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HEADER HYDROLASE(CARBOXYPEPTIDASE) 01-JUL-92 3SC2 3SC2 2
COMPND SERINE CARBOXYPEPTIDASE II (E.C.3.4.16.1) (CPDW-II) 3SC2 3
SOURCE WHEAT (TRITICUM VULGARIS) GERM 3SC2 4
AUTHOR D.-*I.LIAO,S.J.REMINGTON 3SC2 5
REVDAT 1 31-OCT-93 3SC2 0 3SC2 6
SPRSDE 15-OCT-93 3SC2 2SC2 3SC2 7
JRNL AUTH D.-I.LIAO,K.BREDDAM,R.M.SWEET,T.BULLOCK, 3SC2 8
JRNL AUTH 2 S.J.REMINGTON 3SC2 9
JRNL TITL REFINED ATOMIC MODEL OF WHEAT SERINE 3SC2 10
JRNL TITL 2 CARBOXYPEPTIDASE II AT 2.2-ANGSTROMS RESOLUTION 3SC2 11
JRNL REF BIOCHEMISTRY V. 31 9796 1992 3SC2 12
JRNL REFN ASTM BICHAW US ISSN 0006-2960 033 3SC2 13
REMARK 1 3SC2 14
REMARK 1 REFERENCE 1 3SC2 15
REMARK 1 AUTH D.-I.LIAO,S.J.REMINGTON 3SC2 16
REMARK 1 TITL STRUCTURE OF WHEAT SERINE CARBOXYPEPTIDASE II AT 3SC2 17
REMARK 1 TITL 2 3.5 ANGSTROMS RESOLUTION 3SC2 18
REMARK 1 REF J.BIOL.CHEM. V. 265 6528 1990 3SC2 19
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 071 3SC2 20
REMARK 1 REFERENCE 2 3SC2 21
REMARK 1 AUTH K.P.WILSON,D.-I.LIAO,T.BULLOCK,S.J.REMINGTON, 3SC2 22
REMARK 1 AUTH 2 K.BREDDAM 3SC2 23
REMARK 1 TITL CRYSTALLIZATION OF SERINE CARBOXYPEPTIDASES 3SC2 24
REMARK 1 REF J.MOL.BIOL. V. 211 301 1990 3SC2 25
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 3SC2 26
REMARK 1 REFERENCE 3 3SC2 27
REMARK 1 AUTH K.BREDDAM,S.B.SORENSEN,I.SVENDSEN 3SC2 28
REMARK 1 TITL PRIMARY STRUCTURE AND ENZYMATIC PROPERTIES OF 3SC2 29
REMARK 1 TITL 2 CARBOXYPEPTIDASE II FROM WHEAT BRAN 3SC2 30
REMARK 1 REF CARLSBERG RES.COMMUN. V. 52 297 1987 3SC2 31
REMARK 1 REFN ASTM CRCODS DK ISSN 0105-1938 915 3SC2 32
REMARK 2 3SC2 33
REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 3SC2 34
REMARK 3 3SC2 35
REMARK 3 REFINEMENT. 3SC2 36
REMARK 3 PROGRAM TNT 3SC2 37
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 3SC2 38
REMARK 3 R VALUE 0.169 3SC2 39
REMARK 3 RMSD BOND DISTANCES 0.018 ANGSTROMS 3SC2 40
REMARK 3 RMSD BOND ANGLES 2.80 DEGREES 3SC2 41
REMARK 4 3SC2 42
REMARK 4 CPDW II CONTAINS TWO PEPTIDE CHAINS WHICH HAVE BEEN 3SC2 43
REMARK 4 ASSIGNED CHAIN INDICATORS *A* AND *B*. THE RESIDUE 3SC2 44
REMARK 4 NUMBERING IS BASED ON SEQUENCE ALIGNMENT WITH YEAST SERINE 3SC2 45
