Header list of 2bbp.pdb file
Complete list - 9 20 Bytes
HEADER VIRAL PROTEIN 17-OCT-05 2BBP
TITLE NMR STRUCTURES OF THE PEPTIDE LINKED TO THE GENOME (VPG) OF POLIOVIRUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME LINKED PROTEIN VPG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-22;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMAN POLIOVIRUS
SOURCE 4 SEROTYPE 1.
KEYWDS VPG, RNA TRANSCRIPTION PRIMER, FLEXIBLE STRUCTURE, VIRAL POLYMERASE,
KEYWDS 2 PICORNAVIRUS, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR C.H.SCHEIN,N.OEZGUEN
REVDAT 4 09-MAR-22 2BBP 1 REMARK
REVDAT 3 24-FEB-09 2BBP 1 VERSN
REVDAT 2 04-JUL-06 2BBP 1 JRNL
REVDAT 1 28-MAR-06 2BBP 0
JRNL AUTH C.H.SCHEIN,N.OEZGUEN,D.E.VOLK,R.GARIMELLA,A.PAUL,W.BRAUN
JRNL TITL NMR STRUCTURE OF THE VIRAL PEPTIDE LINKED TO THE GENOME
JRNL TITL 2 (VPG) OF POLIOVIRUS.
JRNL REF PEPTIDES V. 27 1676 2006
JRNL REFN ISSN 0196-9781
JRNL PMID 16540201
JRNL DOI 10.1016/J.PEPTIDES.2006.01.018
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.H.SCHEIN,D.E.VOLK,N.OEZGUEN,A.PAUL
REMARK 1 TITL NOVEL, STRUCTURE-BASED MECHANISM FOR URIDYLYLATION OF THE
REMARK 1 TITL 2 GENOME-LINKED PEPTIDE (VPG) OF PICORNAVIRUSES
REMARK 1 REF PROTEINS 2006
REMARK 1 REFN ESSN 1097-0134
REMARK 1 PMID 16498624
REMARK 1 DOI 10.1002/PROT.20891
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NOAH 2.0, DIAMOD 2.2
REMARK 3 AUTHORS : MUMENTHALER, C. ET AL. (NOAH), GUENTERT, P. ET AL.
REMARK 3 (DIAMOD)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT OF THE NOE ASSIGNMENT IS
REMARK 3 PERFORMED ITERATIVELY. NOAH PASSES GEOMETRICAL CONSTRAINTS
REMARK 3 DERIVED FROM THE NOE LIST TO DIAMOD. DIAMOD CALCULATES A BUNDLE
REMARK 3 OF STRUCTURES WITH LEAST VIOLATION OF THE CONSTRAINTS. THE NEW
REMARK 3 BUNDLE OF STRUCTURES IS THE BASIS FOR REFINEMENT OF THE
REMARK 3 ASSIGNMENTS IN NOAH.
REMARK 4
REMARK 4 2BBP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034912.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 3.7 MM PEPTIDE, 10 MM NA
REMARK 210 PHOSPHATE BUFFER, PH 7.2, DSS,
REMARK 210 10% D20, 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIAMOD 2.2, FELIX
REMARK 210 METHOD USED : AUTOMATIC NOE ASSIGNMENT IN
REMARK 210 COMBINATION WITH DISTANCE
REMARK 210 GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 ALA A 2 -61.18 -157.39
REMARK 500 1 TYR A 3 91.49 49.36
REMARK 500 1 ASN A 8 -46.92 -167.26
REMARK 500 1 LYS A 9 143.06 -173.34
REMARK 500 1 LYS A 10 96.67 -17.75
REMARK 500 1 PRO A 11 -73.54 -74.97
REMARK 500 1 THR A 15 86.61 -154.80
REMARK 500 1 ARG A 17 73.51 34.94
REMARK 500 1 THR A 18 -36.06 -150.36
REMARK 500 2 TYR A 3 90.23 12.45
REMARK 500 2 THR A 4 73.26 -112.15
REMARK 500 2 ASN A 8 -47.36 -166.83
REMARK 500 2 LYS A 10 98.04 -22.18
REMARK 500 2 PRO A 11 -71.37 -74.95
REMARK 500 2 THR A 15 86.53 -150.77
REMARK 500 2 THR A 18 -35.68 -143.88
REMARK 500 3 TYR A 3 76.01 49.01
REMARK 500 3 ASN A 8 -46.15 -168.26
REMARK 500 3 LYS A 10 98.14 -23.18
REMARK 500 3 ASN A 12 -43.84 -170.51
REMARK 500 3 THR A 15 79.13 55.56
REMARK 500 3 ILE A 16 45.61 39.10
REMARK 500 3 ARG A 17 70.53 37.08
REMARK 500 3 THR A 18 -25.54 -148.83
REMARK 500 4 ALA A 2 -51.68 -163.05
REMARK 500 4 TYR A 3 91.93 52.09
REMARK 500 4 ASN A 8 -47.00 -169.29
REMARK 500 4 LYS A 10 98.37 -21.86
REMARK 500 4 PRO A 11 -70.26 -75.05
REMARK 500 4 THR A 15 86.50 -154.30
REMARK 500 4 ARG A 17 65.06 39.52
REMARK 500 4 THR A 18 -36.30 -140.91
REMARK 500 5 TYR A 3 88.66 44.50
REMARK 500 5 ASN A 8 -48.15 -168.69
REMARK 500 5 LYS A 10 97.90 -21.61
REMARK 500 5 PRO A 11 -72.20 -75.01
REMARK 500 5 THR A 18 -37.93 -143.65
REMARK 500 5 LYS A 20 -98.89 -130.06
REMARK 500 5 VAL A 21 -58.76 -159.71
REMARK 500 6 TYR A 3 53.46 175.84
REMARK 500 6 THR A 4 77.22 -106.35
REMARK 500 6 ASN A 8 -48.99 -168.31
REMARK 500 6 LYS A 10 98.45 -20.30
REMARK 500 6 PRO A 11 -70.21 -74.93
REMARK 500 6 LYS A 20 73.92 -116.07
REMARK 500 7 ALA A 2 115.92 68.19
REMARK 500 7 TYR A 3 -27.31 -173.11
REMARK 500 7 LEU A 6 40.73 -149.64
REMARK 500 7 ASN A 8 -32.81 -167.58
REMARK 500 7 LYS A 10 101.36 -29.87
REMARK 500
REMARK 500 THIS ENTRY HAS 69 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BBL RELATED DB: PDB
REMARK 900 NMR STRUCTURES OF THE PEPTIDE LINKED TO THE GENOME (VPG) OF
REMARK 900 POLIOVIRUS IN A STABILIZING SOLVENT
DBREF 2BBP A 1 22 UNP P03300 POLG_POL1M 1544 1565
SEQRES 1 A 22 GLY ALA TYR THR GLY LEU PRO ASN LYS LYS PRO ASN VAL
SEQRES 2 A 22 PRO THR ILE ARG THR ALA LYS VAL GLN
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 - 9 20 Bytes