1HEADER    LYASE/LYASE/SIGNALING PROTEIN           16-AUG-99   1CS4
2TITLE     COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN
3TITLE    2 ADENYLYL CYCLASE: COMPLEX WITH 2'-DEOXY-ADENOSINE 3'-
4TITLE    3 MONOPHOSPHATE, PYROPHOSPHATE AND MG
5COMPND    MOL_ID: 1;
6COMPND   2 MOLECULE: TYPE V ADENYLATE CYCLASE;
7SOURCE    MOL_ID: 1;
8SOURCE   2 ORGANISM_SCIENTIFIC: CANIS FAMILIARIS;
9KEYWDS    COMPLEX (LYASE/HYDROLASE), HYDROLASE, SIGNAL TRANSDUCING
10KEYWDS   2 PROTEIN, CYCLASE, EFFECTOR ENZYME, LYASE/HYDROLASE COMPLEX
11EXPDTA    X-RAY DIFFRACTION
12AUTHOR    J.J.G.TESMER,C.A.DESSAUER,R.K.SUNAHARA,R.A.JOHNSON,
13AUTHOR   2 A.G.GILMAN,S.R.SPRANG
14REVDAT   2   21-MAR-01 1CS4    3       HETATM REMARK
15REVDAT   1   10-JAN-01 1CS4    0
16JRNL        AUTH   J.J.G.TESMER,C.A.DESSAUER,R.K.SUNAHARA,L.D.MURRAY,
17JRNL        AUTH 2 R.A.JOHNSON,A.G.GILMAN,S.R.SPRANG
18JRNL        TITL   MOLECULAR BASIS FOR P-SITE INHIBITION OF ADENYLYL
19JRNL        TITL 2 CYCLASE
20JRNL        REF    BIOCHEMISTRY                  V.  39 14464 2000
21JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960
22REMARK   1
23REMARK   1 REFERENCE 1
24REMARK   1  AUTH   J.J.G.TESMER,R.K.SUNAHARA,A.G.GILMAN,S.R.SPRANG
25REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CATALYTIC DOMAINS OF
26REMARK   1  TITL 2 ADENYLYL CYCLASE IN A COMPLEX WITH
27REMARK   1  TITL 3 GS(ALPHA)-GTP(GAMMA)S
28REMARK   1  REF    SCIENCE                       V. 278  1907 1997
29REMARK   1  REFN   ASTM SCIEAS  US ISSN 0036-8075
30REMARK   2
31REMARK   2 RESOLUTION. 2.50 ANGSTROMS.
32REMARK 900 RELATED ENTRIES
33REMARK 900 RELATED ID: 1CUL   RELATED DB: PDB
34DBREF  1CS4 A  363   580  SWS    P30803   CYA5_CANFA     363    580
35DBREF  1CS4 B  870  1081  SWS    P26769   CYA2_RAT       870   1081
36DBREF  1CS4 C    1   394  SWS    P04896   GBAS_BOVIN       1    394
37SEQADV 1CS4 MET A  476  SWS  P30803    VAL   476 ENGINEERED
38SEQRES   4 A  225  ALA ASP ILE GLU GLY PHE THR SER LEU ALA SER GLN CYS
39SEQRES   5 A  225  THR ALA GLN GLU LEU VAL MET THR LEU ASN GLU LEU PHE
40SEQRES   6 A  225  ALA ARG PHE ASP LYS LEU ALA ALA GLU ASN HIS CYS LEU
41SEQRES   7 A  225  ARG ILE LYS ILE LEU GLY ASP CYS TYR TYR CYS VAL SER
42HET     MG    396       1
43HET     MG    397       1
44HET     CL    398       1
45HET    GSP   1000      32
46HET    101   1001      22
47HET    FOK   1002      29
48HET    MES   1003      12
49HET    MES   1004      12
50HET    POP   1005       9
51HETNAM      MG MAGNESIUM ION
52HETNAM      CL CHLORIDE ION
53HETNAM     GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE
54HETNAM     101 2'-DEOXY-ADENOSINE 3'-MONOPHOSPHATE
55HETNAM     FOK FORSKOLIN
56HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
57HETNAM     POP PYROPHOSPHATE 2-
58FORMUL   4   MG    2(MG1 2+)
59FORMUL   6   CL    CL1 1-
60FORMUL   7  GSP    C10 H16 N5 O13 P3 S1
61FORMUL   8  101    C10 H14 N5 O6 P1
62FORMUL   9  FOK    C22 H34 O7
63FORMUL  10  MES    2(C6 H13 N1 O4 S1)
64FORMUL  12  POP    H2 O7 P2 2-
65FORMUL  13  HOH   *77(H2 O1)
66HELIX    1   1 GLY A  399  SER A  405  1                                   7
67HELIX    2   2 THR A  408  ASN A  430  1                                  23
68SHEET    1   A 5 LEU A 433  LEU A 438  0
69SHEET    3   A 5 ILE A 384  ILE A 397 -1  N  SER A 391   O  SER A 446
70SHEET    1  A1 7 LEU A 433  LEU A 438  0
71SHEET    3  A1 7 ILE A 384  ILE A 397 -1  N  SER A 391   O  SER A 446
72ATOM    164  N   ASP A 396      51.711 -11.782  62.798  1.00 51.17           N
73ATOM    165  CA  ASP A 396      52.810 -11.644  61.848  1.00 54.45           C
74ATOM    166  C   ASP A 396      54.137 -11.314  62.530  1.00 55.11           C
75ATOM    167  O   ASP A 396      54.175 -10.524  63.469  1.00 55.34           O
76ATOM    168  CB  ASP A 396      52.437 -10.555  60.831  1.00 57.50           C
77ATOM    169  CG  ASP A 396      53.460 -10.391  59.729  1.00 61.38           C
78ATOM    170  OD1 ASP A 396      54.316  -9.485  59.841  1.00 65.55           O
79ATOM    171  OD2 ASP A 396      53.390 -11.146  58.736  1.00 63.68           O
80ATOM    172  N   ILE A 397      55.216 -11.941  62.066  1.00 57.14           N
81ATOM    173  CA  ILE A 397      56.546 -11.705  62.624  1.00 59.46           C
82ATOM    174  C   ILE A 397      57.020 -10.305  62.230  1.00 60.12           C
83ATOM    175  O   ILE A 397      56.963  -9.927  61.060  1.00 59.12           O
84ATOM    176  CB  ILE A 397      57.583 -12.722  62.094  1.00 60.84           C
85ATOM    177  CG1 ILE A 397      57.184 -14.163  62.447  1.00 63.12           C
86ATOM    178  CG2 ILE A 397      58.975 -12.384  62.632  1.00 61.24           C
87ATOM    179  CD1 ILE A 397      57.408 -14.554  63.895  1.00 63.92           C
88ATOM    180  N   GLU A 398      57.492  -9.548  63.212  1.00 60.23           N
89ATOM    181  CA  GLU A 398      57.975  -8.198  62.971  1.00 62.14           C
90ATOM    182  C   GLU A 398      59.401  -8.277  62.424  1.00 60.59           C
91ATOM    183  O   GLU A 398      60.244  -8.972  62.987  1.00 61.84           O
92ATOM    184  CB  GLU A 398      57.917  -7.386  64.272  1.00 65.47           C
93ATOM    185  CG  GLU A 398      58.037  -5.874  64.091  1.00 70.25           C
94ATOM    186  CD  GLU A 398      57.588  -5.089  65.324  1.00 72.94           C
