HEADER TRANSCRIPTION 10-JAN-12 2LO3
TITLE SOLUTION STRUCTURE OF SGF73(59-102) ZINC FINGER DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SAGA-ASSOCIATED FACTOR 73;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 59-102;
COMPND 5 SYNONYM: 73 KDA SAGA-ASSOCIATED FACTOR, SAGA HISTONE
COMPND 6 ACETYLTRANSFERASE COMPLEX 73 KDA SUBUNIT;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: SGF73, YGL066W;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PGEX4T1
KEYWDS ZINC-FINGER, DEUBIQUITINATION, TRANSCRIPTION FACTOR, SAGA COMPLEX,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.GAO,C.KOEHLER,J.BONNET,D.DEVYS,B.KIEFFER
REVDAT 2 14-JUN-23 2LO3 1 REMARK LINK
REVDAT 1 25-JAN-12 2LO3 0
JRNL AUTH C.KOEHLER,X.GAO,J.BONNET,D.DEVYS,B.KIEFFER
JRNL TITL INSIGHTS INTO THE ROLE OF SGF11 AND SGF73 FOR THE
JRNL TITL 2 INTERACTION BETWEEN SAGA AND NUCLEOSOMES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN, CNS
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), BRUNGER, ADAMS, CLORE,
REMARK 3 GROS, NILGES AND READ (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RECOORD SCRIPTS
REMARK 4
REMARK 4 2LO3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000102621.
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 : 0.175
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.2 MM [U-98% 15N] SGF73, 50 MM
REMARK 210 SODIUM PHOSPHATE, 100 MM SODIUM
REMARK 210 CHLORIDE, 0.05 MM TCEP, 10 % D2O,
REMARK 210 90% H2O/10% D2O; 1 MM [U-99%
REMARK 210 13C; U-98% 15N] SGF73, 20 MM
REMARK 210 SODIUM PHOSPHATE, 75 MM SODIUM
REMARK 210 CHLORIDE, 1 MM DTT, 10 % D2O, 90%
REMARK 210 H2O/10% D2O; 0.2 MM [U-98% 15N]
REMARK 210 SGF73, 50 MM SODIUM PHOSPHATE,
REMARK 210 100 MM SODIUM CHLORIDE, 0.05 MM
REMARK 210 TCEP, 100 % D2O, 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-1H NOESY;
REMARK 210 2D 1H-1H TOCSY; 2D 1H-1H COSY;
REMARK 210 2D 1H-13C HSQC ALIPHATIC; 3D
REMARK 210 CBCA(CO)NH; 3D HNCO; 3D HNCA; 3D
REMARK 210 HNCACB; 3D HCCH-TOCSY; 3D HNCACO;
REMARK 210 3D HN(CO)CA; 2D 1H-15N HSQC R1
REMARK 210 EDITED; 2D 1H-15N HSQC R2 EDITED;
REMARK 210 2D 1H-15N HETERONUCLEAR NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 600 MHZ; 950 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW, CYANA, TALOS,
REMARK 210 SPARKY
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: 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
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 ASP A 12 51.63 -104.80
REMARK 500 3 ALA A 4 -164.38 -104.88
REMARK 500 4 ASN A 3 -66.82 -103.70
REMARK 500 4 ALA A 4 -48.67 -160.56
REMARK 500 4 ASP A 12 -61.63 66.62
REMARK 500 5 PRO A 2 48.92 -92.83
REMARK 500 5 ASN A 3 -60.12 74.74
REMARK 500 5 ALA A 4 -70.98 -144.61
REMARK 500 6 ASP A 12 134.59 162.79
REMARK 500 10 PRO A 2 88.63 -68.55
REMARK 500 11 ALA A 4 -42.98 -145.90
REMARK 500 11 ASP A 12 -167.91 -115.24
REMARK 500 13 ASP A 12 -51.26 69.60
REMARK 500 16 ASN A 3 174.32 72.92
REMARK 500 16 ALA A 43 106.25 -55.26
REMARK 500 18 ALA A 4 145.83 69.72
REMARK 500 20 ALA A 4 95.66 53.91
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 7 ARG A 18 0.10 SIDE CHAIN
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 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 20 SG
REMARK 620 2 CYS A 23 SG 109.6
REMARK 620 3 HIS A 35 NE2 110.8 110.6
REMARK 620 4 HIS A 39 ND1 109.9 110.2 105.6
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 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18192 RELATED DB: BMRB
REMARK 900 RELATED ID: 2LO2 RELATED DB: PDB
DBREF 2LO3 A 1 44 UNP P53165 SGF73_YEAST 59 102
SEQRES 1 A 44 ASN PRO ASN ALA GLN LEU ILE GLU ASP PRO LEU ASP LYS
SEQRES 2 A 44 PRO ILE GLN TYR ARG VAL CYS GLU LYS CYS GLY LYS PRO
SEQRES 3 A 44 LEU ALA LEU THR ALA ILE VAL ASP HIS LEU GLU ASN HIS
SEQRES 4 A 44 CYS ALA GLY ALA SER
HET ZN A 101 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ALA A 31 HIS A 39 1 9
SHEET 1 A 2 TYR A 17 VAL A 19 0
SHEET 2 A 2 PRO A 26 ALA A 28 -1 O LEU A 27 N ARG A 18
LINK SG CYS A 20 ZN ZN A 101 1555 1555 2.35
LINK SG CYS A 23 ZN ZN A 101 1555 1555 2.33
LINK NE2 HIS A 35 ZN ZN A 101 1555 1555 2.09
LINK ND1 HIS A 39 ZN ZN A 101 1555 1555 2.10
SITE 1 AC1 4 CYS A 20 CYS A 23 HIS A 35 HIS A 39
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
