Header list of 2day.pdb file
Complete list - r 9 2 Bytes
HEADER LIGASE 14-DEC-05 2DAY
TITLE SOLUTION STRUCTURE OF THE RWD DOMAIN OF HUMAN RING FINGER PROTEIN 25
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RING FINGER PROTEIN 25;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RWD DOMAIN;
COMPND 5 EC: 6.3.2.-;
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: RNF25;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050509-01;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS LIGASE, METAL-BINDING, UB1 CONJUGATION, UB1 CONJUGATION PATHWAY, RWD
KEYWDS 2 DOMAIN, ALPHA+BETA SANDWICH FOLD, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 3 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 4 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.YONEYAMA,T.KIGAWA,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,S.YOKOYAMA,
AUTHOR 2 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DAY 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DAY 1 VERSN
REVDAT 1 14-JUN-06 2DAY 0
JRNL AUTH M.YONEYAMA,T.KIGAWA,M.SATO,N.TOCHIO,S.KOSHIBA,M.INOUE,
JRNL AUTH 2 S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE RWD DOMAIN OF HUMAN RING FINGER
JRNL TITL 2 PROTEIN 25
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 2DAY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025199.
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 : 0.72MM RWD DOMAIN U-15N,13C;
REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM
REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 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 0.9318, 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 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 6 148.97 -171.89
REMARK 500 1 TRP A 11 115.21 -162.08
REMARK 500 1 TYR A 24 44.40 -96.81
REMARK 500 1 ASN A 34 29.19 42.39
REMARK 500 1 THR A 37 26.56 38.94
REMARK 500 1 ILE A 44 149.07 -170.87
REMARK 500 1 ALA A 49 32.92 -88.71
REMARK 500 1 ALA A 51 94.85 -68.28
REMARK 500 1 GLN A 54 176.38 -51.53
REMARK 500 1 VAL A 59 119.94 -175.40
REMARK 500 1 PRO A 68 -174.97 -69.76
REMARK 500 1 TYR A 71 140.65 -31.87
REMARK 500 1 PRO A 83 83.27 -69.76
REMARK 500 1 VAL A 101 -39.85 -37.34
REMARK 500 2 SER A 3 143.46 -35.88
REMARK 500 2 ASP A 10 172.29 -54.01
REMARK 500 2 TYR A 24 42.39 -90.94
REMARK 500 2 LYS A 32 102.44 -58.60
REMARK 500 2 THR A 37 33.37 -88.36
REMARK 500 2 ALA A 49 44.11 -85.86
REMARK 500 2 SER A 56 -48.71 -130.15
REMARK 500 2 PRO A 68 -175.06 -69.71
REMARK 500 2 TYR A 71 140.33 -30.33
REMARK 500 2 HIS A 73 -38.94 -32.41
REMARK 500 2 PRO A 83 82.72 -69.78
REMARK 500 2 ALA A 109 126.73 -39.36
REMARK 500 3 TRP A 11 122.84 -170.50
REMARK 500 3 TYR A 24 44.29 -91.23
REMARK 500 3 THR A 37 28.26 47.94
REMARK 500 3 PRO A 48 92.87 -69.79
REMARK 500 3 ALA A 49 44.16 -83.28
REMARK 500 3 GLU A 52 33.38 -93.59
REMARK 500 3 PRO A 68 -173.77 -69.77
REMARK 500 3 TYR A 71 141.26 -29.24
REMARK 500 3 HIS A 73 -39.12 -31.68
REMARK 500 3 PRO A 83 85.18 -69.79
REMARK 500 3 VAL A 97 -71.54 -66.16
REMARK 500 3 SER A 123 31.95 -87.72
REMARK 500 4 SER A 2 97.51 -50.59