95ATOM    187  OE1 GLU A 398      58.262  -5.175  66.377  1.00 70.76           O
96ATOM    188  OE2 GLU A 398      56.555  -4.380  65.232  1.00 74.36           O
97ATOM    189  N   GLY A 399      59.642  -7.608  61.298  1.00 57.58           N
98ATOM    190  CA  GLY A 399      60.956  -7.615  60.681  1.00 56.14           C
99ATOM    191  C   GLY A 399      61.452  -8.993  60.265  1.00 58.03           C
100ATOM    192  O   GLY A 399      62.620  -9.322  60.480  1.00 57.47           O
101ATOM    193  N   PHE A 400      60.576  -9.789  59.649  1.00 58.00           N
102ATOM    194  CA  PHE A 400      60.914 -11.143  59.200  1.00 58.07           C
103ATOM    195  C   PHE A 400      61.995 -11.219  58.117  1.00 58.57           C
104ATOM    196  O   PHE A 400      62.862 -12.091  58.161  1.00 59.44           O
105ATOM    197  CB  PHE A 400      59.657 -11.881  58.734  1.00 59.18           C
106ATOM    198  CG  PHE A 400      59.900 -13.316  58.322  1.00 58.53           C
107ATOM    199  CD1 PHE A 400      60.377 -14.251  59.237  1.00 57.59           C
108ATOM    200  CD2 PHE A 400      59.613 -13.736  57.024  1.00 57.95           C
109ATOM    201  CE1 PHE A 400      60.557 -15.583  58.864  1.00 59.98           C
110ATOM    202  CE2 PHE A 400      59.790 -15.063  56.643  1.00 58.52           C
111ATOM    203  CZ  PHE A 400      60.261 -15.990  57.563  1.00 58.10           C
112ATOM    204  N   THR A 401      61.921 -10.341  57.123  1.00 58.08           N
113ATOM    205  CA  THR A 401      62.916 -10.337  56.055  1.00 56.79           C
114ATOM    206  C   THR A 401      64.304 -10.010  56.634  1.00 57.24           C
115ATOM    207  O   THR A 401      65.320 -10.547  56.187  1.00 55.16           O
116ATOM    208  CB  THR A 401      62.528  -9.348  54.936  1.00 55.59           C
117ATOM    209  OG1 THR A 401      61.204  -9.650  54.473  1.00 54.91           O
118ATOM    210  CG2 THR A 401      63.495  -9.452  53.764  1.00 53.04           C
119ATOM    211  N   SER A 402      64.323  -9.169  57.667  1.00 56.99           N
120ATOM    212  CA  SER A 402      65.558  -8.772  58.342  1.00 58.09           C
121ATOM    213  C   SER A 402      66.138  -9.957  59.121  1.00 59.79           C
122ATOM    214  O   SER A 402      67.341 -10.241  59.058  1.00 58.14           O
123ATOM    215  CB  SER A 402      65.260  -7.617  59.306  1.00 58.37           C
124ATOM    216  OG  SER A 402      66.421  -7.159  59.974  1.00 55.94           O
125ATOM    217  N   LEU A 403      65.253 -10.655  59.828  1.00 60.85           N
126ATOM    218  CA  LEU A 403      65.598 -11.807  60.650  1.00 61.09           C
127ATOM    219  C   LEU A 403      66.147 -12.991  59.843  1.00 62.81           C
128ATOM    220  O   LEU A 403      67.235 -13.495  60.131  1.00 61.33           O
129ATOM    221  CB  LEU A 403      64.370 -12.220  61.457  1.00 60.24           C
130ATOM    222  CG  LEU A 403      64.530 -13.262  62.555  1.00 63.33           C
131ATOM    223  CD1 LEU A 403      65.692 -12.895  63.470  1.00 65.31           C
132ATOM    224  CD2 LEU A 403      63.232 -13.353  63.340  1.00 64.51           C
133ATOM    225  N   ALA A 404      65.398 -13.415  58.826  1.00 65.20           N
134ATOM    226  CA  ALA A 404      65.787 -14.532  57.960  1.00 68.38           C
135ATOM    227  C   ALA A 404      67.007 -14.213  57.094  1.00 70.82           C
136ATOM    228  O   ALA A 404      67.607 -15.105  56.479  1.00 71.80           O
137ATOM    229  CB  ALA A 404      64.616 -14.944  57.079  1.00 66.92           C
138ATOM    230  N   SER A 405      67.354 -12.932  57.042  1.00 72.71           N
139ATOM    231  CA  SER A 405      68.485 -12.447  56.265  1.00 73.57           C
140ATOM    232  C   SER A 405      69.791 -12.628  57.045  1.00 75.23           C
141ATOM    233  O   SER A 405      70.878 -12.568  56.467  1.00 76.00           O
142ATOM    234  CB  SER A 405      68.265 -10.966  55.936  1.00 72.32           C
143ATOM    235  OG  SER A 405      69.156 -10.499  54.945  1.00 70.40           O
144ATOM    236  N   GLN A 406      69.675 -12.875  58.350  1.00 76.83           N
145ATOM    237  CA  GLN A 406      70.837 -13.048  59.223  1.00 78.12           C
146ATOM    238  C   GLN A 406      71.259 -14.494  59.465  1.00 80.42           C
147ATOM    239  O   GLN A 406      72.391 -14.881  59.145  1.00 81.68           O
148ATOM    240  CB  GLN A 406      70.597 -12.354  60.557  1.00 75.97           C
149ATOM    241  CG  GLN A 406      70.317 -10.879  60.416  1.00 78.05           C
150ATOM    242  CD  GLN A 406      70.140 -10.212  61.750  1.00 78.52           C
151ATOM    243  OE1 GLN A 406      71.102 -10.029  62.490  1.00 78.65           O
152ATOM    244  NE2 GLN A 406      68.902  -9.859  62.080  1.00 81.68           N
153ATOM    245  N   CYS A 407      70.360 -15.280  60.051  1.00 81.23           N
154ATOM    246  CA  CYS A 407      70.641 -16.682  60.341  1.00 81.90           C
155ATOM    247  C   CYS A 407      70.484 -17.589  59.118  1.00 80.94           C
156ATOM    248  O   CYS A 407      69.924 -17.187  58.095  1.00 79.51           O
157ATOM    249  CB  CYS A 407      69.767 -17.180  61.498  1.00 83.37           C
158ATOM    250  SG  CYS A 407      67.992 -17.169  61.165  1.00 84.69           S
159ATOM    251  N   THR A 408      70.999 -18.811  59.236  1.00 80.19           N
