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HEADER HYDROLASE(CARBOXYLIC ESTERASE) 21-DEC-93 1TAH 1TAH 2
COMPND LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE) 1TAH 3
SOURCE (PSEUDOMONAS GLUMAE), ALSO KNOWN AS (PSEUDOMONAS GLADIOLI) 1TAH 4
AUTHOR M.E.M.NOBLE,A.CLEASBY,L.N.JOHNSON,M.EGMOND,L.G.J.FRENKEN 1TAH 5
REVDAT 1 31-MAY-94 1TAH 0 1TAH 6
JRNL AUTH M.E.M.NOBLE,A.CLEASBY,L.N.JOHNSON,M.R.EGMOND, 1TAH 7
JRNL AUTH 2 L.G.J.FRENKEN 1TAH 8
JRNL TITL THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE 1TAH 9
JRNL TITL 2 FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY 1TAH 10
JRNL TITL 3 REDUNDANT CATALYTIC ASPARTATE 1TAH 11
JRNL REF /FEBS$ LETT. V. 331 123 1993 1TAH 12
JRNL REFN ASTM FEBLAL NE ISSN 0014-5793 0165 1TAH 13
REMARK 1 1TAH 14
REMARK 1 REFERENCE 1 1TAH 15
REMARK 1 AUTH A.CLEASBY,E.GARMAN,M.R.EGMOND,M.BATENBURG 1TAH 16
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY STUDY OF A 1TAH 17
REMARK 1 TITL 2 LIPASE FROM PSEUDOMONAS GLUMAE 1TAH 18
REMARK 1 REF J.MOL.BIOL. V. 224 281 1992 1TAH 19
REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1TAH 20
REMARK 2 1TAH 21
REMARK 2 RESOLUTION. 3.0 ANGSTROMS. 1TAH 22
REMARK 3 1TAH 23
REMARK 3 REFINEMENT. 1TAH 24
REMARK 3 PROGRAM X-PLOR 1TAH 25
REMARK 3 AUTHORS BRUNGER 1TAH 26
REMARK 3 R VALUE 0.159 1TAH 27
REMARK 3 FREE R VALUE 0.226 1TAH 28
REMARK 3 RMSD BOND DISTANCES 0.01 ANGSTROMS 1TAH 29
REMARK 3 RMSD BOND ANGLES 2.5 DEGREES 1TAH 30
REMARK 3 1TAH 31
REMARK 3 NUMBER OF REFLECTIONS 21736 1TAH 32
REMARK 3 RESOLUTION RANGE 6.0 - 3.0 ANGSTROMS 1TAH 33
REMARK 3 1TAH 34
REMARK 3 THE STRUCTURE WAS INITIALLY REFINED WITH STRICT 1TAH 35
REMARK 3 NON-CRYSTALLOGRAPHIC SYMMETRY, AND THEN WITH TIGHTLY 1TAH 36
REMARK 3 RESTRAINED NON-CRYSTALLOGRAPHIC SYMMETRY FOR ALL PARTS OF 1TAH 37
REMARK 3 THE MOLECULE EXCEPT RESIDUES 18 - 29, 132 - 135, 1TAH 38
REMARK 3 150 - 160, 216 - 225, 232 - 236, 67, AND 102. 1TAH 39
REMARK 4 1TAH 40
REMARK 4 FOUR CRYSTALLOGRAPHICALLY INDEPENDENT MOLECULES PER 1TAH 41
REMARK 4 ASYMMETRIC UNIT TIMES FOUR GENERAL EQUIVALENT POSITIONS 1TAH 42
REMARK 4 GIVE SIXTEEN COVALENTLY IDENTICAL SUBUNITS IN THE UNIT 1TAH 43
REMARK 4 CELL. THE CHAINS ARE NAMED A TO D, WITH MOLECULE B AS THE 1TAH 44
REMARK 4 REFERENCE USED FOR SECONDARY STRUCTURE DEFINITION. 1TAH 45
REMARK 4 THE NON-CRYSTALLOGRAPHIC TRANSFORMATIONS PRESENTED ON 1TAH 46
REMARK 4 *MTRIX 1*, *MTRIX 2*, AND *MTRIX 3* RECORDS BELOW WILL 1TAH 47
REMARK 4 YIELD APPROXIMATE COORDINATES FOR CHAINS A, C, AND D, 1TAH 48
REMARK 4 RESPECTIVELY, WHEN APPLIED TO CHAIN B. DEVIATIONS FROM 1TAH 49
REMARK 4 NON-CRYSTALLOGRAPHIC SYMMETRY CORRESPOND TO THOSE PARTS OF 1TAH 50
REMARK 4 THE PROTEIN EXCLUDED FROM THE NCS-RESTRAINT. 1TAH 51
REMARK 5 1TAH 52
