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*** LIPID BINDING PROTEIN 11-OCT-10 3P6D ***elNémo ID: 2402091305182111772Job options:ID = 2402091305182111772 JOBID = LIPID BINDING PROTEIN 11-OCT-10 3P6D USERID = unknown 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 LIPID BINDING PROTEIN 11-OCT-10 3P6D TITLE HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4 IN COMPLEX WITH 3-(4- TITLE 2 METHOXY-3-METHYLPHENYL) PROPIONIC ACID COMPND MOL_ID: 1; COMPND 2 MOLECULE: FATTY ACID-BINDING PROTEIN, ADIPOCYTE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ADIPOCYTE LIPID-BINDING PROTEIN, ALBP, ADIPOCYTE-TYPE FATTY COMPND 5 ACID-BINDING PROTEIN, A-FABP, AFABP, FATTY ACID-BINDING PROTEIN 4; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: FABP4; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A KEYWDS LIPOCALIN, BETA BARREL, FATTY ACID BINDING PROTEIN, LIPID BINDING KEYWDS 2 PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR J.M.GONZALEZ,E.POZHARSKI REVDAT 3 25-FEB-15 3P6D 1 JRNL REVDAT 2 11-FEB-15 3P6D 1 JRNL REVDAT 1 13-APR-11 3P6D 0 JRNL AUTH J.M.GONZALEZ,S.Z.FISHER JRNL TITL STRUCTURAL ANALYSIS OF IBUPROFEN BINDING TO HUMAN ADIPOCYTE JRNL TITL 2 FATTY-ACID BINDING PROTEIN (FABP4). JRNL REF ACTA CRYSTALLOGR F STRUCT V. 71 163 2015 JRNL REF 2 BIOL COMMUN JRNL REFN JRNL PMID 25664790 JRNL DOI 10.1107/S2053230X14027897 REMARK 2 REMARK 2 RESOLUTION. 1.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0109 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 59310 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : 0.141 REMARK 3 R VALUE (WORKING SET) : 0.140 REMARK 3 FREE R VALUE : 0.161 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 2995 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.06 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.09 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3996 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.10 REMARK 3 BIN R VALUE (WORKING SET) : 0.2010 REMARK 3 BIN FREE R VALUE SET COUNT : 231 REMARK 3 BIN FREE R VALUE : 0.2180 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1072 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 14 REMARK 3 SOLVENT ATOMS : 230 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.90 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.86000 REMARK 3 B22 (A**2) : 0.53000 REMARK 3 B33 (A**2) : 0.33000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): NULL REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.017 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.719 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1263 ; 0.021 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 862 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1714 ; 2.016 ; 1.979 REMARK 3 BOND ANGLES OTHERS (DEGREES): 2105 ; 1.006 ; 3.002 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 169 ; 6.436 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 51 ;35.084 ;24.902 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 243 ;13.623 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;16.120 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 192 ; 0.111 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1438 ; 0.012 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 245 ; 0.004 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 777 ; 2.138 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 327 ; 0.618 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1273 ; 3.316 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 486 ; 4.474 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 435 ; 6.291 ; 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): 2125 ; 1.793 ; 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 : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : NULL REMARK 3 ION PROBE RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 4 REMARK 4 3P6D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-OCT-10. REMARK 100 THE RCSB ID CODE IS RCSB062012. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-FEB-10 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRL REMARK 200 BEAMLINE : BL7-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 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 : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59374 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.060 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4 REMARK 200 DATA REDUNDANCY : 6.700 REMARK 200 R MERGE (I) : 0.10300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 14.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1 REMARK 200 DATA REDUNDANCY IN SHELL : 6.00 REMARK 200 R MERGE FOR SHELL (I) : 0.26800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M SODIUM CITRATE, PH 6.5, VAPOR REMARK 280 DIFFUSION, TEMPERATURE 293K 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 16.12200 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.50750 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.69600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.50750 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.12200 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.69600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 GLN A -7 CG CD OE1 NE2 REMARK 470 GLN A -6 CG CD OE1 NE2 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 OE2 GLU A 69 O HOH A 183 1.82 REMARK 500 O HOH A 314 O HOH A 318 1.97 REMARK 500 O HOH A 137 O HOH A 269 2.01 REMARK 500 O HOH A 182 O HOH A 357 2.10 REMARK 500 O VAL A 73 O HOH A 295 2.13 REMARK 500 O HOH A 206 O HOH A 233 2.15 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 O HOH A 302 O HOH A 314 3555 1.73 REMARK 500 O HOH A 302 O HOH A 348 3655 2.14 REMARK 500 O HOH A 228 O HOH A 317 3645 2.17 REMARK 500 O HOH A 209 O HOH A 222 4555 2.18 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 126 NE - CZ - NH1 ANGL. DEV. = 3.5 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 PHE A 57 -70.89 -87.35 REMARK 500 ASP A 110 -133.93 54.49 REMARK 500 LYS A 120 -123.45 48.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 193 DISTANCE = 5.08 ANGSTROMS REMARK 525 HOH A 258 DISTANCE = 8.59 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZGB A 133 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3P6C RELATED DB: PDB REMARK 900 RELATED ID: 3P6E RELATED DB: PDB REMARK 900 RELATED ID: 3P6F RELATED DB: PDB REMARK 900 RELATED ID: 3P6G RELATED DB: PDB REMARK 900 RELATED ID: 3P6H RELATED DB: PDB DBREF 3P6D A 0 131 UNP P15090 FABP4_HUMAN 1 132 SEQADV 3P6D GLN A -7 UNP P15090 EXPRESSION TAG SEQADV 3P6D GLN A -6 UNP P15090 EXPRESSION TAG SEQADV 3P6D MET A -5 UNP P15090 EXPRESSION TAG SEQADV 3P6D GLY A -4 UNP P15090 EXPRESSION TAG SEQADV 3P6D ARG A -3 UNP P15090 EXPRESSION TAG SEQADV 3P6D GLY A -2 UNP P15090 EXPRESSION TAG SEQADV 3P6D SER A -1 UNP P15090 EXPRESSION TAG SEQRES 1 A 139 GLN GLN MET GLY ARG GLY SER MET CYS ASP ALA PHE VAL SEQRES 2 A 139 GLY THR TRP LYS LEU VAL SER SER GLU ASN PHE ASP ASP SEQRES 3 A 139 TYR MET LYS GLU VAL GLY VAL GLY PHE ALA THR ARG LYS SEQRES 4 A 139 VAL ALA GLY MET ALA LYS PRO ASN MET ILE ILE SER VAL SEQRES 5 A 139 ASN GLY ASP VAL ILE THR ILE LYS SER GLU SER THR PHE SEQRES 6 A 139 LYS ASN THR GLU ILE SER PHE ILE LEU GLY GLN GLU PHE SEQRES 7 A 139 ASP GLU VAL THR ALA ASP ASP ARG LYS VAL LYS SER THR SEQRES 8 A 139 ILE THR LEU ASP GLY GLY VAL LEU VAL HIS VAL GLN LYS SEQRES 9 A 139 TRP ASP GLY LYS SER THR THR ILE LYS ARG LYS ARG GLU SEQRES 10 A 139 ASP ASP LYS LEU VAL VAL GLU CYS VAL MET LYS GLY VAL SEQRES 11 A 139 THR SER THR ARG VAL TYR GLU ARG ALA HET ZGB A 133 28 HETNAM ZGB 3-(4-METHOXY-3-METHYLPHENYL)PROPANOIC ACID FORMUL 2 ZGB C11 H14 O3 FORMUL 3 HOH *230(H2 O) HELIX 1 1 SER A -1 VAL A 5 5 7 HELIX 2 2 ASN A 15 GLY A 24 1 10 HELIX 3 3 GLY A 26 ALA A 36 1 11 SHEET 1 A10 THR A 60 PHE A 64 0 SHEET 2 A10 VAL A 48 GLU A 54 -1 N ILE A 49 O PHE A 64 SHEET 3 A10 ASN A 39 ASN A 45 -1 N ASN A 39 O GLU A 54 SHEET 4 A10 GLY A 6 GLU A 14 -1 N TRP A 8 O MET A 40 SHEET 5 A10 VAL A 122 ARG A 130 -1 O VAL A 127 N VAL A 11 SHEET 6 A10 LYS A 112 MET A 119 -1 N VAL A 115 O ARG A 126 SHEET 7 A10 LYS A 100 GLU A 109 -1 N THR A 103 O VAL A 118 SHEET 8 A10 VAL A 90 TRP A 97 -1 N TRP A 97 O LYS A 100 SHEET 9 A10 LYS A 79 ASP A 87 -1 N THR A 85 O VAL A 92 SHEET 10 A10 PHE A 70 VAL A 73 -1 N PHE A 70 O SER A 82 SITE 1 AC1 12 PHE A 16 MET A 20 VAL A 25 ALA A 33 SITE 2 AC1 12 PHE A 57 ALA A 75 ASP A 76 ARG A 78 SITE 3 AC1 12 ARG A 126 TYR A 128 HOH A 281 HOH A 319 CRYST1 32.244 53.392 75.015 90.00 90.00 90.00 P 21 21 21 4 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 0.031014 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018729 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013331 0.00000 ATOM 1 N GLN A -7 -0.540 30.851 -7.351 1.00 33.19 N ANISOU 1 N GLN A -7 4271 4187 4150 -52 -236 -79 N ATOM 2 CA GLN A -7 -1.548 30.249 -8.296 1.00 31.85 C ANISOU 2 CA GLN A -7 4168 4030 3902 -27 -205 -58 C ATOM 3 C GLN A -7 -0.919 29.409 -9.420 1.00 30.32 C ANISOU 3 C GLN A -7 4018 3793 3706 -12 -236 11 C ATOM 4 O GLN A -7 -1.481 29.278 -10.515 1.00 31.71 O ANISOU 4 O GLN A -7 4234 4181 3632 -171 -352 -116 O ATOM 5 CB GLN A -7 -2.428 31.359 -8.878 1.00 32.11 C ANISOU 5 CB GLN A -7 4222 4001 3974 -3 -230 -13 C ATOM 6 N GLN A -6 0.257 28.853 -9.160 1.00 28.06 N ANISOU 6 N GLN A -6 3886 3326 3447 -21 -184 133 N ATOM 7 CA GLN A -6 0.893 27.904 -10.095 1.00 25.76 C ANISOU 7 CA GLN A -6 3720 2782 3285 12 -124 423 C ATOM 8 C GLN A -6 1.224 26.627 -9.385 1.00 23.70 C ANISOU 8 C GLN A -6 3548 2466 2989 8 -124 492 C ATOM 9 O GLN A -6 1.193 26.535 -8.129 1.00 25.02 O ANISOU 9 O GLN A -6 3785 2794 2927 -32 -137 470 O ATOM 10 CB GLN A -6 2.160 28.501 -10.727 1.00 25.96 C ANISOU 10 CB GLN A -6 3831 2629 3402 -98 -20 593 C ATOM 11 N MET A -5 1.486 25.611 -10.193 1.00 23.02 N ANISOU 11 N MET A -5 3398 2334 3014 -121 -164 279 N ATOM 12 CA MET A -5 1.872 24.333 -9.641 1.00 22.27 C ANISOU 12 CA MET A -5 3284 2335 2840 -32 -129 214 C ATOM 13 C MET A -5 3.331 24.390 -9.283 1.00 22.20 C ANISOU 13 C MET A -5 3232 2314 2887 -8 -17 137 C ATOM 14 O MET A -5 4.221 24.628 -10.152 1.00 24.87 O ANISOU 14 O MET A -5 3425 3000 3023 55 -11 350 O ATOM 15 CB MET A -5 1.578 23.114 -10.529 1.00 23.22 C ANISOU 15 CB MET A -5 3385 2458 2978 -67 -184 195 C ATOM 16 CG MET A -5 1.767 21.786 -9.766 1.00 21.77 C ANISOU 16 CG MET A -5 3527 2929 1812 277 -184 104 C ATOM 17 SD MET A -5 1.214 20.391 -10.657 1.00 23.37 S ANISOU 17 SD MET A -5 3855 2477 2545 -144 48 -269 S ATOM 18 CE MET A -5 -0.492 20.622 -10.647 1.00 17.51 C ANISOU 18 CE MET A -5 3355 2108 1189 -255 -101 5 C ATOM 19 N GLY A -4 3.563 24.131 -8.012 1.00 23.23 N ANISOU 19 N GLY A -4 3245 2554 3024 113 -22 -88 N ATOM 20 CA GLY A -4 4.874 24.169 -7.456 1.00 22.44 C ANISOU 20 CA GLY A -4 3142 2419 2966 181 -29 -149 C ATOM 21 C GLY A -4 5.660 22.962 -7.871 1.00 21.98 C ANISOU 21 C GLY A -4 3069 2327 2952 177 -96 -165 C ATOM 22 O GLY A -4 5.144 21.955 -8.372 1.00 23.79 O ANISOU 22 O GLY A -4 3116 2413 3509 212 -22 -408 O ATOM 23 N ARG A -3 6.942 23.062 -7.624 1.00 22.35 N ANISOU 23 N ARG A -3 3062 2362 3065 143 -68 59 N ATOM 24 CA ARG A -3 7.833 21.962 -7.819 1.00 21.95 C ANISOU 24 CA ARG A -3 3098 2407 2835 178 -15 355 C ATOM 25 C ARG A -3 7.826 20.995 -6.619 1.00 19.61 C ANISOU 25 C ARG A -3 2955 2268 2228 199 -32 370 C ATOM 26 O ARG A -3 7.268 21.264 -5.531 1.00 21.99 O ANISOU 26 O ARG A -3 3223 2694 2436 147 8 185 O ATOM 27 CB ARG A -3 9.238 22.495 -8.117 1.00 24.21 C ANISOU 27 CB ARG A -3 3288 2698 3212 140 68 378 C ATOM 28 CG ARG A -3 9.316 23.279 -9.439 1.00 27.49 C ANISOU 28 CG ARG A -3 3662 3217 3566 110 146 520 C ATOM 29 CD ARG A -3 9.329 22.270 -10.588 1.00 30.59 C ANISOU 29 CD ARG A -3 4235 3534 3852 82 110 351 C ATOM 30 NE ARG A -3 9.040 22.780 -11.935 1.00 35.33 N ANISOU 30 NE ARG A -3 4515 4496 4412 336 -82 369 N ATOM 31 CZ ARG A -3 9.913 23.328 -12.781 1.00 37.65 C ANISOU 31 CZ ARG A -3 4714 5005 4584 223 -71 248 C ATOM 32 NH1 ARG A -3 11.188 23.539 -12.452 1.00 38.39 N ANISOU 32 NH1 ARG A -3 4572 5265 4747 225 -29 -165 N ATOM 33 NH2 ARG A -3 9.492 23.698 -13.981 1.00 37.22 N ANISOU 33 NH2 ARG A -3 4840 5126 4176 0 -40 425 N ATOM 34 N GLY A -2 8.425 19.851 -6.893 1.00 18.66 N ANISOU 34 N GLY A -2 2844 2188 2057 65 45 481 N ATOM 35 CA GLY A -2 8.602 18.848 -5.918 1.00 17.85 C ANISOU 35 CA GLY A -2 2721 2078 1980 -81 -43 500 C ATOM 36 C GLY A -2 9.788 19.121 -5.045 1.00 17.42 C ANISOU 36 C GLY A -2 2771 1871 1973 -180 -62 608 C ATOM 37 O GLY A -2 10.507 20.133 -5.178 1.00 19.83 O ANISOU 37 O GLY A -2 3224 1972 2337 -184 -307 725 O ATOM 38 N SER A -1 10.010 18.196 -4.139 1.00 17.53 N ANISOU 38 N SER A -1 2880 2007 1770 -187 -170 443 N ATOM 39 CA SER A -1 11.153 18.315 -3.281 1.00 16.53 C ANISOU 39 CA SER A -1 2913 1597 1770 -226 6 507 C ATOM 40 C SER A -1 11.612 16.946 -2.866 1.00 16.53 C ANISOU 40 C SER A -1 2780 1788 1710 -220 80 456 C ATOM 41 O SER A -1 10.918 15.952 -2.966 1.00 17.86 O ANISOU 41 O SER A -1 3076 1770 1938 -369 79 803 O ATOM 42 CB SER A -1 10.816 19.097 -2.005 1.00 18.93 C ANISOU 42 CB SER A -1 3394 1857 1941 -13 88 530 C ATOM 43 OG SER A -1 10.197 18.315 -1.059 1.00 24.78 O ANISOU 43 OG SER A -1 3854 2958 2601 50 653 456 O ATOM 44 N AMET A 0 12.832 16.856 -2.362 0.50 15.58 N ANISOU 44 N AMET A 0 2791 1597 1530 -297 -5 561 N ATOM 45 N BMET A 0 12.804 16.914 -2.316 0.50 17.67 N ANISOU 45 N BMET A 0 2881 1905 1925 -262 3 473 N ATOM 46 CA AMET A 0 13.333 15.576 -1.860 0.50 15.33 C ANISOU 46 CA AMET A 0 2746 1676 1400 -198 -50 534 C ATOM 47 CA BMET A 0 13.372 15.679 -1.855 0.50 18.34 C ANISOU 47 CA BMET A 0 2920 2033 2014 -197 -11 467 C ATOM 48 C AMET A 0 12.351 14.937 -0.858 0.50 15.42 C ANISOU 48 C AMET A 0 2785 1578 1494 -121 -83 568 C ATOM 49 C BMET A 0 12.487 14.996 -0.802 0.50 17.36 C ANISOU 49 C BMET A 0 2911 1836 1850 -126 -89 531 C ATOM 50 O AMET A 0 12.137 13.722 -0.900 0.50 15.62 O ANISOU 50 O AMET A 0 2642 1685 1608 80 -103 433 O ATOM 51 O BMET A 0 12.496 13.776 -0.730 0.50 17.86 O ANISOU 51 O BMET A 0 3014 1813 1958 -138 -87 693 O ATOM 52 CB AMET A 0 14.721 15.767 -1.254 0.50 15.13 C ANISOU 52 CB AMET A 0 2761 1671 1316 -126 -19 440 C ATOM 53 CB BMET A 0 14.776 15.969 -1.349 0.50 19.47 C ANISOU 53 CB BMET A 0 2987 2300 2108 -121 -24 393 C ATOM 54 CG AMET A 0 15.467 14.488 -0.953 0.50 14.81 C ANISOU 54 CG AMET A 0 2671 1903 1052 -70 -194 597 C ATOM 55 CG BMET A 0 15.794 14.958 -1.763 0.50 22.23 C ANISOU 55 CG BMET A 0 2939 2663 2845 -38 208 319 C ATOM 56 SD AMET A 0 16.770 14.508 0.340 0.50 21.58 S ANISOU 56 SD AMET A 0 3713 2651 1835 171 -578 -291 S ATOM 57 SD BMET A 0 16.345 14.079 -0.312 0.50 29.90 S ANISOU 57 SD BMET A 0 4091 3751 3517 139 -47 30 S ATOM 58 CE AMET A 0 15.774 14.665 1.789 0.50 23.91 C ANISOU 58 CE AMET A 0 3564 2874 2646 153 111 -542 C ATOM 59 CE BMET A 0 14.958 14.286 0.824 0.50 10.59 C ANISOU 59 CE BMET A 0 2199 1075 747 -17 -290 273 C ATOM 60 N CYS A 1 11.715 15.755 -0.001 1.00 17.31 N ANISOU 60 N CYS A 1 2821 1899 1855 -156 -1 531 N ATOM 61 CA ACYS A 1 10.748 15.293 1.043 0.50 17.00 C ANISOU 61 CA ACYS A 1 2986 1701 1771 -49 7 604 C ATOM 62 CA BCYS A 1 10.809 15.133 1.010 0.50 16.52 C ANISOU 62 CA BCYS A 1 2945 1760 1571 -142 -40 520 C ATOM 63 C CYS A 1 9.566 14.495 0.410 1.00 15.82 C ANISOU 63 C CYS A 1 2709 1620 1680 4 74 711 C ATOM 64 O CYS A 1 8.836 13.785 1.133 1.00 16.64 O ANISOU 64 O CYS A 1 2963 1499 1859 96 334 959 O ATOM 65 CB ACYS A 1 10.256 16.513 1.865 0.50 19.14 C ANISOU 65 CB ACYS A 1 2965 2089 2216 5 154 366 C ATOM 66 CB BCYS A 1 10.368 16.069 2.113 0.50 17.06 C ANISOU 66 CB BCYS A 1 2895 1990 1595 6 101 409 C ATOM 67 SG ACYS A 1 10.336 16.441 3.749 0.50 26.21 S ANISOU 67 SG ACYS A 1 4155 3019 2782 138 520 476 S ATOM 68 SG BCYS A 1 11.656 16.811 3.034 0.50 23.25 S ANISOU 68 SG BCYS A 1 3671 3095 2066 -332 -63 -663 S ATOM 69 N ASP A 2 9.427 14.585 -0.895 1.00 15.81 N ANISOU 69 N ASP A 2 2613 1747 1645 -366 -81 853 N ATOM 70 CA ASP A 2 8.382 13.852 -1.526 1.00 17.65 C ANISOU 70 CA ASP A 2 2818 1931 1956 -469 -206 872 C ATOM 71 C ASP A 2 8.554 12.339 -1.314 1.00 16.28 C ANISOU 71 C ASP A 2 2803 1960 1422 -443 -60 763 C ATOM 72 O ASP A 2 7.547 11.665 -1.348 1.00 16.49 O ANISOU 72 O ASP A 2 2912 1860 1491 -506 -79 499 O ATOM 73 CB ASP A 2 8.235 14.246 -2.958 1.00 19.35 C ANISOU 73 CB ASP A 2 3099 2253 1999 -616 -318 1059 C ATOM 74 CG ASP A 2 7.635 15.673 -3.145 1.00 20.64 C ANISOU 74 CG ASP A 2 3260 2310 2272 -48 -468 1210 C ATOM 75 OD1 ASP A 2 6.970 16.213 -2.192 1.00 25.28 O ANISOU 75 OD1 ASP A 2 3719 2821 3064 151 -315 899 O ATOM 76 OD2 ASP A 2 7.849 16.259 -4.178 1.00 24.21 O ANISOU 76 OD2 ASP A 2 3408 2870 2918 -312 -606 1081 O ATOM 77 N ALA A 3 9.776 11.825 -1.048 1.00 16.21 N ANISOU 77 N ALA A 3 2739 2073 1347 -436 285 624 N ATOM 78 CA ALA A 3 10.004 10.412 -0.787 1.00 16.02 C ANISOU 78 CA ALA A 3 2778 1923 1385 -142 253 417 C ATOM 79 C ALA A 3 9.266 9.958 0.462 1.00 13.48 C ANISOU 79 C ALA A 3 2687 1428 1004 -70 156 412 C ATOM 80 O ALA A 3 9.001 8.752 0.593 1.00 14.02 O ANISOU 80 O ALA A 3 2935 1364 1028 16 435 14 O ATOM 81 CB ALA A 3 11.451 10.157 -0.588 1.00 19.48 C ANISOU 81 CB ALA A 3 2949 2483 1967 -179 347 802 C ATOM 82 N PHE A 4 8.957 10.861 1.383 1.00 11.60 N ANISOU 82 N PHE A 4 2561 947 897 -76 159 270 N ATOM 83 CA PHE A 4 8.226 10.506 2.574 1.00 10.49 C ANISOU 83 CA PHE A 4 2496 714 774 51 79 224 C ATOM 84 C PHE A 4 6.722 10.551 2.415 1.00 9.75 C ANISOU 84 C PHE A 4 2393 609 701 -80 167 139 C ATOM 85 O PHE A 4 6.019 9.994 3.256 1.00 10.85 O ANISOU 85 O PHE A 4 2524 790 806 -90 91 174 O ATOM 86 CB PHE A 4 8.609 11.442 3.712 1.00 11.06 C ANISOU 86 CB PHE A 4 2418 815 968 30 -24 24 C ATOM 87 CG PHE A 4 10.025 11.346 4.130 1.00 10.85 C ANISOU 87 CG PHE A 4 2328 924 868 96 -45 1 C ATOM 88 CD1 PHE A 4 10.405 10.322 4.992 1.00 12.76 C ANISOU 88 CD1 PHE A 4 2413 1322 1111 -80 -104 -36 C ATOM 89 CD2 PHE A 4 10.970 12.246 3.761 1.00 14.35 C ANISOU 89 CD2 PHE A 4 2648 1483 1321 -213 -250 339 C ATOM 90 CE1 PHE A 4 11.707 10.166 5.417 1.00 13.55 C ANISOU 90 CE1 PHE A 4 2637 1477 1034 -8 0 126 C ATOM 91 CE2 PHE A 4 12.317 12.090 4.161 1.00 15.38 C ANISOU 91 CE2 PHE A 4 2778 1543 1523 -408 136 310 C ATOM 92 CZ PHE A 4 12.666 11.050 4.993 1.00 13.13 C ANISOU 92 CZ PHE A 4 2340 1521 1128 84 -13 -168 C ATOM 93 N VAL A 5 6.221 11.267 1.427 1.00 10.05 N ANISOU 93 N VAL A 5 2495 686 636 -73 63 148 N ATOM 94 CA VAL A 5 4.798 11.479 1.342 1.00 10.42 C ANISOU 94 CA VAL A 5 2423 795 739 -69 63 -17 C ATOM 95 C VAL A 5 4.051 10.211 1.022 1.00 10.98 C ANISOU 95 C VAL A 5 2485 870 816 -139 65 -309 C ATOM 96 O VAL A 5 4.439 9.439 0.164 1.00 13.99 O ANISOU 96 O VAL A 5 2936 1082 1295 -417 452 -491 O ATOM 97 CB VAL A 5 4.539 12.601 0.317 1.00 12.01 C ANISOU 97 CB VAL A 5 2635 966 963 -45 -8 148 C ATOM 98 CG1 VAL A 5 3.106 12.649 -0.216 1.00 14.86 C ANISOU 98 CG1 VAL A 5 3196 1351 1100 -84 -233 92 C ATOM 99 CG2 VAL A 5 5.116 13.933 0.809 1.00 13.29 C ANISOU 99 CG2 VAL A 5 2939 695 1414 -131 -2 292 C ATOM 100 N GLY A 6 2.929 10.037 1.672 1.00 10.94 N ANISOU 100 N GLY A 6 2450 900 804 -160 128 -249 N ATOM 101 CA GLY A 6 2.086 8.920 1.431 1.00 11.98 C ANISOU 101 CA GLY A 6 2541 1120 891 -312 35 -267 C ATOM 102 C GLY A 6 1.435 8.420 2.684 1.00 10.18 C ANISOU 102 C GLY A 6 2265 828 774 -116 -84 -48 C ATOM 103 O GLY A 6 1.346 9.120 3.672 1.00 11.89 O ANISOU 103 O GLY A 6 2799 796 920 -304 145 -232 O ATOM 104 N THR A 7 0.931 7.215 2.594 1.00 10.26 N ANISOU 104 N THR A 7 2414 707 774 -116 -226 2 N ATOM 105 CA THR A 7 0.189 6.561 3.634 1.00 10.70 C ANISOU 105 CA THR A 7 2461 654 950 -69 -173 0 C ATOM 106 C THR A 7 0.949 5.290 4.007 1.00 10.28 C ANISOU 106 C THR A 7 2421 687 798 -220 -69 55 C ATOM 107 O THR A 7 1.211 4.461 3.150 1.00 12.26 O ANISOU 107 O THR A 7 2896 854 907 47 -277 -161 O ATOM 108 CB THR A 7 -1.206 6.229 3.146 1.00 12.81 C ANISOU 108 CB THR A 7 2508 973 1385 -36 -128 141 C ATOM 109 OG1 THR A 7 -1.776 7.333 2.447 1.00 16.62 O ANISOU 109 OG1 THR A 7 2962 1326 2025 -21 -327 241 O ATOM 110 CG2 THR A 7 -2.103 5.812 4.269 1.00 16.07 C ANISOU 110 CG2 THR A 7 2780 1468 1858 129 68 218 C ATOM 111 N TRP A 8 1.298 5.176 5.276 1.00 10.06 N ANISOU 111 N TRP A 8 2359 764 699 -127 75 70 N ATOM 112 CA TRP A 8 2.214 4.164 5.807 1.00 9.70 C ANISOU 112 CA TRP A 8 2463 585 637 -9 8 112 C ATOM 113 C TRP A 8 1.546 3.416 6.937 1.00 10.00 C ANISOU 113 C TRP A 8 2581 635 580 -128 103 73 C ATOM 114 O TRP A 8 0.736 3.988 7.666 1.00 14.15 O ANISOU 114 O TRP A 8 3308 876 1191 -22 671 182 O ATOM 115 CB TRP A 8 3.435 4.890 6.344 1.00 9.68 C ANISOU 115 CB TRP A 8 2303 792 580 89 31 192 C ATOM 116 CG TRP A 8 4.220 5.699 5.310 1.00 9.50 C ANISOU 116 CG TRP A 8 2432 604 574 -24 -23 111 C ATOM 117 CD1 TRP A 8 4.103 7.027 5.072 1.00 9.55 C ANISOU 117 CD1 TRP A 8 2359 735 532 -64 82 49 C ATOM 118 CD2 TRP A 8 5.185 5.204 4.401 1.00 9.37 C ANISOU 118 CD2 TRP A 8 2200 690 667 -91 -144 65 C ATOM 119 NE1 TRP A 8 4.934 