HEADER LYASE 13-OCT-04 1XQO TITLE CRYSTAL STRUCTURE OF NATIVE PA-AGOG, 8-OXOGUANINE DNA TITLE 2 GLYCOSYLASE FROM PYROBACULUM AEROPHILUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: 8-OXOGUANINE DNA GLYCOSYLASE; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PYROBACULUM AEROPHILUM; SOURCE 3 ORGANISM_TAXID: 13773; SOURCE 4 GENE: PA-AGOG; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28C(+) KEYWDS HELIX-HAIRPIN-HELIX, 8-OXOGUANINE DNA GLYCOSYLASE, ARCHAEA, KEYWDS 2 P.AEROPHILUM, PA-AGOG NATIVE, DNA REPAIR, LYASE EXPDTA X-RAY DIFFRACTION AUTHOR G.M.LINGARAJU,A.A.SARTORI,D.KOSTREWA,A.E.PROTA,J.JIRICNY, AUTHOR 2 F.K.WINKLER REVDAT 3 24-FEB-09 1XQO 1 VERSN REVDAT 2 01-MAR-05 1XQO 1 JRNL REVDAT 1 16-NOV-04 1XQO 0 JRNL AUTH G.M.LINGARAJU,A.A.SARTORI,D.KOSTREWA,A.E.PROTA, JRNL AUTH 2 J.JIRICNY,F.K.WINKLER JRNL TITL A DNA GLYCOSYLASE FROM PYROBACULUM AEROPHILUM WITH JRNL TITL 2 AN 8-OXOGUANINE BINDING MODE AND A NONCANONICAL JRNL TITL 3 HELIX-HAIRPIN-HELIX STRUCTURE JRNL REF STRUCTURE V. 13 87 2005 JRNL REFN ISSN 0969-2126 JRNL PMID 15642264 JRNL DOI 10.1016/J.STR.2004.10.011 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH A.A.SARTORI,G.M.LINGARAJU,P.HUNZIKER,F.K.WINKLER, REMARK 1 AUTH 2 J.JIRICNY REMARK 1 TITL A NOVEL HIGHLY THERMOSTABLE 8-OXOGUANINE DNA REMARK 1 TITL 2 GLYCOSYLASE FROM PYROBACULUM AEROPHILUM REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. 1.03 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.2 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.03 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8 REMARK 3 NUMBER OF REFLECTIONS : 110906 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) : 0.159 REMARK 3 R VALUE (WORKING SET) : 0.158 REMARK 3 FREE R VALUE : 0.183 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 5880 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) : 1.03 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.06 REMARK 3 REFLECTION IN BIN (WORKING SET) : 5467 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.3860 REMARK 3 BIN FREE R VALUE SET COUNT : 308 REMARK 3 BIN FREE R VALUE : 0.4030 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2088 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 346 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 13.00 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.57 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.09000 REMARK 3 B22 (A**2) : -0.06000 REMARK 3 B33 (A**2) : -0.03000 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): 0.028 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.906 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.976 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.969 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2141 ; 0.015 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 2035 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2901 ; 1.689 ; 1.962 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4715 ; 2.496 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 254 ; 5.066 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;27.340 ;22.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 389 ;12.177 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;15.511 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 318 ; 0.120 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2330 ; 0.009 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 465 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 491 ; 0.224 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2163 ; 0.182 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): 1291 ; 0.095 ; 0.200 REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 208 ; 0.140 ; 0.200 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): 10 ; 0.209 ; 0.200 REMARK 3 SYMMETRY VDW OTHERS (A): 50 ; 0.360 ; 0.200 REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.096 ; 0.200 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): 1645 ; 2.297 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 515 ; 1.034 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2058 ; 2.622 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1030 ; 3.657 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 843 ; 4.500 ; 6.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5106 ; 1.726 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 346 ; 7.537 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4124 ; 3.732 ; 3.000 REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 1XQO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-04. REMARK 100 THE RCSB ID CODE IS RCSB030654. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-OCT-03 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9 REMARK 200 MONOCHROMATOR : SAGITALLY FOCUSED SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116782 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.030 REMARK 200 RESOLUTION RANGE LOW (A) : 57.740 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7 REMARK 200 DATA REDUNDANCY : 5.000 REMARK 200 R MERGE (I) : 0.07000 REMARK 200 R SYM (I) : 0.05800 REMARK 200 FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.03 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.10 REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 0.46800 REMARK 200 FOR SHELL : 2.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: MAD REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD REMARK 200 SOFTWARE USED: SHARP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 43.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, HEPES-NAOH, NACL, DITHIO REMARK 280 THREITOL., PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE REMARK 280 100K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X+1/2,Y+1/2,-Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 35.44500 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.84500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.44500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.84500 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 300 REMARK: THE BIOLOGICALLY ACTIVE UNIT IS A MONOMER. 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 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 SER A 255 REMARK 465 GLU A 256 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 CYS A 155 CB CYS A 155 SG -0.163 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 CYS A 155 CA - CB - SG ANGL. DEV. = 11.0 DEGREES REMARK 500 ARG A 177 NE - CZ - NH2 ANGL. DEV. = -3.4 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 ILE A 82 -70.31 -117.75 REMARK 500 ARG A 195 51.74 -91.32 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1XQP RELATED DB: PDB REMARK 900 THE SAME PROTEIN COMPLEXED WITH 8-OXO-2'DEOXYGUANOSINE DBREF 1XQO A 1 256 UNP Q8ZVK6 Q8ZVK6_PYRAE 1 256 SEQRES 1 A 256 MET ALA ALA GLU SER GLN LEU LYS ARG VAL ILE GLU THR SEQRES 2 A 256 LEU ARG ARG LEU GLY ILE GLU GLU VAL LEU LYS LEU GLU SEQRES 3 A 256 ARG ARG ASP PRO GLN TYR ARG ALA VAL CYS ASN VAL VAL SEQRES 4 A 256 LYS ARG HIS GLY GLU THR VAL GLY SER ARG LEU ALA MET SEQRES 5 A 256 LEU ASN ALA LEU ILE SER TYR ARG LEU THR GLY LYS GLY SEQRES 6 A 256 GLU GLU HIS TRP GLU TYR PHE GLY LYS TYR PHE SER GLN SEQRES 7 A 256 LEU GLU VAL ILE ASP LEU CYS ARG ASP PHE LEU LYS TYR SEQRES 8 A 256 ILE GLU THR SER PRO PHE LEU LYS ILE GLY VAL GLU ALA SEQRES 9 A 256 ARG LYS LYS ARG ALA LEU LYS ALA CYS ASP TYR VAL PRO SEQRES 10 A 256 ASN LEU GLU ASP LEU GLY LEU THR LEU ARG GLN LEU SER SEQRES 11 A 256 HIS ILE VAL GLY ALA ARG ARG GLU GLN LYS THR LEU VAL SEQRES 12 A 256 PHE THR ILE LYS ILE LEU ASN TYR ALA TYR MET CYS SER SEQRES 13 A 256 ARG GLY VAL ASN ARG VAL LEU PRO PHE ASP ILE PRO ILE SEQRES 14 A 256 PRO VAL ASP TYR ARG VAL ALA ARG LEU THR TRP CYS ALA SEQRES 15 A 256 GLY LEU ILE ASP PHE PRO PRO GLU GLU ALA LEU ARG ARG SEQRES 16 A 256 TYR GLU ALA VAL GLN LYS ILE TRP ASP ALA VAL ALA ARG SEQRES 17 A 256 GLU THR GLY ILE PRO PRO LEU HIS LEU ASP THR LEU LEU SEQRES 18 A 256 TRP LEU ALA GLY ARG ALA VAL LEU TYR GLY GLU ASN LEU SEQRES 19 A 256 HIS GLY VAL PRO LYS GLU VAL ILE ALA LEU PHE GLN TRP SEQRES 20 A 256 ARG GLY GLY CYS ARG PRO PRO SER GLU FORMUL 2 HOH *346(H2 O) HELIX 1 1 ALA A 2 ARG A 15 1 14 HELIX 2 2 GLY A 18 ARG A 27 1 10 HELIX 3 3 ASP A 29 GLY A 43 1 15 HELIX 4 4 GLY A 43 ILE A 57 1 15 HELIX 5 5 LYS A 64 GLN A 78 1 15 HELIX 6 6 ASP A 83 SER A 95 1 13 HELIX 7 7 GLY A 101 CYS A 113 1 13 HELIX 8 8 ASP A 121 GLY A 134 1 14 HELIX 9 9 GLN A 139 GLY A 158 1 20 HELIX 10 10 ASP A 172 ALA A 182 1 11 HELIX 11 11 PRO A 188 ARG A 195 1 8 HELIX 12 12 ARG A 195 GLY A 211 1 17 HELIX 13 13 PRO A 213 LEU A 229 1 17 HELIX 14 14 PRO A 238 PHE A 245 1 8 SSBOND 1 CYS A 36 CYS A 155 1555 1555 2.03 SSBOND 2 CYS A 85 CYS A 113 1555 1555 2.01 SSBOND 3 CYS A 181 CYS A 251 1555 1555 2.06 CRYST1 70.890 97.690 36.100 90.00 90.00 90.00 P 21 21 2 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 0.014106 0.000000 0.000000 0.00000 SCALE2 0.000000 0.010236 0.000000 0.00000 SCALE3 0.000000 0.000000 0.027701 0.00000 ATOM 1 N ALA A 2 5.126 -0.982 18.082 1.00 30.64 N ANISOU 1 N ALA A 2 3860 3892 3887 -49 -51 14 N ATOM 2 CA ALA A 2 6.373 -0.166 18.205 1.00 29.40 C ANISOU 2 CA ALA A 2 3752 3750 3667 -32 -58 -18 C ATOM 3 C ALA A 2 6.318 0.717 19.426 1.00 28.56 C ANISOU 3 C ALA A 2 3596 3704 3549 -31 -136 -28 C ATOM 4 O ALA A 2 7.309 0.842 20.162 1.00 28.97 O ANISOU 4 O ALA A 2 3586 3926 3493 -15 -266 84 O ATOM 5 CB ALA A 2 6.568 0.688 16.961 1.00 30.28 C ANISOU 5 CB ALA A 2 3884 3822 3799 -57 14 36 C ATOM 6 N ALA A 3 5.167 1.344 19.646 1.00 27.07 N ANISOU 6 N ALA A 3 3494 3485 3307 -86 -233 -105 N ATOM 7 CA ALA A 3 5.024 2.288 20.751 1.00 25.40 C ANISOU 7 CA ALA A 3 3243 3212 3193 -127 -176 -38 C ATOM 8 C ALA A 3 5.198 1.592 22.096 1.00 24.01 C ANISOU 8 C ALA A 3 3044 2931 3146 -177 -244 -16 C ATOM 9 O ALA A 3 5.786 2.161 23.001 1.00 21.96 O ANISOU 9 O ALA A 3 2536 2892 2915 -191 -437 -40 O ATOM 10 CB ALA A 3 3.679 2.987 20.686 1.00 26.14 C ANISOU 10 CB ALA A 3 3422 3187 3322 -26 -214 -22 C ATOM 11 N GLU A 4 4.704 0.363 22.230 1.00 24.47 N ANISOU 11 N GLU A 4 3014 3066 3214 -224 -269 39 N ATOM 12 CA GLU A 4 4.803 -0.390 23.490 1.00 24.10 C ANISOU 12 CA GLU A 4 2983 2989 3184 -104 -174 14 C ATOM 13 C GLU A 4 6.255 -0.783 23.768 1.00 22.13 C ANISOU 13 C GLU A 4 2901 2553 2954 -74 -284 53 C ATOM 14 O GLU A 4 6.728 -0.665 24.902 1.00 21.50 O ANISOU 14 O GLU A 4 2769 2532 2866 -104 -513 90 O ATOM 15 CB GLU A 4 3.914 -1.646 23.445 1.00 24.84 C ANISOU 15 CB GLU A 4 3102 3071 3264 -161 -169 100 C ATOM 16 CG GLU A 4 3.990 -2.530 24.690 1.00 27.72 C ANISOU 16 CG GLU A 4 3471 3591 3468 -104 -130 163 C ATOM 17 CD GLU A 4 3.214 -3.833 24.562 1.00 29.54 C ANISOU 17 CD GLU A 4 3681 3686 3856 -164 -30 89 C ATOM 18 OE1 GLU A 4 2.053 -3.803 24.075 1.00 35.60 O ANISOU 18 OE1 GLU A 4 4045 4767 4712 -163 -270 72 O ATOM 19 OE2 GLU A 4 3.750 -4.906 24.961 1.00 35.27 O ANISOU 19 OE2 GLU A 4 4356 4320 4723 36 -161 173 O ATOM 20 N SER A 5 6.955 -1.259 22.743 1.00 21.13 N ANISOU 20 N SER A 5 2744 2394 2889 -151 -278 104 N ATOM 21 CA SER A 5 8.358 -1.663 22.901 1.00 19.98 C ANISOU 21 CA SER A 5 2669 2164 2756 -91 -261 102 C ATOM 22 C SER A 5 9.272 -0.461 23.124 1.00 18.43 C ANISOU 22 C SER A 5 2473 1929 2601 -53 -362 94 C ATOM 23 O SER A 5 10.229 -0.531 23.905 1.00 18.04 O ANISOU 23 O SER A 5 2525 1967 2362 36 -576 246 O ATOM 24 CB SER A 5 8.865 -2.524 21.736 1.00 21.44 C ANISOU 24 CB SER A 5 2828 2332 2984 -38 -137 24 C ATOM 25 OG SER A 5 8.633 -1.923 20.477 1.00 26.33 O ANISOU 25 OG SER A 5 3656 3084 3263 44 -53 13 O ATOM 26 N GLN A 6 8.999 0.643 22.436 1.00 17.14 N ANISOU 26 N GLN A 6 2421 1920 2168 -46 -395 195 N ATOM 27 CA GLN A 6 9.747 1.871 22.703 1.00 16.88 C ANISOU 27 CA GLN A 6 2251 1929 2232 34 -276 224 C ATOM 28 C GLN A 6 9.514 2.384 24.102 1.00 15.41 C ANISOU 28 C GLN A 6 2041 1725 2087 -87 -171 240 C ATOM 29 O GLN A 6 10.442 2.861 24.729 1.00 16.30 O ANISOU 29 O GLN A 6 1926 1935 2330 -13 -236 295 O ATOM 30 CB GLN A 6 9.446 2.945 21.635 1.00 17.48 C ANISOU 30 CB GLN A 6 2486 1958 2194 87 -275 246 C ATOM 31 CG GLN A 6 10.009 2.599 20.273 1.00 19.91 C ANISOU 31 CG GLN A 6 2674 2309 2579 183 -63 289 C ATOM 32 CD GLN A 6 11.487 2.465 20.325 1.00 19.73 C ANISOU 32 CD GLN A 6 2679 2249 2565 112 90 406 C ATOM 33 OE1 GLN A 6 11.999 1.341 20.290 1.00 21.87 O ANISOU 33 OE1 GLN A 6 2754 2171 3384 352 331 214 O ATOM 34 NE2 GLN A 6 12.191 3.570 20.512 1.00 21.05 N ANISOU 34 NE2 GLN A 6 2814 2447 2736 181 63 244 N ATOM 35 N LEU A 7 8.288 2.289 24.609 1.00 15.97 N ANISOU 35 N LEU A 7 1968 1855 2244 -98 -379 229 N ATOM 36 CA LEU A 7 8.011 2.720 25.972 1.00 15.66 C ANISOU 36 CA LEU A 7 1870 1889 2190 -46 -297 267 C ATOM 37 C LEU A 7 8.856 1.906 26.950 1.00 15.11 C ANISOU 37 C LEU A 7 1941 1595 2202 -6 -263 226 C ATOM 38 O LEU A 7 9.462 2.453 27.861 1.00 15.24 O ANISOU 38 O LEU A 7 1750 1814 2223 -115 -285 264 O ATOM 39 CB LEU A 7 6.529 2.581 26.289 1.00 15.98 C ANISOU 39 CB LEU A 7 1954 1981 2135 9 -386 338 C ATOM 40 CG LEU A 7 6.124 2.941 27.708 1.00 18.31 C ANISOU 40 CG LEU A 7 2086 2379 2490 -51 -195 38 C ATOM 41 CD1 LEU A 7 6.466 4.348 28.106 1.00 19.73 C ANISOU 41 CD1 LEU A 7 2168 2489 2840 -49 -168 -40 C ATOM 42 CD2 LEU A 7 4.631 2.676 27.902 1.00 20.28 C ANISOU 42 CD2 LEU A 7 2226 2824 2655 -86 -124 18 C ATOM 43 N LYS A 8 8.916 0.599 26.740 1.00 16.75 N ANISOU 43 N LYS A 8 2171 1876 2315 -111 -297 353 N ATOM 44 CA LYS A 8 9.738 -0.280 27.574 1.00 16.47 C ANISOU 44 CA LYS A 8 2079 1844 2334 -98 -347 372 C ATOM 45 C LYS A 8 11.204 0.105 27.496 1.00 15.48 C ANISOU 45 C LYS A 8 2002 1733 2144 -99 -234 224 C ATOM 46 O LYS A 8 11.883 0.205 28.530 1.00 15.68 O ANISOU 46 O LYS A 8 2057 1814 2085 151 -371 200 O ATOM 47 CB LYS A 8 9.588 -1.736 27.131 1.00 17.74 C ANISOU 47 CB LYS A 8 2401 1818 2519 -246 -348 442 C ATOM 48 CG LYS A 8 10.334 -2.746 28.006 1.00 19.19 C ANISOU 48 CG LYS A 8 2653 1963 2673 -148 -337 485 C ATOM 49 CD LYS A 8 10.207 -4.188 27.411 1.00 21.44 C ANISOU 49 CD LYS A 8 2969 2195 2978 -53 -178 339 C ATOM 50 CE LYS A 8 11.194 -5.223 27.977 1.00 23.80 C ANISOU 50 CE LYS A 8 3116 2766 3159 215 -10 186 C ATOM 51 NZ LYS A 8 10.975 -5.341 29.416 1.00 25.03 N ANISOU 51 NZ LYS A 8 3411 2898 3201 179 -242 476 N ATOM 52 N ARG A 9 11.705 0.337 26.291 1.00 15.36 N ANISOU 52 N ARG A 9 2024 1785 2025 -47 -227 70 N ATOM 53 CA ARG A 9 13.106 0.736 26.164 1.00 15.23 C ANISOU 53 CA ARG A 9 1868 1835 2084 42 -207 160 C ATOM 54 C ARG A 9 13.391 2.040 26.872 1.00 13.83 C ANISOU 54 C ARG A 9 1633 1628 1993 21 -127 213 C ATOM 55 O ARG A 9 14.381 2.182 27.589 1.00 14.23 O ANISOU 55 O ARG A 9 1630 1824 1953 98 -196 220 O ATOM 56 CB ARG A 9 13.517 0.816 24.692 1.00 16.74 C ANISOU 56 CB ARG A 9 2209 1962 2189 -73 -200 33 C ATOM 57 CG ARG A 9 14.945 1.303 24.469 1.00 17.79 C ANISOU 57 CG ARG A 9 2292 2198 2267 -80 3 111 C ATOM 58 CD ARG A 9 15.419 1.276 23.005 1.00 20.17 C ANISOU 58 CD ARG A 9 2423 2822 2416 -71 -66 184 C ATOM 59 NE ARG A 9 16.679 2.006 22.845 1.00 20.71 N ANISOU 59 NE ARG A 9 2345 2841 2683 -55 -70 69 N ATOM 60 CZ ARG A 9 17.246 2.348 21.695 1.00 23.74 C ANISOU 60 CZ ARG A 9 2767 3368 2883 -144 -132 205 C ATOM 61 NH1 ARG A 9 16.736 1.954 20.536 1.00 27.28 N ANISOU 61 NH1 ARG A 9 3415 3798 3149 -273 -145 58 N ATOM 62 NH2 ARG A 9 18.350 3.080 21.709 1.00 23.25 N ANISOU 62 NH2 ARG A 9 2772 3420 2640 -232 -367 345 N ATOM 63 N VAL A 10 12.519 3.022 26.717 1.00 13.50 N ANISOU 63 N VAL A 10 1610 1644 1872 55 -293 373 N ATOM 64 CA VAL A 10 12.682 4.298 27.398 1.00 13.29 C ANISOU 64 CA VAL A 10 1468 1573 2007 28 -51 210 C ATOM 65 C VAL A 10 12.716 4.104 28.898 1.00 13.73 C ANISOU 65 C VAL A 10 1503 1635 2076 -34 -269 191 C ATOM 66 O VAL A 10 13.591 4.645 29.565 1.00 14.20 O ANISOU 66 O VAL A 10 1591 1587 2218 -43 -149 243 O ATOM 67 CB VAL A 10 11.620 5.311 26.915 1.00 14.58 C ANISOU 67 CB VAL A 10 1637 1799 2104 50 -112 447 C ATOM 68 CG1 VAL A 10 11.577 6.536 27.803 1.00 15.89 C ANISOU 68 CG1 VAL A 10 1950 1761 2323 127 49 330 C ATOM 69 CG2 VAL A 10 11.883 5.703 25.493 1.00 15.40 C ANISOU 69 CG2 VAL A 10 1744 1794 2313 40 -140 417 C ATOM 70 N ILE A 11 11.759 3.364 29.429 1.00 13.41 N ANISOU 70 N ILE A 11 1457 1587 2049 -69 -141 197 N ATOM 71 CA ILE A 11 11.730 3.149 30.875 1.00 13.24 C ANISOU 71 CA ILE A 11 1430 1683 1917 59 11 55 C ATOM 72 C ILE A 11 12.993 2.476 31.365 1.00 12.88 C ANISOU 72 C ILE A 11 1294 1783 1813 -54 -81 164 C ATOM 73 O ILE A 11 13.576 2.898 32.347 1.00 13.63 O ANISOU 73 O ILE A 11 1428 1898 1851 49 -88 119 O ATOM 74 CB ILE A 11 10.485 2.320 31.257 1.00 14.00 C ANISOU 74 CB ILE A 11 1479 1730 2107 39 51 133 C ATOM 75 CG1 ILE A 11 9.222 3.206 31.118 1.00 15.18 C ANISOU 75 CG1 ILE A 11 1504 2054 2209 172 -124 166 C ATOM 76 CG2 ILE A 11 10.594 1.671 32.623 1.00 14.62 C ANISOU 76 CG2 ILE A 11 1500 1905 2147 -6 -36 153 C ATOM 77 CD1 ILE A 11 7.935 2.453 31.127 1.00 15.91 C ANISOU 77 CD1 ILE A 11 1700 2275 2068 36 -37 119 C ATOM 78 N GLU A 12 13.382 1.411 30.690 1.00 12.74 N ANISOU 78 N GLU A 12 1340 1725 1773 109 -81 153 N ATOM 79 CA GLU A 12 14.499 0.612 31.156 1.00 13.10 C ANISOU 79 CA GLU A 12 1414 1726 1837 71 -61 229 C ATOM 80 C GLU A 12 15.864 1.285 30.979 1.00 12.44 C ANISOU 80 C GLU A 12 1478 1609 1640 47 -37 268 C ATOM 81 O GLU A 12 16.837 0.920 31.659 1.00 12.93 O ANISOU 81 O GLU A 12 1423 1720 1769 15 -22 402 O ATOM 82 CB GLU A 12 14.485 -0.754 30.486 1.00 13.69 C ANISOU 82 CB GLU A 12 1580 1690 1929 39 -73 206 C ATOM 83 CG GLU A 12 13.269 -1.540 30.972 1.00 16.20 C ANISOU 83 CG GLU A 12 1658 1989 2506 -72 -130 293 C ATOM 84 CD GLU A 12 13.051 -2.901 30.354 1.00 17.56 C ANISOU 84 CD GLU A 12 2045 1894 2731 -111 -113 248 C ATOM 85 OE1 GLU A 12 13.743 -3.227 29.358 1.00 21.34 O ANISOU 85 OE1 GLU A 12 2587 2135 3386 123 24 -453 O ATOM 86 OE2 GLU A 12 12.157 -3.627 30.866 1.00 20.60 O ANISOU 86 OE2 GLU A 12 2325 1999 3501 -212 -403 470 O ATOM 87 N THR A 13 15.915 2.300 30.112 1.00 12.94 N ANISOU 87 N THR A 13 1511 1542 1862 -33 -74 356 N ATOM 88 CA THR A 13 17.090 3.132 29.965 1.00 12.77 C ANISOU 88 CA THR A 13 1431 1682 1736 -84 -126 294 C ATOM 89 C THR A 13 17.094 4.258 30.988 1.00 13.04 C ANISOU 89 C THR A 13 1449 1805 1700 -86 -82 304 C ATOM 90 O THR A 13 18.120 4.489 31.604 1.00 14.38 O ANISOU 90 O THR A 13 1672 1837 1954 61 -179 99 O ATOM 91 CB THR A 13 17.147 3.673 28.521 1.00 13.14 C ANISOU 91 CB THR A 13 1655 1617 1720 -85 -68 318 C ATOM 92 OG1 THR A 13 17.146 2.570 27.593 1.00 14.70 O ANISOU 92 OG1 THR A 13 1937 1883 1764 24 -70 310 O ATOM 93 CG2 THR A 13 18.404 4.485 28.295 1.00 14.31 C ANISOU 93 CG2 THR A 13 1714 1948 1774 -104 37 371 C ATOM 94 N LEU A 14 15.970 4.954 31.163 1.00 14.37 N ANISOU 94 N LEU A 14 1676 1788 1993 48 40 135 N ATOM 95 CA LEU A 14 15.914 6.032 32.144 1.00 14.85 C ANISOU 95 CA LEU A 14 1720 1807 2115 7 50 69 C ATOM 96 C LEU A 14 16.030 5.480 33.579 1.00 15.48 C ANISOU 96 C LEU A 14 1755 1983 2143 203 -69 49 C ATOM 97 O LEU A 14 16.463 6.224 34.464 1.00 17.09 O ANISOU 97 O LEU A 14 1984 2238 2271 38 -145 -280 O ATOM 98 CB LEU A 14 14.664 6.854 31.988 1.00 15.05 C ANISOU 98 CB LEU A 14 1607 1846 2264 -3 121 7 C ATOM 99 CG LEU A 14 14.593 7.654 30.700 1.00 15.20 C ANISOU 99 CG LEU A 14 1707 1777 2289 54 -62 -54 C ATOM 100 CD1 LEU A 14 13.293 8.444 30.632 1.00 17.75 C ANISOU 100 CD1 LEU A 14 1836 1861 3047 214 2 282 C ATOM 101 CD2 LEU A 14 15.777 8.609 30.496 1.00 17.93 C ANISOU 101 CD2 LEU A 14 1960 2047 2806 -126 146 252 C ATOM 102 N ARG A 15 15.702 4.213 33.818 1.00 15.37 N ANISOU 102 N ARG A 15 1825 2131 1882 -43 83 90 N ATOM 103 CA ARG A 15 15.937 3.563 35.113 1.00 17.39 C ANISOU 103 CA ARG A 15 2173 2364 2070 -87 89 103 C ATOM 104 C ARG A 15 17.403 3.535 35.506 1.00 17.42 C ANISOU 104 C ARG A 15 2307 2310 2000 -77 -74 104 C ATOM 105 O ARG A 15 17.719 3.311 36.689 1.00 18.80 O ANISOU 105 O ARG A 15 2432 2702 2006 -128 -261 275 O ATOM 106 CB ARG A 15 15.442 2.114 35.107 1.00 17.58 C ANISOU 106 CB ARG A 15 2155 2450 2075 -100 92 132 C ATOM 107 CG ARG A 15 14.036 1.968 35.456 1.00 21.34 C ANISOU 107 CG ARG A 15 2528 2823 2756 5 -72 9 C ATOM 108 CD ARG A 15 13.724 0.544 35.585 1.00 21.89 C ANISOU 108 CD ARG A 15 2714 2730 2872 -37 -19 -177 C ATOM 109 NE ARG A 15 12.313 0.420 35.822 1.00 22.92 N ANISOU 109 NE ARG A 15 2964 2978 2763 49 238 84 N ATOM 110 CZ ARG A 15 11.551 -0.483 35.296 1.00 22.89 C ANISOU 110 CZ ARG A 15 2955 2768 2972 47 -81 302 C ATOM 111 NH1 ARG A 15 12.058 -1.434 34.519 1.00 22.75 N ANISOU 111 NH1 ARG A 15 2501 3006 3136 322 34 68 N ATOM 112 NH2 ARG A 15 10.264 -0.464 35.587 1.00 25.84 N ANISOU 112 NH2 ARG A 15 3100 3367 3349 294 165 176 N ATOM 113 N ARG A 16 18.298 3.778 34.554 1.00 16.20 N ANISOU 113 N ARG A 16 1915 2207 2033 100 -165 -38 N ATOM 114 CA ARG A 16 19.739 3.860 34.832 1.00 17.15 C ANISOU 114 CA ARG A 16 2136 2231 2146 88 -219 0 C ATOM 115 C ARG A 16 20.096 5.143 35.591 1.00 18.21 C ANISOU 115 C ARG A 16 2154 2570 2192 138 -290 -196 C ATOM 116 O ARG A 16 21.192 5.214 36.148 1.00 21.34 O ANISOU 116 O ARG A 16 2229 3053 2823 2 -544 -219 O ATOM 117 CB ARG A 16 20.550 3.768 33.531 1.00 16.69 C ANISOU 117 CB ARG A 16 2016 2138 2187 135 -161 -8 C ATOM 118 CG ARG A 16 20.443 2.443 32.830 1.00 15.94 C ANISOU 118 CG ARG A 16 1867 1899 2290 40 -266 126 C ATOM 119 CD ARG A 16 20.954 2.459 31.434 1.00 15.01 C ANISOU 119 CD ARG A 16 1878 1595 2228 -83 -196 26 C ATOM 120 NE ARG A 16 22.344 2.876 31.397 1.00 14.82 N ANISOU 120 NE ARG A 16 1999 1529 2100 -152 120 193 N ATOM 121 CZ ARG A 16 23.363 2.078 31.590 1.00 15.95 C ANISOU 121 CZ ARG A 16 1898 1935 2227 -198 -124 -172 C ATOM 122 NH1 ARG A 16 23.201 0.784 31.817 1.00 15.96 N ANISOU 122 NH1 ARG A 16 1922 1814 2325 178 -212 -108 N ATOM 123 NH2 ARG A 16 24.589 2.600 31.563 1.00 19.24 N ANISOU 123 NH2 ARG A 16 2073 2467 2768 -360 28 -201 N ATOM 124 N LEU A 17 19.190 6.129 35.615 1.00 17.48 N ANISOU 124 N LEU A 17 2063 2540 2037 70 -226 -87 N ATOM 125 CA LEU A 17 19.363 7.396 36.323 1.00 18.92 C ANISOU 125 CA LEU A 17 2372 2599 2218 4 -115 -61 C ATOM 126 C LEU A 17 18.464 7.445 37.549 1.00 20.67 C ANISOU 126 C LEU A 17 2483 2862 2509 -204 -61 -153 C ATOM 127 O LEU A 17 17.292 7.079 37.482 1.00 24.22 O ANISOU 127 O LEU A 17 2516 3747 2937 -60 112 -216 O ATOM 128 CB LEU A 17 18.992 8.578 35.412 1.00 19.16 C ANISOU 128 CB LEU A 17 2350 2585 2345 -61 -172 -24 C ATOM 129 CG LEU A 17 19.717 8.665 34.081 1.00 22.73 C ANISOU 129 CG LEU A 17 3092 2798 2744 197 -26 266 C ATOM 130 CD1 LEU A 17 19.272 9.845 33.284 1.00 24.30 C ANISOU 130 CD1 LEU A 17 3276 2928 3025 371 -101 273 C ATOM 131 CD2 LEU A 17 21.191 8.717 34.297 1.00 28.42 C ANISOU 131 CD2 LEU A 17 3467 3802 3527 -132 61 162 C ATOM 132 N GLY A 18 19.026 7.895 38.664 1.00 20.79 N ANISOU 132 N GLY A 18 2663 2751 2485 -157 126 -304 N ATOM 133 CA GLY A 18 18.253 8.127 39.891 1.00 20.45 C ANISOU 133 CA GLY A 18 2681 2644 2441 -163 211 -122 C ATOM 134 C GLY A 18 17.704 9.540 40.030 1.00 19.60 C ANISOU 134 C GLY A 18 2453 2371 2624 -235 277 -87 C ATOM 135 O GLY A 18 18.259 10.499 39.464 1.00 19.11 O ANISOU 135 O GLY A 18 2508 2362 2387 -239 450 -90 O ATOM 136 N ILE A 19 16.626 9.695 40.809 1.00 20.16 N ANISOU 136 N ILE A 19 2545 2648 2465 -198 367 -84 N ATOM 137 CA ILE A 19 16.032 11.030 41.004 1.00 18.36 C ANISOU 137 CA ILE A 19 2278 2433 2263 -105 355 -98 C ATOM 138 C ILE A 19 17.115 11.988 41.550 1.00 16.57 C ANISOU 138 C ILE A 19 1985 2265 2045 -38 336 57 C ATOM 139 O ILE A 19 17.104 13.171 41.240 1.00 17.78 O ANISOU 139 O ILE A 19 2171 2322 2262 -45 318 153 O ATOM 140 CB ILE A 19 14.747 10.981 41.891 1.00 18.72 C ANISOU 140 CB ILE A 19 2372 2626 2115 -245 312 11 C ATOM 141 CG1 ILE A 19 14.066 12.342 42.048 1.00 19.16 C ANISOU 141 CG1 ILE A 19 2217 2796 2266 -81 236 -158 C ATOM 142 CG2 ILE A 19 15.072 10.408 43.275 1.00 20.19 C ANISOU 142 CG2 ILE A 19 2367 2829 2475 -120 272 139 C ATOM 143 CD1 ILE A 19 13.647 12.941 40.790 1.00 20.43 C ANISOU 143 CD1 ILE A 19 1977 3159 2626 -130 -31 -107 C ATOM 144 N GLU A 20 18.051 11.503 42.397 1.00 18.02 N ANISOU 144 N GLU A 20 2298 2424 2125 3 201 160 N ATOM 145 CA GLU A 20 19.055 12.427 42.979 1.00 19.11 C ANISOU 145 CA GLU A 20 2474 2604 2181 -103 151 71 C ATOM 146 C GLU A 20 19.931 12.998 41.871 1.00 17.37 C ANISOU 146 C GLU A 20 2265 2283 2048 -107 147 180 C ATOM 147 O GLU A 20 20.272 14.153 41.909 1.00 19.13 O ANISOU 147 O GLU A 20 2553 2560 2154 -93 39 88 O ATOM 148 CB GLU A 20 19.926 11.820 44.094 1.00 21.48 C ANISOU 148 CB GLU A 20 2630 3094 2434 -110 42 71 C ATOM 149 CG AGLU A 20 20.962 12.748 44.726 0.50 22.49 C ANISOU 149 CG AGLU A 20 2767 3118 2657 -163 89 -27 C ATOM 150 CG BGLU A 20 20.935 12.839 44.651 0.50 23.34 C ANISOU 150 CG BGLU A 20 2852 3288 2726 -197 73 -12 C ATOM 151 CD AGLU A 20 21.867 12.064 45.754 0.50 23.48 C ANISOU 151 CD AGLU A 20 2883 3200 2838 -114 49 35 C ATOM 152 CD BGLU A 20 20.315 14.189 45.027 0.50 28.09 C ANISOU 152 CD BGLU A 20 3536 3562 3573 16 33 100 C ATOM 153 OE1AGLU A 20 21.814 10.830 45.902 0.50 25.53 O ANISOU 153 OE1AGLU A 20 3074 3256 3369 220 -73 35 O ATOM 154 OE1BGLU A 20 19.482 14.196 45.966 0.50 32.20 O ANISOU 154 OE1BGLU A 20 3944 4421 3869 8 176 -34 O ATOM 155 OE2AGLU A 20 22.633 12.777 46.424 0.50 26.87 O ANISOU 155 OE2AGLU A 20 3284 3716 3207 -213 -12 -46 O ATOM 156 OE2BGLU A 20 20.641 15.253 44.415 0.50 23.66 O ANISOU 156 OE2BGLU A 20 2669 4155 2162 82 296 72 O ATOM 157 N GLU A 21 20.279 12.185 40.881 1.00 17.54 N ANISOU 157 N GLU A 21 2269 2173 2219 -52 170 308 N ATOM 158 CA GLU A 21 21.054 12.676 39.724 1.00 17.67 C ANISOU 158 CA GLU A 21 2225 2278 2210 -79 203 179 C ATOM 159 C GLU A 21 20.297 13.735 38.920 1.00 15.37 C ANISOU 159 C GLU A 21 1953 2016 1868 -31 72 213 C ATOM 160 O GLU A 21 20.880 14.715 38.478 1.00 16.39 O ANISOU 160 O GLU A 21 1869 2129 2230 -24 273 217 O ATOM 161 CB GLU A 21 21.434 11.502 38.841 1.00 19.73 C ANISOU 161 CB GLU A 21 2486 2339 2672 204 292 57 C ATOM 162 CG GLU A 21 22.386 10.479 39.464 1.00 23.94 C ANISOU 162 CG GLU A 21 2970 3143 2982 84 220 128 C ATOM 163 CD GLU A 21 22.323 9.142 38.746 1.00 25.48 C ANISOU 163 CD GLU A 21 3262 3067 3351 141 197 78 C ATOM 164 OE1 GLU A 21 22.782 9.091 37.589 1.00 35.76 O ANISOU 164 OE1 GLU A 21 4888 4917 3782 -97 378 -83 O ATOM 165 OE2 GLU A 21 21.775 8.154 39.294 1.00 31.68 O ANISOU 165 OE2 GLU A 21 3953 3835 4248 -215 259 180 O ATOM 166 N VAL A 22 18.983 13.570 38.801 1.00 15.73 N ANISOU 166 N VAL A 22 2071 1823 2083 -2 223 21 N ATOM 167 CA VAL A 22 18.159 14.570 38.103 1.00 15.86 C ANISOU 167 CA VAL A 22 1907 2233 1886 -103 174 93 C ATOM 168 C VAL A 22 18.122 15.880 38.834 1.00 14.70 C ANISOU 168 C VAL A 22 1731 1801 2052 30 115 171 C ATOM 169 O VAL A 22 18.267 16.941 38.265 1.00 15.95 O ANISOU 169 O VAL A 22 1944 2196 1920 24 29 4 O ATOM 170 CB VAL A 22 16.755 14.052 37.794 1.00 16.76 C ANISOU 170 CB VAL A 22 2018 2324 2025 -17 -10 -130 C ATOM 171 CG1 VAL A 22 15.980 15.063 36.928 1.00 18.31 C ANISOU 171 CG1 VAL A 22 2058 2604 2292 -2 -7 -52 C ATOM 172 CG2 VAL A 22 16.802 12.708 37.095 1.00 18.57 C ANISOU 172 CG2 VAL A 22 2303 2627 2123 -171 97 19 C ATOM 173 N LEU A 23 17.927 15.809 40.168 1.00 16.10 N ANISOU 173 N LEU A 23 2026 2051 2038 -207 99 16 N ATOM 174 CA LEU A 23 17.932 17.010 40.986 1.00 16.14 C ANISOU 174 CA LEU A 23 2158 2124 1851 -46 200 -116 C ATOM 175 C LEU A 23 19.256 17.735 40.853 1.00 14.76 C ANISOU 175 C LEU A 23 1931 2000 1674 31 174 -38 C ATOM 176 O LEU A 23 19.295 18.962 40.851 1.00 17.40 O ANISOU 176 O LEU A 23 2141 2358 2111 13 223 21 O ATOM 177 CB LEU A 23 17.671 16.603 42.431 1.00 17.15 C ANISOU 177 CB LEU A 23 2244 2248 2023 -161 290 -120 C ATOM 178 CG LEU A 23 16.261 16.240 42.805 1.00 18.26 C ANISOU 178 CG LEU A 23 2243 2715 1980 -371 328 -198 C ATOM 179 CD1 LEU A 23 16.252 15.445 44.115 1.00 19.21 C ANISOU 179 CD1 LEU A 23 2634 2584 2080 -206 186 -250 C ATOM 180 CD2 LEU A 23 15.424 17.455 42.897 1.00 21.80 C ANISOU 180 CD2 LEU A 23 2397 2867 3018 -9 -100 -38 C ATOM 181 N LYS A 24 20.352 17.002 40.791 1.00 16.68 N ANISOU 181 N LYS A 24 2033 2278 2025 -47 113 109 N ATOM 182 CA LYS A 24 21.645 17.643 40.603 1.00 16.64 C ANISOU 182 CA LYS A 24 1988 2279 2056 -37 7 31 C ATOM 183 C LYS A 24 21.750 18.344 39.250 1.00 14.78 C ANISOU 183 C LYS A 24 1829 1962 1823 -170 70 -80 C ATOM 184 O LYS A 24 22.257 19.463 39.160 1.00 16.14 O ANISOU 184 O LYS A 24 1894 2200 2036 -185 197 -38 O ATOM 185 CB LYS A 24 22.753 16.621 40.747 1.00 18.55 C ANISOU 185 CB LYS A 24 2182 2480 2384 -166 151 117 C ATOM 186 CG LYS A 24 23.088 16.276 42.146 1.00 22.90 C ANISOU 186 CG LYS A 24 2998 3036 2665 48 -35 190 C ATOM 187 CD LYS A 24 24.327 15.432 42.205 1.00 24.56 C ANISOU 187 CD LYS A 24 3066 3168 3095 38 -203 222 C ATOM 188 CE LYS A 24 24.617 14.935 43.609 1.00 28.17 C ANISOU 188 CE LYS A 24 3691 3734 3278 2 -74 261 C ATOM 189 NZ LYS A 24 24.831 16.021 44.627 1.00 34.38 N ANISOU 189 NZ LYS A 24 4542 4265 4256 -125 -3 -103 N ATOM 190 N LEU A 25 21.224 17.709 38.209 1.00 14.99 N ANISOU 190 N LEU A 25 1910 1930 1854 28 209 -47 N ATOM 191 CA LEU A 25 21.220 18.318 36.883 1.00 15.71 C ANISOU 191 CA LEU A 25 2202 1929 1837 -1 260 24 C ATOM 192 C LEU A 25 20.442 19.610 36.832 1.00 14.92 C ANISOU 192 C LEU A 25 2146 1810 1712 52 191 -90 C ATOM 193 O LEU A 25 20.756 20.492 36.049 1.00 16.61 O ANISOU 193 O LEU A 25 2421 1874 2017 43 223 -79 O ATOM 194 CB LEU A 25 20.699 17.346 35.830 1.00 15.58 C ANISOU 194 CB LEU A 25 2107 1888 1924 1 243 -1 C ATOM 195 CG LEU A 25 21.637 16.222 35.473 1.00 15.12 C ANISOU 195 CG LEU A 25 2107 1976 1661 -119 184 41 C ATOM 196 CD1 LEU A 25 20.916 15.117 34.717 1.00 18.92 C ANISOU 196 CD1 LEU A 25 2549 2104 2533 -168 327 17 C ATOM 197 CD2 LEU A 25 22.841 16.725 34.674 1.00 16.29 C ANISOU 197 CD2 LEU A 25 2122 2198 1868 -102 130 -53 C ATOM 198 N GLU A 26 19.383 19.709 37.631 1.00 15.22 N ANISOU 198 N GLU A 26 2044 1845 1891 53 182 -100 N ATOM 199 CA GLU A 26 18.595 20.928 37.618 1.00 15.30 C ANISOU 199 CA GLU A 26 1952 1923 1936 48 109 -64 C ATOM 200 C GLU A 26 19.384 22.176 37.988 1.00 15.33 C ANISOU 200 C GLU A 26 1869 1822 2134 125 216 -102 C ATOM 201 O GLU A 26 19.108 23.249 37.463 1.00 16.42 O ANISOU 201 O GLU A 26 2087 1948 2200 231 166 -31 O ATOM 202 CB GLU A 26 17.372 20.734 38.513 1.00 15.72 C ANISOU 202 CB GLU A 26 1953 1868 2149 -3 105 -15 C ATOM 203 CG GLU A 26 16.416 19.750 37.807 1.00 16.01 C ANISOU 203 CG GLU A 26 1936 1877 2271 40 153 -97 C ATOM 204 CD GLU A 26 15.169 19.356 38.540 1.00 15.73 C ANISOU 204 CD GLU A 26 1984 1853 2139 47 104 -154 C ATOM 205 OE1 GLU A 26 14.970 19.766 39.700 1.00 17.19 O ANISOU 205 OE1 GLU A 26 2069 2128 2333 -33 240 -339 O ATOM 206 OE2 GLU A 26 14.375 18.607 37.899 1.00 16.62 O ANISOU 206 OE2 GLU A 26 2003 2020 2290 -78 27 -166 O ATOM 207 N ARG A 27 20.404 22.024 38.832 1.00 14.62 N ANISOU 207 N ARG A 27 1760 1667 2127 -4 97 32 N ATOM 208 CA ARG A 27 21.239 23.160 39.153 1.00 15.53 C ANISOU 208 CA ARG A 27 2110 1787 2002 -45 140 -17 C ATOM 209 C ARG A 27 22.007 23.703 37.969 1.00 15.43 C ANISOU 209 C ARG A 27 1983 1816 2061 -123 197 -138 C ATOM 210 O ARG A 27 22.470 24.830 38.006 1.00 17.36 O ANISOU 210 O ARG A 27 2356 2038 2200 -304 301 -223 O ATOM 211 CB ARG A 27 22.219 22.829 40.285 1.00 16.21 C ANISOU 211 CB ARG A 27 2066 2077 2015 -201 212 50 C ATOM 212 CG ARG A 27 21.616 22.986 41.654 1.00 17.68 C ANISOU 212 CG ARG A 27 2260 2289 2166 -146 157 238 C ATOM 213 CD ARG A 27 20.469 22.089 41.936 1.00 19.20 C ANISOU 213 CD ARG A 27 2479 2704 2112 -308 354 -109 C ATOM 214 NE ARG A 27 20.006 22.320 43.284 1.00 20.28 N ANISOU 214 NE ARG A 27 2850 2630 2225 -518 668 -135 N ATOM 215 CZ ARG A 27 19.062 21.634 43.866 1.00 17.83 C ANISOU 215 CZ ARG A 27 2352 2201 2221 -107 372 -82 C ATOM 216 NH1 ARG A 27 18.472 20.659 43.215 1.00 19.74 N ANISOU 216 NH1 ARG A 27 2546 2504 2448 -274 498 -291 N ATOM 217 NH2 ARG A 27 18.742 21.916 45.098 1.00 18.20 N ANISOU 217 NH2 ARG A 27 2416 2346 2152 -175 447 -214 N ATOM 218 N ARG A 28 22.189 22.881 36.935 1.00 16.08 N ANISOU 218 N ARG A 28 2189 1865 2056 -1 129 -133 N ATOM 219 CA ARG A 28 22.914 23.290 35.727 1.00 17.06 C ANISOU 219 CA ARG A 28 2213 2181 2087 37 281 -98 C ATOM 220 C ARG A 28 21.985 23.956 34.705 1.00 17.56 C ANISOU 220 C ARG A 28 2235 2310 2124 -36 188 -67 C ATOM 221 O ARG A 28 22.434 24.580 33.732 1.00 19.59 O ANISOU 221 O ARG A 28 2540 2720 2182 -35 296 248 O ATOM 222 CB ARG A 28 23.509 22.073 35.009 1.00 17.81 C ANISOU 222 CB ARG A 28 2362 2151 2253 59 451 -10 C ATOM 223 CG ARG A 28 24.357 21.149 35.850 1.00 19.57 C ANISOU 223 CG ARG A 28 2516 2155 2762 159 473 30 C ATOM 224 CD ARG A 28 25.706 21.656 36.150 1.00 21.44 C ANISOU 224 CD ARG A 28 2671 2435 3038 19 368 302 C ATOM 225 NE ARG A 28 25.727 22.853 36.978 1.00 21.19 N ANISOU 225 NE ARG A 28 1968 2820 3262 -132 -42 169 N ATOM 226 CZ ARG A 28 25.609 22.868 38.308 1.00 23.71 C ANISOU 226 CZ ARG A 28 2373 3223 3412 4 81 27 C ATOM 227 NH1 ARG A 28 25.528 21.740 38.987 1.00 24.04 N ANISOU 227 NH1 ARG A 28 2343 3408 3383 83 362 280 N ATOM 228 NH2 ARG A 28 25.651 24.010 38.984 1.00 24.53 N ANISOU 228 NH2 ARG A 28 2252 3429 3640 -305 9 -20 N ATOM 229 N ASP A 29 20.679 23.817 34.880 1.00 17.06 N ANISOU 229 N ASP A 29 2162 2238 2079 149 224 -224 N ATOM 230 CA ASP A 29 19.708 24.373 33.913 1.00 16.93 C ANISOU 230 CA ASP A 29 2326 2211 1894 116 87 -145 C ATOM 231 C ASP A 29 19.820 25.876 33.903 1.00 17.43 C ANISOU 231 C ASP A 29 2339 2205 2076 171 232 -133 C ATOM 232 O ASP A 29 19.754 26.486 34.985 1.00 17.91 O ANISOU 232 O ASP A 29 2351 2326 2128 159 231 -349 O ATOM 233 CB ASP A 29 18.311 23.920 34.360 1.00 17.79 C ANISOU 233 CB ASP A 29 2404 2258 2094 117 131 -197 C ATOM 234 CG ASP A 29 17.172 24.367 33.458 1.00 16.59 C ANISOU 234 CG ASP A 29 2328 2052 1922 4 145 -268 C ATOM 235 OD1 ASP A 29 17.379 25.180 32.536 1.00 18.88 O ANISOU 235 OD1 ASP A 29 2699 2085 2387 75 115 -85 O ATOM 236 OD2 ASP A 29 16.041 23.889 33.700 1.00 17.82 O ANISOU 236 OD2 ASP A 29 2441 2121 2209 182 194 -41 O ATOM 237 N PRO A 30 20.006 26.530 32.748 1.00 18.72 N ANISOU 237 N PRO A 30 2656 2338 2117 290 157 -201 N ATOM 238 CA PRO A 30 20.056 27.986 32.743 1.00 19.24 C ANISOU 238 CA PRO A 30 2736 2270 2303 109 199 -139 C ATOM 239 C PRO A 30 18.788 28.606 33.363 1.00 18.44 C ANISOU 239 C PRO A 30 2770 1953 2280 95 269 -107 C ATOM 240 O PRO A 30 18.885 29.723 33.884 1.00 18.45 O ANISOU 240 O PRO A 30 2914 2144 1949 74 237 -89 O ATOM 241 CB PRO A 30 20.213 28.329 31.256 1.00 21.30 C ANISOU 241 CB PRO A 30 3165 2480 2445 14 378 -53 C ATOM 242 CG