Header list of 2d9b.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 09-DEC-05 2D9B
TITLE SOLUTION STRUCTURE OF RSGI RUH-052, A GTF2I DOMAIN IN HUMAN CDNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENERAL TRANSCRIPTION FACTOR II-I;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: GTF2I DOMAIN;
COMPND 5 SYNONYM: GTFII-I; TFII-I; BRUTON TYROSINE KINASE-ASSOCIATED PROTEIN
COMPND 6 135; BTK-ASSOCIATED PROTEIN 135; BAP-135; SRF-PHOX1 INTERACTING
COMPND 7 PROTEIN; SPIN; WILLIAMS-BEUREN SYNDROME CHROMOSOME REGION 6 PROTEIN;
COMPND 8 RSGI RUH-052, A GTF2I DOMAIN IN HUMAN CDNA;
COMPND 9 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: AAC08312;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050613-06;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS(E. COLI)
KEYWDS TRANSCRIPTION FACTOR, STRUCTURAL GENOMICS, UNKNOWN FUNCTION, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Y.DOI-KATAYAMA,H.HIROTA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D9B 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2D9B 1 VERSN
REVDAT 1 09-JUN-06 2D9B 0
JRNL AUTH Y.DOI-KATAYAMA,H.HIROTA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF RSGI RUH-052, A GTF2I DOMAIN IN HUMAN
JRNL TITL 2 CDNA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9B COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025146.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.11MM GTF2I DOMAIN U-15N, 13C;
REMARK 210 20MM D-TRIS-HCL (PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9315, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 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 PRO A 43 80.49 -69.80
REMARK 500 1 GLN A 51 47.14 -95.13
REMARK 500 1 PRO A 60 -170.53 -69.76
REMARK 500 1 PHE A 65 119.58 -34.79
REMARK 500 1 ALA A 84 -30.75 -36.93
REMARK 500 1 ARG A 92 135.29 -178.93
REMARK 500 1 PHE A 94 160.09 -48.82
REMARK 500 2 PRO A 43 79.97 -69.81
REMARK 500 2 GLN A 51 40.22 -84.20
REMARK 500 2 ALA A 53 -35.87 -32.95
REMARK 500 2 PRO A 60 -168.68 -69.68
REMARK 500 2 PHE A 65 117.04 -34.11
REMARK 500 2 PRO A 68 2.28 -69.75
REMARK 500 2 ASN A 82 37.03 -99.73
REMARK 500 2 ARG A 92 129.96 -178.72
REMARK 500 2 PHE A 94 148.40 -35.02
REMARK 500 2 LEU A 95 136.91 -36.17
REMARK 500 2 SER A 104 -46.88 -130.22
REMARK 500 2 PRO A 106 2.83 -69.76
REMARK 500 3 SER A 6 97.62 -47.46
REMARK 500 3 PRO A 43 80.01 -69.77
REMARK 500 3 GLN A 51 47.63 -81.69
REMARK 500 3 SER A 52 -56.07 -125.18
REMARK 500 3 ALA A 53 -36.20 -32.72
REMARK 500 3 PRO A 60 -172.16 -69.80
REMARK 500 3 PHE A 65 121.53 -35.15
REMARK 500 3 HIS A 67 141.01 -39.75
REMARK 500 3 ASN A 82 35.23 -97.93
REMARK 500 3 ALA A 84 -26.47 -38.82
REMARK 500 3 ARG A 92 134.50 -178.55
REMARK 500 3 SER A 108 108.85 -172.05
REMARK 500 4 PRO A 43 80.44 -69.78
REMARK 500 4 ALA A 53 -36.57 -31.79
REMARK 500 4 PHE A 65 120.58 -34.65
REMARK 500 4 ASN A 82 38.98 -99.48
REMARK 500 4 ARG A 92 129.60 -179.17
REMARK 500 4 PHE A 94 153.60 -37.41
REMARK 500 4 HIS A 100 -61.34 -105.71
REMARK 500 5 SER A 2 -47.56 -133.17
REMARK 500 5 PRO A 43 79.83 -69.71
REMARK 500 5 PHE A 65 113.21 -34.31
REMARK 500 5 ASN A 82 40.36 -97.80
REMARK 500 5 ALA A 84 -33.92 -36.27
REMARK 500 5 ARG A 92 125.71 -178.89
REMARK 500 5 PHE A 94 157.55 -37.83
REMARK 500 5 PRO A 97 -173.69 -69.78
REMARK 500 5 SER A 104 -61.16 -122.93
REMARK 500 5 SER A 107 131.28 -33.90
REMARK 500 6 SER A 6 88.33 -66.49
REMARK 500 6 PRO A 43 80.73 -69.74
REMARK 500
REMARK 500 THIS ENTRY HAS 206 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO002001981.1 RELATED DB: TARGETDB
DBREF 2D9B A 8 103 UNP P78347 GTF2I_HUMAN 102 197
SEQADV 2D9B GLY A 1 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 2 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 3 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B GLY A 4 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 5 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 6 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B GLY A 7 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 104 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B GLY A 105 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B PRO A 106 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 107 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B SER A 108 UNP P78347 CLONING ARTIFACT
SEQADV 2D9B GLY A 109 UNP P78347 CLONING ARTIFACT
SEQRES 1 A 109 GLY SER SER GLY SER SER GLY MET SER VAL ASP ALA VAL
SEQRES 2 A 109 GLU ILE GLU THR LEU ARG LYS THR VAL GLU ASP TYR PHE
SEQRES 3 A 109 CYS PHE CYS TYR GLY LYS ALA LEU GLY LYS SER THR VAL
SEQRES 4 A 109 VAL PRO VAL PRO TYR GLU LYS MET LEU ARG ASP GLN SER
SEQRES 5 A 109 ALA VAL VAL VAL GLN GLY LEU PRO GLU GLY VAL ALA PHE
SEQRES 6 A 109 LYS HIS PRO GLU ASN TYR ASP LEU ALA THR LEU LYS TRP
SEQRES 7 A 109 ILE LEU GLU ASN LYS ALA GLY ILE SER PHE ILE ILE LYS
SEQRES 8 A 109 ARG PRO PHE LEU GLU PRO LYS LYS HIS VAL GLY GLY SER
SEQRES 9 A 109 GLY PRO SER SER GLY
HELIX 1 1 VAL A 10 LEU A 34 1 25
HELIX 2 2 TYR A 44 ARG A 49 1 6
HELIX 3 3 LEU A 73 GLU A 81 1 9
SHEET 1 A 2 VAL A 54 GLN A 57 0
SHEET 2 A 2 SER A 87 ILE A 90 -1 N SER A 87 O GLN A 57
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