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HEADER SERINE CARBOXYPEPTIDASE 07-MAR-94 1WHS 1WHS 2
COMPND SERINE CARBOXYPEPTIDASE II (E.C.3.4.16.1) (NATIVE FORM) 1WHS 3
SOURCE WHEAT (TRITICUM VULGARIS) GERM 1WHS 4
AUTHOR T.L.BULLOCK,S.J.REMINGTON 1WHS 5
REVDAT 1 22-JUN-94 1WHS 0 1WHS 6
JRNL AUTH T.L.BULLOCK,S.J.REMINGTON 1WHS 7
JRNL TITL STRUCTURE OF THE COMPLEX OF L-BENZYLSUCCINATE WITH 1WHS 8
JRNL TITL 2 WHEAT SERINE CARBOXYPEPTIDASE II AT 2.0 ANGSTROMS 1WHS 9
JRNL TITL 3 RESOLUTION 1WHS 10
JRNL REF TO BE PUBLISHED REF NOW ASSIGNED AS 1WHS 11
JRNL REFN 0353 1WHS 12
REMARK 1 1WHS 13
REMARK 1 REFERENCE 1 1WHS 14
REMARK 1 AUTH D.-I.LIAO,S.J.REMINGTON 1WHS 15
REMARK 1 TITL STRUCTURE OF WHEAT SERINE CARBOXYPEPTIDASE II AT 1WHS 16
REMARK 1 TITL 2 3.5 ANGSTROMS RESOLUTION 1WHS 17
REMARK 1 REF J.BIOL.CHEM. V. 265 6528 1990 1WHS 18
REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 0071 1WHS 19
REMARK 1 REFERENCE 2 1WHS 20
REMARK 1 AUTH K.P.WILSON,D.-I.LIAO,T.BULLOCK,S.J.REMINGTON, 1WHS 21
REMARK 1 AUTH 2 K.BREDDAM 1WHS 22
REMARK 1 TITL CRYSTALLIZATION OF SERINE CARBOXYPEPTIDASES 1WHS 23
REMARK 1 REF J.MOL.BIOL. V. 211 301 1990 1WHS 24
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1WHS 25
REMARK 1 REFERENCE 3 1WHS 26
REMARK 1 AUTH K.BREDDAM,S.B.SORENSEN,I.SVENDSEN 1WHS 27
REMARK 1 TITL PRIMARY STRUCTURE AND ENZYMATIC PROPERTIES OF 1WHS 28
REMARK 1 TITL 2 CARBOXYPEPTIDASE II FROM WHEAT BRAN 1WHS 29
REMARK 1 REF CARLSBERG RES.COMMUN. V. 52 297 1987 1WHS 30
REMARK 1 REFN ASTM CRCODS DK ISSN 0105-1938 0915 1WHS 31
REMARK 2 1WHS 32
REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 1WHS 33
REMARK 3 1WHS 34
REMARK 3 REFINEMENT. 1WHS 35
REMARK 3 PROGRAM TNT 1WHS 36
REMARK 3 AUTHORS TRONRUD,TEN EYCK,MATTHEWS 1WHS 37
REMARK 3 R VALUE 0.175 1WHS 38
REMARK 3 RMSD BOND DISTANCES 0.012 ANGSTROMS 1WHS 39
REMARK 3 RMSD BOND ANGLES 2.3 DEGREES 1WHS 40
REMARK 3 1WHS 41
REMARK 3 NUMBER OF REFLECTIONS 29338 1WHS 42
REMARK 3 RESOLUTION RANGE 20.0 - 2.0 ANGSTROMS 1WHS 43
REMARK 3 PERCENT COMPLETION 72. 1WHS 44
REMARK 3 1WHS 45
