HEADER IMMUNE SYSTEM 08-NOV-13 3WLB
TITLE HLA-A24 IN COMPLEX WITH HIV-1 NEF126-10(8T10F)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-24 ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 25-298;
COMPND 5 SYNONYM: AW-24, HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-9 ALPHA
COMPND 6 CHAIN, MHC CLASS I ANTIGEN A*24;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 21-119;
COMPND 12 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: PROTEIN NEF;
COMPND 16 CHAIN: C;
COMPND 17 FRAGMENT: UNP RESIDUES 126-135;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21D(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: B2M, CDABP0092, HDCMA22P;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET21A(+);
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 24 ORGANISM_TAXID: 11676;
SOURCE 25 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS HIV-1, NEF, HLA-A24, MHC CLASS I, IMMUNOGLOBURIN DOMAIN, IMMUNE
KEYWDS 2 RESPONSE, IMMUNE SYSTEM, TCR, T CELL RECEPTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SHIMIZU,S.FUKAI,A.YAMAGATA,A.IWAMOTO,C.HAN
REVDAT 4 20-NOV-24 3WLB 1 REMARK
REVDAT 3 08-NOV-23 3WLB 1 SEQADV SSBOND
REVDAT 2 22-NOV-17 3WLB 1 REMARK
REVDAT 1 11-JUN-14 3WLB 0
JRNL AUTH C.HAN,A.KAWANA-TACHIKAWA,A.SHIMIZU,D.ZHU,H.NAKAMURA,
JRNL AUTH 2 E.ADACHI,T.KIKUCHI,M.KOGA,T.KOIBUCHI,G.F.GAO,Y.SATO,
JRNL AUTH 3 A.YAMAGATA,E.MARTIN,S.FUKAI,Z.L.BRUMME,A.IWAMOTO
JRNL TITL SWITCHING AND EMERGENCE OF CTL EPITOPES IN HIV-1 INFECTION
JRNL REF RETROVIROLOGY V. 11 38 2014
JRNL REFN ESSN 1742-4690
JRNL PMID 24886641
JRNL DOI 10.1186/1742-4690-11-38
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 29606
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1559
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1990
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.1750
REMARK 3 BIN FREE R VALUE SET COUNT : 107
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3138
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.84000
REMARK 3 B22 (A**2) : -0.18000
REMARK 3 B33 (A**2) : -0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.112
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.884
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3227 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4376 ; 1.205 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 381 ; 5.931 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;32.187 ;23.276
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 528 ;16.259 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;21.693 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 442 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2553 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 3227 ; 5.284 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 78 ;19.616 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3339 ; 8.536 ; 5.000
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 274
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6735 6.2760 4.4118
REMARK 3 T TENSOR
REMARK 3 T11: 0.0054 T22: 0.0169
REMARK 3 T33: 0.0082 T12: 0.0015
REMARK 3 T13: 0.0027 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0920 L22: 0.2045
REMARK 3 L33: 0.0879 L12: 0.1326
REMARK 3 L13: 0.0274 L23: 0.0077
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.0108 S13: 0.0054
REMARK 3 S21: 0.0124 S22: -0.0177 S23: 0.0046
REMARK 3 S31: 0.0172 S32: -0.0054 S33: 0.0055
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 0 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3934 17.6538 -10.7264
REMARK 3 T TENSOR
REMARK 3 T11: 0.0141 T22: 0.0217
REMARK 3 T33: 0.0035 T12: -0.0142
REMARK 3 T13: 0.0032 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.2823 L22: 0.3912
REMARK 3 L33: 0.3570 L12: 0.2358
REMARK 3 L13: -0.0277 L23: 0.0056
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: 0.0055 S13: 0.0058
REMARK 3 S21: -0.0204 S22: 0.0366 S23: 0.0259
REMARK 3 S31: -0.0354 S32: 0.0500 S33: -0.0110
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3WLB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000096478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31585
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3I6L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG3350, 200 MM SODIUM
