Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 1TCC-pdb

Name Class
1TCC-pdb
HEADER    HYDROLASE(CARBOXYLIC ESTERASE)          28-FEB-94   1TCC      1TCC   2
COMPND    LIPASE (E.C.3.1.1.3) (TRIACYLGLYCEROL HYDROLASE)              1TCC   3
SOURCE    YEAST (CANDIDA ANTARCTICA, FORM B)                            1TCC   4
AUTHOR    J.UPPENBERG,T.A.JONES                                         1TCC   5
REVDAT   1   31-MAY-94 1TCC    0                                        1TCC   6
JRNL        AUTH   J.UPPENBERG,M.T.HANSEN,S.PATKAR,T.A.JONES            1TCC   7
JRNL        TITL   THE SEQUENCE, CRYSTAL STRUCTURE DETERMINATION AND    1TCC   8
JRNL        TITL 2 REFINEMENT OF TWO CRYSTAL FORMS OF LIPASE B FROM     1TCC   9
JRNL        TITL 3 CANDIDA ANTARCTICA                                   1TCC  10
JRNL        REF    STRUCTURE                     V.   2   293 1994      1TCC  11
JRNL        REFN   ASTM         UK ISSN 0969-2126                 2005  1TCC  12
REMARK   1                                                              1TCC  13
REMARK   1 REFERENCE 1                                                  1TCC  14
REMARK   1  AUTH   J.UPPENBERG,S.PATKAR,T.BERGFORS,T.A.JONES            1TCC  15
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY STUDIES OF     1TCC  16
REMARK   1  TITL 2 LIPASE B FROM CANDIDA ANTARCTICA                     1TCC  17
REMARK   1  REF    J.MOL.BIOL.                   V. 235   790 1994      1TCC  18
REMARK   1  REFN   ASTM JMOBAK  UK ISSN 0022-2836                 0070  1TCC  19
REMARK   2                                                              1TCC  20
REMARK   2 RESOLUTION. 2.5  ANGSTROMS.                                  1TCC  21
REMARK   3                                                              1TCC  22
REMARK   3 REFINEMENT.                                                  1TCC  23
REMARK   3   PROGRAM                    X-PLOR                          1TCC  24
REMARK   3   AUTHORS                    BRUNGER                         1TCC  25
REMARK   3   R VALUE                    0.196                           1TCC  26
REMARK   3   RMSD BOND DISTANCES        0.006  ANGSTROMS                1TCC  27
REMARK   3   RMSD BOND ANGLES           1.3    DEGREES                  1TCC  28
REMARK   3                                                              1TCC  29
REMARK   3   NUMBER OF REFLECTIONS      18925                           1TCC  30
REMARK   3   RESOLUTION RANGE       7.5 - 2.5  ANGSTROMS                1TCC  31
REMARK   3   DATA CUTOFF                2.0    SIGMA(F)                 1TCC  32
REMARK   3   PERCENT COMPLETION         94.                             1TCC  33
REMARK   3                                                              1TCC  34
REMARK   3   NUMBER OF PROTEIN ATOMS                       4648         1TCC  35
REMARK   3   NUMBER OF SOLVENT ATOMS                        159         1TCC  36
REMARK   4                                                              1TCC  37
REMARK   4 THE PUTATIVE CATALYTIC SITES CONSIST OF A SERINE TRIAD AND   1TCC  38
REMARK   4 HAVE THE IDENTIFIERS CTA AND CTB IN THIS FORM.               1TCC  39
REMARK   5                                                              1TCC  40
REMARK   5 THIS ENTRY IS ONE OF THREE ENTRIES ASSOCIATED WITH THE JRNL  1TCC  41
REMARK   5 REFERENCE ABOVE, WHICH DESCRIBES THREE DIFFERENT STRUCTURES  1TCC  42
REMARK   5 IN TWO CRYSTAL FORMS.  THE OTHER STRUCTURES CAN BE FOUND IN  1TCC  43
REMARK   5 PROTEIN DATA BANK ENTRIES 1TCA AND 1TCB.                     1TCC  44
REMARK   6                                                              1TCC  45
REMARK   6 THIS IS THE HIGH PH STRUCTURE OF THE MONOCLINIC CRYSTAL;     1TCC  46
REMARK   6 FORM WITH TWO MOLECULES IN THE ASYMMETRIC UNIT.  THE         1TCC  47
