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ID        	=	 22120514373117729
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0

REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.18.2_3874: ???)
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) : 2.40    
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.72   
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.96  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.92 
REMARK   3   NUMBER OF REFLECTIONS             : 69087     
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 39122     
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2353
REMARK   3   R VALUE            (WORKING SET) : 0.2322
REMARK   3   FREE R VALUE                     : 0.2923
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.10  
REMARK   3   FREE R VALUE TEST SET COUNT      : 3525      
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   59.72 -    7.02    0.88     2967   158  0.1541 0.1947   0.929  0.902
REMARK   3     2    7.01 -    5.57    0.71     2317   176  0.1945 0.2175   0.889  0.859
REMARK   3     3    5.57 -    4.87    0.80     2700   134  0.1685 0.2259   0.906  0.820
REMARK   3     4    4.86 -    4.42    0.80     2663   170  0.1647 0.1913   0.923  0.913
REMARK   3     5    4.42 -    4.10    0.80     2696   148  0.1894 0.2686   0.885  0.783
REMARK   3     6    4.10 -    3.86    0.79     2674   144  0.1953 0.2605   0.875  0.695
REMARK   3     7    3.86 -    3.67    0.74     2488   107  0.2533 0.3646   0.799  0.495
REMARK   3     8    3.67 -    3.51    0.73     2465   136  0.2609 0.3204   0.797  0.601
REMARK   3     9    3.51 -    3.37    0.82     2766   129  0.2573 0.3058   0.793  0.711
REMARK   3    10    3.37 -    3.26    0.82     2740   179  0.2584 0.3563   0.786  0.605
REMARK   3    11    3.26 -    3.16    0.80     2707   131  0.2610 0.2926   0.782  0.704
REMARK   3    12    3.16 -    3.07    0.83     2799   158  0.2697 0.3214   0.755  0.479
REMARK   3    13    3.07 -    2.98    0.81     2766   122  0.2670 0.4103   0.776  0.545
REMARK   3    14    2.98 -    2.91    0.81     2670   136  0.2696 0.3419   0.791  0.592
REMARK   3    15    2.91 -    2.85    0.81     2798   141  0.2905 0.3941   0.767  0.619
REMARK   3    16    2.85 -    2.79    0.82     2693   149  0.3011 0.3602   0.708  0.563
REMARK   3    17    2.78 -    2.73    0.82     2793   174  0.2941 0.3561   0.743  0.593
REMARK   3    18    2.73 -    2.68    0.80     2677   118  0.3009 0.3588   0.725  0.539
REMARK   3    19    2.68 -    2.63    0.82     2806   147  0.3066 0.4183   0.693  0.432
REMARK   3    20    2.63 -    2.59    0.80     2728   125  0.3148 0.3398   0.670  0.428
REMARK   3    21    2.59 -    2.54    0.82     2734   145  0.3093 0.3775   0.656  0.411
REMARK   3    22    2.54 -    2.50    0.79     2638   143  0.3172 0.4355   0.678  0.356
REMARK   3    23    2.50 -    2.47    0.70     2337   129  0.3257 0.3953   0.613  0.396
REMARK   3    24    2.47 -    2.43    0.61     2078   121  0.3115 0.3069   0.650  0.586
REMARK   3    25    2.43 -    2.40    0.56     1862   105  0.3101 0.3925   0.596  0.519
REMARK   3  
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.11    
REMARK   3   SHRINKAGE RADIUS   : 0.90    
REMARK   3   GRID STEP FACTOR   : 4.00    
REMARK   3  
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.45    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.69   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  
REMARK   3  
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.013   0.193   8777
REMARK   3    ANGLE     :  1.831  44.731  11932
REMARK   3    CHIRALITY :  0.111   2.645   1385
REMARK   3    PLANARITY :  0.011   0.136   1546
REMARK   3    DIHEDRAL  : 12.085 179.904   1201
REMARK   3    MIN NONBONDED DISTANCE : 2.108
REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 12.76
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS :  0.99 %
REMARK   3      ALLOWED  :  3.32 %
REMARK   3      FAVORED  : 95.70 %
REMARK   3    ROTAMER OUTLIERS :  0.65 %
REMARK   3    CBETA DEVIATIONS :  0.75 %
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 : 0.37 %
REMARK   3  
REMARK   3  RAMA-Z (RAMACHANDRAN PLOT Z-SCORE):
REMARK   3  INTERPRETATION: BAD |RAMA-Z| > 3; SUSPICIOUS 2 < |RAMA-Z| < 3; GOOD |RAMA-Z| < 2.
REMARK   3  SCORES FOR WHOLE/HELIX/SHEET/LOOP ARE SCALED INDEPENDENTLY;
REMARK   3  THEREFORE, THE VALUES ARE NOT RELATED IN A SIMPLE MANNER.
REMARK   3    WHOLE: -1.25 (0.23), RESIDUES: 1124
REMARK   3    HELIX: -1.06 (0.21), RESIDUES: 430
REMARK   3    SHEET: -0.92 (0.45), RESIDUES: 106
REMARK   3    LOOP : -0.48 (0.25), RESIDUES: 588
REMARK   3  
REMARK   3                  min    max   mean    iso aniso
REMARK   3     Overall:   22.22 160.55  49.64   3.74  8746  8746
REMARK   3     Protein:   22.22 160.55  49.71   3.74  8605  8605
REMARK   3     Water:     24.20  72.57  45.18    N/A   141   141
REMARK   3     Chain  A:  22.22 103.63  45.24    N/A  2186  2186
REMARK   3     Chain  C:  23.80 102.36  49.77    N/A  2160  2160
REMARK   3     Chain  B:  23.31 160.55  49.94    N/A  2153  2153
REMARK   3     Chain  D:  25.76 132.46  54.05    N/A  2106  2106
REMARK   3     Chain  F:  24.20  72.57  45.18    N/A   141   141
REMARK   3     Histogram:
REMARK   3         Values      Number of atoms
REMARK   3      22.22 - 36.05      1504
REMARK   3      36.05 - 49.88      3521
REMARK   3      49.88 - 63.72      2360
REMARK   3      63.72 - 77.55       937
REMARK   3      77.55 - 91.38       285
REMARK   3      91.38 - 105.22       99
REMARK   3     105.22 - 119.05       24
REMARK   3     119.05 - 132.89       10
REMARK   3     132.89 - 146.72        0
REMARK   3     146.72 - 160.55        6
REMARK   3  
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 1     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: all
REMARK   3    ORIGIN FOR THE GROUP (A): -11.2354  16.2754  22.9753
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2097 T22:   0.3183                       
REMARK   3      T33:   0.2525 T12:   0.0010                       
REMARK   3      T13:  -0.0366 T23:  -0.0036                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   0.0772 L22:   0.7949                       
REMARK   3      L33:   0.5878 L12:  -0.0032                       
REMARK   3      L13:  -0.1686 L23:   0.0068                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0159 S12:  -0.0570 S13:   0.0291         
REMARK   3      S21:   0.0325 S22:   0.0334 S23:   0.0327         
REMARK   3      S31:   0.0150 S32:   0.0517 S33:  -0.0472         
REMARK   3  
REMARK   3  TORSION NCS DETAILS.
REMARK   3   NUMBER OF NCS GROUPS : 1     
REMARK   3   NCS GROUP : 1     
REMARK   3     SELECTION          : (chain 'A' and (resid 0 through 1
REMARK   3                        : or (resid 2 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 3 through 14 or (resid 15
REMARK   3                        : and (name N or name CA or name C
REMARK   3                        : or name O or name CB )) or resid
REMARK   3                        : 16 through 22 or (resid 23 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 24
REMARK   3                        : through 31 or (resid 32 and (name
REMARK   3                        : N or name CA or name C or name O
REMARK   3                        : or name CB )) or resid 33 through
REMARK   3                        : 34 or (resid 35 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 36 through 38
REMARK   3                        : or (resid 39 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 40 through 60 or
REMARK   3                        : (resid 67 through 70 and (name N
REMARK   3                        : or name CA or name C or name O or
REMARK   3                        : name CB )) or resid 71 through 72
REMARK   3                        : or (resid 73 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 74 through 76 or
REMARK   3                        : (resid 77 through 79 and (name N
REMARK   3                        : or name CA or name C or name O or
REMARK   3                        : name CB )) or resid 80 through 82
REMARK   3                        : or (resid 83 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 84 through 134 or
REMARK   3                        : (resid 135 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 136 through 173 or (resid
REMARK   3                        : 174 through 177 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 178 through
REMARK   3                        : 204 or (resid 205 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 206 through
REMARK   3                        : 225 or (resid 226 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 228 through
REMARK   3                        : 229 or (resid 230 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 231 through
REMARK   3                        : 236 or (resid 237 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 238 through
REMARK   3                        : 239 or (resid 240 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 241 through
REMARK   3                        : 243 or resid 245 through 250 or
REMARK   3                        : resid 252 through 260 or (resid
REMARK   3                        : 261 through 262 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 263 through
REMARK   3                        : 278 or (resid 279 through 281 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB ))))
REMARK   3     SELECTION          : (chain 'B' and (resid 0 through 22
REMARK   3                        : or (resid 23 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 24 through 41 or
REMARK   3                        : (resid 42 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 43 through 48 or (resid
REMARK   3                        : 49 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 50 through 60 or (resid 67 through
REMARK   3                        : 70 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 71 or (resid 72 through 73 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 74
REMARK   3                        : or (resid 75 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 76 through 82 or
REMARK   3                        : (resid 83 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 84 through 163 or (resid
REMARK   3                        : 164 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 165 through 171 or (resid 172
REMARK   3                        : through 177 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 178 through 225 or (resid
REMARK   3                        : 226 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 228 through 229 or (resid 230 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 231
REMARK   3                        : through 235 or (resid 236 through
REMARK   3                        : 237 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 238 through 239 or (resid 240 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 241
REMARK   3                        : through 243 or resid 245 through
REMARK   3                        : 250 or resid 252 through 260 or
REMARK   3                        : (resid 261 through 262 and (name N
REMARK   3                        : or name CA or name C or name O or
REMARK   3                        : name CB )) or resid 263 through
REMARK   3                        : 278 or (resid 279 through 281 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB ))))
REMARK   3     SELECTION          : (chain 'C' and (resid 0 through 14
REMARK   3                        : or (resid 15 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 16 through 31 or
REMARK   3                        : (resid 32 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 33 through 34 or (resid
REMARK   3                        : 35 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 36 through 38 or (resid 39 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 40
REMARK   3                        : or (resid 41 through 42 and (name
REMARK   3                        : N or name CA or name C or name O
REMARK   3                        : or name CB )) or resid 43 through
REMARK   3                        : 48 or (resid 49 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 50 through 60
REMARK   3                        : or (resid 67 through 70 and (name
REMARK   3                        : N or name CA or name C or name O
REMARK   3                        : or name CB )) or resid 71 or
REMARK   3                        : (resid 72 through 73 and (name N
REMARK   3                        : or name CA or name C or name O or
REMARK   3                        : name CB )) or resid 74 through 78
REMARK   3                        : or (resid 79 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 80 through 82 or
REMARK   3                        : (resid 83 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 84 through 134 or (resid
REMARK   3                        : 135 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 136 through 163 or (resid 164 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 165
REMARK   3                        : through 171 or (resid 172 through
REMARK   3                        : 177 and (name N or name CA or name
REMARK   3                        : C or name O or name CB )) or resid
REMARK   3                        : 178 through 204 or (resid 205 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 206
REMARK   3                        : through 225 or (resid 226 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 228
REMARK   3                        : through 243 or resid 245 through
REMARK   3                        : 250 or resid 252 through 260 or
REMARK   3                        : (resid 261 through 262 and (name N
REMARK   3                        : or name CA or name C or name O or
REMARK   3                        : name CB )) or resid 263 through
REMARK   3                        : 278 or (resid 279 through 281 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB ))))
REMARK   3     SELECTION          : (chain 'D' and (resid 0 through 1
REMARK   3                        : or (resid 2 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 3 through 14 or (resid 15
REMARK   3                        : and (name N or name CA or name C
REMARK   3                        : or name O or name CB )) or resid
REMARK   3                        : 16 through 22 or (resid 23 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 24
REMARK   3                        : through 31 or (resid 32 and (name
REMARK   3                        : N or name CA or name C or name O
REMARK   3                        : or name CB )) or resid 33 through
REMARK   3                        : 34 or (resid 35 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 36 through 38
REMARK   3                        : or (resid 39 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 40 through 68 or
REMARK   3                        : (resid 69 through 70 and (name N
REMARK   3                        : or name CA or name C or name O or
REMARK   3                        : name CB )) or resid 71 or (resid
REMARK   3                        : 72 through 73 and (name N or name
REMARK   3                        : CA or name C or name O or name CB
REMARK   3                        : )) or resid 74 or (resid 75 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 76
REMARK   3                        : or (resid 77 through 79 and (name
REMARK   3                        : N or name CA or name C or name O
REMARK   3                        : or name CB )) or resid 80 through
REMARK   3                        : 134 or (resid 135 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 136 through
REMARK   3                        : 163 or (resid 164 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 165 through
REMARK   3                        : 176 or (resid 177 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 178 through
REMARK   3                        : 204 or (resid 205 and (name N or
REMARK   3                        : name CA or name C or name O or
REMARK   3                        : name CB )) or resid 206 through
REMARK   3                        : 226 or resid 228 through 236 or
REMARK   3                        : (resid 237 and (name N or name CA
REMARK   3                        : or name C or name O or name CB ))
REMARK   3                        : or resid 238 through 243 or resid
REMARK   3                        : 245 through 250 or resid 252
REMARK   3                        : through 261 or (resid 262 and
REMARK   3                        : (name N or name CA or name C or
REMARK   3                        : name O or name CB )) or resid 263
REMARK   3                        : through 279 or (resid 280 through
REMARK   3                        : 281 and (name N or name CA or name
REMARK   3                        : C or name O or name CB ))))
REMARK   3     RESTRAINED TORSIONS: 3236
REMARK   3     BELOW LIMIT RMSD   : 2.595     
REMARK   3     ALL RESTRAINT RMSD : 14.430    
REMARK   3    Histogram of differences under limit:
REMARK   3       0.000 -    1.500: 1677
REMARK   3       1.500 -    3.000: 922
REMARK   3       3.000 -    4.500: 308
REMARK   3       4.500 -    6.000: 95
REMARK   3       6.000 -    7.500: 52
REMARK   3       7.500 -    9.000: 36
REMARK   3       9.000 -   10.500: 14
REMARK   3      10.500 -   12.000: 13
REMARK   3      12.000 -   13.500: 3
REMARK   3      13.500 -   15.000: 4
REMARK   3    Histogram of differences over limit:
REMARK   3      15.000 -   31.000: 23
REMARK   3      31.000 -   47.000: 24
REMARK   3      47.000 -   63.000: 14
REMARK   3      63.000 -   79.000: 16
REMARK   3      79.000 -   95.000: 13
REMARK   3      95.000 -  111.000: 6
REMARK   3     111.000 -  127.000: 6
REMARK   3     127.000 -  143.000: 2
REMARK   3     143.000 -  159.000: 3
REMARK   3     159.000 -  175.000: 5
REMARK   3
CRYST1   58.085   66.981   85.822  91.16 100.66 116.15 P 1
SCALE1      0.017216  0.008453  0.004243        0.00000
SCALE2      0.000000  0.016632  0.001931        0.00000
SCALE3      0.000000  0.000000  0.011936        0.00000
ATOM      1  N   PRO A   0       0.295 -21.540  20.634  1.00 74.14           N
ANISOU    1  N   PRO A   0    10543   9262   8364   1109    -86    386       N
ATOM      2  CA  PRO A   0      -1.147 -21.566  20.349  1.00 66.44           C
ANISOU    2  CA  PRO A   0     9618   8247   7378   1001    -79    379       C
ATOM      3  C   PRO A   0      -1.536 -20.810  19.085  1.00 58.28           C
ANISOU    3  C   PRO A   0     8542   7216   6384    927    -77    362       C
ATOM      4  O   PRO A   0      -1.207 -21.196  17.962  1.00 47.75           O
ANISOU    4  O   PRO A   0     7251   5846   5044    934    -45    365       O
ATOM      5  CB  PRO A   0      -1.752 -20.880  21.586  1.00 65.55           C
ANISOU    5  CB  PRO A   0     9452   8178   7278    970   -118    371       C
ATOM      6  CG  PRO A   0      -0.647 -19.932  22.083  1.00 59.92           C
ANISOU    6  CG  PRO A   0     8619   7543   6604   1031   -156    363       C
ATOM      7  CD  PRO A   0       0.641 -20.662  21.777  1.00 66.46           C
ANISOU    7  CD  PRO A   0     9471   8362   7418   1133   -135    378       C
ATOM      8  N   MET A   1      -2.251 -19.714  19.288  1.00 55.55           N
ANISOU    8  N   MET A   1     8116   6912   6077    857   -111    345       N
ATOM      9  CA  MET A   1      -2.587 -18.823  18.196  1.00 55.72           C
ANISOU    9  CA  MET A   1     8085   6946   6140    791   -117    328       C
ATOM     10  C   MET A   1      -1.444 -17.823  18.011  1.00 57.35           C
ANISOU   10  C   MET A   1     8181   7216   6394    838   -132    317       C
ATOM     11  O   MET A   1      -0.989 -17.198  18.978  1.00 62.64           O
ANISOU   11  O   MET A   1     8772   7944   7085    871   -162    312       O
ATOM     12  CB  MET A   1      -3.916 -18.143  18.522  1.00 53.51           C
ANISOU   12  CB  MET A   1     7773   6678   5880    698   -145    316       C
ATOM     13  CG  MET A   1      -4.634 -17.473  17.384  1.00 50.74           C
ANISOU   13  CG  MET A   1     7399   6321   5558    616   -152    302       C
ATOM     14  SD  MET A   1      -6.196 -16.722  17.936  1.00 48.62           S
ANISOU   14  SD  MET A   1     7086   6069   5317    517   -184    291       S
ATOM     15  CE  MET A   1      -7.291 -18.121  18.018  1.00 54.55           C
ANISOU   15  CE  MET A   1     7965   6743   6018    470   -158    304       C
ATOM     16  N   LYS A   2      -1.005 -17.652  16.768  1.00 50.27           N
ANISOU   16  N   LYS A   2     7281   6308   5513    836   -110    313       N
ATOM     17  CA  LYS A   2       0.109 -16.763  16.462  1.00 44.45           C
ANISOU   17  CA  LYS A   2     6444   5624   4822    877   -114    302       C
ATOM     18  C   LYS A   2      -0.243 -15.304  16.767  1.00 45.84           C
ANISOU   18  C   LYS A   2     6510   5861   5047    824   -155    281       C
ATOM     19  O   LYS A   2      -1.366 -14.855  16.501  1.00 43.64           O
ANISOU   19  O   LYS A   2     6235   5572   4775    742   -170    273       O
ATOM     20  CB  LYS A   2       0.498 -16.911  14.992  1.00 46.00           C
ANISOU   20  CB  LYS A   2     6676   5783   5020    875    -74    301       C
ATOM     21  CG  LYS A   2       1.421 -18.064  14.687  1.00 46.38           C
ANISOU   21  CG  LYS A   2     6795   5789   5036    958    -29    319       C
ATOM     22  CD  LYS A   2       2.158 -17.818  13.364  1.00 51.16           C
ANISOU   22  CD  LYS A   2     7395   6382   5662    971     11    314       C
ATOM     23  CE  LYS A   2       2.673 -19.113  12.705  1.00 55.76           C
ANISOU   23  CE  LYS A   2     8089   6895   6201   1027     69    332       C
ATOM     24  NZ  LYS A   2       1.617 -19.984  12.069  1.00 53.80           N
ANISOU   24  NZ  LYS A   2     7977   6567   5899    967     87    339       N
ATOM     25  N   THR A   3       0.725 -14.560  17.318  1.00 43.42           N
ANISOU   25  N   THR A   3     6103   5618   4775    872   -175    273       N
ATOM     26  CA  THR A   3       0.569 -13.141  17.626  1.00 39.39           C
ANISOU   26  CA  THR A   3     5487   5167   4311    830   -210    253       C
ATOM     27  C   THR A   3       1.134 -12.301  16.482  1.00 37.54           C
ANISOU   27  C   THR A   3     5197   4947   4118    817   -194    238       C
ATOM     28  O   THR A   3       2.267 -12.524  16.052  1.00 40.92           O
ANISOU   28  O   THR A   3     5610   5380   4556    876   -168    241       O
ATOM     29  CB  THR A   3       1.315 -12.768  18.912  1.00 43.25           C
ANISOU   29  CB  THR A   3     5903   5717   4814    883   -243    249       C
ATOM     30  OG1 THR A   3       0.677 -13.350  20.056  1.00 49.46           O
ANISOU   30  OG1 THR A   3     6739   6492   5563    886   -261    260       O
ATOM     31  CG2 THR A   3       1.419 -11.228  19.077  1.00 37.89           C
ANISOU   31  CG2 THR A   3     5110   5101   4187    846   -274    226       C
ATOM     32  N   ILE A   4       0.366 -11.318  16.024  1.00 32.83           N
ANISOU   32  N   ILE A   4     4569   4358   3546    741   -208    224       N
ATOM     33  CA  ILE A   4       0.757 -10.403  14.948  1.00 34.64           C
ANISOU   33  CA  ILE A   4     4751   4598   3811    719   -194    209       C
ATOM     34  C   ILE A   4       0.791  -8.968  15.484  1.00 36.00           C
ANISOU   34  C   ILE A   4     4816   4834   4029    691   -227    189       C
ATOM     35  O   ILE A   4      -0.198  -8.497  16.070  1.00 33.28           O
ANISOU   35  O   ILE A   4     4459   4500   3685    642   -258    185       O
ATOM     36  CB  ILE A   4      -0.208 -10.481  13.758  1.00 32.53           C
ANISOU   36  CB  ILE A   4     4554   4276   3529    652   -181    210       C
ATOM     37  CG1 ILE A   4      -0.146 -11.878  13.114  1.00 38.54           C
ANISOU   37  CG1 ILE A   4     5429   4972   4245    678   -143    228       C
ATOM     38  CG2 ILE A   4       0.132  -9.393  12.791  1.00 32.31           C
ANISOU   38  CG2 ILE A   4     4476   4263   3537    627   -171    194       C
ATOM     39  CD1 ILE A   4      -1.354 -12.192  12.230  1.00 30.98           C
ANISOU   39  CD1 ILE A   4     4557   3956   3260    605   -143    231       C
ATOM     40  N   LEU A   5       1.916  -8.269  15.280  1.00 31.74           N
ANISOU   40  N   LEU A   5     4199   4335   3527    722   -218    176       N
ATOM     41  CA  LEU A   5       2.020  -6.856  15.649  1.00 30.14           C
ANISOU   41  CA  LEU A   5     3898   4187   3367    691   -245    155       C
ATOM     42  C   LEU A   5       1.769  -5.975  14.414  1.00 32.74           C
ANISOU   42  C   LEU A   5     4220   4502   3719    637   -226    143       C
ATOM     43  O   LEU A   5       2.524  -6.051  13.438  1.00 32.25           O
ANISOU   43  O   LEU A   5     4165   4423   3667    657   -188    141       O
ATOM     44  CB  LEU A   5       3.393  -6.565  16.251  1.00 31.70           C
ANISOU   44  CB  LEU A   5     4010   4439   3594    751   -250    146       C
ATOM     45  CG  LEU A   5       3.804  -5.096  16.387  1.00 35.12           C
ANISOU   45  CG  LEU A   5     4341   4927   4076    723   -266    121       C
ATOM     46  CD1 LEU A   5       2.892  -4.444  17.377  1.00 31.44           C
ANISOU   46  CD1 LEU A   5     3855   4484   3606    680   -309    114       C
ATOM     47  CD2 LEU A   5       5.277  -4.941  16.832  1.00 35.91           C
ANISOU   47  CD2 LEU A   5     4357   5079   4207    784   -268    113       C
ATOM     48  N   VAL A   6       0.722  -5.144  14.451  1.00 26.26           N
ANISOU   48  N   VAL A   6     3388   3684   2906    572   -251    135       N
ATOM     49  CA  VAL A   6       0.391  -4.258  13.334  1.00 32.04           C
ANISOU   49  CA  VAL A   6     4118   4401   3657    520   -240    124       C
ATOM     50  C   VAL A   6       0.649  -2.803  13.732  1.00 32.37           C
ANISOU   50  C   VAL A   6     4064   4495   3740    499   -257    102       C
ATOM     51  O   VAL A   6      -0.045  -2.250  14.600  1.00 26.52           O
ANISOU   51  O   VAL A   6     3292   3778   3005    471   -291     98       O
ATOM     52  CB  VAL A   6      -1.067  -4.413  12.878  1.00 30.57           C
ANISOU   52  CB  VAL A   6     3996   4171   3447    461   -255    132       C
ATOM     53  CG1 VAL A   6      -1.344  -3.447  11.679  1.00 23.25           C
ANISOU   53  CG1 VAL A   6     3068   3228   2537    413   -247    122       C
ATOM     54  CG2 VAL A   6      -1.382  -5.860  12.542  1.00 29.06           C
ANISOU   54  CG2 VAL A   6     3904   3925   3212    474   -240    152       C
ATOM     55  N   THR A   7       1.579  -2.164  13.030  1.00 28.26           N
ANISOU   55  N   THR A   7     3504   3986   3248    507   -229     89       N
ATOM     56  CA  THR A   7       1.826  -0.741  13.176  1.00 26.99           C
ANISOU   56  CA  THR A   7     3264   3866   3126    478   -238     67       C
ATOM     57  C   THR A   7       0.853   0.068  12.324  1.00 26.45           C
ANISOU   57  C   THR A   7     3223   3770   3058    416   -239     63       C
ATOM     58  O   THR A   7       0.288  -0.416  11.330  1.00 23.08           O
ANISOU   58  O   THR A   7     2871   3291   2607    398   -226     75       O
ATOM     59  CB  THR A   7       3.235  -0.372  12.732  1.00 29.02           C
ANISOU   59  CB  THR A   7     3467   4144   3415    508   -202     54       C
ATOM     60  OG1 THR A   7       3.364  -0.649  11.326  1.00 26.76           O
ANISOU   60  OG1 THR A   7     3240   3808   3119    504   -156     59       O
ATOM     61  CG2 THR A   7       4.278  -1.130  13.543  1.00 30.06           C
ANISOU   61  CG2 THR A   7     3563   4308   3551    576   -204     58       C
ATOM     62  N   GLY A   8       0.696   1.334  12.706  1.00 26.89           N
ANISOU   62  N   GLY A   8     3218   3859   3142    383   -256     46       N
ATOM     63  CA  GLY A   8      -0.276   2.197  12.072  1.00 23.40           C
ANISOU   63  CA  GLY A   8     2794   3395   2702    328   -264     43       C
ATOM     64  C   GLY A   8      -1.660   1.591  12.168  1.00 23.57           C
ANISOU   64  C   GLY A   8     2872   3386   2696    304   -293     61       C
ATOM     65  O   GLY A   8      -2.418   1.558  11.190  1.00 22.22           O
ANISOU   65  O   GLY A   8     2757   3173   2512    272   -293     68       O
ATOM     66  N   GLY A   9      -2.002   1.128  13.368  1.00 22.27           N
ANISOU   66  N   GLY A   9     2695   3242   2524    316   -318     67       N
ATOM     67  CA  GLY A   9      -3.298   0.517  13.576  1.00 26.05           C
ANISOU   67  CA  GLY A   9     3223   3695   2981    291   -340     83       C
ATOM     68  C   GLY A   9      -4.475   1.443  13.346  1.00 28.99           C
ANISOU   68  C   GLY A   9     3587   4060   3367    238   -361     81       C
ATOM     69  O   GLY A   9      -5.588   0.954  13.130  1.00 35.07           O
ANISOU   69  O   GLY A   9     4402   4800   4124    210   -377     94       O
ATOM     70  N   SER A  10      -4.277   2.767  13.399  1.00 26.52           N
ANISOU   70  N   SER A  10     3218   3775   3083    222   -362     64       N
ATOM     71  CA  SER A  10      -5.394   3.694  13.215  1.00 27.94           C
ANISOU   71  CA  SER A  10     3390   3949   3278    177   -382     63       C
ATOM     72  C   SER A  10      -5.494   4.223  11.784  1.00 31.99           C
ANISOU   72  C   SER A  10     3934   4430   3793    154   -372     62       C
ATOM     73  O   SER A  10      -6.362   5.062  11.506  1.00 37.73           O
ANISOU   73  O   SER A  10     4654   5150   4532    121   -389     61       O
ATOM     74  CB  SER A  10      -5.332   4.876  14.202  1.00 25.57           C
ANISOU   74  CB  SER A  10     3020   3691   3004    170   -390     48       C
ATOM     75  OG  SER A  10      -4.065   5.537  14.256  1.00 33.60           O
ANISOU   75  OG  SER A  10     3992   4737   4036    188   -371     29       O
ATOM     76  N   GLY A  11      -4.652   3.738  10.870  1.00 27.78           N
ANISOU   76  N   GLY A  11     3436   3873   3244    173   -345     62       N
ATOM     77  CA  GLY A  11      -4.676   4.160   9.480  1.00 29.79           C
ANISOU   77  CA  GLY A  11     3734   4092   3494    154   -332     61       C
ATOM     78  C   GLY A  11      -5.672   3.423   8.586  1.00 28.26           C
ANISOU   78  C   GLY A  11     3619   3848   3272    130   -351     78       C
ATOM     79  O   GLY A  11      -6.349   2.467   8.969  1.00 28.31           O
ANISOU   79  O   GLY A  11     3651   3844   3263    127   -371     91       O
ATOM     80  N   PHE A  12      -5.713   3.880   7.337  1.00 28.68           N
ANISOU   80  N   PHE A  12     3714   3866   3315    112   -343     77       N
ATOM     81  CA  PHE A  12      -6.636   3.343   6.339  1.00 32.43           C
ANISOU   81  CA  PHE A  12     4268   4291   3762     85   -367     91       C
ATOM     82  C   PHE A  12      -6.523   1.835   6.193  1.00 30.91           C
ANISOU   82  C   PHE A  12     4138   4070   3537    100   -358    103       C
ATOM     83  O   PHE A  12      -7.536   1.131   6.132  1.00 29.44           O
ANISOU   83  O   PHE A  12     3991   3861   3334     76   -391    116       O
ATOM     84  CB  PHE A  12      -6.353   3.989   4.993  1.00 32.55           C
ANISOU   84  CB  PHE A  12     4331   4272   3766     74   -350     86       C
ATOM     85  CG  PHE A  12      -7.020   3.315   3.843  1.00 30.17           C
ANISOU   85  CG  PHE A  12     4124   3913   3426     52   -369    100       C
ATOM     86  CD1 PHE A  12      -8.350   3.553   3.564  1.00 32.82           C
ANISOU   86  CD1 PHE A  12     4475   4235   3760     15   -423    109       C
ATOM     87  CD2 PHE A  12      -6.306   2.470   3.015  1.00 35.40           C
ANISOU   87  CD2 PHE A  12     4861   4535   4055     69   -333    102       C
ATOM     88  CE1 PHE A  12      -8.962   2.950   2.485  1.00 34.68           C
ANISOU   88  CE1 PHE A  12     4798   4418   3959     -9   -447    120       C
ATOM     89  CE2 PHE A  12      -6.910   1.860   1.925  1.00 34.40           C
ANISOU   89  CE2 PHE A  12     4831   4352   3888     45   -352    113       C
ATOM     90  CZ  PHE A  12      -8.244   2.102   1.658  1.00 33.14           C
ANISOU   90  CZ  PHE A  12     4686   4180   3725      5   -412    121       C
ATOM     91  N   LEU A  13      -5.295   1.332   6.026  1.00 30.55           N
ANISOU   91  N   LEU A  13     4106   4019   3480    138   -313     99       N
ATOM     92  CA  LEU A  13      -5.079  -0.102   5.846  1.00 28.02           C
ANISOU   92  CA  LEU A  13     3852   3667   3127    159   -297    111       C
ATOM     93  C   LEU A  13      -4.961  -0.865   7.163  1.00 26.80           C
ANISOU   93  C   LEU A  13     3662   3544   2976    187   -301    116       C
ATOM     94  O   LEU A  13      -5.573  -1.933   7.321  1.00 22.68           O
ANISOU   94  O   LEU A  13     3190   2998   2429    180   -315    129       O
ATOM     95  CB  LEU A  13      -3.840  -0.328   4.980  1.00 24.84           C
ANISOU   95  CB  LEU A  13     3489   3240   2711    191   -242    107       C
ATOM     96  CG  LEU A  13      -3.491  -1.792   4.784  1.00 27.73           C
ANISOU   96  CG  LEU A  13     3925   3570   3040    220   -217    119       C
ATOM     97  CD1 LEU A  13      -4.613  -2.582   4.138  1.00 23.35           C
ANISOU   97  CD1 LEU A  13     3463   2962   2445    182   -247    133       C
ATOM     98  CD2 LEU A  13      -2.234  -1.881   3.953  1.00 34.43           C
ANISOU   98  CD2 LEU A  13     4803   4396   3883    255   -155    114       C
ATOM     99  N   GLY A  14      -4.194  -0.323   8.116  1.00 26.42           N
ANISOU   99  N   GLY A  14     3532   3548   2959    215   -290    105       N
ATOM    100  CA  GLY A  14      -3.966  -1.029   9.373  1.00 24.59           C
ANISOU  100  CA  GLY A  14     3272   3345   2727    248   -294    110       C
ATOM    101  C   GLY A  14      -5.246  -1.406  10.096  1.00 26.77           C
ANISOU  101  C   GLY A  14     3555   3619   2996    219   -332    120       C
ATOM    102  O   GLY A  14      -5.389  -2.539  10.565  1.00 27.97           O
ANISOU  102  O   GLY A  14     3745   3758   3124    234   -332    132       O
ATOM    103  N   ARG A  15      -6.180  -0.441  10.226  1.00 28.19           N
ANISOU  103  N   ARG A  15     3700   3814   3199    177   -362    116       N
ATOM    104  CA  ARG A  15      -7.442  -0.672  10.928  1.00 27.22           C
ANISOU  104  CA  ARG A  15     3572   3692   3077    147   -395    124       C
ATOM    105  C   ARG A  15      -8.241  -1.777  10.250  1.00 29.49           C
ANISOU  105  C   ARG A  15     3942   3929   3334    121   -405    139       C
ATOM    106  O   ARG A  15      -8.863  -2.615  10.916  1.00 29.37           O
ANISOU  106  O   ARG A  15     3945   3906   3308    114   -414    149       O
ATOM    107  CB  ARG A  15      -8.247   0.637  11.026  1.00 27.70           C
ANISOU  107  CB  ARG A  15     3580   3773   3171    111   -420    117       C
ATOM    108  CG  ARG A  15      -9.163   0.910   9.834  1.00 30.51           C
ANISOU  108  CG  ARG A  15     3975   4094   3525     68   -443    123       C
ATOM    109  CD  ARG A  15      -9.865   2.217   9.976  1.00 35.32           C
ANISOU  109  CD  ARG A  15     4528   4724   4167     43   -466    117       C
ATOM    110  NE  ARG A  15     -10.706   2.274  11.180  1.00 37.94           N
ANISOU  110  NE  ARG A  15     4814   5082   4520     31   -482    121       N
ATOM    111  CZ  ARG A  15     -10.989   3.399  11.838  1.00 38.84           C
ANISOU  111  CZ  ARG A  15     4864   5228   4666     26   -487    113       C
ATOM    112  NH1 ARG A  15     -11.767   3.377  12.912  1.00 42.46           N
ANISOU  112  NH1 ARG A  15     5289   5705   5141     16   -496    117       N
ATOM    113  NH2 ARG A  15     -10.505   4.555  11.412  1.00 37.67           N
ANISOU  113  NH2 ARG A  15     4692   5091   4532     29   -480    101       N
ATOM    114  N   ARG A  16      -8.214  -1.812   8.925  1.00 30.52           N
ANISOU  114  N   ARG A  16     4128   4021   3448    107   -402    140       N
ATOM    115  CA  ARG A  16      -8.882  -2.888   8.229  1.00 26.81           C
ANISOU  115  CA  ARG A  16     3743   3499   2944     81   -413    153       C
ATOM    116  C   ARG A  16      -8.086  -4.191   8.359  1.00 30.42           C
ANISOU  116  C   ARG A  16     4257   3935   3367    121   -378    160       C
ATOM    117  O   ARG A  16      -8.662  -5.270   8.232  1.00 32.04           O
ANISOU  117  O   ARG A  16     4528   4102   3542    104   -384    170       O
ATOM    118  CB  ARG A  16      -9.090  -2.492   6.773  1.00 27.06           C
ANISOU  118  CB  ARG A  16     3824   3494   2963     53   -423    152       C
ATOM    119  CG  ARG A  16     -10.314  -1.613   6.519  1.00 28.50           C
ANISOU  119  CG  ARG A  16     3979   3681   3169      4   -471    152       C
ATOM    120  CD  ARG A  16     -10.131  -0.764   5.240  1.00 33.56           C
ANISOU  120  CD  ARG A  16     4648   4301   3804     -6   -475    147       C
ATOM    121  NE  ARG A  16     -11.225   0.189   5.049  1.00 35.80           N
ANISOU  121  NE  ARG A  16     4897   4593   4113    -44   -521    147       N
ATOM    122  CZ  ARG A  16     -11.204   1.468   5.423  1.00 35.35           C
ANISOU  122  CZ  ARG A  16     4769   4572   4092    -40   -524    139       C
ATOM    123  NH1 ARG A  16     -10.133   1.996   6.005  1.00 32.03           N
ANISOU  123  NH1 ARG A  16     4299   4184   3686     -4   -485    128       N
ATOM    124  NH2 ARG A  16     -12.279   2.218   5.222  1.00 37.26           N
ANISOU  124  NH2 ARG A  16     4986   4817   4354    -71   -567    143       N
ATOM    125  N   LEU A  17      -6.763  -4.140   8.566  1.00 25.05           N
ANISOU  125  N   LEU A  17     3554   3273   2689    175   -341    154       N
ATOM    126  CA  LEU A  17      -6.068  -5.407   8.818  1.00 29.62           C
ANISOU  126  CA  LEU A  17     4183   3834   3238    219   -310    163       C
ATOM    127  C   LEU A  17      -6.411  -5.947  10.204  1.00 30.39           C
ANISOU  127  C   LEU A  17     4257   3954   3336    231   -322    169       C
ATOM    128  O   LEU A  17      -6.700  -7.142  10.359  1.00 26.85           O
ANISOU  128  O   LEU A  17     3873   3472   2855    233   -316    181       O
ATOM    129  CB  LEU A  17      -4.552  -5.265   8.647  1.00 27.17           C
ANISOU  129  CB  LEU A  17     3852   3539   2934    277   -267    156       C
ATOM    130  CG  LEU A  17      -4.098  -5.053   7.198  1.00 29.70           C
ANISOU  130  CG  LEU A  17     4222   3821   3243    273   -240    153       C
ATOM    131  CD1 LEU A  17      -2.818  -4.181   7.186  1.00 23.48           C
ANISOU  131  CD1 LEU A  17     3364   3070   2488    310   -207    139       C
ATOM    132  CD2 LEU A  17      -3.853  -6.376   6.462  1.00 23.89           C
ANISOU  132  CD2 LEU A  17     3591   3025   2460    291   -209    165       C
ATOM    133  N   VAL A  18      -6.416  -5.068  11.212  1.00 29.87           N
ANISOU  133  N   VAL A  18     4104   3941   3303    235   -337    160       N
ATOM    134  CA  VAL A  18      -6.787  -5.456  12.574  1.00 28.69           C
ANISOU  134  CA  VAL A  18     3933   3813   3154    243   -348    165       C
ATOM    135  C   VAL A  18      -8.139  -6.184  12.559  1.00 34.05           C
ANISOU  135  C   VAL A  18     4666   4456   3816    194   -366    177       C
ATOM    136  O   VAL A  18      -8.263  -7.323  13.039  1.00 34.52           O
ANISOU  136  O   VAL A  18     4778   4492   3846    206   -355    187       O
ATOM    137  CB  VAL A  18      -6.793  -4.211  13.489  1.00 29.60           C
ANISOU  137  CB  VAL A  18     3955   3985   3308    241   -365    153       C
ATOM    138  CG1 VAL A  18      -7.445  -4.479  14.842  1.00 23.02           C
ANISOU  138  CG1 VAL A  18     3105   3167   2473    236   -378    158       C
ATOM    139  CG2 VAL A  18      -5.340  -3.626  13.663  1.00 24.24           C
ANISOU  139  CG2 VAL A  18     3220   3345   2645    291   -347    141       C
ATOM    140  N   SER A  19      -9.155  -5.574  11.942  1.00 26.22           N
ANISOU  140  N   SER A  19     3666   3455   2842    137   -392    174       N
ATOM    141  CA  SER A  19     -10.474  -6.206  11.923  1.00 32.56           C
ANISOU  141  CA  SER A  19     4508   4227   3636     85   -412    183       C
ATOM    142  C   SER A  19     -10.374  -7.618  11.358  1.00 32.13           C
ANISOU  142  C   SER A  19     4555   4118   3536     88   -395    194       C
ATOM    143  O   SER A  19     -10.989  -8.558  11.872  1.00 35.39           O
ANISOU  143  O   SER A  19     5008   4509   3931     71   -393    202       O
ATOM    144  CB  SER A  19     -11.465  -5.387  11.084  1.00 26.68           C
ANISOU  144  CB  SER A  19     3744   3476   2916     29   -448    180       C
ATOM    145  OG  SER A  19     -11.453  -4.018  11.460  1.00 35.16           O
ANISOU  145  OG  SER A  19     4733   4596   4030     31   -459    170       O
ATOM    146  N   HIS A  20      -9.583  -7.791  10.307  1.00 31.25           N
ANISOU  146  N   HIS A  20     4491   3981   3403    108   -378    193       N
ATOM    147  CA  HIS A  20      -9.547  -9.082   9.634  1.00 33.08           C
ANISOU  147  CA  HIS A  20     4828   4154   3587    107   -360    202       C
ATOM    148  C   HIS A  20      -8.872 -10.166  10.482  1.00 30.17           C
ANISOU  148  C   HIS A  20     4493   3778   3190    160   -326    211       C
ATOM    149  O   HIS A  20      -9.347 -11.305  10.531  1.00 36.51           O
ANISOU  149  O   HIS A  20     5373   4539   3960    144   -319    221       O
ATOM    150  CB  HIS A  20      -8.833  -8.915   8.308  1.00 28.47           C
ANISOU  150  CB  HIS A  20     4287   3543   2987    119   -344    199       C
ATOM    151  CG  HIS A  20      -8.741 -10.172   7.505  1.00 29.84           C
ANISOU  151  CG  HIS A  20     4577   3651   3109    117   -323    208       C
ATOM    152  ND1 HIS A  20      -9.846 -10.784   6.951  1.00 27.06           N
ANISOU  152  ND1 HIS A  20     4294   3254   2734     55   -349    212       N
ATOM    153  CD2 HIS A  20      -7.674 -10.923   7.148  1.00 29.17           C
