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3ds1.pdb
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3ds1.pdb
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HEADER VIRAL PROTEIN 11-JUL-08 3DS1
TITLE HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (E187A) IN COMPLEX WITH AN
TITLE 2 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 CAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, UNP RESIDUES 278-363;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: PEPTIDE INHIBITOR OF CAPSID ASSEMBLY;
COMPND 9 CHAIN: T;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_COMMON: HIV-1;
SOURCE 4 ORGANISM_TAXID: 11698;
SOURCE 5 STRAIN: NL4-3;
SOURCE 6 GENE: GAG;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODONPLUS-RIL;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET11C;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 OTHER_DETAILS: CAI PEPTIDE WAS OBTAINED AS LYOPHILIZED
SOURCE 15 TRIFLUOROACETIC ACID SALTS.
KEYWDS HIV, CAPSID, MUTANT, INHIBITOR, ASSEMBLY, POLYPROTEIN, COMPLEX (VIRAL
KEYWDS 2 PROTEIN-PEPTIDE), MAINLY ALPHA, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.-C.VANEY,S.IGONET,F.A.REY
REVDAT 5 25-OCT-17 3DS1 1 REMARK
REVDAT 4 24-FEB-09 3DS1 1 VERSN
REVDAT 3 25-NOV-08 3DS1 1 JRNL
REVDAT 2 09-SEP-08 3DS1 1 JRNL
REVDAT 1 02-SEP-08 3DS1 0
JRNL AUTH V.BARTONOVA,S.IGONET,J.STICHT,B.GLASS,A.HABERMANN,M.C.VANEY,
JRNL AUTH 2 P.SEHR,J.LEWIS,F.A.REY,H.G.KRAUSSLICH
JRNL TITL RESIDUES IN THE HIV-1 CAPSID ASSEMBLY INHIBITOR BINDING SITE
JRNL TITL 2 ARE ESSENTIAL FOR MAINTAINING THE ASSEMBLY-COMPETENT
JRNL TITL 3 QUATERNARY STRUCTURE OF THE CAPSID PROTEIN.
JRNL REF J.BIOL.CHEM. V. 283 32024 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18772135
JRNL DOI 10.1074/JBC.M804230200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.TERNOIS,J.STICHT,S.DUQUERROY,H.-G.KRAUSSLICH,F.A.REY
REMARK 1 TITL THE HIV-1 CAPSID PROTEIN C-TERMINAL DOMAIN IN COMPLEX WITH A
REMARK 1 TITL 2 VIRUS ASSEMBLY INHIBITOR
REMARK 1 REF NAT.STRUCT.MOL.BIOL. V. 12 678 2005
REMARK 1 REFN ISSN 1545-9993
REMARK 1 PMID 16041386
REMARK 1 DOI 10.1038/NSMB967
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0073
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.17
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 11189
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 559
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 800
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 717
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.12000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.24000
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): 0.172
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.628
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 780 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1059 ; 1.357 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 98 ; 4.843 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 35 ;31.027 ;24.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 134 ;12.312 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;16.118 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 117 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 594 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 379 ; 0.212 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 540 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 61 ; 0.130 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 50 ; 0.251 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.132 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 499 ; 1.266 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 787 ; 1.959 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 318 ; 3.271 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 271 ; 3.879 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 817 ; 2.852 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 95 ; 4.918 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 763 ; 3.207 ; 3.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.044
REMARK 200 MONOCHROMATOR : SI(111) MONOCHROMATOR
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11802
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 38.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 73.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 19.70
REMARK 200 R MERGE FOR SHELL (I) : 0.36800
REMARK 200 R SYM FOR SHELL (I) : 0.36800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 9.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2BUO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 100MM AMMONIUM ACETATE,
REMARK 280 10MM MGCL2, PH 4.2, EVAPORATION, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.40650
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 21.44700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 21.44700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 22.70325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 21.44700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 21.44700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 68.10975
