HEADER VIRAL PROTEIN, DNA-BINDING PROTEIN 06-OCT-09 3K4T
TITLE CRYSTAL STRUCTURE OF THE VIRION-ASSOCIATED PROTEIN P3 FROM
TITLE 2 CAULIMOVIRUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VIRION-ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 1-95;
COMPND 5 SYNONYM: VAP, DNA-BINDING PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CAULIFLOWER MOSAIC VIRUS (STRAIN STRASBOURG);
SOURCE 3 ORGANISM_COMMON: CAMV;
SOURCE 4 ORGANISM_TAXID: 10648;
SOURCE 5 STRAIN: STRASBOURG;
SOURCE 6 GENE: ORF III;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21-DE3;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-3A
KEYWDS COILED-COIL, VIRAL PROTEIN, TETRAMER, DNA-BINDING PROTEIN, PROTEIN
KEYWDS 2 BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR C.DUMAS,F.HOH
REVDAT 4 06-SEP-23 3K4T 1 REMARK
REVDAT 3 13-JUL-11 3K4T 1 VERSN
REVDAT 2 19-MAY-10 3K4T 1 JRNL
REVDAT 1 16-MAR-10 3K4T 0
JRNL AUTH F.HOH,M.UZEST,M.DRUCKER,C.PLISSON-CHASTANG,P.BRON,S.BLANC,
JRNL AUTH 2 C.DUMAS
JRNL TITL STRUCTURAL INSIGHTS INTO THE MOLECULAR MECHANISMS OF
JRNL TITL 2 CAULIFLOWER MOSAIC VIRUS TRANSMISSION BY ITS INSECT VECTOR.
JRNL REF J.VIROL. V. 84 4706 2010
JRNL REFN ISSN 0022-538X
JRNL PMID 20181714
JRNL DOI 10.1128/JVI.02662-09
REMARK 2
REMARK 2 RESOLUTION. 2.59 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 8660
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.100
REMARK 3 FREE R VALUE TEST SET COUNT : 657
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) : 2.59
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.65
REMARK 3 REFLECTION IN BIN (WORKING SET) : 618
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.4400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2153
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 29
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 60.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.07000
REMARK 3 B33 (A**2) : 0.03000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.08000
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): 0.391
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.311
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 33.250
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.911
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2171 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2927 ; 1.255 ; 2.015
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 280 ; 5.391 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;42.551 ;30.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 468 ;20.609 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 371 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1500 ; 0.005 ; 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): 1414 ; 0.373 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2294 ; 0.722 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 757 ; 1.274 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 633 ; 2.187 ; 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): 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 32
