Browse entries in the PDBbind-CN Database
HEADER GENE REGULATION/RNA 27-OCT-10 3PF4 TITLE CRYSTAL STRUCTURE OF BS-CSPB IN COMPLEX WITH R(GUCUUUA) COMPND MOL_ID: 1; COMPND 2 MOLECULE: COLD SHOCK PROTEIN CSPB; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: MAJOR COLD SHOCK PROTEIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: HEXARIBONUCLEOTIDE (RGUCUUUA); COMPND 8 CHAIN: R; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 GENE: BSU09100, CSPA, CSPB; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11; SOURCE 10 MOL_ID: 2; SOURCE 11 SYNTHETIC: YES; SOURCE 12 OTHER_DETAILS: CHEMICALLY SYNTHESIZED KEYWDS BETA BARREL, PROTEIN-RNA COMPLEX, COLD SHOCK RESPONSE, TRANSCRIPTION KEYWDS 2 REGULATION, TRANSLATION REGULATION, OB FOLD, COLD SHOCK DOMAIN, KEYWDS 3 RNA/DNA BINDING, SINGLE-STRANDED RNA AND DNA, CYTOSOL, GENE KEYWDS 4 REGULATION-RNA COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR R.SACHS,K.E.A.MAX,U.HEINEMANN REVDAT 3 28-DEC-11 3PF4 1 JRNL REVDAT 2 14-DEC-11 3PF4 1 JRNL REVDAT 1 21-SEP-11 3PF4 0 JRNL AUTH R.SACHS,K.E.MAX,U.HEINEMANN,J.BALBACH JRNL TITL RNA SINGLE STRANDS BIND TO A CONSERVED SURFACE OF THE MAJOR JRNL TITL 2 COLD SHOCK PROTEIN IN CRYSTALS AND SOLUTION. JRNL REF RNA V. 18 65 2012 JRNL REFN ISSN 1355-8382 JRNL PMID 22128343 JRNL DOI 10.1261/RNA.02809212 REMARK 2 REMARK 2 RESOLUTION. 1.38 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0072 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.38 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.02 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : NULL REMARK 3 NUMBER OF REFLECTIONS : 30207 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) : 0.156 REMARK 3 R VALUE (WORKING SET) : 0.154 REMARK 3 FREE R VALUE : 0.194 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1511 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.38 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.42 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2063 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2110 REMARK 3 BIN FREE R VALUE SET COUNT : 109 REMARK 3 BIN FREE R VALUE : 0.2550 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1030 REMARK 3 NUCLEIC ACID ATOMS : 97 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 194 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 22.78 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.25 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.01000 REMARK 3 B22 (A**2) : 0.10000 REMARK 3 B33 (A**2) : -0.10000 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): 0.063 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.060 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.077 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1225 ; 0.017 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): 803 ; 0.001 ; 0.020 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1678 ; 1.634 ; 2.053 REMARK 3 BOND ANGLES OTHERS (DEGREES): 1978 ; 0.865 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 146 ; 5.844 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 60 ;35.564 ;26.333 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 193 ;11.977 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 2 ;20.246 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 181 ; 0.099 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1329 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 245 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 669 ; 2.234 ; 2.000 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 287 ; 1.144 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1072 ; 3.291 ; 3.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 556 ; 4.185 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 599 ; 5.907 ; 6.000 REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2028 ; 2.010 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 199 ; 8.931 ; 3.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 1989 ; 4.260 ; 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 : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS REMARK 3 U VALUES : REFINED INDIVIDUALLY REMARK 4 REMARK 4 3PF4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-10. REMARK 100 THE RCSB ID CODE IS RCSB062301. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JUL-09 REMARK 200 TEMPERATURE (KELVIN) : 110 REMARK 200 PH : 8.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : BESSY REMARK 200 BEAMLINE : 14.2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184 REMARK 200 MONOCHROMATOR : SI-(111) CRYSTAL REMARK 200 OPTICS : MIRRORS DOUBLE CRYSTAL REMARK 200 MONOCHROMATOR (SI-111 CRYSTALS) REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30207 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.380 REMARK 200 RESOLUTION RANGE LOW (A) : 19.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 4.740 REMARK 200 R MERGE (I) : 0.03900 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7300 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.38 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 4.72 REMARK 200 R MERGE FOR SHELL (I) : 0.59000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 1CSP REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.19 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN BUFFER: 50MM TRIS, 20MM NA- REMARK 280 HEPES, PH 7.5; BS-CSPB.RGUCUUUA COMPLEX CONCENTRATION: 50MG/ML; REMARK 280 CRYSTALLIZATION BUFFER: 30% (W/V) PEG 4000, 0.2M MGCL2, 0.1M TRIS REMARK 280 PH 8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 24.63750 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.90100 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.25600 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.90100 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.63750 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.25600 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 890 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 5080 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, R 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 ALA A 67 REMARK 465 ALA B 67 REMARK 465 G R 0 REMARK 465 A R 6 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 U R 1 P OP1 OP2 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A 69 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 160 O REMARK 620 2 HOH A 115 O 94.5 REMARK 620 3 HOH A 127 O 85.9 93.0 REMARK 620 4 HOH A 122 O 89.1 89.5 174.6 REMARK 620 5 HOH A 92 O 179.1 85.8 93.3 91.7 REMARK 620 6 HOH A 131 O 88.0 174.8 91.8 86.0 91.7 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A 68 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLY A 37 O REMARK 620 2 GLY A 35 O 120.4 REMARK 620 N 1 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 68 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 69 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CSP RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS MAJOR COLD SHOCK REMARK 900 PROTEIN, CSPB: A UNIVERSAL NUCLEIC-ACID BINDING DOMAIN REMARK 900 RELATED ID: 2HAX RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF BACILLUS CALDOLYTICUS COLD SHOCK REMARK 900 PROTEIN IN COMPLEX WITH HEXATHYMIDINE REMARK 900 RELATED ID: 2ES2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS SUBTILIS COLD REMARK 900 SHOCK PROTEIN BS-CSPB IN COMPLEX WITH HEXATHYMIDINE REMARK 900 RELATED ID: 2F52 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF COLD SHOCK PROTEIN CSPB FROM BACILLUS REMARK 900 SUBTILIS IN COMPLEX WITH HEPTATHYMIDINE REMARK 900 RELATED ID: 1C9O RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS CALDOLYTICUS REMARK 900 COLD SHOCK PROTEIN BC-CSP DBREF 3PF4 A 1 67 UNP P32081 CSPB_BACSU 1 67 DBREF 3PF4 B 1 67 UNP P32081 CSPB_BACSU 1 67 DBREF 3PF4 R 0 6 PDB 3PF4 3PF4 0 6 SEQRES 1 A 67 MET LEU GLU GLY LYS VAL LYS TRP PHE ASN SER GLU LYS SEQRES 2 A 67 GLY PHE GLY PHE ILE GLU VAL GLU GLY GLN ASP ASP VAL SEQRES 3 A 67 PHE VAL HIS PHE SER ALA ILE GLN GLY GLU GLY PHE LYS SEQRES 4 A 67 THR LEU GLU GLU GLY GLN ALA VAL SER PHE GLU ILE VAL SEQRES 5 A 67 GLU GLY ASN ARG GLY PRO GLN ALA ALA ASN VAL THR LYS SEQRES 6 A 67 GLU ALA SEQRES 1 B 67 MET LEU GLU GLY LYS VAL LYS TRP PHE ASN SER GLU LYS SEQRES 2 B 67 GLY PHE GLY PHE ILE GLU VAL GLU GLY GLN ASP ASP VAL SEQRES 3 B 67 PHE VAL HIS PHE SER ALA ILE GLN GLY GLU GLY PHE LYS SEQRES 4 B 67 THR LEU GLU GLU GLY GLN ALA VAL SER PHE GLU ILE VAL SEQRES 5 B 67 GLU GLY ASN ARG GLY PRO GLN ALA ALA ASN VAL THR LYS SEQRES 6 B 67 GLU ALA SEQRES 1 R 7 G U C U U U A HET NA A 68 1 HET MG A 69 1 HETNAM NA SODIUM ION HETNAM MG MAGNESIUM ION FORMUL 4 NA NA 1+ FORMUL 5 MG MG 2+ FORMUL 6 HOH *194(H2 O) HELIX 1 1 SER A 31 ILE A 33 5 3 HELIX 2 2 SER B 31 ILE B 33 5 3 SHEET 1 A 5 VAL A 26 HIS A 29 0 SHEET 2 A 5 PHE A 15 GLU A 19 -1 N ILE A 18 O VAL A 26 SHEET 3 A 5 LEU A 2 ASN A 10 -1 N LYS A 5 O GLU A 19 SHEET 4 A 5 ALA A 46 GLY A 54 -1 O PHE A 49 N LEU A 2 SHEET 5 A 5 GLY A 57 LYS A 65 -1 O GLN A 59 N VAL A 52 SHEET 1 B 5 VAL B 26 HIS B 29 0 SHEET 2 B 5 PHE B 15 GLU B 19 -1 N ILE B 18 O VAL B 26 SHEET 3 B 5 LEU B 2 ASN B 10 -1 N ASN B 10 O PHE B 15 SHEET 4 B 5 ALA B 46 GLY B 54 -1 O PHE B 49 N LEU B 2 SHEET 5 B 5 GLY B 57 LYS B 65 -1 O GLN B 59 N VAL B 52 LINK MG MG A 69 O HOH A 160 1555 1555 1.99 LINK MG MG A 69 O HOH A 115 1555 1555 2.00 LINK MG MG A 69 O HOH A 127 1555 1555 2.04 LINK MG MG A 69 O HOH A 122 1555 1555 2.06 LINK MG MG A 69 O HOH A 92 1555 1555 2.18 LINK MG MG A 69 O HOH A 131 1555 1555 2.18 LINK O GLY A 37 NA NA A 68 1555 1555 2.62 LINK O GLY A 35 NA NA A 68 1555 1555 3.08 SITE 1 AC1 4 GLY A 35 GLU A 36 GLY A 37 LYS A 39 SITE 1 AC2 6 HOH A 92 HOH A 115 HOH A 122 HOH A 127 SITE 2 AC2 6 HOH A 131 HOH A 160 CRYST1 49.275 50.512 57.802 90.00 90.00 90.00 P 21 21 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.020294 0.000000 0.000000 0.00000 SCALE2 0.000000 0.019797 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017300 0.00000 ATOM 1 N MET A 1 24.159 14.416 -4.217 1.00 22.14 N ANISOU 1 N MET A 1 2508 3103 2799 -95 606 -101 N ATOM 2 CA MET A 1 23.608 13.260 -3.387 1.00 21.01 C ANISOU 2 CA MET A 1 2559 2981 2439 -5 434 13 C ATOM 3 C MET A 1 24.656 12.588 -2.569 1.00 20.21 C ANISOU 3 C MET A 1 2389 2687 2601 9 367 1 C ATOM 4 O MET A 1 25.654 12.050 -3.038 1.00 21.65 O ANISOU 4 O MET A 1 2572 2810 2843 137 649 67 O ATOM 5 CB MET A 1 22.890 12.158 -4.157 1.00 22.96 C ANISOU 5 CB MET A 1 2959 3136 2628 167 438 -195 C ATOM 6 CG MET A 1 21.849 12.627 -5.123 1.00 28.17 C ANISOU 6 CG MET A 1 3704 3622 3376 75 26 -4 C ATOM 7 SD MET A 1 20.382 13.272 -4.355 1.00 35.51 S ANISOU 7 SD MET A 1 4204 4966 4319 67 12 240 S ATOM 8 CE MET A 1 19.980 11.861 -3.368 1.00 27.13 C ANISOU 8 CE MET A 1 3768 3680 2858 138 266 -205 C ATOM 9 N LEU A 2 24.351 12.539 -1.304 1.00 18.47 N ANISOU 9 N LEU A 2 2327 2390 2300 -9 448 -20 N ATOM 10 CA LEU A 2 25.175 11.960 -0.303 1.00 18.94 C ANISOU 10 CA LEU A 2 2154 2385 2654 43 255 -211 C ATOM 11 C LEU A 2 24.913 10.504 -0.153 1.00 19.04 C ANISOU 11 C LEU A 2 2234 2408 2591 109 283 -71 C ATOM 12 O LEU A 2 23.874 10.026 -0.554 1.00 18.69 O ANISOU 12 O LEU A 2 1960 2411 2730 241 299 -251 O ATOM 13 CB LEU A 2 24.849 12.681 1.041 1.00 18.14 C ANISOU 13 CB LEU A 2 2446 2346 2099 230 381 -94 C ATOM 14 CG LEU A 2 25.067 14.213 1.069 1.00 23.98 C ANISOU 14 CG LEU A 2 2976 2968 3165 -48 173 -1 C ATOM 15 CD1 LEU A 2 24.609 14.808 2.397 1.00 25.80 C ANISOU 15 CD1 LEU A 2 3376 2903 3524 107 208 -276 C ATOM 16 CD2 LEU A 2 26.502 14.554 0.826 1.00 24.57 C ANISOU 16 CD2 LEU A 2 3164 3008 3162 -529 110 149 C ATOM 17 N GLU A 3 25.863 9.802 0.448 1.00 22.35 N ANISOU 17 N GLU A 3 2570 2740 3181 101 170 -47 N ATOM 18 CA GLU A 3 25.749 8.352 0.633 1.00 22.50 C ANISOU 18 CA GLU A 3 2723 2697 3127 237 159 -20 C ATOM 19 C GLU A 3 25.998 8.019 2.096 1.00 21.90 C ANISOU 19 C GLU A 3 2586 2651 3083 213 94 -30 C ATOM 20 O GLU A 3 26.858 8.635 2.746 1.00 22.94 O ANISOU 20 O GLU A 3 2723 2878 3115 -183 10 278 O ATOM 21 CB GLU A 3 26.775 7.630 -0.277 1.00 25.52 C ANISOU 21 CB GLU A 3 3325 3094 3276 184 196 -120 C ATOM 22 CG GLU A 3 26.507 7.810 -1.741 1.00 28.40 C ANISOU 22 CG GLU A 3 3817 3593 3377 178 127 -66 C ATOM 23 CD GLU A 3 27.701 7.455 -2.625 0.50 30.77 C ANISOU 23 CD GLU A 3 3789 3974 3927 175 81 -14 C ATOM 24 OE1 GLU A 3 28.564 6.634 -2.211 0.50 32.71 O ANISOU 24 OE1 GLU A 3 3988 4153 4285 314 193 21 O ATOM 25 OE2 GLU A 3 27.770 8.019 -3.736 0.50 34.17 O ANISOU 25 OE2 GLU A 3 4425 4346 4212 -3 64 -26 O ATOM 26 N GLY A 4 25.267 7.045 2.620 1.00 19.66 N ANISOU 26 N GLY A 4 2273 2543 2654 291 -39 -31 N ATOM 27 CA GLY A 4 25.503 6.584 3.967 1.00 19.90 C ANISOU 27 CA GLY A 4 2336 2474 2748 210 -24 -13 C ATOM 28 C GLY A 4 24.775 5.282 4.168 1.00 17.54 C ANISOU 28 C GLY A 4 1983 2149 2531 374 -146 42 C ATOM 29 O GLY A 4 24.411 4.583 3.199 1.00 19.09 O ANISOU 29 O GLY A 4 2278 2111 2865 318 -201 -143 O ATOM 30 N LYS A 5 24.572 4.939 5.428 1.00 17.79 N ANISOU 30 N LYS A 5 1876 2280 2602 339 -143 -17 N ATOM 31 CA LYS A 5 23.840 3.726 5.740 1.00 16.24 C ANISOU 31 CA LYS A 5 1742 1964 2463 365 -43 -72 C ATOM 32 C LYS A 5 22.946 3.962 6.926 1.00 16.13 C ANISOU 32 C LYS A 5 1871 1988 2269 332 -127 35 C ATOM 33 O LYS A 5 23.210 4.817 7.747 1.00 18.06 O ANISOU 33 O LYS A 5 2101 2137 2624 196 -125 -117 O ATOM 34 CB LYS A 5 24.793 2.514 5.959 1.00 20.75 C ANISOU 34 CB LYS A 5 2532 2524 2826 393 90 -38 C ATOM 35 CG LYS A 5 25.591 2.471 7.190 1.00 21.64 C ANISOU 35 CG LYS A 5 2576 2467 3176 423 99 -379 C ATOM 36 CD LYS A 5 26.416 1.161 7.289 1.00 21.10 C ANISOU 36 CD LYS A 5 2497 2474 3045 751 -118 -56 C ATOM 37 CE LYS A 5 27.242 1.163 8.549 1.00 23.61 C ANISOU 37 CE LYS A 5 2740 3056 3174 670 71 -110 C ATOM 38 NZ LYS A 5 28.145 -0.029 8.567 1.00 30.59 N ANISOU 38 NZ LYS A 5 3958 3189 4474 863 51 -155 N ATOM 39 N VAL A 6 21.904 3.174 7.050 1.00 15.43 N ANISOU 39 N VAL A 6 1801 1879 2180 272 -222 -52 N ATOM 40 CA VAL A 6 20.953 3.332 8.126 1.00 15.74 C ANISOU 40 CA VAL A 6 1941 1911 2127 294 -262 -141 C ATOM 41 C VAL A 6 21.594 2.827 9.423 1.00 15.09 C ANISOU 41 C VAL A 6 1851 1715 2167 429 -355 -27 C ATOM 42 O VAL A 6 21.978 1.654 9.538 1.00 17.29 O ANISOU 42 O VAL A 6 2361 1672 2534 639 -468 -76 O ATOM 43 CB VAL A 6 19.628 2.591 7.800 1.00 15.91 C ANISOU 43 CB VAL A 6 2076 1790 2177 242 -146 -2 C ATOM 44 CG1 VAL A 6 18.661 2.650 8.986 1.00 16.20 C ANISOU 44 CG1 VAL A 6 1799 2221 2134 172 75 -14 C ATOM 45 CG2 VAL A 6 19.007 3.151 6.466 1.00 17.65 C ANISOU 45 CG2 VAL A 6 2221 2177 2308 239 -359 113 C ATOM 46 N LYS A 7 21.718 3.712 10.393 1.00 15.04 N ANISOU 46 N LYS A 7 1969 1915 1828 480 -374 60 N ATOM 47 CA LYS A 7 22.238 3.357 11.696 1.00 17.25 C ANISOU 47 CA LYS A 7 2107 2139 2309 341 -386 137 C ATOM 48 C LYS A 7 21.240 2.543 12.509 1.00 17.99 C ANISOU 48 C LYS A 7 2294 2123 2418 285 -198 160 C ATOM 49 O LYS A 7 21.577 1.569 13.139 1.00 21.58 O ANISOU 49 O LYS A 7 2825 2440 2933 438 -492 405 O ATOM 50 CB LYS A 7 22.586 4.622 12.444 1.00 17.70 C ANISOU 50 CB LYS A 7 2144 2213 2367 379 -245 47 C ATOM 51 CG LYS A 7 23.450 4.478 13.680 1.00 18.50 C ANISOU 51 CG LYS A 7 2357 2366 2304 99 -459 155 C ATOM 52 CD LYS A 7 23.780 5.824 14.307 1.00 19.36 C ANISOU 52 CD LYS A 7 2410 2566 2376 272 -300 235 C ATOM 53 CE LYS A 7 24.813 5.653 15.403 1.00 20.35 C ANISOU 53 CE LYS A 7 2770 2624 2338 606 -424 211 C ATOM 54 NZ LYS A 7 25.032 6.858 16.187 1.00 22.29 N ANISOU 54 NZ LYS A 7 3062 2851 2554 123 -648 71 N ATOM 55 N TRP A 8 20.008 3.007 12.542 1.00 15.98 N ANISOU 55 N TRP A 8 1903 1805 2363 305 -322 318 N ATOM 56 CA TRP A 8 18.901 2.312 13.140 1.00 17.99 C ANISOU 56 CA TRP A 8 2175 2127 2533 218 -250 295 C ATOM 57 C TRP A 8 17.630 2.949 12.583 1.00 16.60 C ANISOU 57 C TRP A 8 1877 2023 2406 53 -250 145 C ATOM 58 O TRP A 8 17.649 4.098 12.068 1.00 16.26 O ANISOU 58 O TRP A 8 2309 1614 2255 70 -537 176 O ATOM 59 CB TRP A 8 18.931 2.402 14.660 1.00 18.20 C ANISOU 59 CB TRP A 8 1878 2332 2705 30 -237 243 C ATOM 60 CG TRP A 8 18.812 3.742 15.244 1.00 17.26 C ANISOU 60 CG TRP A 8 2329 2202 2026 35 -280 347 C ATOM 61 CD1 TRP A 8 19.850 4.560 15.595 1.00 18.90 C ANISOU 61 CD1 TRP A 8 2275 2670 2234 122 -318 100 C ATOM 62 CD2 TRP A 8 17.608 4.441 15.609 1.00 18.54 C ANISOU 62 CD2 TRP A 8 2566 2578 1900 -14 -313 391 C ATOM 63 NE1 TRP A 8 19.371 5.706 16.144 1.00 22.68 N ANISOU 63 NE1 TRP A 8 2752 2881 2982 209 62 192 N ATOM 64 CE2 TRP A 8 18.005 5.663 16.166 1.00 20.60 C ANISOU 64 CE2 TRP A 8 2956 2413 2455 -98 -49 250 C ATOM 65 CE3 TRP A 8 16.237 4.167 15.500 1.00 17.60 C ANISOU 65 CE3 TRP A 8 2449 2371 1866 200 2 501 C ATOM 66 CZ2 TRP A 8 17.102 6.595 16.624 1.00 18.70 C ANISOU 66 CZ2 TRP A 8 2596 2628 1880 203 -158 276 C ATOM 67 CZ3 TRP A 8 15.331 5.120 15.988 1.00 20.20 C ANISOU 67 CZ3 TRP A 8 2756 2737 2179 81 -41 220 C ATOM 68 CH2 TRP A 8 15.770 6.288 16.532 1.00 18.65 C ANISOU 68 CH2 TRP A 8 2565 2334 2187 368 74 261 C ATOM 69 N PHE A 9 16.551 2.191 12.631 1.00 16.79 N ANISOU 69 N PHE A 9 2101 1604 2674 3 -231 264 N ATOM 70 CA PHE A 9 15.257 2.684 12.181 1.00 16.70 C ANISOU 70 CA PHE A 9 1958 1954 2431 46 -25 167 C ATOM 71 C PHE A 9 14.150 1.979 12.951 1.00 17.62 C ANISOU 71 C PHE A 9 2367 1818 2506 -169 -108 370 C ATOM 72 O PHE A 9 14.052 0.754 12.896 1.00 21.47 O ANISOU 72 O PHE A 9 2855 1773 3530 -403 32 242 O ATOM 73 CB PHE A 9 15.093 2.463 10.657 1.00 17.04 C ANISOU 73 CB PHE A 9 2108 1831 2533 -6 -179 159 C ATOM 74 CG PHE A 9 13.962 3.245 10.057 1.00 15.98 C ANISOU 74 CG PHE A 9 1992 1920 2160 22 -14 -29 C ATOM 75 CD1 PHE A 9 14.129 4.575 9.715 1.00 16.23 C ANISOU 75 CD1 PHE A 9 2250 1635 2282 179 -243 36 C ATOM 76 CD2 PHE A 9 12.737 2.642 9.802 1.00 15.02 C ANISOU 76 CD2 PHE A 9 1952 1438 2317 -75 39 -66 C ATOM 77 CE1 PHE A 9 13.094 5.298 9.150 1.00 15.26 C ANISOU 77 CE1 PHE A 9 2063 2045 1687 -8 59 165 C ATOM 78 CE2 PHE A 9 11.680 3.368 9.247 1.00 15.60 C ANISOU 78 CE2 PHE A 9 1781 2128 2019 -144 -148 150 C ATOM 79 CZ PHE A 9 11.876 4.707 8.928 1.00 15.50 C ANISOU 79 CZ PHE A 9 2066 2109 1714 169 -206 77 C ATOM 80 N ASN A 10 13.322 2.762 13.632 1.00 17.67 N ANISOU 80 N ASN A 10 2364 2023 2325 -236 -82 385 N ATOM 81 CA ASN A 10 12.083 2.310 14.322 1.00 18.67 C ANISOU 81 CA ASN A 10 2451 2233 2408 -224 86 289 C ATOM 82 C ASN A 10 11.029 2.163 13.244 1.00 18.86 C ANISOU 82 C ASN A 10 2401 2282 2481 -289 96 97 C ATOM 83 O ASN A 10 10.494 3.158 12.773 1.00 17.91 O ANISOU 83 O ASN A 10 2234 2594 1975 -200 48 -33 O ATOM 84 CB ASN A 10 11.688 3.366 15.362 1.00 20.82 C ANISOU 84 CB ASN A 10 2708 2847 2356 -339 186 219 C ATOM 85 CG ASN A 10 10.361 3.089 16.073 1.00 22.03 C ANISOU 85 CG ASN A 10 2889 3101 2381 -419 242 43 C ATOM 86 OD1 ASN A 10 9.431 2.457 15.550 1.00 25.39 O ANISOU 86 OD1 ASN A 10 3358 3653 2632 -1012 226 140 O ATOM 87 ND2 ASN A 10 10.271 3.591 17.318 1.00 25.80 N ANISOU 87 ND2 ASN A 10 3753 3702 2347 -291 108 -176 N ATOM 88 N SER A 11 10.741 0.936 12.801 1.00 21.03 N ANISOU 88 N SER A 11 2765 2488 2736 -311 -6 265 N ATOM 89 CA ASER A 11 9.810 0.772 11.678 0.50 21.44 C ANISOU 89 CA ASER A 11 2767 2546 2833 -254 -64 53 C ATOM 90 CA BSER A 11 9.815 0.767 11.688 0.50 21.73 C ANISOU 90 CA BSER A 11 2799 2555 2899 -288 -57 68 C ATOM 91 C SER A 11 8.368 1.052 12.094 1.00 20.53 C ANISOU 91 C SER A 11 2753 2352 2694 -335 -18 -14 C ATOM 92 O SER A 11 7.571 1.471 11.269 1.00 21.14 O ANISOU 92 O SER A 11 2602 2651 2778 -331 -123 149 O ATOM 93 CB ASER A 11 9.907 -0.615 11.044 0.50 22.59 C ANISOU 93 CB ASER A 11 2907 2738 2936 -165 -84 5 C ATOM 94 CB BSER A 11 9.910 -0.642 11.162 0.50 23.15 C ANISOU 94 CB BSER A 11 2976 2763 3055 -193 -60 16 C ATOM 95 OG ASER A 11 9.079 -0.709 9.883 0.50 22.55 O ANISOU 95 OG ASER A 11 2955 2876 2736 260 -161 67 O ATOM 96 OG BSER A 11 9.606 -1.525 12.210 0.50 25.14 O ANISOU 96 OG BSER A 11 3285 2812 3454 -228 -64 272 O ATOM 97 N GLU A 12 8.017 0.805 13.360 1.00 20.96 N ANISOU 97 N GLU A 12 2696 2331 2934 -643 40 78 N ATOM 98 CA GLU