160ATOM    252  CA  THR A 408      70.929 -19.796  58.161  1.00 79.55           C
161ATOM    253  C   THR A 408      69.486 -20.243  57.912  1.00 78.78           C
162ATOM    254  O   THR A 408      68.644 -20.148  58.803  1.00 78.45           O
163ATOM    255  CB  THR A 408      71.833 -21.015  58.462  1.00 79.73           C
164ATOM    256  OG1 THR A 408      71.645 -22.019  57.457  1.00 81.02           O
165ATOM    257  CG2 THR A 408      71.529 -21.596  59.844  1.00 79.82           C
166ATOM    258  N   ALA A 409      69.200 -20.711  56.699  1.00 77.92           N
167ATOM    259  CA  ALA A 409      67.852 -21.159  56.345  1.00 77.59           C
168ATOM    260  C   ALA A 409      67.379 -22.335  57.200  1.00 78.55           C
169ATOM    261  O   ALA A 409      66.180 -22.525  57.402  1.00 79.07           O
170ATOM    262  CB  ALA A 409      67.782 -21.510  54.870  1.00 77.63           C
171ATOM    263  N   GLN A 410      68.334 -23.115  57.700  1.00 79.69           N
172ATOM    264  CA  GLN A 410      68.060 -24.276  58.545  1.00 79.08           C
173ATOM    265  C   GLN A 410      67.537 -23.818  59.908  1.00 77.23           C
174ATOM    266  O   GLN A 410      66.458 -24.222  60.329  1.00 76.62           O
175ATOM    267  CB  GLN A 410      69.348 -25.102  58.711  1.00 82.32           C
176ATOM    268  CG  GLN A 410      69.228 -26.383  59.543  1.00 84.09           C
177ATOM    269  CD  GLN A 410      70.580 -27.067  59.772  1.00 88.07           C
178ATOM    270  OE1 GLN A 410      71.637 -26.497  59.490  1.00 87.61           O
179ATOM    271  NE2 GLN A 410      70.548 -28.292  60.291  1.00 88.14           N
180ATOM    272  N   GLU A 411      68.299 -22.945  60.565  1.00 76.61           N
181ATOM    273  CA  GLU A 411      67.958 -22.399  61.881  1.00 75.61           C
182ATOM    274  C   GLU A 411      66.599 -21.695  61.903  1.00 72.48           C
183ATOM    275  O   GLU A 411      65.829 -21.860  62.850  1.00 70.94           O
184ATOM    276  CB  GLU A 411      69.059 -21.429  62.325  1.00 80.11           C
185ATOM    277  CG  GLU A 411      68.889 -20.815  63.707  1.00 85.62           C
186ATOM    278  CD  GLU A 411      69.999 -19.818  64.045  1.00 90.46           C
187ATOM    279  OE1 GLU A 411      71.161 -20.037  63.621  1.00 91.03           O
188ATOM    280  OE2 GLU A 411      69.706 -18.811  64.731  1.00 92.20           O
189ATOM    281  N   LEU A 412      66.318 -20.917  60.856  1.00 69.31           N
190ATOM    282  CA  LEU A 412      65.061 -20.174  60.726  1.00 67.35           C
191ATOM    283  C   LEU A 412      63.840 -21.084  60.777  1.00 66.69           C
192ATOM    284  O   LEU A 412      62.876 -20.805  61.493  1.00 64.91           O
193ATOM    285  CB  LEU A 412      65.037 -19.374  59.418  1.00 66.39           C
194ATOM    286  CG  LEU A 412      63.717 -18.675  59.065  1.00 67.30           C
195ATOM    287  CD1 LEU A 412      63.542 -17.406  59.889  1.00 67.03           C
196ATOM    288  CD2 LEU A 412      63.656 -18.357  57.578  1.00 68.24           C
197ATOM    289  N   VAL A 413      63.884 -22.165  60.004  1.00 65.47           N
198ATOM    290  CA  VAL A 413      62.782 -23.113  59.948  1.00 65.09           C
199ATOM    291  C   VAL A 413      62.579 -23.846  61.275  1.00 66.81           C
200ATOM    292  O   VAL A 413      61.457 -24.212  61.621  1.00 65.95           O
201ATOM    293  CB  VAL A 413      62.948 -24.092  58.778  1.00 64.62           C
202ATOM    294  CG1 VAL A 413      61.754 -25.020  58.682  1.00 64.48           C
203ATOM    295  CG2 VAL A 413      63.109 -23.316  57.481  1.00 64.55           C
204ATOM    296  N   MET A 414      63.658 -24.040  62.028  1.00 69.09           N
205ATOM    297  CA  MET A 414      63.557 -24.704  63.325  1.00 71.89           C
206ATOM    298  C   MET A 414      62.815 -23.776  64.288  1.00 70.25           C
207ATOM    299  O   MET A 414      61.939 -24.216  65.034  1.00 70.70           O
208ATOM    300  CB  MET A 414      64.945 -25.045  63.881  1.00 76.81           C
209ATOM    301  CG  MET A 414      65.735 -26.040  63.042  1.00 83.62           C
210ATOM    302  SD  MET A 414      67.404 -26.358  63.684  1.00 91.35           S
211ATOM    303  CE  MET A 414      67.448 -28.177  63.619  1.00 92.43           C
212ATOM    304  N   THR A 415      63.153 -22.488  64.234  1.00 68.43           N
213ATOM    305  CA  THR A 415      62.537 -21.466  65.081  1.00 66.56           C
214ATOM    306  C   THR A 415      61.056 -21.288  64.753  1.00 66.36           C
215ATOM    307  O   THR A 415      60.236 -21.063  65.641  1.00 65.56           O
216ATOM    308  CB  THR A 415      63.253 -20.111  64.923  1.00 65.51           C
217ATOM    309  OG1 THR A 415      64.628 -20.247  65.302  1.00 65.76           O
218ATOM    310  CG2 THR A 415      62.605 -19.060  65.794  1.00 66.85           C
219ATOM    311  N   LEU A 416      60.729 -21.379  63.467  1.00 66.65           N
220ATOM    312  CA  LEU A 416      59.353 -21.239  62.999  1.00 65.89           C
221ATOM    313  C   LEU A 416      58.514 -22.477  63.305  1.00 66.53           C
222ATOM    314  O   LEU A 416      57.352 -22.357  63.690  1.00 67.40           O
223ATOM    315  CB  LEU A 416      59.321 -20.954  61.496  1.00 64.04           C
224ATOM    316  CG  LEU A 416      59.134 -19.521  60.996  1.00 63.11           C