REMARK 5 THE ACTIVE SITE (SITES ACB, ACA, ACC, ACD BELOW) PROBABLY 1TAH 53
REMARK 5 CORRESPONDS TO THE TRIAD: SER 87 - HIS 285 - ASP 263, 1TAH 54
REMARK 5 ALTHOUGH THEY ARE BURIED IN THIS STRUCTURE. ASP 263 IS 1TAH 55
REMARK 5 INVOLVED IN A HYDROGEN BOND WITH GLU 288, DESPITE THE HIGH 1TAH 56
REMARK 5 PH (9) OF THE CRYSTALLIZATION MEDIUM. 1TAH 57
REMARK 6 1TAH 58
REMARK 6 THE ENZYME ALSO HAS A CALCIUM SITE (SITES CAB, CAA, CAC, 1TAH 59
REMARK 6 CAD BELOW) NEAR TO THE ACTIVE SITE, DEDUCED FROM THE 1TAH 60
REMARK 6 ELECTRON DENSITY. 1TAH 61
REMARK 7 1TAH 62
REMARK 7 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN 1TAH 63
REMARK 7 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, 1TAH 64
REMARK 7 TWO SHEETS ARE DEFINED. STRANDS 2, 3, 4, 5 OF 1A AND 1B 1TAH 65
REMARK 7 ARE IDENTICAL. 1TAH 66
REMARK 8 1TAH 67
REMARK 8 CROSS REFERENCE TO SEQUENCE DATABASE 1TAH 68
REMARK 8 PIR ENTRY NAME PDB ENTRY CHAIN NAME 1TAH 69
REMARK 8 PGLIP B 1TAH 70
REMARK 8 PGLIP A 1TAH 71
REMARK 8 PGLIP C 1TAH 72
REMARK 8 PGLIP D 1TAH 73
SEQRES 1 B 318 ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU VAL 1TAH 74
SEQRES 2 B 318 HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL VAL 1TAH 75
SEQRES 3 B 318 ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER HIS 1TAH 76
SEQRES 4 B 318 GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE GLN 1TAH 77
SEQRES 5 B 318 SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU LEU 1TAH 78
SEQRES 6 B 318 ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA THR 1TAH 79
SEQRES 7 B 318 LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU THR 1TAH 80
SEQRES 8 B 318 SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL ALA 1TAH 81
SEQRES 9 B 318 SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER GLU 1TAH 82
SEQRES 10 B 318 PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP PRO 1TAH 83
SEQRES 11 B 318 THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL ASN 1TAH 84
SEQRES 12 B 318 VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR ASP 1TAH 85
SEQRES 13 B 318 GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR ALA 1TAH 86
SEQRES 14 B 318 GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA GLY 1TAH 87
SEQRES 15 B 318 LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA THR 1TAH 88
SEQRES 16 B 318 GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER TRP 1TAH 89
SEQRES 17 B 318 GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU GLY 1TAH 90
SEQRES 18 B 318 VAL THR GLY ALA THR ASP THR SER THR GLY THR LEU ASP 1TAH 91
SEQRES 19 B 318 VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU LEU 1TAH 92
SEQRES 20 B 318 ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY GLN 1TAH 93
