Header list of 1vd0.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN 17-MAR-04 1VD0
TITLE CAPSID STABILIZING PROTEIN GPD, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEAD DECORATION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GPD, MAJOR CAPSID PROTEIN D;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE LAMBDA;
SOURCE 3 ORGANISM_TAXID: 10710;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: T7-PROMOTER;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PAT101
KEYWDS VIRUS/VIRAL PROTEIN, CAPSID PROTEIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 SCOTTISH STRUCTURAL PROTEOMICS FACILITY, SSPF, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.IWAI,P.FORRER,A.PLUCKTHUN,P.GUNTERT,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 5 02-MAR-22 1VD0 1 REMARK ATOM
REVDAT 4 24-FEB-09 1VD0 1 VERSN
REVDAT 3 16-OCT-07 1VD0 1 REMARK AUTHOR KEYWDS
REVDAT 2 21-JUN-05 1VD0 1 JRNL
REVDAT 1 29-MAR-05 1VD0 0
JRNL AUTH H.IWAI,P.FORRER,A.PLUCKTHUN,P.GUNTERT
JRNL TITL NMR SOLUTION STRUCTURE OF THE MONOMERIC FORM OF THE
JRNL TITL 2 BACTERIOPHAGE LAMBDA CAPSID STABILIZING PROTEIN GPD.
JRNL REF J.BIOMOL.NMR V. 31 351 2005
JRNL REFN ISSN 0925-2738
JRNL PMID 15929002
JRNL DOI 10.1007/S10858-005-0945-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.IWAI,P.FORRER,A.PLUCKTHUN,P.GUNTERT
REMARK 1 TITL ASSIGNMENTS OF 1H AND 15N RESONANCES OF THE BACTERIOPHAGE
REMARK 1 TITL 2 LAMBDA CAPSID STABILIZING PROTEIN GPD
REMARK 1 REF J.BIOMOL.NMR V. 28 89 2004
REMARK 1 REFN ISSN 0925-2738
REMARK 1 PMID 14739644
REMARK 1 DOI 10.1023/B:JNMR.0000012844.21707.8C
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1VD0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000006478.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.3MM 15N LABELLED GPD, 20MM
REMARK 210 SODIUM PHOSPHATE; 1.3MM GPD,
REMARK 210 50MM SODIUM PHOSPHATE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: 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 1 SER A 2 107.58 -170.30
REMARK 500 1 THR A 5 148.27 -173.03
REMARK 500 1 HIS A 8 87.20 -56.85
REMARK 500 1 HIS A 19 43.22 -107.08
REMARK 500 1 PRO A 24 2.85 -69.77
REMARK 500 1 PHE A 101 30.17 -99.94
REMARK 500 2 THR A 5 53.98 -106.75
REMARK 500 2 PHE A 6 44.63 -99.38
REMARK 500 2 TYR A 9 121.89 -35.35
REMARK 500 2 PRO A 11 -174.43 -69.72
REMARK 500 2 ALA A 18 150.32 -42.21
REMARK 500 2 PRO A 24 3.25 -69.78
REMARK 500 2 THR A 53 105.99 -36.13
REMARK 500 3 SER A 2 119.92 -166.77
REMARK 500 3 PHE A 6 111.79 -173.10
REMARK 500 3 PRO A 11 -174.23 -69.80
REMARK 500 3 GLN A 12 33.90 33.83
REMARK 500 3 ASN A 14 36.47 33.94
REMARK 500 3 PRO A 24 3.26 -69.75
REMARK 500 3 THR A 53 120.82 -37.34
REMARK 500 3 ALA A 64 154.08 -46.20
REMARK 500 3 LYS A 76 -32.06 -131.08
REMARK 500 4 SER A 2 147.80 -173.20
REMARK 500 4 LYS A 3 53.97 -105.03
REMARK 500 4 GLN A 12 44.60 -97.09
REMARK 500 4 ALA A 18 155.52 -37.14
REMARK 500 4 PRO A 24 1.61 -69.77
REMARK 500 4 ALA A 90 -29.59 -36.64
REMARK 500 5 GLU A 4 111.35 -171.21
REMARK 500 5 PHE A 6 138.20 -174.82
REMARK 500 5 PRO A 24 0.68 -69.84
REMARK 500 5 ALA A 33 -174.72 -61.84
REMARK 500 5 ASP A 40 -175.84 -68.94
REMARK 500 5 ALA A 48 152.49 -49.03
REMARK 500 5 ALA A 91 95.41 -69.36
REMARK 500 6 PHE A 6 42.75 -84.04
REMARK 500 6 TYR A 9 121.91 -170.95
REMARK 500 6 ALA A 18 52.73 34.17
REMARK 500 7 PHE A 6 135.27 -174.98
REMARK 500 7 TYR A 9 148.31 -170.47
REMARK 500 7 GLN A 12 40.84 -85.07
REMARK 500 7 ALA A 18 31.53 -86.24
REMARK 500 7 PRO A 24 4.93 -69.72
REMARK 500 7 ALA A 48 153.91 -48.26
REMARK 500 8 GLU A 4 129.93 -174.50
REMARK 500 8 HIS A 8 -41.55 -133.35
REMARK 500 8 PRO A 24 6.17 -69.79
REMARK 500 8 THR A 53 108.10 -38.07
REMARK 500 8 LYS A 76 -30.80 -130.80
REMARK 500 9 LYS A 3 146.15 -172.36
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5807 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFTS
REMARK 900 RELATED ID: MY_001000120.1 RELATED DB: TARGETDB
DBREF 1VD0 A 1 109 UNP P03712 VCAD_LAMBD 2 110
SEQRES 1 A 109 THR SER LYS GLU THR PHE THR HIS TYR GLN PRO GLN GLY
SEQRES 2 A 109 ASN SER ASP PRO ALA HIS THR ALA THR ALA PRO GLY GLY
SEQRES 3 A 109 LEU SER ALA LYS ALA PRO ALA MET THR PRO LEU MET LEU
SEQRES 4 A 109 ASP THR SER SER ARG LYS LEU VAL ALA TRP ASP GLY THR
SEQRES 5 A 109 THR ASP GLY ALA ALA VAL GLY ILE LEU ALA VAL ALA ALA
SEQRES 6 A 109 ASP GLN THR SER THR THR LEU THR PHE TYR LYS SER GLY
SEQRES 7 A 109 THR PHE ARG TYR GLU ASP VAL LEU TRP PRO GLU ALA ALA
SEQRES 8 A 109 SER ASP GLU THR LYS LYS ARG THR ALA PHE ALA GLY THR
SEQRES 9 A 109 ALA ILE SER ILE VAL
HELIX 1 1 ASP A 93 THR A 99 1 7
SHEET 1 A 2 THR A 20 ALA A 23 0
SHEET 2 A 2 LEU A 72 TYR A 75 -1 O PHE A 74 N ALA A 21
SHEET 1 B 3 LEU A 46 ALA A 48 0
SHEET 2 B 3 THR A 35 LEU A 39 -1 N MET A 38 O VAL A 47
SHEET 3 B 3 ALA A 57 LEU A 61 -1 O VAL A 58 N LEU A 37
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes