HEADER HYDROLASE(ALPHA-AMINOACYLPEPTIDE) 02-DEC-92 1MAT 1MAT 2 COMPND METHIONINE AMINOPEPTIDASE (E.C.3.4.11.18) 1MAT 3 SOURCE (ESCHERICHIA COLI) 1MAT 4 AUTHOR S.L.RODERICK,B.W.MATTHEWS 1MAT 5 REVDAT 1 31-JAN-94 1MAT 0 1MAT 6 JRNL AUTH S.L.RODERICK,B.W.MATTHEWS 1MAT 7 JRNL TITL STRUCTURE OF THE COBALT-DEPENDENT METHIONINE 1MAT 8 JRNL TITL 2 AMINOPEPTIDASE FROM ESCHERICHIA COLI: A NEW TYPE 1MAT 9 JRNL TITL 3 OF PROTEOLYTIC ENZYME 1MAT 10 JRNL REF BIOCHEMISTRY V. 32 3907 1993 1MAT 11 JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 1MAT 12 REMARK 1 1MAT 13 REMARK 1 REFERENCE 1 1MAT 14 REMARK 1 AUTH S.L.RODERICK,B.W.MATTHEWS 1MAT 15 REMARK 1 TITL CRYSTALLIZATION OF METHIONINE AMINOPEPTIDASE FROM 1MAT 16 REMARK 1 TITL 2 ESCHERICHIA COLI 1MAT 17 REMARK 1 REF J.BIOL.CHEM. V. 263 16531 1988 1MAT 18 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 1MAT 19 REMARK 1 REFERENCE 2 1MAT 20 REMARK 1 AUTH A.BEN-BASSAT,K.BAUER,S.-Y.CHANG,K.MYAMBO,A.BOOSMAN, 1MAT 21 REMARK 1 AUTH 2 S.CHANG 1MAT 22 REMARK 1 TITL PROCESSING OF THE INITIATION METHIONINE FROM 1MAT 23 REMARK 1 TITL 2 PROTEINS: PROPERTIES OF THE ESCHERICHIA COLI 1MAT 24 REMARK 1 TITL 3 METHIONINE AMINOPEPTIDASE AND ITS GENE STRUCTURE 1MAT 25 REMARK 1 REF J.BACTERIOL. V. 169 751 1987 1MAT 26 REMARK 1 REFN ASTM JOBAAY US ISSN 0021-9193 767 1MAT 27 REMARK 2 1MAT 28 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 1MAT 29 REMARK 3 1MAT 30 REMARK 3 REFINEMENT. 1MAT 31 REMARK 3 PROGRAM TNT 1MAT 32 REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1MAT 33 REMARK 3 R VALUE 0.182 1MAT 34 REMARK 3 RMSD BOND DISTANCES 0.019 ANGSTROMS 1MAT 35 REMARK 3 RMSD BOND ANGLES 2.9 DEGREES 1MAT 36 REMARK 4 1MAT 37 REMARK 4 SOME SIDE CHAINS ARE INCOMPLETE. SEE FTNOTES 2 - 7 BELOW. 1MAT 38 REMARK 5 1MAT 39 REMARK 5 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN 1MAT 40 REMARK 5 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW 1MAT 41 REMARK 5 TWO SHEETS ARE DEFINED. STRANDS 2, 3, AND 4 OF 1A AND 1B 1MAT 42 REMARK 5 ARE IDENTICAL. 