A 12 6.650 1.040 13.814 1.00 22.75 C ANISOU 98 CA GLU A 12 2897 2789 2956 -343 35 76 C ATOM 99 C GLU A 12 6.246 2.507 13.686 1.00 21.07 C ANISOU 99 C GLU A 12 2642 2665 2696 -389 74 205 C ATOM 100 O GLU A 12 5.275 2.835 13.020 1.00 22.83 O ANISOU 100 O GLU A 12 2642 2747 3282 -545 205 217 O ATOM 101 CB GLU A 12 6.516 0.599 15.265 1.00 24.20 C ANISOU 101 CB GLU A 12 3198 3052 2943 -360 124 181 C ATOM 102 CG GLU A 12 5.162 0.847 15.929 1.00 29.85 C ANISOU 102 CG GLU A 12 3497 3988 3854 -12 -45 22 C ATOM 103 CD GLU A 12 5.254 0.736 17.445 0.50 32.32 C ANISOU 103 CD GLU A 12 4130 4239 3911 -1 88 40 C ATOM 104 OE1 GLU A 12 5.548 -0.370 17.934 0.50 36.82 O ANISOU 104 OE1 GLU A 12 4738 4577 4674 91 72 161 O ATOM 105 OE2 GLU A 12 5.065 1.753 18.149 0.50 34.40 O ANISOU 105 OE2 GLU A 12 4485 4407 4176 43 151 -96 O ATOM 106 N LYS A 13 7.074 3.405 14.229 1.00 22.01 N ANISOU 106 N LYS A 13 2761 2771 2831 -515 249 76 N ATOM 107 CA LYS A 13 6.801 4.847 14.099 1.00 21.52 C ANISOU 107 CA LYS A 13 2716 2690 2771 -250 146 115 C ATOM 108 C LYS A 13 7.324 5.460 12.787 1.00 18.78 C ANISOU 108 C LYS A 13 2255 2193 2686 -127 173 44 C ATOM 109 O LYS A 13 6.824 6.511 12.276 1.00 21.94 O ANISOU 109 O LYS A 13 2547 2769 3019 34 223 79 O ATOM 110 CB LYS A 13 7.413 5.604 15.282 1.00 23.49 C ANISOU 110 CB LYS A 13 3104 2811 3010 -395 13 14 C ATOM 111 CG LYS A 13 6.794 5.322 16.644 1.00 25.24 C ANISOU 111 CG LYS A 13 3365 2962 3264 -381 44 7 C ATOM 112 CD LYS A 13 5.381 5.951 16.726 1.00 30.33 C ANISOU 112 CD LYS A 13 3808 4008 3708 -106 207 66 C ATOM 113 CE LYS A 13 4.667 5.711 18.067 1.00 30.62 C ANISOU 113 CE LYS A 13 4003 3986 3644 1 137 -105 C ATOM 114 NZ LYS A 13 3.197 5.992 17.861 1.00 35.15 N ANISOU 114 NZ LYS A 13 4322 4342 4688 -35 -19 -442 N ATOM 115 N GLY A 14 8.349 4.843 12.244 1.00 16.29 N ANISOU 115 N GLY A 14 1851 1900 2435 -384 179 -144 N ATOM 116 CA GLY A 14 8.868 5.311 10.986 1.00 15.35 C ANISOU 116 CA GLY A 14 1817 2025 1990 -328 25 -13 C ATOM 117 C GLY A 14 9.891 6.448 11.056 1.00 14.59 C ANISOU 117 C GLY A 14 1706 1946 1889 -264 28 28 C ATOM 118 O GLY A 14 9.816 7.380 10.286 1.00 14.45 O ANISOU 118 O GLY A 14 1565 2053 1871 -67 -103 -76 O ATOM 119 N PHE A 15 10.897 6.283 11.918 1.00 13.11 N ANISOU 119 N PHE A 15 1517 1830 1634 -215 162 103 N ATOM 120 CA PHE A 15 12.012 7.209 11.933 1.00 13.32 C ANISOU 120 CA PHE A 15 1751 1669 1638 -243 28 59 C ATOM 121 C PHE A 15 13.276 6.537 12.426 1.00 13.28 C ANISOU 121 C PHE A 15 1723 1744 1576 -211 -126 123 C ATOM 122 O PHE A 15 13.213 5.468 13.035 1.00 14.83 O ANISOU 122 O PHE A 15 2041 1830 1763 -323 -130 336 O ATOM 123 CB PHE A 15 11.683 8.463 12.763 1.00 14.77 C ANISOU 123 CB PHE A 15 1745 1864 2003 -155 -43 -4 C ATOM 124 CG PHE A 15 11.404 8.195 14.198 1.00 15.12 C ANISOU 124 CG PHE A 15 1993 1723 2027 21 -83 -210 C ATOM 125 CD1 PHE A 15 12.437 7.959 15.073 1.00 17.86 C ANISOU 125 CD1 PHE A 15 2257 2695 1833 242 221 178 C ATOM 126 CD2 PHE A 15 10.113 8.223 14.695 1.00 17.61 C ANISOU 126 CD2 PHE A 15 2309 2315 2064 0 72 -220 C ATOM 127 CE1 PHE A 15 12.180 7.663 16.423 1.00 19.76 C ANISOU 127 CE1 PHE A 15 2628 3096 1784 279 -2 193 C ATOM 128 CE2 PHE A 15 9.869 7.951 16.065 1.00 17.15 C ANISOU 128 CE2 PHE A 15 2043 2296 2177 -70 271 -375 C ATOM 129 CZ PHE A 15 10.903 7.698 16.895 1.00 19.97 C ANISOU 129 CZ PHE A 15 2591 2965 2031 123 165 59 C ATOM 130 N GLY A 16 14.421 7.171 12.160 1.00 13.27 N ANISOU 130 N GLY A 16 1651 1730 1661 -114 -254 149 N ATOM 131 CA GLY A 16 15.687 6.670 12.588 1.00 13.34 C ANISOU 131 CA GLY A 16 1749 1662 1658 49 -161 125 C ATOM 132 C GLY A 16 16.785 7.618 12.160 1.00 13.35 C ANISOU 132 C GLY A 16 1677 1862 1533 4 -123 12 C ATOM 133 O GLY A 16 16.537 8.816 12.001 1.00 12.23 O ANISOU 133 O GLY A 16 1687 1620 1340 43 -120 108 O ATOM 134 N PHE A 17 17.995 7.097 12.043 1.00 11.90 N ANISOU 134 N PHE A 17 1580 1402 1539 157 -147 56 N ATOM 135 CA PHE A 17 19.159 7.910 11.668 1.00 11.87 C ANISOU 135 CA PHE A 17 1416 1610 1483 93 -216 70 C ATOM 136 C PHE A 17 19.965 7.205 10.584 1.00 12.52 C ANISOU 136 C PHE A 17 1479 1680 1595 56 -189 -75 C ATOM 137 O PHE A 17 20.069 5.950 10.566 1.00 13.72 O ANISOU 137 O PHE A 17 1694 1675 1842 333 -131 134 O ATOM 138 CB PHE A 17 20.052 8.178 12.877 1.00 13.13 C ANISOU 138 CB PHE A 17 1527 1824 1637 -104 -279 78 C ATOM 139 CG PHE A 17 19.546 9.285 13.737 1.00 13.57 C ANISOU 139 CG PHE A 17 1721 1858 1576 -61 -456 169 C ATOM 140 CD1 PHE A 17 18.644 9.037 14.746 1.00 16.09 C ANISOU 140 CD1 PHE A 17 2227 2107 1777 158 -125 -177 C ATOM 141 CD2 PHE A 17 19.961 10.576 13.512 1.00 14.31 C ANISOU 141 CD2 PHE A 17 2002 1825 1610 93 -298 192 C ATOM 142 CE1 PHE A 17 18.184 10.055 15.536 1.00 17.36 C ANISOU 142 CE1 PHE A 17 2368 2281 1946 104 45 -394 C ATOM 143 CE2 PHE A 17 19.477 11.625 14.306 1.00 16.78 C ANISOU 143 CE2 PHE A 17 2565 1864 1943 246 -374 -49 C ATOM 144 CZ PHE A 17 18.600 11.354 15.302 1.00 16.34 C ANISOU 144 CZ PHE A 17 2554 2111 1543 193 -321 -254 C ATOM 145 N ILE A 18 20.570 8.029 9.723 1.00 12.69 N ANISOU 145 N ILE A 18 1430 1753 1637 158 -79 -118 N ATOM 146 CA ILE A 18 21.539 7.611 8.726 1.00 13.15 C ANISOU 146 CA ILE A 18 1604 1619 1774 4 -29 -194 C ATOM 147 C ILE A 18 22.882 8.036 9.259 1.00 15.39 C ANISOU 147 C ILE A 18 1664 1905 2277 200 -107 -356 C ATOM 148 O ILE A 18 23.054 9.170 9.691 1.00 16.17 O ANISOU 148 O ILE A 18 1746 2160 2235 98 -369 -297 O ATOM 149 CB ILE A 18 21.270 8.304 7.375 1.00 12.82 C ANISOU 149 CB ILE A 18 1582 1483 1805 -68 -117 -95 C ATOM 150 CG1 ILE A 18 19.905 7.874 6.830 1.00 13.10 C ANISOU 150 CG1 ILE A 18 1515 1854 1606 150 -85 -106 C ATOM 151 CG2 ILE A 18 22.343 7.997 6.358 1.00 16.21 C ANISOU 151 CG2 ILE A 18 1545 2480 2131 250 139 -261 C ATOM 152 CD1 ILE A 18 19.366 8.713 5.672 1.00 14.77 C ANISOU 152 CD1 ILE A 18 1798 2095 1718 570 -223 112 C ATOM 153 N GLU A 19 23.845 7.114 9.200 1.00 16.51 N ANISOU 153 N GLU A 19 1664 1928 2680 108 -373 -263 N ATOM 154 CA GLU A 19 25.222 7.401 9.589 1.00 17.42 C ANISOU 154 CA GLU A 19 1734 2251 2631 74 -216 -213 C ATOM 155 C GLU A 19 26.031 7.660 8.326 1.00 18.88 C ANISOU 155 C GLU A 19 2027 2491 2654 153 -180 -78 C ATOM 156 O GLU A 19 25.852 7.001 7.276 1.00 19.62 O ANISOU 156 O GLU A 19 1904 2730 2818 298 -303 -122 O ATOM 157 CB GLU A 19 25.825 6.305 10.459 1.00 20.07 C ANISOU 157 CB GLU A 19 2007 2689 2929 15 -136 -61 C ATOM 158 CG GLU A 19 25.926 4.933 9.886 1.00 21.82 C ANISOU 158 CG GLU A 19 2417 2957 2917 253 -274 -79 C ATOM 159 CD GLU A 19 26.461 3.931 10.956 1.00 23.51 C ANISOU 159 CD GLU A 19 2784 2714 3432 343 -114 176 C ATOM 160 OE1 GLU A 19 27.575 4.158 11.446 1.00 29.99 O ANISOU 160 OE1 GLU A 19 3456 3961 3975 64 -524 -215 O ATOM 161 OE2 GLU A 19 25.787 2.919 11.316 1.00 27.40 O ANISOU 161 OE2 GLU A 19 2952 3206 4252 624 -406 161 O ATOM 162 N VAL A 20 26.915 8.643 8.421 1.00 21.51 N ANISOU 162 N VAL A 20 2371 2861 2941 170 -85 -217 N ATOM 163 CA VAL A 20 27.765 9.062 7.336 1.00 24.59 C ANISOU 163 CA VAL A 20 2806 3178 3357 -41 -79 -122 C ATOM 164 C VAL A 20 29.177 9.145 7.944 1.00 25.62 C ANISOU 164 C VAL A 20 2780 3526 3425 -15 50 -145 C ATOM 165 O VAL A 20 29.406 9.878 8.910 1.00 24.89 O ANISOU 165 O VAL A 20 2107 4027 3320 -80 -13 -178 O ATOM 166 CB VAL A 20 27.276 10.404 6.749 1.00 26.42 C ANISOU 166 CB VAL A 20 2808 3490 3739 -62 -86 -5 C ATOM 167 CG1 VAL A 20 28.010 10.704 5.454 1.00 31.45 C ANISOU 167 CG1 VAL A 20 4256 3872 3820 5 53 178 C ATOM 168 CG2 VAL A 20 25.740 10.383 6.518 1.00 27.81 C ANISOU 168 CG2 VAL A 20 3050 3544 3972 70 -364 78 C ATOM 169 N GLU A 21 30.079 8.311 7.428 1.00 28.16 N ANISOU 169 N GLU A 21 3020 3901 3776 -19 112 -103 N ATOM 170 CA GLU A 21 31.482 8.308 7.850 1.00 30.07 C ANISOU 170 CA GLU A 21 3385 4035 4004 34 46 -39 C ATOM 171 C GLU A 21 32.056 9.729 8.010 1.00 30.51 C ANISOU 171 C GLU A 21 3405 4127 4060 -43 153 9 C ATOM 172 O GLU A 21 32.078 10.521 7.048 1.00 30.18 O ANISOU 172 O GLU A 21 3154 4114 4196 -39 364 252 O ATOM 173 CB GLU A 21 32.346 7.501 6.844 1.00 32.28 C ANISOU 173 CB GLU A 21 3833 4226 4204 27 116 -64 C ATOM 174 CG GLU A 21 32.456 6.011 7.168 1.00 34.19 C ANISOU 174 CG GLU A 21 4185 4300 4506 -70 81 -109 C ATOM 175 CD GLU A 21 33.271 5.238 6.152 0.50 34.04 C ANISOU 175 CD GLU A 21 4263 4370 4298 63 -46 -112 C ATOM 176 OE1 GLU A 21 32.779 5.050 5.010 0.50 34.07 O ANISOU 176 OE1 GLU A 21 4344 4475 4124 -69 19 -58 O ATOM 177 OE2 GLU A 21 34.394 4.813 6.502 0.50 32.08 O ANISOU 177 OE2 GLU A 21 4121 4290 3775 148 72 -281 O ATOM 178 N GLY A 22 32.452 10.064 9.240 1.00 30.21 N ANISOU 178 N GLY A 22 3197 4108 4172 -98 28 54 N ATOM 179 CA GLY A 22 33.100 11.343 9.522 1.00 30.59 C ANISOU 179 CA GLY A 22 3506 3955 4160 -75 -43 -11 C ATOM 180 C GLY A 22 32.201 12.563 9.574 1.00 29.86 C ANISOU 180 C GLY A 22 3336 3840 4168 -160 -15 -48 C ATOM 181 O GLY A 22 32.672 13.705 9.569 1.00 32.51 O ANISOU 181 O GLY A 22 3506 4116 4730 -391 -74 -7 O ATOM 182 N GLN A 23 30.891 12.347 9.614 1.00 27.51 N ANISOU 182 N GLN A 23 2921 3661 3870 -320 -26 27 N ATOM 183 CA GLN A 23 29.904 13.451 9.670 1.00 27.18 C ANISOU 183 CA GLN A 23 3129 3527 3668 -161 -1 5 C ATOM 184 C GLN A 23 28.829 13.135 10.689 1.00 24.53 C ANISOU 184 C GLN A 23 2542 3186 3592 -279 -198 18 C ATOM 185 O GLN A 23 28.760 12.046 11.204 1.00 23.29 O ANISOU 185 O GLN A 23 2101 3089 3660 -386 -497 -86 O ATOM 186 CB GLN A 23 29.221 13.684 8.314 1.00 29.61 C ANISOU 186 CB GLN A 23 3498 3930 3821 -69 -51 53 C ATOM 187 CG GLN A 23 30.198 13.676 7.107 1.00 33.20 C ANISOU 187 CG GLN A 23 4052 4303 4260 -103 109 0 C ATOM 188 CD GLN A 23 30.906 14.995 6.930 1.00 39.03 C ANISOU 188 CD GLN A 23 4902 4863 5065 -225 62 108 C ATOM 189 OE1 GLN A 23 32.032 15.056 6.419 1.00 43.45 O ANISOU 189 OE1 GLN A 23 4920 5819 5768 100 150 -27 O ATOM 190 NE2 GLN A 23 30.248 16.070 7.343 1.00 43.23 N ANISOU 190 NE2 GLN A 23 5428 5201 5794 -15 133 51 N ATOM 191 N ASP A 24 28.062 14.147 11.063 1.00 23.01 N ANISOU 191 N ASP A 24 2337 2947 3458 -256 -139 -62 N ATOM 192 CA ASP A 24 26.969 13.960 12.021 1.00 22.37 C ANISOU 192 CA ASP A 24 2338 2994 3166 -247 -198 -63 C ATOM 193 C ASP A 24 25.939 12.958 11.422 1.00 19.11 C ANISOU 193 C ASP A 24 1994 2644 2622 -287 -277 9 C ATOM 194 O ASP A 24 25.694 12.933 10.203 1.00 20.39 O ANISOU 194 O ASP A 24 2112 2952 2680 -363 -167 224 O ATOM 195 CB ASP A 24 26.249 15.275 12.319 1.00 24.83 C ANISOU 195 CB ASP A 24 2794 3158 3480 -251 -146 -148 C ATOM 196 CG ASP A 24 27.084 16.259 13.118 1.00 30.35 C ANISOU 196 CG ASP A 24 3651 3694 4185 -319 -257 -124 C ATOM 197 OD1 ASP A 24 28.110 15.864 13.722 1.00 32.58 O ANISOU 197 OD1 ASP A 24 3750 4203 4424 -334 -352 -30 O ATOM 198 OD2 ASP A 24 26.648 17.428 13.172 1.00 36.49 O ANISOU 198 OD2 ASP A 24 4563 4188 5112 -132 -245 -141 O ATOM 199 N ASP A 25 25.346 12.148 12.278 1.00 17.00 N ANISOU 199 N ASP A 25 1772 2348 2337 -40 -500 179 N ATOM 200 CA ASP A 25 24.201 11.332 11.898 1.00 15.10 C ANISOU 200 CA ASP A 25 1725 2024 1986 -81 -248 41 C ATOM 201 C ASP A 25 23.104 12.283 11.397 1.00 14.94 C ANISOU 201 C ASP A 25 1825 1847 2002 97 -298 -46 C ATOM 202 O ASP A 25 22.963 13.411 11.883 1.00 15.65 O ANISOU 202 O ASP A 25 1844 2101 1999 -16 -684 49 O ATOM 203 CB ASP A 25 23.616 10.571 13.108 1.00 16.34 C ANISOU 203 CB ASP A 25 1902 2097 2209 -34 -287 233 C ATOM 204 CG ASP A 25 24.547 9.506 13.687 1.00 18.26 C ANISOU 204 CG ASP A 25 2394 2356 2188 178 -212 239 C ATOM 205 OD1 ASP A 25 25.502 9.113 13.025 1.00 18.78 O ANISOU 205 OD1 ASP A 25 2268 2321 2545 386 -807 255 O ATOM 206 OD2 ASP A 25 24.239 9.095 14.828 1.00 18.48 O ANISOU 206 OD2 ASP A 25 2330 2382 2309 254 -394 254 O ATOM 207 N VAL A 26 22.287 11.784 10.475 1.00 12.69 N ANISOU 207 N VAL A 26 1576 1522 1723 92 -167 21 N ATOM 208 CA VAL A 26 21.196 12.548 9.881 1.00 12.23 C ANISOU 208 CA VAL A 26 1537 1594 1514 91 -67 -20 C ATOM 209 C VAL A 26 19.872 11.839 10.177 1.00 11.18 C ANISOU 209 C VAL A 26 1368 1676 1203 107 -161 -30 C ATOM 210 O VAL A 26 19.711 10.658 9.883 1.00 12.40 O ANISOU 210 O VAL A 26 1627 1644 1441 109 -164 45 O ATOM 211 CB VAL A 26 21.365 12.670 8.377 1.00 11.58 C ANISOU 211 CB VAL A 26 1375 1675 1350 15 177 17 C ATOM 212 CG1 VAL A 26 20.173 13.432 7.746 1.00 13.59 C ANISOU 212 CG1 VAL A 26 1630 1805 1725 172 -218 42 C ATOM 213 CG2 VAL A 26 22.703 13.349 8.045 1.00 14.59 C ANISOU 213 CG2 VAL A 26 1642 1946 1954 -284 43 -8 C ATOM 214 N PHE A 27 18.949 12.559 10.844 1.00 11.36 N ANISOU 214 N PHE A 27 1459 1669 1188 -21 -31 -160 N ATOM 215 CA PHE A 27 17.631 12.048 11.117 1.00 10.78 C ANISOU 215 CA PHE A 27 1459 1461 1176 -6 0 71 C ATOM 216 C PHE A 27 16.920 11.758 9.840 1.00 10.70 C ANISOU 216 C PHE A 27 1406 1318 1341 -19 57 -34 C ATOM 217 O PHE A 27 16.955 12.569 8.912 1.00 11.28 O ANISOU 217 O PHE A 27 1311 1437 1536 94 27 186 O ATOM 218 CB PHE A 27 16.852 13.123 11.904 1.00 11.48 C ANISOU 218 CB PHE A 27 1491 1649 1222 -53 -97 -22 C ATOM 219 CG PHE A 27 15.451 12.711 12.288 1.00 12.58 C ANISOU 219 CG PHE A 27 1614 1659 1504 16 21 -152 C ATOM 220 CD1 PHE A 27 15.216 11.959 13.402 1.00 13.59 C ANISOU 220 CD1 PHE A 27 1679 1820 1664 -90 211 -80 C ATOM 221 CD2 PHE A 27 14.374 13.096 11.512 1.00 13.60 C ANISOU 221 CD2 PHE A 27 1714 1858 1593 -122 -56 -187 C ATOM 222 CE1 PHE A 27 13.941 11.556 13.726 1.00 16.14 C ANISOU 222 CE1 PHE A 27 2133 1996 2004 -203 329 -179 C ATOM 223 CE2 PHE A 27 13.100 12.693 11.859 1.00 14.51 C ANISOU 223 CE2 PHE A 27 1607 1907 1998 -67 -82 -336 C ATOM 224 CZ PHE A 27 12.912 11.941 12.981 1.00 14.77 C ANISOU 224 CZ PHE A 27 1664 1756 2191 -43 309 -169 C ATOM 225 N VAL A 28 16.210 10.637 9.816 1.00 9.64 N ANISOU 225 N VAL A 28 1214 1270 1177 -130 -47 14 N ATOM 226 CA VAL A 28 15.374 10.269 8.671 1.00 10.62 C ANISOU 226 CA VAL A 28 1303 1458 1273 12 -69 35 C ATOM 227 C VAL A 28 13.971 9.879 9.111 1.00 11.26 C ANISOU 227 C VAL A 28 1481 1490 1307 12 -91 -53 C ATOM 228 O VAL A 28 13.813 9.013 9.965 1.00 11.82 O ANISOU 228 O VAL A 28 1416 1609 1463 -99 -64 177 O ATOM 229 CB VAL A 28 16.027 9.126 7.799 1.00 10.50 C ANISOU 229 CB VAL A 28 1295 1372 1320 -32 45 -7 C ATOM 230 CG1 VAL A 28 16.378 7.909 8.631 1.00 12.17 C ANISOU 230 CG1 VAL A 28 1756 1323 1542 175 -127 168 C ATOM 231 CG2 VAL A 28 15.108 8.763 6.623 1.00 12.31 C ANISOU 231 CG2 VAL A 28 1508 1897 1270 132 -181 -210 C ATOM 232 N HIS A 29 12.979 10.479 8.478 1.00 11.48 N ANISOU 232 N HIS A 29 1365 1729 1268 -146 -159 48 N ATOM 233 CA HIS A 29 11.595 10.128 8.656 1.00 11.82 C ANISOU 233 CA HIS A 29 1422 1646 1421 52 2 -85 C ATOM 234 C HIS A 29 11.095 9.353 7.465 1.00 11.99 C ANISOU 234 C HIS A 29 1388 1644 1521 -48 -93 -42 C ATOM 235 O HIS A 29 11.600 9.519 6.351 1.00 12.36 O ANISOU 235 O HIS A 29 1341 1833 1522 -116 5 -50 O ATOM 236 CB HIS A 29 10.797 11.417 8.783 1.00 12.85 C ANISOU 236 CB HIS A 29 1577 1647 1658 34 -138 -331 C ATOM 237 CG HIS A 29 9.364 11.217 9.144 1.00 14.45 C ANISOU 237 CG HIS A 29 1590 2300 1598 -8 -38 -340 C ATOM 238 ND1 HIS A 29 8.351 11.310 8.218 1.00 13.29 N ANISOU 238 ND1 HIS A 29 1400 1806 1843 211 59 -360 N ATOM 239 CD2 HIS A 29 8.791 10.895 10.326 1.00 16.37 C ANISOU 239 CD2 HIS A 29 1851 2577 1790 -36 -96 -45 C ATOM 240 CE1 HIS A 29 7.205 11.037 8.819 1.00 15.01 C ANISOU 240 CE1 HIS A 29 1597 2363 1741 -33 63 -285 C ATOM 241 NE2 HIS A 29 7.445 10.795 10.105 1.00 15.53 N ANISOU 241 NE2 HIS A 29 1655 2380 1862 145 -7 -321 N ATOM 242 N PHE A 30 10.107 8.489 7.683 1.00 12.76 N ANISOU 242 N PHE A 30 1554 1682 1611 -34 44 -192 N ATOM 243 CA PHE A 30 9.647 7.633 6.607 1.00 12.45 C ANISOU 243 CA PHE A 30 1457 1688 1582 -128 -13 -112 C ATOM 244 C PHE A 30 9.202 8.415 5.396 1.00 12.85 C ANISOU 244 C PHE A 30 1404 1787 1692 -160 -22 -134 C ATOM 245 O PHE A 30 9.276 7.900 4.293 1.00 13.99 O ANISOU 245 O PHE A 30 1673 1992 1650 -261 -250 -353 O ATOM 246 CB PHE A 30 8.500 6.706 7.101 1.00 12.61 C ANISOU 246 CB PHE A 30 1520 1646 1624 -107 -109 -148 C ATOM 247 CG PHE A 30 7.190 7.407 7.392 1.00 13.79 C ANISOU 247 CG PHE A 30 1516 2033 1690 -247 -158 -115 C ATOM 248 CD1 PHE A 30 6.347 7.811 6.347 1.00 16.04 C ANISOU 248 CD1 PHE A 30 1852 2093 2149 -90 -381 -210 C ATOM 249 CD2 PHE A 30 6.784 7.598 8.680 1.00 15.51 C ANISOU 249 CD2 PHE A 30 1500 2302 2089 -310 -115 -153 C ATOM 250 CE1 PHE A 30 5.165 8.441 6.629 1.00 18.73 C ANISOU 250 CE1 PHE A 30 1752 2830 2532 -277 -367 -88 C ATOM 251 CE2 PHE A 30 5.567 8.190 8.975 1.00 15.97 C ANISOU 251 CE2 PHE A 30 1665 2605 1795 -225 12 -146 C ATOM 252 CZ PHE A 30 4.752 8.629 7.937 1.00 17.68 C ANISOU 252 CZ PHE A 30 1359 2719 2639 -64 -227 21 C ATOM 253 N SER A 31 8.692 9.629 5.602 1.00 13.05 N ANISOU 253 N SER A 31 1693 1901 1364 138 -40 -26 N ATOM 254 CA SER A 31 8.196 10.440 4.475 1.00 14.43 C ANISOU 254 CA SER A 31 1718 1919 1846 101 -209 -12 C ATOM 255 C SER A 31 9.252 10.837 3.479 1.00 14.85 C ANISOU 255 C SER A 31 1842 2129 1671 243 -103 168 C ATOM 256 O SER A 31 8.911 11.223 2.346 1.00 18.84 O ANISOU 256 O SER A 31 2123 3162 1872 236 -351 310 O ATOM 257 CB SER A 31 7.477 11.665 4.984 1.00 16.49 C ANISOU 257 CB SER A 31 1858 2368 2037 388 66 68 C ATOM 258 OG SER A 31 8.303 12.502 5.766 1.00 17.91 O ANISOU 258 OG SER A 31 2025 2341 2437 432 -58 -65 O ATOM 259 N ALA A 32 10.530 10.700 3.845 1.00 12.38 N ANISOU 259 N ALA A 32 1511 1751 1442 96 -273 85 N ATOM 260 CA ALA A 32 11.636 10.992 2.973 1.00 12.74 C ANISOU 260 CA ALA A 32 1740 1701 1400 146 -177 219 C ATOM 261 C ALA A 32 11.994 9.846 2.047 1.00 13.79 C ANISOU 261 C ALA A 32 1773 1872 1595 77 -189 23 C ATOM 262 O ALA A 32 12.756 10.038 1.108 1.00 14.12 O ANISOU 262 O ALA A 32 1894 1720 1747 29 -12 52 O ATOM 263 CB ALA A 32 12.898 11.394 3.779 1.00 14.47 C ANISOU 263 CB ALA A 32 1856 1945 1694 -56 -276 -54 C ATOM 264 N ILE A 33 11.483 8.648 2.309 1.00 13.73 N ANISOU 264 N ILE A 33 1671 2029 1517 95 -47 -14 N ATOM 265 CA ILE A 33 11.874 7.438 1.569 1.00 14.09 C ANISOU 265 CA ILE A 33 1762 1920 1670 -139 -79 -69 C ATOM 266 C ILE A 33 11.173 7.446 0.211 1.00 14.40 C ANISOU 266 C ILE A 33 1760 2015 1695 -73 -19 -9 C ATOM 267 O ILE A 33 9.956 7.577 0.107 1.00 16.15 O ANISOU 267 O ILE A 33 1723 2524 1886 -205 -197 -184 O ATOM 268 CB ILE A 33 11.532 6.171 2.368 1.00 13.12 C ANISOU 268 CB ILE A 33 1682 1704 1596 -32 -65 -264 C ATOM 269 CG1 ILE A 33 12.259 6.236 3.729 1.00 13.64 C ANISOU 269 CG1 ILE A 33 1441 1947 1794 -66 -237 -163 C ATOM 270 CG2 ILE A 33 11.908 4.930 1.614 1.00 15.95 C ANISOU 270 CG2 ILE A 33 2139 1680 2240 -77 47 -472 C ATOM 271 CD1 ILE A 33 11.762 5.140 4.722 1.00 14.31 C ANISOU 271 CD1 ILE A 33 1580 2060 1797 26 -38 55 C ATOM 272 N GLN A 34 11.979 7.219 -0.817 1.00 15.43 N ANISOU 272 N GLN A 34 1950 2440 1471 -172 -143 -136 N ATOM 273 CA GLN A 34 11.499 7.163 -2.171 1.00 17.66 C ANISOU 273 CA GLN A 34 2379 2403 1925 -97 -271 -4 C ATOM 274 C GLN A 34 11.106 5.752 -2.547 1.00 19.04 C ANISOU 274 C GLN A 34 2490 2470 2275 -129 -344 -40 C ATOM 275 O GLN A 34 11.439 4.807 -1.883 1.00 22.22 O ANISOU 275 O GLN A 34 3503 2667 2270 -373 -494 -144 O ATOM 276 CB GLN A 34 12.565 7.664 -3.129 1.00 18.36 C ANISOU 276 CB GLN A 34 2515 2659 1799 -218 -254 64 C ATOM 277 CG GLN A 34 13.074 9.060 -2.805 1.00 19.90 C ANISOU 277 CG GLN A 34 2961 2603 1994 -190 -52 113 C ATOM 278 CD GLN A 34 11.936 10.106 -2.748 1.00 19.61 C ANISOU 278 CD GLN A 34 3084 2360 2005 -25 -243 97 C ATOM 279 OE1 GLN A 34 11.312 10.415 -3.791 1.00 24.52 O ANISOU 279 OE1 GLN A 34 3584 3398 2331 -119 -790 245 O ATOM 280 NE2 GLN A 34 11.622 10.611 -1.549 1.00 21.50 N ANISOU 280 NE2 GLN A 34 3174 2670 2322 -208 -21 94 N ATOM 281 N GLY A 35 10.463 5.623 -3.683 1.00 21.60 N ANISOU 281 N GLY A 35 3129 2836 2242 -180 -108 -47 N ATOM 282 CA GLY A 35 10.141 4.325 -4.240 1.00 20.79 C ANISOU 282 CA GLY A 35 2814 2833 2249 -251 -58 -234 C ATOM 283 C GLY A 35 8.745 3.893 -3.938 1.00 22.80 C ANISOU 283 C GLY A 35 2951 3073 2637 -187 11 -376 C ATOM 284 O GLY A 35 7.944 4.655 -3.460 1.00 27.44 O ANISOU 284 O GLY A 35 3197 3576 3652 -239 -138 -709 O ATOM 285 N