7.412 4.056 1.00 10.13 N ANISOU 119 NE1 TRP A 8 2452 657 738 -130 48 82 N ATOM 120 CE2 TRP A 8 5.620 6.302 3.628 1.00 9.70 C ANISOU 120 CE2 TRP A 8 2186 923 576 -174 63 9 C ATOM 121 CE3 TRP A 8 5.745 3.943 4.151 1.00 10.31 C ANISOU 121 CE3 TRP A 8 2323 936 657 -188 -146 -10 C ATOM 122 CZ2 TRP A 8 6.616 6.158 2.662 1.00 11.12 C ANISOU 122 CZ2 TRP A 8 2365 995 861 -270 26 -64 C ATOM 123 CZ3 TRP A 8 6.698 3.812 3.210 1.00 10.79 C ANISOU 123 CZ3 TRP A 8 2313 990 796 -108 -72 -148 C ATOM 124 CH2 TRP A 8 7.114 4.884 2.455 1.00 11.77 C ANISOU 124 CH2 TRP A 8 2308 1386 779 -237 150 -304 C ATOM 125 N LYS A 9 1.872 2.164 7.086 1.00 9.54 N ANISOU 125 N LYS A 9 2392 617 616 -152 -63 194 N ATOM 126 CA LYS A 9 1.321 1.341 8.149 1.00 10.46 C ANISOU 126 CA LYS A 9 2276 824 873 -103 -48 205 C ATOM 127 C LYS A 9 2.459 0.676 8.917 1.00 9.98 C ANISOU 127 C LYS A 9 2212 795 784 -210 26 189 C ATOM 128 O LYS A 9 3.416 0.178 8.315 1.00 10.18 O ANISOU 128 O LYS A 9 2333 806 726 -69 -17 137 O ATOM 129 CB LYS A 9 0.395 0.282 7.577 1.00 12.32 C ANISOU 129 CB LYS A 9 2424 1003 1252 -378 -256 450 C ATOM 130 CG LYS A 9 0.951 -0.672 6.629 1.00 18.74 C ANISOU 130 CG LYS A 9 3434 1578 2108 -508 -368 140 C ATOM 131 CD LYS A 9 -0.097 -1.660 6.213 1.00 24.47 C ANISOU 131 CD LYS A 9 3808 2436 3050 -581 -524 -282 C ATOM 132 CE LYS A 9 0.439 -2.706 5.295 1.00 26.43 C ANISOU 132 CE LYS A 9 3993 2215 3831 -831 -543 -646 C ATOM 133 NZ LYS A 9 0.555 -2.172 3.905 1.00 33.37 N ANISOU 133 NZ LYS A 9 4648 3516 4514 -271 -318 87 N ATOM 134 N LEU A 10 2.397 0.686 10.238 1.00 10.56 N ANISOU 134 N LEU A 10 2154 1125 733 -184 13 289 N ATOM 135 CA LEU A 10 3.447 0.048 11.055 1.00 10.43 C ANISOU 135 CA LEU A 10 2126 1107 728 -310 -43 222 C ATOM 136 C LEU A 10 3.403 -1.464 10.864 1.00 11.22 C ANISOU 136 C LEU A 10 2387 1032 844 -381 -143 298 C ATOM 137 O LEU A 10 2.345 -2.053 11.078 1.00 13.82 O ANISOU 137 O LEU A 10 2403 1390 1455 -559 -192 463 O ATOM 138 CB LEU A 10 3.245 0.393 12.529 1.00 11.23 C ANISOU 138 CB LEU A 10 2147 1413 706 -142 1 304 C ATOM 139 CG LEU A 10 4.329 -0.173 13.464 1.00 11.67 C ANISOU 139 CG LEU A 10 2263 1459 711 -241 -19 247 C ATOM 140 CD1 LEU A 10 5.633 0.506 13.259 1.00 12.26 C ANISOU 140 CD1 LEU A 10 2038 1658 963 -71 23 86 C ATOM 141 CD2 LEU A 10 3.898 -0.053 14.925 1.00 16.13 C ANISOU 141 CD2 LEU A 10 2366 2841 920 72 -23 310 C ATOM 142 N VAL A 11 4.558 -2.045 10.538 1.00 11.45 N ANISOU 142 N VAL A 11 2479 865 1003 -381 -314 254 N ATOM 143 CA VAL A 11 4.673 -3.488 10.389 1.00 13.24 C ANISOU 143 CA VAL A 11 2963 790 1275 -270 -427 210 C ATOM 144 C VAL A 11 5.612 -4.185 11.377 1.00 14.07 C ANISOU 144 C VAL A 11 3077 820 1448 -274 -484 426 C ATOM 145 O VAL A 11 5.492 -5.378 11.551 1.00 18.26 O ANISOU 145 O VAL A 11 3699 934 2302 -382 -1097 541 O ATOM 146 CB VAL A 11 5.012 -3.906 8.986 1.00 14.05 C ANISOU 146 CB VAL A 11 3091 710 1537 -92 -407 10 C ATOM 147 CG1 VAL A 11 3.932 -3.451 8.037 1.00 16.46 C ANISOU 147 CG1 VAL A 11 3556 1130 1567 68 -495 -94 C ATOM 148 CG2 VAL A 11 6.411 -3.500 8.514 1.00 16.84 C ANISOU 148 CG2 VAL A 11 3471 1368 1559 0 26 -388 C ATOM 149 N SER A 12 6.566 -3.472 11.977 1.00 12.54 N ANISOU 149 N SER A 12 2872 709 1181 -185 -473 182 N ATOM 150 CA SER A 12 7.388 -4.107 12.960 1.00 13.14 C ANISOU 150 CA SER A 12 2818 940 1232 -63 -450 249 C ATOM 151 C SER A 12 7.901 -3.055 13.919 1.00 11.80 C ANISOU 151 C SER A 12 2430 951 1100 -154 -367 329 C ATOM 152 O SER A 12 8.052 -1.881 13.572 1.00 11.52 O ANISOU 152 O SER A 12 2597 822 959 -293 -245 393 O ATOM 153 CB SER A 12 8.526 -4.860 12.337 1.00 16.52 C ANISOU 153 CB SER A 12 3016 1588 1673 155 -561 132 C ATOM 154 OG SER A 12 9.492 -4.040 11.817 1.00 18.53 O ANISOU 154 OG SER A 12 3408 1960 1670 376 -281 339 O ATOM 155 N SER A 13 8.186 -3.529 15.122 1.00 12.35 N ANISOU 155 N SER A 13 2682 854 1155 -318 -464 468 N ATOM 156 CA SER A 13 8.747 -2.675 16.131 1.00 13.05 C ANISOU 156 CA SER A 13 2833 1028 1098 -325 -395 495 C ATOM 157 C SER A 13 9.703 -3.472 17.005 1.00 12.78 C ANISOU 157 C SER A 13 2790 931 1133 -202 -446 568 C ATOM 158 O SER A 13 9.407 -4.605 17.363 1.00 16.35 O ANISOU 158 O SER A 13 3194 1199 1819 -395 -765 868 O ATOM 159 CB SER A 13 7.561 -2.157 16.965 1.00 14.64 C ANISOU 159 CB SER A 13 3059 1208 1294 -271 -487 403 C ATOM 160 OG SER A 13 7.931 -1.276 18.008 1.00 16.58 O ANISOU 160 OG SER A 13 3789 1268 1243 -265 -696 283 O ATOM 161 N AGLU A 14 10.792 -2.842 17.367 0.33 8.30 N ANISOU 161 N AGLU A 14 2356 366 430 -271 -329 93 N ATOM 162 N CGLU A 14 10.881 -2.916 17.288 0.33 9.83 N ANISOU 162 N CGLU A 14 2425 606 703 -99 -264 385 N ATOM 163 CA AGLU A 14 11.747 -3.447 18.220 0.50 10.27 C ANISOU 163 CA AGLU A 14 2606 416 880 107 -203 -160 C ATOM 164 CA CGLU A 14 11.922 -3.499 18.167 0.50 12.39 C ANISOU 164 CA CGLU A 14 2654 924 1126 104 -274 158 C ATOM 165 C GLU A 14 12.151 -2.522 19.298 1.00 9.93 C ANISOU 165 C GLU A 14 2348 562 861 139 -199 129 C ATOM 166 O GLU A 14 12.436 -1.349 19.042 1.00 10.53 O ANISOU 166 O GLU A 14 2599 530 872 38 -188 95 O ATOM 167 CB AGLU A 14 12.990 -3.853 17.426 0.50 12.87 C ANISOU 167 CB AGLU A 14 2654 975 1257 187 -143 -207 C ATOM 168 CB CGLU A 14 13.254 -3.804 17.384 0.50 14.57 C ANISOU 168 CB CGLU A 14 2830 1269 1435 196 -180 -3 C ATOM 169 CG AGLU A 14 12.826 -5.013 16.505 0.50 13.75 C ANISOU 169 CG AGLU A 14 2890 846 1488 319 -89 -724 C ATOM 170 CG CGLU A 14 14.633 -3.703 18.184 0.50 20.78 C ANISOU 170 CG CGLU A 14 2975 2606 2312 140 -144 47 C ATOM 171 CD AGLU A 14 12.756 -6.416 17.187 0.50 14.32 C ANISOU 171 CD AGLU A 14 2774 758 1906 182 -230 -428 C ATOM 172 CD CGLU A 14 15.385 -5.030 18.566 0.50 22.69 C ANISOU 172 CD CGLU A 14 3124 2687 2810 -18 -140 148 C ATOM 173 OE1AGLU A 14 13.002 -6.528 18.394 0.50 16.14 O ANISOU 173 OE1AGLU A 14 2883 1205 2045 193 -664 -140 O ATOM 174 OE1CGLU A 14 16.336 -5.511 17.858 0.50 19.57 O ANISOU 174 OE1CGLU A 14 2723 1278 3433 295 -444 -229 O ATOM 175 OE2AGLU A 14 12.462 -7.381 16.469 0.50 17.38 O ANISOU 175 OE2AGLU A 14 2928 1148 2526 67 -237 -700 O ATOM 176 OE2CGLU A 14 15.131 -5.551 19.686 0.50 21.20 O ANISOU 176 OE2CGLU A 14 2849 3302 1902 -189 -772 510 O ATOM 177 N ASN A 15 12.145 -3.018 20.525 1.00 9.79 N ANISOU 177 N ASN A 15 2336 514 870 14 -196 141 N ATOM 178 CA AASN A 15 12.665 -2.288 21.687 0.50 8.84 C ANISOU 178 CA AASN A 15 2169 494 695 57 -111 159 C ATOM 179 CA BASN A 15 12.617 -2.315 21.699 0.50 10.52 C ANISOU 179 CA BASN A 15 2326 710 960 11 -95 87 C ATOM 180 C ASN A 15 11.836 -1.060 22.049 1.00 9.62 C ANISOU 180 C ASN A 15 2188 620 845 -43 -83 41 C ATOM 181 O ASN A 15 12.312 -0.207 22.776 1.00 10.04 O ANISOU 181 O ASN A 15 2223 701 888 19 -38 83 O ATOM 182 CB AASN A 15 14.137 -1.881 21.558 0.50 8.44 C ANISOU 182 CB AASN A 15 2103 597 507 150 -64 50 C ATOM 183 CB BASN A 15 14.109 -2.083 21.624 0.50 11.67 C ANISOU 183 CB BASN A 15 2433 888 1112 -54 -74 159 C ATOM 184 CG AASN A 15 14.906 -1.956 22.895 0.50 8.39 C ANISOU 184 CG AASN A 15 1875 708 605 191 -63 208 C ATOM 185 CG BASN A 15 14.858 -3.389 21.548 0.50 15.76 C ANISOU 185 CG BASN A 15 2617 1660 1711 51 169 -369 C ATOM 186 OD1AASN A 15 14.741 -2.878 23.700 0.50 9.53 O ANISOU 186 OD1AASN A 15 2177 611 831 -53 -133 384 O ATOM 187 OD1BASN A 15 14.866 -4.159 22.502 0.50 19.64 O ANISOU 187 OD1BASN A 15 2992 2070 2399 51 45 -239 O ATOM 188 ND2AASN A 15 15.741 -0.947 23.114 0.50 8.32 N ANISOU 188 ND2AASN A 15 1826 548 784 29 -81 139 N ATOM 189 ND2BASN A 15 15.427 -3.670 20.410 0.50 17.03 N ANISOU 189 ND2BASN A 15 3267 1237 1965 -193 389 -361 N ATOM 190 N PHE A 16 10.582 -1.010 21.607 1.00 9.90 N ANISOU 190 N PHE A 16 2217 578 966 16 -76 1 N ATOM 191 CA PHE A 16 9.758 0.175 21.869 1.00 10.07 C ANISOU 191 CA PHE A 16 2158 708 959 -45 -77 23 C ATOM 192 C PHE A 16 9.395 0.307 23.323 1.00 10.01 C ANISOU 192 C PHE A 16 2073 894 836 -36 -23 108 C ATOM 193 O PHE A 16 9.327 1.425 23.841 1.00 9.93 O ANISOU 193 O PHE A 16 2224 677 870 -35 -61 26 O ATOM 194 CB PHE A 16 8.543 0.180 20.950 1.00 10.41 C ANISOU 194 CB PHE A 16 2174 753 1027 -3 -95 11 C ATOM 195 CG PHE A 16 7.778 1.505 20.919 1.00 11.08 C ANISOU 195 CG PHE A 16 2314 1094 801 126 -143 -51 C ATOM 196 CD1 PHE A 16 8.402 2.667 20.550 1.00 12.38 C ANISOU 196 CD1 PHE A 16 2619 1015 1068 350 -282 -22 C ATOM 197 CD2 PHE A 16 6.433 1.529 21.181 1.00 12.86 C ANISOU 197 CD2 PHE A 16 2429 1523 934 323 -93 -55 C ATOM 198 CE1 PHE A 16 7.699 3.895 20.466 1.00 13.70 C ANISOU 198 CE1 PHE A 16 2934 1113 1157 188 -449 -43 C ATOM 199 CE2 PHE A 16 5.725 2.745 21.093 1.00 14.86 C ANISOU 199 CE2 PHE A 16 2492 2152 1000 729 53 -319 C ATOM 200 CZ PHE A 16 6.398 3.880 20.737 1.00 14.55 C ANISOU 200 CZ PHE A 16 2890 1578 1060 588 -425 -247 C ATOM 201 N ASP A 17 9.173 -0.816 24.017 1.00 11.01 N ANISOU 201 N ASP A 17 2478 673 1029 -98 119 152 N ATOM 202 CA ASP A 17 8.863 -0.720 25.440 1.00 11.79 C ANISOU 202 CA ASP A 17 2562 906 1009 -92 34 300 C ATOM 203 C ASP A 17 10.029 -0.105 26.211 1.00 11.26 C ANISOU 203 C ASP A 17 2474 753 1049 -40 53 496 C ATOM 204 O ASP A 17 9.831 0.775 27.048 1.00 11.53 O ANISOU 204 O ASP A 17 2652 863 863 -63 127 197 O ATOM 205 CB ASP A 17 8.500 -2.091 25.990 1.00 13.18 C ANISOU 205 CB ASP A 17 2841 971 1195 -144 71 262 C ATOM 206 CG ASP A 17 7.965 -2.004 27.383 1.00 15.52 C ANISOU 206 CG ASP A 17 3130 1282 1482 -277 228 479 C ATOM 207 OD1 ASP A 17 8.594 -2.575 28.277 1.00 21.98 O ANISOU 207 OD1 ASP A 17 3590 2933 1828 132 247 722 O ATOM 208 OD2 ASP A 17 6.941 -1.367 27.626 1.00 17.23 O ANISOU 208 OD2 ASP A 17 3416 1672 1457 25 485 380 O ATOM 209 N ASP A 18 11.248 -0.523 25.903 1.00 11.82 N ANISOU 209 N ASP A 18 2445 751 1292 64 30 379 N ATOM 210 CA ASP A 18 12.382 0.025 26.574 1.00 12.86 C ANISOU 210 CA ASP A 18 2401 1107 1375 162 -168 493 C ATOM 211 C ASP A 18 12.611 1.478 26.244 1.00 11.12 C ANISOU 211 C ASP A 18 2212 887 1123 124 -33 284 C ATOM 212 O ASP A 18 12.987 2.274 27.110 1.00 11.78 O ANISOU 212 O ASP A 18 2422 1142 910 92 -110 248 O ATOM 213 CB ASP A 18 13.623 -0.793 26.289 1.00 16.11 C ANISOU 213 CB ASP A 18 2596 1319 2205 160 13 582 C ATOM 214 CG ASP A 18 13.661 -2.098 27.163 1.00 25.09 C ANISOU 214 CG ASP A 18 3523 3010 2998 420 -253 869 C ATOM 215 OD1 ASP A 18 12.982 -2.238 28.168 1.00 32.08 O ANISOU 215 OD1 ASP A 18 4814 3044 4329 421 -34 1995 O ATOM 216 OD2 ASP A 18 14.296 -3.033 26.791 1.00 30.88 O ANISOU 216 OD2 ASP A 18 5332 2751 3647 331 -560 1705 O ATOM 217 N TYR A 19 12.371 1.880 24.996 1.00 9.83 N ANISOU 217 N TYR A 19 2184 758 792 -16 9 159 N ATOM 218 CA TYR A 19 12.411 3.288 24.642 1.00 9.41 C ANISOU 218 CA TYR A 19 2172 701 703 -64 0 172 C ATOM 219 C TYR A 19 11.418 4.096 25.462 1.00 9.30 C ANISOU 219 C TYR A 19 2105 875 552 -12 61 175 C ATOM 220 O TYR A 19 11.756 5.134 26.053 1.00 9.68 O ANISOU 220 O TYR A 19 2293 788 595 -126 -43 6 O ATOM 221 CB TYR A 19 12.182 3.465 23.137 1.00 9.51 C ANISOU 221 CB TYR A 19 2111 810 691 -84 44 -36 C ATOM 222 CG TYR A 19 11.983 4.904 22.721 1.00 9.38 C ANISOU 222 CG TYR A 19 2140 854 569 -51 91 -39 C ATOM 223 CD1 TYR A 19 13.065 5.792 22.649 1.00 9.35 C ANISOU 223 CD1 TYR A 19 2152 725 674 -163 41 29 C ATOM 224 CD2 TYR A 19 10.696 5.362 22.467 1.00 9.49 C ANISOU 224 CD2 TYR A 19 2185 852 567 -201 3 70 C ATOM 225 CE1 TYR A 19 12.837 7.138 22.354 1.00 9.45 C ANISOU 225 CE1 TYR A 19 2190 748 650 -184 84 39 C ATOM 226 CE2 TYR A 19 10.491 6.700 22.144 1.00 10.21 C ANISOU 226 CE2 TYR A 19 2047 1130 699 -63 4 63 C ATOM 227 CZ TYR A 19 11.552 7.571 22.085 1.00 9.62 C ANISOU 227 CZ TYR A 19 2260 882 512 -75 -27 -9 C ATOM 228 OH TYR A 19 11.323 8.911 21.794 1.00 10.61 O ANISOU 228 OH TYR A 19 2441 783 804 49 -28 151 O ATOM 229 N MET A 20 10.179 3.634 25.500 1.00 9.03 N ANISOU 229 N MET A 20 2168 658 604 -66 26 50 N ATOM 230 CA MET A 20 9.161 4.323 26.255 1.00 9.55 C ANISOU 230 CA MET A 20 2140 808 678 -63 27 167 C ATOM 231 C MET A 20 9.544 4.411 27.746 1.00 10.04 C ANISOU 231 C MET A 20 2265 937 611 -221 52 114 C ATOM 232 O MET A 20 9.317 5.441 28.385 1.00 10.52 O ANISOU 232 O MET A 20 2392 993 611 -207 -4 -40 O ATOM 233 CB MET A 20 7.779 3.697 26.102 1.00 9.70 C ANISOU 233 CB MET A 20 2179 902 602 -71 58 74 C ATOM 234 CG MET A 20 7.158 3.908 24.717 1.00 10.04 C ANISOU 234 CG MET A 20 2177 956 680 108 110 133 C ATOM 235 SD MET A 20 5.433 3.368 24.667 1.00 12.06 S ANISOU 235 SD MET A 20 2269 1571 742 -18 14 -31 S ATOM 236 CE MET A 20 5.672 1.577 24.691 1.00 13.30 C ANISOU 236 CE MET A 20 2340 1717 996 -209 -5 -87 C ATOM 237 N LYS A 21 10.103 3.344 28.312 1.00 10.62 N ANISOU 237 N LYS A 21 2404 1062 569 -103 59 199 N ATOM 238 CA LYS A 21 10.530 3.379 29.697 1.00 12.33 C ANISOU 238 CA LYS A 21 2672 1409 603 -270 65 362 C ATOM 239 C LYS A 21 11.571 4.457 29.892 1.00 12.82 C ANISOU 239 C LYS A 21 2653 1574 642 -213 -96 263 C ATOM 240 O LYS A 21 11.516 5.206 30.902 1.00 14.05 O ANISOU 240 O LYS A 21 3066 1569 701 -318 -79 131 O ATOM 241 CB LYS A 21 11.110 2.041 30.149 1.00 13.35 C ANISOU 241 CB LYS A 21 2803 1595 673 -110 20 542 C ATOM 242 CG LYS A 21 10.199 0.902 30.349 1.00 15.03 C ANISOU 242 CG LYS A 21 2778 1667 1265 -101 87 747 C ATOM 243 CD LYS A 21 10.880 -0.274 30.930 1.00 18.06 C ANISOU 243 CD LYS A 21 3284 1790 1786 96 75 904 C ATOM 244 CE LYS A 21 9.950 -1.349 31.235 1.00 22.74 C ANISOU 244 CE LYS A 21 3447 2534 2656 153 -50 1060 C ATOM 245 NZ LYS A 21 10.575 -2.433 31.880 1.00 27.32 N ANISOU 245 NZ LYS A 21 4121 2843 3416 317 -107 1185 N ATOM 246 N GLU A 22 12.515 4.555 28.971 1.00 12.32 N ANISOU 246 N GLU A 22 2532 1439 710 -253 -159 175 N ATOM 247 CA GLU A 22 13.595 5.507 29.102 1.00 13.16 C ANISOU 247 CA GLU A 22 2548 1651 800 -286 -209 178 C ATOM 248 C GLU A 22 13.034 6.950 29.038 1.00 12.69 C ANISOU 248 C GLU A 22 2605 1710 506 -473 -148 4 C ATOM 249 O GLU A 22 13.495 7.838 29.735 1.00 14.73 O ANISOU 249 O GLU A 22 2945 1785 866 -585 -321 -22 O ATOM 250 CB GLU A 22 14.667 5.257 28.045 1.00 13.57 C ANISOU 250 CB GLU A 22 2503 1607 1045 -261 -214 103 C ATOM 251 CG GLU A 22 16.019 5.747 28.354 1.00 16.53 C ANISOU 251 CG GLU A 22 2626 2180 1474 -132 -205 93 C ATOM 252 CD GLU A 22 16.758 4.901 29.432 1.00 16.69 C ANISOU 252 CD GLU A 22 2821 1787 1734 53 -375 532 C ATOM 253 OE1 GLU A 22 16.288 3.851 29.886 1.00 20.87 O ANISOU 253 OE1 GLU A 22 3491 2431 2006 77 -494 703 O ATOM 254 OE2 GLU A 22 17.902 5.317 29.772 1.00 21.94 O ANISOU 254 OE2 GLU A 22 3069 2977 2289 87 -547 -121 O ATOM 255 N VAL A 23 12.017 7.173 28.184 1.00 11.50 N ANISOU 255 N VAL A 23 2644 1063 663 -316 -88 49 N ATOM 256 CA VAL A 23 11.351 8.420 28.052 1.00 11.97 C ANISOU 256 CA VAL A 23 2721 1073 751 -336 -66 57 C ATOM 257 C VAL A 23 10.587 8.828 29.345 1.00 12.55 C ANISOU 257 C VAL A 23 2881 1235 650 -303 -23 -51 C ATOM 258 O VAL A 23 10.483 9.998 29.638 1.00 15.04 O ANISOU 258 O VAL A 23 3552 1125 1036 -317 212 -176 O ATOM 259 CB VAL A 23 10.409 8.402 26.822 1.00 11.61 C ANISOU 259 CB VAL A 23 2651 1008 750 -244 -90 48 C ATOM 260 CG1 VAL A 23 9.456 9.588 26.796 1.00 13.06 C ANISOU 260 CG1 VAL A 23 3000 896 1065 -174 -142 -43 C ATOM 261 CG2 VAL A 23 11.216 8.363 25.551 1.00 12.15 C ANISOU 261 CG2 VAL A 23 2783 1063 766 -77 36 71 C ATOM 262 N GLY A 24 10.101 7.830 30.057 1.00 12.38 N ANISOU 262 N GLY A 24 2830 1198 675 -451 17 -18 N ATOM 263 CA GLY A 24 9.353 8.021 31.287 1.00 12.95 C ANISOU 263 CA GLY A 24 2778 1436 704 -288 -38 -61 C ATOM 264 C GLY A 24 7.880 7.661 31.207 1.00 12.26 C ANISOU 264 C GLY A 24 2886 1167 604 -254 179 -95 C ATOM 265 O GLY A 24 7.122 8.023 32.106 1.00 14.56 O ANISOU 265 O GLY A 24 3131 1532 867 -407 239 -318 O ATOM 266 N VAL A 25 7.478 6.899 30.208 1.00 10.90 N ANISOU 266 N VAL A 25 2605 829 708 -107 48 -13 N ATOM 267 CA VAL A 25 6.092 6.532 30.060 1.00 11.00 C ANISOU 267 CA VAL A 25 2445 895 837 -32 64 -43 C ATOM 268 C VAL A 25 5.733 5.504 31.104 1.00 11.44 C ANISOU 268 C VAL A 25 2521 1118 706 -112 -5 -79 C ATOM 269 O VAL A 25 6.472 4.547 31.339 1.00 12.12 O ANISOU 269 O VAL A 25 2773 1064 767 -213 -25 128 O ATOM 270 CB VAL A 25 5.851 5.935 28.656 1.00 10.88 C ANISOU 270 CB VAL A 25 2426 971 735 -9 -38 11 C ATOM 271 CG1 VAL A 25 4.397 5.637 28.454 1.00 12.31 C ANISOU 271 CG1 VAL A 25 2468 1200 1007 -66 -45 -79 C ATOM 272 CG2 VAL A 25 6.360 6.887 27.558 1.00 12.31 C ANISOU 272 CG2 VAL A 25 2924 890 860 -9 -104 204 C ATOM 273 N GLY A 26 4.569 5.670 31.724 1.00 12.98 N ANISOU 273 N GLY A 26 2541 1478 911 -267 75 -193 N ATOM 274 CA GLY A 26 4.087 4.751 32.739 1.00 13.62 C ANISOU 274 CA GLY A 26 2636 1785 752 -395 154 -142 C ATOM 275 C GLY A 26 3.581 3.438 32.210 1.00 12.39 C ANISOU 275 C GLY A 26 2495 1564 647 -433 78 -130 C ATOM 276 O GLY A 26 3.327 3.269 31.040 1.00 12.67 O ANISOU 276 O GLY A 26 2776 1458 576 -413 37 -119 O ATOM 277 N PHE A 27 3.363 2.506 33.123 1.00 12.81 N ANISOU 277 N PHE A 27 2728 1636 503 -397 -27 -29 N ATOM 278 CA PHE A 27 3.090 1.127 32.763 1.00 12.61 C ANISOU 278 CA PHE A 27 2588 1502 698 -258 22 60 C ATOM 279 C PHE A 27 1.858 1.008 31.844 1.00 11.87 C ANISOU 279 C PHE A 27 2588 1223 698 -376 72 146 C ATOM 280 O PHE A 27 1.927 0.390 30.776 1.00 12.26 O ANISOU 280 O PHE A 27 2676 1353 627 -334 -68 40 O ATOM 281 CB PHE A 27 2.851 0.303 34.049 1.00 13.47 C ANISOU 281 CB PHE A 27 2658 1655 804 -155 16 193 C ATOM 282 CG PHE A 27 2.447 -1.138 33.772 1.00 13.89 C ANISOU 282 CG PHE A 27 2756 1765 754 -359 -125 352 C ATOM 283 CD1 PHE A 27 3.401 -2.133 33.652 1.00 16.14 C ANISOU 283 CD1 PHE A 27 3055 1886 1189 -323 -89 265 C ATOM 284 CD2 PHE A 27 1.124 -1.472 33.646 1.00 16.01 C ANISOU 284 CD2 PHE A 27 2827 1873 1382 -264 -441 814 C ATOM 285 CE1 PHE A 27 3.012 -3.463 33.390 1.00 17.39 C ANISOU 285 CE1 PHE A 27 3344 1684 1576 -281 48 318 C ATOM 286 CE2 PHE A 27 0.747 -2.807 33.364 1.00 17.02 C ANISOU 286 CE2 PHE A 27 3061 2117 1287 -614 -461 724 C ATOM 287 CZ PHE A 27 1.688 -3.739 33.210 1.00 17.73 C ANISOU 287 CZ PHE A 27 3460 1995 1278 -643 -349 352 C ATOM 288 N ALA A 28 0.718 1.556 32.257 1.00 12.55 N ANISOU 288 N ALA A 28 2706 1349 710 -285 69 76 N ATOM 289 CA ALA A 28 -0.507 1.305 31.490 1.00 12.99 C ANISOU 289 CA ALA A 28 2601 1355 979 -321 115 71 C ATOM 290 C ALA A 28 -0.399 1.921 30.114 1.00 12.36 C ANISOU 290 C ALA A 28 2563 1174 957 -138 88 54 C ATOM 291 O ALA A 28 -0.860 1.339 29.115 1.00 13.77 O ANISOU 291 O ALA A 28 2663 1604 964 -397 -138 10 O ATOM 292 CB ALA A 28 -1.710 1.818 32.214 1.00 15.15 C ANISOU 292 CB ALA A 28 2839 1495 1420 -181 338 198 C ATOM 293 N THR A 29 0.150 3.141 30.017 1.00 11.96 N ANISOU 293 N THR A 29 2603 1071 869 -202 -9 -12 N ATOM 294 CA THR A 29 0.326 3.770 28.739 1.00 11.78 C ANISOU 294 CA THR A 29 2500 1045 930 -166 -148 58 C ATOM 295 C THR A 29 1.273 2.943 27.868 1.00 11.57 C ANISOU 295 C THR A 29 2401 1100 893 -328 10 -51 C ATOM 296 O THR A 29 1.005 2.778 26.683 1.00 12.24 O ANISOU 296 O THR A 29 2649 1334 666 -256 -148 -80 O ATOM 297 CB THR A 29 0.794 5.228 28.879 1.00 12.80 C ANISOU 297 CB THR A 29 2571 1141 1151 -78 -152 70 C ATOM 298 OG1 THR A 29 -0.196 5.969 29.619 1.00 15.68 O ANISOU 298 OG1 THR A 29 2907 1401 1649 4 132 -11 O ATOM 299 CG2 THR A 29 0.998 5.868 27.542 1.00 14.91 C ANISOU 299 CG2 THR A 29 2978 1129 1557 -170 -257 414 C ATOM 300 N ARG A 30 2.371 2.427 28.423 1.00 11.10 N ANISOU 300 N ARG A 30 2400 1160 656 -286 -122 50 N ATOM 301 CA ARG A 30 3.274 1.609 27.607 1.00 10.80 C ANISOU 301 CA ARG A 30 2270 1309 522 -219 15 54 C ATOM 302 C ARG A 30 2.560 0.403 27.070 1.00 10.58 C ANISOU 302 C ARG A 30 2235 1191 594 -169 -125 10 C ATOM 303 O ARG A 30 2.787 0.029 25.914 1.00 11.08 O ANISOU 303 O ARG A 30 2280 1278 653 -205 -16 64 O ATOM 304 CB ARG A 30 4.542 1.090 28.359 1.00 11.58 C ANISOU 304 CB ARG A 30 2493 1302 602 -313 -59 98 C ATOM 305 CG ARG A 30 5.499 2.191 28.743 1.00 11.48 C ANISOU 305 CG ARG A 30 2388 1296 677 -326 68 97 C ATOM 306 CD ARG A 30 6.880 1.648 29.055 1.00 11.25 C ANISOU 306 CD ARG A 30 2378 1239 658 -208 40 109 C ATOM 307 NE ARG A 30 6.837 0.474 29.932 1.00 11.68 N ANISOU 307 NE ARG A 30 2556 1221 658 -185 -3 62 N ATOM 308 CZ ARG A 30 6.692 0.518 31.246 1.00 11.21 C ANISOU 308 CZ ARG A 30 2448 1070 740 -114 67 201 C ATOM 309 NH1 ARG A 30 6.573 1.674 31.899 1.00 12.02 N ANISOU 309 NH1 ARG A 30 2745 1209 612 -144 26 252 N ATOM 310 NH2 ARG A 30 6.645 -0.613 31.916 1.00 13.22 N ANISOU 310 NH2 ARG A 30 3027 1276 718 18 77 74 N ATOM 311 N LYS A 31 1.762 -0.261 27.889 1.00 10.98 N ANISOU 311 N LYS A 31 2344 1174 653 -273 18 39 N ATOM 312 CA LYS A 31 1.108 -1.477 27.424 1.00 11.63 C ANISOU 312 CA LYS A 31 2411 1124 882 -155 -26 -129 C ATOM 313 C LYS A 31 0.142 -1.209 26.272 1.00 11.58 C ANISOU 313 C LYS A 31 2199 1328 871 -236 -46 -131 C ATOM 314 O LYS A 31 0.167 -1.918 25.250 1.00 13.40 O ANISOU 314 O LYS A 31 2402 1692 997 -145 -62 -456 O ATOM 315 CB LYS A 31 0.387 -2.212 28.549 1.00 12.61 C ANISOU 315 CB LYS A 31 2675 1189 925 -273 75 -77 C ATOM 316 CG LYS A 31 1.296 -2.704 29.628 1.00 16.33 C ANISOU 316 CG LYS A 31 3217 1710 1276 -178 -114 300 C ATOM 317 CD LYS A 31 2.238 -3.759 29.120 1.00 21.34 C ANISOU 317 CD LYS