REMARK   6 MOLECULES ARE CALLED A AND B.  THE RMS DEVIATIONS ARE 0.23   1TCC  48
REMARK   6 ANGSTROMS FOR C-ALPHAS AND 0.33 ANGSTROMS FOR ALL ATOMS.     1TCC  49
REMARK   7                                                              1TCC  50
REMARK   7 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL   1TCC  51
REMARK   7 YIELD APPROXIMATE COORDINATES FOR CHAIN B WHEN APPLIED TO    1TCC  52
REMARK   7 CHAIN A.                                                     1TCC  53
REMARK   8                                                              1TCC  54
REMARK   8 THERE IS ESSENTIALLY NO ELECTRON DENSITY FOR THE FOLLOWING   1TCC  55
REMARK   8 SIDE CHAIN ATOMS:                                            1TCC  56
REMARK   8                                                              1TCC  57
REMARK   8   MOLECULE A:                                                1TCC  58
REMARK   8                                                              1TCC  59
REMARK   8   LYS  32:  CD, CE, NZ                                       1TCC  60
REMARK   8   ARG 242:  NE, CZ, NH1, NH2                                 1TCC  61
REMARK   8   ARG 249:  CB, NE, NH2                                      1TCC  62
REMARK   8   ILE 255:  CG1, CD1                                         1TCC  63
REMARK   8   THR 256:  CG2                                              1TCC  64
REMARK   8   GLU 269:  CB, CG, CD, OE1, OE2                             1TCC  65
REMARK   8   ARG 309:  CB, NE, CZ, NH1, NH2                             1TCC  66
REMARK   8                                                              1TCC  67
REMARK   8   MOLECULE B:                                                1TCC  68
REMARK   8                                                              1TCC  69
REMARK   8   LYS  32:  NZ                                               1TCC  70
REMARK   8   142 - 149:  NO CONNECTED DENSITY                           1TCC  71
REMARK   8   ARG 242:  CB, CG, CD, NE, CZ, NH1, NH2                     1TCC  72
REMARK   8   ARG 249:  NE, CZ, NH1, NH2                                 1TCC  73
REMARK   8   ILE 255:  CD1, CG2                                         1TCC  74
REMARK   8   THR 256:  CG2                                              1TCC  75
REMARK   8   GLU 269:  N, CB, CG, OE2                                   1TCC  76
REMARK   8   LYS 290:  CE, NZ                                           1TCC  77
REMARK   8   ARG 309:  NE, CZ, NH1, NH2                                 1TCC  78
REMARK   9                                                              1TCC  79
REMARK   9 THE SEQUENCE HAS NOT BEEN REPORTED.  IT WAS DERIVED FROM     1TCC  80
REMARK   9 THE DNA SEQUENCE OF J.UPPENBERG ET AL., 1994, LISTED IN      1TCC  81
REMARK   9 THE JRNL REFERENCE ABOVE.                                    1TCC  82
SEQRES   1 A  317  LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS  1TCC  83
SEQRES   2 A  317  SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER  1TCC  84
SEQRES   3 A  317  PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY  1TCC  85
SEQRES   4 A  317  THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP  1TCC  86
SEQRES   5 A  317  ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP  1TCC  87
SEQRES   6 A  317  ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL  1TCC  88
SEQRES   7 A  317  ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR  1TCC  89
SEQRES   8 A  317  ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP  1TCC  90
SEQRES   9 A  317  SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE  1TCC  91
SEQRES  10 A  317  PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA  1TCC  92
SEQRES  11 A  317  PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO  1TCC  93
SEQRES  12 A  317  LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN  1TCC  94
