HEADER PROTEINASE INHIBITOR (TRYPSIN) 14-FEB-91 1TIE 1TIE 2 COMPND ERYTHRINA TRYPSIN INHIBITOR (KUNITZ) DE-3 1TIE 3 SOURCE (ERYTHRINA $CAFFRA) 1TIE 4 AUTHOR S.ONESTI,P.BRICK,D.M.BLOW 1TIEA 1 REVDAT 3 15-MAY-95 1TIEB 1 REMARK 1TIEB 1 REVDAT 2 31-OCT-93 1TIEA 1 AUTHOR 1TIEA 2 REVDAT 1 15-JUL-92 1TIE 0 1TIE 6 JRNL AUTH S.ONESTI,P.BRICK,D.M.BLOW 1TIE 7 JRNL TITL CRYSTAL STRUCTURE OF A KUNITZ-TYPE TRYPSIN 1TIE 8 JRNL TITL 2 INHIBITOR FROM ERYTHRINA $CAFFRA SEEDS 1TIE 9 JRNL REF J.MOL.BIOL. V. 217 153 1991 1TIE 10 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1TIE 11 REMARK 1 1TIE 12 REMARK 1 REFERENCE 1 1TIE 13 REMARK 1 AUTH S.ONESTI,L.F.LLOYD,P.BRICK,D.M.BLOW 1TIE 14 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY DIFFRACTION STUDIES 1TIE 15 REMARK 1 TITL 2 OF ERYTHRINA TRYPSIN INHIBITOR 1TIE 16 REMARK 1 REF J.MOL.BIOL. V. 210 241 1989 1TIEB 2 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1TIE 18 REMARK 2 1TIE 19 REMARK 2 RESOLUTION. 2.5 ANGSTROMS. 1TIE 20 REMARK 3 1TIE 21 REMARK 3 REFINEMENT. BY A COMBINATION OF SIMULATED ANNEALING AND 1TIE 22 REMARK 3 CONVENTIONAL RESTRAINED CRYSTALLOGRAPHIC REFINEMENT BY 1TIE 23 REMARK 3 THE METHOD OF A. BRUNGER, J. KURIYAN, AND M. KARPLUS 1TIE 24 REMARK 3 (PROGRAM *XPLOR*). THE R VALUE IS 0.208 FOR 7770 1TIE 25 REMARK 3 REFLECTIONS IN THE RESOLUTION RANGE 10.0 TO 2.5 1TIE 26 REMARK 3 ANGSTROMS. THE RMS DEVIATION FROM IDEALITY OF THE BOND 1TIE 27 REMARK 3 LENGTHS IS 0.016 ANGSTROMS. 1TIE 28 REMARK 4 1TIE 29 REMARK 4 THE ELECTRON DENSITY IS VERY POOR FOR RESIDUES 94 - 97 1TIE 30 REMARK 4 AND C-TERMINAL RESIDUES 171 - 172 AND NO ATOMIC MODEL 1TIE 31 REMARK 4 COULD BE BUILT FOR THESE RESIDUES. FOR LOOPS 104 - 110 1TIE 32 REMARK 4 AND 133 - 138 ONLY THE MAIN CHAIN WAS TRACED AND THE 1TIE 33 REMARK 4 RELIABILITY OF THE DIHEDRAL ANGLES IS LOW. THIS 1TIE 34 REMARK 4 UNCERTAINTY IS ALSO REFLECTED IN THE UNUSUALLY HIGH 1TIE 35 REMARK 4 TEMPERATURE FACTORS FOR BOTH LOOPS; THE POSITION OF 1TIE 36 REMARK 4 THESE LOOPS WAS CONFIRMED BY CALCULATING A MAP USING 1TIE 37 REMARK 4 PHASES WITH NO BIAS FROM THE MODEL LOOPS. 1TIE 38 REMARK 5 1TIE 39 REMARK 5 ETI CONSISTS OF 12 ANTIPARALLEL BETA-STRANDS JOINED BY 1TIE 40 REMARK 5 LONG LOOPS. SIX OF THE STRANDS FORM A SHORT BARREL WHICH 1TIE 41 REMARK 5 IS CLOSED AT ONE END BY A "LID" CONSISTING OF THE OTHER 1TIE 42 REMARK 5 SIX STRANDS COUPLED IN THREE PAIRS. THE MOLECULE SHOWS 1TIE 43 REMARK 5 APPROXIMATE THREE-FOLD SYMMETRY ABOUT THE THE AXIS OF THE 1TIE 44 REMARK 5 BARREL, WITH THE REPEATING UNIT CONSISTING OF FOUR 1TIE 45 REMARK 5 SEQUENTIAL BETA-STRANDS AND THE CONNECTING LOOPS. THE SHEET 1TIE 46 REMARK 5 PRESENTED AS *B1* ON SHEET RECORDS BELOW IS ACTUALLY THE 1TIE 47 REMARK 5 SIX-STRANDED BETA-BARREL. THIS IS REPRESENTED BY A 1TIE 48 REMARK 5 SEVEN-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS 1TIE 49 REMARK 5 ARE IDENTICAL. 