ANISOU  153  CD2 HIS A  20     4554   3538   2992    170   -276    212       C
ATOM    154  CE1 HIS A  20      -9.461 -11.850   6.275  1.00 29.61           C
ANISOU  154  CE1 HIS A  20     4722   3519   3007     68   -320    219       C
ATOM    155  NE2 HIS A  20      -8.151 -11.968   6.392  1.00 34.68           N
ANISOU  155  NE2 HIS A  20     5363   4170   3644    139   -273    220       N
ATOM    156  N   LEU A  21      -7.772  -9.843  11.148  1.00 31.13           N
ANISOU  156  N   LEU A  21     4564   3940   3325    222   -306    208       N
ATOM    157  CA  LEU A  21      -6.968 -10.846  11.828  1.00 32.05           C
ANISOU  157  CA  LEU A  21     4715   4049   3413    284   -275    217       C
ATOM    158  C   LEU A  21      -7.352 -11.090  13.282  1.00 35.65           C
ANISOU  158  C   LEU A  21     5145   4529   3871    292   -284    222       C
ATOM    159  O   LEU A  21      -6.950 -12.114  13.850  1.00 37.11           O
ANISOU  159  O   LEU A  21     5381   4697   4025    334   -262    233       O
ATOM    160  CB  LEU A  21      -5.501 -10.426  11.768  1.00 34.52           C
ANISOU  160  CB  LEU A  21     4984   4392   3739    352   -251    212       C
ATOM    161  CG  LEU A  21      -5.095  -9.915  10.385  1.00 33.01           C
ANISOU  161  CG  LEU A  21     4805   4185   3554    342   -238    205       C
ATOM    162  CD1 LEU A  21      -3.742  -9.209  10.437  1.00 24.20           C
ANISOU  162  CD1 LEU A  21     3618   3110   2466    399   -217    196       C
ATOM    163  CD2 LEU A  21      -5.108 -11.079   9.404  1.00 32.19           C
ANISOU  163  CD2 LEU A  21     4818   4011   3403    341   -211    216       C
ATOM    164  N   SER A  22      -8.125 -10.197  13.896  1.00 33.06           N
ANISOU  164  N   SER A  22     4747   4237   3578    253   -313    215       N
ATOM    165  CA  SER A  22      -8.284 -10.246  15.346  1.00 35.71           C
ANISOU  165  CA  SER A  22     5050   4600   3916    270   -316    217       C
ATOM    166  C   SER A  22      -8.977 -11.504  15.846  1.00 33.42           C
ANISOU  166  C   SER A  22     4839   4268   3591    255   -304    230       C
ATOM    167  O   SER A  22      -8.761 -11.882  17.003  1.00 38.69           O
ANISOU  167  O   SER A  22     5509   4947   4244    291   -295    235       O
ATOM    168  CB  SER A  22      -9.042  -8.999  15.828  1.00 40.07           C
ANISOU  168  CB  SER A  22     5517   5195   4514    228   -344    206       C
ATOM    169  OG  SER A  22      -9.353  -9.077  17.214  1.00 55.09           O
ANISOU  169  OG  SER A  22     7400   7116   6416    236   -345    209       O
ATOM    170  N   LYS A  23      -9.771 -12.182  15.015  1.00 36.30           N
ANISOU  170  N   LYS A  23     5272   4581   3937    205   -303    235       N
ATOM    171  CA  LYS A  23     -10.377 -13.436  15.464  1.00 37.89           C
ANISOU  171  CA  LYS A  23     5556   4738   4103    189   -286    246       C
ATOM    172  C   LYS A  23      -9.441 -14.625  15.263  1.00 38.02           C
ANISOU  172  C   LYS A  23     5662   4716   4070    247   -252    257       C
ATOM    173  O   LYS A  23      -9.354 -15.497  16.136  1.00 44.36           O
ANISOU  173  O   LYS A  23     6512   5500   4841    276   -232    267       O
ATOM    174  CB  LYS A  23     -11.723 -13.664  14.776  1.00 41.97           C
ANISOU  174  CB  LYS A  23     6104   5219   4625    102   -303    245       C
ATOM    175  CG  LYS A  23     -12.769 -12.631  15.239  1.00 45.74           C
ANISOU  175  CG  LYS A  23     6493   5734   5153     50   -332    238       C
ATOM    176  CD  LYS A  23     -14.139 -12.789  14.599  1.00 47.64           C
ANISOU  176  CD  LYS A  23     6749   5944   5407    -36   -354    237       C
ATOM    177  CE  LYS A  23     -15.092 -11.666  15.014  1.00 45.11           C
ANISOU  177  CE  LYS A  23     6331   5665   5143    -78   -381    230       C
ATOM    178  NZ  LYS A  23     -16.494 -11.993  14.557  1.00 47.99           N
ANISOU  178  NZ  LYS A  23     6709   6000   5524   -161   -402    231       N
ATOM    179  N   ASN A  24      -8.693 -14.673  14.164  1.00 38.13           N
ANISOU  179  N   ASN A  24     5703   4713   4074    270   -242    256       N
ATOM    180  CA  ASN A  24      -7.840 -15.840  13.956  1.00 36.68           C
ANISOU  180  CA  ASN A  24     5608   4487   3842    328   -204    268       C
ATOM    181  C   ASN A  24      -6.447 -15.677  14.552  1.00 39.35           C
ANISOU  181  C   ASN A  24     5903   4865   4185    420   -189    271       C
ATOM    182  O   ASN A  24      -5.686 -16.640  14.569  1.00 37.29           O
ANISOU  182  O   ASN A  24     5706   4574   3887    480   -158    283       O
ATOM    183  CB  ASN A  24      -7.676 -16.113  12.467  1.00 35.83           C
ANISOU  183  CB  ASN A  24     5564   4335   3716    311   -192    268       C
ATOM    184  CG  ASN A  24      -8.923 -16.663  11.837  1.00 41.87           C
ANISOU  184  CG  ASN A  24     6401   5046   4461    228   -204    268       C
ATOM    185  OD1 ASN A  24      -9.645 -17.454  12.442  1.00 46.08           O
ANISOU  185  OD1 ASN A  24     6982   5553   4974    201   -199    274       O
ATOM    186  ND2 ASN A  24      -9.189 -16.249  10.611  1.00 43.85           N
ANISOU  186  ND2 ASN A  24     6663   5280   4718    185   -220    261       N
ATOM    187  N   TYR A  25      -6.132 -14.522  15.128  1.00 41.28           N
ANISOU  187  N   TYR A  25     6039   5173   4471    434   -212    260       N
ATOM    188  CA  TYR A  25      -4.811 -14.277  15.668  1.00 36.97           C
ANISOU  188  CA  TYR A  25     5443   4670   3935    516   -205    260       C
ATOM    189  C   TYR A  25      -4.977 -13.398  16.886  1.00 37.29           C
ANISOU  189  C   TYR A  25     5395   4768   4004    515   -236    252       C
ATOM    190  O   TYR A  25      -6.054 -12.849  17.136  1.00 37.82           O
ANISOU  190  O   TYR A  25     5436   4844   4090    451   -257    246       O
ATOM    191  CB  TYR A  25      -3.891 -13.579  14.663  1.00 33.16           C
ANISOU  191  CB  TYR A  25     4916   4205   3478    538   -197    251       C
ATOM    192  CG  TYR A  25      -3.632 -14.361  13.400  1.00 33.92           C
ANISOU  192  CG  TYR A  25     5100   4242   3545    543   -162    258       C
ATOM    193  CD1 TYR A  25      -2.669 -15.374  13.364  1.00 38.10           C
ANISOU  193  CD1 TYR A  25     5688   4745   4044    617   -125    271       C
ATOM    194  CD2 TYR A  25      -4.314 -14.075  12.235  1.00 33.16           C
ANISOU  194  CD2 TYR A  25     5033   4115   3450    477   -167    252       C
ATOM    195  CE1 TYR A  25      -2.398 -16.088  12.191  1.00 29.83           C
ANISOU  195  CE1 TYR A  25     4728   3639   2967    624    -87    277       C
ATOM    196  CE2 TYR A  25      -4.065 -14.789  11.063  1.00 34.91           C
ANISOU  196  CE2 TYR A  25     5345   4279   3640    481   -134    257       C
ATOM    197  CZ  TYR A  25      -3.104 -15.787  11.048  1.00 36.66           C
ANISOU  197  CZ  TYR A  25     5626   4473   3831    554    -92    270       C
ATOM    198  OH  TYR A  25      -2.874 -16.491   9.880  1.00 42.29           O
ANISOU  198  OH  TYR A  25     6436   5124   4510    557    -55    275       O
ATOM    199  N   THR A  26      -3.914 -13.328  17.665  1.00 32.26           N
ANISOU  199  N   THR A  26     4718   4169   3369    587   -237    254       N
ATOM    200  CA  THR A  26      -3.776 -12.345  18.726  1.00 36.50           C
ANISOU  200  CA  THR A  26     5167   4768   3936    594   -267    243       C
ATOM    201  C   THR A  26      -3.084 -11.139  18.100  1.00 36.47           C
ANISOU  201  C   THR A  26     5072   4807   3977    595   -276    226       C
ATOM    202  O   THR A  26      -1.882 -11.198  17.807  1.00 33.93           O
ANISOU  202  O   THR A  26     4729   4500   3661    653   -264    226       O
ATOM    203  CB  THR A  26      -2.950 -12.902  19.883  1.00 36.38           C
ANISOU  203  CB  THR A  26     5157   4770   3895    671   -270    252       C
ATOM    204  OG1 THR A  26      -3.633 -14.024  20.462  1.00 43.58           O
ANISOU  204  OG1 THR A  26     6162   5635   4761    668   -257    268       O
ATOM    205  CG2 THR A  26      -2.739 -11.838  20.940  1.00 34.90           C
ANISOU  205  CG2 THR A  26     4880   4646   3736    677   -304    239       C
ATOM    206  N   VAL A  27      -3.837 -10.057  17.898  1.00 27.47           N
ANISOU  206  N   VAL A  27     3881   3687   2871    531   -295    213       N
ATOM    207  CA  VAL A  27      -3.384  -8.879  17.166  1.00 32.46           C
ANISOU  207  CA  VAL A  27     4441   4351   3544    518   -300    197       C
ATOM    208  C   VAL A  27      -3.120  -7.737  18.141  1.00 30.94           C
ANISOU  208  C   VAL A  27     4154   4219   3382    522   -327    182       C
ATOM    209  O   VAL A  27      -4.048  -7.232  18.781  1.00 33.88           O
ANISOU  209  O   VAL A  27     4507   4602   3763    479   -346    178       O
ATOM    210  CB  VAL A  27      -4.428  -8.442  16.130  1.00 35.43           C
ANISOU  210  CB  VAL A  27     4832   4699   3932    444   -304    193       C
ATOM    211  CG1 VAL A  27      -3.954  -7.185  15.400  1.00 32.25           C
ANISOU  211  CG1 VAL A  27     4360   4325   3568    431   -307    176       C
ATOM    212  CG2 VAL A  27      -4.755  -9.585  15.184  1.00 32.60           C
ANISOU  212  CG2 VAL A  27     4573   4277   3538    432   -282    206       C
ATOM    213  N   VAL A  28      -1.888  -7.254  18.172  1.00 29.21           N
ANISOU  213  N   VAL A  28     3875   4040   3185    567   -327    173       N
ATOM    214  CA  VAL A  28      -1.512  -6.114  18.994  1.00 29.63           C
ANISOU  214  CA  VAL A  28     3839   4151   3268    568   -353    156       C
ATOM    215  C   VAL A  28      -1.139  -4.972  18.079  1.00 33.22           C
ANISOU  215  C   VAL A  28     4234   4625   3763    543   -347    139       C
ATOM    216  O   VAL A  28      -0.177  -5.075  17.306  1.00 33.60           O
ANISOU  216  O   VAL A  28     4273   4673   3821    574   -325    137       O
ATOM    217  CB  VAL A  28      -0.362  -6.434  19.945  1.00 36.28           C
ANISOU  217  CB  VAL A  28     4653   5029   4102    640   -365    157       C
ATOM    218  CG1 VAL A  28      -0.123  -5.249  20.857  1.00 34.26           C
ANISOU  218  CG1 VAL A  28     4314   4830   3873    631   -397    138       C
ATOM    219  CG2 VAL A  28      -0.718  -7.680  20.739  1.00 35.30           C
ANISOU  219  CG2 VAL A  28     4606   4876   3932    670   -365    177       C
ATOM    220  N   ALA A  29      -1.940  -3.902  18.146  1.00 33.21           N
ANISOU  220  N   ALA A  29     4197   4638   3784    487   -363    127       N
ATOM    221  CA  ALA A  29      -1.821  -2.723  17.311  1.00 31.96           C
ANISOU  221  CA  ALA A  29     3991   4491   3660    453   -359    111       C
ATOM    222  C   ALA A  29      -1.665  -1.509  18.219  1.00 34.45           C
ANISOU  222  C   ALA A  29     4228   4859   4003    441   -382     93       C
ATOM    223  O   ALA A  29      -2.643  -0.808  18.513  1.00 34.93           O
ANISOU  223  O   ALA A  29     4277   4921   4072    396   -396     89       O
ATOM    224  CB  ALA A  29      -3.034  -2.596  16.400  1.00 29.57           C
ANISOU  224  CB  ALA A  29     3730   4148   3356    394   -356    116       C
ATOM    225  N   PRO A  30      -0.453  -1.233  18.676  1.00 35.42           N
ANISOU  225  N   PRO A  30     4296   5023   4140    482   -386     82       N
ATOM    226  CA  PRO A  30      -0.217  -0.071  19.543  1.00 38.00           C
ANISOU  226  CA  PRO A  30     4551   5398   4490    469   -410     62       C
ATOM    227  C   PRO A  30      -0.463   1.244  18.814  1.00 39.29           C
ANISOU  227  C   PRO A  30     4677   5566   4686    418   -402     46       C
ATOM    228  O   PRO A  30      -0.332   1.343  17.594  1.00 34.21           O
ANISOU  228  O   PRO A  30     4046   4899   4053    406   -376     45       O
ATOM    229  CB  PRO A  30       1.262  -0.211  19.920  1.00 42.03           C
ANISOU  229  CB  PRO A  30     5012   5947   5010    524   -415     54       C
ATOM    230  CG  PRO A  30       1.865  -0.995  18.742  1.00 37.66           C
ANISOU  230  CG  PRO A  30     4488   5364   4456    554   -379     64       C
ATOM    231  CD  PRO A  30       0.779  -1.986  18.387  1.00 34.33           C
ANISOU  231  CD  PRO A  30     4157   4888   3999    541   -369     86       C
ATOM    232  N   THR A  31      -0.738   2.287  19.598  1.00 46.46           N
ANISOU  232  N   THR A  31     5542   6504   5608    391   -421     31       N
ATOM    233  CA  THR A  31      -0.888   3.645  19.075  1.00 48.89           C
ANISOU  233  CA  THR A  31     5812   6819   5946    347   -415     14       C
ATOM    234  C   THR A  31       0.463   4.356  19.048  1.00 48.28           C
ANISOU  234  C   THR A  31     5667   6781   5896    361   -410     -8       C
ATOM    235  O   THR A  31       1.469   3.848  19.563  1.00 49.09           O
ANISOU  235  O   THR A  31     5745   6911   5997    405   -419    -10       O
ATOM    236  CB  THR A  31      -1.854   4.469  19.934  1.00 46.82           C
ANISOU  236  CB  THR A  31     5538   6566   5685    311   -433      9       C
ATOM    237  OG1 THR A  31      -1.168   4.890  21.130  1.00 45.99           O
ANISOU  237  OG1 THR A  31     5388   6505   5582    327   -455     -7       O
ATOM    238  CG2 THR A  31      -3.144   3.660  20.287  1.00 43.65           C
ANISOU  238  CG2 THR A  31     5193   6132   5258    302   -439     30       C
ATOM    239  N   HIS A  32       0.475   5.559  18.452  1.00 45.84           N
ANISOU  239  N   HIS A  32     5329   6475   5614    322   -396    -25       N
ATOM    240  CA  HIS A  32       1.714   6.338  18.400  1.00 48.73           C
ANISOU  240  CA  HIS A  32     5629   6877   6010    326   -388    -48       C
ATOM    241  C   HIS A  32       2.197   6.654  19.806  1.00 46.90           C
ANISOU  241  C   HIS A  32     5348   6693   5779    337   -422    -62       C
ATOM    242  O   HIS A  32       3.400   6.567  20.093  1.00 48.67           O
ANISOU  242  O   HIS A  32     5523   6952   6018    366   -429    -74       O
ATOM    243  CB  HIS A  32       1.528   7.626  17.576  1.00 53.71           C
ANISOU  243  CB  HIS A  32     6246   7496   6664    277   -365    -64       C
ATOM    244  CG  HIS A  32       2.644   8.626  17.738  1.00 59.70           C
ANISOU  244  CG  HIS A  32     6935   8294   7455    268   -358    -92       C
ATOM    245  ND1 HIS A  32       3.978   8.298  17.584  1.00 61.50           N
ANISOU  245  ND1 HIS A  32     7118   8546   7702    299   -346   -100       N
ATOM    246  CD2 HIS A  32       2.620   9.944  18.062  1.00 61.84           C
ANISOU  246  CD2 HIS A  32     7170   8582   7742    228   -362   -113       C
ATOM    247  CE1 HIS A  32       4.725   9.368  17.805  1.00 60.31           C
ANISOU  247  CE1 HIS A  32     6905   8428   7581    276   -343   -127       C
ATOM    248  NE2 HIS A  32       3.926  10.379  18.099  1.00 62.00           N
ANISOU  248  NE2 HIS A  32     7128   8638   7793    232   -352   -136       N
ATOM    249  N   GLY A  33       1.262   6.938  20.720  1.00 54.95           N
ANISOU  249  N   GLY A  33     6385   7713   6781    318   -446    -60       N
ATOM    250  CA  GLY A  33       1.637   7.161  22.106  1.00 52.11           C
ANISOU  250  CA  GLY A  33     5993   7392   6413    329   -481    -71       C
ATOM    251  C   GLY A  33       2.129   5.915  22.817  1.00 53.74           C
ANISOU  251  C   GLY A  33     6214   7612   6595    385   -504    -58       C
ATOM    252  O   GLY A  33       2.959   6.010  23.725  1.00 57.76           O
ANISOU  252  O   GLY A  33     6683   8160   7103    407   -534    -70       O
ATOM    253  N   GLU A  34       1.591   4.737  22.465  1.00 55.09           N
ANISOU  253  N   GLU A  34     6443   7746   6741    408   -492    -32       N
ATOM    254  CA  GLU A  34       2.077   3.509  23.095  1.00 53.87           C
ANISOU  254  CA  GLU A  34     6309   7597   6560    465   -510    -18       C
ATOM    255  C   GLU A  34       3.459   3.109  22.588  1.00 56.35           C
ANISOU  255  C   GLU A  34     6583   7933   6895    510   -503    -21       C
ATOM    256  O   GLU A  34       4.227   2.478  23.329  1.00 62.45           O
ANISOU  256  O   GLU A  34     7341   8730   7655    560   -529    -18       O
ATOM    257  CB  GLU A  34       1.136   2.329  22.860  1.00 52.89           C
ANISOU  257  CB  GLU A  34     6265   7426   6404    476   -496     10       C
ATOM    258  CG  GLU A  34      -0.347   2.598  22.949  1.00 53.34           C
ANISOU  258  CG  GLU A  34     6363   7452   6451    428   -490     17       C
ATOM    259  CD  GLU A  34      -1.145   1.304  22.985  1.00 54.65           C
ANISOU  259  CD  GLU A  34     6604   7576   6582    442   -482     43       C
ATOM    260  OE1 GLU A  34      -0.623   0.325  23.547  1.00 62.42           O
ANISOU  260  OE1 GLU A  34     7612   8563   7541    491   -492     53       O
ATOM    261  OE2 GLU A  34      -2.222   1.224  22.357  1.00 53.57           O
ANISOU  261  OE2 GLU A  34     6504   7403   6446    405   -465     53       O
ATOM    262  N   LEU A  35       3.761   3.387  21.313  1.00 51.92           N
ANISOU  262  N   LEU A  35     6008   7358   6363    495   -466    -26       N
ATOM    263  CA  LEU A  35       5.006   2.914  20.696  1.00 49.30           C
ANISOU  263  CA  LEU A  35     5643   7037   6052    538   -447    -27       C
ATOM    264  C   LEU A  35       5.438   3.947  19.661  1.00 49.76           C
ANISOU  264  C   LEU A  35     5657   7098   6151    501   -413    -46       C
ATOM    265  O   LEU A  35       4.825   4.048  18.593  1.00 46.57           O
ANISOU  265  O   LEU A  35     5295   6652   5746    472   -379    -40       O
ATOM    266  CB  LEU A  35       4.812   1.544  20.057  1.00 47.46           C
ANISOU  266  CB  LEU A  35     5478   6760   5793    576   -422      0       C
ATOM    267  CG  LEU A  35       6.016   0.718  19.614  1.00 49.62           C
ANISOU  267  CG  LEU A  35     5734   7040   6079    638   -402      7       C
ATOM    268  CD1 LEU A  35       5.511  -0.649  19.259  1.00 46.61           C
ANISOU  268  CD1 LEU A  35     5443   6609   5659    669   -384     35       C
ATOM    269  CD2 LEU A  35       6.732   1.312  18.425  1.00 48.58           C
ANISOU  269  CD2 LEU A  35     5563   6907   5989    623   -358     -7       C
ATOM    270  N   ASP A  36       6.452   4.733  19.985  1.00 49.69           N
ANISOU  270  N   ASP A  36     5567   7136   6176    498   -423    -70       N
ATOM    271  CA  ASP A  36       6.957   5.692  19.019  1.00 50.00           C
ANISOU  271  CA  ASP A  36     5566   7177   6256    463   -385    -90       C
ATOM    272  C   ASP A  36       8.049   5.022  18.201  1.00 52.70           C
ANISOU  272  C   ASP A  36     5885   7517   6620    507   -348    -86       C
ATOM    273  O   ASP A  36       9.100   4.659  18.746  1.00 53.57           O
ANISOU  273  O   ASP A  36     5937   7667   6748    551   -366    -90       O
ATOM    274  CB  ASP A  36       7.497   6.947  19.676  1.00 53.45           C
ANISOU  274  CB  ASP A  36     5926   7660   6721    429   -407   -121       C
ATOM    275  CG  ASP A  36       8.336   7.731  18.723  1.00 58.86           C
ANISOU  275  CG  ASP A  36     6562   8352   7452    404   -364   -141       C
ATOM    276  OD1 ASP A  36       7.759   8.319  17.781  1.00 60.29           O
ANISOU  276  OD1 ASP A  36     6778   8495   7635    363   -326   -143       O
ATOM    277  OD2 ASP A  36       9.571   7.725  18.882  1.00 59.96           O
ANISOU  277  OD2 ASP A  36     6627   8531   7625    428   -365   -155       O
ATOM    278  N   LEU A  37       7.815   4.878  16.892  1.00 52.62           N
ANISOU  278  N   LEU A  37     5921   7460   6612    495   -297    -78       N
ATOM    279  CA  LEU A  37       8.723   4.079  16.067  1.00 54.84           C
ANISOU  279  CA  LEU A  37     6201   7729   6908    541   -253    -69       C
ATOM    280  C   LEU A  37      10.097   4.721  15.870  1.00 60.55           C
ANISOU  280  C   LEU A  37     6828   8491   7687    545   -230    -93       C
ATOM    281  O   LEU A  37      11.058   4.004  15.546  1.00 59.44           O
ANISOU  281  O   LEU A  37     6662   8356   7566    596   -203    -87       O
ATOM    282  CB  LEU A  37       8.086   3.812  14.709  1.00 53.62           C
ANISOU  282  CB  LEU A  37     6129   7510   6736    523   -204    -55       C
ATOM    283  CG  LEU A  37       6.697   3.160  14.660  1.00 49.10           C
ANISOU  283  CG  LEU A  37     5653   6891   6113    512   -221    -32       C
ATOM    284  CD1 LEU A  37       6.119   3.418  13.293  1.00 41.96           C
ANISOU  284  CD1 LEU A  37     4811   5931   5199    475   -180    -29       C
ATOM    285  CD2 LEU A  37       6.735   1.667  14.927  1.00 37.71           C
ANISOU  285  CD2 LEU A  37     4257   5433   4640    571   -227     -7       C
ATOM    286  N   THR A  38      10.216   6.038  16.099  1.00 60.39           N
ANISOU  286  N   THR A  38     6753   8499   7693    492   -238   -121       N
ATOM    287  CA  THR A  38      11.477   6.767  15.981  1.00 59.28           C
ANISOU  287  CA  THR A  38     6518   8399   7609    483   -217   -147       C
ATOM    288  C   THR A  38      12.419   6.557  17.164  1.00 61.89           C
ANISOU  288  C   THR A  38     6761   8794   7960    522   -268   -157       C
ATOM    289  O   THR A  38      13.549   7.054  17.114  1.00 63.90           O
ANISOU  289  O   THR A  38     6926   9087   8266    519   -255   -179       O
ATOM    290  CB  THR A  38      11.207   8.257  15.772  1.00 56.01           C
ANISOU  290  CB  THR A  38     6087   7985   7211    409   -206   -173       C
ATOM    291  OG1 THR A  38      10.279   8.716  16.760  1.00 59.55           O
ANISOU  291  OG1 THR A  38     6555   8443   7629    380   -260   -175       O
ATOM    292  CG2 THR A  38      10.625   8.501  14.411  1.00 58.15           C
ANISOU  292  CG2 THR A  38     6429   8193   7470    378   -147   -167       C
ATOM    293  N   ASP A  39      11.998   5.827  18.208  1.00 63.23           N
ANISOU  293  N   ASP A  39     6956   8976   8093    557   -325   -140       N
ATOM    294  CA  ASP A  39      12.842   5.532  19.376  1.00 66.65           C
ANISOU  294  CA  ASP A  39     7318   9468   8537    600   -382   -146       C
ATOM    295  C   ASP A  39      13.404   4.116  19.277  1.00 67.04           C
ANISOU  295  C   ASP A  39     7376   9513   8582    684   -376   -120       C
ATOM    296  O   ASP A  39      12.694   3.135  19.535  1.00 64.69           O
ANISOU  296  O   ASP A  39     7158   9185   8235    719   -390    -93       O
ATOM    297  CB  ASP A  39      12.070   5.699  20.678  1.00 64.41           C
ANISOU  297  CB  ASP A  39     7062   9200   8212    587   -450   -145       C
ATOM    298  CG  ASP A  39      12.981   5.838  21.881  1.00 66.65           C
ANISOU  298  CG  ASP A  39     7264   9549   8512    610   -514   -161       C
ATOM    299  OD1 ASP A  39      13.124   4.857  22.644  1.00 68.16           O
ANISOU  299  OD1 ASP A  39     7469   9753   8676    671   -556   -142       O
ATOM    300  OD2 ASP A  39      13.540   6.942  22.080  1.00 71.93           O
ANISOU  300  OD2 ASP A  39     7859  10255   9216    565   -524   -192       O
ATOM    301  N   ARG A  40      14.695   4.019  18.936  1.00 77.16           N
ANISOU  301  N   ARG A  40     8575  10825   9916    718   -352   -129       N
ATOM    302  CA  ARG A  40      15.332   2.718  18.750  1.00 78.61           C
ANISOU  302  CA  ARG A  40     8763  11004  10102    802   -337   -105       C
ATOM    303  C   ARG A  40      15.194   1.869  20.007  1.00 81.39           C
ANISOU  303  C   ARG A  40     9133  11377  10414    858   -409    -87       C
ATOM    304  O   ARG A  40      14.778   0.703  19.939  1.00 81.09           O
ANISOU  304  O   ARG A  40     9175  11302  10335    909   -401    -57       O
ATOM    305  CB  ARG A  40      16.805   2.902  18.339  1.00 80.67           C
ANISOU  305  CB  ARG A  40     8912  11304  10436    827   -306   -121       C
ATOM    306  CG  ARG A  40      17.728   1.653  18.509  1.00 82.14           C
ANISOU  306  CG  ARG A  40     9067  11507  10636    926   -309   -100       C
ATOM    307  CD  ARG A  40      18.938   1.695  17.563  1.00 86.82           C
ANISOU  307  CD  ARG A  40     9580  12109  11298    948   -239   -109       C
ATOM    308  NE  ARG A  40      19.895   0.607  17.729  1.00 88.10           N
ANISOU  308  NE  ARG A  40     9699  12292  11483   1045   -240    -90       N
ATOM    309  CZ  ARG A  40      21.205   0.754  17.729  1.00 89.91           C
ANISOU  309  CZ  ARG A  40     9805  12572  11785   1075   -232   -104       C
ATOM    310  NH1 ARG A  40      21.755   1.941  17.464  1.00 94.70           N
ANISOU  310  NH1 ARG A  40    10320  13211  12451   1011   -213   -138       N
ATOM    311  NH2 ARG A  40      21.973  -0.315  17.824  1.00 94.01           N
ANISOU  311  NH2 ARG A  40    10297  13103  12320   1170   -229    -82       N
ATOM    312  N   GLU A  41      15.456   2.457  21.175  1.00 77.39           N
ANISOU  312  N   GLU A  41     8567  10926   9913    845   -479   -105       N
ATOM    313  CA  GLU A  41      15.358   1.700  22.420  1.00 72.01           C
ANISOU  313  CA  GLU A  41     7908  10264   9190    899   -549    -89       C
ATOM    314  C   GLU A  41      13.924   1.241  22.717  1.00 69.35           C
ANISOU  314  C   GLU A  41     7694   9876   8781    886   -558    -68       C
ATOM    315  O   GLU A  41      13.685   0.064  23.007  1.00 66.91           O
ANISOU  315  O   GLU A  41     7449   9543   8431    945   -567    -40       O
ATOM    316  CB  GLU A  41      15.921   2.557  23.565  1.00 80.67           C
ANISOU  316  CB  GLU A  41     8918  11427  10304    878   -623   -117       C
ATOM    317  N   LYS A  42      12.951   2.151  22.630  1.00 66.14           N
ANISOU  317  N   LYS A  42     7322   9449   8360    808   -551    -80       N
ATOM    318  CA  LYS A  42      11.601   1.793  23.056  1.00 63.24           C
ANISOU  318  CA  LYS A  42     7057   9040   7931    793   -564    -62       C
ATOM    319  C   LYS A  42      11.037   0.664  22.209  1.00 61.36           C
ANISOU  319  C   LYS A  42     6908   8741   7665    823   -515    -33       C
ATOM    320  O   LYS A  42      10.350  -0.224  22.732  1.00 58.79           O
ANISOU  320  O   LYS A  42     6660   8389   7289    850   -533    -10       O
ATOM    321  CB  LYS A  42      10.664   2.998  23.016  1.00 59.85           C
ANISOU  321  CB  LYS A  42     6643   8600   7499    708   -559    -81       C
ATOM    322  N   ILE A  43      11.304   0.677  20.901  1.00 61.63           N
ANISOU  322  N   ILE A  43     6939   8750   7729    815   -453    -33       N
ATOM    323  CA  ILE A  43      10.688  -0.345  20.072  1.00 57.56           C
ANISOU  323  CA  ILE A  43     6517   8172   7182    835   -408     -6       C
ATOM    324  C   ILE A  43      11.368  -1.689  20.295  1.00 56.98           C
ANISOU  324  C   ILE A  43     6458   8096   7094    924   -411     17       C
ATOM    325  O   ILE A  43      10.701  -2.730  20.321  1.00 55.88           O
ANISOU  325  O   ILE A  43     6411   7913   6907    950   -405     43       O
ATOM    326  CB  ILE A  43      10.666   0.056  18.590  1.00 55.34           C
ANISOU  326  CB  ILE A  43     6246   7855   6926    798   -341    -12       C
ATOM    327  CG1 ILE A  43      12.014  -0.142  17.941  1.00 59.37           C
ANISOU  327  CG1 ILE A  43     6692   8382   7484    842   -301    -16       C
ATOM    328  CG2 ILE A  43      10.244   1.489  18.413  1.00 57.46           C
ANISOU  328  CG2 ILE A  43     6484   8133   7215    718   -340    -37       C
ATOM    329  CD1 ILE A  43      11.842  -0.252  16.492  1.00 55.27           C
ANISOU  329  CD1 ILE A  43     6223   7808   6968    825   -229    -10       C
ATOM    330  N   ILE A  44      12.694  -1.701  20.483  1.00 57.86           N
ANISOU  330  N   ILE A  44     6479   8256   7249    973   -420      9       N
ATOM    331  CA  ILE A  44      13.356  -2.971  20.769  1.00 55.69           C
ANISOU  331  CA  ILE A  44     6216   7982   6962   1066   -426     33       C
ATOM    332  C   ILE A  44      12.754  -3.575  22.023  1.00 58.33           C
ANISOU  332  C   ILE A  44     6609   8317   7239   1091   -486     49       C
ATOM    333  O   ILE A  44      12.457  -4.776  22.072  1.00 57.36           O
ANISOU  333  O   ILE A  44     6569   8153   7072   1142   -477     76       O
ATOM    334  CB  ILE A  44      14.881  -2.795  20.906  1.00 58.05           C
ANISOU  334  CB  ILE A  44     6393   8341   7321   1114   -436     20       C
ATOM    335  CG1 ILE A  44      15.515  -2.359  19.585  1.00 59.45           C
ANISOU  335  CG1 ILE A  44     6524   8510   7556   1096   -362      8       C
ATOM    336  CG2 ILE A  44      15.548  -4.090  21.428  1.00 51.29           C
ANISOU  336  CG2 ILE A  44     5546   7492   6450   1218   -457     46       C
ATOM    337  CD1 ILE A  44      15.535  -3.404  18.514  1.00 53.45           C
ANISOU  337  CD1 ILE A  44     5835   7690   6784   1140   -291     32       C
ATOM    338  N   SER A  45      12.514  -2.741  23.039  1.00 55.33           N
ANISOU  338  N   SER A  45     6195   7975   6854   1053   -544     31       N
ATOM    339  CA  SER A  45      11.930  -3.260  24.267  1.00 57.38           C
ANISOU  339  CA  SER A  45     6514   8231   7055   1074   -598     44       C
ATOM    340  C   SER A  45      10.548  -3.821  23.998  1.00 58.40           C
ANISOU  340  C   SER A  45     6764   8293   7132   1046   -568     64       C
ATOM    341  O   SER A  45      10.255  -4.979  24.322  1.00 58.00           O
ANISOU  341  O   SER A  45     6792   8210   7034   1095   -570     90       O
ATOM    342  CB  SER A  45      11.817  -2.155  25.318  1.00 56.86           C
ANISOU  342  CB  SER A  45     6400   8212   6991   1028   -658     20       C
ATOM    343  OG  SER A  45      13.010  -1.425  25.469  1.00 61.31           O
ANISOU  343  OG  SER A  45     6847   8838   7609   1033   -685     -4       O
ATOM    344  N   GLU A  46       9.704  -3.022  23.341  1.00 60.30           N
ANISOU  344  N   GLU A  46     7018   8511   7381    967   -538     52       N
ATOM    345  CA  GLU A  46       8.303  -3.384  23.180  1.00 55.82           C
ANISOU  345  CA  GLU A  46     6553   7887   6769    929   -519     67       C
ATOM    346  C   GLU A  46       8.125  -4.548  22.214  1.00 51.23           C
ANISOU  346  C   GLU A  46     6049   7248   6169    959   -468     91       C
ATOM    347  O   GLU A  46       7.293  -5.430  22.456  1.00 50.56           O
ANISOU  347  O   GLU A  46     6056   7120   6035    967   -465    112       O
ATOM    348  CB  GLU A  46       7.514  -2.161  22.726  1.00 54.66           C
ANISOU  348  CB  GLU A  46     6392   7734   6641    841   -505     47       C
ATOM    349  CG  GLU A  46       7.305  -1.111  23.819  1.00 60.28           C
ANISOU  349  CG  GLU A  46     7061   8487   7354    803   -554     27       C
ATOM    350  CD  GLU A  46       6.011  -1.312  24.615  1.00 67.41           C
ANISOU  350  CD  GLU A  46     8041   9361   8209    777   -571     38       C
ATOM    351  OE1 GLU A  46       5.592  -0.359  25.316  1.00 65.11           O
ANISOU  351  OE1 GLU A  46     7730   9091   7919    733   -596     22       O
ATOM    352  OE2 GLU A  46       5.418  -2.416  24.545  1.00 65.27           O
ANISOU  352  OE2 GLU A  46     7852   9046   7900    800   -555     63       O
ATOM    353  N   VAL A  47       8.892  -4.574  21.119  1.00 55.93           N
ANISOU  353  N   VAL A  47     6611   7839   6800    976   -424     89       N
ATOM    354  CA  VAL A  47       8.757  -5.671  20.165  1.00 53.54           C
ANISOU  354  CA  VAL A  47     6388   7478   6476   1004   -372    111       C
ATOM    355  C   VAL A  47       9.164  -6.985  20.821  1.00 55.33           C
ANISOU  355  C   VAL A  47     6658   7696   6668   1089   -385    136       C
ATOM    356  O   VAL A  47       8.473  -8.008  20.680  1.00 53.38           O
ANISOU  356  O   VAL A  47     6514   7393   6373   1101   -366    158       O
ATOM    357  CB  VAL A  47       9.572  -5.392  18.886  1.00 50.65           C
ANISOU  357  CB  VAL A  47     5981   7109   6157   1007   -317    103       C
ATOM    358  CG1 VAL A  47       9.660  -6.667  18.019  1.00 47.69           C
ANISOU  358  CG1 VAL A  47     5689   6674   5757   1054   -264    127       C
ATOM    359  CG2 VAL A  47       8.998  -4.233  18.114  1.00 29.32           C
ANISOU  359  CG2 VAL A  47     3265   4399   3478    923   -298     83       C
ATOM    360  N   THR A  48      10.270  -6.970  21.588  1.00 52.86           N
ANISOU  360  N   THR A  48     6270   7438   6378   1149   -422    132       N
ATOM    361  CA  THR A  48      10.674  -8.166  22.328  1.00 52.87           C
ANISOU  361  CA  THR A  48     6310   7434   6343   1236   -443    156       C
ATOM    362  C   THR A  48       9.677  -8.520  23.421  1.00 54.52           C
ANISOU  362  C   THR A  48     6597   7626   6492   1224   -482    166       C
ATOM    363  O   THR A  48       9.577  -9.699  23.788  1.00 53.95           O
ANISOU  363  O   THR A  48     6604   7520   6373   1280   -481    191       O
ATOM    364  CB  THR A  48      12.109  -8.033  22.883  1.00 59.61           C
ANISOU  364  CB  THR A  48     7058   8354   7237   1305   -479    149       C
ATOM    365  OG1 THR A  48      12.269  -6.821  23.639  1.00 62.96           O
ANISOU  365  OG1 THR A  48     7395   8839   7688   1262   -534    122       O
ATOM    366  CG2 THR A  48      13.203  -8.263  21.826  1.00 56.46           C
ANISOU  366  CG2 THR A  48     6608   7958   6889   1350   -426    151       C
ATOM    367  N   LYS A  49       8.945  -7.530  23.957  1.00 52.30           N
ANISOU  367  N   LYS A  49     6298   7364   6211   1153   -513    148       N
ATOM    368  CA  LYS A  49       7.885  -7.824  24.930  1.00 52.32           C
ANISOU  368  CA  LYS A  49     6378   7343   6157   1133   -539    158       C
ATOM    369  C   LYS A  49       6.663  -8.419  24.239  1.00 47.67           C
ANISOU  369  C   LYS A  49     5893   6684   5536   1091   -492    172       C
ATOM    370  O   LYS A  49       6.125  -9.442  24.683  1.00 46.38           O
ANISOU  370  O   LYS A  49     5823   6480   5321   1115   -489    194       O
ATOM    371  CB  LYS A  49       7.479  -6.568  25.705  1.00 51.15           C
ANISOU  371  CB  LYS A  49     6180   7235   6020   1072   -581    134       C
ATOM    372  N   ILE A  50       6.197  -7.786  23.157  1.00 46.17           N
ANISOU  372  N   ILE A  50     5691   6478   5375   1026   -457    161       N
ATOM    373  CA  ILE A  50       5.047  -8.349  22.453  1.00 46.40           C
ANISOU  373  CA  ILE A  50     5814   6441   5374    984   -418    174       C
ATOM    374  C   ILE A  50       5.388  -9.707  21.850  1.00 44.20           C
ANISOU  374  C   ILE A  50     5609   6115   5069   1042   -380    198       C
ATOM    375  O   ILE A  50       4.524 -10.588  21.781  1.00 40.79           O
ANISOU  375  O   ILE A  50     5277   5629   4594   1031   -361    215       O
ATOM    376  CB  ILE A  50       4.506  -7.375  21.389  1.00 44.80           C
ANISOU  376  CB  ILE A  50     5585   6231   5207    906   -394    158       C
ATOM    377  CG1 ILE A  50       3.950  -6.129  22.035  1.00 39.02           C
ANISOU  377  CG1 ILE A  50     4801   5535   4492    847   -428    138       C
ATOM    378  CG2 ILE A  50       3.408  -8.009  20.549  1.00 44.03           C
ANISOU  378  CG2 ILE A  50     5582   6066   5080    866   -359    171       C
ATOM    379  CD1 ILE A  50       3.641  -5.076  21.020  1.00 41.01           C
ANISOU  379  CD1 ILE A  50     5016   5786   4781    782   -407    121       C
ATOM    380  N   ASN A  51       6.637  -9.904  21.430  1.00 45.34           N
ANISOU  380  N   ASN A  51     5708   6280   5241   1104   -366    199       N
ATOM    381  CA  ASN A  51       7.081 -11.133  20.780  1.00 41.71           C
ANISOU  381  CA  ASN A  51     5313   5775   4761   1165   -323    221       C
ATOM    382  C   ASN A  51       6.112 -11.578  19.682  1.00 41.59           C
ANISOU  382  C   ASN A  51     5392   5689   4721   1113   -275    228       C
ATOM    383  O   ASN A  51       5.397 -12.572  19.840  1.00 42.33           O
ANISOU  383  O   ASN A  51     5588   5732   4765   1116   -264    247       O
ATOM    384  CB  ASN A  51       7.327 -12.256  21.779  1.00 40.43           C
ANISOU  384  CB  ASN A  51     5206   5603   4553   1242   -343    243       C
ATOM    385  CG  ASN A  51       8.307 -13.296  21.238  1.00 46.06           C
ANISOU  385  CG  ASN A  51     5945   6293   5263   1330   -305    262       C
ATOM    386  OD1 ASN A  51       9.423 -12.960  20.801  1.00 43.45           O
ANISOU  386  OD1 ASN A  51     5530   5998   4981   1369   -294    255       O
ATOM    387  ND2 ASN A  51       7.908 -14.565  21.284  1.00 48.41           N
ANISOU  387  ND2 ASN A  51     6358   6530   5505   1363   -282    287       N
ATOM    388  N   PRO A  52       5.970 -10.780  18.622  1.00 39.92           N
ANISOU  388  N   PRO A  52     5150   5474   4543   1057   -250    213       N
ATOM    389  CA  PRO A  52       5.105 -11.170  17.512  1.00 39.32           C
ANISOU  389  CA  PRO A  52     5162   5332   4444   1008   -210    219       C
ATOM    390  C   PRO A  52       5.736 -12.241  16.638  1.00 41.73           C
ANISOU  390  C   PRO A  52     5531   5590   4733   1064   -157    236       C
ATOM    391  O   PRO A  52       6.951 -12.219  16.373  1.00 43.01           O
ANISOU  391  O   PRO A  52     5640   5776   4927   1123   -136    235       O
ATOM    392  CB  PRO A  52       4.958  -9.875  16.726  1.00 38.92           C
ANISOU  392  CB  PRO A  52     5049   5300   4437    942   -206    197       C
ATOM    393  CG  PRO A  52       6.274  -9.192  16.987  1.00 39.56           C
ANISOU  393  CG  PRO A  52     5018   5444   4567    985   -213    183       C
ATOM    394  CD  PRO A  52       6.565  -9.455  18.401  1.00 38.57           C
ANISOU  394  CD  PRO A  52     4866   5358   4430   1033   -260    188       C
ATOM    395  N   GLN A  53       4.901 -13.190  16.187  1.00 34.85           N
ANISOU  395  N   GLN A  53     4778   4650   3814   1044   -133    252       N
ATOM    396  CA  GLN A  53       5.333 -14.061  15.088  1.00 41.15           C
ANISOU  396  CA  GLN A  53     5650   5393   4595   1078    -74    264       C
ATOM    397  C   GLN A  53       5.409 -13.315  13.772  1.00 37.13           C
ANISOU  397  C   GLN A  53     5121   4872   4115   1032    -42    250       C
ATOM    398  O   GLN A  53       6.307 -13.559  12.967  1.00 37.41           O
ANISOU  398  O   GLN A  53     5160   4892   4163   1075      6    252       O
ATOM    399  CB  GLN A  53       4.343 -15.226  14.900  1.00 47.41           C
ANISOU  399  CB  GLN A  53     6580   6110   5325   1056    -58    282       C
ATOM    400  CG  GLN A  53       4.374 -16.517  15.745  1.00 50.26           C
ANISOU  400  CG  GLN A  53     7018   6443   5636   1117    -57    305       C
ATOM    401  CD  GLN A  53       3.931 -16.442  17.212  1.00 47.70           C
ANISOU  401  CD  GLN A  53     6672   6153   5299   1117   -108    307       C
ATOM    402  OE1 GLN A  53       3.502 -15.392  17.688  1.00 48.30           O
ANISOU  402  OE1 GLN A  53     6673   6274   5403   1066   -148    290       O
ATOM    403  NE2 GLN A  53       3.783 -17.656  17.778  1.00 58.48           N
ANISOU  403  NE2 GLN A  53     8131   7477   6612   1160    -99    328       N
ATOM    404  N   ILE A  54       4.483 -12.391  13.543  1.00 38.00           N
ANISOU  404  N   ILE A  54     5214   4989   4236    947    -67    234       N
ATOM    405  CA  ILE A  54       4.408 -11.650  12.297  1.00 37.99           C
ANISOU  405  CA  ILE A  54     5208   4972   4256    897    -41    221       C
ATOM    406  C   ILE A  54       4.266 -10.174  12.631  1.00 38.92           C
ANISOU  406  C   ILE A  54     5220   5150   4420    849    -78    199       C
ATOM    407  O   ILE A  54       3.570  -9.801  13.583  1.00 38.34           O
ANISOU  407  O   ILE A  54     5118   5104   4345    819   -125    195       O
ATOM    408  CB  ILE A  54       3.251 -12.150  11.422  1.00 38.60           C
ANISOU  408  CB  ILE A  54     5399   4978   4290    835    -30    228       C
ATOM    409  CG1 ILE A  54       3.437 -13.624  11.059  1.00 35.57           C
ANISOU  409  CG1 ILE A  54     5128   4531   3857    882     12    249       C
ATOM    410  CG2 ILE A  54       3.080 -11.272  10.172  1.00 39.70           C
ANISOU  410  CG2 ILE A  54     5534   5102   4447    780    -12    214       C
ATOM    411  CD1 ILE A  54       2.501 -14.528  11.779  1.00 37.56           C
ANISOU  411  CD1 ILE A  54     5455   4754   4063    868    -11    263       C
ATOM    412  N   ILE A  55       4.954  -9.337  11.869  1.00 33.87           N
ANISOU  412  N   ILE A  55     4524   4526   3819    843    -52    184       N
ATOM    413  CA  ILE A  55       4.862  -7.896  12.002  1.00 29.56           C
ANISOU  413  CA  ILE A  55     3888   4029   3316    795    -78    162       C
ATOM    414  C   ILE A  55       4.428  -7.353  10.659  1.00 33.04           C
ANISOU  414  C   ILE A  55     4368   4430   3757    737    -51    154       C
ATOM    415  O   ILE A  55       5.101  -7.583   9.641  1.00 32.84           O
ANISOU  415  O   ILE A  55     4371   4373   3733    759      2    155       O
ATOM    416  CB  ILE A  55       6.194  -7.276  12.418  1.00 32.58           C
ANISOU  416  CB  ILE A  55     4157   4473   3749    840    -74    148       C
ATOM    417  CG1 ILE A  55       6.553  -7.717  13.834  1.00 32.86           C
ANISOU  417  CG1 ILE A  55     4152   4551   3781    894   -114    155       C
ATOM    418  CG2 ILE A  55       6.111  -5.750  12.286  1.00 32.80           C
ANISOU  418  CG2 ILE A  55     4106   4539   3819    782    -88    124       C
ATOM    419  CD1 ILE A  55       8.055  -7.594  14.164  1.00 27.04           C
ANISOU  419  CD1 ILE A  55     3321   3866   3089    962   -105    149       C
ATOM    420  N   ILE A  56       3.305  -6.649  10.641  1.00 30.62           N
ANISOU  420  N   ILE A  56     4065   4121   3446    667    -86    147       N