PRO A 30 19.756 27.098 30.548 1.00 23.54 C ANISOU 242 CG PRO A 30 3549 2756 2638 170 -22 60 C ATOM 243 CD PRO A 30 20.245 25.969 31.396 1.00 19.36 C ANISOU 243 CD PRO A 30 3097 2180 2079 277 237 -105 C ATOM 244 N GLN A 31 17.626 27.916 33.279 1.00 17.74 N ANISOU 244 N GLN A 31 2693 1953 2092 127 153 -142 N ATOM 245 CA GLN A 31 16.434 28.418 33.943 1.00 16.82 C ANISOU 245 CA GLN A 31 2485 1730 2173 360 59 -141 C ATOM 246 C GLN A 31 16.623 28.508 35.467 1.00 15.79 C ANISOU 246 C GLN A 31 2159 1729 2109 227 126 -25 C ATOM 247 O GLN A 31 16.260 29.475 36.109 1.00 16.76 O ANISOU 247 O GLN A 31 2423 1729 2213 353 34 -233 O ATOM 248 CB GLN A 31 15.230 27.517 33.593 1.00 17.98 C ANISOU 248 CB GLN A 31 2573 1950 2307 244 25 -165 C ATOM 249 CG GLN A 31 14.841 27.571 32.145 1.00 18.56 C ANISOU 249 CG GLN A 31 2673 2012 2367 89 -181 -27 C ATOM 250 CD GLN A 31 13.857 26.516 31.675 1.00 19.49 C ANISOU 250 CD GLN A 31 2572 1981 2851 279 -144 -22 C ATOM 251 OE1 GLN A 31 13.149 26.748 30.678 1.00 20.01 O ANISOU 251 OE1 GLN A 31 2594 2359 2651 401 -128 -21 O ATOM 252 NE2 GLN A 31 13.838 25.347 32.312 1.00 21.49 N ANISOU 252 NE2 GLN A 31 3144 2122 2899 34 -243 123 N ATOM 253 N TYR A 32 17.227 27.455 36.026 1.00 16.54 N ANISOU 253 N TYR A 32 2403 1795 2084 239 174 -161 N ATOM 254 CA TYR A 32 17.541 27.424 37.472 1.00 15.95 C ANISOU 254 CA TYR A 32 2184 1742 2132 216 44 -144 C ATOM 255 C TYR A 32 18.506 28.540 37.831 1.00 15.44 C ANISOU 255 C TYR A 32 2065 1795 2005 308 81 7 C ATOM 256 O TYR A 32 18.335 29.262 38.825 1.00 15.67 O ANISOU 256 O TYR A 32 2183 1686 2082 229 154 -101 O ATOM 257 CB TYR A 32 18.121 26.080 37.854 1.00 16.32 C ANISOU 257 CB TYR A 32 2176 1793 2230 183 159 -85 C ATOM 258 CG TYR A 32 18.420 25.984 39.344 1.00 15.26 C ANISOU 258 CG TYR A 32 2000 1733 2063 143 347 102 C ATOM 259 CD1 TYR A 32 19.577 26.510 39.892 1.00 15.16 C ANISOU 259 CD1 TYR A 32 2052 1750 1955 113 234 111 C ATOM 260 CD2 TYR A 32 17.532 25.367 40.207 1.00 17.40 C ANISOU 260 CD2 TYR A 32 2066 2208 2334 139 118 132 C ATOM 261 CE1 TYR A 32 19.834 26.443 41.260 1.00 16.57 C ANISOU 261 CE1 TYR A 32 2129 1877 2287 27 55 92 C ATOM 262 CE2 TYR A 32 17.757 25.273 41.549 1.00 18.89 C ANISOU 262 CE2 TYR A 32 2184 2735 2257 109 193 356 C ATOM 263 CZ TYR A 32 18.911 25.826 42.086 1.00 17.37 C ANISOU 263 CZ TYR A 32 2188 2298 2113 180 89 220 C ATOM 264 OH TYR A 32 19.127 25.706 43.437 1.00 21.16 O ANISOU 264 OH TYR A 32 2818 3191 2030 409 208 256 O ATOM 265 N ARG A 33 19.562 28.695 37.040 1.00 15.76 N ANISOU 265 N ARG A 33 2118 1822 2047 216 224 -180 N ATOM 266 CA ARG A 33 20.552 29.702 37.341 1.00 16.51 C ANISOU 266 CA ARG A 33 2164 1915 2192 245 93 -2 C ATOM 267 C ARG A 33 19.977 31.109 37.318 1.00 15.33 C ANISOU 267 C ARG A 33 2004 1895 1925 163 94 17 C ATOM 268 O ARG A 33 20.280 31.915 38.222 1.00 15.28 O ANISOU 268 O ARG A 33 1879 1862 2063 102 -51 88 O ATOM 269 CB ARG A 33 21.735 29.561 36.382 1.00 17.16 C ANISOU 269 CB ARG A 33 2035 2057 2428 126 148 -13 C ATOM 270 CG ARG A 33 22.469 28.227 36.570 1.00 24.44 C ANISOU 270 CG ARG A 33 3203 2833 3248 181 -37 18 C ATOM 271 CD ARG A 33 23.771 28.052 35.782 1.00 27.80 C ANISOU 271 CD ARG A 33 3253 3556 3754 316 129 17 C ATOM 272 NE ARG A 33 23.586 27.457 34.451 1.00 32.27 N ANISOU 272 NE ARG A 33 3973 4034 4250 -45 -113 -90 N ATOM 273 CZ ARG A 33 23.592 28.129 33.295 1.00 35.34 C ANISOU 273 CZ ARG A 33 4496 4597 4335 14 21 -33 C ATOM 274 NH1 ARG A 33 23.795 29.447 33.248 1.00 39.30 N ANISOU 274 NH1 ARG A 33 5165 4895 4869 -108 -2 0 N ATOM 275 NH2 ARG A 33 23.390 27.472 32.154 1.00 38.55 N ANISOU 275 NH2 ARG A 33 5154 4896 4595 -47 -17 -14 N ATOM 276 N ALA A 34 19.161 31.430 36.320 1.00 14.76 N ANISOU 276 N ALA A 34 2009 1877 1723 52 21 11 N ATOM 277 CA ALA A 34 18.550 32.747 36.264 1.00 14.81 C ANISOU 277 CA ALA A 34 2072 1659 1894 124 -12 45 C ATOM 278 C ALA A 34 17.637 32.972 37.464 1.00 14.60 C ANISOU 278 C ALA A 34 1995 1490 2060 187 -113 53 C ATOM 279 O ALA A 34 17.664 34.030 38.093 1.00 14.83 O ANISOU 279 O ALA A 34 2118 1671 1843 83 -45 -33 O ATOM 280 CB ALA A 34 17.775 32.861 34.968 1.00 15.72 C ANISOU 280 CB ALA A 34 2108 1700 2162 277 -3 29 C ATOM 281 N VAL A 35 16.773 31.996 37.742 1.00 14.41 N ANISOU 281 N VAL A 35 1957 1550 1965 34 32 -105 N ATOM 282 CA VAL A 35 15.874 32.089 38.890 1.00 15.13 C ANISOU 282 CA VAL A 35 1950 1748 2049 182 101 -31 C ATOM 283 C VAL A 35 16.681 32.302 40.170 1.00 14.25 C ANISOU 283 C VAL A 35 1953 1587 1872 105 233 -93 C ATOM 284 O VAL A 35 16.352 33.135 41.011 1.00 14.77 O ANISOU 284 O VAL A 35 2087 1613 1910 64 110 -76 O ATOM 285 CB VAL A 35 14.960 30.857 38.975 1.00 16.08 C ANISOU 285 CB VAL A 35 2078 1805 2225 39 117 -132 C ATOM 286 CG1 VAL A 35 14.191 30.834 40.283 1.00 15.81 C ANISOU 286 CG1 VAL A 35 1987 1820 2200 -22 116 -152 C ATOM 287 CG2 VAL A 35 13.986 30.837 37.784 1.00 16.71 C ANISOU 287 CG2 VAL A 35 2111 1811 2426 140 94 -270 C ATOM 288 N CYS A 36 17.728 31.519 40.350 1.00 14.72 N ANISOU 288 N CYS A 36 2076 1587 1928 129 95 -65 N ATOM 289 CA CYS A 36 18.493 31.584 41.572 1.00 14.80 C ANISOU 289 CA CYS A 36 2053 1605 1966 99 124 77 C ATOM 290 C CYS A 36 19.198 32.922 41.738 1.00 14.08 C ANISOU 290 C CYS A 36 1850 1673 1825 156 116 34 C ATOM 291 O CYS A 36 19.233 33.483 42.820 1.00 14.96 O ANISOU 291 O CYS A 36 2182 1599 1902 34 -64 46 O ATOM 292 CB CYS A 36 19.438 30.407 41.662 1.00 16.42 C ANISOU 292 CB CYS A 36 2359 1723 2154 146 14 115 C ATOM 293 SG ACYS A 36 19.906 30.104 43.368 0.50 14.25 S ANISOU 293 SG ACYS A 36 1765 1711 1937 17 139 214 S ATOM 294 SG BCYS A 36 20.676 30.314 43.012 0.50 20.82 S ANISOU 294 SG BCYS A 36 2903 2488 2519 347 -270 192 S ATOM 295 N ASN A 37 19.734 33.455 40.646 1.00 14.14 N ANISOU 295 N ASN A 37 1951 1726 1693 115 96 15 N ATOM 296 CA ASN A 37 20.324 34.778 40.700 1.00 13.56 C ANISOU 296 CA ASN A 37 1695 1691 1766 63 -19 67 C ATOM 297 C ASN A 37 19.322 35.840 41.135 1.00 13.47 C ANISOU 297 C ASN A 37 1909 1541 1668 118 -79 173 C ATOM 298 O ASN A 37 19.642 36.704 41.959 1.00 13.62 O ANISOU 298 O ASN A 37 1829 1668 1676 80 -106 75 O ATOM 299 CB ASN A 37 20.921 35.134 39.361 1.00 15.38 C ANISOU 299 CB ASN A 37 1925 1887 2031 130 -41 189 C ATOM 300 CG ASN A 37 22.206 34.346 39.052 1.00 17.72 C ANISOU 300 CG ASN A 37 2305 2173 2254 188 55 92 C ATOM 301 OD1 ASN A 37 22.804 33.758 39.944 1.00 20.53 O ANISOU 301 OD1 ASN A 37 2152 2687 2961 340 161 470 O ATOM 302 ND2 ASN A 37 22.637 34.379 37.809 1.00 18.42 N ANISOU 302 ND2 ASN A 37 2325 2218 2455 96 350 63 N ATOM 303 N VAL A 38 18.091 35.760 40.630 1.00 13.53 N ANISOU 303 N VAL A 38 1836 1583 1718 38 -114 1 N ATOM 304 CA VAL A 38 17.060 36.720 40.997 1.00 13.34 C ANISOU 304 CA VAL A 38 1838 1577 1654 23 -108 86 C ATOM 305 C VAL A 38 16.632 36.519 42.450 1.00 13.41 C ANISOU 305 C VAL A 38 1809 1487 1798 4 -106 100 C ATOM 306 O VAL A 38 16.427 37.494 43.154 1.00 14.35 O ANISOU 306 O VAL A 38 2137 1493 1821 -5 2 44 O ATOM 307 CB VAL A 38 15.913 36.641 39.987 1.00 13.41 C ANISOU 307 CB VAL A 38 1767 1653 1672 17 -126 20 C ATOM 308 CG1 VAL A 38 14.730 37.469 40.425 1.00 15.15 C ANISOU 308 CG1 VAL A 38 2204 1842 1709 171 -131 -40 C ATOM 309 CG2 VAL A 38 16.412 37.059 38.610 1.00 14.36 C ANISOU 309 CG2 VAL A 38 1947 1852 1654 65 -208 -42 C ATOM 310 N VAL A 39 16.466 35.270 42.890 1.00 13.96 N ANISOU 310 N VAL A 39 1944 1535 1824 45 -19 57 N ATOM 311 CA VAL A 39 16.098 35.004 44.286 1.00 14.24 C ANISOU 311 CA VAL A 39 2015 1603 1789 -4 108 77 C ATOM 312 C VAL A 39 17.199 35.462 45.211 1.00 14.52 C ANISOU 312 C VAL A 39 2138 1511 1865 200 103 160 C ATOM 313 O VAL A 39 16.914 36.000 46.286 1.00 15.90 O ANISOU 313 O VAL A 39 2571 1794 1673 108 97 21 O ATOM 314 CB VAL A 39 15.784 33.529 44.473 1.00 15.36 C ANISOU 314 CB VAL A 39 2146 1594 2094 96 280 66 C ATOM 315 CG1 VAL A 39 15.774 33.158 45.924 1.00 16.84 C ANISOU 315 CG1 VAL A 39 2622 1623 2152 60 267 293 C ATOM 316 CG2 VAL A 39 14.471 33.154 43.809 1.00 16.27 C ANISOU 316 CG2 VAL A 39 2151 1707 2324 -56 340 -1 C ATOM 317 N LYS A 40 18.454 35.231 44.860 1.00 15.05 N ANISOU 317 N LYS A 40 2273 1644 1799 143 -120 -15 N ATOM 318 CA LYS A 40 19.524 35.709 45.738 1.00 16.53 C ANISOU 318 CA LYS A 40 2402 1964 1914 3 -69 126 C ATOM 319 C LYS A 40 19.510 37.213 45.828 1.00 15.37 C ANISOU 319 C LYS A 40 2314 1757 1767 -60 -210 39 C ATOM 320 O LYS A 40 19.831 37.769 46.869 1.00 17.00 O ANISOU 320 O LYS A 40 2881 1792 1785 -195 -153 49 O ATOM 321 CB LYS A 40 20.887 35.195 45.281 1.00 17.35 C ANISOU 321 CB LYS A 40 2469 2100 2023 46 -248 -2 C ATOM 322 CG LYS A 40 21.092 33.696 45.454 1.00 20.50 C ANISOU 322 CG LYS A 40 3000 2466 2320 256 -325 279 C ATOM 323 CD LYS A 40 22.444 33.288 44.898 1.00 24.16 C ANISOU 323 CD LYS A 40 3110 3121 2946 207 -177 27 C ATOM 324 CE LYS A 40 22.797 31.868 45.206 1.00 28.19 C ANISOU 324 CE LYS A 40 3662 3382 3665 296 -167 90 C ATOM 325 NZ LYS A 40 23.869 31.380 44.265 1.00 29.76 N ANISOU 325 NZ LYS A 40 3640 3737 3929 362 -48 -4 N ATOM 326 N ARG A 41 19.234 37.901 44.738 1.00 13.77 N ANISOU 326 N ARG A 41 1989 1653 1587 62 -21 141 N ATOM 327 CA ARG A 41 19.227 39.356 44.734 1.00 14.57 C ANISOU 327 CA ARG A 41 2016 1776 1741 -8 -144 69 C ATOM 328 C ARG A 41 18.025 39.926 45.503 1.00 15.01 C ANISOU 328 C ARG A 41 2175 1721 1807 -140 -63 57 C ATOM 329 O ARG A 41 18.169 40.923 46.223 1.00 16.55 O ANISOU 329 O ARG A 41 2447 1827 2014 -267 -65 -127 O ATOM 330 CB ARG A 41 19.232 39.896 43.276 1.00 14.18 C ANISOU 330 CB ARG A 41 1946 1729 1712 -69 -20 146 C ATOM 331 CG ARG A 41 19.074 41.409 43.207 1.00 15.11 C ANISOU 331 CG ARG A 41 2080 1836 1823 4 -144 99 C ATOM 332 CD ARG A 41 20.197 42.148 43.866 1.00 16.01 C ANISOU 332 CD ARG A 41 2064 1769 2247 -232 -247 185 C ATOM 333 NE ARG A 41 20.061 43.587 43.690 1.00 17.64 N ANISOU 333 NE ARG A 41 2589 1677 2434 -149 -28 205 N ATOM 334 CZ ARG A 41 19.227 44.346 44.377 1.00 17.88 C ANISOU 334 CZ ARG A 41 2540 1723 2529 -171 -147 -147 C ATOM 335 NH1 ARG A 41 18.441 43.834 45.325 1.00 20.80 N ANISOU 335 NH1 ARG A 41 3166 2118 2616 87 -5 -220 N ATOM 336 NH2 ARG A 41 19.147 45.637 44.108 1.00 20.16 N ANISOU 336 NH2 ARG A 41 2887 1949 2820 196 -59 147 N ATOM 337 N HIS A 42 16.844 39.346 45.298 1.00 13.79 N ANISOU 337 N HIS A 42 1978 1607 1655 -120 -1 123 N ATOM 338 CA HIS A 42 15.597 39.952 45.757 1.00 14.56 C ANISOU 338 CA HIS A 42 2112 1657 1760 -36 4 97 C ATOM 339 C HIS A 42 14.905 39.278 46.918 1.00 14.90 C ANISOU 339 C HIS A 42 2041 1813 1804 -65 -15 127 C ATOM 340 O HIS A 42 13.930 39.828 47.425 1.00 16.33 O ANISOU 340 O HIS A 42 2377 2019 1805 79 182 81 O ATOM 341 CB HIS A 42 14.629 40.100 44.585 1.00 14.84 C ANISOU 341 CB HIS A 42 1959 1836 1842 80 37 60 C ATOM 342 CG HIS A 42 15.095 41.133 43.620 1.00 14.18 C ANISOU 342 CG HIS A 42 1783 1879 1726 238 -109 77 C ATOM 343 ND1 HIS A 42 15.106 42.475 43.939 1.00 17.62 N ANISOU 343 ND1 HIS A 42 2772 1871 2052 390 316 208 N ATOM 344 CD2 HIS A 42 15.599 41.030 42.365 1.00 15.23 C ANISOU 344 CD2 HIS A 42 2041 2064 1680 135 -104 86 C ATOM 345 CE1 HIS A 42 15.595 43.151 42.920 1.00 17.82 C ANISOU 345 CE1 HIS A 42 2595 1874 2300 75 181 300 C ATOM 346 NE2 HIS A 42 15.918 42.308 41.959 1.00 16.29 N ANISOU 346 NE2 HIS A 42 1925 2228 2034 230 39 345 N ATOM 347 N GLY A 43 15.402 38.113 47.324 1.00 14.47 N ANISOU 347 N GLY A 43 1957 1815 1723 49 -3 164 N ATOM 348 CA GLY A 43 14.788 37.313 48.361 1.00 14.36 C ANISOU 348 CA GLY A 43 1979 1819 1656 -30 -46 191 C ATOM 349 C GLY A 43 13.727 36.400 47.797 1.00 14.44 C ANISOU 349 C GLY A 43 2133 1663 1687 61 -17 48 C ATOM 350 O GLY A 43 13.320 36.489 46.634 1.00 15.30 O ANISOU 350 O GLY A 43 2157 1958 1698 -129 -120 176 O ATOM 351 N GLU A 44 13.250 35.502 48.651 1.00 15.04 N ANISOU 351 N GLU A 44 2144 1806 1763 -87 -159 81 N ATOM 352 CA GLU A 44 12.352 34.463 48.222 1.00 14.84 C ANISOU 352 CA GLU A 44 2055 1674 1910 -40 -85 78 C ATOM 353 C GLU A 44 11.031 35.006 47.712 1.00 14.68 C ANISOU 353 C GLU A 44 2196 1559 1823 -23 -11 89 C ATOM 354 O GLU A 44 10.522 34.541 46.681 1.00 14.86 O ANISOU 354 O GLU A 44 2071 1880 1693 -63 -86 -34 O ATOM 355 CB GLU A 44 12.090 33.515 49.384 1.00 15.93 C ANISOU 355 CB GLU A 44 2167 1832 2053 -182 -46 184 C ATOM 356 CG GLU A 44 11.158 32.363 49.051 1.00 16.88 C ANISOU 356 CG GLU A 44 2467 1852 2094 -15 -268 204 C ATOM 357 CD GLU A 44 11.066 31.337 50.132 1.00 16.17 C ANISOU 357 CD GLU A 44 1967 1966 2210 -113 -4 184 C ATOM 358 OE1 GLU A 44 12.138 30.861 50.530 1.00 16.76 O ANISOU 358 OE1 GLU A 44 2508 1789 2070 12 81 331 O ATOM 359 OE2 GLU A 44 9.943 30.990 50.529 1.00 18.87 O ANISOU 359 OE2 GLU A 44 2227 2166 2773 -5 -76 404 O ATOM 360 N THR A 45 10.420 35.924 48.425 1.00 14.60 N ANISOU 360 N THR A 45 2244 1703 1597 -56 62 40 N ATOM 361 CA THR A 45 9.069 36.307 48.067 1.00 15.91 C ANISOU 361 CA THR A 45 2199 1944 1900 -110 183 40 C ATOM 362 C THR A 45 9.063 37.099 46.751 1.00 14.75 C ANISOU 362 C THR A 45 2175 1683 1744 -140 53 -72 C ATOM 363 O THR A 45 8.363 36.767 45.819 1.00 15.34 O ANISOU 363 O THR A 45 2101 1878 1846 -120 30 -11 O ATOM 364 CB THR A 45 8.310 36.967 49.195 1.00 17.44 C ANISOU 364 CB THR A 45 2312 2381 1932 -47 217 3 C ATOM 365 OG1ATHR A 45 8.679 38.315 49.320 0.50 21.21 O ANISOU 365 OG1ATHR A 45 3205 2746 2107 -278 372 41 O ATOM 366 OG1BTHR A 45 8.163 36.133 50.357 0.50 17.90 O ANISOU 366 OG1BTHR A 45 2532 2530 1739 111 248 47 O ATOM 367 CG2ATHR A 45 8.621 36.312 50.532 0.50 16.29 C ANISOU 367 CG2ATHR A 45 1786 2522 1881 -178 -101 -91 C ATOM 368 CG2BTHR A 45 7.068 37.751 48.867 0.50 17.20 C ANISOU 368 CG2BTHR A 45 2266 2629 1638 136 135 -84 C ATOM 369 N VAL A 46 9.850 38.149 46.652 1.00 13.95 N ANISOU 369 N VAL A 46 2108 1590 1603 -68 -38 -32 N ATOM 370 CA VAL A 46 9.903 38.936 45.431 1.00 13.99 C ANISOU 370 CA VAL A 46 1993 1675 1647 -106 -100 -20 C ATOM 371 C VAL A 46 10.493 38.104 44.304 1.00 13.61 C ANISOU 371 C VAL A 46 1826 1644 1701 -65 87 -2 C ATOM 372 O VAL A 46 9.973 38.124 43.199 1.00 13.77 O ANISOU 372 O VAL A 46 1966 1639 1626 -51 -114 -36 O ATOM 373 CB VAL A 46 10.725 40.231 45.681 1.00 14.43 C ANISOU 373 CB VAL A 46 2148 1710 1625 -80 -30 66 C ATOM 374 CG1 VAL A 46 11.013 40.930 44.346 1.00 15.19 C ANISOU 374 CG1 VAL A 46 2276 1691 1804 -118 -91 -16 C ATOM 375 CG2 VAL A 46 9.984 41.146 46.640 1.00 16.38 C ANISOU 375 CG2 VAL A 46 2508 1824 1890 -24 -9 -134 C ATOM 376 N GLY A 47 11.574 37.380 44.569 1.00 13.83 N ANISOU 376 N GLY A 47 1972 1647 1636 -81 -38 -116 N ATOM 377 CA GLY A 47 12.194 36.591 43.509 1.00 13.55 C ANISOU 377 CA GLY A 47 1791 1609 1746 -90 20 -21 C ATOM 378 C GLY A 47 11.297 35.522 42.966 1.00 13.52 C ANISOU 378 C GLY A 47 1761 1740 1635 143 17 -76 C ATOM 379 O GLY A 47 11.263 35.286 41.749 1.00 14.19 O ANISOU 379 O GLY A 47 1882 1832 1676 88 20 -113 O ATOM 380 N SER A 48 10.572 34.821 43.847 1.00 13.78 N ANISOU 380 N SER A 48 1885 1746 1604 -33 -73 -71 N ATOM 381 CA SER A 48 9.634 33.798 43.372 1.00 13.94 C ANISOU 381 CA SER A 48 1946 1498 1850 70 19 -45 C ATOM 382 C SER A 48 8.519 34.389 42.556 1.00 13.32 C ANISOU 382 C SER A 48 1777 1497 1785 137 -33 -20 C ATOM 383 O SER A 48 8.085 33.778 41.569 1.00 14.29 O ANISOU 383 O SER A 48 1961 1548 1920 -54 -139 -61 O ATOM 384 CB SER A 48 9.110 32.951 44.506 1.00 15.17 C ANISOU 384 CB SER A 48 2214 1699 1848 -157 -35 9 C ATOM 385 OG ASER A 48 8.201 33.614 45.338 0.75 15.84 O ANISOU 385 OG ASER A 48 2375 1807 1836 -421 134 -131 O ATOM 386 OG BSER A 48 9.998 32.335 45.372 0.25 15.49 O ANISOU 386 OG BSER A 48 2266 1692 1924 227 -79 -57 O ATOM 387 N ARG A 49 8.023 35.571 42.958 1.00 13.36 N ANISOU 387 N ARG A 49 1724 1580 1770 23 -92 -96 N ATOM 388 CA ARG A 49 6.972 36.226 42.162 1.00 13.17 C ANISOU 388 CA ARG A 49 1735 1511 1758 -22 -53 -59 C ATOM 389 C ARG A 49 7.483 36.637 40.785 1.00 13.22 C ANISOU 389 C ARG A 49 1840 1558 1625 123 1 -137 C ATOM 390 O ARG A 49 6.790 36.436 39.784 1.00 13.54 O ANISOU 390 O ARG A 49 1720 1636 1788 77 -10 -115 O ATOM 391 CB ARG A 49 6.419 37.412 42.920 1.00 13.65 C ANISOU 391 CB ARG A 49 1790 1484 1910 117 48 8 C ATOM 392 CG ARG A 49 5.558 37.016 44.106 1.00 15.68 C ANISOU 392 CG ARG A 49 2153 1894 1907 116 194 56 C ATOM 393 CD ARG A 49 5.210 38.194 44.994 1.00 16.66 C ANISOU 393 CD ARG A 49 2316 2050 1962 156 361 -50 C ATOM 394 NE ARG A 49 4.312 39.115 44.321 1.00 16.21 N ANISOU 394 NE ARG A 49 2117 2008 2032 397 270 -103 N ATOM 395 CZ ARG A 49 3.965 40.306 44.753 1.00 18.31 C ANISOU 395 CZ ARG A 49 2300 2320 2335 557 46 -220 C ATOM 396 NH1 ARG A 49 4.458 40.810 45.861 1.00 20.55 N ANISOU 396 NH1 ARG A 49 2587 2586 2635 209 -44 -546 N ATOM 397 NH2 ARG A 49 3.138 41.045 44.031 1.00 18.81 N ANISOU 397 NH2 ARG A 49 2334 2163 2648 374 -311 -426 N ATOM 398 N LEU A 50 8.704 37.202 40.719 1.00 12.65 N ANISOU 398 N LEU A 50 1680 1514 1609 49 -51 -45 N ATOM 399 CA LEU A 50 9.242 37.572 39.424 1.00 13.49 C ANISOU 399 CA LEU A 50 1825 1599 1701 -41 -60 -146 C ATOM 400 C LEU A 50 9.427 36.354 38.535 1.00 12.51 C ANISOU 400 C LEU A 50 1571 1547 1632 -33 11 -86 C ATOM 401 O LEU A 50 9.098 36.373 37.345 1.00 13.53 O ANISOU 401 O LEU A 50 1815 1724 1602 -81 3 -200 O ATOM 402 CB LEU A 50 10.580 38.297 39.612 1.00 13.28 C ANISOU 402 CB LEU A 50 1872 1624 1550 10 7 -60 C ATOM 403 CG LEU A 50 10.492 39.684 40.250 1.00 13.31 C ANISOU 403 CG LEU A 50 1839 1644 1575 -169 56 -14 C ATOM 404 CD1 LEU A 50 11.886 40.137 40.630 1.00 14.41 C ANISOU 404 CD1 LEU A 50 1979 1703 1793 -160 174 50 C ATOM 405 CD2 LEU A 50 9.836 40.699 39.335 1.00 14.51 C ANISOU 405 CD2 LEU A 50 2010 1720 1783 34 27 -163 C ATOM 406 N ALA A 51 9.958 35.269 39.091 1.00 13.39 N ANISOU 406 N ALA A 51 1864 1532 1691 33 3 -199 N ATOM 407 CA ALA A 51 10.164 34.051 38.325 1.00 13.45 C ANISOU 407 CA ALA A 51 1754 1551 1804 43 23 -214 C ATOM 408 C ALA A 51 8.845 33.471 37.851 1.00 13.32 C ANISOU 408 C ALA A 51 1764 1487 1809 69 -5 -184 C ATOM 409 O ALA A 51 8.741 33.008 36.730 1.00 13.90 O ANISOU 409 O ALA A 51 1773 1652 1854 81 -20 -261 O ATOM 410 CB ALA A 51 10.919 33.054 39.148 1.00 14.37 C ANISOU 410 CB ALA A 51 1781 1639 2038 26 -88 -317 C ATOM 411 N MET A 52 7.838 33.461 38.716 1.00 13.21 N ANISOU 411 N MET A 52 1756 1521 1739 19 -28 -110 N ATOM 412 CA MET A 52 6.494 33.010 38.377 1.00 13.34 C ANISOU 412 CA MET A 52 1738 1504 1825 -104 22 -116 C ATOM 413 C MET A 52 5.936 33.786 37.202 1.00 12.78 C ANISOU 413 C MET A 52 1664 1488 1704 -79 101 -228 C ATOM 414 O MET A 52 5.425 33.208 36.255 1.00 13.27 O ANISOU 414 O MET A 52 1808 1618 1615 -66 26 -198 O ATOM 415 CB MET A 52 5.595 33.194 39.599 1.00 13.28 C ANISOU 415 CB MET A 52 1643 1603 1797 1 20 -113 C ATOM 416 CG MET A 52 4.184 32.688 39.404 1.00 14.19 C ANISOU 416 CG MET A 52 1879 1730 1782 -58 136 -108 C ATOM 417 SD MET A 52 3.074 33.134 40.744 1.00 14.72 S ANISOU 417 SD MET A 52 1830 1834 1929 -114 142 -231 S ATOM 418 CE MET A 52 2.920 34.892 40.497 1.00 15.34 C ANISOU 418 CE MET A 52 1934 1946 1947 78 143 -115 C ATOM 419 N LEU A 53 5.983 35.121 37.300 1.00 12.86 N ANISOU 419 N LEU A 53 1699 1551 1635 -25 -38 -209 N ATOM 420 CA LEU A 53 5.431 35.953 36.217 1.00 13.24 C ANISOU 420 CA LEU A 53 1720 1576 1733 -5 28 -171 C ATOM 421 C LEU A 53 6.183 35.685 34.926 1.00 13.30 C ANISOU 421 C LEU A 53 1709 1639 1703 -50 45 -79 C ATOM 422 O LEU A 53 5.575 35.604 33.855 1.00 13.86 O ANISOU 422 O LEU A 53 1774 1740 1750 -122 -6 -122 O ATOM 423 CB LEU A 53 5.484 37.425 36.598 1.00 13.92 C ANISOU 423 CB LEU A 53 1738 1662 1887 -93 156 -59 C ATOM 424 CG LEU A 53 4.571 37.808 37.782 1.00 13.54 C ANISOU 424 CG LEU A 53 1597 1726 1819 -15 -59 -101 C ATOM 425 CD1 LEU A 53 4.829 39.212 38.266 1.00 15.22 C ANISOU 425 CD1 LEU A 53 1982 1697 2102 -133 286 -297 C ATOM 426 CD2 LEU A 53 3.096 37.633 37.448 1.00 16.40 C ANISOU 426 CD2 LEU A 53 1842 1976 2413 64 -103 -225 C ATOM 427 N ASN A 54 7.511 35.538 34.996 1.00 13.13 N ANISOU 427 N ASN A 54 1831 1568 1590 4 -85 -204 N ATOM 428 CA ASN A 54 8.260 35.230 33.778 1.00 13.61 C ANISOU 428 CA ASN A 54 1805 1696 1670 -13 2 -267 C ATOM 429 C ASN A 54 7.853 33.896 33.169 1.00 13.83 C ANISOU 429 C ASN A 54 1789 1739 1724 -41 187 -192 C ATOM 430 O ASN A 54 7.731 33.766 31.956 1.00 14.99 O ANISOU 430 O ASN A 54 2292 1694 1708 -169 157 -356 O ATOM 431 CB ASN A 54 9.768 35.273 34.034 1.00 14.16 C ANISOU 431 CB ASN A 54 1902 1722 1754 17 140 -210 C ATOM 432 CG ASN A 54 10.544 35.493 32.769 1.00 13.48 C ANISOU 432 CG ASN A 54 2004 1509 1606 -240 36 -173 C ATOM 433 OD1 ASN A 54 10.336 36.514 32.119 1.00 14.69 O ANISOU 433 OD1 ASN A 54 2011 1666 1901 -62 169 -173 O ATOM 434 ND2 ASN A 54 11.428 34.555 32.407 1.00 14.54 N ANISOU 434 ND2 ASN A 54 1967 1710 1846 -29 -2 -296 N ATOM 435 N ALA A 55 7.653 32.898 34.016 1.00 13.37 N ANISOU 435 N ALA A 55 1744 1609 1725 -30 5 -210 N ATOM 436 CA ALA A 55 7.203 31.599 33.548 1.00 14.27 C ANISOU 436 CA ALA A 55 1813 1719 1887 23 -32 -266 C ATOM 437 C ALA A 55 5.824 31.662 32.903 1.00 14.13 C ANISOU 437 C ALA A 55 1844 1716 1807 -120 117 -131 C ATOM 438 O ALA A 55 5.568 31.033 31.871 1.00 14.44 O ANISOU 438 O ALA A 55 1864 1854 1768 -113 29 -292 O ATOM 439 CB ALA A 55 7.228 30.583 34.659 1.00 14.54 C ANISOU 439 CB ALA A 55 1816 1664 2043 44 43 -136 C ATOM 440 N LEU A 56 4.921 32.448 33.479 1.00 13.85 N ANISOU 440 N LEU A 56 1743 1831 1685 -72 23 -247 N ATOM 441 CA LEU A 56 3.561 32.567 32.969 1.00 14.41 C ANISOU 441 CA LEU A 56 1713 1987 1773 -93 -69 -167 C ATOM 442 C LEU A 56 3.516 33.167 31.586 1.00 14.30 C ANISOU 442 C LEU A 56 1716 1896 1820 -94 -18 -21 C ATOM 443 O LEU A 56 2.534 32.934 30.884 1.00 15.54 O ANISOU 443 O LEU A 56 1748 2277 1877 -205 -67 -137 O ATOM 444 CB LEU A 56 2.714 33.386 33.938 1.00 14.37 C ANISOU 444 CB LEU A 56 1679 1881 1898 -55 48 -256 C ATOM 445 CG LEU A 56 2.344 32.667 35.233 1.00 14.75 C ANISOU 445 CG LEU A 56 1737 1926 1941 -76 145 -103 C ATOM 446 CD1 LEU A 56 1.659 33.600 36.201 1.00 16.11 C ANISOU 446 CD1 LEU A 56 1982 2163 1975 -238 210 -246 C ATOM 447 CD2 LEU A 56 1.445 31.446 35.003 1.00 15.51 C ANISOU 447 CD2 LEU A 56 1802 2059 2031 93 127 -70 C ATOM 448 N ILE A 57 4.499 33.959 31.209 1.00 14.85 N ANISOU 448 N ILE A 57 1764 2048 1828 -169 -113 -35 N ATOM 449 CA ILE A 57 4.544 34.543 29.890 1.00 15.15 C ANISOU 449 CA ILE A 57 1807 2174 1772 -246 -184 -36 C ATOM 450 C ILE A 57 5.612 33.934 28.987 1.00 15.06 C ANISOU 450 C ILE A 57 1968 2017 1736 -241 -80 -40 C ATOM 451 O ILE A 57 5.948 34.486 27.937 1.00 15.85 O ANISOU 451 O ILE A 57 2080 2232 1709 -244 -25 -81 O ATOM 452 CB ILE A 57 4.611 36.083 29.919 1.00 16.39 C ANISOU 452 CB ILE A 57 2224 2129 1874 -141 -189 156 C ATOM 453 CG1 ILE A 57 5.877 36.588 30.596 1.00 18.56 C ANISOU 453 CG1 ILE A 57 2620 2376 2054 -264 -158 254 C ATOM 454 CG2 ILE A 57 3.342 36.661 30.577 1.00 18.20 C ANISOU 454 CG2 ILE A 57 2485 2274 2154 -37 201 140 C ATOM 455 CD1 ILE A 57 6.164 37.951 30.375 1.00 20.17 C ANISOU 455 CD1 ILE A 57 2553 2519 2592 -154 49 -128 C ATOM 456 N SER A 58 6.096 32.745 29.353 1.00 15.34 N ANISOU 456 N SER A 58 2026 2028 1775 -176 37 -103 N ATOM 457 CA SER A 58 7.114 32.030 28.564 1.00 16.15 C ANISOU 457 CA SER A 58 2146 2169 1819 -115 -61 -136 C ATOM 458 C SER A 58 6.472 31.168 27.468 1.00 17.49 C ANISOU 458 C SER A 58 2389 2078 2177 -172 -167 -118 C ATOM 459 O SER A 58 6.440 29.943 27.529 1.00 20.85 O ANISOU 459 O SER A 58 3156 2344 2422 -230 -326 -148 O ATOM 460 CB SER A 58 8.009 31.200 29.454 1.00 16.67 C ANISOU 460 CB SER A 58 2326 2242 1766 59 87 -170 C ATOM 461 OG SER A 58 8.810 31.989 30.289 1.00 17.79 O ANISOU 461 OG SER A 58 2233 2559 1967 -6 -48 -180 O ATOM 462 N TYR A 59 5.860 31.845 26.521 1.00 17.37 N ANISOU 462 N TYR A 59 2510 1939 2150 -135 -213 -325 N ATOM 463 CA TYR A 59 5.171 31.225 25.376 1.00 17.69 C ANISOU 463 CA TYR A 59 2316 2247 2156 -322 -170 -300 C ATOM 464 C TYR A 59 5.378 32.116 24.155 1.00 16.70 C ANISOU 464 C TYR A 59 2359 1927 2057 -189 -129 -310 C ATOM 465 O TYR A 59 5.627 33.289 24.289 1.00 17.22 O ANISOU 465 O TYR A 59 2431 2095 2014 -271 -149 -231 O ATOM 466 CB TYR A 59 3.665 31.020 25.670 1.00 18.60 C ANISOU 466 CB TYR A 59 2434 2211 2422 -514 -129 -209 C ATOM 467 CG TYR A 59 2.911 32.293 25.861 1.00 18.26 C ANISOU 467 CG TYR A 59 2233 2444 2262 -395 -206 -88 C ATOM 468 CD1 TYR A 59 2.449 33.008 24.773 1.00 19.64 C ANISOU 468 CD1 TYR A 59 2590 2848 2024 -233 -169 -119 C ATOM 469 CD2 TYR A 59 2.647 32.795 27.122 1.00 17.66 C ANISOU 469 CD2 TYR A 59 2142 2565 2000 -502 -278 -27 C ATOM 470 CE1 TYR A 59 1.747 34.187 24.936 1.00 20.37 C ANISOU 470 CE1 TYR A 59 2668 2640 2430 -166 -279 -14 C ATOM 471 CE2 TYR A 59 1.954 33.982 27.297 1.00 19.00 C ANISOU 471 CE2 TYR A 59 2234 2482 2502 -322 -191 -101 C ATOM 472 CZ TYR A 59 1.510 34.689 26.210 1.00 19.15 C ANISOU 472 CZ TYR A 59 2296 2456 2524 -272 -110 -77 C ATOM 473 OH TYR A 59 0.810 35.873 26.406 1.00 21.10 O ANISOU 473 OH TYR A 59 2288 2726 3003 -76 -188 -42 O ATOM 474 N ARG A 60 5.223 31.531 22.964 1.00 16.96 N ANISOU 474 N ARG A 60 2371 2016 2056 -399 -106 -284 N ATOM 475 CA ARG A 60 5.381 32.271 21.707 1.00 18.35 C ANISOU 475 CA ARG A 60 2481 2273 2215 -275 -35 -264 C ATOM 476 C ARG A 60 6.648 33.114 21.687 1.00 16.66 C ANISOU 476 C ARG A 60 2295 2090 1943 -211 -128 -172 C ATOM 477 O ARG A 60 6.612 34.327 21.477 1.00 18.24 O ANISOU 477 O ARG A 60 2580 2305 2045 -323 -354 -169 O ATOM 478 CB ARG A 60 4.138 33.102 21.407 1.00 18.95 C ANISOU 478 CB ARG A 60 2561 2601 2038 -247 -139 -33 C ATOM 479 CG ARG A 60 2.944 32.221 21.059 1.00 21.94 C ANISOU 479 CG ARG A 60 2782 2776 2775 -331 -32 -307 C ATOM 480 CD ARG A 60 1.766 32.964 20.543 1.00 24.96 C ANISOU 480 CD ARG A 60 3122 3089 3270 -140 -120 -87 C ATOM 481 NE ARG A 60 2.069 33.460 19.204 1.00 29.06 N ANISOU 481 NE ARG A 60 3721 3678 3639 -168 -12 72 N ATOM 482 CZ ARG A 60 1.459 34.479 18.619 1.00 30.70 C ANISOU 482 CZ ARG A 60 3880 3808 3973 -20 1 99 C ATOM 483 NH1 ARG A 60 0.501 35.156 19.248 1.00 33.40 N ANISOU 483 NH1 ARG A 60 4105 4206 4380 76 162 -46 N ATOM 484 NH2 ARG A 60 1.815 34.836 17.389 1.00 31.28 N ANISOU 484 NH2 ARG A 60 3942 4012 3931 58 16 20 N ATOM 485 N LEU A 61 7.745 32.420 21.939 1.00 16.33 N ANISOU 485 N LEU A 61 2232 2029 1943 -250 95 -358 N ATOM 486 CA LEU A 61 9.064 33.004 22.077 1.00 17.36 C ANISOU 486 CA LEU A 61 2201 2321 2073 -275 81 -426 C ATOM 487 C LEU A 61 9.923 32.832 20.814 1.00 17.21 C ANISOU 487 C LEU A 61 2273 2226 2037 -240 49 -332 C ATOM 488 O LEU A 61 11.095 33.180 20.835 1.00 18.28 O ANISOU 488 O LEU A 61 2181 2665 2100 -361 155 -481 O ATOM 489 CB LEU A 61 9.829 32.412 23.270 1.00 18.19 C ANISOU 489 CB LEU A 61 2409 2317 2185 -183 9 -528 C ATOM 490 CG LEU A 61 9.163 32.641 24.621 1.00 18.37 C ANISOU 490 CG LEU A 61 2477 2382 2119 -370 95 -373 C ATOM 491 CD1 LEU A 61 9.966 31.966 25.744 1.00 20.19 C ANISOU 491 CD1 LEU A 61 2821 2480 2369 -167 40 -359 C ATOM 492 CD2 LEU A 61 8.952 34.074 24.929 1.00 18.78 C ANISOU 492 CD2 LEU A 61 2389 2438 2306 -268 118 -541 C ATOM 493 N THR A 62 9.381 32.268 19.730 1.00 18.49 N ANISOU 493 N THR A 62 2346 2514 2164 -215 93 -548 N ATOM 494 CA THR A 62 10.082 32.203 18.446 1.00 18.54 C ANISOU 494 CA THR A 62 2410 2575 2059 -66 -13 -418 C ATOM 495 C THR A 62 11.474 31.586 18.617 1.00 17.17 C ANISOU 495 C THR A 62 2363 2456 1702 -142 -10 -511 C ATOM 496 O THR A 62 12.461 32.061 18.053 1.00 19.09 O ANISOU 496 O THR A 62 2307 2770 2176 -275 -206 -368 O ATOM 497 CB THR A 62 10.185 33.603 17.871 1.00 21.50 C ANISOU 497 CB THR A 62 2631 2962 2576 107 -2 -181 C ATOM 498 OG1 THR A 62 8.914 34.267 17.948 1.00 25.57 O ANISOU 498 OG1 THR A 62 2741 3644 3329 386 175 -284 O ATOM 499 CG2 THR A 62 10.469 33.581 16.398 1.00 23.62 C ANISOU 499 CG2 THR A 62 2894 3212 2869 36 83 -232 C ATOM 500 N GLY A 63 11.538 30.523 19.385 1.00 18.30 N ANISOU 500 N GLY A 63 2484 2208 2261 -269 -63 -532 N ATOM 501 CA GLY A 63 12.756 29.766 19.569 1.00 19.07 C ANISOU 501 CA GLY A 63 2606 2232 2405 -174 -222 -460 C ATOM 502 C GLY A 63 13.777 30.326 20.547 1.00 19.51 C ANISOU 502 C GLY A 63 2724 2319 2367 -27 -238 -501 C ATOM 503 O GLY A 63 14.888 29.796 20.654 1.00 22.21 O ANISOU 503 O GLY A 63 3011 2645 2782 140 -410 -768 O ATOM 504 N LYS A 64 13.406 31.362 21.292 1.00 17.94 N ANISOU 504 N LYS A 64 2605 2136 2074 -21 -269 -560 N ATOM 505 CA LYS A 64 14.377 32.081 22.120 1.00 19.62 C ANISOU 505 CA LYS A 64 2714 2305 2432 -100 -237 -401 C ATOM 506 C LYS A 64 14.179 31.848 23.617 1.00 18.67 C ANISOU 506 C LYS A 64 2766 2155 2170 -47 -191 -408 C ATOM 507 O LYS A 64 14.578 32.684 24.443 1.00 19.17 O ANISOU 507 O LYS A 64 2937 2316 2027 50 -294 -609 O ATOM 508 CB LYS A 64 14.365 33.572 21.803 1.00 19.91 C ANISOU 508 CB LYS A 64 2823 2406 2334 -176 -288 -395 C ATOM 509 CG LYS A 64 14.728 33.884 20.360 1.00 22.63 C ANISOU 509 CG LYS A 64 3229 2899 2470 -116 -212 -294 C ATOM 510 CD LYS A 64 16.107 33.365 19.973 1.00 25.49 C ANISOU 510 CD LYS A 64 3099 3440 3144 -83 -84 -139 C ATOM 511 CE LYS A 64 16.573 33.887 18.615 1.00 28.07 C ANISOU 511 CE LYS A 64 3473 3743 3447 -95 190 -152 C ATOM 512 NZ LYS A 64 17.975 33.445 18.341 1.00 31.55 N ANISOU 512 NZ LYS A 64 3670 4161 4153 112 53 -70 N ATOM 513 N GLY A 65 13.614 30.709 24.014 1.00 19.24 N ANISOU 513 N GLY A 65 2685 2299 2324 -156 -136 -501 N ATOM 514 CA GLY A 65 13.390 30.469 25.447 1.00 19.49 C ANISOU 514 CA GLY A 65 2706 2283 2413 -15 9 -394 C ATOM 515 C GLY A 65 14.638 30.575 26.306 1.00 19.07 C ANISOU 515 C GLY A 65 2743 2351 2151 142 60 -307 C ATOM 516 O GLY A 65 14.649 31.182 27.396 1.00 19.48 O ANISOU 516 O GLY A 65 3121 2336 1941 147 92 -498 O ATOM 517 N GLU A 66 15.726 29.988 25.858 1.00 20.20 N ANISOU 517 N GLU A 66 2784 2345 2544 127 58 -476 N ATOM 518 CA GLU A 66 16.961 30.037 26.648 1.00 19.93 C ANISOU 518 CA GLU A 66 2746 2256 2571 270 52 -357 C ATOM 519 C GLU A 66 17.496 31.490 26.863 1.00 20.53 C ANISOU 519 C GLU A 66 3062 2235 2501 265 48 -541 C ATOM 520 O GLU A 66 17.840 31.931 27.991 1.00 21.41 O ANISOU 520 O GLU A 66 3075 2626 2432 286 250 -708 O ATOM 521 CB GLU A 66 18.028 29.150 26.004 1.00 21.82 C ANISOU 521 CB GLU A 66 2914 2591 2783 294 -60 -486 C ATOM 522 CG GLU A 66 17.763 27.643 26.096 1.00 25.25 C ANISOU 522 CG GLU A 66 3507 2826 3260 133 -169 -406 C ATOM 523 CD GLU A 66 16.643 27.120 25.193 1.00 25.04 C ANISOU 523 CD GLU A 66 3352 2878 3283 14 -184 -15 C ATOM 524 OE1 GLU A 66 16.362 27.760 24.146 1.00 25.23 O ANISOU 524 OE1 GLU A 66 4030 2619 2935 319 -206 -258 O ATOM 525 OE2 GLU A 66 16.016 26.076 25.543 1.00 27.57 O ANISOU 525 OE2 GLU A 66 4115 3112 3248 43 -45 69 O ATOM 526 N GLU A 67 17.507 32.238 25.777 1.00 19.80 N ANISOU 526 N GLU A 67 2847 2418 2255 154 230 -634 N ATOM 527 CA GLU A 67 17.942 33.629 25.804 1.00 19.10 C ANISOU 527 CA GLU A 67 2647 2401 2207 145 153 -326 C ATOM 528 C GLU A 67 17.051 34.492 26.689 1.00 18.00 C ANISOU 528 C GLU A 67 2623 2267 1949 93 85 -498 C ATOM 529 O GLU A 67 17.510 35.401 27.364 1.00 17.39 O ANISOU 529 O GLU A 67 2631 2251 1723 -91 -143 -527 O ATOM 530 CB GLU A 67 17.965 34.202 24.383 1.00 19.64 C ANISOU 530 CB GLU A 67 2759 2484 2219 -97 103 -355 C ATOM 531 CG GLU A 67 19.046 33.633 23.477 1.00 22.25 C ANISOU 531 CG GLU A 67 2989 3102 2362 85 213 -240 C ATOM 532 CD GLU A 67 18.669 32.371 22.740 1.00 24.27 C ANISOU 532 CD GLU A 67 3089 3202 2927 121 207 -284 C ATOM 533 OE1 GLU A 67 17.607 31.770 22.982 1.00 24.62 O ANISOU 533 OE1 GLU A 67 3591 3368 2394 0 236 -683 O ATOM 534 OE2 GLU A 67 19.472 32.013 21.858 1.00 28.17 O ANISOU 534 OE2 GLU A 67 3647 3998 3057 290 316 -616 O ATOM 535 N HIS A 68 15.767 34.195 26.627 1.00 18.28 N ANISOU 535 N HIS A 68 2678 2279 1988 -25 -90 -261 N ATOM 536 CA HIS A 68 14.730 34.857 27.403 1.00 17.09 C ANISOU 536 CA HIS A 68 2390 2241 1861 -15 -154 -227 C ATOM 537 C HIS A 68 14.996 34.657 28.912 1.00 15.70 C ANISOU 537 C HIS A 68 2218 1937 1808 -105 -216 -288 C ATOM 538 O HIS A 68 14.991 35.606 29.676 1.00 15.20 O ANISOU 538 O HIS A 68 2351 1762 1659 32 -267 -374 O ATOM 539 CB HIS A 68 13.383 34.336 26.930 1.00 18.44 C ANISOU 539 CB HIS A 68 2595 2213 2197 -76 -277 -333 C ATOM 540 CG HIS A 68 12.280 34.420 27.905 1.00 16.47 C ANISOU 540 CG HIS A 68 2388 1901 1969 -290 -413 -201 C ATOM 541 ND1 HIS A 68 11.636 35.594 28.268 1.00 16.91 N ANISOU 541 ND1 HIS A 68 2363 2068 1993 -181 -406 -275 N ATOM 542 CD2 HIS A 68 11.637 33.412 28.532 1.00 20.10 C ANISOU 542 CD2 HIS A 68 2632 2496 2506 -246 -436 -19 C ATOM 543 CE1 HIS A 68 10.658 35.295 29.093 1.00 17.34 C ANISOU 543 CE1 HIS A 68 2077 2383 2128 -392 -369 16 C ATOM 544 NE2 HIS A 68 10.650 33.972 29.286 1.00 18.73 N ANISOU 544 NE2 HIS A 68 2564 2616 1936 -457 -340 -57 N ATOM 545 N TRP A 69 15.255 33.427 29.346 1.00 15.45 N ANISOU 545 N TRP A 69 2202 1853 1811 42 -3 -392 N ATOM 546 CA TRP A 69 15.579 33.217 30.773 1.00 14.84 C ANISOU 546 CA TRP A 69 2011 1838 1790 137 61 -292 C ATOM 547 C TRP A 69 16.910 33.864 31.159 1.00 14.90 C ANISOU 547 C TRP A 69 2033 1865 1764 239 32 -169 C ATOM 548 O TRP A 69 17.033 34.428 32.242 1.00 14.33 O ANISOU 548 O TRP A 69 1996 1795 1652 227 28 -274 O ATOM 549 CB TRP A 69 15.537 31.727 31.138 1.00 15.77 C ANISOU 549 CB TRP A 69 2117 1937 1936 227 -37 -235 C ATOM 550 CG TRP A 69 14.148 31.285 31.297 1.00 15.76 C ANISOU 550 CG TRP A 69 2199 1754 2032 55 -64 -191 C ATOM 551 CD1 TRP A 69 13.353 30.683 30.378 1.00 16.31 C ANISOU 551 CD1 TRP A 69 2428 1728 2039 166 56 -262 C ATOM 552 CD2 TRP A 69 13.325 31.505 32.448 1.00 14.97 C ANISOU 552 CD2 TRP A 69 2050 1859 1777 49 -83 -150 C ATOM 553 NE1 TRP A 69 12.087 30.523 30.875 1.00 16.35 N ANISOU 553 NE1 TRP A 69 2363 1788 2060 -30 -186 -239 N ATOM 554 CE2 TRP A 69 12.038 31.022 32.144 1.00 15.05 C ANISOU 554 CE2 TRP A 69 2081 1797 1838 70 -124 -64 C ATOM 555 CE3 TRP A 69 13.536 32.101 33.689 1.00 15.36 C ANISOU 555 CE3 TRP A 69 1756 1879 2199 61 -179 -335 C ATOM 556 CZ2 TRP A 69 10.994 31.106 33.041 1.00 15.87 C ANISOU 556 CZ2 TRP A 69 2019 1804 2203 -37 -229 -53 C ATOM 557 CZ3 TRP A 69 12.488 32.169 34.575 1.00 15.53 C ANISOU 557 CZ3 TRP A 69 2078 2011 1811 59 -91 -112 C ATOM 558 CH2 TRP A 69 11.232 31.674 34.252 1.00 14.69 C ANISOU 558 CH2 TRP A 69 1855 1770 1956 26 -94 -6 C ATOM 559 N GLU A 70 17.901 33.814 30.297 1.00 15.97 N ANISOU 559 N GLU A 70 2167 1889 2010 145 115 -235 N ATOM 560 CA GLU A 70 19.163 34.470 30.603 1.00 16.20 C ANISOU 560 CA GLU A 70 1976 2099 2078 212 181 -152 C ATOM 561 C GLU A 70 18.951 35.995 30.758 1.00 14.74 C ANISOU 561 C GLU A 70 1767 1917 1914 144 42 -251 C ATOM 562 O GLU A 70 19.499 36.618 31.658 1.00 15.30 O ANISOU 562 O GLU A 70 1566 2206 2039 318 -95 -469 O ATOM 563 CB GLU A 70 20.140 