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elNémo ID: 21042909454578593

Job options:

ID        	=	 21042909454578593
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
TITLE     SWISS-MODEL SERVER (https://swissmodel.expasy.org)
TITLE    2 PREDICTEDinsulin-likegrowthfactor1receptorOreochromisniloticusNCBIRef
TITLE    3 erenceSequenceXP_003440646.2
EXPDTA    THEORETICAL MODEL (SWISS-MODEL SERVER)
AUTHOR    SWISS-MODEL SERVER (SEE REFERENCE IN JRNL Records)
REVDAT   1   05-JUL-18 1MOD    1       10:46
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   S.BIENERT,A.WATERHOUSE,T.A.P.DE BEER,G.TAURIELLO,G.STUDER,
REMARK   1  AUTH 2 L.BORDOLI,T.SCHWEDE
REMARK   1  TITL   THE SWISS-MODEL REPOSITORY - NEW FEATURES AND FUNCTIONALITY
REMARK   1  REF    NUCLEIC.ACIDS.RES..           V.  22       2017
REMARK   1  REFN                   ISSN 0305-1048
REMARK   1  PMID   27899672
REMARK   1  DOI    10.1093/nar/gkw1132
REMARK   1
REMARK   1 REFERENCE 2
REMARK   1  AUTH   N.GUEX,M.C.PEITSCH,T.SCHWEDE
REMARK   1  TITL   AUTOMATED COMPARATIVE PROTEIN STRUCTURE MODELING WITH
REMARK   1  TITL 2 SWISS-MODEL AND SWISS-PDBVIEWER: A HISTORICAL PERSPECTIVE
REMARK   1  REF    ELECTROPHORESIS               V.30         2009
REMARK   1  REFN                   ISSN 0173-0835
REMARK   1  PMID   19517507
REMARK   1  DOI    10.1002/elps.200900140
REMARK   1
REMARK   1 REFERENCE 3
REMARK   1  AUTH   P.BENKERT,M.BIASINI,T.SCHWEDE
REMARK   1  TITL   TOWARD THE ESTIMATION OF THE ABSOLUTE QUALITY OF INDIVIDUAL
REMARK   1  TITL 2 PROTEIN STRUCTURE MODELS
REMARK   1  REF    BIOINFORMATICS                V.27         2011
REMARK   1  REFN                   ISSN 1367-4803
REMARK   1  PMID   21134891
REMARK   1  DOI    10.1093/bioinformatics/btq662
REMARK   1
REMARK   1 REFERENCE 4
REMARK   1  AUTH   M.BERTONI,F.KIEFER,M.BIASINI,L.BORDOLI,T.SCHWEDE
REMARK   1  TITL   MODELING PROTEIN QUATERNARY STRUCTURE OF HOMO- AND
REMARK   1  TITL 2 HETERO-OLIGOMERS BEYOND BINARY INTERACTIONS BY HOMOLOGY
REMARK   1  REF    SCI.REP.                      V. 7         2017
REMARK   1  REFN                   ISSN
REMARK   1  PMID   28874689
REMARK   1  DOI    10.1038/s41598-017-09654-8
REMARK   1
REMARK   1 DISCLAIMER
REMARK   1 The SWISS-MODEL SERVER produces theoretical models for proteins.
REMARK   1 The results of any theoretical modelling procedure is
REMARK   1 NON-EXPERIMENTAL and MUST be considered with care. These models may
REMARK   1 contain significant errors. This is especially true for automated
REMARK   1 modeling since there is no human intervention during model
REMARK   1 building. Please read the header section and the logfile carefully
REMARK   1 to know what templates and alignments were used during the model
REMARK   1 building process. All information by the SWISS-MODEL SERVER is
REMARK   1 provided "AS-IS", without any warranty, expressed or implied.
REMARK   2
REMARK   2 COPYRIGHT NOTICE
REMARK   2 This SWISS-MODEL protein model is copyright. It is produced by the
REMARK   2 SWISS-MODEL server, developed by the Computational Structural
REMARK   2 Biology Group at the SIB Swiss Institute of Bioinformatics at the
REMARK   2 Biozentrum, University of Basel (https://swissmodel.expasy.org). This
REMARK   2 model is licensed under the CC BY-SA 4.0 Creative Commons
REMARK   2 Attribution-ShareAlike 4.0 International License
REMARK   2 (https://creativecommons.org/licenses/by-sa/4.0/legalcode), i.e. you
REMARK   2 can copy and redistribute the model in any medium or format,
REMARK   2 transform and build upon the model for any purpose, even
REMARK   2 commercially, under the following terms:
REMARK   2 Attribution - You must give appropriate credit, provide a link to
REMARK   2 the license, and indicate if changes were made. You may do so in any
REMARK   2 reasonable manner, but not in any way that suggests the licensor
REMARK   2 endorses you or your use. When you publish, patent or distribute
REMARK   2 results that were fully or partially based on the model, please cite
REMARK   2 the corresponding papers mentioned under JRNL.
REMARK   2 ShareAlike - If you remix, transform, or build upon the material,
REMARK   2 you must distribute your contributions under the same license as the
REMARK   2 original.
REMARK   2 No additional restrictions - you may not apply legal terms or
REMARK   2 technological measures that legally restrict others from doing
REMARK   2 anything the license permits.
REMARK   2 Find a human-readable summary of (and not a substitute for) the
REMARK   2 CC BY-SA 4.0 license at this link:
REMARK   2 https://creativecommons.org/licenses/by-sa/4.0/
REMARK   3 
REMARK   3 MODEL INFORMATION
REMARK   3  ENGIN   PROMOD3
REMARK   3  VERSN   1.1.0
REMARK   3  OSTAT   monomer
REMARK   3  OSRSN   PREDICTION
REMARK   3  QSPRD   0.413
REMARK   3  GMQE    0.49
REMARK   3  QMN4    -3.21
REMARK   3  MODT    FALSE
REMARK   3 
REMARK   3 TEMPLATE 1
REMARK   3  PDBID   5u8q
REMARK   3  CHAIN   A
REMARK   3  MMCIF   A
REMARK   3  PDBV    2018-06-22
REMARK   3  SMTLE   5u8q.1.A
REMARK   3  SMTLV   2018-06-29
REMARK   3  MTHD    X-RAY DIFFRACTION 3.27 A
REMARK   3  FOUND   BLAST
REMARK   3  GMQE    0.49
REMARK   3  SIM     0.50
REMARK   3  SID     62.63
REMARK   3  OSTAT   homo-dimer
REMARK   3  LIGND   MLT
REMARK   3  LIGND 2 MLT
REMARK   3  LIGND 3 NAG
REMARK   3  LIGND 4 NAG
REMARK   3  LIGND 5 NAG
REMARK   3  LIGND 6 NAG
REMARK   3  LIGND 7 NAG
REMARK   3  LIGND 8 NAG
REMARK   3  LIGND 9 NAG
REMARK   3  LIGND 10 NAG
REMARK   3  LIGND 11 NAG
REMARK   3  LIGND 12 NAG
REMARK   3  LIGND 13 NAG
REMARK   3  LIGND 14 NAG
REMARK   3  LIGND 15 NAG
REMARK   3  LIGND 16 NAG
REMARK   3  LIGND 17 NAG
REMARK   3  LIGND 18 NAG
ATOM      1  N   GLU A  35      29.998  43.702 -41.319  1.00  0.75
ATOM      2  CA  GLU A  35      28.689  43.366 -40.697  1.00  0.75
ATOM      3  C   GLU A  35      28.415  41.889 -40.573  1.00  0.75
ATOM      4  O   GLU A  35      28.454  41.168 -41.568  1.00  0.75
ATOM      5  CB  GLU A  35      27.582  44.082 -41.511  1.00  0.75
ATOM      6  CG  GLU A  35      26.168  43.948 -40.902  1.00  0.75
ATOM      7  CD  GLU A  35      26.053  44.507 -39.487  1.00  0.75
ATOM      8  OE1 GLU A  35      27.080  44.994 -38.948  1.00  0.75
ATOM      9  OE2 GLU A  35      24.930  44.421 -38.941  1.00  0.75
ATOM     10  N   ILE A  36      28.177  41.398 -39.343  1.00  0.87
ATOM     11  CA  ILE A  36      27.996  39.983 -39.065  1.00  0.87
ATOM     12  C   ILE A  36      26.619  39.873 -38.472  1.00  0.87
ATOM     13  O   ILE A  36      26.346  40.431 -37.414  1.00  0.87
ATOM     14  CB  ILE A  36      28.999  39.378 -38.070  1.00  0.87
ATOM     15  CG1 ILE A  36      30.469  39.583 -38.508  1.00  0.87
ATOM     16  CG2 ILE A  36      28.693  37.872 -37.878  1.00  0.87
ATOM     17  CD1 ILE A  36      31.477  39.141 -37.434  1.00  0.87
ATOM     18  N   CYS A  37      25.714  39.159 -39.152  1.00  0.87
ATOM     19  CA  CYS A  37      24.326  39.083 -38.747  1.00  0.87
ATOM     20  C   CYS A  37      24.054  37.689 -38.234  1.00  0.87
ATOM     21  O   CYS A  37      24.393  36.718 -38.900  1.00  0.87
ATOM     22  CB  CYS A  37      23.392  39.363 -39.950  1.00  0.87
ATOM     23  SG  CYS A  37      23.543  41.065 -40.571  1.00  0.87
ATOM     24  N   GLY A  38      23.458  37.537 -37.033  1.00  0.86
ATOM     25  CA  GLY A  38      23.259  36.210 -36.465  1.00  0.86
ATOM     26  C   GLY A  38      22.585  36.240 -35.122  1.00  0.86
ATOM     27  O   GLY A  38      21.976  37.253 -34.778  1.00  0.86
ATOM     28  N   PRO A  39      22.656  35.173 -34.323  1.00  0.79
ATOM     29  CA  PRO A  39      23.245  33.872 -34.630  1.00  0.79
ATOM     30  C   PRO A  39      22.404  33.010 -35.531  1.00  0.79
ATOM     31  O   PRO A  39      22.897  31.962 -35.903  1.00  0.79
ATOM     32  CB  PRO A  39      23.408  33.181 -33.262  1.00  0.79
ATOM     33  CG  PRO A  39      22.859  34.170 -32.225  1.00  0.79
ATOM     34  CD  PRO A  39      21.989  35.132 -33.032  1.00  0.79
ATOM     35  N   ASP A  40      21.163  33.397 -35.864  1.00  0.81
ATOM     36  CA  ASP A  40      20.330  32.639 -36.766  1.00  0.81
ATOM     37  C   ASP A  40      19.456  33.637 -37.501  1.00  0.81
ATOM     38  O   ASP A  40      19.059  34.649 -36.919  1.00  0.81
ATOM     39  CB  ASP A  40      19.409  31.668 -35.988  1.00  0.81
ATOM     40  CG  ASP A  40      20.223  30.514 -35.437  1.00  0.81
ATOM     41  OD1 ASP A  40      21.006  29.925 -36.227  1.00  0.81
ATOM     42  OD2 ASP A  40      20.007  30.161 -34.249  1.00  0.81
ATOM     43  N   ILE A  41      19.122  33.421 -38.793  1.00  0.85
ATOM     44  CA  ILE A  41      18.169  34.274 -39.497  1.00  0.85
ATOM     45  C   ILE A  41      17.006  33.441 -40.041  1.00  0.85
ATOM     46  O   ILE A  41      17.155  32.693 -41.004  1.00  0.85
ATOM     47  CB  ILE A  41      18.797  35.094 -40.635  1.00  0.85
ATOM     48  CG1 ILE A  41      20.059  35.897 -40.214  1.00  0.85
ATOM     49  CG2 ILE A  41      17.743  36.047 -41.241  1.00  0.85
ATOM     50  CD1 ILE A  41      19.850  36.985 -39.149  1.00  0.85
ATOM     51  N   ASP A  42      15.782  33.590 -39.476  1.00  0.85
ATOM     52  CA  ASP A  42      14.557  33.071 -40.073  1.00  0.85
ATOM     53  C   ASP A  42      13.736  34.246 -40.609  1.00  0.85
ATOM     54  O   ASP A  42      13.518  35.240 -39.907  1.00  0.85
ATOM     55  CB  ASP A  42      13.777  32.117 -39.097  1.00  0.85
ATOM     56  CG  ASP A  42      12.637  31.342 -39.741  1.00  0.85
ATOM     57  OD1 ASP A  42      11.687  31.971 -40.265  1.00  0.85
ATOM     58  OD2 ASP A  42      12.646  30.083 -39.687  1.00  0.85
ATOM     59  N   LEU A  43      13.341  34.170 -41.900  1.00  0.80
ATOM     60  CA  LEU A  43      12.595  35.146 -42.665  1.00  0.80
ATOM     61  C   LEU A  43      11.436  34.435 -43.323  1.00  0.80
ATOM     62  O   LEU A  43      11.610  33.526 -44.139  1.00  0.80
ATOM     63  CB  LEU A  43      13.433  35.849 -43.783  1.00  0.80
ATOM     64  CG  LEU A  43      14.712  36.534 -43.259  1.00  0.80
ATOM     65  CD1 LEU A  43      15.616  37.119 -44.353  1.00  0.80
ATOM     66  CD2 LEU A  43      14.424  37.563 -42.172  1.00  0.80
ATOM     67  N   ARG A  44      10.201  34.833 -42.983  1.00  0.73
ATOM     68  CA  ARG A  44       9.047  34.093 -43.422  1.00  0.73
ATOM     69  C   ARG A  44       7.813  34.955 -43.421  1.00  0.73
ATOM     70  O   ARG A  44       7.783  36.012 -42.790  1.00  0.73
ATOM     71  CB  ARG A  44       8.792  32.844 -42.538  1.00  0.73