ATOM    421  CA  ILE A  56       2.821  -6.016   9.426  1.00 26.84           C
ANISOU  421  CA  ILE A  56     3622   3609   2968    610    -70    139       C
ATOM    422  C   ILE A  56       3.032  -4.525   9.613  1.00 26.58           C
ANISOU  422  C   ILE A  56     3491   3627   2982    581    -85    118       C
ATOM    423  O   ILE A  56       2.409  -3.914  10.495  1.00 30.10           O
ANISOU  423  O   ILE A  56     3890   4109   3439    551   -131    111       O
ATOM    424  CB  ILE A  56       1.353  -6.363   9.147  1.00 28.21           C
ANISOU  424  CB  ILE A  56     3878   3737   3102    553    -99    149       C
ATOM    425  CG1 ILE A  56       1.124  -7.854   9.293  1.00 29.56           C
ANISOU  425  CG1 ILE A  56     4137   3866   3228    581    -90    169       C
ATOM    426  CG2 ILE A  56       0.968  -5.915   7.742  1.00 26.99           C
ANISOU  426  CG2 ILE A  56     3777   3539   2939    505    -81    144       C
ATOM    427  CD1 ILE A  56      -0.321  -8.239   8.995  1.00 28.22           C
ANISOU  427  CD1 ILE A  56     4048   3651   3022    519   -118    177       C
ATOM    428  N   HIS A  57       3.966  -3.964   8.872  1.00 24.90           N
ANISOU  428  N   HIS A  57     3246   3417   2796    591    -43    106       N
ATOM    429  CA  HIS A  57       4.336  -2.552   9.012  1.00 25.85           C
ANISOU  429  CA  HIS A  57     3275   3585   2963    565    -49     83       C
ATOM    430  C   HIS A  57       3.665  -1.722   7.924  1.00 27.98           C
ANISOU  430  C   HIS A  57     3584   3820   3228    504    -40     76       C
ATOM    431  O   HIS A  57       4.098  -1.690   6.762  1.00 29.62           O
ANISOU  431  O   HIS A  57     3833   3989   3432    504      9     74       O
ATOM    432  CB  HIS A  57       5.846  -2.418   9.058  1.00 29.95           C
ANISOU  432  CB  HIS A  57     3720   4137   3522    616     -9     73       C
ATOM    433  CG  HIS A  57       6.397  -1.034   9.128  1.00 34.06           C
ANISOU  433  CG  HIS A  57     4146   4702   4091    590     -6     48       C
ATOM    434  ND1 HIS A  57       6.122  -0.162  10.148  1.00 37.91           N
ANISOU  434  ND1 HIS A  57     4562   5243   4599    564    -55     35       N
ATOM    435  CD2 HIS A  57       7.458  -0.493   8.482  1.00 34.99           C
ANISOU  435  CD2 HIS A  57     4220   4827   4246    599     46     34       C
ATOM    436  CE1 HIS A  57       6.840   0.939  10.013  1.00 35.37           C
ANISOU  436  CE1 HIS A  57     4166   4952   4321    547    -37     13       C
ATOM    437  NE2 HIS A  57       7.680   0.757   9.018  1.00 35.92           N
ANISOU  437  NE2 HIS A  57     4248   4997   4403    568     25     11       N
ATOM    438  N   THR A  58       2.587  -1.015   8.328  1.00 27.43           N
ANISOU  438  N   THR A  58     3502   3763   3157    453    -89     72       N
ATOM    439  CA  THR A  58       1.796  -0.156   7.456  1.00 25.94           C
ANISOU  439  CA  THR A  58     3346   3546   2964    396    -94     67       C
ATOM    440  C   THR A  58       1.878   1.317   7.801  1.00 31.61           C
ANISOU  440  C   THR A  58     3983   4307   3720    366   -107     46       C
ATOM    441  O   THR A  58       1.355   2.123   7.029  1.00 34.32           O
ANISOU  441  O   THR A  58     4352   4627   4062    323   -107     41       O
ATOM    442  CB  THR A  58       0.308  -0.483   7.575  1.00 27.02           C
ANISOU  442  CB  THR A  58     3538   3659   3070    357   -142     80       C
ATOM    443  OG1 THR A  58      -0.206   0.132   8.791  1.00 23.05           O
ANISOU  443  OG1 THR A  58     2965   3205   2588    341   -187     74       O
ATOM    444  CG2 THR A  58       0.031  -1.964   7.560  1.00 24.50           C
ANISOU  444  CG2 THR A  58     3295   3303   2711    379   -141    100       C
ATOM    445  N   ALA A  59       2.462   1.696   8.937  1.00 30.06           N
ANISOU  445  N   ALA A  59     3697   4170   3555    385   -121     35       N
ATOM    446  CA  ALA A  59       2.361   3.089   9.370  1.00 32.49           C
ANISOU  446  CA  ALA A  59     3936   4515   3894    350   -139     16       C
ATOM    447  C   ALA A  59       3.132   4.041   8.469  1.00 32.34           C
ANISOU  447  C   ALA A  59     3897   4490   3899    335    -94     -2       C
ATOM    448  O   ALA A  59       4.278   3.771   8.080  1.00 32.22           O
ANISOU  448  O   ALA A  59     3866   4476   3900    367    -48     -7       O
ATOM    449  CB  ALA A  59       2.888   3.238  10.795  1.00 32.08           C
ANISOU  449  CB  ALA A  59     3798   4525   3865    373   -166      7       C
ATOM    450  N   ALA A  60       2.514   5.190   8.200  1.00 41.49           N
ANISOU  450  N   ALA A  60     5055   5645   5065    288   -104    -11       N
ATOM    451  CA  ALA A  60       3.145   6.311   7.501  1.00 47.11           C
ANISOU  451  CA  ALA A  60     5744   6353   5801    265    -64    -30       C
ATOM    452  C   ALA A  60       4.157   6.995   8.419  1.00 51.72           C
ANISOU  452  C   ALA A  60     6225   6998   6429    273    -60    -53       C
ATOM    453  O   ALA A  60       4.179   6.761   9.625  1.00 55.25           O
ANISOU  453  O   ALA A  60     6621   7489   6884    290    -98    -53       O
ATOM    454  CB  ALA A  60       2.090   7.312   7.031  1.00 44.78           C
ANISOU  454  CB  ALA A  60     5484   6034   5496    216    -83    -32       C
ATOM    455  N   ILE A  61       4.982   7.878   7.860  1.00 51.12           N
ANISOU  455  N   ILE A  61     6119   6924   6381    258    -14    -73       N
ATOM    456  CA  ILE A  61       6.010   8.576   8.667  1.00 61.94           C
ANISOU  456  CA  ILE A  61     7387   8352   7796    259     -9    -97       C
ATOM    457  C   ILE A  61       5.399   9.913   9.068  1.00 70.53           C
ANISOU  457  C   ILE A  61     8453   9454   8892    210    -34   -112       C
ATOM    458  O   ILE A  61       5.723  10.975   8.529  1.00 74.45           O
ANISOU  458  O   ILE A  61     8940   9941   9406    177     -0   -130       O
ATOM    459  CB  ILE A  61       7.343   8.724   7.917  1.00 64.81           C
ANISOU  459  CB  ILE A  61     7721   8712   8192    270     59   -112       C
ATOM    460  CG1 ILE A  61       7.809   7.369   7.362  1.00 57.18           C
ANISOU  460  CG1 ILE A  61     6795   7720   7213    321     91    -93       C
ATOM    461  CG2 ILE A  61       8.433   9.354   8.814  1.00 60.97           C
ANISOU  461  CG2 ILE A  61     7119   8290   7755    270     58   -137       C
ATOM    462  CD1 ILE A  61       7.715   6.211   8.353  1.00 53.28           C
ANISOU  462  CD1 ILE A  61     6286   7253   6706    368     46    -76       C
ATOM    463  N   SER A  62       4.492   9.865  10.053  1.00 88.55           N
ANISOU  463  N   SER A  62    10730  11755  11159    205    -92   -104       N
ATOM    464  CA  SER A  62       3.736  11.046  10.468  1.00 88.17           C
ANISOU  464  CA  SER A  62    10672  11716  11114    162   -117   -114       C
ATOM    465  C   SER A  62       4.206  11.625  11.802  1.00 92.44           C
ANISOU  465  C   SER A  62    11129  12314  11678    158   -144   -134       C
ATOM    466  O   SER A  62       3.495  12.460  12.384  1.00 91.91           O
ANISOU  466  O   SER A  62    11056  12256  11609    128   -170   -140       O
ATOM    467  CB  SER A  62       2.237  10.738  10.546  1.00 88.31           C
ANISOU  467  CB  SER A  62    10749  11707  11099    154   -158    -92       C
ATOM    468  OG  SER A  62       1.883  10.212  11.813  1.00 93.71           O
ANISOU  468  OG  SER A  62    11406  12424  11777    171   -202    -85       O
ATOM    469  N   ASN A  63       5.373  11.200  12.302  1.00 83.39           N
ANISOU  469  N   ASN A  63     9920  11208  10555    187   -139   -144       N
ATOM    470  CA  ASN A  63       6.001  11.782  13.482  1.00 75.31           C
ANISOU  470  CA  ASN A  63     8816  10241   9556    181   -165   -167       C
ATOM    471  C   ASN A  63       7.158  12.718  13.121  1.00 71.89           C
ANISOU  471  C   ASN A  63     8325   9826   9165    156   -124   -196       C
ATOM    472  O   ASN A  63       8.059  12.939  13.937  1.00 68.95           O
ANISOU  472  O   ASN A  63     7875   9505   8820    160   -139   -215       O
ATOM    473  CB  ASN A  63       6.486  10.676  14.422  1.00 75.03           C
ANISOU  473  CB  ASN A  63     8747  10243   9519    231   -199   -158       C
ATOM    474  N   THR A  64       7.162  13.263  11.913  1.00 75.57           N
ANISOU  474  N   THR A  64     8828  10251   9635    131    -72   -200       N
ATOM    475  CA  THR A  64       8.216  14.164  11.474  1.00 70.59           C
ANISOU  475  CA  THR A  64     8149   9629   9042    103    -23   -227       C
ATOM    476  C   THR A  64       7.666  15.581  11.426  1.00 71.89           C
ANISOU  476  C   THR A  64     8331   9779   9205     47    -19   -243       C
ATOM    477  O   THR A  64       6.561  15.814  10.923  1.00 73.00           O
ANISOU  477  O   THR A  64     8546   9877   9316     33    -22   -228       O
ATOM    478  CB  THR A  64       8.777  13.765  10.098  1.00 69.19           C
ANISOU  478  CB  THR A  64     8006   9411   8873    115     44   -222       C
ATOM    479  OG1 THR A  64       7.698  13.537   9.178  1.00 71.91           O
ANISOU  479  OG1 THR A  64     8453   9694   9176    112     51   -199       O
ATOM    480  CG2 THR A  64       9.646  12.521  10.201  1.00 63.20           C
ANISOU  480  CG2 THR A  64     7212   8673   8128    171     51   -212       C
ATOM    481  N   GLY A  65       8.425  16.521  11.984  1.00 67.27           N
ANISOU  481  N   GLY A  65     7676   9230   8652     15    -14   -274       N
ATOM    482  CA  GLY A  65       8.081  17.913  11.794  1.00 65.31           C
ANISOU  482  CA  GLY A  65     7448   8963   8405    -39      4   -292       C
ATOM    483  C   GLY A  65       8.062  18.243  10.330  1.00 64.60           C
ANISOU  483  C   GLY A  65     7420   8815   8310    -55     69   -289       C
ATOM    484  O   GLY A  65       7.190  18.983   9.857  1.00 66.50           O
ANISOU  484  O   GLY A  65     7724   9014   8526    -81     76   -284       O
ATOM    485  N   LEU A  66       9.001  17.647   9.589  1.00 68.36           N
ANISOU  485  N   LEU A  66     7881   9285   8806    -34    116   -289       N
ATOM    486  CA  LEU A  66       9.044  17.759   8.145  1.00 69.96           C
ANISOU  486  CA  LEU A  66     8153   9428   9000    -42    181   -284       C
ATOM    487  C   LEU A  66       7.652  17.389   7.684  1.00 70.48           C
ANISOU  487  C   LEU A  66     8316   9447   9015    -30    153   -253       C
ATOM    488  O   LEU A  66       7.232  16.229   7.796  1.00 76.62           O
ANISOU  488  O   LEU A  66     9115  10224   9772     10    121   -229       O
ATOM    489  CB  LEU A  66      10.156  16.878   7.537  1.00 68.16           C
ANISOU  489  CB  LEU A  66     7900   9201   8798     -9    231   -283       C
ATOM    490  CG  LEU A  66      10.323  16.966   6.012  1.00 66.30           C
ANISOU  490  CG  LEU A  66     7739   8899   8552    -17    309   -279       C
ATOM    491  CD1 LEU A  66      11.762  16.806   5.641  1.00 63.15           C
ANISOU  491  CD1 LEU A  66     7279   8514   8202    -10    376   -296       C
ATOM    492  CD2 LEU A  66       9.508  15.889   5.318  1.00 73.63           C
ANISOU  492  CD2 LEU A  66     8761   9782   9434     20    298   -245       C
ATOM    493  N   CYS A  67       6.900  18.408   7.278  1.00 69.55           N
ANISOU  493  N   CYS A  67     8254   9293   8878    -65    158   -255       N
ATOM    494  CA  CYS A  67       5.542  18.230   6.767  1.00 73.33           C
ANISOU  494  CA  CYS A  67     8823   9726   9313    -59    130   -228       C
ATOM    495  C   CYS A  67       4.584  17.756   7.839  1.00 78.92           C
ANISOU  495  C   CYS A  67     9517  10463  10006    -41     56   -212       C
ATOM    496  O   CYS A  67       3.691  16.969   7.526  1.00 81.43           O
ANISOU  496  O   CYS A  67     9890  10756  10295    -20     28   -185       O
ATOM    497  CB  CYS A  67       5.487  17.256   5.564  1.00 78.57           C
ANISOU  497  CB  CYS A  67     9560  10341   9951    -32    157   -206       C
ATOM    498  SG  CYS A  67       6.590  17.532   4.201  1.00 70.06           S
ANISOU  498  SG  CYS A  67     8515   9220   8886    -43    252   -220       S
ATOM    499  N   GLU A  68       4.675  18.183   9.118  1.00 87.34           N
ANISOU  499  N   GLU A  68    10515  11579  11090    -51     23   -227       N
ATOM    500  CA  GLU A  68       3.450  17.806   9.874  1.00 88.89           C
ANISOU  500  CA  GLU A  68    10728  11784  11263    -38    -39   -206       C
ATOM    501  C   GLU A  68       2.255  18.625   9.359  1.00 96.84           C
ANISOU  501  C   GLU A  68    11801  12747  12248    -60    -45   -195       C
ATOM    502  O   GLU A  68       1.203  18.470   9.976  1.00 99.09           O
ANISOU  502  O   GLU A  68    12094  13037  12519    -53    -91   -180       O
ATOM    503  CB  GLU A  68       3.325  17.975  11.440  1.00 90.52           C
ANISOU  503  CB  GLU A  68    10872  12042  11478    -39    -86   -215       C
ATOM    504  CG  GLU A  68       3.501  19.534  11.865  1.00 79.83           C
ANISOU  504  CG  GLU A  68     9493  10698  10139    -84    -73   -244       C
ATOM    505  CD  GLU A  68       4.812  19.854  12.597  1.00 81.88           C
ANISOU  505  CD  GLU A  68     9672  11008  10432    -98    -64   -275       C
ATOM    506  OE1 GLU A  68       5.754  19.083  13.097  1.00 89.56           O
ANISOU  506  OE1 GLU A  68    10583  12022  11423    -75    -75   -281       O
ATOM    507  OE2 GLU A  68       5.302  20.708  11.840  1.00 82.99           O
ANISOU  507  OE2 GLU A  68     9820  11125  10585   -129    -15   -292       O
ATOM    508  N   GLN A  69       2.382  19.374   8.226  1.00103.63           N
ANISOU  508  N   GLN A  69    12710  13563  13104    -81      0   -201       N
ATOM    509  CA  GLN A  69       1.428  20.280   7.628  1.00 96.05           C
ANISOU  509  CA  GLN A  69    11813  12559  12124   -101      0   -194       C
ATOM    510  C   GLN A  69       1.820  21.633   8.201  1.00 93.08           C
ANISOU  510  C   GLN A  69    11401  12199  11768   -136     20   -221       C
ATOM    511  O   GLN A  69       1.018  22.586   8.224  1.00 86.60           O
ANISOU  511  O   GLN A  69    10610  11357  10936   -152     13   -220       O
ATOM    512  CB  GLN A  69      -0.041  19.945   7.919  1.00 92.02           C
ANISOU  512  CB  GLN A  69    11331  12039  11591    -86    -57   -167       C
ATOM    513  N   ASN A  70       3.060  21.699   8.702  1.00 83.03           N
ANISOU  513  N   ASN A  70    10059  10965  10523   -146     45   -247       N
ATOM    514  CA  ASN A  70       3.610  22.866   9.369  1.00 77.96           C
ANISOU  514  CA  ASN A  70     9373  10346   9903   -184     61   -278       C
ATOM    515  C   ASN A  70       5.069  23.014   8.899  1.00 67.82           C
ANISOU  515  C   ASN A  70     8051   9069   8648   -202    120   -304       C
ATOM    516  O   ASN A  70       5.253  22.947   7.682  1.00 70.05           O
ANISOU  516  O   ASN A  70     8386   9307   8923   -201    166   -298       O
ATOM    517  CB  ASN A  70       3.365  22.700  10.868  1.00 72.84           C
ANISOU  517  CB  ASN A  70     8667   9749   9260   -177      7   -282       C
ATOM    518  N   PRO A  71       6.127  23.200   9.705  1.00 62.06           N
ANISOU  518  N   PRO A  71     7239   8389   7953   -219    124   -332       N
ATOM    519  CA  PRO A  71       7.402  23.444   9.022  1.00 59.79           C
ANISOU  519  CA  PRO A  71     6924   8098   7696   -240    190   -355       C
ATOM    520  C   PRO A  71       8.076  22.154   8.570  1.00 51.99           C
ANISOU  520  C   PRO A  71     5914   7119   6721   -200    204   -343       C
ATOM    521  O   PRO A  71       8.477  21.318   9.384  1.00 46.41           O
ANISOU  521  O   PRO A  71     5142   6463   6030   -172    166   -342       O
ATOM    522  CB  PRO A  71       8.232  24.204  10.075  1.00 50.41           C
ANISOU  522  CB  PRO A  71     5652   6961   6542   -277    185   -391       C
ATOM    523  CG  PRO A  71       7.837  23.640  11.347  1.00 49.92           C
ANISOU  523  CG  PRO A  71     5549   6946   6473   -253    112   -383       C
ATOM    524  CD  PRO A  71       6.377  23.198  11.166  1.00 61.23           C
ANISOU  524  CD  PRO A  71     7058   8345   7863   -222     77   -347       C
ATOM    525  N   GLU A  72       8.317  22.060   7.269  1.00 53.99           N
ANISOU  525  N   GLU A  72     6221   7323   6968   -199    263   -337       N
ATOM    526  CA  GLU A  72       9.007  20.916   6.702  1.00 54.38           C
ANISOU  526  CA  GLU A  72     6260   7371   7029   -162    290   -327       C
ATOM    527  C   GLU A  72      10.498  21.196   6.539  1.00 52.15           C
ANISOU  527  C   GLU A  72     5906   7111   6799   -182    353   -357       C
ATOM    528  O   GLU A  72      10.903  22.273   6.096  1.00 50.64           O
ANISOU  528  O   GLU A  72     5722   6898   6621   -228    407   -380       O
ATOM    529  CB  GLU A  72       8.408  20.579   5.343  1.00 54.21           C
ANISOU  529  CB  GLU A  72     6348   7279   6969   -148    321   -303       C
ATOM    530  N   LEU A  73      11.320  20.216   6.886  1.00 47.94           N
ANISOU  530  N   LEU A  73     5301   6619   6295   -147    348   -357       N
ATOM    531  CA  LEU A  73      12.762  20.386   6.731  1.00 45.32           C
ANISOU  531  CA  LEU A  73     4889   6312   6020   -162    407   -384       C
ATOM    532  C   LEU A  73      13.156  20.382   5.249  1.00 47.00           C
ANISOU  532  C   LEU A  73     5164   6462   6231   -165    500   -381       C
ATOM    533  O   LEU A  73      13.996  21.188   4.815  1.00 40.69           O
ANISOU  533  O   LEU A  73     4340   5653   5466   -206    568   -408       O
ATOM    534  CB  LEU A  73      13.510  19.281   7.513  1.00 41.00           C
ANISOU  534  CB  LEU A  73     4247   5826   5504   -114    373   -381       C
ATOM    535  CG  LEU A  73      14.991  18.996   7.220  1.00 41.41           C
ANISOU  535  CG  LEU A  73     4214   5903   5617   -106    432   -398       C
ATOM    536  CD1 LEU A  73      15.739  20.279   7.249  1.00 41.13           C
ANISOU  536  CD1 LEU A  73     4125   5880   5623   -171    475   -437       C
ATOM    537  CD2 LEU A  73      15.711  17.922   8.113  1.00 42.86           C
ANISOU  537  CD2 LEU A  73     4299   6153   5833    -53    387   -394       C
ATOM    538  N   SER A  74      12.522  19.510   4.453  1.00 47.26           N
ANISOU  538  N   SER A  74     5287   6448   6223   -126    503   -350       N
ATOM    539  CA  SER A  74      12.807  19.353   3.026  1.00 49.05           C
ANISOU  539  CA  SER A  74     5590   6608   6438   -123    587   -343       C
ATOM    540  C   SER A  74      14.285  18.989   2.798  1.00 45.62           C
ANISOU  540  C   SER A  74     5076   6196   6063   -112    658   -360       C
ATOM    541  O   SER A  74      15.021  19.673   2.079  1.00 44.13           O
ANISOU  541  O   SER A  74     4888   5980   5899   -146    741   -381       O
ATOM    542  CB  SER A  74      12.405  20.604   2.224  1.00 46.56           C
ANISOU  542  CB  SER A  74     5359   6235   6099   -173    631   -353       C
ATOM    543  OG  SER A  74      11.016  20.610   1.946  1.00 46.71           O
ANISOU  543  OG  SER A  74     5479   6211   6056   -166    583   -327       O
ATOM    544  N   GLU A  75      14.719  17.901   3.442  1.00 50.06           N
ANISOU  544  N   GLU A  75     5566   6807   6647    -62    624   -351       N
ATOM    545  CA  GLU A  75      16.061  17.357   3.225  1.00 56.51           C
ANISOU  545  CA  GLU A  75     6306   7646   7521    -38    685   -361       C
ATOM    546  C   GLU A  75      15.988  16.221   2.195  1.00 55.13           C
ANISOU  546  C   GLU A  75     6215   7416   7316     13    730   -332       C
ATOM    547  O   GLU A  75      14.929  15.932   1.626  1.00 44.43           O
ANISOU  547  O   GLU A  75     4977   6007   5898     22    712   -307       O
ATOM    548  CB  GLU A  75      16.693  16.863   4.536  1.00 52.43           C
ANISOU  548  CB  GLU A  75     5656   7215   7049    -10    625   -368       C
ATOM    549  N   SER A  76      17.136  15.567   1.952  1.00 61.92           N
ANISOU  549  N   SER A  76     7013   8290   8223     47    789   -336       N
ATOM    550  CA  SER A  76      17.251  14.374   1.100  1.00 56.60           C
ANISOU  550  CA  SER A  76     6405   7570   7529    102    835   -310       C
ATOM    551  C   SER A  76      17.890  13.286   1.994  1.00 62.38           C
ANISOU  551  C   SER A  76     7036   8368   8299    164    797   -302       C
ATOM    552  O   SER A  76      19.107  13.087   1.966  1.00 60.91           O
ANISOU  552  O   SER A  76     6758   8209   8175    184    852   -314       O
ATOM    553  CB  SER A  76      18.106  14.665  -0.156  1.00 59.79           C
ANISOU  553  CB  SER A  76     6840   7921   7956     87    961   -322       C
ATOM    554  OG  SER A  76      17.488  15.593  -1.040  1.00 54.25           O
ANISOU  554  OG  SER A  76     6249   7152   7212     36    996   -326       O
ATOM    555  N   ILE A  77      17.063  12.648   2.825  1.00 64.74           N
ANISOU  555  N   ILE A  77     7346   8692   8561    194    702   -281       N
ATOM    556  CA  ILE A  77      17.518  11.639   3.775  1.00 71.28           C
ANISOU  556  CA  ILE A  77     8090   9580   9414    254    653   -271       C
ATOM    557  C   ILE A  77      16.641  10.397   3.618  1.00 66.21           C
ANISOU  557  C   ILE A  77     7547   8901   8709    304    618   -235       C
ATOM    558  O   ILE A  77      16.200  10.067   2.514  1.00 60.63           O
ANISOU  558  O   ILE A  77     6956   8122   7959    308    665   -219       O
ATOM    559  CB  ILE A  77      17.486  12.141   5.232  1.00 71.53           C
ANISOU  559  CB  ILE A  77     8021   9690   9468    236    562   -288       C
ATOM    560  CG1 ILE A  77      18.221  13.461   5.383  1.00 67.70           C
ANISOU  560  CG1 ILE A  77     7449   9235   9037    174    591   -326       C
ATOM    561  CG2 ILE A  77      18.393  11.246   6.120  1.00 69.81           C
ANISOU  561  CG2 ILE A  77     7692   9538   9295    297    531   -285       C
ATOM    562  CD1 ILE A  77      19.651  13.373   5.092  1.00 68.28           C
ANISOU  562  CD1 ILE A  77     7428   9332   9185    188    663   -342       C
ATOM    563  N   ASN A  78      16.380   9.714   4.734  1.00 69.71           N
ANISOU  563  N   ASN A  78     7950   9393   9145    342    535   -222       N
ATOM    564  CA  ASN A  78      15.659   8.455   4.878  1.00 78.88           C
ANISOU  564  CA  ASN A  78     9183  10534  10254    393    493   -190       C
ATOM    565  C   ASN A  78      15.336   8.267   6.357  1.00 79.50           C
ANISOU  565  C   ASN A  78     9198  10677  10331    407    394   -188       C
ATOM    566  O   ASN A  78      16.130   8.641   7.226  1.00 76.90           O
ANISOU  566  O   ASN A  78     8752  10414  10052    408    370   -207       O
ATOM    567  CB  ASN A  78      16.469   7.267   4.343  1.00 80.99           C
ANISOU  567  CB  ASN A  78     9456  10782  10534    460    553   -174       C
ATOM    568  N   LEU A  79      14.165   7.699   6.630  1.00 89.99           N
ANISOU  568  N   LEU A  79    10606  11985  11601    416    336   -165       N
ATOM    569  CA  LEU A  79      13.678   7.585   7.995  1.00 90.15           C
ANISOU  569  CA  LEU A  79    10587  12057  11610    423    245   -162       C
ATOM    570  C   LEU A  79      14.395   6.491   8.784  1.00 83.49           C
ANISOU  570  C   LEU A  79     9683  11256  10784    494    219   -150       C
ATOM    571  O   LEU A  79      15.029   5.585   8.237  1.00 82.16           O
ANISOU  571  O   LEU A  79     9525  11068  10624    546    268   -137       O
ATOM    572  CB  LEU A  79      12.172   7.314   8.005  1.00 90.39           C
ANISOU  572  CB  LEU A  79    10721  12048  11575    408    198   -140       C
ATOM    573  N   ASN A  80      14.199   6.554  10.103  1.00 80.14           N
ANISOU  573  N   ASN A  80     9205  10885  10358    498    140   -154       N
ATOM    574  CA  ASN A  80      14.836   5.678  11.076  1.00 77.37           C
ANISOU  574  CA  ASN A  80     8791  10583  10022    562     99   -145       C
ATOM    575  C   ASN A  80      13.886   4.662  11.666  1.00 72.98           C
ANISOU  575  C   ASN A  80     8308  10013   9407    596     44   -117       C
ATOM    576  O   ASN A  80      14.320   3.557  12.009  1.00 67.39           O
ANISOU  576  O   ASN A  80     7594   9316   8697    664     35    -99       O
ATOM    577  CB  ASN A  80      15.425   6.499  12.237  1.00 78.99           C
ANISOU  577  CB  ASN A  80     8880  10864  10268    543     46   -172       C
ATOM    578  CG  ASN A  80      16.575   7.391  11.812  1.00 79.44           C
ANISOU  578  CG  ASN A  80     8845  10947  10393    515     97   -202       C
ATOM    579  OD1 ASN A  80      16.578   8.591  12.106  1.00 80.02           O
ANISOU  579  OD1 ASN A  80     8875  11044  10485    454     84   -229       O
ATOM    580  ND2 ASN A  80      17.568   6.811  11.142  1.00 78.05           N
ANISOU  580  ND2 ASN A  80     8636  10765  10254    559    160   -198       N
ATOM    581  N   GLY A  81      12.626   5.055  11.872  1.00 74.44           N
ANISOU  581  N   GLY A  81     8556  10177   9550    551      7   -113       N
ATOM    582  CA  GLY A  81      11.590   4.152  12.338  1.00 66.72           C
ANISOU  582  CA  GLY A  81     7656   9178   8517    572    -38    -87       C
ATOM    583  C   GLY A  81      11.597   2.783  11.696  1.00 58.19           C
ANISOU  583  C   GLY A  81     6649   8052   7409    626     -4    -60       C
ATOM    584  O   GLY A  81      11.497   1.756  12.370  1.00 59.50           O
ANISOU  584  O   GLY A  81     6833   8224   7550    676    -37    -41       O
ATOM    585  N   THR A  82      11.816   2.759  10.392  1.00 61.30           N
ANISOU  585  N   THR A  82     7087   8398   7807    620     65    -58       N
ATOM    586  CA  THR A  82      11.781   1.492   9.685  1.00 58.12           C
ANISOU  586  CA  THR A  82     6767   7943   7373    667    103    -33       C
ATOM    587  C   THR A  82      12.978   0.603  10.006  1.00 57.97           C
ANISOU  587  C   THR A  82     6693   7952   7383    745    121    -26       C
ATOM    588  O   THR A  82      12.800  -0.582  10.309  1.00 56.99           O
ANISOU  588  O   THR A  82     6617   7812   7225    797    106     -2       O
ATOM    589  CB  THR A  82      11.703   1.771   8.194  1.00 51.63           C
ANISOU  589  CB  THR A  82     6013   7059   6544    636    174    -35       C
ATOM    590  OG1 THR A  82      10.366   2.149   7.853  1.00 44.47           O
ANISOU  590  OG1 THR A  82     5189   6114   5594    580    149    -30       O
ATOM    591  CG2 THR A  82      12.117   0.559   7.420  1.00 50.87           C
ANISOU  591  CG2 THR A  82     5981   6915   6431    692    230    -14       C
ATOM    592  N   LYS A  83      14.188   1.165  10.035  1.00 57.81           N
ANISOU  592  N   LYS A  83     6566   7974   7424    756    148    -46       N
ATOM    593  CA  LYS A  83      15.371   0.348  10.304  1.00 57.16           C
ANISOU  593  CA  LYS A  83     6421   7920   7375    834    165    -38       C
ATOM    594  C   LYS A  83      15.288  -0.331  11.664  1.00 56.31           C
ANISOU  594  C   LYS A  83     6289   7856   7251    882     87    -26       C
ATOM    595  O   LYS A  83      15.569  -1.527  11.800  1.00 53.53           O
ANISOU  595  O   LYS A  83     5963   7491   6882    954     92     -3       O
ATOM    596  CB  LYS A  83      16.639   1.197  10.222  1.00 62.75           C
ANISOU  596  CB  LYS A  83     7005   8677   8161    828    198    -65       C
ATOM    597  CG  LYS A  83      17.916   0.395  10.434  1.00 57.53           C
ANISOU  597  CG  LYS A  83     6267   8048   7544    912    219    -58       C
ATOM    598  CD  LYS A  83      19.132   1.270  10.274  1.00 60.20           C
ANISOU  598  CD  LYS A  83     6477   8431   7963    898    257    -87       C
ATOM    599  CE  LYS A  83      20.407   0.500  10.571  1.00 62.69           C
ANISOU  599  CE  LYS A  83     6703   8787   8331    984    270    -79       C
ATOM    600  NZ  LYS A  83      20.686  -0.538   9.525  1.00 63.09           N
ANISOU  600  NZ  LYS A  83     6825   8776   8372   1042    356    -56       N
ATOM    601  N   TYR A  84      14.939   0.431  12.692  1.00 58.78           N
ANISOU  601  N   TYR A  84     6552   8217   7566    844     17    -41       N
ATOM    602  CA  TYR A  84      14.882  -0.138  14.029  1.00 56.73           C
ANISOU  602  CA  TYR A  84     6271   7997   7287    887    -58    -30       C
ATOM    603  C   TYR A  84      13.839  -1.241  14.109  1.00 53.08           C
ANISOU  603  C   TYR A  84     5929   7483   6755    909    -73     -0       C
ATOM    604  O   TYR A  84      14.061  -2.274  14.754  1.00 48.35           O
ANISOU  604  O   TYR A  84     5341   6892   6137    977    -99     19       O
ATOM    605  CB  TYR A  84      14.590   0.967  15.050  1.00 61.11           C
ANISOU  605  CB  TYR A  84     6766   8603   7850    833   -126    -53       C
ATOM    606  CG  TYR A  84      15.533   2.143  14.957  1.00 67.49           C
ANISOU  606  CG  TYR A  84     7462   9458   8724    798   -111    -86       C
ATOM    607  CD1 TYR A  84      16.871   1.943  14.646  1.00 70.92           C
ANISOU  607  CD1 TYR A  84     7812   9919   9216    843    -73    -92       C
ATOM    608  CD2 TYR A  84      15.093   3.444  15.171  1.00 66.25           C
ANISOU  608  CD2 TYR A  84     7283   9317   8574    721   -132   -111       C
ATOM    609  CE1 TYR A  84      17.754   2.998  14.551  1.00 74.51           C
ANISOU  609  CE1 TYR A  84     8160  10416   9735    807    -57   -123       C
ATOM    610  CE2 TYR A  84      15.973   4.510  15.074  1.00 71.96           C
ANISOU  610  CE2 TYR A  84     7906  10078   9356    685   -115   -142       C
ATOM    611  CZ  TYR A  84      17.310   4.274  14.760  1.00 76.03           C
ANISOU  611  CZ  TYR A  84     8336  10622   9931    726    -78   -149       C
ATOM    612  OH  TYR A  84      18.233   5.292  14.652  1.00 77.68           O
ANISOU  612  OH  TYR A  84     8442  10870  10204    689    -58   -181       O
ATOM    613  N   LEU A  85      12.697  -1.048  13.447  1.00 51.94           N
ANISOU  613  N   LEU A  85     5876   7285   6572    853    -57      4       N
ATOM    614  CA  LEU A  85      11.647  -2.047  13.540  1.00 49.25           C
ANISOU  614  CA  LEU A  85     5647   6897   6168    865    -74     30       C
ATOM    615  C   LEU A  85      12.196  -3.362  13.026  1.00 46.88           C
ANISOU  615  C   LEU A  85     5396   6562   5856    938    -28     53       C
ATOM    616  O   LEU A  85      12.093  -4.395  13.687  1.00 47.09           O
ANISOU  616  O   LEU A  85     5458   6584   5850    990    -55     74       O
ATOM    617  CB  LEU A  85      10.411  -1.639  12.734  1.00 47.15           C
ANISOU  617  CB  LEU A  85     5467   6578   5870    793    -60     30       C
ATOM    618  CG  LEU A  85       9.136  -2.401  13.186  1.00 40.23           C
ANISOU  618  CG  LEU A  85     4684   5668   4934    786    -98     51       C
ATOM    619  CD1 LEU A  85       7.862  -1.660  12.720  1.00 47.78           C
ANISOU  619  CD1 LEU A  85     5691   6594   5871    706   -107     46       C
ATOM    620  CD2 LEU A  85       8.992  -3.905  13.098  1.00 41.88           C
ANISOU  620  CD2 LEU A  85     4979   5834   5100    840    -85     79       C
ATOM    621  N   ALA A  86      12.882  -3.311  11.881  1.00 49.65           N
ANISOU  621  N   ALA A  86     5743   6887   6234    946     44     49       N
ATOM    622  CA  ALA A  86      13.477  -4.510  11.307  1.00 46.81           C
ANISOU  622  CA  ALA A  86     5430   6490   5866   1017     97     70       C
ATOM    623  C   ALA A  86      14.525  -5.092  12.232  1.00 49.85           C
ANISOU  623  C   ALA A  86     5735   6926   6279   1100     74     77       C
ATOM    624  O   ALA A  86      14.605  -6.314  12.401  1.00 51.94           O
ANISOU  624  O   ALA A  86     6056   7167   6513   1167     79    102       O
ATOM    625  CB  ALA A  86      14.114  -4.192   9.960  1.00 45.21           C
ANISOU  625  CB  ALA A  86     5228   6256   5695   1008    183     62       C
ATOM    626  N   GLU A  87      15.353  -4.233  12.830  1.00 52.03           N
ANISOU  626  N   GLU A  87     5882   7274   6613   1098     47     55       N
ATOM    627  CA  GLU A  87      16.393  -4.740  13.716  1.00 52.57           C
ANISOU  627  CA  GLU A  87     5866   7396   6712   1179     17     61       C
ATOM    628  C   GLU A  87      15.780  -5.466  14.900  1.00 52.04           C
ANISOU  628  C   GLU A  87     5844   7336   6591   1210    -56     79       C
ATOM    629  O   GLU A  87      16.313  -6.491  15.339  1.00 47.19           O
ANISOU  629  O   GLU A  87     5234   6728   5970   1294    -64     99       O
ATOM    630  CB  GLU A  87      17.315  -3.601  14.153  1.00 52.06           C
ANISOU  630  CB  GLU A  87     5655   7408   6719   1159     -5     30       C
ATOM    631  CG  GLU A  87      18.285  -3.215  13.028  1.00 57.23           C
ANISOU  631  CG  GLU A  87     6253   8056   7434   1158     80     17       C
ATOM    632  CD  GLU A  87      19.338  -2.170  13.403  1.00 60.89           C
ANISOU  632  CD  GLU A  87     6564   8595   7977   1141     66    -13       C
ATOM    633  OE1 GLU A  87      19.257  -1.559  14.499  1.00 62.73           O
ANISOU  633  OE1 GLU A  87     6734   8884   8215   1116    -14    -29       O
ATOM    634  OE2 GLU A  87      20.258  -1.975  12.573  1.00 57.66           O
ANISOU  634  OE2 GLU A  87     6100   8185   7624   1151    139    -23       O
ATOM    635  N   ALA A  88      14.626  -4.987  15.378  1.00 52.84           N
ANISOU  635  N   ALA A  88     5989   7433   6654   1144   -103     73       N
ATOM    636  CA  ALA A  88      13.906  -5.691  16.430  1.00 50.22           C
ANISOU  636  CA  ALA A  88     5717   7097   6266   1166   -163     91       C
ATOM    637  C   ALA A  88      13.434  -7.051  15.940  1.00 53.62           C
ANISOU  637  C   ALA A  88     6272   7457   6643   1206   -126    122       C
ATOM    638  O   ALA A  88      13.544  -8.058  16.654  1.00 56.46           O
ANISOU  638  O   ALA A  88     6665   7814   6971   1273   -150    143       O
ATOM    639  CB  ALA A  88      12.727  -4.841  16.913  1.00 51.08           C
ANISOU  639  CB  ALA A  88     5849   7211   6351   1082   -208     78       C
ATOM    640  N   ALA A  89      12.942  -7.111  14.709  1.00 48.43           N
ANISOU  640  N   ALA A  89     5689   6740   5972   1168    -66    125       N
ATOM    641  CA  ALA A  89      12.496  -8.386  14.177  1.00 50.00           C
ANISOU  641  CA  ALA A  89     6012   6867   6118   1200    -28    152       C
ATOM    642  C   ALA A  89      13.656  -9.368  14.024  1.00 56.70           C
ANISOU  642  C   ALA A  89     6850   7713   6982   1300     11    169       C
ATOM    643  O   ALA A  89      13.460 -10.580  14.188  1.00 56.90           O
ANISOU  643  O   ALA A  89     6962   7697   6960   1352     18    194       O
ATOM    644  CB  ALA A  89      11.786  -8.167  12.845  1.00 46.83           C
ANISOU  644  CB  ALA A  89     5691   6404   5700   1136     25    149       C
ATOM    645  N   SER A  90      14.864  -8.876  13.711  1.00 60.48           N
ANISOU  645  N   SER A  90     7223   8231   7527   1328     41    155       N
ATOM    646  CA  SER A  90      16.023  -9.763  13.630  1.00 61.45           C
ANISOU  646  CA  SER A  90     7320   8356   7672   1429     77    172       C
ATOM    647  C   SER A  90      16.340 -10.370  14.995  1.00 62.54           C
ANISOU  647  C   SER A  90     7427   8537   7798   1500      9    185       C
ATOM    648  O   SER A  90      16.735 -11.537  15.083  1.00 63.82           O
ANISOU  648  O   SER A  90     7635   8675   7940   1586     27    211       O
ATOM    649  CB  SER A  90      17.230  -9.027  13.035  1.00 61.23           C
ANISOU  649  CB  SER A  90     7174   8365   7724   1438    124    152       C
ATOM    650  OG  SER A  90      17.594  -7.875  13.782  1.00 63.13           O
ANISOU  650  OG  SER A  90     7286   8684   8015   1403     68    126       O
ATOM    651  N   LYS A  91      16.159  -9.598  16.076  1.00 60.17           N
ANISOU  651  N   LYS A  91     7057   8298   7507   1468    -71    169       N
ATOM    652  CA  LYS A  91      16.447 -10.128  17.407  1.00 60.80           C
ANISOU  652  CA  LYS A  91     7113   8417   7570   1534   -141    182       C
ATOM    653  C   LYS A  91      15.566 -11.329  17.720  1.00 61.53           C
ANISOU  653  C   LYS A  91     7347   8450   7583   1560   -147    211       C
ATOM    654  O   LYS A  91      16.036 -12.338  18.268  1.00 59.03           O
ANISOU  654  O   LYS A  91     7052   8131   7246   1650   -160    234       O
ATOM    655  CB  LYS A  91      16.192  -9.060  18.470  1.00 56.05           C
ANISOU  655  CB  LYS A  91     6437   7879   6979   1480   -223    159       C
ATOM    656  CG  LYS A  91      16.895  -7.734  18.307  1.00 56.50           C
ANISOU  656  CG  LYS A  91     6361   7996   7110   1435   -227    126       C
ATOM    657  CD  LYS A  91      18.389  -7.868  18.376  1.00 63.67           C
ANISOU  657  CD  LYS A  91     7153   8955   8082   1512   -222    124       C
ATOM    658  CE  LYS A  91      18.959  -6.705  19.169  1.00 66.87           C
ANISOU  658  CE  LYS A  91     7425   9444   8539   1480   -287     94       C
ATOM    659  NZ  LYS A  91      18.876  -6.941  20.654  1.00 68.45           N
ANISOU  659  NZ  LYS A  91     7618   9683   8705   1514   -383    100       N
ATOM    660  N   ILE A  92      14.298 -11.265  17.317  1.00 57.91           N
ANISOU  660  N   ILE A  92     6986   7938   7078   1484   -134    211       N
ATOM    661  CA  ILE A  92      13.326 -12.286  17.671  1.00 58.92           C
ANISOU  661  CA  ILE A  92     7246   8011   7131   1491   -143    234       C
ATOM    662  C   ILE A  92      12.882 -13.101  16.465  1.00 55.95           C
ANISOU  662  C   ILE A  92     6987   7550   6720   1486    -68    250       C
ATOM    663  O   ILE A  92      11.911 -13.862  16.558  1.00 52.86           O
ANISOU  663  O   ILE A  92     6713   7103   6266   1470    -67    266       O
ATOM    664  CB  ILE A  92      12.134 -11.650  18.399  1.00 55.48           C
ANISOU  664  CB  ILE A  92     6830   7584   6665   1410   -198    223       C
ATOM    665  CG1 ILE A  92      11.302 -10.806  17.439  1.00 53.65           C
ANISOU  665  CG1 ILE A  92     6615   7327   6442   1310   -169    205       C
ATOM    666  CG2 ILE A  92      12.635 -10.765  19.495  1.00 52.44           C
ANISOU  666  CG2 ILE A  92     6331   7280   6315   1411   -267    205       C
ATOM    667  CD1 ILE A  92       9.957 -10.360  18.003  1.00 46.72           C
ANISOU  667  CD1 ILE A  92     5779   6443   5531   1231   -212    199       C
ATOM    668  N   ASN A  93      13.580 -12.967  15.338  1.00 56.30           N
ANISOU  668  N   ASN A  93     7007   7582   6804   1496     -3    245       N
ATOM    669  CA  ASN A  93      13.359 -13.806  14.157  1.00 56.43           C
ANISOU  669  CA  ASN A  93     7137   7515   6787   1503     73    260       C
ATOM    670  C   ASN A  93      11.891 -13.791  13.743  1.00 48.89           C
ANISOU  670  C   ASN A  93     6292   6504   5779   1412     72    259       C
ATOM    671  O   ASN A  93      11.239 -14.831  13.588  1.00 45.05           O
ANISOU  671  O   ASN A  93     5931   5954   5234   1419     89    279       O
ATOM    672  CB  ASN A  93      13.882 -15.231  14.378  1.00 56.39           C
ANISOU  672  CB  ASN A  93     7196   7478   6751   1608     97    290       C
ATOM    673  CG  ASN A  93      15.363 -15.244  14.742  1.00 59.74           C
ANISOU  673  CG  ASN A  93     7504   7960   7235   1703     98    293       C
ATOM    674  OD1 ASN A  93      16.210 -14.826  13.948  1.00 60.30           O
ANISOU  674  OD1 ASN A  93     7506   8044   7363   1714    149    282       O
ATOM    675  ND2 ASN A  93      15.675 -15.676  15.964  1.00 56.98           N
ANISOU  675  ND2 ASN A  93     7126   7648   6875   1768     38    305       N
ATOM    676  N   SER A  94      11.365 -12.585  13.609  1.00 46.27           N
ANISOU  676  N   SER A  94     5910   6199   5470   1326     48    235       N
ATOM    677  CA  SER A  94       9.974 -12.417  13.246  1.00 43.48           C
ANISOU  677  CA  SER A  94     5642   5802   5077   1237     38    232       C
ATOM    678  C   SER A  94       9.859 -12.296  11.724  1.00 35.79           C
ANISOU  678  C   SER A  94     4724   4773   4102   1199    103    228       C
ATOM    679  O   SER A  94      10.802 -11.913  11.028  1.00 35.15           O
ANISOU  679  O   SER A  94     4590   4703   4065   1221    149    219       O
ATOM    680  CB  SER A  94       9.387 -11.193  13.954  1.00 41.67           C
ANISOU  680  CB  SER A  94     5337   5627   4869   1168    -24    211       C
ATOM    681  OG  SER A  94       8.019 -11.070  13.654  1.00 40.11           O
ANISOU  681  OG  SER A  94     5216   5389   4634   1087    -35    210       O
ATOM    682  N   LYS A  95       8.711 -12.686  11.207  1.00 33.51           N
ANISOU  682  N   LYS A  95     4547   4422   3762   1143    108    235       N
ATOM    683  CA  LYS A  95       8.437 -12.578   9.780  1.00 35.60           C
ANISOU  683  CA  LYS A  95     4881   4630   4016   1098    159    231       C
ATOM    684  C   LYS A  95       7.746 -11.236   9.562  1.00 34.20           C
ANISOU  684  C   LYS A  95     4656   4477   3861   1009    127    208       C
ATOM    685  O   LYS A  95       6.645 -10.993  10.079  1.00 32.10           O
ANISOU  685  O   LYS A  95     4405   4217   3576    953     75    206       O
ATOM    686  CB  LYS A  95       7.596 -13.764   9.305  1.00 33.70           C
ANISOU  686  CB  LYS A  95     4792   4307   3707   1087    178    250       C
ATOM    687  CG  LYS A  95       7.294 -13.791   7.814  1.00 33.08           C
ANISOU  687  CG  LYS A  95     4803   4161   3606   1043    228    247       C
ATOM    688  CD  LYS A  95       8.252 -14.698   7.015  1.00 29.35           C
