CNRS Nantes University US2B US2B
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***  3096  ***

elNémo ID: 2609071050242286421

Job options:

ID        	=	 2609071050242286421
JOBID     	=	 3096
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:

HEADER 3096

REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX ("2.1_6048": ???)
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) : 1.25    
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.40   
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.00 
REMARK   3   NUMBER OF REFLECTIONS             : 38302     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 38302     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1888
REMARK   3   R VALUE            (WORKING SET) : 0.1874
REMARK   3   FREE R VALUE                     : 0.2141
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.79  
REMARK   3   FREE R VALUE TEST SET COUNT      : 1836      
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   19.40 -    2.94    0.89     2758   105  0.1712 0.1922   0.934  0.904
REMARK   3     2    2.94 -    2.33    0.93     2725   183  0.1810 0.2127   0.922  0.906
REMARK   3     3    2.33 -    2.04    0.95     2788   141  0.1579 0.1894   0.939  0.932
REMARK   3     4    2.04 -    1.85    0.96     2781   168  0.1663 0.2250   0.939  0.872
REMARK   3     5    1.85 -    1.72    0.95     2780   139  0.1757 0.1803   0.933  0.930
REMARK   3     6    1.72 -    1.62    0.97     2837   126  0.1922 0.2011   0.921  0.892
REMARK   3     7    1.62 -    1.54    0.97     2833   137  0.1989 0.2186   0.917  0.889
REMARK   3     8    1.54 -    1.47    0.98     2842   136  0.2263 0.2578   0.902  0.863
REMARK   3     9    1.47 -    1.41    0.98     2875   125  0.2588 0.2774   0.853  0.825
REMARK   3    10    1.41 -    1.36    0.98     2815   155  0.2830 0.2987   0.841  0.815
REMARK   3    11    1.36 -    1.32    0.97     2833   119  0.2991 0.3221   0.805  0.794
REMARK   3    12    1.32 -    1.28    0.97     2783   142  0.3277 0.3341   0.796  0.701
REMARK   3    13    1.28 -    1.25    0.98     2816   160  0.3639 0.4253   0.743  0.731
REMARK   3  
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10    
REMARK   3   SHRINKAGE RADIUS   : 0.90    
REMARK   3   GRID STEP          : 0.60    
REMARK   3  
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.18    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.87   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 16.79   
REMARK   3   Individual atomic B
REMARK   3                  min    max   mean    iso aniso
REMARK   3     Overall:   12.78  80.99  28.31   4.46  1112   953
REMARK   3     Protein:   12.78  80.99  26.78   4.47   949   949
REMARK   3     Water:     15.59  60.71  36.84    N/A   126     0
REMARK   3     Other:     18.54  50.01  38.64    N/A    37     4
REMARK   3     Chain  A:  12.78  80.99  26.78    N/A   949   949
REMARK   3     Chain  K:  18.54  20.07  19.30    N/A     4     4
REMARK   3     Chain  S:  15.59  60.71  36.84    N/A   126     0
REMARK   3     Chain  B:  34.89  50.01  40.99    N/A    33     0
REMARK   3     Histogram:
REMARK   3         Values      Number of atoms
REMARK   3      12.78 - 19.60       250
REMARK   3      19.60 - 26.42       348
REMARK   3      26.42 - 33.25       203
REMARK   3      33.25 - 40.07       149
REMARK   3      40.07 - 46.89        93
REMARK   3      46.89 - 53.71        40
REMARK   3      53.71 - 60.53        17
REMARK   3      60.53 - 67.35         8
REMARK   3      67.35 - 74.17         1
REMARK   3      74.17 - 80.99         3
REMARK   3  
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3  DEVIATIONS FROM IDEAL VALUES - RMSD, RMSZ FOR BONDS AND ANGLES.
REMARK   3    BOND      :  0.010   0.076   1016  Z= 0.447
REMARK   3    ANGLE     :  1.031   5.208   1373  Z= 0.592
REMARK   3    CHIRALITY :  0.090   0.237    147
REMARK   3    PLANARITY :  0.008   0.046    176
REMARK   3    DIHEDRAL  : 14.972  59.639    377
REMARK   3    MIN NONBONDED DISTANCE : 2.269
REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 6.65
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS :  0.00 %
REMARK   3      ALLOWED  :  3.45 %
REMARK   3      FAVORED  : 96.55 %
REMARK   3    ROTAMER:
REMARK   3      OUTLIERS :  0.00 %
REMARK   3      ALLOWED  :  8.49 %
REMARK   3      FAVORED  : 91.51 %
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 VALUES WITH (UNCERTAINTIES):
REMARK   3  INTERPRETATION: POOR |RAMA-Z| > 3; SUSPICIOUS 2 < |RAMA-Z| < 3; GOOD |RAMA-Z| < 2.
REMARK   3  SCORES BELOW ARE SCALED INDEPENDENTLY, SO THEY ARE NOT RELATED IN A SIMPLE WAY.
REMARK   3    WHOLE: -0.15 (0.78), RESIDUES: 132
REMARK   3    HELIX: -1.85 (1.40), RESIDUES: 12
REMARK   3    SHEET: -0.63 (0.78), RESIDUES: 36
REMARK   3    LOOP :  0.60 (0.79), RESIDUES: 84
REMARK   3  
REMARK   3  MAX DEVIATION FROM PLANES:
REMARK   3     TYPE  MAXDEV  MEANDEV LINEINFILE
REMARK   3   ARG   0.012   0.003   ARG A 103 
REMARK   3   TYR   0.017   0.005   TYR A 106 
REMARK   3   PHE   0.024   0.008   PHE A  40 
REMARK   3   TRP   0.023   0.006   TRP A  74 
REMARK   3   HIS   0.008   0.004   HIS A  67 
REMARK   3  
REMARK   3  DETAILS OF BONDING TYPE RMSD
REMARK   3    COVALENT GEOMETRY    : BOND        0.00948 ( 1010)
REMARK   3    COVALENT GEOMETRY    : ANGLE       1.02770 ( 1368)
REMARK   3    SS BOND              : BOND        0.03859 (    1)
REMARK   3    SS BOND              : ANGLE       1.92721 (    2)
REMARK   3    METAL COORDINATION   : BOND        0.05196 (    4)
REMARK   3    METAL COORDINATION   : ANGLE       1.63329 (    3)
REMARK   3    MISC. BOND           : BOND        0.00079 (    1)
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 6     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: chain 'A' and (resid 8 through 28 )
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3047  12.4436   9.6192
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1995 T22:   0.1170                       
REMARK   3      T33:   0.1473 T12:  -0.0321                       
REMARK   3      T13:  -0.0068 T23:  -0.0116                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   6.2920 L22:   5.9111                       
REMARK   3      L33:   5.3072 L12:   0.8173                       
REMARK   3      L13:  -1.4488 L23:  -0.6770                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0668 S12:   0.2409 S13:   0.1132         
REMARK   3      S21:  -0.4138 S22:   0.1149 S23:   0.4013         
REMARK   3      S31:   0.1760 S32:  -0.3789 S33:  -0.1484         
REMARK   3   TLS GROUP : 2     
REMARK   3    SELECTION: chain 'A' and (resid 29 through 44 )
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6010  20.2862  26.8758
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.3567 T22:   0.3256                       
REMARK   3      T33:   0.1783 T12:   0.0383                       
REMARK   3      T13:   0.0284 T23:   0.0162                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   6.2348 L22:   8.6637                       
REMARK   3      L33:   5.1025 L12:   2.6132                       
REMARK   3      L13:  -3.6660 L23:   1.2444                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.3389 S12:   0.0147 S13:  -0.2295         
REMARK   3      S21:  -0.6721 S22:   0.2439 S23:  -0.1977         
REMARK   3      S31:   0.1423 S32:   0.2079 S33:   0.0129         
REMARK   3   TLS GROUP : 3     
REMARK   3    SELECTION: chain 'A' and (resid 45 through 62 )
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8923  11.2213   9.1822
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1636 T22:   0.1173                       
REMARK   3      T33:   0.1711 T12:  -0.0132                       
REMARK   3      T13:  -0.0066 T23:  -0.0165                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   5.3416 L22:   8.8066                       
REMARK   3      L33:   5.0436 L12:   2.2952                       
REMARK   3      L13:   2.7002 L23:   3.9557                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.2535 S12:   0.1857 S13:  -0.4460         
REMARK   3      S21:  -0.1277 S22:   0.0642 S23:  -0.1882         
REMARK   3      S31:   0.4283 S32:   0.0811 S33:  -0.2631         
REMARK   3   TLS GROUP : 4     
REMARK   3    SELECTION: chain 'A' and (resid 63 through 90 )
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2469  23.0676   9.6809
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1258 T22:   0.1614                       
REMARK   3      T33:   0.1598 T12:  -0.0352                       
REMARK   3      T13:   0.0478 T23:  -0.0017                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   2.0113 L22:   2.3049                       
REMARK   3      L33:   8.4541 L12:  -0.7672                       
REMARK   3      L13:  -0.1429 L23:   1.9134                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0278 S12:  -0.0400 S13:   0.1344         
REMARK   3      S21:   0.0179 S22:   0.0206 S23:  -0.0833         
REMARK   3      S31:  -0.3292 S32:   0.2643 S33:  -0.0286         
REMARK   3   TLS GROUP : 5     
REMARK   3    SELECTION: chain 'A' and (resid 91 through 125 )
REMARK   3    ORIGIN FOR THE GROUP (A):  12.6346  10.9526  15.0662
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.1964 T22:   0.1171                       
REMARK   3      T33:   0.1611 T12:   0.0072                       
REMARK   3      T13:   0.0273 T23:   0.0055                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   8.0918 L22:   3.9106                       
REMARK   3      L33:   2.1694 L12:   4.7295                       
REMARK   3      L13:  -0.3378 L23:  -0.4825                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.1570 S12:  -0.3928 S13:  -0.2252         
REMARK   3      S21:   0.0503 S22:  -0.2029 S23:  -0.0385         
REMARK   3      S31:   0.3110 S32:   0.0809 S33:   0.0268         
REMARK   3   TLS GROUP : 6     
REMARK   3    SELECTION: chain 'K'
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5570  26.1215  15.1720
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2410 T22:   0.2638                       
REMARK   3      T33:   0.2116 T12:  -0.0560                       
REMARK   3      T13:   0.0388 T23:  -0.0296                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   2.1952 L22:   2.1819                       
REMARK   3      L33:   2.4003 L12:   0.2904                       
REMARK   3      L13:   1.7227 L23:   1.7271                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0739 S12:  -0.2223 S13:  -0.3658         
REMARK   3      S21:   0.2452 S22:   0.2236 S23:  -0.1528         
REMARK   3      S31:   0.2816 S32:   0.4267 S33:  -0.0399         
REMARK   3
SSBOND   1 CYS A   70    CYS A   85 
LINK         CD  ARG A  52                 O5 BPG4 B   1 
LINK        FE2  FES K 201                 ND1 HIS A  86 
LINK        FE2  FES K 201                 ND1 HIS A  67 
LINK        FE1  FES K 201                 SG  CYS A  83 
LINK        FE1  FES K 201                 SG  CYS A  65 
CRYST1   46.800  108.510  113.050  90.00  90.00  90.00 F 2 2 2
SCALE1      0.021368  0.000000  0.000000        0.00000
SCALE2      0.000000  0.009216  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008846        0.00000
ATOM      1  N   ALA A   8       5.987   5.676  25.696  1.00 48.54           N
ANISOU    1  N   ALA A   8     7200   7058   4186   -470    156   1378       N
ATOM      2  CA  ALA A   8       5.086   5.907  26.798  1.00 48.19           C
ANISOU    2  CA  ALA A   8     7224   7174   3910   -560    361   1350       C
ATOM      3  C   ALA A   8       3.965   6.934  26.540  1.00 46.13           C
ANISOU    3  C   ALA A   8     6869   6935   3721   -682    609   1043       C
ATOM      4  O   ALA A   8       3.014   6.983  27.325  1.00 46.16           O
ANISOU    4  O   ALA A   8     6898   7023   3619   -739    836   1053       O
ATOM      5  CB  ALA A   8       5.899   6.247  28.126  1.00 37.34           C
ANISOU    5  CB  ALA A   8     5934   6123   2130   -517    210   1343       C
ATOM      6  HA  ALA A   8       4.608   5.072  26.928  1.00 57.83           H
ATOM      7  HB1 ALA A   8       5.271   6.410  28.848  1.00 44.75           H
ATOM      8  HB2 ALA A   8       6.470   5.495  28.348  1.00 44.75           H
ATOM      9  HB3 ALA A   8       6.439   7.038  27.972  1.00 44.75           H
ATOM     10  N   ASP A   9       4.021   7.728  25.463  1.00 40.54           N
ANISOU   10  N   ASP A   9     6052   6139   3212   -702    591    790       N
ATOM     11  CA  ASP A   9       2.847   8.522  25.093  1.00 36.58           C
ANISOU   11  CA  ASP A   9     5439   5584   2875   -773    833    564       C
ATOM     12  C   ASP A   9       2.855   8.806  23.598  1.00 33.08           C
ANISOU   12  C   ASP A   9     4875   4901   2794   -734    763    430       C
ATOM     13  O   ASP A   9       3.460   9.785  23.148  1.00 30.89           O
ANISOU   13  O   ASP A   9     4548   4622   2566   -674    680    193       O
ATOM     14  CB  ASP A   9       2.699   9.808  25.901  1.00 48.89           C
ANISOU   14  CB  ASP A   9     6987   7327   4263   -763    948    266       C
ATOM     15  CG  ASP A   9       1.306  10.421  25.762  1.00 54.49           C
ANISOU   15  CG  ASP A   9     7562   7974   5168   -780   1237    126       C
ATOM     16  OD1 ASP A   9       0.343   9.658  25.536  1.00 57.44           O
ANISOU   16  OD1 ASP A   9     7851   8266   5707   -831   1364    316       O
ATOM     17  OD2 ASP A   9       1.172  11.660  25.863  1.00 60.91           O
ANISOU   17  OD2 ASP A   9     8333   8797   6013   -737   1328   -163       O
ATOM     18  H   ASP A   9       4.705   7.820  24.950  1.00 48.66           H
ATOM     19  HA  ASP A   9       2.080   7.959  25.283  1.00 43.90           H
ATOM     20  HB2 ASP A   9       2.852   9.614  26.839  1.00 58.68           H
ATOM     21  HB3 ASP A   9       3.348  10.457  25.586  1.00 58.68           H
ATOM     22  N   PHE A  10       2.138   7.982  22.852  1.00 30.92           N
ANISOU   22  N   PHE A  10     4544   4409   2795   -769    789    568       N
ATOM     23  CA  PHE A  10       2.056   8.129  21.413  1.00 25.99           C
ANISOU   23  CA  PHE A  10     3814   3566   2496   -725    690    452       C
ATOM     24  C   PHE A  10       0.972   9.129  21.029  1.00 24.51           C
ANISOU   24  C   PHE A  10     3447   3398   2469   -744    837    276       C
ATOM     25  O   PHE A  10      -0.138   9.106  21.567  1.00 30.92           O
ANISOU   25  O   PHE A  10     4163   4289   3296   -828   1042    321       O
ATOM     26  CB  PHE A  10       1.724   6.775  20.784  1.00 27.52           C
ANISOU   26  CB  PHE A  10     4041   3522   2894   -791    638    642       C
ATOM     27  CG  PHE A  10       2.914   5.870  20.570  1.00 28.28           C
ANISOU   27  CG  PHE A  10     4283   3469   2991   -690    469    769       C
ATOM     28  CD1 PHE A  10       3.814   6.120  19.561  1.00 29.83           C
ANISOU   28  CD1 PHE A  10     4472   3568   3296   -568    326    628       C
ATOM     29  CD2 PHE A  10       3.101   4.736  21.348  1.00 34.41           C
ANISOU   29  CD2 PHE A  10     5199   4187   3688   -703    481   1059       C
ATOM     30  CE1 PHE A  10       4.886   5.284  19.331  1.00 29.69           C
ANISOU   30  CE1 PHE A  10     4548   3404   3328   -442    216    735       C
ATOM     31  CE2 PHE A  10       4.185   3.892  21.124  1.00 33.08           C
ANISOU   31  CE2 PHE A  10     5139   3846   3585   -558    341   1197       C
ATOM     32  CZ  PHE A  10       5.073   4.165  20.116  1.00 33.32           C
ANISOU   32  CZ  PHE A  10     5127   3786   3747   -419    218   1020       C
ATOM     33  H   PHE A  10       1.683   7.321  23.161  1.00 37.12           H
ATOM     34  HA  PHE A  10       2.906   8.451  21.072  1.00 31.20           H
ATOM     35  HB2 PHE A  10       1.104   6.309  21.366  1.00 33.04           H
ATOM     36  HB3 PHE A  10       1.315   6.929  19.919  1.00 33.04           H
ATOM     37  HD1 PHE A  10       3.697   6.869  19.023  1.00 35.81           H
ATOM     38  HD2 PHE A  10       2.497   4.538  22.027  1.00 41.31           H
ATOM     39  HE1 PHE A  10       5.484   5.476  18.645  1.00 35.64           H
ATOM     40  HE2 PHE A  10       4.307   3.142  21.659  1.00 39.71           H
ATOM     41  HZ  PHE A  10       5.796   3.600  19.963  1.00 39.99           H
ATOM     42  N   ILE A  11       1.314  10.011  20.095  1.00 24.54           N
ANISOU   42  N   ILE A  11     3389   3327   2607   -652    745    101       N
ATOM     43  CA  ILE A  11       0.451  11.077  19.603  1.00 24.10           C
ANISOU   43  CA  ILE A  11     3162   3255   2738   -608    845    -33       C
ATOM     44  C   ILE A  11       0.297  10.898  18.101  1.00 19.84           C
ANISOU   44  C   ILE A  11     2551   2561   2425   -589    670     -7       C
ATOM     45  O   ILE A  11       1.295  10.794  17.381  1.00 20.29           O
ANISOU   45  O   ILE A  11     2716   2531   2462   -542    513    -35       O
ATOM     46  CB  ILE A  11       1.052  12.467  19.904  1.00 27.63           C
ANISOU   46  CB  ILE A  11     3645   3740   3112   -519    909   -253       C
ATOM     47  CG1 ILE A  11       1.235  12.672  21.404  1.00 31.11           C
ANISOU   47  CG1 ILE A  11     4195   4372   3255   -571   1065   -334       C
ATOM     48  CG2 ILE A  11       0.174  13.553  19.276  1.00 30.76           C
ANISOU   48  CG2 ILE A  11     3871   4047   3768   -424   1014   -343       C
ATOM     49  CD1 ILE A  11      -0.038  12.662  22.175  1.00 47.08           C
ANISOU   49  CD1 ILE A  11     6127   6496   5263   -611   1344   -313       C
ATOM     50  H   ILE A  11       2.083  10.011  19.711  1.00 29.46           H
ATOM     51  HA  ILE A  11      -0.420  11.008  20.024  1.00 28.93           H
ATOM     52  HB  ILE A  11       1.935  12.523  19.506  1.00 33.16           H
ATOM     53 HG12 ILE A  11       1.796  11.960  21.749  1.00 37.35           H
ATOM     54 HG13 ILE A  11       1.662  13.531  21.551  1.00 37.35           H
ATOM     55 HG21 ILE A  11       0.396  14.409  19.675  1.00 36.92           H
ATOM     56 HG22 ILE A  11       0.339  13.580  18.321  1.00 36.92           H
ATOM     57 HG23 ILE A  11      -0.758  13.341  19.444  1.00 36.92           H
ATOM     58 HD11 ILE A  11       0.159  12.817  23.112  1.00 56.50           H
ATOM     59 HD12 ILE A  11      -0.618  13.363  21.838  1.00 56.50           H
ATOM     60 HD13 ILE A  11      -0.466  11.798  22.067  1.00 56.50           H
ATOM     61  N   GLY A  12      -0.946  10.865  17.626  1.00 23.78           N
ANISOU   61  N   GLY A  12     2856   3058   3123   -631    696     45       N
ATOM     62  CA  GLY A  12      -1.171  10.774  16.192  1.00 22.52           C
ANISOU   62  CA  GLY A  12     2632   2808   3117   -633    496     61       C
ATOM     63  C   GLY A  12      -0.883  12.105  15.522  1.00 23.22           C
ANISOU   63  C   GLY A  12     2691   2868   3264   -473    466    -24       C
ATOM     64  O   GLY A  12      -1.263  13.165  16.020  1.00 25.40           O
ANISOU   64  O   GLY A  12     2863   3173   3615   -369    629    -80       O
ATOM     65  H   GLY A  12      -1.660  10.892  18.105  1.00 28.55           H
ATOM     66  HA2 GLY A  12      -0.589  10.099  15.811  1.00 27.04           H
ATOM     67  HA3 GLY A  12      -2.094  10.530  16.020  1.00 27.04           H
ATOM     68  N   ILE A  13      -0.190  12.054  14.378  1.00 19.97           N
ANISOU   68  N   ILE A  13     2392   2375   2821   -451    289    -32       N
ATOM     69  CA  ILE A  13       0.225  13.280  13.691  1.00 20.22           C
ANISOU   69  CA  ILE A  13     2437   2353   2891   -315    274    -68       C
ATOM     70  C   ILE A  13      -0.210  13.305  12.238  1.00 25.07           C
ANISOU   70  C   ILE A  13     3009   2965   3551   -310     80     23       C
ATOM     71  O   ILE A  13       0.164  14.226  11.499  1.00 28.04           O
ANISOU   71  O   ILE A  13     3430   3289   3936   -205     55     50       O
ATOM     72  CB  ILE A  13       1.742  13.524  13.822  1.00 22.53           C
ANISOU   72  CB  ILE A  13     2921   2587   3052   -286    299   -164       C
ATOM     73  CG1 ILE A  13       2.547  12.378  13.207  1.00 23.02           C
ANISOU   73  CG1 ILE A  13     3127   2616   3002   -345    174   -152       C
ATOM     74  CG2 ILE A  13       2.098  13.769  15.278  1.00 21.79           C
ANISOU   74  CG2 ILE A  13     2850   2549   2880   -296    452   -261       C
ATOM     75  CD1 ILE A  13       4.020  12.740  13.023  1.00 29.91           C
ANISOU   75  CD1 ILE A  13     4110   3452   3804   -293    194   -221       C
ATOM     76  H   ILE A  13       0.048  11.327  13.984  1.00 23.98           H
ATOM     77  HA  ILE A  13      -0.247  14.008  14.125  1.00 24.27           H
ATOM     78  HB  ILE A  13       1.977  14.319  13.317  1.00 27.05           H
ATOM     79 HG12 ILE A  13       2.496  11.605  13.790  1.00 27.63           H
ATOM     80 HG13 ILE A  13       2.178  12.162  12.336  1.00 27.63           H
ATOM     81 HG21 ILE A  13       3.039  13.997  15.339  1.00 26.16           H
ATOM     82 HG22 ILE A  13       1.558  14.501  15.616  1.00 26.16           H
ATOM     83 HG23 ILE A  13       1.919  12.963  15.787  1.00 26.16           H
ATOM     84 HD11 ILE A  13       4.469  12.013  12.565  1.00 35.91           H
ATOM     85 HD12 ILE A  13       4.082  13.552  12.496  1.00 35.91           H
ATOM     86 HD13 ILE A  13       4.421  12.881  13.895  1.00 35.91           H
ATOM     87  N   GLY A  14      -1.018  12.335  11.817  1.00 24.26           N
ANISOU   87  N   GLY A  14     2828   2925   3466   -442    -61     77       N
ATOM     88  CA  GLY A  14      -1.523  12.304  10.460  1.00 24.81           C
ANISOU   88  CA  GLY A  14     2855   3053   3520   -476   -292    149       C
ATOM     89  C   GLY A  14      -1.559  10.912   9.867  1.00 24.50           C
ANISOU   89  C   GLY A  14     2932   3007   3369   -686   -453     86       C
ATOM     90  O   GLY A  14      -1.091   9.958  10.487  1.00 25.50           O
ANISOU   90  O   GLY A  14     3190   3034   3465   -775   -364     13       O
ATOM     91  H   GLY A  14      -1.286  11.681  12.306  1.00 29.13           H
ATOM     92  HA2 GLY A  14      -2.426  12.660  10.449  1.00 29.79           H
ATOM     93  HA3 GLY A  14      -0.959  12.858   9.898  1.00 29.79           H
ATOM     94  N   LYS A  15      -2.144  10.760   8.685  1.00 23.29           N
ANISOU   94  N   LYS A  15     2743   2953   3154   -776   -694    117       N
ATOM     95  CA  LYS A  15      -2.174   9.473   8.010  1.00 24.93           C
ANISOU   95  CA  LYS A  15     3105   3129   3237  -1009   -847     -5       C
ATOM     96  C   LYS A  15      -0.894   9.254   7.214  1.00 25.49           C
ANISOU   96  C   LYS A  15     3523   3097   3065   -967   -823   -130       C
ATOM     97  O   LYS A  15      -0.293  10.196   6.683  1.00 24.99           O
ANISOU   97  O   LYS A  15     3534   3073   2890   -808   -799    -76       O
ATOM     98  CB  LYS A  15      -3.346   9.405   7.038  1.00 31.38           C
ANISOU   98  CB  LYS A  15     3738   4143   4039  -1162  -1151     46       C
ATOM     99  CG  LYS A  15      -4.716   9.384   7.680  1.00 38.66           C
ANISOU   99  CG  LYS A  15     4256   5192   5240  -1251  -1190    158       C
ATOM    100  CD  LYS A  15      -5.823   9.400   6.631  1.00 49.76           C
ANISOU  100  CD  LYS A  15     5424   6849   6632  -1396  -1553    230       C
ATOM    101  CE  LYS A  15      -5.638   8.327   5.554  1.00 48.93           C
ANISOU  101  CE  LYS A  15     5619   6711   6260  -1584  -1685     12       C
ATOM    102  NZ  LYS A  15      -6.723   8.370   4.533  1.00 48.49           N
ANISOU  102  NZ  LYS A  15     5366   6912   6146  -1659  -1976     50       N
ATOM    103  H   LYS A  15      -2.533  11.393   8.251  1.00 27.96           H
ATOM    104  HA  LYS A  15      -2.266   8.774   8.677  1.00 29.92           H
ATOM    105  HB2 LYS A  15      -3.309  10.182   6.459  1.00 37.66           H
ATOM    106  HB3 LYS A  15      -3.261   8.595   6.511  1.00 37.66           H
ATOM    107  HG2 LYS A  15      -4.810   8.578   8.211  1.00 46.40           H
ATOM    108  HG3 LYS A  15      -4.818  10.167   8.244  1.00 46.40           H
ATOM    109  HD2 LYS A  15      -6.674   9.243   7.068  1.00 59.72           H
ATOM    110  HD3 LYS A  15      -5.830  10.266   6.193  1.00 59.72           H
ATOM    111  HE2 LYS A  15      -4.792   8.469   5.103  1.00 58.72           H
ATOM    112  HE3 LYS A  15      -5.650   7.451   5.971  1.00 58.72           H
ATOM    113  HZ1 LYS A  15      -6.775   9.185   4.178  1.00 58.20           H
ATOM    114  HZ2 LYS A  15      -6.555   7.783   3.885  1.00 58.20           H
ATOM    115  HZ3 LYS A  15      -7.504   8.169   4.910  1.00 58.20           H
ATOM    116  N   LEU A  16      -0.516   7.980   7.061  1.00 26.17           N
ANISOU  116  N   LEU A  16     3821   3034   3087  -1118   -812   -295       N
ATOM    117  CA  LEU A  16       0.735   7.693   6.368  1.00 27.17           C
ANISOU  117  CA  LEU A  16     4257   3049   3018  -1051   -725   -434       C
ATOM    118  C   LEU A  16       0.730   8.301   4.970  1.00 31.21           C
ANISOU  118  C   LEU A  16     4867   3728   3264  -1049   -873   -438       C
ATOM    119  O   LEU A  16       1.750   8.824   4.520  1.00 29.48           O
ANISOU  119  O   LEU A  16     4799   3501   2903   -905   -745   -441       O
ATOM    120  CB  LEU A  16       0.951   6.179   6.293  1.00 30.20           C
ANISOU  120  CB  LEU A  16     4766   3259   3448  -1108   -632   -578       C
ATOM    121  CG  LEU A  16       2.188   5.701   5.532  1.00 32.80           C
ANISOU  121  CG  LEU A  16     5324   3490   3650   -985   -487   -713       C
ATOM    122  CD1 LEU A  16       3.443   5.980   6.292  1.00 34.79           C
ANISOU  122  CD1 LEU A  16     5593   3651   3976   -778   -287   -657       C
ATOM    123  CD2 LEU A  16       2.070   4.199   5.264  1.00 39.05           C
ANISOU  123  CD2 LEU A  16     6216   4109   4513  -1080   -458   -868       C
ATOM    124  H   LEU A  16      -0.952   7.293   7.339  1.00 31.41           H
ATOM    125  HA  LEU A  16       1.473   8.079   6.866  1.00 32.62           H
ATOM    126  HB2 LEU A  16       1.027   5.842   7.200  1.00 36.25           H
ATOM    127  HB3 LEU A  16       0.179   5.787   5.857  1.00 36.25           H
ATOM    128  HG  LEU A  16       2.242   6.182   4.691  1.00 39.38           H
ATOM    129 HD11 LEU A  16       4.203   5.683   5.767  1.00 41.76           H
ATOM    130 HD12 LEU A  16       3.507   6.934   6.457  1.00 41.76           H
ATOM    131 HD13 LEU A  16       3.416   5.500   7.135  1.00 41.76           H
ATOM    132 HD21 LEU A  16       2.809   3.919   4.703  1.00 46.88           H
ATOM    133 HD22 LEU A  16       2.098   3.725   6.110  1.00 46.88           H
ATOM    134 HD23 LEU A  16       1.228   4.024   4.815  1.00 46.88           H
ATOM    135  N   ASP A  17      -0.416   8.254   4.281  1.00 32.14           N
ANISOU  135  N   ASP A  17     4862   4026   3322  -1193  -1123   -405       N
ATOM    136  CA  ASP A  17      -0.480   8.769   2.911  1.00 32.28           C
ANISOU  136  CA  ASP A  17     4973   4242   3050  -1179  -1276   -367       C
ATOM    137  C   ASP A  17      -0.560  10.295   2.850  1.00 38.65           C
ANISOU  137  C   ASP A  17     5656   5192   3837  -1005  -1346    -92       C
ATOM    138  O   ASP A  17      -0.512  10.860   1.751  1.00 41.50           O
ANISOU  138  O   ASP A  17     6129   5718   3921   -977  -1473     10       O
ATOM    139  CB  ASP A  17      -1.581   8.098   2.081  1.00 46.55           C
ANISOU  139  CB  ASP A  17     6696   6205   4786  -1361  -1507   -439       C
ATOM    140  CG  ASP A  17      -2.861   7.851   2.849  1.00 58.55           C
ANISOU  140  CG  ASP A  17     7878   7775   6592  -1489  -1642   -369       C
ATOM    141  OD1 ASP A  17      -2.831   7.220   3.928  1.00 45.01           O
ANISOU  141  OD1 ASP A  17     6113   5868   5119  -1534  -1480   -423       O
ATOM    142  OD2 ASP A  17      -3.919   8.257   2.340  1.00 66.47           O
ANISOU  142  OD2 ASP A  17     8650   9022   7583  -1534  -1898   -246       O
ATOM    143  H   ASP A  17      -1.157   7.935   4.580  1.00 38.57           H
ATOM    144  HA  ASP A  17       0.339   8.513   2.460  1.00 38.75           H
ATOM    145  HB2 ASP A  17      -1.794   8.668   1.326  1.00 55.87           H
ATOM    146  HB3 ASP A  17      -1.256   7.240   1.766  1.00 55.87           H
ATOM    147  N   ASP A  18      -0.691  10.980   3.983  1.00 35.27           N
ANISOU  147  N   ASP A  18     4989   4688   3723   -845  -1202     46       N
ATOM    148  CA  ASP A  18      -0.498  12.425   3.985  1.00 31.22           C
ANISOU  148  CA  ASP A  18     4395   4191   3277   -611  -1124    272       C
ATOM    149  C   ASP A  18       0.962  12.826   3.754  1.00 29.73           C
ANISOU  149  C   ASP A  18     4465   3876   2956   -507   -882    230       C
ATOM    150  O   ASP A  18       1.226  14.016   3.549  1.00 33.34           O
ANISOU  150  O   ASP A  18     4912   4316   3440   -355   -808    415       O
ATOM    151  CB  ASP A  18      -0.908  13.043   5.336  1.00 36.85           C
ANISOU  151  CB  ASP A  18     4832   4815   4355   -478   -971    354       C
ATOM    152  CG  ASP A  18      -2.387  12.886   5.654  1.00 44.94           C
ANISOU  152  CG  ASP A  18     5515   5976   5583   -537  -1142    443       C
ATOM    153  OD1 ASP A  18      -3.201  12.672   4.726  1.00 38.44           O
ANISOU  153  OD1 ASP A  18     4602   5353   4651   -643  -1443    521       O
ATOM    154  OD2 ASP A  18      -2.736  12.994   6.860  1.00 40.94           O
ANISOU  154  OD2 ASP A  18     4814   5403   5339   -487   -969    435       O
ATOM    155  H   ASP A  18      -0.887  10.638   4.748  1.00 42.33           H
ATOM    156  HA  ASP A  18      -1.064  12.781   3.283  1.00 37.48           H
ATOM    157  HB2 ASP A  18      -0.405  12.610   6.044  1.00 44.23           H
ATOM    158  HB3 ASP A  18      -0.708  13.992   5.319  1.00 44.23           H
ATOM    159  N   PHE A  19       1.918  11.895   3.819  1.00 25.84           N
ANISOU  159  N   PHE A  19     4176   3274   2368   -576   -735      7       N
ATOM    160  CA  PHE A  19       3.348  12.228   3.814  1.00 23.20           C
ANISOU  160  CA  PHE A  19     3993   2830   1993   -472   -473    -37       C
ATOM    161  C   PHE A  19       3.961  11.761   2.503  1.00 28.01           C
ANISOU  161  C   PHE A  19     4886   3500   2255   -537   -449   -140       C
ATOM    162  O   PHE A  19       3.817  10.573   2.162  1.00 32.72           O
ANISOU  162  O   PHE A  19     5623   4086   2724   -669   -514   -346       O
ATOM    163  CB  PHE A  19       4.055  11.582   5.010  1.00 23.84           C
ANISOU  163  CB  PHE A  19     4034   2754   2270   -447   -297   -181       C
ATOM    164  CG  PHE A  19       3.588  12.141   6.321  1.00 20.76           C
ANISOU  164  CG  PHE A  19     3411   2331   2144   -388   -272    -99       C
ATOM    165  CD1 PHE A  19       4.070  13.361   6.783  1.00 20.87           C
ANISOU  165  CD1 PHE A  19     3348   2304   2277   -276   -137    -19       C
ATOM    166  CD2 PHE A  19       2.614  11.502   7.064  1.00 22.22           C
