HEADER HYDROLASE(C-TERMINAL PEPTIDASE) 02-APR-93 2CTC 2CTC 2 COMPND CARBOXYPEPTIDASE A (E.C.3.4.17.1) COMPLEX WITH L-PHENYL 2CTC 3 COMPND 2 LACTATE (L-O-PHE) 2CTC 4 SOURCE BOVINE (BOS TAURUS) PANCREAS 2CTC 5 AUTHOR A.TEPLYAKOV,K.S.WILSON,P.ORIOLI,S.MANGANI 2CTC 6 REVDAT 1 31-JAN-94 2CTC 0 2CTC 7 JRNL AUTH A.TEPLYAKOV,K.S.WILSON,P.ORIOLI,S.MANGANI 2CTC 8 JRNL TITL THE HIGH RESOLUTION CRYSTAL STRUCTURE OF THE 2CTC 9 JRNL TITL 2 COMPLEX BETWEEN CARBOXYPEPTIDASE A AND L-PHENYL 2CTC 10 JRNL TITL 3 LACTATE 2CTC 11 JRNL REF TO BE PUBLISHED 2CTC 12 JRNL REFN 353 2CTC 13 REMARK 1 2CTC 14 REMARK 2 2CTC 15 REMARK 2 RESOLUTION. 1.4 ANGSTROMS. 2CTC 16 REMARK 3 2CTC 17 REMARK 3 REFINEMENT. 2CTC 18 REMARK 3 PROGRAM PROLSQ 2CTC 19 REMARK 3 AUTHORS KONNERT,HENDRICKSON 2CTC 20 REMARK 3 R VALUE 0.161 2CTC 21 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 2CTC 22 REMARK 3 RMSD BOND DISTANCES 1-3 0.037 ANGSTROMS 2CTC 23 REMARK 3 RMSD BOND DISTANCES 1-4 0.054 ANGSTROMS 2CTC 24 REMARK 3 RMSD PLANAR GROUPS 0.013 ANGSTROMS 2CTC 25 REMARK 3 RMSD CHIRAL VOLUMES 0.137 ANGSTROMS**3 2CTC 26 REMARK 3 RMSD PEPTIDE TORSION ANGLES 2.6 DEGREES 2CTC 27 REMARK 3 RMSD B-FACTORS: 2CTC 28 REMARK 3 MAIN CHAIN ATOMS 2.6 ANGSTROMS**2 2CTC 29 REMARK 3 SIDE CHAIN ATOMS 5.8 ANGSTROMS**2 2CTC 30 REMARK 3 2CTC 31 REMARK 3 NUMBER OF REFLECTIONS 45829 2CTC 32 REMARK 3 2CTC 33 REMARK 3 NUMBER OF PROTEIN ATOMS 2442 2CTC 34 REMARK 3 NUMBER OF INHIBITOR ATOMS 12 2CTC 35 REMARK 3 NUMBER OF SOLVENT ATOMS 181 2CTC 36 SEQRES 1 307 ALA ARG SER THR ASN THR PHE ASN TYR ALA THR TYR HIS 2CTC 37 SEQRES 2 307 THR LEU ASP GLU ILE TYR ASP PHE MET ASP LEU LEU VAL 2CTC 38 SEQRES 3 307 ALA GLU HIS PRO GLN LEU VAL SER LYS LEU GLN ILE GLY 2CTC 39 SEQRES 4 307 ARG SER TYR GLU GLY ARG PRO ILE TYR VAL LEU LYS PHE 2CTC 40 SEQRES 5 307 SER THR GLY GLY SER ASN ARG PRO ALA ILE TRP ILE ASP 2CTC 41 SEQRES 6 307 LEU GLY ILE HIS SER ARG GLU TRP ILE THR GLN ALA THR 2CTC 42 SEQRES 7 307 GLY VAL TRP PHE ALA LYS LYS PHE THR GLU ASP TYR GLY 2CTC 43 SEQRES 8 307 GLN ASP PRO SER PHE THR ALA ILE LEU ASP SER MET ASP 2CTC 44 SEQRES 9 307 ILE PHE LEU GLU ILE VAL THR ASN PRO ASP GLY PHE ALA 2CTC 45 SEQRES 10 307 PHE THR HIS SER GLN ASN ARG LEU TRP ARG LYS THR ARG 2CTC 46 SEQRES 11 307 SER VAL THR SER SER SER LEU CYS VAL GLY VAL ASP ALA 2CTC 47 SEQRES 12 307 ASN ARG ASN TRP ASP ALA GLY PHE GLY LYS ALA GLY ALA 2CTC 48 SEQRES 13 307 SER SER SER PRO CYS SER GLU THR TYR HIS GLY LYS TYR 2CTC 49 SEQRES 14 307 ALA ASN SER GLU VAL GLU VAL LYS SER ILE VAL ASP PHE 2CTC 50 SEQRES 15 307 VAL LYS ASP HIS GLY ASN PHE LYS ALA PHE LEU SER ILE 2CTC 51 SEQRES 16 307 HIS SER TYR SER GLN LEU LEU LEU TYR PRO TYR GLY TYR 2CTC 52 SEQRES 17 307 THR THR GLN SER ILE PRO ASP LYS THR GLU LEU ASN GLN 2CTC 53 SEQRES 18 307 VAL ALA LYS SER ALA VAL GLU ALA LEU LYS SER LEU TYR 2CTC 54 SEQRES 19 307 GLY THR SER TYR LYS TYR GLY SER ILE ILE