REMARK 3 NUMBER OF PROTEIN ATOMS 3206 1WHS 46
REMARK 3 NUMBER OF SOLVENT ATOMS 383 1WHS 47
REMARK 3 1WHS 48
REMARK 3 RESTRAINED B = 4.3 ANGSTROMS**2. 1WHS 49
REMARK 4 1WHS 50
REMARK 4 THE NATIVE FORM WAS SOLVED AT -170 DEGREES CELSIUS 1WHS 51
REMARK 5 1WHS 52
REMARK 5 RESIDUES GLU 24, ARG 74, LYS 163 OF CHAIN *A* AND ARG 282, 1WHS 53
REMARK 5 ASP 375, AND GLN 375A OF CHAIN *B* HAVE INCOMPLETE SIDE 1WHS 54
REMARK 5 CHAIN ATOMS. 1WHS 55
REMARK 6 1WHS 56
REMARK 6 PDB ADVISORY NOTICE: 1WHS 57
REMARK 6 THERE ARE A FEW WATER MOLECULES WHICH MAY BE ASSOCIATED 1WHS 58
REMARK 6 WITH SYMMETRY-RELATED PROTEIN MOLECULES. 1WHS 59
SEQRES 1 A 255 HIS ALA ALA ASP ARG ILE ALA ARG LEU PRO GLY GLN PRO 1WHS 60
SEQRES 2 A 255 ALA VAL ASP PHE ASP MET TYR SER GLY TYR ILE THR VAL 1WHS 61
SEQRES 3 A 255 ASP GLU GLY ALA GLY ARG SER LEU PHE TYR LEU LEU GLN 1WHS 62
SEQRES 4 A 255 GLU ALA PRO GLU ASP ALA GLN PRO ALA PRO LEU VAL LEU 1WHS 63
SEQRES 5 A 255 TRP LEU ASN GLY GLY PRO GLY CYS SER SER VAL ALA TYR 1WHS 64
SEQRES 6 A 255 GLY ALA SER GLU GLU LEU GLY ALA PHE ARG VAL LYS PRO 1WHS 65
SEQRES 7 A 255 ARG GLY ALA GLY LEU VAL LEU ASN GLU TYR ARG TRP ASN 1WHS 66
SEQRES 8 A 255 LYS VAL ALA ASN VAL LEU PHE LEU ASP SER PRO ALA GLY 1WHS 67
SEQRES 9 A 255 VAL GLY PHE SER TYR THR ASN THR SER SER ASP ILE TYR 1WHS 68
SEQRES 10 A 255 THR SER GLY ASP ASN ARG THR ALA HIS ASP SER TYR ALA 1WHS 69
SEQRES 11 A 255 PHE LEU ALA LYS TRP PHE GLU ARG PHE PRO HIS TYR LYS 1WHS 70
SEQRES 12 A 255 TYR ARG ASP PHE TYR ILE ALA GLY GLU SER TYR ALA GLY 1WHS 71
SEQRES 13 A 255 HIS TYR VAL PRO GLU LEU SER GLN LEU VAL HIS ARG SER 1WHS 72
SEQRES 14 A 255 LYS ASN PRO VAL ILE ASN LEU LYS GLY PHE MET VAL GLY 1WHS 73
SEQRES 15 A 255 ASN GLY LEU ILE ASP ASP TYR HIS ASP TYR VAL GLY THR 1WHS 74
SEQRES 16 A 255 PHE GLU PHE TRP TRP ASN HIS GLY ILE VAL SER ASP ASP 1WHS 75
SEQRES 17 A 255 THR TYR ARG ARG LEU LYS GLU ALA CYS LEU HIS ASP SER 1WHS 76
SEQRES 18 A 255 PHE ILE HIS PRO SER PRO ALA CYS ASP ALA ALA THR ASP 1WHS 77
SEQRES 19 A 255 VAL ALA THR ALA GLU GLN GLY ASN ILE ASP MET TYR SER 1WHS 78