ANISOU  166  CD2 PHE A  19     3463   2524   2454   -467   -361   -113       C
ATOM    167  CE1 PHE A  19       3.593  13.922   7.977  1.00 20.41           C
ANISOU  167  CE1 PHE A  19     3111   2215   2428   -230    -87      7       C
ATOM    168  CE2 PHE A  19       2.165  12.041   8.269  1.00 21.40           C
ANISOU  168  CE2 PHE A  19     3164   2415   2552   -412   -289    -53       C
ATOM    169  CZ  PHE A  19       2.645  13.253   8.706  1.00 20.69           C
ANISOU  169  CZ  PHE A  19     3026   2289   2546   -287   -153    -11       C
ATOM    170  H   PHE A  19       1.763  11.051   3.868  1.00 31.02           H
ATOM    171  HA  PHE A  19       3.462  13.189   3.883  1.00 27.85           H
ATOM    172  HB2 PHE A  19       3.875  10.629   5.008  1.00 28.62           H
ATOM    173  HB3 PHE A  19       5.009  11.740   4.938  1.00 28.62           H
ATOM    174  HD1 PHE A  19       4.719  13.812   6.292  1.00 25.05           H
ATOM    175  HD2 PHE A  19       2.253  10.702   6.756  1.00 26.67           H
ATOM    176  HE1 PHE A  19       3.919  14.742   8.273  1.00 24.50           H
ATOM    177  HE2 PHE A  19       1.540  11.579   8.779  1.00 25.69           H
ATOM    178  HZ  PHE A  19       2.324  13.620   9.498  1.00 24.84           H
ATOM    179  N   PRO A  20       4.560  12.626   1.673  1.00 31.33           N
ANISOU  179  N   PRO A  20     5426   3983   2495   -471   -350    -11       N
ATOM    180  CA  PRO A  20       5.118  12.132   0.404  1.00 31.33           C
ANISOU  180  CA  PRO A  20     5698   4072   2132   -537   -282   -127       C
ATOM    181  C   PRO A  20       6.435  11.403   0.605  1.00 35.49           C
ANISOU  181  C   PRO A  20     6265   4451   2769   -480     24   -341       C
ATOM    182  O   PRO A  20       7.248  11.758   1.458  1.00 34.29           O
ANISOU  182  O   PRO A  20     6032   4182   2815   -391    215   -328       O
ATOM    183  CB  PRO A  20       5.306  13.403  -0.449  1.00 37.52           C
ANISOU  183  CB  PRO A  20     6546   4970   2739   -470   -243    151       C
ATOM    184  CG  PRO A  20       4.444  14.431   0.203  1.00 41.96           C
ANISOU  184  CG  PRO A  20     6886   5507   3549   -386   -400    419       C
ATOM    185  CD  PRO A  20       4.480  14.100   1.682  1.00 35.93           C
ANISOU  185  CD  PRO A  20     5903   4568   3180   -353   -324    272       C
ATOM    186  HA  PRO A  20       4.482  11.543  -0.033  1.00 37.60           H
ATOM    187  HB2 PRO A  20       6.237  13.673  -0.439  1.00 45.03           H
ATOM    188  HB3 PRO A  20       5.019  13.235  -1.360  1.00 45.03           H
ATOM    189  HG2 PRO A  20       4.805  15.317   0.038  1.00 50.36           H
ATOM    190  HG3 PRO A  20       3.540  14.372  -0.143  1.00 50.36           H
ATOM    191  HD2 PRO A  20       5.260  14.489   2.108  1.00 43.13           H
ATOM    192  HD3 PRO A  20       3.673  14.402   2.127  1.00 43.13           H
ATOM    193  N   VAL A  21       6.635  10.356  -0.199  1.00 33.74           N
ANISOU  193  N   VAL A  21     6142   4245   2431   -524     60   -533       N
ATOM    194  CA  VAL A  21       7.856   9.573  -0.099  1.00 33.26           C
ANISOU  194  CA  VAL A  21     6088   4048   2500   -436    329   -701       C
ATOM    195  C   VAL A  21       9.054  10.460  -0.385  1.00 34.20           C
ANISOU  195  C   VAL A  21     6199   4200   2594   -341    591   -603       C
ATOM    196  O   VAL A  21       9.109  11.144  -1.412  1.00 36.05           O
ANISOU  196  O   VAL A  21     6542   4583   2573   -369    625   -498       O
ATOM    197  CB  VAL A  21       7.783   8.363  -1.047  1.00 34.51           C
ANISOU  197  CB  VAL A  21     6395   4213   2505   -498    329   -925       C
ATOM    198  CG1 VAL A  21       9.140   7.725  -1.182  1.00 43.26           C
ANISOU  198  CG1 VAL A  21     7521   5207   3708   -372    630  -1064       C
ATOM    199  CG2 VAL A  21       6.756   7.390  -0.547  1.00 38.04           C
ANISOU  199  CG2 VAL A  21     6807   4568   3076   -603    123  -1030       C
ATOM    200  H   VAL A  21       6.084  10.086  -0.802  1.00 40.50           H
ATOM    201  HA  VAL A  21       7.951   9.237   0.806  1.00 39.92           H
ATOM    202  HB  VAL A  21       7.512   8.651  -1.933  1.00 41.42           H
ATOM    203 HG11 VAL A  21       9.034   6.830  -1.542  1.00 51.92           H
ATOM    204 HG12 VAL A  21       9.683   8.260  -1.781  1.00 51.92           H
ATOM    205 HG13 VAL A  21       9.557   7.682  -0.307  1.00 51.92           H
ATOM    206 HG21 VAL A  21       6.722   6.630  -1.147  1.00 45.65           H
ATOM    207 HG22 VAL A  21       7.006   7.098   0.344  1.00 45.65           H
ATOM    208 HG23 VAL A  21       5.891   7.829  -0.520  1.00 45.65           H
ATOM    209  N   GLY A  22      10.006  10.480   0.545  1.00 32.03           N
ANISOU  209  N   GLY A  22     5769   3806   2596   -238    767   -611       N
ATOM    210  CA  GLY A  22      11.257  11.180   0.351  1.00 32.76           C
ANISOU  210  CA  GLY A  22     5789   3923   2737   -171   1035   -544       C
ATOM    211  C   GLY A  22      11.223  12.676   0.554  1.00 34.10           C
ANISOU  211  C   GLY A  22     5911   4128   2917   -202   1066   -322       C
ATOM    212  O   GLY A  22      12.251  13.338   0.347  1.00 39.44           O
ANISOU  212  O   GLY A  22     6505   4819   3661   -186   1296   -250       O
ATOM    213  H   GLY A  22       9.944  10.087   1.308  1.00 38.45           H
ATOM    214  HA2 GLY A  22      11.909  10.818   0.971  1.00 39.33           H
ATOM    215  HA3 GLY A  22      11.560  11.017  -0.556  1.00 39.33           H
ATOM    216  N   ILE A  23      10.089  13.229   0.954  1.00 30.82           N
ANISOU  216  N   ILE A  23     5529   3714   2469   -249    854   -200       N
ATOM    217  CA  ILE A  23       9.941  14.673   1.063  1.00 32.50           C
ANISOU  217  CA  ILE A  23     5702   3914   2733   -262    875     53       C
ATOM    218  C   ILE A  23       9.595  15.023   2.500  1.00 24.28           C
ANISOU  218  C   ILE A  23     4413   2757   2057   -232    756     58       C
ATOM    219  O   ILE A  23       8.481  14.727   2.948  1.00 25.40           O
ANISOU  219  O   ILE A  23     4515   2901   2235   -231    520     53       O
ATOM    220  CB  ILE A  23       8.858  15.180   0.097  1.00 32.18           C
ANISOU  220  CB  ILE A  23     5824   3989   2416   -296    671    263       C
ATOM    221  CG1 ILE A  23       9.259  14.802  -1.327  1.00 33.62           C
ANISOU  221  CG1 ILE A  23     6143   4329   2301   -323    740    218       C
ATOM    222  CG2 ILE A  23       8.643  16.673   0.274  1.00 36.34           C
ANISOU  222  CG2 ILE A  23     6266   4426   3117   -261    679    562       C
ATOM    223  CD1 ILE A  23       8.458  15.479  -2.394  1.00 38.57           C
ANISOU  223  CD1 ILE A  23     6879   5124   2653   -343    566    470       C
ATOM    224  H   ILE A  23       9.385  12.786   1.171  1.00 37.00           H
ATOM    225  HA  ILE A  23      10.782  15.101   0.840  1.00 39.01           H
ATOM    226  HB  ILE A  23       8.006  14.759   0.293  1.00 38.63           H
ATOM    227 HG12 ILE A  23      10.189  15.043  -1.461  1.00 40.35           H
ATOM    228 HG13 ILE A  23       9.145  13.845  -1.437  1.00 40.35           H
ATOM    229 HG21 ILE A  23       7.974  16.973  -0.361  1.00 43.63           H
ATOM    230 HG22 ILE A  23       8.340  16.843   1.179  1.00 43.63           H
ATOM    231 HG23 ILE A  23       9.482  17.134   0.113  1.00 43.63           H
ATOM    232 HD11 ILE A  23       8.636  15.046  -3.244  1.00 46.30           H
ATOM    233 HD12 ILE A  23       7.516  15.406  -2.175  1.00 46.30           H
ATOM    234 HD13 ILE A  23       8.716  16.413  -2.437  1.00 46.30           H
ATOM    235  N   PRO A  24      10.513  15.625   3.257  1.00 23.56           N
ANISOU  235  N   PRO A  24     4147   2582   2224   -231    918     50       N
ATOM    236  CA  PRO A  24      10.202  15.956   4.652  1.00 23.44           C
ANISOU  236  CA  PRO A  24     3936   2483   2486   -224    813     13       C
ATOM    237  C   PRO A  24       9.042  16.938   4.744  1.00 20.25           C
ANISOU  237  C   PRO A  24     3536   2011   2147   -210    685    176       C
ATOM    238  O   PRO A  24       8.941  17.872   3.940  1.00 22.96           O
ANISOU  238  O   PRO A  24     3971   2311   2441   -210    743    374       O
ATOM    239  CB  PRO A  24      11.511  16.578   5.161  1.00 22.47           C
ANISOU  239  CB  PRO A  24     3654   2317   2568   -274   1010    -28       C
ATOM    240  CG  PRO A  24      12.566  15.987   4.310  1.00 24.65           C
ANISOU  240  CG  PRO A  24     3966   2674   2726   -263   1209    -72       C
ATOM    241  CD  PRO A  24      11.928  15.907   2.937  1.00 25.92           C
ANISOU  241  CD  PRO A  24     4396   2887   2567   -256   1208     37       C
ATOM    242  HA  PRO A  24       9.994  15.157   5.162  1.00 28.14           H
ATOM    243  HB2 PRO A  24      11.481  17.542   5.060  1.00 26.98           H
ATOM    244  HB3 PRO A  24      11.647  16.347   6.094  1.00 26.98           H
ATOM    245  HG2 PRO A  24      13.348  16.562   4.299  1.00 29.59           H
ATOM    246  HG3 PRO A  24      12.806  15.106   4.637  1.00 29.59           H
ATOM    247  HD2 PRO A  24      12.016  16.748   2.462  1.00 31.12           H
ATOM    248  HD3 PRO A  24      12.316  15.188   2.414  1.00 31.12           H
ATOM    249  N   LYS A  25       8.141  16.691   5.706  1.00 19.33           N
ANISOU  249  N   LYS A  25     3316   1882   2146   -183    528    118       N
ATOM    250  CA  LYS A  25       7.023  17.590   5.968  1.00 20.96           C
ANISOU  250  CA  LYS A  25     3466   2013   2485   -129    443    250       C
ATOM    251  C   LYS A  25       6.995  17.916   7.447  1.00 19.72           C
ANISOU  251  C   LYS A  25     3161   1773   2559   -134    489    113       C
ATOM    252  O   LYS A  25       7.191  17.037   8.277  1.00 19.42           O
ANISOU  252  O   LYS A  25     3063   1810   2506   -165    453    -40       O
ATOM    253  CB  LYS A  25       5.684  16.957   5.597  1.00 24.74           C
ANISOU  253  CB  LYS A  25     3941   2607   2853    -98    213    318       C
ATOM    254  CG  LYS A  25       5.463  16.835   4.104  1.00 35.73           C
ANISOU  254  CG  LYS A  25     5496   4116   3964   -108    112    468       C
ATOM    255  CD  LYS A  25       5.446  18.211   3.425  1.00 32.89           C
ANISOU  255  CD  LYS A  25     5191   3674   3633    -36    174    745       C
ATOM    256  CE  LYS A  25       5.676  18.148   1.910  1.00 46.53           C
ANISOU  256  CE  LYS A  25     7143   5543   4994    -71    146    902       C
ATOM    257  NZ  LYS A  25       4.525  18.683   1.134  1.00 57.94           N
ANISOU  257  NZ  LYS A  25     8595   7085   6334     10    -93   1209       N
ATOM    258  H   LYS A  25       8.163  16.003   6.221  1.00 23.21           H
ATOM    259  HA  LYS A  25       7.142  18.400   5.447  1.00 25.16           H
ATOM    260  HB2 LYS A  25       5.645  16.065   5.977  1.00 29.70           H
ATOM    261  HB3 LYS A  25       4.969  17.504   5.960  1.00 29.70           H
ATOM    262  HG2 LYS A  25       6.180  16.312   3.714  1.00 42.89           H
ATOM    263  HG3 LYS A  25       4.610  16.404   3.939  1.00 42.89           H
ATOM    264  HD2 LYS A  25       4.581  18.625   3.576  1.00 39.49           H
ATOM    265  HD3 LYS A  25       6.148  18.759   3.809  1.00 39.49           H
ATOM    266  HE2 LYS A  25       6.459  18.675   1.686  1.00 55.85           H
ATOM    267  HE3 LYS A  25       5.811  17.224   1.648  1.00 55.85           H
ATOM    268  HZ1 LYS A  25       4.694  18.628   0.262  1.00 69.54           H
ATOM    269  HZ2 LYS A  25       3.791  18.213   1.316  1.00 69.54           H
ATOM    270  HZ3 LYS A  25       4.383  19.535   1.348  1.00 69.54           H
ATOM    271  N   LYS A  26       6.716  19.142   7.781  1.00 20.35           N
ANISOU  271  N   LYS A  26     3205   1692   2836   -100    573    169       N
ATOM    272  CA  LYS A  26       6.711  19.604   9.163  1.00 20.06           C
ANISOU  272  CA  LYS A  26     3072   1568   2981   -124    653     -8       C
ATOM    273  C   LYS A  26       5.270  19.604   9.659  1.00 20.98           C
ANISOU  273  C   LYS A  26     3099   1690   3182    -16    584     23       C
ATOM    274  O   LYS A  26       4.378  20.162   9.000  1.00 24.79           O
ANISOU  274  O   LYS A  26     3564   2104   3752    104    547    221       O
ATOM    275  CB  LYS A  26       7.335  21.005   9.145  1.00 25.89           C
ANISOU  275  CB  LYS A  26     3853   2070   3914   -172    838     -1       C
ATOM    276  CG  LYS A  26       7.668  21.608  10.445  1.00 32.39           C
ANISOU  276  CG  LYS A  26     4585   2890   4833   -244    895   -230       C
ATOM    277  CD  LYS A  26       8.760  22.686  10.281  1.00 22.03           C
ANISOU  277  CD  LYS A  26     3278   1474   3620   -359   1015   -257       C
ATOM    278  CE  LYS A  26       8.587  23.657   9.097  1.00 24.23           C
ANISOU  278  CE  LYS A  26     3649   1556   4002   -295   1099    -13       C
ATOM    279  NZ  LYS A  26       9.153  24.999   9.454  1.00 27.35           N
ANISOU  279  NZ  LYS A  26     4040   1774   4575   -387   1231    -96       N
ATOM    280  H   LYS A  26       6.517  19.758   7.215  1.00 24.43           H
ATOM    281  HA  LYS A  26       7.206  19.038   9.776  1.00 24.08           H
ATOM    282  HB2 LYS A  26       8.160  20.958   8.637  1.00 31.08           H
ATOM    283  HB3 LYS A  26       6.710  21.605   8.708  1.00 31.08           H
ATOM    284  HG2 LYS A  26       6.877  22.025  10.821  1.00 38.88           H
ATOM    285  HG3 LYS A  26       7.999  20.922  11.046  1.00 38.88           H
ATOM    286  HD2 LYS A  26       8.780  23.223  11.088  1.00 26.45           H
ATOM    287  HD3 LYS A  26       9.612  22.239  10.159  1.00 26.45           H
ATOM    288  HE2 LYS A  26       9.058  23.315   8.321  1.00 29.09           H
ATOM    289  HE3 LYS A  26       7.644  23.760   8.893  1.00 29.09           H
ATOM    290  HZ1 LYS A  26       9.836  24.901  10.016  1.00 32.83           H
ATOM    291  HZ2 LYS A  26       9.440  25.414   8.720  1.00 32.83           H
ATOM    292  HZ3 LYS A  26       8.528  25.500   9.843  1.00 32.83           H
ATOM    293  N   VAL A  27       5.050  19.015  10.837  1.00 19.56           N
ANISOU  293  N   VAL A  27     2845   1605   2984    -52    577   -147       N
ATOM    294  CA  VAL A  27       3.739  19.015  11.475  1.00 20.34           C
ANISOU  294  CA  VAL A  27     2825   1724   3179     32    579   -143       C
ATOM    295  C   VAL A  27       3.856  19.273  12.979  1.00 21.86           C
ANISOU  295  C   VAL A  27     2997   1907   3401    -19    725   -375       C
ATOM    296  O   VAL A  27       4.905  19.053  13.587  1.00 21.55           O
ANISOU  296  O   VAL A  27     3017   1927   3243   -141    734   -528       O
ATOM    297  CB  VAL A  27       3.008  17.675  11.218  1.00 22.95           C
ANISOU  297  CB  VAL A  27     3092   2248   3381     12    403    -67       C
ATOM    298  CG1 VAL A  27       2.822  17.434   9.709  1.00 26.27           C
ANISOU  298  CG1 VAL A  27     3560   2710   3710     32    237    119       C
ATOM    299  CG2 VAL A  27       3.772  16.526  11.834  1.00 21.22           C
ANISOU  299  CG2 VAL A  27     2930   2140   2993   -104    372   -191       C
ATOM    300  H   VAL A  27       5.655  18.604  11.289  1.00 23.49           H
ATOM    301  HA  VAL A  27       3.220  19.754  11.119  1.00 24.42           H
ATOM    302  HB  VAL A  27       2.131  17.721  11.630  1.00 27.55           H
ATOM    303 HG11 VAL A  27       2.291  16.632   9.580  1.00 31.53           H
ATOM    304 HG12 VAL A  27       2.368  18.198   9.320  1.00 31.53           H
ATOM    305 HG13 VAL A  27       3.694  17.323   9.297  1.00 31.53           H
ATOM    306 HG21 VAL A  27       3.386  15.690  11.529  1.00 25.48           H
ATOM    307 HG22 VAL A  27       4.701  16.580  11.558  1.00 25.48           H
ATOM    308 HG23 VAL A  27       3.709  16.587  12.800  1.00 25.48           H
ATOM    309  N   ALA A  28       2.744  19.697  13.577  1.00 21.16           N
ANISOU  309  N   ALA A  28     2809   1777   3452     79    835   -398       N
ATOM    310  CA  ALA A  28       2.669  19.893  15.022  1.00 21.54           C
ANISOU  310  CA  ALA A  28     2864   1854   3469     30   1005   -635       C
ATOM    311  C   ALA A  28       2.578  18.556  15.744  1.00 19.21           C
ANISOU  311  C   ALA A  28     2544   1815   2939    -66    921   -651       C
ATOM    312  O   ALA A  28       2.038  17.582  15.211  1.00 22.53           O
ANISOU  312  O   ALA A  28     2890   2340   3330    -58    784   -481       O
ATOM    313  CB  ALA A  28       1.416  20.678  15.355  1.00 25.37           C
ANISOU  313  CB  ALA A  28     3230   2231   4179    190   1184   -631       C
ATOM    314  H   ALA A  28       2.013  19.880  13.163  1.00 25.40           H
ATOM    315  HA  ALA A  28       3.459  20.368  15.324  1.00 25.87           H
ATOM    316  HB1 ALA A  28       1.369  20.804  16.316  1.00 30.46           H
ATOM    317  HB2 ALA A  28       1.455  21.539  14.910  1.00 30.46           H
ATOM    318  HB3 ALA A  28       0.642  20.181  15.048  1.00 30.46           H
ATOM    319  N   VAL A  29       3.155  18.489  16.939  1.00 41.35           N
ANISOU  319  N   VAL A  29     8177   5202   2331  -1423    696   -478       N
ATOM    320  CA  VAL A  29       2.970  17.349  17.831  1.00 39.45           C
ANISOU  320  CA  VAL A  29     7754   4921   2315  -1334    855   -626       C
ATOM    321  C   VAL A  29       2.350  17.913  19.094  1.00 42.47           C
ANISOU  321  C   VAL A  29     7889   5430   2820  -1051    550   -435       C
ATOM    322  O   VAL A  29       2.983  18.716  19.788  1.00 37.73           O
ANISOU  322  O   VAL A  29     7099   4817   2419   -819    580   -299       O
ATOM    323  CB  VAL A  29       4.283  16.634  18.168  1.00 44.70           C
ANISOU  323  CB  VAL A  29     8327   5361   3296  -1246   1412   -787       C
ATOM    324  CG1 VAL A  29       3.994  15.406  19.065  1.00 43.93           C
ANISOU  324  CG1 VAL A  29     8068   5167   3456  -1113   1602   -894       C
ATOM    325  CG2 VAL A  29       4.987  16.222  16.930  1.00 45.94           C
ANISOU  325  CG2 VAL A  29     8717   5349   3391  -1533   1743   -966       C
ATOM    326  H   VAL A  29       3.667  19.101  17.260  1.00 49.56           H
ATOM    327  HA  VAL A  29       2.381  16.699  17.416  1.00 47.28           H
ATOM    328  HB  VAL A  29       4.864  17.242  18.651  1.00 53.65           H
ATOM    329 HG11 VAL A  29       4.807  14.884  19.158  1.00 52.73           H
ATOM    330 HG12 VAL A  29       3.697  15.713  19.936  1.00 52.73           H
ATOM    331 HG13 VAL A  29       3.302  14.868  18.650  1.00 52.73           H
ATOM    332 HG21 VAL A  29       5.771  15.704  17.169  1.00 55.14           H
ATOM    333 HG22 VAL A  29       4.388  15.684  16.389  1.00 55.14           H
ATOM    334 HG23 VAL A  29       5.253  17.015  16.439  1.00 55.14           H
ATOM    335  N   THR A  30       1.133  17.486  19.404  1.00 47.48           N
ANISOU  335  N   THR A  30     8371   6157   3511  -1053    258   -431       N
ATOM    336  CA  THR A  30       0.284  18.163  20.377  1.00 49.52           C
ANISOU  336  CA  THR A  30     8293   6518   4002   -802   -102   -228       C
ATOM    337  C   THR A  30      -0.205  17.144  21.398  1.00 32.34           C
ANISOU  337  C   THR A  30     5838   4283   2166   -693      7   -316       C
ATOM    338  O   THR A  30      -1.004  16.268  21.060  1.00 42.29           O
ANISOU  338  O   THR A  30     7128   5552   3389   -894    -21   -479       O
ATOM    339  CB  THR A  30      -0.884  18.836  19.646  1.00 67.05           C
ANISOU  339  CB  THR A  30    10586   8915   5974   -923   -606   -105       C
ATOM    340  OG1 THR A  30      -1.562  17.875  18.823  1.00 68.05           O
ANISOU  340  OG1 THR A  30    10861   9128   5866  -1246   -691   -310       O
ATOM    341  CG2 THR A  30      -0.380  19.974  18.744  1.00 59.14           C
ANISOU  341  CG2 THR A  30     9855   7920   4695   -960   -690     73       C
ATOM    342  H   THR A  30       0.768  16.789  19.056  1.00 56.99           H
ATOM    343  HA  THR A  30       0.789  18.832  20.865  1.00 59.43           H
ATOM    344  HB  THR A  30      -1.495  19.202  20.305  1.00 80.47           H
ATOM    345  HG1 THR A  30      -1.949  17.306  19.305  1.00 81.67           H
ATOM    346 HG21 THR A  30      -1.132  20.472  18.387  1.00 70.98           H
ATOM    347 HG22 THR A  30       0.184  20.577  19.253  1.00 70.98           H
ATOM    348 HG23 THR A  30       0.134  19.609  18.006  1.00 70.98           H
ATOM    349  N   SER A  31       0.283  17.252  22.635  1.00 38.53           N
ANISOU  349  N   SER A  31     6381   5011   3249   -411    143   -216       N
ATOM    350  CA  SER A  31      -0.218  16.408  23.709  1.00 35.69           C
ANISOU  350  CA  SER A  31     5810   4584   3166   -295    242   -233       C
ATOM    351  C   SER A  31      -1.522  16.988  24.241  1.00 28.64           C
ANISOU  351  C   SER A  31     4697   3800   2385   -257    -77   -165       C
ATOM    352  O   SER A  31      -1.690  18.212  24.327  1.00 36.11           O
ANISOU  352  O   SER A  31     5559   4838   3322   -163   -315    -30       O
ATOM    353  CB  SER A  31       0.796  16.309  24.848  1.00 39.11           C
ANISOU  353  CB  SER A  31     6100   4957   3804    -24    460   -119       C
ATOM    354  OG  SER A  31       0.258  15.578  25.943  1.00 46.40           O
ANISOU  354  OG  SER A  31     6889   5813   4929     87    541    -77       O
ATOM    355  H   SER A  31       0.900  17.802  22.871  1.00 46.25           H
ATOM    356  HA  SER A  31      -0.374  15.512  23.372  1.00 42.84           H
ATOM    357  HB2 SER A  31       1.590  15.855  24.525  1.00 46.95           H
ATOM    358  HB3 SER A  31       1.024  17.203  25.147  1.00 46.95           H
ATOM    359  HG  SER A  31       0.827  15.524  26.559  1.00 55.69           H
ATOM    360  N   SER A  32      -2.453  16.103  24.590  1.00 34.02           N
ANISOU  360  N   SER A  32     5274   4432   3221   -338    -27   -276       N
ATOM    361  CA  SER A  32      -3.686  16.540  25.235  1.00 37.66           C
ANISOU  361  CA  SER A  32     5460   4958   3892   -298   -236   -252       C
ATOM    362  C   SER A  32      -3.465  16.984  26.678  1.00 37.07           C
ANISOU  362  C   SER A  32     5235   4844   4004    -58   -109   -122       C
ATOM    363  O   SER A  32      -4.313  17.693  27.230  1.00 42.16           O
ANISOU  363  O   SER A  32     5661   5526   4831     -4   -240    -96       O
ATOM    364  CB  SER A  32      -4.717  15.409  25.188  1.00 46.31           C
ANISOU  364  CB  SER A  32     6478   5994   5121   -510   -149   -462       C
ATOM    365  OG  SER A  32      -4.178  14.189  25.677  1.00 57.70           O
ANISOU  365  OG  SER A  32     8064   7226   6634   -506    282   -523       O
ATOM    366  H   SER A  32      -2.394  15.253  24.467  1.00 40.84           H
ATOM    367  HA  SER A  32      -4.043  17.298  24.747  1.00 45.21           H
ATOM    368  HB2 SER A  32      -5.478  15.657  25.737  1.00 55.58           H
ATOM    369  HB3 SER A  32      -4.999  15.281  24.269  1.00 55.58           H
ATOM    370  HG  SER A  32      -4.741  13.571  25.589  1.00 69.25           H
ATOM    371  N   LYS A  33      -2.342  16.613  27.287  1.00 30.79           N
ANISOU  371  N   LYS A  33     4543   3984   3171     77    137    -45       N
ATOM    372  CA  LYS A  33      -2.142  16.818  28.719  1.00 28.57           C
ANISOU  372  CA  LYS A  33     4167   3706   2981    248    248     66       C
ATOM    373  C   LYS A  33      -1.927  18.292  29.031  1.00 33.03           C
ANISOU  373  C   LYS A  33     4632   4396   3522    332     79    135       C
ATOM    374  O   LYS A  33      -1.320  19.030  28.254  1.00 34.71           O
ANISOU  374  O   LYS A  33     4903   4662   3623    329    -39    160       O
ATOM    375  CB  LYS A  33      -0.953  15.985  29.189  1.00 27.18           C
ANISOU  375  CB  LYS A  33     4104   3464   2761    385    476    170       C
ATOM    376  CG  LYS A  33      -1.239  14.475  29.241  1.00 36.55           C
ANISOU  376  CG  LYS A  33     5404   4433   4052    342    752    135       C
ATOM    377  CD  LYS A  33       0.034  13.634  29.233  1.00 46.25           C
ANISOU  377  CD  LYS A  33     6734   5536   5303    505    970    250       C
ATOM    378  CE  LYS A  33      -0.264  12.163  29.532  1.00 56.36           C
ANISOU  378  CE  LYS A  33     8149   6525   6740    510   1310    269       C
ATOM    379  NZ  LYS A  33       0.750  11.238  28.941  1.00 61.72           N
ANISOU  379  NZ  LYS A  33     8928   6983   7538    602   1583    285       N
ATOM    380  H   LYS A  33      -1.677  16.238  26.892  1.00 36.96           H
ATOM    381  HA  LYS A  33      -2.928  16.534  29.212  1.00 34.29           H
ATOM    382  HB2 LYS A  33      -0.213  16.126  28.577  1.00 32.63           H
ATOM    383  HB3 LYS A  33      -0.704  16.271  30.082  1.00 32.63           H
ATOM    384  HG2 LYS A  33      -1.726  14.274  30.055  1.00 43.88           H
ATOM    385  HG3 LYS A  33      -1.768  14.226  28.467  1.00 43.88           H
ATOM    386  HD2 LYS A  33       0.449  13.689  28.358  1.00 55.51           H
ATOM    387  HD3 LYS A  33       0.643  13.966  29.911  1.00 55.51           H
ATOM    388  HE2 LYS A  33      -0.267  12.030  30.493  1.00 67.65           H
ATOM    389  HE3 LYS A  33      -1.131  11.934  29.163  1.00 67.65           H
ATOM    390  HZ1 LYS A  33       0.535  10.394  29.125  1.00 74.07           H
ATOM    391  HZ2 LYS A  33       0.779  11.343  28.058  1.00 74.07           H
ATOM    392  HZ3 LYS A  33       1.554  11.412  29.279  1.00 74.07           H
ATOM    393  N   MET A  34      -2.433  18.720  30.193  1.00 31.21           N
ANISOU  393  N   MET A  34     4283   4178   3397    375    131    143       N
ATOM    394  CA  MET A  34      -2.463  20.134  30.544  1.00 33.36           C
ANISOU  394  CA  MET A  34     4455   4508   3713    411     44    150       C
ATOM    395  C   MET A  34      -1.647  20.474  31.789  1.00 24.68           C
ANISOU  395  C   MET A  34     3381   3505   2493    460    170    179       C
ATOM    396  O   MET A  34      -1.764  21.598  32.307  1.00 29.87           O
ANISOU  396  O   MET A  34     3966   4183   3199    439    187    125       O
ATOM    397  CB  MET A  34      -3.913  20.591  30.733  1.00 47.68           C
ANISOU  397  CB  MET A  34     6070   6241   5805    372     13     71       C
ATOM    398  CG  MET A  34      -4.753  20.546  29.466  1.00 55.85           C
ANISOU  398  CG  MET A  34     7011   7257   6954    320   -236     58       C
ATOM    399  SD  MET A  34      -4.660  22.063  28.491  1.00 78.75           S
ANISOU  399  SD  MET A  34     9897  10161   9865    402   -520    190       S
ATOM    400  CE  MET A  34      -3.155  21.797  27.558  1.00 44.15           C
ANISOU  400  CE  MET A  34     5845   5851   5079    355   -529    253       C
ATOM    401  H   MET A  34      -2.766  18.203  30.794  1.00 37.46           H
ATOM    402  HA  MET A  34      -2.077  20.629  29.803  1.00 40.04           H
ATOM    403  HB2 MET A  34      -4.336  20.013  31.387  1.00 57.23           H
ATOM    404  HB3 MET A  34      -3.910  21.507  31.052  1.00 57.23           H
ATOM    405  HG2 MET A  34      -4.443  19.815  28.909  1.00 67.04           H
ATOM    406  HG3 MET A  34      -5.682  20.405  29.710  1.00 67.04           H
ATOM    407  HE1 MET A  34      -3.166  22.366  26.772  1.00 52.99           H
ATOM    408  HE2 MET A  34      -2.394  22.020  28.117  1.00 52.99           H
ATOM    409  HE3 MET A  34      -3.108  20.866  27.292  1.00 52.99           H
ATOM    410  N   ASP A  35      -0.830  19.552  32.275  1.00 23.64           N
ANISOU  410  N   ASP A  35     3343   3429   2210    519    252    266       N
ATOM    411  CA  ASP A  35       0.092  19.865  33.352  1.00 22.44           C
ANISOU  411  CA  ASP A  35     3199   3449   1879    557    267    319       C
ATOM    412  C   ASP A  35       1.249  20.719  32.830  1.00 21.90           C
ANISOU  412  C   ASP A  35     3068   3501   1751    566    159    293       C
ATOM    413  O   ASP A  35       1.544  20.765  31.621  1.00 21.52           O
ANISOU  413  O   ASP A  35     3036   3383   1759    571    118    281       O
ATOM    414  CB  ASP A  35       0.619  18.587  33.965  1.00 24.05           C
ANISOU  414  CB  ASP A  35     3498   3671   1969    667    332    489       C
ATOM    415  CG  ASP A  35       1.379  17.762  32.981  1.00 24.64           C
ANISOU  415  CG  ASP A  35     3581   3666   2114    777    332    561       C
ATOM    416  OD1 ASP A  35       0.725  17.147  32.111  1.00 30.05           O
ANISOU  416  OD1 ASP A  35     4327   4164   2928    726    415    498       O
ATOM    417  OD2 ASP A  35       2.630  17.776  33.001  1.00 25.47           O
ANISOU  417  OD2 ASP A  35     3609   3897   2171    885    263    640       O
ATOM    418  H   ASP A  35      -0.790  18.739  31.999  1.00 28.38           H
ATOM    419  HA  ASP A  35      -0.364  20.370  34.043  1.00 26.87           H
ATOM    420  HB2 ASP A  35       1.214  18.807  34.698  1.00 28.87           H
ATOM    421  HB3 ASP A  35      -0.127  18.058  34.290  1.00 28.87           H
ATOM    422  N   ALA A  36       1.927  21.380  33.776  1.00 22.65           N
ANISOU  422  N   ALA A  36     3112   3789   1705    525    138    259       N
ATOM    423  CA  ALA A  36       2.918  22.405  33.445  1.00 22.66           C
ANISOU  423  CA  ALA A  36     3024   3900   1686    464     91    163       C
ATOM    424  C   ALA A  36       4.005  21.887  32.512  1.00 22.67           C
ANISOU  424  C   ALA A  36     2975   3913   1725    553     59    220       C
ATOM    425  O   ALA A  36       4.333  22.549  31.532  1.00 22.72           O
ANISOU  425  O   ALA A  36     2995   3842   1797    489     96    142       O
ATOM    426  CB  ALA A  36       3.522  22.951  34.742  1.00 24.34           C
ANISOU  426  CB  ALA A  36     3174   4371   1702    359     64     85       C
ATOM    427  H   ALA A  36       1.830  21.253  34.621  1.00 27.12           H
ATOM    428  HA  ALA A  36       2.473  23.126  32.974  1.00 27.13           H
ATOM    429  HB1 ALA A  36       4.180  23.629  34.523  1.00 29.15           H
ATOM    430  HB2 ALA A  36       2.815  23.338  35.281  1.00 29.15           H
ATOM    431  HB3 ALA A  36       3.944  22.223  35.224  1.00 29.15           H
ATOM    432  N   TRP A  37       4.613  20.742  32.826  1.00 23.76           N
ANISOU  432  N   TRP A  37     3066   4122   1840    700     30    363       N
ATOM    433  CA  TRP A  37       5.707  20.234  32.004  1.00 24.49           C
ANISOU  433  CA  TRP A  37     3063   4192   2051    795     71    388       C
ATOM    434  C   TRP A  37       5.257  20.004  30.575  1.00 23.37           C
ANISOU  434  C   TRP A  37     3084   3797   2001    744    202    330       C
ATOM    435  O   TRP A  37       5.969  20.351  29.622  1.00 23.67           O
ANISOU  435  O   TRP A  37     3118   3789   2086    679    293    236       O
ATOM    436  CB  TRP A  37       6.216  18.900  32.552  1.00 26.48           C