34.164 29.490 1.00 18.21 C ANISOU 563 CB GLU A 70 2185 2274 2460 324 89 -323 C ATOM 564 CG GLU A 70 21.485 34.827 29.584 1.00 21.12 C ANISOU 564 CG GLU A 70 2512 2776 2737 41 128 -152 C ATOM 565 CD GLU A 70 22.444 34.382 28.489 1.00 24.71 C ANISOU 565 CD GLU A 70 2757 3372 3258 62 257 -157 C ATOM 566 OE1 GLU A 70 22.117 33.484 27.676 1.00 34.92 O ANISOU 566 OE1 GLU A 70 4385 4591 4290 180 -127 -488 O ATOM 567 OE2 GLU A 70 23.556 34.933 28.447 1.00 31.49 O ANISOU 567 OE2 GLU A 70 3333 4417 4211 -111 250 2 O ATOM 568 N TYR A 71 18.164 36.582 29.868 1.00 13.91 N ANISOU 568 N TYR A 71 1767 1985 1533 208 -36 -346 N ATOM 569 CA TYR A 71 17.842 37.990 29.920 1.00 13.53 C ANISOU 569 CA TYR A 71 1676 1856 1607 34 82 -264 C ATOM 570 C TYR A 71 17.085 38.343 31.214 1.00 13.94 C ANISOU 570 C TYR A 71 1870 1847 1578 -23 -43 -398 C ATOM 571 O TYR A 71 17.375 39.346 31.865 1.00 14.43 O ANISOU 571 O TYR A 71 1851 2049 1581 -81 -119 -395 O ATOM 572 CB TYR A 71 17.026 38.369 28.683 1.00 13.99 C ANISOU 572 CB TYR A 71 1748 2027 1540 -32 81 -183 C ATOM 573 CG TYR A 71 16.656 39.820 28.621 1.00 13.99 C ANISOU 573 CG TYR A 71 1664 2156 1495 43 0 -167 C ATOM 574 CD1 TYR A 71 17.538 40.763 28.106 1.00 16.25 C ANISOU 574 CD1 TYR A 71 2043 2213 1915 37 -16 -133 C ATOM 575 CD2 TYR A 71 15.433 40.275 29.087 1.00 14.25 C ANISOU 575 CD2 TYR A 71 1717 2063 1631 -90 -58 -270 C ATOM 576 CE1 TYR A 71 17.183 42.128 28.064 1.00 18.37 C ANISOU 576 CE1 TYR A 71 2097 2229 2652 -100 -148 94 C ATOM 577 CE2 TYR A 71 15.084 41.604 29.067 1.00 15.46 C ANISOU 577 CE2 TYR A 71 1875 2183 1814 140 -118 -177 C ATOM 578 CZ TYR A 71 15.958 42.530 28.558 1.00 15.95 C ANISOU 578 CZ TYR A 71 2167 1921 1969 76 -174 -185 C ATOM 579 OH TYR A 71 15.573 43.854 28.586 1.00 17.35 O ANISOU 579 OH TYR A 71 2250 2130 2212 135 -148 43 O ATOM 580 N PHE A 72 16.069 37.543 31.554 1.00 13.29 N ANISOU 580 N PHE A 72 1794 1756 1498 99 44 -431 N ATOM 581 CA PHE A 72 15.357 37.707 32.812 1.00 13.46 C ANISOU 581 CA PHE A 72 1652 1723 1736 3 -49 -343 C ATOM 582 C PHE A 72 16.307 37.796 34.003 1.00 12.97 C ANISOU 582 C PHE A 72 1618 1705 1603 91 -27 -206 C ATOM 583 O PHE A 72 16.208 38.673 34.852 1.00 13.50 O ANISOU 583 O PHE A 72 1831 1779 1518 126 -137 -224 O ATOM 584 CB PHE A 72 14.366 36.544 32.974 1.00 13.88 C ANISOU 584 CB PHE A 72 1554 1883 1835 37 -121 -290 C ATOM 585 CG PHE A 72 13.776 36.441 34.350 1.00 13.88 C ANISOU 585 CG PHE A 72 1868 1741 1664 -57 23 -270 C ATOM 586 CD1 PHE A 72 12.732 37.269 34.748 1.00 14.10 C ANISOU 586 CD1 PHE A 72 1797 1706 1854 -22 91 -160 C ATOM 587 CD2 PHE A 72 14.257 35.520 35.261 1.00 14.29 C ANISOU 587 CD2 PHE A 72 1734 1838 1856 -48 5 -124 C ATOM 588 CE1 PHE A 72 12.204 37.182 36.015 1.00 14.40 C ANISOU 588 CE1 PHE A 72 1645 1801 2025 34 -66 -256 C ATOM 589 CE2 PHE A 72 13.718 35.437 36.546 1.00 14.60 C ANISOU 589 CE2 PHE A 72 1847 1828 1869 -80 -105 -14 C ATOM 590 CZ PHE A 72 12.703 36.272 36.914 1.00 14.54 C ANISOU 590 CZ PHE A 72 1781 1826 1917 -144 -2 -295 C ATOM 591 N GLY A 73 17.225 36.838 34.079 1.00 13.63 N ANISOU 591 N GLY A 73 1846 1640 1689 247 -139 -229 N ATOM 592 CA GLY A 73 18.131 36.771 35.224 1.00 14.40 C ANISOU 592 CA GLY A 73 1832 1828 1809 93 -227 -205 C ATOM 593 C GLY A 73 19.013 38.001 35.255 1.00 14.11 C ANISOU 593 C GLY A 73 1719 1860 1781 240 -219 -210 C ATOM 594 O GLY A 73 19.208 38.616 36.296 1.00 14.88 O ANISOU 594 O GLY A 73 1908 1936 1809 255 -400 -157 O ATOM 595 N LYS A 74 19.569 38.385 34.109 1.00 14.65 N ANISOU 595 N LYS A 74 1798 1908 1857 60 -139 -183 N ATOM 596 CA LYS A 74 20.451 39.560 34.073 1.00 16.20 C ANISOU 596 CA LYS A 74 1940 2094 2119 60 -203 -166 C ATOM 597 C LYS A 74 19.687 40.822 34.389 1.00 15.04 C ANISOU 597 C LYS A 74 1736 1889 2090 -2 -217 -234 C ATOM 598 O LYS A 74 20.180 41.677 35.125 1.00 17.18 O ANISOU 598 O LYS A 74 1933 2163 2428 -15 -377 -402 O ATOM 599 CB LYS A 74 21.144 39.669 32.723 1.00 17.29 C ANISOU 599 CB LYS A 74 2034 2167 2369 -143 -9 -29 C ATOM 600 CG LYS A 74 22.166 38.550 32.477 1.00 21.84 C ANISOU 600 CG LYS A 74 2405 2876 3017 110 113 -128 C ATOM 601 CD LYS A 74 22.900 38.713 31.181 1.00 24.92 C ANISOU 601 CD LYS A 74 3105 3274 3087 157 23 -148 C ATOM 602 CE LYS A 74 23.522 37.405 30.731 1.00 28.13 C ANISOU 602 CE LYS A 74 3340 3686 3660 285 272 -177 C ATOM 603 NZ LYS A 74 23.679 37.438 29.258 1.00 31.44 N ANISOU 603 NZ LYS A 74 4045 4173 3725 94 -39 -15 N ATOM 604 N TYR A 75 18.478 40.933 33.885 1.00 13.67 N ANISOU 604 N TYR A 75 1703 1802 1687 66 -121 -150 N ATOM 605 CA TYR A 75 17.680 42.151 34.036 1.00 13.67 C ANISOU 605 CA TYR A 75 1730 1708 1756 74 -141 -215 C ATOM 606 C TYR A 75 17.390 42.409 35.496 1.00 13.05 C ANISOU 606 C TYR A 75 1613 1694 1648 -28 -59 -305 C ATOM 607 O TYR A 75 17.595 43.517 36.002 1.00 15.19 O ANISOU 607 O TYR A 75 2018 1917 1836 -28 -23 -376 O ATOM 608 CB TYR A 75 16.395 42.054 33.200 1.00 13.42 C ANISOU 608 CB TYR A 75 1636 1861 1603 187 -170 -71 C ATOM 609 CG TYR A 75 15.513 43.294 33.198 1.00 13.15 C ANISOU 609 CG TYR A 75 1536 1787 1673 -72 -115 -77 C ATOM 610 CD1 TYR A 75 14.648 43.596 34.255 1.00 12.82 C ANISOU 610 CD1 TYR A 75 1471 1959 1438 -96 -173 -193 C ATOM 611 CD2 TYR A 75 15.546 44.156 32.129 1.00 15.41 C ANISOU 611 CD2 TYR A 75 2070 2041 1743 289 135 -11 C ATOM 612 CE1 TYR A 75 13.874 44.728 34.236 1.00 13.27 C ANISOU 612 CE1 TYR A 75 1475 1974 1593 0 -84 -175 C ATOM 613 CE2 TYR A 75 14.759 45.263 32.105 1.00 14.92 C ANISOU 613 CE2 TYR A 75 1812 1889 1967 338 113 122 C ATOM 614 CZ TYR A 75 13.907 45.549 33.161 1.00 14.87 C ANISOU 614 CZ TYR A 75 1740 1976 1931 213 103 -32 C ATOM 615 OH TYR A 75 13.103 46.670 33.151 1.00 16.45 O ANISOU 615 OH TYR A 75 1690 2026 2531 194 195 147 O ATOM 616 N PHE A 76 16.835 41.416 36.183 1.00 12.89 N ANISOU 616 N PHE A 76 1688 1637 1571 23 -227 -214 N ATOM 617 CA PHE A 76 16.420 41.630 37.556 1.00 13.56 C ANISOU 617 CA PHE A 76 1774 1692 1684 183 -102 -163 C ATOM 618 C PHE A 76 17.525 41.454 38.592 1.00 14.01 C ANISOU 618 C PHE A 76 1921 1579 1822 159 -299 -46 C ATOM 619 O PHE A 76 17.439 42.025 39.671 1.00 14.91 O ANISOU 619 O PHE A 76 2245 1820 1600 136 -150 -177 O ATOM 620 CB PHE A 76 15.231 40.725 37.874 1.00 14.08 C ANISOU 620 CB PHE A 76 1903 1673 1774 245 -198 -83 C ATOM 621 CG PHE A 76 13.958 41.209 37.259 1.00 13.06 C ANISOU 621 CG PHE A 76 1669 1699 1594 71 -153 64 C ATOM 622 CD1 PHE A 76 13.368 42.398 37.667 1.00 14.32 C ANISOU 622 CD1 PHE A 76 1700 1884 1856 267 -234 -73 C ATOM 623 CD2 PHE A 76 13.384 40.515 36.203 1.00 13.76 C ANISOU 623 CD2 PHE A 76 1631 1668 1929 135 -57 -18 C ATOM 624 CE1 PHE A 76 12.202 42.849 37.060 1.00 13.79 C ANISOU 624 CE1 PHE A 76 1669 1893 1677 248 12 4 C ATOM 625 CE2 PHE A 76 12.244 40.994 35.601 1.00 14.09 C ANISOU 625 CE2 PHE A 76 1556 1855 1940 -184 -195 -12 C ATOM 626 CZ PHE A 76 11.652 42.147 36.047 1.00 14.12 C ANISOU 626 CZ PHE A 76 1562 1953 1848 65 -187 191 C ATOM 627 N SER A 77 18.599 40.729 38.275 1.00 14.43 N ANISOU 627 N SER A 77 2090 1742 1652 308 -382 -122 N ATOM 628 CA SER A 77 19.696 40.528 39.241 1.00 14.87 C ANISOU 628 CA SER A 77 2096 1705 1849 195 -431 -106 C ATOM 629 C SER A 77 20.452 41.824 39.520 1.00 14.80 C ANISOU 629 C SER A 77 1863 2011 1747 46 -192 -202 C ATOM 630 O SER A 77 21.122 41.912 40.527 1.00 17.19 O ANISOU 630 O SER A 77 2283 2527 1718 31 -447 -417 O ATOM 631 CB SER A 77 20.701 39.469 38.727 1.00 16.38 C ANISOU 631 CB SER A 77 2231 1643 2346 335 -765 -114 C ATOM 632 OG ASER A 77 20.025 38.237 38.860 0.75 17.52 O ANISOU 632 OG ASER A 77 2775 1619 2261 374 -403 -33 O ATOM 633 OG BSER A 77 21.796 40.238 38.298 0.25 22.57 O ANISOU 633 OG BSER A 77 2900 2845 2829 213 1 166 O ATOM 634 N GLN A 78 20.358 42.783 38.609 1.00 14.82 N ANISOU 634 N GLN A 78 1888 1801 1938 173 -156 -210 N ATOM 635 CA GLN A 78 21.108 44.046 38.632 1.00 17.07 C ANISOU 635 CA GLN A 78 2048 1983 2453 191 -74 -139 C ATOM 636 C GLN A 78 20.226 45.292 38.764 1.00 15.63 C ANISOU 636 C GLN A 78 1789 1863 2286 117 -73 -210 C ATOM 637 O GLN A 78 20.657 46.402 38.477 1.00 15.18 O ANISOU 637 O GLN A 78 1585 1897 2285 119 -195 98 O ATOM 638 CB GLN A 78 21.943 44.174 37.353 1.00 19.63 C ANISOU 638 CB GLN A 78 2430 2347 2681 8 -16 -165 C ATOM 639 CG GLN A 78 21.149 44.572 36.096 1.00 24.13 C ANISOU 639 CG GLN A 78 2782 3227 3159 -10 -51 92 C ATOM 640 CD GLN A 78 22.020 44.884 34.878 1.00 25.57 C ANISOU 640 CD GLN A 78 3142 3443 3131 59 72 -22 C ATOM 641 OE1 GLN A 78 23.165 45.347 34.999 1.00 33.64 O ANISOU 641 OE1 GLN A 78 3864 4580 4337 -181 -45 -45 O ATOM 642 NE2 GLN A 78 21.465 44.638 33.693 1.00 31.73 N ANISOU 642 NE2 GLN A 78 4077 4451 3527 36 -77 15 N ATOM 643 N LEU A 79 18.984 45.111 39.169 1.00 14.17 N ANISOU 643 N LEU A 79 1554 1715 2115 206 -80 -173 N ATOM 644 CA LEU A 79 18.049 46.205 39.246 1.00 13.94 C ANISOU 644 CA LEU A 79 1588 1825 1880 180 -110 -186 C ATOM 645 C LEU A 79 17.260 46.123 40.529 1.00 13.83 C ANISOU 645 C LEU A 79 1680 1592 1982 110 -25 -218 C ATOM 646 O LEU A 79 16.792 45.046 40.901 1.00 15.26 O ANISOU 646 O LEU A 79 1799 1639 2359 107 63 -35 O ATOM 647 CB LEU A 79 17.113 46.133 38.053 1.00 15.82 C ANISOU 647 CB LEU A 79 2028 1996 1987 43 -189 -311 C ATOM 648 CG LEU A 79 16.234 47.340 37.778 1.00 15.76 C ANISOU 648 CG LEU A 79 1766 2315 1905 127 -394 -248 C ATOM 649 CD1 LEU A 79 17.025 48.554 37.351 1.00 15.85 C ANISOU 649 CD1 LEU A 79 2169 2077 1775 181 -471 -196 C ATOM 650 CD2 LEU A 79 15.265 46.966 36.692 1.00 18.45 C ANISOU 650 CD2 LEU A 79 1978 2775 2256 5 -420 -246 C ATOM 651 N GLU A 80 17.114 47.257 41.202 1.00 12.49 N ANISOU 651 N GLU A 80 1385 1601 1757 51 61 -204 N ATOM 652 CA GLU A 80 16.241 47.337 42.368 1.00 13.23 C ANISOU 652 CA GLU A 80 1493 1657 1875 14 19 2 C ATOM 653 C GLU A 80 14.797 47.227 41.907 1.00 13.49 C ANISOU 653 C GLU A 80 1590 1843 1690 -106 -36 9 C ATOM 654 O GLU A 80 14.402 47.794 40.889 1.00 14.84 O ANISOU 654 O GLU A 80 1520 2267 1848 -134 -51 302 O ATOM 655 CB GLU A 80 16.496 48.639 43.097 1.00 13.33 C ANISOU 655 CB GLU A 80 1560 1719 1784 0 -70 -16 C ATOM 656 CG GLU A 80 15.667 48.836 44.348 1.00 15.49 C ANISOU 656 CG GLU A 80 2006 1955 1923 -33 121 -18 C ATOM 657 CD AGLU A 80 16.217 48.091 45.547 0.50 20.70 C ANISOU 657 CD AGLU A 80 2709 2744 2410 151 -46 88 C ATOM 658 CD BGLU A 80 15.882 47.808 45.436 0.50 15.55 C ANISOU 658 CD BGLU A 80 2005 1892 2009 4 -36 -85 C ATOM 659 OE1AGLU A 80 17.376 47.625 45.501 0.50 19.77 O ANISOU 659 OE1AGLU A 80 2463 2942 2104 -98 -182 -139 O ATOM 660 OE1BGLU A 80 15.488 46.628 45.219 0.50 17.09 O ANISOU 660 OE1BGLU A 80 2178 2140 2176 139 -139 131 O ATOM 661 OE2AGLU A 80 15.523 48.053 46.581 0.50 22.56 O ANISOU 661 OE2AGLU A 80 2779 3264 2528 -39 104 122 O ATOM 662 OE2BGLU A 80 16.389 48.227 46.523 0.50 15.14 O ANISOU 662 OE2BGLU A 80 1828 1796 2128 -381 -350 192 O ATOM 663 N VAL A 81 14.006 46.453 42.643 1.00 13.07 N ANISOU 663 N VAL A 81 1457 1792 1717 -73 41 -16 N ATOM 664 CA VAL A 81 12.572 46.246 42.392 1.00 13.98 C ANISOU 664 CA VAL A 81 1486 1911 1911 -147 -4 -28 C ATOM 665 C VAL A 81 11.826 46.903 43.551 1.00 14.16 C ANISOU 665 C VAL A 81 1728 1838 1813 -232 15 -32 C ATOM 666 O VAL A 81 12.120 46.653 44.721 1.00 15.81 O ANISOU 666 O VAL A 81 2001 2160 1842 -90 44 80 O ATOM 667 CB VAL A 81 12.258 44.764 42.236 1.00 14.73 C ANISOU 667 CB VAL A 81 1814 1811 1971 -312 -13 -67 C ATOM 668 CG1 VAL A 81 10.752 44.492 42.231 1.00 15.81 C ANISOU 668 CG1 VAL A 81 1777 1935 2292 -362 144 -95 C ATOM 669 CG2 VAL A 81 12.900 44.239 40.932 1.00 14.72 C ANISOU 669 CG2 VAL A 81 1947 1685 1959 -207 -132 -207 C ATOM 670 N ILE A 82 10.847 47.722 43.212 1.00 14.77 N ANISOU 670 N ILE A 82 1599 1976 2035 -128 44 -40 N ATOM 671 CA ILE A 82 10.068 48.445 44.216 1.00 16.30 C ANISOU 671 CA ILE A 82 1941 2161 2089 -56 29 -180 C ATOM 672 C ILE A 82 8.610 48.018 44.137 1.00 17.79 C ANISOU 672 C ILE A 82 2043 2337 2377 0 -60 -16 C ATOM 673 O ILE A 82 8.160 47.226 44.988 1.00 21.91 O ANISOU 673 O ILE A 82 2420 3097 2807 -32 -26 132 O ATOM 674 CB ILE A 82 10.247 49.959 44.041 1.00 17.53 C ANISOU 674 CB ILE A 82 2252 2150 2259 0 -125 -147 C ATOM 675 CG1 ILE A 82 11.722 50.371 44.194 1.00 16.51 C ANISOU 675 CG1 ILE A 82 2428 1821 2022 -90 -53 -31 C ATOM 676 CG2 ILE A 82 9.429 50.751 45.039 1.00 18.92 C ANISOU 676 CG2 ILE A 82 2165 2554 2468 130 -19 -168 C ATOM 677 CD1 ILE A 82 12.321 50.106 45.553 1.00 17.86 C ANISOU 677 CD1 ILE A 82 2438 2227 2121 -53 -93 -24 C ATOM 678 N ASP A 83 7.919 48.415 43.060 1.00 18.37 N ANISOU 678 N ASP A 83 2196 2250 2532 -199 -166 -83 N ATOM 679 CA ASP A 83 6.529 47.989 42.762 1.00 18.33 C ANISOU 679 CA ASP A 83 1987 2449 2528 -81 -69 -329 C ATOM 680 C ASP A 83 6.625 46.876 41.761 1.00 16.42 C ANISOU 680 C ASP A 83 1765 2129 2344 -173 84 -147 C ATOM 681 O ASP A 83 6.830 47.073 40.572 1.00 15.27 O ANISOU 681 O ASP A 83 1612 2029 2160 -389 18 -243 O ATOM 682 CB ASP A 83 5.657 49.115 42.204 1.00 20.98 C ANISOU 682 CB ASP A 83 2413 2756 2800 49 -97 -257 C ATOM 683 CG ASP A 83 4.155 48.716 42.010 1.00 23.07 C ANISOU 683 CG ASP A 83 2627 2978 3157 -105 -201 -266 C ATOM 684 OD1 ASP A 83 3.797 47.756 41.266 1.00 21.70 O ANISOU 684 OD1 ASP A 83 2165 2761 3317 -277 249 -314 O ATOM 685 OD2 ASP A 83 3.239 49.419 42.509 1.00 31.14 O ANISOU 685 OD2 ASP A 83 3476 4145 4207 212 199 -165 O ATOM 686 N LEU A 84 6.482 45.688 42.290 1.00 16.45 N ANISOU 686 N LEU A 84 1835 2087 2328 -178 268 -151 N ATOM 687 CA LEU A 84 6.787 44.500 41.556 1.00 15.80 C ANISOU 687 CA LEU A 84 1798 1987 2216 -123 159 -87 C ATOM 688 C LEU A 84 5.963 44.395 40.252 1.00 14.90 C ANISOU 688 C LEU A 84 1693 1858 2110 -196 410 -136 C ATOM 689 O LEU A 84 6.489 44.126 39.173 1.00 15.38 O ANISOU 689 O LEU A 84 1567 2123 2154 -178 272 -43 O ATOM 690 CB LEU A 84 6.518 43.326 42.481 1.00 17.90 C ANISOU 690 CB LEU A 84 2372 2181 2248 -222 149 -151 C ATOM 691 CG LEU A 84 7.059 41.966 42.063 1.00 19.09 C ANISOU 691 CG LEU A 84 2551 2270 2430 41 -33 -133 C ATOM 692 CD1 LEU A 84 7.315 41.058 43.258 1.00 20.52 C ANISOU 692 CD1 LEU A 84 2626 2241 2926 182 -242 132 C ATOM 693 CD2 LEU A 84 6.114 41.284 41.110 1.00 19.48 C ANISOU 693 CD2 LEU A 84 2692 2333 2375 67 -187 -196 C ATOM 694 N CYS A 85 4.668 44.630 40.339 1.00 15.46 N ANISOU 694 N CYS A 85 1566 1981 2327 -290 281 -245 N ATOM 695 CA CYS A 85 3.815 44.552 39.174 1.00 15.72 C ANISOU 695 CA CYS A 85 1498 1947 2528 -202 224 -207 C ATOM 696 C CYS A 85 4.218 45.550 38.097 1.00 14.40 C ANISOU 696 C CYS A 85 1311 1844 2315 -220 162 -231 C ATOM 697 O CYS A 85 4.397 45.207 36.920 1.00 15.00 O ANISOU 697 O CYS A 85 1366 1978 2353 -329 295 -221 O ATOM 698 CB CYS A 85 2.356 44.772 39.561 1.00 17.16 C ANISOU 698 CB CYS A 85 1674 2049 2794 -379 244 -215 C ATOM 699 SG CYS A 85 1.234 44.568 38.163 1.00 19.01 S ANISOU 699 SG CYS A 85 1631 2297 3294 -433 318 -1 S ATOM 700 N ARG A 86 4.398 46.811 38.495 1.00 14.10 N ANISOU 700 N ARG A 86 1186 1795 2376 -201 397 -246 N ATOM 701 CA ARG A 86 4.809 47.839 37.569 1.00 14.03 C ANISOU 701 CA ARG A 86 1262 1755 2314 -76 173 -191 C ATOM 702 C ARG A 86 6.174 47.542 36.933 1.00 13.17 C ANISOU 702 C ARG A 86 1252 1637 2115 -54 218 -205 C ATOM 703 O ARG A 86 6.342 47.702 35.731 1.00 14.11 O ANISOU 703 O ARG A 86 1259 1900 2202 140 215 -207 O ATOM 704 CB ARG A 86 4.827 49.211 38.212 1.00 15.55 C ANISOU 704 CB ARG A 86 1516 1960 2432 -146 705 -250 C ATOM 705 CG ARG A 86 3.364 49.700 38.468 1.00 18.03 C ANISOU 705 CG ARG A 86 1773 2598 2477 -451 473 -130 C ATOM 706 CD ARG A 86 3.258 51.060 38.905 1.00 17.06 C ANISOU 706 CD ARG A 86 1520 2526 2434 145 210 13 C ATOM 707 NE ARG A 86 2.004 51.245 39.598 1.00 18.03 N ANISOU 707 NE ARG A 86 1754 2747 2348 96 419 145 N ATOM 708 CZ ARG A 86 1.874 52.147 40.496 1.00 17.30 C ANISOU 708 CZ ARG A 86 1768 2245 2557 114 226 57 C ATOM 709 NH1 ARG A 86 2.883 52.979 40.724 1.00 21.06 N ANISOU 709 NH1 ARG A 86 2017 2525 3460 -120 451 105 N ATOM 710 NH2 ARG A 86 0.748 52.273 41.123 1.00 15.46 N ANISOU 710 NH2 ARG A 86 1416 2272 2186 221 170 192 N ATOM 711 N ASP A 87 7.106 47.064 37.739 1.00 12.68 N ANISOU 711 N ASP A 87 1074 1877 1864 -131 193 -274 N ATOM 712 CA ASP A 87 8.439 46.773 37.285 1.00 12.50 C ANISOU 712 CA ASP A 87 1247 1681 1820 -83 165 -291 C ATOM 713 C ASP A 87 8.393 45.596 36.307 1.00 12.33 C ANISOU 713 C ASP A 87 1156 1858 1670 -76 -37 -206 C ATOM 714 O ASP A 87 9.123 45.600 35.295 1.00 12.92 O ANISOU 714 O ASP A 87 1318 1768 1821 -62 127 -144 O ATOM 715 CB ASP A 87 9.365 46.495 38.459 1.00 13.52 C ANISOU 715 CB ASP A 87 1266 1908 1961 -119 165 -288 C ATOM 716 CG ASP A 87 9.657 47.710 39.294 1.00 13.74 C ANISOU 716 CG ASP A 87 1289 2145 1785 -304 193 -185 C ATOM 717 OD1 ASP A 87 9.309 48.841 38.911 1.00 16.70 O ANISOU 717 OD1 ASP A 87 1827 2079 2436 -305 53 -437 O ATOM 718 OD2 ASP A 87 10.210 47.556 40.369 1.00 16.29 O ANISOU 718 OD2 ASP A 87 1839 2285 2063 -339 9 -266 O ATOM 719 N PHE A 88 7.536 44.606 36.569 1.00 12.80 N ANISOU 719 N PHE A 88 1329 1807 1724 -50 112 -324 N ATOM 720 CA PHE A 88 7.423 43.488 35.662 1.00 12.45 C ANISOU 720 CA PHE A 88 1327 1735 1669 -16 90 -224 C ATOM 721 C PHE A 88 6.822 43.897 34.336 1.00 12.70 C ANISOU 721 C PHE A 88 1378 1532 1913 -155 23 -181 C ATOM 722 O PHE A 88 7.262 43.434 33.263 1.00 13.41 O ANISOU 722 O PHE A 88 1455 1762 1877 -60 -14 -244 O ATOM 723 CB PHE A 88 6.679 42.304 36.276 1.00 12.93 C ANISOU 723 CB PHE A 88 1231 1783 1898 -139 51 -110 C ATOM 724 CG PHE A 88 6.930 41.038 35.520 1.00 12.62 C ANISOU 724 CG PHE A 88 1472 1631 1690 -69 3 -180 C ATOM 725 CD1 PHE A 88 8.105 40.330 35.712 1.00 13.79 C ANISOU 725 CD1 PHE A 88 1669 1760 1809 50 -104 -69 C ATOM 726 CD2 PHE A 88 6.063 40.617 34.541 1.00 14.20 C ANISOU 726 CD2 PHE A 88 1794 1602 1996 -5 -79 -156 C ATOM 727 CE1 PHE A 88 8.387 39.229 34.934 1.00 14.92 C ANISOU 727 CE1 PHE A 88 1742 1706 2219 207 334 39 C ATOM 728 CE2 PHE A 88 6.344 39.514 33.789 1.00 15.91 C ANISOU 728 CE2 PHE A 88 2178 1776 2090 -232 -104 -375 C ATOM 729 CZ PHE A 88 7.488 38.832 33.978 1.00 15.52 C ANISOU 729 CZ PHE A 88 2339 1586 1971 74 439 -318 C ATOM 730 N LEU A 89 5.774 44.704 34.390 1.00 12.76 N ANISOU 730 N LEU A 89 1191 1673 1983 -81 -26 -159 N ATOM 731 CA LEU A 89 5.147 45.144 33.156 1.00 14.22 C ANISOU 731 CA LEU A 89 1466 1732 2204 -64 49 27 C ATOM 732 C LEU A 89 6.126 45.932 32.295 1.00 12.99 C ANISOU 732 C LEU A 89 1236 1695 2002 -17 111 -87 C ATOM 733 O LEU A 89 6.118 45.797 31.069 1.00 14.89 O ANISOU 733 O LEU A 89 1537 2027 2092 -33 114 48 O ATOM 734 CB LEU A 89 3.852 45.899 33.388 1.00 15.37 C ANISOU 734 CB LEU A 89 1509 1873 2457 -98 124 101 C ATOM 735 CG LEU A 89 2.592 45.025 33.410 1.00 20.70 C ANISOU 735 CG LEU A 89 1928 2621 3315 -150 169 110 C ATOM 736 CD1 LEU A 89 2.653 43.730 34.181 1.00 22.15 C ANISOU 736 CD1 LEU A 89 2483 2691 3241 -214 253 71 C ATOM 737 CD2 LEU A 89 1.395 45.864 33.859 1.00 20.57 C ANISOU 737 CD2 LEU A 89 1962 2691 3161 -37 129 133 C ATOM 738 N LYS A 90 6.950 46.790 32.908 1.00 12.98 N ANISOU 738 N LYS A 90 1270 1529 2131 -103 160 22 N ATOM 739 CA LYS A 90 7.975 47.530 32.216 1.00 14.17 C ANISOU 739 CA LYS A 90 1431 1716 2236 -54 140 -5 C ATOM 740 C LYS A 90 8.986 46.576 31.566 1.00 13.59 C ANISOU 740 C LYS A 90 1454 1730 1980 -21 137 -110 C ATOM 741 O LYS A 90 9.416 46.772 30.420 1.00 15.30 O ANISOU 741 O LYS A 90 1927 1951 1932 69 168 46 O ATOM 742 CB LYS A 90 8.653 48.522 33.172 1.00 14.75 C ANISOU 742 CB LYS A 90 1367 1742 2493 -205 84 -5 C ATOM 743 CG LYS A 90 9.763 49.344 32.548 1.00 16.98 C ANISOU 743 CG LYS A 90 1659 2266 2525 -176 262 -79 C ATOM 744 CD LYS A 90 10.298 50.437 33.479 1.00 18.78 C ANISOU 744 CD LYS A 90 2044 2366 2726 -275 -35 -81 C ATOM 745 CE LYS A 90 11.385 51.224 32.794 1.00 21.77 C ANISOU 745 CE LYS A 90 2454 2828 2986 -378 68 125 C ATOM 746 NZ LYS A 90 11.828 52.394 33.562 1.00 26.61 N ANISOU 746 NZ LYS A 90 3049 3288 3774 -326 -53 -263 N ATOM 747 N TYR A 91 9.374 45.538 32.288 1.00 12.79 N ANISOU 747 N TYR A 91 1369 1627 1863 86 120 -67 N ATOM 748 CA TYR A 91 10.267 44.492 31.755 1.00 13.07 C ANISOU 748 CA TYR A 91 1448 1707 1810 -25 27 -145 C ATOM 749 C TYR A 91 9.662 43.866 30.514 1.00 12.86 C ANISOU 749 C TYR A 91 1404 1744 1736 -6 56 -89 C ATOM 750 O TYR A 91 10.380 43.637 29.528 1.00 14.23 O ANISOU 750 O TYR A 91 1639 1925 1843 38 58 -155 O ATOM 751 CB TYR A 91 10.564 43.487 32.875 1.00 12.59 C ANISOU 751 CB TYR A 91 1415 1738 1627 71 -11 -157 C ATOM 752 CG TYR A 91 10.963 42.114 32.403 1.00 12.91 C ANISOU 752 CG TYR A 91 1285 1715 1905 167 108 -27 C ATOM 753 CD1 TYR A 91 12.270 41.844 31.990 1.00 12.09 C ANISOU 753 CD1 TYR A 91 1382 1526 1683 -29 -111 -46 C ATOM 754 CD2 TYR A 91 10.052 41.056 32.376 1.00 12.47 C ANISOU 754 CD2 TYR A 91 1491 1749 1497 -30 -47 -121 C ATOM 755 CE1 TYR A 91 12.663 40.610 31.578 1.00 13.27 C ANISOU 755 CE1 TYR A 91 1520 1974 1546 279 68 -193 C ATOM 756 CE2 TYR A 91 10.419 39.827 31.944 1.00 13.39 C ANISOU 756 CE2 TYR A 91 1584 1666 1836 -73 -137 -188 C ATOM 757 CZ TYR A 91 11.739 39.575 31.573 1.00 13.09 C ANISOU 757 CZ TYR A 91 1767 1521 1684 157 -70 -158 C ATOM 758 OH TYR A 91 12.136 38.337 31.134 1.00 13.74 O ANISOU 758 OH TYR A 91 1772 1739 1709 155 116 -231 O ATOM 759 N ILE A 92 8.369 43.548 30.547 1.00 14.01 N ANISOU 759 N ILE A 92 1711 1872 1740 -9 -114 -51 N ATOM 760 CA ILE A 92 7.720 42.927 29.380 1.00 14.46 C ANISOU 760 CA ILE A 92 1834 1873 1784 -76 -3 -121 C ATOM 761 C ILE A 92 7.885 43.821 28.153 1.00 15.53 C ANISOU 761 C ILE A 92 1823 2214 1861 -95 114 -130 C ATOM 762 O ILE A 92 8.196 43.353 27.068 1.00 17.08 O ANISOU 762 O ILE A 92 2221 2383 1884 -145 164 -227 O ATOM 763 CB ILE A 92 6.227 42.622 29.636 1.00 14.69 C ANISOU 763 CB ILE A 92 1727 2082 1770 -79 -83 -183 C ATOM 764 CG1 ILE A 92 6.073 41.523 30.679 1.00 14.82 C ANISOU 764 CG1 ILE A 92 1863 1848 1918 -272 -194 -219 C ATOM 765 CG2 ILE A 92 5.559 42.177 28.366 1.00 16.69 C ANISOU 765 CG2 ILE A 92 2026 2325 1990 -191 -100 -145 C ATOM 766 CD1 ILE A 92 4.646 41.286 31.124 1.00 15.76 C ANISOU 766 CD1 ILE A 92 1840 2022 2125 -30 -94 -167 C ATOM 767 N GLU A 93 7.690 45.121 28.365 1.00 15.36 N ANISOU 767 N GLU A 93 2001 2066 1769 177 10 20 N ATOM 768 CA GLU A 93 7.785 46.089 27.276 1.00 17.19 C ANISOU 768 CA GLU A 93 2188 2216 2124 71 -26 175 C ATOM 769 C GLU A 93 9.191 46.215 26.734 1.00 18.37 C ANISOU 769 C GLU A 93 2285 2551 2144 -33 71 -112 C ATOM 770 O GLU A 93 9.373 46.596 25.569 1.00 20.11 O ANISOU 770 O GLU A 93 2770 2796 2073 0 83 -36 O ATOM 771 CB GLU A 93 7.315 47.493 27.727 1.00 17.80 C ANISOU 771 CB GLU A 93 2305 2316 2141 103 -61 147 C ATOM 772 CG GLU A 93 5.856 47.544 28.146 1.00 21.68 C ANISOU 772 CG GLU A 93 2597 2759 2881 34 65 15 C ATOM 773 CD GLU A 93 5.443 48.853 28.805 1.00 24.33 C ANISOU 773 CD GLU A 93 2964 3008 3270 158 185 -109 C ATOM 774 OE1 GLU A 93 6.232 49.817 28.800 1.00 30.58 O ANISOU 774 OE1 GLU A 93 3667 3702 4248 -314 138 -258 O ATOM 775 OE2 GLU A 93 4.307 48.905 29.336 1.00 30.13 O ANISOU 775 OE2 GLU A 93 3329 4013 4103 186 180 -201 O ATOM 776 N THR A 94 10.180 45.999 27.567 1.00 17.42 N ANISOU 776 N THR A 94 2215 2120 2282 -92 128 51 N ATOM 777 CA THR A 94 11.591 46.193 27.239 1.00 17.68 C ANISOU 777 CA THR A 94 2166 2368 2183 -148 93 -52 C ATOM 778 C THR A 94 12.264 44.988 26.595 1.00 16.78 C ANISOU 778 C THR A 94 2053 2210 2110 -245 107 -39 C ATOM 779 O THR A 94 13.198 45.112 25.805 1.00 17.58 O ANISOU 779 O THR A 94 2229 2047 2403 -328 135 -242 O ATOM 780 CB THR A 94 12.326 46.458 28.582 1.00 18.74 C ANISOU 780 CB THR A 94 2372 2374 2374 -232 -67 129 C ATOM 781 OG1 THR A 94 11.738 47.580 29.216 1.00 22.20 O ANISOU 781 OG1 THR A 94 2304 3305 2825 -229 48 -149 O ATOM 782 CG2 THR A 94 13.757 46.859 28.325 1.00 21.26 C ANISOU 782 CG2 THR A 94 2490 2838 2750 -142 100 14 C ATOM 783 N SER A 95 11.792 43.799 26.937 1.00 16.54 N ANISOU 783 N SER A 95 1978 2207 2100 -328 228 -139 N ATOM 784 CA SER A 95 12.489 42.585 26.555 1.00 16.12 C ANISOU 784 CA SER A 95 1999 2250 1873 -162 43 -264 C ATOM 785 C SER A 95 12.491 42.405 25.039 1.00 16.80 C ANISOU 785 C SER A 95 2120 2293 1969 -112 -8 -167 C ATOM 786 O SER A 95 11.432 42.474 24.402 1.00 18.33 O ANISOU 786 O SER A 95 2249 2495 2221 26 -37 -127 O ATOM 787 CB SER A 95 11.830 41.374 27.182 1.00 15.52 C ANISOU 787 CB SER A 95 2024 2127 1745 -260 -87 -402 C ATOM 788 OG SER A 95 12.413 40.224 26.604 1.00 15.95 O ANISOU 788 OG SER A 95 2314 2165 1581 -178 -123 -296 O ATOM 789 N PRO A 96 13.663 42.131 24.458 1.00 17.45 N ANISOU 789 N PRO A 96 2111 2374 2142 -103 -41 -139 N ATOM 790 CA PRO A 96 13.748 41.783 23.053 1.00 17.42 C ANISOU 790 CA PRO A 96 2115 2379 2125 -130 39 -219 C ATOM 791 C PRO A 96 13.018 40.512 22.675 1.00 17.19 C ANISOU 791 C PRO A 96 2367 2377 1786 -160 28 -310 C ATOM 792 O PRO A 96 12.792 40.278 21.487 1.00 19.09 O ANISOU 792 O PRO A 96 2662 2778 1811 -85 -38 -371 O ATOM 793 CB PRO A 96 15.262 41.590 22.828 1.00 19.44 C ANISOU 793 CB PRO A 96 2175 2636 2575 -119 92 -328 C ATOM 794 CG PRO A 96 15.921 42.243 23.930 1.00 21.11 C ANISOU 794 CG PRO A 96 2318 3102 2600 -75 26 -215 C ATOM 795 CD PRO A 96 14.997 42.159 25.087 1.00 18.35 C ANISOU 795 CD PRO A 96 2072 2369 2531 -178 -51 -151 C ATOM 796 N PHE A 97 12.664 39.707 23.668 1.00 16.67 N ANISOU 796 N PHE A 97 2280 2338 1716 -253 -17 -248 N ATOM 797 CA PHE A 97 12.166 38.380 23.431 1.00 16.80 C ANISOU 797 CA PHE A 97 2239 2270 1874 -144 -3 -320 C ATOM 798 C PHE A 97 10.646 38.221 23.523 1.00 16.35 C ANISOU 798 C PHE A 97 2258 2140 1814 -232 -19 -226 C ATOM 799 O PHE A 97 10.111 37.172 23.151 1.00 18.27 O ANISOU 799 O PHE A 97 2326 2433 2180 -438 -126 -533 O ATOM 800 CB PHE A 97 12.885 37.410 24.371 1.00 17.90 C ANISOU 800 CB PHE A 97 2513 2160 2126 -197 18 -411 C ATOM 801 CG PHE A 97 14.362 37.459 24.233 1.00 18.39 C ANISOU 801 CG PHE A 97 2361 2197 2429 -137 -220 -322 C ATOM 802 CD1 PHE A 97 14.948 37.043 23.042 1.00 20.72 C ANISOU 802 CD1 PHE A 97 2739 2527 2605 7 -58 -220 C ATOM 803 CD2 PHE A 97 15.172 38.035 25.208 1.00 17.53 C ANISOU 803 CD2 PHE A 97 2454 2389 1817 -176 -49 -184 C ATOM 804 CE1 PHE A 97 16.337 37.133 22.856 1.00 22.22 C ANISOU 804 CE1 PHE A 97 2757 3064 2621 19 130 -423 C ATOM 805 CE2 PHE A 97 16.549 38.127 25.037 1.00 20.65 C ANISOU 805 CE2 PHE A 97 2493 2763 2590 -57 -157 -296 C ATOM 806 CZ PHE A 97 17.139 37.690 23.852 1.00 22.47 C ANISOU 806 CZ PHE A 97 2597 3109 2831 -34 -77 -234 C ATOM 807 N LEU A 98 9.963 39.272 23.974 1.00 17.33 N ANISOU 807 N LEU A 98 2242 2321 2018 -233 -23 -343 N ATOM 808 CA LEU A 98 8.546 39.218 24.312 1.00 17.48 C ANISOU 808 CA LEU A 98 2256 2357 2027 -238 -24 -203 C ATOM 809 C LEU A 98 7.673 40.057 23.385 1.00 17.75 C ANISOU 809 C LEU A 98 2386 2356 2000 -225 -55 -97 C ATOM 810 O LEU A 98 6.525 40.370 23.722 1.00 18.41 O ANISOU 810 O LEU A 98 2419 2713 1859 -307 -185 -107 O ATOM 811 CB LEU A 98 8.367 39.650 25.768 1.00 17.51 C ANISOU 811 CB LEU A 98 2176 2387 2090 -230 -7 -278 C ATOM 812 CG LEU A 98 9.094 38.743 26.783 1.00 15.83 C ANISOU 812 CG LEU A 98 1922 2323 1768 -274 -31 -359 C ATOM 813 CD1 LEU A 98 8.930 39.261 28.183 1.00 15.71 C ANISOU 813 CD1 LEU A 98 2139 1990 1840 -93 55 -221 C ATOM 814 CD2 LEU A 98 8.629 37.309 26.677 1.00 17.40 C ANISOU 814 CD2 LEU A 98 2387 2186 2035 -155 -268 -551 C ATOM 815 N LYS A 99 8.194 40.406 22.206 1.00 19.60 N ANISOU 815 N LYS A 99 2580 2686 2178 -134 -3 63 N ATOM 816 CA LYS A 99 7.492 41.337 21.325 1.00 20.92 C ANISOU 816 CA LYS A 99 2772 2763 2413 -65 -106 96 C ATOM 817 C LYS A 99 6.214 40.769 20.706 1.00 20.93 C ANISOU 817 C LYS A 99 2848 2806 2297 -95 -143 37 C ATOM 818 O LYS A 99 5.287 41.535 20.448 1.00 23.17 O ANISOU 818 O LYS A 99 3076 3045 2682 1 -317 -29 O ATOM 819 CB LYS A 99 8.414 41.884 20.217 1.00 22.05 C ANISOU 819 CB LYS A 99 2938 2899 2539 -32 43 88 C ATOM 820 CG LYS A 99 9.642 42.587 20.777 1.00 25.02 C ANISOU 820 CG LYS A 99 3137 3340 3028 -42 -78 -37 C ATOM 821 CD LYS A 99 10.549 43.136 19.680 1.00 24.85 C ANISOU 821 CD LYS A 99 3051 3303 3087 -102 -29 39 C ATOM 822 CE LYS A 99 11.934 43.471 20.265 1.00 27.80 C ANISOU 822 CE LYS A 99 3243 3687 3631 -128 -117 -80 C ATOM 823 NZ LYS A 99 12.844 44.110 19.278 1.00 30.41 N ANISOU 823 NZ LYS A 99 3603 4041 3910 -191 87 -54 N ATOM 824 N ILE A 100 6.142 39.470 20.457 1.00 22.17 N ANISOU 824 N ILE A 100 2848 3028 2548 -72 -104 47 N ATOM 825 CA ILE A 100 4.919 38.890 19.872 1.00 21.78 C ANISOU 825 CA ILE A 100 2816 2972 2484 -121 -196 121 C ATOM 826 C ILE A 100 3.839 38.910 20.927 1.00 21.18 C ANISOU 826 C ILE A 100 2700 2705 2642 -75 -193 130 C ATOM 827 O ILE A 100 4.054 38.383 22.013 1.00 21.67 O ANISOU 827 O ILE A 100 2754 3049 2429 -177 -296 286 O ATOM 828 CB ILE A 100 5.112 37.433 19.390 1.00 23.28 C ANISOU 828 CB ILE A 100 2912 3158 2773 -43 -178 64 C ATOM 829 CG1 ILE A 100 5.944 37.353 18.118 1.00 26.34 C ANISOU 829 CG1 ILE A 100 3403 3411 3192 -116 50 -7 C ATOM 830 CG2 ILE A 100 3.750 36.810 19.008 1.00 23.95 C ANISOU 830 CG2 ILE A 100 3010 3126 2963 -144 -63 -38 C ATOM 831 CD1 ILE A 100 7.198 38.091 18.118 1.00 29.15 C ANISOU 831 CD1 ILE A 100 3569 3784 3721 -89 -73 -76 C ATOM 832 N GLY A 101 2.700 39.519 20.640 1.00 21.78 N ANISOU 832 N GLY A 101 2761 3083 2430 -108 -271 159 N ATOM 833 CA GLY A 101 1.573 39.500 21.572 1.00 22.48 C ANISOU 833 CA GLY A 101 2829 2985 2725 -106 -142 62 C ATOM 834 C GLY A 101 1.851 40.205 22.879 1.00 22.51 C ANISOU 834 C GLY A 101 2856 3037 2657 -127 -149 136 C ATOM 835 O GLY A 101 1.360 39.804 23.931 1.00 21.57 O ANISOU 835 O GLY A 101 2702 2885 2606 -105 -169 143 O ATOM 836 N VAL A 102 2.620 41.281 22.820 1.00 21.64 N ANISOU 836 N VAL A 102 2776 3006 2441 -150 -229 135 N ATOM 837 CA VAL A 102 3.090 41.916 24.048 1.00 20.73 C ANISOU 837 CA VAL A 102 2713 2722 2438 -96 -251 275 C ATOM 838 C VAL A 102 1.933 42.409 24.931 1.00 19.90 C ANISOU 838 C VAL A 102 2578 2567 2413 -164 -272 347 C ATOM 839 O VAL A 102 1.998 42.272 26.158 1.00 21.29 O ANISOU 839 O VAL A 102 2706 2658 2722 -327 -215 312 O ATOM 840 CB VAL A 102 4.100 43.059 23.716 1.00 21.57 C ANISOU 840 CB VAL A 102 2821 2938 2434 -209 -140 173 C ATOM 841 CG1 VAL A 102 3.427 44.231 23.061 1.00 22.01 C ANISOU 841 CG1 VAL A 102 2749 2993 2619 -117 -215 38 C ATOM 842 CG2 VAL A 102 4.860 43.456 24.969 1.00 23.08 C ANISOU 842 CG2 VAL A 102 2811 3337 2621 -159 -224 53 C ATOM 843 N GLU A 103 0.844 42.900 24.320 1.00 20.08 N ANISOU 843 N GLU A 103 2705 2587 2337 -117 -266 333 N ATOM 844 CA GLU A 103 -0.272 43.419 25.120 1.00 20.65 C ANISOU 844 CA GLU A 103 2632 2672 2541 -88 -219 242 C ATOM 845 C GLU A 103 -0.969 42.307 25.910 1.00 21.02 C ANISOU 845 C GLU A 103 2536 2729 2720 -99 -201 159 C ATOM 846 O GLU A 103 -1.334 42.498 27.049 1.00 20.38 O ANISOU 846 O GLU A 103 2383 2512 2849 -178 -253 17 O ATOM 847 CB GLU A 103 -1.255 44.232 24.275 1.00 22.19 C ANISOU 847 CB GLU A 103 2793 2926 2712 -96 -149 169 C ATOM 848 CG GLU A 103 -0.640 45.507 23.721 1.00 23.39 C ANISOU 848 CG GLU A 103 2969 2882 3036 -28 -108 225 C ATOM 849 CD GLU A 103 -0.034 46.424 24.788 1.00 25.55 C ANISOU 849 CD GLU A 103 3316 3095 3295 -28 -37 34 C ATOM 850 OE1 GLU A 103 -0.624 46.592 25.880 1.00 26.58 O ANISOU 850 OE1 GLU A 103 3265 3072 3760 -62 59 -22 O ATOM 851 OE2 GLU A 103 1.050 46.986 24.528 1.00 28.23 O ANISOU 851 OE2 GLU A 103 3281 3714 3729 -158 -94 -50 O ATOM 852 N ALA A 104 -1.122 41.139 25.300 1.00 20.16 N ANISOU 852 N ALA A 104 2542 2656 2459 -111 -298 170 N ATOM 853 CA ALA A 104 -1.736 40.008 26.000 1.00 20.16 C ANISOU 853 CA ALA A 104 2442 2695 2520 -132 -243 107 C ATOM 854 C ALA A 104 -0.830 39.433 27.088 1.00 18.88 C ANISOU 854 C ALA A 104 2224 2564 2386 -293 -229 75 C ATOM 855 O ALA A 104 -1.323 38.943 28.104 1.00 18.25 O ANISOU 855 O ALA A 104 2297 2383 2254 -438 -96 -1 O ATOM 856 CB ALA A 104 -2.137 38.952 25.008 1.00 21.49 C ANISOU 856 CB ALA A 104 2592 2824 2748 -241 -152 -25 C ATOM 857 N ARG A 105 0.490 39.486 26.882 1.00 18.83 N ANISOU 857 N ARG A 105 2249 2463 2442 -144 -143 230 N ATOM 858 CA ARG A 105 1.444 39.126 27.934 1.00 18.16 C ANISOU 858 CA ARG A 105 2215 2312 2371 -91 -196 195 C ATOM 859 C ARG A 105 1.244 40.036 29.118 1.00 18.15 C ANISOU 859 C ARG A 105 1999 2351 2545 -103 -132 111 C ATOM 860 O ARG A 105 1.227 39.569 30.241 1.00 17.86 O ANISOU 860 O ARG A 105 1923 2158 2704 -281 -304 184 O ATOM 861 CB ARG A 105 2.899 39.287 27.499 1.00 17.93 C ANISOU 861 CB ARG A 105 2218 2343 2250 -108 -221 123 C ATOM 862 CG ARG A 105 3.349 38.330 26.436 1.00 18.57 C ANISOU 862 CG ARG A 105 2325 2249 2479 -235 -146 92 C ATOM 863 CD ARG A 105 4.830 38.461 26.130 1.00 18.18 C ANISOU 863 CD ARG A 105 2216 2297 2393 -1 -42 -25 C ATOM 864 NE ARG A 105 5.150 37.927 24.828 1.00 18.85 N ANISOU 864 NE ARG A 105 2536 2296 2329 -156 -113 189 N ATOM 865 CZ ARG A 105 5.270 36.636 24.572 1.00 16.87 C ANISOU 865 CZ ARG A 105 2193 2325 1889 -198 -97 -68 C ATOM 866 NH1 ARG A 105 5.188 35.731 25.548 1.00 17.59 N ANISOU 866 NH1 ARG A 105 2365 2155 2163 -234 11 -146 N ATOM 867 NH2 ARG A 105 5.513 36.252 23.331 1.00 20.20 N ANISOU 867 NH2 ARG A 105 3079 2520 2075 -234 -241 48 N ATOM 868 N LYS A 106 1.132 41.348 28.873 1.00 18.06 N ANISOU 868 N LYS A 106 2093 2290 2478 -149 -213 251 N ATOM 869 CA LYS A 106 0.928 42.298 29.968 1.00 18.05 C ANISOU 869 CA LYS A 106 2222 2240 2395 -45 -278 193 C ATOM 870 C LYS A 106 -0.380 41.978 30.701 1.00 18.21 C ANISOU 870 C LYS A 106 2201 2142 2576 -93 -242 55 C ATOM 871 O LYS A 106 -0.438 41.984 31.915 1.00 18.42 O ANISOU 871 O LYS A 106 2063 2197 2738 -246 -153 83 O ATOM 872 CB LYS A 106 0.919 43.746 29.475 1.00 19.00 C ANISOU 872 CB LYS A 106 2287 2326 2606 5 -181 198 C ATOM 873 CG LYS A 106 2.259 44.227 28.927 1.00 19.72 C ANISOU 873 CG LYS A 106 2401 2337 2752 -73 -97 90 C ATOM 874 CD LYS A 106 2.213 45.638 28.352 1.00 22.24 C ANISOU 874 CD LYS A 106 2697 2696 3058 -235 -17 163 C ATOM 875 CE LYS A 106 2.153 46.633 29.478 1.00 25.79 C ANISOU 875 CE LYS A 106 3250 3140 3410 -9 -56 45 C ATOM 876 NZ LYS A 106 1.986 48.024 28.981 1.00 25.23 N ANISOU 876 NZ LYS A 106 3276 2673 3635 -173 79 18 N ATOM 877 N LYS A 107 -1.431 41.669 29.950 1.00 19.43 N ANISOU 877 N LYS A 107 2430 2287 2664 -81 -184 163 N ATOM 878 CA LYS A 107 -2.707 41.380 30.571 1.00 19.65 C ANISOU 878 CA LYS A 107 2360 2383 2723 -81 -158 144 C ATOM 879 C LYS A 107 -2.659 40.109 31.416 1.00 17.56 C ANISOU 879 C LYS A 107 1910 2128 2633 -140 -272 98 C ATOM 880 O LYS A 107 -3.240 40.060 32.486 1.00 18.33 O ANISOU 880 O LYS A 107 1822 2169 2973 -212 -134 132 O ATOM 881 CB LYS A 107 -3.761 41.262 29.494 1.00 18.97 C ANISOU 881 CB LYS A 107 2344 2239 2626 103 -232 