ATOM     72  CG  ARG A  44       8.516  33.161 -41.056  1.00  0.73
ATOM     73  CD  ARG A  44       8.030  31.949 -40.260  1.00  0.73
ATOM     74  NE  ARG A  44       9.198  31.050 -40.051  1.00  0.73
ATOM     75  CZ  ARG A  44       9.152  29.788 -39.621  1.00  0.73
ATOM     76  NH1 ARG A  44       8.003  29.193 -39.334  1.00  0.73
ATOM     77  NH2 ARG A  44      10.283  29.114 -39.450  1.00  0.73
ATOM     78  N   ASN A  45       6.762  34.496 -44.133  1.00  0.64
ATOM     79  CA  ASN A  45       5.463  35.139 -44.237  1.00  0.64
ATOM     80  C   ASN A  45       5.527  36.374 -45.133  1.00  0.64
ATOM     81  O   ASN A  45       5.275  36.319 -46.334  1.00  0.64
ATOM     82  CB  ASN A  45       4.799  35.474 -42.861  1.00  0.64
ATOM     83  CG  ASN A  45       4.897  34.325 -41.863  1.00  0.64
ATOM     84  OD1 ASN A  45       4.798  33.132 -42.152  1.00  0.64
ATOM     85  ND2 ASN A  45       5.096  34.692 -40.575  1.00  0.64
ATOM     86  N   ASP A  46       5.886  37.532 -44.558  1.00  0.63
ATOM     87  CA  ASP A  46       6.008  38.784 -45.256  1.00  0.63
ATOM     88  C   ASP A  46       7.159  38.832 -46.250  1.00  0.63
ATOM     89  O   ASP A  46       8.322  38.600 -45.920  1.00  0.63
ATOM     90  CB  ASP A  46       6.230  39.927 -44.248  1.00  0.63
ATOM     91  CG  ASP A  46       5.098  39.952 -43.249  1.00  0.63
ATOM     92  OD1 ASP A  46       3.974  40.334 -43.656  1.00  0.63
ATOM     93  OD2 ASP A  46       5.356  39.562 -42.077  1.00  0.63
ATOM     94  N   ILE A  47       6.865  39.230 -47.499  1.00  0.63
ATOM     95  CA  ILE A  47       7.853  39.469 -48.535  1.00  0.63
ATOM     96  C   ILE A  47       8.862  40.564 -48.171  1.00  0.63
ATOM     97  O   ILE A  47      10.063  40.460 -48.420  1.00  0.63
ATOM     98  CB  ILE A  47       7.163  39.763 -49.867  1.00  0.63
ATOM     99  CG1 ILE A  47       6.338  41.074 -49.897  1.00  0.63
ATOM    100  CG2 ILE A  47       6.287  38.559 -50.275  1.00  0.63
ATOM    101  CD1 ILE A  47       5.866  41.457 -51.304  1.00  0.63
ATOM    102  N   ASP A  48       8.387  41.627 -47.493  1.00  0.71
ATOM    103  CA  ASP A  48       9.154  42.797 -47.136  1.00  0.71
ATOM    104  C   ASP A  48      10.008  42.556 -45.883  1.00  0.71
ATOM    105  O   ASP A  48      10.890  43.344 -45.539  1.00  0.71
ATOM    106  CB  ASP A  48       8.175  43.991 -46.951  1.00  0.71
ATOM    107  CG  ASP A  48       7.518  44.409 -48.269  1.00  0.71
ATOM    108  OD1 ASP A  48       8.135  44.221 -49.349  1.00  0.71
ATOM    109  OD2 ASP A  48       6.376  44.938 -48.219  1.00  0.71
ATOM    110  N   GLN A  49       9.841  41.398 -45.197  1.00  0.70
ATOM    111  CA  GLN A  49      10.673  41.003 -44.068  1.00  0.70
ATOM    112  C   GLN A  49      12.081  40.588 -44.494  1.00  0.70
ATOM    113  O   GLN A  49      13.002  40.514 -43.680  1.00  0.70
ATOM    114  CB  GLN A  49       9.982  39.900 -43.222  1.00  0.70
ATOM    115  CG  GLN A  49      10.593  39.685 -41.816  1.00  0.70
ATOM    116  CD  GLN A  49       9.902  38.609 -40.974  1.00  0.70
ATOM    117  OE1 GLN A  49      10.617  37.789 -40.388  1.00  0.70
ATOM    118  NE2 GLN A  49       8.556  38.632 -40.860  1.00  0.70
ATOM    119  N   PHE A  50      12.320  40.395 -45.811  1.00  0.77
ATOM    120  CA  PHE A  50      13.652  40.193 -46.360  1.00  0.77
ATOM    121  C   PHE A  50      14.593  41.334 -46.198  1.00  0.77
ATOM    122  O   PHE A  50      15.805  41.145 -46.243  1.00  0.77
ATOM    123  CB  PHE A  50      13.606  39.909 -47.876  1.00  0.77
ATOM    124  CG  PHE A  50      13.217  38.488 -48.137  1.00  0.77
ATOM    125  CD1 PHE A  50      13.491  37.416 -47.272  1.00  0.77
ATOM    126  CD2 PHE A  50      12.483  38.234 -49.292  1.00  0.77
ATOM    127  CE1 PHE A  50      12.971  36.143 -47.513  1.00  0.77
ATOM    128  CE2 PHE A  50      12.017  36.959 -49.583  1.00  0.77
ATOM    129  CZ  PHE A  50      12.238  35.924 -48.689  1.00  0.77
ATOM    130  N   LYS A  51      14.076  42.538 -45.950  1.00  0.81
ATOM    131  CA  LYS A  51      14.881  43.711 -45.771  1.00  0.81
ATOM    132  C   LYS A  51      15.974  43.596 -44.701  1.00  0.81
ATOM    133  O   LYS A  51      17.025  44.208 -44.820  1.00  0.81
ATOM    134  CB  LYS A  51      13.943  44.892 -45.522  1.00  0.81
ATOM    135  CG  LYS A  51      14.625  46.205 -45.868  1.00  0.81
ATOM    136  CD  LYS A  51      13.738  47.392 -45.532  1.00  0.81
ATOM    137  CE  LYS A  51      14.504  48.681 -45.785  1.00  0.81
ATOM    138  NZ  LYS A  51      13.672  49.812 -45.356  1.00  0.81
ATOM    139  N   ARG A  52      15.805  42.708 -43.691  1.00  0.80
ATOM    140  CA  ARG A  52      16.793  42.395 -42.662  1.00  0.80
ATOM    141  C   ARG A  52      18.185  41.959 -43.153  1.00  0.80
ATOM    142  O   ARG A  52      19.120  41.890 -42.361  1.00  0.80
ATOM    143  CB  ARG A  52      16.256  41.259 -41.731  1.00  0.80
ATOM    144  CG  ARG A  52      15.028  41.663 -40.878  1.00  0.80
ATOM    145  CD  ARG A  52      14.176  40.520 -40.285  1.00  0.80
ATOM    146  NE  ARG A  52      15.041  39.631 -39.443  1.00  0.80
ATOM    147  CZ  ARG A  52      14.650  38.461 -38.915  1.00  0.80
ATOM    148  NH1 ARG A  52      13.411  37.988 -39.009  1.00  0.80
ATOM    149  NH2 ARG A  52      15.545  37.708 -38.277  1.00  0.80
ATOM    150  N   LEU A  53      18.373  41.675 -44.459  1.00  0.84
ATOM    151  CA  LEU A  53      19.659  41.329 -45.032  1.00  0.84
ATOM    152  C   LEU A  53      20.333  42.515 -45.722  1.00  0.84
ATOM    153  O   LEU A  53      21.388  42.355 -46.331  1.00  0.84
ATOM    154  CB  LEU A  53      19.500  40.144 -46.022  1.00  0.84
ATOM    155  CG  LEU A  53      18.845  38.888 -45.399  1.00  0.84
ATOM    156  CD1 LEU A  53      18.603  37.801 -46.458  1.00  0.84
ATOM    157  CD2 LEU A  53      19.655  38.315 -44.223  1.00  0.84
ATOM    158  N   GLU A  54      19.783  43.749 -45.605  1.00  0.83
ATOM    159  CA  GLU A  54      20.278  44.966 -46.247  1.00  0.83
ATOM    160  C   GLU A  54      21.734  45.317 -45.956  1.00  0.83
ATOM    161  O   GLU A  54      22.475  45.728 -46.851  1.00  0.83
ATOM    162  CB  GLU A  54      19.341  46.184 -45.983  1.00  0.83
ATOM    163  CG  GLU A  54      19.087  46.604 -44.506  1.00  0.83
ATOM    164  CD  GLU A  54      17.952  47.633 -44.414  1.00  0.83
ATOM    165  OE1 GLU A  54      18.026  48.687 -45.099  1.00  0.83
ATOM    166  OE2 GLU A  54      16.965  47.374 -43.675  1.00  0.83
ATOM    167  N   ASN A  55      22.208  45.118 -44.711  1.00  0.85
ATOM    168  CA  ASN A  55      23.593  45.398 -44.367  1.00  0.85
ATOM    169  C   ASN A  55      24.485  44.158 -44.298  1.00  0.85
ATOM    170  O   ASN A  55      25.712  44.266 -44.316  1.00  0.85
ATOM    171  CB  ASN A  55      23.644  46.080 -42.980  1.00  0.85
ATOM    172  CG  ASN A  55      22.802  47.347 -43.006  1.00  0.85
ATOM    173  OD1 ASN A  55      22.878  48.142 -43.945  1.00  0.85
ATOM    174  ND2 ASN A  55      21.970  47.543 -41.960  1.00  0.85
ATOM    175  N   CYS A  56      23.906  42.946 -44.219  1.00  0.87
ATOM    176  CA  CYS A  56      24.630  41.727 -43.877  1.00  0.87
ATOM    177  C   CYS A  56      25.608  41.234 -44.939  1.00  0.87
ATOM    178  O   CYS A  56      25.219  40.900 -46.053  1.00  0.87
ATOM    179  CB  CYS A  56      23.656  40.567 -43.552  1.00  0.87
ATOM    180  SG  CYS A  56      22.447  41.029 -42.275  1.00  0.87
ATOM    181  N   THR A  57      26.914  41.137 -44.606  1.00  0.87
ATOM    182  CA  THR A  57      27.919  40.564 -45.514  1.00  0.87
ATOM    183  C   THR A  57      28.219  39.124 -45.148  1.00  0.87
ATOM    184  O   THR A  57      28.464  38.275 -46.006  1.00  0.87
ATOM    185  CB  THR A  57      29.194  41.420 -45.618  1.00  0.87
ATOM    186  OG1 THR A  57      30.271  40.779 -46.288  1.00  0.87
ATOM    187  CG2 THR A  57      29.734  41.831 -44.244  1.00  0.87
ATOM    188  N   VAL A  58      28.112  38.787 -43.852  1.00  0.89
ATOM    189  CA  VAL A  58      28.302  37.434 -43.374  1.00  0.89
ATOM    190  C   VAL A  58      27.111  37.080 -42.523  1.00  0.89
ATOM    191  O   VAL A  58      26.751  37.811 -41.596  1.00  0.89
ATOM    192  CB  VAL A  58      29.584  37.273 -42.566  1.00  0.89
ATOM    193  CG1 VAL A  58      29.761  35.808 -42.109  1.00  0.89
ATOM    194  CG2 VAL A  58      30.775  37.704 -43.445  1.00  0.89
ATOM    195  N   VAL A  59      26.456  35.944 -42.823  1.00  0.89
ATOM    196  CA  VAL A  59      25.378  35.439 -41.994  1.00  0.89
ATOM    197  C   VAL A  59      25.962  34.383 -41.103  1.00  0.89
ATOM    198  O   VAL A  59      26.369  33.306 -41.544  1.00  0.89
ATOM    199  CB  VAL A  59      24.194  34.875 -42.762  1.00  0.89
ATOM    200  CG1 VAL A  59      23.120  34.335 -41.793  1.00  0.89
ATOM    201  CG2 VAL A  59      23.591  36.008 -43.610  1.00  0.89
ATOM    202  N   GLU A  60      26.024  34.694 -39.802  1.00  0.85
ATOM    203  CA  GLU A  60      26.474  33.774 -38.799  1.00  0.85
ATOM    204  C   GLU A  60      25.285  32.926 -38.428  1.00  0.85
ATOM    205  O   GLU A  60      24.255  33.455 -38.021  1.00  0.85
ATOM    206  CB  GLU A  60      27.091  34.530 -37.600  1.00  0.85
ATOM    207  CG  GLU A  60      28.075  33.683 -36.761  1.00  0.85
ATOM    208  CD  GLU A  60      29.025  34.540 -35.936  1.00  0.85
ATOM    209  OE1 GLU A  60      28.554  35.382 -35.133  1.00  0.85
ATOM    210  OE2 GLU A  60      30.272  34.412 -36.097  1.00  0.85
ATOM    211  N   GLY A  61      25.374  31.604 -38.647  1.00  0.88
ATOM    212  CA  GLY A  61      24.288  30.672 -38.424  1.00  0.88
ATOM    213  C   GLY A  61      23.641  30.150 -39.655  1.00  0.88
ATOM    214  O   GLY A  61      24.255  30.022 -40.713  1.00  0.88
ATOM    215  N   TYR A  62      22.350  29.796 -39.544  1.00  0.86
ATOM    216  CA  TYR A  62      21.555  29.390 -40.685  1.00  0.86
ATOM    217  C   TYR A  62      20.774  30.547 -41.278  1.00  0.86
ATOM    218  O   TYR A  62      20.515  31.568 -40.640  1.00  0.86
ATOM    219  CB  TYR A  62      20.639  28.160 -40.405  1.00  0.86
ATOM    220  CG  TYR A  62      19.594  28.383 -39.348  1.00  0.86
ATOM    221  CD1 TYR A  62      18.451  29.142 -39.623  1.00  0.86
ATOM    222  CD2 TYR A  62      19.736  27.842 -38.067  1.00  0.86
ATOM    223  CE1 TYR A  62      17.499  29.394 -38.626  1.00  0.86
ATOM    224  CE2 TYR A  62      18.826  28.142 -37.046  1.00  0.86
ATOM    225  CZ  TYR A  62      17.705  28.923 -37.328  1.00  0.86
ATOM    226  OH  TYR A  62      16.808  29.290 -36.306  1.00  0.86
ATOM    227  N   LEU A  63      20.344  30.378 -42.539  1.00  0.89