ANISOU  436  CB  TRP A  37     3244   4466   2349   1019     54    600       C
ATOM    437  CG  TRP A  37       7.375  18.318  31.744  1.00 32.49           C
ANISOU  437  CG  TRP A  37     3851   5156   3338   1146    162    611       C
ATOM    438  CD1 TRP A  37       8.698  18.554  31.951  1.00 47.82           C
ANISOU  438  CD1 TRP A  37     5484   7299   5385   1217     86    602       C
ATOM    439  CD2 TRP A  37       7.301  17.423  30.612  1.00 57.73           C
ANISOU  439  CD2 TRP A  37     7170   8052   6713   1184    408    588       C
ATOM    440  NE1 TRP A  37       9.459  17.868  31.030  1.00 40.38           N
ANISOU  440  NE1 TRP A  37     4442   6172   4730   1326    301    583       N
ATOM    441  CE2 TRP A  37       8.626  17.167  30.199  1.00 57.29           C
ANISOU  441  CE2 TRP A  37     6878   7993   6894   1294    521    566       C
ATOM    442  CE3 TRP A  37       6.249  16.818  29.913  1.00 52.68           C
ANISOU  442  CE3 TRP A  37     6798   7157   6063   1101    556    546       C
ATOM    443  CZ2 TRP A  37       8.928  16.334  29.118  1.00 54.65           C
ANISOU  443  CZ2 TRP A  37     6614   7368   6782   1318    840    494       C
ATOM    444  CZ3 TRP A  37       6.553  15.985  28.834  1.00 42.00           C
ANISOU  444  CZ3 TRP A  37     5532   5555   4872   1094    828    468       C
ATOM    445  CH2 TRP A  37       7.881  15.753  28.452  1.00 47.54           C
ANISOU  445  CH2 TRP A  37     6041   6220   5803   1201    997    439       C
ATOM    446  H   TRP A  37       4.413  20.248  33.501  1.00 28.45           H
ATOM    447  HA  TRP A  37       6.420  20.891  32.029  1.00 29.33           H
ATOM    448  HB2 TRP A  37       6.524  19.032  33.462  1.00 31.71           H
ATOM    449  HB3 TRP A  37       5.490  18.257  32.537  1.00 31.71           H
ATOM    450  HD1 TRP A  37       9.041  19.102  32.620  1.00 57.39           H
ATOM    451  HE1 TRP A  37      10.318  17.879  30.984  1.00 48.47           H
ATOM    452  HE3 TRP A  37       5.365  16.968  30.162  1.00 63.23           H
ATOM    453  HZ2 TRP A  37       9.808  16.179  28.860  1.00 65.59           H
ATOM    454  HZ3 TRP A  37       5.864  15.579  28.361  1.00 50.41           H
ATOM    455  HH2 TRP A  37       8.056  15.192  27.731  1.00 57.06           H
ATOM    456  N   ASN A  38       4.067  19.426  30.393  1.00 22.69           N
ANISOU  456  N   ASN A  38     3152   3553   1916    731    222    363       N
ATOM    457  CA  ASN A  38       3.581  19.163  29.039  1.00 26.77           C
ANISOU  457  CA  ASN A  38     3833   3888   2451    632    288    292       C
ATOM    458  C   ASN A  38       3.234  20.444  28.292  1.00 22.23           C
ANISOU  458  C   ASN A  38     3335   3307   1806    492    196    221       C
ATOM    459  O   ASN A  38       3.453  20.531  27.086  1.00 23.79           O
ANISOU  459  O   ASN A  38     3684   3421   1932    391    243    174       O
ATOM    460  CB  ASN A  38       2.369  18.230  29.077  1.00 33.55           C
ANISOU  460  CB  ASN A  38     4785   4615   3346    613    312    307       C
ATOM    461  CG  ASN A  38       2.763  16.768  28.985  1.00 33.60           C
ANISOU  461  CG  ASN A  38     4846   4473   3446    699    517    351       C
ATOM    462  OD1 ASN A  38       3.247  16.309  27.944  1.00 33.73           O
ANISOU  462  OD1 ASN A  38     4954   4372   3489    642    665    265       O
ATOM    463  ND2 ASN A  38       2.547  16.028  30.059  1.00 34.72           N
ANISOU  463  ND2 ASN A  38     4970   4584   3639    823    574    482       N
ATOM    464  H   ASN A  38       3.534  19.182  31.023  1.00 27.24           H
ATOM    465  HA  ASN A  38       4.292  18.719  28.551  1.00 32.14           H
ATOM    466  HB2 ASN A  38       1.893  18.362  29.912  1.00 40.27           H
ATOM    467  HB3 ASN A  38       1.788  18.434  28.328  1.00 40.27           H
ATOM    468 HD21 ASN A  38       2.754  15.193  30.056  1.00 41.68           H
ATOM    469 HD22 ASN A  38       2.200  16.382  30.762  1.00 41.68           H
ATOM    470  N   ILE A  39       2.687  21.453  28.980  1.00 23.24           N
ANISOU  470  N   ILE A  39     3392   3490   1948    478     98    220       N
ATOM    471  CA  ILE A  39       2.420  22.719  28.300  1.00 22.10           C
ANISOU  471  CA  ILE A  39     3325   3279   1794    393     40    204       C
ATOM    472  C   ILE A  39       3.729  23.308  27.821  1.00 21.94           C
ANISOU  472  C   ILE A  39     3339   3281   1717    328    161    147       C
ATOM    473  O   ILE A  39       3.851  23.779  26.698  1.00 22.76           O
ANISOU  473  O   ILE A  39     3631   3276   1740    237    191    159       O
ATOM    474  CB  ILE A  39       1.669  23.699  29.214  1.00 24.29           C
ANISOU  474  CB  ILE A  39     3497   3548   2184    401      6    187       C
ATOM    475  CG1 ILE A  39       0.305  23.147  29.599  1.00 29.70           C
ANISOU  475  CG1 ILE A  39     4119   4181   2987    441    -58    209       C
ATOM    476  CG2 ILE A  39       1.524  25.038  28.480  1.00 24.79           C
ANISOU  476  CG2 ILE A  39     3651   3474   2294    357    -11    215       C
ATOM    477  CD1 ILE A  39      -0.376  23.953  30.720  1.00 33.38           C
ANISOU  477  CD1 ILE A  39     4461   4618   3604    436     18    142       C
ATOM    478  H   ILE A  39       2.470  21.429  29.812  1.00 27.90           H
ATOM    479  HA  ILE A  39       1.847  22.546  27.537  1.00 26.54           H
ATOM    480  HB  ILE A  39       2.173  23.824  30.033  1.00 29.16           H
ATOM    481 HG12 ILE A  39      -0.274  23.168  28.821  1.00 35.66           H
ATOM    482 HG13 ILE A  39       0.411  22.234  29.909  1.00 35.66           H
ATOM    483 HG21 ILE A  39       0.911  25.604  28.974  1.00 29.76           H
ATOM    484 HG22 ILE A  39       2.394  25.463  28.423  1.00 29.76           H
ATOM    485 HG23 ILE A  39       1.177  24.874  27.589  1.00 29.76           H
ATOM    486 HD11 ILE A  39      -1.191  23.499  30.985  1.00 40.07           H
ATOM    487 HD12 ILE A  39       0.228  24.016  31.476  1.00 40.07           H
ATOM    488 HD13 ILE A  39      -0.585  24.841  30.388  1.00 40.07           H
ATOM    489  N   PHE A  40       4.715  23.321  28.704  1.00 22.84           N
ANISOU  489  N   PHE A  40     3268   3547   1861    353    228     83       N
ATOM    490  CA  PHE A  40       6.023  23.866  28.398  1.00 23.72           C
ANISOU  490  CA  PHE A  40     3316   3706   1988    268    367    -24       C
ATOM    491  C   PHE A  40       6.692  23.127  27.248  1.00 27.50           C
ANISOU  491  C   PHE A  40     3893   4089   2467    249    520    -41       C
ATOM    492  O   PHE A  40       7.182  23.740  26.288  1.00 26.64           O
ANISOU  492  O   PHE A  40     3937   3871   2314    106    683   -110       O
ATOM    493  CB  PHE A  40       6.827  23.741  29.684  1.00 27.49           C
ANISOU  493  CB  PHE A  40     3505   4438   2501    313    318    -76       C
ATOM    494  CG  PHE A  40       8.218  24.127  29.525  1.00 28.02           C
ANISOU  494  CG  PHE A  40     3388   4611   2649    229    434   -217       C
ATOM    495  CD1 PHE A  40       8.583  25.447  29.679  1.00 44.89           C
ANISOU  495  CD1 PHE A  40     5491   6776   4790     34    523   -386       C
ATOM    496  CD2 PHE A  40       9.174  23.182  29.255  1.00 44.46           C
ANISOU  496  CD2 PHE A  40     5295   6737   4860    336    496   -203       C
ATOM    497  CE1 PHE A  40       9.875  25.807  29.539  1.00 49.35           C
ANISOU  497  CE1 PHE A  40     5842   7442   5464    -87    658   -562       C
ATOM    498  CE2 PHE A  40      10.453  23.538  29.122  1.00 48.55           C
ANISOU  498  CE2 PHE A  40     5566   7356   5525    254    619   -361       C
ATOM    499  CZ  PHE A  40      10.791  24.859  29.306  1.00 48.19           C
ANISOU  499  CZ  PHE A  40     5474   7379   5458     27    683   -551       C
ATOM    500  H   PHE A  40       4.651  23.014  29.504  1.00 27.42           H
ATOM    501  HA  PHE A  40       5.965  24.791  28.113  1.00 28.47           H
ATOM    502  HB2 PHE A  40       6.432  24.315  30.359  1.00 33.00           H
ATOM    503  HB3 PHE A  40       6.805  22.818  29.981  1.00 33.00           H
ATOM    504  HD1 PHE A  40       7.939  26.087  29.878  1.00 53.88           H
ATOM    505  HD2 PHE A  40       8.929  22.290  29.164  1.00 53.36           H
ATOM    506  HE1 PHE A  40      10.126  26.701  29.604  1.00 59.23           H
ATOM    507  HE2 PHE A  40      11.102  22.907  28.909  1.00 58.27           H
ATOM    508  HZ  PHE A  40      11.688  25.101  29.268  1.00 57.84           H
ATOM    509  N   GLU A  41       6.723  21.804  27.316  1.00 25.53           N
ANISOU  509  N   GLU A  41     3594   3836   2271    373    533     11       N
ATOM    510  CA  GLU A  41       7.357  21.032  26.261  1.00 29.98           C
ANISOU  510  CA  GLU A  41     4252   4263   2876    336    764    -53       C
ATOM    511  C   GLU A  41       6.645  21.228  24.927  1.00 26.02           C
ANISOU  511  C   GLU A  41     4131   3596   2158    149    800    -72       C
ATOM    512  O   GLU A  41       7.271  21.140  23.881  1.00 31.48           O
ANISOU  512  O   GLU A  41     4998   4175   2789      5   1043   -176       O
ATOM    513  CB  GLU A  41       7.409  19.553  26.651  1.00 30.41           C
ANISOU  513  CB  GLU A  41     4201   4276   3077    519    814     19       C
ATOM    514  CG  GLU A  41       8.749  18.856  26.332  1.00 51.04           C
ANISOU  514  CG  GLU A  41     6633   6821   5941    600   1090    -52       C
ATOM    515  CD  GLU A  41       9.922  19.398  27.145  1.00 52.24           C
ANISOU  515  CD  GLU A  41     6385   7195   6270    695   1024    -64       C
ATOM    516  OE1 GLU A  41       9.691  20.176  28.097  1.00 55.46           O
ANISOU  516  OE1 GLU A  41     6687   7823   6561    691    765    -19       O
ATOM    517  OE2 GLU A  41      11.080  19.044  26.826  1.00 57.39           O
ANISOU  517  OE2 GLU A  41     6808   7804   7195    751   1250   -150       O
ATOM    518  H   GLU A  41       6.389  21.334  27.955  1.00 30.65           H
ATOM    519  HA  GLU A  41       8.272  21.332  26.150  1.00 35.99           H
ATOM    520  HB2 GLU A  41       7.260  19.480  27.607  1.00 36.50           H
ATOM    521  HB3 GLU A  41       6.711  19.082  26.169  1.00 36.50           H
ATOM    522  HG2 GLU A  41       8.664  17.909  26.526  1.00 61.27           H
ATOM    523  HG3 GLU A  41       8.954  18.984  25.393  1.00 61.27           H
ATOM    524  N   GLY A  42       5.340  21.471  24.937  1.00 24.79           N
ANISOU  524  N   GLY A  42     4102   3436   1881    137    560     25       N
ATOM    525  CA  GLY A  42       4.636  21.743  23.700  1.00 27.75           C
ANISOU  525  CA  GLY A  42     4809   3718   2017    -32    484     53       C
ATOM    526  C   GLY A  42       5.030  23.044  23.042  1.00 27.06           C
ANISOU  526  C   GLY A  42     4916   3568   1796   -153    536     84       C
ATOM    527  O   GLY A  42       4.958  23.162  21.831  1.00 29.08           O
ANISOU  527  O   GLY A  42     5518   3740   1789   -328    572    103       O
ATOM    528  H   GLY A  42       4.846  21.484  25.641  1.00 29.75           H
ATOM    529  HA2 GLY A  42       4.814  21.025  23.073  1.00 33.31           H
ATOM    530  HA3 GLY A  42       3.684  21.775  23.881  1.00 33.31           H
ATOM    531  N   LEU A  43       5.400  24.043  23.832  1.00 26.33           N
ANISOU  531  N   LEU A  43     4646   3506   1852    -90    553     89       N
ATOM    532  CA  LEU A  43       5.834  25.320  23.289  1.00 27.84           C
ANISOU  532  CA  LEU A  43     5029   3580   1967   -215    682    108       C
ATOM    533  C   LEU A  43       7.271  25.293  22.801  1.00 29.38           C
ANISOU  533  C   LEU A  43     5257   3734   2174   -369   1058    -71       C
ATOM    534  O   LEU A  43       7.617  26.103  21.932  1.00 36.64           O
ANISOU  534  O   LEU A  43     6480   4498   2943   -543   1247    -59       O
ATOM    535  CB  LEU A  43       5.692  26.395  24.367  1.00 27.01           C
ANISOU  535  CB  LEU A  43     4715   3491   2058   -139    635    113       C
ATOM    536  CG  LEU A  43       4.271  26.693  24.832  1.00 26.28           C
ANISOU  536  CG  LEU A  43     4576   3371   2039      0    355    267       C
ATOM    537  CD1 LEU A  43       4.291  27.428  26.150  1.00 26.94           C
ANISOU  537  CD1 LEU A  43     4405   3493   2337     42    410    171       C
ATOM    538  CD2 LEU A  43       3.547  27.538  23.769  1.00 30.59           C
ANISOU  538  CD2 LEU A  43     5440   3717   2465    -16    238    491       C
ATOM    539  H   LEU A  43       5.408  24.006  24.691  1.00 31.53           H
ATOM    540  HA  LEU A  43       5.271  25.553  22.534  1.00 33.34           H
ATOM    541  HB2 LEU A  43       6.195  26.110  25.146  1.00 32.36           H
ATOM    542  HB3 LEU A  43       6.059  27.223  24.020  1.00 32.36           H
ATOM    543  HG  LEU A  43       3.790  25.860  24.957  1.00 31.48           H
ATOM    544 HD11 LEU A  43       3.379  27.621  26.418  1.00 32.34           H
ATOM    545 HD12 LEU A  43       4.720  26.869  26.817  1.00 32.34           H
ATOM    546 HD13 LEU A  43       4.786  28.255  26.043  1.00 32.34           H
ATOM    547 HD21 LEU A  43       2.650  27.737  24.081  1.00 36.72           H
ATOM    548 HD22 LEU A  43       4.039  28.363  23.632  1.00 36.72           H
ATOM    549 HD23 LEU A  43       3.506  27.036  22.940  1.00 36.72           H
ATOM    550  N  AVAL A  44       8.113  24.391  23.301  0.59 29.06           N
ANISOU  550  N  AVAL A  44     4912   3801   2328   -305   1193   -221       N
ATOM    551  CA AVAL A  44       9.510  24.324  22.868  0.59 31.19           C
ANISOU  551  CA AVAL A  44     5107   4024   2718   -432   1579   -422       C
ATOM    552  C  AVAL A  44       9.744  23.189  21.879  0.59 32.75           C
ANISOU  552  C  AVAL A  44     5495   4103   2846   -508   1814   -501       C
ATOM    553  O  AVAL A  44      10.453  23.367  20.884  0.59 45.43           O
ANISOU  553  O  AVAL A  44     7333   5557   4370   -732   2184   -638       O
ATOM    554  CB AVAL A  44      10.468  24.223  24.076  0.59 36.98           C
ANISOU  554  CB AVAL A  44     5300   4961   3790   -307   1584   -543       C
ATOM    555  CG1AVAL A  44       9.997  23.164  25.046  0.59 39.96           C
ANISOU  555  CG1AVAL A  44     5433   5491   4260    -47   1309   -424       C
ATOM    556  CG2AVAL A  44      11.890  23.919  23.600  0.59 38.93           C
ANISOU  556  CG2AVAL A  44     5357   5163   4272   -400   1978   -762       C
ATOM    557  H  AVAL A  44       7.900  23.806  23.895  0.59 34.81           H
ATOM    558  HA AVAL A  44       9.716  25.154  22.410  0.59 37.36           H
ATOM    559  HB AVAL A  44      10.475  25.074  24.541  0.59 44.39           H
ATOM    560 HG11AVAL A  44      10.770  22.722  25.431  0.59 47.97           H
ATOM    561 HG12AVAL A  44       9.476  23.588  25.746  0.59 47.97           H
ATOM    562 HG13AVAL A  44       9.450  22.520  24.570  0.59 47.97           H
ATOM    563 HG21AVAL A  44      12.513  24.121  24.316  0.59 46.73           H
ATOM    564 HG22AVAL A  44      11.951  22.979  23.365  0.59 46.73           H
ATOM    565 HG23AVAL A  44      12.088  24.467  22.825  0.59 46.73           H
ATOM    566  N  BVAL A  44       8.096  24.382  23.322  0.41 29.01           N
ANISOU  566  N  BVAL A  44     4902   3798   2323   -300   1187   -219       N
ATOM    567  CA BVAL A  44       9.499  24.327  22.951  0.41 31.06           C
ANISOU  567  CA BVAL A  44     5068   4021   2715   -420   1563   -419       C
ATOM    568  C  BVAL A  44       9.821  23.171  22.010  0.41 32.66           C
ANISOU  568  C  BVAL A  44     5426   4108   2874   -488   1811   -508       C
ATOM    569  O  BVAL A  44      10.732  23.309  21.199  0.41 41.36           O
ANISOU  569  O  BVAL A  44     6651   5080   3984   -681   2203   -673       O
ATOM    570  CB BVAL A  44      10.447  24.305  24.172  0.41 36.58           C
ANISOU  570  CB BVAL A  44     5232   4925   3743   -303   1563   -540       C
ATOM    571  CG1BVAL A  44      10.309  25.585  24.998  0.41 37.14           C
ANISOU  571  CG1BVAL A  44     5199   5088   3826   -351   1436   -553       C
ATOM    572  CG2BVAL A  44      10.212  23.058  25.015  0.41 40.23           C
ANISOU  572  CG2BVAL A  44     5426   5526   4334    -44   1353   -447       C
ATOM    573  H  BVAL A  44       7.861  23.785  23.894  0.41 34.75           H
ATOM    574  HA BVAL A  44       9.689  25.145  22.466  0.41 37.22           H
ATOM    575  HB BVAL A  44      11.363  24.271  23.855  0.41 43.91           H
ATOM    576 HG11BVAL A  44      11.190  25.970  25.133  0.41 44.58           H
ATOM    577 HG12BVAL A  44       9.745  26.211  24.519  0.41 44.58           H
ATOM    578 HG13BVAL A  44       9.909  25.367  25.854  0.41 44.58           H
ATOM    579 HG21BVAL A  44      10.507  23.230  25.923  0.41 48.29           H
ATOM    580 HG22BVAL A  44       9.266  22.846  25.009  0.41 48.29           H
ATOM    581 HG23BVAL A  44      10.719  22.322  24.638  0.41 48.29           H
ATOM    582  N   MET A  45       9.163  22.016  22.149  1.00 28.14           N
ANISOU  582  N   MET A  45     3407   4246   3038   -785    747  -1172       N
ATOM    583  CA  MET A  45       9.379  20.852  21.280  1.00 27.69           C
ANISOU  583  CA  MET A  45     3433   4094   2995   -770    644   -860       C
ATOM    584  C   MET A  45       8.054  20.429  20.649  1.00 31.25           C
ANISOU  584  C   MET A  45     3720   4602   3550   -823    837   -897       C
ATOM    585  O   MET A  45       7.593  19.293  20.807  1.00 40.52           O
ANISOU  585  O   MET A  45     5036   5830   4528  -1009    914   -774       O
ATOM    586  CB  MET A  45       9.939  19.657  22.061  1.00 31.52           C
ANISOU  586  CB  MET A  45     4282   4584   3109   -938    516   -653       C
ATOM    587  CG  MET A  45      11.294  19.876  22.725  1.00 31.71           C
ANISOU  587  CG  MET A  45     4475   4527   3048   -873    223   -622       C
ATOM    588  SD  MET A  45      12.754  19.635  21.663  1.00 39.44           S
ANISOU  588  SD  MET A  45     5320   5280   4386   -614    -90   -471       S
ATOM    589  CE  MET A  45      12.788  17.869  21.400  1.00 34.57           C
ANISOU  589  CE  MET A  45     4934   4549   3652   -658   -253   -209       C
ATOM    590  H   MET A  45       8.644  21.863  22.818  1.00 33.78           H
ATOM    591  HA  MET A  45      10.020  21.120  20.604  1.00 33.24           H
ATOM    592  HB2 MET A  45       9.308  19.429  22.762  1.00 37.83           H
ATOM    593  HB3 MET A  45      10.037  18.912  21.447  1.00 37.83           H
ATOM    594  HG2 MET A  45      11.326  20.788  23.054  1.00 38.07           H
ATOM    595  HG3 MET A  45      11.373  19.254  23.465  1.00 38.07           H
ATOM    596  HE1 MET A  45      13.573  17.643  20.876  1.00 41.49           H
ATOM    597  HE2 MET A  45      12.824  17.422  22.260  1.00 41.49           H
ATOM    598  HE3 MET A  45      11.985  17.605  20.923  1.00 41.49           H
ATOM    599  N   GLY A  46       7.428  21.345  19.929  1.00 23.43           N
ANISOU  599  N   GLY A  46     2443   3560   2900   -662    860  -1069       N
ATOM    600  CA  GLY A  46       6.062  21.161  19.498  1.00 23.50           C
ANISOU  600  CA  GLY A  46     2299   3557   3071   -660    895  -1145       C
ATOM    601  C   GLY A  46       5.878  20.819  18.039  1.00 20.40           C
ANISOU  601  C   GLY A  46     1838   3029   2884   -520    764   -990       C
ATOM    602  O   GLY A  46       4.735  20.814  17.569  1.00 23.54           O
ANISOU  602  O   GLY A  46     2087   3401   3456   -480    747  -1101       O
ATOM    603  H   GLY A  46       7.781  22.088  19.677  1.00 28.13           H
ATOM    604  HA2 GLY A  46       5.670  20.443  20.018  1.00 28.21           H
ATOM    605  HA3 GLY A  46       5.572  21.980  19.670  1.00 28.21           H
ATOM    606  N   SER A  47       6.958  20.539  17.313  1.00 20.81           N
ANISOU  606  N   SER A  47     1992   2993   2923   -458    656   -763       N
ATOM    607  CA  SER A  47       6.854  20.238  15.893  1.00 18.84           C
ANISOU  607  CA  SER A  47     1736   2610   2810   -350    516   -612       C
ATOM    608  C   SER A  47       7.994  19.336  15.465  1.00 16.52           C
ANISOU  608  C   SER A  47     1645   2265   2366   -359    443   -370       C
ATOM    609  O   SER A  47       9.080  19.336  16.041  1.00 17.82           O
ANISOU  609  O   SER A  47     1907   2430   2433   -371    417   -321       O
ATOM    610  CB  SER A  47       6.839  21.519  15.046  1.00 22.97           C
ANISOU  610  CB  SER A  47     2188   2960   3579   -176    351   -650       C
ATOM    611  OG  SER A  47       7.948  22.342  15.382  1.00 23.22           O
ANISOU  611  OG  SER A  47     2297   2927   3598   -154    323   -622       O
ATOM    612  H   SER A  47       7.760  20.517  17.621  1.00 24.99           H
ATOM    613  HA  SER A  47       6.028  19.754  15.736  1.00 22.61           H
ATOM    614  HB2 SER A  47       6.892  21.281  14.108  1.00 27.57           H
ATOM    615  HB3 SER A  47       6.018  22.006  15.219  1.00 27.57           H
ATOM    616  HG  SER A  47       7.692  23.132  15.506  1.00 27.87           H
ATOM    617  N   VAL A  48       7.717  18.561  14.416  1.00 15.74           N
ANISOU  617  N   VAL A  48     1579   2114   2289   -338    384   -268       N
ATOM    618  CA  VAL A  48       8.647  17.570  13.889  1.00 15.03           C
ANISOU  618  CA  VAL A  48     1630   1973   2109   -328    324   -121       C
ATOM    619  C   VAL A  48       8.680  17.603  12.370  1.00 14.82           C
ANISOU  619  C   VAL A  48     1632   1868   2133   -249    256    -69       C
ATOM    620  O   VAL A  48       7.724  18.023  11.713  1.00 15.73           O
ANISOU  620  O   VAL A  48     1705   1945   2326   -216    190   -100       O
ATOM    621  CB  VAL A  48       8.291  16.139  14.376  1.00 15.69           C
ANISOU  621  CB  VAL A  48     1814   2071   2078   -450    326    -64       C
ATOM    622  CG1 VAL A  48       8.440  16.006  15.882  1.00 19.30           C
ANISOU  622  CG1 VAL A  48     2375   2590   2367   -590    372    -64       C
ATOM    623  CG2 VAL A  48       6.886  15.760  13.932  1.00 16.88           C
ANISOU  623  CG2 VAL A  48     1871   2244   2298   -520    363   -120       C
ATOM    624  H   VAL A  48       6.975  18.593  13.983  1.00 18.90           H
ATOM    625  HA  VAL A  48       9.539  17.807  14.189  1.00 18.05           H
ATOM    626  HB  VAL A  48       8.917  15.517  13.973  1.00 18.84           H
ATOM    627 HG11 VAL A  48       8.213  15.100  16.143  1.00 23.17           H
ATOM    628 HG12 VAL A  48       9.359  16.200  16.126  1.00 23.17           H
ATOM    629 HG13 VAL A  48       7.843  16.635  16.315  1.00 23.17           H
ATOM    630 HG21 VAL A  48       6.657  14.897  14.311  1.00 20.27           H
ATOM    631 HG22 VAL A  48       6.263  16.434  14.244  1.00 20.27           H
ATOM    632 HG23 VAL A  48       6.863  15.711  12.963  1.00 20.27           H
ATOM    633  N   TRP A  49       9.792  17.105  11.847  1.00 14.84           N
ANISOU  633  N   TRP A  49     1709   1844   2087   -225    256    -23       N
ATOM    634  CA  TRP A  49       9.956  16.765  10.437  1.00 14.52           C
ANISOU  634  CA  TRP A  49     1750   1769   1999   -205    245     -2       C
ATOM    635  C   TRP A  49       9.669  15.270  10.276  1.00 16.09           C
ANISOU  635  C   TRP A  49     1989   1949   2176   -203    188    -16       C
ATOM    636  O   TRP A  49      10.250  14.430  10.989  1.00 16.41           O
ANISOU  636  O   TRP A  49     2033   1961   2241   -195    155    -27       O
ATOM    637  CB  TRP A  49      11.395  17.022   9.974  1.00 15.29           C
ANISOU  637  CB  TRP A  49     1847   1880   2083   -214    348    -38       C
ATOM    638  CG  TRP A  49      11.708  18.451   9.719  1.00 16.43           C
ANISOU  638  CG  TRP A  49     2017   1997   2229   -276    407      2       C
ATOM    639  CD1 TRP A  49      12.524  19.285  10.455  1.00 15.80           C
ANISOU  639  CD1 TRP A  49     1842   1915   2248   -304    457    -33       C
ATOM    640  CD2 TRP A  49      11.229  19.240   8.626  1.00 15.44           C
ANISOU  640  CD2 TRP A  49     2071   1796   2000   -339    370     96       C
ATOM    641  NE1 TRP A  49      12.536  20.536   9.902  1.00 17.26           N
ANISOU  641  NE1 TRP A  49     2126   2014   2418   -393    477     39       N
ATOM    642  CE2 TRP A  49      11.778  20.532   8.761  1.00 16.68           C
ANISOU  642  CE2 TRP A  49     2252   1882   2204   -421    410    138       C
ATOM    643  CE3 TRP A  49      10.403  18.971   7.519  1.00 18.13           C
ANISOU  643  CE3 TRP A  49     2594   2093   2202   -345    259    155       C
ATOM    644  CZ2 TRP A  49      11.507  21.563   7.850  1.00 18.40           C
ANISOU  644  CZ2 TRP A  49     2714   1951   2326   -521    327    274       C
ATOM    645  CZ3 TRP A  49      10.147  19.985   6.618  1.00 18.16           C
ANISOU  645  CZ3 TRP A  49     2843   1970   2089   -425    153    281       C
ATOM    646  CH2 TRP A  49      10.696  21.263   6.779  1.00 19.49           C
ANISOU  646  CH2 TRP A  49     3075   2035   2293   -520    183    357       C
ATOM    647  H   TRP A  49      10.501  16.948  12.308  1.00 17.82           H
ATOM    648  HA  TRP A  49       9.350  17.301   9.901  1.00 17.44           H
ATOM    649  HB2 TRP A  49      12.003  16.705  10.660  1.00 18.36           H
ATOM    650  HB3 TRP A  49      11.546  16.536   9.148  1.00 18.36           H
ATOM    651  HD1 TRP A  49      12.996  19.034  11.216  1.00 18.98           H
ATOM    652  HE1 TRP A  49      12.954  21.217  10.220  1.00 20.73           H
ATOM    653  HE3 TRP A  49      10.036  18.126   7.396  1.00 21.77           H
ATOM    654  HZ2 TRP A  49      11.860  22.415   7.965  1.00 22.09           H
ATOM    655  HZ3 TRP A  49       9.598  19.815   5.887  1.00 21.81           H
ATOM    656  HH2 TRP A  49      10.509  21.921   6.149  1.00 23.39           H
ATOM    657  N   VAL A  50       8.786  14.920   9.334  1.00 15.41           N
ANISOU  657  N   VAL A  50     1958   1838   2060   -206    120    -19       N
ATOM    658  CA  VAL A  50       8.405  13.535   9.037  1.00 15.23           C
ANISOU  658  CA  VAL A  50     1981   1764   2041   -218     43    -51       C
ATOM    659  C   VAL A  50       8.911  13.192   7.645  1.00 15.60           C
ANISOU  659  C   VAL A  50     2136   1804   1986   -176     42   -124       C
ATOM    660  O   VAL A  50       8.621  13.916   6.681  1.00 17.34           O
ANISOU  660  O   VAL A  50     2457   2043   2088   -190     23   -104       O
ATOM    661  CB  VAL A  50       6.878  13.376   9.073  1.00 16.94           C
ANISOU  661  CB  VAL A  50     2138   1970   2329   -282    -42    -60       C
ATOM    662  CG1 VAL A  50       6.499  11.934   8.801  1.00 18.79           C
ANISOU  662  CG1 VAL A  50     2427   2122   2591   -333   -128    -91       C
ATOM    663  CG2 VAL A  50       6.327  13.838  10.428  1.00 18.57           C
ANISOU  663  CG2 VAL A  50     2211   2238   2606   -370     48    -60       C
ATOM    664  H   VAL A  50       8.379  15.490   8.835  1.00 18.51           H
ATOM    665  HA  VAL A  50       8.816  12.942   9.685  1.00 18.29           H
ATOM    666  HB  VAL A  50       6.481  13.930   8.383  1.00 20.34           H
ATOM    667 HG11 VAL A  50       5.562  11.808   9.015  1.00 22.56           H
ATOM    668 HG12 VAL A  50       6.653  11.738   7.864  1.00 22.56           H
ATOM    669 HG13 VAL A  50       7.046  11.354   9.354  1.00 22.56           H
ATOM    670 HG21 VAL A  50       5.375  13.655  10.460  1.00 22.29           H
ATOM    671 HG22 VAL A  50       6.781  13.353  11.135  1.00 22.29           H
ATOM    672 HG23 VAL A  50       6.485  14.790  10.526  1.00 22.29           H
ATOM    673  N   ILE A  51       9.635  12.082   7.535  1.00 16.54           N
ANISOU  673  N   ILE A  51     2265   1877   2143   -131     38   -225       N
ATOM    674  CA  ILE A  51      10.158  11.636   6.250  1.00 17.07           C
ANISOU  674  CA  ILE A  51     2409   1966   2109   -102     90   -384       C
ATOM    675  C   ILE A  51       9.720  10.190   6.040  1.00 19.23           C
ANISOU  675  C   ILE A  51     2724   2115   2467    -65    -68   -480       C
ATOM    676  O   ILE A  51      10.279   9.266   6.644  1.00 18.58           O
ANISOU  676  O   ILE A  51     2593   1911   2557      5   -148   -548       O
ATOM    677  CB  ILE A  51      11.682  11.739   6.130  1.00 20.45           C
ANISOU  677  CB  ILE A  51     2735   2460   2574    -62    270   -549       C
ATOM    678  CG1 ILE A  51      12.208  13.088   6.623  1.00 24.62           C
ANISOU  678  CG1 ILE A  51     3195   3070   3092   -123    405   -451       C
ATOM    679  CG2 ILE A  51      12.114  11.541   4.675  1.00 25.29           C
ANISOU  679  CG2 ILE A  51     3440   3169   3001   -107    430   -754       C
ATOM    680  CD1 ILE A  51      12.931  12.994   7.945  1.00 29.19           C
ANISOU  680  CD1 ILE A  51     3601   3600   3891    -45    344   -464       C
ATOM    681  H   ILE A  51       9.836  11.569   8.195  1.00 19.86           H
ATOM    682  HA  ILE A  51       9.761  12.195   5.564  1.00 20.49           H
ATOM    683  HB  ILE A  51      12.055  11.040   6.691  1.00 24.55           H
ATOM    684 HG12 ILE A  51      12.828  13.443   5.967  1.00 29.56           H
ATOM    685 HG13 ILE A  51      11.460  13.696   6.734  1.00 29.56           H
ATOM    686 HG21 ILE A  51      13.080  11.604   4.621  1.00 30.37           H
ATOM    687 HG22 ILE A  51      11.822  10.667   4.374  1.00 30.37           H
ATOM    688 HG23 ILE A  51      11.706  12.232   4.128  1.00 30.37           H
ATOM    689 HD11 ILE A  51      13.233  13.879   8.203  1.00 35.04           H
ATOM    690 HD12 ILE A  51      12.322  12.643   8.614  1.00 35.04           H
ATOM    691 HD13 ILE A  51      13.692  12.400   7.847  1.00 35.04           H
ATOM    692  N   ARG A  52       8.790   9.982   5.124  1.00 18.76           N
ANISOU  692  N   ARG A  52     2778   2049   2302   -103   -162   -502       N
ATOM    693  CA  ARG A  52       8.348   8.650   4.743  1.00 20.15           C
ANISOU  693  CA  ARG A  52     3006   2094   2558    -86   -322   -625       C
ATOM    694  C   ARG A  52       9.322   8.055   3.745  1.00 24.27           C
ANISOU  694  C   ARG A  52     3578   2638   3007     -5   -239   -901       C
ATOM    695  O   ARG A  52       9.785   8.727   2.829  1.00 24.61           O
ANISOU  695  O   ARG A  52     3703   2842   2805    -42    -64   -985       O
ATOM    696  CB  ARG A  52       6.962   8.728   4.118  1.00 21.42           C
ANISOU  696  CB  ARG A  52     3235   2245   2658   -157   -486   -590       C
ATOM    697  CG  ARG A  52       6.322   7.403   3.666  1.00 22.15           C
ANISOU  697  CG  ARG A  52     3377   2188   2851   -174   -682   -727       C
ATOM    698  CD  ARG A  52       5.040   7.754   2.902  1.00 25.07           C
ANISOU  698  CD  ARG A  52     3787   2579   3159   -226   -875   -730       C
ATOM    699  NE  ARG A  52       4.361   6.582   2.368  1.00 33.27           N
ANISOU  699  NE  ARG A  52     4863   3479   4298   -259  -1086   -886       N
ATOM    700  CZ  ARG A  52       3.245   6.640   1.656  1.00 37.14           C
