| content |
HEADER THIOESTERASE 19-APR-94 1THT 1THT 2
COMPND THIOESTERASE 1THT 3
SOURCE (VIBRIO HARVEYI) 1THT 4
EXPDTA X-RAY DIFFRACTION 1THT 5
AUTHOR D.M.LAWSON,U.DEREWENDA,L.SERRE,S.FERRI,R.SZITTER,Y.WEI, 1THTA 1
AUTHOR 2 E.A.MEIGHEN,Z.S.DEREWENDA 1THT 7
REVDAT 2 20-JUL-95 1THTA 1 AUTHOR 1THTA 2
REVDAT 1 07-JUN-95 1THT 0 1THT 8
JRNL AUTH D.M.LAWSON,U.DEREWENDA,L.SERRE,S.FERRI,R.SZITTNER, 1THT 9
JRNL AUTH 2 Y.WEI,E.A.MEIGHEN,Z.S.DEREWENDA 1THT 10
JRNL TITL STRUCTURE OF A MYRISTOYL-ACP-SPECIFIC THIOESTERASE 1THT 11
JRNL TITL 2 FROM VIBRIO HARVEYI 1THT 12
JRNL REF BIOCHEMISTRY V. 33 9382 1994 1THT 13
JRNL REFN ASTM BICHAW US ISSN 0006-2960 0033 1THT 14
REMARK 1 1THT 15
REMARK 2 1THT 16
REMARK 2 RESOLUTION. 2.1 ANGSTROMS. 1THT 17
REMARK 3 1THT 18
REMARK 3 REFINEMENT. 1THT 19
REMARK 3 PROGRAM 1 PROLSQ 1THT 20
REMARK 3 AUTHORS 1 KONNERT,HENDRICKSON 1THT 21
REMARK 3 PROGRAM 2 X-PLOR 1THT 22
REMARK 3 AUTHORS 2 BRUNGER 1THT 23
REMARK 3 PROGRAM 3 ARP 1THT 24
REMARK 3 AUTHORS 3 LAMZIN,WILSON 1THT 25
REMARK 3 R VALUE 0.227 1THT 26
REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1THT 27
REMARK 3 RMSD BOND ANGLES 2.904 DEGREES 1THT 28
REMARK 3 1THT 29
REMARK 3 NUMBER OF REFLECTIONS 36771 (BETWEEN 30-2.1 A) 1THT 30
REMARK 3 RESOLUTION RANGE 8.0 - 2.1 ANGSTROMS (REFINEMENT) 1THT 31
REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 1THT 32
REMARK 3 PERCENT COMPLETION 86.2 1THT 33
REMARK 3 1THT 34
REMARK 3 NUMBER OF PROTEIN ATOMS 4594 1THT 35
REMARK 3 NUMBER OF SOLVENT ATOMS 55 1THT 36
REMARK 3 1THT 37
REMARK 3 GEOMETRICAL RESTRAINTS USED IN LAST CYCLES OF 1THT 38
REMARK 3 ENERGY MINIMIZATION (X-PLOR) ARE THE RESTRAINTS DESCRIBED 1THT 39
REMARK 3 IN THE PARAMETER FILE PARAM19X.PRO FOUND IN THE TOPPAR 1THT 40
REMARK 3 DIRECTORY (3.1). TO IMPROVE THE GEOMETRY, THE WEIGHT 1THT 41
REMARK 3 APPLIED ON THE DIFFRACTION DATA WAS DECREASED IN THE LAST 1THT 42
REMARK 3 CYCLES OF REFINEMENT FROM 0.34E+06 TO 0.24E+06. 1THT 43
REMARK 3 1THT 44
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES GIVEN WITH PROLSQ 1THT 45
REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 1THT 46
REMARK 3 BOND DISTANCE 0.020 1THT 47
REMARK 3 ANGLE DISTANCE 0.058 1THT 48
REMARK 3 PLANAR 1-4 DISTANCE 0.077 1THT 49
REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.028 1THT 50
REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.137 1THT 51
REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 1THT 52
REMARK 3 SINGLE TORSION CONTACT 0.174 1THT 53
REMARK 3 MULTIPLE TORSION CONTACT 0.260 1THT 54
REMARK 3 POSSIBLE HYDROGEN BOND 0.116 1THT 55
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 1THT 56
REMARK 3 PLANAR 4.794 1THT 57
REMARK 3 STAGGERED 18.324 1THT 58
REMARK 3 ORTHONORMAL 32.107 1THT 59
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 1THT 60
REMARK 3 MAIN-CHAIN BOND 3.388 1THT 61
REMARK 3 MAIN-CHAIN ANGLE 5.124 1THT 62
REMARK 3 SIDE-CHAIN BOND 4.025 1THT 63
REMARK 3 SIDE-CHAIN ANGLE 6.024 1THT 64
REMARK 3 1THT 65
REMARK 3 REFINEMENT: RESTRAINED LEAST_SQUARES, USING PROLSQ AND 1THT 66
REMARK 3 SIMULATING ANNEALING AND CONJUGATE GRADIENT MINIMIZATION 1THT 67
REMARK 3 X-PLOR. CYCLES OF CONJUGATE GRADIENT MINIIZATION WERE 1THT 68
REMARK 3 WITH ALTERNATED WITH AUTOMATIC REFINEMENT PROCEDURE 1THT 69
REMARK 3 ( OPTION UNRESTRAINED) DESCRIBED IN V.S. LAMZIN & 1THT 70
REMARK 3 WILSON K.S., ACTA CRYST., D49, 213-222 (1993). 1THT 71
REMARK 4 1THT 72
REMARK 4 THIS STRUCTURE WAS SOLVED BY THE MULTIPLE ISOMORPHOUS 1THT 73
REMARK 4 REPLACEMENT METHOD USING FOUR DERIVATIVES. 1THT 74
REMARK 5 1THT 75
REMARK 5 THERE ARE TWO MOLECULES PER ASYMMETRIC UNIT. 1THT 76
REMARK 6 1THT 77
REMARK 6 THE FOUR FIRST N-TERMINAL RESIDUES ARE NOT DEFINED IN THE 1THT 78
REMARK 6 MODEL FOR EACH MOLECULE. 1THT 79
REMARK 7 1THT 80
REMARK 7 THE LOOP 72 TO 83 IS ABSENT IN THE MODEL SINCE IT IS TOO 1THT 81
REMARK 7 MOBILE. 1THT 82
REMARK 8 1THT 83
REMARK 8 THE FOLLOWING RESIDUES HAVE SIDE CHAINS WHICH ARE NOT 1THT 84
REMARK 8 VISIBLE IN THE ELECTRON DENSITY AND HAVE BEEN MODELED AS 1THT 85
REMARK 8 EITHER ALA OR GLY: 1THT 86
REMARK 8 1THT 87
REMARK 8 MOLECULE A: GLN A 4, LYS A 6, ARG A 13, VAL A 14, 1THT 88
REMARK 8 ARG A 46, ARG A 47, GLU A 83, LYS A 103, AND LYS A 294. 1THT 89
REMARK 8 MOLECULE B: LYS B 6, GLU B 83, HIS B 170, 1THT 90
REMARK 8 ASN B 209, ASN B 210, GLU B 217, AND LYS B 294. 1THT 91
REMARK 9 1THT 92
REMARK 9 THE STRANDS OF S2 IN *SHEET* RECORDS BELOW BOTH BELONG TO 1THT 93
REMARK 9 THE CAP DOMAIN. 1THT 94
REMARK 10 1THT 95
REMARK 10 THE SITE IDENTIFIED AS CAT AND CBT IN *SITE* RECORDS BELOW 1THT 96
REMARK 10 IS A CATALYTIC TRIAD. 1THT 97
REMARK 11 1THTA 3
REMARK 11 CORRECTION. CORRECT PUNCTUATION ERROR ON AUTHOR RECORD. 1THTA 4
REMARK 11 20-JUL-95. 1THTA 5
REMARK 999 1THT 98
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1THT 99
