Header list of 1tfb.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION FACTOR 14-NOV-96 1TFB
TITLE NMR STUDIES OF HUMAN GENERAL TRANSCRIPTION FACTOR TFIIB: DYNAMICS AND
TITLE 2 INTERACTION WITH VP16 ACTIVATION DOMAIN, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TFIIB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CONSTRUCT COMPRISES RESIDUES 1 - 3 AND 112 - 316 OF FULL
COMPND 5 LENGTH HUMAN TFIIB;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: RESIDUES MET 1 AND ALA 2 ARE OMITTED FROM THE
COMPND 9 COORDINATES, AND SER 3 IS NUMBERED AS SER 111
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 GENE: HUMAN TFIIB DELTA 4-111;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 11 EXPRESSION_SYSTEM_GENE: HUMAN TFIIB DELTA 4-111;
SOURCE 12 OTHER_DETAILS: FURTHER DETAILS CAN BE FOUND IN HA ET AL., GENES AND
SOURCE 13 DEVELOPMENT 7 (1993) 1021
KEYWDS TRANSCRIPTION FACTOR, HUMAN GENERAL TRANSCRIPTION FACTOR TFIIB, C-
KEYWDS 2 TERMINAL CORE DOMAIN, CYCLIN BOX FOLD
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.BAGBY,M.IKURA
REVDAT 3 02-MAR-22 1TFB 1 REMARK
REVDAT 2 24-FEB-09 1TFB 1 VERSN
REVDAT 1 12-MAR-97 1TFB 0
JRNL AUTH F.HAYASHI,R.ISHIMA,D.LIU,K.I.TONG,S.KIM,D.REINBERG,S.BAGBY,
JRNL AUTH 2 M.IKURA
JRNL TITL HUMAN GENERAL TRANSCRIPTION FACTOR TFIIB: CONFORMATIONAL
JRNL TITL 2 VARIABILITY AND INTERACTION WITH VP16 ACTIVATION DOMAIN.
JRNL REF BIOCHEMISTRY V. 37 7941 1998
JRNL REFN ISSN 0006-2960
JRNL PMID 9609687
JRNL DOI 10.1021/BI9801098
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH D.B.NIKOLOV,H.CHEN,E.D.HALAY,A.A.USHEVA,K.HISATAKE,D.K.LEE,
REMARK 1 AUTH 2 R.G.ROEDER,S.K.BURLEY
REMARK 1 TITL CRYSTAL STRUCTURE OF A TFIIB-TBP-TATA-ELEMENT TERNARY
REMARK 1 TITL 2 COMPLEX
REMARK 1 REF NATURE V. 377 119 1995
REMARK 1 REFN ISSN 0028-0836
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.BAGBY,S.KIM,E.MALDONADO,K.I.TONG,D.REINBERG,M.IKURA
REMARK 1 TITL SOLUTION STRUCTURE OF THE C-TERMINAL CORE DOMAIN OF HUMAN
REMARK 1 TITL 2 TFIIB: SIMILARITY TO CYCLIN A AND INTERACTION WITH
REMARK 1 TITL 3 TATA-BINDING PROTEIN
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 82 857 1995
REMARK 1 REFN ISSN 0092-8674
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TFB 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_1000176652.