ANISOU  700  CZ  ARG A  52     5365   3956   4790   -291  -1322   -944       C
ATOM    701  NH1 ARG A  52       2.651   7.797   1.396  1.00 34.44           N
ANISOU  701  NH1 ARG A  52     5014   3694   4376   -273  -1435   -866       N
ATOM    702  NH2 ARG A  52       2.702   5.513   1.210  1.00 34.74           N
ANISOU  702  NH2 ARG A  52     5045   3562   4592   -314  -1431  -1048       N
ATOM    703  H   ARG A  52       8.388  10.610   4.697  1.00 22.53           H
ATOM    704  HA  ARG A  52       8.305   8.074   5.522  1.00 24.20           H
ATOM    705  HB2 ARG A  52       6.362   9.123   4.770  1.00 25.71           H
ATOM    706  HB3 ARG A  52       7.020   9.296   3.334  1.00 25.71           H
ATOM    707  HG2 ARG A  52       6.924   6.920   3.079  1.00 26.59           H
ATOM    708  HG3 ARG A  52       6.099   6.856   4.435  1.00 26.59           H
ATOM    709  HD2 ARG A  52       4.428   8.207   3.503  1.00 30.09           H
ATOM    710  HD3 ARG A  52       5.265   8.335   2.158  1.00 30.09           H
ATOM    711  HE  ARG A  52       4.703   5.809   2.524  1.00 39.93           H
ATOM    712 HH11 ARG A  52       2.989   8.530   1.692  1.00 41.34           H
ATOM    713 HH12 ARG A  52       1.927   7.814   0.932  1.00 41.34           H
ATOM    714 HH21 ARG A  52       3.075   4.758   1.384  1.00 41.70           H
ATOM    715 HH22 ARG A  52       1.978   5.539   0.747  1.00 41.70           H
ATOM    716  N   GLN A  53       9.627   6.778   3.934  1.00 27.53           N
ANISOU  716  N   GLN A  53     3955   2873   3633     83   -365  -1061       N
ATOM    717  CA  GLN A  53      10.629   6.068   3.166  1.00 32.28           C
ANISOU  717  CA  GLN A  53     4521   3469   4276    202   -294  -1423       C
ATOM    718  C   GLN A  53       9.912   5.244   2.097  1.00 33.20           C
ANISOU  718  C   GLN A  53     4793   3524   4298    186   -424  -1603       C
ATOM    719  O   GLN A  53       8.702   5.046   2.164  1.00 28.58           O
ANISOU  719  O   GLN A  53     4299   2844   3714     99   -624  -1436       O
ATOM    720  CB  GLN A  53      11.431   5.176   4.119  1.00 36.65           C
ANISOU  720  CB  GLN A  53     4934   3795   5195    354   -452  -1499       C
ATOM    721  CG  GLN A  53      11.879   5.887   5.426  1.00 31.60           C
ANISOU  721  CG  GLN A  53     4200   3152   4656    356   -452  -1276       C
ATOM    722  CD  GLN A  53      12.954   6.904   5.163  1.00 34.69           C
ANISOU  722  CD  GLN A  53     4418   3785   4980    376   -157  -1412       C
ATOM    723  OE1 GLN A  53      13.878   6.646   4.385  1.00 39.92           O
ANISOU  723  OE1 GLN A  53     4942   4548   5678    440     -2  -1713       O
ATOM    724  NE2 GLN A  53      12.833   8.080   5.787  1.00 29.96           N
ANISOU  724  NE2 GLN A  53     3809   3310   4264    274    -52  -1151       N
ATOM    725  H   GLN A  53       9.250   6.284   4.528  1.00 33.05           H
ATOM    726  HA  GLN A  53      11.252   6.664   2.720  1.00 38.75           H
ATOM    727  HB2 GLN A  53      10.882   4.417   4.369  1.00 43.99           H
ATOM    728  HB3 GLN A  53      12.230   4.871   3.660  1.00 43.99           H
ATOM    729  HG2 GLN A  53      11.119   6.342   5.820  1.00 37.93           H
ATOM    730  HG3 GLN A  53      12.229   5.227   6.045  1.00 37.93           H
ATOM    731 HE21 GLN A  53      12.165   8.224   6.309  1.00 35.96           H
ATOM    732 HE22 GLN A  53      13.424   8.693   5.667  1.00 35.96           H
ATOM    733  N   LYS A  54      10.673   4.770   1.108  1.00 33.99           N
ANISOU  733  N   LYS A  54     4883   3715   4318    237   -271  -1884       N
ATOM    734  CA  LYS A  54      10.086   4.004   0.014  1.00 41.28           C
ANISOU  734  CA  LYS A  54     5963   4613   5108    203   -358  -2027       C
ATOM    735  C   LYS A  54       9.479   2.681   0.458  1.00 30.88           C
ANISOU  735  C   LYS A  54     4606   3016   4110    259   -660  -1985       C
ATOM    736  O   LYS A  54       8.730   2.078  -0.315  1.00 33.95           O
ANISOU  736  O   LYS A  54     5111   3362   4427    210   -781  -2061       O
ATOM    737  CB  LYS A  54      11.164   3.686  -1.020  1.00 40.91           C
ANISOU  737  CB  LYS A  54     5897   4707   4939    246   -108  -2350       C
ATOM    738  CG  LYS A  54      11.508   4.830  -1.945  1.00 64.36           C
ANISOU  738  CG  LYS A  54     9039   7966   7448    107    190  -2370       C
ATOM    739  CD  LYS A  54      12.799   4.566  -2.708  1.00 65.67           C
ANISOU  739  CD  LYS A  54     9071   8298   7584    134    495  -2682       C
ATOM    740  CE  LYS A  54      13.597   5.856  -2.875  1.00 80.34           C
ANISOU  740  CE  LYS A  54    10881  10425   9220    -19    840  -2604       C
ATOM    741  NZ  LYS A  54      12.821   6.931  -3.561  1.00 80.99           N
ANISOU  741  NZ  LYS A  54    11329  10642   8803   -219    848  -2352       N
ATOM    742  H   LYS A  54      11.524   4.879   1.049  1.00 40.80           H
ATOM    743  HA  LYS A  54       9.386   4.549  -0.378  1.00 49.55           H
ATOM    744  HB2 LYS A  54      11.976   3.435  -0.551  1.00 49.10           H
ATOM    745  HB3 LYS A  54      10.856   2.948  -1.569  1.00 49.10           H
ATOM    746  HG2 LYS A  54      10.793   4.949  -2.589  1.00 77.24           H
ATOM    747  HG3 LYS A  54      11.623   5.641  -1.424  1.00 77.24           H
ATOM    748  HD2 LYS A  54      13.342   3.928  -2.218  1.00 78.82           H
ATOM    749  HD3 LYS A  54      12.591   4.216  -3.588  1.00 78.82           H
ATOM    750  HE2 LYS A  54      13.854   6.184  -1.999  1.00 96.42           H
ATOM    751  HE3 LYS A  54      14.388   5.672  -3.405  1.00 96.42           H
ATOM    752  HZ1 LYS A  54      13.317   7.667  -3.631  1.00 97.20           H
ATOM    753  HZ2 LYS A  54      12.586   6.663  -4.377  1.00 97.20           H
ATOM    754  HZ3 LYS A  54      12.086   7.120  -3.096  1.00 97.20           H
ATOM    755  N   ASP A  55       9.797   2.196   1.655  1.00 34.96           N
ANISOU  755  N   ASP A  55     4994   3337   4951    337   -796  -1855       N
ATOM    756  CA  ASP A  55       9.185   0.990   2.198  1.00 37.76           C
ANISOU  756  CA  ASP A  55     5379   3413   5556    329  -1081  -1739       C
ATOM    757  C   ASP A  55       8.033   1.294   3.140  1.00 36.40           C
ANISOU  757  C   ASP A  55     5273   3159   5398    144  -1187  -1394       C
ATOM    758  O   ASP A  55       7.504   0.384   3.783  1.00 35.50           O
ANISOU  758  O   ASP A  55     5208   2828   5452     62  -1370  -1243       O
ATOM    759  CB  ASP A  55      10.235   0.121   2.894  1.00 36.17           C
ANISOU  759  CB  ASP A  55     5064   3023   5657    497  -1225  -1795       C
ATOM    760  CG  ASP A  55      10.699   0.701   4.211  1.00 42.87           C
ANISOU  760  CG  ASP A  55     5867   3839   6583    500  -1255  -1561       C
ATOM    761  OD1 ASP A  55      10.552   1.917   4.416  1.00 36.86           O
ANISOU  761  OD1 ASP A  55     5104   3252   5649    416  -1069  -1448       O
ATOM    762  OD2 ASP A  55      11.212  -0.061   5.054  1.00 41.34           O
ANISOU  762  OD2 ASP A  55     5661   3433   6613    583  -1501  -1490       O
ATOM    763  H   ASP A  55      10.375   2.556   2.181  1.00 41.96           H
ATOM    764  HA  ASP A  55       8.830   0.470   1.460  1.00 45.33           H
ATOM    765  HB2 ASP A  55       9.854  -0.754   3.070  1.00 43.42           H
ATOM    766  HB3 ASP A  55      11.008   0.036   2.315  1.00 43.42           H
ATOM    767  N   ASP A  56       7.648   2.563   3.244  1.00 28.95           N
ANISOU  767  N   ASP A  56     4330   2394   4276     52  -1059  -1277       N
ATOM    768  CA  ASP A  56       6.581   3.084   4.098  1.00 30.10           C
ANISOU  768  CA  ASP A  56     4470   2531   4435   -138  -1092  -1002       C
ATOM    769  C   ASP A  56       6.940   3.156   5.576  1.00 32.94           C
ANISOU  769  C   ASP A  56     4821   2793   4900   -194  -1083   -770       C
ATOM    770  O   ASP A  56       6.070   3.461   6.390  1.00 32.71           O
ANISOU  770  O   ASP A  56     4782   2777   4870   -397  -1051   -559       O
ATOM    771  CB  ASP A  56       5.251   2.353   3.930  1.00 30.94           C
ANISOU  771  CB  ASP A  56     4582   2549   4625   -294  -1224   -953       C
ATOM    772  CG  ASP A  56       4.592   2.654   2.620  1.00 31.44           C
ANISOU  772  CG  ASP A  56     4658   2744   4542   -277  -1273  -1113       C
ATOM    773  OD1 ASP A  56       5.003   3.635   1.973  1.00 32.36           O
ANISOU  773  OD1 ASP A  56     4825   3040   4431   -199  -1192  -1188       O
ATOM    774  OD2 ASP A  56       3.647   1.938   2.267  1.00 32.46           O
ANISOU  774  OD2 ASP A  56     4772   2797   4764   -361  -1404  -1148       O
ATOM    775  H   ASP A  56       8.022   3.192   2.792  1.00 34.75           H
ATOM    776  HA  ASP A  56       6.436   3.999   3.810  1.00 36.13           H
ATOM    777  HB2 ASP A  56       5.407   1.397   3.976  1.00 37.14           H
ATOM    778  HB3 ASP A  56       4.649   2.626   4.640  1.00 37.14           H
ATOM    779  N   SER A  57       8.169   2.827   5.949  1.00 29.06           N
ANISOU  779  N   SER A  57     4323   2220   4499    -32  -1116   -822       N
ATOM    780  CA  SER A  57       8.651   3.219   7.268  1.00 29.69           C
ANISOU  780  CA  SER A  57     4420   2259   4601    -62  -1123   -613       C
ATOM    781  C   SER A  57       8.831   4.731   7.302  1.00 27.35           C
ANISOU  781  C   SER A  57     4029   2198   4163    -63   -907   -593       C
ATOM    782  O   SER A  57       8.866   5.399   6.270  1.00 27.10           O
ANISOU  782  O   SER A  57     3922   2384   3992     -5   -742   -731       O
ATOM    783  CB  SER A  57       9.999   2.584   7.570  1.00 32.29           C
ANISOU  783  CB  SER A  57     4711   2466   5093    155  -1273   -717       C
ATOM    784  OG  SER A  57      10.991   3.031   6.665  1.00 36.27           O
ANISOU  784  OG  SER A  57     5030   3129   5622    352  -1120  -1026       O
ATOM    785  H   SER A  57       8.732   2.388   5.470  1.00 34.89           H
ATOM    786  HA  SER A  57       8.009   2.929   7.935  1.00 35.64           H
ATOM    787  HB2 SER A  57      10.265   2.825   8.471  1.00 38.76           H
ATOM    788  HB3 SER A  57       9.916   1.621   7.495  1.00 38.76           H
ATOM    789  HG  SER A  57      11.735   2.698   6.867  1.00 43.53           H
ATOM    790  N   LEU A  58       8.989   5.287   8.511  1.00 24.87           N
ANISOU  790  N   LEU A  58     3724   1915   3810   -138   -869   -376       N
ATOM    791  CA  LEU A  58       9.180   6.720   8.694  1.00 24.36           C
ANISOU  791  CA  LEU A  58     3531   2126   3599   -134   -637   -315       C
ATOM    792  C   LEU A  58      10.362   7.009   9.610  1.00 24.51           C
ANISOU  792  C   LEU A  58     3522   2115   3674    -34   -677   -288       C
ATOM    793  O   LEU A  58      10.716   6.221  10.490  1.00 26.54           O
ANISOU  793  O   LEU A  58     3917   2136   4031    -32   -919   -209       O
ATOM    794  CB  LEU A  58       7.910   7.374   9.269  1.00 32.97           C
ANISOU  794  CB  LEU A  58     4606   3338   4583   -350   -524   -132       C
ATOM    795  CG  LEU A  58       6.634   7.154   8.459  1.00 35.57           C
ANISOU  795  CG  LEU A  58     4901   3687   4926   -448   -539   -187       C
ATOM    796  CD1 LEU A  58       5.622   6.446   9.344  1.00 33.46           C
ANISOU  796  CD1 LEU A  58     4685   3306   4722   -717   -571    -67       C
ATOM    797  CD2 LEU A  58       6.036   8.417   7.914  1.00 31.70           C
ANISOU  797  CD2 LEU A  58     4278   3408   4358   -427   -431   -212       C
ATOM    798  H   LEU A  58       8.989   4.843   9.247  1.00 29.85           H
ATOM    799  HA  LEU A  58       9.385   7.118   7.834  1.00 29.24           H
ATOM    800  HB2 LEU A  58       7.756   7.013  10.156  1.00 39.58           H
ATOM    801  HB3 LEU A  58       8.058   8.332   9.321  1.00 39.58           H
ATOM    802  HG  LEU A  58       6.861   6.618   7.683  1.00 42.69           H
ATOM    803 HD11 LEU A  58       4.796   6.332   8.849  1.00 40.17           H
ATOM    804 HD12 LEU A  58       5.978   5.580   9.599  1.00 40.17           H
ATOM    805 HD13 LEU A  58       5.463   6.985  10.134  1.00 40.17           H
ATOM    806 HD21 LEU A  58       5.236   8.197   7.412  1.00 38.05           H
ATOM    807 HD22 LEU A  58       5.812   9.005   8.653  1.00 38.05           H
ATOM    808 HD23 LEU A  58       6.682   8.848   7.333  1.00 38.05           H
ATOM    809  N   LYS A  59      10.995   8.139   9.362  1.00 19.34           N
ANISOU  809  N   LYS A  59     2713   1673   2963     38   -483   -357       N
ATOM    810  CA  LYS A  59      11.880   8.761  10.339  1.00 20.99           C
ANISOU  810  CA  LYS A  59     2860   1909   3208     84   -495   -313       C
ATOM    811  C   LYS A  59      11.262  10.088  10.731  1.00 18.15           C
ANISOU  811  C   LYS A  59     2469   1750   2677    -46   -298   -165       C
ATOM    812  O   LYS A  59      10.713  10.800   9.889  1.00 17.00           O
ANISOU  812  O   LYS A  59     2275   1744   2441    -81   -136   -181       O
ATOM    813  CB  LYS A  59      13.279   9.000   9.776  1.00 23.62           C
ANISOU  813  CB  LYS A  59     2980   2300   3694    260   -426   -581       C
ATOM    814  CG  LYS A  59      14.081   7.714   9.623  1.00 30.83           C
ANISOU  814  CG  LYS A  59     3848   2981   4885    450   -675   -818       C
ATOM    815  CD  LYS A  59      15.234   7.867   8.654  1.00 36.42           C
ANISOU  815  CD  LYS A  59     4268   3817   5753    586   -484  -1211       C
ATOM    816  CE  LYS A  59      15.914   6.523   8.410  1.00 39.19           C
ANISOU  816  CE  LYS A  59     4522   4037   6330    731   -714  -1411       C
ATOM    817  NZ  LYS A  59      17.133   6.354   9.238  1.00 44.77           N
ANISOU  817  NZ  LYS A  59     5038   4676   7296    847   -960  -1507       N
ATOM    818  H   LYS A  59      10.929   8.575   8.624  1.00 23.22           H
ATOM    819  HA  LYS A  59      11.978   8.188  11.115  1.00 25.20           H
ATOM    820  HB2 LYS A  59      13.201   9.412   8.901  1.00 28.35           H
ATOM    821  HB3 LYS A  59      13.764   9.587  10.376  1.00 28.35           H
ATOM    822  HG2 LYS A  59      14.444   7.461  10.486  1.00 37.01           H
ATOM    823  HG3 LYS A  59      13.498   7.014   9.290  1.00 37.01           H
ATOM    824  HD2 LYS A  59      14.903   8.205   7.807  1.00 43.72           H
ATOM    825  HD3 LYS A  59      15.888   8.481   9.023  1.00 43.72           H
ATOM    826  HE2 LYS A  59      15.296   5.809   8.631  1.00 47.03           H
ATOM    827  HE3 LYS A  59      16.171   6.461   7.477  1.00 47.03           H
ATOM    828  HZ1 LYS A  59      17.727   6.986   9.038  1.00 53.73           H
ATOM    829  HZ2 LYS A  59      16.926   6.415  10.101  1.00 53.73           H
ATOM    830  HZ3 LYS A  59      17.497   5.556   9.084  1.00 53.73           H
ATOM    831  N   VAL A  60      11.339  10.429  12.016  1.00 16.50           N
ANISOU  831  N   VAL A  60     2315   1533   2420   -113   -351    -36       N
ATOM    832  CA  VAL A  60      10.727  11.644  12.547  1.00 16.16           C
ANISOU  832  CA  VAL A  60     2229   1661   2251   -225   -179     46       C
ATOM    833  C   VAL A  60      11.738  12.341  13.438  1.00 16.03           C
ANISOU  833  C   VAL A  60     2173   1671   2245   -175   -216     32       C
ATOM    834  O   VAL A  60      12.288  11.721  14.360  1.00 17.68           O
ANISOU  834  O   VAL A  60     2515   1749   2456   -166   -435     80       O
ATOM    835  CB  VAL A  60       9.432  11.333  13.321  1.00 16.28           C
ANISOU  835  CB  VAL A  60     2360   1681   2147   -442   -148    167       C
ATOM    836  CG1 VAL A  60       8.896  12.616  13.954  1.00 18.98           C
ANISOU  836  CG1 VAL A  60     2598   2202   2410   -524     35    153       C
ATOM    837  CG2 VAL A  60       8.390  10.671  12.439  1.00 18.12           C
ANISOU  837  CG2 VAL A  60     2579   1880   2425   -504   -135    145       C
ATOM    838  H   VAL A  60      11.749   9.962  12.611  1.00 19.81           H
ATOM    839  HA  VAL A  60      10.508  12.244  11.817  1.00 19.40           H
ATOM    840  HB  VAL A  60       9.633  10.699  14.027  1.00 19.55           H
ATOM    841 HG11 VAL A  60       7.973  12.475  14.218  1.00 22.78           H
ATOM    842 HG12 VAL A  60       9.433  12.833  14.731  1.00 22.78           H
ATOM    843 HG13 VAL A  60       8.948  13.334  13.304  1.00 22.78           H
ATOM    844 HG21 VAL A  60       7.554  10.614  12.927  0.65 21.75           H
ATOM    845 HG22 VAL A  60       8.270  11.203  11.638  1.00 21.75           H
ATOM    846 HG23 VAL A  60       8.696   9.781  12.202  0.82 21.75           H
ATOM    847  N   PHE A  61      11.992  13.608  13.156  1.00 14.97           N
ANISOU  847  N   PHE A  61     1892   1670   2126   -149    -56    -27       N
ATOM    848  CA  PHE A  61      12.976  14.379  13.889  1.00 14.37           C
ANISOU  848  CA  PHE A  61     1741   1620   2101   -109    -87    -77       C
ATOM    849  C   PHE A  61      12.374  15.653  14.452  1.00 14.79           C
ANISOU  849  C   PHE A  61     1772   1782   2065   -196     41    -49       C
ATOM    850  O   PHE A  61      11.477  16.255  13.857  1.00 15.77           O
ANISOU  850  O   PHE A  61     1858   1961   2174   -231    171    -40       O
ATOM    851  CB  PHE A  61      14.150  14.815  12.968  1.00 15.09           C
ANISOU  851  CB  PHE A  61     1632   1742   2361    -18      3   -239       C
ATOM    852  CG  PHE A  61      14.858  13.673  12.335  1.00 16.69           C
ANISOU  852  CG  PHE A  61     1769   1859   2712     96    -83   -385       C
ATOM    853  CD1 PHE A  61      15.760  12.928  13.068  1.00 19.28           C
ANISOU  853  CD1 PHE A  61     2057   2046   3222    224   -361   -480       C
ATOM    854  CD2 PHE A  61      14.658  13.330  11.003  1.00 18.40           C
ANISOU  854  CD2 PHE A  61     1971   2116   2904     93     69   -466       C
ATOM    855  CE1 PHE A  61      16.421  11.856  12.497  1.00 20.23           C
ANISOU  855  CE1 PHE A  61     2073   2050   3563    376   -486   -684       C
ATOM    856  CE2 PHE A  61      15.327  12.275  10.421  1.00 20.67           C
ANISOU  856  CE2 PHE A  61     2168   2332   3352    212      8   -680       C
ATOM    857  CZ  PHE A  61      16.201  11.526  11.179  1.00 20.05           C
ANISOU  857  CZ  PHE A  61     1999   2095   3525    369   -272   -806       C
ATOM    858  H   PHE A  61      11.598  14.050  12.532  1.00 17.98           H
ATOM    859  HA  PHE A  61      13.294  13.824  14.618  1.00 17.26           H
ATOM    860  HB2 PHE A  61      13.801  15.378  12.260  1.00 18.12           H
ATOM    861  HB3 PHE A  61      14.796  15.309  13.497  1.00 18.12           H
ATOM    862  HD1 PHE A  61      15.926  13.150  13.955  1.00 23.15           H
ATOM    863  HD2 PHE A  61      14.058  13.825  10.492  1.00 22.09           H
ATOM    864  HE1 PHE A  61      17.017  11.355  13.006  1.00 24.29           H
ATOM    865  HE2 PHE A  61      15.189  12.070   9.524  1.00 24.81           H
ATOM    866  HZ  PHE A  61      16.641  10.799  10.801  1.00 24.08           H
ATOM    867  N   SER A  62      12.884  16.102  15.599  1.00 14.29           N
ANISOU  867  N   SER A  62     1732   1729   1967   -212    -40    -70       N
ATOM    868  CA  SER A  62      12.551  17.445  16.067  1.00 15.06           C
ANISOU  868  CA  SER A  62     1767   1915   2040   -261     77   -123       C
ATOM    869  C   SER A  62      12.978  18.480  15.032  1.00 14.70           C
ANISOU  869  C   SER A  62     1567   1860   2156   -214    183   -176       C
ATOM    870  O   SER A  62      14.016  18.360  14.394  1.00 14.76           O
ANISOU  870  O   SER A  62     1489   1839   2282   -174    185   -221       O
ATOM    871  CB  SER A  62      13.245  17.741  17.395  1.00 14.77           C
ANISOU  871  CB  SER A  62     1796   1881   1933   -280    -62   -173       C
ATOM    872  OG  SER A  62      12.922  19.015  17.890  1.00 15.45           O
ANISOU  872  OG  SER A  62     1822   2042   2008   -320     44   -273       O
ATOM    873  H   SER A  62      13.413  15.659  16.112  1.00 17.16           H
ATOM    874  HA  SER A  62      11.593  17.507  16.205  1.00 18.08           H
ATOM    875  HB2 SER A  62      12.969  17.077  18.045  1.00 17.73           H
ATOM    876  HB3 SER A  62      14.205  17.695  17.260  1.00 17.73           H
ATOM    877  HG  SER A  62      12.185  19.268  17.574  1.00 18.56           H
ATOM    878  N   THR A  63      12.234  19.581  14.984  1.00 17.52           N
ANISOU  878  N   THR A  63     1893   2724   2041   -568    828   -129       N
ATOM    879  CA  THR A  63      12.658  20.758  14.241  1.00 15.96           C
ANISOU  879  CA  THR A  63     1641   2503   1921   -387    728   -153       C
ATOM    880  C   THR A  63      13.689  21.597  14.990  1.00 15.46           C
ANISOU  880  C   THR A  63     1684   2336   1854   -285    672   -131       C
ATOM    881  O   THR A  63      14.210  22.550  14.407  1.00 17.10           O
ANISOU  881  O   THR A  63     1911   2476   2111   -198    606   -141       O
ATOM    882  CB  THR A  63      11.433  21.619  13.938  1.00 20.75           C
ANISOU  882  CB  THR A  63     2074   3310   2500   -282    736   -257       C
ATOM    883  OG1 THR A  63      10.823  21.995  15.186  1.00 22.06           O
ANISOU  883  OG1 THR A  63     2201   3608   2571   -255    802   -310       O
ATOM    884  CG2 THR A  63      10.407  20.903  13.044  1.00 21.69           C
ANISOU  884  CG2 THR A  63     2032   3594   2615   -379    756   -318       C
ATOM    885  H   THR A  63      11.475  19.669  15.377  1.00 21.04           H
ATOM    886  HA  THR A  63      13.061  20.479  13.404  1.00 19.17           H
ATOM    887  HB  THR A  63      11.714  22.405  13.444  1.00 24.91           H
ATOM    888  HG1 THR A  63      10.127  22.443  15.042  1.00 26.48           H
ATOM    889 HG21 THR A  63       9.640  21.477  12.893  1.00 26.04           H
ATOM    890 HG22 THR A  63      10.809  20.683  12.189  1.00 26.04           H
ATOM    891 HG23 THR A  63      10.109  20.085  13.471  1.00 26.04           H
ATOM    892  N  AASN A  64      14.028  21.247  16.229  0.41 17.16           N
ANISOU  892  N  AASN A  64     1992   2536   1994   -315    699   -105       N
ATOM    893  CA AASN A  64      14.909  22.045  17.089  0.41 18.87           C
ANISOU  893  CA AASN A  64     2283   2707   2180   -235    640   -121       C
ATOM    894  C  AASN A  64      16.358  21.624  16.886  0.41 15.93           C
ANISOU  894  C  AASN A  64     1969   2256   1830   -232    559    -79       C
ATOM    895  O  AASN A  64      16.703  20.462  17.138  0.41 16.90           O
ANISOU  895  O  AASN A  64     2174   2352   1897   -238    563    -20       O
ATOM    896  CB AASN A  64      14.498  21.812  18.548  0.41 21.43           C
ANISOU  896  CB AASN A  64     2667   3102   2373   -243    704   -126       C
ATOM    897  CG AASN A  64      15.240  22.694  19.542  0.41 22.95           C
ANISOU  897  CG AASN A  64     2930   3282   2509   -157    637   -176       C
ATOM    898  OD1AASN A  64      15.257  23.913  19.415  0.41 30.66           O
ANISOU  898  OD1AASN A  64     3898   4233   3517    -96    594   -254       O
ATOM    899  ND2AASN A  64      15.833  22.071  20.547  0.41 29.45           N
ANISOU  899  ND2AASN A  64     3859   4109   3223   -147    623   -140       N
ATOM    900  H  AASN A  64      13.752  20.527  16.611  0.41 20.61           H
ATOM    901  HA AASN A  64      14.841  22.985  16.860  0.41 22.65           H
ATOM    902  HB2AASN A  64      13.550  21.997  18.639  0.41 25.73           H
ATOM    903  HB3AASN A  64      14.679  20.887  18.780  0.41 25.73           H
ATOM    904 HD21AASN A  64      16.266  22.523  21.137  0.41 35.35           H
ATOM    905 HD22AASN A  64      15.785  21.215  20.611  0.41 35.35           H
ATOM    906  N  BASN A  64      13.989  21.276  16.234  0.59 17.05           N
ANISOU  906  N  BASN A  64     1973   2525   1978   -314    701   -107       N
ATOM    907  CA BASN A  64      14.940  22.071  16.999  0.59 18.84           C
ANISOU  907  CA BASN A  64     2277   2699   2184   -234    635   -121       C
ATOM    908  C  BASN A  64      16.367  21.625  16.746  0.59 16.01           C
ANISOU  908  C  BASN A  64     1971   2261   1850   -234    557    -78       C
ATOM    909  O  BASN A  64      16.689  20.435  16.832  0.59 17.05           O
ANISOU  909  O  BASN A  64     2175   2363   1939   -245    562    -18       O
ATOM    910  CB BASN A  64      14.651  21.996  18.490  0.59 19.80           C
ANISOU  910  CB BASN A  64     2460   2883   2179   -227    685   -133       C
ATOM    911  CG BASN A  64      13.392  22.714  18.871  0.59 22.52           C
ANISOU  911  CG BASN A  64     2719   3366   2473   -179    755   -214       C
ATOM    912  OD1BASN A  64      12.962  23.657  18.208  0.59 28.37           O
ANISOU  912  OD1BASN A  64     3395   4125   3261    -78    724   -279       O
ATOM    913  ND2BASN A  64      12.781  22.269  19.951  0.59 32.94           N
ANISOU  913  ND2BASN A  64     4054   4797   3665   -227    854   -214       N
ATOM    914  H  BASN A  64      13.659  20.605  16.659  0.59 20.47           H
ATOM    915  HA BASN A  64      14.853  22.991  16.704  0.59 22.62           H
ATOM    916  HB2BASN A  64      14.557  21.066  18.748  0.59 23.77           H
ATOM    917  HB3BASN A  64      15.387  22.401  18.976  0.59 23.77           H
ATOM    918 HD21BASN A  64      12.054  22.642  20.218  0.59 39.54           H
ATOM    919 HD22BASN A  64      13.110  21.607  20.389  0.59 39.54           H
ATOM    920  N   CYS A  65      17.211  22.572  16.474  1.00 15.30           N
ANISOU  920  N   CYS A  65     1863   2149   1802   -218    490   -120       N
ATOM    921  CA  CYS A  65      18.605  22.262  16.189  1.00 15.26           C
ANISOU  921  CA  CYS A  65     1832   2163   1802   -223    419   -117       C
ATOM    922  C   CYS A  65      19.332  21.836  17.458  1.00 15.10           C
ANISOU  922  C   CYS A  65     1855   2217   1666   -158    366   -134       C
ATOM    923  O   CYS A  65      19.229  22.516  18.502  1.00 16.88           O
ANISOU  923  O   CYS A  65     2116   2468   1830   -154    355   -189       O
ATOM    924  CB  CYS A  65      19.323  23.476  15.595  1.00 16.74           C
ANISOU  924  CB  CYS A  65     1983   2338   2040   -301    389   -175       C
ATOM    925  SG  CYS A  65      21.022  23.190  15.149  1.00 16.61           S
ANISOU  925  SG  CYS A  65     1841   2460   2011   -346    326   -212       S
ATOM    926  HA  CYS A  65      18.626  21.533  15.550  1.00 18.32           H
ATOM    927  HB2 CYS A  65      18.852  23.750  14.792  1.00 20.10           H
ATOM    928  HB3 CYS A  65      19.309  24.193  16.248  1.00 20.10           H
ATOM    929  H  ACYS A  65      17.003  23.398  16.353  0.41 18.37           H
ATOM    930  H  BCYS A  65      17.018  23.410  16.443  0.59 18.37           H
ATOM    931  N   PRO A  66      20.092  20.733  17.413  1.00 16.76           N
ANISOU  931  N   PRO A  66     2084   2466   1818    -66    319   -100       N
ATOM    932  CA  PRO A  66      20.828  20.281  18.606  1.00 18.36           C
ANISOU  932  CA  PRO A  66     2351   2758   1867     67    243   -119       C
ATOM    933  C   PRO A  66      22.013  21.143  19.001  1.00 19.56           C
ANISOU  933  C   PRO A  66     2353   3095   1983     64    140   -248       C
ATOM    934  O   PRO A  66      22.587  20.898  20.088  1.00 20.56           O
ANISOU  934  O   PRO A  66     2511   3342   1960    195     56   -290       O
ATOM    935  CB  PRO A  66      21.277  18.867  18.238  1.00 21.74           C
ANISOU  935  CB  PRO A  66     2881   3156   2222    222    211    -53       C
ATOM    936  CG  PRO A  66      21.347  18.893  16.705  1.00 20.04           C
ANISOU  936  CG  PRO A  66     2545   2921   2146    151    235    -54       C
ATOM    937  CD  PRO A  66      20.195  19.772  16.294  1.00 17.35           C
ANISOU  937  CD  PRO A  66     2165   2494   1933    -34    328    -45       C
ATOM    938  HA  PRO A  66      20.214  20.241  19.356  1.00 22.04           H
ATOM    939  HB2 PRO A  66      22.145  18.679  18.627  1.00 26.10           H
ATOM    940  HB3 PRO A  66      20.626  18.218  18.549  1.00 26.10           H
ATOM    941  HG2 PRO A  66      22.194  19.269  16.417  1.00 24.05           H
ATOM    942  HG3 PRO A  66      21.246  17.996  16.351  1.00 24.05           H
ATOM    943  HD2 PRO A  66      20.388  20.230  15.461  1.00 20.83           H
ATOM    944  HD3 PRO A  66      19.379  19.255  16.206  1.00 20.83           H
ATOM    945  N   HIS A  67      22.396  22.130  18.188  1.00 18.68           N
ANISOU  945  N   HIS A  67     2100   3019   1980    -96    146   -318       N
ATOM    946  CA  HIS A  67      23.421  23.084  18.606  1.00 19.02           C
ANISOU  946  CA  HIS A  67     2013   3233   1983   -203     74   -466       C
ATOM    947  C   HIS A  67      22.845  24.045  19.640  1.00 19.01           C
ANISOU  947  C   HIS A  67     2128   3146   1950   -271     81   -521       C
ATOM    948  O   HIS A  67      23.137  23.919  20.839  1.00 21.18           O
ANISOU  948  O   HIS A  67     2422   3534   2092   -175      8   -580       O
ATOM    949  CB  HIS A  67      23.981  23.816  17.388  1.00 19.34           C
ANISOU  949  CB  HIS A  67     1927   3302   2119   -411    112   -512       C
ATOM    950  CG  HIS A  67      25.000  24.850  17.731  1.00 20.78           C
ANISOU  950  CG  HIS A  67     1988   3653   2255   -624     69   -681       C
ATOM    951  ND1 HIS A  67      24.949  26.131  17.213  1.00 22.59           N
ANISOU  951  ND1 HIS A  67     2299   3739   2546   -908    142   -722       N
ATOM    952  CD2 HIS A  67      26.082  24.815  18.546  1.00 21.98           C
ANISOU  952  CD2 HIS A  67     1964   4106   2282   -614    -40   -833       C
ATOM    953  CE1 HIS A  67      25.962  26.828  17.679  1.00 23.23           C
ANISOU  953  CE1 HIS A  67     2264   4007   2553  -1123     97   -895       C
ATOM    954  NE2 HIS A  67      26.659  26.064  18.508  1.00 24.81           N
ANISOU  954  NE2 HIS A  67     2270   4514   2642   -948    -22   -979       N
ATOM    955  H   HIS A  67      22.081  22.266  17.399  1.00 22.43           H
ATOM    956  HA  HIS A  67      24.165  22.624  19.025  1.00 22.84           H
ATOM    957  HB2 HIS A  67      24.401  23.169  16.800  1.00 23.22           H
ATOM    958  HB3 HIS A  67      23.251  24.260  16.927  1.00 23.22           H
ATOM    959  HD2 HIS A  67      26.380  24.085  19.038  1.00 26.32           H
ATOM    960  HE1 HIS A  67      26.157  27.711  17.463  1.00 27.88           H
ATOM    961  HE2 HIS A  67      27.355  26.308  18.949  1.00 29.78           H
ATOM    962  N   LEU A  68      22.022  25.022  19.205  1.00 17.68           N
ANISOU  962  N   LEU A  68     2061   2782   1875   -396    161   -510       N
ATOM    963  CA  LEU A  68      21.506  26.045  20.108  1.00 20.06           C
ANISOU  963  CA  LEU A  68     2499   2991   2130   -428    164   -587       C
ATOM    964  C   LEU A  68      20.014  26.321  19.879  1.00 19.58           C
ANISOU  964  C   LEU A  68     2574   2750   2117   -349    257   -514       C
