LongText Report for: 1YSC-pdb
1YSC-pdb | HEADER HYDROLASE(CARBOXYPEPTIDASE) 08-MAR-94 1YSC 1YSC 2
COMPND SERINE CARBOXYPEPTIDASE (CPY, CPD-Y, OR PROTEINASE C) 1YSC 3
COMPND 2 (E.C.3.4.16.5) 1YSC 4
SOURCE YEAST (SACCHAROMYCES CEREVISIAE) 1YSC 5
AUTHOR J.A.ENDRIZZI,S.J.REMINGTON 1YSC 6
REVDAT 1 22-JUN-94 1YSC 0 1YSC 7
JRNL AUTH J.A.ENDRIZZI,K.BREDDAM,S.J.REMINGTON 1YSC 8
JRNL TITL 2.8 ANGSTROMS STRUCTURE OF YEAST SERINE 1YSC 9
JRNL TITL 2 CARBOXYPEPTIDASE 1YSC 10
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1YSC 11
JRNL REFN 0353 1YSC 12
REMARK 1 1YSC 13
REMARK 2 1YSC 14
REMARK 2 RESOLUTION. 2.8 ANGSTROMS. 1YSC 15
REMARK 3 1YSC 16
REMARK 3 REFINEMENT. 1YSC 17
REMARK 3 PROGRAM TNT 1YSC 18
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1YSC 19
REMARK 3 R VALUE 0.162 1YSC 20
REMARK 3 RMSD BOND DISTANCES 0.16 ANGSTROMS 1YSC 21
REMARK 3 RMSD BOND ANGLES 2.75 DEGREES 1YSC 22
REMARK 3 1YSC 23
REMARK 3 NUMBER OF PROTEIN ATOMS 3253 1YSC 24
REMARK 3 NUMBER OF SOLVENT ATOMS 38 1YSC 25
REMARK 4 1YSC 26
REMARK 4 IN *SITE RECORDS BELOW, CAT REFERS TO CATALYTIC RESIDUES, 1YSC 27
REMARK 4 CBS REFERS TO CARBOXYLATE BINDING SITE, S1P REFERS TO A 1YSC 28
REMARK 4 S1' SUBSITE (BINDS C-TERMINAL SIDE CHAIN), AND S1S REFERS 1YSC 29
REMARK 4 TO A S1 SUBSITE (BINDS PENULTIMATE SIDE CHAIN). 1YSC 30
REMARK 5 1YSC 31
REMARK 5 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN 1YSC 32
REMARK 5 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, 1YSC 33
REMARK 5 TWO SHEETS ARE DEFINED. STRANDS 1, 2, 3, 5, 6, 7, 8, 9, 10 1YSC 34
REMARK 5 AND 11 OF S1A AND S1B ARE IDENTICAL. 1YSC 35
REMARK 6 1YSC 36
REMARK 6 SOME SURFACE LOOPS ARE POORLY DEFINED AND HAVE HIGH 1YSC 37
REMARK 6 B-VALUES, INCLUDING RESIDUES 1 - 17, 23 - 26, 105 - 108, 1YSC 38
REMARK 6 134 - 138, 263 - 266, 282 - 286, 375 - 376. 1YSC 39
REMARK 6 1YSC 40
REMARK 6 PDB ADVISORY NOTICE: 1YSC 41
REMARK 6 RESIDUES ILE 71, ILE 275, ILE 302 AND ILE 415 HAVE 1YSC 42
REMARK 6 CHIRALITY PROBLEM. 1YSC 43
REMARK 7 1YSC 44
REMARK 7 SIDE CHAIN ATOMS OF RESIDUES ARE MISSING BECAUSE THE 1YSC 45
REMARK 7 ELECTRON DENSITY WAS ILL-DEFINED. 1YSC 46
SEQRES 1 421 LYS ILE LYS ASP PRO LYS ILE LEU GLY ILE ASP PRO ASN 1YSC 47
SEQRES 2 421 VAL THR GLN TYR THR GLY TYR LEU ASP VAL GLU ASP GLU 1YSC 48
SEQRES 3 421 ASP LYS HIS PHE PHE PHE TRP THR PHE GLU SER ARG ASN 1YSC 49
SEQRES 4 421 ASP PRO ALA LYS ASP PRO VAL ILE LEU TRP LEU ASN GLY 1YSC 50
SEQRES 5 421 GLY PRO GLY CYS SER SER LEU THR GLY LEU PHE PHE GLU 1YSC 51
SEQRES 6 421 LEU GLY PRO SER SER ILE GLY PRO ASP LEU LYS PRO ILE 1YSC 52
SEQRES 7 421 GLY ASN PRO TYR SER TRP ASN SER ASN ALA THR VAL ILE 1YSC 53
