LongText Report for: 1CPY-pdb
1CPY-pdb | HEADER HYDROLASE (CARBOXYPEPTIDASE) 24-MAR-95 1CPY 1CPY 2
COMPND MOL_ID: 1; 1CPY 3
COMPND 2 MOLECULE: SERINE CARBOXYPEPTIDASE; 1CPY 4
COMPND 3 CHAIN: NULL; 1CPY 5
COMPND 4 EC: 3.4.16.5; 1CPY 6
COMPND 5 MUTATION: E65A, E145A 1CPY 7
SOURCE MOL_ID: 1; 1CPY 8
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; 1CPY 9
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST 1CPY 10
EXPDTA X-RAY DIFFRACTION 1CPY 11
AUTHOR S.B.SORENSEN,M.RAASCHOU-NIELSEN,U.MORTENSEN,S.J.REMINGTON, 1CPY 12
AUTHOR 2 K.BREDDAM 1CPY 13
REVDAT 1 15-SEP-95 1CPY 0 1CPY 14
JRNL AUTH S.B.SORENSEN,M.RAASCHOU-NIELSEN,U.H.MORTENSEN, 1CPY 15
JRNL AUTH 2 S.J.REMINGTON,K.BREDDAM 1CPY 16
JRNL TITL SITE-DIRECTED MUTAGENESIS ON (SERINE) 1CPY 17
JRNL TITL 2 CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF 1CPY 18
JRNL TITL 3 THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS 1CPY 19
JRNL TITL 4 REACTIONS 1CPY 20
JRNL REF J.AM.CHEM.SOC. V. 117 5944 1995 1CPY 21
JRNL REFN ASTM JACSAT US ISSN 0002-7863 0004 1CPY 22
REMARK 1 1CPY 23
REMARK 1 REFERENCE 1 1CPY 24
REMARK 1 AUTH J.A.ENDRIZZI,K.BREDDAM,S.J.REMINGTON 1CPY 25
REMARK 1 TITL 2.8 ANGSTROMS STRUCTURE OF YEAST SERINE 1CPY 26
REMARK 1 TITL 2 CARBOXYPEPTIDASE 1CPY 27
REMARK 1 REF BIOCHEMISTRY V. 33 11106 1994 1CPY 28
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960 0033 1CPY 29
REMARK 2 1CPY 30
REMARK 2 RESOLUTION. 2.6 ANGSTROMS. 1CPY 31
REMARK 3 1CPY 32
REMARK 3 REFINEMENT. 1CPY 33
REMARK 3 PROGRAM : TNT 1CPY 34
REMARK 3 AUTHORS : TRONRUD,TEN EYCK,MATTHEWS 1CPY 35
REMARK 3 1CPY 36
REMARK 3 MODEL QUALITY. 1CPY 37
REMARK 3 R VALUE (NO SIGMA CUTOFF) : 0.180 1CPY 38
REMARK 3 SIGMA CUTOFF LEVEL : 0.0 1CPY 39
REMARK 3 1CPY 40
REMARK 3 NUMBER OF ATOMS USED IN REFINEMENT. 1CPY 41
REMARK 3 PROTEIN ATOMS : 3245 1CPY 42
REMARK 3 NUCLEIC ACID ATOMS : 0 1CPY 43
REMARK 3 HETEROGEN ATOMS : 42 1CPY 44
REMARK 3 SOLVENT ATOMS : 38 1CPY 45
REMARK 3 1CPY 46
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. RMS WEIGHT COUNT 1CPY 47
REMARK 3 BOND LENGTHS (A) : 0.023 ; ; 1CPY 48
REMARK 3 BOND ANGLES (DEGREES) : 3.3 ; ; 1CPY 49
REMARK 3 1CPY 50
REMARK 3 DATA COLLECTION. 1CPY 51
REMARK 3 NUMBER OF UNIQUE REFLECTIONS 14110 1CPY 52
REMARK 3 RESOLUTION RANGE 20.0 - 2.6 ANGSTROMS 1CPY 53
REMARK 3 COMPLETENESS OF DATA 92.0 % 1CPY 54