SEQRES  13 A  317  GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN  1TCC  95
SEQRES  14 A  317  ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU  1TCC  96
SEQRES  15 A  317  TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER  1TCC  97
SEQRES  16 A  317  ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS  1TCC  98
SEQRES  17 A  317  ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL  1TCC  99
SEQRES  18 A  317  ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR  1TCC 100
SEQRES  19 A  317  VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN  1TCC 101
SEQRES  20 A  317  ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO  1TCC 102
SEQRES  21 A  317  LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA  1TCC 103
SEQRES  22 A  317  ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL  1TCC 104
SEQRES  23 A  317  ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO  1TCC 105
SEQRES  24 A  317  TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER  1TCC 106
SEQRES  25 A  317  GLY ILE VAL THR PRO                                  1TCC 107
SEQRES   1 B  317  LEU PRO SER GLY SER ASP PRO ALA PHE SER GLN PRO LYS  1TCC 108
SEQRES   2 B  317  SER VAL LEU ASP ALA GLY LEU THR CYS GLN GLY ALA SER  1TCC 109
SEQRES   3 B  317  PRO SER SER VAL SER LYS PRO ILE LEU LEU VAL PRO GLY  1TCC 110
SEQRES   4 B  317  THR GLY THR THR GLY PRO GLN SER PHE ASP SER ASN TRP  1TCC 111
SEQRES   5 B  317  ILE PRO LEU SER THR GLN LEU GLY TYR THR PRO CYS TRP  1TCC 112
SEQRES   6 B  317  ILE SER PRO PRO PRO PHE MET LEU ASN ASP THR GLN VAL  1TCC 113
SEQRES   7 B  317  ASN THR GLU TYR MET VAL ASN ALA ILE THR ALA LEU TYR  1TCC 114
SEQRES   8 B  317  ALA GLY SER GLY ASN ASN LYS LEU PRO VAL LEU THR TRP  1TCC 115
SEQRES   9 B  317  SER GLN GLY GLY LEU VAL ALA GLN TRP GLY LEU THR PHE  1TCC 116
SEQRES  10 B  317  PHE PRO SER ILE ARG SER LYS VAL ASP ARG LEU MET ALA  1TCC 117
SEQRES  11 B  317  PHE ALA PRO ASP TYR LYS GLY THR VAL LEU ALA GLY PRO  1TCC 118
SEQRES  12 B  317  LEU ASP ALA LEU ALA VAL SER ALA PRO SER VAL TRP GLN  1TCC 119
SEQRES  13 B  317  GLN THR THR GLY SER ALA LEU THR THR ALA LEU ARG ASN  1TCC 120
SEQRES  14 B  317  ALA GLY GLY LEU THR GLN ILE VAL PRO THR THR ASN LEU  1TCC 121
SEQRES  15 B  317  TYR SER ALA THR ASP GLU ILE VAL GLN PRO GLN VAL SER  1TCC 122
SEQRES  16 B  317  ASN SER PRO LEU ASP SER SER TYR LEU PHE ASN GLY LYS  1TCC 123
SEQRES  17 B  317  ASN VAL GLN ALA GLN ALA VAL CYS GLY PRO LEU PHE VAL  1TCC 124
SEQRES  18 B  317  ILE ASP HIS ALA GLY SER LEU THR SER GLN PHE SER TYR  1TCC 125
SEQRES  19 B  317  VAL VAL GLY ARG SER ALA LEU ARG SER THR THR GLY GLN  1TCC 126
SEQRES  20 B  317  ALA ARG SER ALA ASP TYR GLY ILE THR ASP CYS ASN PRO  1TCC 127
SEQRES  21 B  317  LEU PRO ALA ASN ASP LEU THR PRO GLU GLN LYS VAL ALA  1TCC 128
SEQRES  22 B  317  ALA ALA ALA LEU LEU ALA PRO ALA ALA ALA ALA ILE VAL  1TCC 129
SEQRES  23 B  317  ALA GLY PRO LYS GLN ASN CYS GLU PRO ASP LEU MET PRO  1TCC 130
SEQRES  24 B  317  TYR ALA ARG PRO PHE ALA VAL GLY LYS ARG THR CYS SER  1TCC 131
SEQRES  25 B  317  GLY ILE VAL THR PRO                                  1TCC 132
FTNOTE   1                                                              1TCC 133
FTNOTE   1 CIS PROLINE - PRO A    70                                    1TCC 134
FTNOTE   2                                                              1TCC 135
FTNOTE   2 CIS PROLINE - PRO A   192                                    1TCC 136
FTNOTE   3                                                              1TCC 137
FTNOTE   3 CIS PROLINE - PRO B    70                                    1TCC 138
FTNOTE   4                                                              1TCC 139
FTNOTE   4 CIS PROLINE - PRO B   192                                    1TCC 140
