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*** LIPID BINDING PROTEIN 12-MAY-11 3RZY ***elNémo ID: 220125132214134349Job options:ID = 220125132214134349 JOBID = LIPID BINDING PROTEIN 12-MAY-11 3RZY USERID = test2 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 12-MAY-11 3RZY TITLE HUMAN ADIPOCYTE LIPID-BINDING PROTEIN FABP4, APO FORM AT 1.08 ANG TITLE 2 RESOLUTION. 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 3RZY 1 JRNL REVDAT 2 11-FEB-15 3RZY 1 JRNL REVDAT 1 29-JUN-11 3RZY 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. 1.08 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) : 1.08 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.50 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1 REMARK 3 NUMBER OF REFLECTIONS : 50942 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.154 REMARK 3 R VALUE (WORKING SET) : 0.152 REMARK 3 FREE R VALUE : 0.189 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 2728 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.08 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.10 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2691 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.63 REMARK 3 BIN R VALUE (WORKING SET) : 0.2600 REMARK 3 BIN FREE R VALUE SET COUNT : 144 REMARK 3 BIN FREE R VALUE : 0.2960 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1073 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 147 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.24 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 1.66000 REMARK 3 B22 (A**2) : -0.61000 REMARK 3 B33 (A**2) : -1.04000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.031 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.034 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.031 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.492 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1182 ; 0.025 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 811 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1598 ; 2.172 ; 1.960 REMARK 3 BOND ANGLES OTHERS (DEGREES): 1994 ; 1.188 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 158 ; 6.172 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;34.193 ;24.792 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 230 ;16.168 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;18.220 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 181 ; 0.130 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1350 ; 0.010 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 235 ; 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): 749 ; 2.654 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 315 ; 1.002 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1218 ; 4.149 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 433 ; 5.844 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 380 ; 8.428 ; 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): 1993 ; 2.552 ; 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 WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3RZY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-MAY-11. REMARK 100 THE RCSB ID CODE IS RCSB065586. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-APR-11 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 : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.94312 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE REMARK 200 DATA SCALING SOFTWARE : SCALA REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53794 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.080 REMARK 200 RESOLUTION RANGE LOW (A) : 43.500 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 200 DATA REDUNDANCY : 4.000 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.04900 REMARK 200 FOR THE DATA SET : 11.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.08 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.13 REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7 REMARK 200 DATA REDUNDANCY IN SHELL : 3.40 REMARK 200 R MERGE FOR SHELL (I) : 0.43700 REMARK 200 R SYM FOR SHELL (I) : 0.43700 REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10 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 16.26250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.47550 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 26.71150 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.47550 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.26250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 26.71150 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 OE1 GLU A 14 O HOH A 146 2.00 REMARK 500 O LEU A 86 O HOH A 139 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 OD2 ASP A 71 O HOH A 255 3555 1.51 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS 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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) 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 RES CSSEQI ATM2 DEVIATION REMARK 500 GLU A 22 CB GLU A 22 CG -0.124 REMARK 500 LYS A 107 CB LYS A 107 CG -0.193 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 SER A 55 N - CA - CB ANGL. DEV. = 9.3 DEGREES REMARK 500 ARG A 78 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES REMARK 500 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.6 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 ASP A 110 -134.18 51.62 REMARK 500 LYS A 120 87.98 14.71 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3P6C RELATED DB: PDB REMARK 900 RELATED ID: 3P6D 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 3RZY A 0 131 UNP P15090 FABP4_HUMAN 1 132 SEQADV 3RZY GLN A -7 UNP P15090 EXPRESSION TAG SEQADV 3RZY GLN A -6 UNP P15090 EXPRESSION TAG SEQADV 3RZY MET A -5 UNP P15090 EXPRESSION TAG SEQADV 3RZY GLY A -4 UNP P15090 EXPRESSION TAG SEQADV 3RZY ARG A -3 UNP P15090 EXPRESSION TAG SEQADV 3RZY GLY A -2 UNP P15090 EXPRESSION TAG SEQADV 3RZY 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 FORMUL 2 HOH *147(H2 O) HELIX 1 1 VAL A 5 VAL A 5 1 1 HELIX 2 2 ASN A 15 GLY A 24 1 10 HELIX 3 3 GLY A 26 ALA A 36 1 11 SHEET 1 1 1 GLY A 6 GLU A 14 0 SHEET 2 2 1 ASN A 39 ASN A 45 0 SHEET 3 3 1 VAL A 48 GLU A 54 0 SHEET 4 4 1 THR A 60 PHE A 64 0 SHEET 5 5 1 PHE A 70 VAL A 73 0 SHEET 6 6 1 LYS A 79 ASP A 87 0 SHEET 7 7 1 VAL A 90 TRP A 97 0 SHEET 8 8 1 LYS A 100 GLU A 109 0 SHEET 9 9 1 LYS A 112 MET A 119 0 SHEET 10 10 1 VAL A 122 ARG A 130 0 CRYST1 32.525 53.423 74.951 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 0.030746 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018719 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013342 0.00000 ATOM 1 N VAL A 5 6.379 11.299 1.378 1.00 12.11 N ANISOU 1 N VAL A 5 1444 1558 1598 -149 140 146 N ATOM 2 CA VAL A 5 4.942 11.548 1.295 1.00 12.70 C ANISOU 2 CA VAL A 5 1599 1521 1702 -230 122 104 C ATOM 3 C VAL A 5 4.206 10.266 1.000 1.00 12.61 C ANISOU 3 C VAL A 5 1327 1644 1820 -279 -37 -134 C ATOM 4 O VAL A 5 4.605 9.450 0.168 1.00 16.08 O ANISOU 4 O VAL A 5 1996 1922 2189 -454 376 -447 O ATOM 5 CB VAL A 5 4.673 12.604 0.245 1.00 13.97 C ANISOU 5 CB VAL A 5 1389 1695 2222 -87 -158 164 C ATOM 6 CG1 VAL A 5 3.232 12.676 -0.179 1.00 18.31 C ANISOU 6 CG1 VAL A 5 2225 2147 2585 -177 -230 395 C ATOM 7 CG2 VAL A 5 5.171 13.996 0.792 1.00 15.83 C ANISOU 7 CG2 VAL A 5 2092 1618 2302 -376 -385 39 C ATOM 8 N GLY A 6 3.098 10.098 1.688 1.00 12.81 N ANISOU 8 N GLY A 6 1636 1623 1606 -351 49 -162 N ATOM 9 CA GLY A 6 2.227 8.969 1.459 1.00 12.52 C ANISOU 9 CA GLY A 6 918 1891 1947 -385 -24 -190 C ATOM 10 C GLY A 6 1.613 8.471 2.711 1.00 11.96 C ANISOU 10 C GLY A 6 1296 1711 1535 -264 -159 -99 C ATOM 11 O GLY A 6 1.607 9.132 3.720 1.00 12.96 O ANISOU 11 O GLY A 6 1563 1599 1761 -276 150 -121 O ATOM 12 N THR A 7 1.028 7.294 2.594 1.00 11.53 N ANISOU 12 N THR A 7 944 1752 1683 -165 -330 -51 N ATOM 13 CA THR A 7 0.379 6.634 3.671 1.00 12.90 C ANISOU 13 CA THR A 7 1382 1622 1898 -77 -116 -40 C ATOM 14 C THR A 7 1.117 5.384 3.996 1.00 12.66 C ANISOU 14 C THR A 7 1486 1505 1819 -103 -45 -14 C ATOM 15 O THR A 7 1.355 4.544 3.121 1.00 14.04 O ANISOU 15 O THR A 7 1642 1789 1902 124 -279 -153 O ATOM 16 CB THR A 7 -1.057 6.253 3.228 1.00 14.12 C ANISOU 16 CB THR A 7 1191 1637 2535 -60 -68 150 C ATOM 17 OG1 THR A 7 -1.708 7.398 2.659 1.00 20.97 O ANISOU 17 OG1 THR A 7 1574 2267 4126 -337 -609 414 O ATOM 18 CG2 THR A 7 -1.881 5.733 4.406 1.00 19.15 C ANISOU 18 CG2 THR A 7 1986 2402 2885 -588 187 23 C ATOM 19 N TRP A 8 1.486 5.252 5.257 1.00 11.57 N ANISOU 19 N TRP A 8 1214 1530 1651 36 143 -3 N ATOM 20 CA TRP A 8 2.393 4.219 5.731 1.00 11.55 C ANISOU 20 CA TRP A 8 1157 1543 1687 -2 41 53 C ATOM 21 C TRP A 8 1.722 3.461 6.858 1.00 12.23 C ANISOU 21 C TRP A 8 1448 1547 1652 -193 323 -3 C ATOM 22 O TRP A 8 0.910 4.018 7.608 1.00 16.07 O ANISOU 22 O TRP A 8 2366 1658 2080 -64 672 97 O ATOM 23 CB TRP A 8 3.654 4.904 6.271 1.00 11.18 C ANISOU 23 CB TRP A 8 1189 1537 1521 4 29 217 C ATOM 24 CG TRP A 8 4.358 5.710 5.256 1.00 11.25 C ANISOU 24 CG TRP A 8 1390 1501 1383 -48 -105 45 C ATOM 25 CD1 TRP A 8 4.254 7.047 5.041 1.00 11.89 C ANISOU 25 CD1 TRP A 8 1439 1516 1560 -109 52 49 C ATOM 26 CD2 TRP A 8 5.324 5.223 4.331 1.00 10.44 C ANISOU 26 CD2 TRP A 8 930 1437 1597 82 36 11 C ATOM 27 NE1 TRP A 8 5.115 7.425 4.024 1.00 11.71 N ANISOU 27 NE1 TRP A 8 1473 1279 1695 -152 116 104 N ATOM 28 CE2 TRP A 8 5.766 6.323 3.562 1.00 10.33 C ANISOU 28 CE2 TRP A 8 620 1673 1629 -179 4 -38 C ATOM 29 CE3 TRP A 8 5.854 3.962 4.076 1.00 11.16 C ANISOU 29 CE3 TRP A 8 1154 1595 1488 -53 -138 -154 C ATOM 30 CZ2 TRP A 8 6.746 6.173 2.581 1.00 11.98 C ANISOU 30 CZ2 TRP A 8 1001 1660 1889 -308 195 97 C ATOM 31 CZ3 TRP A 8 6.802 3.817 3.094 1.00 11.43 C ANISOU 31 CZ3 TRP A 8 894 1634 1813 154 -92 -217 C ATOM 32 CH2 TRP A 8 7.193 4.905 2.351 1.00 12.23 C ANISOU 32 CH2 TRP A 8 815 2044 1786 -135 254 -196 C ATOM 33 N LYS A 9 2.025 2.184 6.981 1.00 11.25 N ANISOU 33 N LYS A 9 983 1662 1627 -194 15 187 N ATOM 34 CA LYS A 9 1.442 1.315 8.030 1.00 12.94 C ANISOU 34 CA LYS A 9 1239 1878 1799 -190 -83 140 C ATOM 35 C LYS A 9 2.553 0.632 8.767 1.00 11.13 C ANISOU 35 C LYS A 9 682 1804 1740 -259 -99 117 C ATOM 36 O LYS A 9 3.491 0.156 8.176 1.00 11.76 O ANISOU 36 O LYS A 9 1190 1577 1701 -155 15 166 O ATOM 37 CB LYS A 9 0.465 0.289 7.440 1.00 14.61 C ANISOU 37 CB LYS A 9 1207 2218 2127 -332 -294 473 C ATOM 38 CG LYS A 9 0.992 -0.662 6.446 1.00 23.00 C ANISOU 38 CG LYS A 9 2633 3125 2981 -411 -40 290 C ATOM 39 CD LYS A 9 -0.028 -1.672 5.997 1.00 28.81 C ANISOU 39 CD LYS A 9 3402 3461 4083 -596 -190 -35 C ATOM 40 CE LYS A 9 0.604 -2.625 5.026 1.00 31.40 C ANISOU 40 CE LYS A 9 3959 3859 4110 -389 52 -76 C ATOM 41 NZ LYS A 9 0.497 -2.153 3.594 1.00 35.42 N ANISOU 41 NZ LYS A 9 4644 3925 4887 152 -194 626 N ATOM 42 N LEU A 10 2.458 0.625 10.093 1.00 12.14 N ANISOU 42 N LEU A 10 959 1942 1710 -165 -51 184 N ATOM 43 CA LEU A 10 3.493 -0.019 10.918 1.00 11.39 C ANISOU 43 CA LEU A 10 256 2116 1953 -80 10 165 C ATOM 44 C LEU A 10 3.453 -1.505 10.679 1.00 13.02 C ANISOU 44 C LEU A 10 922 1975 2048 -268 -250 359 C ATOM 45 O LEU A 10 2.403 -2.132 10.857 1.00 15.99 O ANISOU 45 O LEU A 10 1105 2240 2728 -540 -279 463 O ATOM 46 CB LEU A 10 3.301 0.230 12.408 1.00 13.04 C ANISOU 46 CB LEU A 10 777 2234 1944 -98 28 169 C ATOM 47 CG LEU A 10 4.370 -0.303 13.326 1.00 13.75 C ANISOU 47 CG LEU A 10 930 2319 1974 -40 -156 247 C ATOM 48 CD1 LEU A 10 5.594 0.446 13.181 1.00 15.21 C ANISOU 48 CD1 LEU A 10 1121 2682 1973 -238 -240 298 C ATOM 49 CD2 LEU A 10 3.888 -0.240 14.790 1.00 19.54 C ANISOU 49 CD2 LEU A 10 1977 3826 1620 437 -38 330 C ATOM 50 N VAL A 11 4.616 -2.067 10.378 1.00 13.03 N ANISOU 50 N VAL A 11 1386 1403 2161 -395 -453 216 N ATOM 51 CA VAL A 11 4.782 -3.496 10.212 1.00 16.39 C ANISOU 51 CA VAL A 11 2198 1659 2368 -318 -760 138 C ATOM 52 C VAL A 11 5.677 -4.201 11.188 1.00 17.22 C ANISOU 52 C VAL A 11 2414 1742 2387 -216 -773 264 C ATOM 53 O VAL A 11 5.539 -5.421 11.334 1.00 21.12 O ANISOU 53 O VAL A 11 3098 1740 3184 -410 -1310 472 O ATOM 54 CB VAL A 11 5.214 -3.867 8.793 1.00 18.17 C ANISOU 54 CB VAL A 11 2446 1785 2671 38 -577 5 C ATOM 55 CG1 VAL A 11 4.137 -3.482 7.798 1.00 21.56 C ANISOU 55 CG1 VAL A 11 2862 2462 2866 -373 -902 139 C ATOM 56 CG2 VAL A 11 6.628 -3.397 8.375 1.00 19.50 C ANISOU 56 CG2 VAL A 11 2554 2319 2535 8 -110 -172 C ATOM 57 N SER A 12 6.596 -3.512 11.847 1.00 15.44 N ANISOU 57 N SER A 12 2178 1517 2171 -89 -730 122 N ATOM 58 CA SER A 12 7.450 -4.149 12.836 1.00 16.19 C ANISOU 58 CA SER A 12 2257 1675 2219 -60 -610 186 C ATOM 59 C SER A 12 7.975 -3.093 13.785 1.00 14.41 C ANISOU 59 C SER A 12 1721 1647 2107 -210 -512 181 C ATOM 60 O SER A 12 8.103 -1.921 13.446 1.00 12.55 O ANISOU 60 O SER A 12 1269 1529 1968 -240 -168 355 O ATOM 61 CB SER A 12 8.571 -4.907 12.195 1.00 19.50 C ANISOU 61 CB SER A 12 2690 2191 2526 23 -650 138 C ATOM 62 OG SER A 12 9.560 -4.114 11.649 1.00 21.77 O ANISOU 62 OG SER A 12 3068 2474 2730 334 -450 365 O ATOM 63 N SER A 13 8.284 -3.570 14.968 1.00 14.68 N ANISOU 63 N SER A 13 1890 1616 2070 -490 -480 298 N ATOM 64 CA SER A 13 8.802 -2.738 16.027 1.00 15.58 C ANISOU 64 CA SER A 13 2175 1718 2027 -414 -474 298 C ATOM 65 C SER A 13 9.759 -3.538 16.859 1.00 15.08 C ANISOU 65 C SER A 13 2022 1818 1888 -336 -484 384 C ATOM 66 O SER A 13 9.515 -4.727 17.172 1.00 18.26 O ANISOU 66 O SER A 13 2522 1793 2622 -572 -719 624 O ATOM 67 CB SER A 13 7.607 -2.227 16.852 1.00 17.57 C ANISOU 67 CB SER A 13 2494 2051 2129 -580 -495 52 C ATOM 68 OG SER A 13 7.970 -1.378 17.868 1.00 19.74 O ANISOU 68 OG SER A 13 3011 2255 2233 -241 -643 182 O ATOM 69 N GLU A 14 10.849 -2.925 17.241 1.00 13.15 N ANISOU 69 N GLU A 14 1705 1474 1816 -149 -501 91 N ATOM 70 CA GLU A 14 11.851 -3.540 18.119 1.00 14.05 C ANISOU 70 CA GLU A 14 1739 1521 2075 68 -333 41 C ATOM 71 C GLU A 14 12.217 -2.566 19.206 1.00 12.53 C ANISOU 71 C GLU A 14 1606 1350 1803 110 -210 74 C ATOM 72 O GLU A 14 12.516 -1.412 18.934 1.00 12.86 O ANISOU 72 O GLU A 14 1684 1414 1788 12 -262 116 O ATOM 73 CB GLU A 14 13.154 -3.934 17.356 1.00 16.70 C ANISOU 73 CB GLU A 14 1988 1987 2368 194 -239 -243 C ATOM 74 CG GLU A 14 12.959 -5.092 16.346 1.00 25.80 C ANISOU 74 CG GLU A 14 3493 2729 3578 -19 -153 -406 C ATOM 75 CD GLU A 14 12.831 -6.496 17.017 1.00 30.97 C ANISOU 75 CD GLU A 14 4520 2897 4348 -244 -225 -425 C ATOM 76 OE1 GLU A 14 13.237 -6.685 18.188 1.00 36.18 O ANISOU 76 OE1 GLU A 14 4823 3895 5027 110 -954 -385 O ATOM 77 OE2 GLU A 14 12.308 -7.430 16.370 1.00 37.25 O ANISOU 77 OE2 GLU A 14 5758 3428 4967 -478 171 -1231 O ATOM 78 N AASN A 15 12.348 -3.101 20.402 0.50 11.43 N ANISOU 78 N AASN A 15 1374 1226 1741 0 -178 153 N ATOM 79 N BASN A 15 12.062 -2.991 20.451 0.50 12.69 N ANISOU 79 N BASN A 15 1593 1433 1796 -172 -198 225 N ATOM 80 CA AASN A 15 12.797 -2.348 21.564 0.50 10.51 C ANISOU 80 CA AASN A 15 898 1433 1660 -12 -225 113 C ATOM 81 CA BASN A 15 12.607 -2.304 21.640 0.50 13.44 C ANISOU 81 CA BASN A 15 1681 1582 1842 -73 -163 150 C ATOM 82 C AASN A 15 11.946 -1.104 21.936 0.50 9.50 C ANISOU 82 C AASN A 15 361 1616 1632 0 -227 153 C ATOM 83 C BASN A 15 11.870 -1.091 22.043 0.50 11.97 C ANISOU 83 C BASN A 15 1201 1656 1690 -91 -125 248 C ATOM 84 O AASN A 15 12.417 -0.223 22.608 0.50 11.38 O ANISOU 84 O AASN A 15 1003 1578 1741 -152 -173 -82 O ATOM 85 O BASN A 15 12.324 -0.233 22.784 0.50 12.29 O ANISOU 85 O BASN A 15 1294 1626 1748 -28 -128 189 O ATOM 86 CB AASN A 15 14.282 -2.002 21.428 0.50 10.67 C ANISOU 86 CB AASN A 15 936 1366 1751 180 -230 53 C ATOM 87 CB BASN A 15 14.067 -1.979 21.499 0.50 14.01 C ANISOU 87 CB BASN A 15 1722 1650 1948 -34 -27 165 C ATOM 88 CG AASN A 15 15.023 -2.043 22.739 0.50 10.32 C ANISOU 88 CG AASN A 15 638 1654 1627 -71 -350 342 C ATOM 89 CG BASN A 15 14.871 -3.172 21.329 0.50 18.50 C ANISOU 89 CG BASN A 15 2426 2370 2232 412 70 67 C ATOM 90 OD1AASN A 15 14.800 -2.965 23.551 0.50 12.17 O ANISOU 90 OD1AASN A 15 785 1880 1957 -131 -550 250 O ATOM 91 OD1BASN A 15 14.860 -4.037 22.177 0.50 21.45 O ANISOU 91 OD1BASN A 15 3279 2005 2866 690 341 172 O ATOM 92 ND2AASN A 15 15.870 -1.065 22.980 0.50 10.48 N ANISOU 92 ND2AASN A 15 760 1620 1600 75 -86 141 N ATOM 93 ND2BASN A 15 15.621 -3.243 20.256 0.50 21.18 N ANISOU 93 ND2BASN A 15 2599 3122 2325 599 226 208 N ATOM 94 N PHE A 16 10.706 -1.023 21.514 1.00 11.12 N ANISOU 94 N PHE A 16 922 1492 1810 -4 -200 4 N ATOM 95 CA PHE A 16 9.815 0.153 21.754 1.00 11.45 C ANISOU 95 CA PHE A 16 603 1777 1967 27 -166 104 C ATOM 96 C PHE A 16 9.478 0.283 23.210 1.00 11.84 C ANISOU 96 C PHE A 16 982 1605 1911 138 -70 114 C ATOM 97 O PHE A 16 9.383 1.394 23.744 1.00 12.43 O ANISOU 97 O PHE A 16 1657 1315 1751 -210 -89 18 O ATOM 98 CB PHE A 16 8.641 0.141 20.827 1.00 12.75 C ANISOU 98 CB PHE A 16 949 1779 2114 259 -34 -104 C ATOM 99 CG PHE A 16 7.870 1.461 20.786 1.00 14.68 C ANISOU 99 CG PHE A 16 1670 2368 1541 40 -116 -191 C ATOM 100 CD1 PHE A 16 8.470 2.628 20.480 1.00 14.47 C ANISOU 100 CD1 PHE A 16 808 2275 2413 278 -220 -63 C ATOM 101 CD2 PHE A 16 6.566 1.498 20.992 1.00 16.69 C ANISOU 101 CD2 PHE A 16 2050 2386 1905 377 -242 -256 C ATOM 102 CE1 PHE A 16 7.795 3.826 20.377 1.00 17.48 C ANISOU 102 CE1 PHE A 16 1961 2306 2375 691 -507 -169 C ATOM 103 CE2 PHE A 16 5.864 2.700 20.895 1.00 16.40 C ANISOU 103 CE2 PHE A 16 1599 2660 1968 544 -85 35 C ATOM 104 CZ PHE A 16 6.496 3.848 20.629 1.00 17.21 C