ATOM    228  CA  LEU A  63      19.413  31.282 -43.179  1.00  0.89
ATOM    229  C   LEU A  63      18.188  30.505 -43.635  1.00  0.89
ATOM    230  O   LEU A  63      18.274  29.532 -44.388  1.00  0.89
ATOM    231  CB  LEU A  63      20.092  32.031 -44.353  1.00  0.89
ATOM    232  CG  LEU A  63      19.216  33.030 -45.150  1.00  0.89
ATOM    233  CD1 LEU A  63      18.513  34.078 -44.272  1.00  0.89
ATOM    234  CD2 LEU A  63      20.081  33.758 -46.192  1.00  0.89
ATOM    235  N   ARG A  64      16.997  30.917 -43.159  1.00  0.87
ATOM    236  CA  ARG A  64      15.721  30.374 -43.583  1.00  0.87
ATOM    237  C   ARG A  64      14.937  31.409 -44.352  1.00  0.87
ATOM    238  O   ARG A  64      14.714  32.520 -43.880  1.00  0.87
ATOM    239  CB  ARG A  64      14.795  29.961 -42.415  1.00  0.87
ATOM    240  CG  ARG A  64      15.359  28.918 -41.456  1.00  0.87
ATOM    241  CD  ARG A  64      15.659  27.593 -42.130  1.00  0.87
ATOM    242  NE  ARG A  64      15.920  26.606 -41.045  1.00  0.87
ATOM    243  CZ  ARG A  64      14.957  25.945 -40.392  1.00  0.87
ATOM    244  NH1 ARG A  64      15.318  25.031 -39.501  1.00  0.87
ATOM    245  NH2 ARG A  64      13.667  26.184 -40.596  1.00  0.87
ATOM    246  N   ILE A  65      14.482  31.037 -45.558  1.00  0.85
ATOM    247  CA  ILE A  65      13.646  31.851 -46.410  1.00  0.85
ATOM    248  C   ILE A  65      12.430  30.999 -46.771  1.00  0.85
ATOM    249  O   ILE A  65      12.490  30.118 -47.632  1.00  0.85
ATOM    250  CB  ILE A  65      14.497  32.254 -47.610  1.00  0.85
ATOM    251  CG1 ILE A  65      15.627  33.196 -47.135  1.00  0.85
ATOM    252  CG2 ILE A  65      13.657  32.895 -48.719  1.00  0.85
ATOM    253  CD1 ILE A  65      16.387  33.870 -48.272  1.00  0.85
ATOM    254  N   LEU A  66      11.295  31.199 -46.059  1.00  0.81
ATOM    255  CA  LEU A  66      10.209  30.215 -45.997  1.00  0.81
ATOM    256  C   LEU A  66       8.827  30.846 -46.188  1.00  0.81
ATOM    257  O   LEU A  66       8.486  31.830 -45.540  1.00  0.81
ATOM    258  CB  LEU A  66      10.143  29.511 -44.600  1.00  0.81
ATOM    259  CG  LEU A  66      11.078  28.317 -44.281  1.00  0.81
ATOM    260  CD1 LEU A  66      12.478  28.377 -44.879  1.00  0.81
ATOM    261  CD2 LEU A  66      11.222  28.221 -42.756  1.00  0.81
ATOM    262  N   LEU A  67       7.966  30.272 -47.063  1.00  0.71
ATOM    263  CA  LEU A  67       6.528  30.569 -47.120  1.00  0.71
ATOM    264  C   LEU A  67       6.200  31.985 -47.544  1.00  0.71
ATOM    265  O   LEU A  67       5.336  32.672 -47.005  1.00  0.71
ATOM    266  CB  LEU A  67       5.787  30.234 -45.805  1.00  0.71
ATOM    267  CG  LEU A  67       5.945  28.777 -45.343  1.00  0.71
ATOM    268  CD1 LEU A  67       5.342  28.638 -43.944  1.00  0.71
ATOM    269  CD2 LEU A  67       5.285  27.794 -46.320  1.00  0.71
ATOM    270  N   ILE A  68       6.917  32.425 -48.574  1.00  0.68
ATOM    271  CA  ILE A  68       6.990  33.792 -49.021  1.00  0.68
ATOM    272  C   ILE A  68       6.137  33.846 -50.267  1.00  0.68
ATOM    273  O   ILE A  68       6.624  33.865 -51.393  1.00  0.68
ATOM    274  CB  ILE A  68       8.443  34.180 -49.326  1.00  0.68
ATOM    275  CG1 ILE A  68       9.392  33.830 -48.141  1.00  0.68
ATOM    276  CG2 ILE A  68       8.475  35.667 -49.752  1.00  0.68
ATOM    277  CD1 ILE A  68       9.281  34.826 -46.999  1.00  0.68
ATOM    278  N   ASN A  69       4.813  33.790 -50.102  1.00  0.56
ATOM    279  CA  ASN A  69       3.890  33.750 -51.207  1.00  0.56
ATOM    280  C   ASN A  69       2.941  34.890 -50.923  1.00  0.56
ATOM    281  O   ASN A  69       3.350  36.043 -50.818  1.00  0.56
ATOM    282  CB  ASN A  69       3.238  32.329 -51.282  1.00  0.56
ATOM    283  CG  ASN A  69       2.356  32.144 -52.511  1.00  0.56
ATOM    284  OD1 ASN A  69       2.278  32.996 -53.393  1.00  0.56
ATOM    285  ND2 ASN A  69       1.666  30.987 -52.595  1.00  0.56
ATOM    286  N   GLU A  70       1.657  34.583 -50.741  1.00  0.38
ATOM    287  CA  GLU A  70       0.658  35.443 -50.181  1.00  0.38
ATOM    288  C   GLU A  70       1.003  35.985 -48.797  1.00  0.38
ATOM    289  O   GLU A  70       1.651  35.321 -47.990  1.00  0.38
ATOM    290  CB  GLU A  70      -0.620  34.595 -50.038  1.00  0.38
ATOM    291  CG  GLU A  70      -1.106  33.940 -51.356  1.00  0.38
ATOM    292  CD  GLU A  70      -1.631  34.901 -52.421  1.00  0.38
ATOM    293  OE1 GLU A  70      -1.718  36.132 -52.179  1.00  0.38
ATOM    294  OE2 GLU A  70      -1.966  34.366 -53.507  1.00  0.38
ATOM    295  N   LYS A  71       0.529  37.197 -48.447  1.00  0.39
ATOM    296  CA  LYS A  71       0.757  37.822 -47.151  1.00  0.39
ATOM    297  C   LYS A  71      -0.182  37.278 -46.071  1.00  0.39
ATOM    298  O   LYS A  71      -0.737  38.035 -45.289  1.00  0.39
ATOM    299  CB  LYS A  71       0.601  39.372 -47.235  1.00  0.39
ATOM    300  CG  LYS A  71       1.328  40.075 -48.404  1.00  0.39
ATOM    301  CD  LYS A  71       0.874  41.547 -48.529  1.00  0.39
ATOM    302  CE  LYS A  71       1.642  42.404 -49.544  1.00  0.39
ATOM    303  NZ  LYS A  71       1.104  43.785 -49.508  1.00  0.39
ATOM    304  N   THR A  72      -0.370  35.948 -46.014  1.00  0.35
ATOM    305  CA  THR A  72      -1.203  35.129 -45.129  1.00  0.35
ATOM    306  C   THR A  72      -1.694  33.993 -46.030  1.00  0.35
ATOM    307  O   THR A  72      -0.962  33.047 -46.292  1.00  0.35
ATOM    308  CB  THR A  72      -2.368  35.779 -44.335  1.00  0.35
ATOM    309  OG1 THR A  72      -1.915  36.781 -43.428  1.00  0.35
ATOM    310  CG2 THR A  72      -3.130  34.691 -43.539  1.00  0.35
ATOM    311  N   SER A  73      -2.942  34.039 -46.537  1.00  0.45
ATOM    312  CA  SER A  73      -3.557  32.959 -47.308  1.00  0.45
ATOM    313  C   SER A  73      -4.407  33.534 -48.422  1.00  0.45
ATOM    314  O   SER A  73      -4.546  32.952 -49.491  1.00  0.45
ATOM    315  CB  SER A  73      -4.519  32.122 -46.412  1.00  0.45
ATOM    316  OG  SER A  73      -5.458  32.958 -45.717  1.00  0.45
ATOM    317  N   ASN A  74      -4.956  34.736 -48.167  1.00  0.41
ATOM    318  CA  ASN A  74      -5.473  35.688 -49.122  1.00  0.41
ATOM    319  C   ASN A  74      -4.491  36.870 -49.106  1.00  0.41
ATOM    320  O   ASN A  74      -3.287  36.657 -49.005  1.00  0.41
ATOM    321  CB  ASN A  74      -6.923  36.053 -48.676  1.00  0.41
ATOM    322  CG  ASN A  74      -7.757  36.768 -49.737  1.00  0.41
ATOM    323  OD1 ASN A  74      -7.247  37.433 -50.637  1.00  0.41
ATOM    324  ND2 ASN A  74      -9.101  36.694 -49.600  1.00  0.41
ATOM    325  N   ASN A  75      -4.948  38.138 -49.206  1.00  0.54
ATOM    326  CA  ASN A  75      -4.099  39.307 -49.364  1.00  0.54
ATOM    327  C   ASN A  75      -3.560  39.412 -50.780  1.00  0.54
ATOM    328  O   ASN A  75      -2.533  40.064 -50.955  1.00  0.54
ATOM    329  CB  ASN A  75      -2.952  39.441 -48.324  1.00  0.54
ATOM    330  CG  ASN A  75      -3.565  39.593 -46.948  1.00  0.54
ATOM    331  OD1 ASN A  75      -4.227  40.591 -46.669  1.00  0.54
ATOM    332  ND2 ASN A  75      -3.358  38.621 -46.043  1.00  0.54
ATOM    333  N   SER A  76      -4.261  38.796 -51.782  1.00  0.38
ATOM    334  CA  SER A  76      -3.968  38.747 -53.227  1.00  0.38
ATOM    335  C   SER A  76      -2.630  39.319 -53.667  1.00  0.38
ATOM    336  O   SER A  76      -2.517  40.488 -54.045  1.00  0.38
ATOM    337  CB  SER A  76      -5.127  39.285 -54.115  1.00  0.38
ATOM    338  OG  SER A  76      -4.983  38.881 -55.482  1.00  0.38
ATOM    339  N   GLN A  77      -1.570  38.503 -53.568  1.00  0.44
ATOM    340  CA  GLN A  77      -0.218  38.895 -53.868  1.00  0.44
ATOM    341  C   GLN A  77       0.155  38.529 -55.285  1.00  0.44
ATOM    342  O   GLN A  77      -0.036  37.411 -55.746  1.00  0.44
ATOM    343  CB  GLN A  77       0.737  38.179 -52.888  1.00  0.44
ATOM    344  CG  GLN A  77       2.260  38.362 -53.105  1.00  0.44
ATOM    345  CD  GLN A  77       2.730  39.815 -53.144  1.00  0.44
ATOM    346  OE1 GLN A  77       2.512  40.630 -52.244  1.00  0.44
ATOM    347  NE2 GLN A  77       3.441  40.178 -54.238  1.00  0.44
ATOM    348  N   GLN A  78       0.740  39.475 -56.040  1.00  0.50
ATOM    349  CA  GLN A  78       1.293  39.189 -57.346  1.00  0.50
ATOM    350  C   GLN A  78       2.452  38.202 -57.305  1.00  0.50
ATOM    351  O   GLN A  78       3.389  38.352 -56.514  1.00  0.50
ATOM    352  CB  GLN A  78       1.737  40.528 -57.982  1.00  0.50
ATOM    353  CG  GLN A  78       1.769  40.535 -59.525  1.00  0.50
ATOM    354  CD  GLN A  78       2.117  41.929 -60.054  1.00  0.50
ATOM    355  OE1 GLN A  78       2.065  42.937 -59.344  1.00  0.50
ATOM    356  NE2 GLN A  78       2.484  41.992 -61.350  1.00  0.50
ATOM    357  N   GLU A  79       2.428  37.187 -58.191  1.00  0.53
ATOM    358  CA  GLU A  79       3.456  36.188 -58.342  1.00  0.53
ATOM    359  C   GLU A  79       4.657  36.818 -59.006  1.00  0.53
ATOM    360  O   GLU A  79       5.766  36.320 -58.900  1.00  0.53
ATOM    361  CB  GLU A  79       2.946  34.931 -59.108  1.00  0.53
ATOM    362  CG  GLU A  79       2.574  35.107 -60.609  1.00  0.53
ATOM    363  CD  GLU A  79       1.196  35.713 -60.902  1.00  0.53
ATOM    364  OE1 GLU A  79       0.684  36.511 -60.074  1.00  0.53
ATOM    365  OE2 GLU A  79       0.634  35.353 -61.969  1.00  0.53
ATOM    366  N   ASP A  80       4.524  38.000 -59.618  1.00  0.57
ATOM    367  CA  ASP A  80       5.652  38.870 -59.887  1.00  0.57
ATOM    368  C   ASP A  80       6.135  39.583 -58.609  1.00  0.57
ATOM    369  O   ASP A  80       5.962  40.791 -58.441  1.00  0.57
ATOM    370  CB  ASP A  80       5.338  39.919 -60.981  1.00  0.57
ATOM    371  CG  ASP A  80       4.617  39.288 -62.155  1.00  0.57
ATOM    372  OD1 ASP A  80       5.231  38.450 -62.856  1.00  0.57
ATOM    373  OD2 ASP A  80       3.438  39.677 -62.368  1.00  0.57
ATOM    374  N   PHE A  81       6.746  38.851 -57.645  1.00  0.47
ATOM    375  CA  PHE A  81       7.432  39.405 -56.484  1.00  0.47
ATOM    376  C   PHE A  81       8.350  40.599 -56.825  1.00  0.47
ATOM    377  O   PHE A  81       8.993  40.661 -57.868  1.00  0.47
ATOM    378  CB  PHE A  81       8.138  38.277 -55.668  1.00  0.47
ATOM    379  CG  PHE A  81       9.033  38.762 -54.568  1.00  0.47
ATOM    380  CD1 PHE A  81       8.535  39.594 -53.557  1.00  0.47
ATOM    381  CD2 PHE A  81      10.403  38.460 -54.599  1.00  0.47
ATOM    382  CE1 PHE A  81       9.415  40.186 -52.645  1.00  0.47
