HEADER TRANSCRIPTION 22-FEB-08 2K16
TITLE SOLUTION STRUCTURE OF THE FREE TAF3 PHD DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PLANTHOMEODOMAIN FINGER;
COMPND 5 SYNONYM: TBP-ASSOCIATED FACTOR 3, TRANSCRIPTION INITIATION FACTOR
COMPND 6 TFIID 140 KDA SUBUNIT, 140 KDA TATA BOX-BINDING PROTEIN-ASSOCIATED
COMPND 7 FACTOR, TAF140, TAFII140;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 GENE: TAF3;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PROTEIN, ALTERNATIVE SPLICING, METAL-BINDING, NUCLEUS,
KEYWDS 2 PHOSPHOPROTEIN, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC, ZINC-
KEYWDS 3 FINGER
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.VAN INGEN,F.M.A.VAN SCHAIK,H.WIENK,M.TIMMERS,R.BOELENS
REVDAT 4 14-JUN-23 2K16 1 REMARK
REVDAT 3 19-FEB-20 2K16 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2K16 1 VERSN
REVDAT 1 15-JUL-08 2K16 0
JRNL AUTH H.VAN INGEN,F.M.A.VAN SCHAIK,H.WIENK,J.BALLERING,
JRNL AUTH 2 A.DESCHESNE,J.KRUIJZER,H.TIMMERS,R.BOELENS
JRNL TITL RECOGNITION OF THE H3K4ME3 MARK BY THE TAF3-PHD FINGER
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER, ADAMS, CLORE, GROS, NILGES AND READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT IN EXPLICIT SOLVENT USING
REMARK 3 RECOORD PROTOCOL
REMARK 4
REMARK 4 2K16 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000100545.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 150 MM [U-13C; U-15N] TAF3_PHD,
REMARK 210 150 MM POTASSIUM CHLORIDE, 20 MM
REMARK 210 POTASSIUM PHOSPHATE, 0.01 MM
REMARK 210 ZNCL2, 95% H2O/5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D 1H-13C
REMARK 210 NOESY; 2D 1H-1H NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 700 MHZ; 600
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA, NMRPIPE, SPARKY
REMARK 210 METHOD USED : SIMULATED 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: 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 ASN A 874 24.00 82.29
REMARK 500 1 LYS A 919 -68.76 71.40
REMARK 500 1 LYS A 920 -50.96 -176.91
REMARK 500 2 ALA A 856 -150.72 60.37
REMARK 500 2 ASN A 874 21.86 82.50
REMARK 500 2 ASP A 921 134.68 71.02
REMARK 500 3 HIS A 852 103.18 -166.57
REMARK 500 3 TYR A 857 64.25 -108.53
REMARK 500 3 ASP A 921 -83.10 67.75
REMARK 500 4 SER A 851 83.63 43.21
REMARK 500 4 PRO A 871 13.60 -67.39
REMARK 500 4 CYS A 888 -95.06 -105.55
REMARK 500 4 ASP A 889 -20.46 174.62
REMARK 500 4 ALA A 902 96.35 -44.64
REMARK 500 4 GLU A 906 -20.24 148.65
REMARK 500 4 GLN A 908 152.52 -46.98
REMARK 500 4 LYS A 920 -45.78 -146.16
REMARK 500 5 HIS A 852 -70.11 65.41
REMARK 500 5 ALA A 854 -163.38 -167.40
REMARK 500 5 ALA A 856 -88.52 -68.15
REMARK 500 5 PRO A 912 -9.97 -59.92
REMARK 500 6 MET A 853 34.96 -155.59
REMARK 500 6 PRO A 871 2.88 -63.30
REMARK 500 6 LYS A 919 81.47 70.09
REMARK 500 6 ASP A 921 86.86 59.98
REMARK 500 7 SER A 851 13.75 -149.11
REMARK 500 7 HIS A 852 -84.48 -79.03
REMARK 500 7 MET A 855 24.71 -147.94
REMARK 500 7 ASN A 874 26.26 87.55
REMARK 500 7 CYS A 888 -143.93 -119.12
REMARK 500 7 TRP A 891 117.30 -161.09
REMARK 500 7 ALA A 902 96.70 -39.21