225ATOM    317  CD1 LEU A 416      60.079 -18.547  61.678  1.00 64.09           C
226ATOM    318  CD2 LEU A 416      59.338 -19.507  59.494  1.00 63.76           C
227ATOM    319  N   ASN A 417      59.099 -23.660  63.120  1.00 67.04           N
228ATOM    320  CA  ASN A 417      58.397 -24.918  63.376  1.00 67.09           C
229ATOM    321  C   ASN A 417      58.130 -25.087  64.863  1.00 66.60           C
230ATOM    322  O   ASN A 417      57.105 -25.634  65.258  1.00 66.98           O
231ATOM    323  CB  ASN A 417      59.187 -26.114  62.839  1.00 68.26           C
232ATOM    324  CG  ASN A 417      58.359 -27.393  62.789  1.00 69.42           C
233ATOM    325  OD1 ASN A 417      57.128 -27.354  62.740  1.00 71.71           O
234ATOM    326  ND2 ASN A 417      59.037 -28.534  62.786  1.00 69.52           N
235ATOM    327  N   GLU A 418      59.066 -24.621  65.681  1.00 66.84           N
236ATOM    328  CA  GLU A 418      58.928 -24.697  67.125  1.00 67.28           C
237ATOM    329  C   GLU A 418      57.761 -23.803  67.536  1.00 65.76           C
238ATOM    330  O   GLU A 418      56.918 -24.183  68.346  1.00 66.20           O
239ATOM    331  CB  GLU A 418      60.225 -24.219  67.790  1.00 69.59           C
240ATOM    332  CG  GLU A 418      60.267 -24.352  69.309  1.00 76.09           C
241ATOM    333  CD  GLU A 418      60.448 -25.790  69.791  1.00 79.64           C
242ATOM    334  OE1 GLU A 418      61.316 -26.009  70.666  1.00 81.84           O
243ATOM    335  OE2 GLU A 418      59.724 -26.695  69.313  1.00 78.13           O
244ATOM    336  N   LEU A 419      57.685 -22.642  66.897  1.00 64.54           N
245ATOM    337  CA  LEU A 419      56.649 -21.659  67.167  1.00 62.87           C
246ATOM    338  C   LEU A 419      55.259 -22.040  66.645  1.00 61.83           C
247ATOM    339  O   LEU A 419      54.289 -22.033  67.405  1.00 62.63           O
248ATOM    340  CB  LEU A 419      57.079 -20.307  66.603  1.00 63.90           C
249ATOM    341  CG  LEU A 419      56.228 -19.079  66.913  1.00 66.74           C
250ATOM    342  CD1 LEU A 419      56.266 -18.792  68.409  1.00 66.71           C
251ATOM    343  CD2 LEU A 419      56.750 -17.883  66.120  1.00 66.52           C
252ATOM    344  N   PHE A 420      55.163 -22.387  65.362  1.00 58.95           N
253ATOM    345  CA  PHE A 420      53.872 -22.732  64.761  1.00 57.02           C
254ATOM    346  C   PHE A 420      53.251 -24.059  65.199  1.00 56.61           C
255ATOM    347  O   PHE A 420      52.045 -24.261  65.047  1.00 53.15           O
256ATOM    348  CB  PHE A 420      53.908 -22.603  63.234  1.00 56.63           C
257ATOM    349  CG  PHE A 420      54.194 -21.206  62.746  1.00 55.74           C
258ATOM    350  CD1 PHE A 420      55.015 -20.999  61.645  1.00 57.12           C
259ATOM    351  CD2 PHE A 420      53.660 -20.098  63.394  1.00 56.12           C
260ATOM    352  CE1 PHE A 420      55.302 -19.709  61.198  1.00 56.66           C
261ATOM    353  CE2 PHE A 420      53.941 -18.805  62.954  1.00 54.98           C
262ATOM    354  CZ  PHE A 420      54.762 -18.613  61.856  1.00 54.24           C
263ATOM    355  N   ALA A 421      54.071 -24.973  65.713  1.00 57.27           N
264ATOM    356  CA  ALA A 421      53.562 -26.258  66.189  1.00 57.22           C
265ATOM    357  C   ALA A 421      52.740 -25.985  67.451  1.00 58.05           C
266ATOM    358  O   ALA A 421      51.617 -26.486  67.599  1.00 57.54           O
267ATOM    359  CB  ALA A 421      54.708 -27.206  66.484  1.00 58.02           C
268ATOM    360  N   ARG A 422      53.299 -25.156  68.333  1.00 57.10           N
269ATOM    361  CA  ARG A 422      52.633 -24.764  69.566  1.00 58.40           C
270ATOM    362  C   ARG A 422      51.337 -24.020  69.244  1.00 58.87           C
271ATOM    363  O   ARG A 422      50.294 -24.299  69.838  1.00 60.99           O
272ATOM    364  CB  ARG A 422      53.542 -23.866  70.403  1.00 60.84           C
273ATOM    365  CG  ARG A 422      54.852 -24.518  70.776  1.00 67.03           C
274ATOM    366  CD  ARG A 422      55.693 -23.648  71.695  1.00 70.54           C
275ATOM    367  NE  ARG A 422      57.063 -24.156  71.784  1.00 78.36           N
276ATOM    368  CZ  ARG A 422      57.564 -24.828  72.820  1.00 80.58           C
277ATOM    369  NH1 ARG A 422      56.809 -25.080  73.885  1.00 82.01           N
278ATOM    370  NH2 ARG A 422      58.821 -25.260  72.784  1.00 79.95           N
279ATOM    371  N   PHE A 423      51.400 -23.080  68.302  1.00 56.49           N
280ATOM    372  CA  PHE A 423      50.218 -22.318  67.908  1.00 56.22           C
281ATOM    373  C   PHE A 423      49.107 -23.257  67.432  1.00 58.41           C
282ATOM    374  O   PHE A 423      47.934 -23.086  67.789  1.00 56.37           O
283ATOM    375  CB  PHE A 423      50.540 -21.335  66.776  1.00 53.62           C
284ATOM    376  CG  PHE A 423      51.338 -20.131  67.198  1.00 51.59           C
285ATOM    377  CD1 PHE A 423      51.973 -20.077  68.433  1.00 55.51           C
286ATOM    378  CD2 PHE A 423      51.467 -19.048  66.336  1.00 49.59           C
287ATOM    379  CE1 PHE A 423      52.730 -18.954  68.801  1.00 54.22           C
288ATOM    380  CE2 PHE A 423      52.214 -17.930  66.691  1.00 49.52           C
