50 17.49 N ANISOU 1236 N BVAL B 18 1925 2818 1901 -92 -4 -234 N ATOM 1237 CA AVAL B 18 2.335 -19.025 22.499 0.50 13.49 C ANISOU 1237 CA AVAL B 18 1632 1975 1518 -217 -55 -175 C ATOM 1238 CA BVAL B 18 2.398 -19.122 22.559 0.50 16.26 C ANISOU 1238 CA BVAL B 18 2028 2311 1838 -86 -52 -157 C ATOM 1239 C AVAL B 18 3.114 -17.788 22.942 0.50 13.64 C ANISOU 1239 C AVAL B 18 1631 1872 1680 -72 -88 -238 C ATOM 1240 C BVAL B 18 3.157 -17.827 22.795 0.50 15.02 C ANISOU 1240 C BVAL B 18 1791 2115 1798 35 -50 -213 C ATOM 1241 O AVAL B 18 2.553 -16.689 23.027 0.50 14.88 O ANISOU 1241 O AVAL B 18 1862 1960 1829 47 -95 -289 O ATOM 1242 O BVAL B 18 2.631 -16.728 22.575 0.50 16.05 O ANISOU 1242 O BVAL B 18 2076 2367 1654 246 -53 -161 O ATOM 1243 CB AVAL B 18 2.056 -18.923 20.989 0.50 13.51 C ANISOU 1243 CB AVAL B 18 1560 1962 1611 -99 -257 -125 C ATOM 1244 CB BVAL B 18 2.209 -19.313 21.062 0.50 17.86 C ANISOU 1244 CB BVAL B 18 2050 2656 2080 -25 -210 -157 C ATOM 1245 CG1AVAL B 18 3.350 -18.870 20.221 0.50 10.12 C ANISOU 1245 CG1AVAL B 18 1129 1697 1019 -321 -132 -307 C ATOM 1246 CG1BVAL B 18 1.360 -20.540 20.787 0.50 19.64 C ANISOU 1246 CG1BVAL B 18 3181 2281 1998 -194 -411 -368 C ATOM 1247 CG2AVAL B 18 1.255 -20.112 20.520 0.50 14.19 C ANISOU 1247 CG2AVAL B 18 1763 2093 1533 -177 -189 -437 C ATOM 1248 CG2BVAL B 18 1.582 -18.087 20.482 0.50 23.69 C ANISOU 1248 CG2BVAL B 18 3039 3364 2597 344 -349 132 C ATOM 1249 N LEU B 19 4.392 -17.966 23.261 1.00 14.03 N ANISOU 1249 N LEU B 19 1725 2006 1598 -141 3 -114 N ATOM 1250 CA LEU B 19 5.265 -16.811 23.466 1.00 14.11 C ANISOU 1250 CA LEU B 19 1754 1941 1665 -173 -197 -151 C ATOM 1251 C LEU B 19 6.230 -16.750 22.292 1.00 14.52 C ANISOU 1251 C LEU B 19 1771 2000 1746 38 -146 -164 C ATOM 1252 O LEU B 19 6.868 -17.757 21.967 1.00 15.55 O ANISOU 1252 O LEU B 19 2063 1819 2024 109 201 35 O ATOM 1253 CB LEU B 19 6.048 -16.938 24.773 1.00 15.07 C ANISOU 1253 CB LEU B 19 1798 2098 1830 -317 -94 79 C ATOM 1254 CG LEU B 19 5.185 -16.994 26.031 1.00 20.20 C ANISOU 1254 CG LEU B 19 2883 2558 2234 -295 -100 -294 C ATOM 1255 CD1 LEU B 19 4.887 -18.449 26.403 1.00 24.90 C ANISOU 1255 CD1 LEU B 19 3306 2894 3259 -263 37 -233 C ATOM 1256 CD2 LEU B 19 5.877 -16.279 27.180 1.00 25.01 C ANISOU 1256 CD2 LEU B 19 3439 3047 3014 -326 -514 -115 C ATOM 1257 N ARG B 20 6.257 -15.609 21.600 1.00 14.27 N ANISOU 1257 N ARG B 20 1869 2104 1448 -101 130 22 N ATOM 1258 CA ARG B 20 7.171 -15.417 20.465 1.00 13.80 C ANISOU 1258 CA ARG B 20 1610 1901 1730 -168 255 -138 C ATOM 1259 C ARG B 20 8.227 -14.396 20.886 1.00 14.78 C ANISOU 1259 C ARG B 20 1901 1819 1893 -174 216 -210 C ATOM 1260 O ARG B 20 7.885 -13.265 21.257 1.00 15.89 O ANISOU 1260 O ARG B 20 1994 1866 2177 -17 112 -8 O ATOM 1261 CB ARG B 20 6.421 -14.956 19.193 1.00 15.79 C ANISOU 1261 CB ARG B 20 2096 2304 1596 -244 201 -6 C ATOM 1262 CG ARG B 20 7.326 -14.789 17.973 1.00 17.14 C ANISOU 1262 CG ARG B 20 2259 2257 1993 -290 164 148 C ATOM 1263 CD ARG B 20 6.583 -14.854 16.594 1.00 20.21 C ANISOU 1263 CD ARG B 20 2581 2679 2416 149 -185 59 C ATOM 1264 NE ARG B 20 5.692 -13.718 16.398 1.00 20.16 N ANISOU 1264 NE ARG B 20 2510 3026 2123 70 -32 127 N ATOM 1265 CZ ARG B 20 4.818 -13.570 15.397 1.00 19.67 C ANISOU 1265 CZ ARG B 20 2584 2770 2118 509 -613 -494 C ATOM 1266 NH1 ARG B 20 4.495 -14.594 14.603 1.00 23.38 N ANISOU 1266 NH1 ARG B 20 3015 3468 2399 200 156 -396 N ATOM 1267 NH2 ARG B 20 4.097 -12.458 15.340 1.00 23.76 N ANISOU 1267 NH2 ARG B 20 2949 3446 2632 621 -214 357 N ATOM 1268 N ILE B 21 9.491 -14.816 20.891 1.00 14.71 N ANISOU 1268 N ILE B 21 1822 1745 2022 -247 -62 -129 N ATOM 1269 CA ILE B 21 10.569 -13.948 21.356 1.00 15.28 C ANISOU 1269 CA ILE B 21 1949 1918 1938 -181 113 -131 C ATOM 1270 C ILE B 21 11.526 -13.769 20.191 1.00 15.84 C ANISOU 1270 C ILE B 21 1877 2023 2117 -154 77 -30 C ATOM 1271 O ILE B 21 12.047 -14.738 19.631 1.00 15.58 O ANISOU 1271 O ILE B 21 1957 1781 2181 -284 89 -125 O ATOM 1272 CB ILE B 21 11.305 -14.593 22.563 1.00 18.66 C ANISOU 1272 CB ILE B 21 2447 2500 2143 -407 68 -7 C ATOM 1273 CG1 ILE B 21 10.286 -14.853 23.679 1.00 22.06 C ANISOU 1273 CG1 ILE B 21 3087 2970 2323 -198 89 -48 C ATOM 1274 CG2 ILE B 21 12.470 -13.693 23.046 1.00 20.31 C ANISOU 1274 CG2 ILE B 21 2416 2706 2595 42 -192 -512 C ATOM 1275 CD1 ILE B 21 10.623 -16.015 24.549 1.00 30.48 C ANISOU 1275 CD1 ILE B 21 3938 4767 2874 536 -490 1439 C ATOM 1276 N ARG B 22 11.729 -12.519 19.811 1.00 15.57 N ANISOU 1276 N ARG B 22 1758 1991 2167 -162 6 5 N ATOM 1277 CA ARG B 22 12.691 -12.190 18.777 1.00 15.04 C ANISOU 1277 CA ARG B 22 1870 1967 1875 44 11 -42 C ATOM 1278 C ARG B 22 13.834 -11.422 19.377 1.00 15.87 C ANISOU 1278 C ARG B 22 1788 2006 2236 22 -39 -263 C ATOM 1279 O ARG B 22 13.630 -10.571 20.239 1.00 17.46 O ANISOU 1279 O ARG B 22 2232 1930 2471 -71 -11 -194 O ATOM 1280 CB ARG B 22 12.048 -11.332 17.707 1.00 17.81 C ANISOU 1280 CB ARG B 22 2335 2295 2135 -114 -40 15 C ATOM 1281 CG ARG B 22 11.026 -12.042 16.894 1.00 18.51 C ANISOU 1281 CG ARG B 22 2297 2673 2062 183 -351 135 C ATOM 1282 CD ARG B 22 10.302 -11.015 16.062 1.00 22.29 C ANISOU 1282 CD ARG B 22 2819 3204 2447 -38 -639 313 C ATOM 1283 NE ARG B 22 9.334 -11.640 15.183 1.00 22.71 N ANISOU 1283 NE ARG B 22 2682 3560 2384 -223 -268 268 N ATOM 1284 CZ ARG B 22 8.396 -10.982 14.511 1.00 26.42 C ANISOU 1284 CZ ARG B 22 4188 3250 2597 487 -708 67 C ATOM 1285 NH1 ARG B 22 8.287 -9.663 14.606 1.00 31.68 N ANISOU 1285 NH1 ARG B 22 3982 4079 3975 1197 -1248 163 N ATOM 1286 NH2 ARG B 22 7.542 -11.658 13.770 1.00 29.61 N ANISOU 1286 NH2 ARG B 22 3461 4588 3201 -604 -1001 310 N ATOM 1287 N GLY B 23 15.038 -11.674 18.895 1.00 17.68 N ANISOU 1287 N GLY B 23 1929 2125 2664 -398 -11 -85 N ATOM 1288 CA GLY B 23 16.192 -10.978 19.442 1.00 16.83 C ANISOU 1288 CA GLY B 23 2038 2093 2263 -250 15 -218 C ATOM 1289 C GLY B 23 17.439 -11.204 18.636 1.00 18.25 C ANISOU 1289 C GLY B 23 1996 2399 2537 -284 20 -79 C ATOM 1290 O GLY B 23 17.400 -11.832 17.581 1.00 18.88 O ANISOU 1290 O GLY B 23 2083 2480 2608 -443 172 -315 O ATOM 1291 N LEU B 24 18.549 -10.696 19.165 1.00 18.67 N ANISOU 1291 N LEU B 24 2140 2523 2428 -277 -94 -36 N ATOM 1292 CA LEU B 24 19.859 -10.771 18.532 1.00 18.59 C ANISOU 1292 CA LEU B 24 2157 2414 2493 -327 53 149 C ATOM 1293 C LEU B 24 20.851 -11.253 19.589 1.00 18.67 C ANISOU 1293 C LEU B 24 2211 2270 2612 -314 19 35 C ATOM 1294 O LEU B 24 20.891 -10.724 20.706 1.00 20.84 O ANISOU 1294 O LEU B 24 2345 2896 2677 -84 221 93 O ATOM 1295 CB LEU B 24 20.256 -9.377 18.011 1.00 20.71 C ANISOU 1295 CB LEU B 24 2577 2478 2814 -230 172 340 C ATOM 1296 CG LEU B 24 21.693 -9.155 17.535 1.00 23.01 C ANISOU 1296 CG LEU B 24 3162 2072 3506 -380 583 112 C ATOM 1297 CD1 LEU B 24 21.979 -10.036 16.347 1.00 22.43 C ANISOU 1297 CD1 LEU B 24 2864 2900 2758 -152 -146 -175 C ATOM 1298 CD2 LEU B 24 21.922 -7.688 17.169 1.00 24.13 C ANISOU 1298 CD2 LEU B 24 3786 1725 3655 24 421 303 C ATOM 1299 N VAL B 25 21.611 -12.299 19.276 1.00 18.88 N ANISOU 1299 N VAL B 25 2077 2377 2719 -293 -45 172 N ATOM 1300 CA VAL B 25 22.692 -12.729 20.174 1.00 18.79 C ANISOU 1300 CA VAL B 25 2294 2377 2468 -154 38 312 C ATOM 1301 C VAL B 25 23.942 -11.875 19.917 1.00 19.49 C ANISOU 1301 C VAL B 25 2244 2437 2722 -116 -72 89 C ATOM 1302 O VAL B 25 24.413 -11.804 18.784 1.00 19.29 O ANISOU 1302 O VAL B 25 2309 2617 2401 -35 290 279 O ATOM 1303 CB VAL B 25 23.039 -14.211 19.941 1.00 18.14 C ANISOU 1303 CB VAL B 25 2023 2212 2656 -376 -63 263 C ATOM 1304 CG1 VAL B 25 24.166 -14.644 20.864 1.00 20.54 C ANISOU 1304 CG1 VAL B 25 2459 2820 2524 147 -439 136 C ATOM 1305 CG2 VAL B 25 21.791 -15.091 20.121 1.00 22.04 C ANISOU 1305 CG2 VAL B 25 2569 2403 3401 -570 134 207 C ATOM 1306 N PRO B 26 24.471 -11.201 20.955 1.00 19.15 N ANISOU 1306 N PRO B 26 2368 2427 2481 -270 280 228 N ATOM 1307 CA PRO B 26 25.654 -10.363 20.709 1.00 20.51 C ANISOU 1307 CA PRO B 26 2443 2328 3021 -195 9 151 C ATOM 1308 C PRO B 26 26.893 -11.191 20.322 1.00 22.50 C ANISOU 1308 C PRO B 26 2571 2755 3222 -361 325 308 C ATOM 1309 O PRO B 26 26.968 -12.385 20.634 1.00 22.58 O ANISOU 1309 O PRO B 26 2233 2861 3483 -380 202 335 O ATOM 1310 CB PRO B 26 25.861 -9.643 22.046 1.00 23.85 C ANISOU 1310 CB PRO B 26 2713 2974 3374 -311 2 -32 C ATOM 1311 CG PRO B 26 25.139 -10.466 23.047 1.00 25.97 C ANISOU 1311 CG PRO B 26 3434 3124 3307 -668 -131 -43 C ATOM 1312 CD PRO B 26 23.994 -11.123 22.345 1.00 20.80 C ANISOU 1312 CD PRO B 26 2628 2558 2716 -168 210 -44 C ATOM 1313 N PRO B 27 27.822 -10.583 19.560 1.00 25.08 N ANISOU 1313 N PRO B 27 2575 3049 3903 -327 461 276 N ATOM 1314 CA PRO B 27 29.016 -11.281 19.062 1.00 26.97 C ANISOU 1314 CA PRO B 27 2738 3462 4048 -442 676 180 C ATOM 1315 C PRO B 27 29.834 -11.957 20.164 1.00 27.62 C ANISOU 1315 C PRO B 27 2413 3634 4446 -504 265 58 C ATOM 1316 O PRO B 27 30.572 -12.894 19.884 1.00 30.54 O ANISOU 1316 O PRO B 27 2550 3977 5075 -521 535 -79 O ATOM 1317 CB PRO B 27 29.859 -10.174 18.412 1.00 27.64 C ANISOU 1317 CB PRO B 27 3032 3484 3984 -501 855 358 C ATOM 1318 CG PRO B 27 29.014 -8.973 18.342 1.00 29.22 C ANISOU 1318 CG PRO B 27 3048 3535 4518 -218 1001 337 C ATOM 1319 CD PRO B 27 27.774 -9.162 19.175 1.00 26.47 C ANISOU 1319 CD PRO B 27 2871 2988 4195 -341 880 320 C ATOM 1320 N ASN B 28 29.750 -11.446 21.390 1.00 28.27 N ANISOU 1320 N ASN B 28 2356 3971 4415 -532 -54 85 N ATOM 1321 CA ASN B 28 30.544 -11.972 22.508 1.00 29.18 C ANISOU 1321 CA ASN B 28 2409 3991 4686 -670 -470 13 C ATOM 1322 C ASN B 28 29.764 -12.811 23.539 1.00 30.07 C ANISOU 1322 C ASN B 28 2767 4109 4549 -350 -384 240 C ATOM 1323 O ASN B 28 30.269 -13.094 24.630 1.00 31.59 O ANISOU 1323 O ASN B 28 2672 4677 4654 -688 -591 251 O ATOM 1324 CB ASN B 28 31.309 -10.838 23.204 1.00 31.52 C ANISOU 1324 CB ASN B 28 2668 4254 5054 -814 -715 -227 C ATOM 1325 CG ASN B 28 30.407 -9.946 24.055 1.00 33.92 C ANISOU 1325 CG ASN B 28 3152 4461 5273 -687 -796 -449 C ATOM 1326 OD1 ASN B 28 29.181 -10.002 23.952 1.00 39.50 O ANISOU 1326 OD1 ASN B 28 3822 4682 6500 -396 -544 -586 O ATOM 1327 ND2 ASN B 28 31.017 -9.116 24.902 1.00 32.29 N ANISOU 1327 ND2 ASN B 28 4215 4157 3894 -972 -457 198 N ATOM 1328 N ALA B 29 28.543 -13.213 23.199 1.00 26.45 N ANISOU 1328 N ALA B 29 2363 3756 3929 -123 -482 203 N ATOM 1329 CA ALA B 29 27.638 -13.868 24.166 1.00 25.74 C ANISOU 1329 CA ALA B 29 2486 3514 3777 -282 -447 89 C ATOM 1330 C ALA B 29 28.156 -15.198 24.710 1.00 26.58 C ANISOU 1330 C ALA B 29 2578 3729 3790 -181 -439 137 C ATOM 1331 O ALA B 29 28.634 -16.048 23.947 1.00 27.87 O ANISOU 1331 O ALA B 29 2849 3755 3984 -348 -42 -9 O ATOM 1332 CB ALA B 29 26.245 -14.064 23.556 1.00 25.25 C ANISOU 1332 CB ALA B 29 2318 3511 3762 -284 -251 -4 C ATOM 1333 N SER B 30 27.905 -15.431 26.003 1.00 25.60 N ANISOU 1333 N SER B 30 2709 3399 3619 -452 -674 167 N ATOM 1334 CA SER B 30 28.120 -16.738 26.629 1.00 26.93 C ANISOU 1334 CA SER B 30 3013 3291 3928 -188 -531 231 C ATOM 1335 C SER B 30 26.805 -17.511 26.668 1.00 24.87 C ANISOU 1335 C SER B 30 2644 3093 3713 35 -178 190 C ATOM 1336 O SER B 30 26.747 -18.669 26.274 1.00 26.73 O ANISOU 1336 O SER B 30 2893 3350 3911 126 -596 -201 O ATOM 1337 CB SER B 30 28.676 -16.578 28.055 1.00 27.80 C ANISOU 1337 CB SER B 30 3349 3254 3957 -258 -444 396 C ATOM 1338 OG SER B 30 28.405 -17.734 28.842 1.00 33.15 O ANISOU 1338 OG SER B 30 4442 3842 4309 -111 -335 401 O ATOM 1339 N ARG B 31 25.758 -16.881 27.202 1.00 23.40 N ANISOU 1339 N ARG B 31 2526 2854 3509 153 -341 232 N ATOM 1340 CA ARG B 31 24.464 -17.538 27.346 1.00 23.87 C ANISOU 1340 CA ARG B 31 2635 3081 3352 193 -5 201 C ATOM 1341 C ARG B 31 23.356 -16.525 27.636 1.00 21.00 C ANISOU 1341 C ARG B 31 2350 2576 3053 134 -458 152 C ATOM 1342 O ARG B 31 23.617 -15.385 28.041 1.00 21.98 O ANISOU 1342 O ARG B 31 2441 2733 3177 42 -262 128 O ATOM 1343 CB ARG B 31 24.516 -18.554 28.477 1.00 24.73 C ANISOU 1343 CB ARG B 31 2776 3365 3252 156 -180 38 C ATOM 1344 CG ARG B 31 24.694 -17.909 29.842 1.00 27.68 C ANISOU 1344 CG ARG B 31 3361 3777 3377 228 -998 -318 C ATOM 1345 CD ARG B 31 25.031 -18.954 30.868 1.00 30.35 C ANISOU 1345 CD ARG B 31 3440 4014 4076 24 -782 381 C ATOM 1346 NE ARG B 31 26.382 -19.457 30.637 1.00 33.93 N ANISOU 1346 NE ARG B 31 4111 4508 4273 451 -768 472 N ATOM 1347 CZ ARG B 31 26.971 -20.388 31.375 1.00 36.45 C ANISOU 1347 CZ ARG B 31 4256 4686 4906 455 -457 728 C ATOM 1348 NH1 ARG B 31 26.367 -20.857 32.458 1.00 37.47 N ANISOU 1348 NH1 ARG B 31 4159 5148 4928 -235 -43 235 N ATOM 1349 NH2 ARG B 31 28.204 -20.773 31.086 1.00 39.63 N ANISOU 1349 NH2 ARG B 31 4687 5192 5177 1003 -22 267 N ATOM 1350 N PHE B 32 22.120 -16.928 27.371 1.00 20.57 N ANISOU 1350 N PHE B 32 2284 2477 3053 90 -112 231 N ATOM 1351 CA PHE B 32 20.982 -16.120 27.759 1.00 19.52 C ANISOU 1351 CA PHE B 32 2081 2576 2757 88 -138 287 C ATOM 1352 C PHE B 32 19.850 -17.045 28.154 1.00 18.29 C ANISOU 1352 C PHE B 32 2179 2408 2360 104 -132 426 C ATOM 1353 O PHE B 32 19.947 -18.272 28.010 1.00 20.22 O ANISOU 1353 O PHE B 32 2507 2439 2736 -30 -467 470 O ATOM 1354 CB PHE B 32 20.566 -15.146 26.645 1.00 19.07 C ANISOU 1354 CB PHE B 32 2277 2434 2532 -88 -163 218 C ATOM 1355 CG PHE B 32 19.894 -15.802 25.471 1.00 19.28 C ANISOU 1355 CG PHE B 32 2698 2305 2321 -55 -11 234 C ATOM 1356 CD1 PHE B 32 20.648 -16.237 24.387 1.00 21.14 C ANISOU 1356 CD1 PHE B 32 3025 2147 2858 164 162 234 C ATOM 1357 CD2 PHE B 32 18.509 -15.816 25.360 1.00 18.90 C ANISOU 1357 CD2 PHE B 32 2676 2471 2031 -361 -375 120 C ATOM 1358 CE1 PHE B 32 20.028 -16.814 23.271 1.00 25.45 C ANISOU 1358 CE1 PHE B 32 4042 2371 3256 -313 238 107 C ATOM 1359 CE2 PHE B 32 17.874 -16.394 24.237 1.00 23.49 C ANISOU 1359 CE2 PHE B 32 3453 2521 2949 -240 -539 344 C ATOM 1360 CZ PHE B 32 18.644 -16.889 23.198 1.00 23.65 C ANISOU 1360 CZ PHE B 32 3964 2424 2598 -106 -626 498 C ATOM 1361 N HIS B 33 18.777 -16.479 28.673 1.00 18.78 N ANISOU 1361 N HIS B 33 2276 2542 2314 -49 -227 241 N ATOM 1362 CA HIS B 33 17.719 -17.323 29.170 1.00 18.47 C ANISOU 1362 CA HIS B 33 2383 2603 2031 -268 -360 379 C ATOM 1363 C HIS B 33 16.339 -16.708 29.000 1.00 17.45 C ANISOU 1363 C HIS B 33 2515 1932 2181 30 -118 305 C ATOM 1364 O HIS B 33 16.174 -15.483 28.914 1.00 18.06 O ANISOU 1364 O HIS B 33 2432 2138 2290 -206 -201 147 O ATOM 1365 CB HIS B 33 17.981 -17.676 30.638 1.00 21.54 C ANISOU 1365 CB HIS B 33 2817 3119 2245 -192 -511 341 C ATOM 1366 CG HIS B 33 17.835 -16.509 31.553 1.00 23.47 C ANISOU 1366 CG HIS B 33 3026 3631 2258 -429 -762 170 C ATOM 1367 ND1 HIS B 33 18.910 -15.745 31.955 1.00 29.45 N ANISOU 1367 ND1 HIS B 33 3595 4501 3091 -1115 -486 106 N ATOM 1368 CD2 HIS B 33 16.741 -15.954 32.126 1.00 29.22 C ANISOU 1368 CD2 HIS B 33 3929 4162 3010 -369 -368 105 C ATOM 1369 CE1 HIS B 33 18.483 -14.775 32.747 1.00 31.05 C ANISOU 1369 CE1 HIS B 33 3880 4470 3446 -734 -654 -85 C ATOM 1370 NE2 HIS B 33 17.175 -14.896 32.887 1.00 31.81 N ANISOU 1370 NE2 HIS B 33 4302 4655 3130 -803 -43 -294 N ATOM 1371 N VAL B 34 15.358 -17.600 28.850 1.00 16.89 N ANISOU 1371 N VAL B 34 2132 2016 2267 -155 24 256 N ATOM 1372 CA VAL B 34 13.938 -17.264 28.947 1.00 16.52 C ANISOU 1372 CA VAL B 34 2253 1831 2192 -178 -109 323 C ATOM 1373 C VAL B 34 13.347 -18.109 30.069 1.00 16.48 C ANISOU 1373 C VAL B 34 2489 1651 2121 -201 -22 288 C ATOM 1374 O VAL B 34 13.497 -19.338 30.055 1.00 17.60 O ANISOU 1374 O VAL B 34 2595 1553 2539 -63 184 168 O ATOM 1375 CB VAL B 34 13.184 -17.599 27.631 1.00 16.03 C ANISOU 1375 CB VAL B 34 2160 1849 2081 88 -170 436 C ATOM 1376 CG1 VAL B 34 11.704 -17.276 27.793 1.00 16.94 C ANISOU 1376 CG1 VAL B 34 2406 2020 2009 -189 -260 124 C ATOM 1377 CG2 VAL B 34 13.815 -16.844 26.447 1.00 18.03 C ANISOU 1377 CG2 VAL B 34 2997 1892 1961 -90 60 193 C ATOM 1378 N ASN B 35 12.783 -17.453 31.079 1.00 16.57 N ANISOU 1378 N ASN B 35 2511 1798 1987 -236 -101 249 N ATOM 1379 CA ASN B 35 12.148 -18.146 32.195 1.00 16.64 C ANISOU 1379 CA ASN B 35 2545 2015 1762 -266 -195 272 C ATOM 1380 C ASN B 35 10.646 -17.913 32.241 1.00 15.73 C ANISOU 1380 C ASN B 35 2518 1702 1756 -70 -202 124 C ATOM 1381 O ASN B 35 10.166 -16.796 31.991 1.00 16.94 O ANISOU 1381 O ASN B 35 2755 1603 2078 -165 -87 208 O ATOM 1382 CB ASN B 35 12.753 -17.706 33.541 1.00 17.71 C ANISOU 1382 CB ASN B 35 2646 2115 1968 -183 -439 118 C ATOM 1383 CG ASN B 35 14.226 -18.063 33.691 1.00 21.75 C ANISOU 1383 CG ASN B 35 2936 2612 2714 -220 -568 260 C ATOM 1384 OD1 ASN B 35 14.746 -18.938 33.002 1.00 24.07 O ANISOU 1384 OD1 ASN B 35 3225 2621 3299 32 -683 -208 O ATOM 1385 ND2 ASN B 35 14.921 -17.311 34.530 1.00 27.30 N ANISOU 1385 ND2 ASN B 35 3620 3914 2838 -139 -472 -506 N ATOM 1386 N LEU B 36 9.893 -18.957 32.563 1.00 15.05 N ANISOU 1386 N LEU B 36 2380 1764 1572 -201 -220 243 N ATOM 1387 CA LEU B 36 8.499 -18.816 32.927 1.00 15.82 C ANISOU 1387 CA LEU B 36 2525 1722 1764 -234 -195 87 C ATOM 1388 C LEU B 36 8.448 -18.959 34.442 1.00 15.94 C ANISOU 1388 C LEU B 36 2652 1724 1680 37 -172 260 C ATOM 1389 O LEU B 36 8.746 -20.030 34.964 1.00 17.46 O ANISOU 1389 O LEU B 36 2930 1894 1810 -75 -46 402 O ATOM 1390 CB LEU B 36 7.625 -19.861 32.215 1.00 15.41 C ANISOU 1390 CB LEU B 36 2619 1659 1575 -231 -69 391 C ATOM 1391 CG LEU B 36 7.692 -19.780 30.684 1.00 16.58 C ANISOU 1391 CG LEU B 36 2809 1861 1629 -307 -293 279 C ATOM 1392 CD1 LEU B 36 6.841 -20.889 30.085 1.00 18.31 C ANISOU 1392 CD1 LEU B 36 2734 2300 1920 -332 -386 91 C ATOM 1393 CD2 LEU B 36 7.299 -18.411 30.143 1.00 20.10 C ANISOU 1393 CD2 LEU B 36 3118 2143 2373 -371 -439 347 C ATOM 1394 N LEU B 37 7.957 -17.914 35.100 1.00 16.99 N ANISOU 1394 N LEU B 37 2833 2033 1587 -323 -238 145 N ATOM 1395 CA LEU B 37 7.972 -17.801 36.561 1.00 16.10 C ANISOU 1395 CA LEU B 37 2809 2024 1283 -438 -245 230 C ATOM 1396 C LEU B 37 6.569 -17.773 37.164 1.00 17.18 C ANISOU 1396 C LEU B 37 2567 2247 1714 -454 -266 458 C ATOM 1397 O LEU B 37 5.602 -17.387 36.501 1.00 18.61 O ANISOU 1397 O LEU B 37 2932 2290 1846 -280 -85 230 O ATOM 1398 CB LEU B 37 8.672 -16.503 36.970 1.00 19.09 C ANISOU 1398 CB LEU B 37 3148 2203 1899 -622 -266 -4 C ATOM 1399 CG LEU B 37 10.118 -16.368 36.489 1.00 22.94 C ANISOU 1399 CG LEU B 37 3096 2668 2949 -660 -144 -239 C ATOM 1400 CD1 LEU B 37 10.766 -15.073 36.998 1.00 27.85 C ANISOU 1400 CD1 LEU B 37 3926 2375 4279 -1096 118 172 C ATOM 1401 CD2 LEU B 37 10.916 -17.582 36.920 1.00 23.67 C ANISOU 1401 CD2 LEU B 37 3034 3359 2600 -259 162 310 C HETATM 1402 N CSX B 38 