HEADER VIRAL PROTEIN 13-DEC-05 2C9N
TITLE STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN AT APPROXIMATELY 3.
TITLE 2 5 ANGSTROM RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*AP*CP*TP*GP*AP*CP*TP*CP*AP *T)-3';
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(*CP*AP*TP*GP*AP*GP*TP*CP*AP*GP *T)-3';
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: BZLF1 TRANS-ACTIVATOR PROTEIN;
COMPND 11 CHAIN: Y, Z;
COMPND 12 FRAGMENT: DNA-BINDING AND DIMERIZATION DOMAIN, RESIDUES 175-236;
COMPND 13 SYNONYM: EB1, ZEBRA;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;
SOURCE 4 ORGANISM_TAXID: 10376;
SOURCE 5 MOL_ID: 2;
SOURCE 6 SYNTHETIC: YES;
SOURCE 7 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;
SOURCE 8 ORGANISM_TAXID: 10376;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 4;
SOURCE 11 ORGANISM_TAXID: 10376;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS VIRAL PROTEIN, EPSTEIN-BARR VIRUS, EBV, ZEBRA, BZLF1, ZTA, Z, LYTIC
KEYWDS 2 CYCLE ACTIVATION, BZIP PROTEIN, VIRAL PROTEIN DNA-BINDING, NUCLEAR
KEYWDS 3 PROTEIN, TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.PETOSA,P.MORAND,F.BAUDIN,M.MOULIN,J.B.ARTERO,C.W.MULLER
REVDAT 3 13-DEC-23 2C9N 1 REMARK
REVDAT 2 24-FEB-09 2C9N 1 VERSN
REVDAT 1 21-FEB-06 2C9N 0
JRNL AUTH C.PETOSA,P.MORAND,F.BAUDIN,M.MOULIN,J.B.ARTERO,C.W.MULLER
JRNL TITL STRUCTURAL BASIS OF LYTIC CYCLE ACTIVATION BY THE
JRNL TITL 2 EPSTEIN-BARR VIRUS ZEBRA PROTEIN
JRNL REF MOL.CELL V. 21 565 2006
JRNL REFN ISSN 1097-2765
JRNL PMID 16483937
JRNL DOI 10.1016/J.MOLCEL.2006.01.006
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 10000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 2965
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 SET) : 0.368
REMARK 3 FREE R VALUE : 0.366
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 159
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 972
REMARK 3 NUCLEIC ACID ATOMS : 442
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.61700
REMARK 3 B22 (A**2) : -36.42700
REMARK 3 B33 (A**2) : 31.81000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 25.14900
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 13.30
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: GIVEN THE ANISOTROPY AND LOW RESOLUTION
REMARK 3 OF THE DATA, LITTLE EFFORT WAS SPENT ON PROPERLY REFINING THIS
REMARK 3 STRUCTURE. FOR A HIGH RESOLUTION STRUCTURE OF ESSENTIALLY THE
REMARK 3 SAME PROTEIN-DNA COMPLEX, SEE PDB ENTRY 2C91. RESIDUES 175-177
REMARK 3 AND 237-245 SHOW POOR DENSITY AND ARE NOT INCLUDED IN THE MODEL
REMARK 4
REMARK 4 2C9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1290026822.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9861
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.40
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.26000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2C91
REMARK 200
REMARK 200 REMARK: CRYSTALS DIFFRACT ANISOTROPICALLY. CRYSTALS DIFFRACT TO
REMARK 200 3.7 A ALONG A-STAR AND B-STAR, AND TO BETTER THAN 3A ALONG C-
REMARK 200 STAR. WE ESTIMATE THAT THE TRUE COMPLETENESS DOES NOT EXCEED 50
REMARK 200 PERCENT FOR REFLECTIONS IN THE 3.3 - 3.7 A SHELL.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.00
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.65000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.18500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.65000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.18500