1MAT 43 REMARK 6 1MAT 44 REMARK 6 RESIDUE MET 1 IS NOT PRESENT IN THE ELECTRON DENSITY MAP. 1MAT 45 REMARK 7 1MAT 46 REMARK 7 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL 1MAT 47 REMARK 7 YIELD APPROXIMATE COORDINATES FOR PORTIONS OF THE CHAIN 1MAT 48 REMARK 7 WHEN APPLIED TO OTHER PORTIONS OF THE CHAIN AS FOLLOWS: 1MAT 49 REMARK 7 1MAT 50 REMARK 7 APPLYING MTRIX TO YIELDS 1MAT 51 REMARK 7 ----------------- ----------------- 1MAT 52 REMARK 7 THR 119 - MET 139 ILE 11 - TYR 31 1MAT 53 REMARK 7 VAL 140 - ILE 144 VAL 32 - VAL 36 1MAT 54 REMARK 7 ASN 145 - ALA 159 SER 37 - ASN 51 1MAT 55 REMARK 7 GLY 198 - ASN 208 GLY 91 - ILE 101 1MAT 56 REMARK 7 LEU 230 - THR 241 PHE 105 - GLY 116 1MAT 57 SEQRES 1 264 MET ALA ILE SER ILE LYS THR PRO GLU ASP ILE GLU LYS 1MAT 58 SEQRES 2 264 MET ARG VAL ALA GLY ARG LEU ALA ALA GLU VAL LEU GLU 1MAT 59 SEQRES 3 264 MET ILE GLU PRO TYR VAL LYS PRO GLY VAL SER THR GLY 1MAT 60 SEQRES 4 264 GLU LEU ASP ARG ILE CYS ASN ASP TYR ILE VAL ASN GLU 1MAT 61 SEQRES 5 264 GLN HIS ALA VAL SER ALA CYS LEU GLY TYR HIS GLY TYR 1MAT 62 SEQRES 6 264 PRO LYS SER VAL CYS ILE SER ILE ASN GLU VAL VAL CYS 1MAT 63 SEQRES 7 264 HIS GLY ILE PRO ASP ASP ALA LYS LEU LEU LYS ASP GLY 1MAT 64 SEQRES 8 264 ASP ILE VAL ASN ILE ASP VAL THR VAL ILE LYS ASP GLY 1MAT 65 SEQRES 9 264 PHE HIS GLY ASP THR SER LYS MET PHE ILE VAL GLY LYS 1MAT 66 SEQRES 10 264 PRO THR ILE MET GLY GLU ARG LEU CYS ARG ILE THR GLN 1MAT 67 SEQRES 11 264 GLU SER LEU TYR LEU ALA LEU ARG MET VAL LYS PRO GLY 1MAT 68 SEQRES 12 264 ILE ASN LEU ARG GLU ILE GLY ALA ALA ILE GLN LYS PHE 1MAT 69 SEQRES 13 264 VAL GLU ALA GLU GLY PHE SER VAL VAL ARG GLU TYR CYS 1MAT 70 SEQRES 14 264 GLY HIS GLY ILE GLY ARG GLY PHE HIS GLU GLU PRO GLN 1MAT 71 SEQRES 15 264 VAL LEU HIS TYR ASP SER ARG GLU THR ASN VAL VAL LEU 1MAT 72 SEQRES 16 264 LYS PRO GLY MET THR PHE THR ILE GLU PRO MET VAL ASN 1MAT 73 SEQRES 17 264 ALA GLY LYS LYS GLU ILE ARG THR MET LYS ASP GLY TRP 1MAT 74 SEQRES 18 264 THR VAL LYS THR LYS ASP ARG SER LEU SER ALA GLN TYR 1MAT 75 SEQRES 19 264 GLU HIS THR ILE VAL VAL THR ASP ASN GLY CYS GLU ILE 1MAT 76 SEQRES 20 264 LEU THR LEU ARG LYS ASP ASP THR ILE PRO ALA ILE ILE 1MAT 77 SEQRES 21 264 SER HIS ASP GLU 1MAT 78 FTNOTE 1 1MAT 79 FTNOTE 1 CIS PROLINE - PRO 181 1MAT 80 FTNOTE 2 1MAT 81 FTNOTE 2 FOLLOWING RESIDUES TRUNCATED TO ALA: GLU 12, LYS 13, 1MAT 82 FTNOTE 2 LYS 117, GLU 123, VAL 194, LEU 195, AND LYS 218. 1MAT 83 FTNOTE 3 1MAT 84 FTNOTE 3 RESIDUE LEU 88 TRUNCATED TO GLY. 1MAT 85 FTNOTE 4 1MAT 86 FTNOTE 4 FOLLOWING RESIDUES TRUNCATED TO GAMMA CARBON: GLU 9, ARG 1MAT 87 FTNOTE 4 93, LYS 86, LEU 87, LYS 89, THR 119, GLU 167, LYS 211, LYS 1MAT 88 FTNOTE 4 226, ARG 228, AND GLU 264. 