HEADER HYDROLASE(SERINE PROTEASE) 18-JUL-91 1PK4 COMPND PLASMINOGEN KRINGLE 4 SOURCE HUMAN (HOMO SAPIENS) AUTHOR A.TULINSKY,A.M.MULICHAK REVDAT 1 31-OCT-93 1PK4 0 JRNL AUTH A.M.MULICHAK,A.TULINSKY,K.G.RAVICHANDRAN JRNL TITL CRYSTAL AND MOLECULAR STRUCTURE OF HUMAN JRNL TITL 2 PLASMINOGEN KRINGLE 4 REFINED AT 1.9-ANGSTROMS JRNL TITL 3 RESOLUTION JRNL REF BIOCHEMISTRY V. 30 10576 1991 JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.P.SESHADRI,A.TULINSKY,E.SKRZYPCZAK-JANKUN, REMARK 1 AUTH 2 C.H.PARK REMARK 1 TITL STRUCTURE OF BOVINE PROTHROMBIN FRAGMENT 1 REMARK 1 TITL 2 REFINED AT 2.25 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 220 481 1991 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.M.MULICHAK,A.TULINSKY REMARK 1 TITL STRUCTURE OF THE LYSINE-FIBRIN BINDING SUBSITE OF REMARK 1 TITL 2 HUMAN PLASMINOGEN KRINGLE 4 REMARK 1 REF BLOOD COAGULATION V. 1 673 1990 REMARK 1 REF 2 FIBRINOLYSIS REMARK 1 REFN ASTM BLFIE7 UK ISSN 0957-5235 796 REMARK 1 REFERENCE 3 REMARK 1 AUTH A.TULINSKY,C.H.PARK,B.MAO,M.LLINAS REMARK 1 TITL LYSINE(SLASH)FIBRIN BINDING SITES OF KRINGLES REMARK 1 TITL 2 MODELED AFTER THE STRUCTURE OF KRINGLE 1 OF REMARK 1 TITL 3 PROTHROMBIN REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 3 85 1988 REMARK 1 REF 2 GENET. REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 REMARK 1 REFERENCE 4 REMARK 1 AUTH A.TULINSKY,C.H.PARK,E.SKRZYPCZAK-JANKUN REMARK 1 TITL STRUCTURE OF PROTHROMBIN FRAGMENT 1 REFINED AT 2.8 REMARK 1 TITL 2 ANGSTROMS RESOLUTION REMARK 1 REF J.MOL.BIOL. V. 202 885 1988 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 2 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROFFT REMARK 3 AUTHORS KONNERT,HENDRICKSON,FINZEL REMARK 3 R VALUE 0.142 REMARK 3 RMSD BOND DISTANCES 0.018 ANGSTROMS REMARK 3 RMSD BOND ANGLE DISTANCES 0.044 ANGSTROMS REMARK 4 REMARK 4 SEQUENCE NUMBERING IS BASED ON PLASMINOGEN KRINGLE 5. REMARK 5 REMARK 5 FINAL STRUCTURE CONSISTS OF ASP 0 THROUGH CYS 80, ONE REMARK 5 SULFATE ANION (RESIDUE 100), AND 96 WATER MOLECULES. REMARK 6 REMARK 6 NO ELECTRON DENSITY WAS OBSERVED FOR THE SIDE CHAINS OF REMARK 6 RESIDUES ASP 0, THR 12, GLU 39, LYS 78, LYS 79. THESE WERE REMARK 6 REFINED AS ALA OR GLY. SEQRES 1 79 ASP CYS TYR HIS GLY ASP GLY GLN SER TYR ARG GLY THR SEQRES 2 79 SER SER THR THR THR THR GLY LYS LYS CYS GLN SER TRP SEQRES 3 79 SER SER MET THR PRO HIS ARG HIS GLN LYS THR PRO GLU SEQRES 4 79 ASN TYR PRO ASN ALA GLY LEU THR MET ASN TYR CYS ARG SEQRES 5 79 ASN PRO ASP ALA ASP LYS GLY PRO TRP CYS PHE THR THR SEQRES 6 79 ASP PRO SER VAL ARG TRP GLU TYR CYS ASN LEU LYS LYS SEQRES 7 79 CYS FTNOTE 1 FTNOTE 1 CIS PROLINE - PRO 30 HET SO4 100 5 SULFATE FORMUL 2 SO4 O4 S1 FORMUL 3 HOH *96(H2 O1) SHEET 1 B1 2 SER 14 THR 16 0 SHEET 2 B1 2 LYS 20 CYS 22 -1 SHEET 1 B2 2 LYS 21 GLN 23 0 SHEET 2 B2 2 PHE 64 THR 66 -1 SHEET 1 B3 2 PRO 61 THR 65 0 SHEET 2 B3 2 ARG 71 CYS 75 -1 TURN 1 T1 HIS 3 GLY 6 TYPE II' TURN 2 T2 GLY 6 TYR 9 TYPE I TURN 3 T3 THR 16 GLY 19 TYPE I TURN 4 T4 SER 24 SER 27 TYPE I TURN 5 T5 THR 37 ASN 40 TYPE III TURN 6 T6 TYR 41 ALA 44 TYPE I TURN 7 T7 THR 47 TYR 50 TYPE II' TURN 8 T8 ASN 53 ALA 56 TYPE I TURN 9 T9 ASP 67 VAL 70 TYPE I SSBOND 1 CYS 1 CYS 80 SSBOND 2 CYS 22 CYS 63 SSBOND 3 CYS 51 CYS 75 CRYST1 32.110 49.090 49.390 90.00 90.00 90.00 P 21 21 21 4 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 0.031143 0.000000 0.000000 0.00000 SCALE2 0.000000 0.020371 0.000000 0.00000 SCALE3 0.000000 0.000000 0.020247 0.00000