CNRS Nantes University UFIP UFIP
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elNémo ID: 21120215544649895

Job options:

ID        	=	 21120215544649895
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   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.19.2_4158: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65    
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.66   
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.99 
REMARK   3   NUMBER OF REFLECTIONS             : 28851     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 15737     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1902
REMARK   3   R VALUE            (WORKING SET) : 0.1880
REMARK   3   FREE R VALUE                     : 0.2233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.28  
REMARK   3   FREE R VALUE TEST SET COUNT      : 1813      
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE  CCWORK CCFREE
REMARK   3     1   34.66 -    3.88    0.98     2068   147  0.1531 0.1820   0.938  0.911
REMARK   3     2    3.88 -    3.08    0.96     2029   136  0.1738 0.2010   0.926  0.893
REMARK   3     3    3.08 -    2.69    0.98     2080   140  0.1851 0.2291   0.910  0.867
REMARK   3     4    2.69 -    2.44    0.98     2061   138  0.1989 0.2461   0.905  0.756
REMARK   3     5    2.44 -    2.27    0.96     2059   134  0.1921 0.2100   0.905  0.871
REMARK   3     6    2.27 -    2.14    0.95     2021   130  0.1959 0.2659   0.904  0.776
REMARK   3     7    2.13 -    2.03    0.98     2074   139  0.2052 0.2353   0.915  0.900
REMARK   3     8    2.03 -    1.94    0.99     2113   139  0.2239 0.2814   0.891  0.744
REMARK   3     9    1.94 -    1.87    0.99     2091   143  0.2192 0.2856   0.883  0.651
REMARK   3    10    1.87 -    1.80    0.99     2107   140  0.2370 0.2599   0.874  0.823
REMARK   3    11    1.80 -    1.74    1.00     2105   142  0.2474 0.2927   0.882  0.794
REMARK   3    12    1.74 -    1.69    1.00     2109   146  0.2721 0.3003   0.864  0.805
REMARK   3    13    1.69 -    1.65    1.00     2121   139  0.3337 0.3748   0.786  0.732
REMARK   3  
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11    
REMARK   3   SHRINKAGE RADIUS   : 0.90    
REMARK   3   GRID STEP FACTOR   : 4.00    
REMARK   3  
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.22    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.04   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 26.19   
REMARK   3  
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.012   0.088   1181
REMARK   3    ANGLE     :  1.202   7.877   1613
REMARK   3    CHIRALITY :  0.083   0.278    173
REMARK   3    PLANARITY :  0.010   0.064    220
REMARK   3    DIHEDRAL  :  5.744  22.290    168
REMARK   3    MIN NONBONDED DISTANCE : 1.746
REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 9.19
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS :  0.00 %
REMARK   3      ALLOWED  :  1.53 %
REMARK   3      FAVORED  : 98.47 %
REMARK   3    ROTAMER OUTLIERS :  0.79 %
REMARK   3    CBETA DEVIATIONS :  0.00 %
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 0.00 %
REMARK   3      CIS-GENERAL     : 0.00 %
REMARK   3      TWISTED PROLINE : 0.00 %
REMARK   3      TWISTED GENERAL : 0.00 %
REMARK   3  
REMARK   3  RAMA-Z (RAMACHANDRAN PLOT Z-SCORE):
REMARK   3  INTERPRETATION: BAD |RAMA-Z| > 3; SUSPICIOUS 2 < |RAMA-Z| < 3; GOOD |RAMA-Z| < 2.
REMARK   3  SCORES FOR WHOLE/HELIX/SHEET/LOOP ARE SCALED INDEPENDENTLY;
REMARK   3  THEREFORE, THE VALUES ARE NOT RELATED IN A SIMPLE MANNER.
REMARK   3    WHOLE: -0.54 (0.60), RESIDUES: 164
REMARK   3    HELIX: -1.60 (0.51), RESIDUES: 62
REMARK   3    SHEET: -0.56 (0.64), RESIDUES: 51
REMARK   3    LOOP :  2.18 (0.87), RESIDUES: 51
REMARK   3  
REMARK   3                  min    max   mean    iso aniso
REMARK   3     Overall:   18.29  92.11  33.09   3.44  1257  1149
REMARK   3     Protein:   18.29  92.11  32.61   3.44  1149  1149
REMARK   3     Water:     23.03  54.38  38.24    N/A   108     0
REMARK   3     Chain  A:  18.29  92.11  32.61    N/A  1149  1149
REMARK   3     Chain  S:  23.03  54.38  38.24    N/A   108     0
REMARK   3     Histogram:
REMARK   3         Values      Number of atoms
REMARK   3      18.29 - 25.67       295
REMARK   3      25.67 - 33.06       426
REMARK   3      33.06 - 40.44       325
REMARK   3      40.44 - 47.82       129
REMARK   3      47.82 - 55.20        43
REMARK   3      55.20 - 62.58        15
REMARK   3      62.58 - 69.96        12
REMARK   3      69.96 - 77.34         6
REMARK   3      77.34 - 84.73         2
REMARK   3      84.73 - 92.11         4
REMARK   3  
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 1     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: (chain 'A' and resid 2 through 134)
REMARK   3    ORIGIN FOR THE GROUP (A): -16.5995  -3.7596   6.6632
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1923 T22:   0.1784                       
REMARK   3      T33:   0.1941 T12:  -0.0198                       
REMARK   3      T13:   0.0489 T23:  -0.0179                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   2.3324 L22:   2.3972                       
REMARK   3      L33:   2.3891 L12:   0.3283                       
REMARK   3      L13:   0.5520 L23:   0.5738                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.1297 S12:  -0.0928 S13:   0.1708         
REMARK   3      S21:   0.0982 S22:  -0.0610 S23:  -0.0050         
REMARK   3      S31:  -0.1073 S32:  -0.1253 S33:  -0.0691         
REMARK   3
CRYST1   39.810   45.800   69.310  90.00  90.00  90.00 P 21 21 21
SCALE1      0.025119  0.000000  0.000000        0.00000
SCALE2      0.000000  0.021834  0.000000        0.00000
SCALE3      0.000000  0.000000  0.014428        0.00000
ATOM      1  N   GLY A   2      -0.395   3.272  19.937  1.00 69.70           N
ANISOU    1  N   GLY A   2     8677   8661   9145  -1262   -919  -1426       N
ATOM      2  CA  GLY A   2      -1.670   3.267  19.249  1.00 53.30           C
ANISOU    2  CA  GLY A   2     6697   6527   7027  -1187   -718  -1342       C
ATOM      3  C   GLY A   2      -1.534   2.630  17.884  1.00 52.11           C
ANISOU    3  C   GLY A   2     6419   6373   7010  -1124   -621  -1212       C
ATOM      4  O   GLY A   2      -0.668   3.007  17.097  1.00 54.19           O
ANISOU    4  O   GLY A   2     6532   6604   7452  -1180   -591  -1219       O
ATOM      5  N   ILE A   3      -2.399   1.656  17.617  1.00 47.91           N
ANISOU    5  N   ILE A   3     5947   5879   6380  -1018   -568  -1101       N
ATOM      6  CA  ILE A   3      -2.356   0.917  16.359  1.00 40.38           C
ANISOU    6  CA  ILE A   3     4892   4929   5522   -946   -485   -989       C
ATOM      7  C   ILE A   3      -2.683   1.852  15.201  1.00 39.17           C
ANISOU    7  C   ILE A   3     4720   4680   5482   -973   -299   -972       C
ATOM      8  O   ILE A   3      -3.673   2.592  15.237  1.00 43.90           O
ANISOU    8  O   ILE A   3     5441   5209   6032   -972   -200   -985       O
ATOM      9  CB  ILE A   3      -3.314  -0.275  16.434  1.00 40.94           C
ANISOU    9  CB  ILE A   3     5055   5046   5455   -844   -480   -887       C
ATOM     10  CG1 ILE A   3      -3.099  -1.060  17.742  1.00 39.96           C
ANISOU   10  CG1 ILE A   3     4999   4998   5186   -837   -670   -891       C
ATOM     11  CG2 ILE A   3      -3.209  -1.157  15.194  1.00 39.25           C
ANISOU   11  CG2 ILE A   3     4742   4838   5333   -765   -421   -792       C
ATOM     12  CD1 ILE A   3      -3.953  -2.304  17.860  1.00 41.35           C
ANISOU   12  CD1 ILE A   3     5272   5209   5233   -760   -677   -776       C
ATOM     13  H   ILE A   3      -3.024   1.401  18.150  1.00 57.50           H
ATOM     14  N   ALA A   4      -1.844   1.821  14.163  1.00 38.31           N
ANISOU   14  N   ALA A   4     4458   4572   5525   -993   -252   -941       N
ATOM     15  CA  ALA A   4      -1.982   2.663  12.979  1.00 35.46           C
ANISOU   15  CA  ALA A   4     4079   4127   5265  -1035    -84   -902       C
ATOM     16  C   ALA A   4      -2.894   2.000  11.956  1.00 32.35           C
ANISOU   16  C   ALA A   4     3725   3743   4823   -929     32   -788       C
ATOM     17  O   ALA A   4      -3.184   0.803  12.023  1.00 32.55           O
ANISOU   17  O   ALA A   4     3752   3841   4775   -835    -17   -744       O
ATOM     18  CB  ALA A   4      -0.624   2.936  12.332  1.00 36.29           C
ANISOU   18  CB  ALA A   4     3999   4253   5539  -1128    -70   -923       C
ATOM     19  H   ALA A   4      -1.161   1.301  14.122  1.00 45.97           H
ATOM     20  N   VAL A   5      -3.329   2.788  10.981  1.00 31.46           N
ANISOU   20  N   VAL A   5     3649   3549   4755   -950    174   -737       N
ATOM     21  CA  VAL A   5      -4.104   2.265   9.851  1.00 30.34           C
ANISOU   21  CA  VAL A   5     3534   3420   4574   -862    279   -631       C
ATOM     22  C   VAL A   5      -3.253   2.461   8.596  1.00 31.74           C
ANISOU   22  C   VAL A   5     3597   3608   4853   -919    377   -587       C
ATOM     23  O   VAL A   5      -2.858   3.589   8.269  1.00 32.13           O
ANISOU   23  O   VAL A   5     3647   3576   4987  -1027    443   -586       O
ATOM     24  CB  VAL A   5      -5.460   2.970   9.724  1.00 32.06           C
ANISOU   24  CB  VAL A   5     3901   3546   4735   -822    355   -597       C
ATOM     25  CG1 VAL A   5      -6.176   2.567   8.446  1.00 31.06           C
ANISOU   25  CG1 VAL A   5     3792   3432   4578   -746    451   -489       C
ATOM     26  CG2 VAL A   5      -6.311   2.775  10.989  1.00 32.03           C
ANISOU   26  CG2 VAL A   5     3993   3556   4619   -774    284   -656       C
ATOM     27  H   VAL A   5      -3.190   3.636  10.948  1.00 37.75           H
ATOM     28  N   SER A   6      -2.959   1.370   7.896  1.00 32.68           N
ANISOU   28  N   SER A   6     3626   3824   4965   -853    393   -553       N
ATOM     29  CA  SER A   6      -2.048   1.499   6.773  1.00 31.53           C
ANISOU   29  CA  SER A   6     3357   3721   4903   -912    497   -531       C
ATOM     30  C   SER A   6      -2.683   2.293   5.650  1.00 31.31           C
ANISOU   30  C   SER A   6     3426   3623   4848   -941    643   -433       C
ATOM     31  O   SER A   6      -3.910   2.332   5.492  1.00 29.49           O
ANISOU   31  O   SER A   6     3334   3341   4530   -865    657   -375       O
ATOM     32  CB  SER A   6      -1.605   0.135   6.255  1.00 34.31           C
ANISOU   32  CB  SER A   6     3592   4193   5252   -818    487   -540       C
ATOM     33  OG  SER A   6      -2.585  -0.399   5.391  1.00 35.13           O
ANISOU   33  OG  SER A   6     3786   4302   5258   -727    555   -466       O
ATOM     34  H   SER A   6      -3.262   0.580   8.046  1.00 39.21           H
ATOM     35  HG  SER A   6      -2.453  -1.221   5.279  1.00 42.15           H
ATOM     36  N  AASP A   7      -1.817   2.947   4.871  0.50 33.32           N
ANISOU   36  N  AASP A   7     3602   3878   5180  -1060    748   -410       N
ATOM     37  CA AASP A   7      -2.266   3.706   3.711  0.50 34.24           C
ANISOU   37  CA AASP A   7     3817   3931   5263  -1103    884   -296       C
ATOM     38  C  AASP A   7      -3.033   2.832   2.736  0.50 31.04           C
ANISOU   38  C  AASP A   7     3460   3597   4737   -980    934   -227       C
ATOM     39  O  AASP A   7      -3.968   3.301   2.085  0.50 29.64           O
ANISOU   39  O  AASP A   7     3423   3351   4488   -953    983   -131       O
ATOM     40  CB AASP A   7      -1.064   4.311   2.993  0.50 35.17           C
ANISOU   40  CB AASP A   7     3820   4074   5468  -1266   1001   -279       C
ATOM     41  CG AASP A   7      -0.382   5.360   3.808  0.50 39.80           C
ANISOU   41  CG AASP A   7     4376   4564   6183  -1416    960   -336       C
ATOM     42  OD1AASP A   7      -1.065   5.978   4.653  0.50 40.12           O
ANISOU   42  OD1AASP A   7     4549   4472   6225  -1401    875   -357       O
ATOM     43  OD2AASP A   7       0.832   5.584   3.592  0.50 40.99           O
ANISOU   43  OD2AASP A   7     4366   4774   6436  -1554   1016   -369       O
ATOM     44  H  AASP A   7      -0.967   2.965   4.994  0.50 39.99           H
ATOM     45  N  BASP A   7      -1.817   2.947   4.871  0.50 33.32           N
ANISOU   45  N  BASP A   7     3602   3878   5180  -1060    748   -410       N
ATOM     46  CA BASP A   7      -2.266   3.706   3.711  0.50 34.24           C
ANISOU   46  CA BASP A   7     3817   3931   5263  -1103    884   -296       C
ATOM     47  C  BASP A   7      -3.033   2.832   2.736  0.50 31.05           C
ANISOU   47  C  BASP A   7     3461   3598   4738   -980    934   -227       C
ATOM     48  O  BASP A   7      -3.968   3.302   2.085  0.50 29.64           O
ANISOU   48  O  BASP A   7     3423   3351   4489   -953    983   -131       O
ATOM     49  CB BASP A   7      -1.064   4.311   2.993  0.50 35.17           C
ANISOU   49  CB BASP A   7     3820   4074   5468  -1266   1001   -279       C
ATOM     50  CG BASP A   7      -0.381   5.359   3.808  0.50 39.80           C
ANISOU   50  CG BASP A   7     4376   4564   6183  -1416    960   -336       C
ATOM     51  OD1BASP A   7      -1.064   5.980   4.652  0.50 40.12           O
ANISOU   51  OD1BASP A   7     4549   4472   6225  -1402    875   -357       O
ATOM     52  OD2BASP A   7       0.833   5.581   3.594  0.50 40.99           O
ANISOU   52  OD2BASP A   7     4365   4775   6436  -1554   1016   -369       O
ATOM     53  H  BASP A   7      -0.967   2.966   4.994  0.50 39.99           H
ATOM     54  N   ASP A   8      -2.640   1.566   2.612  1.00 30.29           N
ANISOU   54  N   ASP A   8     3251   3633   4624   -901    911   -282       N
ATOM     55  CA  ASP A   8      -3.316   0.679   1.676  1.00 31.28           C
ANISOU   55  CA  ASP A   8     3420   3825   4639   -791    951   -238       C
ATOM     56  C   ASP A   8      -4.766   0.493   2.039  1.00 29.61           C
ANISOU   56  C   ASP A   8     3357   3549   4343   -689    875   -201       C
ATOM     57  O   ASP A   8      -5.600   0.295   1.160  1.00 26.89           O
ANISOU   57  O   ASP A   8     3096   3215   3904   -630    915   -134       O
ATOM     58  CB  ASP A   8      -2.642  -0.682   1.620  1.00 30.77           C
ANISOU   58  CB  ASP A   8     3214   3885   4592   -711    918   -325       C
ATOM     59  CG  ASP A   8      -3.022  -1.440   0.375  1.00 34.50           C
ANISOU   59  CG  ASP A   8     3711   4434   4963   -635    997   -298       C
ATOM     60  OD1 ASP A   8      -3.036  -0.805  -0.716  1.00 31.38           O
ANISOU   60  OD1 ASP A   8     3360   4056   4508   -699   1129   -224       O
ATOM     61  OD2 ASP A   8      -3.357  -2.641   0.489  1.00 33.57           O
ANISOU   61  OD2 ASP A   8     3590   4352   4816   -516    920   -345       O
ATOM     62  H   ASP A   8      -1.995   1.206   3.052  1.00 36.35           H
ATOM     63  N   CYS A   9      -5.094   0.516   3.333  1.00 26.88           N
ANISOU   63  N   CYS A   9     3040   3152   4022   -669    763   -250       N
ATOM     64  CA  CYS A   9      -6.501   0.476   3.706  1.00 27.21           C
ANISOU   64  CA  CYS A   9     3209   3142   3989   -589    715   -220       C
ATOM     65  C   CYS A   9      -7.285   1.589   3.028  1.00 24.39           C
ANISOU   65  C   CYS A   9     2967   2693   3609   -602    784   -133       C
ATOM     66  O   CYS A   9      -8.378   1.358   2.502  1.00 25.07           O
ANISOU   66  O   CYS A   9     3126   2782   3619   -521    787    -79       O
ATOM     67  CB  CYS A   9      -6.667   0.594   5.219  1.00 24.37           C
ANISOU   67  CB  CYS A   9     2871   2743   3646   -593    613   -289       C
ATOM     68  SG  CYS A   9      -6.056  -0.762   6.182  1.00 25.18           S
ANISOU   68  SG  CYS A   9     2887   2932   3747   -555    488   -363       S
ATOM     69  H   CYS A   9      -4.538   0.552   3.988  1.00 32.26           H
ATOM     70  N   VAL A  10      -6.774   2.812   3.104  1.00 26.45           N
ANISOU   70  N   VAL A  10     3247   2860   3944   -703    823   -121       N
ATOM     71  CA  VAL A  10      -7.448   3.952   2.484  1.00 27.37           C
ANISOU   71  CA  VAL A  10     3488   2857   4056   -714    873    -28       C
ATOM     72  C   VAL A  10      -7.469   3.829   0.967  1.00 30.27           C
ANISOU   72  C   VAL A  10     3879   3273   4349   -714    961     82       C
ATOM     73  O   VAL A  10      -8.473   4.150   0.324  1.00 30.30           O
ANISOU   73  O   VAL A  10     3993   3229   4292   -648    962    169       O
ATOM     74  CB  VAL A  10      -6.772   5.254   2.945  1.00 27.39           C
ANISOU   74  CB  VAL A  10     3511   2727   4170   -840    887    -45       C
ATOM     75  CG1 VAL A  10      -7.467   6.457   2.327  1.00 29.23           C
ANISOU   75  CG1 VAL A  10     3892   2801   4413   -843    922     59       C
ATOM     76  CG2 VAL A  10      -6.841   5.294   4.476  1.00 29.81           C
ANISOU   76  CG2 VAL A  10     3806   3003   4517   -828    789   -172       C
ATOM     77  H   VAL A  10      -6.040   3.011   3.507  1.00 31.75           H
ATOM     78  N   GLN A  11      -6.389   3.311   0.381  1.00 28.39           N
ANISOU   78  N   GLN A  11     3535   3144   4108   -777   1030     71       N
ATOM     79  CA  GLN A  11      -6.331   3.170  -1.066  1.00 29.95           C
ANISOU   79  CA  GLN A  11     3759   3412   4210   -788   1129    162       C
ATOM     80  C   GLN A  11      -7.406   2.220  -1.560  1.00 27.43           C
ANISOU   80  C   GLN A  11     3488   3162   3772   -648   1084    176       C
ATOM     81  O   GLN A  11      -8.162   2.546  -2.476  1.00 27.40           O
ANISOU   81  O   GLN A  11     3596   3139   3677   -616   1102    278       O
ATOM     82  CB  GLN A  11      -4.938   2.701  -1.487  1.00 30.59           C
ANISOU   82  CB  GLN A  11     3687   3620   4314   -873   1223    112       C
ATOM     83  CG  GLN A  11      -4.831   2.344  -2.983  1.00 35.77           C
ANISOU   83  CG  GLN A  11     4360   4391   4841   -877   1340    178       C
ATOM     84  CD  GLN A  11      -4.937   3.594  -3.815  1.00 39.96           C
ANISOU   84  CD  GLN A  11     5023   4834   5325   -984   1427    330       C
ATOM     85  OE1 GLN A  11      -4.500   4.657  -3.384  1.00 44.59           O
ANISOU   85  OE1 GLN A  11     5624   5303   6015  -1103   1444    363       O
ATOM     86  NE2 GLN A  11      -5.448   3.468  -5.041  1.00 42.90           N
ANISOU   86  NE2 GLN A  11     5498   5264   5539   -953   1480    427       N
ATOM     87  H   GLN A  11      -5.686   3.039   0.796  1.00 34.07           H
ATOM     88 HE21 GLN A  11      -5.525   4.158  -5.548  1.00 51.49           H
ATOM     89 HE22 GLN A  11      -5.700   2.696  -5.324  1.00 51.49           H
ATOM     90  N   LYS A  12      -7.497   1.037  -0.958  1.00 25.19           N
ANISOU   90  N   LYS A  12     3126   2954   3490   -568   1013     77       N
ATOM     91  CA  LYS A  12      -8.515   0.098  -1.372  1.00 24.39           C
ANISOU   91  CA  LYS A  12     3066   2909   3292   -455    963     81       C
ATOM     92  C   LYS A  12      -9.907   0.664  -1.109  1.00 25.73           C
ANISOU   92  C   LYS A  12     3346   2989   3443   -392    898    136       C
ATOM     93  O   LYS A  12     -10.848   0.414  -1.862  1.00 25.39           O
ANISOU   93  O   LYS A  12     3363   2972   3311   -323    877    186       O
ATOM     94  CB  LYS A  12      -8.334  -1.222  -0.590  1.00 26.70           C
ANISOU   94  CB  LYS A  12     3268   3264   3613   -397    886    -28       C
ATOM     95  CG  LYS A  12      -7.604  -2.210  -1.336  1.00 26.92           C
ANISOU   95  CG  LYS A  12     3217   3399   3611   -378    929    -79       C
ATOM     96  CD  LYS A  12      -6.169  -1.820  -1.423  1.00 31.09           C
ANISOU   96  CD  LYS A  12     3636   3963   4213   -468   1013   -112       C
ATOM     97  CE  LYS A  12      -5.514  -2.735  -2.428  1.00 32.44           C
ANISOU   97  CE  LYS A  12     3727   4259   4338   -438   1087   -170       C
ATOM     98  NZ  LYS A  12      -4.093  -2.342  -2.666  1.00 33.43           N
ANISOU   98  NZ  LYS A  12     3719   4450   4535   -533   1198   -207       N
ATOM     99  H   LYS A  12      -6.988   0.765  -0.320  1.00 30.23           H
ATOM    100  HZ1 LYS A  12      -4.042  -1.470  -2.835  1.00 40.12           H
ATOM    101  HZ2 LYS A  12      -3.602  -2.526  -1.946  1.00 40.12           H
ATOM    102  HZ3 LYS A  12      -3.765  -2.791  -3.361  1.00 40.12           H
ATOM    103  N   PHE A  13     -10.085   1.366   0.017  1.00 25.98           N
ANISOU  103  N   PHE A  13     3391   2923   3559   -407    857    108       N
ATOM    104  CA  PHE A  13     -11.379   1.954   0.288  1.00 25.23           C
ANISOU  104  CA  PHE A  13     3379   2747   3461   -336    806    140       C
ATOM    105  C   PHE A  13     -11.737   2.970  -0.795  1.00 25.12           C
ANISOU  105  C   PHE A  13     3469   2657   3418   -335    840    262       C
ATOM    106  O   PHE A  13     -12.888   3.019  -1.240  1.00 29.38           O
ANISOU  106  O   PHE A  13     4065   3189   3910   -243    794    312       O
ATOM    107  CB  PHE A  13     -11.346   2.661   1.640  1.00 24.05           C
ANISOU  107  CB  PHE A  13     3231   2503   3403   -360    775     71       C
ATOM    108  CG  PHE A  13     -12.551   3.503   1.892  1.00 28.22           C
ANISOU  108  CG  PHE A  13     3838   2933   3952   -285    744     88       C
ATOM    109  CD1 PHE A  13     -13.751   2.886   2.154  1.00 27.62           C
ANISOU  109  CD1 PHE A  13     3747   2915   3833   -187    697     62       C
ATOM    110  CD2 PHE A  13     -12.493   4.904   1.872  1.00 31.06           C
ANISOU  110  CD2 PHE A  13     4278   3137   4386   -312    761    124       C
ATOM    111  CE1 PHE A  13     -14.908   3.639   2.380  1.00 28.97           C
ANISOU  111  CE1 PHE A  13     3962   3012   4035   -100    671     61       C
ATOM    112  CE2 PHE A  13     -13.615   5.651   2.094  1.00 30.88           C
ANISOU  112  CE2 PHE A  13     4319   3017   4398   -217    724    124       C
ATOM    113  CZ  PHE A  13     -14.841   5.012   2.349  1.00 26.80           C
ANISOU  113  CZ  PHE A  13     3764   2580   3838   -103    681     87       C
ATOM    114  H   PHE A  13      -9.484   1.506   0.616  1.00 31.18           H
ATOM    115  N   ASN A  14     -10.772   3.800  -1.200  1.00 26.11           N
ANISOU  115  N   ASN A  14     3621   2724   3577   -442    913    317       N
ATOM    116  CA  ASN A  14     -11.037   4.807  -2.208  1.00 27.65           C
ANISOU  116  CA  ASN A  14     3939   2828   3738   -459    942    456       C
ATOM    117  C   ASN A  14     -11.329   4.143  -3.553  1.00 30.07           C
ANISOU  117  C   ASN A  14     4276   3256   3893   -421    961    532       C
ATOM    118  O   ASN A  14     -12.135   4.655  -4.341  1.00 32.41           O
ANISOU  118  O   ASN A  14     4685   3504   4125   -367    926    644       O
ATOM    119  CB  ASN A  14      -9.849   5.773  -2.318  1.00 32.24           C
ANISOU  119  CB  ASN A  14     4539   3323   4388   -616   1028    502       C
ATOM    120  CG  ASN A  14      -9.834   6.804  -1.169  1.00 34.91           C
ANISOU  120  CG  ASN A  14     4905   3487   4872   -646    987    450       C
ATOM    121  OD1 ASN A  14     -10.849   7.008  -0.501  1.00 38.96           O
ANISOU  121  OD1 ASN A  14     5455   3930   5420   -535    906    406       O
ATOM    122  ND2 ASN A  14      -8.698   7.474  -0.969  1.00 36.18           N
ANISOU  122  ND2 ASN A  14     5045   3582   5119   -800   1046    445       N
ATOM    123  H   ASN A  14      -9.964   3.796  -0.904  1.00 31.34           H
ATOM    124 HD21 ASN A  14      -8.648   8.057  -0.339  1.00 43.42           H
ATOM    125 HD22 ASN A  14      -8.015   7.322  -1.470  1.00 43.42           H
ATOM    126  N   GLU A  15     -10.700   2.996  -3.819  1.00 28.72           N
ANISOU  126  N   GLU A  15     4010   3239   3664   -439   1004    464       N
ATOM    127  CA  GLU A  15     -10.999   2.261  -5.040  1.00 28.80           C
ANISOU  127  CA  GLU A  15     4049   3373   3520   -397   1017    502       C
ATOM    128  C   GLU A  15     -12.442   1.778  -5.012  1.00 28.85           C
ANISOU  128  C   GLU A  15     4084   3390   3486   -264    898    493       C
ATOM    129  O   GLU A  15     -13.123   1.776  -6.041  1.00 30.44           O
ANISOU  129  O   GLU A  15     4367   3628   3569   -216    866    572       O
ATOM    130  CB  GLU A  15     -10.045   1.080  -5.189  1.00 26.29           C
ANISOU  130  CB  GLU A  15     3611   3202   3175   -424   1080    395       C
ATOM    131  CG  GLU A  15      -8.691   1.546  -5.546  1.00 28.82           C
ANISOU  131  CG  GLU A  15     3890   3549   3511   -556   1214    414       C
ATOM    132  CD  GLU A  15      -7.650   0.477  -5.398  1.00 31.97           C
ANISOU  132  CD  GLU A  15     4133   4074   3939   -567   1266    279       C
ATOM    133  OE1 GLU A  15      -7.968  -0.648  -4.943  1.00 31.76           O
ANISOU  133  OE1 GLU A  15     4048   4093   3927   -471   1185    177       O
ATOM    134  OE2 GLU A  15      -6.494   0.765  -5.718  1.00 34.66           O
ANISOU  134  OE2 GLU A  15     4403   4465   4299   -675   1386    275       O
ATOM    135  H   GLU A  15     -10.107   2.630  -3.316  1.00 34.47           H
ATOM    136  N   LEU A  16     -12.922   1.349  -3.847  1.00 23.84           N
ANISOU  136  N   LEU A  16     3380   2738   2941   -210    829    398       N
ATOM    137  CA  LEU A  16     -14.312   0.948  -3.742  1.00 26.39           C
ANISOU  137  CA  LEU A  16     3709   3077   3243   -102    728    385       C
ATOM    138  C   LEU A  16     -15.228   2.170  -3.834  1.00 30.66           C
ANISOU  138  C   LEU A  16     4334   3500   3815    -44    678    475       C
ATOM    139  O   LEU A  16     -16.216   2.169  -4.581  1.00 28.00           O
ANISOU  139  O   LEU A  16     4041   3186   3410     36    607    533       O
ATOM    140  CB  LEU A  16     -14.529   0.199  -2.415  1.00 25.61           C
