Header list of 2cpm.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 19-MAY-05 2CPM TITLE SOLUTION STRUCTURE OF THE R3H DOMAIN OF HUMAN SPERM-ASSOCIATED ANTIGEN TITLE 2 7 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPERM-ASSOCIATED ANTIGEN 7; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: R3H DOMAIN; COMPND 5 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: SPAG7; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P041101-24; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS R3H DOMAIN, STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN KEYWDS 2 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL KEYWDS 3 GENOMICS/PROTEOMICS INITIATIVE, RSGI, UNKNOWN FUNCTION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU,S.YOKOYAMA,RIKEN AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 3 09-MAR-22 2CPM 1 REMARK SEQADV REVDAT 2 24-FEB-09 2CPM 1 VERSN REVDAT 1 19-NOV-05 2CPM 0 JRNL AUTH T.NAGATA,Y.MUTO,M.INOUE,T.KIGAWA,T.TERADA,M.SHIROUZU, JRNL AUTH 2 S.YOKOYAMA JRNL TITL SOLUTION STRUCTURE OF THE R3H DOMAIN OF HUMAN JRNL TITL 2 SPERM-ASSOCIATED ANTIGEN 7 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 2CPM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAY-05. REMARK 100 THE DEPOSITION ID IS D_1000024482. 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 : 1.33MM 13C/15N-PROTEIN; 20MM D REMARK 210 -TRIS-HCL(PH7.0); 100MM NACL; REMARK 210 1MM D-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 : 700 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20030801/20031121, REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.925, REMARK 210 CYANA 2.0.17 REMARK 210 METHOD USED : TORSION ANGLE DYANAMICS, REMARK 210 SIMULATED ANNEALING 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 PRO A 72 89.02 -69.77 REMARK 500 2 PRO A 72 88.68 -69.77 REMARK 500 3 PRO A 72 83.58 -69.78 REMARK 500 4 PRO A 72 80.70 -69.78 REMARK 500 4 GLU A 77 -35.46 -38.12 REMARK 500 5 ASP A 62 104.72 -59.23 REMARK 500 5 PRO A 72 99.84 -69.74 REMARK 500 5 GLU A 77 -31.85 -39.80 REMARK 500 6 PRO A 72 89.92 -69.84 REMARK 500 7 PRO A 72 83.65 -69.79 REMARK 500 7 GLU A 77 -27.37 -37.82 REMARK 500 7 PRO A 127 0.82 -69.77 REMARK 500 8 ASP A 62 105.96 -59.81 REMARK 500 8 PRO A 72 92.28 -69.76 REMARK 500 8 GLU A 77 -34.34 -37.55 REMARK 500 8 PRO A 127 4.07 -69.76 REMARK 500 9 PRO A 72 92.17 -69.77 REMARK 500 9 GLU A 77 -32.74 -38.09 REMARK 500 10 PRO A 72 79.93 -69.72 REMARK 500 10 GLU A 77 -29.03 -38.52 REMARK 500 11 PRO A 72 81.43 -69.78 REMARK 500 12 PRO A 72 81.50 -69.76 REMARK 500 12 GLU A 77 -39.61 -36.82 REMARK 500 12 PRO A 127 -175.68 -69.77 REMARK 500 13 PRO A 72 79.98 -69.80 REMARK 500 14 PRO A 72 80.73 -69.83 REMARK 500 15 PRO A 72 80.20 -69.85 REMARK 500 16 PRO A 72 99.43 -69.83 REMARK 500 17 PRO A 72 95.55 -69.78 REMARK 500 17 GLU A 77 -38.53 -33.68 REMARK 500 18 PRO A 72 82.73 -69.81 REMARK 500 18 GLU A 77 -31.94 -39.83 REMARK 500 19 PRO A 72 83.28 -69.79 REMARK 500 19 GLU A 77 -30.17 -39.64 REMARK 500 20 PRO A 72 79.79 -69.78 REMARK 500 20 GLU A 77 -30.92 -38.99 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: HSI002012436.1 RELATED DB: TARGETDB DBREF 2CPM A 44 124 UNP O75391 SPAG7_HUMAN 44 124 SEQADV 2CPM GLY A 37 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 38 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 39 UNP O75391 CLONING ARTIFACT SEQADV 2CPM GLY A 40 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 41 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 42 UNP O75391 CLONING ARTIFACT SEQADV 2CPM GLY A 43 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 125 UNP O75391 CLONING ARTIFACT SEQADV 2CPM GLY A 126 UNP O75391 CLONING ARTIFACT SEQADV 2CPM PRO A 127 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 128 UNP O75391 CLONING ARTIFACT SEQADV 2CPM SER A 129 UNP O75391 CLONING ARTIFACT SEQADV 2CPM GLY A 130 UNP O75391 CLONING ARTIFACT SEQRES 1 A 94 GLY SER SER GLY SER SER GLY GLN LYS VAL GLU PHE ARG SEQRES 2 A 94 LYS ARG MET GLU LYS GLU VAL SER ASP PHE ILE GLN ASP SEQRES 3 A 94 SER GLY GLN ILE LYS LYS LYS PHE GLN PRO MET ASN LYS SEQRES 4 A 94 ILE GLU ARG SER ILE LEU HIS ASP VAL VAL GLU VAL ALA SEQRES 5 A 94 GLY LEU THR SER PHE SER PHE GLY GLU ASP ASP ASP CYS SEQRES 6 A 94 ARG TYR VAL MET ILE PHE LYS LYS GLU PHE ALA PRO SER SEQRES 7 A 94 ASP GLU GLU LEU ASP SER TYR ARG ARG GLY SER GLY PRO SEQRES 8 A 94 SER SER GLY HELIX 1 1 VAL A 46 GLN A 61 1 16 HELIX 2 2 GLU A 77 ALA A 88 1 12 HELIX 3 3 ASP A 115 ARG A 123 1 9 SHEET 1 A 3 LYS A 67 LYS A 69 0 SHEET 2 A 3 TYR A 103 PHE A 107 -1 O ILE A 106 N LYS A 68 SHEET 3 A 3 THR A 91 PHE A 95 -1 N PHE A 93 O MET A 105 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