ATOM    383  CE2 PHE A  81      11.274  39.016 -53.656  1.00  0.47
ATOM    384  CZ  PHE A  81      10.777  39.888 -52.683  1.00  0.47
ATOM    385  N   ARG A  82       8.394  41.615 -55.940  1.00  0.59
ATOM    386  CA  ARG A  82       9.269  42.764 -56.056  1.00  0.59
ATOM    387  C   ARG A  82      10.760  42.464 -56.101  1.00  0.59
ATOM    388  O   ARG A  82      11.251  41.441 -55.637  1.00  0.59
ATOM    389  CB  ARG A  82       9.041  43.759 -54.899  1.00  0.59
ATOM    390  CG  ARG A  82       7.594  44.272 -54.792  1.00  0.59
ATOM    391  CD  ARG A  82       7.429  45.309 -53.677  1.00  0.59
ATOM    392  NE  ARG A  82       5.995  45.747 -53.685  1.00  0.59
ATOM    393  CZ  ARG A  82       5.512  46.649 -52.819  1.00  0.59
ATOM    394  NH1 ARG A  82       4.256  47.076 -52.950  1.00  0.59
ATOM    395  NH2 ARG A  82       6.264  47.130 -51.834  1.00  0.59
ATOM    396  N   SER A  83      11.549  43.385 -56.671  1.00  0.75
ATOM    397  CA  SER A  83      12.979  43.221 -56.807  1.00  0.75
ATOM    398  C   SER A  83      13.721  43.621 -55.539  1.00  0.75
ATOM    399  O   SER A  83      13.691  44.765 -55.092  1.00  0.75
ATOM    400  CB  SER A  83      13.515  44.017 -58.027  1.00  0.75
ATOM    401  OG  SER A  83      12.998  45.352 -58.055  1.00  0.75
ATOM    402  N   VAL A  84      14.416  42.654 -54.909  1.00  0.78
ATOM    403  CA  VAL A  84      15.207  42.893 -53.711  1.00  0.78
ATOM    404  C   VAL A  84      16.571  42.296 -53.955  1.00  0.78
ATOM    405  O   VAL A  84      16.686  41.100 -54.202  1.00  0.78
ATOM    406  CB  VAL A  84      14.626  42.281 -52.434  1.00  0.78
ATOM    407  CG1 VAL A  84      15.371  42.826 -51.203  1.00  0.78
ATOM    408  CG2 VAL A  84      13.128  42.603 -52.314  1.00  0.78
ATOM    409  N   SER A  85      17.635  43.120 -53.904  1.00  0.83
ATOM    410  CA  SER A  85      18.977  42.704 -54.288  1.00  0.83
ATOM    411  C   SER A  85      19.955  42.898 -53.156  1.00  0.83
ATOM    412  O   SER A  85      20.137  44.011 -52.665  1.00  0.83
ATOM    413  CB  SER A  85      19.566  43.531 -55.465  1.00  0.83
ATOM    414  OG  SER A  85      18.739  43.463 -56.624  1.00  0.83
ATOM    415  N   PHE A  86      20.655  41.829 -52.727  1.00  0.85
ATOM    416  CA  PHE A  86      21.609  41.883 -51.630  1.00  0.85
ATOM    417  C   PHE A  86      23.036  41.550 -52.072  1.00  0.85
ATOM    418  O   PHE A  86      23.528  40.464 -51.760  1.00  0.85
ATOM    419  CB  PHE A  86      21.222  40.896 -50.496  1.00  0.85
ATOM    420  CG  PHE A  86      19.844  41.168 -49.975  1.00  0.85
ATOM    421  CD1 PHE A  86      19.586  42.309 -49.203  1.00  0.85
ATOM    422  CD2 PHE A  86      18.800  40.265 -50.227  1.00  0.85
ATOM    423  CE1 PHE A  86      18.303  42.555 -48.700  1.00  0.85
ATOM    424  CE2 PHE A  86      17.517  40.500 -49.726  1.00  0.85
ATOM    425  CZ  PHE A  86      17.275  41.646 -48.960  1.00  0.85
ATOM    426  N   PRO A  87      23.788  42.411 -52.763  1.00  0.86
ATOM    427  CA  PRO A  87      25.157  42.108 -53.185  1.00  0.86
ATOM    428  C   PRO A  87      26.153  42.151 -52.040  1.00  0.86
ATOM    429  O   PRO A  87      27.322  41.839 -52.245  1.00  0.86
ATOM    430  CB  PRO A  87      25.449  43.209 -54.215  1.00  0.86
ATOM    431  CG  PRO A  87      24.641  44.408 -53.711  1.00  0.86
ATOM    432  CD  PRO A  87      23.363  43.748 -53.195  1.00  0.86
ATOM    433  N   LYS A  88      25.731  42.562 -50.833  1.00  0.85
ATOM    434  CA  LYS A  88      26.551  42.549 -49.641  1.00  0.85
ATOM    435  C   LYS A  88      26.936  41.141 -49.201  1.00  0.85
ATOM    436  O   LYS A  88      28.082  40.899 -48.835  1.00  0.85
ATOM    437  CB  LYS A  88      25.792  43.231 -48.472  1.00  0.85
ATOM    438  CG  LYS A  88      25.168  44.608 -48.777  1.00  0.85
ATOM    439  CD  LYS A  88      26.149  45.796 -48.779  1.00  0.85
ATOM    440  CE  LYS A  88      25.416  47.133 -48.983  1.00  0.85
ATOM    441  NZ  LYS A  88      26.327  48.289 -48.803  1.00  0.85
ATOM    442  N   LEU A  89      25.972  40.192 -49.225  1.00  0.88
ATOM    443  CA  LEU A  89      26.134  38.846 -48.706  1.00  0.88
ATOM    444  C   LEU A  89      27.063  37.971 -49.527  1.00  0.88
ATOM    445  O   LEU A  89      26.840  37.730 -50.713  1.00  0.88
ATOM    446  CB  LEU A  89      24.757  38.143 -48.551  1.00  0.88
ATOM    447  CG  LEU A  89      24.803  36.715 -47.950  1.00  0.88
ATOM    448  CD1 LEU A  89      25.522  36.680 -46.596  1.00  0.88
ATOM    449  CD2 LEU A  89      23.403  36.104 -47.792  1.00  0.88
ATOM    450  N   THR A  90      28.124  37.448 -48.879  1.00  0.89
ATOM    451  CA  THR A  90      29.112  36.595 -49.524  1.00  0.89
ATOM    452  C   THR A  90      29.307  35.268 -48.813  1.00  0.89
ATOM    453  O   THR A  90      29.643  34.270 -49.459  1.00  0.89
ATOM    454  CB  THR A  90      30.479  37.268 -49.618  1.00  0.89
ATOM    455  OG1 THR A  90      30.935  37.690 -48.342  1.00  0.89
ATOM    456  CG2 THR A  90      30.370  38.523 -50.493  1.00  0.89
ATOM    457  N   VAL A  91      29.088  35.195 -47.480  1.00  0.89
ATOM    458  CA  VAL A  91      29.375  33.999 -46.693  1.00  0.89
ATOM    459  C   VAL A  91      28.208  33.626 -45.785  1.00  0.89
ATOM    460  O   VAL A  91      27.685  34.449 -45.034  1.00  0.89
ATOM    461  CB  VAL A  91      30.637  34.132 -45.827  1.00  0.89
ATOM    462  CG1 VAL A  91      31.026  32.769 -45.208  1.00  0.89
ATOM    463  CG2 VAL A  91      31.812  34.658 -46.673  1.00  0.89
ATOM    464  N   ILE A  92      27.785  32.343 -45.807  1.00  0.89
ATOM    465  CA  ILE A  92      26.849  31.778 -44.836  1.00  0.89
ATOM    466  C   ILE A  92      27.589  30.709 -44.035  1.00  0.89
ATOM    467  O   ILE A  92      28.256  29.837 -44.593  1.00  0.89
ATOM    468  CB  ILE A  92      25.583  31.233 -45.511  1.00  0.89
ATOM    469  CG1 ILE A  92      24.799  32.423 -46.129  1.00  0.89
ATOM    470  CG2 ILE A  92      24.715  30.441 -44.502  1.00  0.89
ATOM    471  CD1 ILE A  92      23.480  32.058 -46.825  1.00  0.89
ATOM    472  N   THR A  93      27.567  30.774 -42.681  1.00  0.87
ATOM    473  CA  THR A  93      28.358  29.862 -41.847  1.00  0.87
ATOM    474  C   THR A  93      27.729  28.494 -41.707  1.00  0.87
ATOM    475  O   THR A  93      28.422  27.478 -41.737  1.00  0.87
ATOM    476  CB  THR A  93      28.774  30.390 -40.467  1.00  0.87
ATOM    477  OG1 THR A  93      27.716  30.418 -39.523  1.00  0.87
ATOM    478  CG2 THR A  93      29.306  31.820 -40.620  1.00  0.87
ATOM    479  N   GLY A  94      26.396  28.425 -41.550  1.00  0.88
ATOM    480  CA  GLY A  94      25.633  27.192 -41.489  1.00  0.88
ATOM    481  C   GLY A  94      25.064  26.830 -42.826  1.00  0.88
ATOM    482  O   GLY A  94      25.726  26.918 -43.857  1.00  0.88
ATOM    483  N   TYR A  95      23.802  26.376 -42.826  1.00  0.86
ATOM    484  CA  TYR A  95      23.077  25.984 -44.014  1.00  0.86
ATOM    485  C   TYR A  95      22.127  27.069 -44.527  1.00  0.86
ATOM    486  O   TYR A  95      21.715  27.978 -43.804  1.00  0.86
ATOM    487  CB  TYR A  95      22.291  24.663 -43.765  1.00  0.86
ATOM    488  CG  TYR A  95      21.266  24.799 -42.667  1.00  0.86
ATOM    489  CD1 TYR A  95      19.976  25.250 -42.981  1.00  0.86
ATOM    490  CD2 TYR A  95      21.559  24.467 -41.334  1.00  0.86
ATOM    491  CE1 TYR A  95      18.995  25.361 -41.990  1.00  0.86
ATOM    492  CE2 TYR A  95      20.572  24.558 -40.340  1.00  0.86
ATOM    493  CZ  TYR A  95      19.288  25.012 -40.666  1.00  0.86
ATOM    494  OH  TYR A  95      18.301  25.120 -39.661  1.00  0.86
ATOM    495  N   LEU A  96      21.719  26.949 -45.804  1.00  0.89
ATOM    496  CA  LEU A  96      20.721  27.800 -46.429  1.00  0.89
ATOM    497  C   LEU A  96      19.495  26.973 -46.808  1.00  0.89
ATOM    498  O   LEU A  96      19.596  25.929 -47.452  1.00  0.89
ATOM    499  CB  LEU A  96      21.344  28.486 -47.673  1.00  0.89
ATOM    500  CG  LEU A  96      20.396  29.299 -48.586  1.00  0.89
ATOM    501  CD1 LEU A  96      19.594  30.368 -47.830  1.00  0.89
ATOM    502  CD2 LEU A  96      21.201  29.966 -49.714  1.00  0.89
ATOM    503  N   LEU A  97      18.289  27.412 -46.384  1.00  0.89
ATOM    504  CA  LEU A  97      17.044  26.703 -46.637  1.00  0.89
ATOM    505  C   LEU A  97      16.035  27.613 -47.319  1.00  0.89
ATOM    506  O   LEU A  97      15.642  28.652 -46.784  1.00  0.89
ATOM    507  CB  LEU A  97      16.453  26.168 -45.306  1.00  0.89
ATOM    508  CG  LEU A  97      15.541  24.920 -45.393  1.00  0.89
ATOM    509  CD1 LEU A  97      15.389  24.287 -44.003  1.00  0.89
ATOM    510  CD2 LEU A  97      14.151  25.166 -45.999  1.00  0.89
ATOM    511  N   LEU A  98      15.580  27.214 -48.521  1.00  0.89
ATOM    512  CA  LEU A  98      14.589  27.918 -49.310  1.00  0.89
ATOM    513  C   LEU A  98      13.363  27.034 -49.472  1.00  0.89
ATOM    514  O   LEU A  98      13.451  25.925 -50.000  1.00  0.89
ATOM    515  CB  LEU A  98      15.161  28.236 -50.712  1.00  0.89
ATOM    516  CG  LEU A  98      16.301  29.270 -50.687  1.00  0.89
ATOM    517  CD1 LEU A  98      17.263  29.034 -51.848  1.00  0.89
ATOM    518  CD2 LEU A  98      15.770  30.705 -50.746  1.00  0.89
ATOM    519  N   PHE A  99      12.185  27.492 -48.996  1.00  0.87
ATOM    520  CA  PHE A  99      10.973  26.692 -49.047  1.00  0.87
ATOM    521  C   PHE A  99       9.759  27.534 -49.421  1.00  0.87
ATOM    522  O   PHE A  99       9.420  28.506 -48.749  1.00  0.87
ATOM    523  CB  PHE A  99      10.790  25.954 -47.690  1.00  0.87
ATOM    524  CG  PHE A  99       9.555  25.100 -47.592  1.00  0.87
ATOM    525  CD1 PHE A  99       9.408  23.932 -48.357  1.00  0.87
ATOM    526  CD2 PHE A  99       8.541  25.449 -46.687  1.00  0.87
ATOM    527  CE1 PHE A  99       8.264  23.133 -48.227  1.00  0.87
ATOM    528  CE2 PHE A  99       7.400  24.651 -46.547  1.00  0.87
ATOM    529  CZ  PHE A  99       7.259  23.494 -47.322  1.00  0.87
ATOM    530  N   ARG A 100       9.059  27.170 -50.519  1.00  0.81
ATOM    531  CA  ARG A 100       7.808  27.784 -50.954  1.00  0.81
ATOM    532  C   ARG A 100       7.783  29.300 -51.064  1.00  0.81
ATOM    533  O   ARG A 100       6.882  29.978 -50.570  1.00  0.81
ATOM    534  CB  ARG A 100       6.592  27.287 -50.149  1.00  0.81
ATOM    535  CG  ARG A 100       6.475  25.755 -50.161  1.00  0.81
ATOM    536  CD  ARG A 100       5.106  25.221 -49.746  1.00  0.81
ATOM    537  NE  ARG A 100       4.193  25.520 -50.892  1.00  0.81
ATOM    538  CZ  ARG A 100       2.901  25.179 -50.929  1.00  0.81