ANISOU  140  CB  LEU A  16     3516   2993   3221    -83    687    268       C
ATOM    141  CG  LEU A  16     -15.936  -0.189  -1.940  1.00 23.81           C
ANISOU  141  CG  LEU A  16     3261   2783   3003      1    602    235       C
ATOM    142  CD1 LEU A  16     -15.908  -1.449  -1.003  1.00 23.87           C
ANISOU  142  CD1 LEU A  16     3187   2854   3028    -15    578    134       C
ATOM    143  CD2 LEU A  16     -16.637   0.966  -1.225  1.00 25.53           C
ANISOU  143  CD2 LEU A  16     3501   2895   3306     46    582    245       C
ATOM    144  H   LEU A  16     -12.469   1.283  -3.119  1.00 28.61           H
ATOM    145  N   LYS A  17     -14.894   3.237  -3.095  1.00 28.31           N
ANISOU  145  N   LYS A  17     4062   3068   3628    -78    702    480       N
ATOM    146  CA  LYS A  17     -15.808   4.358  -2.942  1.00 29.94           C
ANISOU  146  CA  LYS A  17     4337   3137   3900      1    643    531       C
ATOM    147  C   LYS A  17     -15.834   5.199  -4.194  1.00 33.38           C
ANISOU  147  C   LYS A  17     4907   3504   4273     -1    636    692       C
ATOM    148  O   LYS A  17     -16.898   5.621  -4.649  1.00 36.97           O
ANISOU  148  O   LYS A  17     5417   3913   4716    109    545    759       O
ATOM    149  CB  LYS A  17     -15.379   5.229  -1.755  1.00 29.36           C
ANISOU  149  CB  LYS A  17     4263   2929   3964    -40    669    468       C
ATOM    150  CG  LYS A  17     -16.284   6.420  -1.581  1.00 33.74           C
ANISOU  150  CG  LYS A  17     4892   3322   4606     56    609    501       C
ATOM    151  CD  LYS A  17     -15.829   7.317  -0.436  1.00 35.76           C
ANISOU  151  CD  LYS A  17     5162   3432   4993     12    635    419       C
ATOM    152  CE  LYS A  17     -14.516   7.960  -0.780  1.00 37.45           C
ANISOU  152  CE  LYS A  17     5443   3556   5230   -140    703    488       C
ATOM    153  NZ  LYS A  17     -14.089   9.053   0.166  1.00 41.30           N
ANISOU  153  NZ  LYS A  17     5973   3863   5856   -193    711    422       N
ATOM    154  H   LYS A  17     -14.148   3.330  -2.679  1.00 33.98           H
ATOM    155  HZ1 LYS A  17     -13.391   9.491  -0.171  1.00 49.57           H
ATOM    156  HZ2 LYS A  17     -14.758   9.626   0.290  1.00 49.57           H
ATOM    157  HZ3 LYS A  17     -13.858   8.703   0.951  1.00 49.57           H
ATOM    158  N   LEU A  18     -14.655   5.490  -4.732  1.00 31.64           N
ANISOU  158  N   LEU A  18     4737   3273   4014   -129    730    759       N
ATOM    159  CA  LEU A  18     -14.541   6.305  -5.928  1.00 36.47           C
ANISOU  159  CA  LEU A  18     5496   3820   4543   -165    741    933       C
ATOM    160  C   LEU A  18     -14.676   5.400  -7.156  1.00 41.04           C
ANISOU  160  C   LEU A  18     6090   4576   4929   -152    742    978       C
ATOM    161  O   LEU A  18     -15.558   5.617  -7.986  1.00 46.16           O
ANISOU  161  O   LEU A  18     6831   5220   5487    -68    652   1080       O
ATOM    162  CB  LEU A  18     -13.218   7.074  -5.908  1.00 36.38           C
ANISOU  162  CB  LEU A  18     5525   3720   4579   -334    858    983       C
ATOM    163  CG  LEU A  18     -13.238   8.092  -4.747  1.00 38.29           C
ANISOU  163  CG  LEU A  18     5778   3760   5011   -336    830    935       C
ATOM    164  CD1 LEU A  18     -11.850   8.726  -4.483  1.00 36.79           C
ANISOU  164  CD1 LEU A  18     5588   3491   4899   -525    938    941       C
ATOM    165  CD2 LEU A  18     -14.376   9.140  -4.805  1.00 41.22           C
ANISOU  165  CD2 LEU A  18     6273   3943   5446   -209    716   1016       C
ATOM    166  H   LEU A  18     -13.901   5.222  -4.418  1.00 37.98           H
ATOM    167  N   GLY A  19     -13.852   4.377  -7.288  1.00 37.76           N
ANISOU  167  N   GLY A  19     5585   4314   4448   -222    830    894       N
ATOM    168  CA  GLY A  19     -13.888   3.665  -8.562  1.00 36.68           C
ANISOU  168  CA  GLY A  19     5490   4333   4115   -220    843    934       C
ATOM    169  C   GLY A  19     -14.968   2.589  -8.690  1.00 36.74           C
ANISOU  169  C   GLY A  19     5446   4450   4064    -97    730    854       C
ATOM    170  O   GLY A  19     -15.113   2.038  -9.789  1.00 32.85           O
ANISOU  170  O   GLY A  19     5002   4079   3399    -88    720    880       O
ATOM    171  H   GLY A  19     -13.297   4.090  -6.698  1.00 45.32           H
ATOM    172  N   HIS A  20     -15.713   2.279  -7.612  1.00 34.01           N
ANISOU  172  N   HIS A  20     5005   4069   3847    -17    649    755       N
ATOM    173  CA  HIS A  20     -16.606   1.108  -7.580  1.00 35.90           C
ANISOU  173  CA  HIS A  20     5167   4418   4054     64    560    660       C
ATOM    174  C   HIS A  20     -15.863  -0.161  -7.996  1.00 33.38           C
ANISOU  174  C   HIS A  20     4799   4240   3644     13    622    566       C
ATOM    175  O   HIS A  20     -16.417  -1.038  -8.665  1.00 34.04           O
ANISOU  175  O   HIS A  20     4883   4426   3624     55    560    528       O
ATOM    176  CB  HIS A  20     -17.840   1.318  -8.474  1.00 39.71           C
ANISOU  176  CB  HIS A  20     5721   4921   4446    160    431    743       C
ATOM    177  CG  HIS A  20     -18.375   2.706  -8.436  1.00 40.12           C
ANISOU  177  CG  HIS A  20     5856   4823   4565    218    372    865       C
ATOM    178  ND1 HIS A  20     -19.008   3.227  -7.332  1.00 40.54           N
ANISOU  178  ND1 HIS A  20     5845   4769   4789    287    329    818       N
ATOM    179  CD2 HIS A  20     -18.341   3.701  -9.352  1.00 45.20           C
ANISOU  179  CD2 HIS A  20     6652   5394   5129    217    351   1030       C
ATOM    180  CE1 HIS A  20     -19.348   4.481  -7.567  1.00 43.42           C
ANISOU  180  CE1 HIS A  20     6312   4990   5195    341    277    937       C
ATOM    181  NE2 HIS A  20     -18.955   4.795  -8.788  1.00 44.91           N
ANISOU  181  NE2 HIS A  20     6639   5188   5235    297    282   1078       N
ATOM    182  H   HIS A  20     -15.718   2.737  -6.883  1.00 40.81           H
ATOM    183  HD1 HIS A  20     -19.159   2.801  -6.600  1.00 48.65           H
ATOM    184  HE2 HIS A  20     -19.065   5.558  -9.168  1.00 53.89           H
ATOM    185  N   GLN A  21     -14.588  -0.266  -7.617  1.00 30.42           N
ANISOU  185  N   GLN A  21     4377   3868   3315    -73    739    518       N
ATOM    186  CA  GLN A  21     -13.774  -1.360  -8.137  1.00 28.28           C
ANISOU  186  CA  GLN A  21     4059   3724   2963   -107    808    428       C
ATOM    187  C   GLN A  21     -13.933  -2.668  -7.360  1.00 30.35           C
ANISOU  187  C   GLN A  21     4214   4020   3298    -66    754    282       C
ATOM    188  O   GLN A  21     -13.531  -3.728  -7.866  1.00 27.55           O
ANISOU  188  O   GLN A  21     3831   3759   2879    -62    775    192       O
ATOM    189  CB  GLN A  21     -12.295  -0.980  -8.138  1.00 28.36           C
ANISOU  189  CB  GLN A  21     4037   3739   2998   -212    956    428       C
ATOM    190  CG  GLN A  21     -11.961   0.233  -9.020  1.00 32.54           C
ANISOU  190  CG  GLN A  21     4684   4240   3439   -289   1035    584       C
ATOM    191  CD  GLN A  21     -10.467   0.453  -9.177  1.00 38.38           C
ANISOU  191  CD  GLN A  21     5371   5024   4190   -414   1201    572       C
ATOM    192  OE1 GLN A  21      -9.715  -0.491  -9.396  1.00 41.52           O
ANISOU  192  OE1 GLN A  21     5673   5545   4558   -424   1274    455       O
ATOM    193  NE2 GLN A  21     -10.025   1.696  -8.983  1.00 42.12           N
ANISOU  193  NE2 GLN A  21     5889   5385   4729   -510   1257    679       N
ATOM    194  H   GLN A  21     -14.184   0.268  -7.076  1.00 36.51           H
ATOM    195 HE21 GLN A  21      -9.186   1.871  -9.061  1.00 50.54           H
ATOM    196 HE22 GLN A  21     -10.578   2.323  -8.781  1.00 50.54           H
ATOM    197  N   HIS A  22     -14.445  -2.604  -6.141  1.00 26.16           N
ANISOU  197  N   HIS A  22     3631   3412   2898    -42    692    255       N
ATOM    198  CA  HIS A  22     -14.533  -3.755  -5.232  1.00 26.19           C
ANISOU  198  CA  HIS A  22     3549   3427   2976    -25    643    141       C
ATOM    199  C   HIS A  22     -15.916  -3.739  -4.630  1.00 25.96           C
ANISOU  199  C   HIS A  22     3510   3365   2988     24    544    150       C
ATOM    200  O   HIS A  22     -16.411  -2.662  -4.307  1.00 27.36           O
ANISOU  200  O   HIS A  22     3711   3476   3209     42    534    214       O
ATOM    201  CB  HIS A  22     -13.486  -3.691  -4.100  1.00 25.10           C
ANISOU  201  CB  HIS A  22     3341   3241   2956    -74    691     92       C
ATOM    202  CG  HIS A  22     -12.118  -3.292  -4.573  1.00 26.05           C
ANISOU  202  CG  HIS A  22     3444   3384   3068   -136    804     98       C
ATOM    203  ND1 HIS A  22     -11.437  -3.962  -5.571  1.00 25.55           N
ANISOU  203  ND1 HIS A  22     3367   3418   2921   -140    866     53       N
ATOM    204  CD2 HIS A  22     -11.323  -2.261  -4.205  1.00 25.19           C
ANISOU  204  CD2 HIS A  22     3326   3219   3027   -205    872    137       C
ATOM    205  CE1 HIS A  22     -10.270  -3.376  -5.770  1.00 28.11           C
ANISOU  205  CE1 HIS A  22     3657   3758   3263   -212    978     66       C
ATOM    206  NE2 HIS A  22     -10.182  -2.337  -4.958  1.00 28.42           N
ANISOU  206  NE2 HIS A  22     3700   3700   3397   -260    979    122       N
ATOM    207  H   HIS A  22     -14.762  -1.882  -5.798  1.00 31.40           H
ATOM    208  HD1 HIS A  22     -11.727  -4.652  -5.995  1.00 30.66           H
ATOM    209  HE2 HIS A  22      -9.516  -1.795  -4.911  1.00 34.11           H
ATOM    210  N   ARG A  23     -16.523  -4.919  -4.415  1.00 23.58           N
ANISOU  210  N   ARG A  23     3167   3103   2688     42    473     78       N
ATOM    211  CA  ARG A  23     -17.800  -4.974  -3.706  1.00 21.93           C
ANISOU  211  CA  ARG A  23     2920   2879   2531     68    398     75       C
ATOM    212  C   ARG A  23     -17.589  -4.771  -2.217  1.00 21.12           C
ANISOU  212  C   ARG A  23     2774   2719   2533     38    423     49       C
ATOM    213  O   ARG A  23     -18.457  -4.210  -1.531  1.00 21.14           O
ANISOU  213  O   ARG A  23     2751   2698   2583     59    406     60       O
ATOM    214  CB  ARG A  23     -18.488  -6.320  -3.932  1.00 22.46           C
ANISOU  214  CB  ARG A  23     2960   3003   2572     67    320     10       C
ATOM    215  CG  ARG A  23     -19.869  -6.504  -3.252  1.00 23.91           C
ANISOU  215  CG  ARG A  23     3081   3196   2808     72    252      1       C
ATOM    216  CD  ARG A  23     -20.760  -5.311  -3.576  1.00 25.83           C
ANISOU  216  CD  ARG A  23     3321   3441   3052    136    227     68       C
ATOM    217  NE  ARG A  23     -20.844  -5.162  -5.028  1.00 31.83           N
ANISOU  217  NE  ARG A  23     4145   4246   3703    174    184    110       N
ATOM    218  CZ  ARG A  23     -21.341  -4.093  -5.619  1.00 31.63           C
ANISOU  218  CZ  ARG A  23     4155   4210   3652    239    150    192       C
ATOM    219  NH1 ARG A  23     -21.686  -3.023  -4.914  1.00 27.31           N
ANISOU  219  NH1 ARG A  23     3586   3594   3197    281    165    229       N
ATOM    220  NH2 ARG A  23     -21.451  -4.075  -6.947  1.00 33.52           N
ANISOU  220  NH2 ARG A  23     4466   4503   3766    265     97    236       N
ATOM    221  H   ARG A  23     -16.218  -5.683  -4.666  1.00 28.30           H
ATOM    222  HE  ARG A  23     -20.554  -5.803  -5.521  1.00 38.20           H
ATOM    223 HH11 ARG A  23     -21.586  -3.021  -4.060  1.00 32.78           H
ATOM    224 HH12 ARG A  23     -22.009  -2.332  -5.311  1.00 32.78           H
ATOM    225 HH21 ARG A  23     -21.200  -4.756  -7.408  1.00 40.23           H
ATOM    226 HH22 ARG A  23     -21.774  -3.383  -7.342  1.00 40.23           H
ATOM    227  N   TYR A  24     -16.417  -5.179  -1.741  1.00 21.69           N
ANISOU  227  N   TYR A  24     2833   2773   2634     -4    463      8       N
ATOM    228  CA  TYR A  24     -16.118  -5.105  -0.309  1.00 19.82           C
ANISOU  228  CA  TYR A  24     2566   2492   2474    -38    470    -21       C
ATOM    229  C   TYR A  24     -14.599  -5.200  -0.106  1.00 21.82           C
ANISOU  229  C   TYR A  24     2803   2727   2759    -74    511    -51       C
ATOM    230  O   TYR A  24     -13.852  -5.732  -0.951  1.00 20.09           O
ANISOU  230  O   TYR A  24     2577   2544   2512    -69    532    -73       O
ATOM    231  CB  TYR A  24     -16.847  -6.215   0.477  1.00 19.65           C
ANISOU  231  CB  TYR A  24     2516   2488   2463    -55    408    -60       C
ATOM    232  CG  TYR A  24     -16.406  -7.626   0.197  1.00 19.83           C
ANISOU  232  CG  TYR A  24     2538   2522   2473    -67    365   -104       C
ATOM    233  CD1 TYR A  24     -15.275  -8.187   0.859  1.00 20.97           C
ANISOU  233  CD1 TYR A  24     2674   2633   2660    -87    356   -139       C
ATOM    234  CD2 TYR A  24     -17.113  -8.431  -0.697  1.00 18.57           C
ANISOU  234  CD2 TYR A  24     2386   2398   2270    -53    316   -120       C
ATOM    235  CE1 TYR A  24     -14.847  -9.494   0.531  1.00 21.21           C
ANISOU  235  CE1 TYR A  24     2708   2653   2697    -76    306   -188       C
ATOM    236  CE2 TYR A  24     -16.723  -9.719  -0.961  1.00 19.54           C
ANISOU  236  CE2 TYR A  24     2520   2509   2394    -57    271   -175       C
ATOM    237  CZ  TYR A  24     -15.597 -10.244  -0.354  1.00 21.54           C
ANISOU  237  CZ  TYR A  24     2770   2717   2699    -63    268   -209       C
ATOM    238  OH  TYR A  24     -15.221 -11.534  -0.657  1.00 27.76           O
ANISOU  238  OH  TYR A  24     3572   3474   3503    -47    212   -272       O
ATOM    239  H   TYR A  24     -15.780  -5.501  -2.221  1.00 26.03           H
ATOM    240  HH  TYR A  24     -14.468 -11.700  -0.322  1.00 33.32           H
ATOM    241  N   VAL A  25     -14.144  -4.733   1.062  1.00 21.02           N
ANISOU  241  N   VAL A  25     2686   2583   2717   -107    518    -66       N
ATOM    242  CA  VAL A  25     -12.755  -4.890   1.487  1.00 18.50           C
ANISOU  242  CA  VAL A  25     2329   2254   2447   -142    530   -106       C
ATOM    243  C   VAL A  25     -12.817  -5.251   2.960  1.00 20.32           C
ANISOU  243  C   VAL A  25     2552   2462   2705   -166    470   -137       C
ATOM    244  O   VAL A  25     -13.592  -4.643   3.722  1.00 20.80           O
ANISOU  244  O   VAL A  25     2639   2504   2761   -176    470   -128       O
ATOM    245  CB  VAL A  25     -11.919  -3.601   1.324  1.00 20.14           C
ANISOU  245  CB  VAL A  25     2532   2427   2692   -183    601    -84       C
ATOM    246  CG1 VAL A  25     -10.455  -3.846   1.635  1.00 22.98           C
ANISOU  246  CG1 VAL A  25     2820   2800   3113   -222    610   -137       C
ATOM    247  CG2 VAL A  25     -12.106  -3.003  -0.104  1.00 20.25           C
ANISOU  247  CG2 VAL A  25     2587   2454   2650   -172    666    -19       C
ATOM    248  H   VAL A  25     -14.633  -4.315   1.633  1.00 25.23           H
ATOM    249  N   THR A  26     -12.063  -6.272   3.349  1.00 18.45           N
ANISOU  249  N   THR A  26     2287   2232   2492   -168    414   -175       N
ATOM    250  CA  THR A  26     -11.969  -6.563   4.781  1.00 20.47           C
ANISOU  250  CA  THR A  26     2554   2467   2756   -199    347   -189       C
ATOM    251  C   THR A  26     -10.581  -6.196   5.287  1.00 21.45           C
ANISOU  251  C   THR A  26     2629   2580   2942   -222    331   -226       C
ATOM    252  O   THR A  26      -9.610  -6.095   4.526  1.00 21.88           O
ANISOU  252  O   THR A  26     2619   2649   3044   -212    366   -250       O
ATOM    253  CB  THR A  26     -12.308  -8.029   5.085  1.00 19.96           C
ANISOU  253  CB  THR A  26     2514   2398   2673   -189    262   -186       C
ATOM    254  OG1 THR A  26     -11.266  -8.907   4.615  1.00 22.11           O
ANISOU  254  OG1 THR A  26     2748   2659   2996   -148    219   -223       O
ATOM    255  CG2 THR A  26     -13.712  -8.372   4.494  1.00 19.93           C
ANISOU  255  CG2 THR A  26     2540   2412   2620   -182    278   -158       C
ATOM    256  H   THR A  26     -11.614  -6.789   2.827  1.00 22.15           H
ATOM    257  HG1 THR A  26     -11.399  -9.687   4.897  1.00 26.54           H
ATOM    258  N   PHE A  27     -10.499  -5.950   6.592  1.00 19.42           N
ANISOU  258  N   PHE A  27     2395   2309   2676   -261    280   -238       N
ATOM    259  CA  PHE A  27      -9.276  -5.494   7.202  1.00 20.21           C
ANISOU  259  CA  PHE A  27     2446   2403   2832   -293    246   -281       C
ATOM    260  C   PHE A  27      -9.053  -6.210   8.528  1.00 21.39           C
ANISOU  260  C   PHE A  27     2626   2552   2950   -307    123   -289       C
ATOM    261  O   PHE A  27     -10.011  -6.559   9.213  1.00 20.09           O
ANISOU  261  O   PHE A  27     2541   2390   2702   -322    101   -258       O
ATOM    262  CB  PHE A  27      -9.277  -3.984   7.535  1.00 22.87           C
ANISOU  262  CB  PHE A  27     2797   2712   3182   -347    305   -300       C
ATOM    263  CG  PHE A  27      -9.863  -3.084   6.422  1.00 22.20           C
ANISOU  263  CG  PHE A  27     2729   2602   3103   -337    416   -264       C
ATOM    264  CD1 PHE A  27     -11.249  -2.870   6.320  1.00 20.87           C
ANISOU  264  CD1 PHE A  27     2623   2425   2880   -306    448   -232       C
ATOM    265  CD2 PHE A  27      -9.028  -2.478   5.506  1.00 25.30           C
ANISOU  265  CD2 PHE A  27     3072   2985   3555   -363    481   -257       C
ATOM    266  CE1 PHE A  27     -11.770  -2.032   5.316  1.00 22.45           C
ANISOU  266  CE1 PHE A  27     2846   2595   3088   -283    522   -190       C
ATOM    267  CE2 PHE A  27      -9.536  -1.660   4.499  1.00 23.07           C
ANISOU  267  CE2 PHE A  27     2829   2672   3264   -359    568   -203       C
ATOM    268  CZ  PHE A  27     -10.892  -1.443   4.400  1.00 23.72           C
ANISOU  268  CZ  PHE A  27     2984   2735   3296   -311    576   -167       C
ATOM    269  H   PHE A  27     -11.152  -6.044   7.144  1.00 23.31           H
ATOM    270  N   LYS A  28      -7.779  -6.416   8.860  1.00 20.71           N
ANISOU  270  N   LYS A  28     2471   2470   2928   -304     43   -328       N
ATOM    271  CA  LYS A  28      -7.367  -7.140  10.062  1.00 24.91           C
ANISOU  271  CA  LYS A  28     3032   2999   3433   -307   -104   -326       C
ATOM    272  C   LYS A  28      -6.101  -6.523  10.640  1.00 26.48           C
ANISOU  272  C   LYS A  28     3150   3213   3697   -337   -170   -388       C
ATOM    273  O   LYS A  28      -5.402  -5.748   9.996  1.00 25.19           O
ANISOU  273  O   LYS A  28     2888   3061   3623   -357   -100   -433       O
ATOM    274  CB  LYS A  28      -7.107  -8.609   9.760  1.00 22.86           C
ANISOU  274  CB  LYS A  28     2763   2716   3208   -233   -194   -304       C
ATOM    275  CG  LYS A  28      -5.755  -8.819   9.021  1.00 28.39           C
ANISOU  275  CG  LYS A  28     3316   3429   4042   -172   -212   -369       C
ATOM    276  CD  LYS A  28      -5.283 -10.277   9.030  1.00 31.20           C
ANISOU  276  CD  LYS A  28     3659   3743   4452    -79   -344   -370       C
ATOM    277  CE  LYS A  28      -3.883 -10.410   8.401  1.00 33.43           C
ANISOU  277  CE  LYS A  28     3766   4056   4879     -8   -356   -461       C
ATOM    278  NZ  LYS A  28      -3.386 -11.815   8.319  1.00 35.94           N
ANISOU  278  NZ  LYS A  28     4060   4319   5276    111   -486   -483       N
ATOM    279  H   LYS A  28      -7.114  -6.138   8.390  1.00 24.86           H
ATOM    280  HZ1 LYS A  28      -3.204 -12.122   9.134  1.00 43.13           H
ATOM    281  HZ2 LYS A  28      -4.005 -12.335   7.946  1.00 43.13           H
ATOM    282  HZ3 LYS A  28      -2.646 -11.848   7.826  1.00 43.13           H
ATOM    283  N   MET A  29      -5.805  -6.872  11.896  1.00 24.80           N
ANISOU  283  N   MET A  29     2984   3005   3432   -354   -313   -387       N
ATOM    284  CA  MET A  29      -4.551  -6.450  12.493  1.00 28.01           C
ANISOU  284  CA  MET A  29     3304   3434   3905   -378   -414   -452       C
ATOM    285  C   MET A  29      -3.392  -7.220  11.842  1.00 33.40           C
ANISOU  285  C   MET A  29     3837   4125   4729   -298   -479   -481       C
ATOM    286  O   MET A  29      -3.517  -8.405  11.524  1.00 32.02           O
ANISOU  286  O   MET A  29     3678   3923   4566   -214   -530   -443       O
ATOM    287  CB  MET A  29      -4.611  -6.759  13.985  1.00 31.17           C
ANISOU  287  CB  MET A  29     3812   3845   4186   -407   -568   -432       C
ATOM    288  CG  MET A  29      -5.651  -5.915  14.602  1.00 29.83           C
ANISOU  288  CG  MET A  29     3764   3686   3883   -482   -481   -436       C
ATOM    289  SD  MET A  29      -5.321  -4.173  14.582  1.00 39.27           S
ANISOU  289  SD  MET A  29     4908   4877   5134   -560   -390   -541       S
ATOM    290  CE  MET A  29      -6.890  -3.655  15.331  1.00 32.47           C
ANISOU  290  CE  MET A  29     4216   4023   4097   -600   -294   -537       C
ATOM    291  H   MET A  29      -6.309  -7.345  12.409  1.00 29.76           H
ATOM    292  N   ASN A  30      -2.267  -6.540  11.626  1.00 34.14           N
ANISOU  292  N   ASN A  30     3779   4254   4941   -326   -473   -558       N
ATOM    293  CA  ASN A  30      -1.104  -7.232  11.090  1.00 36.61           C
ANISOU  293  CA  ASN A  30     3919   4595   5398   -245   -532   -608       C
ATOM    294  C   ASN A  30      -0.509  -8.131  12.176  1.00 41.45           C
ANISOU  294  C   ASN A  30     4533   5200   6015   -182   -770   -605       C
ATOM    295  O   ASN A  30      -0.941  -8.118  13.334  1.00 41.05           O
ANISOU  295  O   ASN A  30     4623   5134   5840   -222   -880   -560       O
ATOM    296  CB  ASN A  30      -0.096  -6.227  10.528  1.00 37.27           C
ANISOU  296  CB  ASN A  30     3821   4733   5608   -313   -440   -689       C
ATOM    297  CG  ASN A  30       0.556  -5.327  11.594  1.00 40.88           C
ANISOU  297  CG  ASN A  30     4241   5209   6083   -411   -541   -744       C
ATOM    298  OD1 ASN A  30       0.275  -5.417  12.790  1.00 37.49           O
ANISOU  298  OD1 ASN A  30     3928   4763   5554   -424   -682   -726       O
ATOM    299  ND2 ASN A  30       1.354  -4.371  11.117  1.00 41.29           N
ANISOU  299  ND2 ASN A  30     4144   5295   6249   -500   -451   -808       N
ATOM    300  H   ASN A  30      -2.157  -5.701  11.777  1.00 40.98           H
ATOM    301 HD21 ASN A  30       1.751  -3.833  11.658  1.00 49.55           H
ATOM    302 HD22 ASN A  30       1.472  -4.293  10.269  1.00 49.55           H
ATOM    303  N   ALA A  31       0.470  -8.951  11.777  1.00 43.46           N
ANISOU  303  N   ALA A  31     4636   5468   6410    -75   -852   -653       N
ATOM    304  CA  ALA A  31       1.030  -9.936  12.699  1.00 45.15           C
ANISOU  304  CA  ALA A  31     4856   5655   6645     15  -1101   -637       C
ATOM    305  C   ALA A  31       1.559  -9.287  13.970  1.00 47.69           C
ANISOU  305  C   ALA A  31     5177   6017   6926    -61  -1257   -657       C
ATOM    306  O   ALA A  31       1.447  -9.858  15.062  1.00 47.22           O
ANISOU  306  O   ALA A  31     5245   5927   6770    -39  -1452   -594       O
ATOM    307  CB  ALA A  31       2.130 -10.738  12.005  1.00 46.20           C
ANISOU  307  CB  ALA A  31     4781   5801   6971    156  -1157   -718       C
ATOM    308  H   ALA A  31       0.819  -8.955  10.991  1.00 52.16           H
ATOM    309  N   SER A  32       2.141  -8.099  13.860  1.00 47.26           N
ANISOU  309  N   SER A  32     4992   6028   6936   -160  -1179   -742       N
ATOM    310  CA  SER A  32       2.710  -7.439  15.028  1.00 48.97           C
ANISOU  310  CA  SER A  32     5197   6286   7124   -241  -1334   -786       C
ATOM    311  C   SER A  32       1.689  -6.637  15.834  1.00 47.17           C
ANISOU  311  C   SER A  32     5186   6039   6698   -361  -1290   -748       C
ATOM    312  O   SER A  32       2.046  -6.087  16.875  1.00 48.30           O
ANISOU  312  O   SER A  32     5354   6215   6784   -433  -1420   -792       O
ATOM    313  CB  SER A  32       3.899  -6.567  14.591  1.00 50.23           C
ANISOU  313  CB  SER A  32     5100   6519   7465   -304  -1290   -908       C
ATOM    314  OG  SER A  32       3.583  -5.791  13.443  1.00 52.12           O
ANISOU  314  OG  SER A  32     5298   6757   7747   -377  -1025   -921       O
ATOM    315  H   SER A  32       2.218  -7.659  13.125  1.00 56.71           H
ATOM    316  HG  SER A  32       4.269  -5.390  13.169  1.00 62.54           H
ATOM    317  N   ASN A  33       0.419  -6.612  15.420  1.00 46.83           N
ANISOU  317  N   ASN A  33     5298   5950   6546   -375  -1121   -678       N
ATOM    318  CA  ASN A  33      -0.620  -5.797  16.072  1.00 44.87           C
ANISOU  318  CA  ASN A  33     5232   5690   6126   -476  -1045   -662       C
ATOM    319  C   ASN A  33      -0.220  -4.332  16.192  1.00 42.50           C
ANISOU  319  C   ASN A  33     4869   5406   5872   -593   -982   -765       C
ATOM    320  O   ASN A  33      -0.641  -3.630  17.113  1.00 44.63           O
ANISOU  320  O   ASN A  33     5263   5677   6017   -672  -1002   -798       O
ATOM    321  CB  ASN A  33      -1.024  -6.352  17.435  1.00 47.68           C
ANISOU  321  CB  ASN A  33     5767   6056   6292   -481  -1212   -605       C
ATOM    322  CG  ASN A  33      -1.717  -7.677  17.326  1.00 50.88           C
ANISOU  322  CG  ASN A  33     6283   6418   6630   -399  -1240   -483       C
ATOM    323  OD1 ASN A  33      -2.408  -7.943  16.338  1.00 46.74           O
ANISOU  323  OD1 ASN A  33     5762   5857   6142   -367  -1084   -446       O
ATOM    324  ND2 ASN A  33      -1.559  -8.513  18.332  1.00 53.43           N