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 21.44700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 21.44700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.70325
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 21.44700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 21.44700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 68.10975
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 45.40650
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 300 REMARK: AUTHORS STATE THAT THE ASYMMETRIC UNIT IS COMPOSED
REMARK 300 OF A HETERODIMER OF CHAIN A IN COMPLEX WITH THE INHIBITOR
REMARK 300 OF PARTICLE ASSEMBLY (CHAIN T). TO BUILD THE BIOLOGICAL
REMARK 300 HOMODIMER, ONE SHOULD APPLY THE TRANSFORMATION MATRICES
REMARK 300 DEFINED BELOW ON THE TWO CHAINS A AND T.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, T
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 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 90.81300
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 88 LIES ON A SPECIAL POSITION.
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 SER A 146
REMARK 465 PRO A 147
REMARK 465 ARG A 229
REMARK 465 VAL A 230
REMARK 465 LEU A 231
REMARK 465 PRO T 12
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DS4 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (L211S) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DS2 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (Y169A)
REMARK 900 RELATED ID: 3DS3 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (Y169A) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DTJ RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (E187A)
REMARK 900 RELATED ID: 3DS5 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (N183A)
REMARK 900 RELATED ID: 3DS0 RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (N183A) IN COMPLEX WITH AN
REMARK 900 INHIBITOR OF PARTICLE ASSEMBLY (CAI)
REMARK 900 RELATED ID: 3DPH RELATED DB: PDB
REMARK 900 HIV-1 CAPSID C-TERMINAL DOMAIN MUTANT (L211S)
DBREF 3DS1 A 146 231 UNP Q72497 Q72497_9HIV1 278 363
DBREF 3DS1 T 1 12 PDB 3DS1 3DS1 1 12
SEQADV 3DS1 ALA A 187 UNP Q72497 GLU 319 ENGINEERED
SEQRES 1 A 86 SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY PRO LYS
SEQRES 2 A 86 GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR LYS THR
SEQRES 3 A 86 LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS ASN TRP
SEQRES 4 A 86 MET THR ALA THR LEU LEU VAL GLN ASN ALA ASN PRO ASP
SEQRES 5 A 86 CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY ALA THR
SEQRES 6 A 86 LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL GLY GLY
SEQRES 7 A 86 PRO GLY HIS LYS ALA ARG VAL LEU
SEQRES 1 T 12 ILE THR PHE GLU ASP LEU LEU ASP TYR TYR GLY PRO
FORMUL 3 HOH *87(H2 O)
HELIX 1 1 SER A 149 ILE A 153 5 5
HELIX 2 2 PRO A 160 GLU A 175 1 16
HELIX 3 3 SER A 178 ASN A 193 1 16
HELIX 4 4 ASN A 195 GLY A 206 1 12
HELIX 5 5 THR A 210 GLN A 219 1 10
HELIX 6 6 THR T 2 GLY T 11 1 10
CISPEP 1 GLY A 223 PRO A 224 0 5.07
CRYST1 42.894 42.894 90.813 90.00 90.00 90.00 P 41 21 2 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 0.023313 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011012 0.00000
ATOM 1 N THR A 148 3.942 2.836 32.262 1.00 37.01 N
ANISOU 1 N THR A 148 4727 4643 4691 -25 -25 12 N
ATOM 2 CA THR A 148 5.032 3.798 32.417 1.00 34.29 C
ANISOU 2 CA THR A 148 4463 4295 4271 -14 -51 -32 C
ATOM 3 C THR A 148 5.305 4.114 33.906 1.00 31.82 C
ANISOU 3 C THR A 148 4107 3991 3989 -36 -29 -19 C
ATOM 4 O THR A 148 4.648 3.552 34.798 1.00 32.58 O
ANISOU 4 O THR A 148 4221 4040 4118 -108 -44 -49 O
ATOM 5 CB THR A 148 4.753 5.074 31.573 1.00 34.89 C
ANISOU 5 CB THR A 148 4514 4409 4332 -16 -55 -6 C
ATOM 6 OG1 THR A 148 4.362 4.682 30.248 1.00 36.93 O
ANISOU 6 OG1 THR A 148 4813 4617 4602 -56 -63 -20 O
ATOM 7 CG2 THR A 148 5.998 5.972 31.462 1.00 34.21 C
ANISOU 7 CG2 THR A 148 4448 4305 4245 -15 -26 -7 C
ATOM 8 N SER A 149 6.307 4.954 34.167 1.00 27.39 N
ANISOU 8 N SER A 149 3795 3218 3391 11 -33 -77 N
ATOM 9 CA SER A 149 6.637 5.404 35.530 1.00 23.65 C
ANISOU 9 CA SER A 149 3247 2725 3013 95 -5 -31 C
ATOM 10 C SER A 149 6.742 6.903 35.467 1.00 20.54 C
ANISOU 10 C SER A 149 2865 2346 2593 108 27 -78 C
ATOM 11 O SER A 149 7.232 7.452 34.485 1.00 20.11 O
ANISOU 11 O SER A 149 2970 2141 2529 278 96 -181 O
ATOM 12 CB SER A 149 8.000 4.868 35.983 1.00 23.39 C
ANISOU 12 CB SER A 149 3197 2786 2904 93 -27 -30 C
ATOM 13 OG SER A 149 8.457 5.457 37.213 1.00 21.07 O
ANISOU 13 OG SER A 149 2765 2356 2883 200 -90 35 O
ATOM 14 N ILE A 150 6.338 7.565 36.543 1.00 18.31 N
ANISOU 14 N ILE A 150 2474 2070 2412 145 11 -27 N
ATOM 15 CA ILE A 150 6.545 9.002 36.649 1.00 17.23 C
ANISOU 15 CA ILE A 150 2267 1962 2315 115 118 22 C
ATOM 16 C ILE A 150 8.026 9.369 36.499 1.00 17.20 C
ANISOU 16 C ILE A 150 2267 1982 2286 144 58 23 C
ATOM 17 O ILE A 150 8.361 10.466 36.066 1.00 17.38 O
ANISOU 17 O ILE A 150 2263 2026 2312 204 223 158 O
ATOM 18 CB ILE A 150 5.949 9.546 37.996 1.00 16.23 C
ANISOU 18 CB ILE A 150 2160 1807 2197 159 115 -62 C
ATOM 19 CG1 ILE A 150 5.868 11.096 38.006 1.00 15.65 C
ANISOU 19 CG1 ILE A 150 2060 1729 2155 70 61 97 C