GLU A 36 8.445 2.645 -4.206 1.00 24.62 N ANISOU 285 N GLU A 36 3192 3170 2991 -253 185 -428 N ATOM 286 CA GLU A 36 7.084 2.159 -4.038 1.00 24.87 C ANISOU 286 CA GLU A 36 3105 3261 3080 -227 20 -354 C ATOM 287 C GLU A 36 6.985 1.367 -2.771 1.00 23.62 C ANISOU 287 C GLU A 36 2795 3126 3051 -300 -19 -349 C ATOM 288 O GLU A 36 7.981 1.049 -2.101 1.00 24.18 O ANISOU 288 O GLU A 36 2669 3153 3365 -363 154 -270 O ATOM 289 CB GLU A 36 6.704 1.281 -5.230 1.00 27.05 C ANISOU 289 CB GLU A 36 3531 3526 3218 -323 -61 -280 C ATOM 290 CG GLU A 36 6.703 2.022 -6.558 1.00 29.69 C ANISOU 290 CG GLU A 36 3920 3784 3575 -178 -112 -78 C ATOM 291 CD GLU A 36 5.774 3.215 -6.542 0.50 30.96 C ANISOU 291 CD GLU A 36 3808 3988 3964 -1 -71 -17 C ATOM 292 OE1 GLU A 36 4.647 3.057 -6.028 0.50 31.54 O ANISOU 292 OE1 GLU A 36 4012 4217 3752 -92 22 45 O ATOM 293 OE2 GLU A 36 6.166 4.304 -7.029 0.50 33.08 O ANISOU 293 OE2 GLU A 36 4086 4068 4415 64 63 116 O ATOM 294 N GLY A 37 5.758 1.075 -2.393 1.00 22.18 N ANISOU 294 N GLY A 37 2605 3042 2778 -254 29 -416 N ATOM 295 CA GLY A 37 5.530 0.211 -1.279 1.00 20.28 C ANISOU 295 CA GLY A 37 2428 2749 2528 -116 82 -358 C ATOM 296 C GLY A 37 5.544 0.952 0.074 1.00 18.26 C ANISOU 296 C GLY A 37 2115 2401 2421 -239 -38 -310 C ATOM 297 O GLY A 37 5.665 2.197 0.181 1.00 18.52 O ANISOU 297 O GLY A 37 2291 2384 2361 -184 -206 -228 O ATOM 298 N PHE A 38 5.408 0.157 1.111 1.00 17.52 N ANISOU 298 N PHE A 38 1957 2262 2438 -230 106 -170 N ATOM 299 CA PHE A 38 5.465 0.629 2.497 1.00 17.16 C ANISOU 299 CA PHE A 38 1836 2268 2414 -262 -109 -127 C ATOM 300 C PHE A 38 6.821 1.260 2.731 1.00 16.22 C ANISOU 300 C PHE A 38 1750 2052 2358 -193 -96 -184 C ATOM 301 O PHE A 38 7.837 0.640 2.437 1.00 18.01 O ANISOU 301 O PHE A 38 1971 2200 2669 -222 -29 -437 O ATOM 302 CB PHE A 38 5.250 -0.546 3.437 1.00 17.69 C ANISOU 302 CB PHE A 38 1999 2297 2425 -309 -130 -126 C ATOM 303 CG PHE A 38 5.273 -0.211 4.881 1.00 18.39 C ANISOU 303 CG PHE A 38 2082 2430 2475 -482 -137 16 C ATOM 304 CD1 PHE A 38 4.369 0.669 5.434 1.00 19.85 C ANISOU 304 CD1 PHE A 38 2431 2389 2722 -657 84 -101 C ATOM 305 CD2 PHE A 38 6.171 -0.853 5.725 1.00 21.32 C ANISOU 305 CD2 PHE A 38 2252 2821 3025 -118 -8 106 C ATOM 306 CE1 PHE A 38 4.392 0.945 6.853 1.00 20.17 C ANISOU 306 CE1 PHE A 38 2323 2363 2978 -833 -16 116 C ATOM 307 CE2 PHE A 38 6.178 -0.601 7.076 1.00 23.04 C ANISOU 307 CE2 PHE A 38 2550 2979 3225 -414 -174 -7 C ATOM 308 CZ PHE A 38 5.280 0.272 7.642 1.00 22.17 C ANISOU 308 CZ PHE A 38 2559 2776 3089 -650 -302 -175 C ATOM 309 N LYS A 39 6.818 2.486 3.247 1.00 16.35 N ANISOU 309 N LYS A 39 1832 2165 2214 -293 -154 -113 N ATOM 310 CA LYS A 39 8.046 3.253 3.409 1.00 15.91 C ANISOU 310 CA LYS A 39 1875 2043 2125 -257 -224 -86 C ATOM 311 C LYS A 39 8.728 2.890 4.735 1.00 15.40 C ANISOU 311 C LYS A 39 1955 1855 2042 -202 -207 -56 C ATOM 312 O LYS A 39 8.227 3.186 5.839 1.00 16.35 O ANISOU 312 O LYS A 39 1716 2438 2056 -242 -264 -20 O ATOM 313 CB LYS A 39 7.767 4.734 3.305 1.00 17.75 C ANISOU 313 CB LYS A 39 2195 2291 2255 -257 -187 8 C ATOM 314 CG LYS A 39 7.286 5.095 1.929 1.00 19.64 C ANISOU 314 CG LYS A 39 2497 2332 2631 -218 -766 -34 C ATOM 315 CD LYS A 39 7.178 6.581 1.793 1.00 22.72 C ANISOU 315 CD LYS A 39 2688 2772 3169 -52 -377 59 C ATOM 316 CE LYS A 39 6.748 7.064 0.381 1.00 23.13 C ANISOU 316 CE LYS A 39 2884 2713 3190 -317 -382 -95 C ATOM 317 NZ LYS A 39 7.416 6.246 -0.648 1.00 26.67 N ANISOU 317 NZ LYS A 39 3087 4120 2923 62 -765 -359 N ATOM 318 N THR A 40 9.842 2.191 4.597 1.00 15.58 N ANISOU 318 N THR A 40 1919 1963 2036 -112 -240 46 N ATOM 319 CA THR A 40 10.594 1.756 5.734 1.00 17.17 C ANISOU 319 CA THR A 40 2103 2222 2199 -232 -131 85 C ATOM 320 C THR A 40 12.059 1.526 5.356 1.00 15.67 C ANISOU 320 C THR A 40 1917 2021 2014 -70 -117 -11 C ATOM 321 O THR A 40 12.429 1.509 4.179 1.00 16.86 O ANISOU 321 O THR A 40 2040 2130 2234 -28 -139 -79 O ATOM 322 CB THR A 40 9.953 0.499 6.342 1.00 18.07 C ANISOU 322 CB THR A 40 2317 2339 2209 -245 -65 239 C ATOM 323 OG1 THR A 40 10.451 0.328 7.687 1.00 20.88 O ANISOU 323 OG1 THR A 40 2501 2991 2441 -590 -238 388 O ATOM 324 CG2 THR A 40 10.141 -0.749 5.444 1.00 21.38 C ANISOU 324 CG2 THR A 40 2747 2230 3146 -364 93 37 C ATOM 325 N LEU A 41 12.881 1.357 6.396 1.00 15.19 N ANISOU 325 N LEU A 41 2032 1826 1912 -13 -181 16 N ATOM 326 CA LEU A 41 14.329 1.138 6.245 1.00 15.11 C ANISOU 326 CA LEU A 41 1984 1766 1990 10 -50 -101 C ATOM 327 C LEU A 41 14.776 0.115 7.259 1.00 16.81 C ANISOU 327 C LEU A 41 2316 1878 2193 33 0 -25 C ATOM 328 O LEU A 41 14.165 -0.019 8.315 1.00 18.51 O ANISOU 328 O LEU A 41 2615 2027 2390 137 -119 80 O ATOM 329 CB LEU A 41 15.149 2.419 6.480 1.00 14.16 C ANISOU 329 CB LEU A 41 1941 1634 1804 50 -139 -38 C ATOM 330 CG LEU A 41 14.958 3.491 5.406 1.00 14.65 C ANISOU 330 CG LEU A 41 1535 1977 2052 -79 -126 213 C ATOM 331 CD1 LEU A 41 15.452 4.835 5.963 1.00 14.71 C ANISOU 331 CD1 LEU A 41 2147 1588 1853 -110 -186 -51 C ATOM 332 CD2 LEU A 41 15.664 3.119 4.109 1.00 15.96 C ANISOU 332 CD2 LEU A 41 2423 1940 1700 -146 -94 -219 C ATOM 333 N GLU A 42 15.842 -0.590 6.924 1.00 17.89 N ANISOU 333 N GLU A 42 2264 2098 2436 56 -143 230 N ATOM 334 CA GLU A 42 16.433 -1.587 7.839 1.00 20.00 C ANISOU 334 CA GLU A 42 2475 2283 2840 216 -173 147 C ATOM 335 C GLU A 42 17.830 -1.120 8.228 1.00 19.87 C ANISOU 335 C GLU A 42 2533 2270 2745 249 -180 105 C ATOM 336 O GLU A 42 18.553 -0.589 7.398 1.00 19.19 O ANISOU 336 O GLU A 42 2332 2121 2836 420 -313 162 O ATOM 337 CB GLU A 42 16.505 -2.970 7.149 1.00 21.64 C ANISOU 337 CB GLU A 42 2771 2445 3002 101 -305 109 C ATOM 338 CG GLU A 42 15.196 -3.514 6.601 1.00 28.48 C ANISOU 338 CG GLU A 42 3573 3375 3872 -96 -182 -128 C ATOM 339 CD GLU A 42 14.479 -4.424 7.573 0.50 29.11 C ANISOU 339 CD GLU A 42 3599 3702 3756 -113 58 -34 C ATOM 340 OE1 GLU A 42 14.648 -4.291 8.811 0.50 31.37 O ANISOU 340 OE1 GLU A 42 4059 4015 3842 -187 -111 87 O ATOM 341 OE2 GLU A 42 13.748 -5.292 7.074 0.50 32.80 O ANISOU 341 OE2 GLU A 42 4160 3965 4336 -225 -127 -224 O ATOM 342 N GLU A 43 18.216 -1.417 9.467 1.00 20.38 N ANISOU 342 N GLU A 43 2700 2311 2729 222 -33 252 N ATOM 343 CA GLU A 43 19.560 -1.169 9.946 1.00 20.81 C ANISOU 343 CA GLU A 43 2873 2225 2807 148 -169 189 C ATOM 344 C GLU A 43 20.581 -1.752 8.978 1.00 19.88 C ANISOU 344 C GLU A 43 2662 2131 2758 238 -241 159 C ATOM 345 O GLU A 43 20.461 -2.914 8.555 1.00 21.97 O ANISOU 345 O GLU A 43 3081 2221 3045 406 -528 159 O ATOM 346 CB GLU A 43 19.724 -1.766 11.350 1.00 23.27 C ANISOU 346 CB GLU A 43 3191 2756 2892 95 -190 170 C ATOM 347 CG GLU A 43 21.076 -1.476 12.010 1.00 27.04 C ANISOU 347 CG GLU A 43 3659 3064 3549 -97 -259 143 C ATOM 348 CD GLU A 43 21.091 -1.774 13.518 1.00 35.61 C ANISOU 348 CD GLU A 43 4657 4776 4095 20 -62 169 C ATOM 349 OE1 GLU A 43 20.052 -1.543 14.225 1.00 38.31 O ANISOU 349 OE1 GLU A 43 4998 5166 4390 179 -69 79 O ATOM 350 OE2 GLU A 43 22.159 -2.221 13.985 1.00 37.82 O ANISOU 350 OE2 GLU A 43 5016 5025 4325 158 -345 303 O ATOM 351 N GLY A 44 21.578 -0.940 8.637 1.00 19.18 N ANISOU 351 N GLY A 44 2363 2082 2841 502 -114 29 N ATOM 352 CA GLY A 44 22.668 -1.323 7.773 1.00 19.98 C ANISOU 352 CA GLY A 44 2503 2306 2782 369 -46 40 C ATOM 353 C GLY A 44 22.395 -1.108 6.305 1.00 19.32 C ANISOU 353 C GLY A 44 2362 2236 2740 361 -88 60 C ATOM 354 O GLY A 44 23.300 -1.192 5.536 1.00 22.55 O ANISOU 354 O GLY A 44 2606 2718 3242 854 -87 -2 O ATOM 355 N GLN A 45 21.166 -0.763 5.910 1.00 19.19 N ANISOU 355 N GLN A 45 2391 2213 2687 349 -167 185 N ATOM 356 CA GLN A 45 20.866 -0.542 4.516 1.00 19.26 C ANISOU 356 CA GLN A 45 2511 2212 2594 282 -31 -56 C ATOM 357 C GLN A 45 21.619 0.676 3.971 1.00 18.24 C ANISOU 357 C GLN A 45 2263 2103 2561 230 -116 -90 C ATOM 358 O GLN A 45 21.624 1.775 4.576 1.00 18.71 O ANISOU 358 O GLN A 45 2440 1956 2713 464 -407 -299 O ATOM 359 CB GLN A 45 19.355 -0.295 4.377 1.00 21.24 C ANISOU 359 CB GLN A 45 2624 2699 2747 40 -103 14 C ATOM 360 CG GLN A 45 18.928 0.305 3.064 1.00 24.42 C ANISOU 360 CG GLN A 45 2764 3486 3026 48 -204 -29 C ATOM 361 CD GLN A 45 18.732 -0.713 2.000 1.00 29.89 C ANISOU 361 CD GLN A 45 3810 3703 3841 -101 85 -172 C ATOM 362 OE1 GLN A 45 17.787 -1.535 2.062 1.00 34.26 O ANISOU 362 OE1 GLN A 45 4560 3669 4785 -96 -182 291 O ATOM 363 NE2 GLN A 45 19.593 -0.659 0.976 1.00 29.92 N ANISOU 363 NE2 GLN A 45 3581 3635 4152 -10 124 -129 N ATOM 364 N ALA A 46 22.193 0.520 2.794 1.00 19.18 N ANISOU 364 N ALA A 46 2555 2035 2696 300 -72 -176 N ATOM 365 CA ALA A 46 22.856 1.621 2.091 1.00 18.61 C ANISOU 365 CA ALA A 46 2324 2171 2575 215 102 -259 C ATOM 366 C ALA A 46 21.795 2.519 1.523 1.00 18.25 C ANISOU 366 C ALA A 46 2259 2161 2513 254 -2 -358 C ATOM 367 O ALA A 46 20.825 2.047 0.970 1.00 18.41 O ANISOU 367 O ALA A 46 2372 2017 2602 644 -338 -530 O ATOM 368 CB ALA A 46 23.734 1.137 0.952 1.00 19.78 C ANISOU 368 CB ALA A 46 2590 2202 2720 437 221 -293 C ATOM 369 N VAL A 47 22.011 3.818 1.654 1.00 18.21 N ANISOU 369 N VAL A 47 2305 2050 2562 251 -44 -190 N ATOM 370 CA VAL A 47 21.128 4.833 1.093 1.00 16.33 C ANISOU 370 CA VAL A 47 2011 2001 2191 267 -39 -256 C ATOM 371 C VAL A 47 21.885 5.977 0.405 1.00 16.79 C ANISOU 371 C VAL A 47 2168 2103 2106 407 174 -263 C ATOM 372 O VAL A 47 23.002 6.320 0.807 1.00 17.96 O ANISOU 372 O VAL A 47 2227 1959 2635 334 112 -259 O ATOM 373 CB VAL A 47 20.216 5.459 2.183 1.00 15.75 C ANISOU 373 CB VAL A 47 1775 2017 2189 220 -39 -100 C ATOM 374 CG1 VAL A 47 19.208 4.436 2.677 1.00 17.21 C ANISOU 374 CG1 VAL A 47 2327 1821 2390 83 -114 -142 C ATOM 375 CG2 VAL A 47 21.062 6.062 3.314 1.00 17.18 C ANISOU 375 CG2 VAL A 47 2195 2059 2270 181 -137 -164 C ATOM 376 N SER A 48 21.232 6.603 -0.579 1.00 16.08 N ANISOU 376 N SER A 48 2205 1980 1924 278 93 -379 N ATOM 377 CA SER A 48 21.608 7.905 -1.118 1.00 17.73 C ANISOU 377 CA SER A 48 2445 2176 2112 264 239 -290 C ATOM 378 C SER A 48 20.553 8.889 -0.680 1.00 15.96 C ANISOU 378 C SER A 48 2121 2050 1891 202 135 -208 C ATOM 379 O SER A 48 19.366 8.528 -0.585 1.00 16.57 O ANISOU 379 O SER A 48 2302 1829 2162 116 14 -484 O ATOM 380 CB SER A 48 21.720 7.912 -2.646 1.00 20.61 C ANISOU 380 CB SER A 48 2650 2777 2402 290 315 -240 C ATOM 381 OG SER A 48 20.559 7.493 -3.262 1.00 25.86 O ANISOU 381 OG SER A 48 3458 3259 3108 208 71 -207 O ATOM 382 N PHE A 49 20.958 10.128 -0.461 1.00 13.83 N ANISOU 382 N PHE A 49 1726 1829 1700 49 284 26 N ATOM 383 CA PHE A 49 20.035 11.116 0.098 1.00 14.37 C ANISOU 383 CA PHE A 49 1855 1862 1741 -33 224 -83 C ATOM 384 C PHE A 49 20.597 12.509 0.017 1.00 13.21 C ANISOU 384 C PHE A 49 1630 1819 1569 24 135 -63 C ATOM 385 O PHE A 49 21.773 12.714 -0.301 1.00 14.97 O ANISOU 385 O PHE A 49 1796 1961 1930 89 367 -147 O ATOM 386 CB PHE A 49 19.696 10.760 1.588 1.00 14.64 C ANISOU 386 CB PHE A 49 1983 1717 1861 -107 271 -16 C ATOM 387 CG PHE A 49 20.878 10.921 2.526 1.00 14.30 C ANISOU 387 CG PHE A 49 2065 1881 1485 142 275 55 C ATOM 388 CD1 PHE A 49 21.894 9.969 2.548 1.00 15.52 C ANISOU 388 CD1 PHE A 49 1820 2060 2015 175 175 70 C ATOM 389 CD2 PHE A 49 21.014 12.030 3.333 1.00 16.14 C ANISOU 389 CD2 PHE A 49 2363 2034 1735 -49 -168 117 C ATOM 390 CE1 PHE A 49 23.004 10.123 3.324 1.00 17.43 C ANISOU 390 CE1 PHE A 49 2216 2119 2288 520 -49 -88 C ATOM 391 CE2 PHE A 49 22.152 12.176 4.134 1.00 18.90 C ANISOU 391 CE2 PHE A 49 2486 2135 2557 30 -337 -170 C ATOM 392 CZ PHE A 49 23.142 11.218 4.128 1.00 19.16 C ANISOU 392 CZ PHE A 49 2777 2416 2085 250 -255 168 C ATOM 393 N GLU A 50 19.740 13.469 0.340 1.00 12.58 N ANISOU 393 N GLU A 50 1752 1547 1480 4 298 -137 N ATOM 394 CA GLU A 50 20.112 14.862 0.541 1.00 13.24 C ANISOU 394 CA GLU A 50 1866 1519 1645 -102 168 -101 C ATOM 395 C GLU A 50 19.749 15.279 1.957 1.00 12.84 C ANISOU 395 C GLU A 50 1890 1470 1517 -95 51 22 C ATOM 396 O GLU A 50 18.917 14.616 2.619 1.00 12.95 O ANISOU 396 O GLU A 50 1696 1609 1614 -51 105 -11 O ATOM 397 CB GLU A 50 19.436 15.781 -0.469 1.00 15.12 C ANISOU 397 CB GLU A 50 2583 1398 1761 -158 223 -3 C ATOM 398 CG GLU A 50 19.860 15.576 -1.888 1.00 19.95 C ANISOU 398 CG GLU A 50 2689 2501 2388 13 93 -114 C ATOM 399 CD GLU A 50 18.926 16.258 -2.878 1.00 25.04 C ANISOU 399 CD GLU A 50 3262 3407 2843 174 -134 -37 C ATOM 400 OE1 GLU A 50 17.702 16.157 -2.733 1.00 25.52 O ANISOU 400 OE1 GLU A 50 3441 3719 2536 -157 -511 478 O ATOM 401 OE2 GLU A 50 19.452 16.879 -3.803 1.00 33.68 O ANISOU 401 OE2 GLU A 50 4672 4136 3987 28 13 414 O ATOM 402 N ILE A 51 20.349 16.365 2.420 1.00 11.77 N ANISOU 402 N ILE A 51 1558 1415 1499 24 218 -1 N ATOM 403 CA ILE A 51 19.981 16.947 3.717 1.00 11.33 C ANISOU 403 CA ILE A 51 1737 1360 1207 57 238 122 C ATOM 404 C ILE A 51 19.220 18.229 3.490 1.00 11.51 C ANISOU 404 C ILE A 51 1574 1371 1427 45 216 69 C ATOM 405 O ILE A 51 19.744 19.118 2.806 1.00 13.81 O ANISOU 405 O ILE A 51 2012 1410 1823 -123 444 376 O ATOM 406 CB ILE A 51 21.187 17.207 4.589 1.00 12.30 C ANISOU 406 CB ILE A 51 1600 1666 1407 62 283 56 C ATOM 407 CG1 ILE A 51 21.998 15.928 4.856 1.00 14.26 C ANISOU 407 CG1 ILE A 51 1757 1945 1715 82 86 10 C ATOM 408 CG2 ILE A 51 20.813 17.893 5.942 1.00 14.49 C ANISOU 408 CG2 ILE A 51 2132 2076 1298 -38 440 -81 C ATOM 409 CD1 ILE A 51 23.419 16.161 5.412 1.00 15.26 C ANISOU 409 CD1 ILE A 51 1632 2252 1912 47 224 82 C ATOM 410 N VAL A 52 18.034 18.340 4.071 1.00 11.29 N ANISOU 410 N VAL A 52 1633 1347 1307 -32 141 205 N ATOM 411 CA AVAL A 52 17.156 19.520 3.957 0.50 12.06 C ANISOU 411 CA AVAL A 52 1756 1389 1435 14 178 116 C ATOM 412 CA BVAL A 52 17.246 19.572 3.950 0.50 12.67 C ANISOU 412 CA BVAL A 52 1843 1493 1475 48 151 60 C ATOM 413 C VAL A 52 17.038 20.179 5.319 1.00 12.40 C ANISOU 413 C VAL A 52 1863 1376 1470 -43 327 -10 C ATOM 414 O VAL A 52 16.726 19.479 6.291 1.00 14.59 O ANISOU 414 O VAL A 52 2389 1578 1574 -110 376 99 O ATOM 415 CB AVAL A 52 15.752 19.127 3.379 0.50 11.78 C ANISOU 415 CB AVAL A 52 1678 1519 1275 151 115 79 C ATOM 416 CB BVAL A 52 15.907 19.382 3.220 0.50 13.01 C ANISOU 416 CB BVAL A 52 1813 1628 1499 9 20 -89 C ATOM 417 CG1AVAL A 52 15.022 18.082 4.206 0.50 13.21 C ANISOU 417 CG1AVAL A 52 1470 1735 1810 -295 216 70 C ATOM 418 CG1BVAL A 52 15.191 20.732 3.056 0.50 15.01 C ANISOU 418 CG1BVAL A 52 1813 1844 2046 65 -119 80 C ATOM 419 CG2AVAL A 52 14.851 20.370 3.161 0.50 12.37 C ANISOU 419 CG2AVAL A 52 1803 1305 1592 47 16 301 C ATOM 420 CG2BVAL A 52 16.098 18.767 1.806 0.50 15.58 C ANISOU 420 CG2BVAL A 52 2527 2227 1166 319 -17 -16 C ATOM 421 N GLU A 53 17.299 21.469 5.390 1.00 12.25 N ANISOU 421 N GLU A 53 1945 1448 1262 -27 147 91 N ATOM 422 CA GLU A 53 17.198 22.198 6.631 1.00 12.21 C ANISOU 422 CA GLU A 53 1881 1490 1266 10 158 90 C ATOM 423 C GLU A 53 16.273 23.433 6.515 1.00 13.58 C ANISOU 423 C GLU A 53 2015 1709 1433 49 149 -11 C ATOM 424 O GLU A 53 16.448 24.296 5.678 1.00 14.16 O ANISOU 424 O GLU A 53 2105 1660 1612 170 471 42 O ATOM 425 CB GLU A 53 18.571 22.651 7.068 1.00 14.70 C ANISOU 425 CB GLU A 53 1968 1895 1719 -27 66 -94 C ATOM 426 CG GLU A 53 18.547 23.445 8.398 1.00 15.69 C ANISOU 426 CG GLU A 53 1974 2131 1854 -14 175 -400 C ATOM 427 CD GLU A 53 19.835 23.398 9.195 1.00 21.92 C ANISOU 427 CD GLU A 53 2498 3192 2636 -8 -7 -534 C ATOM 428 OE1 GLU A 53 20.831 22.809 8.732 1.00 24.27 O ANISOU 428 OE1 GLU A 53 2777 3132 3312 122 168 -576 O ATOM 429 OE2 GLU A 53 19.819 23.876 10.366 1.00 26.93 O ANISOU 429 OE2 GLU A 53 3691 3797 2741 -182 32 -1035 O ATOM 430 N GLY A 54 15.296 23.487 7.402 1.00 13.05 N ANISOU 430 N GLY A 54 2001 1488 1467 186 277 13 N ATOM 431 CA GLY A 54 14.471 24.642 7.660 1.00 14.08 C ANISOU 431 CA GLY A 54 1856 1810 1682 231 86 137 C ATOM 432 C GLY A 54 14.612 24.969 9.148 1.00 13.94 C ANISOU 432 C GLY A 54 1840 1674 1779 195 134 43 C ATOM 433 O GLY A 54 15.605 24.669 9.789 1.00 16.15 O ANISOU 433 O GLY A 54 2054 2098 1985 166 117 49 O ATOM 434 N ASN A 55 13.574 25.560 9.703 1.00 13.93 N ANISOU 434 N ASN A 55 1904 1709 1679 221 177 130 N ATOM 435 CA ASN A 55 13.597 26.034 11.065 1.00 15.50 C ANISOU 435 CA ASN A 55 2454 1590 1843 78 51 45 C ATOM 436 C ASN A 55 13.668 24.940 12.131 1.00 16.01 C ANISOU 436 C ASN A 55 2508 1806 1766 88 132 126 C ATOM 437 O ASN A 55 14.012 25.226 13.260 1.00 18.32 O ANISOU 437 O ASN A 55 3334 2055 1570 38 11 -54 O ATOM 438 CB ASN A 55 12.400 26.962 11.390 1.00 16.75 C ANISOU 438 CB ASN A 55 2511 1898 1955 308 173 86 C ATOM 439 CG ASN A 55 11.015 26.268 11.274 1.00 18.32 C ANISOU 439 CG ASN A 55 2463 2567 1931 422 556 126 C ATOM 440 OD1 ASN A 55 10.875 25.092 11.077 1.00 24.20 O ANISOU 440 OD1 ASN A 55 2884 3323 2986 228 361 81 O ATOM 441 ND2 ASN A 55 9.959 27.069 11.400 1.00 26.38 N ANISOU 441 ND2 ASN A 55 2925 3334 3763 827 458 71 N ATOM 442 N ARG A 56 13.411 23.696 11.763 1.00 15.75 N ANISOU 442 N ARG A 56 2561 1769 1652 194 187 110 N ATOM 443 CA ARG A 56 13.476 22.565 12.676 1.00 14.54 C ANISOU 443 CA ARG A 56 2262 1806 1456 112 244 80 C ATOM 444 C ARG A 56 14.838 21.863 12.689 1.00 14.12 C ANISOU 444 C ARG A 56 2096 1699 1570 -7 204 50 C ATOM 445 O ARG A 56 15.074 20.956 13.495 1.00 15.26 O ANISOU 445 O ARG A 56 2416 1672 1707 -52 -4 108 O ATOM 446 CB ARG A 56 12.359 21.621 12.310 1.00 15.92 C ANISOU 446 CB ARG A 56 2313 2126 1607 228 219 66 C ATOM 447 CG ARG A 56 12.048 20.524 13.276 1.00 17.06 C ANISOU 447 CG ARG A 56 2478 2404 1598 108 134 73 C ATOM 448 CD ARG A 56 10.694 19.924 13.021 1.00 16.95 C ANISOU 448 CD ARG A 56 2360 2333 1745 14 197 -122 C ATOM 449 NE ARG A 56 10.544 18.823 13.925 1.00 14.91 N ANISOU 449 NE ARG A 56 2030 2301 1334 -154 345 -363 N ATOM 450 CZ ARG A 56 9.749 17.809 13.751 1.00 14.88 C ANISOU 450 CZ ARG A 56 1736 2058 1860 -3 141 -214 C ATOM 451 NH1 ARG A 56 8.894 17.839 12.723 1.00 18.55 N ANISOU 451 NH1 ARG A 56 2226 3083 1738 -177 -170 -30 N ATOM 452 NH2 ARG A 56 9.766 16.817 14.587 1.00 16.61 N ANISOU 452 NH2 ARG A 56 1978 2691 1640 -142 39 -198 N ATOM 453 N GLY A 57 15.758 22.301 11.834 1.00 14.69 N ANISOU 453 N GLY A 57 2158 1711 1710 -3 319 21 N ATOM 454 CA GLY A 57 17.045 21.711 11.687 1.00 13.95 C ANISOU 454 CA GLY A 57 1977 1695 1628 -81 107 -27 C ATOM 455 C GLY A 57 17.123 20.716 10.516 1.00 13.15 C ANISOU 455 C GLY A 57 1757 1795 1443 -81 105 -69 C ATOM 456 O GLY A 57 16.191 20.555 9.743 1.00 15.20 O ANISOU 456 O GLY A 57 1921 1954 1899 135 253 -62 O ATOM 457 N PRO A 58 18.294 20.082 10.385 1.00 12.90 N ANISOU 457 N PRO A 58 1761 1578 1561 -147 154 -71 N ATOM 458 CA PRO A 58 18.554 19.235 9.221 1.00 12.46 C ANISOU 458 CA PRO A 58 1862 1407 1462 -99 164 -115 C ATOM 459 C PRO A 58 17.952 17.860 9.365 1.00 11.49 C ANISOU 459 C PRO A 58 1632 1313 1418 49 256 -281 C ATOM 460 O PRO A 58 17.986 17.255 10.458 1.00 12.68 O ANISOU 460 O PRO A 58 1715 1657 1444 -148 92 -105 O ATOM 461 CB PRO A 58 20.086 19.165 9.191 1.00 15.23 C ANISOU 461 CB PRO A 58 2121 1945 1718 -163 221 -245 C ATOM 462 CG PRO A 58 20.518 19.277 10.672 1.00 14.50 C ANISOU 462 CG PRO A 58 1583 2007 1917 -464 -50 -195 C ATOM 463 CD PRO A 58 19.487 20.214 11.237 1.00 14.12 C ANISOU 463 CD PRO A 58 1812 1800 1750 -319 60 18 C ATOM 464 N GLN A 59 17.416 17.334 8.263 1.00 12.08 N ANISOU 464 N GLN A 59 1767 1563 1261 -78 112 3 N ATOM 465 CA GLN A 59 16.952 15.931 8.178 1.00 11.26 C ANISOU 465 CA GLN A 59 1446 1392 1441 -97 74 -104 C ATOM 466 C GLN A 59 17.170 15.436 6.778 1.00 10.41 C ANISOU 466 C GLN A 59 1509 1143 1303 -25 -88 33 C ATOM 467 O GLN A 59 17.353 16.228 5.828 1.00 11.57 O ANISOU 467 O GLN A 59 1668 1316 1413 107 -4 154 O ATOM 468 CB GLN A 59 15.488 15.786 8.577 1.00 11.98 C ANISOU 468 CB GLN A 59 1613 1341 1596 -136 264 140 C ATOM 469 CG GLN A 59 14.532 16.471 7.630 1.00 13.14 C ANISOU 469 CG GLN A 59 1637 1551 1804 52 150 68 C ATOM 470 CD GLN A 59 13.083 16.307 8.018 1.00 12.89 C ANISOU 470 CD GLN A 59 1794 1583 1521 157 193 -187 C ATOM 471 OE1 GLN A 59 12.646 15.227 8.344 1.00 15.75 O ANISOU 471 OE1 GLN A 59 1678 2026 2280 -29 408 -19 O ATOM 472 NE2 GLN A 59 12.324 17.405 7.920 1.00 14.55 N ANISOU 472 NE2 GLN A 59 2036 1650 1843 366 31 -76 N ATOM 473 N ALA A 60 17.025 14.134 6.604 1.00 10.95 N ANISOU 473 N ALA A 60 1530 1203 1423 91 98 -66 N ATOM 474 CA ALA A 60 17.166 13.526 5.273 1.00 10.49 C ANISOU 474 CA ALA A 60 1459 1316 1211 152 66 32 C ATOM 475 C ALA A 60 15.976 13.835 4.374 1.00 11.90 C ANISOU 475 C ALA A 60 1585 1517 1417 17 41 -46 C ATOM 476 O ALA A 60 14.844 13.932 4.838 1.00 12.08 O ANISOU 476 O ALA A 60 1560 1604 1425 63 22 89 O ATOM 477 CB ALA A 60 17.336 12.014 5.419 1.00 11.89 C ANISOU 477 CB ALA A 60 1763 1312 1441 65 41 97 C ATOM 478 N ALA A 61 16.269 13.923 3.081 1.00 12.46 N ANISOU 478 N ALA A 61 1573 1772 1390 22 31 -50 N ATOM 479 CA ALA A 61 15.264 14.088 2.025 1.00 12.69 C ANISOU 479 CA ALA A 61 1736 1524 1563 35 -15 -52 C ATOM 480 C ALA A 61 15.693 13.159 0.887 1.00 13.00 C ANISOU 480 C ALA A 61 1707 1638 1592 105 -38 5 C ATOM 481 O ALA A 61 16.872 12.874 0.720 1.00 12.71 O ANISOU 481 O ALA A 61 1794 1540 1495 7 -56 42 O ATOM 482 CB ALA A 61 15.170 15.546 1.531 1.00 15.35 C ANISOU 482 CB ALA A 61 2523 1495 1814 173 -107 -58 C ATOM 483 N ASN A 62 14.713 12.722 0.096 1.00 13.82 N ANISOU 483 N ASN A 62 1957 1606 1686 111 -192 60 N ATOM 484 CA ASN A 62 15.026 12.081 -1.175 1.00 14.47 C ANISOU 484 CA ASN A 62 1948 1937 1611 -134 -33 -73 C ATOM 485 C ASN A 62 15.901 10.841 -0.925 1.00 14.09 C ANISOU 485 C ASN A 62 1802 1873 1679 -110 -44 -167 C ATOM 486 O ASN A 62 16.897 10.625 -1.582 1.00 15.78 O ANISOU 486 O ASN A 62 1891 2404 1700 -151 75 -51 O ATOM 487 CB ASN A 62 15.714 13.081 -2.142 1.00 17.11 C ANISOU 487 CB ASN A 62 2466 2293 1740 -252 -75 170 C ATOM 488 CG ASN A 62 15.689 12.673 -3.550 1.00 23.14 C ANISOU 488 CG ASN A 62 3046 3104 2641 -95 176 0 C ATOM 489 OD1 ASN A 62 16.591 13.065 -4.304 1.00 34.17 O ANISOU 489 OD1 ASN A 62 4488 5216 3278 -385 315 428 O ATOM 490 ND2 ASN A 62 14.655 12.008 -3.969 1.00 24.61 N ANISOU 490 ND2 ASN A 62 3626 3479 2244 -552 24 271 N ATOM 491 N VAL A 63 15.484 10.010 0.034 1.00 13.00 N ANISOU 491 N VAL A 63 1777 1536 1623 34 109 -171 N ATOM 492 CA VAL A 63 16.257 8.862 0.494 1.00 13.02 C ANISOU 492 CA VAL A 63 1832 1551 1561 98 45 -17 C ATOM 493 C VAL A 63 15.937 7.644 -0.393 1.00 14.70 C ANISOU 493 C VAL A 63 1890 1899 1794 -32 -18 -144 C ATOM 494 O VAL A 63 14.770 7.187 -0.446 1.00 15.00 O ANISOU 494 O VAL A 63 2117 1762 1818 -124 -42 -315 O ATOM 495 CB VAL A 63 15.929 8.499 1.958 1.00 12.74 C ANISOU 495 CB VAL A 63 1720 1513 1606 -62 162 12 C ATOM 496 CG1 VAL A 63 16.688 7.223 2.350 1.00 13.70 C ANISOU 496 CG1 VAL A 63 2064 1283 1858 315 1 184 C ATOM 497 CG2 VAL A 63 16.330 9.624 2.903 1.00 13.37 C ANISOU 497 CG2 VAL A 63 1885 1481 1713 76 -109 -444 C ATOM 498 N THR A 64 16.947 7.165 -1.122 1.00 15.60 N ANISOU 498 N THR A 64 2259 1674 1993 -107 87 -98 N ATOM 499 CA THR A 64 16.737 5.988 -1.972 1.00 18.41 C ANISOU 499 CA THR A 64 2744 2179 2072 11 39 -181 C ATOM 500 C THR A 64 17.585 4.847 -1.460 1.00 18.51 C ANISOU 500 C THR A 64 2580 2315 2135 146 66 -348 C ATOM 501 O THR A 64 18.758 5.007 -1.207 1.00 18.86 O ANISOU 501 O THR A 64 2756 1904 2505 115 54 -580 O ATOM 502 CB THR A 64 17.061 6.232 -3.457 1.00 20.12 C ANISOU 502 CB THR A 64 3027 2438 2178 192 134 -137 C ATOM 503 OG1 THR A 64 16.277 7.317 -3.976 1.00 22.71 O ANISOU 503 OG1 THR A 64 3120 3328 2180 495 347 6 O ATOM 504 CG2 THR A 64 16.787 4.950 -4.286 1.00 23.67 C ANISOU 504 CG2 THR A 64 3319 3039 2634 114 216 -433 C ATOM 505 N LYS A 65 16.998 3.668 -1.332 1.00 20.52 N ANISOU 505 N LYS A 65 2668 2440 2688 -52 -134 -222 N ATOM 506 CA LYS A 65 17.820 2.500 -0.953 1.00 24.60 C ANISOU 506 CA LYS A 65 3185 2997 3165 118 -114 -40 C ATOM 507 C LYS A 65 18.762 2.074 -2.113 1.00 28.67 C ANISOU 507 C LYS A 65 3852 3567 3473 107 -114 -305 C ATOM 508 O LYS A 65 18.314 1.938 -3.259 1.00 30.55 O ANISOU 508 O LYS A 65 4345 3724 3537 144 -206 -438 O ATOM 509 CB LYS A 65 16.937 1.328 -0.651 1.00 26.28 C ANISOU 509 CB LYS A 65 3415 3414 3155 23 -13 -54 C ATOM 510 CG LYS A 65 15.995 1.621 0.466 1.00 24.77 C ANISOU 510 CG LYS A 65 3514 2755 3143 309 451 93 C ATOM 511 CD LYS A 65 14.932 0.591 0.497 1.00 25.71 C ANISOU 511 CD LYS A 65 3095 3195 3478 232 -124 -141 C ATOM 512 CE LYS A 65 13.844 0.967 1.459 1.00 21.30 C ANISOU 512 CE LYS A 65 2587 2913 2589 26 33 47 C ATOM 513 NZ LYS A 65 12.751 -0.146 1.657 1.00 22.07 N ANISOU 513 NZ LYS A 65 3064 1948 3372 -83 -414 -386 N ATOM 514 N GLU A 66 20.046 1.874 -1.809 1.00 29.08 N ANISOU 514 N GLU A 66 3812 3549 3688 243 96 -209 N ATOM 515 CA GLU A 66 21.082 1.552 -2.806 1.00 31.32 C ANISOU 515 CA GLU A 66 4159 3826 3912 165 119 -77 C ATOM 516 C GLU A 66 21.635 0.171 -2.516 1.00 31.65 C ANISOU 516 C GLU A 66 4272 3677 4076 232 85 -94 C ATOM 517 O GLU A 66 21.231 -0.465 -1.549 1.00 32.80 O ANISOU 517 O GLU A 66 4341 3874 4248 220 279 -165 O ATOM 518 CB GLU A 66 22.240 2.563 -2.733 1.00 31.89 C ANISOU 518 CB GLU A 66 4148 3970 3996 133 102 -86 C ATOM 519 CG GLU A 66 21.869 4.025 -3.070 1.00 33.15 C ANISOU 519 CG GLU A 66 4640 3835 4119 22 91 -154 C ATOM 520 CD GLU A 66 21.392 4.216 -4.505 0.50 32.42 C ANISOU 520 CD GLU A 66 4367 3893 4055 81 8 -67 C ATOM 521 OE1 GLU A 66 21.600 3.314 -5.350 0.50 32.17 O ANISOU 521 OE1 GLU A 66 4213 3876 4132 30 169 -237 O ATOM 522 OE2 GLU A 66 20.813 5.279 -4.800 0.50 30.11 O ANISOU 522 OE2 GLU A 66 4241 3637 3560 135 237 -364 O TER 523 GLU A 66 ATOM 524 N MET B 1 13.450 24.243 36.862 1.00 16.69 N ANISOU 524 N MET B 1 2287 2031 2024 1 -194 -206 N ATOM 525 CA MET B 1 13.006 23.322 35.773 1.00 15.00 C ANISOU 525 CA MET B 1 1921 1974 1804 -65 -215 -129 C ATOM 526 C MET B 1 12.141 22.189 36.304 1.00 15.05 C ANISOU 526 C MET B 1 2086 1994 1635 -80 14 -114 C ATOM 527 O MET B 1 12.365 21.665 37.400 1.00 16.63 O ANISOU 527 O MET B 1 2466 1990 1862 -225 -385 37 O ATOM 528 CB MET B 1 14.191 22.628 35.099 1.00 17.47 C ANISOU 528 CB MET B 1 2009 2308 2321 26 -80 -199 C ATOM 529 CG MET B 1 15.225 23.561 34.547 1.00 23.93 C ANISOU 529 CG MET B 1 2983 3063 3044 -15 108 18 C ATOM 530 SD MET B 1 14.677 24.664 33.305 1.00 31.79 S ANISOU 530 SD MET B 1 3772 4353 3953 -16 63 187 S ATOM 531 CE MET B 1 14.254 23.523 32.168 1.00 21.83 C ANISOU 531 CE MET B 1 2327 2723 3242 14 -272 92 C ATOM 532 N LEU B 2 11.143 21.841 35.533 1.00 13.73 N ANISOU 532 N LEU B 2 2011 1845 1358 -15 -31 -212 N ATOM 533 CA LEU B 2 10.272 20.711 35.826 1.00 14.66 C ANISOU 533 CA LEU B 2 2070 2019 1479 -8 -57 -88 C ATOM 534 C LEU B 2 10.821 19.460 35.112 1.00 13.55 C ANISOU 534 C LEU B 2 1692 1952 1503 83 46 -88 C ATOM 535 O LEU B 2 11.568 19.553 34.131 1.00 14.55 O ANISOU 535 O LEU B 2 2000 2079 1448 185 171 -17 O ATOM 536 CB LEU B 2 8.827 21.001 35.362 1.00 14.96 C ANISOU 536 CB LEU B 2 2145 2000 1538 -8 -29 -169 C ATOM 537 CG LEU B 2 8.232 22.271 35.943 1.00 16.63 C ANISOU 537 CG LEU B 2 2351 2089 1876 33 50 -101 C ATOM 538 CD1 LEU B 2 6.853 22.457 35.353 1.00 17.46 C ANISOU 538 CD1 LEU B 2 2296 2071 2265 281 -10 -5 C ATOM 539 CD2 LEU B 2 8.282 22.308 37.457 1.00 17.89 C ANISOU 539 CD2 LEU B 2 2271 2647 1879 47 -247 -82 C ATOM 540 N GLU B 3 10.404 18.299 35.580 1.00 15.67 N ANISOU 540 N GLU B 3 2186 2063 1703 -27 27 -153 N ATOM 541 CA AGLU B 3 10.771 17.000 35.005 0.50 16.55 C ANISOU 541 CA AGLU B 3 2217 2139 1930 131 61 -62 C ATOM 542 CA BGLU B 3 10.764 17.065 34.911 0.50 16.50 C ANISOU 542 CA BGLU B 3 2218 2135 1916 112 66 -45 C ATOM 543 C GLU B 3 9.519 16.325 34.476 1.00 15.56 C ANISOU 543 C GLU B 3 2111 2072 1728 133 88 -143 C ATOM 544 O GLU B 3 8.448 16.407 35.122 1.00 16.44 O ANISOU 544 O GLU B 3 2192 2205 1847 -166 365 -269 O ATOM 545 CB AGLU B 3 11.389 16.065 36.065 0.50 19.05 C ANISOU 545 CB AGLU B 3 2628 2272 2335 248 55 -42 C ATOM 546 CB BGLU B 3 11.656 16.201 35.789 0.50 19.17 C ANISOU 546 CB BGLU B 3 2577 2367 2339 185 -48 -25 C ATOM 547 CG AGLU B 3 12.708 16.543 36.671 0.50 25.09 C ANISOU 547 CG AGLU B 3 3215 3152 3165 85 -124 -92 C ATOM 548 CG BGLU B 3 13.007 16.821 36.019 0.50 24.61 C ANISOU 548 CG BGLU B 3 3085 3238 3027 -49 101 17 C ATOM 549 CD AGLU B 3 13.783 16.902 35.621 0.50 29.69 C ANISOU 549 CD AGLU B 3 3678 3829 3774 13 120 -17 C ATOM 550 CD BGLU B 3 13.793 16.049 37.026 0.50 29.22 C ANISOU 550 CD BGLU B 3 3689 3884 3529 79 -160 102 C ATOM 551 OE1AGLU B 3 13.879 16.225 34.559 0.50 30.01 O ANISOU 551 OE1AGLU B 3 3910 3928 3564 -35 12 36 O ATOM 552 OE1BGLU B 3 13.196 15.676 38.061 0.50 31.42 O ANISOU 552 OE1BGLU B 3 4053 4377 3506 -47 -120 60 O ATOM 553 OE2AGLU B 3 14.540 17.873 35.868 0.50 34.30 O ANISOU 553 OE2AGLU B 3 4169 4410 4453 -140 -38 -283 O ATOM 554 OE2BGLU B 3 14.982 15.794 36.763 0.50 33.34 O ANISOU 554 OE2BGLU B 3 3850 4582 4235 18 -75 75 O ATOM 555 N GLY B 4 9.635 15.654 33.347 1.00 13.78 N ANISOU 555 N GLY B 4 1772 1899 1562 121 100 -97 N ATOM 556 CA GLY B 4 8.563 14.843 32.855 1.00 14.95 C ANISOU 556 CA GLY B 4 1828 2050 1800 99 53 -166 C ATOM 557 C GLY B 4 9.056 13.828 31.848 1.00 12.77 C ANISOU 557 C GLY B 4 1677 1763 1412 -49 120 -52 C ATOM 558 O GLY B 4 10.242 13.599 31.706 1.00 14.04 O ANISOU 558 O GLY B 4 1540 2037 1757 53 215 -183 O ATOM 559 N LYS B 5 8.099 13.181 31.199 1.00 14.54 N ANISOU 559 N LYS B 5 1873 2072 1578 72 39 158 N ATOM 560 CA ALYS B 5 8.298 12.098 30.249 0.50 15.09 C ANISOU 560 CA ALYS B 5 2109 1915 1710 141 3 62 C ATOM 561 CA BLYS B 5 8.443 12.217 30.176 0.50 14.21 C ANISOU 561 CA BLYS B 5 1966 1805 1625 155 -4 105 C ATOM 562 C LYS B 5 7.479 12.430 29.014 1.00 14.31 C ANISOU 562 C LYS B 5 1889 1812 1735 9 62 -39 C ATOM 563 O LYS B 5 6.344 12.835 29.168 1.00 15.54 O ANISOU 563 O LYS B 5 1852 2285 1765 233 123 -159 O ATOM 564 CB ALYS B 5 7.714 10.792 30.852 0.50 16.88 C ANISOU 564 CB ALYS B 5 2383 2046 1985 111 9 50 C ATOM 565 CB BLYS B 5 8.418 10.758 30.713 0.50 15.25 C ANISOU 565 CB BLYS B 5 1980 1908 1905 78 -89 192 C ATOM 566 CG ALYS B 5 8.522 10.153 31.950 0.50 20.29 C ANISOU 566 CG ALYS B 5 2806 2447 2457 59 -78 48 C ATOM 567 CG BLYS B 5 9.110 10.556 32.076 0.50 20.54 C ANISOU 567 CG BLYS B 5 2658 2567 2579 77 -55 95 C ATOM 568 CD ALYS B 5 10.032 10.280 31.699 0.50 24.50 C ANISOU 568 CD ALYS B 5 2881 3243 3185 -52 99 -23 C ATOM 569 CD BLYS B 5 8.918 9.143 32.678 0.50 25.71 C ANISOU 569 CD BLYS B 5 3459 2973 3335 9 -2 197 C ATOM 570 CE ALYS B 5 10.876 9.093 32.189 0.50 26.62 C ANISOU 570 CE ALYS B 5 3363 3221 3527 -53 62 -54 C ATOM 571 CE BLYS B 5 9.802 9.026 33.889 0.50 28.47 C ANISOU 571 CE BLYS B 5 3504 3442 3869 89 -141 -25 C ATOM 572 NZ ALYS B 5 11.474 8.352 31.024 0.50 24.23 N ANISOU 572 NZ ALYS B 5 3203 2806 3195 54 17 -60 N ATOM 573 NZ BLYS B 5 11.113 9.599 33.490 0.50 26.97 N ANISOU 573 NZ BLYS B 5 3450 3571 3224 3 0 229 N ATOM 574 N VAL B 6 7.983 12.231 27.821 1.00 13.07 N ANISOU 574 N VAL B 6 1804 1571 1591 82 90 70 N ATOM 575 CA VAL B 6 7.184 12.432 26.631 1.00 12.53 C ANISOU 575 CA VAL B 6 1645 1483 1633 -70 38 -114 C ATOM 576 C VAL B 6 6.073 11.368 26.589 1.00 14.06 C ANISOU 576 C VAL B 6 1831 1655 1856 -63 262 -62 C ATOM 577 O VAL B 6 6.319 10.171 26.606 1.00 15.70 O ANISOU 577 O VAL B 6 2014 1679 2269 -302 147 -16 O ATOM 578 CB VAL B 6 8.052 12.376 25.393 1.00 13.12 C ANISOU 578 CB VAL B 6 1504 1807 1674 -24 -151 -127 C ATOM 579 CG1 VAL B 6 7.233 12.578 24.133 1.00 13.85 C ANISOU 579 CG1 VAL B 6 1775 1887 1598 64 -269 -14 C ATOM 580 CG2 VAL B 6 9.154 13.442 25.465 1.00 14.09 C ANISOU 580 CG2 VAL B 6 1685 1860 1805 -400 317 -44 C ATOM 581 N LYS B 7 4.832 11.839 26.562 1.00 13.39 N ANISOU 581 N LYS B 7 1675 1553 1860 -19 121 -154 N ATOM 582 CA LYS B 7 3.648 10.969 26.443 1.00 14.65 C ANISOU 582 CA LYS B 7 1944 1684 1938 -179 229 -153 C ATOM 583 C LYS B 7 3.580 10.378 25.034 1.00 15.31 C ANISOU 583 C LYS B 7 2119 1714 1984 -124 81 -138 C ATOM 584 O LYS B 7 3.422 9.171 24.856 1.00 17.06 O ANISOU 584 O LYS B 7 2452 1699 2331 -133 105 -67 O ATOM 585 CB LYS B 7 2.393 11.785 26.772 1.00 14.73 C ANISOU 585 CB LYS B 7 1674 2052 1869 -320 169 -113 C ATOM 586 CG LYS B 7 1.138 10.914 26.935 1.00 16.86 C ANISOU 586 CG LYS B 7 1929 2109 2366 -269 228 -112 C ATOM 587 CD LYS B 7 -0.087 11.771 27.190 1.00 19.08 C ANISOU 587 CD LYS B 7 2069 2486 2694 -236 356 -109 C ATOM 588 CE LYS B 7 -1.328 10.932 27.313 1.00 23.39 C ANISOU 588 CE LYS B 7 2559 2686 3640 -378 -20 -218 C ATOM 589 NZ LYS B 7 -2.478 11.778 27.722 1.00 26.10 N ANISOU 589 NZ LYS B 7 2602 3366 3950 -374 354 -118 N ATOM 590 N TRP B 8 3.672 11.269 24.056 1.00 14.34 N ANISOU 590 N TRP B 8 2011 1634 1804 -149 207 -141 N ATOM 591 CA TRP B 8 3.754 10.939 22.639 1.00 14.33 C ANISOU 591 CA TRP B 8 1769 1723 1950 -249 129 -147 C ATOM 592 C TRP B 8 4.228 12.160 21.898 1.00 13.43 C ANISOU 592 C TRP B 8 1532 1777 1793 -4 75 -86 C ATOM 593 O TRP B 8 4.159 13.284 22.432 1.00 13.01 O ANISOU 593 O TRP B 8 1686 1559 1695 -157 62 -274 O ATOM 594 CB TRP B 8 2.402 10.473 22.085 1.00 15.30 C ANISOU 594 CB TRP B 8 1917 1895 1999 -298 -30 -61 C ATOM 595 CG TRP B 8 1.293 11.501 22.158 1.00 14.64 C ANISOU 595 CG TRP B 8 1723 1966 1871 -385 172 -370 C ATOM 596 CD1 TRP B 8 0.385 11.624 23.158 1.00 18.02 C ANISOU 596 CD1 TRP B 8 2130 2756 1960 -38 282 -83 C ATOM 597 CD2 TRP B 8 0.963 12.510 21.191 1.00 16.26 C ANISOU 597 CD2 TRP B 8 1704 2108 2366 -16 -71 -382 C ATOM 598 NE1 TRP B 8 -0.470 12.668 22.893 1.00 18.66 N ANISOU 598 NE1 TRP B 8 2152 2686 2251 -112 23 -176 N ATOM 599 CE2 TRP B 8 -0.156 13.208 21.683 1.00 16.77 C ANISOU 599 CE2 TRP B 8 1920 2265 2184 -156 -174 -241 C ATOM 600 CE3 TRP B 8 1.510 12.894 19.960 1.00 15.71 C ANISOU 600 CE3 TRP B 8 1951 1841 2175 -200 -176 -357 C ATOM 601 CZ2 TRP B 8 -0.733 14.257 20.993 1.00 18.10 C ANISOU 601 CZ2 TRP B 8 2342 2494 2041 -37 -158 -238 C ATOM 602 CZ3 TRP B 8 0.930 13.909 19.272 1.00 15.87 C ANISOU 602 CZ3 TRP B 8 1744 2251 2034 -166 -60 -392 C ATOM 603 CH2 TRP B 8 -0.186 14.587 19.793 1.00 16.32 C ANISOU 603 CH2 TRP B 8 1717 2315 2168 -110 -208 -288 C ATOM 604 N PHE B 9 4.757 11.953 20.709 1.00 13.64 N ANISOU 604 N PHE B 9 1584 1707 1890 -1 47 -354 N ATOM 605 CA PHE B 9 5.197 13.029 19.877 1.00 13.06 C ANISOU 605 CA PHE B 9 1705 1627 1631 131 87 -252 C ATOM 606 C PHE B 9 5.093 12.611 18.400 1.00 14.05 C ANISOU 606 C PHE B 9 1906 1644 1785 71 99 -293 C ATOM 607 O PHE B 9 5.585 11.543 17.986 1.00 18.00 O ANISOU 607 O PHE B 9 2800 1852 2188 448 149 -437 O ATOM 608 CB PHE B 9 6.641 13.411 20.240 1.00 14.48 C ANISOU 608 CB PHE B 9 1596 1925 1979 187 68 -117 C ATOM 609 CG PHE B 9 7.134 14.703 19.643 1.00 13.06 C ANISOU 609 CG PHE B 9 1360 1965 1636 -153 51 -208 C ATOM 610 CD1 PHE B 9 6.818 15.893 20.274 1.00 13.31 C ANISOU 610 CD1 PHE B 9 1635 1769 1650 -124 -20 -128 C ATOM 611 CD2 PHE B 9 7.849 14.750 18.429 1.00 13.30 C ANISOU 611 CD2 PHE B 9 1752 1766 1533 52 8 -221 C ATOM 612 CE1 PHE B 9 7.244 17.085 19.812 1.00 12.66 C ANISOU 612 CE1 PHE B 9 1573 1712 1522 -137 -158 -301 C ATOM 613 CE2 PHE B 9 8.262 15.981 17.939 1.00 13.16 C ANISOU 613 CE2 PHE B 9 1478 2065 1458 165 -36 27 C ATOM 614 CZ PHE B 9 7.975 17.140 18.638 1.00 12.66 C ANISOU 614 CZ PHE B 9 1444 1926 1440 -102 -140 -28 C ATOM 615 N ASN B 10 4.422 13.434 17.631 1.00 13.86 N ANISOU 615 N ASN B 10 1724 1884 1657 98 -6 -304 N ATOM 616 CA ASN B 10 4.280 13.209 16.183 1.00 14.90 C ANISOU 616 CA ASN B 10 1939 1915 1806 94 -133 -157 C ATOM 617 C ASN B 10 5.550 13.737 15.535 1.00 15.68 C ANISOU 617 C ASN B 10 2042 2147 1767 166 -102 -222 C ATOM 618 O ASN B 10 5.775 14.940 15.475 1.00 15.57 O ANISOU 618 O ASN B 10 1926 2288 1701 219 -278 -230 O ATOM 619 CB ASN B 10 3.037 13.951 15.669 1.00 16.71 C ANISOU 619 CB ASN B 10 2114 2336 1898 187 -211 -356 C ATOM 620 CG ASN B 10 2.786 13.745 14.206 1.00 18.18 C ANISOU 620 CG ASN B 10 1925 2962 2020 270 -11 -383 C ATOM 621 OD1 ASN B 10 3.687 13.810 13.394 1.00 18.99 O ANISOU 621 OD1 ASN B 10 2518 2857 1840 29 -120 -599 O ATOM 622 ND2 ASN B 10 1.491 13.657 13.863 1.00 26.21 N ANISOU 622 ND2 ASN B 10 2563 4112 3283 231 -404 -578 N ATOM 623 N ASER B 11 6.355 12.782 15.076 0.50 15.99 N ANISOU 623 N ASER B 11 2190 2145 1739 147 -22 -174 N ATOM 624 N BSER B 11 6.452 12.860 15.099 0.50 15.92 N ANISOU 624 N BSER B 11 2102 2183 1762 169 0 -158 N ATOM 625 CA ASER B 11 7.621 13.029 14.430 0.50 17.17 C ANISOU 625 CA ASER B 11 2283 2219 2019 110 -15 -84 C ATOM 626 CA BSER B 11 7.701 13.389 14.560 0.50 16.60 C ANISOU 626 CA BSER B 11 2149 2139 2017 126 15 -74 C ATOM 627 C ASER B 11 7.568 13.952 13.207 0.50 17.14 C ANISOU 627 C ASER B 11 2273 2229 2010 121 -34 -161 C ATOM 628 C BSER B 11 7.477 14.161 13.247 0.50 17.02 C ANISOU 628 C BSER B 11 2162 2270 2033 148 28 -163 C ATOM 629 O ASER B 11 8.447 14.797 13.001 0.50 16.76 O ANISOU 629 O ASER B 11 2544 1894 1928 131 -192 -84 O ATOM 630 O BSER B 11 8.104 15.190 13.059 0.50 18.47 O ANISOU 630 O BSER B 11 2578 2246 2190 113 -126 -112 O ATOM 631 CB ASER B 11 8.146 11.656 13.970 0.50 16.78 C ANISOU 631 CB ASER B 11 2271 2055 2047 71 -164 45 C ATOM 632 CB BSER B 11 8.765 12.286 14.388 0.50 16.70 C ANISOU 632 CB BSER B 11 1912 2168 2265 118 52 61 C ATOM 633 OG ASER B 11 9.435 11.766 13.526 0.50 17.84 O ANISOU 633 OG ASER B 11 2654 2225 1896 427 281 -93 O ATOM 634 OG BSER B 11 8.965 11.565 15.590 0.50 22.11 O ANISOU 634 OG BSER B 11 2741 2697 2961 117 -14 54 O ATOM 635 N GLU B 12 6.567 13.722 12.371 1.00 16.84 N ANISOU 635 N GLU B 12 2198 2251 1948 239 48 -273 N ATOM 636 CA GLU B 12 6.402 14.444 11.104 1.00 19.63 C ANISOU 636 CA GLU B 12 2647 2496 2315 207 -87 -151 C ATOM 637 C GLU B 12 5.995 15.894 11.351 1.00 18.26 C ANISOU 637 C GLU B 12 2503 2430 2002 171 -337 -129 C ATOM 638 O GLU B 12 6.610 16.822 10.823 1.00 21.18 O ANISOU 638 O GLU B 12 3007 3043 1994 -15 -298 -314 O ATOM 639 CB GLU B 12 5.325 13.764 10.254 1.00 20.56 C ANISOU 639 CB GLU B 12 2543 2798 2467 285 -38 -251 C ATOM 640 CG GLU B 12 5.176 14.418 8.881 1.00 24.82 C ANISOU 640 CG GLU B 12 3539 3193 2698 158 -134 -196 C ATOM 641 CD GLU B 12 4.157 13.742 7.978 1.00 30.92 C ANISOU 641 CD GLU B 12 4191 3798 3758 -133 -384 -125 C ATOM 642 OE1 GLU B 12 3.725 12.592 8.278 1.00 34.35 O ANISOU 642 OE1 GLU B 12 4714 4012 4323 -136 -514 -155 O ATOM 643 OE2 GLU B 12 3.765 14.417 6.988 1.00 34.46 O ANISOU 643 OE2 GLU B 12 4873 4621 3597 -172 -332 36 O ATOM 644 N LYS B 13 4.985 16.070 12.199 1.00 17.03 N ANISOU 644 N LYS B 13 2570 2176 1722 198 -329 -157 N ATOM 645 CA LYS B 13 4.379 17.402 12.425 1.00 17.74 C ANISOU 645 CA LYS B 13 2726 2280 1733 218 -270 -364 C ATOM 646 C LYS B 13 5.076 18.173 13.514 1.00 17.26 C ANISOU 646 C LYS B 13 2526 2164 1866 279 -248 -284 C ATOM 647 O LYS B 13 5.006 19.394 13.506 1.00 19.17 O ANISOU 647 O LYS B 13 3129 2291 1864 334 -330 -139 O ATOM 648 CB LYS B 13 2.920 17.251 12.724 1.00 20.28 C ANISOU 648 CB LYS B 13 2835 2387 2483 95 -449 -442 C ATOM 649 CG LYS B 13 2.173 16.790 11.499 1.00 24.69 C ANISOU 649 CG LYS B 13 3394 3142 2845 75 -409 -373 C ATOM 650 CD LYS B 13 0.686 16.685 11.750 1.00 31.54 C ANISOU 650 CD LYS B 13 4032 3918 4033 -59 -72 -172 C ATOM 651 CE LYS B 13 -0.027 16.375 10.420 1.00 35.81 C ANISOU 651 CE LYS B 13 4573 4635 4397 -122 -233 -159 C ATOM 652 NZ LYS B 13 -1.451 16.779 10.463 1.00 38.90 N ANISOU 652 NZ LYS B 13 4640 5052 5086 -134 -1 -19 N ATOM 653 N GLY B 14 5.818 17.475 14.397 1.00 15.08 N ANISOU 653 N GLY B 14 2191 1890 1650 197 -240 -275 N ATOM 654 CA GLY B 14 6.620 18.198 15.407 1.00 14.42 C ANISOU 654 CA GLY B 14 2189 1958 1331 83 -34 -266 C ATOM 655 C GLY B 14 5.828 18.751 16.584 1.00 13.43 C ANISOU 655 C GLY B 14 1757 1881 1463 92 -11 -72 C ATOM 656 O GLY B 14 6.154 19.847 17.042 1.00 14.82 O ANISOU 656 O GLY B 14 2209 1973 1447 88 196 -264 O ATOM 657 N PHE B 15 4.868 18.002 17.099 1.00 12.22 N ANISOU 657 N PHE B 15 1594 1734 1315 43 -67 -292 N ATOM 658 CA PHE B 15 4.206 18.352 18.342 1.00 12.64 C ANISOU 658 CA PHE B 15 1549 1754 1499 181 -88 -140 C ATOM 659 C PHE B 15 3.783 17.088 19.088 1.00 12.73 C ANISOU 659 C PHE B 15 1612 1614 1610 249 -3 -128 C ATOM 660 O PHE B 15 3.674 15.995 18.506 1.00 13.06 O ANISOU 660 O PHE B 