ANISOU  324  ND2 ASN A  33     6710   6740   6852   -374  -1444   -416       N
ATOM    325  H   ASN A  33       0.125  -7.066  14.752  1.00 56.20           H
ATOM    326 HD21 ASN A  33      -1.077  -8.287  19.007  1.00 64.12           H
ATOM    327 HD22 ASN A  33      -1.937  -9.285  18.313  1.00 64.12           H
ATOM    328  N   THR A  34       0.574  -3.863  15.243  1.00 41.78           N
ANISOU  328  N   THR A  34     4591   5322   5960   -612   -897   -821       N
ATOM    329  CA  THR A  34       0.945  -2.461  15.162  1.00 42.53           C
ANISOU  329  CA  THR A  34     4627   5407   6127   -740   -815   -906       C
ATOM    330  C   THR A  34       0.154  -1.688  14.117  1.00 38.53           C
ANISOU  330  C   THR A  34     4168   4839   5633   -778   -576   -874       C
ATOM    331  O   THR A  34       0.108  -0.464  14.194  1.00 37.89           O
ANISOU  331  O   THR A  34     4112   4710   5574   -885   -506   -925       O
ATOM    332  CB  THR A  34       2.434  -2.327  14.833  1.00 41.19           C
ANISOU  332  CB  THR A  34     4205   5291   6153   -769   -875   -986       C
ATOM    333  OG1 THR A  34       2.722  -3.068  13.644  1.00 45.68           O
ANISOU  333  OG1 THR A  34     4641   5885   6830   -679   -782   -954       O
ATOM    334  CG2 THR A  34       3.291  -2.850  15.971  1.00 47.32           C
ANISOU  334  CG2 THR A  34     4924   6127   6928   -741  -1142  -1034       C
ATOM    335  H   THR A  34       0.919  -4.347  14.621  1.00 50.14           H
ATOM    336  HG1 THR A  34       3.537  -2.999  13.452  1.00 54.82           H
ATOM    337  N   GLU A  35      -0.460  -2.360  13.139  1.00 36.46           N
ANISOU  337  N   GLU A  35     3924   4568   5361   -693   -463   -793       N
ATOM    338  CA  GLU A  35      -1.129  -1.676  12.035  1.00 33.68           C
ANISOU  338  CA  GLU A  35     3605   4166   5024   -720   -256   -754       C
ATOM    339  C   GLU A  35      -2.336  -2.474  11.563  1.00 29.56           C
ANISOU  339  C   GLU A  35     3200   3631   4399   -625   -190   -665       C
ATOM    340  O   GLU A  35      -2.303  -3.699  11.586  1.00 29.66           O
ANISOU  340  O   GLU A  35     3203   3674   4394   -535   -271   -633       O
ATOM    341  CB  GLU A  35      -0.139  -1.478  10.870  1.00 37.85           C
ANISOU  341  CB  GLU A  35     3947   4726   5707   -750   -157   -773       C
ATOM    342  CG  GLU A  35      -0.596  -0.514   9.809  1.00 36.67           C
ANISOU  342  CG  GLU A  35     3837   4522   5575   -814     40   -729       C
ATOM    343  CD  GLU A  35       0.503  -0.210   8.799  1.00 42.31           C
ANISOU  343  CD  GLU A  35     4367   5283   6426   -881    142   -750       C
ATOM    344  OE1 GLU A  35       1.238  -1.138   8.411  1.00 56.32           O
ANISOU  344  OE1 GLU A  35     5991   7147   8261   -814    119   -776       O
ATOM    345  OE2 GLU A  35       0.629   0.964   8.410  1.00 43.85           O
ANISOU  345  OE2 GLU A  35     4569   5421   6670  -1004    249   -741       O
ATOM    346  H   GLU A  35      -0.503  -3.218  13.095  1.00 43.76           H
ATOM    347  N  AVAL A  36      -3.390  -1.782  11.144  0.07 28.74           N
ANISOU  347  N  AVAL A  36     3204   3474   4241   -643    -57   -627       N
ATOM    348  CA AVAL A  36      -4.503  -2.431  10.463  0.07 27.87           C
ANISOU  348  CA AVAL A  36     3172   3360   4059   -564     19   -549       C
ATOM    349  C  AVAL A  36      -4.177  -2.470   8.980  0.07 27.45           C
ANISOU  349  C  AVAL A  36     3029   3317   4084   -546    136   -521       C
ATOM    350  O  AVAL A  36      -3.743  -1.469   8.402  0.07 28.09           O
ANISOU  350  O  AVAL A  36     3064   3376   4235   -618    229   -530       O
ATOM    351  CB AVAL A  36      -5.831  -1.703  10.720  0.07 27.18           C
ANISOU  351  CB AVAL A  36     3225   3223   3880   -577     93   -529       C
ATOM    352  CG1AVAL A  36      -5.738  -0.257  10.299  0.07 27.57           C
ANISOU  352  CG1AVAL A  36     3276   3203   3998   -645    191   -552       C
ATOM    353  CG2AVAL A  36      -6.967  -2.402   9.983  0.07 25.92           C
ANISOU  353  CG2AVAL A  36     3120   3071   3658   -502    158   -453       C
ATOM    354  H  AVAL A  36      -3.484  -0.933  11.243  0.07 34.49           H
ATOM    355  N  BVAL A  36      -3.401  -1.776  11.163  0.93 28.04           N
ANISOU  355  N  BVAL A  36     3117   3385   4150   -643    -58   -627       N
ATOM    356  CA BVAL A  36      -4.515  -2.398  10.447  0.93 27.95           C
ANISOU  356  CA BVAL A  36     3183   3368   4070   -566     22   -548       C
ATOM    357  C  BVAL A  36      -4.122  -2.480   8.984  0.93 27.68           C
ANISOU  357  C  BVAL A  36     3052   3348   4116   -547    134   -523       C
ATOM    358  O  BVAL A  36      -3.588  -1.513   8.432  0.93 27.48           O
ANISOU  358  O  BVAL A  36     2969   3304   4167   -620    220   -537       O
ATOM    359  CB BVAL A  36      -5.807  -1.586  10.606  0.93 27.05           C
ANISOU  359  CB BVAL A  36     3204   3202   3874   -581    106   -529       C
ATOM    360  CG1BVAL A  36      -7.003  -2.337   9.963  0.93 26.06           C
ANISOU  360  CG1BVAL A  36     3140   3085   3675   -503    164   -453       C
ATOM    361  CG2BVAL A  36      -6.069  -1.211  12.102  0.93 27.89           C
ANISOU  361  CG2BVAL A  36     3400   3304   3894   -622     23   -586       C
ATOM    362  H  BVAL A  36      -3.503  -0.932  11.296  0.93 33.65           H
ATOM    363  N   VAL A  37      -4.391  -3.628   8.367  1.00 24.99           N
ANISOU  363  N   VAL A  37     2704   3038   3753   -458    134   -487       N
ATOM    364  CA  VAL A  37      -4.009  -3.878   6.980  1.00 25.21           C
ANISOU  364  CA  VAL A  37     2645   3100   3832   -429    237   -479       C
ATOM    365  C   VAL A  37      -5.175  -4.502   6.219  1.00 25.39           C
ANISOU  365  C   VAL A  37     2763   3117   3769   -360    289   -419       C
ATOM    366  O   VAL A  37      -6.148  -4.989   6.792  1.00 21.30           O
ANISOU  366  O   VAL A  37     2346   2574   3173   -329    232   -387       O
ATOM    367  CB  VAL A  37      -2.763  -4.782   6.875  1.00 26.77           C
ANISOU  367  CB  VAL A  37     2689   3357   4126   -379    168   -541       C
ATOM    368  CG1 VAL A  37      -1.555  -4.142   7.570  1.00 30.03           C
ANISOU  368  CG1 VAL A  37     2978   3793   4640   -454    107   -609       C
ATOM    369  CG2 VAL A  37      -3.071  -6.149   7.494  1.00 27.18           C
ANISOU  369  CG2 VAL A  37     2792   3395   4141   -280     23   -532       C
ATOM    370  H   VAL A  37      -4.800  -4.288   8.734  1.00 29.99           H
ATOM    371  N   VAL A  38      -5.054  -4.478   4.886  1.00 24.09           N
ANISOU  371  N   VAL A  38     2558   2984   3613   -347    403   -406       N
ATOM    372  CA  VAL A  38      -6.055  -5.095   4.018  1.00 22.70           C
ANISOU  372  CA  VAL A  38     2457   2813   3356   -284    444   -364       C
ATOM    373  C   VAL A  38      -5.944  -6.607   4.104  1.00 22.37           C
ANISOU  373  C   VAL A  38     2394   2784   3322   -196    349   -399       C
ATOM    374  O   VAL A  38      -4.849  -7.166   3.991  1.00 22.66           O
ANISOU  374  O   VAL A  38     2317   2854   3438   -159    321   -465       O
ATOM    375  CB  VAL A  38      -5.897  -4.620   2.573  1.00 25.17           C
ANISOU  375  CB  VAL A  38     2748   3165   3651   -301    585   -342       C
ATOM    376  CG1 VAL A  38      -6.835  -5.418   1.675  1.00 22.65           C
ANISOU  376  CG1 VAL A  38     2499   2866   3243   -229    599   -318       C
ATOM    377  CG2 VAL A  38      -6.186  -3.111   2.443  1.00 25.22           C
ANISOU  377  CG2 VAL A  38     2813   3123   3647   -387    666   -280       C
ATOM    378  H   VAL A  38      -4.401  -4.110   4.463  1.00 28.92           H
ATOM    379  N   GLU A  39      -7.092  -7.281   4.342  1.00 22.36           N
ANISOU  379  N   GLU A  39     2498   2749   3248   -162    296   -360       N
ATOM    380  CA  GLU A  39      -7.141  -8.738   4.392  1.00 22.23           C
ANISOU  380  CA  GLU A  39     2493   2712   3240    -89    200   -381       C
ATOM    381  C   GLU A  39      -7.682  -9.295   3.073  1.00 21.37           C
ANISOU  381  C   GLU A  39     2407   2623   3091    -43    263   -389       C
ATOM    382  O   GLU A  39      -6.944  -9.943   2.333  1.00 24.46           O
ANISOU  382  O   GLU A  39     2730   3039   3526     18    276   -458       O
ATOM    383  CB  GLU A  39      -7.993  -9.213   5.594  1.00 20.37           C
ANISOU  383  CB  GLU A  39     2361   2426   2952   -108     94   -329       C
ATOM    384  CG  GLU A  39      -8.198 -10.767   5.584  1.00 23.67           C
ANISOU  384  CG  GLU A  39     2822   2793   3379    -48     -9   -330       C
ATOM    385  CD  GLU A  39      -9.346 -11.203   6.509  1.00 20.28           C
ANISOU  385  CD  GLU A  39     2513   2323   2870    -98    -71   -255       C
ATOM    386  OE1 GLU A  39     -10.401 -10.545   6.546  1.00 21.59           O
ANISOU  386  OE1 GLU A  39     2723   2517   2965   -152      3   -218       O
ATOM    387  OE2 GLU A  39      -9.169 -12.237   7.192  1.00 25.43           O
ANISOU  387  OE2 GLU A  39     3212   2914   3536    -82   -197   -234       O
ATOM    388  H   GLU A  39      -7.854  -6.904   4.477  1.00 26.83           H
ATOM    389  N   HIS A  40      -8.947  -9.043   2.761  1.00 21.32           N
ANISOU  389  N   HIS A  40     2488   2612   3001    -65    299   -334       N
ATOM    390  CA  HIS A  40      -9.528  -9.541   1.503  1.00 22.65           C
ANISOU  390  CA  HIS A  40     2685   2805   3115    -28    340   -345       C
ATOM    391  C   HIS A  40     -10.047  -8.377   0.680  1.00 22.69           C
ANISOU  391  C   HIS A  40     2715   2852   3053    -60    447   -296       C
ATOM    392  O   HIS A  40     -10.526  -7.388   1.227  1.00 21.30           O
ANISOU  392  O   HIS A  40     2568   2657   2868   -104    464   -241       O
ATOM    393  CB  HIS A  40     -10.688 -10.496   1.764  1.00 24.09           C
ANISOU  393  CB  HIS A  40     2948   2944   3262    -22    257   -323       C
ATOM    394  CG  HIS A  40     -10.294 -11.737   2.514  1.00 23.40           C
ANISOU  394  CG  HIS A  40     2869   2788   3234      7    137   -350       C
ATOM    395  ND1 HIS A  40      -9.253 -12.558   2.127  1.00 27.09           N
ANISOU  395  ND1 HIS A  40     3282   3237   3773     82    102   -431       N
ATOM    396  CD2 HIS A  40     -10.798 -12.276   3.656  1.00 22.03           C
ANISOU  396  CD2 HIS A  40     2758   2554   3057    -29     42   -300       C
ATOM    397  CE1 HIS A  40      -9.136 -13.552   2.997  1.00 27.70           C
ANISOU  397  CE1 HIS A  40     3397   3228   3901    101    -28   -424       C
ATOM    398  NE2 HIS A  40     -10.066 -13.403   3.925  1.00 24.45           N
ANISOU  398  NE2 HIS A  40     3064   2791   3433     24    -64   -336       N
ATOM    399  H   HIS A  40      -9.489  -8.591   3.252  1.00 25.59           H
ATOM    400  HD1 HIS A  40      -8.759 -12.443   1.433  1.00 32.51           H
ATOM    401  HE2 HIS A  40     -10.192 -13.931   4.592  1.00 29.34           H
ATOM    402  N   VAL A  41      -9.977  -8.527  -0.643  1.00 22.63           N
ANISOU  402  N   VAL A  41     2707   2898   2993    -33    511   -318       N
ATOM    403  CA  VAL A  41     -10.571  -7.581  -1.592  1.00 23.26           C
ANISOU  403  CA  VAL A  41     2837   3015   2986    -54    590   -255       C
ATOM    404  C   VAL A  41     -11.530  -8.375  -2.456  1.00 22.53           C
ANISOU  404  C   VAL A  41     2802   2949   2810    -13    553   -269       C
ATOM    405  O   VAL A  41     -11.107  -9.328  -3.123  1.00 23.07           O
ANISOU  405  O   VAL A  41     2855   3049   2862     28    552   -349       O
ATOM    406  CB  VAL A  41      -9.502  -6.886  -2.455  1.00 28.41           C
ANISOU  406  CB  VAL A  41     3445   3726   3622    -82    713   -259       C
ATOM    407  CG1 VAL A  41     -10.151  -5.941  -3.431  1.00 26.43           C
ANISOU  407  CG1 VAL A  41     3276   3500   3267   -107    776   -169       C
ATOM    408  CG2 VAL A  41      -8.491  -6.154  -1.560  1.00 28.80           C
ANISOU  408  CG2 VAL A  41     3420   3748   3774   -138    737   -260       C
ATOM    409  H   VAL A  41      -9.579  -9.186  -1.026  1.00 27.16           H
ATOM    410  N   GLY A  42     -12.809  -8.006  -2.454  1.00 21.70           N
ANISOU  410  N   GLY A  42     2753   2833   2659    -19    517   -205       N
ATOM    411  CA  GLY A  42     -13.813  -8.705  -3.259  1.00 23.14           C
ANISOU  411  CA  GLY A  42     2979   3046   2766      8    464   -220       C
ATOM    412  C   GLY A  42     -14.117  -7.904  -4.514  1.00 24.59           C
ANISOU  412  C   GLY A  42     3213   3292   2839     16    514   -167       C
ATOM    413  O   GLY A  42     -14.406  -6.709  -4.425  1.00 26.06           O
ANISOU  413  O   GLY A  42     3421   3460   3020      2    543    -79       O
ATOM    414  H   GLY A  42     -13.122  -7.351  -1.993  1.00 26.04           H
ATOM    415  N   GLY A  43     -14.141  -8.592  -5.678  1.00 25.26           N
ANISOU  415  N   GLY A  43     3329   3441   2828     43    511   -221       N
ATOM    416  CA  GLY A  43     -14.431  -7.920  -6.938  1.00 29.46           C
ANISOU  416  CA  GLY A  43     3928   4045   3221     48    546   -164       C
ATOM    417  C   GLY A  43     -15.828  -7.314  -6.997  1.00 30.28           C
ANISOU  417  C   GLY A  43     4071   4138   3295     61    464    -76       C
ATOM    418  O   GLY A  43     -16.684  -7.595  -6.156  1.00 25.17           O
ANISOU  418  O   GLY A  43     3387   3448   2728     64    386    -82       O
ATOM    419  H   GLY A  43     -13.994  -9.437  -5.750  1.00 30.32           H
ATOM    420  N  APRO A  44     -16.093  -6.475  -8.006  0.50 26.62           N
ANISOU  420  N  APRO A  44     3681   3719   2714     70    478      9       N
ATOM    421  CA APRO A  44     -17.410  -5.817  -8.059  0.50 28.68           C
ANISOU  421  CA APRO A  44     3966   3964   2966    105    383     93       C
ATOM    422  C  APRO A  44     -18.586  -6.776  -8.045  0.50 29.65           C
ANISOU  422  C  APRO A  44     4053   4118   3095    129    257     28       C
ATOM    423  O  APRO A  44     -19.666  -6.417  -7.546  0.50 28.87           O
ANISOU  423  O  APRO A  44     3912   3996   3062    153    183     65       O
ATOM    424  CB APRO A  44     -17.352  -5.014  -9.376  0.50 30.18           C
ANISOU  424  CB APRO A  44     4264   4207   2997    113    403    190       C
ATOM    425  CG APRO A  44     -15.904  -4.879  -9.674  0.50 31.17           C
ANISOU  425  CG APRO A  44     4407   4354   3082     58    550    182       C
ATOM    426  CD APRO A  44     -15.252  -6.124  -9.162  0.50 31.46           C
ANISOU  426  CD APRO A  44     4359   4405   3190     50    576     34       C
ATOM    427  N  BPRO A  44     -16.093  -6.475  -8.006  0.50 26.62           N
ANISOU  427  N  BPRO A  44     3681   3719   2714     70    478      9       N
ATOM    428  CA BPRO A  44     -17.410  -5.817  -8.059  0.50 28.67           C
ANISOU  428  CA BPRO A  44     3966   3964   2965    105    383     93       C
ATOM    429  C  BPRO A  44     -18.586  -6.776  -8.045  0.50 29.65           C
ANISOU  429  C  BPRO A  44     4052   4117   3095    129    257     28       C
ATOM    430  O  BPRO A  44     -19.667  -6.417  -7.546  0.50 28.87           O
ANISOU  430  O  BPRO A  44     3912   3996   3062    153    183     65       O
ATOM    431  CB BPRO A  44     -17.352  -5.013  -9.375  0.50 30.18           C
ANISOU  431  CB BPRO A  44     4264   4207   2997    113    403    190       C
ATOM    432  CG BPRO A  44     -15.905  -4.879  -9.674  0.50 31.17           C
ANISOU  432  CG BPRO A  44     4407   4354   3082     58    550    182       C
ATOM    433  CD BPRO A  44     -15.253  -6.124  -9.162  0.50 31.46           C
ANISOU  433  CD BPRO A  44     4359   4405   3190     50    576     34       C
ATOM    434  N   ASN A  45     -18.429  -7.991  -8.563  1.00 23.90           N
ANISOU  434  N   ASN A  45     3331   3439   2312    120    231    -77       N
ATOM    435  CA  ASN A  45     -19.539  -8.914  -8.620  1.00 25.18           C
ANISOU  435  CA  ASN A  45     3463   3622   2483    120    106   -140       C
ATOM    436  C   ASN A  45     -19.472  -9.983  -7.550  1.00 26.72           C
ANISOU  436  C   ASN A  45     3594   3751   2809     81     91   -222       C
ATOM    437  O   ASN A  45     -20.262 -10.933  -7.586  1.00 27.29           O
ANISOU  437  O   ASN A  45     3645   3827   2898     57     -4   -286       O
ATOM    438  CB  ASN A  45     -19.610  -9.555 -10.016  1.00 33.10           C
ANISOU  438  CB  ASN A  45     4537   4714   3325    132     58   -207       C
ATOM    439  CG  ASN A  45     -20.134  -8.587 -11.015  1.00 35.15           C
ANISOU  439  CG  ASN A  45     4866   5044   3447    167     17   -106       C
ATOM    440  OD1 ASN A  45     -21.300  -8.196 -10.952  1.00 40.95           O
ANISOU  440  OD1 ASN A  45     5568   5784   4207    194    -92    -51       O
ATOM    441  ND2 ASN A  45     -19.294  -8.201 -11.955  1.00 39.31           N
ANISOU  441  ND2 ASN A  45     5486   5627   3823    168    101    -78       N
ATOM    442  H   ASN A  45     -17.692  -8.296  -8.885  1.00 28.69           H
ATOM    443 HD21 ASN A  45     -18.491  -8.508 -11.966  1.00 47.17           H
ATOM    444 HD22 ASN A  45     -19.549  -7.641 -12.556  1.00 47.17           H
ATOM    445  N   ALA A  46     -18.557  -9.842  -6.587  1.00 23.68           N
ANISOU  445  N   ALA A  46     3182   3300   2514     65    173   -216       N
ATOM    446  CA  ALA A  46     -18.536 -10.725  -5.425  1.00 25.03           C
ANISOU  446  CA  ALA A  46     3308   3398   2802     27    146   -262       C
ATOM    447  C   ALA A  46     -19.845 -10.556  -4.648  1.00 24.92           C
ANISOU  447  C   ALA A  46     3241   3380   2849     -4     88   -218       C
ATOM    448  O   ALA A  46     -20.475  -9.504  -4.687  1.00 25.26           O
ANISOU  448  O   ALA A  46     3262   3453   2882     23     93   -150       O
ATOM    449  CB  ALA A  46     -17.339 -10.400  -4.529  1.00 24.20           C
ANISOU  449  CB  ALA A  46     3186   3239   2771     22    229   -249       C
ATOM    450  H   ALA A  46     -17.939  -9.244  -6.586  1.00 28.42           H
ATOM    451  N   THR A  47     -20.259 -11.603  -3.918  1.00 22.04           N
ANISOU  451  N   THR A  47     2850   2973   2553    -62     36   -257       N
ATOM    452  CA  THR A  47     -21.570 -11.657  -3.293  1.00 20.43           C
ANISOU  452  CA  THR A  47     2580   2787   2397   -112    -10   -234       C
ATOM    453  C   THR A  47     -21.464 -11.394  -1.786  1.00 21.11           C
ANISOU  453  C   THR A  47     2634   2831   2557   -154     46   -193       C
ATOM    454  O   THR A  47     -20.380 -11.441  -1.220  1.00 19.51           O
ANISOU  454  O   THR A  47     2468   2570   2373   -152     89   -191       O
ATOM    455  CB  THR A  47     -22.225 -13.027  -3.468  1.00 20.32           C
ANISOU  455  CB  THR A  47     2562   2757   2403   -182   -103   -297       C
ATOM    456  OG1 THR A  47     -21.477 -13.976  -2.683  1.00 22.03           O
ANISOU  456  OG1 THR A  47     2822   2873   2677   -228    -99   -319       O
ATOM    457  CG2 THR A  47     -22.337 -13.460  -4.952  1.00 24.21           C
ANISOU  457  CG2 THR A  47     3096   3291   2809   -150   -174   -365       C
ATOM    458  H   THR A  47     -19.783 -12.304  -3.774  1.00 26.46           H
ATOM    459  HG1 THR A  47     -20.682 -14.011  -2.955  1.00 26.44           H
ATOM    460  N   TYR A  48     -22.607 -11.097  -1.151  1.00 23.39           N
ANISOU  460  N   TYR A  48     2846   3160   2879   -189     45   -168       N
ATOM    461  CA  TYR A  48     -22.607 -10.939   0.308  1.00 22.57           C
ANISOU  461  CA  TYR A  48     2721   3036   2820   -242    104   -141       C
ATOM    462  C   TYR A  48     -22.082 -12.203   0.979  1.00 20.45           C
ANISOU  462  C   TYR A  48     2508   2692   2571   -325     77   -150       C
ATOM    463  O   TYR A  48     -21.305 -12.139   1.931  1.00 21.95           O
ANISOU  463  O   TYR A  48     2736   2835   2769   -339    111   -127       O
ATOM    464  CB  TYR A  48     -24.010 -10.598   0.835  1.00 22.15           C
ANISOU  464  CB  TYR A  48     2561   3060   2797   -275    118   -135       C
ATOM    465  CG  TYR A  48     -23.880 -10.204   2.289  1.00 23.63           C
ANISOU  465  CG  TYR A  48     2740   3240   2997   -314    202   -116       C
ATOM    466  CD1 TYR A  48     -23.508  -8.910   2.634  1.00 22.66           C
ANISOU  466  CD1 TYR A  48     2620   3114   2877   -239    267   -109       C
ATOM    467  CD2 TYR A  48     -24.069 -11.133   3.304  1.00 23.86           C
ANISOU  467  CD2 TYR A  48     2778   3259   3027   -434    211   -105       C
ATOM    468  CE1 TYR A  48     -23.321  -8.552   3.951  1.00 24.12           C
ANISOU  468  CE1 TYR A  48     2811   3295   3058   -274    338   -110       C
ATOM    469  CE2 TYR A  48     -23.896 -10.766   4.647  1.00 23.12           C
ANISOU  469  CE2 TYR A  48     2697   3172   2914   -474    286    -88       C
ATOM    470  CZ  TYR A  48     -23.518  -9.478   4.939  1.00 23.70           C
ANISOU  470  CZ  TYR A  48     2768   3253   2984   -389    348   -101       C
ATOM    471  OH  TYR A  48     -23.306  -9.083   6.228  1.00 25.74           O
ANISOU  471  OH  TYR A  48     3048   3522   3210   -425    415   -103       O
ATOM    472  H   TYR A  48     -23.370 -10.985  -1.530  1.00 28.07           H
ATOM    473  HH  TYR A  48     -23.286  -9.754   6.734  1.00 30.89           H
ATOM    474  N   GLU A  49     -22.392 -13.362   0.406  1.00 19.95           N
ANISOU  474  N   GLU A  49     2463   2602   2515   -371     -2   -185       N
ATOM    475  CA  GLU A  49     -21.934 -14.610   1.003  1.00 23.40           C
ANISOU  475  CA  GLU A  49     2969   2937   2984   -444    -47   -186       C
ATOM    476  C   GLU A  49     -20.431 -14.816   0.837  1.00 21.85           C
ANISOU  476  C   GLU A  49     2847   2662   2792   -369    -54   -211       C
ATOM    477  O   GLU A  49     -19.789 -15.367   1.742  1.00 23.54           O
ANISOU  477  O   GLU A  49     3113   2793   3037   -398    -74   -185       O
ATOM    478  CB  GLU A  49     -22.740 -15.759   0.420  1.00 24.05           C
ANISOU  478  CB  GLU A  49     3053   2995   3089   -520   -135   -226       C
ATOM    479  CG  GLU A  49     -22.363 -17.086   0.976  1.00 30.74           C
ANISOU  479  CG  GLU A  49     3989   3709   3983   -598   -197   -220       C
ATOM    480  CD  GLU A  49     -22.743 -17.306   2.427  1.00 31.73           C
ANISOU  480  CD  GLU A  49     4121   3814   4120   -720   -167   -132       C
ATOM    481  OE1 GLU A  49     -23.525 -16.519   3.052  1.00 33.96           O
ANISOU  481  OE1 GLU A  49     4319   4206   4377   -762    -87    -93       O
ATOM    482  OE2 GLU A  49     -22.229 -18.312   2.971  1.00 33.00           O
ANISOU  482  OE2 GLU A  49     4381   3845   4313   -771   -227   -104       O
ATOM    483  H   GLU A  49     -22.856 -13.452  -0.312  1.00 23.95           H
ATOM    484  N   ASP A  50     -19.845 -14.376  -0.280  1.00 21.40           N
ANISOU  484  N   ASP A  50     2794   2636   2703   -274    -37   -257       N
ATOM    485  CA  ASP A  50     -18.385 -14.431  -0.446  1.00 20.58           C
ANISOU  485  CA  ASP A  50     2726   2485   2610   -200    -19   -291       C
ATOM    486  C   ASP A  50     -17.674 -13.723   0.702  1.00 21.38           C
ANISOU  486  C   ASP A  50     2816   2573   2734   -199     32   -238       C
ATOM    487  O   ASP A  50     -16.609 -14.161   1.164  1.00 21.98           O
ANISOU  487  O   ASP A  50     2915   2583   2852   -177      8   -252       O
ATOM    488  CB  ASP A  50     -17.974 -13.745  -1.746  1.00 21.83           C
ANISOU  488  CB  ASP A  50     2875   2715   2704   -120     30   -330       C
ATOM    489  CG  ASP A  50     -18.281 -14.586  -2.992  1.00 26.86           C
ANISOU  489  CG  ASP A  50     3544   3362   3299   -103    -28   -414       C
ATOM    490  OD1 ASP A  50     -18.504 -15.832  -2.879  1.00 25.86           O
ANISOU  490  OD1 ASP A  50     3452   3155   3219   -141   -111   -464       O
ATOM    491  OD2 ASP A  50     -18.360 -13.964  -4.110  1.00 23.23           O
ANISOU  491  OD2 ASP A  50     3087   2990   2751    -58      3   -427       O
ATOM    492  H   ASP A  50     -20.264 -14.043  -0.954  1.00 25.69           H
ATOM    493  N   PHE A  51     -18.248 -12.604   1.151  1.00 20.30           N
ANISOU  493  N   PHE A  51     2640   2499   2574   -215     92   -186       N
ATOM    494  CA  PHE A  51     -17.733 -11.840   2.280  1.00 18.83           C
ANISOU  494  CA  PHE A  51     2449   2307   2399   -225    137   -149       C
ATOM    495  C   PHE A  51     -17.985 -12.571   3.604  1.00 20.38           C
ANISOU  495  C   PHE A  51     2678   2462   2605   -308     97   -113       C
ATOM    496  O   PHE A  51     -17.045 -12.871   4.356  1.00 21.99           O
ANISOU  496  O   PHE A  51     2919   2611   2827   -310     64   -104       O
ATOM    497  CB  PHE A  51     -18.407 -10.452   2.286  1.00 18.29           C
ANISOU  497  CB  PHE A  51     2337   2306   2308   -209    209   -123       C
ATOM    498  CG  PHE A  51     -18.412  -9.768   3.643  1.00 20.19           C
ANISOU  498  CG  PHE A  51     2573   2548   2551   -243    251   -100       C
ATOM    499  CD1 PHE A  51     -17.221  -9.386   4.235  1.00 18.88           C
ANISOU  499  CD1 PHE A  51     2429   2346   2400   -234    262   -105       C
ATOM    500  CD2 PHE A  51     -19.616  -9.499   4.293  1.00 20.18           C
ANISOU  500  CD2 PHE A  51     2536   2597   2535   -284    280    -87       C
ATOM    501  CE1 PHE A  51     -17.206  -8.771   5.513  1.00 22.06           C
ANISOU  501  CE1 PHE A  51     2840   2755   2788   -270    290    -98       C
ATOM    502  CE2 PHE A  51     -19.620  -8.872   5.563  1.00 23.95           C
