Header list of 1nha.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 19-DEC-02 1NHA
TITLE SOLUTION STRUCTURE OF THE CARBOXYL-TERMINAL DOMAIN OF RAP74 AND NMR
TITLE 2 CHARACTERIZATION OF THE FCP-BINDING SITES OF RAP74 AND CTD OF RAP74,
TITLE 3 THE SUBUNIT OF HUMAN TFIIF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION INITIATION FACTOR IIF, ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: TFIIF-ALPHA;
COMPND 6 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: RAP74;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: GST-2T
KEYWDS TRANSCRIPTION FACTOR, HUMAN GENERAL TRANSCRIPTION FACTOR TFIIF,
KEYWDS 2 RAP74, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.D.NGUYEN,H.T.CHEN,M.S.KOBOR,J.GREENBLATT,P.LEGAULT,J.G.OMICHINSKI
REVDAT 3 23-FEB-22 1NHA 1 REMARK
REVDAT 2 24-FEB-09 1NHA 1 VERSN
REVDAT 1 25-FEB-03 1NHA 0
JRNL AUTH B.D.NGUYEN,H.T.CHEN,M.S.KOBOR,J.GREENBLATT,P.LEGAULT,
JRNL AUTH 2 J.G.OMICHINSKI
JRNL TITL SOLUTION STRUCTURE OF THE CARBOXYL-TERMINAL DOMAIN OF RAP74
JRNL TITL 2 AND NMR CHARACTERIZATION OF THE FCP1-BINDING SITES OF RAP74
JRNL TITL 3 AND HUMAN TFIIB.
JRNL REF BIOCHEMISTRY V. 42 1460 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12578358
JRNL DOI 10.1021/BI0265473
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, CNS MODIFIED CNS WITH CONFORMATIONAL
REMARK 3 DATABASE POTENTIAL
REMARK 3 AUTHORS : BRUNGER (CNS), KAY AND CHOY, CLORES (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1063 RESTRAINTS, 959 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 104 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1NHA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000017871.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM CTERRAP74 UNLABELED, 20MM
REMARK 210 SODIUM PHOSPHATE, AND 1MM EDTA;
REMARK 210 1MM CTERRAP74 U-15N, 20MM SODIUM
REMARK 210 PHOSPHATE, AND 1MM EDTA; 1MM
REMARK 210 CTERRAP74 U-15N AND U-13C, 20MM
REMARK 210 SODIUM PHOSPHATE, AND 1MM EDTA;
REMARK 210 1MM CTERRAP74 U-15N AND U-13C,
REMARK 210 20MM SODIUM PHOSPHATE, AND 1MM
REMARK 210 EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_15N/13C-
REMARK 210 SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE NULL, PIPP NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 67
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS,STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY
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 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 SER A 436
REMARK 465 THR A 437
REMARK 465 PRO A 438
REMARK 465 GLN A 439
REMARK 465 PRO A 440
REMARK 465 PRO A 441
REMARK 465 SER A 442
REMARK 465 GLY A 443
REMARK 465 LYS A 444
REMARK 465 THR A 445
REMARK 465 THR A 446
REMARK 465 PRO A 447
REMARK 465 ASN A 448
REMARK 465 SER A 449
REMARK 465 GLY A 450
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 ASN A 501 60.01 60.58
REMARK 500 2 LYS A 480 -63.28 -176.47
REMARK 500 2 LYS A 481 -47.17 -142.61
REMARK 500 5 LYS A 481 86.84 -62.73
REMARK 500 6 LYS A 480 -74.92 -157.83
REMARK 500 6 LYS A 481 -46.17 -140.55
REMARK 500 7 THR A 479 75.80 -157.29
REMARK 500 7 LYS A 481 85.42 -61.17
REMARK 500 8 THR A 479 86.56 -153.19
REMARK 500 9 THR A 482 -39.19 -178.45
REMARK 500 10 LYS A 480 -70.17 -85.24
REMARK 500 10 LYS A 481 33.08 -169.07
REMARK 500 11 PHE A 477 30.59 -98.33
REMARK 500 12 LYS A 481 -43.32 -168.23
REMARK 500 13 THR A 479 73.30 -173.11
REMARK 500 13 LYS A 480 -75.10 -90.03
REMARK 500 13 LYS A 481 31.49 -161.15
REMARK 500 14 THR A 479 30.71 -97.93
REMARK 500 15 THR A 479 76.41 179.08
REMARK 500 15 GLU A 503 -176.31 49.45
REMARK 500 17 LYS A 481 81.30 -63.75
REMARK 500 18 THR A 482 -44.08 -160.04
REMARK 500 19 PHE A 477 64.54 -110.49
REMARK 500 19 GLN A 478 -63.34 -103.77
REMARK 500 20 PHE A 477 64.51 -103.08
REMARK 500 20 GLN A 478 -42.89 -169.40
REMARK 500 20 LYS A 480 -79.84 -70.99
REMARK 500 20 LYS A 481 82.85 178.46
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1NHA A 436 517 UNP P35269 T2FA_HUMAN 436 517
SEQRES 1 A 82 SER THR PRO GLN PRO PRO SER GLY LYS THR THR PRO ASN
SEQRES 2 A 82 SER GLY ASP VAL GLN VAL THR GLU ASP ALA VAL ARG ARG
SEQRES 3 A 82 TYR LEU THR ARG LYS PRO MET THR THR LYS ASP LEU LEU
SEQRES 4 A 82 LYS LYS PHE GLN THR LYS LYS THR GLY LEU SER SER GLU
SEQRES 5 A 82 GLN THR VAL ASN VAL LEU ALA GLN ILE LEU LYS ARG LEU
SEQRES 6 A 82 ASN PRO GLU ARG LYS MET ILE ASN ASP LYS MET HIS PHE
SEQRES 7 A 82 SER LEU LYS GLU
HELIX 1 1 THR A 455 LYS A 466 1 12
HELIX 2 2 THR A 469 PHE A 477 1 9
HELIX 3 3 SER A 485 ASN A 501 1 17
SHEET 1 A 2 GLU A 503 ILE A 507 0
SHEET 2 A 2 LYS A 510 SER A 514 -1 O HIS A 512 N LYS A 505
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