Header list of 2cr9.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 20-MAY-05 2CR9 TITLE SOLUTION STRUCTURE OF WGR DOMAIN OF POLY(ADP-RIBOSE) POLYMERASE-1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: POLY [ADP-RIBOSE] POLYMERASE-1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: WGR DOMAIN; COMPND 5 SYNONYM: PARP-1, ADPRT, NAD+, ADP-RIBOSYLTRANSFERASE-1, POLY[ADP- COMPND 6 RIBOSE] SYNTHETASE-1; COMPND 7 EC: 2.4.2.30; COMPND 8 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: PARP1, ADPRT, PPOL; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040517-11; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PARP, DNA REPAIR, NECROSIS, APOPTOSIS, STRUCTURAL GENOMICS, NPPSFA, KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSFERASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS AUTHOR 2 INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CR9 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CR9 1 VERSN REVDAT 1 20-NOV-05 2CR9 0 JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF WGR DOMAIN OF POLY(ADP-RIBOSE) JRNL TITL 2 POLYMERASE-1 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 1.0.7 REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2CR9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024536. 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 : 1.15MM WGR DOMAIN U-13C,15N; REMARK 210 20MM TRISHCL, 100MM NACL, 1MM REMARK 210 DTT, 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : INOVA 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 1.0.7 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 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O LEU A 49 H SER A 58 1.45 REMARK 500 H LEU A 36 O LEU A 64 1.52 REMARK 500 O HIS A 103 H LEU A 107 1.53 REMARK 500 O GLU A 98 H GLU A 102 1.60 REMARK 500 H ASP A 67 O ARG A 72 1.60 REMARK 500 REMARK 500 REMARK: NULL 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 2 152.64 178.22 REMARK 500 1 SER A 9 124.06 -170.33 REMARK 500 1 LYS A 14 80.55 62.15 REMARK 500 1 SER A 32 -54.83 -132.82 REMARK 500 1 PHE A 43 50.25 -90.78 REMARK 500 1 ASP A 68 44.69 -108.90 REMARK 500 1 GLU A 70 -54.48 -128.62 REMARK 500 1 ASN A 71 86.29 170.62 REMARK 500 1 ARG A 81 172.97 -59.25 REMARK 500 1 ASN A 120 128.03 62.73 REMARK 500 1 LYS A 123 93.10 -69.37 REMARK 500 1 LYS A 126 -41.96 86.36 REMARK 500 1 LEU A 131 -81.32 -72.43 REMARK 500 1 SER A 137 141.43 68.38 REMARK 500 1 SER A 138 161.88 58.13 REMARK 500 2 SER A 2 -59.00 -150.24 REMARK 500 2 SER A 3 167.90 57.48 REMARK 500 2 ARG A 12 86.97 -153.74 REMARK 500 2 LYS A 14 175.61 -58.98 REMARK 500 2 LEU A 17 -72.11 -63.82 REMARK 500 2 LYS A 18 -72.87 -43.91 REMARK 500 2 SER A 32 -60.82 -133.32 REMARK 500 2 PHE A 43 49.49 -88.58 REMARK 500 2 GLU A 70 78.64 59.85 REMARK 500 2 ASN A 71 -54.19 -165.32 REMARK 500 2 SER A 118 69.28 -154.71 REMARK 500 2 LYS A 119 -177.53 51.60 REMARK 500 2 ASN A 120 155.36 -41.58 REMARK 500 2 LYS A 123 93.46 -67.71 REMARK 500 2 LYS A 126 -1.08 78.40 REMARK 500 2 LEU A 131 -76.50 -68.12 REMARK 500 2 GLU A 132 90.44 -62.58 REMARK 500 2 SER A 134 101.38 175.04 REMARK 500 2 SER A 138 -60.66 179.22 REMARK 500 3 SER A 3 103.40 -178.31 REMARK 500 3 SER A 5 136.32 179.86 REMARK 500 3 LYS A 8 125.42 64.56 REMARK 500 3 SER A 9 105.80 168.65 REMARK 500 3 GLU A 10 151.08 59.80 REMARK 500 3 LEU A 15 124.01 -174.43 REMARK 500 3 LEU A 17 -65.75 72.88 REMARK 500 3 LYS A 18 114.95 -39.59 REMARK 500 3 SER A 32 -55.24 -138.72 REMARK 500 3 LYS A 69 54.86 -158.85 REMARK 500 3 GLU A 70 -110.14 -134.56 REMARK 500 3 ASN A 71 59.57 -179.16 REMARK 500 3 VAL A 82 -79.70 69.86 REMARK 500 3 THR A 84 -179.49 -52.18 REMARK 500 3 ILE A 86 155.09 -43.36 REMARK 500 3 SER A 118 -49.61 -134.57 REMARK 500 REMARK 500 THIS ENTRY HAS 314 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: HSS001003531.1 RELATED DB: TARGETDB DBREF 2CR9 A 8 133 UNP P09874 PARP1_HUMAN 517 642 SEQADV 2CR9 GLY A 1 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 2 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 3 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 GLY A 4 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 5 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 6 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 GLY A 7 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 134 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 GLY A 135 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 PRO A 136 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 137 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 SER A 138 UNP P09874 CLONING ARTIFACT SEQADV 2CR9 GLY A 139 UNP P09874 CLONING ARTIFACT SEQRES 1 A 139 GLY SER SER GLY SER SER GLY LYS SER GLU LYS ARG MET SEQRES 2 A 139 LYS LEU THR LEU LYS GLY GLY ALA ALA VAL ASP PRO ASP SEQRES 3 A 139 SER GLY LEU GLU HIS SER ALA HIS VAL LEU GLU LYS GLY SEQRES 4 A 139 GLY LYS VAL PHE SER ALA THR LEU GLY LEU VAL ASP ILE SEQRES 5 A 139 VAL LYS GLY THR ASN SER TYR TYR LYS LEU GLN LEU LEU SEQRES 6 A 139 GLU ASP ASP LYS GLU ASN ARG TYR TRP ILE PHE ARG SER SEQRES 7 A 139 TRP GLY ARG VAL GLY THR VAL ILE GLY SER ASN LYS LEU SEQRES 8 A 139 GLU GLN MET PRO SER LYS GLU ASP ALA ILE GLU HIS PHE SEQRES 9 A 139 MET LYS LEU TYR GLU GLU LYS THR GLY ASN ALA TRP HIS SEQRES 10 A 139 SER LYS ASN PHE THR LYS TYR PRO LYS LYS PHE TYR PRO SEQRES 11 A 139 LEU GLU ILE SER GLY PRO SER SER GLY HELIX 1 1 SER A 96 THR A 112 1 17 SHEET 1 A 4 ALA A 33 VAL A 35 0 SHEET 2 A 4 ASN A 57 ASP A 67 -1 O GLU A 66 N HIS A 34 SHEET 3 A 4 ARG A 72 TRP A 79 -1 O ARG A 72 N ASP A 67 SHEET 4 A 4 SER A 88 MET A 94 -1 O MET A 94 N TYR A 73 SHEET 1 B 4 ALA A 33 VAL A 35 0 SHEET 2 B 4 ASN A 57 ASP A 67 -1 O GLU A 66 N HIS A 34 SHEET 3 B 4 SER A 44 VAL A 50 -1 N LEU A 49 O SER A 58 SHEET 4 B 4 TYR A 129 PRO A 130 -1 O TYR A 129 N GLY A 48 SHEET 1 C 2 GLU A 37 LYS A 38 0 SHEET 2 C 2 LYS A 41 VAL A 42 -1 O LYS A 41 N LYS A 38 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