Header list of 2cou.pdb file
Complete list - r 9 2 Bytes
HEADER CELL CYCLE 18-MAY-05 2COU TITLE SOLUTION STRUCTURE OF THE SECOND BRCT DOMAIN OF EPITHELIAL CELL TITLE 2 TRANSFORMING 2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: ECT2 PROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: BRCA1 C-TURMINUS (BRCT) DOMAIN; COMPND 5 SYNONYM: EPITHELIAL CELL TRANSFORMING SEQUENCE 2 ONCOGENE; 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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: P041018-12; SOURCE 7 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS BRCT DOMAIN, ECT2, RHO GTPASE, STRUCTURAL GENOMICS, NPPSFA, NATIONAL KEYWDS 2 PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN KEYWDS 3 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, CELL CYCLE 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 2COU 1 REMARK SEQADV REVDAT 2 24-FEB-09 2COU 1 VERSN REVDAT 1 18-NOV-05 2COU 0 JRNL AUTH T.NAGASHIMA,F.HAYASHI,S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE SECOND BRCT DOMAIN OF EPITHELIAL JRNL TITL 2 CELL TRANSFORMING 2 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 2COU 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_1000024462. 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 : 1.02MM BRCT 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 : 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 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 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 77.27 -103.70 REMARK 500 1 ASP A 25 -26.88 -38.72 REMARK 500 1 LYS A 98 36.11 37.73 REMARK 500 2 ASP A 25 -34.89 -35.13 REMARK 500 2 SER A 82 -36.70 -35.00 REMARK 500 3 ASP A 47 169.27 -46.69 REMARK 500 3 THR A 59 -32.63 -130.32 REMARK 500 3 LYS A 61 -54.58 -132.88 REMARK 500 3 SER A 82 -38.03 -34.87 REMARK 500 3 THR A 92 -19.75 -48.90 REMARK 500 3 LYS A 98 41.85 -86.46 REMARK 500 3 PRO A 106 -175.02 -69.75 REMARK 500 4 PHE A 23 155.59 -48.45 REMARK 500 4 THR A 35 -31.65 -38.37 REMARK 500 4 ASP A 47 172.34 -49.34 REMARK 500 4 SER A 82 -33.23 -35.45 REMARK 500 4 ARG A 88 97.49 -59.92 REMARK 500 4 GLU A 97 42.13 -96.62 REMARK 500 4 ALA A 99 104.69 -57.81 REMARK 500 5 GLN A 14 116.88 -34.94 REMARK 500 5 ASP A 25 -34.25 -35.99 REMARK 500 5 THR A 35 -30.41 -37.29 REMARK 500 5 ARG A 49 -37.95 -35.46 REMARK 500 5 ASN A 58 -26.00 -38.92 REMARK 500 5 LYS A 61 -48.54 -130.66 REMARK 500 5 LEU A 95 107.74 -50.38 REMARK 500 5 GLU A 97 47.73 -108.14 REMARK 500 5 LYS A 98 53.03 35.44 REMARK 500 5 PRO A 106 92.46 -69.78 REMARK 500 6 ASP A 25 -39.19 -33.70 REMARK 500 6 ARG A 49 -30.47 -37.13 REMARK 500 6 SER A 82 -35.86 -37.22 REMARK 500 6 ARG A 88 104.34 -57.85 REMARK 500 6 GLU A 97 49.63 -80.44 REMARK 500 6 LYS A 98 43.17 34.34 REMARK 500 6 GLU A 103 39.77 71.27 REMARK 500 6 PRO A 106 2.81 -69.75 REMARK 500 6 SER A 107 141.48 -34.65 REMARK 500 6 SER A 108 38.10 70.16 REMARK 500 7 SER A 6 161.53 -49.24 REMARK 500 7 LYS A 9 143.59 -170.32 REMARK 500 7 ASP A 25 -33.64 -34.96 REMARK 500 7 SER A 82 -36.40 -35.27 REMARK 500 7 LYS A 98 48.61 -87.51 REMARK 500 7 ALA A 99 -60.66 -127.18 REMARK 500 7 SER A 107 -52.76 -126.58 REMARK 500 8 GLN A 14 124.39 -39.73 REMARK 500 8 ASP A 15 50.09 39.94 REMARK 500 8 LYS A 61 -60.13 -98.29 REMARK 500 8 SER A 82 -37.65 -38.05 REMARK 500 REMARK 500 THIS ENTRY HAS 124 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMI002020893.1 RELATED DB: TARGETDB DBREF 2COU A 8 103 UNP Q07139 ECT2_MOUSE 91 186 SEQADV 2COU GLY A 1 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 2 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 3 UNP Q07139 CLONING ARTIFACT SEQADV 2COU GLY A 4 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 5 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 6 UNP Q07139 CLONING ARTIFACT SEQADV 2COU GLY A 7 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 104 UNP Q07139 CLONING ARTIFACT SEQADV 2COU GLY A 105 UNP Q07139 CLONING ARTIFACT SEQADV 2COU PRO A 106 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 107 UNP Q07139 CLONING ARTIFACT SEQADV 2COU SER A 108 UNP Q07139 CLONING ARTIFACT SEQADV 2COU GLY A 109 UNP Q07139 CLONING ARTIFACT SEQRES 1 A 109 GLY SER SER GLY SER SER GLY PHE LYS VAL PRO PRO PHE SEQRES 2 A 109 GLN ASP CYS ILE LEU SER PHE LEU GLY PHE SER ASP GLU SEQRES 3 A 109 GLU LYS HIS SER MET GLU GLU MET THR GLU MET GLN GLY SEQRES 4 A 109 GLY SER TYR LEU PRO VAL GLY ASP GLU ARG CYS THR HIS SEQRES 5 A 109 LEU ILE VAL GLU GLU ASN THR VAL LYS ASP LEU PRO PHE SEQRES 6 A 109 GLU PRO SER LYS LYS LEU PHE VAL VAL LYS GLN GLU TRP SEQRES 7 A 109 PHE TRP GLY SER ILE GLN MET ASP ALA ARG ALA GLY GLU SEQRES 8 A 109 THR MET TYR LEU TYR GLU LYS ALA ASN THR PRO GLU SER SEQRES 9 A 109 GLY PRO SER SER GLY HELIX 1 1 SER A 24 GLY A 39 1 16 HELIX 2 2 LYS A 75 MET A 85 1 11 HELIX 3 3 GLY A 90 TYR A 94 5 5 SHEET 1 A 3 LEU A 18 LEU A 21 0 SHEET 2 A 3 HIS A 52 VAL A 55 1 O ILE A 54 N SER A 19 SHEET 3 A 3 PHE A 72 VAL A 74 1 O VAL A 74 N LEU A 53 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