A 31 3505 2529 2074 465 -240 863 C ATOM 318 CE LYS A 31 3.562 -3.896 29.920 1.00 26.22 C ANISOU 318 CE LYS A 31 3737 3589 2636 349 -112 -38 C ATOM 319 NZ LYS A 31 4.748 -4.334 29.083 1.00 30.32 N ANISOU 319 NZ LYS A 31 3991 4060 3469 364 235 -162 N ATOM 320 N VAL A 32 -0.671 -0.171 26.408 1.00 11.43 N ANISOU 320 N VAL A 32 2149 1380 810 -108 -22 -282 N ATOM 321 CA AVAL A 32 -1.660 0.192 25.377 0.50 12.53 C ANISOU 321 CA AVAL A 32 2210 1532 1018 -103 -64 -337 C ATOM 322 CA BVAL A 32 -1.631 0.077 25.347 0.50 12.94 C ANISOU 322 CA BVAL A 32 2199 1681 1036 -144 -72 -258 C ATOM 323 C VAL A 32 -0.962 0.740 24.150 1.00 11.86 C ANISOU 323 C VAL A 32 2112 1525 867 -36 -110 -245 C ATOM 324 O VAL A 32 -1.307 0.426 23.004 1.00 12.88 O ANISOU 324 O VAL A 32 2218 1870 803 -91 -93 -398 O ATOM 325 CB AVAL A 32 -2.722 1.220 25.925 0.50 12.84 C ANISOU 325 CB AVAL A 32 2195 1406 1276 60 18 -402 C ATOM 326 CB BVAL A 32 -2.886 0.816 25.868 0.50 13.69 C ANISOU 326 CB BVAL A 32 2119 1992 1091 -70 24 -302 C ATOM 327 CG1AVAL A 32 -3.664 1.659 24.826 0.50 13.83 C ANISOU 327 CG1AVAL A 32 2155 1737 1363 147 25 -512 C ATOM 328 CG1BVAL A 32 -3.595 -0.019 26.954 0.50 14.17 C ANISOU 328 CG1BVAL A 32 2139 1719 1524 -6 291 -308 C ATOM 329 CG2AVAL A 32 -3.556 0.581 27.048 0.50 15.72 C ANISOU 329 CG2AVAL A 32 2575 1905 1493 -57 32 -260 C ATOM 330 CG2BVAL A 32 -2.505 2.218 26.389 0.50 15.14 C ANISOU 330 CG2BVAL A 32 2546 1878 1326 79 -92 -352 C ATOM 331 N ALA A 33 0.005 1.622 24.351 1.00 11.84 N ANISOU 331 N ALA A 33 2280 1456 762 -1 -240 -91 N ATOM 332 CA ALA A 33 0.706 2.222 23.224 1.00 11.94 C ANISOU 332 CA ALA A 33 2462 1374 701 31 -204 81 C ATOM 333 C ALA A 33 1.480 1.179 22.445 1.00 12.31 C ANISOU 333 C ALA A 33 2429 1487 760 -82 -177 167 C ATOM 334 O ALA A 33 1.598 1.265 21.225 1.00 13.05 O ANISOU 334 O ALA A 33 2825 1518 614 -84 -94 180 O ATOM 335 CB ALA A 33 1.620 3.314 23.691 1.00 13.26 C ANISOU 335 CB ALA A 33 2637 1431 969 -164 -149 187 C ATOM 336 N GLY A 34 2.052 0.184 23.129 1.00 12.46 N ANISOU 336 N GLY A 34 2423 1673 638 188 -1 162 N ATOM 337 CA GLY A 34 2.834 -0.826 22.459 1.00 13.03 C ANISOU 337 CA GLY A 34 2312 1815 824 211 2 244 C ATOM 338 C GLY A 34 2.026 -1.755 21.563 1.00 11.90 C ANISOU 338 C GLY A 34 2351 1452 716 263 99 180 C ATOM 339 O GLY A 34 2.592 -2.277 20.608 1.00 14.67 O ANISOU 339 O GLY A 34 2376 2156 1042 217 163 -116 O ATOM 340 N MET A 35 0.722 -1.883 21.779 1.00 11.72 N ANISOU 340 N MET A 35 2475 1164 814 113 351 385 N ATOM 341 CA MET A 35 -0.125 -2.685 20.890 1.00 11.34 C ANISOU 341 CA MET A 35 2376 1021 909 21 186 190 C ATOM 342 C MET A 35 -0.419 -2.008 19.567 1.00 10.83 C ANISOU 342 C MET A 35 2165 934 1015 -27 225 412 C ATOM 343 O MET A 35 -0.727 -2.670 18.558 1.00 12.85 O ANISOU 343 O MET A 35 2592 1057 1232 -196 -40 248 O ATOM 344 CB MET A 35 -1.456 -3.028 21.555 1.00 12.52 C ANISOU 344 CB MET A 35 2438 808 1509 48 337 350 C ATOM 345 CG MET A 35 -1.351 -3.895 22.782 1.00 12.67 C ANISOU 345 CG MET A 35 2873 858 1081 -300 396 234 C ATOM 346 SD MET A 35 -0.667 -5.500 22.482 1.00 12.89 S ANISOU 346 SD MET A 35 2849 969 1080 106 225 302 S ATOM 347 CE MET A 35 -1.632 -6.211 21.303 1.00 18.60 C ANISOU 347 CE MET A 35 4103 1651 1310 112 -116 640 C ATOM 348 N ALA A 36 -0.401 -0.685 19.543 1.00 10.90 N ANISOU 348 N ALA A 36 2295 861 985 -111 53 418 N ATOM 349 CA ALA A 36 -0.950 0.020 18.401 1.00 11.20 C ANISOU 349 CA ALA A 36 2118 1116 1018 -131 117 433 C ATOM 350 C ALA A 36 -0.122 -0.198 17.154 1.00 10.87 C ANISOU 350 C ALA A 36 2164 1102 861 -200 99 311 C ATOM 351 O ALA A 36 1.114 -0.292 17.188 1.00 12.63 O ANISOU 351 O ALA A 36 2117 1743 938 -102 57 325 O ATOM 352 CB ALA A 36 -0.999 1.488 18.719 1.00 13.76 C ANISOU 352 CB ALA A 36 2882 1151 1196 103 101 388 C ATOM 353 N LYS A 37 -0.808 -0.265 16.039 1.00 10.99 N ANISOU 353 N LYS A 37 2142 1063 969 -222 -16 291 N ATOM 354 CA LYS A 37 -0.209 -0.419 14.708 1.00 11.96 C ANISOU 354 CA LYS A 37 2470 1126 944 -215 106 101 C ATOM 355 C LYS A 37 -0.706 0.763 13.881 1.00 11.43 C ANISOU 355 C LYS A 37 2318 1235 787 -261 55 177 C ATOM 356 O LYS A 37 -1.624 0.624 13.099 1.00 13.17 O ANISOU 356 O LYS A 37 2389 1589 1022 -452 -176 334 O ATOM 357 CB LYS A 37 -0.594 -1.768 14.039 1.00 14.51 C ANISOU 357 CB LYS A 37 2757 1426 1330 -195 63 0 C ATOM 358 CG LYS A 37 -0.012 -2.965 14.746 1.00 17.56 C ANISOU 358 CG LYS A 37 3141 1271 2259 -147 303 132 C ATOM 359 CD LYS A 37 1.472 -3.042 14.523 1.00 20.40 C ANISOU 359 CD LYS A 37 3371 2445 1932 130 100 415 C ATOM 360 CE LYS A 37 2.023 -4.401 14.791 1.00 24.82 C ANISOU 360 CE LYS A 37 3864 2877 2686 246 193 290 C ATOM 361 NZ LYS A 37 1.837 -4.755 16.175 1.00 25.82 N ANISOU 361 NZ LYS A 37 4039 2842 2927 483 292 669 N ATOM 362 N PRO A 38 -0.147 1.927 14.093 1.00 10.97 N ANISOU 362 N PRO A 38 2350 1055 763 -171 49 73 N ATOM 363 CA PRO A 38 -0.721 3.124 13.474 1.00 12.07 C ANISOU 363 CA PRO A 38 2517 1264 805 -119 204 164 C ATOM 364 C PRO A 38 -0.570 3.175 11.976 1.00 11.49 C ANISOU 364 C PRO A 38 2438 1076 851 -248 233 46 C ATOM 365 O PRO A 38 0.329 2.585 11.389 1.00 12.07 O ANISOU 365 O PRO A 38 2565 1137 884 -215 282 51 O ATOM 366 CB PRO A 38 0.092 4.285 14.101 1.00 13.86 C ANISOU 366 CB PRO A 38 3020 1309 938 -142 127 -241 C ATOM 367 CG PRO A 38 0.750 3.759 15.183 1.00 17.49 C ANISOU 367 CG PRO A 38 3123 1567 1952 -408 -223 35 C ATOM 368 CD PRO A 38 0.926 2.304 15.013 1.00 11.98 C ANISOU 368 CD PRO A 38 2411 1297 844 -263 95 32 C ATOM 369 N ASN A 39 -1.440 3.971 11.381 1.00 11.34 N ANISOU 369 N ASN A 39 2603 945 760 -91 278 179 N ATOM 370 CA ASN A 39 -1.268 4.481 10.049 1.00 12.96 C ANISOU 370 CA ASN A 39 3202 869 853 -12 262 67 C ATOM 371 C ASN A 39 -0.770 5.879 10.107 1.00 13.97 C ANISOU 371 C ASN A 39 3517 878 913 -229 515 -104 C ATOM 372 O ASN A 39 -1.292 6.707 10.836 1.00 19.67 O ANISOU 372 O ASN A 39 4280 1146 2044 -571 1476 -393 O ATOM 373 CB ASN A 39 -2.586 4.492 9.335 1.00 16.48 C ANISOU 373 CB ASN A 39 3637 1508 1116 106 -303 74 C ATOM 374 CG ASN A 39 -2.760 3.288 8.555 1.00 20.91 C ANISOU 374 CG ASN A 39 3712 2108 2123 106 -189 115 C ATOM 375 OD1 ASN A 39 -2.484 2.168 9.008 1.00 25.82 O ANISOU 375 OD1 ASN A 39 4831 2195 2782 -124 -714 -432 O ATOM 376 ND2 ASN A 39 -3.130 3.493 7.322 1.00 25.78 N ANISOU 376 ND2 ASN A 39 4068 3738 1986 758 -589 -866 N ATOM 377 N MET A 40 0.281 6.144 9.372 1.00 13.14 N ANISOU 377 N MET A 40 3458 728 804 -158 459 -29 N ATOM 378 CA MET A 40 0.877 7.447 9.346 1.00 12.09 C ANISOU 378 CA MET A 40 3020 778 794 -47 353 0 C ATOM 379 C MET A 40 0.752 8.027 7.982 1.00 11.69 C ANISOU 379 C MET A 40 3071 636 735 -217 339 32 C ATOM 380 O MET A 40 1.133 7.396 6.996 1.00 13.11 O ANISOU 380 O MET A 40 3430 727 823 107 437 86 O ATOM 381 CB MET A 40 2.315 7.278 9.733 1.00 12.74 C ANISOU 381 CB MET A 40 3241 803 796 -206 151 86 C ATOM 382 CG MET A 40 3.132 8.555 9.621 1.00 14.05 C ANISOU 382 CG MET A 40 3110 985 1242 -106 -76 312 C ATOM 383 SD MET A 40 4.820 8.449 10.205 1.00 15.72 S ANISOU 383 SD MET A 40 3585 1009 1377 -138 -125 -15 S ATOM 384 CE MET A 40 5.478 7.098 9.278 1.00 16.69 C ANISOU 384 CE MET A 40 3125 1524 1693 -64 -30 118 C ATOM 385 N ILE A 41 0.223 9.234 7.921 1.00 11.50 N ANISOU 385 N ILE A 41 2900 657 810 -184 273 -40 N ATOM 386 CA ILE A 41 -0.003 9.951 6.687 1.00 11.47 C ANISOU 386 CA ILE A 41 2694 748 913 -73 149 -57 C ATOM 387 C ILE A 41 0.917 11.142 6.679 1.00 9.94 C ANISOU 387 C ILE A 41 2631 523 622 -141 -62 66 C ATOM 388 O ILE A 41 0.855 11.985 7.568 1.00 11.18 O ANISOU 388 O ILE A 41 2791 712 745 -279 168 -102 O ATOM 389 CB ILE A 41 -1.510 10.385 6.520 1.00 13.81 C ANISOU 389 CB ILE A 41 2656 1141 1450 -208 -4 -287 C ATOM 390 CG1 ILE A 41 -2.488 9.207 6.598 1.00 18.00 C ANISOU 390 CG1 ILE A 41 2884 1718 2235 -262 -85 -426 C ATOM 391 CG2 ILE A 41 -1.725 11.127 5.214 1.00 16.82 C ANISOU 391 CG2 ILE A 41 3002 1667 1720 -104 -292 -72 C ATOM 392 CD1 ILE A 41 -3.963 9.672 6.711 1.00 22.89 C ANISOU 392 CD1 ILE A 41 3224 2507 2964 124 -257 -278 C ATOM 393 N ILE A 42 1.767 11.225 5.669 1.00 9.92 N ANISOU 393 N ILE A 42 2525 652 589 -103 55 -15 N ATOM 394 CA ILE A 42 2.715 12.315 5.533 1.00 9.31 C ANISOU 394 CA ILE A 42 2403 588 545 -97 53 -28 C ATOM 395 C ILE A 42 2.364 13.062 4.258 1.00 9.28 C ANISOU 395 C ILE A 42 2404 463 659 -98 -1 2 C ATOM 396 O ILE A 42 2.232 12.467 3.196 1.00 9.99 O ANISOU 396 O ILE A 42 2669 617 508 -102 -78 -55 O ATOM 397 CB ILE A 42 4.181 11.810 5.493 1.00 9.55 C ANISOU 397 CB ILE A 42 2503 664 460 -32 -13 -7 C ATOM 398 CG1 ILE A 42 4.489 11.042 6.789 1.00 10.32 C ANISOU 398 CG1 ILE A 42 2579 737 605 33 -30 38 C ATOM 399 CG2 ILE A 42 5.152 12.982 5.276 1.00 10.54 C ANISOU 399 CG2 ILE A 42 2483 733 787 -27 4 11 C ATOM 400 CD1 ILE A 42 5.904 10.487 6.821 1.00 12.47 C ANISOU 400 CD1 ILE A 42 2783 1118 835 170 -183 127 C ATOM 401 N SER A 43 2.240 14.376 4.371 1.00 9.47 N ANISOU 401 N SER A 43 2475 614 508 -28 -92 36 N ATOM 402 CA SER A 43 1.925 15.223 3.244 1.00 10.36 C ANISOU 402 CA SER A 43 2589 670 675 19 -110 8 C ATOM 403 C SER A 43 2.711 16.491 3.294 1.00 9.83 C ANISOU 403 C SER A 43 2645 550 539 174 -165 23 C ATOM 404 O SER A 43 3.208 16.905 4.358 1.00 10.47 O ANISOU 404 O SER A 43 2776 717 484 -57 -82 51 O ATOM 405 CB SER A 43 0.445 15.508 3.224 1.00 13.03 C ANISOU 405 CB SER A 43 2742 1042 1165 -143 -227 286 C ATOM 406 OG SER A 43 -0.035 16.148 4.344 1.00 15.47 O ANISOU 406 OG SER A 43 2894 1387 1596 140 -264 115 O ATOM 407 N VAL A 44 2.828 17.134 2.157 1.00 10.51 N ANISOU 407 N VAL A 44 2895 593 503 5 -186 35 N ATOM 408 CA VAL A 44 3.544 18.406 2.038 1.00 11.42 C ANISOU 408 CA VAL A 44 2977 741 619 3 -158 148 C ATOM 409 C VAL A 44 2.711 19.358 1.242 1.00 11.40 C ANISOU 409 C VAL A 44 3078 765 485 -48 -277 68 C ATOM 410 O VAL A 44 2.133 18.989 0.216 1.00 15.21 O ANISOU 410 O VAL A 44 4113 851 816 -86 -746 79 O ATOM 411 CB VAL A 44 4.893 18.211 1.341 1.00 13.55 C ANISOU 411 CB VAL A 44 3026 1007 1113 -54 -185 230 C ATOM 412 CG1 VAL A 44 5.658 19.549 1.181 1.00 20.51 C ANISOU 412 CG1 VAL A 44 3513 1506 2772 -248 -38 384 C ATOM 413 CG2 VAL A 44 5.785 17.272 2.076 1.00 15.81 C ANISOU 413 CG2 VAL A 44 2943 1482 1580 -226 -128 -46 C ATOM 414 N ASN A 45 2.656 20.600 1.693 1.00 10.53 N ANISOU 414 N ASN A 45 2747 672 583 -47 -213 67 N ATOM 415 CA ASN A 45 1.947 21.654 0.998 1.00 10.63 C ANISOU 415 CA ASN A 45 2691 797 550 -34 -166 59 C ATOM 416 C ASN A 45 2.796 22.904 1.131 1.00 10.68 C ANISOU 416 C ASN A 45 2771 711 576 21 -159 118 C ATOM 417 O ASN A 45 2.922 23.467 2.212 1.00 10.38 O ANISOU 417 O ASN A 45 2526 709 708 -25 -171 116 O ATOM 418 CB ASN A 45 0.576 21.824 1.585 1.00 11.88 C ANISOU 418 CB ASN A 45 2761 866 883 -173 -253 145 C ATOM 419 CG ASN A 45 -0.291 22.832 0.893 1.00 11.42 C ANISOU 419 CG ASN A 45 2497 976 865 -52 -398 69 C ATOM 420 OD1 ASN A 45 -1.545 22.647 0.799 1.00 13.14 O ANISOU 420 OD1 ASN A 45 2641 1175 1176 -173 -203 -34 O ATOM 421 ND2 ASN A 45 0.304 23.874 0.401 1.00 12.10 N ANISOU 421 ND2 ASN A 45 2598 818 1180 -143 -595 339 N ATOM 422 N GLY A 46 3.486 23.263 0.058 1.00 12.47 N ANISOU 422 N GLY A 46 3102 1004 629 -272 -65 203 N ATOM 423 CA GLY A 46 4.442 24.372 0.154 1.00 13.14 C ANISOU 423 CA GLY A 46 2963 1182 846 -249 43 274 C ATOM 424 C GLY A 46 5.577 24.019 1.099 1.00 12.53 C ANISOU 424 C GLY A 46 2713 1120 927 -203 74 313 C ATOM 425 O GLY A 46 6.167 22.941 0.971 1.00 14.73 O ANISOU 425 O GLY A 46 2925 1421 1248 -112 181 86 O ATOM 426 N ASP A 47 5.828 24.869 2.066 1.00 11.55 N ANISOU 426 N ASP A 47 2629 970 789 -146 103 222 N ATOM 427 CA ASP A 47 6.863 24.629 3.054 1.00 12.37 C ANISOU 427 CA ASP A 47 2455 1287 958 -168 65 270 C ATOM 428 C ASP A 47 6.361 23.815 4.239 1.00 10.38 C ANISOU 428 C ASP A 47 2350 842 750 11 31 92 C ATOM 429 O ASP A 47 7.162 23.510 5.133 1.00 11.88 O ANISOU 429 O ASP A 47 2271 1309 934 4 -54 212 O ATOM 430 CB ASP A 47 7.408 25.965 3.600 1.00 14.44 C ANISOU 430 CB ASP A 47 2781 1430 1275 -332 -200 379 C ATOM 431 CG ASP A 47 8.081 26.803 2.582 1.00 19.85 C ANISOU 431 CG ASP A 47 3323 1981 2237 -629 -234 404 C ATOM 432 OD1 ASP A 47 8.629 26.224 1.631 1.00 25.00 O ANISOU 432 OD1 ASP A 47 3530 3400 2567 -1119 617 655 O ATOM 433 OD2 ASP A 47 8.086 28.040 2.787 1.00 27.34 O ANISOU 433 OD2 ASP A 47 4871 2320 3196 -969 -299 970 O ATOM 434 N VAL A 48 5.058 23.531 4.309 1.00 9.43 N ANISOU 434 N VAL A 48 2221 661 700 -30 -51 141 N ATOM 435 CA VAL A 48 4.506 22.894 5.472 1.00 9.04 C ANISOU 435 CA VAL A 48 2207 669 556 -84 24 146 C ATOM 436 C VAL A 48 4.405 21.400 5.273 1.00 8.76 C ANISOU 436 C VAL A 48 2261 630 437 -54 -28 111 C ATOM 437 O VAL A 48 3.760 20.910 4.358 1.00 10.19 O ANISOU 437 O VAL A 48 2504 761 604 -65 -301 101 O ATOM 438 CB VAL A 48 3.137 23.467 5.807 1.00 10.45 C ANISOU 438 CB VAL A 48 2201 908 860 73 66 176 C ATOM 439 CG1 VAL A 48 2.575 22.834 7.083 1.00 11.66 C ANISOU 439 CG1 VAL A 48 2601 910 918 64 206 142 C ATOM 440 CG2 VAL A 48 3.166 24.979 5.977 1.00 12.74 C ANISOU 440 CG2 VAL A 48 2686 878 1275 224 125 144 C ATOM 441 N ILE A 49 5.007 20.655 6.183 1.00 8.50 N ANISOU 441 N ILE A 49 2153 635 441 -85 -70 11 N ATOM 442 CA ILE A 49 4.912 19.200 6.249 1.00 8.61 C ANISOU 442 CA ILE A 49 2142 652 477 -77 -98 -8 C ATOM 443 C ILE A 49 3.939 18.823 7.343 1.00 8.10 C ANISOU 443 C ILE A 49 2090 497 490 -49 -112 11 C ATOM 444 O ILE A 49 3.981 19.402 8.437 1.00 8.93 O ANISOU 444 O ILE A 49 2218 675 499 -153 33 -52 O ATOM 445 CB ILE A 49 6.307 18.600 6.523 1.00 9.22 C ANISOU 445 CB ILE A 49 2178 836 488 -75 -43 -61 C ATOM 446 CG1 ILE A 49 7.325 19.031 5.475 1.00 10.76 C ANISOU 446 CG1 ILE A 49 2261 1133 691 -59 129 -87 C ATOM 447 CG2 ILE A 49 6.272 17.072 6.620 1.00 10.44 C ANISOU 447 CG2 ILE A 49 2377 761 826 81 -130 11 C ATOM 448 CD1 ILE A 49 8.792 18.744 5.886 1.00 15.70 C ANISOU 448 CD1 ILE A 49 2310 2222 1430 65 178 198 C ATOM 449 N THR A 50 3.072 17.873 7.055 1.00 8.47 N ANISOU 449 N THR A 50 2239 552 427 -45 -52 23 N ATOM 450 CA THR A 50 2.163 17.328 8.049 1.00 8.67 C ANISOU 450 CA THR A 50 2121 710 463 -150 -6 -42 C ATOM 451 C THR A 50 2.413 15.850 8.211 1.00 8.40 C ANISOU 451 C THR A 50 2101 565 525 -108 13 75 C ATOM 452 O THR A 50 2.496 15.105 7.233 1.00 9.64 O ANISOU 452 O THR A 50 2643 524 495 -123 31 -6 O ATOM 453 CB THR A 50 0.692 17.633 7.670 1.00 9.97 C ANISOU 453 CB THR A 50 2304 820 662 -218 -15 -55 C ATOM 454 OG1 THR A 50 0.478 19.022 7.556 1.00 11.03 O ANISOU 454 OG1 THR A 50 2284 899 1007 -2 -48 134 O ATOM 455 CG2 THR A 50 -0.267 17.047 8.668 1.00 12.07 C ANISOU 455 CG2 THR A 50 2415 1125 1044 -244 65 -98 C ATOM 456 N ILE A 51 2.513 15.420 9.473 1.00 8.65 N ANISOU 456 N ILE A 51 2237 512 536 -101 9 25 N ATOM 457 CA ILE A 51 2.637 13.999 9.841 1.00 9.28 C ANISOU 457 CA ILE A 51 2372 590 561 -169 34 -62 C ATOM 458 C ILE A 51 1.473 13.680 10.770 1.00 9.26 C ANISOU 458 C ILE A 51 2391 594 531 -82 113 86 C ATOM 459 O ILE A 51 1.391 14.225 11.877 1.00 9.97 O ANISOU 459 O ILE A 51 2422 759 607 -80 123 -29 O ATOM 460 CB ILE A 51 3.946 13.669 10.498 1.00 9.77 C ANISOU 460 CB ILE A 51 2366 695 650 -25 90 -89 C ATOM 461 CG1 ILE A 51 5.143 14.022 9.603 1.00 10.57 C ANISOU 461 CG1 ILE A 51 2425 755 836 -97 117 -129 C ATOM 462 CG2 ILE A 51 3.993 12.190 10.904 1.00 11.70 C ANISOU 462 CG2 ILE A 51 2815 664 967 40 149 3 C ATOM 463 CD1 ILE A 51 6.484 13.810 10.226 1.00 13.06 C ANISOU 463 CD1 ILE A 51 2374 1067 1521 191 -81 -180 C ATOM 464 N LYS A 52 0.550 12.854 10.304 1.00 10.05 N ANISOU 464 N LYS A 52 2496 674 648 -214 203 -34 N ATOM 465 CA LYS A 52 -0.600 12.426 11.050 1.00 11.64 C ANISOU 465 CA LYS A 52 2575 919 927 -331 314 -171 C ATOM 466 C LYS A 52 -0.435 10.964 11.406 1.00 11.71 C ANISOU 466 C LYS A 52 2804 693 951 -312 425 -157 C ATOM 467 O LYS A 52 -0.109 10.175 10.532 1.00 15.25 O ANISOU 467 O LYS A 52 3970 692 1132 -348 808 -86 O ATOM 468 CB LYS A 52 -1.855 12.637 10.209 1.00 14.88 C ANISOU 468 CB LYS A 52 2516 1844 1291 -258 238 -313 C ATOM 469 CG LYS A 52 -3.213 12.466 10.792 1.00 19.18 C ANISOU 469 CG LYS A 52 3049 2230 2006 -448 194 115 C ATOM 470 CD LYS A 52 -4.243 12.820 9.694 1.00 25.59 C ANISOU 470 CD LYS A 52 3348 3542 2833 -76 -244 -147 C ATOM 471 CE LYS A 52 -4.021 14.264 9.112 1.00 30.78 C ANISOU 471 CE LYS A 52 3821 4056 3816 -343 -253 -230 C ATOM 472 NZ LYS A 52 -3.131 14.480 7.902 1.00 34.71 N ANISOU 472 NZ LYS A 52 3945 4650 4593 -100 35 -335 N ATOM 473 N SER A 53 -0.741 10.607 12.641 1.00 11.33 N ANISOU 473 N SER A 53 2647 816 841 -246 346 -114 N ATOM 474 CA SER A 53 -0.761 9.236 13.071 1.00 11.41 C ANISOU 474 CA SER A 53 2530 770 1033 -248 398 25 C ATOM 475 C SER A 53 -2.196 8.902 13.486 1.00 11.01 C ANISOU 475 C SER A 53 2645 775 762 -249 303 -139 C ATOM 476 O SER A 53 -2.739 9.529 14.387 1.00 12.91 O ANISOU 476 O SER A 53 2660 1032 1211 -381 448 -147 O ATOM 477 CB SER A 53 0.176 9.059 14.269 1.00 13.05 C ANISOU 477 CB SER A 53 2481 943 1531 -138 294 -43 C ATOM 478 OG SER A 53 0.171 7.708 14.741 1.00 15.17 O ANISOU 478 OG SER A 53 3001 1255 1508 -205 193 58 O ATOM 479 N GLU A 54 -2.778 7.925 12.831 1.00 11.98 N ANISOU 479 N GLU A 54 2604 1128 818 -346 333 -89 N ATOM 480 CA GLU A 54 -4.123 7.446 13.139 1.00 12.66 C ANISOU 480 CA GLU A 54 2556 1218 1034 -285 165 -97 C ATOM 481 C GLU A 54 -3.904 6.103 13.870 1.00 11.78 C ANISOU 481 C GLU A 54 2419 1127 927 -308 139 -7 C ATOM 482 O GLU A 54 -3.383 5.160 13.293 1.00 12.49 O ANISOU 482 O GLU A 54 2783 1059 901 -254 182 128 O ATOM 483 CB GLU A 54 -4.928 7.196 11.870 1.00 14.99 C ANISOU 483 CB GLU A 54 2917 1484 1294 -292 -88 209 C ATOM 484 CG GLU A 54 -5.130 8.414 11.023 1.00 20.59 C ANISOU 484 CG GLU A 54 3367 2307 2149 -418 -78 472 C ATOM 485 CD GLU A 54 -6.112 8.223 9.911 1.00 23.40 C ANISOU 485 CD GLU A 54 3680 2730 2480 -115 -372 720 C ATOM 486 OE1 GLU A 54 -5.997 7.233 9.176 1.00 27.48 O ANISOU 486 OE1 GLU A 54 4367 3630 2441 -656 -871 -188 O ATOM 487 OE2 GLU A 54 -6.983 9.109 9.741 1.00 31.27 O ANISOU 487 OE2 GLU A 54 4328 3233 4317 214 -283 294 O ATOM 488 N ASER A 55 -4.300 6.115 15.106 0.50 10.94 N ANISOU 488 N ASER A 55 2420 981 753 -165 117 -3 N ATOM 489 N BSER A 55 -4.308 5.924 15.131 0.50 13.84 N ANISOU 489 N BSER A 55 2460 1656 1142 -133 225 40 N ATOM 490 CA ASER A 55 -3.837 5.105 16.021 0.50 9.05 C ANISOU 490 CA ASER A 55 2119 635 684 -163 110 91 C ATOM 491 CA BSER A 55 -4.351 4.530 15.765 0.50 14.46 C ANISOU 491 CA BSER A 55 2310 1864 1318 -100 146 282 C ATOM 492 C ASER A 55 -4.946 4.682 16.923 0.50 9.54 C ANISOU 492 C ASER A 55 2057 837 729 -138 98 -23 C ATOM 493 C BSER A 55 -5.523 4.346 16.725 0.50 12.82 C ANISOU 493 C BSER A 55 2198 1618 1052 -146 265 318 C ATOM 494 O ASER A 55 -5.667 5.514 17.446 0.50 10.87 O ANISOU 494 O ASER A 55 2193 1069 865 105 190 154 O ATOM 495 O BSER A 55 -6.244 5.265 17.061 0.50 12.50 O ANISOU 495 O BSER A 55 2195 1347 1204 -123 89 470 O ATOM 496 CB ASER A 55 -2.735 5.618 16.893 0.50 9.48 C ANISOU 496 CB ASER A 55 2162 746 692 -46 171 182 C ATOM 497 CB BSER A 55 -3.068 4.039 16.501 0.50 15.87 C ANISOU 497 CB BSER A 55 2459 1818 1751 -102 229 198 C ATOM 498 OG ASER A 55 -2.269 4.698 17.876 0.50 11.19 O ANISOU 498 OG ASER A 55 2003 1264 982 -23 37 348 O ATOM 499 OG BSER A 55 -2.864 4.670 17.737 0.50 14.51 O ANISOU 499 OG BSER A 55 2042 2143 1329 137 -18 659 O ATOM 500 N ATHR A 56 -5.002 3.400 17.220 0.50 8.76 N ANISOU 500 N ATHR A 56 1754 822 753 -111 173 54 N ATOM 501 N BTHR A 56 -5.674 3.128 17.204 0.50 13.17 N ANISOU 501 N BTHR A 56 2247 1364 1393 -33 186 265 N ATOM 502 CA ATHR A 56 -5.928 2.856 18.231 0.50 8.87 C ANISOU 502 CA ATHR A 56 1841 665 861 -46 197 31 C ATOM 503 CA BTHR A 56 -6.653 2.835 18.227 0.50 13.20 C ANISOU 503 CA BTHR A 56 2280 1242 1494 -37 273 366 C ATOM 504 C ATHR A 56 -5.485 3.250 19.636 0.50 9.05 C ANISOU 504 C ATHR A 56 1734 838 864 -45 173 189 C ATOM 505 C BTHR A 56 -6.205 3.405 19.565 0.50 12.62 C ANISOU 505 C BTHR A 56 2093 1150 1552 -39 154 350 C ATOM 506 O ATHR A 56 -6.261 3.034 20.594 0.50 10.67 O ANISOU 506 O ATHR A 56 2200 909 945 74 202 150 O ATOM 507 O BTHR A 56 -7.040 3.578 20.407 0.50 14.66 O ANISOU 507 O BTHR A 56 2262 1673 1634 -118 361 141 O ATOM 508 CB ATHR A 56 -6.013 1.336 18.114 0.50 9.95 C ANISOU 508 CB ATHR A 56 1797 1030 953 -113 294 157 C ATOM 509 CB BTHR A 56 -6.909 1.345 18.390 0.50 15.07 C ANISOU 509 CB BTHR A 56 2637 1188 1899 -92 237 520 C ATOM 510 OG1ATHR A 56 -4.683 0.869 18.207 0.50 8.87 O ANISOU 510 OG1ATHR A 56 2071 642 657 -55 283 86 O ATOM 511 OG1BTHR A 56 -5.732 0.699 18.875 0.50 18.14 O ANISOU 511 OG1BTHR A 56 3012 1486 2394 7 97 161 O ATOM 512 CG2ATHR A 56 -6.654 0.875 16.824 0.50 12.56 C ANISOU 512 CG2ATHR A 56 1834 1372 1566 -238 51 -160 C ATOM 513 CG2BTHR A 56 -7.331 0.704 17.091 0.50 16.18 C ANISOU 513 CG2BTHR A 56 2856 1385 1904 -164 207 227 C ATOM 514 N APHE A 57 -4.233 3.722 19.821 0.50 9.35 N ANISOU 514 N APHE A 57 1933 773 844 4 183 93 N ATOM 515 N BPHE A 57 -4.924 3.693 19.772 0.50 11.40 N ANISOU 515 N BPHE A 57 1878 1299 1155 -150 311 361 N ATOM 516 CA APHE A 57 -3.764 4.269 21.098 0.50 9.92 C ANISOU 