REMARK 3 RESIDUE RANGE : B 3 B 32
REMARK 3 RESIDUE RANGE : C 2 C 32
REMARK 3 RESIDUE RANGE : D 3 D 32
REMARK 3 ORIGIN FOR THE GROUP (A): 44.7070 14.8960 33.4180
REMARK 3 T TENSOR
REMARK 3 T11: 0.3462 T22: 0.0963
REMARK 3 T33: 0.3788 T12: -0.0759
REMARK 3 T13: 0.1228 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 8.0085 L22: 2.9031
REMARK 3 L33: 15.4977 L12: 3.7416
REMARK 3 L13: 9.0064 L23: 6.6741
REMARK 3 S TENSOR
REMARK 3 S11: 0.0963 S12: 0.3411 S13: -0.2461
REMARK 3 S21: 0.1280 S22: 0.0537 S23: -0.0297
REMARK 3 S31: 0.4047 S32: 0.0757 S33: -0.1500
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 40
REMARK 3 RESIDUE RANGE : B 33 B 40
REMARK 3 RESIDUE RANGE : C 33 C 40
REMARK 3 RESIDUE RANGE : D 33 D 40
REMARK 3 ORIGIN FOR THE GROUP (A): 26.6190 6.7800 10.5510
REMARK 3 T TENSOR
REMARK 3 T11: 0.9189 T22: 1.1426
REMARK 3 T33: 0.9101 T12: -0.1008
REMARK 3 T13: 0.2440 T23: -0.3757
REMARK 3 L TENSOR
REMARK 3 L11: 5.9853 L22: 0.5922
REMARK 3 L33: 14.9008 L12: 1.8632
REMARK 3 L13: 9.4293 L23: 2.9433
REMARK 3 S TENSOR
REMARK 3 S11: 0.0348 S12: 1.0522 S13: -0.1775
REMARK 3 S21: 0.0830 S22: 0.2694 S23: 0.0273
REMARK 3 S31: 0.1583 S32: 1.5074 S33: -0.3042
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 41 A 59
REMARK 3 RESIDUE RANGE : B 41 B 59
REMARK 3 RESIDUE RANGE : C 41 C 59
REMARK 3 RESIDUE RANGE : D 41 D 59
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7410 2.5580 -4.2190
REMARK 3 T TENSOR
REMARK 3 T11: 0.3387 T22: 0.7070
REMARK 3 T33: 0.4490 T12: -0.1046
REMARK 3 T13: 0.1086 T23: -0.2382
REMARK 3 L TENSOR
REMARK 3 L11: 8.6028 L22: 4.1179
REMARK 3 L33: 12.6448 L12: 1.7426
REMARK 3 L13: 6.2067 L23: 2.9202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0196 S12: 0.3547 S13: -0.1758
REMARK 3 S21: 0.0944 S22: 0.3656 S23: -0.1087
REMARK 3 S31: -0.0347 S32: 1.1541 S33: -0.3460
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 60 A 71
REMARK 3 RESIDUE RANGE : B 60 B 73
REMARK 3 RESIDUE RANGE : C 60 C 74
REMARK 3 RESIDUE RANGE : D 60 D 70
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8970 -3.2740 -21.2210
REMARK 3 T TENSOR
REMARK 3 T11: 0.3262 T22: 0.6189
REMARK 3 T33: 0.5163 T12: -0.0138
REMARK 3 T13: 0.0775 T23: -0.3080
REMARK 3 L TENSOR
REMARK 3 L11: 12.6134 L22: 10.9730
REMARK 3 L33: 17.6170 L12: 3.9628
REMARK 3 L13: 10.5499 L23: 3.5073
REMARK 3 S TENSOR
REMARK 3 S11: 0.0902 S12: 0.1911 S13: -0.0709
REMARK 3 S21: 0.5813 S22: 0.5375 S23: -0.7238
REMARK 3 S31: -0.1406 S32: 1.6196 S33: -0.6277
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: WEIGHT MATRIX 0.035
REMARK 4
REMARK 4 3K4T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000055546.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979250
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9317
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
REMARK 200 RESOLUTION RANGE LOW (A) : 18.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