REMARK 500 4 TYR A 24 45.52 -95.42
REMARK 500 4 GLU A 27 -31.97 -35.82
REMARK 500 4 LYS A 32 101.95 -40.55
REMARK 500 4 THR A 37 31.39 -92.95
REMARK 500 4 ALA A 49 43.17 -89.21
REMARK 500 4 ALA A 51 44.27 -87.30
REMARK 500 4 GLU A 52 43.06 35.04
REMARK 500 4 ASP A 53 49.64 34.97
REMARK 500 4 TYR A 71 141.22 -31.65
REMARK 500 4 PRO A 83 80.79 -69.73
REMARK 500 4 LEU A 95 -70.65 -76.56
REMARK 500
REMARK 500 THIS ENTRY HAS 253 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000178.1 RELATED DB: TARGETDB
DBREF 2DAY A 8 122 UNP Q96BH1 RNF25_HUMAN 10 125
SEQADV 2DAY GLY A 1 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 2 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 3 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY GLY A 4 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 5 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 6 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY GLY A 7 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 123 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY GLY A 124 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY PRO A 125 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 126 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY SER A 127 UNP Q96BH1 CLONING ARTIFACT
SEQADV 2DAY GLY A 128 UNP Q96BH1 CLONING ARTIFACT
SEQRES 1 A 128 GLY SER SER GLY SER SER GLY GLU GLU ASP TRP VAL LEU
SEQRES 2 A 128 PRO SER GLU VAL GLU VAL LEU GLU SER ILE TYR LEU ASP
SEQRES 3 A 128 GLU LEU GLN VAL ILE LYS GLY ASN GLY ARG THR SER PRO
SEQRES 4 A 128 TRP GLU ILE TYR ILE THR LEU HIS PRO ALA THR ALA GLU
SEQRES 5 A 128 ASP GLN ASP SER GLN TYR VAL CYS PHE THR LEU VAL LEU
SEQRES 6 A 128 GLN VAL PRO ALA GLU TYR PRO HIS GLU VAL PRO GLN ILE
SEQRES 7 A 128 SER ILE ARG ASN PRO ARG GLY LEU SER ASP GLU GLN ILE
SEQRES 8 A 128 HIS THR ILE LEU GLN VAL LEU GLY HIS VAL ALA LYS ALA
SEQRES 9 A 128 GLY LEU GLY THR ALA MET LEU TYR GLU LEU ILE GLU LYS
SEQRES 10 A 128 GLY LYS GLU ILE LEU SER GLY PRO SER SER GLY
HELIX 1 1 TRP A 11 TYR A 24 1 14
HELIX 2 2 SER A 87 GLY A 105 1 19
HELIX 3 3 MET A 110 SER A 123 1 14
SHEET 1 A 4 LEU A 28 ILE A 31 0
SHEET 2 A 4 TRP A 40 LEU A 46 -1 O GLU A 41 N ILE A 31
SHEET 3 A 4 CYS A 60 VAL A 67 -1 O LEU A 65 N ILE A 42
SHEET 4 A 4 GLN A 77 ARG A 84 -1 O SER A 79 N VAL A 64
CISPEP 1 TYR A 71 PRO A 72 1 -0.01
CISPEP 2 TYR A 71 PRO A 72 2 -0.07
CISPEP 3 TYR A 71 PRO A 72 3 -0.04
CISPEP 4 TYR A 71 PRO A 72 4 0.02
CISPEP 5 TYR A 71 PRO A 72 5 -0.07
CISPEP 6 TYR A 71 PRO A 72 6 -0.08
CISPEP 7 TYR A 71 PRO A 72 7 -0.06
CISPEP 8 TYR A 71 PRO A 72 8 -0.11
CISPEP 9 TYR A 71 PRO A 72 9 -0.02
CISPEP 10 TYR A 71 PRO A 72 10 -0.11
CISPEP 11 TYR A 71 PRO A 72 11 -0.11
CISPEP 12 TYR A 71 PRO A 72 12 -0.04
CISPEP 13 TYR A 71 PRO A 72 13 -0.09
CISPEP 14 TYR A 71 PRO A 72 14 -0.04
CISPEP 15 TYR A 71 PRO A 72 15 -0.04
CISPEP 16 TYR A 71 PRO A 72 16 -0.04
CISPEP 17 TYR A 71 PRO A 72 17 0.00
CISPEP 18 TYR A 71 PRO A 72 18 -0.03
CISPEP 19 TYR A 71 PRO A 72 19 -0.04
CISPEP 20 TYR A 71 PRO A 72 20 0.00
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