Header list of 2db8.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 15-DEC-05 2DB8
TITLE SOLUTION STRUCTURES OF THE FN3 DOMAIN OF HUMAN TRIPARTITE MOTIF
TITLE 2 PROTEIN 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRIPARTITE MOTIF PROTEIN 9, ISOFORM 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIBRONECTIN TYPE III DOMAIN;
COMPND 5 SYNONYM: TRIPARTITE MOTIF PROTEIN 9;
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: TRIM9;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P040921-16;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RING FINGER PROTEIN 91, TRIM9, KIAA0282, RNF91, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL
KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 4 PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DB8 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DB8 1 VERSN
REVDAT 1 15-JUN-06 2DB8 0
JRNL AUTH M.SATO,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURES OF THE FN3 DOMAIN OF HUMAN TRIPARTITE
JRNL TITL 2 MOTIF PROTEIN 9
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 2DB8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000025209.
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 : 1MM FN3 DOMAIN U-15N,13C; 20MM D
REMARK 210 -TRIS HCL; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3; 90% H2O, 10% D2O
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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, 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 LEAST RESTRAINT 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 GLN A 16 47.84 -109.64
REMARK 500 1 LEU A 17 124.91 -38.59
REMARK 500 1 CYS A 20 -46.66 -130.21
REMARK 500 1 ASN A 25 58.31 -110.34
REMARK 500 1 TRP A 31 -177.68 -60.44
REMARK 500 1 SER A 37 103.81 -56.96
REMARK 500 1 ASP A 50 40.38 -86.92
REMARK 500 1 MET A 66 115.44 -166.15
REMARK 500 1 ASN A 75 44.27 34.57
REMARK 500 1 THR A 88 -72.51 -52.26
REMARK 500 1 THR A 96 113.94 -34.03
REMARK 500 1 SER A 108 -59.87 -131.84
REMARK 500 2 SER A 6 50.46 -101.46
REMARK 500 2 PRO A 8 -174.69 -69.74
REMARK 500 2 GLU A 18 -66.59 -102.20
REMARK 500 2 GLU A 19 107.10 -46.84
REMARK 500 2 ASN A 25 41.42 -108.46
REMARK 500 2 TRP A 31 175.54 -48.33
REMARK 500 2 PRO A 35 0.62 -69.74
REMARK 500 2 ASP A 50 39.37 -89.47
REMARK 500 2 ASN A 75 44.86 38.69
REMARK 500 2 THR A 88 -71.37 -44.78
REMARK 500 2 SER A 94 -177.36 -64.94
REMARK 500 2 THR A 96 118.15 -35.69
REMARK 500 3 LEU A 15 90.59 -54.18
REMARK 500 3 GLN A 16 54.33 -119.96
REMARK 500 3 LEU A 17 167.72 -47.82
REMARK 500 3 GLU A 19 106.21 -37.71
REMARK 500 3 CYS A 20 -63.43 -104.75
REMARK 500 3 HIS A 23 -47.82 -131.19
REMARK 500 3 ASP A 50 35.34 -86.06
REMARK 500 3 LYS A 63 52.96 -117.08
REMARK 500 3 THR A 96 125.73 -35.87
REMARK 500 3 LEU A 99 77.01 -113.05
REMARK 500 3 SER A 108 94.36 -59.31
REMARK 500 3 SER A 109 165.20 -49.73
REMARK 500 4 ALA A 11 130.29 -35.43
REMARK 500 4 GLN A 16 75.87 -111.57
REMARK 500 4 CYS A 21 112.84 -170.98
REMARK 500 4 ASN A 24 -71.12 -61.47
REMARK 500 4 ASP A 50 44.47 -81.30
REMARK 500 4 ASN A 75 52.60 38.01
REMARK 500 4 LYS A 95 103.93 -35.70
REMARK 500 4 THR A 96 114.88 -34.66
REMARK 500 4 THR A 101 154.21 -37.51
REMARK 500 5 CYS A 20 -55.58 -122.85
REMARK 500 5 ASN A 25 49.09 -94.81
REMARK 500 5 SER A 30 58.12 -113.55
REMARK 500 5 TRP A 31 155.03 -46.81
REMARK 500 5 ASP A 50 44.28 -82.36
REMARK 500
REMARK 500 THIS ENTRY HAS 213 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSI002012704.1 RELATED DB: TARGETDB
DBREF 2DB8 A 8 104 UNP Q9C026 TRIM9_HUMAN 437 534
SEQADV 2DB8 GLY A 1 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 2 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 3 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 GLY A 4 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 5 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 6 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 GLY A 7 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 105 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 GLY A 106 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 PRO A 107 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 108 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 SER A 109 UNP Q9C026 CLONING ARTIFACT
SEQADV 2DB8 GLY A 110 UNP Q9C026 CLONING ARTIFACT
SEQRES 1 A 110 GLY SER SER GLY SER SER GLY PRO VAL PRO ALA THR PRO
SEQRES 2 A 110 ILE LEU GLN LEU GLU GLU CYS CYS THR HIS ASN ASN SER
SEQRES 3 A 110 ALA THR LEU SER TRP LYS GLN PRO PRO LEU SER THR VAL
SEQRES 4 A 110 PRO ALA ASP GLY TYR ILE LEU GLU LEU ASP ASP GLY ASN
SEQRES 5 A 110 GLY GLY GLN PHE ARG GLU VAL TYR VAL GLY LYS GLU THR
SEQRES 6 A 110 MET CYS THR VAL ASP GLY LEU HIS PHE ASN SER THR TYR
SEQRES 7 A 110 ASN ALA ARG VAL LYS ALA PHE ASN LYS THR GLY VAL SER
SEQRES 8 A 110 PRO TYR SER LYS THR LEU VAL LEU GLN THR SER GLU GLY
SEQRES 9 A 110 SER GLY PRO SER SER GLY
SHEET 1 A 2 SER A 26 LEU A 29 0
SHEET 2 A 2 CYS A 67 ASP A 70 -1 O CYS A 67 N LEU A 29
SHEET 1 B 4 ARG A 57 GLY A 62 0
SHEET 2 B 4 GLY A 43 LEU A 48 -1 N LEU A 46 O TYR A 60
SHEET 3 B 4 ASN A 79 PHE A 85 -1 O PHE A 85 N GLY A 43
SHEET 4 B 4 LEU A 97 VAL A 98 -1 O LEU A 97 N ALA A 80
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