289ATOM    381  CZ  PHE A 423      52.847 -17.880  67.922  1.00 51.42           C
290ATOM    382  N   ASP A 424      49.481 -24.250  66.628  1.00 59.69           N
291ATOM    383  CA  ASP A 424      48.508 -25.202  66.101  1.00 61.34           C
292ATOM    384  C   ASP A 424      47.809 -26.013  67.198  1.00 62.33           C
293ATOM    385  O   ASP A 424      46.640 -26.375  67.051  1.00 61.80           O
294ATOM    386  CB  ASP A 424      49.129 -26.105  65.021  1.00 62.07           C
295ATOM    387  CG  ASP A 424      49.233 -25.419  63.644  1.00 61.74           C
296ATOM    388  OD1 ASP A 424      49.891 -25.982  62.740  1.00 59.30           O
297ATOM    389  OD2 ASP A 424      48.650 -24.330  63.452  1.00 60.36           O
298ATOM    390  N   LYS A 425      48.518 -26.270  68.300  1.00 63.53           N
299ATOM    391  CA  LYS A 425      47.964 -27.017  69.435  1.00 64.76           C
300ATOM    392  C   LYS A 425      47.063 -26.091  70.264  1.00 64.55           C
301ATOM    393  O   LYS A 425      45.979 -26.488  70.700  1.00 63.51           O
302ATOM    394  CB  LYS A 425      49.085 -27.609  70.298  1.00 66.02           C
303ATOM    395  CG  LYS A 425      49.942 -28.649  69.575  1.00 69.79           C
304ATOM    396  CD  LYS A 425      51.268 -28.888  70.291  1.00 72.86           C
305ATOM    397  CE  LYS A 425      52.258 -29.648  69.403  1.00 75.05           C
306ATOM    398  NZ  LYS A 425      53.660 -29.608  69.934  1.00 73.84           N
307ATOM    399  N   LEU A 426      47.515 -24.851  70.451  1.00 64.14           N
308ATOM    400  CA  LEU A 426      46.761 -23.840  71.195  1.00 62.66           C
309ATOM    401  C   LEU A 426      45.469 -23.511  70.460  1.00 62.89           C
310ATOM    402  O   LEU A 426      44.500 -23.067  71.068  1.00 65.31           O
311ATOM    403  CB  LEU A 426      47.582 -22.558  71.337  1.00 60.88           C
312ATOM    404  CG  LEU A 426      48.880 -22.624  72.136  1.00 59.87           C
313ATOM    405  CD1 LEU A 426      49.701 -21.376  71.896  1.00 59.27           C
314ATOM    406  CD2 LEU A 426      48.581 -22.796  73.611  1.00 59.59           C
315ATOM    407  N   ALA A 427      45.472 -23.704  69.143  1.00 62.85           N
316ATOM    408  CA  ALA A 427      44.301 -23.431  68.318  1.00 62.31           C
317ATOM    409  C   ALA A 427      43.199 -24.436  68.594  1.00 62.78           C
318ATOM    410  O   ALA A 427      42.021 -24.087  68.587  1.00 63.29           O
319ATOM    411  CB  ALA A 427      44.671 -23.443  66.845  1.00 62.07           C
320ATOM    412  N   ALA A 428      43.591 -25.687  68.830  1.00 64.92           N
321ATOM    413  CA  ALA A 428      42.643 -26.762  69.122  1.00 65.33           C
322ATOM    414  C   ALA A 428      42.016 -26.570  70.503  1.00 65.78           C
323ATOM    415  O   ALA A 428      40.825 -26.832  70.693  1.00 64.54           O
324ATOM    416  CB  ALA A 428      43.332 -28.117  69.032  1.00 65.35           C
325ATOM    417  N   GLU A 429      42.830 -26.116  71.457  1.00 67.26           N
326ATOM    418  CA  GLU A 429      42.376 -25.864  72.828  1.00 68.66           C
327ATOM    419  C   GLU A 429      41.382 -24.706  72.875  1.00 67.80           C
328ATOM    420  O   GLU A 429      40.354 -24.787  73.543  1.00 69.58           O
329ATOM    421  CB  GLU A 429      43.562 -25.524  73.739  1.00 69.06           C
330ATOM    422  CG  GLU A 429      44.494 -26.688  74.050  1.00 71.68           C
331ATOM    423  CD  GLU A 429      45.709 -26.275  74.876  1.00 73.62           C
332ATOM    424  OE1 GLU A 429      46.624 -27.114  75.040  1.00 71.45           O
333ATOM    425  OE2 GLU A 429      45.758 -25.117  75.360  1.00 75.83           O
334ATOM    426  N   ASN A 430      41.691 -23.642  72.140  1.00 66.29           N
335ATOM    427  CA  ASN A 430      40.861 -22.447  72.110  1.00 63.46           C
336ATOM    428  C   ASN A 430      39.696 -22.419  71.125  1.00 62.93           C
337ATOM    429  O   ASN A 430      39.073 -21.383  70.939  1.00 63.70           O
338ATOM    430  CB  ASN A 430      41.741 -21.211  71.962  1.00 61.34           C
339ATOM    431  CG  ASN A 430      42.679 -21.034  73.134  1.00 61.28           C
340ATOM    432  OD1 ASN A 430      42.239 -20.902  74.274  1.00 63.96           O
341ATOM    433  ND2 ASN A 430      43.977 -21.042  72.866  1.00 60.75           N
342ATOM    434  N   HIS A 431      39.387 -23.557  70.516  1.00 64.80           N
343ATOM    435  CA  HIS A 431      38.273 -23.666  69.565  1.00 67.70           C
344ATOM    436  C   HIS A 431      38.429 -22.828  68.285  1.00 65.99           C
345ATOM    437  O   HIS A 431      37.444 -22.339  67.725  1.00 63.95           O
346ATOM    438  CB  HIS A 431      36.936 -23.345  70.252  1.00 72.64           C
347ATOM    439  CG  HIS A 431      36.796 -23.944  71.617  1.00 78.81           C
348ATOM    440  ND1 HIS A 431      36.841 -25.303  71.843  1.00 81.38           N
349ATOM    441  CD2 HIS A 431      36.647 -23.363  72.832  1.00 81.03           C
350ATOM    442  CE1 HIS A 431      36.731 -25.534  73.140  1.00 83.56           C
351ATOM    443  NE2 HIS A 431      36.612 -24.374  73.763  1.00 84.39           N
352ATOM    444  N   CYS A 432      39.670 -22.699  67.819  1.00 64.72           N
353ATOM    445  CA  CYS A 432      39.985 -21.941  66.611  1.00 63.54           C