ATOM 20 CG2 ILE A 150 6.674 8.969 39.211 1.00 17.15 C
ANISOU 20 CG2 ILE A 150 1986 2178 2348 173 167 0 C
ATOM 21 CD1 ILE A 150 5.087 11.668 36.813 1.00 16.55 C
ANISOU 21 CD1 ILE A 150 2101 1960 2225 206 75 62 C
ATOM 22 N LEU A 151 8.913 8.437 36.852 1.00 17.85 N
ANISOU 22 N LEU A 151 2302 2074 2403 191 131 71 N
ATOM 23 CA LEU A 151 10.342 8.689 36.790 1.00 19.68 C
ANISOU 23 CA LEU A 151 2465 2473 2539 171 88 115 C
ATOM 24 C LEU A 151 10.826 8.838 35.353 1.00 20.52 C
ANISOU 24 C LEU A 151 2550 2600 2645 113 137 110 C
ATOM 25 O LEU A 151 11.895 9.422 35.111 1.00 22.18 O
ANISOU 25 O LEU A 151 2657 2856 2911 151 205 191 O
ATOM 26 CB LEU A 151 11.089 7.551 37.465 1.00 19.91 C
ANISOU 26 CB LEU A 151 2513 2477 2575 231 114 175 C
ATOM 27 CG LEU A 151 10.812 7.376 38.954 1.00 22.16 C
ANISOU 27 CG LEU A 151 2834 2851 2733 196 56 189 C
ATOM 28 CD1 LEU A 151 11.638 6.212 39.450 1.00 24.28 C
ANISOU 28 CD1 LEU A 151 3090 3141 2993 327 19 231 C
ATOM 29 CD2 LEU A 151 11.148 8.619 39.710 1.00 23.00 C
ANISOU 29 CD2 LEU A 151 3026 2871 2841 414 21 116 C
ATOM 30 N ASP A 152 10.030 8.316 34.424 1.00 20.88 N
ANISOU 30 N ASP A 152 2680 2636 2615 122 180 60 N
ATOM 31 CA ASP A 152 10.339 8.325 32.991 1.00 22.01 C
ANISOU 31 CA ASP A 152 2852 2826 2684 86 109 54 C
ATOM 32 C ASP A 152 9.888 9.591 32.273 1.00 20.70 C
ANISOU 32 C ASP A 152 2687 2638 2540 77 143 41 C
ATOM 33 O ASP A 152 10.174 9.757 31.083 1.00 21.60 O
ANISOU 33 O ASP A 152 2817 2856 2531 117 141 -22 O
ATOM 34 CB ASP A 152 9.702 7.107 32.313 1.00 23.45 C
ANISOU 34 CB ASP A 152 2997 3029 2881 0 108 19 C
ATOM 35 CG ASP A 152 10.217 5.778 32.877 1.00 27.00 C
ANISOU 35 CG ASP A 152 3374 3396 3488 72 -46 37 C
ATOM 36 OD1 ASP A 152 11.352 5.747 33.409 1.00 31.99 O
ANISOU 36 OD1 ASP A 152 3566 4190 4399 263 -60 22 O
ATOM 37 OD2 ASP A 152 9.479 4.769 32.809 1.00 31.30 O
ANISOU 37 OD2 ASP A 152 4129 3840 3922 -70 147 -124 O
ATOM 38 N ILE A 153 9.173 10.478 32.965 1.00 19.29 N
ANISOU 38 N ILE A 153 2485 2500 2345 24 100 45 N
ATOM 39 CA ILE A 153 8.617 11.669 32.301 1.00 18.26 C
ANISOU 39 CA ILE A 153 2338 2321 2279 40 129 11 C
ATOM 40 C ILE A 153 9.598 12.816 32.383 1.00 18.12 C
ANISOU 40 C ILE A 153 2325 2287 2270 43 122 18 C
ATOM 41 O ILE A 153 9.974 13.254 33.465 1.00 19.04 O
ANISOU 41 O ILE A 153 2466 2426 2341 -43 169 112 O
ATOM 42 CB ILE A 153 7.239 12.088 32.891 1.00 17.42 C
ANISOU 42 CB ILE A 153 2231 2161 2225 53 125 27 C
ATOM 43 CG1 ILE A 153 6.272 10.892 32.847 1.00 18.54 C
ANISOU 43 CG1 ILE A 153 2305 2440 2299 -18 -31 -52 C
ATOM 44 CG2 ILE A 153 6.677 13.326 32.158 1.00 17.18 C
ANISOU 44 CG2 ILE A 153 2137 2321 2067 76 24 -31 C
ATOM 45 CD1 ILE A 153 5.987 10.367 31.441 1.00 19.54 C
ANISOU 45 CD1 ILE A 153 2452 2538 2433 51 146 -159 C
ATOM 46 N ARG A 154 10.044 13.277 31.224 1.00 17.29 N
ANISOU 46 N ARG A 154 2245 2145 2175 96 102 92 N
ATOM 47 CA ARG A 154 10.948 14.407 31.190 1.00 18.57 C
ANISOU 47 CA ARG A 154 2326 2355 2372 104 92 50 C
ATOM 48 C ARG A 154 10.615 15.321 30.018 1.00 16.90 C
ANISOU 48 C ARG A 154 2084 2209 2128 112 102 11 C
ATOM 49 O ARG A 154 10.165 14.864 28.975 1.00 17.49 O
ANISOU 49 O ARG A 154 2080 2304 2260 133 160 -41 O
ATOM 50 CB ARG A 154 12.407 13.952 31.114 1.00 19.11 C
ANISOU 50 CB ARG A 154 2337 2463 2459 3 32 98 C
ATOM 51 CG ARG A 154 12.784 13.035 29.985 1.00 22.94 C
ANISOU 51 CG ARG A 154 2850 2930 2933 134 16 85 C
ATOM 52 CD ARG A 154 14.273 12.619 30.125 1.00 23.64 C
ANISOU 52 CD ARG A 154 2744 3081 3154 214 86 -69 C
ATOM 53 NE ARG A 154 15.051 13.648 30.819 1.00 31.27 N
ANISOU 53 NE ARG A 154 3589 3896 4396 90 140 -123 N
ATOM 54 CZ ARG A 154 15.381 13.620 32.112 1.00 28.35 C
ANISOU 54 CZ ARG A 154 3476 3458 3834 -115 -86 -37 C
ATOM 55 NH1 ARG A 154 15.036 12.589 32.881 1.00 34.53 N
ANISOU 55 NH1 ARG A 154 3864 4629 4627 111 39 -146 N
ATOM 56 NH2 ARG A 154 16.057 14.631 32.644 1.00 33.82 N
ANISOU 56 NH2 ARG A 154 3688 4560 4601 289 164 61 N
ATOM 57 N GLN A 155 10.829 16.609 30.218 1.00 16.06 N
ANISOU 57 N GLN A 155 2017 2091 1994 135 208 59 N
ATOM 58 CA GLN A 155 10.464 17.596 29.214 1.00 16.01 C
ANISOU 58 CA GLN A 155 2107 2082 1894 90 217 41 C
ATOM 59 C GLN A 155 11.326 17.436 27.984 1.00 16.98 C
ANISOU 59 C GLN A 155 2210 2224 2015 39 206 78 C
ATOM 60 O GLN A 155 12.537 17.286 28.105 1.00 17.88 O
ANISOU 60 O GLN A 155 2285 2450 2059 86 241 109 O
ATOM 61 CB GLN A 155 10.639 18.991 29.785 1.00 15.67 C
ANISOU 61 CB GLN A 155 2071 1972 1912 69 267 42 C
ATOM 62 CG GLN A 155 10.067 20.092 28.900 1.00 14.50 C
ANISOU 62 CG GLN A 155 1811 1928 1768 -13 135 84 C
ATOM 63 CD GLN A 155 10.160 21.461 29.576 1.00 14.73 C
ANISOU 63 CD GLN A 155 1658 2059 1879 -132 72 -39 C
ATOM 64 OE1 GLN A 155 10.795 21.619 30.625 1.00 15.53 O
ANISOU 64 OE1 GLN A 155 1847 2225 1825 -85 -20 0 O
ATOM 65 NE2 GLN A 155 9.498 22.441 28.998 1.00 16.99 N
ANISOU 65 NE2 GLN A 155 2132 2234 2089 -120 33 149 N
ATOM 66 N GLY A 156 10.685 17.428 26.815 1.00 17.69 N
ANISOU 66 N GLY A 156 2312 2391 2019 18 224 79 N
ATOM 67 CA GLY A 156 11.425 17.427 25.542 1.00 18.67 C
ANISOU 67 CA GLY A 156 2513 2465 2115 -18 273 47 C
