HEADER IMMUNE SYSTEM 21-SEP-10 3OX8
TITLE CRYSTAL STRUCTURE OF HLA A*02:03 BOUND TO HBV CORE 18-27
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MHC CLASS I ANTIGEN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: UNP RESIDUES 25-299;
COMPND 5 SYNONYM: CLASS I HISTOCOMPATIBILITY ANTIGEN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, E;
COMPND 10 SYNONYM: BETA-2-MICROGLOBULIN FORM PI 5.3;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: 10MER PEPTIDE FROM PRE-CORE-PROTEIN;
COMPND 14 CHAIN: C, F;
COMPND 15 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, MHC HLA-A*02:03;
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: PET30A;
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, BETA 2-MICROGLOBULIN, 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: PET30A;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 ORGANISM_SCIENTIFIC: HEPATITIS B VIRUS;
SOURCE 24 ORGANISM_COMMON: HBV;
SOURCE 25 ORGANISM_TAXID: 10407;
SOURCE 26 OTHER_DETAILS: HEPATITIS B VIRUS CORE 18-27 IS SYNTHESIZED.
KEYWDS PROTEIN-PEPTIDE COMPLEX, HOST-VIRUS INTERACTION, IMMUNOGENICITY,
KEYWDS 2 THERAPEUTIC DESIGN, TCR RECOGNITION, HELIX, BETA-SHEET, ANTIGEN
KEYWDS 3 PRESENTATION, PEPTIDE BINDING, CELL SURFACE, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LIU,Y.CHEN,L.LAI,E.REN
REVDAT 2 06-JUL-11 3OX8 1 JRNL
REVDAT 1 04-MAY-11 3OX8 0
JRNL AUTH J.LIU,K.Y.CHEN,E.C.REN
JRNL TITL STRUCTURAL INSIGHTS INTO THE BINDING OF HEPATITIS B VIRUS
JRNL TITL 2 CORE PEPTIDE TO HLA-A2 ALLELES: TOWARDS DESIGNING BETTER
JRNL TITL 3 VACCINES.
JRNL REF EUR.J.IMMUNOL. V. 41 2097 2011
JRNL REFN ISSN 0014-2980
JRNL PMID 21538979
JRNL DOI 10.1002/EJI.201041370
REMARK 2
REMARK 2 RESOLUTION. 2.16 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 64.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 50693
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2733
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) : 2.16
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.22
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3171
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 179
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 450
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.06
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.06000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : -0.02000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.218
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.614
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6566 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8916 ; 1.313 ; 1.920
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 768 ; 7.824 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 358 ;35.764 ;23.073
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1060 ;19.434 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;22.504 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 896 ; 0.125 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5202 ; 0.017 ; 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): 3846 ; 1.620 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6208 ; 2.762 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2720 ; 4.462 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2706 ; 6.669 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OX8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER PLATINUM 135
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM PLUS
REMARK 200 DATA SCALING SOFTWARE : PROTEUM PLUS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68748
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 64.120
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.71
REMARK 200 R MERGE FOR SHELL (I) : 0.34490
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPSE PH7.5, 1.4M SODIUM CITRATE
REMARK 280 TRIBASIC DIHYDRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG D 219 O HOH A 319 1645 0.97
REMARK 500 CD PRO A 250 CE MET D 138 1456 2.16
REMARK 500 CE MET A 138 CD PRO D 250 1465 2.17
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 ARG A 17 134.70 -176.67
REMARK 500 ASP A 29 -124.54 51.46
REMARK 500 ASP A 122 136.02 -35.77
REMARK 500 TYR A 123 -71.28 -122.79
REMARK 500 ALA A 193 77.62 -57.71
REMARK 500 LYS B 48 51.51 -102.33
REMARK 500 TRP B 60 -2.71 76.86
REMARK 500 SER C 4 -179.73 -62.29
REMARK 500 ARG D 17 133.83 -172.04
REMARK 500 ASP D 29 -121.13 49.51
REMARK 500 TYR D 123 -66.26 -121.64
REMARK 500 ALA D 193 81.56 -57.83
REMARK 500 LYS E 48 55.23 -97.33
REMARK 500 TRP E 60 -5.35 78.62
REMARK 500 SER F 4 -175.33 -66.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG D 111 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 672 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH D 533 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH E 767 DISTANCE = 6.73 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3OXR RELATED DB: PDB
REMARK 900 ANOTHER HLA-A2 ALLELE BOUND TO THE SAME PEPTIDE
REMARK 900 RELATED ID: 3OXS RELATED DB: PDB
REMARK 900 ANOTHER HLA-A2 ALLELE BOUND TO THE SAME PEPTIDE
DBREF 3OX8 A 1 275 UNP Q2LC95 Q2LC95_HUMAN 25 299
DBREF 3OX8 B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3OX8 C 1 10 UNP Q9YJW5 Q9YJW5_HBV 47 56
DBREF 3OX8 D 1 275 UNP Q2LC95 Q2LC95_HUMAN 25 299
DBREF 3OX8 E 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 3OX8 F 1 10 UNP Q9YJW5 Q9YJW5_HBV 47 56
SEQADV 3OX8 MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 3OX8 MET E 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 275 LYS HIS LYS TRP GLU THR ALA HIS GLU ALA GLU GLN TRP
SEQRES 13 A 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 275 TRP GLU
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 PHE LEU PRO SER ASP PHE PHE PRO SER VAL
SEQRES 1 D 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 D 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 D 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 D 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 D 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 D 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 D 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 D 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 D 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 D 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 D 275 LYS HIS LYS TRP GLU THR ALA HIS GLU ALA GLU GLN TRP
SEQRES 13 D 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 D 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 D 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 D 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 D 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 D 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 D 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 D 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 D 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 D 275 TRP GLU
SEQRES 1 E 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 E 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 E 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 E 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 E 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 E 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 E 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 E 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 F 10 PHE LEU PRO SER ASP PHE PHE PRO SER VAL
FORMUL 7 HOH *450(H2 O)
HELIX 1 1 ALA A 49 GLU A 55 5 7
HELIX 2 2 GLY A 56 TYR A 85 1 30
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 GLN A 253 GLN A 255 5 3
HELIX 8 8 TRP D 51 GLU D 55 5 5
HELIX 9 9 GLY D 56 TYR D 85 1 30
HELIX 10 10 ASP D 137 ALA D 150 1 14
HELIX 11 11 HIS D 151 GLY D 162 1 12
HELIX 12 12 GLY D 162 GLY D 175 1 14
HELIX 13 13 GLY D 175 GLN D 180 1 6
HELIX 14 14 GLN D 253 GLN D 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 VAL A 28 O THR A 31
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 ARG A 97 N PHE A 9
SHEET 6 A 8 PHE A 109 TYR A 118 -1 O ARG A 111 N ASP A 102
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O TYR A 123 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 HIS A 192 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 ALA A 245 N CYS A 203
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 HIS A 192 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 ALA A 245 N CYS A 203
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 ASP A 223 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 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 H 8 GLU D 46 PRO D 47 0
SHEET 2 H 8 THR D 31 ASP D 37 -1 N ARG D 35 O GLU D 46
SHEET 3 H 8 ARG D 21 VAL D 28 -1 N VAL D 28 O THR D 31
SHEET 4 H 8 HIS D 3 VAL D 12 -1 N THR D 10 O ILE D 23
SHEET 5 H 8 THR D 94 VAL D 103 -1 O ARG D 97 N PHE D 9
SHEET 6 H 8 PHE D 109 TYR D 118 -1 O ARG D 111 N ASP D 102
SHEET 7 H 8 LYS D 121 LEU D 126 -1 O ILE D 124 N TYR D 116
SHEET 8 H 8 TRP D 133 ALA D 135 -1 O THR D 134 N ALA D 125
SHEET 1 I 4 LYS D 186 HIS D 192 0
SHEET 2 I 4 GLU D 198 PHE D 208 -1 O TRP D 204 N HIS D 188
SHEET 3 I 4 PHE D 241 PRO D 250 -1 O ALA D 245 N CYS D 203
SHEET 4 I 4 THR D 228 LEU D 230 -1 N GLU D 229 O ALA D 246
SHEET 1 J 4 LYS D 186 HIS D 192 0
SHEET 2 J 4 GLU D 198 PHE D 208 -1 O TRP D 204 N HIS D 188
SHEET 3 J 4 PHE D 241 PRO D 250 -1 O ALA D 245 N CYS D 203
SHEET 4 J 4 ARG D 234 PRO D 235 -1 N ARG D 234 O GLN D 242
SHEET 1 K 4 GLU D 222 GLN D 224 0
SHEET 2 K 4 THR D 214 ARG D 219 -1 N ARG D 219 O GLU D 222
SHEET 3 K 4 TYR D 257 GLN D 262 -1 O HIS D 260 N THR D 216
SHEET 4 K 4 LEU D 270 ARG D 273 -1 O LEU D 272 N CYS D 259
SHEET 1 L 4 LYS E 6 SER E 11 0
SHEET 2 L 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 L 4 PHE E 62 PHE E 70 -1 O THR E 68 N LEU E 23
SHEET 4 L 4 GLU E 50 HIS E 51 -1 N GLU E 50 O TYR E 67
SHEET 1 M 4 LYS E 6 SER E 11 0
SHEET 2 M 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 M 4 PHE E 62 PHE E 70 -1 O THR E 68 N LEU E 23
SHEET 4 M 4 SER E 55 PHE E 56 -1 N SER E 55 O TYR E 63
SHEET 1 N 4 GLU E 44 ARG E 45 0
SHEET 2 N 4 GLU E 36 LYS E 41 -1 N LYS E 41 O GLU E 44
SHEET 3 N 4 TYR E 78 ASN E 83 -1 O ALA E 79 N LEU E 40
SHEET 4 N 4 LYS E 91 LYS E 94 -1 O LYS E 91 N VAL E 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.01
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.04
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.02
SSBOND 4 CYS D 101 CYS D 164 1555 1555 2.01
SSBOND 5 CYS D 203 CYS D 259 1555 1555 2.05
SSBOND 6 CYS E 25 CYS E 80 1555 1555 2.02
CISPEP 1 TYR A 209 PRO A 210 0 7.44
CISPEP 2 HIS B 31 PRO B 32 0 -2.08
CISPEP 3 TYR D 209 PRO D 210 0 0.91
CISPEP 4 HIS E 31 PRO E 32 0 0.76
CRYST1 60.279 68.269 68.318 70.20 84.40 84.45 P 1 2
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 0.016590 -0.001612 -0.001157 0.00000
SCALE2 0.000000 0.014717 -0.005188 0.00000
SCALE3 0.000000 0.000000 0.015595 0.00000
(ATOM LINES ARE NOT SHOWN.)
END