ATOM    539  NH1 ARG A 100       2.298  24.617 -49.889  1.00  0.81
ATOM    540  NH2 ARG A 100       2.203  25.433 -52.034  1.00  0.81
ATOM    541  N   VAL A 101       8.780  29.862 -51.755  1.00  0.77
ATOM    542  CA  VAL A 101       8.864  31.276 -52.054  1.00  0.77
ATOM    543  C   VAL A 101       8.285  31.479 -53.427  1.00  0.77
ATOM    544  O   VAL A 101       8.755  30.900 -54.402  1.00  0.77
ATOM    545  CB  VAL A 101      10.305  31.750 -52.061  1.00  0.77
ATOM    546  CG1 VAL A 101      10.465  33.245 -52.416  1.00  0.77
ATOM    547  CG2 VAL A 101      10.941  31.426 -50.699  1.00  0.77
ATOM    548  N   SER A 102       7.225  32.286 -53.539  1.00  0.73
ATOM    549  CA  SER A 102       6.545  32.507 -54.798  1.00  0.73
ATOM    550  C   SER A 102       7.032  33.772 -55.430  1.00  0.73
ATOM    551  O   SER A 102       7.226  34.791 -54.769  1.00  0.73
ATOM    552  CB  SER A 102       5.017  32.614 -54.641  1.00  0.73
ATOM    553  OG  SER A 102       4.326  32.673 -55.889  1.00  0.73
ATOM    554  N   GLY A 103       7.262  33.731 -56.750  1.00  0.75
ATOM    555  CA  GLY A 103       7.700  34.907 -57.468  1.00  0.75
ATOM    556  C   GLY A 103       9.151  35.220 -57.392  1.00  0.75
ATOM    557  O   GLY A 103       9.613  36.264 -57.839  1.00  0.75
ATOM    558  N   LEU A 104       9.951  34.310 -56.848  1.00  0.77
ATOM    559  CA  LEU A 104      11.380  34.375 -57.016  1.00  0.77
ATOM    560  C   LEU A 104      11.785  33.530 -58.212  1.00  0.77
ATOM    561  O   LEU A 104      11.792  32.305 -58.129  1.00  0.77
ATOM    562  CB  LEU A 104      12.109  33.877 -55.745  1.00  0.77
ATOM    563  CG  LEU A 104      13.646  33.963 -55.817  1.00  0.77
ATOM    564  CD1 LEU A 104      14.117  35.417 -55.958  1.00  0.77
ATOM    565  CD2 LEU A 104      14.285  33.300 -54.590  1.00  0.77
ATOM    566  N   ASP A 105      12.130  34.145 -59.367  1.00  0.83
ATOM    567  CA  ASP A 105      12.569  33.401 -60.538  1.00  0.83
ATOM    568  C   ASP A 105      13.973  32.802 -60.447  1.00  0.83
ATOM    569  O   ASP A 105      14.265  31.769 -61.038  1.00  0.83
ATOM    570  CB  ASP A 105      12.582  34.256 -61.824  1.00  0.83
ATOM    571  CG  ASP A 105      11.212  34.736 -62.249  1.00  0.83
ATOM    572  OD1 ASP A 105      10.343  33.897 -62.570  1.00  0.83
ATOM    573  OD2 ASP A 105      11.064  35.972 -62.375  1.00  0.83
ATOM    574  N   SER A 106      14.910  33.440 -59.731  1.00  0.85
ATOM    575  CA  SER A 106      16.278  32.962 -59.690  1.00  0.85
ATOM    576  C   SER A 106      16.931  33.423 -58.409  1.00  0.85
ATOM    577  O   SER A 106      16.624  34.489 -57.885  1.00  0.85
ATOM    578  CB  SER A 106      17.145  33.457 -60.868  1.00  0.85
ATOM    579  OG  SER A 106      18.485  33.017 -60.696  1.00  0.85
ATOM    580  N   LEU A 107      17.906  32.650 -57.883  1.00  0.85
ATOM    581  CA  LEU A 107      18.642  33.029 -56.690  1.00  0.85
ATOM    582  C   LEU A 107      19.649  34.156 -56.912  1.00  0.85
ATOM    583  O   LEU A 107      20.112  34.764 -55.947  1.00  0.85
ATOM    584  CB  LEU A 107      19.368  31.828 -56.025  1.00  0.85
ATOM    585  CG  LEU A 107      18.479  30.635 -55.596  1.00  0.85
ATOM    586  CD1 LEU A 107      19.288  29.655 -54.727  1.00  0.85
ATOM    587  CD2 LEU A 107      17.208  31.063 -54.844  1.00  0.85
ATOM    588  N   SER A 108      19.982  34.510 -58.174  1.00  0.83
ATOM    589  CA  SER A 108      20.855  35.644 -58.477  1.00  0.83
ATOM    590  C   SER A 108      20.240  36.981 -58.146  1.00  0.83
ATOM    591  O   SER A 108      20.938  37.951 -57.867  1.00  0.83
ATOM    592  CB  SER A 108      21.239  35.718 -59.978  1.00  0.83
ATOM    593  OG  SER A 108      20.102  35.853 -60.834  1.00  0.83
ATOM    594  N   VAL A 109      18.896  37.042 -58.171  1.00  0.81
ATOM    595  CA  VAL A 109      18.112  38.213 -57.848  1.00  0.81
ATOM    596  C   VAL A 109      18.360  38.653 -56.421  1.00  0.81
ATOM    597  O   VAL A 109      18.563  39.831 -56.149  1.00  0.81
ATOM    598  CB  VAL A 109      16.631  37.910 -58.061  1.00  0.81
ATOM    599  CG1 VAL A 109      15.746  39.116 -57.689  1.00  0.81
ATOM    600  CG2 VAL A 109      16.396  37.509 -59.533  1.00  0.81
ATOM    601  N   LEU A 110      18.406  37.693 -55.476  1.00  0.84
ATOM    602  CA  LEU A 110      18.644  38.001 -54.085  1.00  0.84
ATOM    603  C   LEU A 110      20.117  38.041 -53.712  1.00  0.84
ATOM    604  O   LEU A 110      20.587  39.041 -53.177  1.00  0.84
ATOM    605  CB  LEU A 110      17.947  36.966 -53.172  1.00  0.84
ATOM    606  CG  LEU A 110      16.438  36.786 -53.434  1.00  0.84
ATOM    607  CD1 LEU A 110      15.858  35.736 -52.478  1.00  0.84
ATOM    608  CD2 LEU A 110      15.649  38.098 -53.321  1.00  0.84
ATOM    609  N   PHE A 111      20.898  36.971 -53.986  1.00  0.86
ATOM    610  CA  PHE A 111      22.259  36.853 -53.468  1.00  0.86
ATOM    611  C   PHE A 111      23.257  36.629 -54.588  1.00  0.86
ATOM    612  O   PHE A 111      23.721  35.502 -54.778  1.00  0.86
ATOM    613  CB  PHE A 111      22.425  35.688 -52.450  1.00  0.86
ATOM    614  CG  PHE A 111      21.330  35.711 -51.431  1.00  0.86
ATOM    615  CD1 PHE A 111      21.194  36.794 -50.552  1.00  0.86
ATOM    616  CD2 PHE A 111      20.394  34.666 -51.384  1.00  0.86
ATOM    617  CE1 PHE A 111      20.121  36.850 -49.658  1.00  0.86
ATOM    618  CE2 PHE A 111      19.313  34.722 -50.496  1.00  0.86
ATOM    619  CZ  PHE A 111      19.172  35.822 -49.640  1.00  0.86
ATOM    620  N   PRO A 112      23.660  37.631 -55.357  1.00  0.85
ATOM    621  CA  PRO A 112      24.504  37.405 -56.519  1.00  0.85
ATOM    622  C   PRO A 112      25.933  37.137 -56.106  1.00  0.85
ATOM    623  O   PRO A 112      26.661  36.484 -56.846  1.00  0.85
ATOM    624  CB  PRO A 112      24.362  38.712 -57.312  1.00  0.85
ATOM    625  CG  PRO A 112      24.077  39.780 -56.252  1.00  0.85
ATOM    626  CD  PRO A 112      23.209  39.023 -55.248  1.00  0.85
ATOM    627  N   ASN A 113      26.358  37.629 -54.930  1.00  0.85
ATOM    628  CA  ASN A 113      27.736  37.573 -54.494  1.00  0.85
ATOM    629  C   ASN A 113      27.981  36.457 -53.485  1.00  0.85
ATOM    630  O   ASN A 113      29.073  36.364 -52.928  1.00  0.85
ATOM    631  CB  ASN A 113      28.170  38.932 -53.882  1.00  0.85
ATOM    632  CG  ASN A 113      28.244  40.030 -54.941  1.00  0.85
ATOM    633  OD1 ASN A 113      27.709  39.959 -56.047  1.00  0.85
ATOM    634  ND2 ASN A 113      28.967  41.120 -54.604  1.00  0.85
ATOM    635  N   LEU A 114      26.994  35.564 -53.238  1.00  0.87
ATOM    636  CA  LEU A 114      27.149  34.428 -52.340  1.00  0.87
ATOM    637  C   LEU A 114      28.188  33.428 -52.834  1.00  0.87
ATOM    638  O   LEU A 114      28.003  32.763 -53.850  1.00  0.87
ATOM    639  CB  LEU A 114      25.788  33.728 -52.097  1.00  0.87
ATOM    640  CG  LEU A 114      25.788  32.521 -51.127  1.00  0.87
ATOM    641  CD1 LEU A 114      26.309  32.881 -49.727  1.00  0.87
ATOM    642  CD2 LEU A 114      24.374  31.931 -51.004  1.00  0.87
ATOM    643  N   SER A 115      29.321  33.317 -52.111  1.00  0.86
ATOM    644  CA  SER A 115      30.499  32.621 -52.604  1.00  0.86
ATOM    645  C   SER A 115      30.773  31.356 -51.827  1.00  0.86
ATOM    646  O   SER A 115      31.192  30.347 -52.398  1.00  0.86
ATOM    647  CB  SER A 115      31.780  33.499 -52.483  1.00  0.86
ATOM    648  OG  SER A 115      31.791  34.560 -53.436  1.00  0.86
ATOM    649  N   VAL A 116      30.542  31.359 -50.499  1.00  0.88
ATOM    650  CA  VAL A 116      30.876  30.228 -49.649  1.00  0.88
ATOM    651  C   VAL A 116      29.718  29.937 -48.714  1.00  0.88
ATOM    652  O   VAL A 116      29.263  30.797 -47.957  1.00  0.88
ATOM    653  CB  VAL A 116      32.180  30.412 -48.859  1.00  0.88
ATOM    654  CG1 VAL A 116      32.467  29.178 -47.975  1.00  0.88
ATOM    655  CG2 VAL A 116      33.359  30.589 -49.839  1.00  0.88
ATOM    656  N   ILE A 117      29.220  28.685 -48.730  1.00  0.87
ATOM    657  CA  ILE A 117      28.308  28.187 -47.709  1.00  0.87
ATOM    658  C   ILE A 117      29.101  27.187 -46.901  1.00  0.87
ATOM    659  O   ILE A 117      29.418  26.091 -47.353  1.00  0.87
ATOM    660  CB  ILE A 117      27.044  27.538 -48.272  1.00  0.87
ATOM    661  CG1 ILE A 117      26.224  28.596 -49.051  1.00  0.87
ATOM    662  CG2 ILE A 117      26.213  26.919 -47.121  1.00  0.87
ATOM    663  CD1 ILE A 117      24.905  28.069 -49.636  1.00  0.87
ATOM    664  N   ARG A 118      29.487  27.541 -45.663  1.00  0.82
ATOM    665  CA  ARG A 118      30.420  26.712 -44.928  1.00  0.82
ATOM    666  C   ARG A 118      29.778  25.488 -44.313  1.00  0.82
ATOM    667  O   ARG A 118      30.443  24.486 -44.065  1.00  0.82
ATOM    668  CB  ARG A 118      31.134  27.496 -43.806  1.00  0.82
ATOM    669  CG  ARG A 118      31.937  28.708 -44.305  1.00  0.82
ATOM    670  CD  ARG A 118      32.641  29.463 -43.175  1.00  0.82
ATOM    671  NE  ARG A 118      33.702  28.576 -42.572  1.00  0.82
ATOM    672  CZ  ARG A 118      35.015  28.682 -42.827  1.00  0.82
ATOM    673  NH1 ARG A 118      35.445  29.424 -43.832  1.00  0.82
ATOM    674  NH2 ARG A 118      35.879  28.079 -42.016  1.00  0.82
ATOM    675  N   GLY A 119      28.456  25.511 -44.055  1.00  0.86
ATOM    676  CA  GLY A 119      27.761  24.343 -43.540  1.00  0.86
ATOM    677  C   GLY A 119      28.239  23.835 -42.207  1.00  0.86
ATOM    678  O   GLY A 119      28.229  22.634 -41.980  1.00  0.86
ATOM    679  N   HIS A 120      28.692  24.715 -41.287  1.00  0.80
ATOM    680  CA  HIS A 120      29.293  24.330 -40.013  1.00  0.80
ATOM    681  C   HIS A 120      28.369  23.459 -39.188  1.00  0.80
ATOM    682  O   HIS A 120      28.749  22.400 -38.690  1.00  0.80
ATOM    683  CB  HIS A 120      29.627  25.597 -39.194  1.00  0.80
ATOM    684  CG  HIS A 120      30.272  25.326 -37.873  1.00  0.80
ATOM    685  ND1 HIS A 120      31.528  24.757 -37.858  1.00  0.80
ATOM    686  CD2 HIS A 120      29.836  25.558 -36.607  1.00  0.80
ATOM    687  CE1 HIS A 120      31.836  24.657 -36.578  1.00  0.80
ATOM    688  NE2 HIS A 120      30.846  25.124 -35.781  1.00  0.80
ATOM    689  N   ASN A 121      27.090  23.857 -39.146  1.00  0.80
ATOM    690  CA  ASN A 121      26.000  23.028 -38.696  1.00  0.80
ATOM    691  C   ASN A 121      25.081  22.813 -39.886  1.00  0.80
ATOM    692  O   ASN A 121      24.919  23.702 -40.722  1.00  0.80
ATOM    693  CB  ASN A 121      25.212  23.698 -37.548  1.00  0.80
ATOM    694  CG  ASN A 121      26.107  23.812 -36.321  1.00  0.80