516 CA APHE A 57 1781 1135 852 -22 136 236 C ATOM 517 CA BPHE A 57 -4.478 4.301 21.039 0.50 11.70 C ANISOU 517 CA BPHE A 57 1898 1231 1316 -106 144 408 C ATOM 518 C APHE A 57 -4.077 5.781 21.218 0.50 10.20 C ANISOU 518 C APHE A 57 1974 1011 892 -8 95 193 C ATOM 519 C BPHE A 57 -4.748 5.762 21.007 0.50 11.18 C ANISOU 519 C BPHE A 57 2037 1039 1171 -69 93 439 C ATOM 520 O APHE A 57 -4.892 6.167 22.066 0.50 12.50 O ANISOU 520 O APHE A 57 2217 1237 1292 -8 338 241 O ATOM 521 O BPHE A 57 -5.678 6.206 21.575 0.50 14.06 O ANISOU 521 O BPHE A 57 2041 1586 1712 -77 346 395 O ATOM 522 CB APHE A 57 -2.249 3.985 21.314 0.50 9.93 C ANISOU 522 CB APHE A 57 1861 1022 888 -58 -7 310 C ATOM 523 CB BPHE A 57 -3.002 4.034 21.355 0.50 12.20 C ANISOU 523 CB BPHE A 57 1971 1167 1496 57 129 342 C ATOM 524 CG APHE A 57 -1.653 4.758 22.417 0.50 11.74 C ANISOU 524 CG APHE A 57 1967 1232 1262 116 -27 142 C ATOM 525 CG BPHE A 57 -2.484 4.794 22.536 0.50 14.95 C ANISOU 525 CG BPHE A 57 2334 1542 1804 47 -167 205 C ATOM 526 CD1APHE A 57 -2.220 4.759 23.656 0.50 12.95 C ANISOU 526 CD1APHE A 57 2103 1481 1335 -17 143 62 C ATOM 527 CD1BPHE A 57 -1.324 5.561 22.418 0.50 17.30 C ANISOU 527 CD1BPHE A 57 2536 1803 2232 9 -57 -68 C ATOM 528 CD2APHE A 57 -0.562 5.580 22.182 0.50 13.42 C ANISOU 528 CD2APHE A 57 2013 1561 1525 91 110 268 C ATOM 529 CD2BPHE A 57 -3.158 4.805 23.735 0.50 17.96 C ANISOU 529 CD2BPHE A 57 2729 1991 2103 -41 -267 45 C ATOM 530 CE1APHE A 57 -1.667 5.538 24.650 0.50 15.74 C ANISOU 530 CE1APHE A 57 2421 1881 1675 -181 -297 73 C ATOM 531 CE1BPHE A 57 -0.842 6.281 23.486 0.50 18.03 C ANISOU 531 CE1BPHE A 57 2437 2124 2288 304 -109 6 C ATOM 532 CE2APHE A 57 -0.010 6.352 23.161 0.50 15.84 C ANISOU 532 CE2APHE A 57 2491 1302 2225 -31 -285 632 C ATOM 533 CE2BPHE A 57 -2.667 5.537 24.816 0.50 20.41 C ANISOU 533 CE2BPHE A 57 2720 2634 2399 153 -364 0 C ATOM 534 CZ APHE A 57 -0.569 6.338 24.389 0.50 14.95 C ANISOU 534 CZ APHE A 57 2527 1315 1837 123 -354 101 C ATOM 535 CZ BPHE A 57 -1.517 6.275 24.668 0.50 18.10 C ANISOU 535 CZ BPHE A 57 2751 2015 2110 109 -258 -99 C ATOM 536 N ALYS A 58 -3.405 6.647 20.471 0.50 10.75 N ANISOU 536 N ALYS A 58 2022 1055 1008 -167 -5 93 N ATOM 537 N BLYS A 58 -3.949 6.496 20.262 0.50 12.00 N ANISOU 537 N BLYS A 58 2240 860 1458 -50 413 397 N ATOM 538 CA ALYS A 58 -3.726 8.090 20.519 0.50 11.35 C ANISOU 538 CA ALYS A 58 2178 1202 932 -128 -68 -74 C ATOM 539 CA BLYS A 58 -4.025 7.919 20.245 0.50 14.33 C ANISOU 539 CA BLYS A 58 2523 1273 1646 -96 322 235 C ATOM 540 C ALYS A 58 -3.446 8.669 19.147 0.50 9.10 C ANISOU 540 C ALYS A 58 1969 625 861 -223 69 -77 C ATOM 541 C BLYS A 58 -3.795 8.302 18.756 0.50 14.47 C ANISOU 541 C BLYS A 58 2575 1142 1780 -58 509 190 C ATOM 542 O ALYS A 58 -2.333 8.520 18.675 0.50 9.12 O ANISOU 542 O ALYS A 58 1868 697 899 -4 188 148 O ATOM 543 O BLYS A 58 -3.309 7.617 17.822 0.50 17.69 O ANISOU 543 O BLYS A 58 2996 1809 1914 94 603 256 O ATOM 544 CB ALYS A 58 -2.921 8.814 21.607 0.50 12.76 C ANISOU 544 CB ALYS A 58 2376 1233 1238 -120 -123 -206 C ATOM 545 CB BLYS A 58 -3.062 8.539 21.335 0.50 14.99 C ANISOU 545 CB BLYS A 58 2613 1191 1892 -200 217 219 C ATOM 546 CG ALYS A 58 -3.058 8.284 22.929 0.50 18.25 C ANISOU 546 CG ALYS A 58 2840 2328 1764 -201 -9 -268 C ATOM 547 CG BLYS A 58 -3.132 10.137 21.721 0.50 12.73 C ANISOU 547 CG BLYS A 58 2492 1155 1188 -181 122 11 C ATOM 548 CD ALYS A 58 -4.352 8.604 23.574 0.50 21.67 C ANISOU 548 CD ALYS A 58 3110 2465 2656 -55 65 -326 C ATOM 549 CD BLYS A 58 -4.532 10.519 22.118 0.50 15.90 C ANISOU 549 CD BLYS A 58 2725 1762 1552 -198 105 -270 C ATOM 550 CE ALYS A 58 -4.472 7.672 24.748 0.50 21.17 C ANISOU 550 CE ALYS A 58 3382 2419 2241 14 201 -558 C ATOM 551 CE BLYS A 58 -4.677 12.040 22.163 0.50 19.78 C ANISOU 551 CE BLYS A 58 3093 2288 2135 -79 3 -239 C ATOM 552 NZ ALYS A 58 -3.119 7.504 25.370 0.50 24.16 N ANISOU 552 NZ ALYS A 58 3839 2203 3137 266 73 -156 N ATOM 553 NZ BLYS A 58 -6.069 12.531 22.334 0.50 24.46 N ANISOU 553 NZ BLYS A 58 3348 3193 2752 106 79 -187 N ATOM 554 N ASN A 59 -4.459 9.324 18.481 1.00 11.79 N ANISOU 554 N ASN A 59 2317 974 1185 -36 438 97 N ATOM 555 CA ASN A 59 -4.219 10.006 17.237 1.00 12.16 C ANISOU 555 CA ASN A 59 2469 877 1275 -67 366 15 C ATOM 556 C ASN A 59 -3.388 11.248 17.512 1.00 12.35 C ANISOU 556 C ASN A 59 2736 816 1141 -27 498 -66 C ATOM 557 O ASN A 59 -3.575 11.904 18.520 1.00 14.77 O ANISOU 557 O ASN A 59 3111 1050 1449 -303 743 -208 O ATOM 558 CB ASN A 59 -5.545 10.451 16.642 1.00 13.56 C ANISOU 558 CB ASN A 59 2616 1046 1489 -80 295 250 C ATOM 559 CG ASN A 59 -6.484 9.321 16.276 1.00 14.91 C ANISOU 559 CG ASN A 59 2428 1510 1727 117 11 205 C ATOM 560 OD1 ASN A 59 -6.059 8.320 15.744 1.00 14.31 O ANISOU 560 OD1 ASN A 59 2343 1287 1806 4 107 271 O ATOM 561 ND2 ASN A 59 -7.769 9.427 16.653 1.00 21.54 N ANISOU 561 ND2 ASN A 59 2606 2660 2916 -53 205 11 N ATOM 562 N THR A 60 -2.475 11.527 16.595 1.00 11.71 N ANISOU 562 N THR A 60 2638 843 966 -75 448 -51 N ATOM 563 CA THR A 60 -1.664 12.720 16.687 1.00 11.81 C ANISOU 563 CA THR A 60 2704 725 1057 -148 455 -39 C ATOM 564 C THR A 60 -1.552 13.360 15.309 1.00 10.77 C ANISOU 564 C THR A 60 2547 533 1012 -112 405 -26 C ATOM 565 O THR A 60 -1.677 12.711 14.281 1.00 10.96 O ANISOU 565 O THR A 60 2552 676 935 -138 289 -35 O ATOM 566 CB THR A 60 -0.241 12.451 17.246 1.00 12.78 C ANISOU 566 CB THR A 60 2774 1047 1034 -236 259 -69 C ATOM 567 OG1 THR A 60 0.469 11.606 16.361 1.00 12.73 O ANISOU 567 OG1 THR A 60 2528 1285 1023 -64 168 94 O ATOM 568 CG2 THR A 60 -0.210 11.860 18.647 1.00 14.07 C ANISOU 568 CG2 THR A 60 3025 1373 947 -214 216 -12 C ATOM 569 N GLU A 61 -1.268 14.640 15.288 1.00 11.28 N ANISOU 569 N GLU A 61 2633 772 878 -75 424 -21 N ATOM 570 CA GLU A 61 -0.991 15.353 14.045 1.00 11.27 C ANISOU 570 CA GLU A 61 2499 747 1036 -66 336 -90 C ATOM 571 C GLU A 61 -0.109 16.528 14.326 1.00 11.09 C ANISOU 571 C GLU A 61 2561 638 1012 -60 306 -139 C ATOM 572 O GLU A 61 -0.358 17.316 15.262 1.00 13.37 O ANISOU 572 O GLU A 61 2978 871 1228 -220 630 -250 O ATOM 573 CB GLU A 61 -2.300 15.815 13.431 1.00 13.63 C ANISOU 573 CB GLU A 61 2555 1015 1608 -89 255 106 C ATOM 574 CG GLU A 61 -2.148 16.551 12.146 1.00 17.60 C ANISOU 574 CG GLU A 61 2649 1806 2230 -34 -5 624 C ATOM 575 CD GLU A 61 -3.457 16.968 11.539 1.00 24.60 C ANISOU 575 CD GLU A 61 2870 3344 3133 -122 -24 786 C ATOM 576 OE1 GLU A 61 -3.461 18.008 10.875 1.00 28.12 O ANISOU 576 OE1 GLU A 61 2900 4058 3724 -131 -447 1238 O ATOM 577 OE2 GLU A 61 -4.486 16.275 11.749 1.00 29.22 O ANISOU 577 OE2 GLU A 61 3104 3923 4073 -359 -95 581 O ATOM 578 N ILE A 62 0.969 16.619 13.567 1.00 9.33 N ANISOU 578 N ILE A 62 2294 693 555 -48 158 -45 N ATOM 579 CA ILE A 62 1.843 17.766 13.647 1.00 9.41 C ANISOU 579 CA ILE A 62 2369 555 650 -137 38 -74 C ATOM 580 C ILE A 62 1.995 18.348 12.232 1.00 8.59 C ANISOU 580 C ILE A 62 2210 501 550 -138 68 -11 C ATOM 581 O ILE A 62 2.100 17.620 11.256 1.00 10.11 O ANISOU 581 O ILE A 62 2758 544 538 -206 54 -41 O ATOM 582 CB ILE A 62 3.224 17.406 14.237 1.00 10.14 C ANISOU 582 CB ILE A 62 2453 807 592 -137 -91 -41 C ATOM 583 CG1 ILE A 62 3.988 16.317 13.475 1.00 10.60 C ANISOU 583 CG1 ILE A 62 2169 1032 824 -147 -147 -82 C ATOM 584 CG2 ILE A 62 3.068 16.987 15.726 1.00 12.55 C ANISOU 584 CG2 ILE A 62 2644 1443 679 68 -7 174 C ATOM 585 CD1 ILE A 62 5.391 16.124 13.913 1.00 13.36 C ANISOU 585 CD1 ILE A 62 2370 1452 1250 -109 -183 -208 C ATOM 586 N SER A 63 2.044 19.654 12.174 1.00 8.51 N ANISOU 586 N SER A 63 2122 612 500 -35 65 -107 N ATOM 587 CA SER A 63 2.410 20.393 10.971 1.00 8.62 C ANISOU 587 CA SER A 63 2206 521 547 -23 36 -14 C ATOM 588 C SER A 63 3.530 21.356 11.305 1.00 8.40 C ANISOU 588 C SER A 63 2049 541 602 -38 17 -176 C ATOM 589 O SER A 63 3.508 21.985 12.355 1.00 10.04 O ANISOU 589 O SER A 63 2256 741 817 -173 160 -190 O ATOM 590 CB SER A 63 1.227 21.182 10.409 1.00 9.44 C ANISOU 590 CB SER A 63 2151 822 613 -37 45 -59 C ATOM 591 OG SER A 63 0.182 20.322 9.961 1.00 11.54 O ANISOU 591 OG SER A 63 2244 1148 990 71 -134 -109 O ATOM 592 N PHE A 64 4.498 21.485 10.399 1.00 8.52 N ANISOU 592 N PHE A 64 2101 681 454 -39 -50 21 N ATOM 593 CA PHE A 64 5.717 22.199 10.730 1.00 8.43 C ANISOU 593 CA PHE A 64 2034 639 529 -97 -58 -51 C ATOM 594 C PHE A 64 6.432 22.621 9.457 1.00 8.17 C ANISOU 594 C PHE A 64 2084 515 504 -11 -30 47 C ATOM 595 O PHE A 64 6.208 22.059 8.376 1.00 8.69 O ANISOU 595 O PHE A 64 2131 693 476 -139 -47 -18 O ATOM 596 CB PHE A 64 6.624 21.359 11.637 1.00 8.89 C ANISOU 596 CB PHE A 64 2001 802 572 -187 -79 55 C ATOM 597 CG PHE A 64 6.992 20.042 11.018 1.00 8.98 C ANISOU 597 CG PHE A 64 2032 807 570 -17 -135 83 C ATOM 598 CD1 PHE A 64 6.160 18.913 11.164 1.00 9.29 C ANISOU 598 CD1 PHE A 64 1995 821 711 -91 -175 11 C ATOM 599 CD2 PHE A 64 8.111 19.909 10.270 1.00 9.27 C ANISOU 599 CD2 PHE A 64 2049 809 662 -19 -112 102 C ATOM 600 CE1 PHE A 64 6.447 17.728 10.547 1.00 10.28 C ANISOU 600 CE1 PHE A 64 2310 858 738 -134 -265 15 C ATOM 601 CE2 PHE A 64 8.408 18.727 9.650 1.00 10.64 C ANISOU 601 CE2 PHE A 64 2269 1116 657 112 -52 166 C ATOM 602 CZ PHE A 64 7.593 17.625 9.810 1.00 10.55 C ANISOU 602 CZ PHE A 64 2477 860 669 76 -210 14 C ATOM 603 N ILE A 65 7.325 23.560 9.660 1.00 8.50 N ANISOU 603 N ILE A 65 2053 587 587 -97 -34 -51 N ATOM 604 CA ILE A 65 8.281 24.013 8.669 1.00 8.45 C ANISOU 604 CA ILE A 65 2082 556 571 -28 -16 3 C ATOM 605 C ILE A 65 9.673 23.577 9.137 1.00 8.58 C ANISOU 605 C ILE A 65 2170 480 608 -112 -56 7 C ATOM 606 O ILE A 65 9.990 23.704 10.335 1.00 8.55 O ANISOU 606 O ILE A 65 2066 530 653 -51 -69 -57 O ATOM 607 CB ILE A 65 8.195 25.545 8.476 1.00 9.59 C ANISOU 607 CB ILE A 65 2281 555 805 -31 -114 7 C ATOM 608 CG1 ILE A 65 6.807 25.864 7.916 1.00 11.39 C ANISOU 608 CG1 ILE A 65 2268 929 1129 -26 -103 163 C ATOM 609 CG2 ILE A 65 9.306 26.030 7.563 1.00 10.50 C ANISOU 609 CG2 ILE A 65 2368 674 947 -94 79 167 C ATOM 610 CD1 ILE A 65 6.473 27.364 7.823 1.00 14.77 C ANISOU 610 CD1 ILE A 65 2630 845 2136 213 -26 421 C ATOM 611 N LEU A 66 10.465 23.013 8.247 1.00 8.38 N ANISOU 611 N LEU A 66 2054 562 568 -1 36 -34 N ATOM 612 CA LEU A 66 11.793 22.569 8.634 1.00 8.81 C ANISOU 612 CA LEU A 66 2188 525 632 1 96 22 C ATOM 613 C LEU A 66 12.591 23.682 9.300 1.00 8.72 C ANISOU 613 C LEU A 66 2038 501 772 1 133 71 C ATOM 614 O LEU A 66 12.632 24.809 8.808 1.00 9.48 O ANISOU 614 O LEU A 66 2078 571 952 -87 11 180 O ATOM 615 CB LEU A 66 12.552 21.996 7.433 1.00 9.78 C ANISOU 615 CB LEU A 66 2287 675 754 72 -12 81 C ATOM 616 CG LEU A 66 11.929 20.749 6.788 1.00 10.61 C ANISOU 616 CG LEU A 66 2387 855 788 43 98 -222 C ATOM 617 CD1 LEU A 66 12.662 20.433 5.482 1.00 14.20 C ANISOU 617 CD1 LEU A 66 3251 1085 1058 69 211 -377 C ATOM 618 CD2 LEU A 66 12.071 19.546 7.732 1.00 11.86 C ANISOU 618 CD2 LEU A 66 2729 636 1140 -44 -68 -34 C ATOM 619 N GLY A 67 13.204 23.341 10.420 1.00 8.71 N ANISOU 619 N GLY A 67 2044 544 718 36 13 84 N ATOM 620 CA GLY A 67 14.063 24.280 11.151 1.00 9.48 C ANISOU 620 CA GLY A 67 2053 733 817 -63 -64 -18 C ATOM 621 C GLY A 67 13.355 25.195 12.099 1.00 8.31 C ANISOU 621 C GLY A 67 1978 483 696 -69 2 15 C ATOM 622 O GLY A 67 14.038 25.947 12.794 1.00 9.58 O ANISOU 622 O GLY A 67 2016 695 929 -92 -121 -130 O ATOM 623 N GLN A 68 12.033 25.153 12.167 1.00 8.39 N ANISOU 623 N GLN A 68 1992 463 732 -137 -84 -55 N ATOM 624 CA GLN A 68 11.224 26.113 12.930 1.00 8.53 C ANISOU 624 CA GLN A 68 2109 413 718 -99 -111 -80 C ATOM 625 C GLN A 68 10.517 25.419 14.072 1.00 8.68 C ANISOU 625 C GLN A 68 2065 371 862 0 -24 -113 C ATOM 626 O GLN A 68 9.637 24.563 13.876 1.00 8.95 O ANISOU 626 O GLN A 68 2008 554 836 -58 16 -147 O ATOM 627 CB GLN A 68 10.245 26.801 11.988 1.00 9.53 C ANISOU 627 CB GLN A 68 2174 487 958 -31 -186 -219 C ATOM 628 CG GLN A 68 11.008 27.517 10.885 1.00 11.77 C ANISOU 628 CG GLN A 68 2780 762 928 -322 -274 97 C ATOM 629 CD GLN A 68 10.277 28.513 10.090 1.00 13.47 C ANISOU 629 CD GLN A 68 3119 583 1416 -102 -543 292 C ATOM 630 OE1 GLN A 68 9.065 28.791 10.368 1.00 17.05 O ANISOU 630 OE1 GLN A 68 3251 940 2285 202 -952 265 O ATOM 631 NE2 GLN A 68 10.975 29.061 9.117 1.00 15.04 N ANISOU 631 NE2 GLN A 68 3702 759 1251 -223 -380 390 N ATOM 632 N GLU A 69 10.907 25.774 15.298 1.00 8.65 N ANISOU 632 N GLU A 69 2072 444 772 -86 -10 -78 N ATOM 633 CA GLU A 69 10.390 25.122 16.518 1.00 9.05 C ANISOU 633 CA GLU A 69 2178 400 860 -81 -104 -14 C ATOM 634 C GLU A 69 8.889 25.272 16.630 1.00 8.84 C ANISOU 634 C GLU A 69 2216 480 659 -69 2 9 C ATOM 635 O GLU A 69 8.336 26.327 16.292 1.00 9.85 O ANISOU 635 O GLU A 69 2156 468 1117 27 -11 35 O ATOM 636 CB GLU A 69 11.101 25.719 17.734 1.00 11.37 C ANISOU 636 CB GLU A 69 2233 1243 843 -111 -131 215 C ATOM 637 CG GLU A 69 10.727 25.153 19.075 1.00 13.52 C ANISOU 637 CG GLU A 69 2821 1172 1143 -179 -122 20 C ATOM 638 CD GLU A 69 11.631 25.664 20.167 1.00 19.64 C ANISOU 638 CD GLU A 69 3640 2779 1041 -565 -398 162 C ATOM 639 OE1 GLU A 69 11.517 26.894 20.487 1.00 29.58 O ANISOU 639 OE1 GLU A 69 4885 4188 2165 -916 -509 -1365 O ATOM 640 OE2 GLU A 69 12.392 24.806 20.699 1.00 25.04 O ANISOU 640 OE2 GLU A 69 3917 3743 1851 -628 -819 116 O ATOM 641 N PHE A 70 8.249 24.266 17.190 1.00 8.14 N ANISOU 641 N PHE A 70 1983 460 648 97 15 9 N ATOM 642 CA PHE A 70 6.826 24.242 17.409 1.00 8.50 C ANISOU 642 CA PHE A 70 2103 429 695 128 100 -55 C ATOM 643 C PHE A 70 6.509 23.485 18.682 1.00 9.03 C ANISOU 643 C PHE A 70 2205 508 717 105 143 -51 C ATOM 644 O PHE A 70 7.309 22.702 19.209 1.00 9.82 O ANISOU 644 O PHE A 70 2197 794 738 209 149 35 O ATOM 645 CB PHE A 70 6.090 23.655 16.208 1.00 8.70 C ANISOU 645 CB PHE A 70 1984 685 634 48 21 -18 C ATOM 646 CG PHE A 70 6.442 22.236 15.874 1.00 8.85 C ANISOU 646 CG PHE A 70 2038 622 699 -72 -76 38 C ATOM 647 CD1 PHE A 70 7.554 21.938 15.094 1.00 8.49 C ANISOU 647 CD1 PHE A 70 2019 654 550 -11 8 25 C ATOM 648 CD2 PHE A 70 5.650 21.185 16.302 1.00 10.67 C ANISOU 648 CD2 PHE A 70 2183 939 932 -164 181 -208 C ATOM 649 CE1 PHE A 70 7.878 20.627 14.755 1.00 9.23 C ANISOU 649 CE1 PHE A 70 2240 668 599 15 -72 -81 C ATOM 650 CE2 PHE A 70 5.973 19.875 15.971 1.00 11.40 C ANISOU 650 CE2 PHE A 70 2519 922 888 -401 191 -136 C ATOM 651 CZ PHE A 70 7.077 19.603 15.201 1.00 10.04 C ANISOU 651 CZ PHE A 70 2481 644 690 -92 -32 -101 C ATOM 652 N ASP A 71 5.283 23.683 19.164 1.00 9.63 N ANISOU 652 N ASP A 71 2166 604 886 253 213 116 N ATOM 653 CA ASP A 71 4.735 22.939 20.304 1.00 10.42 C ANISOU 653 CA ASP A 71 2372 723 862 222 333 105 C ATOM 654 C ASP A 71 4.074 21.664 19.812 1.00 10.84 C ANISOU 654 C ASP A 71 2202 1002 913 70 220 90 C ATOM 655 O ASP A 71 3.346 21.650 18.814 1.00 11.96 O ANISOU 655 O ASP A 71 2423 985 1137 49 38 157 O ATOM 656 CB ASP A 71 3.658 23.735 20.996 1.00 11.02 C ANISOU 656 CB ASP A 71 2280 962 943 249 213 139 C ATOM 657 CG ASP A 71 4.194 24.988 21.614 1.00 11.44 C ANISOU 657 CG ASP A 71 2387 1138 819 170 -24 -99 C ATOM 658 OD1 ASP A 71 5.164 24.844 22.451 1.00 14.18 O ANISOU 658 OD1 ASP A 71 3012 1093 1283 315 -268 -247 O ATOM 659 OD2 ASP A 71 3.652 26.082 21.397 1.00 12.06 O ANISOU 659 OD2 ASP A 71 2555 900 1127 184 14 39 O ATOM 660 N GLU A 72 4.314 20.578 20.556 1.00 11.06 N ANISOU 660 N GLU A 72 2354 834 1011 136 225 291 N ATOM 661 CA GLU A 72 3.767 19.267 20.219 1.00 11.91 C ANISOU 661 CA GLU A 72 2242 974 1309 61 165 473 C ATOM 662 C GLU A 72 3.248 18.600 21.500 1.00 13.11 C ANISOU 662 C GLU A 72 2409 1015 1555 168 180 476 C ATOM 663 O GLU A 72 3.897 18.662 22.519 1.00 13.75 O ANISOU 663 O GLU A 72 2545 1344 1333 52 349 419 O ATOM 664 CB GLU A 72 4.857 18.420 19.531 1.00 11.10 C ANISOU 664 CB GLU A 72 2207 1008 1001 54 217 226 C ATOM 665 CG GLU A 72 4.493 16.960 19.246 1.00 11.31 C ANISOU 665 CG GLU A 72 2372 1012 912 2 101 271 C ATOM 666 CD GLU A 72 5.573 16.163 18.574 1.00 11.94 C ANISOU 666 CD GLU A 72 2475 1178 881 171 202 181 C ATOM 667 OE1 GLU A 72 6.729 16.608 18.487 1.00 12.35 O ANISOU 667 OE1 GLU A 72 2336 1241 1113 57 188 -97 O ATOM 668 OE2 GLU A 72 5.295 14.992 18.135 1.00 13.51 O ANISOU 668 OE2 GLU A 72 2759 859 1516 48 278 -32 O ATOM 669 N AVAL A 73 2.036 18.088 21.591 0.50 13.80 N ANISOU 669 N AVAL A 73 2391 1303 1549 177 170 478 N ATOM 670 N BVAL A 73 2.137 17.868 21.228 0.50 13.55 N ANISOU 670 N BVAL A 73 2173 1119 1853 214 290 766 N ATOM 671 CA AVAL A 73 1.696 17.240 22.749 0.50 11.92 C ANISOU 671 CA AVAL A 73 2347 1008 1174 186 200 356 C ATOM 672 CA BVAL A 73 1.531 16.928 22.153 0.50 13.69 C ANISOU 672 CA BVAL A 73 2168 1142 1890 130 244 742 C ATOM 673 C AVAL A 73 1.734 15.782 22.145 0.50 12.59 C ANISOU 673 C AVAL A 73 2323 1282 1179 143 314 431 C ATOM 674 C BVAL A 73 1.833 15.561 21.694 0.50 13.90 C ANISOU 674 C BVAL A 73 2259 1237 1782 52 162 734 C ATOM 675 O AVAL A 73 1.012 15.474 21.262 0.50 11.33 O ANISOU 675 O AVAL A 73 2472 1025 808 135 169 -24 O ATOM 676 O BVAL A 73 1.367 15.104 20.572 0.50 14.21 O ANISOU 676 O BVAL A 73 2373 799 2226 64 28 693 O ATOM 677 CB AVAL A 73 0.319 17.577 23.249 0.50 12.21 C ANISOU 677 CB AVAL A 73 2348 1147 1142 167 262 309 C ATOM 678 CB BVAL A 73 0.030 17.090 22.325 0.50 14.30 C ANISOU 678 CB BVAL A 73 2204 1264 1965 189 202 652 C ATOM 679 CG1AVAL A 73 -0.070 16.608 24.369 0.50 13.11 C ANISOU 679 CG1AVAL A 73 2467 1297 1216 23 468 124 C ATOM 680 CG1BVAL A 73 -0.498 16.056 23.345 0.50 16.87 C ANISOU 680 CG1BVAL A 73 2434 1640 2336 -90 359 562 C ATOM 681 CG2AVAL A 73 0.229 19.030 23.763 0.50 13.78 C ANISOU 681 CG2AVAL A 73 2581 1129 1522 232 324 49 C ATOM 682 CG2BVAL A 73 -0.237 18.467 22.782 0.50 16.30 C ANISOU 682 CG2BVAL A 73 2307 1653 2230 191 417 586 C ATOM 683 N THR A 74 2.647 14.913 22.532 1.00 13.22 N ANISOU 683 N THR A 74 2313 1446 1264 269 202 603 N ATOM 684 CA THR A 74 2.978 13.594 22.029 1.00 12.87 C ANISOU 684 CA THR A 74 2384 1487 1017 34 146 458 C ATOM 685 C THR A 74 1.884 12.575 22.385 1.00 13.43 C ANISOU 685 C THR A 74 2261 1623 1216 138 48 471 C ATOM 686 O THR A 74 0.989 12.844 23.171 1.00 14.47 O ANISOU 686 O THR A 74 2404 1582 1510 152 353 659 O ATOM 687 CB THR A 74 4.333 13.105 22.589 1.00 11.54 C ANISOU 687 CB THR A 74 2370 1214 801 81 132 232 C ATOM 688 OG1 THR A 74 4.170 12.920 23.992 1.00 12.02 O ANISOU 688 OG1 THR A 74 2464 1181 920 227 166 297 O ATOM 689 CG2 THR A 74 5.421 14.108 22.305 1.00 12.35 C ANISOU 689 CG2 THR A 74 2443 1060 1189 77 175 181 C ATOM 690 N ALA A 75 1.943 11.403 21.750 1.00 14.05 N ANISOU 690 N ALA A 75 2408 1860 1069 -53 129 515 N ATOM 691 CA ALA A 75 0.929 10.339 21.933 1.00 14.58 C ANISOU 691 CA ALA A 75 2425 1908 1205 -139 33 446 C ATOM 692 C ALA A 75 0.834 9.945 23.413 1.00 14.85 C ANISOU 692 C ALA A 75 2472 1787 1382 -154 -2 464 C ATOM 693 O ALA A 75 -0.261 9.666 23.886 1.00 17.26 O ANISOU 693 O ALA A 75 2724 2312 1521 -346 206 546 O ATOM 694 CB ALA A 75 1.245 9.161 21.096 1.00 14.88 C ANISOU 694 CB ALA A 75 2536 1823 1293 -186 -33 328 C ATOM 695 N ASP A 76 1.970 9.931 24.119 1.00 14.09 N ANISOU 695 N ASP A 76 2619 1587 1146 -179 33 513 N ATOM 696 CA ASP A 76 2.032 9.626 25.552 1.00 14.60 C ANISOU 696 CA ASP A 76 2753 1646 1147 -247 66 424 C ATOM 697 C ASP A 76 1.787 10.885 26.435 1.00 14.77 C ANISOU 697 C ASP A 76 2880 1754 978 -285 287 458 C ATOM 698 O ASP A 76 1.956 10.845 27.616 1.00 17.28 O ANISOU 698 O ASP A 76 3301 2083 1178 -125 205 392 O ATOM 699 CB ASP A 76 3.377 8.980 25.911 1.00 14.80 C ANISOU 699 CB ASP A 76 2878 1342 1401 -297 -43 478 C ATOM 700 CG ASP A 76 4.559 9.838 25.610 1.00 13.39 C ANISOU 700 CG ASP A 76 2943 1054 1089 43 -205 357 C ATOM 701 OD1 ASP A 76 4.666 10.323 24.446 1.00 12.80 O ANISOU 701 OD1 ASP A 76 2688 1142 1033 5 -96 334 O ATOM 702 OD2 ASP A 76 5.378 10.082 26.519 1.00 14.49 O ANISOU 702 OD2 ASP A 76 3279 1051 1175 -185 -261 469 O ATOM 703 N ASP A 77 1.367 12.001 25.837 1.00 15.56 N ANISOU 703 N ASP A 77 2831 1865 1216 -145 508 400 N ATOM 704 CA ASP A 77 0.888 13.169 26.562 1.00 17.31 C ANISOU 704 CA ASP A 77 2835 2158 1582 -69 679 306 C ATOM 705 C ASP A 77 1.978 14.023 27.151 1.00 16.12 C ANISOU 705 C ASP A 77 2958 1712 1454 65 681 198 C ATOM 706 O ASP A 77 1.726 14.785 28.080 1.00 19.79 O ANISOU 706 O ASP A 77 3256 2173 2088 2 875 -301 O ATOM 707 CB ASP A 77 -0.185 12.859 27.591 1.00 19.29 C ANISOU 707 CB ASP A 77 2999 2429 1901 -219 764 338 C ATOM 708 CG ASP A 77 -1.142 14.027 27.789 1.00 23.21 C ANISOU 708 CG ASP A 77 3283 2966 2568 -304 1028 315 C ATOM 709 OD1 ASP A 77 -1.700 14.119 28.905 1.00 28.68 O ANISOU 709 OD1 ASP A 77 3694 4145 3056 94 1509 -49 O ATOM 710 OD2 ASP A 77 -1.350 14.864 26.859 1.00 28.22 O ANISOU 710 OD2 ASP A 77 3644 3702 3375 -163 986 493 O ATOM 711 N ARG A 78 3.184 13.978 26.597 1.00 14.30 N ANISOU 711 N ARG A 78 2881 1404 1147 190 602 323 N ATOM 712 CA ARG A 78 4.194 14.964 26.931 1.00 13.87 C ANISOU 712 CA ARG A 78 2926 1336 1005 179 574 306 C ATOM 713 C ARG A 78 3.941 16.236 26.149 1.00 13.68 C ANISOU 713 C ARG A 78 2897 1183 1116 386 612 285 C ATOM 714 O ARG A 78 3.555 16.199 