REMARK 4 CARBOXYPEPTIDASE WHICH CONTAINS ONE CHAIN. THUS THE 3SC2 46
REMARK 4 RESIDUE NUMBERING FOR CHAIN *B* BEGINS WITH 262. 3SC2 47
REMARK 5 3SC2 48
REMARK 5 THE SECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO KABSCH 3SC2 49
REMARK 5 AND SANDER (BIOPOLYMERS 22, 2577-2637, 1983) DSSP PROGRAM 3SC2 50
REMARK 5 EXCEPT FOR RESIDUES -1 TO 1 AND 102 TO 105. BOTH STRANDS 3SC2 51
REMARK 5 ARE INVOLVED IN THE HYDROGEN BONDING OF A BETA SHEET, BUT 3SC2 52
REMARK 5 NEITHER OF THEM IS ASSIGNED AS A BETA STRAND BY DSSP. 3SC2 53
REMARK 6 3SC2 54
REMARK 6 SOME OF THE SIDE CHAINS ARE DISORDERED AND HAVE NO 3SC2 55
REMARK 6 ELECTRON DENSITY. THESE SIDE CHAINS ARE MODELED WITH ZERO 3SC2 56
REMARK 6 OCCUPANCY ASSIGNED TO ALL OR PART OF THE SIDE CHAIN ATOMS. 3SC2 57
SEQRES 1 A 259 VAL GLU PRO SER GLY HIS ALA ALA ASP ARG ILE ALA ARG 3SC2 58
SEQRES 2 A 259 LEU PRO GLY GLN PRO ALA VAL ASP PHE ASP MET TYR SER 3SC2 59
SEQRES 3 A 259 GLY TYR ILE THR VAL ASP GLU GLY ALA GLY ARG SER LEU 3SC2 60
SEQRES 4 A 259 PHE TYR LEU LEU GLN GLU ALA PRO GLU ASP ALA GLN PRO 3SC2 61
SEQRES 5 A 259 ALA PRO LEU VAL LEU TRP LEU ASN GLY GLY PRO GLY CYS 3SC2 62
SEQRES 6 A 259 SER SER VAL ALA TYR GLY ALA SER GLU GLU LEU GLY ALA 3SC2 63
SEQRES 7 A 259 PHE ARG VAL LYS PRO ALA GLY ALA GLY LEU VAL LEU ASN 3SC2 64
SEQRES 8 A 259 GLU TYR ARG TRP ASN LYS VAL ALA ASN VAL LEU PHE LEU 3SC2 65
SEQRES 9 A 259 ASP SER PRO ALA GLY VAL GLY PHE SER TYR THR ASN THR 3SC2 66
SEQRES 10 A 259 SER SER ASP ILE TYR THR SER GLY ASP ASN ARG THR ALA 3SC2 67
SEQRES 11 A 259 HIS ASP SER TYR ALA PHE LEU ALA LYS TRP PHE GLU ARG 3SC2 68
SEQRES 12 A 259 PHE PRO HIS TYR LYS TYR ARG ASP PHE TYR ILE ALA GLY 3SC2 69
SEQRES 13 A 259 GLU SER TYR ALA GLY HIS TYR VAL PRO GLU LEU SER GLN 3SC2 70
SEQRES 14 A 259 LEU VAL HIS ARG SER LYS ASN PRO VAL ILE ASN LEU LYS 3SC2 71
SEQRES 15 A 259 GLY PHE MET VAL GLY ASN GLY LEU ILE ASP ASP TYR HIS 3SC2 72
SEQRES 16 A 259 ASP TYR VAL GLY THR PHE GLU PHE TRP TRP ASN HIS GLY 3SC2 73
SEQRES 17 A 259 ILE VAL SER ASP ASP THR TYR ARG ARG LEU LYS GLU ALA 3SC2 74
SEQRES 18 A 259 CYS LEU HIS ASP SER PHE ILE HIS PRO SER PRO ALA CYS 3SC2 75