15 1700 1562 1698 44 -8 -350 O ATOM 661 CB PHE B 15 3.020 19.290 18.073 1.00 15.46 C ANISOU 661 CB PHE B 15 1776 2089 2009 328 113 -183 C ATOM 662 CG PHE B 15 1.834 18.636 17.401 1.00 17.48 C ANISOU 662 CG PHE B 15 1985 2657 1997 435 -167 23 C ATOM 663 CD1 PHE B 15 0.828 18.035 18.130 1.00 18.51 C ANISOU 663 CD1 PHE B 15 2032 2600 2400 -15 -458 -7 C ATOM 664 CD2 PHE B 15 1.749 18.602 16.023 1.00 23.26 C ANISOU 664 CD2 PHE B 15 2631 3894 2311 7 1 -324 C ATOM 665 CE1 PHE B 15 -0.268 17.417 17.498 1.00 23.44 C ANISOU 665 CE1 PHE B 15 2538 3235 3133 -91 -223 -139 C ATOM 666 CE2 PHE B 15 0.652 17.994 15.383 1.00 27.60 C ANISOU 666 CE2 PHE B 15 3256 4104 3126 -174 -305 -169 C ATOM 667 CZ PHE B 15 -0.334 17.393 16.130 1.00 27.14 C ANISOU 667 CZ PHE B 15 3185 3815 3309 24 -167 -159 C ATOM 668 N GLY B 16 3.536 17.248 20.399 1.00 11.61 N ANISOU 668 N GLY B 16 1544 1492 1373 47 -69 -293 N ATOM 669 CA GLY B 16 3.030 16.168 21.216 1.00 12.37 C ANISOU 669 CA GLY B 16 1605 1554 1540 -43 -49 -220 C ATOM 670 C GLY B 16 2.802 16.694 22.604 1.00 11.73 C ANISOU 670 C GLY B 16 1312 1723 1421 -133 -96 -99 C ATOM 671 O GLY B 16 2.495 17.902 22.788 1.00 12.36 O ANISOU 671 O GLY B 16 1491 1617 1587 13 -67 -312 O ATOM 672 N PHE B 17 2.848 15.787 23.566 1.00 11.29 N ANISOU 672 N PHE B 17 1555 1299 1433 104 201 -115 N ATOM 673 CA PHE B 17 2.590 16.116 24.997 1.00 11.68 C ANISOU 673 CA PHE B 17 1564 1294 1580 -55 70 -135 C ATOM 674 C PHE B 17 3.624 15.493 25.894 1.00 11.83 C ANISOU 674 C PHE B 17 1332 1508 1655 -184 141 -146 C ATOM 675 O PHE B 17 4.115 14.390 25.638 1.00 12.42 O ANISOU 675 O PHE B 17 1577 1458 1684 87 -47 -141 O ATOM 676 CB PHE B 17 1.174 15.634 25.421 1.00 12.85 C ANISOU 676 CB PHE B 17 1304 1608 1970 -236 52 8 C ATOM 677 CG PHE B 17 0.080 16.552 25.035 1.00 12.59 C ANISOU 677 CG PHE B 17 1263 1710 1809 -176 191 -101 C ATOM 678 CD1 PHE B 17 -0.547 16.400 23.824 1.00 16.31 C ANISOU 678 CD1 PHE B 17 1751 2291 2153 17 -54 -43 C ATOM 679 CD2 PHE B 17 -0.351 17.561 25.884 1.00 13.24 C ANISOU 679 CD2 PHE B 17 1319 1808 1902 -124 -27 -114 C ATOM 680 CE1 PHE B 17 -1.530 17.261 23.430 1.00 16.21 C ANISOU 680 CE1 PHE B 17 1415 2539 2204 58 -348 -249 C ATOM 681 CE2 PHE B 17 -1.358 18.444 25.470 1.00 14.58 C ANISOU 681 CE2 PHE B 17 1414 1786 2336 -57 86 -84 C ATOM 682 CZ PHE B 17 -1.943 18.275 24.267 1.00 16.67 C ANISOU 682 CZ PHE B 17 1828 2161 2342 299 -100 -24 C ATOM 683 N ILE B 18 3.921 16.239 26.956 1.00 11.13 N ANISOU 683 N ILE B 18 1332 1512 1384 -90 -101 -163 N ATOM 684 CA ILE B 18 4.749 15.819 28.070 1.00 12.29 C ANISOU 684 CA ILE B 18 1232 1801 1637 26 152 -2 C ATOM 685 C ILE B 18 3.869 15.501 29.242 1.00 12.77 C ANISOU 685 C ILE B 18 1505 1729 1617 -20 145 28 C ATOM 686 O ILE B 18 3.033 16.314 29.644 1.00 14.15 O ANISOU 686 O ILE B 18 1627 2010 1738 22 393 -14 O ATOM 687 CB ILE B 18 5.759 16.915 28.458 1.00 11.24 C ANISOU 687 CB ILE B 18 1232 1540 1497 43 101 -17 C ATOM 688 CG1 ILE B 18 6.714 17.197 27.278 1.00 12.77 C ANISOU 688 CG1 ILE B 18 1451 1883 1518 -55 42 150 C ATOM 689 CG2 ILE B 18 6.556 16.523 29.714 1.00 12.84 C ANISOU 689 CG2 ILE B 18 1536 1837 1506 24 -139 -28 C ATOM 690 CD1 ILE B 18 7.547 18.463 27.414 1.00 13.72 C ANISOU 690 CD1 ILE B 18 1674 1545 1991 -252 15 234 C ATOM 691 N GLU B 19 4.091 14.341 29.816 1.00 14.12 N ANISOU 691 N GLU B 19 1704 1985 1676 213 335 48 N ATOM 692 CA GLU B 19 3.388 13.985 31.032 1.00 14.78 C ANISOU 692 CA GLU B 19 1786 2052 1777 42 362 76 C ATOM 693 C GLU B 19 4.237 14.328 32.239 1.00 14.92 C ANISOU 693 C GLU B 19 1738 2091 1839 63 353 122 C ATOM 694 O GLU B 19 5.441 14.156 32.250 1.00 16.43 O ANISOU 694 O GLU B 19 1716 2780 1747 134 252 292 O ATOM 695 CB GLU B 19 2.893 12.546 30.962 1.00 19.58 C ANISOU 695 CB GLU B 19 2390 2649 2401 -187 516 395 C ATOM 696 CG GLU B 19 3.787 11.449 30.939 1.00 24.88 C ANISOU 696 CG GLU B 19 3108 3222 3120 -145 352 178 C ATOM 697 CD GLU B 19 3.029 10.133 30.605 0.50 25.70 C ANISOU 697 CD GLU B 19 3250 2947 3564 -196 129 149 C ATOM 698 OE1 GLU B 19 1.780 10.016 30.826 0.50 23.13 O ANISOU 698 OE1 GLU B 19 3160 2242 3387 119 42 379 O ATOM 699 OE2 GLU B 19 3.687 9.230 30.077 0.50 30.83 O ANISOU 699 OE2 GLU B 19 3966 3480 4267 -57 253 119 O ATOM 700 N VAL B 20 3.562 14.832 33.255 1.00 16.42 N ANISOU 700 N VAL B 20 1983 2379 1875 87 344 65 N ATOM 701 CA VAL B 20 4.186 15.468 34.432 1.00 17.04 C ANISOU 701 CA VAL B 20 2148 2322 2002 -48 304 132 C ATOM 702 C VAL B 20 3.397 14.915 35.619 1.00 17.43 C ANISOU 702 C VAL B 20 2015 2531 2076 -90 310 179 C ATOM 703 O VAL B 20 2.180 15.136 35.730 1.00 18.99 O ANISOU 703 O VAL B 20 2351 2929 1932 231 462 163 O ATOM 704 CB VAL B 20 4.047 16.999 34.393 1.00 18.54 C ANISOU 704 CB VAL B 20 2486 2451 2107 -103 362 89 C ATOM 705 CG1 VAL B 20 4.837 17.644 35.543 1.00 20.92 C ANISOU 705 CG1 VAL B 20 2931 2623 2393 -118 76 258 C ATOM 706 CG2 VAL B 20 4.536 17.519 33.074 1.00 22.63 C ANISOU 706 CG2 VAL B 20 3281 2776 2541 28 462 379 C ATOM 707 N GLU B 21 4.089 14.226 36.501 1.00 18.51 N ANISOU 707 N GLU B 21 2351 2477 2204 -3 504 187 N ATOM 708 CA GLU B 21 3.422 13.607 37.636 1.00 20.40 C ANISOU 708 CA GLU B 21 2738 2606 2406 -14 424 253 C ATOM 709 C GLU B 21 2.598 14.619 38.409 1.00 20.27 C ANISOU 709 C GLU B 21 2680 2661 2360 -46 362 187 C ATOM 710 O GLU B 21 3.094 15.648 38.785 1.00 19.70 O ANISOU 710 O GLU B 21 2688 2668 2129 101 576 265 O ATOM 711 CB GLU B 21 4.439 12.967 38.550 1.00 21.76 C ANISOU 711 CB GLU B 21 2882 2937 2447 -29 287 354 C ATOM 712 CG GLU B 21 5.101 11.746 37.945 1.00 28.36 C ANISOU 712 CG GLU B 21 3820 3555 3398 13 95 56 C ATOM 713 CD GLU B 21 6.147 11.106 38.858 0.50 31.00 C ANISOU 713 CD GLU B 21 4087 3811 3880 132 -76 146 C ATOM 714 OE1 GLU B 21 6.125 11.356 40.083 0.50 34.23 O ANISOU 714 OE1 GLU B 21 4705 4251 4047 77 -137 149 O ATOM 715 OE2 GLU B 21 6.994 10.354 38.333 0.50 35.10 O ANISOU 715 OE2 GLU B 21 4629 4257 4449 168 42 78 O ATOM 716 N GLY B 22 1.337 14.275 38.670 1.00 19.29 N ANISOU 716 N GLY B 22 2535 2658 2133 -7 473 155 N ATOM 717 CA GLY B 22 0.462 15.108 39.489 1.00 20.78 C ANISOU 717 CA GLY B 22 2557 2840 2498 -45 605 153 C ATOM 718 C GLY B 22 -0.273 16.251 38.818 1.00 19.96 C ANISOU 718 C GLY B 22 2537 2744 2300 -33 460 112 C ATOM 719 O GLY B 22 -0.949 16.999 39.476 1.00 21.03 O ANISOU 719 O GLY B 22 2599 2871 2520 -224 775 135 O ATOM 720 N GLN B 23 -0.084 16.489 37.524 1.00 19.01 N ANISOU 720 N GLN B 23 2250 2775 2195 10 690 158 N ATOM 721 CA GLN B 23 -0.713 17.616 36.885 1.00 18.14 C ANISOU 721 CA GLN B 23 1996 2637 2258 9 454 77 C ATOM 722 C GLN B 23 -0.997 17.313 35.426 1.00 17.33 C ANISOU 722 C GLN B 23 1902 2569 2113 -86 606 138 C ATOM 723 O GLN B 23 -0.647 16.250 34.947 1.00 17.55 O ANISOU 723 O GLN B 23 1952 2509 2205 -216 499 156 O ATOM 724 CB GLN B 23 0.131 18.870 37.082 1.00 17.46 C ANISOU 724 CB GLN B 23 2022 2585 2025 -41 478 41 C ATOM 725 CG GLN B 23 1.461 18.850 36.349 1.00 16.33 C ANISOU 725 CG GLN B 23 2046 2202 1954 162 389 294 C ATOM 726 CD GLN B 23 2.354 19.992 36.798 1.00 17.71 C ANISOU 726 CD GLN B 23 2297 2335 2096 -14 257 185 C ATOM 727 OE1 GLN B 23 2.915 19.973 37.899 1.00 22.17 O ANISOU 727 OE1 GLN B 23 2918 3191 2315 -199 65 271 O ATOM 728 NE2 GLN B 23 2.482 21.034 35.948 1.00 19.68 N ANISOU 728 NE2 GLN B 23 2717 2423 2338 69 413 360 N ATOM 729 N ASP B 24 -1.661 18.250 34.743 1.00 16.66 N ANISOU 729 N ASP B 24 1684 2670 1974 105 549 28 N ATOM 730 CA ASP B 24 -2.100 18.088 33.375 1.00 18.83 C ANISOU 730 CA ASP B 24 2079 2748 2325 62 338 30 C ATOM 731 C ASP B 24 -0.877 17.884 32.468 1.00 15.51 C ANISOU 731 C ASP B 24 1654 2252 1985 -53 386 8 C ATOM 732 O ASP B 24 0.180 18.479 32.650 1.00 15.32 O ANISOU 732 O ASP B 24 1830 2009 1980 -16 275 38 O ATOM 733 CB ASP B 24 -2.873 19.326 32.897 1.00 21.55 C ANISOU 733 CB ASP B 24 2390 3147 2649 185 287 26 C ATOM 734 CG ASP B 24 -4.274 19.412 33.481 1.00 26.70 C ANISOU 734 CG ASP B 24 3022 3656 3466 201 199 -2 C ATOM 735 OD1 ASP B 24 -4.638 18.544 34.301 1.00 28.43 O ANISOU 735 OD1 ASP B 24 2578 5014 3210 123 846 -118 O ATOM 736 OD2 ASP B 24 -5.002 20.331 33.045 1.00 35.35 O ANISOU 736 OD2 ASP B 24 3364 5162 4904 832 83 -201 O ATOM 737 N ASP B 25 -1.074 17.086 31.436 1.00 15.39 N ANISOU 737 N ASP B 25 1584 2385 1878 -158 398 -59 N ATOM 738 CA ASP B 25 -0.096 16.980 30.358 1.00 13.46 C ANISOU 738 CA ASP B 25 1341 1945 1826 -72 218 -33 C ATOM 739 C ASP B 25 0.175 18.374 29.773 1.00 13.20 C ANISOU 739 C ASP B 25 1478 1700 1837 -161 24 -51 C ATOM 740 O ASP B 25 -0.697 19.213 29.720 1.00 13.75 O ANISOU 740 O ASP B 25 1339 1661 2220 -126 265 23 O ATOM 741 CB ASP B 25 -0.628 16.148 29.188 1.00 13.29 C ANISOU 741 CB ASP B 25 1328 1627 2092 -159 278 -142 C ATOM 742 CG ASP B 25 -0.957 14.715 29.567 1.00 17.45 C ANISOU 742 CG ASP B 25 2379 2003 2247 -204 70 -161 C ATOM 743 OD1 ASP B 25 -0.366 14.209 30.525 1.00 17.88 O ANISOU 743 OD1 ASP B 25 2151 2065 2574 -542 345 79 O ATOM 744 OD2 ASP B 25 -1.775 14.118 28.832 1.00 21.61 O ANISOU 744 OD2 ASP B 25 2556 2075 3580 -436 -264 -170 O ATOM 745 N VAL B 26 1.408 18.614 29.328 1.00 11.56 N ANISOU 745 N VAL B 26 1257 1525 1609 -156 256 -53 N ATOM 746 CA VAL B 26 1.835 19.903 28.770 1.00 11.98 C ANISOU 746 CA VAL B 26 1434 1599 1519 -137 74 -36 C ATOM 747 C VAL B 26 2.135 19.706 27.271 1.00 11.08 C ANISOU 747 C VAL B 26 1349 1325 1534 -93 91 24 C ATOM 748 O VAL B 26 2.931 18.865 26.855 1.00 11.69 O ANISOU 748 O VAL B 26 1380 1460 1601 -20 55 -146 O ATOM 749 CB VAL B 26 3.093 20.408 29.528 1.00 12.13 C ANISOU 749 CB VAL B 26 1585 1609 1412 -21 172 -77 C ATOM 750 CG1 VAL B 26 3.573 21.725 28.916 1.00 13.39 C ANISOU 750 CG1 VAL B 26 1886 1469 1730 -177 255 205 C ATOM 751 CG2 VAL B 26 2.782 20.497 31.029 1.00 13.94 C ANISOU 751 CG2 VAL B 26 1885 1958 1450 -364 229 -41 C ATOM 752 N PHE B 27 1.462 20.493 26.445 1.00 10.99 N ANISOU 752 N PHE B 27 1292 1427 1456 86 157 -85 N ATOM 753 CA PHE B 27 1.697 20.516 25.015 1.00 10.60 C ANISOU 753 CA PHE B 27 1147 1495 1386 -109 -29 2 C ATOM 754 C PHE B 27 3.097 20.964 24.717 1.00 11.27 C ANISOU 754 C PHE B 27 1192 1526 1564 16 79 -104 C ATOM 755 O PHE B 27 3.596 21.912 25.340 1.00 11.77 O ANISOU 755 O PHE B 27 1206 1649 1617 13 -92 -204 O ATOM 756 CB PHE B 27 0.715 21.483 24.397 1.00 11.75 C ANISOU 756 CB PHE B 27 1312 1534 1617 59 -76 -86 C ATOM 757 CG PHE B 27 0.839 21.608 22.901 1.00 11.64 C ANISOU 757 CG PHE B 27 1456 1386 1579 146 -43 -74 C ATOM 758 CD1 PHE B 27 0.211 20.691 22.073 1.00 14.14 C ANISOU 758 CD1 PHE B 27 1731 1945 1696 122 51 -135 C ATOM 759 CD2 PHE B 27 1.605 22.595 22.336 1.00 12.95 C ANISOU 759 CD2 PHE B 27 1557 1678 1686 329 -196 72 C ATOM 760 CE1 PHE B 27 0.339 20.780 20.713 1.00 15.62 C ANISOU 760 CE1 PHE B 27 2073 2091 1770 182 -81 -180 C ATOM 761 CE2 PHE B 27 1.720 22.696 20.953 1.00 16.22 C ANISOU 761 CE2 PHE B 27 1795 2248 2117 297 101 79 C ATOM 762 CZ PHE B 27 1.052 21.739 20.150 1.00 15.48 C ANISOU 762 CZ PHE B 27 1783 2343 1754 405 -1 101 C ATOM 763 N VAL B 28 3.749 20.292 23.767 1.00 10.93 N ANISOU 763 N VAL B 28 1306 1480 1364 -31 83 -256 N ATOM 764 CA VAL B 28 5.106 20.671 23.357 1.00 11.12 C ANISOU 764 CA VAL B 28 1382 1523 1318 -79 -82 -66 C ATOM 765 C VAL B 28 5.178 20.777 21.842 1.00 11.66 C ANISOU 765 C VAL B 28 1427 1698 1303 -79 25 -110 C ATOM 766 O VAL B 28 4.800 19.837 21.105 1.00 12.52 O ANISOU 766 O VAL B 28 1670 1597 1488 -226 -111 -106 O ATOM 767 CB VAL B 28 6.194 19.696 23.902 1.00 9.69 C ANISOU 767 CB VAL B 28 1198 1345 1137 -74 17 16 C ATOM 768 CG1 VAL B 28 5.851 18.225 23.580 1.00 11.63 C ANISOU 768 CG1 VAL B 28 1650 1320 1447 -72 -2 -26 C ATOM 769 CG2 VAL B 28 7.588 20.102 23.425 1.00 11.99 C ANISOU 769 CG2 VAL B 28 1251 1759 1545 -233 182 -109 C ATOM 770 N HIS B 29 5.711 21.898 21.366 1.00 12.06 N ANISOU 770 N HIS B 29 1581 1806 1194 -143 100 -131 N ATOM 771 CA HIS B 29 5.950 22.107 19.946 1.00 11.72 C ANISOU 771 CA HIS B 29 1588 1712 1150 -28 -34 -64 C ATOM 772 C HIS B 29 7.467 21.974 19.737 1.00 12.59 C ANISOU 772 C HIS B 29 1698 1942 1141 40 3 56 C ATOM 773 O HIS B 29 8.274 22.264 20.624 1.00 11.66 O ANISOU 773 O HIS B 29 1467 1818 1146 -29 38 -51 O ATOM 774 CB HIS B 29 5.450 23.495 19.575 1.00 13.96 C ANISOU 774 CB HIS B 29 1858 2080 1364 132 -153 68 C ATOM 775 CG HIS B 29 5.594 23.829 18.141 1.00 14.36 C ANISOU 775 CG HIS B 29 2110 1727 1616 316 -61 62 C ATOM 776 ND1 HIS B 29 6.640 24.591 17.671 1.00 16.60 N ANISOU 776 ND1 HIS B 29 2254 2258 1795 488 109 317 N ATOM 777 CD2 HIS B 29 4.886 23.425 17.056 1.00 17.40 C ANISOU 777 CD2 HIS B 29 2036 2529 2043 221 -149 130 C ATOM 778 CE1 HIS B 29 6.520 24.714 16.352 1.00 17.91 C ANISOU 778 CE1 HIS B 29 2562 2317 1923 91 -127 471 C ATOM 779 NE2 HIS B 29 5.482 23.997 15.954 1.00 18.23 N ANISOU 779 NE2 HIS B 29 2629 2461 1834 60 -150 306 N ATOM 780 N PHE B 30 7.881 21.633 18.517 1.00 12.38 N ANISOU 780 N PHE B 30 1661 1996 1044 32 20 -184 N ATOM 781 CA PHE B 30 9.303 21.356 18.268 1.00 13.20 C ANISOU 781 CA PHE B 30 1896 1967 1150 118 125 -91 C ATOM 782 C PHE B 30 10.193 22.567 18.562 1.00 13.28 C ANISOU 782 C PHE B 30 1926 2047 1073 56 213 111 C ATOM 783 O PHE B 30 11.356 22.395 18.864 1.00 14.08 O ANISOU 783 O PHE B 30 1819 2027 1502 -89 252 -158 O ATOM 784 CB PHE B 30 9.522 20.857 16.845 1.00 13.75 C ANISOU 784 CB PHE B 30 1869 2193 1160 162 250 16 C ATOM 785 CG PHE B 30 9.259 21.882 15.754 1.00 13.73 C ANISOU 785 CG PHE B 30 1839 1823 1554 227 228 -182 C ATOM 786 CD1 PHE B 30 10.218 22.818 15.422 1.00 16.66 C ANISOU 786 CD1 PHE B 30 2326 2379 1622 -33 146 -165 C ATOM 787 CD2 PHE B 30 8.094 21.810 15.002 1.00 14.99 C ANISOU 787 CD2 PHE B 30 2103 2360 1232 -144 302 -78 C ATOM 788 CE1 PHE B 30 10.007 23.697 14.369 1.00 18.89 C ANISOU 788 CE1 PHE B 30 2906 2368 1901 -84 242 141 C ATOM 789 CE2 PHE B 30 7.873 22.680 13.932 1.00 17.19 C ANISOU 789 CE2 PHE B 30 2404 2532 1595 84 -357 -132 C ATOM 790 CZ PHE B 30 8.829 23.624 13.645 1.00 20.50 C ANISOU 790 CZ PHE B 30 2877 2937 1974 13 130 468 C ATOM 791 N SER B 31 9.648 23.773 18.380 1.00 13.20 N ANISOU 791 N SER B 31 1955 1608 1452 -80 111 48 N ATOM 792 CA SER B 31 10.395 25.014 18.601 1.00 14.74 C ANISOU 792 CA SER B 31 2010 1944 1645 -162 120 147 C ATOM 793 C SER B 31 10.910 25.171 20.033 1.00 13.65 C ANISOU 793 C SER B 31 1866 1742 1576 -134 116 12 C ATOM 794 O SER B 31 11.855 25.931 20.283 1.00 16.49 O ANISOU 794 O SER B 31 2236 2264 1764 -435 246 150 O ATOM 795 CB SER B 31 9.567 26.235 18.218 1.00 16.99 C ANISOU 795 CB SER B 31 2313 2188 1952 -161 -103 214 C ATOM 796 OG SER B 31 8.380 26.308 18.964 1.00 17.89 O ANISOU 796 OG SER B 31 2879 1875 2040 218 -57 150 O ATOM 797 N ALA B 32 10.342 24.403 20.976 1.00 12.67 N ANISOU 797 N ALA B 32 1760 1652 1402 -92 103 82 N ATOM 798 CA ALA B 32 10.776 24.455 22.356 1.00 11.95 C ANISOU 798 CA ALA B 32 1684 1459 1396 -94 32 -132 C ATOM 799 C ALA B 32 11.975 23.585 22.611 1.00 11.58 C ANISOU 799 C ALA B 32 1381 1627 1390 -193 119 16 C ATOM 800 O ALA B 32 12.587 23.660 23.688 1.00 12.99 O ANISOU 800 O ALA B 32 1638 1897 1400 -200 4 -159 O ATOM 801 CB ALA B 32 9.619 24.018 23.290 1.00 12.50 C ANISOU 801 CB ALA B 32 1529 1690 1528 -118 194 136 C ATOM 802 N ILE B 33 12.329 22.689 21.674 1.00 12.26 N ANISOU 802 N ILE B 33 1701 1514 1442 -180 200 -142 N ATOM 803 CA ILE B 33 13.335 21.670 21.953 1.00 12.81 C ANISOU 803 CA ILE B 33 1722 1790 1352 -298 22 -114 C ATOM 804 C ILE B 33 14.731 22.245 21.819 1.00 14.12 C ANISOU 804 C ILE B 33 1782 1934 1647 -111 188 -108 C ATOM 805 O ILE B 33 15.062 22.818 20.775 1.00 16.24 O ANISOU 805 O ILE B 33 2074 2280 1814 -497 224 26 O ATOM 806 CB ILE B 33 13.155 20.460 21.014 1.00 12.30 C ANISOU 806 CB ILE B 33 1804 1559 1309 -156 0 117 C ATOM 807 CG1 ILE B 33 11.745 19.838 21.217 1.00 12.39 C ANISOU 807 CG1 ILE B 33 1671 1542 1493 -238 210 -47 C ATOM 808 CG2 ILE B 33 14.212 19.426 21.275 1.00 13.77 C ANISOU 808 CG2 ILE B 33 1755 1738 1737 267 73 -148 C ATOM 809 CD1 ILE B 33 11.394 18.825 20.127 1.00 13.29 C ANISOU 809 CD1 ILE B 33 1735 1835 1477 -51 -1 -267 C ATOM 810 N GLN B 34 15.535 22.050 22.861 1.00 14.14 N ANISOU 810 N GLN B 34 1752 1830 1788 -296 249 -129 N ATOM 811 CA GLN B 34 16.893 22.538 22.935 1.00 16.29 C ANISOU 811 CA GLN B 34 1880 2244 2065 -379 100 -291 C ATOM 812 C GLN B 34 17.865 21.560 22.301 1.00 16.13 C ANISOU 812 C GLN B 34 1714 1981 2434 -312 200 -138 C ATOM 813 O GLN B 34 17.528 20.418 21.985 1.00 16.70 O ANISOU 813 O GLN B 34 1720 2116 2508 -302 473 -302 O ATOM 814 CB GLN B 34 17.279 22.782 24.396 1.00 16.53 C ANISOU 814 CB GLN B 34 1700 2388 2189 -560 -126 -297 C ATOM 815 CG GLN B 34 16.346 23.702 25.133 1.00 18.22 C ANISOU 815 CG GLN B 34 1990 2359 2574 -438 44 -375 C ATOM 816 CD GLN B 34 16.230 25.038 24.485 1.00 16.77 C ANISOU 816 CD GLN B 34 2050 1861 2459 -548 276 -223 C ATOM 817 OE1 GLN B 34 17.235 25.793 24.499 1.00 24.55 O ANISOU 817 OE1 GLN B 34 2511 2760 4055 -1159 275 -359 O ATOM 818 NE2 GLN B 34 15.100 25.343 23.830 1.00 18.49 N ANISOU 818 NE2 GLN B 34 2498 2161 2365 -449 370 -475 N ATOM 819 N GLY B 35 19.098 22.008 22.116 1.00 17.52 N ANISOU 819 N GLY B 35 1678 2286 2689 -147 202 -162 N ATOM 820 CA GLY B 35 20.152 21.146 21.610 1.00 18.71 C ANISOU 820 CA GLY B 35 1986 2382 2739 -165 58 -183 C ATOM 821 C GLY B 35 20.311 21.378 20.125 1.00 18.13 C ANISOU 821 C GLY B 35 1629 2442 2817 -242 243 -20 C ATOM 822 O GLY B 35 19.802 22.358 19.559 1.00 21.93 O ANISOU 822 O GLY B 35 2286 3295 2749 -21 283 126 O ATOM 823 N GLU B 36 21.028 20.449 19.515 1.00 18.22 N ANISOU 823 N GLU B 36 1930 2420 2572 -463 139 -309 N ATOM 824 CA GLU B 36 21.433 20.526 18.131 1.00 21.95 C ANISOU 824 CA GLU B 36 2467 3037 2834 -280 89 -279 C ATOM 825 C GLU B 36 20.634 19.496 17.304 1.00 20.16 C ANISOU 825 C GLU B 36 2395 2641 2621 -293 231 -313 C ATOM 826 O GLU B 36 19.868 18.654 17.824 1.00 21.58 O ANISOU 826 O GLU B 36 2720 2889 2591 -457 528 -474 O ATOM 827 CB GLU B 36 22.970 20.303 18.002 1.00 25.83 C ANISOU 827 CB GLU B 36 2827 3593 3392 -147 217 -243 C ATOM 828 CG GLU B 36 23.869 20.887 19.150 1.00 29.86 C ANISOU 828 CG GLU B 36 3347 3990 4009 -77 174 -27 C ATOM 829 CD GLU B 36 23.496 22.300 19.512 1.00 34.71 C ANISOU 829 CD GLU B 36 4019 4277 4893 -424 98 -164 C ATOM 830 OE1 GLU B 36 23.376 23.101 18.553 1.00 42.34 O ANISOU 830 OE1 GLU B 36 4970 5715 5399 -317 93 413 O ATOM 831 OE2 GLU B 36 23.250 22.596 20.730 1.00 31.16 O ANISOU 831 OE2 GLU B 36 2987 4337 4514 -1230 -258 15 O ATOM 832 N GLY B 37 20.780 19.593 15.999 1.00 19.15 N ANISOU 832 N GLY B 37 2218 2470 2584 -309 216 -84 N ATOM 833 CA GLY B 37 20.170 18.650 15.105 1.00 18.92 C ANISOU 833 CA GLY B 37 2227 2583 2376 -59 220 -155 C ATOM 834 C GLY B 37 18.714 18.886 14.854 1.00 16.08 C ANISOU 834 C GLY B 37 1997 2037 2076 -44 147 17 C ATOM 835 O GLY B 37 18.153 19.977 15.083 1.00 19.00 O ANISOU 835 O GLY B 37 2259 2185 2776 -51 351 -318 O ATOM 836 N PHE B 38 18.067 17.850 14.362 1.00 14.21 N ANISOU 836 N PHE B 38 2086 1705 1605 -24 372 -72 N ATOM 837 CA PHE B 38 16.653 17.921 14.054 1.00 13.95 C ANISOU 837 CA PHE B 38 2067 1732 1501 70 135 106 C ATOM 838 C PHE B 38 15.875 17.931 15.364 1.00 13.32 C ANISOU 838 C PHE B 38 1707 1801 1551 194 184 71 C ATOM 839 O PHE B 38 16.056 17.052 16.185 1.00 13.84 O ANISOU 839 O PHE B 38 2014 1702 1543 216 185 122 O ATOM 840 CB PHE B 38 16.204 16.746 13.181 1.00 13.76 C ANISOU 840 CB PHE B 38 2103 1762 1360 31 251 -4 C ATOM 841 CG PHE B 38 14.833 16.902 12.617 1.00 14.05 C ANISOU 841 CG PHE B 38 1993 1841 1505 171 223 -177 C ATOM 842 CD1 PHE B 38 14.565 17.883 11.658 1.00 14.79 C ANISOU 842 CD1 PHE B 38 1994 2018 1604 -82 373 -58 C ATOM 843 CD2 PHE B 38 13.800 16.057 13.003 1.00 14.34 C ANISOU 843 CD2 PHE B 38 2283 1605 1558 293 314 -208 C ATOM 844 CE1 PHE B 38 13.318 18.024 11.119 1.00 14.84 C ANISOU 844 CE1 PHE B 38 2238 1962 1435 59 142 -79 C ATOM 845 CE2 PHE B 38 12.562 16.183 12.435 1.00 15.29 C ANISOU 845 CE2 PHE B 38 2180 1994 1633 -63 404 -328 C ATOM 846 CZ PHE B 38 12.315 17.169 11.500 1.00 15.29 