24.982 1.00 15.06 O ANISOU 714 O ARG A 78 3339 1204 1178 439 482 275 O ATOM 715 CB ARG A 78 5.591 14.508 26.626 1.00 12.84 C ANISOU 715 CB ARG A 78 2749 1163 966 100 345 337 C ATOM 716 CG ARG A 78 6.144 13.437 27.538 1.00 12.64 C ANISOU 716 CG ARG A 78 2845 960 995 -66 226 306 C ATOM 717 CD ARG A 78 7.503 12.914 27.021 1.00 12.98 C ANISOU 717 CD ARG A 78 2797 1146 987 81 12 266 C ATOM 718 NE ARG A 78 7.238 12.024 25.883 1.00 11.97 N ANISOU 718 NE ARG A 78 2700 1001 846 152 -13 65 N ATOM 719 CZ ARG A 78 7.797 12.095 24.674 1.00 11.67 C ANISOU 719 CZ ARG A 78 2391 982 1060 265 -79 120 C ATOM 720 NH1 ARG A 78 8.820 12.908 24.441 1.00 12.38 N ANISOU 720 NH1 ARG A 78 2515 1167 1021 52 -53 75 N ATOM 721 NH2 ARG A 78 7.327 11.299 23.731 1.00 12.17 N ANISOU 721 NH2 ARG A 78 2671 957 995 110 -167 -55 N ATOM 722 N LYS A 79 4.175 17.387 26.786 1.00 14.20 N ANISOU 722 N LYS A 79 2998 1255 1141 309 678 245 N ATOM 723 CA LYS A 79 4.125 18.699 26.121 1.00 14.29 C ANISOU 723 CA LYS A 79 2889 1187 1351 430 642 117 C ATOM 724 C LYS A 79 5.554 19.077 25.830 1.00 13.43 C ANISOU 724 C LYS A 79 2811 1048 1241 326 504 63 C ATOM 725 O LYS A 79 6.345 19.371 26.755 1.00 15.84 O ANISOU 725 O LYS A 79 3225 1711 1079 147 522 -119 O ATOM 726 CB LYS A 79 3.462 19.696 27.027 1.00 16.27 C ANISOU 726 CB LYS A 79 3120 1386 1676 434 818 161 C ATOM 727 CG LYS A 79 1.977 19.397 27.242 1.00 23.20 C ANISOU 727 CG LYS A 79 3436 2467 2910 612 699 -320 C ATOM 728 CD LYS A 79 1.605 18.157 27.976 1.00 29.45 C ANISOU 728 CD LYS A 79 4070 3314 3806 317 389 -60 C ATOM 729 CE LYS A 79 0.128 18.224 28.367 1.00 32.54 C ANISOU 729 CE LYS A 79 4186 4017 4161 107 385 121 C ATOM 730 NZ LYS A 79 -0.566 16.941 28.177 1.00 34.02 N ANISOU 730 NZ LYS A 79 4607 3982 4336 34 365 135 N ATOM 731 N VAL A 80 5.941 19.014 24.556 1.00 12.00 N ANISOU 731 N VAL A 80 2662 1038 858 259 414 141 N ATOM 732 CA VAL A 80 7.326 19.167 24.183 1.00 10.90 C ANISOU 732 CA VAL A 80 2572 809 760 305 240 121 C ATOM 733 C VAL A 80 7.493 20.352 23.212 1.00 10.62 C ANISOU 733 C VAL A 80 2447 921 666 302 162 -106 C ATOM 734 O VAL A 80 6.529 20.778 22.582 1.00 11.63 O ANISOU 734 O VAL A 80 2579 855 985 209 213 94 O ATOM 735 CB VAL A 80 7.883 17.836 23.536 1.00 11.24 C ANISOU 735 CB VAL A 80 2543 829 898 134 302 145 C ATOM 736 CG1 VAL A 80 7.596 16.650 24.455 1.00 12.56 C ANISOU 736 CG1 VAL A 80 3110 808 851 206 151 239 C ATOM 737 CG2 VAL A 80 7.284 17.601 22.196 1.00 11.54 C ANISOU 737 CG2 VAL A 80 2712 877 794 178 247 104 C ATOM 738 N LYS A 81 8.725 20.787 23.104 1.00 10.22 N ANISOU 738 N LYS A 81 2465 767 648 229 110 18 N ATOM 739 CA LYS A 81 9.141 21.742 22.088 1.00 10.22 C ANISOU 739 CA LYS A 81 2705 558 617 231 121 -18 C ATOM 740 C LYS A 81 9.945 20.970 21.063 1.00 9.65 C ANISOU 740 C LYS A 81 2433 557 675 86 18 53 C ATOM 741 O LYS A 81 10.960 20.356 21.405 1.00 10.71 O ANISOU 741 O LYS A 81 2497 901 671 207 -108 3 O ATOM 742 CB LYS A 81 9.981 22.876 22.696 1.00 12.46 C ANISOU 742 CB LYS A 81 3056 697 981 94 163 -201 C ATOM 743 CG LYS A 81 9.356 23.686 23.686 1.00 17.51 C ANISOU 743 CG LYS A 81 3600 1310 1740 122 88 -477 C ATOM 744 CD LYS A 81 8.419 24.686 23.155 1.00 20.41 C ANISOU 744 CD LYS A 81 3550 2313 1890 150 -99 -240 C ATOM 745 CE LYS A 81 7.749 25.457 24.304 1.00 23.09 C ANISOU 745 CE LYS A 81 3700 2733 2339 329 -197 -467 C ATOM 746 NZ LYS A 81 6.779 26.486 23.888 1.00 23.75 N ANISOU 746 NZ LYS A 81 4087 2386 2551 339 -755 -430 N ATOM 747 N SER A 82 9.494 21.020 19.817 1.00 9.04 N ANISOU 747 N SER A 82 2246 609 580 198 75 52 N ATOM 748 CA SER A 82 10.041 20.190 18.771 1.00 8.78 C ANISOU 748 CA SER A 82 2199 440 695 185 24 19 C ATOM 749 C SER A 82 10.625 21.012 17.666 1.00 8.06 C ANISOU 749 C SER A 82 2045 497 520 8 29 72 C ATOM 750 O SER A 82 10.109 22.057 17.276 1.00 8.74 O ANISOU 750 O SER A 82 2097 513 709 69 40 84 O ATOM 751 CB SER A 82 8.938 19.307 18.182 1.00 9.55 C ANISOU 751 CB SER A 82 2294 619 714 76 211 84 C ATOM 752 OG SER A 82 8.575 18.350 19.149 1.00 11.84 O ANISOU 752 OG SER A 82 2526 756 1215 96 266 285 O ATOM 753 N THR A 83 11.693 20.478 17.067 1.00 8.32 N ANISOU 753 N THR A 83 2033 586 543 74 -41 32 N ATOM 754 CA THR A 83 12.281 21.048 15.848 1.00 8.72 C ANISOU 754 CA THR A 83 2158 584 567 30 -7 27 C ATOM 755 C THR A 83 12.630 19.905 14.928 1.00 8.81 C ANISOU 755 C THR A 83 2211 518 615 64 107 95 C ATOM 756 O THR A 83 13.259 18.926 15.367 1.00 9.53 O ANISOU 756 O THR A 83 2372 663 583 205 -17 12 O ATOM 757 CB THR A 83 13.564 21.881 16.172 1.00 10.38 C ANISOU 757 CB THR A 83 2163 680 1101 -86 120 -49 C ATOM 758 OG1 THR A 83 13.301 22.783 17.219 1.00 11.93 O ANISOU 758 OG1 THR A 83 2474 825 1234 -238 8 -274 O ATOM 759 CG2 THR A 83 13.999 22.598 14.940 1.00 13.53 C ANISOU 759 CG2 THR A 83 2788 855 1494 -199 294 -93 C ATOM 760 N ILE A 84 12.190 19.989 13.674 1.00 8.31 N ANISOU 760 N ILE A 84 2185 517 455 99 -26 -9 N ATOM 761 CA ILE A 84 12.431 18.961 12.698 1.00 8.42 C ANISOU 761 CA ILE A 84 2241 449 508 106 21 43 C ATOM 762 C ILE A 84 13.227 19.573 11.570 1.00 8.95 C ANISOU 762 C ILE A 84 2329 575 494 -8 69 -3 C ATOM 763 O ILE A 84 12.881 20.626 11.033 1.00 9.08 O ANISOU 763 O ILE A 84 2325 476 646 70 15 108 O ATOM 764 CB ILE A 84 11.117 18.343 12.182 1.00 9.05 C ANISOU 764 CB ILE A 84 2310 567 559 101 49 99 C ATOM 765 CG1 ILE A 84 10.338 17.770 13.381 1.00 8.71 C ANISOU 765 CG1 ILE A 84 2127 628 553 75 -36 151 C ATOM 766 CG2 ILE A 84 11.411 17.267 11.130 1.00 9.85 C ANISOU 766 CG2 ILE A 84 2356 702 683 79 128 -59 C ATOM 767 CD1 ILE A 84 9.042 17.192 13.046 1.00 10.10 C ANISOU 767 CD1 ILE A 84 2214 895 727 23 91 213 C ATOM 768 N THR A 85 14.323 18.892 11.203 1.00 9.27 N ANISOU 768 N THR A 85 2365 549 608 52 174 86 N ATOM 769 CA THR A 85 15.215 19.304 10.116 1.00 9.90 C ANISOU 769 CA THR A 85 2360 696 705 26 134 -8 C ATOM 770 C THR A 85 15.457 18.104 9.216 1.00 9.92 C ANISOU 770 C THR A 85 2455 557 756 -75 195 66 C ATOM 771 O THR A 85 15.125 16.974 9.541 1.00 10.86 O ANISOU 771 O THR A 85 2773 653 699 39 382 24 O ATOM 772 CB THR A 85 16.518 19.823 10.660 1.00 11.33 C ANISOU 772 CB THR A 85 2376 849 1079 41 249 4 C ATOM 773 OG1 THR A 85 17.101 18.840 11.501 1.00 14.41 O ANISOU 773 OG1 THR A 85 2719 1319 1435 235 -114 -68 O ATOM 774 CG2 THR A 85 16.314 21.176 11.394 1.00 13.35 C ANISOU 774 CG2 THR A 85 2624 983 1464 -131 125 -440 C ATOM 775 N ALEU A 86 15.744 18.408 7.944 0.50 10.20 N ANISOU 775 N ALEU A 86 2417 693 764 -111 307 36 N ATOM 776 N BLEU A 86 16.243 18.315 8.147 0.50 10.26 N ANISOU 776 N BLEU A 86 2327 745 825 -89 359 -25 N ATOM 777 CA ALEU A 86 16.158 17.413 6.960 0.50 10.81 C ANISOU 777 CA ALEU A 86 2351 863 893 -118 255 -106 C ATOM 778 CA BLEU A 86 16.827 17.225 7.358 0.50 10.50 C ANISOU 778 CA BLEU A 86 2157 789 1043 -146 300 -240 C ATOM 779 C ALEU A 86 17.673 17.400 6.865 0.50 12.63 C ANISOU 779 C ALEU A 86 2372 1022 1402 -124 358 -133 C ATOM 780 C BLEU A 86 18.317 17.154 7.616 0.50 10.88 C ANISOU 780 C BLEU A 86 2123 883 1127 -177 386 -96 C ATOM 781 O ALEU A 86 18.262 18.395 6.403 0.50 16.36 O ANISOU 781 O ALEU A 86 2857 1044 2315 -212 625 -160 O ATOM 782 O BLEU A 86 18.986 18.201 7.619 0.50 13.44 O ANISOU 782 O BLEU A 86 2459 1065 1581 -340 363 -317 O ATOM 783 CB ALEU A 86 15.604 17.730 5.619 0.50 12.23 C ANISOU 783 CB ALEU A 86 2570 1176 899 -226 77 87 C ATOM 784 CB BLEU A 86 16.579 17.452 5.868 0.50 10.61 C ANISOU 784 CB BLEU A 86 2159 1000 870 -103 570 32 C ATOM 785 CG ALEU A 86 14.490 16.905 5.040 0.50 16.65 C ANISOU 785 CG ALEU A 86 2809 1676 1840 -316 -325 110 C ATOM 786 CG BLEU A 86 15.135 17.247 5.442 0.50 10.83 C ANISOU 786 CG BLEU A 86 2318 1017 779 -497 130 -11 C ATOM 787 CD1ALEU A 86 14.200 17.462 3.635 0.50 15.83 C ANISOU 787 CD1ALEU A 86 2846 1596 1572 -239 -353 312 C ATOM 788 CD1BLEU A 86 14.921 17.864 4.058 0.50 12.81 C ANISOU 788 CD1BLEU A 86 2676 1225 965 23 421 5 C ATOM 789 CD2ALEU A 86 14.775 15.387 5.034 0.50 14.65 C ANISOU 789 CD2ALEU A 86 3171 1108 1286 -329 -134 -116 C ATOM 790 CD2BLEU A 86 14.842 15.701 5.362 0.50 13.81 C ANISOU 790 CD2BLEU A 86 3081 1215 950 -167 472 -10 C ATOM 791 N AASP A 87 18.297 16.288 7.251 0.50 12.56 N ANISOU 791 N AASP A 87 2314 1141 1315 -78 336 -343 N ATOM 792 N BASP A 87 18.831 15.919 7.764 0.50 11.50 N ANISOU 792 N BASP A 87 1952 1161 1255 -224 257 -235 N ATOM 793 CA AASP A 87 19.753 16.158 7.343 0.50 14.88 C ANISOU 793 CA AASP A 87 2472 1640 1538 -134 196 -440 C ATOM 794 CA BASP A 87 20.251 15.611 7.828 0.50 12.96 C ANISOU 794 CA BASP A 87 2144 1345 1434 -133 108 -182 C ATOM 795 C AASP A 87 20.124 15.040 6.400 0.50 13.97 C ANISOU 795 C AASP A 87 2382 1590 1334 -102 215 -365 C ATOM 796 C BASP A 87 20.455 14.689 6.656 0.50 12.82 C ANISOU 796 C BASP A 87 2213 1333 1322 -96 127 -74 C ATOM 797 O AASP A 87 19.938 13.852 6.681 0.50 14.65 O ANISOU 797 O AASP A 87 2523 1577 1466 -340 213 -248 O ATOM 798 O BASP A 87 20.096 13.514 6.713 0.50 14.54 O ANISOU 798 O BASP A 87 2444 1372 1706 -219 272 -10 O ATOM 799 CB AASP A 87 20.174 15.873 8.800 0.50 17.02 C ANISOU 799 CB AASP A 87 2738 1941 1785 -131 175 -481 C ATOM 800 CB BASP A 87 20.607 14.893 9.138 0.50 14.85 C ANISOU 800 CB BASP A 87 2280 1738 1623 -112 40 12 C ATOM 801 CG AASP A 87 21.662 15.551 8.965 0.50 21.82 C ANISOU 801 CG AASP A 87 3146 2637 2506 -42 -26 -285 C ATOM 802 CG BASP A 87 22.048 14.418 9.185 0.50 18.69 C ANISOU 802 CG BASP A 87 2869 2000 2230 82 -43 -270 C ATOM 803 OD1AASP A 87 22.496 15.982 8.138 0.50 26.95 O ANISOU 803 OD1AASP A 87 3809 3125 3303 -122 118 -123 O ATOM 804 OD1BASP A 87 22.852 14.868 8.352 0.50 23.37 O ANISOU 804 OD1BASP A 87 2859 2958 3061 40 -147 64 O ATOM 805 OD2AASP A 87 22.008 14.858 9.948 0.50 27.97 O ANISOU 805 OD2AASP A 87 4028 3532 3064 65 85 44 O ATOM 806 OD2BASP A 87 22.384 13.614 10.082 0.50 24.26 O ANISOU 806 OD2BASP A 87 3245 2998 2973 82 -296 208 O ATOM 807 N AGLY A 88 20.598 15.430 5.221 0.50 12.75 N ANISOU 807 N AGLY A 88 2244 1380 1219 -121 244 -199 N ATOM 808 N BGLY A 88 20.986 15.204 5.556 0.50 13.05 N ANISOU 808 N BGLY A 88 2104 1231 1622 -78 316 7 N ATOM 809 CA AGLY A 88 20.738 14.525 4.153 0.50 13.85 C ANISOU 809 CA AGLY A 88 2299 1642 1319 -59 342 -138 C ATOM 810 CA BGLY A 88 21.188 14.345 4.411 0.50 14.05 C ANISOU 810 CA BGLY A 88 2295 1614 1428 -81 192 -26 C ATOM 811 C AGLY A 88 19.341 14.147 3.835 0.50 13.01 C ANISOU 811 C AGLY A 88 2289 1622 1031 -119 377 -224 C ATOM 812 C BGLY A 88 20.030 13.392 4.096 0.50 13.32 C ANISOU 812 C BGLY A 88 2281 1671 1107 19 266 -75 C ATOM 813 O AGLY A 88 18.488 14.991 3.712 0.50 14.27 O ANISOU 813 O AGLY A 88 2576 1815 1030 -2 293 153 O ATOM 814 O BGLY A 88 20.231 12.167 4.033 0.50 14.89 O ANISOU 814 O BGLY A 88 2653 1599 1405 118 114 -320 O ATOM 815 N AGLY A 89 19.124 12.846 3.671 0.50 12.97 N ANISOU 815 N AGLY A 89 2288 1680 957 -275 494 -320 N ATOM 816 N BGLY A 89 18.835 13.925 3.838 0.50 13.73 N ANISOU 816 N BGLY A 89 2384 1882 947 48 404 0 N ATOM 817 CA AGLY A 89 17.814 12.229 3.459 0.50 13.88 C ANISOU 817 CA AGLY A 89 2452 1850 968 -317 312 -547 C ATOM 818 CA BGLY A 89 17.725 13.085 3.430 0.50 12.98 C ANISOU 818 CA BGLY A 89 2574 1745 610 -34 373 -185 C ATOM 819 C AGLY A 89 17.051 11.864 4.705 0.50 14.07 C ANISOU 819 C AGLY A 89 2456 1811 1076 -430 361 -573 C ATOM 820 C BGLY A 89 16.972 12.335 4.580 0.50 13.88 C ANISOU 820 C BGLY A 89 2472 1888 914 -260 262 -240 C ATOM 821 O AGLY A 89 16.083 11.097 4.651 0.50 15.59 O ANISOU 821 O AGLY A 89 2599 2167 1157 -398 218 -850 O ATOM 822 O BGLY A 89 15.959 11.735 4.299 0.50 15.35 O ANISOU 822 O BGLY A 89 2597 2461 773 -499 14 -308 O ATOM 823 N VAL A 90 17.454 12.383 5.854 1.00 12.72 N ANISOU 823 N VAL A 90 2431 1577 823 -365 338 -383 N ATOM 824 CA VAL A 90 16.825 11.897 7.060 1.00 11.60 C ANISOU 824 CA VAL A 90 2361 1140 906 -282 367 -284 C ATOM 825 C VAL A 90 16.098 13.017 7.741 1.00 9.88 C ANISOU 825 C VAL A 90 2295 830 630 -128 150 -146 C ATOM 826 O VAL A 90 16.660 14.094 7.971 1.00 10.87 O ANISOU 826 O VAL A 90 2557 800 772 -200 283 -125 O ATOM 827 CB VAL A 90 17.884 11.316 8.043 1.00 12.48 C ANISOU 827 CB VAL A 90 2517 964 1261 -112 399 -153 C ATOM 828 CG1 VAL A 90 17.236 10.817 9.314 1.00 12.35 C ANISOU 828 CG1 VAL A 90 2430 1039 1222 11 261 93 C ATOM 829 CG2 VAL A 90 18.700 10.222 7.402 1.00 15.83 C ANISOU 829 CG2 VAL A 90 2615 1348 2050 53 649 -388 C ATOM 830 N LEU A 91 14.808 12.825 8.043 1.00 9.38 N ANISOU 830 N LEU A 91 2290 723 551 -201 106 -110 N ATOM 831 CA LEU A 91 14.089 13.795 8.855 1.00 9.26 C ANISOU 831 CA LEU A 91 2223 632 663 -45 47 148 C ATOM 832 C LEU A 91 14.483 13.548 10.323 1.00 8.76 C ANISOU 832 C LEU A 91 2150 703 475 128 176 91 C ATOM 833 O LEU A 91 14.310 12.430 10.820 1.00 9.40 O ANISOU 833 O LEU A 91 2441 596 532 31 156 56 O ATOM 834 CB LEU A 91 12.601 13.630 8.702 1.00 11.00 C ANISOU 834 CB LEU A 91 2465 858 853 -4 51 360 C ATOM 835 CG LEU A 91 11.936 14.199 7.471 1.00 12.14 C ANISOU 835 CG LEU A 91 2659 1135 817 32 27 -92 C ATOM 836 CD1 LEU A 91 10.551 13.658 7.343 1.00 14.83 C ANISOU 836 CD1 LEU A 91 2759 1586 1288 8 -3 56 C ATOM 837 CD2 LEU A 91 11.923 15.686 7.596 1.00 12.74 C ANISOU 837 CD2 LEU A 91 2568 661 1608 223 18 160 C ATOM 838 N VAL A 92 14.982 14.587 10.969 1.00 9.01 N ANISOU 838 N VAL A 92 2292 631 499 143 108 32 N ATOM 839 CA VAL A 92 15.483 14.493 12.332 1.00 9.29 C ANISOU 839 CA VAL A 92 2279 686 564 179 95 30 C ATOM 840 C VAL A 92 14.558 15.332 13.218 1.00 8.90 C ANISOU 840 C VAL A 92 2386 435 558 214 -31 39 C ATOM 841 O VAL A 92 14.513 16.582 13.030 1.00 10.19 O ANISOU 841 O VAL A 92 2515 640 717 182 202 93 O ATOM 842 CB VAL A 92 16.936 14.945 12.427 1.00 10.47 C ANISOU 842 CB VAL A 92 2320 1012 643 193 15 -72 C ATOM 843 CG1 VAL A 92 17.456 14.868 13.877 1.00 12.44 C ANISOU 843 CG1 VAL A 92 2336 1387 1002 94 10 -4 C ATOM 844 CG2 VAL A 92 17.853 14.155 11.490 1.00 12.21 C ANISOU 844 CG2 VAL A 92 2364 1273 1003 194 164 -211 C ATOM 845 N HIS A 93 13.891 14.720 14.142 1.00 8.83 N ANISOU 845 N HIS A 93 2516 358 478 225 57 73 N ATOM 846 CA HIS A 93 12.856 15.344 14.988 1.00 8.85 C ANISOU 846 CA HIS A 93 2260 598 505 217 78 138 C ATOM 847 C HIS A 93 13.324 15.301 16.418 1.00 8.94 C ANISOU 847 C HIS A 93 2334 587 473 247 74 78 C ATOM 848 O HIS A 93 13.397 14.227 17.015 1.00 9.43 O ANISOU 848 O HIS A 93 2546 519 518 141 -68 80 O ATOM 849 CB HIS A 93 11.572 14.572 14.766 1.00 9.22 C ANISOU 849 CB HIS A 93 2315 673 514 266 41 143 C ATOM 850 CG HIS A 93 10.374 14.969 15.538 1.00 9.96 C ANISOU 850 CG HIS A 93 2261 786 736 222 -31 297 C ATOM 851 ND1 HIS A 93 9.213 14.256 15.309 1.00 12.08 N ANISOU 851 ND1 HIS A 93 2350 1195 1045 394 221 407 N ATOM 852 CD2 HIS A 93 10.098 15.928 16.476 1.00 10.55 C ANISOU 852 CD2 HIS A 93 2502 737 770 354 201 227 C ATOM 853 CE1 HIS A 93 8.275 14.755 16.065 1.00 12.71 C ANISOU 853 CE1 HIS A 93 2531 1225 1072 359 185 398 C ATOM 854 NE2 HIS A 93 8.756 15.774 16.777 1.00 12.85 N ANISOU 854 NE2 HIS A 93 2694 1191 995 657 501 529 N ATOM 855 N VAL A 94 13.643 16.468 16.980 1.00 8.88 N ANISOU 855 N VAL A 94 2313 564 495 171 22 8 N ATOM 856 CA VAL A 94 14.127 16.557 18.353 1.00 9.09 C ANISOU 856 CA VAL A 94 2280 630 541 108 24 26 C ATOM 857 C VAL A 94 13.012 17.122 19.203 1.00 8.60 C ANISOU 857 C VAL A 94 2315 396 554 103 -35 47 C ATOM 858 O VAL A 94 12.462 18.165 18.875 1.00 10.42 O ANISOU 858 O VAL A 94 2604 670 685 260 264 212 O ATOM 859 CB VAL A 94 15.409 17.392 18.438 1.00 10.30 C ANISOU 859 CB VAL A 94 2256 716 940 63 30 0 C ATOM 860 CG1 VAL A 94 15.939 17.444 19.858 1.00 13.97 C ANISOU 860 CG1 VAL A 94 2380 1765 1161 -62 -235 -241 C ATOM 861 CG2 VAL A 94 16.480 16.936 17.453 1.00 14.34 C ANISOU 861 CG2 VAL A 94 2742 1373 1333 246 174 115 C ATOM 862 N GLN A 95 12.689 16.430 20.301 1.00 8.68 N ANISOU 862 N GLN A 95 2324 429 543 199 -57 41 N ATOM 863 CA GLN A 95 11.674 16.855 21.272 1.00 8.84 C ANISOU 863 CA GLN A 95 2321 540 498 83 23 14 C ATOM 864 C GLN A 95 12.366 17.183 22.583 1.00 9.33 C ANISOU 864 C GLN A 95 2378 605 559 45 -10 37 C ATOM 865 O GLN A 95 13.107 16.349 23.124 1.00 10.49 O ANISOU 865 O GLN A 95 2600 725 659 176 -98 -21 O ATOM 866 CB GLN A 95 10.700 15.715 21.521 1.00 9.30 C ANISOU 866 CB GLN A 95 2361 619 553 82 67 69 C ATOM 867 CG GLN A 95 9.888 15.289 20.312 1.00 9.53 C ANISOU 867 CG GLN A 95 2323 638 659 152 -10 -9 C ATOM 868 CD GLN A 95 8.973 14.117 20.540 1.00 9.89 C ANISOU 868 CD GLN A 95 2307 616 833 -10 64 140 C ATOM 869 OE1 GLN A 95 7.969 13.955 19.770 1.00 12.45 O ANISOU 869 OE1 GLN A 95 2432 1143 1152 -28 -50 135 O ATOM 870 NE2 GLN A 95 9.284 13.267 21.442 1.00 9.68 N ANISOU 870 NE2 GLN A 95 2348 546 783 -46 -70 213 N ATOM 871 N LYS A 96 12.067 18.337 23.136 1.00 9.90 N ANISOU 871 N LYS A 96 2578 641 542 92 -122 -88 N ATOM 872 CA LYS A 96 12.625 18.823 24.397 1.00 11.01 C ANISOU 872 CA LYS A 96 2740 755 687 159 -96 -95 C ATOM 873 C LYS A 96 11.510 19.041 25.407 1.00 11.29 C ANISOU 873 C LYS A 96 2897 745 647 153 -133 -207 C ATOM 874 O LYS A 96 10.517 19.716 25.110 1.00 12.35 O ANISOU 874 O LYS A 96 3123 961 609 303 -3 -172 O ATOM 875 CB LYS A 96 13.329 20.171 24.189 1.00 12.92 C ANISOU 875 CB LYS A 96 2695 1159 1054 -9 -234 -112 C ATOM 876 CG LYS A 96 14.406 20.248 23.216 1.00 15.21 C ANISOU 876 CG LYS A 96 2926 1321 1530 46 21 -153 C ATOM 877 CD LYS A 96 15.584 19.362 23.503 1.00 16.03 C ANISOU 877 CD LYS A 96 3300 1310 1479 -81 -48 -307 C ATOM 878 CE LYS A 96 16.764 19.666 22.639 1.00 17.27 C ANISOU 878 CE LYS A 96 3004 1349 2208 -70 -111 -424 C ATOM 879 NZ LYS A 96 17.915 18.739 22.846 1.00 18.97 N ANISOU 879 NZ LYS A 96 3227 1283 2696 -144 115 25 N ATOM 880 N TRP A 97 11.689 18.546 26.623 1.00 11.87 N ANISOU 880 N TRP A 97 3116 794 599 189 -99 -104 N ATOM 881 CA TRP A 97 10.737 18.791 27.705 1.00 13.35 C ANISOU 881 CA TRP A 97 3358 1124 587 329 40 -67 C ATOM 882 C TRP A 97 11.427 18.476 29.016 1.00 14.99 C ANISOU 882 C TRP A 97 3751 1292 653 279 -11 -214 C ATOM 883 O TRP A 97 12.211 17.546 29.104 1.00 15.66 O ANISOU 883 O TRP A 97 4044 1265 638 365 -123 -96 O ATOM 884 CB TRP A 97 9.467 17.904 27.540 1.00 13.93 C ANISOU 884 CB TRP A 97 3216 1314 762 269 185 50 C ATOM 885 CG TRP A 97 9.643 16.458 27.930 1.00 13.39 C ANISOU 885 CG TRP A 97 3081 1165 841 118 346 19 C ATOM 886 CD1 TRP A 97 9.174 15.876 29.042 1.00 14.38 C ANISOU 886 CD1 TRP A 97 3079 1417 966 142 351 9 C ATOM 887 CD2 TRP A 97 10.438 15.456 27.265 1.00 11.89 C ANISOU 887 CD2 TRP A 97 2919 943 654 103 88 -94 C ATOM 888 NE1 TRP A 97 9.566 14.585 29.135 1.00 13.55 N ANISOU 888 NE1 TRP A 97 2969 1352 826 26 267 99 N ATOM 889 CE2 TRP A 97 10.380 14.308 28.069 1.00 12.82 C ANISOU 889 CE2 TRP A 97 2921 1193 755 -119 64 16 C ATOM 890 CE3 TRP A 97 11.190 15.405 26.092 1.00 11.60 C ANISOU 890 CE3 TRP A 97 2707 924 776 -121 40 -106 C ATOM 891 CZ2 TRP A 97 11.042 13.116 27.720 1.00 13.12 C ANISOU 891 CZ2 TRP A 97 2931 966 1088 -172 -28 120 C ATOM 892 CZ3 TRP A 97 11.841 14.234 25.784 1.00 12.06 C ANISOU 892 CZ3 TRP A 97 2828 956 798 -113 181 -241 C ATOM 893 CH2 TRP A 97 11.762 13.116 26.581 1.00 12.50 C ANISOU 893 CH2 TRP A 97 2677 1088 984 46 90 -175 C ATOM 894 N ASP A 98 11.074 19.257 30.039 1.00 16.40 N ANISOU 894 N ASP A 98 3931 1669 631 432 -52 -233 N ATOM 895 CA AASP A 98 11.533 19.042 31.409 0.50 18.51 C ANISOU 895 CA AASP A 98 3890 2207 934 289 -86 -383 C ATOM 896 CA BASP A 98 11.501 18.926 31.394 0.50 18.29 C ANISOU 896 CA BASP A 98 3882 2167 897 293 -57 -333 C ATOM 897 C ASP A 98 13.015 18.726 31.483 1.00 17.72 C ANISOU 897 C ASP A 98 3903 2156 671 142 -144 -524 C ATOM 898 O ASP A 98 13.452 17.886 32.284 1.00 21.21 O ANISOU 898 O ASP A 98 4416 2716 925 248 -343 -258 O ATOM 899 CB AASP A 98 10.729 17.944 32.111 0.50 19.89 C ANISOU 899 CB AASP A 98 4031 2499 1027 245 -26 -258 C ATOM 900 CB BASP A 98 10.772 17.647 31.892 0.50 19.34 C ANISOU 900 CB BASP A 98 3986 2531 830 258 52 -108 C ATOM 901 CG AASP A 98 9.242 18.261 32.229 0.50 22.11 C ANISOU 901 CG AASP A 98 4080 2945 1373 140 -25 -184 C ATOM 902 CG BASP A 98 10.739 17.537 33.425 0.50 22.67 C ANISOU 902 CG BASP A 98 4191 3109 1310 165 52 109 C ATOM 903 OD1AASP A 98 8.885 19.456 32.347 0.50 27.89 O ANISOU 903 OD1AASP A 98 4486 3371 2737 285 101 257 O ATOM 904 OD1BASP A 98 10.956 18.558 34.107 0.50 24.93 O ANISOU 904 OD1BASP A 98 4679 3777 1015 216 -9 -101 O ATOM 905 OD2AASP A 98 8.437 17.296 32.233 0.50 26.71 O ANISOU 905 OD2AASP A 98 4251 3743 2153 -64 72 -352 O ATOM 906 OD2BASP A 98 10.494 16.427 33.974 0.50 26.89 O ANISOU 906 OD2BASP A 98 4973 3931 1311 85 191 630 O ATOM 907 N GLY A 99 13.800 19.465 30.720 1.00 18.22 N ANISOU 907 N GLY A 99 3730 1971 1218 53 -363 -621 N ATOM 908 CA GLY A 99 15.208 19.310 30.653 1.00 18.19 C ANISOU 908 CA GLY A 99 3635 1835 1439 -3 -556 -651 C ATOM 909 C GLY A 99 15.736 18.046 29.986 1.00 18.35 C ANISOU 909 C GLY A 99 3567 1704 1700 57 -505 -657 C ATOM 910 O GLY A 99 16.947 17.817 30.003 1.00 20.61 O ANISOU 910 O GLY A 99 3527 2135 2170 -101 -788 -799 O ATOM 911 N LYS A 100 14.863 17.254 29.361 1.00 15.30 N ANISOU 911 N LYS A 100 3542 1381 890 63 -569 -528 N ATOM 912 CA LYS A 100 15.188 16.023 28.662 1.00 14.35 C ANISOU 912 CA LYS A 100 3239 1409 802 133 -472 -136 C ATOM 913 C LYS A 100 15.071 16.255 27.163 1.00 12.75 C ANISOU 913 C LYS A 100 3023 1010 811 -44 -456 -236 C ATOM 914 O LYS A 100 14.512 17.236 26.689 1.00 12.81 O ANISOU 914 O LYS A 100 3187 882 797 114 -364 -135 O ATOM 915 CB LYS A 100 14.204 14.934 29.091 1.00 14.28 C ANISOU 915 CB LYS A 100 3367 1380 678 190 -251 -21 C ATOM 916 CG LYS A 100 14.199 14.665 30.581 1.00 19.66 C ANISOU 916 CG LYS A 100 4019 2197 1254 94 -258 -5 C ATOM 917 CD LYS A 100 13.031 13.719 31.007 1.00 21.27 C ANISOU 917 CD LYS A 100 4073 2681 1324 168 62 307 C ATOM 918 CE LYS A 100 12.902 13.570 32.477 1.00 26.39 C ANISOU 918 CE LYS A 100 4491 3411 2121 44 198 141 C ATOM 919 NZ LYS A 100 11.476 13.319 32.878 1.00 32.53 N ANISOU 919 NZ LYS A 100 4750 4184 3423 -66 92 253 N ATOM 920 N SER A 101 15.590 15.285 26.414 1.00 12.02 N ANISOU 920 N SER A 101 2890 926 751 8 -482 -95 N ATOM 921 CA SER A 101 15.532 15.334 24.959 1.00 11.64 C ANISOU 921 CA SER A 101 2721 873 828 -66 -276 59 C ATOM 922 C SER A 101 15.449 13.930 24.408 1.00 10.40 C ANISOU 922 C SER A 101 2586 706 659 -52 -167 81 C ATOM 923 O SER A 101 16.076 13.003 24.921 1.00 11.82 O ANISOU 923 O SER A 101 2752 807 932 83 -462 42 O ATOM 924 CB SER A 101 16.834 15.946 24.466 1.00 12.98 C ANISOU 924 CB SER A 101 2755 999 1177 -136 -178 -163 C ATOM 925 OG SER A 101 16.840 16.162 23.113 1.00 15.00 O ANISOU 925 OG SER A 101 3074 1248 1375 -399 -144 -5 O ATOM 926 N THR A 102 14.679 13.752 23.325 1.00 9.48 N ANISOU 926 N THR A 102 2325 654 621 52 -208 30 N ATOM 927 CA THR A 102 14.665 12.526 22.550 1.00 8.91 C ANISOU 927 CA THR A 102 2254 544 586 79 -94 17 C ATOM 928 C THR A 102 14.656 12.904 21.078 1.00 8.85 C ANISOU 928 C THR A 102 2252 451 659 20 -176 117 C ATOM 929 O THR A 102 14.154 13.957 20.712 1.00 9.82 O ANISOU 929 O THR A 102 2482 620 629 180 14 89 O ATOM 930 CB THR A 102 13.471 11.668 22.960 1.00 9.77 C ANISOU 930 CB THR A 102 2409 703 598 75 -115 -10 C ATOM 931 OG1 THR A 102 13.547 10.378 22.330 1.00 10.27 O ANISOU 931 OG1 THR A 102 2336 616 949 0 -44 20 O ATOM 932 CG2 THR A 102 12.147 12.219 22.632 1.00 10.85 C ANISOU 932 CG2 THR A 102 2512 826 784 115 -35 -57 C ATOM 933 N THR A 103 15.198 12.015 20.245 1.00 9.02 N ANISOU 933 N THR A 103 2298 533 595 136 -94 53 N ATOM 934 CA THR A 103 15.290 12.253 18.805 1.00 9.47 C ANISOU 934 CA THR A 103 2384 575 638 169 -3 0 C ATOM 935 C THR A 103 14.619 11.096 18.084 1.00 9.74 C ANISOU 935 C THR A 103 2644 601 454 222 -44 12 C ATOM 936 O THR A 103 14.878 9.916 18.364 1.00 11.28 O ANISOU 936 O THR A 103 3015 520 747 269 -340 38 O ATOM 937 CB THR A 103 16.747 12.427 18.403 1.00 11.13 C ANISOU 937 CB THR A 103 2410 938 879 173 16 -10 C ATOM 938 OG1 THR A 103 17.281 13.597 19.047 1.00 13.87 O ANISOU 938 OG1 THR A 103 2565 1428 1276 -241 41 19 O ATOM 939 CG2 THR A 103 16.889 12.660 16.888 1.00 12.85 C ANISOU 939 CG2 THR A 103 2686 1357 836 155 76 133 C ATOM 940 N ILE A 104 13.777 11.444 17.122 1.00 8.90 N ANISOU 940 N ILE A 104 2510 403 467 176 -41 24 N ATOM 941 CA ILE A 104 13.103 10.505 16.238 1.00 8.86 C ANISOU 941 CA ILE A 104 2417 512 435 168 38 28 C ATOM 942 C ILE A 104 13.653 10.787 14.836 1.00 8.72 C ANISOU 942 C ILE A 104 2335 523 452 59 -16 24 C ATOM 943 O ILE A 104 13.482 11.898 14.333 1.00 9.91 O ANISOU 943 O ILE A 104 2764 510 489 265 79 92 O ATOM 944 CB ILE A 104 11.606 10.650 16.265 1.00 9.87 C ANISOU 944 CB ILE A 104 2472 730 545 79 68 86 C ATOM 945 CG1 ILE A 104 11.045 10.439 17.683 1.00 11.61 C ANISOU 945 CG1 ILE A 104 2399 1211 801 -46 139 -40 C ATOM 946 CG2 ILE A 104 10.938 9.690 15.280 1.00 11.92 C ANISOU 946 CG2 ILE A 104 2696 1131 700 18 -55 -68 C ATOM 947 CD1 ILE A 104 9.635 10.839 17.792 1.00 15.91 C ANISOU 947 CD1 ILE A 104 2715 1975 1355 -27 338 115 C ATOM 948 N LYS A 105 14.255 9.780 14.212 1.00 8.71 N ANISOU 948 N LYS A 105 2365 505 439 122 -4 -44 N ATOM 949 CA LYS A 105 14.748 9.888 12.838 1.00 8.85 C ANISOU 949 CA LYS A 105 2333 559 469 118 -46 -2 C ATOM 950 C LYS A 105 13.866 9.084 11.941 1.00 8.76 C ANISOU 950 C LYS A 105 2374 497 457 132 46 -31 C ATOM 951 O LYS A 105 13.466 7.965 12.280 1.00 10.89 O ANISOU 951 O LYS A 105 2988 547 600 -119 -180 129 O ATOM 952 CB LYS A 105 16.201 9.420 12.737 1.00 10.47 C ANISOU 952 CB LYS A 105 2392 945 639 130 -23 -32 C ATOM 953 CG LYS A 105 17.210 10.402 13.421 1.00 13.94 C ANISOU 953 CG LYS A 105 2414 1552 1330 183 -105 -294 C ATOM 954 CD LYS A 105 18.656 10.068 13.221 1.00 18.94 C ANISOU 954 CD LYS A 105 2651 2658 1886 54 -37 -86 C ATOM 955 CE LYS A 105 19.565 11.064 13.901 1.00 23.92 C ANISOU 955 CE LYS A 105 2890 3118 3080 -93 -228 49 C ATOM 956 NZ LYS A 105 21.005 10.663 13.844 1.00 28.74 N ANISOU 956 NZ LYS A 105 3215 3689 4016 53 -263 93 N ATOM 957 N ARG A 106 13.562 9.622 10.770 1.00 8.59 N ANISOU 957 N ARG A 106 2348 457 456 -8 68 21 N ATOM 958 CA ARG A 106 12.710 8.936 9.773 1.00 9.26 C ANISOU 958 CA ARG A 106 2289 726 503 -99 39 111 C ATOM 959 C ARG A 106 13.497 8.927 8.460 1.00 8.99 C ANISOU 959 C ARG A 106 2238 744 431 -90 27 19 C ATOM 960 O ARG A 106 13.969 9.966 8.002 1.00 9.61 O ANISOU 960 O ARG A 106 2420 706 525 -156 51 38 O ATOM 961 CB ARG A 106 11.384 9.634 9.627 1.00 10.31 C ANISOU 961 CB ARG A 106 2332 1039 544 -228 0 3 C ATOM 962 CG ARG A 106 10.571 9.651 10.926 1.00 11.14 C ANISOU 962 CG ARG A 106 2290 1130 812 -88 106 62 C ATOM 963 CD ARG A 106 9.297 10.445 10.864 1.00 13.41 C ANISOU 963 CD ARG A 106 2325 1991 776 -267 141 -11 C ATOM 964 NE ARG A 106 8.449 10.354 12.059 1.00 13.97 N ANISOU 964 NE ARG A 106 2473 1771 1061 -257 150 -66 N ATOM 965 CZ ARG A 106 8.376 11.250 13.010 1.00 14.12 C ANISOU 965 CZ ARG A 106 2285 1892 1188 -29 97 74 C ATOM 966 NH1 ARG A 106 9.197 12.258 13.089 1.00 13.05 N ANISOU 966 NH1 ARG A 106 2320 1693 944 286 88 55 N ATOM 967 NH2 ARG A 106 7.490 11.105 13.992 1.00 16.37 N ANISOU 967 NH2 ARG A 106 2605 2526 1087 -220 538 14 N ATOM 968 N LYS A 107 13.618 7.747 7.860 1.00 9.19 N ANISOU 968 N LYS A 107 2284 723 483 -190 103 -51 N ATOM 969 CA LYS A 107 14.434 7.572 6.649 1.00 10.13 C ANISOU 969 CA LYS A 107 2295 902 651 -231 119 -201 C ATOM 970 C LYS A 107 13.779 6.548 5.763 1.00 9.54 C ANISOU 970 C LYS A 107 2354 759 509 -146 88 50 C ATOM 971 O LYS A 107 13.323 5.521 6.207 1.00 11.79 O ANISOU 971 O LYS A 107 2993 979 506 -493 126 -21 O ATOM 972 CB LYS A 107 15.844 7.157 7.021 1.00 12.71 C ANISOU 972 CB LYS A 107 2484 1380 964 -169 110 -503 C ATOM 973 CG LYS A 107 16.874 7.149 5.894 1.00 15.57 C ANISOU 973 CG LYS A 107 2594 1973 1348 -175 72 -492 C ATOM 974 CD LYS A 107 18.278 6.727 6.319 1.00 17.80 C ANISOU 974 CD LYS A 107 2610 2220 1930 128 294 -764 C ATOM 975 CE LYS A 107 19.353 7.231 5.286 1.00 22.62 C ANISOU 975 CE LYS A 107 3279 2923 2392 -24 337 -770 C ATOM 976 NZ LYS A 107 18.926 8.443 4.510 1.00 30.57 N ANISOU 976 NZ LYS A 107 4119 3391 4105 24 188 -511 N ATOM 977 N ARG A 108 13.873 6.775 4.454 1.00 9.58 N ANISOU 977 N ARG A 108 2336 762 540 -137 159 -27 N ATOM 978 CA ARG A 108 13.453 5.791 3.503 1.00 10.59 C ANISOU 978 CA ARG A 108 2339 1144 541 -188 185 -76 C ATOM 979 C ARG A 108 14.544 4.714 3.318 1.00 11.07 C ANISOU 979 C ARG A 108 2291 1222 690 -97 189 -352 C ATOM 980 O ARG A 108 15.721 5.038 3.092 1.00 13.43 O ANISOU 980 O ARG A 108 2371 1326 1403 -121 240 -540 O ATOM 981 CB ARG A 108 13.199 6.396 2.145 1.00 12.12 C ANISOU 981 CB ARG A 108 2640 1362 601 -274 104 40 C ATOM 982 CG ARG A 108 11.893 7.109 2.073 1.00 13.45 C ANISOU 982 CG ARG A 108 2730 1553 826 -131 105 271 C ATOM 983 CD ARG A 108 10.646 6.306 2.281 1.00 16.59 C ANISOU 983 CD ARG A 108 2918 2304 1082 -188 -209 712 C ATOM 984 NE ARG A 108 10.712 5.154 1.346 1.00 18.38 N ANISOU 984 NE ARG A 108 2926 1947 2108 51 -281 1051 N ATOM 985 CZ ARG A 108 10.424 5.213 0.044 1.00 15.63 C ANISOU 985 CZ ARG A 108 2633 878 2427 -106 0 -34 C ATOM 986 NH1 ARG A 108 9.900 6.325 -0.549 1.00 15.75 N ANISOU 986 NH1 ARG A 108 3001 1495 1486 130 -251 149 N ATOM 987 NH2 ARG A 108 10.603 4.166 -0.730 1.00 20.82 N ANISOU 987 NH2 ARG A 108 3126 2037 2746 127 -631 -254 N ATOM 988 N GLU A 109 14.157 3.442 3.347 1.00 10.94 N ANISOU 988 N GLU A 109 2293 1089 773 -86 107 -368 N ATOM 989 CA GLU A 109 15.047 2.293 3.144 1.00 11.67 C ANISOU 989 CA GLU A 109 2396 1192 845 51 132 -250 C ATOM 990 C GLU A 109 14.286 1.339 2.259 1.00 11.25 C ANISOU 990 C GLU A 109 2473 1073 726 10 141 -204 C ATOM 991 O GLU A 109 13.284 0.782 2.702 1.00 11.72 O ANISOU 991 O GLU A 109 2558 1273 621 -106 200 -141 O ATOM 992 CB GLU A 109 15.442 1.617 4.453 1.00 13.52 C ANISOU 992 CB GLU A 109 2572 1466 1097 159 -74 -222 C ATOM 993 CG GLU A 109 16.193 2.481 5.408 1.00 17.17 C ANISOU 993 CG GLU A 109 2961 2145 1418 162 -268 -162 C ATOM 994 CD GLU A 109 17.595 2.746 4.988 1.00 20.82 C ANISOU 994 CD GLU A 109 3414 2881 1615 -38 -235 -291 C ATOM 995 OE1 GLU A 109 18.271 3.478 5.735 1.00 24.80 O ANISOU 995 OE1 GLU A 109 3607 3383 2431 -294 38 -560 O ATOM 996 OE2 GLU A 109 18.025 2.214 3.936 1.00 25.41 O ANISOU 996 OE2 GLU A 109 3936 3327 2389 285 323 -538 O ATOM 997 N ASP A 110 14.724 1.169 1.020 1.00 10.63 N ANISOU 997 N ASP A 110 2386 1025 627 -28 207 -61 N ATOM 998 CA ASP A 110 13.965 0.359 0.066 1.00 10.74 C ANISOU 998 CA ASP A 110 2554 952 571 15 225 -31 C ATOM 999 C ASP A 110 12.551 0.897 0.000 1.00 10.44 C ANISOU 999 C ASP A 110 2340 1179 448 -108 199 -143 C ATOM 1000 O ASP A 110 12.390 2.141 -0.095 1.00 10.91 O ANISOU 1000 O ASP A 110 2538 904 701 10 166 -6 O ATOM 1001 CB ASP A 110 14.112 -1.134 0.370 1.00 11.91 C ANISOU 1001 CB ASP A 110 2639 1077 806 75 184 -96 C ATOM 1002 CG ASP A 110 15.544 -1.575 0.343 1.00 14.49 C ANISOU 1002 CG ASP A 110 2982 1210 1311 5 121 244 C ATOM 1003 OD1 ASP A 110 16.274 -1.167 -0.571 1.00 18.40 O ANISOU 1003 OD1 ASP A 110 3202 1875 1912 340 558 194 O ATOM 1004 OD2 ASP A 110 15.904 -2.454 1.143 1.00 22.37 O ANISOU 1004 OD2 ASP A 110 3428 2679 2390 760 291 943 O ATOM 1005 N ASP A 111 11.518 0.081 0.045 1.00 11.29 N ANISOU 1005 N ASP A 111 2586 1156 548 -45 95 -225 N ATOM 1006 CA ASP A 111 10.142 0.520 -0.009 1.00 11.52 C ANISOU 1006 CA ASP A 111 2634 1140 601 -75 123 -310 C ATOM 1007 C ASP A 111 9.586 0.890 1.364 1.00 12.09 C ANISOU 1007 C ASP A 111 2433 1253 905 -23 57 -326 C ATOM 1008 O ASP A 111 8.405 1.170 1.462 1.00 15.30 O ANISOU 1008 O ASP A 111 2715 1998 1098 223 -30 -721 O ATOM 1009 CB ASP A 111 9.267 -0.463 -0.729 1.00 12.70 C ANISOU 1009 CB ASP A 111 2658 1437 730 -127 71 -347 C ATOM 1010 CG ASP A 111 9.559 -0.516 -2.209 1.00 12.75 C ANISOU 1010 CG ASP A 111 2585 1450 807 -99 -12 -237 C ATOM 1011 OD1 ASP A 111 9.782 0.559 -2.811 1.00 15.41 O ANISOU 1011 OD1 ASP A 111 3526 1556 770 -365 1 -87 O ATOM 1012 OD2 ASP A 111 9.545 -1.620 -2.754 1.00 16.09 O ANISOU 1012 OD2 ASP A 111 3847 1489 778 -157 235 -368 O ATOM 1013 N LYS A 112 10.428 0.870 2.391 1.00 10.95 N ANISOU 1013 N LYS A 112 2482 1083 596 -136 191 -104 N ATOM 1014 CA LYS A 112 9.977 1.119 3.780 1.00 10.45 C ANISOU 1014 CA LYS A 112 2473 913 584 -70 251 -83 C ATOM 1015 C LYS A 112 10.319 2.511 4.214 1.00 9.66 C ANISOU 1015 C LYS A 112 2268 952 451 -102 34 98 C ATOM 1016 O LYS A 112 11.165 3.195 3.636 1.00 10.53 O ANISOU 1016 O LYS A 112 2407 921 671 -129 213 7 O ATOM 1017 CB LYS A 112 10.648 0.096 4.697 1.00 11.95 C ANISOU 1017 CB LYS A 112 2799 974 766 92 383 110 C ATOM 1018 CG LYS A 112 10.334 -1.330 4.290 1.00 15.59 C ANISOU 1018 CG LYS A 112 3271 1030 1622 130 511 72 C ATOM 1019 CD LYS A 112 10.869 -2.392 5.048 1.00 21.04 C ANISOU 1019 CD LYS A 112 4053 1919 2021 412 635 115 C ATOM 1020 CE LYS A 112 10.533 -3.781 4.372 1.00 25.30 C ANISOU 1020 CE LYS A 112 4431 2109 3070 199 462 156 C ATOM 1021 NZ LYS A 112 11.037 -4.924 5.134 1.00 30.21 N ANISOU 1021 NZ LYS A 112 4955 2744 3777 297 -74 -103 N ATOM 1022 N LEU A 113 9.655 2.917 5.291 1.00 9.40 N ANISOU 1022 N LEU A 113 2229 791 551 -146 104 -30 N ATOM 1023 CA ALEU A 113 9.995 4.120 6.031 0.50 9.56 C ANISOU 1023 CA ALEU A 113 2298 836 497 -37 90 -23 C ATOM 1024 CA BLEU A 113 9.974 4.113 6.040 0.50 9.52 C ANISOU 1024 CA BLEU A 113 2325 804 485 -22 62 -22 C ATOM 1025 C LEU A 113 10.355 3.640 7.431 1.00 9.41 C ANISOU 1025 C LEU A 113 2274 666 633 -121 149 -78 C ATOM 1026 O LEU A 113 9.525 3.049 8.129 1.00 10.55 O ANISOU 1026 O LEU A 113 2331 1030 647 -245 128 20 O ATOM 1027 CB ALEU A 113 8.824 5.092 5.981 0.50 10.30 C ANISOU 1027 CB ALEU A 113 2251 1050 610 -103 76 -142 C ATOM 1028 CB BLEU A 113 8.764 5.026 6.051 0.50 10.33 C ANISOU 1028 CB BLEU A 113 2347 848 728 -109 0 -12 C ATOM 1029 CG ALEU A 113 9.034 6.527 6.489 0.50 11.62 C ANISOU 1029 CG ALEU A 113 2331 1250 832 -124 199 -81 C ATOM 1030 CG BLEU A 113 8.967 6.298 6.866 0.50 11.56 C ANISOU 1030 CG BLEU A 113 2520 1242 628 31 -208 -246 C ATOM 1031 CD1ALEU A 113 7.832 7.383 6.075 0.50 10.88 C ANISOU 1031 CD1ALEU A 113 2499 775 858 48 13 -182 C ATOM 1032 CD1BLEU A 113 10.233 7.034 6.395 0.50 13.91 C ANISOU 1032 CD1BLEU A 113 2717 927 1640 -93 -342 12 C ATOM 1033 CD2ALEU A 113 9.246 6.605 7.965 0.50 12.16 C ANISOU 1033 CD2ALEU A 113 2089 1491 1038 -34 -45 -12 C ATOM 1034 CD2BLEU A 113 7.768 7.224 6.700 0.50 17.31 C ANISOU 1034 CD2BLEU A 113 2786 2035 1756 233 -93 -176 C ATOM 1035 N VAL A 114 11.631 3.822 7.772 1.00 9.10 N ANISOU 1035 N VAL A 114 2224 706 525 -87 68 73 N ATOM 1036 CA VAL A 114 12.165 3.364 9.062 1.00 9.75 C ANISOU 1036 CA VAL A 114 2254 801 647 -51 -27 124 C ATOM 1037 C VAL A 114 12.220 4.533 10.002 1.00 9.67 C ANISOU 1037 C VAL A 114 2316 766 590 -102 -76 115 C ATOM 1038 O VAL A 114 12.662 5.635 9.664 1.00 10.55 O ANISOU 1038 O VAL A 114 2635 783 587 -257 79 48 O ATOM 1039 CB VAL A 114 13.532 2.753 8.858 1.00 11.48 C ANISOU 1039 CB VAL A 114 2465 1048 848 24 -29 200 C ATOM 1040 CG1 VAL A 114 14.130 2.260 10.207 1.00 13.61 C ANISOU 1040 CG1 VAL A 114 2703 1343 1123 296 -18 276 C ATOM 1041 CG2 VAL A 114 13.512 1.583 7.848 1.00 14.00 C ANISOU 1041 CG2 VAL A 114 2841 1368 1109 299 73 -218 C ATOM 1042 N VAL A 115 11.726 4.301 11.218 1.00 9.94 N ANISOU 1042 N VAL A 115 2526 707 541 -290 39 92 N ATOM 1043 CA VAL A 115 11.627 5.280 12.270 1.00 10.13 C ANISOU 1043 CA VAL A 115 2641 629 576 -286 -53 34 C ATOM 1044 C VAL A 115 12.498 4.808 13.437 1.00 10.40 C ANISOU 1044 C VAL A 115 2731 730 491 -181 -44 161 C ATOM 1045 O VAL A 115 12.211 3.789 14.025 1.00 13.41 O ANISOU 1045 O VAL A 115 3149 1028 917 -537 -436 393 O ATOM 1046 CB VAL A 115 10.160 5.500 12.680 1.00 11.10 C ANISOU 1046 CB VAL A 115 2588 848 780 -274 35 82 C ATOM 1047 CG1 VAL A 115 10.043 6.566 13.769 1.00 13.35 C ANISOU 1047 CG1 VAL A 115 3128 1236 706 -147 72 -172 C ATOM 1048 CG2 VAL A 115 9.277 5.892 11.479 1.00 12.87 C ANISOU 1048 CG2 VAL A 115 2824 1128 934 -269 -177 42 C ATOM 1049 N AGLU A 116 13.502 5.615 13.799 0.50 9.22 N ANISOU 1049 N AGLU A 116 2573 391 539 -97 22 -160 N ATOM 1050 N BGLU A 116 13.579 5.519 13.723 0.50 9.98 N ANISOU 1050 N BGLU A 116 2536 825 430 -52 -22 166 N ATOM 1051 CA AGLU A 116 14.458 5.250 14.835 0.50 9.44 C ANISOU 1051 CA AGLU A 116 2446 524 615 43 18 31 C ATOM 1052 CA BGLU A 116 14.382 5.257 14.889 0.50 10.14 C ANISOU 1052 CA BGLU A 116 2470 661 720 88 -20 136 C ATOM 1053 C AGLU A 116 14.346 6.234 15.976 0.50 8.94 C ANISOU 1053 C AGLU A 116 2307 414 675 -17 -112 -16 C ATOM 1054 C BGLU A 116 14.079 6.260 15.947 0.50 8.60 C ANISOU 1054 C BGLU A 116 2245 507 516 194 -259 62 C ATOM 1055 O AGLU A 116 14.696 7.417 15.795 0.50 8.62 O ANISOU 1055 O AGLU A 116 2093 459 721 65 -224 -13 O ATOM 1056 O BGLU A 116 14.087 7.462 15.721 0.50 8.48 O ANISOU 1056 O BGLU A 116 2217 514 489 197 -263 182 O ATOM 1057 CB AGLU A 116 15.881 5.223 14.269 0.50 11.22 C ANISOU 1057 CB AGLU A 116 2555 859 849 208 13 42 C ATOM 1058 CB BGLU A 116 15.851 5.343 14.571 0.50 12.69 C ANISOU 1058 CB BGLU A 116 2651 1017 1153 156 -9 -8 C ATOM 1059 CG AGLU A 116 16.938 4.886 15.339 0.50 13.05 C ANISOU 1059 CG AGLU A 116 2590 1555 813 442 171 244 C ATOM 1060 CG BGLU A 116 16.446 4.116 13.991 0.50 16.46 C ANISOU 1060 CG BGLU A 116 2747 1524 1982 179 136 -2 C ATOM 1061 CD AGLU A 116 18.342 5.572 15.174 0.50 18.77 C ANISOU 1061 CD AGLU A 116 2956 2166 2009 301 -1 64 C ATOM 1062 CD BGLU A 116 17.968 4.101 14.170 0.50 20.49 C ANISOU 1062 CD BGLU A 116 2921 2168 2694 141 -30 -92 C ATOM 1063 OE1AGLU A 116 18.475 6.826 15.067 0.50 18.27 O ANISOU 1063 OE1AGLU A 116 2865 2255 1819 289 148 493 O ATOM 1064 OE1BGLU A 116 18.523 5.037 14.765 0.50 21.82 O ANISOU 1064 OE1BGLU A 116 2768 2960 2562 320 -462 -397 O ATOM 1065 OE2AGLU A 116 19.353 4.841 15.189 0.50 20.08 O ANISOU 1065 OE2AGLU A 116 2998 2695 1937 381 263 512 O ATOM 1066 OE2BGLU A 116 18.608 3.140 13.727 0.50 22.83 O ANISOU 1066 OE2BGLU A 116 3242 2658 2774 565 131 192 O ATOM 1067 N CYS A 117 13.844 5.765 17.135 1.00 9.02 N ANISOU 1067 N CYS A 117 2461 412 553 110 -117 103 N ATOM 1068 CA CYS A 117 13.546 6.598 18.297 1.00 9.70 C ANISOU 1068 CA CYS A 117 2421 665 598 191 -36 39 C ATOM 1069 C CYS A 117 14.666 6.395 19.299 1.00 9.58 C ANISOU 1069 C CYS A 117 2339 707 591 197 48 114 C ATOM 1070 O CYS A 117 14.904 5.249 19.704 1.00 10.42 O ANISOU 1070 O CYS A 117 2614 525 819 134 -309 141 O ATOM 1071 CB CYS A 117 12.215 6.137 18.934 1.00 11.42 C ANISOU 1071 CB CYS A 117 2398 1286 652 237 -212 -103 C ATOM 1072 SG CYS A 117 10.805 6.200 17.781 1.00 13.99 S ANISOU 1072 SG CYS A 117 2516 1774 1024 63 -259 224 S ATOM 1073 N VAL A 118 15.305 7.487 19.732 1.00 9.34 N ANISOU 1073 N VAL A 118 2350 529 669 106 -41 -32 N ATOM 1074 CA VAL A 118 16.504 7.379 20.565 1.00 9.63 C ANISOU 1074 CA VAL A 118 2209 584 864 54 -28 42 C ATOM 1075 C VAL A 118 16.327 8.207 21.809 1.00 9.64 C ANISOU 1075 C VAL A 118 2259 516 885 20 -108 49 C ATOM 1076 O VAL A 118 15.980 9.405 21.731 1.00 10.15 O ANISOU 1076 O VAL A 118 2507 516 831 148 -175 -1 O ATOM 1077 CB VAL A 118 17.770 7.805 19.814 1.00 12.63 C ANISOU 1077 CB VAL A 118 2478 901 1419 53 175 -58 C ATOM 1078 CG1 VAL A 118 18.961 7.828 20.711 1.00 16.72 C ANISOU 1078 CG1 VAL A 118 2237 1877 2236 58 55 -26 C ATOM 1079 CG2 VAL A 118 18.043 6.897 18.667 1.00 15.78 C ANISOU 1079 CG2 VAL A 118 2734 1404 1855 58 409 -167 C ATOM 1080 N AMET A 119 16.333 7.565 22.968 0.50 8.64 N ANISOU 1080 N AMET A 119 1946 437 897 60 -81 138 N ATOM 1081 N BMET A 119 16.833 7.702 22.933 0.50 9.41 N ANISOU 1081 N BMET A 119 2110 667 796 145 -83 34 N ATOM 1082 CA AMET A 119 16.392 8.239 24.249 0.50 8.69 C ANISOU 1082 CA AMET A 119 1777 631 893 23 -86 39 C ATOM 1083 CA BMET A 119 17.037 8.504 24.118 0.50 10.85 C ANISOU 1083 CA BMET A 119 2316 865 940 10 -168 -152 C ATOM 1084 C AMET A 119 17.698 7.758 24.923 0.50 9.77 C ANISOU 1084 C AMET A 119 2074 871 763 80 -220 -21 C ATOM 1085 C BMET A 119 18.051 7.847 25.006 0.50 11.99 C ANISOU 1085 C BMET A 119 2387 1087 1079 113 -401 -206 C ATOM 1086 O AMET A 119 17.859 6.577 25.244 0.50 10.13 O ANISOU 1086 O AMET A 119 2154 908 784 155 -135 -121 O ATOM 1087 O BMET A 119 17.804 6.725 25.506 0.50 11.85 O ANISOU 1087 O BMET A 119 2740 661 1099 368 -542 -31 O ATOM 1088 CB AMET A 119 15.158 7.903 25.055 0.50 8.61 C ANISOU 1088 CB AMET A 119 1947 633 691 33 -59 111 C ATOM 1089 CB BMET A 119 15.734 8.625 24.887 0.50 11.07 C ANISOU 1089 CB BMET A 119 2133 1235 837 -8 -239 137 C ATOM 1090 CG AMET A 119 15.131 8.563 26.436 0.50 9.35 C ANISOU 1090 CG AMET A 119 2221 678 651 -107 -228 195 C ATOM 1091 CG BMET A 119 15.856 9.718 25.988 0.50 13.61 C ANISOU 1091 CG BMET A 119 2373 1833 965 123 -324 81 C ATOM 1092 SD AMET A 119 15.021 10.366 26.221 0.50 10.93 S ANISOU 1092 SD AMET A 119 2411 845 895 219 26 119 S ATOM 1093 SD BMET A 119 14.289 10.017 26.771 0.50 14.85 S ANISOU 1093 SD BMET A 119 2838 1477 1325 53 76 -249 S ATOM 1094 CE AMET A 119 15.005 10.821 27.956 0.50 14.39 C ANISOU 1094 CE AMET A 119 3038 848 1581 78 201 -475 C ATOM 1095 CE BMET A 119 14.755 11.126 28.122 0.50 15.34 C ANISOU 1095 CE BMET A 119 3036 1737 1053 450 -150 -308 C ATOM 1096 N ALYS A 120 18.651 8.673 25.105 0.50 11.42 N ANISOU 1096 N ALYS A 120 2021 915 1401 115 -375 187 N ATOM 1097 N BLYS A 120 19.127 8.571 25.304 0.50 15.29 N ANISOU 1097 N BLYS A 120 2411 1446 1950 109 -303 3 N ATOM 1098 CA ALYS A 120 19.979 8.320 25.674 0.50 11.81 C ANISOU 1098 CA ALYS A 120 2111 1047 1328 -45 -372 245 C ATOM 1099 CA BLYS A 120 20.041 8.130 26.368 0.50 17.72 C ANISOU 1099 CA BLYS A 120 2598 2036 2096 58 -226 72 C ATOM 1100 C ALYS A 120 20.553 7.083 24.957 0.50 10.26 C ANISOU 1100 C ALYS A 120 2065 547 1286 -13 -341 247 C ATOM 1101 C BLYS A 120 20.508 6.682 26.219 0.50 18.47 C ANISOU 1101 C BLYS A 120 2639 2149 2227 37 -189 129 C ATOM 1102 O ALYS A 120 20.731 7.124 23.734 0.50 12.11 O ANISOU 1102 O ALYS A 120 2171 950 1478 -10 -102 570 O ATOM 1103 O BLYS A 120 20.401 5.906 27.156 0.50 21.27 O ANISOU 1103 O BLYS A 120 3039 2457 2583 -22 -155 175 O ATOM 1104 CB ALYS A 120 19.902 8.162 27.210 0.50 11.64 C ANISOU 1104 CB ALYS A 120 2171 944 1304 15 -195 -11 C ATOM 1105 CB BLYS A 120 