HEADER TRANSCRIPTION 21-MAY-05 2CSH
TITLE SOLUTION STRUCTURE OF TANDEM REPEAT OF THE ZF-C2H2 DOMAINS OF HUMAN
TITLE 2 ZINC FINGER PROTEIN 297B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER PROTEIN 297B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-C2H2 DOMAIN;
COMPND 5 SYNONYM: ZNF-X, ZINC FINGER AND BTB DOMAIN CONTAINING PROTEIN 22B;
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: KAZUSA CDNA HH00161;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P021021-05;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ZF-C2H2 DOMAIN, ZINC FINGER PROTEIN 297B, ZINC FINGER AND BTB DOMAIN
KEYWDS 2 CONTAINING PROTEIN 22B, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 3 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 4 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.INOUE,K.SAITOH,F.HAYASHI,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CSH 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CSH 1 VERSN
REVDAT 1 21-NOV-05 2CSH 0
JRNL AUTH K.INOUE,K.SAITOH,F.HAYASHI,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF TANDEM REPEAT OF THE ZF-C2H2 DOMAINS
JRNL TITL 2 OF HUMAN ZINC FINGER PROTEIN 297B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CSH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024573.
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 : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.18MM U-15N, 13C-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 0.02% NAN3; 0.1MM ZNCL2;
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9296, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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 LEU A 33 166.31 -44.56
REMARK 500 1 THR A 61 149.95 -36.71
REMARK 500 1 ALA A 97 39.23 37.85
REMARK 500 1 ALA A 104 161.22 -41.05
REMARK 500 2 THR A 61 134.30 -36.08
REMARK 500 2 ILE A 63 132.05 -35.45
REMARK 500 2 LYS A 96 152.83 -40.44
REMARK 500 2 GLU A 98 53.43 30.30
REMARK 500 2 GLN A 99 54.62 35.97
REMARK 500 2 THR A 102 46.65 -82.84
REMARK 500 2 SER A 105 141.62 -172.47
REMARK 500 2 PRO A 107 -177.66 -69.76
REMARK 500 3 SER A 5 128.17 -174.66
REMARK 500 3 ASP A 8 136.27 -38.97
REMARK 500 3 LEU A 35 77.85 -119.75
REMARK 500 3 PRO A 65 2.51 -69.76
REMARK 500 3 CYS A 68 173.31 -58.35
REMARK 500 3 CYS A 88 -35.15 -38.59
REMARK 500 3 ALA A 97 47.55 -85.72
REMARK 500 3 ASN A 100 98.53 -38.87
REMARK 500 3 GLU A 103 146.93 -35.65
REMARK 500 3 PRO A 107 -173.23 -69.75
REMARK 500 4 SER A 2 115.80 -169.21
REMARK 500 4 SER A 3 140.78 -170.40
REMARK 500 4 SER A 6 -42.56 -131.18
REMARK 500 4 GLU A 67 141.24 -172.00
REMARK 500 4 PHE A 81 -71.10 -61.84
REMARK 500 4 SER A 87 30.13 -86.27
REMARK 500 4 LYS A 96 164.11 -42.47
REMARK 500 4 THR A 101 140.47 -34.28
REMARK 500 4 THR A 102 102.83 -35.79
REMARK 500 5 SER A 2 146.51 -174.87
REMARK 500 5 LEU A 33 176.37 -49.03
REMARK 500 5 THR A 61 -176.90 -56.68
REMARK 500 5 LYS A 96 166.44 -47.73
REMARK 500 5 THR A 102 85.97 -59.29
REMARK 500 5 PRO A 107 7.90 -69.78
REMARK 500 5 SER A 108 131.72 -28.35
REMARK 500 6 SER A 2 141.21 -174.78
REMARK 500 6 ASP A 8 126.18 -170.56
REMARK 500 6 LEU A 33 170.30 -45.33
REMARK 500 6 THR A 61 121.90 -39.66
REMARK 500 6 CYS A 68 171.04 -53.36
REMARK 500 6 LYS A 90 -38.43 -34.40
REMARK 500 6 GLN A 99 42.31 -104.95
REMARK 500 7 LYS A 17 174.96 -59.01
REMARK 500 7 LEU A 33 45.61 -89.47
REMARK 500 7 LEU A 35 45.27 -97.15
REMARK 500 7 THR A 61 151.33 -40.46
REMARK 500 7 LYS A 64 70.71 -113.38