ATOM 68 C GLY A 156 12.298 18.674 25.415 1.00 19.33 C
ANISOU 68 C GLY A 156 2473 2575 2295 -27 238 28 C
ATOM 69 O GLY A 156 12.022 19.703 26.043 1.00 18.50 O
ANISOU 69 O GLY A 156 2399 2532 2097 -50 275 122 O
ATOM 70 N PRO A 157 13.361 18.601 24.588 1.00 21.31 N
ANISOU 70 N PRO A 157 2775 2749 2572 -24 276 46 N
ATOM 71 CA PRO A 157 14.317 19.696 24.457 1.00 21.82 C
ANISOU 71 CA PRO A 157 2708 2862 2719 -33 274 12 C
ATOM 72 C PRO A 157 13.643 21.008 24.065 1.00 21.81 C
ANISOU 72 C PRO A 157 2688 2907 2692 -59 230 14 C
ATOM 73 O PRO A 157 14.101 22.069 24.480 1.00 22.71 O
ANISOU 73 O PRO A 157 2816 2960 2851 -162 225 44 O
ATOM 74 CB PRO A 157 15.238 19.240 23.304 1.00 22.14 C
ANISOU 74 CB PRO A 157 2798 2994 2618 -32 306 -5 C
ATOM 75 CG PRO A 157 14.481 18.100 22.605 1.00 23.61 C
ANISOU 75 CG PRO A 157 2953 3061 2955 -48 309 69 C
ATOM 76 CD PRO A 157 13.693 17.453 23.728 1.00 21.62 C
ANISOU 76 CD PRO A 157 2779 2869 2564 24 298 -22 C
ATOM 77 N LYS A 158 12.591 20.932 23.249 1.00 21.05 N
ANISOU 77 N LYS A 158 2567 2850 2578 -180 240 23 N
ATOM 78 CA LYS A 158 11.872 22.111 22.817 1.00 21.27 C
ANISOU 78 CA LYS A 158 2662 2882 2537 -175 118 44 C
ATOM 79 C LYS A 158 10.382 22.082 23.191 1.00 19.72 C
ANISOU 79 C LYS A 158 2498 2591 2404 -206 59 108 C
ATOM 80 O LYS A 158 9.621 22.937 22.780 1.00 18.85 O
ANISOU 80 O LYS A 158 2454 2498 2208 -313 -7 128 O
ATOM 81 CB LYS A 158 12.072 22.343 21.307 1.00 21.97 C
ANISOU 81 CB LYS A 158 2749 2982 2615 -192 143 104 C
ATOM 82 CG LYS A 158 13.516 22.736 20.972 1.00 23.89 C
ANISOU 82 CG LYS A 158 2936 3308 2833 -118 146 163 C
ATOM 83 CD LYS A 158 13.703 23.029 19.497 1.00 24.79 C
ANISOU 83 CD LYS A 158 3264 3337 2817 -97 144 35 C
ATOM 84 CE LYS A 158 13.013 24.335 19.067 1.00 30.31 C
ANISOU 84 CE LYS A 158 3936 3855 3725 23 51 41 C
ATOM 85 NZ LYS A 158 13.646 25.577 19.611 1.00 31.53 N
ANISOU 85 NZ LYS A 158 4026 3971 3980 -179 45 -125 N
ATOM 86 N GLU A 159 9.997 21.126 24.040 1.00 18.49 N
ANISOU 86 N GLU A 159 2387 2457 2180 -276 69 56 N
ATOM 87 CA GLU A 159 8.606 20.935 24.371 1.00 17.47 C
ANISOU 87 CA GLU A 159 2298 2264 2075 -133 52 55 C
ATOM 88 C GLU A 159 8.112 22.101 25.219 1.00 17.50 C
ANISOU 88 C GLU A 159 2269 2336 2044 -184 94 59 C
ATOM 89 O GLU A 159 8.765 22.465 26.205 1.00 17.22 O
ANISOU 89 O GLU A 159 2218 2326 1998 -351 84 31 O
ATOM 90 CB GLU A 159 8.442 19.621 25.138 1.00 17.15 C
ANISOU 90 CB GLU A 159 2315 2196 2001 -242 145 47 C
ATOM 91 CG GLU A 159 6.990 19.321 25.558 1.00 16.69 C
ANISOU 91 CG GLU A 159 2118 2248 1973 -155 123 16 C
ATOM 92 CD GLU A 159 6.850 18.036 26.350 1.00 16.36 C
ANISOU 92 CD GLU A 159 2121 2053 2040 -74 61 -76 C
ATOM 93 OE1 GLU A 159 7.838 17.599 26.955 1.00 17.10 O
ANISOU 93 OE1 GLU A 159 2404 2189 1904 -111 97 48 O
ATOM 94 OE2 GLU A 159 5.714 17.499 26.426 1.00 18.42 O
ANISOU 94 OE2 GLU A 159 2121 2393 2482 -134 -176 -150 O
ATOM 95 N PRO A 160 6.933 22.651 24.886 1.00 17.80 N
ANISOU 95 N PRO A 160 2431 2332 1996 -105 2 95 N
ATOM 96 CA PRO A 160 6.333 23.653 25.775 1.00 17.37 C
ANISOU 96 CA PRO A 160 2336 2302 1962 -63 60 115 C
ATOM 97 C PRO A 160 6.179 23.134 27.193 1.00 16.79 C
ANISOU 97 C PRO A 160 2248 2255 1875 -86 81 30 C
ATOM 98 O PRO A 160 5.739 21.993 27.397 1.00 17.22 O
ANISOU 98 O PRO A 160 2562 2176 1802 -39 98 78 O
ATOM 99 CB PRO A 160 4.957 23.879 25.158 1.00 18.06 C
ANISOU 99 CB PRO A 160 2418 2348 2096 -60 -33 95 C
ATOM 100 CG PRO A 160 5.189 23.627 23.704 1.00 18.13 C
ANISOU 100 CG PRO A 160 2482 2363 2041 -90 111 165 C
ATOM 101 CD PRO A 160 6.092 22.423 23.690 1.00 18.57 C
ANISOU 101 CD PRO A 160 2333 2573 2149 -88 -5 64 C
ATOM 102 N PHE A 161 6.579 23.950 28.159 1.00 16.60 N
ANISOU 102 N PHE A 161 2209 2290 1806 -85 109 60 N
ATOM 103 CA PHE A 161 6.422 23.553 29.572 1.00 16.69 C
ANISOU 103 CA PHE A 161 2280 2266 1794 -86 51 -15 C
ATOM 104 C PHE A 161 4.987 23.105 29.866 1.00 16.53 C
ANISOU 104 C PHE A 161 2207 2192 1881 -17 2 -22 C
ATOM 105 O PHE A 161 4.768 22.099 30.560 1.00 16.38 O
ANISOU 105 O PHE A 161 2110 2239 1874 -109 30 44 O
ATOM 106 CB PHE A 161 6.832 24.708 30.482 1.00 17.04 C
ANISOU 106 CB PHE A 161 2339 2327 1808 -55 55 -47 C
ATOM 107 CG PHE A 161 6.767 24.373 31.927 1.00 18.55 C
ANISOU 107 CG PHE A 161 2623 2385 2039 33 158 35 C
ATOM 108 CD1 PHE A 161 7.703 23.538 32.505 1.00 17.46 C
ANISOU 108 CD1 PHE A 161 2358 2289 1987 -149 10 31 C
ATOM 109 CD2 PHE A 161 5.768 24.943 32.728 1.00 16.96 C
ANISOU 109 CD2 PHE A 161 2103 2434 1904 -133 300 -26 C
ATOM 110 CE1 PHE A 161 7.612 23.215 33.906 1.00 17.52 C
ANISOU 110 CE1 PHE A 161 2539 2104 2014 -64 129 133 C
ATOM 111 CE2 PHE A 161 5.681 24.632 34.097 1.00 19.22 C
ANISOU 111 CE2 PHE A 161 2684 2524 2092 -53 42 -19 C
ATOM 112 CZ PHE A 161 6.604 23.777 34.674 1.00 18.19 C
ANISOU 112 CZ PHE A 161 2619 2387 1902 -91 80 50 C
ATOM 113 N ARG A 162 4.002 23.830 29.340 1.00 17.34 N
ANISOU 113 N ARG A 162 2404 2266 1918 25 -9 28 N
ATOM 114 CA ARG A 162 2.602 23.458 29.540 1.00 18.33 C
ANISOU 114 CA ARG A 162 2374 2473 2116 100 -34 67 C
ATOM 115 C ARG A 162 2.277 22.023 29.068 1.00 17.71 C
ANISOU 115 C ARG A 162 2277 2432 2019 86 -26 64 C
ATOM 116 O ARG A 162 1.468 21.314 29.662 1.00 17.97 O
ANISOU 116 O ARG A 162 2274 2589 1962 92 -28 109 O
ATOM 117 CB ARG A 162 1.650 24.493 28.889 1.00 18.80 C
ANISOU 117 CB ARG A 162 2495 2384 2262 160 -18 46 C
ATOM 118 CG ARG A 162 1.815 24.646 27.404 1.00 21.43 C
ANISOU 118 CG ARG A 162 2800 2764 2577 103 -50 117 C
ATOM 119 CD ARG A 162 0.637 24.106 26.594 1.00 24.94 C
ANISOU 119 CD ARG A 162 3182 3173 3118 50 -94 -94 C
ATOM 120 NE ARG A 162 0.900 24.245 25.162 1.00 26.82 N
ANISOU 120 NE ARG A 162 3509 3361 3322 47 -123 84 N
ATOM 121 CZ ARG A 162 0.860 25.395 24.500 1.00 28.73 C
ANISOU 121 CZ ARG A 162 3976 3394 3545 -19 -46 31 C
ATOM 122 NH1 ARG A 162 0.523 26.523 25.124 1.00 29.63 N
ANISOU 122 NH1 ARG A 162 4099 3612 3544 56 47 -104 N
ATOM 123 NH2 ARG A 162 1.130 25.422 23.204 1.00 30.78 N
ANISOU 123 NH2 ARG A 162 4184 3719 3792 -26 42 -161 N
ATOM 124 N ASP A 163 2.931 21.577 27.997 1.00 17.62 N
ANISOU 124 N ASP A 163 2272 2482 1938 75 -56 19 N
ATOM 125 CA ASP A 163 2.701 20.244 27.494 1.00 17.26 C
ANISOU 125 CA ASP A 163 2222 2361 1975 86 -66 94 C
ATOM 126 C ASP A 163 3.330 19.221 28.441 1.00 16.84 C
ANISOU 126 C ASP A 163 2138 2328 1933 4 -95 79 C
ATOM 127 O ASP A 163 2.736 18.200 28.742 1.00 17.78 O
ANISOU 127 O ASP A 163 2277 2405 2071 -71 -236 58 O
ATOM 128 CB ASP A 163 3.346 20.093 26.125 1.00 17.92 C
ANISOU 128 CB ASP A 163 2371 2535 1901 15 -124 86 C
ATOM 129 CG ASP A 163 2.495 20.611 25.000 1.00 18.26 C
ANISOU 129 CG ASP A 163 2258 2569 2108 99 -66 89 C
ATOM 130 OD1 ASP A 163 1.403 21.189 25.223 1.00 18.74 O
ANISOU 130 OD1 ASP A 163 2590 2540 1989 22 -223 64 O
ATOM 131 OD2 ASP A 163 2.964 20.387 23.859 1.00 20.72 O
ANISOU 131 OD2 ASP A 163 2936 3021 1916 111 -141 173 O
ATOM 132 N TYR A 164 4.534 19.521 28.918 1.00 15.52 N
ANISOU 132 N TYR A 164 1942 2159 1794 37 -106 119 N
ATOM 133 CA TYR A 164 5.244 18.600 29.806 1.00 14.71 C
ANISOU 133 CA TYR A 164 1800 2001 1785 4 -68 60 C
ATOM 134 C TYR A 164 4.481 18.429 31.120 1.00 14.31 C
ANISOU 134 C TYR A 164 1738 1898 1800 -17 -48 83 C
ATOM 135 O TYR A 164 4.339 17.302 31.620 1.00 14.39 O
ANISOU 135 O TYR A 164 1779 1882 1803 -184 36 56 O
ATOM 136 CB TYR A 164 6.669 19.135 30.030 1.00 15.00 C
ANISOU 136 CB TYR A 164 1838 2064 1797 -36 -41 103 C
ATOM 137 CG TYR A 164 7.382 18.651 31.281 1.00 13.54 C
ANISOU 137 CG TYR A 164 1748 1709 1687 69 31 134 C
ATOM 138 CD1 TYR A 164 7.686 17.286 31.482 1.00 14.00 C
ANISOU 138 CD1 TYR A 164 1887 1681 1750 -75 36 -27 C
ATOM 139 CD2 TYR A 164 7.788 19.573 32.253 1.00 13.78 C
ANISOU 139 CD2 TYR A 164 1747 1938 1550 -45 305 95 C
ATOM 140 CE1 TYR A 164 8.368 16.870 32.607 1.00 14.16 C
ANISOU 140 CE1 TYR A 164 1597 1898 1883 -54 19 -22 C
ATOM 141 CE2 TYR A 164 8.449 19.165 33.399 1.00 13.10 C
ANISOU 141 CE2 TYR A 164 1580 1669 1728 50 -8 66 C
ATOM 142 CZ TYR A 164 8.740 17.801 33.573 1.00 13.15 C
ANISOU 142 CZ TYR A 164 1590 1678 1725 65 97 17 C
ATOM 143 OH TYR A 164 9.437 17.374 34.688 1.00 14.80 O
ANISOU 143 OH TYR A 164 1728 1912 1982 151 15 195 O
ATOM 144 N VAL A 165 3.977 19.533 31.669 1.00 14.19 N
ANISOU 144 N VAL A 165 1773 1899 1718 -67 -15 43 N
ATOM 145 CA VAL A 165 3.220 19.441 32.929 1.00 14.53 C
ANISOU 145 CA VAL A 165 1864 1819 1835 0 77 -26 C
ATOM 146 C VAL A 165 1.999 18.531 32.740 1.00 15.33 C
ANISOU 146 C VAL A 165 1847 2058 1917 51 -37 -10 C
ATOM 147 O VAL A 165 1.718 17.671 33.589 1.00 14.83 O
ANISOU 147 O VAL A 165 1689 1992 1953 22 -62 72 O
ATOM 148 CB VAL A 165 2.808 20.805 33.470 1.00 15.31 C
ANISOU 148 CB VAL A 165 1981 1978 1855 8 62 24 C
ATOM 149 CG1 VAL A 165 1.983 20.623 34.752 1.00 16.12 C
ANISOU 149 CG1 VAL A 165 2132 1977 2014 -13 250 -83 C
ATOM 150 CG2 VAL A 165 4.051 21.619 33.759 1.00 15.63 C
ANISOU 150 CG2 VAL A 165 2217 1763 1956 -52 -79 -16 C
ATOM 151 N ASP A 166 1.316 18.690 31.604 1.00 16.99 N
ANISOU 151 N ASP A 166 2027 2278 2148 62 -113 -45 N
ATOM 152 CA ASP A 166 0.154 17.867 31.292 1.00 18.15 C
ANISOU 152 CA ASP A 166 2164 2473 2257 -3 -165 0 C
ATOM 153 C ASP A 166 0.531 16.378 31.275 1.00 17.01 C
ANISOU 153 C ASP A 166 1999 2406 2057 -29 -190 -15 C
ATOM 154 O ASP A 166 -0.140 15.559 31.895 1.00 17.12 O
ANISOU 154 O ASP A 166 1834 2456 2214 4 -138 13 O
ATOM 155 CB ASP A 166 -0.438 18.305 29.945 1.00 19.97 C
ANISOU 155 CB ASP A 166 2463 2740 2382 47 -197 66 C
ATOM 156 CG ASP A 166 -1.905 17.929 29.803 1.00 25.65 C
ANISOU 156 CG ASP A 166 3005 3205 3532 -15 -203 29 C
ATOM 157 OD1 ASP A 166 -2.245 16.749 29.978 1.00 30.05 O
ANISOU 157 OD1 ASP A 166 3580 3730 4107 -87 -75 194 O
ATOM 158 OD2 ASP A 166 -2.735 18.822 29.518 1.00 32.54 O
ANISOU 158 OD2 ASP A 166 3784 4157 4422 148 -213 136 O
ATOM 159 N ARG A 167 1.639 16.039 30.620 1.00 15.40 N
ANISOU 159 N ARG A 167 1768 2214 1867 -77 -178 -44 N
ATOM 160 CA ARG A 167 2.085 14.638 30.551 1.00 15.31 C
ANISOU 160 CA ARG A 167 1744 2180 1892 -86 -98 -33 C
ATOM 161 C ARG A 167 2.480 14.107 31.937 1.00 14.17 C
ANISOU 161 C ARG A 167 1653 1941 1788 -93 -119 19 C
ATOM 162 O ARG A 167 2.162 12.968 32.301 1.00 14.90 O
ANISOU 162 O ARG A 167 1550 2072 2038 -214 -84 -65 O
ATOM 163 CB ARG A 167 3.255 14.476 29.588 1.00 15.68 C
ANISOU 163 CB ARG A 167 1877 2278 1801 -147 -83 -19 C
ATOM 164 CG ARG A 167 2.867 14.871 28.166 1.00 15.66 C
ANISOU 164 CG ARG A 167 1992 2206 1751 -28 -13 97 C
ATOM 165 CD ARG A 167 3.874 14.354 27.179 1.00 15.83 C
ANISOU 165 CD ARG A 167 1761 2349 1903 11 -43 -64 C
ATOM 166 NE ARG A 167 5.204 14.935 27.370 1.00 16.56 N
ANISOU 166 NE ARG A 167 2080 2124 2088 -120 134 -224 N
ATOM 167 CZ ARG A 167 6.269 14.311 27.864 1.00 17.03 C
ANISOU 167 CZ ARG A 167 2479 2086 1903 0 116 -36 C
ATOM 168 NH1 ARG A 167 6.224 13.026 28.271 1.00 17.68 N
ANISOU 168 NH1 ARG A 167 2666 1950 2102 77 57 -60 N
ATOM 169 NH2 ARG A 167 7.409 14.985 27.942 1.00 17.26 N
ANISOU 169 NH2 ARG A 167 2450 2126 1982 -42 34 -155 N
ATOM 170 N PHE A 168 3.156 14.952 32.714 1.00 13.73 N
ANISOU 170 N PHE A 168 1606 1801 1808 -70 -57 -33 N
ATOM 171 CA PHE A 168 3.587 14.586 34.057 1.00 13.76 C
ANISOU 171 CA PHE A 168 1696 1799 1734 -183 33 -6 C
ATOM 172 C PHE A 168 2.338 14.290 34.903 1.00 13.28 C
ANISOU 172 C PHE A 168 1513 1745 1787 -166 9 12 C
ATOM 173 O PHE A 168 2.288 13.274 35.590 1.00 14.52 O
ANISOU 173 O PHE A 168 1580 1866 2070 -258 67 69 O
ATOM 174 CB PHE A 168 4.400 15.750 34.645 1.00 13.77 C
ANISOU 174 CB PHE A 168 1738 1839 1652 -114 -103 -75 C
ATOM 175 CG PHE A 168 4.963 15.505 36.032 1.00 12.20 C
ANISOU 175 CG PHE A 168 1526 1637 1471 35 -41 -67 C
ATOM 176 CD1 PHE A 168 6.281 15.078 36.187 1.00 14.33 C
ANISOU 176 CD1 PHE A 168 1810 1735 1900 209 -85 -48 C
ATOM 177 CD2 PHE A 168 4.196 15.730 37.167 1.00 11.42 C
ANISOU 177 CD2 PHE A 168 1599 1337 1403 -122 24 0 C
ATOM 178 CE1 PHE A 168 6.823 14.858 37.458 1.00 14.34 C
ANISOU 178 CE1 PHE A 168 1766 2035 1645 64 18 -49 C
ATOM 179 CE2 PHE A 168 4.740 15.525 38.464 1.00 12.58 C
ANISOU 179 CE2 PHE A 168 1549 1553 1675 -28 -149 41 C
ATOM 180 CZ PHE A 168 6.048 15.095 38.608 1.00 14.07 C
ANISOU 180 CZ PHE A 168 1701 1895 1748 115 81 51 C
ATOM 181 N TYR A 169 1.350 15.177 34.849 1.00 14.02 N
ANISOU 181 N TYR A 169 1564 1936 1825 -218 92 47 N
ATOM 182 CA TYR A 169 0.109 14.976 35.598 1.00 15.81 C
ANISOU 182 CA TYR A 169 1741 2133 2131 -65 55 -29 C
ATOM 183 C TYR A 169 -0.571 13.666 35.205 1.00 16.21 C
ANISOU 183 C TYR A 169 1765 2191 2203 -108 -11 20 C
ATOM 184 O TYR A 169 -0.953 12.855 36.068 1.00 16.95 O
ANISOU 184 O TYR A 169 1704 2363 2372 -96 -79 3 O
ATOM 185 CB TYR A 169 -0.815 16.138 35.337 1.00 16.38 C
ANISOU 185 CB TYR A 169 1808 2172 2242 -50 42 -41 C
ATOM 186 CG TYR A 169 -2.217 15.953 35.877 1.00 18.26 C
ANISOU 186 CG TYR A 169 1900 2528 2509 -26 62 -71 C
ATOM 187 CD1 TYR A 169 -2.452 15.830 37.249 1.00 17.65 C
ANISOU 187 CD1 TYR A 169 1890 2417 2399 -56 74 -151 C
ATOM 188 CD2 TYR A 169 -3.304 15.916 35.015 1.00 19.79 C
ANISOU 188 CD2 TYR A 169 2200 2710 2606 -23 1 -95 C
ATOM 189 CE1 TYR A 169 -3.750 15.709 37.756 1.00 21.78 C
ANISOU 189 CE1 TYR A 169 2387 3112 2777 -90 126 -96 C
ATOM 190 CE2 TYR A 169 -4.598 15.770 35.509 1.00 20.84 C
ANISOU 190 CE2 TYR A 169 2175 2897 2846 -102 21 -16 C
ATOM 191 CZ TYR A 169 -4.809 15.671 36.876 1.00 20.27 C
ANISOU 191 CZ TYR A 169 1938 2876 2886 -45 202 -48 C
ATOM 192 OH TYR A 169 -6.099 15.531 37.358 1.00 23.10 O
ANISOU 192 OH TYR A 169 1901 3348 3525 -154 215 -202 O
ATOM 193 N LYS A 170 -0.694 13.435 33.900 1.00 17.06 N
ANISOU 193 N LYS A 170 1973 2260 2246 -127 -59 10 N
ATOM 194 CA LYS A 170 -1.398 12.228 33.438 1.00 19.03 C
ANISOU 194 CA LYS A 170 2276 2493 2461 -140 9 -46 C
ATOM 195 C LYS A 170 -0.721 10.959 33.940 1.00 18.15 C
ANISOU 195 C LYS A 170 2114 2410 2372 -147 30 -19 C
ATOM 196 O LYS A 170 -1.392 10.018 34.384 1.00 19.83 O
ANISOU 196 O LYS A 170 2251 2490 2793 -195 9 12 O
ATOM 197 CB LYS A 170 -1.604 12.239 31.916 1.00 19.32 C
ANISOU 197 CB LYS A 170 2354 2554 2429 -162 -42 -20 C
ATOM 198 CG LYS A 170 -2.519 13.378 31.476 1.00 21.88 C
ANISOU 198 CG LYS A 170 2663 2925 2724 -33 -57 -17 C
ATOM 199 CD LYS A 170 -2.616 13.561 29.951 1.00 23.04 C
ANISOU 199 CD LYS A 170 2878 3021 2855 -57 -46 36 C
ATOM 200 CE LYS A 170 -4.032 14.028 29.557 1.00 29.95 C
ANISOU 200 CE LYS A 170 3700 3895 3785 66 -162 -41 C
ATOM 201 NZ LYS A 170 -4.430 15.363 30.124 1.00 31.28 N
ANISOU 201 NZ LYS A 170 4143 3680 4062 133 -39 -110 N
ATOM 202 N THR A 171 0.613 10.940 33.908 1.00 17.27 N
ANISOU 202 N THR A 171 2015 2275 2269 -98 -91 -22 N
ATOM 203 CA THR A 171 1.349 9.772 34.362 1.00 17.40 C
ANISOU 203 CA THR A 171 2017 2346 2248 -80 -22 -102 C
ATOM 204 C THR A 171 1.246 9.633 35.880 1.00 17.03 C
ANISOU 204 C THR A 171 1963 2256 2250 -84 25 -8 C
ATOM 205 O THR A 171 1.141 8.515 36.419 1.00 16.38 O
ANISOU 205 O THR A 171 1793 2052 2375 -220 98 -171 O
ATOM 206 CB THR A 171 2.826 9.887 33.908 1.00 17.38 C
ANISOU 206 CB THR A 171 1975 2433 2195 -69 -53 -60 C
ATOM 207 OG1 THR A 171 2.874 9.913 32.475 1.00 21.80 O
ANISOU 207 OG1 THR A 171 2578 3207 2495 78 148 18 O
ATOM 208 CG2 THR A 171 3.628 8.696 34.375 1.00 17.48 C
ANISOU 208 CG2 THR A 171 2222 2095 2324 -19 71 -80 C
ATOM 209 N LEU A 172 1.303 10.764 36.585 1.00 16.13 N
ANISOU 209 N LEU A 172 1910 2154 2063 -188 -27 13 N
ATOM 210 CA LEU A 172 1.350 10.697 38.050 1.00 16.08 C
ANISOU 210 CA LEU A 172 1900 2157 2053 -201 58 9 C