ANISOU  688  CD  LYS A  95     4392   3638   3121   1114    308    261       C
ATOM    689  CE  LYS A  95       7.899 -14.611   5.544  1.00 29.32           C
ANISOU  689  CE  LYS A  95     4482   3566   3092   1063    354    256       C
ATOM    690  NZ  LYS A  95       8.757 -15.466   4.722  1.00 33.84           N
ANISOU  690  NZ  LYS A  95     5125   4083   3650   1127    437    269       N
ATOM    691  N   LEU A  96       8.423 -10.334   8.873  1.00 31.35           N
ANISOU  691  N   LEU A  96     4232   4133   3545    998    159    192       N
ATOM    692  CA  LEU A  96       7.931  -8.969   8.731  1.00 33.97           C
ANISOU  692  CA  LEU A  96     4508   4494   3903    922    131    170       C
ATOM    693  C   LEU A  96       7.319  -8.757   7.353  1.00 31.69           C
ANISOU  693  C   LEU A  96     4307   4143   3591    864    165    167       C
ATOM    694  O   LEU A  96       7.960  -9.039   6.341  1.00 35.04           O
ANISOU  694  O   LEU A  96     4772   4527   4014    888    230    169       O
ATOM    695  CB  LEU A  96       9.056  -7.961   8.985  1.00 35.21           C
ANISOU  695  CB  LEU A  96     4532   4718   4128    941    138    150       C
ATOM    696  CG  LEU A  96       8.611  -6.513   8.874  1.00 27.67           C
ANISOU  696  CG  LEU A  96     3521   3793   3201    865    113    127       C
ATOM    697  CD1 LEU A  96       9.332  -5.685   9.884  1.00 27.22           C
ANISOU  697  CD1 LEU A  96     3330   3815   3196    879     80    110       C
ATOM    698  CD2 LEU A  96       8.915  -6.072   7.492  1.00 27.27           C
ANISOU  698  CD2 LEU A  96     3498   3702   3160    841    176    119       C
ATOM    699  N   ILE A  97       6.114  -8.200   7.314  1.00 30.66           N
ANISOU  699  N   ILE A  97     4201   4005   3443    789    120    161       N
ATOM    700  CA  ILE A  97       5.413  -7.906   6.066  1.00 27.38           C
ANISOU  700  CA  ILE A  97     3866   3534   3003    728    137    158       C
ATOM    701  C   ILE A  97       5.385  -6.400   5.956  1.00 30.08           C
ANISOU  701  C   ILE A  97     4127   3916   3387    680    122    136       C
ATOM    702  O   ILE A  97       4.847  -5.719   6.841  1.00 32.08           O
ANISOU  702  O   ILE A  97     4316   4216   3657    649     66    128       O
ATOM    703  CB  ILE A  97       4.000  -8.491   6.040  1.00 26.18           C
ANISOU  703  CB  ILE A  97     3809   3339   2799    679     97    169       C
ATOM    704  CG1 ILE A  97       4.052  -9.961   6.458  1.00 31.33           C
ANISOU  704  CG1 ILE A  97     4530   3962   3413    729    106    190       C
ATOM    705  CG2 ILE A  97       3.390  -8.355   4.671  1.00 26.13           C
ANISOU  705  CG2 ILE A  97     3897   3270   2762    626    114    168       C
ATOM    706  CD1 ILE A  97       4.850 -10.864   5.480  1.00 27.41           C
ANISOU  706  CD1 ILE A  97     4115   3407   2892    778    180    201       C
ATOM    707  N   PHE A  98       6.053  -5.871   4.941  1.00 27.32           N
ANISOU  707  N   PHE A  98     3778   3548   3055    677    176    126       N
ATOM    708  CA  PHE A  98       6.203  -4.429   4.779  1.00 32.13           C
ANISOU  708  CA  PHE A  98     4312   4192   3706    636    173    104       C
ATOM    709  C   PHE A  98       5.249  -3.862   3.729  1.00 30.07           C
ANISOU  709  C   PHE A  98     4128   3883   3416    568    167    101       C
ATOM    710  O   PHE A  98       5.030  -4.468   2.676  1.00 33.20           O
ANISOU  710  O   PHE A  98     4632   4211   3770    563    199    111       O
ATOM    711  CB  PHE A  98       7.653  -4.088   4.424  1.00 32.63           C
ANISOU  711  CB  PHE A  98     4310   4272   3814    677    239     93       C
ATOM    712  CG  PHE A  98       7.884  -2.628   4.200  1.00 29.93           C
ANISOU  712  CG  PHE A  98     3898   3960   3513    634    245     70       C
ATOM    713  CD1 PHE A  98       7.400  -1.695   5.111  1.00 30.53           C
ANISOU  713  CD1 PHE A  98     3898   4091   3612    597    183     57       C
ATOM    714  CD2 PHE A  98       8.567  -2.190   3.074  1.00 27.31           C
ANISOU  714  CD2 PHE A  98     3584   3597   3196    629    316     60       C
ATOM    715  CE1 PHE A  98       7.579  -0.326   4.901  1.00 31.64           C
ANISOU  715  CE1 PHE A  98     3980   4254   3787    555    190     35       C
ATOM    716  CE2 PHE A  98       8.774  -0.836   2.860  1.00 34.81           C
ANISOU  716  CE2 PHE A  98     4475   4570   4182    587    325     38       C
ATOM    717  CZ  PHE A  98       8.271   0.115   3.795  1.00 32.34           C
ANISOU  717  CZ  PHE A  98     4085   4313   3891    549    260     26       C
ATOM    718  N   CYS A  99       4.682  -2.696   4.014  1.00 27.67           N
ANISOU  718  N   CYS A  99     3770   3611   3132    518    125     88       N
ATOM    719  CA  CYS A  99       3.820  -2.000   3.043  1.00 31.58           C
ANISOU  719  CA  CYS A  99     4327   4065   3606    457    115     84       C
ATOM    720  C   CYS A  99       4.673  -1.044   2.207  1.00 28.87           C
ANISOU  720  C   CYS A  99     3962   3716   3289    450    173     67       C
ATOM    721  O   CYS A  99       5.158  -0.017   2.706  1.00 26.10           O
ANISOU  721  O   CYS A  99     3514   3418   2986    444    172     50       O
ATOM    722  CB  CYS A  99       2.668  -1.298   3.761  1.00 28.28           C
ANISOU  722  CB  CYS A  99     3873   3679   3193    408     42     81       C
ATOM    723  SG  CYS A  99       1.435  -2.550   4.371  1.00 42.93           S
ANISOU  723  SG  CYS A  99     5791   5517   5005    402    -14    102       S
ATOM    724  N   SER A 100       4.950  -1.455   0.962  1.00 28.42           N
ANISOU  724  N   SER A 100     4000   3594   3203    456    229     72       N
ATOM    725  CA  SER A 100       5.694  -0.698  -0.040  1.00 29.53           C
ANISOU  725  CA  SER A 100     4150   3712   3359    448    295     59       C
ATOM    726  C   SER A 100       4.744  -0.165  -1.102  1.00 25.86           C
ANISOU  726  C   SER A 100     3781   3191   2853    391    280     60       C
ATOM    727  O   SER A 100       3.528  -0.304  -0.992  1.00 29.59           O
ANISOU  727  O   SER A 100     4297   3653   3294    358    213     69       O
ATOM    728  CB  SER A 100       6.798  -1.565  -0.667  1.00 30.55           C
ANISOU  728  CB  SER A 100     4319   3805   3485    502    378     65       C
ATOM    729  OG  SER A 100       7.630  -0.807  -1.544  1.00 29.10           O
ANISOU  729  OG  SER A 100     4132   3602   3323    497    452     50       O
ATOM    730  N   SER A 101       5.289   0.314  -2.215  1.00 26.19           N
ANISOU  730  N   SER A 101     3871   3191   2890    384    344     52       N
ATOM    731  CA  SER A 101       4.460   1.073  -3.136  1.00 30.48           C
ANISOU  731  CA  SER A 101     4490   3689   3400    330    325     50       C
ATOM    732  C   SER A 101       4.785   0.772  -4.596  1.00 29.77           C
ANISOU  732  C   SER A 101     4528   3518   3267    331    393     53       C
ATOM    733  O   SER A 101       5.934   0.496  -4.955  1.00 30.31           O
ANISOU  733  O   SER A 101     4595   3572   3351    368    476     49       O
ATOM    734  CB  SER A 101       4.631   2.585  -2.877  1.00 25.82           C
ANISOU  734  CB  SER A 101     3814   3142   2854    301    322     30       C
ATOM    735  OG  SER A 101       3.662   3.316  -3.594  1.00 25.62           O
ANISOU  735  OG  SER A 101     3859   3080   2797    252    287     30       O
ATOM    736  N   ASP A 102       3.755   0.849  -5.444  1.00 26.46           N
ANISOU  736  N   ASP A 102     4219   3043   2793    290    356     61       N
ATOM    737  CA  ASP A 102       4.007   0.825  -6.875  1.00 28.06           C
ANISOU  737  CA  ASP A 102     4547   3165   2950    282    416     62       C
ATOM    738  C   ASP A 102       4.529   2.169  -7.368  1.00 29.37           C
ANISOU  738  C   ASP A 102     4689   3329   3141    263    462     44       C
ATOM    739  O   ASP A 102       4.874   2.289  -8.548  1.00 27.49           O
ANISOU  739  O   ASP A 102     4551   3024   2869    258    524     43       O
ATOM    740  CB  ASP A 102       2.743   0.419  -7.638  1.00 26.90           C
ANISOU  740  CB  ASP A 102     4532   2957   2733    244    355     75       C
ATOM    741  CG  ASP A 102       1.649   1.452  -7.547  1.00 30.95           C
ANISOU  741  CG  ASP A 102     5027   3489   3245    195    274     73       C
ATOM    742  OD1 ASP A 102       1.678   2.288  -6.617  1.00 32.50           O
ANISOU  742  OD1 ASP A 102     5101   3752   3495    191    250     63       O
ATOM    743  OD2 ASP A 102       0.752   1.440  -8.413  1.00 32.46           O
ANISOU  743  OD2 ASP A 102     5327   3626   3382    161    234     81       O
ATOM    744  N   GLN A 103       4.567   3.190  -6.495  1.00 30.90           N
ANISOU  744  N   GLN A 103     4761   3592   3389    251    434     31       N
ATOM    745  CA  GLN A 103       5.190   4.454  -6.867  1.00 30.44           C
ANISOU  745  CA  GLN A 103     4671   3534   3359    234    487     12       C
ATOM    746  C   GLN A 103       6.672   4.266  -7.106  1.00 31.87           C
ANISOU  746  C   GLN A 103     4822   3711   3574    271    594      2       C
ATOM    747  O   GLN A 103       7.290   5.095  -7.766  1.00 30.66           O
ANISOU  747  O   GLN A 103     4682   3535   3434    257    662    -12       O
ATOM    748  CB  GLN A 103       4.980   5.527  -5.792  1.00 28.84           C
ANISOU  748  CB  GLN A 103     4342   3408   3209    213    437     -1       C
ATOM    749  CG  GLN A 103       3.534   5.973  -5.603  1.00 25.83           C
ANISOU  749  CG  GLN A 103     3982   3030   2802    175    340      7       C
ATOM    750  CD  GLN A 103       3.036   6.731  -6.798  1.00 34.41           C
ANISOU  750  CD  GLN A 103     5175   4053   3845    140    344      7       C
ATOM    751  OE1 GLN A 103       3.793   7.460  -7.453  1.00 36.99           O
ANISOU  751  OE1 GLN A 103     5520   4354   4179    135    416     -6       O
ATOM    752  NE2 GLN A 103       1.767   6.532  -7.131  1.00 33.95           N
ANISOU  752  NE2 GLN A 103     5193   3966   3741    117    268     23       N
ATOM    753  N   ILE A 104       7.237   3.146  -6.651  1.00 32.77           N
ANISOU  753  N   ILE A 104     4907   3842   3702    318    615     10       N
ATOM    754  CA  ILE A 104       8.633   2.848  -6.953  1.00 33.27           C
ANISOU  754  CA  ILE A 104     4946   3897   3799    360    720      3       C
ATOM    755  C   ILE A 104       8.881   2.756  -8.459  1.00 36.02           C
ANISOU  755  C   ILE A 104     5436   4151   4098    354    802      5       C
ATOM    756  O   ILE A 104       9.992   3.036  -8.928  1.00 40.11           O
ANISOU  756  O   ILE A 104     5937   4654   4647    370    900     -6       O
ATOM    757  CB  ILE A 104       9.039   1.557  -6.224  1.00 28.32           C
ANISOU  757  CB  ILE A 104     4277   3297   3185    416    719     16       C
ATOM    758  CG1 ILE A 104       8.934   1.772  -4.716  1.00 27.85           C
ANISOU  758  CG1 ILE A 104     4075   3331   3177    423    647     11       C
ATOM    759  CG2 ILE A 104      10.431   1.165  -6.571  1.00 33.31           C
ANISOU  759  CG2 ILE A 104     4888   3918   3852    465    826     11       C
ATOM    760  CD1 ILE A 104       9.358   0.601  -3.933  1.00 28.00           C
ANISOU  760  CD1 ILE A 104     4049   3380   3209    480    642     23       C
ATOM    761  N   TYR A 105       7.861   2.426  -9.239  1.00 28.73           N
ANISOU  761  N   TYR A 105     4652   3163   3100    328    762     19       N
ATOM    762  CA  TYR A 105       8.008   2.374 -10.681  1.00 35.39           C
ANISOU  762  CA  TYR A 105     5645   3913   3889    319    832     22       C
ATOM    763  C   TYR A 105       7.854   3.720 -11.385  1.00 33.39           C
ANISOU  763  C   TYR A 105     5428   3632   3626    274    846      9       C
ATOM    764  O   TYR A 105       7.996   3.769 -12.610  1.00 36.47           O
ANISOU  764  O   TYR A 105     5948   3941   3967    265    907     10       O
ATOM    765  CB  TYR A 105       6.989   1.394 -11.250  1.00 36.51           C
ANISOU  765  CB  TYR A 105     5930   3992   3949    310    779     42       C
ATOM    766  CG  TYR A 105       7.122  -0.032 -10.751  1.00 34.22           C
ANISOU  766  CG  TYR A 105     5638   3710   3654    354    776     56       C
ATOM    767  CD1 TYR A 105       8.155  -0.841 -11.192  1.00 33.53           C
ANISOU  767  CD1 TYR A 105     5589   3584   3566    403    876     60       C
ATOM    768  CD2 TYR A 105       6.182  -0.579  -9.880  1.00 28.73           C
ANISOU  768  CD2 TYR A 105     4912   3053   2951    347    676     67       C
ATOM    769  CE1 TYR A 105       8.268  -2.164 -10.746  1.00 38.20           C
ANISOU  769  CE1 TYR A 105     6187   4177   4149    447    874     74       C
ATOM    770  CE2 TYR A 105       6.276  -1.875  -9.433  1.00 33.96           C
ANISOU  770  CE2 TYR A 105     5582   3717   3604    386    674     81       C
ATOM    771  CZ  TYR A 105       7.327  -2.679  -9.868  1.00 37.63           C
ANISOU  771  CZ  TYR A 105     6087   4144   4067    438    773     85       C
ATOM    772  OH  TYR A 105       7.423  -3.993  -9.451  1.00 32.22           O
ANISOU  772  OH  TYR A 105     5420   3455   3369    480    774    100       O
ATOM    773  N   ASN A 106       7.550   4.796 -10.666  1.00 34.75           N
ANISOU  773  N   ASN A 106     5499   3866   3839    246    794     -3       N
ATOM    774  CA  ASN A 106       7.101   6.024 -11.339  1.00 36.26           C
ANISOU  774  CA  ASN A 106     5746   4024   4007    200    787    -11       C
ATOM    775  C   ASN A 106       8.223   6.805 -12.138  1.00 38.37           C
ANISOU  775  C   ASN A 106     6033   4254   4293    196    909    -29       C
ATOM    776  O   ASN A 106       7.984   7.931 -12.577  1.00 37.70           O
ANISOU  776  O   ASN A 106     5978   4148   4197    160    911    -38       O
ATOM    777  CB  ASN A 106       6.389   6.930 -10.326  1.00 36.28           C
ANISOU  777  CB  ASN A 106     5642   4098   4044    173    697    -17       C
ATOM    778  CG  ASN A 106       7.340   7.615  -9.375  1.00 38.07           C
ANISOU  778  CG  ASN A 106     5711   4400   4354    180    733    -38       C
ATOM    779  OD1 ASN A 106       8.544   7.606  -9.579  1.00 40.54           O
ANISOU  779  OD1 ASN A 106     5991   4710   4702    200    829    -50       O
ATOM    780  ND2 ASN A 106       6.798   8.225  -8.328  1.00 37.49           N
ANISOU  780  ND2 ASN A 106     5537   4394   4313    163    656    -43       N
ATOM    781  N   GLY A 107       9.414   6.262 -12.331  1.00 38.99           N
ANISOU  781  N   GLY A 107     6092   4321   4400    232   1010    -34       N
ATOM    782  CA  GLY A 107      10.486   6.939 -13.031  1.00 40.49           C
ANISOU  782  CA  GLY A 107     6292   4478   4615    228   1130    -51       C
ATOM    783  C   GLY A 107      10.860   6.101 -14.240  1.00 40.77           C
ANISOU  783  C   GLY A 107     6475   4420   4595    251   1216    -40       C
ATOM    784  O   GLY A 107      11.505   6.579 -15.185  1.00 39.92           O
ANISOU  784  O   GLY A 107     6436   4254   4479    242   1318    -50       O
ATOM    785  N   ASN A 108      10.419   4.844 -14.222  1.00 37.36           N
ANISOU  785  N   ASN A 108     6101   3971   4122    278   1177    -20       N
ATOM    786  CA  ASN A 108      10.729   3.918 -15.304  1.00 43.12           C
ANISOU  786  CA  ASN A 108     6977   4611   4796    302   1254     -9       C
ATOM    787  C   ASN A 108      10.173   4.417 -16.638  1.00 44.24           C
ANISOU  787  C   ASN A 108     7298   4656   4855    263   1267     -7       C
ATOM    788  O   ASN A 108       9.056   4.935 -16.721  1.00 41.78           O
ANISOU  788  O   ASN A 108     7034   4341   4502    224   1170     -3       O
ATOM    789  CB  ASN A 108      10.171   2.531 -14.969  1.00 42.63           C
ANISOU  789  CB  ASN A 108     6951   4549   4699    331   1192     12       C
ATOM    790  CG  ASN A 108      10.933   1.856 -13.836  1.00 45.07           C
ANISOU  790  CG  ASN A 108     7110   4935   5082    382   1205     12       C
ATOM    791  OD1 ASN A 108      10.700   2.124 -12.627  1.00 39.21           O
ANISOU  791  OD1 ASN A 108     6226   4281   4390    380   1128      8       O
ATOM    792  ND2 ASN A 108      11.862   0.971 -14.219  1.00 42.99           N
ANISOU  792  ND2 ASN A 108     6878   4635   4823    431   1304     17       N
ATOM    793  N   ALA A 109      10.975   4.293 -17.689  1.00 42.29           N
ANISOU  793  N   ALA A 109     7152   4332   4586    276   1390    -10       N
ATOM    794  CA  ALA A 109      10.529   4.788 -18.982  1.00 45.02           C
ANISOU  794  CA  ALA A 109     7676   4582   4850    241   1409     -8       C
ATOM    795  C   ALA A 109       9.831   3.716 -19.812  1.00 46.67           C
ANISOU  795  C   ALA A 109     8067   4708   4960    245   1380     11       C
ATOM    796  O   ALA A 109       9.197   4.057 -20.821  1.00 44.64           O
ANISOU  796  O   ALA A 109     7966   4372   4621    213   1362     16       O
ATOM    797  CB  ALA A 109      11.713   5.392 -19.770  1.00 40.28           C
ANISOU  797  CB  ALA A 109     7104   3930   4269    244   1562    -24       C
ATOM    798  N   GLU A 110       9.879   2.455 -19.371  1.00 46.50           N
ANISOU  798  N   GLU A 110     8026   4701   4940    282   1366     24       N
ATOM    799  CA  GLU A 110       9.328   1.319 -20.099  1.00 41.84           C
ANISOU  799  CA  GLU A 110     7604   4032   4261    287   1348     41       C
ATOM    800  C   GLU A 110       7.812   1.405 -20.205  1.00 39.71           C
ANISOU  800  C   GLU A 110     7411   3753   3924    241   1203     51       C
ATOM    801  O   GLU A 110       7.145   2.217 -19.555  1.00 47.47           O
ANISOU  801  O   GLU A 110     8301   4800   4936    212   1110     47       O
ATOM    802  CB  GLU A 110       9.707   0.007 -19.416  1.00 45.93           C
ANISOU  802  CB  GLU A 110     8065   4581   4806    337   1360     51       C
ATOM    803  CG  GLU A 110      11.161  -0.413 -19.633  1.00 53.46           C
ANISOU  803  CG  GLU A 110     8996   5514   5802    391   1513     47       C
ATOM    804  CD  GLU A 110      12.102   0.151 -18.576  1.00 52.03           C
ANISOU  804  CD  GLU A 110     8598   5432   5737    416   1548     33       C
ATOM    805  OE1 GLU A 110      13.256  -0.329 -18.495  1.00 51.85           O
ANISOU  805  OE1 GLU A 110     8522   5414   5765    468   1655     31       O
ATOM    806  OE2 GLU A 110      11.677   1.065 -17.825  1.00 49.54           O
ANISOU  806  OE2 GLU A 110     8168   5191   5463    385   1467     23       O
ATOM    807  N   LYS A 111       7.274   0.581 -21.084  1.00 38.68           N
ANISOU  807  N   LYS A 111     7457   3538   3702    233   1187     64       N
ATOM    808  CA  LYS A 111       5.842   0.479 -21.286  1.00 40.73           C
ANISOU  808  CA  LYS A 111     7802   3780   3892    190   1050     75       C
ATOM    809  C   LYS A 111       5.349  -0.895 -20.840  1.00 40.83           C
ANISOU  809  C   LYS A 111     7827   3801   3884    202    992     89       C
ATOM    810  O   LYS A 111       6.108  -1.874 -20.834  1.00 36.33           O
ANISOU  810  O   LYS A 111     7275   3210   3319    244   1073     93       O
ATOM    811  CB  LYS A 111       5.494   0.692 -22.754  1.00 45.39           C
ANISOU  811  CB  LYS A 111     8605   4259   4382    160   1065     78       C
ATOM    812  CG  LYS A 111       5.763   2.089 -23.272  1.00 42.67           C
ANISOU  812  CG  LYS A 111     8272   3896   4043    141   1107     66       C
ATOM    813  CD  LYS A 111       5.389   2.119 -24.738  1.00 47.85           C
ANISOU  813  CD  LYS A 111     9158   4434   4588    116   1118     71       C
ATOM    814  CE  LYS A 111       5.590   3.478 -25.381  1.00 54.60           C
ANISOU  814  CE  LYS A 111    10055   5256   5433     96   1160     61       C
ATOM    815  NZ  LYS A 111       5.361   3.397 -26.870  1.00 60.78           N
ANISOU  815  NZ  LYS A 111    11079   5913   6101     78   1186     67       N
ATOM    816  N   GLY A 112       4.060  -0.956 -20.485  1.00 38.46           N
ANISOU  816  N   GLY A 112     7522   3529   3561    165    852     96       N
ATOM    817  CA  GLY A 112       3.432  -2.182 -20.077  1.00 32.37           C
ANISOU  817  CA  GLY A 112     6770   2764   2766    165    785    109       C
ATOM    818  C   GLY A 112       3.628  -2.463 -18.598  1.00 36.85           C
ANISOU  818  C   GLY A 112     7147   3434   3420    194    762    108       C
ATOM    819  O   GLY A 112       4.334  -1.745 -17.874  1.00 34.47           O
ANISOU  819  O   GLY A 112     6697   3202   3200    216    801     98       O
ATOM    820  N   PRO A 113       2.971  -3.514 -18.127  1.00 31.61           N
ANISOU  820  N   PRO A 113     6492   2781   2737    190    695    119       N
ATOM    821  CA  PRO A 113       3.105  -3.935 -16.720  1.00 37.34           C
ANISOU  821  CA  PRO A 113     7056   3597   3535    219    670    121       C
ATOM    822  C   PRO A 113       4.552  -4.272 -16.347  1.00 35.23           C
ANISOU  822  C   PRO A 113     6715   3348   3323    285    791    118       C
ATOM    823  O   PRO A 113       5.248  -5.001 -17.057  1.00 35.66           O
ANISOU  823  O   PRO A 113     6873   3334   3342    316    884    122       O
ATOM    824  CB  PRO A 113       2.199  -5.176 -16.638  1.00 35.57           C
ANISOU  824  CB  PRO A 113     6911   3346   3257    202    598    134       C
ATOM    825  CG  PRO A 113       1.230  -5.033 -17.812  1.00 36.53           C
ANISOU  825  CG  PRO A 113     7197   3390   3291    145    538    137       C
ATOM    826  CD  PRO A 113       2.026  -4.345 -18.891  1.00 32.77           C
ANISOU  826  CD  PRO A 113     6807   2854   2792    155    634    130       C
ATOM    827  N   LEU A 114       4.995  -3.737 -15.217  1.00 30.90           N
ANISOU  827  N   LEU A 114     5986   2894   2862    307    788    111       N
ATOM    828  CA  LEU A 114       6.374  -3.832 -14.777  1.00 34.58           C
ANISOU  828  CA  LEU A 114     6352   3392   3393    367    892    105       C
ATOM    829  C   LEU A 114       6.539  -4.909 -13.713  1.00 38.75           C
ANISOU  829  C   LEU A 114     6804   3968   3952    410    876    115       C
ATOM    830  O   LEU A 114       5.677  -5.091 -12.843  1.00 31.11           O
ANISOU  830  O   LEU A 114     5778   3051   2992    392    776    120       O
ATOM    831  CB  LEU A 114       6.852  -2.480 -14.236  1.00 37.29           C
ANISOU  831  CB  LEU A 114     6545   3808   3815    362    902     89       C
ATOM    832  CG  LEU A 114       6.862  -1.283 -15.192  1.00 35.90           C
ANISOU  832  CG  LEU A 114     6429   3591   3621    324    931     77       C
ATOM    833  CD1 LEU A 114       7.786  -0.190 -14.651  1.00 36.57           C
ANISOU  833  CD1 LEU A 114     6362   3742   3793    335    983     59       C
ATOM    834  CD2 LEU A 114       7.298  -1.721 -16.608  1.00 38.65           C
ANISOU  834  CD2 LEU A 114     6955   3828   3901    332   1027     81       C
ATOM    835  N   SER A 115       7.658  -5.620 -13.784  1.00 40.69           N
ANISOU  835  N   SER A 115     7051   4196   4216    471    979    119       N
ATOM    836  CA  SER A 115       7.946  -6.691 -12.845  1.00 39.04           C
ANISOU  836  CA  SER A 115     6779   4022   4030    523    976    130       C
ATOM    837  C   SER A 115       8.942  -6.262 -11.767  1.00 40.69           C
ANISOU  837  C   SER A 115     6797   4326   4339    570   1006    121       C
ATOM    838  O   SER A 115       9.616  -5.233 -11.857  1.00 38.57           O
ANISOU  838  O   SER A 115     6449   4084   4121    567   1051    106       O
ATOM    839  CB  SER A 115       8.429  -7.934 -13.604  1.00 43.40           C
ANISOU  839  CB  SER A 115     7472   4489   4530    564   1062    142       C
ATOM    840  OG  SER A 115       7.396  -8.408 -14.455  1.00 43.23           O
ANISOU  840  OG  SER A 115     7623   4387   4414    515   1016    149       O
ATOM    841  N   GLU A 116       9.014  -7.082 -10.721  1.00 39.54           N
ANISOU  841  N   GLU A 116     6579   4228   4218    611    976    131       N
ATOM    842  CA  GLU A 116       9.892  -6.790  -9.605  1.00 38.54           C
ANISOU  842  CA  GLU A 116     6273   4192   4180    657    988    125       C
ATOM    843  C   GLU A 116      11.346  -6.860 -10.010  1.00 49.78           C
ANISOU  843  C   GLU A 116     7667   5601   5645    716   1114    121       C
ATOM    844  O   GLU A 116      12.185  -6.259  -9.335  1.00 52.23           O
ANISOU  844  O   GLU A 116     7825   5983   6036    742   1135    110       O
ATOM    845  CB  GLU A 116       9.665  -7.786  -8.466  1.00 40.94           C
ANISOU  845  CB  GLU A 116     6528   4538   4490    694    933    139       C
ATOM    846  CG  GLU A 116       8.246  -7.818  -7.938  1.00 37.57           C
ANISOU  846  CG  GLU A 116     6118   4129   4028    639    812    144       C
ATOM    847  CD  GLU A 116       7.353  -8.691  -8.785  1.00 34.85           C
ANISOU  847  CD  GLU A 116     5952   3696   3593    608    795    156       C
ATOM    848  OE1 GLU A 116       6.132  -8.682  -8.515  1.00 29.94           O
ANISOU  848  OE1 GLU A 116     5354   3082   2942    555    699    159       O
ATOM    849  OE2 GLU A 116       7.881  -9.373  -9.711  1.00 34.82           O
ANISOU  849  OE2 GLU A 116     6065   3616   3551    637    879    163       O
ATOM    850  N   ASP A 117      11.668  -7.562 -11.106  1.00 49.70           N
ANISOU  850  N   ASP A 117     7801   5499   5584    736   1201    130       N
ATOM    851  CA  ASP A 117      13.074  -7.706 -11.450  1.00 57.16           C
ANISOU  851  CA  ASP A 117     8713   6430   6575    799   1328    128       C
ATOM    852  C   ASP A 117      13.666  -6.457 -12.112  1.00 61.29           C
ANISOU  852  C   ASP A 117     9204   6950   7135    771   1395    108       C
ATOM    853  O   ASP A 117      14.883  -6.278 -12.049  1.00 70.33           O
ANISOU  853  O   ASP A 117    10255   8117   8347    817   1485    101       O
ATOM    854  CB  ASP A 117      13.290  -8.983 -12.282  1.00 53.99           C
ANISOU  854  CB  ASP A 117     8472   5933   6110    841   1406    145       C
ATOM    855  CG  ASP A 117      12.295  -9.115 -13.398  1.00 59.80           C
ANISOU  855  CG  ASP A 117     9403   6574   6745    780   1386    148       C
ATOM    856  OD1 ASP A 117      11.410  -8.227 -13.465  1.00 60.42           O
ANISOU  856  OD1 ASP A 117     9483   6668   6808    710   1305    139       O
ATOM    857  OD2 ASP A 117      12.356 -10.117 -14.156  1.00 61.93           O
ANISOU  857  OD2 ASP A 117     9824   6756   6952    803   1444    161       O
ATOM    858  N   ILE A 118      12.875  -5.578 -12.728  1.00 61.39           N
ANISOU  858  N   ILE A 118     9285   6934   7108    699   1356     98       N
ATOM    859  CA  ILE A 118      13.457  -4.306 -13.121  1.00 61.90           C
ANISOU  859  CA  ILE A 118     9294   7010   7217    673   1411     78       C
ATOM    860  C   ILE A 118      13.811  -3.390 -11.972  1.00 60.46           C
ANISOU  860  C   ILE A 118     8910   6937   7126    669   1370     63       C
ATOM    861  O   ILE A 118      13.061  -3.225 -11.010  1.00 60.11           O
ANISOU  861  O   ILE A 118     8794   6956   7090    648   1258     63       O
ATOM    862  CB  ILE A 118      12.663  -3.572 -14.206  1.00 57.90           C
ANISOU  862  CB  ILE A 118     8924   6433   6641    604   1397     72       C
ATOM    863  CG1 ILE A 118      13.027  -3.892 -15.649  1.00 66.52           C
ANISOU  863  CG1 ILE A 118    10190   7413   7673    609   1506     76       C
ATOM    864  CG2 ILE A 118      11.599  -2.603 -13.682  1.00 56.60           C
ANISOU  864  CG2 ILE A 118     8708   6321   6476    541   1274     65       C
ATOM    865  CD1 ILE A 118      12.216  -3.133 -16.625  1.00 58.47           C
ANISOU  865  CD1 ILE A 118     9301   6331   6584    542   1479     71       C
ATOM    866  N   ASP A 119      15.065  -2.934 -12.031  1.00 71.43           N
ANISOU  866  N   ASP A 119    10206   8348   8587    697   1468     49       N
ATOM    867  CA  ASP A 119      15.603  -1.574 -12.173  1.00 71.07           C
ANISOU  867  CA  ASP A 119    10077   8330   8597    662   1509     26       C
ATOM    868  C   ASP A 119      14.620  -0.414 -12.200  1.00 63.02           C
ANISOU  868  C   ASP A 119     9072   7320   7553    585   1427     14       C
ATOM    869  O   ASP A 119      13.984  -0.148 -13.225  1.00 61.74           O
ANISOU  869  O   ASP A 119     9058   7082   7320    544   1432     16       O
ATOM    870  CB  ASP A 119      16.399  -1.613 -13.452  1.00 72.77           C
ANISOU  870  CB  ASP A 119    10392   8459   8799    675   1651     23       C
ATOM    871  CG  ASP A 119      17.541  -2.590 -13.369  1.00 85.01           C
ANISOU  871  CG  ASP A 119    11900  10008  10393    756   1746     32       C
ATOM    872  OD1 ASP A 119      18.652  -2.144 -13.020  1.00 94.56           O
ANISOU  872  OD1 ASP A 119    12967  11270  11693    780   1810     18       O
ATOM    873  OD2 ASP A 119      17.297  -3.820 -13.482  1.00 90.94           O
ANISOU  873  OD2 ASP A 119    12743  10718  11094    797   1742     53       O
ATOM    874  N   VAL A 120      14.553   0.301 -11.081  1.00 54.46           N
ANISOU  874  N   VAL A 120     7834   6330   6528    569   1355      2       N
ATOM    875  CA  VAL A 120      13.582   1.357 -10.867  1.00 46.87           C
ANISOU  875  CA  VAL A 120     6865   5391   5551    504   1265     -7       C
ATOM    876  C   VAL A 120      14.312   2.632 -10.448  1.00 48.28           C
ANISOU  876  C   VAL A 120     6905   5630   5809    481   1294    -33       C
ATOM    877  O   VAL A 120      15.440   2.601  -9.951  1.00 47.99           O
ANISOU  877  O   VAL A 120     6743   5643   5848    517   1350    -42       O
ATOM    878  CB  VAL A 120      12.555   0.922  -9.811  1.00 45.27           C
ANISOU  878  CB  VAL A 120     6625   5241   5332    501   1134      5       C
ATOM    879  CG1 VAL A 120      11.692  -0.184 -10.382  1.00 45.85           C
ANISOU  879  CG1 VAL A 120     6856   5245   5320    505   1104     28       C
ATOM    880  CG2 VAL A 120      13.273   0.426  -8.575  1.00 43.97           C
ANISOU  880  CG2 VAL A 120     6309   5161   5238    553   1123      5       C
ATOM    881  N   HIS A 121      13.685   3.766 -10.698  1.00 43.93           N
ANISOU  881  N   HIS A 121     6380   5071   5240    421   1260    -44       N
ATOM    882  CA  HIS A 121      14.306   5.013 -10.266  1.00 44.15           C
ANISOU  882  CA  HIS A 121     6281   5154   5338    393   1282    -69       C
ATOM    883  C   HIS A 121      13.209   6.049 -10.093  1.00 42.57           C
ANISOU  883  C   HIS A 121     6098   4965   5111    333   1193    -75       C
ATOM    884  O   HIS A 121      12.992   6.901 -10.963  1.00 42.62           O
ANISOU  884  O   HIS A 121     6189   4917   5086    292   1224    -82       O
ATOM    885  CB  HIS A 121      15.407   5.474 -11.238  1.00 44.68           C
ANISOU  885  CB  HIS A 121     6372   5172   5431    391   1422    -84       C
ATOM    886  CG  HIS A 121      15.113   5.179 -12.674  1.00 42.76           C
ANISOU  886  CG  HIS A 121     6323   4817   5107    384   1482    -73       C
ATOM    887  ND1 HIS A 121      15.314   3.932 -13.231  1.00 44.32           N
ANISOU  887  ND1 HIS A 121     6613   4959   5267    431   1531    -54       N
ATOM    888  CD2 HIS A 121      14.621   5.961 -13.662  1.00 39.45           C
ANISOU  888  CD2 HIS A 121     6029   4329   4633    336   1500    -77       C
ATOM    889  CE1 HIS A 121      14.957   3.961 -14.503  1.00 42.58           C
ANISOU  889  CE1 HIS A 121     6569   4640   4971    409   1575    -49       C
ATOM    890  NE2 HIS A 121      14.532   5.181 -14.787  1.00 41.65           N
ANISOU  890  NE2 HIS A 121     6473   4512   4840    353   1555    -62       N
ATOM    891  N   PRO A 122      12.495   5.977  -8.971  1.00 44.13           N
ANISOU  891  N   PRO A 122     6220   5229   5317    330   1082    -70       N
ATOM    892  CA  PRO A 122      11.365   6.887  -8.733  1.00 43.94           C
ANISOU  892  CA  PRO A 122     6210   5218   5269    279    991    -72       C
ATOM    893  C   PRO A 122      11.777   8.358  -8.594  1.00 49.05           C
ANISOU  893  C   PRO A 122     6781   5893   5961    238   1018    -98       C
ATOM    894  O   PRO A 122      12.899   8.691  -8.192  1.00 47.07           O
ANISOU  894  O   PRO A 122     6416   5685   5781    247   1078   -117       O
ATOM    895  CB  PRO A 122      10.755   6.335  -7.437  1.00 41.19           C
ANISOU  895  CB  PRO A 122     5777   4941   4933    296    885    -62       C
ATOM    896  CG  PRO A 122      11.934   5.696  -6.725  1.00 38.46           C
ANISOU  896  CG  PRO A 122     5314   4648   4650    347    928    -67       C
ATOM    897  CD  PRO A 122      12.690   5.029  -7.857  1.00 41.02           C
ANISOU  897  CD  PRO A 122     5729   4901   4957    378   1036    -61       C
ATOM    898  N   VAL A 123      10.822   9.242  -8.904  1.00 51.78           N
ANISOU  898  N   VAL A 123     7191   6214   6268    192    969    -99       N
ATOM    899  CA  VAL A 123      11.091  10.669  -9.072  1.00 53.12           C
ANISOU  899  CA  VAL A 123     7336   6385   6462    148   1005   -121       C
ATOM    900  C   VAL A 123      10.462  11.563  -8.013  1.00 56.41           C
ANISOU  900  C   VAL A 123     7661   6868   6905    118    916   -130       C
ATOM    901  O   VAL A 123      10.794  12.766  -7.979  1.00 58.07           O
ANISOU  901  O   VAL A 123     7831   7088   7144     83    947   -151       O
ATOM    902  CB  VAL A 123      10.654  11.153 -10.470  1.00 52.43           C
ANISOU  902  CB  VAL A 123     7413   6202   6308    120   1043   -116       C
ATOM    903  CG1 VAL A 123      11.425  10.409 -11.532  1.00 56.70           C
ANISOU  903  CG1 VAL A 123     8043   6672   6826    147   1148   -112       C
ATOM    904  CG2 VAL A 123       9.151  10.948 -10.663  1.00 49.14           C
ANISOU  904  CG2 VAL A 123     7096   5757   5819    108    937    -95       C
ATOM    905  N   ASN A 124       9.557  11.049  -7.177  1.00 47.41           N
ANISOU  905  N   ASN A 124     6492   5769   5752    129    813   -115       N
ATOM    906  CA  ASN A 124       8.915  11.835  -6.126  1.00 43.41           C
ANISOU  906  CA  ASN A 124     5903   5324   5268    104    730   -122       C
ATOM    907  C   ASN A 124       9.286  11.268  -4.760  1.00 43.64           C
ANISOU  907  C   ASN A 124     5796   5437   5349    133    690   -124       C
ATOM    908  O   ASN A 124       9.804  10.154  -4.658  1.00 43.92           O
ANISOU  908  O   ASN A 124     5816   5480   5393    175    710   -115       O
ATOM    909  CB  ASN A 124       7.395  11.876  -6.349  1.00 35.51           C
ANISOU  909  CB  ASN A 124     4993   4293   4206     87    641   -102       C
ATOM    910  CG  ASN A 124       6.700  10.532  -6.057  1.00 43.23           C
ANISOU  910  CG  ASN A 124     5996   5274   5153    116    575    -78       C
ATOM    911  OD1 ASN A 124       7.340   9.469  -5.903  1.00 40.51           O
ANISOU  911  OD1 ASN A 124     5632   4940   4821    154    604    -73       O
ATOM    912  ND2 ASN A 124       5.363  10.569  -6.052  1.00 44.05           N
ANISOU  912  ND2 ASN A 124     6154   5367   5216     99    489    -63       N
ATOM    913  N   VAL A 125       9.006  12.032  -3.697  1.00 42.16           N
ANISOU  913  N   VAL A 125     5514   5312   5193    111    632   -136       N
ATOM    914  CA  VAL A 125       9.540  11.657  -2.386  1.00 42.84           C
ANISOU  914  CA  VAL A 125     5466   5478   5331    136    602   -143       C
ATOM    915  C   VAL A 125       8.954  10.337  -1.895  1.00 42.32           C
ANISOU  915  C   VAL A 125     5413   5425   5240    175    540   -119       C
ATOM    916  O   VAL A 125       9.678   9.532  -1.285  1.00 40.40           O
ANISOU  916  O   VAL A 125     5101   5222   5029    215    547   -118       O
ATOM    917  CB  VAL A 125       9.353  12.777  -1.331  1.00 44.05           C
ANISOU  917  CB  VAL A 125     5525   5692   5519    102    554   -162       C
ATOM    918  CG1 VAL A 125      10.221  13.984  -1.672  1.00 49.39           C
ANISOU  918  CG1 VAL A 125     6168   6365   6233     66    627   -190       C
ATOM    919  CG2 VAL A 125       7.884  13.185  -1.167  1.00 46.67           C
ANISOU  919  CG2 VAL A 125     5912   6013   5809     78    473   -149       C
ATOM    920  N   TYR A 126       7.675  10.057  -2.192  1.00 37.33           N
ANISOU  920  N   TYR A 126     4874   4757   4552    165    480    -98       N
ATOM    921  CA  TYR A 126       7.067   8.813  -1.713  1.00 39.31           C
ANISOU  921  CA  TYR A 126     5140   5018   4778    196    422    -76       C
ATOM    922  C   TYR A 126       7.792   7.591  -2.274  1.00 38.68           C
ANISOU  922  C   TYR A 126     5103   4906   4688    241    479    -65       C
ATOM    923  O   TYR A 126       8.141   6.654  -1.537  1.00 33.39           O
ANISOU  923  O   TYR A 126     4381   4272   4034    281    466    -58       O
ATOM    924  CB  TYR A 126       5.603   8.752  -2.118  1.00 32.25           C
ANISOU  924  CB  TYR A 126     4343   4082   3827    173    357    -58       C
ATOM    925  CG  TYR A 126       4.794   7.732  -1.357  1.00 32.43           C
ANISOU  925  CG  TYR A 126     4361   4127   3832    191    284    -39       C
ATOM    926  CD1 TYR A 126       4.478   7.930  -0.021  1.00 36.41           C
ANISOU  926  CD1 TYR A 126     4771   4698   4367    190    225    -42       C
ATOM    927  CD2 TYR A 126       4.318   6.584  -1.973  1.00 27.28           C
ANISOU  927  CD2 TYR A 126     3807   3426   3131    206    275    -18       C
ATOM    928  CE1 TYR A 126       3.727   7.025   0.674  1.00 31.84           C
ANISOU  928  CE1 TYR A 126     4192   4136   3771    204    163    -25       C
ATOM    929  CE2 TYR A 126       3.537   5.688  -1.284  1.00 26.19           C
ANISOU  929  CE2 TYR A 126     3668   3305   2977    217    211     -2       C
ATOM    930  CZ  TYR A 126       3.260   5.907   0.034  1.00 28.05           C
ANISOU  930  CZ  TYR A 126     3806   3605   3244    217    158     -5       C
ATOM    931  OH  TYR A 126       2.497   5.005   0.731  1.00 36.57           O
ANISOU  931  OH  TYR A 126     4889   4699   4307    227    100     11       O
ATOM    932  N   GLY A 127       8.032   7.593  -3.584  1.00 36.02           N
ANISOU  932  N   GLY A 127     4866   4499   4322    235    546    -64       N
ATOM    933  CA  GLY A 127       8.753   6.489  -4.198  1.00 35.98           C
ANISOU  933  CA  GLY A 127     4910   4456   4305    277    612    -54       C
ATOM    934  C   GLY A 127      10.188   6.387  -3.721  1.00 40.65           C
ANISOU  934  C   GLY A 127     5389   5094   4964    313    676    -68       C
ATOM    935  O   GLY A 127      10.671   5.286  -3.433  1.00 41.94           O
ANISOU  935  O   GLY A 127     5532   5267   5134    363    689    -57       O
ATOM    936  N   LYS A 128      10.888   7.527  -3.633  1.00 42.16           N
ANISOU  936  N   LYS A 128     5503   5311   5203    287    715    -93       N
ATOM    937  CA  LYS A 128      12.268   7.532  -3.158  1.00 42.87           C
ANISOU  937  CA  LYS A 128     5473   5452   5365    315    772   -109       C
ATOM    938  C   LYS A 128      12.364   6.825  -1.797  1.00 44.34           C
ANISOU  938  C   LYS A 128     5555   5711   5579    354    706   -103       C
ATOM    939  O   LYS A 128      13.259   6.003  -1.563  1.00 48.65           O
ANISOU  939  O   LYS A 128     6051   6278   6156    406    740    -99       O
ATOM    940  CB  LYS A 128      12.796   8.979  -3.062  1.00 45.50           C
ANISOU  940  CB  LYS A 128     5730   5811   5746    269    803   -138       C
ATOM    941  CG  LYS A 128      12.760   9.897  -4.363  1.00 54.45           C
ANISOU  941  CG  LYS A 128     6962   6872   6854    225    874   -148       C
ATOM    942  CD  LYS A 128      12.532  11.422  -3.928  1.00 56.11           C
ANISOU  942  CD  LYS A 128     7118   7113   7087    167    847   -171       C
ATOM    943  CE  LYS A 128      12.259  12.487  -5.030  1.00 51.26           C
ANISOU  943  CE  LYS A 128     6604   6432   6442    119    895   -179       C
ATOM    944  NZ  LYS A 128      13.395  12.792  -5.958  1.00 58.32           N
ANISOU  944  NZ  LYS A 128     7513   7285   7360    113   1018   -195       N
ATOM    945  N   HIS A 129      11.434   7.124  -0.887  1.00 41.65           N
ANISOU  945  N   HIS A 129     5188   5410   5228    333    611   -101       N
ATOM    946  CA  HIS A 129      11.537   6.591   0.469  1.00 43.96           C
ANISOU  946  CA  HIS A 129     5383   5773   5546    366    548    -98       C
ATOM    947  C   HIS A 129      11.138   5.112   0.569  1.00 44.05           C
ANISOU  947  C   HIS A 129     5454   5765   5518    414    522    -70       C
ATOM    948  O   HIS A 129      11.802   4.335   1.268  1.00 43.00           O
ANISOU  948  O   HIS A 129     5255   5671   5411    465    519    -65       O
ATOM    949  CB  HIS A 129      10.690   7.448   1.403  1.00 43.71           C
ANISOU  949  CB  HIS A 129     5308   5785   5515    325    465   -106       C
ATOM    950  CG  HIS A 129      10.315   6.775   2.687  1.00 51.54           C
ANISOU  950  CG  HIS A 129     6248   6829   6505    353    387    -95       C
ATOM    951  ND1 HIS A 129       9.082   6.187   2.888  1.00 47.85           N
ANISOU  951  ND1 HIS A 129     5851   6343   5989    351    323    -74       N
ATOM    952  CD2 HIS A 129      11.001   6.618   3.846  1.00 57.14           C
ANISOU  952  CD2 HIS A 129     6844   7607   7257    381    360   -103       C
ATOM    953  CE1 HIS A 129       9.028   5.690   4.111  1.00 53.05           C
ANISOU  953  CE1 HIS A 129     6446   7054   6657    378    267    -69       C
ATOM    954  NE2 HIS A 129      10.181   5.934   4.712  1.00 59.36           N
ANISOU  954  NE2 HIS A 129     7138   7907   7510    398    286    -86       N
ATOM    955  N   LYS A 130      10.084   4.689  -0.130  1.00 41.16           N
ANISOU  955  N   LYS A 130     5214   5338   5088    400    503    -52       N