245 C ATOM 882 CG LYS A 107 -5.105 40.723 29.914 1.00 24.64 C ANISOU 882 CG LYS A 107 2964 3149 3246 -206 96 50 C ATOM 883 CD LYS A 107 -6.155 41.137 28.903 1.00 26.05 C ANISOU 883 CD LYS A 107 3029 3396 3472 -185 -66 11 C ATOM 884 CE LYS A 107 -7.453 40.338 29.003 1.00 27.75 C ANISOU 884 CE LYS A 107 3127 3722 3694 -251 49 0 C ATOM 885 NZ LYS A 107 -8.545 41.079 28.328 1.00 30.25 N ANISOU 885 NZ LYS A 107 3517 4166 3808 -191 -20 7 N ATOM 886 N ARG A 108 -1.940 39.093 30.965 1.00 18.08 N ANISOU 886 N ARG A 108 1954 2172 2742 -170 -166 137 N ATOM 887 CA ARG A 108 -1.819 37.884 31.784 1.00 19.09 C ANISOU 887 CA ARG A 108 2161 2274 2817 -85 -159 229 C ATOM 888 C ARG A 108 -1.036 38.156 33.047 1.00 18.50 C ANISOU 888 C ARG A 108 2018 2240 2770 -278 -146 222 C ATOM 889 O ARG A 108 -1.394 37.723 34.135 1.00 19.14 O ANISOU 889 O ARG A 108 2185 2212 2875 -236 -76 277 O ATOM 890 CB ARG A 108 -1.120 36.762 31.049 1.00 18.62 C ANISOU 890 CB ARG A 108 2169 2224 2680 -167 -241 102 C ATOM 891 CG ARG A 108 -0.906 35.557 31.952 1.00 20.64 C ANISOU 891 CG ARG A 108 2506 2443 2894 -63 -163 246 C ATOM 892 CD ARG A 108 -0.348 34.394 31.269 1.00 22.00 C ANISOU 892 CD ARG A 108 2433 2697 3227 -40 -127 177 C ATOM 893 NE ARG A 108 -1.392 33.729 30.531 1.00 23.02 N ANISOU 893 NE ARG A 108 2713 3148 2884 0 -370 67 N ATOM 894 CZ ARG A 108 -1.227 32.612 29.861 1.00 27.81 C ANISOU 894 CZ ARG A 108 3462 3427 3675 -123 32 -269 C ATOM 895 NH1 ARG A 108 -0.039 32.051 29.725 1.00 29.48 N ANISOU 895 NH1 ARG A 108 3413 3805 3984 -108 -70 -2 N ATOM 896 NH2 ARG A 108 -2.264 32.086 29.249 1.00 28.69 N ANISOU 896 NH2 ARG A 108 3322 3747 3830 -76 -147 -230 N ATOM 897 N ALA A 109 0.085 38.845 32.909 1.00 17.81 N ANISOU 897 N ALA A 109 1929 2239 2598 -304 -204 231 N ATOM 898 CA ALA A 109 0.889 39.181 34.061 1.00 18.12 C ANISOU 898 CA ALA A 109 1986 2344 2552 -397 -162 284 C ATOM 899 C ALA A 109 0.059 39.991 35.040 1.00 17.78 C ANISOU 899 C ALA A 109 1872 2100 2782 -434 -310 231 C ATOM 900 O ALA A 109 0.112 39.791 36.273 1.00 19.97 O ANISOU 900 O ALA A 109 1987 2586 3014 -171 -253 523 O ATOM 901 CB ALA A 109 2.112 39.922 33.659 1.00 18.50 C ANISOU 901 CB ALA A 109 2170 2530 2325 -489 -210 329 C ATOM 902 N LEU A 110 -0.740 40.908 34.512 1.00 18.10 N ANISOU 902 N LEU A 110 1939 2166 2769 -384 -259 300 N ATOM 903 CA LEU A 110 -1.572 41.723 35.376 1.00 17.14 C ANISOU 903 CA LEU A 110 1871 1887 2754 -395 -241 288 C ATOM 904 C LEU A 110 -2.551 40.895 36.215 1.00 16.59 C ANISOU 904 C LEU A 110 1695 1716 2891 -340 -130 208 C ATOM 905 O LEU A 110 -2.766 41.178 37.394 1.00 18.82 O ANISOU 905 O LEU A 110 1956 1985 3208 -291 -197 -6 O ATOM 906 CB LEU A 110 -2.310 42.736 34.532 1.00 19.03 C ANISOU 906 CB LEU A 110 2198 2249 2784 -228 -291 136 C ATOM 907 CG LEU A 110 -1.775 44.152 34.527 1.00 20.70 C ANISOU 907 CG LEU A 110 2761 2421 2683 -126 -190 38 C ATOM 908 CD1 LEU A 110 -2.615 44.913 33.561 1.00 21.44 C ANISOU 908 CD1 LEU A 110 3119 2455 2568 -102 -67 95 C ATOM 909 CD2 LEU A 110 -1.820 44.785 35.896 1.00 19.98 C ANISOU 909 CD2 LEU A 110 2695 2295 2599 218 138 -192 C ATOM 910 N LYS A 111 -3.111 39.843 35.626 1.00 17.63 N ANISOU 910 N LYS A 111 2013 1917 2766 -365 -237 98 N ATOM 911 CA LYS A 111 -4.020 38.958 36.347 1.00 17.50 C ANISOU 911 CA LYS A 111 1857 1967 2825 -257 8 83 C ATOM 912 C LYS A 111 -3.318 38.343 37.559 1.00 15.96 C ANISOU 912 C LYS A 111 1919 1547 2598 -267 34 85 C ATOM 913 O LYS A 111 -3.936 38.180 38.612 1.00 17.96 O ANISOU 913 O LYS A 111 1844 2087 2892 -117 255 -33 O ATOM 914 CB LYS A 111 -4.542 37.827 35.442 1.00 18.81 C ANISOU 914 CB LYS A 111 2202 2204 2740 -388 -13 157 C ATOM 915 CG LYS A 111 -5.515 38.301 34.375 1.00 21.25 C ANISOU 915 CG LYS A 111 2581 2454 3037 -217 -64 138 C ATOM 916 CD LYS A 111 -6.029 37.157 33.488 1.00 23.31 C ANISOU 916 CD LYS A 111 2984 2998 2874 -368 -114 -42 C ATOM 917 CE LYS A 111 -7.023 37.599 32.454 1.00 27.23 C ANISOU 917 CE LYS A 111 3442 3674 3227 -195 -154 -6 C ATOM 918 NZ LYS A 111 -7.364 36.454 31.542 1.00 30.37 N ANISOU 918 NZ LYS A 111 4067 3768 3703 -334 31 -236 N ATOM 919 N ALA A 112 -2.035 38.008 37.409 1.00 15.70 N ANISOU 919 N ALA A 112 1681 1814 2468 -155 136 -81 N ATOM 920 CA ALA A 112 -1.277 37.347 38.453 1.00 15.46 C ANISOU 920 CA ALA A 112 1747 1572 2553 -137 -69 -54 C ATOM 921 C ALA A 112 -0.397 38.287 39.253 1.00 15.47 C ANISOU 921 C ALA A 112 1694 1628 2555 6 86 -50 C ATOM 922 O ALA A 112 0.339 37.832 40.102 1.00 16.24 O ANISOU 922 O ALA A 112 1914 1833 2422 88 68 -23 O ATOM 923 CB ALA A 112 -0.404 36.284 37.816 1.00 16.02 C ANISOU 923 CB ALA A 112 1676 1887 2522 -111 -102 -251 C ATOM 924 N CYS A 113 -0.465 39.587 38.991 1.00 15.36 N ANISOU 924 N CYS A 113 1748 1745 2340 -379 -22 -70 N ATOM 925 CA CYS A 113 0.515 40.515 39.528 1.00 16.77 C ANISOU 925 CA CYS A 113 1832 1854 2682 -410 61 -12 C ATOM 926 C CYS A 113 0.641 40.531 41.049 1.00 17.45 C ANISOU 926 C CYS A 113 1952 1959 2718 -160 -105 72 C ATOM 927 O CYS A 113 1.739 40.692 41.561 1.00 19.77 O ANISOU 927 O CYS A 113 2052 2476 2983 -251 -101 -364 O ATOM 928 CB CYS A 113 0.222 41.960 39.067 1.00 17.91 C ANISOU 928 CB CYS A 113 1885 2280 2639 -467 138 -154 C ATOM 929 SG CYS A 113 1.294 42.590 37.811 1.00 19.74 S ANISOU 929 SG CYS A 113 1946 2369 3183 -559 28 90 S ATOM 930 N ASP A 114 -0.475 40.369 41.744 1.00 16.78 N ANISOU 930 N ASP A 114 2067 1725 2581 -19 -128 -105 N ATOM 931 CA ASP A 114 -0.514 40.453 43.199 1.00 16.57 C ANISOU 931 CA ASP A 114 2120 1620 2554 3 108 -38 C ATOM 932 C ASP A 114 -0.536 39.107 43.873 1.00 17.08 C ANISOU 932 C ASP A 114 2369 1669 2450 30 46 -19 C ATOM 933 O ASP A 114 -0.603 39.044 45.087 1.00 20.13 O ANISOU 933 O ASP A 114 3197 1926 2525 182 56 -190 O ATOM 934 CB ASP A 114 -1.748 41.233 43.646 1.00 18.02 C ANISOU 934 CB ASP A 114 2442 1584 2818 146 80 -46 C ATOM 935 CG ASP A 114 -1.811 42.623 43.078 1.00 18.93 C ANISOU 935 CG ASP A 114 2144 1805 3242 77 175 242 C ATOM 936 OD1 ASP A 114 -0.750 43.279 42.869 1.00 20.41 O ANISOU 936 OD1 ASP A 114 2678 1889 3188 -188 188 -6 O ATOM 937 OD2 ASP A 114 -2.924 43.140 42.851 1.00 29.19 O ANISOU 937 OD2 ASP A 114 3025 3193 4873 -123 363 423 O ATOM 938 N TYR A 115 -0.481 38.031 43.103 1.00 15.23 N ANISOU 938 N TYR A 115 1981 1665 2138 46 -48 -80 N ATOM 939 CA TYR A 115 -0.610 36.708 43.619 1.00 14.50 C ANISOU 939 CA TYR A 115 1701 1615 2192 92 7 -70 C ATOM 940 C TYR A 115 0.742 36.256 44.159 1.00 14.16 C ANISOU 940 C TYR A 115 1870 1624 1886 -32 6 -62 C ATOM 941 O TYR A 115 1.760 36.322 43.483 1.00 14.92 O ANISOU 941 O TYR A 115 1787 1962 1918 108 -23 60 O ATOM 942 CB TYR A 115 -1.096 35.762 42.535 1.00 14.82 C ANISOU 942 CB TYR A 115 1752 1762 2114 -18 -83 -70 C ATOM 943 CG TYR A 115 -1.078 34.318 42.996 1.00 14.33 C ANISOU 943 CG TYR A 115 1780 1601 2064 172 -148 -8 C ATOM 944 CD1 TYR A 115 -1.953 33.864 43.974 1.00 14.82 C ANISOU 944 CD1 TYR A 115 1742 1803 2085 138 -212 -137 C ATOM 945 CD2 TYR A 115 -0.159 33.407 42.479 1.00 15.08 C ANISOU 945 CD2 TYR A 115 1859 1839 2031 59 -167 -77 C ATOM 946 CE1 TYR A 115 -1.932 32.575 44.398 1.00 14.25 C ANISOU 946 CE1 TYR A 115 1878 1634 1902 -7 -204 66 C ATOM 947 CE2 TYR A 115 -0.128 32.093 42.927 1.00 15.21 C ANISOU 947 CE2 TYR A 115 1726 1792 2259 99 -279 -84 C ATOM 948 CZ TYR A 115 -0.996 31.675 43.892 1.00 14.30 C ANISOU 948 CZ TYR A 115 1717 1569 2145 153 -463 -168 C ATOM 949 OH TYR A 115 -0.916 30.412 44.357 1.00 15.89 O ANISOU 949 OH TYR A 115 2042 1544 2451 311 -475 -47 O ATOM 950 N VAL A 116 0.709 35.784 45.389 1.00 14.34 N ANISOU 950 N VAL A 116 1907 1687 1852 150 16 -87 N ATOM 951 CA VAL A 116 1.904 35.290 46.049 1.00 15.24 C ANISOU 951 CA VAL A 116 2081 1688 2022 132 -187 -46 C ATOM 952 C VAL A 116 1.833 33.759 46.085 1.00 15.00 C ANISOU 952 C VAL A 116 1966 1680 2053 191 -161 -23 C ATOM 953 O VAL A 116 0.984 33.207 46.726 1.00 16.63 O ANISOU 953 O VAL A 116 2191 1863 2264 239 -55 57 O ATOM 954 CB VAL A 116 2.043 35.850 47.451 1.00 17.47 C ANISOU 954 CB VAL A 116 2645 1961 2029 142 -312 -148 C ATOM 955 CG1 VAL A 116 3.312 35.352 48.042 1.00 20.77 C ANISOU 955 CG1 VAL A 116 3078 2348 2466 350 -376 -236 C ATOM 956 CG2 VAL A 116 1.975 37.404 47.447 1.00 17.86 C ANISOU 956 CG2 VAL A 116 2759 2050 1975 110 -380 -202 C ATOM 957 N PRO A 117 2.689 33.057 45.354 1.00 14.44 N ANISOU 957 N PRO A 117 1886 1668 1929 162 -320 -114 N ATOM 958 CA PRO A 117 2.608 31.599 45.327 1.00 14.23 C ANISOU 958 CA PRO A 117 1674 1632 2100 99 -301 -89 C ATOM 959 C PRO A 117 2.994 30.992 46.664 1.00 14.99 C ANISOU 959 C PRO A 117 1794 1677 2223 89 -334 -26 C ATOM 960 O PRO A 117 3.851 31.524 47.349 1.00 15.86 O ANISOU 960 O PRO A 117 1991 1925 2110 -14 -297 21 O ATOM 961 CB PRO A 117 3.571 31.226 44.210 1.00 15.61 C ANISOU 961 CB PRO A 117 2076 1756 2096 173 -228 -56 C ATOM 962 CG PRO A 117 4.607 32.335 44.230 1.00 16.30 C ANISOU 962 CG PRO A 117 2180 1923 2090 119 -54 -130 C ATOM 963 CD PRO A 117 3.813 33.577 44.552 1.00 15.43 C ANISOU 963 CD PRO A 117 2012 1826 2022 99 -274 -108 C ATOM 964 N ASN A 118 2.387 29.846 46.985 1.00 15.75 N ANISOU 964 N ASN A 118 1720 1754 2510 32 -171 -130 N ATOM 965 CA ASN A 118 2.769 29.091 48.169 1.00 16.51 C ANISOU 965 CA ASN A 118 1914 1914 2445 71 -22 -13 C ATOM 966 C ASN A 118 3.729 28.010 47.739 1.00 14.92 C ANISOU 966 C ASN A 118 1973 1846 1849 100 -36 38 C ATOM 967 O ASN A 118 3.346 26.984 47.133 1.00 15.70 O ANISOU 967 O ASN A 118 1939 1813 2213 -2 -152 -47 O ATOM 968 CB ASN A 118 1.596 28.439 48.973 1.00 19.60 C ANISOU 968 CB ASN A 118 2474 2023 2949 142 179 -247 C ATOM 969 CG ASN A 118 2.110 27.736 50.283 1.00 19.15 C ANISOU 969 CG ASN A 118 2275 2261 2738 -181 167 295 C ATOM 970 OD1 ASN A 118 3.304 27.543 50.499 1.00 22.32 O ANISOU 970 OD1 ASN A 118 3159 2349 2972 474 620 45 O ATOM 971 ND2 ASN A 118 1.194 27.520 51.226 1.00 23.38 N ANISOU 971 ND2 ASN A 118 2976 3282 2624 -329 266 -62 N ATOM 972 N LEU A 119 5.000 28.227 48.049 1.00 14.38 N ANISOU 972 N LEU A 119 1965 1601 1897 64 -261 48 N ATOM 973 CA LEU A 119 6.038 27.342 47.623 1.00 14.08 C ANISOU 973 CA LEU A 119 1783 1733 1832 99 -187 122 C ATOM 974 C LEU A 119 6.045 25.993 48.335 1.00 14.94 C ANISOU 974 C LEU A 119 1854 1737 2084 254 -163 214 C ATOM 975 O LEU A 119 6.680 25.066 47.871 1.00 16.30 O ANISOU 975 O LEU A 119 2187 1782 2222 292 6 107 O ATOM 976 CB LEU A 119 7.404 27.994 47.771 1.00 15.32 C ANISOU 976 CB LEU A 119 2165 1901 1753 32 -197 95 C ATOM 977 CG LEU A 119 7.577 29.314 47.032 1.00 15.56 C ANISOU 977 CG LEU A 119 2187 1776 1947 -94 -98 14 C ATOM 978 CD1 LEU A 119 9.000 29.816 47.214 1.00 18.11 C ANISOU 978 CD1 LEU A 119 2647 2075 2158 -309 -132 109 C ATOM 979 CD2 LEU A 119 7.252 29.212 45.555 1.00 17.15 C ANISOU 979 CD2 LEU A 119 2633 1987 1894 -62 -199 85 C ATOM 980 N GLU A 120 5.355 25.895 49.479 1.00 14.01 N ANISOU 980 N GLU A 120 1704 1681 1938 188 -278 225 N ATOM 981 CA GLU A 120 5.208 24.647 50.207 1.00 14.38 C ANISOU 981 CA GLU A 120 1731 1774 1955 152 -218 199 C ATOM 982 C GLU A 120 3.886 23.967 49.954 1.00 15.30 C ANISOU 982 C GLU A 120 1738 2017 2057 164 -378 282 C ATOM 983 O GLU A 120 3.632 22.914 50.536 1.00 17.66 O ANISOU 983 O GLU A 120 2429 1934 2345 -55 -568 523 O ATOM 984 CB GLU A 120 5.573 24.844 51.694 1.00 14.90 C ANISOU 984 CB GLU A 120 1763 1779 2118 191 -173 299 C ATOM 985 CG GLU A 120 7.074 25.099 51.787 1.00 15.76 C ANISOU 985 CG GLU A 120 1576 2003 2407 1 -215 161 C ATOM 986 CD GLU A 120 7.633 25.328 53.180 1.00 15.13 C ANISOU 986 CD GLU A 120 1694 1917 2137 87 -123 4 C ATOM 987 OE1 GLU A 120 6.850 25.646 54.089 1.00 17.48 O ANISOU 987 OE1 GLU A 120 1886 2295 2457 53 -87 13 O ATOM 988 OE2 GLU A 120 8.869 25.211 53.346 1.00 15.18 O ANISOU 988 OE2 GLU A 120 1487 1976 2305 31 -204 270 O ATOM 989 N ASP A 121 3.049 24.522 49.082 1.00 15.46 N ANISOU 989 N ASP A 121 2020 1830 2023 49 -404 276 N ATOM 990 CA ASP A 121 1.844 23.801 48.634 1.00 16.28 C ANISOU 990 CA ASP A 121 2048 2119 2017 -79 -365 309 C ATOM 991 C ASP A 121 1.680 24.077 47.154 1.00 15.52 C ANISOU 991 C ASP A 121 2123 1955 1820 60 -453 227 C ATOM 992 O ASP A 121 0.872 24.932 46.721 1.00 15.37 O ANISOU 992 O ASP A 121 2036 1939 1866 218 -301 227 O ATOM 993 CB ASP A 121 0.633 24.228 49.441 1.00 18.09 C ANISOU 993 CB ASP A 121 2273 2551 2046 -69 -420 363 C ATOM 994 CG ASP A 121 -0.576 23.379 49.173 1.00 20.15 C ANISOU 994 CG ASP A 121 2421 2799 2435 -250 -98 478 C ATOM 995 OD1 ASP A 121 -0.549 22.545 48.236 1.00 22.21 O ANISOU 995 OD1 ASP A 121 3162 2538 2736 -359 -799 640 O ATOM 996 OD2 ASP A 121 -1.580 23.458 49.921 1.00 26.66 O ANISOU 996 OD2 ASP A 121 2941 3968 3220 -499 134 457 O ATOM 997 N LEU A 122 2.512 23.400 46.364 1.00 17.23 N ANISOU 997 N LEU A 122 2407 1939 2198 408 -400 226 N ATOM 998 CA LEU A 122 2.488 23.630 44.921 1.00 16.94 C ANISOU 998 CA LEU A 122 2266 2010 2158 352 -300 -2 C ATOM 999 C LEU A 122 1.213 23.135 44.252 1.00 18.27 C ANISOU 999 C LEU A 122 2578 1920 2442 345 -426 -39 C ATOM 1000 O LEU A 122 0.780 23.689 43.243 1.00 17.69 O ANISOU 1000 O LEU A 122 2483 1942 2296 369 -538 97 O ATOM 1001 CB LEU A 122 3.791 23.158 44.230 1.00 20.20 C ANISOU 1001 CB LEU A 122 2602 2762 2308 499 -281 -208 C ATOM 1002 CG LEU A 122 5.055 24.002 44.559 1.00 21.35 C ANISOU 1002 CG LEU A 122 2245 3634 2232 509 -450 -435 C ATOM 1003 CD1 LEU A 122 6.280 23.363 43.861 1.00 24.98 C ANISOU 1003 CD1 LEU A 122 2649 4018 2822 546 -158 -377 C ATOM 1004 CD2 LEU A 122 4.935 25.413 44.149 1.00 23.28 C ANISOU 1004 CD2 LEU A 122 2416 3764 2664 -106 84 -449 C ATOM 1005 N GLY A 123 0.563 22.134 44.823 1.00 18.00 N ANISOU 1005 N GLY A 123 2535 2015 2287 180 -687 145 N ATOM 1006 CA GLY A 123 -0.746 21.728 44.293 1.00 17.81 C ANISOU 1006 CA GLY A 123 2543 1819 2404 -31 -474 168 C ATOM 1007 C GLY A 123 -1.833 22.776 44.445 1.00 16.32 C ANISOU 1007 C GLY A 123 2320 1650 2229 -57 -613 337 C ATOM 1008 O GLY A 123 -2.588 23.055 43.500 1.00 18.10 O ANISOU 1008 O GLY A 123 2599 1911 2368 5 -873 129 O ATOM 1009 N LEU A 124 -1.910 23.411 45.601 1.00 17.30 N ANISOU 1009 N LEU A 124 2330 2057 2185 -79 -541 416 N ATOM 1010 CA LEU A 124 -2.854 24.508 45.777 1.00 15.94 C ANISOU 1010 CA LEU A 124 2077 2023 1957 -147 -330 327 C ATOM 1011 C LEU A 124 -2.445 25.693 44.877 1.00 13.95 C ANISOU 1011 C LEU A 124 1996 1744 1559 -119 -295 206 C ATOM 1012 O LEU A 124 -3.311 26.310 44.230 1.00 14.59 O ANISOU 1012 O LEU A 124 1786 2004 1751 16 -308 295 O ATOM 1013 CB LEU A 124 -2.875 24.972 47.232 1.00 18.20 C ANISOU 1013 CB LEU A 124 2594 2237 2081 -68 -283 294 C ATOM 1014 CG LEU A 124 -3.725 26.199 47.571 1.00 20.55 C ANISOU 1014 CG LEU A 124 2957 2774 2077 122 -146 261 C ATOM 1015 CD1 LEU A 124 -5.196 26.012 47.203 1.00 22.92 C ANISOU 1015 CD1 LEU A 124 3087 3281 2339 111 79 279 C ATOM 1016 CD2 LEU A 124 -3.604 26.577 49.034 1.00 22.34 C ANISOU 1016 CD2 LEU A 124 3216 3029 2242 206 -135 133 C ATOM 1017 N THR A 125 -1.140 25.963 44.792 1.00 14.07 N ANISOU 1017 N THR A 125 1951 1776 1618 119 -410 144 N ATOM 1018 CA THR A 125 -0.678 27.024 43.941 1.00 13.59 C ANISOU 1018 CA THR A 125 1798 1542 1823 75 -313 32 C ATOM 1019 C THR A 125 -1.103 26.771 42.486 1.00 12.86 C ANISOU 1019 C THR A 125 1715 1565 1603 -1 -173 62 C ATOM 1020 O THR A 125 -1.557 27.690 41.824 1.00 13.30 O ANISOU 1020 O THR A 125 1742 1608 1701 53 -136 134 O ATOM 1021 CB THR A 125 0.830 27.176 44.084 1.00 14.12 C ANISOU 1021 CB THR A 125 1889 1536 1937 235 -245 -5 C ATOM 1022 OG1 THR A 125 1.122 27.650 45.411 1.00 15.73 O ANISOU 1022 OG1 THR A 125 2121 1742 2111 -31 -402 -83 O ATOM 1023 CG2 THR A 125 1.408 28.183 43.089 1.00 15.17 C ANISOU 1023 CG2 THR A 125 1701 1869 2193 173 -269 -32 C ATOM 1024 N LEU A 126 -0.965 25.537 42.015 1.00 13.52 N ANISOU 1024 N LEU A 126 1857 1614 1664 112 -273 59 N ATOM 1025 CA LEU A 126 -1.341 25.215 40.654 1.00 13.76 C ANISOU 1025 CA LEU A 126 1839 1637 1750 160 -100 33 C ATOM 1026 C LEU A 126 -2.856 25.438 40.461 1.00 13.73 C ANISOU 1026 C LEU A 126 1980 1480 1756 131 -174 64 C ATOM 1027 O LEU A 126 -3.298 26.018 39.464 1.00 13.74 O ANISOU 1027 O LEU A 126 1960 1482 1776 79 -203 33 O ATOM 1028 CB LEU A 126 -0.932 23.783 40.324 1.00 14.83 C ANISOU 1028 CB LEU A 126 1923 1784 1925 158 -346 -66 C ATOM 1029 CG LEU A 126 -1.316 23.288 38.922 1.00 15.72 C ANISOU 1029 CG LEU A 126 2079 1812 2080 353 -252 -176 C ATOM 1030 CD1 LEU A 126 -0.817 24.188 37.824 1.00 15.36 C ANISOU 1030 CD1 LEU A 126 2043 1907 1885 32 -163 -57 C ATOM 1031 CD2 LEU A 126 -0.833 21.889 38.725 1.00 16.66 C ANISOU 1031 CD2 LEU A 126 2337 1697 2295 161 -282 -61 C ATOM 1032 N ARG A 127 -3.646 24.989 41.432 1.00 14.06 N ANISOU 1032 N ARG A 127 1947 1677 1715 -57 -355 112 N ATOM 1033 CA ARG A 127 -5.107 25.227 41.336 1.00 14.10 C ANISOU 1033 CA ARG A 127 1812 1778 1768 -204 -166 190 C ATOM 1034 C ARG A 127 -5.424 26.710 41.295 1.00 11.94 C ANISOU 1034 C ARG A 127 1727 1596 1211 -96 -90 266 C ATOM 1035 O ARG A 127 -6.255 27.167 40.487 1.00 12.90 O ANISOU 1035 O ARG A 127 1663 1801 1437 7 -161 143 O ATOM 1036 CB ARG A 127 -5.795 24.539 42.473 1.00 16.39 C ANISOU 1036 CB ARG A 127 2178 2039 2011 -181 -166 272 C ATOM 1037 CG ARG A 127 -7.254 24.475 42.398 1.00 20.07 C ANISOU 1037 CG ARG A 127 2509 2583 2533 -25 12 217 C ATOM 1038 CD ARG A 127 -7.874 23.504 43.389 1.00 24.04 C ANISOU 1038 CD ARG A 127 2981 3001 3152 -439 163 116 C ATOM 1039 NE ARG A 127 -7.145 23.334 44.663 1.00 30.91 N ANISOU 1039 NE ARG A 127 3918 4084 3739 29 -128 132 N ATOM 1040 CZ ARG A 127 -6.230 22.375 44.921 1.00 32.42 C ANISOU 1040 CZ ARG A 127 4285 3926 4104 14 -46 105 C ATOM 1041 NH1 ARG A 127 -5.875 21.483 44.002 1.00 35.66 N ANISOU 1041 NH1 ARG A 127 4730 4443 4373 161 -47 57 N ATOM 1042 NH2 ARG A 127 -5.638 22.321 46.114 1.00 33.85 N ANISOU 1042 NH2 ARG A 127 4466 4230 4162 17 -103 73 N ATOM 1043 N GLN A 128 -4.790 27.486 42.167 1.00 12.72 N ANISOU 1043 N GLN A 128 1667 1713 1450 37 -242 150 N ATOM 1044 CA GLN A 128 -5.024 28.922 42.179 1.00 12.48 C ANISOU 1044 CA GLN A 128 1615 1765 1360 -25 -224 7 C ATOM 1045 C GLN A 128 -4.613 29.592 40.884 1.00 12.26 C ANISOU 1045 C GLN A 128 1525 1645 1487 0 -123 39 C ATOM 1046 O GLN A 128 -5.359 30.392 40.324 1.00 12.08 O ANISOU 1046 O GLN A 128 1715 1577 1297 24 -206 95 O ATOM 1047 CB GLN A 128 -4.327 29.548 43.381 1.00 13.59 C ANISOU 1047 CB GLN A 128 1775 1981 1407 159 -358 77 C ATOM 1048 CG GLN A 128 -4.952 29.110 44.694 1.00 13.37 C ANISOU 1048 CG GLN A 128 1929 1939 1210 189 -302 117 C ATOM 1049 CD GLN A 128 -4.202 29.519 45.933 1.00 13.98 C ANISOU 1049 CD GLN A 128 1806 2035 1470 198 -532 138 C ATOM 1050 OE1 GLN A 128 -2.972 29.646 45.915 1.00 15.39 O ANISOU 1050 OE1 GLN A 128 2039 2181 1627 392 -701 16 O ATOM 1051 NE2 GLN A 128 -4.931 29.694 47.039 1.00 15.38 N ANISOU 1051 NE2 GLN A 128 2154 2394 1295 564 -689 17 N ATOM 1052 N LEU A 129 -3.437 29.240 40.367 1.00 12.58 N ANISOU 1052 N LEU A 129 1737 1732 1309 27 -119 123 N ATOM 1053 CA LEU A 129 -2.983 29.764 39.094 1.00 12.66 C ANISOU 1053 CA LEU A 129 1588 1782 1441 -39 35 110 C ATOM 1054 C LEU A 129 -3.955 29.431 37.968 1.00 12.82 C ANISOU 1054 C LEU A 129 1557 1910 1403 -46 -12 34 C ATOM 1055 O LEU A 129 -4.150 30.246 37.043 1.00 13.58 O ANISOU 1055 O LEU A 129 1824 1907 1429 -133 15 167 O ATOM 1056 CB LEU A 129 -1.570 29.297 38.752 1.00 14.44 C ANISOU 1056 CB LEU A 129 1759 1975 1751 20 -11 182 C ATOM 1057 CG LEU A 129 -0.469 29.981 39.559 1.00 15.31 C ANISOU 1057 CG LEU A 129 1686 2183 1946 -189 -91 159 C ATOM 1058 CD1 LEU A 129 0.873 29.271 39.307 1.00 18.60 C ANISOU 1058 CD1 LEU A 129 1723 2843 2499 162 -105 326 C ATOM 1059 CD2 LEU A 129 -0.329 31.428 39.229 1.00 16.78 C ANISOU 1059 CD2 LEU A 129 1752 2385 2238 -462 -153 155 C ATOM 1060 N SER A 130 -4.519 28.227 37.974 1.00 12.35 N ANISOU 1060 N SER A 130 1776 1726 1190 -58 8 75 N ATOM 1061 CA SER A 130 -5.461 27.851 36.922 1.00 12.86 C ANISOU 1061 CA SER A 130 1859 1689 1337 39 31 10 C ATOM 1062 C SER A 130 -6.663 28.793 36.883 1.00 11.46 C ANISOU 1062 C SER A 130 1707 1548 1096 -199 165 22 C ATOM 1063 O SER A 130 -7.133 29.181 35.806 1.00 12.62 O ANISOU 1063 O SER A 130 1847 1818 1129 -89 89 94 O ATOM 1064 CB SER A 130 -5.822 26.398 37.068 1.00 14.87 C ANISOU 1064 CB SER A 130 2352 1659 1638 -51 -99 25 C ATOM 1065 OG ASER A 130 -6.825 26.174 38.003 0.50 11.94 O ANISOU 1065 OG ASER A 130 2027 1254 1253 -52 -326 238 O ATOM 1066 OG BSER A 130 -7.106 25.961 36.756 0.50 19.13 O ANISOU 1066 OG BSER A 130 2697 2190 2380 -15 -312 -68 O ATOM 1067 N HIS A 131 -7.127 29.191 38.058 1.00 10.85 N ANISOU 1067 N HIS A 131 1697 1532 892 -127 1 138 N ATOM 1068 CA HIS A 131 -8.198 30.198 38.143 1.00 11.31 C ANISOU 1068 CA HIS A 131 1644 1531 1119 -176 -12 -26 C ATOM 1069 C HIS A 131 -7.752 31.585 37.719 1.00 11.90 C ANISOU 1069 C HIS A 131 1778 1446 1296 -135 -16 1 C ATOM 1070 O HIS A 131 -8.509 32.325 37.057 1.00 13.81 O ANISOU 1070 O HIS A 131 1952 1719 1576 -32 -208 176 O ATOM 1071 CB HIS A 131 -8.790 30.272 39.550 1.00 11.83 C ANISOU 1071 CB HIS A 131 1807 1637 1049 -12 -107 -41 C ATOM 1072 CG HIS A 131 -9.573 29.076 39.938 1.00 11.32 C ANISOU 1072 CG HIS A 131 1789 1603 909 67 -128 -60 C ATOM 1073 ND1 HIS A 131 -8.971 27.917 40.340 1.00 13.09 N ANISOU 1073 ND1 HIS A 131 1946 1879 1148 -124 -101 248 N ATOM 1074 CD2 HIS A 131 -10.908 28.847 39.967 1.00 11.33 C ANISOU 1074 CD2 HIS A 131 1593 1895 817 -130 -91 358 C ATOM 1075 CE1 HIS A 131 -9.904 27.035 40.658 1.00 12.32 C ANISOU 1075 CE1 HIS A 131 2365 1657 658 -190 -17 417 C ATOM 1076 NE2 HIS A 131 -11.089 27.569 40.421 1.00 12.41 N ANISOU 1076 NE2 HIS A 131 2084 2002 628 -442 -69 393 N ATOM 1077 N ILE A 132 -6.552 31.984 38.125 1.00 12.19 N ANISOU 1077 N ILE A 132 1690 1501 1437 -215 -76 163 N ATOM 1078 CA ILE A 132 -6.061 33.306 37.825 1.00 13.19 C ANISOU 1078 CA ILE A 132 1833 1590 1587 -222 -127 33 C ATOM 1079 C ILE A 132 -5.836 33.527 36.336 1.00 14.45 C ANISOU 1079 C ILE A 132 2039 1759 1690 -68 -87 139 C ATOM 1080 O ILE A 132 -6.261 34.544 35.796 1.00 16.88 O ANISOU 1080 O ILE A 132 2290 2085 2037 47 8 573 O ATOM 1081 CB ILE A 132 -4.792 33.583 38.628 1.00 14.77 C ANISOU 1081 CB ILE A 132 2061 1789 1759 -341 -69 -39 C ATOM 1082 CG1 ILE A 132 -5.127 33.651 40.099 1.00 13.71 C ANISOU 1082 CG1 ILE A 132 1905 1667 1636 -231 -74 -74 C ATOM 1083 CG2 ILE A 132 -4.092 34.848 38.153 1.00 16.26 C ANISOU 1083 CG2 ILE A 132 2147 2082 1950 -451 -137 240 C ATOM 1084 CD1 ILE A 132 -3.904 33.571 41.019 1.00 16.37 C ANISOU 1084 CD1 ILE A 132 2362 2204 1653 -196 -183 -172 C ATOM 1085 N VAL A 133 -5.135 32.583 35.726 1.00 14.56 N ANISOU 1085 N VAL A 133 2095 2007 1429 -183 215 237 N ATOM 1086 CA VAL A 133 -4.742 32.636 34.312 1.00 17.29 C ANISOU 1086 CA VAL A 133 2416 2439 1714 -229 215 162 C ATOM 1087 C VAL A 133 -5.849 32.209 33.382 1.00 15.94 C ANISOU 1087 C VAL A 133 2240 2292 1522 -194 205 224 C ATOM 1088 O VAL A 133 -5.910 32.632 32.224 1.00 18.35 O ANISOU 1088 O VAL A 133 2391 2891 1686 -59 371 394 O ATOM 1089 CB VAL A 133 -3.452 31.722 34.117 1.00 20.99 C ANISOU 1089 CB VAL A 133 2472 3182 2320 -230 376 134 C ATOM 1090 CG1 VAL A 133 -3.039 31.538 32.633 1.00 23.78 C ANISOU 1090 CG1 VAL A 133 2887 3187 2958 62 431 5 C ATOM 1091 CG2 VAL A 133 -2.333 32.300 34.926 1.00 24.87 C ANISOU 1091 CG2 VAL A 133 3025 3501 2922 -221 151 69 C ATOM 1092 N GLY A 134 -6.711 31.323 33.868 1.00 15.40 N ANISOU 1092 N GLY A 134 2238 2149 1464 -290 255 96 N ATOM 1093 CA GLY A 134 -7.783 30.788 33.072 1.00 15.61 C ANISOU 1093 CA GLY A 134 2071 2297 1564 13 160 79 C ATOM 1094 C GLY A 134 -7.313 29.710 32.109 1.00 15.95 C ANISOU 1094 C GLY A 134 2157 2267 1636 -110 233 -46 C ATOM 1095 O GLY A 134 -7.429 29.829 30.895 1.00 19.73 O ANISOU 1095 O GLY A 134 2966 2710 1818 76 279 11 O ATOM 1096 N ALA A 135 -6.797 28.634 32.666 1.00 15.55 N ANISOU 1096 N ALA A 135 2036 2399 1471 7 92 -84 N ATOM 1097 CA ALA A 135 -6.282 27.506 31.879 1.00 16.37 C ANISOU 1097 CA ALA A 135 2098 2390 1731 101 176 -91 C ATOM 1098 C ALA A 135 -6.451 26.241 32.677 1.00 15.64 C ANISOU 1098 C ALA A 135 1939 2294 1708 49 46 -169 C ATOM 1099 O ALA A 135 -6.462 26.279 33.912 1.00 14.93 O ANISOU 1099 O ALA A 135 2260 1961 1452 152 217 -201 O ATOM 1100 CB ALA A 135 -4.805 27.695 31.493 1.00 19.55 C ANISOU 1100 CB ALA A 135 2422 2754 2251 -45 357 -18 C ATOM 1101 N ARG A 136 -6.467 25.116 31.977 1.00 15.83 N ANISOU 1101 N ARG A 136 2100 2373 1539 136 132 -287 N ATOM 1102 CA ARG A 136 -6.460 23.826 32.619 1.00 16.41 C ANISOU 1102 CA ARG A 136 1978 2262 1992 7 151 -199 C ATOM 1103 C ARG A 136 -5.186 23.658 33.417 1.00 15.20 C ANISOU 1103 C ARG A 136 1894 2062 1818 89 282 -221 C ATOM 1104 O ARG A 136 -4.101 24.130 33.022 1.00 15.85 O ANISOU 1104 O ARG A 136 1963 2195 1861 161 400 -159 O ATOM 1105 CB ARG A 136 -6.506 22.705 31.586 1.00 19.31 C ANISOU 1105 CB ARG A 136 2606 2485 2246 12 112 -154 C ATOM 1106 CG ARG A 136 -7.729 22.743 30.674 1.00 22.33 C ANISOU 1106 CG ARG A 136 2819 3124 2539 -158 -118 -103 C ATOM 1107 CD ARG A 136 -7.816 21.600 29.705 1.00 25.44 C ANISOU 1107 CD ARG A 136 3365 3214 3085 -122 68 -219 C ATOM 1108 NE ARG A 136 -8.996 21.661 28.846 1.00 31.39 N ANISOU 1108 NE ARG A 136 4087 4053 3785 -36 -193 -90 N ATOM 1109 CZ ARG A 136 -9.118 20.988 27.711 1.00 34.06 C ANISOU 1109 CZ ARG A 136 4476 4318 4147 -5 -107 -140 C ATOM 1110 NH1 ARG A 136 -8.135 20.191 27.292 1.00 37.03 N ANISOU 1110 NH1 ARG A 136 4575 4804 4691 172 -36 -47 N ATOM 1111 NH2 ARG A 136 -10.221 21.103 26.990 1.00 33.96 N ANISOU 1111 NH2 ARG A 136 4433 4323 4147 81 -36 -147 N ATOM 1112 N ARG A 137 -5.275 22.929 34.524 1.00 15.92 N ANISOU 1112 N ARG A 137 1999 2285 1765 107 262 -122 N ATOM 1113 CA ARG A 137 -4.131 22.724 35.392 1.00 16.85 C ANISOU 1113 CA ARG A 137 2253 2387 1761 174 183 -200 C ATOM 1114 C ARG A 137 -2.993 22.022 34.670 1.00 16.16 C ANISOU 1114 C ARG A 137 2044 2351 1746 44 119 -252 C ATOM 1115 O ARG A 137 -1.866 22.216 35.024 1.00 19.85 O ANISOU 1115 O ARG A 137 2150 3194 2196 85 16 -523 O ATOM 1116 CB ARG A 137 -4.496 21.968 36.656 1.00 19.82 C ANISOU 1116 CB ARG A 137 2541 2874 2115 303 381 -108 C ATOM 1117 CG ARG A 137 -4.905 20.554 36.448 1.00 23.23 C ANISOU 1117 CG ARG A 137 3112 3202 2510 -38 100 89 C ATOM 1118 CD ARG A 137 -5.219 19.805 37.726 1.00 23.29 C ANISOU 1118 CD ARG A 137 3090 3096 2661 92 262 181 C ATOM 1119 NE ARG A 137 -4.018 19.445 38.473 1.00 26.52 N ANISOU 1119 NE ARG A 137 3176 3507 3392 178 235 199 N ATOM 1120 CZ ARG A 137 -3.219 18.410 38.156 1.00 27.20 C ANISOU 1120 CZ ARG A 137 3336 3381 3615 -53 122 382 C ATOM 1121 NH1 ARG A 137 -3.485 17.625 37.119 1.00 28.80 N ANISOU 1121 NH1 ARG A 137 3624 3512 3807 11 294 324 N ATOM 1122 NH2 ARG A 137 -2.171 18.143 38.890 1.00 25.15 N ANISOU 1122 NH2 ARG A 137 2924 2946 3685 127 151 244 N ATOM 1123 N GLU A 138 -3.304 21.245 33.644 1.00 15.64 N ANISOU 1123 N GLU A 138 2026 2165 1750 159 113 -232 N ATOM 1124 CA GLU A 138 -2.274 20.501 32.914 1.00 15.67 C ANISOU 1124 CA GLU A 138 1894 2127 1931 43 194 -268 C ATOM 1125 C GLU A 138 -1.640 21.288 31.759 1.00 15.16 C ANISOU 1125 C GLU A 138 1751 2132 1877 98 115 -329 C ATOM 1126 O GLU A 138 -0.760 20.769 31.087 1.00 16.07 O ANISOU 1126 O GLU A 138 1770 2313 2022 150 165 -361 O ATOM 1127 CB GLU A 138 -2.888 19.212 32.381 1.00 17.35 C ANISOU 1127 CB GLU A 138 2010 2290 2291 -17 332 -281 C ATOM 1128 CG GLU A 138 -3.509 18.274 33.406 1.00 20.46 C ANISOU 1128 CG GLU A 138 2452 2512 2811 11 368 -31 C ATOM 1129 CD GLU A 138 -4.930 18.629 33.797 1.00 22.56 C ANISOU 1129 CD GLU A 138 2587 2860 3122 58 454 56 C ATOM 1130 OE1 GLU A 138 -5.593 19.497 33.169 1.00 19.68 O ANISOU 1130 OE1 GLU A 138 2132 2609 2737 -133 165 -24 O ATOM 1131 OE2 GLU A 138 -5.411 18.024 34.779 1.00 29.32 O ANISOU 1131 OE2 GLU A 138 3212 3942 3985 79 653 503 O ATOM 1132 N GLN A 139 -2.075 22.516 31.541 1.00 14.79 N ANISOU 1132 N GLN A 139 1699 2317 1603 62 287 -254 N ATOM 1133 CA GLN A 139 -1.590 23.326 30.442 1.00 16.09 C ANISOU 1133 CA GLN A 139 1917 2518 1679 207 193 -144 C ATOM 1134 C GLN A 139 -0.106 23.659 30.614 1.00 14.90 C ANISOU 1134 C GLN A 139 1796 2155 1708 194 97 -168 C ATOM 1135 O GLN A 139 0.366 23.883 31.732 1.00 14.74 O ANISOU 1135 O GLN A 139 1731 1984 1884 81 36 -215 O ATOM 1136 CB GLN A 139 -2.461 24.575 30.320 1.00 17.94 C ANISOU 1136 CB GLN A 139 2177 2687 1950 325 165 257 C ATOM 1137 CG GLN A 139 -2.436 25.116 28.952 1.00 19.46 C ANISOU 1137 CG GLN A 139 2312 2747 2333 204 115 261 C ATOM 1138 CD GLN A 139 -1.274 26.003 28.732 1.00 22.27 C ANISOU 1138 CD GLN A 139 2943 2642 2874 65 -85 405 C ATOM 1139 OE1 GLN A 139 -0.760 26.601 29.685 1.00 22.25 O ANISOU 1139 OE1 GLN A 139 2765 2260 3426 117 144 163 O ATOM 1140 NE2 GLN A 139 -0.812 26.087 27.467 1.00 26.04 N ANISOU 1140 NE2 GLN A 139 3371 3374 3149 120 331 376 N ATOM 1141 N LYS A 140 0.616 23.692 29.500 1.00 14.86 N ANISOU 1141 N LYS A 140 1766 2273 1605 112 100 -71 N ATOM 1142 CA LYS A 140 2.079 23.772 29.541 1.00 14.64 C ANISOU 1142 CA LYS A 140 1750 2065 1745 40 127 20 C ATOM 1143 C LYS A 140 2.605 24.884 30.404 1.00 15.52 C ANISOU 1143 C LYS A 140 1773 2002 2121 133 106 227 C ATOM 1144 O LYS A 140 3.520 24.701 31.196 1.00 15.58 O ANISOU 1144 O LYS A 140 1855 1907 2156 -47 -79 181 O ATOM 1145 CB LYS A 140 2.629 23.918 28.120 1.00 16.75 C ANISOU 1145 CB LYS A 140 1922 2497 1943 79 124 71 C ATOM 1146 CG LYS A 140 4.150 23.962 28.075 1.00 17.94 C ANISOU 1146 CG LYS A 140 2056 2538 2221 38 389 80 C ATOM 1147 CD LYS A 140 4.771 25.317 28.194 1.00 26.43 C ANISOU 1147 CD LYS A 140 3120 3323 3598 -366 81 250 C ATOM 1148 CE LYS A 140 6.230 25.170 28.473 1.00 27.55 C ANISOU 1148 CE LYS A 140 3109 3711 3645 -452 -77 -51 C ATOM 1149 NZ LYS A 140 7.011 26.403 28.315 1.00 32.13 N ANISOU 1149 NZ LYS A 140 3859 4037 4309 -621 43 -45 N ATOM 1150 N THR A 141 2.071 26.067 30.226 1.00 15.82 N ANISOU 1150 N THR A 141 1992 2004 2015 251 59 -23 N ATOM 1151 CA THR A 141 2.661 27.175 30.924 1.00 16.84 C ANISOU 1151 CA THR A 141 2129 1888 2380 170 102 159 C ATOM 1152 C THR A 141 2.431 27.058 32.455 1.00 16.79 C ANISOU 1152 C THR A 141 2116 1887 2375 119 -48 37 C ATOM 1153 O THR A 141 3.282 27.462 33.249 1.00 16.73 O ANISOU 1153 O THR A 141 2040 1919 2396 9 -205 -35 O ATOM 1154 CB THR A 141 2.197 28.512 30.307 1.00 20.00 C ANISOU 1154 CB THR A 141 2674 2370 2554 -1 53 51 C ATOM 1155 OG1ATHR A 141 0.911 28.812 30.780 0.33 16.44 O ANISOU 1155 OG1ATHR A 141 2359 1930 1955 34 -135 -40 O ATOM 1156 OG1BTHR A 141 3.035 29.020 29.257 0.33 20.69 O ANISOU 1156 OG1BTHR A 141 2738 2684 2438 129 84 213 O ATOM 1157 OG1CTHR A 141 2.509 28.533 28.908 0.33 20.08 O ANISOU 1157 OG1CTHR A 141 2647 2390 2590 -135 -10 172 O ATOM 1158 CG2ATHR A 141 2.129 28.424 28.770 0.33 17.36 C ANISOU 1158 CG2ATHR A 141 2035 2146 2414 -194 36 226 C ATOM 1159 CG2BTHR A 141 1.985 29.640 31.349 0.33 18.09 C ANISOU 1159 CG2BTHR A 141 2456 2074 2341 -163 51 143 C ATOM 1160 CG2CTHR A 141 2.783 29.757 30.870 0.33 17.25 C ANISOU 1160 CG2CTHR A 141 1909 2291 2353 2 -104 30 C ATOM 1161 N LEU A 142 1.304 26.495 32.873 1.00 14.42 N ANISOU 1161 N LEU A 142 1875 1704 1900 211 -117 -175 N ATOM 1162 CA LEU A 142 1.038 26.353 34.287 1.00 14.56 C ANISOU 1162 CA LEU A 142 1846 1700 1984 115 25 -288 C ATOM 1163 C LEU A 142 1.944 25.300 34.913 1.00 14.57 C ANISOU 1163 C LEU A 142 1741 1800 1993 133 -87 -255 C ATOM 1164 O LEU A 142 2.516 25.550 35.973 1.00 14.36 O ANISOU 1164 O LEU A 142 1811 1763 1879 61 -6 -253 O ATOM 1165 CB LEU A 142 -0.425 26.027 34.548 1.00 15.49 C ANISOU 1165 CB LEU A 142 1747 2150 1986 241 -22 -379 C ATOM 1166 CG LEU A 142 -1.376 27.159 34.197 1.00 16.94 C ANISOU 1166 CG LEU A 142 2322 2169 1944 169 92 -390 C ATOM 1167 CD1 LEU A 142 -2.779 26.737 34.642 1.00 19.39 C ANISOU 1167 CD1 LEU A 142 2102 2501 2762 206 22 -263 C ATOM 1168 CD2 LEU A 142 -0.971 28.423 34.824 1.00 22.87 C ANISOU 1168 CD2 LEU A 142 2922 2469 3296 513 -130 -334 C ATOM 1169 N VAL A 143 2.064 24.118 34.326 1.00 13.89 N ANISOU 1169 N VAL A 143 1733 1622 1921 92 -21 -260 N ATOM 1170 CA VAL A 143 2.930 23.105 34.926 1.00 14.13 C ANISOU 1170 CA VAL A 143 1902 1608 1857 8 97 -218 C ATOM 1171 C VAL A 143 4.401 23.553 34.869 1.00 13.53 C ANISOU 1171 C VAL A 143 1765 1486 1889 41 39 -147 C ATOM 1172 O VAL A 143 5.153 23.287 35.803 1.00 14.39 O ANISOU 1172 O VAL A 143 1817 1756 1893 98 -88 -167 O ATOM 1173 CB VAL A 143 2.660 21.692 34.369 1.00 13.69 C ANISOU 1173 CB VAL A 143 1840 1636 1722 63 66 -126 C ATOM 1174 CG1 VAL A 143 1.254 21.255 34.716 1.00 15.05 C ANISOU 1174 CG1 VAL A 143 2048 1808 1862 -149 -17 -54 C ATOM 1175 CG2 VAL A 143 2.908 21.560 32.862 1.00 14.60 C ANISOU 1175 CG2 VAL A 143 1864 1755 1928 -60 79 -187 C ATOM 1176 N PHE A 144 4.805 24.242 33.802 1.00 13.82 N ANISOU 1176 N PHE A 144 1742 1661 1848 61 -43 -139 N ATOM 1177 CA PHE A 144 6.143 24.821 33.738 1.00 14.09 C ANISOU 1177 CA PHE A 144 1649 1703 1999 64 27 -98 C ATOM 1178 C PHE A 144 6.361 25.819 34.853 1.00 13.90 C ANISOU 1178 C PHE A 144 1844 1554 1883 -2 118 -36 C ATOM 1179 O PHE A 144 7.432 25.860 35.482 1.00 14.27 O ANISOU 1179 O PHE A 144 1678 1727 2016 -27 -49 -188 O ATOM 1180 CB PHE A 144 6.368 25.477 32.382 1.00 15.08 C ANISOU 1180 CB PHE A 144 1895 1878 1954 -83 10 -106 C ATOM 1181 CG PHE A 144 7.632 26.194 32.235 1.00 15.54 C ANISOU 1181 CG PHE A 144 1945 2034 1926 -129 -107 -57 C ATOM 1182 CD1 PHE A 144 8.811 25.516 32.304 1.00 17.44 C ANISOU 1182 CD1 PHE A 144 2262 1853 2510 55 80 89 C ATOM 1183 CD2 PHE A 144 7.656 27.578 31.989 1.00 16.31 C ANISOU 1183 CD2 PHE A 144 2151 1841 2202 -45 -7 -230 C ATOM 1184 CE1 PHE A 144 10.034 26.195 32.151 1.00 18.47 C ANISOU 1184 CE1 PHE A 144 2137 2264 2615 2 286 108 C ATOM 1185 CE2 PHE A 144 8.857 28.226 31.822 1.00 16.44 C ANISOU 1185 CE2 PHE A 144 2184 1757 2305 -147 -8 -106 C ATOM 1186 CZ PHE A 144 10.034 27.528 31.941 1.00 16.88 C ANISOU 1186 CZ PHE A 144 1788 2100 2524 -95 96 -126 C ATOM 1187 N THR A 145 5.353 26.647 35.158 1.00 13.97 N ANISOU 1187 N THR A 145 1776 1675 1856 82 -76 -146 N ATOM 1188 CA THR A 145 5.456 27.584 36.262 1.00 13.67 C ANISOU 1188 CA THR A 145 1739 1534 1919 33 58 -59 C ATOM 1189 C THR A 145 5.694 26.872 37.592 1.00 13.98 C ANISOU 1189 C THR A 145 1779 1564 1966 78 42 -220 C ATOM 1190 O THR A 145 6.478 27.356 38.412 1.00 14.65 O ANISOU 1190 O THR A 145 1811 1757 1997 82 -56 -220 O ATOM 1191 CB THR A 145 4.222 28.496 36.298 1.00 14.69 C ANISOU 1191 CB THR A 145 1775 1674 2132 -71 -42 -138 C ATOM 1192 OG1 THR A 145 4.180 29.289 35.104 1.00 15.42 O ANISOU 1192 OG1 THR A 145 1799 1628 2430 -8 -51 -62 O ATOM 1193 CG2 THR A 145 4.284 29.452 37.463 1.00 15.27 C ANISOU 1193 CG2 THR