Header list of 1kq8.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 04-JAN-02 1KQ8 TITLE SOLUTION STRUCTURE OF WINGED HELIX PROTEIN HFH-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEPATOCYTE NUCLEAR FACTOR 3 FORKHEAD HOMOLOG 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: HFH-1; HNF-3/FORKHEAD HOMOLOG-1; WINGED HELIX/FORKHEAD COMPND 5 TRANSCRIPTION FACTOR; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 3 ORGANISM_COMMON: NORWAY RAT; SOURCE 4 ORGANISM_TAXID: 10116; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS WINGED HELIX PROTEIN, HFH-1, TRANSCRIPTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR W.SHENG,M.RANCE,X.LIAO REVDAT 6 23-FEB-22 1KQ8 1 REMARK SEQADV REVDAT 5 24-FEB-09 1KQ8 1 VERSN REVDAT 4 25-FEB-03 1KQ8 1 REMARK REVDAT 3 18-MAR-02 1KQ8 1 JRNL REVDAT 2 22-FEB-02 1KQ8 1 AUTHOR JRNL REVDAT 1 22-JAN-02 1KQ8 0 JRNL AUTH W.SHENG,M.RANCE,X.LIAO JRNL TITL STRUCTURE COMPARISON OF TWO CONSERVED HNF-3/FKH PROTEINS JRNL TITL 2 HFH-1 AND GENESIS INDICATES THE EXISTENCE OF FOLDING JRNL TITL 3 DIFFERENCES IN THEIR COMPLEXES WITH A DNA BINDING SEQUENCE. JRNL REF BIOCHEMISTRY V. 41 3286 2002 JRNL REFN ISSN 0006-2960 JRNL PMID 11876636 JRNL DOI 10.1021/BI011908K REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH I.MARSDEN,C.JIN,X.LIAO REMARK 1 TITL STRUCTURAL CHANGES IN THE REGION DIRECTLY ADJACENT TO THE REMARK 1 TITL 2 DNA-BINDING HELIX HIGHLIGHT A POSSIBLE MECHANISM TO EXPLAIN REMARK 1 TITL 3 THE OBSERVED CHANGES IN THE SEQUENCE-SPECIFIC BINDING OF REMARK 1 TITL 4 WINGED HELIX PROTEINS REMARK 1 REF J.MOL.BIOL. V. 278 293 1998 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.1998.1703 REMARK 1 REFERENCE 2 REMARK 1 AUTH C.JIN,I.MARSDEN,X.CHEN,X.LIAO REMARK 1 TITL SEQUENCE SPECIFIC COLLECTIVE MOTIONS IN A WINGED HELIX DNA REMARK 1 TITL 2 BINDING DOMAIN DETECTED BY 15N RELAXATION NMR REMARK 1 REF BIOCHEMISTRY V. 37 6179 1998 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI980031V REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GUNTER, P. REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1KQ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JAN-02. REMARK 100 THE DEPOSITION ID IS D_1000015223. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 290 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY; HNCA-J; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX; UNITYPLUS REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION 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 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-20 REMARK 465 RES C SSSEQI REMARK 465 PRO A 2 REMARK 465 LYS A 3 REMARK 465 PRO A 4 REMARK 465 PRO A 5 REMARK 465 TYR A 6 REMARK 465 SER A 7 REMARK 465 ASN A 83 REMARK 465 SER A 84 REMARK 465 GLU A 85 REMARK 465 TYR A 86 REMARK 465 THR A 87 REMARK 465 PHE A 88 REMARK 465 ALA A 89 REMARK 465 ASP A 90 REMARK 465 GLY A 91 REMARK 465 VAL A 92 REMARK 465 PHE A 93 REMARK 465 ARG A 94 REMARK 465 ARG A 95 REMARK 465 ARG A 96 REMARK 465 ARG A 97 REMARK 465 TYR A 98 REMARK 465 ARG A 99 REMARK 465 LEU A 