Header list of 2dbc.pdb file
Complete list - r 9 2 Bytes
HEADER SIGNALING PROTEIN 15-DEC-05 2DBC TITLE SOLUTION STRUCTURE OF THE THIOREDOXIN-LIKE DOMAIN OF PHOSDUCIN-LIKE TITLE 2 PROTEIN 2(PDCL2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: UNNAMED PROTEIN PRODUCT; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: THIOREDOXIN-LIKE DOMAIN, RESIDUES 8-129; COMPND 5 SYNONYM: PDCL2; COMPND 6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: PDCL2; SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P050302-72; SOURCE 9 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS KEYWDS PHOSDUCIN-LIKE PROTEIN, THIOREDOXIN_FOLD, STRUCTURAL GENOMICS, KEYWDS 2 NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL KEYWDS 3 ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 4 SIGNALING PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.KUROSAKI,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2DBC 1 REMARK SEQADV REVDAT 2 24-FEB-09 2DBC 1 VERSN REVDAT 1 15-JUN-06 2DBC 0 JRNL AUTH C.KUROSAKI,M.YOSHIDA,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE THIOREDOXIN-LIKE DOMAIN OF JRNL TITL 2 PHOSDUCIN-LIKE PROTEIN 2(PDCL2) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 2.0.17 REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2DBC 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_1000025213. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.31MM 13C, 15N-LABELED PROTEIN; 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 : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.933, 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 GLU A 23 -74.51 -95.25 REMARK 500 1 GLU A 28 174.51 -56.82 REMARK 500 1 ASP A 30 45.13 -84.92 REMARK 500 1 VAL A 69 33.06 -83.81 REMARK 500 1 GLU A 74 -67.26 -97.35 REMARK 500 1 TYR A 76 105.25 -41.90 REMARK 500 1 CYS A 80 -50.33 -125.93 REMARK 500 1 LYS A 88 -60.87 -109.18 REMARK 500 1 GLU A 127 123.57 -39.61 REMARK 500 1 SER A 133 -51.68 -122.02 REMARK 500 2 GLU A 11 143.58 -174.85 REMARK 500 2 GLU A 23 -70.54 -105.15 REMARK 500 2 VAL A 24 -71.23 -65.62 REMARK 500 2 ASN A 26 31.99 -84.04 REMARK 500 2 GLU A 28 156.66 -44.35 REMARK 500 2 CYS A 72 -71.93 -38.10 REMARK 500 2 HIS A 77 -67.41 -123.15 REMARK 500 2 ASP A 78 -32.67 -132.07 REMARK 500 2 GLU A 127 141.24 -36.70 REMARK 500 3 SER A 2 108.06 -50.49 REMARK 500 3 SER A 3 42.84 39.09 REMARK 500 3 TYR A 20 -39.00 -36.13 REMARK 500 3 VAL A 21 -71.23 -77.75 REMARK 500 3 GLU A 23 -72.01 -94.42 REMARK 500 3 VAL A 24 -71.22 -69.54 REMARK 500 3 ASN A 26 32.97 -84.82 REMARK 500 3 GLU A 28 171.33 -46.14 REMARK 500 3 ASP A 30 46.81 34.44 REMARK 500 3 ASN A 70 113.73 -35.27 REMARK 500 3 CYS A 72 -60.46 -130.19 REMARK 500 3 HIS A 75 36.24 -97.10 REMARK 500 3 LYS A 88 -63.60 -109.54 REMARK 500 3 LEU A 126 128.72 -39.99 REMARK 500 3 GLU A 127 141.80 -37.32 REMARK 500 4 GLU A 23 -74.99 -99.54 REMARK 500 4 ASN A 26 34.24 -83.39 REMARK 500 4 GLU A 28 -174.05 -53.05 REMARK 500 4 ASP A 30 39.23 35.50 REMARK 500 4 VAL A 69 45.03 -81.55 REMARK 500 4 CYS A 72 -62.11 -90.43 REMARK 500 4 HIS A 75 38.92 -82.43 