HEADER TRANSCRIPTION 28-APR-06 2DOE
TITLE SOLUTION STRUCTURE OF THE THIRD FF DOMAIN OF HUMAN TRANSCRIPTION
TITLE 2 FACTOR CA150
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION ELONGATION REGULATOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FF DOMAIN;
COMPND 5 SYNONYM: TATA BOX-BINDING PROTEIN- ASSOCIATED FACTOR 2S,
COMPND 6 TRANSCRIPTION FACTOR CA150;
COMPND 7 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: TCERG1, CA150, TAF2S;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P051128-09;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FF DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DOE 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DOE 1 VERSN
REVDAT 1 28-OCT-06 2DOE 0
JRNL AUTH S.SUZUKI,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE THIRD FF DOMAIN OF HUMAN
JRNL TITL 2 TRANSCRIPTION FACTOR CA150
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DOE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000025652.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1MM 13C/15N-PROTEIN; 20MM D
REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3;90% H2O,
REMARK 210 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9321, OLIVIA 1.10.5,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS,
REMARK 210 SIMULATED ANNEALING
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 SER A 781 134.41 -172.90
REMARK 500 1 GLU A 786 74.41 -104.64
REMARK 500 1 HIS A 806 30.64 -83.59
REMARK 500 1 HIS A 807 54.93 33.81
REMARK 500 1 ASN A 850 111.75 -39.16
REMARK 500 1 PRO A 856 2.74 -69.78
REMARK 500 2 ASP A 787 141.14 -36.31
REMARK 500 2 HIS A 806 33.30 -82.86
REMARK 500 2 HIS A 807 54.99 33.41
REMARK 500 2 LEU A 808 162.58 -43.86
REMARK 500 2 SER A 815 -39.90 -35.07
REMARK 500 2 GLU A 822 -27.59 -39.10
REMARK 500 3 GLU A 784 -45.61 -134.32
REMARK 500 3 ASP A 787 144.99 -35.95
REMARK 500 3 HIS A 806 30.96 -84.11
REMARK 500 3 HIS A 807 55.01 34.46
REMARK 500 3 LEU A 808 164.13 -43.24
REMARK 500 3 GLN A 811 30.03 -85.78
REMARK 500 3 GLU A 822 -27.40 -39.29
REMARK 500 3 ASP A 852 130.62 -35.60
REMARK 500 3 PRO A 856 87.75 -69.78
REMARK 500 3 SER A 857 95.62 -63.43
REMARK 500 4 SER A 779 29.33 40.04
REMARK 500 4 SER A 782 140.69 -172.29
REMARK 500 4 SER A 788 79.46 -109.82
REMARK 500 4 HIS A 806 32.89 -84.21
REMARK 500 4 HIS A 807 54.88 34.59
REMARK 500 4 LEU A 808 168.12 -48.75
REMARK 500 4 GLN A 811 30.05 -88.36
REMARK 500 4 SER A 815 -35.36 -33.78
REMARK 500 4 GLU A 822 -29.58 -36.38
REMARK 500 4 SER A 823 30.02 -84.19
REMARK 500 4 PRO A 856 97.38 -69.73
REMARK 500 4 SER A 858 42.21 38.05
REMARK 500 5 SER A 788 36.71 -93.69
REMARK 500 5 THR A 790 39.29 -91.70
REMARK 500 5 HIS A 806 34.12 -83.57
REMARK 500 5 HIS A 807 54.98 33.19
REMARK 500 5 LEU A 808 163.30 -44.94
REMARK 500 5 SER A 858 42.22 37.58
REMARK 500 6 SER A 778 147.63 -38.08
REMARK 500 6 HIS A 806 36.51 -82.35
REMARK 500 6 HIS A 807 55.02 32.96
REMARK 500 6 LEU A 808 168.65 -46.31
REMARK 500 6 GLN A 811 30.10 -84.50
REMARK 500 6 SER A 815 -35.35 -36.39
REMARK 500 6 GLU A 822 -30.20 -35.95
REMARK 500 6 LYS A 849 48.45 -84.96
REMARK 500 7 HIS A 806 33.70 -82.61
REMARK 500 7 HIS A 807 54.92 34.34
REMARK 500
REMARK 500 THIS ENTRY HAS 145 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003002637.3 RELATED DB: TARGETDB
DBREF 2DOE A 784 853 UNP O14776 TCRG1_HUMAN 784 853
SEQADV 2DOE GLY A 777 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 778 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 779 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE GLY A 780 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 781 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 782 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE GLY A 783 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 854 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE GLY A 855 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE PRO A 856 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 857 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE SER A 858 UNP O14776 CLONING ARTIFACT
SEQADV 2DOE GLY A 859 UNP O14776 CLONING ARTIFACT
SEQRES 1 A 83 GLY SER SER GLY SER SER GLY GLU LYS GLU ASP SER LYS
SEQRES 2 A 83 THR ARG GLY GLU LYS ILE LYS SER ASP PHE PHE GLU LEU
SEQRES 3 A 83 LEU SER ASN HIS HIS LEU ASP SER GLN SER ARG TRP SER
SEQRES 4 A 83 LYS VAL LYS ASP LYS VAL GLU SER ASP PRO ARG TYR LYS
SEQRES 5 A 83 ALA VAL ASP SER SER SER MET ARG GLU ASP LEU PHE LYS
SEQRES 6 A 83 GLN TYR ILE GLU LYS ILE ALA LYS ASN LEU ASP SER SER
SEQRES 7 A 83 GLY PRO SER SER GLY
HELIX 1 1 GLY A 792 ASN A 805 1 14
HELIX 2 2 TRP A 814 VAL A 821 1 8
HELIX 3 3 PRO A 825 ALA A 829 1 5
HELIX 4 4 SER A 833 ALA A 848 1 16
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
(ATOM LINES ARE NOT SHOWN.)
END