REMARK 3 REJECTION CRITERIA 0.0 SIGMA(I) 1CPY 55
REMARK 4 1CPY 56
REMARK 4 IN *SITE RECORDS BELOW, CAT REFERS TO CATALYTIC RESIDUES, 1CPY 57
REMARK 4 CBS REFERS TO CARBOXYLATE BINDING SITE, S1P REFERS TO A 1CPY 58
REMARK 4 S1' SUBSITE (BINDS C-TERMINAL SIDE CHAIN), AND S1S REFERS 1CPY 59
REMARK 4 TO A S1 SUBSITE (BINDS PENULTIMATE SIDE CHAIN). 1CPY 60
REMARK 5 1CPY 61
REMARK 5 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN 1CPY 62
REMARK 5 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, 1CPY 63
REMARK 5 TWO SHEETS ARE DEFINED. STRANDS 1, 2, 3, 5, 6, 7, 8, 9, 10 1CPY 64
REMARK 5 AND 11 OF S1A AND S1B ARE IDENTICAL. 1CPY 65
REMARK 6 1CPY 66
REMARK 6 SOME SURFACE LOOPS ARE POORLY DEFINED AND HAVE HIGH 1CPY 67
REMARK 6 B-VALUES, INCLUDING RESIDUES 1 - 17, 23 - 26, 105 - 108, 1CPY 68
REMARK 6 134 - 138, 263 - 266, 282 - 286, 375 - 376. 1CPY 69
REMARK 6 1CPY 70
REMARK 6 PDB ADVISORY NOTICE: 1CPY 71
REMARK 6 RESIDUES ILE 275, ILE 302 AND ILE 415 HAVE A CHIRALITY 1CPY 72
REMARK 6 PROBLEM. 1CPY 73
REMARK 7 1CPY 74
REMARK 7 SIDE CHAIN ATOMS OF RESIDUES ARE MISSING BECAUSE THE 1CPY 75
REMARK 7 ELECTRON DENSITY WAS ILL-DEFINED. 1CPY 76
REMARK 19 1CPY 77
REMARK 19 MATTHEWS COEFFICIENT (VM) : 2.1 ANGSTROMS**3/DA 1CPY 78
REMARK 999 1CPY 79
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1CPY 80
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1CPY 81
REMARK 999 CBPY_YEAST 1CPY 82
SEQRES 1 421 LYS ILE LYS ASP PRO LYS ILE LEU GLY ILE ASP PRO ASN 1CPY 83
SEQRES 2 421 VAL THR GLN TYR THR GLY TYR LEU ASP VAL GLU ASP GLU 1CPY 84
SEQRES 3 421 ASP LYS HIS PHE PHE PHE TRP THR PHE GLU SER ARG ASN 1CPY 85
SEQRES 4 421 ASP PRO ALA LYS ASP PRO VAL ILE LEU TRP LEU ASN GLY 1CPY 86
SEQRES 5 421 GLY PRO GLY CYS SER SER LEU THR GLY LEU PHE PHE ALA 1CPY 87
SEQRES 6 421 LEU GLY PRO SER SER ILE GLY PRO ASP LEU LYS PRO ILE 1CPY 88
SEQRES 7 421 GLY ASN PRO TYR SER TRP ASN SER ASN ALA THR VAL ILE 1CPY 89
SEQRES 8 421 PHE LEU ASP GLN PRO VAL ASN VAL GLY PHE SER TYR SER 1CPY 90
SEQRES 9 421 GLY SER SER GLY VAL SER ASN THR VAL ALA ALA GLY LYS 1CPY 91
SEQRES 10 421 ASP VAL TYR ASN PHE LEU GLU LEU PHE PHE ASP GLN PHE 1CPY 92
SEQRES 11 421 PRO GLU TYR VAL ASN LYS GLY GLN ASP PHE HIS ILE ALA 1CPY 93
SEQRES 12 421 GLY ALA SER TYR ALA GLY HIS TYR ILE PRO VAL PHE ALA 1CPY 94