ANISOU 104 CZ PHE A 16 2168 2253 2115 1036 -377 -103 C ATOM 105 N ASP A 17 9.212 -0.829 23.885 1.00 12.98 N ANISOU 105 N ASP A 17 1472 1425 2034 -254 62 88 N ATOM 106 CA ASP A 17 8.880 -0.709 25.334 1.00 14.35 C ANISOU 106 CA ASP A 17 1709 1758 1982 -198 91 231 C ATOM 107 C ASP A 17 10.071 -0.135 26.136 1.00 12.58 C ANISOU 107 C ASP A 17 980 1863 1937 -243 10 458 C ATOM 108 O ASP A 17 9.868 0.751 26.951 1.00 14.02 O ANISOU 108 O ASP A 17 1928 1674 1725 -349 150 135 O ATOM 109 CB ASP A 17 8.448 -2.075 25.878 1.00 16.48 C ANISOU 109 CB ASP A 17 1819 2018 2425 -161 111 369 C ATOM 110 CG ASP A 17 7.882 -2.010 27.275 1.00 19.88 C ANISOU 110 CG ASP A 17 2569 2362 2622 -346 174 545 C ATOM 111 OD1 ASP A 17 8.460 -2.637 28.165 1.00 26.47 O ANISOU 111 OD1 ASP A 17 2907 4078 3070 274 -145 917 O ATOM 112 OD2 ASP A 17 6.937 -1.291 27.526 1.00 22.04 O ANISOU 112 OD2 ASP A 17 2918 2741 2713 139 747 437 O ATOM 113 N ASP A 18 11.271 -0.589 25.848 1.00 12.97 N ANISOU 113 N ASP A 18 1133 1866 1926 -43 -20 340 N ATOM 114 CA ASP A 18 12.466 -0.080 26.475 1.00 14.07 C ANISOU 114 CA ASP A 18 1542 1886 1915 60 -159 331 C ATOM 115 C ASP A 18 12.639 1.397 26.161 1.00 14.09 C ANISOU 115 C ASP A 18 1733 1768 1851 129 28 152 C ATOM 116 O ASP A 18 13.014 2.173 27.055 1.00 13.20 O ANISOU 116 O ASP A 18 1303 1839 1873 5 -294 170 O ATOM 117 CB ASP A 18 13.716 -0.892 26.128 1.00 16.75 C ANISOU 117 CB ASP A 18 1786 2252 2325 252 -88 263 C ATOM 118 CG ASP A 18 13.753 -2.248 26.857 1.00 25.08 C ANISOU 118 CG ASP A 18 2687 3248 3593 224 17 526 C ATOM 119 OD1 ASP A 18 12.964 -2.495 27.766 1.00 31.89 O ANISOU 119 OD1 ASP A 18 3489 4099 4525 146 -218 1519 O ATOM 120 OD2 ASP A 18 14.695 -3.023 26.567 1.00 34.12 O ANISOU 120 OD2 ASP A 18 3690 3848 5424 780 -99 344 O ATOM 121 N TYR A 19 12.388 1.808 24.922 1.00 12.02 N ANISOU 121 N TYR A 19 1390 1573 1602 2 -24 49 N ATOM 122 CA TYR A 19 12.498 3.236 24.581 1.00 10.86 C ANISOU 122 CA TYR A 19 834 1609 1682 -118 -65 95 C ATOM 123 C TYR A 19 11.478 4.036 25.381 1.00 10.49 C ANISOU 123 C TYR A 19 794 1691 1498 123 -32 224 C ATOM 124 O TYR A 19 11.825 5.054 25.981 1.00 11.43 O ANISOU 124 O TYR A 19 1279 1573 1488 -173 -89 39 O ATOM 125 CB TYR A 19 12.314 3.394 23.074 1.00 11.46 C ANISOU 125 CB TYR A 19 944 1849 1560 -180 -109 1 C ATOM 126 CG TYR A 19 12.048 4.873 22.665 1.00 10.68 C ANISOU 126 CG TYR A 19 772 1788 1496 -441 -38 -61 C ATOM 127 CD1 TYR A 19 13.085 5.704 22.573 1.00 10.48 C ANISOU 127 CD1 TYR A 19 258 1930 1792 11 -89 -91 C ATOM 128 CD2 TYR A 19 10.832 5.338 22.425 1.00 11.53 C ANISOU 128 CD2 TYR A 19 615 2081 1684 -365 -237 172 C ATOM 129 CE1 TYR A 19 12.944 7.035 22.284 1.00 10.71 C ANISOU 129 CE1 TYR A 19 650 1714 1702 -448 41 -12 C ATOM 130 CE2 TYR A 19 10.640 6.670 22.110 1.00 12.43 C ANISOU 130 CE2 TYR A 19 728 2184 1808 -158 -183 237 C ATOM 131 CZ TYR A 19 11.701 7.506 22.046 1.00 11.46 C ANISOU 131 CZ TYR A 19 962 1880 1511 -322 -104 -14 C ATOM 132 OH TYR A 19 11.495 8.860 21.725 1.00 13.37 O ANISOU 132 OH TYR A 19 1621 1665 1794 -55 -195 215 O ATOM 133 N MET A 20 10.250 3.582 25.426 1.00 10.30 N ANISOU 133 N MET A 20 778 1668 1467 -141 24 23 N ATOM 134 CA MET A 20 9.255 4.291 26.159 1.00 11.26 C ANISOU 134 CA MET A 20 1216 1591 1471 -94 52 78 C ATOM 135 C MET A 20 9.660 4.355 27.655 1.00 11.27 C ANISOU 135 C MET A 20 1007 1728 1546 -278 -8 82 C ATOM 136 O MET A 20 9.344 5.367 28.297 1.00 13.16 O ANISOU 136 O MET A 20 1737 1675 1585 -298 -151 -75 O ATOM 137 CB MET A 20 7.867 3.653 25.958 1.00 11.67 C ANISOU 137 CB MET A 20 1200 1915 1317 -156 66 51 C ATOM 138 CG MET A 20 7.283 3.911 24.613 1.00 12.38 C ANISOU 138 CG MET A 20 1245 1714 1743 108 119 90 C ATOM 139 SD MET A 20 5.535 3.414 24.515 1.00 14.72 S ANISOU 139 SD MET A 20 1201 2554 1838 -155 32 15 S ATOM 140 CE MET A 20 5.779 1.617 24.531 1.00 16.51 C ANISOU 140 CE MET A 20 1347 2520 2405 -486 23 -142 C ATOM 141 N LYS A 21 10.188 3.264 28.220 1.00 12.21 N ANISOU 141 N LYS A 21 1302 1784 1553 -260 80 137 N ATOM 142 CA LYS A 21 10.554 3.329 29.631 1.00 14.42 C ANISOU 142 CA LYS A 21 1628 2237 1611 -118 82 180 C ATOM 143 C LYS A 21 11.596 4.426 29.818 1.00 15.11 C ANISOU 143 C LYS A 21 1825 2282 1634 -208 -118 78 C ATOM 144 O LYS A 21 11.516 5.191 30.786 1.00 17.76 O ANISOU 144 O LYS A 21 2526 2546 1676 -355 -205 -20 O ATOM 145 CB LYS A 21 11.180 1.979 30.073 1.00 15.84 C ANISOU 145 CB LYS A 21 1732 2491 1792 -110 -64 262 C ATOM 146 CG LYS A 21 10.180 0.889 30.244 1.00 18.18 C ANISOU 146 CG LYS A 21 1785 2903 2220 -266 -30 425 C ATOM 147 CD LYS A 21 10.816 -0.351 30.866 1.00 20.41 C ANISOU 147 CD LYS A 21 1817 3004 2932 278 -109 646 C ATOM 148 CE LYS A 21 9.857 -1.374 31.196 1.00 26.64 C ANISOU 148 CE LYS A 21 2549 3680 3893 225 -276 712 C ATOM 149 NZ LYS A 21 10.432 -2.474 31.925 1.00 32.98 N ANISOU 149 NZ LYS A 21 2764 4664 5101 868 -674 961 N ATOM 150 N GLU A 22 12.591 4.508 28.903 1.00 14.62 N ANISOU 150 N GLU A 22 1516 2398 1638 -270 -279 124 N ATOM 151 CA GLU A 22 13.652 5.513 28.994 1.00 15.60 C ANISOU 151 CA GLU A 22 1531 2426 1970 -319 -386 -35 C ATOM 152 C GLU A 22 13.065 6.909 28.950 1.00 15.26 C ANISOU 152 C GLU A 22 1931 2214 1651 -656 -403 -36 C ATOM 153 O GLU A 22 13.540 7.813 29.641 1.00 18.05 O ANISOU 153 O GLU A 22 2215 2788 1854 -768 -300 -155 O ATOM 154 CB GLU A 22 14.782 5.177 27.972 1.00 15.11 C ANISOU 154 CB GLU A 22 1010 2584 2146 -80 -196 109 C ATOM 155 CG GLU A 22 16.088 5.582 28.238 1.00 19.18 C ANISOU 155 CG GLU A 22 690 3391 3207 450 -253 -202 C ATOM 156 CD GLU A 22 16.883 4.777 29.322 1.00 24.30 C ANISOU 156 CD GLU A 22 441 4724 4067 -128 -845 324 C ATOM 157 OE1 GLU A 22 16.214 3.868 29.874 1.00 27.84 O ANISOU 157 OE1 GLU A 22 2308 4734 3534 -600 -378 183 O ATOM 158 OE2 GLU A 22 17.990 5.084 29.648 1.00 29.38 O ANISOU 158 OE2 GLU A 22 1714 5223 4223 167 -1027 -124 O ATOM 159 N VAL A 23 12.059 7.118 28.100 1.00 14.16 N ANISOU 159 N VAL A 23 1812 1861 1707 -505 -135 36 N ATOM 160 CA VAL A 23 11.394 8.379 27.989 1.00 14.83 C ANISOU 160 CA VAL A 23 2149 1880 1606 -623 -47 -27 C ATOM 161 C VAL A 23 10.600 8.743 29.222 1.00 16.37 C ANISOU 161 C VAL A 23 2442 1968 1808 -536 -121 -86 C ATOM 162 O VAL A 23 10.406 9.908 29.495 1.00 20.26 O ANISOU 162 O VAL A 23 3600 1961 2136 -581 512 -164 O ATOM 163 CB VAL A 23 10.488 8.336 26.723 1.00 15.09 C ANISOU 163 CB VAL A 23 1893 2051 1790 -198 53 1 C ATOM 164 CG1 VAL A 23 9.494 9.522 26.659 1.00 17.77 C ANISOU 164 CG1 VAL A 23 2749 1965 2038 -73 -218 -56 C ATOM 165 CG2 VAL A 23 11.331 8.309 25.463 1.00 17.28 C ANISOU 165 CG2 VAL A 23 2632 2099 1831 -289 126 35 C ATOM 166 N GLY A 24 10.180 7.748 29.989 1.00 15.63 N ANISOU 166 N GLY A 24 2417 1940 1581 -432 -1 -89 N ATOM 167 CA GLY A 24 9.392 7.960 31.192 1.00 15.89 C ANISOU 167 CA GLY A 24 2157 2116 1765 -411 27 -133 C ATOM 168 C GLY A 24 7.912 7.662 31.085 1.00 14.91 C ANISOU 168 C GLY A 24 2156 1925 1582 -366 33 -165 C ATOM 169 O GLY A 24 7.117 8.032 31.953 1.00 16.74 O ANISOU 169 O GLY A 24 2214 2352 1794 -377 140 -274 O ATOM 170 N VAL A 25 7.491 6.936 30.074 1.00 13.35 N ANISOU 170 N VAL A 25 1751 1705 1615 -359 99 -36 N ATOM 171 CA VAL A 25 6.098 6.581 29.889 1.00 13.56 C ANISOU 171 CA VAL A 25 1871 1607 1671 -315 36 -23 C ATOM 172 C VAL A 25 5.711 5.514 30.940 1.00 13.65 C ANISOU 172 C VAL A 25 1834 1730 1620 -247 149 -47 C ATOM 173 O VAL A 25 6.441 4.569 31.173 1.00 14.96 O ANISOU 173 O VAL A 25 2150 1820 1715 -343 -54 197 O ATOM 174 CB VAL A 25 5.907 5.991 28.480 1.00 12.27 C ANISOU 174 CB VAL A 25 1326 1673 1663 -319 88 88 C ATOM 175 CG1 VAL A 25 4.494 5.706 28.232 1.00 13.90 C ANISOU 175 CG1 VAL A 25 1666 1915 1697 -329 -33 45 C ATOM 176 CG2 VAL A 25 6.444 6.945 27.368 1.00 14.49 C ANISOU 176 CG2 VAL A 25 2276 1601 1626 -304 3 327 C ATOM 177 N GLY A 26 4.550 5.735 31.545 1.00 15.59 N ANISOU 177 N GLY A 26 2133 2092 1695 -475 98 4 N ATOM 178 CA GLY A 26 4.015 4.847 32.553 1.00 15.64 C ANISOU 178 CA GLY A 26 2044 2368 1529 -429 168 -143 C ATOM 179 C GLY A 26 3.574 3.510 32.015 1.00 14.73 C ANISOU 179 C GLY A 26 1878 2139 1577 -468 200 23 C ATOM 180 O GLY A 26 3.300 3.335 30.855 1.00 14.41 O ANISOU 180 O GLY A 26 1801 2234 1437 -606 34 45 O ATOM 181 N PHE A 27 3.363 2.594 32.930 1.00 14.51 N ANISOU 181 N PHE A 27 1842 2164 1506 -514 -110 36 N ATOM 182 CA PHE A 27 3.059 1.236 32.594 1.00 14.40 C ANISOU 182 CA PHE A 27 1683 2190 1596 -433 64 64 C ATOM 183 C PHE A 27 1.845 1.105 31.673 1.00 13.30 C ANISOU 183 C PHE A 27 1629 1802 1622 -353 16 228 C ATOM 184 O PHE A 27 1.948 0.473 30.632 1.00 13.94 O ANISOU 184 O PHE A 27 1852 1934 1508 -456 -22 142 O ATOM 185 CB PHE A 27 2.799 0.427 33.894 1.00 15.05 C ANISOU 185 CB PHE A 27 1678 2352 1688 -366 -110 209 C ATOM 186 CG PHE A 27 2.426 -1.019 33.627 1.00 14.54 C ANISOU 186 CG PHE A 27 1162 2650 1711 -520 -178 338 C ATOM 187 CD1 PHE A 27 3.394 -2.012 33.505 1.00 18.43 C ANISOU 187 CD1 PHE A 27 2514 2486 2001 -306 143 389 C ATOM 188 CD2 PHE A 27 1.148 -1.372 33.525 1.00 16.28 C ANISOU 188 CD2 PHE A 27 1611 2314 2257 -188 -338 770 C ATOM 189 CE1 PHE A 27 3.015 -3.345 33.252 1.00 20.45 C ANISOU 189 CE1 PHE A 27 2926 2611 2231 -204 88 582 C ATOM 190 CE2 PHE A 27 0.769 -2.685 33.256 1.00 17.95 C ANISOU 190 CE2 PHE A 27 2092 2557 2168 -577 -274 670 C ATOM 191 CZ PHE A 27 1.690 -3.655 33.114 1.00 21.26 C ANISOU 191 CZ PHE A 27 3084 2619 2372 -383 -398 219 C ATOM 192 N ALA A 28 0.684 1.636 32.067 1.00 14.58 N ANISOU 192 N ALA A 28 1816 2026 1696 -307 98 43 N ATOM 193 CA ALA A 28 -0.535 1.396 31.297 1.00 14.11 C ANISOU 193 CA ALA A 28 1463 1977 1920 -395 -78 85 C ATOM 194 C ALA A 28 -0.428 2.002 29.931 1.00 13.46 C ANISOU 194 C ALA A 28 1461 1708 1943 -300 -9 52 C ATOM 195 O ALA A 28 -0.883 1.400 28.944 1.00 14.50 O ANISOU 195 O ALA A 28 1291 2120 2095 -408 -217 141 O ATOM 196 CB ALA A 28 -1.775 1.874 32.044 1.00 15.54 C ANISOU 196 CB ALA A 28 1865 2046 1992 -113 280 134 C ATOM 197 N THR A 29 0.121 3.193 29.823 1.00 14.14 N ANISOU 197 N THR A 29 1786 1857 1727 -365 -161 0 N ATOM 198 CA THR A 29 0.347 3.809 28.558 1.00 13.75 C ANISOU 198 CA THR A 29 1615 1883 1725 -252 -149 195 C ATOM 199 C THR A 29 1.305 2.983 27.700 1.00 13.37 C ANISOU 199 C THR A 29 1555 1886 1636 -380 -103 132 C ATOM 200 O THR A 29 1.008 2.814 26.501 1.00 14.22 O ANISOU 200 O THR A 29 1769 2055 1577 -368 -159 38 O ATOM 201 CB THR A 29 0.797 5.264 28.713 1.00 15.39 C ANISOU 201 CB THR A 29 2079 1859 1907 -404 -225 152 C ATOM 202 OG1 THR A 29 -0.175 6.009 29.442 1.00 19.70 O ANISOU 202 OG1 THR A 29 2727 2182 2574 -136 86 114 O ATOM 203 CG2 THR A 29 1.029 5.957 27.356 1.00 17.26 C ANISOU 203 CG2 THR A 29 2248 2155 2155 -50 -332 312 C ATOM 204 N ARG A 30 2.393 2.489 28.254 1.00 13.52 N ANISOU 204 N ARG A 30 1777 1849 1508 -413 -327 198 N ATOM 205 CA ARG A 30 3.274 1.673 27.457 1.00 13.10 C ANISOU 205 CA ARG A 30 1525 2009 1441 -414 -78 146 C ATOM 206 C ARG A 30 2.600 0.463 26.880 1.00 14.13 C ANISOU 206 C ARG A 30 1732 2085 1552 -352 -178 184 C ATOM 207 O ARG A 30 2.881 0.080 25.767 1.00 13.63 O ANISOU 207 O ARG A 30 1471 2247 1459 -268 -29 96 O ATOM 208 CB ARG A 30 4.553 1.195 28.222 1.00 14.51 C ANISOU 208 CB ARG A 30 1785 2182 1546 -509 -215 243 C ATOM 209 CG ARG A 30 5.516 2.259 28.594 1.00 14.28 C ANISOU 209 CG ARG A 30 1707 2089 1629 -193 34 131 C ATOM 210 CD ARG A 30 6.849 1.671 28.908 1.00 13.72 C ANISOU 210 CD ARG A 30 1269 2226 1716 -58 -217 207 C ATOM 211 NE ARG A 30 6.801 0.497 29.796 1.00 13.77 N ANISOU 211 NE ARG A 30 1529 2022 1681 -175 15 127 N ATOM 212 CZ ARG A 30 6.631 0.562 31.113 1.00 14.81 C ANISOU 212 CZ ARG A 30 1670 2041 1917 -58 -15 147 C ATOM 213 NH1 ARG A 30 6.525 1.706 31.762 1.00 16.20 N ANISOU 213 NH1 ARG A 30 2584 1964 1607 -346 -11 418 N ATOM 214 NH2 ARG A 30 6.624 -0.587 31.808 1.00 16.65 N ANISOU 214 NH2 ARG A 30 2684 1927 1712 -108 249 197 N ATOM 215 N LYS A 31 1.796 -0.208 27.711 1.00 12.99 N ANISOU 215 N LYS A 31 1393 2053 1490 -415 -70 91 N ATOM 216 CA LYS A 31 1.134 -1.409 27.255 1.00 13.24 C ANISOU 216 CA LYS A 31 1430 1966 1634 -327 7 -1 C ATOM 217 C LYS A 31 0.231 -1.138 26.103 1.00 13.02 C ANISOU 217 C LYS A 31 1196 2066 1682 -238 101 -92 C ATOM 218 O LYS A 31 0.231 -1.848 25.102 1.00 14.52 O ANISOU 218 O LYS A 31 1392 2259 1865 -156 -72 -260 O ATOM 219 CB LYS A 31 0.448 -2.131 28.375 1.00 14.09 C ANISOU 219 CB LYS A 31 1232 2054 2066 -365 51 58 C ATOM 220 CG LYS A 31 1.392 -2.651 29.438 1.00 17.34 C ANISOU 220 CG LYS A 31 1934 2408 2246 -395 -68 146 C ATOM 221 CD LYS A 31 2.312 -3.727 28.902 1.00 25.32 C ANISOU 221 CD LYS A 31 3648 2894 3077 291 -96 297 C ATOM 222 CE LYS A 31 3.440 -4.115 29.881 1.00 29.03 C ANISOU 222 CE LYS A 31 3701 3851 3477 328 -74 -78 C ATOM 223 NZ LYS A 31 4.750 -4.307 29.186 1.00 34.49 N ANISOU 223 NZ LYS A 31 4191 4761 4152 17 140 -138 N ATOM 224 N VAL A 32 -0.628 -0.151 26.271 1.00 12.24 N ANISOU 224 N VAL A 32 952 2028 1670 -149 8 -115 N ATOM 225 CA VAL A 32 -1.580 0.151 25.190 1.00 13.25 C ANISOU 225 CA VAL A 32 873 2357 1802 -294 21 -242 C ATOM 226 C VAL A 32 -0.901 0.740 23.975 1.00 12.89 C ANISOU 226 C VAL A 32 926 2243 1726 -392 1 -87 C ATOM 227 O VAL A 32 -1.263 0.424 22.836 1.00 13.60 O ANISOU 227 O VAL A 32 1039 2409 1720 -266 -62 -168 O ATOM 228 CB VAL A 32 -2.736 1.045 25.759 1.00 15.08 C ANISOU 228 CB VAL A 32 980 2710 2038 -314 -143 -237 C ATOM 229 CG1 VAL A 32 -3.670 1.557 24.669 1.00 18.82 C ANISOU 229 CG1 VAL A 32 1397 3190 2561 285 96 -155 C ATOM 230 CG2 VAL A 32 -3.481 0.298 26.860 1.00 17.31 C ANISOU 230 CG2 VAL A 32 496 3309 2772 -121 468 -128 C ATOM 231 N ALA A 33 0.022 1.641 24.170 1.00 12.67 N ANISOU 231 N ALA A 33 1095 2064 1653 -177 -142 9 N ATOM 232 CA ALA A 33 0.779 2.232 23.065 1.00 14.03 C ANISOU 232 CA ALA A 33 1560 2192 1579 -340 -194 182 C ATOM 233 C ALA A 33 1.525 1.186 22.304 1.00 13.54 C ANISOU 233 C ALA A 33 1302 2256 1586 -298 -211 248 C ATOM 234 O ALA A 33 1.684 1.246 21.091 1.00 15.22 O ANISOU 234 O ALA A 33 1717 2450 1612 -200 -146 363 O ATOM 235 CB ALA A 33 1.662 3.351 23.541 1.00 15.79 C ANISOU 235 CB ALA A 33 1829 2284 1885 -533 -201 282 C ATOM 236 N GLY A 34 2.132 0.242 23.017 1.00 14.68 N ANISOU 236 N GLY A 34 1587 2471 1517 67 -35 213 N ATOM 237 CA GLY A 34 2.913 -0.775 22.368 1.00 15.02 C ANISOU 237 CA GLY A 34 1430 2536 1738 188 112 283 C ATOM 238 C GLY A 34 2.096 -1.722 21.495 1.00 15.73 C ANISOU 238 C GLY A 34 1884 2496 1594 226 338 239 C ATOM 239 O GLY A 34 2.675 -2.274 20.578 1.00 18.00 O ANISOU 239 O GLY A 34 1643 3151 2044 295 371 -132 O ATOM 240 N MET A 35 0.804 -1.900 21.753 1.00 15.26 N ANISOU 240 N MET A 35 1939 2131 1725 64 458 262 N ATOM 241 CA MET A 35 -0.069 -2.689 20.903 1.00 14.85 C ANISOU 241 CA MET A 35 1555 2039 2047 46 371 346 C ATOM 242 C MET A 35 -0.427 -2.008 19.588 1.00 13.73 C ANISOU 242 C MET A 35 1221 1909 2087 -85 428 310 C ATOM 243 O MET A 35 -0.779 -2.689 18.636 1.00 16.83 O ANISOU 243 O MET A 35 1797 2194 2403 -336 -165 395 O ATOM 244 CB MET A 35 -1.369 -2.997 21.634 1.00 16.63 C ANISOU 244 CB MET A 35 1850 2000 2466 -31 685 465 C ATOM 245 CG MET A 35 -1.246 -3.961 22.751 1.00 16.95 C ANISOU 245 CG MET A 35 2086 2117 2235 -58 658 111 C ATOM 246 SD MET A 35 -0.732 -5.580 22.285 1.00 16.25 S ANISOU 246 SD MET A 35 1938 1921 2313 117 280 326 S ATOM 247 CE MET A 35 -2.161 -6.080 21.420 1.00 23.73 C ANISOU 247 CE MET A 35 3877 2769 2368 -637 -984 509 C ATOM 248 N ALA A 36 -0.338 -0.699 19.530 1.00 13.55 N ANISOU 248 N ALA A 36 1196 1991 1959 -50 210 365 N ATOM 249 CA ALA A 36 -0.926 0.008 18.402 1.00 13.64 C ANISOU 249 CA ALA A 36 971 2216 1994 -114 158 447 C ATOM 250 C ALA A 36 -0.099 -0.269 17.107 1.00 12.99 C ANISOU 250 C ALA A 36 942 2031 1962 -390 -39 371 C ATOM 251 O ALA A 36 1.107 -0.468 17.136 1.00 13.54 O ANISOU 251 O ALA A 36 760 2449 1934 -246 -196 214 O ATOM 252 CB ALA A 36 -0.946 1.477 18.674 1.00 16.15 C ANISOU 252 CB ALA A 36 1654 2253 2229 72 304 282 C ATOM 253 N LYS A 37 -0.871 -0.273 16.035 1.00 14.06 N ANISOU 253 N LYS A 37 1096 2101 2145 -378 -41 403 N ATOM 254 CA LYS A 37 -0.296 -0.454 14.694 1.00 15.89 C ANISOU 254 CA LYS A 37 1896 2033 2107 -291 -1 120 C ATOM 255 C LYS A 37 -0.729 0.721 13.853 1.00 14.40 C ANISOU 255 C LYS A 37 1595 1992 1882 -380 13 240 C ATOM 256 O LYS A 37 -1.609 0.638 13.047 1.00 15.79 O ANISOU 256 O LYS A 37 1561 2306 2131 -373 -174 382 O ATOM 257 CB LYS A 37 -0.730 -1.789 14.064 1.00 18.40 C ANISOU 257 CB LYS A 37 2496 2084 2412 -294 -201 111 C ATOM 258 CG LYS A 37 -0.159 -3.020 14.775 1.00 22.51 C ANISOU 258 CG LYS A 37 2893 2498 3160 -422 -217 38 C ATOM 259 CD LYS A 37 1.346 -3.071 14.573 1.00 28.39 C ANISOU 259 CD LYS A 37 3558 3603 3625 80 -190 -26 C ATOM 260 CE LYS A 37 1.889 -4.428 14.100 1.00 34.48 C ANISOU 260 CE LYS A 37 4393 4145 4561 8 -5 -179 C ATOM 261 NZ LYS A 37 1.737 -4.590 12.554 1.00 35.89 N ANISOU 261 NZ LYS A 37 4821 4502 4313 -62 318 331 N ATOM 262 N PRO A 38 -0.114 1.873 14.055 1.00 13.62 N ANISOU 262 N PRO A 38 1519 1895 1760 -162 187 212 N ATOM 263 CA PRO A 38 -0.643 3.070 13.444 1.00 15.49 C ANISOU 263 CA PRO A 38 2145 1886 1854 -97 303 190 C ATOM 264 C PRO A 38 -0.413 3.125 11.954 1.00 14.79 C ANISOU 264 C PRO A 38 2147 1692 1778 -250 525 86 C ATOM 265 O PRO A 38 0.467 2.510 11.402 1.00 14.92 O ANISOU 265 O PRO A 38 1896 1881 1890 -145 531 72 O ATOM 266 CB PRO A 38 0.166 4.191 14.101 1.00 16.65 C ANISOU 266 CB PRO A 38 2362 1896 2067 -31 207 92 C ATOM 267 CG PRO A 38 1.333 3.522 14.636 1.00 18.79 C ANISOU 267 CG PRO A 38 2027 2350 