ANISOU  502  CE2 PHE A  51     3017   3088   2996   -315    329    -86       C
ATOM    503  CZ  PHE A  51     -18.418  -8.505   6.159  1.00 21.57           C
ANISOU  503  CZ  PHE A  51     2759   2743   2695   -308    329    -92       C
ATOM    504  H   PHE A  51     -18.956 -12.258   0.807  1.00 24.37           H
ATOM    505  N   LYS A  52     -19.254 -12.850   3.906  1.00 18.61           N
ANISOU  505  N   LYS A  52     2436   2270   2364   -383     97    -88       N
ATOM    506  CA  LYS A  52     -19.644 -13.351   5.228  1.00 19.29           C
ANISOU  506  CA  LYS A  52     2556   2343   2432   -486     88    -37       C
ATOM    507  C   LYS A  52     -19.046 -14.707   5.495  1.00 21.97           C
ANISOU  507  C   LYS A  52     2982   2569   2798   -522    -10    -17       C
ATOM    508  O   LYS A  52     -18.650 -15.014   6.642  1.00 23.62           O
ANISOU  508  O   LYS A  52     3254   2736   2984   -572    -39     37       O
ATOM    509  CB  LYS A  52     -21.176 -13.458   5.281  1.00 24.84           C
ANISOU  509  CB  LYS A  52     3199   3119   3122   -569    119    -25       C
ATOM    510  CG  LYS A  52     -21.788 -13.936   6.619  1.00 24.43           C
ANISOU  510  CG  LYS A  52     3170   3082   3029   -705    142     33       C
ATOM    511  CD  LYS A  52     -23.289 -14.158   6.454  1.00 28.18           C
ANISOU  511  CD  LYS A  52     3555   3640   3514   -793    175     30       C
ATOM    512  CE  LYS A  52     -23.647 -15.656   6.445  1.00 40.35           C
ANISOU  512  CE  LYS A  52     5151   5102   5080   -922     98     67       C
ATOM    513  NZ  LYS A  52     -23.194 -16.271   7.725  1.00 55.46           N
ANISOU  513  NZ  LYS A  52     7179   6950   6943  -1019     86    151       N
ATOM    514  H   LYS A  52     -19.914 -12.757   3.363  1.00 22.33           H
ATOM    515  HZ1 LYS A  52     -23.273 -17.156   7.682  1.00 66.55           H
ATOM    516  HZ2 LYS A  52     -22.342 -16.064   7.878  1.00 66.55           H
ATOM    517  HZ3 LYS A  52     -23.690 -15.969   8.400  1.00 66.55           H
ATOM    518  N   SER A  53     -18.999 -15.558   4.468  1.00 21.42           N
ANISOU  518  N   SER A  53     2927   2440   2771   -496    -74    -60       N
ATOM    519  CA  SER A  53     -18.573 -16.947   4.707  1.00 25.35           C
ANISOU  519  CA  SER A  53     3516   2801   3315   -527   -182    -47       C
ATOM    520  C   SER A  53     -17.126 -17.069   5.182  1.00 24.64           C
ANISOU  520  C   SER A  53     3471   2635   3254   -448   -234    -46       C
ATOM    521  O   SER A  53     -16.753 -18.108   5.769  1.00 24.87           O
ANISOU  521  O   SER A  53     3589   2542   3319   -474   -335     -7       O
ATOM    522  CB  SER A  53     -18.719 -17.770   3.420  1.00 23.93           C
ANISOU  522  CB  SER A  53     3344   2566   3181   -495   -240   -126       C
ATOM    523  OG  SER A  53     -17.892 -17.226   2.443  1.00 24.99           O
ANISOU  523  OG  SER A  53     3440   2739   3316   -367   -209   -205       O
ATOM    524  H   SER A  53     -19.200 -15.368   3.654  1.00 25.70           H
ATOM    525  HG  SER A  53     -17.903 -17.708   1.756  1.00 29.99           H
ATOM    526  N   GLN A  54     -16.324 -16.025   5.006  1.00 21.59           N
ANISOU  526  N   GLN A  54     3026   2315   2862   -361   -175    -82       N
ATOM    527  CA  GLN A  54     -14.915 -16.060   5.350  1.00 22.59           C
ANISOU  527  CA  GLN A  54     3159   2393   3033   -282   -223    -99       C
ATOM    528  C   GLN A  54     -14.589 -15.387   6.682  1.00 25.95           C
ANISOU  528  C   GLN A  54     3598   2851   3413   -320   -217    -38       C
ATOM    529  O   GLN A  54     -13.442 -15.416   7.090  1.00 26.80           O
ANISOU  529  O   GLN A  54     3702   2923   3557   -264   -277    -50       O
ATOM    530  CB  GLN A  54     -14.074 -15.439   4.227  1.00 23.80           C
ANISOU  530  CB  GLN A  54     3231   2596   3216   -174   -165   -189       C
ATOM    531  CG  GLN A  54     -14.271 -16.137   2.844  1.00 24.50           C
ANISOU  531  CG  GLN A  54     3318   2665   3327   -126   -172   -270       C
ATOM    532  CD  GLN A  54     -14.060 -17.658   2.959  1.00 26.07           C
ANISOU  532  CD  GLN A  54     3590   2718   3596   -113   -299   -292       C
ATOM    533  OE1 GLN A  54     -12.979 -18.142   3.311  1.00 25.51           O
ANISOU  533  OE1 GLN A  54     3525   2570   3597    -41   -371   -316       O
ATOM    534  NE2 GLN A  54     -15.098 -18.415   2.629  1.00 28.71           N
ANISOU  534  NE2 GLN A  54     3978   3007   3924   -179   -337   -290       N
ATOM    535  H   GLN A  54     -16.581 -15.271   4.682  1.00 25.91           H
ATOM    536 HE21 GLN A  54     -15.037 -19.271   2.675  1.00 34.46           H
ATOM    537 HE22 GLN A  54     -15.832 -18.049   2.370  1.00 34.46           H
ATOM    538  N   LEU A  55     -15.571 -14.830   7.381  1.00 24.42           N
ANISOU  538  N   LEU A  55     3411   2726   3139   -413   -152     14       N
ATOM    539  CA  LEU A  55     -15.281 -14.158   8.630  1.00 24.37           C
ANISOU  539  CA  LEU A  55     3427   2761   3072   -449   -141     51       C
ATOM    540  C   LEU A  55     -14.876 -15.196   9.670  1.00 24.68           C
ANISOU  540  C   LEU A  55     3574   2713   3091   -494   -266    126       C
ATOM    541  O   LEU A  55     -15.475 -16.282   9.741  1.00 27.05           O
ANISOU  541  O   LEU A  55     3947   2942   3390   -561   -319    182       O
ATOM    542  CB  LEU A  55     -16.515 -13.380   9.082  1.00 23.14           C
ANISOU  542  CB  LEU A  55     3251   2707   2835   -529    -30     69       C
ATOM    543  CG  LEU A  55     -16.831 -12.136   8.225  1.00 21.65           C
ANISOU  543  CG  LEU A  55     2967   2593   2666   -468     76      6       C
ATOM    544  CD1 LEU A  55     -18.181 -11.648   8.670  1.00 23.58           C
ANISOU  544  CD1 LEU A  55     3182   2924   2852   -534    165     17       C
ATOM    545  CD2 LEU A  55     -15.804 -11.006   8.384  1.00 23.91           C
ANISOU  545  CD2 LEU A  55     3224   2892   2966   -408    102    -35       C
ATOM    546  H   LEU A  55     -16.400 -14.829   7.154  1.00 29.30           H
ATOM    547  N   PRO A  56     -13.833 -14.924  10.455  1.00 25.66           N
ANISOU  547  N   PRO A  56     3716   2830   3205   -462   -331    131       N
ATOM    548  CA  PRO A  56     -13.369 -15.926  11.433  1.00 27.77           C
ANISOU  548  CA  PRO A  56     4099   3005   3450   -490   -480    215       C
ATOM    549  C   PRO A  56     -14.331 -16.044  12.613  1.00 29.49           C
ANISOU  549  C   PRO A  56     4421   3263   3521   -639   -455    317       C
ATOM    550  O   PRO A  56     -14.739 -15.046  13.216  1.00 28.43           O
ANISOU  550  O   PRO A  56     4268   3248   3287   -691   -354    303       O
ATOM    551  CB  PRO A  56     -12.004 -15.386  11.889  1.00 25.28           C
ANISOU  551  CB  PRO A  56     3744   2701   3159   -411   -554    177       C
ATOM    552  CG  PRO A  56     -12.156 -13.880  11.756  1.00 27.01           C
ANISOU  552  CG  PRO A  56     3872   3046   3346   -417   -410    106       C
ATOM    553  CD  PRO A  56     -13.079 -13.668  10.529  1.00 23.55           C
ANISOU  553  CD  PRO A  56     3370   2634   2943   -411   -282     67       C
ATOM    554  N   GLU A  57     -14.592 -17.293  13.009  1.00 30.68           N
ANISOU  554  N   GLU A  57     4694   3308   3656   -707   -554    419       N
ATOM    555  CA  GLU A  57     -15.515 -17.538  14.106  1.00 37.59           C
ANISOU  555  CA  GLU A  57     5678   4224   4380   -872   -520    531       C
ATOM    556  C   GLU A  57     -14.970 -16.977  15.405  1.00 35.05           C
ANISOU  556  C   GLU A  57     5423   3973   3922   -897   -556    567       C
ATOM    557  O   GLU A  57     -15.740 -16.466  16.236  1.00 37.99           O
ANISOU  557  O   GLU A  57     5827   4468   4142  -1013   -447    593       O
ATOM    558  CB  GLU A  57     -15.770 -19.049  14.225  1.00 39.59           C
ANISOU  558  CB  GLU A  57     6068   4318   4658   -948   -638    648       C
ATOM    559  CG  GLU A  57     -17.032 -19.469  13.454  1.00 58.38           C
ANISOU  559  CG  GLU A  57     8406   6695   7078  -1039   -542    640       C
ATOM    560  CD  GLU A  57     -17.123 -20.970  13.201  1.00 86.16           C
ANISOU  560  CD  GLU A  57    12042  10015  10681  -1085   -674    717       C
ATOM    561  OE1 GLU A  57     -16.788 -21.754  14.112  1.00 92.11           O
ANISOU  561  OE1 GLU A  57    12957  10655  11384  -1144   -800    847       O
ATOM    562  OE2 GLU A  57     -17.487 -21.363  12.069  1.00 75.57           O
ANISOU  562  OE2 GLU A  57    10640   8617   9456  -1057   -664    643       O
ATOM    563  H   GLU A  57     -14.251 -18.002  12.661  1.00 36.82           H
ATOM    564  N   ARG A  58     -13.643 -16.997  15.589  1.00 33.95           N
ANISOU  564  N   ARG A  58     5292   3773   3833   -787   -702    550       N
ATOM    565  CA  ARG A  58     -13.060 -16.591  16.867  1.00 33.64           C
ANISOU  565  CA  ARG A  58     5331   3792   3657   -815   -776    588       C
ATOM    566  C   ARG A  58     -12.034 -15.483  16.721  1.00 31.34           C
ANISOU  566  C   ARG A  58     4919   3565   3425   -704   -782    462       C
ATOM    567  O   ARG A  58     -11.104 -15.384  17.515  1.00 32.26           O
ANISOU  567  O   ARG A  58     5076   3683   3498   -677   -918    474       O
ATOM    568  CB  ARG A  58     -12.432 -17.783  17.586  1.00 33.77           C
ANISOU  568  CB  ARG A  58     5507   3674   3651   -818   -996    722       C
ATOM    569  CG  ARG A  58     -13.326 -18.931  17.716  1.00 38.89           C
ANISOU  569  CG  ARG A  58     6290   4226   4258   -938  -1008    859       C
ATOM    570  CD  ARG A  58     -12.614 -20.030  18.494  1.00 41.39           C
ANISOU  570  CD  ARG A  58     6786   4390   4550   -931  -1249   1005       C
ATOM    571  NE  ARG A  58     -13.508 -21.095  18.915  1.00 48.87           N
ANISOU  571  NE  ARG A  58     7909   5245   5415  -1093  -1263   1173       N
ATOM    572  CZ  ARG A  58     -13.993 -21.257  20.144  1.00 67.68           C
ANISOU  572  CZ  ARG A  58    10462   7682   7571  -1263  -1261   1322       C
ATOM    573  NH1 ARG A  58     -13.681 -20.434  21.138  1.00 62.62           N
ANISOU  573  NH1 ARG A  58     9852   7194   6747  -1286  -1254   1316       N
ATOM    574  NH2 ARG A  58     -14.800 -22.286  20.388  1.00 49.98           N
ANISOU  574  NH2 ARG A  58     8363   5344   5284  -1419  -1262   1471       N
ATOM    575  H   ARG A  58     -13.071 -17.240  14.994  1.00 40.74           H
ATOM    576  HE  ARG A  58     -13.744 -21.668  18.320  1.00 58.65           H
ATOM    577 HH11 ARG A  58     -13.150 -19.772  20.998  1.00 75.15           H
ATOM    578 HH12 ARG A  58     -14.009 -20.564  21.923  1.00 75.15           H
ATOM    579 HH21 ARG A  58     -15.002 -22.834  19.756  1.00 59.98           H
ATOM    580 HH22 ARG A  58     -15.121 -22.404  21.177  1.00 59.98           H
ATOM    581  N   ASP A  59     -12.204 -14.597  15.748  1.00 27.49           N
ANISOU  581  N   ASP A  59     4284   3133   3028   -651   -641    346       N
ATOM    582  CA  ASP A  59     -11.403 -13.378  15.700  1.00 27.48           C
ANISOU  582  CA  ASP A  59     4178   3200   3063   -588   -614    234       C
ATOM    583  C   ASP A  59     -12.294 -12.266  15.147  1.00 24.82           C
ANISOU  583  C   ASP A  59     3757   2952   2722   -610   -412    156       C
ATOM    584  O   ASP A  59     -13.390 -12.520  14.652  1.00 24.61           O
ANISOU  584  O   ASP A  59     3727   2934   2690   -647   -312    178       O
ATOM    585  CB  ASP A  59     -10.119 -13.580  14.859  1.00 29.47           C
ANISOU  585  CB  ASP A  59     4320   3381   3497   -453   -711    172       C
ATOM    586  CG  ASP A  59      -9.004 -12.565  15.189  1.00 31.18           C
ANISOU  586  CG  ASP A  59     4451   3654   3743   -415   -749     84       C
ATOM    587  OD1 ASP A  59      -9.151 -11.709  16.112  1.00 29.54           O
ANISOU  587  OD1 ASP A  59     4285   3527   3414   -487   -721     66       O
ATOM    588  OD2 ASP A  59      -7.990 -12.585  14.457  1.00 33.53           O
ANISOU  588  OD2 ASP A  59     4627   3922   4193   -317   -794     19       O
ATOM    589  H   ASP A  59     -12.772 -14.677  15.107  1.00 32.99           H
ATOM    590  N   CYS A  60     -11.855 -11.019  15.330  1.00 24.90           N
ANISOU  590  N   CYS A  60     3706   3023   2731   -592   -364     65       N
ATOM    591  CA  CYS A  60     -12.540  -9.846  14.796  1.00 22.08           C
ANISOU  591  CA  CYS A  60     3274   2723   2393   -589   -195    -14       C
ATOM    592  C   CYS A  60     -11.956  -9.394  13.469  1.00 24.41           C
ANISOU  592  C   CYS A  60     3447   2980   2848   -500   -160    -74       C
ATOM    593  O   CYS A  60     -10.810  -9.685  13.140  1.00 25.11           O
ANISOU  593  O   CYS A  60     3487   3024   3029   -443   -253    -90       O
ATOM    594  CB  CYS A  60     -12.509  -8.657  15.776  1.00 24.05           C
ANISOU  594  CB  CYS A  60     3547   3045   2547   -632   -151    -85       C
ATOM    595  SG  CYS A  60     -12.918  -9.067  17.505  1.00 26.14           S
ANISOU  595  SG  CYS A  60     3970   3384   2579   -746   -198    -29       S
ATOM    596  H   CYS A  60     -11.143 -10.825  15.772  1.00 29.88           H
ATOM    597  N   ARG A  61     -12.773  -8.646  12.741  1.00 21.61           N
ANISOU  597  N   ARG A  61     3042   2651   2517   -489    -24   -109       N
ATOM    598  CA  ARG A  61     -12.406  -8.018  11.475  1.00 21.57           C
ANISOU  598  CA  ARG A  61     2942   2622   2629   -422     35   -154       C
ATOM    599  C   ARG A  61     -13.151  -6.706  11.380  1.00 20.65           C
ANISOU  599  C   ARG A  61     2809   2537   2501   -427    158   -199       C
ATOM    600  O   ARG A  61     -14.215  -6.519  11.983  1.00 22.47           O
ANISOU  600  O   ARG A  61     3076   2812   2650   -463    216   -200       O
ATOM    601  CB  ARG A  61     -12.809  -8.904  10.281  1.00 18.98           C
ANISOU  601  CB  ARG A  61     2589   2269   2355   -380     45   -120       C
ATOM    602  CG  ARG A  61     -12.044 -10.202  10.187  1.00 21.22           C
ANISOU  602  CG  ARG A  61     2886   2496   2682   -350    -77    -94       C
ATOM    603  CD  ARG A  61     -10.593  -9.979   9.831  1.00 22.80           C
ANISOU  603  CD  ARG A  61     3006   2678   2978   -290   -121   -147       C
ATOM    604  NE  ARG A  61      -9.939 -11.250   9.663  1.00 24.39           N
ANISOU  604  NE  ARG A  61     3209   2820   3240   -235   -237   -138       N
ATOM    605  CZ  ARG A  61      -9.229 -11.861  10.603  1.00 24.40           C
ANISOU  605  CZ  ARG A  61     3245   2785   3241   -228   -380   -114       C
ATOM    606  NH1 ARG A  61      -9.176 -11.404  11.854  1.00 23.85           N
ANISOU  606  NH1 ARG A  61     3230   2745   3085   -290   -426    -91       N
ATOM    607  NH2 ARG A  61      -8.569 -12.976  10.289  1.00 25.74           N
ANISOU  607  NH2 ARG A  61     3401   2883   3496   -150   -490   -119       N
ATOM    608  H   ARG A  61     -13.585  -8.477  12.967  1.00 25.94           H
ATOM    609  HE  ARG A  61     -10.012 -11.640   8.900  1.00 29.28           H
ATOM    610 HH11 ARG A  61      -9.610 -10.694  12.071  1.00 28.62           H
ATOM    611 HH12 ARG A  61      -8.708 -11.820  12.444  1.00 28.62           H
ATOM    612 HH21 ARG A  61      -8.608 -13.287   9.488  1.00 30.89           H
ATOM    613 HH22 ARG A  61      -8.105 -13.384  10.887  1.00 30.89           H
ATOM    614  N   TYR A  62     -12.619  -5.806  10.548  1.00 19.59           N
ANISOU  614  N   TYR A  62     2616   2374   2456   -388    204   -236       N
ATOM    615  CA  TYR A  62     -13.356  -4.684  10.018  1.00 22.90           C
ANISOU  615  CA  TYR A  62     3019   2787   2897   -366    309   -259       C
ATOM    616  C   TYR A  62     -13.670  -4.950   8.552  1.00 19.91           C
ANISOU  616  C   TYR A  62     2599   2398   2567   -314    344   -219       C
ATOM    617  O   TYR A  62     -12.969  -5.706   7.878  1.00 18.56           O
ANISOU  617  O   TYR A  62     2401   2219   2432   -295    305   -202       O
ATOM    618  CB  TYR A  62     -12.557  -3.380  10.041  1.00 23.54           C
ANISOU  618  CB  TYR A  62     3084   2822   3039   -374    334   -312       C
ATOM    619  CG  TYR A  62     -11.984  -2.941  11.361  1.00 23.15           C
ANISOU  619  CG  TYR A  62     3069   2775   2952   -428    285   -375       C
ATOM    620  CD1 TYR A  62     -12.800  -2.634  12.463  1.00 25.48           C
ANISOU  620  CD1 TYR A  62     3425   3105   3150   -453    308   -417       C
ATOM    621  CD2 TYR A  62     -10.603  -2.819  11.504  1.00 23.92           C
ANISOU  621  CD2 TYR A  62     3129   2852   3108   -457    215   -403       C
ATOM    622  CE1 TYR A  62     -12.226  -2.211  13.675  1.00 23.40           C
ANISOU  622  CE1 TYR A  62     3207   2852   2831   -506    256   -487       C
ATOM    623  CE2 TYR A  62     -10.038  -2.393  12.696  1.00 26.00           C
ANISOU  623  CE2 TYR A  62     3423   3123   3335   -510    150   -469       C
ATOM    624  CZ  TYR A  62     -10.838  -2.091  13.766  1.00 26.00           C
ANISOU  624  CZ  TYR A  62     3504   3152   3221   -534    167   -510       C
ATOM    625  OH  TYR A  62     -10.232  -1.654  14.927  1.00 24.55           O
ANISOU  625  OH  TYR A  62     3361   2983   2985   -591     94   -587       O
ATOM    626  H   TYR A  62     -11.805  -5.836  10.273  1.00 23.52           H
ATOM    627  HH  TYR A  62     -10.809  -1.345  15.453  1.00 29.47           H
ATOM    628  N   ALA A  63     -14.703  -4.285   8.048  1.00 20.42           N
ANISOU  628  N   ALA A  63     2659   2466   2633   -282    415   -214       N
ATOM    629  CA  ALA A  63     -14.988  -4.405   6.611  1.00 20.78           C
ANISOU  629  CA  ALA A  63     2678   2509   2708   -233    437   -176       C
ATOM    630  C   ALA A  63     -15.722  -3.167   6.122  1.00 22.79           C
ANISOU  630  C   ALA A  63     2934   2739   2986   -189    498   -172       C
ATOM    631  O   ALA A  63     -16.405  -2.474   6.890  1.00 21.32           O
ANISOU  631  O   ALA A  63     2756   2549   2795   -182    527   -208       O
ATOM    632  CB  ALA A  63     -15.840  -5.641   6.358  1.00 21.38           C
ANISOU  632  CB  ALA A  63     2749   2629   2745   -232    405   -148       C
ATOM    633  H   ALA A  63     -15.236  -3.778   8.494  1.00 24.50           H
ATOM    634  N   ILE A  64     -15.592  -2.909   4.821  1.00 20.89           N
ANISOU  634  N   ILE A  64     2689   2480   2767   -152    515   -130       N
ATOM    635  CA  ILE A  64     -16.436  -1.978   4.092  1.00 22.04           C
ANISOU  635  CA  ILE A  64     2847   2600   2928    -93    543    -99       C
ATOM    636  C   ILE A  64     -17.140  -2.785   3.013  1.00 21.93           C
ANISOU  636  C   ILE A  64     2815   2644   2872    -57    514    -59       C
ATOM    637  O   ILE A  64     -16.495  -3.539   2.275  1.00 21.58           O
ANISOU  637  O   ILE A  64     2773   2624   2803    -71    501    -45       O
ATOM    638  CB  ILE A  64     -15.624  -0.839   3.467  1.00 22.59           C
ANISOU  638  CB  ILE A  64     2954   2590   3041    -98    580    -66       C
ATOM    639  CG1 ILE A  64     -15.009   0.066   4.547  1.00 22.15           C
ANISOU  639  CG1 ILE A  64     2917   2463   3038   -142    598   -120       C
ATOM    640  CG2 ILE A  64     -16.504  -0.001   2.485  1.00 22.36           C
ANISOU  640  CG2 ILE A  64     2958   2522   3017    -25    585     -3       C
ATOM    641  CD1 ILE A  64     -15.968   1.088   5.128  1.00 26.17           C
ANISOU  641  CD1 ILE A  64     3450   2913   3579    -91    612   -156       C
ATOM    642  H   ILE A  64     -14.995  -3.279   4.324  1.00 25.07           H
ATOM    643  N   PHE A  65     -18.453  -2.673   2.959  1.00 22.80           N
ANISOU  643  N   PHE A  65     2899   2783   2979    -10    502    -57       N
ATOM    644  CA  PHE A  65     -19.254  -3.366   1.943  1.00 23.82           C
ANISOU  644  CA  PHE A  65     3005   2973   3073     22    456    -29       C
ATOM    645  C   PHE A  65     -20.081  -2.318   1.237  1.00 24.52           C
ANISOU  645  C   PHE A  65     3095   3041   3181    107    445      9       C
ATOM    646  O   PHE A  65     -20.795  -1.548   1.894  1.00 24.36           O
ANISOU  646  O   PHE A  65     3045   3000   3212    150    460    -18       O
ATOM    647  CB  PHE A  65     -20.156  -4.426   2.608  1.00 22.72           C
ANISOU  647  CB  PHE A  65     2807   2903   2921    -15    431    -65       C
ATOM    648  CG  PHE A  65     -20.670  -5.461   1.637  1.00 21.46           C
ANISOU  648  CG  PHE A  65     2629   2797   2727    -17    370    -53       C
ATOM    649  CD1 PHE A  65     -21.701  -5.146   0.745  1.00 21.89           C
ANISOU  649  CD1 PHE A  65     2648   2891   2778     45    330    -35       C
ATOM    650  CD2 PHE A  65     -20.134  -6.732   1.626  1.00 18.54           C
ANISOU  650  CD2 PHE A  65     2280   2431   2335    -74    339    -68       C
ATOM    651  CE1 PHE A  65     -22.138  -6.110  -0.218  1.00 21.07           C
ANISOU  651  CE1 PHE A  65     2533   2839   2633     35    259    -37       C
ATOM    652  CE2 PHE A  65     -20.530  -7.677   0.675  1.00 22.28           C
ANISOU  652  CE2 PHE A  65     2750   2937   2779    -78    278    -76       C
ATOM    653  CZ  PHE A  65     -21.534  -7.389  -0.221  1.00 21.66           C
ANISOU  653  CZ  PHE A  65     2638   2908   2684    -32    240    -64       C
ATOM    654  H   PHE A  65     -18.918  -2.196   3.504  1.00 27.36           H
ATOM    655  N   ASP A  66     -19.958  -2.267  -0.093  1.00 24.88           N
ANISOU  655  N   ASP A  66     3181   3091   3182    136    415     69       N
ATOM    656  CA  ASP A  66     -20.750  -1.368  -0.917  1.00 25.00           C
ANISOU  656  CA  ASP A  66     3215   3085   3200    224    374    128       C
ATOM    657  C   ASP A  66     -22.078  -2.071  -1.165  1.00 26.61           C
ANISOU  657  C   ASP A  66     3335   3382   3393    261    300    103       C
ATOM    658  O   ASP A  66     -22.217  -2.849  -2.115  1.00 22.60           O
ANISOU  658  O   ASP A  66     2835   2939   2814    252    246    118       O
ATOM    659  CB  ASP A  66     -20.008  -1.058  -2.208  1.00 24.65           C
ANISOU  659  CB  ASP A  66     3263   3019   3083    221    375    211       C
ATOM    660  CG  ASP A  66     -20.695   0.013  -3.027  1.00 31.60           C
ANISOU  660  CG  ASP A  66     4196   3851   3960    310    321    299       C
ATOM    661  OD1 ASP A  66     -21.702   0.584  -2.539  1.00 30.61           O
ANISOU  661  OD1 ASP A  66     4019   3696   3913    390    281    280       O
ATOM    662  OD2 ASP A  66     -20.282   0.197  -4.190  1.00 30.32           O
ANISOU  662  OD2 ASP A  66     4121   3692   3708    305    312    383       O
ATOM    663  H   ASP A  66     -19.411  -2.755  -0.544  1.00 29.86           H
ATOM    664  N   TYR A  67     -23.046  -1.845  -0.262  1.00 25.74           N
ANISOU  664  N   TYR A  67     3136   3290   3354    293    304     51       N
ATOM    665  CA  TYR A  67     -24.292  -2.618  -0.248  1.00 25.34           C
ANISOU  665  CA  TYR A  67     2972   3345   3312    297    252     10       C
ATOM    666  C   TYR A  67     -25.312  -2.039  -1.228  1.00 26.32           C
ANISOU  666  C   TYR A  67     3059   3491   3452    410    158     48       C
ATOM    667  O   TYR A  67     -25.798  -0.924  -1.045  1.00 25.76           O
ANISOU  667  O   TYR A  67     2967   3369   3454    511    152     52       O
ATOM    668  CB  TYR A  67     -24.888  -2.704   1.175  1.00 25.13           C
ANISOU  668  CB  TYR A  67     2850   3356   3344    267    317    -69       C
ATOM    669  CG  TYR A  67     -25.929  -3.771   1.203  1.00 25.31           C
ANISOU  669  CG  TYR A  67     2759   3495   3365    217    281   -105       C
ATOM    670  CD1 TYR A  67     -27.256  -3.471   0.926  1.00 30.13           C
ANISOU  670  CD1 TYR A  67     3240   4175   4032    293    233   -129       C
ATOM    671  CD2 TYR A  67     -25.574  -5.110   1.315  1.00 24.51           C
ANISOU  671  CD2 TYR A  67     2677   3422   3213     98    275   -109       C
ATOM    672  CE1 TYR A  67     -28.211  -4.477   0.846  1.00 32.21           C
ANISOU  672  CE1 TYR A  67     3386   4551   4303    228    192   -162       C
ATOM    673  CE2 TYR A  67     -26.525  -6.124   1.234  1.00 26.67           C
ANISOU  673  CE2 TYR A  67     2857   3785   3492     33    232   -135       C
ATOM    674  CZ  TYR A  67     -27.840  -5.803   0.992  1.00 28.72           C
ANISOU  674  CZ  TYR A  67     2979   4127   3808     88    195   -162       C
ATOM    675  OH  TYR A  67     -28.797  -6.789   0.883  1.00 31.20           O
ANISOU  675  OH  TYR A  67     3182   4534   4138      7    150   -193       O
ATOM    676  H   TYR A  67     -23.002  -1.247   0.354  1.00 30.89           H
ATOM    677  HH  TYR A  67     -29.489  -6.479   0.522  1.00 37.44           H
ATOM    678  N   GLU A  68     -25.649  -2.819  -2.242  1.00 24.42           N
ANISOU  678  N   GLU A  68     2810   3322   3145    398     71     66       N
ATOM    679  CA  GLU A  68     -26.533  -2.427  -3.326  1.00 28.09           C
ANISOU  679  CA  GLU A  68     3253   3822   3597    497    -50    110       C
ATOM    680  C   GLU A  68     -27.925  -2.994  -3.123  1.00 27.62           C
ANISOU  680  C   GLU A  68     3020   3877   3599    505   -115     41       C
ATOM    681  O   GLU A  68     -28.089  -4.174  -2.785  1.00 29.06           O
ANISOU  681  O   GLU A  68     3141   4128   3770    395   -101    -17       O
ATOM    682  CB  GLU A  68     -25.982  -2.936  -4.671  1.00 27.50           C
ANISOU  682  CB  GLU A  68     3290   3772   3386    471   -113    164       C
ATOM    683  CG  GLU A  68     -24.593  -2.559  -4.928  1.00 32.70           C
ANISOU  683  CG  GLU A  68     4096   4351   3980    438    -32    222       C