ATOM    695  OD1 ASN A 121      26.601  22.805 -35.812  1.00  0.80
ATOM    696  ND2 ASN A 121      26.310  25.050 -35.815  1.00  0.80
ATOM    697  N   LEU A 122      24.478  21.614 -40.006  1.00  0.81
ATOM    698  CA  LEU A 122      23.776  21.200 -41.203  1.00  0.81
ATOM    699  C   LEU A 122      22.317  20.971 -40.913  1.00  0.81
ATOM    700  O   LEU A 122      21.925  20.573 -39.818  1.00  0.81
ATOM    701  CB  LEU A 122      24.339  19.883 -41.796  1.00  0.81
ATOM    702  CG  LEU A 122      25.810  19.959 -42.238  1.00  0.81
ATOM    703  CD1 LEU A 122      26.289  18.578 -42.707  1.00  0.81
ATOM    704  CD2 LEU A 122      26.009  20.997 -43.352  1.00  0.81
ATOM    705  N   PHE A 123      21.457  21.192 -41.919  1.00  0.85
ATOM    706  CA  PHE A 123      20.066  20.818 -41.824  1.00  0.85
ATOM    707  C   PHE A 123      19.940  19.403 -42.332  1.00  0.85
ATOM    708  O   PHE A 123      19.868  19.166 -43.534  1.00  0.85
ATOM    709  CB  PHE A 123      19.180  21.791 -42.638  1.00  0.85
ATOM    710  CG  PHE A 123      17.707  21.561 -42.449  1.00  0.85
ATOM    711  CD1 PHE A 123      17.049  22.016 -41.295  1.00  0.85
ATOM    712  CD2 PHE A 123      16.964  20.917 -43.449  1.00  0.85
ATOM    713  CE1 PHE A 123      15.670  21.830 -41.145  1.00  0.85
ATOM    714  CE2 PHE A 123      15.585  20.728 -43.305  1.00  0.85
ATOM    715  CZ  PHE A 123      14.942  21.188 -42.151  1.00  0.85
ATOM    716  N   TYR A 124      19.962  18.411 -41.418  1.00  0.79
ATOM    717  CA  TYR A 124      19.712  17.021 -41.764  1.00  0.79
ATOM    718  C   TYR A 124      20.750  16.451 -42.754  1.00  0.79
ATOM    719  O   TYR A 124      20.436  15.672 -43.649  1.00  0.79
ATOM    720  CB  TYR A 124      18.239  16.899 -42.282  1.00  0.79
ATOM    721  CG  TYR A 124      17.611  15.540 -42.320  1.00  0.79
ATOM    722  CD1 TYR A 124      18.284  14.391 -41.884  1.00  0.79
ATOM    723  CD2 TYR A 124      16.370  15.386 -42.970  1.00  0.79
ATOM    724  CE1 TYR A 124      17.781  13.135 -42.173  1.00  0.79
ATOM    725  CE2 TYR A 124      15.874  14.133 -43.280  1.00  0.79
ATOM    726  CZ  TYR A 124      16.592  13.061 -42.859  1.00  0.79
ATOM    727  OH  TYR A 124      16.095  11.813 -43.150  1.00  0.79
ATOM    728  N   ASN A 125      22.028  16.863 -42.591  1.00  0.79
ATOM    729  CA  ASN A 125      23.189  16.530 -43.416  1.00  0.79
ATOM    730  C   ASN A 125      23.282  17.328 -44.712  1.00  0.79
ATOM    731  O   ASN A 125      24.202  17.141 -45.511  1.00  0.79
ATOM    732  CB  ASN A 125      23.411  15.012 -43.654  1.00  0.79
ATOM    733  CG  ASN A 125      23.487  14.327 -42.298  1.00  0.79
ATOM    734  OD1 ASN A 125      24.028  14.873 -41.334  1.00  0.79
ATOM    735  ND2 ASN A 125      22.947  13.093 -42.199  1.00  0.79
ATOM    736  N   TYR A 126      22.393  18.320 -44.902  1.00  0.82
ATOM    737  CA  TYR A 126      22.393  19.180 -46.064  1.00  0.82
ATOM    738  C   TYR A 126      22.825  20.602 -45.717  1.00  0.82
ATOM    739  O   TYR A 126      22.476  21.167 -44.679  1.00  0.82
ATOM    740  CB  TYR A 126      21.000  19.248 -46.741  1.00  0.82
ATOM    741  CG  TYR A 126      20.514  17.873 -47.133  1.00  0.82
ATOM    742  CD1 TYR A 126      21.066  17.187 -48.228  1.00  0.82
ATOM    743  CD2 TYR A 126      19.490  17.249 -46.404  1.00  0.82
ATOM    744  CE1 TYR A 126      20.590  15.918 -48.599  1.00  0.82
ATOM    745  CE2 TYR A 126      19.024  15.975 -46.758  1.00  0.82
ATOM    746  CZ  TYR A 126      19.558  15.314 -47.868  1.00  0.82
ATOM    747  OH  TYR A 126      19.033  14.050 -48.227  1.00  0.82
ATOM    748  N   ALA A 127      23.625  21.219 -46.608  1.00  0.88
ATOM    749  CA  ALA A 127      24.097  22.582 -46.468  1.00  0.88
ATOM    750  C   ALA A 127      23.281  23.556 -47.304  1.00  0.88
ATOM    751  O   ALA A 127      23.227  24.755 -47.030  1.00  0.88
ATOM    752  CB  ALA A 127      25.561  22.638 -46.936  1.00  0.88
ATOM    753  N   LEU A 128      22.575  23.044 -48.321  1.00  0.89
ATOM    754  CA  LEU A 128      21.664  23.821 -49.123  1.00  0.89
ATOM    755  C   LEU A 128      20.446  22.973 -49.416  1.00  0.89
ATOM    756  O   LEU A 128      20.549  21.836 -49.880  1.00  0.89
ATOM    757  CB  LEU A 128      22.354  24.293 -50.425  1.00  0.89
ATOM    758  CG  LEU A 128      21.474  25.057 -51.441  1.00  0.89
ATOM    759  CD1 LEU A 128      20.826  26.317 -50.849  1.00  0.89
ATOM    760  CD2 LEU A 128      22.322  25.449 -52.660  1.00  0.89
ATOM    761  N   VAL A 129      19.254  23.519 -49.119  1.00  0.89
ATOM    762  CA  VAL A 129      17.981  22.889 -49.406  1.00  0.89
ATOM    763  C   VAL A 129      17.156  23.859 -50.225  1.00  0.89
ATOM    764  O   VAL A 129      16.866  24.976 -49.794  1.00  0.89
ATOM    765  CB  VAL A 129      17.213  22.495 -48.151  1.00  0.89
ATOM    766  CG1 VAL A 129      15.817  21.922 -48.489  1.00  0.89
ATOM    767  CG2 VAL A 129      18.036  21.457 -47.361  1.00  0.89
ATOM    768  N   ILE A 130      16.752  23.445 -51.441  1.00  0.89
ATOM    769  CA  ILE A 130      15.837  24.194 -52.288  1.00  0.89
ATOM    770  C   ILE A 130      14.643  23.293 -52.517  1.00  0.89
ATOM    771  O   ILE A 130      14.712  22.333 -53.284  1.00  0.89
ATOM    772  CB  ILE A 130      16.480  24.586 -53.624  1.00  0.89
ATOM    773  CG1 ILE A 130      17.720  25.476 -53.359  1.00  0.89
ATOM    774  CG2 ILE A 130      15.465  25.302 -54.546  1.00  0.89
ATOM    775  CD1 ILE A 130      18.466  25.925 -54.620  1.00  0.89
ATOM    776  N   TYR A 131      13.512  23.568 -51.835  1.00  0.89
ATOM    777  CA  TYR A 131      12.407  22.627 -51.794  1.00  0.89
ATOM    778  C   TYR A 131      11.075  23.312 -52.018  1.00  0.89
ATOM    779  O   TYR A 131      10.755  24.315 -51.385  1.00  0.89
ATOM    780  CB  TYR A 131      12.408  21.858 -50.439  1.00  0.89
ATOM    781  CG  TYR A 131      11.478  20.664 -50.375  1.00  0.89
ATOM    782  CD1 TYR A 131      11.240  19.854 -51.491  1.00  0.89
ATOM    783  CD2 TYR A 131      10.890  20.289 -49.158  1.00  0.89
ATOM    784  CE1 TYR A 131      10.439  18.718 -51.414  1.00  0.89
ATOM    785  CE2 TYR A 131      10.139  19.109 -49.052  1.00  0.89
ATOM    786  CZ  TYR A 131       9.909  18.333 -50.195  1.00  0.89
ATOM    787  OH  TYR A 131       9.180  17.145 -50.197  1.00  0.89
ATOM    788  N   GLU A 132      10.275  22.789 -52.968  1.00  0.84
ATOM    789  CA  GLU A 132       8.957  23.303 -53.321  1.00  0.84
ATOM    790  C   GLU A 132       8.971  24.777 -53.720  1.00  0.84
ATOM    791  O   GLU A 132       8.082  25.569 -53.399  1.00  0.84
ATOM    792  CB  GLU A 132       7.878  23.056 -52.233  1.00  0.84
ATOM    793  CG  GLU A 132       7.433  21.586 -52.045  1.00  0.84
ATOM    794  CD  GLU A 132       6.048  21.496 -51.405  1.00  0.84
ATOM    795  OE1 GLU A 132       5.839  22.108 -50.326  1.00  0.84
ATOM    796  OE2 GLU A 132       5.169  20.836 -52.017  1.00  0.84
ATOM    797  N   MET A 133      10.002  25.190 -54.469  1.00  0.84
ATOM    798  CA  MET A 133      10.170  26.545 -54.923  1.00  0.84
ATOM    799  C   MET A 133       9.467  26.712 -56.250  1.00  0.84
ATOM    800  O   MET A 133       9.954  26.357 -57.322  1.00  0.84
ATOM    801  CB  MET A 133      11.661  26.927 -55.026  1.00  0.84
ATOM    802  CG  MET A 133      12.334  27.108 -53.652  1.00  0.84
ATOM    803  SD  MET A 133      11.865  28.619 -52.776  1.00  0.84
ATOM    804  CE  MET A 133      12.723  29.759 -53.907  1.00  0.84
ATOM    805  N   THR A 134       8.244  27.255 -56.176  1.00  0.79
ATOM    806  CA  THR A 134       7.429  27.612 -57.326  1.00  0.79
ATOM    807  C   THR A 134       7.976  28.845 -58.015  1.00  0.79
ATOM    808  O   THR A 134       8.669  29.642 -57.387  1.00  0.79
ATOM    809  CB  THR A 134       5.964  27.764 -56.949  1.00  0.79
ATOM    810  OG1 THR A 134       5.121  27.826 -58.082  1.00  0.79
ATOM    811  CG2 THR A 134       5.697  29.010 -56.095  1.00  0.79
ATOM    812  N   SER A 135       7.749  28.997 -59.334  1.00  0.79
ATOM    813  CA  SER A 135       8.293  30.082 -60.160  1.00  0.79
ATOM    814  C   SER A 135       9.816  30.079 -60.359  1.00  0.79
ATOM    815  O   SER A 135      10.333  30.753 -61.241  1.00  0.79
ATOM    816  CB  SER A 135       7.934  31.531 -59.685  1.00  0.79
ATOM    817  OG  SER A 135       6.569  31.707 -59.296  1.00  0.79
ATOM    818  N   LEU A 136      10.600  29.348 -59.537  1.00  0.81
ATOM    819  CA  LEU A 136      12.053  29.326 -59.584  1.00  0.81
ATOM    820  C   LEU A 136      12.629  28.584 -60.790  1.00  0.81
ATOM    821  O   LEU A 136      12.423  27.386 -60.972  1.00  0.81
ATOM    822  CB  LEU A 136      12.613  28.733 -58.261  1.00  0.81
ATOM    823  CG  LEU A 136      14.113  28.994 -57.983  1.00  0.81
ATOM    824  CD1 LEU A 136      14.366  30.454 -57.591  1.00  0.81
ATOM    825  CD2 LEU A 136      14.649  28.082 -56.869  1.00  0.81
ATOM    826  N   LYS A 137      13.390  29.295 -61.643  1.00  0.80
ATOM    827  CA  LYS A 137      13.860  28.828 -62.928  1.00  0.80
ATOM    828  C   LYS A 137      15.319  28.429 -62.929  1.00  0.80
ATOM    829  O   LYS A 137      15.716  27.559 -63.698  1.00  0.80
ATOM    830  CB  LYS A 137      13.718  29.967 -63.960  1.00  0.80
ATOM    831  CG  LYS A 137      12.275  30.463 -64.056  1.00  0.80
ATOM    832  CD  LYS A 137      12.097  31.575 -65.090  1.00  0.80
ATOM    833  CE  LYS A 137      10.656  32.076 -65.087  1.00  0.80
ATOM    834  NZ  LYS A 137      10.530  33.263 -65.950  1.00  0.80
ATOM    835  N   ASP A 138      16.149  29.003 -62.045  1.00  0.83
ATOM    836  CA  ASP A 138      17.547  28.650 -61.983  1.00  0.83
ATOM    837  C   ASP A 138      18.150  28.887 -60.606  1.00  0.83
ATOM    838  O   ASP A 138      17.677  29.681 -59.786  1.00  0.83
ATOM    839  CB  ASP A 138      18.380  29.331 -63.093  1.00  0.83
ATOM    840  CG  ASP A 138      18.289  30.825 -63.117  1.00  0.83
ATOM    841  OD1 ASP A 138      17.356  31.458 -63.668  1.00  0.83
ATOM    842  OD2 ASP A 138      19.311  31.375 -62.630  1.00  0.83
ATOM    843  N   ILE A 139      19.258  28.177 -60.314  1.00  0.82
ATOM    844  CA  ILE A 139      20.086  28.462 -59.159  1.00  0.82
ATOM    845  C   ILE A 139      21.087  29.518 -59.587  1.00  0.82
ATOM    846  O   ILE A 139      22.191  29.233 -60.036  1.00  0.82
ATOM    847  CB  ILE A 139      20.819  27.243 -58.588  1.00  0.82
ATOM    848  CG1 ILE A 139      19.844  26.122 -58.156  1.00  0.82
ATOM    849  CG2 ILE A 139      21.704  27.654 -57.385  1.00  0.82
ATOM    850  CD1 ILE A 139      19.659  25.040 -59.228  1.00  0.82