SEQRES 8 421 PHE LEU ASP GLN PRO VAL ASN VAL GLY PHE SER TYR SER 1YSC 54
SEQRES 9 421 GLY SER SER GLY VAL SER ASN THR VAL ALA ALA GLY LYS 1YSC 55
SEQRES 10 421 ASP VAL TYR ASN PHE LEU GLU LEU PHE PHE ASP GLN PHE 1YSC 56
SEQRES 11 421 PRO GLU TYR VAL ASN LYS GLY GLN ASP PHE HIS ILE ALA 1YSC 57
SEQRES 12 421 GLY GLU SER TYR ALA GLY HIS TYR ILE PRO VAL PHE ALA 1YSC 58
SEQRES 13 421 SER GLU ILE LEU SER HIS LYS ASP ARG ASN PHE ASN LEU 1YSC 59
SEQRES 14 421 THR SER VAL LEU ILE GLY ASN GLY LEU THR ASP PRO LEU 1YSC 60
SEQRES 15 421 THR GLN TYR ASN TYR TYR GLU PRO MET ALA CYS GLY GLU 1YSC 61
SEQRES 16 421 GLY GLY GLU PRO SER VAL LEU PRO SER GLU GLU CYS SER 1YSC 62
SEQRES 17 421 ALA MET GLU ASP SER LEU GLU ARG CYS LEU GLY LEU ILE 1YSC 63
SEQRES 18 421 GLU SER CYS TYR ASP SER GLN SER VAL TRP SER CYS VAL 1YSC 64
SEQRES 19 421 PRO ALA THR ILE TYR CYS ASN ASN ALA GLN LEU ALA PRO 1YSC 65
SEQRES 20 421 TYR GLN ARG THR GLY ARG ASN VAL TYR ASP ILE ARG LYS 1YSC 66
SEQRES 21 421 ASP CYS GLU GLY GLY ASN LEU CYS TYR PRO THR LEU GLN 1YSC 67
SEQRES 22 421 ASP ILE ASP ASP TYR LEU ASN GLN ASP TYR VAL LYS GLU 1YSC 68
SEQRES 23 421 ALA VAL GLY ALA GLU VAL ASP HIS TYR GLU SER CYS ASN 1YSC 69
SEQRES 24 421 PHE ASP ILE ASN ARG ASN PHE LEU PHE ALA GLY ASP TRP 1YSC 70
SEQRES 25 421 MET LYS PRO TYR HIS THR ALA VAL THR ASP LEU LEU ASN 1YSC 71
SEQRES 26 421 GLN ASP LEU PRO ILE LEU VAL TYR ALA GLY ASP LYS ASP 1YSC 72
SEQRES 27 421 PHE ILE CYS ASN TRP LEU GLY ASN LYS ALA TRP THR ASP 1YSC 73
SEQRES 28 421 VAL LEU PRO TRP LYS TYR ASP GLU GLU PHE ALA SER GLN 1YSC 74
SEQRES 29 421 LYS VAL ARG ASN TRP THR ALA SER ILE THR ASP GLU VAL 1YSC 75
SEQRES 30 421 ALA GLY GLU VAL LYS SER TYR LYS HIS PHE THR TYR LEU 1YSC 76
SEQRES 31 421 ARG VAL PHE ASN GLY GLY HIS MET VAL PRO PHE ASP VAL 1YSC 77
SEQRES 32 421 PRO GLU ASN ALA LEU SER MET VAL ASN GLU TRP ILE HIS 1YSC 78
SEQRES 33 421 GLY GLY PHE SER LEU 1YSC 79
FTNOTE 1 1YSC 80
FTNOTE 1 CIS PROLINE - PRO 54 1YSC 81
FTNOTE 2 1YSC 82
FTNOTE 2 CIS PROLINE - PRO 96 1YSC 83
FTNOTE 3 1YSC 84
FTNOTE 3 RESIDUE NAG 871 HAS STRONGER ELECTRON DENSITY BETWEEN IT 1YSC 85
FTNOTE 3 AND ASN 39 THAN ASN 87. IT IS EXPECTED TO RESIDE ON THE 1YSC 86
FTNOTE 3 LATTER RESIDUE. 1YSC 87
HET NAG 871 14 N-ACETYL-D-GLUCOSAMINE 1YSC 88
HET NAG 1681 14 N-ACETYL-D-GLUCOSAMINE 1YSC 89
HET NAG 3681 14 N-ACETYL-D-GLUCOSAMINE 1YSC 90
FORMUL 2 NAG 3(C8 H15 N1 O6) 1YSC 91
FORMUL 3 HOH *38(H2 O1) 1YSC 92
HELIX 1 A LEU 59 LEU 62 1 1YSC 93
HELIX 2 B TRP 84 ASN 87 5 1YSC 94
HELIX 3 C VAL 113 GLN 129 1 1YSC 95
HELIX 4 D PRO 131 TYR 133 5 1YSC 96
HELIX 5 E ALA 148 LEU 160 1 1YSC 97