A 145 1721 1682 2397 143 82 -377 C ATOM 1194 N ILE A 146 5.041 25.732 37.814 1.00 13.69 N ANISOU 1194 N ILE A 146 1793 1657 1752 -31 -28 -217 N ATOM 1195 CA ILE A 146 5.307 24.976 39.013 1.00 13.69 C ANISOU 1195 CA ILE A 146 1829 1684 1687 24 27 -224 C ATOM 1196 C ILE A 146 6.759 24.521 39.095 1.00 14.26 C ANISOU 1196 C ILE A 146 1863 1610 1945 -36 -22 -262 C ATOM 1197 O ILE A 146 7.365 24.608 40.159 1.00 14.48 O ANISOU 1197 O ILE A 146 1879 1672 1950 5 -51 -180 O ATOM 1198 CB ILE A 146 4.302 23.802 39.133 1.00 14.59 C ANISOU 1198 CB ILE A 146 1896 1804 1841 -18 -42 -253 C ATOM 1199 CG1 ILE A 146 2.865 24.321 39.209 1.00 15.42 C ANISOU 1199 CG1 ILE A 146 1978 1822 2057 -57 -25 -219 C ATOM 1200 CG2 ILE A 146 4.644 22.908 40.338 1.00 15.31 C ANISOU 1200 CG2 ILE A 146 1876 1877 2063 -72 -44 -130 C ATOM 1201 CD1 ILE A 146 2.588 25.235 40.337 1.00 16.70 C ANISOU 1201 CD1 ILE A 146 1943 1927 2475 -29 -78 -379 C ATOM 1202 N LYS A 147 7.307 24.037 37.995 1.00 14.12 N ANISOU 1202 N LYS A 147 1829 1655 1881 54 -59 -215 N ATOM 1203 CA LYS A 147 8.720 23.672 37.955 1.00 14.44 C ANISOU 1203 CA LYS A 147 1860 1633 1992 142 -77 -190 C ATOM 1204 C LYS A 147 9.609 24.870 38.363 1.00 14.42 C ANISOU 1204 C LYS A 147 1877 1746 1857 168 39 -132 C ATOM 1205 O LYS A 147 10.528 24.730 39.179 1.00 14.17 O ANISOU 1205 O LYS A 147 1876 1656 1852 131 -40 -170 O ATOM 1206 CB LYS A 147 9.091 23.138 36.562 1.00 15.56 C ANISOU 1206 CB LYS A 147 2016 1603 2293 68 -3 -356 C ATOM 1207 CG LYS A 147 10.579 22.914 36.381 1.00 17.30 C ANISOU 1207 CG LYS A 147 2242 2111 2220 335 148 -310 C ATOM 1208 CD LYS A 147 10.932 22.129 35.171 1.00 19.74 C ANISOU 1208 CD LYS A 147 2285 2565 2650 51 110 -487 C ATOM 1209 CE LYS A 147 12.390 22.284 34.845 1.00 22.44 C ANISOU 1209 CE LYS A 147 2445 3312 2769 136 210 -698 C ATOM 1210 NZ LYS A 147 12.825 21.090 34.160 1.00 23.07 N ANISOU 1210 NZ LYS A 147 2787 2640 3338 197 139 -65 N ATOM 1211 N ILE A 148 9.337 26.032 37.773 1.00 14.03 N ANISOU 1211 N ILE A 148 1848 1570 1910 180 -39 -159 N ATOM 1212 CA ILE A 148 10.128 27.229 38.044 1.00 13.95 C ANISOU 1212 CA ILE A 148 1843 1611 1845 -12 -22 -176 C ATOM 1213 C ILE A 148 10.002 27.621 39.524 1.00 14.21 C ANISOU 1213 C ILE A 148 1772 1573 2053 164 -29 -63 C ATOM 1214 O ILE A 148 10.977 28.019 40.151 1.00 13.89 O ANISOU 1214 O ILE A 148 1747 1678 1853 80 -42 -196 O ATOM 1215 CB ILE A 148 9.710 28.340 37.110 1.00 13.60 C ANISOU 1215 CB ILE A 148 1668 1598 1899 11 -52 -130 C ATOM 1216 CG1 ILE A 148 10.173 28.037 35.654 1.00 14.40 C ANISOU 1216 CG1 ILE A 148 1942 1697 1830 47 1 -148 C ATOM 1217 CG2 ILE A 148 10.165 29.709 37.596 1.00 14.66 C ANISOU 1217 CG2 ILE A 148 2002 1655 1911 77 -15 -155 C ATOM 1218 CD1 ILE A 148 11.661 28.004 35.436 1.00 15.16 C ANISOU 1218 CD1 ILE A 148 1791 2124 1842 175 59 -125 C ATOM 1219 N LEU A 149 8.802 27.501 40.070 1.00 14.01 N ANISOU 1219 N LEU A 149 1723 1735 1864 29 22 -247 N ATOM 1220 CA LEU A 149 8.612 27.773 41.484 1.00 14.32 C ANISOU 1220 CA LEU A 149 1801 1655 1985 104 -62 -282 C ATOM 1221 C LEU A 149 9.403 26.795 42.349 1.00 13.82 C ANISOU 1221 C LEU A 149 1799 1821 1628 105 163 -264 C ATOM 1222 O LEU A 149 9.925 27.191 43.407 1.00 14.57 O ANISOU 1222 O LEU A 149 1855 1841 1840 77 -10 -250 O ATOM 1223 CB LEU A 149 7.136 27.769 41.860 1.00 14.40 C ANISOU 1223 CB LEU A 149 1948 1739 1785 82 -42 -198 C ATOM 1224 CG LEU A 149 6.340 28.938 41.294 1.00 15.63 C ANISOU 1224 CG LEU A 149 2031 1972 1934 209 -85 -221 C ATOM 1225 CD1 LEU A 149 4.831 28.735 41.578 1.00 17.28 C ANISOU 1225 CD1 LEU A 149 2077 2273 2213 377 -73 -496 C ATOM 1226 CD2 LEU A 149 6.773 30.231 41.890 1.00 16.48 C ANISOU 1226 CD2 LEU A 149 2168 1942 2151 331 -39 -16 C ATOM 1227 N ASN A 150 9.522 25.534 41.947 1.00 14.29 N ANISOU 1227 N ASN A 150 1871 1741 1818 80 -47 -177 N ATOM 1228 CA ASN A 150 10.345 24.595 42.687 1.00 14.35 C ANISOU 1228 CA ASN A 150 1931 1714 1807 42 -112 -67 C ATOM 1229 C ASN A 150 11.811 24.991 42.603 1.00 14.03 C ANISOU 1229 C ASN A 150 1960 1591 1778 38 -30 -47 C ATOM 1230 O ASN A 150 12.533 24.856 43.588 1.00 14.42 O ANISOU 1230 O ASN A 150 1795 1802 1879 14 -15 -96 O ATOM 1231 CB ASN A 150 10.136 23.165 42.198 1.00 14.84 C ANISOU 1231 CB ASN A 150 1932 1766 1936 5 -118 -286 C ATOM 1232 CG ASN A 150 10.577 22.168 43.237 1.00 14.60 C ANISOU 1232 CG ASN A 150 1791 1647 2107 86 3 -171 C ATOM 1233 OD1 ASN A 150 10.164 22.271 44.407 1.00 16.17 O ANISOU 1233 OD1 ASN A 150 2178 1937 2026 235 235 -46 O ATOM 1234 ND2 ASN A 150 11.375 21.201 42.842 1.00 14.70 N ANISOU 1234 ND2 ASN A 150 1817 1858 1909 15 19 -196 N ATOM 1235 N TYR A 151 12.252 25.490 41.464 1.00 14.11 N ANISOU 1235 N TYR A 151 1741 1855 1762 81 -86 -68 N ATOM 1236 CA TYR A 151 13.613 25.987 41.363 1.00 14.59 C ANISOU 1236 CA TYR A 151 1924 1717 1900 62 -3 7 C ATOM 1237 C TYR A 151 13.819 27.127 42.374 1.00 14.21 C ANISOU 1237 C TYR A 151 1882 1728 1786 179 19 86 C ATOM 1238 O TYR A 151 14.828 27.167 43.065 1.00 14.90 O ANISOU 1238 O TYR A 151 1895 1874 1891 53 -88 1 O ATOM 1239 CB TYR A 151 13.903 26.497 39.956 1.00 14.65 C ANISOU 1239 CB TYR A 151 1792 1832 1940 122 5 11 C ATOM 1240 CG TYR A 151 14.125 25.439 38.884 1.00 14.59 C ANISOU 1240 CG TYR A 151 1860 1720 1961 138 55 53 C ATOM 1241 CD1 TYR A 151 14.128 24.068 39.136 1.00 14.69 C ANISOU 1241 CD1 TYR A 151 1828 1760 1995 -10 127 0 C ATOM 1242 CD2 TYR A 151 14.436 25.850 37.591 1.00 15.26 C ANISOU 1242 CD2 TYR A 151 2200 1672 1925 63 3 3 C ATOM 1243 CE1 TYR A 151 14.480 23.156 38.139 1.00 15.10 C ANISOU 1243 CE1 TYR A 151 2048 1631 2055 165 201 -95 C ATOM 1244 CE2 TYR A 151 14.817 24.950 36.623 1.00 16.45 C ANISOU 1244 CE2 TYR A 151 2555 1826 1868 38 162 -218 C ATOM 1245 CZ TYR A 151 14.852 23.601 36.917 1.00 15.57 C ANISOU 1245 CZ TYR A 151 2150 1686 2078 106 177 -159 C ATOM 1246 OH TYR A 151 15.256 22.665 35.999 1.00 16.79 O ANISOU 1246 OH TYR A 151 2315 1851 2213 177 204 -169 O ATOM 1247 N ALA A 152 12.892 28.071 42.422 1.00 14.55 N ANISOU 1247 N ALA A 152 1954 1753 1820 46 -97 -65 N ATOM 1248 CA ALA A 152 12.986 29.190 43.360 1.00 14.17 C ANISOU 1248 CA ALA A 152 1847 1670 1867 43 -81 -90 C ATOM 1249 C ALA A 152 13.055 28.713 44.789 1.00 14.78 C ANISOU 1249 C ALA A 152 1839 1672 2101 16 -56 -149 C ATOM 1250 O ALA A 152 13.867 29.210 45.587 1.00 15.09 O ANISOU 1250 O ALA A 152 2061 1756 1916 -131 -165 -21 O ATOM 1251 CB ALA A 152 11.793 30.122 43.171 1.00 15.44 C ANISOU 1251 CB ALA A 152 2067 1754 2044 78 -41 -181 C ATOM 1252 N TYR A 153 12.245 27.724 45.142 1.00 14.68 N ANISOU 1252 N TYR A 153 1893 1753 1933 -55 -62 -146 N ATOM 1253 CA TYR A 153 12.227 27.169 46.519 1.00 13.65 C ANISOU 1253 CA TYR A 153 1653 1764 1768 9 98 -155 C ATOM 1254 C TYR A 153 13.552 26.487 46.849 1.00 13.86 C ANISOU 1254 C TYR A 153 1583 1702 1978 -181 112 -67 C ATOM 1255 O TYR A 153 14.144 26.726 47.905 1.00 14.03 O ANISOU 1255 O TYR A 153 1779 1800 1752 -172 5 -126 O ATOM 1256 CB TYR A 153 11.089 26.177 46.629 1.00 14.48 C ANISOU 1256 CB TYR A 153 1756 1796 1948 24 48 -216 C ATOM 1257 CG TYR A 153 10.929 25.575 47.976 1.00 13.58 C ANISOU 1257 CG TYR A 153 1601 1653 1903 -61 -40 -87 C ATOM 1258 CD1 TYR A 153 10.403 26.322 49.027 1.00 14.54 C ANISOU 1258 CD1 TYR A 153 1687 1807 2029 -149 0 -61 C ATOM 1259 CD2 TYR A 153 11.319 24.270 48.226 1.00 14.01 C ANISOU 1259 CD2 TYR A 153 1697 1942 1684 -94 190 -153 C ATOM 1260 CE1 TYR A 153 10.228 25.780 50.285 1.00 14.14 C ANISOU 1260 CE1 TYR A 153 1621 1802 1950 -4 -172 -55 C ATOM 1261 CE2 TYR A 153 11.165 23.723 49.485 1.00 14.50 C ANISOU 1261 CE2 TYR A 153 1411 1861 2237 12 -32 -198 C ATOM 1262 CZ TYR A 153 10.594 24.470 50.517 1.00 13.48 C ANISOU 1262 CZ TYR A 153 1478 1676 1965 -142 2 -80 C ATOM 1263 OH TYR A 153 10.437 23.891 51.752 1.00 15.04 O ANISOU 1263 OH TYR A 153 1572 1944 2196 -170 48 225 O ATOM 1264 N MET A 154 14.024 25.622 45.950 1.00 13.57 N ANISOU 1264 N MET A 154 1785 1610 1759 -83 64 -93 N ATOM 1265 CA MET A 154 15.271 24.908 46.172 1.00 13.87 C ANISOU 1265 CA MET A 154 1759 1736 1771 -26 73 -20 C ATOM 1266 C MET A 154 16.440 25.863 46.320 1.00 14.19 C ANISOU 1266 C MET A 154 1848 1607 1934 -46 4 -14 C ATOM 1267 O MET A 154 17.292 25.690 47.206 1.00 14.20 O ANISOU 1267 O MET A 154 1791 1748 1857 -60 150 64 O ATOM 1268 CB MET A 154 15.522 23.883 45.068 1.00 14.28 C ANISOU 1268 CB MET A 154 1775 1827 1822 135 -7 -73 C ATOM 1269 CG MET A 154 14.534 22.695 45.109 1.00 13.96 C ANISOU 1269 CG MET A 154 1825 1682 1796 -71 26 -52 C ATOM 1270 SD MET A 154 15.081 21.284 44.142 1.00 15.45 S ANISOU 1270 SD MET A 154 2125 1819 1924 -83 86 -64 S ATOM 1271 CE MET A 154 14.955 22.023 42.545 1.00 16.55 C ANISOU 1271 CE MET A 154 1941 2234 2110 -75 106 244 C ATOM 1272 N CYS A 155 16.477 26.898 45.499 1.00 13.96 N ANISOU 1272 N CYS A 155 1780 1682 1840 -187 22 115 N ATOM 1273 CA CYS A 155 17.539 27.866 45.612 1.00 14.64 C ANISOU 1273 CA CYS A 155 1900 1676 1985 -122 -10 219 C ATOM 1274 C CYS A 155 17.457 28.657 46.890 1.00 14.19 C ANISOU 1274 C CYS A 155 1869 1595 1926 -181 -80 232 C ATOM 1275 O CYS A 155 18.469 28.853 47.564 1.00 16.04 O ANISOU 1275 O CYS A 155 1990 1818 2286 -164 -108 -7 O ATOM 1276 CB CYS A 155 17.609 28.684 44.374 1.00 17.14 C ANISOU 1276 CB CYS A 155 2286 2190 2033 -407 91 173 C ATOM 1277 SG ACYS A 155 18.315 30.404 44.598 0.50 13.42 S ANISOU 1277 SG ACYS A 155 1884 1421 1790 -171 55 228 S ATOM 1278 SG BCYS A 155 16.591 29.924 43.994 0.50 23.67 S ANISOU 1278 SG BCYS A 155 3021 3094 2879 -140 -69 125 S ATOM 1279 N SER A 156 16.274 29.129 47.235 1.00 14.42 N ANISOU 1279 N SER A 156 1733 1774 1971 -232 -98 124 N ATOM 1280 CA SER A 156 16.098 29.955 48.410 1.00 14.74 C ANISOU 1280 CA SER A 156 1943 1629 2028 -138 85 135 C ATOM 1281 C SER A 156 16.457 29.212 49.684 1.00 14.53 C ANISOU 1281 C SER A 156 1923 1532 2064 -157 13 -51 C ATOM 1282 O SER A 156 17.132 29.732 50.562 1.00 16.32 O ANISOU 1282 O SER A 156 2183 1718 2298 -452 -17 49 O ATOM 1283 CB SER A 156 14.685 30.432 48.513 1.00 15.69 C ANISOU 1283 CB SER A 156 2076 1829 2053 20 98 140 C ATOM 1284 OG SER A 156 14.512 31.162 49.714 1.00 17.24 O ANISOU 1284 OG SER A 156 2373 1931 2245 -55 13 -163 O ATOM 1285 N ARG A 157 15.960 27.989 49.810 1.00 14.08 N ANISOU 1285 N ARG A 157 2069 1570 1712 -237 -65 16 N ATOM 1286 CA ARG A 157 16.060 27.222 51.053 1.00 13.77 C ANISOU 1286 CA ARG A 157 1889 1561 1780 -60 159 108 C ATOM 1287 C ARG A 157 17.327 26.372 51.098 1.00 13.76 C ANISOU 1287 C ARG A 157 1874 1503 1851 -212 79 45 C ATOM 1288 O ARG A 157 17.709 25.911 52.173 1.00 14.77 O ANISOU 1288 O ARG A 157 2094 1687 1830 -62 -29 157 O ATOM 1289 CB ARG A 157 14.838 26.307 51.240 1.00 13.93 C ANISOU 1289 CB ARG A 157 1889 1469 1933 -165 49 -5 C ATOM 1290 CG ARG A 157 13.518 27.023 51.254 1.00 14.84 C ANISOU 1290 CG ARG A 157 1940 1568 2128 -112 -17 22 C ATOM 1291 CD ARG A 157 13.434 28.104 52.335 1.00 14.65 C ANISOU 1291 CD ARG A 157 1950 1752 1862 -157 40 -86 C ATOM 1292 NE ARG A 157 12.140 28.768 52.264 1.00 15.13 N ANISOU 1292 NE ARG A 157 1986 1709 2053 -128 88 -88 N ATOM 1293 CZ ARG A 157 11.010 28.292 52.782 1.00 14.24 C ANISOU 1293 CZ ARG A 157 1875 1558 1978 -118 106 -127 C ATOM 1294 NH1 ARG A 157 11.025 27.244 53.591 1.00 16.35 N ANISOU 1294 NH1 ARG A 157 2100 1789 2323 -70 134 195 N ATOM 1295 NH2 ARG A 157 9.860 28.872 52.522 1.00 15.73 N ANISOU 1295 NH2 ARG A 157 1790 1802 2383 -91 49 116 N ATOM 1296 N GLY A 158 17.987 26.145 49.968 1.00 14.03 N ANISOU 1296 N GLY A 158 1922 1531 1874 -80 46 76 N ATOM 1297 CA GLY A 158 19.123 25.264 49.920 1.00 13.48 C ANISOU 1297 CA GLY A 158 1738 1545 1836 -182 55 57 C ATOM 1298 C GLY A 158 18.765 23.829 50.186 1.00 13.33 C ANISOU 1298 C GLY A 158 1785 1454 1825 -194 46 55 C ATOM 1299 O GLY A 158 19.405 23.141 50.980 1.00 14.48 O ANISOU 1299 O GLY A 158 1770 1633 2098 -300 18 173 O ATOM 1300 N VAL A 159 17.750 23.343 49.505 1.00 12.94 N ANISOU 1300 N VAL A 159 1675 1518 1723 -148 29 -1 N ATOM 1301 CA VAL A 159 17.242 21.993 49.672 1.00 12.59 C ANISOU 1301 CA VAL A 159 1387 1388 2007 -99 69 -16 C ATOM 1302 C VAL A 159 16.956 21.371 48.316 1.00 12.49 C ANISOU 1302 C VAL A 159 1471 1553 1721 -7 163 -122 C ATOM 1303 O VAL A 159 16.782 22.074 47.325 1.00 14.47 O ANISOU 1303 O VAL A 159 1979 1632 1883 -76 185 15 O ATOM 1304 CB VAL A 159 15.920 21.917 50.537 1.00 13.76 C ANISOU 1304 CB VAL A 159 1517 1741 1968 -69 272 -44 C ATOM 1305 CG1 VAL A 159 16.126 22.484 51.921 1.00 14.98 C ANISOU 1305 CG1 VAL A 159 1962 1641 2089 -75 278 -194 C ATOM 1306 CG2 VAL A 159 14.744 22.587 49.840 1.00 14.36 C ANISOU 1306 CG2 VAL A 159 1604 1829 2019 -54 259 -227 C ATOM 1307 N ASN A 160 16.892 20.052 48.302 1.00 12.72 N ANISOU 1307 N ASN A 160 1467 1624 1741 -11 110 -114 N ATOM 1308 CA ASN A 160 16.205 19.323 47.254 1.00 12.94 C ANISOU 1308 CA ASN A 160 1572 1680 1664 -23 76 -115 C ATOM 1309 C ASN A 160 14.760 19.153 47.632 1.00 13.28 C ANISOU 1309 C ASN A 160 1454 1691 1899 -133 154 48 C ATOM 1310 O ASN A 160 14.461 18.989 48.805 1.00 14.44 O ANISOU 1310 O ASN A 160 1535 2086 1865 -75 269 -4 O ATOM 1311 CB ASN A 160 16.811 17.938 47.073 1.00 14.51 C ANISOU 1311 CB ASN A 160 1699 1885 1929 -55 152 -154 C ATOM 1312 CG ASN A 160 18.118 17.963 46.390 1.00 15.11 C ANISOU 1312 CG ASN A 160 1813 1891 2036 224 206 -276 C ATOM 1313 OD1 ASN A 160 18.302 18.656 45.405 1.00 16.18 O ANISOU 1313 OD1 ASN A 160 1859 2191 2096 45 469 -97 O ATOM 1314 ND2 ASN A 160 19.060 17.174 46.897 1.00 18.59 N ANISOU 1314 ND2 ASN A 160 2178 2634 2248 420 570 3 N ATOM 1315 N ARG A 161 13.875 19.124 46.658 1.00 14.10 N ANISOU 1315 N ARG A 161 1520 1890 1945 -163 -6 -70 N ATOM 1316 CA ARG A 161 12.500 18.762 46.889 1.00 15.69 C ANISOU 1316 CA ARG A 161 1634 2135 2190 -101 -120 233 C ATOM 1317 C ARG A 161 11.957 18.147 45.619 1.00 16.56 C ANISOU 1317 C ARG A 161 1797 2336 2158 -371 -157 304 C ATOM 1318 O ARG A 161 11.941 18.790 44.557 1.00 19.53 O ANISOU 1318 O ARG A 161 2396 2695 2328 -715 -534 469 O ATOM 1319 CB ARG A 161 11.653 19.929 47.300 1.00 17.11 C ANISOU 1319 CB ARG A 161 1610 2385 2506 31 151 366 C ATOM 1320 CG ARG A 161 10.268 19.316 47.373 1.00 20.98 C ANISOU 1320 CG ARG A 161 2230 2593 3145 -19 222 230 C ATOM 1321 CD ARG A 161 9.191 20.172 47.668 1.00 19.15 C ANISOU 1321 CD ARG A 161 2149 2019 3107 48 133 506 C ATOM 1322 NE ARG A 161 9.124 21.333 46.826 1.00 16.92 N ANISOU 1322 NE ARG A 161 1841 2066 2519 197 239 324 N ATOM 1323 CZ ARG A 161 8.509 22.447 47.173 1.00 15.59 C ANISOU 1323 CZ ARG A 161 1640 1869 2412 87 51 93 C ATOM 1324 NH1 ARG A 161 7.833 22.492 48.294 1.00 16.80 N ANISOU 1324 NH1 ARG A 161 1965 2113 2302 237 39 212 N ATOM 1325 NH2 ARG A 161 8.520 23.449 46.378 1.00 15.01 N ANISOU 1325 NH2 ARG A 161 1921 1682 2098 262 -29 -1 N ATOM 1326 N VAL A 162 11.552 16.905 45.697 1.00 15.61 N ANISOU 1326 N VAL A 162 1851 2151 1928 -322 -165 100 N ATOM 1327 CA VAL A 162 11.005 16.172 44.575 1.00 16.12 C ANISOU 1327 CA VAL A 162 1822 2310 1993 -239 -167 68 C ATOM 1328 C VAL A 162 9.532 16.578 44.388 1.00 16.54 C ANISOU 1328 C VAL A 162 1749 2457 2077 -258 0 86 C ATOM 1329 O VAL A 162 8.741 16.612 45.347 1.00 17.67 O ANISOU 1329 O VAL A 162 1725 3062 1925 -200 -17 49 O ATOM 1330 CB VAL A 162 11.168 14.657 44.755 1.00 16.41 C ANISOU 1330 CB VAL A 162 1792 2420 2021 -194 -108 45 C ATOM 1331 CG1 VAL A 162 10.591 13.897 43.605 1.00 17.38 C ANISOU 1331 CG1 VAL A 162 2159 2270 2172 -43 -99 -52 C ATOM 1332 CG2 VAL A 162 12.637 14.294 44.911 1.00 18.42 C ANISOU 1332 CG2 VAL A 162 2035 2400 2563 -92 -154 2 C ATOM 1333 N LEU A 163 9.191 16.896 43.155 1.00 16.06 N ANISOU 1333 N LEU A 163 1766 2429 1906 -199 -71 -81 N ATOM 1334 CA LEU A 163 7.837 17.272 42.789 1.00 15.79 C ANISOU 1334 CA LEU A 163 1864 2085 2049 -137 -85 -176 C ATOM 1335 C LEU A 163 6.885 16.090 42.764 1.00 15.51 C ANISOU 1335 C LEU A 163 1899 2147 1846 -116 -85 -184 C ATOM 1336 O LEU A 163 7.299 14.938 42.709 1.00 16.54 O ANISOU 1336 O LEU A 163 1958 2147 2179 -129 -216 -100 O ATOM 1337 CB LEU A 163 7.899 17.993 41.433 1.00 16.00 C ANISOU 1337 CB LEU A 163 1975 2107 1995 -84 -64 -138 C ATOM 1338 CG LEU A 163 8.534 19.380 41.548 1.00 16.57 C ANISOU 1338 CG LEU A 163 1991 2012 2291 0 28 -119 C ATOM 1339 CD1 LEU A 163 8.981 19.886 40.185 1.00 17.91 C ANISOU 1339 CD1 LEU A 163 2260 2124 2419 -187 -257 -122 C ATOM 1340 CD2 LEU A 163 7.550 20.330 42.196 1.00 18.74 C ANISOU 1340 CD2 LEU A 163 2229 2102 2788 -280 116 -403 C ATOM 1341 N PRO A 164 5.579 16.374 42.843 1.00 16.64 N ANISOU 1341 N PRO A 164 1994 2191 2134 -46 -196 -160 N ATOM 1342 CA PRO A 164 4.592 15.306 42.866 1.00 16.95 C ANISOU 1342 CA PRO A 164 2003 2418 2018 -154 49 -88 C ATOM 1343 C PRO A 164 4.477 14.574 41.548 1.00 15.25 C ANISOU 1343 C PRO A 164 1696 2251 1846 -173 -58 11 C ATOM 1344 O PRO A 164 4.629 15.150 40.485 1.00 16.39 O ANISOU 1344 O PRO A 164 2189 2252 1785 -195 -93 94 O ATOM 1345 CB PRO A 164 3.263 16.045 43.146 1.00 20.11 C ANISOU 1345 CB PRO A 164 2166 2947 2527 -103 77 -307 C ATOM 1346 CG PRO A 164 3.543 17.452 43.361 1.00 21.33 C ANISOU 1346 CG PRO A 164 2390 2875 2837 115 -164 278 C ATOM 1347 CD PRO A 164 4.928 17.694 42.955 1.00 18.26 C ANISOU 1347 CD PRO A 164 2030 2489 2417 -79 -96 -282 C ATOM 1348 N PHE A 165 4.128 13.298 41.626 1.00 15.23 N ANISOU 1348 N PHE A 165 1822 2252 1711 -63 -85 123 N ATOM 1349 CA PHE A 165 3.821 12.540 40.412 1.00 15.15 C ANISOU 1349 CA PHE A 165 1855 2057 1844 -46 -136 27 C ATOM 1350 C PHE A 165 2.596 13.038 39.672 1.00 14.59 C ANISOU 1350 C PHE A 165 1797 1920 1825 33 -80 44 C ATOM 1351 O PHE A 165 2.496 12.822 38.468 1.00 16.17 O ANISOU 1351 O PHE A 165 2200 2233 1709 90 -163 -34 O ATOM 1352 CB PHE A 165 3.719 11.059 40.749 1.00 15.62 C ANISOU 1352 CB PHE A 165 1968 2125 1842 -46 -63 184 C ATOM 1353 CG PHE A 165 5.049 10.410 40.947 1.00 16.11 C ANISOU 1353 CG PHE A 165 1868 2212 2040 76 -28 284 C ATOM 1354 CD1 PHE A 165 5.738 9.868 39.869 1.00 15.88 C ANISOU 1354 CD1 PHE A 165 2018 1884 2129 -49 -111 109 C ATOM 1355 CD2 PHE A 165 5.621 10.332 42.216 1.00 17.24 C ANISOU 1355 CD2 PHE A 165 2063 2546 1940 92 -54 141 C ATOM 1356 CE1 PHE A 165 6.986 9.292 40.052 1.00 16.98 C ANISOU 1356 CE1 PHE A 165 2165 2217 2070 104 184 -8 C ATOM 1357 CE2 PHE A 165 6.867 9.737 42.398 1.00 18.63 C ANISOU 1357 CE2 PHE A 165 2137 2865 2074 281 -10 119 C ATOM 1358 CZ PHE A 165 7.548 9.232 41.313 1.00 17.72 C ANISOU 1358 CZ PHE A 165 1876 2573 2282 297 -55 186 C ATOM 1359 N ASP A 166 1.656 13.650 40.380 1.00 14.92 N ANISOU 1359 N ASP A 166 1872 2031 1765 -2 -137 49 N ATOM 1360 CA ASP A 166 0.382 14.027 39.791 1.00 15.18 C ANISOU 1360 CA ASP A 166 1803 2030 1933 -94 -164 36 C ATOM 1361 C ASP A 166 0.368 15.376 39.095 1.00 14.67 C ANISOU 1361 C ASP A 166 1792 1997 1784 -33 -13 -70 C ATOM 1362 O ASP A 166 -0.699 15.786 38.649 1.00 16.71 O ANISOU 1362 O ASP A 166 1836 2280 2232 54 -145 250 O ATOM 1363 CB ASP A 166 -0.767 13.922 40.790 1.00 17.29 C ANISOU 1363 CB ASP A 166 2135 2321 2113 -48 -129 169 C ATOM 1364 CG ASP A 166 -0.689 14.910 41.916 1.00 19.36 C ANISOU 1364 CG ASP A 166 2258 2826 2269 -77 -2 264 C ATOM 1365 OD1 ASP A 166 0.248 15.716 42.033 1.00 20.40 O ANISOU 1365 OD1 ASP A 166 2133 3231 2387 133 42 -506 O ATOM 1366 OD2 ASP A 166 -1.603 14.908 42.780 1.00 22.92 O ANISOU 1366 OD2 ASP A 166 2850 3288 2568 38 525 60 O ATOM 1367 N ILE A 167 1.526 15.995 38.883 1.00 14.23 N ANISOU 1367 N ILE A 167 1835 1890 1680 -27 -160 -27 N ATOM 1368 CA ILE A 167 1.625 17.201 38.044 1.00 14.43 C ANISOU 1368 CA ILE A 167 1880 1903 1698 52 -79 -30 C ATOM 1369 C ILE A 167 2.361 16.772 36.779 1.00 14.78 C ANISOU 1369 C ILE A 167 1910 1941 1761 122 -34 -93 C ATOM 1370 O ILE A 167 3.491 16.318 36.820 1.00 14.87 O ANISOU 1370 O ILE A 167 1805 2102 1743 220 -120 -57 O ATOM 1371 CB ILE A 167 2.303 18.376 38.731 1.00 14.81 C ANISOU 1371 CB ILE A 167 2016 1917 1692 -26 -57 -7 C ATOM 1372 CG1 ILE A 167 1.529 18.758 40.021 1.00 16.02 C ANISOU 1372 CG1 ILE A 167 2211 1935 1940 -47 -12 -100 C ATOM 1373 CG2 ILE A 167 2.416 19.550 37.780 1.00 15.47 C ANISOU 1373 CG2 ILE A 167 2004 1903 1968 88 35 -74 C ATOM 1374 CD1 ILE A 167 2.155 19.886 40.813 1.00 16.36 C ANISOU 1374 CD1 ILE A 167 2252 2056 1908 -80 -17 -155 C ATOM 1375 N PRO A 168 1.702 16.864 35.633 1.00 14.47 N ANISOU 1375 N PRO A 168 1868 1921 1710 84 20 13 N ATOM 1376 CA PRO A 168 2.240 16.268 34.405 1.00 14.16 C ANISOU 1376 CA PRO A 168 1865 1818 1696 105 48 -61 C ATOM 1377 C PRO A 168 3.288 17.149 33.705 1.00 13.88 C ANISOU 1377 C PRO A 168 1792 1744 1735 100 -5 -131 C ATOM 1378 O PRO A 168 3.549 18.296 34.060 1.00 14.97 O ANISOU 1378 O PRO A 168 1937 1920 1829 9 167 -207 O ATOM 1379 CB PRO A 168 0.992 16.092 33.536 1.00 15.01 C ANISOU 1379 CB PRO A 168 1943 1991 1766 -14 -58 29 C ATOM 1380 CG PRO A 168 0.140 17.251 33.929 1.00 15.37 C ANISOU 1380 CG PRO A 168 1860 2285 1694 170 3 -34 C ATOM 1381 CD PRO A 168 0.335 17.389 35.414 1.00 14.86 C ANISOU 1381 CD PRO A 168 1926 1935 1785 131 -38 1 C ATOM 1382 N ILE A 169 3.898 16.548 32.682 1.00 13.87 N ANISOU 1382 N ILE A 169 1882 1666 1719 27 82 -102 N ATOM 1383 CA ILE A 169 5.016 17.189 31.994 1.00 14.18 C ANISOU 1383 CA ILE A 169 1803 1736 1849 65 120 -6 C ATOM 1384 C ILE A 169 4.517 18.356 31.130 1.00 14.30 C ANISOU 1384 C ILE A 169 1800 1745 1886 80 162 -61 C ATOM 1385 O ILE A 169 3.401 18.288 30.625 1.00 14.24 O ANISOU 1385 O ILE A 169 1723 1876 1808 16 157 26 O ATOM 1386 CB ILE A 169 5.753 16.119 31.145 1.00 14.35 C ANISOU 1386 CB ILE A 169 1787 1824 1840 159 -5 -40 C ATOM 1387 CG1 ILE A 169 7.171 16.534 30.799 1.00 16.18 C ANISOU 1387 CG1 ILE A 169 1827 2136 2182 177 123 -234 C ATOM 1388 CG2 ILE A 169 4.980 15.710 29.930 1.00 14.78 C ANISOU 1388 CG2 ILE A 169 1800 1948 1866 80 22 -200 C ATOM 1389 CD1 ILE A 169 8.025 15.371 30.293 1.00 16.89 C ANISOU 1389 CD1 ILE A 169 1843 2202 2371 206 72 -77 C ATOM 1390 N PRO A 170 5.303 19.437 30.956 1.00 14.63 N ANISOU 1390 N PRO A 170 1752 1872 1934 16 70 -52 N ATOM 1391 CA PRO A 170 4.854 20.562 30.121 1.00 14.80 C ANISOU 1391 CA PRO A 170 1710 1910 2001 157 150 -19 C ATOM 1392 C PRO A 170 5.079 20.219 28.673 1.00 15.42 C ANISOU 1392 C PRO A 170 1820 2122 1917 283 118 47 C ATOM 1393 O PRO A 170 6.197 20.083 28.233 1.00 18.00 O ANISOU 1393 O PRO A 170 1883 2817 2136 208 211 -123 O ATOM 1394 CB PRO A 170 5.737 21.760 30.596 1.00 16.11 C ANISOU 1394 CB PRO A 170 1950 1964 2206 62 208 -35 C ATOM 1395 CG PRO A 170 6.556 21.237 31.782 1.00 17.09 C ANISOU 1395 CG PRO A 170 2009 2023 2460 -60 -41 -85 C ATOM 1396 CD PRO A 170 6.595 19.774 31.579 1.00 16.54 C ANISOU 1396 CD PRO A 170 1973 2034 2276 62 -134 -46 C ATOM 1397 N VAL A 171 3.980 20.109 27.937 1.00 14.55 N ANISOU 1397 N VAL A 171 1783 1945 1797 94 326 -31 N ATOM 1398 CA VAL A 171 4.046 19.680 26.559 1.00 14.47 C ANISOU 1398 CA VAL A 171 1781 1913 1804 228 238 44 C ATOM 1399 C VAL A 171 4.029 20.902 25.655 1.00 14.98 C ANISOU 1399 C VAL A 171 1850 1846 1995 232 258 -2 C ATOM 1400 O VAL A 171 3.010 21.543 25.461 1.00 19.08 O ANISOU 1400 O VAL A 171 2026 2742 2479 598 240 322 O ATOM 1401 CB VAL A 171 2.937 18.719 26.177 1.00 14.67 C ANISOU 1401 CB VAL A 171 1837 2068 1669 202 310 7 C ATOM 1402 CG1 VAL A 171 3.120 18.303 24.698 1.00 15.46 C ANISOU 1402 CG1 VAL A 171 2178 1996 1698 123 218 -4 C ATOM 1403 CG2 VAL A 171 2.877 17.538 27.102 1.00 16.77 C ANISOU 1403 CG2 VAL A 171 2290 2280 1799 -196 335 91 C ATOM 1404 N ASP A 172 5.182 21.275 25.162 1.00 14.78 N ANISOU 1404 N ASP A 172 1836 1716 2062 197 176 115 N ATOM 1405 CA ASP A 172 5.339 22.231 24.056 1.00 16.06 C ANISOU 1405 CA ASP A 172 2196 1714 2189 137 333 84 C ATOM 1406 C ASP A 172 5.702 21.449 22.792 1.00 14.76 C ANISOU 1406 C ASP A 172 1882 1559 2166 135 375 161 C ATOM 1407 O ASP A 172 5.811 20.218 22.827 1.00 14.14 O ANISOU 1407 O ASP A 172 1824 1535 2011 13 347 139 O ATOM 1408 CB ASP A 172 6.379 23.312 24.386 1.00 18.15 C ANISOU 1408 CB ASP A 172 2605 1768 2520 7 305 112 C ATOM 1409 CG ASP A 172 7.747 22.774 24.707 1.00 18.82 C ANISOU 1409 CG ASP A 172 2391 2230 2527 -225 233 -157 C ATOM 1410 OD1 ASP A 172 8.032 21.579 24.540 1.00 17.95 O ANISOU 1410 OD1 ASP A 172 2169 1996 2653 -70 120 -105 O ATOM 1411 OD2 ASP A 172 8.625 23.548 25.188 1.00 21.14 O ANISOU 1411 OD2 ASP A 172 2605 2329 3097 -344 27 22 O ATOM 1412 N TYR A 173 5.874 22.150 21.664 1.00 15.02 N ANISOU 1412 N TYR A 173 1968 1423 2316 -16 404 291 N ATOM 1413 CA TYR A 173 6.151 21.463 20.413 1.00 13.91 C ANISOU 1413 CA TYR A 173 1654 1433 2197 41 247 224 C ATOM 1414 C TYR A 173 7.419 20.634 20.537 1.00 13.48 C ANISOU 1414 C TYR A 173 1733 1405 1982 -75 166 341 C ATOM 1415 O TYR A 173 7.515 19.535 20.002 1.00 14.16 O ANISOU 1415 O TYR A 173 1771 1468 2141 90 195 181 O ATOM 1416 CB TYR A 173 6.284 22.478 19.274 1.00 13.78 C ANISOU 1416 CB TYR A 173 1640 1336 2260 -54 167 265 C ATOM 1417 CG TYR A 173 6.512 21.896 17.927 1.00 12.59 C ANISOU 1417 CG TYR A 173 1306 1261 2217 -40 233 334 C ATOM 1418 CD1 TYR A 173 5.501 21.248 17.240 1.00 14.09 C ANISOU 1418 CD1 TYR A 173 1160 1731 2461 -303 272 268 C ATOM 1419 CD2 TYR A 173 7.741 22.041 17.298 1.00 13.20 C ANISOU 1419 CD2 TYR A 173 1111 1676 2227 -8 227 95 C ATOM 1420 CE1 TYR A 173 5.687 20.743 15.968 1.00 14.51 C ANISOU 1420 CE1 TYR A 173 1325 1854 2331 -342 101 320 C ATOM 1421 CE2 TYR A 173 7.930 21.556 16.017 1.00 13.83 C ANISOU 1421 CE2 TYR A 173 1165 1773 2316 -144 408 186 C ATOM 1422 CZ TYR A 173 6.920 20.885 15.374 1.00 13.35 C ANISOU 1422 CZ TYR A 173 1367 1478 2224 -184 206 371 C ATOM 1423 OH TYR A 173 7.139 20.389 14.109 1.00 15.89 O ANISOU 1423 OH TYR A 173 1976 1829 2230 -490 426 390 O ATOM 1424 N ARG A 174 8.427 21.163 21.234 1.00 13.93 N ANISOU 1424 N ARG A 174 1646 1504 2141 72 200 203 N ATOM 1425 CA ARG A 174 9.669 20.432 21.439 1.00 14.21 C ANISOU 1425 CA ARG A 174 1481 1725 2191 -124 124 135 C ATOM 1426 C ARG A 174 9.453 19.082 22.115 1.00 13.61 C ANISOU 1426 C ARG A 174 1546 1462 2162 -26 59 226 C ATOM 1427 O ARG A 174 9.975 18.061 21.691 1.00 14.19 O ANISOU 1427 O ARG A 174 1560 1620 2208 -90 189 107 O ATOM 1428 CB ARG A 174 10.635 21.302 22.203 1.00 15.02 C ANISOU 1428 CB ARG A 174 1616 1914 2176 84 29 96 C ATOM 1429 CG ARG A 174 11.940 20.667 22.513 1.00 15.80 C ANISOU 1429 CG ARG A 174 1572 2099 2332 -79 60 95 C ATOM 1430 CD ARG A 174 12.878 21.609 23.238 1.00 17.18 C ANISOU 1430 CD ARG A 174 1782 2245 2501 -157 -37 75 C ATOM 1431 NE ARG A 174 12.182 22.160 24.378 1.00 17.54 N ANISOU 1431 NE ARG A 174 2009 2128 2524 -185 -78 -127 N ATOM 1432 CZ ARG A 174 12.006 21.523 25.521 1.00 19.25 C ANISOU 1432 CZ ARG A 174 2658 2186 2470 -25 -82 36 C ATOM 1433 NH1 ARG A 174 12.713 20.439 25.838 1.00 19.47 N ANISOU 1433 NH1 ARG A 174 2176 2823 2397 101 15 183 N ATOM 1434 NH2 ARG A 174 11.135 22.026 26.390 1.00 21.85 N ANISOU 1434 NH2 ARG A 174 2973 2664 2662 243 67 -84 N ATOM 1435 N VAL A 175 8.715 19.090 23.220 1.00 14.12 N ANISOU 1435 N VAL A 175 1706 1506 2151 22 143 144 N ATOM 1436 CA VAL A 175 8.451 17.831 23.934 1.00 13.86 C ANISOU 1436 CA VAL A 175 1583 1681 2000 19 18 138 C ATOM 1437 C VAL A 175 7.633 16.899 23.049 1.00 12.80 C ANISOU 1437 C VAL A 175 1605 1555 1703 27 128 186 C ATOM 1438 O VAL A 175 7.862 15.674 23.023 1.00 13.40 O ANISOU 1438 O VAL A 175 1691 1590 1810 -9 61 266 O ATOM 1439 CB VAL A 175 7.766 18.119 25.291 1.00 13.66 C ANISOU 1439 CB VAL A 175 1414 1729 2044 4 -35 67 C ATOM 1440 CG1 VAL A 175 7.160 16.877 25.881 1.00 14.64 C ANISOU 1440 CG1 VAL A 175 1736 1918 1909 244 16 163 C ATOM 1441 CG2 VAL A 175 8.769 18.747 26.241 1.00 15.80 C ANISOU 1441 CG2 VAL A 175 2001 1901 2098 87 51 -157 C ATOM 1442 N ALA A 176 6.693 17.441 22.292 1.00 13.07 N ANISOU 1442 N ALA A 176 1603 1468 1895 23 5 59 N ATOM 1443 CA ALA A 176 5.950 16.608 21.334 1.00 13.00 C ANISOU 1443 CA ALA A 176 1584 1532 1823 27 63 202 C ATOM 1444 C ALA A 176 6.881 15.993 20.306 1.00 12.94 C ANISOU 1444 C ALA A 176 1648 1442 1825 112 4 210 C ATOM 1445 O ALA A 176 6.776 14.789 20.020 1.00 12.76 O ANISOU 1445 O ALA A 176 1585 1554 1708 79 -53 118 O ATOM 1446 CB ALA A 176 4.860 17.429 20.645 1.00 13.63 C ANISOU 1446 CB ALA A 176 1598 1523 2057 86 -4 97 C ATOM 1447 N ARG A 177 7.805 16.802 19.773 1.00 13.10 N ANISOU 1447 N ARG A 177 1515 1561 1901 9 81 136 N ATOM 1448 CA ARG A 177 8.765 16.285 18.813 1.00 13.33 C ANISOU 1448 CA ARG A 177 1674 1537 1853 82 40 300 C ATOM 1449 C ARG A 177 9.629 15.182 19.422 1.00 12.71 C ANISOU 1449 C ARG A 177 1463 1508 1858 22 95 216 C ATOM 1450 O ARG A 177 9.944 14.194 18.766 1.00 14.03 O ANISOU 1450 O ARG A 177 1804 1635 1888 160 -141 254 O ATOM 1451 CB ARG A 177 9.685 17.411 18.298 1.00 14.92 C ANISOU 1451 CB ARG A 177 1814 1694 2158 149 212 236 C ATOM 1452 CG ARG A 177 9.110 18.400 17.355 1.00 15.94 C ANISOU 1452 CG ARG A 177 1720 2180 2154 140 152 238 C ATOM 1453 CD ARG A 177 10.210 19.134 16.518 1.00 19.52 C ANISOU 1453 CD ARG A 177 2419 2317 2679 13 145 262 C ATOM 1454 NE ARG A 177 10.938 18.208 15.687 1.00 19.24 N ANISOU 1454 NE ARG A 177 2315 2702 2291 -152 177 100 N ATOM 1455 CZ ARG A 177 12.080 18.407 15.020 1.00 15.39 C ANISOU 1455 CZ ARG A 177 1845 1920 2080 102 40 247 C ATOM 1456 NH1 ARG A 177 12.763 19.526 15.090 1.00 16.42 N ANISOU 1456 NH1 ARG A 177 1710 2004 2523 132 313 -13 N ATOM 1457 NH2 ARG A 177 12.571 17.380 14.361 1.00 17.61 N ANISOU 1457 NH2 ARG A 177 2070 2023 2597 12 -87 161 N ATOM 1458 N LEU A 178 10.117 15.381 20.644 1.00 12.97 N ANISOU 1458 N LEU A 178 1438 1586 1903 25 62 30 N ATOM 1459 CA LEU A 178 10.957 14.357 21.277 1.00 12.77 C ANISOU 1459 CA LEU A 178 1565 1506 1777 17 -21 144 C ATOM 1460 C LEU A 178 10.199 13.084 21.511 1.00 12.60 C ANISOU 1460 C LEU A 178 1513 1588 1686 103 -103 223 C ATOM 1461 O LEU A 178 10.747 11.988 21.370 1.00 13.10 O ANISOU 1461 O LEU A 178 1464 1604 1907 131 -75 161 O ATOM 1462 CB LEU A 178 11.538 14.913 22.588 1.00 13.18 C ANISOU 1462 CB LEU A 178 1599 1696 1711 30 -16 74 C ATOM 1463 CG LEU A 178 12.593 15.996 22.380 1.00 13.83 C ANISOU 1463 CG LEU A 178 1528 1748 1978 -26 -153 103 C ATOM 1464 CD1 LEU A 178 12.915 16.653 23.731 1.00 16.58 C ANISOU 1464 CD1 LEU A 178 2005 2244 2051 -259 -213 -49 C ATOM 1465 CD2 LEU A 178 13.888 15.419 21.734 1.00 14.64 C ANISOU 1465 CD2 LEU A 178 1507 2025 2028 -216 -92 40 C ATOM 1466 N THR A 179 8.928 13.184 21.885 1.00 12.21 N ANISOU 1466 N THR A 179 1450 1437 1752 72 88 160 N ATOM 1467 CA THR A 179 8.115 12.013 22.123 1.00 12.61 C ANISOU 1467 CA THR A 179 1527 1461 1802 8 24 216 C ATOM 1468 C THR A 179 7.953 11.213 20.833 1.00 12.37 C ANISOU 1468 C THR A 179 1365 1388 1945 -2 -37 257 C ATOM 1469 O THR A 179 8.038 9.994 20.829 1.00 13.95 O ANISOU 1469 O THR A 179 1789 1520 1990 105 -112 213 O ATOM 1470 CB THR A 179 6.750 12.470 22.684 1.00 13.32 C ANISOU 1470 CB THR A 179 1621 1482 1958 226 34 248 C ATOM 1471 OG1 THR A 179 6.960 13.240 23.899 1.00 13.25 O ANISOU 1471 OG1 THR A 179 1717 1601 1716 3 100 188 O ATOM 1472 CG2 THR A 179 5.866 11.298 23.086 1.00 13.53 C ANISOU 1472 CG2 THR A 179 1544 1586 2010 -44 125 93 C ATOM 1473 N TRP A 180 7.738 11.935 19.730 1.00 12.42 N ANISOU 1473 N TRP A 180 1583 1325 1810 62 35 211 N ATOM 1474 CA TRP A 180 7.648 11.320 18.404 1.00 13.24 C ANISOU 1474 CA TRP A 180 1525 1616 1889 65 37 241 C ATOM 1475 C TRP A 180 9.003 10.726 17.982 1.00 12.86 C ANISOU 1475 C TRP A 180 1397 1686 1800 164 -71 170 C ATOM 1476 O TRP A 180 9.057 9.593 17.479 1.00 13.49 O ANISOU 1476 O TRP A 180 1679 1539 1904 56 -94 101 O ATOM 1477 CB TRP A 180 7.204 12.396 17.422 1.00 14.97 C ANISOU 1477 CB TRP A 180 1947 1773 1966 252 -100 146 C ATOM 1478 CG TRP A 180 7.030 11.945 16.029 1.00 16.81 C ANISOU 1478 CG TRP A 180 2128 2039 2219 373 -133 113 C ATOM 1479 CD1 TRP A 180 5.887 11.391 15.472 1.00 19.85 C ANISOU 1479 CD1 TRP A 180 2295 2935 2311 228 -140 81 C ATOM 1480 CD2 TRP A 180 7.961 12.034 14.974 1.00 19.68 C ANISOU 1480 CD2 TRP A 180 2213 2687 2576 451 -9 116 C ATOM 1481 NE1 TRP A 180 6.078 11.123 14.144 1.00 20.30 N ANISOU 1481 NE1 TRP A 180 2406 2983 2322 -12 -123 -142 N ATOM 1482 CE2 TRP A 180 7.348 11.493 13.807 1.00 18.20 C ANISOU 1482 CE2 TRP A 180 2201 2768 1943 204 5 -101 C ATOM 1483 CE3 TRP A 180 9.276 12.458 14.891 1.00 21.87 C ANISOU 1483 CE3 TRP A 180 2690 2795 2823 -230 -98 105 C ATOM 1484 CZ2 TRP A 180 8.010 11.397 12.581 1.00 20.06 C ANISOU 1484 CZ2 TRP A 180 2497 2737 2385 94 99 -94 C ATOM 1485 CZ3 TRP A 180 9.926 12.363 13.670 1.00 22.26 C ANISOU 1485 CZ3 TRP A 180 2620 3047 2788 -66 96 215 C ATOM 1486 CH2 TRP A 180 9.298 11.848 12.539 1.00 21.18 C ANISOU 1486 CH2 TRP A 180 2529 2845 2673 16 210 178 C ATOM 1487 N CYS A 181 10.106 11.453 18.209 1.00 12.58 N ANISOU 1487 N CYS A 181 1389 1516 1875 157 -60 162 N ATOM 1488 CA CYS A 181 11.423 11.007 17.830 1.00 13.31 C ANISOU 1488 CA CYS A 181 1507 1484 2063 79 101 208 C ATOM 1489 C CYS A 181 11.835 9.718 18.532 1.00 13.67 C ANISOU 1489 C CYS A 181 1429 1593 2169 61 23 135 C ATOM 1490 O CYS A 181 12.594 8.920 17.979 1.00 14.14 O ANISOU 1490 O CYS A 181 1700 1535 2137 233 -15 158 O ATOM 1491 CB CYS A 181 12.472 12.067 18.116 1.00 14.91 C ANISOU 1491 CB CYS A 181 1741 1619 2303 135 23 165 C ATOM 1492 SG CYS A 181 12.521 13.387 16.872 1.00 17.38 S ANISOU 1492 SG CYS A 181 1845 1817 2940 16 63 473 S ATOM 1493 N ALA A 182 11.336 9.507 19.755 1.00 13.40 N ANISOU 1493 N ALA A 182 1451 1635 2003 135 -74 241 N ATOM 1494 CA ALA A 182 11.573 8.288 20.508 1.00 13.67 C ANISOU 1494 CA ALA A 182 1591 1575 2025 42 36 172 C ATOM 1495 C ALA A 182 10.631 7.146 20.128 1.00 13.99 C ANISOU 1495 C ALA A 182 1782 1589 1944 106 -42 149 C ATOM 1496 O ALA A 182 10.729 6.057 20.672 1.00 14.76 O ANISOU 1496 O ALA A 182 1617 1639 2349 17 -105 286 O ATOM 1497 CB ALA A 182 11.431 8.591 21.978 1.00 14.38 C ANISOU 1497 CB ALA A 182 1631 1671 2159 -19 -127 187 C ATOM 1498 N GLY A 183 9.707 7.397 19.218 1.00 14.03 N ANISOU 1498 N GLY A 183 1631 1646 2053 -39 -9 196 N ATOM 1499 CA GLY A 183 8.801 6.339 18.761 1.00 14.07 C ANISOU 1499 CA GLY A 183 1707 1606 2029 0 -86 143 C ATOM 1500 C GLY A 183 7.713 6.026 19.760 1.00 14.35 C ANISOU 1500 C GLY A 183 1592 1593 2266 -4 -124 125 C ATOM 1501 O GLY A 183 7.091 4.973 19.678 1.00 15.87 O ANISOU 1501 O GLY A 183 1957 1686 2384 -124 -21 95 O ATOM 1502 N LEU A 184 7.431 6.940 20.679 1.00 14.22 N ANISOU 1502 N LEU A 184 1609 1585 2210 -81 14 147 N ATOM 1503 CA LEU A 184 6.436 6.682 21.722 1.00 13.96 C ANISOU 1503 CA LEU A 184 1641 1550 2111 59 -13 203 C ATOM 1504 C LEU A 184 5.008 6.958 21.286 1.00 14.62 C ANISOU 1504 C LEU A 184 1628 1733 2191 -25 56 201 C ATOM 1505 O LEU A 184 4.070 6.482 21.927 1.00 16.05 O