Header list of 2d9w.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 13-DEC-05 2D9W TITLE SOLUTION STRUCTURE OF THE PH DOMAIN OF DOCKING PROTEIN 2 FROM HUMAN COMPND MOL_ID: 1; COMPND 2 MOLECULE: DOCKING PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PH DOMAIN; COMPND 5 SYNONYM: DOWNSTREAM OF TYROSINE KINASE 2, P56DOK-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: DOK2; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P050302-66; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PH DOMAIN, DOCKING PROTEIN 2, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2D9W 1 REMARK SEQADV REVDAT 2 24-FEB-09 2D9W 1 VERSN REVDAT 1 13-JUN-06 2D9W 0 JRNL AUTH H.LI,T.TOMIZAWA,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE PH DOMAIN OF DOCKING PROTEIN 2 JRNL TITL 2 FROM HUMAN 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 2D9W 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_1000025167. 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 : 0.93MM PH DOMAIN U-15N, 13C; REMARK 210 20MM D-TRIS-HCL(PH 7.0); 100MM REMARK 210 NACL; 1MM D-DTT; 0.02% NAN3; 90% REMARK 210 H2O, 10% 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 0.932, 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 SER A 6 -60.54 -103.79 REMARK 500 1 ASP A 10 97.74 -61.84 REMARK 500 1 GLN A 24 -58.12 -129.57 REMARK 500 1 PRO A 54 -167.94 -69.82 REMARK 500 1 PRO A 57 90.88 -69.82 REMARK 500 1 ARG A 68 109.56 -49.80 REMARK 500 1 CYS A 72 102.98 -45.86 REMARK 500 1 ALA A 82 178.02 -59.10 REMARK 500 1 SER A 84 150.37 -37.59 REMARK 500 1 LYS A 96 -37.45 -34.76 REMARK 500 1 TRP A 112 -72.91 -43.13 REMARK 500 1 LEU A 119 -62.87 -93.37 REMARK 500 2 SER A 3 41.83 -96.85 REMARK 500 2 GLU A 55 26.76 42.29 REMARK 500 2 LYS A 56 144.97 -36.30 REMARK 500 2 ALA A 62 42.69 -100.12 REMARK 500 2 CYS A 72 96.30 -50.56 REMARK 500 2 ALA A 78 49.31 -93.95 REMARK 500 2 LEU A 93 106.22 -163.72 REMARK 500 2 SER A 122 79.73 -69.07 REMARK 500 2 PRO A 124 -165.98 -69.75 REMARK 500 3 SER A 2 41.78 -98.42 REMARK 500 3 MET A 8 25.85 39.24 REMARK 500 3 ALA A 12 144.04 -36.67 REMARK 500 3 GLN A 23 44.06 -105.76 REMARK 500 3 THR A 25 -72.19 -85.64 REMARK 500 3 LYS A 56 145.65 -39.47 REMARK 500 3 ARG A 59 150.75 -49.42 REMARK 500 3 ALA A 63 145.21 -38.54 REMARK 500 3 CYS A 72 104.13 -44.50 REMARK 500 3 GLU A 81 -32.62 -39.41 REMARK 500 3 SER A 84 148.17 -36.46 REMARK 500 3 LYS A 96 -34.01 -37.24 REMARK 500 3 ALA A 106 -28.91 -36.95 REMARK 500 3 TRP A 112 -70.71 -39.06 REMARK 500 3 PRO A 124 1.77 -69.84 REMARK 500 3 SER A 125 130.13 -34.70 REMARK 500 4 PHE A 26 113.49 -38.18 REMARK 500 4 ALA A 82 144.84 -35.63 REMARK 500 4 SER A 84 152.00 -37.52 REMARK 500 4 PRO A 85 -164.30 -69.75 REMARK 500 4 ALA A 106 -33.39 -34.10 REMARK 500 4 TRP A 112 -70.72 -34.45 REMARK 500 5 CYS A 43 90.90 -62.54 REMARK 500 5 PRO A 54 -167.62 -69.72 REMARK 500 5 PRO A 57 96.87 -69.72 REMARK 500 5 ARG A 59 -34.15 -130.20 REMARK 500 5 CYS A 72 102.01 -54.45 REMARK 500 5 ALA A 82 155.54 -40.89 REMARK 500 5 SER A 84 152.97 -44.22 REMARK 500 REMARK 500 THIS ENTRY HAS 228 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSO002002623.1 RELATED DB: TARGETDB DBREF 2D9W A 8 121 UNP O60496 DOK2_HUMAN 1 114 SEQADV 2D9W GLY A 1 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 2 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 3 UNP O60496 CLONING ARTIFACT SEQADV 2D9W GLY A 4 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 5 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 6 UNP O60496 CLONING ARTIFACT SEQADV 2D9W GLY A 7 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 122 UNP O60496 CLONING ARTIFACT SEQADV 2D9W GLY A 123 UNP O60496 CLONING ARTIFACT SEQADV 2D9W PRO A 124 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 125 UNP O60496 CLONING ARTIFACT SEQADV 2D9W SER A 126 UNP O60496 CLONING ARTIFACT SEQADV 2D9W GLY A 127 UNP O60496 CLONING ARTIFACT SEQRES 1 A 127 GLY SER SER GLY SER SER GLY MET GLY ASP GLY ALA VAL SEQRES 2 A 127 LYS GLN GLY PHE LEU TYR LEU GLN GLN GLN GLN THR PHE SEQRES 3 A 127 GLY LYS LYS TRP ARG ARG PHE GLY ALA SER LEU TYR GLY SEQRES 4 A 127 GLY SER ASP CYS ALA LEU ALA ARG LEU GLU LEU GLN GLU SEQRES 5 A 127 GLY PRO GLU LYS PRO ARG ARG CYS GLU ALA ALA ARG LYS SEQRES 6 A 127 VAL ILE ARG LEU SER ASP CYS LEU ARG VAL ALA GLU ALA SEQRES 7 A 127 GLY GLY GLU ALA SER SER PRO ARG ASP THR SER ALA PHE SEQRES 8 A 127 PHE LEU GLU THR LYS GLU ARG LEU TYR LEU LEU ALA ALA SEQRES 9 A 127 PRO ALA ALA GLU ARG GLY ASP TRP VAL GLN ALA ILE CYS SEQRES 10 A 127 LEU LEU ALA PHE SER GLY PRO SER SER GLY HELIX 1 1 ALA A 106 ALA A 120 1 15 SHEET 1 A 7 ARG A 64 ILE A 67 0 SHEET 2 A 7 ARG A 47 GLN A 51 -1 N LEU A 48 O ILE A 67 SHEET 3 A 7 ARG A 32 TYR A 38 -1 N SER A 36 O GLU A 49 SHEET 4 A 7 LYS A 14 LEU A 20 -1 N LYS A 14 O LEU A 37 SHEET 5 A 7 LEU A 99 ALA A 104 -1 O ALA A 103 N TYR A 19 SHEET 6 A 7 SER A 89 THR A 95 -1 N SER A 89 O ALA A 104 SHEET 7 A 7 CYS A 72 GLU A 77 -1 N ALA A 76 O PHE A 92 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