Header list of 1ni8.pdb file
Complete list - 23 202 Bytes
HEADER DNA BINDING PROTEIN 22-DEC-02 1NI8
TITLE H-NS DIMERIZATION MOTIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-BINDING PROTEIN H-NS;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL RESIDUES 1-46;
COMPND 5 SYNONYM: H-NS; HISTONE-LIKE PROTEIN HLP-II; PROTEIN H1; PROTEIN B1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: HNS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS DIMERIZATION, PROTEIN-DNA INTERACTION, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR V.BLOCH,Y.YANG,E.MARGEAT,A.CHAVANIEU,M.T.AUG,B.ROBERT,S.AROLD,
AUTHOR 2 S.RIMSKY,M.KOCHOYAN
REVDAT 3 23-FEB-22 1NI8 1 REMARK
REVDAT 2 24-FEB-09 1NI8 1 VERSN
REVDAT 1 18-FEB-03 1NI8 0
JRNL AUTH V.BLOCH,Y.YANG,E.MARGEAT,A.CHAVANIEU,M.T.AUGE,B.ROBERT,
JRNL AUTH 2 S.AROLD,S.RIMSKY,M.KOCHOYAN
JRNL TITL THE H-NS DIMERISATION DOMAIN DEFINES A NEW FOLD CONTRIBUTING
JRNL TITL 2 TO DNA RECOGNITION
JRNL REF NAT.STRUCT.BIOL. V. 10 3 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12592399
JRNL DOI 10.1038/NSB904
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : GIFA 4, X-PLOR 3.8
REMARK 3 AUTHORS : DELSUC (GIFA), BRUNGER, NILGES (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NI8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017895.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 200 MM NACL
REMARK 210 PRESSURE : NORMAL
REMARK 210 SAMPLE CONTENTS : PEPTIDE 1 TO 2 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 13C FILTRED-
REMARK 210 12CEDITED 2D-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.8
REMARK 210 METHOD USED : SA ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: EXPERIMENTS ON HETEROLABELLED 13C-12C DIMER
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
DBREF 1NI8 A 1 46 UNP P0ACF8 HNS_ECOLI 1 46
DBREF 1NI8 B 1 46 UNP P0ACF8 HNS_ECOLI 1 46
SEQRES 1 A 46 SER GLU ALA LEU LYS ILE LEU ASN ASN ILE ARG THR LEU
SEQRES 2 A 46 ARG ALA GLN ALA ARG GLU CYS THR LEU GLU THR LEU GLU
SEQRES 3 A 46 GLU MET LEU GLU LYS LEU GLU VAL VAL VAL ASN GLU ARG
SEQRES 4 A 46 ARG GLU GLU GLU SER ALA ALA
SEQRES 1 B 46 SER GLU ALA LEU LYS ILE LEU ASN ASN ILE ARG THR LEU
SEQRES 2 B 46 ARG ALA GLN ALA ARG GLU CYS THR LEU GLU THR LEU GLU
SEQRES 3 B 46 GLU MET LEU GLU LYS LEU GLU VAL VAL VAL ASN GLU ARG
SEQRES 4 B 46 ARG GLU GLU GLU SER ALA ALA
HELIX 1 1 SER A 1 ASN A 9 1 9
HELIX 2 2 ASN A 9 ARG A 18 1 10
HELIX 3 3 THR A 21 ALA A 46 1 26
HELIX 4 4 SER B 1 ASN B 9 1 9
HELIX 5 5 ASN B 9 ARG B 18 1 10
HELIX 6 6 THR B 21 ALA B 46 1 26
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 - 23 202 Bytes