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Y, Z
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 Y 174
REMARK 465 LEU Y 175
REMARK 465 GLU Y 176
REMARK 465 ILE Y 177
REMARK 465 MET Z 174
REMARK 465 LEU Z 175
REMARK 465 GLU Z 176
REMARK 465 ILE Z 177
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CA LYS Y 192 N PHE Y 193 1.56
REMARK 500 C LYS Y 192 CA PHE Y 193 1.57
REMARK 500 N LYS Y 192 N PHE Y 193 1.63
REMARK 500 NH2 ARG Y 215 OE2 GLU Z 210 2.06
REMARK 500 O CYS Y 189 CD2 PHE Y 193 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 O ASP Y 236 NZ LYS Z 219 4444 0.55
REMARK 500 C ASP Y 236 CE LYS Z 219 4444 0.91
REMARK 500 OXT ASP Y 236 CE LYS Z 219 4444 1.04
REMARK 500 O ASP Y 236 CE LYS Z 219 4444 1.48
REMARK 500 C ASP Y 236 NZ LYS Z 219 4444 1.56
REMARK 500 C5' DC A 4 O3' DT A 14 1545 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS Y 189 CB CYS Y 189 SG -0.398
REMARK 500 CYS Z 189 CB CYS Z 189 SG -0.396
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS Y 192 CA - C - N ANGL. DEV. = -49.3 DEGREES
REMARK 500 LYS Y 192 O - C - N ANGL. DEV. = 40.3 DEGREES
REMARK 500 PHE Y 193 C - N - CA ANGL. DEV. = -50.8 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 PRO Y 235 -179.25 -67.07
REMARK 500 SER Z 224 49.16 -90.59
REMARK 500 PRO Z 235 72.88 -62.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZSD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HLA-B*3501 PRESENTING AN 11-MER EBVANTIGEN
REMARK 900 EPLPQGQLTAY
REMARK 900 RELATED ID: 2AXF RELATED DB: PDB
REMARK 900 THE IMMUNOGENICITY OF A VIRAL CYTOTOXIC T CELL EPITOPE ISCONTROLLED
REMARK 900 BY ITS MHC-BOUND CONFORMATION
REMARK 900 RELATED ID: 2AXG RELATED DB: PDB
REMARK 900 THE IMMUNOGENICITY OF A VIRAL CYTOTOXIC T CELL EPITOPE ISCONTROLLED
REMARK 900 BY ITS MHC-BOUND CONFORMATION
REMARK 900 RELATED ID: 2C9L RELATED DB: PDB
REMARK 900 STRUCTURE OF THE EPSTEIN-BARR VIRUS ZEBRA PROTEIN
DBREF 2C9N A 4 14 PDB 2C9N 2C9N 4 14
DBREF 2C9N B 106 116 PDB 2C9N 2C9N 106 116
DBREF 2C9N Y 174 174 PDB 2C9N 2C9N 174 174
DBREF 2C9N Y 175 236 UNP P03206 BZLF1_EBV 175 236
DBREF 2C9N Z 174 174 PDB 2C9N 2C9N 174 174
DBREF 2C9N Z 175 236 UNP P03206 BZLF1_EBV 175 236
SEQRES 1 A 11 DC DA DC DT DG DA DC DT DC DA DT
SEQRES 1 B 11 DC DA DT DG DA DG DT DC DA DG DT
SEQRES 1 Y 63 MET LEU GLU ILE LYS ARG TYR LYS ASN ARG VAL ALA SER
SEQRES 2 Y 63 ARG LYS CYS ARG ALA LYS PHE LYS GLN LEU LEU GLN HIS
SEQRES 3 Y 63 TYR ARG GLU VAL ALA ALA ALA LYS SER SER GLU ASN ASP
SEQRES 4 Y 63 ARG LEU ARG LEU LEU LEU LYS GLN MET CYS PRO SER LEU
SEQRES 5 Y 63 ASP VAL ASP SER ILE ILE PRO ARG THR PRO ASP
SEQRES 1 Z 63 MET LEU GLU ILE LYS ARG TYR LYS ASN ARG VAL ALA SER
SEQRES 2 Z 63 ARG LYS CYS ARG ALA LYS PHE LYS GLN LEU LEU GLN HIS
SEQRES 3 Z 63 TYR ARG GLU VAL ALA ALA ALA LYS SER SER GLU ASN ASP
SEQRES 4 Z 63 ARG LEU ARG LEU LEU LEU LYS GLN MET CYS PRO SER LEU
SEQRES 5 Z 63 ASP VAL ASP SER ILE ILE PRO ARG THR PRO ASP
HELIX 1 1 LYS Y 178 CYS Y 222 1 45
HELIX 2 2 ASP Y 226 ILE Y 231 1 6
HELIX 3 3 LYS Z 178 CYS Z 222 1 45
HELIX 4 4 ASP Z 226 ILE Z 230 5 5
CRYST1 185.300 36.370 26.470 90.00 95.25 90.00 C 1 2 1 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 0.005397 0.000000 0.000496 0.00000
SCALE2 0.000000 0.027495 0.000000 0.00000
SCALE3 0.000000 0.000000 0.037938 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
