Header list of 2hfh.pdb file
Complete list - r 9 2 Bytes
HEADER HNF-3 HOMOLOGUES 27-JAN-98 2HFH
TITLE THE NMR STRUCTURES OF A WINGED HELIX PROTEIN: GENESIS, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENESIS;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: HFH-2;
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 CELL_LINE: 293;
SOURCE 6 ORGAN: LIVER, LUNG, HEART;
SOURCE 7 CELLULAR_LOCATION: NUCLEUS;
SOURCE 8 GENE: HFH-2, GENESIS;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: HMS-174;
SOURCE 12 EXPRESSION_SYSTEM_ORGANELLE: INCLUSION BODIES;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET21;
SOURCE 15 EXPRESSION_SYSTEM_GENE: T7;
SOURCE 16 OTHER_DETAILS: FIRST PUBLISHED IN PNAS 90, 3948-3952
KEYWDS HNF-3 HOMOLOGUES, WINGED HELIX PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR I.MARSDEN,C.JIN,X.LIAO
REVDAT 3 09-MAR-22 2HFH 1 REMARK
REVDAT 2 24-FEB-09 2HFH 1 VERSN
REVDAT 1 17-JUN-98 2HFH 0
JRNL AUTH I.MARSDEN,C.JIN,X.LIAO
JRNL TITL STRUCTURAL CHANGES IN THE REGION DIRECTLY ADJACENT TO THE
JRNL TITL 2 DNA-BINDING HELIX HIGHLIGHT A POSSIBLE MECHANISM TO EXPLAIN
JRNL TITL 3 THE OBSERVED CHANGES IN THE SEQUENCE-SPECIFIC BINDING OF
JRNL TITL 4 WINGED HELIX PROTEINS.
JRNL REF J.MOL.BIOL. V. 278 293 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9571051
JRNL DOI 10.1006/JMBI.1998.1703
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH I.MARSDEN,Y.CHEN,C.JIN,X.LIAO
REMARK 1 TITL EVIDENCE THAT THE DNA BINDING SPECIFICITY OF WINGED HELIX
REMARK 1 TITL 2 PROTEINS IS MEDIATED BY A STRUCTURAL CHANGE IN THE AMINO
REMARK 1 TITL 3 ACID SEQUENCE ADJACENT TO THE PRINCIPAL DNA BINDING HELIX
REMARK 1 REF BIOCHEMISTRY V. 36 13248 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA
REMARK 3 AUTHORS : GUNTERT,WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HFH 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_1000178184.
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 : NOESYHSQC; HNCA; HNCACB;
REMARK 210 CBCA(CO)HN; HBHA(CO)HN; HCCHTOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; UNITY PLUS 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TRIAD
REMARK 210 METHOD USED : DIANA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST 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 ARG A 94
REMARK 465 ARG A 95
REMARK 465 ARG A 96
REMARK 465 LYS A 97
REMARK 465 ARG A 98
REMARK 465 PHE A 99
REMARK 465 LYS A 100
REMARK 465 ARG A 101
REMARK 465 LEU A 102
REMARK 465 GLN A 103
REMARK 465 HIS A 104
REMARK 465 HIS A 105
REMARK 465 HIS A 106
REMARK 465 HIS A 107
REMARK 465 HIS A 108
REMARK 465 HIS A 109
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 TYR A 40 H PHE A 44 1.57