ATOM    956  CA  LYS A 130       9.690   3.280  -0.061  1.00 41.78           C
ANISOU  956  CA  LYS A 130     5355   5393   5126    440    481    -27       C
ATOM    957  C   LYS A 130      10.758   2.358  -0.644  1.00 39.94           C
ANISOU  957  C   LYS A 130     5143   5131   4901    495    564    -20       C
ATOM    958  O   LYS A 130      11.021   1.282  -0.093  1.00 39.70           O
ANISOU  958  O   LYS A 130     5097   5117   4871    548    554     -6       O
ATOM    959  CB  LYS A 130       8.354   3.079  -0.765  1.00 34.85           C
ANISOU  959  CB  LYS A 130     4607   4454   4180    406    444    -11       C
ATOM    960  CG  LYS A 130       7.213   3.747  -0.040  1.00 34.83           C
ANISOU  960  CG  LYS A 130     4580   4483   4171    363    356    -13       C
ATOM    961  CD  LYS A 130       6.954   3.132   1.317  1.00 36.74           C
ANISOU  961  CD  LYS A 130     4755   4781   4423    388    292     -5       C
ATOM    962  CE  LYS A 130       5.498   3.402   1.760  1.00 31.93           C
ANISOU  962  CE  LYS A 130     4170   4177   3787    348    209      3       C
ATOM    963  NZ  LYS A 130       5.268   2.856   3.116  1.00 31.81           N
ANISOU  963  NZ  LYS A 130     4092   4213   3782    370    153      9       N
ATOM    964  N   LEU A 131      11.403   2.763  -1.747  1.00 37.64           N
ANISOU  964  N   LEU A 131     4890   4796   4617    486    650    -29       N
ATOM    965  CA  LEU A 131      12.437   1.899  -2.319  1.00 43.91           C
ANISOU  965  CA  LEU A 131     5703   5560   5422    541    737    -23       C
ATOM    966  C   LEU A 131      13.609   1.730  -1.351  1.00 46.42           C
ANISOU  966  C   LEU A 131     5875   5952   5812    591    750    -31       C
ATOM    967  O   LEU A 131      14.172   0.629  -1.225  1.00 42.26           O
ANISOU  967  O   LEU A 131     5345   5422   5289    654    776    -16       O
ATOM    968  CB  LEU A 131      12.909   2.423  -3.675  1.00 42.59           C
ANISOU  968  CB  LEU A 131     5604   5328   5249    520    833    -32       C
ATOM    969  CG  LEU A 131      14.249   1.880  -4.219  1.00 43.49           C
ANISOU  969  CG  LEU A 131     5704   5422   5397    572    943    -33       C
ATOM    970  CD1 LEU A 131      14.279   0.346  -4.333  1.00 39.15           C
ANISOU  970  CD1 LEU A 131     5225   4838   4812    634    957     -7       C
ATOM    971  CD2 LEU A 131      14.513   2.508  -5.581  1.00 38.54           C
ANISOU  971  CD2 LEU A 131     5163   4724   4755    540   1035    -42       C
ATOM    972  N   GLU A 132      14.007   2.815  -0.681  1.00 46.22           N
ANISOU  972  N   GLU A 132     5729   5991   5843    563    731    -54       N
ATOM    973  CA  GLU A 132      15.101   2.722   0.271  1.00 47.44           C
ANISOU  973  CA  GLU A 132     5739   6220   6067    606    732    -63       C
ATOM    974  C   GLU A 132      14.711   1.833   1.440  1.00 46.21           C
ANISOU  974  C   GLU A 132     5555   6106   5897    647    649    -46       C
ATOM    975  O   GLU A 132      15.545   1.098   1.983  1.00 47.09           O
ANISOU  975  O   GLU A 132     5598   6252   6042    710    657    -40       O
ATOM    976  CB  GLU A 132      15.495   4.113   0.763  1.00 51.42           C
ANISOU  976  CB  GLU A 132     6128   6781   6627    558    721    -93       C
ATOM    977  CG  GLU A 132      16.715   4.095   1.696  1.00 63.38           C
ANISOU  977  CG  GLU A 132     7488   8376   8220    597    722   -107       C
ATOM    978  CD  GLU A 132      17.979   3.502   1.050  1.00 62.51           C
ANISOU  978  CD  GLU A 132     7350   8248   8151    650    822   -105       C
ATOM    979  OE1 GLU A 132      18.144   3.653  -0.181  1.00 63.77           O
ANISOU  979  OE1 GLU A 132     7589   8342   8299    635    910   -106       O
ATOM    980  OE2 GLU A 132      18.791   2.869   1.769  1.00 61.46           O
ANISOU  980  OE2 GLU A 132     7123   8167   8061    711    813   -101       O
ATOM    981  N   ALA A 133      13.441   1.881   1.832  1.00 46.12           N
ANISOU  981  N   ALA A 133     5596   6090   5836    613    569    -38       N
ATOM    982  CA  ALA A 133      12.969   1.031   2.918  1.00 46.83           C
ANISOU  982  CA  ALA A 133     5673   6212   5907    647    493    -21       C
ATOM    983  C   ALA A 133      13.143  -0.443   2.573  1.00 45.22           C
ANISOU  983  C   ALA A 133     5544   5965   5671    711    525      4       C
ATOM    984  O   ALA A 133      13.578  -1.246   3.415  1.00 42.90           O
ANISOU  984  O   ALA A 133     5202   5709   5392    769    503     14       O
ATOM    985  CB  ALA A 133      11.505   1.367   3.228  1.00 41.61           C
ANISOU  985  CB  ALA A 133     5067   5543   5198    594    414    -17       C
ATOM    986  N   GLU A 134      12.805  -0.816   1.337  1.00 40.80           N
ANISOU  986  N   GLU A 134     5110   5325   5065    701    577     14       N
ATOM    987  CA  GLU A 134      13.035  -2.182   0.893  1.00 41.07           C
ANISOU  987  CA  GLU A 134     5226   5310   5068    759    619     37       C
ATOM    988  C   GLU A 134      14.512  -2.510   0.949  1.00 45.49           C
ANISOU  988  C   GLU A 134     5702   5895   5686    826    689     34       C
ATOM    989  O   GLU A 134      14.896  -3.627   1.303  1.00 49.37           O
ANISOU  989  O   GLU A 134     6196   6387   6174    894    695     52       O
ATOM    990  CB  GLU A 134      12.529  -2.375  -0.530  1.00 39.52           C
ANISOU  990  CB  GLU A 134     5179   5021   4814    731    670     44       C
ATOM    991  CG  GLU A 134      11.061  -2.585  -0.693  1.00 35.49           C
ANISOU  991  CG  GLU A 134     4778   4471   4235    684    605     56       C
ATOM    992  CD  GLU A 134      10.669  -2.595  -2.163  1.00 36.01           C
ANISOU  992  CD  GLU A 134     4986   4448   4248    652    654     60       C
ATOM    993  OE1 GLU A 134       9.455  -2.519  -2.459  1.00 34.22           O
ANISOU  993  OE1 GLU A 134     4844   4187   3969    602    600     65       O
ATOM    994  OE2 GLU A 134      11.581  -2.672  -3.033  1.00 38.12           O
ANISOU  994  OE2 GLU A 134     5279   4677   4527    677    748     57       O
ATOM    995  N   ARG A 135      15.360  -1.549   0.582  1.00 44.86           N
ANISOU  995  N   ARG A 135     5547   5835   5664    808    744     12       N
ATOM    996  CA  ARG A 135      16.781  -1.841   0.488  1.00 44.85           C
ANISOU  996  CA  ARG A 135     5465   5852   5723    870    820      9       C
ATOM    997  C   ARG A 135      17.334  -2.206   1.853  1.00 50.23           C
ANISOU  997  C   ARG A 135     6021   6616   6449    924    763     11       C
ATOM    998  O   ARG A 135      18.039  -3.216   1.993  1.00 51.39           O
ANISOU  998  O   ARG A 135     6152   6763   6609   1002    793     27       O
ATOM    999  CB  ARG A 135      17.507  -0.625  -0.090  1.00 51.26           C
ANISOU  999  CB  ARG A 135     6214   6673   6590    828    885    -18       C
ATOM   1000  CG  ARG A 135      18.842  -0.856  -0.802  1.00 58.32           C
ANISOU 1000  CG  ARG A 135     7073   7550   7537    875   1000    -22       C
ATOM   1001  CD  ARG A 135      19.346   0.480  -1.402  1.00 59.48           C
ANISOU 1001  CD  ARG A 135     7172   7698   7729    816   1061    -51       C
ATOM   1002  NE  ARG A 135      20.754   0.461  -1.794  1.00 61.28           N
ANISOU 1002  NE  ARG A 135     7320   7935   8031    855   1164    -60       N
ATOM   1003  CZ  ARG A 135      21.189   0.222  -3.034  1.00 61.25           C
ANISOU 1003  CZ  ARG A 135     7399   7857   8019    867   1278    -56       C
ATOM   1004  NH1 ARG A 135      20.321  -0.027  -4.008  1.00 63.67           N
ANISOU 1004  NH1 ARG A 135     7876   8075   8242    842   1299    -44       N
ATOM   1005  NH2 ARG A 135      22.492   0.216  -3.305  1.00 59.70           N
ANISOU 1005  NH2 ARG A 135     7115   7673   7897    904   1373    -65       N
ATOM   1006  N   LYS A 136      16.928  -1.472   2.895  1.00 49.81           N
ANISOU 1006  N   LYS A 136     5888   6627   6409    887    675     -2       N
ATOM   1007  CA  LYS A 136      17.409  -1.813   4.232  1.00 52.90           C
ANISOU 1007  CA  LYS A 136     6169   7095   6836    937    612      0       C
ATOM   1008  C   LYS A 136      16.802  -3.123   4.742  1.00 54.38           C
ANISOU 1008  C   LYS A 136     6432   7264   6966    987    566     30       C
ATOM   1009  O   LYS A 136      17.490  -3.911   5.406  1.00 54.17           O
ANISOU 1009  O   LYS A 136     6352   7270   6961   1062    557     42       O
ATOM   1010  CB  LYS A 136      17.161  -0.654   5.193  1.00 47.35           C
ANISOU 1010  CB  LYS A 136     5370   6461   6160    881    535    -23       C
ATOM   1011  CG  LYS A 136      17.967   0.595   4.844  1.00 48.39           C
ANISOU 1011  CG  LYS A 136     5408   6620   6357    839    582    -53       C
ATOM   1012  CD  LYS A 136      19.439   0.303   4.725  1.00 54.96           C
ANISOU 1012  CD  LYS A 136     6143   7480   7260    898    647    -58       C
ATOM   1013  CE  LYS A 136      20.022  -0.178   6.041  1.00 56.45           C
ANISOU 1013  CE  LYS A 136     6220   7745   7483    958    580    -54       C
ATOM   1014  NZ  LYS A 136      19.892   0.841   7.106  1.00 58.11           N
ANISOU 1014  NZ  LYS A 136     6334   8027   7717    909    497    -77       N
ATOM   1015  N   LEU A 137      15.519  -3.375   4.454  1.00 49.64           N
ANISOU 1015  N   LEU A 137     5956   6610   6293    948    536     42       N
ATOM   1016  CA  LEU A 137      14.891  -4.612   4.917  1.00 49.40           C
ANISOU 1016  CA  LEU A 137     6005   6558   6208    988    496     69       C
ATOM   1017  C   LEU A 137      15.529  -5.857   4.307  1.00 50.63           C
ANISOU 1017  C   LEU A 137     6223   6664   6351   1064    569     90       C
ATOM   1018  O   LEU A 137      15.708  -6.866   5.000  1.00 49.22           O
ANISOU 1018  O   LEU A 137     6044   6496   6160   1130    546    109       O
ATOM   1019  CB  LEU A 137      13.410  -4.596   4.599  1.00 43.23           C
ANISOU 1019  CB  LEU A 137     5342   5727   5358    925    457     75       C
ATOM   1020  CG  LEU A 137      12.615  -3.949   5.703  1.00 42.81           C
ANISOU 1020  CG  LEU A 137     5238   5726   5303    881    364     67       C
ATOM   1021  CD1 LEU A 137      11.371  -3.467   5.045  1.00 40.63           C
ANISOU 1021  CD1 LEU A 137     5053   5403   4981    805    347     65       C
ATOM   1022  CD2 LEU A 137      12.312  -4.936   6.831  1.00 35.37           C
ANISOU 1022  CD2 LEU A 137     4301   4805   4334    927    304     85       C
ATOM   1023  N   GLN A 138      15.800  -5.840   2.998  1.00 52.66           N
ANISOU 1023  N   GLN A 138     6547   6858   6602   1056    657     89       N
ATOM   1024  CA  GLN A 138      16.471  -6.984   2.375  1.00 56.33           C
ANISOU 1024  CA  GLN A 138     7072   7273   7057   1129    736    108       C
ATOM   1025  C   GLN A 138      17.891  -7.168   2.898  1.00 59.00           C
ANISOU 1025  C   GLN A 138     7278   7668   7471   1209    767    107       C
ATOM   1026  O   GLN A 138      18.403  -8.294   2.910  1.00 54.44           O
ANISOU 1026  O   GLN A 138     6727   7070   6887   1290    802    128       O
ATOM   1027  CB  GLN A 138      16.422  -6.886   0.847  1.00 59.42           C
ANISOU 1027  CB  GLN A 138     7574   7581   7423   1100    826    106       C
ATOM   1028  CG  GLN A 138      14.985  -6.971   0.390  1.00 58.85           C
ANISOU 1028  CG  GLN A 138     7643   7449   7269   1034    785    113       C
ATOM   1029  CD  GLN A 138      14.362  -8.310   0.777  1.00 58.47           C
ANISOU 1029  CD  GLN A 138     7686   7369   7159   1070    750    139       C
ATOM   1030  OE1 GLN A 138      14.981  -9.369   0.628  1.00 60.74           O
ANISOU 1030  OE1 GLN A 138     8010   7627   7441   1144    802    156       O
ATOM   1031  NE2 GLN A 138      13.163  -8.245   1.376  1.00 55.56           N
ANISOU 1031  NE2 GLN A 138     7347   7011   6751   1022    660    141       N
ATOM   1032  N   GLU A 139      18.569  -6.074   3.247  1.00 73.47           N
ANISOU 1032  N   GLU A 139     8970   9568   9375   1187    760     82       N
ATOM   1033  CA  GLU A 139      19.894  -6.199   3.839  1.00 71.49           C
ANISOU 1033  CA  GLU A 139     8579   9382   9202   1259    775     79       C
ATOM   1034  C   GLU A 139      19.800  -6.858   5.214  1.00 69.35           C
ANISOU 1034  C   GLU A 139     8264   9165   8922   1312    684     94       C
ATOM   1035  O   GLU A 139      20.508  -7.836   5.486  1.00 74.46           O
ANISOU 1035  O   GLU A 139     8892   9817   9583   1402    702    113       O
ATOM   1036  CB  GLU A 139      20.573  -4.817   3.917  1.00 73.02           C
ANISOU 1036  CB  GLU A 139     8634   9636   9473   1211    783     47       C
ATOM   1037  CG  GLU A 139      21.895  -4.764   4.700  1.00 76.96           C
ANISOU 1037  CG  GLU A 139     8964  10218  10061   1272    777     39       C
ATOM   1038  CD  GLU A 139      22.244  -3.362   5.223  1.00 79.29           C
ANISOU 1038  CD  GLU A 139     9120  10587  10418   1209    739      5       C
ATOM   1039  OE1 GLU A 139      21.950  -2.356   4.532  1.00 74.95           O
ANISOU 1039  OE1 GLU A 139     8592  10014   9869   1130    772    -16       O
ATOM   1040  OE2 GLU A 139      22.819  -3.270   6.333  1.00 74.68           O
ANISOU 1040  OE2 GLU A 139     8410  10085   9882   1240    675     -2       O
ATOM   1041  N   ILE A 140      18.906  -6.364   6.082  1.00 59.28           N
ANISOU 1041  N   ILE A 140     6979   7924   7621   1259    587     87       N
ATOM   1042  CA  ILE A 140      18.833  -6.848   7.465  1.00 54.56           C
ANISOU 1042  CA  ILE A 140     6334   7380   7015   1303    497     97       C
ATOM   1043  C   ILE A 140      17.959  -8.092   7.619  1.00 50.58           C
ANISOU 1043  C   ILE A 140     5965   6822   6430   1334    475    127       C
ATOM   1044  O   ILE A 140      18.310  -9.006   8.374  1.00 48.77           O
ANISOU 1044  O   ILE A 140     5724   6611   6195   1412    449    146       O
ATOM   1045  CB  ILE A 140      18.367  -5.737   8.419  1.00 48.25           C
ANISOU 1045  CB  ILE A 140     5456   6646   6229   1237    408     75       C
ATOM   1046  CG1 ILE A 140      19.155  -4.461   8.176  1.00 52.11           C
ANISOU 1046  CG1 ILE A 140     5825   7180   6793   1195    435     44       C
ATOM   1047  CG2 ILE A 140      18.566  -6.181   9.849  1.00 48.82           C
ANISOU 1047  CG2 ILE A 140     5465   6781   6305   1291    324     84       C
ATOM   1048  CD1 ILE A 140      18.543  -3.263   8.787  1.00 48.36           C
ANISOU 1048  CD1 ILE A 140     5305   6747   6320   1113    366     20       C
ATOM   1049  N   LEU A 141      16.809  -8.167   6.952  1.00 44.62           N
ANISOU 1049  N   LEU A 141     5341   6000   5611   1274    482    132       N
ATOM   1050  CA  LEU A 141      15.851  -9.255   7.168  1.00 43.66           C
ANISOU 1050  CA  LEU A 141     5346   5830   5413   1287    453    157       C
ATOM   1051  C   LEU A 141      15.622 -10.047   5.891  1.00 42.70           C
ANISOU 1051  C   LEU A 141     5367   5614   5245   1294    532    172       C
ATOM   1052  O   LEU A 141      14.616  -9.834   5.206  1.00 43.03           O
ANISOU 1052  O   LEU A 141     5507   5604   5239   1223    532    169       O
ATOM   1053  CB  LEU A 141      14.506  -8.728   7.649  1.00 43.14           C
ANISOU 1053  CB  LEU A 141     5315   5769   5306   1206    375    150       C
ATOM   1054  CG  LEU A 141      14.385  -8.308   9.096  1.00 47.66           C
ANISOU 1054  CG  LEU A 141     5795   6418   5895   1203    284    142       C
ATOM   1055  CD1 LEU A 141      13.130  -7.502   9.173  1.00 42.38           C
ANISOU 1055  CD1 LEU A 141     5158   5744   5199   1110    236    130       C
ATOM   1056  CD2 LEU A 141      14.338  -9.542  10.037  1.00 45.63           C
ANISOU 1056  CD2 LEU A 141     5573   6161   5602   1276    247    168       C
ATOM   1057  N   PRO A 142      16.484 -11.011   5.578  1.00 40.12           N
ANISOU 1057  N   PRO A 142     5060   5260   4924   1379    596    189       N
ATOM   1058  CA  PRO A 142      16.347 -11.726   4.300  1.00 41.54           C
ANISOU 1058  CA  PRO A 142     5379   5345   5058   1385    681    202       C
ATOM   1059  C   PRO A 142      15.038 -12.504   4.171  1.00 40.98           C
ANISOU 1059  C   PRO A 142     5465   5209   4899   1350    650    218       C
ATOM   1060  O   PRO A 142      14.641 -12.837   3.047  1.00 40.62           O
ANISOU 1060  O   PRO A 142     5544   5082   4806   1323    704    223       O
ATOM   1061  CB  PRO A 142      17.576 -12.653   4.279  1.00 42.16           C
ANISOU 1061  CB  PRO A 142     5432   5420   5166   1496    746    220       C
ATOM   1062  CG  PRO A 142      18.504 -12.109   5.340  1.00 42.95           C
ANISOU 1062  CG  PRO A 142     5354   5620   5345   1536    703    209       C
ATOM   1063  CD  PRO A 142      17.599 -11.528   6.384  1.00 42.54           C
ANISOU 1063  CD  PRO A 142     5269   5619   5277   1477    593    199       C
ATOM   1064  N   THR A 143      14.391 -12.858   5.285  1.00 36.53           N
ANISOU 1064  N   THR A 143     4900   4673   4307   1351    569    227       N
ATOM   1065  CA  THR A 143      13.079 -13.497   5.253  1.00 37.12           C
ANISOU 1065  CA  THR A 143     5109   4691   4303   1307    534    239       C
ATOM   1066  C   THR A 143      11.929 -12.504   5.103  1.00 38.93           C
ANISOU 1066  C   THR A 143     5348   4925   4518   1200    482    221       C
ATOM   1067  O   THR A 143      10.775 -12.942   4.930  1.00 37.83           O
ANISOU 1067  O   THR A 143     5320   4737   4318   1152    455    229       O
ATOM   1068  CB  THR A 143      12.881 -14.356   6.508  1.00 38.41           C
ANISOU 1068  CB  THR A 143     5274   4876   4442   1357    477    257       C
ATOM   1069  OG1 THR A 143      12.598 -13.523   7.633  1.00 31.91           O
ANISOU 1069  OG1 THR A 143     4346   4132   3648   1326    394    244       O
ATOM   1070  CG2 THR A 143      14.152 -15.184   6.812  1.00 50.18           C
ANISOU 1070  CG2 THR A 143     6727   6379   5959   1474    520    274       C
ATOM   1071  N   SER A 144      12.213 -11.195   5.159  1.00 36.69           N
ANISOU 1071  N   SER A 144     4953   4697   4290   1161    467    198       N
ATOM   1072  CA  SER A 144      11.176 -10.171   5.085  1.00 35.69           C
ANISOU 1072  CA  SER A 144     4825   4579   4155   1066    417    181       C
ATOM   1073  C   SER A 144      10.571 -10.100   3.696  1.00 34.76           C
ANISOU 1073  C   SER A 144     4825   4385   3997   1010    458    180       C
ATOM   1074  O   SER A 144      11.233 -10.323   2.691  1.00 37.66           O
ANISOU 1074  O   SER A 144     5236   4708   4366   1034    537    181       O
ATOM   1075  CB  SER A 144      11.745  -8.806   5.402  1.00 37.70           C
ANISOU 1075  CB  SER A 144     4939   4906   4478   1043    402    157       C
ATOM   1076  OG  SER A 144      12.677  -8.461   4.388  1.00 42.32           O
ANISOU 1076  OG  SER A 144     5508   5473   5098   1056    484    148       O
ATOM   1077  N   VAL A 145       9.318  -9.702   3.644  1.00 34.24           N
ANISOU 1077  N   VAL A 145     4806   4306   3899    933    404    175       N
ATOM   1078  CA  VAL A 145       8.555  -9.671   2.412  1.00 33.22           C
ANISOU 1078  CA  VAL A 145     4796   4103   3722    874    424    175       C
ATOM   1079  C   VAL A 145       8.067  -8.254   2.203  1.00 28.04           C
ANISOU 1079  C   VAL A 145     4090   3475   3090    800    392    155       C
ATOM   1080  O   VAL A 145       7.377  -7.712   3.062  1.00 30.41           O
ANISOU 1080  O   VAL A 145     4332   3821   3400    765    320    149       O
ATOM   1081  CB  VAL A 145       7.367 -10.642   2.493  1.00 32.11           C
ANISOU 1081  CB  VAL A 145     4772   3914   3514    849    384    192       C
ATOM   1082  CG1 VAL A 145       6.671 -10.696   1.165  1.00 34.87           C
ANISOU 1082  CG1 VAL A 145     5249   4186   3814    793    404    192       C
ATOM   1083  CG2 VAL A 145       7.849 -12.029   2.909  1.00 30.13           C
ANISOU 1083  CG2 VAL A 145     4564   3642   3240    925    411    212       C
ATOM   1084  N   SER A 146       8.366  -7.673   1.057  1.00 28.20           N
ANISOU 1084  N   SER A 146     4142   3461   3114    777    445    145       N
ATOM   1085  CA  SER A 146       7.874  -6.341   0.718  1.00 32.15           C
ANISOU 1085  CA  SER A 146     4613   3974   3629    707    420    127       C
ATOM   1086  C   SER A 146       6.794  -6.438  -0.349  1.00 30.13           C
ANISOU 1086  C   SER A 146     4492   3644   3311    649    409    131       C
ATOM   1087  O   SER A 146       6.977  -7.123  -1.363  1.00 28.71           O
ANISOU 1087  O   SER A 146     4422   3394   3092    662    465    140       O
ATOM   1088  CB  SER A 146       8.999  -5.432   0.253  1.00 30.54           C
ANISOU 1088  CB  SER A 146     4337   3790   3479    718    484    109       C
ATOM   1089  OG  SER A 146       9.734  -5.057   1.387  1.00 32.51           O
ANISOU 1089  OG  SER A 146     4443   4120   3788    751    465    100       O
ATOM   1090  N   LEU A 147       5.647  -5.802  -0.080  1.00 29.77           N
ANISOU 1090  N   LEU A 147     4439   3615   3256    586    335    127       N
ATOM   1091  CA  LEU A 147       4.486  -5.838  -0.962  1.00 28.97           C
ANISOU 1091  CA  LEU A 147     4454   3454   3100    526    306    131       C
ATOM   1092  C   LEU A 147       4.293  -4.465  -1.594  1.00 27.24           C
ANISOU 1092  C   LEU A 147     4217   3236   2896    476    302    115       C
ATOM   1093  O   LEU A 147       4.023  -3.482  -0.898  1.00 29.86           O
ANISOU 1093  O   LEU A 147     4454   3626   3266    451    258    104       O
ATOM   1094  CB  LEU A 147       3.237  -6.262  -0.188  1.00 26.89           C
ANISOU 1094  CB  LEU A 147     4201   3203   2813    495    224    141       C
ATOM   1095  CG  LEU A 147       3.243  -7.536   0.682  1.00 31.26           C
ANISOU 1095  CG  LEU A 147     4764   3761   3351    537    214    156       C
ATOM   1096  CD1 LEU A 147       1.868  -7.675   1.379  1.00 26.24           C
ANISOU 1096  CD1 LEU A 147     4134   3138   2698    489    132    162       C
ATOM   1097  CD2 LEU A 147       3.593  -8.846  -0.097  1.00 27.10           C
ANISOU 1097  CD2 LEU A 147     4361   3159   2774    572    271    171       C
ATOM   1098  N   ARG A 148       4.392  -4.390  -2.908  1.00 28.19           N
ANISOU 1098  N   ARG A 148     4437   3290   2983    460    349    115       N
ATOM   1099  CA  ARG A 148       4.207  -3.100  -3.571  1.00 26.77           C
ANISOU 1099  CA  ARG A 148     4254   3105   2812    414    348    101       C
ATOM   1100  C   ARG A 148       2.709  -2.872  -3.768  1.00 26.85           C
ANISOU 1100  C   ARG A 148     4321   3097   2784    352    265    106       C
ATOM   1101  O   ARG A 148       2.073  -3.495  -4.622  1.00 26.56           O
ANISOU 1101  O   ARG A 148     4409   2993   2688    330    255    116       O
ATOM   1102  CB  ARG A 148       4.992  -3.060  -4.874  1.00 27.32           C
ANISOU 1102  CB  ARG A 148     4407   3112   2863    425    437     97       C
ATOM   1103  CG  ARG A 148       6.534  -3.103  -4.609  1.00 31.55           C
ANISOU 1103  CG  ARG A 148     4859   3677   3452    486    522     90       C
ATOM   1104  CD  ARG A 148       7.417  -3.140  -5.891  1.00 31.84           C
ANISOU 1104  CD  ARG A 148     4976   3648   3475    503    627     87       C
ATOM   1105  NE  ARG A 148       8.815  -2.903  -5.538  1.00 31.59           N
ANISOU 1105  NE  ARG A 148     4835   3658   3511    552    699     77       N
ATOM   1106  CZ  ARG A 148       9.834  -2.852  -6.397  1.00 31.32           C
ANISOU 1106  CZ  ARG A 148     4828   3585   3488    577    801     71       C
ATOM   1107  NH1 ARG A 148       9.643  -3.005  -7.711  1.00 31.30           N
ANISOU 1107  NH1 ARG A 148     4972   3494   3427    558    849     75       N
ATOM   1108  NH2 ARG A 148      11.054  -2.617  -5.926  1.00 29.74           N
ANISOU 1108  NH2 ARG A 148     4507   3435   3358    619    856     61       N
ATOM   1109  N   LEU A 149       2.130  -2.006  -2.930  1.00 28.51           N
ANISOU 1109  N   LEU A 149     4438   3366   3029    325    202     98       N
ATOM   1110  CA  LEU A 149       0.701  -1.737  -2.919  1.00 25.49           C
ANISOU 1110  CA  LEU A 149     4082   2979   2623    270    119    103       C
ATOM   1111  C   LEU A 149       0.347  -0.609  -3.896  1.00 27.08           C
ANISOU 1111  C   LEU A 149     4325   3152   2814    228    114     95       C
ATOM   1112  O   LEU A 149       1.180   0.230  -4.258  1.00 28.45           O
ANISOU 1112  O   LEU A 149     4471   3329   3011    237    168     83       O
ATOM   1113  CB  LEU A 149       0.278  -1.357  -1.525  1.00 25.00           C
ANISOU 1113  CB  LEU A 149     3903   2992   2605    266     62    100       C
ATOM   1114  CG  LEU A 149       0.839  -2.240  -0.415  1.00 27.64           C
ANISOU 1114  CG  LEU A 149     4178   3365   2958    315     72    106       C
ATOM   1115  CD1 LEU A 149       0.261  -1.819   0.971  1.00 24.56           C
ANISOU 1115  CD1 LEU A 149     3684   3044   2603    304      9    103       C
ATOM   1116  CD2 LEU A 149       0.578  -3.700  -0.716  1.00 25.37           C
ANISOU 1116  CD2 LEU A 149     3993   3026   2621    328     77    122       C
ATOM   1117  N   THR A 150      -0.913  -0.562  -4.295  1.00 26.98           N
ANISOU 1117  N   THR A 150     4373   3111   2765    183     47    103       N
ATOM   1118  CA  THR A 150      -1.349   0.520  -5.166  1.00 27.77           C
ANISOU 1118  CA  THR A 150     4512   3186   2853    145     31     98       C
ATOM   1119  C   THR A 150      -2.214   1.494  -4.380  1.00 26.55           C
ANISOU 1119  C   THR A 150     4266   3086   2734    117    -39     94       C
ATOM   1120  O   THR A 150      -2.477   1.291  -3.183  1.00 26.50           O
ANISOU 1120  O   THR A 150     4173   3136   2761    124    -72     96       O
ATOM   1121  CB  THR A 150      -2.109  -0.026  -6.363  1.00 25.65           C
ANISOU 1121  CB  THR A 150     4389   2841   2517    115      6    108       C
ATOM   1122  OG1 THR A 150      -3.456  -0.309  -5.958  1.00 25.41           O
ANISOU 1122  OG1 THR A 150     4355   2822   2477     80    -85    118       O
ATOM   1123  CG2 THR A 150      -1.420  -1.253  -6.883  1.00 26.11           C
ANISOU 1123  CG2 THR A 150     4537   2848   2537    145     67    115       C
ATOM   1124  N   TRP A 151      -2.632   2.571  -5.054  1.00 25.90           N
ANISOU 1124  N   TRP A 151     4209   2987   2645     87    -57     90       N
ATOM   1125  CA  TRP A 151      -3.688   3.410  -4.519  1.00 26.92           C
ANISOU 1125  CA  TRP A 151     4278   3153   2797     57   -130     90       C
ATOM   1126  C   TRP A 151      -4.897   2.521  -4.268  1.00 30.62           C
ANISOU 1126  C   TRP A 151     4772   3616   3245     35   -204    105       C
ATOM   1127  O   TRP A 151      -5.188   1.620  -5.076  1.00 25.20           O
ANISOU 1127  O   TRP A 151     4192   2875   2509     24   -212    115       O
ATOM   1128  CB  TRP A 151      -4.045   4.542  -5.499  1.00 33.23           C
ANISOU 1128  CB  TRP A 151     5129   3917   3578     31   -142     87       C
ATOM   1129  CG  TRP A 151      -4.878   5.713  -4.870  1.00 34.24           C
ANISOU 1129  CG  TRP A 151     5176   4091   3742     10   -200     85       C
ATOM   1130  CD1 TRP A 151      -4.924   6.089  -3.527  1.00 33.32           C
ANISOU 1130  CD1 TRP A 151     4935   4045   3680     18   -215     79       C
ATOM   1131  CD2 TRP A 151      -5.746   6.621  -5.551  1.00 25.42           C
ANISOU 1131  CD2 TRP A 151     4100   2949   2608    -17   -247     89       C
ATOM   1132  NE1 TRP A 151      -5.744   7.155  -3.366  1.00 25.70           N
ANISOU 1132  NE1 TRP A 151     3935   3097   2731     -4   -262     79       N
ATOM   1133  CE2 TRP A 151      -6.263   7.508  -4.586  1.00 26.71           C
ANISOU 1133  CE2 TRP A 151     4159   3169   2819    -23   -283     86       C
ATOM   1134  CE3 TRP A 151      -6.128   6.782  -6.884  1.00 35.22           C
ANISOU 1134  CE3 TRP A 151     5460   4125   3798    -35   -262     96       C
ATOM   1135  CZ2 TRP A 151      -7.162   8.521  -4.910  1.00 30.93           C
ANISOU 1135  CZ2 TRP A 151     4701   3697   3352    -44   -334     90       C
ATOM   1136  CZ3 TRP A 151      -7.015   7.822  -7.212  1.00 35.01           C
ANISOU 1136  CZ3 TRP A 151     5441   4093   3769    -56   -317    100       C
ATOM   1137  CH2 TRP A 151      -7.516   8.669  -6.226  1.00 30.58           C
ANISOU 1137  CH2 TRP A 151     4771   3589   3258    -58   -351     97       C
ATOM   1138  N   MET A 152      -5.528   2.692  -3.096  1.00 31.29           N
ANISOU 1138  N   MET A 152     4760   3759   3369     28   -252    107       N
ATOM   1139  CA  MET A 152      -6.644   1.850  -2.676  1.00 28.34           C
ANISOU 1139  CA  MET A 152     4393   3389   2987      6   -316    119       C
ATOM   1140  C   MET A 152      -7.947   2.637  -2.445  1.00 33.85           C
ANISOU 1140  C   MET A 152     5049   4108   3704    -29   -392    124       C
ATOM   1141  O   MET A 152      -8.009   3.865  -2.498  1.00 26.94           O
ANISOU 1141  O   MET A 152     4134   3249   2851    -33   -397    117       O
ATOM   1142  CB  MET A 152      -6.251   1.046  -1.439  1.00 27.80           C
ANISOU 1142  CB  MET A 152     4258   3362   2942     34   -299    120       C
ATOM   1143  CG  MET A 152      -4.968   0.229  -1.625  1.00 29.29           C
ANISOU 1143  CG  MET A 152     4482   3532   3115     76   -225    118       C
ATOM   1144  SD  MET A 152      -4.398  -0.611  -0.125  1.00 25.21           S
ANISOU 1144  SD  MET A 152     3883   3068   2627    118   -206    119       S
ATOM   1145  CE  MET A 152      -5.925  -1.088   0.531  1.00 30.55           C
ANISOU 1145  CE  MET A 152     4552   3755   3301     79   -284    131       C
ATOM   1146  N   TYR A 153      -9.010   1.893  -2.157  1.00 34.53           N
ANISOU 1146  N   TYR A 153     5142   4194   3784    -54   -449    135       N
ATOM   1147  CA  TYR A 153     -10.292   2.524  -1.878  1.00 37.49           C
ANISOU 1147  CA  TYR A 153     5469   4591   4183    -86   -520    140       C
ATOM   1148  C   TYR A 153     -11.159   1.493  -1.175  1.00 38.51           C
ANISOU 1148  C   TYR A 153     5581   4732   4318   -106   -560    149       C
ATOM   1149  O   TYR A 153     -11.085   0.289  -1.467  1.00 32.86           O
ANISOU 1149  O   TYR A 153     4937   3983   3567   -110   -552    155       O
ATOM   1150  CB  TYR A 153     -10.982   3.036  -3.162  1.00 30.33           C
ANISOU 1150  CB  TYR A 153     4640   3638   3246   -115   -565    145       C
ATOM   1151  CG  TYR A 153     -11.231   1.916  -4.140  1.00 31.61           C
ANISOU 1151  CG  TYR A 153     4920   3739   3350   -136   -582    153       C
ATOM   1152  CD1 TYR A 153     -12.292   1.056  -3.963  1.00 32.66           C
ANISOU 1152  CD1 TYR A 153     5064   3868   3478   -169   -641    163       C
ATOM   1153  CD2 TYR A 153     -10.391   1.702  -5.222  1.00 32.63           C
ANISOU 1153  CD2 TYR A 153     5154   3813   3431   -124   -535    150       C
ATOM   1154  CE1 TYR A 153     -12.512  -0.008  -4.801  1.00 35.72           C
ANISOU 1154  CE1 TYR A 153     5562   4199   3812   -192   -657    168       C
ATOM   1155  CE2 TYR A 153     -10.609   0.628  -6.108  1.00 33.09           C
ANISOU 1155  CE2 TYR A 153     5330   3811   3431   -144   -549    157       C
ATOM   1156  CZ  TYR A 153     -11.692  -0.234  -5.886  1.00 37.53           C
ANISOU 1156  CZ  TYR A 153     5902   4372   3988   -180   -613    165       C
ATOM   1157  OH  TYR A 153     -11.983  -1.343  -6.708  1.00 35.46           O
ANISOU 1157  OH  TYR A 153     5757   4048   3667   -207   -631    171       O
ATOM   1158  N   ASP A 154     -11.987   1.973  -0.258  1.00 40.08           N
ANISOU 1158  N   ASP A 154     5690   4976   4561   -118   -598    151       N
ATOM   1159  CA  ASP A 154     -13.099   1.172   0.223  1.00 40.33           C
ANISOU 1159  CA  ASP A 154     5710   5013   4600   -149   -646    161       C
ATOM   1160  C   ASP A 154     -14.350   1.644  -0.504  1.00 42.73           C
ANISOU 1160  C   ASP A 154     6029   5301   4905   -189   -719    169       C
ATOM   1161  O   ASP A 154     -14.315   2.590  -1.298  1.00 41.83           O
ANISOU 1161  O   ASP A 154     5936   5172   4784   -187   -730    167       O
ATOM   1162  CB  ASP A 154     -13.245   1.255   1.753  1.00 39.29           C
ANISOU 1162  CB  ASP A 154     5473   4939   4516   -137   -637    159       C
ATOM   1163  CG  ASP A 154     -13.847  -0.028   2.376  1.00 38.78           C
ANISOU 1163  CG  ASP A 154     5415   4871   4447   -156   -651    167       C
ATOM   1164  OD1 ASP A 154     -14.488  -0.796   1.630  1.00 35.41           O
ANISOU 1164  OD1 ASP A 154     5061   4404   3991   -190   -685    174       O
ATOM   1165  OD2 ASP A 154     -13.688  -0.271   3.609  1.00 37.98           O
ANISOU 1165  OD2 ASP A 154     5254   4807   4371   -139   -628    166       O
ATOM   1166  N   HIS A 155     -15.441   0.918  -0.291  1.00 45.55           N
ANISOU 1166  N   HIS A 155     6383   5656   5269   -225   -768    177       N
ATOM   1167  CA  HIS A 155     -16.715   1.294  -0.891  1.00 46.68           C
ANISOU 1167  CA  HIS A 155     6528   5789   5420   -264   -845    185       C
ATOM   1168  C   HIS A 155     -17.126   2.669  -0.380  1.00 45.31           C
ANISOU 1168  C   HIS A 155     6257   5659   5298   -252   -861    185       C
ATOM   1169  O   HIS A 155     -16.890   2.981   0.796  1.00 43.46           O
ANISOU 1169  O   HIS A 155     5938   5470   5103   -231   -826    181       O
ATOM   1170  CB  HIS A 155     -17.802   0.277  -0.552  1.00 47.32           C
ANISOU 1170  CB  HIS A 155     6602   5868   5509   -307   -890    193       C
ATOM   1171  CG  HIS A 155     -19.073   0.470  -1.316  1.00 51.10           C
ANISOU 1171  CG  HIS A 155     7093   6332   5993   -351   -974    201       C
ATOM   1172  ND1 HIS A 155     -19.339  -0.187  -2.502  1.00 56.34           N
ANISOU 1172  ND1 HIS A 155     7862   6941   6604   -384  -1015    204       N
ATOM   1173  CD2 HIS A 155     -20.152   1.248  -1.068  1.00 51.68           C
ANISOU 1173  CD2 HIS A 155     7084   6435   6115   -366  -1028    207       C
ATOM   1174  CE1 HIS A 155     -20.533   0.165  -2.943  1.00 58.39           C
ANISOU 1174  CE1 HIS A 155     8102   7201   6882   -419  -1096    211       C
ATOM   1175  NE2 HIS A 155     -21.046   1.037  -2.093  1.00 58.41           N
ANISOU 1175  NE2 HIS A 155     7989   7256   6948   -407  -1104    214       N
ATOM   1176  N   PRO A 156     -17.693   3.522  -1.242  1.00 49.01           N
ANISOU 1176  N   PRO A 156     6743   6114   5766   -263   -910    190       N
ATOM   1177  CA  PRO A 156     -18.076   4.878  -0.803  1.00 45.39           C
ANISOU 1177  CA  PRO A 156     6199   5692   5354   -247   -921    191       C
ATOM   1178  C   PRO A 156     -19.053   4.896   0.359  1.00 45.24           C
ANISOU 1178  C   PRO A 156     6075   5720   5395   -259   -943    196       C
ATOM   1179  O   PRO A 156     -18.933   5.740   1.252  1.00 42.62           O
ANISOU 1179  O   PRO A 156     5663   5427   5103   -236   -915    192       O
ATOM   1180  CB  PRO A 156     -18.717   5.474  -2.058  1.00 44.57           C
ANISOU 1180  CB  PRO A 156     6149   5555   5230   -262   -984    199       C
ATOM   1181  CG  PRO A 156     -18.240   4.634  -3.193  1.00 46.48           C
ANISOU 1181  CG  PRO A 156     6515   5740   5405   -275   -984    198       C
ATOM   1182  CD  PRO A 156     -18.043   3.270  -2.652  1.00 47.71           C
ANISOU 1182  CD  PRO A 156     6681   5895   5553   -288   -959    195       C
ATOM   1183  N   SER A 157     -19.976   3.940   0.413  1.00 46.49           N
ANISOU 1183  N   SER A 157     6234   5871   5558   -297   -986    203       N
ATOM   1184  CA  SER A 157     -20.985   3.886   1.460  1.00 46.73           C
ANISOU 1184  CA  SER A 157     6169   5941   5646   -314  -1004    209       C
ATOM   1185  C   SER A 157     -20.539   3.066   2.681  1.00 48.40           C
ANISOU 1185  C   SER A 157     6350   6173   5865   -307   -947    203       C
ATOM   1186  O   SER A 157     -21.382   2.645   3.478  1.00 49.51           O
ANISOU 1186  O   SER A 157     6434   6335   6043   -329   -959    208       O
ATOM   1187  CB  SER A 157     -22.291   3.320   0.887  1.00 46.53           C
ANISOU 1187  CB  SER A 157     6153   5898   5627   -363  -1082    219       C
ATOM   1188  OG  SER A 157     -22.778   4.112  -0.191  1.00 45.59           O
ANISOU 1188  OG  SER A 157     6058   5762   5501   -366  -1143    226       O
ATOM   1189  N   SER A 158     -19.243   2.807   2.823  1.00 50.88           N
ANISOU 1189  N   SER A 158     6703   6482   6147   -276   -887    194       N
ATOM   1190  CA  SER A 158     -18.745   2.037   3.954  1.00 47.97           C
ANISOU 1190  CA  SER A 158     6313   6132   5782   -263   -837    190       C
ATOM   1191  C   SER A 158     -18.811   2.862   5.231  1.00 49.31           C
ANISOU 1191  C   SER A 158     6382   6351   6001   -241   -811    186       C
ATOM   1192  O   SER A 158     -18.441   4.040   5.253  1.00 48.22           O
ANISOU 1192  O   SER A 158     6212   6232   5879   -216   -798    181       O
ATOM   1193  CB  SER A 158     -17.294   1.597   3.709  1.00 46.78           C
ANISOU 1193  CB  SER A 158     6226   5962   5585   -231   -782    181       C
ATOM   1194  OG  SER A 158     -16.744   0.858   4.801  1.00 41.41           O
ANISOU 1194  OG  SER A 158     5528   5300   4905   -211   -736    178       O
ATOM   1195  N   LYS A 159     -19.244   2.224   6.315  1.00 46.24           N
ANISOU 1195  N   LYS A 159     5953   5981   5634   -251   -798    189       N
ATOM   1196  CA  LYS A 159     -19.179   2.886   7.606  1.00 46.15           C
ANISOU 1196  CA  LYS A 159     5861   6012   5661   -228   -765    184       C
ATOM   1197  C   LYS A 159     -17.733   3.119   8.042  1.00 47.37           C
ANISOU 1197  C   LYS A 159     6022   6181   5795   -184   -711    173       C
ATOM   1198  O   LYS A 159     -17.466   4.086   8.760  1.00 48.42           O
ANISOU 1198  O   LYS A 159     6098   6347   5954   -161   -689    166       O
ATOM   1199  CB  LYS A 159     -19.941   2.069   8.652  1.00 49.22           C
ANISOU 1199  CB  LYS A 159     6217   6413   6073   -250   -758    190       C
ATOM   1200  N   ILE A 160     -16.784   2.292   7.593  1.00 51.73           N
ANISOU 1200  N   ILE A 160     6643   6709   6302   -171   -689    170       N
ATOM   1201  CA  ILE A 160     -15.380   2.406   8.051  1.00 47.30           C
ANISOU 1201  CA  ILE A 160     6081   6164   5725   -127   -638    159       C
ATOM   1202  C   ILE A 160     -14.779   3.726   7.554  1.00 49.61           C
ANISOU 1202  C   ILE A 160     6356   6466   6026   -109   -629    149       C
ATOM   1203  O   ILE A 160     -14.810   3.993   6.339  1.00 50.09           O
ANISOU 1203  O   ILE A 160     6464   6497   6069   -119   -648    151       O
ATOM   1204  CB  ILE A 160     -14.553   1.207   7.545  1.00 45.86           C
ANISOU 1204  CB  ILE A 160     5979   5949   5496   -115   -616    159       C
ATOM   1205  CG1 ILE A 160     -15.189  -0.161   7.860  1.00 44.24           C
ANISOU 1205  CG1 ILE A 160     5808   5724   5276   -139   -624    169       C
ATOM   1206  CG2 ILE A 160     -13.135   1.248   8.143  1.00 48.41           C
ANISOU 1206  CG2 ILE A 160     6288   6295   5810    -68   -565    149       C
ATOM   1207  CD1 ILE A 160     -15.208  -0.539   9.342  1.00 40.34           C
ANISOU 1207  CD1 ILE A 160     5269   5261   4798   -125   -600    169       C
ATOM   1208  N   PRO A 161     -14.178   4.556   8.428  1.00 48.47           N
ANISOU 1208  N   PRO A 161     6154   6360   5903    -83   -600    139       N
ATOM   1209  CA  PRO A 161     -13.731   5.901   8.004  1.00 51.87           C
ANISOU 1209  CA  PRO A 161     6566   6798   6345    -72   -592    129       C
ATOM   1210  C   PRO A 161     -12.653   5.822   6.935  1.00 53.43           C
ANISOU 1210  C   PRO A 161     6824   6969   6509    -58   -569    123       C
ATOM   1211  O   PRO A 161     -11.840   4.896   6.922  1.00 51.23           O
ANISOU 1211  O   PRO A 161     6579   6681   6204    -41   -543    121       O
ATOM   1212  CB  PRO A 161     -13.167   6.512   9.305  1.00 48.90           C
ANISOU 1212  CB  PRO A 161     6122   6466   5991    -49   -560    117       C
ATOM   1213  CG  PRO A 161     -13.721   5.715  10.410  1.00 47.74           C
ANISOU 1213  CG  PRO A 161     5951   6334   5853    -53   -563    124       C
ATOM   1214  CD  PRO A 161     -13.898   4.306   9.855  1.00 47.14           C
ANISOU 1214  CD  PRO A 161     5938   6225   5747    -64   -574    134       C
ATOM   1215  N   GLN A 162     -12.637   6.795   6.017  1.00 56.22           N
ANISOU 1215  N   GLN A 162     7194   7306   6861    -63   -576    120       N
ATOM   1216  CA  GLN A 162     -11.582   6.662   5.022  1.00 63.87           C
ANISOU 1216  CA  GLN A 162     8225   8246   7797    -50   -545    114       C
ATOM   1217  C   GLN A 162     -11.418   8.074   4.391  1.00 63.19           C
ANISOU 1217  C   GLN A 162     8138   8154   7718    -51   -540    106       C
ATOM   1218  O   GLN A 162     -12.339   8.912   4.433  1.00 64.63           O
ANISOU 1218  O   GLN A 162     8293   8342   7923    -64   -573    111       O
ATOM   1219  CB  GLN A 162     -12.049   5.570   4.039  1.00 58.32           C
ANISOU 1219  CB  GLN A 162     7606   7496   7058    -69   -572    126       C
ATOM   1220  CG  GLN A 162     -12.983   6.221   2.830  1.00 62.62           C
ANISOU 1220  CG  GLN A 162     8194   8006   7592    -96   -621    135       C
ATOM   1221  CD  GLN A 162     -13.698   5.020   2.084  1.00 58.03           C
ANISOU 1221  CD  GLN A 162     7687   7384   6978   -124   -661    148       C
ATOM   1222  OE1 GLN A 162     -13.743   3.995   2.771  1.00 56.82           O
ANISOU 1222  OE1 GLN A 162     7525   7240   6825   -125   -654    150       O
ATOM   1223  NE2 GLN A 162     -13.887   5.152   0.767  1.00 56.76           N
