Header list of 1vdb.pdb file
Complete list - 2 20 Bytes
HEADER TRANSCRIPTION 20-MAR-04 1VDB
TITLE NMR STRUCTURE OF FMBP-1 TANDEM REPEAT 1 IN 30%(V/V) TFE SOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROIN-MODULATOR-BINDING-PROTEIN-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FMBP-1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC CONSTRUCT
KEYWDS TANDEM REPEAT, N-CAP, DNA BINDING, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR K.KAWAGUCHI,T.YAMAKI,T.AIZAWA,S.TAKIYA,M.DEMURA,K.NITTA
REVDAT 3 02-MAR-22 1VDB 1 REMARK
REVDAT 2 24-FEB-09 1VDB 1 VERSN
REVDAT 1 29-MAR-05 1VDB 0
JRNL AUTH K.KAWAGUCHI,T.YAMAKI,T.AIZAWA,S.TAKIYA,M.DEMURA,K.NITTA
JRNL TITL NMR STRUCTURE OF FMBP-1 TANDEM REPEAT 1 IN 30%(V/V) TFE
JRNL TITL 2 SOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 207 RESTRAINTS, 174 ARE NOE-
REMARK 3 DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 9 DIHEDRAL ANGLE RESTRAINTS,24 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1VDB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1000006489.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 4.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM PEPTIDE; PH 4.6 ; 70% H2O,
REMARK 210 30% TFE-D2; 1.5MM PEPTIDE; PH
REMARK 210 4.6 ; 70% H2O, 30% TFE-D3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; ALPHA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; JEOL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 5 ALA A 22 -78.42 -63.47
REMARK 500 9 THR A 2 -174.53 -170.21
REMARK 500 9 LEU A 21 -67.45 -99.97
REMARK 500 9 ALA A 22 -173.74 60.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VD7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FMBP-1 TANDEM REPEAT 1
REMARK 900 RELATED ID: 1VD8 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FMBP-1 TANDEM REPEAT 2
REMARK 900 RELATED ID: 1VD9 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FMBP-1 TANDEM REPEAT 3
REMARK 900 RELATED ID: 1VDA RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF FMBP-1 TANDEM REPEAT 4
DBREF 1VDB A 1 23 PDB 1VDB 1VDB 1 23
SEQRES 1 A 23 GLU THR SER GLU GLU ARG ALA ALA ARG LEU ALA LYS MET
SEQRES 2 A 23 SER ALA TYR ALA ALA GLN ARG LEU ALA ASN
HELIX 1 1 SER A 3 ALA A 22 1 20
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 - 2 20 Bytes