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 VAL A 2 -27.56 85.98
REMARK 500 1 LYS A 3 60.59 26.16
REMARK 500 1 GLN A 21 -84.77 -120.41
REMARK 500 1 LYS A 22 42.68 -179.44
REMARK 500 1 ASN A 58 -82.09 -88.60
REMARK 500 1 CYS A 60 49.61 95.85
REMARK 500 1 ARG A 66 71.68 63.43
REMARK 500 1 LYS A 73 -60.62 -121.58
REMARK 500 1 GLN A 82 -54.82 -122.76
REMARK 500 1 SER A 83 -71.03 -79.47
REMARK 500 1 GLU A 84 18.01 51.30
REMARK 500 1 ASP A 88 68.30 -173.47
REMARK 500 1 SER A 91 -57.01 175.97
REMARK 500 1 PHE A 92 53.54 178.99
REMARK 500 2 PRO A 20 25.38 -75.02
REMARK 500 2 LYS A 22 30.91 95.06
REMARK 500 2 ASN A 58 -76.42 -86.11
REMARK 500 2 CYS A 60 31.06 97.69
REMARK 500 2 ARG A 66 85.86 176.56
REMARK 500 2 ASN A 70 78.20 -119.56
REMARK 500 2 LYS A 73 -86.42 -143.81
REMARK 500 2 GLN A 82 -56.62 174.73
REMARK 500 2 ASP A 88 66.55 175.49
REMARK 500 3 VAL A 2 29.48 42.51
REMARK 500 3 GLN A 21 -82.24 -124.75
REMARK 500 3 LYS A 22 39.06 178.29
REMARK 500 3 ASN A 58 -83.27 -113.55
REMARK 500 3 CYS A 60 52.32 92.24
REMARK 500 3 PRO A 65 33.61 -74.96
REMARK 500 3 ARG A 66 63.99 -173.96
REMARK 500 3 PRO A 68 36.33 -75.00
REMARK 500 3 LYS A 73 -55.00 -142.31
REMARK 500 3 GLN A 82 49.96 74.44
REMARK 500 3 MET A 86 -73.46 -79.90
REMARK 500 3 PHE A 87 -61.78 158.39
REMARK 500 3 SER A 91 79.44 159.72
REMARK 500 4 VAL A 2 27.62 41.99
REMARK 500 4 TYR A 6 -78.80 -119.92
REMARK 500 4 GLN A 21 -82.87 -140.76
REMARK 500 4 LYS A 22 38.71 179.83
REMARK 500 4 ASN A 58 -84.81 -88.12
REMARK 500 4 CYS A 60 44.14 94.62
REMARK 500 4 ARG A 66 84.78 176.57
REMARK 500 4 LYS A 73 -66.36 -120.45
REMARK 500 4 GLN A 82 45.70 176.57
REMARK 500 4 PHE A 87 -53.92 174.84
REMARK 500 4 ASP A 88 31.50 -141.70
REMARK 500 5 TYR A 6 -83.03 -119.22
REMARK 500 5 GLN A 21 -76.76 -106.61
REMARK 500 5 LYS A 22 42.50 167.37
REMARK 500
REMARK 500 THIS ENTRY HAS 271 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HFH A 2 101 UNP Q63245 FOXD3_RAT 2 101
SEQRES 1 A 109 MET VAL LYS PRO PRO TYR SER TYR ILE ALA LEU ILE THR
SEQRES 2 A 109 MET ALA ILE LEU GLN SER PRO GLN LYS LYS LEU THR LEU
SEQRES 3 A 109 SER GLY ILE CYS GLU PHE ILE SER ASN ARG PHE PRO TYR
SEQRES 4 A 109 TYR ARG GLU LYS PHE PRO ALA TRP GLN ASN SER ILE ARG
SEQRES 5 A 109 HIS ASN LEU SER LEU ASN ASP CYS PHE VAL LYS ILE PRO
SEQRES 6 A 109 ARG GLU PRO GLY ASN PRO GLY LYS GLY ASN TYR TRP THR
SEQRES 7 A 109 LEU ASP PRO GLN SER GLU ASP MET PHE ASP ASN GLY SER
SEQRES 8 A 109 PHE LEU ARG ARG ARG LYS ARG PHE LYS ARG LEU GLN HIS
SEQRES 9 A 109 HIS HIS HIS HIS HIS
HELIX 1 1 TYR A 8 LEU A 17 1 10
HELIX 2 2 LEU A 26 SER A 34 1 9
HELIX 3 3 PRO A 38 ARG A 41 1 4
HELIX 4 4 PRO A 45 ASN A 58 5 14
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 - r 9 2 Bytes