SEQRES 13 421 SER GLU ILE LEU SER HIS LYS ASP ARG ASN PHE ASN LEU 1CPY 95
SEQRES 14 421 THR SER VAL LEU ILE GLY ASN GLY LEU THR ASP PRO LEU 1CPY 96
SEQRES 15 421 THR GLN TYR ASN TYR TYR GLU PRO MET ALA CYS GLY GLU 1CPY 97
SEQRES 16 421 GLY GLY GLU PRO SER VAL LEU PRO SER GLU GLU CYS SER 1CPY 98
SEQRES 17 421 ALA MET GLU ASP SER LEU GLU ARG CYS LEU GLY LEU ILE 1CPY 99
SEQRES 18 421 GLU SER CYS TYR ASP SER GLN SER VAL TRP SER CYS VAL 1CPY 100
SEQRES 19 421 PRO ALA THR ILE TYR CYS ASN ASN ALA GLN LEU ALA PRO 1CPY 101
SEQRES 20 421 TYR GLN ARG THR GLY ARG ASN VAL TYR ASP ILE ARG LYS 1CPY 102
SEQRES 21 421 ASP CYS GLU GLY GLY ASN LEU CYS TYR PRO THR LEU GLN 1CPY 103
SEQRES 22 421 ASP ILE ASP ASP TYR LEU ASN GLN ASP TYR VAL LYS GLU 1CPY 104
SEQRES 23 421 ALA VAL GLY ALA GLU VAL ASP HIS TYR GLU SER CYS ASN 1CPY 105
SEQRES 24 421 PHE ASP ILE ASN ARG ASN PHE LEU PHE ALA GLY ASP TRP 1CPY 106
SEQRES 25 421 MET LYS PRO TYR HIS THR ALA VAL THR ASP LEU LEU ASN 1CPY 107
SEQRES 26 421 GLN ASP LEU PRO ILE LEU VAL TYR ALA GLY ASP LYS ASP 1CPY 108
SEQRES 27 421 PHE ILE CYS ASN TRP LEU GLY ASN LYS ALA TRP THR ASP 1CPY 109
SEQRES 28 421 VAL LEU PRO TRP LYS TYR ASP GLU GLU PHE ALA SER GLN 1CPY 110
SEQRES 29 421 LYS VAL ARG ASN TRP THR ALA SER ILE THR ASP GLU VAL 1CPY 111
SEQRES 30 421 ALA GLY GLU VAL LYS SER TYR LYS HIS PHE THR TYR LEU 1CPY 112
SEQRES 31 421 ARG VAL PHE ASN GLY GLY HIS MET VAL PRO PHE ASP VAL 1CPY 113
SEQRES 32 421 PRO GLU ASN ALA LEU SER MET VAL ASN GLU TRP ILE HIS 1CPY 114
SEQRES 33 421 GLY GLY PHE SER LEU 1CPY 115
FTNOTE 1 1CPY 116
FTNOTE 1 CIS PROLINE - PRO 54 1CPY 117
FTNOTE 2 1CPY 118
FTNOTE 2 CIS PROLINE - PRO 96 1CPY 119
HET NAG 871 14 N-ACETYL-D-GLUCOSAMINE 1CPY 120
HET NAG 1681 14 N-ACETYL-D-GLUCOSAMINE 1CPY 121
HET NAG 3681 14 N-ACETYL-D-GLUCOSAMINE 1CPY 122
FORMUL 2 NAG 3(C8 H15 N1 O6) 1CPY 123
FORMUL 3 HOH *38(H2 O1) 1CPY 124
HELIX 1 A LEU 59 LEU 62 1 1CPY 125
HELIX 2 B TRP 84 ASN 87 5 1CPY 126
HELIX 3 C VAL 113 GLN 129 1 1CPY 127
HELIX 4 D PRO 131 TYR 133 5 1CPY 128
HELIX 5 E ALA 148 LEU 160 1 1CPY 129
HELIX 6 F PRO 181 ALA 192 1 1CPY 130
HELIX 7 G SER 204 SER 227 1 1CPY 131
HELIX 8 H VAL 230 THR 251 1 1CPY 132
HELIX 9 I THR 271 ASN 280 1 1CPY 133
HELIX 10 J ASP 282 ALA 287 1 1CPY 134
HELIX 11 K PHE 300 LEU 307 1 1CPY 135
HELIX 12 L ASP 311 MET 313 5 1CPY 136
HELIX 13 M HIS 317 ASN 325 1 1CPY 137