REMARK 200 R SYM FOR SHELL (I) : 0.34500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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 3F6N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 1000, 0.1M MES-NAOH BUFFER,
REMARK 280 1.2 MOLAR-EXCESS DNA OLIGONUCLEOTIDE (POLY-AT, 14 BP) , PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 14.40900
REMARK 290 SMTRY3 2 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -141.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 1
REMARK 465 THR A 72
REMARK 465 GLN A 73
REMARK 465 PRO A 74
REMARK 465 LYS A 75
REMARK 465 GLU A 76
REMARK 465 GLN A 77
REMARK 465 LEU A 78
REMARK 465 ILE A 79
REMARK 465 GLU A 80
REMARK 465 GLN A 81
REMARK 465 PRO A 82
REMARK 465 LYS A 83
REMARK 465 GLU A 84
REMARK 465 LYS A 85
REMARK 465 GLY A 86
REMARK 465 LYS A 87
REMARK 465 GLY A 88
REMARK 465 LEU A 89
REMARK 465 ASN A 90
REMARK 465 LEU A 91
REMARK 465 GLY A 92
REMARK 465 LYS A 93
REMARK 465 TYR A 94
REMARK 465 SER A 95
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PRO B 74
REMARK 465 LYS B 75
REMARK 465 GLU B 76
REMARK 465 GLN B 77
REMARK 465 LEU B 78
REMARK 465 ILE B 79
REMARK 465 GLU B 80
REMARK 465 GLN B 81
REMARK 465 PRO B 82
REMARK 465 LYS B 83
REMARK 465 GLU B 84
REMARK 465 LYS B 85
REMARK 465 GLY B 86
REMARK 465 LYS B 87
REMARK 465 GLY B 88
REMARK 465 LEU B 89
REMARK 465 ASN B 90
REMARK 465 LEU B 91
REMARK 465 GLY B 92
REMARK 465 LYS B 93
REMARK 465 TYR B 94
REMARK 465 SER B 95
REMARK 465 MET C 1
REMARK 465 LYS C 75
REMARK 465 GLU C 76
REMARK 465 GLN C 77
REMARK 465 LEU C 78
REMARK 465 ILE C 79
REMARK 465 GLU C 80
REMARK 465 GLN C 81
REMARK 465 PRO C 82
REMARK 465 LYS C 83
REMARK 465 GLU C 84
REMARK 465 LYS C 85
REMARK 465 GLY C 86
REMARK 465 LYS C 87
REMARK 465 GLY C 88
REMARK 465 LEU C 89
REMARK 465 ASN C 90
REMARK 465 LEU C 91
REMARK 465 GLY C 92
REMARK 465 LYS C 93
REMARK 465 TYR C 94
REMARK 465 SER C 95
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLY D 71
REMARK 465 THR D 72
REMARK 465 GLN D 73
REMARK 465 PRO D 74
REMARK 465 LYS D 75
REMARK 465 GLU D 76
REMARK 465 GLN D 77
REMARK 465 LEU D 78
REMARK 465 ILE D 79
REMARK 465 GLU D 80
REMARK 465 GLN D 81
REMARK 465 PRO D 82
REMARK 465 LYS D 83
REMARK 465 GLU D 84
REMARK 465 LYS D 85
REMARK 465 GLY D 86
REMARK 465 LYS D 87
REMARK 465 GLY D 88
REMARK 465 LEU D 89
REMARK 465 ASN D 90
REMARK 465 LEU D 91
REMARK 465 GLY D 92
REMARK 465 LYS D 93
REMARK 465 TYR D 94
REMARK 465 SER D 95
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 N ASN B 3 O HOH B 109 2.13
REMARK 500 O LEU B 67 OG1 THR B 72 2.15
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 B 37 150.29 -48.88
REMARK 500 CYS B 60 70.21 40.22
REMARK 500 PRO C 37 126.63 -31.77
REMARK 500 CYS C 60 70.21 54.84
REMARK 500 PRO D 37 137.62 -33.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F6N RELATED DB: PDB
REMARK 900 THE SAME PROTEIN, P64 CRYSTAL FORM
DBREF 3K4T A 1 95 UNP P03551 VDBP_CAMVS 1 95
DBREF 3K4T B 1 95 UNP P03551 VDBP_CAMVS 1 95
DBREF 3K4T C 1 95 UNP P03551 VDBP_CAMVS 1 95