ATOM    684  CD  GLU A  68     -24.297  -2.515  -6.422  1.00 39.58           C
ANISOU  684  CD  GLU A  68     5083   5249   4708    456    -96    298       C
ATOM    685  OE1 GLU A  68     -23.631  -1.552  -6.857  1.00 38.58           O
ANISOU  685  OE1 GLU A  68     5071   5047   4542    478    -62    393       O
ATOM    686  OE2 GLU A  68     -24.683  -3.472  -7.144  1.00 41.22           O
ANISOU  686  OE2 GLU A  68     5275   5552   4834    434   -174    261       O
ATOM    687  H   GLU A  68     -25.362  -3.625  -2.330  1.00 29.30           H
ATOM    688  N   PHE A  69     -28.932  -2.166  -3.350  1.00 28.09           N
ANISOU  688  N   PHE A  69     2993   3950   3730    633   -192     49       N
ATOM    689  CA  PHE A  69     -30.322  -2.618  -3.246  1.00 28.22           C
ANISOU  689  CA  PHE A  69     2811   4092   3819    648   -262    -22       C
ATOM    690  C   PHE A  69     -31.184  -1.731  -4.123  1.00 29.40           C
ANISOU  690  C   PHE A  69     2915   4247   4008    816   -411     21       C
ATOM    691  O   PHE A  69     -30.717  -0.725  -4.657  1.00 32.75           O
ANISOU  691  O   PHE A  69     3475   4561   4407    915   -446    112       O
ATOM    692  CB  PHE A  69     -30.836  -2.611  -1.801  1.00 31.09           C
ANISOU  692  CB  PHE A  69     3027   4495   4291    617   -141   -118       C
ATOM    693  CG  PHE A  69     -30.688  -1.278  -1.092  1.00 32.96           C
ANISOU  693  CG  PHE A  69     3282   4634   4609    731    -66   -128       C
ATOM    694  CD1 PHE A  69     -29.445  -0.864  -0.612  1.00 33.85           C
ANISOU  694  CD1 PHE A  69     3554   4624   4682    694     33    -99       C
ATOM    695  CD2 PHE A  69     -31.784  -0.454  -0.912  1.00 33.99           C
ANISOU  695  CD2 PHE A  69     3262   4790   4862    878   -101   -180       C
ATOM    696  CE1 PHE A  69     -29.319   0.359   0.070  1.00 33.81           C
ANISOU  696  CE1 PHE A  69     3572   4516   4757    789     95   -126       C
ATOM    697  CE2 PHE A  69     -31.651   0.766  -0.266  1.00 35.30           C
ANISOU  697  CE2 PHE A  69     3454   4846   5110    991    -37   -209       C
ATOM    698  CZ  PHE A  69     -30.422   1.169   0.208  1.00 32.74           C
ANISOU  698  CZ  PHE A  69     3305   4392   4742    940     58   -181       C
ATOM    699  H   PHE A  69     -28.843  -1.338  -3.566  1.00 33.71           H
ATOM    700  N   GLN A  70     -32.440  -2.132  -4.305  1.00 28.16           N
ANISOU  700  N   GLN A  70     2568   4217   3913    841   -510    -38       N
ATOM    701  CA  GLN A  70     -33.398  -1.367  -5.082  1.00 33.62           C
ANISOU  701  CA  GLN A  70     3182   4933   4661   1012   -679     -8       C
ATOM    702  C   GLN A  70     -34.490  -0.802  -4.189  1.00 37.92           C
ANISOU  702  C   GLN A  70     3495   5525   5389   1116   -650   -105       C
ATOM    703  O   GLN A  70     -34.987  -1.476  -3.280  1.00 33.92           O
ANISOU  703  O   GLN A  70     2817   5124   4945   1016   -549   -212       O
ATOM    704  CB  GLN A  70     -34.037  -2.234  -6.159  1.00 35.78           C
ANISOU  704  CB  GLN A  70     3399   5332   4864    976   -851    -11       C
ATOM    705  CG  GLN A  70     -33.037  -3.016  -6.945  1.00 35.63           C
ANISOU  705  CG  GLN A  70     3581   5296   4663    857   -858     40       C
ATOM    706  CD  GLN A  70     -33.686  -3.685  -8.122  1.00 38.87           C
ANISOU  706  CD  GLN A  70     3959   5820   4990    846  -1051     32       C
ATOM    707  OE1 GLN A  70     -34.830  -4.134  -8.034  1.00 39.23           O
ANISOU  707  OE1 GLN A  70     3791   5984   5128    836  -1138    -50       O
ATOM    708  NE2 GLN A  70     -32.980  -3.735  -9.249  1.00 44.84           N
ANISOU  708  NE2 GLN A  70     4920   6551   5565    844  -1120    111       N
ATOM    709  N   VAL A  71     -34.880   0.433  -4.464  1.00 38.04           N
ANISOU  709  N   VAL A  71     3504   5461   5488   1318   -739    -68       N
ATOM    710  CA  VAL A  71     -36.041   1.020  -3.833  1.00 41.86           C
ANISOU  710  CA  VAL A  71     3746   5999   6159   1459   -745   -173       C
ATOM    711  C   VAL A  71     -36.937   1.509  -4.956  1.00 48.57           C
ANISOU  711  C   VAL A  71     4526   6874   7054   1640   -991   -122       C
ATOM    712  O   VAL A  71     -36.500   2.302  -5.800  1.00 48.66           O
ANISOU  712  O   VAL A  71     4734   6747   7007   1751  -1109     11       O
ATOM    713  CB  VAL A  71     -35.676   2.171  -2.893  1.00 41.24           C
ANISOU  713  CB  VAL A  71     3720   5774   6177   1563   -616   -205       C
ATOM    714  CG1 VAL A  71     -36.937   2.968  -2.578  1.00 46.55           C
ANISOU  714  CG1 VAL A  71     4154   6484   7048   1772   -672   -308       C
ATOM    715  CG2 VAL A  71     -34.955   1.672  -1.656  1.00 43.24           C
ANISOU  715  CG2 VAL A  71     4006   6034   6389   1389   -386   -277       C
ATOM    716  N   ASP A  72     -38.181   1.032  -4.968  1.00 48.84           N
ANISOU  716  N   ASP A  72     4282   7085   7188   1661  -1074   -221       N
ATOM    717  CA  ASP A  72     -39.132   1.326  -6.038  1.00 54.65           C
ANISOU  717  CA  ASP A  72     4914   7880   7970   1822  -1336   -187       C
ATOM    718  C   ASP A  72     -38.486   1.153  -7.414  1.00 54.14           C
ANISOU  718  C   ASP A  72     5108   7762   7700   1795  -1501    -28       C
ATOM    719  O   ASP A  72     -38.666   1.976  -8.316  1.00 54.98           O
ANISOU  719  O   ASP A  72     5305   7793   7790   1969  -1698     82       O
ATOM    720  CB  ASP A  72     -39.730   2.733  -5.883  1.00 61.74           C
ANISOU  720  CB  ASP A  72     5732   8679   9049   2101  -1413   -197       C
ATOM    721  CG  ASP A  72     -40.442   2.950  -4.528  1.00 69.25           C
ANISOU  721  CG  ASP A  72     6423   9696  10191   2129  -1228   -375       C
ATOM    722  OD1 ASP A  72     -41.112   2.019  -4.015  1.00 71.04           O
ANISOU  722  OD1 ASP A  72     6424  10116  10453   1980  -1137   -489       O
ATOM    723  OD2 ASP A  72     -40.357   4.080  -3.991  1.00 66.34           O
ANISOU  723  OD2 ASP A  72     6111   9175   9921   2270  -1154   -386       O
ATOM    724  N   GLY A  73     -37.726   0.061  -7.575  1.00 51.86           N
ANISOU  724  N   GLY A  73     4944   7513   7246   1574  -1421    -16       N
ATOM    725  CA  GLY A  73     -37.065  -0.253  -8.827  1.00 56.33           C
ANISOU  725  CA  GLY A  73     5748   8057   7597   1523  -1541    104       C
ATOM    726  C   GLY A  73     -35.830   0.568  -9.146  1.00 55.22           C
ANISOU  726  C   GLY A  73     5915   7729   7337   1555  -1484    252       C
ATOM    727  O   GLY A  73     -35.136   0.256 -10.127  1.00 62.71           O
ANISOU  727  O   GLY A  73     7073   8671   8084   1486  -1537    346       O
ATOM    728  N   GLY A  74     -35.540   1.614  -8.370  1.00 47.94           N
ANISOU  728  N   GLY A  74     5026   6658   6531   1651  -1374    269       N
ATOM    729  CA  GLY A  74     -34.329   2.383  -8.560  1.00 43.33           C
ANISOU  729  CA  GLY A  74     4722   5889   5854   1650  -1300    401       C
ATOM    730  C   GLY A  74     -33.176   1.807  -7.761  1.00 40.45           C
ANISOU  730  C   GLY A  74     4442   5494   5434   1461  -1062    358       C
ATOM    731  O   GLY A  74     -33.354   1.233  -6.690  1.00 38.62           O
ANISOU  731  O   GLY A  74     4055   5328   5290   1379   -928    227       O
ATOM    732  N  AGLN A  75     -31.971   1.966  -8.295  0.38 38.68           N
ANISOU  732  N  AGLN A  75     4464   5175   5058   1388  -1010    473       N
ATOM    733  CA AGLN A  75     -30.777   1.455  -7.638  0.38 36.28           C
ANISOU  733  CA AGLN A  75     4245   4839   4701   1220   -805    439       C
ATOM    734  C  AGLN A  75     -30.316   2.393  -6.530  0.38 36.80           C
ANISOU  734  C  AGLN A  75     4332   4754   4896   1253   -666    420       C
ATOM    735  O  AGLN A  75     -30.335   3.615  -6.679  0.38 37.09           O
ANISOU  735  O  AGLN A  75     4453   4645   4995   1379   -714    500       O
ATOM    736  CB AGLN A  75     -29.661   1.274  -8.660  0.38 36.85           C
ANISOU  736  CB AGLN A  75     4547   4887   4568   1131   -796    554       C
ATOM    737  CG AGLN A  75     -30.187   0.683  -9.944  0.38 36.55           C
ANISOU  737  CG AGLN A  75     4528   4977   4384   1140   -971    588       C
ATOM    738  CD AGLN A  75     -30.558  -0.785  -9.834  0.38 35.97           C
ANISOU  738  CD AGLN A  75     4317   5062   4288   1028   -973    452       C
ATOM    739  OE1AGLN A  75     -29.863  -1.561  -9.188  0.38 38.18           O
ANISOU  739  OE1AGLN A  75     4593   5348   4566    896   -823    378       O
ATOM    740  NE2AGLN A  75     -31.718  -1.140 -10.363  0.38 37.45           N
ANISOU  740  NE2AGLN A  75     4377   5367   4485   1083  -1152    415       N
ATOM    741  H  AGLN A  75     -31.818   2.367  -9.039  0.38 46.42           H
ATOM    742 HE21AGLN A  75     -32.216  -0.551 -10.743  0.38 44.94           H
ATOM    743 HE22AGLN A  75     -31.974  -1.960 -10.327  0.38 44.94           H
ATOM    744  N  BGLN A  75     -31.967   1.976  -8.287  0.43 38.79           N
ANISOU  744  N  BGLN A  75     4479   5187   5073   1388  -1009    473       N
ATOM    745  CA BGLN A  75     -30.795   1.430  -7.624  0.43 36.68           C
ANISOU  745  CA BGLN A  75     4291   4894   4753   1219   -805    436       C
ATOM    746  C  BGLN A  75     -30.285   2.380  -6.547  0.43 37.97           C
ANISOU  746  C  BGLN A  75     4486   4903   5040   1249   -664    423       C
ATOM    747  O  BGLN A  75     -30.246   3.597  -6.730  0.43 37.27           O
ANISOU  747  O  BGLN A  75     4492   4666   5005   1369   -711    508       O
ATOM    748  CB BGLN A  75     -29.687   1.134  -8.634  0.43 36.66           C
ANISOU  748  CB BGLN A  75     4510   4879   4542   1120   -793    541       C
ATOM    749  CG BGLN A  75     -28.514   0.330  -8.061  0.43 35.86           C
ANISOU  749  CG BGLN A  75     4457   4782   4388    948   -607    483       C
ATOM    750  CD BGLN A  75     -27.282   0.372  -8.944  0.43 35.34           C
ANISOU  750  CD BGLN A  75     4604   4678   4144    873   -559    585       C
ATOM    751  OE1BGLN A  75     -27.365   0.158 -10.166  0.43 37.51           O
ANISOU  751  OE1BGLN A  75     4970   5022   4262    879   -665    650       O
ATOM    752  NE2BGLN A  75     -26.132   0.644  -8.344  0.43 33.67           N
ANISOU  752  NE2BGLN A  75     4468   4373   3950    796   -399    593       N
ATOM    753  H  BGLN A  75     -31.804   2.399  -9.018  0.43 46.55           H
ATOM    754 HE21BGLN A  75     -26.113   0.785  -7.496  0.43 40.40           H
ATOM    755 HE22BGLN A  75     -25.405   0.679  -8.802  0.43 40.40           H
ATOM    756  N  CGLN A  75     -31.975   1.987  -8.296  0.19 39.00           N
ANISOU  756  N  CGLN A  75     4505   5213   5099   1390  -1011    474       N
ATOM    757  CA CGLN A  75     -30.778   1.482  -7.646  0.19 36.09           C
ANISOU  757  CA CGLN A  75     4223   4813   4678   1223   -807    442       C
ATOM    758  C  CGLN A  75     -30.316   2.407  -6.525  0.19 36.73           C
ANISOU  758  C  CGLN A  75     4323   4743   4888   1254   -665    421       C
ATOM    759  O  CGLN A  75     -30.324   3.632  -6.666  0.19 37.53           O
ANISOU  759  O  CGLN A  75     4510   4698   5053   1379   -712    501       O
ATOM    760  CB CGLN A  75     -29.653   1.317  -8.662  0.19 36.54           C
ANISOU  760  CB CGLN A  75     4511   4842   4529   1134   -796    557       C
ATOM    761  CG CGLN A  75     -28.510   0.497  -8.127  0.19 35.87           C
ANISOU  761  CG CGLN A  75     4473   4768   4389    963   -615    500       C
ATOM    762  CD CGLN A  75     -28.928  -0.920  -7.803  0.19 35.66           C
ANISOU  762  CD CGLN A  75     4301   4885   4363    865   -607    369       C
ATOM    763  OE1CGLN A  75     -29.683  -1.547  -8.548  0.19 36.96           O
ANISOU  763  OE1CGLN A  75     4408   5164   4473    872   -743    347       O
ATOM    764  NE2CGLN A  75     -28.468  -1.419  -6.669  0.19 34.44           N
ANISOU  764  NE2CGLN A  75     4093   4719   4275    768   -460    284       N
ATOM    765  H  CGLN A  75     -31.828   2.400  -9.036  0.19 46.80           H
ATOM    766 HE21CGLN A  75     -27.962  -0.942  -6.163  0.19 41.33           H
ATOM    767 HE22CGLN A  75     -28.675  -2.221  -6.436  0.19 41.33           H
ATOM    768  N   ARG A  76     -29.924   1.813  -5.402  1.00 33.24           N
ANISOU  768  N   ARG A  76     3812   4331   4486   1138   -503    312       N
ATOM    769  CA  ARG A  76     -29.278   2.562  -4.332  1.00 33.78           C
ANISOU  769  CA  ARG A  76     3926   4269   4641   1133   -360    281       C
ATOM    770  C   ARG A  76     -28.081   1.774  -3.828  1.00 32.22           C
ANISOU  770  C   ARG A  76     3800   4083   4359    953   -214    256       C
ATOM    771  O   ARG A  76     -28.015   0.550  -3.959  1.00 31.39           O
ANISOU  771  O   ARG A  76     3655   4097   4176    844   -206    220       O
ATOM    772  CB  ARG A  76     -30.220   2.832  -3.164  1.00 33.75           C
ANISOU  772  CB  ARG A  76     3728   4294   4800   1210   -313    145       C
ATOM    773  CG  ARG A  76     -31.595   3.238  -3.611  1.00 38.79           C
ANISOU  773  CG  ARG A  76     4218   4982   5538   1384   -466    130       C
ATOM    774  CD  ARG A  76     -31.760   4.721  -3.467  1.00 39.64           C
ANISOU  774  CD  ARG A  76     4375   4912   5775   1566   -502    152       C
ATOM    775  NE  ARG A  76     -33.098   5.178  -3.828  1.00 46.58           N
ANISOU  775  NE  ARG A  76     5093   5828   6777   1764   -660    127       N
ATOM    776  CZ  ARG A  76     -33.622   5.202  -5.054  1.00 56.32           C
ANISOU  776  CZ  ARG A  76     6341   7092   7967   1852   -862    231       C
ATOM    777  NH1 ARG A  76     -32.933   4.821  -6.128  1.00 46.36           N
ANISOU  777  NH1 ARG A  76     5265   5829   6520   1758   -927    372       N
ATOM    778  NH2 ARG A  76     -34.879   5.613  -5.209  1.00 68.79           N
ANISOU  778  NH2 ARG A  76     7737   8714   9687   2043  -1006    184       N
ATOM    779  H   ARG A  76     -30.044   0.982  -5.217  1.00 39.89           H
ATOM    780  HE  ARG A  76     -33.598   5.460  -3.187  1.00 55.90           H
ATOM    781 HH11 ARG A  76     -32.121   4.549  -6.044  1.00 55.63           H
ATOM    782 HH12 ARG A  76     -33.299   4.848  -6.905  1.00 55.63           H
ATOM    783 HH21 ARG A  76     -35.339   5.858  -4.525  1.00 82.56           H
ATOM    784 HH22 ARG A  76     -35.231   5.633  -5.993  1.00 82.56           H
ATOM    785  N  AASN A  77     -27.150   2.498  -3.219  0.55 31.44           N
ANISOU  785  N  AASN A  77     3805   3851   4291    927   -110    267       N
ATOM    786  CA AASN A  77     -25.948   1.922  -2.642  0.55 30.60           C
ANISOU  786  CA AASN A  77     3759   3740   4128    774     18    240       C
ATOM    787  C  AASN A  77     -25.722   2.576  -1.295  0.55 31.23           C
ANISOU  787  C  AASN A  77     3818   3736   4311    776    122    156       C
ATOM    788  O  AASN A  77     -26.058   3.744  -1.107  0.55 32.30           O
ANISOU  788  O  AASN A  77     3970   3756   4545    889    104    156       O
ATOM    789  CB AASN A  77     -24.746   2.180  -3.541  0.55 31.70           C
ANISOU  789  CB AASN A  77     4076   3804   4165    716     31    357       C
ATOM    790  CG AASN A  77     -24.685   1.225  -4.705  0.55 29.61           C
ANISOU  790  CG AASN A  77     3840   3652   3757    670    -30    403       C
ATOM    791  OD1AASN A  77     -23.906   0.283  -4.713  0.55 31.11           O
ANISOU  791  OD1AASN A  77     4047   3901   3872    560     32    372       O
ATOM    792  ND2AASN A  77     -25.584   1.423  -5.658  0.55 30.73           N
ANISOU  792  ND2AASN A  77     3980   3830   3866    767   -166    462       N
ATOM    793  H  AASN A  77     -27.195   3.352  -3.125  0.55 37.73           H
ATOM    794 HD21AASN A  77     -26.152   2.065  -5.588  0.55 36.88           H
ATOM    795 HD22AASN A  77     -25.598   0.910  -6.348  0.55 36.88           H
ATOM    796  N  BASN A  77     -27.111   2.475  -3.253  0.45 31.30           N
ANISOU  796  N  BASN A  77     3793   3833   4268    922   -110    270       N
ATOM    797  CA BASN A  77     -25.991   1.785  -2.625  0.45 30.60           C
ANISOU  797  CA BASN A  77     3747   3757   4123    767     19    232       C
ATOM    798  C  BASN A  77     -25.570   2.559  -1.385  0.45 31.23           C
ANISOU  798  C  BASN A  77     3837   3731   4299    765    124    169       C
ATOM    799  O  BASN A  77     -25.623   3.789  -1.364  0.45 31.94           O
ANISOU  799  O  BASN A  77     3985   3682   4468    859    107    197       O
ATOM    800  CB BASN A  77     -24.811   1.591  -3.602  0.45 31.71           C
ANISOU  800  CB BASN A  77     4045   3870   4133    684     28    335       C
ATOM    801  CG BASN A  77     -23.988   2.846  -3.787  0.45 31.89           C
ANISOU  801  CG BASN A  77     4215   3728   4174    698     62    426       C
ATOM    802  OD1BASN A  77     -24.508   3.854  -4.259  0.45 32.10           O
ANISOU  802  OD1BASN A  77     4291   3662   4244    810    -19    501       O
ATOM    803  ND2BASN A  77     -22.693   2.782  -3.467  0.45 30.89           N
ANISOU  803  ND2BASN A  77     4158   3558   4020    580    170    426       N
ATOM    804  H  BASN A  77     -27.079   3.334  -3.214  0.45 37.57           H
ATOM    805 HD21BASN A  77     -22.360   2.048  -3.169  0.45 37.07           H
ATOM    806 HD22BASN A  77     -22.193   3.476  -3.558  0.45 37.07           H
ATOM    807  N   LYS A  78     -25.147   1.828  -0.362  1.00 27.69           N
ANISOU  807  N   LYS A  78     3344   3338   3838    655    221     83       N
ATOM    808  CA  LYS A  78     -24.749   2.412   0.919  1.00 28.22           C
ANISOU  808  CA  LYS A  78     3418   3333   3970    636    318      2       C
ATOM    809  C   LYS A  78     -23.384   1.847   1.278  1.00 26.27           C
ANISOU  809  C   LYS A  78     3249   3078   3653    492    387      7       C
ATOM    810  O   LYS A  78     -23.228   0.623   1.426  1.00 27.93           O
ANISOU  810  O   LYS A  78     3420   3394   3798    403    399    -13       O
ATOM    811  CB  LYS A  78     -25.754   2.137   2.044  1.00 29.16           C
ANISOU  811  CB  LYS A  78     3387   3552   4141    656    365   -126       C
ATOM    812  CG  LYS A  78     -27.113   2.846   1.888  1.00 30.96           C
ANISOU  812  CG  LYS A  78     3502   3787   4473    820    309   -165       C
ATOM    813  CD  LYS A  78     -27.021   4.382   1.958  1.00 34.33           C
ANISOU  813  CD  LYS A  78     4007   4033   5005    949    297   -168       C
ATOM    814  CE  LYS A  78     -28.388   5.030   1.745  1.00 38.04           C
ANISOU  814  CE  LYS A  78     4352   4507   5594   1137    222   -211       C
ATOM    815  NZ  LYS A  78     -28.311   6.068   0.662  1.00 46.06           N
ANISOU  815  NZ  LYS A  78     5491   5353   6658   1261     99    -87       N
ATOM    816  H   LYS A  78     -24.976   0.989  -0.440  1.00 33.23           H
ATOM    817  HZ1 LYS A  78     -27.592   6.578   0.779  1.00 55.28           H
ATOM    818  HZ2 LYS A  78     -28.259   5.674  -0.135  1.00 55.28           H
ATOM    819  HZ3 LYS A  78     -29.037   6.583   0.682  1.00 55.28           H
ATOM    820  N  AILE A  79     -22.401   2.729   1.422  0.63 27.54           N
ANISOU  820  N  AILE A  79     3514   3108   3840    470    425     30       N
ATOM    821  CA AILE A  79     -21.087   2.351   1.926  0.63 26.48           C
ANISOU  821  CA AILE A  79     3430   2964   3668    343    486     15       C
ATOM    822  C  AILE A  79     -21.255   1.976   3.393  0.63 27.47           C
ANISOU  822  C  AILE A  79     3490   3145   3802    302    538   -102       C
ATOM    823  O  AILE A  79     -21.509   2.843   4.233  0.63 27.29           O
ANISOU  823  O  AILE A  79     3468   3061   3841    343    570   -177       O
ATOM    824  CB AILE A  79     -20.081   3.493   1.753  0.63 27.63           C
ANISOU  824  CB AILE A  79     3686   2955   3856    319    511     61       C
ATOM    825  CG1AILE A  79     -19.882   3.759   0.266  0.63 28.46           C
ANISOU  825  CG1AILE A  79     3870   3025   3920    336    471    197       C
ATOM    826  CG2AILE A  79     -18.751   3.154   2.409  0.63 27.25           C
ANISOU  826  CG2AILE A  79     3656   2909   3790    192    566     24       C
ATOM    827  CD1AILE A  79     -19.185   5.016   0.025  0.63 29.55           C
ANISOU  827  CD1AILE A  79     4120   2996   4111    317    490    262       C
ATOM    828  H  AILE A  79     -22.471   3.564   1.231  0.63 33.05           H
ATOM    829  N  BILE A  79     -22.402   2.735   1.420  0.37 27.86           N
ANISOU  829  N  BILE A  79     3555   3148   3881    470    425     30       N
ATOM    830  CA BILE A  79     -21.084   2.371   1.930  0.37 26.78           C
ANISOU  830  CA BILE A  79     3468   3000   3707    344    487     15       C
ATOM    831  C  BILE A  79     -21.263   1.977   3.393  0.37 27.50           C
ANISOU  831  C  BILE A  79     3493   3149   3805    303    538   -102       C
ATOM    832  O  BILE A  79     -21.538   2.833   4.238  0.37 27.79           O
ANISOU  832  O  BILE A  79     3528   3127   3904    345    570   -178       O
ATOM    833  CB BILE A  79     -20.088   3.530   1.789  0.37 28.32           C
ANISOU  833  CB BILE A  79     3773   3039   3947    320    512     59       C
ATOM    834  CG1BILE A  79     -19.992   4.017   0.334  0.37 28.47           C
ANISOU  834  CG1BILE A  79     3878   2999   3941    353    468    195       C
ATOM    835  CG2BILE A  79     -18.717   3.119   2.318  0.37 27.29           C
ANISOU  835  CG2BILE A  79     3663   2916   3790    190    565     31       C
ATOM    836  CD1BILE A  79     -19.564   2.973  -0.653  0.37 28.61           C
ANISOU  836  CD1BILE A  79     3898   3128   3844    295    460    257       C
ATOM    837  H  BILE A  79     -22.476   3.569   1.225  0.37 33.43           H
ATOM    838  N   THR A  80     -21.102   0.691   3.696  1.00 24.57           N
ANISOU  838  N   THR A  80     3081   2888   3366    221    543   -118       N
ATOM    839  CA  THR A  80     -21.403   0.133   5.018  1.00 24.10           C
ANISOU  839  CA  THR A  80     2968   2905   3282    169    585   -205       C
ATOM    840  C   THR A  80     -20.114  -0.294   5.714  1.00 23.19           C
ANISOU  840  C   THR A  80     2909   2776   3125     63    601   -217       C
ATOM    841  O   THR A  80     -19.395  -1.155   5.222  1.00 23.04           O
ANISOU  841  O   THR A  80     2908   2776   3070     11    571   -169       O
ATOM    842  CB  THR A  80     -22.374  -1.046   4.857  1.00 24.87           C
ANISOU  842  CB  THR A  80     2979   3130   3342    151    562   -200       C
ATOM    843  OG1 THR A  80     -23.578  -0.604   4.202  1.00 25.83           O
ANISOU  843  OG1 THR A  80     3026   3274   3513    255    531   -197       O
ATOM    844  CG2 THR A  80     -22.720  -1.648   6.203  1.00 24.44           C
ANISOU  844  CG2 THR A  80     2881   3159   3245     76    615   -268       C
ATOM    845  H   THR A  80     -20.816   0.100   3.141  1.00 29.49           H
ATOM    846  HG1 THR A  80     -23.399  -0.324   3.431  1.00 31.00           H
ATOM    847  N   PHE A  81     -19.842   0.268   6.908  1.00 25.09           N
ANISOU  847  N   PHE A  81     3173   2989   3370     38    640   -295       N
ATOM    848  CA  PHE A  81     -18.708  -0.150   7.724  1.00 25.50           C
ANISOU  848  CA  PHE A  81     3268   3043   3377    -58    634   -316       C
ATOM    849  C   PHE A  81     -19.183  -1.196   8.727  1.00 25.09           C
ANISOU  849  C   PHE A  81     3192   3102   3240   -118    641   -344       C
ATOM    850  O   PHE A  81     -20.217  -0.999   9.369  1.00 24.69           O
ANISOU  850  O   PHE A  81     3102   3110   3169    -99    693   -402       O
ATOM    851  CB  PHE A  81     -18.148   1.045   8.532  1.00 22.96           C
ANISOU  851  CB  PHE A  81     2999   2634   3091    -65    658   -394       C
ATOM    852  CG  PHE A  81     -17.028   0.640   9.468  1.00 26.45           C
ANISOU  852  CG  PHE A  81     3475   3091   3482   -162    631   -425       C
ATOM    853  CD1 PHE A  81     -15.726   0.546   9.012  1.00 24.43           C
ANISOU  853  CD1 PHE A  81     3234   2789   3259   -210    591   -385       C
ATOM    854  CD2 PHE A  81     -17.294   0.339  10.785  1.00 28.01           C
ANISOU  854  CD2 PHE A  81     3687   3363   3594   -205    643   -496       C
ATOM    855  CE1 PHE A  81     -14.702   0.152   9.835  1.00 27.28           C
ANISOU  855  CE1 PHE A  81     3609   3170   3587   -286    544   -415       C
ATOM    856  CE2 PHE A  81     -16.264  -0.044  11.653  1.00 29.57           C
ANISOU  856  CE2 PHE A  81     3925   3577   3734   -289    592   -516       C
ATOM    857  CZ  PHE A  81     -14.973  -0.121  11.187  1.00 28.61           C
ANISOU  857  CZ  PHE A  81     3805   3402   3665   -322    534   -479       C
ATOM    858  H   PHE A  81     -20.309   0.898   7.261  1.00 30.11           H
ATOM    859  N   ILE A  82     -18.437  -2.279   8.861  1.00 22.76           N
ANISOU  859  N   ILE A  82     2918   2832   2896   -191    594   -303       N
ATOM    860  CA  ILE A  82     -18.843  -3.404   9.716  1.00 22.55           C
ANISOU  860  CA  ILE A  82     2892   2892   2783   -263    586   -297       C
ATOM    861  C   ILE A  82     -17.721  -3.719  10.697  1.00 24.20           C
ANISOU  861  C   ILE A  82     3167   3090   2937   -334    539   -306       C
ATOM    862  O   ILE A  82     -16.560  -3.866  10.290  1.00 24.64           O
ANISOU  862  O   ILE A  82     3238   3090   3032   -335    480   -282       O
ATOM    863  CB  ILE A  82     -19.194  -4.654   8.866  1.00 24.07           C
ANISOU  863  CB  ILE A  82     3056   3114   2976   -277    543   -226       C
ATOM    864  CG1 ILE A  82     -20.385  -4.359   7.930  1.00 22.50           C