2761 -552 -93 87 C ATOM 268 CD PRO A 38 0.969 2.145 14.985 1.00 15.73 C ANISOU 268 CD PRO A 38 2010 2091 1874 -233 220 -4 C ATOM 269 N ASN A 39 -1.242 3.941 11.345 1.00 14.44 N ANISOU 269 N ASN A 39 1866 1876 1741 -195 582 176 N ATOM 270 CA ASN A 39 -1.010 4.495 10.013 1.00 15.84 C ANISOU 270 CA ASN A 39 2301 1762 1955 -258 645 28 C ATOM 271 C ASN A 39 -0.437 5.857 10.164 1.00 17.18 C ANISOU 271 C ASN A 39 2932 1632 1962 -241 884 -96 C ATOM 272 O ASN A 39 -0.897 6.662 10.947 1.00 21.94 O ANISOU 272 O ASN A 39 3844 1862 2630 -517 1441 -194 O ATOM 273 CB ASN A 39 -2.232 4.542 9.169 1.00 19.42 C ANISOU 273 CB ASN A 39 2848 2143 2385 65 317 27 C ATOM 274 CG ASN A 39 -2.499 3.241 8.466 1.00 23.88 C ANISOU 274 CG ASN A 39 3125 2896 3051 -422 -128 49 C ATOM 275 OD1 ASN A 39 -2.080 2.168 8.893 1.00 30.08 O ANISOU 275 OD1 ASN A 39 4139 3301 3988 -431 -319 -119 O ATOM 276 ND2 ASN A 39 -3.129 3.359 7.315 1.00 30.82 N ANISOU 276 ND2 ASN A 39 2843 4939 3925 -99 -869 156 N ATOM 277 N MET A 40 0.564 6.147 9.374 1.00 16.00 N ANISOU 277 N MET A 40 2665 1590 1822 -220 619 -44 N ATOM 278 CA MET A 40 1.186 7.430 9.373 1.00 15.69 C ANISOU 278 CA MET A 40 2494 1582 1882 -191 543 -76 C ATOM 279 C MET A 40 1.010 8.053 7.998 1.00 15.11 C ANISOU 279 C MET A 40 2467 1547 1726 -78 459 6 C ATOM 280 O MET A 40 1.378 7.436 7.006 1.00 15.71 O ANISOU 280 O MET A 40 2607 1562 1799 187 493 134 O ATOM 281 CB MET A 40 2.649 7.273 9.657 1.00 17.57 C ANISOU 281 CB MET A 40 2812 1845 2018 -465 334 70 C ATOM 282 CG MET A 40 3.392 8.554 9.657 1.00 19.44 C ANISOU 282 CG MET A 40 2987 2075 2321 -500 266 -71 C ATOM 283 SD MET A 40 5.065 8.423 10.170 1.00 25.01 S ANISOU 283 SD MET A 40 3825 2304 3371 -613 -826 113 S ATOM 284 CE MET A 40 5.603 7.016 9.287 1.00 25.84 C ANISOU 284 CE MET A 40 2243 3592 3983 -360 362 50 C ATOM 285 N ILE A 41 0.481 9.261 7.935 1.00 13.24 N ANISOU 285 N ILE A 41 1807 1472 1751 -127 415 -17 N ATOM 286 CA ILE A 41 0.229 9.940 6.696 1.00 13.24 C ANISOU 286 CA ILE A 41 1577 1537 1915 -323 231 -104 C ATOM 287 C ILE A 41 1.115 11.169 6.684 1.00 11.97 C ANISOU 287 C ILE A 41 1518 1284 1745 -262 83 -42 C ATOM 288 O ILE A 41 1.016 12.006 7.573 1.00 13.71 O ANISOU 288 O ILE A 41 1956 1483 1768 -466 420 -80 O ATOM 289 CB ILE A 41 -1.263 10.371 6.532 1.00 15.94 C ANISOU 289 CB ILE A 41 1772 1847 2437 -349 193 -309 C ATOM 290 CG1 ILE A 41 -2.230 9.194 6.702 1.00 20.39 C ANISOU 290 CG1 ILE A 41 1643 2699 3404 -552 148 -392 C ATOM 291 CG2 ILE A 41 -1.479 11.067 5.217 1.00 22.15 C ANISOU 291 CG2 ILE A 41 2976 2443 2997 -247 -300 -142 C ATOM 292 CD1 ILE A 41 -3.668 9.677 7.062 1.00 27.77 C ANISOU 292 CD1 ILE A 41 1278 4197 5073 -893 617 -169 C ATOM 293 N ILE A 42 1.974 11.272 5.690 1.00 10.65 N ANISOU 293 N ILE A 42 1155 1391 1500 -136 14 -59 N ATOM 294 CA ILE A 42 2.931 12.383 5.540 1.00 9.65 C ANISOU 294 CA ILE A 42 778 1416 1471 -133 50 -2 C ATOM 295 C ILE A 42 2.550 13.119 4.285 1.00 10.42 C ANISOU 295 C ILE A 42 990 1456 1513 -259 28 5 C ATOM 296 O ILE A 42 2.409 12.519 3.231 1.00 12.13 O ANISOU 296 O ILE A 42 1692 1440 1474 -83 -90 -56 O ATOM 297 CB ILE A 42 4.325 11.874 5.494 1.00 10.75 C ANISOU 297 CB ILE A 42 1277 1464 1344 -145 84 -10 C ATOM 298 CG1 ILE A 42 4.696 11.081 6.779 1.00 11.43 C ANISOU 298 CG1 ILE A 42 1029 1631 1683 210 159 -47 C ATOM 299 CG2 ILE A 42 5.289 13.055 5.274 1.00 11.07 C ANISOU 299 CG2 ILE A 42 309 1894 2000 -90 164 -127 C ATOM 300 CD1 ILE A 42 6.044 10.526 6.808 1.00 13.86 C ANISOU 300 CD1 ILE A 42 1433 1989 1844 164 -99 62 C ATOM 301 N SER A 43 2.336 14.424 4.404 1.00 10.68 N ANISOU 301 N SER A 43 1232 1463 1360 -143 -106 36 N ATOM 302 CA SER A 43 2.007 15.251 3.288 1.00 11.53 C ANISOU 302 CA SER A 43 1302 1503 1574 27 -215 77 C ATOM 303 C SER A 43 2.759 16.557 3.362 1.00 11.60 C ANISOU 303 C SER A 43 1511 1397 1499 99 -114 16 C ATOM 304 O SER A 43 3.277 16.952 4.416 1.00 11.32 O ANISOU 304 O SER A 43 1631 1370 1300 -123 -28 57 O ATOM 305 CB SER A 43 0.548 15.489 3.249 1.00 14.48 C ANISOU 305 CB SER A 43 1436 1784 2280 4 -185 284 C ATOM 306 OG SER A 43 0.097 16.150 4.372 1.00 18.94 O ANISOU 306 OG SER A 43 2176 2509 2509 449 -261 172 O ATOM 307 N VAL A 44 2.870 17.205 2.220 1.00 12.01 N ANISOU 307 N VAL A 44 1825 1334 1403 -27 -293 67 N ATOM 308 CA VAL A 44 3.557 18.471 2.094 1.00 12.10 C ANISOU 308 CA VAL A 44 1552 1412 1632 -59 -357 94 C ATOM 309 C VAL A 44 2.686 19.447 1.329 1.00 13.18 C ANISOU 309 C VAL A 44 1797 1665 1546 -67 -355 180 C ATOM 310 O VAL A 44 2.089 19.074 0.323 1.00 17.17 O ANISOU 310 O VAL A 44 3168 1604 1750 64 -799 56 O ATOM 311 CB VAL A 44 4.881 18.316 1.436 1.00 14.04 C ANISOU 311 CB VAL A 44 1359 1793 2182 35 18 187 C ATOM 312 CG1 VAL A 44 5.633 19.673 1.459 1.00 19.80 C ANISOU 312 CG1 VAL A 44 2034 2014 3474 -296 114 251 C ATOM 313 CG2 VAL A 44 5.818 17.351 2.180 1.00 18.12 C ANISOU 313 CG2 VAL A 44 1910 2348 2623 -88 -346 17 C ATOM 314 N ASN A 45 2.610 20.666 1.774 1.00 11.86 N ANISOU 314 N ASN A 45 1450 1601 1454 -32 -281 105 N ATOM 315 CA ASN A 45 1.881 21.763 1.050 1.00 11.91 C ANISOU 315 CA ASN A 45 1256 1727 1540 34 -312 177 C ATOM 316 C ASN A 45 2.773 22.977 1.213 1.00 11.53 C ANISOU 316 C ASN A 45 1196 1633 1552 -36 -204 138 C ATOM 317 O ASN A 45 2.876 23.530 2.287 1.00 11.86 O ANISOU 317 O ASN A 45 1339 1626 1540 -22 -115 194 O ATOM 318 CB ASN A 45 0.530 21.901 1.644 1.00 12.09 C ANISOU 318 CB ASN A 45 1216 1655 1721 -120 -216 28 C ATOM 319 CG ASN A 45 -0.357 22.930 0.948 1.00 12.82 C ANISOU 319 CG ASN A 45 1495 1682 1692 185 -578 65 C ATOM 320 OD1 ASN A 45 -1.627 22.738 0.866 1.00 14.87 O ANISOU 320 OD1 ASN A 45 1648 2102 1898 -7 -426 -203 O ATOM 321 ND2 ASN A 45 0.226 23.950 0.478 1.00 12.31 N ANISOU 321 ND2 ASN A 45 1166 1508 2003 80 -470 340 N ATOM 322 N GLY A 46 3.446 23.326 0.136 1.00 14.23 N ANISOU 322 N GLY A 46 1963 1861 1581 -252 -267 211 N ATOM 323 CA GLY A 46 4.402 24.404 0.220 1.00 15.84 C ANISOU 323 CA GLY A 46 2128 2037 1852 -320 -88 301 C ATOM 324 C GLY A 46 5.502 24.068 1.163 1.00 14.30 C ANISOU 324 C GLY A 46 1621 2001 1809 -433 39 353 C ATOM 325 O GLY A 46 6.122 23.028 1.027 1.00 17.38 O ANISOU 325 O GLY A 46 2336 2091 2176 -177 235 146 O ATOM 326 N ASP A 47 5.774 24.921 2.131 1.00 14.68 N ANISOU 326 N ASP A 47 1776 1939 1861 -308 90 379 N ATOM 327 CA ASP A 47 6.817 24.658 3.148 1.00 14.17 C ANISOU 327 CA ASP A 47 1223 2129 2032 -81 -112 450 C ATOM 328 C ASP A 47 6.322 23.867 4.335 1.00 11.18 C ANISOU 328 C ASP A 47 639 1767 1839 -68 -131 216 C ATOM 329 O ASP A 47 7.135 23.591 5.210 1.00 13.38 O ANISOU 329 O ASP A 47 723 2299 2059 4 -28 249 O ATOM 330 CB ASP A 47 7.343 25.997 3.667 1.00 18.17 C ANISOU 330 CB ASP A 47 2276 2393 2234 -313 -263 482 C ATOM 331 CG ASP A 47 8.007 26.816 2.626 1.00 23.43 C ANISOU 331 CG ASP A 47 2491 3167 3243 -626 -282 331 C ATOM 332 OD1 ASP A 47 8.519 26.271 1.630 1.00 29.60 O ANISOU 332 OD1 ASP A 47 3180 4646 3418 -1110 959 714 O ATOM 333 OD2 ASP A 47 7.983 28.058 2.792 1.00 33.81 O ANISOU 333 OD2 ASP A 47 4692 3316 4836 -809 -175 544 O ATOM 334 N VAL A 48 5.062 23.600 4.378 1.00 10.37 N ANISOU 334 N VAL A 48 596 1708 1634 32 -251 179 N ATOM 335 CA VAL A 48 4.490 22.950 5.564 1.00 10.27 C ANISOU 335 CA VAL A 48 824 1548 1529 -48 21 148 C ATOM 336 C VAL A 48 4.367 21.467 5.355 1.00 10.03 C ANISOU 336 C VAL A 48 805 1613 1393 -73 8 17 C ATOM 337 O VAL A 48 3.699 20.993 4.441 1.00 11.48 O ANISOU 337 O VAL A 48 1279 1584 1499 -171 -312 125 O ATOM 338 CB VAL A 48 3.067 23.532 5.907 1.00 13.12 C ANISOU 338 CB VAL A 48 1556 1755 1673 -133 12 122 C ATOM 339 CG1 VAL A 48 2.473 22.899 7.140 1.00 14.29 C ANISOU 339 CG1 VAL A 48 1801 1816 1811 96 345 125 C ATOM 340 CG2 VAL A 48 3.129 25.079 6.058 1.00 14.85 C ANISOU 340 CG2 VAL A 48 1661 1719 2262 276 426 23 C ATOM 341 N ILE A 49 4.962 20.740 6.273 1.00 9.35 N ANISOU 341 N ILE A 49 773 1457 1319 -232 -40 7 N ATOM 342 CA ILE A 49 4.908 19.264 6.299 1.00 9.13 C ANISOU 342 CA ILE A 49 386 1670 1411 -218 14 10 C ATOM 343 C ILE A 49 3.926 18.871 7.381 1.00 9.15 C ANISOU 343 C ILE A 49 417 1657 1403 -38 0 123 C ATOM 344 O ILE A 49 3.938 19.478 8.478 1.00 10.04 O ANISOU 344 O ILE A 49 802 1553 1456 -193 72 -7 O ATOM 345 CB ILE A 49 6.262 18.678 6.585 1.00 10.28 C ANISOU 345 CB ILE A 49 294 1909 1701 -262 26 -94 C ATOM 346 CG1 ILE A 49 7.346 19.111 5.612 1.00 11.42 C ANISOU 346 CG1 ILE A 49 311 2112 1913 -324 93 -275 C ATOM 347 CG2 ILE A 49 6.221 17.151 6.716 1.00 12.76 C ANISOU 347 CG2 ILE A 49 1943 1285 1619 4 -247 44 C ATOM 348 CD1 ILE A 49 8.668 18.898 6.021 1.00 15.42 C ANISOU 348 CD1 ILE A 49 348 3171 2337 -484 198 -148 C ATOM 349 N THR A 50 3.020 17.957 7.093 1.00 9.20 N ANISOU 349 N THR A 50 277 1758 1461 -189 18 68 N ATOM 350 CA THR A 50 2.108 17.387 8.078 1.00 9.80 C ANISOU 350 CA THR A 50 647 1522 1553 -433 152 -74 C ATOM 351 C THR A 50 2.394 15.922 8.240 1.00 10.23 C ANISOU 351 C THR A 50 845 1527 1513 -237 147 -63 C ATOM 352 O THR A 50 2.539 15.159 7.258 1.00 11.77 O ANISOU 352 O THR A 50 1619 1439 1414 -318 57 12 O ATOM 353 CB THR A 50 0.682 17.638 7.690 1.00 11.08 C ANISOU 353 CB THR A 50 614 1734 1861 -463 146 19 C ATOM 354 OG1 THR A 50 0.447 19.079 7.591 1.00 13.34 O ANISOU 354 OG1 THR A 50 995 2114 1957 -41 -164 11 O ATOM 355 CG2 THR A 50 -0.251 17.093 8.677 1.00 13.98 C ANISOU 355 CG2 THR A 50 667 2192 2451 -286 90 -149 C ATOM 356 N ILE A 51 2.512 15.480 9.492 1.00 9.93 N ANISOU 356 N ILE A 51 1036 1306 1432 -218 149 -57 N ATOM 357 CA ILE A 51 2.626 14.031 9.856 1.00 9.56 C ANISOU 357 CA ILE A 51 387 1527 1715 -175 179 -75 C ATOM 358 C ILE A 51 1.441 13.711 10.763 1.00 10.48 C ANISOU 358 C ILE A 51 398 1723 1858 7 -82 -69 C ATOM 359 O ILE A 51 1.307 14.265 11.858 1.00 12.16 O ANISOU 359 O ILE A 51 1533 1499 1587 -130 204 -81 O ATOM 360 CB ILE A 51 3.893 13.731 10.504 1.00 10.28 C ANISOU 360 CB ILE A 51 288 1769 1847 -47 231 -30 C ATOM 361 CG1 ILE A 51 5.144 14.077 9.645 1.00 12.83 C ANISOU 361 CG1 ILE A 51 1338 1496 2040 -96 63 -315 C ATOM 362 CG2 ILE A 51 3.965 12.216 10.855 1.00 12.94 C ANISOU 362 CG2 ILE A 51 1326 1565 2023 -72 -2 204 C ATOM 363 CD1 ILE A 51 6.474 13.787 10.290 1.00 14.53 C ANISOU 363 CD1 ILE A 51 814 2183 2522 128 -74 -173 C ATOM 364 N LYS A 52 0.519 12.902 10.269 1.00 11.88 N ANISOU 364 N LYS A 52 1143 1777 1591 -171 337 21 N ATOM 365 CA LYS A 52 -0.629 12.406 11.033 1.00 14.14 C ANISOU 365 CA LYS A 52 1857 1604 1909 -240 497 -135 C ATOM 366 C LYS A 52 -0.357 10.939 11.379 1.00 15.63 C ANISOU 366 C LYS A 52 2252 1627 2060 -407 593 -246 C ATOM 367 O LYS A 52 0.055 10.167 10.559 1.00 18.38 O ANISOU 367 O LYS A 52 3297 1526 2159 -379 1072 -71 O ATOM 368 CB LYS A 52 -1.864 12.568 10.152 1.00 17.35 C ANISOU 368 CB LYS A 52 1925 2309 2358 -356 382 -238 C ATOM 369 CG LYS A 52 -3.166 12.341 10.701 1.00 24.19 C ANISOU 369 CG LYS A 52 2928 3147 3116 -174 256 340 C ATOM 370 CD LYS A 52 -4.197 12.802 9.665 1.00 27.77 C ANISOU 370 CD LYS A 52 2444 4149 3956 123 -573 294 C ATOM 371 CE LYS A 52 -5.602 13.036 10.342 1.00 31.75 C ANISOU 371 CE LYS A 52 2862 4591 4608 440 -375 276 C ATOM 372 NZ LYS A 52 -6.849 13.285 9.473 1.00 34.11 N ANISOU 372 NZ LYS A 52 1706 5584 5668 132 -472 236 N ATOM 373 N SER A 53 -0.716 10.575 12.595 1.00 14.74 N ANISOU 373 N SER A 53 2034 1565 2001 -389 744 -163 N ATOM 374 CA SER A 53 -0.677 9.208 13.031 1.00 15.90 C ANISOU 374 CA SER A 53 2053 1795 2191 -500 809 -37 C ATOM 375 C SER A 53 -2.078 8.844 13.476 1.00 15.98 C ANISOU 375 C SER A 53 2108 1858 2105 -427 842 -212 C ATOM 376 O SER A 53 -2.675 9.502 14.325 1.00 19.24 O ANISOU 376 O SER A 53 2866 1952 2490 -717 1203 -285 O ATOM 377 CB SER A 53 0.273 9.036 14.172 1.00 17.74 C ANISOU 377 CB SER A 53 2306 1885 2547 -207 674 65 C ATOM 378 OG SER A 53 0.345 7.658 14.622 1.00 24.19 O ANISOU 378 OG SER A 53 3775 2463 2951 -194 430 240 O ATOM 379 N GLU A 54 -2.596 7.817 12.880 1.00 16.04 N ANISOU 379 N GLU A 54 2028 1945 2119 -598 837 -166 N ATOM 380 CA GLU A 54 -3.964 7.322 13.211 1.00 17.42 C ANISOU 380 CA GLU A 54 2145 2137 2334 -369 672 -107 C ATOM 381 C GLU A 54 -3.792 5.935 13.836 1.00 15.25 C ANISOU 381 C GLU A 54 1763 1946 2084 -479 462 -34 C ATOM 382 O GLU A 54 -3.231 5.045 13.213 1.00 15.00 O ANISOU 382 O GLU A 54 1932 1849 1917 -163 459 180 O ATOM 383 CB GLU A 54 -4.783 7.215 11.926 1.00 20.95 C ANISOU 383 CB GLU A 54 2586 2546 2827 -276 523 147 C ATOM 384 CG GLU A 54 -5.025 8.516 11.171 1.00 27.57 C ANISOU 384 CG GLU A 54 3497 3478 3497 -194 331 297 C ATOM 385 CD GLU A 54 -5.974 8.283 10.016 1.00 35.22 C ANISOU 385 CD GLU A 54 4184 4875 4322 125 -66 165 C ATOM 386 OE1 GLU A 54 -5.685 7.398 9.147 1.00 35.72 O ANISOU 386 OE1 GLU A 54 4341 5170 4058 -57 -288 -142 O ATOM 387 OE2 GLU A 54 -7.015 8.982 9.981 1.00 42.05 O ANISOU 387 OE2 GLU A 54 4787 5532 5658 658 438 152 O ATOM 388 N SER A 55 -4.259 5.732 15.064 1.00 15.58 N ANISOU 388 N SER A 55 1322 2455 2141 -273 573 -118 N ATOM 389 CA SER A 55 -4.204 4.393 15.695 1.00 16.83 C ANISOU 389 CA SER A 55 1602 2600 2193 168 355 206 C ATOM 390 C SER A 55 -5.309 4.256 16.666 1.00 16.08 C ANISOU 390 C SER A 55 1594 2416 2099 3 457 90 C ATOM 391 O SER A 55 -5.985 5.195 17.037 1.00 16.92 O ANISOU 391 O SER A 55 1907 2026 2496 216 665 440 O ATOM 392 CB SER A 55 -2.888 3.916 16.392 1.00 18.81 C ANISOU 392 CB SER A 55 2051 2543 2551 21 359 223 C ATOM 393 OG SER A 55 -2.693 4.472 17.668 1.00 17.25 O ANISOU 393 OG SER A 55 1484 2955 2116 43 82 566 O ATOM 394 N THR A 56 -5.409 3.057 17.137 1.00 16.75 N ANISOU 394 N THR A 56 1920 2152 2292 245 131 74 N ATOM 395 CA THR A 56 -6.383 2.766 18.155 1.00 17.51 C ANISOU 395 CA THR A 56 2550 1973 2130 -235 213 171 C ATOM 396 C THR A 56 -5.944 3.303 19.503 1.00 17.94 C ANISOU 396 C THR A 56 2666 2045 2104 -459 453 179 C ATOM 397 O THR A 56 -6.773 3.423 20.382 1.00 22.76 O ANISOU 397 O THR A 56 3271 3151 2225 -877 972 60 O ATOM 398 CB THR A 56 -6.538 1.214 18.314 1.00 19.92 C ANISOU 398 CB THR A 56 2846 1970 2751 -206 59 -54 C ATOM 399 OG1 THR A 56 -5.225 0.639 18.466 1.00 26.36 O ANISOU 399 OG1 THR A 56 4423 2225 3368 572 -1359 -263 O ATOM 400 CG2 THR A 56 -7.196 0.629 17.088 1.00 21.06 C ANISOU 400 CG2 THR A 56 3209 2187 2603 -99 -585 -129 C ATOM 401 N PHE A 57 -4.685 3.654 19.670 1.00 17.48 N ANISOU 401 N PHE A 57 2755 2049 1834 -238 342 238 N ATOM 402 CA PHE A 57 -4.240 4.252 20.917 1.00 18.10 C ANISOU 402 CA PHE A 57 2766 2061 2050 -251 419 256 C ATOM 403 C PHE A 57 -4.535 5.741 20.947 1.00 18.33 C ANISOU 403 C PHE A 57 2551 2090 2323 -174 585 252 C ATOM 404 O PHE A 57 -5.218 6.213 21.805 1.00 20.80 O ANISOU 404 O PHE A 57 3040 2165 2695 -171 969 142 O ATOM 405 CB PHE A 57 -2.746 3.935 21.120 1.00 19.31 C ANISOU 405 CB PHE A 57 2995 2296 2043 -80 306 316 C ATOM 406 CG PHE A 57 -2.057 4.763 22.158 1.00 22.51 C ANISOU 406 CG PHE A 57 3329 2401 2821 -77 21 529 C ATOM 407 CD1 PHE A 57 -2.496 4.777 23.446 1.00 23.27 C ANISOU 407 CD1 PHE A 57 3552 2532 2756 -161 130 -86 C ATOM 408 CD2 PHE A 57 -0.956 5.534 21.829 1.00 22.95 C ANISOU 408 CD2 PHE A 57 3094 2533 3093 137 -55 356 C ATOM 409 CE1 PHE A 57 -1.869 5.576 24.409 1.00 23.71 C ANISOU 409 CE1 PHE A 57 2986 3003 3018 -199 -256 99 C ATOM 410 CE2 PHE A 57 -0.321 6.308 22.786 1.00 25.49 C ANISOU 410 CE2 PHE A 57 3522 2751 3411 30 -109 453 C ATOM 411 CZ PHE A 57 -0.796 6.326 24.053 1.00 23.49 C ANISOU 411 CZ PHE A 57 2904 2866 3154 210 -288 -27 C ATOM 412 N ALYS A 58 -3.909 6.504 20.062 0.50 17.94 N ANISOU 412 N ALYS A 58 2448 1969 2396 -6 750 306 N ATOM 413 N BLYS A 58 -4.067 6.510 19.967 0.50 18.93 N ANISOU 413 N BLYS A 58 2474 2150 2568 -77 750 309 N ATOM 414 CA ALYS A 58 -4.187 7.905 19.954 0.50 17.88 C ANISOU 414 CA ALYS A 58 2254 1941 2598 -49 625 175 C ATOM 415 CA BLYS A 58 -4.084 7.966 20.089 0.50 19.33 C ANISOU 415 CA BLYS A 58 2369 2199 2774 -112 596 187 C ATOM 416 C ALYS A 58 -4.041 8.290 18.473 0.50 16.97 C ANISOU 416 C ALYS A 58 1983 1836 2627 -187 778 178 C ATOM 417 C BLYS A 58 -3.747 8.641 18.782 0.50 17.71 C ANISOU 417 C BLYS A 58 1990 1986 2753 -209 881 229 C ATOM 418 O ALYS A 58 -3.442 7.626 17.625 0.50 16.60 O ANISOU 418 O ALYS A 58 2005 1588 2713 -108 828 220 O ATOM 419 O BLYS A 58 -2.565 8.578 18.406 0.50 15.93 O ANISOU 419 O BLYS A 58 1424 1773 2854 4 977 133 O ATOM 420 CB ALYS A 58 -3.231 8.673 20.899 0.50 18.83 C ANISOU 420 CB ALYS A 58 2133 2005 3015 -45 499 137 C ATOM 421 CB BLYS A 58 -2.974 8.372 21.061 0.50 21.59 C ANISOU 421 CB BLYS A 58 2557 2389 3257 -202 407 227 C ATOM 422 CG ALYS A 58 -3.461 10.147 21.142 0.50 21.21 C ANISOU 422 CG ALYS A 58 2778 2377 2904 -71 108 -59 C ATOM 423 CG BLYS A 58 -3.415 9.049 22.291 0.50 24.48 C ANISOU 423 CG BLYS A 58 2801 2987 3511 -361 173 9 C ATOM 424 CD ALYS A 58 -4.657 10.448 22.013 0.50 23.66 C ANISOU 424 CD ALYS A 58 2681 2975 3334 -227 -11 -159 C ATOM 425 CD BLYS A 58 -3.639 10.532 21.975 0.50 27.30 C ANISOU 425 CD BLYS A 58 3316 3393 3660 -57 94 138 C ATOM 426 CE ALYS A 58 -4.988 11.945 21.939 0.50 25.87 C ANISOU 426 CE ALYS A 58 3057 3143 3630 48 -13 -210 C ATOM 427 CE BLYS A 58 -4.346 11.280 23.107 0.50 29.86 C ANISOU 427 CE BLYS A 58 3776 3553 4016 -36 54 -88 C ATOM 428 NZ ALYS A 58 -6.456 12.284 22.077 0.50 28.07 N ANISOU 428 NZ ALYS A 58 3227 3295 4143 334 -5 -149 N ATOM 429 NZ BLYS A 58 -4.653 12.683 22.701 0.50 31.45 N ANISOU 429 NZ BLYS A 58 3824 3526 4596 -300 124 -115 N ATOM 430 N ASN A 59 -4.719 9.336 18.151 1.00 15.87 N ANISOU 430 N ASN A 59 1680 1824 2525 -163 918 78 N ATOM 431 CA ASN A 59 -4.512 10.027 16.886 1.00 