Header list of 2ctd.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 24-MAY-05 2CTD
TITLE SOLUTION STRUCTURE OF TWO ZF-C2H2 DOMAINS FROM HUMAN ZINC FINGER
TITLE 2 PROTEIN 512
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZINC FINGER PROTEIN 512;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZF-C2H2 DOMAINS;
COMPND 5 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: ZNF512;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041018-04;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS ZINC BINDING, TWO ZF-C2H2 DOMAIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, METAL BINDING
KEYWDS 4 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CTD 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CTD 1 VERSN
REVDAT 1 24-NOV-05 2CTD 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF TWO ZF-C2H2 DOMAINS FROM HUMAN ZINC
JRNL TITL 2 FINGER PROTEIN 512
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CTD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000024600.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.06MM ZF-C2H2 DOMAINS U
REMARK 210 -15N,13C; 20MM D-TRIS-HCL; 100MM
REMARK 210 NACL; 1MM D-DTT; 0.25MM ZNCL2;
REMARK 210 1MM IDA; 0.02% NAN3; 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 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR 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 LYS A 11 72.71 -117.17
REMARK 500 1 ALA A 18 40.34 -81.63
REMARK 500 1 LYS A 59 89.13 -47.12
REMARK 500 1 ALA A 84 -60.26 -93.05
REMARK 500 1 HIS A 86 46.97 -89.67
REMARK 500 1 SER A 88 78.93 -117.72
REMARK 500 1 SER A 91 -60.75 -130.04
REMARK 500 1 PRO A 93 0.06 -69.75
REMARK 500 2 ARG A 10 -69.99 -130.03
REMARK 500 2 LYS A 59 134.60 -173.72
REMARK 500 2 LYS A 79 -29.72 -39.68
REMARK 500 2 HIS A 86 39.73 -85.74
REMARK 500 2 SER A 95 46.80 35.82
REMARK 500 3 ARG A 8 43.24 -101.66
REMARK 500 3 ILE A 9 49.87 39.25
REMARK 500 3 PRO A 14 -179.48 -69.76
REMARK 500 3 THR A 64 117.84 -161.15
REMARK 500 3 HIS A 67 -72.60 -55.23
REMARK 500 3 LYS A 79 -26.16 -39.10
REMARK 500 3 ASN A 87 35.20 39.41
REMARK 500 3 SER A 88 108.63 -34.59
REMARK 500 4 HIS A 86 39.76 -86.26
REMARK 500 5 PRO A 14 -176.87 -69.76
REMARK 500 5 THR A 39 -62.48 -95.19
REMARK 500 5 LYS A 59 93.52 -33.16
REMARK 500 5 GLN A 60 108.03 -56.52
REMARK 500 5 ALA A 76 -71.23 -51.54
REMARK 500 5 ASN A 87 39.76 74.83
REMARK 500 6 TYR A 16 150.42 -48.86
REMARK 500 6 ALA A 18 40.36 -83.27
REMARK 500 6 PRO A 38 0.17 -69.76
REMARK 500 6 ALA A 76 -72.59 -47.47
REMARK 500 7 PRO A 14 -168.60 -69.76
REMARK 500 7 ALA A 17 174.77 -58.34
REMARK 500 7 ALA A 18 39.45 -92.02
REMARK 500 7 THR A 39 -61.21 -95.56
REMARK 500 7 ASN A 57 -35.81 -132.27
REMARK 500 7 THR A 64 116.45 -163.97
REMARK 500 7 LYS A 79 -27.35 -37.83
REMARK 500 7 ASN A 87 35.05 34.38
REMARK 500 7 SER A 91 99.35 -55.65
REMARK 500 8 SER A 2 146.30 -173.12
REMARK 500 8 LYS A 11 108.58 -161.47
REMARK 500 8 PRO A 14 -174.52 -69.85
REMARK 500 8 GLU A 56 -39.28 -34.20
REMARK 500 8 LYS A 59 37.59 -89.81
REMARK 500 8 ALA A 84 -67.26 -107.40
REMARK 500 8 ASN A 87 48.65 34.16
REMARK 500 8 SER A 88 141.81 -170.35
REMARK 500 8 PRO A 93 2.90 -69.77
REMARK 500
REMARK 500 THIS ENTRY HAS 141 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 37 SG
REMARK 620 2 CYS A 40 SG 96.3
REMARK 620 3 HIS A 54 NE2 113.9 112.6
REMARK 620 4 CYS A 58 SG 116.3 117.1 101.3
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 65 SG
REMARK 620 2 CYS A 68 SG 114.4
REMARK 620 3 HIS A 81 NE2 97.2 116.7
REMARK 620 4 HIS A 86 NE2 117.0 97.6 115.2
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: HSK002001773.1 RELATED DB: TARGETDB
DBREF 2CTD A 8 90 UNP Q96ME7 ZN512_HUMAN 142 224
SEQADV 2CTD GLY A 1 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 2 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 3 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD GLY A 4 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 5 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 6 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD GLY A 7 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 91 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD GLY A 92 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD PRO A 93 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 94 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD SER A 95 UNP Q96ME7 CLONING ARTIFACT
SEQADV 2CTD GLY A 96 UNP Q96ME7 CLONING ARTIFACT
SEQRES 1 A 96 GLY SER SER GLY SER SER GLY ARG ILE ARG LYS GLU PRO
SEQRES 2 A 96 PRO VAL TYR ALA ALA GLY SER LEU GLU GLU GLN TRP TYR
SEQRES 3 A 96 LEU GLU ILE VAL ASP LYS GLY SER VAL SER CYS PRO THR
SEQRES 4 A 96 CYS GLN ALA VAL GLY ARG LYS THR ILE GLU GLY LEU LYS
SEQRES 5 A 96 LYS HIS MET GLU ASN CYS LYS GLN GLU MET PHE THR CYS
SEQRES 6 A 96 HIS HIS CYS GLY LYS GLN LEU ARG SER LEU ALA GLY MET
SEQRES 7 A 96 LYS TYR HIS VAL MET ALA ASN HIS ASN SER LEU PRO SER
SEQRES 8 A 96 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 SER A 20 LYS A 32 1 13
HELIX 2 2 THR A 47 LYS A 59 1 13
HELIX 3 3 SER A 74 HIS A 86 1 13
SHEET 1 A 2 VAL A 35 SER A 36 0
SHEET 2 A 2 GLY A 44 ARG A 45 -1 O ARG A 45 N VAL A 35
LINK SG CYS A 37 ZN ZN A 201 1555 1555 2.37
LINK SG CYS A 40 ZN ZN A 201 1555 1555 2.33
LINK NE2 HIS A 54 ZN ZN A 201 1555 1555 2.36
LINK SG CYS A 58 ZN ZN A 201 1555 1555 2.33
LINK SG CYS A 65 ZN ZN A 401 1555 1555 2.35
LINK SG CYS A 68 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 81 ZN ZN A 401 1555 1555 2.37
LINK NE2 HIS A 86 ZN ZN A 401 1555 1555 2.34
SITE 1 AC1 4 CYS A 37 CYS A 40 HIS A 54 CYS A 58
SITE 1 AC2 4 CYS A 65 CYS A 68 HIS A 81 HIS A 86
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 9 2 Bytes