SEQRES 21 B 318 ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE GLY 1TAH 94
SEQRES 22 B 318 GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU ASP 1TAH 95
SEQRES 23 B 318 GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN ALA 1TAH 96
SEQRES 24 B 318 GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN ARG 1TAH 97
SEQRES 25 B 318 LEU LYS LEU GLN GLY VAL 1TAH 98
SEQRES 1 A 318 ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU VAL 1TAH 99
SEQRES 2 A 318 HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL VAL 1TAH 100
SEQRES 3 A 318 ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER HIS 1TAH 101
SEQRES 4 A 318 GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE GLN 1TAH 102
SEQRES 5 A 318 SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU LEU 1TAH 103
SEQRES 6 A 318 ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA THR 1TAH 104
SEQRES 7 A 318 LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU THR 1TAH 105
SEQRES 8 A 318 SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL ALA 1TAH 106
SEQRES 9 A 318 SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER GLU 1TAH 107
SEQRES 10 A 318 PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP PRO 1TAH 108
SEQRES 11 A 318 THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL ASN 1TAH 109
SEQRES 12 A 318 VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR ASP 1TAH 110
SEQRES 13 A 318 GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR ALA 1TAH 111
SEQRES 14 A 318 GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA GLY 1TAH 112
SEQRES 15 A 318 LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA THR 1TAH 113
SEQRES 16 A 318 GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER TRP 1TAH 114
SEQRES 17 A 318 GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU GLY 1TAH 115
SEQRES 18 A 318 VAL THR GLY ALA THR ASP THR SER THR GLY THR LEU ASP 1TAH 116
SEQRES 19 A 318 VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU LEU 1TAH 117
SEQRES 20 A 318 ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY GLN 1TAH 118
SEQRES 21 A 318 ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE GLY 1TAH 119
SEQRES 22 A 318 GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU ASP 1TAH 120
SEQRES 23 A 318 GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN ALA 1TAH 121
SEQRES 24 A 318 GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN ARG 1TAH 122
SEQRES 25 A 318 LEU LYS LEU GLN GLY VAL 1TAH 123
SEQRES 1 C 318 ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU VAL 1TAH 124
SEQRES 2 C 318 HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL VAL 1TAH 125
SEQRES 3 C 318 ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER HIS 1TAH 126
SEQRES 4 C 318 GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE GLN 1TAH 127
