Header list of 1x6h.pdb file
Complete list - r 2 2 Bytes
HEADER DNA BINDING PROTEIN 17-MAY-05 1X6H
TITLE SOLUTION STRUCTURES OF THE C2H2 TYPE ZINC FINGER DOMAIN OF HUMAN
TITLE 2 TRANSCRIPTIONAL REPRESSOR CTCF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REPRESSOR CTCF;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C2H2 TYPE ZINC FINGER DOMAIN;
COMPND 5 SYNONYM: CCCTC-BINDING FACTOR, CTCFL PARALOG, 11-ZINC FINGER PROTEIN;
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: CTCF;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040719-09;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ZINC FINGER PROTEIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SATO,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X6H 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1X6H 1 VERSN
REVDAT 1 17-NOV-05 1X6H 0
JRNL AUTH M.SATO,K.SAITO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE C2H2 TYPE ZINC FINGER DOMAIN OF
JRNL TITL 2 HUMAN TRANSCRIPTIONAL REPRESSOR CTCF
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X6H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024439.
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 : 1.5MM C2H2 TYPE ZINC FINGER
REMARK 210 DOMAIN U-15N,13C; 20MM D-TRIS
REMARK 210 HCL; 100MM NACL; 5MM D-DTT; 0.02%
REMARK 210 NAN3; 10UM ZNCL2; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 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 0.9295, 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 LEAST RESTRAINT 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 SER A 3 42.10 35.05
REMARK 500 1 HIS A 10 107.13 -163.76
REMARK 500 1 GLU A 13 105.32 -41.69
REMARK 500 1 LYS A 14 106.90 -40.94
REMARK 500 1 ASP A 22 49.32 -97.55
REMARK 500 1 ARG A 37 -61.39 -97.08
REMARK 500 1 PRO A 41 1.57 -69.75
REMARK 500 1 CYS A 50 174.70 -54.04
REMARK 500 1 SER A 81 136.45 -170.36
REMARK 500 2 SER A 5 43.33 34.32
REMARK 500 2 GLU A 13 108.89 -167.01
REMARK 500 2 ASP A 22 45.62 -96.16
REMARK 500 2 ARG A 37 -62.60 -96.10
REMARK 500 2 PRO A 41 2.08 -69.78
REMARK 500 2 SER A 81 118.97 -35.99
REMARK 500 3 THR A 11 41.99 -100.60
REMARK 500 3 LYS A 14 106.56 -49.69
REMARK 500 3 ASP A 22 53.68 -103.04
REMARK 500 3 ARG A 37 -62.32 -97.07
REMARK 500 3 PRO A 83 -177.01 -69.80
REMARK 500 4 SER A 2 112.91 -168.29
REMARK 500 4 ARG A 37 -62.11 -97.10
REMARK 500 4 PRO A 41 2.35 -69.82
REMARK 500 4 GLU A 77 -61.15 -126.80
REMARK 500 4 ASN A 80 139.25 -174.72
REMARK 500 5 HIS A 10 42.01 -99.67
REMARK 500 5 LYS A 14 102.45 -41.79
REMARK 500 5 ASP A 22 51.07 -97.43
REMARK 500 5 ARG A 37 -62.38 -96.81
REMARK 500 5 PRO A 41 2.97 -69.73
REMARK 500 5 CYS A 50 174.07 -50.60
REMARK 500 6 ASP A 22 47.58 -102.98
REMARK 500 6 ARG A 37 -62.53 -96.63
REMARK 500 6 PRO A 41 2.87 -69.70
REMARK 500 6 PRO A 73 95.61 -69.75
REMARK 500 6 GLU A 77 -42.39 -133.42
REMARK 500 7 ASP A 22 52.32 -98.30
REMARK 500 7 ARG A 37 -61.51 -97.03
REMARK 500 7 CYS A 50 168.22 -45.72
REMARK 500 7 ALA A 71 -35.80 -134.17
REMARK 500 7 ASP A 74 41.35 36.51
REMARK 500 7 SER A 81 141.84 -34.74
REMARK 500 8 HIS A 10 131.77 -37.14
REMARK 500 8 ASP A 22 43.57 -99.14
REMARK 500 8 ARG A 37 -60.90 -96.47
REMARK 500 8 CYS A 50 172.01 -54.45
REMARK 500 8 THR A 58 33.25 -88.68
REMARK 500 9 ASP A 22 51.80 -100.86
REMARK 500 9 ARG A 37 -62.36 -97.22
REMARK 500 9 PRO A 41 1.19 -69.81
REMARK 500
REMARK 500 THIS ENTRY HAS 125 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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 18 SG
REMARK 620 2 CYS A 21 SG 110.5
REMARK 620 3 HIS A 34 NE2 115.5 86.8
REMARK 620 4 HIS A 39 NE2 108.8 117.4 116.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 50 SG
REMARK 620 2 CYS A 53 SG 117.8
REMARK 620 3 HIS A 66 NE2 98.3 113.6
REMARK 620 4 CYS A 70 SG 117.7 112.2 93.4
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000882.1 RELATED DB: TARGETDB
DBREF 1X6H A 8 80 UNP P49711 CTCF_HUMAN 515 587
SEQADV 1X6H GLY A 1 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 2 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 3 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H GLY A 4 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 5 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 6 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H GLY A 7 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 81 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H GLY A 82 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H PRO A 83 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 84 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H SER A 85 UNP P49711 CLONING ARTIFACT
SEQADV 1X6H GLY A 86 UNP P49711 CLONING ARTIFACT
SEQRES 1 A 86 GLY SER SER GLY SER SER GLY ARG THR HIS THR GLY GLU
SEQRES 2 A 86 LYS PRO TYR ALA CYS SER HIS CYS ASP LYS THR PHE ARG
SEQRES 3 A 86 GLN LYS GLN LEU LEU ASP MET HIS PHE LYS ARG TYR HIS
SEQRES 4 A 86 ASP PRO ASN PHE VAL PRO ALA ALA PHE VAL CYS SER LYS
SEQRES 5 A 86 CYS GLY LYS THR PHE THR ARG ARG ASN THR MET ALA ARG
SEQRES 6 A 86 HIS ALA ASP ASN CYS ALA GLY PRO ASP GLY VAL GLU GLY
SEQRES 7 A 86 GLU ASN SER GLY PRO SER SER GLY
HET ZN A 201 1
HET ZN A 401 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLN A 27 TYR A 38 1 12
HELIX 2 2 ARG A 59 CYS A 70 1 12
SHEET 1 A 2 TYR A 16 ALA A 17 0
SHEET 2 A 2 THR A 24 PHE A 25 -1 O PHE A 25 N TYR A 16
SHEET 1 B 2 PHE A 48 VAL A 49 0
SHEET 2 B 2 THR A 56 PHE A 57 -1 O PHE A 57 N PHE A 48
LINK SG CYS A 18 ZN ZN A 201 1555 1555 2.37
LINK SG CYS A 21 ZN ZN A 201 1555 1555 2.33
LINK NE2 HIS A 34 ZN ZN A 201 1555 1555 2.36
LINK NE2 HIS A 39 ZN ZN A 201 1555 1555 2.35
LINK SG CYS A 50 ZN ZN A 401 1555 1555 2.35
LINK SG CYS A 53 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 66 ZN ZN A 401 1555 1555 2.37
LINK SG CYS A 70 ZN ZN A 401 1555 1555 2.33
SITE 1 AC1 4 CYS A 18 CYS A 21 HIS A 34 HIS A 39
SITE 1 AC2 4 CYS A 50 CYS A 53 HIS A 66 CYS A 70
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 - r 2 2 Bytes