15.04 C ANISOU 431 CA ASN A 59 1174 1946 2593 -456 795 -28 C ATOM 432 C ASN A 59 -3.732 11.266 17.226 1.00 16.55 C ANISOU 432 C ASN A 59 2141 1949 2198 -383 741 -118 C ATOM 433 O ASN A 59 -4.061 11.993 18.169 1.00 20.32 O ANISOU 433 O ASN A 59 2826 2179 2716 -433 1239 -327 O ATOM 434 CB ASN A 59 -5.814 10.331 16.286 1.00 15.87 C ANISOU 434 CB ASN A 59 758 2350 2921 -317 515 135 C ATOM 435 CG ASN A 59 -6.655 9.109 16.008 1.00 19.81 C ANISOU 435 CG ASN A 59 1740 2904 2880 -440 350 -86 C ATOM 436 OD1 ASN A 59 -6.154 8.136 15.466 1.00 17.92 O ANISOU 436 OD1 ASN A 59 1315 2584 2907 -125 295 48 O ATOM 437 ND2 ASN A 59 -7.956 9.142 16.386 1.00 25.48 N ANISOU 437 ND2 ASN A 59 1834 4276 3570 -207 722 174 N ATOM 438 N THR A 60 -2.772 11.548 16.392 1.00 15.21 N ANISOU 438 N THR A 60 2020 1762 1994 -282 574 -86 N ATOM 439 CA THR A 60 -1.967 12.745 16.530 1.00 15.79 C ANISOU 439 CA THR A 60 2128 1924 1944 -247 420 -1 C ATOM 440 C THR A 60 -1.751 13.377 15.152 1.00 14.44 C ANISOU 440 C THR A 60 1905 1737 1842 -132 575 -22 C ATOM 441 O THR A 60 -1.825 12.715 14.136 1.00 13.68 O ANISOU 441 O THR A 60 1778 1563 1854 -169 460 2 O ATOM 442 CB THR A 60 -0.581 12.466 17.134 1.00 16.62 C ANISOU 442 CB THR A 60 2311 1978 2025 -65 232 30 C ATOM 443 OG1 THR A 60 0.182 11.631 16.271 1.00 18.78 O ANISOU 443 OG1 THR A 60 2059 2425 2650 95 153 275 O ATOM 444 CG2 THR A 60 -0.670 11.890 18.528 1.00 21.58 C ANISOU 444 CG2 THR A 60 2972 2684 2542 -57 134 477 C ATOM 445 N GLU A 61 -1.505 14.669 15.154 1.00 14.11 N ANISOU 445 N GLU A 61 1975 1620 1764 -251 604 -129 N ATOM 446 CA GLU A 61 -1.122 15.358 13.927 1.00 13.57 C ANISOU 446 CA GLU A 61 1681 1686 1789 -263 291 -102 C ATOM 447 C GLU A 61 -0.244 16.502 14.273 1.00 12.48 C ANISOU 447 C GLU A 61 1531 1500 1709 -163 235 -166 C ATOM 448 O GLU A 61 -0.573 17.279 15.179 1.00 14.50 O ANISOU 448 O GLU A 61 1515 1835 2156 -343 467 -209 O ATOM 449 CB GLU A 61 -2.394 15.881 13.253 1.00 16.23 C ANISOU 449 CB GLU A 61 1860 2069 2236 -295 194 -23 C ATOM 450 CG GLU A 61 -2.178 16.680 11.993 1.00 21.15 C ANISOU 450 CG GLU A 61 2307 2877 2849 -562 -78 286 C ATOM 451 CD GLU A 61 -3.512 17.246 11.441 1.00 28.90 C ANISOU 451 CD GLU A 61 2627 4015 4339 -655 -107 681 C ATOM 452 OE1 GLU A 61 -3.465 18.376 10.884 1.00 35.98 O ANISOU 452 OE1 GLU A 61 4100 4327 5244 -859 163 1194 O ATOM 453 OE2 GLU A 61 -4.606 16.625 11.630 1.00 35.99 O ANISOU 453 OE2 GLU A 61 3378 5011 5283 -1258 -323 638 O ATOM 454 N ILE A 62 0.863 16.621 13.542 1.00 11.39 N ANISOU 454 N ILE A 62 1419 1437 1470 -185 219 -150 N ATOM 455 CA ILE A 62 1.765 17.758 13.658 1.00 12.26 C ANISOU 455 CA ILE A 62 1739 1439 1477 -452 82 -210 C ATOM 456 C ILE A 62 1.916 18.399 12.278 1.00 11.51 C ANISOU 456 C ILE A 62 1472 1437 1462 -224 269 57 C ATOM 457 O ILE A 62 1.978 17.672 11.277 1.00 13.22 O ANISOU 457 O ILE A 62 2258 1324 1439 -262 199 -39 O ATOM 458 CB ILE A 62 3.120 17.410 14.316 1.00 12.22 C ANISOU 458 CB ILE A 62 1588 1643 1412 -449 -9 -20 C ATOM 459 CG1 ILE A 62 3.879 16.364 13.541 1.00 13.93 C ANISOU 459 CG1 ILE A 62 1803 1816 1671 -418 -369 111 C ATOM 460 CG2 ILE A 62 2.856 16.966 15.763 1.00 17.05 C ANISOU 460 CG2 ILE A 62 2661 2118 1699 -240 35 173 C ATOM 461 CD1 ILE A 62 5.303 16.129 13.989 1.00 16.43 C ANISOU 461 CD1 ILE A 62 1900 2280 2060 -164 -485 16 C ATOM 462 N SER A 63 2.009 19.696 12.246 1.00 10.11 N ANISOU 462 N SER A 63 961 1490 1389 -121 113 -101 N ATOM 463 CA SER A 63 2.341 20.457 11.051 1.00 9.60 C ANISOU 463 CA SER A 63 633 1591 1423 -76 10 -28 C ATOM 464 C SER A 63 3.494 21.380 11.411 1.00 9.51 C ANISOU 464 C SER A 63 708 1358 1547 19 16 3 C ATOM 465 O SER A 63 3.496 21.986 12.469 1.00 11.24 O ANISOU 465 O SER A 63 1067 1515 1686 -281 268 -231 O ATOM 466 CB SER A 63 1.178 21.238 10.481 1.00 11.53 C ANISOU 466 CB SER A 63 955 1810 1616 -52 -87 1 C ATOM 467 OG SER A 63 0.174 20.371 10.026 1.00 13.78 O ANISOU 467 OG SER A 63 1019 2084 2130 70 -294 -168 O ATOM 468 N PHE A 64 4.458 21.508 10.522 1.00 9.41 N ANISOU 468 N PHE A 64 825 1429 1318 -34 36 7 N ATOM 469 CA PHE A 64 5.690 22.217 10.844 1.00 8.59 C ANISOU 469 CA PHE A 64 445 1343 1477 -109 -63 -28 C ATOM 470 C PHE A 64 6.355 22.644 9.565 1.00 9.52 C ANISOU 470 C PHE A 64 718 1398 1498 21 -50 83 C ATOM 471 O PHE A 64 6.122 22.110 8.486 1.00 9.19 O ANISOU 471 O PHE A 64 646 1445 1401 -134 21 39 O ATOM 472 CB PHE A 64 6.556 21.361 11.734 1.00 9.97 C ANISOU 472 CB PHE A 64 830 1505 1451 -287 -41 70 C ATOM 473 CG PHE A 64 6.928 20.059 11.105 1.00 9.72 C ANISOU 473 CG PHE A 64 313 1717 1663 -254 -170 117 C ATOM 474 CD1 PHE A 64 6.099 18.952 11.246 1.00 10.33 C ANISOU 474 CD1 PHE A 64 656 1730 1537 -108 -81 32 C ATOM 475 CD2 PHE A 64 8.051 19.930 10.397 1.00 9.46 C ANISOU 475 CD2 PHE A 64 259 1524 1811 -28 -93 148 C ATOM 476 CE1 PHE A 64 6.438 17.759 10.626 1.00 12.38 C ANISOU 476 CE1 PHE A 64 1420 1609 1674 9 -287 52 C ATOM 477 CE2 PHE A 64 8.322 18.736 9.742 1.00 11.52 C ANISOU 477 CE2 PHE A 64 907 1698 1772 210 -101 147 C ATOM 478 CZ PHE A 64 7.518 17.659 9.873 1.00 12.47 C ANISOU 478 CZ PHE A 64 1743 1512 1480 31 -194 -95 C ATOM 479 N ILE A 65 7.318 23.560 9.765 1.00 9.34 N ANISOU 479 N ILE A 65 485 1673 1388 -47 120 -100 N ATOM 480 CA ILE A 65 8.259 23.977 8.768 1.00 9.74 C ANISOU 480 CA ILE A 65 769 1380 1552 30 198 -53 C ATOM 481 C ILE A 65 9.628 23.541 9.224 1.00 8.95 C ANISOU 481 C ILE A 65 390 1381 1629 96 291 294 C ATOM 482 O ILE A 65 9.964 23.673 10.408 1.00 9.40 O ANISOU 482 O ILE A 65 767 1336 1467 33 19 54 O ATOM 483 CB ILE A 65 8.193 25.528 8.572 1.00 11.09 C ANISOU 483 CB ILE A 65 1181 1310 1720 15 -127 23 C ATOM 484 CG1 ILE A 65 6.756 25.874 8.049 1.00 13.66 C ANISOU 484 CG1 ILE A 65 1582 1504 2102 -159 -59 320 C ATOM 485 CG2 ILE A 65 9.211 26.016 7.632 1.00 10.60 C ANISOU 485 CG2 ILE A 65 515 1613 1900 -18 55 248 C ATOM 486 CD1 ILE A 65 6.385 27.348 7.960 1.00 15.62 C ANISOU 486 CD1 ILE A 65 1183 1786 2963 133 -250 220 C ATOM 487 N LEU A 66 10.455 22.996 8.341 1.00 8.70 N ANISOU 487 N LEU A 66 314 1492 1497 -239 124 62 N ATOM 488 CA LEU A 66 11.755 22.548 8.698 1.00 9.23 C ANISOU 488 CA LEU A 66 276 1591 1637 -72 153 173 C ATOM 489 C LEU A 66 12.563 23.631 9.350 1.00 9.48 C ANISOU 489 C LEU A 66 532 1442 1625 -132 -130 175 C ATOM 490 O LEU A 66 12.595 24.762 8.880 1.00 10.79 O ANISOU 490 O LEU A 66 641 1606 1850 -74 28 229 O ATOM 491 CB LEU A 66 12.489 21.981 7.454 1.00 10.83 C ANISOU 491 CB LEU A 66 723 1596 1793 83 241 50 C ATOM 492 CG LEU A 66 11.864 20.698 6.839 1.00 11.11 C ANISOU 492 CG LEU A 66 297 1900 2023 224 121 -232 C ATOM 493 CD1 LEU A 66 12.644 20.503 5.484 1.00 17.28 C ANISOU 493 CD1 LEU A 66 2122 2244 2198 546 447 -350 C ATOM 494 CD2 LEU A 66 12.020 19.513 7.753 1.00 14.07 C ANISOU 494 CD2 LEU A 66 1664 1582 2098 10 4 138 C ATOM 495 N GLY A 67 13.206 23.291 10.437 1.00 10.14 N ANISOU 495 N GLY A 67 791 1356 1706 -58 30 116 N ATOM 496 CA GLY A 67 14.066 24.184 11.186 1.00 10.36 C ANISOU 496 CA GLY A 67 671 1612 1651 19 89 68 C ATOM 497 C GLY A 67 13.371 25.109 12.150 1.00 9.51 C ANISOU 497 C GLY A 67 298 1514 1800 -187 39 143 C ATOM 498 O GLY A 67 14.102 25.853 12.848 1.00 11.51 O ANISOU 498 O GLY A 67 820 1604 1945 -223 -149 -42 O ATOM 499 N GLN A 68 12.084 25.075 12.204 1.00 9.12 N ANISOU 499 N GLN A 68 763 1170 1532 -243 10 -14 N ATOM 500 CA GLN A 68 11.294 26.061 12.958 1.00 9.94 C ANISOU 500 CA GLN A 68 731 1329 1715 -154 -33 -40 C ATOM 501 C GLN A 68 10.587 25.383 14.141 1.00 9.62 C ANISOU 501 C GLN A 68 370 1529 1756 -133 -76 -34 C ATOM 502 O GLN A 68 9.689 24.544 13.935 1.00 9.84 O ANISOU 502 O GLN A 68 535 1431 1770 -57 32 -64 O ATOM 503 CB GLN A 68 10.285 26.784 12.049 1.00 9.87 C ANISOU 503 CB GLN A 68 619 1321 1809 -20 -99 -37 C ATOM 504 CG GLN A 68 11.045 27.490 10.982 1.00 14.08 C ANISOU 504 CG GLN A 68 1777 1642 1931 -376 -527 177 C ATOM 505 CD GLN A 68 10.278 28.429 10.198 1.00 15.74 C ANISOU 505 CD GLN A 68 1680 1644 2652 -229 -541 300 C ATOM 506 OE1 GLN A 68 9.093 28.745 10.440 1.00 20.04 O ANISOU 506 OE1 GLN A 68 2006 2137 3470 261 -1144 242 O ATOM 507 NE2 GLN A 68 11.046 28.998 9.202 1.00 18.02 N ANISOU 507 NE2 GLN A 68 2535 1822 2489 -202 -567 593 N ATOM 508 N AGLU A 69 10.967 25.716 15.350 0.50 9.83 N ANISOU 508 N AGLU A 69 783 1214 1737 -191 70 -4 N ATOM 509 N BGLU A 69 10.994 25.732 15.357 0.50 10.33 N ANISOU 509 N BGLU A 69 790 1340 1795 -173 35 27 N ATOM 510 CA AGLU A 69 10.487 24.970 16.510 0.50 10.43 C ANISOU 510 CA AGLU A 69 1109 1277 1574 -168 27 -32 C ATOM 511 CA BGLU A 69 10.495 25.137 16.620 0.50 11.74 C ANISOU 511 CA BGLU A 69 1091 1564 1806 -82 25 31 C ATOM 512 C AGLU A 69 9.008 25.192 16.716 0.50 10.53 C ANISOU 512 C AGLU A 69 1213 1300 1486 14 156 7 C ATOM 513 C BGLU A 69 8.999 25.209 16.709 0.50 11.04 C ANISOU 513 C BGLU A 69 1190 1439 1562 8 142 52 C ATOM 514 O AGLU A 69 8.441 26.253 16.375 0.50 10.88 O ANISOU 514 O AGLU A 69 1081 1146 1905 70 -22 78 O ATOM 515 O BGLU A 69 8.418 26.244 16.345 0.50 10.98 O ANISOU 515 O BGLU A 69 1038 1202 1929 67 -53 76 O ATOM 516 CB AGLU A 69 11.330 25.363 17.733 0.50 11.52 C ANISOU 516 CB AGLU A 69 1334 1407 1634 -69 9 68 C ATOM 517 CB BGLU A 69 11.041 25.942 17.839 0.50 13.04 C ANISOU 517 CB BGLU A 69 977 2165 1809 -227 -116 281 C ATOM 518 CG AGLU A 69 10.813 24.990 19.184 0.50 14.44 C ANISOU 518 CG AGLU A 69 1842 1933 1712 32 -300 70 C ATOM 519 CG BGLU A 69 10.630 27.393 17.833 0.50 18.44 C ANISOU 519 CG BGLU A 69 1484 2710 2812 -158 -81 -134 C ATOM 520 CD AGLU A 69 11.613 25.666 20.296 0.50 21.60 C ANISOU 520 CD AGLU A 69 2356 3275 2575 88 -666 -44 C ATOM 521 CD BGLU A 69 10.715 28.140 19.197 0.50 21.69 C ANISOU 521 CD BGLU A 69 1466 3286 3486 463 -551 -137 C ATOM 522 OE1AGLU A 69 11.475 26.878 20.515 0.50 27.77 O ANISOU 522 OE1AGLU A 69 3750 3527 3275 -300 -727 -81 O ATOM 523 OE1BGLU A 69 9.869 29.081 19.469 0.50 25.12 O ANISOU 523 OE1BGLU A 69 2326 3405 3813 542 130 -433 O ATOM 524 OE2AGLU A 69 12.410 24.976 20.919 0.50 24.81 O ANISOU 524 OE2AGLU A 69 687 4833 3903 204 -1027 -146 O ATOM 525 OE2BGLU A 69 11.643 27.785 19.958 0.50 24.07 O ANISOU 525 OE2BGLU A 69 2238 3286 3620 -119 -1167 418 O ATOM 526 N PHE A 70 8.346 24.191 17.280 1.00 9.18 N ANISOU 526 N PHE A 70 741 1208 1540 196 94 -29 N ATOM 527 CA PHE A 70 6.970 24.189 17.547 1.00 9.47 C ANISOU 527 CA PHE A 70 688 1235 1673 219 263 0 C ATOM 528 C PHE A 70 6.679 23.396 18.829 1.00 11.06 C ANISOU 528 C PHE A 70 1209 1345 1646 248 310 -78 C ATOM 529 O PHE A 70 7.473 22.623 19.320 1.00 12.67 O ANISOU 529 O PHE A 70 1498 1706 1609 545 221 136 O ATOM 530 CB PHE A 70 6.149 23.632 16.352 1.00 10.95 C ANISOU 530 CB PHE A 70 1202 1368 1589 60 254 42 C ATOM 531 CG PHE A 70 6.494 22.221 15.991 1.00 10.34 C ANISOU 531 CG PHE A 70 535 1642 1751 7 54 179 C ATOM 532 CD1 PHE A 70 7.585 21.902 15.205 1.00 9.61 C ANISOU 532 CD1 PHE A 70 663 1397 1590 20 0 5 C ATOM 533 CD2 PHE A 70 5.713 21.194 16.429 1.00 12.76 C ANISOU 533 CD2 PHE A 70 1408 1466 1972 15 297 -67 C ATOM 534 CE1 PHE A 70 7.906 20.604 14.864 1.00 10.76 C ANISOU 534 CE1 PHE A 70 1085 1540 1462 -179 -11 -2 C ATOM 535 CE2 PHE A 70 6.031 19.886 16.079 1.00 12.77 C ANISOU 535 CE2 PHE A 70 912 1807 2133 -400 298 37 C ATOM 536 CZ PHE A 70 7.082 19.608 15.310 1.00 11.27 C ANISOU 536 CZ PHE A 70 1048 1556 1677 35 -20 -136 C ATOM 537 N ASP A 71 5.497 23.649 19.368 1.00 12.91 N ANISOU 537 N ASP A 71 1551 1446 1909 276 536 275 N ATOM 538 CA ASP A 71 4.918 22.880 20.503 1.00 15.38 C ANISOU 538 CA ASP A 71 2009 1859 1973 338 684 47 C ATOM 539 C ASP A 71 4.206 21.675 20.061 1.00 14.37 C ANISOU 539 C ASP A 71 1589 1960 1909 214 504 199 C ATOM 540 O ASP A 71 3.457 21.700 19.053 1.00 16.28 O ANISOU 540 O ASP A 71 1465 2238 2481 221 352 630 O ATOM 541 CB ASP A 71 3.801 23.713 21.192 1.00 16.76 C ANISOU 541 CB ASP A 71 1993 2207 2165 516 731 70 C ATOM 542 CG ASP A 71 4.289 24.934 21.745 1.00 19.92 C ANISOU 542 CG ASP A 71 2585 2713 2268 390 41 35 C ATOM 543 OD1 ASP A 71 5.274 24.816 22.484 1.00 21.57 O ANISOU 543 OD1 ASP A 71 2825 2963 2407 709 -292 109 O ATOM 544 OD2 ASP A 71 3.666 26.031 21.527 1.00 21.12 O ANISOU 544 OD2 ASP A 71 2473 2922 2630 619 -161 -198 O ATOM 545 N GLU A 72 4.443 20.581 20.766 1.00 13.72 N ANISOU 545 N GLU A 72 1399 1877 1934 83 304 370 N ATOM 546 CA GLU A 72 3.859 19.302 20.414 1.00 16.20 C ANISOU 546 CA GLU A 72 1915 2085 2155 -46 260 459 C ATOM 547 C GLU A 72 3.366 18.645 21.732 1.00 15.24 C ANISOU 547 C GLU A 72 1529 2112 2148 -39 381 473 C ATOM 548 O GLU A 72 4.047 18.705 22.728 1.00 18.04 O ANISOU 548 O GLU A 72 2019 2700 2133 -223 310 597 O ATOM 549 CB GLU A 72 4.893 18.400 19.675 1.00 16.12 C ANISOU 549 CB GLU A 72 2191 2024 1907 -76 334 298 C ATOM 550 CG GLU A 72 4.522 17.000 19.397 1.00 18.42 C ANISOU 550 CG GLU A 72 2478 2318 2201 -29 124 494 C ATOM 551 CD GLU A 72 5.531 16.155 18.680 1.00 19.96 C ANISOU 551 CD GLU A 72 3414 2232 1935 -96 448 348 C ATOM 552 OE1 GLU A 72 6.714 16.551 18.606 1.00 19.20 O ANISOU 552 OE1 GLU A 72 2949 1951 2393 -54 603 59 O ATOM 553 OE2 GLU A 72 5.163 15.017 18.237 1.00 22.86 O ANISOU 553 OE2 GLU A 72 3543 2446 2694 91 233 -14 O ATOM 554 N VAL A 73 2.181 18.094 21.713 1.00 15.73 N ANISOU 554 N VAL A 73 1586 2134 2255 67 269 634 N ATOM 555 CA VAL A 73 1.726 17.210 22.808 1.00 16.39 C ANISOU 555 CA VAL A 73 1592 2239 2394 38 424 432 C ATOM 556 C VAL A 73 1.818 15.822 22.216 1.00 16.13 C ANISOU 556 C VAL A 73 1839 2127 2160 -35 281 536 C ATOM 557 O VAL A 73 1.118 15.491 21.272 1.00 17.60 O ANISOU 557 O VAL A 73 1985 2258 2444 -52 6 575 O ATOM 558 CB VAL A 73 0.373 17.563 23.285 1.00 18.95 C ANISOU 558 CB VAL A 73 2059 2401 2740 190 646 387 C ATOM 559 CG1 VAL A 73 -0.134 16.571 24.346 1.00 20.25 C ANISOU 559 CG1 VAL A 73 1267 3221 3204 152 789 524 C ATOM 560 CG2 VAL A 73 0.400 19.030 23.852 1.00 20.40 C ANISOU 560 CG2 VAL A 73 1484 2696 3570 164 995 116 C ATOM 561 N THR A 74 2.688 14.999 22.748 1.00 15.35 N ANISOU 561 N THR A 74 1527 2119 2185 -25 228 459 N ATOM 562 CA THR A 74 3.000 13.687 22.173 1.00 16.76 C ANISOU 562 CA THR A 74 1956 2227 2185 -211 289 496 C ATOM 563 C THR A 74 1.879 12.685 22.510 1.00 17.14 C ANISOU 563 C THR A 74 1721 2345 2445 -62 194 526 C ATOM 564 O THR A 74 1.010 12.932 23.332 1.00 18.32 O ANISOU 564 O THR A 74 1908 2366 2683 -180 366 592 O ATOM 565 CB THR A 74 4.340 13.152 22.678 1.00 16.03 C ANISOU 565 CB THR A 74 1810 2334 1946 -89 58 384 C ATOM 566 OG1 THR A 74 4.159 12.883 24.063 1.00 17.17 O ANISOU 566 OG1 THR A 74 2030 2444 2049 101 227 333 O ATOM 567 CG2 THR A 74 5.423 14.164 22.412 1.00 17.06 C ANISOU 567 CG2 THR A 74 2044 2177 2260 -156 345 489 C ATOM 568 N ALA A 75 1.917 11.535 21.841 1.00 17.54 N ANISOU 568 N ALA A 75 1738 2259 2666 -315 159 419 N ATOM 569 CA ALA A 75 0.875 10.529 22.030 1.00 20.13 C ANISOU 569 CA ALA A 75 2236 2475 2938 -415 144 465 C ATOM 570 C ALA A 75 0.805 10.119 23.491 1.00 20.19 C ANISOU 570 C ALA A 75 2185 2472 3012 -715 151 629 C ATOM 571 O ALA A 75 -0.286 9.785 23.986 1.00 23.24 O ANISOU 571 O ALA A 75 2215 2950 3664 -751 290 647 O ATOM 572 CB ALA A 75 1.119 9.289 21.105 1.00 21.38 C ANISOU 572 CB ALA A 75 2453 2559 3109 -398 192 490 C ATOM 573 N ASP A 76 1.928 10.059 24.165 1.00 20.58 N ANISOU 573 N ASP A 76 2597 2526 2695 -320 255 645 N ATOM 574 CA ASP A 76 1.976 9.684 25.588 1.00 21.51 C ANISOU 574 CA ASP A 76 2883 2660 2627 -215 273 689 C ATOM 575 C ASP A 76 1.799 10.884 26.528 1.00 22.93 C ANISOU 575 C ASP A 76 3091 2944 2676 -155 551 639 C ATOM 576 O ASP A 76 2.034 10.785 27.730 1.00 26.28 O ANISOU 576 O ASP A 76 3719 3580 2685 60 446 589 O ATOM 577 CB ASP A 76 3.287 8.977 25.925 1.00 21.36 C ANISOU 577 CB ASP A 76 2808 2448 2858 -261 246 732 C ATOM 578 CG ASP A 76 4.506 9.834 25.609 1.00 20.41 C ANISOU 578 CG ASP A 76 2454 2493 2806 -50 -35 858 C ATOM 579 OD1 ASP A 76 4.682 10.253 24.434 1.00 19.45 O ANISOU 579 OD1 ASP A 76 1921 2661 2806 51 68 826 O ATOM 580 OD2 ASP A 76 5.305 10.098 26.520 1.00 20.29 O ANISOU 580 OD2 ASP A 76 2710 2209 2789 -180 74 675 O ATOM 581 N ASP A 77 1.344 12.005 25.988 1.00 22.44 N ANISOU 581 N ASP A 77 3051 2865 2610 -239 743 627 N ATOM 582 CA ASP A 77 0.994 13.196 26.741 1.00 23.58 C ANISOU 582 CA ASP A 77 2953 3249 2758 -157 813 447 C ATOM 583 C ASP A 77 2.121 14.032 27.343 1.00 23.25 C ANISOU 583 C ASP A 77 3118 3155 2562 -76 782 316 C ATOM 584 O ASP A 77 1.884 14.758 28.327 1.00 26.28 O ANISOU 584 O ASP A 77 3216 3753 3014 -112 1131 83 O ATOM 585 CB ASP A 77 -0.074 12.904 27.808 1.00 25.22 C ANISOU 585 CB ASP A 77 3095 3484 3003 -312 882 415 C ATOM 586 CG ASP A 77 -1.044 14.027 27.936 1.00 31.44 C ANISOU 586 CG ASP A 77 3527 4665 3751 -54 1058 458 C ATOM 587 OD1 ASP A 77 -1.584 14.204 29.058 1.00 39.25 O ANISOU 587 OD1 ASP A 77 4903 5940 4067 -339 1582 580 O ATOM 588 OD2 ASP A 77 -1.271 14.760 26.930 1.00 39.60 O ANISOU 588 OD2 ASP A 77 4542 5937 4567 -182 1088 933 O ATOM 589 N ARG A 78 3.320 13.987 26.759 1.00 19.75 N ANISOU 589 N ARG A 78 2783 2548 2173 46 779 411 N ATOM 590 CA ARG A 78 4.342 14.975 27.092 1.00 17.82 C ANISOU 590 CA ARG A 78 2557 2311 1903 195 553 329 C ATOM 591 C ARG A 78 4.135 16.246 26.293 1.00 16.17 C ANISOU 591 C ARG A 78 2095 2226 1820 157 723 318 C ATOM 592 O ARG A 78 3.779 16.192 25.115 1.00 17.98 O ANISOU 592 O ARG A 78 2411 2252 2169 200 465 301 O ATOM 593 CB ARG A 78 5.704 14.454 26.748 1.00 17.88 C ANISOU 593 CB ARG A 78 2625 2101 2066 163 416 264 C ATOM 594 CG ARG A 78 6.205 13.364 27.670 1.00 17.43 C ANISOU 594 CG ARG A 