SEQRES 5 C 318 SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU LEU 1TAH 128
SEQRES 6 C 318 ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA THR 1TAH 129
SEQRES 7 C 318 LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU THR 1TAH 130
SEQRES 8 C 318 SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL ALA 1TAH 131
SEQRES 9 C 318 SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER GLU 1TAH 132
SEQRES 10 C 318 PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP PRO 1TAH 133
SEQRES 11 C 318 THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL ASN 1TAH 134
SEQRES 12 C 318 VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR ASP 1TAH 135
SEQRES 13 C 318 GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR ALA 1TAH 136
SEQRES 14 C 318 GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA GLY 1TAH 137
SEQRES 15 C 318 LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA THR 1TAH 138
SEQRES 16 C 318 GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER TRP 1TAH 139
SEQRES 17 C 318 GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU GLY 1TAH 140
SEQRES 18 C 318 VAL THR GLY ALA THR ASP THR SER THR GLY THR LEU ASP 1TAH 141
SEQRES 19 C 318 VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU LEU 1TAH 142
SEQRES 20 C 318 ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY GLN 1TAH 143
SEQRES 21 C 318 ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE GLY 1TAH 144
SEQRES 22 C 318 GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU ASP 1TAH 145
SEQRES 23 C 318 GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN ALA 1TAH 146
SEQRES 24 C 318 GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN ARG 1TAH 147
SEQRES 25 C 318 LEU LYS LEU GLN GLY VAL 1TAH 148
SEQRES 1 D 318 ASP THR TYR ALA ALA THR ARG TYR PRO VAL ILE LEU VAL 1TAH 149
SEQRES 2 D 318 HIS GLY LEU ALA GLY THR ASP LYS PHE ALA ASN VAL VAL 1TAH 150
SEQRES 3 D 318 ASP TYR TRP TYR GLY ILE GLN SER ASP LEU GLN SER HIS 1TAH 151
SEQRES 4 D 318 GLY ALA LYS VAL TYR VAL ALA ASN LEU SER GLY PHE GLN 1TAH 152
SEQRES 5 D 318 SER ASP ASP GLY PRO ASN GLY ARG GLY GLU GLN LEU LEU 1TAH 153
SEQRES 6 D 318 ALA TYR VAL LYS GLN VAL LEU ALA ALA THR GLY ALA THR 1TAH 154
SEQRES 7 D 318 LYS VAL ASN LEU ILE GLY HIS SER GLN GLY GLY LEU THR 1TAH 155
SEQRES 8 D 318 SER ARG TYR VAL ALA ALA VAL ALA PRO GLN LEU VAL ALA 1TAH 156
SEQRES 9 D 318 SER VAL THR THR ILE GLY THR PRO HIS ARG GLY SER GLU 1TAH 157
SEQRES 10 D 318 PHE ALA ASP PHE VAL GLN ASP VAL LEU LYS THR ASP PRO 1TAH 158
SEQRES 11 D 318 THR GLY LEU SER SER THR VAL ILE ALA ALA PHE VAL ASN 1TAH 159
SEQRES 12 D 318 VAL PHE GLY THR LEU VAL SER SER SER HIS ASN THR ASP 1TAH 160
SEQRES 13 D 318 GLN ASP ALA LEU ALA ALA LEU ARG THR LEU THR THR ALA 1TAH 161