SEQRES 19 A 259 ASP ALA ALA THR ASP VAL ALA THR ALA GLU GLN GLY ASN 3SC2 76
SEQRES 20 A 259 ILE ASP MET TYR SER LEU TYR THR PRO VAL CYS ASN 3SC2 77
SEQRES 1 B 152 SER TYR ASP PRO CYS THR GLU ARG TYR SER THR ALA TYR 3SC2 78
SEQRES 2 B 152 TYR ASN ARG ARG ASP VAL GLN MET ALA LEU HIS ALA ASN 3SC2 79
SEQRES 3 B 152 VAL THR GLY ALA MET ASN TYR THR TRP ALA THR CYS SER 3SC2 80
SEQRES 4 B 152 ASP THR ILE ASN THR HIS TRP HIS ASP ALA PRO ARG SER 3SC2 81
SEQRES 5 B 152 MET LEU PRO ILE TYR ARG GLU LEU ILE ALA ALA GLY LEU 3SC2 82
SEQRES 6 B 152 ARG ILE TRP VAL PHE SER GLY ASP THR ASP ALA VAL VAL 3SC2 83
SEQRES 7 B 152 PRO LEU THR ALA THR ARG TYR SER ILE GLY ALA LEU GLY 3SC2 84
SEQRES 8 B 152 LEU PRO THR THR THR SER TRP TYR PRO TRP TYR ASP ASP 3SC2 85
SEQRES 9 B 152 GLN GLU VAL GLY GLY TRP SER GLN VAL TYR LYS GLY LEU 3SC2 86
SEQRES 10 B 152 THR LEU VAL SER VAL ARG GLY ALA GLY HIS GLU VAL PRO 3SC2 87
SEQRES 11 B 152 LEU HIS ARG PRO ARG GLN ALA LEU VAL LEU PHE GLN TYR 3SC2 88
SEQRES 12 B 152 PHE LEU GLN GLY LYS PRO MET PRO GLY 3SC2 89
FTNOTE 1 3SC2 90
FTNOTE 1 THERE IS NO APPARENT ELECTRON DENSITY FOR THE SIDE CHAINS 3SC2 91
FTNOTE 1 OF RESIDUES GLU A 24, LYS A 163, ARG B 282, THR B 293, AND 3SC2 92
FTNOTE 1 GLN B 375A. THE SIDE CHAINS ARE MODELLED WITH ZERO 3SC2 93
FTNOTE 1 OCCUPANCY. 3SC2 94
FTNOTE 2 3SC2 95
FTNOTE 2 RESIDUES PRO A 43, PRO A 54, AND PRO A 96 ARE CIS PROLINES. 3SC2 96
HET NAG 51 14 N-ACETYL-D-GLUCOSAMINE 3SC2 97
HET NAG 52 14 N-ACETYL-D-GLUCOSAMINE 3SC2 98
HET MAN 54 11 ALPHA-D-MANNOSE 3SC2 99
HET FUC 105A 10 FUCOSE 3SC2 100
HET NAG 131 14 N-ACETYL-D-GLUCOSAMINE 3SC2 101
HET NAG 132 14 N-ACETYL-D-GLUCOSAMINE 3SC2 102
HET MAN 133 11 ALPHA-D-MANNOSE 3SC2 103
HET FUC 136 10 FUCOSE 3SC2 104
HET NAG 911 14 N-ACETYL-D-GLUCOSAMINE 3SC2 105
HET NAG 912 14 N-ACETYL-D-GLUCOSAMINE 3SC2 106
FORMUL 3 NAG 6(C8 H15 N1 O6) 3SC2 107
FORMUL 4 MAN 2(C6 H12 O6) 3SC2 108
FORMUL 5 FUC 2(C6 H12 O6) 3SC2 109
FORMUL 6 HOH *197(H2 O1) 3SC2 110
HELIX 1 H1 PRO A 38 GLN A 42 5 3SC2 111
HELIX 2 H2 GLY A 61 GLU A 64 1 3SC2 112
HELIX 3 H3 ARG A 83 VAL A 87 5 3SC2 113
HELIX 4 H4 ASP A 112C ARG A 129 1 3SC2 114
HELIX 5 H5 ALA A 148 ARG A 161 1 3SC2 115
HELIX 6 H6 ASP A 181 ASN A 194 1 3SC2 116