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 : 20
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
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 MET A 109
REMARK 465 ALA A 110
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 ARG A 112 -64.91 -124.96
REMARK 500 1 GLN A 148 172.89 -46.77
REMARK 500 1 LEU A 151 57.11 -142.89
REMARK 500 1 ALA A 155 75.02 163.12
REMARK 500 1 ILE A 166 -60.37 -92.08
REMARK 500 1 GLU A 171 101.81 168.07
REMARK 500 1 ARG A 175 -92.93 62.48
REMARK 500 1 THR A 176 -152.64 178.51
REMARK 500 1 SER A 187 94.88 45.00
REMARK 500 1 LEU A 202 65.20 -157.48
REMARK 500 1 GLU A 203 -90.84 -49.77
REMARK 500 1 THR A 204 -68.95 -179.08
REMARK 500 1 SER A 205 35.22 78.39
REMARK 500 1 ASP A 207 94.99 -52.54
REMARK 500 1 LEU A 208 21.29 -155.21
REMARK 500 1 ILE A 209 -81.77 -146.98
REMARK 500 1 THR A 210 26.40 43.85
REMARK 500 1 THR A 211 -33.20 -132.75
REMARK 500 1 SER A 220 55.28 -113.21
REMARK 500 1 CYS A 223 36.76 73.44
REMARK 500 1 ASP A 243 82.22 61.04
REMARK 500 1 VAL A 245 63.83 -165.93
REMARK 500 1 PRO A 246 42.78 -81.32
REMARK 500 1 ARG A 248 -92.88 -98.57
REMARK 500 1 ALA A 266 25.99 44.20
REMARK 500 1 ARG A 269 -141.87 -138.98
REMARK 500 1 VAL A 280 -88.78 -86.88
REMARK 500 1 ALA A 281 147.32 -173.81
REMARK 500 1 LEU A 291 57.70 -155.89
REMARK 500 1 ARG A 295 30.85 -179.33
REMARK 500 1 ALA A 296 164.25 163.47
REMARK 500 1 ASP A 298 39.13 -90.34
REMARK 500 1 THR A 302 -23.76 160.70
REMARK 500 1 PHE A 304 93.86 -46.67
REMARK 500 1 PHE A 306 65.83 75.06
REMARK 500 1 ASP A 311 27.40 44.03
REMARK 500 1 LYS A 312 66.33 160.04
REMARK 500 1 LEU A 313 78.43 -115.70
REMARK 500 1 GLN A 315 99.80 71.09
REMARK 500 2 ARG A 112 -48.41 -141.97
REMARK 500 2 ASN A 129 65.69 69.42
REMARK 500 2 PRO A 131 -159.30 -77.88
REMARK 500 2 LYS A 152 28.13 40.17
REMARK 500 2 ALA A 155 83.94 160.72
REMARK 500 2 ILE A 166 -71.97 -80.75
REMARK 500 2 GLU A 171 89.42 162.43
REMARK 500 2 PRO A 174 -158.43 -78.05
REMARK 500 2 ARG A 175 -103.09 59.74
REMARK 500 2 THR A 176 -152.85 178.78
REMARK 500 2 ARG A 185 49.88 -142.56
REMARK 500
REMARK 500 THIS ENTRY HAS 769 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 112 0.25 SIDE CHAIN
REMARK 500 1 ARG A 127 0.29 SIDE CHAIN
REMARK 500 1 ARG A 132 0.32 SIDE CHAIN
REMARK 500 1 ARG A 137 0.30 SIDE CHAIN
REMARK 500 1 ARG A 154 0.24 SIDE CHAIN
REMARK 500 1 ARG A 169 0.24 SIDE CHAIN
REMARK 500 1 ARG A 175 0.26 SIDE CHAIN
REMARK 500 1 ARG A 185 0.09 SIDE CHAIN
REMARK 500 1 ARG A 193 0.19 SIDE CHAIN
REMARK 500 1 ARG A 217 0.15 SIDE CHAIN
REMARK 500 1 ARG A 237 0.23 SIDE CHAIN
REMARK 500 1 ARG A 248 0.30 SIDE CHAIN
REMARK 500 1 ARG A 269 0.15 SIDE CHAIN
REMARK 500 1 ARG A 290 0.27 SIDE CHAIN
REMARK 500 1 ARG A 295 0.31 SIDE CHAIN
REMARK 500 2 ARG A 112 0.22 SIDE CHAIN
REMARK 500 2 ARG A 127 0.30 SIDE CHAIN
REMARK 500 2 ARG A 132 0.20 SIDE CHAIN
REMARK 500 2 ARG A 137 0.32 SIDE CHAIN
