Header list of 1wk0.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 29-MAY-04 1WK0
TITLE SOLUTION STRUCTURE OF FIBRONECTIN TYPE III DOMAIN DERIVED FROM HUMAN
TITLE 2 KIAA0970 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KIAA0970 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIBRONECTIN TYPE3 DOMAIN;
COMPND 5 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 HH13674;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P030723-24;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS FIBRONECTIN TYPE III DOMAIN, STRUCTURAL GENOMICS, RIKEN STRUCTURAL
KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.KOBAYASHI,S.KOSHIBA,M.INOUE,F.HAYASHI,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WK0 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WK0 1 VERSN
REVDAT 1 29-NOV-04 1WK0 0
JRNL AUTH N.KOBAYASHI,S.KOSHIBA,M.INOUE,F.HAYASHI,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF FIBRONECTIN TYPE III DOMAIN DERIVED
JRNL TITL 2 FROM HUMAN KIAA0970 PROTEIN
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), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WK0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000023660.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.11MM FIBRONECTIN TYPE III
REMARK 210 DOMAIN U-13C,15N; 20MM PHOSPHATE
REMARK 210 BUFFER NA (PH6.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.901, 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 VIOLATIONS, 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 GLU A 9 -38.94 -38.16
REMARK 500 1 ASP A 28 35.16 34.40
REMARK 500 1 ALA A 31 -70.37 -38.50
REMARK 500 1 ASP A 50 165.21 -49.01
REMARK 500 1 SER A 52 40.16 -93.28
REMARK 500 1 TYR A 58 100.08 -50.96
REMARK 500 1 SER A 66 -30.13 -36.63
REMARK 500 1 GLU A 81 166.73 -48.59
REMARK 500 1 PRO A 123 93.08 -69.77
REMARK 500 1 ASP A 124 -65.96 -106.06
REMARK 500 2 ASP A 28 41.37 34.30
REMARK 500 2 ASP A 50 150.32 -41.88
REMARK 500 2 SER A 52 33.71 -94.20
REMARK 500 2 TYR A 58 105.59 -44.37
REMARK 500 2 VAL A 76 -35.63 -132.11
REMARK 500 2 GLU A 112 168.52 -46.91
REMARK 500 2 CYS A 121 -32.08 -35.34
REMARK 500 2 PRO A 123 90.09 -69.81
REMARK 500 2 ILE A 131 106.14 -47.34
REMARK 500 2 SER A 135 132.40 -171.70
REMARK 500 3 SER A 3 107.00 -48.01
REMARK 500 3 SER A 5 41.26 39.06
REMARK 500 3 ASP A 28 37.00 35.49
REMARK 500 3 ALA A 31 -73.27 -35.86
REMARK 500 3 TYR A 58 100.94 -43.38
REMARK 500 3 ASP A 70 44.10 -101.57
REMARK 500 3 SER A 111 -176.64 -59.28
REMARK 500 3 GLU A 112 178.82 -58.67
REMARK 500 3 CYS A 121 -29.20 -39.46
REMARK 500 3 PRO A 123 87.28 -69.75
REMARK 500 4 ASP A 28 41.53 33.11
REMARK 500 4 ALA A 31 -73.79 -38.06
REMARK 500 4 SER A 52 34.17 -90.57
REMARK 500 4 TYR A 58 107.13 -53.04
REMARK 500 4 ASP A 70 47.70 -76.98
REMARK 500 4 ASP A 88 38.27 73.13
REMARK 500 4 SER A 111 -177.73 -69.48
REMARK 500 4 GLU A 112 -176.71 -52.50
REMARK 500 4 CYS A 121 -38.03 -37.74
REMARK 500 4 PRO A 123 99.71 -69.71
REMARK 500 4 ASP A 124 -70.65 -115.78
REMARK 500 4 PRO A 126 93.53 -69.76
REMARK 500 5 ASP A 28 39.62 34.29
REMARK 500 5 ALA A 31 -72.67 -40.68
REMARK 500 5 SER A 52 32.11 -87.73
REMARK 500 5 SER A 53 -71.78 -100.90
REMARK 500 5 TYR A 58 104.72 -51.76
REMARK 500 5 GLU A 81 139.51 -34.10
REMARK 500 5 ASP A 88 37.80 72.96
REMARK 500 5 SER A 111 -175.58 -61.22
REMARK 500
REMARK 500 THIS ENTRY HAS 236 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK002100947.1 RELATED DB: TARGETDB
DBREF 1WK0 A 8 131 UNP Q9Y2H6 FNDC3_HUMAN 209 332
SEQADV 1WK0 GLY A 1 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 2 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 3 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 GLY A 4 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 5 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 6 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 GLY A 7 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 132 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 GLY A 133 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 PRO A 134 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 135 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 SER A 136 UNP Q9Y2H6 CLONING ARTIFACT
SEQADV 1WK0 GLY A 137 UNP Q9Y2H6 CLONING ARTIFACT
SEQRES 1 A 137 GLY SER SER GLY SER SER GLY ASP GLU GLU THR LYS ALA
SEQRES 2 A 137 PHE GLU ALA LEU LEU SER ASN ILE VAL LYS PRO VAL ALA
SEQRES 3 A 137 SER ASP ILE GLN ALA ARG THR VAL VAL LEU THR TRP SER
SEQRES 4 A 137 PRO PRO SER SER LEU ILE ASN GLY GLU THR ASP GLU SER
SEQRES 5 A 137 SER VAL PRO GLU LEU TYR GLY TYR GLU VAL LEU ILE SER
SEQRES 6 A 137 SER THR GLY LYS ASP GLY LYS TYR LYS SER VAL TYR VAL
SEQRES 7 A 137 GLY GLU GLU THR ASN ILE THR LEU ASN ASP LEU LYS PRO
SEQRES 8 A 137 ALA MET ASP TYR HIS ALA LYS VAL GLN ALA GLU TYR ASN
SEQRES 9 A 137 SER ILE LYS GLY THR PRO SER GLU ALA GLU ILE PHE THR
SEQRES 10 A 137 THR LEU SER CYS GLU PRO ASP ILE PRO ASN PRO PRO ARG
SEQRES 11 A 137 ILE SER GLY PRO SER SER GLY
HELIX 1 1 GLY A 7 LEU A 18 1 12
SHEET 1 A 3 VAL A 25 SER A 27 0
SHEET 2 A 3 VAL A 34 THR A 37 -1 O THR A 37 N VAL A 25
SHEET 3 A 3 ASN A 83 LEU A 86 -1 O ILE A 84 N LEU A 36
SHEET 1 B 4 LYS A 74 GLY A 79 0
SHEET 2 B 4 GLY A 59 ILE A 64 -1 N TYR A 60 O GLY A 79
SHEET 3 B 4 ALA A 97 TYR A 103 -1 O LYS A 98 N LEU A 63
SHEET 4 B 4 ILE A 106 LYS A 107 -1 O ILE A 106 N TYR A 103
SHEET 1 C 2 ASP A 94 TYR A 95 0
SHEET 2 C 2 PHE A 116 THR A 117 -1 O PHE A 116 N TYR A 95
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 2 2 Bytes