ANISOU 1223  NE2 GLN A 162     7604   7178   6784   -138   -685    152       N
ATOM   1224  N   HIS A 163     -10.240   8.365   3.867  1.00 58.90           N
ANISOU 1224  N   HIS A 163     7621   7599   7160    -35   -494     94       N
ATOM   1225  CA  HIS A 163     -10.046   9.686   3.263  1.00 56.04           C
ANISOU 1225  CA  HIS A 163     7265   7226   6802    -37   -483     86       C
ATOM   1226  C   HIS A 163     -10.587   9.726   1.824  1.00 47.23           C
ANISOU 1226  C   HIS A 163     6235   6056   5652    -53   -511     97       C
ATOM   1227  O   HIS A 163     -11.090   8.730   1.288  1.00 45.85           O
ANISOU 1227  O   HIS A 163     6116   5854   5452    -65   -542    109       O
ATOM   1228  CB  HIS A 163      -8.564  10.069   3.252  1.00 56.88           C
ANISOU 1228  CB  HIS A 163     7363   7341   6909    -18   -419     68       C
ATOM   1229  CG  HIS A 163      -8.031  10.582   4.560  1.00 63.16           C
ANISOU 1229  CG  HIS A 163     8069   8189   7739     -5   -396     53       C
ATOM   1230  ND1 HIS A 163      -6.707  10.943   4.724  1.00 65.63           N
ANISOU 1230  ND1 HIS A 163     8357   8518   8061      9   -344     34       N
ATOM   1231  CD2 HIS A 163      -8.624  10.786   5.761  1.00 63.39           C
ANISOU 1231  CD2 HIS A 163     8031   8257   7796     -7   -419     54       C
ATOM   1232  CE1 HIS A 163      -6.504  11.327   5.972  1.00 65.37           C
ANISOU 1232  CE1 HIS A 163     8247   8533   8057     15   -340     24       C
ATOM   1233  NE2 HIS A 163      -7.652  11.247   6.622  1.00 67.75           N
ANISOU 1233  NE2 HIS A 163     8525   8847   8368      6   -383     36       N
ATOM   1234  N   LYS A 164     -10.500  10.902   1.183  1.00 43.06           N
ANISOU 1234  N   LYS A 164     5726   5511   5122    -55   -504     92       N
ATOM   1235  CA  LYS A 164     -11.059  11.057  -0.168  1.00 42.81           C
ANISOU 1235  CA  LYS A 164     5783   5428   5057    -68   -536    103       C
ATOM   1236  C   LYS A 164     -10.208  10.280  -1.167  1.00 43.11           C
ANISOU 1236  C   LYS A 164     5910   5421   5049    -65   -501    101       C
ATOM   1237  O   LYS A 164      -9.125  10.734  -1.555  1.00 47.65           O
ANISOU 1237  O   LYS A 164     6507   5983   5616    -53   -442     88       O
ATOM   1238  CB  LYS A 164     -11.149  12.529  -0.574  1.00 43.62           C
ANISOU 1238  CB  LYS A 164     5889   5520   5165    -67   -533     99       C
ATOM   1239  N   ASN A 165     -10.715   9.143  -1.640  1.00 39.17           N
ANISOU 1239  N   ASN A 165     5468   4895   4521    -77   -536    113       N
ATOM   1240  CA  ASN A 165     -10.069   8.383  -2.708  1.00 38.77           C
ANISOU 1240  CA  ASN A 165     5519   4792   4421    -76   -507    114       C
ATOM   1241  C   ASN A 165     -10.966   8.387  -3.943  1.00 38.85           C
ANISOU 1241  C   ASN A 165     5622   4748   4389    -98   -564    127       C
ATOM   1242  O   ASN A 165     -12.056   8.984  -3.943  1.00 39.06           O
ANISOU 1242  O   ASN A 165     5627   4783   4430   -112   -626    136       O
ATOM   1243  CB  ASN A 165      -9.740   6.956  -2.253  1.00 36.42           C
ANISOU 1243  CB  ASN A 165     5223   4500   4116    -69   -491    116       C
ATOM   1244  CG  ASN A 165     -10.898   6.299  -1.506  1.00 40.75           C
ANISOU 1244  CG  ASN A 165     5728   5073   4681    -87   -553    127       C
ATOM   1245  OD1 ASN A 165     -12.051   6.365  -1.945  1.00 39.58           O
ANISOU 1245  OD1 ASN A 165     5603   4909   4527   -113   -618    139       O
ATOM   1246  ND2 ASN A 165     -10.600   5.683  -0.357  1.00 42.31           N
ANISOU 1246  ND2 ASN A 165     5862   5310   4903    -74   -533    124       N
ATOM   1247  N   LEU A 166     -10.506   7.683  -4.986  1.00 36.83           N
ANISOU 1247  N   LEU A 166     5474   4438   4082   -101   -543    128       N
ATOM   1248  CA  LEU A 166     -11.073   7.806  -6.333  1.00 36.41           C
ANISOU 1248  CA  LEU A 166     5531   4325   3979   -119   -585    137       C
ATOM   1249  C   LEU A 166     -12.592   7.694  -6.408  1.00 39.28           C
ANISOU 1249  C   LEU A 166     5889   4690   4344   -147   -685    153       C
ATOM   1250  O   LEU A 166     -13.215   8.544  -7.073  1.00 36.46           O
ANISOU 1250  O   LEU A 166     5563   4313   3976   -154   -730    159       O
ATOM   1251  CB  LEU A 166     -10.493   6.726  -7.257  1.00 37.09           C
ANISOU 1251  CB  LEU A 166     5733   4353   4007   -121   -553    138       C
ATOM   1252  CG  LEU A 166     -11.110   6.928  -8.650  1.00 42.84           C
ANISOU 1252  CG  LEU A 166     6582   5017   4678   -142   -602    147       C
ATOM   1253  CD1 LEU A 166     -10.674   8.180  -9.461  1.00 37.65           C
ANISOU 1253  CD1 LEU A 166     5975   4327   4002   -131   -572    142       C
ATOM   1254  CD2 LEU A 166     -11.436   5.671  -9.446  1.00 34.20           C
ANISOU 1254  CD2 LEU A 166     5598   3870   3527   -164   -632    155       C
ATOM   1255  N   PRO A 167     -13.236   6.638  -5.870  1.00 41.07           N
ANISOU 1255  N   PRO A 167     6089   4935   4581   -164   -724    159       N
ATOM   1256  CA  PRO A 167     -14.708   6.568  -5.952  1.00 43.02           C
ANISOU 1256  CA  PRO A 167     6322   5186   4838   -194   -819    173       C
ATOM   1257  C   PRO A 167     -15.413   7.712  -5.237  1.00 36.55           C
ANISOU 1257  C   PRO A 167     5399   4415   4075   -188   -850    176       C
ATOM   1258  O   PRO A 167     -16.383   8.260  -5.764  1.00 34.88           O
ANISOU 1258  O   PRO A 167     5199   4193   3863   -200   -919    187       O
ATOM   1259  CB  PRO A 167     -15.011   5.205  -5.313  1.00 38.81           C
ANISOU 1259  CB  PRO A 167     5769   4667   4311   -212   -830    176       C
ATOM   1260  CG  PRO A 167     -13.789   4.421  -5.621  1.00 35.96           C
ANISOU 1260  CG  PRO A 167     5479   4274   3910   -196   -757    168       C
ATOM   1261  CD  PRO A 167     -12.708   5.400  -5.272  1.00 37.42           C
ANISOU 1261  CD  PRO A 167     5618   4483   4118   -160   -686    156       C
ATOM   1262  N   ILE A 168     -14.934   8.122  -4.062  1.00 40.93           N
ANISOU 1262  N   ILE A 168     5855   5020   4676   -166   -802    167       N
ATOM   1263  CA  ILE A 168     -15.588   9.242  -3.390  1.00 41.78           C
ANISOU 1263  CA  ILE A 168     5871   5168   4834   -159   -826    170       C
ATOM   1264  C   ILE A 168     -15.459  10.504  -4.240  1.00 39.86           C
ANISOU 1264  C   ILE A 168     5673   4898   4574   -147   -826    170       C
ATOM   1265  O   ILE A 168     -16.413  11.271  -4.387  1.00 39.40           O
ANISOU 1265  O   ILE A 168     5593   4844   4533   -148   -881    180       O
ATOM   1266  CB  ILE A 168     -15.017   9.435  -1.974  1.00 39.65           C
ANISOU 1266  CB  ILE A 168     5500   4954   4611   -140   -771    159       C
ATOM   1267  CG1 ILE A 168     -15.370   8.232  -1.071  1.00 40.98           C
ANISOU 1267  CG1 ILE A 168     5624   5149   4798   -153   -780    162       C
ATOM   1268  CG2 ILE A 168     -15.490  10.779  -1.366  1.00 33.98           C
ANISOU 1268  CG2 ILE A 168     4702   4270   3939   -128   -780    159       C
ATOM   1269  CD1 ILE A 168     -14.480   8.077   0.175  1.00 39.46           C
ANISOU 1269  CD1 ILE A 168     5363   4999   4631   -131   -717    150       C
ATOM   1270  N   MET A 169     -14.308  10.687  -4.884  1.00 38.02           N
ANISOU 1270  N   MET A 169     5509   4631   4304   -134   -764    159       N
ATOM   1271  CA  MET A 169     -14.108  11.860  -5.730  1.00 38.82           C
ANISOU 1271  CA  MET A 169     5665   4700   4384   -123   -755    158       C
ATOM   1272  C   MET A 169     -15.022  11.853  -6.952  1.00 40.21           C
ANISOU 1272  C   MET A 169     5934   4827   4518   -138   -831    174       C
ATOM   1273  O   MET A 169     -15.449  12.923  -7.417  1.00 39.22           O
ANISOU 1273  O   MET A 169     5826   4688   4389   -129   -859    180       O
ATOM   1274  CB  MET A 169     -12.648  11.956  -6.172  1.00 40.92           C
ANISOU 1274  CB  MET A 169     5988   4938   4621   -110   -665    142       C
ATOM   1275  CG  MET A 169     -11.604  12.114  -5.037  1.00 38.23           C
ANISOU 1275  CG  MET A 169     5557   4645   4322    -93   -589    125       C
ATOM   1276  SD  MET A 169      -9.936  12.226  -5.764  1.00 48.74           S
ANISOU 1276  SD  MET A 169     6961   5938   5621    -81   -486    107       S
ATOM   1277  CE  MET A 169      -8.927  12.555  -4.295  1.00 41.73           C
ANISOU 1277  CE  MET A 169     5944   5118   4793    -64   -419     87       C
ATOM   1278  N   LEU A 170     -15.314  10.679  -7.509  1.00 41.81           N
ANISOU 1278  N   LEU A 170     6201   5000   4684   -160   -867    180       N
ATOM   1279  CA  LEU A 170     -16.237  10.654  -8.635  1.00 43.05           C
ANISOU 1279  CA  LEU A 170     6443   5113   4801   -177   -950    194       C
ATOM   1280  C   LEU A 170     -17.633  11.098  -8.204  1.00 46.30           C
ANISOU 1280  C   LEU A 170     6772   5561   5258   -184  -1037    209       C
ATOM   1281  O   LEU A 170     -18.256  11.944  -8.860  1.00 43.32           O
ANISOU 1281  O   LEU A 170     6425   5164   4870   -177  -1090    219       O
ATOM   1282  CB  LEU A 170     -16.283   9.252  -9.230  1.00 42.69           C
ANISOU 1282  CB  LEU A 170     6481   5031   4708   -204   -971    197       C
ATOM   1283  CG  LEU A 170     -15.081   8.984 -10.122  1.00 44.89           C
ANISOU 1283  CG  LEU A 170     6879   5252   4926   -196   -899    188       C
ATOM   1284  CD1 LEU A 170     -15.153   7.609 -10.808  1.00 36.83           C
ANISOU 1284  CD1 LEU A 170     5958   4186   3851   -222   -920    191       C
ATOM   1285  CD2 LEU A 170     -14.977  10.137 -11.116  1.00 44.39           C
ANISOU 1285  CD2 LEU A 170     6893   5145   4827   -183   -901    190       C
ATOM   1286  N   LEU A 171     -18.099  10.614  -7.051  1.00 41.06           N
ANISOU 1286  N   LEU A 171     6000   4951   4649   -192  -1047    209       N
ATOM   1287  CA  LEU A 171     -19.413  11.026  -6.597  1.00 40.96           C
ANISOU 1287  CA  LEU A 171     5902   4974   4687   -197  -1120    222       C
ATOM   1288  C   LEU A 171     -19.448  12.531  -6.343  1.00 44.61           C
ANISOU 1288  C   LEU A 171     6318   5454   5180   -165  -1106    223       C
ATOM   1289  O   LEU A 171     -20.347  13.219  -6.834  1.00 48.92           O
ANISOU 1289  O   LEU A 171     6867   5990   5729   -159  -1173    237       O
ATOM   1290  CB  LEU A 171     -19.796  10.236  -5.352  1.00 36.45           C
ANISOU 1290  CB  LEU A 171     5228   4454   4168   -212  -1117    221       C
ATOM   1291  CG  LEU A 171     -19.844   8.719  -5.565  1.00 41.46           C
ANISOU 1291  CG  LEU A 171     5910   5069   4773   -245  -1133    220       C
ATOM   1292  CD1 LEU A 171     -19.857   8.002  -4.212  1.00 44.03           C
ANISOU 1292  CD1 LEU A 171     6143   5443   5145   -252  -1100    216       C
ATOM   1293  CD2 LEU A 171     -21.005   8.258  -6.437  1.00 39.83           C
ANISOU 1293  CD2 LEU A 171     5750   4836   4547   -280  -1233    234       C
ATOM   1294  N   GLU A 172     -18.425  13.084  -5.686  1.00 40.41           N
ANISOU 1294  N   GLU A 172     5752   4941   4663   -143  -1020    209       N
ATOM   1295  CA  GLU A 172     -18.433  14.531  -5.483  1.00 45.21           C
ANISOU 1295  CA  GLU A 172     6326   5559   5294   -116  -1002    209       C
ATOM   1296  C   GLU A 172     -18.470  15.257  -6.822  1.00 49.92           C
ANISOU 1296  C   GLU A 172     7029   6098   5839   -106  -1028    216       C
ATOM   1297  O   GLU A 172     -19.242  16.209  -6.992  1.00 53.55           O
ANISOU 1297  O   GLU A 172     7474   6558   6313    -90  -1074    228       O
ATOM   1298  CB  GLU A 172     -17.220  14.986  -4.672  1.00 40.21           C
ANISOU 1298  CB  GLU A 172     5651   4948   4677    -99   -905    189       C
ATOM   1299  N   ALA A 173     -17.695  14.780  -7.807  1.00 49.10           N
ANISOU 1299  N   ALA A 173     7040   5944   5673   -115  -1003    210       N
ATOM   1300  CA  ALA A 173     -17.737  15.389  -9.134  1.00 48.53           C
ANISOU 1300  CA  ALA A 173     7084   5810   5543   -107  -1028    217       C
ATOM   1301  C   ALA A 173     -19.150  15.343  -9.703  1.00 53.85           C
ANISOU 1301  C   ALA A 173     7772   6475   6213   -115  -1144    239       C
ATOM   1302  O   ALA A 173     -19.595  16.291 -10.367  1.00 53.59           O
ANISOU 1302  O   ALA A 173     7784   6416   6163    -96  -1184    250       O
ATOM   1303  CB  ALA A 173     -16.753  14.698 -10.078  1.00 44.74           C
ANISOU 1303  CB  ALA A 173     6728   5275   4997   -119   -982    208       C
ATOM   1304  N   LYS A 174     -19.872  14.244  -9.451  1.00 52.07           N
ANISOU 1304  N   LYS A 174     7509   6270   6004   -142  -1202    245       N
ATOM   1305  CA  LYS A 174     -21.250  14.167  -9.915  1.00 50.33           C
ANISOU 1305  CA  LYS A 174     7287   6048   5790   -153  -1317    264       C
ATOM   1306  C   LYS A 174     -22.173  15.034  -9.068  1.00 55.82           C
ANISOU 1306  C   LYS A 174     7857   6794   6557   -132  -1349    275       C
ATOM   1307  O   LYS A 174     -23.084  15.670  -9.612  1.00 62.71           O
ANISOU 1307  O   LYS A 174     8739   7656   7431   -119  -1427    292       O
ATOM   1308  CB  LYS A 174     -21.736  12.721  -9.924  1.00 50.23           C
ANISOU 1308  CB  LYS A 174     7274   6039   5772   -195  -1365    266       C
ATOM   1309  CG  LYS A 174     -23.239  12.570  -9.703  1.00 51.35           C
ANISOU 1309  CG  LYS A 174     7335   6213   5961   -211  -1470    282       C
ATOM   1310  CD  LYS A 174     -23.777  11.267 -10.309  1.00 54.21           C
ANISOU 1310  CD  LYS A 174     7753   6553   6292   -258  -1540    285       C
ATOM   1311  CE  LYS A 174     -25.268  11.115 -10.019  1.00 52.04           C
ANISOU 1311  CE  LYS A 174     7383   6314   6074   -277  -1641    300       C
ATOM   1312  NZ  LYS A 174     -25.926  10.095 -10.872  1.00 46.24           N
ANISOU 1312  NZ  LYS A 174     6718   5550   5302   -324  -1731    304       N
ATOM   1313  N   GLU A 175     -21.945  15.117  -7.745  1.00 53.34           N
ANISOU 1313  N   GLU A 175     7430   6534   6303   -126  -1290    266       N
ATOM   1314  CA  GLU A 175     -22.836  15.953  -6.939  1.00 57.88           C
ANISOU 1314  CA  GLU A 175     7892   7153   6946   -104  -1315    276       C
ATOM   1315  C   GLU A 175     -22.651  17.437  -7.253  1.00 60.18           C
ANISOU 1315  C   GLU A 175     8212   7426   7230    -64  -1296    280       C
ATOM   1316  O   GLU A 175     -23.637  18.156  -7.469  1.00 58.84           O
ANISOU 1316  O   GLU A 175     8017   7257   7081    -44  -1361    297       O
ATOM   1317  CB  GLU A 175     -22.640  15.748  -5.430  1.00 54.04           C
ANISOU 1317  CB  GLU A 175     7287   6724   6521   -105  -1254    266       C
ATOM   1318  CG  GLU A 175     -23.155  17.035  -4.713  1.00 63.73           C
ANISOU 1318  CG  GLU A 175     8428   7982   7803    -71  -1247    273       C
ATOM   1319  CD  GLU A 175     -23.103  17.072  -3.189  1.00 70.22           C
ANISOU 1319  CD  GLU A 175     9133   8859   8687    -67  -1191    264       C
ATOM   1320  OE1 GLU A 175     -22.685  16.088  -2.537  1.00 67.66           O
ANISOU 1320  OE1 GLU A 175     8783   8555   8370    -90  -1156    253       O
ATOM   1321  OE2 GLU A 175     -23.473  18.141  -2.645  1.00 70.08           O
ANISOU 1321  OE2 GLU A 175     9058   8861   8710    -38  -1179    269       O
ATOM   1322  N   LYS A 176     -21.406  17.899  -7.378  1.00 58.08           N
ANISOU 1322  N   LYS A 176     8003   7136   6929    -53  -1209    264       N
ATOM   1323  CA  LYS A 176     -21.159  19.326  -7.542  1.00 61.80           C
ANISOU 1323  CA  LYS A 176     8497   7590   7396    -19  -1178    264       C
ATOM   1324  C   LYS A 176     -21.041  19.755  -9.001  1.00 63.45           C
ANISOU 1324  C   LYS A 176     8844   7731   7534    -10  -1206    272       C
ATOM   1325  O   LYS A 176     -20.957  20.959  -9.276  1.00 64.78           O
ANISOU 1325  O   LYS A 176     9045   7877   7691     20  -1189    275       O
ATOM   1326  CB  LYS A 176     -19.891  19.724  -6.775  1.00 56.40           C
ANISOU 1326  CB  LYS A 176     7788   6920   6721    -14  -1065    241       C
ATOM   1327  N   ASN A 177     -21.116  18.810  -9.937  1.00 60.84           N
ANISOU 1327  N   ASN A 177     8599   7364   7152    -34  -1253    276       N
ATOM   1328  CA  ASN A 177     -20.986  19.099 -11.363  1.00 57.54           C
ANISOU 1328  CA  ASN A 177     8328   6877   6658    -28  -1281    283       C
ATOM   1329  C   ASN A 177     -19.649  19.773 -11.691  1.00 58.55           C
ANISOU 1329  C   ASN A 177     8536   6965   6744    -16  -1176    266       C
ATOM   1330  O   ASN A 177     -19.591  20.692 -12.514  1.00 54.89           O
ANISOU 1330  O   ASN A 177     8163   6453   6239      5  -1178    272       O
ATOM   1331  CB  ASN A 177     -22.157  19.940 -11.861  1.00 55.90           C
ANISOU 1331  CB  ASN A 177     8127   6659   6454     -1  -1375    307       C
ATOM   1332  CG  ASN A 177     -22.255  19.942 -13.371  1.00 61.21           C
ANISOU 1332  CG  ASN A 177     8953   7260   7043     -1  -1432    317       C
ATOM   1333  OD1 ASN A 177     -22.180  21.004 -14.008  1.00 57.82           O
ANISOU 1333  OD1 ASN A 177     8599   6789   6580     30  -1429    324       O
ATOM   1334  ND2 ASN A 177     -22.395  18.748 -13.963  1.00 55.50           N
ANISOU 1334  ND2 ASN A 177     8287   6517   6283    -36  -1480    317       N
ATOM   1335  N   VAL A 178     -18.583  19.356 -11.010  1.00 55.06           N
ANISOU 1335  N   VAL A 178     8058   6544   6317    -30  -1083    245       N
ATOM   1336  CA  VAL A 178     -17.215  19.792 -11.292  1.00 51.71           C
ANISOU 1336  CA  VAL A 178     7702   6086   5860    -26   -977    226       C
ATOM   1337  C   VAL A 178     -16.408  18.587 -11.780  1.00 53.64           C
ANISOU 1337  C   VAL A 178     8016   6303   6061    -52   -941    215       C
ATOM   1338  O   VAL A 178     -16.312  17.582 -11.059  1.00 52.91           O
ANISOU 1338  O   VAL A 178     7854   6251   5999    -69   -934    209       O
ATOM   1339  CB  VAL A 178     -16.560  20.444 -10.063  1.00 50.72           C
ANISOU 1339  CB  VAL A 178     7471   6009   5791    -17   -893    209       C
ATOM   1340  CG1 VAL A 178     -15.134  20.868 -10.373  1.00 47.77           C
ANISOU 1340  CG1 VAL A 178     7162   5602   5388    -19   -785    188       C
ATOM   1341  CG2 VAL A 178     -17.381  21.649  -9.589  1.00 46.34           C
ANISOU 1341  CG2 VAL A 178     6854   5476   5276     10   -925    220       C
ATOM   1342  N   PRO A 179     -15.803  18.638 -12.975  1.00 53.73           N
ANISOU 1342  N   PRO A 179     8169   6245   6002    -54   -913    213       N
ATOM   1343  CA  PRO A 179     -15.108  17.450 -13.503  1.00 50.65           C
ANISOU 1343  CA  PRO A 179     7854   5823   5569    -76   -880    204       C
ATOM   1344  C   PRO A 179     -13.884  17.032 -12.680  1.00 47.31           C
ANISOU 1344  C   PRO A 179     7366   5432   5177    -80   -774    182       C
ATOM   1345  O   PRO A 179     -13.164  17.855 -12.103  1.00 43.45           O
ANISOU 1345  O   PRO A 179     6825   4964   4721    -69   -700    168       O
ATOM   1346  CB  PRO A 179     -14.702  17.867 -14.930  1.00 52.62           C
ANISOU 1346  CB  PRO A 179     8270   5986   5736    -71   -861    206       C
ATOM   1347  CG  PRO A 179     -15.527  19.023 -15.274  1.00 52.80           C
ANISOU 1347  CG  PRO A 179     8314   5995   5753    -50   -922    222       C
ATOM   1348  CD  PRO A 179     -15.929  19.706 -13.982  1.00 49.04           C
ANISOU 1348  CD  PRO A 179     7683   5592   5359    -35   -925    221       C
ATOM   1349  N   PHE A 180     -13.685  15.720 -12.599  1.00 47.48           N
ANISOU 1349  N   PHE A 180     7390   5459   5191    -98   -773    179       N
ATOM   1350  CA  PHE A 180     -12.474  15.146 -12.024  1.00 47.08           C
ANISOU 1350  CA  PHE A 180     7301   5428   5160   -100   -676    160       C
ATOM   1351  C   PHE A 180     -11.389  15.057 -13.100  1.00 46.32           C
ANISOU 1351  C   PHE A 180     7334   5263   5003    -99   -598    151       C
ATOM   1352  O   PHE A 180     -11.624  14.522 -14.191  1.00 46.76           O
ANISOU 1352  O   PHE A 180     7514   5259   4995   -109   -630    160       O
ATOM   1353  CB  PHE A 180     -12.771  13.775 -11.413  1.00 45.66           C
ANISOU 1353  CB  PHE A 180     7066   5283   5000   -115   -708    163       C
ATOM   1354  CG  PHE A 180     -11.556  13.055 -10.914  1.00 45.14           C
ANISOU 1354  CG  PHE A 180     6972   5232   4946   -111   -617    147       C
ATOM   1355  CD1 PHE A 180     -11.075  13.290  -9.643  1.00 45.34           C
ANISOU 1355  CD1 PHE A 180     6871   5322   5035   -101   -571    135       C
ATOM   1356  CD2 PHE A 180     -10.939  12.090 -11.687  1.00 46.56           C
ANISOU 1356  CD2 PHE A 180     7252   5363   5076   -118   -581    144       C
ATOM   1357  CE1 PHE A 180      -9.967  12.612  -9.161  1.00 46.21           C
ANISOU 1357  CE1 PHE A 180     6949   5449   5158    -94   -494    121       C
ATOM   1358  CE2 PHE A 180      -9.836  11.409 -11.212  1.00 44.72           C
ANISOU 1358  CE2 PHE A 180     6988   5146   4858   -109   -498    131       C
ATOM   1359  CZ  PHE A 180      -9.355  11.671  -9.944  1.00 46.17           C
ANISOU 1359  CZ  PHE A 180     7040   5397   5107    -97   -458    119       C
ATOM   1360  N   VAL A 181     -10.226  15.633 -12.812  1.00 44.74           N
ANISOU 1360  N   VAL A 181     7108   5068   4823    -89   -496    133       N
ATOM   1361  CA  VAL A 181      -9.142  15.741 -13.779  1.00 46.12           C
ANISOU 1361  CA  VAL A 181     7396   5179   4949    -88   -408    122       C
ATOM   1362  C   VAL A 181      -8.273  14.498 -13.659  1.00 51.31           C
ANISOU 1362  C   VAL A 181     8052   5837   5604    -91   -349    113       C
ATOM   1363  O   VAL A 181      -7.777  14.174 -12.572  1.00 52.95           O
ANISOU 1363  O   VAL A 181     8144   6105   5869    -86   -314    103       O
ATOM   1364  CB  VAL A 181      -8.310  17.008 -13.541  1.00 46.73           C
ANISOU 1364  CB  VAL A 181     7442   5261   5052    -79   -324    106       C
ATOM   1365  CG1 VAL A 181      -7.341  17.217 -14.681  1.00 52.36           C
ANISOU 1365  CG1 VAL A 181     8285   5898   5711    -81   -236     97       C
ATOM   1366  CG2 VAL A 181      -9.214  18.224 -13.378  1.00 52.86           C
ANISOU 1366  CG2 VAL A 181     8194   6049   5843    -72   -382    115       C
ATOM   1367  N   THR A 182      -8.087  13.799 -14.772  1.00 45.98           N
ANISOU 1367  N   THR A 182     7513   5094   4863    -97   -338    118       N
ATOM   1368  CA  THR A 182      -7.144  12.691 -14.831  1.00 44.62           C
ANISOU 1368  CA  THR A 182     7362   4909   4683    -95   -266    110       C
ATOM   1369  C   THR A 182      -6.272  12.886 -16.073  1.00 46.53           C
ANISOU 1369  C   THR A 182     7747   5068   4864    -92   -182    103       C
ATOM   1370  O   THR A 182      -6.189  13.991 -16.627  1.00 46.50           O
ANISOU 1370  O   THR A 182     7797   5030   4841    -91   -161    101       O
ATOM   1371  CB  THR A 182      -7.919  11.370 -14.818  1.00 43.49           C
ANISOU 1371  CB  THR A 182     7238   4768   4520   -107   -343    123       C
ATOM   1372  OG1 THR A 182      -6.991  10.287 -14.900  1.00 42.13           O
ANISOU 1372  OG1 THR A 182     7094   4578   4335   -101   -270    116       O
ATOM   1373  CG2 THR A 182      -8.884  11.296 -15.992  1.00 40.53           C
ANISOU 1373  CG2 THR A 182     7000   4329   4072   -123   -426    139       C
ATOM   1374  N   THR A 183      -5.656  11.801 -16.569  1.00 41.96           N
ANISOU 1374  N   THR A 183     7243   4450   4252    -91   -132    102       N
ATOM   1375  CA  THR A 183      -4.787  11.920 -17.741  1.00 42.77           C
ANISOU 1375  CA  THR A 183     7484   4470   4298    -88    -42     96       C
ATOM   1376  C   THR A 183      -4.658  10.589 -18.476  1.00 40.73           C
ANISOU 1376  C   THR A 183     7340   4154   3979    -91    -31    102       C
ATOM   1377  O   THR A 183      -4.842   9.518 -17.896  1.00 40.74           O
ANISOU 1377  O   THR A 183     7290   4190   3999    -90    -60    106       O
ATOM   1378  CB  THR A 183      -3.386  12.421 -17.359  1.00 40.78           C
ANISOU 1378  CB  THR A 183     7165   4236   4095    -74     87     75       C
ATOM   1379  OG1 THR A 183      -2.572  12.501 -18.538  1.00 37.29           O
ANISOU 1379  OG1 THR A 183     6862   3709   3597    -72    181     69       O
ATOM   1380  CG2 THR A 183      -2.734  11.475 -16.370  1.00 34.25           C
ANISOU 1380  CG2 THR A 183     6221   3468   3323    -60    125     67       C
ATOM   1381  N   VAL A 184      -4.290  10.675 -19.764  1.00 36.77           N
ANISOU 1381  N   VAL A 184     7003   3562   3405    -93     18    102       N
ATOM   1382  CA  VAL A 184      -3.895   9.480 -20.510  1.00 41.11           C
ANISOU 1382  CA  VAL A 184     7673   4049   3897    -93     59    105       C
ATOM   1383  C   VAL A 184      -2.415   9.151 -20.342  1.00 39.31           C
ANISOU 1383  C   VAL A 184     7415   3820   3702    -70    202     90       C
ATOM   1384  O   VAL A 184      -1.996   8.035 -20.686  1.00 37.77           O
ANISOU 1384  O   VAL A 184     7287   3587   3477    -63    245     91       O
ATOM   1385  CB  VAL A 184      -4.210   9.632 -22.017  1.00 45.53           C
ANISOU 1385  CB  VAL A 184     8439   4505   4356   -105     46    113       C
ATOM   1386  CG1 VAL A 184      -5.708   9.653 -22.242  1.00 45.01           C
ANISOU 1386  CG1 VAL A 184     8411   4438   4254   -127   -107    130       C
ATOM   1387  CG2 VAL A 184      -3.557  10.903 -22.608  1.00 37.38           C
ANISOU 1387  CG2 VAL A 184     7461   3430   3312    -99    128    104       C
ATOM   1388  N   ASN A 185      -1.645  10.038 -19.719  1.00 38.47           N
ANISOU 1388  N   ASN A 185     7196   3758   3661    -59    272     75       N
ATOM   1389  CA  ASN A 185      -0.215   9.894 -19.499  1.00 37.65           C
ANISOU 1389  CA  ASN A 185     7042   3661   3600    -38    406     59       C
ATOM   1390  C   ASN A 185       0.118   9.193 -18.175  1.00 37.71           C
ANISOU 1390  C   ASN A 185     6884   3758   3685    -21    406     54       C
ATOM   1391  O   ASN A 185       1.266   9.268 -17.704  1.00 35.96           O
ANISOU 1391  O   ASN A 185     6576   3567   3521     -2    503     40       O
ATOM   1392  CB  ASN A 185       0.436  11.289 -19.561  1.00 40.30           C
ANISOU 1392  CB  ASN A 185     7348   3997   3966    -41    480     43       C
ATOM   1393  CG  ASN A 185       0.193  12.006 -20.921  1.00 39.47           C
ANISOU 1393  CG  ASN A 185     7420   3796   3779    -56    491     48       C
ATOM   1394  OD1 ASN A 185       0.277  11.382 -21.974  1.00 39.27           O
ANISOU 1394  OD1 ASN A 185     7550   3689   3681    -56    518     54       O
ATOM   1395  ND2 ASN A 185      -0.087  13.310 -20.886  1.00 38.23           N
ANISOU 1395  ND2 ASN A 185     7246   3647   3633    -67    473     44       N
ATOM   1396  N   GLU A 186      -0.859   8.511 -17.574  1.00 33.97           N
ANISOU 1396  N   GLU A 186     6367   3324   3214    -26    300     67       N
ATOM   1397  CA  GLU A 186      -0.676   7.760 -16.341  1.00 37.07           C
ANISOU 1397  CA  GLU A 186     6620   3794   3669    -10    290     65       C
ATOM   1398  C   GLU A 186      -1.287   6.374 -16.492  1.00 40.97           C
ANISOU 1398  C   GLU A 186     7180   4266   4120    -12    235     80       C
ATOM   1399  O   GLU A 186      -2.458   6.229 -16.876  1.00 40.04           O
ANISOU 1399  O   GLU A 186     7131   4125   3956    -37    135     93       O
ATOM   1400  CB  GLU A 186      -1.288   8.462 -15.126  1.00 35.47           C
ANISOU 1400  CB  GLU A 186     6265   3681   3532    -17    216     63       C
ATOM   1401  CG  GLU A 186      -0.782   7.895 -13.821  1.00 37.06           C
ANISOU 1401  CG  GLU A 186     6318   3962   3803      5    232     57       C
ATOM   1402  CD  GLU A 186      -1.569   8.410 -12.605  1.00 40.38           C
ANISOU 1402  CD  GLU A 186     6601   4464   4277     -5    147     58       C
ATOM   1403  OE1 GLU A 186      -2.699   8.946 -12.783  1.00 39.95           O
ANISOU 1403  OE1 GLU A 186     6572   4405   4202    -27     61     67       O
ATOM   1404  OE2 GLU A 186      -1.057   8.250 -11.467  1.00 37.57           O
ANISOU 1404  OE2 GLU A 186     6115   4176   3982     13    166     50       O
ATOM   1405  N   TYR A 187      -0.499   5.367 -16.161  1.00 35.55           N
ANISOU 1405  N   TYR A 187     6469   3588   3451     14    297     78       N
ATOM   1406  CA  TYR A 187      -0.917   3.978 -16.194  1.00 38.45           C
ANISOU 1406  CA  TYR A 187     6891   3935   3782     15    261     90       C
ATOM   1407  C   TYR A 187      -0.875   3.501 -14.750  1.00 35.81           C
ANISOU 1407  C   TYR A 187     6398   3689   3517     33    237     90       C
ATOM   1408  O   TYR A 187       0.205   3.365 -14.161  1.00 34.15           O
ANISOU 1408  O   TYR A 187     6102   3514   3358     66    317     81       O
ATOM   1409  CB  TYR A 187      -0.010   3.171 -17.123  1.00 37.92           C
ANISOU 1409  CB  TYR A 187     6950   3790   3668     35    362     90       C
ATOM   1410  CG  TYR A 187      -0.516   3.188 -18.545  1.00 38.70           C
ANISOU 1410  CG  TYR A 187     7240   3792   3673      9    345     97       C
ATOM   1411  CD1 TYR A 187      -1.450   2.248 -18.966  1.00 40.82           C
ANISOU 1411  CD1 TYR A 187     7613   4020   3877    -13    265    110       C
ATOM   1412  CD2 TYR A 187      -0.099   4.157 -19.453  1.00 36.41           C
ANISOU 1412  CD2 TYR A 187     7029   3450   3357      5    402     90       C
ATOM   1413  CE1 TYR A 187      -1.953   2.244 -20.250  1.00 42.06           C
ANISOU 1413  CE1 TYR A 187     7947   4088   3945    -39    239    116       C
ATOM   1414  CE2 TYR A 187      -0.601   4.166 -20.773  1.00 40.87           C
ANISOU 1414  CE2 TYR A 187     7780   3921   3828    -19    380     97       C
ATOM   1415  CZ  TYR A 187      -1.537   3.196 -21.160  1.00 42.57           C
ANISOU 1415  CZ  TYR A 187     8096   4099   3979    -40    294    110       C
ATOM   1416  OH  TYR A 187      -2.080   3.136 -22.440  1.00 40.74           O
ANISOU 1416  OH  TYR A 187     8052   3776   3652    -65    260    117       O
ATOM   1417  N   ARG A 188      -2.045   3.326 -14.154  1.00 33.00           N
ANISOU 1417  N   ARG A 188     5999   3372   3167     10    128     99       N
ATOM   1418  CA  ARG A 188      -2.098   3.040 -12.729  1.00 34.34           C
ANISOU 1418  CA  ARG A 188     6018   3628   3403     24    100     98       C
ATOM   1419  C   ARG A 188      -3.217   2.057 -12.457  1.00 29.49           C
ANISOU 1419  C   ARG A 188     5424   3016   2764      3      9    111       C
ATOM   1420  O   ARG A 188      -4.222   2.036 -13.166  1.00 34.25           O
ANISOU 1420  O   ARG A 188     6118   3578   3318    -31    -64    120       O
ATOM   1421  CB  ARG A 188      -2.324   4.354 -11.948  1.00 35.41           C
ANISOU 1421  CB  ARG A 188     6026   3831   3599     16     69     90       C
ATOM   1422  CG  ARG A 188      -2.450   4.265 -10.435  1.00 39.08           C
ANISOU 1422  CG  ARG A 188     6333   4385   4130     27     35     88       C
ATOM   1423  CD  ARG A 188      -3.273   5.453  -9.792  1.00 39.33           C
ANISOU 1423  CD  ARG A 188     6274   4470   4201      6    -35     85       C
ATOM   1424  NE  ARG A 188      -2.569   6.737  -9.607  1.00 36.65           N
ANISOU 1424  NE  ARG A 188     5868   4156   3901     12     16     70       N
ATOM   1425  CZ  ARG A 188      -2.047   7.188  -8.461  1.00 34.54           C
ANISOU 1425  CZ  ARG A 188     5465   3959   3699     27     36     58       C
ATOM   1426  NH1 ARG A 188      -2.082   6.467  -7.340  1.00 30.56           N
ANISOU 1426  NH1 ARG A 188     4873   3510   3229     41     14     61       N
ATOM   1427  NH2 ARG A 188      -1.462   8.379  -8.440  1.00 39.21           N
ANISOU 1427  NH2 ARG A 188     6014   4564   4319     25     81     44       N
ATOM   1428  N   ALA A 189      -3.051   1.259 -11.415  1.00 29.71           N
ANISOU 1428  N   ALA A 189     5368   3092   2829     23     10    113       N
ATOM   1429  CA  ALA A 189      -4.117   0.393 -10.931  1.00 36.12           C
ANISOU 1429  CA  ALA A 189     6177   3919   3631      1    -75    124       C
ATOM   1430  C   ALA A 189      -4.609   0.921  -9.591  1.00 33.97           C
ANISOU 1430  C   ALA A 189     5749   3734   3426     -2   -128    123       C
ATOM   1431  O   ALA A 189      -3.853   1.558  -8.849  1.00 26.01           O
ANISOU 1431  O   ALA A 189     4634   2778   2472     24    -84    112       O
ATOM   1432  CB  ALA A 189      -3.655  -1.067 -10.757  1.00 31.90           C
ANISOU 1432  CB  ALA A 189     5681   3364   3077     24    -34    130       C
ATOM   1433  N   ILE A 190      -5.882   0.652  -9.287  1.00 28.97           N
ANISOU 1433  N   ILE A 190     5106   3114   2788    -36   -222    132       N
ATOM   1434  CA  ILE A 190      -6.438   0.937  -7.969  1.00 27.70           C
ANISOU 1434  CA  ILE A 190     4809   3031   2687    -39   -271    132       C
ATOM   1435  C   ILE A 190      -7.061  -0.340  -7.448  1.00 26.79           C
ANISOU 1435  C   ILE A 190     4700   2918   2561    -51   -310    141       C
ATOM   1436  O   ILE A 190      -7.604  -1.143  -8.211  1.00 30.70           O
ANISOU 1436  O   ILE A 190     5304   3359   3003    -77   -340    149       O
ATOM   1437  CB  ILE A 190      -7.458   2.091  -7.978  1.00 29.04           C
ANISOU 1437  CB  ILE A 190     4937   3222   2874    -69   -345    133       C
ATOM   1438  CG1 ILE A 190      -8.697   1.707  -8.768  1.00 30.02           C
ANISOU 1438  CG1 ILE A 190     5152   3302   2951   -112   -429    145       C
ATOM   1439  CG2 ILE A 190      -6.836   3.367  -8.550  1.00 33.85           C
ANISOU 1439  CG2 ILE A 190     5553   3820   3487    -59   -302    124       C
ATOM   1440  CD1 ILE A 190      -9.718   2.809  -8.751  1.00 33.11           C
ANISOU 1440  CD1 ILE A 190     5498   3717   3365   -135   -504    148       C
ATOM   1441  N   THR A 191      -6.939  -0.557  -6.162  1.00 25.26           N
ANISOU 1441  N   THR A 191     4397   2785   2415    -32   -306    140       N
ATOM   1442  CA  THR A 191      -7.271  -1.847  -5.611  1.00 27.61           C
ANISOU 1442  CA  THR A 191     4706   3083   2703    -35   -322    148       C
ATOM   1443  C   THR A 191      -8.287  -1.635  -4.508  1.00 30.81           C
ANISOU 1443  C   THR A 191     5009   3547   3152    -57   -389    151       C
ATOM   1444  O   THR A 191      -8.095  -0.775  -3.635  1.00 29.63           O
ANISOU 1444  O   THR A 191     4747   3456   3054    -41   -384    145       O
ATOM   1445  CB  THR A 191      -5.994  -2.553  -5.096  1.00 29.58           C
ANISOU 1445  CB  THR A 191     4936   3341   2961     18   -239    146       C
ATOM   1446  OG1 THR A 191      -4.980  -2.538  -6.117  1.00 25.70           O
ANISOU 1446  OG1 THR A 191     4526   2800   2438     42   -167    141       O
ATOM   1447  CG2 THR A 191      -6.281  -3.998  -4.752  1.00 29.39           C
ANISOU 1447  CG2 THR A 191     4957   3299   2911     17   -247    155       C
ATOM   1448  N   PHE A 192      -9.381  -2.390  -4.577  1.00 27.03           N
ANISOU 1448  N   PHE A 192     4570   3049   2652    -97   -450    160       N
ATOM   1449  CA  PHE A 192     -10.311  -2.444  -3.469  1.00 28.04           C
ANISOU 1449  CA  PHE A 192     4607   3227   2820   -116   -502    164       C
ATOM   1450  C   PHE A 192      -9.579  -3.032  -2.272  1.00 28.27           C
ANISOU 1450  C   PHE A 192     4573   3293   2874    -76   -452    163       C
ATOM   1451  O   PHE A 192      -8.844  -4.008  -2.408  1.00 31.71           O
ANISOU 1451  O   PHE A 192     5069   3699   3280    -51   -403    165       O
ATOM   1452  CB  PHE A 192     -11.535  -3.287  -3.851  1.00 35.36           C
ANISOU 1452  CB  PHE A 192     5598   4119   3718   -169   -568    173       C
ATOM   1453  CG  PHE A 192     -12.454  -3.604  -2.695  1.00 36.80           C
ANISOU 1453  CG  PHE A 192     5697   4346   3940   -190   -609    177       C
ATOM   1454  CD1 PHE A 192     -12.903  -2.590  -1.842  1.00 35.49           C
ANISOU 1454  CD1 PHE A 192     5411   4240   3832   -190   -635    175       C
ATOM   1455  CD2 PHE A 192     -12.873  -4.909  -2.466  1.00 37.43           C
ANISOU 1455  CD2 PHE A 192     5823   4403   3997   -212   -618    183       C
ATOM   1456  CE1 PHE A 192     -13.750  -2.877  -0.777  1.00 38.77           C
ANISOU 1456  CE1 PHE A 192     5754   4693   4284   -209   -665    179       C
ATOM   1457  CE2 PHE A 192     -13.731  -5.212  -1.409  1.00 38.50           C
ANISOU 1457  CE2 PHE A 192     5885   4575   4168   -235   -650    186       C
ATOM   1458  CZ  PHE A 192     -14.168  -4.198  -0.560  1.00 40.21           C
ANISOU 1458  CZ  PHE A 192     5981   4852   4444   -233   -672    185       C
ATOM   1459  N   VAL A 193      -9.735  -2.400  -1.107  1.00 32.29           N
ANISOU 1459  N   VAL A 193     4963   3867   3437    -67   -463    160       N
ATOM   1460  CA  VAL A 193      -8.952  -2.771   0.071  1.00 30.53           C
ANISOU 1460  CA  VAL A 193     4675   3684   3239    -24   -419    157       C
ATOM   1461  C   VAL A 193      -9.260  -4.184   0.522  1.00 27.10           C
ANISOU 1461  C   VAL A 193     4281   3233   2783    -28   -422    166       C
ATOM   1462  O   VAL A 193      -8.387  -4.861   1.082  1.00 28.00           O
ANISOU 1462  O   VAL A 193     4392   3354   2893     15   -373    167       O
ATOM   1463  CB  VAL A 193      -9.181  -1.750   1.211  1.00 28.77           C
ANISOU 1463  CB  VAL A 193     4326   3530   3074    -20   -437    151       C
ATOM   1464  CG1 VAL A 193     -10.607  -1.727   1.620  1.00 33.20           C
ANISOU 1464  CG1 VAL A 193     4858   4105   3653    -64   -502    158       C
ATOM   1465  CG2 VAL A 193      -8.431  -2.169   2.419  1.00 26.83           C
ANISOU 1465  CG2 VAL A 193     4022   3325   2849     22   -400    149       C
ATOM   1466  N   GLY A 194     -10.475  -4.674   0.244  1.00 28.65           N
ANISOU 1466  N   GLY A 194     4520   3404   2963    -80   -477    173       N
ATOM   1467  CA  GLY A 194     -10.831  -6.039   0.648  1.00 29.64           C
ANISOU 1467  CA  GLY A 194     4691   3508   3064    -91   -478    181       C
ATOM   1468  C   GLY A 194      -9.924  -7.121   0.071  1.00 27.84           C
ANISOU 1468  C   GLY A 194     4567   3226   2784    -61   -423    184       C
ATOM   1469  O   GLY A 194      -9.509  -8.042   0.780  1.00 28.30           O
ANISOU 1469  O   GLY A 194     4632   3286   2835    -32   -389    189       O
ATOM   1470  N   GLU A 195      -9.580  -7.015  -1.207  1.00 25.12           N
ANISOU 1470  N   GLU A 195     4308   2833   2403    -65   -410    182       N
ATOM   1471  CA  GLU A 195      -8.674  -8.002  -1.785  1.00 27.72           C
ANISOU 1471  CA  GLU A 195     4739   3109   2684    -32   -349    185       C
ATOM   1472  C   GLU A 195      -7.271  -7.898  -1.187  1.00 30.69           C
ANISOU 1472  C   GLU A 195     5061   3517   3084     40   -278    183       C
ATOM   1473  O   GLU A 195      -6.612  -8.929  -0.986  1.00 27.28           O
ANISOU 1473  O   GLU A 195     4672   3063   2628     78   -230    188       O
ATOM   1474  CB  GLU A 195      -8.619  -7.844  -3.301  1.00 28.88           C
ANISOU 1474  CB  GLU A 195     4995   3195   2785    -53   -348    184       C
ATOM   1475  CG  GLU A 195      -9.621  -8.695  -4.051  1.00 35.01           C
ANISOU 1475  CG  GLU A 195     5882   3910   3509   -111   -396    189       C
ATOM   1476  CD  GLU A 195      -9.699  -8.350  -5.525  1.00 37.27           C
ANISOU 1476  CD  GLU A 195     6271   4140   3750   -136   -408    186       C
ATOM   1477  OE1 GLU A 195      -8.639  -8.197  -6.180  1.00 38.68           O
ANISOU 1477  OE1 GLU A 195     6500   4289   3908    -97   -343    184       O
ATOM   1478  OE2 GLU A 195     -10.832  -8.229  -6.027  1.00 37.50           O
ANISOU 1478  OE2 GLU A 195     6331   4152   3766   -196   -484    187       O
ATOM   1479  N   VAL A 196      -6.793  -6.665  -0.906  1.00 25.08           N
ANISOU 1479  N   VAL A 196     4254   2856   2418     60   -269    174       N
ATOM   1480  CA  VAL A 196      -5.498  -6.500  -0.243  1.00 25.71           C
ANISOU 1480  CA  VAL A 196     4266   2975   2529    125   -210    169       C
ATOM   1481  C   VAL A 196      -5.544  -7.161   1.108  1.00 24.77           C
ANISOU 1481  C   VAL A 196     4091   2894   2427    147   -215    175       C
ATOM   1482  O   VAL A 196      -4.632  -7.906   1.500  1.00 24.96           O
ANISOU 1482  O   VAL A 196     4122   2916   2444    201   -166    179       O
ATOM   1483  CB  VAL A 196      -5.122  -5.008  -0.086  1.00 29.75           C
ANISOU 1483  CB  VAL A 196     4679   3536   3088    131   -208    157       C
ATOM   1484  CG1 VAL A 196      -3.873  -4.902   0.721  1.00 24.52           C
ANISOU 1484  CG1 VAL A 196     3938   2919   2460    191   -157    151       C
ATOM   1485  CG2 VAL A 196      -4.972  -4.298  -1.439  1.00 24.76           C
ANISOU 1485  CG2 VAL A 196     4108   2864   2437    113   -195    151       C
ATOM   1486  N   VAL A 197      -6.650  -6.962   1.816  1.00 25.70           N
ANISOU 1486  N   VAL A 197     4161   3040   2564    108   -272    176       N
ATOM   1487  CA  VAL A 197      -6.731  -7.458   3.180  1.00 28.12           C
ANISOU 1487  CA  VAL A 197     4411   3384   2889    128   -277    181       C
ATOM   1488  C   VAL A 197      -6.935  -8.966   3.215  1.00 25.26           C
ANISOU 1488  C   VAL A 197     4140   2975   2482    129   -265    192       C
ATOM   1489  O   VAL A 197      -6.289  -9.665   4.006  1.00 25.68           O
ANISOU 1489  O   VAL A 197     4185   3040   2532    178   -233    198       O
ATOM   1490  CB  VAL A 197      -7.846  -6.704   3.925  1.00 30.46           C
ANISOU 1490  CB  VAL A 197     4626   3724   3223     85   -334    178       C