1MAT 89 FTNOTE 5 1MAT 90 FTNOTE 5 FOLLOWING RESIDUES TRUNCATED TO DELTA CARBON: ARG 19, LYS 1MAT 91 FTNOTE 5 155, ARG 189, AND LYS 196. 1MAT 92 FTNOTE 6 1MAT 93 FTNOTE 6 RESIDUE LYS 252 TRUNCATED TO EPSILON CARBON. 1MAT 94 FTNOTE 7 1MAT 95 FTNOTE 7 FOLLOWING RESIDUES TRUNCATED TO VAL: ILE 49, ILE 120, AND 1MAT 96 FTNOTE 7 ILE 144. 1MAT 97 HET CO 401 1 COBALT ++ CATION 1MAT 98 HET CO 402 1 COBALT ++ CATION 1MAT 99 FORMUL 2 CO 2(CO1 ++) 1MAT 100 FORMUL 3 HOH *15(H2 O1) 1MAT 101 HELIX 1 A THR 7 GLU 29 1 RELATED TO C BY PSEUDO-2 FOLD 1MAT 102 HELIX 2 B SER 37 HIS 54 1 RELATED TO D BY PSEUDO-2 FOLD 1MAT 103 HELIX 3 C ILE 120 VAL 140 1 RELATED TO A BY PSEUDO-2 FOLD 1MAT 104 HELIX 4 D ASN 145 GLU 160 1 RELATED TO B BY PSEUDO-2 FOLD 1MAT 105 SHEET 1 1A 5 VAL 56 ALA 58 0 1MAT 106 SHEET 2 1A 5 ASP 92 LYS 102 -1 O ILE 101 N VAL 56 1MAT 107 SHEET 3 1A 5 HIS 106 VAL 115 -1 O THR 109 N VAL 98 1MAT 108 SHEET 4 1A 5 SER 231 VAL 240 -1 N GLU 235 O SER 110 1MAT 109 SHEET 5 1A 5 MET 199 ALA 209 -1 N PHE 201 O ILE 238 1MAT 110 SHEET 1 1B 6 CYS 70 ASN 74 0 1MAT 111 SHEET 2 1B 6 ASP 92 LYS 102 -1 N ASP 97 O CYS 70 1MAT 112 SHEET 3 1B 6 HIS 106 VAL 115 -1 O THR 109 N VAL 98 1MAT 113 SHEET 4 1B 6 SER 231 VAL 240 -1 N GLU 235 O SER 110 1MAT 114 SHEET 5 1B 6 GLY 244 LEU 248 -1 N GLU 246 O VAL 239 1MAT 115 SHEET 6 1B 6 ALA 258 HIS 262 -1 O ILE 260 N CYS 245 1MAT 116 TURN 1 A LYS 33 VAL 36 1MAT 117 TURN 2 B CYS 59 TYR 62 1MAT 118 TURN 3 C TYR 62 TYR 65 1MAT 119 TURN 4 D ILE 73 VAL 76 1MAT 120 TURN 5 E LYS 102 PHE 105 1MAT 121 TURN 6 F LYS 141 ILE 144 1MAT 122 TURN 7 G GLU 158 GLY 161 1MAT 123 TURN 8 H SER 188 THR 191 1MAT 124 TURN 9 I LYS 196 GLY 198 1MAT 125 TURN 10 J THR 241 GLY 244 1MAT 126 TURN 11 K ARG 251 ASP 254 1MAT 127 SITE 1 ACT 7 ASP 97 ASP 108 HIS 171 GLU 204 1MAT 128 SITE 2 ACT 7 GLU 235 CO 401 ALA 2 1MAT 129 CRYST1 39.000 61.700 54.500 90.00 107.30 90.00 P 21 2 1MAT 130 ORIGX1 1.000000 0.000000 0.000000 0.00000 1MAT 131 ORIGX2 0.000000 1.000000 0.000000 0.00000 1MAT 132 ORIGX3 0.000000 0.000000 1.000000 0.00000 1MAT 133 SCALE1 0.025641 0.000000 0.007986 0.00000 1MAT 134 SCALE2 0.000000 0.016207 0.000000 0.00000 1MAT 135 SCALE3 0.000000 0.000000 0.019218 0.00000 1MAT 136 MTRIX1 1 0.333795 0.741892 0.581532 -63.26726 1 1MAT 137 MTRIX2 1 0.657432 -0.625330 0.420413 52.73847 1 1MAT 138 MTRIX3 1 0.675552 0.241987 -0.696475 76.57813 1 1MAT 139