HET    NAG    401      14     N-ACETYL-D-GLUCOSAMINE                    1TCC 141
HET    NAG    402      14     N-ACETYL-D-GLUCOSAMINE                    1TCC 142
HET    BOG    501      20     B-OCTYLGLUCOSIDE                          1TCC 143
FORMUL   3  NAG    2(C8 H15 N1 O6)                                      1TCC 144
FORMUL   4  BOG    C14 H28 O6                                           1TCC 145
FORMUL   5  HOH   *159(H2 O1)                                           1TCC 146
HELIX    1  A1 LYS A   13  ALA A   18  1                                1TCC 147
HELIX    2  A2 GLY A   44  THR A   57  1                                1TCC 148
HELIX    3  A3 THR A   76  GLY A   93  1                                1TCC 149
HELIX    4  A4 GLN A  106  PHE A  117  1                                1TCC 150
HELIX    5  A5 GLY A  142  ALA A  146  1                                1TCC 151
HELIX    6  A6 PRO A  152  GLN A  156  1                                1TCC 152
HELIX    7  A7 ALA A  162  ASN A  169  1                                1TCC 153
HELIX    8  A8 ALA A  212  CYS A  216  1                                1TCC 154
HELIX    9  A9 GLY A  226  ARG A  242  1                                1TCC 155
HELIX   10 A10 PRO A  268  ALA A  287  1                                1TCC 156
HELIX   11 TH1 PRO A  119  ILE A  121  5                                1TCC 157
HELIX   12 TH2 VAL A  139  ALA A  141  5                                1TCC 158
HELIX   13 TH3 SER A  250  ASP A  252  5                                1TCC 159
HELIX   14 TH4 ILE A  255  ASP A  257  5                                1TCC 160
HELIX   15 TH5 ARG A  302  PHE A  304  5                                1TCC 161
HELIX   16 AP1 PRO A   68  PRO A   70 10                                1TCC 162
HELIX   17  B1 LYS B   13  ALA B   18  1                                1TCC 163
HELIX   18  B2 GLY B   44  THR B   57  1                                1TCC 164
HELIX   19  B3 THR B   76  GLY B   93  1                                1TCC 165
HELIX   20  B4 GLN B  106  PHE B  117  1                                1TCC 166
HELIX   21  B5 GLY B  142  ALA B  146  1                                1TCC 167
HELIX   22  B6 PRO B  152  GLN B  156  1                                1TCC 168
HELIX   23  B7 ALA B  162  ASN B  169  1                                1TCC 169
HELIX   24  B8 ALA B  212  CYS B  216  1                                1TCC 170
HELIX   25  B9 GLY B  226  ARG B  242  1                                1TCC 171
HELIX   26 B10 PRO B  268  ALA B  287  1                                1TCC 172
HELIX   27 TB1 PRO B  119  ILE B  121  5                                1TCC 173
HELIX   28 TB2 VAL B  139  ALA B  141  5                                1TCC 174
HELIX   29 TB3 SER B  250  ASP B  252  5                                1TCC 175
HELIX   30 TB4 ILE B  255  ASP B  257  5                                1TCC 176
HELIX   31 TB5 ARG B  302  PHE B  304  5                                1TCC 177
HELIX   32 BP1 PRO B   68  PRO B   70 10                                1TCC 178
SHEET    1 AS1 7 LEU A  20  CYS A  22  0                                1TCC 179
SHEET    2 AS1 7 THR A  62  ILE A  66 -1                                1TCC 180
SHEET    3 AS1 7 PRO A  33  VAL A  37  1                                1TCC 181
SHEET    4 AS1 7 LEU A  99  TRP A 104  1                                1TCC 182
SHEET    5 AS1 7 VAL A 125  PHE A 131  1                                1TCC 183
SHEET    6 AS1 7 THR A 179  TYR A 183  1                                1TCC 184
SHEET    7 AS1 7 LYS A 208  GLN A 211  1                                1TCC 185
SHEET    1 AS2 2 ARG A 309  THR A 310  0                                1TCC 186
SHEET    2 AS2 2 GLY A 313  ILE A 314 -1                                1TCC 187
SHEET    1 BS1 7 LEU B  20  CYS B  22  0                                1TCC 188