REMARK 280 PHOSPHATE DIBASIC, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 33.54200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.54850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.86250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.54850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 33.54200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.86250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 CYS B 80 CA - CB - SG ANGL. DEV. = 8.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 29 -122.49 46.68
REMARK 500 HIS A 114 98.84 -166.72
REMARK 500 ASP A 227 24.83 81.14
REMARK 500 LYS B 48 51.40 -94.51
REMARK 500 TRP B 60 -1.88 77.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WL9 RELATED DB: PDB
DBREF 3WLB A 1 274 UNP P05534 1A24_HUMAN 25 298
DBREF 3WLB B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3WLB C 1 10 UNP Q9WPV9 Q9WPV9_9HIV1 126 135
SEQADV 3WLB MET A 0 UNP P05534 EXPRESSION TAG
SEQADV 3WLB MET B 0 UNP P61769 EXPRESSION TAG
SEQRES 1 A 275 MET GLY SER HIS SER MET ARG TYR PHE SER THR SER VAL
SEQRES 2 A 275 SER ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL
SEQRES 3 A 275 GLY TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER
SEQRES 4 A 275 ASP ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP
SEQRES 5 A 275 ILE GLU GLN GLU GLY PRO GLU TYR TRP ASP GLU GLU THR
SEQRES 6 A 275 GLY LYS VAL LYS ALA HIS SER GLN THR ASP ARG GLU ASN
SEQRES 7 A 275 LEU ARG ILE ALA LEU ARG TYR TYR ASN GLN SER GLU ALA
SEQRES 8 A 275 GLY SER HIS THR LEU GLN MET MET PHE GLY CYS ASP VAL
SEQRES 9 A 275 GLY SER ASP GLY ARG PHE LEU ARG GLY TYR HIS GLN TYR
SEQRES 10 A 275 ALA TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP
SEQRES 11 A 275 LEU ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN ILE
SEQRES 12 A 275 THR LYS ARG LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN
SEQRES 13 A 275 GLN ARG ALA TYR LEU GLU GLY THR CYS VAL ASP GLY LEU
SEQRES 14 A 275 ARG ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG
SEQRES 15 A 275 THR ASP PRO PRO LYS THR HIS MET THR HIS HIS PRO ILE
SEQRES 16 A 275 SER ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU GLY
SEQRES 17 A 275 PHE TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP
SEQRES 18 A 275 GLY GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR
SEQRES 19 A 275 ARG PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA
SEQRES 20 A 275 VAL VAL VAL PRO SER GLY GLU GLU GLN ARG TYR THR CYS
SEQRES 21 A 275 HIS VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU
SEQRES 22 A 275 ARG TRP
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 10 ASN TYR THR PRO GLY PRO GLY THR ARG PHE
FORMUL 4 HOH *279(H2 O)
HELIX 1 1 ALA A 49 GLU A 53 5 5
HELIX 2 2 GLY A 56 ASN A 86 1 31
HELIX 3 3 ASP A 137 ALA A 150 1 14
HELIX 4 4 HIS A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLY A 175 GLN A 180 1 6
HELIX 7 7 GLU A 253 GLN A 255 5 3
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N GLY A 26 O PHE A 33
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N THR A 10 O ILE A 23
SHEET 5 A 8 THR A 94 VAL A 103 -1 O LEU A 95 N SER A 11
SHEET 6 A 8 PHE A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O ILE A 124 N TYR A 116
SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 B 4 LYS A 186 PRO A 193 0
SHEET 2 B 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O VAL A 249 N ALA A 199
SHEET 4 B 4 THR A 228 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 C 4 LYS A 186 PRO A 193 0
SHEET 2 C 4 GLU A 198 PHE A 208 -1 O TRP A 204 N HIS A 188
SHEET 3 C 4 PHE A 241 PRO A 250 -1 O VAL A 249 N ALA A 199
SHEET 4 C 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 D 4 GLU A 222 GLN A 224 0
SHEET 2 D 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222
SHEET 3 D 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216
SHEET 4 D 4 LEU A 270 ARG A 273 -1 O LEU A 272 N CYS A 259
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O THR B 68 N LEU B 23
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 ILE B 35 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 HIS B 84 -1 O ALA B 79 N LEU B 40
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.08
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.13
CISPEP 1 TYR A 209 PRO A 210 0 -0.68
CISPEP 2 HIS B 31 PRO B 32 0 0.84
CISPEP 3 GLY C 5 PRO C 6 0 -0.78
CRYST1 67.084 77.725 87.097 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014907 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011481 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