THR THR ILE 2CTC 55 SEQRES 20 307 TYR GLN ALA SER GLY GLY SER ILE ASP TRP SER TYR ASN 2CTC 56 SEQRES 21 307 GLN GLY ILE LYS TYR SER PHE THR PHE GLU LEU ARG ASP 2CTC 57 SEQRES 22 307 THR GLY ARG TYR GLY PHE LEU LEU PRO ALA SER GLN ILE 2CTC 58 SEQRES 23 307 ILE PRO THR ALA GLN GLU THR TRP LEU GLY VAL LEU THR 2CTC 59 SEQRES 24 307 ILE MET GLU HIS THR LEU ASN ASN 2CTC 60 FTNOTE 1 2CTC 61 FTNOTE 1 PEPTIDE BONDS BETWEEN RESIDUES SER 197 - TYR 198, 2CTC 62 FTNOTE 1 PRO 205 - TYR 206, AND ARG 272 - ASP 273 ARE IN CIS 2CTC 63 FTNOTE 1 CONFORMATION. 2CTC 64 HET ZN 308 1 ZINC 2CTC 65 HET LOF 309 12 L-PHENYL LACTATE 2CTC 66 FORMUL 2 ZN ZN1 ++ 2CTC 67 FORMUL 3 LOF C9 H9 O3 2CTC 68 FORMUL 4 HOH *181(H2 O1) 2CTC 69 HELIX 1 H1 LEU 15 GLU 28 1 2CTC 70 HELIX 2 H2 TRP 73 ASP 89 1 2CTC 71 HELIX 3 H3 PRO 94 SER 102 1 2CTC 72 HELIX 4 H4 PRO 113 SER 121 1 2CTC 73 HELIX 5 H5 VAL 174 HIS 186 1 2CTC 74 HELIX 6 H6 LYS 216 LYS 231 1 2CTC 75 HELIX 7 H7 ILE 243 THR 246 1 2CTC 76 HELIX 8 H8 SER 254 ASN 260 1 2CTC 77 HELIX 9 H9 ILE 286 ASN 306 1 2CTC 78 SHEET 1 S1 8 LEU 32 LEU 36 0 2CTC 79 SHEET 2 S1 8 VAL 49 SER 53 -1 N LYS 51 O SER 34 2CTC 80 SHEET 3 S1 8 ASP 104 GLU 108 -1 N LEU 107 O LEU 50 2CTC 81 SHEET 4 S1 8 PRO 60 LEU 66 1 N ILE 64 O PHE 106 2CTC 82 SHEET 5 S1 8 LYS 190 HIS 196 1 N LEU 193 O TRP 63 2CTC 83 SHEET 6 S1 8 TYR 265 LEU 271 1 N PHE 269 O SER 194 2CTC 84 SHEET 7 S1 8 GLN 200 TYR 204 -1 N LEU 203 O THR 268 2CTC 85 SHEET 8 S1 8 LYS 239 ILE 243 1 N GLY 241 O LEU 202 2CTC 86 TURN 1 T1 SER 3 THR 6 TYPE III 2CTC 87 TURN 2 T2 ASN 8 THR 11 TYPE I 2CTC 88 TURN 3 T3 HIS 29 LEU 32 TYPE III 2CTC 89 TURN 4 T4 SER 41 GLY 44 TYPE I 2CTC 90 TURN 5 T5 HIS 69 GLU 72 TYPE III 2CTC 91 TURN 6 T6 GLU 72 THR 75 TYPE III 2CTC 92 TURN 7 T7 ASP 89 GLN 92 TYPE II 2CTC 93 TURN 8 T8 ILE 99 SER 102 TYPE III 2CTC 94 TURN 9 T9 ASN 123 TRP 126 TYPE I 2CTC 95 TURN 10 T10 THR 133 SER 136 TYPE I 2CTC 96 TURN 11 T11 ASP 142 ARG 145 TYPE I 2CTC 97 TURN 12 T12 ALA 143 ASN 146 TYPE I 2CTC 98 TURN 13 T13 GLY 150 LYS 153 TYPE II 2CTC 99 TURN 14 T14 SER 159 SER 162 TYPE III 2CTC 100 TURN 15 T15 SER 162 TYR 165 TYPE I 2CTC 101 TURN 16 T16 TYR 169 SER 172 TYPE II 2CTC 102 TURN 17 T17 GLU 173 VAL 176 TYPE III 2CTC 103 TURN 18 T18 ILE 213 LYS 216 TYPE I 2CTC 104 TURN 19 T19 LEU 230 LEU 233 TYPE III 2CTC 105 TURN 20 T20 TYR 259 GLY 262 TYPE I 2CTC 106 TURN 21 T21 TYR 277 LEU 280 TYPE II' 2CTC 107 TURN 22 T22 PRO 282 GLN 285 TYPE III 2CTC 108 TURN 23 T23 ALA 283 ILE 286 TYPE I 2CTC 109 SSBOND 1 CYS 138 CYS 161 2CTC 110 CRYST1 51.600 60.270 47.250 90.00 97.27 90.00 P 21 2 2CTC 111 ORIGX1 1.000000 0.000000 0.000000 0.00000 2CTC 112 ORIGX2 0.000000 1.000000 0.000000 0.00000 2CTC 113 ORIGX3 0.000000 0.000000 1.000000 0.00000 2CTC 114 SCALE1 0.019380 0.000000 0.002472 0.00000 2CTC 115 SCALE2 0.000000 0.016592 0.000000 0.00000 2CTC 116 SCALE3 0.000000 0.000000 0.021336 0.00000 2CTC 117