6.475 -18.117 38.453 1.00 19.32 N ANISOU 1402 N CSX B 38 3283 2395 1662 -568 55 345 N HETATM 1403 CA CSX B 38 5.168 -18.351 39.066 1.00 22.13 C ANISOU 1403 CA CSX B 38 3457 3073 1876 -573 149 375 C HETATM 1404 CB CSX B 38 5.210 -19.614 39.939 1.00 26.07 C ANISOU 1404 CB CSX B 38 3949 3758 2196 -462 102 492 C HETATM 1405 SG CSX B 38 5.555 -21.131 38.951 1.00 32.81 S ANISOU 1405 SG CSX B 38 3708 3642 5116 -761 -616 724 S HETATM 1406 C CSX B 38 4.629 -17.135 39.823 1.00 26.35 C ANISOU 1406 C CSX B 38 3931 3653 2427 -609 378 9 C HETATM 1407 O CSX B 38 3.511 -17.144 40.348 1.00 29.95 O ANISOU 1407 O CSX B 38 4133 4165 3081 -511 504 -542 O ATOM 1408 N GLY B 39 5.394 -16.060 39.810 1.00 26.46 N ANISOU 1408 N GLY B 39 4154 3052 2845 -361 215 -260 N ATOM 1409 CA GLY B 39 4.986 -14.839 40.501 1.00 29.52 C ANISOU 1409 CA GLY B 39 4442 3585 3189 -461 128 -349 C ATOM 1410 C GLY B 39 6.077 -13.792 40.468 1.00 31.10 C ANISOU 1410 C GLY B 39 4693 3603 3521 -493 129 -15 C ATOM 1411 O GLY B 39 7.140 -14.012 39.877 1.00 32.36 O ANISOU 1411 O GLY B 39 4637 4024 3635 -195 -91 -151 O ATOM 1412 N GLU B 40 5.817 -12.665 41.131 1.00 32.87 N ANISOU 1412 N GLU B 40 4983 3861 3641 -516 169 -227 N ATOM 1413 CA GLU B 40 6.602 -11.441 40.955 1.00 35.65 C ANISOU 1413 CA GLU B 40 5206 4039 4298 -525 23 -172 C ATOM 1414 C GLU B 40 7.862 -11.404 41.825 1.00 35.83 C ANISOU 1414 C GLU B 40 5320 4202 4092 -754 -72 -191 C ATOM 1415 O GLU B 40 8.781 -10.625 41.562 1.00 38.06 O ANISOU 1415 O GLU B 40 5489 4518 4452 -1011 -269 -358 O ATOM 1416 CB GLU B 40 5.741 -10.207 41.253 1.00 38.47 C ANISOU 1416 CB GLU B 40 5585 4394 4636 -394 -35 -236 C ATOM 1417 CG GLU B 40 4.605 -9.987 40.266 1.00 38.87 C ANISOU 1417 CG GLU B 40 5272 4115 5381 -311 64 381 C ATOM 1418 CD GLU B 40 4.980 -9.031 39.155 1.00 47.52 C ANISOU 1418 CD GLU B 40 5868 5858 6327 -273 99 944 C ATOM 1419 OE1 GLU B 40 6.194 -8.879 38.889 1.00 53.18 O ANISOU 1419 OE1 GLU B 40 6256 6615 7332 -414 179 1201 O ATOM 1420 OE2 GLU B 40 4.063 -8.408 38.572 1.00 51.51 O ANISOU 1420 OE2 GLU B 40 6053 6615 6902 -147 -395 1139 O ATOM 1421 N GLU B 41 7.884 -12.200 42.891 1.00 36.91 N ANISOU 1421 N GLU B 41 5557 4539 3928 -749 -163 -392 N ATOM 1422 CA GLU B 41 8.988 -12.145 43.849 1.00 39.68 C ANISOU 1422 CA GLU B 41 5600 5004 4470 -736 -104 -149 C ATOM 1423 C GLU B 41 10.275 -12.679 43.231 1.00 39.73 C ANISOU 1423 C GLU B 41 5549 5071 4474 -677 -258 -239 C ATOM 1424 O GLU B 41 10.245 -13.626 42.446 1.00 39.52 O ANISOU 1424 O GLU B 41 5526 5032 4456 -722 -369 -280 O ATOM 1425 CB GLU B 41 8.640 -12.921 45.119 1.00 39.67 C ANISOU 1425 CB GLU B 41 5764 4957 4348 -715 1 -231 C ATOM 1426 CG GLU B 41 7.567 -12.244 45.964 1.00 45.02 C ANISOU 1426 CG GLU B 41 6162 5816 5126 -946 520 39 C ATOM 1427 CD GLU B 41 6.736 -13.235 46.759 1.00 49.62 C ANISOU 1427 CD GLU B 41 6802 6278 5773 -1466 546 -202 C ATOM 1428 OE1 GLU B 41 6.415 -14.321 46.219 1.00 53.08 O ANISOU 1428 OE1 GLU B 41 7122 6342 6703 -1415 453 -536 O ATOM 1429 OE2 GLU B 41 6.414 -12.928 47.929 1.00 48.39 O ANISOU 1429 OE2 GLU B 41 6451 6221 5712 -2195 546 -604 O ATOM 1430 N GLN B 42 11.393 -12.017 43.529 1.00 40.33 N ANISOU 1430 N GLN B 42 5562 5175 4587 -959 -376 -402 N ATOM 1431 CA GLN B 42 12.712 -12.543 43.184 1.00 40.53 C ANISOU 1431 CA GLN B 42 5553 5238 4607 -913 -451 -315 C ATOM 1432 C GLN B 42 12.888 -13.944 43.761 1.00 40.78 C ANISOU 1432 C GLN B 42 5604 5325 4563 -835 -596 -200 C ATOM 1433 O GLN B 42 12.607 -14.184 44.941 1.00 42.18 O ANISOU 1433 O GLN B 42 5857 5634 4534 -766 -523 -272 O ATOM 1434 CB GLN B 42 13.823 -11.612 43.693 1.00 42.40 C ANISOU 1434 CB GLN B 42 5740 5547 4823 -1102 -371 -361 C ATOM 1435 CG GLN B 42 15.240 -12.033 43.280 1.00 47.68 C ANISOU 1435 CG GLN B 42 5976 6255 5883 -1224 -359 -157 C ATOM 1436 CD GLN B 42 15.854 -11.115 42.221 1.00 54.93 C ANISOU 1436 CD GLN B 42 6988 7347 6535 -1370 -79 11 C ATOM 1437 OE1 GLN B 42 16.466 -10.092 42.547 1.00 58.27 O ANISOU 1437 OE1 GLN B 42 7291 7708 7139 -1435 -579 -248 O ATOM 1438 NE2 GLN B 42 15.731 -11.503 40.953 1.00 53.46 N ANISOU 1438 NE2 GLN B 42 6677 7079 6555 -1857 -314 -435 N ATOM 1439 N GLY B 43 13.297 -14.882 42.914 1.00 38.64 N ANISOU 1439 N GLY B 43 5202 4972 4506 -785 -833 -193 N ATOM 1440 CA GLY B 43 13.471 -16.267 43.349 1.00 37.34 C ANISOU 1440 CA GLY B 43 5150 4844 4190 -820 -897 121 C ATOM 1441 C GLY B 43 12.184 -17.079 43.360 1.00 36.01 C ANISOU 1441 C GLY B 43 5072 4543 4066 -722 -839 137 C ATOM 1442 O GLY B 43 12.141 -18.173 43.919 1.00 36.57 O ANISOU 1442 O GLY B 43 5321 4781 3793 -742 -934 291 O ATOM 1443 N SER B 44 11.126 -16.536 42.762 1.00 34.16 N ANISOU 1443 N SER B 44 4963 4337 3677 -708 -785 13 N ATOM 1444 CA SER B 44 9.883 -17.282 42.554 1.00 32.04 C ANISOU 1444 CA SER B 44 4699 4128 3344 -598 -793 -17 C ATOM 1445 C SER B 44 10.144 -18.563 41.761 1.00 30.69 C ANISOU 1445 C SER B 44 4661 3986 3011 -530 -627 97 C ATOM 1446 O SER B 44 11.096 -18.636 40.979 1.00 30.81 O ANISOU 1446 O SER B 44 4573 4337 2793 -498 -643 56 O ATOM 1447 CB SER B 44 8.869 -16.397 41.815 1.00 32.00 C ANISOU 1447 CB SER B 44 4105 4377 3673 -868 -1091 -57 C ATOM 1448 OG SER B 44 7.985 -17.153 41.003 1.00 36.67 O ANISOU 1448 OG SER B 44 5283 4682 3966 -566 -1417 -276 O ATOM 1449 N ASP B 45 9.335 -19.592 41.998 1.00 25.84 N ANISOU 1449 N ASP B 45 4483 3347 1985 -374 -711 58 N ATOM 1450 CA ASP B 45 9.494 -20.840 41.250 1.00 25.47 C ANISOU 1450 CA ASP B 45 4234 3429 2010 -297 -520 185 C ATOM 1451 C ASP B 45 9.508 -20.592 39.743 1.00 22.41 C ANISOU 1451 C ASP B 45 3737 2899 1877 -110 -459 543 C ATOM 1452 O ASP B 45 8.822 -19.690 39.241 1.00 22.99 O ANISOU 1452 O ASP B 45 3614 3088 2033 -246 -566 286 O ATOM 1453 CB ASP B 45 8.377 -21.810 41.597 1.00 24.07 C ANISOU 1453 CB ASP B 45 4016 3337 1791 -252 -221 265 C ATOM 1454 CG ASP B 45 8.513 -22.368 42.995 1.00 26.31 C ANISOU 1454 CG ASP B 45 4020 3672 2303 -177 -448 294 C ATOM 1455 OD1 ASP B 45 9.514 -22.056 43.686 1.00 28.62 O ANISOU 1455 OD1 ASP B 45 4274 4314 2286 -439 -243 217 O ATOM 1456 OD2 ASP B 45 7.658 -23.187 43.376 1.00 29.38 O ANISOU 1456 OD2 ASP B 45 4404 3794 2964 -581 -38 876 O ATOM 1457 N ALA B 46 10.280 -21.416 39.036 1.00 21.31 N ANISOU 1457 N ALA B 46 3623 2745 1729 -285 -439 415 N ATOM 1458 CA ALA B 46 10.328 -21.375 37.565 1.00 20.65 C ANISOU 1458 CA ALA B 46 3251 2583 2011 -192 -176 355 C ATOM 1459 C ALA B 46 9.803 -22.691 36.985 1.00 18.84 C ANISOU 1459 C ALA B 46 3359 2083 1716 -61 -232 491 C ATOM 1460 O ALA B 46 10.429 -23.735 37.156 1.00 21.82 O ANISOU 1460 O ALA B 46 3605 2345 2340 42 -98 756 O ATOM 1461 CB ALA B 46 11.765 -21.103 37.071 1.00 23.48 C ANISOU 1461 CB ALA B 46 3457 2765 2699 -366 -211 335 C ATOM 1462 N ALA B 47 8.700 -22.623 36.239 1.00 18.93 N ANISOU 1462 N ALA B 47 3236 1834 2120 -252 -57 331 N ATOM 1463 CA ALA B 47 8.197 -23.774 35.502 1.00 17.52 C ANISOU 1463 CA ALA B 47 2943 1932 1780 -236 22 445 C ATOM 1464 C ALA B 47 9.134 -24.143 34.354 1.00 18.33 C ANISOU 1464 C ALA B 47 3049 1677 2238 -345 255 297 C ATOM 1465 O ALA B 47 9.228 -25.309 33.967 1.00 20.50 O ANISOU 1465 O ALA B 47 3426 1736 2626 -415 391 209 O ATOM 1466 CB ALA B 47 6.790 -23.495 34.969 1.00 19.30 C ANISOU 1466 CB ALA B 47 3094 1851 2384 -125 126 243 C ATOM 1467 N LEU B 48 9.760 -23.137 33.751 1.00 16.87 N ANISOU 1467 N LEU B 48 2551 1998 1859 -409 140 423 N ATOM 1468 CA LEU B 48 10.652 -23.358 32.623 1.00 16.43 C ANISOU 1468 CA LEU B 48 2507 1734 2000 -226 -215 155 C ATOM 1469 C LEU B 48 11.804 -22.384 32.715 1.00 17.31 C ANISOU 1469 C LEU B 48 2654 1858 2063 -218 3 432 C ATOM 1470 O LEU B 48 11.606 -21.184 32.931 1.00 18.18 O ANISOU 1470 O LEU B 48 2676 1667 2561 -61 -263 534 O ATOM 1471 CB LEU B 48 9.904 -23.202 31.290 1.00 17.85 C ANISOU 1471 CB LEU B 48 2861 2024 1896 -413 32 222 C ATOM 1472 CG LEU B 48 10.772 -23.329 30.031 1.00 16.95 C ANISOU 1472 CG LEU B 48 2270 2173 1996 -242 -86 402 C ATOM 1473 CD1 LEU B 48 11.247 -24.752 29.881 1.00 21.89 C ANISOU 1473 CD1 LEU B 48 3168 2605 2543 142 229 347 C ATOM 1474 CD2 LEU B 48 9.950 -22.875 28.808 1.00 20.26 C ANISOU 1474 CD2 LEU B 48 2748 2774 2176 -206 74 187 C ATOM 1475 N HIS B 49 13.010 -22.930 32.601 1.00 17.04 N ANISOU 1475 N HIS B 49 2467 1777 2230 -77 -138 502 N ATOM 1476 CA HIS B 49 14.235 -22.152 32.393 1.00 17.28 C ANISOU 1476 CA HIS B 49 2613 2014 1939 -155 -279 429 C ATOM 1477 C HIS B 49 14.829 -22.702 31.098 1.00 17.10 C ANISOU 1477 C HIS B 49 2661 1974 1860 231 -220 357 C ATOM 1478 O HIS B 49 15.196 -23.878 31.027 1.00 20.19 O ANISOU 1478 O HIS B 49 3002 2160 2506 389 -35 498 O ATOM 1479 CB HIS B 49 15.192 -22.374 33.587 1.00 19.52 C ANISOU 1479 CB HIS B 49 2541 2616 2256 24 -634 649 C ATOM 1480 CG HIS B 49 16.586 -21.843 33.399 1.00 20.05 C ANISOU 1480 CG HIS B 49 2630 2443 2545 69 -790 499 C ATOM 1481 ND1 HIS B 49 16.874 -20.495 33.426 1.00 22.54 N ANISOU 1481 ND1 HIS B 49 2943 2844 2774 -346 -455 264 N ATOM 1482 CD2 HIS B 49 17.785 -22.478 33.454 1.00 20.69 C ANISOU 1482 CD2 HIS B 49 2695 2686 2480 -17 -506 546 C ATOM 1483 CE1 HIS B 49 18.184 -20.325 33.362 1.00 23.78 C ANISOU 1483 CE1 HIS B 49 3406 2774 2854 -389 -661 683 C ATOM 1484 NE2 HIS B 49 18.760 -21.508 33.458 1.00 25.02 N ANISOU 1484 NE2 HIS B 49 2906 3216 3382 -390 -317 478 N ATOM 1485 N PHE B 50 14.858 -21.851 30.073 1.00 18.15 N ANISOU 1485 N PHE B 50 2800 2236 1860 -203 5 539 N ATOM 1486 CA PHE B 50 15.365 -22.195 28.736 1.00 17.14 C ANISOU 1486 CA PHE B 50 2412 2019 2079 67 -198 458 C ATOM 1487 C PHE B 50 16.653 -21.402 28.500 1.00 17.92 C ANISOU 1487 C PHE B 50 2556 1990 2260 -10 -329 157 C ATOM 1488 O PHE B 50 16.621 -20.168 28.475 1.00 18.30 O ANISOU 1488 O PHE B 50 2459 1958 2536 -3 -285 377 O ATOM 1489 CB PHE B 50 14.287 -21.809 27.709 1.00 16.76 C ANISOU 1489 CB PHE B 50 2259 1882 2227 26 -93 412 C ATOM 1490 CG PHE B 50 14.741 -21.860 26.276 1.00 16.05 C ANISOU 1490 CG PHE B 50 2408 1579 2109 109 -93 400 C ATOM 1491 CD1 PHE B 50 14.824 -23.067 25.598 1.00 21.01 C ANISOU 1491 CD1 PHE B 50 2815 2334 2831 203 98 -207 C ATOM 1492 CD2 PHE B 50 14.984 -20.692 25.568 1.00 18.76 C ANISOU 1492 CD2 PHE B 50 2610 2149 2367 -116 33 346 C ATOM 1493 CE1 PHE B 50 15.204 -23.108 24.252 1.00 20.85 C ANISOU 1493 CE1 PHE B 50 3148 2050 2721 111 130 235 C ATOM 1494 CE2 PHE B 50 15.347 -20.736 24.227 1.00 17.38 C ANISOU 1494 CE2 PHE B 50 2341 2029 2233 197 -140 303 C ATOM 1495 CZ PHE B 50 15.429 -21.935 23.565 1.00 19.26 C ANISOU 1495 CZ PHE B 50 2574 2127 2615 270 24 -179 C ATOM 1496 N ASN B 51 17.795 -22.096 28.454 1.00 19.42 N ANISOU 1496 N ASN B 51 2535 2311 2532 -10 -357 526 N ATOM 1497 CA ASN B 51 19.112 -21.464 28.642 1.00 19.85 C ANISOU 1497 CA ASN B 51 2615 2380 2545 105 -156 323 C ATOM 1498 C ASN B 51 20.106 -21.867 27.547 1.00 19.82 C ANISOU 1498 C ASN B 51 2568 2347 2615 310 -257 497 C ATOM 1499 O ASN B 51 20.961 -22.734 27.754 1.00 22.25 O ANISOU 1499 O ASN B 51 2577 2452 3421 470 -288 558 O ATOM 1500 CB ASN B 51 19.648 -21.854 30.025 1.00 21.44 C ANISOU 1500 CB ASN B 51 2763 2644 2738 171 -500 608 C ATOM 1501 CG ASN B 51 20.939 -21.148 30.404 1.00 23.74 C ANISOU 1501 CG ASN B 51 2847 3102 3070 340 -299 620 C ATOM 1502 OD1 ASN B 51 21.654 -21.648 31.269 1.00 30.05 O ANISOU 1502 OD1 ASN B 51 3419 4282 3716 186 -1067 831 O ATOM 1503 ND2 ASN B 51 21.111 -19.900 29.970 1.00 24.59 N ANISOU 1503 ND2 ASN B 51 3474 3042 2825 92 -342 351 N ATOM 1504 N PRO B 52 20.004 -21.224 26.387 1.00 19.57 N ANISOU 1504 N PRO B 52 2356 2407 2670 256 -176 340 N ATOM 1505 CA PRO B 52 20.983 -21.452 25.337 1.00 20.38 C ANISOU 1505 CA PRO B 52 2574 2420 2749 392 -24 139 C ATOM 1506 C PRO B 52 22.397 -21.095 25.783 1.00 20.36 C ANISOU 1506 C PRO B 52 2802 2379 2556 381 -379 112 C ATOM 1507 O PRO B 52 22.614 -20.033 26.378 1.00 21.00 O ANISOU 1507 O PRO B 52 2555 2515 2909 205 -69 221 O ATOM 1508 CB PRO B 52 20.506 -20.528 24.214 1.00 20.50 C ANISOU 1508 CB PRO B 52 2612 2734 2441 239 -235 302 C ATOM 1509 CG PRO B 52 19.039 -20.391 24.465 1.00 22.11 C ANISOU 1509 CG PRO B 52 2802 2935 2663 642 365 238 C ATOM 1510 CD PRO B 52 18.913 -20.339 25.950 1.00 19.57 C ANISOU 1510 CD PRO B 52 2834 2075 2523 701 -394 275 C ATOM 1511 N ARG B 53 23.330 -22.015 25.566 1.00 22.34 N ANISOU 1511 N ARG B 53 2611 2789 3089 377 -27 368 N ATOM 1512 CA ARG B 53 24.726 -21.795 25.930 1.00 23.42 C ANISOU 1512 CA ARG B 53 2606 2834 3456 504 -202 555 C ATOM 1513 C ARG B 53 25.583 -21.670 24.678 1.00 24.63 C ANISOU 1513 C ARG B 53 3017 2961 3378 578 -2 459 C ATOM 1514 O ARG B 53 25.883 -22.673 24.021 1.00 26.96 O ANISOU 1514 O ARG B 53 3086 3255 3900 557 282 364 O ATOM 1515 CB ARG B 53 25.236 -22.944 26.798 1.00 24.45 C ANISOU 1515 CB ARG B 53 2883 2836 3569 685 -314 675 C ATOM 1516 CG ARG B 53 24.334 -23.260 27.956 1.00 27.16 C ANISOU 1516 CG ARG B 53 2920 3611 3787 195 -340 545 C ATOM 1517 CD ARG B 53 24.505 -22.241 29.061 1.00 28.70 C ANISOU 1517 CD ARG B 53 3370 3510 4024 325 73 336 C ATOM 1518 NE ARG B 53 23.860 -22.674 30.303 1.00 28.75 N ANISOU 1518 NE ARG B 53 3308 3901 3712 95 102 289 N ATOM 1519 CZ ARG B 53 24.393 -23.497 31.199 1.00 27.66 C ANISOU 1519 CZ ARG B 53 3041 3331 4135 73 32 664 C ATOM 1520 NH1 ARG B 53 25.627 -23.959 31.037 1.00 34.79 N ANISOU 1520 NH1 ARG B 53 3325 4608 5282 235 -330 -236 N ATOM 1521 NH2 ARG B 53 23.722 -23.784 32.312 1.00 30.19 N ANISOU 1521 NH2 ARG B 53 3539 4213 3716 -631 -515 878 N ATOM 1522 N LEU B 54 25.995 -20.448 24.354 1.00 23.48 N ANISOU 1522 N LEU B 54 2504 3104 3313 421 145 271 N ATOM 1523 CA LEU B 54 26.867 -20.232 23.188 1.00 24.71 C ANISOU 1523 CA LEU B 54 2802 3036 3551 349 177 318 C ATOM 1524 C LEU B 54 28.284 -20.715 23.465 1.00 26.35 C ANISOU 1524 C LEU B 54 2725 3335 3952 311 -127 165 C ATOM 1525 O LEU B 54 28.996 -21.121 22.550 1.00 27.67 O ANISOU 1525 O LEU B 54 2883 3761 3867 313 -60 122 O ATOM 1526 CB LEU B 54 26.906 -18.757 22.768 1.00 23.85 C ANISOU 1526 CB LEU B 54 2920 2809 3330 287 -114 47 C ATOM 1527 CG LEU B 54 25.680 -18.149 22.084 1.00 26.97 C ANISOU 1527 CG LEU B 54 3435 3113 3699 200 -314 -18 C ATOM 1528 CD1 LEU B 54 25.942 -16.685 21.792 1.00 34.65 C ANISOU 1528 CD1 LEU B 54 4166 4149 4848 -380 60 184 C ATOM 1529 CD2 LEU B 54 25.319 -18.901 20.814 1.00 27.83 C ANISOU 1529 CD2 LEU B 54 2962 3628 3981 176 -467 539 C ATOM 1530 N ASP B 55 28.708 -20.623 24.723 1.00 28.40 N ANISOU 1530 N ASP B 55 2929 3644 4215 661 -271 192 N ATOM 1531 CA ASP B 55 30.084 -20.954 25.080 1.00 29.17 C ANISOU 1531 CA ASP B 55 2724 3810 4546 572 -400 186 C ATOM 1532 C ASP B 55 30.376 -22.461 25.041 1.00 32.11 C ANISOU 1532 C ASP B 55 3115 4063 5021 673 -364 326 C ATOM 1533 O ASP B 55 31.482 -22.863 24.671 1.00 35.24 O ANISOU 1533 O ASP B 55 3069 4685 5636 594 -377 211 O ATOM 1534 CB ASP B 55 30.517 -20.312 26.415 1.00 30.92 C ANISOU 1534 CB ASP B 55 3137 4123 4486 477 -342 332 C ATOM 1535 CG ASP B 55 29.585 -20.647 27.578 1.00 32.62 C ANISOU 1535 CG ASP B 55 3833 3952 4606 143 -533 383 C ATOM 1536 OD1 ASP B 55 28.592 -21.379 27.389 1.00 33.74 O ANISOU 1536 OD1 ASP B 55 3449 4378 4991 980 -749 313 O ATOM 1537 OD2 ASP B 55 29.880 -20.200 28.709 1.00 38.78 O ANISOU 1537 OD2 ASP B 55 5374 4545 4812 41 -404 447 O ATOM 1538 N THR B 56 29.362 -23.289 25.297 1.00 31.01 N ANISOU 1538 N THR B 56 3077 3891 4812 843 -359 386 N ATOM 1539 CA THR B 56 29.541 -24.744 25.261 1.00 31.18 C ANISOU 1539 CA THR B 56 3261 3788 4796 977 -185 379 C ATOM 1540 C THR B 56 28.696 -25.455 24.201 1.00 31.88 C ANISOU 1540 C THR B 56 3499 3769 4842 896 -39 317 C ATOM 1541 O THR B 56 28.681 -26.686 24.134 1.00 32.23 O ANISOU 1541 O THR B 56 3644 3565 5034 1176 83 39 O ATOM 1542 CB THR B 56 29.260 -25.390 26.632 1.00 31.46 C ANISOU 1542 CB THR B 56 3189 3986 4776 1074 -292 402 C ATOM 1543 OG1 THR B 56 27.918 -25.090 27.039 1.00 33.36 O ANISOU 1543 OG1 THR B 56 3096 4884 4693 1247 -510 747 O ATOM 1544 CG2 THR B 56 30.244 -24.876 27.683 1.00 33.17 C ANISOU 1544 CG2 THR B 56 3452 4228 4920 752 -489 302 C ATOM 1545 N SER B 57 28.019 -24.678 23.359 1.00 29.62 N ANISOU 1545 N SER B 57 3300 3405 4549 919 118 284 N ATOM 1546 CA SER B 57 27.186 -25.223 22.287 1.00 30.34 C ANISOU 1546 CA SER B 57 3478 3590 4458 776 556 54 C ATOM 1547 C SER B 57 26.140 -26.242 22.749 1.00 31.02 C ANISOU 1547 C SER B 57 3764 3374 4645 653 515 64 C ATOM 1548 O SER B 57 25.977 -27.299 22.138 1.00 32.25 O ANISOU 1548 O SER B 57 3842 3470 4942 973 557 -8 O ATOM 1549 CB SER B 57 28.050 -25.771 21.144 1.00 30.79 C ANISOU 1549 CB SER B 57 3576 3267 4855 948 814 56 C ATOM 1550 OG SER B 57 28.721 -24.709 20.486 1.00 34.26 O ANISOU 1550 OG SER B 57 4360 3925 4730 546 707 100 O ATOM 1551 N GLU B 58 25.330 -25.837 23.730 1.00 29.02 N ANISOU 1551 N GLU B 58 3358 3209 4458 829 416 184 N ATOM 1552 CA GLU B 58 24.234 -26.659 24.262 1.00 27.08 C ANISOU 1552 CA GLU B 58 3236 2855 4197 800 57 365 C ATOM 1553 C GLU B 58 23.039 -25.750 24.527 1.00 26.82 C ANISOU 1553 C GLU B 58 3280 2973 3936 590 199 196 C ATOM 1554 O GLU B 58 23.186 -24.530 24.533 1.00 27.64 O ANISOU 1554 O GLU B 58 3470 2995 4035 663 396 338 O ATOM 1555 CB GLU B 58 24.645 -27.309 25.593 1.00 28.99 C ANISOU 1555 CB GLU B 58 3602 2956 4455 954 50 589 C ATOM 1556 CG GLU B 58 25.919 -28.110 25.540 1.00 34.07 C ANISOU 1556 CG GLU B 58 4091 3685 5169 752 -222 282 C ATOM 1557 CD GLU B 58 26.374 -28.534 26.925 1.00 38.84 C ANISOU 1557 CD GLU B 58 4740 4236 5780 953 -724 907 C ATOM 1558 OE1 GLU B 58 26.730 -27.648 27.733 1.00 43.22 O ANISOU 1558 OE1 GLU B 58 5496 5060 5862 735 -549 329 O ATOM 1559 OE2 GLU B 58 26.284 -29.738 27.238 1.00 42.99 O ANISOU 1559 OE2 GLU B 58 5730 4269 6332 840 -141 1163 O ATOM 1560 N VAL B 59 21.886 -26.347 24.807 1.00 25.09 N ANISOU 1560 N VAL B 59 3066 2807 3659 663 51 236 N ATOM 1561 CA VAL B 59 20.778 -25.646 25.460 1.00 24.79 C ANISOU 1561 CA VAL B 59 3188 2646 3582 273 0 122 C ATOM 1562 C VAL B 59 20.397 -26.394 26.714 1.00 24.04 C ANISOU 1562 C VAL B 59 3144 2484 3504 370 -105 226 C ATOM 1563 O VAL B 59 20.031 -27.571 26.655 1.00 28.40 O ANISOU 1563 O VAL B 59 3822 2727 4241 105 -15 272 O ATOM 1564 CB VAL B 59 19.507 -25.571 24.576 1.00 23.23 C ANISOU 1564 CB VAL B 59 2929 2652 3243 235 238 367 C ATOM 1565 CG1 VAL B 59 18.412 -24.798 25.296 1.00 25.59 C ANISOU 1565 CG1 VAL B 59 3638 2435 3648 450 -52 168 C ATOM 1566 CG2 VAL B 59 19.821 -24.958 23.215 1.00 25.57 C ANISOU 1566 CG2 VAL B 59 3456 3121 3139 260 -57 158 C ATOM 1567 N VAL B 60 20.441 -25.697 27.841 1.00 22.18 N ANISOU 1567 N VAL B 60 2818 2224 3383 327 -383 475 N ATOM 1568 CA VAL B 60 20.079 -26.286 