78 2511 2118 1992 314 268 351 C ATOM 595 CD ARG A 78 7.481 12.770 27.103 1.00 16.89 C ANISOU 595 CD ARG A 78 2185 2196 2036 88 -42 308 C ATOM 596 NE ARG A 78 7.226 11.966 25.932 1.00 16.40 N ANISOU 596 NE ARG A 78 1902 2062 2267 337 94 314 N ATOM 597 CZ ARG A 78 7.848 12.026 24.752 1.00 16.94 C ANISOU 597 CZ ARG A 78 2155 2085 2194 31 100 194 C ATOM 598 NH1 ARG A 78 8.935 12.784 24.545 1.00 15.61 N ANISOU 598 NH1 ARG A 78 1757 2246 1926 196 195 156 N ATOM 599 NH2 ARG A 78 7.383 11.244 23.778 1.00 17.49 N ANISOU 599 NH2 ARG A 78 2291 2054 2299 11 130 10 N ATOM 600 N LYS A 79 4.357 17.370 26.939 1.00 17.04 N ANISOU 600 N LYS A 79 2266 2358 1850 244 558 211 N ATOM 601 CA LYS A 79 4.380 18.674 26.294 1.00 17.05 C ANISOU 601 CA LYS A 79 2154 2304 2018 423 473 148 C ATOM 602 C LYS A 79 5.812 18.987 25.986 1.00 16.79 C ANISOU 602 C LYS A 79 2245 2210 1923 196 485 16 C ATOM 603 O LYS A 79 6.578 19.214 26.888 1.00 19.10 O ANISOU 603 O LYS A 79 2849 2631 1778 172 549 -105 O ATOM 604 CB LYS A 79 3.765 19.716 27.222 1.00 19.69 C ANISOU 604 CB LYS A 79 2591 2502 2388 435 618 129 C ATOM 605 CG LYS A 79 2.244 19.566 27.445 1.00 27.31 C ANISOU 605 CG LYS A 79 3350 3485 3539 349 553 -51 C ATOM 606 CD LYS A 79 1.694 18.211 27.809 1.00 34.90 C ANISOU 606 CD LYS A 79 4280 4377 4602 -38 405 86 C ATOM 607 CE LYS A 79 0.264 18.339 28.400 1.00 38.35 C ANISOU 607 CE LYS A 79 4546 5006 5016 1 423 140 C ATOM 608 NZ LYS A 79 -0.560 17.071 28.254 1.00 40.14 N ANISOU 608 NZ LYS A 79 5086 4934 5231 80 484 36 N ATOM 609 N VAL A 80 6.152 18.952 24.706 1.00 14.74 N ANISOU 609 N VAL A 80 2168 1857 1572 129 351 100 N ATOM 610 CA VAL A 80 7.515 19.086 24.293 1.00 14.09 C ANISOU 610 CA VAL A 80 2042 1674 1634 16 209 21 C ATOM 611 C VAL A 80 7.650 20.242 23.302 1.00 13.90 C ANISOU 611 C VAL A 80 2029 1677 1573 285 274 -20 C ATOM 612 O VAL A 80 6.693 20.727 22.702 1.00 14.94 O ANISOU 612 O VAL A 80 2081 1763 1831 187 355 220 O ATOM 613 CB VAL A 80 8.019 17.780 23.641 1.00 13.09 C ANISOU 613 CB VAL A 80 1610 1588 1773 153 247 124 C ATOM 614 CG1 VAL A 80 7.769 16.547 24.577 1.00 16.49 C ANISOU 614 CG1 VAL A 80 2823 1538 1903 1 288 278 C ATOM 615 CG2 VAL A 80 7.380 17.515 22.278 1.00 14.00 C ANISOU 615 CG2 VAL A 80 1932 1753 1632 55 326 98 C ATOM 616 N LYS A 81 8.889 20.669 23.175 1.00 12.87 N ANISOU 616 N LYS A 81 2055 1383 1453 106 125 1 N ATOM 617 CA LYS A 81 9.293 21.614 22.139 1.00 12.90 C ANISOU 617 CA LYS A 81 1803 1468 1628 167 36 -22 C ATOM 618 C LYS A 81 10.079 20.841 21.095 1.00 11.15 C ANISOU 618 C LYS A 81 1401 1251 1583 285 113 -31 C ATOM 619 O LYS A 81 11.019 20.163 21.425 1.00 12.61 O ANISOU 619 O LYS A 81 1571 1726 1492 382 -39 16 O ATOM 620 CB LYS A 81 10.129 22.721 22.750 1.00 15.24 C ANISOU 620 CB LYS A 81 2244 1762 1782 27 171 -41 C ATOM 621 CG LYS A 81 9.496 23.555 23.767 1.00 21.92 C ANISOU 621 CG LYS A 81 3059 2432 2836 33 -8 -187 C ATOM 622 CD LYS A 81 8.391 24.428 23.242 1.00 27.79 C ANISOU 622 CD LYS A 81 3687 3412 3457 229 -273 -190 C ATOM 623 CE LYS A 81 7.990 25.417 24.340 1.00 30.70 C ANISOU 623 CE LYS A 81 4116 3686 3863 217 -263 -373 C ATOM 624 NZ LYS A 81 7.056 26.426 23.814 1.00 32.67 N ANISOU 624 NZ LYS A 81 4716 3743 3953 46 -910 -249 N ATOM 625 N SER A 82 9.579 20.873 19.876 1.00 11.22 N ANISOU 625 N SER A 82 1578 1342 1341 261 108 61 N ATOM 626 CA SER A 82 10.084 20.060 18.802 1.00 9.67 C ANISOU 626 CA SER A 82 853 1321 1500 211 -14 56 C ATOM 627 C SER A 82 10.714 20.879 17.712 1.00 9.94 C ANISOU 627 C SER A 82 1129 1314 1334 208 -71 53 C ATOM 628 O SER A 82 10.212 21.956 17.367 1.00 10.28 O ANISOU 628 O SER A 82 1065 1285 1554 203 129 99 O ATOM 629 CB SER A 82 8.953 19.264 18.233 1.00 11.43 C ANISOU 629 CB SER A 82 951 1715 1676 59 244 38 C ATOM 630 OG SER A 82 8.585 18.255 19.158 1.00 13.92 O ANISOU 630 OG SER A 82 1890 1458 1940 109 396 319 O ATOM 631 N THR A 83 11.777 20.352 17.107 1.00 9.44 N ANISOU 631 N THR A 83 971 1222 1391 163 46 51 N ATOM 632 CA THR A 83 12.356 20.968 15.902 1.00 9.92 C ANISOU 632 CA THR A 83 810 1428 1528 120 -7 93 C ATOM 633 C THR A 83 12.634 19.802 14.955 1.00 10.55 C ANISOU 633 C THR A 83 1319 1275 1412 302 133 201 C ATOM 634 O THR A 83 13.251 18.820 15.374 1.00 11.67 O ANISOU 634 O THR A 83 1682 1365 1385 395 47 81 O ATOM 635 CB THR A 83 13.584 21.755 16.187 1.00 11.34 C ANISOU 635 CB THR A 83 590 1679 2040 4 -33 -22 C ATOM 636 OG1 THR A 83 13.358 22.662 17.271 1.00 15.06 O ANISOU 636 OG1 THR A 83 1846 1670 2205 24 -128 -243 O ATOM 637 CG2 THR A 83 13.940 22.489 14.931 1.00 14.44 C ANISOU 637 CG2 THR A 83 1538 1666 2280 -217 327 43 C ATOM 638 N ILE A 84 12.175 19.914 13.720 1.00 9.47 N ANISOU 638 N ILE A 84 899 1256 1443 334 127 147 N ATOM 639 CA ILE A 84 12.365 18.890 12.691 1.00 9.55 C ANISOU 639 CA ILE A 84 901 1273 1453 182 269 182 C ATOM 640 C ILE A 84 13.176 19.514 11.576 1.00 10.36 C ANISOU 640 C ILE A 84 1099 1392 1443 21 133 86 C ATOM 641 O ILE A 84 12.846 20.573 11.068 1.00 10.41 O ANISOU 641 O ILE A 84 1110 1441 1403 143 186 183 O ATOM 642 CB ILE A 84 11.020 18.306 12.237 1.00 9.42 C ANISOU 642 CB ILE A 84 767 1323 1489 214 133 128 C ATOM 643 CG1 ILE A 84 10.316 17.705 13.423 1.00 10.10 C ANISOU 643 CG1 ILE A 84 853 1539 1442 148 12 300 C ATOM 644 CG2 ILE A 84 11.282 17.225 11.158 1.00 12.00 C ANISOU 644 CG2 ILE A 84 1696 1347 1515 50 191 -93 C ATOM 645 CD1 ILE A 84 8.984 17.151 13.120 1.00 11.41 C ANISOU 645 CD1 ILE A 84 838 1844 1650 97 161 232 C ATOM 646 N THR A 85 14.269 18.838 11.188 1.00 10.18 N ANISOU 646 N THR A 85 999 1361 1507 -48 174 170 N ATOM 647 CA THR A 85 15.153 19.245 10.124 1.00 11.80 C ANISOU 647 CA THR A 85 1353 1378 1751 -25 251 57 C ATOM 648 C THR A 85 15.368 18.038 9.199 1.00 11.30 C ANISOU 648 C THR A 85 1212 1438 1643 -55 393 64 C ATOM 649 O THR A 85 15.099 16.903 9.526 1.00 12.33 O ANISOU 649 O THR A 85 1601 1473 1610 -31 460 106 O ATOM 650 CB THR A 85 16.468 19.771 10.676 1.00 12.74 C ANISOU 650 CB THR A 85 1232 1641 1966 5 317 -42 C ATOM 651 OG1 THR A 85 17.015 18.741 11.494 1.00 16.00 O ANISOU 651 OG1 THR A 85 1626 2135 2317 202 -299 -89 O ATOM 652 CG2 THR A 85 16.267 21.044 11.442 1.00 16.03 C ANISOU 652 CG2 THR A 85 1584 1952 2552 -393 279 -514 C ATOM 653 N ALEU A 86 15.658 18.351 7.945 0.50 12.53 N ANISOU 653 N ALEU A 86 1616 1474 1669 -122 235 123 N ATOM 654 N BLEU A 86 16.136 18.308 8.147 0.50 11.18 N ANISOU 654 N BLEU A 86 965 1461 1818 -17 538 34 N ATOM 655 CA ALEU A 86 16.017 17.365 6.929 0.50 12.45 C ANISOU 655 CA ALEU A 86 1255 1709 1765 -224 334 115 C ATOM 656 CA BLEU A 86 16.734 17.255 7.296 0.50 12.49 C ANISOU 656 CA BLEU A 86 1513 1453 1779 -80 318 -22 C ATOM 657 C ALEU A 86 17.533 17.400 6.726 0.50 13.51 C ANISOU 657 C ALEU A 86 1504 1812 1814 -246 406 146 C ATOM 658 C BLEU A 86 18.234 17.213 7.477 0.50 13.62 C ANISOU 658 C BLEU A 86 1284 1800 2089 -209 373 42 C ATOM 659 O ALEU A 86 18.086 18.420 6.283 0.50 16.44 O ANISOU 659 O ALEU A 86 1997 1930 2318 -87 743 32 O ATOM 660 O BLEU A 86 18.849 18.273 7.438 0.50 14.70 O ANISOU 660 O BLEU A 86 1511 1602 2473 -515 389 -65 O ATOM 661 CB ALEU A 86 15.359 17.722 5.626 0.50 14.37 C ANISOU 661 CB ALEU A 86 1720 1898 1839 -245 197 93 C ATOM 662 CB BLEU A 86 16.440 17.443 5.800 0.50 14.34 C ANISOU 662 CB BLEU A 86 1769 1854 1824 -23 229 232 C ATOM 663 CG ALEU A 86 14.157 16.998 5.041 0.50 19.81 C ANISOU 663 CG ALEU A 86 2331 2679 2514 -387 33 116 C ATOM 664 CG BLEU A 86 15.052 17.078 5.289 0.50 14.51 C ANISOU 664 CG BLEU A 86 1481 1793 2237 -123 -155 569 C ATOM 665 CD1ALEU A 86 14.088 17.401 3.587 0.50 18.06 C ANISOU 665 CD1ALEU A 86 2213 2613 2036 -475 -28 -56 C ATOM 666 CD1BLEU A 86 14.697 17.785 3.983 0.50 18.68 C ANISOU 666 CD1BLEU A 86 2446 2653 1996 -36 186 336 C ATOM 667 CD2ALEU A 86 14.168 15.462 5.103 0.50 18.03 C ANISOU 667 CD2ALEU A 86 2519 2329 2002 -922 177 -86 C ATOM 668 CD2BLEU A 86 14.906 15.566 5.139 0.50 13.31 C ANISOU 668 CD2BLEU A 86 305 2277 2472 -312 -106 119 C ATOM 669 N AASP A 87 18.209 16.319 7.115 0.50 15.11 N ANISOU 669 N AASP A 87 1735 1968 2036 -176 353 47 N ATOM 670 N BASP A 87 18.774 16.005 7.667 0.50 13.63 N ANISOU 670 N BASP A 87 1137 1903 2138 -406 308 54 N ATOM 671 CA AASP A 87 19.678 16.232 7.198 0.50 17.53 C ANISOU 671 CA AASP A 87 1958 2363 2340 -189 364 -16 C ATOM 672 CA BASP A 87 20.193 15.709 7.683 0.50 15.11 C ANISOU 672 CA BASP A 87 1229 2153 2359 -141 150 95 C ATOM 673 C AASP A 87 20.079 15.129 6.268 0.50 16.09 C ANISOU 673 C AASP A 87 1588 2300 2225 -183 434 -45 C ATOM 674 C BASP A 87 20.320 14.711 6.574 0.50 14.63 C ANISOU 674 C BASP A 87 1358 1995 2203 -238 141 150 C ATOM 675 O AASP A 87 20.000 13.959 6.612 0.50 16.86 O ANISOU 675 O AASP A 87 1576 2392 2437 -381 380 -32 O ATOM 676 O BASP A 87 19.926 13.559 6.715 0.50 17.22 O ANISOU 676 O BASP A 87 1790 2125 2627 -553 329 126 O ATOM 677 CB AASP A 87 20.113 15.885 8.645 0.50 18.07 C ANISOU 677 CB AASP A 87 1796 2652 2417 -281 287 -11 C ATOM 678 CB BASP A 87 20.662 15.019 8.965 0.50 16.49 C ANISOU 678 CB BASP A 87 1308 2303 2654 -123 115 106 C ATOM 679 CG AASP A 87 21.589 15.377 8.775 0.50 24.14 C ANISOU 679 CG AASP A 87 2381 3619 3172 -270 516 149 C ATOM 680 CG BASP A 87 22.225 15.176 9.216 0.50 20.95 C ANISOU 680 CG BASP A 87 1555 3082 3320 140 -114 307 C ATOM 681 OD1AASP A 87 22.439 15.653 7.899 0.50 30.61 O ANISOU 681 OD1AASP A 87 3429 4849 3350 -888 740 254 O ATOM 682 OD1BASP A 87 22.980 14.177 9.206 0.50 27.99 O ANISOU 682 OD1BASP A 87 1265 4041 5327 -36 118 -477 O ATOM 683 OD2AASP A 87 21.933 14.731 9.816 0.50 27.93 O ANISOU 683 OD2AASP A 87 2096 4591 3925 -363 892 621 O ATOM 684 OD2BASP A 87 22.664 16.317 9.462 0.50 30.96 O ANISOU 684 OD2BASP A 87 3146 3740 4877 -166 207 -101 O ATOM 685 N AGLY A 88 20.543 15.507 5.086 0.50 16.44 N ANISOU 685 N AGLY A 88 1969 2086 2191 -103 308 26 N ATOM 686 N BGLY A 88 20.941 15.115 5.477 0.50 16.04 N ANISOU 686 N BGLY A 88 1567 2194 2330 -191 237 119 N ATOM 687 CA AGLY A 88 20.618 14.568 4.026 0.50 16.16 C ANISOU 687 CA AGLY A 88 1942 2121 2074 -20 352 17 C ATOM 688 CA BGLY A 88 21.264 14.135 4.481 0.50 15.76 C ANISOU 688 CA BGLY A 88 1557 2276 2152 -79 123 93 C ATOM 689 C AGLY A 88 19.220 14.139 3.732 0.50 16.21 C ANISOU 689 C AGLY A 88 1984 2225 1947 -125 419 9 C ATOM 690 C BGLY A 88 20.106 13.231 4.097 0.50 15.70 C ANISOU 690 C BGLY A 88 1610 2336 2018 -100 245 11 C ATOM 691 O AGLY A 88 18.318 14.972 3.587 0.50 18.26 O ANISOU 691 O AGLY A 88 2285 2448 2202 -141 509 64 O ATOM 692 O BGLY A 88 20.242 12.031 4.018 0.50 15.88 O ANISOU 692 O BGLY A 88 1422 2293 2317 -121 173 91 O ATOM 693 N AGLY A 89 19.072 12.827 3.630 0.50 14.09 N ANISOU 693 N AGLY A 89 1664 2005 1684 -189 309 -85 N ATOM 694 N BGLY A 89 18.950 13.800 3.834 0.50 15.08 N ANISOU 694 N BGLY A 89 1648 2284 1795 -17 452 54 N ATOM 695 CA AGLY A 89 17.804 12.154 3.409 0.50 14.86 C ANISOU 695 CA AGLY A 89 1784 2081 1780 -171 217 -137 C ATOM 696 CA BGLY A 89 17.814 13.005 3.448 0.50 15.16 C ANISOU 696 CA BGLY A 89 1820 2165 1773 -34 238 -56 C ATOM 697 C AGLY A 89 17.108 11.754 4.681 0.50 13.13 C ANISOU 697 C AGLY A 89 1363 1950 1673 -196 274 -147 C ATOM 698 C BGLY A 89 17.034 12.251 4.566 0.50 13.83 C ANISOU 698 C BGLY A 89 1423 2126 1703 -266 232 2 C ATOM 699 O AGLY A 89 16.182 10.930 4.650 0.50 14.42 O ANISOU 699 O AGLY A 89 1892 1775 1812 -85 69 -303 O ATOM 700 O BGLY A 89 16.025 11.614 4.275 0.50 14.82 O ANISOU 700 O BGLY A 89 1777 2174 1678 -363 -143 -77 O ATOM 701 N VAL A 90 17.502 12.334 5.815 1.00 13.52 N ANISOU 701 N VAL A 90 1423 2064 1647 -378 344 -157 N ATOM 702 CA VAL A 90 16.888 11.835 7.041 1.00 12.90 C ANISOU 702 CA VAL A 90 1577 1626 1698 -302 280 -171 C ATOM 703 C VAL A 90 16.131 12.966 7.687 1.00 11.10 C ANISOU 703 C VAL A 90 1155 1611 1450 -54 209 -47 C ATOM 704 O VAL A 90 16.660 14.051 7.919 1.00 12.30 O ANISOU 704 O VAL A 90 1484 1465 1725 -253 362 -116 O ATOM 705 CB VAL A 90 17.928 11.265 8.028 1.00 13.75 C ANISOU 705 CB VAL A 90 1475 1690 2058 -30 390 -154 C ATOM 706 CG1 VAL A 90 17.342 10.734 9.291 1.00 14.48 C ANISOU 706 CG1 VAL A 90 1530 1986 1983 -101 395 35 C ATOM 707 CG2 VAL A 90 18.838 10.186 7.382 1.00 16.73 C ANISOU 707 CG2 VAL A 90 1417 2088 2851 460 568 -34 C ATOM 708 N ALEU A 91 14.843 12.770 7.944 0.50 10.91 N ANISOU 708 N ALEU A 91 1236 1423 1487 -88 71 -43 N ATOM 709 N BLEU A 91 14.913 12.678 8.038 0.50 10.55 N ANISOU 709 N BLEU A 91 1011 1532 1465 -134 217 8 N ATOM 710 CA ALEU A 91 14.060 13.697 8.835 0.50 11.12 C ANISOU 710 CA ALEU A 91 1378 1328 1518 55 -15 39 C ATOM 711 CA BLEU A 91 14.055 13.635 8.710 0.50 10.85 C ANISOU 711 CA BLEU A 91 1196 1400 1527 7 209 166 C ATOM 712 C ALEU A 91 14.511 13.426 10.253 0.50 11.20 C ANISOU 712 C ALEU A 91 1482 1386 1385 205 166 -52 C ATOM 713 C BLEU A 91 14.346 13.462 10.229 0.50 11.55 C ANISOU 713 C BLEU A 91 1545 1416 1427 105 332 11 C ATOM 714 O ALEU A 91 14.450 12.313 10.760 0.50 11.09 O ANISOU 714 O ALEU A 91 1648 1209 1356 154 80 56 O ATOM 715 O BLEU A 91 14.059 12.394 10.763 0.50 10.87 O ANISOU 715 O BLEU A 91 1295 1263 1570 11 412 180 O ATOM 716 CB ALEU A 91 12.515 13.575 8.745 0.50 11.44 C ANISOU 716 CB ALEU A 91 1175 1611 1557 81 -97 -45 C ATOM 717 CB BLEU A 91 12.606 13.342 8.316 0.50 10.80 C ANISOU 717 CB BLEU A 91 882 1616 1602 -129 214 183 C ATOM 718 CG ALEU A 91 11.954 14.121 7.422 0.50 12.88 C ANISOU 718 CG ALEU A 91 1577 1591 1726 36 -153 -8 C ATOM 719 CG BLEU A 91 11.730 14.446 8.865 0.50 11.37 C ANISOU 719 CG BLEU A 91 1027 1673 1618 234 376 188 C ATOM 720 CD1ALEU A 91 10.572 13.556 7.243 0.50 15.14 C ANISOU 720 CD1ALEU A 91 1682 1837 2232 -97 166 77 C ATOM 721 CD1BLEU A 91 11.882 15.726 8.091 0.50 10.91 C ANISOU 721 CD1BLEU A 91 855 1866 1422 207 216 143 C ATOM 722 CD2ALEU A 91 11.908 15.668 7.398 0.50 13.04 C ANISOU 722 CD2ALEU A 91 2378 1193 1382 434 206 81 C ATOM 723 CD2BLEU A 91 10.387 13.930 8.830 0.50 16.38 C ANISOU 723 CD2BLEU A 91 718 2505 2998 -50 820 369 C ATOM 724 N VAL A 92 14.942 14.480 10.894 1.00 9.82 N ANISOU 724 N VAL A 92 1036 1198 1497 135 223 74 N ATOM 725 CA VAL A 92 15.449 14.413 12.265 1.00 9.95 C ANISOU 725 CA VAL A 92 933 1415 1431 283 223 89 C ATOM 726 C VAL A 92 14.538 15.275 13.141 1.00 10.14 C ANISOU 726 C VAL A 92 1073 1392 1385 315 50 10 C ATOM 727 O VAL A 92 14.448 16.485 12.954 1.00 11.88 O ANISOU 727 O VAL A 92 1765 1186 1559 270 282 136 O ATOM 728 CB VAL A 92 16.863 14.836 12.374 1.00 11.38 C ANISOU 728 CB VAL A 92 877 1708 1736 220 169 42 C ATOM 729 CG1 VAL A 92 17.393 14.762 13.817 1.00 14.05 C ANISOU 729 CG1 VAL A 92 1315 2235 1788 297 -82 -117 C ATOM 730 CG2 VAL A 92 17.767 14.070 11.402 1.00 13.94 C ANISOU 730 CG2 VAL A 92 660 2271 2366 335 304 -266 C ATOM 731 N HIS A 93 13.831 14.626 14.072 1.00 9.68 N ANISOU 731 N HIS A 93 977 1293 1405 261 138 63 N ATOM 732 CA HIS A 93 12.812 15.229 14.965 1.00 9.89 C ANISOU 732 CA HIS A 93 1002 1308 1447 249 153 186 C ATOM 733 C HIS A 93 13.362 15.191 16.387 1.00 10.22 C ANISOU 733 C HIS A 93 1298 1173 1411 278 76 43 C ATOM 734 O HIS A 93 13.454 14.131 16.954 1.00 11.96 O ANISOU 734 O HIS A 93 2059 1110 1372 178 -47 36 O ATOM 735 CB HIS A 93 11.511 14.490 14.776 1.00 9.77 C ANISOU 735 CB HIS A 93 619 1563 1526 111 195 226 C ATOM 736 CG HIS A 93 10.395 14.931 15.593 1.00 10.73 C ANISOU 736 CG HIS A 93 926 1581 1570 147 -11 406 C ATOM 737 ND1 HIS A 93 9.178 14.321 15.469 1.00 14.45 N ANISOU 737 ND1 HIS A 93 757 2271 2460 71 103 767 N ATOM 738 CD2 HIS A 93 10.238 15.925 16.514 1.00 13.66 C ANISOU 738 CD2 HIS A 93 1725 1891 1574 340 307 394 C ATOM 739 CE1 HIS A 93 8.333 14.906 16.276 1.00 15.95 C ANISOU 739 CE1 HIS A 93 609 2447 3002 148 525 1053 C ATOM 740 NE2 HIS A 93 8.939 15.876 16.932 1.00 16.64 N ANISOU 740 NE2 HIS A 93 1666 2318 2338 341 596 892 N ATOM 741 N VAL A 94 13.726 16.345 16.939 1.00 9.70 N ANISOU 741 N VAL A 94 1269 1132 1284 248 -3 99 N ATOM 742 CA VAL A 94 14.181 16.449 18.298 1.00 9.89 C ANISOU 742 CA VAL A 94 867 1377 1513 97 -33 102 C ATOM 743 C VAL A 94 13.110 17.012 19.179 1.00 10.80 C ANISOU 743 C VAL A 94 1314 1364 1425 199 -4 -3 C ATOM 744 O VAL A 94 12.506 18.035 18.841 1.00 13.11 O ANISOU 744 O VAL A 94 2006 1503 1469 606 248 214 O ATOM 745 CB VAL A 94 15.417 17.287 18.387 1.00 12.41 C ANISOU 745 CB VAL A 94 1113 1725 1877 133 -60 7 C ATOM 746 CG1 VAL A 94 16.002 17.383 19.805 1.00 15.90 C ANISOU 746 CG1 VAL A 94 1795 2241 2004 -280 -394 -33 C ATOM 747 CG2 VAL A 94 16.482 16.802 17.410 1.00 15.49 C ANISOU 747 CG2 VAL A 94 1134 2440 2311 -238 190 -83 C ATOM 748 N GLN A 95 12.841 16.354 20.293 1.00 10.61 N ANISOU 748 N GLN A 95 1502 1180 1348 155 -25 13 N ATOM 749 CA GLN A 95 11.872 16.765 21.276 1.00 11.29 C ANISOU 749 CA GLN A 95 1555 1381 1352 147 -7 69 C ATOM 750 C GLN A 95 12.569 17.078 22.571 1.00 12.07 C ANISOU 750 C GLN A 95 1843 1354 1387 51 -52 66 C ATOM 751 O GLN A 95 13.315 16.231 23.089 1.00 13.00 O ANISOU 751 O GLN A 95 2018 1416 1503 204 -230 17 O ATOM 752 CB GLN A 95 10.895 15.626 21.543 1.00 11.94 C ANISOU 752 CB GLN A 95 1585 1506 1445 144 -25 42 C ATOM 753 CG GLN A 95 10.051 15.244 20.368 1.00 11.96 C ANISOU 753 CG GLN A 95 1295 1435 1811 -13 9 144 C ATOM 754 CD GLN A 95 9.053 14.130 20.633 1.00 13.16 C ANISOU 754 CD GLN A 95 1476 1632 1892 -54 -48 38 C ATOM 755 OE1 GLN A 95 8.031 14.005 19.893 1.00 16.51 O ANISOU 755 OE1 GLN A 95 1861 2288 2125 -183 -126 164 O ATOM 756 NE2 GLN A 95 9.395 13.242 21.510 1.00 14.90 N ANISOU 756 NE2 GLN A 95 2156 1483 2021 -161 -241 334 N ATOM 757 N LYS A 96 12.237 18.206 23.166 