HELIX 14 N TRP 343 THR 350 1 1CPY 138
HELIX 15 O GLU 359 SER 363 1 1CPY 139
HELIX 16 P VAL 399 ASP 402 1 1CPY 140
HELIX 17 Q PRO 404 ILE 415 1 1CPY 141
SHEET 1 S1A11 LYS 1 LYS 3 0 1CPY 142
SHEET 2 S1A11 TYR 17 VAL 23 -1 1CPY 143
SHEET 3 S1A11 LYS 28 PHE 35 1 1CPY 144
SHEET 4 S1A11 THR 89 ILE 91 -1 1CPY 145
SHEET 5 S1A11 VAL 46 LEU 50 -1 1CPY 146
SHEET 6 S1A11 PHE 140 ALA 145 -1 1CPY 147
SHEET 7 S1A11 LEU 169 GLY 175 -1 1CPY 148
SHEET 8 S1A11 ILE 330 GLY 335 -1 1CPY 149
SHEET 9 S1A11 PHE 387 VAL 392 -1 1CPY 150
SHEET 10 S1A11 VAL 377 TYR 384 1 1CPY 151
SHEET 11 S1A11 ARG 367 THR 370 -1 1CPY 152
SHEET 1 S1B11 LYS 1 LYS 3 0 1CPY 153
SHEET 2 S1B11 TYR 17 VAL 23 -1 1CPY 154
SHEET 3 S1B11 LYS 28 PHE 35 1 1CPY 155
SHEET 4 S1B11 TYR 103 SER 104 -1 1CPY 156
SHEET 5 S1B11 VAL 46 LEU 50 -1 1CPY 157
SHEET 6 S1B11 PHE 140 ALA 145 -1 1CPY 158
SHEET 7 S1B11 LEU 169 GLY 175 -1 1CPY 159
SHEET 8 S1B11 ILE 330 GLY 335 -1 1CPY 160
SHEET 9 S1B11 PHE 387 VAL 392 -1 1CPY 161
SHEET 10 S1B11 VAL 377 TYR 384 1 1CPY 162
SHEET 11 S1B11 ARG 367 THR 370 -1 1CPY 163
TURN 1 T1 GLU 24 ASP 27 HIGH BETA-LOOP 1CPY 164
TURN 2 T2 GLY 52 GLY 55 1CPY 165
TURN 3 T3 GLY 72 LEU 75 1CPY 166
TURN 4 T4 ASN 85 ALA 88 1CPY 167
TURN 5 T5 PRO 96 VAL 99 1CPY 168
TURN 6 T6 VAL 99 SER 102 1CPY 169
TURN 7 T7 VAL 134 GLY 137 1CPY 170
TURN 8 T8 ALA 145 ALA 148 1CPY 171
TURN 9 T9 GLN 249 GLY 252 1CPY 172
TURN 10 T10 ASN 254 ASP 257 3.6 ANGSTROMS 1CPY 173
SSBOND 1 CYS 56 CYS 298 1CPY 174
SSBOND 2 CYS 193 CYS 207 1CPY 175
SSBOND 3 CYS 217 CYS 240 1CPY 176
SSBOND 4 CYS 224 CYS 233 1CPY 177
SSBOND 5 CYS 262 CYS 268 1CPY 178
SITE 1 CAT 4 SER 146 ASP 338 HIS 397 ALA 145 1CPY 179
SITE 1 CBS 4 ASN 51 GLY 52 ALA 145 HIS 397 1CPY 180
SITE 1 S1P 7 THR 60 PHE 64 ALA 65 TYR 256 1CPY 181
SITE 2 S1P 7 TYR 269 LEU 272 MET 398 1CPY 182
SITE 1 S1S 6 TYR 147 LEU 178 LEU 245 TRP 312 1CPY 183
SITE 2 S1S 6 ILE 340 CYS 341 1CPY 184
CRYST1 112.000 112.000 112.000 90.00 90.00 90.00 P 21 3 12 1CPY 185
ORIGX1 1.000000 0.000000 0.000000 0.00000 1CPY 186
ORIGX2 0.000000 1.000000 0.000000 0.00000 1CPY 187
ORIGX3 0.000000 0.000000 1.000000 0.00000 1CPY 188
SCALE1 0.008929 0.000000 0.000000 0.00000 1CPY 189
SCALE2 0.000000 0.008929 0.000000 0.00000 1CPY 190
SCALE3 0.000000 0.000000 0.008929 0.00000 1CPY 191
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