REMARK 500 2 ARG A 154 0.28 SIDE CHAIN
REMARK 500 2 ARG A 169 0.24 SIDE CHAIN
REMARK 500 2 ARG A 175 0.28 SIDE CHAIN
REMARK 500 2 ARG A 185 0.16 SIDE CHAIN
REMARK 500 2 ARG A 193 0.26 SIDE CHAIN
REMARK 500 2 ARG A 217 0.10 SIDE CHAIN
REMARK 500 2 ARG A 237 0.31 SIDE CHAIN
REMARK 500 2 ARG A 248 0.26 SIDE CHAIN
REMARK 500 2 ARG A 269 0.21 SIDE CHAIN
REMARK 500 2 ARG A 286 0.30 SIDE CHAIN
REMARK 500 2 ARG A 290 0.25 SIDE CHAIN
REMARK 500 3 ARG A 112 0.30 SIDE CHAIN
REMARK 500 3 ARG A 127 0.32 SIDE CHAIN
REMARK 500 3 ARG A 132 0.21 SIDE CHAIN
REMARK 500 3 ARG A 137 0.11 SIDE CHAIN
REMARK 500 3 ARG A 154 0.15 SIDE CHAIN
REMARK 500 3 ARG A 169 0.30 SIDE CHAIN
REMARK 500 3 ARG A 175 0.22 SIDE CHAIN
REMARK 500 3 ARG A 185 0.16 SIDE CHAIN
REMARK 500 3 ARG A 193 0.30 SIDE CHAIN
REMARK 500 3 ARG A 217 0.27 SIDE CHAIN
REMARK 500 3 ARG A 237 0.28 SIDE CHAIN
REMARK 500 3 ARG A 248 0.29 SIDE CHAIN
REMARK 500 3 ARG A 269 0.22 SIDE CHAIN
REMARK 500 3 ARG A 286 0.13 SIDE CHAIN
REMARK 500 3 ARG A 290 0.32 SIDE CHAIN
REMARK 500 3 ARG A 295 0.12 SIDE CHAIN
REMARK 500 4 ARG A 112 0.32 SIDE CHAIN
REMARK 500 4 ARG A 127 0.31 SIDE CHAIN
REMARK 500 4 ARG A 132 0.24 SIDE CHAIN
REMARK 500 4 ARG A 137 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 312 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TFB A 112 316 UNP Q00403 TF2B_HUMAN 112 316
SEQRES 1 A 208 MET ALA SER ARG ALA MET MET ASN ALA PHE LYS GLU ILE
SEQRES 2 A 208 THR THR MET ALA ASP ARG ILE ASN LEU PRO ARG ASN ILE
SEQRES 3 A 208 VAL ASP ARG THR ASN ASN LEU PHE LYS GLN VAL TYR GLU
SEQRES 4 A 208 GLN LYS SER LEU LYS GLY ARG ALA ASN ASP ALA ILE ALA
SEQRES 5 A 208 SER ALA CYS LEU TYR ILE ALA CYS ARG GLN GLU GLY VAL
SEQRES 6 A 208 PRO ARG THR PHE LYS GLU ILE CYS ALA VAL SER ARG ILE
SEQRES 7 A 208 SER LYS LYS GLU ILE GLY ARG CYS PHE LYS LEU ILE LEU
SEQRES 8 A 208 LYS ALA LEU GLU THR SER VAL ASP LEU ILE THR THR GLY
SEQRES 9 A 208 ASP PHE MET SER ARG PHE CYS SER ASN LEU CYS LEU PRO
SEQRES 10 A 208 LYS GLN VAL GLN MET ALA ALA THR HIS ILE ALA ARG LYS
SEQRES 11 A 208 ALA VAL GLU LEU ASP LEU VAL PRO GLY ARG SER PRO ILE
SEQRES 12 A 208 SER VAL ALA ALA ALA ALA ILE TYR MET ALA SER GLN ALA
SEQRES 13 A 208 SER ALA GLU LYS ARG THR GLN LYS GLU ILE GLY ASP ILE
SEQRES 14 A 208 ALA GLY VAL ALA ASP VAL THR ILE ARG GLN SER TYR ARG
SEQRES 15 A 208 LEU ILE TYR PRO ARG ALA PRO ASP LEU PHE PRO THR ASP
SEQRES 16 A 208 PHE LYS PHE ASP THR PRO VAL ASP LYS LEU PRO GLN LEU
HELIX 1 1 ALA A 113 ARG A 127 1 15
HELIX 2 2 ARG A 132 GLN A 144 1 13
HELIX 3 3 ASN A 156 ALA A 167 1 12
HELIX 4 4 PHE A 177 ALA A 182 1 6
HELIX 5 5 LYS A 188 LEU A 202 1 15
HELIX 6 6 PHE A 218 SER A 220 5 3
HELIX 7 7 LYS A 226 LEU A 242 1 17
HELIX 8 8 PRO A 250 ALA A 261 1 12
HELIX 9 9 GLN A 271 ILE A 274 1 4
HELIX 10 10 ASP A 276 ALA A 278 5 3
HELIX 11 11 ASP A 282 ILE A 285 1 4
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 2 2 Bytes