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1THT 100
REMARK 999 LUXD_VIBHA A 1THT 101
REMARK 999 1THT 102
REMARK 999 SEQUENCE ADVISORY NOTICE 1THT 103
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1THT 104
REMARK 999 1THT 105
REMARK 999 SWISS-PROT ENTRY NAME: LUXD_VIBHA 1THT 106
REMARK 999 1THT 107
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES 1THT 108
REMARK 999 1THT 109
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1THT 110
REMARK 999 GLU 60 THR A 60 1THT 111
REMARK 999 SER 299 ASN A 299 1THT 112
REMARK 999 1THT 113
REMARK 999 CROSS REFERENCE TO SEQUENCE DATABASE 1THT 114
REMARK 999 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1THT 115
REMARK 999 LUXD_VIBHA B 1THT 116
REMARK 999 1THT 117
REMARK 999 SEQUENCE ADVISORY NOTICE 1THT 118
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1THT 119
REMARK 999 1THT 120
REMARK 999 SWISS-PROT ENTRY NAME: LUXD_VIBHA 1THT 121
REMARK 999 1THT 122
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES 1THT 123
REMARK 999 1THT 124
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1THT 125
REMARK 999 GLU 60 THR B 60 1THT 126
REMARK 999 SER 299 ASN B 299 1THT 127
SEQRES 1 A 305 MET ASN ASN GLN CYS LYS THR ILE ALA HIS VAL LEU ARG 1THT 128
SEQRES 2 A 305 VAL ASN ASN GLY GLN GLU LEU HIS VAL TRP GLU THR PRO 1THT 129
SEQRES 3 A 305 PRO LYS GLU ASN VAL PRO PHE LYS ASN ASN THR ILE LEU 1THT 130
SEQRES 4 A 305 ILE ALA SER GLY PHE ALA ARG ARG MET ASP HIS PHE ALA 1THT 131
SEQRES 5 A 305 GLY LEU ALA GLU TYR LEU SER THR ASN GLY PHE HIS VAL 1THT 132
SEQRES 6 A 305 PHE ARG TYR ASP SER LEU HIS HIS VAL GLY LEU SER SER 1THT 133
SEQRES 7 A 305 GLY SER ILE ASP GLU PHE THR MET THR THR GLY LYS ASN 1THT 134
SEQRES 8 A 305 SER LEU CYS THR VAL TYR HIS TRP LEU GLN THR LYS GLY 1THT 135
SEQRES 9 A 305 THR GLN ASN ILE GLY LEU ILE ALA ALA SER LEU SER ALA 1THT 136
SEQRES 10 A 305 ARG VAL ALA TYR GLU VAL ILE SER ASP LEU GLU LEU SER 1THT 137
SEQRES 11 A 305 PHE LEU ILE THR ALA VAL GLY VAL VAL ASN LEU ARG ASP 1THT 138
SEQRES 12 A 305 THR LEU GLU LYS ALA LEU GLY PHE ASP TYR LEU SER LEU 1THT 139
SEQRES 13 A 305 PRO ILE ASP GLU LEU PRO ASN ASP LEU ASP PHE GLU GLY 1THT 140
SEQRES 14 A 305 HIS LYS LEU GLY SER GLU VAL PHE VAL ARG ASP CYS PHE 1THT 141
SEQRES 15 A 305 GLU HIS HIS TRP ASP THR LEU ASP SER THR LEU ASP LYS 1THT 142
SEQRES 16 A 305 VAL ALA ASN THR SER VAL PRO LEU ILE ALA PHE THR ALA 1THT 143