29.122 1.00 23.59 C ANISOU 1568 CA VAL B 60 2957 2561 3441 158 -257 464 C ATOM 1569 C VAL B 60 18.627 -25.938 29.481 1.00 23.08 C ANISOU 1569 C VAL B 60 2941 2503 3325 288 -318 474 C ATOM 1570 O VAL B 60 18.172 -24.803 29.285 1.00 22.00 O ANISOU 1570 O VAL B 60 3056 2323 2977 352 -345 362 O ATOM 1571 CB VAL B 60 21.045 -25.812 30.235 1.00 24.66 C ANISOU 1571 CB VAL B 60 2975 2886 3507 236 -460 666 C ATOM 1572 CG1 VAL B 60 20.531 -26.232 31.604 1.00 29.49 C ANISOU 1572 CG1 VAL B 60 3985 3568 3651 119 -355 608 C ATOM 1573 CG2 VAL B 60 22.438 -26.368 29.986 1.00 28.84 C ANISOU 1573 CG2 VAL B 60 3513 3203 4240 760 -276 668 C ATOM 1574 N PHE B 61 17.866 -26.960 29.858 1.00 22.61 N ANISOU 1574 N PHE B 61 2944 2396 3248 91 -278 349 N ATOM 1575 CA PHE B 61 16.502 -26.760 30.348 1.00 22.43 C ANISOU 1575 CA PHE B 61 2969 2359 3194 152 -174 501 C ATOM 1576 C PHE B 61 16.447 -27.168 31.813 1.00 21.21 C ANISOU 1576 C PHE B 61 2984 2102 2971 260 -323 650 C ATOM 1577 O PHE B 61 17.011 -28.181 32.197 1.00 23.21 O ANISOU 1577 O PHE B 61 3257 2188 3371 437 -271 856 O ATOM 1578 CB PHE B 61 15.489 -27.622 29.570 1.00 19.10 C ANISOU 1578 CB PHE B 61 2905 1658 2691 117 -377 352 C ATOM 1579 CG PHE B 61 15.289 -27.223 28.138 1.00 20.90 C ANISOU 1579 CG PHE B 61 2823 2122 2994 16 -38 409 C ATOM 1580 CD1 PHE B 61 16.190 -27.601 27.153 1.00 21.86 C ANISOU 1580 CD1 PHE B 61 2846 2460 3000 -138 -30 468 C ATOM 1581 CD2 PHE B 61 14.078 -26.666 27.743 1.00 21.79 C ANISOU 1581 CD2 PHE B 61 2841 2313 3122 351 -724 88 C ATOM 1582 CE1 PHE B 61 15.946 -27.267 25.814 1.00 24.00 C ANISOU 1582 CE1 PHE B 61 3393 2654 3071 137 -402 -15 C ATOM 1583 CE2 PHE B 61 13.838 -26.305 26.424 1.00 25.61 C ANISOU 1583 CE2 PHE B 61 3837 2591 3303 96 -191 107 C ATOM 1584 CZ PHE B 61 14.763 -26.614 25.453 1.00 22.54 C ANISOU 1584 CZ PHE B 61 3179 2484 2901 -85 -177 123 C ATOM 1585 N ASN B 62 15.680 -26.451 32.619 1.00 20.79 N ANISOU 1585 N ASN B 62 2944 2286 2668 266 -325 766 N ATOM 1586 CA ASN B 62 15.486 -26.855 34.001 1.00 20.77 C ANISOU 1586 CA ASN B 62 2886 2335 2671 -52 -415 642 C ATOM 1587 C ASN B 62 14.229 -26.190 34.570 1.00 20.27 C ANISOU 1587 C ASN B 62 2875 2098 2729 270 -412 923 C ATOM 1588 O ASN B 62 13.535 -25.416 33.885 1.00 20.62 O ANISOU 1588 O ASN B 62 3198 2016 2621 117 -280 590 O ATOM 1589 CB ASN B 62 16.735 -26.487 34.837 1.00 22.65 C ANISOU 1589 CB ASN B 62 3240 2708 2659 188 -963 875 C ATOM 1590 CG ASN B 62 17.029 -27.488 35.960 1.00 23.88 C ANISOU 1590 CG ASN B 62 3174 3027 2871 216 -1541 591 C ATOM 1591 OD1 ASN B 62 16.172 -28.302 36.319 1.00 26.72 O ANISOU 1591 OD1 ASN B 62 3677 2836 3639 459 -1046 1915 O ATOM 1592 ND2 ASN B 62 18.231 -27.396 36.553 1.00 32.55 N ANISOU 1592 ND2 ASN B 62 3547 4646 4172 -133 -947 940 N ATOM 1593 N SER B 63 13.929 -26.519 35.820 1.00 21.82 N ANISOU 1593 N SER B 63 3408 2295 2585 286 -174 644 N ATOM 1594 CA SER B 63 12.835 -25.912 36.557 1.00 24.10 C ANISOU 1594 CA SER B 63 3781 2648 2728 211 -353 651 C ATOM 1595 C SER B 63 13.332 -25.657 37.966 1.00 25.12 C ANISOU 1595 C SER B 63 4098 2925 2521 242 -388 779 C ATOM 1596 O SER B 63 14.316 -26.257 38.387 1.00 27.90 O ANISOU 1596 O SER B 63 4418 3070 3112 523 -818 766 O ATOM 1597 CB SER B 63 11.623 -26.847 36.578 1.00 23.93 C ANISOU 1597 CB SER B 63 3888 2029 3176 140 -65 915 C ATOM 1598 OG SER B 63 11.937 -28.094 37.176 1.00 33.87 O ANISOU 1598 OG SER B 63 5439 2772 4655 185 -110 760 O ATOM 1599 N LYS B 64 12.706 -24.717 38.661 1.00 25.49 N ANISOU 1599 N LYS B 64 4561 3202 1921 -76 -490 733 N ATOM 1600 CA LYS B 64 13.092 -24.420 40.039 1.00 27.61 C ANISOU 1600 CA LYS B 64 4595 3724 2169 -28 -742 828 C ATOM 1601 C LYS B 64 11.866 -24.452 40.944 1.00 31.39 C ANISOU 1601 C LYS B 64 4929 4128 2869 -201 -314 848 C ATOM 1602 O LYS B 64 10.866 -23.796 40.650 1.00 30.43 O ANISOU 1602 O LYS B 64 4895 4149 2517 -168 -274 1019 O ATOM 1603 CB LYS B 64 13.741 -23.032 40.102 1.00 28.60 C ANISOU 1603 CB LYS B 64 4755 3784 2328 -248 -690 640 C ATOM 1604 CG LYS B 64 14.154 -22.573 41.498 1.00 32.10 C ANISOU 1604 CG LYS B 64 5016 4476 2702 -352 -1105 599 C ATOM 1605 CD LYS B 64 14.950 -21.279 41.396 1.00 38.09 C ANISOU 1605 CD LYS B 64 5496 4877 4097 -512 -872 165 C ATOM 1606 CE LYS B 64 15.391 -20.782 42.758 1.00 38.77 C ANISOU 1606 CE LYS B 64 5744 4748 4239 113 -1366 505 C ATOM 1607 NZ LYS B 64 14.918 -19.390 42.989 1.00 45.26 N ANISOU 1607 NZ LYS B 64 5634 5057 6505 252 -861 109 N ATOM 1608 N GLU B 65 11.968 -25.129 42.088 1.00 35.97 N ANISOU 1608 N GLU B 65 5311 4561 3792 -65 -403 745 N ATOM 1609 CA GLU B 65 10.780 -25.377 42.903 1.00 42.48 C ANISOU 1609 CA GLU B 65 6119 5381 4639 -120 -204 631 C ATOM 1610 C GLU B 65 10.712 -24.579 44.205 1.00 45.90 C ANISOU 1610 C GLU B 65 6603 5699 5136 -120 -289 534 C ATOM 1611 O GLU B 65 9.910 -23.651 44.324 1.00 50.04 O ANISOU 1611 O GLU B 65 6954 6144 5914 -89 -214 261 O ATOM 1612 CB GLU B 65 10.561 -26.871 43.143 1.00 44.53 C ANISOU 1612 CB GLU B 65 6381 5355 5184 -186 -82 478 C ATOM 1613 CG GLU B 65 9.779 -27.555 42.013 1.00 48.79 C ANISOU 1613 CG GLU B 65 6911 6179 5446 -199 45 390 C ATOM 1614 CD GLU B 65 9.507 -29.026 42.284 1.00 56.40 C ANISOU 1614 CD GLU B 65 8137 6592 6699 -514 146 103 C ATOM 1615 OE1 GLU B 65 9.384 -29.410 43.472 1.00 59.80 O ANISOU 1615 OE1 GLU B 65 8571 7547 6604 -714 780 162 O ATOM 1616 OE2 GLU B 65 9.429 -29.802 41.304 1.00 59.32 O ANISOU 1616 OE2 GLU B 65 8109 7293 7138 -615 35 -496 O ATOM 1617 N GLN B 66 11.566 -24.910 45.167 1.00 47.77 N ANISOU 1617 N GLN B 66 7083 6187 4877 -345 -516 584 N ATOM 1618 CA GLN B 66 11.516 -24.243 46.467 1.00 49.77 C ANISOU 1618 CA GLN B 66 7251 6456 5201 -396 -529 559 C ATOM 1619 C GLN B 66 12.741 -23.362 46.697 1.00 48.92 C ANISOU 1619 C GLN B 66 7186 6508 4891 -416 -645 538 C ATOM 1620 O GLN B 66 13.180 -23.163 47.844 1.00 51.91 O ANISOU 1620 O GLN B 66 7473 7086 5163 -509 -893 447 O ATOM 1621 CB GLN B 66 11.375 -25.267 47.591 1.00 51.00 C ANISOU 1621 CB GLN B 66 7627 6519 5229 -412 -534 786 C ATOM 1622 CG GLN B 66 10.092 -26.081 47.531 1.00 57.29 C ANISOU 1622 CG GLN B 66 8018 7267 6481 -516 -327 803 C ATOM 1623 CD GLN B 66 9.956 -27.039 48.700 1.00 64.88 C ANISOU 1623 CD GLN B 66 9274 7944 7432 -549 -237 1231 C ATOM 1624 OE1 GLN B 66 10.951 -27.548 49.221 1.00 68.17 O ANISOU 1624 OE1 GLN B 66 9345 8201 8354 -333 -274 1301 O ATOM 1625 NE2 GLN B 66 8.720 -27.283 49.124 1.00 68.20 N ANISOU 1625 NE2 GLN B 66 9504 8301 8106 -491 43 1187 N ATOM 1626 N GLY B 67 13.291 -22.843 45.598 1.00 45.87 N ANISOU 1626 N GLY B 67 6548 6222 4658 -388 -755 572 N ATOM 1627 CA GLY B 67 14.638 -22.293 45.606 1.00 43.61 C ANISOU 1627 CA GLY B 67 6386 5942 4239 -217 -912 708 C ATOM 1628 C GLY B 67 15.647 -23.306 45.102 1.00 42.19 C ANISOU 1628 C GLY B 67 6088 5793 4149 -175 -921 810 C ATOM 1629 O GLY B 67 16.833 -23.003 44.981 1.00 44.51 O ANISOU 1629 O GLY B 67 6302 6055 4555 -237 -845 822 O ATOM 1630 N SER B 68 15.184 -24.530 44.867 1.00 38.83 N ANISOU 1630 N SER B 68 5831 5225 3696 48 -1050 1003 N ATOM 1631 CA SER B 68 16.055 -25.598 44.394 1.00 38.92 C ANISOU 1631 CA SER B 68 5777 5275 3733 35 -914 1096 C ATOM 1632 C SER B 68 15.869 -25.890 42.908 1.00 37.58 C ANISOU 1632 C SER B 68 5401 5042 3835 117 -771 1066 C ATOM 1633 O SER B 68 14.781 -26.259 42.462 1.00 35.24 O ANISOU 1633 O SER B 68 5188 4819 3381 148 -970 1367 O ATOM 1634 CB SER B 68 15.820 -26.870 45.206 1.00 39.07 C ANISOU 1634 CB SER B 68 5967 5322 3554 75 -1043 1336 C ATOM 1635 OG SER B 68 16.211 -26.695 46.562 1.00 42.74 O ANISOU 1635 OG SER B 68 6775 6113 3350 -180 -824 1381 O ATOM 1636 N TRP B 69 16.954 -25.794 42.152 1.00 36.68 N ANISOU 1636 N TRP B 69 5114 5050 3771 138 -757 984 N ATOM 1637 CA TRP B 69 16.945 -26.254 40.771 1.00 33.92 C ANISOU 1637 CA TRP B 69 4825 4483 3578 336 -884 846 C ATOM 1638 C TRP B 69 16.801 -27.770 40.690 1.00 34.48 C ANISOU 1638 C TRP B 69 5019 4448 3633 360 -760 1210 C ATOM 1639 O TRP B 69 17.249 -28.497 41.583 1.00 36.58 O ANISOU 1639 O TRP B 69 5232 4816 3850 750 -1048 1357 O ATOM 1640 CB TRP B 69 18.196 -25.769 40.028 1.00 35.11 C ANISOU 1640 CB TRP B 69 4829 4568 3942 310 -855 774 C ATOM 1641 CG TRP B 69 18.179 -24.290 39.750 1.00 34.51 C ANISOU 1641 CG TRP B 69 4688 4564 3857 -27 -930 366 C ATOM 1642 CD1 TRP B 69 18.848 -23.314 40.437 1.00 37.56 C ANISOU 1642 CD1 TRP B 69 5202 4919 4150 -140 -908 526 C ATOM 1643 CD2 TRP B 69 17.374 -23.615 38.777 1.00 35.11 C ANISOU 1643 CD2 TRP B 69 5266 4403 3670 -198 -671 753 C ATOM 1644 NE1 TRP B 69 18.512 -22.075 39.944 1.00 37.37 N ANISOU 1644 NE1 TRP B 69 5080 4781 4338 -93 -1403 489 N ATOM 1645 CE2 TRP B 69 17.620 -22.235 38.913 1.00 34.58 C ANISOU 1645 CE2 TRP B 69 4883 4585 3670 -236 -1234 388 C ATOM 1646 CE3 TRP B 69 16.468 -24.047 37.802 1.00 31.51 C ANISOU 1646 CE3 TRP B 69 4783 4649 2538 50 -770 1078 C ATOM 1647 CZ2 TRP B 69 16.989 -21.281 38.111 1.00 36.28 C ANISOU 1647 CZ2 TRP B 69 5461 4421 3903 -316 -1255 456 C ATOM 1648 CZ3 TRP B 69 15.841 -23.097 37.006 1.00 30.57 C ANISOU 1648 CZ3 TRP B 69 4852 4210 2551 37 -258 737 C ATOM 1649 CH2 TRP B 69 16.107 -21.732 37.165 1.00 33.39 C ANISOU 1649 CH2 TRP B 69 5272 4519 2893 -330 -465 438 C ATOM 1650 N GLY B 70 16.053 -28.229 39.692 1.00 33.20 N ANISOU 1650 N GLY B 70 4609 4080 3923 463 -815 1095 N ATOM 1651 CA GLY B 70 15.882 -29.653 39.444 1.00 35.74 C ANISOU 1651 CA GLY B 70 5207 4194 4178 349 -472 1248 C ATOM 1652 C GLY B 70 17.024 -30.198 38.617 1.00 34.87 C ANISOU 1652 C GLY B 70 4984 3955 4308 439 -568 1376 C ATOM 1653 O GLY B 70 18.072 -29.564 38.504 1.00 36.16 O ANISOU 1653 O GLY B 70 5101 4223 4413 667 -667 1469 O ATOM 1654 N AARG B 71 16.828 -31.369 38.022 0.50 36.39 N ANISOU 1654 N AARG B 71 5169 3997 4659 373 -364 1194 N ATOM 1655 N BARG B 71 16.796 -31.348 37.994 0.50 36.22 N ANISOU 1655 N BARG B 71 5179 3971 4612 361 -347 1204 N ATOM 1656 CA AARG B 71 17.865 -31.968 37.191 0.50 37.42 C ANISOU 1656 CA AARG B 71 5257 3958 5002 325 -314 1084 C ATOM 1657 CA BARG B 71 17.799 -31.979 37.150 0.50 37.10 C ANISOU 1657 CA BARG B 71 5259 3920 4917 298 -284 1069 C ATOM 1658 C AARG B 71 17.822 -31.420 35.769 0.50 35.85 C ANISOU 1658 C AARG B 71 4958 3713 4947 398 -303 946 C ATOM 1659 C BARG B 71 17.792 -31.359 35.762 0.50 35.65 C ANISOU 1659 C BARG B 71 4965 3682 4897 385 -293 942 C ATOM 1660 O AARG B 71 16.787 -31.464 35.107 0.50 35.79 O ANISOU 1660 O AARG B 71 5041 3599 4956 250 -345 754 O ATOM 1661 O BARG B 71 16.759 -31.331 35.095 0.50 35.74 O ANISOU 1661 O BARG B 71 5058 3614 4905 209 -349 726 O ATOM 1662 CB AARG B 71 17.757 -33.496 37.189 0.50 38.81 C ANISOU 1662 CB AARG B 71 5513 4000 5230 376 -209 1161 C ATOM 1663 CB BARG B 71 17.533 -33.483 37.050 0.50 38.36 C ANISOU 1663 CB BARG B 71 5516 3954 5106 319 -147 1099 C ATOM 1664 CG AARG B 71 18.470 -34.177 38.355 0.50 41.79 C ANISOU 1664 CG AARG B 71 5880 4374 5622 374 -435 1304 C ATOM 1665 CG BARG B 71 16.091 -33.831 36.714 0.50 38.35 C ANISOU 1665 CG BARG B 71 5602 3921 5047 164 -92 938 C ATOM 1666 CD AARG B 71 19.892 -33.655 38.533 0.50 43.22 C ANISOU 1666 CD AARG B 71 5882 4717 5822 406 -675 1437 C ATOM 1667 CD BARG B 71 15.870 -33.871 35.218 0.50 38.42 C ANISOU 1667 CD BARG B 71 5467 3920 5209 346 -380 941 C ATOM 1668 NE AARG B 71 20.795 -34.136 37.488 0.50 41.99 N ANISOU 1668 NE AARG B 71 5984 4375 5595 364 -872 1489 N ATOM 1669 NE BARG B 71 16.957 -34.560 34.530 0.50 37.66 N ANISOU 1669 NE BARG B 71 5176 3617 5517 736 -651 1124 N ATOM 1670 CZ AARG B 71 22.114 -34.240 37.628 0.50 41.78 C ANISOU 1670 CZ AARG B 71 6046 4015 5811 484 -620 1474 C ATOM 1671 CZ BARG B 71 17.051 -34.670 33.210 0.50 39.21 C ANISOU 1671 CZ BARG B 71 5507 3697 5691 756 -333 1140 C ATOM 1672 NH1AARG B 71 22.688 -33.937 38.786 0.50 39.76 N ANISOU 1672 NH1AARG B 71 5236 3725 6145 437 -892 1593 N ATOM 1673 NH1BARG B 71 16.131 -34.113 32.433 0.50 41.04 N ANISOU 1673 NH1BARG B 71 5183 4347 6061 958 -620 650 N ATOM 1674 NH2AARG B 71 22.859 -34.667 36.618 0.50 39.98 N ANISOU 1674 NH2AARG B 71 5504 3995 5689 6 -644 1405 N ATOM 1675 NH2BARG B 71 18.086 -35.292 32.666 0.50 40.71 N ANISOU 1675 NH2BARG B 71 5763 3477 6226 859 -211 905 N ATOM 1676 N GLU B 72 18.949 -30.870 35.326 1.00 34.74 N ANISOU 1676 N GLU B 72 4746 3553 4898 397 -315 1029 N ATOM 1677 CA GLU B 72 19.083 -30.312 33.983 1.00 32.47 C ANISOU 1677 CA GLU B 72 4102 3575 4658 510 -324 912 C ATOM 1678 C GLU B 72 18.724 -31.341 32.921 1.00 30.81 C ANISOU 1678 C GLU B 72 3753 3190 4762 418 -210 891 C ATOM 1679 O GLU B 72 19.020 -32.529 33.065 1.00 31.26 O ANISOU 1679 O GLU B 72 3611 3089 5174 771 -431 1154 O ATOM 1680 CB GLU B 72 20.520 -29.833 33.753 1.00 34.55 C ANISOU 1680 CB GLU B 72 4355 4017 4754 322 -228 893 C ATOM 1681 CG GLU B 72 20.841 -28.487 34.371 1.00 35.54 C ANISOU 1681 CG GLU B 72 4475 4267 4760 337 -133 1008 C ATOM 1682 CD GLU B 72 22.318 -28.134 34.265 1.00 38.23 C ANISOU 1682 CD GLU B 72 4282 4707 5534 490 -516 447 C ATOM 1683 OE1 GLU B 72 23.086 -28.922 33.659 1.00 41.11 O ANISOU 1683 OE1 GLU B 72 4999 4495 6122 345 -339 520 O ATOM 1684 OE2 GLU B 72 22.717 -27.079 34.802 1.00 42.42 O ANISOU 1684 OE2 GLU B 72 5244 4632 6241 661 -144 174 O ATOM 1685 N GLU B 73 18.035 -30.883 31.883 1.00 27.41 N ANISOU 1685 N GLU B 73 3673 2609 4131 416 79 848 N ATOM 1686 CA GLU B 73 18.014 -31.547 30.589 1.00 26.77 C ANISOU 1686 CA GLU B 73 3494 2272 4405 582 101 707 C ATOM 1687 C GLU B 73 18.908 -30.786 29.622 1.00 29.37 C ANISOU 1687 C GLU B 73 3783 2598 4776 487 -10 759 C ATOM 1688 O GLU B 73 18.685 -29.607 29.363 1.00 28.28 O ANISOU 1688 O GLU B 73 3928 2121 4695 630 230 657 O ATOM 1689 CB GLU B 73 16.578 -31.621 30.048 1.00 25.61 C ANISOU 1689 CB GLU B 73 3398 2493 3840 264 133 928 C ATOM 1690 CG GLU B 73 15.685 -32.550 30.870 1.00 28.00 C ANISOU 1690 CG GLU B 73 3342 2800 4493 191 323 1015 C ATOM 1691 CD GLU B 73 14.202 -32.462 30.519 1.00 26.09 C ANISOU 1691 CD GLU B 73 3460 2919 3531 80 -209 1050 C ATOM 1692 OE1 GLU B 73 13.865 -32.311 29.326 1.00 28.97 O ANISOU 1692 OE1 GLU B 73 4215 3136 3656 -43 351 785 O ATOM 1693 OE2 GLU B 73 13.370 -32.651 31.437 1.00 27.90 O ANISOU 1693 OE2 GLU B 73 3427 2981 4192 123 171 599 O ATOM 1694 N ARG B 74 20.052 -31.385 29.303 1.00 31.63 N ANISOU 1694 N ARG B 74 4107 2899 5009 628 209 518 N ATOM 1695 CA ARG B 74 21.072 -30.726 28.498 1.00 34.42 C ANISOU 1695 CA ARG B 74 4502 3488 5087 589 4 625 C ATOM 1696 C ARG B 74 20.969 -31.181 27.045 1.00 35.82 C ANISOU 1696 C ARG B 74 4751 3674 5183 543 114 554 C ATOM 1697 O ARG B 74 21.292 -32.326 26.726 1.00 37.20 O ANISOU 1697 O ARG B 74 4960 3574 5597 738 156 707 O ATOM 1698 CB ARG B 74 22.465 -31.029 29.060 1.00 35.71 C ANISOU 1698 CB ARG B 74 4388 3886 5294 544 -57 703 C ATOM 1699 CG ARG B 74 23.574 -30.181 28.470 1.00 40.39 C ANISOU 1699 CG ARG B 74 4923 4772 5651 386 -50 721 C ATOM 1700 CD ARG B 74 24.834 -30.238 29.320 1.00 44.60 C ANISOU 1700 CD ARG B 74 5155 5542 6248 661 -295 245 C ATOM 1701 NE ARG B 74 24.683 -29.568 30.613 1.00 43.21 N ANISOU 1701 NE ARG B 74 4971 5009 6434 1331 -267 -42 N ATOM 1702 CZ ARG B 74 25.317 -28.449 30.963 1.00 40.37 C ANISOU 1702 CZ ARG B 74 3760 5484 6095 1499 -570 440 C ATOM 1703 NH1 ARG B 74 26.112 -27.825 30.101 1.00 44.05 N ANISOU 1703 NH1 ARG B 74 4713 6057 5966 1617 -101 463 N ATOM 1704 NH2 ARG B 74 25.156 -27.949 32.182 1.00 43.00 N ANISOU 1704 NH2 ARG B 74 4597 5851 5888 1149 -208 322 N ATOM 1705 N GLY B 75 20.374 -30.337 26.204 1.00 35.85 N ANISOU 1705 N GLY B 75 4954 3460 5207 655 89 502 N ATOM 1706 CA GLY B 75 20.277 -30.621 24.769 1.00 36.30 C ANISOU 1706 CA GLY B 75 4979 3538 5274 528 129 378 C ATOM 1707 C GLY B 75 21.571 -30.356 24.014 1.00 36.77 C ANISOU 1707 C GLY B 75 4981 3487 5500 588 245 368 C ATOM 1708 O GLY B 75 22.162 -29.277 24.130 1.00 35.51 O ANISOU 1708 O GLY B 75 4842 2977 5670 857 -5 325 O ATOM 1709 N PRO B 76 22.049 -31.353 23.255 1.00 36.82 N ANISOU 1709 N PRO B 76 5136 3303 5550 520 369 337 N ATOM 1710 CA PRO B 76 23.234 -31.115 22.432 1.00 36.33 C ANISOU 1710 CA PRO B 76 4834 3391 5578 753 442 253 C ATOM 1711 C PRO B 76 22.935 -30.212 21.234 1.00 34.20 C ANISOU 1711 C PRO B 76 4489 3218 5288 548 493 274 C ATOM 1712 O PRO B 76 21.855 -30.294 20.640 1.00 33.26 O ANISOU 1712 O PRO B 76 4535 3146 4955 458 381 336 O ATOM 1713 CB PRO B 76 23.622 -32.524 21.963 1.00 37.71 C ANISOU 1713 CB PRO B 76 5109 3293 5922 987 376 253 C ATOM 1714 CG PRO B 76 23.065 -33.429 23.011 1.00 39.75 C ANISOU 1714 CG PRO B 76 5407 3658 6038 769 629 228 C ATOM 1715 CD PRO B 76 21.778 -32.792 23.437 1.00 38.42 C ANISOU 1715 CD PRO B 76 5311 3359 5926 547 429 222 C ATOM 1716 N GLY B 77 23.890 -29.358 20.880 1.00 32.98 N ANISOU 1716 N GLY B 77 4182 3338 5010 781 569 280 N ATOM 1717 CA GLY B 77 23.671 -28.379 19.820 1.00 30.32 C ANISOU 1717 CA GLY B 77 3830 3204 4487 715 643 380 C ATOM 1718 C GLY B 77 23.007 -27.122 20.348 1.00 29.03 C ANISOU 1718 C GLY B 77 3477 2982 4570 585 489 528 C ATOM 1719 O GLY B 77 22.192 -27.169 21.276 1.00 28.89 O ANISOU 1719 O GLY B 77 3513 2969 4492 441 529 292 O ATOM 1720 N VAL B 78 23.402 -25.979 19.804 1.00 27.62 N ANISOU 1720 N VAL B 78 3323 2902 4268 475 297 466 N ATOM 1721 CA VAL B 78 22.714 -24.734 20.113 1.00 25.70 C ANISOU 1721 CA VAL B 78 3032 2827 3905 388 298 346 C ATOM 1722 C VAL B 78 22.221 -24.096 18.823 1.00 25.95 C ANISOU 1722 C VAL B 78 2971 2891 3998 247 285 290 C ATOM 1723 O VAL B 78 23.022 -23.840 17.914 1.00 26.25 O ANISOU 1723 O VAL B 78 3035 3011 3926 260 451 112 O ATOM 1724 CB VAL B 78 23.621 -23.769 20.940 1.00 24.67 C ANISOU 1724 CB VAL B 78 2926 2530 3916 485 165 412 C ATOM 1725 CG1 VAL B 78 24.821 -23.293 20.122 1.00 25.56 C ANISOU 1725 CG1 VAL B 78 2796 3080 3835 178 201 65 C ATOM 1726 CG2 VAL B 78 22.821 -22.577 21.491 1.00 24.28 C ANISOU 1726 CG2 VAL B 78 3022 2742 3460 688 311 221 C ATOM 1727 N PRO B 79 20.896 -23.874 18.717 1.00 23.03 N ANISOU 1727 N PRO B 79 2733 2627 3389 84 236 267 N ATOM 1728 CA PRO B 79 20.360 -23.405 17.444 1.00 22.67 C ANISOU 1728 CA PRO B 79 2710 2438 3463 -54 256 343 C ATOM 1729 C PRO B 79 20.395 -21.871 17.388 1.00 22.28 C ANISOU 1729 C PRO B 79 2702 2605 3160 -30 189 126 C ATOM 1730 O PRO B 79 19.478 -21.252 16.866 1.00 21.83 O ANISOU 1730 O PRO B 79 2760 2556 2975 -222 183 151 O ATOM 1731 CB PRO B 79 18.922 -23.941 17.461 1.00 23.17 C ANISOU 1731 CB PRO B 79 2868 2680 3254 -31 279 157 C ATOM 1732 CG PRO B 79 18.553 -23.932 18.904 1.00 21.45 C ANISOU 1732 CG PRO B 79 2623 2408 3119 -100 84 554 C ATOM 1733 CD PRO B 79 19.828 -24.210 19.679 1.00 22.86 C ANISOU 1733 