C ANISOU 846 CZ PHE B 38 1899 2075 1836 171 180 -287 C ATOM 847 N LYS B 39 14.985 18.891 15.530 1.00 12.80 N ANISOU 847 N LYS B 39 1892 1786 1183 161 269 151 N ATOM 848 CA LYS B 39 14.258 19.058 16.783 1.00 12.57 C ANISOU 848 CA LYS B 39 1612 1806 1357 140 282 29 C ATOM 849 C LYS B 39 13.089 18.078 16.850 1.00 12.53 C ANISOU 849 C LYS B 39 1688 1609 1463 235 131 -153 C ATOM 850 O LYS B 39 12.114 18.213 16.111 1.00 13.90 O ANISOU 850 O LYS B 39 1917 1889 1472 133 105 -101 O ATOM 851 CB LYS B 39 13.784 20.501 16.913 1.00 13.33 C ANISOU 851 CB LYS B 39 1818 1836 1409 306 179 -144 C ATOM 852 CG LYS B 39 14.892 21.527 16.964 1.00 16.24 C ANISOU 852 CG LYS B 39 2037 2031 2101 0 367 -131 C ATOM 853 CD LYS B 39 14.403 22.949 17.177 1.00 22.27 C ANISOU 853 CD LYS B 39 2804 2856 2799 212 195 -103 C ATOM 854 CE LYS B 39 15.612 23.883 17.161 1.00 27.87 C ANISOU 854 CE LYS B 39 3310 3549 3730 -144 253 -84 C ATOM 855 NZ LYS B 39 16.698 23.507 18.150 1.00 34.57 N ANISOU 855 NZ LYS B 39 4183 4422 4529 -239 -111 -94 N ATOM 856 N THR B 40 13.201 17.095 17.730 1.00 12.31 N ANISOU 856 N THR B 40 1684 1625 1367 91 202 -47 N ATOM 857 CA THR B 40 12.187 16.064 17.826 1.00 12.48 C ANISOU 857 CA THR B 40 1681 1652 1408 145 138 -135 C ATOM 858 C THR B 40 12.296 15.379 19.199 1.00 10.90 C ANISOU 858 C THR B 40 1459 1473 1208 97 142 -67 C ATOM 859 O THR B 40 13.276 15.573 19.953 1.00 12.30 O ANISOU 859 O THR B 40 1524 1801 1348 -48 75 -23 O ATOM 860 CB THR B 40 12.281 15.052 16.659 1.00 12.23 C ANISOU 860 CB THR B 40 1902 1419 1326 93 88 -70 C ATOM 861 OG1 THR B 40 11.034 14.347 16.593 1.00 14.50 O ANISOU 861 OG1 THR B 40 1860 2059 1589 32 30 -266 O ATOM 862 CG2 THR B 40 13.449 14.104 16.837 1.00 14.46 C ANISOU 862 CG2 THR B 40 1905 1729 1860 152 208 -311 C ATOM 863 N LEU B 41 11.284 14.590 19.540 1.00 12.24 N ANISOU 863 N LEU B 41 1490 1707 1450 -44 36 4 N ATOM 864 CA LEU B 41 11.186 13.838 20.768 1.00 11.11 C ANISOU 864 CA LEU B 41 1384 1445 1392 40 32 -20 C ATOM 865 C LEU B 41 10.599 12.478 20.468 1.00 12.49 C ANISOU 865 C LEU B 41 1660 1531 1554 85 -41 -89 C ATOM 866 O LEU B 41 9.917 12.314 19.466 1.00 13.68 O ANISOU 866 O LEU B 41 1754 1779 1664 -2 -57 -58 O ATOM 867 CB LEU B 41 10.280 14.585 21.779 1.00 11.81 C ANISOU 867 CB LEU B 41 1550 1582 1352 20 50 -54 C ATOM 868 CG LEU B 41 10.734 15.930 22.326 1.00 11.06 C ANISOU 868 CG LEU B 41 1450 1511 1240 -3 207 47 C ATOM 869 CD1 LEU B 41 9.600 16.665 22.995 1.00 11.95 C ANISOU 869 CD1 LEU B 41 1418 1505 1617 329 163 -280 C ATOM 870 CD2 LEU B 41 11.937 15.782 23.250 1.00 12.73 C ANISOU 870 CD2 LEU B 41 1220 1971 1644 67 -66 -229 C ATOM 871 N GLU B 42 10.817 11.550 21.387 1.00 13.74 N ANISOU 871 N GLU B 42 1819 1760 1642 -114 -106 -48 N ATOM 872 CA GLU B 42 10.275 10.194 21.287 1.00 14.95 C ANISOU 872 CA GLU B 42 2147 1647 1886 -84 -10 -84 C ATOM 873 C GLU B 42 9.486 9.824 22.515 1.00 14.30 C ANISOU 873 C GLU B 42 1921 1540 1972 34 -23 -119 C ATOM 874 O GLU B 42 9.828 10.251 23.615 1.00 14.16 O ANISOU 874 O GLU B 42 1923 1631 1824 -49 19 -54 O ATOM 875 CB GLU B 42 11.406 9.146 21.144 1.00 17.61 C ANISOU 875 CB GLU B 42 2475 2064 2151 -88 368 -213 C ATOM 876 CG GLU B 42 12.221 9.305 19.859 1.00 21.69 C ANISOU 876 CG GLU B 42 2974 2882 2384 127 192 300 C ATOM 877 CD GLU B 42 13.480 8.411 19.789 1.00 27.25 C ANISOU 877 CD GLU B 42 3103 3773 3474 171 87 48 C ATOM 878 OE1 GLU B 42 13.383 7.330 20.338 1.00 29.36 O ANISOU 878 OE1 GLU B 42 3655 3442 4056 710 56 -149 O ATOM 879 OE2 GLU B 42 14.526 8.801 19.171 1.00 30.41 O ANISOU 879 OE2 GLU B 42 2951 4715 3886 443 61 -353 O ATOM 880 N GLU B 43 8.433 9.030 22.315 1.00 15.68 N ANISOU 880 N GLU B 43 2063 1981 1913 -86 -60 -205 N ATOM 881 CA AGLU B 43 7.614 8.565 23.424 0.50 16.18 C ANISOU 881 CA AGLU B 43 2069 1887 2191 -73 70 -193 C ATOM 882 CA BGLU B 43 7.595 8.492 23.391 0.50 16.93 C ANISOU 882 CA BGLU B 43 2202 1967 2261 -55 72 -194 C ATOM 883 C GLU B 43 8.477 7.915 24.492 1.00 16.05 C ANISOU 883 C GLU B 43 2247 1696 2154 -102 127 -219 C ATOM 884 O GLU B 43 9.403 7.113 24.209 1.00 17.12 O ANISOU 884 O GLU B 43 2465 1703 2335 0 195 -97 O ATOM 885 CB AGLU B 43 6.492 7.655 22.930 0.50 16.65 C ANISOU 885 CB AGLU B 43 2040 2016 2270 -110 112 -160 C ATOM 886 CB BGLU B 43 6.635 7.423 22.827 0.50 18.71 C ANISOU 886 CB BGLU B 43 2350 2357 2401 -164 41 -156 C ATOM 887 CG AGLU B 43 5.817 6.761 23.978 0.50 18.15 C ANISOU 887 CG AGLU B 43 2161 2294 2439 -107 18 63 C ATOM 888 CG BGLU B 43 5.252 7.341 23.477 0.50 22.45 C ANISOU 888 CG BGLU B 43 2763 2802 2965 6 172 -80 C ATOM 889 CD AGLU B 43 4.647 6.010 23.359 0.50 23.48 C ANISOU 889 CD AGLU B 43 2730 3213 2977 -182 -103 -209 C ATOM 890 CD BGLU B 43 4.180 6.696 22.564 0.50 25.01 C ANISOU 890 CD BGLU B 43 3107 3304 3092 -90 -40 -47 C ATOM 891 OE1AGLU B 43 4.783 5.532 22.199 0.50 24.18 O ANISOU 891 OE1AGLU B 43 2846 3489 2849 -187 -37 -19 O ATOM 892 OE1BGLU B 43 3.911 7.203 21.456 0.50 24.37 O ANISOU 892 OE1BGLU B 43 2744 3063 3453 -184 165 374 O ATOM 893 OE2AGLU B 43 3.591 5.930 24.030 0.50 28.89 O ANISOU 893 OE2AGLU B 43 3375 3967 3633 -460 260 -40 O ATOM 894 OE2BGLU B 43 3.582 5.665 22.961 0.50 30.99 O ANISOU 894 OE2BGLU B 43 4123 3935 3715 -237 139 64 O ATOM 895 N GLY B 44 8.199 8.292 25.736 1.00 16.39 N ANISOU 895 N GLY B 44 2315 1766 2147 -48 119 -121 N ATOM 896 CA GLY B 44 8.856 7.741 26.897 1.00 17.02 C ANISOU 896 CA GLY B 44 2270 2140 2056 69 179 42 C ATOM 897 C GLY B 44 10.142 8.450 27.292 1.00 15.99 C ANISOU 897 C GLY B 44 2249 1820 2005 50 -20 6 C ATOM 898 O GLY B 44 10.663 8.232 28.385 1.00 19.08 O ANISOU 898 O GLY B 44 2731 2375 2141 -44 -22 145 O ATOM 899 N GLN B 45 10.614 9.383 26.468 1.00 15.36 N ANISOU 899 N GLN B 45 2133 1865 1838 51 105 -169 N ATOM 900 CA GLN B 45 11.863 10.073 26.739 1.00 16.60 C ANISOU 900 CA GLN B 45 2377 1852 2075 250 11 -197 C ATOM 901 C GLN B 45 11.751 11.001 27.938 1.00 14.77 C ANISOU 901 C GLN B 45 2016 1688 1907 0 0 -174 C ATOM 902 O GLN B 45 10.816 11.793 28.025 1.00 14.58 O ANISOU 902 O GLN B 45 1800 1848 1892 218 -93 50 O ATOM 903 CB GLN B 45 12.233 10.862 25.468 1.00 18.98 C ANISOU 903 CB GLN B 45 2720 2415 2074 65 287 -247 C ATOM 904 CG GLN B 45 13.524 11.449 25.428 1.00 22.61 C ANISOU 904 CG GLN B 45 3265 2651 2673 9 52 49 C ATOM 905 CD GLN B 45 14.041 11.680 24.016 1.00 21.81 C ANISOU 905 CD GLN B 45 2857 2984 2444 -67 156 116 C ATOM 906 OE1 GLN B 45 13.253 11.906 23.052 1.00 17.11 O ANISOU 906 OE1 GLN B 45 1807 2675 2018 -290 -56 70 O ATOM 907 NE2 GLN B 45 15.390 11.676 23.888 1.00 22.88 N ANISOU 907 NE2 GLN B 45 2730 3069 2894 215 -319 0 N ATOM 908 N ALA B 46 12.722 10.953 28.845 1.00 14.80 N ANISOU 908 N ALA B 46 1988 1750 1883 252 -79 11 N ATOM 909 CA ALA B 46 12.774 11.907 29.953 1.00 13.85 C ANISOU 909 CA ALA B 46 1761 1601 1900 234 -60 21 C ATOM 910 C ALA B 46 13.199 13.304 29.457 1.00 14.00 C ANISOU 910 C ALA B 46 1714 1601 2003 70 65 -37 C ATOM 911 O ALA B 46 14.052 13.438 28.566 1.00 15.69 O ANISOU 911 O ALA B 46 1773 1873 2314 347 237 -44 O ATOM 912 CB ALA B 46 13.741 11.460 31.041 1.00 16.26 C ANISOU 912 CB ALA B 46 2241 1993 1942 403 -403 -92 C ATOM 913 N VAL B 47 12.528 14.334 29.993 1.00 12.32 N ANISOU 913 N VAL B 47 1526 1530 1622 113 51 -24 N ATOM 914 CA VAL B 47 12.784 15.733 29.629 1.00 12.98 C ANISOU 914 CA VAL B 47 1550 1716 1664 79 61 -40 C ATOM 915 C VAL B 47 12.777 16.606 30.875 1.00 13.02 C ANISOU 915 C VAL B 47 1583 1659 1705 127 -12 -5 C ATOM 916 O VAL B 47 12.116 16.282 31.882 1.00 14.11 O ANISOU 916 O VAL B 47 1804 1915 1641 21 124 59 O ATOM 917 CB VAL B 47 11.748 16.270 28.594 1.00 12.14 C ANISOU 917 CB VAL B 47 1537 1449 1626 93 -115 78 C ATOM 918 CG1 VAL B 47 11.943 15.618 27.234 1.00 14.30 C ANISOU 918 CG1 VAL B 47 1929 2051 1454 -82 168 -20 C ATOM 919 CG2 VAL B 47 10.303 16.122 29.110 1.00 15.14 C ANISOU 919 CG2 VAL B 47 1578 2248 1923 291 88 -136 C ATOM 920 N SER B 48 13.572 17.660 30.790 1.00 13.42 N ANISOU 920 N SER B 48 1534 1804 1759 155 148 -57 N ATOM 921 CA ASER B 48 13.593 18.772 31.713 0.33 13.26 C ANISOU 921 CA ASER B 48 1699 1674 1664 30 48 -75 C ATOM 922 CA BSER B 48 13.522 18.766 31.730 0.33 13.21 C ANISOU 922 CA BSER B 48 1662 1682 1674 11 58 -52 C ATOM 923 CA CSER B 48 13.490 18.762 31.729 0.33 13.57 C ANISOU 923 CA CSER B 48 1743 1693 1720 36 62 -47 C ATOM 924 C SER B 48 13.025 19.966 30.933 1.00 13.35 C ANISOU 924 C SER B 48 1744 1758 1569 153 70 -113 C ATOM 925 O SER B 48 13.373 20.134 29.753 1.00 15.34 O ANISOU 925 O SER B 48 2201 1891 1737 385 333 219 O ATOM 926 CB ASER B 48 15.053 19.044 32.101 0.33 15.15 C ANISOU 926 CB ASER B 48 1906 1990 1859 10 -12 -76 C ATOM 927 CB BSER B 48 14.900 19.053 32.333 0.33 15.48 C ANISOU 927 CB BSER B 48 1901 2024 1957 44 -21 -64 C ATOM 928 CB CSER B 48 14.829 19.026 32.409 0.33 15.96 C ANISOU 928 CB CSER B 48 1978 2055 2030 69 1 -72 C ATOM 929 OG ASER B 48 15.151 20.018 33.113 0.33 16.85 O ANISOU 929 OG ASER B 48 2087 2092 2220 42 -169 -440 O ATOM 930 OG BSER B 48 15.806 19.493 31.337 0.33 16.06 O ANISOU 930 OG BSER B 48 1513 2448 2140 -156 -150 -6 O ATOM 931 OG CSER B 48 15.213 17.896 33.162 0.33 18.74 O ANISOU 931 OG CSER B 48 2253 2475 2392 200 -163 121 O ATOM 932 N PHE B 49 12.175 20.786 31.542 1.00 11.85 N ANISOU 932 N PHE B 49 1680 1551 1268 17 -56 -51 N ATOM 933 CA PHE B 49 11.524 21.840 30.804 1.00 10.70 C ANISOU 933 CA PHE B 49 1310 1484 1269 -19 17 22 C ATOM 934 C PHE B 49 10.867 22.851 31.729 1.00 11.93 C ANISOU 934 C PHE B 49 1449 1590 1491 173 -75 -101 C ATOM 935 O PHE B 49 10.847 22.639 32.948 1.00 13.22 O ANISOU 935 O PHE B 49 1802 1805 1416 256 -143 -74 O ATOM 936 CB PHE B 49 10.442 21.258 29.856 1.00 12.65 C ANISOU 936 CB PHE B 49 1517 1845 1442 91 -78 -93 C ATOM 937 CG PHE B 49 9.280 20.651 30.574 1.00 12.49 C ANISOU 937 CG PHE B 49 1452 1651 1641 37 -37 -344 C ATOM 938 CD1 PHE B 49 9.375 19.452 31.272 1.00 13.95 C ANISOU 938 CD1 PHE B 49 1689 2004 1605 -378 -151 -94 C ATOM 939 CD2 PHE B 49 8.095 21.347 30.660 1.00 15.58 C ANISOU 939 CD2 PHE B 49 1842 1454 2622 152 -33 -139 C ATOM 940 CE1 PHE B 49 8.299 18.981 32.002 1.00 15.50 C ANISOU 940 CE1 PHE B 49 2006 1774 2107 -163 -187 84 C ATOM 941 CE2 PHE B 49 7.025 20.837 31.354 1.00 19.23 C ANISOU 941 CE2 PHE B 49 1893 2264 3147 198 311 -401 C ATOM 942 CZ PHE B 49 7.130 19.686 32.023 1.00 20.01 C ANISOU 942 CZ PHE B 49 2401 2466 2737 -365 66 -347 C ATOM 943 N GLU B 50 10.367 23.936 31.141 1.00 11.22 N ANISOU 943 N GLU B 50 1373 1638 1251 132 -120 -131 N ATOM 944 CA GLU B 50 9.564 24.927 31.838 1.00 11.66 C ANISOU 944 CA GLU B 50 1499 1552 1376 73 26 -194 C ATOM 945 C GLU B 50 8.204 25.017 31.186 1.00 12.00 C ANISOU 945 C GLU B 50 1493 1733 1333 175 -1 -42 C ATOM 946 O GLU B 50 8.046 24.612 30.013 1.00 11.73 O ANISOU 946 O GLU B 50 1375 1765 1314 8 81 -177 O ATOM 947 CB GLU B 50 10.237 26.298 31.769 1.00 13.83 C ANISOU 947 CB GLU B 50 1756 1666 1830 46 -115 -441 C ATOM 948 CG GLU B 50 11.499 26.400 32.574 1.00 17.15 C ANISOU 948 CG GLU B 50 2257 2334 1923 -122 -66 -277 C ATOM 949 CD GLU B 50 12.416 27.549 32.195 1.00 17.86 C ANISOU 949 CD GLU B 50 1979 2364 2442 23 -53 -89 C ATOM 950 OE1 GLU B 50 12.598 27.896 31.010 1.00 21.97 O ANISOU 950 OE1 GLU B 50 2485 3127 2733 -369 10 -249 O ATOM 951 OE2 GLU B 50 13.048 28.057 33.129 1.00 20.76 O ANISOU 951 OE2 GLU B 50 2831 2441 2615 -10 -314 -189 O ATOM 952 N ILE B 51 7.213 25.561 31.907 1.00 10.86 N ANISOU 952 N ILE B 51 1419 1488 1218 302 -207 -127 N ATOM 953 CA ILE B 51 5.886 25.819 31.334 1.00 10.92 C ANISOU 953 CA ILE B 51 1546 1413 1189 114 -75 -227 C ATOM 954 C ILE B 51 5.804 27.317 31.076 1.00 11.15 C ANISOU 954 C ILE B 51 1626 1356 1253 9 -129 -147 C ATOM 955 O ILE B 51 6.095 28.107 31.966 1.00 12.68 O ANISOU 955 O ILE B 51 1914 1414 1488 205 -324 -301 O ATOM 956 CB ILE B 51 4.743 25.345 32.239 1.00 12.06 C ANISOU 956 CB ILE B 51 1521 1789 1271 122 5 -225 C ATOM 957 CG1 ILE B 51 4.797 23.832 32.415 1.00 13.31 C ANISOU 957 CG1 ILE B 51 1701 1813 1540 146 74 135 C ATOM 958 CG2 ILE B 51 3.369 25.721 31.637 1.00 14.56 C ANISOU 958 CG2 ILE B 51 1395 2347 1788 251 -264 -149 C ATOM 959 CD1 ILE B 51 3.928 23.274 33.564 1.00 14.71 C ANISOU 959 CD1 ILE B 51 1729 2215 1644 -12 198 126 C ATOM 960 N VAL B 52 5.478 27.712 29.847 1.00 11.23 N ANISOU 960 N VAL B 52 1688 1303 1276 72 -95 -174 N ATOM 961 CA VAL B 52 5.272 29.108 29.489 1.00 12.12 C ANISOU 961 CA VAL B 52 1700 1490 1413 148 -228 -142 C ATOM 962 C VAL B 52 3.834 29.327 29.142 1.00 12.41 C ANISOU 962 C VAL B 52 1720 1568 1425 187 -273 -277 C ATOM 963 O VAL B 52 3.239 28.571 28.371 1.00 14.37 O ANISOU 963 O VAL B 52 1846 1679 1933 270 -557 -426 O ATOM 964 CB VAL B 52 6.187 29.526 28.294 1.00 12.82 C ANISOU 964 CB VAL B 52 1599 1694 1574 55 -269 -29 C ATOM 965 CG1 VAL B 52 5.978 28.642 27.059 1.00 18.16 C ANISOU 965 CG1 VAL B 52 2439 2517 1941 145 -63 -227 C ATOM 966 CG2 VAL B 52 5.951 31.023 27.975 1.00 15.46 C ANISOU 966 CG2 VAL B 52 2392 1786 1695 113 57 43 C ATOM 967 N GLU B 53 3.251 30.340 29.757 1.00 13.54 N ANISOU 967 N GLU B 53 1781 1659 1705 249 -315 -328 N ATOM 968 CA GLU B 53 1.869 30.720 29.530 1.00 13.94 C ANISOU 968 CA GLU B 53 1688 1812 1793 56 -439 -229 C ATOM 969 C GLU B 53 1.829 32.085 28.894 1.00 14.03 C ANISOU 969 C GLU B 53 1686 1892 1752 55 -253 -224 C ATOM 970 O GLU B 53 2.340 33.040 29.446 1.00 14.50 O ANISOU 970 O GLU B 53 1961 1546 2000 160 -441 -30 O ATOM 971 CB GLU B 53 1.086 30.733 30.820 1.00 15.89 C ANISOU 971 CB GLU B 53 1875 2104 2058 158 -377 63 C ATOM 972 CG GLU B 53 -0.369 31.033 30.612 1.00 19.17 C ANISOU 972 CG GLU B 53 2135 2671 2478 190 -116 172 C ATOM 973 CD GLU B 53 -1.119 31.422 31.865 0.50 16.31 C ANISOU 973 CD GLU B 53 1715 2424 2058 106 94 148 C ATOM 974 OE1 GLU B 53 -0.506 31.427 32.944 0.50 18.84 O ANISOU 974 OE1 GLU B 53 1945 3060 2153 -448 101 4 O ATOM 975 OE2 GLU B 53 -2.339 31.745 31.782 0.50 18.90 O ANISOU 975 OE2 GLU B 53 1860 2969 2352 94 -216 134 O ATOM 976 N GLY B 54 1.205 32.168 27.711 1.00 15.57 N ANISOU 976 N GLY B 54 1897 1929 2089 -188 -406 -106 N ATOM 977 CA GLY B 54 0.794 33.406 27.088 1.00 17.42 C ANISOU 977 CA GLY B 54 2142 2331 2145 -55 -286 3 C ATOM 978 C GLY B 54 -0.711 33.485 27.094 1.00 17.55 C ANISOU 978 C GLY B 54 2155 2320 2192 89 -169 281 C ATOM 979 O GLY B 54 -1.380 32.794 27.869 1.00 19.19 O ANISOU 979 O GLY B 54 2060 2555 2674 7 -187 444 O ATOM 980 N ASN B 55 -1.281 34.333 26.228 1.00 17.88 N ANISOU 980 N ASN B 55 2313 2250 2230 -45 -245 399 N ATOM 981 CA ASN B 55 -2.729 34.548 26.279 1.00 17.75 C ANISOU 981 CA ASN B 55 2235 2161 2347 81 -98 217 C ATOM 982 C ASN B 55 -3.559 33.402 25.699 1.00 16.28 C ANISOU 982 C ASN B 55 1741 2218 2226 103 -83 187 C ATOM 983 O ASN B 55 -4.777 33.454 25.811 1.00 20.31 O ANISOU 983 O ASN B 55 2149 2827 2738 3 -52 260 O ATOM 984 CB ASN B 55 -3.180 35.909 25.728 1.00 19.62 C ANISOU 984 CB ASN B 55 2123 2438 2892 -38 -73 35 C ATOM 985 CG ASN B 55 -3.015 36.026 24.260 1.00 18.66 C ANISOU 985 CG ASN B 55 2146 2119 2822 -259 -490 404 C ATOM 986 OD1 ASN B 55 -2.387 35.163 23.621 1.00 20.14 O ANISOU 986 OD1 ASN B 55 2493 2858 2301 -367 -437 481 O ATOM 987 ND2 ASN B 55 -3.628 37.121 23.671 1.00 22.86 N ANISOU 987 ND2 ASN B 55 2406 2622 3655 -101 -1021 647 N ATOM 988 N ARG B 56 -2.935 32.357 25.154 1.00 16.04 N ANISOU 988 N ARG B 56 1786 1967 2340 -44 -275 234 N ATOM 989 CA ARG B 56 -3.692 31.195 24.765 1.00 17.52 C ANISOU 989 CA ARG B 56 1980 2031 2645 2 -291 203 C ATOM 990 C ARG B 56 -3.536 29.982 25.656 1.00 16.80 C ANISOU 990 C ARG B 56 1881 1992 2510 -45 -285 252 C ATOM 991 O ARG B 56 -4.245 28.971 25.484 1.00 19.50 O ANISOU 991 O ARG B 56 2228 2230 2951 -274 -451 397 O ATOM 992 CB ARG B 56 -3.474 30.761 23.354 1.00 18.48 C ANISOU 992 CB ARG B 56 2271 2165 2585 -80 -349 246 C ATOM 993 CG ARG B 56 -4.664 29.889 22.940 1.00 20.40 C ANISOU 993 CG ARG B 56 2582 2327 2842 -29 -112 145 C ATOM 994 CD ARG B 56 -4.921 29.851 21.480 1.00 20.16 C ANISOU 994 CD ARG B 56 2318 2706 2635 227 -178 83 C ATOM 995 NE ARG B 56 -6.142 29.114 21.278 1.00 18.72 N ANISOU 995 NE ARG B 56 2162 2480 2468 377 23 23 N ATOM 996 CZ ARG B 56 -6.564 28.593 20.140 1.00 18.64 C ANISOU 996 CZ ARG B 56 2133 2520 2430 464 -156 103 C ATOM 997 NH1 ARG B 56 -5.894 28.744 19.012 1.00 18.60 N ANISOU 997 NH1 ARG B 56 2146 2476 2443 217 34 148 N ATOM 998 NH2 ARG B 56 -7.698 27.924 20.141 1.00 18.21 N ANISOU 998 NH2 ARG B 56 2260 2654 2006 399 -83 84 N ATOM 999 N GLY B 57 -2.667 30.077 26.637 1.00 16.15 N ANISOU 999 N GLY B 57 1830 2098 2207 -107 -365 222 N ATOM 1000 CA GLY B 57 -2.527 28.992 27.583 1.00 15.56 C ANISOU 1000 CA GLY B 57 1861 1936 2113 41 -316 129 C ATOM 1001 C GLY B 57 -1.110 28.506 27.721 1.00 13.32 C ANISOU 1001 C GLY B 57 1560 1775 1723 79 24 150 C ATOM 1002 O GLY B 57 -0.198 29.114 27.178 1.00 15.00 O ANISOU 1002 O GLY B 57 1583 2080 2035 50 -372 349 O ATOM 1003 N PRO B 58 -0.946 27.425 28.473 1.00 12.47 N ANISOU 1003 N PRO B 58 1409 1680 1648 223 -23 56 N ATOM 1004 CA PRO B 58 0.361 26.876 28.794 1.00 12.10 C ANISOU 1004 CA PRO B 58 1285 1639 1673 174 39 8 C ATOM 1005 C PRO B 58 0.911 25.908 27.732 1.00 11.67 C ANISOU 1005 C PRO B 58 1485 1480 1467 21 67 43 C ATOM 1006 O PRO B 58 0.165 25.139 27.146 1.00 13.36 O ANISOU 1006 O PRO B 58 1555 1609 1911 2 -109 -48 O ATOM 1007 CB PRO B 58 0.110 26.121 30.086 1.00 13.03 C ANISOU 1007 CB PRO B 58 1484 1713 1754 260 -64 -38 C ATOM 1008 CG PRO B 58 -1.334 25.652 29.930 1.00 14.47 C ANISOU 1008 CG PRO B 58 1682 1855 1960 143 195 278 C ATOM 1009 CD PRO B 58 -2.037 26.686 29.125 1.00 13.56 C ANISOU 1009 CD PRO B 58 1569 1761 1822 145 31 168 C ATOM 1010 N GLN B 59 2.212 25.947 27.503 1.00 11.55 N ANISOU 1010 N GLN B 59 1457 1475 1456 56 11 -168 N ATOM 1011 CA GLN B 59 2.891 24.964 26.681 1.00 11.63 C ANISOU 1011 CA GLN B 59 1544 1387 1486 147 -18 -193 C ATOM 1012 C GLN B 59 4.317 24.845 27.215 1.00 10.96 C ANISOU 1012 C GLN B 59 1415 1527 1220 54 -105 -179 C ATOM 1013 O GLN B 59 4.784 25.624 28.053 1.00 11.38 O ANISOU 1013 O GLN B 59 1547 1337 1440 76 -250 -350 O ATOM 1014 CB GLN B 59 2.903 25.333 25.205 1.00 13.02 C ANISOU 1014 CB GLN B 59 1758 1614 1574 298 -200 -294 C ATOM 1015 CG GLN B 59 3.648 26.563 24.895 1.00 15.26 C ANISOU 1015 CG GLN B 59 2178 1890 1729 319 10 -29 C ATOM 1016 CD GLN B 59 3.562 26.938 23.442 1.00 18.88 C ANISOU 1016 CD GLN B 59 2988 2147 2036 254 299 77 C ATOM 1017 OE1 GLN B 59 3.837 26.123 22.555 1.00 19.55 O ANISOU 1017 OE1 GLN B 59 3074 2200 2153 532 23 104 O ATOM 1018 NE2 GLN B 59 3.137 28.165 23.197 1.00 22.49 N ANISOU 1018 NE2 GLN B 59 3266 2974 2304 702 0 313 N ATOM 1019 N ALA B 60 5.016 23.861 26.709 1.00 10.59 N ANISOU 1019 N ALA B 60 1432 1350 1239 -30 90 -143 N ATOM 1020 CA ALA B 60 6.409 23.621 27.109 1.00 10.37 C ANISOU 1020 CA ALA B 60 1259 1475 1205 -17 8 -16 C ATOM 1021 C ALA B 60 7.366 24.640 26.491 1.00 11.28 C ANISOU 1021 C ALA B 60 1436 1453 1393 -220 22 -70 C ATOM 1022 O ALA B 60 7.156 25.133 25.373 1.00 12.46 O ANISOU 1022 O ALA B 60 1614 1623 1494 -153 38 68 O ATOM 1023 CB ALA B 60 6.827 22.202 26.738 1.00 11.97 C ANISOU 1023 CB ALA B 60 1300 1558 1689 160 96 -2 C ATOM 1024 N ALA B 61 8.409 24.948 27.236 1.00 10.68 N ANISOU 1024 N ALA B 61 1249 1434 1375 -147 -25 -75 N ATOM 1025 CA ALA B 61 9.522 25.806 26.800 1.00 11.09 C ANISOU 1025 CA ALA B 61 1420 1329 1464 -155 149 -41 C ATOM 1026 C ALA B 61 10.817 25.156 27.280 1.00 12.04 C ANISOU 1026 C ALA B 61 1549 1528 1497 -181 53 -40 C ATOM 1027 O ALA B 61 10.841 24.466 28.297 1.00 11.71 O ANISOU 1027 O ALA B 61 1465 1561 1422 -162 90 -189 O ATOM 1028 CB ALA B 61 9.425 27.207 27.373 1.00 13.58 C ANISOU 1028 CB ALA B 61 1546 1480 2133 213 -25 -202 C ATOM 1029 N ASN B 62 11.899 25.417 26.569 1.00 11.86 N ANISOU 1029 N ASN B 62 1633 1510 1363 -14 201 -45 N ATOM 1030 CA ASN B 62 13.220 25.077 27.064 1.00 12.82 C ANISOU 1030 CA ASN B 62 1493 1780 1596 -37 176 -45 C ATOM 1031 C ASN B 62 13.323 23.589 27.407 1.00 13.01 C ANISOU 1031 C ASN B 62 1563 1772 1608 -95 96 -122 C ATOM 1032 