1TIE 50 REMARK 6 1TIE 51 REMARK 6 A NUMBER OF SIDE CHAIN ATOMS HAVE BEEN OMITTED FROM THE 1TIE 52 REMARK 6 MODEL BECAUSE THEY HAVE NO ELECTRON DENSITY IN THE FINAL 1TIE 53 REMARK 6 MAP: GLU 36, THR 38, TYR 79, LYS 82, GLU 93, GLN 123, 1TIE 54 REMARK 6 LYS 149, GLU 158, ASP 159, TYR 160, GLU 170. 1TIE 55 REMARK 7 1TIEA 3 REMARK 7 CORRECTION. CHANGE PERIOD TO COMMA IN AUTHOR RECORD. 1TIEA 4 REMARK 7 31-OCT-93. 1TIEA 5 REMARK 8 1TIEB 3 REMARK 8 CORRECTION. CORRECT SPACING IN REFERENCE. 15-MAY-95. 1TIEB 4 SEQRES 1 172 VAL LEU LEU ASP GLY ASN GLY GLU VAL VAL GLN ASN GLY 1TIE 56 SEQRES 2 172 GLY THR TYR TYR LEU LEU PRO GLN VAL TRP ALA GLN GLY 1TIE 57 SEQRES 3 172 GLY GLY VAL GLN LEU ALA LYS THR GLY GLU GLU THR CYS 1TIE 58 SEQRES 4 172 PRO LEU THR VAL VAL GLN SER PRO ASN GLU LEU SER ASP 1TIE 59 SEQRES 5 172 GLY LYS PRO ILE ARG ILE GLU SER ARG LEU ARG SER ALA 1TIE 60 SEQRES 6 172 PHE ILE PRO ASP ASP ASP LYS VAL ARG ILE GLY PHE ALA 1TIE 61 SEQRES 7 172 TYR ALA PRO LYS CYS ALA PRO SER PRO TRP TRP THR VAL 1TIE 62 SEQRES 8 172 VAL GLU ASP GLU GLN GLU GLY LEU SER VAL LYS LEU SER 1TIE 63 SEQRES 9 172 GLU ASP GLU SER THR GLN PHE ASP TYR PRO PHE LYS PHE 1TIE 64 SEQRES 10 172 GLU GLN VAL SER ASP GLN LEU HIS SER TYR LYS LEU LEU 1TIE 65 SEQRES 11 172 TYR CYS GLU GLY LYS HIS GLU LYS CYS ALA SER ILE GLY 1TIE 66 SEQRES 12 172 ILE ASN ARG ASP GLN LYS GLY TYR ARG ARG LEU VAL VAL 1TIE 67 SEQRES 13 172 THR GLU ASP TYR PRO LEU THR VAL VAL LEU LYS LYS ASP 1TIE 68 SEQRES 14 172 GLU SER SER 1TIE 69 FORMUL 2 HOH *61(H2 O1) 1TIE 70 SHEET 1 B1 7 THR 15 PRO 20 0 1TIE 71 SHEET 2 B1 7 ILE 56 SER 60 -1 1TIE 72 SHEET 3 B1 7 VAL 73 PHE 77 -1 1TIE 73 SHEET 4 B1 7 PHE 115 SER 121 -1 1TIE 74 SHEET 5 B1 7 SER 126 CYS 132 -1 1TIE 75 SHEET 6 B1 7 THR 163 LYS 168 -1 1TIE 76 SHEET 7 B1 7 THR 15 PRO 20 -1 1TIE 77 SHEET 1 B2 2 VAL 29 ALA 32 0 1TIE 78 SHEET 2 B2 2 THR 42 ASN 45 -1 1TIE 79 SHEET 1 B3 2 TRP 89 VAL 92 0 1TIE 80 SHEET 2 B3 2 SER 100 LEU 103 -1 1TIE 81 SHEET 1 B4 2 CYS 139 ARG 146 0 1TIE 82 SHEET 2 B4 2 ARG 152 VAL 156 -1 1TIE 83 TURN 1 T01 ASP 4 GLY 7 TYPE I 1TIE 84 TURN 2 T02 GLN 11 GLY 14 TYPE II 1TIE 85 TURN 3 T03 VAL 22 ASN 25 TYPE III 1TIE 86 TURN 4 T04 TRP 23 GLY 26 TYPE III 1TIE 87 TURN 5 T05 ASN 48 SER 51 TYPE I 1TIE 88 TURN 6 T06 PRO 68 ASP 71 TYPE II 1TIE 89 TURN 7 T07 ALA 109 ASP 112 TYPE I 1TIE 90 TURN 8 T08 ASP 147 GLY 150 TYPE I 1TIE 91 SSBOND 1 CYS 39 CYS 83 1TIE 92 SSBOND 2 CYS 132 CYS 139 1TIE 93 CRYST1 73.400 73.400 143.000 90.00 90.00 120.00 P 65 2 2 12 1TIE 94 ORIGX1 1.000000 0.000000 0.000000 0.00000 1TIE 95 ORIGX2 0.000000 1.000000 0.000000 0.00000 1TIE 96 ORIGX3 0.000000 0.000000 1.000000 0.00000 1TIE 97 SCALE1 0.013624 0.007866 0.000000 0.00000 1TIE 98 SCALE2 0.000000 0.015732 0.000000 0.00000 1TIE 99 SCALE3 0.000000 0.000000 0.006993 0.00000 1TIE 100