CD PRO B 79 2680 2465 3538 275 39 602 C ATOM 1734 N PHE B 80 21.451 -21.283 17.944 1.00 20.53 N ANISOU 1734 N PHE B 80 2369 2354 3075 -221 223 62 N ATOM 1735 CA PHE B 80 21.659 -19.837 17.947 1.00 19.54 C ANISOU 1735 CA PHE B 80 2308 2431 2683 -283 119 80 C ATOM 1736 C PHE B 80 23.109 -19.633 17.556 1.00 22.35 C ANISOU 1736 C PHE B 80 2487 2647 3358 -218 351 0 C ATOM 1737 O PHE B 80 23.930 -20.500 17.809 1.00 22.73 O ANISOU 1737 O PHE B 80 2383 2724 3529 -81 189 0 O ATOM 1738 CB PHE B 80 21.456 -19.272 19.365 1.00 19.74 C ANISOU 1738 CB PHE B 80 2106 2688 2706 -512 26 -57 C ATOM 1739 CG PHE B 80 20.050 -19.426 19.882 1.00 19.61 C ANISOU 1739 CG PHE B 80 2345 2416 2687 -408 -35 64 C ATOM 1740 CD1 PHE B 80 19.061 -18.506 19.544 1.00 20.47 C ANISOU 1740 CD1 PHE B 80 2274 2882 2618 -179 221 -179 C ATOM 1741 CD2 PHE B 80 19.688 -20.565 20.580 1.00 20.64 C ANISOU 1741 CD2 PHE B 80 2591 2656 2595 -130 133 196 C ATOM 1742 CE1 PHE B 80 17.757 -18.685 19.983 1.00 17.98 C ANISOU 1742 CE1 PHE B 80 2303 2317 2209 -261 -181 -244 C ATOM 1743 CE2 PHE B 80 18.397 -20.746 21.035 1.00 22.34 C ANISOU 1743 CE2 PHE B 80 2082 3184 3221 -111 37 30 C ATOM 1744 CZ PHE B 80 17.433 -19.800 20.749 1.00 20.39 C ANISOU 1744 CZ PHE B 80 2597 2416 2732 -138 -628 27 C ATOM 1745 N GLN B 81 23.434 -18.463 17.016 1.00 21.97 N ANISOU 1745 N GLN B 81 2303 2443 3601 -291 547 -6 N ATOM 1746 CA GLN B 81 24.810 -18.132 16.647 1.00 23.93 C ANISOU 1746 CA GLN B 81 2661 2921 3507 -373 516 -99 C ATOM 1747 C GLN B 81 25.134 -16.741 17.189 1.00 22.36 C ANISOU 1747 C GLN B 81 2374 2664 3458 -109 321 122 C ATOM 1748 O GLN B 81 24.310 -15.829 17.091 1.00 21.18 O ANISOU 1748 O GLN B 81 2381 2827 2838 -186 570 -143 O ATOM 1749 CB GLN B 81 24.976 -18.173 15.117 1.00 23.45 C ANISOU 1749 CB GLN B 81 2617 2826 3467 -284 232 -516 C ATOM 1750 CG GLN B 81 24.747 -19.547 14.491 1.00 27.53 C ANISOU 1750 CG GLN B 81 3159 2846 4455 -619 627 -382 C ATOM 1751 CD GLN B 81 23.285 -19.786 14.110 1.00 26.90 C ANISOU 1751 CD GLN B 81 3275 3228 3715 -290 522 -62 C ATOM 1752 OE1 GLN B 81 22.642 -18.939 13.468 1.00 30.02 O ANISOU 1752 OE1 GLN B 81 3903 2948 4555 -608 1073 11 O ATOM 1753 NE2 GLN B 81 22.777 -20.974 14.434 1.00 25.88 N ANISOU 1753 NE2 GLN B 81 2933 3116 3782 -287 743 -692 N ATOM 1754 N ARG B 82 26.343 -16.553 17.715 1.00 22.34 N ANISOU 1754 N ARG B 82 2424 2619 3444 -283 345 -175 N ATOM 1755 CA ARG B 82 26.821 -15.214 18.018 1.00 21.76 C ANISOU 1755 CA ARG B 82 2310 2676 3279 -130 333 160 C ATOM 1756 C ARG B 82 26.668 -14.283 16.827 1.00 21.28 C ANISOU 1756 C ARG B 82 2351 2674 3058 -248 244 32 C ATOM 1757 O ARG B 82 27.000 -14.641 15.696 1.00 23.88 O ANISOU 1757 O ARG B 82 2837 2972 3264 -287 873 -154 O ATOM 1758 CB ARG B 82 28.269 -15.256 18.499 1.00 23.05 C ANISOU 1758 CB ARG B 82 2275 3044 3436 123 136 341 C ATOM 1759 CG ARG B 82 28.433 -15.915 19.857 1.00 25.48 C ANISOU 1759 CG ARG B 82 2557 3423 3698 111 -159 325 C ATOM 1760 CD ARG B 82 29.900 -16.055 20.239 1.00 25.22 C ANISOU 1760 CD ARG B 82 2339 3927 3316 203 241 251 C ATOM 1761 NE ARG B 82 30.011 -16.723 21.528 1.00 29.35 N ANISOU 1761 NE ARG B 82 2619 4420 4109 44 -9 944 N ATOM 1762 CZ ARG B 82 31.097 -17.336 21.973 1.00 37.00 C ANISOU 1762 CZ ARG B 82 3227 5783 5047 955 231 1496 C ATOM 1763 NH1 ARG B 82 32.247 -17.228 21.315 1.00 40.98 N ANISOU 1763 NH1 ARG B 82 3683 6577 5309 750 649 1008 N ATOM 1764 NH2 ARG B 82 31.056 -17.966 23.142 1.00 39.25 N ANISOU 1764 NH2 ARG B 82 3310 6735 4867 601 273 1563 N ATOM 1765 N GLY B 83 26.144 -13.090 17.097 1.00 19.63 N ANISOU 1765 N GLY B 83 2284 2426 2747 -301 210 120 N ATOM 1766 CA GLY B 83 25.949 -12.058 16.083 1.00 19.94 C ANISOU 1766 CA GLY B 83 2462 2598 2514 -514 287 155 C ATOM 1767 C GLY B 83 24.757 -12.259 15.152 1.00 19.46 C ANISOU 1767 C GLY B 83 2280 2604 2509 -432 304 194 C ATOM 1768 O GLY B 83 24.595 -11.488 14.204 1.00 21.00 O ANISOU 1768 O GLY B 83 2501 2747 2729 -453 2 6 O ATOM 1769 N GLN B 84 23.905 -13.255 15.413 1.00 18.81 N ANISOU 1769 N GLN B 84 2210 2619 2315 -323 188 240 N ATOM 1770 CA GLN B 84 22.753 -13.526 14.539 1.00 18.79 C ANISOU 1770 CA GLN B 84 2327 2422 2387 -526 181 -76 C ATOM 1771 C GLN B 84 21.423 -13.360 15.269 1.00 20.07 C ANISOU 1771 C GLN B 84 2436 2696 2492 -196 227 88 C ATOM 1772 O GLN B 84 21.322 -13.651 16.474 1.00 19.63 O ANISOU 1772 O GLN B 84 2412 2325 2720 -457 -72 12 O ATOM 1773 CB GLN B 84 22.821 -14.919 13.918 1.00 20.09 C ANISOU 1773 CB GLN B 84 2294 2559 2779 -21 408 -82 C ATOM 1774 CG GLN B 84 24.070 -15.143 13.046 1.00 20.25 C ANISOU 1774 CG GLN B 84 2259 3146 2289 -291 306 36 C ATOM 1775 CD GLN B 84 24.059 -14.355 11.731 1.00 24.33 C ANISOU 1775 CD GLN B 84 2790 3605 2848 158 473 44 C ATOM 1776 OE1 GLN B 84 23.077 -13.684 11.393 1.00 27.85 O ANISOU 1776 OE1 GLN B 84 2809 4628 3145 18 -176 -4 O ATOM 1777 NE2 GLN B 84 25.181 -14.357 11.038 1.00 28.64 N ANISOU 1777 NE2 GLN B 84 3022 3464 4393 8 1280 83 N ATOM 1778 N PRO B 85 20.396 -12.881 14.539 1.00 19.13 N ANISOU 1778 N PRO B 85 2333 2724 2211 -350 46 86 N ATOM 1779 CA PRO B 85 19.049 -12.783 15.083 1.00 19.90 C ANISOU 1779 CA PRO B 85 2379 2669 2511 -271 39 184 C ATOM 1780 C PRO B 85 18.392 -14.153 15.189 1.00 18.68 C ANISOU 1780 C PRO B 85 2200 2615 2280 -418 213 52 C ATOM 1781 O PRO B 85 18.812 -15.105 14.534 1.00 20.97 O ANISOU 1781 O PRO B 85 2337 2646 2985 -499 367 -179 O ATOM 1782 CB PRO B 85 18.318 -11.898 14.069 1.00 22.60 C ANISOU 1782 CB PRO B 85 2599 3283 2705 -1 361 343 C ATOM 1783 CG PRO B 85 19.040 -12.130 12.783 1.00 22.14 C ANISOU 1783 CG PRO B 85 2684 3277 2451 -270 132 171 C ATOM 1784 CD PRO B 85 20.481 -12.357 13.159 1.00 21.09 C ANISOU 1784 CD PRO B 85 2251 3260 2500 -316 196 436 C ATOM 1785 N PHE B 86 17.325 -14.235 15.976 1.00 16.98 N ANISOU 1785 N PHE B 86 2024 2225 2200 -361 166 110 N ATOM 1786 CA PHE B 86 16.588 -15.484 16.123 1.00 16.30 C ANISOU 1786 CA PHE B 86 2058 2077 2057 -272 1 40 C ATOM 1787 C PHE B 86 15.106 -15.204 16.353 1.00 15.33 C ANISOU 1787 C PHE B 86 2004 1878 1943 -201 90 -186 C ATOM 1788 O PHE B 86 14.730 -14.084 16.702 1.00 15.79 O ANISOU 1788 O PHE B 86 2022 2064 1913 -196 -50 -20 O ATOM 1789 CB PHE B 86 17.144 -16.240 17.332 1.00 16.39 C ANISOU 1789 CB PHE B 86 2184 2068 1973 -267 -231 66 C ATOM 1790 CG PHE B 86 16.986 -15.507 18.640 1.00 15.87 C ANISOU 1790 CG PHE B 86 1819 2156 2053 -120 -91 67 C ATOM 1791 CD1 PHE B 86 15.801 -15.552 19.364 1.00 16.76 C ANISOU 1791 CD1 PHE B 86 2027 2146 2196 -154 -145 -5 C ATOM 1792 CD2 PHE B 86 18.061 -14.821 19.177 1.00 18.16 C ANISOU 1792 CD2 PHE B 86 2240 2342 2315 -623 -248 -145 C ATOM 1793 CE1 PHE B 86 15.677 -14.880 20.575 1.00 17.83 C ANISOU 1793 CE1 PHE B 86 2236 2311 2228 -99 -506 -195 C ATOM 1794 CE2 PHE B 86 17.947 -14.152 20.385 1.00 20.54 C ANISOU 1794 CE2 PHE B 86 2554 2479 2771 -437 -82 -251 C ATOM 1795 CZ PHE B 86 16.779 -14.201 21.097 1.00 19.92 C ANISOU 1795 CZ PHE B 86 2036 3025 2508 -594 -145 -227 C ATOM 1796 N GLU B 87 14.284 -16.239 16.188 1.00 15.26 N ANISOU 1796 N GLU B 87 1891 2057 1850 -263 181 22 N ATOM 1797 CA GLU B 87 12.899 -16.214 16.633 1.00 13.83 C ANISOU 1797 CA GLU B 87 1790 1933 1531 -112 -63 210 C ATOM 1798 C GLU B 87 12.625 -17.523 17.344 1.00 13.81 C ANISOU 1798 C GLU B 87 1528 1936 1781 -72 -117 -23 C ATOM 1799 O GLU B 87 12.820 -18.596 16.774 1.00 15.63 O ANISOU 1799 O GLU B 87 1956 1944 2039 -109 81 -342 O ATOM 1800 CB GLU B 87 11.949 -16.040 15.436 1.00 16.38 C ANISOU 1800 CB GLU B 87 2112 2430 1679 -108 -71 62 C ATOM 1801 CG GLU B 87 10.483 -15.993 15.824 1.00 19.25 C ANISOU 1801 CG GLU B 87 2144 2890 2278 248 -579 77 C ATOM 1802 CD GLU B 87 9.564 -15.710 14.646 1.00 26.73 C ANISOU 1802 CD GLU B 87 2739 3799 3617 726 -318 -275 C ATOM 1803 OE1 GLU B 87 9.607 -14.580 14.119 1.00 30.74 O ANISOU 1803 OE1 GLU B 87 3508 4992 3178 602 -146 359 O ATOM 1804 OE2 GLU B 87 8.697 -16.556 14.353 1.00 31.84 O ANISOU 1804 OE2 GLU B 87 3328 4664 4104 957 -419 -930 O ATOM 1805 N VAL B 88 12.239 -17.423 18.609 1.00 13.23 N ANISOU 1805 N VAL B 88 1540 1893 1592 -182 96 126 N ATOM 1806 CA VAL B 88 11.857 -18.569 19.425 1.00 14.15 C ANISOU 1806 CA VAL B 88 1670 1977 1727 -221 99 69 C ATOM 1807 C VAL B 88 10.352 -18.569 19.648 1.00 14.26 C ANISOU 1807 C VAL B 88 1718 1873 1824 -162 -40 -131 C ATOM 1808 O VAL B 88 9.779 -17.519 19.947 1.00 15.07 O ANISOU 1808 O VAL B 88 1830 1769 2124 -143 -142 -249 O ATOM 1809 CB VAL B 88 12.539 -18.469 20.813 1.00 15.75 C ANISOU 1809 CB VAL B 88 1816 2162 2003 -142 -202 168 C ATOM 1810 CG1 VAL B 88 11.952 -19.499 21.798 1.00 18.54 C ANISOU 1810 CG1 VAL B 88 2645 2330 2068 -580 -302 306 C ATOM 1811 CG2 VAL B 88 14.032 -18.628 20.664 1.00 18.07 C ANISOU 1811 CG2 VAL B 88 1869 2534 2460 60 -209 236 C ATOM 1812 N LEU B 89 9.733 -19.746 19.574 1.00 13.62 N ANISOU 1812 N LEU B 89 1731 1734 1709 -152 101 -131 N ATOM 1813 CA LEU B 89 8.362 -19.927 20.088 1.00 13.62 C ANISOU 1813 CA LEU B 89 1722 1859 1592 -131 123 -61 C ATOM 1814 C LEU B 89 8.437 -20.841 21.284 1.00 13.49 C ANISOU 1814 C LEU B 89 1720 1733 1670 13 2 -163 C ATOM 1815 O LEU B 89 9.054 -21.914 21.204 1.00 15.70 O ANISOU 1815 O LEU B 89 2214 1792 1958 111 404 -123 O ATOM 1816 CB LEU B 89 7.411 -20.530 19.035 1.00 15.40 C ANISOU 1816 CB LEU B 89 2005 2139 1707 -103 44 -231 C ATOM 1817 CG LEU B 89 7.367 -19.931 17.621 1.00 15.29 C ANISOU 1817 CG LEU B 89 1866 2181 1760 -106 -174 -82 C ATOM 1818 CD1 LEU B 89 6.402 -20.731 16.757 1.00 17.84 C ANISOU 1818 CD1 LEU B 89 1947 2727 2105 -531 -279 -487 C ATOM 1819 CD2 LEU B 89 6.979 -18.459 17.681 1.00 19.53 C ANISOU 1819 CD2 LEU B 89 2803 2311 2304 -139 67 -170 C ATOM 1820 N ILE B 90 7.819 -20.421 22.386 1.00 14.70 N ANISOU 1820 N ILE B 90 1868 1781 1936 -111 144 -101 N ATOM 1821 CA ILE B 90 7.535 -21.352 23.462 1.00 15.84 C ANISOU 1821 CA ILE B 90 1889 2115 2015 -275 -27 -63 C ATOM 1822 C ILE B 90 6.046 -21.598 23.471 1.00 14.73 C ANISOU 1822 C ILE B 90 1879 1800 1917 -62 148 -120 C ATOM 1823 O ILE B 90 5.259 -20.654 23.647 1.00 15.66 O ANISOU 1823 O ILE B 90 1970 1793 2186 -113 268 -183 O ATOM 1824 CB ILE B 90 8.000 -20.798 24.830 1.00 17.11 C ANISOU 1824 CB ILE B 90 2031 2302 2168 -321 15 -97 C ATOM 1825 CG1 ILE B 90 9.482 -20.397 24.801 1.00 18.09 C ANISOU 1825 CG1 ILE B 90 2338 2329 2204 -39 -34 246 C ATOM 1826 CG2 ILE B 90 7.648 -21.771 25.943 1.00 19.18 C ANISOU 1826 CG2 ILE B 90 2592 2442 2253 -173 204 167 C ATOM 1827 CD1 ILE B 90 10.407 -21.521 24.608 1.00 19.55 C ANISOU 1827 CD1 ILE B 90 2501 2083 2844 -60 307 -294 C ATOM 1828 N ILE B 91 5.653 -22.854 23.257 1.00 14.63 N ANISOU 1828 N ILE B 91 1903 1757 1898 -245 18 -114 N ATOM 1829 CA ILE B 91 4.243 -23.192 23.051 1.00 15.57 C ANISOU 1829 CA ILE B 91 1982 1867 2066 -325 50 -8 C ATOM 1830 C ILE B 91 3.828 -24.130 24.189 1.00 15.24 C ANISOU 1830 C ILE B 91 1886 2161 1744 -137 59 63 C ATOM 1831 O ILE B 91 4.422 -25.198 24.374 1.00 16.83 O ANISOU 1831 O ILE B 91 2255 2065 2075 -111 422 189 O ATOM 1832 CB ILE B 91 4.044 -23.931 21.689 1.00 16.86 C ANISOU 1832 CB ILE B 91 2161 2508 1738 -342 242 14 C ATOM 1833 CG1 ILE B 91 4.598 -23.118 20.517 1.00 17.47 C ANISOU 1833 CG1 ILE B 91 2347 2575 1713 -272 265 -97 C ATOM 1834 CG2 ILE B 91 2.575 -24.289 21.457 1.00 19.31 C ANISOU 1834 CG2 ILE B 91 2300 2563 2472 -676 -110 -25 C ATOM 1835 CD1 ILE B 91 4.827 -23.961 19.254 1.00 17.53 C ANISOU 1835 CD1 ILE B 91 2438 2378 1845 -183 152 -195 C ATOM 1836 N ALA B 92 2.825 -23.719 24.953 1.00 16.91 N ANISOU 1836 N ALA B 92 2125 2310 1987 -248 78 -248 N ATOM 1837 CA ALA B 92 2.307 -24.560 26.039 1.00 16.36 C ANISOU 1837 CA ALA B 92 2116 2226 1872 -313 15 -208 C ATOM 1838 C ALA B 92 1.382 -25.619 25.453 1.00 18.40 C ANISOU 1838 C ALA B 92 2320 2443 2229 -355 150 -301 C ATOM 1839 O ALA B 92 0.480 -25.302 24.691 1.00 18.58 O ANISOU 1839 O ALA B 92 2095 2720 2245 -358 118 -345 O ATOM 1840 CB ALA B 92 1.548 -23.714 27.061 1.00 18.34 C ANISOU 1840 CB ALA B 92 2241 2640 2085 -269 139 -463 C ATOM 1841 N SER B 93 1.623 -26.869 25.809 1.00 19.88 N ANISOU 1841 N SER B 93 2408 2340 2805 -483 101 -275 N ATOM 1842 CA SER B 93 0.715 -27.969 25.511 1.00 21.17 C ANISOU 1842 CA SER B 93 2604 2440 2998 -605 180 -449 C ATOM 1843 C SER B 93 0.267 -28.636 26.831 1.00 22.57 C ANISOU 1843 C SER B 93 2730 2834 3010 -484 226 -463 C ATOM 1844 O SER B 93 0.690 -28.228 27.909 1.00 21.07 O ANISOU 1844 O SER B 93 2594 2245 3166 -542 538 -337 O ATOM 1845 CB SER B 93 1.414 -28.983 24.596 1.00 24.15 C ANISOU 1845 CB SER B 93 3014 3082 3079 -252 -140 -311 C ATOM 1846 OG SER B 93 2.271 -29.811 25.360 1.00 28.51 O ANISOU 1846 OG SER B 93 3305 3472 4055 -269 -298 -653 O ATOM 1847 N ASP B 94 -0.577 -29.665 26.744 1.00 24.35 N ANISOU 1847 N ASP B 94 2710 2934 3606 -684 53 -434 N ATOM 1848 CA ASP B 94 -1.000 -30.412 27.934 1.00 24.74 C ANISOU 1848 CA ASP B 94 2948 2562 3891 -892 249 -269 C ATOM 1849 C ASP B 94 0.166 -31.084 28.684 1.00 25.07 C ANISOU 1849 C ASP B 94 3321 2598 3605 -817 402 -197 C ATOM 1850 O ASP B 94 0.149 -31.186 29.920 1.00 24.66 O ANISOU 1850 O ASP B 94 3021 2500 3846 -638 486 42 O ATOM 1851 CB ASP B 94 -2.063 -31.462 27.565 1.00 28.79 C ANISOU 1851 CB ASP B 94 3341 3261 4334 -1072 138 -130 C ATOM 1852 CG ASP B 94 -3.389 -30.835 27.117 1.00 32.43 C ANISOU 1852 CG ASP B 94 3405 4063 4852 -975 228 -703 C ATOM 1853 OD1 ASP B 94 -4.012 -30.116 27.926 1.00 40.63 O ANISOU 1853 OD1 ASP B 94 5031 4044 6362 -592 572 -958 O ATOM 1854 OD2 ASP B 94 -3.846 -31.134 25.986 1.00 41.95 O ANISOU 1854 OD2 ASP B 94 5678 5299 4960 -935 -47 216 O ATOM 1855 N AASP B 95 1.145 -31.557 27.913 0.50 22.22 N ANISOU 1855 N AASP B 95 3012 1866 3565 -687 456 -92 N ATOM 1856 N BASP B 95 1.148 -31.593 27.946 0.50 22.04 N ANISOU 1856 N BASP B 95 2961 1805 3607 -678 397 -71 N ATOM 1857 CA AASP B 95 2.219 -32.407 28.421 0.50 23.76 C ANISOU 1857 CA AASP B 95 3357 2121 3549 -552 397 -261 C ATOM 1858 CA BASP B 95 2.205 -32.387 28.573 0.50 23.23 C ANISOU 1858 CA BASP B 95 3247 2026 3551 -583 278 -204 C ATOM 1859 C AASP B 95 3.462 -31.628 28.835 0.50 21.24 C ANISOU 1859 C AASP B 95 2977 1972 3121 -502 548 96 C ATOM 1860 C BASP B 95 3.530 -31.663 28.792 0.50 21.08 C ANISOU 1860 C BASP B 95 2959 1866 3183 -550 464 140 C ATOM 1861 O AASP B 95 4.217 -32.075 29.699 0.50 23.38 O ANISOU 1861 O AASP B 95 3218 2345 3318 -357 558 -143 O ATOM 1862 O BASP B 95 4.377 -32.146 29.543 0.50 22.61 O ANISOU 1862 O BASP B 95 3087 2051 3450 -602 406 26 O ATOM 1863 CB AASP B 95 2.593 -33.458 27.372 0.50 25.39 C ANISOU 1863 CB AASP B 95 3634 2342 3668 -549 459 -373 C ATOM 1864 CB BASP B 95 2.422 -33.705 27.824 0.50 25.13 C ANISOU 1864 CB BASP B 95 3474 2239 3834 -604 346 -313 C ATOM 1865 CG AASP B 95 1.471 -34.452 27.109 0.50 27.73 C ANISOU 1865 CG AASP B 95 4146 2612 3776 -819 490 -453 C ATOM 1866 CG BASP B 95 2.868 -33.495 26.388 0.50 25.27 C ANISOU 1866 CG BASP B 95 3277 2571 3753 -573 356 -310 C ATOM 1867 OD1AASP B 95 0.593 -34.619 27.983 0.50 29.81 O ANISOU 1867 OD1AASP B 95 4266 2547 4513 -885 665 -155 O ATOM 1868 OD1BASP B 95 2.604 -32.410 25.835 0.50 29.52 O ANISOU 1868 OD1BASP B 95 3994 2922 4297 -402 458 -286 O ATOM 1869 OD2AASP B 95 1.498 -35.103 26.045 0.50 32.68 O ANISOU 1869 OD2AASP B 95 5119 2989 4308 -993 -1 -931 O ATOM 1870 OD2BASP B 95 3.422 -34.440 25.785 0.50 34.19 O ANISOU 1870 OD2BASP B 95 4768 3010 5211 -140 644 -491 O ATOM 1871 N GLY B 96 3.705 -30.490 28.184 1.00 19.75 N ANISOU 1871 N GLY B 96 2460 1801 3241 -613 276 -91 N ATOM 1872 CA GLY B 96 4.926 -29.739 28.405 1.00 20.42 C ANISOU 1872 CA GLY B 96 2703 2049 3005 -611 269 167 C ATOM 1873 C GLY B 96 4.974 -28.499 27.549 1.00 19.70 C ANISOU 1873 C GLY B 96 2637 1787 3062 -404 -62 93 C ATOM 1874 O GLY B 96 3.961 -28.077 26.982 1.00 20.53 O ANISOU 1874 O GLY B 96 2826 2157 2817 -108 -7 529 O ATOM 1875 N PHE B 97 6.177 -27.974 27.393 1.00 17.94 N ANISOU 1875 N PHE B 97 2563 1731 2520 -203 323 195 N ATOM 1876 CA PHE B 97 6.432 -26.812 26.558 1.00 16.97 C ANISOU 1876 CA PHE B 97 2377 1888 2180 -328 92 347 C ATOM 1877 C PHE B 97 7.213 -27.231 25.336 1.00 15.92 C ANISOU 1877 C PHE B 97 2094 1856 2097 68 147 161 C ATOM 1878 O PHE B 97 8.258 -27.890 25.459 1.00 19.70 O ANISOU 1878 O PHE B 97 2551 2328 2604 111 361 329 O ATOM 1879 CB PHE B 97 7.243 -25.754 27.318 1.00 18.03 C ANISOU 1879 CB PHE B 97 2502 2022 2326 -224 -36 215 C ATOM 1880 CG PHE B 97 6.550 -25.216 28.523 1.00 16.85 C ANISOU 1880 CG PHE B 97 2524 1599 2280 -208 73 119 C ATOM 1881 CD1 PHE B 97 5.532 -24.271 28.413 1.00 16.38 C ANISOU 1881 CD1 PHE B 97 2202 1591 2429 -325 106 -49 C ATOM 1882 CD2 PHE B 97 6.928 -25.638 29.782 1.00 17.60 C ANISOU 1882 CD2 PHE B 97 2495 1871 2319 -287 298 373 C ATOM 1883 CE1 PHE B 97 4.895 -23.786 29.538 1.00 17.89 C ANISOU 1883 CE1 PHE B 97 2702 1685 2411 -631 -24 -207 C ATOM 1884 CE2 PHE B 97 6.306 -25.155 30.901 1.00 18.53 C ANISOU 1884 CE2 PHE B 97 2723 2078 2240 -304 267 125 C ATOM 1885 CZ PHE B 97 5.287 -24.222 30.794 1.00 18.27 C ANISOU 1885 CZ PHE B 97 2563 1784 2594 -309 317 -56 C ATOM 1886 N LYS B 98 6.728 -26.835 24.159 1.00 17.01 N ANISOU 1886 N LYS B 98 2383 2250 1831 -320 289 -32 N ATOM 1887 CA LYS B 98 7.501 -27.020 22.933 1.00 16.62 C ANISOU 1887 CA LYS B 98 2118 2060 2137 -226 409 33 C ATOM 1888 C LYS B 98 8.373 -25.801 22.728 1.00 15.75 C ANISOU 1888 C LYS B 98 2036 1659 2286 -193 209 228 C ATOM 1889 O LYS B 98 7.864 -24.666 22.736 1.00 18.42 O ANISOU 1889 O LYS B 98 2281 1942 2774 177 437 201 O ATOM 1890 CB LYS B 98 6.585 -27.164 21.709 1.00 17.23 C ANISOU 1890 CB LYS B 98 2377 1931 2238 -581 157 41 C ATOM 1891 CG LYS B 98 5.603 -28.325 21.821 1.00 20.63 C ANISOU 1891 CG LYS B 98 2744 2479 2612 -595 99 -261 C ATOM 1892 CD LYS B 98 4.572 -28.240 20.695 1.00 19.44 C ANISOU 1892 CD LYS B 98 2460 2548 2379 -765 -23 -325 C ATOM 1893 CE LYS B 98 3.725 -29.494 20.615 1.00 23.82 C ANISOU 1893 CE LYS B 98 2607 2723 3721 -588 -381 457 C ATOM 1894 NZ LYS B 98 2.616 -29.310 19.637 1.00 22.20 N ANISOU 1894 NZ LYS B 98 2405 2715 3314 -219 -299 28 N ATOM 1895 N ALA B 99 9.676 -26.021 22.566 1.00 15.84 N ANISOU 1895 N ALA B 99 2134 1792 2091 -135 320 77 N ATOM 1896 CA ALA B 99 10.594 -24.944 22.228 1.00 15.39 C ANISOU 1896 CA ALA B 99 1934 1942 1971 -127 95 92 C ATOM 1897 C ALA B 99 10.979 -25.027 20.774 1.00 15.98 C ANISOU 1897 C ALA B 99 2162 1866 2041 126 302 -2 C ATOM 1898 O ALA B 99 11.616 -26.001 20.359 1.00 18.10 O ANISOU 1898 O ALA B 99 2472 2061 2343 217 462 86 O ATOM 1899 CB ALA B 99 11.819 -25.003 23.113 1.00 17.82 C ANISOU 1899 CB ALA B 99 2353 2137 2279 136 -213 72 C ATOM 1900 N VAL B 100 10.570 -24.023 19.993 1.00 15.30 N ANISOU 1900 N VAL B 100 2211 1824 1778 -53 232 -112 N ATOM 1901 CA VAL B 100 10.843 -23.992 18.556 1.00 15.04 C ANISOU 1901 CA VAL B 100 1880 1882 1949 -104 195 19 C ATOM 1902 C VAL B 100 11.849 -22.867 18.304 1.00 15.10 C ANISOU 1902 C VAL B 100 2018 1728 1991 -152 128 -196 C ATOM 1903 O VAL B 100 11.731 -21.764 18.834 1.00 15.41 O ANISOU 1903 O VAL B 100 1929 1896 2028 -137 153 -251 O ATOM 1904 CB VAL B 100 9.542 -23.660 17.771 1.00 15.23 C ANISOU 1904 CB VAL B 100 1915 2077 1792 -287 27 -207 C ATOM 1905 CG1 VAL B 100 9.800 -23.504 16.285 1.00 18.64 C ANISOU 1905 CG1 VAL B 100 2435 2754 1893 -167 138 -224 C ATOM 1906 CG2 VAL B 100 8.488 -24.724 17.994 1.00 17.28 C ANISOU 1906 CG2 VAL B 100 2389 1916 2261 -445 63 -141 C ATOM 1907 N VAL B 101 12.849 -23.155 17.483 1.00 16.30 N ANISOU 1907 N VAL B 101 1829 2236 2129 -237 319 30 N ATOM 1908 CA VAL B 101 13.825 -22.142 17.101 1.00 15.55 C ANISOU 1908 CA VAL B 101 2030 1952 1926 -51 54 182 C ATOM 1909 C VAL B 101 13.976 -22.243 15.600 1.00 16.13 C ANISOU 1909 C VAL B 101 1968 2223 1937 -261 22 4 C ATOM 1910 O VAL B 101 13.928 -23.335 15.050 1.00 17.31 O ANISOU 1910 O VAL B 101 2101 2303 2171 246 331 -43 O ATOM 1911 CB VAL B 101 15.202 -22.352 17.776 1.00 16.45 C ANISOU 1911 CB VAL B 101 1969 2133 2146 -251 34 337 C ATOM 1912 CG1 VAL B 101 16.087 -21.158 17.491 1.00 18.60 C ANISOU 1912 CG1 VAL B 101 2185 2753 2128 -271 112 445 C ATOM 1913 CG2 VAL B 101 15.045 -22.559 19.276 1.00 17.18 C ANISOU 1913 CG2 VAL B 101 1954 2482 2090 -168 -184 204 C ATOM 1914 N GLY B 102 14.050 -21.124 14.899 1.00 17.68 N ANISOU 1914 N GLY B 102 2049 2340 2326 -276 185 216 N ATOM 1915 CA GLY B 102 14.145 -21.236 13.441 1.00 18.15 C ANISOU 1915 CA GLY B 102 2052 2456 2386 -453 197 -124 C ATOM 1916 C GLY B 102 12.923 -21.947 12.846 1.00 16.93 C ANISOU 1916 C GLY B 102 2144 2380 1906 -283 -96 150 C ATOM 1917 O GLY B 102 11.789 -21.522 13.070 1.00 18.06 O ANISOU 1917 O GLY B 102 2247 2454 2157 -92 -78 -325 O ATOM 1918 N ASP B 103 13.141 -23.030 12.102 1.00 18.13 N ANISOU 1918 N ASP B 103 2233 2454 2201 -291 212 -2 N ATOM 1919 CA ASP B 103 12.052 -23.704 11.394 1.00 18.46 C ANISOU 1919 CA ASP B 103 2412 2351 2250 -365 622 -467 C ATOM 1920 C ASP B 103 11.724 -25.069 11.990 1.00 20.81 C ANISOU 1920 C ASP B 103 2727 2832 2348 -272 542 -262 C ATOM 1921 O ASP B 103 11.011 -25.849 11.360 1.00 24.64 O ANISOU 1921 O ASP B 103 3289 2940 3133 -463 537 -414 O ATOM 1922 CB ASP B 103 12.386 -23.854 9.901 1.00 21.74 C ANISOU 1922 CB ASP B 103 3020 2691 2550 -420 421 -237 C ATOM 1923 CG ASP B 103 12.674 -22.524 9.238 1.00 20.38 C ANISOU 1923 CG ASP B 103 2526 2894 2323 -653 304 -236 C ATOM 1924 OD1 ASP B 103 11.968 -21.544 9.557 1.00 25.39 O ANISOU 1924 OD1 ASP B 103 2339 4031 3274 58 -6 -166 O ATOM 1925 OD2 ASP B 103 13.663 -22.438 8.477 1.00 29.73 O ANISOU 1925 OD2 ASP B 103 3700 4205 3390 -124 1281 -220 O ATOM 1926 N ALA B 104 12.210 -25.349 13.204 1.00 20.02 N ANISOU 1926 N ALA B 104 2771 2296 2537 -151 579 -58 N ATOM 1927 CA ALA B 104 12.011 -26.677 13.788 1.00 21.62 C ANISOU 1927 CA ALA B 104 3260 2100 2853 50 908 -307 C ATOM 1928 C ALA B 104 11.850 -26.661 15.312 1.00 20.30 C ANISOU 1928 C ALA B 104 2976 2110 2626 -153 534 -149 C ATOM 1929 O ALA B 104 12.480 -25.858 16.017 1.00 20.37 O ANISOU 1929 O ALA B 104 2871 2263 2603 -76 556 64 O ATOM 1930 CB ALA B 104 13.153 -27.613 13.376 1.00 25.18 C ANISOU 1930 CB ALA B 104 3468 2644 3454 100 1091 -151 C ATOM 1931 N GLN B 105 11.027 -27.574 15.826 1.00 22.15 N ANISOU 1931 N GLN B 105 3329 2437 2650 -96 805 -164 N ATOM 1932 CA GLN B 105 10.988 -27.816 17.272 1.00 21.52 C ANISOU 1932 CA GLN B 105 2953 2424 2798 -205 703 -172 C ATOM 1933 C GLN B 105 12.329 -28.379 17.757 1.00 20.17 C ANISOU 1933 C GLN B 105 3048 1923 2689 -130 526 -297 C ATOM 1934 O GLN B 105 12.832 -29.371 17.192 1.00 25.32 O ANISOU 1934 O GLN B 105 3784 2158 3675 285 686 -649 O ATOM 1935 CB GLN B 105 9.854 -28.783 17.606 1.00 23.06 C ANISOU 1935 CB GLN B 105 3466 2497 2796 -369 931 -420 C ATOM 1936 CG GLN B 105 9.705 -29.059 19.089 1.00 24.71 C ANISOU 1936 CG GLN B 105 3477 3011 2901 -512 776 -427 C ATOM 1937 CD GLN B 105 8.440 -29.828 19.398 1.00 28.71 C ANISOU 1937 CD GLN B 105 3562 3836 3510 -690 663 -835 C ATOM 1938 OE1 GLN B 105 7.336 -29.366 19.098 1.00 31.71 O ANISOU 1938 OE1 GLN B 105 4021 3811 4213 -551 1127 -911 O ATOM 1939 NE2 GLN B 105 8.595 -31.038 19.915 1.00 32.77 N ANISOU 1939 NE2 GLN B 105 4627 3780 4044 -1167 537 -528 N ATOM 1940 N TYR B 106 12.914 -27.744 18.772 1.00 20.18 N ANISOU 1940 N TYR B 106 2949 2038 2680 181 651 -59 N ATOM 1941 CA TYR B 106 14.236 -28.098 19.269 1.00 20.56 C ANISOU 1941 CA TYR B 106 2867 2148 2796 -91 755 -111 C ATOM 1942 C TYR B 106 14.104 -29.117 20.400 1.00 20.71 C ANISOU 1942 C TYR B 106 2845 2209 2814 259 779 177 C ATOM 1943 O TYR B 106 14.887 -30.059 20.486 1.00 23.33 O ANISOU 1943 O TYR B 106 3353 2060 3451 250 790 352 O ATOM 1944 CB TYR B 106 15.000 -26.855 19.757 1.00 21.39 C ANISOU 1944 CB TYR B 106 2626 2200 3300 208 662 -222 C ATOM 1945 CG TYR B 106 16.317 -27.173 20.444 1.00 22.44 C ANISOU 1945 CG TYR B 106 2706 2266 3552 -56 640 166 C ATOM 1946 CD1 TYR B 106 17.473 -27.387 19.702 1.00 24.48 C ANISOU 1946 CD1 TYR B 106 2947 2349 4005 659 925 242 C ATOM 1947 CD2 TYR B 106 16.371 -27.403 21.813 1.00 27.06 C ANISOU 1947 CD2 TYR B 106 3051 3306 3923 -14 85 -53 C ATOM 1948 CE1 TYR B 106 18.682 -27.757 20.326 1.00 25.09 C ANISOU 1948 CE1 TYR B 106 3068 2489 3975 422 480 309 C ATOM 1949 CE2 TYR B 106 17.551 -27.787 22.442 1.00 31.14 C ANISOU 1949 CE2 TYR B 106 3451 4052 4327 256 323 -216 C ATOM 1950 CZ TYR B 106 18.708 -27.969 21.698 1.00 27.01 C ANISOU 1950 CZ TYR B 106 3014 3097 4152 717 22 -177 C ATOM 1951 OH TYR B 106 19.881 -28.323 22.346 1.00 27.91 O ANISOU 1951 OH TYR B 106 3175 3339 4090 253 22 -382 O ATOM 1952 N HIS B 107 13.129 -28.920 21.286 1.00 19.00 N ANISOU 1952 N HIS B 107 2863 1754 2599 79 679 3 N ATOM 1953 CA HIS B 107 12.962 -29.794 22.449 1.00 20.54 C ANISOU 1953 CA HIS B 107 3045 1867 2890 -37 456 140 C ATOM 1954 C HIS B 107 11.538 -29.703 22.966 1.00 20.37 C ANISOU 1954 C HIS B 107 3049 1615 3075 -42 452 68 C ATOM 1955 O HIS B 107 10.846 -28.705 22.761 1.00 20.33 O ANISOU 1955 O HIS B 107 2882 1968 2874 -173 645 141 O ATOM 1956 CB HIS B 107 13.966 -29.434 23.559 1.00 21.44 C ANISOU 1956 CB HIS B 107 3305 1930 2910 301 282 190 C ATOM 1957 CG HIS B 107 13.974 -30.395 24.712 1.00 24.05 C ANISOU 1957 CG HIS B 107 4046 1974 3117 626 297 304 C ATOM 1958 ND1 HIS B 107 14.310 -31.726 24.571 1.00 32.19 N ANISOU 1958 ND1 HIS B 107 5384 2872 3974 1077 223 390 N ATOM 1959 CD2 HIS B 107 13.741 -30.205 26.033 1.00 23.87 C ANISOU 1959 CD2 HIS B 107 3653 2054 3361 75 163 427 C ATOM 1960 CE1 HIS B 107 14.231 -32.323 25.748 1.00 29.94 C ANISOU 1960 CE1 HIS B 107 5243 2057 4073 790 439 347 C ATOM 1961 NE2 HIS B 107 13.906 -31.418 26.655 1.00 28.55 N ANISOU 1961 NE2 HIS B 107 4820 2767 3259 782 756 520 N ATOM 1962 N HIS B 108 11.096 -30.779 23.601 1.00 22.39 N ANISOU 1962 N HIS B 108 3369 2086 3049 -310 568 18 N ATOM 1963 CA HIS B 108 9.878 -30.779 24.383 1.00 21.67 C ANISOU 1963 CA HIS B 108 3398 1649 3185 -495 446 99 C ATOM 1964 C HIS B 108 10.261 -30.955 25.851 1.00 22.94 C ANISOU 1964 C HIS B 108 3530 2015 3169 17 433 149 C ATOM 1965 O HIS B 108 10.879 -31.956 26.227 1.00 25.70 O ANISOU 1965 O HIS B 108 4144 1943 3677 89 607 401 O ATOM 1966 CB HIS B 108 8.970 -31.927 23.923 1.00 26.45 C ANISOU 1966 CB HIS B 108 3667 2640 3743 -712 681 -431 C ATOM 1967 CG HIS B 108 7.761 -32.119 24.779 1.00 26.36 C ANISOU 1967 CG HIS B 108 3221 3074 3718 -672 517 -174 C ATOM 1968 ND1 HIS B 108 6.552 -31.512 24.504 1.00 33.06 N ANISOU 1968 ND1 HIS B 108 3246 4167 5149 533 989 -106 N ATOM 1969 CD2 HIS B 108 7.571 -32.850 25.903 1.00 29.48 C ANISOU 1969 CD2 HIS B 108 3767 3327 4104 -480 923 516 C ATOM 1970 CE1 HIS B 108 5.667 -31.871 25.420 1.00 32.81 C ANISOU 1970 CE1 HIS B 108 3704 3856 4905 -174 1143 224 C ATOM 1971 NE2 HIS B 108 6.266 -32.662 26.294 1.00 35.34 N ANISOU 1971 NE2 HIS B 108 4097 4101 5230 -640 1129 -127 N ATOM 1972 N PHE B 109 9.868 -30.000 26.681 1.00 19.63 N ANISOU 1972 N PHE B 109 2913 1895 2649 -309 326 135 N ATOM 1973 CA PHE B 109 10.182 -30.051 28.100 1.00 18.47 C ANISOU 1973 CA PHE B 109 2498 1859 2660 -117 323 297 C ATOM 1974 C PHE B 109 8.935 -30.411 28.886 1.00 18.64 C ANISOU 1974 C PHE B 109 2756 1540 2787 10 496 212 C ATOM 1975 O PHE B 109 7.983 -29.625 28.963 1.00 18.57 O ANISOU 1975 O PHE B 109 2579 1806 2670 -6 404 292 O ATOM 1976 CB PHE B 109 10.702 -28.700 28.572 1.00 18.17 C ANISOU 1976 CB PHE B 109 2846 1542 2513 119 -129 325 C ATOM 1977 CG PHE B 109 11.142 -28.682 30.009 1.00 18.22 C ANISOU 1977 CG PHE B 109 2576 1902 2443 -107 114 161 C ATOM 1978 CD1 PHE B 109 12.392 -29.177 30.361 1.00 21.74 C ANISOU 1978 CD1 PHE B 109 3409 1917 2933 126 -79 270 C ATOM 1979 CD2 PHE B 109 10.339 -28.110 30.994 1.00 20.72 C ANISOU 1979 CD2 PHE B 109 3492 1787 2593 63 163 498 C ATOM 1980 CE1 PHE B 109 12.837 -29.142 31.673 1.00 21.58 C ANISOU 1980 CE1 PHE B 109 3015 2190 2993 -160 245 389 C ATOM 1981 CE2 PHE B 109 10.762 -28.095 32.321 1.00 21.34 C ANISOU 1981 CE2 PHE B 109 3185 2432 2489 5 -237 602 C ATOM 1982 CZ PHE B 109 12.035 -28.566 32.652 1.00 20.83 C ANISOU 1982 CZ PHE B 109 3571 1862 2480 116 -63 289 C ATOM 1983 N ARG B 110 8.899 -31.630 29.395 1.00 20.38 N ANISOU 1983 N ARG B 110 3019 1810 2912 -195 338 537 N ATOM 1984 CA ARG B 110 7.739 -32.125 30.124 1.00 19.43 C ANISOU 1984 CA ARG B 110 3063 1762 2557 -344 559 382 C ATOM 1985 C ARG B 110 7.460 -31.254 31.356 1.00 18.97 C ANISOU 1985 C ARG B 110 3060 1631 2515 -587 477 578 C ATOM 1986 O ARG B 110 8.400 -30.843 32.062 1.00 21.25 O ANISOU 1986 O ARG B 110 3067 2014 2992 -277 354 783 O ATOM 1987 CB ARG B 110 8.026 -33.576 30.529 1.00 22.83 C ANISOU 1987 CB ARG B 110 3461 2015 3197 -20 752 330 C ATOM 1988 CG ARG B 110 7.039 -34.218 31.486 1.00 22.57 C ANISOU 1988 CG ARG B 110 3330 2099 3146 175 870 124 C ATOM 1989 CD ARG B 110 7.446 -35.682 31.719 1.00 26.69 C ANISOU 1989 CD ARG B 110 4054 2564 3521 -112 1193 823 C ATOM 1990 NE ARG B 110 6.470 -36.404 32.528 1.00 29.07 N ANISOU 1990 NE ARG B 110 4576 2695 3771 -896 574 841 N ATOM 1991 CZ ARG B 110 6.478 -36.442 33.857 1.00 35.37 C ANISOU 1991 CZ ARG B 110 5064 4295 4080 -885 28 521 C ATOM 1992 NH1 ARG B 110 7.475 -35.895 34.541 1.00 33.47 N ANISOU 1992 NH1 ARG B 110 4326 4303 4088 -84 145 841 N ATOM 1993 NH2 ARG B 110 5.513 -37.086 34.501 1.00 35.62 N ANISOU 1993 NH2 ARG B 110 4470 4826 4236 -1098 492 919 N ATOM 1994 N HIS B 111 6.193 -30.934 31.611 1.00 20.27 N ANISOU 1994 N HIS B 111 3382 1684 2634 -290 678 501 N ATOM 1995 CA HIS B 111 5.869 -30.119 32.789 1.00 23.27 C ANISOU 1995 CA HIS B 111 3540 2248 3053 -466 486 286 C ATOM 1996 C HIS B 111 6.386 -30.760 34.066 1.00 21.18 C ANISOU 1996 C HIS B 111 3570 1806 2669 -622 574 435 C ATOM 1997 O HIS B 111 6.170 -31.960 34.301 1.00 23.97 O ANISOU 1997 O HIS B 111 4102 1785 3220 -319 1030 553 O ATOM 1998 CB HIS B 111 4.364 -29.891 32.942 1.00 20.97 C ANISOU 1998 CB HIS B 111 3190 1980 2796 -686 613 370 C ATOM 1999 CG HIS B 111 3.747 -29.099 31.834 1.00 18.67 C ANISOU 1999 CG HIS B 111 2946 1703 2442 -486 533 -95 C ATOM 2000 ND1 HIS B 111 4.211 -27.856 31.453 1.00 19.46 N ANISOU 2000 ND1 HIS B 111 2838 1703 2851 -559 437 121 N ATOM 2001 CD2 HIS B 111 2.675 -29.358 31.048 1.00 22.27 C ANISOU 2001 CD2 HIS B 111 2937 2329 3193 -633 519 -258 C ATOM 2002 CE1 HIS B 111 3.432 -27.377 30.497 1.00 20.03 C ANISOU 2002 CE1 HIS B 111 2609 2072 2927 -114 20 0 C ATOM 2003 NE2 HIS B 111 2.535 -28.295 30.189 1.00 22.64 N ANISOU 2003 NE2 HIS B 111 3123 2258 3222 -189 780 -533 N ATOM 2004 N ARG B 112 7.008 -29.952 34.916 1.00 23.19 N ANISOU 2004 N ARG B 112 3845 2215 2751 -342 611 640 N ATOM 2005 CA ARG B 112 7.358 -30.382 36.258 1.00 22.88 C ANISOU 2005 CA ARG B 112 4035 2224 2431 -402 461 686 C ATOM 2006 C ARG B 112 6.527 -29.688 37.331 1.00 25.03 C ANISOU 2006 C ARG B 112 4240 2380 2887 -283 704 646 C ATOM 2007 O ARG B 112 6.220 -30.283 38.370 1.00 28.21 O ANISOU 2007 O ARG B 112 4859 2830 3030 -515 633 872 O ATOM 2008 CB ARG B 112 8.848 -30.164 36.512 1.00 26.16 C ANISOU 2008 CB ARG B 112 4235 2436 3268 -286 683 707 C ATOM 2009 CG ARG B 112 9.741 -30.888 35.513 1.00 24.30 C ANISOU 2009 CG ARG B 112 4278 2363 2590 99 36 559 C ATOM 2010 CD ARG B 112 11.191 -30.582 35.805 1.00 31.56 C ANISOU 2010 CD ARG B 112 4524 3194 4272 378 273 819 C ATOM 2011 NE ARG B 112 12.108 -31.151 34.824 1.00 24.97 N ANISOU 2011 NE ARG B 112 3605 2202 3680 148 252 1806 N ATOM 2012 CZ ARG B 112 13.425 -30.954 34.858 1.00 28.51 C ANISOU 2012 CZ ARG B 112 4141 3467 3223 415 434 455 C ATOM 2013 NH1 ARG B 112 13.960 -30.190 35.808 1.00 30.88 N ANISOU 2013 NH1 ARG B 112 3931 3475 4327 309 -264 388 N ATOM 2014 NH2 ARG B 112 14.204 -31.524 33.950 1.00 26.11 N ANISOU 2014 NH2 ARG B 112 4342 2855 2721 555 143 831 N ATOM 2015 N LEU B 113 6.238 -28.409 37.125 1.00 23.04 N ANISOU 2015 N LEU B 113 4136 2325 2292 -287 599 613 N ATOM 2016 CA LEU B 113 5.279 -27.679 37.959 1.00 24.28 C ANISOU 2016 CA LEU B 113 3911 2557 2755 -434 535 324 C ATOM 2017 C LEU B 113 3.963 -27.614 37.212 1.00 21.38 C ANISOU 2017 C LEU B 113 3522 2192 2407 -699 445 108 C ATOM 2018 O LEU B 113 3.958 -27.583 35.989 1.00 24.68 O ANISOU 2018 O LEU B 113 4067 2611 2697 -679 401 -27 O ATOM 2019 CB LEU B 113 5.776 -26.247 38.220 1.00 23.44 C ANISOU 2019 CB LEU B 113 3839 2519 2544 -410 488 237 C ATOM 2020 CG LEU B 113 7.054 -26.079 39.044 1.00 26.53 C ANISOU 2020 CG LEU B 113 4671 2683 2723 -678 354 45 C ATOM 2021 CD1 LEU B 113 7.373 -24.608 39.242 1.00 30.78 C ANISOU 2021 CD1 LEU B 113 5395 2975 3322 -570 602 -25 C ATOM 2022 CD2 LEU B 113 6.884 -26.768 40.383 1.00 36.02 C ANISOU 2022 CD2 LEU B 113 5775 4511 3398 -639 -10 416 C ATOM 2023 N PRO B 114 2.855 -27.405 37.930 1.00 24.02 N ANISOU 2023 N PRO B 114 3731 2687 2708 -876 415 46 N ATOM 2024 CA PRO B 114 1.589 -27.199 37.236 1.00 22.91 C ANISOU 2024 CA PRO B 114 3393 2833 2478 -855 471 -72 C ATOM 2025 C PRO B 114 1.622 -25.991 36.309 1.00 23.04 C ANISOU 2025 C PRO B 114 3649 2654 2450 -797 291 -279 C ATOM 2026 O PRO B 114 2.040 -24.900 36.711 1.00 23.41 O ANISOU 2026 O PRO B 114 3558 2795 2539 -943 479 -31 O ATOM 2027 CB PRO B 114 0.581 -26.994 38.376 1.00 25.15 C ANISOU 2027 CB PRO B 114 3893 3083 2579 -571 739 -215 C ATOM 2028 CG PRO B 114 1.219 -27.625 39.576 1.00 27.67 C ANISOU 2028 CG PRO B 114 3801 3415 3294 -935 518 -70 C ATOM 2029 CD PRO B 114 2.699 -27.395 39.393 1.00 23.39 C ANISOU 2029 CD PRO B 114 3342 3182 2360 -725 741 105 C ATOM 2030 N LEU B 115 1.206 -26.212 35.064 1.00 22.01 N ANISOU 2030 N LEU B 115 3104 2863 2395 -828 257 102 N ATOM 2031 CA LEU B 115 1.158 -25.166 34.054 1.00 22.07 C ANISOU 2031 CA LEU B 115 3247 2698 2438 -703 136 -70 C ATOM 2032 C LEU B 115 0.439 -23.897 34.527 1.00 22.60 C ANISOU 2032 C LEU B 115 3351 2719 2514 -796 229 -40 C ATOM 2033 O LEU B 115 0.886 -22.785 34.262 1.00 22.91 O ANISOU 2033 O LEU B 115 3721 3014 1967 -1022 502 -93 O ATOM 2034 CB LEU B 115 0.517 -25.719 32.770 1.00 24.16 C ANISOU 2034 CB LEU B 115 3380 2930 2867 -810 65 -350 C ATOM 2035 CG LEU B 115 0.357 -24.743 31.605 1.00 23.21 C ANISOU 2035 CG LEU B 115 2999 2852 2965 -562 -365 -359 C ATOM 2036 CD1 LEU B 115 1.707 -24.188 31.160 1.00 24.58 C ANISOU 2036 CD1 LEU B 115 3353 2905 3079 -786 468 -206 C ATOM 2037 CD2 LEU B 115 -0.388 -25.387 30.432 1.00 23.15 C ANISOU 2037 CD2 LEU B 115 2951 3024 2821 -337 -363 -604 C ATOM 2038 N ALA B 116 -0.641 -24.067 35.288 1.00 23.52 N ANISOU 2038 N ALA B 116 3354 2978 2603 -701 393 -216 N ATOM 2039 CA ALA B 116 -1.467 -22.946 35.729 1.00 22.56 C ANISOU 2039 CA ALA B 116 3257 2862 2453 -622 514 -235 C ATOM 2040 C ALA B 116 -0.781 -22.014 36.729 1.00 21.91 C ANISOU 2040 C ALA B 116 3162 2637 2526 -697 382 36 C ATOM 2041 O ALA B 116 -1.282 -20.930 37.030 1.00 24.30 O ANISOU 2041 O ALA B 116 3755 3007 2470 -583 382 -73 O ATOM 2042 CB ALA B 116 -2.770 -23.462 36.306 1.00 25.04 C ANISOU 2042 CB ALA B 116 3342 3235 2933 -606 465 -196 C ATOM 2043 N ARG B 117 0.382 -22.404 37.223 1.00 20.73 N ANISOU 2043 N ARG B 117 3158 2556 2161 -892 355 14 N ATOM 2044 CA ARG B 117 1.097 -21.519 38.140 1.00 19.80 C ANISOU 2044 CA ARG B 117 3120 2278 2122 -865 193 -10 C ATOM 2045 C ARG B 117 1.899 -20.435 37.406 1.00 19.25 C ANISOU 2045 C ARG B 117 3057 2412 1844 -795 239 29 C ATOM 2046 O ARG B 117 2.398 -19.526 38.033 1.00 20.52 O ANISOU 2046 O ARG B 117 3396 2188 2213 -747 -13 281 O ATOM 2047 CB ARG B 117 1.996 -22.329 39.079 1.00 21.90 C ANISOU 2047 CB ARG B 117 3407 2451 2463 -871 198 252 C ATOM 2048 CG ARG B 117 1.272 -22.871 40.338 1.00 26.92 C ANISOU 2048 CG ARG B 117 3972 3161 3094 -1177 66 454 C ATOM 2049 CD ARG B 117 1.954 -22.276 41.592 1.00 33.56 C ANISOU 2049 CD ARG B 117 5096 4480 3175 -291 510 451 C ATOM 2050 NE ARG B 117 3.135 -23.076 41.836 1.00 28.45 N ANISOU 2050 NE ARG B 117 4436 3717 2655 -2 708 1773 N ATOM 2051 CZ ARG B 117 4.295 -22.716 42.391 1.00 27.61 C ANISOU 2051 CZ ARG B 117 4971 3347 2171 -275 544 506 C ATOM 2052 NH1 ARG B 117 4.509 -21.518 42.935 1.00 27.14 N ANISOU 2052 NH1 ARG B 117 4466 3432 2413 -826 351 332 N ATOM 2053 NH2 ARG B 117 5.258 -23.636 42.440 1.00 32.67 N ANISOU 2053 NH2 ARG B 117 5195 3814 3401 508 777 1051 N ATOM 2054 N VAL B 118 2.063 -20.543 36.087 1.00 18.50 N ANISOU 2054 N VAL B 118 2988 2098 1943 -669 200 19 N ATOM 2055 CA VAL B 118 2.904 -19.588 35.366 1.00 18.83 C ANISOU 2055 CA VAL B 118 2915 2111 2125 -611 177 -87 C ATOM 2056 C VAL B 118 2.216 -18.242 35.218 1.00 19.29 C ANISOU 2056 C VAL B 118 2927 2672 1729 -607 261 177 C ATOM 2057 O VAL B 118 1.066 -18.172 34.788 1.00 21.28 O ANISOU 2057 O VAL B 118 3031 2694 2358 -551 210 505 O ATOM 2058 CB VAL B 118 3.283 -20.117 33.973 1.00 17.89 C ANISOU 2058 CB VAL B 118 2794 2057 1943 -131 301 92 C ATOM 2059 CG1 VAL B 118 4.019 -19.026 33.164 1.00 18.24 C ANISOU 2059 CG1 VAL B 118 2533 2496 1900 -531 156 287 C ATOM 2060 CG2 VAL B 118 4.097 -21.405 34.091 1.00 19.99 C ANISOU 2060 CG2 VAL B 118 2892 2282 2420 -385 216 -434 C ATOM 2061 N ARG B 119 2.906 -17.184 35.643 1.00 19.84 N ANISOU 2061 N ARG B 119 3068 2266 2204 -625 418 124 N ATOM 2062 CA ARG B 119 2.338 -15.835 35.646 1.00 21.15 C ANISOU 2062 CA ARG B 119 3384 2480 2172 -381 532 254 C ATOM 2063 C ARG B 119 3.142 -14.799 34.888 1.00 18.78 C ANISOU 