SEQRES 14 D 318 GLN THR ALA THR TYR ASN ARG ASN PHE PRO SER ALA GLY 1TAH 162
SEQRES 15 D 318 LEU GLY ALA PRO GLY SER CYS GLN THR GLY ALA ALA THR 1TAH 163
SEQRES 16 D 318 GLU THR VAL GLY GLY SER GLN HIS LEU LEU TYR SER TRP 1TAH 164
SEQRES 17 D 318 GLY GLY THR ALA ILE GLN PRO THR SER THR VAL LEU GLY 1TAH 165
SEQRES 18 D 318 VAL THR GLY ALA THR ASP THR SER THR GLY THR LEU ASP 1TAH 166
SEQRES 19 D 318 VAL ALA ASN VAL THR ASP PRO SER THR LEU ALA LEU LEU 1TAH 167
SEQRES 20 D 318 ALA THR GLY ALA VAL MET ILE ASN ARG ALA SER GLY GLN 1TAH 168
SEQRES 21 D 318 ASN ASP GLY LEU VAL SER ARG CYS SER SER LEU PHE GLY 1TAH 169
SEQRES 22 D 318 GLN VAL ILE SER THR SER TYR HIS TRP ASN HIS LEU ASP 1TAH 170
SEQRES 23 D 318 GLU ILE ASN GLN LEU LEU GLY VAL ARG GLY ALA ASN ALA 1TAH 171
SEQRES 24 D 318 GLU ASP PRO VAL ALA VAL ILE ARG THR HIS VAL ASN ARG 1TAH 172
SEQRES 25 D 318 LEU LYS LEU GLN GLY VAL 1TAH 173
HET CA B 320 1 CALCIUM +2 COUNTER ION 1TAH 174
HET CA A 320 1 CALCIUM +2 COUNTER ION 1TAH 175
HET CA C 320 1 CALCIUM +2 COUNTER ION 1TAH 176
HET CA D 320 1 CALCIUM +2 COUNTER ION 1TAH 177
FORMUL 5 CA 4(CA1) 1TAH 178
HELIX 1 B1 ILE B 33 SER B 39 1 1TAH 179
HELIX 2 B2 ARG B 61 THR B 76 1 1TAH 180
HELIX 3 B3 GLN B 88 VAL B 99 1 PART OF A NUCLEOPHILE ELBOW 1TAH 181
HELIX 4 BA PRO B 101 LEU B 103 5 1TAH 182
HELIX 5 B4 GLU B 118 THR B 129 1 1TAH 183
HELIX 6 B5 THR B 137 LEU B 149 1 1TAH 184
HELIX 7 B6 ASP B 157 ARG B 165 1 1TAH 185
HELIX 8 B7 THR B 169 ASN B 178 1 1TAH 186
HELIX 9 B8 ALA B 237 THR B 240 1 1TAH 187
HELIX 10 B9 SER B 243 ILE B 255 1 1TAH 188
HELIX 11 B10 ARG B 268 SER B 271 1 1TAH 189
HELIX 12 BB ASP B 287 ILE B 289 5 1TAH 190
HELIX 13 A1 ILE A 33 SER A 39 1 1TAH 191
HELIX 14 A2 ARG A 61 THR A 76 1 1TAH 192
HELIX 15 A3 GLN A 88 VAL A 99 1 PART OF A NUCLEOPHILE ELBOW 1TAH 193
HELIX 16 AA PRO A 101 LEU A 103 5 1TAH 194
HELIX 17 A4 GLU A 118 THR A 129 1 1TAH 195
HELIX 18 A5 THR A 137 LEU A 149 1 1TAH 196
HELIX 19 A6 ASP A 157 ARG A 165 1 1TAH 197
HELIX 20 A7 THR A 169 ASN A 178 1 1TAH 198
HELIX 21 A8 ALA A 237 THR A 240 1 1TAH 199
HELIX 22 A9 SER A 243 ILE A 255 1 1TAH 200
HELIX 23 A10 ARG A 268 SER A 271 1 1TAH 201
HELIX 24 AB ASP A 287 ILE A 289 5 1TAH 202
HELIX 25 C1 ILE C 33 SER C 39 1 1TAH 203
HELIX 26 C2 ARG C 61 THR C 76 1 1TAH 204
HELIX 27 C3 GLN C 88 VAL C 99 1 PART OF A NUCLEOPHILE ELBOW 1TAH 205
HELIX 28 CA PRO C 101 LEU C 103 5 1TAH 206
HELIX 29 C4 GLU C 118 THR C 129 1 1TAH 207
HELIX 30 C5 THR C 137 LEU C 149 1 1TAH 208
HELIX 31 C6 ASP C 157 ARG C 165 1 1TAH 209
HELIX 32 C7 THR C 169 ASN C 178 1 1TAH 210
HELIX 33 C8 ALA C 237 THR C 240 1 1TAH 211
HELIX 34 C9 SER C 243 ILE C 255 1 1TAH 212
HELIX 35 C10 ARG C 268 SER C 271 1 1TAH 213
HELIX 36 CB ASP C 287 ILE C 289 5 1TAH 214
