HEADER COMPLEX (PROTEINASE/INHIBITOR) 27-SEP-82 1TGS 1TGS 3 COMPND TRYPSINOGEN COMPLEX WITH PORCINE PANCREATIC SECRETORY 1TGSA 1 COMPND 2 TRYPSIN INHIBITOR 1TGSA 2 SOURCE BOVINE (BOS TAURUS) PANCREAS AND PORCINE (SUS SCROFA) 1TGS 6 SOURCE 2 PANCREAS 1TGS 7 AUTHOR M.BOLOGNESI,G.GATTI,E.MENEGATTI,M.GUARNERI,M.MARQUART, 1TGS 8 AUTHOR 2 E.PAPAMOKOS,R.HUBER 1TGS 9 REVDAT 5 14-MAR-85 1TGSD 3 SEQRES ATOM 1TGSD 1 REVDAT 4 23-FEB-84 1TGSC 1 REMARK 1TGSC 1 REVDAT 3 30-SEP-83 1TGSB 1 REVDAT 1TGSB 1 REVDAT 2 07-MAR-83 1TGSA 1 COMPND 1TGSB 2 REVDAT 1 18-JAN-83 1TGS 0 1TGSB 3 JRNL AUTH M.BOLOGNESI,G.GATTI,E.MENEGATTI,M.GUARNERI, 1TGS 10 JRNL AUTH 2 M.MARQUART,E.PAPAMOKOS,R.HUBER 1TGS 11 JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN 1TGS 12 JRNL TITL 2 PANCREATIC SECRETORY INHIBITOR (KAZAL TYPE) AND 1TGS 13 JRNL TITL 3 TRYPSINOGEN AT 1.8 ANGSTROMS RESOLUTION. STRUCTURE 1TGS 14 JRNL TITL 4 SOLUTION, CRYSTALLOGRAPHIC REFINEMENT AND 1TGS 15 JRNL TITL 5 PRELIMINARY STRUCTURAL INTERPRETATION 1TGS 16 JRNL REF J.MOL.BIOL. V. 162 839 1982 1TGS 17 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1TGS 18 REMARK 1 1TGS 19 REMARK 1 REFERENCE 1 1TGSC 2 REMARK 1 AUTH M.MARQUART,J.WALTER,J.DEISENHOFER,W.BODE,R.HUBER 1TGSC 3 REMARK 1 TITL THE GEOMETRY OF THE REACTIVE SITE AND OF THE 1TGSC 4 REMARK 1 TITL 2 PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS 1TGSC 5 REMARK 1 TITL 3 COMPLEXES WITH INHIBITORS 1TGSC 6 REMARK 1 REF ACTA CRYSTALLOGR.,SECT.B V. 39 480 1983 1TGSC 7 REMARK 1 REFN ASTM ASBSDK DK ISSN 0108-7681 622 1TGSC 8 REMARK 1 REFERENCE 2 1TGSC 9 REMARK 1 EDIT M.O.DAYHOFF 1TGS 21 REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 105 1972 1TGS 22 REMARK 1 REF 2 AND STRUCTURE (DATA SECTION) 1TGS 23 REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, 1TGS 24 REMARK 1 PUBL 2 SILVER SPRING,MD. 1TGS 25 REMARK 1 REFN ISBN 0-912466-02-2 435 1TGS 26 REMARK 1 REFERENCE 3 1TGSC 10 REMARK 1 EDIT M.O.DAYHOFF 1TGS 28 REMARK 1 REF ATLAS OF PROTEIN SEQUENCE V. 5 88 1973 1TGS 29 REMARK 1 REF 2 AND STRUCTURE,SUPPLEMENT 1 1TGS 30 REMARK 1 PUBL NATIONAL BIOMEDICAL RESEARCH FOUNDATION, 1TGS 31 REMARK 1 PUBL 2 SILVER SPRING,MD. 1TGS 32 REMARK 1 REFN ISBN 0-912466-04-9 435 1TGS 33 REMARK 2 1TGS 34 REMARK 2 RESOLUTION. 1.8 ANGSTROMS. 