2063 C ARG B 119 2877 2133 2124 -290 299 319 C ATOM 2064 O ARG B 119 2.627 -13.722 34.588 1.00 21.20 O ANISOU 2064 O ARG B 119 3039 2384 2630 -155 695 576 O ATOM 2065 CB ARG B 119 2.129 -15.348 37.075 1.00 22.73 C ANISOU 2065 CB ARG B 119 3823 2322 2489 -367 607 10 C ATOM 2066 CG ARG B 119 1.394 -16.330 37.911 1.00 32.12 C ANISOU 2066 CG ARG B 119 5042 3662 3498 -528 1088 857 C ATOM 2067 CD ARG B 119 0.154 -15.729 38.469 1.00 37.11 C ANISOU 2067 CD ARG B 119 5061 3993 5046 -152 856 182 C ATOM 2068 NE ARG B 119 -0.473 -16.625 39.433 1.00 42.29 N ANISOU 2068 NE ARG B 119 5687 5187 5194 -598 664 599 N ATOM 2069 CZ ARG B 119 -1.419 -17.508 39.128 1.00 41.37 C ANISOU 2069 CZ ARG B 119 5713 5197 4808 -761 685 29 C ATOM 2070 NH1 ARG B 119 -1.847 -17.618 37.877 1.00 49.32 N ANISOU 2070 NH1 ARG B 119 6358 7177 5204 -808 178 230 N ATOM 2071 NH2 ARG B 119 -1.970 -18.251 40.086 1.00 40.05 N ANISOU 2071 NH2 ARG B 119 4895 5663 4657 -838 1186 501 N ATOM 2072 N LEU B 120 4.419 -15.078 34.664 1.00 16.72 N ANISOU 2072 N LEU B 120 2655 1927 1768 -275 321 477 N ATOM 2073 CA LEU B 120 5.351 -14.061 34.174 1.00 18.53 C ANISOU 2073 CA LEU B 120 2852 2025 2160 -523 219 -40 C ATOM 2074 C LEU B 120 6.393 -14.704 33.250 1.00 16.10 C ANISOU 2074 C LEU B 120 2651 1970 1495 -362 237 114 C ATOM 2075 O LEU B 120 6.793 -15.873 33.469 1.00 16.81 O ANISOU 2075 O LEU B 120 3026 1667 1694 -259 185 53 O ATOM 2076 CB LEU B 120 6.046 -13.429 35.397 1.00 21.59 C ANISOU 2076 CB LEU B 120 3076 2375 2750 -432 383 -446 C ATOM 2077 CG LEU B 120 7.024 -12.270 35.301 1.00 30.11 C ANISOU 2077 CG LEU B 120 3789 3883 3767 -605 16 -361 C ATOM 2078 CD1 LEU B 120 6.833 -11.389 36.522 1.00 36.37 C ANISOU 2078 CD1 LEU B 120 4452 4801 4563 -675 434 -929 C ATOM 2079 CD2 LEU B 120 8.450 -12.787 35.220 1.00 33.20 C ANISOU 2079 CD2 LEU B 120 4315 4089 4211 287 -391 49 C ATOM 2080 N VAL B 121 6.826 -13.965 32.225 1.00 15.65 N ANISOU 2080 N VAL B 121 2294 1834 1818 -155 132 271 N ATOM 2081 CA VAL B 121 8.009 -14.342 31.436 1.00 14.65 C ANISOU 2081 CA VAL B 121 2164 1741 1661 -284 -43 49 C ATOM 2082 C VAL B 121 9.150 -13.360 31.675 1.00 15.15 C ANISOU 2082 C VAL B 121 2219 1674 1863 -219 -65 -6 C ATOM 2083 O VAL B 121 8.925 -12.150 31.748 1.00 16.45 O ANISOU 2083 O VAL B 121 2458 1486 2304 -113 -144 285 O ATOM 2084 CB VAL B 121 7.686 -14.440 29.933 1.00 17.26 C ANISOU 2084 CB VAL B 121 2440 2227 1891 -289 33 96 C ATOM 2085 CG1 VAL B 121 7.119 -13.147 29.412 1.00 20.22 C ANISOU 2085 CG1 VAL B 121 2998 2342 2340 -212 -45 96 C ATOM 2086 CG2 VAL B 121 8.917 -14.830 29.152 1.00 18.85 C ANISOU 2086 CG2 VAL B 121 2790 2770 1602 -342 256 -75 C ATOM 2087 N GLU B 122 10.351 -13.897 31.877 1.00 14.51 N ANISOU 2087 N GLU B 122 2056 1683 1773 -312 -22 60 N ATOM 2088 CA GLU B 122 11.554 -13.103 32.041 1.00 16.68 C ANISOU 2088 CA GLU B 122 2440 1801 2096 -360 -101 -1 C ATOM 2089 C GLU B 122 12.550 -13.476 30.959 1.00 16.54 C ANISOU 2089 C GLU B 122 2336 1759 2190 -230 -72 60 C ATOM 2090 O GLU B 122 12.742 -14.657 30.651 1.00 18.76 O ANISOU 2090 O GLU B 122 2554 1856 2716 -407 143 1 O ATOM 2091 CB GLU B 122 12.147 -13.390 33.410 1.00 18.77 C ANISOU 2091 CB GLU B 122 2616 2108 2406 -224 -186 31 C ATOM 2092 CG GLU B 122 13.442 -12.702 33.736 1.00 26.22 C ANISOU 2092 CG GLU B 122 3632 3286 3045 -435 -629 -309 C ATOM 2093 CD GLU B 122 13.987 -13.174 35.075 1.00 36.77 C ANISOU 2093 CD GLU B 122 5553 4688 3727 41 -1357 -284 C ATOM 2094 OE1 GLU B 122 14.184 -14.402 35.224 1.00 38.87 O ANISOU 2094 OE1 GLU B 122 5539 4567 4662 -346 -2054 -489 O ATOM 2095 OE2 GLU B 122 14.007 -12.366 36.031 1.00 46.00 O ANISOU 2095 OE2 GLU B 122 7123 5359 4993 -110 -969 -906 O ATOM 2096 N VAL B 123 13.198 -12.475 30.375 1.00 17.56 N ANISOU 2096 N VAL B 123 2236 2132 2303 -532 21 205 N ATOM 2097 CA VAL B 123 14.256 -12.723 29.406 1.00 16.93 C ANISOU 2097 CA VAL B 123 2352 1873 2205 -56 -94 -35 C ATOM 2098 C VAL B 123 15.498 -11.964 29.839 1.00 20.08 C ANISOU 2098 C VAL B 123 2724 2115 2790 -191 80 -263 C ATOM 2099 O VAL B 123 15.446 -10.751 30.035 1.00 22.83 O ANISOU 2099 O VAL B 123 2775 2298 3601 -253 537 -570 O ATOM 2100 CB VAL B 123 13.853 -12.261 27.994 1.00 18.25 C ANISOU 2100 CB VAL B 123 2494 2126 2312 31 282 -64 C ATOM 2101 CG1 VAL B 123 14.955 -12.598 26.983 1.00 19.44 C ANISOU 2101 CG1 VAL B 123 2506 2685 2192 23 405 -217 C ATOM 2102 CG2 VAL B 123 12.528 -12.866 27.601 1.00 20.38 C ANISOU 2102 CG2 VAL B 123 3231 2225 2287 -42 -462 201 C ATOM 2103 N GLY B 124 16.598 -12.681 30.029 1.00 20.70 N ANISOU 2103 N GLY B 124 2186 2682 2998 -452 -78 -253 N ATOM 2104 CA GLY B 124 17.822 -12.070 30.536 1.00 22.45 C ANISOU 2104 CA GLY B 124 2374 2947 3208 -559 -211 -476 C ATOM 2105 C GLY B 124 19.073 -12.731 29.996 1.00 21.71 C ANISOU 2105 C GLY B 124 2327 2818 3104 -702 -79 -337 C ATOM 2106 O GLY B 124 19.006 -13.623 29.148 1.00 19.86 O ANISOU 2106 O GLY B 124 2246 2633 2667 -346 -199 -303 O ATOM 2107 N GLY B 125 20.228 -12.270 30.461 1.00 22.96 N ANISOU 2107 N GLY B 125 2405 3305 3014 -334 -163 -218 N ATOM 2108 CA GLY B 125 21.486 -12.811 29.968 1.00 21.30 C ANISOU 2108 CA GLY B 125 2194 3208 2691 -369 40 -60 C ATOM 2109 C GLY B 125 21.994 -12.057 28.758 1.00 21.36 C ANISOU 2109 C GLY B 125 2557 2812 2744 -360 -411 43 C ATOM 2110 O GLY B 125 21.660 -10.893 28.549 1.00 21.01 O ANISOU 2110 O GLY B 125 2553 2886 2544 -461 -133 -21 O ATOM 2111 N ASP B 126 22.860 -12.717 27.995 1.00 20.81 N ANISOU 2111 N ASP B 126 2306 2751 2847 -128 -318 233 N ATOM 2112 CA ASP B 126 23.578 -12.093 26.884 1.00 21.75 C ANISOU 2112 CA ASP B 126 2358 3057 2849 -122 -305 323 C ATOM 2113 C ASP B 126 22.720 -12.105 25.626 1.00 20.70 C ANISOU 2113 C ASP B 126 2495 2647 2721 -194 -302 70 C ATOM 2114 O ASP B 126 22.820 -13.011 24.803 1.00 22.08 O ANISOU 2114 O ASP B 126 2761 2722 2903 -120 -208 169 O ATOM 2115 CB ASP B 126 24.894 -12.838 26.611 1.00 22.35 C ANISOU 2115 CB ASP B 126 2333 3008 3150 -135 -584 403 C ATOM 2116 CG ASP B 126 25.830 -12.832 27.805 1.00 24.06 C ANISOU 2116 CG ASP B 126 2696 3133 3311 85 -977 -180 C ATOM 2117 OD1 ASP B 126 25.806 -11.860 28.599 1.00 29.66 O ANISOU 2117 OD1 ASP B 126 3054 3888 4327 -82 -1067 -267 O ATOM 2118 OD2 ASP B 126 26.552 -13.833 27.981 1.00 29.94 O ANISOU 2118 OD2 ASP B 126 3422 3341 4609 426 -1427 -161 O ATOM 2119 N VAL B 127 21.812 -11.137 25.530 1.00 18.69 N ANISOU 2119 N VAL B 127 2156 2602 2343 -244 -357 196 N ATOM 2120 CA VAL B 127 20.846 -11.092 24.442 1.00 17.91 C ANISOU 2120 CA VAL B 127 2260 2120 2422 -206 -329 -139 C ATOM 2121 C VAL B 127 20.362 -9.657 24.333 1.00 17.63 C ANISOU 2121 C VAL B 127 2355 2215 2127 -81 -296 -207 C ATOM 2122 O VAL B 127 20.179 -8.976 25.355 1.00 19.72 O ANISOU 2122 O VAL B 127 2460 2521 2509 -26 -16 -447 O ATOM 2123 CB VAL B 127 19.665 -12.133 24.639 1.00 18.06 C ANISOU 2123 CB VAL B 127 2139 2440 2282 -303 -441 105 C ATOM 2124 CG1 VAL B 127 18.854 -11.859 25.898 1.00 20.21 C ANISOU 2124 CG1 VAL B 127 2337 2617 2724 210 -272 435 C ATOM 2125 CG2 VAL B 127 18.741 -12.167 23.425 1.00 22.58 C ANISOU 2125 CG2 VAL B 127 2782 3098 2697 -724 -1069 -27 C ATOM 2126 N GLN B 128 20.109 -9.228 23.096 1.00 18.96 N ANISOU 2126 N GLN B 128 2277 2455 2472 -315 -131 -13 N ATOM 2127 CA GLN B 128 19.390 -7.998 22.796 1.00 20.17 C ANISOU 2127 CA GLN B 128 2167 2674 2821 -392 -318 -64 C ATOM 2128 C GLN B 128 17.976 -8.387 22.387 1.00 20.88 C ANISOU 2128 C GLN B 128 2430 2799 2702 -195 -361 -252 C ATOM 2129 O GLN B 128 17.770 -9.087 21.393 1.00 23.42 O ANISOU 2129 O GLN B 128 2548 3426 2921 -238 -479 -458 O ATOM 2130 CB GLN B 128 20.102 -7.221 21.680 1.00 21.49 C ANISOU 2130 CB GLN B 128 2535 3051 2578 -268 -336 177 C ATOM 2131 CG GLN B 128 19.270 -6.146 20.984 1.00 30.39 C ANISOU 2131 CG GLN B 128 3674 3838 4033 -239 11 992 C ATOM 2132 CD GLN B 128 19.838 -5.779 19.608 1.00 35.92 C ANISOU 2132 CD GLN B 128 4688 5200 3760 224 80 544 C ATOM 2133 OE1 GLN B 128 19.134 -5.830 18.590 1.00 36.30 O ANISOU 2133 OE1 GLN B 128 4963 4857 3972 701 -63 196 O ATOM 2134 NE2 GLN B 128 21.121 -5.424 19.573 1.00 41.30 N ANISOU 2134 NE2 GLN B 128 5389 4846 5456 -481 59 591 N ATOM 2135 N LEU B 129 17.035 -8.098 23.274 1.00 20.17 N ANISOU 2135 N LEU B 129 2322 2305 3034 -293 -340 -243 N ATOM 2136 CA LEU B 129 15.646 -8.483 23.056 1.00 18.70 C ANISOU 2136 CA LEU B 129 2305 2424 2375 -422 -92 -203 C ATOM 2137 C LEU B 129 14.990 -7.504 22.082 1.00 17.85 C ANISOU 2137 C LEU B 129 2392 2119 2270 -360 1 -14 C ATOM 2138 O LEU B 129 15.026 -6.291 22.296 1.00 20.54 O ANISOU 2138 O LEU B 129 3166 2117 2521 -272 -297 -88 O ATOM 2139 CB LEU B 129 14.913 -8.466 24.398 1.00 19.70 C ANISOU 2139 CB LEU B 129 2298 2839 2345 -379 -5 -62 C ATOM 2140 CG LEU B 129 13.420 -8.785 24.387 1.00 18.61 C ANISOU 2140 CG LEU B 129 2482 2547 2039 -257 195 -71 C ATOM 2141 CD1 LEU B 129 13.174 -10.199 23.850 1.00 21.09 C ANISOU 2141 CD1 LEU B 129 2930 2214 2869 -704 -139 -123 C ATOM 2142 CD2 LEU B 129 12.803 -8.613 25.771 1.00 24.83 C ANISOU 2142 CD2 LEU B 129 3716 3446 2270 -1043 639 -463 C ATOM 2143 N ASP B 130 14.455 -8.012 20.981 1.00 17.29 N ANISOU 2143 N ASP B 130 2031 2240 2299 -259 -139 -128 N ATOM 2144 CA ASP B 130 13.771 -7.158 20.010 1.00 18.82 C ANISOU 2144 CA ASP B 130 2584 1894 2670 -298 -50 -69 C ATOM 2145 C ASP B 130 12.274 -7.032 20.351 1.00 18.81 C ANISOU 2145 C ASP B 130 2523 1864 2758 -219 -17 -104 C ATOM 2146 O ASP B 130 11.720 -5.936 20.328 1.00 21.34 O ANISOU 2146 O ASP B 130 2786 2033 3287 -273 -294 -363 O ATOM 2147 CB ASP B 130 13.981 -7.655 18.560 1.00 20.79 C ANISOU 2147 CB ASP B 130 2903 2378 2616 -169 -70 -253 C ATOM 2148 CG ASP B 130 15.477 -7.676 18.134 1.00 26.37 C ANISOU 2148 CG ASP B 130 3897 3057 3064 -606 473 -167 C ATOM 2149 OD1 ASP B 130 16.304 -6.918 18.698 1.00 27.07 O ANISOU 2149 OD1 ASP B 130 3903 2569 3813 -587 582 -163 O ATOM 2150 OD2 ASP B 130 15.833 -8.446 17.205 1.00 30.98 O ANISOU 2150 OD2 ASP B 130 4531 3738 3501 -319 777 -560 O ATOM 2151 N SER B 131 11.630 -8.149 20.691 1.00 17.87 N ANISOU 2151 N SER B 131 2400 1881 2505 -543 8 -386 N ATOM 2152 CA SER B 131 10.258 -8.138 21.177 1.00 18.59 C ANISOU 2152 CA SER B 131 2390 2168 2504 -329 -213 -34 C ATOM 2153 C SER B 131 9.865 -9.448 21.852 1.00 16.69 C ANISOU 2153 C SER B 131 1991 1953 2396 -298 -48 -275 C ATOM 2154 O SER B 131 10.381 -10.542 21.522 1.00 17.80 O ANISOU 2154 O SER B 131 2326 2021 2415 21 -44 -342 O ATOM 2155 CB SER B 131 9.276 -7.824 20.042 1.00 19.11 C ANISOU 2155 CB SER B 131 2671 2244 2343 -92 -191 108 C ATOM 2156 OG SER B 131 9.349 -8.824 19.043 1.00 22.88 O ANISOU 2156 OG SER B 131 3350 2526 2817 -414 -334 37 O ATOM 2157 N VAL B 132 8.871 -9.315 22.734 1.00 17.93 N ANISOU 2157 N VAL B 132 2434 2196 2182 -161 183 -193 N ATOM 2158 CA VAL B 132 8.166 -10.451 23.321 1.00 16.74 C ANISOU 2158 CA VAL B 132 2436 2107 1818 -315 -217 -99 C ATOM 2159 C VAL B 132 6.677 -10.291 23.074 1.00 17.29 C ANISOU 2159 C VAL B 132 2542 1922 2105 491 89 60 C ATOM 2160 O VAL B 132 6.075 -9.289 23.462 1.00 20.26 O ANISOU 2160 O VAL B 132 3150 2109 2438 553 163 -174 O ATOM 2161 CB VAL B 132 8.376 -10.570 24.859 1.00 21.40 C ANISOU 2161 CB VAL B 132 3049 2798 2281 -321 100 -17 C ATOM 2162 CG1 VAL B 132 7.415 -11.603 25.443 1.00 25.46 C ANISOU 2162 CG1 VAL B 132 2827 3538 3308 -280 -87 544 C ATOM 2163 CG2 VAL B 132 9.807 -10.936 25.164 1.00 25.98 C ANISOU 2163 CG2 VAL B 132 3280 3868 2723 -92 -679 -96 C ATOM 2164 N AARG B 133 6.096 -11.302 22.436 0.50 17.06 N ANISOU 2164 N AARG B 133 2406 2256 1816 173 -177 -52 N ATOM 2165 N BARG B 133 6.077 -11.255 22.391 0.50 17.53 N ANISOU 2165 N BARG B 133 2418 2318 1925 270 -162 -91 N ATOM 2166 CA AARG B 133 4.662 -11.349 22.186 0.50 17.91 C ANISOU 2166 CA AARG B 133 2446 2513 1845 382 -83 -146 C ATOM 2167 CA BARG B 133 4.633 -11.231 22.197 0.50 18.85 C ANISOU 2167 CA BARG B 133 2423 2715 2024 497 -54 -247 C ATOM 2168 C AARG B 133 4.086 -12.532 22.895 0.50 16.85 C ANISOU 2168 C AARG B 133 2214 2256 1931 234 -293 -527 C ATOM 2169 C BARG B 133 4.034 -12.505 22.748 0.50 17.09 C ANISOU 2169 C BARG B 133 2228 2341 1923 326 -281 -539 C ATOM 2170 O AARG B 133 4.673 -13.617 22.866 0.50 18.75 O ANISOU 2170 O AARG B 133 2393 2016 2714 256 -59 -678 O ATOM 2171 O BARG B 133 4.652 -13.570 22.662 0.50 18.64 O ANISOU 2171 O BARG B 133 2296 2099 2685 364 10 -712 O ATOM 2172 CB AARG B 133 4.367 -11.515 20.696 0.50 19.61 C ANISOU 2172 CB AARG B 133 2748 2917 1785 509 -318 130 C ATOM 2173 CB BARG B 133 4.262 -11.064 20.714 0.50 20.98 C ANISOU 2173 CB BARG B 133 2536 3274 2158 881 -308 11 C ATOM 2174 CG AARG B 133 4.686 -10.299 19.890 0.50 23.28 C ANISOU 2174 CG AARG B 133 3286 2961 2599 -131 50 601 C ATOM 2175 CG BARG B 133 4.915 -9.863 20.014 0.50 26.73 C ANISOU 2175 CG BARG B 133 3173 3842 3140 746 -36 15 C ATOM 2176 CD AARG B 133 4.605 -9.051 20.758 0.50 27.81 C ANISOU 2176 CD AARG B 133 4585 4482 1500 404 -78 697 C ATOM 2177 CD BARG B 133 3.914 -8.728 19.701 0.50 24.11 C ANISOU 2177 CD BARG B 133 1853 3969 3337 198 -827 -222 C ATOM 2178 NE AARG B 133 4.549 -7.850 19.945 0.50 30.93 N ANISOU 2178 NE AARG B 133 4292 3704 3753 1010 -427 634 N ATOM 2179 NE BARG B 133 4.571 -7.547 19.113 0.50 25.53 N ANISOU 2179 NE BARG B 133 2817 4667 2214 -205 -11 -493 N ATOM 2180 CZ AARG B 133 3.564 -7.565 19.099 0.50 26.76 C ANISOU 2180 CZ AARG B 133 3663 3200 3303 354 -454 773 C ATOM 2181 CZ BARG B 133 5.219 -6.631 19.829 0.50 20.45 C ANISOU 2181 CZ BARG B 133 2105 2515 3150 -130 492 -151 C ATOM 2182 NH1AARG B 133 2.473 -8.330 19.033 0.50 18.42 N ANISOU 2182 NH1AARG B 133 3050 2176 1770 245 -874 -451 N ATOM 2183 NH1BARG B 133 5.248 -6.752 21.133 0.50 18.19 N ANISOU 2183 NH1BARG B 133 1664 3191 2054 -4 -627 -657 N ATOM 2184 NH2AARG B 133 3.670 -6.495 18.331 0.50 31.91 N ANISOU 2184 NH2AARG B 133 5566 2273 4284 847 772 213 N ATOM 2185 NH2BARG B 133 5.808 -5.584 19.255 0.50 23.72 N ANISOU 2185 NH2BARG B 133 2430 4430 2152 172 -578 524 N ATOM 2186 N ILE B 134 2.838 -12.395 23.318 1.00 17.98 N ANISOU 2186 N ILE B 134 2540 2312 1977 222 -69 -530 N ATOM 2187 CA ILE B 134 2.129 -13.537 23.856 1.00 18.78 C ANISOU 2187 CA ILE B 134 2329 2759 2045 150 -69 -497 C ATOM 2188 C ILE B 134 0.811 -13.641 23.105 1.00 19.79 C ANISOU 2188 C ILE B 134 2107 2799 2613 385 -289 -580 C ATOM 2189 O ILE B 134 0.047 -12.680 23.046 1.00 24.24 O ANISOU 2189 O ILE B 134 2566 3352 3289 824 -498 -874 O ATOM 2190 CB ILE B 134 1.934 -13.401 25.378 1.00 21.56 C ANISOU 2190 CB ILE B 134 2704 3318 2169 -87 7 -253 C ATOM 2191 CG1 ILE B 134 3.311 -13.262 26.058 1.00 23.55 C ANISOU 2191 CG1 ILE B 134 3217 3396 2335 -596 -202 -272 C ATOM 2192 CG2 ILE B 134 1.137 -14.597 25.911 1.00 24.28 C ANISOU 2192 CG2 ILE B 134 3086 3484 2655 -347 479 -544 C ATOM 2193 CD1 ILE B 134 3.280 -12.734 27.481 1.00 29.84 C ANISOU 2193 CD1 ILE B 134 4393 3487 3455 -304 -507 -605 C ATOM 2194 N PHE B 135 0.616 -14.769 22.433 1.00 19.89 N ANISOU 2194 N PHE B 135 2165 3068 2321 98 -456 -406 N ATOM 2195 CA PHE B 135 -0.558 -15.003 21.601 1.00 22.77 C ANISOU 2195 CA PHE B 135 2159 3310 3183 0 -350 -280 C ATOM 2196 C PHE B 135 -1.382 -16.145 22.204 1.00 27.57 C ANISOU 2196 C PHE B 135 2566 4033 3873 -142 -535 118 C ATOM 2197 O PHE B 135 -0.876 -16.955 22.987 1.00 26.35 O ANISOU 2197 O PHE B 135 2301 3769 3940 192 -457 146 O ATOM 2198 CB PHE B 135 -0.120 -15.353 20.170 1.00 21.31 C ANISOU 2198 CB PHE B 135 2486 3264 2345 -196 -567 -221 C ATOM 2199 CG PHE B 135 0.602 -14.235 19.453 1.00 21.49 C ANISOU 2199 CG PHE B 135 2231 3389 2542 72 -493 -270 C ATOM 2200 CD1 PHE B 135 -0.048 -13.034 19.175 1.00 20.69 C ANISOU 2200 CD1 PHE B 135 2406 2660 2795 -266 -600 -529 C ATOM 2201 CD2 PHE B 135 1.884 -14.422 18.963 1.00 22.89 C ANISOU 2201 CD2 PHE B 135 2403 3516 2778 -182 -419 -171 C ATOM 2202 CE1 PHE B 135 0.601 -12.010 18.502 1.00 20.67 C ANISOU 2202 CE1 PHE B 135 2293 3094 2467 199 -726 -407 C ATOM 2203 CE2 PHE B 135 2.546 -13.405 18.289 1.00 22.96 C ANISOU 2203 CE2 PHE B 135 2873 3812 2036 -56 -408 469 C ATOM 2204 CZ PHE B 135 1.896 -12.193 18.048 1.00 21.33 C ANISOU 2204 CZ PHE B 135 2310 3825 1968 -135 -531 -287 C ATOM 2205 OXT PHE B 135 -2.575 -16.312 21.897 1.00 31.84 O ANISOU 2205 OXT PHE B 135 2718 4454 4924 -337 -766 444 O TER 2206 PHE B 135 HETATM 2207 C ACT A1136 -3.366 -0.893 2.327 1.00 42.94 C ANISOU 2207 C ACT A1136 5753 4296 6264 361 873 -562 C HETATM 2208 O ACT A1136 -2.391 -0.174 1.982 1.00 46.15 O ANISOU 2208 O ACT A1136 6055 4877 6602 519 1181 -543 O HETATM 2209 OXT ACT A1136 -3.428 -1.190 3.546 1.00 40.31 O ANISOU 2209 OXT ACT A1136 5368 4020 5928 271 1067 -842 O HETATM 2210 CH3 ACT A1136 -4.400 -1.367 1.343 1.00 39.28 C ANISOU 2210 CH3 ACT A1136 5484 3439 6000 481 919 -610 C HETATM 2211 O HOH A2001 1.569 -23.076 -6.802 1.00 34.86 O ANISOU 2211 O HOH A2001 3931 4944 4369 -844 -831 -430 O HETATM 2212 O HOH A2002 4.004 -20.865 -5.279 1.00 65.76 O ANISOU 2212 O HOH A2002 7887 5844 11253 -443 244 -2871 O HETATM 2213 O HOH A2003 -5.981 -22.869 -10.508 1.00 44.22 O ANISOU 2213 O HOH A2003 5696 5020 6084 438 -1007 720 O HETATM 2214 O HOH A2004 -6.608 -27.798 -7.430 1.00 53.44 O ANISOU 2214 O HOH A2004 6922 7038 6343 1268 -601 -333 O HETATM 2215 O HOH A2005 -8.229 -22.397 -5.576 1.00 37.44 O ANISOU 2215 O HOH A2005 3655 4822 5746 -553 -220 -731 O HETATM 2216 O HOH A2006 4.432 -26.414 -6.206 1.00 39.38 O ANISOU 2216 O HOH A2006 5345 4913 4703 1395 554 -172 O HETATM 2217 O HOH A2007 3.516 -24.385 -2.908 1.00 57.29 O ANISOU 2217 O HOH A2007 10269 4010 7488 3582 -978 -2300 O HETATM 2218 O HOH A2008 -3.853 -21.789 -11.191 1.00 27.38 O ANISOU 2218 O HOH A2008 3513 3410 3477 626 -340 -411 O HETATM 2219 O HOH A2009 -5.044 -25.139 -8.109 1.00 41.01 O ANISOU 2219 O HOH A2009 4495 4681 6403 -211 -389 46 O HETATM 2220 O HOH A2010 -1.541 -17.084 -7.915 1.00 25.23 O ANISOU 2220 O HOH A2010 2822 3613 3149 -803 774 -586 O HETATM 2221 O HOH A2011 -6.635 -22.165 -7.600 1.00 42.80 O ANISOU 2221 O HOH A2011 4614 4945 6701 -1114 643 -1659 O HETATM 2222 O HOH A2012 3.176 -30.767 -5.454 1.00 46.08 O ANISOU 2222 O HOH A2012 7256 4246 6005 4148 2192 -1297 O HETATM 2223 O HOH A2013 -2.928 -35.808 0.417 1.00 39.30 O ANISOU 2223 O HOH A2013 5999 4015 4915 604 -257 741 O HETATM 2224 O HOH A2014 -1.395 -22.148 -4.895 1.00 31.81 O ANISOU 2224 O HOH A2014 4919 3258 3908 1405 -885 -805 O HETATM 2225 O HOH A2015 -0.374 -23.479 -2.646 1.00 26.54 O ANISOU 2225 O HOH A2015 3071 3358 3652 330 -275 -103 O HETATM 2226 O HOH A2016 2.558 -26.394 -3.716 1.00 38.33 O ANISOU 2226 O HOH A2016 3864 5826 4870 431 567 834 O HETATM 2227 O HOH A2017 4.197 -31.681 9.809 1.00 38.01 O ANISOU 2227 O HOH A2017 3776 4782 5882 -45 -241 585 O HETATM 2228 O HOH A2018 -4.301 -24.366 -5.270 1.00 23.10 O ANISOU 2228 O HOH A2018 3457 2340 2980 117 199 -932 O HETATM 2229 O HOH A2019 -0.643 -30.837 -4.203 1.00 57.56 O ANISOU 2229 O HOH A2019 7451 4057 10360 -402 1260 -2226 O HETATM 2230 O HOH A2020 2.920 -28.901 -3.208 1.00 39.89 O ANISOU 2230 O HOH A2020 4153 4673 6329 670 1810 1052 O HETATM 2231 O HOH A2021 1.910 -30.470 -1.170 1.00 43.76 O ANISOU 2231 O HOH A2021 4945 5180 6502 3396 2287 -1693 O HETATM 2232 O HOH A2022 0.184 -27.543 3.971 1.00 23.62 O ANISOU 2232 O HOH A2022 2819 2949 3206 204 -316 -168 O HETATM 2233 O HOH A2023 6.567 -28.058 4.126 1.00 41.51 O ANISOU 2233 O HOH A2023 3693 3421 8655 -226 -1164 -881 O HETATM 2234 O HOH A2024 6.879 -25.568 3.296 1.00 23.45 O ANISOU 2234 O HOH A2024 3162 2583 3165 594 1250 -262 O HETATM 2235 O HOH A2025 -8.385 -32.462 21.171 1.00 31.84 O ANISOU 2235 O HOH A2025 3571 4653 3874 -749 -403 689 O HETATM 2236 O HOH A2026 -5.715 -34.651 -0.497 1.00 33.13 O ANISOU 2236 O HOH A2026 4992 3926 3666 -864 753 420 O HETATM 2237 O HOH A2027 -7.287 -32.375 -0.279 1.00 37.94 O ANISOU 2237 O HOH A2027 5489 5415 3508 447 1317 851 O HETATM 2238 O HOH A2028 -5.331 -31.637 -4.700 1.00 57.16 O ANISOU 2238 O HOH A2028 7597 8506 5615 -1291 368 -997 O HETATM 2239 O HOH A2029 -1.382 -34.974 -3.740 1.00 41.02 O ANISOU 2239 O HOH A2029 4843 5802 4938 329 819 -474 O HETATM 2240 O HOH A2030 4.359 -28.997 6.262 1.00 37.85 O ANISOU 2240 O HOH A2030 2895 6109 5376 445 -132 -1083 O HETATM 2241 O HOH A2031 14.820 -17.132 12.443 1.00 42.09 O ANISOU 2241 O HOH A2031 6404 6708 2878 2210 -674 -251 O HETATM 2242 O HOH A2032 2.869 -34.286 4.455 1.00 35.17 O ANISOU 2242 O HOH A2032 3601 4934 4827 1286 644 2361 O HETATM 2243 O HOH A2033 2.875 -32.425 7.887 1.00 38.29 O ANISOU 2243 O HOH A2033 3476 4680 6390 99 -742 955 O HETATM 2244 O HOH A2034 -1.130 -35.270 1.882 1.00 42.84 O ANISOU 2244 O HOH A2034 5297 5042 5937 1139 622 -82 O HETATM 2245 O HOH A2035 0.128 -35.504 13.192 1.00 23.07 O ANISOU 2245 O HOH A2035 3095 2698 2972 315 -256 -144 O HETATM 2246 O HOH A2036 -1.042 -42.375 14.385 1.00 43.06 O ANISOU 2246 O HOH A2036 5533 6135 4691 1546 -545 246 O HETATM 2247 O HOH A2037 -1.556 -42.430 12.390 1.00 31.66 O ANISOU 2247 O HOH A2037 3264 2224 6540 -581 1158 727 O HETATM 2248 O HOH A2038 -4.332 -4.317 -7.645 1.00 73.03 O ANISOU 2248 O HOH A2038 12873 7202 7671 3573 6973 5884 O HETATM 2249 O HOH A2039 -0.963 -5.043 -10.382 1.00 47.17 O ANISOU 2249 O HOH A2039 4268 6741 6912 209 719 3296 O HETATM 2250 O HOH A2040 -3.684 -5.083 -13.097 1.00 53.39 O ANISOU 2250 O HOH A2040 6327 4960 8999 241 -533 -1873 O HETATM 2251 O HOH A2041 -0.534 -9.253 -16.194 1.00 41.39 O ANISOU 2251 O HOH A2041 3837 5986 5903 -187 79 -677 O HETATM 2252 O HOH A2042 1.725 -13.121 -14.345 1.00 63.12 O ANISOU 2252 O HOH A2042 7984 10589 5410 2667 53 -1042 O HETATM 2253 O HOH A2043 2.106 -9.357 -12.404 1.00 28.28 O ANISOU 2253 O HOH A2043 2369 4904 3469 47 -113 515 O HETATM 2254 O HOH A2044 1.875 -8.600 -14.966 1.00 40.92 O ANISOU 2254 O HOH A2044 5218 7185 3145 -1267 172 617 O HETATM 2255 O HOH A2045 -0.134 -34.923 17.455 1.00 32.02 O ANISOU 2255 O HOH A2045 5351 3800 3014 -365 -1631 604 O HETATM 2256 O HOH A2046 -3.336 -36.751 18.675 1.00 33.25 O ANISOU 2256 O HOH A2046 4315 5368 2948 -638 -1486 -366 O HETATM 2257 O HOH A2047 1.221 -37.235 18.577 1.00 37.60 O ANISOU 2257 O HOH A2047 6026 3007 5254 -663 -2361 1154 O HETATM 2258 O HOH A2048 -10.064 -16.220 -10.796 1.00 47.74 O ANISOU 2258 O HOH A2048 5525 4715 7897 1426 -1372 1022 O HETATM 2259 O HOH A2049 -17.322 -19.969 -2.600 1.00 26.21 O ANISOU 2259 O HOH A2049 2811 3313 3834 438 -241 101 O HETATM 2260 O HOH A2050 -14.659 -23.154 -0.679 1.00 42.09 O ANISOU 2260 O HOH A2050 3950 4867 7174 321 355 2107 O HETATM 2261 O HOH A2051 -13.267 -25.277 0.436 1.00 28.54 O ANISOU 2261 O HOH A2051 3895 3049 3900 -100 1111 19 O HETATM 2262 O HOH A2052 -10.067 -26.694 -1.592 1.00 31.48 O ANISOU 2262 O HOH A2052 4083 3520 4357 466 -517 -758 O HETATM 2263 O HOH A2053 -9.283 -19.790 -5.080 1.00 29.76 O ANISOU 2263 O HOH A2053 3942 3627 3736 804 -74 -571 O HETATM 2264 O HOH A2054 -6.394 -33.922 15.129 1.00 16.20 O ANISOU 2264 O HOH A2054 1961 2295 1897 107 -469 288 O HETATM 2265 O HOH A2055 -6.604 -33.410 19.252 1.00 33.17 O ANISOU 2265 O HOH A2055 3656 4488 4457 -826 -418 922 O HETATM 2266 O HOH A2056 -13.990 -27.847 0.206 1.00 32.13 O ANISOU 2266 O HOH A2056 5450 3312 3446 824 -385 1166 O HETATM 2267 O HOH A2057 -10.630 -30.765 0.652 1.00 33.43 O ANISOU 2267 O HOH A2057 5301 3548 3852 638 1640 261 O HETATM 2268 O HOH A2058 -0.156 -32.311 17.983 1.00 37.16 O ANISOU 2268 O HOH A2058 3018 6422 4676 521 -466 -178 O HETATM 2269 O HOH A2059 0.211 -29.817 20.832 1.00 48.26 O ANISOU 2269 O HOH A2059 5284 6655 6396 242 802 1088 O HETATM 2270 O HOH A2060 -1.742 -30.893 24.256 1.00 32.39 O ANISOU 2270 O HOH A2060 3990 4058 4257 -782 -1459 163 O HETATM 2271 O HOH A2061 -12.161 -28.184 -2.051 1.00 36.70 O ANISOU 2271 O HOH A2061 5236 4595 4112 -332 13 -117 O HETATM 2272 O HOH A2062 -17.042 -21.680 -0.543 1.00 35.91 O ANISOU 2272 O HOH A2062 4473 4795 4375 2352 2199 659 O HETATM 2273 O HOH A2063 6.421 -21.323 8.028 1.00 17.63 O ANISOU 2273 O HOH A2063 2136 2712 1849 -275 240 -499 O HETATM 2274 O HOH A2064 11.574 -17.895 12.254 1.00 24.16 O ANISOU 2274 O HOH A2064 2660 3546 2971 266 -984 -404 O HETATM 2275 O HOH A2065 8.474 -19.125 14.219 1.00 25.36 O ANISOU 2275 O HOH A2065 2139 5033 2461 -23 -97 -10 O HETATM 2276 O HOH A2066 -10.776 -3.229 4.599 1.00 30.75 O ANISOU 2276 O HOH A2066 4325 2901 4454 -682 1148 -240 O HETATM 2277 O HOH A2067 8.257 -14.446 6.926 1.00 33.12 O ANISOU 2277 O HOH A2067 4138 3055 5390 -371 -2583 856 O HETATM 2278 O HOH A2068 8.064 -13.711 9.268 1.00 47.24 O ANISOU 2278 O HOH A2068 5880 4098 7972 513 2120 1894 O HETATM 2279 O HOH A2069 10.026 -19.279 6.393 1.00 26.06 O ANISOU 2279 O HOH A2069 1740 3453 4706 101 339 263 O HETATM 2280 O HOH A2070 12.518 -19.222 10.174 1.00 25.58 O ANISOU 2280 O HOH A2070 2296 3820 3602 184 -73 -683 O HETATM 2281 O HOH A2071 8.159 -13.726 12.164 1.00 69.32 O ANISOU 2281 O HOH A2071 3784 8081 14472 -914 -2454 -528 O HETATM 2282 O HOH A2072 -21.638 -25.251 12.203 1.00 27.18 O ANISOU 2282 O HOH A2072 3050 3099 4175 -72 320 188 O HETATM 2283 O HOH A2073 12.023 -14.874 9.429 1.00 32.70 O ANISOU 2283 O HOH A2073 3634 4659 4129 -711 -211 -639 O HETATM 2284 O HOH A2074 -21.672 -25.838 14.753 1.00 34.82 O ANISOU 2284 O HOH A2074 3951 4892 4386 492 89 1027 O HETATM 2285 O HOH A2075 -24.660 -25.976 11.156 1.00 36.24 O ANISOU 2285 O HOH A2075 5548 4872 3349 232 -934 741 O HETATM 2286 O HOH A2076 -22.269 -20.480 13.978 1.00 34.95 O ANISOU 2286 O HOH A2076 4064 6569 2645 -1559 1017 -331 O HETATM 2287 O HOH A2077 -21.597 -18.192 13.802 1.00 37.07 O ANISOU 2287 O HOH A2077 5612 4750 3723 -4 -307 -839 O HETATM 2288 O HOH A2078 -19.838 -14.064 13.834 1.00 42.93 O ANISOU 2288 O HOH A2078 5569 5753 4990 -548 972 -1512 O HETATM 2289 O HOH A2079 -1.956 -5.797 -8.053 1.00 32.10 O ANISOU 2289 O HOH A2079 4138 3285 4772 218 -555 -213 O HETATM 2290 O HOH A2080 -19.155 -21.593 17.260 1.00 30.84 O ANISOU 2290 O HOH A2080 2988 4813 3913 -60 945 -456 O HETATM 2291 O HOH A2081 -18.464 -9.579 11.519 1.00 49.25 O ANISOU 2291 O HOH A2081 6065 4481 8168 -863 2994 -2299 O HETATM 2292 O HOH A2082 -0.441 -13.122 -9.912 1.00 11.61 O ANISOU 2292 O HOH A2082 1583 1361 1465 208 -256 -283 O HETATM 2293 O HOH A2083 -7.165 -10.388 -11.109 1.00 42.06 O ANISOU 2293 O HOH A2083 4441 5490 6049 684 -523 100 O HETATM 2294 O HOH A2084 -1.283 -6.973 -13.545 1.00 37.17 O ANISOU 2294 O HOH A2084 4603 4081 5438 -1623 -873 1456 O HETATM 2295 O HOH A2085 -3.739 -7.218 -13.960 1.00 29.20 O ANISOU 2295 O HOH A2085 3441 3142 4511 -112 -292 330 O HETATM 2296 O HOH A2086 0.492 -11.696 -12.272 1.00 26.12 O ANISOU 2296 O HOH A2086 2753 3789 3382 262 -187 358 O HETATM 2297 O HOH A2087 -2.948 -14.815 -8.747 1.00 23.59 O ANISOU 2297 O HOH A2087 2667 3519 2774 242 111 -598 O HETATM 2298 O HOH A2088 -9.168 -10.359 -8.082 1.00 44.34 O ANISOU 2298 O HOH A2088 4807 7761 4278 -71 -1379 4456 O HETATM 2299 O HOH A2089 -0.361 -7.135 8.542 1.00 27.02 O ANISOU 2299 O HOH A2089 3978 2800 3487 37 145 -628 O HETATM 2300 O HOH A2090 -7.337 -14.959 -9.421 1.00 32.23 O ANISOU 2300 O HOH A2090 4216 5502 2526 1550 -230 -228 O HETATM 2301 O HOH A2091 -11.971 -12.234 -8.505 1.00 36.41 O ANISOU 2301 O HOH A2091 2819 5590 5424 1595 -1704 -1951 O HETATM 2302 O HOH A2092 -9.687 -12.308 -11.598 1.00 44.91 O ANISOU 2302 O HOH A2092 4987 6966 5109 1896 1346 485 O HETATM 2303 O HOH A2093 -14.498 -19.030 -2.656 1.00 29.28 O ANISOU 2303 O HOH A2093 2751 2073 6299 324 542 109 O HETATM 2304 O HOH A2094 -13.268 -15.139 -6.521 1.00 34.70 O ANISOU 2304 O HOH A2094 5735 3345 4101 559 2226 -567 O HETATM 2305 O HOH A2095 3.835 -9.174 8.355 1.00 28.74 O ANISOU 2305 O HOH A2095 2811 4019 4090 -1057 -476 -65 O HETATM 2306 O HOH A2096 6.738 -11.057 5.910 1.00 37.41 O ANISOU 2306 O HOH A2096 6146 3155 4912 -692 -486 -863 O HETATM 2307 O HOH A2097 5.539 -10.008 10.269 1.00 37.88 O ANISOU 2307 O HOH A2097 4435 5901 4055 -1397 -1564 1085 O HETATM 2308 O HOH A2098 9.309 -10.578 4.633 1.00 37.74 O ANISOU 2308 O HOH A2098 4253 4292 5793 630 -865 -1421 O HETATM 2309 O HOH A2099 -11.602 -22.091 -1.463 1.00 42.58 O ANISOU 2309 O HOH A2099 5692 6632 3852 -312 1740 2535 O HETATM 2310 O HOH A2100 -10.931 -24.390 -0.284 1.00 22.19 O ANISOU 2310 O HOH A2100 3043 3092 2296 0 -772 -54 O HETATM 2311 O HOH A2101 -9.601 -19.572 -2.181 1.00 14.84 O ANISOU 2311 O HOH A2101 2409 1588 1640 -306 -345 15 O HETATM 2312 O HOH A2102 -6.185 -26.442 -2.611 1.00 71.35 O ANISOU 2312 O HOH A2102 7676 6552 12881 728 -2310 -923 O HETATM 2313 O HOH A2103 -12.582 -26.729 2.726 1.00 46.15 O ANISOU 2313 O HOH A2103 4437 5868 7228 268 397 1824 O HETATM 2314 O HOH A2104 -8.780 -28.212 0.515 1.00 27.24 O ANISOU 2314 O HOH A2104 4733 2773 2842 708 146 -379 O HETATM 2315 O HOH A2105 -3.504 -6.004 11.108 1.00 37.21 O ANISOU 2315 O HOH A2105 5581 4039 4518 -579 51 -1165 O HETATM 2316 O HOH A2106 8.842 -4.539 14.166 1.00 48.11 O ANISOU 2316 O HOH A2106 7248 5488 5544 640 -1235 -3693 O HETATM 2317 O HOH A2107 -12.590 -37.590 6.670 1.00 25.75 O ANISOU 2317 O HOH A2107 3583 2091 4108 649 -1005 -471 O HETATM 2318 O HOH A2108 -10.494 -37.615 10.591 1.00 19.27 O ANISOU 2318 O HOH A2108 3320 1610 2391 -221 259 44 O HETATM 2319 O HOH A2109 -6.517 -8.816 20.160 1.00 52.25 O ANISOU 2319 O HOH A2109 5858 5583 8411 -909 -42 -1491 O HETATM 2320 O HOH A2110 -8.433 -9.530 18.852 1.00 45.49 O ANISOU 2320 O HOH A2110 5750 4819 6714 -168 881 -979 O HETATM 2321 O HOH A2111 -7.400 -6.668 14.158 1.00 38.44 O ANISOU 2321 O HOH A2111 5256 4121 5228 -1270 -485 -1032 O HETATM 2322 O HOH A2112 -9.087 -33.338 1.452 1.00 20.12 O ANISOU 2322 O HOH A2112 3394 2285 1965 -67 72 75 O HETATM 2323 O HOH A2113 -21.317 -22.668 15.997 1.00 51.71 O ANISOU 2323 O HOH A2113 4961 7581 7105 -780 161 -1092 O HETATM 2324 O HOH A2114 -15.048 -29.742 20.399 1.00 85.94 O ANISOU 2324 O HOH A2114 10166 13727 8760 754 -1099 1157 O HETATM 2325 O HOH A2115 -15.216 -35.872 4.961 1.00 22.68 O ANISOU 2325 O HOH A2115 3143 1908 3565 -264 -546 36 O HETATM 2326 O HOH A2116 -11.481 -37.924 -3.435 1.00 41.62 O ANISOU 2326 O HOH A2116 6633 5212 3970 1298 -1500 -3088 O HETATM 2327 O HOH A2117 -11.398 -30.752 -1.840 1.00 36.06 O ANISOU 2327 O HOH A2117 5197 3024 5477 -39 -596 -30 O HETATM 2328 O HOH A2118 -7.041 -30.144 -3.459 1.00 59.41 O ANISOU 2328 O HOH A2118 8275 6147 8149 555 -656 1398 O HETATM 2329 O HOH A2119 -17.634 -33.538 3.331 1.00 26.53 O ANISOU 2329 O HOH A2119 2945 4064 3071 -704 -1014 1089 O HETATM 2330 O HOH A2120 -13.094 -29.680 1.781 1.00 22.45 O ANISOU 2330 O HOH A2120 3283 2696 2551 37 -565 621 O HETATM 2331 O HOH A2121 -8.433 -19.423 -9.360 1.00 37.93 O ANISOU 2331 O HOH A2121 6165 4305 3942 -1445 -113 -1821 O HETATM 2332 O HOH A2122 -11.368 -16.925 -7.566 1.00 51.13 O ANISOU 2332 O HOH A2122 7357 3846 8222 287 -4534 -4048 O HETATM 2333 O HOH A2123 12.473 -15.794 6.653 1.00 31.93 O ANISOU 2333 O HOH A2123 4603 3409 4118 335 48 -406 O HETATM 2334 O HOH A2124 -14.079 -26.660 14.049 1.00 14.47 O ANISOU 2334 O HOH A2124 1743 2128 1624 -130 354 21 O HETATM 2335 O HOH A2125 -15.651 -19.722 1.772 1.00 26.33 O ANISOU 2335 O HOH A2125 2924 2711 4369 511 -927 233 O HETATM 2336 O HOH A2126 -16.694 -11.940 0.163 1.00 13.94 O ANISOU 2336 O HOH A2126 1444 1731 2120 -143 -342 21 O HETATM 2337 O HOH A2127 -10.140 -5.968 -4.703 1.00 34.75 O ANISOU 2337 O HOH A2127 3498 4581 5121 1099 -168 664 O HETATM 2338 O HOH A2128 -8.731 -6.292 -0.836 1.00 24.13 O ANISOU 2338 O HOH A2128 2629 2620 3918 -21 -732 -874 O HETATM 2339 O HOH A2129 -12.722 -5.256 -2.717 1.00 27.87 O ANISOU 2339 O HOH A2129 4526 2868 3194 -275 -160 49 O HETATM 2340 O HOH A2130 -15.570 -5.516 2.314 1.00 62.63 O ANISOU 2340 O HOH A2130 6837 8263 8696 813 -1336 1479 O HETATM 2341 O HOH A2131 -17.142 -6.930 0.303 1.00 38.56 O ANISOU 2341 O HOH A2131 3167 4381 7099 -283 204 -2572 O HETATM 2342 O HOH A2132 -12.982 -4.769 4.342 1.00 34.64 O ANISOU 2342 O HOH A2132 4714 3924 4524 222 919 -953 O HETATM 2343 O HOH A2133 -11.014 -2.340 -0.301 1.00 35.08 O ANISOU 2343 O HOH A2133 5631 2734 4963 -94 -63 -533 O HETATM 2344 O HOH A2134 -19.985 -8.577 4.828 1.00 38.52 O ANISOU 2344 O HOH A2134 3766 4460 6408 942 -799 -387 O HETATM 2345 O HOH A2135 -15.719 -7.944 6.218 1.00 26.54 O ANISOU 2345 O HOH A2135 2756 3344 3981 686 -67 -504 O HETATM 2346 O HOH A2136 -13.303 -9.347 6.802 1.00 17.66 O ANISOU 2346 O HOH A2136 2112 2061 2535 243 459 -492 O HETATM 2347 O HOH A2137 -18.028 -20.360 3.500 1.00 15.95 O ANISOU 2347 O HOH A2137 2090 1917 2052 -113 327 -159 O HETATM 2348 O HOH A2138 -20.027 -26.967 10.693 1.00 26.10 O ANISOU 2348 O HOH A2138 2609 2930 4377 -326 759 262 O HETATM 2349 O HOH A2139 -21.775 -27.536 8.942 1.00 33.51 O ANISOU 2349 O HOH A2139 3203 4762 4764 -114 233 -143 O HETATM 2350 O HOH A2140 -23.173 -29.976 9.751 1.00 65.29 O ANISOU 2350 O HOH A2140 6095 7358 11352 -2322 42 -1332 O HETATM 2351 O HOH A2141 -20.211 -28.747 12.732 1.00 36.70 O ANISOU 2351 O HOH A2141 4005 4680 5257 110 1088 1699 O HETATM 2352 O HOH A2142 -19.386 -31.291 15.756 1.00 33.78 O ANISOU 2352 O HOH A2142 3942 4190 4703 -1146 327 -555 O HETATM 2353 O HOH A2143 -20.550 -34.393 15.469 1.00 47.98 O ANISOU 2353 O HOH A2143 3359 5882 8988 2207 -161 -1264 O HETATM 2354 O HOH A2144 -22.712 -37.408 6.746 1.00 37.93 O ANISOU 2354 O HOH A2144 4590 4519 5301 712 1573 1364 O HETATM 2355 O HOH A2145 -25.730 -28.739 2.475 1.00 23.45 O ANISOU 2355 O HOH A2145 2973 2627 3310 -106 204 -363 O HETATM 2356 O HOH A2146 -25.214 -32.146 6.039 1.00 25.24 O ANISOU 2356 O HOH A2146 2920 2858 3810 -91 -270 228 O HETATM 2357 O HOH A2147 -24.137 -26.753 8.349 1.00 30.19 O ANISOU 2357 O HOH A2147 4015 2534 4922 -1 1001 86 O HETATM 2358 O HOH A2148 -20.042 -27.702 -0.857 1.00 66.60 O ANISOU 2358 O HOH A2148 6183 12573 6546 1036 414 -891 O HETATM 2359 O HOH A2149 -18.989 -21.878 1.108 1.00 31.39 O ANISOU 2359 O HOH A2149 4322 3404 4199 -655 -1299 -483 O HETATM 2360 O HOH A2150 -18.503 -26.202 -1.574 1.00 34.09 O ANISOU 2360 O HOH A2150 4332 4951 3669 545 -22 -1421 O HETATM 2361 O HOH A2151 -22.318 -22.598 12.024 1.00 19.00 O ANISOU 2361 O HOH A2151 2443 2499 2277 -35 606 353 O HETATM 2362 O HOH A2152 -21.325 -15.696 11.982 1.00 28.09 O ANISOU 2362 O HOH A2152 3121 4091 3459 -430 645 -863 O HETATM 2363 O HOH A2153 -23.200 -13.763 11.787 1.00 45.30 O ANISOU 2363 O HOH A2153 3906 6102 7202 -39 -402 -1228 O HETATM 2364 O HOH A2154 -26.666 -12.868 7.028 1.00 25.55 O ANISOU 2364 O HOH A2154 2791 3200 3715 -346 628 -250 O HETATM 2365 O HOH A2155 -19.839 -13.489 8.511 1.00 21.75 O ANISOU 2365 O HOH A2155 2459 2216 3587 -214 149 80 O HETATM 2366 O HOH A2156 -19.796 -18.286 -0.078 1.00 31.39 O ANISOU 2366 O HOH A2156 2593 4550 4783 1391 -1353 -1604 O HETATM 2367 O HOH A2157 -15.897 -18.159 16.913 1.00 24.45 O ANISOU 2367 O HOH A2157 3133 3478 2676 1164 106 -187 O HETATM 2368 O HOH A2158 -17.013 -21.042 15.584 1.00 16.89 O ANISOU 2368 O HOH A2158 1912 2451 2053 91 5 -192 O HETATM 2369 O HOH A2159 -19.106 -11.771 10.869 1.00 84.46 O ANISOU 2369 O HOH A2159 10744 10093 11254 -1963 610 -2859 O HETATM 2370 O HOH A2160 -17.977 -12.734 12.421 1.00 28.47 O ANISOU 2370 O HOH A2160 4062 2900 3852 459 1234 -983 O HETATM 2371 O HOH A2161 -14.407 -9.339 13.514 1.00 84.76 O ANISOU 2371 O HOH A2161 10878 10781 10545 -1697 -1497 -535 O HETATM 2372 O HOH A2162 -16.016 -8.121 10.505 1.00 45.68 O ANISOU 2372 O HOH A2162 4057 3082 10215 413 191 -3017 O HETATM 2373 O HOH A2163 -7.652 -5.793 9.702 1.00 32.28 O ANISOU 2373 O HOH A2163 5483 2672 4110 -1343 -61 -70 O HETATM 2374 O HOH A2164 -14.643 -5.554 8.915 1.00 34.20 O ANISOU 2374 O HOH A2164 3593 5025 4375 231 702 -1 O HETATM 2375 O HOH A2165 -13.475 -3.482 10.099 1.00 53.88 O ANISOU 2375 O HOH A2165 6036 3858 10576 -2021 2297 -2665 O HETATM 2376 O HOH A2166 -8.103 -3.892 7.295 1.00 31.21 O ANISOU 2376 O HOH A2166 5808 1627 4422 -1205 3247 -1691 O HETATM 2377 O HOH A2167 -4.133 -3.976 4.605 1.00 36.63 O ANISOU 2377 O HOH A2167 5382 3121 5412 77 1787 -300 O HETATM 2378 O HOH A2168 -0.241 -9.176 6.674 1.00 20.30 O ANISOU 2378 O HOH A2168 2215 2761 2737 265 81 125 O HETATM 2379 O HOH A2169 -6.285 -5.943 0.187 1.00 28.29 O ANISOU 2379 O HOH A2169 2625 2888 5234 151 -82 343 O HETATM 2380 O HOH A2170 -0.342 -9.654 2.180 1.00 14.74 O ANISOU 2380 O HOH A2170 1538 1969 2093 380 40 -9 O HETATM 2381 O HOH A2171 -1.858 -5.401 4.710 1.00 40.35 O ANISOU 2381 O HOH A2171 3814 5237 6277 -855 365 -607 O HETATM 2382 O HOH A2172 -4.711 -5.323 -2.367 1.00 20.88 O ANISOU 2382 O HOH A2172 1991 3386 2557 1436 -194 -424 O HETATM 2383 O HOH A2173 0.086 -5.204 -6.288 1.00 35.52 O ANISOU 2383 O HOH A2173 3492 5222 4780 278 -336 1058 O HETATM 2384 O HOH A2174 -1.464 -3.094 -4.371 1.00 54.35 O ANISOU 2384 O HOH A2174 5055 10032 5563 3371 -2131 1056 O HETATM 2385 O HOH A2175 -5.073 -3.973 -5.177 1.00 58.91 O ANISOU 2385 O HOH A2175 7746 3638 10997 -534 -368 -218 O HETATM 2386 O HOH A2176 -10.584 -8.120 -8.008 1.00 39.64 O ANISOU 2386 O HOH A2176 4351 5959 4749 1395 708 1771 O HETATM 2387 O HOH A2177 0.927 -8.496 4.281 1.00 20.27 O ANISOU 2387 O HOH A2177 2196 2885 2618 37 50 -92 