354ATOM    446  C   CYS A 432      40.455 -22.855  65.494  1.00 60.43           C
355ATOM    447  O   CYS A 432      41.248 -23.766  65.728  1.00 62.51           O
356ATOM    448  CB  CYS A 432      41.102 -20.932  66.889  1.00 66.14           C
357ATOM    449  SG  CYS A 432      40.628 -19.507  67.869  1.00 71.63           S
358ATOM    450  N   LEU A 433      39.979 -22.602  64.281  1.00 55.75           N
359ATOM    451  CA  LEU A 433      40.396 -23.389  63.128  1.00 52.43           C
360ATOM    452  C   LEU A 433      41.465 -22.618  62.378  1.00 50.87           C
361ATOM    453  O   LEU A 433      41.193 -21.545  61.842  1.00 51.07           O
362ATOM    454  CB  LEU A 433      39.219 -23.670  62.195  1.00 49.96           C
363ATOM    455  CG  LEU A 433      39.539 -24.291  60.830  1.00 50.69           C
364ATOM    456  CD1 LEU A 433      40.280 -25.624  60.979  1.00 50.91           C
365ATOM    457  CD2 LEU A 433      38.263 -24.475  60.027  1.00 46.25           C
366ATOM    458  N   ARG A 434      42.686 -23.145  62.362  1.00 49.08           N
367ATOM    459  CA  ARG A 434      43.772 -22.480  61.650  1.00 46.09           C
368ATOM    460  C   ARG A 434      43.575 -22.547  60.137  1.00 45.45           C
369ATOM    461  O   ARG A 434      43.069 -23.540  59.607  1.00 42.02           O
370ATOM    462  CB  ARG A 434      45.124 -23.052  62.050  1.00 44.77           C
371ATOM    463  CG  ARG A 434      46.289 -22.279  61.479  1.00 44.40           C
372ATOM    464  CD  ARG A 434      46.791 -22.911  60.212  1.00 44.46           C
373ATOM    465  NE  ARG A 434      47.907 -23.809  60.473  1.00 46.69           N
374ATOM    466  CZ  ARG A 434      48.341 -24.729  59.622  1.00 47.51           C
375ATOM    467  NH1 ARG A 434      47.745 -24.889  58.448  1.00 46.99           N
376ATOM    468  NH2 ARG A 434      49.410 -25.452  59.927  1.00 49.60           N
377ATOM    469  N   ILE A 435      43.929 -21.463  59.455  1.00 46.06           N
378ATOM    470  CA  ILE A 435      43.791 -21.405  58.007  1.00 47.94           C
379ATOM    471  C   ILE A 435      45.128 -21.768  57.354  1.00 49.27           C
380ATOM    472  O   ILE A 435      45.316 -22.911  56.925  1.00 50.94           O
381ATOM    473  CB  ILE A 435      43.255 -20.038  57.551  1.00 47.15           C
382ATOM    474  CG1 ILE A 435      41.973 -19.706  58.315  1.00 45.98           C
383ATOM    475  CG2 ILE A 435      42.947 -20.058  56.062  1.00 48.42           C
384ATOM    476  CD1 ILE A 435      40.863 -20.738  58.156  1.00 43.91           C
385ATOM    477  N   LYS A 436      46.066 -20.824  57.308  1.00 48.78           N
386ATOM    478  CA  LYS A 436      47.382 -21.114  56.741  1.00 45.74           C
387ATOM    479  C   LYS A 436      48.551 -20.279  57.227  1.00 44.92           C
388ATOM    480  O   LYS A 436      48.382 -19.355  58.023  1.00 45.05           O
389ATOM    481  CB  LYS A 436      47.364 -21.306  55.217  1.00 47.03           C
390ATOM    482  CG  LYS A 436      46.733 -20.214  54.377  1.00 45.37           C
391ATOM    483  CD  LYS A 436      46.225 -20.811  53.058  1.00 40.72           C
392ATOM    484  CE  LYS A 436      46.260 -19.807  51.913  1.00 44.25           C
393ATOM    485  NZ  LYS A 436      45.622 -20.326  50.664  1.00 45.35           N
394ATOM    486  N   ILE A 437      49.751 -20.706  56.849  1.00 44.66           N
395ATOM    487  CA  ILE A 437      50.969 -20.017  57.239  1.00 45.23           C
396ATOM    488  C   ILE A 437      51.637 -19.439  55.998  1.00 46.08           C
397ATOM    489  O   ILE A 437      52.033 -20.177  55.093  1.00 48.18           O
398ATOM    490  CB  ILE A 437      51.950 -20.971  57.958  1.00 45.87           C
399ATOM    491  CG1 ILE A 437      51.241 -21.704  59.099  1.00 46.15           C
400ATOM    492  CG2 ILE A 437      53.147 -20.193  58.503  1.00 43.43           C
401ATOM    493  CD1 ILE A 437      52.124 -22.722  59.814  1.00 46.81           C
402ATOM    494  N   LEU A 438      51.729 -18.114  55.951  1.00 46.84           N
403ATOM    495  CA  LEU A 438      52.348 -17.415  54.830  1.00 44.42           C
404ATOM    496  C   LEU A 438      53.758 -16.989  55.211  1.00 44.90           C
405ATOM    497  O   LEU A 438      54.061 -15.795  55.283  1.00 42.12           O
406ATOM    498  CB  LEU A 438      51.507 -16.200  54.427  1.00 41.59           C
407ATOM    499  CG  LEU A 438      50.063 -16.485  54.001  1.00 42.78           C
408ATOM    500  CD1 LEU A 438      49.345 -15.182  53.690  1.00 41.92           C
409ATOM    501  CD2 LEU A 438      49.993 -17.430  52.810  1.00 39.08           C
410ATOM    502  N   GLY A 439      54.619 -17.980  55.437  1.00 46.64           N
411ATOM    503  CA  GLY A 439      55.996 -17.717  55.814  1.00 48.31           C
412ATOM    504  C   GLY A 439      56.099 -17.326  57.273  1.00 49.55           C
413ATOM    505  O   GLY A 439      56.500 -18.130  58.108  1.00 50.85           O
414ATOM    506  N   ASP A 440      55.690 -16.096  57.569  1.00 51.02           N
415ATOM    507  CA  ASP A 440      55.712 -15.540  58.917  1.00 50.96           C
416ATOM    508  C   ASP A 440      54.334 -15.024  59.352  1.00 50.15           C
417ATOM    509  O   ASP A 440      54.193 -14.464  60.438  1.00 51.63           O
418ATOM    510  CB  ASP A 440      56.724 -14.394  58.985  1.00 51.43           C
