Header list of 2cps.pdb file
Complete list - r 9 2 Bytes
HEADER VIRAL PROTEIN 16-APR-98 2CPS
TITLE SOLUTION NMR STRUCTURES OF THE MAJOR COAT PROTEIN OF FILAMENTOUS
TITLE 2 BACTERIOPHAGE M13 SOLUBILIZED IN SODIUM DODECYL SULPHATE MICELLES, 25
TITLE 3 LOWEST ENERGY STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: M13 MAJOR COAT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: M13 GENE-VIII-PROTEIN OR M13 GVIIIP;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE M13;
SOURCE 3 ORGANISM_TAXID: 10870;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_PLASMID: M13
KEYWDS MAJOR COAT PROTEIN, BACTERIOPHAGE M13, ASSEMBLY, MICELLE, MEMBRANE,
KEYWDS 2 VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR C.H.M.PAPAVOINE,B.E.C.CHRISTIAANS,R.H.A.FOLMER,R.N.H.KONINGS,
AUTHOR 2 C.W.HILBERS
REVDAT 3 09-MAR-22 2CPS 1 REMARK
REVDAT 2 24-FEB-09 2CPS 1 VERSN
REVDAT 1 11-NOV-98 2CPS 0
JRNL AUTH C.H.PAPAVOINE,B.E.CHRISTIAANS,R.H.FOLMER,R.N.KONINGS,
JRNL AUTH 2 C.W.HILBERS
JRNL TITL SOLUTION STRUCTURE OF THE M13 MAJOR COAT PROTEIN IN
JRNL TITL 2 DETERGENT MICELLES: A BASIS FOR A MODEL OF PHAGE ASSEMBLY
JRNL TITL 3 INVOLVING SPECIFIC RESIDUES.
JRNL REF J.MOL.BIOL. V. 282 401 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9735296
JRNL DOI 10.1006/JMBI.1998.1860
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.H.PAPAVOINE,M.L.REMEROWSKI,L.M.HORSTINK,R.N.KONINGS,
REMARK 1 AUTH 2 C.W.HILBERS,F.J.VAN DE VEN
REMARK 1 TITL BACKBONE DYNAMICS OF THE MAJOR COAT PROTEIN OF BACTERIOPHAGE
REMARK 1 TITL 2 M13 IN DETERGENT MICELLES BY 15N NUCLEAR MAGNETIC RESONANCE
REMARK 1 TITL 3 RELAXATION MEASUREMENTS USING THE MODEL-FREE APPROACH AND
REMARK 1 TITL 4 REDUCED SPECTRAL DENSITY MAPPING
REMARK 1 REF BIOCHEMISTRY V. 36 4015 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH C.H.PAPAVOINE,J.M.AELEN,R.N.KONINGS,C.W.HILBERS,
REMARK 1 AUTH 2 F.J.VAN DE VEN
REMARK 1 TITL NMR STUDIES OF THE MAJOR COAT PROTEIN OF BACTERIOPHAGE M13.
REMARK 1 TITL 2 STRUCTURAL INFORMATION OF GVIIIP IN DODECYLPHOSPHOCHOLINE
REMARK 1 TITL 3 MICELLES
REMARK 1 REF EUR.J.BIOCHEM. V. 232 490 1995
REMARK 1 REFN ISSN 0014-2956
REMARK 1 REFERENCE 3
REMARK 1 AUTH C.H.PAPAVOINE,R.N.KONINGS,C.W.HILBERS,F.J.VAN DE VEN
REMARK 1 TITL LOCATION OF M13 COAT PROTEIN IN SODIUM DODECYL SULFATE
REMARK 1 TITL 2 MICELLES AS DETERMINED BY NMR
REMARK 1 REF BIOCHEMISTRY V. 33 12990 1994
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 4
REMARK 1 AUTH F.J.VAN DE VEN,J.W.VAN OS,J.M.AELEN,S.S.WYMENGA,
REMARK 1 AUTH 2 M.L.REMEROWSKI,R.N.KONINGS,C.W.HILBERS
REMARK 1 TITL ASSIGNMENT OF 1H, 15N, AND BACKBONE 13C RESONANCES IN
REMARK 1 TITL 2 DETERGENT-SOLUBILIZED M13 COAT PROTEIN VIA MULTINUCLEAR
REMARK 1 TITL 3 MULTIDIMENSIONAL NMR: A MODEL FOR THE COAT PROTEIN MONOMER
REMARK 1 REF BIOCHEMISTRY V. 32 8322 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CPS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177944.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 311
REMARK 210 PH : 4.9
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; TOCSY; NOESY; NOESY
REMARK 210 -HMQC (15N AND 13C); TOCSY-HMQC
REMARK 210 (15N); HCCH-TOCSY; ROESY-GHSQC;
REMARK 210 HMQC-NOESY-GHSQC; HMQC-J; HNHA;