19.333 8.151 27.711 0.50 17.43 C ANISOU 1105 CB BLYS A 120 2524 1884 2212 97 -253 141 C ATOM 1106 CG ALYS A 120 19.557 9.473 27.855 0.50 13.27 C ANISOU 1106 CG ALYS A 120 2175 1462 1402 21 -431 -209 C ATOM 1107 CG BLYS A 120 18.797 9.434 28.182 0.50 19.66 C ANISOU 1107 CG BLYS A 120 2564 2419 2486 133 -256 -6 C ATOM 1108 CD ALYS A 120 19.179 9.317 29.283 0.50 17.96 C ANISOU 1108 CD ALYS A 120 2700 2317 1805 72 15 0 C ATOM 1109 CD BLYS A 120 18.218 9.189 29.540 0.50 23.56 C ANISOU 1109 CD BLYS A 120 3020 3119 2809 -46 -49 -140 C ATOM 1110 CE ALYS A 120 20.399 9.149 30.162 0.50 22.47 C ANISOU 1110 CE ALYS A 120 2820 3047 2670 71 -68 -117 C ATOM 1111 CE BLYS A 120 19.317 8.711 30.486 0.50 24.72 C ANISOU 1111 CE BLYS A 120 3324 3338 2728 -165 -50 8 C ATOM 1112 NZ ALYS A 120 21.408 10.168 29.747 0.50 25.18 N ANISOU 1112 NZ ALYS A 120 3111 3213 3242 4 47 -26 N ATOM 1113 NZ BLYS A 120 18.796 7.793 31.529 0.50 26.78 N ANISOU 1113 NZ BLYS A 120 3764 3610 2800 -266 127 53 N ATOM 1114 N AGLY A 121 20.882 6.015 25.691 0.50 10.59 N ANISOU 1114 N AGLY A 121 2025 909 1087 50 -195 412 N ATOM 1115 N BGLY A 121 21.003 6.293 25.059 0.50 17.64 N ANISOU 1115 N BGLY A 121 2486 2103 2112 -6 -109 140 N ATOM 1116 CA AGLY A 121 21.469 4.828 25.112 0.50 12.72 C ANISOU 1116 CA AGLY A 121 2128 1244 1461 -9 -198 387 C ATOM 1117 CA BGLY A 121 21.496 4.939 24.863 0.50 16.09 C ANISOU 1117 CA BGLY A 121 2341 1841 1929 -12 -106 259 C ATOM 1118 C GLY A 121 20.480 3.893 24.458 1.00 11.97 C ANISOU 1118 C GLY A 121 2083 1173 1289 129 -107 372 C ATOM 1119 O GLY A 121 20.875 2.803 24.041 1.00 13.47 O ANISOU 1119 O GLY A 121 2303 1277 1539 391 47 337 O ATOM 1120 N VAL A 122 19.193 4.215 24.557 1.00 11.16 N ANISOU 1120 N VAL A 122 2190 925 1123 145 -135 163 N ATOM 1121 CA VAL A 122 18.122 3.263 24.160 1.00 10.29 C ANISOU 1121 CA VAL A 122 2240 786 880 247 -95 131 C ATOM 1122 C VAL A 122 17.528 3.667 22.835 1.00 10.15 C ANISOU 1122 C VAL A 122 2288 532 1035 125 -188 128 C ATOM 1123 O VAL A 122 17.070 4.803 22.673 1.00 11.67 O ANISOU 1123 O VAL A 122 2712 744 975 285 -382 -3 O ATOM 1124 CB VAL A 122 17.036 3.217 25.233 1.00 11.54 C ANISOU 1124 CB VAL A 122 2233 978 1173 269 -81 204 C ATOM 1125 CG1 VAL A 122 15.927 2.251 24.825 1.00 14.30 C ANISOU 1125 CG1 VAL A 122 2482 1307 1643 222 124 139 C ATOM 1126 CG2 VAL A 122 17.625 2.768 26.564 1.00 13.67 C ANISOU 1126 CG2 VAL A 122 2530 1527 1135 257 36 384 C ATOM 1127 N THR A 123 17.545 2.754 21.892 1.00 10.42 N ANISOU 1127 N THR A 123 2284 606 1069 188 -221 67 N ATOM 1128 CA THR A 123 16.977 2.963 20.577 1.00 10.37 C ANISOU 1128 CA THR A 123 2441 625 874 141 -132 109 C ATOM 1129 C THR A 123 15.818 1.980 20.360 1.00 11.00 C ANISOU 1129 C THR A 123 2637 627 915 54 -286 108 C ATOM 1130 O THR A 123 15.886 0.796 20.721 1.00 14.06 O ANISOU 1130 O THR A 123 2947 724 1670 -74 -507 471 O ATOM 1131 CB THR A 123 18.044 2.698 19.519 1.00 12.93 C ANISOU 1131 CB THR A 123 2624 1144 1142 100 19 56 C ATOM 1132 OG1 THR A 123 19.100 3.609 19.736 1.00 16.02 O ANISOU 1132 OG1 THR A 123 2983 1517 1584 -111 366 -65 O ATOM 1133 CG2 THR A 123 17.512 2.871 18.115 1.00 14.90 C ANISOU 1133 CG2 THR A 123 2802 1853 1006 154 137 94 C ATOM 1134 N SER A 124 14.775 2.453 19.711 1.00 10.62 N ANISOU 1134 N SER A 124 2728 454 853 -6 -293 115 N ATOM 1135 CA SER A 124 13.737 1.593 19.147 1.00 10.78 C ANISOU 1135 CA SER A 124 2661 584 850 33 -180 285 C ATOM 1136 C SER A 124 13.656 1.817 17.654 1.00 9.96 C ANISOU 1136 C SER A 124 2443 617 723 70 -66 173 C ATOM 1137 O SER A 124 13.697 2.939 17.188 1.00 11.74 O ANISOU 1137 O SER A 124 3148 581 732 -3 -195 189 O ATOM 1138 CB SER A 124 12.393 1.886 19.803 1.00 10.87 C ANISOU 1138 CB SER A 124 2665 669 796 -33 -99 179 C ATOM 1139 OG SER A 124 11.313 1.225 19.166 1.00 11.82 O ANISOU 1139 OG SER A 124 2768 798 922 55 -56 155 O ATOM 1140 N THR A 125 13.522 0.733 16.892 1.00 9.42 N ANISOU 1140 N THR A 125 2268 612 697 -9 -142 127 N ATOM 1141 CA THR A 125 13.375 0.797 15.479 1.00 9.99 C ANISOU 1141 CA THR A 125 2323 769 703 74 20 143 C ATOM 1142 C THR A 125 11.986 0.333 15.105 1.00 9.75 C ANISOU 1142 C THR A 125 2478 675 552 -117 -63 297 C ATOM 1143 O THR A 125 11.607 -0.807 15.448 1.00 11.82 O ANISOU 1143 O THR A 125 2839 786 863 -181 -206 306 O ATOM 1144 CB THR A 125 14.447 -0.052 14.776 1.00 12.57 C ANISOU 1144 CB THR A 125 2585 1144 1044 184 70 33 C ATOM 1145 OG1 THR A 125 15.750 0.411 15.166 1.00 15.72 O ANISOU 1145 OG1 THR A 125 2494 1498 1980 283 232 -126 O ATOM 1146 CG2 THR A 125 14.300 -0.030 13.264 1.00 15.05 C ANISOU 1146 CG2 THR A 125 3077 1660 980 311 230 8 C ATOM 1147 N ARG A 126 11.282 1.143 14.352 1.00 9.98 N ANISOU 1147 N ARG A 126 2368 760 661 -327 -30 208 N ATOM 1148 CA ARG A 126 9.885 0.906 13.940 1.00 11.16 C ANISOU 1148 CA ARG A 126 2441 1083 715 -399 -80 403 C ATOM 1149 C ARG A 126 9.833 0.990 12.422 1.00 10.62 C ANISOU 1149 C ARG A 126 2488 869 677 -256 -80 306 C ATOM 1150 O ARG A 126 10.323 1.947 11.847 1.00 14.21 O ANISOU 1150 O ARG A 126 3355 1326 717 -798 -228 309 O ATOM 1151 CB ARG A 126 8.982 1.918 14.608 1.00 12.06 C ANISOU 1151 CB ARG A 126 2283 1577 720 -254 -118 124 C ATOM 1152 CG ARG A 126 8.929 1.567 16.093 1.00 16.03 C ANISOU 1152 CG ARG A 126 2781 2267 1041 24 -161 36 C ATOM 1153 CD ARG A 126 8.242 2.479 16.935 1.00 16.20 C ANISOU 1153 CD ARG A 126 2622 2275 1259 -149 77 167 C ATOM 1154 NE ARG A 126 6.840 2.735 16.697 1.00 16.24 N ANISOU 1154 NE ARG A 126 2601 2564 1006 73 -31 -53 N ATOM 1155 CZ ARG A 126 5.791 2.136 17.273 1.00 15.90 C ANISOU 1155 CZ ARG A 126 2691 2466 884 -370 -282 -216 C ATOM 1156 NH1 ARG A 126 5.862 0.976 17.905 1.00 17.81 N ANISOU 1156 NH1 ARG A 126 3245 2698 824 -113 -266 23 N ATOM 1157 NH2 ARG A 126 4.619 2.665 17.113 1.00 16.91 N ANISOU 1157 NH2 ARG A 126 2843 2376 1206 -351 55 107 N ATOM 1158 N VAL A 127 9.311 -0.001 11.779 1.00 9.52 N ANISOU 1158 N VAL A 127 2221 756 640 -150 -12 160 N ATOM 1159 CA VAL A 127 9.321 -0.078 10.314 1.00 9.97 C ANISOU 1159 CA VAL A 127 2248 892 647 -120 20 130 C ATOM 1160 C VAL A 127 7.908 0.067 9.823 1.00 9.33 C ANISOU 1160 C VAL A 127 2186 731 626 -139 76 -20 C ATOM 1161 O VAL A 127 6.999 -0.684 10.239 1.00 10.07 O ANISOU 1161 O VAL A 127 2302 864 659 -153 -46 54 O ATOM 1162 CB VAL A 127 9.921 -1.400 9.861 1.00 11.56 C ANISOU 1162 CB VAL A 127 2504 998 890 155 -43 27 C ATOM 1163 CG1 VAL A 127 9.873 -1.451 8.302 1.00 13.39 C ANISOU 1163 CG1 VAL A 127 2716 1422 949 278 102 -207 C ATOM 1164 CG2 VAL A 127 11.344 -1.561 10.349 1.00 14.86 C ANISOU 1164 CG2 VAL A 127 2685 1619 1341 418 34 141 C ATOM 1165 N TYR A 128 7.717 1.005 8.896 1.00 8.95 N ANISOU 1165 N TYR A 128 2091 704 604 -136 10 87 N ATOM 1166 CA TYR A 128 6.458 1.215 8.225 1.00 9.16 C ANISOU 1166 CA TYR A 128 2114 734 631 -148 35 9 C ATOM 1167 C TYR A 128 6.562 0.804 6.747 1.00 9.83 C ANISOU 1167 C TYR A 128 2318 713 705 -112 -28 35 C ATOM 1168 O TYR A 128 7.612 1.015 6.115 1.00 10.46 O ANISOU 1168 O TYR A 128 2370 938 665 -170 83 -71 O ATOM 1169 CB TYR A 128 6.054 2.688 8.289 1.00 9.46 C ANISOU 1169 CB TYR A 128 2130 809 654 -142 34 69 C ATOM 1170 CG TYR A 128 5.630 3.206 9.664 1.00 8.91 C ANISOU 1170 CG TYR A 128 2023 770 592 -166 6 87 C ATOM 1171 CD1 TYR A 128 6.551 3.458 10.651 1.00 10.03 C ANISOU 1171 CD1 TYR A 128 2024 1009 776 -59 10 -101 C ATOM 1172 CD2 TYR A 128 4.297 3.418 9.934 1.00 9.43 C ANISOU 1172 CD2 TYR A 128 2132 804 646 -187 -16 170 C ATOM 1173 CE1 TYR A 128 6.127 3.958 11.901 1.00 11.03 C ANISOU 1173 CE1 TYR A 128 2213 1297 679 -104 -211 -46 C ATOM 1174 CE2 TYR A 128 3.879 3.913 11.170 1.00 10.42 C ANISOU 1174 CE2 TYR A 128 2143 1046 768 -64 22 168 C ATOM 1175 CZ TYR A 128 4.799 4.177 12.132 1.00 10.84 C ANISOU 1175 CZ TYR A 128 2173 1224 721 -40 106 46 C ATOM 1176 OH TYR A 128 4.363 4.665 13.350 1.00 13.62 O ANISOU 1176 OH TYR A 128 2434 2023 717 230 109 -163 O ATOM 1177 N GLU A 129 5.476 0.252 6.227 1.00 10.52 N ANISOU 1177 N GLU A 129 2384 969 643 -124 15 -117 N ATOM 1178 CA AGLU A 129 5.310 -0.130 4.827 0.50 10.93 C ANISOU 1178 CA AGLU A 129 2421 923 807 -2 -11 -193 C ATOM 1179 CA BGLU A 129 5.430 0.013 4.781 0.50 11.37 C ANISOU 1179 CA BGLU A 129 2520 937 863 -18 -54 -257 C ATOM 1180 C GLU A 129 4.223 0.741 4.215 1.00 9.94 C ANISOU 1180 C GLU A 129 2345 743 688 -82 -64 -98 C ATOM 1181 O GLU A 129 3.382 1.249 4.905 1.00 10.53 O ANISOU 1181 O GLU A 129 2464 819 717 40 -105 -34 O ATOM 1182 CB AGLU A 129 4.954 -1.629 4.746 0.50 10.87 C ANISOU 1182 CB AGLU A 129 2322 878 926 -28 -43 -117 C ATOM 1183 CB BGLU A 129 5.369 -1.468 4.450 0.50 12.36 C ANISOU 1183 CB BGLU A 129 2653 985 1056 142 -151 -135 C ATOM 1184 CG AGLU A 129 6.217 -2.449 5.048 0.50 15.99 C ANISOU 1184 CG AGLU A 129 2984 1638 1453 370 -201 -101 C ATOM 1185 CG BGLU A 129 4.033 -2.058 4.849 0.50 16.96 C ANISOU 1185 CG BGLU A 129 3139 1568 1736 -192 -254 -187 C ATOM 1186 CD AGLU A 129 6.110 -3.887 4.591 0.50 20.36 C ANISOU 1186 CD AGLU A 129 3508 2163 2061 232 -94 -94 C ATOM 1187 CD BGLU A 129 3.975 -3.596 4.588 0.50 23.02 C ANISOU 1187 CD BGLU A 129 3866 2218 2661 -103 -286 -215 C ATOM 1188 OE1AGLU A 129 5.375 -4.130 3.615 0.50 25.65 O ANISOU 1188 OE1AGLU A 129 4358 2816 2572 82 -146 -347 O ATOM 1189 OE1BGLU A 129 5.016 -4.284 4.563 0.50 22.58 O ANISOU 1189 OE1BGLU A 129 4963 921 2694 154 -129 -297 O ATOM 1190 OE2AGLU A 129 6.731 -4.755 5.231 0.50 23.97 O ANISOU 1190 OE2AGLU A 129 4276 2180 2651 393 -261 -319 O ATOM 1191 OE2BGLU A 129 2.884 -4.154 4.396 0.50 25.91 O ANISOU 1191 OE2BGLU A 129 4473 1876 3494 -549 -441 166 O ATOM 1192 N ARG A 130 4.194 0.857 2.896 1.00 11.41 N ANISOU 1192 N ARG A 130 2500 1188 646 -1 -46 -297 N ATOM 1193 CA ARG A 130 3.097 1.551 2.259 1.00 11.65 C ANISOU 1193 CA ARG A 130 2423 1227 777 -13 -148 -193 C ATOM 1194 C ARG A 130 1.771 0.863 2.541 1.00 12.60 C ANISOU 1194 C ARG A 130 2442 1257 1086 -86 -235 -359 C ATOM 1195 O ARG A 130 1.663 -0.366 2.473 1.00 14.67 O ANISOU 1195 O ARG A 130 2768 875 1929 -104 -514 -366 O ATOM 1196 CB ARG A 130 3.268 1.622 0.761 1.00 14.52 C ANISOU 1196 CB ARG A 130 2607 2051 858 37 -253 -54 C ATOM 1197 CG ARG A 130 4.497 2.314 0.305 1.00 16.06 C ANISOU 1197 CG ARG A 130 2994 1968 1140 -138 -221 198 C ATOM 1198 CD ARG A 130 4.219 3.746 0.290 1.00 16.61 C ANISOU 1198 CD ARG A 130 2990 2093 1227 -109 -104 -125 C ATOM 1199 NE ARG A 130 5.357 4.490 -0.275 1.00 17.03 N ANISOU 1199 NE ARG A 130 2990 1454 2026 16 -219 182 N ATOM 1200 CZ ARG A 130 5.410 5.800 -0.497 1.00 15.05 C ANISOU 1200 CZ ARG A 130 2959 1405 1352 -80 -112 71 C ATOM 1201 NH1 ARG A 130 4.370 6.539 -0.292 1.00 15.18 N ANISOU 1201 NH1 ARG A 130 3045 1397 1324 -121 -67 58 N ATOM 1202 NH2 ARG A 130 6.575 6.342 -0.855 1.00 17.89 N ANISOU 1202 NH2 ARG A 130 3246 1819 1731 -48 128 376 N ATOM 1203 N ALA A 131 0.771 1.662 2.863 1.00 13.49 N ANISOU 1203 N ALA A 131 2455 1114 1553 -112 -283 -267 N ATOM 1204 CA ALA A 131 -0.546 1.116 3.203 1.00 17.42 C ANISOU 1204 CA ALA A 131 2694 1646 2276 -234 -277 -199 C ATOM 1205 C ALA A 131 -1.223 0.557 1.952 1.00 20.10 C ANISOU 1205 C ALA A 131 3095 1762 2779 -298 -275 -216 C ATOM 1206 O ALA A 131 -0.881 0.978 0.833 1.00 21.91 O ANISOU 1206 O ALA A 131 3255 2336 2732 -414 -779 -63 O ATOM 1207 CB ALA A 131 -1.382 2.160 3.957 1.00 19.65 C ANISOU 1207 CB ALA A 131 2882 1895 2686 -183 23 -286 C TER 1208 ALA A 131 HETATM 1209 C1 AZGB A 133 3.605 6.441 22.354 0.70 18.58 C ANISOU 1209 C1 AZGB A 133 2763 2229 2068 295 38 -379 C HETATM 1210 C1 BZGB A 133 6.593 7.911 22.798 0.30 14.61 C ANISOU 1210 C1 BZGB A 133 2569 1368 1611 -271 263 998 C HETATM 1211 O1 AZGB A 133 6.046 7.366 23.632 0.70 16.19 O ANISOU 1211 O1 AZGB A 133 3059 1657 1435 284 -169 -14 O HETATM 1212 O1 BZGB A 133 4.228 6.624 23.643 0.30 21.97 O ANISOU 1212 O1 BZGB A 133 3377 2075 2896 72 215 -504 O HETATM 1213 C2 AZGB A 133 4.787 7.021 21.596 0.70 15.94 C ANISOU 1213 C2 AZGB A 133 2802 1537 1718 331 -125 -513 C HETATM 1214 C2 BZGB A 133 5.522 7.418 21.805 0.30 19.55 C ANISOU 1214 C2 BZGB A 133 2637 1885 2906 159 13 -56 C HETATM 1215 O2 AZGB A 133 5.654 7.142 15.226 0.70 14.72 O ANISOU 1215 O2 AZGB A 133 3203 1445 945 431 -216 -194 O HETATM 1216 O2 BZGB A 133 6.199 5.263 15.309 0.30 22.16 O ANISOU 1216 O2 BZGB A 133 3199 2801 2418 81 -127 -518 O HETATM 1217 C3 AZGB A 133 4.674 7.028 20.242 0.70 15.64 C ANISOU 1217 C3 AZGB A 133 2653 1416 1871 190 8 516 C HETATM 1218 C3 BZGB A 133 5.690 7.571 20.440 0.30 20.47 C ANISOU 1218 C3 BZGB A 133 2805 1962 3010 116 47 89 C HETATM 1219 O3 AZGB A 133 6.003 4.981 15.349 0.70 13.66 O ANISOU 1219 O3 AZGB A 133 2887 1545 755 537 -249 -169 O HETATM 1220 O3 BZGB A 133 6.245 7.481 15.530 0.30 23.23 O ANISOU 1220 O3 BZGB A 133 3288 3229 2306 -176 112 -36 O HETATM 1221 C4 AZGB A 133 5.956 7.446 22.304 0.70 14.06 C ANISOU 1221 C4 AZGB A 133 2948 1550 843 140 -289 -147 C HETATM 1222 C4 BZGB A 133 4.379 6.788 22.296 0.30 21.10 C ANISOU 1222 C4 BZGB A 133 2925 2230 2860 31 274 -118 C HETATM 1223 C5 AZGB A 133 7.310 7.762 24.189 0.70 15.41 C ANISOU 1223 C5 AZGB A 133 2899 1411 1544 35 -9 193 C HETATM 1224 C5 BZGB A 133 2.843 6.394 23.940 0.30 22.67 C ANISOU 1224 C5 BZGB A 133 3438 2078 3097 -211 135 -903 C HETATM 1225 C6 AZGB A 133 6.977 7.953 21.483 0.70 15.39 C ANISOU 1225 C6 AZGB A 133 3402 1194 1251 279 231 216 C HETATM 1226 C6 BZGB A 133 3.408 6.314 21.415 0.30 22.01 C ANISOU 1226 C6 BZGB A 133 3026 2531 2804 152 76 44 C HETATM 1227 C7 AZGB A 133 6.907 7.964 20.095 0.70 12.96 C ANISOU 1227 C7 AZGB A 133 2831 1183 908 304 -14 -70 C HETATM 1228 C7 BZGB A 133 3.567 6.471 20.034 0.30 21.32 C ANISOU 1228 C7 BZGB A 133 2950 2301 2848 333 133 -78 C HETATM 1229 C8 AZGB A 133 5.751 7.542 19.501 0.70 16.08 C ANISOU 1229 C8 AZGB A 133 2916 1306 1885 139 -457 248 C HETATM 1230 C8 BZGB A 133 4.708 7.097 19.560 0.30 22.50 C ANISOU 1230 C8 BZGB A 133 2832 2628 3088 133 -59 -1 C HETATM 1231 C9 AZGB A 133 5.656 7.557 18.018 0.70 17.40 C ANISOU 1231 C9 AZGB A 133 3211 1620 1779 115 -190 -523 C HETATM 1232 C9 BZGB A 133 4.884 7.263 18.060 0.30 20.89 C ANISOU 1232 C9 BZGB A 133 2551 2432 2952 -3 26 -439 C HETATM 1233 C10AZGB A 133 6.405 6.350 17.334 0.70 16.94 C ANISOU 1233 C10AZGB A 133 3122 1421 1893 -254 -524 -275 C HETATM 1234 C10BZGB A 133 5.776 6.154 17.480 0.30 20.64 C ANISOU 1234 C10BZGB A 133 2808 2605 2428 27 149 -425 C HETATM 1235 C11AZGB A 133 6.053 6.134 15.829 0.70 13.45 C ANISOU 1235 C11AZGB A 133 2665 1410 1035 72 -293 -87 C HETATM 1236 C11BZGB A 133 6.106 6.317 15.979 0.30 22.40 C ANISOU 1236 C11BZGB A 133 3295 2785 2431 26 55 -323 C HETATM 1237 O HOH A 134 5.293 -0.966 -1.150 1.00 34.22 O ANISOU 1237 O HOH A 134 5158 4262 3579 278 -633 -2464 O HETATM 1238 O HOH A 135 3.126 21.325 23.859 1.00 30.50 O ANISOU 1238 O HOH A 135 5476 2784 3327 1387 1499 370 O HETATM 1239 O HOH A 136 12.985 5.958 33.550 1.00114.74 O ANISOU 1239 O HOH A 136 17562 19829 6203 3732 -3152 -2200 O HETATM 1240 O HOH A 137 18.438 11.998 21.593 1.00 36.67 O ANISOU 1240 O HOH A 137 3774 5822 4335 480 -861 -1856 O HETATM 1241 O HOH A 138 10.433 22.097 12.768 1.00 8.64 O ANISOU 1241 O HOH A 138 2112 531 636 37 19 12 O HETATM 1242 O HOH A 139 12.763 25.487 6.073 1.00 28.28 O ANISOU 1242 O HOH A 139 5899 2588 2259 -125 767 1003 O HETATM 1243 O HOH A 140 17.650 0.946 13.179 1.00 28.90 O ANISOU 1243 O HOH A 140 3694 3654 3633 61 733 -31 O HETATM 1244 O HOH A 141 7.212 24.890 12.324 1.00 10.26 O ANISOU 1244 O HOH A 141 1992 1048 859 -58 -2 -322 O HETATM 1245 O HOH A 142 17.800 10.950 0.148 1.00 18.05 O ANISOU 1245 O HOH A 142 4233 1737 886 61 653 -283 O HETATM 1246 O HOH A 143 4.401 14.552 30.862 1.00 35.81 O ANISOU 1246 O HOH A 143 8110 2898 2595 -85 832 -214 O HETATM 1247 O HOH A 144 14.783 10.359 0.761 1.00 32.02 O ANISOU 1247 O HOH A 144 6263 3397 2506 -109 1035 1005 O HETATM 1248 O HOH A 145 3.990 1.066 -3.114 1.00 94.02 O ANISOU 1248 O HOH A 145 17060 13666 4995 1459 -115 -5484 O HETATM 1249 O AHOH A 146 13.287 2.535 33.523 0.50 30.28 O ANISOU 1249 O AHOH A 146 5135 4725 1642 914 331 246 O HETATM 1250 O BHOH A 146 14.998 4.271 32.621 0.50 29.71 O ANISOU 1250 O BHOH A 146 6052 3172 2062 -73 -756 55 O HETATM 1251 O HOH A 147 1.912 22.801 25.856 1.00 37.13 O ANISOU 1251 O HOH A 147 6177 4635 3294 2497 1617 753 O HETATM 1252 O HOH A 148 18.622 0.097 22.150 1.00 10.67 O ANISOU 1252 O HOH A 148 2240 770 1042 164 -101 63 O HETATM 1253 O HOH A 149 15.052 8.330 -0.935 1.00 22.25 O ANISOU 1253 O HOH A 149 3931 1979 2541 -513 436 -361 O HETATM 1254 O HOH A 150 -1.690 7.754 -0.368 1.00 27.41 O ANISOU 1254 O HOH A 150 5670 3377 1367 -1560 208 44 O HETATM 1255 O HOH A 151 0.895 7.247 -1.939 1.00 23.44 O ANISOU 1255 O HOH A 151 4089 3099 1716 76 -518 390 O HETATM 1256 O HOH A 152 6.415 21.667 -1.424 1.00 34.58 O ANISOU 1256 O HOH A 152 7189 3360 2590 -124 1558 -578 O HETATM 1257 O HOH A 153 -2.277 4.626 -0.320 1.00 33.31 O ANISOU 1257 O HOH A 153 4355 3152 5149 -147 -369 182 O HETATM 1258 O HOH A 154 22.664 6.287 29.253 1.00 37.06 O ANISOU 1258 O HOH A 154 4977 3121 5982 -30 -1765 994 O HETATM 1259 O HOH A 155 13.834 -3.999 2.405 1.00 80.45 O ANISOU 1259 O HOH A 155 15889 2596 12081 747 1787 1914 O HETATM 1260 O HOH A 156 6.482 20.120 29.402 1.00 35.51 O ANISOU 1260 O HOH A 156 5520 5573 2398 555 229 -1079 O HETATM 1261 O HOH A 157 5.151 19.187 -8.226 1.00 29.88 O ANISOU 1261 O HOH A 157 4146 3033 4173 -815 94 -59 O HETATM 1262 O HOH A 158 -4.027 6.024 7.516 1.00 31.46 O ANISOU 1262 O HOH A 158 3710 3754 4489 -319 -3 -194 O HETATM 1263 O HOH A 159 3.309 27.628 -6.424 1.00 41.76 O ANISOU 1263 O HOH A 159 5347 5315 5202 -662 -1177 -1366 O HETATM 1264 O HOH A 160 -3.805 -0.553 22.383 1.00 11.23 O ANISOU 1264 O HOH A 160 2363 944 956 -185 -135 144 O HETATM 1265 O HOH A 161 -6.757 5.313 23.929 1.00 33.36 O ANISOU 1265 O HOH A 161 6166 2855 3652 -1509 675 30 O HETATM 1266 O HOH A 162 -2.576 0.851 -1.339 1.00 39.85 O ANISOU 1266 O HOH A 162 6069 5490 3581 -40 -2327 133 O HETATM 1267 O HOH A 163 -2.704 20.044 1.453 1.00 23.82 O ANISOU 1267 O HOH A 163 4114 3001 1935 -1715 116 -160 O HETATM 1268 O HOH A 164 14.686 -5.411 22.512 0.50 16.54 O ANISOU 1268 O HOH A 164 3750 612 1920 -117 -1019 85 O HETATM 1269 O HOH A 165 11.330 24.945 4.319 1.00 32.30 O ANISOU 1269 O HOH A 165 4189 4678 3405 -592 1095 1561 O HETATM 1270 O HOH A 166 12.042 -6.500 23.269 1.00 21.48 O ANISOU 1270 O HOH A 166 4011 1817 2330 255 -40 257 O HETATM 1271 O HOH A 167 4.677 24.371 13.210 1.00 10.58 O ANISOU 1271 O HOH A 167 2215 888 917 0 -40 -254 O HETATM 1272 O HOH A 168 19.659 10.134 17.661 1.00 30.38 O ANISOU 1272 O HOH A 168 4491 3044 4009 457 682 446 O HETATM 1273 O AHOH A 169 16.695 21.046 4.175 0.50 23.64 O ANISOU 1273 O AHOH A 169 4828 2653 1500 -246 543 65 O HETATM 1274 O BHOH A 169 15.597 22.225 4.952 0.50 29.83 O ANISOU 1274 O BHOH A 169 4701 3904 2727 -20 760 1367 O HETATM 1275 O HOH A 170 14.127 -2.085 31.552 1.00 32.47 O ANISOU 1275 O HOH A 170 4540 3987 3808 827 757 892 O HETATM 1276 O HOH A 171 9.960 21.365 2.794 1.00 39.86 O ANISOU 1276 O HOH A 171 7299 4614 3231 366 1108 -956 O HETATM 1277 O HOH A 172 3.440 10.029 13.405 1.00 30.87 O ANISOU 1277 O HOH A 172 4254 5092 2382 777 462 1199 O HETATM 1278 O HOH A 173 7.317 4.001 35.583 1.00 32.27 O ANISOU 1278 O HOH A 173 6194 3591 2476 -1334 -274 -230 O HETATM 1279 O HOH A 174 5.035 29.007 4.254 1.00 27.82 O ANISOU 1279 O HOH A 174 3949 2374 4244 -402 -199 -1323 O HETATM 1280 O HOH A 175 6.645 23.126 26.398 1.00 56.47 O ANISOU 1280 O HOH A 175 9243 9286 2923 -927 391 -400 O HETATM 1281 O HOH A 176 15.001 22.115 32.640 1.00 37.52 O ANISOU 1281 O HOH A 176 8059 2877 3317 -1551 -201 -1027 O HETATM 1282 O HOH A 177 6.104 -2.283 22.926 1.00 28.97 O ANISOU 1282 O HOH A 177 4144 4218 2645 435 -348 -95 O HETATM 1283 O HOH A 178 3.085 -4.682 22.524 1.00 31.08 O ANISOU 1283 O HOH A 178 5041 3539 3228 752 993 769 O HETATM 1284 O HOH A 179 -3.606 3.147 28.994 1.00 27.43 O ANISOU 1284 O HOH A 179 4332 2515 3573 -148 -703 -441 O HETATM 1285 O HOH A 180 -3.701 11.681 26.015 1.00 42.10 O ANISOU 1285 O HOH A 180 5906 5064 5024 -545 106 -1079 O HETATM 1286 O HOH A 181 1.239 -6.860 18.535 1.00 27.65 O ANISOU 1286 O HOH A 181 4517 2610 3375 -715 -25 95 O HETATM 1287 O HOH A 182 7.637 2.383 -2.753 1.00 33.42 O ANISOU 1287 O HOH A 182 4925 4001 3769 684 264 857 O HETATM 1288 O HOH A 183 13.505 23.658 21.561 1.00 34.47 O ANISOU 1288 O HOH A 183 5669 3068 4358 -60 -1297 -1444 O HETATM 1289 O HOH A 184 16.779 0.409 32.522 1.00 46.75 O ANISOU 1289 O HOH A 184 6319 5662 5780 20 -2187 3150 O HETATM 1290 O HOH A 185 11.824 12.422 12.138 1.00 10.74 O ANISOU 1290 O HOH A 185 2544 811 722 141 111 36 O HETATM 1291 O HOH A 186 16.596 -0.464 28.816 1.00 29.40 O ANISOU 1291 O HOH A 186 4531 4002 2634 1763 280 -81 O HETATM 1292 O HOH A 187 13.276 -8.672 22.743 1.00 30.51 O ANISOU 1292 O HOH A 187 4010 3384 4198 551 -53 -579 O HETATM 1293 O HOH A 188 9.019 6.846 -3.295 1.00 49.59 O ANISOU 1293 O HOH A 188 7690 8121 3028 276 -120 -205 O HETATM 1294 O HOH A 189 9.009 -4.009 0.951 1.00 34.55 