O ASN B 62 13.748 23.197 28.481 1.00 13.46 O ANISOU 1032 O ASN B 62 1595 1838 1679 -143 -74 -63 O ATOM 1033 CB ASN B 62 13.532 26.005 28.271 1.00 13.42 C ANISOU 1033 CB ASN B 62 1545 1812 1739 -130 -19 -148 C ATOM 1034 CG ASN B 62 14.988 26.080 28.629 1.00 20.06 C ANISOU 1034 CG ASN B 62 2202 2832 2585 -306 88 -498 C ATOM 1035 OD1 ASN B 62 15.841 25.727 27.841 1.00 21.39 O ANISOU 1035 OD1 ASN B 62 2038 3115 2971 -176 -63 -629 O ATOM 1036 ND2 ASN B 62 15.279 26.571 29.836 1.00 23.86 N ANISOU 1036 ND2 ASN B 62 2769 3435 2862 -20 -34 -565 N ATOM 1037 N VAL B 63 12.919 22.737 26.461 1.00 13.01 N ANISOU 1037 N VAL B 63 1669 1654 1618 -66 39 -99 N ATOM 1038 CA VAL B 63 12.839 21.332 26.676 1.00 11.96 C ANISOU 1038 CA VAL B 63 1481 1566 1497 -46 -49 -22 C ATOM 1039 C VAL B 63 14.166 20.699 26.324 1.00 12.22 C ANISOU 1039 C VAL B 63 1633 1493 1517 -101 -117 -49 C ATOM 1040 O VAL B 63 14.600 20.765 25.157 1.00 13.42 O ANISOU 1040 O VAL B 63 1625 1966 1508 -96 78 -206 O ATOM 1041 CB VAL B 63 11.735 20.711 25.798 1.00 11.84 C ANISOU 1041 CB VAL B 63 1348 1637 1511 55 -31 -50 C ATOM 1042 CG1 VAL B 63 11.717 19.159 25.917 1.00 13.43 C ANISOU 1042 CG1 VAL B 63 2009 1310 1783 75 63 -208 C ATOM 1043 CG2 VAL B 63 10.340 21.337 26.111 1.00 12.17 C ANISOU 1043 CG2 VAL B 63 1230 1635 1757 203 -13 -61 C ATOM 1044 N THR B 64 14.825 20.086 27.303 1.00 12.85 N ANISOU 1044 N THR B 64 1513 1794 1574 151 -61 18 N ATOM 1045 CA THR B 64 16.059 19.322 27.077 1.00 14.63 C ANISOU 1045 CA THR B 64 1842 1979 1737 136 116 -85 C ATOM 1046 C THR B 64 15.793 17.844 27.328 1.00 14.08 C ANISOU 1046 C THR B 64 1896 1878 1573 156 72 87 C ATOM 1047 O THR B 64 15.326 17.439 28.387 1.00 14.93 O ANISOU 1047 O THR B 64 1915 1820 1936 176 248 -99 O ATOM 1048 CB THR B 64 17.170 19.801 28.046 1.00 17.37 C ANISOU 1048 CB THR B 64 1937 2360 2301 -3 -163 -128 C ATOM 1049 OG1 THR B 64 17.443 21.173 27.811 1.00 21.81 O ANISOU 1049 OG1 THR B 64 2710 2828 2746 -223 -218 3 O ATOM 1050 CG2 THR B 64 18.451 18.978 27.860 1.00 20.45 C ANISOU 1050 CG2 THR B 64 2067 2814 2886 187 -105 182 C ATOM 1051 N LYS B 65 16.147 17.017 26.366 1.00 14.43 N ANISOU 1051 N LYS B 65 1764 1849 1868 117 437 48 N ATOM 1052 CA LYS B 65 15.865 15.599 26.419 1.00 17.89 C ANISOU 1052 CA LYS B 65 2357 2033 2405 230 203 -164 C ATOM 1053 C LYS B 65 17.067 14.837 26.910 1.00 20.84 C ANISOU 1053 C LYS B 65 2267 2572 3080 82 263 53 C ATOM 1054 O LYS B 65 18.219 15.268 26.787 1.00 22.87 O ANISOU 1054 O LYS B 65 2033 2685 3970 321 184 344 O ATOM 1055 CB LYS B 65 15.332 15.081 24.998 1.00 19.87 C ANISOU 1055 CB LYS B 65 2708 2363 2478 99 215 -253 C ATOM 1056 CG LYS B 65 16.294 15.176 23.811 1.00 20.35 C ANISOU 1056 CG LYS B 65 2306 2619 2807 -250 -12 -12 C ATOM 1057 CD LYS B 65 15.591 14.948 22.439 1.00 17.94 C ANISOU 1057 CD LYS B 65 1969 2526 2319 312 194 -688 C ATOM 1058 CE LYS B 65 16.578 14.497 21.425 1.00 19.97 C ANISOU 1058 CE LYS B 65 2432 2659 2496 -196 304 -335 C ATOM 1059 NZ LYS B 65 15.938 14.462 20.199 1.00 18.43 N ANISOU 1059 NZ LYS B 65 2103 2934 1965 280 274 66 N ATOM 1060 N GLU B 66 16.756 13.648 27.429 1.00 22.42 N ANISOU 1060 N GLU B 66 2621 2572 3323 281 100 92 N ATOM 1061 CA GLU B 66 17.746 12.660 27.885 1.00 25.57 C ANISOU 1061 CA GLU B 66 2958 3209 3546 306 -53 -55 C ATOM 1062 C GLU B 66 17.757 11.518 26.856 1.00 28.68 C ANISOU 1062 C GLU B 66 3476 3412 4008 0 -172 -208 C ATOM 1063 O GLU B 66 16.684 10.917 26.569 1.00 30.78 O ANISOU 1063 O GLU B 66 3490 3869 4335 29 -407 -257 O ATOM 1064 CB GLU B 66 17.296 12.150 29.251 1.00 27.48 C ANISOU 1064 CB GLU B 66 3293 3455 3692 267 79 52 C ATOM 1065 CG GLU B 66 18.361 11.747 30.229 1.00 32.84 C ANISOU 1065 CG GLU B 66 3998 4317 4163 204 -6 83 C ATOM 1066 CD GLU B 66 17.807 11.731 31.675 1.00 32.69 C ANISOU 1066 CD GLU B 66 4093 4378 3947 162 -127 40 C ATOM 1067 OE1 GLU B 66 17.155 10.729 32.072 1.00 33.38 O ANISOU 1067 OE1 GLU B 66 4002 4249 4429 360 -424 119 O ATOM 1068 OE2 GLU B 66 17.987 12.741 32.395 1.00 37.75 O ANISOU 1068 OE2 GLU B 66 4828 4776 4736 149 -359 -72 O TER 1069 GLU B 66 ATOM 1070 O5'A U R 1 -2.567 26.122 14.895 0.50 63.02 O ANISOU 1070 O5'A U R 1 8004 8004 7935 15 -8 5 O ATOM 1071 C5'A U R 1 -1.882 25.800 16.098 0.50 62.35 C ANISOU 1071 C5'A U R 1 7872 7897 7918 22 1 0 C ATOM 1072 C4'A U R 1 -0.594 25.055 15.804 0.50 61.23 C ANISOU 1072 C4'A U R 1 7776 7761 7728 -16 -8 35 C ATOM 1073 O4'A U R 1 0.533 25.951 15.948 0.50 60.92 O ANISOU 1073 O4'A U R 1 7718 7732 7694 37 12 20 O ATOM 1074 C3'A U R 1 -0.278 23.910 16.758 0.50 59.80 C ANISOU 1074 C3'A U R 1 7550 7551 7618 -44 -14 -14 C ATOM 1075 O3'A U R 1 -0.955 22.718 16.336 0.50 57.44 O ANISOU 1075 O3'A U R 1 7210 7349 7264 25 5 0 O ATOM 1076 C2'A U R 1 1.249 23.819 16.730 0.50 59.28 C ANISOU 1076 C2'A U R 1 7516 7525 7482 13 4 -4 C ATOM 1077 O2'A U R 1 1.697 22.704 15.984 0.50 58.12 O ANISOU 1077 O2'A U R 1 7335 7414 7330 5 -11 38 O ATOM 1078 C1'A U R 1 1.694 25.160 16.118 0.50 59.65 C ANISOU 1078 C1'A U R 1 7557 7562 7543 -1 -21 -3 C ATOM 1079 N1 A U R 1 2.663 25.935 16.959 0.50 58.62 N ANISOU 1079 N1 A U R 1 7388 7417 7465 26 14 22 N ATOM 1080 C2 A U R 1 2.489 25.977 18.327 0.50 57.98 C ANISOU 1080 C2 A U R 1 7322 7278 7429 34 0 -5 C ATOM 1081 O2 A U R 1 1.573 25.415 18.902 0.50 57.95 O ANISOU 1081 O2 A U R 1 7460 7203 7353 33 -3 48 O ATOM 1082 N3 A U R 1 3.433 26.705 19.008 0.50 57.23 N ANISOU 1082 N3 A U R 1 7249 7133 7363 79 36 -19 N ATOM 1083 C4 A U R 1 4.505 27.385 18.463 0.50 57.02 C ANISOU 1083 C4 A U R 1 7208 7115 7339 70 1 -48 C ATOM 1084 O4 A U R 1 5.266 27.993 19.204 0.50 56.78 O ANISOU 1084 O4 A U R 1 7107 7122 7343 116 -46 -43 O ATOM 1085 C5 A U R 1 4.622 27.304 17.029 0.50 57.27 C ANISOU 1085 C5 A U R 1 7249 7175 7334 79 5 2 C ATOM 1086 C6 A U R 1 3.714 26.595 16.348 0.50 57.85 C ANISOU 1086 C6 A U R 1 7313 7292 7374 47 -15 -9 C ATOM 1087 P A C R 2 -2.541 22.706 16.581 0.50 54.96 P ANISOU 1087 P A C R 2 7020 6783 7077 -8 6 -63 P ATOM 1088 OP1A C R 2 -3.172 23.445 15.469 0.50 54.44 O ANISOU 1088 OP1A C R 2 6942 6917 6823 -1 19 -35 O ATOM 1089 OP2A C R 2 -2.737 23.178 17.972 0.50 56.65 O ANISOU 1089 OP2A C R 2 7148 7228 7149 25 45 0 O ATOM 1090 O5'A C R 2 -2.995 21.172 16.526 0.50 49.56 O ANISOU 1090 O5'A C R 2 6225 6439 6166 104 -16 102 O ATOM 1091 O5'B C R 2 -3.405 19.319 17.880 0.50 45.12 O ANISOU 1091 O5'B C R 2 5538 5809 5796 128 -42 -17 O ATOM 1092 C5'A C R 2 -2.409 20.230 17.413 0.50 44.10 C ANISOU 1092 C5'A C R 2 5495 5682 5579 -32 116 -30 C ATOM 1093 C5'B C R 2 -2.931 20.112 18.982 0.50 46.53 C ANISOU 1093 C5'B C R 2 5836 5915 5928 52 19 -31 C ATOM 1094 C4'A C R 2 -3.414 19.592 18.367 0.50 38.68 C ANISOU 1094 C4'A C R 2 4810 4964 4922 161 -101 -110 C ATOM 1095 C4'B C R 2 -3.477 19.607 20.311 0.50 45.68 C ANISOU 1095 C4'B C R 2 5736 5774 5846 18 -32 -21 C ATOM 1096 O4'A C R 2 -3.079 19.897 19.760 0.50 33.80 O ANISOU 1096 O4'A C R 2 4006 4213 4622 196 57 -176 O ATOM 1097 O4'B C R 2 -2.790 20.202 21.437 0.50 45.54 O ANISOU 1097 O4'B C R 2 5875 5709 5717 97 17 9 O ATOM 1098 C3'A C R 2 -4.851 20.075 18.233 0.50 36.18 C ANISOU 1098 C3'A C R 2 4593 4512 4638 67 -29 -141 C ATOM 1099 C3'B C R 2 -4.926 19.950 20.586 0.50 44.45 C ANISOU 1099 C3'B C R 2 5663 5580 5645 -16 20 3 C ATOM 1100 O3'A C R 2 -5.748 19.128 18.761 0.50 34.70 O ANISOU 1100 O3'A C R 2 4517 4160 4506 138 -77 -204 O ATOM 1101 O3'B C R 2 -5.412 19.016 21.479 0.50 41.66 O ANISOU 1101 O3'B C R 2 5125 5166 5536 -2 23 -102 O ATOM 1102 C2'A C R 2 -4.848 21.310 19.122 0.50 33.03 C ANISOU 1102 C2'A C R 2 4046 4221 4282 40 -59 -55 C ATOM 1103 C2'B C R 2 -4.880 21.288 21.298 0.50 43.78 C ANISOU 1103 C2'B C R 2 5542 5537 5554 12 -37 -54 C ATOM 1104 O2'A C R 2 -6.140 21.683 19.539 0.50 30.98 O ANISOU 1104 O2'A C R 2 3968 3738 4063 79 -60 -250 O ATOM 1105 O2'B C R 2 -6.005 21.404 22.132 0.50 44.07 O ANISOU 1105 O2'B C R 2 5571 5473 5698 -8 -11 -65 O ATOM 1106 C1'A C R 2 -4.071 20.777 20.306 0.50 29.59 C ANISOU 1106 C1'A C R 2 3547 3704 3989 3 71 -130 C ATOM 1107 C1'B C R 2 -3.613 21.131 22.133 0.50 43.71 C ANISOU 1107 C1'B C R 2 5517 5473 5616 -23 -9 9 C ATOM 1108 N1 A C R 2 -3.363 21.787 21.113 0.50 21.43 N ANISOU 1108 N1 A C R 2 2018 2904 3218 625 155 79 N ATOM 1109 N1 B C R 2 -2.787 22.373 22.365 0.50 40.61 N ANISOU 1109 N1 B C R 2 5080 5155 5193 65 42 -46 N ATOM 1110 C2 A C R 2 -3.421 21.687 22.525 0.50 19.14 C ANISOU 1110 C2 A C R 2 1503 2627 3143 350 -86 -175 C ATOM 1111 C2 B C R 2 -2.503 22.831 23.671 0.50 38.61 C ANISOU 1111 C2 B C R 2 4724 4816 5128 81 64 96 C ATOM 1112 O2 A C R 2 -4.072 20.781 23.085 0.50 24.97 O ANISOU 1112 O2 A C R 2 2864 2971 3653 438 98 138 O ATOM 1113 O2 B C R 2 -2.963 22.209 24.642 0.50 38.36 O ANISOU 1113 O2 B C R 2 4607 4835 5131 258 114 182 O ATOM 1114 N3 A C R 2 -2.733 22.606 23.243 0.50 16.17 N ANISOU 1114 N3 A C R 2 1492 1935 2717 789 79 -420 N ATOM 1115 N3 B C R 2 -1.734 23.951 23.834 0.50 36.18 N ANISOU 1115 N3 B C R 2 4315 4507 4922 232 83 -41 N ATOM 1116 C4 A C R 2 -2.032 23.567 22.609 0.50 14.82 C ANISOU 1116 C4 A C R 2 1323 1523 2784 918 -81 -119 C ATOM 1117 C4 B C R 2 -1.272 24.573 22.726 0.50 36.47 C ANISOU 1117 C4 B C R 2 4530 4537 4790 159 24 -43 C ATOM 1118 N4 A C R 2 -1.342 24.430 23.378 0.50 18.12 N ANISOU 1118 N4 A C R 2 1742 1526 3617 827 -225 -544 N ATOM 1119 N4 B C R 2 -0.525 25.665 22.846 0.50 36.31 N ANISOU 1119 N4 B C R 2 4423 4748 4623 7 111 -19 N ATOM 1120 C5 A C R 2 -1.968 23.668 21.187 0.50 17.40 C ANISOU 1120 C5 A C R 2 1635 1973 3003 880 -82 -247 C ATOM 1121 C5 B C R 2 -1.553 24.118 21.404 0.50 37.27 C ANISOU 1121 C5 B C R 2 4563 4760 4837 166 -9 -42 C ATOM 1122 C6 A C R 2 -2.649 22.756 20.483 0.50 17.58 C ANISOU 1122 C6 A C R 2 1330 2135 3214 840 -148 -157 C ATOM 1123 C6 B C R 2 -2.304 23.023 21.273 0.50 38.72 C ANISOU 1123 C6 B C R 2 4826 4812 5073 77 -50 -28 C ATOM 1124 P A U R 3 -5.943 17.710 18.062 0.50 33.99 P ANISOU 1124 P A U R 3 4373 4132 4407 50 -413 -275 P ATOM 1125 P B U R 3 -6.586 18.036 21.043 0.50 38.17 P ANISOU 1125 P B U R 3 4513 5005 4985 244 -313 -77 P ATOM 1126 OP1A U R 3 -5.655 17.888 16.623 0.50 35.43 O ANISOU 1126 OP1A U R 3 4501 4384 4577 -11 -32 -23 O ATOM 1127 OP1B U R 3 -6.899 18.302 19.617 0.50 39.48 O ANISOU 1127 OP1B U R 3 4950 5160 4888 -4 3 -13 O ATOM 1128 OP2A U R 3 -7.219 17.207 18.584 0.50 33.80 O ANISOU 1128 OP2A U R 3 4298 3991 4553 256 14 -122 O ATOM 1129 OP2B U R 3 -7.570 18.045 22.154 0.50 35.89 O ANISOU 1129 OP2B U R 3 4319 4450 4868 0 -80 -116 O ATOM 1130 O5'A U R 3 -4.800 16.754 18.713 0.50 32.45 O ANISOU 1130 O5'A U R 3 4234 3931 4165 114 34 -1 O ATOM 1131 O5'B U R 3 -5.900 16.623 21.094 0.50 35.40 O ANISOU 1131 O5'B U R 3 4408 4547 4492 -39 8 -120 O ATOM 1132 C5'A U R 3 -4.859 16.414 20.130 0.50 31.04 C ANISOU 1132 C5'A U R 3 3909 3948 3936 -41 -84 -70 C ATOM 1133 C5'B U R 3 -4.896 16.361 20.153 0.50 32.28 C ANISOU 1133 C5'B U R 3 4099 4100 4066 -27 -112 -18 C ATOM 1134 C4' U R 3 -4.362 15.017 20.534 1.00 27.30 C ANISOU 1134 C4' U R 3 3218 3855 3301 -97 -28 -198 C ATOM 1135 O4' U R 3 -3.736 15.198 21.829 1.00 22.27 O ANISOU 1135 O4' U R 3 2513 3227 2722 35 52 -206 O ATOM 1136 C3' U R 3 -5.411 13.922 20.782 1.00 28.54 C ANISOU 1136 C3' U R 3 3500 3741 3601 -148 60 -270 C ATOM 1137 O3' U R 3 -4.965 12.614 20.368 1.00 27.38 O ANISOU 1137 O3' U R 3 2806 3558 4037 -801 365 -481 O ATOM 1138 C2' U R 3 -5.618 13.910 22.285 1.00 26.09 C ANISOU 1138 C2' U R 3 3073 3391 3449 -221 165 -77 C ATOM 1139 O2' U R 3 -6.040 12.670 22.846 1.00 29.98 O ANISOU 1139 O2' U R 3 3955 3636 3798 -344 141 -370 O ATOM 1140 C1' U R 3 -4.201 14.215 22.727 1.00 23.89 C ANISOU 1140 C1' U R 3 2727 3218 3132 87 192 -141 C ATOM 1141 N1 U R 3 -4.076 14.747 24.100 1.00 21.21 N ANISOU 1141 N1 U R 3 2190 2998 2870 -148 321 73 N ATOM 1142 C2 U R 3 -3.242 14.158 25.041 1.00 21.93 C ANISOU 1142 C2 U R 3 2740 2627 2964 -84 77 -170 C ATOM 1143 O2 U R 3 -2.569 13.139 24.818 1.00 29.49 O ANISOU 1143 O2 U R 3 4155 3482 3564 565 958 290 O ATOM 1144 N3 U R 3 -3.201 14.765 26.257 1.00 23.33 N ANISOU 1144 N3 U R 3 2651 3481 2731 77 340 161 N ATOM 1145 C4 U R 3 -3.874 15.879 26.640 1.00 22.23 C ANISOU 1145 C4 U R 3 2430 2946 3068 -304 47 200 C ATOM 1146 O4 U R 3 -3.761 16.344 27.790 1.00 26.90 O ANISOU 1146 O4 U R 3 2804 4351 3063 -129 107 -109 O ATOM 1147 C5 U R 3 -4.678 16.453 25.597 1.00 20.34 C ANISOU 1147 C5 U R 3 1793 3092 2841 140 178 21 C ATOM 1148 C6 U R 3 -4.772 15.890 24.405 1.00 21.39 C ANISOU 1148 C6 U R 3 2107 3035 2984 -85 27 -47 C ATOM 1149 P U R 4 -5.750 11.815 19.185 1.00 33.26 P ANISOU 1149 P U R 4 3429 4912 4295 -593 -90 -779 P ATOM 1150 OP1 U R 4 -7.102 12.376 19.024 1.00 38.22 O ANISOU 1150 OP1 U R 4 4369 5069 5083 128 -88 -196 O ATOM 1151 OP2 U R 4 -5.570 10.432 19.611 1.00 37.93 O ANISOU 1151 OP2 U R 4 4521 4818 5071 -342 -39 -228 O ATOM 1152 O5' U R 4 -4.891 12.075 17.836 1.00 33.45 O ANISOU 1152 O5' U R 4 4061 4524 4121 -355 -28 -428 O ATOM 1153 C5' U R 4 -4.969 13.322 17.136 1.00 34.55 C ANISOU 1153 C5' U R 4 4297 4811 4018 -70 -152 -292 C ATOM 1154 C4' U R 4 -3.676 13.611 16.399 1.00 35.44 C ANISOU 1154 C4' U R 4 4280 4882 4302 -233 -321 -108 C ATOM 1155 O4' U R 4 -2.582 13.752 17.335 1.00 30.52 O ANISOU 1155 O4' U R 4 3661 4335 3598 -499 -380 -395 O ATOM 1156 C3' U R 4 -3.223 12.473 15.493 1.00 39.80 C ANISOU 1156 C3' U R 4 4805 5226 5091 -11 13 -188 C ATOM 1157 O3' U R 4 -3.868 12.580 14.229 1.00 45.78 O ANISOU 1157 O3' U R 4 5890 5929 5574 13 -251 35 O ATOM 1158 C2' U R 4 -1.708 12.652 15.410 1.00 34.98 C ANISOU 1158 C2' U R 4 4589 4589 4113 -233 -75 -146 C ATOM 1159 O2' U R 4 -1.263 13.689 14.548 1.00 34.42 O ANISOU 1159 O2' U R 4 4262 4321 4494 138 164 175 O ATOM 1160 C1' U R 4 -1.448 13.006 16.871 1.00 31.27 C ANISOU 1160 C1' U R 4 4089 3975 3817 -221 -263 -187 C ATOM 1161 N1 U R 4 -1.116 11.857 17.799 1.00 26.10 N ANISOU 1161 N1 U R 4 3357 3293 3265 -484 -215 -550 N ATOM 1162 C2 U R 4 0.080 11.181 17.557 1.00 26.65 C ANISOU 1162 C2 U R 4 3583 3124 3418 -147 44 -110 C ATOM 1163 O2 U R 4 0.795 11.483 16.599 1.00 28.60 O ANISOU 1163 O2 U R 4 3950 3476 3440 -423 137 -67 O ATOM 1164 N3 U R 4 0.389 10.135 18.426 1.00 23.54 N ANISOU 1164 N3 U R 4 2999 2739 3205 -540 -438 -335 N ATOM 1165 C4 U R 4 -0.367 9.791 19.538 1.00 22.44 C ANISOU 1165 C4 U R 4 3277 1957 3290 -614 -335 -355 C ATOM 1166 O4 U R 4 0.005 8.888 20.273 1.00 25.88 O ANISOU 1166 O4 U R 4 3363 2846 3623 -771 -905 -51 O ATOM 1167 C5 U R 4 -1.581 10.543 19.762 1.00 23.32 C ANISOU 1167 C5 U R 4 2905 2521 3433 -656 -397 -561 C ATOM 1168 C6 U R 4 -1.920 11.523 18.897 1.00 23.97 C ANISOU 1168 C6 U R 4 3039 2839 3229 -591 -253 -628 C ATOM 1169 P U R 5 -4.305 11.238 13.460 1.00 53.08 P ANISOU 1169 P U R 5 6906 6722 6537 -342 -374 -368 P ATOM 1170 OP1 U R 5 -5.112 11.685 12.287 1.00 54.96 O ANISOU 1170 OP1 U R 5 6880 7058 6941 9 -126 -51 O ATOM 1171 OP2 U R 5 -4.830 10.240 14.448 1.00 53.60 O ANISOU 1171 OP2 U R 5 6712 7068 6584 -242 -88 -207 O ATOM 1172 O5' U R 5 -2.864 10.724 12.932 1.00 61.59 O ANISOU 1172 O5' U R 5 7597 8071 7730 17 -8 -131 O ATOM 1173 C5' U R 5 -2.469 9.352 12.925 1.00 69.19 C ANISOU 1173 C5' U R 5 8874 8516 8898 56 17 -47 C ATOM 1174 C4' U R 5 -1.285 9.083 13.841 1.00 73.29 C ANISOU 1174 C4' U R 5 9233 9301 9310 19 -97 19 C ATOM 1175 O4' U R 5 -1.717 9.137 15.221 1.00 75.06 O ANISOU 1175 O4' U R 5 9637 9453 9429 -27 -45 -45 O ATOM 1176 C3' U R 5 -0.692 7.689 13.660 1.00 75.21 C ANISOU 1176 C3' U R 5 9508 9486 9580 40 3 -3 C ATOM 1177 O3' U R 5 0.360 7.700 12.697 1.00 75.33 O ANISOU 1177 O3' U R 5 9479 9591 9552 -21 -13 29 O ATOM 1178 C2' U R 5 -0.236 7.274 15.066 1.00 76.33 C ANISOU 1178 C2' U R 5 9644 9702 9655 -13 -19 5 C ATOM 1179 O2' U R 5 1.173 7.227 15.242 1.00 75.15 O ANISOU 1179 O2' U R 5 9562 9475 9516 -11 -3 -42 O ATOM 1180 C1' U R 5 -0.855 8.323 15.997 1.00 77.05 C ANISOU 1180 C1' U R 5 9795 9732 9747 15 -78 -42 C ATOM 1181 N1 U R 5 -1.604 7.778 17.204 1.00 78.92 N ANISOU 1181 N1 U R 5 10024 10020 9941 -75 20 -43 N ATOM 1182 C2 U R 5 -1.023 6.793 18.001 1.00 79.95 C ANISOU 1182 C2 U R 5 10158 10080 10136 -23 -29 -44 C ATOM 1183 O2 U R 5 0.075 6.297 17.800 1.00 80.12 O ANISOU 1183 O2 U R 5 10186 10076 10177 -16 -20 -71 O ATOM 1184 N3 U R 5 -1.781 6.383 19.073 1.00 80.69 N ANISOU 1184 N3 U R 5 10234 10188 10235 -76 10 -37 N ATOM 1185 C4 U R 5 -3.031 6.853 19.430 1.00 81.23 C ANISOU 1185 C4 U R 5 10262 10286 10315 -35 -10 -13 C ATOM 1186 O4 U R 5 -3.583 6.389 20.418 1.00 82.75 O ANISOU 1186 O4 U R 5 10514 10538 10388 -38 23 8 O ATOM 1187 C5 U R 5 -3.576 7.875 18.572 1.00 81.02 C ANISOU 1187 C5 U R 5 10255 10261 10267 -38 9 -4 C ATOM 1188 C6 U R 5 -2.857 8.291 17.519 1.00 80.23 C ANISOU 1188 C6 U R 5 10110 10174 10199 1 -22 -42 C TER 1189 U R 5 HETATM 1190 NA NA A 68 5.948 4.450 -1.124 1.00 38.69 NA ANISOU 1190 NA NA A 68 4639 5598 4461 -469 169 362 NA HETATM 1191 MG MG A 69 29.083 7.018 14.131 1.00 26.86 MG ANISOU 1191 MG MG A 69 2760 3905 3538 492 -597 477 MG HETATM 1192 O HOH A 70 18.041 9.256 -3.640 1.00 28.33 O ANISOU 1192 O HOH A 70 4526 3226 3010 -243 366 -497 O HETATM 1193 O HOH A 71 13.596 12.893 7.091 1.00 12.33 O ANISOU 1193 O HOH A 71 1481 1644 1558 -130 -39 161 O HETATM 1194 O AHOH A 72 2.817 -3.309 2.679 0.50 17.13 O ANISOU 1194 O AHOH A 72 1497 2389 2621 -617 -514 969 O HETATM 1195 O HOH A 73 19.629 15.335 11.446 1.00 13.06 O ANISOU 1195 O HOH A 73 1499 1653 1807 -175 53 -204 O HETATM 1196 O HOH A 74 23.164 17.930 13.014 1.00 29.58 O ANISOU 1196 O HOH A 74 4231 3335 3671 -255 -400 -1106 O HETATM 1197 O HOH A 75 20.921 21.317 4.409 1.00 21.02 O ANISOU 1197 O HOH A 75 2598 2423 2963 474 -29 183 O HETATM 1198 O HOH A 76 22.252 16.010 11.230 1.00 15.61 O ANISOU 1198 O HOH A 76 1686 2120 2122 -276 -63 -197 O HETATM 1199 O HOH A 77 12.604 22.160 9.014 1.00 18.81 O ANISOU 1199 O HOH A 77 3148 2311 1685 -206 311 140 O HETATM 1200 O HOH A 78 13.805 -1.730 3.813 1.00 34.82 O ANISOU 1200 O HOH A 78 3888 4517 4824 358 -162 60 O HETATM 1201 O HOH A 79 10.378 1.466 1.655 1.00 18.65 O ANISOU 1201 O HOH A 79 2280 2548 2259 -105 -102 -434 O HETATM 1202 O HOH A 80 5.037 -2.616 0.520 1.00 30.12 O ANISOU 1202 O HOH A 80 3991 3016 4437 -937 275 -549 O HETATM 1203 O HOH A 81 9.225 17.202 8.734 1.00 34.33 O ANISOU 1203 O HOH A 81 4591 4601 3850 407 150 7 O HETATM 1204 O HOH A 82 16.280 -0.880 3.930 1.00 24.89 O ANISOU 1204 O HOH A 82 4313 2111 3032 369 -88 -67 O HETATM 1205 O HOH A 83 27.315 9.563 11.161 1.00 20.82 O ANISOU 1205 O HOH A 83 2154 2931 2824 -202 -300 170 O HETATM 1206 O HOH A 84 29.154 7.900 4.170 1.00 38.33 O ANISOU 1206 O HOH A 84 3990 5036 5538 293 78 -16 O HETATM 1207 O HOH A 85 3.452 1.872 -3.865 1.00 33.30 O ANISOU 1207 O HOH A 85 3408 5359 3883 -260 -125 193 O HETATM 1208 O HOH A 86 25.844 12.336 15.331 1.00 26.04 O ANISOU 1208 O HOH A 86 3399 3846 2646 -500 -862 415 O HETATM 1209 O HOH A 87 10.312 2.384 -0.952 1.00 23.19 O ANISOU 1209 O HOH A 87 2974 3098 2738 -568 -384 -143 O HETATM 1210 O HOH A 88 22.347 -2.135 1.586 1.00 31.65 O ANISOU 1210 O HOH A 88 4650 2839 4533 537 178 -810 O HETATM 1211 O HOH A 89 16.336 -2.289 11.505 1.00 31.27 O ANISOU 1211 O HOH A 89 3921 4203 3757 -126 -48 271 O HETATM 1212 O HOH A 90 14.035 3.628 -2.005 1.00 28.35 O ANISOU 1212 O HOH A 90 2895 3244 4632 -347 -583 -17 O HETATM 1213 O HOH A 91 10.747 0.995 -4.794 1.00 37.08 O ANISOU 1213 O HOH A 91 4737 4244 5107 -300 -17 -482 O HETATM 1214 O HOH A 92 29.104 7.634 12.043 1.00 26.85 O ANISOU 1214 O HOH A 92 3045 3570 3584 372 -314 238 O HETATM 1215 O HOH A 93 22.151 14.441 14.510 1.00 27.83 O ANISOU 1215 O HOH A 93 3249 3774 3550 278 -348 -159 O HETATM 1216 O HOH A 94 12.204 16.434 -0.811 1.00 34.73 O ANISOU 1216 O HOH A 94 4966 3788 4440 -53 -450 245 O HETATM 1217 O HOH A 95 17.701 25.375 11.267 1.00 22.52 O ANISOU 1217 O HOH A 95 3079 3129 2348 -24 -148 -290 O HETATM 1218 O HOH A 96 8.340 19.695 10.604 1.00 29.03 O ANISOU 1218 O HOH A 96 3696 4233 3098 -484 -693 335 O HETATM 1219 O HOH A 97 11.926 13.920 0.637 1.00 