O HETATM 2388 O HOH A2178 4.466 -7.323 4.422 1.00 39.48 O ANISOU 2388 O HOH A2178 4604 4469 5925 -64 109 -1195 O HETATM 2389 O HOH A2179 4.999 -8.899 5.924 1.00 30.62 O ANISOU 2389 O HOH A2179 3568 4668 3399 -292 -562 -815 O HETATM 2390 O HOH A2180 6.521 -13.762 4.925 1.00 21.87 O ANISOU 2390 O HOH A2180 1697 2618 3994 110 -308 80 O HETATM 2391 O HOH A2181 1.638 -10.712 7.949 1.00 16.49 O ANISOU 2391 O HOH A2181 2117 1927 2220 -14 38 -482 O HETATM 2392 O HOH A2182 2.213 -13.827 12.488 1.00 25.59 O ANISOU 2392 O HOH A2182 3226 4356 2137 -92 8 -693 O HETATM 2393 O HOH A2183 5.143 -11.768 11.939 1.00 31.46 O ANISOU 2393 O HOH A2183 4274 3837 3840 -38 -835 -617 O HETATM 2394 O HOH A2184 6.130 -16.796 13.744 1.00 23.89 O ANISOU 2394 O HOH A2184 2905 2965 3204 140 528 -116 O HETATM 2395 O HOH A2185 -8.237 -20.508 21.598 1.00 33.17 O ANISOU 2395 O HOH A2185 3789 4789 4023 -148 201 119 O HETATM 2396 O HOH A2186 -6.527 -24.892 25.814 1.00 28.37 O ANISOU 2396 O HOH A2186 2559 5775 2443 -515 -60 -19 O HETATM 2397 O HOH A2187 -11.451 -29.335 22.554 1.00 33.33 O ANISOU 2397 O HOH A2187 3666 5441 3557 -338 -51 -347 O HETATM 2398 O HOH A2188 -8.859 -30.630 22.602 1.00 39.56 O ANISOU 2398 O HOH A2188 3578 5370 6081 927 1 877 O HETATM 2399 O HOH A2189 -10.076 -29.727 26.752 1.00 49.76 O ANISOU 2399 O HOH A2189 5247 5880 7777 -1042 1006 -1818 O HETATM 2400 O HOH A2190 -5.982 -28.879 28.792 1.00 44.12 O ANISOU 2400 O HOH A2190 5104 5261 6398 434 1306 1222 O HETATM 2401 O HOH A2191 -7.717 -24.723 28.470 1.00 45.10 O ANISOU 2401 O HOH A2191 4651 7273 5211 -147 -675 -540 O HETATM 2402 O HOH A2192 -5.007 -20.509 24.392 1.00 46.41 O ANISOU 2402 O HOH A2192 3768 10971 2895 -147 -341 -1841 O HETATM 2403 O HOH A2193 -3.854 -8.980 12.327 1.00 42.87 O ANISOU 2403 O HOH A2193 5375 2689 8223 -2415 -536 -2562 O HETATM 2404 O HOH A2194 -1.776 -7.422 10.857 1.00 38.99 O ANISOU 2404 O HOH A2194 6761 3966 4088 -409 79 -989 O HETATM 2405 O HOH A2195 1.391 -6.740 12.403 1.00 42.49 O ANISOU 2405 O HOH A2195 6421 4326 5395 315 -2155 -195 O HETATM 2406 O HOH A2196 6.347 -11.299 17.390 1.00 32.91 O ANISOU 2406 O HOH A2196 4140 4267 4098 -886 -1712 -1316 O HETATM 2407 O HOH A2197 7.261 -9.337 17.129 1.00 98.28 O ANISOU 2407 O HOH A2197 6699 13457 17185 -2607 -7548 -5060 O HETATM 2408 O HOH A2198 7.596 -5.697 16.154 1.00 43.04 O ANISOU 2408 O HOH A2198 5260 3166 7928 -239 -269 203 O HETATM 2409 O HOH A2199 -4.859 -7.296 17.687 1.00 31.78 O ANISOU 2409 O HOH A2199 4205 3028 4840 -469 -152 -2097 O HETATM 2410 O HOH A2200 -3.870 -14.342 20.819 1.00 71.32 O ANISOU 2410 O HOH A2200 6322 10690 10083 1003 80 -2563 O HETATM 2411 O HOH A2201 -9.398 -12.034 18.317 1.00 28.75 O ANISOU 2411 O HOH A2201 3187 3904 3833 -85 410 -752 O HETATM 2412 O HOH A2202 -12.024 -11.014 14.897 1.00 34.87 O ANISOU 2412 O HOH A2202 2963 3336 6948 113 -28 -224 O HETATM 2413 O HOH A2203 -9.159 -8.527 15.544 1.00 38.46 O ANISOU 2413 O HOH A2203 5054 4269 5289 985 171 -1782 O HETATM 2414 O HOH A2204 -12.246 -12.971 17.490 1.00 30.53 O ANISOU 2414 O HOH A2204 4339 2906 4352 1578 2161 -650 O HETATM 2415 O HOH A2205 -14.978 -14.327 17.088 1.00 49.18 O ANISOU 2415 O HOH A2205 8068 3305 7313 346 3668 -359 O HETATM 2416 O HOH A2206 -19.099 -24.432 21.787 1.00 59.15 O ANISOU 2416 O HOH A2206 5992 10147 6334 1179 508 -803 O HETATM 2417 O HOH A2207 -18.998 -24.069 18.380 1.00 30.64 O ANISOU 2417 O HOH A2207 2411 5071 4157 694 1513 190 O HETATM 2418 O HOH A2208 -12.018 -27.873 15.362 1.00 16.06 O ANISOU 2418 O HOH A2208 2052 2330 1718 -31 21 -203 O HETATM 2419 O HOH A2209 -17.056 -30.057 18.770 1.00 41.07 O ANISOU 2419 O HOH A2209 4792 5878 4931 2716 954 728 O HETATM 2420 O HOH A2210 -12.332 -30.178 20.171 1.00 24.06 O ANISOU 2420 O HOH A2210 2911 3944 2284 159 -47 -337 O HETATM 2421 O HOH A2211 -11.124 -32.996 20.081 1.00 28.43 O ANISOU 2421 O HOH A2211 3693 5430 1678 -305 239 249 O HETATM 2422 O HOH A2212 -7.134 -37.150 13.403 1.00 22.51 O ANISOU 2422 O HOH A2212 3016 2431 3103 596 -203 286 O HETATM 2423 O HOH A2213 -15.669 -36.924 16.601 1.00 24.35 O ANISOU 2423 O HOH A2213 3137 2696 3417 695 444 685 O HETATM 2424 O HOH A2214 -17.877 -35.728 18.159 1.00 67.44 O ANISOU 2424 O HOH A2214 8795 6489 10339 -1101 300 -583 O HETATM 2425 O HOH A2215 -13.223 -37.650 11.018 1.00 24.61 O ANISOU 2425 O HOH A2215 3572 2405 3373 153 298 114 O HETATM 2426 O HOH A2216 -15.916 -39.093 7.808 1.00 59.54 O ANISOU 2426 O HOH A2216 7402 5878 9340 -344 1899 -507 O HETATM 2427 O HOH A2217 -4.213 -37.382 6.525 1.00 32.70 O ANISOU 2427 O HOH A2217 5925 2132 4367 534 1348 -629 O HETATM 2428 O HOH A2218 -1.176 -42.255 8.521 1.00 36.46 O ANISOU 2428 O HOH A2218 3380 5100 5371 1389 1803 -386 O HETATM 2429 O HOH A2219 -8.794 -17.753 -6.921 1.00 28.05 O ANISOU 2429 O HOH A2219 3093 3570 3993 -214 -276 -415 O HETATM 2430 O HOH A2220 1.317 -21.110 -5.389 1.00 25.43 O ANISOU 2430 O HOH A2220 3131 2812 3718 679 -120 -1079 O HETATM 2431 O HOH A2221 2.126 -21.797 -3.354 1.00 24.79 O ANISOU 2431 O HOH A2221 3843 2649 2926 405 -886 -704 O HETATM 2432 O HOH A2222 7.334 -17.138 -1.388 1.00 20.46 O ANISOU 2432 O HOH A2222 1931 3049 2793 -149 195 344 O HETATM 2433 O HOH A2223 4.111 -20.047 -7.701 1.00 33.24 O ANISOU 2433 O HOH A2223 5856 1244 5529 -408 -836 -252 O HETATM 2434 O HOH A2224 5.860 -21.545 -3.474 1.00111.68 O ANISOU 2434 O HOH A2224 8337 25983 8113 10514 6763 6351 O HETATM 2435 O HOH A2225 7.656 -23.281 -0.796 1.00 49.30 O ANISOU 2435 O HOH A2225 6173 4044 8513 -35 1109 -1544 O HETATM 2436 O HOH A2226 8.680 -24.327 1.595 1.00 26.67 O ANISOU 2436 O HOH A2226 3320 2589 4222 -57 1683 -350 O HETATM 2437 O HOH A2227 10.300 -16.583 5.568 1.00 27.85 O ANISOU 2437 O HOH A2227 3309 4399 2871 -1346 882 -726 O HETATM 2438 O HOH A2228 7.926 -14.568 2.667 1.00 23.26 O ANISOU 2438 O HOH A2228 2141 2671 4023 150 163 -394 O HETATM 2439 O HOH A2229 10.868 -23.071 6.674 1.00 51.84 O ANISOU 2439 O HOH A2229 9911 5410 4375 29 -4062 733 O HETATM 2440 O HOH A2230 10.427 -25.808 3.666 1.00 31.96 O ANISOU 2440 O HOH A2230 3553 3566 5022 -574 20 -45 O HETATM 2441 O HOH A2231 14.263 -25.068 7.289 1.00 31.30 O ANISOU 2441 O HOH A2231 4266 4361 3263 -15 1386 584 O HETATM 2442 O HOH A2232 5.611 -29.043 9.372 1.00 26.72 O ANISOU 2442 O HOH A2232 4089 2615 3448 167 1141 -320 O HETATM 2443 O HOH A2233 3.828 -31.725 12.827 1.00 78.76 O ANISOU 2443 O HOH A2233 14545 5515 9862 741 2805 -92 O HETATM 2444 O HOH A2234 6.879 -30.114 14.244 1.00 48.91 O ANISOU 2444 O HOH A2234 6350 4721 7511 601 505 1849 O HETATM 2445 O HOH A2235 5.949 -30.402 17.094 1.00 35.67 O ANISOU 2445 O HOH A2235 5892 2924 4734 -253 383 -798 O HETATM 2446 O HOH B2001 19.265 -9.018 28.645 1.00 37.82 O ANISOU 2446 O HOH B2001 5172 3175 6022 -791 444 -1376 O HETATM 2447 O HOH B2002 22.370 -7.641 28.422 1.00 43.64 O ANISOU 2447 O HOH B2002 5302 4600 6678 -100 -84 395 O HETATM 2448 O HOH B2003 20.268 -7.346 27.211 1.00 33.35 O ANISOU 2448 O HOH B2003 4036 2871 5762 135 872 -584 O HETATM 2449 O HOH B2004 17.836 -6.539 25.116 1.00 68.32 O ANISOU 2449 O HOH B2004 5253 10441 10262 1111 629 -1255 O HETATM 2450 O HOH B2005 -8.651 -15.260 21.265 1.00 52.90 O ANISOU 2450 O HOH B2005 5678 8931 5488 -379 1487 -208 O HETATM 2451 O HOH B2006 6.437 -6.201 29.354 1.00 33.76 O ANISOU 2451 O HOH B2006 5277 3293 4257 -357 -788 737 O HETATM 2452 O HOH B2007 10.313 -10.699 38.903 1.00 83.13 O ANISOU 2452 O HOH B2007 12165 10905 8513 -784 -1276 133 O HETATM 2453 O HOH B2008 12.356 -7.862 15.166 1.00 45.37 O ANISOU 2453 O HOH B2008 6660 4571 6006 -400 -1451 1361 O HETATM 2454 O HOH B2009 -1.749 -15.055 28.746 1.00 57.87 O ANISOU 2454 O HOH B2009 3056 15488 3442 -3258 1485 2722 O HETATM 2455 O HOH B2010 -2.393 -15.918 25.083 1.00 38.52 O ANISOU 2455 O HOH B2010 4315 5639 4681 142 236 -895 O HETATM 2456 O HOH B2011 -6.296 -14.155 22.432 1.00 58.34 O ANISOU 2456 O HOH B2011 3100 10875 8189 665 -894 -1328 O HETATM 2457 O HOH B2012 -0.739 -19.759 33.906 1.00 36.09 O ANISOU 2457 O HOH B2012 4903 5085 3722 558 320 -577 O HETATM 2458 O HOH B2013 -1.389 -17.776 34.058 1.00 29.80 O ANISOU 2458 O HOH B2013 3588 3888 3846 191 273 -1010 O HETATM 2459 O HOH B2014 -3.891 -24.327 32.138 1.00 46.01 O ANISOU 2459 O HOH B2014 6625 5328 5529 1606 4154 1050 O HETATM 2460 O HOH B2015 -4.642 -20.738 33.769 1.00 34.14 O ANISOU 2460 O HOH B2015 4327 5846 2799 -710 567 263 O HETATM 2461 O HOH B2016 8.314 -11.333 19.194 1.00 18.42 O ANISOU 2461 O HOH B2016 2387 2418 2192 -127 73 -154 O HETATM 2462 O HOH B2017 30.939 -22.196 17.946 1.00 52.10 O ANISOU 2462 O HOH B2017 5490 7293 7010 341 1560 2194 O HETATM 2463 O HOH B2018 11.836 -12.973 13.247 1.00 27.75 O ANISOU 2463 O HOH B2018 3548 3692 3303 -35 -639 7 O HETATM 2464 O HOH B2019 9.596 -7.711 16.597 1.00 30.05 O ANISOU 2464 O HOH B2019 5082 3323 3012 -322 -294 -139 O HETATM 2465 O HOH B2020 19.144 -26.439 14.463 1.00 47.56 O ANISOU 2465 O HOH B2020 4905 5684 7481 851 1095 -377 O HETATM 2466 O HOH B2021 21.759 -16.493 31.159 1.00 23.88 O ANISOU 2466 O HOH B2021 2504 3949 2618 -263 -987 477 O HETATM 2467 O HOH B2022 17.778 -17.655 35.283 1.00 66.08 O ANISOU 2467 O HOH B2022 5136 10996 8975 1946 -2419 20 O HETATM 2468 O HOH B2023 16.213 -28.478 15.857 1.00 36.12 O ANISOU 2468 O HOH B2023 5914 3420 4387 1399 1023 340 O HETATM 2469 O HOH B2024 12.016 -12.952 39.338 1.00 73.00 O ANISOU 2469 O HOH B2024 5539 12315 9881 36 664 924 O HETATM 2470 O HOH B2025 -5.270 -18.747 36.975 1.00 34.20 O ANISOU 2470 O HOH B2025 4960 4497 3535 -662 -877 368 O HETATM 2471 O HOH B2026 13.344 -17.159 40.109 1.00 45.52 O ANISOU 2471 O HOH B2026 5251 6871 5173 -2025 -397 -257 O HETATM 2472 O HOH B2027 11.956 -20.965 44.018 1.00 38.66 O ANISOU 2472 O HOH B2027 5189 4843 4654 -1590 -2666 1209 O HETATM 2473 O HOH B2028 6.932 -19.482 43.836 1.00 38.50 O ANISOU 2473 O HOH B2028 5412 5173 4043 -655 431 -1252 O HETATM 2474 O HOH B2029 7.242 -27.120 34.593 1.00 21.04 O ANISOU 2474 O HOH B2029 3418 2004 2572 -228 493 671 O HETATM 2475 O HOH B2030 28.213 -22.139 20.187 1.00 38.61 O ANISOU 2475 O HOH B2030 4659 3939 6071 355 1407 -497 O HETATM 2476 O HOH B2031 25.027 -31.260 25.510 1.00 57.36 O ANISOU 2476 O HOH B2031 7861 5710 8221 1733 -3004 -799 O HETATM 2477 O HOH B2032 20.178 -25.214 35.472 1.00 40.27 O ANISOU 2477 O HOH B2032 4495 6458 4347 -497 -1166 577 O HETATM 2478 O HOH B2033 12.276 -29.606 44.221 1.00 67.35 O ANISOU 2478 O HOH B2033 3943 11478 10167 1977 -1297 5180 O HETATM 2479 O HOH B2034 15.690 -21.977 49.648 1.00 55.10 O ANISOU 2479 O HOH B2034 7084 5078 8773 583 -3072 1715 O HETATM 2480 O HOH B2035 13.393 -28.586 41.605 1.00 48.44 O ANISOU 2480 O HOH B2035 5971 4826 7607 40 684 753 O HETATM 2481 O HOH B2036 19.329 -25.935 43.386 1.00 82.49 O ANISOU 2481 O HOH B2036 6724 16141 8475 -7210 -2597 6982 O HETATM 2482 O HOH B2037 14.290 -32.567 38.302 1.00 46.42 O ANISOU 2482 O HOH B2037 3582 5013 9040 -1979 1568 1294 O HETATM 2483 O HOH B2038 13.756 -34.947 33.097 1.00 58.14 O ANISOU 2483 O HOH B2038 11210 3029 7849 1469 53 881 O HETATM 2484 O HOH B2039 22.326 -32.956 41.283 1.00 70.82 O ANISOU 2484 O HOH B2039 8876 9621 8412 -76 -1179 3388 O HETATM 2485 O HOH B2040 21.617 -32.741 32.932 1.00 77.57 O ANISOU 2485 O HOH B2040 9527 10437 9506 1958 2279 2530 O HETATM 2486 O HOH B2041 11.262 -33.400 29.158 1.00 29.88 O ANISOU 2486 O HOH B2041 3730 3149 4474 1089 536 -74 O HETATM 2487 O HOH B2042 10.827 -32.109 32.450 1.00 24.50 O ANISOU 2487 O HOH B2042 3859 1936 3512 187 415 762 O HETATM 2488 O HOH B2043 19.397 -31.458 21.210 1.00 34.97 O ANISOU 2488 O HOH B2043 5085 2706 5493 397 -613 -157 O HETATM 2489 O HOH B2044 25.548 -26.094 17.796 1.00 36.52 O ANISOU 2489 O HOH B2044 4895 5281 3697 287 534 -1344 O HETATM 2490 O HOH B2045 23.373 -26.647 15.885 1.00 37.09 O ANISOU 2490 O HOH B2045 5542 3426 5124 223 704 -650 O HETATM 2491 O HOH B2046 23.933 -23.284 15.463 1.00 31.42 O ANISOU 2491 O HOH B2046 4207 3517 4214 453 881 538 O HETATM 2492 O HOH B2047 20.764 -27.160 17.288 1.00 34.14 O ANISOU 2492 O HOH B2047 4137 4087 4747 429 928 -38 O HETATM 2493 O HOH B2048 17.924 -21.907 14.179 1.00 27.93 O ANISOU 2493 O HOH B2048 3313 3421 3876 -505 404 13 O HETATM 2494 O HOH B2049 18.230 -19.093 15.644 1.00 30.43 O ANISOU 2494 O HOH B2049 3369 4696 3495 868 -56 204 O HETATM 2495 O HOH B2050 26.692 -21.197 17.955 1.00 28.56 O ANISOU 2495 O HOH B2050 2749 3254 4849 252 501 41 O HETATM 2496 O HOH B2051 21.100 -16.732 16.793 1.00 22.85 O ANISOU 2496 O HOH B2051 2671 2673 3337 -73 783 23 O HETATM 2497 O HOH B2052 22.011 -18.180 10.680 1.00 36.23 O ANISOU 2497 O HOH B2052 3858 5675 4230 1744 1752 53 O HETATM 2498 O HOH B2053 20.208 -17.529 14.810 1.00 38.86 O ANISOU 2498 O HOH B2053 5238 4329 5197 -705 1682 -118 O HETATM 2499 O HOH B2054 20.469 -22.221 13.171 1.00 35.04 O ANISOU 2499 O HOH B2054 3117 5318 4876 12 567 -1102 O HETATM 2500 O HOH B2055 28.174 -18.818 17.615 1.00 33.63 O ANISOU 2500 O HOH B2055 2319 2296 8163 91 1547 1268 O HETATM 2501 O HOH B2056 28.118 -16.364 13.927 1.00 39.55 O ANISOU 2501 O HOH B2056 3866 6021 5139 -1319 384 -1000 O HETATM 2502 O HOH B2057 20.759 -14.672 10.133 1.00 29.70 O ANISOU 2502 O HOH B2057 3143 4330 3809 -905 838 -695 O HETATM 2503 O HOH B2058 19.426 -15.966 12.043 1.00 31.02 O ANISOU 2503 O HOH B2058 3345 4341 4099 16 424 -196 O HETATM 2504 O HOH B2059 14.198 -12.176 14.693 1.00 25.55 O ANISOU 2504 O HOH B2059 3859 2787 3062 35 -70 144 O HETATM 2505 O HOH B2060 15.543 -18.493 14.726 1.00 21.05 O ANISOU 2505 O HOH B2060 2544 2644 2809 -191 238 -527 O HETATM 2506 O HOH B2061 11.120 -19.685 14.916 1.00 27.04 O ANISOU 2506 O HOH B2061 2973 3800 3498 747 -1217 -2059 O HETATM 2507 O HOH B2062 0.207 -34.667 30.274 1.00 47.72 O ANISOU 2507 O HOH B2062 7275 4270 6587 -1073 1293 1071 O HETATM 2508 O HOH B2063 -1.083 -29.392 31.814 1.00 46.03 O ANISOU 2508 O HOH B2063 5571 6365 5554 1296 1144 -1694 O HETATM 2509 O HOH B2064 1.576 -37.765 28.316 1.00 45.02 O ANISOU 2509 O HOH B2064 5844 4586 6673 2069 -1324 -1123 O HETATM 2510 O HOH B2065 3.545 -36.956 26.453 1.00 42.21 O ANISOU 2510 O HOH B2065 5219 4410 6407 -1216 -177 275 O HETATM 2511 O HOH B2066 1.554 -31.875 20.167 1.00 30.47 O ANISOU 2511 O HOH B2066 3325 3572 4678 -542 -382 552 O HETATM 2512 O HOH B2067 17.003 -24.489 14.344 1.00 26.91 O ANISOU 2512 O HOH B2067 3163 3298 3763 -26 428 -77 O HETATM 2513 O HOH B2068 15.459 -25.727 16.251 1.00 25.45 O ANISOU 2513 O HOH B2068 2981 2823 3863 827 591 -3 O HETATM 2514 O HOH B2069 15.730 -24.354 11.878 1.00 26.88 O ANISOU 2514 O HOH B2069 2396 3779 4038 569 982 173 O HETATM 2515 O HOH B2070 12.239 -20.713 6.741 1.00 30.24 O ANISOU 2515 O HOH B2070 1971 5850 3667 984 230 153 O HETATM 2516 O HOH B2071 9.678 -29.276 13.826 1.00 27.74 O ANISOU 2516 O HOH B2071 3882 2712 3946 -468 865 -770 O HETATM 2517 O HOH B2072 12.495 -32.032 17.932 1.00 47.19 O ANISOU 2517 O HOH B2072 7045 5585 5297 704 -522 -1216 O HETATM 2518 O HOH B2073 6.350 -32.969 20.702 1.00 43.10 O ANISOU 2518 O HOH B2073 3934 5961 6478 -1662 1717 -1380 O HETATM 2519 O HOH B2074 11.200 -32.210 20.283 1.00 40.88 O ANISOU 2519 O HOH B2074 7169 3587 4776 104 1224 4 O HETATM 2520 O HOH B2075 17.227 -30.882 19.366 1.00 34.75 O ANISOU 2520 O HOH B2075 5179 2926 5098 1426 500 -49 O HETATM 2521 O HOH B2076 15.653 -32.266 22.064 1.00 55.79 O ANISOU 2521 O HOH B2076 8339 6986 5872 993 1731 1126 O HETATM 2522 O HOH B2077 12.278 -33.087 22.429 1.00 79.96 O ANISOU 2522 O HOH B2077 14504 6046 9830 684 -2106 -284 O HETATM 2523 O HOH B2078 9.863 -34.674 33.457 1.00 33.40 O ANISOU 2523 O HOH B2078 5219 3589 3882 665 1111 1115 O HETATM 2524 O HOH B2079 4.904 -26.208 33.670 1.00 22.33 O ANISOU 2524 O HOH B2079 3367 2133 2982 -607 495 329 O HETATM 2525 O HOH B2080 0.031 -28.883 34.411 1.00 28.00 O ANISOU 2525 O HOH B2080 3517 3388 3731 -1051 561 -542 O HETATM 2526 O HOH B2081 -1.831 -26.841 35.758 1.00 29.04 O ANISOU 2526 O HOH B2081 3676 3366 3991 -1216 532 292 O HETATM 2527 O HOH B2082 -2.821 -19.029 35.447 1.00 53.68 O ANISOU 2527 O HOH B2082 6675 7229 6492 -345 -402 293 O HETATM 2528 O HOH B2083 -2.893 -19.532 35.691 1.00 30.14 O ANISOU 2528 O HOH B2083 3663 4669 3118 65 268 -257 O HETATM 2529 O HOH B2084 4.200 -26.468 42.535 1.00 36.17 O ANISOU 2529 O HOH B2084 5789 3031 4923 119 -287 652 O HETATM 2530 O HOH B2085 2.089 -20.152 42.902 1.00 46.95 O ANISOU 2530 O HOH B2085 6977 4844 6015 -1795 453 -1044 O HETATM 2531 O HOH B2086 14.124 -15.356 37.697 1.00 53.01 O ANISOU 2531 O HOH B2086 4319 8558 7265 -2188 580 -989 O HETATM 2532 O HOH B2087 16.801 -8.868 28.229 1.00 35.33 O ANISOU 2532 O HOH B2087 5074 4143 4205 -1809 673 1443 O HETATM 2533 O HOH B2088 20.350 -11.078 33.311 1.00 47.35 O ANISOU 2533 O HOH B2088 4564 7491 5934 1482 -539 -2831 O HETATM 2534 O HOH B2089 25.838 -9.458 27.297 1.00 70.77 O ANISOU 2534 O HOH B2089 6786 6635 13468 569 -598 -484 O HETATM 2535 O HOH B2090 23.424 -8.422 26.153 1.00 35.54 O ANISOU 2535 O HOH B2090 4468 4283 4750 -193 -944 -505 O HETATM 2536 O HOH B2091 19.463 -5.790 15.397 1.00 53.69 O ANISOU 2536 O HOH B2091 5218 8462 6717 -486 -565 1603 O HETATM 2537 O HOH B2092 17.779 -8.125 15.643 1.00 38.95 O ANISOU 2537 O HOH B2092 4232 5668 4899 1008 -473 305 O HETATM 2538 O HOH B2093 14.375 -9.513 15.374 1.00 35.79 O ANISOU 2538 O HOH B2093 6426 3702 3467 -1695 26 -19 O HETATM 2539 O HOH B2094 12.900 -4.225 18.308 1.00 27.68 O ANISOU 2539 O HOH B2094 3988 3024 3503 -22 46 -607 O HETATM 2540 O HOH B2095 8.395 -6.547 23.652 1.00 25.75 O ANISOU 2540 O HOH B2095 4282 2473 3027 -598 164 -486 O HETATM 2541 O HOH B2096 -1.027 -10.353 21.560 1.00 40.38 O ANISOU 2541 O HOH B2096 6144 3947 5251 -731 -120 -87 O HETATM 2542 O HOH B2097 -3.343 -11.952 21.921 1.00 42.69 O ANISOU 2542 O HOH B2097 6267 5624 4330 -2471 668 -196 O HETATM 2543 O HOH B2098 -0.788 -10.400 24.833 1.00 40.39 O ANISOU 2543 O HOH B2098 5269 5053 5022 98 -406 992 O CONECT 279 285 CONECT 285 279 286 CONECT 286 285 287 289 CONECT 287 286 288 CONECT 288 287 291 CONECT 289 286 290 292 CONECT 290 289 CONECT 291 288 CONECT 292 289 CONECT 1396 1402 CONECT 1402 1396 1403 CONECT 1403 1402 1404 1406 CONECT 1404 1403 1405 CONECT 1405 1404 CONECT 1406 1403 1407 1408 CONECT 1407 1406 CONECT 1408 1406 CONECT 2207 2208 2209 2210 CONECT 2208 2207 CONECT 2209 2207 CONECT 2210 2207 MASTER 410 0 3 2 30 0 2 6 2474 2 21 22 END If you find results from this site helpful for your research, please cite one of our papers:
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