Header list of 1prs.pdb file
Complete list - r 2 2 Bytes
HEADER BINDING PROTEIN 25-MAR-94 1PRS TITLE NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN S TITLE 2 COMPLEXED WITH CALCIUM COMPND MOL_ID: 1; COMPND 2 MOLECULE: DEVELOPMENT-SPECIFIC PROTEIN S; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MYXOCOCCUS XANTHUS; SOURCE 3 ORGANISM_TAXID: 34 KEYWDS BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR S.BAGBY,T.S.HARVEY,S.G.EAGLE,S.INOUYE,M.IKURA REVDAT 3 02-MAR-22 1PRS 1 REMARK LINK REVDAT 2 24-FEB-09 1PRS 1 VERSN REVDAT 1 31-AUG-94 1PRS 0 JRNL AUTH S.BAGBY,T.S.HARVEY,S.G.EAGLE,S.INOUYE,M.IKURA JRNL TITL NMR-DERIVED THREE-DIMENSIONAL SOLUTION STRUCTURE OF PROTEIN JRNL TITL 2 S COMPLEXED WITH CALCIUM. JRNL REF STRUCTURE V. 2 107 1994 JRNL REFN ISSN 0969-2126 JRNL PMID 8081742 JRNL DOI 10.1016/S0969-2126(00)00013-7 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH S.BAGBY,T.S.HARVEY,S.G.EAGLE,S.INOUYE,M.IKURA REMARK 1 TITL STRUCTURAL SIMILARITY OF A DEVELOPMENTALLY REGULATED REMARK 1 TITL 2 BACTERIAL SPORE COAT PROTEIN TO BETAGAMMA-CRYSTALLINS OF THE REMARK 1 TITL 3 VERTEBRATE EYE LENS REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 91 4308 1994 REMARK 1 REFN ISSN 0027-8424 REMARK 1 REFERENCE 2 REMARK 1 AUTH S.BAGBY,T.S.HARVEY,L.E.KAY,S.G.EAGLE,S.INOUYE,M.IKURA REMARK 1 TITL UNUSUAL HELIX-CONTAINING GREEK KEYS IN DEVELOPMENT-SPECIFIC REMARK 1 TITL 2 CA2+-BINDING PROTEIN S. 1H, 15N AND 13C ASSIGNMENTS AND REMARK 1 TITL 3 SECONDARY STRUCTURE DETERMINED USING MULTIDIMENSIONAL DOUBLE REMARK 1 TITL 4 AND TRIPLE RESONANCE HETERONUCLEAR NMR SPECTROSCOPY REMARK 1 REF BIOCHEMISTRY V. 33 2409 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1PRS 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_1000175812. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : NULL REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : NULL REMARK 210 SPECTROMETER MODEL : NULL REMARK 210 SPECTROMETER MANUFACTURER : NULL REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : NULL REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 174 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 10 OE1 REMARK 620 2 GLU A 71 OE2 119.8 REMARK 620 3 GLU A 71 OE1 86.8 42.6 REMARK 620 N 1 2 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 175 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 99 OE2 REMARK 620 2 SER A 130 N 147.9 REMARK 620 3 SER A 130 OG 137.6 48.3 REMARK 620 4 THR A 159 OG1 71.8 140.2 104.3 REMARK 620 5 LEU A 160 N 115.4 77.2 106.4 87.2 REMARK 620 6 GLY A 161 N 66.9 94.2 140.9 113.7 68.0 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 174 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 175 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1PRR RELATED DB: PDB DBREF 1PRS A 1 173 UNP P02966 DESS_MYXXA 1 173 SEQRES 1 A 173 MET ALA ASN ILE THR VAL PHE TYR ASN GLU ASP PHE GLN SEQRES 2 A 173 GLY LYS GLN VAL ASP LEU PRO PRO GLY ASN TYR THR ARG SEQRES 3 A 173 ALA GLN LEU ALA ALA LEU GLY ILE GLU ASN ASN THR ILE SEQRES 4 A 173 SER SER VAL LYS VAL PRO PRO GLY VAL LYS ALA ILE LEU SEQRES 5 A 173 TYR GLN ASN ASP GLY PHE ALA GLY ASP GLN ILE GLU VAL SEQRES 6 A 173 VAL ALA ASN ALA GLU GLU LEU GLY PRO LEU ASN ASN ASN SEQRES 7 A 173 VAL SER SER ILE ARG VAL ILE SER VAL PRO VAL GLN PRO SEQRES 8 A 173 ARG ALA ARG PHE PHE TYR LYS GLU GLN PHE ASP GLY LYS SEQRES 9 A 173 GLU VAL ASP LEU PRO PRO GLY GLN TYR THR GLN ALA GLU SEQRES 10 A 173 LEU GLU ARG TYR GLY ILE ASP ASN ASN THR ILE SER SER SEQRES 11 A 173 VAL LYS PRO GLN GLY LEU ALA VAL VAL LEU PHE LYS ASN SEQRES 12 A 173 ASP ASN PHE SER GLY ASP THR LEU PRO VAL ASN SER ASP SEQRES 13 A 173 ALA PRO THR LEU GLY ALA MET ASN ASN ASN THR SER SER SEQRES 14 A 173 ILE ARG ILE SER HET CA A 174 1 HET CA A 175 1 HETNAM CA CALCIUM ION FORMUL 2 CA 2(CA 2+) HELIX 1 H1 ARG A 26 GLY A 33 1 8 HELIX 2 H2 GLN A 115 GLY A 122 1 8 SHEET 1 BN1 4 LYS A 15 PRO A 20 0 SHEET 2 BN1 4 ASN A 3 TYR A 8 -1 SHEET 3 BN1 4 SER A 41 VAL A 44 -1 SHEET 4 BN1 4 ASN A 68 GLU A 70 -1 SHEET 1 BN2 4 GLY A 22 TYR A 24 0 SHEET 2 BN2 4 SER A 81 SER A 86 -1 SHEET 3 BN2 4 VAL A 48 TYR A 53 -1 SHEET 4 BN2 4 ASP A 61 VAL A 65 -1 SHEET 1 BC1 4 LYS A 104 PRO A 109 0 SHEET 2 BC1 4 ARG A 92 TYR A 97 -1 SHEET 3 BC1 4 SER A 130 PRO A 133 -1 SHEET 4 BC1 4 ASP A 156 PRO A 158 -1 SHEET 1 BC2 4 GLY A 111 THR A 114 0 SHEET 2 BC2 4 SER A 169 SER A 173 -1 SHEET 3 BC2 4 ALA A 137 PHE A 141 -1 SHEET 4 BC2 4 ASP A 149 ASN A 154 -1 LINK OE1 GLU A 10 CA CA A 174 1555 1555 1.80 LINK OE2 GLU A 71 CA CA A 174 1555 1555 3.02 LINK OE1 GLU A 71 CA CA A 174 1555 1555 3.01 LINK OE2 GLU A 99 CA CA A 175 1555 1555 2.87 LINK N SER A 130 CA CA A 175 1555 1555 3.11 LINK OG SER A 130 CA CA A 175 1555 1555 3.24 LINK OG1 THR A 159 CA CA A 175 1555 1555 2.84 LINK N LEU A 160 CA CA A 175 1555 1555 1.92 LINK N GLY A 161 CA CA A 175 1555 1555 2.72 SITE 1 AC1 2 GLU A 10 GLU A 71 SITE 1 AC2 5 GLU A 99 SER A 130 THR A 159 LEU A 160 SITE 2 AC2 5 GLY A 161 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