1.00 12.50 N ANISOU 757 N LYS A 96 1881 1411 1457 119 -244 -15 N ATOM 758 CA LYS A 96 12.835 18.675 24.432 1.00 13.21 C ANISOU 758 CA LYS A 96 1749 1663 1606 82 -249 -69 C ATOM 759 C LYS A 96 11.729 18.933 25.440 1.00 14.14 C ANISOU 759 C LYS A 96 2283 1516 1570 166 -146 -163 C ATOM 760 O LYS A 96 10.763 19.585 25.143 1.00 14.98 O ANISOU 760 O LYS A 96 2488 1670 1533 361 44 -151 O ATOM 761 CB LYS A 96 13.549 19.990 24.217 1.00 15.30 C ANISOU 761 CB LYS A 96 1763 2056 1991 -142 -189 -319 C ATOM 762 CG LYS A 96 14.638 19.961 23.237 1.00 19.09 C ANISOU 762 CG LYS A 96 1824 2734 2693 -154 -67 -261 C ATOM 763 CD LYS A 96 15.848 19.161 23.546 1.00 21.31 C ANISOU 763 CD LYS A 96 1798 2963 3334 161 142 -292 C ATOM 764 CE LYS A 96 17.020 19.370 22.604 1.00 21.34 C ANISOU 764 CE LYS A 96 742 3494 3870 -466 -92 -199 C ATOM 765 NZ LYS A 96 18.198 18.595 22.755 1.00 24.19 N ANISOU 765 NZ LYS A 96 1413 3785 3993 -763 -180 -19 N ATOM 766 N TRP A 97 11.932 18.422 26.651 1.00 15.03 N ANISOU 766 N TRP A 97 2444 1728 1537 242 -75 -154 N ATOM 767 CA TRP A 97 10.945 18.621 27.714 1.00 16.21 C ANISOU 767 CA TRP A 97 2681 1863 1614 338 -19 -73 C ATOM 768 C TRP A 97 11.636 18.324 29.032 1.00 19.15 C ANISOU 768 C TRP A 97 3383 2185 1705 343 -131 -187 C ATOM 769 O TRP A 97 12.485 17.459 29.103 1.00 20.14 O ANISOU 769 O TRP A 97 3715 2397 1538 560 -258 -58 O ATOM 770 CB TRP A 97 9.668 17.754 27.561 1.00 17.20 C ANISOU 770 CB TRP A 97 2850 1954 1730 198 159 -68 C ATOM 771 CG TRP A 97 9.866 16.337 27.947 1.00 16.16 C ANISOU 771 CG TRP A 97 2668 1691 1778 19 360 85 C ATOM 772 CD1 TRP A 97 9.345 15.727 29.031 1.00 18.75 C ANISOU 772 CD1 TRP A 97 2890 2432 1801 -90 445 228 C ATOM 773 CD2 TRP A 97 10.612 15.335 27.252 1.00 15.29 C ANISOU 773 CD2 TRP A 97 2412 1750 1645 -272 212 -191 C ATOM 774 NE1 TRP A 97 9.726 14.431 29.084 1.00 17.80 N ANISOU 774 NE1 TRP A 97 2853 2149 1760 27 231 197 N ATOM 775 CE2 TRP A 97 10.512 14.153 28.006 1.00 16.08 C ANISOU 775 CE2 TRP A 97 2647 1829 1633 48 98 71 C ATOM 776 CE3 TRP A 97 11.363 15.301 26.060 1.00 15.09 C ANISOU 776 CE3 TRP A 97 2321 1731 1679 -156 51 -62 C ATOM 777 CZ2 TRP A 97 11.170 12.987 27.635 1.00 16.32 C ANISOU 777 CZ2 TRP A 97 2557 1665 1976 -247 62 221 C ATOM 778 CZ3 TRP A 97 11.986 14.134 25.721 1.00 13.86 C ANISOU 778 CZ3 TRP A 97 1412 1951 1904 5 -45 -62 C ATOM 779 CH2 TRP A 97 11.855 13.005 26.487 1.00 16.39 C ANISOU 779 CH2 TRP A 97 2599 1589 2039 52 46 -186 C ATOM 780 N ASP A 98 11.333 19.115 30.059 1.00 21.91 N ANISOU 780 N ASP A 98 3932 2611 1780 384 -87 -252 N ATOM 781 CA ASP A 98 11.800 18.812 31.429 1.00 24.86 C ANISOU 781 CA ASP A 98 4165 3071 2210 194 -253 -250 C ATOM 782 C ASP A 98 13.298 18.555 31.514 1.00 24.55 C ANISOU 782 C ASP A 98 4271 2917 2139 114 -332 -457 C ATOM 783 O ASP A 98 13.758 17.683 32.259 1.00 27.61 O ANISOU 783 O ASP A 98 4785 3376 2328 165 -482 -268 O ATOM 784 CB ASP A 98 11.002 17.608 31.957 1.00 27.82 C ANISOU 784 CB ASP A 98 4517 3444 2607 201 -317 -154 C ATOM 785 CG ASP A 98 10.990 17.496 33.478 1.00 33.77 C ANISOU 785 CG ASP A 98 5286 4217 3327 167 -275 -49 C ATOM 786 OD1 ASP A 98 11.029 18.543 34.150 1.00 39.07 O ANISOU 786 OD1 ASP A 98 6067 4654 4122 544 -259 -465 O ATOM 787 OD2 ASP A 98 10.875 16.346 33.985 1.00 43.35 O ANISOU 787 OD2 ASP A 98 6846 4998 4627 343 -211 582 O ATOM 788 N GLY A 99 14.086 19.291 30.744 1.00 24.40 N ANISOU 788 N GLY A 99 4021 2899 2350 -64 -394 -608 N ATOM 789 CA GLY A 99 15.540 19.053 30.706 1.00 24.43 C ANISOU 789 CA GLY A 99 3769 2874 2638 -105 -464 -516 C ATOM 790 C GLY A 99 16.021 17.777 30.009 1.00 24.36 C ANISOU 790 C GLY A 99 3699 2896 2660 -41 -541 -446 C ATOM 791 O GLY A 99 17.219 17.502 29.956 1.00 27.26 O ANISOU 791 O GLY A 99 3828 3355 3173 -209 -1056 -611 O ATOM 792 N LYS A 100 15.106 17.036 29.391 1.00 20.61 N ANISOU 792 N LYS A 100 3369 2432 2030 -40 -730 -307 N ATOM 793 CA LYS A 100 15.362 15.794 28.654 1.00 19.69 C ANISOU 793 CA LYS A 100 3227 2373 1878 132 -639 -114 C ATOM 794 C LYS A 100 15.242 16.051 27.135 1.00 16.95 C ANISOU 794 C LYS A 100 2664 2084 1691 67 -739 -2 C ATOM 795 O LYS A 100 14.686 17.060 26.705 1.00 17.08 O ANISOU 795 O LYS A 100 3081 1649 1760 -77 -712 -69 O ATOM 796 CB LYS A 100 14.340 14.760 29.069 1.00 19.34 C ANISOU 796 CB LYS A 100 3290 2194 1865 327 -557 19 C ATOM 797 CG LYS A 100 14.364 14.373 30.539 1.00 24.46 C ANISOU 797 CG LYS A 100 3682 3317 2293 120 -445 74 C ATOM 798 CD LYS A 100 13.120 13.582 30.935 1.00 30.09 C ANISOU 798 CD LYS A 100 4340 3858 3235 103 -12 438 C ATOM 799 CE LYS A 100 12.851 13.532 32.426 1.00 34.65 C ANISOU 799 CE LYS A 100 4764 4569 3831 62 95 220 C ATOM 800 NZ LYS A 100 11.349 13.683 32.706 1.00 39.14 N ANISOU 800 NZ LYS A 100 4920 5314 4637 77 134 485 N ATOM 801 N SER A 101 15.773 15.114 26.364 1.00 16.87 N ANISOU 801 N SER A 101 2851 1842 1715 92 -625 -35 N ATOM 802 CA SER A 101 15.713 15.182 24.908 1.00 16.07 C ANISOU 802 CA SER A 101 2655 1659 1790 -21 -508 32 C ATOM 803 C SER A 101 15.639 13.803 24.330 1.00 13.81 C ANISOU 803 C SER A 101 2018 1564 1662 143 -448 55 C ATOM 804 O SER A 101 16.267 12.898 24.838 1.00 13.85 O ANISOU 804 O SER A 101 1444 1798 2019 116 -557 31 O ATOM 805 CB SER A 101 16.997 15.847 24.436 1.00 18.60 C ANISOU 805 CB SER A 101 3082 1955 2027 -269 -394 65 C ATOM 806 OG SER A 101 17.000 16.027 23.069 1.00 22.15 O ANISOU 806 OG SER A 101 3470 2415 2530 -557 -415 33 O ATOM 807 N THR A 102 14.854 13.657 23.262 1.00 11.58 N ANISOU 807 N THR A 102 1417 1474 1506 47 -407 32 N ATOM 808 CA THR A 102 14.866 12.434 22.495 1.00 11.47 C ANISOU 808 CA THR A 102 1334 1400 1622 201 -270 -41 C ATOM 809 C THR A 102 14.859 12.844 21.010 1.00 10.95 C ANISOU 809 C THR A 102 1492 1282 1383 89 -75 67 C ATOM 810 O THR A 102 14.393 13.906 20.659 1.00 11.48 O ANISOU 810 O THR A 102 1489 1277 1594 123 -159 36 O ATOM 811 CB THR A 102 13.640 11.573 22.898 1.00 12.29 C ANISOU 811 CB THR A 102 1385 1610 1675 -8 -93 -132 C ATOM 812 OG1 THR A 102 13.755 10.279 22.274 1.00 13.53 O ANISOU 812 OG1 THR A 102 1640 1396 2103 8 -91 11 O ATOM 813 CG2 THR A 102 12.350 12.171 22.550 1.00 13.10 C ANISOU 813 CG2 THR A 102 1335 1739 1900 59 -155 -38 C ATOM 814 N THR A 103 15.369 11.938 20.177 1.00 10.94 N ANISOU 814 N THR A 103 1264 1271 1619 202 -236 46 N ATOM 815 CA THR A 103 15.421 12.141 18.755 1.00 12.13 C ANISOU 815 CA THR A 103 1866 1284 1458 260 -8 86 C ATOM 816 C THR A 103 14.746 11.014 18.027 1.00 12.35 C ANISOU 816 C THR A 103 1971 1275 1444 187 -135 -45 C ATOM 817 O THR A 103 15.003 9.846 18.309 1.00 14.18 O ANISOU 817 O THR A 103 2565 1203 1618 297 -474 11 O ATOM 818 CB THR A 103 16.870 12.311 18.289 1.00 14.06 C ANISOU 818 CB THR A 103 1861 1697 1784 -1 4 -82 C ATOM 819 OG1 THR A 103 17.470 13.432 18.976 1.00 18.83 O ANISOU 819 OG1 THR A 103 2528 2357 2266 -333 -91 30 O ATOM 820 CG2 THR A 103 16.927 12.620 16.825 1.00 17.57 C ANISOU 820 CG2 THR A 103 2500 2254 1920 50 51 -110 C ATOM 821 N ILE A 104 13.907 11.345 17.062 1.00 10.66 N ANISOU 821 N ILE A 104 1489 1159 1403 194 -51 13 N ATOM 822 CA ILE A 104 13.209 10.424 16.185 1.00 10.97 C ANISOU 822 CA ILE A 104 1549 1222 1398 123 -58 37 C ATOM 823 C ILE A 104 13.685 10.713 14.775 1.00 9.88 C ANISOU 823 C ILE A 104 1121 1332 1298 59 -52 45 C ATOM 824 O ILE A 104 13.545 11.803 14.276 1.00 11.74 O ANISOU 824 O ILE A 104 1802 1324 1334 259 90 66 O ATOM 825 CB ILE A 104 11.661 10.595 16.256 1.00 12.19 C ANISOU 825 CB ILE A 104 1669 1572 1391 58 109 135 C ATOM 826 CG1 ILE A 104 11.173 10.434 17.698 1.00 13.52 C ANISOU 826 CG1 ILE A 104 1605 1738 1792 -132 347 -94 C ATOM 827 CG2 ILE A 104 10.961 9.651 15.335 1.00 14.48 C ANISOU 827 CG2 ILE A 104 1799 2106 1595 -173 -41 -105 C ATOM 828 CD1 ILE A 104 9.793 10.910 17.880 1.00 23.88 C ANISOU 828 CD1 ILE A 104 2780 3742 2551 491 624 -63 C ATOM 829 N LYS A 105 14.283 9.729 14.140 1.00 10.12 N ANISOU 829 N LYS A 105 1381 1126 1336 18 -11 48 N ATOM 830 CA LYS A 105 14.798 9.833 12.790 1.00 10.46 C ANISOU 830 CA LYS A 105 1279 1266 1427 32 53 83 C ATOM 831 C LYS A 105 13.955 8.997 11.874 1.00 10.53 C ANISOU 831 C LYS A 105 1340 1287 1373 -111 -1 47 C ATOM 832 O LYS A 105 13.585 7.883 12.200 1.00 13.38 O ANISOU 832 O LYS A 105 2284 1304 1493 -273 -222 128 O ATOM 833 CB LYS A 105 16.199 9.334 12.707 1.00 12.29 C ANISOU 833 CB LYS A 105 1437 1735 1497 -26 -7 -64 C ATOM 834 CG LYS A 105 17.205 10.229 13.465 1.00 15.84 C ANISOU 834 CG LYS A 105 1329 2456 2232 203 -176 -125 C ATOM 835 CD LYS A 105 18.654 9.930 13.291 1.00 19.64 C ANISOU 835 CD LYS A 105 1305 3310 2845 -25 -203 -132 C ATOM 836 CE LYS A 105 19.536 11.055 14.012 1.00 24.72 C ANISOU 836 CE LYS A 105 1920 3700 3772 281 -598 -182 C ATOM 837 NZ LYS A 105 21.000 10.834 14.040 1.00 32.22 N ANISOU 837 NZ LYS A 105 2571 4673 4996 605 -595 46 N ATOM 838 N ARG A 106 13.592 9.537 10.731 1.00 10.23 N ANISOU 838 N ARG A 106 1262 1254 1370 -92 75 61 N ATOM 839 CA ARG A 106 12.794 8.834 9.721 1.00 11.54 C ANISOU 839 CA ARG A 106 1456 1494 1431 -350 37 69 C ATOM 840 C ARG A 106 13.627 8.834 8.434 1.00 10.50 C ANISOU 840 C ARG A 106 1345 1281 1363 -136 -103 -10 C ATOM 841 O ARG A 106 14.073 9.872 7.962 1.00 11.67 O ANISOU 841 O ARG A 106 1674 1324 1433 -283 30 24 O ATOM 842 CB ARG A 106 11.443 9.527 9.523 1.00 12.90 C ANISOU 842 CB ARG A 106 1283 1943 1673 -464 80 57 C ATOM 843 CG ARG A 106 10.583 9.515 10.798 1.00 14.55 C ANISOU 843 CG ARG A 106 1448 2065 2015 -272 325 160 C ATOM 844 CD ARG A 106 9.322 10.311 10.669 1.00 20.07 C ANISOU 844 CD ARG A 106 1569 3302 2756 -107 659 97 C ATOM 845 NE ARG A 106 8.437 10.240 11.847 1.00 25.51 N ANISOU 845 NE ARG A 106 2315 3919 3458 -311 1204 183 N ATOM 846 CZ ARG A 106 8.414 11.090 12.857 1.00 24.38 C ANISOU 846 CZ ARG A 106 2366 3911 2987 16 813 455 C ATOM 847 NH1 ARG A 106 9.215 12.097 12.970 1.00 20.91 N ANISOU 847 NH1 ARG A 106 1972 3507 2463 741 360 757 N ATOM 848 NH2 ARG A 106 7.545 10.887 13.842 1.00 26.79 N ANISOU 848 NH2 ARG A 106 2578 4509 3091 -299 1218 314 N ATOM 849 N LYS A 107 13.732 7.671 7.809 1.00 11.16 N ANISOU 849 N LYS A 107 1413 1434 1392 -404 152 17 N ATOM 850 CA LYS A 107 14.488 7.498 6.594 1.00 12.65 C ANISOU 850 CA LYS A 107 1491 1750 1563 -155 -8 -45 C ATOM 851 C LYS A 107 13.871 6.467 5.680 1.00 13.44 C ANISOU 851 C LYS A 107 1869 1741 1497 -499 76 -43 C ATOM 852 O LYS A 107 13.347 5.494 6.124 1.00 15.15 O ANISOU 852 O LYS A 107 2326 2006 1421 -813 93 -13 O ATOM 853 CB LYS A 107 15.911 7.161 6.892 1.00 15.87 C ANISOU 853 CB LYS A 107 1979 2316 1734 -190 118 -319 C ATOM 854 CG LYS A 107 16.241 5.920 7.230 1.00 24.30 C ANISOU 854 CG LYS A 107 2929 3051 3251 -166 -149 -170 C ATOM 855 CD LYS A 107 17.672 5.606 6.562 1.00 28.61 C ANISOU 855 CD LYS A 107 2904 3852 4114 500 -6 -48 C ATOM 856 CE LYS A 107 18.639 6.779 6.385 1.00 25.78 C ANISOU 856 CE LYS A 107 3009 3235 3551 468 158 -53 C ATOM 857 NZ LYS A 107 19.327 7.049 5.060 1.00 29.45 N ANISOU 857 NZ LYS A 107 3014 4265 3908 -275 743 -304 N ATOM 858 N ARG A 108 13.988 6.697 4.401 1.00 12.23 N ANISOU 858 N ARG A 108 1496 1642 1508 -428 57 -61 N ATOM 859 CA ARG A 108 13.575 5.702 3.418 1.00 11.69 C ANISOU 859 CA ARG A 108 972 1894 1576 -340 224 1 C ATOM 860 C ARG A 108 14.678 4.654 3.249 1.00 12.65 C ANISOU 860 C ARG A 108 1120 2072 1613 -202 238 -267 C ATOM 861 O ARG A 108 15.840 4.974 3.024 1.00 15.30 O ANISOU 861 O ARG A 108 1239 2149 2422 -280 455 -500 O ATOM 862 CB ARG A 108 13.296 6.374 2.095 1.00 14.26 C ANISOU 862 CB ARG A 108 1406 2364 1645 -458 156 60 C ATOM 863 CG ARG A 108 11.960 7.077 2.049 1.00 16.76 C ANISOU 863 CG ARG A 108 2038 2422 1905 -188 48 395 C ATOM 864 CD ARG A 108 10.806 6.100 2.157 1.00 18.03 C ANISOU 864 CD ARG A 108 1703 3065 2082 -391 132 563 C ATOM 865 NE ARG A 108 10.861 4.995 1.154 1.00 18.91 N ANISOU 865 NE ARG A 108 1075 3270 2837 -281 -95 507 N ATOM 866 CZ ARG A 108 10.580 5.134 -0.125 1.00 17.10 C ANISOU 866 CZ ARG A 108 1048 2218 3229 -131 -256 74 C ATOM 867 NH1 ARG A 108 10.052 6.240 -0.618 1.00 19.05 N ANISOU 867 NH1 ARG A 108 1888 2613 2735 196 46 274 N ATOM 868 NH2 ARG A 108 10.729 4.105 -0.935 1.00 23.19 N ANISOU 868 NH2 ARG A 108 2291 2934 3583 -12 -208 -348 N ATOM 869 N GLU A 109 14.226 3.374 3.271 1.00 11.86 N ANISOU 869 N GLU A 109 1078 1796 1631 -248 275 -292 N ATOM 870 CA GLU A 109 15.129 2.263 3.026 1.00 13.93 C ANISOU 870 CA GLU A 109 1521 2171 1599 49 111 -216 C ATOM 871 C GLU A 109 14.371 1.299 2.166 1.00 12.65 C ANISOU 871 C GLU A 109 1308 1886 1613 -82 249 -136 C ATOM 872 O GLU A 109 13.403 0.714 2.628 1.00 13.76 O ANISOU 872 O GLU A 109 1666 2065 1495 -243 254 -125 O ATOM 873 CB GLU A 109 15.547 1.550 4.352 1.00 16.55 C ANISOU 873 CB GLU A 109 1896 2456 1935 25 -39 -219 C ATOM 874 CG GLU A 109 16.306 2.423 5.316 1.00 20.86 C ANISOU 874 CG GLU A 109 2856 2683 2383 -27 -66 -190 C ATOM 875 CD GLU A 109 17.713 2.679 4.857 1.00 29.23 C ANISOU 875 CD GLU A 109 3624 4138 3342 -189 205 -494 C ATOM 876 OE1 GLU A 109 18.459 3.421 5.546 1.00 36.45 O ANISOU 876 OE1 GLU A 109 5208 4430 4210 -452 -475 -732 O ATOM 877 OE2 GLU A 109 18.119 2.162 3.780 1.00 38.20 O ANISOU 877 OE2 GLU A 109 5393 4965 4157 127 518 -620 O ATOM 878 N ASP A 110 14.833 1.094 0.951 1.00 12.32 N ANISOU 878 N ASP A 110 1368 1785 1526 8 137 -75 N ATOM 879 CA ASP A 110 14.086 0.303 -0.012 1.00 12.46 C ANISOU 879 CA ASP A 110 1423 1829 1480 -112 329 -15 C ATOM 880 C ASP A 110 12.687 0.847 -0.071 1.00 11.09 C ANISOU 880 C ASP A 110 875 2020 1315 -261 155 -184 C ATOM 881 O ASP A 110 12.529 2.074 -0.188 1.00 12.12 O ANISOU 881 O ASP A 110 1205 1735 1663 -213 245 -89 O ATOM 882 CB ASP A 110 14.189 -1.181 0.259 1.00 14.71 C ANISOU 882 CB ASP A 110 1892 1952 1743 -81 421 -185 C ATOM 883 CG ASP A 110 15.589 -1.670 0.222 1.00 18.80 C ANISOU 883 CG ASP A 110 2405 2296 2442 346 607 147 C ATOM 884 OD1 ASP A 110 16.391 -1.275 -0.698 1.00 22.73 O ANISOU 884 OD1 ASP A 110 2838 3012 2784 452 770 -102 O ATOM 885 OD2 ASP A 110 15.966 -2.508 1.071 1.00 28.92 O ANISOU 885 OD2 ASP A 110 4105 3290 3591 759 188 949 O ATOM 886 N ASP A 111 11.631 0.040 -0.046 1.00 12.48 N ANISOU 886 N ASP A 111 1040 2119 1582 -274 70 -382 N ATOM 887 CA ASP A 111 10.289 0.519 -0.118 1.00 12.92 C ANISOU 887 CA ASP A 111 1033 2288 1585 -486 51 -162 C ATOM 888 C ASP A 111 9.694 0.862 1.257 1.00 12.35 C ANISOU 888 C ASP A 111 740 2105 1845 -9 -77 -361 C ATOM 889 O ASP A 111 8.548 1.190 1.313 1.00 15.37 O ANISOU 889 O ASP A 111 1086 2743 2007 37 -134 -697 O ATOM 890 CB ASP A 111 9.417 -0.495 -0.832 1.00 13.05 C ANISOU 890 CB ASP A 111 802 2339 1815 -438 67 -192 C ATOM 891 CG ASP A 111 9.706 -0.567 -2.317 1.00 15.36 C ANISOU 891 CG ASP A 111 1409 2636 1789 -348 38 -397 C ATOM 892 OD1 ASP A 111 9.881 0.503 -2.923 1.00 18.20 O ANISOU 892 OD1 ASP A 111 2595 2519 1798 -509 158 -124 O ATOM 893 OD2 ASP A 111 9.737 -1.666 -2.847 1.00 19.77 O ANISOU 893 OD2 ASP A 111 3305 2418 1789 -310 261 -548 O ATOM 894 N LYS A 112 10.565 0.857 2.276 1.00 12.84 N ANISOU 894 N LYS A 112 1370 1771 1736 -175 181 -107 N ATOM 895 CA LYS A 112 10.068 1.086 3.652 1.00 12.91 C ANISOU 895 CA LYS A 112 1671 1768 1467 -94 333 -85 C ATOM 896 C LYS A 112 10.429 2.464 4.129 1.00 10.92 C ANISOU 896 C LYS A 112 1010 1637 1502 -248 59 -76 C ATOM 897 O LYS A 112 11.301 3.132 3.606 1.00 11.69 O ANISOU 897 O LYS A 112 1054 1788 1597 -383 225 -93 O ATOM 898 CB LYS A 112 10.717 0.062 4.565 1.00 13.84 C ANISOU 898 CB LYS A 112 1894 1718 1644 35 465 -135 C ATOM 899 CG LYS A 112 10.417 -1.372 4.203 1.00 18.80 C ANISOU 899 CG LYS A 112 2731 1991 2421 12 444 -163 C ATOM 900 CD LYS A 112 11.351 -2.242 4.970 1.00 27.62 C ANISOU 900 CD LYS A 112 3951 3074 3468 358 261 -173 C ATOM 901 CE LYS A 112 12.666 -2.631 4.162 1.00 32.68 C ANISOU 901 CE LYS A 112 4076 3910 4427 33 362 83 C ATOM 902 NZ LYS A 112 13.811 -1.627 4.287 1.00 30.04 N ANISOU 902 NZ LYS A 112 3916 3351 4145 -15 729 900 N ATOM 903 N ALEU A 113 9.757 2.891 5.181 0.50 10.47 N ANISOU 903 N ALEU A 113 1113 1448 1416 -173 97 -59 N ATOM 904 N BLEU A 113 9.754 2.817 5.201 0.50 10.87 N ANISOU 904 N BLEU A 113 1178 1536 1416 -213 141 -120 N ATOM 905 CA ALEU A 113 10.118 4.086 5.927 0.50 10.69 C ANISOU 905 CA ALEU A 113 1189 1509 1365 -76 20 -49 C ATOM 906 CA BLEU A 113 10.073 3.953 6.006 0.50 10.91 C ANISOU 906 CA BLEU A 113 1190 1548 1405 -232 172 -27 C ATOM 907 C ALEU A 113 10.450 3.614 7.328 0.50 9.61 C ANISOU 907 C ALEU A 113 895 1373 1382 94 104 -91 C ATOM 908 C BLEU A 113 10.510 3.416 7.346 0.50 10.22 C ANISOU 908 C BLEU A 113 1034 1455 1395 -79 182 -115 C ATOM 909 O ALEU A 113 9.579 3.127 8.041 0.50 10.25 O ANISOU 909 O ALEU A 113 1295 1177 1420 99 135 -104 O ATOM 910 O BLEU A 113 9.849 2.639 8.003 0.50 9.57 O ANISOU 910 O BLEU A 113 887 1237 1510 -29 232 61 O ATOM 911 CB ALEU A 113 8.955 5.060 5.893 0.50 12.03 C ANISOU 911 CB ALEU A 113 1537 1628 1406 -253 27 31 C ATOM 912 CB BLEU A 113 8.873 4.853 6.090 0.50 12.75 C ANISOU 912 CB BLEU A 113 1674 1664 1506 -313 124 -77 C ATOM 913 CG ALEU A 113 9.237 6.440 6.497 0.50 11.72 C ANISOU 913 CG ALEU A 113 694 1905 1851 174 -75 -92 C ATOM 914 CG BLEU A 113 9.203 6.109 6.873 0.50 14.35 C ANISOU 914 CG BLEU A 113 1677 1974 1798 -376 -69 -113 C ATOM 915 CD1ALEU A 113 8.100 7.289 6.099 0.50 12.51 C ANISOU 915 CD1ALEU A 113 1263 1856 1634 -6 -133 -184 C ATOM 916 CD1BLEU A 113 10.325 6.958 6.167 0.50 15.52 C ANISOU 916 CD1BLEU A 113 1376 1975 2545 -421 220 -236 C ATOM 917 CD2ALEU A 113 9.281 6.442 7.985 0.50 15.21 C ANISOU 917 CD2ALEU