Header list of 1bw6.pdb file
Complete list - 16 202 Bytes
HEADER DNA BINDING PROTEIN 30-SEP-98 1BW6
TITLE HUMAN CENTROMERE PROTEIN B (CENP-B) DNA BINDIGN DOMAIN RP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (CENTROMERE PROTEIN B);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PRSETA;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PHR1
KEYWDS CENTROMERE PROTEIN, DNA-BINDING, HELIX-TURN-HELIX, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, DNA
KEYWDS 3 BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR J.IWAHARA,T.KIGAWA,K.KITAGAWA,H.MASUMOTO,T.OKAZAKI,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 4 16-FEB-22 1BW6 1 REMARK
REVDAT 3 24-FEB-09 1BW6 1 VERSN
REVDAT 2 29-DEC-99 1BW6 4 HEADER COMPND REMARK JRNL
REVDAT 2 2 4 ATOM SOURCE SEQRES
REVDAT 1 07-OCT-98 1BW6 0
JRNL AUTH J.IWAHARA,T.KIGAWA,K.KITAGAWA,H.MASUMOTO,T.OKAZAKI,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL A HELIX-TURN-HELIX STRUCTURE UNIT IN HUMAN CENTROMERE
JRNL TITL 2 PROTEIN B (CENP-B).
JRNL REF EMBO J. V. 17 827 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9451007
JRNL DOI 10.1093/EMBOJ/17.3.827
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: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1BW6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000008234.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 400 MM NA2SO4
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX-500; AMX-600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 ENERGY-MINIMIZED STRUCTURE. THE STRUCTRURE WAS DETERMINED USING
REMARK 210 TRIPLE-
REMARK 210 RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED CENP-B DBD RP1.
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 PRO A 3 -103.33 -78.64
REMARK 500 ARG A 5 -56.85 -166.44
REMARK 500 ARG A 6 -52.84 -140.32
REMARK 500 ASN A 36 -100.13 -163.17
REMARK 500 PRO A 38 174.18 -59.67
REMARK 500 SER A 40 -60.51 -100.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 5 0.30 SIDE CHAIN
REMARK 500 ARG A 6 0.29 SIDE CHAIN
REMARK 500 ARG A 11 0.15 SIDE CHAIN
REMARK 500 ARG A 15 0.30 SIDE CHAIN
REMARK 500 ARG A 27 0.29 SIDE CHAIN
REMARK 500 ARG A 33 0.21 SIDE CHAIN
REMARK 500 ARG A 34 0.32 SIDE CHAIN
REMARK 500 ARG A 50 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MY_001000013.1 RELATED DB: TARGETDB
DBREF 1BW6 A 1 56 UNP P07199 CENPB_HUMAN 1 56
SEQRES 1 A 56 MET GLY PRO LYS ARG ARG GLN LEU THR PHE ARG GLU LYS
SEQRES 2 A 56 SER ARG ILE ILE GLN GLU VAL GLU GLU ASN PRO ASP LEU
SEQRES 3 A 56 ARG LYS GLY GLU ILE ALA ARG ARG PHE ASN ILE PRO PRO
SEQRES 4 A 56 SER THR LEU SER THR ILE LEU LYS ASN LYS ARG ALA ILE
SEQRES 5 A 56 LEU ALA SER GLU
HELIX 1 H1 PHE A 10 ASN A 23 1 14
HELIX 2 H2 LYS A 28 PHE A 35 1 8
HELIX 3 H3 SER A 40 ASN A 48 1 9
HELIX 4 H4 LYS A 49 ALA A 54 1 6
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
Complete list - 16 202 Bytes