ATOM    965  O   LEU A  68      19.522  27.395  20.237  1.00 20.62           O
ANISOU  965  O   LEU A  68     2846   2767   2223   -354    269   -585       O
ATOM    966  CB  LEU A  68      22.350  27.330  20.051  1.00 23.16           C
ANISOU  966  CB  LEU A  68     2909   3370   2519   -661    130   -735       C
ATOM    967  CG  LEU A  68      23.740  27.204  20.662  1.00 23.28           C
ANISOU  967  CG  LEU A  68     2742   3667   2439   -744     22   -876       C
ATOM    968  CD1 LEU A  68      24.493  28.501  20.509  1.00 26.89           C
ANISOU  968  CD1 LEU A  68     3224   4103   2890  -1073     19  -1038       C
ATOM    969  CD2 LEU A  68      23.695  26.821  22.136  1.00 27.68           C
ANISOU  969  CD2 LEU A  68     3317   4351   2851   -562    -62   -927       C
ATOM    970  H   LEU A  68      21.756  25.107  18.391  1.00 21.23           H
ATOM    971  HA  LEU A  68      21.581  25.725  21.021  1.00 24.08           H
ATOM    972  HB2 LEU A  68      22.460  27.585  19.122  1.00 27.80           H
ATOM    973  HB3 LEU A  68      21.880  28.029  20.533  1.00 27.80           H
ATOM    974  HG  LEU A  68      24.203  26.494  20.190  1.00 27.95           H
ATOM    975 HD11 LEU A  68      25.373  28.405  20.906  1.00 32.28           H
ATOM    976 HD12 LEU A  68      24.576  28.709  19.566  1.00 32.28           H
ATOM    977 HD13 LEU A  68      24.002  29.206  20.961  1.00 32.28           H
ATOM    978 HD21 LEU A  68      24.571  26.966  22.527  1.00 33.23           H
ATOM    979 HD22 LEU A  68      23.037  27.373  22.586  1.00 33.23           H
ATOM    980 HD23 LEU A  68      23.450  25.885  22.212  1.00 33.23           H
ATOM    981  N   GLY A  69      19.297  25.376  19.277  1.00 18.15           N
ANISOU  981  N   GLY A  69     2352   2561   1984   -268    317   -395       N
ATOM    982  CA  GLY A  69      17.860  25.372  19.308  1.00 18.79           C
ANISOU  982  CA  GLY A  69     2480   2595   2066   -180    398   -356       C
ATOM    983  C   GLY A  69      17.148  26.177  18.240  1.00 18.21           C
ANISOU  983  C   GLY A  69     2444   2410   2066   -163    431   -358       C
ATOM    984  O   GLY A  69      15.923  26.352  18.329  1.00 20.99           O
ANISOU  984  O   GLY A  69     2800   2785   2388    -48    483   -369       O
ATOM    985  H   GLY A  69      19.636  24.719  18.839  1.00 21.79           H
ATOM    986  HA2 GLY A  69      17.558  24.454  19.224  1.00 22.57           H
ATOM    987  HA3 GLY A  69      17.575  25.720  20.167  1.00 22.57           H
ATOM    988  N   CYS A  70      17.858  26.738  17.264  1.00 18.07           N
ANISOU  988  N   CYS A  70     2461   2293   2111   -259    406   -358       N
ATOM    989  CA  CYS A  70      17.142  27.380  16.158  1.00 18.72           C
ANISOU  989  CA  CYS A  70     2628   2256   2228   -198    433   -334       C
ATOM    990  C   CYS A  70      16.339  26.346  15.374  1.00 17.08           C
ANISOU  990  C   CYS A  70     2276   2146   2067   -127    470   -259       C
ATOM    991  O   CYS A  70      16.552  25.135  15.484  1.00 18.07           O
ANISOU  991  O   CYS A  70     2283   2371   2213   -174    481   -211       O
ATOM    992  CB  CYS A  70      18.101  28.105  15.227  1.00 19.01           C
ANISOU  992  CB  CYS A  70     2771   2159   2295   -355    425   -329       C
ATOM    993  SG  CYS A  70      18.821  29.618  15.966  1.00 20.87           S
ANISOU  993  SG  CYS A  70     3261   2216   2453   -507    400   -450       S
ATOM    994  H   CYS A  70      18.717  26.761  17.219  1.00 21.70           H
ATOM    995  HA  CYS A  70      16.531  28.040  16.520  1.00 22.47           H
ATOM    996  HB2 CYS A  70      18.831  27.508  15.000  1.00 22.83           H
ATOM    997  HB3 CYS A  70      17.623  28.364  14.423  1.00 22.83           H
ATOM    998  N   GLY A  71      15.384  26.826  14.595  1.00 17.99           N
ANISOU  998  N   GLY A  71     2428   2232   2175      2    480   -261       N
ATOM    999  CA  GLY A  71      14.599  25.925  13.758  1.00 17.03           C
ANISOU  999  CA  GLY A  71     2152   2233   2086     43    503   -223       C
ATOM   1000  C   GLY A  71      15.386  25.418  12.568  1.00 17.04           C
ANISOU 1000  C   GLY A  71     2131   2187   2156    -57    491   -153       C
ATOM   1001  O   GLY A  71      16.072  26.166  11.877  1.00 18.22           O
ANISOU 1001  O   GLY A  71     2404   2210   2310    -95    477   -131       O
ATOM   1002  H   GLY A  71      15.169  27.656  14.530  1.00 21.60           H
ATOM   1003  HA2 GLY A  71      14.315  25.161  14.285  1.00 20.45           H
ATOM   1004  HA3 GLY A  71      13.814  26.391  13.430  1.00 20.45           H
ATOM   1005  N   ILE A  72      15.268  24.121  12.308  1.00 15.19           N
ANISOU 1005  N   ILE A  72     1765   2050   1955   -114    509   -121       N
ATOM   1006  CA  ILE A  72      15.910  23.470  11.164  1.00 15.12           C
ANISOU 1006  CA  ILE A  72     1728   2025   1994   -170    498    -70       C
ATOM   1007  C   ILE A  72      14.971  23.516   9.977  1.00 15.51           C
ANISOU 1007  C   ILE A  72     1738   2117   2038    -86    490    -79       C
ATOM   1008  O   ILE A  72      13.800  23.158  10.101  1.00 15.93           O
ANISOU 1008  O   ILE A  72     1689   2298   2067    -44    503   -129       O
ATOM   1009  CB  ILE A  72      16.258  22.021  11.530  1.00 16.29           C
ANISOU 1009  CB  ILE A  72     1827   2213   2149   -239    508    -45       C
ATOM   1010  CG1 ILE A  72      17.317  21.968  12.640  1.00 18.23           C
ANISOU 1010  CG1 ILE A  72     2111   2453   2364   -261    487    -44       C
ATOM   1011  CG2 ILE A  72      16.694  21.257  10.276  1.00 17.00           C
ANISOU 1011  CG2 ILE A  72     1895   2298   2268   -250    495    -17       C
ATOM   1012  CD1 ILE A  72      17.601  20.596  13.160  1.00 20.41           C
ANISOU 1012  CD1 ILE A  72     2424   2736   2596   -254    486    -13       C
ATOM   1013  H   ILE A  72      14.809  23.577  12.791  1.00 18.24           H
ATOM   1014  HA  ILE A  72      16.718  23.948  10.920  1.00 18.16           H
ATOM   1015  HB  ILE A  72      15.466  21.588  11.885  1.00 19.56           H
ATOM   1016 HG12 ILE A  72      18.148  22.327  12.292  1.00 21.89           H
ATOM   1017 HG13 ILE A  72      17.010  22.507  13.386  1.00 21.89           H
ATOM   1018 HG21 ILE A  72      17.014  20.379  10.536  1.00 20.42           H
ATOM   1019 HG22 ILE A  72      15.934  21.169   9.680  1.00 20.42           H
ATOM   1020 HG23 ILE A  72      17.404  21.751   9.837  1.00 20.42           H
ATOM   1021 HD11 ILE A  72      18.393  20.628  13.719  1.00 24.51           H
ATOM   1022 HD12 ILE A  72      16.841  20.293  13.680  1.00 24.51           H
ATOM   1023 HD13 ILE A  72      17.749  19.999  12.410  1.00 24.51           H
ATOM   1024  N   ASP A  73      15.492  23.948   8.844  1.00 15.55           N
ANISOU 1024  N   ASP A  73     1813   2052   2044    -71    474    -41       N
ATOM   1025  CA  ASP A  73      14.752  23.986   7.591  1.00 15.37           C
ANISOU 1025  CA  ASP A  73     1776   2077   1989     38    449    -46       C
ATOM   1026  C   ASP A  73      15.127  22.806   6.714  1.00 14.81           C
ANISOU 1026  C   ASP A  73     1623   2054   1950    -36    449    -28       C
ATOM   1027  O   ASP A  73      16.218  22.278   6.812  1.00 16.43           O
ANISOU 1027  O   ASP A  73     1831   2223   2187   -131    466      4       O
ATOM   1028  CB  ASP A  73      15.089  25.295   6.844  1.00 16.97           C
ANISOU 1028  CB  ASP A  73     2190   2132   2127    116    442     -1       C
ATOM   1029  CG  ASP A  73      14.667  26.534   7.582  1.00 20.53           C
ANISOU 1029  CG  ASP A  73     2808   2478   2514    232    431    -30       C
ATOM   1030  OD1 ASP A  73      13.616  26.535   8.248  1.00 22.24           O
ANISOU 1030  OD1 ASP A  73     2932   2813   2704    370    409   -104       O
ATOM   1031  OD2 ASP A  73      15.432  27.539   7.515  1.00 25.35           O
ANISOU 1031  OD2 ASP A  73     3662   2886   3085    166    455     12       O
ATOM   1032  H   ASP A  73      16.300  24.234   8.771  1.00 18.67           H
ATOM   1033  HA  ASP A  73      13.799  23.943   7.770  1.00 18.46           H
ATOM   1034  HB2 ASP A  73      16.049  25.341   6.711  1.00 20.38           H
ATOM   1035  HB3 ASP A  73      14.635  25.291   5.986  1.00 20.38           H
ATOM   1036  N   TRP A  74      14.227  22.428   5.811  1.00 16.58           N
ANISOU 1036  N   TRP A  74     1775   2382   2144     35    418    -70       N
ATOM   1037  CA  TRP A  74      14.566  21.513   4.728  1.00 15.44           C
ANISOU 1037  CA  TRP A  74     1604   2259   2003     -4    406    -65       C
ATOM   1038  C   TRP A  74      14.762  22.294   3.436  1.00 16.42           C
ANISOU 1038  C   TRP A  74     1826   2358   2056    112    385    -24       C
ATOM   1039  O   TRP A  74      13.888  23.068   3.028  1.00 18.77           O
ANISOU 1039  O   TRP A  74     2157   2699   2274    275    341    -47       O
ATOM   1040  CB  TRP A  74      13.454  20.503   4.518  1.00 17.05           C
ANISOU 1040  CB  TRP A  74     1676   2604   2197    -46    385   -161       C
ATOM   1041  CG  TRP A  74      13.681  19.612   3.306  1.00 16.68           C
ANISOU 1041  CG  TRP A  74     1636   2568   2134    -68    359   -183       C
ATOM   1042  CD1 TRP A  74      13.015  19.650   2.107  1.00 17.52           C
ANISOU 1042  CD1 TRP A  74     1690   2797   2171     22    299   -244       C
ATOM   1043  CD2 TRP A  74      14.668  18.581   3.179  1.00 14.16           C
ANISOU 1043  CD2 TRP A  74     1395   2144   1840   -144    378   -157       C
ATOM   1044  NE1 TRP A  74      13.507  18.683   1.277  1.00 17.66           N
ANISOU 1044  NE1 TRP A  74     1751   2778   2180    -28    290   -261       N
ATOM   1045  CE2 TRP A  74      14.536  18.024   1.891  1.00 15.80           C
ANISOU 1045  CE2 TRP A  74     1606   2399   2000   -112    339   -208       C
ATOM   1046  CE3 TRP A  74      15.640  18.059   4.036  1.00 16.47           C
ANISOU 1046  CE3 TRP A  74     1765   2328   2165   -191    412   -110       C
ATOM   1047  CZ2 TRP A  74      15.312  16.950   1.466  1.00 16.96           C
ANISOU 1047  CZ2 TRP A  74     1843   2465   2135   -129    340   -218       C
ATOM   1048  CZ3 TRP A  74      16.427  17.010   3.609  1.00 16.77           C
ANISOU 1048  CZ3 TRP A  74     1888   2304   2181   -173    404   -117       C
ATOM   1049  CH2 TRP A  74      16.262  16.468   2.316  1.00 19.03           C
ANISOU 1049  CH2 TRP A  74     2190   2618   2424   -141    372   -171       C
ATOM   1050  H   TRP A  74      13.408  22.691   5.805  1.00 19.91           H
ATOM   1051  HA  TRP A  74      15.389  21.051   4.951  1.00 18.54           H
ATOM   1052  HB2 TRP A  74      13.394  19.934   5.301  1.00 20.47           H
ATOM   1053  HB3 TRP A  74      12.618  20.978   4.388  1.00 20.47           H
ATOM   1054  HD1 TRP A  74      12.333  20.245   1.892  1.00 21.04           H
ATOM   1055  HE1 TRP A  74      13.213  18.513   0.487  1.00 21.20           H
ATOM   1056  HE3 TRP A  74      15.756  18.416   4.887  1.00 19.78           H
ATOM   1057  HZ2 TRP A  74      15.187  16.572   0.625  1.00 20.36           H
ATOM   1058  HZ3 TRP A  74      17.072  16.656   4.178  1.00 20.14           H
ATOM   1059  HH2 TRP A  74      16.811  15.770   2.040  1.00 22.85           H
ATOM   1060  N   ALA A  75      15.918  22.114   2.818  1.00 16.51           N
ANISOU 1060  N   ALA A  75     1893   2315   2065     50    419     32       N
ATOM   1061  CA  ALA A  75      16.269  22.781   1.565  1.00 16.89           C
ANISOU 1061  CA  ALA A  75     2065   2333   2018    114    431     89       C
ATOM   1062  C   ALA A  75      16.118  21.773   0.437  1.00 18.08           C
ANISOU 1062  C   ALA A  75     2146   2589   2136    158    398     47       C
ATOM   1063  O   ALA A  75      16.918  20.842   0.331  1.00 17.90           O
ANISOU 1063  O   ALA A  75     2069   2589   2145     85    422     34       O
ATOM   1064  CB  ALA A  75      17.699  23.298   1.645  1.00 20.21           C
ANISOU 1064  CB  ALA A  75     2564   2681   2433    -31    518    157       C
ATOM   1065  H   ALA A  75      16.538  21.595   3.111  1.00 19.82           H
ATOM   1066  HA  ALA A  75      15.670  23.525   1.396  1.00 20.28           H
ATOM   1067  HB1 ALA A  75      17.932  23.714   0.800  1.00 24.26           H
ATOM   1068  HB2 ALA A  75      17.760  23.949   2.362  1.00 24.26           H
ATOM   1069  HB3 ALA A  75      18.295  22.553   1.823  1.00 24.26           H
ATOM   1070  N   ASN A  76      15.078  21.958  -0.382  1.00 19.47           N
ANISOU 1070  N   ASN A  76     2330   2843   2226    308    329      8       N
ATOM   1071  CA  ASN A  76      14.784  20.970  -1.408  1.00 22.25           C
ANISOU 1071  CA  ASN A  76     2608   3311   2535    339    280    -66       C
ATOM   1072  C   ASN A  76      15.792  21.000  -2.555  1.00 23.38           C
ANISOU 1072  C   ASN A  76     2858   3434   2592    358    327      0       C
ATOM   1073  O   ASN A  76      15.897  20.008  -3.280  1.00 27.46           O
ANISOU 1073  O   ASN A  76     3326   4023   3084    362    302    -65       O
ATOM   1074  CB  ASN A  76      13.364  21.143  -1.943  1.00 29.00           C
ANISOU 1074  CB  ASN A  76     3390   4330   3298    502    175   -163       C
ATOM   1075  CG  ASN A  76      12.414  20.062  -1.446  1.00 52.28           C
ANISOU 1075  CG  ASN A  76     6127   7428   6310    382    133   -316       C
ATOM   1076  OD1 ASN A  76      12.700  18.862  -1.545  1.00 47.33           O
ANISOU 1076  OD1 ASN A  76     5476   6775   5730    225    147   -368       O
ATOM   1077  ND2 ASN A  76      11.278  20.485  -0.898  1.00 50.79           N
ANISOU 1077  ND2 ASN A  76     5805   7396   6099    449     89   -398       N
ATOM   1078  H   ASN A  76      14.544  22.632  -0.361  1.00 23.38           H
ATOM   1079  HA  ASN A  76      14.829  20.091  -1.000  1.00 26.71           H
ATOM   1080  HB2 ASN A  76      13.019  22.002  -1.653  1.00 34.81           H
ATOM   1081  HB3 ASN A  76      13.384  21.103  -2.912  1.00 34.81           H
ATOM   1082 HD21 ASN A  76      11.116  21.327  -0.840  1.00 60.97           H
ATOM   1083 HD22 ASN A  76      10.706  19.916  -0.600  1.00 60.97           H
ATOM   1084  N   ASP A  77      16.530  22.098  -2.731  1.00 19.82           N
ANISOU 1084  N   ASP A  77     2568   2887   2077    348    405    117       N
ATOM   1085  CA  ASP A  77      17.498  22.165  -3.823  1.00 20.40           C
ANISOU 1085  CA  ASP A  77     2730   2982   2040    325    483    179       C
ATOM   1086  C   ASP A  77      18.727  21.310  -3.523  1.00 20.23           C
ANISOU 1086  C   ASP A  77     2570   3027   2089    189    552    152       C
ATOM   1087  O   ASP A  77      19.117  20.457  -4.339  1.00 23.20           O
ANISOU 1087  O   ASP A  77     2895   3509   2411    239    554    103       O
ATOM   1088  CB  ASP A  77      17.825  23.615  -4.196  1.00 23.98           C
ANISOU 1088  CB  ASP A  77     3448   3304   2360    310    566    311       C
ATOM   1089  CG  ASP A  77      18.331  24.482  -3.060  1.00 26.47           C
ANISOU 1089  CG  ASP A  77     3837   3474   2745    140    638    362       C
ATOM   1090  OD1 ASP A  77      18.418  24.079  -1.891  1.00 23.36           O
ANISOU 1090  OD1 ASP A  77     3278   3096   2502     59    618    304       O
ATOM   1091  OD2 ASP A  77      18.654  25.661  -3.355  1.00 31.10           O
ANISOU 1091  OD2 ASP A  77     4705   3904   3209     75    722    466       O
ATOM   1092  H   ASP A  77      16.490  22.803  -2.241  1.00 23.80           H
ATOM   1093  HA  ASP A  77      17.097  21.792  -4.624  1.00 24.49           H
ATOM   1094  HB2 ASP A  77      18.512  23.607  -4.881  1.00 28.79           H
ATOM   1095  HB3 ASP A  77      17.019  24.032  -4.539  1.00 28.79           H
ATOM   1096  N   VAL A  78      19.327  21.470  -2.341  1.00 19.36           N
ANISOU 1096  N   VAL A  78     2396   2878   2080     59    593    160       N
ATOM   1097  CA  VAL A  78      20.468  20.637  -1.970  1.00 19.48           C
ANISOU 1097  CA  VAL A  78     2263   3004   2134      3    630    111       C
ATOM   1098  C   VAL A  78      20.043  19.348  -1.289  1.00 15.52           C
ANISOU 1098  C   VAL A  78     1690   2483   1724     76    540     25       C
ATOM   1099  O   VAL A  78      20.896  18.496  -1.009  1.00 17.41           O
ANISOU 1099  O   VAL A  78     1858   2793   1965    114    542    -24       O
ATOM   1100  CB  VAL A  78      21.475  21.440  -1.130  1.00 19.08           C
ANISOU 1100  CB  VAL A  78     2170   2975   2103   -173    714    143       C
ATOM   1101  CG1 VAL A  78      22.062  22.578  -1.918  1.00 20.81           C
ANISOU 1101  CG1 VAL A  78     2505   3203   2199   -320    839    221       C
ATOM   1102  CG2 VAL A  78      20.822  21.965   0.148  1.00 18.29           C
ANISOU 1102  CG2 VAL A  78     2115   2731   2105   -215    668    153       C
ATOM   1103  H   VAL A  78      19.095  22.047  -1.747  1.00 23.24           H
ATOM   1104  HA  VAL A  78      20.941  20.364  -2.772  1.00 23.38           H
ATOM   1105  HB  VAL A  78      22.198  20.842  -0.884  1.00 22.90           H
ATOM   1106 HG11 VAL A  78      22.706  23.046  -1.364  1.00 24.98           H
ATOM   1107 HG12 VAL A  78      22.500  22.223  -2.707  1.00 24.98           H
ATOM   1108 HG13 VAL A  78      21.349  23.182  -2.179  1.00 24.98           H
ATOM   1109 HG21 VAL A  78      21.505  22.361   0.712  1.00 21.96           H
ATOM   1110 HG22 VAL A  78      20.160  22.634  -0.088  1.00 21.96           H
ATOM   1111 HG23 VAL A  78      20.397  21.227   0.612  1.00 21.96           H
ATOM   1112  N   SER A  79      18.765  19.190  -0.968  1.00 17.14           N
ANISOU 1112  N   SER A  79     1926   2605   1983     96    468     -1       N
ATOM   1113  CA  SER A  79      18.241  18.024  -0.261  1.00 16.85           C
ANISOU 1113  CA  SER A  79     1873   2516   2012     87    412    -75       C
ATOM   1114  C   SER A  79      19.046  17.748   1.009  1.00 16.61           C
ANISOU 1114  C   SER A  79     1825   2452   2035     54    432    -61       C
ATOM   1115  O   SER A  79      19.591  16.665   1.223  1.00 17.03           O
ANISOU 1115  O   SER A  79     1915   2486   2069    117    413   -102       O
ATOM   1116  CB  SER A  79      18.188  16.787  -1.160  1.00 20.78           C
ANISOU 1116  CB  SER A  79     2416   3025   2454    153    371   -159       C
ATOM   1117  OG  SER A  79      17.163  16.970  -2.134  1.00 27.67           O
ANISOU 1117  OG  SER A  79     3287   3952   3275    175    324   -201       O
ATOM   1118  H   SER A  79      18.156  19.767  -1.155  1.00 20.58           H
ATOM   1119  HA  SER A  79      17.330  18.228   0.002  1.00 20.23           H
ATOM   1120  HB2 SER A  79      19.042  16.673  -1.606  1.00 24.94           H
ATOM   1121  HB3 SER A  79      17.987  16.004  -0.623  1.00 24.94           H
ATOM   1122  HG  SER A  79      17.111  16.292  -2.627  1.00 33.22           H
ATOM   1123  N   ARG A  80      19.105  18.784   1.858  1.00 15.55           N
ANISOU 1123  N   ARG A  80     1663   2303   1943    -17    460    -10       N
ATOM   1124  CA  ARG A  80      19.709  18.724   3.191  1.00 13.94           C
ANISOU 1124  CA  ARG A  80     1433   2089   1777    -50    465     -6       C
ATOM   1125  C   ARG A  80      18.828  19.492   4.160  1.00 15.03           C
ANISOU 1125  C   ARG A  80     1588   2154   1967   -119    464     15       C
ATOM   1126  O   ARG A  80      18.116  20.417   3.773  1.00 14.87           O
ANISOU 1126  O   ARG A  80     1594   2115   1941   -121    469     34       O
ATOM   1127  CB  ARG A  80      21.106  19.340   3.228  1.00 15.56           C
ANISOU 1127  CB  ARG A  80     1548   2419   1944    -84    510      2       C
ATOM   1128  CG  ARG A  80      22.113  18.789   2.253  1.00 16.28           C
ANISOU 1128  CG  ARG A  80     1568   2666   1953     -3    532    -34       C
ATOM   1129  CD  ARG A  80      22.480  17.322   2.553  1.00 16.42           C
ANISOU 1129  CD  ARG A  80     1607   2698   1935    181    467    -98       C
ATOM   1130  NE  ARG A  80      23.681  16.956   1.806  1.00 16.43           N
ANISOU 1130  NE  ARG A  80     1493   2920   1831    303    488   -159       N
ATOM   1131  CZ  ARG A  80      24.095  15.715   1.597  1.00 19.28           C
ANISOU 1131  CZ  ARG A  80     1908   3308   2111    535    434   -228       C
ATOM   1132  NH1 ARG A  80      23.407  14.677   2.066  1.00 19.94           N
ANISOU 1132  NH1 ARG A  80     2214   3157   2207    627    364   -233       N
ATOM   1133  NH2 ARG A  80      25.222  15.503   0.921  1.00 20.21           N
ANISOU 1133  NH2 ARG A  80     1877   3691   2110    674    460   -302       N
ATOM   1134  H   ARG A  80      18.789  19.562   1.674  1.00 18.67           H
ATOM   1135  HA  ARG A  80      19.773  17.795   3.461  1.00 16.75           H
ATOM   1136  HB2 ARG A  80      21.022  20.289   3.043  1.00 18.68           H
ATOM   1137  HB3 ARG A  80      21.470  19.207   4.118  1.00 18.68           H
ATOM   1138  HG2 ARG A  80      21.743  18.829   1.357  1.00 19.55           H
ATOM   1139  HG3 ARG A  80      22.925  19.318   2.300  1.00 19.55           H
ATOM   1140  HD2 ARG A  80      22.656  17.215   3.501  1.00 19.72           H
ATOM   1141  HD3 ARG A  80      21.753  16.740   2.283  1.00 19.72           H
ATOM   1142  HE  ARG A  80      24.156  17.594   1.478  1.00 19.73           H
ATOM   1143 HH11 ARG A  80      22.683  14.807   2.511  1.00 23.95           H
ATOM   1144 HH12 ARG A  80      23.687  13.876   1.923  1.00 23.95           H
ATOM   1145 HH21 ARG A  80      25.676  16.170   0.623  1.00 24.26           H
ATOM   1146 HH22 ARG A  80      25.496  14.700   0.782  1.00 24.26           H
ATOM   1147  N   PHE A  81      18.910  19.119   5.443  1.00 13.98           N
ANISOU 1147  N   PHE A  81     1463   1991   1858   -137    453      7       N
ATOM   1148  CA  PHE A  81      18.425  19.971   6.529  1.00 13.61           C
ANISOU 1148  CA  PHE A  81     1421   1911   1840   -190    463     18       C
ATOM   1149  C   PHE A  81      19.465  21.037   6.819  1.00 14.08           C
ANISOU 1149  C   PHE A  81     1459   2002   1889   -243    482     28       C
ATOM   1150  O   PHE A  81      20.664  20.750   6.916  1.00 16.10           O
ANISOU 1150  O   PHE A  81     1645   2355   2116   -247    479      7       O
ATOM   1151  CB  PHE A  81      18.162  19.146   7.776  1.00 14.63           C
ANISOU 1151  CB  PHE A  81     1590   2002   1965   -199    456      9       C
ATOM   1152  CG  PHE A  81      16.974  18.254   7.683  1.00 12.78           C
ANISOU 1152  CG  PHE A  81     1398   1731   1728   -247    469    -13       C
ATOM   1153  CD1 PHE A  81      15.694  18.797   7.655  1.00 14.68           C
ANISOU 1153  CD1 PHE A  81     1567   2030   1981   -292    487    -46       C
ATOM   1154  CD2 PHE A  81      17.102  16.884   7.665  1.00 14.59           C
ANISOU 1154  CD2 PHE A  81     1746   1879   1918   -254    466    -19       C
ATOM   1155  CE1 PHE A  81      14.585  18.008   7.601  1.00 15.81           C
ANISOU 1155  CE1 PHE A  81     1691   2210   2105   -394    511   -100       C
ATOM   1156  CE2 PHE A  81      15.979  16.067   7.598  1.00 15.68           C
ANISOU 1156  CE2 PHE A  81     1945   1973   2039   -385    498    -57       C
ATOM   1157  CZ  PHE A  81      14.715  16.627   7.574  1.00 17.02           C
ANISOU 1157  CZ  PHE A  81     1976   2261   2229   -484    526   -105       C
ATOM   1158  H   PHE A  81      19.245  18.373   5.709  1.00 16.79           H
ATOM   1159  HA  PHE A  81      17.592  20.396   6.271  1.00 16.35           H
ATOM   1160  HB2 PHE A  81      18.936  18.588   7.947  1.00 17.57           H
ATOM   1161  HB3 PHE A  81      18.017  19.750   8.522  1.00 17.57           H
ATOM   1162  HD1 PHE A  81      15.593  19.721   7.674  1.00 17.63           H
ATOM   1163  HD2 PHE A  81      17.949  16.501   7.697  1.00 17.52           H
ATOM   1164  HE1 PHE A  81      13.740  18.396   7.582  1.00 18.98           H
ATOM   1165  HE2 PHE A  81      16.078  15.143   7.570  1.00 18.83           H
ATOM   1166  HZ  PHE A  81      13.961  16.084   7.540  1.00 20.43           H
ATOM   1167  N   LEU A  82      19.016  22.289   6.926  1.00 15.29           N
ANISOU 1167  N   LEU A  82     1679   2087   2044   -284    500     41       N
ATOM   1168  CA  LEU A  82      19.889  23.429   7.154  1.00 15.78           C
ANISOU 1168  CA  LEU A  82     1784   2129   2081   -403    532     39       C
ATOM   1169  C   LEU A  82      19.436  24.189   8.378  1.00 17.91           C
ANISOU 1169  C   LEU A  82     2132   2317   2357   -416    518     13       C
ATOM   1170  O   LEU A  82      18.243  24.445   8.547  1.00 18.78           O
ANISOU 1170  O   LEU A  82     2306   2362   2467   -311    504     14       O
ATOM   1171  CB  LEU A  82      19.832  24.422   5.992  1.00 18.30           C
ANISOU 1171  CB  LEU A  82     2244   2360   2349   -443    580     87       C
ATOM   1172  CG  LEU A  82      20.175  23.876   4.611  1.00 18.41           C
ANISOU 1172  CG  LEU A  82     2213   2454   2326   -422    607    116       C
ATOM   1173  CD1 LEU A  82      20.147  25.010   3.581  1.00 24.04           C
ANISOU 1173  CD1 LEU A  82     3135   3052   2948   -471    668    182       C
ATOM   1174  CD2 LEU A  82      21.549  23.207   4.588  1.00 19.51           C
ANISOU 1174  CD2 LEU A  82     2176   2784   2453   -500    632     75       C
ATOM   1175  H   LEU A  82      18.185  22.503   6.868  1.00 18.36           H
ATOM   1176  HA  LEU A  82      20.791  23.093   7.274  1.00 18.94           H
ATOM   1177  HB2 LEU A  82      18.929  24.774   5.942  1.00 21.97           H
ATOM   1178  HB3 LEU A  82      20.458  25.139   6.178  1.00 21.97           H
ATOM   1179  HG  LEU A  82      19.515  23.204   4.381  1.00 22.10           H
ATOM   1180 HD11 LEU A  82      20.361  24.649   2.707  1.00 28.86           H
ATOM   1181 HD12 LEU A  82      19.260  25.403   3.568  1.00 28.86           H
ATOM   1182 HD13 LEU A  82      20.801  25.681   3.831  1.00 28.86           H
ATOM   1183 HD21 LEU A  82      21.749  22.928   3.680  1.00 23.42           H
ATOM   1184 HD22 LEU A  82      22.215  23.843   4.892  1.00 23.42           H
ATOM   1185 HD23 LEU A  82      21.535  22.436   5.176  1.00 23.42           H
ATOM   1186  N   CYS A  83      20.397  24.598   9.183  1.00 16.44           N
ANISOU 1186  N   CYS A  83     1922   2169   2155   -536    519    -32       N
ATOM   1187  CA  CYS A  83      20.088  25.495  10.298  1.00 16.60           C
ANISOU 1187  CA  CYS A  83     2051   2095   2160   -563    506    -73       C
ATOM   1188  C   CYS A  83      20.757  26.830  10.030  1.00 16.99           C
ANISOU 1188  C   CYS A  83     2258   2034   2163   -757    551    -94       C
ATOM   1189  O   CYS A  83      22.010  26.917  10.029  1.00 20.04           O
ANISOU 1189  O   CYS A  83     2543   2546   2527   -958    574   -144       O
ATOM   1190  CB  CYS A  83      20.574  24.989  11.645  1.00 16.08           C
ANISOU 1190  CB  CYS A  83     1879   2146   2084   -563    460   -133       C
ATOM   1191  SG  CYS A  83      20.167  26.161  12.976  1.00 17.99           S
ANISOU 1191  SG  CYS A  83     2276   2274   2286   -587    444   -202       S
ATOM   1192  H   CYS A  83      21.225  24.378   9.112  1.00 19.74           H
ATOM   1193  HA  CYS A  83      19.122  25.571  10.346  1.00 19.93           H
ATOM   1194  HB2 CYS A  83      20.147  24.141  11.842  1.00 19.31           H
ATOM   1195  HB3 CYS A  83      21.537  24.878  11.618  1.00 19.31           H
ATOM   1196  N   PRO A  84      20.007  27.905   9.755  1.00 21.08           N
ANISOU 1196  N   PRO A  84     3040   2329   2640   -714    569    -68       N
ATOM   1197  CA  PRO A  84      20.643  29.160   9.330  1.00 24.08           C
ANISOU 1197  CA  PRO A  84     3676   2528   2944   -934    634    -68       C
ATOM   1198  C   PRO A  84      21.320  29.920  10.453  1.00 23.24           C
ANISOU 1198  C   PRO A  84     3646   2376   2808  -1146    631   -175       C
ATOM   1199  O   PRO A  84      21.974  30.917  10.177  1.00 27.54           O
ANISOU 1199  O   PRO A  84     4411   2772   3281  -1416    700   -195       O
ATOM   1200  CB  PRO A  84      19.468  29.972   8.764  1.00 31.66           C
ANISOU 1200  CB  PRO A  84     4960   3235   3835   -718    628     -8       C
ATOM   1201  CG  PRO A  84      18.289  29.471   9.519  1.00 33.07           C
ANISOU 1201  CG  PRO A  84     5013   3500   4052   -433    552    -43       C
ATOM   1202  CD  PRO A  84      18.536  27.999   9.786  1.00 33.01           C
ANISOU 1202  CD  PRO A  84     4642   3760   4141   -450    534    -49       C
ATOM   1203  HA  PRO A  84      21.288  28.981   8.628  1.00 28.90           H
ATOM   1204  HB2 PRO A  84      19.609  30.919   8.921  1.00 38.00           H
ATOM   1205  HB3 PRO A  84      19.374  29.804   7.813  1.00 38.00           H
ATOM   1206  HG2 PRO A  84      18.207  29.960  10.352  1.00 39.70           H
ATOM   1207  HG3 PRO A  84      17.488  29.590   8.984  1.00 39.70           H
ATOM   1208  HD2 PRO A  84      18.190  27.741  10.655  1.00 39.63           H
ATOM   1209  HD3 PRO A  84      18.138  27.449   9.094  1.00 39.63           H
ATOM   1210  N   CYS A  85      21.205  29.495  11.709  1.00 22.22           N
ANISOU 1210  N   CYS A  85     3365   2366   2711  -1061    561   -249       N
ATOM   1211  CA  CYS A  85      21.796  30.276  12.790  1.00 21.51           C
ANISOU 1211  CA  CYS A  85     3363   2239   2573  -1249    542   -372       C
ATOM   1212  C   CYS A  85      23.314  30.215  12.773  1.00 23.05           C
ANISOU 1212  C   CYS A  85     3354   2659   2747  -1582    567   -462       C
ATOM   1213  O   CYS A  85      23.976  31.251  12.861  1.00 26.50           O
ANISOU 1213  O   CYS A  85     3943   3017   3109  -1829    598   -530       O
ATOM   1214  CB  CYS A  85      21.223  29.825  14.118  1.00 22.11           C
ANISOU 1214  CB  CYS A  85     3341   2402   2657  -1043    463   -424       C
ATOM   1215  SG  CYS A  85      19.566  30.541  14.365  1.00 22.23           S
ANISOU 1215  SG  CYS A  85     3649   2166   2631   -738    454   -402       S
ATOM   1216  H   CYS A  85      20.800  28.777  11.955  1.00 26.67           H
ATOM   1217  HA  CYS A  85      21.560  31.209  12.670  1.00 25.83           H
ATOM   1218  HB2 CYS A  85      21.149  28.858  14.128  1.00 26.54           H
ATOM   1219  HB3 CYS A  85      21.800  30.121  14.839  1.00 26.54           H
ATOM   1220  N   HIS A  86      23.882  28.999  12.627  1.00 21.33           N
ANISOU 1220  N   HIS A  86     2779   2760   2564  -1512    538   -459       N
ATOM   1221  CA  HIS A  86      25.339  28.879  12.592  1.00 22.63           C
ANISOU 1221  CA  HIS A  86     2690   3233   2673  -1702    534   -560       C
ATOM   1222  C   HIS A  86      25.774  27.908  11.496  1.00 25.76           C
ANISOU 1222  C   HIS A  86     2876   3829   3083  -1586    553   -494       C
ATOM   1223  O   HIS A  86      26.832  27.277  11.594  1.00 28.50           O
ANISOU 1223  O   HIS A  86     2946   4502   3379  -1561    510   -578       O
ATOM   1224  CB  HIS A  86      25.912  28.459  13.950  1.00 26.52           C
ANISOU 1224  CB  HIS A  86     2953   3993   3130  -1687    431   -707       C
ATOM   1225  CG  HIS A  86      25.331  29.221  15.090  1.00 24.91           C
ANISOU 1225  CG  HIS A  86     2968   3590   2908  -1711    388   -773       C
ATOM   1226  ND1 HIS A  86      24.249  28.753  15.813  1.00 24.57           N
ANISOU 1226  ND1 HIS A  86     3011   3435   2889  -1391    332   -704       N
ATOM   1227  CD2 HIS A  86      25.647  30.434  15.601  1.00 29.90           C
ANISOU 1227  CD2 HIS A  86     3788   4096   3474  -1939    397   -874       C
ATOM   1228  CE1 HIS A  86      23.940  29.653  16.735  1.00 24.40           C
ANISOU 1228  CE1 HIS A  86     3194   3257   2819  -1441    306   -788       C
ATOM   1229  NE2 HIS A  86      24.762  30.680  16.620  1.00 28.60           N
ANISOU 1229  NE2 HIS A  86     3812   3754   3302  -1798    339   -908       N
ATOM   1230  H   HIS A  86      23.451  28.259  12.550  1.00 25.60           H
ATOM   1231  HA  HIS A  86      25.716  29.749  12.389  1.00 27.09           H
ATOM   1232  HB2 HIS A  86      25.725  27.518  14.093  1.00 31.83           H
ATOM   1233  HB3 HIS A  86      26.870  28.610  13.947  1.00 31.83           H
ATOM   1234  HD2 HIS A  86      26.333  30.994  15.316  1.00 35.89           H
ATOM   1235  HE1 HIS A  86      23.256  29.574  17.360  1.00 29.29           H
ATOM   1236  HE2 HIS A  86      24.746  31.389  17.106  1.00 34.34           H
ATOM   1237  N   GLU A  87      24.998  27.836  10.420  1.00 23.71           N
ANISOU 1237  N   GLU A  87     2764   3380   2865  -1498    610   -361       N
ATOM   1238  CA  GLU A  87      25.370  27.075   9.231  1.00 23.92           C
ANISOU 1238  CA  GLU A  87     2651   3548   2889  -1406    633   -305       C
ATOM   1239  C   GLU A  87      25.444  25.581   9.527  1.00 23.76           C
ANISOU 1239  C   GLU A  87     2376   3755   2897  -1166    563   -320       C
ATOM   1240  O   GLU A  87      26.293  24.862   8.980  1.00 24.64           O
ANISOU 1240  O   GLU A  87     2300   4097   2965  -1090    547   -351       O
ATOM   1241  CB  GLU A  87      26.671  27.590   8.625  1.00 29.47           C
ANISOU 1241  CB  GLU A  87     3283   4415   3500  -1612    679   -370       C
ATOM   1242  CG  GLU A  87      26.643  29.076   8.252  1.00 35.35           C
ANISOU 1242  CG  GLU A  87     4340   4909   4182  -1865    766   -350       C
ATOM   1243  CD  GLU A  87      27.888  29.536   7.504  1.00 47.43           C
ANISOU 1243  CD  GLU A  87     5806   6611   5603  -2107    844   -410       C
ATOM   1244  OE1 GLU A  87      28.309  28.841   6.558  1.00 46.08           O
ANISOU 1244  OE1 GLU A  87     5469   6620   5418  -2035    866   -386       O
ATOM   1245  OE2 GLU A  87      28.445  30.593   7.860  1.00 55.49           O
ANISOU 1245  OE2 GLU A  87     6953   7594   6539  -2381    891   -491       O
ATOM   1246  H   GLU A  87      24.235  28.228  10.352  1.00 28.46           H
ATOM   1247  HA  GLU A  87      24.675  27.196   8.565  1.00 28.72           H
ATOM   1248  HB2 GLU A  87      27.386  27.461   9.269  1.00 35.37           H
ATOM   1249  HB3 GLU A  87      26.858  27.086   7.818  1.00 35.37           H
ATOM   1250  HG2 GLU A  87      25.876  29.242   7.683  1.00 42.43           H
ATOM   1251  HG3 GLU A  87      26.574  29.602   9.064  1.00 42.43           H
ATOM   1252  N   GLY A  88      24.539  25.100  10.370  1.00 20.33           N
ANISOU 1252  N   GLY A  88     1981   3232   2512  -1006    514   -296       N
ATOM   1253  CA  GLY A  88      24.417  23.664  10.575  1.00 18.88           C
ANISOU 1253  CA  GLY A  88     1691   3152   2332   -729    441   -275       C
ATOM   1254  C   GLY A  88      23.864  22.999   9.318  1.00 18.64           C
ANISOU 1254  C   GLY A  88     1706   3042   2335   -615    478   -183       C
ATOM   1255  O   GLY A  88      22.975  23.527   8.644  1.00 18.90           O
ANISOU 1255  O   GLY A  88     1895   2878   2408   -650    526   -110       O
ATOM   1256  H   GLY A  88      23.990  25.577  10.830  1.00 24.41           H
ATOM   1257  HA2 GLY A  88      25.287  23.285  10.775  1.00 22.67           H
ATOM   1258  HA3 GLY A  88      23.817  23.486  11.316  1.00 22.67           H
ATOM   1259  N   VAL A  89      24.367  21.797   9.018  1.00 16.86           N
ANISOU 1259  N   VAL A  89     1363   2973   2072   -439    439   -201       N
ATOM   1260  CA  VAL A  89      23.851  21.006   7.900  1.00 15.45           C
ANISOU 1260  CA  VAL A  89     1243   2717   1910   -317    458   -139       C
ATOM   1261  C   VAL A  89      23.732  19.559   8.358  1.00 14.45           C
ANISOU 1261  C   VAL A  89     1165   2577   1750    -74    381   -140       C
ATOM   1262  O   VAL A  89      24.685  19.025   8.932  1.00 17.47           O
ANISOU 1262  O   VAL A  89     1452   3141   2045     65    319   -208       O
ATOM   1263  CB  VAL A  89      24.777  21.058   6.674  1.00 16.95           C
ANISOU 1263  CB  VAL A  89     1295   3101   2042   -366    517   -170       C
ATOM   1264  CG1 VAL A  89      24.174  20.260   5.513  1.00 16.32           C
ANISOU 1264  CG1 VAL A  89     1303   2930   1969   -229    525   -118       C
ATOM   1265  CG2 VAL A  89      25.045  22.491   6.237  1.00 18.48           C
ANISOU 1265  CG2 VAL A  89     1537   3250   2234   -631    595   -154       C
ATOM   1266  H   VAL A  89      25.008  21.420   9.449  1.00 20.25           H
ATOM   1267  HA  VAL A  89      22.978  21.351   7.656  1.00 18.55           H
ATOM   1268  HB  VAL A  89      25.625  20.659   6.923  1.00 20.35           H
ATOM   1269 HG11 VAL A  89      24.699  20.421   4.713  1.00 19.60           H
ATOM   1270 HG12 VAL A  89      24.192  19.316   5.736  1.00 19.60           H
ATOM   1271 HG13 VAL A  89      23.259  20.549   5.372  1.00 19.60           H
ATOM   1272 HG21 VAL A  89      25.625  22.480   5.459  1.00 22.19           H
ATOM   1273 HG22 VAL A  89      24.202  22.917   6.016  1.00 22.19           H
ATOM   1274 HG23 VAL A  89      25.476  22.967   6.964  1.00 22.19           H
ATOM   1275  N   PHE A  90      22.589  18.930   8.069  1.00 14.63           N
ANISOU 1275  N   PHE A  90     1350   2395   1816    -24    385    -77       N
ATOM   1276  CA  PHE A  90      22.318  17.544   8.407  1.00 15.23           C
ANISOU 1276  CA  PHE A  90     1572   2371   1844    142    339    -67       C
ATOM   1277  C   PHE A  90      21.784  16.832   7.173  1.00 16.56           C
ANISOU 1277  C   PHE A  90     1823   2446   2023    171    356    -56       C
ATOM   1278  O   PHE A  90      21.093  17.440   6.344  1.00 15.84           O
ANISOU 1278  O   PHE A  90     1701   2324   1993     55    398    -37       O
ATOM   1279  CB  PHE A  90      21.270  17.414   9.560  1.00 16.35           C
ANISOU 1279  CB  PHE A  90     1863   2345   2004     85    345    -21       C
ATOM   1280  CG  PHE A  90      21.545  18.311  10.745  1.00 14.72           C
ANISOU 1280  CG  PHE A  90     1592   2211   1791     34    333    -37       C
ATOM   1281  CD1 PHE A  90      21.114  19.607  10.751  1.00 17.26           C
ANISOU 1281  CD1 PHE A  90     1851   2524   2182   -119    373    -39       C
ATOM   1282  CD2 PHE A  90      22.225  17.830  11.840  1.00 18.79           C
ANISOU 1282  CD2 PHE A  90     2147   2788   2203    170    270    -57       C
ATOM   1283  CE1 PHE A  90      21.387  20.455  11.826  1.00 16.83           C
ANISOU 1283  CE1 PHE A  90     1769   2516   2110   -174    357    -75       C
ATOM   1284  CE2 PHE A  90      22.493  18.647  12.921  1.00 18.40           C
ANISOU 1284  CE2 PHE A  90     2035   2825   2133    123    246    -93       C
ATOM   1285  CZ  PHE A  90      22.080  19.947  12.909  1.00 18.39           C
ANISOU 1285  CZ  PHE A  90     1967   2805   2215    -65    293   -107       C
ATOM   1286  H   PHE A  90      21.932  19.307   7.661  1.00 17.57           H
ATOM   1287  HA  PHE A  90      23.141  17.121   8.696  1.00 18.29           H
ATOM   1288  HB2 PHE A  90      20.395  17.646   9.212  1.00 19.63           H
ATOM   1289  HB3 PHE A  90      21.269  16.498   9.877  1.00 19.63           H
ATOM   1290  HD1 PHE A  90      20.629  19.931  10.026  1.00 20.72           H
ATOM   1291  HD2 PHE A  90      22.508  16.944  11.852  1.00 22.56           H
ATOM   1292  HE1 PHE A  90      21.109  21.343  11.814  1.00 20.21           H
ATOM   1293  HE2 PHE A  90      22.954  18.312  13.655  1.00 22.09           H
ATOM   1294  HZ  PHE A  90      22.266  20.496  13.636  1.00 22.08           H
ATOM   1295  N   ASP A  91      22.133  15.556   7.019  1.00 17.54           N
ANISOU 1295  N   ASP A  91     2277   2523   1865    -44    667   -265       N
ATOM   1296  CA  ASP A  91      21.559  14.760   5.942  1.00 17.68           C
ANISOU 1296  CA  ASP A  91     2376   2583   1758   -193    764   -412       C
ATOM   1297  C   ASP A  91      20.126  14.344   6.286  1.00 17.03           C
ANISOU 1297  C   ASP A  91     2396   2362   1712   -169    661   -355       C
ATOM   1298  O   ASP A  91      19.606  14.630   7.361  1.00 17.34           O
ANISOU 1298  O   ASP A  91     2433   2277   1879    -35    543   -228       O
ATOM   1299  CB  ASP A  91      22.506  13.613   5.528  1.00 22.40           C
ANISOU 1299  CB  ASP A  91     2897   3169   2446   -151   1026   -689       C
ATOM   1300  CG  ASP A  91      22.557  12.455   6.528  1.00 22.99           C
ANISOU 1300  CG  ASP A  91     2916   2974   2844    114   1077   -728       C
ATOM   1301  OD1 ASP A  91      21.682  12.328   7.403  1.00 21.47           O
ANISOU 1301  OD1 ASP A  91     2790   2651   2716    209    929   -579       O
ATOM   1302  OD2 ASP A  91      23.518  11.657   6.373  1.00 27.28           O
ANISOU 1302  OD2 ASP A  91     3322   3439   3605    204   1277   -909       O
ATOM   1303  H   ASP A  91      22.694  15.136   7.518  1.00 21.07           H
ATOM   1304  HA  ASP A  91      21.471  15.289   5.133  1.00 21.16           H
ATOM   1305  HB2 ASP A  91      22.207  13.254   4.678  1.00 26.90           H
ATOM   1306  HB3 ASP A  91      23.404  13.967   5.442  1.00 26.90           H
ATOM   1307  N   VAL A  92      19.467  13.705   5.314  1.00 19.72           N
ANISOU 1307  N   VAL A  92     2820   2764   1908   -353    719   -470       N
ATOM   1308  CA  VAL A  92      18.052  13.377   5.438  1.00 20.17           C
ANISOU 1308  CA  VAL A  92     2964   2734   1967   -385    609   -401       C
ATOM   1309  C   VAL A  92      17.814  12.328   6.507  1.00 21.70           C
ANISOU 1309  C   VAL A  92     3168   2689   2386   -154    662   -468       C
ATOM   1310  O   VAL A  92      16.656  12.111   6.892  1.00 23.44           O
ANISOU 1310  O   VAL A  92     3445   2824   2638   -148    565   -393       O
ATOM   1311  CB  VAL A  92      17.508  12.980   4.055  1.00 23.54           C
ANISOU 1311  CB  VAL A  92     3468   3346   2128   -711    651   -504       C
ATOM   1312  CG1 VAL A  92      17.983  11.584   3.669  1.00 24.04           C
ANISOU 1312  CG1 VAL A  92     3557   3358   2219   -728    932   -866       C
ATOM   1313  CG2 VAL A  92      15.984  13.044   3.991  1.00 28.35           C
ANISOU 1313  CG2 VAL A  92     4133   3938   2700   -816    461   -333       C
ATOM   1314  H   VAL A  92      19.821  13.451   4.573  1.00 23.68           H
ATOM   1315  HA  VAL A  92      17.538  14.150   5.720  1.00 24.22           H
ATOM   1316  HB  VAL A  92      17.853  13.623   3.417  1.00 28.25           H
ATOM   1317 HG11 VAL A  92      17.785  11.432   2.732  1.00 28.86           H
ATOM   1318 HG12 VAL A  92      18.939  11.523   3.820  1.00 28.86           H
ATOM   1319 HG13 VAL A  92      17.519  10.931   4.216  1.00 28.86           H
ATOM   1320 HG21 VAL A  92      15.696  12.812   3.094  1.00 34.03           H
ATOM   1321 HG22 VAL A  92      15.614  12.416   4.630  1.00 34.03           H
ATOM   1322 HG23 VAL A  92      15.696  13.945   4.207  1.00 34.03           H
ATOM   1323  N   ASN A  93      18.876  11.665   6.973  1.00 21.31           N
ANISOU 1323  N   ASN A  93     3042   2537   2517     16    799   -574       N
ATOM   1324  CA  ASN A  93      18.829  10.749   8.114  1.00 23.96           C
ANISOU 1324  CA  ASN A  93     3346   2652   3106    221    797   -533       C
ATOM   1325  C   ASN A  93      19.162  11.415   9.441  1.00 22.13           C
ANISOU 1325  C   ASN A  93     3041   2426   2943    354    658   -320       C
ATOM   1326  O   ASN A  93      19.313  10.711  10.451  1.00 23.68           O
ANISOU 1326  O   ASN A  93     3182   2499   3314    475    626   -224       O
ATOM   1327  CB  ASN A  93      19.792   9.584   7.865  1.00 26.00           C
ANISOU 1327  CB  ASN A  93     3506   2758   3614    315   1004   -724       C
ATOM   1328  CG  ASN A  93      19.383   8.728   6.691  1.00 33.96           C
ANISOU 1328  CG  ASN A  93     4584   3743   4576    145   1177  -1004       C
ATOM   1329  OD1 ASN A  93      18.196   8.478   6.491  1.00 31.34           O
ANISOU 1329  OD1 ASN A  93     4387   3397   4122     27   1134  -1022       O
ATOM   1330  ND2 ASN A  93      20.356   8.304   5.890  1.00 34.26           N
ANISOU 1330  ND2 ASN A  93     4513   3818   4687     91   1329  -1192       N
ATOM   1331  H   ASN A  93      19.663  11.733   6.632  1.00 25.58           H
ATOM   1332  HA  ASN A  93      17.927  10.400   8.189  1.00 28.77           H
ATOM   1333  HB2 ASN A  93      20.677   9.938   7.685  1.00 31.21           H
ATOM   1334  HB3 ASN A  93      19.814   9.019   8.654  1.00 31.21           H
ATOM   1335 HD21 ASN A  93      21.173   8.520   6.053  1.00 41.13           H
ATOM   1336 HD22 ASN A  93      20.169   7.814   5.208  1.00 41.13           H
ATOM   1337  N   GLY A  94      19.275  12.735   9.469  1.00 19.28           N
ANISOU 1337  N   GLY A  94     2666   2208   2451    294    572   -236       N
ATOM   1338  CA  GLY A  94      19.542  13.469  10.681  1.00 16.88           C
ANISOU 1338  CA  GLY A  94     2299   1938   2175    350    473   -102       C
ATOM   1339  C   GLY A  94      20.999  13.581  11.094  1.00 18.79           C
ANISOU 1339  C   GLY A  94     2410   2244   2485    425    497    -59       C
ATOM   1340  O   GLY A  94      21.275  14.213  12.133  1.00 19.58           O
ANISOU 1340  O   GLY A  94     2457   2420   2563    416    414     42       O
ATOM   1341  H   GLY A  94      19.197  13.238   8.776  1.00 23.15           H
ATOM   1342  HA2 GLY A  94      19.202  14.371  10.573  1.00 20.26           H
ATOM   1343  HA3 GLY A  94      19.067  13.039  11.409  1.00 20.26           H
ATOM   1344  N   LYS A  95      21.938  13.042  10.322  1.00 19.09           N
ANISOU 1344  N   LYS A  95     2375   2273   2603    467    622   -155       N
ATOM   1345  CA  LYS A  95      23.346  13.049  10.716  1.00 22.06           C
ANISOU 1345  CA  LYS A  95     2577   2696   3107    554    644    -96       C
ATOM   1346  C   LYS A  95      23.948  14.425  10.446  1.00 22.92           C
ANISOU 1346  C   LYS A  95     2664   2993   3051    453    618    -84       C
ATOM   1347  O   LYS A  95      23.728  15.002   9.373  1.00 22.25           O
ANISOU 1347  O   LYS A  95     2652   2987   2817    327    663   -172       O
ATOM   1348  CB  LYS A  95      24.124  11.982   9.952  1.00 23.15           C
ANISOU 1348  CB  LYS A  95     2598   2723   3474    639    834   -253       C
ATOM   1349  CG  LYS A  95      25.582  11.869  10.364  1.00 39.11           C
ANISOU 1349  CG  LYS A  95     4376   4758   5726    754    855   -167       C
ATOM   1350  CD  LYS A  95      26.434  11.134   9.319  1.00 54.45           C
ANISOU 1350  CD  LYS A  95     6165   6614   7910    804   1120   -424       C
ATOM   1351  CE  LYS A  95      27.934  11.193   9.652  1.00 52.59           C
ANISOU 1351  CE  LYS A  95     5662   6421   7900    898   1115   -325       C
ATOM   1352  NZ  LYS A  95      28.274  12.080  10.811  1.00 60.64           N
ANISOU 1352  NZ  LYS A  95     6624   7602   8815    897    885    -10       N
ATOM   1353  H   LYS A  95      21.786  12.665   9.563  1.00 22.92           H
ATOM   1354  HA  LYS A  95      23.416  12.854  11.664  1.00 26.48           H
ATOM   1355  HB2 LYS A  95      23.705  11.121  10.107  1.00 27.79           H
ATOM   1356  HB3 LYS A  95      24.100  12.197   9.006  1.00 27.79           H
ATOM   1357  HG2 LYS A  95      25.949  12.759  10.478  1.00 46.94           H
ATOM   1358  HG3 LYS A  95      25.638  11.376  11.198  1.00 46.94           H
ATOM   1359  HD2 LYS A  95      26.167  10.201   9.288  1.00 65.35           H
ATOM   1360  HD3 LYS A  95      26.300  11.546   8.451  1.00 65.35           H
ATOM   1361  HE2 LYS A  95      28.239  10.298   9.869  1.00 63.12           H
ATOM   1362  HE3 LYS A  95      28.411  11.528   8.877  1.00 63.12           H
ATOM   1363  HZ1 LYS A  95      28.023  12.917  10.639  1.00 72.78           H
ATOM   1364  HZ2 LYS A  95      29.152  12.067  10.957  1.00 72.78           H
ATOM   1365  HZ3 LYS A  95      27.855  11.798  11.544  1.00 72.78           H
ATOM   1366  N   THR A  96      24.697  14.957  11.408  1.00 22.41           N
ANISOU 1366  N   THR A  96     2495   3019   3002    468    529     50       N
ATOM   1367  CA  THR A  96      25.383  16.225  11.192  1.00 21.73           C
ANISOU 1367  CA  THR A  96     2371   3087   2797    366    513     56       C
ATOM   1368  C   THR A  96      26.503  16.032  10.190  1.00 24.69           C
ANISOU 1368  C   THR A  96     2630   3534   3217    376    654    -36       C
ATOM   1369  O   THR A  96      27.356  15.150  10.363  1.00 28.28           O
ANISOU 1369  O   THR A  96     2917   3946   3883    502    724    -34       O
ATOM   1370  CB  THR A  96      26.025  16.730  12.476  1.00 31.73           C
ANISOU 1370  CB  THR A  96     3537   4463   4055    338    403    191       C
ATOM   1371  OG1 THR A  96      25.115  16.580  13.549  1.00 39.21           O
ANISOU 1371  OG1 THR A  96     4555   5380   4965    304    314    246       O
ATOM   1372  CG2 THR A  96      26.391  18.198  12.287  1.00 21.44           C
ANISOU 1372  CG2 THR A  96     2240   3273   2634    198    384    167       C
ATOM   1373  H   THR A  96      24.822  14.609  12.184  1.00 26.91           H
ATOM   1374  HA  THR A  96      24.731  16.869  10.876  1.00 26.08           H
ATOM   1375  HB  THR A  96      26.828  16.230  12.690  1.00 38.09           H
ATOM   1376  HG1 THR A  96      25.462  16.857  14.261  1.00 47.07           H
ATOM   1377 HG21 THR A  96      26.410  18.648  13.146  1.00 25.74           H
ATOM   1378 HG22 THR A  96      27.265  18.271  11.874  1.00 25.74           H
ATOM   1379 HG23 THR A  96      25.736  18.632  11.719  1.00 25.74           H
ATOM   1380  N   ILE A  97      26.537  16.874   9.159  1.00 21.92           N
ANISOU 1380  N   ILE A  97     2335   3295   2700    224    695   -101       N
ATOM   1381  CA  ILE A  97      27.628  16.830   8.197  1.00 24.89           C
ANISOU 1381  CA  ILE A  97     2593   3806   3056    165    853   -216       C
ATOM   1382  C   ILE A  97      28.413  18.123   8.119  1.00 22.07           C
ANISOU 1382  C   ILE A  97     2181   3623   2581     33    795   -126       C
ATOM   1383  O   ILE A  97      29.497  18.132   7.519  1.00 24.48           O
ANISOU 1383  O   ILE A  97     2350   4072   2880    -18    925   -206       O
ATOM   1384  CB  ILE A  97      27.157  16.376   6.803  1.00 25.58           C
ANISOU 1384  CB  ILE A  97     2768   3941   3009     21   1004   -406       C
ATOM   1385  CG1 ILE A  97      26.164  17.351   6.190  1.00 21.21           C
ANISOU 1385  CG1 ILE A  97     2381   3466   2210   -199    865   -295       C
ATOM   1386  CG2 ILE A  97      26.512  14.993   6.931  1.00 32.70           C
ANISOU 1386  CG2 ILE A  97     3703   4641   4082    155   1090   -530       C
ATOM   1387  CD1 ILE A  97      25.724  16.979   4.776  1.00 26.80           C
ANISOU 1387  CD1 ILE A  97     3169   4316   2697   -442    976   -436       C
ATOM   1388  H   ILE A  97      25.942  17.474   9.000  1.00 26.32           H
ATOM   1389  HA  ILE A  97      28.257  16.155   8.497  1.00 29.87           H
ATOM   1390  HB  ILE A  97      27.930  16.344   6.217  1.00 30.71           H
ATOM   1391 HG12 ILE A  97      25.372  17.380   6.749  1.00 25.46           H
ATOM   1392 HG13 ILE A  97      26.574  18.229   6.151  1.00 25.46           H
ATOM   1393 HG21 ILE A  97      26.356  14.634   6.044  1.00 39.26           H
ATOM   1394 HG22 ILE A  97      27.111  14.410   7.424  1.00 39.26           H
ATOM   1395 HG23 ILE A  97      25.671  15.080   7.406  1.00 39.26           H
ATOM   1396 HD11 ILE A  97      25.203  17.708   4.405  1.00 32.17           H
ATOM   1397 HD12 ILE A  97      26.511  16.824   4.231  1.00 32.17           H
ATOM   1398 HD13 ILE A  97      25.185  16.173   4.815  1.00 32.17           H
ATOM   1399  N   SER A  98      27.935  19.205   8.722  1.00 20.31           N
ANISOU 1399  N   SER A  98     2037   3377   2301    -34    628     10       N
ATOM   1400  C   SER A  98      28.135  21.317   9.888  1.00 19.08           C
ANISOU 1400  C   SER A  98     1873   3237   2139   -183    430    168       C
ATOM   1401  O   SER A  98      26.967  21.179  10.273  1.00 20.81           O
ANISOU 1401  O   SER A  98     2195   3306   2406   -142    382    157       O
ATOM   1402  CA ASER A  98      28.736  20.417   8.818  0.26 19.88           C
ANISOU 1402  CA ASER A  98     1916   3444   2195   -156    572     92       C
ATOM   1403  CB ASER A  98      28.888  21.135   7.471  0.26 22.98           C
ANISOU 1403  CB ASER A  98     2336   3969   2428   -377    598    110       C
ATOM   1404  OG ASER A  98      27.700  21.794   7.078  0.26 27.19           O
ANISOU 1404  OG ASER A  98     3002   4400   2929   -495    471    218       O
ATOM   1405  H  ASER A  98      27.155  19.261   9.081  0.26 24.38           H
ATOM   1406  HA ASER A  98      29.633  20.182   9.104  0.26 23.87           H
ATOM   1407  HB2ASER A  98      29.596  21.794   7.548  0.26 27.59           H
ATOM   1408  HB3ASER A  98      29.117  20.480   6.794  0.26 27.59           H
ATOM   1409  HG ASER A  98      27.515  22.402   7.626  0.26 32.64           H
ATOM   1410  CA BSER A  98      28.688  20.452   8.764  0.74 19.66           C
ANISOU 1410  CA BSER A  98     1895   3414   2159   -165    570     93       C
ATOM   1411  CB BSER A  98      28.596  21.185   7.421  0.74 22.10           C
ANISOU 1411  CB BSER A  98     2258   3828   2311   -388    577    123       C
ATOM   1412  OG BSER A  98      29.564  22.211   7.333  0.74 21.75           O
ANISOU 1412  OG BSER A  98     2125   3913   2225   -522    550    199       O
ATOM   1413  H  BSER A  98      27.172  19.243   9.118  0.74 24.38           H
ATOM   1414  HA BSER A  98      29.622  20.274   8.955  0.74 23.60           H
ATOM   1415  HB2BSER A  98      28.746  20.549   6.704  0.74 26.53           H
ATOM   1416  HB3BSER A  98      27.713  21.578   7.336  0.74 26.53           H
ATOM   1417  HG BSER A  98      29.580  22.653   8.048  0.74 26.11           H
ATOM   1418  N   GLY A  99      28.980  22.211  10.405  1.00 23.26           N
ANISOU 1418  N   GLY A  99     2318   3854   2665   -270    390    209       N
ATOM   1419  CA  GLY A  99      28.570  23.119  11.453  1.00 21.58           C
ANISOU 1419  CA  GLY A  99     2135   3558   2507   -348    313    199       C
ATOM   1420  C   GLY A  99      28.850  22.621  12.854  1.00 24.22           C
ANISOU 1420  C   GLY A  99     2408   3978   2815   -316    289    183       C
ATOM   1421  O   GLY A  99      29.413  21.545  13.058  1.00 23.34           O
ANISOU 1421  O   GLY A  99     2206   3960   2702   -202    293    248       O
ATOM   1422  H   GLY A  99      29.799  22.305  10.159  1.00 27.92           H
ATOM   1423  HA2 GLY A  99      29.036  23.962  11.338  1.00 25.91           H
ATOM   1424  HA3 GLY A  99      27.615  23.274  11.377  1.00 25.91           H
ATOM   1425  N   PRO A 100      28.424  23.399  13.852  1.00 20.92           N
ANISOU 1425  N   PRO A 100     2020   3527   2402   -447    265    100       N
ATOM   1426  CA  PRO A 100      28.883  23.180  15.228  1.00 22.23           C
ANISOU 1426  CA  PRO A 100     2112   3882   2452   -548    225    101       C
ATOM   1427  C   PRO A 100      28.054  22.234  16.073  1.00 21.88           C
ANISOU 1427  C   PRO A 100     2113   3843   2358   -513    203    105       C
ATOM   1428  O   PRO A 100      28.351  22.094  17.271  1.00 23.33           O
ANISOU 1428  O   PRO A 100     2236   4234   2395   -674    147    137       O
ATOM   1429  CB  PRO A 100      28.819  24.601  15.815  1.00 23.72           C
ANISOU 1429  CB  PRO A 100     2312   4050   2651   -786    260    -68       C
ATOM   1430  CG  PRO A 100      27.679  25.227  15.128  1.00 21.68           C
ANISOU 1430  CG  PRO A 100     2147   3485   2604   -739    313   -165       C
ATOM   1431  CD  PRO A 100      27.765  24.711  13.703  1.00 22.53           C
ANISOU 1431  CD  PRO A 100     2278   3542   2741   -569    280      2       C
ATOM   1432  HA  PRO A 100      29.798  22.860  15.216  1.00 26.69           H
ATOM   1433  HB2 PRO A 100      28.670  24.559  16.773  1.00 28.48           H
ATOM   1434  HB3 PRO A 100      29.644  25.076  15.628  1.00 28.48           H
ATOM   1435  HG2 PRO A 100      26.847  24.956  15.548  1.00 26.02           H
ATOM   1436  HG3 PRO A 100      27.764  26.193  15.154  1.00 26.02           H
ATOM   1437  HD2 PRO A 100      26.880  24.610  13.319  1.00 27.05           H
ATOM   1438  HD3 PRO A 100      28.300  25.304  13.153  1.00 27.05           H
ATOM   1439  N   ALA A 101      27.012  21.595  15.543  1.00 20.73           N
ANISOU 1439  N   ALA A 101     2067   3512   2296   -358    233     88       N
ATOM   1440  CA  ALA A 101      26.173  20.768  16.403  1.00 20.10           C
ANISOU 1440  CA  ALA A 101     2032   3443   2164   -360    212     92       C
ATOM   1441  C   ALA A 101      26.994  19.622  16.989  1.00 23.04           C
ANISOU 1441  C   ALA A 101     2284   3989   2482   -326    108    321       C
ATOM   1442  O   ALA A 101      27.778  18.997  16.268  1.00 24.30           O
ANISOU 1442  O   ALA A 101     2350   4117   2763   -158     98    444       O
ATOM   1443  CB  ALA A 101      24.990  20.190  15.634  1.00 22.48           C
ANISOU 1443  CB  ALA A 101     2446   3521   2575   -198    252     59       C
ATOM   1444  H   ALA A 101      26.777  21.623  14.717  1.00 24.89           H
ATOM   1445  HA  ALA A 101      25.831  21.320  17.124  1.00 24.14           H
ATOM   1446  HB1 ALA A 101      24.454  19.652  16.237  1.00 26.99           H
ATOM   1447  HB2 ALA A 101      24.458  20.919  15.279  1.00 26.99           H
ATOM   1448  HB3 ALA A 101      25.324  19.640  14.907  1.00 26.99           H
ATOM   1449  N   PRO A 102      26.850  19.325  18.282  1.00 21.61           N
ANISOU 1449  N   PRO A 102     2072   3993   2144   -507     29    394       N
ATOM   1450  CA  PRO A 102      27.633  18.238  18.889  1.00 24.70           C
ANISOU 1450  CA  PRO A 102     2306   4543   2538   -503   -131    715       C
ATOM   1451  C   PRO A 102      27.051  16.858  18.668  1.00 22.81           C
ANISOU 1451  C   PRO A 102     2080   4118   2468   -303   -165    859       C
ATOM   1452  O   PRO A 102      27.638  15.877  19.144  1.00 27.35           O
ANISOU 1452  O   PRO A 102     2492   4751   3149   -278   -314   1170       O
ATOM   1453  CB  PRO A 102      27.599  18.592  20.384  1.00 26.57           C
ANISOU 1453  CB  PRO A 102     2517   5110   2469   -880   -217    746       C
ATOM   1454  CG  PRO A 102      26.239  19.216  20.522  1.00 26.03           C
ANISOU 1454  CG  PRO A 102     2629   4941   2320   -977    -53    408       C
ATOM   1455  CD  PRO A 102      26.069  20.060  19.298  1.00 22.39           C
ANISOU 1455  CD  PRO A 102     2243   4201   2063   -783     87    189       C
ATOM   1456  HA  PRO A 102      28.547  18.264  18.566  1.00 29.66           H
ATOM   1457  HB2 PRO A 102      27.684  17.794  20.928  1.00 31.90           H
ATOM   1458  HB3 PRO A 102      28.305  19.220  20.604  1.00 31.90           H
ATOM   1459  HG2 PRO A 102      25.561  18.524  20.561  1.00 31.25           H
ATOM   1460  HG3 PRO A 102      26.205  19.760  21.324  1.00 31.25           H
ATOM   1461  HD2 PRO A 102      25.135  20.117  19.043  1.00 26.88           H
ATOM   1462  HD3 PRO A 102      26.430  20.949  19.436  1.00 26.88           H
ATOM   1463  N   ARG A 103      25.912  16.767  17.991  1.00 21.43           N
ANISOU 1463  N   ARG A 103     2073   3716   2354   -181    -47    668       N
ATOM   1464  CA  ARG A 103      25.234  15.509  17.707  1.00 22.73           C
ANISOU 1464  CA  ARG A 103     2276   3683   2675    -16    -53    750       C
ATOM   1465  C   ARG A 103      24.261  15.778  16.570  1.00 22.11           C
ANISOU 1465  C   ARG A 103     2364   3386   2651    104     92    502       C
ATOM   1466  O   ARG A 103      24.045  16.927  16.177  1.00 21.44           O
ANISOU 1466  O   ARG A 103     2345   3303   2500     43    162    325       O
ATOM   1467  CB  ARG A 103      24.498  14.983  18.937  1.00 21.59           C
ANISOU 1467  CB  ARG A 103     2157   3662   2383   -200   -155    880       C
ATOM   1468  CG  ARG A 103      23.609  16.015  19.612  1.00 25.11           C
ANISOU 1468  CG  ARG A 103     2720   4255   2568   -452    -74    634       C
ATOM   1469  CD  ARG A 103      22.476  15.348  20.347  1.00 24.93           C
ANISOU 1469  CD  ARG A 103     2767   4267   2440   -576    -92    663       C
ATOM   1470  NE  ARG A 103      21.577  14.690  19.412  1.00 20.82           N
ANISOU 1470  NE  ARG A 103     2349   3443   2120   -336    -26    600       N
ATOM   1471  CZ  ARG A 103      20.725  13.736  19.739  1.00 21.85           C
ANISOU 1471  CZ  ARG A 103     2525   3521   2254   -355    -64    696       C
ATOM   1472  NH1 ARG A 103      20.590  13.325  21.000  1.00 24.17           N
ANISOU 1472  NH1 ARG A 103     2777   4061   2347   -619   -172    877       N
ATOM   1473  NH2 ARG A 103      19.951  13.209  18.789  1.00 21.40           N
ANISOU 1473  NH2 ARG A 103     2562   3194   2373   -154      5    611       N
ATOM   1474  H   ARG A 103      25.495  17.448  17.672  1.00 25.73           H
ATOM   1475  HA  ARG A 103      25.877  14.836  17.433  1.00 27.28           H
ATOM   1476  HB2 ARG A 103      23.936  14.240  18.669  1.00 25.92           H
ATOM   1477  HB3 ARG A 103      25.153  14.687  19.588  1.00 25.92           H
ATOM   1478  HG2 ARG A 103      24.132  16.524  20.251  1.00 30.15           H
ATOM   1479  HG3 ARG A 103      23.235  16.608  18.942  1.00 30.15           H
ATOM   1480  HD2 ARG A 103      22.831  14.682  20.956  1.00 29.93           H
ATOM   1481  HD3 ARG A 103      21.973  16.015  20.841  1.00 29.93           H
ATOM   1482  HE  ARG A 103      21.603  14.939  18.589  1.00 25.00           H
ATOM   1483 HH11 ARG A 103      21.064  13.683  21.622  1.00 29.02           H
ATOM   1484 HH12 ARG A 103      20.029  12.702  21.192  1.00 29.02           H
ATOM   1485 HH21 ARG A 103      20.012  13.491  17.979  1.00 25.69           H
ATOM   1486 HH22 ARG A 103      19.391  12.587  18.986  1.00 25.69           H
ATOM   1487  N   GLY A 104      23.646  14.710  16.068  1.00 20.84           N
ANISOU 1487  N   GLY A 104     2256   3034   2629    245    119    516       N
ATOM   1488  CA  GLY A 104      22.651  14.837  15.020  1.00 18.92           C
ANISOU 1488  CA  GLY A 104     2158   2627   2403    307    222    327       C
ATOM   1489  C   GLY A 104      21.269  15.218  15.548  1.00 17.44           C