SEQRES 17 A 305 ASN ASN ASP ASP TRP VAL LYS GLN GLU GLU VAL TYR ASP 1THT 144
SEQRES 18 A 305 MET LEU ALA HIS ILE ARG THR GLY HIS CYS LYS LEU TYR 1THT 145
SEQRES 19 A 305 SER LEU LEU GLY SER SER HIS ASP LEU GLY GLU ASN LEU 1THT 146
SEQRES 20 A 305 VAL VAL LEU ARG ASN PHE TYR GLN SER VAL THR LYS ALA 1THT 147
SEQRES 21 A 305 ALA ILE ALA MET ASP GLY GLY SER LEU GLU ILE ASP VAL 1THT 148
SEQRES 22 A 305 ASP PHE ILE GLU PRO ASP PHE GLU GLN LEU THR ILE ALA 1THT 149
SEQRES 23 A 305 THR VAL ASN GLU ARG ARG LEU LYS ALA GLU ILE GLU ASN 1THT 150
SEQRES 24 A 305 ARG THR PRO GLU MET ALA 1THT 151
SEQRES 1 B 305 MET ASN ASN GLN CYS LYS THR ILE ALA HIS VAL LEU ARG 1THT 152
SEQRES 2 B 305 VAL ASN ASN GLY GLN GLU LEU HIS VAL TRP GLU THR PRO 1THT 153
SEQRES 3 B 305 PRO LYS GLU ASN VAL PRO PHE LYS ASN ASN THR ILE LEU 1THT 154
SEQRES 4 B 305 ILE ALA SER GLY PHE ALA ARG ARG MET ASP HIS PHE ALA 1THT 155
SEQRES 5 B 305 GLY LEU ALA GLU TYR LEU SER THR ASN GLY PHE HIS VAL 1THT 156
SEQRES 6 B 305 PHE ARG TYR ASP SER LEU HIS HIS VAL GLY LEU SER SER 1THT 157
SEQRES 7 B 305 GLY SER ILE ASP GLU PHE THR MET THR THR GLY LYS ASN 1THT 158
SEQRES 8 B 305 SER LEU CYS THR VAL TYR HIS TRP LEU GLN THR LYS GLY 1THT 159
SEQRES 9 B 305 THR GLN ASN ILE GLY LEU ILE ALA ALA SER LEU SER ALA 1THT 160
SEQRES 10 B 305 ARG VAL ALA TYR GLU VAL ILE SER ASP LEU GLU LEU SER 1THT 161
SEQRES 11 B 305 PHE LEU ILE THR ALA VAL GLY VAL VAL ASN LEU ARG ASP 1THT 162
SEQRES 12 B 305 THR LEU GLU LYS ALA LEU GLY PHE ASP TYR LEU SER LEU 1THT 163
SEQRES 13 B 305 PRO ILE ASP GLU LEU PRO ASN ASP LEU ASP PHE GLU GLY 1THT 164
SEQRES 14 B 305 HIS LYS LEU GLY SER GLU VAL PHE VAL ARG ASP CYS PHE 1THT 165
SEQRES 15 B 305 GLU HIS HIS TRP ASP THR LEU ASP SER THR LEU ASP LYS 1THT 166
SEQRES 16 B 305 VAL ALA ASN THR SER VAL PRO LEU ILE ALA PHE THR ALA 1THT 167
SEQRES 17 B 305 ASN ASN ASP ASP TRP VAL LYS GLN GLU GLU VAL TYR ASP 1THT 168
SEQRES 18 B 305 MET LEU ALA HIS ILE ARG THR GLY HIS CYS LYS LEU TYR 1THT 169
SEQRES 19 B 305 SER LEU LEU GLY SER SER HIS ASP LEU GLY GLU ASN LEU 1THT 170
SEQRES 20 B 305 VAL VAL LEU ARG ASN PHE TYR GLN SER VAL THR LYS ALA 1THT 171
SEQRES 21 B 305 ALA ILE ALA MET ASP GLY GLY SER LEU GLU ILE ASP VAL 1THT 172
SEQRES 22 B 305 ASP PHE ILE GLU PRO ASP PHE GLU GLN LEU THR ILE ALA 1THT 173
SEQRES 23 B 305 THR VAL ASN GLU ARG ARG LEU LYS ALA GLU ILE GLU ASN 1THT 174
SEQRES 24 B 305 ARG THR PRO GLU MET ALA 1THT 175
FORMUL 3 HOH *55(H2 O1) 1THT 176
HELIX 1 AH1 ALA A 52 THR A 60 1 1THT 177
HELIX 2 AH2 MET A 86 THR A 102 1 1THT 178
HELIX 3 AH3 LEU A 115 VAL A 123 1 1THT 179
HELIX 4 AC1 LEU A 141 LEU A 149 1 BELONGS TO THE CAP DOMAIN 1THT 180
HELIX 5 AC2 SER A 174 GLU A 183 1 BELONGS TO THE CAP DOMAIN 1THT 181
HELIX 6 AH4 LEU A 189 VAL A 196 1 1THT 182
HELIX 7 AH5 GLN A 216 LEU A 223 1 1THT 183
HELIX 8 AH6 LEU A 247 ASP A 265 1 1THT 184
HELIX 9 AH7 PHE A 280 GLU A 296 1 1THT 185
HELIX 10 BH1 ALA B 52 THR B 60 1 1THT 186
HELIX 11 BH2 MET B 86 THR B 102 1 1THT 187
HELIX 12 BH3 LEU B 115 VAL B 123 1 1THT 188
HELIX 13 BC1 LEU B 141 LEU B 149 1 BELONGS TO THE CAP DOMAIN 1THT 189
HELIX 14 BC2 SER B 174 GLU B 183 1 BELONGS TO THE CAP DOMAIN 1THT 190
HELIX 15 BH4 LEU B 189 VAL B 196 1 1THT 191
HELIX 16 BH5 GLN B 216 LEU B 223 1 1THT 192
HELIX 17 BH6 LEU B 247 ASP B 265 1 1THT 193
HELIX 18 BH7 PHE B 280 GLU B 296 1 1THT 194
SHEET 1 S1A 9 ILE A 8 VAL A 14 0 1THT 195
SHEET 2 S1A 9 GLN A 18 THR A 25 -1 1THT 196
SHEET 3 S1A 9 THR A 37 ALA A 41 -1 1THT 197
SHEET 4 S1A 9 VAL A 65 TYR A 68 1 1THT 198
SHEET 5 S1A 9 ILE A 108 ALA A 113 1 1THT 199
SHEET 6 S1A 9 PHE A 131 ALA A 135 1 1THT 200
SHEET 7 S1A 9 LEU A 203 ALA A 208 1 1THT 201
SHEET 8 S1A 9 CYS A 231 LEU A 236 1 1THT 202
SHEET 9 S1A 9 PRO A 302 MET A 304 1 1THT 203
SHEET 1 S2A 2 ASP A 164 LEU A 165 0 1THT 204
SHEET 2 S2A 2 LEU A 172 GLY A 173 -1 1THT 205
SHEET 1 S1B 9 ILE B 8 VAL B 14 0 1THT 206
SHEET 2 S1B 9 GLN B 18 THR B 25 -1 1THT 207
SHEET 3 S1B 9 THR B 37 ALA B 41 -1 1THT 208
SHEET 4 S1B 9 VAL B 65 TYR B 68 1 1THT 209
SHEET 5 S1B 9 ILE B 108 ALA B 113 1 1THT 210
SHEET 6 S1B 9 PHE B 131 ALA B 135 1 1THT 211
SHEET 7 S1B 9 LEU B 203 ALA B 208 1 1THT 212
SHEET 8 S1B 9 CYS B 231 LEU B 236 1 1THT 213
SHEET 9 S1B 9 PRO B 302 MET B 304 1 1THT 214
SHEET 1 S2B 2 ASP B 164 LEU B 165 0 1THT 215
SHEET 2 S2B 2 LEU B 172 GLY B 173 -1 1THT 216
SITE 1 CAT 3 SER A 114 HIS A 241 ASP A 211 1THT 217
SITE 1 CBT 3 SER B 114 HIS B 241 ASP B 211 1THT 218
CRYST1 97.500 83.800 47.400 90.00 97.30 90.00 P 21 4 1THT 219
ORIGX1 1.000000 0.000000 0.000000 0.00000 1THT 220
ORIGX2 0.000000 1.000000 0.000000 0.00000 1THT 221
ORIGX3 0.000000 0.000000 1.000000 0.00000 1THT 222
SCALE1 0.010256 0.000000 0.001314 0.00000 1THT 223
SCALE2 0.000000 0.011933 0.000000 0.00000 1THT 224
SCALE3 0.000000 0.000000 0.021269 0.00000 1THT 225 |