Header list of 1fli.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION/DNA 15-SEP-94 1FLI
TITLE DNA-BINDING DOMAIN OF FLI-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLI-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: T7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: T7;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3B;
SOURCE 10 EXPRESSION_SYSTEM_GENE: T7
KEYWDS TRANSCRIPTION/DNA, TRANSCRIPTION-DNA COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR H.LIANG,X.MAO,E.T.OLEJNICZAK,D.G.NETTESHEIM,L.YU,R.P.MEADOWS,
AUTHOR 2 C.B.THOMPSON,S.W.FESIK
REVDAT 3 23-FEB-22 1FLI 1 REMARK
REVDAT 2 24-FEB-09 1FLI 1 VERSN
REVDAT 1 15-SEP-95 1FLI 0
JRNL AUTH H.LIANG,X.MAO,E.T.OLEJNICZAK,D.G.NETTESHEIM,L.YU,
JRNL AUTH 2 R.P.MEADOWS,C.B.THOMPSON,S.W.FESIK
JRNL TITL SOLUTION STRUCTURE OF THE ETS DOMAIN OF FLI-1 WHEN BOUND TO
JRNL TITL 2 DNA.
JRNL REF NAT.STRUCT.BIOL. V. 1 871 1994
JRNL REFN ISSN 1072-8368
JRNL PMID 7773776
JRNL DOI 10.1038/NSB1294-871
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.LIANG,E.T.OLEJNICZAK,X.MAO,D.G.NETTESHEIM,L.YU,
REMARK 1 AUTH 2 C.B.THOMPSON,S.W.FESIK
REMARK 1 TITL THE SECONDARY STRUCTURE OF THE ETS DOMAIN OF HUMAN FLI-1
REMARK 1 TITL 2 RESEMBLES THAT OF THE HELIX-TURN-HELIX DNA-BINDING MOTIF OF
REMARK 1 TITL 3 THE ESCHERICHIA COLI CATABOLITE GENE ACTIVATOR PROTEIN
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 11655 1994
REMARK 1 REFN ISSN 0027-8424
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FLI 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_1000173331.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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
DBREF 1FLI A 276 373 UNP Q01543 FLI1_HUMAN 276 373
SEQRES 1 A 98 PRO GLY SER GLY GLN ILE GLN LEU TRP GLN PHE LEU LEU
SEQRES 2 A 98 GLU LEU LEU SER ASP SER ALA ASN ALA SER CYS ILE THR
SEQRES 3 A 98 TRP GLU GLY THR ASN GLY GLU PHE LYS MET THR ASP PRO
SEQRES 4 A 98 ASP GLU VAL ALA ARG ARG TRP GLY GLU ARG LYS SER LYS
SEQRES 5 A 98 PRO ASN MET ASN TYR ASP LYS LEU SER ARG ALA LEU ARG
SEQRES 6 A 98 TYR TYR TYR ASP LYS ASN ILE MET THR LYS VAL HIS GLY
SEQRES 7 A 98 LYS ARG TYR ALA TYR LYS PHE ASP PHE HIS GLY ILE ALA
SEQRES 8 A 98 GLN ALA LEU GLN PRO HIS PRO
HELIX 1 1 TRP A 284 SER A 292 1 9
HELIX 2 2 PRO A 314 ARG A 324 1 11
HELIX 3 3 ASP A 333 ASP A 344 1 12
SHEET 1 A 2 ILE A 300 THR A 301 0
SHEET 2 A 2 LYS A 310 MET A 311 -1 N LYS A 310 O THR A 301
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 - b 23 2 Bytes