ANISOU 1489  C   GLY A 104     2083   2433   2111    195    221    237       C
ATOM   1490  O   GLY A 104      21.054  15.447  16.745  1.00 17.49           O
ANISOU 1490  O   GLY A 104     2069   2581   1997     41    180    261       O
ATOM   1491  H   GLY A 104      23.792  13.901  16.321  1.00 25.02           H
ATOM   1492  HA2 GLY A 104      22.934  15.521  14.393  1.00 22.72           H
ATOM   1493  HA3 GLY A 104      22.573  13.992  14.551  1.00 22.72           H
ATOM   1494  N   MET A 105      20.312  15.282  14.616  1.00 16.20           N
ANISOU 1494  N   MET A 105     2025   2132   1998    240    276    124       N
ATOM   1495  CA  MET A 105      18.960  15.721  14.927  1.00 15.72           C
ANISOU 1495  CA  MET A 105     2025   2026   1921    159    291     28       C
ATOM   1496  C   MET A 105      18.314  14.753  15.922  1.00 16.40           C
ANISOU 1496  C   MET A 105     2132   2142   1958    109    263     89       C
ATOM   1497  O   MET A 105      18.642  13.567  15.991  1.00 17.64           O
ANISOU 1497  O   MET A 105     2284   2264   2156    176    217    230       O
ATOM   1498  CB  MET A 105      18.138  15.860  13.641  1.00 14.85           C
ANISOU 1498  CB  MET A 105     1980   1777   1886    202    307    -23       C
ATOM   1499  CG  MET A 105      18.588  17.065  12.817  1.00 15.54           C
ANISOU 1499  CG  MET A 105     2031   1865   2007    170    301    -34       C
ATOM   1500  SD  MET A 105      18.006  17.144  11.111  1.00 16.16           S
ANISOU 1500  SD  MET A 105     2160   1884   2097    135    263     14       S
ATOM   1501  CE  MET A 105      16.258  17.207  11.380  1.00 17.98           C
ANISOU 1501  CE  MET A 105     2393   1983   2456    109    221     10       C
ATOM   1502  H   MET A 105      20.426  15.074  13.790  1.00 19.45           H
ATOM   1503  HA  MET A 105      18.977  16.602  15.333  1.00 18.87           H
ATOM   1504  HB2 MET A 105      18.249  15.061  13.102  1.00 17.83           H
ATOM   1505  HB3 MET A 105      17.203  15.977  13.870  1.00 17.83           H
ATOM   1506  HG2 MET A 105      18.271  17.868  13.261  1.00 18.66           H
ATOM   1507  HG3 MET A 105      19.557  17.063  12.786  1.00 18.66           H
ATOM   1508  HE1 MET A 105      15.809  17.279  10.523  1.00 21.59           H
ATOM   1509  HE2 MET A 105      15.978  16.395  11.832  1.00 21.59           H
ATOM   1510  HE3 MET A 105      16.050  17.979  11.929  1.00 21.59           H
ATOM   1511  N   TYR A 106      17.400  15.277  16.716  1.00 16.13           N
ANISOU 1511  N   TYR A 106     2098   2162   1869    -29    302    -20       N
ATOM   1512  CA  TYR A 106      16.716  14.466  17.723  1.00 16.57           C
ANISOU 1512  CA  TYR A 106     2169   2304   1825   -145    284     31       C
ATOM   1513  C   TYR A 106      15.653  13.606  17.032  1.00 16.65           C
ANISOU 1513  C   TYR A 106     2259   2134   1934    -48    285     43       C
ATOM   1514  O   TYR A 106      14.817  14.128  16.289  1.00 18.13           O
ANISOU 1514  O   TYR A 106     2464   2202   2223     -7    331    -78       O
ATOM   1515  CB  TYR A 106      16.049  15.394  18.746  1.00 16.93           C
ANISOU 1515  CB  TYR A 106     2167   2490   1776   -368    388   -177       C
ATOM   1516  CG  TYR A 106      16.989  16.315  19.466  1.00 16.40           C
ANISOU 1516  CG  TYR A 106     2027   2617   1587   -530    416   -253       C
ATOM   1517  CD1 TYR A 106      17.847  15.819  20.431  1.00 18.91           C
ANISOU 1517  CD1 TYR A 106     2307   3201   1675   -701    316    -69       C
ATOM   1518  CD2 TYR A 106      16.990  17.692  19.236  1.00 17.86           C
ANISOU 1518  CD2 TYR A 106     2160   2721   1903   -549    529   -488       C
ATOM   1519  CE1 TYR A 106      18.708  16.651  21.115  1.00 20.18           C
ANISOU 1519  CE1 TYR A 106     2398   3588   1681   -905    331   -136       C
ATOM   1520  CE2 TYR A 106      17.840  18.544  19.926  1.00 18.37           C
ANISOU 1520  CE2 TYR A 106     2162   2964   1855   -735    573   -594       C
ATOM   1521  CZ  TYR A 106      18.699  18.023  20.869  1.00 19.91           C
ANISOU 1521  CZ  TYR A 106     2337   3471   1758   -926    478   -433       C
ATOM   1522  OH  TYR A 106      19.541  18.875  21.541  1.00 22.40           O
ANISOU 1522  OH  TYR A 106     2587   4000   1924  -1156    513   -541       O
ATOM   1523  H   TYR A 106      17.152  16.100  16.697  1.00 19.37           H
ATOM   1524  HA  TYR A 106      17.344  13.887  18.183  1.00 19.90           H
ATOM   1525  HB2 TYR A 106      15.397  15.944  18.284  1.00 20.33           H
ATOM   1526  HB3 TYR A 106      15.606  14.847  19.415  1.00 20.33           H
ATOM   1527  HD1 TYR A 106      17.843  14.909  20.622  1.00 22.70           H
ATOM   1528  HD2 TYR A 106      16.406  18.046  18.604  1.00 21.44           H
ATOM   1529  HE1 TYR A 106      19.296  16.296  21.742  1.00 24.23           H
ATOM   1530  HE2 TYR A 106      17.831  19.458  19.753  1.00 22.06           H
ATOM   1531  HH  TYR A 106      20.319  18.558  21.556  1.00 26.89           H
ATOM   1532  N  ASER A 107      15.658  12.302  17.291  0.45 17.93           N
ANISOU 1532  N  ASER A 107     2448   2270   2093    -34    217    213       N
ATOM   1533  CA ASER A 107      14.784  11.385  16.568  0.45 17.95           C
ANISOU 1533  CA ASER A 107     2532   2089   2197     44    222    214       C
ATOM   1534  C  ASER A 107      13.772  10.718  17.490  0.45 18.49           C
ANISOU 1534  C  ASER A 107     2621   2215   2189   -102    202    271       C
ATOM   1535  O  ASER A 107      14.134  10.130  18.510  0.45 20.75           O
ANISOU 1535  O  ASER A 107     2870   2622   2393   -219    121    460       O
ATOM   1536  CB ASER A 107      15.605  10.324  15.835  0.45 23.76           C
ANISOU 1536  CB ASER A 107     3276   2660   3091    194    198    317       C
ATOM   1537  OG ASER A 107      16.287   9.508  16.765  0.45 24.02           O
ANISOU 1537  OG ASER A 107     3232   2720   3176    170    102    554       O
ATOM   1538  H  ASER A 107      16.159  11.926  17.880  0.45 21.52           H
ATOM   1539  HA ASER A 107      14.271  11.902  15.927  0.45 21.55           H
ATOM   1540  HB2ASER A 107      15.011   9.772  15.303  0.45 28.52           H
ATOM   1541  HB3ASER A 107      16.253  10.763  15.262  0.45 28.52           H
ATOM   1542  HG ASER A 107      15.736   9.054  17.207  0.45 28.84           H
ATOM   1543  N  BSER A 107      15.674  12.301  17.310  0.55 17.89           N
ANISOU 1543  N  BSER A 107     2443   2268   2087    -36    215    215       N
ATOM   1544  CA BSER A 107      14.837  11.310  16.632  0.55 18.02           C
ANISOU 1544  CA BSER A 107     2539   2102   2205     42    216    230       C
ATOM   1545  C  BSER A 107      13.739  10.823  17.570  0.55 18.67           C
ANISOU 1545  C  BSER A 107     2639   2257   2198   -117    207    260       C
ATOM   1546  O  BSER A 107      14.003  10.529  18.735  0.55 21.73           O
ANISOU 1546  O  BSER A 107     2982   2818   2456   -275    147    401       O
ATOM   1547  CB BSER A 107      15.703  10.120  16.199  0.55 22.62           C
ANISOU 1547  CB BSER A 107     3115   2537   2943    173    172    379       C
ATOM   1548  OG BSER A 107      14.977   9.153  15.443  0.55 24.37           O
ANISOU 1548  OG BSER A 107     3418   2561   3281    226    204    336       O
ATOM   1549  H  BSER A 107      16.183  11.953  17.910  0.55 21.48           H
ATOM   1550  HA BSER A 107      14.414  11.712  15.857  0.55 21.63           H
ATOM   1551  HB2BSER A 107      16.432  10.453  15.652  0.55 27.16           H
ATOM   1552  HB3BSER A 107      16.054   9.690  16.994  0.55 27.16           H
ATOM   1553  HG BSER A 107      14.377   8.807  15.919  0.55 29.26           H
ATOM   1554  N   TYR A 108      12.519  10.741  17.068  1.00 16.72           N
ANISOU 1554  N   TYR A 108     2441   1913   1999   -115    253    150       N
ATOM   1555  CA  TYR A 108      11.383  10.259  17.846  1.00 18.39           C
ANISOU 1555  CA  TYR A 108     2660   2193   2136   -271    265    156       C
ATOM   1556  C   TYR A 108      11.076   8.799  17.535  1.00 19.44           C
ANISOU 1556  C   TYR A 108     2872   2167   2348   -237    197    307       C
ATOM   1557  O   TYR A 108      11.059   8.389  16.362  1.00 20.33           O
ANISOU 1557  O   TYR A 108     3046   2085   2593   -104    206    265       O
ATOM   1558  CB  TYR A 108      10.113  11.043  17.477  1.00 19.83           C
ANISOU 1558  CB  TYR A 108     2803   2340   2389   -292    357    -50       C
ATOM   1559  CG  TYR A 108      10.028  12.420  18.058  1.00 18.70           C
ANISOU 1559  CG  TYR A 108     2542   2308   2256   -375    468   -248       C
ATOM   1560  CD1 TYR A 108      10.874  13.460  17.640  1.00 20.33           C
ANISOU 1560  CD1 TYR A 108     2707   2479   2539   -287    480   -308       C
ATOM   1561  CD2 TYR A 108       9.070  12.727  19.000  1.00 23.74           C
ANISOU 1561  CD2 TYR A 108     3090   3070   2858   -562    592   -416       C
ATOM   1562  CE1 TYR A 108      10.785  14.711  18.190  1.00 19.92           C
ANISOU 1562  CE1 TYR A 108     2534   2477   2558   -376    604   -521       C
ATOM   1563  CE2 TYR A 108       8.976  13.994  19.565  1.00 23.94           C
ANISOU 1563  CE2 TYR A 108     2979   3162   2954   -661    753   -679       C
ATOM   1564  CZ  TYR A 108       9.842  14.983  19.146  1.00 21.41           C
ANISOU 1564  CZ  TYR A 108     2625   2763   2746   -559    754   -729       C
ATOM   1565  OH  TYR A 108       9.743  16.235  19.694  1.00 25.32           O
ANISOU 1565  OH  TYR A 108     2975   3271   3375   -664    932  -1019       O
ATOM   1566  H   TYR A 108      12.316  10.962  16.262  1.00 20.08           H
ATOM   1567  HA  TYR A 108      11.607  10.361  18.785  1.00 22.09           H
ATOM   1568  HB2 TYR A 108      10.077  11.132  16.512  1.00 23.80           H
ATOM   1569  HB3 TYR A 108       9.343  10.546  17.794  1.00 23.80           H
ATOM   1570  HD1 TYR A 108      11.507  13.295  16.978  1.00 24.41           H
ATOM   1571  HD2 TYR A 108       8.469  12.068  19.265  1.00 28.50           H
ATOM   1572  HE1 TYR A 108      11.368  15.380  17.912  1.00 23.92           H
ATOM   1573  HE2 TYR A 108       8.337  14.172  20.218  1.00 28.74           H
ATOM   1574  HH  TYR A 108       8.936  16.439  19.801  1.00 30.40           H
ATOM   1575  N   ARG A 109      10.779   8.024  18.577  1.00 21.36           N
ANISOU 1575  N   ARG A 109     3108   2505   2503   -402    139    472       N
ATOM   1576  CA  ARG A 109      10.193   6.694  18.405  1.00 21.99           C
ANISOU 1576  CA  ARG A 109     3253   2415   2688   -413     85    603       C
ATOM   1577  C   ARG A 109       8.868   6.862  17.677  1.00 20.69           C
ANISOU 1577  C   ARG A 109     3135   2185   2540   -414    167    401       C
ATOM   1578  O   ARG A 109       8.040   7.700  18.050  1.00 22.34           O
ANISOU 1578  O   ARG A 109     3285   2550   2654   -516    243    253       O
ATOM   1579  CB  ARG A 109      10.008   6.074  19.795  1.00 24.20           C
ANISOU 1579  CB  ARG A 109     3495   2879   2821   -664     -9    847       C
ATOM   1580  CG  ARG A 109       9.353   4.744  19.783  1.00 29.45           C
ANISOU 1580  CG  ARG A 109     4213   3372   3605   -718    -78   1017       C
ATOM   1581  CD  ARG A 109       9.258   4.206  21.192  1.00 30.17           C
ANISOU 1581  CD  ARG A 109     4251   3694   3517  -1019   -205   1325       C
ATOM   1582  NE  ARG A 109       8.716   2.855  21.194  1.00 36.65           N
ANISOU 1582  NE  ARG A 109     5109   4309   4508  -1066   -296   1532       N
ATOM   1583  CZ  ARG A 109       7.792   2.430  22.039  1.00 39.66           C
ANISOU 1583  CZ  ARG A 109     5469   4887   4713  -1301   -325   1583       C
ATOM   1584  NH1 ARG A 109       7.286   3.227  22.968  1.00 40.63           N
ANISOU 1584  NH1 ARG A 109     5542   5412   4482  -1558   -259   1455       N
ATOM   1585  NH2 ARG A 109       7.369   1.171  21.957  1.00 47.86           N
ANISOU 1585  NH2 ARG A 109     6522   5713   5950  -1287   -403   1722       N
ATOM   1586  H   ARG A 109      10.907   8.245  19.398  1.00 25.65           H
ATOM   1587  HA  ARG A 109      10.755   6.096  17.888  1.00 26.40           H
ATOM   1588  HB2 ARG A 109      10.879   5.969  20.207  1.00 29.05           H
ATOM   1589  HB3 ARG A 109       9.458   6.668  20.329  1.00 29.05           H
ATOM   1590  HG2 ARG A 109       8.457   4.823  19.419  1.00 35.35           H
ATOM   1591  HG3 ARG A 109       9.875   4.126  19.248  1.00 35.35           H
ATOM   1592  HD2 ARG A 109      10.143   4.183  21.589  1.00 36.21           H
ATOM   1593  HD3 ARG A 109       8.673   4.774  21.716  1.00 36.21           H
ATOM   1594  HE  ARG A 109       9.014   2.299  20.610  1.00 44.00           H
ATOM   1595 HH11 ARG A 109       7.557   4.041  23.030  1.00 48.76           H
ATOM   1596 HH12 ARG A 109       6.685   2.931  23.508  1.00 48.76           H
ATOM   1597 HH21 ARG A 109       7.696   0.646  21.360  1.00 57.44           H
ATOM   1598 HH22 ARG A 109       6.769   0.883  22.501  1.00 57.44           H
ATOM   1599  N  ATHR A 110       8.677   6.088  16.603  0.64 21.96           N
ANISOU 1599  N  ATHR A 110     3377   2115   2850   -316    164    376       N
ATOM   1600  CA ATHR A 110       7.530   6.241  15.728  0.64 21.27           C
ANISOU 1600  CA ATHR A 110     3324   1988   2771   -338    205    224       C
ATOM   1601  C  ATHR A 110       6.947   4.879  15.382  0.64 26.01           C
ANISOU 1601  C  ATHR A 110     4014   2412   3456   -396    184    270       C
ATOM   1602  O  ATHR A 110       7.668   3.882  15.299  0.64 28.50           O
ANISOU 1602  O  ATHR A 110     4371   2534   3923   -342    168    357       O
ATOM   1603  CB ATHR A 110       7.964   6.915  14.408  0.64 23.62           C
ANISOU 1603  CB ATHR A 110     3635   2233   3106   -222    231     94       C
ATOM   1604  OG1ATHR A 110       8.641   8.142  14.708  0.64 23.15           O
ANISOU 1604  OG1ATHR A 110     3492   2293   3011   -162    245     67       O
ATOM   1605  CG2ATHR A 110       6.774   7.204  13.508  0.64 22.30           C
ANISOU 1605  CG2ATHR A 110     3463   2078   2930   -295    220     11       C
ATOM   1606  H  ATHR A 110       9.213   5.459  16.363  0.64 26.36           H
ATOM   1607  HA ATHR A 110       6.848   6.762  16.181  0.64 25.54           H
ATOM   1608  HB ATHR A 110       8.554   6.316  13.925  0.64 28.35           H
ATOM   1609  HG1ATHR A 110       8.906   8.506  13.999  0.64 27.79           H
ATOM   1610 HG21ATHR A 110       7.048   7.766  12.766  0.64 26.77           H
ATOM   1611 HG22ATHR A 110       6.413   6.375  13.159  0.64 26.77           H
ATOM   1612 HG23ATHR A 110       6.081   7.662  14.011  0.64 26.77           H
ATOM   1613  N  BTHR A 110       8.682   6.089  16.603  0.36 22.04           N
ANISOU 1613  N  BTHR A 110     3387   2125   2860   -315    164    377       N
ATOM   1614  CA BTHR A 110       7.542   6.239  15.717  0.36 21.43           C
ANISOU 1614  CA BTHR A 110     3345   2006   2792   -336    205    223       C
ATOM   1615  C  BTHR A 110       6.947   4.876  15.388  0.36 25.98           C
ANISOU 1615  C  BTHR A 110     4011   2409   3453   -397    184    271       C
ATOM   1616  O  BTHR A 110       7.660   3.871  15.328  0.36 28.49           O
ANISOU 1616  O  BTHR A 110     4370   2534   3921   -345    166    361       O
ATOM   1617  CB BTHR A 110       7.974   6.892  14.383  0.36 23.53           C
ANISOU 1617  CB BTHR A 110     3626   2218   3097   -221    231     94       C
ATOM   1618  OG1BTHR A 110       8.926   6.047  13.724  0.36 33.87           O
ANISOU 1618  OG1BTHR A 110     5002   3357   4508   -136    253     88       O
ATOM   1619  CG2BTHR A 110       8.602   8.253  14.628  0.36 22.79           C
ANISOU 1619  CG2BTHR A 110     3441   2251   2966   -160    246     56       C
ATOM   1620  H  BTHR A 110       9.218   5.460  16.368  0.36 26.45           H
ATOM   1621  HA BTHR A 110       6.868   6.778  16.159  0.36 25.73           H
ATOM   1622  HB BTHR A 110       7.195   7.013  13.818  0.36 28.25           H
ATOM   1623  HG1BTHR A 110       9.251   6.445  13.059  0.36 40.65           H
ATOM   1624 HG21BTHR A 110       9.427   8.333  14.124  0.36 27.36           H
ATOM   1625 HG22BTHR A 110       7.993   8.955  14.349  0.36 27.36           H
ATOM   1626 HG23BTHR A 110       8.798   8.363  15.572  0.36 27.36           H
ATOM   1627  N   LYS A 111       5.632   4.848  15.174  1.00 20.86           N
ANISOU 1627  N   LYS A 111     3365   1803   2759   -510    190    207       N
ATOM   1628  CA  LYS A 111       4.960   3.654  14.665  1.00 21.08           C
ANISOU 1628  CA  LYS A 111     3484   1671   2854   -597    180    207       C
ATOM   1629  C   LYS A 111       3.849   4.090  13.716  1.00 21.56           C
ANISOU 1629  C   LYS A 111     3530   1802   2859   -675    178     84       C
ATOM   1630  O   LYS A 111       3.406   5.239  13.723  1.00 22.41           O
ANISOU 1630  O   LYS A 111     3521   2059   2936   -665    171     53       O
ATOM   1631  CB  LYS A 111       4.364   2.779  15.769  1.00 25.09           C
ANISOU 1631  CB  LYS A 111     3994   2186   3355   -746    138    372       C
ATOM   1632  CG  LYS A 111       3.181   3.392  16.486  1.00 25.16           C
ANISOU 1632  CG  LYS A 111     3905   2436   3217   -895    159    347       C
ATOM   1633  CD  LYS A 111       2.631   2.452  17.546  1.00 27.59           C
ANISOU 1633  CD  LYS A 111     4221   2792   3469  -1100    121    522       C
ATOM   1634  CE  LYS A 111       1.472   3.073  18.319  1.00 27.98           C
ANISOU 1634  CE  LYS A 111     4145   3119   3368  -1281    194    439       C
ATOM   1635  NZ  LYS A 111       0.845   2.152  19.305  1.00 30.02           N
ANISOU 1635  NZ  LYS A 111     4410   3478   3519  -1543    163    609       N
ATOM   1636  H   LYS A 111       5.102   5.510  15.320  1.00 25.05           H
ATOM   1637  HA  LYS A 111       5.612   3.117  14.188  1.00 25.31           H
ATOM   1638  HB2 LYS A 111       4.067   1.944  15.375  1.00 30.12           H
ATOM   1639  HB3 LYS A 111       5.051   2.607  16.432  1.00 30.12           H
ATOM   1640  HG2 LYS A 111       3.458   4.214  16.920  1.00 30.20           H
ATOM   1641  HG3 LYS A 111       2.476   3.575  15.845  1.00 30.20           H
ATOM   1642  HD2 LYS A 111       2.311   1.642  17.119  1.00 33.12           H
ATOM   1643  HD3 LYS A 111       3.335   2.238  18.178  1.00 33.12           H
ATOM   1644  HE2 LYS A 111       1.798   3.846  18.804  1.00 33.59           H
ATOM   1645  HE3 LYS A 111       0.785   3.342  17.689  1.00 33.59           H
ATOM   1646  HZ1 LYS A 111       1.471   1.665  19.708  1.00 36.04           H
ATOM   1647  HZ2 LYS A 111       0.403   2.620  19.920  1.00 36.04           H
ATOM   1648  HZ3 LYS A 111       0.276   1.606  18.893  1.00 36.04           H
ATOM   1649  N   VAL A 112       3.400   3.163  12.881  1.00 23.64           N
ANISOU 1649  N   VAL A 112     3890   1944   3148   -774    179     24       N
ATOM   1650  CA  VAL A 112       2.187   3.355  12.090  1.00 24.14           C
ANISOU 1650  CA  VAL A 112     3926   2108   3140   -922    135    -26       C
ATOM   1651  C   VAL A 112       1.175   2.338  12.592  1.00 21.39           C
ANISOU 1651  C   VAL A 112     3608   1711   2809  -1078    124     25       C
ATOM   1652  O   VAL A 112       1.466   1.140  12.613  1.00 25.19           O
ANISOU 1652  O   VAL A 112     4206   1989   3374  -1118    156     18       O
ATOM   1653  CB  VAL A 112       2.450   3.164  10.592  1.00 25.65           C
ANISOU 1653  CB  VAL A 112     4206   2276   3264  -1006    147   -161       C
ATOM   1654  CG1 VAL A 112       1.163   3.380   9.814  1.00 27.26           C
ANISOU 1654  CG1 VAL A 112     4355   2637   3366  -1215     49   -139       C
ATOM   1655  CG2 VAL A 112       3.555   4.105  10.109  1.00 29.21           C
ANISOU 1655  CG2 VAL A 112     4631   2787   3682   -879    163   -196       C
ATOM   1656  H   VAL A 112       3.783   2.404  12.752  1.00 28.38           H
ATOM   1657  HA  VAL A 112       1.842   4.252  12.223  1.00 28.99           H
ATOM   1658  HB  VAL A 112       2.756   2.257  10.432  1.00 30.79           H
ATOM   1659 HG11 VAL A 112       1.339   3.250   8.869  1.00 32.73           H
ATOM   1660 HG12 VAL A 112       0.499   2.741  10.118  1.00 32.73           H
ATOM   1661 HG13 VAL A 112       0.847   4.284   9.971  1.00 32.73           H
ATOM   1662 HG21 VAL A 112       3.659   4.004   9.150  1.00 35.07           H
ATOM   1663 HG22 VAL A 112       3.306   5.019  10.321  1.00 35.07           H
ATOM   1664 HG23 VAL A 112       4.383   3.876  10.558  1.00 35.07           H
ATOM   1665  N   GLU A 113      -0.006   2.793  13.012  1.00 23.89           N
ANISOU 1665  N   GLU A 113     3794   2187   3095  -1168     89     74       N
ATOM   1666  CA  GLU A 113      -1.045   1.909  13.538  1.00 24.67           C
ANISOU 1666  CA  GLU A 113     3900   2284   3190  -1343     80    128       C
ATOM   1667  C   GLU A 113      -2.342   2.244  12.828  1.00 25.09           C
ANISOU 1667  C   GLU A 113     3838   2466   3227  -1481     19    111       C
ATOM   1668  O   GLU A 113      -2.795   3.398  12.882  1.00 25.18           O
ANISOU 1668  O   GLU A 113     3649   2617   3302  -1428      0    125       O
ATOM   1669  CB  GLU A 113      -1.237   2.081  15.054  1.00 24.35           C
ANISOU 1669  CB  GLU A 113     3764   2366   3124  -1369    123    216       C
ATOM   1670  CG  GLU A 113      -2.445   1.295  15.567  1.00 29.18           C
ANISOU 1670  CG  GLU A 113     4352   3033   3704  -1592    117    276       C
ATOM   1671  CD  GLU A 113      -2.721   1.506  17.033  1.00 43.14           C
ANISOU 1671  CD  GLU A 113     6010   5003   5380  -1703    182    333       C
ATOM   1672  OE1 GLU A 113      -1.776   1.366  17.814  1.00 36.32           O
ANISOU 1672  OE1 GLU A 113     5200   4144   4456  -1684    179    436       O
ATOM   1673  OE2 GLU A 113      -3.874   1.815  17.399  1.00 53.79           O
ANISOU 1673  OE2 GLU A 113     7199   6528   6713  -1839    241    271       O
ATOM   1674  H   GLU A 113      -0.232   3.623  13.001  1.00 28.68           H
ATOM   1675  HA  GLU A 113      -0.795   0.989  13.363  1.00 29.62           H
ATOM   1676  HB2 GLU A 113      -0.446   1.758  15.515  1.00 29.24           H
ATOM   1677  HB3 GLU A 113      -1.377   3.020  15.254  1.00 29.24           H
ATOM   1678  HG2 GLU A 113      -3.233   1.574  15.074  1.00 35.03           H
ATOM   1679  HG3 GLU A 113      -2.285   0.348  15.428  1.00 35.03           H
ATOM   1680  N   ASN A 114      -2.901   1.262  12.122  1.00 26.82           N
ANISOU 1680  N   ASN A 114     4148   2637   3406  -1633    -17     82       N
ATOM   1681  CA  ASN A 114      -4.121   1.466  11.345  1.00 29.39           C
ANISOU 1681  CA  ASN A 114     4353   3117   3696  -1785   -110    104       C
ATOM   1682  C   ASN A 114      -4.000   2.678  10.428  1.00 27.78           C
ANISOU 1682  C   ASN A 114     4036   3026   3493  -1779   -206    146       C
ATOM   1683  O   ASN A 114      -4.917   3.490  10.307  1.00 30.57           O
ANISOU 1683  O   ASN A 114     4153   3511   3950  -1821   -303    262       O
ATOM   1684  CB  ASN A 114      -5.341   1.529  12.245  1.00 31.04           C
ANISOU 1684  CB  ASN A 114     4385   3437   3972  -1858   -107    178       C
ATOM   1685  CG  ASN A 114      -5.478   0.289  13.108  1.00 30.21           C
ANISOU 1685  CG  ASN A 114     4391   3251   3835  -1910    -47    188       C
ATOM   1686  OD1 ASN A 114      -5.066  -0.809  12.717  1.00 31.00           O
ANISOU 1686  OD1 ASN A 114     4667   3193   3919  -1930    -41    149       O
ATOM   1687  ND2 ASN A 114      -6.076   0.455  14.278  1.00 34.59           N
ANISOU 1687  ND2 ASN A 114     4817   3919   4408  -1956      7    236       N
ATOM   1688  H   ASN A 114      -2.589   0.462  12.078  1.00 32.20           H
ATOM   1689  HA  ASN A 114      -4.248   0.702  10.762  1.00 35.28           H
ATOM   1690  HB2 ASN A 114      -5.266   2.299  12.831  1.00 37.26           H
ATOM   1691  HB3 ASN A 114      -6.138   1.607  11.697  1.00 37.26           H
ATOM   1692 HD21 ASN A 114      -6.180  -0.215  14.807  1.00 41.52           H
ATOM   1693 HD22 ASN A 114      -6.361   1.233  14.509  1.00 41.52           H
ATOM   1694  N  AASN A 115      -2.849   2.795   9.784  0.62 25.69           N
ANISOU 1694  N  AASN A 115     3907   2701   3152  -1723   -184     72       N
ATOM   1695  CA AASN A 115      -2.543   3.814   8.787  0.62 25.65           C
ANISOU 1695  CA AASN A 115     3820   2825   3100  -1727   -286    133       C
ATOM   1696  C  AASN A 115      -2.349   5.209   9.357  0.62 26.91           C
ANISOU 1696  C  AASN A 115     3769   3007   3447  -1500   -308    239       C
ATOM   1697  O  AASN A 115      -2.218   6.172   8.582  0.62 26.42           O
ANISOU 1697  O  AASN A 115     3592   3035   3412  -1508   -427    357       O
ATOM   1698  CB AASN A 115      -3.607   3.876   7.685  0.62 29.95           C
ANISOU 1698  CB AASN A 115     4262   3574   3544  -1976   -456    250       C
ATOM   1699  CG AASN A 115      -3.057   4.426   6.388  0.62 30.65           C
ANISOU 1699  CG AASN A 115     4369   3822   3453  -2096   -555    298       C
ATOM   1700  OD1AASN A 115      -1.911   4.165   6.024  0.62 30.34           O
ANISOU 1700  OD1AASN A 115     4513   3734   3281  -2093   -441    125       O
ATOM   1701  ND2AASN A 115      -3.857   5.219   5.705  0.62 38.10           N
ANISOU 1701  ND2AASN A 115     5101   4962   4413  -2196   -765    551       N
ATOM   1702  H  AASN A 115      -2.187   2.263   9.917  0.62 30.84           H
ATOM   1703  HA AASN A 115      -1.697   3.557   8.389  0.62 30.79           H
ATOM   1704  HB2AASN A 115      -3.942   2.981   7.516  0.62 35.95           H
ATOM   1705  HB3AASN A 115      -4.332   4.452   7.974  0.62 35.95           H
ATOM   1706 HD21AASN A 115      -4.643   5.398   6.004  0.62 45.73           H
ATOM   1707 HD22AASN A 115      -3.592   5.559   4.961  0.62 45.73           H
ATOM   1708  N  BASN A 115      -2.846   2.793   9.777  0.38 25.80           N
ANISOU 1708  N  BASN A 115     3922   2716   3165  -1724   -184     72       N
ATOM   1709  CA BASN A 115      -2.524   3.813   8.783  0.38 25.73           C
ANISOU 1709  CA BASN A 115     3834   2835   3109  -1726   -285    131       C
ATOM   1710  C  BASN A 115      -2.319   5.208   9.355  0.38 26.90           C
ANISOU 1710  C  BASN A 115     3771   3004   3444  -1497   -306    236       C
ATOM   1711  O  BASN A 115      -2.158   6.165   8.584  0.38 26.56           O
ANISOU 1711  O  BASN A 115     3619   3049   3424  -1503   -422    351       O
ATOM   1712  CB BASN A 115      -3.563   3.885   7.656  0.38 29.94           C
ANISOU 1712  CB BASN A 115     4265   3573   3538  -1976   -455    247       C
ATOM   1713  CG BASN A 115      -3.580   2.640   6.799  0.38 33.96           C
ANISOU 1713  CG BASN A 115     4978   4117   3810  -2171   -398     83       C
ATOM   1714  OD1BASN A 115      -2.560   1.976   6.629  0.38 44.70           O
ANISOU 1714  OD1BASN A 115     6532   5349   5104  -2140   -244   -125       O
ATOM   1715  ND2BASN A 115      -4.739   2.323   6.251  0.38 36.06           N
ANISOU 1715  ND2BASN A 115     5174   4544   3982  -2368   -505    167       N
ATOM   1716  H  BASN A 115      -2.189   2.252   9.904  0.38 30.97           H
ATOM   1717  HA BASN A 115      -1.675   3.545   8.397  0.38 30.89           H
ATOM   1718  HB2BASN A 115      -4.445   3.993   8.046  0.38 35.94           H
ATOM   1719  HB3BASN A 115      -3.357   4.640   7.084  0.38 35.94           H
ATOM   1720 HD21BASN A 115      -5.430   2.815   6.391  0.38 43.28           H
ATOM   1721 HD22BASN A 115      -4.803   1.624   5.754  0.38 43.28           H
ATOM   1722  N   THR A 116      -2.304   5.358  10.674  1.00 24.30           N
ANISOU 1722  N   THR A 116     3378   2607   3246  -1336   -193    198       N
ATOM   1723  CA  THR A 116      -2.015   6.637  11.307  1.00 22.48           C
ANISOU 1723  CA  THR A 116     2961   2377   3202  -1146   -153    210       C
ATOM   1724  C   THR A 116      -0.580   6.626  11.814  1.00 22.23           C
ANISOU 1724  C   THR A 116     3086   2274   3086   -988    -47    119       C
ATOM   1725  O   THR A 116      -0.130   5.620  12.384  1.00 22.54           O
ANISOU 1725  O   THR A 116     3293   2249   3021   -996     27     70       O
ATOM   1726  CB  THR A 116      -2.989   6.885  12.454  1.00 26.30           C
ANISOU 1726  CB  THR A 116     3238   2893   3861  -1144    -61    172       C
ATOM   1727  OG1 THR A 116      -4.309   7.042  11.918  1.00 36.43           O
ANISOU 1727  OG1 THR A 116     4309   4233   5299  -1267   -173    282       O
ATOM   1728  CG2 THR A 116      -2.607   8.118  13.241  1.00 25.69           C
ANISOU 1728  CG2 THR A 116     2981   2798   3982   -981     52     85       C
ATOM   1729  H   THR A 116      -2.441   4.721  11.236  1.00 29.17           H
ATOM   1730  HA  THR A 116      -2.107   7.365  10.673  1.00 26.99           H
ATOM   1731  HB  THR A 116      -2.969   6.132  13.066  1.00 31.57           H
ATOM   1732  HG1 THR A 116      -4.854   7.195  12.538  1.00 43.73           H
ATOM   1733 HG21 THR A 116      -3.351   8.401  13.795  1.00 30.84           H
ATOM   1734 HG22 THR A 116      -1.846   7.926  13.810  1.00 30.84           H
ATOM   1735 HG23 THR A 116      -2.374   8.839  12.635  1.00 30.84           H
ATOM   1736  N   VAL A 117       0.132   7.734  11.589  1.00 20.65           N
ANISOU 1736  N   VAL A 117     2809   2073   2964   -859    -61    134       N
ATOM   1737  CA  VAL A 117       1.487   7.907  12.112  1.00 19.66           C
ANISOU 1737  CA  VAL A 117     2784   1905   2781   -713     29     63       C
ATOM   1738  C   VAL A 117       1.386   8.391  13.555  1.00 19.24           C
ANISOU 1738  C   VAL A 117     2610   1886   2812   -660    150    -12       C
ATOM   1739  O   VAL A 117       0.756   9.429  13.821  1.00 20.68           O
ANISOU 1739  O   VAL A 117     2566   2085   3206   -639    183    -51       O
ATOM   1740  CB  VAL A 117       2.280   8.910  11.254  1.00 19.34           C
ANISOU 1740  CB  VAL A 117     2709   1871   2770   -637    -35    108       C
ATOM   1741  CG1 VAL A 117       3.664   9.112  11.777  1.00 22.72           C
ANISOU 1741  CG1 VAL A 117     3219   2270   3145   -497     53     39       C
ATOM   1742  CG2 VAL A 117       2.320   8.447   9.800  1.00 23.61           C
ANISOU 1742  CG2 VAL A 117     3359   2461   3151   -786   -138    158       C
ATOM   1743  H   VAL A 117      -0.151   8.406  11.133  1.00 24.79           H
ATOM   1744  HA  VAL A 117       1.952   7.056  12.093  1.00 23.61           H
ATOM   1745  HB  VAL A 117       1.827   9.766  11.298  1.00 23.23           H
ATOM   1746 HG11 VAL A 117       4.171   9.633  11.134  1.00 27.28           H
ATOM   1747 HG12 VAL A 117       3.616   9.585  12.622  1.00 27.28           H
ATOM   1748 HG13 VAL A 117       4.083   8.247  11.905  1.00 27.28           H
ATOM   1749 HG21 VAL A 117       2.878   9.054   9.290  1.00 28.34           H
ATOM   1750 HG22 VAL A 117       2.688   7.550   9.764  1.00 28.34           H
ATOM   1751 HG23 VAL A 117       1.418   8.448   9.443  1.00 28.34           H
ATOM   1752  N   PHE A 118       2.028   7.669  14.474  1.00 20.46           N
ANISOU 1752  N   PHE A 118     2891   2055   2829   -667    220    -32       N
ATOM   1753  CA  PHE A 118       2.086   8.033  15.887  1.00 19.59           C
ANISOU 1753  CA  PHE A 118     2694   2062   2688   -709    336   -105       C
ATOM   1754  C   PHE A 118       3.539   8.257  16.284  1.00 19.99           C
ANISOU 1754  C   PHE A 118     2821   2129   2645   -624    349    -90       C
ATOM   1755  O   PHE A 118       4.423   7.462  15.942  1.00 21.86           O
ANISOU 1755  O   PHE A 118     3208   2278   2821   -567    284     13       O
ATOM   1756  CB  PHE A 118       1.515   6.910  16.774  1.00 20.86           C
ANISOU 1756  CB  PHE A 118     2912   2298   2716   -886    358    -52       C
ATOM   1757  CG  PHE A 118       0.019   6.768  16.704  1.00 20.79           C
ANISOU 1757  CG  PHE A 118     2786   2326   2788  -1007    380    -91       C
ATOM   1758  CD1 PHE A 118      -0.804   7.513  17.523  1.00 21.90           C
ANISOU 1758  CD1 PHE A 118     2706   2603   3012  -1099    524   -246       C
ATOM   1759  CD2 PHE A 118      -0.562   5.896  15.799  1.00 22.83           C
ANISOU 1759  CD2 PHE A 118     3133   2485   3055  -1050    276     -4       C
ATOM   1760  CE1 PHE A 118      -2.163   7.388  17.456  1.00 24.30           C
ANISOU 1760  CE1 PHE A 118     2861   2937   3435  -1202    552   -282       C
ATOM   1761  CE2 PHE A 118      -1.927   5.781  15.724  1.00 24.34           C
ANISOU 1761  CE2 PHE A 118     3195   2729   3323  -1173    278    -18       C
ATOM   1762  CZ  PHE A 118      -2.733   6.528  16.544  1.00 27.57           C
ANISOU 1762  CZ  PHE A 118     3364   3265   3846  -1234    409   -141       C
ATOM   1763  H   PHE A 118       2.451   6.942  14.296  1.00 24.57           H
ATOM   1764  HA  PHE A 118       1.575   8.845  16.030  1.00 23.52           H
ATOM   1765  HB2 PHE A 118       1.903   6.066  16.495  1.00 25.04           H
ATOM   1766  HB3 PHE A 118       1.749   7.094  17.697  1.00 25.04           H
ATOM   1767  HD1 PHE A 118      -0.429   8.110  18.130  1.00 26.29           H
ATOM   1768  HD2 PHE A 118      -0.024   5.385  15.238  1.00 27.40           H
ATOM   1769  HE1 PHE A 118      -2.703   7.885  18.027  1.00 29.17           H
ATOM   1770  HE2 PHE A 118      -2.308   5.193  15.113  1.00 29.22           H
ATOM   1771  HZ  PHE A 118      -3.659   6.455  16.485  1.00 33.10           H
ATOM   1772  N   VAL A 119       3.783   9.309  17.061  1.00 19.36           N
ANISOU 1772  N   VAL A 119     2616   2157   2584   -635    450   -212       N
ATOM   1773  CA  VAL A 119       5.112   9.577  17.605  1.00 19.07           C
ANISOU 1773  CA  VAL A 119     2626   2189   2429   -606    459   -195       C
ATOM   1774  C   VAL A 119       5.055   9.559  19.123  1.00 19.60           C
ANISOU 1774  C   VAL A 119     2641   2497   2308   -831    557   -250       C
ATOM   1775  O   VAL A 119       4.109  10.079  19.728  1.00 22.94           O
ANISOU 1775  O   VAL A 119     2921   3032   2763   -971    704   -446       O
ATOM   1776  CB  VAL A 119       5.714  10.897  17.097  1.00 21.70           C
ANISOU 1776  CB  VAL A 119     2877   2465   2904   -472    484   -292       C
ATOM   1777  CG1 VAL A 119       5.869  10.850  15.588  1.00 26.87           C
ANISOU 1777  CG1 VAL A 119     3592   2958   3658   -330    367   -195       C
ATOM   1778  CG2 VAL A 119       4.858  12.036  17.463  1.00 25.44           C
ANISOU 1778  CG2 VAL A 119     3139   2949   3579   -519    619   -498       C
ATOM   1779  H   VAL A 119       3.189   9.888  17.288  1.00 23.25           H
ATOM   1780  HA  VAL A 119       5.697   8.858  17.318  1.00 22.89           H
ATOM   1781  HB  VAL A 119       6.584  11.018  17.508  1.00 26.05           H
ATOM   1782 HG11 VAL A 119       6.184  11.712  15.275  1.00 32.25           H
ATOM   1783 HG12 VAL A 119       6.511  10.160  15.358  1.00 32.25           H
ATOM   1784 HG13 VAL A 119       5.009  10.647  15.188  1.00 32.25           H
ATOM   1785 HG21 VAL A 119       5.207  12.840  17.048  1.00 30.54           H
ATOM   1786 HG22 VAL A 119       3.956  11.867  17.150  1.00 30.54           H
ATOM   1787 HG23 VAL A 119       4.860  12.135  18.428  1.00 30.54           H
ATOM   1788  N   ASP A 120       6.060   8.951  19.721  1.00 22.75           N
ANISOU 1788  N   ASP A 120     3130   2990   2523   -894    476    -72       N
ATOM   1789  CA  ASP A 120       6.147   8.834  21.177  1.00 21.96           C
ANISOU 1789  CA  ASP A 120     2990   3195   2159  -1192    518    -46       C
ATOM   1790  C   ASP A 120       7.076   9.929  21.673  1.00 24.70           C
ANISOU 1790  C   ASP A 120     3270   3696   2418  -1236    590   -180       C
ATOM   1791  O   ASP A 120       8.304   9.783  21.641  1.00 25.57           O
ANISOU 1791  O   ASP A 120     3432   3805   2480  -1167    466      7       O
ATOM   1792  CB  ASP A 120       6.683   7.467  21.568  1.00 26.67           C
ANISOU 1792  CB  ASP A 120     3688   3805   2642  -1277    330    322       C
ATOM   1793  CG  ASP A 120       6.916   7.331  23.069  1.00 29.90           C
ANISOU 1793  CG  ASP A 120     4048   4593   2720  -1653    310    451       C
ATOM   1794  OD1 ASP A 120       6.555   8.260  23.815  1.00 31.93           O
ANISOU 1794  OD1 ASP A 120     4207   5106   2821  -1840    470    157       O
ATOM   1795  OD2 ASP A 120       7.458   6.289  23.471  1.00 34.21           O
ANISOU 1795  OD2 ASP A 120     4629   5142   3229  -1720    104    817       O
ATOM   1796  H   ASP A 120       6.719   8.589  19.303  1.00 27.31           H
ATOM   1797  HA  ASP A 120       5.267   8.957  21.564  1.00 26.37           H
ATOM   1798  HB2 ASP A 120       6.043   6.789  21.301  1.00 32.02           H
ATOM   1799  HB3 ASP A 120       7.530   7.319  21.119  1.00 32.02           H
ATOM   1800  N   TYR A 121       6.495  11.037  22.122  1.00 28.39           N
ANISOU 1800  N   TYR A 121     3599   4277   2911  -1357    807   -524       N
ATOM   1801  CA  TYR A 121       7.330  12.176  22.499  1.00 30.78           C
ANISOU 1801  CA  TYR A 121     3834   4684   3179  -1405    905   -712       C
ATOM   1802  C   TYR A 121       8.086  11.960  23.806  1.00 33.81           C
ANISOU 1802  C   TYR A 121     4239   5405   3201  -1700    821   -620       C
ATOM   1803  O   TYR A 121       8.914  12.804  24.167  1.00 35.33           O
ANISOU 1803  O   TYR A 121     4394   5680   3351  -1748    833   -740       O
ATOM   1804  CB  TYR A 121       6.494  13.459  22.589  1.00 39.08           C
ANISOU 1804  CB  TYR A 121     4710   5649   4491  -1406   1132  -1133       C
ATOM   1805  CG  TYR A 121       5.517  13.474  23.725  1.00 34.43           C
ANISOU 1805  CG  TYR A 121     4059   5228   3794  -1659   1215  -1358       C
ATOM   1806  CD1 TYR A 121       4.249  12.956  23.580  1.00 39.72           C
ANISOU 1806  CD1 TYR A 121     4686   5848   4557  -1656   1265  -1383       C
ATOM   1807  CD2 TYR A 121       5.868  14.031  24.942  1.00 40.91           C
ANISOU 1807  CD2 TYR A 121     4853   6270   4420  -1938   1250  -1567       C
ATOM   1808  CE1 TYR A 121       3.352  12.975  24.622  1.00 42.90           C
ANISOU 1808  CE1 TYR A 121     5034   6419   4848  -1898   1361  -1614       C
ATOM   1809  CE2 TYR A 121       4.986  14.046  25.986  1.00 40.49           C
ANISOU 1809  CE2 TYR A 121     4742   6392   4249  -2220   1345  -1814       C
ATOM   1810  CZ  TYR A 121       3.734  13.527  25.824  1.00 36.60           C
ANISOU 1810  CZ  TYR A 121     4220   5846   3843  -2187   1407  -1843       C
ATOM   1811  OH  TYR A 121       2.863  13.572  26.902  1.00 45.58           O
ANISOU 1811  OH  TYR A 121     5293   7177   4847  -2492   1520  -2123       O
ATOM   1812  H   TYR A 121       5.648  11.153  22.215  1.00 34.08           H
ATOM   1813  HA  TYR A 121       7.986  12.305  21.797  1.00 36.95           H
ATOM   1814  HB2 TYR A 121       7.094  14.212  22.706  1.00 46.91           H
ATOM   1815  HB3 TYR A 121       5.991  13.561  21.766  1.00 46.91           H
ATOM   1816  HD1 TYR A 121       3.995  12.588  22.764  1.00 47.68           H
ATOM   1817  HD2 TYR A 121       6.715  14.399  25.051  1.00 49.10           H
ATOM   1818  HE1 TYR A 121       2.500  12.619  24.516  1.00 51.49           H
ATOM   1819  HE2 TYR A 121       5.239  14.410  26.804  1.00 48.60           H
ATOM   1820  HH  TYR A 121       3.252  13.894  27.573  1.00 54.70           H
ATOM   1821  N   ALA A 122       7.850  10.859  24.502  1.00 29.20           N
ANISOU 1821  N   ALA A 122     3704   4989   2403  -1887    679   -385       N
ATOM   1822  CA  ALA A 122       8.584  10.545  25.727  1.00 34.18           C
ANISOU 1822  CA  ALA A 122     4322   5925   2741  -2166    504   -221       C
ATOM   1823  C   ALA A 122       9.808   9.670  25.459  1.00 35.90           C
ANISOU 1823  C   ALA A 122     4592   6090   2957  -2058    250    258       C
ATOM   1824  O   ALA A 122      10.507   9.295  26.400  1.00 37.28           O
ANISOU 1824  O   ALA A 122     4713   6495   2958  -2272     54    478       O
ATOM   1825  CB  ALA A 122       7.654   9.886  26.759  1.00 38.64           C
ANISOU 1825  CB  ALA A 122     4864   6718   3101  -2469    461   -225       C
ATOM   1826  H   ALA A 122       7.263  10.268  24.287  1.00 35.05           H
ATOM   1827  HA  ALA A 122       8.899  11.369  26.130  1.00 41.03           H
ATOM   1828  HB1 ALA A 122       8.122   9.815  27.606  1.00 46.39           H
ATOM   1829  HB2 ALA A 122       6.861  10.435  26.864  1.00 46.39           H
ATOM   1830  HB3 ALA A 122       7.406   9.004  26.443  1.00 46.39           H
ATOM   1831  N   ALA A 123      10.102   9.361  24.187  1.00 30.33           N
ANISOU 1831  N   ALA A 123     3968   5075   2482  -1746    242    418       N
ATOM   1832  CA  ALA A 123      11.192   8.469  23.802  1.00 39.74           C
ANISOU 1832  CA  ALA A 123     5192   6110   3797  -1588     13    846       C
ATOM   1833  C   ALA A 123      11.978   9.092  22.638  1.00 27.31           C
ANISOU 1833  C   ALA A 123     3634   4267   2474  -1226     50    726       C
ATOM   1834  O   ALA A 123      11.953   8.608  21.492  1.00 30.07           O
ANISOU 1834  O   ALA A 123     4043   4272   3108   -919     29    745       O
ATOM   1835  CB  ALA A 123      10.638   7.109  23.372  1.00 37.17           C
ANISOU 1835  CB  ALA A 123     4935   5528   3660  -1490    -98   1102       C
ATOM   1836  H   ALA A 123       9.667   9.670  23.513  1.00 36.41           H
ATOM   1837  HA  ALA A 123      11.786   8.371  24.562  1.00 47.70           H
ATOM   1838  HB1 ALA A 123      11.284   6.421  23.592  1.00 44.61           H
ATOM   1839  HB2 ALA A 123       9.805   6.945  23.842  1.00 44.61           H
ATOM   1840  HB3 ALA A 123      10.480   7.121  22.415  1.00 44.61           H
ATOM   1841  N   ILE A 124      12.642  10.207  22.902  1.00 28.12           N
ANISOU 1841  N   ILE A 124     3681   4540   2463  -1288    122    559       N
ATOM   1842  CA  ILE A 124      13.442  10.899  21.898  1.00 24.99           C
ANISOU 1842  CA  ILE A 124     3285   3936   2274   -993    148    451       C
ATOM   1843  C   ILE A 124      14.897  10.532  22.100  1.00 26.19           C
ANISOU 1843  C   ILE A 124     3377   4147   2428   -968    -33    769       C
ATOM   1844  O   ILE A 124      15.389  10.468  23.235  1.00 32.18           O
ANISOU 1844  O   ILE A 124     4063   5228   2938  -1267   -138    963       O
ATOM   1845  CB  ILE A 124      13.228  12.419  21.981  1.00 27.12           C
ANISOU 1845  CB  ILE A 124     3508   4293   2503  -1062    348     60       C
ATOM   1846  CG1 ILE A 124      11.756  12.748  21.717  1.00 29.63           C
ANISOU 1846  CG1 ILE A 124     3821   4493   2943  -1050    518   -221       C
ATOM   1847  CG2 ILE A 124      14.138  13.128  20.998  1.00 28.12           C
ANISOU 1847  CG2 ILE A 124     3630   4237   2818   -805    342     14       C
ATOM   1848  CD1 ILE A 124      11.297  14.078  22.279  1.00 38.85           C
ANISOU 1848  CD1 ILE A 124     4879   5774   4107  -1229    753   -622       C
ATOM   1849  H   ILE A 124      12.646  10.591  23.671  1.00 33.76           H
ATOM   1850  HA  ILE A 124      13.178  10.606  21.012  1.00 30.00           H
ATOM   1851  HB  ILE A 124      13.453  12.728  22.872  1.00 32.55           H
ATOM   1852 HG12 ILE A 124      11.612  12.770  20.758  1.00 35.57           H
ATOM   1853 HG13 ILE A 124      11.208  12.055  22.118  1.00 35.57           H
ATOM   1854 HG21 ILE A 124      13.839  14.045  20.895  1.00 33.76           H
ATOM   1855 HG22 ILE A 124      15.046  13.113  21.341  1.00 33.76           H
ATOM   1856 HG23 ILE A 124      14.100  12.669  20.145  1.00 33.76           H
ATOM   1857 HD11 ILE A 124      10.357  14.199  22.076  1.00 46.63           H
ATOM   1858 HD12 ILE A 124      11.431  14.077  23.240  1.00 46.63           H
ATOM   1859 HD13 ILE A 124      11.818  14.789  21.874  1.00 46.63           H
ATOM   1860  N   THR A 125      15.583  10.282  21.000  1.00 26.05           N
ANISOU 1860  N   THR A 125     3366   3843   2688   -647    -68    827       N
ATOM   1861  CA  THR A 125      16.950   9.814  21.013  1.00 28.17           C
ANISOU 1861  CA  THR A 125     3533   4087   3084   -559   -222   1123       C
ATOM   1862  C   THR A 125      17.888  10.866  20.442  1.00 30.38           C
ANISOU 1862  C   THR A 125     3776   4374   3395   -434   -153    959       C
ATOM   1863  O   THR A 125      17.611  11.560  19.437  1.00 23.95           O
ANISOU 1863  O   THR A 125     3030   3407   2663   -271    -13    682       O
ATOM   1864  CB  THR A 125      17.066   8.561  20.142  1.00 35.74           C
ANISOU 1864  CB  THR A 125     4494   4676   4410   -295   -268   1274       C
ATOM   1865  OG1 THR A 125      16.364   7.484  20.772  1.00 38.29           O
ANISOU 1865  OG1 THR A 125     4828   4975   4746   -430   -373   1507       O
ATOM   1866  CG2 THR A 125      18.512   8.168  19.954  1.00 45.93           C
ANISOU 1866  CG2 THR A 125     5627   5862   5962   -141   -372   1510       C
ATOM   1867  OXT THR A 125      18.976  11.022  20.994  1.00 34.34           O
ANISOU 1867  OXT THR A 125     4160   5051   3836   -522   -264   1148       O
ATOM   1868  H   THR A 125      15.266  10.380  20.206  1.00 31.27           H
ATOM   1869  HA  THR A 125      17.226   9.619  21.922  1.00 33.82           H
ATOM   1870  HB  THR A 125      16.685   8.738  19.268  1.00 42.90           H
ATOM   1871  HG1 THR A 125      15.685   7.778  21.170  1.00 45.96           H
ATOM   1872 HG21 THR A 125      18.574   7.227  19.727  1.00 55.13           H
ATOM   1873 HG22 THR A 125      18.908   8.690  19.239  1.00 55.13           H
ATOM   1874 HG23 THR A 125      19.009   8.327  20.772  1.00 55.13           H
TER
HETATM 1875  S1  FES K 201      21.400  26.699  16.408  1.00 19.16           S
ANISOU 1875  S1  FES K 201     2539   2672   2068   -596    417   -181       S
HETATM 1876  S2  FES K 201      23.704  25.578  13.873  1.00 20.07           S
ANISOU 1876  S2  FES K 201     2447   2833   2347   -531    372   -449       S
HETATM 1877 FE1  FES K 201      21.561  25.416  14.600  1.00 18.54          Fe
ANISOU 1877 FE1  FES K 201     2432   2449   2162   -586    434   -244      Fe
HETATM 1878 FE2  FES K 201      23.559  26.808  15.780  1.00 19.43          Fe
ANISOU 1878 FE2  FES K 201     2415   2857   2109   -530    335   -353      Fe
HETATM 1879 O    HOH S   7       7.387  12.311   4.115  1.00 22.84           O
HETATM 1880 O    HOH S  20      16.492  17.898  15.736  1.00 15.59           O
HETATM 1881 O    HOH S  22      20.435  14.358   2.613  0.87 20.03           O
HETATM 1882 O    HOH S  24       0.460  20.479  11.957  0.93 24.74           O
HETATM 1883 O    HOH S  26      10.264  18.684  18.519  0.81 16.46           O
HETATM 1884 O    HOH S  27      31.798  23.190  10.020  0.91 40.62           O
HETATM 1885 O    HOH S  29      12.428   8.501  13.917  1.00 20.61           O
HETATM 1886 O    HOH S  34       8.965  25.892  19.390  0.68 30.30           O
HETATM 1887 O    HOH S  39      11.482  25.460   8.008  0.62 23.89           O
HETATM 1888 O    HOH S  42      14.176  26.049  20.280  0.91 28.72           O
HETATM 1889 O    HOH S  48      25.890  21.359  12.770  0.61 20.33           O
HETATM 1890 O    HOH S  51      10.947   4.600  15.620  1.00 34.87           O
HETATM 1891 O    HOH S  53      23.812  11.866  16.872  1.00 34.00           O
HETATM 1892 O    HOH S  60      11.831  27.437  15.544  0.44 27.09           O
HETATM 1893 O    HOH S  69      -5.686   3.525  15.691  0.97 52.51           O
HETATM 1894 O    HOH S  70      28.678  24.707   7.857  0.91 24.75           O
HETATM 1895 O    HOH S  73      -0.000   0.000  17.381  0.35 35.55           O
HETATM 1896 O    HOH S  75       6.230  20.952   5.473  1.00 30.93           O
HETATM 1897 O    HOH S  76      23.359  25.892   6.861  0.97 27.78           O
HETATM 1898 O    HOH S  78      23.049  31.296  19.365  0.86 50.14           O
HETATM 1899 O    HOH S  81      30.254  19.754  15.171  0.49 26.31           O
HETATM 1900 O    HOH S  84       3.217  20.873   6.717  0.98 43.77           O
HETATM 1901 O    HOH S  85      -6.332  -1.534  10.377  0.86 36.63           O
HETATM 1902 O    HOH S  87      17.959  26.437  -5.897  0.86 28.07           O
HETATM 1903 O    HOH S  89      15.221   9.755   5.736  1.00 27.02           O
HETATM 1904 O   AHOH S  92      11.979  24.325   5.445  0.91 26.99           O
HETATM 1905 O   BHOH S  92      11.491  25.280   5.408  0.09 27.24           O
HETATM 1906 O    HOH S  96      10.370  10.431  20.632  0.00 26.44           O
HETATM 1907 O    HOH S 106      25.341  12.928  13.584  1.00 25.15           O
HETATM 1908 O    HOH S 110      11.052  24.967  13.991  0.70 28.20           O
HETATM 1909 O    HOH S 113      11.736  24.715  11.260  0.83 26.42           O
HETATM 1910 O    HOH S 115      20.841  31.478  18.055  0.86 29.75           O
HETATM 1911 O    HOH S 116      29.733  18.028   4.603  0.75 23.70           O
HETATM 1912 O    HOH S 118      17.648  29.452  19.440  0.97 28.49           O
HETATM 1913 O    HOH S 119      -1.282   0.388   9.434  1.00 34.33           O
HETATM 1914 O    HOH S 120      20.160  11.551  15.167  1.00 37.80           O
HETATM 1915 O    HOH S 121      14.179   6.890  17.314  0.92 40.19           O
HETATM 1916 O    HOH S 122       7.624  16.633  21.455  0.83 32.39           O
HETATM 1917 O    HOH S 124       2.656   0.570   7.171  1.00 45.57           O
HETATM 1918 O    HOH S 125       0.271   6.274  24.583  0.64 37.65           O
HETATM 1919 O    HOH S 131       8.542  24.578  14.041  0.64 17.97           O
HETATM 1920 O    HOH S 132      17.342  27.644   5.488  1.00 40.77           O
HETATM 1921 O    HOH S 133      18.498   8.293  11.304  0.76 32.28           O
HETATM 1922 O    HOH S 136      21.807  27.974   6.318  0.98 39.58           O
HETATM 1923 O    HOH S 140      -3.738  13.369  17.212  0.86 42.79           O
HETATM 1924 O    HOH S 145       7.389  25.461  11.633  0.65 19.79           O
HETATM 1925 O    HOH S 146      11.787   5.968  12.999  0.68 24.22           O
HETATM 1926 O    HOH S 153      13.839   7.239  20.095  0.80 29.90           O
HETATM 1927 O    HOH S 164       7.709   1.322  15.933  0.81 31.10           O
HETATM 1928 O    HOH S 168      -3.362  10.997  19.374  0.99 35.90           O
HETATM 1929 O    HOH S 170       7.752  23.751  17.696  1.00 29.91           O
HETATM 1930 O    HOH S 174      -6.389   0.020  18.297  0.99 51.59           O
HETATM 1931 O    HOH S 177       6.984  23.350   5.871  0.84 37.56           O
HETATM 1932 O    HOH S 180      -7.574  -3.853  11.728  0.99 46.71           O
HETATM 1933 O    HOH S 183       1.392  24.051  24.783  1.00 39.37           O
HETATM 1934 O    HOH S 184      14.802  11.682   0.701  0.95 41.33           O
HETATM 1935 O    HOH S 185      19.648  28.541   5.062  0.83 39.36           O
HETATM 1936 O    HOH S 186      19.843  25.746  -0.150  0.89 29.94           O
HETATM 1937 O    HOH S 187       0.000   6.113   0.000  0.15 41.44           O
HETATM 1938 O    HOH S 188       7.577  24.356  34.000  1.00 49.86           O
HETATM 1939 O    HOH S 190      19.946  13.033   0.310  1.00 34.95           O
HETATM 1940 O    HOH S 191      -3.686  11.784  13.561  0.98 40.12           O
HETATM 1941 O    HOH S 193      -3.134  11.451   2.697  1.00 41.92           O
HETATM 1942 O    HOH S 194      -1.430  12.757  25.577  0.99 44.65           O
HETATM 1943 O    HOH S 196       1.800   2.957   0.834  0.80 40.88           O
HETATM 1944 O    HOH S 199      13.475   5.532   1.315  1.00 48.28           O
HETATM 1945 O    HOH S 200      -3.770  16.896  32.173  0.99 45.17           O
HETATM 1946 O    HOH S 201      22.163  10.984   2.597  1.00 42.33           O
HETATM 1947 O    HOH S 202      -0.007  16.950  13.372  0.77 29.74           O
HETATM 1948 O    HOH S 204       7.393  11.455  -3.704  0.86 44.54           O
HETATM 1949 O    HOH S 205      21.692  14.155  23.538  1.00 30.98           O
HETATM 1950 O    HOH S 206      23.334  29.971   6.689  0.66 45.72           O
HETATM 1951 O    HOH S 207      25.608  11.625   4.942  1.00 43.65           O
HETATM 1952 O    HOH S 209      13.412  26.010  17.082  0.50 26.15           O
HETATM 1953 O    HOH S 211      12.945   2.283   2.591  0.97 48.36           O
HETATM 1954 O    HOH S 212      27.387  16.267  15.368  0.56 28.70           O
HETATM 1955 O    HOH S 213       9.405  20.118   2.435  0.96 33.03           O
HETATM 1956 O    HOH S 214       2.527  -0.054   3.713  0.93 45.66           O
HETATM 1957 O    HOH S 219      -0.742  16.341  16.918  1.00 44.50           O
HETATM 1958 O    HOH S 226      15.775  26.416   3.167  1.00 36.85           O
HETATM 1959 O    HOH S 228      -2.726  15.426  18.277  0.56 46.73           O
HETATM 1960 O    HOH S 232       1.716  21.064   8.699  0.79 43.02           O
HETATM 1961 O    HOH S 233      -6.114  13.559   4.425  1.00 48.99           O
HETATM 1962 O    HOH S 236      30.647  25.858   9.536  0.68 38.59           O
HETATM 1963 O    HOH S 244      -6.390   0.673   7.757  1.00 50.33           O
HETATM 1964 O    HOH S 247      20.896   5.508   4.503  0.85 50.93           O
HETATM 1965 O    HOH S 253      13.301   3.997   8.839  0.99 43.67           O
HETATM 1966 O    HOH S 254      23.516  11.113  14.012  0.62 36.08           O
HETATM 1967 O    HOH S 255      -6.510   5.211   7.084  0.86 40.07           O
HETATM 1968 O    HOH S 256      -2.109  22.724  34.748  1.00 27.23           O
HETATM 1969 O    HOH S 258       4.824   1.698   7.894  0.98 45.30           O
HETATM 1970 O    HOH S 263      -2.002  15.998  33.747  0.99 37.75           O
HETATM 1971 O    HOH S 266      20.707  10.450  12.835  0.82 37.44           O
HETATM 1972 O    HOH S 268      13.012  10.994  25.791  1.00 42.91           O
HETATM 1973 O    HOH S 269      13.028  -0.178   0.853  0.64 47.93           O
HETATM 1974 O    HOH S 272      14.459   9.621   2.560  0.70 35.28           O
HETATM 1975 O    HOH S 275      16.689  13.365   0.016  0.71 37.53           O
HETATM 1976 O    HOH S 281      16.551   7.763  13.085  1.00 42.61           O
HETATM 1977 O    HOH S 284       9.405  24.263   4.495  1.00 48.06           O
HETATM 1978 O    HOH S 294      18.070  13.666  24.061  1.00 42.22           O
HETATM 1979 O    HOH S 295      24.404  11.957   1.149  0.99 41.76           O
HETATM 1980 O    HOH S 296      -0.098   1.365   6.442  1.00 44.71           O
HETATM 1981 O    HOH S 297      -0.632  15.970   9.049  0.40 34.54           O
HETATM 1982 O    HOH S 302      13.654   2.584   5.799  0.78 58.10           O
HETATM 1983 O    HOH S 303      13.387   7.949   0.912  1.00 45.09           O
HETATM 1984 O    HOH S 305      15.471  11.399  25.681  0.92 60.71           O
HETATM 1985 O    HOH S 308      29.012  13.700   3.964  0.98 45.38           O
HETATM 1986 O    HOH S 309      -2.127  11.509  -0.070  0.81 36.48           O
HETATM 1987 O    HOH S 313       1.307  24.147  22.182  0.25 32.72           O
HETATM 1988 O    HOH S 316      14.654   4.827   6.439  0.37 39.53           O
HETATM 1989  O   HOH S 318      14.177  16.062  -2.082  1.00 43.12           O
HETATM 1990  O   HOH S 319      -1.573   4.428  20.153  1.00 44.19           O
HETATM 1991  O   HOH S 320       1.168  13.831   0.050  0.99 42.09           O
HETATM 1992  O   HOH S 322       0.006   9.271   0.004  0.23 40.56           O
HETATM 1993  O   HOH S 324      -5.214  10.094   2.652  0.99 31.98           O
HETATM 1994  O   HOH S 325       2.610   4.319  -1.252  0.98 44.90           O
HETATM 1995  O   HOH S 327      25.238  26.178   4.900  1.00 38.27           O
HETATM 1996  O   HOH S 328      27.204  31.863  10.108  0.77 51.54           O
HETATM 1997  O   HOH S 329      23.294   9.106   6.872  0.71 32.70           O
HETATM 1998  O  AHOH S 330      11.016   5.643  25.577  0.40 33.09           O
HETATM 1999  O  BHOH S 330       9.535   5.974  25.522  0.60 28.84           O
HETATM 2000  O   HOH S 331      -0.361  20.206  25.991  1.00 40.06           O
HETATM 2001  O   HOH S 332       9.675  21.869  17.936  0.49 30.61           O
HETATM 2002  O   HOH S 333      11.700   4.524  28.262  1.00 38.69           O
HETATM 2003  O   HOH S 334       9.425   3.172  10.453  1.00 45.18           O
HETATM 2004  O   HOH S 335      28.663  19.104  13.580  0.86 42.60           O
HETATM 2005  C1 APG4 B   1       6.067  -2.700   3.400  0.45 34.89           C
HETATM 2006  C2 APG4 B   1       5.515  -2.963   2.020  0.45 38.28           C
HETATM 2007  C3 APG4 B   1       5.205  -1.102   0.601  0.45 37.58           C
HETATM 2008  C4 APG4 B   1       5.999   0.006  -0.046  0.45 37.15           C
HETATM 2009  C5 APG4 B   1       5.936   1.766  -1.563  0.45 38.13           C
HETATM 2010  C6 APG4 B   1       5.173   3.042  -1.825  0.45 39.19           C
HETATM 2011  O1 APG4 B   1       5.424  -1.589   3.987  0.45 39.73           O
HETATM 2012  O2 APG4 B   1       6.088  -2.092   1.071  0.45 43.19           O
HETATM 2013  O3 APG4 B   1       5.176   0.866  -0.802  0.45 37.74           O
HETATM 2014  O4 APG4 B   1       4.295   2.831  -2.901  0.45 40.26           O
HETATM 2015  O5 APG4 B   1      -0.064   3.880  -7.295  0.45 44.64           O
HETATM 2016  H11APG4 B   1       5.948  -3.498   3.939  0.45 41.88           H
HETATM 2017  H12APG4 B   1       7.023  -2.551   3.328  0.45 41.88           H
HETATM 2018  H21APG4 B   1       5.688  -3.890   1.796  0.45 45.94           H
HETATM 2019  H22APG4 B   1       4.551  -2.859   2.054  0.45 45.94           H
HETATM 2020  H31APG4 B   1       4.581  -1.475  -0.041  0.45 45.11           H
HETATM 2021  H32APG4 B   1       4.675  -0.741   1.329  0.45 45.11           H
HETATM 2022  H41APG4 B   1       6.461   0.491   0.655  0.45 44.60           H
HETATM 2023  H42APG4 B   1       6.682  -0.401  -0.602  0.45 44.60           H
HETATM 2024  H51APG4 B   1       6.763   1.981  -1.104  0.45 45.76           H
HETATM 2025  H52APG4 B   1       6.183   1.365  -2.411  0.45 45.76           H
HETATM 2026  H61APG4 B   1       4.697   3.295  -1.018  0.45 47.04           H
HETATM 2027  H62APG4 B   1       5.805   3.754  -2.012  0.45 47.04           H
HETATM 2028  HO1APG4 B   1       4.587  -1.739   3.986  0.45 47.68           H
HETATM 2029  HO5APG4 B   1       0.125   4.490  -7.864  0.45 53.58           H
HETATM 2030  C1 BPG4 B   1       6.028  -2.558   3.359  0.55 35.01           C
HETATM 2031  C2 BPG4 B   1       5.527  -2.835   1.964  0.55 38.40           C
HETATM 2032  C3 BPG4 B   1       5.224  -0.925   0.601  0.55 37.68           C
HETATM 2033  C4 BPG4 B   1       6.026   0.189  -0.026  0.55 37.16           C
HETATM 2034  C5 BPG4 B   1       5.981   1.935  -1.573  0.55 38.76           C
HETATM 2035  C6 BPG4 B   1       5.208   3.214  -1.792  0.55 39.43           C
HETATM 2036  O1 BPG4 B   1       5.416  -1.374   3.819  0.55 38.95           O
HETATM 2037  O2 BPG4 B   1       6.105  -1.918   1.065  0.55 43.62           O
HETATM 2038  O3 BPG4 B   1       5.217   1.028  -0.820  0.55 37.69           O
HETATM 2039  O4 BPG4 B   1       5.273   3.956  -0.602  0.55 36.60           O
HETATM 2040  O5 BPG4 B   1       4.294   8.665   3.613  0.55 46.06           O
HETATM 2041  H11BPG4 B   1       5.819  -3.314   3.930  0.55 42.02           H
HETATM 2042  H12BPG4 B   1       6.995  -2.479   3.342  0.55 42.02           H
HETATM 2043  H21BPG4 B   1       5.748  -3.750   1.731  0.55 46.09           H
HETATM 2044  H22BPG4 B   1       4.559  -2.772   1.964  0.55 46.09           H
HETATM 2045  H31BPG4 B   1       4.605  -1.290  -0.051  0.55 45.23           H
HETATM 2046  H32BPG4 B   1       4.688  -0.573   1.329  0.55 45.23           H
HETATM 2047  H41BPG4 B   1       6.454   0.689   0.687  0.55 44.60           H
HETATM 2048  H42BPG4 B   1       6.736  -0.212  -0.552  0.55 44.60           H
HETATM 2049  H51BPG4 B   1       6.814   2.138  -1.120  0.55 46.52           H
HETATM 2050  H52BPG4 B   1       6.216   1.552  -2.433  0.55 46.52           H
HETATM 2051  H61BPG4 B   1       5.592   3.695  -2.542  0.55 47.33           H
HETATM 2052  H62BPG4 B   1       4.295   2.998  -2.036  0.55 47.33           H
HETATM 2053  HO1BPG4 B   1       4.574  -1.470   3.755  0.55 46.75           H
HETATM 2054  HO5BPG4 B   1       3.651   9.221   3.701  0.55 55.29           H
HETATM 2055  C1  PG4 B   2       8.229   6.941  31.766  0.47 43.41           C
HETATM 2056  C2  PG4 B   2       8.249   7.083  30.263  0.47 49.55           C
HETATM 2057  C3  PG4 B   2      10.546   7.151  29.721  0.47 49.85           C
HETATM 2058  C4  PG4 B   2      11.107   7.374  28.332  0.47 40.79           C
HETATM 2059  C5  PG4 B   2      13.024   7.164  27.001  0.47 50.01           C
HETATM 2060  C6  PG4 B   2      14.335   7.873  26.765  0.47 45.19           C
HETATM 2061  C7  PG4 B   2      15.220   6.908  24.796  0.47 43.47           C
HETATM 2062  O1  PG4 B   2       7.402   7.943  32.308  0.47 38.58           O
HETATM 2063  O2  PG4 B   2       9.350   7.872  29.859  0.47 42.65           O
HETATM 2064  O3  PG4 B   2      12.521   7.391  28.301  0.47 39.44           O
HETATM 2065  O4  PG4 B   2      15.276   6.982  26.201  0.47 49.50           O
HETATM 2066  H11 PG4 B   2       9.137   7.009  32.102  0.47 52.11           H
HETATM 2067  H12 PG4 B   2       7.911   6.054  31.996  0.47 52.11           H
HETATM 2068  H21 PG4 B   2       8.287   6.196  29.871  0.47 59.47           H
HETATM 2069  H22 PG4 B   2       7.408   7.477  29.981  0.47 59.47           H
HETATM 2070  H31 PG4 B   2      11.195   7.434  30.384  0.47 59.83           H
HETATM 2071  H32 PG4 B   2      10.394   6.204  29.864  0.47 59.83           H
HETATM 2072  H41 PG4 B   2      10.759   6.672  27.759  0.47 48.96           H
HETATM 2073  H42 PG4 B   2      10.746   8.211  28.001  0.47 48.96           H
HETATM 2074  H51 PG4 B   2      13.154   6.213  26.856  0.47 60.03           H
HETATM 2075  H52 PG4 B   2      12.383   7.464  26.338  0.47 60.03           H
HETATM 2076  H61 PG4 B   2      14.173   8.633  26.184  0.47 54.24           H
HETATM 2077  H62 PG4 B   2      14.648   8.231  27.611  0.47 54.24           H
HETATM 2078  H71 PG4 B   2      15.894   6.299  24.457  0.47 52.18           H
HETATM 2079  H72 PG4 B   2      14.362   6.569  24.498  0.47 52.18           H
HETATM 2080  HO1 PG4 B   2       7.608   8.681  31.941  0.47 46.30           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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.