ANISOU  864  CG1 ILE A  82     2783   2944   2823   -210    569   -222       C
ATOM    865  CG2 ILE A  82     -19.433  -5.866   9.804  1.00 24.89           C
ANISOU  865  CG2 ILE A  82     3186   3275   2996   -375    523   -200       C
ATOM    866  CD1 ILE A  82     -20.570  -5.369   6.701  1.00 25.00           C
ANISOU  866  CD1 ILE A  82     3077   3268   3153   -207    509   -165       C
ATOM    867  H   ILE A  82     -17.682  -2.395   8.466  1.00 27.31           H
ATOM    868  N   LEU A  83     -18.053  -3.746  11.996  1.00 23.00           N
ANISOU  868  N   LEU A  83     3049   2999   2690   -389    566   -348       N
ATOM    869  CA  LEU A  83     -17.171  -4.314  13.003  1.00 25.59           C
ANISOU  869  CA  LEU A  83     3450   3337   2934   -465    497   -337       C
ATOM    870  C   LEU A  83     -17.702  -5.712  13.270  1.00 22.08           C
ANISOU  870  C   LEU A  83     3027   2949   2414   -533    472   -257       C
ATOM    871  O   LEU A  83     -18.835  -5.855  13.711  1.00 25.03           O
ANISOU  871  O   LEU A  83     3384   3404   2723   -572    549   -264       O
ATOM    872  CB  LEU A  83     -17.189  -3.485  14.289  1.00 26.50           C
ANISOU  872  CB  LEU A  83     3616   3491   2963   -496    536   -430       C
ATOM    873  CG  LEU A  83     -16.541  -4.259  15.412  1.00 27.00           C
ANISOU  873  CG  LEU A  83     3766   3593   2899   -584    454   -400       C
ATOM    874  CD1 LEU A  83     -15.092  -4.644  15.044  1.00 26.35           C
ANISOU  874  CD1 LEU A  83     3692   3433   2886   -575    322   -357       C
ATOM    875  CD2 LEU A  83     -16.686  -3.455  16.744  1.00 32.17           C
ANISOU  875  CD2 LEU A  83     4482   4309   3430   -623    501   -507       C
ATOM    876  H   LEU A  83     -18.790  -3.437  12.311  1.00 27.60           H
ATOM    877  N   TRP A  84     -16.944  -6.732  12.864  1.00 21.68           N
ANISOU  877  N   TRP A  84     3000   2847   2391   -543    370   -185       N
ATOM    878  CA  TRP A  84     -17.247  -8.123  13.154  1.00 23.62           C
ANISOU  878  CA  TRP A  84     3292   3104   2578   -615    318   -100       C
ATOM    879  C   TRP A  84     -16.470  -8.452  14.419  1.00 23.71           C
ANISOU  879  C   TRP A  84     3404   3118   2484   -676    235    -76       C
ATOM    880  O   TRP A  84     -15.232  -8.451  14.411  1.00 23.54           O
ANISOU  880  O   TRP A  84     3398   3040   2507   -640    134    -81       O
ATOM    881  CB  TRP A  84     -16.835  -9.026  11.984  1.00 23.54           C
ANISOU  881  CB  TRP A  84     3259   3017   2667   -572    242    -52       C
ATOM    882  CG  TRP A  84     -16.793 -10.492  12.346  1.00 22.01           C
ANISOU  882  CG  TRP A  84     3141   2786   2435   -638    150     34       C
ATOM    883  CD1 TRP A  84     -15.685 -11.287  12.379  1.00 22.06           C
ANISOU  883  CD1 TRP A  84     3198   2709   2476   -615     19     69       C
ATOM    884  CD2 TRP A  84     -17.902 -11.333  12.680  1.00 22.46           C
ANISOU  884  CD2 TRP A  84     3230   2875   2430   -738    176     96       C
ATOM    885  NE1 TRP A  84     -16.035 -12.560  12.725  1.00 24.62           N
ANISOU  885  NE1 TRP A  84     3603   2991   2763   -687    -48    156       N
ATOM    886  CE2 TRP A  84     -17.390 -12.616  12.934  1.00 24.82           C
ANISOU  886  CE2 TRP A  84     3622   3086   2724   -778     51    179       C
ATOM    887  CE3 TRP A  84     -19.274 -11.119  12.818  1.00 23.84           C
ANISOU  887  CE3 TRP A  84     3354   3143   2562   -799    292     87       C
ATOM    888  CZ2 TRP A  84     -18.201 -13.684  13.292  1.00 24.39           C
ANISOU  888  CZ2 TRP A  84     3630   3019   2617   -894     40    266       C
ATOM    889  CZ3 TRP A  84     -20.078 -12.173  13.176  1.00 24.89           C
ANISOU  889  CZ3 TRP A  84     3525   3290   2643   -920    294    163       C
ATOM    890  CH2 TRP A  84     -19.542 -13.453  13.408  1.00 27.34           C
ANISOU  890  CH2 TRP A  84     3948   3497   2945   -977    169    259       C
ATOM    891  H   TRP A  84     -16.225  -6.634  12.402  1.00 26.02           H
ATOM    892  HE1 TRP A  84     -15.492 -13.222  12.800  1.00 29.55           H
ATOM    893  N   ALA A  85     -17.187  -8.681  15.507  1.00 24.40           N
ANISOU  893  N   ALA A  85     3555   3286   2429   -770    279    -54       N
ATOM    894  CA  ALA A  85     -16.580  -8.859  16.828  1.00 24.94           C
ANISOU  894  CA  ALA A  85     3740   3380   2357   -837    206    -31       C
ATOM    895  C   ALA A  85     -17.331  -9.959  17.569  1.00 28.75           C
ANISOU  895  C   ALA A  85     4313   3909   2702   -962    211     77       C
ATOM    896  O   ALA A  85     -18.103  -9.702  18.494  1.00 28.99           O
ANISOU  896  O   ALA A  85     4379   4052   2582  -1048    314     60       O
ATOM    897  CB  ALA A  85     -16.592  -7.539  17.609  1.00 28.00           C
ANISOU  897  CB  ALA A  85     4131   3840   2668   -834    282   -150       C
ATOM    898  H   ALA A  85     -18.045  -8.740  15.511  1.00 29.28           H
ATOM    899  N   PRO A  86     -17.133 -11.205  17.169  1.00 29.06           N
ANISOU  899  N   PRO A  86     4393   3859   2790   -981    107    186       N
ATOM    900  CA  PRO A  86     -17.933 -12.291  17.727  1.00 27.89           C
ANISOU  900  CA  PRO A  86     4333   3730   2535  -1117    117    303       C
ATOM    901  C   PRO A  86     -17.616 -12.493  19.194  1.00 30.95           C
ANISOU  901  C   PRO A  86     4877   4167   2717  -1215     63    368       C
ATOM    902  O   PRO A  86     -16.471 -12.329  19.618  1.00 29.83           O
ANISOU  902  O   PRO A  86     4794   3985   2555  -1162    -70    362       O
ATOM    903  CB  PRO A  86     -17.510 -13.507  16.897  1.00 31.56           C
ANISOU  903  CB  PRO A  86     4820   4044   3129  -1088    -18    388       C
ATOM    904  CG  PRO A  86     -16.144 -13.168  16.368  1.00 28.89           C
ANISOU  904  CG  PRO A  86     4444   3624   2910   -944   -133    329       C
ATOM    905  CD  PRO A  86     -16.164 -11.669  16.156  1.00 28.26           C
ANISOU  905  CD  PRO A  86     4257   3629   2852   -879    -18    197       C
ATOM    906  N   ASP A  87     -18.638 -12.899  19.953  1.00 33.09           N
ANISOU  906  N   ASP A  87     5210   4532   2831  -1365    164    436       N
ATOM    907  CA  ASP A  87     -18.437 -13.065  21.382  1.00 35.01           C
ANISOU  907  CA  ASP A  87     5619   4846   2839  -1475    130    505       C
ATOM    908  C   ASP A  87     -17.328 -14.077  21.654  1.00 37.25           C
ANISOU  908  C   ASP A  87     6053   4985   3116  -1467   -110    642       C
ATOM    909  O   ASP A  87     -16.637 -13.989  22.671  1.00 36.40           O
ANISOU  909  O   ASP A  87     6072   4905   2852  -1489   -214    673       O
ATOM    910  CB  ASP A  87     -19.745 -13.524  22.054  1.00 36.59           C
ANISOU  910  CB  ASP A  87     5864   5168   2872  -1662    288    579       C
ATOM    911  CG  ASP A  87     -20.803 -12.420  22.071  1.00 42.25           C
ANISOU  911  CG  ASP A  87     6431   6058   3565  -1661    524    421       C
ATOM    912  OD1 ASP A  87     -20.439 -11.229  21.968  1.00 44.83           O
ANISOU  912  OD1 ASP A  87     6683   6416   3935  -1536    553    267       O
ATOM    913  OD2 ASP A  87     -22.000 -12.737  22.226  1.00 47.89           O
ANISOU  913  OD2 ASP A  87     7091   6869   4237  -1775    673    444       O
ATOM    914  H   ASP A  87     -19.430 -13.077  19.670  1.00 39.71           H
ATOM    915  N  ASER A  88     -17.127 -15.014  20.722  0.48 36.84           N
ANISOU  915  N  ASER A  88     5983   4775   3241  -1422   -211    711       N
ATOM    916  CA ASER A  88     -16.151 -16.086  20.861  0.48 38.37           C
ANISOU  916  CA ASER A  88     6306   4805   3468  -1393   -445    837       C
ATOM    917  C  ASER A  88     -14.710 -15.627  20.695  0.48 36.13           C
ANISOU  917  C  ASER A  88     5978   4466   3282  -1227   -603    758       C
ATOM    918  O  ASER A  88     -13.805 -16.380  21.056  0.48 38.72           O
ANISOU  918  O  ASER A  88     6412   4683   3615  -1191   -814    851       O
ATOM    919  CB ASER A  88     -16.473 -17.186  19.844  0.48 38.64           C
ANISOU  919  CB ASER A  88     6321   4685   3675  -1388   -485    902       C
ATOM    920  OG ASER A  88     -17.881 -17.324  19.696  0.48 38.15           O
ANISOU  920  OG ASER A  88     6221   4699   3577  -1527   -305    920       O
ATOM    921  H  ASER A  88     -17.558 -15.048  19.979  0.48 44.22           H
ATOM    922  HG ASER A  88     -18.056 -18.010  19.243  0.48 45.79           H
ATOM    923  N  BSER A  88     -17.120 -15.030  20.751  0.52 36.88           N
ANISOU  923  N  BSER A  88     5992   4780   3241  -1424   -214    715       N
ATOM    924  CA BSER A  88     -16.129 -16.068  21.003  0.52 38.37           C
ANISOU  924  CA BSER A  88     6321   4814   3444  -1401   -449    843       C
ATOM    925  C  BSER A  88     -14.696 -15.626  20.719  0.52 36.18           C
ANISOU  925  C  BSER A  88     5987   4473   3286  -1228   -606    759       C
ATOM    926  O  BSER A  88     -13.775 -16.393  21.004  0.52 38.68           O
ANISOU  926  O  BSER A  88     6403   4673   3621  -1184   -818    848       O
ATOM    927  CB BSER A  88     -16.462 -17.311  20.173  0.52 39.06           C
ANISOU  927  CB BSER A  88     6422   4741   3677  -1420   -504    937       C
ATOM    928  OG BSER A  88     -16.378 -17.019  18.798  0.52 37.11           O
ANISOU  928  OG BSER A  88     6002   4448   3649  -1287   -466    815       O
ATOM    929  H  BSER A  88     -17.533 -15.097  20.000  0.52 44.26           H
ATOM    930  HG BSER A  88     -16.697 -17.653  18.349  0.52 44.53           H
ATOM    931  N   ALA A  89     -14.472 -14.427  20.176  1.00 35.07           N
ANISOU  931  N   ALA A  89     5691   4401   3235  -1130   -514    595       N
ATOM    932  CA  ALA A  89     -13.105 -13.943  20.011  1.00 34.81           C
ANISOU  932  CA  ALA A  89     5596   4327   3303   -996   -649    515       C
ATOM    933  C   ALA A  89     -12.464 -13.693  21.388  1.00 36.47           C
ANISOU  933  C   ALA A  89     5929   4601   3325  -1040   -768    539       C
ATOM    934  O   ALA A  89     -13.159 -13.415  22.375  1.00 36.83           O
ANISOU  934  O   ALA A  89     6076   4765   3151  -1162   -680    560       O
ATOM    935  CB  ALA A  89     -13.066 -12.663  19.186  1.00 30.56           C
ANISOU  935  CB  ALA A  89     4882   3843   2886   -913   -514    349       C
ATOM    936  H   ALA A  89     -15.080 -13.879  19.913  1.00 42.09           H
ATOM    937  N   PRO A  90     -11.138 -13.809  21.484  1.00 33.85           N
ANISOU  937  N   PRO A  90     5587   4204   3070   -942   -972    530       N
ATOM    938  CA  PRO A  90     -10.466 -13.570  22.773  1.00 36.56           C
ANISOU  938  CA  PRO A  90     6045   4612   3235   -978  -1117    546       C
ATOM    939  C   PRO A  90     -10.614 -12.114  23.183  1.00 37.49           C
ANISOU  939  C   PRO A  90     6110   4875   3261  -1011   -982    389       C
ATOM    940  O   PRO A  90     -10.665 -11.216  22.350  1.00 36.82           O
ANISOU  940  O   PRO A  90     5868   4800   3324   -952   -853    255       O
ATOM    941  CB  PRO A  90      -9.007 -13.910  22.479  1.00 37.01           C
ANISOU  941  CB  PRO A  90     6032   4566   3466   -838  -1352    534       C
ATOM    942  CG  PRO A  90      -9.069 -14.852  21.341  1.00 37.23           C
ANISOU  942  CG  PRO A  90     5997   4451   3697   -758  -1360    581       C
ATOM    943  CD  PRO A  90     -10.218 -14.368  20.481  1.00 37.58           C
ANISOU  943  CD  PRO A  90     5956   4540   3783   -800  -1098    517       C
ATOM    944  N   ILE A  91     -10.651 -11.867  24.495  1.00 34.56           N
ANISOU  944  N   ILE A  91     5885   4610   2639  -1105  -1024    403       N
ATOM    945  CA  ILE A  91     -10.934 -10.506  24.963  1.00 39.60           C
ANISOU  945  CA  ILE A  91     6494   5382   3172  -1144   -882    238       C
ATOM    946  C   ILE A  91      -9.884  -9.524  24.450  1.00 34.01           C
ANISOU  946  C   ILE A  91     5627   4641   2652  -1040   -940     79       C
ATOM    947  O   ILE A  91     -10.196  -8.396  24.088  1.00 34.78           O
ANISOU  947  O   ILE A  91     5627   4774   2812  -1027   -780    -68       O
ATOM    948  CB  ILE A  91     -11.061 -10.490  26.500  1.00 39.68           C
ANISOU  948  CB  ILE A  91     6705   5518   2854  -1264   -934    274       C
ATOM    949  CG1 ILE A  91     -11.182  -9.054  27.058  1.00 45.34           C
ANISOU  949  CG1 ILE A  91     7401   6363   3464  -1289   -818     70       C
ATOM    950  CG2 ILE A  91      -9.920 -11.219  27.160  1.00 45.45           C
ANISOU  950  CG2 ILE A  91     7547   6199   3523  -1243  -1235    384       C
ATOM    951  CD1 ILE A  91     -12.376  -8.309  26.516  1.00 46.34           C
ANISOU  951  CD1 ILE A  91     7426   6539   3642  -1297   -530    -41       C
ATOM    952  H   ILE A  91     -10.520 -12.449  25.115  1.00 41.48           H
ATOM    953  N   LYS A  92      -8.629  -9.957  24.397  1.00 36.56           N
ANISOU  953  N   LYS A  92     5919   4891   3081   -966  -1171    110       N
ATOM    954  CA  LYS A  92      -7.540  -9.162  23.835  1.00 38.40           C
ANISOU  954  CA  LYS A  92     5979   5093   3519   -880  -1232    -26       C
ATOM    955  C   LYS A  92      -7.911  -8.650  22.440  1.00 37.38           C
ANISOU  955  C   LYS A  92     5681   4911   3610   -822  -1036   -100       C
ATOM    956  O   LYS A  92      -7.680  -7.484  22.077  1.00 35.67           O
ANISOU  956  O   LYS A  92     5357   4706   3489   -811   -949   -240       O
ATOM    957  CB  LYS A  92      -6.348 -10.080  23.662  1.00 45.68           C
ANISOU  957  CB  LYS A  92     6855   5928   4573   -787  -1481     48       C
ATOM    958  CG  LYS A  92      -5.046  -9.558  23.975  1.00 54.77           C
ANISOU  958  CG  LYS A  92     7915   7099   5795   -748  -1660    -49       C
ATOM    959  CD  LYS A  92      -5.224  -8.732  25.185  1.00 68.98           C
ANISOU  959  CD  LYS A  92     9837   9016   7357   -854  -1666   -122       C
ATOM    960  CE  LYS A  92      -3.840  -8.383  25.611  1.00 85.26           C
ANISOU  960  CE  LYS A  92    11817  11097   9481   -823  -1899   -206       C
ATOM    961  NZ  LYS A  92      -3.604  -7.168  26.366  1.00 61.25           N
ANISOU  961  NZ  LYS A  92     8793   8148   6333   -903  -1903   -365       N
ATOM    962  H   LYS A  92      -8.373 -10.725  24.686  1.00 43.88           H
ATOM    963  HZ1 LYS A  92      -2.742  -7.102  26.575  1.00 73.51           H
ATOM    964  HZ2 LYS A  92      -3.839  -6.459  25.882  1.00 73.51           H
ATOM    965  HZ3 LYS A  92      -4.083  -7.178  27.116  1.00 73.51           H
ATOM    966  N   SER A  93      -8.429  -9.558  21.611  1.00 36.44           N
ANISOU  966  N   SER A  93     5545   4722   3579   -786   -983      0       N
ATOM    967  CA  SER A  93      -8.717  -9.223  20.222  1.00 31.73           C
ANISOU  967  CA  SER A  93     4801   4076   3180   -724   -828    -53       C
ATOM    968  C   SER A  93      -9.878  -8.242  20.126  1.00 31.68           C
ANISOU  968  C   SER A  93     4791   4132   3113   -775   -601   -127       C
ATOM    969  O   SER A  93      -9.790  -7.251  19.399  1.00 31.35           O
ANISOU  969  O   SER A  93     4637   4076   3197   -738   -500   -229       O
ATOM    970  CB  SER A  93      -9.016 -10.481  19.409  1.00 36.27           C
ANISOU  970  CB  SER A  93     5373   4563   3847   -678   -842     59       C
ATOM    971  OG  SER A  93      -9.770 -10.100  18.266  1.00 38.88           O
ANISOU  971  OG  SER A  93     5608   4883   4280   -655   -654     16       O
ATOM    972  H   SER A  93      -8.620 -10.368  21.828  1.00 43.73           H
ATOM    973  HG  SER A  93     -10.100 -10.781  17.900  1.00 46.65           H
ATOM    974  N   LYS A  94     -10.977  -8.507  20.848  1.00 30.42           N
ANISOU  974  N   LYS A  94     4753   4042   2765   -860   -519    -74       N
ATOM    975  CA  LYS A  94     -12.090  -7.561  20.890  1.00 30.69           C
ANISOU  975  CA  LYS A  94     4771   4149   2739   -895   -310   -163       C
ATOM    976  C   LYS A  94     -11.626  -6.192  21.345  1.00 32.38           C
ANISOU  976  C   LYS A  94     4965   4397   2940   -893   -294   -321       C
ATOM    977  O   LYS A  94     -12.013  -5.181  20.761  1.00 30.77           O
ANISOU  977  O   LYS A  94     4678   4177   2835   -856   -159   -423       O
ATOM    978  CB  LYS A  94     -13.246  -8.068  21.764  1.00 33.25           C
ANISOU  978  CB  LYS A  94     5219   4570   2845  -1001   -223    -95       C
ATOM    979  CG  LYS A  94     -13.485  -9.579  21.672  1.00 39.14           C
ANISOU  979  CG  LYS A  94     6036   5267   3567  -1041   -297     84       C
ATOM    980  CD  LYS A  94     -14.884  -9.984  22.165  1.00 42.55           C
ANISOU  980  CD  LYS A  94     6538   5794   3834  -1160   -144    147       C
ATOM    981  CE  LYS A  94     -14.762 -11.028  23.262  1.00 44.77           C
ANISOU  981  CE  LYS A  94     7009   6092   3909  -1271   -265    301       C
ATOM    982  NZ  LYS A  94     -16.063 -11.540  23.764  1.00 42.70           N
ANISOU  982  NZ  LYS A  94     6819   5924   3479  -1417   -114    384       N
ATOM    983  H   LYS A  94     -11.097  -9.219  21.315  1.00 36.51           H
ATOM    984  HZ1 LYS A  94     -15.927 -12.135  24.412  1.00 51.24           H
ATOM    985  HZ2 LYS A  94     -16.551 -10.869  24.086  1.00 51.24           H
ATOM    986  HZ3 LYS A  94     -16.512 -11.932  23.103  1.00 51.24           H
ATOM    987  N   MET A  95     -10.840  -6.149  22.429  1.00 30.67           N
ANISOU  987  N   MET A  95     4838   4221   2595   -936   -441   -341       N
ATOM    988  CA  MET A  95     -10.234  -4.920  22.922  1.00 33.63           C
ANISOU  988  CA  MET A  95     5201   4616   2962   -945   -465   -499       C
ATOM    989  C   MET A  95      -9.486  -4.161  21.816  1.00 31.81           C
ANISOU  989  C   MET A  95     4811   4285   2990   -875   -459   -576       C
ATOM    990  O   MET A  95      -9.645  -2.947  21.671  1.00 33.54           O
ANISOU  990  O   MET A  95     4993   4485   3267   -873   -357   -706       O
ATOM    991  CB  MET A  95      -9.295  -5.374  24.049  1.00 36.97           C
ANISOU  991  CB  MET A  95     5729   5083   3236   -990   -688   -467       C
ATOM    992  CG  MET A  95     -10.026  -5.885  25.255  1.00 39.74           C
ANISOU  992  CG  MET A  95     6263   5546   3289  -1083   -678   -403       C
ATOM    993  SD  MET A  95      -9.437  -5.129  26.777  1.00 38.81           S
ANISOU  993  SD  MET A  95     6278   5538   2932  -1159   -799   -532       S
ATOM    994  CE  MET A  95     -10.566  -5.737  27.996  1.00 39.99           C
ANISOU  994  CE  MET A  95     6641   5839   2713  -1278   -712   -446       C
ATOM    995  H   MET A  95     -10.641  -6.837  22.905  1.00 36.81           H
ATOM    996  N   MET A  96      -8.607  -4.857  21.078  1.00 30.15           N
ANISOU  996  N   MET A  96     4511   4009   2936   -820   -573   -500       N
ATOM    997  CA  MET A  96      -7.809  -4.219  20.036  1.00 30.44           C
ANISOU  997  CA  MET A  96     4393   3970   3203   -772   -562   -562       C
ATOM    998  C   MET A  96      -8.718  -3.602  18.972  1.00 28.97           C
ANISOU  998  C   MET A  96     4151   3741   3116   -739   -356   -582       C
ATOM    999  O   MET A  96      -8.570  -2.433  18.598  1.00 32.83           O
ANISOU  999  O   MET A  96     4586   4185   3703   -742   -282   -678       O
ATOM   1000  CB  MET A  96      -6.895  -5.286  19.399  1.00 34.57           C
ANISOU 1000  CB  MET A  96     4827   4450   3857   -708   -693   -475       C
ATOM   1001  CG  MET A  96      -5.638  -4.825  18.705  1.00 41.84           C
ANISOU 1001  CG  MET A  96     5584   5332   4982   -678   -746   -542       C
ATOM   1002  SD  MET A  96      -4.436  -6.178  18.767  1.00 52.25           S
ANISOU 1002  SD  MET A  96     6837   6642   6374   -606   -980   -470       S
ATOM   1003  CE  MET A  96      -5.525  -7.609  18.776  1.00 45.25           C
ANISOU 1003  CE  MET A  96     6091   5731   5372   -573   -971   -313       C
ATOM   1004  H   MET A  96      -8.458  -5.699  21.164  1.00 36.18           H
ATOM   1005  N   TYR A  97      -9.710  -4.362  18.520  1.00 29.14           N
ANISOU 1005  N   TYR A  97     4194   3769   3108   -714   -272   -489       N
ATOM   1006  CA  TYR A  97     -10.518  -3.906  17.388  1.00 26.87           C
ANISOU 1006  CA  TYR A  97     3841   3442   2925   -669   -110   -494       C
ATOM   1007  C   TYR A  97     -11.529  -2.851  17.802  1.00 28.87           C
ANISOU 1007  C   TYR A  97     4136   3723   3109   -685     28   -585       C
ATOM   1008  O   TYR A  97     -11.793  -1.922  17.035  1.00 28.68           O
ANISOU 1008  O   TYR A  97     4056   3640   3200   -645    126   -635       O
ATOM   1009  CB  TYR A  97     -11.237  -5.077  16.714  1.00 26.81           C
ANISOU 1009  CB  TYR A  97     3829   3435   2922   -639    -80   -378       C
ATOM   1010  CG  TYR A  97     -10.360  -5.894  15.811  1.00 24.65           C
ANISOU 1010  CG  TYR A  97     3481   3105   2780   -586   -167   -320       C
ATOM   1011  CD1 TYR A  97      -9.530  -6.889  16.331  1.00 27.44           C
ANISOU 1011  CD1 TYR A  97     3862   3452   3111   -584   -334   -267       C
ATOM   1012  CD2 TYR A  97     -10.366  -5.688  14.429  1.00 22.82           C
ANISOU 1012  CD2 TYR A  97     3154   2829   2689   -529    -88   -321       C
ATOM   1013  CE1 TYR A  97      -8.732  -7.676  15.480  1.00 25.72           C
ANISOU 1013  CE1 TYR A  97     3563   3180   3029   -514   -410   -234       C
ATOM   1014  CE2 TYR A  97      -9.590  -6.450  13.597  1.00 24.56           C
ANISOU 1014  CE2 TYR A  97     3303   3012   3015   -476   -149   -288       C
ATOM   1015  CZ  TYR A  97      -8.762  -7.406  14.108  1.00 26.92           C
ANISOU 1015  CZ  TYR A  97     3613   3302   3313   -463   -304   -256       C
ATOM   1016  OH  TYR A  97      -8.001  -8.168  13.237  1.00 26.23           O
ANISOU 1016  OH  TYR A  97     3442   3177   3348   -391   -358   -245       O
ATOM   1017  H   TYR A  97      -9.933  -5.128  18.841  1.00 34.97           H
ATOM   1018  HH  TYR A  97      -7.661  -8.818  13.647  1.00 31.48           H
ATOM   1019  N  ATHR A  98     -12.064  -2.937  19.025  0.36 30.09           N
ANISOU 1019  N  ATHR A  98     4393   3963   3076   -741     35   -613       N
ATOM   1020  CA ATHR A  98     -13.002  -1.910  19.451  0.36 30.45           C
ANISOU 1020  CA ATHR A  98     4466   4042   3063   -742    173   -728       C
ATOM   1021  C  ATHR A  98     -12.280  -0.600  19.756  0.36 32.36           C
ANISOU 1021  C  ATHR A  98     4712   4224   3359   -748    148   -873       C
ATOM   1022  O  ATHR A  98     -12.804   0.481  19.461  0.36 32.69           O
ANISOU 1022  O  ATHR A  98     4732   4212   3476   -707    257   -969       O
ATOM   1023  CB ATHR A  98     -13.823  -2.384  20.657  0.36 31.94           C
ANISOU 1023  CB ATHR A  98     4758   4360   3017   -809    215   -727       C
ATOM   1024  OG1ATHR A  98     -14.877  -3.261  20.209  0.36 31.56           O
ANISOU 1024  OG1ATHR A  98     4683   4353   2955   -807    302   -621       O
ATOM   1025  CG2ATHR A  98     -14.445  -1.188  21.321  0.36 32.26           C
ANISOU 1025  CG2ATHR A  98     4828   4440   2989   -806    334   -895       C
ATOM   1026  H  ATHR A  98     -11.905  -3.557  19.599  0.36 36.11           H
ATOM   1027  HG1ATHR A  98     -15.252  -3.620  20.869  0.36 37.87           H
ATOM   1028  N  BTHR A  98     -12.087  -2.950  19.014  0.64 30.18           N
ANISOU 1028  N  BTHR A  98     4404   3975   3087   -741     37   -611       N
ATOM   1029  CA BTHR A  98     -12.993  -1.899  19.456  0.64 30.56           C
ANISOU 1029  CA BTHR A  98     4479   4054   3076   -742    173   -730       C
ATOM   1030  C  BTHR A  98     -12.234  -0.596  19.671  0.64 32.37           C
ANISOU 1030  C  BTHR A  98     4707   4219   3375   -745    146   -869       C
ATOM   1031  O  BTHR A  98     -12.676   0.475  19.230  0.64 32.80           O
ANISOU 1031  O  BTHR A  98     4729   4207   3526   -700    249   -955       O
ATOM   1032  CB BTHR A  98     -13.711  -2.326  20.739  0.64 31.94           C
ANISOU 1032  CB BTHR A  98     4764   4359   3013   -812    203   -736       C
ATOM   1033  OG1BTHR A  98     -12.730  -2.562  21.752  0.64 31.46           O
ANISOU 1033  OG1BTHR A  98     4793   4332   2827   -875     48   -742       O
ATOM   1034  CG2BTHR A  98     -14.495  -3.611  20.479  0.64 31.85           C
ANISOU 1034  CG2BTHR A  98     4755   4396   2952   -833    236   -589       C
ATOM   1035  H  BTHR A  98     -11.961  -3.591  19.573  0.64 36.22           H
ATOM   1036  HG1BTHR A  98     -13.076  -2.978  22.395  0.64 37.75           H
ATOM   1037  N   SER A  99     -11.079  -0.652  20.347  1.00 30.99           N
ANISOU 1037  N   SER A  99     4564   4051   3160   -797     -6   -895       N
ATOM   1038  CA  SER A  99     -10.398   0.608  20.647  1.00 28.94           C
ANISOU 1038  CA  SER A  99     4305   3729   2960   -822    -36  -1044       C
ATOM   1039  C   SER A  99      -9.777   1.243  19.406  1.00 31.19           C
ANISOU 1039  C   SER A  99     4479   3885   3488   -792    -20  -1039       C
ATOM   1040  O   SER A  99      -9.548   2.454  19.404  1.00 34.24           O
ANISOU 1040  O   SER A  99     4867   4186   3958   -809      7  -1155       O
ATOM   1041  CB  SER A  99      -9.338   0.449  21.751  1.00 36.94           C
ANISOU 1041  CB  SER A  99     5376   4797   3863   -896   -216  -1089       C
ATOM   1042  OG  SER A  99      -8.364  -0.527  21.419  1.00 38.03           O
ANISOU 1042  OG  SER A  99     5450   4935   4066   -891   -364   -973       O
ATOM   1043  H   SER A  99     -10.695  -1.369  20.625  1.00 37.19           H
ATOM   1044  HG  SER A  99      -7.900  -0.261  20.771  1.00 45.64           H