100 REMARK 465 SER A 101 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LEU A 24 H TRP A 78 1.47 REMARK 500 O TRP A 47 H VAL A 51 1.51 REMARK 500 REMARK 500 REMARK: NULL 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 SER A 19 -142.05 -89.09 REMARK 500 1 ALA A 20 33.61 -168.50 REMARK 500 1 SER A 43 -69.55 -143.50 REMARK 500 1 TYR A 44 107.99 -169.93 REMARK 500 1 ASN A 58 -76.16 -108.43 REMARK 500 1 CYS A 60 59.77 88.93 REMARK 500 1 PHE A 61 -169.52 -119.19 REMARK 500 1 ARG A 66 89.01 40.34 REMARK 500 1 SER A 69 65.74 -177.59 REMARK 500 1 TRP A 72 -36.89 91.33 REMARK 500 1 LYS A 74 51.20 177.30 REMARK 500 2 SER A 19 -144.33 -86.23 REMARK 500 2 ALA A 20 31.68 -166.07 REMARK 500 2 SER A 43 -79.93 -135.47 REMARK 500 2 TYR A 44 119.44 -165.65 REMARK 500 2 ASN A 58 -88.93 -99.21 REMARK 500 2 CYS A 60 64.47 92.46 REMARK 500 2 PHE A 61 -165.33 -119.22 REMARK 500 2 ARG A 66 95.42 49.01 REMARK 500 2 SER A 69 58.05 -176.32 REMARK 500 2 ARG A 70 65.35 -170.45 REMARK 500 2 TRP A 72 25.16 48.63 REMARK 500 2 LYS A 74 42.45 -161.57 REMARK 500 2 ASP A 75 -68.85 -175.61 REMARK 500 3 SER A 19 -143.28 -82.79 REMARK 500 3 ALA A 20 32.91 -169.32 REMARK 500 3 SER A 43 -72.97 -150.30 REMARK 500 3 TYR A 44 117.65 -174.81 REMARK 500 3 ASN A 58 -89.84 -98.39 REMARK 500 3 CYS A 60 63.88 91.40 REMARK 500 3 PHE A 61 -165.33 -119.73 REMARK 500 3 SER A 69 41.04 177.50 REMARK 500 3 ARG A 70 68.52 -171.57 REMARK 500 3 TRP A 72 -38.58 80.63 REMARK 500 3 LYS A 74 -40.74 -173.24 REMARK 500 3 ASN A 81 75.97 -167.49 REMARK 500 4 ALA A 20 43.24 82.19 REMARK 500 4 SER A 43 -76.82 -69.90 REMARK 500 4 THR A 45 48.67 -94.02 REMARK 500 4 ASN A 58 -80.97 -93.06 REMARK 500 4 CYS A 60 78.90 95.77 REMARK 500 4 PHE A 61 -166.52 -123.96 REMARK 500 4 ARG A 66 75.80 -154.97 REMARK 500 4 SER A 69 41.81 -167.25 REMARK 500 4 ARG A 70 67.31 -165.32 REMARK 500 4 TRP A 72 -40.06 -178.52 REMARK 500 4 LYS A 74 -40.16 -173.34 REMARK 500 5 SER A 19 -149.71 -86.19 REMARK 500 5 ALA A 20 23.18 -154.45 REMARK 500 5 SER A 43 -74.80 -69.48 REMARK 500 REMARK 500 THIS ENTRY HAS 217 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1KQ8 A 2 101 UNP Q63244 FOXQ1_RAT 99 198 SEQADV 1KQ8 THR A 13 UNP Q63244 ALA 110 CONFLICT SEQADV 1KQ8 TYR A 98 UNP Q63244 LYS 195 CONFLICT SEQRES 1 A 100 PRO LYS PRO PRO TYR SER TYR ILE ALA LEU ILE THR MET SEQRES 2 A 100 ALA ILE ARG ASP SER ALA GLY GLY ARG LEU THR LEU ALA SEQRES 3 A 100 GLU ILE ASN GLU TYR LEU MET GLY LYS PHE PRO PHE PHE SEQRES 4 A 100 ARG GLY SER TYR THR GLY TRP ARG ASN SER VAL ARG HIS SEQRES 5 A 100 ASN LEU SER LEU ASN ASP CYS PHE VAL LYS VAL LEU ARG SEQRES 6 A 100 ASP PRO SER ARG PRO TRP GLY LYS ASP ASN TYR TRP MET SEQRES 7 A 100 LEU ASN PRO ASN SER GLU TYR THR PHE ALA ASP GLY VAL SEQRES 8 A 100 PHE ARG ARG ARG ARG TYR ARG LEU SER HELIX 1 1 TYR A 8 ARG A 17 1 10 HELIX 2 2 THR A 25 PHE A 37 1 13 HELIX 3 3 PHE A 39 SER A 43 5 5 HELIX 4 4 TRP A 47 ASP A 59 1 13 SHEET 1 A 2 VAL A 62 LYS A 63 0 SHEET 2 A 2 TRP A 78 MET A 79 -1 O MET A 79 N VAL A 62 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