Header list of 2d9n.pdb file
Complete list - r 9 2 Bytes
HEADER RNA BINDING PROTEIN 12-DEC-05 2D9N
TITLE SOLUTION STRUCTURE OF CCCH TYPE ZINC-FINGER DOMAIN 2 IN CLEAVAGE AND
TITLE 2 POLYADENYLATION SPECIFICITY FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR, 30 KDA
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: CCCH-TYPE ZINC FINGER MOTIF;
COMPND 6 SYNONYM: CPSF 30 KDA SUBUNIT, NS1 EFFECTOR DOMAIN-BINDING PROTEIN 1,
COMPND 7 NEB-1, NO ARCHES HOMOLOG;
COMPND 8 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: CPSF4;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050302-51;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS CCCH ZINC-FINGER, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON
KEYWDS 2 PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2D9N 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2D9N 1 VERSN
REVDAT 1 12-JUN-06 2D9N 0
JRNL AUTH C.ABE,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF CCCH TYPE ZINC-FINGER DOMAIN 2 IN
JRNL TITL 2 CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR
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
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D9N COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025158.
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
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM D-TRIS-HCL(PH7.0), 100MM
REMARK 210 NACL, 1MM D-DTT, 0.02% NAN3,
REMARK 210 50UM ZNCL2+1MM IDA, 90% H2O, 10%
REMARK 210 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 0.93191, CYANA 2.0
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 SER A 60 143.01 -170.29
REMARK 500 1 THR A 65 -36.83 -36.65
REMARK 500 1 CYS A 82 166.10 -48.95
REMARK 500 1 LYS A 101 -63.25 -103.40
REMARK 500 1 SER A 106 45.23 -89.74
REMARK 500 1 PRO A 111 3.65 -69.80
REMARK 500 1 PRO A 117 3.02 -69.71
REMARK 500 1 CYS A 124 157.67 -42.38
REMARK 500 2 THR A 65 -32.25 -36.16
REMARK 500 2 LYS A 101 -64.45 -103.46
REMARK 500 2 SER A 106 41.55 -98.06
REMARK 500 2 PRO A 111 3.68 -69.80
REMARK 500 2 PRO A 117 2.20 -69.77
REMARK 500 2 ASP A 123 73.09 -66.32
REMARK 500 3 LYS A 64 0.24 -69.94
REMARK 500 3 THR A 65 -38.31 -33.49
REMARK 500 3 LYS A 101 -64.99 -102.67
REMARK 500 3 SER A 106 39.33 -94.86
REMARK 500 3 GLU A 109 43.49 -102.48
REMARK 500 3 PRO A 111 4.33 -69.79
REMARK 500 3 PRO A 117 1.78 -69.79
REMARK 500 3 CYS A 124 162.69 -43.10
REMARK 500 3 PRO A 125 4.41 -69.73
REMARK 500 3 SER A 131 -45.00 -133.06
REMARK 500 4 SER A 61 38.71 -83.35
REMARK 500 4 THR A 65 -37.96 -32.46
REMARK 500 4 LYS A 101 -64.41 -100.81
REMARK 500 4 SER A 106 44.18 -92.90
REMARK 500 4 GLU A 109 47.83 -109.82
REMARK 500 4 PRO A 111 3.56 -69.79
REMARK 500 4 PRO A 117 1.44 -69.82
REMARK 500 4 LYS A 120 54.02 -102.65
REMARK 500 4 ASP A 123 44.74 -103.21
REMARK 500 4 TRP A 126 150.95 -49.74
REMARK 500 4 SER A 127 123.49 -174.59
REMARK 500 5 SER A 60 94.48 -51.72
REMARK 500 5 GLU A 63 176.32 -59.60
REMARK 500 5 THR A 65 -36.26 -33.64
REMARK 500 5 CYS A 82 166.21 -49.74
REMARK 500 5 PHE A 98 -70.77 -71.86
REMARK 500 5 LYS A 101 -63.64 -101.67
REMARK 500 5 SER A 106 40.78 -90.84
REMARK 500 5 GLU A 109 42.64 -101.91
REMARK 500 5 PRO A 111 2.95 -69.72
REMARK 500 5 PRO A 117 3.42 -69.78
REMARK 500 5 PRO A 125 2.89 -69.75
REMARK 500 6 GLU A 63 -175.12 -69.09
REMARK 500 6 LYS A 64 0.03 -68.83
REMARK 500 6 THR A 65 -35.71 -32.61
REMARK 500 6 CYS A 82 165.51 -48.65
REMARK 500
REMARK 500 THIS ENTRY HAS 195 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 256 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 68 SG
REMARK 620 2 CYS A 76 SG 116.8
REMARK 620 3 CYS A 82 SG 92.7 118.5
REMARK 620 4 HIS A 86 NE2 111.5 118.4 94.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 456 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 96 SG
REMARK 620 2 CYS A 105 SG 108.3
REMARK 620 3 CYS A 110 SG 116.3 115.7
REMARK 620 4 HIS A 114 NE2 107.9 90.0 115.5
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 256
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 456
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002004475.1 RELATED DB: TARGETDB
DBREF 2D9N A 61 126 UNP O95639 CPSF4_HUMAN 61 126
SEQADV 2D9N GLY A 56 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N SER A 57 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N SER A 58 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N GLY A 59 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N SER A 60 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N SER A 127 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N GLY A 128 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N PRO A 129 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N SER A 130 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N SER A 131 UNP O95639 CLONING ARTIFACT
SEQADV 2D9N GLY A 132 UNP O95639 CLONING ARTIFACT
SEQRES 1 A 77 GLY SER SER GLY SER SER GLY GLU LYS THR VAL VAL CYS
SEQRES 2 A 77 LYS HIS TRP LEU ARG GLY LEU CYS LYS LYS GLY ASP GLN
SEQRES 3 A 77 CYS GLU PHE LEU HIS GLU TYR ASP MET THR LYS MET PRO
SEQRES 4 A 77 GLU CYS TYR PHE TYR SER LYS PHE GLY GLU CYS SER ASN
SEQRES 5 A 77 LYS GLU CYS PRO PHE LEU HIS ILE ASP PRO GLU SER LYS
SEQRES 6 A 77 ILE LYS ASP CYS PRO TRP SER GLY PRO SER SER GLY
HET ZN A 256 1
HET ZN A 456 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 CYS A 68 ARG A 73 1 6
HELIX 2 2 CYS A 96 PHE A 102 1 7
LINK SG CYS A 68 ZN ZN A 256 1555 1555 2.37
LINK SG CYS A 76 ZN ZN A 256 1555 1555 2.33
LINK SG CYS A 82 ZN ZN A 256 1555 1555 2.33
LINK NE2 HIS A 86 ZN ZN A 256 1555 1555 2.33
LINK SG CYS A 96 ZN ZN A 456 1555 1555 2.35
LINK SG CYS A 105 ZN ZN A 456 1555 1555 2.37
LINK SG CYS A 110 ZN ZN A 456 1555 1555 2.36
LINK NE2 HIS A 114 ZN ZN A 456 1555 1555 2.37
SITE 1 AC1 4 CYS A 68 CYS A 76 CYS A 82 HIS A 86
SITE 1 AC2 4 CYS A 96 CYS A 105 CYS A 110 HIS A 114
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