419ATOM    511  CG  ASP A 440      56.280 -13.162  58.196  1.00 55.29           C
420ATOM    512  OD1 ASP A 440      56.528 -12.030  58.669  1.00 57.12           O
421ATOM    513  OD2 ASP A 440      55.685 -13.319  57.108  1.00 52.55           O
422ATOM    514  N   CYS A 441      53.333 -15.191  58.493  1.00 49.26           N
423ATOM    515  CA  CYS A 441      51.971 -14.737  58.775  1.00 49.62           C
424ATOM    516  C   CYS A 441      51.077 -15.923  59.132  1.00 48.96           C
425ATOM    517  O   CYS A 441      50.803 -16.789  58.301  1.00 50.50           O
426ATOM    518  CB  CYS A 441      51.409 -13.972  57.565  1.00 51.82           C
427ATOM    519  SG  CYS A 441      49.727 -13.277  57.723  1.00 54.53           S
428TER    5650      LEU A 388
429HETATM 5651 MG    MG   396      21.268   2.687  30.885  1.00 42.93          MG
430HETATM 5652 MG    MG   397      56.525  -9.697  58.914  1.00 46.49          MG
431HETATM 5653 CL    CL   398      24.138   0.155  20.056  1.00 39.10          CL
432HETATM 5654  PG  GSP  1000      23.652   3.086  28.951  1.00 49.34           P
433HETATM 5655  O3B GSP  1000      22.508   3.216  27.969  1.00 40.31           O
434HETATM 5656  S1G GSP  1000      25.038   4.394  28.744  1.00 56.58           S
435HETATM 5657  O2G GSP  1000      23.111   3.286  30.325  1.00 53.03           O
436HETATM 5658  O3G GSP  1000      24.387   1.832  28.647  1.00 48.74           O
437HETATM 5659  PB  GSP  1000      21.138   2.622  27.791  1.00 35.52           P
438HETATM 5660  O1B GSP  1000      21.248   1.472  26.859  1.00 40.21           O
439HETATM 5661  O2B GSP  1000      20.552   2.401  29.131  1.00 35.64           O
440HETATM 5662  PA  GSP  1000      19.076   4.412  27.420  1.00 29.38           P
441HETATM 5663  O1A GSP  1000      18.040   3.406  27.751  1.00 32.23           O
442HETATM 5664  O2A GSP  1000      19.382   5.499  28.377  1.00 34.35           O
443HETATM 5665  O3A GSP  1000      20.349   3.694  27.102  1.00 36.36           O
444HETATM 5666  O5* GSP  1000      18.663   5.093  26.040  1.00 31.37           O
445HETATM 5667  C5* GSP  1000      19.357   6.237  25.552  1.00 31.94           C
446HETATM 5668  C4* GSP  1000      18.382   7.282  25.060  1.00 33.17           C
447HETATM 5669  O4* GSP  1000      17.725   6.848  23.844  1.00 35.89           O
448HETATM 5670  C3* GSP  1000      17.265   7.647  26.035  1.00 35.73           C
449HETATM 5671  O3* GSP  1000      17.079   9.058  26.012  1.00 35.05           O
450HETATM 5672  C2* GSP  1000      16.051   6.941  25.455  1.00 36.34           C
451HETATM 5673  O2* GSP  1000      14.824   7.588  25.710  1.00 41.09           O
452HETATM 5674  C1* GSP  1000      16.317   6.966  23.969  1.00 34.58           C
453HETATM 5675  N9  GSP  1000      15.707   5.829  23.288  1.00 34.26           N
454HETATM 5676  C8  GSP  1000      15.811   4.517  23.670  1.00 33.81           C
455HETATM 5677  N7  GSP  1000      15.158   3.701  22.890  1.00 33.38           N
456HETATM 5678  C5  GSP  1000      14.589   4.523  21.926  1.00 31.82           C
457HETATM 5679  C6  GSP  1000      13.783   4.195  20.821  1.00 28.04           C
458HETATM 5680  O6  GSP  1000      13.402   3.087  20.456  1.00 33.22           O
459HETATM 5681  N1  GSP  1000      13.414   5.316  20.106  1.00 28.68           N
460HETATM 5682  C2  GSP  1000      13.770   6.599  20.413  1.00 33.38           C
461HETATM 5683  N2  GSP  1000      13.284   7.553  19.591  1.00 33.04           N
462HETATM 5684  N3  GSP  1000      14.537   6.928  21.448  1.00 35.65           N
463HETATM 5685  C4  GSP  1000      14.910   5.841  22.158  1.00 33.16           C
464HETATM 5686  P   101  1001      55.023 -10.382  55.260  1.00 57.15           P
465HETATM 5687  O1P 101  1001      56.106  -9.960  56.176  1.00 56.63           O
466HETATM 5688  O2P 101  1001      53.931  -9.426  54.936  1.00 58.99           O
467HETATM 5689  O3P 101  1001      54.402 -11.615  55.816  1.00 57.14           O
468HETATM 5690  O5* 101  1001      59.690 -12.066  53.734  1.00 54.73           O
469HETATM 5691  C5* 101  1001      59.117 -11.254  52.717  1.00 49.20           C
470HETATM 5692  C4* 101  1001      57.649 -11.579  52.560  1.00 51.66           C
471HETATM 5693  O4* 101  1001      57.511 -12.868  51.904  1.00 46.96           O
472HETATM 5694  C3* 101  1001      56.880 -11.674  53.885  1.00 52.57           C
473HETATM 5695  O3* 101  1001      55.668 -10.900  53.867  1.00 56.54           O
474HETATM 5696  C2* 101  1001      56.575 -13.157  54.018  1.00 48.44           C
475HETATM 5697  C1* 101  1001      56.527 -13.631  52.575  1.00 45.63           C
476HETATM 5698  N9  101  1001      56.847 -15.055  52.418  1.00 43.32           N
477HETATM 5699  C8  101  1001      58.041 -15.693  52.657  1.00 40.75           C
478HETATM 5700  N7  101  1001      57.975 -16.998  52.536  1.00 39.17           N
479HETATM 5701  C5  101  1001      56.656 -17.232  52.174  1.00 37.85           C
480HETATM 5702  C6  101  1001      55.937 -18.421  51.936  1.00 39.27           C
481HETATM 5703  N6  101  1001      56.471 -19.638  52.043  1.00 38.99           N
482HETATM 5704  N1  101  1001      54.633 -18.310  51.581  1.00 36.43           N
483HETATM 5705  C2  101  1001      54.099 -17.088  51.492  1.00 37.35           C