22.99 O ANISOU 1219 O HOH A 97 1921 2960 3853 340 -197 876 O HETATM 1220 O HOH A 98 12.437 15.191 4.228 1.00 19.99 O ANISOU 1220 O HOH A 98 2066 2578 2949 189 261 395 O HETATM 1221 O HOH A 99 29.372 -0.566 6.260 1.00 28.61 O ANISOU 1221 O HOH A 99 3372 3537 3959 1061 283 386 O HETATM 1222 O HOH A 100 10.290 14.508 5.844 1.00 32.61 O ANISOU 1222 O HOH A 100 3236 4617 4536 -445 141 11 O HETATM 1223 O HOH A 101 25.617 15.314 8.637 1.00 26.03 O ANISOU 1223 O HOH A 101 2369 3827 3691 -350 -283 285 O HETATM 1224 O HOH A 102 19.247 8.461 19.238 1.00 35.88 O ANISOU 1224 O HOH A 102 4502 4958 4172 77 -32 -497 O HETATM 1225 O HOH A 103 13.960 19.903 7.220 1.00 25.94 O ANISOU 1225 O HOH A 103 3217 2554 4085 -166 575 711 O HETATM 1226 O HOH A 104 17.060 -0.517 13.817 1.00 23.24 O ANISOU 1226 O HOH A 104 3713 2052 3063 185 -64 376 O HETATM 1227 O HOH A 105 22.072 9.868 16.251 1.00 22.29 O ANISOU 1227 O HOH A 105 2713 3544 2210 71 -581 -110 O HETATM 1228 O HOH A 106 10.005 14.761 8.596 1.00 30.03 O ANISOU 1228 O HOH A 106 2857 3436 5118 -365 290 145 O HETATM 1229 O HOH A 107 8.976 -1.372 -0.848 1.00 39.80 O ANISOU 1229 O HOH A 107 4603 5043 5474 -29 -85 -33 O HETATM 1230 O HOH A 108 5.293 10.901 12.115 1.00 24.28 O ANISOU 1230 O HOH A 108 2687 3674 2864 -362 192 38 O HETATM 1231 O HOH A 109 28.026 5.189 6.564 1.00 31.21 O ANISOU 1231 O HOH A 109 3325 3629 4902 435 87 218 O HETATM 1232 O HOH A 110 13.609 30.338 10.518 1.00 29.18 O ANISOU 1232 O HOH A 110 3703 3859 3522 -196 82 -305 O HETATM 1233 O HOH A 111 20.904 7.825 17.384 1.00 26.89 O ANISOU 1233 O HOH A 111 2724 3579 3914 129 -588 -554 O HETATM 1234 O HOH A 112 24.383 0.523 10.510 1.00 28.53 O ANISOU 1234 O HOH A 112 3077 3753 4009 763 -212 -177 O HETATM 1235 O HOH A 113 23.539 17.191 9.074 1.00 23.58 O ANISOU 1235 O HOH A 113 3216 3048 2695 272 764 200 O HETATM 1236 O HOH A 114 12.618 25.625 15.748 1.00 28.17 O ANISOU 1236 O HOH A 114 3596 4037 3071 -294 522 5 O HETATM 1237 O HOH A 115 30.332 8.543 14.441 1.00 30.28 O ANISOU 1237 O HOH A 115 3346 3801 4358 -135 -859 -8 O HETATM 1238 O HOH A 117 23.586 19.639 8.008 1.00 23.58 O ANISOU 1238 O HOH A 117 2884 2714 3360 -267 46 -142 O HETATM 1239 O HOH A 121 13.741 -1.286 10.798 1.00 28.62 O ANISOU 1239 O HOH A 121 3657 3219 3996 108 -228 636 O HETATM 1240 O HOH A 122 30.704 5.774 13.843 1.00 31.48 O ANISOU 1240 O HOH A 122 3544 3947 4469 145 49 142 O HETATM 1241 O HOH A 123 11.949 17.836 3.784 1.00 33.20 O ANISOU 1241 O HOH A 123 4419 3240 4955 54 -373 402 O HETATM 1242 O HOH A 126 22.844 21.838 9.887 1.00 31.62 O ANISOU 1242 O HOH A 126 4233 3522 4259 -66 79 271 O HETATM 1243 O HOH A 127 27.437 8.139 14.566 1.00 25.88 O ANISOU 1243 O HOH A 127 2909 3374 3547 380 -163 1134 O HETATM 1244 O HOH A 130 9.708 21.812 9.709 1.00 33.29 O ANISOU 1244 O HOH A 130 4260 5142 3245 -163 -466 676 O HETATM 1245 O HOH A 131 27.857 5.274 13.673 1.00 27.89 O ANISOU 1245 O HOH A 131 3312 3697 3586 -70 -103 14 O HETATM 1246 O HOH A 136 17.706 27.898 12.081 1.00 36.41 O ANISOU 1246 O HOH A 136 5361 4113 4358 -32 -259 -352 O HETATM 1247 O HOH A 140 6.488 -1.491 10.747 1.00 35.80 O ANISOU 1247 O HOH A 140 4366 4514 4720 -456 -377 -247 O HETATM 1248 O HOH A 143 15.780 17.188 -1.355 1.00 32.13 O ANISOU 1248 O HOH A 143 4482 3370 4353 -460 20 493 O HETATM 1249 O HOH A 151 7.149 7.925 -3.093 1.00 39.25 O ANISOU 1249 O HOH A 151 5286 5390 4235 78 -279 381 O HETATM 1250 O HOH A 160 29.035 6.465 16.038 1.00 27.70 O ANISOU 1250 O HOH A 160 3648 3730 3146 155 -323 239 O HETATM 1251 O HOH A 168 10.989 27.837 15.150 1.00 39.41 O ANISOU 1251 O HOH A 168 5145 4633 5196 3 251 350 O HETATM 1252 O HOH A 174 12.247 18.339 0.977 1.00 36.54 O ANISOU 1252 O HOH A 174 4760 4056 5067 115 -275 215 O HETATM 1253 O HOH A 176 28.554 11.154 0.606 1.00 33.62 O ANISOU 1253 O HOH A 176 3301 4413 5059 -409 -188 407 O HETATM 1254 O HOH A 178 9.473 8.066 -5.298 1.00 42.73 O ANISOU 1254 O HOH A 178 5228 5260 5746 242 -436 368 O HETATM 1255 O HOH A 184 8.386 9.869 0.060 1.00 33.99 O ANISOU 1255 O HOH A 184 4331 4204 4380 -171 -168 -259 O HETATM 1256 O HOH A 185 22.749 12.458 16.514 1.00 32.50 O ANISOU 1256 O HOH A 185 4660 4256 3431 545 -395 248 O HETATM 1257 O HOH A 186 21.711 23.671 6.069 1.00 29.92 O ANISOU 1257 O HOH A 186 3741 3793 3833 125 -457 -40 O HETATM 1258 O HOH A 188 8.398 -1.909 1.847 1.00 31.94 O ANISOU 1258 O HOH A 188 4314 2812 5009 188 84 -577 O HETATM 1259 O HOH A 189 11.104 -2.924 1.146 1.00 39.35 O ANISOU 1259 O HOH A 189 4402 4898 5650 -348 -259 95 O HETATM 1260 O HOH A 190 14.699 6.908 -6.009 1.00 36.90 O ANISOU 1260 O HOH A 190 4583 5025 4411 -143 -51 197 O HETATM 1261 O HOH A 191 28.349 16.770 10.012 1.00 40.00 O ANISOU 1261 O HOH A 191 4996 4628 5574 -69 108 269 O HETATM 1262 O HOH A 193 7.950 27.406 14.721 1.00 37.06 O ANISOU 1262 O HOH A 193 5307 4446 4326 -18 102 711 O HETATM 1263 O HOH A 194 21.978 16.349 -4.880 1.00 34.29 O ANISOU 1263 O HOH A 194 4424 4300 4304 120 -177 0 O HETATM 1264 O HOH A 195 12.696 4.637 18.772 1.00 37.94 O ANISOU 1264 O HOH A 195 4919 5083 4410 -242 -97 29 O HETATM 1265 O HOH A 196 3.911 6.173 -4.919 1.00 42.28 O ANISOU 1265 O HOH A 196 5160 5515 5389 -230 -102 436 O HETATM 1266 O HOH A 197 20.767 -4.136 6.047 1.00 38.57 O ANISOU 1266 O HOH A 197 4899 4582 5173 197 -81 -13 O HETATM 1267 O HOH A 198 25.513 -0.668 3.664 1.00 33.24 O ANISOU 1267 O HOH A 198 3616 4399 4612 505 103 47 O HETATM 1268 O HOH A 200 7.119 26.829 12.339 1.00 46.14 O ANISOU 1268 O HOH A 200 5860 5594 6075 136 -78 159 O HETATM 1269 O HOH A 203 8.931 -3.868 4.395 1.00 38.04 O ANISOU 1269 O HOH A 203 5175 4180 5097 -276 79 -268 O HETATM 1270 O HOH A 209 12.200 -1.508 13.860 1.00 39.48 O ANISOU 1270 O HOH A 209 4774 4652 5572 -316 28 232 O HETATM 1271 O HOH A 215 30.889 10.431 12.593 1.00 41.16 O ANISOU 1271 O HOH A 215 4826 5681 5129 65 -646 129 O HETATM 1272 O HOH A 217 9.151 17.118 5.104 1.00 44.20 O ANISOU 1272 O HOH A 217 5540 5516 5738 -132 35 116 O HETATM 1273 O HOH A 218 19.517 2.576 -6.392 1.00 48.90 O ANISOU 1273 O HOH A 218 6390 5911 6276 98 -17 111 O HETATM 1274 O HOH A 221 23.925 0.667 14.176 1.00 40.05 O ANISOU 1274 O HOH A 221 4645 5214 5358 89 -378 314 O HETATM 1275 O HOH A 223 30.689 15.003 12.762 1.00 47.43 O ANISOU 1275 O HOH A 223 5570 6166 6283 -29 -100 -63 O HETATM 1276 O HOH A 224 3.251 -0.893 -4.245 1.00 35.61 O ANISOU 1276 O HOH A 224 4419 5072 4035 -153 218 300 O HETATM 1277 O HOH A 230 13.836 1.072 16.892 1.00 54.14 O ANISOU 1277 O HOH A 230 6949 6791 6828 40 -41 76 O HETATM 1278 O HOH A 231 25.335 4.248 0.418 1.00 33.57 O ANISOU 1278 O HOH A 231 4284 3953 4516 356 915 -489 O HETATM 1279 O HOH A 233 29.462 5.688 10.069 1.00 37.48 O ANISOU 1279 O HOH A 233 4783 4469 4989 455 173 69 O HETATM 1280 O HOH A 235 7.736 2.742 18.763 0.50 27.64 O ANISOU 1280 O HOH A 235 3767 3406 3329 -338 70 266 O HETATM 1281 O HOH A 236 4.020 6.905 12.266 1.00 38.66 O ANISOU 1281 O HOH A 236 4250 5503 4934 180 199 -43 O HETATM 1282 O HOH A 237 32.017 16.830 9.700 1.00 37.32 O ANISOU 1282 O HOH A 237 4529 4731 4917 -622 -47 -197 O HETATM 1283 O HOH A 238 4.989 8.929 -1.743 1.00 43.91 O ANISOU 1283 O HOH A 238 5089 5919 5675 -224 -161 154 O HETATM 1284 O HOH A 239 11.834 -2.362 8.230 1.00 45.28 O ANISOU 1284 O HOH A 239 5900 5564 5738 -110 43 251 O HETATM 1285 O HOH A 240 15.191 27.496 14.108 1.00 40.13 O ANISOU 1285 O HOH A 240 5401 4926 4921 -79 -145 -26 O HETATM 1286 O HOH A 241 18.309 -1.850 -1.766 1.00 50.67 O ANISOU 1286 O HOH A 241 6250 6226 6773 119 129 181 O HETATM 1287 O HOH A 253 20.660 23.221 12.972 1.00 39.29 O ANISOU 1287 O HOH A 253 5238 4760 4931 -247 -83 -317 O HETATM 1288 O HOH A 257 15.529 29.399 12.075 1.00 41.77 O ANISOU 1288 O HOH A 257 5152 5282 5437 -25 40 99 O HETATM 1289 O HOH A 258 15.128 -0.502 15.409 1.00 59.71 O ANISOU 1289 O HOH A 258 7629 7609 7447 108 -84 98 O HETATM 1290 O HOH A 259 8.897 23.939 10.069 1.00 36.61 O ANISOU 1290 O HOH A 259 4684 5651 3574 -342 545 100 O HETATM 1291 O HOH A 261 18.852 -3.944 4.147 1.00 42.95 O ANISOU 1291 O HOH A 261 5693 5136 5488 161 -77 13 O HETATM 1292 O HOH A 263 29.027 17.328 16.344 1.00 51.75 O ANISOU 1292 O HOH A 263 6602 6595 6464 -40 -48 -129 O HETATM 1293 O HOH A 264 28.335 3.449 4.723 1.00 36.52 O ANISOU 1293 O HOH A 264 4350 4888 4637 311 705 -217 O HETATM 1294 O HOH A 265 9.753 12.221 -0.247 1.00 39.38 O ANISOU 1294 O HOH A 265 4714 5033 5215 182 21 139 O HETATM 1295 O HOH B 68 5.837 24.167 23.120 1.00 13.17 O ANISOU 1295 O HOH B 68 1805 1565 1634 -124 -3 -358 O HETATM 1296 O HOH B 69 -3.630 22.558 31.015 1.00 24.02 O ANISOU 1296 O HOH B 69 2389 3353 3384 920 571 411 O HETATM 1297 O HOH B 70 -0.408 22.485 27.554 1.00 14.55 O ANISOU 1297 O HOH B 70 1802 1857 1868 200 130 -204 O HETATM 1298 O HOH B 71 16.035 17.027 18.947 1.00 14.41 O ANISOU 1298 O HOH B 71 1711 2126 1636 58 212 7 O HETATM 1299 O HOH B 72 7.830 8.129 19.403 1.00 16.11 O ANISOU 1299 O HOH B 72 1924 2395 1802 -434 64 -269 O HETATM 1300 O HOH B 73 14.335 12.244 20.470 1.00 18.94 O ANISOU 1300 O HOH B 73 2654 2359 2181 463 543 16 O HETATM 1301 O HOH B 74 19.446 15.209 14.230 1.00 15.19 O ANISOU 1301 O HOH B 74 2324 1863 1583 249 49 -200 O HETATM 1302 O HOH B 75 -3.558 32.181 29.324 1.00 29.09 O ANISOU 1302 O HOH B 75 3587 4430 3033 348 261 544 O HETATM 1303 O HOH B 76 0.658 14.764 33.009 1.00 16.82 O ANISOU 1303 O HOH B 76 1926 2297 2165 -227 486 162 O HETATM 1304 O HOH B 77 17.392 11.094 21.789 1.00 27.06 O ANISOU 1304 O HOH B 77 3633 3283 3366 490 180 152 O HETATM 1305 O HOH B 78 4.896 9.062 19.972 1.00 18.77 O ANISOU 1305 O HOH B 78 2271 2283 2578 47 -17 -790 O HETATM 1306 O HOH B 79 16.097 22.525 29.665 1.00 24.97 O ANISOU 1306 O HOH B 79 3038 3277 3172 567 -64 -791 O HETATM 1307 O HOH B 80 -1.073 21.951 30.153 1.00 15.42 O ANISOU 1307 O HOH B 80 2116 1820 1921 129 471 8 O HETATM 1308 O HOH B 81 14.980 9.135 28.450 1.00 22.38 O ANISOU 1308 O HOH B 81 2749 2415 3338 897 -98 11 O HETATM 1309 O HOH B 82 15.434 29.019 32.484 1.00 33.30 O ANISOU 1309 O HOH B 82 3237 4493 4923 -582 102 -411 O HETATM 1310 O HOH B 83 -2.024 32.308 34.893 1.00 35.99 O ANISOU 1310 O HOH B 83 4736 4946 3990 -357 119 -418 O HETATM 1311 O HOH B 84 6.996 14.648 36.655 1.00 25.58 O ANISOU 1311 O HOH B 84 3150 3357 3213 -333 296 387 O HETATM 1312 O HOH B 85 0.511 20.980 33.807 1.00 17.48 O ANISOU 1312 O HOH B 85 2798 1959 1882 -47 289 32 O HETATM 1313 O HOH B 86 6.305 9.813 15.206 1.00 30.59 O ANISOU 1313 O HOH B 86 5225 2736 3658 224 98 -358 O HETATM 1314 O HOH B 87 2.607 29.696 25.691 1.00 20.67 O ANISOU 1314 O HOH B 87 2914 2758 2181 364 -256 -321 O HETATM 1315 O HOH B 88 -0.026 31.484 24.808 1.00 20.00 O ANISOU 1315 O HOH B 88 2284 2618 2694 379 -591 65 O HETATM 1316 O HOH B 89 11.746 27.457 24.420 1.00 19.65 O ANISOU 1316 O HOH B 89 3356 1703 2407 -228 493 199 O HETATM 1317 O HOH B 90 13.563 27.052 35.552 1.00 20.38 O ANISOU 1317 O HOH B 90 3079 2121 2543 -327 55 -226 O HETATM 1318 O HOH B 91 -3.378 18.929 28.978 1.00 24.33 O ANISOU 1318 O HOH B 91 2474 2842 3926 138 113 -196 O HETATM 1319 O HOH B 92 2.531 18.158 39.817 1.00 21.39 O ANISOU 1319 O HOH B 92 2593 3087 2444 -145 715 200 O HETATM 1320 O HOH B 93 18.051 18.640 19.941 1.00 20.30 O ANISOU 1320 O HOH B 93 2353 2657 2703 -415 465 -842 O HETATM 1321 O HOH B 94 17.481 18.360 24.106 1.00 23.55 O ANISOU 1321 O HOH B 94 3453 3033 2462 367 1099 152 O HETATM 1322 O HOH B 95 -6.017 35.557 27.475 1.00 31.86 O ANISOU 1322 O HOH B 95 3275 5185 3644 -670 -369 -195 O HETATM 1323 O HOH B 96 17.443 14.692 16.034 1.00 21.07 O ANISOU 1323 O HOH B 96 3082 2643 2279 523 741 293 O HETATM 1324 O HOH B 97 5.418 8.142 28.299 1.00 33.72 O ANISOU 1324 O HOH B 97 4797 3597 4414 103 477 852 O HETATM 1325 O HOH B 98 -2.070 20.111 39.755 1.00 22.67 O ANISOU 1325 O HOH B 98 2819 3201 2594 255 928 111 O HETATM 1326 O HOH B 99 7.598 27.470 23.972 1.00 21.58 O ANISOU 1326 O HOH B 99 3496 2248 2454 -307 219 177 O HETATM 1327 O HOH B 100 8.553 10.763 17.660 1.00 25.96 O ANISOU 1327 O HOH B 100 3156 3605 3100 199 -314 -554 O HETATM 1328 O HOH B 101 -0.885 11.512 30.861 1.00 25.93 O ANISOU 1328 O HOH B 101 3358 2805 3688 -378 212 339 O HETATM 1329 O HOH B 102 -1.835 26.018 25.567 1.00 26.44 O ANISOU 1329 O HOH B 102 3242 3467 3333 785 -1095 -167 O HETATM 1330 O HOH B 103 11.376 11.522 16.965 1.00 26.15 O ANISOU 1330 O HOH B 103 3577 2777 3581 82 511 51 O HETATM 1331 O HOH B 104 6.139 12.254 34.267 1.00 26.40 O ANISOU 1331 O HOH B 104 3540 3404 3084 -134 261 190 O HETATM 1332 O HOH B 105 11.834 12.714 33.807 1.00 36.20 O ANISOU 1332 O HOH B 105 4392 5045 4317 601 -550 17 O HETATM 1333 O HOH B 106 9.078 18.332 38.196 1.00 25.89 O ANISOU 1333 O HOH B 106 4469 2769 2597 -595 862 -91 O HETATM 1334 O HOH B 107 19.768 15.785 18.200 1.00 33.27 O ANISOU 1334 O HOH B 107 4715 4140 3783 190 63 -374 O HETATM 1335 O HOH B 108 19.686 22.372 27.205 1.00 31.75 O ANISOU 1335 O HOH B 108 3385 4184 4494 -682 -201 145 O HETATM 1336 O HOH B 109 17.777 24.758 13.964 1.00 31.39 O ANISOU 1336 O HOH B 109 5165 3819 2941 233 -303 -79 O HETATM 1337 O HOH B 110 12.558 30.495 34.271 1.00 24.20 O ANISOU 1337 O HOH B 110 3180 2536 3477 301 -500 -352 O HETATM 1338 O HOH B 111 0.603 12.357 34.231 1.00 31.20 O ANISOU 1338 O HOH B 111 4543 3372 3938 -613 378 580 O HETATM 1339 O HOH B 112 -3.708 15.941 30.864 1.00 28.15 O ANISOU 1339 O HOH B 112 2979 3763 3953 -618 -326 -73 O HETATM 1340 O HOH B 113 0.240 25.335 33.620 1.00 29.06 O ANISOU 1340 O HOH B 113 4289 3145 3606 204 509 52 O HETATM 1341 O HOH B 114 0.466 23.123 32.074 1.00 19.34 O ANISOU 1341 O HOH B 114 2400 2386 2559 -232 -217 119 O HETATM 1342 O HOH B 120 5.784 16.339 38.796 1.00 30.46 O ANISOU 1342 O HOH B 120 3047 4466 4058 -131 -78 199 O HETATM 1343 O HOH B 125 14.318 11.082 17.944 1.00 33.18 O ANISOU 1343 O HOH B 125 4112 3773 4720 -400 185 -70 O HETATM 1344 O HOH B 132 11.807 29.592 28.935 1.00 30.99 O ANISOU 1344 O HOH B 132 4417 3852 3505 -53 99 -274 O HETATM 1345 O HOH B 137 1.144 30.230 34.303 1.00 26.97 O ANISOU 1345 O HOH B 137 3402 3431 3412 173 -264 -87 O HETATM 1346 O HOH B 142 17.089 16.372 30.329 1.00 35.01 O ANISOU 1346 O HOH B 142 4252 4382 4666 650 -192 0 O HETATM 1347 O HOH B 150 14.567 25.355 19.961 1.00 31.32 O ANISOU 1347 O HOH B 150 4138 3519 4243 -195 439 -62 O HETATM 1348 O HOH B 163 11.927 6.518 25.130 1.00 33.79 O ANISOU 1348 O HOH B 163 3573 4114 5150 636 77 -357 O HETATM 1349 O HOH B 167 18.893 22.530 14.662 0.50 21.83 O ANISOU 1349 O HOH B 167 3557 2463 2272 -495 -539 -21 O HETATM 1350 O HOH B 172 2.931 14.974 41.978 1.00 31.80 O ANISOU 1350 O HOH B 172 3511 4702 3866 -223 279 471 O HETATM 1351 O HOH B 173 3.470 23.565 37.310 1.00 36.55 O ANISOU 1351 O HOH B 173 5152 4124 4611 -79 200 -60 O HETATM 1352 O HOH B 175 16.429 26.967 35.719 1.00 36.61 O ANISOU 1352 O HOH B 175 4319 4555 5036 -111 -80 -184 O HETATM 1353 O HOH B 182 17.806 11.070 19.063 1.00 35.67 O ANISOU 1353 O HOH B 182 4834 4217 4499 681 -272 296 O HETATM 1354 O HOH B 192 18.150 24.791 28.880 1.00 40.16 O ANISOU 1354 O HOH B 192 5107 4984 5166 -196 -339 29 O HETATM 1355 O HOH B 199 9.494 30.470 27.371 1.00 39.24 O ANISOU 1355 O HOH B 199 4696 4994 5219 -296 185 95 O HETATM 1356 O HOH B 201 4.477 23.858 13.234 1.00 31.44 O ANISOU 1356 O HOH B 201 4215 4507 3225 343 -649 33 O HETATM 1357 O HOH B 202 9.972 5.411 22.108 1.00 32.84 O ANISOU 1357 O HOH B 202 4574 3722 4181 366 -58 -533 O HETATM 1358 O HOH B 204 -3.483 30.241 18.445 1.00 33.19 O ANISOU 1358 O HOH B 204 3679 4892 4038 -230 781 -19 O HETATM 1359 O HOH B 211 5.915 20.675 11.028 1.00 42.36 O ANISOU 1359 O HOH B 211 5336 5619 5139 -178 -172 76 O HETATM 1360 O HOH B 212 21.822 18.330 21.359 1.00 37.41 O ANISOU 1360 O HOH B 212 4857 4370 4985 97 74 -49 O HETATM 1361 O HOH B 213 20.373 23.805 16.978 1.00 42.51 O ANISOU 1361 O HOH B 213 5328 5500 5322 -88 180 63 O HETATM 1362 O HOH B 216 6.784 18.635 39.198 1.00 39.91 O ANISOU 1362 O HOH B 216 4920 5225 5019 -271 517 -184 O HETATM 1363 O AHOH B 219 -1.885 21.743 35.353 0.50 20.43 O ANISOU 1363 O AHOH B 219 2398 2838 2525 629 235 -278 O HETATM 1364 O BHOH B 219 -2.970 20.281 36.490 0.50 22.81 O ANISOU 1364 O BHOH B 219 2626 2865 3175 636 338 -515 O HETATM 1365 O HOH B 226 20.952 20.711 25.306 1.00 46.66 O ANISOU 1365 O HOH B 226 5950 6185 5592 66 66 56 O HETATM 1366 O AHOH B 227 17.886 13.545 18.331 0.50 22.83 O ANISOU 1366 O AHOH B 227 2817 3366 2489 847 386 -63 O HETATM 1367 O BHOH B 227 16.422 12.785 17.772 0.50 19.05 O ANISOU 1367 O BHOH B 227 2663 2611 1961 471 607 457 O HETATM 1368 O HOH B 229 5.925 23.440 10.909 1.00 37.27 O ANISOU 1368 O HOH B 229 5293 5273 3594 25 -529 410 O HETATM 1369 O HOH B 232 19.675 24.865 26.556 1.00 39.83 O ANISOU 1369 O HOH B 232 4671 5037 5425 -392 -259 -120 O HETATM 1370 O HOH B 234 10.021 15.951 39.605 1.00 40.17 O ANISOU 1370 O HOH B 234 5351 5076 4833 95 -141 239 O HETATM 1371 O HOH B 242 20.518 22.708 29.840 1.00 43.86 O ANISOU 1371 O HOH B 242 5043 5769 5852 -6 -20 85 O HETATM 1372 O HOH B 243 -3.737 12.617 30.419 1.00 35.36 O ANISOU 1372 O HOH B 243 3571 4886 4976 -68 -99 197 O HETATM 1373 O HOH B 244 19.995 14.127 24.498 1.00 41.82 O ANISOU 1373 O HOH B 244 4940 5635 5312 16 63 -357 O HETATM 1374 O HOH B 245 -2.850 13.585 33.057 1.00 36.20 O ANISOU 1374 O HOH B 245 4396 4223 5133 -650 532 241 O HETATM 1375 O AHOH B 246 -3.072 14.682 36.808 0.50 33.21 O ANISOU 1375 O AHOH B 246 4010 4663 3946 -273 27 10 O HETATM 1376 O BHOH B 246 -3.940 16.353 36.325 0.50 22.32 O ANISOU 1376 O BHOH B 246 2373 3254 2853 -381 579 -140 O HETATM 1377 O HOH B 247 -7.124 17.131 35.360 1.00 45.93 O ANISOU 1377 O HOH B 247 5920 5813 5718 -80 63 25 O HETATM 1378 O HOH B 248 8.576 27.374 21.609 1.00 46.52 O ANISOU 1378 O HOH B 248 6098 5767 5809 250 -16 -176 O HETATM 1379 O HOH B 249 12.970 27.579 22.044 1.00 36.54 O ANISOU 1379 O HOH B 249 5263 4303 4315 -264 156 -103 O HETATM 1380 O HOH B 251 4.398 31.092 24.557 1.00 36.27 O ANISOU 1380 O HOH B 251 5367 4699 3713 13 -128 -232 O HETATM 1381 O HOH B 252 9.443 29.246 24.594 1.00 37.57 O ANISOU 1381 O HOH B 252 4779 4312 5182 -416 -128 290 O HETATM 1382 O HOH B 260 14.644 19.913 37.722 1.00 40.00 O ANISOU 1382 O HOH B 260 5021 5236 4938 185 -24 270 O HETATM 1383 O HOH B 262 22.767 16.925 17.639 1.00 52.03 O ANISOU 1383 O HOH B 262 6594 6530 6644 68 -6 -129 O HETATM 1384 O HOH R 87 -0.481 28.154 24.152 1.00 31.10 O ANISOU 1384 O HOH R 87 3792 4921 3103 344 -137 138 O HETATM 1385 O HOH R 161 -1.026 8.499 22.614 1.00 37.44 O ANISOU 1385 O HOH R 161 4427 4411 5388 -598 30 128 O HETATM 1386 O HOH R 187 2.981 9.254 17.580 1.00 27.35 O ANISOU 1386 O HOH R 187 3209 3553 3630 17 -342 -596 O HETATM 1387 O HOH R 254 2.509 10.311 14.858 1.00 44.39 O ANISOU 1387 O HOH R 254 5828 5597 5441 3 202 -140 O HETATM 1388 O HOH R 255 0.732 4.853 20.681 1.00 32.37 O ANISOU 1388 O HOH R 255 3939 3057 5301 -635 76 192 O CONECT 284 1190 CONECT 297 1190 CONECT 1190 284 297 CONECT 1191 1214 1237 1240 1243 CONECT 1191 1245 1250 CONECT 1214 1191 CONECT 1237 1191 CONECT 1240 1191 CONECT 1243 1191 CONECT 1245 1191 CONECT 1250 1191 MASTER 312 0 2 2 10 0 3 6 1323 3 11 13 END
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Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
2es2
RCSB PDB
PDBbind
67aa, >2ES2_2|Chain... *
3pf5
RCSB PDB
PDBbind
67aa, >3PF5_1|Chains... at 100%
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
3pf4
Complex Type
Protein-Nucleic Acid
PDBbind Subset
general set
Protein Name
Cold shock protein cspB
Ligand Name
7-mer RNA (GUCUUUA)
EC.Number
E.C.-.-.-.-
Resolution
1.38(Å)
Affinity (Kd/Ki/IC50)
Kd=159nM
Release Year
2011
Protein/NA Sequence
Check fasta file
Primary Reference
(2012) Rna Vol. 18: pp. 65-76
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
P32081
Entrez Gene ID
NCBI Entrez Gene ID:
936224
ASD
Information of known allosteric effects of PDB entries
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