ANISOU 1505 O LEU A 184 1558 2001 2538 -20 176 426 O ATOM 1506 CB LEU A 184 6.765 7.496 22.948 1.00 14.42 C ANISOU 1506 CB LEU A 184 1705 1615 2160 44 148 305 C ATOM 1507 CG LEU A 184 8.097 7.146 23.628 1.00 14.75 C ANISOU 1507 CG LEU A 184 1752 1788 2063 -18 -63 233 C ATOM 1508 CD1 LEU A 184 8.455 8.233 24.602 1.00 16.40 C ANISOU 1508 CD1 LEU A 184 2052 1987 2189 103 -43 133 C ATOM 1509 CD2 LEU A 184 7.983 5.809 24.322 1.00 17.32 C ANISOU 1509 CD2 LEU A 184 1955 1734 2889 20 -413 519 C ATOM 1510 N ILE A 185 4.874 7.779 20.247 1.00 15.61 N ANISOU 1510 N ILE A 185 1719 1909 2301 74 -18 317 N ATOM 1511 CA ILE A 185 3.583 8.052 19.588 1.00 17.64 C ANISOU 1511 CA ILE A 185 1817 2240 2642 94 -69 243 C ATOM 1512 C ILE A 185 3.726 7.832 18.112 1.00 20.86 C ANISOU 1512 C ILE A 185 2407 2699 2819 47 -43 258 C ATOM 1513 O ILE A 185 4.813 8.007 17.584 1.00 21.22 O ANISOU 1513 O ILE A 185 2493 2805 2762 104 42 334 O ATOM 1514 CB ILE A 185 3.131 9.492 19.861 1.00 17.74 C ANISOU 1514 CB ILE A 185 1700 2277 2763 110 -77 238 C ATOM 1515 CG1 ILE A 185 4.174 10.527 19.404 1.00 17.41 C ANISOU 1515 CG1 ILE A 185 1697 2138 2780 197 -254 296 C ATOM 1516 CG2 ILE A 185 2.803 9.624 21.257 1.00 18.62 C ANISOU 1516 CG2 ILE A 185 1906 2477 2692 154 -186 197 C ATOM 1517 CD1 ILE A 185 3.783 11.980 19.508 1.00 18.18 C ANISOU 1517 CD1 ILE A 185 2072 2280 2555 231 -49 374 C ATOM 1518 N ASP A 186 2.636 7.436 17.463 1.00 23.05 N ANISOU 1518 N ASP A 186 2714 3066 2977 -61 -84 155 N ATOM 1519 CA ASP A 186 2.637 7.162 16.020 1.00 23.52 C ANISOU 1519 CA ASP A 186 2857 3087 2991 44 -48 135 C ATOM 1520 C ASP A 186 1.908 8.264 15.252 1.00 24.21 C ANISOU 1520 C ASP A 186 2851 3310 3035 -46 -162 174 C ATOM 1521 O ASP A 186 1.742 8.172 14.040 1.00 27.78 O ANISOU 1521 O ASP A 186 3643 3799 3110 72 20 143 O ATOM 1522 CB ASP A 186 2.001 5.797 15.745 1.00 25.18 C ANISOU 1522 CB ASP A 186 3099 3259 3209 -51 -85 126 C ATOM 1523 CG ASP A 186 2.282 5.285 14.338 1.00 28.40 C ANISOU 1523 CG ASP A 186 3581 3618 3591 0 27 26 C ATOM 1524 OD1 ASP A 186 3.468 5.026 14.012 1.00 35.00 O ANISOU 1524 OD1 ASP A 186 4001 4645 4652 216 179 27 O ATOM 1525 OD2 ASP A 186 1.383 5.098 13.488 1.00 35.65 O ANISOU 1525 OD2 ASP A 186 4213 4726 4603 -15 -255 46 O ATOM 1526 N PHE A 187 1.454 9.284 15.958 1.00 22.77 N ANISOU 1526 N PHE A 187 2585 3083 2982 -79 -146 325 N ATOM 1527 CA PHE A 187 0.854 10.455 15.347 1.00 21.11 C ANISOU 1527 CA PHE A 187 2337 2876 2807 -147 -16 296 C ATOM 1528 C PHE A 187 1.856 11.604 15.398 1.00 19.45 C ANISOU 1528 C PHE A 187 1993 2824 2572 -53 0 439 C ATOM 1529 O PHE A 187 2.736 11.625 16.243 1.00 19.70 O ANISOU 1529 O PHE A 187 1723 2992 2770 -289 132 598 O ATOM 1530 CB PHE A 187 -0.482 10.817 16.012 1.00 22.22 C ANISOU 1530 CB PHE A 187 2545 2939 2958 -25 26 243 C ATOM 1531 CG PHE A 187 -0.463 10.766 17.514 1.00 21.49 C ANISOU 1531 CG PHE A 187 2339 2986 2839 -76 111 246 C ATOM 1532 CD1 PHE A 187 -0.753 9.575 18.186 1.00 22.19 C ANISOU 1532 CD1 PHE A 187 2725 2738 2968 -300 -41 -13 C ATOM 1533 CD2 PHE A 187 -0.176 11.895 18.260 1.00 21.89 C ANISOU 1533 CD2 PHE A 187 2346 2862 3106 55 59 210 C ATOM 1534 CE1 PHE A 187 -0.748 9.517 19.574 1.00 22.47 C ANISOU 1534 CE1 PHE A 187 2492 3037 3009 -195 -38 173 C ATOM 1535 CE2 PHE A 187 -0.182 11.848 19.663 1.00 21.03 C ANISOU 1535 CE2 PHE A 187 2269 2629 3093 96 128 189 C ATOM 1536 CZ PHE A 187 -0.454 10.643 20.315 1.00 21.84 C ANISOU 1536 CZ PHE A 187 2373 2894 3029 -244 176 152 C ATOM 1537 N PRO A 188 1.800 12.510 14.428 1.00 17.95 N ANISOU 1537 N PRO A 188 1838 2571 2410 -103 79 335 N ATOM 1538 CA PRO A 188 2.861 13.506 14.337 1.00 19.08 C ANISOU 1538 CA PRO A 188 2051 2687 2509 -127 197 280 C ATOM 1539 C PRO A 188 2.875 14.570 15.449 1.00 16.98 C ANISOU 1539 C PRO A 188 1563 2581 2307 -55 84 407 C ATOM 1540 O PRO A 188 1.858 14.759 16.142 1.00 17.24 O ANISOU 1540 O PRO A 188 1516 2886 2147 2 320 426 O ATOM 1541 CB PRO A 188 2.608 14.152 12.982 1.00 19.94 C ANISOU 1541 CB PRO A 188 2418 2698 2459 -159 315 302 C ATOM 1542 CG PRO A 188 1.633 13.233 12.240 1.00 21.47 C ANISOU 1542 CG PRO A 188 2426 2898 2831 -142 218 256 C ATOM 1543 CD PRO A 188 0.808 12.617 13.335 1.00 19.09 C ANISOU 1543 CD PRO A 188 2156 2730 2366 -140 -6 391 C ATOM 1544 N PRO A 189 3.993 15.270 15.623 1.00 16.51 N ANISOU 1544 N PRO A 189 1636 2283 2353 71 223 410 N ATOM 1545 CA PRO A 189 4.117 16.229 16.698 1.00 16.53 C ANISOU 1545 CA PRO A 189 1689 2316 2276 -47 160 368 C ATOM 1546 C PRO A 189 3.037 17.289 16.769 1.00 15.89 C ANISOU 1546 C PRO A 189 1704 2174 2158 8 244 504 C ATOM 1547 O PRO A 189 2.636 17.688 17.840 1.00 15.78 O ANISOU 1547 O PRO A 189 1599 2208 2185 -194 253 498 O ATOM 1548 CB PRO A 189 5.521 16.847 16.481 1.00 18.27 C ANISOU 1548 CB PRO A 189 1938 2313 2689 -141 94 229 C ATOM 1549 CG PRO A 189 6.263 15.806 15.743 1.00 18.44 C ANISOU 1549 CG PRO A 189 2047 2321 2637 -58 69 172 C ATOM 1550 CD PRO A 189 5.252 15.152 14.862 1.00 15.43 C ANISOU 1550 CD PRO A 189 1507 2185 2169 78 218 378 C ATOM 1551 N GLU A 190 2.584 17.776 15.620 1.00 15.45 N ANISOU 1551 N GLU A 190 1442 2307 2121 57 351 519 N ATOM 1552 CA GLU A 190 1.534 18.777 15.582 1.00 16.43 C ANISOU 1552 CA GLU A 190 1465 2433 2341 69 385 423 C ATOM 1553 C GLU A 190 0.247 18.262 16.209 1.00 15.73 C ANISOU 1553 C GLU A 190 1474 2437 2065 87 298 433 C ATOM 1554 O GLU A 190 -0.433 18.987 16.950 1.00 18.58 O ANISOU 1554 O GLU A 190 1828 2780 2449 66 608 341 O ATOM 1555 CB GLU A 190 1.268 19.178 14.117 1.00 18.53 C ANISOU 1555 CB GLU A 190 1879 2367 2795 73 424 320 C ATOM 1556 CG GLU A 190 2.483 19.814 13.452 1.00 21.65 C ANISOU 1556 CG GLU A 190 2398 2815 3010 -268 294 278 C ATOM 1557 CD GLU A 190 3.665 18.858 13.192 1.00 26.13 C ANISOU 1557 CD GLU A 190 3263 3024 3641 -8 341 -44 C ATOM 1558 OE1 GLU A 190 3.510 17.613 13.004 1.00 22.56 O ANISOU 1558 OE1 GLU A 190 3148 2910 2512 -266 447 670 O ATOM 1559 OE2 GLU A 190 4.806 19.368 13.166 1.00 29.84 O ANISOU 1559 OE2 GLU A 190 3315 4133 3888 -176 -279 -210 O ATOM 1560 N GLU A 191 -0.091 17.028 15.876 1.00 16.48 N ANISOU 1560 N GLU A 191 1564 2523 2174 -14 268 419 N ATOM 1561 CA GLU A 191 -1.293 16.390 16.432 1.00 16.54 C ANISOU 1561 CA GLU A 191 1469 2506 2310 -35 202 429 C ATOM 1562 C GLU A 191 -1.072 16.135 17.921 1.00 16.03 C ANISOU 1562 C GLU A 191 1509 2391 2188 -7 206 458 C ATOM 1563 O GLU A 191 -1.958 16.384 18.727 1.00 16.62 O ANISOU 1563 O GLU A 191 1594 2612 2106 -136 397 517 O ATOM 1564 CB GLU A 191 -1.553 15.067 15.716 1.00 17.65 C ANISOU 1564 CB GLU A 191 1596 2643 2466 -154 128 320 C ATOM 1565 CG GLU A 191 -2.738 14.282 16.288 1.00 19.28 C ANISOU 1565 CG GLU A 191 1901 2819 2605 -169 379 336 C ATOM 1566 CD GLU A 191 -3.153 13.056 15.483 1.00 22.87 C ANISOU 1566 CD GLU A 191 2610 3031 3045 -217 138 154 C ATOM 1567 OE1 GLU A 191 -2.721 12.856 14.319 1.00 26.64 O ANISOU 1567 OE1 GLU A 191 3369 3335 3415 -241 281 -53 O ATOM 1568 OE2 GLU A 191 -3.970 12.274 16.021 1.00 30.58 O ANISOU 1568 OE2 GLU A 191 3749 3839 4029 -423 386 300 O ATOM 1569 N ALA A 192 0.115 15.630 18.275 1.00 16.62 N ANISOU 1569 N ALA A 192 1726 2382 2206 -31 225 503 N ATOM 1570 CA ALA A 192 0.465 15.389 19.672 1.00 16.35 C ANISOU 1570 CA ALA A 192 1939 2252 2021 -102 212 506 C ATOM 1571 C ALA A 192 0.349 16.644 20.516 1.00 16.56 C ANISOU 1571 C ALA A 192 1940 2322 2028 -51 320 578 C ATOM 1572 O ALA A 192 -0.126 16.592 21.671 1.00 18.01 O ANISOU 1572 O ALA A 192 2105 2686 2050 -170 388 632 O ATOM 1573 CB ALA A 192 1.892 14.812 19.740 1.00 17.34 C ANISOU 1573 CB ALA A 192 2164 2384 2039 -100 25 424 C ATOM 1574 N LEU A 193 0.770 17.781 19.964 1.00 16.84 N ANISOU 1574 N LEU A 193 2114 2172 2112 -223 237 325 N ATOM 1575 CA LEU A 193 0.679 19.015 20.711 1.00 18.07 C ANISOU 1575 CA LEU A 193 2228 2340 2298 -107 216 379 C ATOM 1576 C LEU A 193 -0.777 19.398 20.975 1.00 19.22 C ANISOU 1576 C LEU A 193 2373 2564 2365 -93 123 275 C ATOM 1577 O LEU A 193 -1.129 19.854 22.077 1.00 21.04 O ANISOU 1577 O LEU A 193 2649 2699 2643 -18 267 441 O ATOM 1578 CB LEU A 193 1.497 20.118 20.031 1.00 18.17 C ANISOU 1578 CB LEU A 193 2311 2454 2139 -251 237 341 C ATOM 1579 CG LEU A 193 1.512 21.437 20.772 1.00 18.28 C ANISOU 1579 CG LEU A 193 2206 2244 2495 48 233 349 C ATOM 1580 CD1 LEU A 193 2.129 21.309 22.137 1.00 19.33 C ANISOU 1580 CD1 LEU A 193 2218 2647 2478 -211 215 25 C ATOM 1581 CD2 LEU A 193 2.224 22.487 19.962 1.00 20.29 C ANISOU 1581 CD2 LEU A 193 2428 2446 2832 -202 186 181 C ATOM 1582 N ARG A 194 -1.640 19.195 19.983 1.00 20.28 N ANISOU 1582 N ARG A 194 2232 2758 2715 -29 112 277 N ATOM 1583 CA ARG A 194 -3.075 19.365 20.148 1.00 21.25 C ANISOU 1583 CA ARG A 194 2453 2862 2756 68 114 245 C ATOM 1584 C ARG A 194 -3.604 18.430 21.251 1.00 21.32 C ANISOU 1584 C ARG A 194 2438 3000 2660 68 143 162 C ATOM 1585 O ARG A 194 -4.346 18.855 22.152 1.00 24.54 O ANISOU 1585 O ARG A 194 2777 3392 3152 79 365 -6 O ATOM 1586 CB ARG A 194 -3.817 19.081 18.822 1.00 22.28 C ANISOU 1586 CB ARG A 194 2471 3108 2883 156 19 271 C ATOM 1587 CG ARG A 194 -3.671 20.148 17.744 1.00 25.66 C ANISOU 1587 CG ARG A 194 3213 3147 3389 90 138 232 C ATOM 1588 CD ARG A 194 -4.714 20.058 16.626 1.00 26.02 C ANISOU 1588 CD ARG A 194 3128 3420 3338 64 6 283 C ATOM 1589 NE ARG A 194 -4.557 18.840 15.836 1.00 27.91 N ANISOU 1589 NE ARG A 194 3443 3587 3575 114 -76 228 N ATOM 1590 CZ ARG A 194 -3.721 18.704 14.804 1.00 29.47 C ANISOU 1590 CZ ARG A 194 3740 3779 3677 97 -51 141 C ATOM 1591 NH1 ARG A 194 -2.948 19.713 14.405 1.00 29.71 N ANISOU 1591 NH1 ARG A 194 3607 3812 3866 -69 -128 127 N ATOM 1592 NH2 ARG A 194 -3.649 17.547 14.163 1.00 32.34 N ANISOU 1592 NH2 ARG A 194 4156 4004 4125 -84 90 4 N ATOM 1593 N ARG A 195 -3.225 17.163 21.141 1.00 18.82 N ANISOU 1593 N ARG A 195 2316 2639 2193 -141 74 236 N ATOM 1594 CA ARG A 195 -3.633 16.100 22.073 1.00 20.19 C ANISOU 1594 CA ARG A 195 2481 2850 2340 -214 89 129 C ATOM 1595 C ARG A 195 -2.616 15.974 23.196 1.00 17.67 C ANISOU 1595 C ARG A 195 1973 2610 2129 -185 196 136 C ATOM 1596 O ARG A 195 -2.156 14.878 23.492 1.00 18.50 O ANISOU 1596 O ARG A 195 2361 2682 1985 -243 227 115 O ATOM 1597 CB ARG A 195 -3.767 14.760 21.327 1.00 22.33 C ANISOU 1597 CB ARG A 195 3077 3022 2382 -377 189 75 C ATOM 1598 CG ARG A 195 -4.827 14.688 20.201 1.00 26.75 C ANISOU 1598 CG ARG A 195 3587 3577 3000 -284 9 52 C ATOM 1599 CD ARG A 195 -4.892 13.325 19.399 1.00 27.06 C ANISOU 1599 CD ARG A 195 3599 3636 3044 -194 -27 -119 C ATOM 1600 NE ARG A 195 -4.599 12.158 20.243 1.00 30.83 N ANISOU 1600 NE ARG A 195 3900 3755 4059 -34 55 3 N ATOM 1601 CZ ARG A 195 -4.179 10.971 19.816 1.00 33.65 C ANISOU 1601 CZ ARG A 195 4415 4060 4311 74 44 2 C ATOM 1602 NH1 ARG A 195 -3.997 10.721 18.524 1.00 34.67 N ANISOU 1602 NH1 ARG A 195 4431 4491 4249 39 -25 81 N ATOM 1603 NH2 ARG A 195 -3.943 10.002 20.705 1.00 36.16 N ANISOU 1603 NH2 ARG A 195 4846 4463 4427 131 12 71 N ATOM 1604 N TYR A 196 -2.297 17.081 23.840 1.00 16.68 N ANISOU 1604 N TYR A 196 1887 2429 2022 61 289 107 N ATOM 1605 CA TYR A 196 -1.184 17.063 24.776 1.00 16.53 C ANISOU 1605 CA TYR A 196 1796 2380 2103 100 130 87 C ATOM 1606 C TYR A 196 -1.400 16.176 25.964 1.00 15.36 C ANISOU 1606 C TYR A 196 1812 2188 1836 111 82 23 C ATOM 1607 O TYR A 196 -0.452 15.640 26.515 1.00 15.51 O ANISOU 1607 O TYR A 196 1745 1996 2152 327 70 -168 O ATOM 1608 CB TYR A 196 -0.803 18.461 25.202 1.00 16.58 C ANISOU 1608 CB TYR A 196 1895 2273 2129 69 174 216 C ATOM 1609 CG TYR A 196 -1.778 19.215 26.054 1.00 16.82 C ANISOU 1609 CG TYR A 196 2206 2114 2068 105 212 31 C ATOM 1610 CD1 TYR A 196 -1.728 19.082 27.433 1.00 19.57 C ANISOU 1610 CD1 TYR A 196 2955 2419 2062 382 -42 105 C ATOM 1611 CD2 TYR A 196 -2.688 20.120 25.505 1.00 17.65 C ANISOU 1611 CD2 TYR A 196 2268 2437 2000 307 245 122 C ATOM 1612 CE1 TYR A 196 -2.568 19.788 28.252 1.00 20.59 C ANISOU 1612 CE1 TYR A 196 2965 2726 2129 383 184 88 C ATOM 1613 CE2 TYR A 196 -3.530 20.853 26.325 1.00 20.42 C ANISOU 1613 CE2 TYR A 196 3007 2483 2265 434 435 69 C ATOM 1614 CZ TYR A 196 -3.459 20.668 27.700 1.00 21.64 C ANISOU 1614 CZ TYR A 196 2872 3072 2277 382 292 87 C ATOM 1615 OH TYR A 196 -4.270 21.353 28.577 1.00 23.81 O ANISOU 1615 OH TYR A 196 3403 3251 2391 553 430 -74 O ATOM 1616 N GLU A 197 -2.640 15.929 26.346 1.00 16.08 N ANISOU 1616 N GLU A 197 1777 2493 1839 135 72 217 N ATOM 1617 CA GLU A 197 -2.886 14.976 27.425 1.00 17.37 C ANISOU 1617 CA GLU A 197 1954 2471 2172 227 28 210 C ATOM 1618 C GLU A 197 -2.441 13.567 27.106 1.00 16.52 C ANISOU 1618 C GLU A 197 1920 2369 1987 94 -99 163 C ATOM 1619 O GLU A 197 -2.003 12.842 28.001 1.00 16.66 O ANISOU 1619 O GLU A 197 1870 2604 1854 125 70 318 O ATOM 1620 CB GLU A 197 -4.353 14.997 27.812 1.00 18.36 C ANISOU 1620 CB GLU A 197 2039 2770 2166 202 100 336 C ATOM 1621 CG GLU A 197 -4.773 16.282 28.470 1.00 22.64 C ANISOU 1621 CG GLU A 197 2751 3058 2790 100 64 124 C ATOM 1622 CD GLU A 197 -6.277 16.311 28.708 1.00 25.62 C ANISOU 1622 CD GLU A 197 2986 3398 3349 221 193 14 C ATOM 1623 OE1 GLU A 197 -7.040 15.730 27.896 1.00 33.47 O ANISOU 1623 OE1 GLU A 197 3970 4574 4173 73 -155 -229 O ATOM 1624 OE2 GLU A 197 -6.688 16.912 29.723 1.00 32.36 O ANISOU 1624 OE2 GLU A 197 4077 4392 3824 380 360 -309 O ATOM 1625 N ALA A 198 -2.515 13.161 25.846 1.00 16.83 N ANISOU 1625 N ALA A 198 1889 2585 1919 295 -243 196 N ATOM 1626 CA ALA A 198 -2.038 11.850 25.461 1.00 16.74 C ANISOU 1626 CA ALA A 198 2021 2347 1993 130 -223 92 C ATOM 1627 C ALA A 198 -0.523 11.766 25.647 1.00 15.63 C ANISOU 1627 C ALA A 198 2077 2038 1823 145 -208 -24 C ATOM 1628 O ALA A 198 0.029 10.734 26.053 1.00 17.99 O ANISOU 1628 O ALA A 198 2275 2109 2449 11 -239 19 O ATOM 1629 CB ALA A 198 -2.407 11.553 24.020 1.00 17.44 C ANISOU 1629 CB ALA A 198 2212 2377 2035 110 -326 80 C ATOM 1630 N VAL A 199 0.188 12.835 25.303 1.00 14.81 N ANISOU 1630 N VAL A 199 2057 1778 1791 323 -71 -23 N ATOM 1631 CA VAL A 199 1.615 12.903 25.549 1.00 14.10 C ANISOU 1631 CA VAL A 199 1911 1900 1546 250 104 39 C ATOM 1632 C VAL A 199 1.891 12.813 27.066 1.00 13.29 C ANISOU 1632 C VAL A 199 1737 1854 1457 164 110 89 C ATOM 1633 O VAL A 199 2.789 12.114 27.510 1.00 14.65 O ANISOU 1633 O VAL A 199 1768 2128 1671 302 106 25 O ATOM 1634 CB VAL A 199 2.216 14.150 24.914 1.00 15.13 C ANISOU 1634 CB VAL A 199 2040 2042 1664 351 195 163 C ATOM 1635 CG1 VAL A 199 3.698 14.309 25.278 1.00 16.17 C ANISOU 1635 CG1 VAL A 199 1943 2266 1933 402 50 166 C ATOM 1636 CG2 VAL A 199 2.042 14.133 23.356 1.00 16.54 C ANISOU 1636 CG2 VAL A 199 2048 2297 1937 278 308 122 C ATOM 1637 N GLN A 200 1.152 13.600 27.831 1.00 13.64 N ANISOU 1637 N GLN A 200 1726 1991 1464 184 90 77 N ATOM 1638 CA GLN A 200 1.326 13.545 29.270 1.00 14.04 C ANISOU 1638 CA GLN A 200 1809 1971 1553 113 -16 13 C ATOM 1639 C GLN A 200 1.127 12.161 29.837 1.00 14.11 C ANISOU 1639 C GLN A 200 1725 1982 1651 43 -25 66 C ATOM 1640 O GLN A 200 1.866 11.747 30.735 1.00 14.28 O ANISOU 1640 O GLN A 200 1869 1922 1634 152 -43 -6 O ATOM 1641 CB GLN A 200 0.405 14.557 29.962 1.00 13.46 C ANISOU 1641 CB GLN A 200 1705 1953 1453 48 12 47 C ATOM 1642 CG GLN A 200 0.813 15.988 29.673 1.00 13.66 C ANISOU 1642 CG GLN A 200 1674 1892 1622 106 13 56 C ATOM 1643 CD GLN A 200 -0.083 17.035 30.269 1.00 14.25 C ANISOU 1643 CD GLN A 200 1687 2098 1627 129 117 -74 C ATOM 1644 OE1 GLN A 200 -1.294 16.806 30.413 1.00 14.42 O ANISOU 1644 OE1 GLN A 200 1810 1972 1697 44 109 60 O ATOM 1645 NE2 GLN A 200 0.467 18.172 30.602 1.00 15.03 N ANISOU 1645 NE2 GLN A 200 1752 2134 1823 83 73 66 N ATOM 1646 N LYS A 201 0.154 11.423 29.335 1.00 14.81 N ANISOU 1646 N LYS A 201 1741 2111 1775 61 -71 90 N ATOM 1647 CA LYS A 201 -0.101 10.068 29.832 1.00 15.41 C ANISOU 1647 CA LYS A 201 1797 2182 1875 -4 -77 202 C ATOM 1648 C LYS A 201 1.082 9.147 29.605 1.00 15.04 C ANISOU 1648 C LYS A 201 1861 1923 1928 -125 -49 101 C ATOM 1649 O LYS A 201 1.376 8.287 30.440 1.00 14.93 O ANISOU 1649 O LYS A 201 1825 1868 1977 16 -134 150 O ATOM 1650 CB LYS A 201 -1.380 9.469 29.195 1.00 17.66 C ANISOU 1650 CB LYS A 201 1778 2480 2451 -63 -43 138 C ATOM 1651 CG LYS A 201 -1.745 8.012 29.559 1.00 21.28 C ANISOU 1651 CG LYS A 201 2717 2643 2726 -72 -36 170 C ATOM 1652 CD LYS A 201 -3.072 7.547 28.920 1.00 22.96 C ANISOU 1652 CD LYS A 201 2799 2993 2931 -267 83 150 C ATOM 1653 CE LYS A 201 -3.266 6.025 29.019 1.00 27.39 C ANISOU 1653 CE LYS A 201 3532 3257 3615 -297 0 104 C ATOM 1654 NZ LYS A 201 -4.303 5.490 28.082 1.00 28.83 N ANISOU 1654 NZ LYS A 201 3684 3465 3804 -317 -76 99 N ATOM 1655 N ILE A 202 1.741 9.280 28.461 1.00 14.66 N ANISOU 1655 N ILE A 202 1770 2120 1677 170 -59 52 N ATOM 1656 CA ILE A 202 2.944 8.481 28.185 1.00 15.35 C ANISOU 1656 CA ILE A 202 1874 2084 1874 87 -114 151 C ATOM 1657 C ILE A 202 4.001 8.788 29.232 1.00 14.36 C ANISOU 1657 C ILE A 202 1885 1874 1697 183 -91 -50 C ATOM 1658 O ILE A 202 4.593 7.852 29.806 1.00 14.57 O ANISOU 1658 O ILE A 202 1897 1807 1829 57 24 -74 O ATOM 1659 CB ILE A 202 3.444 8.739 26.752 1.00 16.38 C ANISOU 1659 CB ILE A 202 2223 2125 1873 251 -56 35 C ATOM 1660 CG1 ILE A 202 2.438 8.170 25.749 1.00 17.88 C ANISOU 1660 CG1 ILE A 202 2470 2223 2101 76 -81 -126 C ATOM 1661 CG2 ILE A 202 4.843 8.168 26.573 1.00 17.63 C ANISOU 1661 CG2 ILE A 202 2186 2710 1799 319 -23 -41 C ATOM 1662 CD1 ILE A 202 2.628 8.684 24.368 1.00 19.75 C ANISOU 1662 CD1 ILE A 202 2678 2524 2301 70 107 -53 C ATOM 1663 N TRP A 203 4.288 10.073 29.444 1.00 13.86 N ANISOU 1663 N TRP A 203 1787 1762 1715 109 79 -31 N ATOM 1664 CA TRP A 203 5.355 10.403 30.370 1.00 13.88 C ANISOU 1664 CA TRP A 203 1789 1854 1629 63 34 -34 C ATOM 1665 C TRP A 203 4.964 10.112 31.808 1.00 13.81 C ANISOU 1665 C TRP A 203 1726 1680 1841 28 -12 10 C ATOM 1666 O TRP A 203 5.843 9.879 32.624 1.00 14.19 O ANISOU 1666 O TRP A 203 1780 1840 1769 12 5 142 O ATOM 1667 CB TRP A 203 5.828 11.842 30.165 1.00 14.18 C ANISOU 1667 CB TRP A 203 1948 1724 1716 31 57 1 C ATOM 1668 CG TRP A 203 6.526 11.972 28.833 1.00 13.55 C ANISOU 1668 CG TRP A 203 1788 1635 1725 4 -58 38 C ATOM 1669 CD1 TRP A 203 6.041 12.553 27.714 1.00 14.36 C ANISOU 1669 CD1 TRP A 203 1820 1790 1844 84 123 41 C ATOM 1670 CD2 TRP A 203 7.801 11.418 28.473 1.00 12.92 C ANISOU 1670 CD2 TRP A 203 1752 1447 1709 -47 21 188 C ATOM 1671 NE1 TRP A 203 6.938 12.416 26.680 1.00 14.05 N ANISOU 1671 NE1 TRP A 203 1791 1682 1863 18 112 122 N ATOM 1672 CE2 TRP A 203 8.019 11.718 27.123 1.00 13.55 C ANISOU 1672 CE2 TRP A 203 1760 1557 1828 -56 -42 185 C ATOM 1673 CE3 TRP A 203 8.785 10.705 29.172 1.00 14.21 C ANISOU 1673 CE3 TRP A 203 1938 1623 1837 126 97 184 C ATOM 1674 CZ2 TRP A 203 9.169 11.309 26.435 1.00 14.21 C ANISOU 1674 CZ2 TRP A 203 1773 1699 1925 71 76 128 C ATOM 1675 CZ3 TRP A 203 9.918 10.281 28.502 1.00 14.82 C ANISOU 1675 CZ3 TRP A 203 1807 1744 2079 51 -108 67 C ATOM 1676 CH2 TRP A 203 10.100 10.597 27.141 1.00 15.38 C ANISOU 1676 CH2 TRP A 203 1883 1851 2106 2 190 135 C ATOM 1677 N ASP A 204 3.659 10.068 32.119 1.00 13.81 N ANISOU 1677 N ASP A 204 1789 1804 1654 97 50 103 N ATOM 1678 CA ASP A 204 3.215 9.620 33.432 1.00 14.15 C ANISOU 1678 CA ASP A 204 1668 2019 1689 33 0 80 C ATOM 1679 C ASP A 204 3.549 8.112 33.639 1.00 13.97 C ANISOU 1679 C ASP A 204 1595 1989 1723 37 45 162 C ATOM 1680 O ASP A 204 3.950 7.710 34.711 1.00 15.24 O ANISOU 1680 O ASP A 204 1852 2270 1667 37 -63 197 O ATOM 1681 CB ASP A 204 1.698 9.783 33.588 1.00 14.23 C ANISOU 1681 CB ASP A 204 1655 1966 1783 86 -2 157 C ATOM 1682 CG ASP A 204 1.246 11.187 33.870 1.00 15.60 C ANISOU 1682 CG ASP A 204 1926 2179 1822 27 -9 31 C ATOM 1683 OD1 ASP A 204 2.040 12.005 34.400 1.00 16.48 O ANISOU 1683 OD1 ASP A 204 2135 2248 1877 -103 99 -144 O ATOM 1684 OD2 ASP A 204 0.057 11.498 33.618 1.00 17.33 O ANISOU 1684 OD2 ASP A 204 1989 2358 2235 294 52 -53 O ATOM 1685 N ALA A 205 3.371 7.304 32.603 1.00 14.69 N ANISOU 1685 N ALA A 205 1805 1987 1787 62 -70 199 N ATOM 1686 CA ALA A 205 3.765 5.884 32.676 1.00 14.68 C ANISOU 1686 CA ALA A 205 1827 1873 1875 80 14 102 C ATOM 1687 C ALA A 205 5.261 5.766 32.882 1.00 14.73 C ANISOU 1687 C ALA A 205 1777 1626 2192 90 -34 141 C ATOM 1688 O ALA A 205 5.738 4.973 33.681 1.00 15.83 O ANISOU 1688 O ALA A 205 2102 1837 2073 121 111 285 O ATOM 1689 CB ALA A 205 3.327 5.141 31.430 1.00 16.51 C ANISOU 1689 CB ALA A 205 2011 2021 2240 -117 -78 17 C ATOM 1690 N VAL A 206 6.041 6.569 32.157 1.00 13.89 N ANISOU 1690 N VAL A 206 1969 1572 1734 120 -19 52 N ATOM 1691 CA VAL A 206 7.489 6.564 32.343 1.00 14.05 C ANISOU 1691 CA VAL A 206 1817 1561 1958 257 -7 71 C ATOM 1692 C VAL A 206 7.820 6.973 33.761 1.00 13.60 C ANISOU 1692 C VAL A 206 1796 1631 1740 122 -17 93 C ATOM 1693 O VAL A 206 8.656 6.344 34.413 1.00 14.47 O ANISOU 1693 O VAL A 206 1778 1847 1872 213 34 77 O ATOM 1694 CB VAL A 206 8.184 7.502 31.330 1.00 14.28 C ANISOU 1694 CB VAL A 206 1779 1739 1907 181 239 69 C ATOM 1695 CG1 VAL A 206 9.662 7.607 31.621 1.00 14.71 C ANISOU 1695 CG1 VAL A 206 1805 1832 1949 249 142 224 C ATOM 1696 CG2 VAL A 206 7.943 7.007 29.909 1.00 15.03 C ANISOU 1696 CG2 VAL A 206 1900 1669 2141 232 154 13 C ATOM 1697 N ALA A 207 7.173 8.008 34.267 1.00 14.01 N ANISOU 1697 N ALA A 207 1750 1683 1888 163 -31 112 N ATOM 1698 CA ALA A 207 7.427 8.500 35.609 1.00 14.15 C ANISOU 1698 CA ALA A 207 1614 1924 1836 104 5 89 C ATOM 1699 C ALA A 207 7.181 7.432 36.669 1.00 14.79 C ANISOU 1699 C ALA A 207 1655 1923 2039 298 -70 -5 C ATOM 1700 O ALA A 207 8.023 7.192 37.541 1.00 16.40 O ANISOU 1700 O ALA A 207 1898 2052 2280 314 -179 160 O ATOM 1701 CB ALA A 207 6.562 9.742 35.904 1.00 14.44 C ANISOU 1701 CB ALA A 207 1723 1821 1941 97 -206 -50 C ATOM 1702 N ARG A 208 6.044 6.771 36.558 1.00 15.06 N ANISOU 1702 N ARG A 208 1694 2085 1941 91 -129 103 N ATOM 1703 CA ARG A 208 5.689 5.782 37.560 1.00 16.71 C ANISOU 1703 CA ARG A 208 2032 2282 2032 161 44 230 C ATOM 1704 C ARG A 208 6.691 4.644 37.598 1.00 16.35 C ANISOU 1704 C ARG A 208 2061 2193 1955 181 140 265 C ATOM 1705 O ARG A 208 7.040 4.127 38.667 1.00 19.15 O ANISOU 1705 O ARG A 208 2679 2532 2062 521 139 397 O ATOM 1706 CB ARG A 208 4.298 5.229 37.292 1.00 18.48 C ANISOU 1706 CB ARG A 208 2264 2479 2276 74 257 407 C ATOM 1707 CG ARG A 208 3.208 6.176 37.659 1.00 22.29 C ANISOU 1707 CG ARG A 208 2604 2966 2898 247 122 171 C ATOM 1708 CD ARG A 208 1.889 5.497 37.694 1.00 24.16 C ANISOU 1708 CD ARG A 208 2762 3301 3116 25 76 235 C ATOM 1709 NE ARG A 208 1.540 5.070 36.351 1.00 27.62 N ANISOU 1709 NE ARG A 208 3456 3663 3374 57 90 86 N ATOM 1710 CZ ARG A 208 0.878 5.813 35.460 1.00 27.23 C ANISOU 1710 CZ ARG A 208 3182 3635 3527 -38 36 90 C ATOM 1711 NH1 ARG A 208 0.451 7.039 35.757 1.00 30.16 N ANISOU 1711 NH1 ARG A 208 3580 3747 4130 -88 5 90 N ATOM 1712 NH2 ARG A 208 0.627 5.313 34.271 1.00 26.84 N ANISOU 1712 NH2 ARG A 208 2965 3699 3530 -175 150 40 N ATOM 1713 N GLU A 209 7.137 4.216 36.426 1.00 15.63 N ANISOU 1713 N GLU A 209 2017 2038 1881 148 166 239 N ATOM 1714 CA GLU A 209 7.991 3.059 36.325 1.00 16.08 C ANISOU 1714 CA GLU A 209 2019 1947 2141 1 85 180 C ATOM 1715 C GLU A 209 9.446 3.390 36.587 1.00 16.53 C ANISOU 1715 C GLU A 209 1960 1892 2428 211 20 308 C ATOM 1716 O GLU A 209 10.203 2.483 36.875 1.00 19.71 O ANISOU 1716 O GLU A 209 2185 2105 3198 257 -8 340 O ATOM 1717 CB GLU A 209 7.811 2.400 34.973 1.00 17.38 C ANISOU 1717 CB GLU A 209 2147 2099 2355 49 136 62 C ATOM 1718 CG GLU A 209 6.410 1.880 34.761 1.00 20.88 C ANISOU 1718 CG GLU A 209 2452 2567 2911 -225 -91 -155 C ATOM 1719 CD GLU A 209 5.996 0.824 35.748 1.00 28.41 C ANISOU 1719 CD GLU A 209 3665 3720 3407 16 43 124 C ATOM 1720 OE1 GLU A 209 6.859 0.016 36.148 1.00 29.96 O ANISOU 1720 OE1 GLU A 209 4245 3396 3742 104 102 322 O ATOM 1721 OE2 GLU A 209 4.804 0.815 36.121 1.00 35.16 O ANISOU 1721 OE2 GLU A 209 4125 4651 4583 -109 133 51 O ATOM 1722 N THR A 210 9.859 4.651 36.472 1.00 16.33 N ANISOU 1722 N THR A 210 1764 1936 2501 161 41 288 N ATOM 1723 CA THR A 210 11.241 5.042 36.733 1.00 16.63 C ANISOU 1723 CA THR A 210 1840 2066 2410 188 -61 282 C ATOM 1724 C THR A 210 11.446 5.684 38.099 1.00 16.57 C ANISOU 1724 C THR A 210 1843 2101 2351 271 -116 376 C ATOM 1725 O THR A 210 12.572 5.878 38.528 1.00 18.56 O ANISOU 1725 O THR A 210 1920 2641 2491 163 -82 331 O ATOM 1726 CB THR A 210 11.748 6.046 35.701 1.00 16.10 C ANISOU 1726 CB THR A 210 1848 1982 2286 232 50 153 C ATOM 1727 OG1 THR A 210 10.930 7.230 35.747 1.00 14.71 O ANISOU 1727 OG1 THR A 210 1832 1757 1996 150 25 76 O ATOM 1728 CG2 THR A 210 11.718 5.482 34.252 1.00 16.92 C ANISOU 1728 CG2 THR A 210 1847 2018 2562 97 378 23 C ATOM 1729 N GLY A 211 10.371 6.105 38.756 1.00 15.91 N ANISOU 1729 N GLY A 211 1951 2055 2040 130 -40 386 N ATOM 1730 CA GLY A 211 10.503 6.883 39.970 1.00 16.39 C ANISOU 1730 CA GLY A 211 2014 2172 2039 107 -96 353 C ATOM 1731 C GLY A 211 10.872 8.348 39.793 1.00 17.06 C ANISOU 1731 C GLY A 211 2052 2281 2149 58 -199 261 C ATOM 1732 O GLY A 211 11.224 9.015 40.767 1.00 18.11 O ANISOU 1732 O GLY A 211 2492 2343 2045 -137 -139 176 O ATOM 1733 N ILE A 212 10.793 8.861 38.556 1.00 15.02 N ANISOU 1733 N ILE A 212 1779 2077 1851 58 -124 191 N ATOM 1734 CA ILE A 212 11.167 10.227 38.238 1.00 15.24 C ANISOU 1734 CA ILE A 212 1791 1968 2028 15 -100 120 C ATOM 1735 C ILE A 212 9.900 11.002 37.854 1.00 14.37 C ANISOU 1735 C ILE A 212 1676 1845 1936 24 -56 31 C ATOM 1736 O ILE A 212 9.346 10.743 36.781 1.00 14.69 O ANISOU 1736 O ILE A 212 1663 1914 2004 13 -161 42 O ATOM 1737 CB ILE A 212 12.194 10.276 37.070 1.00 14.65 C ANISOU 1737 CB ILE A 212 1788 1848 1928 -19 -105 98 C ATOM 1738 CG1 ILE A 212 13.424 9.431 37.392 1.00 16.64 C ANISOU 1738 CG1 ILE A 212 1976 1980 2365 106 154 59 C ATOM 1739 CG2 ILE A 212 12.563 11.740 36.811 1.00 15.35 C ANISOU 1739 CG2 ILE A 212 1831 2058 1942 -35 0 -38 C ATOM 1740 CD1 ILE A 212 14.274 9.181 36.127 1.00 17.60 C ANISOU 1740 CD1 ILE A 212 2064 2178 2445 156 76 101 C ATOM 1741 N PRO A 213 9.400 11.876 38.733 1.00 13.91 N ANISOU 1741 N PRO A 213 1599 1901 1782 18 -37 61 N ATOM 1742 CA PRO A 213 8.149 12.553 38.410 1.00 14.23 C ANISOU 1742 CA PRO A 213 1759 1761 1885 -3 -24 -14 C ATOM 1743 C PRO A 213 8.221 13.340 37.108 1.00 13.68 C ANISOU 1743 C PRO A 213 1699 1701 1798 -6 59 -117 C ATOM 1744 O PRO A 213 9.291 13.770 36.695 1.00 13.74 O ANISOU 1744 O PRO A 213 1616 1733 1872 16 -12 -20 O ATOM 1745 CB PRO A 213 7.889 13.467 39.618 1.00 14.91 C ANISOU 1745 CB PRO A 213 1698 2053 1911 -12 52 -21 C ATOM 1746 CG PRO A 213 8.567 12.746 40.741 1.00 15.28 C ANISOU 1746 CG PRO A 213 1723 2011 2072 -74 43 -46 C ATOM 1747 CD PRO A 213 9.838 12.146 40.123 1.00 15.17 C ANISOU 1747 CD PRO A 213 1761 2087 1913 12 -137 -77 C ATOM 1748 N PRO A 214 7.063 13.575 36.494 1.00 13.47 N ANISOU 1748 N PRO A 214 1654 1772 1691 -29 -39 -66 N ATOM 1749 CA PRO A 214 7.071 14.255 35.176 1.00 14.01 C ANISOU 1749 CA PRO A 214 1743 1834 1743 -57 -104 -51 C ATOM 1750 C PRO A 214 7.826 15.573 35.077 1.00 13.94 C ANISOU 1750 C PRO A 214 1705 1717 1872 24 -65 -21 C ATOM 1751 O PRO A 214 8.458 15.823 34.054 1.00 14.36 O ANISOU 1751 O PRO A 214 1838 1790 1828 -24 69 -35 O ATOM 1752 CB PRO A 214 5.584 14.438 34.869 1.00 14.44 C ANISOU 1752 CB PRO A 214 1713 1887 1886 7 -65 -32 C ATOM 1753 CG PRO A 214 4.906 13.292 35.607 1.00 14.43 C ANISOU 1753 CG PRO A 214 1683 1738 2060 130 36 -4 C ATOM 1754 CD PRO A 214 5.697 13.165 36.896 1.00 13.62 C ANISOU 1754 CD PRO A 214 1660 1711 1802 56 -63 -43 C ATOM 1755 N LEU A 215 7.727 16.438 36.085 1.00 14.27 N ANISOU 1755 N LEU A 215 1851 1761 1810 -77 -35 -21 N ATOM 1756 CA LEU A 215 8.394 17.706 35.992 1.00 14.46 C ANISOU 1756 CA LEU A 215 1833 1733 1928 54 -27 -53 C ATOM 1757 C LEU A 215 9.903 17.573 36.139 1.00 14.69 C ANISOU 1757 C LEU A 215 1896 1704 1979 -48 -3 13 C ATOM 1758 O LEU A 215 10.631 18.478 35.745 1.00 15.88 O ANISOU 1758 O LEU A 215 1952 1758 2321 -1 -35 99 O ATOM 1759 CB LEU A 215 7.844 18.721 36.986 1.00 15.14 C ANISOU 1759 CB LEU A 215 1850 1729 2173 59 46 -59 C ATOM 1760 CG LEU A 215 6.480 19.320 36.596 1.00 15.84 C ANISOU 1760 CG LEU A 215 2066 1699 2253 95 18 -164 C ATOM 1761 CD1 LEU A 215 5.957 20.227 37.730 1.00 16.69 C ANISOU 1761 CD1 LEU A 215 2055 1795 2492 215 -17 -217 C ATOM 1762 CD2 LEU A 215 6.492 20.045 35.237 1.00 16.88 C ANISOU 1762 CD2 LEU A 215 2106 1846 2462 164 -144 -152 C ATOM 1763 N HIS A 216 10.399 16.432 36.655 1.00 13.83 N ANISOU 1763 N HIS A 216 1743 1712 1797 -45 42 59 N ATOM 1764 CA HIS A 216 11.806 16.104 36.618 1.00 14.15 C ANISOU 1764 CA HIS A 216 1632 1926 1816 -95 33 15 C ATOM 1765 C HIS A 216 12.191 15.400 35.321 1.00 14.38 C ANISOU 1765 C HIS A 216 1794 1813 1854 -66 -77 69 C ATOM 1766 O HIS A 216 13.288 15.622 34.826 1.00 14.43 O ANISOU 1766 O HIS A 216 1648 1921 1911 -76 -12 45 O ATOM 1767 CB HIS A 216 12.140 15.289 37.868 1.00 14.86 C ANISOU 1767 CB HIS A 216 1847 1995 1801 -13 -8 -3 C ATOM 1768 CG HIS A 216 11.915 16.049 39.143 1.00 13.97 C ANISOU 1768 CG HIS A 216 1792 1697 1817 -87 -52 23 C ATOM 1769 ND1 HIS A 216 12.643 17.157 39.513 1.00 15.46 N ANISOU 1769 ND1 HIS A 216 1964 1974 1933 -221 102 -96 N ATOM 1770 CD2 HIS A 216 11.021 15.830 40.140 1.00 14.93 C ANISOU 1770 CD2 HIS A 216 1903 1818 1949 -104 22 -113 C ATOM 1771 CE1 HIS A 216 12.199 17.578 40.692 1.00 15.71 C ANISOU 1771 CE1 HIS A 216 1913 2089 1967 -292 117 -262 C ATOM 1772 NE2 HIS A 216 11.211 16.804 41.090 1.00 15.78 N ANISOU 1772 NE2 HIS A 216 1860 2105 2028 51 28 -105 N ATOM 1773 N LEU A 217 11.310 14.574 34.753 1.00 13.93 N ANISOU 1773 N LEU A 217 1655 1778 1857 -81 27 -141 N ATOM 1774 CA LEU A 217 11.567 14.064 33.411 1.00 14.17 C ANISOU 1774 CA LEU A 217 1742 1816 1825 -42 55 -22 C ATOM 1775 C LEU A 217 11.763 15.230 32.452 1.00 14.67 C ANISOU 1775 C LEU A 217 1813 1862 1899 -79 46 -123 C ATOM 1776 O LEU A 217 12.561 15.142 31.525 1.00 14.74 O ANISOU 1776 O LEU A 217 1933 1825 1841 -219 51 -54 O ATOM 1777 CB LEU A 217 10.432 13.176 32.933 1.00 13.71 C ANISOU 1777 CB LEU A 217 1710 1737 1759 -127 138 -66 C ATOM 1778 CG LEU A 217 10.328 11.818 33.642 1.00 14.11 C ANISOU 1778 CG LEU A 217 1872 1755 1734 9 -100 75 C ATOM 1779 CD1 LEU A 217 9.006 11.174 33.269 1.00 15.25 C ANISOU 1779 CD1 LEU A 217 2007 1804 1983 -162 76 74 C ATOM 1780 CD2 LEU A 217 11.472 10.918 33.325 1.00 16.12 C ANISOU 1780 CD2 LEU A 217 2078 1869 2175 141 0 -98 C ATOM 1781 N ASP A 218 11.062 16.338 32.667 1.00 14.50 N ANISOU 1781 N ASP A 218 1762 1953 1795 -79 109 52 N ATOM 1782 CA ASP A 218 11.204 17.523 31.825 1.00 15.02 C ANISOU 1782 CA ASP A 218 1898 1863 1943 29 0 10 C ATOM 1783 C ASP A 218 12.659 17.964 31.755 1.00 14.00 C ANISOU 1783 C ASP A 218 1770 1830 1718 84 71 116 C ATOM 1784 O ASP A 218 13.149 18.390 30.718 1.00 14.71 O ANISOU 1784 O ASP A 218 1843 1967 1778 21 -85 96 O ATOM 1785 CB ASP A 218 10.340 18.657 32.349 1.00 15.60 C ANISOU 1785 CB ASP A 218 1852 2031 2043 77 52 90 C ATOM 1786 CG ASP A 218 10.453 19.868 31.552 1.00 17.34 C ANISOU 1786 CG ASP A 218 1958 2142 2486 49 29 91 C ATOM 1787 OD1 ASP A 218 9.902 19.863 30.405 1.00 19.82 O ANISOU 1787 OD1 ASP A 218 2108 2614 2806 112 -107 494 O ATOM 1788 OD2 ASP A 218 11.073 20.828 32.017 1.00 20.71 O ANISOU 1788 OD2 ASP A 218 3150 2017 2702 -30 317 -131 O ATOM 1789 N THR A 219 13.381 17.876 32.874 1.00 14.45 N ANISOU 1789 N THR A 219 1872 1843 1772 -90 -12 -64 N ATOM 1790 CA THR A 219 14.810 18.232 32.906 1.00 14.48 C ANISOU 1790 CA THR A 219 1768 1745 1986 -157 -40 -61 C ATOM 1791 C THR A 219 15.605 17.358 31.965 1.00 13.88 C ANISOU 1791 C THR A 219 1645 1815 1814 -96 -111 -55 C ATOM 1792 O THR A 219 16.503 17.850 31.247 1.00 15.06 O ANISOU 1792 O THR A 219 1922 2018 1783 -92 44 88 O ATOM 1793 CB THR A 219 15.334 18.088 34.346 1.00 15.30 C ANISOU 1793 CB THR A 219 1922 2026 1863 -161 7 -143 C ATOM 1794 OG1 THR A 219 14.481 18.898 35.169 1.00 16.85 O ANISOU 1794 OG1 THR A 219 2113 2180 2108 -72 65 -252 O ATOM 1795 CG2 THR A 219 16.786 18.459 34.494 1.00 16.91 C ANISOU 1795 CG2 THR A 219 1919 2336 2169 -186 31 -133 C ATOM 1796 N LEU A 220 15.351 16.057 32.017 1.00 14.20 N ANISOU 1796 N LEU A 220 1899 1765 1731 -101 -55 59 N ATOM 1797 CA LEU A 220 16.031 15.136 31.115 1.00 14.25 C ANISOU 1797 CA LEU A 220 1851 1790 1772 -51 9 -3 C ATOM 1798 C LEU A 220 15.704 15.406 29.659 1.00 14.05 C ANISOU 1798 C LEU A 220 1850 1772 1715 25 -8 109 C ATOM 1799 O LEU A 220 16.591 15.307 28.799 1.00 14.57 O ANISOU 1799 O LEU A 220 1880 1942 1713 52 -17 176 O ATOM 1800 CB LEU A 220 15.724 13.700 31.500 1.00 14.90 C ANISOU 1800 CB LEU A 220 1849 1807 2004 -16 66 141 C ATOM 1801 CG LEU A 220 16.076 13.284 32.925 1.00 15.08 C ANISOU 1801 CG LEU A 220 1986 2066 1677 30 157 153 C ATOM 1802 CD1 LEU A 220 15.728 11.849 33.170 1.00 16.54 C ANISOU 1802 CD1 LEU A 220 2187 1893 2202 59 22 205 C ATOM 1803 CD2 LEU A 220 17.578 13.573 33.205 1.00 16.55 C ANISOU 1803 CD2 LEU A 220 2103 2161 2021 29 12 315 C ATOM 1804 N LEU A 221 14.443 15.719 29.352 1.00 14.18 N ANISOU 1804 N LEU A 221 1678 1953 1756 2 24 101 N ATOM 1805 CA LEU A 221 14.092 16.064 27.990 1.00 14.44 C ANISOU 1805 CA LEU A 221 1749 1917 1817 -11 -89 154 C ATOM 1806 C LEU A 221 14.731 17.355 27.519 1.00 14.00 C ANISOU 1806 C LEU A 221 1623 1943 1753 -24 -168 141 C ATOM 1807 O LEU A 221 15.056 17.487 26.337 1.00 14.65 O ANISOU 1807 O LEU A 221 1778 2077 1708 -113 -121 186 O ATOM 1808 CB LEU A 221 12.591 16.098 27.783 1.00 14.27 C ANISOU 1808 CB LEU A 221 1639 1922 1858 -174 90 64 C ATOM 1809 CG ALEU A 221 11.831 14.850 28.075 0.50 15.19 C ANISOU 1809 CG ALEU A 221 1766 2055 1948 -88 -57 199 C ATOM 1810 CG BLEU A 221 11.949 14.744 27.386 0.50 15.33 C ANISOU 1810 CG BLEU A 221 1829 2053 1943 -23 129 111 C ATOM 1811 CD1ALEU A 221 10.360 15.101 27.714 0.50 15.87 C ANISOU 1811 CD1ALEU A 221 1823 2154 2051 -35 97 116 C ATOM 1812 CD1BLEU A 221 11.983 13.696 28.459 0.50 15.25 C ANISOU 1812 CD1BLEU A 221 2053 1916 1826 22 -312 5 C ATOM 1813 CD2ALEU A 221 12.462 13.727 27.308 0.50 17.16 C ANISOU 1813 CD2ALEU A 221 2035 2015 2470 -181 4 -128 C ATOM 1814 CD2BLEU A 221 10.514 14.940 26.897 0.50 14.60 C ANISOU 1814 CD2BLEU A 221 1858 1786 1901 -47 -17 14 C ATOM 1815 N TRP A 222 14.928 18.318 28.411 1.00 14.52 N ANISOU 1815 N TRP A 222 1779 1893 1841 75 25 77 N ATOM 1816 CA TRP A 222 15.641 19.520 28.014 1.00 14.52 C ANISOU 1816 CA TRP A 222 1780 1823 1912 86 -125 140 C ATOM 1817 C TRP A 222 17.041 19.152 27.558 1.00 13.68 C ANISOU 1817 C TRP A 222 1674 1679 1844 -22 -107 88 C ATOM 1818 O TRP A 222 17.491 19.565 26.473 1.00 14.56 O ANISOU 1818 O TRP A 