REMARK 500 4 CYS A 80 -41.65 -134.41 REMARK 500 4 PRO A 132 -165.02 -69.82 REMARK 500 4 SER A 133 104.58 -52.46 REMARK 500 4 SER A 134 46.71 37.30 REMARK 500 5 SER A 3 152.10 -46.11 REMARK 500 5 VAL A 21 -72.57 -71.60 REMARK 500 5 GLU A 23 -73.95 -94.90 REMARK 500 5 GLU A 28 160.64 -48.90 REMARK 500 5 ASP A 30 49.16 35.38 REMARK 500 REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007010002.1 RELATED DB: TARGETDB DBREF 2DBC A 8 129 UNP Q9DA99 Q9DA99_MOUSE 40 161 SEQADV 2DBC GLY A 1 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 2 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 3 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC GLY A 4 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 5 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 6 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC GLY A 7 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 130 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC GLY A 131 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC PRO A 132 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 133 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC SER A 134 UNP Q9DA99 CLONING ARTIFACT SEQADV 2DBC GLY A 135 UNP Q9DA99 CLONING ARTIFACT SEQRES 1 A 135 GLY SER SER GLY SER SER GLY LYS PHE GLY GLU LEU ARG SEQRES 2 A 135 GLU ILE SER GLY ASN GLN TYR VAL ASN GLU VAL THR ASN SEQRES 3 A 135 ALA GLU LYS ASP LEU TRP VAL VAL ILE HIS LEU TYR ARG SEQRES 4 A 135 SER SER VAL PRO MET CYS LEU VAL VAL ASN GLN HIS LEU SEQRES 5 A 135 SER VAL LEU ALA ARG LYS PHE PRO GLU THR LYS PHE VAL SEQRES 6 A 135 LYS ALA ILE VAL ASN SER CYS ILE GLU HIS TYR HIS ASP SEQRES 7 A 135 ASN CYS LEU PRO THR ILE PHE VAL TYR LYS ASN GLY GLN SEQRES 8 A 135 ILE GLU GLY LYS PHE ILE GLY ILE ILE GLU CYS GLY GLY SEQRES 9 A 135 ILE ASN LEU LYS LEU GLU GLU LEU GLU TRP LYS LEU SER SEQRES 10 A 135 GLU VAL GLY ALA ILE GLN SER ASP LEU GLU GLU ASN SER SEQRES 11 A 135 GLY PRO SER SER GLY HELIX 1 1 SER A 16 VAL A 24 1 9 HELIX 2 2 VAL A 42 PHE A 59 1 18 HELIX 3 3 LYS A 108 GLY A 120 1 13 SHEET 1 A 5 ARG A 13 GLU A 14 0 SHEET 2 A 5 THR A 62 ALA A 67 1 O LYS A 66 N ARG A 13 SHEET 3 A 5 TRP A 32 LEU A 37 1 N VAL A 34 O LYS A 63 SHEET 4 A 5 THR A 83 TYR A 87 -1 O TYR A 87 N VAL A 33 SHEET 5 A 5 GLY A 94 ILE A 97 -1 O PHE A 96 N ILE A 84 CISPEP 1 LEU A 81 PRO A 82 1 -0.18 CISPEP 2 LEU A 81 PRO A 82 2 -0.15 CISPEP 3 LEU A 81 PRO A 82 3 -0.12 CISPEP 4 LEU A 81 PRO A 82 4 -0.16 CISPEP 5 LEU A 81 PRO A 82 5 -0.09 CISPEP 6 LEU A 81 PRO A 82 6 -0.15 CISPEP 7 LEU A 81 PRO A 82 7 -0.15 CISPEP 8 LEU A 81 PRO A 82 8 -0.16 CISPEP 9 LEU A 81 PRO A 82 9 -0.09 CISPEP 10 LEU A 81 PRO A 82 10 -0.24 CISPEP 11 LEU A 81 PRO A 82 11 -0.11 CISPEP 12 LEU A 81 PRO A 82 12 -0.18 CISPEP 13 LEU A 81 PRO A 82 13 -0.08 CISPEP 14 LEU A 81 PRO A 82 14 -0.16 CISPEP 15 LEU A 81 PRO A 82 15 -0.14 CISPEP 16 LEU A 81 PRO A 82 16 -0.14 CISPEP 17 LEU A 81 PRO A 82 17 -0.16 CISPEP 18 LEU A 81 PRO A 82 18 -0.16 CISPEP 19 LEU A 81 PRO A 82 19 -0.17 CISPEP 20 LEU A 81 PRO A 82 20 -0.10 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