HELIX 6 F PRO 181 ALA 192 1 1YSC 98
HELIX 7 G SER 204 SER 227 1 1YSC 99
HELIX 8 H VAL 230 THR 251 1 1YSC 100
HELIX 9 I THR 271 ASN 280 1 1YSC 101
HELIX 10 J ASP 282 ALA 287 1 1YSC 102
HELIX 11 K PHE 300 LEU 307 1 1YSC 103
HELIX 12 L ASP 311 MET 313 5 1YSC 104
HELIX 13 M HIS 317 ASN 325 1 1YSC 105
HELIX 14 N TRP 343 THR 350 1 1YSC 106
HELIX 15 O GLU 359 SER 363 1 1YSC 107
HELIX 16 P VAL 399 ASP 402 1 1YSC 108
HELIX 17 Q PRO 404 ILE 415 1 1YSC 109
SHEET 1 S1A11 LYS 1 LYS 3 0 1YSC 110
SHEET 2 S1A11 TYR 17 VAL 23 -1 1YSC 111
SHEET 3 S1A11 LYS 28 PHE 35 1 1YSC 112
SHEET 4 S1A11 THR 89 ILE 91 -1 1YSC 113
SHEET 5 S1A11 VAL 46 LEU 50 -1 1YSC 114
SHEET 6 S1A11 PHE 140 GLU 145 -1 1YSC 115
SHEET 7 S1A11 LEU 169 GLY 175 -1 1YSC 116
SHEET 8 S1A11 ILE 330 GLY 335 -1 1YSC 117
SHEET 9 S1A11 PHE 387 VAL 392 -1 1YSC 118
SHEET 10 S1A11 VAL 377 TYR 384 1 1YSC 119
SHEET 11 S1A11 ARG 367 THR 370 -1 1YSC 120
SHEET 1 S1B11 LYS 1 LYS 3 0 1YSC 121
SHEET 2 S1B11 TYR 17 VAL 23 -1 1YSC 122
SHEET 3 S1B11 LYS 28 PHE 35 1 1YSC 123
SHEET 4 S1B11 TYR 103 SER 104 -1 1YSC 124
SHEET 5 S1B11 VAL 46 LEU 50 -1 1YSC 125
SHEET 6 S1B11 PHE 140 GLU 145 -1 1YSC 126
SHEET 7 S1B11 LEU 169 GLY 175 -1 1YSC 127
SHEET 8 S1B11 ILE 330 GLY 335 -1 1YSC 128
SHEET 9 S1B11 PHE 387 VAL 392 -1 1YSC 129
SHEET 10 S1B11 VAL 377 TYR 384 1 1YSC 130
SHEET 11 S1B11 ARG 367 THR 370 -1 1YSC 131
TURN 1 T1 GLU 24 ASP 27 HIGH BETA-LOOP 1YSC 132
TURN 2 T2 GLY 52 GLY 55 1YSC 133
TURN 3 T3 GLY 72 LEU 75 1YSC 134
TURN 4 T4 ASN 85 ALA 88 1YSC 135
TURN 5 T5 PRO 96 VAL 99 1YSC 136
TURN 6 T6 VAL 99 SER 102 1YSC 137
TURN 7 T7 VAL 134 GLY 137 1YSC 138
TURN 8 T8 GLU 145 ALA 148 1YSC 139
TURN 9 T9 GLN 249 GLY 252 1YSC 140
TURN 10 T10 ASN 254 ASP 257 3.6 ANGSTROMS 1YSC 141
SSBOND 1 CYS 56 CYS 298 1YSC 142
SSBOND 2 CYS 193 CYS 207 1YSC 143
SSBOND 3 CYS 217 CYS 240 1YSC 144
SSBOND 4 CYS 224 CYS 233 1YSC 145
SSBOND 5 CYS 262 CYS 268 1YSC 146
SITE 1 CAT 4 SER 146 ASP 338 HIS 397 GLU 145 1YSC 147
SITE 1 CBS 4 ASN 51 GLY 52 GLU 145 HIS 397 1YSC 148
SITE 1 S1P 7 THR 60 PHE 64 GLU 65 TYR 256 1YSC 149
SITE 2 S1P 7 TYR 269 LEU 272 MET 398 1YSC 150
SITE 1 S1S 6 TYR 147 LEU 178 LEU 245 TRP 312 1YSC 151
SITE 2 S1S 6 ILE 340 CYS 341 1YSC 152
CRYST1 111.800 111.800 111.800 90.00 90.00 90.00 P 21 3 12 1YSC 153
ORIGX1 1.000000 0.000000 0.000000 0.00000 1YSC 154
ORIGX2 0.000000 1.000000 0.000000 0.00000 1YSC 155
ORIGX3 0.000000 0.000000 1.000000 0.00000 1YSC 156
SCALE1 0.008945 0.000000 0.000000 0.00000 1YSC 157
SCALE2 0.000000 0.008945 0.000000 0.00000 1YSC 158
SCALE3 0.000000 0.000000 0.008945 0.00000 1YSC 159
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