222 1672 1987 1873 83 -143 274 O ATOM 1819 CB TRP A 222 15.663 20.561 29.175 1.00 16.86 C ANISOU 1819 CB TRP A 222 2201 1892 2312 104 105 -97 C ATOM 1820 CG ATRP A 222 16.256 21.867 28.587 0.50 15.30 C ANISOU 1820 CG ATRP A 222 2216 1560 2037 176 -117 -117 C ATOM 1821 CG BTRP A 222 16.940 21.361 29.255 0.50 16.25 C ANISOU 1821 CG BTRP A 222 2229 2004 1941 191 -9 -120 C ATOM 1822 CD1ATRP A 222 15.624 22.782 27.762 0.50 18.24 C ANISOU 1822 CD1ATRP A 222 2484 2053 2393 70 -59 -76 C ATOM 1823 CD1BTRP A 222 17.406 22.197 28.292 0.50 16.04 C ANISOU 1823 CD1BTRP A 222 2088 1841 2163 61 4 46 C ATOM 1824 CD2ATRP A 222 17.593 22.343 28.724 0.50 17.24 C ANISOU 1824 CD2ATRP A 222 2073 2130 2347 114 41 -103 C ATOM 1825 CD2BTRP A 222 17.961 21.341 30.302 0.50 16.81 C ANISOU 1825 CD2BTRP A 222 2050 1953 2384 46 -64 -99 C ATOM 1826 NE1ATRP A 222 16.489 23.791 27.406 0.50 18.90 N ANISOU 1826 NE1ATRP A 222 2592 2190 2399 252 -85 -19 N ATOM 1827 NE1BTRP A 222 18.615 22.734 28.663 0.50 16.53 N ANISOU 1827 NE1BTRP A 222 2453 1698 2127 -137 15 -88 N ATOM 1828 CE2ATRP A 222 17.708 23.538 27.972 0.50 17.52 C ANISOU 1828 CE2ATRP A 222 2117 1867 2671 -8 -109 -92 C ATOM 1829 CE2BTRP A 222 18.991 22.218 29.875 0.50 16.91 C ANISOU 1829 CE2BTRP A 222 2414 1857 2151 -129 65 -106 C ATOM 1830 CE3ATRP A 222 18.718 21.887 29.411 0.50 18.20 C ANISOU 1830 CE3ATRP A 222 2604 1916 2392 93 -128 -13 C ATOM 1831 CE3BTRP A 222 18.088 20.702 31.568 0.50 16.26 C ANISOU 1831 CE3BTRP A 222 2305 1329 2543 241 -178 -392 C ATOM 1832 CZ2ATRP A 222 18.888 24.271 27.915 0.50 17.81 C ANISOU 1832 CZ2ATRP A 222 2430 1750 2587 100 -134 -134 C ATOM 1833 CZ2BTRP A 222 20.131 22.461 30.623 0.50 16.52 C ANISOU 1833 CZ2BTRP A 222 2304 1945 2025 -15 58 -142 C ATOM 1834 CZ3ATRP A 222 19.884 22.620 29.340 0.50 18.79 C ANISOU 1834 CZ3ATRP A 222 2413 2293 2434 30 -51 -87 C ATOM 1835 CZ3BTRP A 222 19.255 20.944 32.292 0.50 17.89 C ANISOU 1835 CZ3BTRP A 222 2540 1984 2270 103 52 124 C ATOM 1836 CH2ATRP A 222 19.960 23.794 28.605 0.50 18.06 C ANISOU 1836 CH2ATRP A 222 2486 1973 2400 8 -110 -190 C ATOM 1837 CH2BTRP A 222 20.246 21.823 31.814 0.50 16.62 C ANISOU 1837 CH2BTRP A 222 2204 1958 2152 -20 -119 -95 C ATOM 1838 N LEU A 223 17.764 18.376 28.370 1.00 13.42 N ANISOU 1838 N LEU A 223 1541 1698 1858 36 -149 265 N ATOM 1839 CA LEU A 223 19.151 18.014 28.010 1.00 13.52 C ANISOU 1839 CA LEU A 223 1640 1675 1821 5 -184 209 C ATOM 1840 C LEU A 223 19.204 17.162 26.758 1.00 13.78 C ANISOU 1840 C LEU A 223 1654 1685 1896 13 -128 184 C ATOM 1841 O LEU A 223 20.041 17.372 25.859 1.00 13.28 O ANISOU 1841 O LEU A 223 1513 1806 1726 -48 -138 274 O ATOM 1842 CB LEU A 223 19.785 17.269 29.190 1.00 14.25 C ANISOU 1842 CB LEU A 223 1946 1732 1735 72 -206 251 C ATOM 1843 CG LEU A 223 20.106 18.183 30.349 1.00 15.05 C ANISOU 1843 CG LEU A 223 1945 1924 1847 57 -251 -102 C ATOM 1844 CD1 LEU A 223 20.267 17.391 31.640 1.00 16.41 C ANISOU 1844 CD1 LEU A 223 2158 2367 1707 132 -533 -8 C ATOM 1845 CD2 LEU A 223 21.352 19.051 30.078 1.00 18.33 C ANISOU 1845 CD2 LEU A 223 2324 2237 2401 -229 -519 159 C ATOM 1846 N ALA A 224 18.313 16.195 26.653 1.00 14.14 N ANISOU 1846 N ALA A 224 1784 1938 1649 -121 0 99 N ATOM 1847 CA ALA A 224 18.308 15.337 25.477 1.00 15.16 C ANISOU 1847 CA ALA A 224 1989 1897 1874 -83 -29 68 C ATOM 1848 C ALA A 224 17.974 16.139 24.240 1.00 13.88 C ANISOU 1848 C ALA A 224 1873 1760 1642 -110 -82 -85 C ATOM 1849 O ALA A 224 18.569 15.928 23.200 1.00 15.26 O ANISOU 1849 O ALA A 224 2106 1969 1722 -203 -9 28 O ATOM 1850 CB ALA A 224 17.300 14.230 25.641 1.00 15.16 C ANISOU 1850 CB ALA A 224 2177 1884 1698 -225 74 31 C ATOM 1851 N GLY A 225 17.037 17.060 24.336 1.00 14.32 N ANISOU 1851 N GLY A 225 1708 1907 1825 -137 -210 130 N ATOM 1852 CA GLY A 225 16.659 17.897 23.238 1.00 14.47 C ANISOU 1852 CA GLY A 225 1623 1985 1887 -143 -232 122 C ATOM 1853 C GLY A 225 17.774 18.786 22.749 1.00 13.32 C ANISOU 1853 C GLY A 225 1508 1840 1711 45 -342 147 C ATOM 1854 O GLY A 225 17.961 18.940 21.530 1.00 13.58 O ANISOU 1854 O GLY A 225 1483 1960 1715 200 -435 213 O ATOM 1855 N ARG A 226 18.556 19.338 23.666 1.00 13.12 N ANISOU 1855 N ARG A 226 1568 1852 1564 28 -281 134 N ATOM 1856 CA ARG A 226 19.674 20.170 23.280 1.00 12.40 C ANISOU 1856 CA ARG A 226 1441 1642 1626 186 -363 153 C ATOM 1857 C ARG A 226 20.614 19.340 22.430 1.00 12.18 C ANISOU 1857 C ARG A 226 1459 1600 1566 159 -477 295 C ATOM 1858 O ARG A 226 21.122 19.829 21.400 1.00 12.03 O ANISOU 1858 O ARG A 226 1376 1733 1462 211 -468 413 O ATOM 1859 CB ARG A 226 20.413 20.767 24.455 1.00 13.65 C ANISOU 1859 CB ARG A 226 1884 1578 1724 24 -354 159 C ATOM 1860 CG ARG A 226 19.627 21.771 25.251 1.00 15.81 C ANISOU 1860 CG ARG A 226 2015 1887 2104 -128 -167 90 C ATOM 1861 CD ARG A 226 18.952 22.820 24.434 1.00 16.65 C ANISOU 1861 CD ARG A 226 1992 1936 2397 169 -74 -104 C ATOM 1862 NE ARG A 226 19.895 23.559 23.624 1.00 16.63 N ANISOU 1862 NE ARG A 226 2073 1800 2442 267 -192 94 N ATOM 1863 CZ ARG A 226 19.525 24.490 22.753 1.00 17.09 C ANISOU 1863 CZ ARG A 226 2150 1860 2482 76 -277 69 C ATOM 1864 NH1 ARG A 226 18.238 24.773 22.585 1.00 18.55 N ANISOU 1864 NH1 ARG A 226 2424 2047 2576 75 -515 2 N ATOM 1865 NH2 ARG A 226 20.448 25.129 22.040 1.00 19.83 N ANISOU 1865 NH2 ARG A 226 2763 1878 2891 1 -210 228 N ATOM 1866 N ALA A 227 20.884 18.096 22.822 1.00 12.33 N ANISOU 1866 N ALA A 227 1537 1614 1534 228 -318 336 N ATOM 1867 CA ALA A 227 21.785 17.240 22.065 1.00 12.25 C ANISOU 1867 CA ALA A 227 1563 1488 1604 192 -309 303 C ATOM 1868 C ALA A 227 21.230 16.800 20.711 1.00 12.06 C ANISOU 1868 C ALA A 227 1505 1565 1511 110 -386 285 C ATOM 1869 O ALA A 227 21.874 16.971 19.680 1.00 13.36 O ANISOU 1869 O ALA A 227 1533 1924 1619 111 -333 247 O ATOM 1870 CB ALA A 227 22.174 16.005 22.879 1.00 12.91 C ANISOU 1870 CB ALA A 227 1621 1608 1675 220 -474 302 C ATOM 1871 N VAL A 228 20.014 16.283 20.739 1.00 11.61 N ANISOU 1871 N VAL A 228 1380 1496 1533 81 -381 159 N ATOM 1872 CA VAL A 228 19.461 15.635 19.571 1.00 12.17 C ANISOU 1872 CA VAL A 228 1462 1460 1701 93 -481 119 C ATOM 1873 C VAL A 228 18.919 16.638 18.558 1.00 12.06 C ANISOU 1873 C VAL A 228 1282 1526 1773 198 -501 104 C ATOM 1874 O VAL A 228 19.156 16.493 17.356 1.00 15.07 O ANISOU 1874 O VAL A 228 1801 2270 1653 490 -503 -79 O ATOM 1875 CB VAL A 228 18.343 14.660 19.935 1.00 15.39 C ANISOU 1875 CB VAL A 228 2063 1559 2223 1 -488 278 C ATOM 1876 CG1 VAL A 228 17.620 14.157 18.672 1.00 17.74 C ANISOU 1876 CG1 VAL A 228 2026 2065 2648 -36 -516 142 C ATOM 1877 CG2 VAL A 228 18.893 13.563 20.774 1.00 17.14 C ANISOU 1877 CG2 VAL A 228 2226 1811 2475 -167 -637 239 C ATOM 1878 N LEU A 229 18.169 17.630 18.986 1.00 11.56 N ANISOU 1878 N LEU A 229 1298 1507 1586 266 -450 133 N ATOM 1879 CA LEU A 229 17.557 18.562 18.065 1.00 11.60 C ANISOU 1879 CA LEU A 229 1243 1511 1654 114 -574 149 C ATOM 1880 C LEU A 229 18.535 19.631 17.665 1.00 11.33 C ANISOU 1880 C LEU A 229 1193 1469 1641 205 -644 286 C ATOM 1881 O LEU A 229 18.595 20.029 16.506 1.00 11.99 O ANISOU 1881 O LEU A 229 1366 1500 1690 135 -752 290 O ATOM 1882 CB LEU A 229 16.285 19.179 18.666 1.00 12.94 C ANISOU 1882 CB LEU A 229 1210 1777 1928 111 -469 345 C ATOM 1883 CG LEU A 229 15.171 18.198 19.024 1.00 16.18 C ANISOU 1883 CG LEU A 229 1715 2120 2310 92 -157 279 C ATOM 1884 CD1 LEU A 229 14.025 18.949 19.712 1.00 17.75 C ANISOU 1884 CD1 LEU A 229 1609 2371 2763 -3 -163 208 C ATOM 1885 CD2 LEU A 229 14.737 17.403 17.772 1.00 18.85 C ANISOU 1885 CD2 LEU A 229 2052 2284 2826 -189 -402 205 C ATOM 1886 N TYR A 230 19.350 20.122 18.614 1.00 11.75 N ANISOU 1886 N TYR A 230 1145 1522 1796 147 -677 265 N ATOM 1887 CA TYR A 230 20.126 21.335 18.411 1.00 12.02 C ANISOU 1887 CA TYR A 230 1265 1613 1688 88 -786 357 C ATOM 1888 C TYR A 230 21.617 21.114 18.294 1.00 11.97 C ANISOU 1888 C TYR A 230 1264 1612 1668 -25 -697 334 C ATOM 1889 O TYR A 230 22.334 22.022 17.943 1.00 13.81 O ANISOU 1889 O TYR A 230 1316 1883 2047 -13 -1126 612 O ATOM 1890 CB TYR A 230 19.807 22.392 19.494 1.00 13.31 C ANISOU 1890 CB TYR A 230 1476 1748 1831 95 -720 273 C ATOM 1891 CG TYR A 230 18.345 22.747 19.581 1.00 13.45 C ANISOU 1891 CG TYR A 230 1459 1606 2046 127 -711 42 C ATOM 1892 CD1 TYR A 230 17.786 23.658 18.724 1.00 14.04 C ANISOU 1892 CD1 TYR A 230 1395 1827 2110 339 -607 371 C ATOM 1893 CD2 TYR A 230 17.516 22.134 20.520 1.00 16.03 C ANISOU 1893 CD2 TYR A 230 1709 1938 2440 184 -473 285 C ATOM 1894 CE1 TYR A 230 16.432 23.960 18.826 1.00 15.52 C ANISOU 1894 CE1 TYR A 230 1656 2156 2083 552 -477 -18 C ATOM 1895 CE2 TYR A 230 16.155 22.411 20.605 1.00 17.49 C ANISOU 1895 CE2 TYR A 230 1816 2216 2612 160 -166 191 C ATOM 1896 CZ TYR A 230 15.613 23.328 19.751 1.00 16.30 C ANISOU 1896 CZ TYR A 230 1472 2229 2493 256 -409 -196 C ATOM 1897 OH TYR A 230 14.262 23.625 19.865 1.00 19.42 O ANISOU 1897 OH TYR A 230 1612 2608 3158 384 -322 -147 O ATOM 1898 N GLY A 231 22.085 19.890 18.556 1.00 12.44 N ANISOU 1898 N GLY A 231 1375 1774 1577 108 -535 425 N ATOM 1899 CA GLY A 231 23.487 19.557 18.418 1.00 13.59 C ANISOU 1899 CA GLY A 231 1518 1951 1694 197 -482 261 C ATOM 1900 C GLY A 231 24.390 20.112 19.520 1.00 14.38 C ANISOU 1900 C GLY A 231 1476 2162 1825 211 -564 370 C ATOM 1901 O GLY A 231 25.595 20.247 19.312 1.00 18.04 O ANISOU 1901 O GLY A 231 1380 3120 2352 31 -534 427 O ATOM 1902 N GLU A 232 23.824 20.413 20.679 1.00 13.73 N ANISOU 1902 N GLU A 232 1523 2097 1597 96 -577 405 N ATOM 1903 CA GLU A 232 24.542 20.948 21.852 1.00 14.41 C ANISOU 1903 CA GLU A 232 1709 2086 1680 -26 -530 376 C ATOM 1904 C GLU A 232 24.584 19.838 22.889 1.00 14.19 C ANISOU 1904 C GLU A 232 1719 2127 1542 148 -457 348 C ATOM 1905 O GLU A 232 23.605 19.639 23.604 1.00 14.39 O ANISOU 1905 O GLU A 232 1638 2229 1600 77 -527 428 O ATOM 1906 CB GLU A 232 23.823 22.196 22.419 1.00 15.26 C ANISOU 1906 CB GLU A 232 1982 1954 1859 -44 -647 407 C ATOM 1907 CG GLU A 232 24.523 22.825 23.622 1.00 17.33 C ANISOU 1907 CG GLU A 232 2162 2440 1980 106 -640 310 C ATOM 1908 CD GLU A 232 23.833 24.048 24.195 1.00 20.59 C ANISOU 1908 CD GLU A 232 2465 2559 2798 46 -562 9 C ATOM 1909 OE1 GLU A 232 22.603 24.160 24.117 1.00 24.08 O ANISOU 1909 OE1 GLU A 232 2469 3026 3652 -160 -414 -153 O ATOM 1910 OE2 GLU A 232 24.559 24.926 24.729 1.00 26.75 O ANISOU 1910 OE2 GLU A 232 2925 2819 4417 -128 -795 -328 O ATOM 1911 N ASN A 233 25.684 19.102 22.967 1.00 15.19 N ANISOU 1911 N ASN A 233 2109 2181 1480 163 -193 432 N ATOM 1912 CA ASN A 233 25.816 18.026 23.929 1.00 15.23 C ANISOU 1912 CA ASN A 233 2158 2071 1555 113 -460 260 C ATOM 1913 C ASN A 233 26.504 18.552 25.184 1.00 13.22 C ANISOU 1913 C ASN A 233 1957 1839 1226 38 -322 254 C ATOM 1914 O ASN A 233 27.700 18.789 25.208 1.00 16.46 O ANISOU 1914 O ASN A 233 2160 2587 1505 -138 -199 193 O ATOM 1915 CB ASN A 233 26.546 16.827 23.353 1.00 17.58 C ANISOU 1915 CB ASN A 233 2601 2239 1837 113 -472 153 C ATOM 1916 CG ASN A 233 26.482 15.589 24.267 1.00 17.20 C ANISOU 1916 CG ASN A 233 2509 2144 1882 79 -401 50 C ATOM 1917 OD1 ASN A 233 25.882 15.610 25.379 1.00 16.58 O ANISOU 1917 OD1 ASN A 233 2702 1819 1775 -41 -696 82 O ATOM 1918 ND2 ASN A 233 27.106 14.515 23.816 1.00 20.70 N ANISOU 1918 ND2 ASN A 233 2779 2319 2767 -34 -439 46 N ATOM 1919 N LEU A 234 25.716 18.714 26.218 1.00 12.90 N ANISOU 1919 N LEU A 234 1841 1605 1453 -122 -434 358 N ATOM 1920 CA LEU A 234 26.179 19.247 27.473 1.00 12.82 C ANISOU 1920 CA LEU A 234 2012 1551 1305 -139 -378 206 C ATOM 1921 C LEU A 234 26.743 18.174 28.400 1.00 11.53 C ANISOU 1921 C LEU A 234 1689 1409 1281 -217 -253 172 C ATOM 1922 O LEU A 234 27.268 18.495 29.468 1.00 12.36 O ANISOU 1922 O LEU A 234 1808 1586 1300 -203 -357 139 O ATOM 1923 CB LEU A 234 25.033 20.016 28.135 1.00 14.33 C ANISOU 1923 CB LEU A 234 2160 1610 1672 114 -329 376 C ATOM 1924 CG LEU A 234 24.580 21.260 27.376 1.00 15.26 C ANISOU 1924 CG LEU A 234 2174 1937 1685 135 -375 248 C ATOM 1925 CD1 LEU A 234 23.216 21.698 27.893 1.00 18.11 C ANISOU 1925 CD1 LEU A 234 2563 1975 2342 210 -287 259 C ATOM 1926 CD2 LEU A 234 25.596 22.303 27.480 1.00 18.59 C ANISOU 1926 CD2 LEU A 234 2568 2148 2347 -117 -350 381 C ATOM 1927 N HIS A 235 26.587 16.906 28.031 1.00 11.23 N ANISOU 1927 N HIS A 235 1698 1510 1059 -146 -371 223 N ATOM 1928 CA HIS A 235 26.995 15.782 28.849 1.00 11.79 C ANISOU 1928 CA HIS A 235 1713 1500 1266 -58 -284 104 C ATOM 1929 C HIS A 235 26.275 15.738 30.193 1.00 12.18 C ANISOU 1929 C HIS A 235 1872 1458 1295 -195 -125 296 C ATOM 1930 O HIS A 235 26.775 15.173 31.167 1.00 14.37 O ANISOU 1930 O HIS A 235 2331 1834 1294 -119 -177 550 O ATOM 1931 CB HIS A 235 28.501 15.703 29.029 1.00 12.08 C ANISOU 1931 CB HIS A 235 1774 1654 1159 8 -283 135 C ATOM 1932 CG HIS A 235 29.213 15.363 27.771 1.00 13.28 C ANISOU 1932 CG HIS A 235 1995 1704 1345 -9 -374 65 C ATOM 1933 ND1 HIS A 235 29.541 14.078 27.430 1.00 18.98 N ANISOU 1933 ND1 HIS A 235 3099 2257 1853 425 -141 -63 N ATOM 1934 CD2 HIS A 235 29.599 16.143 26.740 1.00 16.90 C ANISOU 1934 CD2 HIS A 235 2623 1970 1826 -521 123 -115 C ATOM 1935 CE1 HIS A 235 30.133 14.084 26.249 1.00 17.96 C ANISOU 1935 CE1 HIS A 235 2419 2389 2013 353 -64 -123 C ATOM 1936 NE2 HIS A 235 30.199 15.327 25.816 1.00 16.23 N ANISOU 1936 NE2 HIS A 235 2086 2478 1601 -471 -62 -350 N ATOM 1937 N GLY A 236 25.037 16.209 30.203 1.00 12.98 N ANISOU 1937 N GLY A 236 1878 1591 1463 -237 -73 92 N ATOM 1938 CA GLY A 236 24.162 16.017 31.361 1.00 15.02 C ANISOU 1938 CA GLY A 236 2250 1743 1713 -223 168 -19 C ATOM 1939 C GLY A 236 23.454 14.682 31.366 1.00 16.46 C ANISOU 1939 C GLY A 236 2627 1841 1784 -410 280 44 C ATOM 1940 O GLY A 236 23.191 14.132 32.436 1.00 20.61 O ANISOU 1940 O GLY A 236 3616 2104 2110 -573 487 122 O ATOM 1941 N VAL A 237 23.104 14.174 30.186 1.00 16.08 N ANISOU 1941 N VAL A 237 2443 1749 1915 -443 321 -67 N ATOM 1942 CA VAL A 237 22.587 12.830 30.033 1.00 16.69 C ANISOU 1942 CA VAL A 237 2324 1777 2240 -343 162 -102 C ATOM 1943 C VAL A 237 23.559 12.037 29.216 1.00 16.35 C ANISOU 1943 C VAL A 237 2123 1843 2245 -254 95 -273 C ATOM 1944 O VAL A 237 24.248 12.572 28.353 1.00 18.01 O ANISOU 1944 O VAL A 237 2078 2436 2329 -535 264 -428 O ATOM 1945 CB VAL A 237 21.151 12.794 29.423 1.00 16.94 C ANISOU 1945 CB VAL A 237 2282 1644 2508 -278 110 -81 C ATOM 1946 CG1 VAL A 237 20.158 13.436 30.367 1.00 18.26 C ANISOU 1946 CG1 VAL A 237 2214 2126 2596 44 244 47 C ATOM 1947 CG2 VAL A 237 21.079 13.452 28.042 1.00 17.95 C ANISOU 1947 CG2 VAL A 237 2116 2181 2523 -471 -26 -364 C ATOM 1948 N PRO A 238 23.635 10.753 29.480 1.00 17.25 N ANISOU 1948 N PRO A 238 2154 1996 2402 -110 18 -240 N ATOM 1949 CA PRO A 238 24.604 9.910 28.798 1.00 18.28 C ANISOU 1949 CA PRO A 238 2422 2149 2375 167 -89 -128 C ATOM 1950 C PRO A 238 24.177 9.518 27.406 1.00 15.91 C ANISOU 1950 C PRO A 238 2062 1791 2191 69 -76 -96 C ATOM 1951 O PRO A 238 23.017 9.695 27.025 1.00 15.20 O ANISOU 1951 O PRO A 238 1850 1630 2293 9 -245 105 O ATOM 1952 CB PRO A 238 24.651 8.679 29.688 1.00 20.19 C ANISOU 1952 CB PRO A 238 2741 2265 2665 208 -187 -103 C ATOM 1953 CG PRO A 238 23.300 8.576 30.275 1.00 21.31 C ANISOU 1953 CG PRO A 238 3053 2232 2811 -58 -87 238 C ATOM 1954 CD PRO A 238 22.873 10.001 30.493 1.00 18.79 C ANISOU 1954 CD PRO A 238 2767 1970 2399 -72 -106 -106 C ATOM 1955 N LYS A 239 25.108 8.927 26.676 1.00 15.73 N ANISOU 1955 N LYS A 239 1893 1965 2118 114 -187 -91 N ATOM 1956 CA LYS A 239 24.922 8.634 25.292 1.00 14.96 C ANISOU 1956 CA LYS A 239 1830 1691 2162 21 -219 48 C ATOM 1957 C LYS A 239 23.668 7.780 25.066 1.00 14.18 C ANISOU 1957 C LYS A 239 1798 1668 1920 -30 -209 164 C ATOM 1958 O LYS A 239 22.949 7.986 24.081 1.00 14.51 O ANISOU 1958 O LYS A 239 1743 1908 1860 -69 -255 491 O ATOM 1959 CB LYS A 239 26.160 7.979 24.724 1.00 16.63 C ANISOU 1959 CB LYS A 239 1729 2204 2385 -113 -235 -22 C ATOM 1960 CG LYS A 239 26.501 6.586 25.320 1.00 19.04 C ANISOU 1960 CG LYS A 239 2180 2308 2744 338 -285 -336 C ATOM 1961 CD LYS A 239 27.840 6.110 24.885 1.00 19.35 C ANISOU 1961 CD LYS A 239 2229 2323 2799 70 -274 -102 C ATOM 1962 CE LYS A 239 28.089 4.651 25.312 1.00 21.44 C ANISOU 1962 CE LYS A 239 2342 2629 3172 237 -203 -44 C ATOM 1963 NZ LYS A 239 28.421 4.487 26.755 1.00 25.93 N ANISOU 1963 NZ LYS A 239 3332 3113 3406 -346 31 164 N ATOM 1964 N GLU A 240 23.407 6.835 25.955 1.00 13.47 N ANISOU 1964 N GLU A 240 1710 1601 1806 27 -359 161 N ATOM 1965 CA GLU A 240 22.258 5.943 25.740 1.00 13.51 C ANISOU 1965 CA GLU A 240 1850 1536 1746 21 -309 262 C ATOM 1966 C GLU A 240 20.907 6.641 25.887 1.00 13.61 C ANISOU 1966 C GLU A 240 1929 1516 1724 -121 -348 358 C ATOM 1967 O GLU A 240 19.923 6.203 25.317 1.00 14.65 O ANISOU 1967 O GLU A 240 1829 1715 2022 -237 -357 199 O ATOM 1968 CB GLU A 240 22.339 4.710 26.666 1.00 15.10 C ANISOU 1968 CB GLU A 240 2096 1725 1914 137 -453 411 C ATOM 1969 CG GLU A 240 22.107 4.937 28.137 1.00 16.69 C ANISOU 1969 CG GLU A 240 2430 1817 2095 -141 -239 437 C ATOM 1970 CD GLU A 240 23.372 5.253 28.875 1.00 19.18 C ANISOU 1970 CD GLU A 240 2779 2066 2441 -166 -233 119 C ATOM 1971 OE1 GLU A 240 24.417 5.610 28.260 1.00 17.92 O ANISOU 1971 OE1 GLU A 240 2555 1926 2328 -16 -698 345 O ATOM 1972 OE2 GLU A 240 23.326 5.175 30.121 1.00 20.82 O ANISOU 1972 OE2 GLU A 240 3506 2152 2250 -258 -105 185 O ATOM 1973 N VAL A 241 20.874 7.697 26.681 1.00 12.73 N ANISOU 1973 N VAL A 241 1694 1544 1597 -187 -271 231 N ATOM 1974 CA VAL A 241 19.672 8.488 26.825 1.00 13.74 C ANISOU 1974 CA VAL A 241 1808 1561 1849 -80 -192 239 C ATOM 1975 C VAL A 241 19.427 9.330 25.572 1.00 13.63 C ANISOU 1975 C VAL A 241 1767 1592 1817 -129 -287 206 C ATOM 1976 O VAL A 241 18.329 9.398 25.042 1.00 15.00 O ANISOU 1976 O VAL A 241 1627 1935 2134 -69 -317 302 O ATOM 1977 CB VAL A 241 19.698 9.334 28.098 1.00 14.94 C ANISOU 1977 CB VAL A 241 1839 1865 1970 -276 -38 122 C ATOM 1978 CG1 VAL A 241 18.552 10.316 28.130 1.00 15.68 C ANISOU 1978 CG1 VAL A 241 1930 1925 2101 -71 -44 -110 C ATOM 1979 CG2 VAL A 241 19.630 8.434 29.351 1.00 16.50 C ANISOU 1979 CG2 VAL A 241 2032 2210 2027 -61 68 148 C ATOM 1980 N ILE A 242 20.480 9.981 25.099 1.00 13.40 N ANISOU 1980 N ILE A 242 1722 1546 1821 -40 -273 434 N ATOM 1981 CA ILE A 242 20.398 10.704 23.833 1.00 14.32 C ANISOU 1981 CA ILE A 242 1903 1562 1975 -90 -372 429 C ATOM 1982 C ILE A 242 19.884 9.805 22.733 1.00 14.08 C ANISOU 1982 C ILE A 242 1632 1664 2052 -28 -351 472 C ATOM 1983 O ILE A 242 19.002 10.189 21.957 1.00 14.26 O ANISOU 1983 O ILE A 242 1701 1691 2024 -91 -443 527 O ATOM 1984 CB ILE A 242 21.784 11.283 23.476 1.00 14.50 C ANISOU 1984 CB ILE A 242 2078 1689 1741 -204 -360 391 C ATOM 1985 CG1 ILE A 242 22.183 12.372 24.462 1.00 15.15 C ANISOU 1985 CG1 ILE A 242 2138 1635 1980 -140 -343 265 C ATOM 1986 CG2 ILE A 242 21.775 11.827 22.068 1.00 15.92 C ANISOU 1986 CG2 ILE A 242 2066 1937 2044 -160 -330 484 C ATOM 1987 CD1 ILE A 242 23.603 12.748 24.427 1.00 17.02 C ANISOU 1987 CD1 ILE A 242 2237 2061 2166 -230 -538 381 C ATOM 1988 N ALA A 243 20.428 8.598 22.658 1.00 13.44 N ANISOU 1988 N ALA A 243 1626 1629 1850 -84 -431 493 N ATOM 1989 CA ALA A 243 20.081 7.682 21.572 1.00 13.66 C ANISOU 1989 CA ALA A 243 1688 1712 1791 -36 -283 380 C ATOM 1990 C ALA A 243 18.588 7.335 21.582 1.00 12.64 C ANISOU 1990 C ALA A 243 1616 1457 1728 66 -233 244 C ATOM 1991 O ALA A 243 18.040 7.006 20.537 1.00 14.03 O ANISOU 1991 O ALA A 243 1840 1787 1701 25 -339 196 O ATOM 1992 CB ALA A 243 20.918 6.453 21.638 1.00 14.32 C ANISOU 1992 CB ALA A 243 1530 2025 1884 11 -235 198 C ATOM 1993 N LEU A 244 17.927 7.356 22.729 1.00 13.32 N ANISOU 1993 N LEU A 244 1724 1620 1717 -72 -215 396 N ATOM 1994 CA LEU A 244 16.490 7.058 22.773 1.00 12.96 C ANISOU 1994 CA LEU A 244 1637 1491 1796 -136 -231 393 C ATOM 1995 C LEU A 244 15.699 7.909 21.807 1.00 13.56 C ANISOU 1995 C LEU A 244 1537 1613 2002 -106 -150 399 C ATOM 1996 O LEU A 244 14.700 7.481 21.241 1.00 14.95 O ANISOU 1996 O LEU A 244 1678 1669 2332 -106 -472 448 O ATOM 1997 CB LEU A 244 15.917 7.324 24.153 1.00 14.23 C ANISOU 1997 CB LEU A 244 1691 1732 1982 -49 -217 284 C ATOM 1998 CG LEU A 244 16.408 6.388 25.248 1.00 13.62 C ANISOU 1998 CG LEU A 244 1794 1660 1721 51 -85 469 C ATOM 1999 CD1 LEU A 244 15.848 6.930 26.579 1.00 15.05 C ANISOU 1999 CD1 LEU A 244 1844 1942 1932 -117 -239 345 C ATOM 2000 CD2 LEU A 244 15.985 4.927 25.019 1.00 14.83 C ANISOU 2000 CD2 LEU A 244 1997 1601 2035 -4 -110 408 C ATOM 2001 N PHE A 245 16.136 9.154 21.690 1.00 13.37 N ANISOU 2001 N PHE A 245 1553 1576 1949 -138 -242 383 N ATOM 2002 CA PHE A 245 15.407 10.192 20.965 1.00 15.14 C ANISOU 2002 CA PHE A 245 1918 1713 2121 122 -206 462 C ATOM 2003 C PHE A 245 15.862 10.320 19.521 1.00 14.97 C ANISOU 2003 C PHE A 245 1890 1689 2110 134 -218 510 C ATOM 2004 O PHE A 245 15.500 11.260 18.851 1.00 15.89 O ANISOU 2004 O PHE A 245 1867 1789 2381 174 -81 686 O ATOM 2005 CB PHE A 245 15.505 11.537 21.710 1.00 15.23 C ANISOU 2005 CB PHE A 245 1871 1727 2187 66 -140 415 C ATOM 2006 CG PHE A 245 14.917 11.481 23.074 1.00 14.18 C ANISOU 2006 CG PHE A 245 1687 1538 2161 -41 -179 214 C ATOM 2007 CD1 PHE A 245 13.559 11.586 23.234 1.00 14.94 C ANISOU 2007 CD1 PHE A 245 1652 1889 2132 45 -218 322 C ATOM 2008 CD2 PHE A 245 15.707 11.236 24.193 1.00 14.85 C ANISOU 2008 CD2 PHE A 245 1665 1634 2341 23 -216 -10 C ATOM 2009 CE1 PHE A 245 12.993 11.493 24.466 1.00 16.11 C ANISOU 2009 CE1 PHE A 245 1758 1970 2392 -63 -251 286 C ATOM 2010 CE2 PHE A 245 15.140 11.116 25.422 1.00 16.27 C ANISOU 2010 CE2 PHE A 245 2034 1954 2191 -124 -313 160 C ATOM 2011 CZ PHE A 245 13.790 11.255 25.573 1.00 16.94 C ANISOU 2011 CZ PHE A 245 2062 2225 2150 -205 -70 296 C ATOM 2012 N GLN A 246 16.606 9.322 19.051 1.00 14.86 N ANISOU 2012 N GLN A 246 1900 1857 1887 254 -199 451 N ATOM 2013 CA GLN A 246 17.053 9.241 17.679 1.00 16.21 C ANISOU 2013 CA GLN A 246 2101 2045 2012 242 -14 428 C ATOM 2014 C GLN A 246 16.476 8.007 16.978 1.00 16.30 C ANISOU 2014 C GLN A 246 2091 2078 2023 301 -43 303 C ATOM 2015 O GLN A 246 16.996 7.539 15.974 1.00 17.58 O ANISOU 2015 O GLN A 246 2174 2288 2216 237 113 204 O ATOM 2016 CB GLN A 246 18.575 9.292 17.644 1.00 17.66 C ANISOU 2016 CB GLN A 246 2285 2354 2070 208 -20 453 C ATOM 2017 CG GLN A 246 19.077 10.558 18.294 1.00 19.37 C ANISOU 2017 CG GLN A 246 2351 2346 2662 290 -137 344 C ATOM 2018 CD GLN A 246 20.505 10.865 18.077 1.00 22.95 C ANISOU 2018 CD GLN A 246 2536 3028 3154 212 -101 215 C ATOM 2019 OE1 GLN A 246 21.380 10.077 18.442 1.00 27.82 O ANISOU 2019 OE1 GLN A 246 2894 3980 3697 567 -264 472 O ATOM 2020 NE2 GLN A 246 20.766 12.047 17.581 1.00 24.22 N ANISOU 2020 NE2 GLN A 246 2319 3315 3565 156 -51 406 N ATOM 2021 N TRP A 247 15.370 7.490 17.482 1.00 17.55 N ANISOU 2021 N TRP A 247 2204 2086 2377 279 -25 99 N ATOM 2022 CA TRP A 247 14.748 6.319 16.874 1.00 17.88 C ANISOU 2022 CA TRP A 247 2366 2073 2354 189 36 98 C ATOM 2023 C TRP A 247 14.217 6.576 15.472 1.00 17.93 C ANISOU 2023 C TRP A 247 2269 2147 2394 92 72 -25 C ATOM 2024 O TRP A 247 14.450 5.782 14.574 1.00 19.35 O ANISOU 2024 O TRP A 247 2639 2188 2522 219 -8 -55 O ATOM 2025 CB TRP A 247 13.658 5.784 17.782 1.00 19.71 C ANISOU 2025 CB TRP A 247 2755 2238 2495 226 185 53 C ATOM 2026 CG TRP A 247 13.120 4.494 17.402 1.00 21.66 C ANISOU 2026 CG TRP A 247 3008 2419 2801 159 200 -24 C ATOM 2027 CD1 TRP A 247 13.712 3.264 17.560 1.00 24.53 C ANISOU 2027 CD1 TRP A 247 3421 2703 3196 50 -90 10 C ATOM 2028 CD2 TRP A 247 11.849 4.257 16.817 1.00 22.13 C ANISOU 2028 CD2 TRP A 247 3177 2623 2605 -54 126 84 C ATOM 2029 NE1 TRP A 247 12.869 2.286 17.101 1.00 25.85 N ANISOU 2029 NE1 TRP A 247 3421 2863 3536 -27 14 1 N ATOM 2030 CE2 TRP A 247 11.731 2.865 16.611 1.00 23.79 C ANISOU 2030 CE2 TRP A 247 3292 2660 3086 -218 17 -57 C ATOM 2031 CE3 TRP A 247 10.809 5.082 16.393 1.00 23.78 C ANISOU 2031 CE3 TRP A 247 3103 2842 3088 24 144 -260 C ATOM 2032 CZ2 TRP A 247 10.593 2.284 16.057 1.00 26.51 C ANISOU 2032 CZ2 TRP A 247 3287 3259 3527 -71 -52 28 C ATOM 2033 CZ3 TRP A 247 9.675 4.499 15.830 1.00 25.33 C ANISOU 2033 CZ3 TRP A 247 3205 3074 3346 -29 -72 -65 C ATOM 2034 CH2 TRP A 247 9.583 3.119 15.663 1.00 26.03 C ANISOU 2034 CH2 TRP A 247 3289 3163 3438 -33 -35 40 C ATOM 2035 N ARG A 248 13.552 7.707 15.281 1.00 17.68 N ANISOU 2035 N ARG A 248 2211 2140 2363 91 -1 113 N ATOM 2036 CA ARG A 248 13.059 8.058 13.957 1.00 19.18 C ANISOU 2036 CA ARG A 248 2503 2424 2360 55 -24 107 C ATOM 2037 C ARG A 248 14.124 8.757 13.097 1.00 19.54 C ANISOU 2037 C ARG A 248 2547 2605 2272 1 122 52 C ATOM 2038 O ARG A 248 14.909 9.570 13.582 1.00 20.08 O ANISOU 2038 O ARG A 248 2475 2857 2297 -127 196 72 O ATOM 2039 CB ARG A 248 11.781 8.891 14.051 1.00 19.67 C ANISOU 2039 CB ARG A 248 2678 2410 2384 100 16 130 C ATOM 2040 CG ARG A 248 10.627 8.149 14.733 1.00 22.17 C ANISOU 2040 CG ARG A 248 2739 2981 2703 31 -44 56 C ATOM 2041 CD ARG A 248 9.222 8.676 14.399 1.00 24.09 C ANISOU 2041 CD ARG A 248 2892 3243 3015 110 -183 -77 C ATOM 2042 NE ARG A 248 8.224 7.588 14.326 1.00 30.14 N ANISOU 2042 NE ARG A 248 3547 3829 4075 -264 117 72 N ATOM 2043 CZ ARG A 248 7.256 7.362 15.216 1.00 28.83 C ANISOU 2043 CZ ARG A 248 3588 3752 3614 -86 -18 -4 C ATOM 2044 NH1 ARG A 248 7.131 8.131 16.260 1.00 29.31 N ANISOU 2044 NH1 ARG A 248 3573 3646 3917 -15 -6 -65 N ATOM 2045 NH2 ARG A 248 6.407 6.352 15.063 1.00 33.24 N ANISOU 2045 NH2 ARG A 248 4003 4292 4333 -192 83 45 N ATOM 2046 N GLY A 249 14.091 8.435 11.812 1.00 20.37 N ANISOU 2046 N GLY A 249 2682 2621 2436 40 58 46 N ATOM 2047 CA AGLY A 249 15.097 8.874 10.801 0.50 20.77 C ANISOU 2047 CA AGLY A 249 2673 2640 2578 7 40 111 C ATOM 2048 CA BGLY A 249 14.908 9.058 10.805 0.50 19.65 C ANISOU 2048 CA BGLY A 249 2527 2517 2420 15 45 99 C ATOM 2049 C AGLY A 249 15.867 10.202 10.845 0.50 20.55 C ANISOU 2049 C AGLY A 249 2700 2612 2494 32 -1 60 C ATOM 2050 C BGLY A 249 14.642 10.534 10.797 0.50 17.90 C ANISOU 2050 C BGLY A 249 2298 2351 2151 34 29 203 C ATOM 2051 O AGLY A 249 17.103 10.215 10.815 0.50 21.64 O ANISOU 2051 O AGLY A 249 2790 2689 2740 107 5 148 O ATOM 2052 O BGLY A 249 13.503 10.999 10.850 0.50 18.54 O ANISOU 2052 O BGLY A 249 2340 2355 2347 19 -83 235 O ATOM 2053 N AGLY A 250 15.138 11.316 10.881 0.50 20.88 N ANISOU 2053 N AGLY A 250 2664 2659 2607 111 -93 163 N ATOM 2054 N BGLY A 250 15.729 11.276 10.782 0.50 18.76 N ANISOU 2054 N BGLY A 250 2335 2419 2370 128 -42 166 N ATOM 2055 CA GLY A 250 15.680 12.706 10.810 1.00 20.36 C ANISOU 2055 CA GLY A 250 2510 2513 2713 123 -79 327 C ATOM 2056 C GLY A 250 15.815 13.359 12.159 1.00 20.58 C ANISOU 2056 C GLY A 250 2488 2459 2870 200 27 357 C ATOM 2057 O GLY A 250 16.018 14.581 12.252 1.00 23.32 O ANISOU 2057 O GLY A 250 2876 2583 3399 194 -58 713 O ATOM 2058 N CYS A 251 15.673 12.566 13.229 1.00 18.27 N ANISOU 2058 N CYS A 251 2158 2233 2549 277 -136 603 N ATOM 2059 CA CYS A 251 15.876 13.048 14.574 1.00 17.18 C ANISOU 2059 CA CYS A 251 1972 1906 2648 212 29 435 C ATOM 2060 C CYS A 251 17.348 13.012 14.876 1.00 16.69 C ANISOU 2060 C CYS A 251 1798 1860 2684 327 13 734 C ATOM 2061 O CYS A 251 17.842 12.068 15.490 1.00 19.32 O ANISOU 2061 O CYS A 251 1965 2231 3142 532 2 1131 O ATOM 2062 CB CYS A 251 15.077 12.185 15.564 1.00 16.13 C ANISOU 2062 CB CYS A 251 2157 1674 2296 11 81 414 C ATOM 2063 SG CYS A 251 13.307 12.327 15.285 1.00 18.20 S ANISOU 2063 SG CYS A 251 1978 2571 2366 -238 44 334 S ATOM 2064 N ARG A 252 18.040 14.011 14.346 1.00 16.89 N ANISOU 2064 N ARG A 252 1735 1807 2874 354 -155 729 N ATOM 2065 CA ARG A 252 19.487 14.112 14.318 1.00 18.54 C ANISOU 2065 CA ARG A 252 1942 2330 2768 179 -147 430 C ATOM 2066 C ARG A 252 19.779 15.621 14.279 1.00 16.07 C ANISOU 2066 C ARG A 252 1641 2036 2427 331 -216 404 C ATOM 2067 O ARG A 252 19.018 16.373 13.664 1.00 13.83 O ANISOU 2067 O ARG A 252 1348 1665 2241 622 -371 457 O ATOM 2068 CB ARG A 252 20.095 13.480 13.034 1.00 20.82 C ANISOU 2068 CB ARG A 252 2195 2529 3186 276 -52 166 C ATOM 2069 CG ARG A 252 19.709 12.026 12.747 1.00 24.33 C ANISOU 2069 CG ARG A 252 2962 2943 3337 -37 15 140 C ATOM 2070 CD ARG A 252 20.382 11.007 13.665 1.00 26.88 C ANISOU 2070 CD ARG A 252 3304 3222 3686 75 -30 100 C ATOM 2071 NE ARG A 252 20.270 9.638 13.162 1.00 27.64 N ANISOU 2071 NE ARG A 252 3504 3055 3941 85 82 -46 N ATOM 2072 CZ ARG A 252 19.197 8.861 13.287 1.00 28.21 C ANISOU 2072 CZ ARG A 252 3478 3362 3876 117 154 -59 C ATOM 2073 NH1 ARG A 252 18.122 9.298 13.925 1.00 25.79 N ANISOU 2073 NH1 ARG A 252 3086 3324 3388 -33 208 193 N ATOM 2074 NH2 ARG A 252 19.208 7.627 12.783 1.00 29.38 N ANISOU 2074 NH2 ARG A 252 3704 3431 4027 2 28 -119 N ATOM 2075 N PRO A 253 20.883 16.116 14.846 1.00 16.28 N ANISOU 2075 N PRO A 253 1713 2461 2012 328 -387 389 N ATOM 2076 CA PRO A 253 21.225 17.548 14.696 1.00 18.66 C ANISOU 2076 CA PRO A 253 2016 2561 2511 144 -359 93 C ATOM 2077 C PRO A 253 21.609 17.865 13.253 1.00 16.97 C ANISOU 2077 C PRO A 253 1826 2327 2293 128 -366 113 C ATOM 2078 O PRO A 253 22.044 16.944 12.569 1.00 16.50 O ANISOU 2078 O PRO A 253 2024 2030 2214 359 -397 136 O ATOM 2079 CB PRO A 253 22.451 17.755 15.618 1.00 21.89 C ANISOU 2079 CB PRO A 253 2535 2967 2812 68 -485 20 C ATOM 2080 CG PRO A 253 22.740 16.446 16.241 1.00 21.78 C ANISOU 2080 CG PRO A 253 2506 2945 2823 120 -402 230 C ATOM 2081 CD PRO A 253 21.804 15.387 15.744 1.00 18.37 C ANISOU 2081 CD PRO A 253 2232 2533 2214 355 -377 504 C ATOM 2082 N PRO A 254 21.496 19.111 12.754 1.00 17.81 N ANISOU 2082 N PRO A 254 1780 2303 2684 228 -361 -105 N ATOM 2083 CA PRO A 254 22.104 19.462 11.461 1.00 20.52 C ANISOU 2083 CA PRO A 254 2328 2663 2803 115 -284 22 C ATOM 2084 C PRO A 254 23.620 19.571 11.549 1.00 21.96 C ANISOU 2084 C PRO A 254 2429 2854 3060 90 -162 -12 C ATOM 2085 O PRO A 254 24.314 19.603 10.536 1.00 26.30 O ANISOU 2085 O PRO A 254 2836 3467 3690 122 -182 68 O ATOM 2086 CB PRO A 254 21.470 20.810 11.098 1.00 21.48 C ANISOU 2086 CB PRO A 254 2498 2716 2948 134 -217 -19 C ATOM 2087 CG PRO A 254 20.728 21.262 12.259 1.00 19.59 C ANISOU 2087 CG PRO A 254 2086 2472 2885 137 -202 -82 C ATOM 2088 CD PRO A 254 20.715 20.228 13.315 1.00 18.54 C ANISOU 2088 CD PRO A 254 1824 2375 2843 175 -270 -122 C TER 2089 PRO A 254 HETATM 2090 O HOH A 257 5.857 16.378 38.267 1.00 9.28 O ANISOU 2090 O HOH A 257 1060 1205 1260 2 134 -12 O HETATM 2091 O HOH A 258 3.223 13.613 32.390 1.00 10.02 O ANISOU 2091 O HOH A 258 1123 1209 1475 -123 31 -100 O HETATM 2092 O HOH A 259 17.467 18.523 50.628 1.00 12.55 O ANISOU 2092 O HOH A 259 1872 1706 1187 184 -213 139 O HETATM 2093 O HOH A 260 12.613 38.198 28.267 1.00 13.34 O ANISOU 2093 O HOH A 260 2525 1443 1098 -326 108 1 O HETATM 2094 O HOH A 261 12.119 20.097 37.547 1.00 11.50 O ANISOU 2094 O HOH A 261 1506 1270 1591 82 -12 -267 O HETATM 2095 O HOH A 262 3.086 38.110 41.942 1.00 12.38 O ANISOU 2095 O HOH A 262 1690 1076 1936 108 291 -8 O HETATM 2096 O HOH A 263 12.488 21.028 40.196 1.00 11.42 O ANISOU 2096 O HOH A 263 1506 1463 1369 -178 341 -268 O HETATM 2097 O HOH A 264 11.699 39.021 48.809 1.00 13.14 O ANISOU 2097 O HOH A 264 1971 1673 1348 38 -172 -224 O HETATM 2098 O HOH A 265 0.857 13.610 36.313 1.00 12.82 O ANISOU 2098 O HOH A 265 1452 1795 1624 82 125 -207 O HETATM 2099 O HOH A 266 1.160 20.636 28.661 1.00 12.27 O ANISOU 2099 O HOH A 266 1152 1840 1669 121 140 -155 O HETATM 2100 O HOH A 267 22.690 18.262 25.879 1.00 12.97 O ANISOU 2100 O HOH A 267 1100 2220 1606 -112 -139 378 O HETATM 2101 O HOH A 268 15.609 20.822 24.691 1.00 14.88 O ANISOU 2101 O HOH A 268 1555 2565 1532 368 -24 223 O HETATM 2102 O HOH A 269 19.787 3.890 23.951 1.00 16.48 O ANISOU 2102 O HOH A 269 2236 1894 2131 -375 275 -386 O HETATM 2103 O HOH A 270 4.477 4.556 23.938 1.00 17.73 O ANISOU 2103 O HOH A 270 1904 2140 2690 -406 -29 189 O HETATM 2104 O HOH A 271 14.904 21.722 32.426 1.00 15.10 O ANISOU 2104 O HOH A 271 2144 1669 1925 277 214 -270 O HETATM 2105 O HOH A 272 5.567 30.099 50.177 1.00 15.92 O ANISOU 2105 O HOH A 272 2388 2264 1396 -350 158 -348 O HETATM 2106 O HOH A 273 -8.533 22.630 35.314 1.00 16.21 O ANISOU 2106 O HOH A 273 1051 3136 1971 -351 96 317 O HETATM 2107 O HOH A 274 3.184 10.775 36.818 1.00 13.32 O ANISOU 2107 O HOH A 274 1582 1737 1741 -190 327 -96 O HETATM 2108 O HOH A 275 11.498 47.049 35.227 1.00 18.06 O ANISOU 2108 O HOH A 275 2013 1590 3257 -136 552 -274 O HETATM 2109 O HOH A 276 8.741 24.081 21.875 1.00 14.05 O ANISOU 2109 O HOH A 276 2322 1393 1622 -94 187 186 O HETATM 2110 O HOH A 277 11.815 19.632 28.440 1.00 15.62 O ANISOU 2110 O HOH A 277 1689 2758 1488 717 117 294 O HETATM 2111 O HOH A 278 18.452 1.914 25.250 1.00 15.73 O ANISOU 2111 O HOH A 278 2102 1961 1912 92 303 115 O HETATM 2112 O HOH A 279 4.871 24.919 21.633 1.00 17.14 O ANISOU 2112 O HOH A 279 3047 1300 2164 372 -135 83 O HETATM 2113 O HOH A 280 6.420 32.900 47.437 1.00 16.97 O ANISOU 2113 O HOH A 280 2148 2581 1718 -748 183 -198 O HETATM 2114 O HOH A 281 -2.776 14.876 31.696 1.00 16.84 O ANISOU 2114 O HOH A 281 1362 2297 2738 -177 150 -11 O HETATM 2115 O HOH A 282 23.401 16.313 27.828 1.00 17.56 O ANISOU 2115 O HOH A 282 1322 2431 2918 -634 -713 781 O HETATM 2116 O HOH A 283 -1.677 36.073 47.010 1.00 18.18 O ANISOU 2116 O HOH A 283 2039 2237 2630 449 696 -309 O HETATM 2117 O HOH A 284 10.130 24.248 55.592 1.00 13.69 O ANISOU 2117 O HOH A 284 1620 1864 1718 174 92 355 O HETATM 2118 O HOH A 285 7.524 32.038 49.964 1.00 16.12 O ANISOU 2118 O HOH A 285 2175 1794 2155 -19 -52 -132 O HETATM 2119 O HOH A 286 -0.434 22.269 27.128 1.00 15.45 O ANISOU 2119 O HOH A 286 2133 1983 1751 332 -251 -330 O HETATM 2120 O HOH A 287 4.439 25.847 55.097 1.00 16.63 O ANISOU 2120 O HOH A 287 1913 2015 2389 429 128 94 O HETATM 2121 O HOH A 288 8.799 43.181 24.361 1.00 21.65 O ANISOU 2121 O HOH A 288 3499 2941 1784 68 -69 553 O HETATM 2122 O HOH A 289 11.945 21.689 16.501 1.00 16.77 O ANISOU 2122 O HOH A 289 2472 2129 1770 517 106 106 O HETATM 2123 O HOH A 290 13.353 25.950 19.009 1.00 19.32 O ANISOU 2123 O HOH A 290 3424 1782 2133 767 -387 433 O HETATM 2124 O HOH A 291 -0.055 18.111 43.248 1.00 19.35 O ANISOU 2124 O HOH A 291 2420 2612 2317 158 222 -110 O HETATM 2125 O HOH A 292 11.388 15.439 12.255 1.00 21.57 O ANISOU 2125 O HOH A 292 3808 2447 1938 -104 -482 147 O HETATM 2126 O HOH A 293 19.859 36.775 26.661 1.00 20.38 O ANISOU 2126 O HOH A 293 2719 2966 2058 -454 774 -92 O HETATM 2127 O HOH A 294 20.753 18.429 44.103 1.00 20.03 O ANISOU 2127 O HOH A 294 1900 3200 2511 135 221 -353 O HETATM 2128 O HOH A 295 -1.268 8.319 25.505 1.00 20.99 O ANISOU 2128 O HOH A 295 2142 2496 3335 -440 -513 -98 O HETATM 2129 O HOH A 296 14.672 35.261 51.230 1.00 19.80 O ANISOU 2129 O HOH A 296 2934 2745 1841 -673 -385 201 O HETATM 2130 O HOH A 297 11.700 35.812 21.395 1.00 23.98 O ANISOU 2130 O HOH A 297 3761 2595 2755 -462 -147 -484 O HETATM 2131 O HOH A 298 7.236 12.835 44.679 1.00 20.22 O ANISOU 2131 O HOH A 298 2587 2665 2431 -508 244 780 O HETATM 2132 O HOH A 299 6.980 30.441 18.903 1.00 24.02 O ANISOU 2132 O HOH A 299 3423 3485 2217 -615 -26 -846 O HETATM 2133 O HOH A 300 24.226 8.779 21.788 1.00 20.42 O ANISOU 2133 O HOH A 300 2396 3004 2359 88 221 -214 O HETATM 2134 O HOH A 301 27.906 9.146 27.576 1.00 21.99 O ANISOU 2134 O HOH A 301 1721 3412 3220 370 -437 -444 O HETATM 2135 O HOH A 302 -3.189 39.218 41.028 1.00 19.10 O ANISOU 2135 O HOH A 302 1536 2759 2961 -90 -42 520 O HETATM 2136 O HOH A 303 4.815 49.684 34.536 1.00 18.04 O ANISOU 2136 O HOH A 303 1630 1573 3650 346 -5 117 O HETATM 2137 O HOH A 304 11.964 22.090 19.167 1.00 16.54 O ANISOU 2137 O HOH A 304 2420 2318 1544 508 164 342 O HETATM 2138 O HOH A 305 32.701 15.207 24.379 1.00 23.48 O ANISOU 2138 O HOH A 305 2869 3066 2984 -26 111 -207 O HETATM 2139 O HOH A 306 4.628 21.806 11.344 1.00 23.38 O ANISOU 2139 O HOH A 306 2814 3019 3048 406 -172 93 O HETATM 2140 O HOH A 307 21.349 24.087 52.519 1.00 20.36 O ANISOU 2140 O HOH A 307 2557 2563 2613 -547 -1102 737 O HETATM 2141 O HOH A 308 15.750 23.674 23.944 1.00 19.22 O ANISOU 2141 O HOH A 308 1908 2766 2627 191 -180 10 O HETATM 2142 O HOH A 309 -0.451 21.715 16.816 1.00 22.71 O ANISOU 2142 O HOH A 309 2220 3128 3279 112 -79 41 O HETATM 2143 O HOH A 310 -1.380 40.988 22.302 1.00 28.12 O ANISOU 2143 O HOH A 310 3741 3546 3398 236 -575 180 O HETATM 2144 O HOH A 311 19.685 24.144 46.521 1.00 19.41 O ANISOU 2144 O HOH A 311 2377 2565 2431 363 147 -43 O HETATM 2145 O HOH A 312 12.829 22.664 30.809 1.00 20.17 O ANISOU 2145 O HOH A 312 2381 2337 2942 -184 33 522 O HETATM 2146 O HOH A 313 11.597 37.144 50.915 1.00 19.84 O ANISOU 2146 O HOH A 313 3680 2053 1804 -107 -316 -340 O HETATM 2147 O HOH A 314 21.326 36.096 36.027 1.00 20.47 O ANISOU 2147 O HOH A 314 2542 2886 2348 305 -34 -70 O HETATM 2148 O HOH A 315 -3.522 21.136 41.813 1.00 21.97 O ANISOU 2148 O HOH A 315 2256 2309 3783 -225 -311 -789 O HETATM 2149 O HOH A 316 9.859 28.786 21.011 1.00 22.62 O ANISOU 2149 O HOH A 316 3414 2620 2561 -402 155 46 O HETATM 2150 O HOH A 317 -2.144 14.843 36.260 1.00 22.01 O ANISOU 2150 O HOH A 317 2233 3088 3041 -462 36 -98 O HETATM 2151 O HOH A 318 18.506 45.699 34.422 1.00 25.37 O ANISOU 2151 O HOH A 318 3994 2057 3586 -808 479 -10 O HETATM 2152 O HOH A 319 -6.014 25.382 29.129 1.00 21.04 O ANISOU 2152 O HOH A 319 2700 2842 2452 168 -34 -495 O HETATM 2153 O HOH A 320 16.314 25.037 30.149 1.00 23.06 O ANISOU 2153 O HOH A 320 2675 3400 2686 614 -33 34 O HETATM 2154 O HOH A 321 8.045 36.915 21.264 1.00 21.39 O ANISOU 2154 O HOH A 321 3765 2389 1971 -164 -294 7 O HETATM 2155 O HOH A 322 22.309 37.431 42.141 1.00 19.71 O ANISOU 2155 O HOH A 322 1823 2400 3264 -615 -404 -127 O HETATM 2156 O HOH A 323 1.277 6.072 21.921 1.00 20.70 O ANISOU 2156 O HOH A 323 1848 3203 2811 -466 -212 -313 O HETATM 2157 O HOH A 324 -5.264 16.780 25.295 1.00 25.02 O ANISOU 2157 O HOH A 324 1812 4150 3542 505 -394 146 O HETATM 2158 O HOH A 325 13.595 28.067 28.255 1.00 20.50 O ANISOU 2158 O HOH A 325 3236 1972 2580 -103 217 59 O HETATM 2159 O HOH A 326 3.889 12.347 44.731 1.00 22.11 O ANISOU 2159 O HOH A 326 3335 2368 2694 -353 1126 468 O HETATM 2160 O HOH A 327 18.564 30.216 29.624 1.00 21.55 O ANISOU 2160 O HOH A 327 2678 2828 2681 250 -69 -431 O HETATM 2161 O HOH A 328 6.727 17.982 13.052 1.00 30.25 O ANISOU 2161 O HOH A 328 4349 3409 3733 -378 124 89 O HETATM 2162 O HOH A 329 -0.889 22.412 23.243 1.00 21.64 O ANISOU 2162 O HOH A 329 2524 3294 2405 221 -143 -8 O HETATM 2163 O HOH A 330 8.378 50.227 41.039 1.00 19.92 O ANISOU 2163 O HOH A 330 2396 2120 3052 -48 -212 46 O HETATM 2164 O HOH A 331 -4.273 30.441 49.790 1.00 25.09 O ANISOU 2164 O HOH A 331 3674 3506 2353 149 -524 -293 O HETATM 2165 O HOH A 332 2.265 22.766 52.732 1.00 21.34 O ANISOU 2165 O HOH A 332 3188 2624 2294 112 152 393 O HETATM 2166 O HOH A 333 -3.512 37.837 45.766 1.00 21.53 O ANISOU 2166 O HOH A 333 1840 3053 3286 473 217 -250 O HETATM 2167 O HOH A 334 3.240 31.909 50.625 1.00 22.81 O ANISOU 2167 O HOH A 334 2974 2719 2970 35 274 -659 O HETATM 2168 O HOH A 335 11.000 29.334 28.385 1.00 20.53 O ANISOU 2168 O HOH A 335 2795 2721 2285 400 -182 -593 O HETATM 2169 O HOH A 336 16.609 28.568 41.008 1.00 20.58 O ANISOU 2169 O HOH A 336 2559 2570 2689 -104 -227 94 O HETATM 2170 O HOH A 337 15.115 31.099 52.894 1.00 28.76 O ANISOU 2170 O HOH A 337 4145 3233 3548 -439 289 -209 O HETATM 2171 O HOH A 338 -0.299 7.009 32.184 1.00 22.30 O ANISOU 2171 O HOH A 338 2361 3216 2895 -754 383 160 O HETATM 2172 O HOH A 339 27.223 11.661 24.573 1.00 21.63 O ANISOU 2172 O HOH A 339 2161 2832 3224 235 139 53 O HETATM 2173 O HOH A 340 -5.485 41.653 32.994 1.00 23.64 O ANISOU 2173 O HOH A 340 2608 2471 3903 525 -650 380 O HETATM 2174 O HOH A 341 8.808 21.517 28.611 1.00 16.37 O ANISOU 2174 O HOH A 341 1841 2109 2270 231 -2 297 O HETATM 2175 O HOH A 342 -1.080 31.462 47.587 1.00 21.45 O ANISOU 2175 O HOH A 342 2558 3038 2554 -193 587 -338 O HETATM 2176 O HOH A 343 -1.741 13.528 33.879 1.00 18.60 O ANISOU 2176 O HOH A 343 1731 2397 2936 225 118 9 O HETATM 2177 O HOH A 344 0.269 43.131 21.198 1.00 27.51 O ANISOU 2177 O HOH A 344 3676 3716 3060 351 -788 652 O HETATM 2178 O HOH A 345 11.334 44.473 46.107 1.00 25.65 O ANISOU 2178 O HOH A 345 3512 2678 3553 -563 103 358 O HETATM 2179 O HOH A 346 12.161 28.487 22.864 1.00 23.11 O ANISOU 2179 O HOH A 346 3958 2512 2310 -458 37 -323 O HETATM 2180 O HOH A 347 6.360 17.838 46.080 1.00 23.42 O ANISOU 2180 O HOH A 347 3357 3167 2373 206 591 -4 O HETATM 2181 O HOH A 348 16.772 27.280 54.500 1.00 28.40 O ANISOU 2181 O HOH A 348 4834 3551 2402 379 -42 432 O HETATM 2182 O HOH A 349 -2.118 18.930 41.487 1.00 24.74 O ANISOU 2182 O HOH A 349 2595 3108 3695 166 284 -184 O HETATM 2183 O HOH A 350 13.796 24.591 22.271 1.00 21.24 O ANISOU 2183 O HOH A 350 2571 2691 2805 609 13 270 O HETATM 2184 O HOH A 351 -4.216 34.653 31.209 1.00 27.60 O ANISOU 2184 O HOH A 351 3192 3757 3537 145 2 228 O HETATM 2185 O HOH A 352 9.710 36.875 19.006 1.00 26.83 O ANISOU 2185 O HOH A 352 3823 3897 2474 249 -466 163 O HETATM 2186 O HOH A 353 22.769 40.936 36.117 1.00 24.74 O ANISOU 2186 O HOH A 353 2772 3202 3425 -405 -395 -386 O HETATM 2187 O HOH A 354 0.719 37.114 24.019 1.00 24.88 O ANISOU 2187 O HOH A 354 3525 3041 2885 344 -888 617 O HETATM 2188 O HOH A 355 24.581 4.192 23.732 1.00 23.36 O ANISOU 2188 O HOH A 355 2693 3041 3138 -132 -159 -706 O HETATM 2189 O HOH A 356 26.929 5.376 29.113 1.00 21.90 O ANISOU 2189 O HOH A 356 2305 2732 3283 36 -484 159 O HETATM 2190 O HOH A 357 0.803 20.342 47.343 1.00 33.24 O ANISOU 2190 O HOH A 357 4461 3988 4178 114 43 37 O HETATM 2191 O HOH A 358 8.628 44.364 45.633 1.00 26.93 O ANISOU 2191 O HOH A 358 3964 2437 3832 538 104 -169 O HETATM 2192 O HOH A 359 21.071 35.158 33.464 1.00 26.03 O ANISOU 2192 O HOH A 359 3546 3233 3108 494 -606 -483 O HETATM 2193 O HOH A 360 14.894 4.564 20.970 1.00 21.85 O ANISOU 2193 O HOH A 360 2810 2163 3328 -79 -311 -48 O HETATM 2194 O HOH A 361 -1.127 28.470 47.512 1.00 22.75 O ANISOU 2194 O HOH A 361 2383 3559 2699 437 47 -5 O HETATM 2195 O HOH A 362 20.911 27.858 46.957 1.00 26.87 O ANISOU 2195 O HOH A 362 2179 4194 3835 351 -490 -248 O HETATM 2196 O HOH A 363 1.043 23.267 24.888 1.00 21.77 O ANISOU 2196 O HOH A 363 2612 3359 2301 302 -223 -60 O HETATM 2197 O HOH A 364 1.430 12.882 43.316 1.00 24.16 O ANISOU 2197 O HOH A 364 2912 3630 2638 -467 842 456 O HETATM 2198 O HOH A 365 2.223 25.221 53.730 1.00 22.61 O ANISOU 2198 O HOH A 365 2527 3032 3029 -44 -155 98 O HETATM 2199 O HOH A 366 28.231 19.899 21.686 1.00 30.17 O ANISOU 2199 O HOH A 366 3530 4424 3507 3 336 168 O HETATM 2200 O HOH A 367 4.357 16.102 10.681 1.00 26.13 O ANISOU 2200 O HOH A 367 3172 3626 3130 -450 -6 307 O HETATM 2201 O HOH A 368 18.137 28.842 22.540 1.00 28.49 O ANISOU 2201 O HOH A 368 4487 3135 3203 21 28 -223 O HETATM 2202 O HOH A 369 -5.856 19.313 30.455 1.00 25.53 O ANISOU 2202 O HOH A 369 2230 3542 3926 359 -215 -245 O HETATM 2203 O HOH A 370 10.142 15.399 15.655 1.00 25.33 O ANISOU 2203 O HOH A 370 3150 3444 3030 -66 42 170 O HETATM 2204 O HOH A 371 -6.659 38.295 38.579 1.00 30.81 O ANISOU 2204 O HOH A 371 2646 4390 4669 720 103 -33 O HETATM 2205 O HOH A 372 4.416 28.857 22.591 1.00 26.04 O ANISOU 2205 O HOH A 372 4746 1977 3169 -567 123 -47 O HETATM 2206 O HOH A 373 24.421 14.402 27.023 1.00 24.23 O ANISOU 2206 O HOH A 373 2967 3060 3180 -494 447 -339 O HETATM 2207 O HOH A 374 -2.435 14.104 12.183 1.00 32.45 O ANISOU 2207 O HOH A 374 4062 4431 3833 -117 -118 -137 O HETATM 2208 O HOH A 375 14.938 7.245 41.309 1.00 29.27 O ANISOU 2208 O HOH A 375 4100 3077 3943 -448 261 156 O HETATM 2209 O HOH A 376 -5.597 23.362 27.460 1.00 26.17 O ANISOU 2209 O HOH A 376 3266 3476 3199 702 -178 -457 O HETATM 2210 O HOH A 377 -3.774 37.737 28.064 1.00 28.34 O ANISOU 2210 O HOH A 377 2995 3906 3865 -439 -530 44 O HETATM 2211 O HOH A 378 15.464 16.412 14.302 1.00 22.15 O ANISOU 2211 O HOH A 378 3191 2366 2858 -338 201 253 O HETATM 2212 O HOH A 379 1.614 43.543 44.120 1.00 21.97 O ANISOU 2212 O HOH A 379 2555 1926 3866 876 -259 -667 O HETATM 2213 O HOH A 380 -8.395 23.933 37.784 1.00 30.97 O ANISOU 2213 O HOH A 380 3947 3241 4578 -430 512 42 O HETATM 2214 O HOH A 381 -1.532 19.720 47.412 1.00 30.68 O ANISOU 2214 O HOH A 381 4013 4230 3412 -39 49 93 O HETATM 2215 O HOH A 382 23.042 20.006 7.779 1.00 30.64 O ANISOU 2215 O HOH A 382 3546 3987 4106 -119 73 -43 O HETATM 2216 O HOH A 383 18.458 8.782 43.452 1.00 27.78 O ANISOU 2216 O HOH A 383 4080 2672 3802 239 -185 652 O HETATM 2217 O HOH A 384 12.834 13.180 12.065 1.00 28.04 O ANISOU 2217 O HOH A 384 3428 4207 3019 -77 -107 620 O HETATM 2218 O HOH A 385 17.548 34.944 48.830 1.00 27.42 O ANISOU 2218 O HOH A 385 3795 4101 2522 121 -404 402 O HETATM 2219 O HOH A 386 13.419 -3.060 26.321 1.00 31.37 O ANISOU 2219 O HOH A 386 3987 3875 4055 416 -148 201 O HETATM 2220 O HOH A 387 18.657 26.991 20.407 1.00 29.93 O ANISOU 2220 O HOH A 387 4619 3424 3329 285 -513 -83 O HETATM 2221 O HOH A 388 -3.794 16.562 42.244 1.00 37.88 O ANISOU 2221 O HOH A 388 4777 4588 5025 -56 148 -78 O HETATM 2222 O HOH A 389 -0.789 8.066 22.754 1.00 25.26 O ANISOU 2222 O HOH A 389 2972 2857 3766 -59 -128 -67 O HETATM 2223 O HOH A 390 0.608 6.126 19.086 1.00 25.63 O ANISOU 2223 O HOH A 390 2782 3564 3389 -236 -392 -216 O HETATM 2224 O HOH A 391 6.374 3.807 17.204 1.00 32.22 O ANISOU 2224 O HOH A 391 4527 3850 3863 -158 -95 -253 O HETATM 2225 O HOH A 392 1.837 1.278 25.533 1.00 38.18 O ANISOU 2225 O HOH A 392 4956 4650 4898 -140 -130 131 O HETATM 2226 O HOH A 393 2.238 4.018 25.387 1.00 24.46 O ANISOU 2226 O HOH A 393 2513 3657 3124 -385 153 299 O HETATM 2227 O HOH A 394 6.458 -4.680 25.450 1.00 43.90 O ANISOU 2227 O HOH A 394 5610 5534 5532 -38 -55 54 O HETATM 2228 O HOH A 395 5.475 -1.148 27.245 1.00 26.86 O ANISOU 2228 O HOH A 395 3240 3062 3903 -679 68 270 O HETATM 2229 O HOH A 396 6.534 -0.459 29.548 1.00 33.97 O ANISOU 2229 O HOH A 396 4408 4205 4293 -47 -41 -191 O HETATM 2230 O HOH A 397 8.307 -1.361 31.357 1.00 34.48 O ANISOU 2230 O HOH A 397 4360 4422 4316 -55 -213 16 O HETATM 2231 O HOH A 398 12.271 -7.866 30.278 1.00 38.34 O ANISOU 2231 O HOH A 398 4924 4679 4964 -151 33 102 O HETATM 2232 O HOH A 399 11.878 -2.775 24.113 1.00 27.75 O ANISOU 2232 O HOH A 399 4009 2336 4196 501 -183 -2 O HETATM 2233 O HOH A 400 1.542 5.112 27.878 1.00 27.37 O ANISOU 2233 O HOH A 400 3474 3322 3600 -237 244 9 O HETATM 2234 O HOH A 401 -0.720 6.051 26.933 1.00 37.80 O ANISOU 2234 O HOH A 401 5012 4267 5081 -81 -35 189 O HETATM 2235 O HOH A 402 14.359 0.333 19.982 1.00 31.23 O ANISOU 2235 O HOH A 402 3995 3845 4024 -29 -111 -316 O HETATM 2236 O HOH A 403 16.843 4.866 19.124 1.00 28.31 O ANISOU 2236 O HOH A 403 4007 3380 3367 -16 -94 -409 O HETATM 2237 O HOH A 404 10.474 -2.646 32.709 1.00 27.61 O ANISOU 2237 O HOH A 404 3177 3379 3935 74 38 531 O HETATM 2238 O HOH A 405 11.628 3.268 40.793 1.00 41.76 O ANISOU 2238 O HOH A 405 5317 5274 5276 74 -9 142 O HETATM 2239 O HOH A 406 12.723 2.035 38.673 1.00 36.05 O ANISOU 2239 O HOH A 406 4504 4755 4436 290 12 -25 O HETATM 2240 O HOH A 407 15.217 6.004 38.740 1.00 28.19 O ANISOU 2240 O HOH A 407 2387 4160 4160 -88 -119 377 O HETATM 2241 O HOH A 408 24.807 5.517 32.316 1.00 28.43 O ANISOU 2241 O HOH A 408 3856 3735 3210 21 -467 -69 O HETATM 2242 O HOH A 409 20.709 9.107 41.819 1.00 31.43 O ANISOU 2242 O HOH A 409 4131 3681 4127 -7 292 37 O HETATM 2243 O HOH A 410 24.603 11.566 41.350 1.00 37.75 O ANISOU 2243 O HOH A 410 5216 4314 4812 26 -1 257 O HETATM 2244 O HOH A 411 -8.066 36.300 36.846 1.00 25.42 O ANISOU 2244 O HOH A 411 3090 2741 3825 1040 76 118 O HETATM 2245 O HOH A 412 23.639 14.400 37.863 1.00 24.73 O ANISOU 2245 O HOH A 412 1748 4015 3633 484 0 225 O HETATM 2246 O HOH A 413 24.446 19.855 41.685 1.00 34.21 O ANISOU 2246 O HOH A 413 4572 4692 3734 34 48 -94 O HETATM 2247 O HOH A 414 27.707 14.860 41.844 1.00 35.83 O ANISOU 2247 O HOH A 414 4364 4719 4529 126 294 269 O HETATM 2248 O HOH A 415 21.855 24.710 47.960 1.00 39.58 O ANISOU 2248 O HOH A 415 4903 5033 5102 -39 163 -54 O HETATM 2249 O HOH A 416 21.354 26.636 44.551 1.00 26.01 O ANISOU 2249 O HOH A 416 2597 4207 3075 -102 -473 219 O HETATM 2250 O HOH A 417 25.265 25.302 32.491 1.00 31.46 O ANISOU 2250 O HOH A 417 4363 3944 3645 219 -184 -40 O HETATM 2251 O HOH A 418 19.406 31.565 31.950 0.50 18.68 O ANISOU 2251 O HOH A 418 2728 2125 2243 212 40 -185 O HETATM 2252 O HOH A 419 20.915 29.899 28.214 1.00 28.21 O ANISOU 2252 O HOH A 419 3482 3867 3369 127 180 -62 O HETATM 2253 O HOH A 420 11.917 24.775 28.980 1.00 24.63 O ANISOU 2253 O HOH A 420 3848 2652 2857 -255 -82 -22 O HETATM 2254 O HOH A 421 13.453 25.839 26.624 1.00 30.00 O ANISOU 2254 O HOH A 421 3783 3929 3685 152 190 -307 O HETATM 2255 O HOH A 422 9.187 24.294 28.351 1.00 36.82 O ANISOU 2255 O HOH A 422 4769 4615 4606 304 -205 93 O HETATM 2256 O HOH A 423 23.675 37.728 39.455 1.00 29.61 O ANISOU 2256 O HOH A 423 3387 3791 4070 -214 -40 151 O HETATM 2257 O HOH A 424 23.113 38.122 36.725 1.00 24.63 O ANISOU 2257 O HOH A 424 2542 3430 3385 -42 -178 -279 O HETATM 2258 O HOH A 425 23.843 35.259 42.760 1.00 35.97 O ANISOU 2258 O HOH A 425 3828 4804 5033 91 -212 65 O HETATM 2259 O HOH A 426 18.499 38.900 49.204 1.00 40.33 O ANISOU 2259 O HOH A 426 5158 5279 4884 65 27 -5 O HETATM 2260 O HOH A 427 16.845 41.036 49.132 1.00 33.35 O ANISOU 2260 O HOH A 427 4411 4043 4214 -76 -135 -205 O HETATM 2261 O HOH A 428 19.845 31.025 49.276 1.00 44.40 O ANISOU 2261 O HOH A 428 5574 5653 5641 -60 -37 -39 O HETATM 2262 O HOH A 429 15.844 44.451 46.744 1.00 36.48 O ANISOU 2262 O HOH A 429 4684 4583 4594 153 257 283 O HETATM 2263 O HOH A 430 13.676 43.096 46.241 1.00 28.97 O ANISOU 2263 O HOH A 430 3470 3924 3610 -130 493 -521 O HETATM 2264 O HOH A 431 6.522 40.544 47.806 1.00 30.43 O ANISOU 2264 O HOH A 431 3521 4065 3974 -172 -152 31 O HETATM 2265 O HOH A 432 10.691 41.258 50.144 1.00 27.42 O ANISOU 2265 O HOH A 432 4120 3269 3029 219 227 -912 O HETATM 2266 O HOH A 433 5.198 45.284 44.894 1.00 26.32 O ANISOU 2266 O HOH A 433 3511 3592 2895 -224 600 -37 O HETATM 2267 O HOH A 434 4.406 43.665 46.507 1.00 29.01 O ANISOU 2267 O HOH A 434 4499 2653 3871 -45 -35 -510 O HETATM 2268 O HOH A 435 2.017 40.941 48.806 1.00 31.31 O ANISOU 2268 O HOH A 435 4170 3884 3841 344 -189 -114 O HETATM 2269 O HOH A 436 -0.075 40.812 47.021 1.00 26.74 O ANISOU 2269 O HOH A 436 4170 2800 3188 302 57 -1042 O HETATM 2270 O HOH A 437 -1.371 33.451 22.050 1.00 36.37 O ANISOU 2270 O HOH A 437 4766 4450 4600 -11 -278 106 O HETATM 2271 O HOH A 438 -0.787 31.084 23.315 1.00 36.15 O ANISOU 2271 O HOH A 438 4685 4627 4420 120 -93 17 O HETATM 2272 O HOH A 439 0.988 29.331 22.516 1.00 31.38 O ANISOU 2272 O HOH A 439 3812 4137 3973 -169 135 51 O HETATM 2273 O HOH A 440 4.419 34.434 15.332 1.00 24.05 O ANISOU 2273 O HOH A 440 3165 3234 2738 37 -86 -358 O HETATM 2274 O HOH A 441 6.996 33.426 16.217 1.00 29.56 O ANISOU 2274 O HOH A 441 3653 3744 3832 41 -85 -509 O HETATM 2275 O HOH A 442 -0.163 34.719 14.715 1.00 33.35 O ANISOU 2275 O HOH A 442 4068 4670 3931 240 -137 -79 O HETATM 2276 O HOH A 443 0.971 32.710 49.452 1.00 28.04 O ANISOU 2276 O HOH A 443 3409 4046 3198 63 109 -292 O HETATM 2277 O HOH A 444 4.777 32.828 17.482 1.00 45.85 O ANISOU 2277 O HOH A 444 6158 5765 5496 -48 -140 -46 O HETATM 2278 O HOH A 445 -1.552 36.145 22.627 1.00 35.45 O ANISOU 2278 O HOH A 445 4549 4536 4383 -134 -169 111 O HETATM 2279 O HOH A 446 2.622 40.650 17.828 1.00 31.83 O ANISOU 2279 O HOH A 446 4366 4288 3438 63 -361 212 O HETATM 2280 O HOH A 447 7.864 29.309 23.198 1.00 27.45 O ANISOU 2280 O HOH A 447 3728 2709 3992 -338 -165 -947 O HETATM 2281 O HOH A 448 7.191 26.300 22.181 1.00 20.67 O ANISOU 2281 O HOH A 448 2605 2155 3090 264 -75 56 O HETATM 2282 O HOH A 449 8.042 27.216 55.854 1.00 23.39 O ANISOU 2282 O HOH A 449 3694 2698 2494 -239 -369 -566 O HETATM 2283 O HOH A 450 7.634 26.208 25.101 1.00 26.21 O ANISOU 2283 O HOH A 450 4221 2242 3495 -677 220 -20 O HETATM 2284 O HOH A 451 11.607 26.252 20.810 1.00 22.67 O ANISOU 2284 O HOH A 451 3238 2650 2726 -255 -205 39 O HETATM 2285 O HOH A 452 11.073 24.636 23.487 1.00 20.67 O ANISOU 2285 O HOH A 452 2836 2017 2998 -320 -426 -228 O HETATM 2286 O HOH A 453 14.625 27.023 22.338 1.00 29.64 O ANISOU 2286 O HOH A 453 4334 3016 3912 8 107 387 O HETATM 2287 O HOH A 454 12.766 36.961 19.092 1.00 32.14 O ANISOU 2287 O HOH A 454 4778 3793 3638 124 -65 -128 O HETATM 2288 O HOH A 455 10.371 39.430 20.536 1.00 27.69 O ANISOU 2288 O HOH A 455 4133 3557 2828 81 55 149 O HETATM 2289 O HOH A 456 11.514 26.946 25.084 1.00 33.93 O ANISOU 2289 O HOH A 456 4724 3936 4231 -239 77 -14 O HETATM 2290 O HOH A 457 16.690 28.337 29.418 1.00 31.75 O ANISOU 2290 O HOH A 457 4207 4226 3629 227 -55 64 O HETATM 2291 O HOH A 458 20.562 28.423 23.305 1.00 31.09 O ANISOU 2291 O HOH A 458 4276 3643 3892 -87 50 -302 O HETATM 2292 O HOH A 459 19.960 36.768 21.618 1.00 38.92 O ANISOU 2292 O HOH A 459 5277 5136 4374 71 213 -22 O HETATM 2293 O HOH A 460 21.741 30.960 24.113 1.00 43.72 O ANISOU 2293 O HOH A 460 5569 5560 5482 -43 51 -64 O HETATM 2294 O HOH A 461 21.018 32.050 26.339 1.00 39.43 O ANISOU 2294 O HOH A 461 4993 5185 4801 -20 61 10 O HETATM 2295 O HOH A 462 21.008 38.546 28.234 1.00 30.35 O ANISOU 2295 O HOH A 462 3630 3760 4141 -121 -10 -417 O HETATM 2296 O HOH A 463 20.711 37.186 24.018 1.00 38.46 O ANISOU 2296 O HOH A 463 4879 5023 4711 -95 197 142 O HETATM 2297 O HOH A 464 5.932 50.486 46.287 1.00 51.77 O ANISOU 2297 O HOH A 464 6504 6600 6564 37 92 110 O HETATM 2298 O HOH A 465 -4.461 42.683 45.434 1.00 25.04 O ANISOU 2298 O HOH A 465 3214 3022 3277 102 492 67 O HETATM 2299 O HOH A 466 2.689 50.178 44.966 1.00 44.62 O ANISOU 2299 O HOH A 466 5673 5488 5790 49 -1 -30 O HETATM 2300 O HOH A 467 -2.275 45.008 45.514 1.00 45.17 O ANISOU 2300 O HOH A 467 5596 5713 5852 13 -89 -41 O HETATM 2301 O HOH A 468 4.780 56.270 41.256 1.00 24.32 O ANISOU 2301 O HOH A 468 2523 3069 3648 44 -174 105 O HETATM 2302 O HOH A 469 2.075 49.323 34.604 1.00 22.36 O ANISOU 2302 O HOH A 469 2549 2467 3477 231 -250 99 O HETATM 2303 O HOH A 470 1.335 49.427 31.674 1.00 30.72 O ANISOU 2303 O HOH A 470 4023 3891 3756 149 -33 -133 O HETATM 2304 O HOH A 471 8.518 50.736 37.221 1.00 26.59 O ANISOU 2304 O HOH A 471 3326 3095 3681 -63 -137 462 O HETATM 2305 O HOH A 472 6.424 51.663 35.825 1.00 22.44 O ANISOU 2305 O HOH A 472 2515 1809 4201 -70 115 19 O HETATM 2306 O HOH A 473 7.677 45.222 23.056 1.00 37.21 O ANISOU 2306 O HOH A 473 4922 4502 4712 119 130 81 O HETATM 2307 O HOH A 474 3.253 47.774 25.836 1.00 38.64 O ANISOU 2307 O HOH A 474 4991 4853 4837 -64 -78 91 O HETATM 2308 O HOH A 475 2.009 52.048 30.414 1.00 37.60 O ANISOU 2308 O HOH A 475 4850 4800 4632 -12 -138 29 O HETATM 2309 O HOH A 476 -1.967 45.154 27.723 1.00 29.62 O ANISOU 2309 O HOH A 476 3592 3812 3850 418 -307 116 O HETATM 2310 O HOH A 477 -5.538 38.851 26.524 1.00 37.54 O ANISOU 2310 O HOH A 477 4617 4813 4831 204 -144 -81 O HETATM 2311 O HOH A 478 -5.102 37.077 30.302 1.00 31.65 O ANISOU 2311 O HOH A 478 3624 4121 4278 116 -87 137 O HETATM 2312 O HOH A 479 4.708 19.735 45.497 1.00 31.23 O ANISOU 2312 O HOH A 479 4215 3851 3798 268 105 -264 O HETATM 2313 O HOH A 480 1.468 18.974 45.417 1.00 29.62 O ANISOU 2313 O HOH A 480 4558 3397 3300 367 -58 342 O HETATM 2314 O HOH A 481 1.486 16.280 46.504 1.00 25.66 O ANISOU 2314 O HOH A 481 3251 3279 3218 126 26 299 O HETATM 2315 O HOH A 482 -10.101 22.988 44.992 1.00 25.93 O ANISOU 2315 O HOH A 482 3612 2830 3411 -105 220 57 O HETATM 2316 O HOH A 483 -5.414 15.275 32.036 1.00 24.93 O ANISOU 2316 O HOH A 483 1909 3504 4057 -59 280 72 O HETATM 2317 O HOH A 484 3.906 27.204 24.640 1.00 23.86 O ANISOU 2317 O HOH A 484 3496 2886 2683 27 241 529 O HETATM 2318 O HOH A 485 3.000 24.902 23.498 1.00 27.97 O ANISOU 2318 O HOH A 485 3522 3550 3554 -370 -71 -253 O HETATM 2319 O HOH A 486 19.541 28.905 52.388 1.00 38.45 O ANISOU 2319 O HOH A 486 4884 4897 4828 -29 -48 -9 O HETATM 2320 O HOH A 487 8.984 11.041 45.295 1.00 25.41 O ANISOU 2320 O HOH A 487 3729 3146 2776 -82 -430 725 O HETATM 2321 O HOH A 488 0.222 10.603 42.369 1.00 29.87 O ANISOU 2321 O HOH A 488 3762 3367 4221 -277 156 92 O HETATM 2322 O HOH A 489 1.486 8.900 37.898 1.00 28.66 O ANISOU 2322 O HOH A 489 3779 2903 4206 -592 665 245 O HETATM 2323 O HOH A 490 -0.138 14.806 45.184 1.00 29.06 O ANISOU 2323 O HOH A 490 4084 4070 2887 -39 293 234 O HETATM 2324 O HOH A 491 -2.442 10.313 12.908 1.00 46.26 O ANISOU 2324 O HOH A 491 5746 6067 5760 -78 -32 4 O HETATM 2325 O HOH A 492 -1.631 23.208 18.809 1.00 28.33 O ANISOU 2325 O HOH A 492 3311 3521 3930 139 45 -273 O HETATM 2326 O HOH A 493 0.703 24.431 22.320 1.00 27.95 O ANISOU 2326 O HOH A 493 3637 3427 3552 173 -39 -236 O HETATM 2327 O HOH A 494 -6.151 19.468 24.164 1.00 40.47 O ANISOU 2327 O HOH A 494 4988 5347 5042 49 68 63 O HETATM 2328 O HOH A 495 -1.601 9.172 33.811 1.00 29.51 O ANISOU 2328 O HOH A 495 3169 3854 4186 -196 312 -88 O HETATM 2329 O HOH A 496 -3.981 8.409 25.178 1.00 32.54 O ANISOU 2329 O HOH A 496 3680 3947 4735 -232 -108 75 O HETATM 2330 O HOH A 497 23.406 25.509 20.915 1.00 35.17 O ANISOU 2330 O HOH A 497 4459 4271 4634 1 -57 240 O HETATM 2331 O HOH A 498 25.105 6.021 21.543 1.00 28.32 O ANISOU 2331 O HOH A 498 3381 3572 3805 285 261 -399 O HETATM 2332 O HOH A 499 26.434 2.220 23.263 1.00 31.59 O ANISOU 2332 O HOH A 499 4188 3902 3912 250 74 -204 O HETATM 2333 O HOH A 500 22.190 2.890 23.069 1.00 21.03 O ANISOU 2333 O HOH A 500 2659 2359 2972 372 222 -319 O HETATM 2334 O HOH A 501 22.295 3.089 20.373 1.00 29.42 O ANISOU 2334 O HOH A 501 3946 3819 3411 206 144 -40 O HETATM 2335 O HOH A 502 15.897 3.177 14.564 1.00 41.40 O ANISOU 2335 O HOH A 502 5357 5273 5097 212 158 -91 O HETATM 2336 O HOH A 503 12.620 5.982 10.739 1.00 37.31 O ANISOU 2336 O HOH A 503 4810 4640 4726 -176 -55 -155 O HETATM 2337 O HOH A 504 23.316 12.430 18.664 1.00 34.79 O ANISOU 2337 O HOH A 504 4740 4592 3886 9 -109 39 O HETATM 2338 O HOH A 505 26.174 16.709 17.928 1.00 35.86 O ANISOU 2338 O HOH A 505 4021 4960 4644 23 118 61 O HETATM 2339 O HOH A 506 24.784 13.806 20.796 1.00 29.51 O ANISOU 2339 O HOH A 506 3634 3762 3815 -340 233 163 O HETATM 2340 O HOH A 507 28.286 16.893 19.700 1.00 45.52 O ANISOU 2340 O HOH A 507 5743 5794 5758 -56 0 6 O HETATM 2341 O HOH A 508 28.510 14.552 21.141 1.00 37.05 O ANISOU 2341 O HOH A 508 4521 4904 4653 18 125 3 O HETATM 2342 O HOH A 509 10.618 -5.166 23.901 1.00 39.58 O ANISOU 2342 O HOH A 509 5246 4770 5020 -80 -4 -112 O HETATM 2343 O HOH A 510 2.144 1.038 29.905 1.00 38.46 O ANISOU 2343 O HOH A 510 4637 5017 4957 3 79 99 O HETATM 2344 O HOH A 511 2.473 -0.308 27.695 1.00 35.63 O ANISOU 2344 O HOH A 511 4579 4572 4385 -121 -131 -3 O HETATM 2345 O HOH A 512 0.795 3.160 29.482 1.00 31.82 O ANISOU 2345 O HOH A 512 4074 3778 4237 -436 -54 -41 O HETATM 2346 O HOH A 513 20.419 2.132 38.016 1.00 44.61 O ANISOU 2346 O HOH A 513 5786 5557 5606 -22 31 87 O HETATM 2347 O HOH A 514 23.527 0.181 35.310 1.00 30.10 O ANISOU 2347 O HOH A 514 4304 3468 3661 199 -18 354 O HETATM 2348 O HOH A 515 17.768 -0.968 38.981 1.00 42.46 O ANISOU 2348 O HOH A 515 5382 5292 5458 34 16 -62 O HETATM 2349 O HOH A 516 20.908 41.093 29.010 1.00 38.77 O ANISOU 2349 O HOH A 516 4609 5175 4944 -50 106 53 O HETATM 2350 O HOH A 517 24.702 9.254 33.642 1.00 38.55 O ANISOU 2350 O HOH A 517 4726 4905 5016 -232 -87 108 O HETATM 2351 O HOH A 518 4.177 37.663 50.855 1.00 27.73 O ANISOU 2351 O HOH A 518 3984 3697 2851 142 -438 -225 O HETATM 2352 O HOH A 519 6.593 34.173 49.727 1.00 28.26 O ANISOU 2352 O HOH A 519 3815 3490 3430 8 62 69 O HETATM 2353 O HOH A 520 4.537 28.522 20.020 1.00 25.46 O ANISOU 2353 O HOH A 520 4010 2253 3410 308 -121 -175 O HETATM 2354 O HOH A 521 5.357 28.342 52.052 1.00 29.00 O ANISOU 2354 O HOH A 521 3983 3368 3665 -47 213 280 O HETATM 2355 O HOH A 522 -1.841 25.586 52.015 1.00 38.17 O ANISOU 2355 O HOH A 522 4833 5158 4509 99 151 -54 O HETATM 2356 O HOH A 523 -3.915 23.110 14.851 1.00 56.32 O ANISOU 2356 O HOH A 523 7152 7131 7115 -32 -3 20 O HETATM 2357 O HOH A 524 -1.147 30.859 50.290 1.00 29.34 O ANISOU 2357 O HOH A 524 3302 3917 3925 135 45 173 O HETATM 2358 O HOH A 525 -3.846 42.055 22.711 1.00 46.59 O ANISOU 2358 O HOH A 525 5887 5880 5935 43 -151 -19 O HETATM 2359 O HOH A 526 19.357 44.307 31.501 1.00 38.57 O ANISOU 2359 O HOH A 526 4677 4967 5010 -162 75 84 O HETATM 2360 O HOH A 527 17.211 45.576 26.824 1.00 40.65 O ANISOU 2360 O HOH A 527 5154 4950 5341 -101 122 125 O HETATM 2361 O HOH A 528 6.590 52.251 40.736 1.00 27.16 O ANISOU 2361 O HOH A 528 3352 2317 4650 728 0 -133 O HETATM 2362 O HOH A 529 6.246 47.199 23.750 1.00 41.36 O ANISOU 2362 O HOH A 529 5360 5184 5171 63 -125 -40 O HETATM 2363 O HOH A 530 29.653 10.274 25.097 1.00 24.04 O ANISOU 2363 O HOH A 530 2350 3211 3572 -292 -170 -409 O HETATM 2364 O HOH A 531 -1.118 37.290 49.346 1.00 28.56 O ANISOU 2364 O HOH A 531 3511 4234 3106 462 95 -454 O HETATM 2365 O HOH A 532 25.918 11.045 22.180 1.00 28.22 O ANISOU 2365 O HOH A 532 3147 4002 3571 -698 323 -154 O HETATM 2366 O HOH A 533 -8.095 19.786 34.354 1.00 33.12 O ANISOU 2366 O HOH A 533 3522 4317 4744 46 169 -42 O HETATM 2367 O HOH A 534 -0.864 11.507 37.148 1.00 29.04 O ANISOU 2367 O HOH A 534 3407 3470 4157 -216 18 -34 O HETATM 2368 O HOH A 535 9.074 2.693 40.173 1.00 44.80 O ANISOU 2368 O HOH A 535 5700 5732 5589 36 80 97 O HETATM 2369 O HOH A 536 9.015 6.116 43.238 1.00 39.46 O ANISOU 2369 O HOH A 536 5074 5182 4736 45 101 51 O HETATM 2370 O HOH A 537 10.967 8.366 43.290 1.00 29.03 O ANISOU 2370 O HOH A 537 4210 3730 3089 111 288 53 O HETATM 2371 O HOH A 538 11.488 10.260 45.569 1.00 39.72 O ANISOU 2371 O HOH A 538 4803 4986 5302 80 75 48 O HETATM 2372 O HOH A 539 2.677 7.508 40.459 1.00 37.38 O ANISOU 2372 O HOH A 539 4832 4212 5158 -332 -28 202 O HETATM 2373 O HOH A 540 7.410 5.537 40.964 1.00 36.36 O ANISOU 2373 O HOH A 540 4710 4648 4455 123 1 -55 O HETATM 2374 O HOH A 541 26.845 28.768 25.403 1.00 41.60 O ANISOU 2374 O HOH A 541 5375 5113 5316 19 74 -99 O HETATM 2375 O HOH A 542 22.333 25.391 26.408 1.00 33.50 O ANISOU 2375 O HOH A 542 3885 4353 4488 -55 -116 1 O HETATM 2376 O HOH A 543 21.095 27.076 27.538 1.00 32.54 O ANISOU 2376 O HOH A 543 4458 3980 3924 -87 97 -121 O HETATM 2377 O HOH A 544 20.885 26.485 24.952 1.00 35.64 O ANISOU 2377 O HOH A 544 4602 4326 4613 -117 30 134 O HETATM 2378 O HOH A 545 27.006 12.231 31.023 1.00 34.14 O ANISOU 2378 O HOH A 545 4734 3953 4283 121 128 298 O HETATM 2379 O HOH A 546 25.725 14.093 34.191 1.00 28.76 O ANISOU 2379 O HOH A 546 3388 3243 4296 -268 20 89 O HETATM 2380 O HOH A 547 17.852 45.581 29.624 1.00 42.11 O ANISOU 2380 O HOH A 547 5433 5241 5323 -177 137 -7 O HETATM 2381 O HOH A 548 13.241 34.651 17.279 1.00 34.06 O ANISOU 2381 O HOH A 548 4815 4148 3976 -280 240 150 O HETATM 2382 O HOH A 549 -4.347 43.073 38.571 1.00 41.25 O ANISOU 2382 O HOH A 549 5067 5345 5259 334 39 162 O HETATM 2383 O HOH A 550 6.139 35.616 47.051 1.00 25.34 O ANISOU 2383 O HOH A 550 3056 3392 3179 27 -175 -134 O HETATM 2384 O HOH A 551 22.857 39.180 44.227 1.00 28.77 O ANISOU 2384 O HOH A 551 3171 3488 4272 -263 -428 -352 O HETATM 2385 O HOH A 552 6.882 43.432 46.876 1.00 35.45 O ANISOU 2385 O HOH A 552 4443 4232 4793 53 -25 -70 O HETATM 2386 O HOH A 553 0.014 10.427 39.634 1.00 33.21 O ANISOU 2386 O HOH A 553 4165 4128 4324 -38 170 116 O HETATM 2387 O HOH A 554 -3.182 12.959 43.417 1.00 41.09 O ANISOU 2387 O HOH A 554 5203 5175 5231 35 87 -65 O HETATM 2388 O HOH A 555 -5.200 21.408 22.515 1.00 41.69 O ANISOU 2388 O HOH A 555 5044 5393 5402 84 -25 56 O HETATM 2389 O HOH A 556 -6.125 12.301 23.087 1.00 33.40 O ANISOU 2389 O HOH A 556 3497 4305 4886 -267 -104 62 O HETATM 2390 O HOH A 557 24.182 21.070 14.779 1.00 44.58 O ANISOU 2390 O HOH A 557 5510 5756 5670 -76 90 42 O HETATM 2391 O HOH A 558 3.390 2.141 17.524 1.00 43.08 O ANISOU 2391 O HOH A 558 5451 5732 5186 49 -191 34 O HETATM 2392 O HOH A 559 16.887 4.057 39.145 1.00 39.94 O ANISOU 2392 O HOH A 559 5179 5211 4783 142 85 -74 O HETATM 2393 O HOH A 560 8.094 41.018 49.888 1.00 39.67 O ANISOU 2393 O HOH A 560 5191 5240 4641 -93 179 -17 O HETATM 2394 O HOH A 561 16.046 33.170 50.676 1.00 30.25 O ANISOU 2394 O HOH A 561 3872 3726 3895 -248 -185 -616 O HETATM 2395 O HOH A 562 17.113 29.785 53.658 1.00 40.98 O ANISOU 2395 O HOH A 562 5253 5047 5268 -43 -30 -50 O HETATM 2396 O HOH A 563 20.108 26.446 53.625 1.00 32.21 O ANISOU 2396 O HOH A 563 4100 4067 4070 -75 -247 316 O HETATM 2397 O HOH A 564 23.571 10.929 35.770 1.00 43.84 O ANISOU 2397 O HOH A 564 5556 5510 5590 -55 38 29 O HETATM 2398 O HOH A 565 20.429 41.687 47.833 1.00 41.08 O ANISOU 2398 O HOH A 565 5140 5401 5068 -33 -75 47 O HETATM 2399 O HOH A 566 19.065 41.752 30.837 1.00 29.39 O ANISOU 2399 O HOH A 566 3984 4014 3165 -86 317 -28 O HETATM 2400 O HOH A 567 13.564 47.239 47.538 1.00 36.04 O ANISOU 2400 O HOH A 567 4721 4358 4612 -35 23 -131 O HETATM 2401 O HOH A 568 -6.302 44.304 32.111 1.00 42.45 O ANISOU 2401 O HOH A 568 5346 5273 5511 -77 -133 -26 O HETATM 2402 O HOH A 569 0.492 3.259 18.248 1.00 45.62 O ANISOU 2402 O HOH A 569 5727 5751 5853 -62 -82 -30 O HETATM 2403 O HOH A 570 4.348 1.327 31.462 1.00 39.60 O ANISOU 2403 O HOH A 570 4945 4989 5111 -92 -51 -26 O HETATM 2404 O HOH A 571 16.125 37.465 52.143 1.00 38.39 O ANISOU 2404 O HOH A 571 5012 4647 4925 -248 -95 19 O HETATM 2405 O HOH A 572 -2.914 24.382 25.771 1.00 30.99 O ANISOU 2405 O HOH A 572 3541 4150 4082 -44 -585 -247 O HETATM 2406 O HOH A 573 18.073 36.705 19.943 1.00 44.08 O ANISOU 2406 O HOH A 573 5475 5633 5638 -66 113 0 O HETATM 2407 O HOH A 574 12.777 46.910 38.564 1.00 28.74 O ANISOU 2407 O HOH A 574 3059 4285 3574 -99 317 -42 O HETATM 2408 O HOH A 575 14.648 48.827 32.586 1.00 29.92 O ANISOU 2408 O HOH A 575 4286 2683 4398 -484 424 199 O HETATM 2409 O HOH A 576 -1.645 38.377 20.973 1.00 42.67 O ANISOU 2409 O HOH A 576 5375 5558 5277 101 -117 7 O HETATM 2410 O HOH A 577 -6.482 41.934 35.326 1.00 33.77 O ANISOU 2410 O HOH A 577 3891 4483 4454 185 280 147 O HETATM 2411 O HOH A 578 -2.767 11.704 38.720 1.00 44.18 O ANISOU 2411 O HOH A 578 5644 5530 5612 -115 -39 -132 O HETATM 2412 O HOH A 579 24.663 16.403 19.984 1.00 28.42 O ANISOU 2412 O HOH A 579 2326 4222 4250 315 346 186 O HETATM 2413 O HOH A 580 21.635 7.347 17.869 1.00 35.69 O ANISOU 2413 O HOH A 580 4365 4499 4694 47 -1 141 O HETATM 2414 O HOH A 581 25.510 33.576 36.994 1.00 35.81 O ANISOU 2414 O HOH A 581 4004 4952 4649 91 371 -39 O HETATM 2415 O HOH A 582 9.556 37.980 52.626 1.00 30.88 O ANISOU 2415 O HOH A 582 4287 4267 3178 -97 134 232 O HETATM 2416 O HOH A 583 15.703 37.347 18.891 1.00 39.80 O ANISOU 2416 O HOH A 583 5138 5029 4955 -72 70 56 O HETATM 2417 O HOH A 584 5.127 50.185 31.811 1.00 36.95 O ANISOU 2417 O HOH A 584 4831 5082 4126 64 218 -98 O HETATM 2418 O HOH A 585 -4.563 41.560 25.295 1.00 45.93 O ANISOU 2418 O HOH A 585 5796 5807 5848 43 -84 75 O HETATM 2419 O HOH A 586 11.049 -1.038 19.442 1.00 33.79 O ANISOU 2419 O HOH A 586 4478 3790 4568 56 -16 -236 O HETATM 2420 O HOH A 587 17.003 6.744 43.255 1.00 42.04 O ANISOU 2420 O HOH A 587 5163 5202 5606 -53 -41 95 O HETATM 2421 O HOH A 588 -0.939 12.117 10.088 1.00 41.27 O ANISOU 2421 O HOH A 588 5281 5184 5213 -152 59 4 O HETATM 2422 O HOH A 589 27.152 24.595 24.851 1.00 35.75 O ANISOU 2422 O HOH A 589 3942 4802 4838 -96 -71 -13 O HETATM 2423 O HOH A 590 3.142 9.690 45.262 1.00 42.35 O ANISOU 2423 O HOH A 590 5304 5440 5345 31 165 175 O HETATM 2424 O HOH A 591 18.151 4.395 41.428 1.00 47.46 O ANISOU 2424 O HOH A 591 6010 6058 5962 -53 -36 0 O HETATM 2425 O HOH A 592 -8.983 18.616 30.659 1.00 43.44 O ANISOU 2425 O HOH A 592 5394 5548 5562 -103 -77 -44 O HETATM 2426 O HOH A 593 2.842 -0.548 20.136 1.00 34.86 O ANISOU 2426 O HOH A 593 4265 4424 4554 -169 -210 -51 O HETATM 2427 O HOH A 594 2.441 -3.448 20.817 1.00 42.80 O ANISOU 2427 O HOH A 594 5434 5438 5391 -62 -95 16 O HETATM 2428 O HOH A 595 8.025 -4.060 18.536 1.00 50.57 O ANISOU 2428 O HOH A 595 6550 6277 6387 -62 -65 -72 O HETATM 2429 O HOH A 596 19.217 5.395 18.758 1.00 39.60 O ANISOU 2429 O HOH A 596 5078 4821 5145 65 36 -90 O HETATM 2430 O HOH A 597 20.574 31.982 33.187 0.50 16.79 O ANISOU 2430 O HOH A 597 1908 1681 2790 -232 148 15 O HETATM 2431 O HOH A 598 -8.242 34.449 33.568 1.00 29.04 O ANISOU 2431 O HOH A 598 3215 3733 4086 136 -13 308 O HETATM 2432 O HOH A 599 -2.971 12.456 30.506 1.00 26.74 O ANISOU 2432 O HOH A 599 3198 3529 3433 -123 -28 -47 O HETATM 2433 O HOH A 600 3.710 2.634 33.735 1.00 49.46 O ANISOU 2433 O HOH A 600 6374 6134 6284 -21 6 77 O HETATM 2434 O HOH A 601 25.736 22.042 10.266 1.00 43.51 O ANISOU 2434 O HOH A 601 5461 5630 5438 -4 -30 -1 O HETATM 2435 O HOH A 602 23.121 23.795 31.158 1.00 22.02 O ANISOU 2435 O HOH A 602 2645 3249 2470 573 359 -5 O CONECT 293 1277 CONECT 699 929 CONECT 929 699 CONECT 1277 293 CONECT 1492 2063 CONECT 2063 1492 MASTER 310 0 0 14 0 0 0 6 2434 1 6 20 END