ATOM    851  N   GLY A 140      20.736  30.807 -59.439  1.00  0.85
ATOM    852  CA  GLY A 140      21.538  31.897 -59.981  1.00  0.85
ATOM    853  C   GLY A 140      22.747  32.288 -59.174  1.00  0.85
ATOM    854  O   GLY A 140      23.295  33.371 -59.344  1.00  0.85
ATOM    855  N   LEU A 141      23.209  31.427 -58.256  1.00  0.81
ATOM    856  CA  LEU A 141      24.360  31.668 -57.405  1.00  0.81
ATOM    857  C   LEU A 141      25.676  31.533 -58.164  1.00  0.81
ATOM    858  O   LEU A 141      26.500  30.666 -57.894  1.00  0.81
ATOM    859  CB  LEU A 141      24.364  30.713 -56.180  1.00  0.81
ATOM    860  CG  LEU A 141      23.096  30.767 -55.300  1.00  0.81
ATOM    861  CD1 LEU A 141      23.182  29.736 -54.161  1.00  0.81
ATOM    862  CD2 LEU A 141      22.859  32.170 -54.720  1.00  0.81
ATOM    863  N   TYR A 142      25.914  32.427 -59.142  1.00  0.78
ATOM    864  CA  TYR A 142      26.997  32.323 -60.100  1.00  0.78
ATOM    865  C   TYR A 142      28.382  32.590 -59.549  1.00  0.78
ATOM    866  O   TYR A 142      29.392  32.205 -60.141  1.00  0.78
ATOM    867  CB  TYR A 142      26.717  33.147 -61.390  1.00  0.78
ATOM    868  CG  TYR A 142      26.235  34.559 -61.149  1.00  0.78
ATOM    869  CD1 TYR A 142      27.081  35.546 -60.615  1.00  0.78
ATOM    870  CD2 TYR A 142      24.933  34.928 -61.530  1.00  0.78
ATOM    871  CE1 TYR A 142      26.630  36.865 -60.454  1.00  0.78
ATOM    872  CE2 TYR A 142      24.478  36.242 -61.359  1.00  0.78
ATOM    873  CZ  TYR A 142      25.325  37.209 -60.814  1.00  0.78
ATOM    874  OH  TYR A 142      24.872  38.532 -60.636  1.00  0.78
ATOM    875  N   ASN A 143      28.445  33.204 -58.362  1.00  0.82
ATOM    876  CA  ASN A 143      29.670  33.385 -57.626  1.00  0.82
ATOM    877  C   ASN A 143      29.904  32.287 -56.594  1.00  0.82
ATOM    878  O   ASN A 143      30.926  32.308 -55.915  1.00  0.82
ATOM    879  CB  ASN A 143      29.635  34.759 -56.916  1.00  0.82
ATOM    880  CG  ASN A 143      29.927  35.858 -57.930  1.00  0.82
ATOM    881  OD1 ASN A 143      30.846  35.744 -58.745  1.00  0.82
ATOM    882  ND2 ASN A 143      29.164  36.968 -57.885  1.00  0.82
ATOM    883  N   LEU A 144      29.023  31.266 -56.466  1.00  0.84
ATOM    884  CA  LEU A 144      29.215  30.169 -55.528  1.00  0.84
ATOM    885  C   LEU A 144      30.411  29.295 -55.888  1.00  0.84
ATOM    886  O   LEU A 144      30.527  28.778 -56.998  1.00  0.84
ATOM    887  CB  LEU A 144      27.929  29.317 -55.405  1.00  0.84
ATOM    888  CG  LEU A 144      27.928  28.201 -54.337  1.00  0.84
ATOM    889  CD1 LEU A 144      27.996  28.757 -52.905  1.00  0.84
ATOM    890  CD2 LEU A 144      26.676  27.326 -54.500  1.00  0.84
ATOM    891  N   ARG A 145      31.360  29.127 -54.944  1.00  0.80
ATOM    892  CA  ARG A 145      32.636  28.511 -55.245  1.00  0.80
ATOM    893  C   ARG A 145      33.013  27.397 -54.303  1.00  0.80
ATOM    894  O   ARG A 145      33.761  26.506 -54.694  1.00  0.80
ATOM    895  CB  ARG A 145      33.782  29.547 -55.114  1.00  0.80
ATOM    896  CG  ARG A 145      33.874  30.604 -56.229  1.00  0.80
ATOM    897  CD  ARG A 145      33.836  30.035 -57.651  1.00  0.80
ATOM    898  NE  ARG A 145      34.552  31.022 -58.525  1.00  0.80
ATOM    899  CZ  ARG A 145      35.871  30.968 -58.771  1.00  0.80
ATOM    900  NH1 ARG A 145      36.637  30.035 -58.212  1.00  0.80
ATOM    901  NH2 ARG A 145      36.428  31.866 -59.581  1.00  0.80
ATOM    902  N   ASN A 146      32.544  27.401 -53.046  1.00  0.83
ATOM    903  CA  ASN A 146      32.880  26.326 -52.144  1.00  0.83
ATOM    904  C   ASN A 146      31.724  26.116 -51.184  1.00  0.83
ATOM    905  O   ASN A 146      31.188  27.053 -50.591  1.00  0.83
ATOM    906  CB  ASN A 146      34.241  26.612 -51.442  1.00  0.83
ATOM    907  CG  ASN A 146      34.717  25.479 -50.534  1.00  0.83
ATOM    908  OD1 ASN A 146      34.161  25.236 -49.468  1.00  0.83
ATOM    909  ND2 ASN A 146      35.808  24.783 -50.924  1.00  0.83
ATOM    910  N   ILE A 147      31.313  24.851 -51.027  1.00  0.81
ATOM    911  CA  ILE A 147      30.442  24.404 -49.968  1.00  0.81
ATOM    912  C   ILE A 147      31.253  23.411 -49.159  1.00  0.81
ATOM    913  O   ILE A 147      31.544  22.301 -49.603  1.00  0.81
ATOM    914  CB  ILE A 147      29.131  23.805 -50.482  1.00  0.81
ATOM    915  CG1 ILE A 147      28.313  24.889 -51.237  1.00  0.81
ATOM    916  CG2 ILE A 147      28.336  23.221 -49.291  1.00  0.81
ATOM    917  CD1 ILE A 147      26.934  24.438 -51.745  1.00  0.81
ATOM    918  N   THR A 148      31.677  23.822 -47.946  1.00  0.78
ATOM    919  CA  THR A 148      32.715  23.149 -47.170  1.00  0.78
ATOM    920  C   THR A 148      32.361  21.748 -46.703  1.00  0.78
ATOM    921  O   THR A 148      33.187  20.837 -46.746  1.00  0.78
ATOM    922  CB  THR A 148      33.152  23.967 -45.951  1.00  0.78
ATOM    923  OG1 THR A 148      33.350  25.330 -46.294  1.00  0.78
ATOM    924  CG2 THR A 148      34.487  23.465 -45.383  1.00  0.78
ATOM    925  N   ARG A 149      31.118  21.540 -46.216  1.00  0.73
ATOM    926  CA  ARG A 149      30.769  20.348 -45.454  1.00  0.73
ATOM    927  C   ARG A 149      29.644  19.506 -46.037  1.00  0.73
ATOM    928  O   ARG A 149      29.874  18.418 -46.561  1.00  0.73
ATOM    929  CB  ARG A 149      30.445  20.738 -43.984  1.00  0.73
ATOM    930  CG  ARG A 149      30.270  19.541 -43.018  1.00  0.73
ATOM    931  CD  ARG A 149      30.038  19.981 -41.565  1.00  0.73
ATOM    932  NE  ARG A 149      29.804  18.758 -40.733  1.00  0.73
ATOM    933  CZ  ARG A 149      29.765  18.785 -39.394  1.00  0.73
ATOM    934  NH1 ARG A 149      29.920  19.910 -38.706  1.00  0.73
ATOM    935  NH2 ARG A 149      29.555  17.656 -38.719  1.00  0.73
ATOM    936  N   GLY A 150      28.375  19.933 -45.869  1.00  0.81
ATOM    937  CA  GLY A 150      27.230  19.091 -46.196  1.00  0.81
ATOM    938  C   GLY A 150      26.888  18.981 -47.649  1.00  0.81
ATOM    939  O   GLY A 150      27.403  19.692 -48.505  1.00  0.81
ATOM    940  N   ALA A 151      25.920  18.094 -47.927  1.00  0.82
ATOM    941  CA  ALA A 151      25.411  17.826 -49.251  1.00  0.82
ATOM    942  C   ALA A 151      24.272  18.766 -49.619  1.00  0.82
ATOM    943  O   ALA A 151      23.880  19.657 -48.866  1.00  0.82
ATOM    944  CB  ALA A 151      24.945  16.361 -49.361  1.00  0.82
ATOM    945  N   MET A 152      23.716  18.605 -50.823  1.00  0.85
ATOM    946  CA  MET A 152      22.670  19.458 -51.338  1.00  0.85
ATOM    947  C   MET A 152      21.399  18.689 -51.642  1.00  0.85
ATOM    948  O   MET A 152      21.418  17.602 -52.223  1.00  0.85
ATOM    949  CB  MET A 152      23.192  20.152 -52.605  1.00  0.85
ATOM    950  CG  MET A 152      22.219  21.136 -53.268  1.00  0.85
ATOM    951  SD  MET A 152      22.924  21.938 -54.727  1.00  0.85
ATOM    952  CE  MET A 152      22.804  20.451 -55.760  1.00  0.85
ATOM    953  N   ARG A 153      20.243  19.265 -51.245  1.00  0.86
ATOM    954  CA  ARG A 153      18.940  18.740 -51.587  1.00  0.86
ATOM    955  C   ARG A 153      18.143  19.747 -52.409  1.00  0.86
ATOM    956  O   ARG A 153      17.767  20.814 -51.931  1.00  0.86
ATOM    957  CB  ARG A 153      18.162  18.302 -50.326  1.00  0.86
ATOM    958  CG  ARG A 153      17.007  17.327 -50.635  1.00  0.86
ATOM    959  CD  ARG A 153      16.391  16.693 -49.379  1.00  0.86
ATOM    960  NE  ARG A 153      16.478  15.198 -49.445  1.00  0.86
ATOM    961  CZ  ARG A 153      15.433  14.373 -49.579  1.00  0.86
ATOM    962  NH1 ARG A 153      14.197  14.778 -49.814  1.00  0.86
ATOM    963  NH2 ARG A 153      15.633  13.067 -49.427  1.00  0.86
ATOM    964  N   ILE A 154      17.865  19.440 -53.691  1.00  0.86
ATOM    965  CA  ILE A 154      17.071  20.297 -54.569  1.00  0.86
ATOM    966  C   ILE A 154      15.888  19.488 -55.068  1.00  0.86
ATOM    967  O   ILE A 154      16.052  18.525 -55.816  1.00  0.86
ATOM    968  CB  ILE A 154      17.858  20.853 -55.760  1.00  0.86
ATOM    969  CG1 ILE A 154      19.028  21.750 -55.295  1.00  0.86
ATOM    970  CG2 ILE A 154      16.913  21.650 -56.682  1.00  0.86
ATOM    971  CD1 ILE A 154      19.842  22.354 -56.450  1.00  0.86
ATOM    972  N   GLU A 155      14.652  19.846 -54.674  1.00  0.85
ATOM    973  CA  GLU A 155      13.533  18.944 -54.861  1.00  0.85
ATOM    974  C   GLU A 155      12.213  19.659 -55.092  1.00  0.85
ATOM    975  O   GLU A 155      11.967  20.759 -54.605  1.00  0.85
ATOM    976  CB  GLU A 155      13.472  18.005 -53.634  1.00  0.85
ATOM    977  CG  GLU A 155      12.510  16.799 -53.688  1.00  0.85
ATOM    978  CD  GLU A 155      12.424  16.137 -52.323  1.00  0.85
ATOM    979  OE1 GLU A 155      13.202  16.528 -51.410  1.00  0.85
ATOM    980  OE2 GLU A 155      11.604  15.201 -52.175  1.00  0.85
ATOM    981  N   LYS A 156      11.325  19.043 -55.896  1.00  0.85
ATOM    982  CA  LYS A 156       9.985  19.526 -56.206  1.00  0.85
ATOM    983  C   LYS A 156       9.912  20.940 -56.767  1.00  0.85
ATOM    984  O   LYS A 156       9.046  21.736 -56.413  1.00  0.85
ATOM    985  CB  LYS A 156       9.002  19.330 -55.027  1.00  0.85
ATOM    986  CG  LYS A 156       8.663  17.861 -54.750  1.00  0.85
ATOM    987  CD  LYS A 156       7.677  17.748 -53.577  1.00  0.85
ATOM    988  CE  LYS A 156       7.623  16.338 -52.983  1.00  0.85
ATOM    989  NZ  LYS A 156       6.669  16.271 -51.864  1.00  0.85
ATOM    990  N   ASN A 157      10.809  21.279 -57.707  1.00  0.85
ATOM    991  CA  ASN A 157      10.810  22.594 -58.316  1.00  0.85
ATOM    992  C   ASN A 157      10.467  22.466 -59.798  1.00  0.85
ATOM    993  O   ASN A 157      11.364  22.225 -60.612  1.00  0.85
ATOM    994  CB  ASN A 157      12.179  23.281 -58.136  1.00  0.85
ATOM    995  CG  ASN A 157      12.592  23.230 -56.671  1.00  0.85
ATOM    996  OD1 ASN A 157      11.937  23.758 -55.779  1.00  0.85
ATOM    997  ND2 ASN A 157      13.721  22.550 -56.396  1.00  0.85
ATOM    998  N   PRO A 158       9.211  22.621 -60.229  1.00  0.83
ATOM    999  CA  PRO A 158       8.776  22.105 -61.527  1.00  0.83
ATOM   1000  C   PRO A 158       9.211  22.984 -62.675  1.00  0.83
ATOM   1001  O   PRO A 158       9.062  22.580 -63.826  1.00  0.83
ATOM   1002  CB  PRO A 158       7.240  22.058 -61.415  1.00  0.83
ATOM   1003  CG  PRO A 158       6.896  23.068 -60.318  1.00  0.83
ATOM   1004  CD  PRO A 158       8.066  22.903 -59.356  1.00  0.83
ATOM   1005  N   GLU A 159       9.734  24.187 -62.394  1.00  0.78