A 113 1635 2211 1931 248 210 121 C ATOM 918 CD2BLEU A 113 7.972 6.913 6.981 0.50 17.73 C ANISOU 918 CD2BLEU A 113 1831 2503 2402 -109 -145 -386 C ATOM 919 N VAL A 114 11.731 3.737 7.702 1.00 10.68 N ANISOU 919 N VAL A 114 1258 1458 1343 -94 13 37 N ATOM 920 CA VAL A 114 12.274 3.257 8.958 1.00 12.21 C ANISOU 920 CA VAL A 114 1693 1462 1481 -139 9 91 C ATOM 921 C VAL A 114 12.392 4.423 9.921 1.00 12.42 C ANISOU 921 C VAL A 114 1771 1592 1355 -416 -114 134 C ATOM 922 O VAL A 114 12.837 5.507 9.584 1.00 12.56 O ANISOU 922 O VAL A 114 1794 1548 1428 -462 70 -9 O ATOM 923 CB VAL A 114 13.634 2.646 8.728 1.00 14.16 C ANISOU 923 CB VAL A 114 1968 1763 1650 -210 113 233 C ATOM 924 CG1 VAL A 114 14.245 2.163 10.029 1.00 15.54 C ANISOU 924 CG1 VAL A 114 1325 2410 2166 -64 -100 189 C ATOM 925 CG2 VAL A 114 13.508 1.473 7.676 1.00 17.04 C ANISOU 925 CG2 VAL A 114 2469 1985 2017 59 153 -145 C ATOM 926 N VAL A 115 11.877 4.200 11.111 1.00 12.62 N ANISOU 926 N VAL A 115 1983 1421 1388 -448 -151 64 N ATOM 927 CA VAL A 115 11.820 5.173 12.181 1.00 12.33 C ANISOU 927 CA VAL A 115 1903 1352 1427 -393 -150 62 C ATOM 928 C VAL A 115 12.719 4.692 13.314 1.00 12.17 C ANISOU 928 C VAL A 115 1875 1417 1331 -240 -185 195 C ATOM 929 O VAL A 115 12.486 3.637 13.874 1.00 16.01 O ANISOU 929 O VAL A 115 2527 1767 1787 -581 -583 373 O ATOM 930 CB VAL A 115 10.398 5.426 12.648 1.00 13.33 C ANISOU 930 CB VAL A 115 1952 1549 1562 -321 14 71 C ATOM 931 CG1 VAL A 115 10.403 6.533 13.683 1.00 16.13 C ANISOU 931 CG1 VAL A 115 2316 1989 1822 -106 127 -2 C ATOM 932 CG2 VAL A 115 9.462 5.738 11.457 1.00 16.62 C ANISOU 932 CG2 VAL A 115 2221 1972 2119 -573 -413 306 C ATOM 933 N AGLU A 116 13.694 5.489 13.706 0.50 11.10 N ANISOU 933 N AGLU A 116 1552 1282 1383 -104 -129 67 N ATOM 934 N BGLU A 116 13.711 5.468 13.694 0.50 11.53 N ANISOU 934 N BGLU A 116 1644 1315 1422 -141 -100 79 N ATOM 935 CA AGLU A 116 14.631 5.181 14.789 0.50 10.94 C ANISOU 935 CA AGLU A 116 1333 1207 1616 44 -128 100 C ATOM 936 CA BGLU A 116 14.556 5.122 14.829 0.50 11.78 C ANISOU 936 CA BGLU A 116 1511 1327 1636 -22 -1 120 C ATOM 937 C AGLU A 116 14.363 6.188 15.873 0.50 11.62 C ANISOU 937 C AGLU A 116 1674 1248 1490 -2 -273 -27 C ATOM 938 C BGLU A 116 14.374 6.172 15.875 0.50 12.10 C ANISOU 938 C BGLU A 116 1760 1298 1539 -57 -225 0 C ATOM 939 O AGLU A 116 14.526 7.385 15.661 0.50 12.60 O ANISOU 939 O AGLU A 116 2066 1163 1557 -32 -219 81 O ATOM 940 O BGLU A 116 14.569 7.364 15.639 0.50 12.86 O ANISOU 940 O BGLU A 116 2105 1172 1609 -65 -220 84 O ATOM 941 CB AGLU A 116 16.073 5.323 14.275 0.50 11.90 C ANISOU 941 CB AGLU A 116 1252 1265 2002 289 -186 20 C ATOM 942 CB BGLU A 116 16.014 4.942 14.426 0.50 13.59 C ANISOU 942 CB BGLU A 116 1581 1518 2065 5 -61 208 C ATOM 943 CG AGLU A 116 17.178 4.865 15.242 0.50 15.38 C ANISOU 943 CG AGLU A 116 1445 2293 2104 80 -163 309 C ATOM 944 CG BGLU A 116 16.201 3.797 13.420 0.50 17.46 C ANISOU 944 CG BGLU A 116 1717 2380 2536 153 297 96 C ATOM 945 CD AGLU A 116 18.563 5.535 15.013 0.50 22.37 C ANISOU 945 CD AGLU A 116 2309 3037 3151 -300 -325 462 C ATOM 946 CD BGLU A 116 17.498 3.017 13.527 0.50 26.37 C ANISOU 946 CD BGLU A 116 1960 3890 4167 0 29 90 C ATOM 947 OE1AGLU A 116 18.689 6.794 14.951 0.50 24.62 O ANISOU 947 OE1AGLU A 116 2486 3374 3494 -729 -9 1034 O ATOM 948 OE1BGLU A 116 18.495 3.600 14.031 0.50 29.72 O ANISOU 948 OE1BGLU A 116 469 5858 4965 472 -112 582 O ATOM 949 OE2AGLU A 116 19.555 4.794 14.952 0.50 25.52 O ANISOU 949 OE2AGLU A 116 3078 3264 3353 97 -117 804 O ATOM 950 OE2BGLU A 116 17.557 1.814 13.057 0.50 30.21 O ANISOU 950 OE2BGLU A 116 2701 4170 4606 -426 630 55 O ATOM 951 N CYS A 117 14.010 5.709 17.055 1.00 11.47 N ANISOU 951 N CYS A 117 1522 1348 1488 33 -207 43 N ATOM 952 CA CYS A 117 13.767 6.558 18.203 1.00 11.94 C ANISOU 952 CA CYS A 117 1468 1486 1581 184 -232 96 C ATOM 953 C CYS A 117 14.847 6.303 19.223 1.00 11.83 C ANISOU 953 C CYS A 117 1480 1405 1610 147 -248 28 C ATOM 954 O CYS A 117 15.068 5.181 19.617 1.00 12.55 O ANISOU 954 O CYS A 117 1786 1205 1774 -10 -526 175 O ATOM 955 CB CYS A 117 12.398 6.142 18.823 1.00 14.99 C ANISOU 955 CB CYS A 117 1639 2391 1663 627 -230 -56 C ATOM 956 SG CYS A 117 11.036 6.149 17.675 1.00 21.00 S ANISOU 956 SG CYS A 117 1681 4207 2089 191 -367 322 S ATOM 957 N VAL A 118 15.514 7.368 19.669 1.00 10.49 N ANISOU 957 N VAL A 118 833 1321 1829 155 -184 48 N ATOM 958 CA VAL A 118 16.676 7.250 20.512 1.00 11.60 C ANISOU 958 CA VAL A 118 700 1597 2109 164 -299 -73 C ATOM 959 C VAL A 118 16.502 8.113 21.769 1.00 11.82 C ANISOU 959 C VAL A 118 1055 1330 2106 172 -316 -39 C ATOM 960 O VAL A 118 16.192 9.318 21.691 1.00 13.25 O ANISOU 960 O VAL A 118 1857 1277 1898 198 -449 -50 O ATOM 961 CB VAL A 118 18.003 7.701 19.842 1.00 14.63 C ANISOU 961 CB VAL A 118 691 2024 2841 286 -111 -106 C ATOM 962 CG1 VAL A 118 19.151 7.748 20.754 1.00 19.95 C ANISOU 962 CG1 VAL A 118 570 3028 3983 148 -113 -112 C ATOM 963 CG2 VAL A 118 18.340 6.822 18.660 1.00 19.64 C ANISOU 963 CG2 VAL A 118 2369 2205 2888 1 525 -69 C ATOM 964 N MET A 119 16.714 7.512 22.917 1.00 13.52 N ANISOU 964 N MET A 119 1781 1424 1932 296 -607 -8 N ATOM 965 CA MET A 119 16.767 8.246 24.176 1.00 14.78 C ANISOU 965 CA MET A 119 1935 1674 2006 239 -560 67 C ATOM 966 C MET A 119 17.935 7.655 24.915 1.00 16.45 C ANISOU 966 C MET A 119 2073 1936 2238 52 -686 -9 C ATOM 967 O MET A 119 17.945 6.498 25.298 1.00 15.28 O ANISOU 967 O MET A 119 1973 1799 2033 228 -736 -67 O ATOM 968 CB MET A 119 15.472 7.991 24.924 1.00 16.51 C ANISOU 968 CB MET A 119 2139 2151 1980 668 -580 -40 C ATOM 969 CG MET A 119 15.285 8.483 26.386 1.00 20.94 C ANISOU 969 CG MET A 119 3003 2468 2483 332 -614 -82 C ATOM 970 SD MET A 119 14.992 10.172 26.332 1.00 26.57 S ANISOU 970 SD MET A 119 4648 2439 3006 1038 -1528 -485 S ATOM 971 CE MET A 119 15.037 10.809 27.961 1.00 20.96 C ANISOU 971 CE MET A 119 3026 2201 2735 -341 -438 -343 C ATOM 972 N ALYS A 120 18.970 8.457 25.165 0.50 19.92 N ANISOU 972 N ALYS A 120 2310 2420 2837 76 -470 31 N ATOM 973 N BLYS A 120 18.926 8.530 25.036 0.50 16.73 N ANISOU 973 N BLYS A 120 1712 2100 2542 125 -478 33 N ATOM 974 CA ALYS A 120 20.250 7.991 25.779 0.50 22.21 C ANISOU 974 CA ALYS A 120 2535 2824 3079 4 -345 12 C ATOM 975 CA BLYS A 120 20.167 8.198 25.627 0.50 16.79 C ANISOU 975 CA BLYS A 120 1729 2093 2557 2 -388 70 C ATOM 976 C ALYS A 120 20.561 6.475 25.846 0.50 20.95 C ANISOU 976 C ALYS A 120 2243 2730 2984 -68 -280 -27 C ATOM 977 C BLYS A 120 20.726 6.958 24.866 0.50 14.39 C ANISOU 977 C BLYS A 120 1330 1913 2224 56 -389 119 C ATOM 978 O ALYS A 120 20.331 5.797 26.863 0.50 22.60 O ANISOU 978 O ALYS A 120 2448 2952 3186 -103 -490 -183 O ATOM 979 O BLYS A 120 20.925 6.974 23.622 0.50 15.14 O ANISOU 979 O BLYS A 120 1263 1926 2561 295 -186 263 O ATOM 980 CB ALYS A 120 20.361 8.531 27.186 0.50 23.93 C ANISOU 980 CB ALYS A 120 2877 3006 3207 58 -338 4 C ATOM 981 CB BLYS A 120 19.905 7.948 27.138 0.50 16.10 C ANISOU 981 CB BLYS A 120 1830 1840 2443 7 -520 -9 C ATOM 982 CG ALYS A 120 19.188 8.193 28.068 0.50 25.66 C ANISOU 982 CG ALYS A 120 3127 3352 3267 171 -307 110 C ATOM 983 CG BLYS A 120 19.462 9.250 27.890 0.50 18.68 C ANISOU 983 CG BLYS A 120 2198 2154 2744 39 -467 -227 C ATOM 984 CD ALYS A 120 18.845 9.438 28.880 0.50 29.59 C ANISOU 984 CD ALYS A 120 3819 3581 3842 164 -68 -34 C ATOM 985 CD BLYS A 120 18.762 8.915 29.194 0.50 25.58 C ANISOU 985 CD BLYS A 120 3342 3206 3170 227 -177 -194 C ATOM 986 CE ALYS A 120 19.051 9.267 30.374 0.50 32.57 C ANISOU 986 CE ALYS A 120 4159 4085 4129 136 -137 33 C ATOM 987 CE BLYS A 120 19.720 8.824 30.362 0.50 29.71 C ANISOU 987 CE BLYS A 120 3665 3870 3753 126 -251 -66 C ATOM 988 NZ ALYS A 120 17.933 8.492 30.996 0.50 33.98 N ANISOU 988 NZ ALYS A 120 4030 4302 4578 -36 -80 -89 N ATOM 989 NZ BLYS A 120 18.898 8.779 31.608 0.50 32.07 N ANISOU 989 NZ BLYS A 120 4095 4363 3725 215 -134 14 N ATOM 990 N AGLY A 121 21.176 5.986 24.772 0.50 19.50 N ANISOU 990 N AGLY A 121 1954 2604 2849 -168 -242 -11 N ATOM 991 N BGLY A 121 21.041 5.868 25.574 0.50 13.81 N ANISOU 991 N BGLY A 121 1302 1865 2077 -132 -278 162 N ATOM 992 CA AGLY A 121 21.637 4.620 24.654 0.50 17.20 C ANISOU 992 CA AGLY A 121 1129 2636 2766 -154 -82 63 C ATOM 993 CA BGLY A 121 21.599 4.746 24.875 0.50 14.28 C ANISOU 993 CA BGLY A 121 735 2282 2406 -103 -189 168 C ATOM 994 C AGLY A 121 20.554 3.658 24.271 0.50 13.81 C ANISOU 994 C AGLY A 121 282 2431 2532 -217 -140 118 C ATOM 995 C BGLY A 121 20.599 3.739 24.362 0.50 12.39 C ANISOU 995 C BGLY A 121 303 2201 2204 -185 -267 175 C ATOM 996 O AGLY A 121 20.845 2.562 23.783 0.50 15.22 O ANISOU 996 O AGLY A 121 494 2449 2840 -352 131 225 O ATOM 997 O BGLY A 121 21.074 2.708 23.870 0.50 15.41 O ANISOU 997 O BGLY A 121 1411 2101 2342 361 -257 433 O ATOM 998 N VAL A 122 19.316 4.025 24.448 1.00 11.93 N ANISOU 998 N VAL A 122 616 1828 2089 -2 -164 248 N ATOM 999 CA VAL A 122 18.242 3.127 24.080 1.00 11.40 C ANISOU 999 CA VAL A 122 262 1919 2151 54 -59 193 C ATOM 1000 C VAL A 122 17.625 3.553 22.747 1.00 12.05 C ANISOU 1000 C VAL A 122 1070 1654 1852 157 -214 174 C ATOM 1001 O VAL A 122 17.182 4.705 22.606 1.00 14.53 O ANISOU 1001 O VAL A 122 2088 1362 2068 419 -674 26 O ATOM 1002 CB VAL A 122 17.198 3.047 25.139 1.00 12.45 C ANISOU 1002 CB VAL A 122 265 2039 2425 137 -37 317 C ATOM 1003 CG1 VAL A 122 16.110 2.169 24.749 1.00 15.83 C ANISOU 1003 CG1 VAL A 122 311 3010 2693 311 278 368 C ATOM 1004 CG2 VAL A 122 17.747 2.584 26.510 1.00 14.40 C ANISOU 1004 CG2 VAL A 122 736 2517 2217 152 277 315 C ATOM 1005 N THR A 123 17.642 2.629 21.802 1.00 12.24 N ANISOU 1005 N THR A 123 1237 1406 2007 173 -317 164 N ATOM 1006 CA THR A 123 17.080 2.847 20.489 1.00 12.90 C ANISOU 1006 CA THR A 123 1448 1562 1889 158 -243 84 C ATOM 1007 C THR A 123 15.947 1.877 20.228 1.00 12.72 C ANISOU 1007 C THR A 123 1624 1291 1917 39 -458 101 C ATOM 1008 O THR A 123 16.048 0.686 20.515 1.00 16.22 O ANISOU 1008 O THR A 123 1894 1372 2896 56 -592 359 O ATOM 1009 CB THR A 123 18.107 2.621 19.439 1.00 15.62 C ANISOU 1009 CB THR A 123 1812 2052 2068 -154 -215 -39 C ATOM 1010 OG1 THR A 123 19.151 3.511 19.663 1.00 19.54 O ANISOU 1010 OG1 THR A 123 2097 2645 2682 -39 364 0 O ATOM 1011 CG2 THR A 123 17.541 2.872 18.022 1.00 16.59 C ANISOU 1011 CG2 THR A 123 717 3240 2343 83 225 243 C ATOM 1012 N SER A 124 14.941 2.360 19.592 1.00 12.35 N ANISOU 1012 N SER A 124 1639 1328 1725 -144 -492 153 N ATOM 1013 CA SER A 124 13.867 1.547 19.046 1.00 12.33 C ANISOU 1013 CA SER A 124 1450 1434 1800 -131 -282 299 C ATOM 1014 C SER A 124 13.762 1.762 17.584 1.00 10.63 C ANISOU 1014 C SER A 124 958 1429 1651 34 -165 204 C ATOM 1015 O SER A 124 13.883 2.868 17.111 1.00 13.98 O ANISOU 1015 O SER A 124 2286 1353 1674 -147 -235 178 O ATOM 1016 CB SER A 124 12.536 1.843 19.736 1.00 12.48 C ANISOU 1016 CB SER A 124 1084 1755 1904 -265 -306 247 C ATOM 1017 OG SER A 124 11.443 1.205 19.106 1.00 14.29 O ANISOU 1017 OG SER A 124 1371 2072 1986 -158 -118 90 O ATOM 1018 N THR A 125 13.559 0.694 16.818 1.00 11.85 N ANISOU 1018 N THR A 125 1576 1275 1650 -96 -205 199 N ATOM 1019 CA THR A 125 13.367 0.741 15.381 1.00 12.27 C ANISOU 1019 CA THR A 125 1417 1512 1733 -30 -43 234 C ATOM 1020 C THR A 125 11.994 0.278 15.021 1.00 11.43 C ANISOU 1020 C THR A 125 1159 1571 1609 -313 -160 138 C ATOM 1021 O THR A 125 11.630 -0.831 15.382 1.00 13.97 O ANISOU 1021 O THR A 125 1861 1536 1911 -426 -295 310 O ATOM 1022 CB THR A 125 14.453 -0.112 14.670 1.00 15.13 C ANISOU 1022 CB THR A 125 1669 1936 2144 280 -46 -83 C ATOM 1023 OG1 THR A 125 15.756 0.389 15.015 1.00 19.97 O ANISOU 1023 OG1 THR A 125 1705 2783 3097 477 -67 -255 O ATOM 1024 CG2 THR A 125 14.326 -0.039 13.174 1.00 18.38 C ANISOU 1024 CG2 THR A 125 2166 2661 2157 321 342 -195 C ATOM 1025 N ARG A 126 11.277 1.112 14.295 1.00 12.09 N ANISOU 1025 N ARG A 126 1567 1479 1546 -344 -169 214 N ATOM 1026 CA ARG A 126 9.935 0.853 13.824 1.00 12.19 C ANISOU 1026 CA ARG A 126 1424 1667 1539 -425 -221 270 C ATOM 1027 C ARG A 126 9.949 0.920 12.313 1.00 12.79 C ANISOU 1027 C ARG A 126 1514 1783 1562 -401 -125 290 C ATOM 1028 O ARG A 126 10.500 1.846 11.732 1.00 16.21 O ANISOU 1028 O ARG A 126 2412 2185 1561 -962 -215 230 O ATOM 1029 CB ARG A 126 8.982 1.838 14.447 1.00 13.62 C ANISOU 1029 CB ARG A 126 1529 2056 1589 -343 -48 132 C ATOM 1030 CG ARG A 126 8.829 1.494 15.966 1.00 19.67 C ANISOU 1030 CG ARG A 126 2503 2844 2125 85 125 15 C ATOM 1031 CD ARG A 126 8.154 2.440 16.796 1.00 21.93 C ANISOU 1031 CD ARG A 126 2449 3553 2329 -62 25 -89 C ATOM 1032 NE ARG A 126 6.743 2.668 16.604 1.00 22.77 N ANISOU 1032 NE ARG A 126 2228 3929 2492 -34 83 -166 N ATOM 1033 CZ ARG A 126 5.717 2.037 17.193 1.00 22.62 C ANISOU 1033 CZ ARG A 126 2683 3926 1986 -456 83 -124 C ATOM 1034 NH1 ARG A 126 5.847 0.849 17.766 1.00 23.88 N ANISOU 1034 NH1 ARG A 126 2760 4217 2093 -94 -411 -234 N ATOM 1035 NH2 ARG A 126 4.517 2.489 17.006 1.00 26.51 N ANISOU 1035 NH2 ARG A 126 3323 3769 2978 -200 195 45 N ATOM 1036 N VAL A 127 9.295 -0.022 11.655 1.00 11.28 N ANISOU 1036 N VAL A 127 1363 1492 1431 -254 -17 97 N ATOM 1037 CA VAL A 127 9.357 -0.096 10.208 1.00 11.79 C ANISOU 1037 CA VAL A 127 1347 1563 1568 21 10 78 C ATOM 1038 C VAL A 127 7.930 -0.011 9.700 1.00 10.45 C ANISOU 1038 C VAL A 127 1162 1410 1398 38 -49 -30 C ATOM 1039 O VAL A 127 7.067 -0.732 10.161 1.00 11.23 O ANISOU 1039 O VAL A 127 1196 1524 1545 -217 63 112 O ATOM 1040 CB VAL A 127 10.034 -1.416 9.716 1.00 12.32 C ANISOU 1040 CB VAL A 127 688 2013 1980 84 0 77 C ATOM 1041 CG1 VAL A 127 10.021 -1.520 8.194 1.00 15.65 C ANISOU 1041 CG1 VAL A 127 1807 2364 1773 343 38 -215 C ATOM 1042 CG2 VAL A 127 11.336 -1.564 10.312 1.00 14.84 C ANISOU 1042 CG2 VAL A 127 545 2523 2567 264 158 -71 C ATOM 1043 N TYR A 128 7.742 0.907 8.750 1.00 10.67 N ANISOU 1043 N TYR A 128 1157 1406 1491 -168 30 -33 N ATOM 1044 CA TYR A 128 6.494 1.141 8.046 1.00 10.56 C ANISOU 1044 CA TYR A 128 1157 1471 1381 -64 -70 9 C ATOM 1045 C TYR A 128 6.611 0.759 6.599 1.00 11.62 C ANISOU 1045 C TYR A 128 1234 1539 1640 -117 -46 10 C ATOM 1046 O TYR A 128 7.662 0.956 5.974 1.00 11.81 O ANISOU 1046 O TYR A 128 1389 1603 1494 -227 12 -128 O ATOM 1047 CB TYR A 128 6.107 2.578 8.150 1.00 10.50 C ANISOU 1047 CB TYR A 128 969 1617 1400 -107 -42 20 C ATOM 1048 CG TYR A 128 5.723 3.095 9.520 1.00 10.59 C ANISOU 1048 CG TYR A 128 914 1345 1764 -221 -181 94 C ATOM 1049 CD1 TYR A 128 6.709 3.349 10.473 1.00 12.29 C ANISOU 1049 CD1 TYR A 128 1177 1605 1885 -88 -49 -57 C ATOM 1050 CD2 TYR A 128 4.406 3.337 9.854 1.00 11.60 C ANISOU 1050 CD2 TYR A 128 937 1699 1768 -222 -89 132 C ATOM 1051 CE1 TYR A 128 6.319 3.866 11.753 1.00 14.17 C ANISOU 1051 CE1 TYR A 128 1543 2028 1811 -24 -44 -170 C ATOM 1052 CE2 TYR A 128 4.050 3.833 11.088 1.00 13.54 C ANISOU 1052 CE2 TYR A 128 1386 1902 1856 -250 183 -16 C ATOM 1053 CZ TYR A 128 4.999 4.085 12.020 1.00 14.33 C ANISOU 1053 CZ TYR A 128 1657 2108 1679 -138 360 -76 C ATOM 1054 OH TYR A 128 4.592 4.575 13.257 1.00 19.12 O ANISOU 1054 OH TYR A 128 2968 2596 1697 285 251 -280 O ATOM 1055 N GLU A 129 5.497 0.257 6.061 1.00 11.89 N ANISOU 1055 N GLU A 129 1283 1638 1594 -166 -92 -202 N ATOM 1056 CA GLU A 129 5.388 -0.031 4.655 1.00 13.72 C ANISOU 1056 CA GLU A 129 1692 1769 1752 84 -187 -190 C ATOM 1057 C GLU A 129 4.268 0.790 4.079 1.00 12.49 C ANISOU 1057 C GLU A 129 1593 1642 1508 -136 -192 -321 C ATOM 1058 O GLU A 129 3.424 1.270 4.778 1.00 12.66 O ANISOU 1058 O GLU A 129 1620 1555 1634 -14 -88 -61 O ATOM 1059 CB GLU A 129 5.154 -1.522 4.409 1.00 16.55 C ANISOU 1059 CB GLU A 129 2211 1924 2151 305 -318 -196 C ATOM 1060 CG GLU A 129 6.421 -2.283 4.822 1.00 25.12 C ANISOU 1060 CG GLU A 129 3309 3015 3220 587 -346 -176 C ATOM 1061 CD GLU A 129 6.624 -3.668 4.239 1.00 34.16 C ANISOU 1061 CD GLU A 129 4754 3747 4475 624 -560 -627 C ATOM 1062 OE1 GLU A 129 5.643 -4.235 3.676 1.00 40.20 O ANISOU 1062 OE1 GLU A 129 5656 4025 5593 -83 -809 -797 O ATOM 1063 OE2 GLU A 129 7.792 -4.170 4.371 1.00 38.86 O ANISOU 1063 OE2 GLU A 129 5427 3945 5392 1193 -762 -674 O ATOM 1064 N ARG A 130 4.238 0.921 2.768 1.00 13.79 N ANISOU 1064 N ARG A 130 1773 1837 1627 7 -165 -323 N ATOM 1065 CA ARG A 130 3.142 1.663 2.122 1.00 14.33 C ANISOU 1065 CA ARG A 130 1808 1949 1688 -8 -195 -208 C ATOM 1066 C ARG A 130 1.839 0.994 2.360 1.00 15.76 C ANISOU 1066 C ARG A 130 1746 2118 2124 -229 -441 -460 C ATOM 1067 O ARG A 130 1.734 -0.233 2.219 1.00 17.42 O ANISOU 1067 O ARG A 130 1533 2198 2887 36 -790 -561 O ATOM 1068 CB ARG A 130 3.367 1.714 0.647 1.00 17.61 C ANISOU 1068 CB ARG A 130 2352 2450 1887 74 -370 -27 C ATOM 1069 CG ARG A 130 4.496 2.465 0.244 1.00 18.18 C ANISOU 1069 CG ARG A 130 2268 2678 1962 290 -216 192 C ATOM 1070 CD ARG A 130 4.230 3.873 0.081 1.00 22.01 C ANISOU 1070 CD ARG A 130 2081 2704 3578 -122 -285 80 C ATOM 1071 NE ARG A 130 5.377 4.589 -0.463 1.00 20.88 N ANISOU 1071 NE ARG A 130 2273 2182 3475 -81 -199 136 N ATOM 1072 CZ ARG A 130 5.439 5.910 -0.601 1.00 16.20 C ANISOU 1072 CZ ARG A 130 1368 2201 2586 -277 -388 252 C ATOM 1073 NH1 ARG A 130 4.415 6.636 -0.377 1.00 18.64 N ANISOU 1073 NH1 ARG A 130 2096 2655 2329 239 -292 95 N ATOM 1074 NH2 ARG A 130 6.595 6.443 -0.961 1.00 19.51 N ANISOU 1074 NH2 ARG A 130 1941 2883 2587 4 153 166 N ATOM 1075 N ALA A 131 0.865 1.774 2.708 1.00 17.30 N ANISOU 1075 N ALA A 131 1799 2204 2569 -336 -471 -382 N ATOM 