HEADER HYDROLASE 07-SEP-92 1POC COMPND PHOSPHOLIPASE A2 (E.C.3.1.1.4) COMPLEX WITH THE COMPND 2 TRANSITION-STATE ANALOGUE SOURCE EUROPEAN HONEYBEE (APIS MELLIFERA) AUTHOR D.L.SCOTT,Z.OTWINOWSKI,P.B.SIGLER REVDAT 1 31-OCT-93 1POC 0 JRNL AUTH D.L.SCOTT,Z.OTWINOWSKI,M.H.GELB,P.B.SIGLER JRNL TITL CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 JRNL TITL 2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE JRNL REF SCIENCE V. 250 1563 1990 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 038 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.L.SCOTT,S.P.WHITE,Z.OTWINOWSKI,W.YUAN,M.H.GELB, REMARK 1 AUTH 2 P.B.SIGLER REMARK 1 TITL INTERFACIAL CATALYSIS: THE MECHANISM OF REMARK 1 TITL 2 PHOSPHOLIPASE A2 REMARK 1 REF SCIENCE V. 250 1541 1990 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 038 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM 1 X-PLOR REMARK 3 AUTHORS 1 BRUNGER REMARK 3 PROGRAM 2 PROFFT REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON,FINZEL REMARK 3 R VALUE 0.192 REMARK 3 RMSD BOND DISTANCES 0.017 ANGSTROMS REMARK 3 RMSD BOND ANGLES 2.10 DEGREES REMARK 4 REMARK 4 DIC8(2PH)PE = L-1-O-OCTYL-2-HEPTYLPHOSPHONYL-SN-GLYCERO-3 REMARK 4 PHOSPHOETHANOLAMINE. SEQRES 1 134 ILE ILE TYR PRO GLY THR LEU TRP CYS GLY HIS GLY ASN SEQRES 2 134 LYS SER SER GLY PRO ASN GLU LEU GLY ARG PHE LYS HIS SEQRES 3 134 THR ASP ALA CYS CYS ARG THR HIS ASP MET CYS PRO ASP SEQRES 4 134 VAL MET SER ALA GLY GLU SER LYS HIS GLY LEU THR ASN SEQRES 5 134 THR ALA SER HIS THR ARG LEU SER CYS ASP CYS ASP ASP SEQRES 6 134 LYS PHE TYR ASP CYS LEU LYS ASN SER ALA ASP THR ILE SEQRES 7 134 SER SER TYR PHE VAL GLY LYS MET TYR PHE ASN LEU ILE SEQRES 8 134 ASP THR LYS CYS TYR LYS LEU GLU HIS PRO VAL THR GLY SEQRES 9 134 CYS GLY GLU ARG THR GLU GLY ARG CYS LEU HIS TYR THR SEQRES 10 134 VAL ASP LYS SER LYS PRO LYS VAL TYR GLN TRP PHE ASP SEQRES 11 134 LEU ARG LYS TYR HET CA 501 1 CALCIUM +2 COUNTER ION HET GEL 420 31 DIC8(2PH)PE - SEE REMARK 4 FORMUL 2 CA CA1 FORMUL 3 GEL C20 H41 N1 O8 P2 FORMUL 4 HOH *80(H2 O1) HELIX 1 H1 PHE 24 CYS 37 1 HELIX 2 H2 CYS 61 SER 74 1 HELIX 3 H3 ASP 76 ASN 89 1 SSBOND 1 CYS 9 CYS 31 SSBOND 2 CYS 30 CYS 70 SSBOND 3 CYS 37 CYS 63 SSBOND 4 CYS 61 CYS 95 SSBOND 5 CYS 105 CYS 113 SITE 1 CA1 4 TRP 8 GLY 10 GLY 12 ASP 35 CRYST1 89.500 89.500 132.500 90.00 90.00 90.00 I 41 2 2 16 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 0.011173 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011173 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007547 0.00000