SHEET    2 BS1 7 THR B  62  ILE B  66 -1                                1TCC 189
SHEET    3 BS1 7 PRO B  33  VAL B  37  1                                1TCC 190
SHEET    4 BS1 7 LEU B  99  TRP B 104  1                                1TCC 191
SHEET    5 BS1 7 VAL B 125  PHE B 131  1                                1TCC 192
SHEET    6 BS1 7 THR B 179  TYR B 183  1                                1TCC 193
SHEET    7 BS1 7 LYS B 208  GLN B 211  1                                1TCC 194
SHEET    1 BS2 2 ARG B 309  THR B 310  0                                1TCC 195
SHEET    2 BS2 2 GLY B 313  ILE B 314 -1                                1TCC 196
TURN     1  A1 SER A  26  SER A  29     TYPE I                          1TCC 197
TURN     2  A2 GLY A  39  THR A  42     TYPE II                         1TCC 198
TURN     3  A3 ASP A 134  GLY A 137     TYPE I                          1TCC 199
TURN     4  A4 THR A 158  SER A 161     TYPE II                         1TCC 200
TURN     5  A5 SER A 184  ASP A 187     TYPE I                          1TCC 201
TURN     6  A6 SER A 197  ASP A 200     TYPE III                        1TCC 202
TURN     7  A7 LEU A 204  GLY A 207     TYPE II (NO GLY AT I 2)         1TCC 203
TURN     8  A8 GLY A 217  PHE A 220     TYPE I                          1TCC 204
TURN     9  A9 ALA A 263  LEU A 266     TYPE I                          1TCC 205
TURN    10 A10 THR A 310  GLY A 313     TYPE III                        1TCC 206
TURN    11  B1 SER B  26  SER B  29     TYPE I                          1TCC 207
TURN    12  B2 GLY B  39  THR B  42     TYPE II                         1TCC 208
TURN    13  B3 ASP B 134  GLY B 137     TYPE I                          1TCC 209
TURN    14  B4 THR B 158  SER B 161     TYPE II                         1TCC 210
TURN    15  B5 SER B 184  ASP B 187     TYPE I                          1TCC 211
TURN    16  B6 SER B 197  ASP B 200     TYPE III                        1TCC 212
TURN    17  B7 LEU B 204  GLY B 207     TYPE II (NO GLY AT I 2)         1TCC 213
TURN    18  B8 GLY B 217  PHE B 220     TYPE I                          1TCC 214
TURN    19  B9 ALA B 263  LEU B 266     TYPE I                          1TCC 215
TURN    20 B10 THR B 310  GLY B 313     TYPE III                        1TCC 216
SSBOND   1 CYS A   22    CYS A   64                                     1TCC 217
SSBOND   2 CYS A  216    CYS A  258                                     1TCC 218
SSBOND   3 CYS A  293    CYS A  311                                     1TCC 219
SSBOND   4 CYS B   22    CYS B   64                                     1TCC 220
SSBOND   5 CYS B  216    CYS B  258                                     1TCC 221
SSBOND   6 CYS B  293    CYS B  311                                     1TCC 222
SITE     1 CTA  3 SER A 105  ASP A 187  HIS A 224                       1TCC 223
SITE     1 CTB  3 SER B 105  ASP B 187  HIS B 224                       1TCC 224
CRYST1   67.000   50.500   86.700  90.00 100.10  90.00 P 21          4  1TCC 225
ORIGX1      1.000000  0.000000  0.000000        0.00000                 1TCC 226
ORIGX2      0.000000  1.000000  0.000000        0.00000                 1TCC 227
ORIGX3      0.000000  0.000000  1.000000        0.00000                 1TCC 228
SCALE1      0.014925  0.000000  0.002659        0.00000                 1TCC 229
SCALE2      0.000000  0.019802  0.000000        0.00000                 1TCC 230
SCALE3      0.000000  0.000000  0.011716        0.00000                 1TCC 231
MTRIX1   1  0.281300  0.935400  0.214100       -4.76610    1            1TCC 232
MTRIX2   1  0.938100 -0.315000  0.144100       -0.25750    1            1TCC 233
MTRIX3   1  0.202200  0.160300 -0.966100       28.25220    1            1TCC 234

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer