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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