O ANISOU 1294 O HOH A 189 5222 3094 4808 -741 414 1330 O HETATM 1295 O HOH A 190 -3.725 -1.095 19.713 1.00 12.06 O ANISOU 1295 O HOH A 190 2233 1200 1147 -329 4 28 O HETATM 1296 O HOH A 191 20.650 1.189 32.201 1.00 37.21 O ANISOU 1296 O HOH A 191 6648 3880 3609 140 1470 -892 O HETATM 1297 O HOH A 192 6.521 -1.569 -3.679 1.00 50.02 O ANISOU 1297 O HOH A 192 6378 5928 6698 -283 -937 3035 O HETATM 1298 O HOH A 193 -3.663 18.188 23.787 1.00 41.25 O ANISOU 1298 O HOH A 193 4056 5180 6436 1562 -590 -1969 O HETATM 1299 O HOH A 194 6.062 -7.512 13.140 1.00 36.52 O ANISOU 1299 O HOH A 194 5471 2268 6134 -471 -1638 1072 O HETATM 1300 O HOH A 195 8.010 -6.403 17.922 1.00 32.60 O ANISOU 1300 O HOH A 195 5803 2542 4039 -801 -1586 1577 O HETATM 1301 O HOH A 196 1.056 20.249 5.128 1.00 13.37 O ANISOU 1301 O HOH A 196 2513 1332 1235 -104 -188 216 O HETATM 1302 O HOH A 197 -0.564 28.137 -5.977 1.00 42.03 O ANISOU 1302 O HOH A 197 8159 4606 3202 403 1157 1015 O HETATM 1303 O HOH A 198 17.452 12.714 30.423 1.00 38.69 O ANISOU 1303 O HOH A 198 6200 5186 3313 1184 -1330 841 O HETATM 1304 O HOH A 199 21.541 8.347 17.243 1.00 45.62 O ANISOU 1304 O HOH A 199 3561 6563 7209 -973 1521 81 O HETATM 1305 O HOH A 200 15.207 9.062 3.228 1.00 15.80 O ANISOU 1305 O HOH A 200 3440 1243 1320 -443 426 34 O HETATM 1306 O HOH A 201 12.859 12.182 -3.229 1.00 34.99 O ANISOU 1306 O HOH A 201 6561 3748 2986 -167 1011 -530 O HETATM 1307 O HOH A 202 -2.800 19.019 20.697 1.00 38.22 O ANISOU 1307 O HOH A 202 5466 4720 4333 -867 1 845 O HETATM 1308 O HOH A 203 20.878 7.875 14.737 1.00 45.32 O ANISOU 1308 O HOH A 203 5751 4357 7110 1157 810 1173 O HETATM 1309 O HOH A 204 6.259 19.217 -2.773 1.00 36.02 O ANISOU 1309 O HOH A 204 5730 4137 3817 1264 990 106 O HETATM 1310 O HOH A 205 9.791 23.028 5.417 1.00 13.43 O ANISOU 1310 O HOH A 205 2518 1839 743 220 1 -27 O HETATM 1311 O HOH A 206 19.113 21.595 9.078 1.00 55.58 O ANISOU 1311 O HOH A 206 6246 5101 9768 -2253 3406 -2256 O HETATM 1312 O HOH A 207 -2.135 0.274 10.606 1.00 39.23 O ANISOU 1312 O HOH A 207 7625 4433 2846 -1816 -1401 1013 O HETATM 1313 O HOH A 208 7.666 25.652 -6.219 1.00 49.77 O ANISOU 1313 O HOH A 208 6375 4517 8017 890 -1164 -2349 O HETATM 1314 O HOH A 209 9.227 14.840 -5.759 1.00 36.74 O ANISOU 1314 O HOH A 209 5939 4126 3891 59 -889 1291 O HETATM 1315 O HOH A 210 20.229 1.477 14.813 1.00 99.22 O ANISOU 1315 O HOH A 210 18387 14576 4735 -341 -3362 1954 O HETATM 1316 O HOH A 211 16.098 23.277 8.709 1.00 30.90 O ANISOU 1316 O HOH A 211 3993 3223 4522 198 1108 -75 O HETATM 1317 O HOH A 212 -0.606 14.356 6.449 1.00 15.10 O ANISOU 1317 O HOH A 212 3023 1175 1537 12 -237 -144 O HETATM 1318 O HOH A 213 1.882 3.825 19.944 1.00 28.87 O ANISOU 1318 O HOH A 213 4303 4010 2654 -384 163 429 O HETATM 1319 O HOH A 214 -8.139 5.726 21.936 1.00 39.12 O ANISOU 1319 O HOH A 214 4745 4824 5294 -537 -995 -81 O HETATM 1320 O HOH A 215 12.510 10.372 31.766 1.00 38.24 O ANISOU 1320 O HOH A 215 6697 5437 2396 -1754 -1570 -609 O HETATM 1321 O HOH A 216 15.865 -3.209 15.003 1.00 98.74 O ANISOU 1321 O HOH A 216 8383 7432 21700 3 -865 774 O HETATM 1322 O HOH A 217 10.661 -4.247 27.929 1.00 47.17 O ANISOU 1322 O HOH A 217 6287 5921 5712 985 -1172 2735 O HETATM 1323 O HOH A 218 -8.650 3.706 15.776 1.00 32.10 O ANISOU 1323 O HOH A 218 4985 4017 3192 -1056 -108 1044 O HETATM 1324 O HOH A 219 1.697 5.781 0.157 1.00 15.59 O ANISOU 1324 O HOH A 219 3295 1422 1205 -288 -64 -435 O HETATM 1325 O HOH A 220 2.594 -6.452 11.705 1.00 36.19 O ANISOU 1325 O HOH A 220 5226 3025 5499 -1376 -366 878 O HETATM 1326 O HOH A 221 11.217 3.730 33.575 1.00 45.16 O ANISOU 1326 O HOH A 221 7846 4754 4556 -845 -52 -1060 O HETATM 1327 O HOH A 222 -5.106 13.082 5.943 1.00 44.64 O ANISOU 1327 O HOH A 222 5302 4762 6893 -267 -1287 -1455 O HETATM 1328 O HOH A 223 8.864 -2.982 20.095 1.00 15.39 O ANISOU 1328 O HOH A 223 2852 1510 1483 49 -165 -261 O HETATM 1329 O HOH A 224 13.758 -1.702 4.185 1.00 40.91 O ANISOU 1329 O HOH A 224 6496 4369 4676 -333 371 2304 O HETATM 1330 O HOH A 225 6.440 11.381 19.542 1.00 13.58 O ANISOU 1330 O HOH A 225 2480 1161 1518 -86 96 108 O HETATM 1331 O HOH A 226 15.991 16.745 33.204 1.00 43.58 O ANISOU 1331 O HOH A 226 7080 4547 4930 -522 -979 -1382 O HETATM 1332 O HOH A 227 -3.016 13.911 5.474 1.00 61.25 O ANISOU 1332 O HOH A 227 6423 5218 11631 -2130 -3055 4999 O HETATM 1333 O HOH A 228 17.737 2.307 31.403 1.00 46.07 O ANISOU 1333 O HOH A 228 4687 7102 5715 923 -915 2537 O HETATM 1334 O HOH A 229 -4.896 2.643 5.101 1.00 58.90 O ANISOU 1334 O HOH A 229 5467 13223 3689 -124 -687 -863 O HETATM 1335 O HOH A 230 -8.584 11.834 18.065 1.00 37.95 O ANISOU 1335 O HOH A 230 3659 4839 5921 581 119 -1579 O HETATM 1336 O HOH A 231 8.879 10.546 21.425 1.00 12.88 O ANISOU 1336 O HOH A 231 2723 1059 1110 -158 44 -8 O HETATM 1337 O HOH A 232 3.612 11.295 19.359 1.00 13.91 O ANISOU 1337 O HOH A 232 2475 1467 1341 -223 192 15 O HETATM 1338 O HOH A 233 19.214 20.520 7.222 1.00 34.47 O ANISOU 1338 O HOH A 233 5427 3030 4637 -1439 1483 -1237 O HETATM 1339 O HOH A 234 18.200 2.988 33.671 1.00 46.34 O ANISOU 1339 O HOH A 234 7012 6891 3702 -621 -1247 1184 O HETATM 1340 O HOH A 235 12.687 20.754 33.909 1.00125.61 O ANISOU 1340 O HOH A 235 25522 13238 8964 -4685 4727 -4217 O HETATM 1341 O HOH A 236 1.954 12.747 14.321 1.00 18.33 O ANISOU 1341 O HOH A 236 3046 2303 1614 66 125 1156 O HETATM 1342 O HOH A 237 21.089 10.823 10.556 1.00 41.77 O ANISOU 1342 O HOH A 237 4556 6777 4536 -232 1187 1827 O HETATM 1343 O HOH A 238 7.494 25.923 -0.924 1.00 37.27 O ANISOU 1343 O HOH A 238 6255 5103 2800 -1978 743 412 O HETATM 1344 O HOH A 239 20.401 5.083 28.393 0.50 12.51 O ANISOU 1344 O HOH A 239 2746 827 1181 243 -222 59 O HETATM 1345 O HOH A 240 13.022 21.809 19.854 1.00 16.77 O ANISOU 1345 O HOH A 240 2685 2618 1068 -430 -159 6 O HETATM 1346 O HOH A 241 11.263 -2.726 0.868 1.00 18.41 O ANISOU 1346 O HOH A 241 3945 1359 1691 -431 -212 -57 O HETATM 1347 O HOH A 242 13.165 -7.086 6.635 1.00 35.78 O ANISOU 1347 O HOH A 242 5303 4726 3565 982 -1268 44 O HETATM 1348 O HOH A 243 2.266 9.745 17.424 1.00 14.21 O ANISOU 1348 O HOH A 243 2675 1370 1351 -162 -58 80 O HETATM 1349 O HOH A 244 17.575 -1.496 20.185 1.00 15.56 O ANISOU 1349 O HOH A 244 2615 1308 1987 137 -317 47 O HETATM 1350 O HOH A 245 4.470 -4.486 26.317 1.00 40.06 O ANISOU 1350 O HOH A 245 6100 5957 3163 -126 516 -166 O HETATM 1351 O HOH A 246 1.638 26.182 2.233 1.00 17.65 O ANISOU 1351 O HOH A 246 3462 1109 2133 -1 54 -244 O HETATM 1352 O HOH A 247 2.583 6.868 13.713 1.00 20.30 O ANISOU 1352 O HOH A 247 2954 1756 3001 -248 839 -600 O HETATM 1353 O HOH A 248 3.053 13.750 18.319 1.00 16.95 O ANISOU 1353 O HOH A 248 2966 1422 2052 -161 33 -65 O HETATM 1354 O HOH A 249 24.275 14.382 6.341 1.00 43.35 O ANISOU 1354 O HOH A 249 5261 4780 6428 1590 480 -1575 O HETATM 1355 O HOH A 250 7.035 27.735 11.942 1.00 18.62 O ANISOU 1355 O HOH A 250 2501 1493 3077 424 -404 -426 O HETATM 1356 O HOH A 251 16.209 18.875 14.214 1.00 17.86 O ANISOU 1356 O HOH A 251 3416 1760 1608 -175 -347 67 O HETATM 1357 O HOH A 252 11.478 -3.081 13.714 1.00 17.53 O ANISOU 1357 O HOH A 252 3843 1345 1469 -62 3 -47 O HETATM 1358 O HOH A 253 16.320 21.142 7.235 1.00 18.01 O ANISOU 1358 O HOH A 253 3685 1026 2129 -391 126 261 O HETATM 1359 O HOH A 254 5.538 -5.546 16.525 1.00 46.36 O ANISOU 1359 O HOH A 254 8246 3127 6239 -651 -1176 78 O HETATM 1360 O HOH A 255 5.340 -4.918 19.269 1.00 45.07 O ANISOU 1360 O HOH A 255 6328 3025 7769 -1016 -4 -710 O HETATM 1361 O HOH A 256 23.004 18.510 10.918 1.00 53.09 O ANISOU 1361 O HOH A 256 7912 8734 3522 -756 1351 -1069 O HETATM 1362 O HOH A 257 4.085 27.117 2.464 1.00 17.38 O ANISOU 1362 O HOH A 257 3309 1450 1845 51 -223 -71 O HETATM 1363 O HOH A 258 11.245 30.822 -7.898 1.00 48.24 O ANISOU 1363 O HOH A 258 6978 4833 6518 1244 -126 1949 O HETATM 1364 O HOH A 259 2.999 19.147 30.927 1.00 51.66 O ANISOU 1364 O HOH A 259 5887 9266 4475 2462 -234 1028 O HETATM 1365 O HOH A 260 11.983 -10.261 17.022 1.00 37.41 O ANISOU 1365 O HOH A 260 5507 3624 5082 -739 -466 25 O HETATM 1366 O HOH A 261 23.450 7.714 12.991 1.00 48.88 O ANISOU 1366 O HOH A 261 4253 6545 7773 -1644 -454 929 O HETATM 1367 O HOH A 262 9.172 10.770 -4.596 1.00 42.68 O ANISOU 1367 O HOH A 262 6871 4806 4537 1653 1078 996 O HETATM 1368 O HOH A 263 14.177 -3.558 13.075 1.00 37.67 O ANISOU 1368 O HOH A 263 4959 2623 6730 433 1225 -750 O HETATM 1369 O HOH A 264 11.079 22.307 26.495 1.00 25.68 O ANISOU 1369 O HOH A 264 5343 2312 2099 31 181 -66 O HETATM 1370 O HOH A 265 19.287 12.906 26.071 1.00 37.14 O ANISOU 1370 O HOH A 265 7574 2547 3990 -371 -509 -241 O HETATM 1371 O HOH A 266 5.168 22.696 24.090 1.00 22.69 O ANISOU 1371 O HOH A 266 4199 2609 1814 1195 -13 199 O HETATM 1372 O HOH A 267 -6.089 0.867 22.222 1.00 16.71 O ANISOU 1372 O HOH A 267 2773 1148 2424 -179 -763 396 O HETATM 1373 O HOH A 268 11.475 -5.739 21.015 1.00 21.09 O ANISOU 1373 O HOH A 268 4042 982 2988 -160 271 657 O HETATM 1374 O HOH A 269 17.737 13.878 21.738 1.00 19.85 O ANISOU 1374 O HOH A 269 3328 2506 1707 -277 -178 -500 O HETATM 1375 O HOH A 270 3.479 3.630 35.830 1.00 23.25 O ANISOU 1375 O HOH A 270 5699 2221 912 -861 -197 173 O HETATM 1376 O HOH A 271 6.329 9.159 -1.765 1.00 19.36 O ANISOU 1376 O HOH A 271 3738 1722 1894 -248 384 -12 O HETATM 1377 O HOH A 272 15.301 19.874 27.334 1.00 22.32 O ANISOU 1377 O HOH A 272 5168 1683 1626 -386 -550 -139 O HETATM 1378 O HOH A 273 14.771 1.622 29.197 1.00 20.98 O ANISOU 1378 O HOH A 273 3216 3288 1468 573 -397 564 O HETATM 1379 O HOH A 274 13.156 21.298 28.401 1.00 22.99 O ANISOU 1379 O HOH A 274 5040 1744 1951 1 -548 -107 O HETATM 1380 O HOH A 275 2.207 -3.750 24.750 1.00 21.25 O ANISOU 1380 O HOH A 275 3176 2884 2010 641 -232 -581 O HETATM 1381 O HOH A 276 6.268 -0.477 1.437 1.00 18.17 O ANISOU 1381 O HOH A 276 2893 2145 1862 78 415 -191 O HETATM 1382 O HOH A 277 0.698 18.241 18.753 1.00 27.94 O ANISOU 1382 O HOH A 277 3373 3192 4048 -571 -797 2240 O HETATM 1383 O HOH A 278 0.260 3.420 -0.221 1.00 21.14 O ANISOU 1383 O HOH A 278 3407 1900 2726 -224 -822 -409 O HETATM 1384 O HOH A 279 0.184 7.756 17.579 1.00 17.14 O ANISOU 1384 O HOH A 279 2948 1938 1624 -68 236 -5 O HETATM 1385 O HOH A 280 18.248 11.398 24.354 1.00 26.36 O ANISOU 1385 O HOH A 280 4042 1418 4555 367 -25 834 O HETATM 1386 O HOH A 281 6.521 8.391 12.922 1.00 19.55 O ANISOU 1386 O HOH A 281 2784 3247 1397 -431 60 275 O HETATM 1387 O HOH A 282 -0.683 18.688 3.764 1.00 18.50 O ANISOU 1387 O HOH A 282 3543 1447 2037 -115 -885 354 O HETATM 1388 O HOH A 283 -3.755 1.859 15.102 1.00 19.54 O ANISOU 1388 O HOH A 283 3673 1347 2404 223 958 444 O HETATM 1389 O HOH A 284 0.367 3.024 34.749 1.00 23.36 O ANISOU 1389 O HOH A 284 5737 2018 1118 346 304 -104 O HETATM 1390 O HOH A 285 8.951 -3.489 23.001 1.00 30.18 O ANISOU 1390 O HOH A 285 6837 1673 2954 -919 1532 -344 O HETATM 1391 O HOH A 286 17.541 13.461 27.895 1.00 25.69 O ANISOU 1391 O HOH A 286 3909 2928 2922 638 -770 799 O HETATM 1392 O HOH A 287 5.031 -1.681 25.549 1.00 21.98 O ANISOU 1392 O HOH A 287 3407 2803 2140 615 -150 -623 O HETATM 1393 O HOH A 288 0.551 5.026 32.382 1.00 20.38 O ANISOU 1393 O HOH A 288 3948 2143 1650 -398 147 -371 O HETATM 1394 O HOH A 289 6.264 11.800 16.607 1.00 26.25 O ANISOU 1394 O HOH A 289 2386 5745 1842 -400 467 445 O HETATM 1395 O HOH A 290 -8.083 6.465 15.258 1.00 26.91 O ANISOU 1395 O HOH A 290 3329 3250 3646 -643 -582 572 O HETATM 1396 O HOH A 291 -7.582 6.391 19.297 1.00 28.12 O ANISOU 1396 O HOH A 291 4071 4118 2493 851 1011 -434 O HETATM 1397 O HOH A 292 -7.062 9.368 19.765 1.00 26.81 O ANISOU 1397 O HOH A 292 2958 4614 2613 -220 887 -274 O HETATM 1398 O HOH A 293 2.890 -2.401 17.721 1.00 24.08 O ANISOU 1398 O HOH A 293 3887 2801 2458 603 -493 -157 O HETATM 1399 O HOH A 294 7.418 -6.312 15.590 1.00 24.54 O ANISOU 1399 O HOH A 294 5279 1358 2686 -1078 -1011 1083 O HETATM 1400 O HOH A 295 1.057 15.607 18.530 1.00 24.02 O ANISOU 1400 O HOH A 295 4704 2546 1876 -526 404 18 O HETATM 1401 O HOH A 296 5.203 10.088 29.263 1.00 24.16 O ANISOU 1401 O HOH A 296 6054 1695 1431 -124 -270 355 O HETATM 1402 O AHOH A 297 2.910 1.003 18.725 0.50 13.55 O ANISOU 1402 O AHOH A 297 2225 1995 927 -457 234 -242 O HETATM 1403 O BHOH A 297 2.132 2.464 18.693 0.50 18.80 O ANISOU 1403 O BHOH A 297 2841 2745 1557 -252 133 7 O HETATM 1404 O HOH A 298 7.104 -3.047 30.535 1.00 23.33 O ANISOU 1404 O HOH A 298 5558 1433 1870 -389 719 275 O HETATM 1405 O HOH A 299 14.402 0.696 31.734 1.00 29.21 O ANISOU 1405 O HOH A 299 4429 4154 2513 287 -122 1336 O HETATM 1406 O HOH A 300 17.147 7.191 2.227 1.00 25.41 O ANISOU 1406 O HOH A 300 4624 2731 2298 -853 1101 -330 O HETATM 1407 O HOH A 301 -4.847 11.455 13.514 1.00 28.52 O ANISOU 1407 O HOH A 301 3574 5091 2169 1026 41 574 O HETATM 1408 O HOH A 302 9.374 28.886 15.227 1.00 20.61 O ANISOU 1408 O HOH A 302 3900 1385 2546 -78 749 -59 O HETATM 1409 O HOH A 303 9.194 21.378 29.601 1.00 24.56 O ANISOU 1409 O HOH A 303 4639 2284 2407 954 115 -483 O HETATM 1410 O HOH A 304 2.563 9.392 -2.400 1.00 26.95 O ANISOU 1410 O HOH A 304 4402 3166 2671 -187 -1284 -546 O HETATM 1411 O HOH A 305 0.044 5.157 18.637 1.00 31.46 O ANISOU 1411 O HOH A 305 4318 2905 4727 -948 -1467 2494 O HETATM 1412 O HOH A 306 1.445 2.307 -2.385 1.00 34.23 O ANISOU 1412 O HOH A 306 4780 5204 3023 893 -925 -833 O HETATM 1413 O HOH A 307 9.031 4.891 32.699 1.00 22.33 O ANISOU 1413 O HOH A 307 3663 2569 2250 -176 -818 127 O HETATM 1414 O HOH A 308 20.594 4.404 17.562 1.00 25.77 O ANISOU 1414 O HOH A 308 4385 2363 3044 312 1028 868 O HETATM 1415 O HOH A 309 4.838 17.030 29.627 1.00 24.83 O ANISOU 1415 O HOH A 309 5548 2302 1582 -25 485 263 O HETATM 1416 O HOH A 310 17.256 9.046 16.407 1.00 22.80 O ANISOU 1416 O HOH A 310 3956 2686 2020 497 -174 550 O HETATM 1417 O HOH A 311 -1.802 20.200 11.649 1.00 29.25 O ANISOU 1417 O HOH A 311 3760 2974 4376 -582 1662 -437 O HETATM 1418 O HOH A 312 9.986 28.912 19.797 1.00 28.89 O ANISOU 1418 O HOH A 312 4012 2711 4252 -359 988 -1311 O HETATM 1419 O HOH A 313 -1.775 15.875 17.882 1.00 25.97 O ANISOU 1419 O HOH A 313 5775 2016 2076 -688 1224 -756 O HETATM 1420 O HOH A 314 -8.957 2.176 20.600 1.00 20.16 O ANISOU 1420 O HOH A 314 3127 1294 3237 57 661 370 O HETATM 1421 O HOH A 315 18.551 4.704 2.405 1.00 23.57 O ANISOU 1421 O HOH A 315 4394 3264 1297 351 -117 -310 O HETATM 1422 O HOH A 316 -0.590 -5.129 17.475 1.00 29.03 O ANISOU 1422 O HOH A 316 3896 1398 5736 136 751 293 O HETATM 1423 O HOH A 317 13.269 28.668 7.849 1.00 32.15 O ANISOU 1423 O HOH A 317 6414 4092 1709 -1598 -558 -60 O HETATM 1424 O HOH A 318 -9.281 4.114 20.786 1.00 20.25 O ANISOU 1424 O HOH A 318 4458 1570 1664 512 853 530 O HETATM 1425 O HOH A 319 4.392 9.394 15.675 1.00 23.99 O ANISOU 1425 O HOH A 319 4230 1854 3030 791 1198 555 O HETATM 1426 O HOH A 320 12.135 -3.142 24.927 1.00 26.66 O ANISOU 1426 O HOH A 320 7173 917 2037 192 806 251 O HETATM 1427 O HOH A 321 -2.260 19.426 6.675 1.00 28.05 O ANISOU 1427 O HOH A 321 3359 3452 3844 168 -915 423 O HETATM 1428 O AHOH A 322 4.238 13.324 15.658 0.50 17.25 O ANISOU 1428 O AHOH A 322 3868 1370 1313 499 105 160 O HETATM 1429 O BHOH A 322 4.396 11.684 14.785 0.50 18.85 O ANISOU 1429 O BHOH A 322 3162 1893 2107 -216 -118 494 O HETATM 1430 O HOH A 323 16.219 -1.008 17.710 1.00 31.02 O ANISOU 1430 O HOH A 323 6673 2511 2601 1587 -1912 -757 O HETATM 1431 O HOH A 324 -1.577 9.233 26.279 1.00 29.43 O ANISOU 1431 O HOH A 324 4478 3420 3282 -274 1385 178 O HETATM 1432 O HOH A 325 20.962 5.118 21.530 1.00 25.04 O ANISOU 1432 O HOH A 325 4705 2743 2065 792 -107 490 O HETATM 1433 O HOH A 326 -2.363 18.872 16.150 1.00 38.61 O ANISOU 1433 O HOH A 326 3627 5454 5588 161 1014 -2851 O HETATM 1434 O HOH A 327 5.282 7.790 34.324 1.00 36.30 O ANISOU 1434 O HOH A 327 6442 4928 2421 -331 1059 -779 O HETATM 1435 O HOH A 328 9.105 12.118 30.767 1.00 22.98 O ANISOU 1435 O HOH A 328 4577 2201 1952 164 648 583 O HETATM 1436 O HOH A 329 7.872 30.727 8.558 1.00 30.65 O ANISOU 1436 O HOH A 329 3959 2157 5528 240 -1174 1296 O HETATM 1437 O HOH A 330 19.612 14.719 18.235 1.00 26.05 O ANISOU 1437 O HOH A 330 2736 3372 3788 -239 -58 1127 O HETATM 1438 O HOH A 331 5.861 29.941 10.060 1.00 26.78 O ANISOU 1438 O HOH A 331 3587 3094 3492 459 -222 5 O HETATM 1439 O HOH A 332 0.191 8.935 29.302 1.00 44.97 O ANISOU 1439 O HOH A 332 10564 2966 3555 613 2498 1209 O HETATM 1440 O HOH A 333 2.882 -2.397 1.182 1.00 36.13 O ANISOU 1440 O HOH A 333 5274 3304 5149 -38 198 -2011 O HETATM 1441 O HOH A 334 2.384 -5.453 19.944 1.00 33.11 O ANISOU 1441 O HOH A 334 5595 3163 3820 1198 1183 -268 O HETATM 1442 O HOH A 335 -2.764 5.970 28.744 1.00 36.76 O ANISOU 1442 O HOH A 335 4663 4085 5217 -187 -641 -1682 O HETATM 1443 O HOH A 336 21.766 11.668 7.819 1.00 41.22 O ANISOU 1443 O HOH A 336 4380 5163 6118 -1367 -1340 2336 O HETATM 1444 O HOH A 337 3.163 12.193 29.933 1.00 29.66 O ANISOU 1444 O HOH A 337 5391 3145 2730 13 78 359 O HETATM 1445 O HOH A 338 19.938 10.069 1.923 1.00 27.07 O ANISOU 1445 O HOH A 338 4333 3662 2288 741 253 122 O HETATM 1446 O HOH A 339 -7.110 2.672 23.672 1.00 23.02 O ANISOU 1446 O HOH A 339 4695 1868 2182 55 334 303 O HETATM 1447 O HOH A 340 10.373 29.645 6.352 1.00 33.86 O ANISOU 1447 O HOH A 340 6821 3198 2843 -1420 -1210 682 O HETATM 1448 O HOH A 341 2.296 30.217 -7.261 1.00 29.65 O ANISOU 1448 O HOH A 341 5753 2916 2593 -430 -239 427 O HETATM 1449 O HOH A 342 5.326 -1.805 19.827 1.00 32.22 O ANISOU 1449 O HOH A 342 4115 3514 4611 -1211 2115 -1472 O HETATM 1450 O HOH A 343 6.194 23.500 -4.172 1.00 42.42 O ANISOU 1450 O HOH A 343 4665 7201 4251 1172 -286 -364 O HETATM 1451 O AHOH A 344 21.441 17.912 4.311 0.50 23.09 O ANISOU 1451 O AHOH A 344 4470 1716 2585 -826 1563 -420 O HETATM 1452 O BHOH A 344 22.064 17.923 5.908 0.50 25.64 O ANISOU 1452 O BHOH A 344 3489 2872 3381 -484 699 549 O HETATM 1453 O HOH A 345 19.334 4.416 31.968 1.00 50.63 O ANISOU 1453 O HOH A 345 7512 7097 4625 179 -478 244 O HETATM 1454 O HOH A 346 -2.976 14.229 19.811 1.00 28.92 O ANISOU 1454 O HOH A 346 4496 3121 3368 -741 1256 -1096 O HETATM 1455 O HOH A 347 18.133 0.808 1.721 1.00 34.63 O ANISOU 1455 O HOH A 347 3553 6269 3332 487 720 -312 O HETATM 1456 O HOH A 348 20.893 2.431 21.490 1.00 28.28 O ANISOU 1456 O HOH A 348 3080 5325 2338 24 117 -887 O HETATM 1457 O HOH A 349 7.716 3.288 -0.639 1.00 24.37 O ANISOU 1457 O HOH A 349 4011 2710 2536 918 889 742 O HETATM 1458 O HOH A 350 21.607 9.454 22.434 1.00 35.83 O ANISOU 1458 O HOH A 350 5365 3697 4552 -859 -447 1644 O HETATM 1459 O HOH A 351 8.603 21.722 26.693 1.00 34.47 O ANISOU 1459 O HOH A 351 7071 3271 2752 1708 -1296 -1511 O HETATM 1460 O HOH A 352 -2.627 13.595 24.584 1.00 40.06 O ANISOU 1460 O HOH A 352 5730 4406 5085 -1897 -1208 501 O HETATM 1461 O HOH A 353 0.657 -4.118 10.639 1.00 26.85 O ANISOU 1461 O HOH A 353 4034 2940 3226 -1465 -226 -155 O HETATM 1462 O HOH A 354 10.197 -7.229 15.108 1.00 35.88 O ANISOU 1462 O HOH A 354 4740 2825 6066 172 -1203 826 O HETATM 1463 O HOH A 355 8.724 -6.055 20.311 1.00 36.40 O ANISOU 1463 O HOH A 355 4690 4874 4265 584 -527 33 O HETATM 1464 O HOH A 356 10.490 22.346 -3.387 1.00 44.23 O ANISOU 1464 O HOH A 356 6214 4574 6014 67 -402 -1627 O HETATM 1465 O HOH A 357 9.593 3.135 -2.847 1.00 31.15 O ANISOU 1465 O HOH A 357 5870 2611 3353 609 767 -761 O HETATM 1466 O HOH A 358 -1.486 14.174 21.861 1.00 29.74 O ANISOU 1466 O HOH A 358 3810 4840 2646 -391 95 -180 O HETATM 1467 O AHOH A 359 2.479 7.291 31.745 0.50 21.87 O ANISOU 1467 O AHOH A 359 3597 2734 1977 303 454 84 O HETATM 1468 O BHOH A 359 3.109 8.316 31.025 0.50 19.96 O ANISOU 1468 O BHOH A 359 3798 1743 2043 445 226 360 O HETATM 1469 O HOH A 360 0.983 -0.689 -1.617 1.00 51.61 O ANISOU 1469 O HOH A 360 9868 3870 5871 709 -3784 -2854 O HETATM 1470 O HOH A 361 10.396 -5.161 9.368 1.00 28.54 O ANISOU 1470 O HOH A 361 5611 2160 3071 539 457 -364 O HETATM 1471 O HOH A 362 15.585 8.188 31.310 1.00 68.24 O ANISOU 1471 O HOH A 362 7046 11124 7757 1638 -381 -4200 O HETATM 1472 O HOH A 363 21.665 10.070 5.367 1.00 32.16 O ANISOU 1472 O HOH A 363 3772 4800 3646 -718 1185 -1185 O CONECT 1209 1213 CONECT 1210 1214 CONECT 1211 1221 1223 CONECT 1212 1222 1224 CONECT 1213 1209 1217 1221 CONECT 1214 1210 1218 1222 CONECT 1215 1235 CONECT 1216 1236 CONECT 1217 1213 1229 CONECT 1218 1214 1230 CONECT 1219 1235 CONECT 1220 1236 CONECT 1221 1211 1213 1225 CONECT 1222 1212 1214 1226 CONECT 1223 1211 CONECT 1224 1212 CONECT 1225 1221 1227 CONECT 1226 1222 1228 CONECT 1227 1225 1229 CONECT 1228 1226 1230 CONECT 1229 1217 1227 1231 CONECT 1230 1218 1228 1232 CONECT 1231 1229 1233 CONECT 1232 1230 1234 CONECT 1233 1231 1235 CONECT 1234 1232 1236 CONECT 1235 1215 1219 1233 CONECT 1236 1216 1220 1234 MASTER 344 0 1 3 10 0 3 6 1316 1 28 11 END If you find results from this site helpful for your research, please cite one of our papers:
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