1TGS 35 REMARK 3 1TGS 36 REMARK 3 REFINEMENT. J. DEISENHOFER*S VERSION OF THE JACK AND 1TGS 37 REMARK 3 LEVITT REFINEMENT PROCEDURE COMBINING CRYSTALLOGRAPHIC AND 1TGS 38 REMARK 3 ENERGY REFINEMENT. (A.JACK,M.LEVITT, ACTA CRYSTALLOGR., 1TGS 39 REMARK 3 A34, 931-935, 1978). THE R-VALUE FOR REFLECTIONS WITHIN 1TGS 40 REMARK 3 THE SHELL 1.8 TO 7.0 ANGSTROMS AND WITH 1TGS 41 REMARK 3 2*(ABS(FO)-ABS(FC))/(ABS(FO)+ABS(FC)) LESS THAN 1.2 IS 1TGS 42 REMARK 3 0.186. 1TGS 43 REMARK 4 1TGS 44 REMARK 4 AN OCCUPANCY OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON 1TGS 45 REMARK 4 DENSITY WAS FOUND IN THE FINAL FOURIER MAP. 1TGS 46 REMARK 5 1TGS 47 REMARK 5 THE 229 AMINO ACIDS OF TRYPSINOGEN ARE IDENTIFIED BY THE 1TGS 48 REMARK 5 RESIDUE NUMBERS OF THE HOMOLOGOUS CHYMOTRYPSINOGEN. 1TGS 49 REMARK 5 IN THIS COMPLEX THE ZYMOGEN IS GIVEN THE CHAIN INDICATOR Z 1TGS 50 REMARK 5 AND THE INHIBITOR IS GIVEN THE CHAIN INDICATOR I. 1TGS 51 REMARK 5 A NULL (BLANK) CHAIN INDICATOR IS ASSIGNED TO THE SULFATE, 1TGS 52 REMARK 5 TO THE CALCIUM, AND TO THE WATER MOLECULES. THE 1TGS 53 REMARK 5 NOMENCLATURE OF THE WATER MOLECULES IS THAT OF THE 1TGS 54 REMARK 5 DEPOSITORS. 1TGS 55 REMARK 6 1TGS 56 REMARK 6 THIS DATA ENTRY CONTAINS NO COORDINATES FOR VAL Z 10 1TGS 57 REMARK 6 THROUGH ASP Z 13. 1TGS 58 REMARK 7 1TGS 59 REMARK 7 THIS COORDINATE SET IS DESIGNATED TGKZ BY THE DEPOSITORS. 1TGS 60 REMARK 8 1TGSA 3 REMARK 8 CORRECTION. REMOVE E.C. CODE FROM COMPND RECORD. 1TGSA 4 REMARK 8 07-MAR-83. 1TGSA 5 REMARK 9 1TGSB 4 REMARK 9 CORRECTION. INSERT REVDAT RECORDS. 30-SEP-83. 1TGSB 5 REMARK 10 1TGSC 11 REMARK 10 CORRECTION. INSERT NEW PUBLICATION AS REFERENCE 1 AND 1TGSC 12 REMARK 10 RENUMBER THE OTHERS. 23-FEB-84. 1TGSC 13 REMARK 11 1TGSD 2 REMARK 11 CORRECTION. CHANGE RESIDUE 165 FROM ASN TO ASP AND CHANGE 1TGSD 3 REMARK 11 RESIDUE 186 FROM GLN TO GLU, UPON DEPOSITORS INSTRUCTIONS. 1TGSD 4 REMARK 11 REVISE ATOM AND SEQRES RECORDS ACCORDINGLY. 14-MAR-85. 1TGSD 5 SEQRES 1 Z 229 VAL ASP ASP ASP ASP LYS ILE VAL GLY GLY TYR THR CYS 1TGS 61 SEQRES 2 Z 229 GLY ALA ASN THR VAL PRO TYR GLN VAL SER LEU ASN SER 1TGS 62 SEQRES 3 Z 229 GLY TYR HIS PHE CYS GLY GLY SER LEU ILE ASN SER GLN 1TGS 63 SEQRES 4 Z 229 TRP VAL VAL SER ALA ALA HIS CYS TYR LYS SER GLY ILE 1TGS 64 SEQRES 5 Z 229 GLN VAL ARG LEU GLY GLU ASP ASN ILE ASN VAL VAL GLU 1TGS 65 SEQRES 6 Z 229 GLY ASN GLU GLN PHE ILE SER ALA SER LYS SER ILE VAL 1TGS 66 SEQRES 7 Z 229 HIS PRO SER TYR ASN SER ASN THR LEU ASN ASN ASP ILE 1TGS 67 SEQRES 8 Z 229 MET LEU ILE LYS LEU