ATOM   1045  N   THR A 100      -9.554   0.477  18.338  1.00 29.54           N
ANISOU 1045  N   THR A 100     4184   3656   3385   -752    -25   -911       N
ATOM   1046  CA  THR A 100      -9.039   1.037  17.089  1.00 30.85           C
ANISOU 1046  CA  THR A 100     4250   3718   3753   -732     15   -893       C
ATOM   1047  C   THR A 100     -10.145   1.390  16.104  1.00 32.22           C
ANISOU 1047  C   THR A 100     4415   3841   3987   -663    165   -854       C
ATOM   1048  O   THR A 100      -9.852   1.957  15.043  1.00 29.59           O
ANISOU 1048  O   THR A 100     4026   3419   3800   -650    211   -829       O
ATOM   1049  CB  THR A 100      -8.032   0.043  16.485  1.00 31.12           C
ANISOU 1049  CB  THR A 100     4189   3772   3864   -726    -80   -799       C
ATOM   1050  OG1 THR A 100      -7.088  -0.285  17.512  1.00 31.21           O
ANISOU 1050  OG1 THR A 100     4209   3835   3814   -775   -242   -838       O
ATOM   1051  CG2 THR A 100      -7.276   0.658  15.321  1.00 28.68           C
ANISOU 1051  CG2 THR A 100     3772   3381   3743   -733    -38   -795       C
ATOM   1052  H   THR A 100      -9.693  -0.371  18.313  1.00 35.45           H
ATOM   1053  HG1 THR A 100      -6.677   0.406  17.756  1.00 37.45           H
ATOM   1054  N   LYS A 101     -11.407   1.091  16.446  1.00 31.69           N
ANISOU 1054  N   LYS A 101     4399   3834   3808   -625    240   -847       N
ATOM   1055  CA  LYS A 101     -12.511   1.293  15.505  1.00 29.66           C
ANISOU 1055  CA  LYS A 101     4114   3545   3610   -548    360   -805       C
ATOM   1056  C   LYS A 101     -12.664   2.756  15.089  1.00 34.54           C
ANISOU 1056  C   LYS A 101     4739   4038   4347   -517    426   -882       C
ATOM   1057  O   LYS A 101     -12.888   3.039  13.907  1.00 32.75           O
ANISOU 1057  O   LYS A 101     4473   3739   4231   -466    473   -814       O
ATOM   1058  CB  LYS A 101     -13.817   0.747  16.072  1.00 32.54           C
ANISOU 1058  CB  LYS A 101     4510   4014   3841   -527    428   -804       C
ATOM   1059  CG  LYS A 101     -14.944   0.626  15.038  1.00 37.32           C
ANISOU 1059  CG  LYS A 101     5058   4615   4508   -449    521   -741       C
ATOM   1060  CD  LYS A 101     -16.301   0.587  15.725  1.00 46.64           C
ANISOU 1060  CD  LYS A 101     6247   5890   5584   -430    616   -795       C
ATOM   1061  CE  LYS A 101     -16.418   1.766  16.675  1.00 51.45           C
ANISOU 1061  CE  LYS A 101     6908   6480   6160   -425    661   -957       C
ATOM   1062  NZ  LYS A 101     -17.804   2.069  17.125  1.00 74.06           N
ANISOU 1062  NZ  LYS A 101     9750   9422   8969   -374    786  -1044       N
ATOM   1063  H   LYS A 101     -11.646   0.775  17.209  1.00 38.03           H
ATOM   1064  HZ1 LYS A 101     -17.851   2.906  17.424  1.00 88.88           H
ATOM   1065  HZ2 LYS A 101     -18.372   1.972  16.447  1.00 88.88           H
ATOM   1066  HZ3 LYS A 101     -18.039   1.515  17.781  1.00 88.88           H
ATOM   1067  N   ASP A 102     -12.568   3.695  16.038  1.00 32.76           N
ANISOU 1067  N   ASP A 102     4576   3777   4096   -545    422  -1021       N
ATOM   1068  CA  ASP A 102     -12.728   5.106  15.707  1.00 35.89           C
ANISOU 1068  CA  ASP A 102     4997   4023   4618   -513    474  -1100       C
ATOM   1069  C   ASP A 102     -11.665   5.566  14.722  1.00 33.67           C
ANISOU 1069  C   ASP A 102     4679   3620   4495   -558    439  -1036       C
ATOM   1070  O   ASP A 102     -11.949   6.357  13.812  1.00 34.53           O
ANISOU 1070  O   ASP A 102     4794   3602   4725   -515    493  -1001       O
ATOM   1071  CB  ASP A 102     -12.661   5.964  16.974  1.00 35.74           C
ANISOU 1071  CB  ASP A 102     5058   3981   4539   -548    460  -1283       C
ATOM   1072  CG  ASP A 102     -13.930   5.912  17.786  1.00 37.75           C
ANISOU 1072  CG  ASP A 102     5349   4332   4662   -485    547  -1374       C
ATOM   1073  OD1 ASP A 102     -14.953   5.473  17.231  1.00 41.95           O
ANISOU 1073  OD1 ASP A 102     5831   4914   5195   -406    625  -1301       O
ATOM   1074  OD2 ASP A 102     -13.893   6.280  18.982  1.00 41.12           O
ANISOU 1074  OD2 ASP A 102     5847   4801   4977   -522    537  -1525       O
ATOM   1075  H   ASP A 102     -12.412   3.540  16.870  1.00 39.32           H
ATOM   1076  N  ASER A 103     -10.423   5.112  14.908  0.63 32.88           N
ANISOU 1076  N  ASER A 103     4539   3558   4396   -649    348  -1020       N
ATOM   1077  CA ASER A 103      -9.327   5.540  14.046  0.63 35.33           C
ANISOU 1077  CA ASER A 103     4792   3777   4854   -714    329   -972       C
ATOM   1078  C  ASER A 103      -9.568   5.139  12.590  0.63 34.67           C
ANISOU 1078  C  ASER A 103     4656   3685   4830   -661    396   -823       C
ATOM   1079  O  ASER A 103      -9.458   5.971  11.684  0.63 34.91           O
ANISOU 1079  O  ASER A 103     4694   3596   4972   -672    448   -779       O
ATOM   1080  CB ASER A 103      -8.007   4.962  14.559  0.63 35.28           C
ANISOU 1080  CB ASER A 103     4720   3847   4837   -804    213   -991       C
ATOM   1081  OG ASER A 103      -7.659   5.511  15.824  0.63 37.13           O
ANISOU 1081  OG ASER A 103     5010   4077   5022   -869    136  -1136       O
ATOM   1082  H  ASER A 103     -10.192   4.558  15.524  0.63 39.46           H
ATOM   1083  HG ASER A 103      -6.973   5.129  16.124  0.63 44.56           H
ATOM   1084  N  BSER A 103     -10.432   5.083  14.891  0.37 32.75           N
ANISOU 1084  N  BSER A 103     4521   3543   4379   -647    348  -1017       N
ATOM   1085  CA BSER A 103      -9.332   5.525  14.041  0.37 35.31           C
ANISOU 1085  CA BSER A 103     4789   3776   4851   -713    329   -971       C
ATOM   1086  C  BSER A 103      -9.568   5.135  12.587  0.37 34.71           C
ANISOU 1086  C  BSER A 103     4661   3692   4836   -661    396   -823       C
ATOM   1087  O  BSER A 103      -9.443   5.968  11.684  0.37 34.87           O
ANISOU 1087  O  BSER A 103     4689   3592   4968   -673    447   -779       O
ATOM   1088  CB BSER A 103      -8.011   4.940  14.544  0.37 35.27           C
ANISOU 1088  CB BSER A 103     4718   3848   4836   -803    213   -989       C
ATOM   1089  OG BSER A 103      -7.991   3.530  14.443  0.37 35.89           O
ANISOU 1089  OG BSER A 103     4746   4056   4836   -763    175   -900       O
ATOM   1090  H  BSER A 103     -10.209   4.504  15.487  0.37 39.30           H
ATOM   1091  HG BSER A 103      -7.240   3.236  14.675  0.37 43.08           H
ATOM   1092  N   ILE A 104      -9.915   3.873  12.339  1.00 35.60           N
ANISOU 1092  N   ILE A 104     4733   3924   4868   -609    391   -743       N
ATOM   1093  CA  ILE A 104     -10.106   3.443  10.952  1.00 30.12           C
ANISOU 1093  CA  ILE A 104     3995   3234   4216   -563    445   -619       C
ATOM   1094  C   ILE A 104     -11.311   4.138  10.327  1.00 31.67           C
ANISOU 1094  C   ILE A 104     4244   3354   4434   -481    524   -588       C
ATOM   1095  O   ILE A 104     -11.230   4.639   9.202  1.00 29.68           O
ANISOU 1095  O   ILE A 104     3995   3025   4257   -474    567   -510       O
ATOM   1096  CB  ILE A 104     -10.205   1.907  10.817  1.00 30.57           C
ANISOU 1096  CB  ILE A 104     4004   3418   4193   -527    411   -554       C
ATOM   1097  CG1 ILE A 104     -10.501   1.566   9.352  1.00 31.52           C
ANISOU 1097  CG1 ILE A 104     4092   3539   4345   -476    470   -449       C
ATOM   1098  CG2 ILE A 104     -11.323   1.284  11.661  1.00 30.16           C
ANISOU 1098  CG2 ILE A 104     3999   3443   4018   -483    405   -573       C
ATOM   1099  CD1 ILE A 104     -10.183   0.190   8.973  1.00 28.98           C
ANISOU 1099  CD1 ILE A 104     3713   3308   3991   -457    432   -400       C
ATOM   1100  H   ILE A 104     -10.042   3.267  12.936  1.00 42.72           H
ATOM   1101  N   LYS A 105     -12.435   4.223  11.053  1.00 32.53           N
ANISOU 1101  N   LYS A 105     4395   3486   4478   -418    542   -650       N
ATOM   1102  CA  LYS A 105     -13.632   4.866  10.510  1.00 30.66           C
ANISOU 1102  CA  LYS A 105     4186   3185   4277   -318    603   -634       C
ATOM   1103  C   LYS A 105     -13.335   6.297  10.083  1.00 33.89           C
ANISOU 1103  C   LYS A 105     4653   3410   4812   -326    618   -645       C
ATOM   1104  O   LYS A 105     -13.791   6.747   9.028  1.00 32.12           O
ANISOU 1104  O   LYS A 105     4449   3107   4649   -266    645   -557       O
ATOM   1105  CB  LYS A 105     -14.761   4.894  11.548  1.00 32.53           C
ANISOU 1105  CB  LYS A 105     4441   3480   4440   -258    631   -738       C
ATOM   1106  CG  LYS A 105     -15.694   3.715  11.526  1.00 30.96           C
ANISOU 1106  CG  LYS A 105     4190   3429   4146   -217    650   -690       C
ATOM   1107  CD  LYS A 105     -16.990   4.074  12.271  1.00 39.95           C
ANISOU 1107  CD  LYS A 105     5326   4609   5245   -145    713   -792       C
ATOM   1108  CE  LYS A 105     -16.720   4.213  13.788  1.00 64.46           C
ANISOU 1108  CE  LYS A 105     8480   7763   8250   -208    715   -926       C
ATOM   1109  NZ  LYS A 105     -17.644   3.479  14.722  1.00 66.62           N
ANISOU 1109  NZ  LYS A 105     8734   8201   8378   -215    769   -972       N
ATOM   1110  H   LYS A 105     -12.526   3.919  11.852  1.00 39.04           H
ATOM   1111  HZ1 LYS A 105     -17.431   3.661  15.567  1.00 79.95           H
ATOM   1112  HZ2 LYS A 105     -18.486   3.728  14.576  1.00 79.95           H
ATOM   1113  HZ3 LYS A 105     -17.576   2.601  14.590  1.00 79.95           H
ATOM   1114  N   LYS A 106     -12.625   7.055  10.926  1.00 29.78           N
ANISOU 1114  N   LYS A 106     4173   2811   4329   -401    592   -752       N
ATOM   1115  CA  LYS A 106     -12.388   8.441  10.574  1.00 30.97           C
ANISOU 1115  CA  LYS A 106     4395   2761   4613   -420    602   -766       C
ATOM   1116  C   LYS A 106     -11.480   8.566   9.359  1.00 33.16           C
ANISOU 1116  C   LYS A 106     4655   2979   4965   -500    613   -628       C
ATOM   1117  O   LYS A 106     -11.535   9.602   8.696  1.00 34.11           O
ANISOU 1117  O   LYS A 106     4846   2928   5186   -501    633   -576       O
ATOM   1118  CB  LYS A 106     -11.779   9.232  11.726  1.00 33.32           C
ANISOU 1118  CB  LYS A 106     4741   2979   4940   -501    565   -925       C
ATOM   1119  CG  LYS A 106     -12.688   9.425  12.951  1.00 34.45           C
ANISOU 1119  CG  LYS A 106     4926   3156   5007   -424    574  -1089       C
ATOM   1120  CD  LYS A 106     -13.275  10.800  12.983  1.00 40.09           C
ANISOU 1120  CD  LYS A 106     5728   3667   5836   -353    597  -1178       C
ATOM   1121  CE  LYS A 106     -14.596  10.833  13.815  1.00 37.81           C
ANISOU 1121  CE  LYS A 106     5447   3446   5472   -218    646  -1316       C
ATOM   1122  NZ  LYS A 106     -15.608  11.812  13.331  1.00 40.83           N
ANISOU 1122  NZ  LYS A 106     5870   3666   5979    -68    680  -1338       N
ATOM   1123  H   LYS A 106     -12.288   6.794  11.673  1.00 35.73           H
ATOM   1124  HZ1 LYS A 106     -15.287  12.640  13.398  1.00 49.01           H
ATOM   1125  HZ2 LYS A 106     -16.350  11.750  13.818  1.00 49.01           H
ATOM   1126  HZ3 LYS A 106     -15.807  11.648  12.479  1.00 49.01           H
ATOM   1127  N   LYS A 107     -10.629   7.569   9.087  1.00 31.09           N
ANISOU 1127  N   LYS A 107     4306   2849   4659   -569    601   -572       N
ATOM   1128  CA  LYS A 107      -9.791   7.610   7.886  1.00 34.31           C
ANISOU 1128  CA  LYS A 107     4681   3233   5120   -644    636   -450       C
ATOM   1129  C   LYS A 107     -10.520   7.156   6.629  1.00 33.09           C
ANISOU 1129  C   LYS A 107     4533   3121   4920   -556    679   -313       C
ATOM   1130  O   LYS A 107     -10.047   7.442   5.521  1.00 33.07           O
ANISOU 1130  O   LYS A 107     4541   3077   4949   -608    724   -203       O
ATOM   1131  CB  LYS A 107      -8.509   6.767   8.028  1.00 34.58           C
ANISOU 1131  CB  LYS A 107     4601   3394   5145   -743    610   -463       C
ATOM   1132  CG  LYS A 107      -7.435   7.362   8.963  1.00 39.93           C
ANISOU 1132  CG  LYS A 107     5254   4022   5894   -870    557   -576       C
ATOM   1133  CD  LYS A 107      -6.976   6.389  10.048  1.00 43.57           C
ANISOU 1133  CD  LYS A 107     5642   4629   6286   -876    466   -666       C
ATOM   1134  CE  LYS A 107      -6.482   7.106  11.334  1.00 53.60           C
ANISOU 1134  CE  LYS A 107     6940   5843   7582   -959    387   -815       C
ATOM   1135  NZ  LYS A 107      -7.537   7.920  12.048  1.00 45.46           N
ANISOU 1135  NZ  LYS A 107     6040   4712   6521   -900    395   -904       N
ATOM   1136  H   LYS A 107     -10.520   6.869   9.576  1.00 37.31           H
ATOM   1137  HZ1 LYS A 107      -7.189   8.302  12.773  1.00 54.55           H
ATOM   1138  HZ2 LYS A 107      -7.847   8.556  11.508  1.00 54.55           H
ATOM   1139  HZ3 LYS A 107      -8.212   7.395  12.294  1.00 54.55           H
ATOM   1140  N   LEU A 108     -11.649   6.471   6.764  1.00 31.16           N
ANISOU 1140  N   LEU A 108     4283   2962   4596   -436    668   -319       N
ATOM   1141  CA  LEU A 108     -12.445   6.028   5.617  1.00 31.52           C
ANISOU 1141  CA  LEU A 108     4330   3052   4593   -349    689   -205       C
ATOM   1142  C   LEU A 108     -13.628   6.977   5.447  1.00 32.56           C
ANISOU 1142  C   LEU A 108     4541   3063   4768   -240    686   -193       C
ATOM   1143  O   LEU A 108     -14.767   6.681   5.811  1.00 34.73           O
ANISOU 1143  O   LEU A 108     4796   3392   5009   -133    672   -237       O
ATOM   1144  CB  LEU A 108     -12.895   4.591   5.820  1.00 30.52           C
ANISOU 1144  CB  LEU A 108     4132   3098   4367   -300    668   -219       C
ATOM   1145  CG  LEU A 108     -11.813   3.561   6.133  1.00 29.82           C
ANISOU 1145  CG  LEU A 108     3967   3117   4246   -376    646   -244       C
ATOM   1146  CD1 LEU A 108     -12.345   2.160   5.895  1.00 29.40           C
ANISOU 1146  CD1 LEU A 108     3868   3195   4107   -320    626   -218       C
ATOM   1147  CD2 LEU A 108     -10.574   3.801   5.252  1.00 29.15           C
ANISOU 1147  CD2 LEU A 108     3855   3011   4211   -465    683   -187       C
ATOM   1148  H   LEU A 108     -11.984   6.244   7.523  1.00 37.40           H
ATOM   1149  N   VAL A 109     -13.336   8.133   4.871  1.00 34.40           N
ANISOU 1149  N   VAL A 109     4858   3127   5085   -271    698   -130       N
ATOM   1150  CA  VAL A 109     -14.305   9.208   4.743  1.00 36.60           C
ANISOU 1150  CA  VAL A 109     5225   3245   5436   -163    677   -121       C
ATOM   1151  C   VAL A 109     -15.405   8.775   3.781  1.00 38.32           C
ANISOU 1151  C   VAL A 109     5434   3529   5597    -34    656    -22       C
ATOM   1152  O   VAL A 109     -15.128   8.280   2.686  1.00 38.33           O
ANISOU 1152  O   VAL A 109     5434   3597   5531    -65    666    103       O
ATOM   1153  CB  VAL A 109     -13.581  10.466   4.245  1.00 38.11           C
ANISOU 1153  CB  VAL A 109     5526   3224   5731   -252    685    -48       C
ATOM   1154  CG1 VAL A 109     -14.517  11.634   4.080  1.00 39.65           C
ANISOU 1154  CG1 VAL A 109     5831   3213   6021   -130    645    -30       C
ATOM   1155  CG2 VAL A 109     -12.385  10.780   5.153  1.00 36.64           C
ANISOU 1155  CG2 VAL A 109     5325   2995   5602   -405    697   -153       C
ATOM   1156  H   VAL A 109     -12.566   8.324   4.538  1.00 41.28           H
ATOM   1157  N   GLY A 110     -16.659   8.972   4.166  1.00 36.76           N
ANISOU 1157  N   GLY A 110     5222   3321   5424    111    626    -86       N
ATOM   1158  CA  GLY A 110     -17.763   8.627   3.289  1.00 35.90           C
ANISOU 1158  CA  GLY A 110     5088   3274   5278    237    587     -3       C
ATOM   1159  C   GLY A 110     -18.543   7.393   3.686  1.00 33.89           C
ANISOU 1159  C   GLY A 110     4708   3227   4941    285    588    -69       C
ATOM   1160  O   GLY A 110     -19.356   6.910   2.881  1.00 34.36           O
ANISOU 1160  O   GLY A 110     4730   3367   4958    363    549     -1       O
ATOM   1161  H   GLY A 110     -16.892   9.301   4.926  1.00 44.12           H
ATOM   1162  N   ILE A 111     -18.301   6.852   4.881  1.00 35.52           N
ANISOU 1162  N   ILE A 111     4856   3522   5116    227    625   -193       N
ATOM   1163  CA  ILE A 111     -19.152   5.794   5.416  1.00 30.25           C
ANISOU 1163  CA  ILE A 111     4083   3030   4379    262    633   -257       C
ATOM   1164  C   ILE A 111     -20.553   6.330   5.651  1.00 32.15           C
ANISOU 1164  C   ILE A 111     4277   3258   4680    410    626   -324       C
ATOM   1165  O   ILE A 111     -20.742   7.381   6.278  1.00 31.68           O
ANISOU 1165  O   ILE A 111     4253   3080   4705    468    640   -418       O
ATOM   1166  CB  ILE A 111     -18.555   5.191   6.705  1.00 30.77           C
ANISOU 1166  CB  ILE A 111     4124   3181   4386    161    668   -361       C
ATOM   1167  CG1 ILE A 111     -17.259   4.424   6.411  1.00 29.15           C
ANISOU 1167  CG1 ILE A 111     3928   3019   4130     38    658   -298       C
ATOM   1168  CG2 ILE A 111     -19.595   4.388   7.475  1.00 29.56           C
ANISOU 1168  CG2 ILE A 111     3882   3181   4169    193    691   -437       C
ATOM   1169  CD1 ILE A 111     -16.342   4.310   7.636  1.00 28.60           C
ANISOU 1169  CD1 ILE A 111     3866   2964   4035    -61    663   -391       C
ATOM   1170  H   ILE A 111     -17.654   7.080   5.399  1.00 42.62           H
ATOM   1171  N   GLN A 112     -21.547   5.585   5.185  1.00 27.72           N
ANISOU 1171  N   GLN A 112     3624   2823   4083    472    603   -294       N
ATOM   1172  CA  GLN A 112     -22.958   5.960   5.296  1.00 30.29           C
ANISOU 1172  CA  GLN A 112     3863   3171   4474    620    592   -358       C
ATOM   1173  C   GLN A 112     -23.741   5.172   6.321  1.00 28.54           C
ANISOU 1173  C   GLN A 112     3514   3125   4204    606    654   -476       C
ATOM   1174  O   GLN A 112     -24.742   5.680   6.829  1.00 31.95           O
ANISOU 1174  O   GLN A 112     3866   3573   4701    715    682   -583       O
ATOM   1175  CB  GLN A 112     -23.641   5.757   3.945  1.00 29.39           C
ANISOU 1175  CB  GLN A 112     3719   3082   4365    703    506   -239       C
ATOM   1176  CG  GLN A 112     -23.126   6.707   2.931  1.00 32.61           C
ANISOU 1176  CG  GLN A 112     4260   3313   4818    738    446   -116       C
ATOM   1177  CD  GLN A 112     -23.706   6.420   1.594  1.00 33.19           C
ANISOU 1177  CD  GLN A 112     4323   3430   4856    804    352     10       C
ATOM   1178  OE1 GLN A 112     -23.282   5.479   0.938  1.00 31.91           O
ANISOU 1178  OE1 GLN A 112     4168   3370   4587    714    344     84       O
ATOM   1179  NE2 GLN A 112     -24.750   7.173   1.215  1.00 38.85           N
ANISOU 1179  NE2 GLN A 112     5014   4082   5665    971    271     19       N
ATOM   1180  H   GLN A 112     -21.430   4.832   4.787  1.00 33.26           H
ATOM   1181 HE21 GLN A 112     -25.118   7.043   0.449  1.00 46.62           H
ATOM   1182 HE22 GLN A 112     -25.050   7.786   1.738  1.00 46.62           H
ATOM   1183  N   VAL A 113     -23.322   3.937   6.594  1.00 28.14           N
ANISOU 1183  N   VAL A 113     3443   3204   4044    475    676   -454       N
ATOM   1184  CA  VAL A 113     -24.007   2.987   7.463  1.00 29.79           C
ANISOU 1184  CA  VAL A 113     3549   3586   4183    424    733   -526       C
ATOM   1185  C   VAL A 113     -22.938   2.261   8.277  1.00 29.61           C
ANISOU 1185  C   VAL A 113     3593   3599   4057    272    761   -529       C
ATOM   1186  O   VAL A 113     -21.840   1.993   7.780  1.00 27.25           O
ANISOU 1186  O   VAL A 113     3371   3245   3738    208    717   -448       O
ATOM   1187  CB  VAL A 113     -24.854   1.996   6.631  1.00 31.48           C
ANISOU 1187  CB  VAL A 113     3660   3920   4379    430    689   -457       C
ATOM   1188  CG1 VAL A 113     -25.510   0.926   7.507  1.00 30.86           C
ANISOU 1188  CG1 VAL A 113     3483   4014   4229    340    752   -512       C
ATOM   1189  CG2 VAL A 113     -25.923   2.746   5.843  1.00 34.48           C
ANISOU 1189  CG2 VAL A 113     3964   4271   4864    592    636   -455       C
ATOM   1190  H   VAL A 113     -22.598   3.608   6.267  1.00 33.77           H
ATOM   1191  N  AGLU A 114     -23.238   1.987   9.550  0.59 31.93           N
ANISOU 1191  N  AGLU A 114     3859   3991   4284    220    833   -627       N
ATOM   1192  CA AGLU A 114     -22.361   1.220  10.430  0.59 31.76           C
ANISOU 1192  CA AGLU A 114     3901   4017   4148     82    842   -625       C
ATOM   1193  C  AGLU A 114     -23.152   0.067  11.034  0.59 33.37           C
ANISOU 1193  C  AGLU A 114     4035   4388   4257      5    887   -627       C
ATOM   1194  O  AGLU A 114     -24.309   0.239  11.441  0.59 34.63           O
ANISOU 1194  O  AGLU A 114     4098   4640   4421     44    962   -704       O
ATOM   1195  CB AGLU A 114     -21.768   2.069  11.594  0.59 32.98           C
ANISOU 1195  CB AGLU A 114     4134   4122   4276     61    880   -740       C
ATOM   1196  CG AGLU A 114     -21.496   3.542  11.293  0.59 35.36           C
ANISOU 1196  CG AGLU A 114     4485   4254   4697    156    869   -793       C
ATOM   1197  CD AGLU A 114     -20.562   4.231  12.305  0.59 39.66           C
ANISOU 1197  CD AGLU A 114     5127   4727   5214     99    874   -894       C
ATOM   1198  OE1AGLU A 114     -20.073   3.587  13.259  0.59 40.70           O
ANISOU 1198  OE1AGLU A 114     5292   4950   5222     -8    877   -921       O
ATOM   1199  OE2AGLU A 114     -20.330   5.443  12.149  0.59 41.92           O
ANISOU 1199  OE2AGLU A 114     5465   4859   5605    160    864   -948       O
ATOM   1200  H  AGLU A 114     -23.963   2.243   9.934  0.59 38.32           H
ATOM   1201  N  BGLU A 114     -23.242   1.983   9.542  0.41 31.69           N
ANISOU 1201  N  BGLU A 114     3828   3960   4253    220    833   -626       N
ATOM   1202  CA BGLU A 114     -22.358   1.189  10.381  0.41 31.84           C
ANISOU 1202  CA BGLU A 114     3911   4028   4160     82    839   -620       C
ATOM   1203  C  BGLU A 114     -23.149   0.065  11.033  0.41 33.17           C
ANISOU 1203  C  BGLU A 114     4010   4362   4232      4    887   -627       C
ATOM   1204  O  BGLU A 114     -24.296   0.253  11.458  0.41 34.46           O
ANISOU 1204  O  BGLU A 114     4078   4617   4398     44    963   -705       O
ATOM   1205  CB BGLU A 114     -21.661   2.016  11.475  0.41 33.08           C
ANISOU 1205  CB BGLU A 114     4151   4126   4291     57    870   -725       C
ATOM   1206  CG BGLU A 114     -20.370   1.348  11.927  0.41 36.06           C
ANISOU 1206  CG BGLU A 114     4612   4505   4585    -68    820   -681       C
ATOM   1207  CD BGLU A 114     -19.968   1.660  13.345  0.41 40.41           C
ANISOU 1207  CD BGLU A 114     5227   5082   5045   -129    847   -792       C
ATOM   1208  OE1BGLU A 114     -20.007   2.846  13.739  0.41 41.96           O
ANISOU 1208  OE1BGLU A 114     5452   5202   5288    -75    880   -906       O
ATOM   1209  OE2BGLU A 114     -19.594   0.708  14.062  0.41 44.47           O
ANISOU 1209  OE2BGLU A 114     5775   5685   5438   -231    826   -763       O
ATOM   1210  H  BGLU A 114     -23.960   2.247   9.936  0.41 38.03           H
ATOM   1211  N   VAL A 115     -22.516  -1.103  11.090  1.00 32.64           N
ANISOU 1211  N   VAL A 115     3988   4328   4087   -107    842   -543       N
ATOM   1212  CA  VAL A 115     -23.070  -2.324  11.673  1.00 29.06           C
ANISOU 1212  CA  VAL A 115     3503   4003   3536   -214    869   -515       C
ATOM   1213  C   VAL A 115     -22.032  -2.892  12.633  1.00 32.35           C
ANISOU 1213  C   VAL A 115     4033   4418   3839   -325    839   -492       C
ATOM   1214  O   VAL A 115     -20.861  -3.015  12.267  1.00 32.38           O
ANISOU 1214  O   VAL A 115     4106   4331   3865   -331    755   -443       O
ATOM   1215  CB  VAL A 115     -23.370  -3.379  10.593  1.00 34.07           C
ANISOU 1215  CB  VAL A 115     4090   4650   4203   -234    805   -415       C
ATOM   1216  CG1 VAL A 115     -23.746  -4.689  11.275  1.00 31.46           C
ANISOU 1216  CG1 VAL A 115     3760   4416   3776   -372    821   -372       C
ATOM   1217  CG2 VAL A 115     -24.470  -2.917   9.650  1.00 31.55           C
ANISOU 1217  CG2 VAL A 115     3653   4352   3983   -129    811   -432       C
ATOM   1218  H   VAL A 115     -21.722  -1.223  10.781  1.00 39.18           H
ATOM   1219  N   GLN A 116     -22.454  -3.300  13.841  1.00 33.62           N
ANISOU 1219  N   GLN A 116     4211   4688   3874   -417    904   -522       N
ATOM   1220  CA  GLN A 116     -21.571  -4.036  14.745  1.00 30.97           C
ANISOU 1220  CA  GLN A 116     3993   4360   3412   -529    851   -474       C
ATOM   1221  C   GLN A 116     -22.214  -5.399  14.976  1.00 33.40           C
ANISOU 1221  C   GLN A 116     4295   4753   3641   -646    860   -382       C
ATOM   1222  O   GLN A 116     -23.315  -5.482  15.532  1.00 37.22           O
ANISOU 1222  O   GLN A 116     4720   5360   4062   -697    971   -417       O
ATOM   1223  CB  GLN A 116     -21.361  -3.308  16.067  1.00 42.44           C
ANISOU 1223  CB  GLN A 116     5515   5861   4751   -556    905   -578       C
ATOM   1224  CG  GLN A 116     -21.230  -1.816  15.947  1.00 61.63           C
ANISOU 1224  CG  GLN A 116     7927   8220   7270   -443    937   -705       C
ATOM   1225  CD  GLN A 116     -20.239  -1.261  16.944  1.00 75.36           C
ANISOU 1225  CD  GLN A 116     9778   9931   8925   -479    901   -779       C
ATOM   1226  OE1 GLN A 116     -20.252  -1.631  18.118  1.00 77.69           O
ANISOU 1226  OE1 GLN A 116    10143  10327   9049   -571    924   -801       O
ATOM   1227  NE2 GLN A 116     -19.397  -0.335  16.489  1.00 71.30           N
