Header list of 1udm.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 01-MAY-03 1UDM TITLE SOLUTION STRUCTURE OF COACTOSIN-LIKE PROTEIN (COFILIN FAMILY) FROM MUS TITLE 2 MUSCULUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: COACTOSIN-LIKE PROTEIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: COFILIN-ADF; COMPND 5 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: RIKEN CDNA 2010004C08; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P020412-60; SOURCE 8 OTHER_DETAILS: CELL-FREE SYNTHESIS SYSTEM KEYWDS ACTIN BINDING PROTEIN, CYTOSKELETAL, RIKEN STRUCTURAL KEYWDS 2 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL GENOMICS, PROTEIN KEYWDS 3 BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR A.K.GORONCY,T.KIGAWA,S.KOSHIBA,N.KOBAYASHI,N.TOCHIO,M.INOUE, AUTHOR 2 S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 02-MAR-22 1UDM 1 REMARK SEQADV REVDAT 3 02-FEB-10 1UDM 1 JRNL REVDAT 2 24-FEB-09 1UDM 1 VERSN REVDAT 1 18-MAY-04 1UDM 0 JRNL AUTH A.K.GORONCY,S.KOSHIBA,N.TOCHIO,T.TOMIZAWA,M.SATO,M.INOUE, JRNL AUTH 2 S.WATANABE,Y.HAYASHIZAKI,A.TANAKA,T.KIGAWA,S.YOKOYAMA JRNL TITL NMR SOLUTION STRUCTURES OF ACTIN DEPOLYMERIZING FACTOR JRNL TITL 2 HOMOLOGY DOMAINS. JRNL REF PROTEIN SCI. V. 18 2384 2009 JRNL REFN ISSN 0961-8368 JRNL PMID 19768801 JRNL DOI 10.1002/PRO.248 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.13 REMARK 3 AUTHORS : BRUKER (XWINNMR), P.GUNTERT (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1UDM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-03. REMARK 100 THE DEPOSITION ID IS D_1000005704. 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 : 0.67MM COFILIN-ADF DOMAIN, 20MM REMARK 210 PHOSPHATE BUFFER, 100MM NACL, REMARK 210 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 : 800 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.801 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 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 ASP A 13 46.93 -81.16 REMARK 500 1 LYS A 14 -49.50 -23.07 REMARK 500 1 ALA A 76 -75.49 -84.46 REMARK 500 1 MET A 77 -74.73 -100.76 REMARK 500 1 PHE A 83 -171.04 53.55 REMARK 500 1 ALA A 84 128.30 -177.22 REMARK 500 1 THR A 101 -37.71 -36.81 REMARK 500 1 PHE A 115 -170.75 -52.40 REMARK 500 1 ALA A 116 -66.78 -97.70 REMARK 500 1 GLU A 128 105.87 -50.01 REMARK 500 1 GLU A 129 -30.91 -38.65 REMARK 500 1 ALA A 139 45.32 33.36 REMARK 500 1 TYR A 144 21.96 47.24 REMARK 500 2 ASP A 13 44.96 -89.03 REMARK 500 2 LYS A 14 -49.32 -22.41 REMARK 500 2 PRO A 45 102.48 -52.12 REMARK 500 2 THR A 101 -39.39 -34.87 REMARK 500 2 PHE A 115 -170.59 -53.18 REMARK 500 2 ALA A 116 -68.07 -95.67 REMARK 500 2 GLU A 128 106.35 -49.94 REMARK 500 2 GLU A 129 -33.68 -39.66 REMARK 500 3 ASP A 13 44.56 -89.59 REMARK 500 3 LYS A 14 -45.38 -24.61 REMARK 500 3 LEU A 23 -18.68 -49.35 REMARK 500 3 ALA A 30 -26.79 -39.20 REMARK 500 3 THR A 73 105.72 -170.64 REMARK 500 3 ASP A 75 -72.25 -97.17 REMARK 500 3 LYS A 79 22.80 42.92 REMARK 500 3 PHE A 83 -174.19 65.48 REMARK 500 3 ALA A 84 130.75 -177.29 REMARK 500 3 VAL A 93 151.79 -49.95 REMARK 500 3 PHE A 115 -167.95 -53.68 REMARK 500 3 GLU A 128 105.38 -50.31 REMARK 500 3 GLU A 129 -34.12 -39.63 REMARK 500 3 SER A 134 -38.41 -39.66 REMARK 500 4 ASP A 13 46.26 -84.86 REMARK 500 4 LYS A 14 -50.44 -22.22 REMARK 500 4 LEU A 23 -19.30 -47.63 REMARK 500 4 PRO A 45 106.02 -52.01 REMARK 500 4 ALA A 76 31.64 -83.31 REMARK 500 4 SER A 78 100.63 -169.15 REMARK 500 4 ARG A 80 -72.04 -101.88 REMARK 500 4 SER A 81 117.78 -170.96 REMARK 500 4 PHE A 115 -170.56 -53.10 REMARK 500 4 ALA A 116 -68.09 -99.22 REMARK 500 4 GLU A 128 105.94 -50.30 REMARK 500 4 GLU A 129 -34.54 -39.15 REMARK 500 4 ALA A 139 173.88 -52.43 REMARK 500 5 ALA A 9 -170.07 63.22 REMARK 500 5 ASP A 13 46.25 -85.26 REMARK 500 REMARK 500 THIS ENTRY HAS 241 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMK001003623.1 RELATED DB: TARGETDB DBREF 1UDM A 8 149 UNP Q9CQI6 COAC_MOUSE 1 142 SEQADV 1UDM GLY A 1 UNP Q9CQI6 CLONING ARTIFACT SEQADV 1UDM SER A 2 UNP Q9CQI6 CLONING ARTIFACT SEQADV 1UDM GLU A 3 UNP Q9CQI6 CLONING ARTIFACT SEQADV 1UDM GLY A 4 UNP Q9CQI6 CLONING ARTIFACT SEQADV 1UDM ALA A 5 UNP Q9CQI6 CLONING ARTIFACT SEQADV 1UDM ALA A 6 UNP Q9CQI6 CLONING ARTIFACT SEQADV 1UDM THR A 7 UNP Q9CQI6 CLONING ARTIFACT SEQRES 1 A 149 GLY SER GLU GLY ALA ALA THR MET ALA THR LYS ILE ASP SEQRES 2 A 149 LYS GLU ALA CYS ARG ALA ALA TYR ASN LEU VAL ARG ASP SEQRES 3 A 149 ASP GLY SER ALA VAL ILE TRP VAL THR PHE ARG TYR ASP SEQRES 4 A 149 GLY ALA THR ILE VAL PRO GLY ASP GLN GLY ALA ASP TYR SEQRES 5 A 149 GLN HIS PHE ILE GLN GLN CYS THR ASP ASP VAL ARG LEU SEQRES 6 A 149 PHE ALA PHE VAL ARG PHE THR THR GLY ASP ALA MET SER SEQRES 7 A 149 LYS ARG SER LYS PHE ALA LEU ILE THR TRP ILE GLY GLU SEQRES 8 A 149 ASP VAL SER GLY LEU GLN ARG ALA LYS THR GLY THR ASP SEQRES 9 A 149 LYS THR LEU VAL LYS GLU VAL VAL GLN ASN PHE ALA LYS SEQRES 10 A 149 GLU PHE VAL ILE SER ASP ARG LYS GLU LEU GLU GLU ASP SEQRES 11 A 149 PHE ILE ARG SER GLU LEU LYS LYS ALA GLY GLY ALA ASN SEQRES 12 A 149 TYR ASP ALA GLN SER GLU HELIX 1 1 ASP A 13 ASP A 26 1 14 HELIX 2 2 ASP A 51 GLN A 57 1 7 HELIX 3 3 SER A 94 GLY A 102 1 9 HELIX 4 4 ASP A 104 VAL A 112 1 9 HELIX 5 5 ASP A 123 GLU A 128 1 6 HELIX 6 6 GLU A 128 ALA A 139 1 12 SHEET 1 A 6 LYS A 11 ILE A 12 0 SHEET 2 A 6 THR A 42 GLY A 49 1 O ILE A 43 N LYS A 11 SHEET 3 A 6 TRP A 33 TYR A 38 -1 N ARG A 37 O VAL A 44 SHEET 4 A 6 ARG A 64 VAL A 69 -1 O PHE A 68 N VAL A 34 SHEET 5 A 6 ALA A 84 ILE A 89 -1 O TRP A 88 N LEU A 65 SHEET 6 A 6 GLU A 118 ILE A 121 1 O ILE A 121 N THR A 87 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