SEQRES 20 A 255 LEU TYR THR PRO VAL CYS ASN ILE 1WHS 79
SEQRES 1 B 153 SER TYR ASP PRO CYS THR GLU ARG TYR SER THR ALA TYR 1WHS 80
SEQRES 2 B 153 TYR ASN ARG ARG ASP VAL GLN MET ALA LEU HIS ALA ASN 1WHS 81
SEQRES 3 B 153 VAL THR GLY ALA MET ASN TYR THR TRP ALA THR CYS SER 1WHS 82
SEQRES 4 B 153 ASP THR ILE ASN THR HIS TRP HIS ASP ALA PRO ARG SER 1WHS 83
SEQRES 5 B 153 MET LEU PRO ILE TYR ARG GLU LEU ILE ALA ALA GLY LEU 1WHS 84
SEQRES 6 B 153 ARG ILE TRP VAL PHE SER GLY ASP THR ASP ALA VAL VAL 1WHS 85
SEQRES 7 B 153 PRO LEU THR ALA THR ARG TYR SER ILE GLY ALA LEU GLY 1WHS 86
SEQRES 8 B 153 LEU PRO THR THR THR SER TRP TYR PRO TRP TYR ASP ASP 1WHS 87
SEQRES 9 B 153 GLN GLU VAL GLY GLY TRP SER GLN VAL TYR LYS GLY LEU 1WHS 88
SEQRES 10 B 153 THR LEU VAL SER VAL ARG GLY ALA GLY HIS GLU VAL PRO 1WHS 89
SEQRES 11 B 153 LEU HIS ARG PRO ARG GLN ALA LEU VAL LEU PHE GLN TYR 1WHS 90
SEQRES 12 B 153 PHE LEU GLN GLY LYS PRO MET PRO GLY GLN 1WHS 91
FTNOTE 1 1WHS 92
FTNOTE 1 CIS PROLINE - PRO A 43 1WHS 93
FTNOTE 2 1WHS 94
FTNOTE 2 CIS PROLINE - PRO A 54 1WHS 95
FTNOTE 3 1WHS 96
FTNOTE 3 CIS PROLINE - PRO A 96 1WHS 97
HET GOL 450 6 GLYCEROL 1WHS 98
HET ACY 460 4 ACETIC ACID 1WHS 99
HET ACY 461 4 ACETIC ACID 1WHS 100
HET NAG 1131 14 N-ACETYL-D-GLUCOSAMINE 1WHS 101
HET FUC 105 10 FUCOSE 1WHS 102
HET NAG 1051 14 N-ACETYL-D-GLUCOSAMINE 1WHS 103
HET NAG 1052 14 N-ACETYL-D-GLUCOSAMINE 1WHS 104
HET NAG 2911 14 N-ACETYL-D-GLUCOSAMINE 1WHS 105
HET NAG 2912 14 N-ACETYL-D-GLUCOSAMINE 1WHS 106
FORMUL 3 GOL C3 H8 O3 1WHS 107
FORMUL 4 ACY 2(C2 H4 O2 ) 1WHS 108
FORMUL 5 NAG 5(C8 H15 N1 O6) 1WHS 109
FORMUL 6 FUC C6 H12 O6 1WHS 110
FORMUL 7 HOH *383(H2 O1) 1WHS 111
HELIX 1 H1 PRO A 38 GLN A 42 5 1WHS 112
HELIX 2 H2 GLY A 61 GLU A 64 1 1WHS 113
HELIX 3 H3 ARG A 83 VAL A 87 5 1WHS 114
HELIX 4 H4 ASP A 112C ARG A 129 1 1WHS 115
HELIX 5 H5 ALA A 148 ARG A 161 1 1WHS 116
HELIX 6 H6 ASP A 181 ASN A 194 1 1WHS 117
HELIX 7 H7 ASP A 200 CYS A 210 1 1WHS 118
HELIX 8 H8 PRO A 220 GLN A 233 1 1WHS 119
HELIX 9 H9 THR B 271 TYR B 279 1 1WHS 120
HELIX 10 H10 ARG B 282 LEU B 288 1 1WHS 121
