HEADER TRANSCRIPTION 29-JUL-16 5GOW
TITLE SOLUTION STRUCTURE OF THE COMPLEX BETWEEN DP1 ACIDIC REGION AND TFIIH
TITLE 2 P62 PH DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DP1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 1;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: UNP RESIDUES 1-108;
COMPND 9 SYNONYM: BASIC TRANSCRIPTION FACTOR 2 62 KDA SUBUNIT,BTF2 P62,GENERAL
COMPND 10 TRANSCRIPTION FACTOR IIH POLYPEPTIDE 1,TFIIH BASAL TRANSCRIPTION
COMPND 11 FACTOR COMPLEX P62 SUBUNIT;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 7 ORGANISM_COMMON: HUMAN;
SOURCE 8 ORGANISM_TAXID: 9606;
SOURCE 9 GENE: GTF2H1, BTF2;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSCRIPTION FACTOR, GENERAL TRANSCRIPTION FACTOR, CELL CYCLE,
KEYWDS 2 TRANSCRIPTION ACTIVATION, SOLUTION STRUCTURE, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.OKUDA,Y.NISHIMURA
REVDAT 2 14-DEC-16 5GOW 1 JRNL
REVDAT 1 07-DEC-16 5GOW 0
JRNL AUTH M.OKUDA,K.ARAKI,K.OHTANI,Y.NISHIMURA
JRNL TITL THE INTERACTION MODE OF THE ACIDIC REGION OF THE CELL CYCLE
JRNL TITL 2 TRANSCRIPTION FACTOR DP1 WITH TFIIH
JRNL REF J. MOL. BIOL. V. 428 4993 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27825926
JRNL DOI 10.1016/J.JMB.2016.11.001
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR_NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5GOW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1300001191.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.02
REMARK 210 PRESSURE : 760 TORR
REMARK 210 SAMPLE CONTENTS : 0.35 MM [U-99% 13C; U-99% 15N]
REMARK 210 DP1, 0.42 MM TFIIH P62, 90% H2O/
REMARK 210 10% D2O; 0.35 MM [U-99% 13C; U-
REMARK 210 99% 15N] DP1, 0.42 MM TFIIH P62,
REMARK 210 100% D2O; 0.35 MM [U-99% 13C; U-
REMARK 210 99% 15N] TFIIH P62, 0.42 MM DP1,
REMARK 210 90% H2O/10% D2O; 0.35 MM [U-99%
REMARK 210 13C; U-99% 15N] TFIIH P62, 0.42
REMARK 210 MM DP1, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 2D 1H-13C HSQC AROMATIC; 3D
REMARK 210 CBCA(CO)NH; 3D HNCO; 3D HBHA(CO)
REMARK 210 NH; 3D C(CO)NH; 3D H(CCO)NH; 3D
REMARK 210 1H-15N NOESY; 3D 1H-13C NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 950 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCEIII
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRDRAW, NMRVIEW, X-PLOR_NIH,
REMARK 210 MOLMOL, PROCHECKNMR
REMARK 210 METHOD USED : DGSA-DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 GLY B -1
REMARK 465 SER B 0
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 HB2 LYS B 54 HG2 GLN B 66 1.27
REMARK 500 HD11 ILE B 31 HD12 LEU B 67 1.33
REMARK 500 HG3 GLU A 399 HE2 LYS B 62 1.34
REMARK 500 H1 TYR A 392 OD1 ASP A 396 1.52
REMARK 500 HZ1 LYS B 13 OE2 GLU B 88 1.55
REMARK 500 OE1 GLU A 398 HZ2 LYS B 62 1.55
REMARK 500 OD2 ASP A 396 HZ1 LYS B 19 1.56
REMARK 500 OD2 ASP A 409 HZ3 LYS B 51 1.56
REMARK 500 OXT ASP A 410 HZ2 LYS B 51 1.57
REMARK 500 HZ2 LYS B 14 OD1 ASP B 21 1.58
REMARK 500 H MET B 1 OE1 GLU B 29 1.59
REMARK 500 O LEU B 65 H PHE B 77 1.59
REMARK 500 HG1 THR B 84 OE1 GLU B 88 1.60
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 GLU A 398 -79.25 169.21
REMARK 500 1 ASP A 401 -49.49 -139.09
REMARK 500 1 ASN A 406 -22.22 -164.28