ATOM   1006  CA  GLU A 159      10.201  25.107 -63.403  1.00  0.78
ATOM   1007  C   GLU A 159      11.714  25.239 -63.424  1.00  0.78
ATOM   1008  O   GLU A 159      12.272  25.861 -64.328  1.00  0.78
ATOM   1009  CB  GLU A 159       9.533  26.475 -63.168  1.00  0.78
ATOM   1010  CG  GLU A 159       8.004  26.371 -63.395  1.00  0.78
ATOM   1011  CD  GLU A 159       7.260  27.700 -63.468  1.00  0.78
ATOM   1012  OE1 GLU A 159       7.902  28.778 -63.429  1.00  0.78
ATOM   1013  OE2 GLU A 159       6.013  27.617 -63.599  1.00  0.78
ATOM   1014  N   LEU A 160      12.413  24.595 -62.466  1.00  0.82
ATOM   1015  CA  LEU A 160      13.842  24.738 -62.267  1.00  0.82
ATOM   1016  C   LEU A 160      14.690  24.085 -63.340  1.00  0.82
ATOM   1017  O   LEU A 160      14.598  22.891 -63.598  1.00  0.82
ATOM   1018  CB  LEU A 160      14.244  24.204 -60.873  1.00  0.82
ATOM   1019  CG  LEU A 160      15.575  24.734 -60.301  1.00  0.82
ATOM   1020  CD1 LEU A 160      15.469  26.216 -59.933  1.00  0.82
ATOM   1021  CD2 LEU A 160      15.964  23.956 -59.039  1.00  0.82
ATOM   1022  N   CYS A 161      15.556  24.871 -63.982  1.00  0.82
ATOM   1023  CA  CYS A 161      16.447  24.477 -65.043  1.00  0.82
ATOM   1024  C   CYS A 161      17.869  24.665 -64.548  1.00  0.82
ATOM   1025  O   CYS A 161      18.094  25.053 -63.403  1.00  0.82
ATOM   1026  CB  CYS A 161      16.187  25.337 -66.312  1.00  0.82
ATOM   1027  SG  CYS A 161      14.928  24.622 -67.413  1.00  0.82
ATOM   1028  N   TYR A 162      18.870  24.332 -65.396  1.00  0.78
ATOM   1029  CA  TYR A 162      20.285  24.502 -65.088  1.00  0.78
ATOM   1030  C   TYR A 162      20.763  23.655 -63.905  1.00  0.78
ATOM   1031  O   TYR A 162      21.468  24.118 -63.011  1.00  0.78
ATOM   1032  CB  TYR A 162      20.692  25.998 -64.905  1.00  0.78
ATOM   1033  CG  TYR A 162      20.477  26.806 -66.162  1.00  0.78
ATOM   1034  CD1 TYR A 162      21.496  26.931 -67.121  1.00  0.78
ATOM   1035  CD2 TYR A 162      19.257  27.462 -66.393  1.00  0.78
ATOM   1036  CE1 TYR A 162      21.298  27.681 -68.288  1.00  0.78
ATOM   1037  CE2 TYR A 162      19.037  28.176 -67.579  1.00  0.78
ATOM   1038  CZ  TYR A 162      20.056  28.275 -68.527  1.00  0.78
ATOM   1039  OH  TYR A 162      19.820  28.955 -69.732  1.00  0.78
ATOM   1040  N   LEU A 163      20.376  22.361 -63.872  1.00  0.80
ATOM   1041  CA  LEU A 163      20.773  21.447 -62.811  1.00  0.80
ATOM   1042  C   LEU A 163      21.992  20.620 -63.192  1.00  0.80
ATOM   1043  O   LEU A 163      22.869  20.362 -62.370  1.00  0.80
ATOM   1044  CB  LEU A 163      19.630  20.469 -62.428  1.00  0.80
ATOM   1045  CG  LEU A 163      18.268  21.147 -62.174  1.00  0.80
ATOM   1046  CD1 LEU A 163      17.333  20.966 -63.379  1.00  0.80
ATOM   1047  CD2 LEU A 163      17.582  20.603 -60.913  1.00  0.80
ATOM   1048  N   ASP A 164      22.085  20.209 -64.469  1.00  0.78
ATOM   1049  CA  ASP A 164      23.097  19.349 -65.034  1.00  0.78
ATOM   1050  C   ASP A 164      24.214  20.166 -65.679  1.00  0.78
ATOM   1051  O   ASP A 164      25.285  19.660 -66.004  1.00  0.78
ATOM   1052  CB  ASP A 164      22.426  18.448 -66.120  1.00  0.78
ATOM   1053  CG  ASP A 164      21.572  19.191 -67.159  1.00  0.78
ATOM   1054  OD1 ASP A 164      21.062  20.313 -66.888  1.00  0.78
ATOM   1055  OD2 ASP A 164      21.399  18.624 -68.264  1.00  0.78
ATOM   1056  N   SER A 165      23.997  21.488 -65.800  1.00  0.82
ATOM   1057  CA  SER A 165      24.975  22.470 -66.246  1.00  0.82
ATOM   1058  C   SER A 165      25.863  22.947 -65.126  1.00  0.82
ATOM   1059  O   SER A 165      26.834  23.667 -65.352  1.00  0.82
ATOM   1060  CB  SER A 165      24.305  23.762 -66.778  1.00  0.82
ATOM   1061  OG  SER A 165      23.386  24.303 -65.830  1.00  0.82
ATOM   1062  N   VAL A 166      25.548  22.587 -63.876  1.00  0.85
ATOM   1063  CA  VAL A 166      26.346  22.989 -62.747  1.00  0.85
ATOM   1064  C   VAL A 166      27.162  21.802 -62.336  1.00  0.85
ATOM   1065  O   VAL A 166      26.664  20.755 -61.927  1.00  0.85
ATOM   1066  CB  VAL A 166      25.536  23.494 -61.571  1.00  0.85
ATOM   1067  CG1 VAL A 166      26.481  23.921 -60.426  1.00  0.85
ATOM   1068  CG2 VAL A 166      24.677  24.682 -62.040  1.00  0.85
ATOM   1069  N   ASP A 167      28.485  21.946 -62.439  1.00  0.82
ATOM   1070  CA  ASP A 167      29.396  20.952 -61.962  1.00  0.82
ATOM   1071  C   ASP A 167      29.587  21.160 -60.477  1.00  0.82
ATOM   1072  O   ASP A 167      30.220  22.108 -60.016  1.00  0.82
ATOM   1073  CB  ASP A 167      30.682  21.083 -62.784  1.00  0.82
ATOM   1074  CG  ASP A 167      31.753  20.093 -62.393  1.00  0.82
ATOM   1075  OD1 ASP A 167      32.160  20.115 -61.206  1.00  0.82
ATOM   1076  OD2 ASP A 167      32.189  19.337 -63.292  1.00  0.82
ATOM   1077  N   TRP A 168      28.981  20.259 -59.692  1.00  0.76
ATOM   1078  CA  TRP A 168      28.984  20.362 -58.260  1.00  0.76
ATOM   1079  C   TRP A 168      30.215  19.706 -57.649  1.00  0.76
ATOM   1080  O   TRP A 168      30.509  19.944 -56.482  1.00  0.76
ATOM   1081  CB  TRP A 168      27.677  19.745 -57.685  1.00  0.76
ATOM   1082  CG  TRP A 168      26.377  20.351 -58.230  1.00  0.76
ATOM   1083  CD1 TRP A 168      25.572  19.871 -59.229  1.00  0.76
ATOM   1084  CD2 TRP A 168      25.767  21.570 -57.769  1.00  0.76
ATOM   1085  NE1 TRP A 168      24.508  20.718 -59.434  1.00  0.76
ATOM   1086  CE2 TRP A 168      24.597  21.765 -58.554  1.00  0.76
ATOM   1087  CE3 TRP A 168      26.120  22.486 -56.783  1.00  0.76
ATOM   1088  CZ2 TRP A 168      23.784  22.868 -58.351  1.00  0.76
ATOM   1089  CZ3 TRP A 168      25.302  23.609 -56.594  1.00  0.76
ATOM   1090  CH2 TRP A 168      24.144  23.796 -57.365  1.00  0.76
ATOM   1091  N   SER A 169      31.004  18.924 -58.421  1.00  0.75
ATOM   1092  CA  SER A 169      32.194  18.229 -57.933  1.00  0.75
ATOM   1093  C   SER A 169      33.339  19.172 -57.600  1.00  0.75
ATOM   1094  O   SER A 169      34.145  18.924 -56.706  1.00  0.75
ATOM   1095  CB  SER A 169      32.675  17.112 -58.905  1.00  0.75
ATOM   1096  OG  SER A 169      33.342  17.609 -60.069  1.00  0.75
ATOM   1097  N   PHE A 170      33.396  20.334 -58.281  1.00  0.72
ATOM   1098  CA  PHE A 170      34.322  21.398 -57.943  1.00  0.72
ATOM   1099  C   PHE A 170      33.729  22.463 -57.032  1.00  0.72
ATOM   1100  O   PHE A 170      34.396  23.448 -56.725  1.00  0.72
ATOM   1101  CB  PHE A 170      34.807  22.107 -59.232  1.00  0.72
ATOM   1102  CG  PHE A 170      35.597  21.170 -60.103  1.00  0.72
ATOM   1103  CD1 PHE A 170      35.310  21.097 -61.474  1.00  0.72
ATOM   1104  CD2 PHE A 170      36.603  20.337 -59.577  1.00  0.72
ATOM   1105  CE1 PHE A 170      35.973  20.177 -62.293  1.00  0.72
ATOM   1106  CE2 PHE A 170      37.256  19.405 -60.392  1.00  0.72
ATOM   1107  CZ  PHE A 170      36.937  19.322 -61.751  1.00  0.72
ATOM   1108  N   ILE A 171      32.478  22.306 -56.553  1.00  0.79
ATOM   1109  CA  ILE A 171      31.886  23.264 -55.620  1.00  0.79
ATOM   1110  C   ILE A 171      31.748  22.627 -54.245  1.00  0.79
ATOM   1111  O   ILE A 171      31.848  23.299 -53.222  1.00  0.79
ATOM   1112  CB  ILE A 171      30.517  23.772 -56.086  1.00  0.79
ATOM   1113  CG1 ILE A 171      30.575  24.296 -57.540  1.00  0.79
ATOM   1114  CG2 ILE A 171      30.023  24.910 -55.156  1.00  0.79
ATOM   1115  CD1 ILE A 171      29.183  24.555 -58.128  1.00  0.79
ATOM   1116  N   MET A 172      31.565  21.298 -54.163  1.00  0.78
ATOM   1117  CA  MET A 172      31.465  20.597 -52.898  1.00  0.78
ATOM   1118  C   MET A 172      32.099  19.232 -52.980  1.00  0.78
ATOM   1119  O   MET A 172      32.260  18.661 -54.054  1.00  0.78
ATOM   1120  CB  MET A 172      30.001  20.393 -52.456  1.00  0.78
ATOM   1121  CG  MET A 172      29.169  19.459 -53.356  1.00  0.78
ATOM   1122  SD  MET A 172      27.461  19.294 -52.778  1.00  0.78
ATOM   1123  CE  MET A 172      26.924  20.903 -53.406  1.00  0.78
ATOM   1124  N   ASN A 173      32.464  18.649 -51.826  1.00  0.73
ATOM   1125  CA  ASN A 173      33.181  17.391 -51.800  1.00  0.73
ATOM   1126  C   ASN A 173      32.284  16.157 -51.866  1.00  0.73
ATOM   1127  O   ASN A 173      32.533  15.210 -52.604  1.00  0.73
ATOM   1128  CB  ASN A 173      34.053  17.314 -50.523  1.00  0.73
ATOM   1129  CG  ASN A 173      35.126  18.396 -50.567  1.00  0.73
ATOM   1130  OD1 ASN A 173      35.682  18.731 -51.611  1.00  0.73
ATOM   1131  ND2 ASN A 173      35.468  18.962 -49.388  1.00  0.73
ATOM   1132  N   THR A 174      31.191  16.110 -51.084  1.00  0.72
ATOM   1133  CA  THR A 174      30.373  14.913 -50.901  1.00  0.72
ATOM   1134  C   THR A 174      29.286  14.770 -51.937  1.00  0.72
ATOM   1135  O   THR A 174      28.126  14.506 -51.625  1.00  0.72
ATOM   1136  CB  THR A 174      29.740  14.837 -49.518  1.00  0.72
ATOM   1137  OG1 THR A 174      29.257  16.121 -49.147  1.00  0.72
ATOM   1138  CG2 THR A 174      30.810  14.403 -48.507  1.00  0.72
ATOM   1139  N   GLU A 175      29.657  14.848 -53.228  1.00  0.71
ATOM   1140  CA  GLU A 175      28.754  14.739 -54.360  1.00  0.71
ATOM   1141  C   GLU A 175      27.915  13.473 -54.346  1.00  0.71
ATOM   1142  O   GLU A 175      26.719  13.497 -54.627  1.00  0.71
ATOM   1143  CB  GLU A 175      29.493  14.929 -55.708  1.00  0.71
ATOM   1144  CG  GLU A 175      30.408  13.772 -56.189  1.00  0.71
ATOM   1145  CD  GLU A 175      31.028  14.091 -57.551  1.00  0.71
ATOM   1146  OE1 GLU A 175      30.286  14.591 -58.437  1.00  0.71
ATOM   1147  OE2 GLU A 175      32.246  13.829 -57.710  1.00  0.71
SPDBVT        1.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         1.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         1.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVV default;
SPDBVV      2.884198722130    1202.311745758954      20.000000000000
SPDBVV        0.8633539277        -0.4937879037         0.1038917782 
SPDBVV        0.2777525752         0.6369368281         0.7191418386 
SPDBVV       -0.4212760406        -0.5920177220         0.6870527741 
SPDBVV       17.2490000000       -24.7960000000       -65.3230000000 
SPDBVV        0.0000000000         0.0000000000         0.0000000000 
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3  3
SPDBVf  3
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 
SPDBVb 0.00 0.00 0.20
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64
SPDBVi        1 1 1 0 1 0 1 1 0 1 0 1 1 0  0
SPDBVp        0
END



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.