ATOM   1491  CG1 VAL A 197      -8.276  -7.473   5.200  1.00 23.95           C
ANISOU 1491  CG1 VAL A 197     3777   2919   2403     89   -343    185       C
ATOM   1492  CG2 VAL A 197      -7.382  -5.240   4.207  1.00 23.64           C
ANISOU 1492  CG2 VAL A 197     3661   2915   2406    100   -333    166       C
ATOM   1493  N   GLU A 198      -7.766  -9.505   2.325  1.00 24.97           N
ANISOU 1493  N   GLU A 198     4198   2883   2407     78   -290    197       N
ATOM   1494  CA  GLU A 198      -8.089 -10.941   2.395  1.00 29.35           C
ANISOU 1494  CA  GLU A 198     4842   3390   2918     69   -281    207       C
ATOM   1495  C   GLU A 198      -6.942 -11.856   1.952  1.00 31.04           C
ANISOU 1495  C   GLU A 198     5141   3560   3092    126   -214    212       C
ATOM   1496  O   GLU A 198      -6.845 -12.992   2.424  1.00 29.40           O
ANISOU 1496  O   GLU A 198     4983   3330   2858    146   -192    221       O
ATOM   1497  CB  GLU A 198      -9.296 -11.246   1.514  1.00 29.83           C
ANISOU 1497  CB  GLU A 198     4983   3402   2948     -6   -330    208       C
ATOM   1498  CG  GLU A 198     -10.622 -10.965   2.153  1.00 35.47           C
ANISOU 1498  CG  GLU A 198     5636   4147   3694    -64   -393    207       C
ATOM   1499  CD  GLU A 198     -11.752 -11.139   1.174  1.00 40.96           C
ANISOU 1499  CD  GLU A 198     6399   4799   4365   -138   -447    207       C
ATOM   1500  OE1 GLU A 198     -11.481 -11.372  -0.043  1.00 39.20           O
ANISOU 1500  OE1 GLU A 198     6276   4522   4097   -145   -438    206       O
ATOM   1501  OE2 GLU A 198     -12.909 -11.067   1.636  1.00 46.24           O
ANISOU 1501  OE2 GLU A 198     7024   5487   5059   -189   -497    208       O
ATOM   1502  N   ASN A 199      -6.034 -11.361   1.129  1.00 27.92           N
ANISOU 1502  N   ASN A 199     4759   3154   2695    156   -177    207       N
ATOM   1503  CA  ASN A 199      -4.882 -12.127   0.713  1.00 29.53           C
ANISOU 1503  CA  ASN A 199     5032   3319   2869    215   -106    213       C
ATOM   1504  C   ASN A 199      -3.743 -12.046   1.693  1.00 26.31           C
ANISOU 1504  C   ASN A 199     4536   2963   2497    292    -65    213       C
ATOM   1505  O   ASN A 199      -2.684 -12.623   1.413  1.00 26.48           O
ANISOU 1505  O   ASN A 199     4599   2960   2503    350     -3    218       O
ATOM   1506  CB  ASN A 199      -4.416 -11.674  -0.661  1.00 26.57           C
ANISOU 1506  CB  ASN A 199     4717   2904   2474    212    -77    207       C
ATOM   1507  CG  ASN A 199      -5.238 -12.275  -1.723  1.00 27.57           C
ANISOU 1507  CG  ASN A 199     4974   2957   2543    155    -99    210       C
ATOM   1508  OD1 ASN A 199      -5.899 -13.286  -1.464  1.00 35.79           O
ANISOU 1508  OD1 ASN A 199     6075   3971   3555    131   -118    217       O
ATOM   1509  ND2 ASN A 199      -5.280 -11.661  -2.898  1.00 26.89           N
ANISOU 1509  ND2 ASN A 199     4938   2839   2440    129   -102    204       N
ATOM   1510  N   ILE A 200      -3.928 -11.367   2.832  1.00 25.69           N
ANISOU 1510  N   ILE A 200     4340   2954   2466    294    -98    209       N
ATOM   1511  CA  ILE A 200      -2.754 -11.101   3.650  1.00 29.52           C
ANISOU 1511  CA  ILE A 200     4736   3492   2988    364    -65    207       C
ATOM   1512  C   ILE A 200      -2.171 -12.382   4.217  1.00 27.29           C
ANISOU 1512  C   ILE A 200     4497   3192   2680    424    -28    221       C
ATOM   1513  O   ILE A 200      -0.949 -12.539   4.227  1.00 26.27           O
ANISOU 1513  O   ILE A 200     4350   3070   2561    492     22    222       O
ATOM   1514  CB  ILE A 200      -3.036 -10.069   4.756  1.00 26.28           C
ANISOU 1514  CB  ILE A 200     4198   3157   2629    354   -108    199       C
ATOM   1515  CG1 ILE A 200      -1.722  -9.334   5.079  1.00 25.12           C
ANISOU 1515  CG1 ILE A 200     3958   3061   2525    412    -74    190       C
ATOM   1516  CG2 ILE A 200      -3.581 -10.731   6.011  1.00 26.95           C
ANISOU 1516  CG2 ILE A 200     4267   3261   2711    357   -134    207       C
ATOM   1517  CD1 ILE A 200      -1.203  -8.502   3.949  1.00 25.17           C
ANISOU 1517  CD1 ILE A 200     3967   3055   2542    404    -46    179       C
ATOM   1518  N   GLU A 201      -3.015 -13.350   4.622  1.00 30.70           N
ANISOU 1518  N   GLU A 201     4991   3595   3079    400    -49    231       N
ATOM   1519  CA  GLU A 201      -2.446 -14.562   5.208  1.00 29.91           C
ANISOU 1519  CA  GLU A 201     4936   3475   2952    461    -13    245       C
ATOM   1520  C   GLU A 201      -1.607 -15.333   4.198  1.00 28.78           C
ANISOU 1520  C   GLU A 201     4892   3272   2772    503     51    252       C
ATOM   1521  O   GLU A 201      -0.610 -15.949   4.578  1.00 28.77           O
ANISOU 1521  O   GLU A 201     4892   3272   2769    580     95    261       O
ATOM   1522  CB  GLU A 201      -3.497 -15.514   5.773  1.00 33.03           C
ANISOU 1522  CB  GLU A 201     5393   3843   3314    424    -39    254       C
ATOM   1523  CG  GLU A 201      -4.027 -15.222   7.136  1.00 37.60           C
ANISOU 1523  CG  GLU A 201     5889   4477   3922    415    -80    253       C
ATOM   1524  CD  GLU A 201      -5.410 -14.612   7.135  1.00 45.05           C
ANISOU 1524  CD  GLU A 201     6806   5430   4880    327   -137    245       C
ATOM   1525  OE1 GLU A 201      -5.807 -13.922   6.151  1.00 44.76           O
ANISOU 1525  OE1 GLU A 201     6773   5384   4851    279   -156    237       O
ATOM   1526  OE2 GLU A 201      -6.124 -14.883   8.129  1.00 53.80           O
ANISOU 1526  OE2 GLU A 201     7897   6554   5992    307   -160    249       O
ATOM   1527  N   LYS A 202      -1.954 -15.286   2.918  1.00 27.14           N
ANISOU 1527  N   LYS A 202     4766   3009   2536    457     57    248       N
ATOM   1528  CA  LYS A 202      -1.117 -16.009   1.972  1.00 29.80           C
ANISOU 1528  CA  LYS A 202     5201   3284   2836    500    125    254       C
ATOM   1529  C   LYS A 202       0.278 -15.392   1.851  1.00 34.85           C
ANISOU 1529  C   LYS A 202     5766   3958   3516    570    177    250       C
ATOM   1530  O   LYS A 202       1.213 -16.108   1.483  1.00 37.39           O
ANISOU 1530  O   LYS A 202     6142   4244   3821    632    243    259       O
ATOM   1531  CB  LYS A 202      -1.793 -16.090   0.604  1.00 27.85           C
ANISOU 1531  CB  LYS A 202     5070   2969   2545    434    120    250       C
ATOM   1532  CG  LYS A 202      -3.020 -16.986   0.541  1.00 27.98           C
ANISOU 1532  CG  LYS A 202     5185   2935   2512    370     82    256       C
ATOM   1533  CD  LYS A 202      -3.777 -16.746  -0.757  1.00 31.04           C
ANISOU 1533  CD  LYS A 202     5658   3270   2865    295     56    248       C
ATOM   1534  CE  LYS A 202      -5.191 -17.286  -0.669  1.00 36.06           C
ANISOU 1534  CE  LYS A 202     6349   3880   3472    215     -5    249       C
ATOM   1535  NZ  LYS A 202      -6.137 -16.239  -0.067  1.00 39.07           N
ANISOU 1535  NZ  LYS A 202     6612   4327   3904    161    -80    241       N
ATOM   1536  N   THR A 203       0.455 -14.093   2.164  1.00 30.05           N
ANISOU 1536  N   THR A 203     5034   3418   2965    561    152    236       N
ATOM   1537  CA  THR A 203       1.792 -13.511   2.082  1.00 27.51           C
ANISOU 1537  CA  THR A 203     4635   3130   2686    623    202    231       C
ATOM   1538  C   THR A 203       2.697 -13.980   3.198  1.00 32.97           C
ANISOU 1538  C   THR A 203     5259   3865   3403    705    220    239       C
ATOM   1539  O   THR A 203       3.919 -13.838   3.079  1.00 38.34           O
ANISOU 1539  O   THR A 203     5892   4562   4113    768    272    238       O
ATOM   1540  CB  THR A 203       1.764 -11.971   2.130  1.00 29.63           C
ANISOU 1540  CB  THR A 203     4793   3458   3008    589    172    213       C
ATOM   1541  OG1 THR A 203       1.404 -11.496   3.457  1.00 26.90           O
ANISOU 1541  OG1 THR A 203     4340   3184   2699    583    115    209       O
ATOM   1542  CG2 THR A 203       0.800 -11.411   1.072  1.00 26.84           C
ANISOU 1542  CG2 THR A 203     4502   3066   2631    509    144    205       C
ATOM   1543  N   PHE A 204       2.133 -14.502   4.288  1.00 27.55           N
ANISOU 1543  N   PHE A 204     4563   3198   2707    705    178    247       N
ATOM   1544  CA  PHE A 204       2.938 -14.910   5.434  1.00 31.96           C
ANISOU 1544  CA  PHE A 204     5058   3800   3286    783    185    256       C
ATOM   1545  C   PHE A 204       3.850 -16.107   5.129  1.00 41.57           C
ANISOU 1545  C   PHE A 204     6351   4969   4475    862    252    272       C
ATOM   1546  O   PHE A 204       4.813 -16.351   5.871  1.00 37.20           O
ANISOU 1546  O   PHE A 204     5736   4452   3946    942    269    279       O
ATOM   1547  CB  PHE A 204       2.035 -15.214   6.604  1.00 33.71           C
ANISOU 1547  CB  PHE A 204     5269   4043   3496    760    128    261       C
ATOM   1548  CG  PHE A 204       1.289 -14.035   7.102  1.00 35.71           C
ANISOU 1548  CG  PHE A 204     5432   4351   3785    699     68    246       C
ATOM   1549  CD1 PHE A 204       1.571 -12.760   6.621  1.00 33.02           C
ANISOU 1549  CD1 PHE A 204     5015   4045   3486    676     65    229       C
ATOM   1550  CD2 PHE A 204       0.305 -14.188   8.064  1.00 35.42           C
ANISOU 1550  CD2 PHE A 204     5390   4330   3739    664     18    249       C
ATOM   1551  CE1 PHE A 204       0.899 -11.669   7.088  1.00 31.20           C
ANISOU 1551  CE1 PHE A 204     4705   3862   3287    623     13    216       C
ATOM   1552  CE2 PHE A 204      -0.378 -13.078   8.546  1.00 37.49           C
ANISOU 1552  CE2 PHE A 204     5566   4641   4035    611    -33    236       C
ATOM   1553  CZ  PHE A 204      -0.077 -11.820   8.052  1.00 34.34           C
ANISOU 1553  CZ  PHE A 204     5094   4277   3678    592    -37    220       C
ATOM   1554  N   GLU A 205       3.488 -16.951   4.162  1.00 46.10           N
ANISOU 1554  N   GLU A 205     7063   5460   4993    843    286    280       N
ATOM   1555  CA  GLU A 205       4.332 -18.078   3.772  1.00 46.08           C
ANISOU 1555  CA  GLU A 205     7145   5403   4960    918    357    296       C
ATOM   1556  C   GLU A 205       5.290 -17.746   2.644  1.00 41.59           C
ANISOU 1556  C   GLU A 205     6583   4812   4408    947    426    291       C
ATOM   1557  O   GLU A 205       6.034 -18.632   2.220  1.00 47.41           O
ANISOU 1557  O   GLU A 205     7391   5501   5123   1011    494    304       O
ATOM   1558  CB  GLU A 205       3.491 -19.291   3.315  1.00 52.18           C
ANISOU 1558  CB  GLU A 205     8080   6088   5657    886    366    308       C
ATOM   1559  CG  GLU A 205       2.224 -19.594   4.111  1.00 53.54           C
ANISOU 1559  CG  GLU A 205     8274   6264   5805    826    300    310       C
ATOM   1560  CD  GLU A 205       2.525 -19.945   5.555  1.00 57.61           C
ANISOU 1560  CD  GLU A 205     8725   6828   6336    886    282    320       C
ATOM   1561  OE1 GLU A 205       3.689 -20.322   5.841  1.00 58.39           O
ANISOU 1561  OE1 GLU A 205     8799   6939   6449    980    324    331       O
ATOM   1562  OE2 GLU A 205       1.599 -19.858   6.394  1.00 58.86           O
ANISOU 1562  OE2 GLU A 205     8861   7010   6493    840    225    319       O
ATOM   1563  N   LEU A 206       5.240 -16.539   2.088  1.00 39.34           N
ANISOU 1563  N   LEU A 206     6240   4552   4156    898    416    273       N
ATOM   1564  CA  LEU A 206       6.021 -16.287   0.888  1.00 37.14           C
ANISOU 1564  CA  LEU A 206     5992   4238   3883    915    488    268       C
ATOM   1565  C   LEU A 206       7.502 -16.155   1.213  1.00 38.00           C
ANISOU 1565  C   LEU A 206     6000   4390   4048   1007    542    270       C
ATOM   1566  O   LEU A 206       7.879 -15.683   2.292  1.00 32.84           O
ANISOU 1566  O   LEU A 206     5217   3816   3445   1035    506    266       O
ATOM   1567  CB  LEU A 206       5.577 -15.044   0.137  1.00 37.36           C
ANISOU 1567  CB  LEU A 206     5996   4272   3925    839    467    249       C
ATOM   1568  CG  LEU A 206       4.217 -14.954  -0.541  1.00 36.68           C
ANISOU 1568  CG  LEU A 206     6009   4139   3790    745    420    245       C
ATOM   1569  CD1 LEU A 206       3.861 -13.497  -0.600  1.00 36.60           C
ANISOU 1569  CD1 LEU A 206     5908   4179   3821    688    375    227       C
ATOM   1570  CD2 LEU A 206       4.297 -15.532  -1.932  1.00 35.21           C
ANISOU 1570  CD2 LEU A 206     5972   3859   3548    737    480    249       C
ATOM   1571  N   PRO A 207       8.358 -16.610   0.307  1.00 40.38           N
ANISOU 1571  N   PRO A 207     6363   4640   4341   1055    629    276       N
ATOM   1572  CA  PRO A 207       9.788 -16.433   0.507  1.00 39.14           C
ANISOU 1572  CA  PRO A 207     6104   4524   4245   1140    686    276       C
ATOM   1573  C   PRO A 207      10.101 -14.962   0.512  1.00 37.26           C
ANISOU 1573  C   PRO A 207     5733   4351   4071   1107    670    254       C
ATOM   1574  O   PRO A 207       9.497 -14.190  -0.226  1.00 36.62           O
ANISOU 1574  O   PRO A 207     5682   4251   3979   1031    658    240       O
ATOM   1575  CB  PRO A 207      10.395 -17.118  -0.718  1.00 37.26           C
ANISOU 1575  CB  PRO A 207     5980   4200   3975   1177    787    285       C
ATOM   1576  CG  PRO A 207       9.377 -18.159  -1.059  1.00 37.15           C
ANISOU 1576  CG  PRO A 207     6134   4107   3876   1142    773    297       C
ATOM   1577  CD  PRO A 207       8.082 -17.441  -0.876  1.00 37.77           C
ANISOU 1577  CD  PRO A 207     6203   4207   3942   1041    682    284       C
ATOM   1578  N   GLY A 208      11.088 -14.593   1.316  1.00 37.85           N
ANISOU 1578  N   GLY A 208     5666   4500   4213   1166    671    250       N
ATOM   1579  CA  GLY A 208      11.545 -13.228   1.387  1.00 36.97           C
ANISOU 1579  CA  GLY A 208     5423   4455   4170   1140    663    228       C
ATOM   1580  C   GLY A 208      11.842 -12.710  -0.002  1.00 38.53           C
ANISOU 1580  C   GLY A 208     5670   4602   4368   1111    737    217       C
ATOM   1581  O   GLY A 208      12.330 -13.449  -0.874  1.00 40.48           O
ANISOU 1581  O   GLY A 208     6009   4782   4590   1151    819    228       O
ATOM   1582  N   GLY A 209      11.519 -11.452  -0.222  1.00 31.06           N
ANISOU 1582  N   GLY A 209     4671   3683   3445   1042    710    197       N
ATOM   1583  CA  GLY A 209      11.672 -10.837  -1.518  1.00 34.73           C
ANISOU 1583  CA  GLY A 209     5189   4100   3906   1005    772    185       C
ATOM   1584  C   GLY A 209      10.638  -9.739  -1.703  1.00 38.99           C
ANISOU 1584  C   GLY A 209     5730   4650   4435    910    709    169       C
ATOM   1585  O   GLY A 209       9.891  -9.406  -0.783  1.00 29.58           O
ANISOU 1585  O   GLY A 209     4484   3508   3248    878    623    166       O
ATOM   1586  N   VAL A 210      10.610  -9.205  -2.931  1.00 31.44           N
ANISOU 1586  N   VAL A 210     4843   3640   3461    870    758    160       N
ATOM   1587  CA  VAL A 210       9.730  -8.114  -3.335  1.00 30.27           C
ANISOU 1587  CA  VAL A 210     4709   3490   3301    786    711    146       C
ATOM   1588  C   VAL A 210       8.584  -8.699  -4.147  1.00 32.61           C
ANISOU 1588  C   VAL A 210     5171   3707   3515    739    687    156       C
ATOM   1589  O   VAL A 210       8.820  -9.452  -5.103  1.00 33.38           O
ANISOU 1589  O   VAL A 210     5390   3727   3567    758    753    166       O
ATOM   1590  CB  VAL A 210      10.493  -7.081  -4.187  1.00 30.00           C
ANISOU 1590  CB  VAL A 210     4648   3448   3301    772    782    128       C
ATOM   1591  CG1 VAL A 210       9.579  -5.978  -4.614  1.00 29.47           C
ANISOU 1591  CG1 VAL A 210     4605   3375   3218    691    734    115       C
ATOM   1592  CG2 VAL A 210      11.706  -6.540  -3.460  1.00 30.24           C
ANISOU 1592  CG2 VAL A 210     4515   3555   3418    817    812    116       C
ATOM   1593  N   TYR A 211       7.347  -8.323  -3.821  1.00 28.98           N
ANISOU 1593  N   TYR A 211     4716   3261   3033    675    596    154       N
ATOM   1594  CA  TYR A 211       6.204  -8.860  -4.549  1.00 28.90           C
ANISOU 1594  CA  TYR A 211     4853   3180   2947    625    562    163       C
ATOM   1595  C   TYR A 211       5.245  -7.741  -4.880  1.00 29.60           C
ANISOU 1595  C   TYR A 211     4941   3275   3030    548    501    151       C
ATOM   1596  O   TYR A 211       4.782  -7.032  -3.978  1.00 31.40           O
ANISOU 1596  O   TYR A 211     5066   3570   3295    524    434    145       O
ATOM   1597  CB  TYR A 211       5.461  -9.932  -3.750  1.00 29.45           C
ANISOU 1597  CB  TYR A 211     4951   3252   2987    630    505    178       C
ATOM   1598  CG  TYR A 211       6.265 -11.167  -3.402  1.00 31.89           C
ANISOU 1598  CG  TYR A 211     5279   3547   3291    708    559    193       C
ATOM   1599  CD1 TYR A 211       7.063 -11.189  -2.270  1.00 32.05           C
ANISOU 1599  CD1 TYR A 211     5171   3638   3368    769    562    194       C
ATOM   1600  CD2 TYR A 211       6.218 -12.313  -4.199  1.00 34.03           C
ANISOU 1600  CD2 TYR A 211     5700   3733   3499    722    604    207       C
ATOM   1601  CE1 TYR A 211       7.779 -12.306  -1.927  1.00 34.87           C
ANISOU 1601  CE1 TYR A 211     5545   3984   3721    845    606    209       C
ATOM   1602  CE2 TYR A 211       6.940 -13.451  -3.861  1.00 32.89           C
ANISOU 1602  CE2 TYR A 211     5576   3572   3348    798    655    222       C
ATOM   1603  CZ  TYR A 211       7.724 -13.441  -2.731  1.00 33.87           C
ANISOU 1603  CZ  TYR A 211     5568   3770   3532    862    656    224       C
ATOM   1604  OH  TYR A 211       8.472 -14.547  -2.373  1.00 34.22           O
ANISOU 1604  OH  TYR A 211     5628   3802   3573    944    704    240       O
ATOM   1605  N   ASN A 212       4.959  -7.579  -6.159  1.00 28.62           N
ANISOU 1605  N   ASN A 212     4936   3080   2859    512    524    150       N
ATOM   1606  CA  ASN A 212       3.800  -6.803  -6.544  1.00 28.23           C
ANISOU 1606  CA  ASN A 212     4918   3021   2785    438    452    144       C
ATOM   1607  C   ASN A 212       2.545  -7.397  -5.914  1.00 30.94           C
ANISOU 1607  C   ASN A 212     5279   3375   3103    404    360    154       C
ATOM   1608  O   ASN A 212       2.286  -8.608  -6.016  1.00 28.12           O
ANISOU 1608  O   ASN A 212     5012   2973   2700    413    361    167       O
ATOM   1609  CB  ASN A 212       3.664  -6.781  -8.057  1.00 28.63           C
ANISOU 1609  CB  ASN A 212     5119   2984   2777    410    488    144       C
ATOM   1610  CG  ASN A 212       4.760  -5.989  -8.722  1.00 30.99           C
ANISOU 1610  CG  ASN A 212     5401   3271   3102    431    577    132       C
ATOM   1611  OD1 ASN A 212       5.392  -5.079  -8.123  1.00 28.77           O
ANISOU 1611  OD1 ASN A 212     4987   3056   2889    445    591    120       O
ATOM   1612  ND2 ASN A 212       5.017  -6.337  -9.966  1.00 32.16           N
ANISOU 1612  ND2 ASN A 212     5689   3334   3198    431    640    135       N
ATOM   1613  N   TYR A 213       1.785  -6.537  -5.229  1.00 27.29           N
ANISOU 1613  N   TYR A 213     4727   2971   2672    365    283    148       N
ATOM   1614  CA  TYR A 213       0.617  -6.926  -4.431  1.00 27.45           C
ANISOU 1614  CA  TYR A 213     4731   3014   2683    333    197    155       C
ATOM   1615  C   TYR A 213      -0.481  -5.884  -4.663  1.00 28.06           C
ANISOU 1615  C   TYR A 213     4796   3103   2762    267    124    149       C
ATOM   1616  O   TYR A 213      -0.573  -4.859  -3.970  1.00 26.11           O
ANISOU 1616  O   TYR A 213     4436   2919   2565    259     94    140       O
ATOM   1617  CB  TYR A 213       1.008  -7.041  -2.967  1.00 27.07           C
ANISOU 1617  CB  TYR A 213     4557   3043   2688    374    187    156       C
ATOM   1618  CG  TYR A 213       0.024  -7.731  -2.061  1.00 27.38           C
ANISOU 1618  CG  TYR A 213     4589   3099   2716    355    121    165       C
ATOM   1619  CD1 TYR A 213      -0.188  -9.105  -2.141  1.00 30.66           C
ANISOU 1619  CD1 TYR A 213     5100   3466   3084    366    129    179       C
ATOM   1620  CD2 TYR A 213      -0.666  -7.011  -1.090  1.00 28.97           C
ANISOU 1620  CD2 TYR A 213     4690   3364   2955    328     55    160       C
ATOM   1621  CE1 TYR A 213      -1.071  -9.755  -1.281  1.00 28.64           C
ANISOU 1621  CE1 TYR A 213     4839   3223   2818    347     75    187       C
ATOM   1622  CE2 TYR A 213      -1.544  -7.634  -0.234  1.00 26.50           C
ANISOU 1622  CE2 TYR A 213     4369   3065   2634    311      2    169       C
ATOM   1623  CZ  TYR A 213      -1.750  -9.006  -0.333  1.00 27.91           C
ANISOU 1623  CZ  TYR A 213     4643   3196   2767    319     12    182       C
ATOM   1624  OH  TYR A 213      -2.625  -9.609   0.536  1.00 25.83           O
ANISOU 1624  OH  TYR A 213     4372   2945   2497    299    -36    190       O
ATOM   1625  N   GLY A 214      -1.339  -6.168  -5.622  1.00 28.57           N
ANISOU 1625  N   GLY A 214     4980   3104   2770    221     92    154       N
ATOM   1626  CA  GLY A 214      -2.429  -5.267  -5.933  1.00 28.21           C
ANISOU 1626  CA  GLY A 214     4933   3064   2722    162     18    150       C
ATOM   1627  C   GLY A 214      -2.992  -5.612  -7.288  1.00 26.87           C
ANISOU 1627  C   GLY A 214     4916   2811   2482    123      5    155       C
ATOM   1628  O   GLY A 214      -2.604  -6.602  -7.911  1.00 27.48           O
ANISOU 1628  O   GLY A 214     5103   2827   2513    139     51    160       O
ATOM   1629  N   ALA A 215      -3.939  -4.787  -7.718  1.00 26.73           N
ANISOU 1629  N   ALA A 215     4907   2791   2458     73    -62    152       N
ATOM   1630  CA  ALA A 215      -4.583  -4.987  -9.004  1.00 29.10           C
ANISOU 1630  CA  ALA A 215     5350   3015   2691     31    -91    156       C
ATOM   1631  C   ALA A 215      -3.624  -4.693 -10.163  1.00 33.02           C
ANISOU 1631  C   ALA A 215     5937   3454   3155     52    -11    151       C
ATOM   1632  O   ALA A 215      -2.644  -3.953 -10.027  1.00 36.58           O
ANISOU 1632  O   ALA A 215     6323   3931   3645     87     53    143       O
ATOM   1633  CB  ALA A 215      -5.831  -4.112  -9.125  1.00 30.17           C
ANISOU 1633  CB  ALA A 215     5462   3169   2833    -22   -187    156       C
ATOM   1634  N   SER A 216      -3.910  -5.316 -11.307  1.00 30.71           N
ANISOU 1634  N   SER A 216     5801   3078   2789     29    -12    156       N
ATOM   1635  CA  SER A 216      -3.243  -5.072 -12.580  1.00 32.42           C
ANISOU 1635  CA  SER A 216     6135   3224   2959     37     54    152       C
ATOM   1636  C   SER A 216      -4.125  -4.169 -13.412  1.00 34.75           C
ANISOU 1636  C   SER A 216     6485   3495   3225    -12    -16    151       C
ATOM   1637  O   SER A 216      -5.324  -4.030 -13.145  1.00 36.27           O
ANISOU 1637  O   SER A 216     6650   3711   3420    -55   -118    155       O
ATOM   1638  CB  SER A 216      -2.984  -6.368 -13.354  1.00 32.84           C
ANISOU 1638  CB  SER A 216     6342   3193   2942     44     99    159       C
ATOM   1639  OG  SER A 216      -4.171  -6.796 -14.020  1.00 34.82           O
ANISOU 1639  OG  SER A 216     6706   3394   3129    -15     14    164       O
ATOM   1640  N   ASN A 217      -3.537  -3.581 -14.449  1.00 34.43           N
ANISOU 1640  N   ASN A 217     6528   3402   3154     -5     40    146       N
ATOM   1641  CA  ASN A 217      -4.316  -2.656 -15.256  1.00 40.08           C
ANISOU 1641  CA  ASN A 217     7300   4092   3838    -46    -24    145       C
ATOM   1642  C   ASN A 217      -3.661  -2.475 -16.613  1.00 38.30           C
ANISOU 1642  C   ASN A 217     7223   3779   3551    -39     48    143       C
ATOM   1643  O   ASN A 217      -2.483  -2.114 -16.691  1.00 35.38           O
ANISOU 1643  O   ASN A 217     6832   3406   3204     -0    152    135       O
ATOM   1644  CB  ASN A 217      -4.465  -1.293 -14.535  1.00 36.57           C
ANISOU 1644  CB  ASN A 217     6708   3724   3464    -45    -54    139       C
ATOM   1645  CG  ASN A 217      -5.499  -0.383 -15.198  1.00 39.25           C
ANISOU 1645  CG  ASN A 217     7092   4047   3776    -87   -142    142       C
ATOM   1646  OD1 ASN A 217      -5.985  -0.666 -16.311  1.00 39.43           O
ANISOU 1646  OD1 ASN A 217     7262   3996   3725   -115   -175    147       O
ATOM   1647  ND2 ASN A 217      -5.830   0.730 -14.521  1.00 34.81           N
ANISOU 1647  ND2 ASN A 217     6405   3549   3271    -89   -180    139       N
ATOM   1648  N   THR A 218      -4.468  -2.632 -17.662  1.00 36.89           N
ANISOU 1648  N   THR A 218     7189   3532   3296    -81    -13    148       N
ATOM   1649  CA  THR A 218      -4.066  -2.504 -19.054  1.00 36.05           C
ANISOU 1649  CA  THR A 218     7252   3332   3115    -83     40    146       C
ATOM   1650  C   THR A 218      -4.591  -1.228 -19.712  1.00 44.82           C
ANISOU 1650  C   THR A 218     8393   4429   4208   -108    -12    145       C
ATOM   1651  O   THR A 218      -4.467  -1.081 -20.934  1.00 48.11           O
ANISOU 1651  O   THR A 218     8965   4762   4551   -118     12    145       O
ATOM   1652  CB  THR A 218      -4.556  -3.715 -19.863  1.00 45.31           C
ANISOU 1652  CB  THR A 218     8594   4424   4200   -111     11    153       C
ATOM   1653  OG1 THR A 218      -5.986  -3.805 -19.778  1.00 50.49           O
ANISOU 1653  OG1 THR A 218     9249   5096   4840   -164   -129    159       O
ATOM   1654  CG2 THR A 218      -3.957  -5.018 -19.346  1.00 37.25           C
ANISOU 1654  CG2 THR A 218     7567   3400   3185    -82     75    155       C
ATOM   1655  N   SER A 219      -5.258  -0.345 -18.974  1.00 43.51           N
ANISOU 1655  N   SER A 219     8095   4337   4098   -120    -89    145       N
ATOM   1656  CA  SER A 219      -5.693   0.912 -19.551  1.00 44.74           C
ANISOU 1656  CA  SER A 219     8276   4482   4241   -137   -132    145       C
ATOM   1657  C   SER A 219      -5.064   2.095 -18.817  1.00 47.32           C
ANISOU 1657  C   SER A 219     8458   4874   4645   -109    -81    136       C
ATOM   1658  O   SER A 219      -4.528   1.955 -17.710  1.00 45.84           O
ANISOU 1658  O   SER A 219     8132   4755   4529    -84    -41    130       O
ATOM   1659  CB  SER A 219      -7.226   1.019 -19.550  1.00 50.91           C
ANISOU 1659  CB  SER A 219     9054   5280   5008   -181   -281    154       C
ATOM   1660  OG  SER A 219      -7.780   0.158 -20.538  1.00 47.28           O
ANISOU 1660  OG  SER A 219     8759   4743   4461   -213   -328    161       O
ATOM   1661  N   ASN A 220      -5.072   3.256 -19.485  1.00 44.55           N
ANISOU 1661  N   ASN A 220     8154   4497   4277   -114    -78    133       N
ATOM   1662  CA  ASN A 220      -4.532   4.453 -18.867  1.00 43.66           C
ANISOU 1662  CA  ASN A 220     7917   4440   4233    -94    -33    124       C
ATOM   1663  C   ASN A 220      -5.573   5.029 -17.901  1.00 37.53           C
ANISOU 1663  C   ASN A 220     7005   3744   3512   -109   -140    128       C
ATOM   1664  O   ASN A 220      -6.738   4.626 -17.904  1.00 32.92           O
ANISOU 1664  O   ASN A 220     6436   3164   2907   -136   -249    139       O
ATOM   1665  CB  ASN A 220      -4.064   5.479 -19.928  1.00 42.44           C
ANISOU 1665  CB  ASN A 220     7867   4222   4038    -92     24    119       C
ATOM   1666  CG  ASN A 220      -5.193   6.010 -20.844  1.00 44.69           C
ANISOU 1666  CG  ASN A 220     8265   4458   4256   -122    -78    130       C
ATOM   1667  OD1 ASN A 220      -6.338   6.210 -20.424  1.00 42.54           O
ANISOU 1667  OD1 ASN A 220     7934   4228   4001   -141   -195    138       O
ATOM   1668  ND2 ASN A 220      -4.838   6.297 -22.096  1.00 45.33           N
ANISOU 1668  ND2 ASN A 220     8509   4449   4264   -123    -30    129       N
ATOM   1669  N   SER A 221      -5.134   5.976 -17.058  1.00 38.43           N
ANISOU 1669  N   SER A 221     6982   3922   3697    -92   -106    119       N
ATOM   1670  CA  SER A 221      -6.031   6.511 -16.029  1.00 40.93           C
ANISOU 1670  CA  SER A 221     7162   4317   4071   -101   -194    122       C
ATOM   1671  C   SER A 221      -7.281   7.147 -16.631  1.00 38.91           C
ANISOU 1671  C   SER A 221     6964   4039   3780   -127   -301    134       C
ATOM   1672  O   SER A 221      -8.396   6.967 -16.121  1.00 37.58           O
ANISOU 1672  O   SER A 221     6737   3910   3631   -145   -402    143       O
ATOM   1673  CB  SER A 221      -5.307   7.513 -15.135  1.00 39.16           C
ANISOU 1673  CB  SER A 221     6801   4155   3921    -81   -135    109       C
ATOM   1674  OG  SER A 221      -4.449   6.870 -14.226  1.00 37.83           O
ANISOU 1674  OG  SER A 221     6538   4034   3803    -58    -72    101       O
ATOM   1675  N   TYR A 222      -7.125   7.909 -17.700  1.00 36.75           N
ANISOU 1675  N   TYR A 222     6804   3703   3458   -128   -280    134       N
ATOM   1676  CA  TYR A 222      -8.304   8.521 -18.284  1.00 39.69           C
ANISOU 1676  CA  TYR A 222     7232   4053   3794   -148   -386    146       C
ATOM   1677  C   TYR A 222      -9.341   7.462 -18.647  1.00 41.04           C
ANISOU 1677  C   TYR A 222     7470   4202   3921   -175   -488    159       C
ATOM   1678  O   TYR A 222     -10.507   7.566 -18.244  1.00 38.85           O
ANISOU 1678  O   TYR A 222     7129   3965   3667   -192   -597    169       O
ATOM   1679  CB  TYR A 222      -7.924   9.343 -19.510  1.00 43.14           C
ANISOU 1679  CB  TYR A 222     7810   4412   4169   -144   -344    145       C
ATOM   1680  CG  TYR A 222      -9.115   9.935 -20.223  1.00 44.21           C
ANISOU 1680  CG  TYR A 222     8021   4517   4259   -159   -457    159       C
ATOM   1681  CD1 TYR A 222     -10.140  10.546 -19.512  1.00 46.51           C
ANISOU 1681  CD1 TYR A 222     8200   4872   4600   -162   -553    167       C
ATOM   1682  CD2 TYR A 222      -9.222   9.862 -21.600  1.00 44.17           C
ANISOU 1682  CD2 TYR A 222     8202   4419   4161   -169   -470    165       C
ATOM   1683  CE1 TYR A 222     -11.233  11.075 -20.159  1.00 50.82           C
ANISOU 1683  CE1 TYR A 222     8809   5392   5108   -171   -660    182       C
ATOM   1684  CE2 TYR A 222     -10.308  10.392 -22.263  1.00 49.63           C
ANISOU 1684  CE2 TYR A 222     8965   5083   4809   -180   -580    180       C
ATOM   1685  CZ  TYR A 222     -11.314  11.005 -21.539  1.00 52.66           C
ANISOU 1685  CZ  TYR A 222     9226   5534   5247   -180   -676    188       C
ATOM   1686  OH  TYR A 222     -12.409  11.548 -22.183  1.00 48.81           O
ANISOU 1686  OH  TYR A 222     8801   5023   4722   -186   -790    204       O
ATOM   1687  N   GLU A 223      -8.923   6.422 -19.389  1.00 40.11           N
ANISOU 1687  N   GLU A 223     7478   4021   3742   -182   -451    158       N
ATOM   1688  CA  GLU A 223      -9.852   5.378 -19.817  1.00 40.62           C
ANISOU 1688  CA  GLU A 223     7622   4056   3757   -214   -543    169       C
ATOM   1689  C   GLU A 223     -10.402   4.598 -18.643  1.00 40.45           C
ANISOU 1689  C   GLU A 223     7467   4107   3794   -225   -592    171       C
ATOM   1690  O   GLU A 223     -11.572   4.200 -18.641  1.00 40.35           O
ANISOU 1690  O   GLU A 223     7454   4104   3773   -257   -703    180       O
ATOM   1691  CB  GLU A 223      -9.146   4.413 -20.761  1.00 44.52           C
ANISOU 1691  CB  GLU A 223     8276   4465   4175   -216   -475    166       C
ATOM   1692  CG  GLU A 223      -8.834   4.922 -22.132  1.00 46.90           C
ANISOU 1692  CG  GLU A 223     8750   4676   4395   -215   -444    166       C
ATOM   1693  CD  GLU A 223     -10.070   5.177 -22.969  1.00 53.20           C
ANISOU 1693  CD  GLU A 223     9646   5435   5132   -246   -574    178       C
ATOM   1694  OE1 GLU A 223     -11.201   5.044 -22.448  1.00 55.60           O
ANISOU 1694  OE1 GLU A 223     9867   5790   5466   -268   -690    186       O
ATOM   1695  OE2 GLU A 223      -9.899   5.438 -24.182  1.00 56.46           O
ANISOU 1695  OE2 GLU A 223    10225   5763   5464   -248   -559    180       O
ATOM   1696  N   THR A 224      -9.554   4.329 -17.656  1.00 38.84           N
ANISOU 1696  N   THR A 224     7155   3953   3649   -200   -510    162       N
ATOM   1697  CA  THR A 224      -9.969   3.544 -16.503  1.00 37.78           C
ANISOU 1697  CA  THR A 224     6903   3883   3567   -207   -545    164       C
ATOM   1698  C   THR A 224     -10.990   4.302 -15.658  1.00 39.86           C
ANISOU 1698  C   THR A 224     7031   4219   3893   -217   -632    169       C
ATOM   1699  O   THR A 224     -12.017   3.736 -15.254  1.00 38.74           O
ANISOU 1699  O   THR A 224     6850   4105   3766   -244   -719    176       O
ATOM   1700  CB  THR A 224      -8.733   3.151 -15.691  1.00 39.60           C
ANISOU 1700  CB  THR A 224     7057   4146   3841   -172   -433    153       C
ATOM   1701  OG1 THR A 224      -7.858   2.361 -16.522  1.00 43.24           O
ANISOU 1701  OG1 THR A 224     7650   4536   4245   -162   -353    150       O
ATOM   1702  CG2 THR A 224      -9.128   2.362 -14.451  1.00 34.72           C
ANISOU 1702  CG2 THR A 224     6322   3593   3276   -176   -466    155       C
ATOM   1703  N   TYR A 225     -10.718   5.587 -15.379  1.00 37.97           N
ANISOU 1703  N   TYR A 225     6723   4011   3694   -196   -607    164       N
ATOM   1704  CA  TYR A 225     -11.604   6.377 -14.531  1.00 38.38           C
ANISOU 1704  CA  TYR A 225     6644   4131   3807   -199   -678    169       C
ATOM   1705  C   TYR A 225     -12.916   6.671 -15.233  1.00 44.17           C
ANISOU 1705  C   TYR A 225     7432   4841   4509   -226   -795    183       C
ATOM   1706  O   TYR A 225     -13.963   6.770 -14.580  1.00 44.18           O
ANISOU 1706  O   TYR A 225     7338   4892   4555   -240   -878    190       O
ATOM   1707  CB  TYR A 225     -10.906   7.667 -14.110  1.00 39.61           C
ANISOU 1707  CB  TYR A 225     6726   4318   4007   -170   -613    160       C
ATOM   1708  CG  TYR A 225      -9.720   7.438 -13.202  1.00 38.52           C
ANISOU 1708  CG  TYR A 225     6501   4219   3914   -145   -512    146       C
ATOM   1709  CD1 TYR A 225      -9.660   6.335 -12.369  1.00 35.25           C
ANISOU 1709  CD1 TYR A 225     6026   3841   3526   -145   -508    146       C
ATOM   1710  CD2 TYR A 225      -8.644   8.316 -13.198  1.00 40.16           C
ANISOU 1710  CD2 TYR A 225     6692   4427   4139   -122   -422    133       C
ATOM   1711  CE1 TYR A 225      -8.568   6.126 -11.533  1.00 35.40           C
ANISOU 1711  CE1 TYR A 225     5966   3897   3586   -118   -422    134       C
ATOM   1712  CE2 TYR A 225      -7.545   8.111 -12.382  1.00 38.65           C
ANISOU 1712  CE2 TYR A 225     6417   4275   3992    -99   -335    120       C
ATOM   1713  CZ  TYR A 225      -7.514   7.018 -11.555  1.00 36.37           C
ANISOU 1713  CZ  TYR A 225     6068   4024   3729    -95   -338    121       C
ATOM   1714  OH  TYR A 225      -6.420   6.803 -10.766  1.00 32.24           O
ANISOU 1714  OH  TYR A 225     5464   3538   3247    -69   -258    110       O
ATOM   1715  N   LYS A 226     -12.872   6.804 -16.561  1.00 41.30           N
ANISOU 1715  N   LYS A 226     7222   4400   4070   -233   -804    186       N
ATOM   1716  CA  LYS A 226     -14.090   6.936 -17.354  1.00 46.08           C
ANISOU 1716  CA  LYS A 226     7897   4975   4634   -259   -924    199       C
ATOM   1717  C   LYS A 226     -14.964   5.687 -17.238  1.00 44.12           C
ANISOU 1717  C   LYS A 226     7652   4733   4379   -297  -1004    205       C
ATOM   1718  O   LYS A 226     -16.198   5.777 -17.216  1.00 49.30           O
ANISOU 1718  O   LYS A 226     8274   5410   5048   -321  -1116    216       O
ATOM   1719  CB  LYS A 226     -13.712   7.215 -18.817  1.00 43.68           C
ANISOU 1719  CB  LYS A 226     7775   4580   4241   -257   -906    201       C
ATOM   1720  CG  LYS A 226     -14.854   7.245 -19.795  1.00 47.76           C
ANISOU 1720  CG  LYS A 226     8392   5054   4700   -284  -1029    214       C
ATOM   1721  CD  LYS A 226     -14.539   8.204 -20.936  1.00 58.86           C
ANISOU 1721  CD  LYS A 226     9931   6391   6042   -267  -1011    216       C
ATOM   1722  CE  LYS A 226     -13.343   7.763 -21.761  1.00 50.85           C
ANISOU 1722  CE  LYS A 226     9062   5299   4959   -261   -901    207       C
ATOM   1723  NZ  LYS A 226     -13.440   8.287 -23.152  1.00 51.53           N
ANISOU 1723  NZ  LYS A 226     9326   5299   4956   -262   -925    213       N
ATOM   1724  N   GLU A 227     -14.347   4.513 -17.157  1.00 43.81           N
ANISOU 1724  N   GLU A 227     7652   4674   4319   -304   -947    199       N
ATOM   1725  CA  GLU A 227     -15.128   3.282 -17.113  1.00 46.53           C
ANISOU 1725  CA  GLU A 227     8016   5015   4649   -344  -1016    203       C
ATOM   1726  C   GLU A 227     -15.753   3.053 -15.737  1.00 44.01           C
ANISOU 1726  C   GLU A 227     7527   4780   4413   -352  -1050    204       C
ATOM   1727  O   GLU A 227     -16.891   2.593 -15.636  1.00 43.44           O
ANISOU 1727  O   GLU A 227     7431   4723   4351   -390  -1146    211       O
ATOM   1728  CB  GLU A 227     -14.232   2.128 -17.500  1.00 44.48           C
ANISOU 1728  CB  GLU A 227     7864   4701   4336   -345   -937    196       C
ATOM   1729  CG  GLU A 227     -14.914   0.820 -17.745  1.00 49.23           C
ANISOU 1729  CG  GLU A 227     8532   5274   4899   -390   -999    199       C
ATOM   1730  CD  GLU A 227     -13.950  -0.144 -18.425  1.00 59.18           C
ANISOU 1730  CD  GLU A 227     9936   6461   6090   -385   -913    193       C
ATOM   1731  OE1 GLU A 227     -12.808   0.283 -18.713  1.00 63.59           O
ANISOU 1731  OE1 GLU A 227    10533   6993   6635   -346   -811    187       O
ATOM   1732  OE2 GLU A 227     -14.307  -1.318 -18.665  1.00 65.44           O
ANISOU 1732  OE2 GLU A 227    10803   7220   6843   -420   -944    193       O
ATOM   1733  N   ILE A 228     -15.030   3.372 -14.667  1.00 43.51           N
ANISOU 1733  N   ILE A 228     7347   4772   4413   -318   -971    197       N
ATOM   1734  CA  ILE A 228     -15.607   3.244 -13.332  1.00 47.56           C
ANISOU 1734  CA  ILE A 228     7703   5363   5003   -323   -998    199       C
ATOM   1735  C   ILE A 228     -16.768   4.215 -13.159  1.00 49.12           C
ANISOU 1735  C   ILE A 228     7822   5600   5243   -332  -1091    208       C
ATOM   1736  O   ILE A 228     -17.801   3.873 -12.572  1.00 51.81           O
ANISOU 1736  O   ILE A 228     8083   5979   5624   -359  -1162    214       O
ATOM   1737  CB  ILE A 228     -14.521   3.435 -12.259  1.00 42.67           C
ANISOU 1737  CB  ILE A 228     6985   4791   4436   -283   -894    189       C
ATOM   1738  CG1 ILE A 228     -13.785   2.114 -12.042  1.00 40.00           C
ANISOU 1738  CG1 ILE A 228     6684   4435   4077   -281   -830    183       C
ATOM   1739  CG2 ILE A 228     -15.114   3.919 -10.937  1.00 41.76           C
ANISOU 1739  CG2 ILE A 228     6704   4758   4404   -279   -922    190       C
ATOM   1740  CD1 ILE A 228     -12.417   2.293 -11.417  1.00 39.39           C
ANISOU 1740  CD1 ILE A 228     6556   4382   4028   -236   -717    173       C
ATOM   1741  N   ALA A 229     -16.646   5.415 -13.720  1.00 49.79           N
ANISOU 1741  N   ALA A 229     7932   5668   5316   -311  -1091    210       N
ATOM   1742  CA  ALA A 229     -17.738   6.378 -13.637  1.00 52.31           C
ANISOU 1742  CA  ALA A 229     8185   6019   5671   -313  -1179    221       C
ATOM   1743  C   ALA A 229     -19.044   5.780 -14.159  1.00 53.34           C
ANISOU 1743  C   ALA A 229     8350   6135   5783   -356  -1301    232       C
ATOM   1744  O   ALA A 229     -20.091   5.922 -13.514  1.00 56.10           O
ANISOU 1744  O   ALA A 229     8590   6535   6190   -369  -1371    239       O
ATOM   1745  CB  ALA A 229     -17.376   7.638 -14.420  1.00 42.33           C
ANISOU 1745  CB  ALA A 229     6985   4721   4378   -284  -1163    222       C
ATOM   1746  N   LYS A 230     -18.989   5.054 -15.290  1.00 52.20           N
ANISOU 1746  N   LYS A 230     8356   5920   5558   -381  -1325    232       N
ATOM   1747  CA  LYS A 230     -20.203   4.467 -15.867  1.00 51.95           C
ANISOU 1747  CA  LYS A 230     8367   5871   5502   -428  -1446    241       C
ATOM   1748  C   LYS A 230     -20.882   3.549 -14.872  1.00 50.35           C
ANISOU 1748  C   LYS A 230     8057   5719   5356   -461  -1475    240       C
ATOM   1749  O   LYS A 230     -22.103   3.593 -14.707  1.00 55.90           O
ANISOU 1749  O   LYS A 230     8691   6453   6096   -489  -1575    249       O
ATOM   1750  CB  LYS A 230     -19.869   3.649 -17.116  1.00 51.16           C
ANISOU 1750  CB  LYS A 230     8452   5685   5303   -453  -1449    238       C
ATOM   1751  CG  LYS A 230     -19.014   4.325 -18.151  1.00 57.57           C
ANISOU 1751  CG  LYS A 230     9395   6431   6046   -423  -1397    236       C
ATOM   1752  CD  LYS A 230     -19.255   3.705 -19.522  1.00 59.12           C
ANISOU 1752  CD  LYS A 230     9775   6544   6145   -457  -1454    239       C
ATOM   1753  CE  LYS A 230     -18.197   4.159 -20.528  1.00 67.61           C
ANISOU 1753  CE  LYS A 230    11000   7545   7145   -428  -1374    235       C
ATOM   1754  NZ  LYS A 230     -17.299   3.000 -20.919  1.00 60.27           N
ANISOU 1754  NZ  LYS A 230    10189   6557   6155   -439  -1291    225       N
ATOM   1755  N   ILE A 231     -20.094   2.739 -14.168  1.00 52.05           N
ANISOU 1755  N   ILE A 231     8251   5944   5581   -457  -1387    231       N
ATOM   1756  CA  ILE A 231     -20.647   1.815 -13.192  1.00 52.07           C
ANISOU 1756  CA  ILE A 231     8163   5990   5632   -487  -1403    229       C
ATOM   1757  C   ILE A 231     -21.339   2.582 -12.059  1.00 59.88           C
ANISOU 1757  C   ILE A 231     8979   7059   6715   -474  -1427    235       C
ATOM   1758  O   ILE A 231     -22.354   2.124 -11.512  1.00 61.64           O