REMARK 500 1 GLU A 408 -174.40 75.82
REMARK 500 1 ALA B 2 61.86 -160.63
REMARK 500 1 THR B 3 -68.07 -156.64
REMARK 500 1 LYS B 14 75.96 18.15
REMARK 500 1 LYS B 18 50.88 71.22
REMARK 500 2 GLU A 395 157.42 75.40
REMARK 500 2 GLU A 398 -62.01 172.86
REMARK 500 2 ASP A 401 -45.34 -138.42
REMARK 500 2 GLU A 405 -76.32 -72.34
REMARK 500 2 GLU A 408 -139.21 51.45
REMARK 500 2 ASP A 409 -163.66 -109.38
REMARK 500 2 SER B 5 47.07 -152.02
REMARK 500 2 LYS B 14 74.36 17.94
REMARK 500 2 CYS B 52 -178.16 -178.38
REMARK 500 3 GLU A 398 -96.13 175.19
REMARK 500 3 ASP A 401 -46.99 -139.48
REMARK 500 3 ASN A 406 -27.42 85.64
REMARK 500 3 GLU A 408 -159.92 62.41
REMARK 500 3 ALA B 2 -146.28 -159.80
REMARK 500 3 GLU B 6 36.40 72.59
REMARK 500 3 LYS B 14 79.68 18.10
REMARK 500 3 LYS B 104 109.08 -59.43
REMARK 500 4 VAL A 393 142.20 -170.24
REMARK 500 4 GLU A 398 -69.54 169.77
REMARK 500 4 ASP A 401 -48.62 -138.45
REMARK 500 4 ASP A 402 6.89 -67.98
REMARK 500 4 GLU A 408 98.60 -50.61
REMARK 500 4 SER B 5 74.77 61.32
REMARK 500 4 LYS B 14 70.10 18.44
REMARK 500 5 ASP A 397 16.88 -64.30
REMARK 500 5 GLU A 398 -77.65 96.16
REMARK 500 5 ASP A 400 77.12 177.70
REMARK 500 5 ASP A 401 -54.20 -139.04
REMARK 500 5 ASP A 402 11.50 -69.90
REMARK 500 5 ASN A 406 -37.02 79.23
REMARK 500 5 GLU A 408 -103.04 51.84
REMARK 500 5 ALA B 2 127.75 -174.23
REMARK 500 5 SER B 4 -47.24 -158.38
REMARK 500 5 LYS B 14 72.78 18.17
REMARK 500 5 ARG B 105 46.59 -89.02
REMARK 500 6 GLU A 398 -84.33 165.25
REMARK 500 6 ASP A 401 -50.31 -138.75
REMARK 500 6 ASN A 406 45.63 175.58
REMARK 500 6 GLU A 408 -170.02 -178.35
REMARK 500 6 ASP A 409 57.98 -175.07
REMARK 500 6 THR B 3 -30.71 -130.27
REMARK 500 6 SER B 4 -153.36 -151.26
REMARK 500
REMARK 500 THIS ENTRY HAS 201 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 36013 RELATED DB: BMRB
DBREF 5GOW A 392 410 PDB 5GOW 5GOW 392 410
DBREF 5GOW B 1 108 UNP P32780 TF2H1_HUMAN 1 108
SEQADV 5GOW GLY B -1 UNP P32780 EXPRESSION TAG
SEQADV 5GOW SER B 0 UNP P32780 EXPRESSION TAG
SEQRES 1 A 19 TYR VAL GLY GLU ASP ASP GLU GLU ASP ASP ASP PHE ASN
SEQRES 2 A 19 GLU ASN ASP GLU ASP ASP
SEQRES 1 B 110 GLY SER MET ALA THR SER SER GLU GLU VAL LEU LEU ILE
SEQRES 2 B 110 VAL LYS LYS VAL ARG GLN LYS LYS GLN ASP GLY ALA LEU
SEQRES 3 B 110 TYR LEU MET ALA GLU ARG ILE ALA TRP ALA PRO GLU GLY
SEQRES 4 B 110 LYS ASP ARG PHE THR ILE SER HIS MET TYR ALA ASP ILE
SEQRES 5 B 110 LYS CYS GLN LYS ILE SER PRO GLU GLY LYS ALA LYS ILE
SEQRES 6 B 110 GLN LEU GLN LEU VAL LEU HIS ALA GLY ASP THR THR ASN
SEQRES 7 B 110 PHE HIS PHE SER ASN GLU SER THR ALA VAL LYS GLU ARG
SEQRES 8 B 110 ASP ALA VAL LYS ASP LEU LEU GLN GLN LEU LEU PRO LYS
SEQRES 9 B 110 PHE LYS ARG LYS ALA ASN
HELIX 1 1 TYR B 47 ASP B 49 5 3
HELIX 2 2 THR B 84 LYS B 104 1 21
SHEET 1 A 7 THR B 42 MET B 46 0
SHEET 2 A 7 ARG B 30 ALA B 34 -1 N ILE B 31 O HIS B 45
SHEET 3 A 7 ASP B 21 MET B 27 -1 N ALA B 23 O ALA B 34
SHEET 4 A 7 LEU B 9 ARG B 16 -1 N VAL B 12 O LEU B 24
SHEET 5 A 7 ASP B 73 PHE B 79 -1 O HIS B 78 N ARG B 16
SHEET 6 A 7 ILE B 63 LEU B 69 -1 N LEU B 65 O PHE B 77
SHEET 7 A 7 ILE B 50 SER B 56 -1 N CYS B 52 O VAL B 68
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
