Header list of 2csw.pdb file
Complete list - r 9 2 Bytes
HEADER LIGASE 23-MAY-05 2CSW
TITLE SOLUTION STRUCTURE OF THE FHA DOMAIN OF HUMAN UBIQUITIN LIGASE PROTEIN
TITLE 2 RNF8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN LIGASE PROTEIN RNF8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FHA DOMAIN;
COMPND 5 SYNONYM: RING FINGER PROTEIN 8;
COMPND 6 EC: 6.3.2.-;
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: RNF8;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040322-86;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS 11-STRANDED BETA SANDWICH, RING FINGER PROTEIN 8, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, LIGASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HAYASHI,T.NAGASHIMA,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS
AUTHOR 2 INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2CSW 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2CSW 1 VERSN
REVDAT 1 23-NOV-05 2CSW 0
JRNL AUTH F.HAYASHI,T.NAGASHIMA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FHA DOMAIN OF HUMAN UBIQUITIN
JRNL TITL 2 LIGASE PROTEIN RNF8
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
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2CSW 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_1000024585.
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 : 1.1MM 13C,15N-LABELED PROTEIN;
REMARK 210 20MM D-TRISHCL; 100MM NACL; 1MM
REMARK 210 D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 900 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 0.9297, CYANA 2.0
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 CYS A 19 -170.90 -172.89
REMARK 500 1 LEU A 32 68.37 -116.73
REMARK 500 1 LYS A 67 149.81 -175.01
REMARK 500 1 CYS A 135 60.50 -110.86
REMARK 500 1 PRO A 138 95.57 -69.73
REMARK 500 2 LEU A 20 71.51 -112.80
REMARK 500 2 ARG A 21 105.45 -51.60
REMARK 500 2 LYS A 67 145.33 -174.61
REMARK 500 2 LEU A 112 -175.87 -61.44
REMARK 500 2 VAL A 124 109.61 -51.60
REMARK 500 2 CYS A 135 60.52 -110.78
REMARK 500 2 PRO A 142 -173.84 -69.73
REMARK 500 3 CYS A 19 -177.96 -172.42
REMARK 500 3 LEU A 32 70.52 -117.88
REMARK 500 3 LYS A 80 77.62 51.79
REMARK 500 3 CYS A 135 61.14 -111.71
REMARK 500 3 PRO A 142 -178.05 -69.69
REMARK 500 4 ASP A 11 139.93 -175.37
REMARK 500 4 CYS A 19 -179.59 -173.70
REMARK 500 4 LEU A 20 71.90 -115.11
REMARK 500 4 ASN A 62 62.82 -115.60
REMARK 500 4 LYS A 80 82.98 50.31
REMARK 500 4 LEU A 112 -178.44 -62.69
REMARK 500 4 CYS A 135 61.65 -112.44
REMARK 500 4 PRO A 138 85.31 -69.73
REMARK 500 4 PRO A 142 -174.36 -69.76
REMARK 500 4 SER A 144 122.56 -171.58
REMARK 500 5 CYS A 19 -175.77 -173.79
REMARK 500 5 LEU A 20 73.87 -116.40
REMARK 500 5 GLN A 102 97.94 -65.73
REMARK 500 5 CYS A 135 60.68 -111.58
REMARK 500 5 PRO A 138 87.95 -69.72
REMARK 500 6 ARG A 16 170.33 -56.53
REMARK 500 6 LEU A 20 71.43 -110.84
REMARK 500 6 ARG A 21 109.32 -51.55
REMARK 500 6 LEU A 32 70.32 -118.94
REMARK 500 6 PHE A 44 32.75 -96.64
REMARK 500 6 LEU A 82 -64.34 -105.50
REMARK 500 6 CYS A 135 59.91 -108.96
REMARK 500 7 SER A 6 -73.54 -122.38
REMARK 500 7 ALA A 13 55.56 -105.01
REMARK 500 7 LEU A 20 73.94 -118.42
REMARK 500 7 LEU A 32 75.57 -117.37
REMARK 500 7 ILE A 54 -71.57 -79.94
REMARK 500 7 LYS A 80 83.73 50.46
REMARK 500 7 CYS A 135 60.60 -111.27
REMARK 500 8 ASP A 11 112.50 -164.24
REMARK 500 8 CYS A 19 -178.32 -173.72
REMARK 500 8 CYS A 55 72.98 -154.34
REMARK 500 8 LYS A 67 148.04 -175.39
REMARK 500
REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001001223.1 RELATED DB: TARGETDB
DBREF 2CSW A 8 139 UNP O76064 RNF8_HUMAN 8 139
SEQADV 2CSW GLY A 1 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 2 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 3 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW GLY A 4 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 5 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 6 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW GLY A 7 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 140 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW GLY A 141 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW PRO A 142 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 143 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW SER A 144 UNP O76064 CLONING ARTIFACT
SEQADV 2CSW GLY A 145 UNP O76064 CLONING ARTIFACT
SEQRES 1 A 145 GLY SER SER GLY SER SER GLY VAL THR GLY ASP ARG ALA
SEQRES 2 A 145 GLY GLY ARG SER TRP CYS LEU ARG ARG VAL GLY MET SER
SEQRES 3 A 145 ALA GLY TRP LEU LEU LEU GLU ASP GLY CYS GLU VAL THR
SEQRES 4 A 145 VAL GLY ARG GLY PHE GLY VAL THR TYR GLN LEU VAL SER
SEQRES 5 A 145 LYS ILE CYS PRO LEU MET ILE SER ARG ASN HIS CYS VAL
SEQRES 6 A 145 LEU LYS GLN ASN PRO GLU GLY GLN TRP THR ILE MET ASP
SEQRES 7 A 145 ASN LYS SER LEU ASN GLY VAL TRP LEU ASN ARG ALA ARG
SEQRES 8 A 145 LEU GLU PRO LEU ARG VAL TYR SER ILE HIS GLN GLY ASP
SEQRES 9 A 145 TYR ILE GLN LEU GLY VAL PRO LEU GLU ASN LYS GLU ASN
SEQRES 10 A 145 ALA GLU TYR GLU TYR GLU VAL THR GLU GLU ASP TRP GLU
SEQRES 11 A 145 THR ILE TYR PRO CYS LEU SER PRO LYS SER GLY PRO SER
SEQRES 12 A 145 SER GLY
HELIX 1 1 CYS A 55 ILE A 59 5 5
HELIX 2 2 TRP A 129 TYR A 133 1 5
SHEET 1 A 3 LEU A 30 LEU A 31 0
SHEET 2 A 3 ARG A 16 LEU A 20 -1 N LEU A 20 O LEU A 30
SHEET 3 A 3 VAL A 124 ASP A 128 -1 O THR A 125 N CYS A 19
SHEET 1 B 5 TYR A 48 GLN A 49 0
SHEET 2 B 5 VAL A 38 GLY A 41 1 N THR A 39 O TYR A 48
SHEET 3 B 5 CYS A 64 GLN A 68 -1 O LEU A 66 N VAL A 38
SHEET 4 B 5 TRP A 74 MET A 77 -1 O MET A 77 N VAL A 65
SHEET 5 B 5 TYR A 98 SER A 99 -1 O TYR A 98 N ILE A 76
SHEET 1 C 2 VAL A 85 LEU A 87 0
SHEET 2 C 2 ILE A 106 LEU A 108 -1 O GLN A 107 N TRP 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