Header list of 1pis.pdb file
Complete list - b 23 2 Bytes
HEADER CARBOXYLIC ESTER HYDROLASE 22-DEC-94 1PIS
TITLE SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE A2;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.4;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: PANCREAS
KEYWDS PHOSPHOLIPASE A2, PHOSPHATIDE-2-ACYL-HYDROLASE, PLA2, CARBOXYLIC
KEYWDS 2 ESTER HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.D.VAN DEN BERG,M.TESSARI,G.H.DE HAAS,H.M.VERHEIJ,R.BOELENS,
AUTHOR 2 R.KAPTEIN
REVDAT 3 23-FEB-22 1PIS 1 REMARK LINK
REVDAT 2 24-FEB-09 1PIS 1 VERSN
REVDAT 1 03-JUN-95 1PIS 0
JRNL AUTH B.VAN DEN BERG,M.TESSARI,G.H.DE HAAS,H.M.VERHEIJ,R.BOELENS,
JRNL AUTH 2 R.KAPTEIN
JRNL TITL SOLUTION STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2.
JRNL REF EMBO J. V. 14 4123 1995
JRNL REFN ISSN 0261-4189
JRNL PMID 7556053
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PIS 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_1000175704.
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 : 20
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 125 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 28 O
REMARK 620 2 GLY A 30 O 84.3
REMARK 620 3 GLY A 32 O 117.4 93.1
REMARK 620 4 GLU A 46 OE1 128.4 131.3 99.0
REMARK 620 5 ASP A 49 OD1 113.5 69.0 123.5 65.0
REMARK 620 6 ASP A 49 OD2 69.7 58.7 151.0 96.1 44.1
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 125
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PIR RELATED DB: PDB
DBREF 1PIS A 1 124 UNP P00592 PA21B_PIG 23 146
SEQRES 1 A 124 ALA LEU TRP GLN PHE ARG SER MET ILE LYS CYS ALA ILE
SEQRES 2 A 124 PRO GLY SER HIS PRO LEU MET ASP PHE ASN ASN TYR GLY
SEQRES 3 A 124 CYS TYR CYS GLY LEU GLY GLY SER GLY THR PRO VAL ASP
SEQRES 4 A 124 GLU LEU ASP ARG CYS CYS GLU THR HIS ASP ASN CYS TYR
SEQRES 5 A 124 ARG ASP ALA LYS ASN LEU ASP SER CYS LYS PHE LEU VAL
SEQRES 6 A 124 ASP ASN PRO TYR THR GLU SER TYR SER TYR SER CYS SER
SEQRES 7 A 124 ASN THR GLU ILE THR CYS ASN SER LYS ASN ASN ALA CYS
SEQRES 8 A 124 GLU ALA PHE ILE CYS ASN CYS ASP ARG ASN ALA ALA ILE
SEQRES 9 A 124 CYS PHE SER LYS ALA PRO TYR ASN LYS GLU HIS LYS ASN
SEQRES 10 A 124 LEU ASP THR LYS LYS TYR CYS
HET CA A 125 1
HETNAM CA CALCIUM ION
FORMUL 2 CA CA 2+
HELIX 1 1 TRP A 3 CYS A 11 1 9
HELIX 2 2 LEU A 19 PHE A 22 1 4
HELIX 3 3 GLU A 40 ALA A 55 1 16
HELIX 4 4 CYS A 91 CYS A 98 1 8
HELIX 5 5 ARG A 100 LYS A 108 1 9
SSBOND 1 CYS A 11 CYS A 77 1555 1555 1.98
SSBOND 2 CYS A 27 CYS A 124 1555 1555 2.01
SSBOND 3 CYS A 29 CYS A 45 1555 1555 2.00
SSBOND 4 CYS A 44 CYS A 105 1555 1555 2.00
SSBOND 5 CYS A 51 CYS A 98 1555 1555 1.98
SSBOND 6 CYS A 61 CYS A 91 1555 1555 1.99
SSBOND 7 CYS A 84 CYS A 96 1555 1555 1.98
LINK O TYR A 28 CA CA A 125 1555 1555 3.04
LINK O GLY A 30 CA CA A 125 1555 1555 3.04
LINK O GLY A 32 CA CA A 125 1555 1555 2.96
LINK OE1 GLU A 46 CA CA A 125 1555 1555 3.26
LINK OD1 ASP A 49 CA CA A 125 1555 1555 3.04
LINK OD2 ASP A 49 CA CA A 125 1555 1555 3.07
SITE 1 AC1 5 TYR A 28 GLY A 30 GLY A 32 GLU A 46
SITE 2 AC1 5 ASP A 49
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 - b 23 2 Bytes