HELIX 37 D1 ILE D 33 SER D 39 1 1TAH 215
HELIX 38 D2 ARG D 61 THR D 76 1 1TAH 216
HELIX 39 D3 GLN D 88 VAL D 99 1 PART OF A NUCLEOPHILE ELBOW 1TAH 217
HELIX 40 DA PRO D 101 LEU D 103 5 1TAH 218
HELIX 41 D4 GLU D 118 THR D 129 1 1TAH 219
HELIX 42 D5 THR D 137 LEU D 149 1 1TAH 220
HELIX 43 D6 ASP D 157 ARG D 165 1 1TAH 221
HELIX 44 D7 THR D 169 ASN D 178 1 1TAH 222
HELIX 45 D8 ALA D 237 THR D 240 1 1TAH 223
HELIX 46 D9 SER D 243 ILE D 255 1 1TAH 224
HELIX 47 D10 ARG D 268 SER D 271 1 1TAH 225
HELIX 48 DB ASP D 287 ILE D 289 5 1TAH 226
SHEET 1 B1A 6 VAL B 44 ALA B 47 0 1TAH 227
SHEET 2 B1A 6 VAL B 11 VAL B 14 1 N LEU B 13 O TYR B 45 1TAH 228
SHEET 3 B1A 6 VAL B 81 HIS B 86 1 O ILE B 84 N VAL B 14 1TAH 229
SHEET 4 B1A 6 VAL B 104 ILE B 110 1 N ALA B 105 O VAL B 81 1TAH 230
SHEET 5 B1A 6 SER B 202 TRP B 209 1 N LEU B 205 O ALA B 105 1TAH 231
SHEET 6 B1A 6 THR B 196 VAL B 199 -1 N GLU B 197 O HIS B 204 1TAH 232
SHEET 1 B1B 6 VAL B 44 ALA B 47 0 1TAH 233
SHEET 2 B1B 6 VAL B 11 VAL B 14 1 N LEU B 13 O TYR B 45 1TAH 234
SHEET 3 B1B 6 VAL B 81 HIS B 86 1 O ILE B 84 N VAL B 14 1TAH 235
SHEET 4 B1B 6 VAL B 104 ILE B 110 1 N ALA B 105 O VAL B 81 1TAH 236
SHEET 5 B1B 6 SER B 202 TRP B 209 1 N LEU B 205 O ALA B 105 1TAH 237
SHEET 6 B1B 6 GLN B 275 VAL B 276 1 N GLN B 275 O LEU B 206 1TAH 238
SHEET 1 B2 2 ILE B 214 VAL B 220 0 1TAH 239
SHEET 2 B2 2 VAL B 223 ASP B 228 -1 N THR B 227 O GLN B 215 1TAH 240
SHEET 1 A1A 6 VAL A 44 ALA A 47 0 1TAH 241
SHEET 2 A1A 6 VAL A 11 VAL A 14 1 N LEU A 13 O TYR A 45 1TAH 242
SHEET 3 A1A 6 VAL A 81 HIS A 86 1 O ILE A 84 N VAL A 14 1TAH 243
SHEET 4 A1A 6 VAL A 104 ILE A 110 1 N ALA A 105 O VAL A 81 1TAH 244
SHEET 5 A1A 6 SER A 202 TRP A 209 1 N LEU A 205 O ALA A 105 1TAH 245
SHEET 6 A1A 6 THR A 196 VAL A 199 -1 N GLU A 197 O HIS A 204 1TAH 246
SHEET 1 A1B 6 VAL A 44 ALA A 47 0 1TAH 247
SHEET 2 A1B 6 VAL A 11 VAL A 14 1 N LEU A 13 O TYR A 45 1TAH 248
SHEET 3 A1B 6 VAL A 81 HIS A 86 1 O ILE A 84 N VAL A 14 1TAH 249
SHEET 4 A1B 6 VAL A 104 ILE A 110 1 N ALA A 105 O VAL A 81 1TAH 250
SHEET 5 A1B 6 SER A 202 TRP A 209 1 N LEU A 205 O ALA A 105 1TAH 251
SHEET 6 A1B 6 GLN A 275 VAL A 276 1 N GLN A 275 O LEU A 206 1TAH 252
SHEET 1 A2 2 ILE A 214 VAL A 220 0 1TAH 253
SHEET 2 A2 2 VAL A 223 ASP A 228 -1 N THR A 227 O GLN A 215 1TAH 254
SHEET 1 C1A 6 VAL C 44 ALA C 47 0 1TAH 255
SHEET 2 C1A 6 VAL C 11 VAL C 14 1 N LEU C 13 O TYR C 45 1TAH 256
SHEET 3 C1A 6 VAL C 81 HIS C 86 1 O ILE C 84 N VAL C 14 1TAH 257
SHEET 4 C1A 6 VAL C 104 ILE C 110 1 N ALA C 105 O VAL C 81 1TAH 258
SHEET 5 C1A 6 SER C 202 TRP C 209 1 N LEU C 205 O ALA C 105 1TAH 259
SHEET 6 C1A 6 THR C 196 VAL C 199 -1 N GLU C 197 O HIS C 204 1TAH 260
SHEET 1 C1B 6 VAL C 44 ALA C 47 0 1TAH 261
SHEET 2 C1B 6 VAL C 11 VAL C 14 1 N LEU C 13 O TYR C 45 1TAH 262