ANISOU 1227  NE2 GLN A 116     9284   9284   8524   -416    844   -820       N
ATOM   1228  H   GLN A 116     -23.243  -3.160  14.151  1.00 40.34           H
ATOM   1229 HE21 GLN A 116     -19.437  -0.085  15.668  1.00 85.57           H
ATOM   1230 HE22 GLN A 116     -18.814   0.012  17.017  1.00 85.57           H
ATOM   1231  N   ALA A 117     -21.541  -6.461  14.552  1.00 27.32           N
ANISOU 1231  N   ALA A 117     3583   3915   2884   -690    747   -271       N
ATOM   1232  CA  ALA A 117     -22.091  -7.798  14.627  1.00 26.71           C
ANISOU 1232  CA  ALA A 117     3515   3876   2759   -804    734   -174       C
ATOM   1233  C   ALA A 117     -21.270  -8.643  15.596  1.00 27.95           C
ANISOU 1233  C   ALA A 117     3820   4009   2790   -906    653    -91       C
ATOM   1234  O   ALA A 117     -20.039  -8.651  15.519  1.00 26.40           O
ANISOU 1234  O   ALA A 117     3694   3720   2619   -862    539    -74       O
ATOM   1235  CB  ALA A 117     -22.098  -8.432  13.227  1.00 24.23           C
ANISOU 1235  CB  ALA A 117     3150   3481   2574   -760    656   -119       C
ATOM   1236  H   ALA A 117     -20.752  -6.426  14.212  1.00 32.79           H
ATOM   1237  N   THR A 118     -21.952  -9.402  16.462  1.00 28.82           N
ANISOU 1237  N   THR A 118     3975   4204   2772  -1047    703    -31       N
ATOM   1238  CA  THR A 118     -21.279 -10.256  17.433  1.00 30.24           C
ANISOU 1238  CA  THR A 118     4316   4359   2813  -1154    615     71       C
ATOM   1239  C   THR A 118     -21.646 -11.734  17.278  1.00 34.09           C
ANISOU 1239  C   THR A 118     4854   4799   3299  -1272    560    212       C
ATOM   1240  O   THR A 118     -21.157 -12.578  18.043  1.00 31.76           O
ANISOU 1240  O   THR A 118     4710   4462   2896  -1365    469    323       O
ATOM   1241  CB  THR A 118     -21.573  -9.804  18.874  1.00 32.71           C
ANISOU 1241  CB  THR A 118     4697   4810   2922  -1241    715     33       C
ATOM   1242  OG1 THR A 118     -22.970  -9.957  19.144  1.00 33.82           O
ANISOU 1242  OG1 THR A 118     4759   5089   3003  -1341    880     24       O
ATOM   1243  CG2 THR A 118     -21.209  -8.340  19.008  1.00 31.21           C
ANISOU 1243  CG2 THR A 118     4465   4642   2750  -1123    759   -123       C
ATOM   1244  H   THR A 118     -22.810  -9.435  16.504  1.00 34.59           H
ATOM   1245  HG1 THR A 118     -23.414  -9.425  18.669  1.00 40.59           H
ATOM   1246  N   ASP A 119     -22.480 -12.073  16.312  1.00 31.17           N
ANISOU 1246  N   ASP A 119     4372   4424   3047  -1273    596    211       N
ATOM   1247  CA  ASP A 119     -22.833 -13.466  16.068  1.00 31.12           C
ANISOU 1247  CA  ASP A 119     4412   4349   3063  -1391    535    330       C
ATOM   1248  C   ASP A 119     -23.399 -13.592  14.658  1.00 31.52           C
ANISOU 1248  C   ASP A 119     4325   4365   3285  -1329    530    287       C
ATOM   1249  O   ASP A 119     -23.537 -12.611  13.910  1.00 30.33           O
ANISOU 1249  O   ASP A 119     4053   4250   3222  -1198    573    183       O
ATOM   1250  CB  ASP A 119     -23.790 -13.999  17.140  1.00 33.63           C
ANISOU 1250  CB  ASP A 119     4771   4780   3226  -1593    643    405       C
ATOM   1251  CG  ASP A 119     -25.167 -13.354  17.106  1.00 33.39           C
ANISOU 1251  CG  ASP A 119     4558   4927   3200  -1627    836    309       C
ATOM   1252  OD1 ASP A 119     -25.491 -12.564  16.166  1.00 33.61           O
ANISOU 1252  OD1 ASP A 119     4429   4975   3366  -1488    868    196       O
ATOM   1253  OD2 ASP A 119     -25.893 -13.610  18.076  1.00 35.16           O
ANISOU 1253  OD2 ASP A 119     4798   5268   3293  -1771    943    343       O
ATOM   1254  H   ASP A 119     -22.859 -11.514  15.780  1.00 37.41           H
ATOM   1255  N   ALA A 120     -23.681 -14.838  14.280  1.00 34.59           N
ANISOU 1255  N   ALA A 120     4751   4669   3720  -1426    460    373       N
ATOM   1256  CA  ALA A 120     -24.053 -15.121  12.896  1.00 33.47           C
ANISOU 1256  CA  ALA A 120     4509   4476   3731  -1369    417    332       C
ATOM   1257  C   ALA A 120     -25.321 -14.377  12.496  1.00 32.11           C
ANISOU 1257  C   ALA A 120     4145   4455   3599  -1362    547    243       C
ATOM   1258  O   ALA A 120     -25.418 -13.867  11.374  1.00 32.49           O
ANISOU 1258  O   ALA A 120     4092   4500   3753  -1234    525    167       O
ATOM   1259  CB  ALA A 120     -24.223 -16.637  12.705  1.00 33.93           C
ANISOU 1259  CB  ALA A 120     4654   4411   3827  -1500    319    430       C
ATOM   1260  H   ALA A 120     -23.664 -15.526  14.796  1.00 41.51           H
ATOM   1261  N   ALA A 121     -26.299 -14.273  13.412  1.00 30.77           N
ANISOU 1261  N   ALA A 121     3920   4430   3341  -1492    684    249       N
ATOM   1262  CA  ALA A 121     -27.521 -13.565  13.055  1.00 30.99           C
ANISOU 1262  CA  ALA A 121     3739   4609   3425  -1468    803    151       C
ATOM   1263  C   ALA A 121     -27.242 -12.081  12.832  1.00 31.12           C
ANISOU 1263  C   ALA A 121     3686   4667   3471  -1269    844     37       C
ATOM   1264  O   ALA A 121     -27.841 -11.448  11.953  1.00 31.80           O
ANISOU 1264  O   ALA A 121     3623   4795   3663  -1161    856    -43       O
ATOM   1265  CB  ALA A 121     -28.594 -13.772  14.121  1.00 36.70           C
ANISOU 1265  CB  ALA A 121     4402   5495   4048  -1652    961    169       C
ATOM   1266  H   ALA A 121     -26.274 -14.592  14.210  1.00 36.93           H
ATOM   1267  N   GLU A 122     -26.307 -11.502  13.598  1.00 31.51           N
ANISOU 1267  N   GLU A 122     3851   4692   3431  -1219    849     29       N
ATOM   1268  CA  GLU A 122     -26.066 -10.071  13.479  1.00 29.30           C
ANISOU 1268  CA  GLU A 122     3516   4434   3182  -1052    892    -82       C
ATOM   1269  C   GLU A 122     -25.287  -9.689  12.222  1.00 27.60           C
ANISOU 1269  C   GLU A 122     3306   4093   3089   -895    778    -96       C
ATOM   1270  O   GLU A 122     -25.311  -8.527  11.821  1.00 25.53           O
ANISOU 1270  O   GLU A 122     2978   3836   2886   -759    806   -177       O
ATOM   1271  CB  GLU A 122     -25.365  -9.569  14.760  1.00 29.76           C
ANISOU 1271  CB  GLU A 122     3693   4514   3100  -1069    934   -100       C
ATOM   1272  CG  GLU A 122     -26.387  -9.379  15.906  1.00 29.84           C
ANISOU 1272  CG  GLU A 122     3649   4704   2987  -1176   1105   -146       C
ATOM   1273  CD  GLU A 122     -25.727  -9.044  17.217  1.00 32.01           C
ANISOU 1273  CD  GLU A 122     4064   5012   3086  -1218   1138   -160       C
ATOM   1274  OE1 GLU A 122     -24.549  -8.623  17.187  1.00 29.99           O
ANISOU 1274  OE1 GLU A 122     3910   4649   2838  -1130   1035   -168       O
ATOM   1275  OE2 GLU A 122     -26.421  -9.072  18.245  1.00 35.38           O
ANISOU 1275  OE2 GLU A 122     4484   5589   3371  -1331   1276   -182       O
ATOM   1276  H   GLU A 122     -25.818 -11.909  14.176  1.00 37.82           H
ATOM   1277  N   ILE A 123     -24.634 -10.634  11.557  1.00 27.89           N
ANISOU 1277  N   ILE A 123     3419   4015   3163   -912    654    -23       N
ATOM   1278  CA  ILE A 123     -23.915 -10.400  10.310  1.00 24.36           C
ANISOU 1278  CA  ILE A 123     2975   3469   2813   -781    562    -36       C
ATOM   1279  C   ILE A 123     -24.667 -10.967   9.114  1.00 26.03           C
ANISOU 1279  C   ILE A 123     3103   3681   3107   -779    516    -34       C
ATOM   1280  O   ILE A 123     -24.149 -10.948   8.001  1.00 24.76           O
ANISOU 1280  O   ILE A 123     2953   3449   3004   -689    440    -42       O
ATOM   1281  CB  ILE A 123     -22.486 -10.952  10.393  1.00 22.20           C
ANISOU 1281  CB  ILE A 123     2839   3073   2524   -774    458     14       C
ATOM   1282  CG1 ILE A 123     -21.670 -10.408   9.234  1.00 26.31           C
ANISOU 1282  CG1 ILE A 123     3347   3523   3126   -637    406    -21       C
ATOM   1283  CG2 ILE A 123     -22.530 -12.470  10.426  1.00 27.61           C
ANISOU 1283  CG2 ILE A 123     3594   3695   3202   -887    378     94       C
ATOM   1284  CD1 ILE A 123     -21.396  -8.977   9.347  1.00 25.77           C
ANISOU 1284  CD1 ILE A 123     3251   3474   3065   -547    466    -79       C
ATOM   1285  H   ILE A 123     -24.591 -11.453  11.818  1.00 33.47           H
ATOM   1286  N   SER A 124     -25.886 -11.449   9.329  1.00 24.23           N
ANISOU 1286  N   SER A 124     2785   3542   2878   -885    565    -31       N
ATOM   1287  CA  SER A 124     -26.739 -11.945   8.241  1.00 27.31           C
ANISOU 1287  CA  SER A 124     3075   3952   3350   -895    514    -44       C
ATOM   1288  C   SER A 124     -27.009 -10.857   7.200  1.00 25.22           C
ANISOU 1288  C   SER A 124     2710   3719   3154   -730    502   -109       C
ATOM   1289  O   SER A 124     -27.019  -9.663   7.500  1.00 25.01           O
ANISOU 1289  O   SER A 124     2646   3730   3127   -631    570   -154       O
ATOM   1290  CB  SER A 124     -28.049 -12.467   8.820  1.00 28.49           C
ANISOU 1290  CB  SER A 124     3115   4218   3492  -1050    590    -39       C
ATOM   1291  OG  SER A 124     -28.936 -11.421   9.251  1.00 32.58           O
ANISOU 1291  OG  SER A 124     3482   4882   4014  -1004    712   -113       O
ATOM   1292  H   SER A 124     -26.253 -11.505  10.104  1.00 29.08           H
ATOM   1293  HG  SER A 124     -29.593 -11.750   9.658  1.00 39.10           H
ATOM   1294  N   GLU A 125     -27.210 -11.262   5.921  1.00 25.66           N
ANISOU 1294  N   GLU A 125     2738   3748   3265   -695    404   -115       N
ATOM   1295  CA  GLU A 125     -27.579 -10.243   4.961  1.00 23.59           C
ANISOU 1295  CA  GLU A 125     2389   3523   3051   -547    382   -159       C
ATOM   1296  C   GLU A 125     -28.866  -9.514   5.382  1.00 24.58           C
ANISOU 1296  C   GLU A 125     2339   3781   3218   -527    461   -212       C
ATOM   1297  O   GLU A 125     -29.034  -8.316   5.108  1.00 28.21           O
ANISOU 1297  O   GLU A 125     2746   4257   3714   -382    475   -248       O
ATOM   1298  CB  GLU A 125     -27.748 -10.879   3.538  1.00 23.73           C
ANISOU 1298  CB  GLU A 125     2402   3517   3097   -530    257   -162       C
ATOM   1299  CG  GLU A 125     -27.770  -9.796   2.512  1.00 24.94           C
ANISOU 1299  CG  GLU A 125     2528   3683   3267   -367    218   -178       C
ATOM   1300  CD  GLU A 125     -27.935 -10.314   1.106  1.00 28.85           C
ANISOU 1300  CD  GLU A 125     3030   4174   3758   -344     95   -187       C
ATOM   1301  OE1 GLU A 125     -28.085 -11.526   0.931  1.00 31.55           O
ANISOU 1301  OE1 GLU A 125     3388   4501   4100   -454     40   -198       O
ATOM   1302  OE2 GLU A 125     -27.926  -9.477   0.193  1.00 27.70           O
ANISOU 1302  OE2 GLU A 125     2885   4038   3603   -218     50   -183       O
ATOM   1303  H   GLU A 125     -27.139 -12.066   5.624  1.00 30.80           H
ATOM   1304  N   ASP A 126     -29.800 -10.218   6.003  1.00 28.05           N
ANISOU 1304  N   ASP A 126     2681   4313   3662   -668    511   -219       N
ATOM   1305  CA  ASP A 126     -31.035  -9.565   6.399  1.00 28.15           C
ANISOU 1305  CA  ASP A 126     2499   4473   3725   -646    599   -288       C
ATOM   1306  C   ASP A 126     -30.747  -8.408   7.351  1.00 31.15           C
ANISOU 1306  C   ASP A 126     2894   4868   4073   -559    716   -331       C
ATOM   1307  O   ASP A 126     -31.398  -7.363   7.300  1.00 31.98           O
ANISOU 1307  O   ASP A 126     2873   5037   4243   -429    755   -406       O
ATOM   1308  CB  ASP A 126     -31.941 -10.536   7.126  1.00 34.41           C
ANISOU 1308  CB  ASP A 126     3194   5370   4510   -848    670   -283       C
ATOM   1309  CG  ASP A 126     -32.787 -11.367   6.214  1.00 37.10           C
ANISOU 1309  CG  ASP A 126     3422   5750   4926   -924    571   -288       C
ATOM   1310  OD1 ASP A 126     -32.959 -11.051   5.012  1.00 37.49           O
ANISOU 1310  OD1 ASP A 126     3422   5786   5035   -799    452   -315       O
ATOM   1311  OD2 ASP A 126     -33.403 -12.277   6.781  1.00 39.47           O
ANISOU 1311  OD2 ASP A 126     3666   6110   5221  -1120    623   -269       O
ATOM   1312  H   ASP A 126     -29.745 -11.053   6.202  1.00 33.66           H
ATOM   1313  N   ALA A 127     -29.793  -8.607   8.251  1.00 31.26           N
ANISOU 1313  N   ALA A 127     3065   4821   3993   -627    763   -293       N
ATOM   1314  CA  ALA A 127     -29.475  -7.586   9.249  1.00 34.20           C
ANISOU 1314  CA  ALA A 127     3470   5208   4318   -566    869   -346       C
ATOM   1315  C   ALA A 127     -28.835  -6.363   8.599  1.00 33.84           C
ANISOU 1315  C   ALA A 127     3471   5062   4327   -375    819   -374       C
ATOM   1316  O   ALA A 127     -29.206  -5.219   8.901  1.00 34.89           O
ANISOU 1316  O   ALA A 127     3535   5222   4498   -262    883   -457       O
ATOM   1317  CB  ALA A 127     -28.567  -8.177  10.326  1.00 30.91           C
ANISOU 1317  CB  ALA A 127     3218   4750   3774   -694    901   -291       C
ATOM   1318  H   ALA A 127     -29.315  -9.319   8.308  1.00 37.52           H
ATOM   1319  N   VAL A 128     -27.866  -6.583   7.706  1.00 29.19           N
ANISOU 1319  N   VAL A 128     2998   4350   3742   -341    708   -308       N
ATOM   1320  CA  VAL A 128     -27.200  -5.490   7.010  1.00 31.31           C
ANISOU 1320  CA  VAL A 128     3324   4519   4054   -190    663   -312       C
ATOM   1321  C   VAL A 128     -28.166  -4.757   6.102  1.00 33.10           C
ANISOU 1321  C   VAL A 128     3426   4778   4375    -56    624   -342       C
ATOM   1322  O   VAL A 128     -28.189  -3.518   6.040  1.00 33.38           O
ANISOU 1322  O   VAL A 128     3454   4766   4462     78    638   -380       O
ATOM   1323  CB  VAL A 128     -26.002  -6.040   6.216  1.00 29.55           C
ANISOU 1323  CB  VAL A 128     3235   4188   3805   -204    570   -237       C
ATOM   1324  CG1 VAL A 128     -25.494  -5.005   5.198  1.00 27.40           C
ANISOU 1324  CG1 VAL A 128     3004   3830   3576    -67    523   -222       C
ATOM   1325  CG2 VAL A 128     -24.944  -6.454   7.183  1.00 31.00           C
ANISOU 1325  CG2 VAL A 128     3536   4325   3917   -291    595   -218       C
ATOM   1326  H   VAL A 128     -27.576  -7.362   7.486  1.00 35.03           H
ATOM   1327  N   SER A 129     -28.935  -5.520   5.326  1.00 33.54           N
ANISOU 1327  N   SER A 129     3391   4897   4457    -88    555   -323       N
ATOM   1328  CA  SER A 129     -29.939  -4.930   4.457  1.00 34.06           C
ANISOU 1328  CA  SER A 129     3323   5009   4609     37    491   -350       C
ATOM   1329  C   SER A 129     -30.930  -4.082   5.253  1.00 39.35           C
ANISOU 1329  C   SER A 129     3836   5766   5348    111    585   -446       C
ATOM   1330  O   SER A 129     -31.259  -2.954   4.865  1.00 37.87           O
ANISOU 1330  O   SER A 129     3604   5544   5240    281    554   -477       O
ATOM   1331  CB  SER A 129     -30.655  -6.042   3.697  1.00 33.06           C
ANISOU 1331  CB  SER A 129     3110   4958   4492    -44    403   -332       C
ATOM   1332  OG  SER A 129     -31.736  -5.526   2.946  1.00 41.54           O
ANISOU 1332  OG  SER A 129     4031   6102   5652     72    327   -365       O
ATOM   1333  H   SER A 129     -28.892  -6.378   5.287  1.00 40.26           H
ATOM   1334  HG  SER A 129     -32.451  -5.604   3.380  1.00 49.85           H
ATOM   1335  N   GLU A 130     -31.402  -4.600   6.392  1.00 37.89           N
ANISOU 1335  N   GLU A 130     3574   5691   5132    -13    705   -497       N
ATOM   1336  CA  GLU A 130     -32.343  -3.824   7.188  1.00 38.04           C
ANISOU 1336  CA  GLU A 130     3431   5813   5208     56    818   -612       C
ATOM   1337  C   GLU A 130     -31.733  -2.494   7.613  1.00 38.20           C
ANISOU 1337  C   GLU A 130     3546   5727   5242    197    861   -663       C
ATOM   1338  O   GLU A 130     -32.405  -1.456   7.588  1.00 43.07           O
ANISOU 1338  O   GLU A 130     4053   6353   5960    360    875   -750       O
ATOM   1339  CB  GLU A 130     -32.794  -4.635   8.396  1.00 36.71           C
ANISOU 1339  CB  GLU A 130     3196   5786   4966   -129    961   -646       C
ATOM   1340  CG  GLU A 130     -33.801  -3.882   9.250  1.00 41.55           C
ANISOU 1340  CG  GLU A 130     3623   6537   5627    -65   1105   -786       C
ATOM   1341  CD  GLU A 130     -34.219  -4.672  10.472  1.00 48.27           C
ANISOU 1341  CD  GLU A 130     4421   7544   6375   -269   1269   -812       C
ATOM   1342  OE1 GLU A 130     -35.019  -5.612  10.308  1.00 54.60           O
ANISOU 1342  OE1 GLU A 130     5090   8458   7196   -404   1273   -786       O
ATOM   1343  OE2 GLU A 130     -33.799  -4.323  11.596  1.00 55.69           O
ANISOU 1343  OE2 GLU A 130     5457   8493   7211   -299   1388   -856       O
ATOM   1344  H   GLU A 130     -31.197  -5.372   6.711  1.00 45.48           H
ATOM   1345  N  AARG A 131     -30.459  -2.512   7.996  0.58 37.56           N
ANISOU 1345  N  AARG A 131     3664   5536   5070    139    872   -615       N
ATOM   1346  CA AARG A 131     -29.779  -1.307   8.452  0.58 39.78           C
ANISOU 1346  CA AARG A 131     4048   5705   5361    241    908   -667       C
ATOM   1347  C  AARG A 131     -29.431  -0.371   7.298  0.58 40.59           C
ANISOU 1347  C  AARG A 131     4213   5657   5554    401    792   -620       C
ATOM   1348  O  AARG A 131     -29.367   0.847   7.496  0.58 41.86           O
ANISOU 1348  O  AARG A 131     4399   5725   5781    530    809   -683       O
ATOM   1349  CB AARG A 131     -28.527  -1.706   9.237  0.58 38.22           C
ANISOU 1349  CB AARG A 131     4028   5454   5040    112    941   -631       C
ATOM   1350  CG AARG A 131     -27.707  -0.549   9.774  0.58 40.00           C
ANISOU 1350  CG AARG A 131     4370   5562   5268    183    970   -690       C
ATOM   1351  CD AARG A 131     -27.688  -0.609  11.302  0.58 42.39           C
ANISOU 1351  CD AARG A 131     4692   5954   5462     92   1096   -782       C
ATOM   1352  NE AARG A 131     -28.138   0.666  11.838  0.58 47.73           N
ANISOU 1352  NE AARG A 131     5323   6615   6197    222   1172   -930       N
ATOM   1353  CZ AARG A 131     -29.005   0.818  12.832  0.58 51.58           C
ANISOU 1353  CZ AARG A 131     5707   7243   6648    218   1307  -1062       C
ATOM   1354  NH1AARG A 131     -29.499  -0.219  13.492  0.58 51.44           N
ANISOU 1354  NH1AARG A 131     5629   7399   6517     66   1393  -1050       N
ATOM   1355  NH2AARG A 131     -29.394   2.045  13.166  0.58 56.44           N
ANISOU 1355  NH2AARG A 131     6280   7821   7343    369   1362  -1212       N
ATOM   1356  H  AARG A 131     -29.963  -3.214   8.001  0.58 45.08           H
ATOM   1357  HE AARG A 131     -27.817   1.380  11.483  0.58 57.28           H
ATOM   1358 HH11AARG A 131     -29.259  -1.017  13.281  0.58 61.73           H
ATOM   1359 HH12AARG A 131     -30.059  -0.094  14.133  0.58 61.73           H
ATOM   1360 HH21AARG A 131     -29.085   2.725  12.741  0.58 67.73           H
ATOM   1361 HH22AARG A 131     -29.955   2.158  13.808  0.58 67.73           H
ATOM   1362  N  BARG A 131     -30.463  -2.498   8.005  0.42 37.60           N
ANISOU 1362  N  BARG A 131     3669   5542   5076    141    873   -616       N
ATOM   1363  CA BARG A 131     -29.829  -1.260   8.445  0.42 39.78           C
ANISOU 1363  CA BARG A 131     4042   5706   5367    249    909   -671       C
ATOM   1364  C  BARG A 131     -29.457  -0.348   7.281  0.42 40.59           C
ANISOU 1364  C  BARG A 131     4209   5655   5556    406    790   -621       C
ATOM   1365  O  BARG A 131     -29.400   0.875   7.456  0.42 41.88           O
ANISOU 1365  O  BARG A 131     4397   5726   5788    536    806   -683       O
ATOM   1366  CB BARG A 131     -28.598  -1.575   9.296  0.42 38.31           C
ANISOU 1366  CB BARG A 131     4030   5467   5058    125    950   -645       C
ATOM   1367  CG BARG A 131     -28.928  -2.156  10.679  0.42 40.90           C
ANISOU 1367  CG BARG A 131     4329   5934   5277    -13   1081   -702       C
ATOM   1368  CD BARG A 131     -29.765  -3.419  10.555  0.42 39.50           C
ANISOU 1368  CD BARG A 131     4039   5891   5078   -143   1090   -654       C
ATOM   1369  NE BARG A 131     -30.028  -4.133  11.793  0.42 40.92           N
ANISOU 1369  NE BARG A 131     4215   6199   5133   -312   1211   -669       N
ATOM   1370  CZ BARG A 131     -29.087  -4.558  12.625  0.42 42.04           C
ANISOU 1370  CZ BARG A 131     4525   6307   5141   -426   1225   -623       C
ATOM   1371  NH1BARG A 131     -27.816  -4.230  12.457  0.42 41.84           N
ANISOU 1371  NH1BARG A 131     4660   6135   5104   -381   1140   -585       N
ATOM   1372  NH2BARG A 131     -29.430  -5.332  13.652  0.42 44.98           N
ANISOU 1372  NH2BARG A 131     4901   6802   5389   -595   1323   -610       N
ATOM   1373  H  BARG A 131     -29.955  -3.192   8.026  0.42 45.13           H
ATOM   1374  HE BARG A 131     -30.848  -4.290  12.000  0.42 49.10           H
ATOM   1375 HH11BARG A 131     -27.584  -3.731  11.796  0.42 50.22           H
ATOM   1376 HH12BARG A 131     -27.221  -4.517  13.008  0.42 50.22           H
ATOM   1377 HH21BARG A 131     -30.254  -5.550  13.770  0.42 53.98           H
ATOM   1378 HH22BARG A 131     -28.829  -5.614  14.198  0.42 53.98           H
ATOM   1379  N   ALA A 132     -29.237  -0.907   6.088  1.00 39.20           N
ANISOU 1379  N   ALA A 132     4069   5449   5376    392    673   -512       N
ATOM   1380  CA  ALA A 132     -28.753  -0.094   4.977  1.00 38.78           C
ANISOU 1380  CA  ALA A 132     4111   5255   5370    513    569   -440       C
ATOM   1381  C   ALA A 132     -29.857   0.746   4.358  1.00 41.09           C
ANISOU 1381  C   ALA A 132     4283   5550   5781    691    502   -468       C
ATOM   1382  O   ALA A 132     -29.609   1.877   3.928  1.00 42.64           O
ANISOU 1382  O   ALA A 132     4557   5606   6040    823    452   -445       O
ATOM   1383  CB  ALA A 132     -28.100  -0.988   3.913  1.00 38.98           C
ANISOU 1383  CB  ALA A 132     4224   5261   5324    437    477   -325       C
ATOM   1384  H   ALA A 132     -29.378  -1.732   5.894  1.00 47.04           H
ATOM   1385  N   LYS A 133     -31.077   0.228   4.288  1.00 45.67           N
ANISOU 1385  N   LYS A 133     4671   6280   6403    698    489   -515       N
ATOM   1386  CA  LYS A 133     -32.178   1.005   3.741  1.00 50.51           C
ANISOU 1386  CA  LYS A 133     5141   6907   7143    883    409   -552       C
ATOM   1387  C   LYS A 133     -33.038   1.642   4.813  1.00 50.48           C
ANISOU 1387  C   LYS A 133     4975   6972   7233    969    523   -709       C
ATOM   1388  O   LYS A 133     -34.095   2.184   4.499  1.00 56.34           O
ANISOU 1388  O   LYS A 133     5550   7755   8102   1129    466   -767       O
ATOM   1389  CB  LYS A 133     -33.013   0.161   2.777  1.00 50.70           C
ANISOU 1389  CB  LYS A 133     5036   7053   7175    864    290   -511       C
ATOM   1390  CG  LYS A 133     -32.994  -1.341   2.982  1.00 48.93           C
ANISOU 1390  CG  LYS A 133     4780   6951   6860    650    328   -499       C
ATOM   1391  CD  LYS A 133     -33.678  -1.951   1.768  1.00 50.82           C
ANISOU 1391  CD  LYS A 133     4932   7263   7114    657    169   -454       C
ATOM   1392  CE  LYS A 133     -34.109  -3.403   1.924  1.00 51.99           C
ANISOU 1392  CE  LYS A 133     4984   7547   7223    461    186   -471       C
ATOM   1393  NZ  LYS A 133     -35.053  -3.772   0.808  1.00 44.17           N
ANISOU 1393  NZ  LYS A 133     3858   6646   6281    496     21   -466       N
ATOM   1394  H   LYS A 133     -31.288  -0.564   4.550  1.00 54.81           H
ATOM   1395  HZ1 LYS A 133     -35.306  -4.621   0.891  1.00 53.01           H
ATOM   1396  HZ2 LYS A 133     -35.775  -3.252   0.836  1.00 53.01           H
ATOM   1397  HZ3 LYS A 133     -34.651  -3.666   0.021  1.00 53.01           H
ATOM   1398  N   LYS A 134     -32.588   1.624   6.061  1.00 51.89           N
ANISOU 1398  N   LYS A 134     5200   7165   7350    877    677   -785       N
ATOM   1399  CA  LYS A 134     -33.239   2.401   7.110  1.00 54.40           C
ANISOU 1399  CA  LYS A 134     5401   7531   7740    971    801   -953       C
ATOM   1400  C   LYS A 134     -33.184   3.876   6.699  1.00 59.59           C
ANISOU 1400  C   LYS A 134     6117   7997   8527   1200    722   -977       C
ATOM   1401  O   LYS A 134     -32.164   4.338   6.179  1.00 58.22           O
ANISOU 1401  O   LYS A 134     6151   7637   8332   1211    647   -874       O
ATOM   1402  CB  LYS A 134     -32.542   2.159   8.451  1.00 55.91           C
ANISOU 1402  CB  LYS A 134     5690   7750   7803    822    960  -1013       C
ATOM   1403  CG  LYS A 134     -33.471   1.917   9.623  1.00 62.87           C
ANISOU 1403  CG  LYS A 134     6391   8833   8664    773   1132  -1164       C
ATOM   1404  CD  LYS A 134     -32.783   2.278  10.924  1.00 73.01           C
ANISOU 1404  CD  LYS A 134     7803  10097   9840    711   1269  -1256       C
ATOM   1405  CE  LYS A 134     -33.453   1.602  12.106  1.00 77.39           C
ANISOU 1405  CE  LYS A 134     8277  10852  10274    561   1416  -1308       C
ATOM   1406  NZ  LYS A 134     -33.379   2.452  13.328  1.00 85.24           N
ANISOU 1406  NZ  LYS A 134     9350  11830  11209    598   1517  -1429       N
ATOM   1407  OXT LYS A 134     -34.140   4.644   6.837  1.00 67.14           O
ANISOU 1407  OXT LYS A 134     6918   8972   9621   1379    727  -1095       O
ATOM   1408  H   LYS A 134     -31.908   1.171   6.327  1.00 62.27           H
ATOM   1409  HZ1 LYS A 134     -33.786   2.044  14.007  1.00102.29           H
ATOM   1410  HZ2 LYS A 134     -32.529   2.598  13.546  1.00102.29           H
ATOM   1411  HZ3 LYS A 134     -33.778   3.233  13.179  1.00102.29           H
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.