Header list of 2cs8.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSCRIPTION 20-MAY-05 2CS8
TITLE SOLUTION STRUCTURE OF TANDEM REPEAT OF THE FIFTH AND SIXTH ZINC-FINGER
TITLE 2 C2HC DOMAINS FROM HUMAN ST18
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA0535 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE FIFTH AND SIXTH C2HC DOMAINS;
COMPND 5 SYNONYM: ST18, SUPPRESSION OF TUMORIGENICITY 18, BREAST CARCINOMA,
COMPND 6 ZINC-FINGER PROTEIN;
COMPND 7 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 HG03847;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040921-02;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS ST18, ZINC-FINGER, C2HC, STRUCTURAL GENOMICS, NPPSFA, NATIONAL
KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN
KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.SUETAKE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CS8 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2CS8 1 VERSN
REVDAT 1 20-NOV-05 2CS8 0
JRNL AUTH T.SUETAKE,T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF TANDEM REPEAT OF THE FIFTH AND SIXTH
JRNL TITL 2 ZINC-FINGER C2HC DOMAINS FROM HUMAN ST18
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 2CS8 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_1000024565.
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 : 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.21MM 13C, 15N-LABELED PROTEIN;
REMARK 210 20MM D-TRIS-HCL; 100MM NACL; 1MM
REMARK 210 D10-DTT; 0.02% NAN3; 0.01MM ZNCL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.927, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATION, TARGET
REMARK 210 FUNCTION
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 10 163.90 -41.71
REMARK 500 1 CYS A 12 108.13 -54.16
REMARK 500 1 LEU A 53 84.37 -67.53
REMARK 500 1 TRP A 55 123.73 -174.55
REMARK 500 1 VAL A 79 -46.23 -133.47
REMARK 500 1 HIS A 83 123.48 -170.36
REMARK 500 1 SER A 87 -34.60 -39.90
REMARK 500 1 LYS A 97 122.05 -174.28
REMARK 500 2 CYS A 12 100.87 -34.50
REMARK 500 2 LYS A 44 52.55 35.63
REMARK 500 2 PRO A 47 3.19 -69.86
REMARK 500 2 LEU A 48 120.27 -34.32
REMARK 500 2 SER A 52 148.19 -172.17
REMARK 500 2 LYS A 56 148.17 -173.41
REMARK 500 2 CYS A 65 133.95 -36.02
REMARK 500 2 VAL A 79 -41.03 -133.82
REMARK 500 2 HIS A 83 125.34 -172.77
REMARK 500 2 LYS A 97 104.86 -36.47
REMARK 500 3 PRO A 8 -176.89 -69.71
REMARK 500 3 CYS A 12 105.32 -43.95
REMARK 500 3 LYS A 44 47.33 -84.13
REMARK 500 3 TRP A 55 -61.78 -107.17
REMARK 500 3 CYS A 65 133.42 -177.98
REMARK 500 3 HIS A 83 149.30 -173.43
REMARK 500 3 ILE A 96 45.42 -78.39
REMARK 500 3 LYS A 100 42.93 -90.95
REMARK 500 3 VAL A 101 42.58 -100.90
REMARK 500 4 SER A 6 42.05 38.18
REMARK 500 4 PRO A 8 -179.64 -69.71
REMARK 500 4 CYS A 12 105.15 -36.54
REMARK 500 4 LYS A 44 111.29 -36.93
REMARK 500 4 TRP A 55 40.13 -89.54
REMARK 500 4 LYS A 56 109.82 -58.18
REMARK 500 4 LEU A 57 43.51 -79.47
REMARK 500 4 ASN A 58 39.97 33.78
REMARK 500 4 GLU A 61 160.16 -40.24
REMARK 500 4 CYS A 65 135.54 -34.90
REMARK 500 4 HIS A 83 121.20 -174.27
REMARK 500 4 LYS A 97 148.08 -174.17
REMARK 500 4 PRO A 105 87.70 -69.75
REMARK 500 5 CYS A 12 109.73 -33.68
REMARK 500 5 VAL A 14 108.47 -59.92
REMARK 500 5 GLN A 43 -39.99 -36.04
REMARK 500 5 LEU A 57 40.42 -102.99
REMARK 500 5 ASN A 58 40.11 -97.75
REMARK 500 5 GLN A 60 145.01 -35.25
REMARK 500 5 PRO A 63 -164.07 -69.75
REMARK 500 5 HIS A 64 133.28 -35.47
REMARK 500 5 CYS A 65 133.61 -34.75
REMARK 500 5 LEU A 67 133.38 -36.36
REMARK 500
REMARK 500 THIS ENTRY HAS 221 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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 SG
REMARK 620 2 CYS A 17 SG 105.6
REMARK 620 3 HIS A 30 NE2 117.3 106.3
REMARK 620 4 CYS A 36 SG 106.5 104.9 115.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 65 SG
REMARK 620 2 CYS A 70 SG 104.9
REMARK 620 3 HIS A 83 NE2 112.1 107.1
REMARK 620 4 CYS A 89 SG 110.6 107.0 114.3
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100521.1 RELATED DB: TARGETDB
DBREF 2CS8 A 8 102 UNP O60284 O60284_HUMAN 812 906
SEQADV 2CS8 GLY A 1 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 2 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 3 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 GLY A 4 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 5 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 6 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 GLY A 7 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 103 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 GLY A 104 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 PRO A 105 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 106 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 SER A 107 UNP O60284 CLONING ARTIFACT
SEQADV 2CS8 GLY A 108 UNP O60284 CLONING ARTIFACT
SEQRES 1 A 108 GLY SER SER GLY SER SER GLY PRO GLU LEU LYS CYS PRO
SEQRES 2 A 108 VAL ILE GLY CYS ASP GLY GLN GLY HIS ILE SER GLY LYS
SEQRES 3 A 108 TYR THR SER HIS ARG THR ALA SER GLY CYS PRO LEU ALA
SEQRES 4 A 108 ALA LYS ARG GLN LYS GLU ASN PRO LEU ASN GLY ALA SER
SEQRES 5 A 108 LEU SER TRP LYS LEU ASN LYS GLN GLU LEU PRO HIS CYS
SEQRES 6 A 108 PRO LEU PRO GLY CYS ASN GLY LEU GLY HIS VAL ASN ASN
SEQRES 7 A 108 VAL PHE VAL THR HIS ARG SER LEU SER GLY CYS PRO LEU
SEQRES 8 A 108 ASN ALA GLN VAL ILE LYS LYS GLY LYS VAL SER SER GLY
SEQRES 9 A 108 PRO SER SER GLY
HET ZN A 401 1
HET ZN A 601 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 CYS A 36 LYS A 44 1 9
HELIX 2 2 CYS A 89 ILE A 96 1 8
LINK SG CYS A 12 ZN ZN A 401 1555 1555 2.29
LINK SG CYS A 17 ZN ZN A 401 1555 1555 2.33
LINK NE2 HIS A 30 ZN ZN A 401 1555 1555 2.04
LINK SG CYS A 36 ZN ZN A 401 1555 1555 2.28
LINK SG CYS A 65 ZN ZN A 601 1555 1555 2.35
LINK SG CYS A 70 ZN ZN A 601 1555 1555 2.33
LINK NE2 HIS A 83 ZN ZN A 601 1555 1555 2.03
LINK SG CYS A 89 ZN ZN A 601 1555 1555 2.32
SITE 1 AC1 4 CYS A 12 CYS A 17 HIS A 30 CYS A 36
SITE 1 AC2 4 CYS A 65 CYS A 70 HIS A 83 CYS A 89
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