SHEET 3 C1B 6 VAL C 81 HIS C 86 1 O ILE C 84 N VAL C 14 1TAH 263
SHEET 4 C1B 6 VAL C 104 ILE C 110 1 N ALA C 105 O VAL C 81 1TAH 264
SHEET 5 C1B 6 SER C 202 TRP C 209 1 N LEU C 205 O ALA C 105 1TAH 265
SHEET 6 C1B 6 GLN C 275 VAL C 276 1 N GLN C 275 O LEU C 206 1TAH 266
SHEET 1 C2 2 ILE C 214 VAL C 220 0 1TAH 267
SHEET 2 C2 2 VAL C 223 ASP C 228 -1 N THR C 227 O GLN C 215 1TAH 268
SHEET 1 D1A 6 VAL D 44 ALA D 47 0 1TAH 269
SHEET 2 D1A 6 VAL D 11 VAL D 14 1 N LEU D 13 O TYR D 45 1TAH 270
SHEET 3 D1A 6 VAL D 81 HIS D 86 1 O ILE D 84 N VAL D 14 1TAH 271
SHEET 4 D1A 6 VAL D 104 ILE D 110 1 N ALA D 105 O VAL D 81 1TAH 272
SHEET 5 D1A 6 SER D 202 TRP D 209 1 N LEU D 205 O ALA D 105 1TAH 273
SHEET 6 D1A 6 THR D 196 VAL D 199 -1 N GLU D 197 O HIS D 204 1TAH 274
SHEET 1 D1B 6 VAL D 44 ALA D 47 0 1TAH 275
SHEET 2 D1B 6 VAL D 11 VAL D 14 1 N LEU D 13 O TYR D 45 1TAH 276
SHEET 3 D1B 6 VAL D 81 HIS D 86 1 O ILE D 84 N VAL D 14 1TAH 277
SHEET 4 D1B 6 VAL D 104 ILE D 110 1 N ALA D 105 O VAL D 81 1TAH 278
SHEET 5 D1B 6 SER D 202 TRP D 209 1 N LEU D 205 O ALA D 105 1TAH 279
SHEET 6 D1B 6 GLN D 275 VAL D 276 1 N GLN D 275 O LEU D 206 1TAH 280
SHEET 1 D2 2 ILE D 214 VAL D 220 0 1TAH 281
SHEET 2 D2 2 VAL D 223 ASP D 228 -1 N THR D 227 O GLN D 215 1TAH 282
TURN 1 B1 THR B 3 ALA B 6 1TAH 283
TURN 2 B2 ASP B 21 ALA B 24 1TAH 284
TURN 3 B3 VAL B 26 TYR B 29 1TAH 285
TURN 4 B4 SER B 39 ALA B 42 1TAH 286
TURN 5 B5 LEU B 49 PHE B 52 1TAH 287
TURN 6 B6 GLY B 57 GLY B 60 1TAH 288
TURN 7 B7 PRO B 113 GLY B 116 1TAH 289
TURN 8 B8 ASP B 130 GLY B 133 1TAH 290
TURN 9 B9 GLY B 133 SER B 136 1TAH 291
TURN 10 B10 ARG B 165 THR B 168 1TAH 292
TURN 11 B11 SER B 181 LEU B 184 1TAH 293
TURN 12 B12 VAL B 199 SER B 202 1TAH 294
TURN 13 B13 VAL B 220 VAL B 223 1TAH 295
TURN 14 B14 GLY B 232 ASP B 235 1TAH 296
TURN 15 B15 ASN B 284 ASP B 287 INCLUDES CATALYTIC HISTIDINE 1TAH 297
TURN 16 B16 GLY B 297 ALA B 300 1TAH 298
TURN 17 A1 THR A 3 ALA A 6 1TAH 299
TURN 18 A2 ASP A 21 ALA A 24 1TAH 300
TURN 19 A3 VAL A 26 TYR A 29 1TAH 301
TURN 20 A4 SER A 39 ALA A 42 1TAH 302
TURN 21 A5 LEU A 49 PHE A 52 1TAH 303
TURN 22 A6 GLY A 57 GLY A 60 1TAH 304
TURN 23 A7 PRO A 113 GLY A 116 1TAH 305
TURN 24 A8 ASP A 130 GLY A 133 1TAH 306
TURN 25 A9 GLY A 133 SER A 136 1TAH 307
TURN 26 A10 ARG A 165 THR A 168 1TAH 308
TURN 27 A11 SER A 181 LEU A 184 1TAH 309
TURN 28 A12 VAL A 199 SER A 202 1TAH 310
TURN 29 A13 VAL A 220 VAL A 223 1TAH 311
TURN 30 A14 GLY A 232 ASP A 235 1TAH 312
TURN 31 A15 ASN A 284 ASP A 287 INCLUDES CATALYTIC HISTIDINE 1TAH 313
TURN 32 A16 GLY A 297 ALA A 300 1TAH 314
TURN 33 C1 THR C 3 ALA C 6 1TAH 315
TURN 34 C2 ASP C 21 ALA C 24 1TAH 316
TURN 35 C3 VAL C 26 TYR C 29 1TAH 317
TURN 36 C4 SER C 39 ALA C 42 1TAH 318