REMARK 500 7 GLU A 906 -20.47 150.92
REMARK 500 7 LYS A 919 -75.19 -64.75
REMARK 500 7 LYS A 920 108.14 -173.92
REMARK 500 8 PRO A 871 0.25 -63.17
REMARK 500 8 ASN A 874 29.51 80.63
REMARK 500 8 LYS A 920 -59.33 -139.16
REMARK 500 8 ASP A 921 82.64 48.37
REMARK 500 9 PRO A 871 1.35 -65.01
REMARK 500 9 CYS A 888 -92.86 -107.70
REMARK 500 9 ASP A 889 -30.78 179.62
REMARK 500 9 LYS A 919 118.77 52.76
REMARK 500 10 SER A 851 -174.20 61.82
REMARK 500 10 ASN A 874 39.78 80.45
REMARK 500 10 ASP A 889 79.54 80.01
REMARK 500 10 ALA A 901 145.81 -173.95
REMARK 500 10 GLU A 906 -11.41 149.80
REMARK 500 10 GLN A 908 157.99 -45.70
REMARK 500 10 ILE A 918 -60.62 -94.72
REMARK 500
REMARK 500 THIS ENTRY HAS 105 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 941 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 870 SG
REMARK 620 2 CYS A 873 SG 112.2
REMARK 620 3 HIS A 893 ND1 108.6 106.4
REMARK 620 4 CYS A 896 SG 113.8 109.8 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 940 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 885 SG
REMARK 620 2 CYS A 888 SG 108.0
REMARK 620 3 CYS A 911 SG 110.0 111.1
REMARK 620 4 CYS A 914 SG 110.9 110.8 106.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 940
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 941
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 15670 RELATED DB: BMRB
REMARK 900 RELATED ID: 2K17 RELATED DB: PDB
DBREF 2K16 A 857 924 UNP Q5HZG4 TAF3_MOUSE 857 924
SEQADV 2K16 GLY A 850 UNP Q5HZG4 EXPRESSION TAG
SEQADV 2K16 SER A 851 UNP Q5HZG4 EXPRESSION TAG
SEQADV 2K16 HIS A 852 UNP Q5HZG4 EXPRESSION TAG
SEQADV 2K16 MET A 853 UNP Q5HZG4 EXPRESSION TAG
SEQADV 2K16 ALA A 854 UNP Q5HZG4 EXPRESSION TAG
SEQADV 2K16 MET A 855 UNP Q5HZG4 EXPRESSION TAG
SEQADV 2K16 ALA A 856 UNP Q5HZG4 EXPRESSION TAG
SEQRES 1 A 75 GLY SER HIS MET ALA MET ALA TYR VAL ILE ARG ASP GLU
SEQRES 2 A 75 TRP GLY ASN GLN ILE TRP ILE CYS PRO GLY CYS ASN LYS
SEQRES 3 A 75 PRO ASP ASP GLY SER PRO MET ILE GLY CYS ASP ASP CYS
SEQRES 4 A 75 ASP ASP TRP TYR HIS TRP PRO CYS VAL GLY ILE MET ALA
SEQRES 5 A 75 ALA PRO PRO GLU GLU MET GLN TRP PHE CYS PRO LYS CYS
SEQRES 6 A 75 ALA ASN LYS ILE LYS LYS ASP LYS LYS HIS
HET ZN A 940 1
HET ZN A 941 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 TRP A 894 GLY A 898 1 5
HELIX 2 2 CYS A 914 LYS A 919 1 6
SHEET 1 A 2 VAL A 858 ARG A 860 0
SHEET 2 A 2 GLN A 866 TRP A 868 -1 O ILE A 867 N ILE A 859
SHEET 1 B 2 MET A 882 GLY A 884 0
SHEET 2 B 2 TRP A 891 HIS A 893 -1 O TYR A 892 N ILE A 883
LINK SG CYS A 870 ZN ZN A 941 1555 1555 2.23
LINK SG CYS A 873 ZN ZN A 941 1555 1555 2.22
LINK SG CYS A 885 ZN ZN A 940 1555 1555 2.30
LINK SG CYS A 888 ZN ZN A 940 1555 1555 2.28
LINK ND1 HIS A 893 ZN ZN A 941 1555 1555 2.23
LINK SG CYS A 896 ZN ZN A 941 1555 1555 2.29
LINK SG CYS A 911 ZN ZN A 940 1555 1555 2.37
LINK SG CYS A 914 ZN ZN A 940 1555 1555 2.28
SITE 1 AC1 5 CYS A 885 ASP A 887 CYS A 888 TYR A 892
SITE 2 AC1 5 LYS A 913
SITE 1 AC2 4 ILE A 869 CYS A 870 CYS A 873 LYS A 875
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
