Header list of 1ssn.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 07-JUN-98 1SSN TITLE STAPHYLOKINASE, SAKSTAR VARIANT, NMR, 20 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: STAPHYLOKINASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: SAK; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS; SOURCE 3 ORGANISM_TAXID: 1280; SOURCE 4 GENE: TAQ PROMOTOR; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMEX602SAKB; SOURCE 9 EXPRESSION_SYSTEM_GENE: TAQ PROMOTOR KEYWDS HYDROLASE, STAPHYLOKINASE EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR O.OHLENSCHLAGER,R.RAMACHANDRAN,K.H.GUHRS,B.SCHLOTT,L.R.BROWN REVDAT 3 02-MAR-22 1SSN 1 REMARK SEQADV REVDAT 2 24-FEB-09 1SSN 1 VERSN REVDAT 1 02-DEC-98 1SSN 0 JRNL AUTH O.OHLENSCHLAGER,R.RAMACHANDRAN,K.H.GUHRS,B.SCHLOTT,L.R.BROWN JRNL TITL NUCLEAR MAGNETIC RESONANCE SOLUTION STRUCTURE OF THE JRNL TITL 2 PLASMINOGEN-ACTIVATOR PROTEIN STAPHYLOKINASE. JRNL REF BIOCHEMISTRY V. 37 10635 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9692953 JRNL DOI 10.1021/BI980673I REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : AMBER REMARK 3 AUTHORS : PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM, REMARK 3 FERGUSON,SEIBEL,SINGH,WEINER,KOLLMAN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: ENERGY MINIMIZED DISTANCE GEOMETRY REMARK 3 STRUCTURES REMARK 4 REMARK 4 1SSN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000176496. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : WATER REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : INOVA750 REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERO-NUCLEAR NMR REMARK 210 SPECTROSCOPY ON A 15N- AND A 13C, 15N-LABELED SAMPLE 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 DBREF 1SSN A 1 136 UNP P68802 SAK_STAAU 28 163 SEQADV 1SSN SER A 34 UNP P68802 GLY 61 VARIANT SEQRES 1 A 136 SER SER SER PHE ASP LYS GLY LYS TYR LYS LYS GLY ASP SEQRES 2 A 136 ASP ALA SER TYR PHE GLU PRO THR GLY PRO TYR LEU MET SEQRES 3 A 136 VAL ASN VAL THR GLY VAL ASP SER LYS GLY ASN GLU LEU SEQRES 4 A 136 LEU SER PRO HIS TYR VAL GLU PHE PRO ILE LYS PRO GLY SEQRES 5 A 136 THR THR LEU THR LYS GLU LYS ILE GLU TYR TYR VAL GLU SEQRES 6 A 136 TRP ALA LEU ASP ALA THR ALA TYR LYS GLU PHE ARG VAL SEQRES 7 A 136 VAL GLU LEU ASP PRO SER ALA LYS ILE GLU VAL THR TYR SEQRES 8 A 136 TYR ASP LYS ASN LYS LYS LYS GLU GLU THR LYS SER PHE SEQRES 9 A 136 PRO ILE THR GLU LYS GLY PHE VAL VAL PRO ASP LEU SER SEQRES 10 A 136 GLU HIS ILE LYS ASN PRO GLY PHE ASN LEU ILE THR LYS SEQRES 11 A 136 VAL VAL ILE GLU LYS LYS HELIX 1 1 LYS A 10 GLY A 12 5 3 HELIX 2 2 LYS A 57 ASP A 69 5 13 SHEET 1 A 4 ASN A 37 LEU A 39 0 SHEET 2 A 4 TYR A 24 VAL A 32 -1 O GLY A 31 N LEU A 39 SHEET 3 A 4 GLY A 124 VAL A 132 1 N PHE A 125 O TYR A 24 SHEET 4 A 4 VAL A 78 GLU A 80 -1 N GLU A 80 O VAL A 132 SHEET 1 B 5 ASN A 37 LEU A 39 0 SHEET 2 B 5 TYR A 24 VAL A 32 -1 O GLY A 31 N LEU A 39 SHEET 3 B 5 GLY A 124 VAL A 132 1 N PHE A 125 O TYR A 24 SHEET 4 B 5 ILE A 87 THR A 90 -1 N GLU A 88 O ASN A 126 SHEET 5 B 5 LYS A 98 PHE A 104 -1 N PHE A 104 O ILE A 87 SHEET 1 C 2 THR A 53 LEU A 55 0 SHEET 2 C 2 PHE A 111 VAL A 113 -1 N PHE A 111 O LEU A 55 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