484HETATM 5706  N3  101  1001      54.671 -15.898  51.709  1.00 38.82           N
485HETATM 5707  C4  101  1001      55.961 -16.044  52.060  1.00 36.23           C
486HETATM 5708  C1  FOK  1002      42.404 -12.814  52.570  1.00 40.03           C
487HETATM 5709  O2  FOK  1002      42.146 -13.905  51.652  1.00 36.59           O
488HETATM 5710  C2  FOK  1002      43.345 -13.346  53.646  1.00 37.70           C
489HETATM 5711  C3  FOK  1002      44.722 -13.704  53.128  1.00 33.13           C
490HETATM 5712  C4  FOK  1002      45.431 -12.480  52.469  1.00 35.66           C
491HETATM 5713  C5  FOK  1002      44.469 -11.938  51.361  1.00 35.93           C
492HETATM 5714  C6  FOK  1002      45.098 -10.866  50.432  1.00 37.17           C
493HETATM 5715  O3  FOK  1002      45.479  -9.692  51.137  1.00 41.60           O
494HETATM 5716  C7  FOK  1002      44.172 -10.545  49.246  1.00 37.25           C
495HETATM 5717  O4  FOK  1002      44.705  -9.418  48.485  1.00 37.43           O
496HETATM 5718  C8  FOK  1002      42.736 -10.141  49.617  1.00 38.76           C
497HETATM 5719  O1  FOK  1002      42.038 -10.149  48.361  1.00 40.53           O
498HETATM 5720  C9  FOK  1002      42.200 -11.309  50.489  1.00 41.39           C
499HETATM 5721  O6  FOK  1002      42.275 -12.455  49.593  1.00 43.23           O
500HETATM 5722  C10 FOK  1002      43.008 -11.601  51.811  1.00 39.11           C
501HETATM 5723  C11 FOK  1002      40.680 -11.078  50.616  1.00 44.36           C
502HETATM 5724  O7  FOK  1002      40.106 -10.945  51.688  1.00 48.77           O
503HETATM 5725  C12 FOK  1002      39.943 -11.046  49.301  1.00 40.67           C
504HETATM 5726  C13 FOK  1002      40.595 -10.085  48.292  1.00 41.47           C
505HETATM 5727  C14 FOK  1002      40.276 -10.620  46.930  1.00 46.69           C
506HETATM 5728  C15 FOK  1002      39.971 -11.751  46.590  1.00 53.22           C
507HETATM 5729  C16 FOK  1002      40.047  -8.685  48.426  1.00 42.42           C
508HETATM 5730  C17 FOK  1002      42.671  -8.737  50.253  1.00 39.67           C
509HETATM 5731  C18 FOK  1002      46.732 -13.026  51.827  1.00 35.74           C
510HETATM 5732  C19 FOK  1002      45.859 -11.483  53.586  1.00 34.48           C
511HETATM 5733  C20 FOK  1002      42.913 -10.426  52.807  1.00 39.44           C
512HETATM 5734  C21 FOK  1002      45.883  -9.553  47.821  1.00 42.15           C
513HETATM 5735  O5  FOK  1002      46.157 -10.520  47.166  1.00 40.91           O
514HETATM 5736  C22 FOK  1002      46.769  -8.315  48.006  1.00 37.08           C
515HETATM 5737  O1  MES  1003      45.676   7.326  49.092  1.00 77.86           O
516HETATM 5738  C2  MES  1003      44.367   6.816  48.900  1.00 75.17           C
517HETATM 5739  C3  MES  1003      44.349   5.317  48.923  1.00 74.42           C
518HETATM 5740  N4  MES  1003      44.832   4.804  50.196  1.00 72.45           N
519HETATM 5741  C5  MES  1003      46.234   5.425  50.473  1.00 73.23           C
520HETATM 5742  C6  MES  1003      46.176   6.914  50.355  1.00 75.06           C
521HETATM 5743  C7  MES  1003      44.806   3.336  50.302  1.00 73.39           C
522HETATM 5744  C8  MES  1003      44.672   2.791  51.713  1.00 76.85           C
523HETATM 5745  S   MES  1003      45.724   1.379  51.967  1.00 78.26           S
524HETATM 5746  O1S MES  1003      47.062   1.828  51.737  1.00 79.39           O
525HETATM 5747  O2S MES  1003      45.303   0.380  51.016  1.00 81.58           O
526HETATM 5748  O3S MES  1003      45.523   0.961  53.326  1.00 80.59           O
527HETATM 5749  O1  MES  1004      59.246  -5.152  27.381  1.00 99.99           O
528HETATM 5750  C2  MES  1004      60.067  -4.021  27.127  1.00 99.99           C
529HETATM 5751  C3  MES  1004      60.447  -3.301  28.378  1.00 99.78           C
530HETATM 5752  N4  MES  1004      61.180  -4.156  29.270  1.00 96.33           N
531HETATM 5753  C5  MES  1004      60.358  -5.461  29.506  1.00 97.90           C
532HETATM 5754  C6  MES  1004      59.965  -6.072  28.203  1.00 99.68           C
533HETATM 5755  C7  MES  1004      61.596  -3.484  30.507  1.00 93.33           C
534HETATM 5756  C8  MES  1004      61.931  -2.010  30.442  1.00 90.74           C
535HETATM 5757  S   MES  1004      60.763  -0.978  31.301  0.50 90.72           S
536HETATM 5758  O1S MES  1004      59.476  -1.170  30.680  0.50 91.60           O
537HETATM 5759  O2S MES  1004      61.249   0.383  31.164  0.50 91.20           O
538HETATM 5760  O3S MES  1004      60.776  -1.430  32.647  0.50 90.05           O
539HETATM 5761  P1  POP  1005      58.812  -7.766  57.091  1.00 57.40           P
540HETATM 5762  O1  POP  1005      60.254  -7.589  56.745  1.00 54.93           O
541HETATM 5763  O2  POP  1005      58.618  -8.839  58.095  1.00 55.36           O
542HETATM 5764  O3  POP  1005      57.949  -8.024  55.908  1.00 55.10           O
543HETATM 5765  O   POP  1005      58.295  -6.370  57.759  1.00 57.30           O
544HETATM 5766  P2  POP  1005      56.998  -5.955  58.661  1.00 59.66           P
545HETATM 5767  O4  POP  1005      57.491  -5.746  60.070  1.00 54.95           O
546HETATM 5768  O5  POP  1005      56.004  -7.075  58.550  1.00 56.24           O
547HETATM 5769  O6  POP  1005      56.427  -4.710  58.044  1.00 56.50           O
548MASTER      405    0    9   30   30    0    0    6 5843    3  116   66
549END
550