DBREF 3K4T D 1 95 UNP P03551 VDBP_CAMVS 1 95
SEQRES 1 A 95 MET ALA ASN LEU ASN GLN ILE GLN LYS GLU VAL SER GLU
SEQRES 2 A 95 ILE LEU SER ASP GLN LYS SER MET LYS ALA ASP ILE LYS
SEQRES 3 A 95 ALA ILE LEU GLU LEU LEU GLY SER GLN ASN PRO ILE LYS
SEQRES 4 A 95 GLU SER LEU GLU THR VAL ALA ALA LYS ILE VAL ASN ASP
SEQRES 5 A 95 LEU THR LYS LEU ILE ASN ASP CYS PRO CYS ASN LYS GLU
SEQRES 6 A 95 ILE LEU GLU ALA LEU GLY THR GLN PRO LYS GLU GLN LEU
SEQRES 7 A 95 ILE GLU GLN PRO LYS GLU LYS GLY LYS GLY LEU ASN LEU
SEQRES 8 A 95 GLY LYS TYR SER
SEQRES 1 B 95 MET ALA ASN LEU ASN GLN ILE GLN LYS GLU VAL SER GLU
SEQRES 2 B 95 ILE LEU SER ASP GLN LYS SER MET LYS ALA ASP ILE LYS
SEQRES 3 B 95 ALA ILE LEU GLU LEU LEU GLY SER GLN ASN PRO ILE LYS
SEQRES 4 B 95 GLU SER LEU GLU THR VAL ALA ALA LYS ILE VAL ASN ASP
SEQRES 5 B 95 LEU THR LYS LEU ILE ASN ASP CYS PRO CYS ASN LYS GLU
SEQRES 6 B 95 ILE LEU GLU ALA LEU GLY THR GLN PRO LYS GLU GLN LEU
SEQRES 7 B 95 ILE GLU GLN PRO LYS GLU LYS GLY LYS GLY LEU ASN LEU
SEQRES 8 B 95 GLY LYS TYR SER
SEQRES 1 C 95 MET ALA ASN LEU ASN GLN ILE GLN LYS GLU VAL SER GLU
SEQRES 2 C 95 ILE LEU SER ASP GLN LYS SER MET LYS ALA ASP ILE LYS
SEQRES 3 C 95 ALA ILE LEU GLU LEU LEU GLY SER GLN ASN PRO ILE LYS
SEQRES 4 C 95 GLU SER LEU GLU THR VAL ALA ALA LYS ILE VAL ASN ASP
SEQRES 5 C 95 LEU THR LYS LEU ILE ASN ASP CYS PRO CYS ASN LYS GLU
SEQRES 6 C 95 ILE LEU GLU ALA LEU GLY THR GLN PRO LYS GLU GLN LEU
SEQRES 7 C 95 ILE GLU GLN PRO LYS GLU LYS GLY LYS GLY LEU ASN LEU
SEQRES 8 C 95 GLY LYS TYR SER
SEQRES 1 D 95 MET ALA ASN LEU ASN GLN ILE GLN LYS GLU VAL SER GLU
SEQRES 2 D 95 ILE LEU SER ASP GLN LYS SER MET LYS ALA ASP ILE LYS
SEQRES 3 D 95 ALA ILE LEU GLU LEU LEU GLY SER GLN ASN PRO ILE LYS
SEQRES 4 D 95 GLU SER LEU GLU THR VAL ALA ALA LYS ILE VAL ASN ASP
SEQRES 5 D 95 LEU THR LYS LEU ILE ASN ASP CYS PRO CYS ASN LYS GLU
SEQRES 6 D 95 ILE LEU GLU ALA LEU GLY THR GLN PRO LYS GLU GLN LEU
SEQRES 7 D 95 ILE GLU GLN PRO LYS GLU LYS GLY LYS GLY LEU ASN LEU
SEQRES 8 D 95 GLY LYS TYR SER
HET CL A 100 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL CL 1-
FORMUL 6 HOH *29(H2 O)
HELIX 1 1 ALA A 2 GLY A 33 1 32
HELIX 2 2 PRO A 37 CYS A 60 1 24
HELIX 3 3 CYS A 62 GLY A 71 1 10
HELIX 4 4 ASN B 3 SER B 34 1 32
HELIX 5 5 PRO B 37 ASP B 59 1 23
HELIX 6 6 CYS B 62 GLY B 71 1 10
HELIX 7 7 ASN C 3 GLY C 33 1 31
HELIX 8 8 PRO C 37 ASN C 58 1 22
HELIX 9 9 ASP C 59 PRO C 61 5 3
HELIX 10 10 CYS C 62 LEU C 70 1 9
HELIX 11 11 ASN D 3 GLN D 35 1 33
HELIX 12 12 PRO D 37 CYS D 60 1 24
HELIX 13 13 CYS D 62 GLU D 68 1 7
SSBOND 1 CYS A 60 CYS D 62 1555 1555 2.05
SSBOND 2 CYS A 62 CYS C 60 1555 1555 2.04
SSBOND 3 CYS B 60 CYS C 62 1555 1555 2.04
SSBOND 4 CYS B 62 CYS D 60 1555 1555 2.04
CRYST1 69.302 28.818 75.957 90.00 92.08 90.00 P 1 21 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 0.014430 0.000000 0.000524 0.00000
SCALE2 0.000000 0.034701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013174 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