ATOM 211 C LEU A 172 0.002 10.225 38.588 1.00 16.79 C
ANISOU 211 C LEU A 172 1948 2219 2213 -209 32 43 C
ATOM 212 O LEU A 172 -0.059 9.508 39.596 1.00 16.83 O
ANISOU 212 O LEU A 172 1828 2257 2309 -312 25 71 O
ATOM 213 CB LEU A 172 1.750 12.039 38.663 1.00 15.88 C
ANISOU 213 CB LEU A 172 2050 2122 1862 -233 -32 2 C
ATOM 214 CG LEU A 172 1.948 12.060 40.181 1.00 15.65 C
ANISOU 214 CG LEU A 172 2017 2032 1895 -251 68 24 C
ATOM 215 CD1 LEU A 172 2.791 10.888 40.623 1.00 17.18 C
ANISOU 215 CD1 LEU A 172 2281 2135 2110 -115 114 144 C
ATOM 216 CD2 LEU A 172 2.583 13.382 40.593 1.00 16.30 C
ANISOU 216 CD2 LEU A 172 2190 1888 2112 -214 -99 -37 C
ATOM 217 N ARG A 173 -1.066 10.591 37.890 1.00 17.92 N
ANISOU 217 N ARG A 173 2044 2374 2390 -173 36 56 N
ATOM 218 CA ARG A 173 -2.406 10.130 38.292 1.00 20.05 C
ANISOU 218 CA ARG A 173 2270 2656 2688 -146 -15 54 C
ATOM 219 C ARG A 173 -2.472 8.608 38.344 1.00 19.84 C
ANISOU 219 C ARG A 173 2249 2641 2646 -137 -54 55 C
ATOM 220 O ARG A 173 -3.105 8.034 39.243 1.00 21.07 O
ANISOU 220 O ARG A 173 2516 2740 2747 -194 -42 99 O
ATOM 221 CB ARG A 173 -3.463 10.623 37.314 1.00 21.02 C
ANISOU 221 CB ARG A 173 2385 2816 2782 -77 -35 52 C
ATOM 222 CG ARG A 173 -3.863 12.064 37.493 1.00 25.71 C
ANISOU 222 CG ARG A 173 3216 3148 3405 4 12 70 C
ATOM 223 CD ARG A 173 -5.207 12.320 36.776 1.00 30.67 C
ANISOU 223 CD ARG A 173 3598 4027 4028 -16 -184 69 C
ATOM 224 NE ARG A 173 -5.222 11.751 35.424 1.00 36.09 N
ANISOU 224 NE ARG A 173 4484 4624 4605 -10 6 -65 N
ATOM 225 CZ ARG A 173 -5.990 12.175 34.421 1.00 35.95 C
ANISOU 225 CZ ARG A 173 4514 4581 4563 117 -142 -9 C
ATOM 226 NH1 ARG A 173 -6.828 13.201 34.589 1.00 39.07 N
ANISOU 226 NH1 ARG A 173 4852 4980 5010 -104 -88 -94 N
ATOM 227 NH2 ARG A 173 -5.909 11.576 33.236 1.00 37.80 N
ANISOU 227 NH2 ARG A 173 4737 4783 4839 50 -69 32 N
ATOM 228 N ALA A 174 -1.828 7.970 37.369 1.00 19.57 N
ANISOU 228 N ALA A 174 2207 2554 2673 -177 -158 -11 N
ATOM 229 CA ALA A 174 -1.819 6.508 37.234 1.00 19.46 C
ANISOU 229 CA ALA A 174 2252 2459 2682 -117 -113 17 C
ATOM 230 C ALA A 174 -0.781 5.772 38.116 1.00 19.84 C
ANISOU 230 C ALA A 174 2399 2426 2710 -139 -183 0 C
ATOM 231 O ALA A 174 -0.896 4.565 38.359 1.00 20.20 O
ANISOU 231 O ALA A 174 2419 2402 2851 -206 -306 17 O
ATOM 232 CB ALA A 174 -1.655 6.143 35.777 1.00 19.41 C
ANISOU 232 CB ALA A 174 2289 2456 2629 -168 -242 2 C
ATOM 233 N GLU A 175 0.215 6.503 38.611 1.00 18.90 N
ANISOU 233 N GLU A 175 2241 2343 2593 -178 -111 55 N
ATOM 234 CA GLU A 175 1.285 5.951 39.432 1.00 19.39 C
ANISOU 234 CA GLU A 175 2385 2369 2611 -173 -78 -14 C
ATOM 235 C GLU A 175 0.714 5.342 40.709 1.00 19.76 C
ANISOU 235 C GLU A 175 2404 2449 2652 -131 -55 -1 C
ATOM 236 O GLU A 175 -0.141 5.948 41.344 1.00 20.41 O
ANISOU 236 O GLU A 175 2659 2338 2758 -119 3 86 O
ATOM 237 CB GLU A 175 2.247 7.111 39.776 1.00 18.62 C
ANISOU 237 CB GLU A 175 2168 2207 2700 -205 -107 65 C
ATOM 238 CG GLU A 175 3.549 6.720 40.487 1.00 18.92 C
ANISOU 238 CG GLU A 175 2168 2542 2477 -196 20 70 C
ATOM 239 CD GLU A 175 4.505 5.944 39.608 1.00 18.66 C
ANISOU 239 CD GLU A 175 2211 2441 2436 -169 12 7 C
ATOM 240 OE1 GLU A 175 4.558 6.194 38.381 1.00 20.39 O
ANISOU 240 OE1 GLU A 175 2400 2778 2568 -75 122 85 O
ATOM 241 OE2 GLU A 175 5.211 5.077 40.149 1.00 20.78 O
ANISOU 241 OE2 GLU A 175 2304 2961 2628 8 127 126 O
ATOM 242 N GLN A 176 1.179 4.154 41.087 1.00 20.83 N
ANISOU 242 N GLN A 176 2593 2627 2692 -162 -22 82 N
ATOM 243 CA AGLN A 176 0.736 3.515 42.324 0.50 22.57 C
ANISOU 243 CA AGLN A 176 2831 2869 2875 -77 -46 47 C
ATOM 244 CA BGLN A 176 0.720 3.531 42.322 0.50 22.32 C
ANISOU 244 CA BGLN A 176 2807 2826 2846 -92 -38 47 C
ATOM 245 C GLN A 176 1.652 3.927 43.474 1.00 22.30 C
ANISOU 245 C GLN A 176 2802 2861 2809 -80 -25 68 C
ATOM 246 O GLN A 176 2.691 3.325 43.690 1.00 23.37 O
ANISOU 246 O GLN A 176 2909 2998 2969 -28 -2 5 O
ATOM 247 CB AGLN A 176 0.694 1.991 42.164 0.50 22.44 C
ANISOU 247 CB AGLN A 176 2855 2833 2838 -74 -31 5 C
ATOM 248 CB BGLN A 176 0.583 2.009 42.155 0.50 22.71 C
ANISOU 248 CB BGLN A 176 2889 2852 2887 -77 -21 6 C
ATOM 249 CG AGLN A 176 -0.393 1.493 41.227 0.50 24.25 C
ANISOU 249 CG AGLN A 176 2971 3159 3083 -72 -60 37 C
ATOM 250 CG BGLN A 176 -0.322 1.565 40.985 0.50 25.45 C
ANISOU 250 CG BGLN A 176 3204 3256 3209 -111 -63 32 C
ATOM 251 CD AGLN A 176 -0.494 -0.018 41.200 0.50 23.31 C
ANISOU 251 CD AGLN A 176 2961 2974 2921 -61 7 -3 C
ATOM 252 CD BGLN A 176 -1.760 2.077 41.090 0.50 25.70 C
ANISOU 252 CD BGLN A 176 3242 3399 3124 74 42 41 C
ATOM 253 OE1AGLN A 176 -1.122 -0.630 42.072 0.50 25.86 O
ANISOU 253 OE1AGLN A 176 3124 3330 3369 -43 -27 16 O
ATOM 254 OE1BGLN A 176 -2.443 1.866 42.092 0.50 28.57 O
ANISOU 254 OE1BGLN A 176 3605 3573 3677 74 -116 70 O
ATOM 255 NE2AGLN A 176 0.113 -0.633 40.186 0.50 25.45 N
ANISOU 255 NE2AGLN A 176 3130 3283 3255 -68 -58 -43 N
ATOM 256 NE2BGLN A 176 -2.222 2.748 40.044 0.50 29.22 N
ANISOU 256 NE2BGLN A 176 3692 3715 3694 -93 30 -8 N
ATOM 257 N ALA A 177 1.259 4.982 44.177 1.00 22.46 N
ANISOU 257 N ALA A 177 2803 2896 2832 -110 -52 45 N
ATOM 258 CA ALA A 177 1.972 5.540 45.325 1.00 22.44 C