1076 CA ALA A 131 -0.447 1.201 2.989 1.00 21.39 C ANISOU 1076 CA ALA A 131 2024 2754 3346 -383 -440 -103 C ATOM 1077 C ALA A 131 -1.132 0.691 1.707 1.00 24.33 C ANISOU 1077 C ALA A 131 2419 3067 3755 -527 -462 -69 C ATOM 1078 O ALA A 131 -0.707 1.097 0.603 1.00 27.60 O ANISOU 1078 O ALA A 131 2839 3765 3880 -534 -947 9 O ATOM 1079 CB ALA A 131 -1.269 2.194 3.760 1.00 23.65 C ANISOU 1079 CB ALA A 131 2259 2901 3824 -477 25 -198 C ATOM 1080 OXT ALA A 131 -2.046 -0.189 1.711 1.00 28.95 O ANISOU 1080 OXT ALA A 131 3224 3449 4325 -778 -455 47 O TER 1081 ALA A 131 HETATM 1082 O HOH A 132 4.795 28.336 0.125 1.00 34.67 O ANISOU 1082 O HOH A 132 2973 4917 5281 -720 265 1439 O HETATM 1083 O HOH A 133 16.168 21.669 32.708 1.00 47.11 O ANISOU 1083 O HOH A 133 8901 3980 5019 -2336 981 -1362 O HETATM 1084 O HOH A 134 8.309 7.699 18.964 1.00 43.74 O ANISOU 1084 O HOH A 134 2172 9002 5443 1010 -273 -454 O HETATM 1085 O HOH A 135 4.077 13.326 15.489 1.00 53.68 O ANISOU 1085 O HOH A 135 10002 3629 6764 -649 3272 17 O HETATM 1086 O HOH A 136 11.582 30.678 2.450 1.00 44.40 O ANISOU 1086 O HOH A 136 4435 7018 5415 -1451 -361 627 O HETATM 1087 O HOH A 137 9.011 -3.989 0.941 1.00 36.55 O ANISOU 1087 O HOH A 137 1838 5371 6678 -139 543 2310 O HETATM 1088 O HOH A 138 5.759 14.677 31.040 1.00 45.94 O ANISOU 1088 O HOH A 138 9591 4034 3828 1083 419 -258 O HETATM 1089 O HOH A 139 19.672 20.035 8.359 1.00126.19 O ANISOU 1089 O HOH A 139 12732 14821 20392 -7585 6939 -7171 O HETATM 1090 O HOH A 140 10.437 22.065 12.821 1.00 10.34 O ANISOU 1090 O HOH A 140 1122 1259 1546 97 107 99 O HETATM 1091 O HOH A 141 13.268 27.523 8.366 1.00 37.90 O ANISOU 1091 O HOH A 141 3711 5070 5619 167 1323 -1857 O HETATM 1092 O HOH A 142 18.844 17.898 14.852 1.00 39.29 O ANISOU 1092 O HOH A 142 2581 4173 8172 -529 -1097 1 O HETATM 1093 O HOH A 143 10.039 16.224 4.262 1.00 45.18 O ANISOU 1093 O HOH A 143 5836 6897 4433 2295 -884 -1106 O HETATM 1094 O HOH A 144 7.200 24.888 12.435 1.00 11.00 O ANISOU 1094 O HOH A 144 639 1811 1730 -123 0 -362 O HETATM 1095 O HOH A 145 3.237 -4.169 4.312 1.00 39.35 O ANISOU 1095 O HOH A 145 4794 4732 5425 -120 62 -601 O HETATM 1096 O HOH A 146 13.421 -7.454 20.030 1.00 42.40 O ANISOU 1096 O HOH A 146 3136 5934 7039 746 -1086 -400 O HETATM 1097 O HOH A 147 14.880 -5.527 22.437 0.50 24.55 O ANISOU 1097 O HOH A 147 4242 1884 3199 -8 -1430 73 O HETATM 1098 O HOH A 148 18.248 0.820 1.630 1.00 46.81 O ANISOU 1098 O HOH A 148 2345 9835 5604 800 534 1378 O HETATM 1099 O HOH A 149 3.313 21.342 24.105 1.00 42.14 O ANISOU 1099 O HOH A 149 7698 4666 3645 2468 1382 247 O HETATM 1100 O HOH A 150 3.838 5.298 16.427 1.00 45.29 O ANISOU 1100 O HOH A 150 4721 6896 5589 -1619 -1035 1738 O HETATM 1101 O HOH A 151 3.982 8.963 13.251 1.00 48.50 O ANISOU 1101 O HOH A 151 5909 7875 4642 -1856 2100 663 O HETATM 1102 O HOH A 152 5.328 -1.543 19.637 1.00 39.48 O ANISOU 1102 O HOH A 152 3125 6145 5728 -1052 1155 -1969 O HETATM 1103 O HOH A 153 -5.494 13.945 14.919 1.00 44.87 O ANISOU 1103 O HOH A 153 4199 3335 9511 1958 625 441 O HETATM 1104 O HOH A 154 2.271 -5.434 19.717 1.00 45.13 O ANISOU 1104 O HOH A 154 6690 5853 4603 1419 781 -1638 O HETATM 1105 O HOH A 155 6.868 -1.740 -3.655 1.00 50.14 O ANISOU 1105 O HOH A 155 3367 9914 5767 -727 -38 -1346 O HETATM 1106 O HOH A 156 10.870 -6.563 14.583 1.00 55.51 O ANISOU 1106 O HOH A 156 6044 6230 8817 3472 -1708 -3830 O HETATM 1107 O HOH A 157 0.350 -3.984 10.266 1.00 78.27 O ANISOU 1107 O HOH A 157 6393 11546 11798 -3343 2394 -566 O HETATM 1108 O HOH A 158 7.443 -6.283 15.510 1.00 28.33 O ANISOU 1108 O HOH A 158 4227 2713 3822 -1108 -1195 1075 O HETATM 1109 O HOH A 159 -7.187 9.577 19.664 1.00 32.85 O ANISOU 1109 O HOH A 159 2898 5744 3839 562 1352 316 O HETATM 1110 O HOH A 160 12.225 25.108 -14.809 1.00 34.78 O ANISOU 1110 O HOH A 160 3813 4039 5360 -1021 -1291 539 O HETATM 1111 O HOH A 161 -0.174 7.634 17.388 1.00 36.03 O ANISOU 1111 O HOH A 161 4202 5227 4258 1305 1725 1024 O HETATM 1112 O HOH A 162 12.527 -3.669 -1.861 1.00 27.13 O ANISOU 1112 O HOH A 162 4719 3066 2521 -888 306 -107 O HETATM 1113 O HOH A 163 0.997 20.248 5.153 1.00 15.57 O ANISOU 1113 O HOH A 163 1351 2388 2175 -241 -262 393 O HETATM 1114 O HOH A 164 13.759 26.668 15.418 1.00 13.56 O ANISOU 1114 O HOH A 164 1575 1494 2082 -342 -402 -121 O HETATM 1115 O HOH A 165 9.673 23.017 5.459 1.00 15.37 O ANISOU 1115 O HOH A 165 1282 2846 1710 316 -13 178 O HETATM 1116 O HOH A 166 16.183 18.691 14.170 1.00 20.71 O ANISOU 1116 O HOH A 166 2571 2845 2450 -121 -286 106 O HETATM 1117 O HOH A 167 -3.735 -0.636 22.106 1.00 14.07 O ANISOU 1117 O HOH A 167 1313 1782 2250 -297 -352 322 O HETATM 1118 O HOH A 168 11.785 12.324 12.111 1.00 13.40 O ANISOU 1118 O HOH A 168 1759 1693 1639 205 170 55 O HETATM 1119 O HOH A 169 1.762 12.848 14.281 1.00 23.67 O ANISOU 1119 O HOH A 169 2744 3480 2766 -103 459 1333 O HETATM 1120 O HOH A 170 15.475 8.911 3.223 1.00 19.86 O ANISOU 1120 O HOH A 170 2489 2192 2864 -636 822 0 O HETATM 1121 O HOH A 171 3.731 25.424 18.058 1.00 16.62 O ANISOU 1121 O HOH A 171 1397 2648 2267 781 -92 -461 O HETATM 1122 O HOH A 172 1.747 15.864 -0.123 1.00 22.89 O ANISOU 1122 O HOH A 172 4629 2292 1774 54 -958 -151 O HETATM 1123 O HOH A 173 4.056 27.190 2.550 1.00 18.26 O ANISOU 1123 O HOH A 173 1459 2456 3021 109 -216 -34 O HETATM 1124 O HOH A 174 13.280 21.532 19.910 1.00 19.99 O ANISOU 1124 O HOH A 174 1881 3455 2257 -859 -89 -13 O HETATM 1125 O HOH A 175 6.383 -0.339 1.278 1.00 21.27 O ANISOU 1125 O HOH A 175 1471 3367 3243 -193 332 -1037 O HETATM 1126 O HOH A 176 8.908 -3.083 19.991 1.00 18.65 O ANISOU 1126 O HOH A 176 2437 2352 2297 -35 -401 -182 O HETATM 1127 O HOH A 177 6.007 27.476 15.548 1.00 18.97 O ANISOU 1127 O HOH A 177 1904 1985 3320 49 -675 -173 O HETATM 1128 O HOH A 178 1.687 5.887 0.087 1.00 17.93 O ANISOU 1128 O HOH A 178 2028 2514 2268 -112 -165 -292 O HETATM 1129 O HOH A 179 -0.572 14.333 6.447 1.00 18.58 O ANISOU 1129 O HOH A 179 2243 2116 2699 -16 -146 75 O HETATM 1130 O HOH A 180 16.310 21.154 7.360 1.00 19.73 O ANISOU 1130 O HOH A 180 2818 1808 2871 -374 364 327 O HETATM 1131 O HOH A 181 2.684 6.692 13.453 1.00 25.25 O ANISOU 1131 O HOH A 181 2752 2907 3931 -76 562 276 O HETATM 1132 O HOH A 182 9.171 10.446 21.592 1.00 20.46 O ANISOU 1132 O HOH A 182 2678 2606 2489 -276 383 336 O HETATM 1133 O HOH A 183 7.117 27.732 11.909 1.00 17.89 O ANISOU 1133 O HOH A 183 1194 2607 2995 207 -370 -413 O HETATM 1134 O HOH A 184 17.804 -1.622 20.014 1.00 20.85 O ANISOU 1134 O HOH A 184 2117 2345 3458 -70 -834 -144 O HETATM 1135 O HOH A 185 6.361 9.252 -1.812 1.00 22.48 O ANISOU 1135 O HOH A 185 2734 2571 3236 -455 766 -426 O HETATM 1136 O HOH A 186 1.602 26.236 2.255 1.00 24.25 O ANISOU 1136 O HOH A 186 2002 2103 5105 -333 529 -440 O HETATM 1137 O HOH A 187 11.387 -2.789 0.739 1.00 20.92 O ANISOU 1137 O HOH A 187 3272 2013 2664 -477 86 -35 O HETATM 1138 O HOH A 188 15.953 -3.031 -2.876 1.00 27.96 O ANISOU 1138 O HOH A 188 5673 2808 2139 542 -51 199 O HETATM 1139 O HOH A 189 11.609 -5.788 20.936 1.00 26.21 O ANISOU 1139 O HOH A 189 4031 1610 4318 -240 216 770 O HETATM 1140 O HOH A 190 2.935 0.891 18.637 1.00 22.21 O ANISOU 1140 O HOH A 190 1792 4330 2315 -746 209 -32 O HETATM 1141 O HOH A 191 11.513 -3.079 13.603 1.00 24.17 O ANISOU 1141 O HOH A 191 4045 2292 2847 -112 85 -146 O HETATM 1142 O HOH A 192 -2.004 15.869 17.786 1.00 28.71 O ANISOU 1142 O HOH A 192 5722 2585 2600 -859 1172 -607 O HETATM 1143 O HOH A 193 2.760 14.020 18.164 1.00 30.13 O ANISOU 1143 O HOH A 193 3834 3335 4276 -601 -287 662 O HETATM 1144 O HOH A 194 4.964 29.088 4.408 1.00 30.78 O ANISOU 1144 O HOH A 194 2907 3268 5518 -585 -735 -1111 O HETATM 1145 O HOH A 195 8.708 -3.492 22.823 1.00 32.20 O ANISOU 1145 O HOH A 195 6644 2518 3070 -1230 1176 -487 O HETATM 1146 O HOH A 196 14.744 1.443 29.153 1.00 24.88 O ANISOU 1146 O HOH A 196 2661 4043 2746 1052 -605 265 O HETATM 1147 O HOH A 197 20.530 4.893 28.321 0.50 17.76 O ANISOU 1147 O HOH A 197 2218 2040 2490 300 -15 5 O HETATM 1148 O HOH A 198 17.603 13.243 27.860 1.00 26.96 O ANISOU 1148 O HOH A 198 2622 3903 3718 510 -773 1062 O HETATM 1149 O HOH A 199 2.191 -3.688 24.644 1.00 23.60 O ANISOU 1149 O HOH A 199 2309 3503 3155 847 -180 -514 O HETATM 1150 O HOH A 200 17.927 13.847 21.658 1.00 24.30 O ANISOU 1150 O HOH A 200 2169 4265 2796 -1015 -200 -258 O HETATM 1151 O HOH A 201 15.638 19.647 27.332 1.00 30.89 O ANISOU 1151 O HOH A 201 6278 2464 2994 -1282 -1576 -223 O HETATM 1152 O HOH A 202 8.769 4.913 32.734 1.00 31.27 O ANISOU 1152 O HOH A 202 4329 3656 3896 -500 -1992 311 O HETATM 1153 O HOH A 203 9.331 21.198 29.647 1.00 35.15 O ANISOU 1153 O HOH A 203 6194 3420 3739 1575 330 -759 O HETATM 1154 O HOH A 204 18.485 4.534 2.416 1.00 26.00 O ANISOU 1154 O HOH A 204 3171 4338 2367 -147 -323 -242 O HETATM 1155 O HOH A 205 0.443 5.078 32.157 1.00 26.11 O ANISOU 1155 O HOH A 205 4131 3233 2557 -38 125 -206 O HETATM 1156 O AHOH A 206 9.438 28.738 15.378 0.50 12.95 O ANISOU 1156 O AHOH A 206 979 1831 2109 -296 427 -42 O HETATM 1157 O BHOH A 206 9.043 28.761 16.837 0.50 22.39 O ANISOU 1157 O BHOH A 206 2087 1758 4662 -111 306 13 O HETATM 1158 O HOH A 207 -7.633 6.565 18.945 1.00 34.26 O ANISOU 1158 O HOH A 207 3601 4089 5324 851 1867 -59 O HETATM 1159 O HOH A 208 9.236 12.000 30.738 1.00 30.91 O ANISOU 1159 O HOH A 208 5507 2933 3304 354 1745 617 O HETATM 1160 O HOH A 209 6.671 5.673 14.928 1.00 30.31 O ANISOU 1160 O HOH A 209 1498 6273 3742 -609 18 -1171 O HETATM 1161 O HOH A 210 -0.705 18.669 3.818 1.00 23.04 O ANISOU 1161 O HOH A 210 3128 2543 3083 -235 -1541 123 O HETATM 1162 O HOH A 211 0.979 15.709 18.525 1.00 38.60 O ANISOU 1162 O HOH A 211 7117 4851 2696 -2233 1236 -533 O HETATM 1163 O HOH A 212 3.426 11.495 19.447 1.00 24.42 O ANISOU 1163 O HOH A 212 1981 3717 3579 -554 551 -107 O HETATM 1164 O HOH A 213 4.910 10.084 29.298 1.00 31.77 O ANISOU 1164 O HOH A 213 5621 3094 3354 677 519 1471 O HETATM 1165 O HOH A 214 -1.885 20.300 11.689 1.00 33.96 O ANISOU 1165 O HOH A 214 3343 3431 6126 -791 2870 7 O HETATM 1166 O HOH A 215 13.436 21.297 28.302 1.00 56.97 O ANISOU 1166 O HOH A 215 12023 4892 4732 -204 -648 1448 O HETATM 1167 O HOH A 216 12.019 -3.077 24.663 1.00 66.37 O ANISOU 1167 O HOH A 216 20247 1591 3377 -3269 -341 1085 O HETATM 1168 O HOH A 217 5.354 22.581 24.352 1.00 30.41 O ANISOU 1168 O HOH A 217 4373 3271 3909 945 1619 -106 O HETATM 1169 O HOH A 218 0.745 19.525 -1.762 1.00 54.24 O ANISOU 1169 O HOH A 218 7066 6244 7298 4071 -3020 -4534 O HETATM 1170 O HOH A 219 -7.202 2.564 23.459 1.00 24.69 O ANISOU 1170 O HOH A 219 3455 2434 3490 -432 429 -410 O HETATM 1171 O HOH A 220 18.536 11.354 24.264 1.00 87.96 O ANISOU 1171 O HOH A 220 9372 4778 19269 157 -2320 2893 O HETATM 1172 O HOH A 221 3.243 -2.292 1.083 1.00 34.84 O ANISOU 1172 O HOH A 221 2979 4068 6190 -292 432 -1692 O HETATM 1173 O HOH A 222 9.824 21.198 3.005 1.00 40.96 O ANISOU 1173 O HOH A 222 7751 4530 3281 603 685 -474 O HETATM 1174 O HOH A 223 -6.664 5.032 23.756 1.00 43.60 O ANISOU 1174 O HOH A 223 6770 5611 4184 -1835 435 -993 O HETATM 1175 O HOH A 224 11.336 24.946 4.402 1.00 36.30 O ANISOU 1175 O HOH A 224 3316 6228 4247 -860 232 1530 O HETATM 1176 O HOH A 225 -0.683 -5.053 17.525 1.00 32.67 O ANISOU 1176 O HOH A 225 3734 2946 5733 100 905 428 O HETATM 1177 O HOH A 226 20.729 4.608 17.613 1.00 50.20 O ANISOU 1177 O HOH A 226 5494 6534 7044 544 3845 -761 O HETATM 1178 O HOH A 227 -4.659 -2.380 24.090 1.00 12.15 O ANISOU 1178 O HOH A 227 1049 1737 1828 36 -32 300 O HETATM 1179 O HOH A 228 -0.357 -8.053 17.995 1.00 41.03 O ANISOU 1179 O HOH A 228 4136 3897 7556 -45 -2378 -2159 O HETATM 1180 O HOH A 229 0.252 3.599 -0.343 1.00 33.98 O ANISOU 1180 O HOH A 229 2959 3358 6593 84 -2267 -128 O HETATM 1181 O HOH A 230 3.058 8.167 31.031 1.00 33.92 O ANISOU 1181 O HOH A 230 3133 4902 4852 1856 -510 -1266 O HETATM 1182 O HOH A 231 3.122 12.288 30.073 1.00 40.05 O ANISOU 1182 O HOH A 231 6024 4898 4295 267 -654 1457 O HETATM 1183 O HOH A 232 15.451 -5.826 19.490 1.00 29.93 O ANISOU 1183 O HOH A 232 1869 4469 5032 -102 -635 1172 O HETATM 1184 O HOH A 233 6.252 11.502 19.695 1.00 32.77 O ANISOU 1184 O HOH A 233 2255 4090 6103 -950 429 -892 O HETATM 1185 O HOH A 234 10.503 -4.066 27.937 1.00 43.35 O ANISOU 1185 O HOH A 234 4737 7202 4529 3108 844 2439 O HETATM 1186 O HOH A 235 15.925 -1.244 17.812 1.00 32.05 O ANISOU 1186 O HOH A 235 4768 3937 3472 2096 -747 -599 O HETATM 1187 O HOH A 236 7.165 -3.072 30.410 1.00 30.09 O ANISOU 1187 O HOH A 236 5886 2395 3152 -159 675 91 O HETATM 1188 O HOH A 237 -4.304 12.446 13.343 1.00 56.28 O ANISOU 1188 O HOH A 237 2969 11674 6740 450 -2270 567 O HETATM 1189 O HOH A 238 -0.021 4.953 18.129 1.00 36.40 O ANISOU 1189 O HOH A 238 3264 4896 5668 -1252 -1360 2636 O HETATM 1190 O HOH A 239 15.935 -3.402 15.842 1.00 44.56 O ANISOU 1190 O HOH A 239 5513 3648 7767 -778 262 393 O HETATM 1191 O HOH A 240 12.645 25.501 6.136 1.00 36.15 O ANISOU 1191 O HOH A 240 6353 3586 3795 -296 400 1565 O HETATM 1192 O HOH A 241 7.621 3.040 -0.868 1.00 31.01 O ANISOU 1192 O HOH A 241 3910 4010 3861 1728 1192 1182 O HETATM 1193 O HOH A 242 2.230 9.927 17.431 1.00 27.15 O ANISOU 1193 O HOH A 242 3775 3728 2810 598 65 121 O HETATM 1194 O HOH A 243 21.367 5.234 21.367 1.00 44.20 O ANISOU 1194 O HOH A 243 7841 5006 3946 3024 -1005 235 O HETATM 1195 O HOH A 244 20.118 10.127 2.179 1.00 36.18 O ANISOU 1195 O HOH A 244 4424 4660 4664 1492 555 490 O HETATM 1196 O HOH A 245 19.640 14.751 18.040 1.00 64.60 O ANISOU 1196 O HOH A 245 3556 8775 12213 212 1819 1313 O HETATM 1197 O HOH A 246 -8.775 11.498 17.991 1.00 79.90 O ANISOU 1197 O HOH A 246 5814 10489 14054 289 -2567 -1536 O HETATM 1198 O HOH A 247 2.711 -2.639 17.704 1.00 32.88 O ANISOU 1198 O HOH A 247 4567 4787 3136 2369 -270 212 O HETATM 1199 O HOH A 248 6.302 22.155 -1.177 1.00 73.61 O ANISOU 1199 O HOH A 248 16031 6222 5715 -479 -590 1326 O HETATM 1200 O HOH A 249 17.245 8.802 16.381 1.00 30.47 O ANISOU 1200 O HOH A 249 4589 3358 3630 590 -319 436 O HETATM 1201 O HOH A 250 5.002 17.005 29.807 1.00 37.54 O ANISOU 1201 O HOH A 250 7550 4086 2626 -625 215 -165 O HETATM 1202 O HOH A 251 -2.811 20.272 1.661 1.00 24.70 O ANISOU 1202 O HOH A 251 2860 3127 3395 -1447 -359 272 O HETATM 1203 O HOH A 252 -1.146 18.377 1.015 1.00 26.35 O ANISOU 1203 O HOH A 252 3045 3119 3846 583 -619 -82 O HETATM 1204 O HOH A 253 0.638 7.618 -1.808 1.00 33.47 O ANISOU 1204 O HOH A 253 4695 4344 3677 257 -1707 669 O HETATM 1205 O HOH A 254 5.860 29.945 10.323 1.00 32.52 O ANISOU 1205 O HOH A 254 3148 3467 5738 -217 318 413 O HETATM 1206 O HOH A 255 -3.690 0.608 16.739 1.00 22.83 O ANISOU 1206 O HOH A 255 3214 2739 2721 -138 361 40 O HETATM 1207 O HOH A 256 18.607 17.084 2.489 1.00 38.30 O ANISOU 1207 O HOH A 256 4851 5853 3847 1546 787 -1594 O HETATM 1208 O HOH A 257 15.047 10.345 0.679 1.00 39.06 O ANISOU 1208 O HOH A 257 6570 3590 4680 1504 -973 -152 O HETATM 1209 O HOH A 258 9.275 3.019 -2.963 1.00 38.50 O ANISOU 1209 O HOH A 258 7283 3307 4039 1995 136 -90 O HETATM 1210 O HOH A 259 10.300 -5.164 9.436 1.00 38.86 O ANISOU 1210 O HOH A 259 8021 2966 3776 40 1279 -165 O HETATM 1211 O HOH A 260 5.099 -1.728 25.455 1.00 32.38 O ANISOU 1211 O HOH A 260 3578 4814 3908 1774 248 -464 O HETATM 1212 O HOH A 261 -1.958 7.967 -0.358 1.00 74.47 O ANISOU 1212 O HOH A 261 16725 5714 5856 -2121 1698 2236 O HETATM 1213 O HOH A 262 10.811 22.114 26.500 1.00121.38 O ANISOU 1213 O HOH A 262 33126 6421 6572 3830 -3305 -4837 O HETATM 1214 O HOH A 263 0.695 8.933 29.598 1.00 97.83 O ANISOU 1214 O HOH A 263 18179 7726 11263 -1801 4417 -743 O HETATM 1215 O HOH A 264 -9.397 3.985 20.554 1.00 23.85 O ANISOU 1215 O HOH A 264 3569 2148 3345 516 776 430 O HETATM 1216 O HOH A 265 12.781 10.270 31.413 1.00 67.67 O ANISOU 1216 O HOH A 265 9169 9196 7343 1117 703 -867 O HETATM 1217 O HOH A 266 11.713 6.309 -3.426 1.00 53.52 O ANISOU 1217 O HOH A 266 9414 6899 4020 -3125 -1081 611 O HETATM 1218 O HOH A 267 5.363 7.957 33.986 1.00 68.35 O ANISOU 1218 O HOH A 267 8014 10405 7551 -6666 2788 -6055 O HETATM 1219 O HOH A 268 1.951 3.744 19.548 1.00 36.37 O ANISOU 1219 O HOH A 268 4037 4908 4874 671 -203 1298 O HETATM 1220 O HOH A 269 -1.385 14.164 21.818 1.00 42.09 O ANISOU 1220 O HOH A 269 5110 5745 5135 -796 -649 -1497 O HETATM 1221 O HOH A 270 18.428 11.310 21.718 1.00 38.85 O ANISOU 1221 O HOH A 270 4288 4272 6200 224 -2144 -1155 O HETATM 1222 O HOH A 271 21.314 18.049 4.459 1.00 65.05 O ANISOU 1222 O HOH A 271 5517 2285 16913 -1134 7667 1480 O HETATM 1223 O HOH A 272 6.076 -2.389 22.817 1.00 39.30 O ANISOU 1223 O HOH A 272 5990 4577 4364 520 -1141 -786 O HETATM 1224 O HOH A 273 10.941 3.686 16.695 1.00 33.23 O ANISOU 1224 O HOH A 273 5099 3710 3813 493 -554 224 O HETATM 1225 O HOH A 274 7.948 30.665 8.504 1.00 50.10 O ANISOU 1225 O HOH A 274 5017 3309 10709 -1473 -1161 477 O HETATM 1226 O HOH A 275 -1.347 0.014 10.403 1.00 39.91 O ANISOU 1226 O HOH A 275 6508 5434 3219 1638 -377 151 O HETATM 1227 O HOH A 276 5.057 30.397 6.753 1.00 36.93 O ANISOU 1227 O HOH A 276 4666 5322 4043 450 542 924 O HETATM 1228 O HOH A 277 3.541 29.845 8.632 1.00 31.23 O ANISOU 1228 O HOH A 277 4203 3075 4585 -409 -1380 493 O HETATM 1229 O HOH A 278 16.824 -0.543 28.750 1.00 33.94 O ANISOU 1229 O HOH A 278 3959 5329 3604 2056 -82 -374 O END If you find results from 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