REMARK 210 HACACB-COSY; HNHB; HSQC(3J CGN);
REMARK 210 HSQC(3JCGC')
REMARK 210 SPECTROMETER FIELD STRENGTH : 400 MHZ; 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; AM; AMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS,
REMARK 210 SIMULATED ANNEALING, THIS
REMARK 210 VERSION OF X-PLOR WAS EXTENDED
REMARK 210 FOR FLOATING CHIRALITY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY, DISTANCE
REMARK 210 RESTRAINTS SMALLER THAN 0.5 A,
REMARK 210 DIHEDRAL VIOLATIONS SMALLER THAN
REMARK 210 5 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N -LABELED M13 COAT PROTEIN SOLUBILIZED
REMARK 210 IN DEUTERATED SODIUM DODECYL SULPHATE MICELLES (CONCENTRATION
REMARK 210 COAT PROTEIN/SDS = 1:250)
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: CLOSE CONTACTS
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
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 1 GLU A 2 63.64 -67.91
REMARK 500 1 ASP A 5 94.18 47.83
REMARK 500 1 ALA A 7 -85.91 -86.75
REMARK 500 1 SER A 17 42.38 -93.24
REMARK 500 1 ALA A 18 69.62 -100.36
REMARK 500 2 ASP A 4 -67.70 -158.77
REMARK 500 2 ASP A 5 79.51 -179.65
REMARK 500 2 ALA A 18 47.89 -93.17
REMARK 500 2 ALA A 49 111.13 -39.47
REMARK 500 3 GLU A 2 50.80 174.34
REMARK 500 3 ASP A 4 -62.70 -103.93
REMARK 500 3 SER A 17 27.11 -151.43
REMARK 500 3 THR A 19 30.57 -97.63
REMARK 500 3 ALA A 49 124.72 68.27
REMARK 500 4 GLU A 2 119.32 67.39
REMARK 500 4 ASP A 5 101.92 -46.37
REMARK 500 4 SER A 17 -54.41 -136.08
REMARK 500 4 ALA A 18 63.81 -100.66
REMARK 500 5 ASP A 5 140.11 63.20
REMARK 500 5 ALA A 18 49.92 -96.18
REMARK 500 6 GLU A 2 130.45 176.01
REMARK 500 6 ASP A 4 44.05 -107.86
REMARK 500 6 ASP A 5 79.48 -176.35
REMARK 500 6 ALA A 7 -48.98 85.96
REMARK 500 6 ALA A 18 64.50 -100.47
REMARK 500 6 ALA A 49 174.26 70.70
REMARK 500 7 GLU A 2 46.74 174.76
REMARK 500 7 ASP A 4 -68.01 -130.35
REMARK 500 7 ASP A 5 116.29 -169.77
REMARK 500 7 THR A 19 37.73 -94.83
REMARK 500 7 SER A 47 40.01 -159.23
REMARK 500 7 ALA A 49 87.89 53.63
REMARK 500 8 GLU A 2 99.18 66.76
REMARK 500 8 ASP A 5 99.47 -42.62
REMARK 500 8 ALA A 18 66.39 -100.34
REMARK 500 8 SER A 47 52.44 -105.67
REMARK 500 9 ASP A 4 -73.80 -108.49
REMARK 500 9 ASP A 5 120.93 62.10
REMARK 500 9 LYS A 8 74.59 33.82
REMARK 500 9 ALA A 9 -73.44 -64.35
REMARK 500 10 ASP A 4 63.50 -68.50
REMARK 500 10 ALA A 9 -78.65 -38.23
REMARK 500 10 THR A 19 34.33 -98.99
REMARK 500 10 SER A 47 24.85 49.03
REMARK 500 10 ALA A 49 156.23 -43.54
REMARK 500 11 GLU A 2 42.51 177.94
REMARK 500 11 ASP A 5 84.35 179.50
REMARK 500 11 ALA A 7 -48.22 85.78
REMARK 500 11 ALA A 9 -73.20 -53.12
REMARK 500 11 SER A 17 55.54 -118.91
REMARK 500
REMARK 500 THIS ENTRY HAS 138 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2CPS A 1 50 UNP P69541 COATB_BPM13 24 73
SEQRES 1 A 50 ALA GLU GLY ASP ASP PRO ALA LYS ALA ALA PHE ASN SER
SEQRES 2 A 50 LEU GLN ALA SER ALA THR GLU TYR ILE GLY TYR ALA TRP
SEQRES 3 A 50 ALA MET VAL VAL VAL ILE VAL GLY ALA THR ILE GLY ILE
SEQRES 4 A 50 LYS LEU PHE LYS LYS PHE THR SER LYS ALA SER
HELIX 1 1 LYS A 8 GLN A 15 1 8
HELIX 2 2 TYR A 24 THR A 46 1 23
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 9 2 Bytes