TURN 37 C5 LEU C 49 PHE C 52 1TAH 319
TURN 38 C6 GLY C 57 GLY C 60 1TAH 320
TURN 39 C7 PRO C 113 GLY C 116 1TAH 321
TURN 40 C8 ASP C 130 GLY C 133 1TAH 322
TURN 41 C9 GLY C 133 SER C 136 1TAH 323
TURN 42 C10 ARG C 165 THR C 168 1TAH 324
TURN 43 C11 SER C 181 LEU C 184 1TAH 325
TURN 44 C12 VAL C 199 SER C 202 1TAH 326
TURN 45 C13 VAL C 220 VAL C 223 1TAH 327
TURN 46 C14 GLY C 232 ASP C 235 1TAH 328
TURN 47 C15 ASN C 284 ASP C 287 INCLUDES CATALYTIC HISTIDINE 1TAH 329
TURN 48 C16 GLY C 297 ALA C 300 1TAH 330
TURN 49 D1 THR D 3 ALA D 6 1TAH 331
TURN 50 D2 ASP D 21 ALA D 24 1TAH 332
TURN 51 D3 VAL D 26 TYR D 29 1TAH 333
TURN 52 D4 SER D 39 ALA D 42 1TAH 334
TURN 53 D5 LEU D 49 PHE D 52 1TAH 335
TURN 54 D6 GLY D 57 GLY D 60 1TAH 336
TURN 55 D7 PRO D 113 GLY D 116 1TAH 337
TURN 56 D8 ASP D 130 GLY D 133 1TAH 338
TURN 57 D9 GLY D 133 SER D 136 1TAH 339
TURN 58 D10 ARG D 165 THR D 168 1TAH 340
TURN 59 D11 SER D 181 LEU D 184 1TAH 341
TURN 60 D12 VAL D 199 SER D 202 1TAH 342
TURN 61 D13 VAL D 220 VAL D 223 1TAH 343
TURN 62 D14 GLY D 232 ASP D 235 1TAH 344
TURN 63 D15 ASN D 284 ASP D 287 INCLUDES CATALYTIC HISTIDINE 1TAH 345
TURN 64 D16 GLY D 297 ALA D 300 1TAH 346
SSBOND 1 CYS B 190 CYS B 269 1TAH 347
SSBOND 2 CYS A 190 CYS A 269 1TAH 348
SSBOND 3 CYS C 190 CYS C 269 1TAH 349
SSBOND 4 CYS D 190 CYS D 269 1TAH 350
SITE 1 ACB 4 SER B 87 HIS B 285 ASP B 263 GLU B 288 1TAH 351
SITE 1 CAB 4 ASP B 287 GLN B 291 ASP B 241 VAL B 295 1TAH 352
SITE 1 ACA 4 SER A 87 HIS A 285 ASP A 263 GLU A 288 1TAH 353
SITE 1 CAA 4 ASP A 287 GLN A 291 ASP A 241 VAL A 295 1TAH 354
SITE 1 ACC 4 SER C 87 HIS C 285 ASP C 263 GLU C 288 1TAH 355
SITE 1 CAC 4 ASP C 287 GLN C 291 ASP C 241 VAL C 295 1TAH 356
SITE 1 ACD 4 SER D 87 HIS D 285 ASP D 263 GLU D 288 1TAH 357
SITE 1 CAD 4 ASP D 287 GLN D 291 ASP D 241 VAL D 295 1TAH 358
CRYST1 158.160 158.640 63.360 90.00 90.00 90.00 P 21 21 21 16 1TAH 359
ORIGX1 1.000000 0.000000 0.000000 0.00000 1TAH 360
ORIGX2 0.000000 1.000000 0.000000 0.00000 1TAH 361
ORIGX3 0.000000 0.000000 1.000000 0.00000 1TAH 362
SCALE1 0.006323 0.000000 0.000000 0.00000 1TAH 363
SCALE2 0.000000 0.006304 0.000000 0.00000 1TAH 364
SCALE3 0.000000 0.000000 0.015783 0.00000 1TAH 365
MTRIX1 1 0.919530 -0.386190 -0.072730 -36.54662 1 1TAH 366
MTRIX2 1 -0.391680 -0.885550 -0.249790 -137.60590 1 1TAH 367
MTRIX3 1 0.032070 0.258190 -0.965570 11.32877 1 1TAH 368
MTRIX1 2 -0.530770 -0.727150 0.435350 -66.96497 1 1TAH 369
MTRIX2 2 0.311920 0.310020 0.898110 -36.55047 1 1TAH 370
MTRIX3 2 -0.788030 0.612490 0.062260 93.23410 1 1TAH 371
MTRIX1 3 -0.876490 -0.252820 -0.409690 -41.48827 1 1TAH 372
MTRIX2 3 -0.417830 -0.023250 0.908230 -43.33078 1 1TAH 373
MTRIX3 3 -0.239150 0.967230 -0.085260 82.01373 1 1TAH 374 |