ANISOU 258 CA ALA A 177 2804 2925 2798 -141 19 70 C
ATOM 259 C ALA A 177 0.964 6.255 46.219 1.00 22.54 C
ANISOU 259 C ALA A 177 2749 2945 2868 -119 -3 86 C
ATOM 260 O ALA A 177 -0.150 6.548 45.787 1.00 21.97 O
ANISOU 260 O ALA A 177 2634 2927 2786 -145 0 178 O
ATOM 261 CB ALA A 177 3.040 6.516 44.866 1.00 22.73 C
ANISOU 261 CB ALA A 177 2792 2968 2874 -201 11 97 C
ATOM 262 N SER A 178 1.364 6.524 47.466 1.00 22.11 N
ANISOU 262 N SER A 178 2689 2945 2767 -115 -23 61 N
ATOM 263 CA SER A 178 0.526 7.222 48.422 1.00 22.39 C
ANISOU 263 CA SER A 178 2676 2997 2833 -108 87 110 C
ATOM 264 C SER A 178 0.336 8.667 47.965 1.00 22.87 C
ANISOU 264 C SER A 178 2734 3013 2941 -34 104 80 C
ATOM 265 O SER A 178 1.182 9.207 47.248 1.00 21.46 O
ANISOU 265 O SER A 178 2428 3006 2718 -2 311 174 O
ATOM 266 CB SER A 178 1.149 7.199 49.821 1.00 21.99 C
ANISOU 266 CB SER A 178 2635 2902 2816 -173 46 47 C
ATOM 267 OG SER A 178 2.312 8.034 49.919 1.00 21.13 O
ANISOU 267 OG SER A 178 2503 3130 2395 -329 223 233 O
ATOM 268 N GLN A 179 -0.771 9.290 48.364 1.00 23.24 N
ANISOU 268 N GLN A 179 2725 3133 2971 49 203 52 N
ATOM 269 CA GLN A 179 -0.973 10.722 48.103 1.00 24.92 C
ANISOU 269 CA GLN A 179 2941 3322 3204 24 165 45 C
ATOM 270 C GLN A 179 0.204 11.584 48.553 1.00 22.21 C
ANISOU 270 C GLN A 179 2581 3033 2825 159 213 32 C
ATOM 271 O GLN A 179 0.646 12.474 47.814 1.00 21.41 O
ANISOU 271 O GLN A 179 2233 3048 2851 163 215 100 O
ATOM 272 CB GLN A 179 -2.269 11.249 48.757 1.00 24.22 C
ANISOU 272 CB GLN A 179 2763 3307 3132 99 270 47 C
ATOM 273 CG GLN A 179 -2.637 12.670 48.286 1.00 28.07 C
ANISOU 273 CG GLN A 179 3320 3552 3794 -37 159 82 C
ATOM 274 CD GLN A 179 -3.579 13.458 49.234 1.00 26.28 C
ANISOU 274 CD GLN A 179 3310 3246 3430 356 252 0 C
ATOM 275 OE1 GLN A 179 -4.143 14.489 48.843 1.00 35.50 O
ANISOU 275 OE1 GLN A 179 4450 4332 4704 1 43 4 O
ATOM 276 NE2 GLN A 179 -3.747 12.977 50.464 1.00 32.84 N
ANISOU 276 NE2 GLN A 179 4178 4235 4064 -91 74 -67 N
ATOM 277 N GLU A 180 0.705 11.298 49.721 1.00 21.38 N
ANISOU 277 N GLU A 180 2480 3005 2636 157 278 -48 N
ATOM 278 CA GLU A 180 1.801 11.985 50.291 1.00 21.19 C
ANISOU 278 CA GLU A 180 2552 2953 2543 141 245 -36 C
ATOM 279 C GLU A 180 3.043 11.885 49.381 1.00 19.79 C
ANISOU 279 C GLU A 180 2338 2725 2456 137 147 -21 C
ATOM 280 O GLU A 180 3.708 12.814 49.108 1.00 19.60 O
ANISOU 280 O GLU A 180 2390 2669 2387 213 195 22 O
ATOM 281 CB GLU A 180 2.053 11.301 51.615 1.00 22.95 C
ANISOU 281 CB GLU A 180 2890 3103 2725 193 195 -15 C
ATOM 282 CG GLU A 180 3.057 11.881 52.444 1.00 27.68 C
ANISOU 282 CG GLU A 180 3343 3453 3718 126 179 -57 C
ATOM 283 CD GLU A 180 3.224 11.146 53.798 1.00 23.04 C
ANISOU 283 CD GLU A 180 2559 3252 2941 -990 39 37 C
ATOM 284 OE1 GLU A 180 2.520 10.217 54.085 1.00 33.47 O
ANISOU 284 OE1 GLU A 180 4323 4382 4012 648 402 83 O
ATOM 285 OE2 GLU A 180 4.083 11.533 54.550 1.00 39.40 O
ANISOU 285 OE2 GLU A 180 5255 5039 4676 483 -296 -184 O
ATOM 286 N VAL A 181 3.290 10.692 48.932 1.00 18.23 N
ANISOU 286 N VAL A 181 2181 2508 2236 124 125 72 N
ATOM 287 CA VAL A 181 4.377 10.441 47.978 1.00 17.52 C
ANISOU 287 CA VAL A 181 2154 2322 2179 140 123 61 C
ATOM 288 C VAL A 181 4.144 11.157 46.638 1.00 16.65 C
ANISOU 288 C VAL A 181 1974 2260 2090 120 27 59 C
ATOM 289 O VAL A 181 5.084 11.710 46.058 1.00 15.81 O
ANISOU 289 O VAL A 181 1716 2269 2021 292 56 102 O
ATOM 290 CB VAL A 181 4.704 8.936 47.816 1.00 17.52 C
ANISOU 290 CB VAL A 181 2199 2251 2206 127 98 73 C
ATOM 291 CG1 VAL A 181 5.539 8.671 46.585 1.00 18.96 C
ANISOU 291 CG1 VAL A 181 2368 2447 2387 47 150 37 C
ATOM 292 CG2 VAL A 181 5.415 8.423 49.051 1.00 18.41 C
ANISOU 292 CG2 VAL A 181 2356 2499 2138 -12 -91 -54 C
ATOM 293 N LYS A 182 2.900 11.173 46.154 1.00 16.20 N
ANISOU 293 N LYS A 182 1964 2228 1962 102 90 99 N
ATOM 294 CA LYS A 182 2.640 11.868 44.901 1.00 15.78 C
ANISOU 294 CA LYS A 182 1841 2160 1991 108 5 100 C
ATOM 295 C LYS A 182 2.921 13.349 45.056 1.00 15.15 C
ANISOU 295 C LYS A 182 1757 2115 1882 71 25 90 C
ATOM 296 O LYS A 182 3.379 13.989 44.107 1.00 14.96 O
ANISOU 296 O LYS A 182 1587 2149 1945 30 88 202 O
ATOM 297 CB LYS A 182 1.208 11.640 44.404 1.00 16.53 C
ANISOU 297 CB LYS A 182 1888 2328 2064 -85 93 65 C
ATOM 298 CG LYS A 182 0.970 10.204 43.972 1.00 16.67 C
ANISOU 298 CG LYS A 182 2004 2225 2105 -130 3 69 C
ATOM 299 CD LYS A 182 -0.286 10.044 43.125 1.00 18.58 C
ANISOU 299 CD LYS A 182 2218 2562 2278 -78 -23 63 C
ATOM 300 CE LYS A 182 -0.493 8.580 42.830 1.00 19.61 C
ANISOU 300 CE LYS A 182 2123 2727 2599 -214 12 39 C
ATOM 301 NZ LYS A 182 -1.626 8.308 41.889 1.00 21.14 N
ANISOU 301 NZ LYS A 182 2335 3128 2568 -64 -199 233 N
ATOM 302 N ASN A 183 2.622 13.902 46.237 1.00 14.84 N
ANISOU 302 N ASN A 183 1716 2037 1882 118 76 45 N
ATOM 303 CA ASN A 183 2.934 15.312 46.512 1.00 15.50 C
ANISOU 303 CA ASN A 183 1713 2189 1985 105 86 -5 C
ATOM 304 C ASN A 183 4.437 15.584 46.460 1.00 16.06 C
ANISOU 304 C ASN A 183 1815 2226 2058 43 -28 18 C
ATOM 305 O ASN A 183 4.908 16.568 45.876 1.00 16.46 O
ANISOU 305 O ASN A 183 1744 2402 2107 164 80 148 O
ATOM 306 CB ASN A 183 2.325 15.744 47.851 1.00 15.83 C