REMARK 500
REMARK 500 THIS ENTRY HAS 122 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 200 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 13 SG
REMARK 620 2 CYS A 15 SG 110.5
REMARK 620 3 HIS A 28 ND1 106.9 107.1
REMARK 620 4 HIS A 32 NE2 106.6 107.5 118.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 300 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 40 SG
REMARK 620 2 CYS A 43 SG 102.6
REMARK 620 3 HIS A 56 NE2 105.4 105.1
REMARK 620 4 HIS A 60 NE2 108.7 114.4 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 400 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 68 SG
REMARK 620 2 CYS A 71 SG 103.1
REMARK 620 3 HIS A 84 NE2 107.3 105.0
REMARK 620 4 CYS A 88 SG 111.8 111.6 116.9
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 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002000403 RELATED DB: TARGETDB
DBREF 2CSH A 8 104 UNP O43298 Z297B_HUMAN 370 466
SEQADV 2CSH GLY A 1 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 2 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 3 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH GLY A 4 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 5 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 6 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH GLY A 7 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 105 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH GLY A 106 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH PRO A 107 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 108 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH SER A 109 UNP O43298 CLONING ARTIFACT
SEQADV 2CSH GLY A 110 UNP O43298 CLONING ARTIFACT
SEQRES 1 A 110 GLY SER SER GLY SER SER GLY ASP LYS LEU TYR PRO CYS
SEQRES 2 A 110 GLN CYS GLY LYS SER PHE THR HIS LYS SER GLN ARG ASP
SEQRES 3 A 110 ARG HIS MET SER MET HIS LEU GLY LEU ARG PRO TYR GLY
SEQRES 4 A 110 CYS GLY VAL CYS GLY LYS LYS PHE LYS MET LYS HIS HIS
SEQRES 5 A 110 LEU VAL GLY HIS MET LYS ILE HIS THR GLY ILE LYS PRO
SEQRES 6 A 110 TYR GLU CYS ASN ILE CYS ALA LYS ARG PHE MET TRP ARG
SEQRES 7 A 110 ASP SER PHE HIS ARG HIS VAL THR SER CYS THR LYS SER
SEQRES 8 A 110 TYR GLU ALA ALA LYS ALA GLU GLN ASN THR THR GLU ALA
SEQRES 9 A 110 SER GLY PRO SER SER GLY
HET ZN A 200 1
HET ZN A 300 1
HET ZN A 400 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
HELIX 1 1 HIS A 21 LEU A 33 1 13
HELIX 2 2 LYS A 50 LYS A 58 1 9
HELIX 3 3 TRP A 77 ALA A 97 1 21
SHEET 1 A 2 TYR A 11 PRO A 12 0
SHEET 2 A 2 SER A 18 PHE A 19 -1 O PHE A 19 N TYR A 11
SHEET 1 B 2 TYR A 38 GLY A 39 0
SHEET 2 B 2 LYS A 46 PHE A 47 -1 O PHE A 47 N TYR A 38
SHEET 1 C 2 TYR A 66 GLU A 67 0
SHEET 2 C 2 ARG A 74 PHE A 75 -1 O PHE A 75 N TYR A 66
LINK SG CYS A 13 ZN ZN A 200 1555 1555 2.35
LINK SG CYS A 15 ZN ZN A 200 1555 1555 2.30
LINK ND1 HIS A 28 ZN ZN A 200 1555 1555 2.05
LINK NE2 HIS A 32 ZN ZN A 200 1555 1555 2.04
LINK SG CYS A 40 ZN ZN A 300 1555 1555 2.35
LINK SG CYS A 43 ZN ZN A 300 1555 1555 2.35
LINK NE2 HIS A 56 ZN ZN A 300 1555 1555 2.05
LINK NE2 HIS A 60 ZN ZN A 300 1555 1555 2.05
LINK SG CYS A 68 ZN ZN A 400 1555 1555 2.35
LINK SG CYS A 71 ZN ZN A 400 1555 1555 2.35
LINK NE2 HIS A 84 ZN ZN A 400 1555 1555 2.05
LINK SG CYS A 88 ZN ZN A 400 1555 1555 2.05
SITE 1 AC1 4 CYS A 13 CYS A 15 HIS A 28 HIS A 32
SITE 1 AC2 4 CYS A 40 CYS A 43 HIS A 56 HIS A 60
SITE 1 AC3 4 CYS A 68 CYS A 71 HIS A 84 CYS A 88
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