HELIX 7 H7 ASP A 200 CYS A 210 1 3SC2 117
HELIX 8 H8 PRO A 220 GLN A 233 1 3SC2 118
HELIX 9 H9 THR B 271 TYR B 279 1 3SC2 119
HELIX 10 H10 ARG B 282 LEU B 288 1 3SC2 120
HELIX 11 H11 ASP B 303B THR B 307 1 3SC2 121
HELIX 12 H12 LEU B 314 ILE B 321 1 3SC2 122
HELIX 13 H13 LEU B 343 GLY B 351 1 3SC2 123
HELIX 14 H14 VAL B 399 HIS B 402 1 3SC2 124
HELIX 15 H15 PRO B 404 GLN B 416 1 3SC2 125
SHEET 1 S1 11 ASP A -1A ILE A 1 0 3SC2 126
SHEET 2 S1 11 MET A 16 ASP A 23A-1 3SC2 127
SHEET 3 S1 11 ARG A 28 LEU A 34 -1 3SC2 128
SHEET 4 S1 11 ALA A 88 PHE A 92 -1 3SC2 129
SHEET 5 S1 11 LEU A 46 LEU A 50 1 3SC2 130
SHEET 6 S1 11 ASP A 139 GLU A 145 1 3SC2 131
SHEET 7 S1 11 ASN A 168 GLY A 175 1 3SC2 132
SHEET 8 S1 11 ARG B 329 GLY B 335 1 3SC2 133
SHEET 9 S1 11 LEU B 387 VAL B 392 1 3SC2 134
SHEET 10 S1 11 GLU B 376 TYR B 384 -1 3SC2 135
SHEET 11 S1 11 THR B 366 TYR B 373 -1 3SC2 136
SHEET 1 S2 2 PHE A 69 VAL A 71 0 3SC2 137
SHEET 2 S2 2 LEU A 77 LEU A 79 -1 3SC2 138
SHEET 1 S3 1 SER A 102 ASN A 105 0 3SC2 139
TURN 1 T01 LEU A 4 GLN A 7 3SC2 140
TURN 2 T02 LYS A 72 GLY A 75 3SC2 141
TURN 3 T03 ASN A 80 ARG A 83 3SC2 142
TURN 4 T04 PRO A 96 VAL A 99 3SC2 143
TURN 5 T05 VAL A 99 SER A 102 3SC2 144
TURN 6 T06 SER A 108 TYR A 111 3SC2 145
TURN 7 T07 PRO A 131 LYS A 134 3SC2 146
TURN 8 T08 TYR A 133 ARG A 138 3SC2 147
TURN 9 T09 ASN A 164 ILE A 167 3SC2 148
TURN 10 T10 CYS A 210 ASP A 213 3SC2 149
TURN 11 T11 ASP A 237 SER A 240 3SC2 150
TURN 12 T12 MET B 286 HIS B 289 3SC2 151
TURN 13 T13 ASN B 291 GLY B 294 3SC2 152
TURN 14 T14 GLY B 335 ASP B 338 3SC2 153
TURN 15 T15 ASP B 374 GLU B 376 3SC2 154
TURN 16 T16 TYR B 384 LEU B 387 3SC2 155
TURN 17 T17 VAL B 392 ALA B 395 3SC2 156
SSBOND 1 CYS A 56 CYS B 303 3SC2 157
SSBOND 2 CYS A 210 CYS A 222 3SC2 158
SSBOND 3 CYS A 246 CYS B 268 3SC2 159
CRYST1 98.400 98.400 209.500 90.00 90.00 90.00 P 41 21 2 8 3SC2 160
ORIGX1 1.000000 0.000000 0.000000 0.00000 3SC2 161
ORIGX2 0.000000 1.000000 0.000000 0.00000 3SC2 162
ORIGX3 0.000000 0.000000 1.000000 0.00000 3SC2 163
SCALE1 0.010163 0.000000 0.000000 0.00000 3SC2 164
SCALE2 0.000000 0.010163 0.000000 0.00000 3SC2 165
SCALE3 0.000000 0.000000 0.004773 0.00000 3SC2 166 |