HELIX 11 H11 ASP B 303B THR B 307 1 1WHS 122
HELIX 12 H12 LEU B 314 ILE B 321 1 1WHS 123
HELIX 13 H13 LEU B 343 GLY B 351 1 1WHS 124
HELIX 14 H14 VAL B 399 HIS B 402 1 1WHS 125
HELIX 15 H15 PRO B 404 GLN B 416 1 1WHS 126
SHEET 1 S1 11 ASP A -1 ILE A 1 0 1WHS 127
SHEET 2 S1 11 MET A 16 ASP A 23A-1 1WHS 128
SHEET 3 S1 11 ARG A 28 LEU A 34 -1 1WHS 129
SHEET 4 S1 11 ALA A 88 PHE A 92 -1 1WHS 130
SHEET 5 S1 11 LEU A 46 LEU A 50 1 1WHS 131
SHEET 6 S1 11 ASP A 139 GLU A 145 1 1WHS 132
SHEET 7 S1 11 ASN A 168 GLY A 175 1 1WHS 133
SHEET 8 S1 11 ARG B 329 GLY B 335 1 1WHS 134
SHEET 9 S1 11 LEU B 387 VAL B 392 1 1WHS 135
SHEET 10 S1 11 GLU B 376 TYR B 384 -1 1WHS 136
SHEET 11 S1 11 THR B 366 TYR B 373 -1 1WHS 137
SHEET 1 S2 2 PHE A 69 VAL A 71 0 1WHS 138
SHEET 2 S2 2 LEU A 77 LEU A 79 -1 1WHS 139
SHEET 1 S3 1 SER A 102 ASN A 105 0 1WHS 140
TURN 1 T01 LEU A 4 GLN A 7 1WHS 141
TURN 2 T02 LYS A 72 GLY A 75 1WHS 142
TURN 3 T03 ASN A 80 ARG A 83 1WHS 143
TURN 4 T04 PRO A 96 VAL A 99 1WHS 144
TURN 5 T05 VAL A 99 SER A 102 1WHS 145
TURN 6 T06 SER A 108 TYR A 111 1WHS 146
TURN 7 T07 PRO A 131 LYS A 134 1WHS 147
TURN 8 T08 TYR A 133 ARG A 138 1WHS 148
TURN 9 T09 ASN A 164 ILE A 167 1WHS 149
TURN 10 T10 CYS A 210 ASP A 213 1WHS 150
TURN 11 T11 ASP A 237 SER A 240 1WHS 151
TURN 12 T12 MET B 286 HIS B 289 1WHS 152
TURN 13 T13 ASN B 291 GLY B 294 1WHS 153
TURN 14 T14 GLY B 335 ASP B 338 1WHS 154
TURN 15 T15 ASP B 374 GLU B 376 1WHS 155
TURN 16 T16 TYR B 384 LEU B 387 1WHS 156
TURN 17 T17 VAL B 392 ALA B 395 1WHS 157
SSBOND 1 CYS A 56 CYS B 303 1WHS 158
SSBOND 2 CYS A 210 CYS A 222 1WHS 159
SSBOND 3 CYS A 246 CYS B 268 1WHS 160
SITE 1 ACT 4 ASP B 338 HIS B 397 SER A 146 GLU A 145 1WHS 161
CRYST1 95.600 95.600 208.800 90.00 90.00 90.00 P 41 21 2 8 1WHS 162
ORIGX1 1.000000 0.000000 0.000000 0.00000 1WHS 163
ORIGX2 0.000000 1.000000 0.000000 0.00000 1WHS 164
ORIGX3 0.000000 0.000000 1.000000 0.00000 1WHS 165
SCALE1 0.010460 0.000000 0.000000 0.00000 1WHS 166
SCALE2 0.000000 0.010460 0.000000 0.00000 1WHS 167
SCALE3 0.000000 0.000000 0.004789 0.00000 1WHS 168 |