LYS SER ALA ALA SER LEU ASN SER 1TGS 68 SEQRES 9 Z 229 ARG VAL ALA SER ILE SER LEU PRO THR SER CYS ALA SER 1TGS 69 SEQRES 10 Z 229 ALA GLY THR GLN CYS LEU ILE SER GLY TRP GLY ASN THR 1TGS 70 SEQRES 11 Z 229 LYS SER SER GLY THR SER TYR PRO ASP VAL LEU LYS CYS 1TGS 71 SEQRES 12 Z 229 LEU LYS ALA PRO ILE LEU SER ASP SER SER CYS LYS SER 1TGSD 6 SEQRES 13 Z 229 ALA TYR PRO GLY GLN ILE THR SER ASN MET PHE CYS ALA 1TGS 73 SEQRES 14 Z 229 GLY TYR LEU GLU GLY GLY LYS ASP SER CYS GLN GLY ASP 1TGSD 7 SEQRES 15 Z 229 SER GLY GLY PRO VAL VAL CYS SER GLY LYS LEU GLN GLY 1TGS 75 SEQRES 16 Z 229 ILE VAL SER TRP GLY SER GLY CYS ALA GLN LYS ASN LYS 1TGS 76 SEQRES 17 Z 229 PRO GLY VAL TYR THR LYS VAL CYS ASN TYR VAL SER TRP 1TGS 77 SEQRES 18 Z 229 ILE LYS GLN THR ILE ALA SER ASN 1TGS 78 SEQRES 1 I 56 THR SER PRO GLN ARG GLU ALA THR CYS THR SER GLU VAL 1TGS 79 SEQRES 2 I 56 SER GLY CYS PRO LYS ILE TYR ASN PRO VAL CYS GLY THR 1TGS 80 SEQRES 3 I 56 ASP GLY ILE THR TYR SER ASN GLU CYS VAL LEU CYS SER 1TGS 81 SEQRES 4 I 56 GLU ASN LYS LYS ARG GLN THR PRO VAL LEU ILE GLN LYS 1TGS 82 SEQRES 5 I 56 SER GLY PRO CYS 1TGS 83 FTNOTE 1 1TGS 84 FTNOTE 1 SEE REMARK 4. 1TGS 85 HET SO4 1 5 SULFATE 1TGS 86 HET CA 800 1 CALCIUM ION 1TGS 87 FORMUL 4 SO4 O4 S1 1TGS 88 FORMUL 5 CA CA1 ++ 1TGS 89 FORMUL 6 HOH *152(H2 O1) 1TGS 90 HELIX 1 H1 SER Z 164 ILE Z 176 1 SNGL ALPHA TURN,REST IRREG. 1TGS 91 HELIX 2 H2 LYS Z 230 VAL Z 235 5 CONTIGUOUS WITH H3 1TGS 92 HELIX 3 H3 SER Z 236 ASN Z 245 1 CONTIGUOUS WITH H2 1TGS 93 HELIX 4 IH1 GLU I 34 LYS I 42 1 1TGS 94 SHEET 1 IS1 3 ASP I 27 TYR I 31 0 1TGS 95 SHEET 2 IS1 3 VAL I 23 THR I 26 -1 1TGS 96 SHEET 3 IS1 3 LEU I 49 SER I 53 -1 1TGS 97 SSBOND 1 CYS Z 22 CYS Z 157 1TGS 98 SSBOND 2 CYS Z 42 CYS Z 58 1TGS 99 SSBOND 3 CYS Z 128 CYS Z 232 1TGS 100 SSBOND 4 CYS Z 136 CYS Z 201 1TGS 101 SSBOND 5 CYS Z 168 CYS Z 182 1TGS 102 SSBOND 6 CYS Z 191 CYS Z 220 1TGS 103 SSBOND 7 CYS I 8 CYS I 38 1TGS 104 SSBOND 8 CYS I 16 CYS I 35 1TGS 105 SSBOND 9 CYS I 24 CYS I 56 1TGS 106 CRYST1 67.100 75.500 66.900 90.00 90.00 90.00 P 21 21 21 4 1TGS 107 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TGS 108 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TGS 109 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TGS 110 SCALE1 .014903 0.000000 0.000000 0.00000 1TGS 111 SCALE2 0.000000 .013245 0.000000 0.00000 1TGS 112 SCALE3 0.000000 0.000000 .014948 0.00000 1TGS 113