ANISOU 1758  O   ILE A 231     9122   7316   6982   -509  -1488    239       O
ATOM   1759  CB  ILE A 231     -19.521   0.904 -12.678  1.00 50.88           C
ANISOU 1759  CB  ILE A 231     8032   5830   5468   -473  -1294    219       C
ATOM   1760  CG1 ILE A 231     -18.997   0.038 -13.837  1.00 49.86           C
ANISOU 1760  CG1 ILE A 231     8080   5619   5247   -489  -1277    215       C
ATOM   1761  CG2 ILE A 231     -19.986   0.024 -11.510  1.00 50.24           C
ANISOU 1761  CG2 ILE A 231     7851   5797   5441   -496  -1296    218       C
ATOM   1762  CD1 ILE A 231     -17.675  -0.663 -13.570  1.00 45.30           C
ANISOU 1762  CD1 ILE A 231     7543   5021   4647   -461  -1157    206       C
ATOM   1763  N   MET A 232     -20.774   3.743 -11.661  1.00 55.14           N
ANISOU 1763  N   MET A 232     8318   6487   6146   -426  -1374    234       N
ATOM   1764  CA  MET A 232     -21.235   4.567 -10.546  1.00 57.22           C
ANISOU 1764  CA  MET A 232     8425   6821   6495   -406  -1377    237       C
ATOM   1765  C   MET A 232     -22.022   5.782 -10.958  1.00 62.54           C
ANISOU 1765  C   MET A 232     9072   7504   7187   -394  -1449    249       C
ATOM   1766  O   MET A 232     -22.491   6.540 -10.073  1.00 68.08           O
ANISOU 1766  O   MET A 232     9647   8262   7959   -375  -1455    253       O
ATOM   1767  CB  MET A 232     -20.075   5.056  -9.717  1.00 54.93           C
ANISOU 1767  CB  MET A 232     8080   6559   6230   -361  -1267    228       C
ATOM   1768  CG  MET A 232     -19.218   4.012  -9.205  1.00 50.03           C
ANISOU 1768  CG  MET A 232     7472   5937   5599   -361  -1191    218       C
ATOM   1769  SD  MET A 232     -17.897   5.063  -8.657  1.00 46.57           S
ANISOU 1769  SD  MET A 232     6988   5523   5184   -304  -1084    208       S
ATOM   1770  CE  MET A 232     -18.430   5.534  -7.009  1.00 42.50           C
ANISOU 1770  CE  MET A 232     6293   5093   4762   -294  -1084    208       C
ATOM   1771  N   ASP A 233     -22.059   6.060 -12.253  1.00 60.79           N
ANISOU 1771  N   ASP A 233     8972   7225   6899   -396  -1493    253       N
ATOM   1772  CA  ASP A 233     -23.383   6.023 -12.799  1.00 66.96           C
ANISOU 1772  CA  ASP A 233     9755   8003   7683   -428  -1618    266       C
ATOM   1773  C   ASP A 233     -23.384   7.557 -13.020  1.00 69.00           C
ANISOU 1773  C   ASP A 233     9995   8267   7953   -382  -1623    273       C
ATOM   1774  O   ASP A 233     -24.426   8.216 -13.096  1.00 70.16           O
ANISOU 1774  O   ASP A 233    10087   8437   8135   -379  -1708    287       O
ATOM   1775  CB  ASP A 233     -24.227   5.405 -11.696  1.00 71.31           C
ANISOU 1775  CB  ASP A 233    10174   8613   8309   -457  -1645    267       C
ATOM   1776  CG  ASP A 233     -25.281   4.392 -12.092  1.00 83.52           C
ANISOU 1776  CG  ASP A 233    11741  10147   9845   -517  -1743    270       C
ATOM   1777  OD1 ASP A 233     -25.678   4.192 -13.281  1.00 83.16           O
ANISOU 1777  OD1 ASP A 233    11806  10053   9741   -543  -1822    275       O
ATOM   1778  OD2 ASP A 233     -25.569   3.620 -11.133  1.00 89.14           O
ANISOU 1778  OD2 ASP A 233    12369  10897  10606   -542  -1726    266       O
ATOM   1779  N   VAL A 234     -22.135   8.053 -12.936  1.00 64.64           N
ANISOU 1779  N   VAL A 234     9476   7702   7383   -345  -1517    264       N
ATOM   1780  CA  VAL A 234     -21.616   9.429 -13.016  1.00 64.26           C
ANISOU 1780  CA  VAL A 234     9426   7653   7339   -298  -1472    264       C
ATOM   1781  C   VAL A 234     -21.448   9.854 -14.474  1.00 65.56           C
ANISOU 1781  C   VAL A 234     9746   7744   7421   -292  -1501    269       C
ATOM   1782  O   VAL A 234     -20.858   9.102 -15.262  1.00 64.88           O
ANISOU 1782  O   VAL A 234     9786   7601   7264   -309  -1477    263       O
ATOM   1783  CB  VAL A 234     -20.264   9.494 -12.288  1.00 57.54           C
ANISOU 1783  CB  VAL A 234     8547   6816   6500   -273  -1342    248       C
ATOM   1784  CG1 VAL A 234     -19.542  10.774 -12.541  1.00 58.67           C
ANISOU 1784  CG1 VAL A 234     8717   6944   6633   -234  -1284    245       C
ATOM   1785  CG2 VAL A 234     -20.452   9.298 -10.802  1.00 57.39           C
ANISOU 1785  CG2 VAL A 234     8374   6870   6562   -273  -1316    245       C
ATOM   1786  N   PRO A 235     -21.895  11.060 -14.853  1.00 72.26           N
ANISOU 1786  N   PRO A 235    10596   8588   8272   -264  -1544    281       N
ATOM   1787  CA  PRO A 235     -21.786  11.502 -16.258  1.00 68.64           C
ANISOU 1787  CA  PRO A 235    10294   8056   7730   -257  -1576    287       C
ATOM   1788  C   PRO A 235     -20.357  11.424 -16.805  1.00 69.17           C
ANISOU 1788  C   PRO A 235    10483   8067   7734   -247  -1464    273       C
ATOM   1789  O   PRO A 235     -19.385  11.791 -16.130  1.00 66.17           O
ANISOU 1789  O   PRO A 235    10052   7708   7382   -224  -1357    260       O
ATOM   1790  CB  PRO A 235     -22.271  12.958 -16.202  1.00 69.45           C
ANISOU 1790  CB  PRO A 235    10349   8176   7863   -216  -1607    299       C
ATOM   1791  CG  PRO A 235     -23.089  13.068 -14.946  1.00 67.42           C
ANISOU 1791  CG  PRO A 235     9912   8000   7705   -215  -1636    304       C
ATOM   1792  CD  PRO A 235     -22.418  12.125 -13.974  1.00 67.40           C
ANISOU 1792  CD  PRO A 235     9844   8031   7733   -234  -1553    288       C
ATOM   1793  N   GLU A 236     -20.253  11.045 -18.087  1.00 68.25           N
ANISOU 1793  N   GLU A 236    10530   7875   7528   -262  -1493    275       N
ATOM   1794  CA  GLU A 236     -18.950  10.843 -18.724  1.00 65.76           C
ANISOU 1794  CA  GLU A 236    10343   7497   7147   -256  -1387    262       C
ATOM   1795  C   GLU A 236     -18.098  12.116 -18.760  1.00 64.41           C
ANISOU 1795  C   GLU A 236    10184   7314   6977   -215  -1299    257       C
ATOM   1796  O   GLU A 236     -16.890  12.060 -18.497  1.00 58.85           O
ANISOU 1796  O   GLU A 236     9482   6603   6273   -204  -1179    242       O
ATOM   1797  CB  GLU A 236     -19.150  10.319 -20.151  1.00 54.66           C
ANISOU 1797  CB  GLU A 236     9120   6007   5641   -279  -1445    267       C
ATOM   1798  N   ASN A 237     -18.705  13.270 -19.083  1.00 61.33           N
ANISOU 1798  N   ASN A 237     9798   6919   6586   -192  -1355    270       N
ATOM   1799  CA  ASN A 237     -17.940  14.504 -19.299  1.00 61.46           C
ANISOU 1799  CA  ASN A 237     9852   6909   6589   -157  -1275    266       C
ATOM   1800  C   ASN A 237     -17.219  14.988 -18.042  1.00 59.78           C
ANISOU 1800  C   ASN A 237     9500   6758   6455   -138  -1175    252       C
ATOM   1801  O   ASN A 237     -16.291  15.801 -18.149  1.00 60.54           O
ANISOU 1801  O   ASN A 237     9629   6832   6541   -118  -1081    242       O
ATOM   1802  CB  ASN A 237     -18.850  15.588 -19.926  1.00 64.51           C
ANISOU 1802  CB  ASN A 237    10281   7275   6956   -134  -1367    285       C
ATOM   1803  CG  ASN A 237     -19.749  16.330 -18.914  1.00 68.15           C
ANISOU 1803  CG  ASN A 237    10577   7811   7505   -114  -1420    295       C
ATOM   1804  OD1 ASN A 237     -19.360  16.639 -17.784  1.00 65.47           O
ANISOU 1804  OD1 ASN A 237    10110   7529   7235   -103  -1350    285       O
ATOM   1805  ND2 ASN A 237     -20.970  16.635 -19.349  1.00 73.84           N
ANISOU 1805  ND2 ASN A 237    11304   8530   8220   -107  -1546    315       N
ATOM   1806  N   LEU A 238     -17.639  14.520 -16.861  1.00 60.49           N
ANISOU 1806  N   LEU A 238     9439   6923   6620   -147  -1194    251       N
ATOM   1807  CA  LEU A 238     -17.120  14.908 -15.551  1.00 58.76           C
ANISOU 1807  CA  LEU A 238     9078   6771   6479   -133  -1117    239       C
ATOM   1808  C   LEU A 238     -15.771  14.279 -15.247  1.00 56.22           C
ANISOU 1808  C   LEU A 238     8761   6446   6154   -138  -1000    219       C
ATOM   1809  O   LEU A 238     -15.324  14.332 -14.089  1.00 51.62           O
ANISOU 1809  O   LEU A 238     8057   5921   5634   -131   -942    208       O
ATOM   1810  CB  LEU A 238     -18.125  14.551 -14.449  1.00 61.24           C
ANISOU 1810  CB  LEU A 238     9242   7160   6868   -142  -1184    246       C
ATOM   1811  CG  LEU A 238     -19.485  15.260 -14.505  1.00 62.35           C
ANISOU 1811  CG  LEU A 238     9339   7318   7034   -131  -1293    266       C
ATOM   1812  CD1 LEU A 238     -20.288  15.065 -13.220  1.00 59.25           C
ANISOU 1812  CD1 LEU A 238     8779   7005   6729   -135  -1328    270       C
ATOM   1813  CD2 LEU A 238     -19.260  16.737 -14.750  1.00 55.88           C
ANISOU 1813  CD2 LEU A 238     8544   6479   6208    -94  -1264    269       C
ATOM   1814  N   VAL A 239     -15.205  13.573 -16.223  1.00 58.89           N
ANISOU 1814  N   VAL A 239     9234   6720   6422   -151   -972    215       N
ATOM   1815  CA  VAL A 239     -13.857  13.028 -16.184  1.00 55.88           C
ANISOU 1815  CA  VAL A 239     8883   6322   6028   -150   -856    198       C
ATOM   1816  C   VAL A 239     -13.065  13.723 -17.289  1.00 54.35           C
ANISOU 1816  C   VAL A 239     8828   6053   5771   -138   -791    193       C
ATOM   1817  O   VAL A 239     -13.278  13.450 -18.476  1.00 51.32           O
ANISOU 1817  O   VAL A 239     8589   5598   5310   -148   -825    201       O
ATOM   1818  CB  VAL A 239     -13.862  11.505 -16.346  1.00 55.19           C
ANISOU 1818  CB  VAL A 239     8837   6220   5913   -175   -870    197       C
ATOM   1819  CG1 VAL A 239     -12.446  10.932 -16.149  1.00 49.20           C
ANISOU 1819  CG1 VAL A 239     8088   5452   5153   -167   -745    180       C
ATOM   1820  CG2 VAL A 239     -14.837  10.897 -15.323  1.00 52.02           C
ANISOU 1820  CG2 VAL A 239     8306   5887   5571   -191   -946    204       C
ATOM   1821  N   GLU A 240     -12.174  14.639 -16.909  1.00 58.73           N
ANISOU 1821  N   GLU A 240     9340   6620   6355   -119   -697    180       N
ATOM   1822  CA  GLU A 240     -11.396  15.410 -17.878  1.00 61.56           C
ANISOU 1822  CA  GLU A 240     9821   6909   6661   -109   -624    174       C
ATOM   1823  C   GLU A 240     -10.055  14.754 -18.157  1.00 62.56           C
ANISOU 1823  C   GLU A 240    10002   7002   6765   -112   -507    158       C
ATOM   1824  O   GLU A 240      -9.420  14.194 -17.259  1.00 65.44           O
ANISOU 1824  O   GLU A 240    10266   7417   7182   -111   -452    146       O
ATOM   1825  CB  GLU A 240     -11.098  16.819 -17.369  1.00 55.08           C
ANISOU 1825  CB  GLU A 240     8932   6113   5882    -90   -577    167       C
ATOM   1826  CG  GLU A 240     -12.186  17.826 -17.530  1.00 64.45           C
ANISOU 1826  CG  GLU A 240    10121   7300   7067    -78   -666    183       C
ATOM   1827  CD  GLU A 240     -11.644  19.243 -17.435  1.00 73.12           C
ANISOU 1827  CD  GLU A 240    11214   8389   8178    -61   -595    174       C
ATOM   1828  OE1 GLU A 240     -10.451  19.439 -17.083  1.00 67.48           O
ANISOU 1828  OE1 GLU A 240    10470   7682   7487    -63   -481    154       O
ATOM   1829  OE2 GLU A 240     -12.416  20.160 -17.750  1.00 72.96           O
ANISOU 1829  OE2 GLU A 240    11224   8354   8145    -45   -655    188       O
ATOM   1830  N   ASN A 241      -9.589  14.879 -19.394  1.00 49.90           N
ANISOU 1830  N   ASN A 241     8560   5314   5087   -112   -464    157       N
ATOM   1831  CA  ASN A 241      -8.256  14.406 -19.730  1.00 46.07           C
ANISOU 1831  CA  ASN A 241     8130   4791   4584   -111   -339    142       C
ATOM   1832  C   ASN A 241      -7.359  15.614 -19.887  1.00 45.26           C
ANISOU 1832  C   ASN A 241     8041   4668   4489   -100   -238    128       C
ATOM   1833  O   ASN A 241      -7.477  16.357 -20.865  1.00 47.20           O
ANISOU 1833  O   ASN A 241     8412   4845   4676    -98   -238    134       O
ATOM   1834  CB  ASN A 241      -8.261  13.580 -21.007  1.00 47.53           C
ANISOU 1834  CB  ASN A 241     8494   4888   4677   -122   -346    149       C
ATOM   1835  CG  ASN A 241      -6.850  13.181 -21.458  1.00 44.97           C
ANISOU 1835  CG  ASN A 241     8239   4515   4331   -117   -205    133       C
ATOM   1836  OD1 ASN A 241      -5.928  13.057 -20.641  1.00 43.35           O
ANISOU 1836  OD1 ASN A 241     7925   4358   4189   -108   -118    118       O
ATOM   1837  ND2 ASN A 241      -6.683  12.982 -22.774  1.00 42.75           N
ANISOU 1837  ND2 ASN A 241     8144   4139   3960   -122   -182    137       N
ATOM   1838  N   ASP A 242      -6.432  15.780 -18.954  1.00 45.51           N
ANISOU 1838  N   ASP A 242     7950   4753   4591    -94   -151    110       N
ATOM   1839  CA  ASP A 242      -5.447  16.847 -19.021  1.00 45.44           C
ANISOU 1839  CA  ASP A 242     7940   4728   4597    -89    -43     94       C
ATOM   1840  C   ASP A 242      -4.139  16.262 -19.555  1.00 45.28           C
ANISOU 1840  C   ASP A 242     7985   4661   4557    -90     81     80       C
ATOM   1841  O   ASP A 242      -3.463  15.499 -18.854  1.00 44.85           O
ANISOU 1841  O   ASP A 242     7839   4653   4550    -86    129     69       O
ATOM   1842  CB  ASP A 242      -5.263  17.489 -17.647  1.00 43.95           C
ANISOU 1842  CB  ASP A 242     7573   4628   4499    -86    -29     82       C
ATOM   1843  CG  ASP A 242      -4.252  18.629 -17.663  1.00 48.64           C
ANISOU 1843  CG  ASP A 242     8160   5209   5113    -87     80     62       C
ATOM   1844  OD1 ASP A 242      -3.816  19.045 -18.762  1.00 46.32           O
ANISOU 1844  OD1 ASP A 242     8004   4835   4762    -89    140     60       O
ATOM   1845  OD2 ASP A 242      -3.865  19.089 -16.568  1.00 50.62           O
ANISOU 1845  OD2 ASP A 242     8270   5527   5435    -87    110     48       O
ATOM   1846  N   THR A 243      -3.782  16.617 -20.794  1.00 44.78           N
ANISOU 1846  N   THR A 243     8083   4507   4423    -92    136     80       N
ATOM   1847  CA  THR A 243      -2.555  16.093 -21.397  1.00 45.98           C
ANISOU 1847  CA  THR A 243     8310   4607   4554    -91    262     67       C
ATOM   1848  C   THR A 243      -1.298  16.848 -20.975  1.00 45.59           C
ANISOU 1848  C   THR A 243     8181   4578   4564    -90    391     43       C
ATOM   1849  O   THR A 243      -0.197  16.455 -21.375  1.00 47.07           O
ANISOU 1849  O   THR A 243     8407   4729   4747    -88    506     31       O
ATOM   1850  CB  THR A 243      -2.643  16.028 -22.942  1.00 41.19           C
ANISOU 1850  CB  THR A 243     7921   3886   3842    -95    275     77       C
ATOM   1851  OG1 THR A 243      -2.460  17.328 -23.523  1.00 49.60           O
ANISOU 1851  OG1 THR A 243     9062   4902   4881    -97    320     72       O
ATOM   1852  CG2 THR A 243      -3.955  15.390 -23.403  1.00 36.65           C
ANISOU 1852  CG2 THR A 243     7429   3291   3207   -100    135     99       C
ATOM   1853  N  AASN A 244      -1.409  17.907 -20.183  0.47 47.64           N
ANISOU 1853  N  AASN A 244     8331   4892   4879    -94    380     36       N
ATOM   1854  CA AASN A 244      -0.182  18.531 -19.709  0.47 48.22           C
ANISOU 1854  CA AASN A 244     8319   4989   5013    -99    500     11       C
ATOM   1855  C  AASN A 244       0.431  17.787 -18.525  0.47 47.04           C
ANISOU 1855  C  AASN A 244     8002   4926   4944    -92    523     -1       C
ATOM   1856  O  AASN A 244       1.592  18.052 -18.187  0.47 45.78           O
ANISOU 1856  O  AASN A 244     7771   4786   4836    -95    628    -22       O
ATOM   1857  CB AASN A 244      -0.442  20.004 -19.370  0.47 47.32           C
ANISOU 1857  CB AASN A 244     8166   4892   4922   -107    490      5       C
ATOM   1858  CG AASN A 244      -0.544  20.866 -20.622  0.47 48.04           C
ANISOU 1858  CG AASN A 244     8431   4886   4937   -112    519     10       C
ATOM   1859  OD1AASN A 244       0.416  21.533 -21.023  0.47 48.27           O
ANISOU 1859  OD1AASN A 244     8501   4874   4966   -124    636     -8       O
ATOM   1860  ND2AASN A 244      -1.702  20.824 -21.269  0.47 47.40           N
ANISOU 1860  ND2AASN A 244     8456   4765   4788   -105    414     33       N
ATOM   1861  N  BASN A 244      -1.419  17.913 -20.187  0.53 49.11           N
ANISOU 1861  N  BASN A 244     8518   5078   5065    -94    379     36       N
ATOM   1862  CA BASN A 244      -0.208  18.544 -19.682  0.53 48.35           C
ANISOU 1862  CA BASN A 244     8332   5008   5030    -99    497     11       C
ATOM   1863  C  BASN A 244       0.457  17.718 -18.587  0.53 46.86           C
ANISOU 1863  C  BASN A 244     7987   4899   4918    -92    525     -1       C
ATOM   1864  O  BASN A 244       1.666  17.863 -18.366  0.53 45.86           O
ANISOU 1864  O  BASN A 244     7805   4785   4837    -94    637    -21       O
ATOM   1865  CB BASN A 244      -0.510  19.957 -19.182  0.53 47.29           C
ANISOU 1865  CB BASN A 244     8138   4902   4927   -107    478      5       C
ATOM   1866  CG BASN A 244       0.503  20.954 -19.674  0.53 47.39           C
ANISOU 1866  CG BASN A 244     8201   4867   4938   -120    604    -14       C
ATOM   1867  OD1BASN A 244       1.474  21.248 -18.982  0.53 46.86           O
ANISOU 1867  OD1BASN A 244     8022   4844   4940   -129    686    -37       O
ATOM   1868  ND2BASN A 244       0.314  21.445 -20.905  0.53 48.48           N
ANISOU 1868  ND2BASN A 244     8513   4911   4997   -122    621     -6       N
ATOM   1869  N   ARG A 245      -0.300  16.841 -17.924  1.00 46.26           N
ANISOU 1869  N   ARG A 245     7844   4876   4857    -83    428     13       N
ATOM   1870  CA  ARG A 245       0.222  16.041 -16.816  1.00 45.74           C
ANISOU 1870  CA  ARG A 245     7630   4888   4860    -73    443      4       C
ATOM   1871  C   ARG A 245       1.105  14.914 -17.336  1.00 43.17           C
ANISOU 1871  C   ARG A 245     7361   4526   4517    -61    523      2       C
ATOM   1872  O   ARG A 245       0.712  14.168 -18.241  1.00 42.37           O
ANISOU 1872  O   ARG A 245     7391   4361   4346    -58    500     16       O
ATOM   1873  CB  ARG A 245      -0.917  15.471 -15.968  1.00 41.82           C
ANISOU 1873  CB  ARG A 245     7055   4453   4381    -69    317     20       C
ATOM   1874  CG  ARG A 245      -1.541  16.521 -15.106  1.00 45.75           C
ANISOU 1874  CG  ARG A 245     7453   5008   4922    -76    258     18       C
ATOM   1875  CD  ARG A 245      -3.040  16.449 -15.130  1.00 49.67           C
ANISOU 1875  CD  ARG A 245     7974   5508   5390    -78    128     40       C
ATOM   1876  NE  ARG A 245      -3.618  17.454 -14.245  1.00 62.26           N
ANISOU 1876  NE  ARG A 245     9467   7158   7030    -80     79     39       N
ATOM   1877  CZ  ARG A 245      -4.089  17.207 -13.024  1.00 67.10           C
ANISOU 1877  CZ  ARG A 245     9947   7850   7699    -77     22     40       C
ATOM   1878  NH1 ARG A 245      -4.016  15.967 -12.514  1.00 56.86           N
ANISOU 1878  NH1 ARG A 245     8598   6587   6419    -71      7     43       N
ATOM   1879  NH2 ARG A 245      -4.592  18.213 -12.298  1.00 57.35           N
ANISOU 1879  NH2 ARG A 245     8633   6656   6501    -78    -13     39       N
ATOM   1880  N   PHE A 246       2.305  14.804 -16.766  1.00 44.39           N
ANISOU 1880  N   PHE A 246     7414   4719   4735    -52    617    -17       N
ATOM   1881  CA  PHE A 246       3.278  13.802 -17.186  1.00 44.24           C
ANISOU 1881  CA  PHE A 246     7431   4668   4710    -35    707    -20       C
ATOM   1882  C   PHE A 246       3.575  13.906 -18.678  1.00 44.10           C
ANISOU 1882  C   PHE A 246     7597   4542   4617    -40    780    -18       C
ATOM   1883  O   PHE A 246       3.534  12.924 -19.423  1.00 43.30           O
ANISOU 1883  O   PHE A 246     7608   4384   4460    -30    790     -7       O
ATOM   1884  CB  PHE A 246       2.791  12.415 -16.793  1.00 40.10           C
ANISOU 1884  CB  PHE A 246     6889   4170   4178    -18    639     -5       C
ATOM   1885  CG  PHE A 246       2.309  12.359 -15.395  1.00 38.62           C
ANISOU 1885  CG  PHE A 246     6542   4079   4052    -15    557     -4       C
ATOM   1886  CD1 PHE A 246       3.210  12.409 -14.339  1.00 39.62           C
ANISOU 1886  CD1 PHE A 246     6517   4279   4259     -3    605    -21       C
ATOM   1887  CD2 PHE A 246       0.959  12.305 -15.120  1.00 40.04           C
ANISOU 1887  CD2 PHE A 246     6724   4278   4211    -25    433     12       C
ATOM   1888  CE1 PHE A 246       2.769  12.366 -13.019  1.00 40.95           C
ANISOU 1888  CE1 PHE A 246     6545   4535   4480      0    530    -20       C
ATOM   1889  CE2 PHE A 246       0.509  12.247 -13.811  1.00 42.42           C
ANISOU 1889  CE2 PHE A 246     6882   4666   4568    -22    363     12       C
ATOM   1890  CZ  PHE A 246       1.418  12.284 -12.756  1.00 42.07           C
ANISOU 1890  CZ  PHE A 246     6695   4692   4599     -9    413     -4       C
ATOM   1891  N   LYS A 247       3.846  15.137 -19.105  1.00 46.64           N
ANISOU 1891  N   LYS A 247     7956   4832   4934    -58    832    -29       N
ATOM   1892  CA  LYS A 247       4.126  15.468 -20.497  1.00 49.32           C
ANISOU 1892  CA  LYS A 247     8473   5065   5202    -66    906    -29       C
ATOM   1893  C   LYS A 247       5.526  15.030 -20.918  1.00 52.52           C
ANISOU 1893  C   LYS A 247     8895   5436   5625    -56   1055    -43       C
ATOM   1894  O   LYS A 247       5.730  14.607 -22.065  1.00 47.45           O
ANISOU 1894  O   LYS A 247     8412   4704   4915    -52   1112    -37       O
ATOM   1895  CB  LYS A 247       3.966  16.978 -20.701  1.00 42.50           C
ANISOU 1895  CB  LYS A 247     7633   4183   4332    -88    915    -37       C
ATOM   1896  N   ALA A 248       6.510  15.181 -20.023  1.00 51.08           N
ANISOU 1896  N   ALA A 248     8551   5322   5533    -52   1123    -63       N
ATOM   1897  CA  ALA A 248       7.881  14.791 -20.345  1.00 51.32           C
ANISOU 1897  CA  ALA A 248     8576   5329   5594    -40   1266    -77       C
ATOM   1898  C   ALA A 248       8.007  13.281 -20.494  1.00 51.35           C
ANISOU 1898  C   ALA A 248     8611   5319   5578     -8   1270    -64       C
ATOM   1899  O   ALA A 248       8.522  12.788 -21.503  1.00 51.16           O
ANISOU 1899  O   ALA A 248     8715   5215   5509      2   1359    -61       O
ATOM   1900  CB  ALA A 248       8.843  15.313 -19.280  1.00 55.92           C
ANISOU 1900  CB  ALA A 248     8968   5997   6284    -44   1322   -101       C
ATOM   1901  N   GLN A 249       7.518  12.536 -19.499  1.00 54.67           N
ANISOU 1901  N   GLN A 249     8926   5817   6031      9   1175    -54       N
ATOM   1902  CA  GLN A 249       7.544  11.076 -19.478  1.00 49.37           C
ANISOU 1902  CA  GLN A 249     8273   5141   5344     39   1166    -41       C
ATOM   1903  C   GLN A 249       6.324  10.584 -18.717  1.00 42.10           C
ANISOU 1903  C   GLN A 249     7307   4275   4415     39   1016    -25       C
ATOM   1904  O   GLN A 249       6.015  11.103 -17.639  1.00 39.40           O
ANISOU 1904  O   GLN A 249     6826   4017   4130     32    952    -30       O
ATOM   1905  CB  GLN A 249       8.815  10.536 -18.802  1.00 47.34           C
ANISOU 1905  CB  GLN A 249     7881   4936   5169     70   1257    -53       C
ATOM   1906  CG  GLN A 249       9.034   9.024 -18.972  1.00 40.02           C
ANISOU 1906  CG  GLN A 249     6998   3987   4221    107   1277    -39       C
ATOM   1907  CD  GLN A 249      10.359   8.578 -18.368  1.00 41.20           C
ANISOU 1907  CD  GLN A 249     7014   4184   4455    142   1373    -51       C
ATOM   1908  OE1 GLN A 249      11.407   8.738 -18.986  1.00 37.44           O
ANISOU 1908  OE1 GLN A 249     6565   3665   3994    150   1503    -63       O
ATOM   1909  NE2 GLN A 249      10.316   8.012 -17.151  1.00 40.27           N
ANISOU 1909  NE2 GLN A 249     6752   4156   4393    165   1311    -49       N
ATOM   1910  N   ALA A 250       5.646   9.587 -19.285  1.00 43.62           N
ANISOU 1910  N   ALA A 250     7620   4419   4537     45    966     -6       N
ATOM   1911  CA  ALA A 250       4.442   9.035 -18.682  1.00 40.72           C
ANISOU 1911  CA  ALA A 250     7224   4093   4156     41    828     10       C
ATOM   1912  C   ALA A 250       4.765   8.443 -17.312  1.00 38.37           C
ANISOU 1912  C   ALA A 250     6751   3892   3938     65    811      7       C
ATOM   1913  O   ALA A 250       5.894   8.021 -17.042  1.00 38.96           O
ANISOU 1913  O   ALA A 250     6762   3984   4059     92    903     -2       O
ATOM   1914  CB  ALA A 250       3.842   7.972 -19.610  1.00 36.44           C
ANISOU 1914  CB  ALA A 250     6848   3473   3524     42    795     28       C
ATOM   1915  N  AARG A 251       3.768   8.437 -16.433  0.62 43.99           N
ANISOU 1915  N  AARG A 251     7383   4665   4665     55    692     15       N
ATOM   1916  CA AARG A 251       3.892   7.795 -15.120  0.62 40.32           C
ANISOU 1916  CA AARG A 251     6768   4287   4264     76    661     14       C
ATOM   1917  C  AARG A 251       3.352   6.376 -15.246  0.62 40.22           C
ANISOU 1917  C  AARG A 251     6825   4250   4206     88    614     32       C
ATOM   1918  O  AARG A 251       2.140   6.153 -15.181  0.62 41.42           O
ANISOU 1918  O  AARG A 251     7010   4404   4324     68    507     46       O
ATOM   1919  CB AARG A 251       3.142   8.593 -14.059  0.62 43.19           C
ANISOU 1919  CB AARG A 251     7009   4729   4672     58    568     12       C
ATOM   1920  CG AARG A 251       3.340   8.103 -12.635  0.62 41.89           C
ANISOU 1920  CG AARG A 251     6686   4655   4576     79    541      9       C
ATOM   1921  CD AARG A 251       2.626   9.029 -11.693  0.62 39.16           C
ANISOU 1921  CD AARG A 251     6235   4376   4268     59    461      5       C
ATOM   1922  NE AARG A 251       3.448   9.586 -10.616  0.62 41.34           N
ANISOU 1922  NE AARG A 251     6356   4727   4623     68    496    -13       N
ATOM   1923  CZ AARG A 251       4.651  10.151 -10.745  0.62 39.90           C
ANISOU 1923  CZ AARG A 251     6136   4546   4477     72    594    -32       C
ATOM   1924  NH1AARG A 251       5.263  10.601  -9.665  0.62 37.35           N
ANISOU 1924  NH1AARG A 251     5667   4297   4225     77    606    -48       N
ATOM   1925  NH2AARG A 251       5.251  10.284 -11.925  0.62 39.97           N
ANISOU 1925  NH2AARG A 251     6251   4482   4454     70    680    -35       N
ATOM   1926  N  BARG A 251       3.769   8.442 -16.433  0.38 42.54           N
ANISOU 1926  N  BARG A 251     7199   4481   4482     55    692     15       N
ATOM   1927  CA BARG A 251       3.895   7.789 -15.128  0.38 42.26           C
ANISOU 1927  CA BARG A 251     7015   4532   4510     76    661     14       C
ATOM   1928  C  BARG A 251       3.352   6.374 -15.266  0.38 40.92           C
ANISOU 1928  C  BARG A 251     6915   4337   4293     88    615     33       C
ATOM   1929  O  BARG A 251       2.138   6.155 -15.213  0.38 40.79           O
ANISOU 1929  O  BARG A 251     6933   4321   4242     67    507     46       O
ATOM   1930  CB BARG A 251       3.152   8.568 -14.049  0.38 42.65           C
ANISOU 1930  CB BARG A 251     6940   4661   4604     59    568     12       C
ATOM   1931  CG BARG A 251       3.776   8.426 -12.678  0.38 41.85           C
ANISOU 1931  CG BARG A 251     6664   4651   4585     80    578      2       C
ATOM   1932  CD BARG A 251       2.832   8.870 -11.612  0.38 41.67           C
ANISOU 1932  CD BARG A 251     6542   4699   4594     65    474      4       C
ATOM   1933  NE BARG A 251       3.480   9.763 -10.662  0.38 41.39           N
ANISOU 1933  NE BARG A 251     6363   4732   4631     65    500    -15       N
ATOM   1934  CZ BARG A 251       2.907  10.176  -9.541  0.38 41.23           C
ANISOU 1934  CZ BARG A 251     6234   4782   4649     56    427    -16       C
ATOM   1935  NH1BARG A 251       3.557  10.991  -8.725  0.38 44.71           N
ANISOU 1935  NH1BARG A 251     6556   5280   5152     54    455    -35       N
ATOM   1936  NH2BARG A 251       1.686   9.761  -9.240  0.38 41.10           N
ANISOU 1936  NH2BARG A 251     6230   4776   4609     49    328      1       N
ATOM   1937  N   ASN A 252       4.251   5.406 -15.470  1.00 42.03           N
ANISOU 1937  N   ASN A 252     7081   4454   4434    120    698     33       N
ATOM   1938  CA  ASN A 252       3.870   4.003 -15.628  1.00 34.88           C
ANISOU 1938  CA  ASN A 252     6252   3518   3482    134    669     49       C
ATOM   1939  C   ASN A 252       4.169   3.293 -14.306  1.00 34.37           C
ANISOU 1939  C   ASN A 252     6043   3535   3482    165    654     50       C
ATOM   1940  O   ASN A 252       5.331   3.017 -13.988  1.00 35.43           O
ANISOU 1940  O   ASN A 252     6110   3691   3663    203    742     43       O
ATOM   1941  CB  ASN A 252       4.584   3.357 -16.818  1.00 34.52           C
ANISOU 1941  CB  ASN A 252     6353   3379   3383    151    771     51       C
ATOM   1942  CG  ASN A 252       4.092   1.883 -17.104  1.00 36.91           C
ANISOU 1942  CG  ASN A 252     6762   3638   3625    159    738     68       C
ATOM   1943  OD1 ASN A 252       2.959   1.536 -16.786  1.00 36.09           O
ANISOU 1943  OD1 ASN A 252     6665   3550   3498    136    627     79       O
ATOM   1944  ND2 ASN A 252       4.942   1.053 -17.732  1.00 31.14           N
ANISOU 1944  ND2 ASN A 252     6116   2847   2869    191    839     71       N
ATOM   1945  N   ILE A 253       3.112   3.003 -13.534  1.00 32.69           N
ANISOU 1945  N   ILE A 253     5782   3367   3270    150    543     59       N
ATOM   1946  CA  ILE A 253       3.199   2.245 -12.288  1.00 33.08           C
ANISOU 1946  CA  ILE A 253     5715   3486   3366    177    515     63       C
ATOM   1947  C   ILE A 253       2.329   0.986 -12.354  1.00 32.14           C
ANISOU 1947  C   ILE A 253     5678   3340   3195    172    452     80       C
ATOM   1948  O   ILE A 253       2.046   0.358 -11.336  1.00 32.65           O
ANISOU 1948  O   ILE A 253     5664   3456   3286    184    405     86       O
ATOM   1949  CB  ILE A 253       2.860   3.115 -11.055  1.00 31.67           C
ANISOU 1949  CB  ILE A 253     5379   3400   3253    165    452     55       C
ATOM   1950  CG1 ILE A 253       1.363   3.422 -10.955  1.00 32.50           C
ANISOU 1950  CG1 ILE A 253     5505   3512   3331    124    335     64       C
ATOM   1951  CG2 ILE A 253       3.596   4.472 -11.085  1.00 32.24           C
ANISOU 1951  CG2 ILE A 253     5387   3494   3371    159    508     36       C
ATOM   1952  CD1 ILE A 253       1.033   4.280  -9.759  1.00 30.36           C
ANISOU 1952  CD1 ILE A 253     5088   3326   3122    115    280     57       C
ATOM   1953  N   SER A 254       1.934   0.601 -13.563  1.00 31.97           N
ANISOU 1953  N   SER A 254     5820   3231   3096    153    454     88       N
ATOM   1954  CA  SER A 254       1.256  -0.664 -13.787  1.00 30.19           C
ANISOU 1954  CA  SER A 254     5691   2965   2814    146    409    103       C
ATOM   1955  C   SER A 254       2.181  -1.817 -13.464  1.00 32.28           C
ANISOU 1955  C   SER A 254     5947   3228   3092    196    484    106       C
ATOM   1956  O   SER A 254       3.295  -1.907 -13.990  1.00 33.54           O
ANISOU 1956  O   SER A 254     6139   3352   3252    229    592    102       O
ATOM   1957  CB  SER A 254       0.830  -0.767 -15.245  1.00 33.65           C
ANISOU 1957  CB  SER A 254     6316   3305   3165    117    408    108       C
ATOM   1958  OG  SER A 254       0.298  -2.049 -15.535  1.00 37.03           O
ANISOU 1958  OG  SER A 254     6849   3686   3535    109    377    120       O
ATOM   1959  N   MET A 255       1.703  -2.734 -12.645  1.00 33.04           N
ANISOU 1959  N   MET A 255     6006   3355   3192    202    430    116       N
ATOM   1960  CA  MET A 255       2.553  -3.795 -12.151  1.00 32.99           C
ANISOU 1960  CA  MET A 255     5974   3357   3204    256    494    120       C
ATOM   1961  C   MET A 255       2.203  -5.127 -12.795  1.00 32.94           C
ANISOU 1961  C   MET A 255     6118   3273   3122    254    495    133       C
ATOM   1962  O   MET A 255       1.053  -5.380 -13.183  1.00 31.47           O
ANISOU 1962  O   MET A 255     6020   3054   2883    205    415    140       O
ATOM   1963  CB  MET A 255       2.449  -3.924 -10.638  1.00 29.94           C
ANISOU 1963  CB  MET A 255     5433   3063   2881    273    445    121       C
ATOM   1964  CG  MET A 255       2.346  -2.657  -9.853  1.00 28.04           C
ANISOU 1964  CG  MET A 255     5049   2901   2704    259    406    110       C
ATOM   1965  SD  MET A 255       2.738  -3.162  -8.151  1.00 27.67           S
ANISOU 1965  SD  MET A 255     4843   2947   2725    303    391    111       S
ATOM   1966  CE  MET A 255       1.334  -4.207  -7.763  1.00 30.92           C
ANISOU 1966  CE  MET A 255     5309   3348   3091    273    293    127       C
ATOM   1967  N   ASN A 256       3.225  -5.969 -12.891  1.00 32.67           N
ANISOU 1967  N   ASN A 256     6111   3212   3088    307    589    137       N
ATOM   1968  CA  ASN A 256       3.094  -7.354 -13.310  1.00 37.66           C
ANISOU 1968  CA  ASN A 256     6874   3777   3657    318    607    150       C
ATOM   1969  C   ASN A 256       2.977  -8.229 -12.060  1.00 34.46           C
ANISOU 1969  C   ASN A 256     6384   3427   3283    346    573    158       C
ATOM   1970  O   ASN A 256       3.915  -8.297 -11.260  1.00 35.25           O
ANISOU 1970  O   ASN A 256     6371   3579   3443    402    623    157       O
ATOM   1971  CB  ASN A 256       4.314  -7.755 -14.147  1.00 35.17           C
ANISOU 1971  CB  ASN A 256     6642   3397   3325    367    738    150       C
ATOM   1972  CG  ASN A 256       4.256  -9.195 -14.607  1.00 44.66           C
ANISOU 1972  CG  ASN A 256     7988   4522   4458    382    767    163       C
ATOM   1973  OD1 ASN A 256       3.252  -9.870 -14.433  1.00 47.55           O
ANISOU 1973  OD1 ASN A 256     8408   4876   4783    348    686    171       O
ATOM   1974  ND2 ASN A 256       5.386  -9.698 -15.056  1.00 49.57           N
ANISOU 1974  ND2 ASN A 256     8657   5099   5078    439    885    166       N
ATOM   1975  N   ILE A 257       1.870  -8.934 -11.912  1.00 35.34           N
ANISOU 1975  N   ILE A 257     6555   3523   3352    308    491    167       N
ATOM   1976  CA  ILE A 257       1.731  -9.691 -10.681  1.00 42.55           C
ANISOU 1976  CA  ILE A 257     7386   4488   4294    332    460    174       C
ATOM   1977  C   ILE A 257       1.901 -11.205 -10.869  1.00 47.47           C
ANISOU 1977  C   ILE A 257     8124   5049   4864    360    501    187       C
ATOM   1978  O   ILE A 257       1.199 -11.988 -10.229  1.00 48.59           O
ANISOU 1978  O   ILE A 257     8269   5199   4992    346    445    195       O
ATOM   1979  CB  ILE A 257       0.396  -9.433 -10.013  1.00 41.17           C
ANISOU 1979  CB  ILE A 257     7159   4359   4127    274    341    175       C
ATOM   1980  CG1 ILE A 257      -0.762  -9.494 -11.003  1.00 39.85           C
ANISOU 1980  CG1 ILE A 257     7123   4128   3889    204    276    176       C
ATOM   1981  CG2 ILE A 257       0.410  -8.069  -9.349  1.00 35.91           C
ANISOU 1981  CG2 ILE A 257     6339   3776   3531    267    308    164       C
ATOM   1982  CD1 ILE A 257      -2.095  -9.485 -10.314  1.00 32.51           C
ANISOU 1982  CD1 ILE A 257     6145   3238   2968    151    163    178       C
ATOM   1983  N   GLN A 258       2.781 -11.667 -11.770  1.00 57.42           N
ANISOU 1983  N   GLN A 258     9487   6238   6091    397    600    190       N
ATOM   1984  CA  GLN A 258       2.871 -13.118 -11.978  1.00 61.25           C
ANISOU 1984  CA  GLN A 258    10094   6657   6520    422    639    203       C
ATOM   1985  C   GLN A 258       3.556 -13.827 -10.805  1.00 56.27           C
ANISOU 1985  C   GLN A 258     9366   6077   5937    493    670    212       C
ATOM   1986  O   GLN A 258       3.161 -14.938 -10.415  1.00 53.64           O
ANISOU 1986  O   GLN A 258     9087   5723   5570    498    651    223       O
ATOM   1987  CB  GLN A 258       3.662 -13.426 -13.227  1.00 61.35           C
ANISOU 1987  CB  GLN A 258    10245   6579   6485    448    744    204       C
ATOM   1988  CG  GLN A 258       3.306 -12.709 -14.438  1.00 67.78           C
ANISOU 1988  CG  GLN A 258    11161   7338   7254    396    737    195       C
ATOM   1989  CD  GLN A 258       3.667 -13.536 -15.636  1.00 77.43           C
ANISOU 1989  CD  GLN A 258    12575   8448   8397    407    819    200       C
ATOM   1990  OE1 GLN A 258       3.714 -14.780 -15.535  1.00 82.04           O
ANISOU 1990  OE1 GLN A 258    13237   8991   8944    431    844    211       O
ATOM   1991  NE2 GLN A 258       4.057 -12.902 -16.716  1.00 72.79           N
ANISOU 1991  NE2 GLN A 258    12064   7809   7785    399    875    193       N
ATOM   1992  N   LYS A 259       4.591 -13.208 -10.256  1.00 43.84           N
ANISOU 1992  N   LYS A 259     7654   4566   4437    548    719    207       N
ATOM   1993  CA  LYS A 259       5.346 -13.811  -9.165  1.00 43.61           C
ANISOU 1993  CA  LYS A 259     7528   4587   4456    622    749    216       C
ATOM   1994  C   LYS A 259       4.384 -14.195  -8.056  1.00 44.50           C
ANISOU 1994  C   LYS A 259     7591   4746   4570    597    652    221       C
ATOM   1995  O   LYS A 259       4.351 -15.347  -7.611  1.00 44.69           O
ANISOU 1995  O   LYS A 259     7660   4751   4569    628    659    234       O
ATOM   1996  CB  LYS A 259       6.402 -12.837  -8.701  1.00 37.44           C
ANISOU 1996  CB  LYS A 259     6587   3879   3759    666    790    206       C
ATOM   1997  CG  LYS A 259       7.394 -13.333  -7.704  1.00 40.40           C
ANISOU 1997  CG  LYS A 259     6856   4306   4189    751    830    214       C
ATOM   1998  CD  LYS A 259       8.554 -12.335  -7.601  1.00 36.19           C
ANISOU 1998  CD  LYS A 259     6189   3828   3735    788    887    201       C
ATOM   1999  CE  LYS A 259       9.314 -12.563  -6.295  1.00 37.03           C
ANISOU 1999  CE  LYS A 259     6148   4015   3908    858    885    206       C
ATOM   2000  NZ  LYS A 259      10.495 -11.683  -6.039  1.00 31.64           N
ANISOU 2000  NZ  LYS A 259     5318   3394   3308    897    934    194       N
ATOM   2001  N   ILE A 260       3.465 -13.289  -7.740  1.00 42.78           N
ANISOU 2001  N   ILE A 260     7307   4575   4370    533    563    212       N
ATOM   2002  CA  ILE A 260       2.528 -13.509  -6.660  1.00 43.84           C
ANISOU 2002  CA  ILE A 260     7385   4759   4515    505    474    215       C
ATOM   2003  C   ILE A 260       1.494 -14.543  -7.058  1.00 42.53           C
ANISOU 2003  C   ILE A 260     7362   4524   4274    458    436    224       C
ATOM   2004  O   ILE A 260       1.034 -15.319  -6.214  1.00 40.73           O
ANISOU 2004  O   ILE A 260     7127   4310   4040    459    401    232       O
ATOM   2005  CB  ILE A 260       1.904 -12.139  -6.288  1.00 39.99           C
ANISOU 2005  CB  ILE A 260     6783   4338   4072    453    399    202       C
ATOM   2006  CG1 ILE A 260       1.055 -12.224  -5.064  1.00 38.56           C
ANISOU 2006  CG1 ILE A 260     6520   4216   3913    431    316    205       C
ATOM   2007  CG2 ILE A 260       1.145 -11.486  -7.408  1.00 42.59           C
ANISOU 2007  CG2 ILE A 260     7195   4625   4365    384    365    195       C
ATOM   2008  CD1 ILE A 260       1.827 -12.541  -3.905  1.00 42.72           C
ANISOU 2008  CD1 ILE A 260     6947   4800   4485    498    339    210       C
ATOM   2009  N   GLU A 261       1.203 -14.663  -8.351  1.00 44.98           N
ANISOU 2009  N   GLU A 261     7814   4753   4522    419    450    222       N
ATOM   2010  CA  GLU A 261       0.239 -15.668  -8.788  1.00 46.33           C
ANISOU 2010  CA  GLU A 261     8129   4855   4619    369    413    228       C
ATOM   2011  C   GLU A 261       0.798 -17.092  -8.718  1.00 42.89           C
ANISOU 2011  C   GLU A 261     7785   4365   4145    424    481    242       C
ATOM   2012  O   GLU A 261       0.053 -18.008  -8.369  1.00 39.62           O
ANISOU 2012  O   GLU A 261     7430   3929   3696    396    442    248       O
ATOM   2013  CB  GLU A 261      -0.253 -15.307 -10.188  1.00 47.85           C
ANISOU 2013  CB  GLU A 261     8448   4978   4755    309    399    221       C
ATOM   2014  CG  GLU A 261      -1.321 -14.211 -10.145  1.00 48.92           C
ANISOU 2014  CG  GLU A 261     8518   5159   4912    236    298    212       C
ATOM   2015  CD  GLU A 261      -1.421 -13.408 -11.437  1.00 53.31           C
ANISOU 2015  CD  GLU A 261     9153   5668   5435    200    298    203       C
ATOM   2016  OE1 GLU A 261      -2.429 -12.677 -11.625  1.00 55.55           O
ANISOU 2016  OE1 GLU A 261     9420   5968   5717    136    210    198       O
ATOM   2017  OE2 GLU A 261      -0.492 -13.507 -12.265  1.00 54.80           O
ANISOU 2017  OE2 GLU A 261     9421   5803   5599    238    388    203       O
ATOM   2018  N   LYS A 262       2.104 -17.295  -8.985  1.00 45.74           N
ANISOU 2018  N   LYS A 262     8154   4707   4517    502    585    246       N
ATOM   2019  CA  LYS A 262       2.684 -18.647  -8.937  1.00 46.00           C
ANISOU 2019  CA  LYS A 262     8277   4686   4514    563    656    261       C
ATOM   2020  C   LYS A 262       2.576 -19.252  -7.550  1.00 43.95           C
ANISOU 2020  C   LYS A 262     7935   4480   4283    595    625    270       C
ATOM   2021  O   LYS A 262       2.478 -20.479  -7.421  1.00 41.18           O
ANISOU 2021  O   LYS A 262     7681   4079   3885    614    646    283       O
ATOM   2022  CB  LYS A 262       4.160 -18.654  -9.359  1.00 43.25           C
ANISOU 2022  CB  LYS A 262     7926   4320   4189    649    774    264       C
ATOM   2023  CG  LYS A 262       4.453 -18.332 -10.815  1.00 52.06           C
ANISOU 2023  CG  LYS A 262     9157   5361   5264    632    834    258       C
ATOM   2024  CD  LYS A 262       5.966 -18.185 -11.047  1.00 54.38           C
ANISOU 2024  CD  LYS A 262     9408   5654   5599    720    953    260       C
ATOM   2025  CE  LYS A 262       6.497 -16.953 -10.315  1.00 52.51           C
ANISOU 2025  CE  LYS A 262     8971   5521   5458    740    938    250       C
ATOM   2026  NZ  LYS A 262       7.970 -16.691 -10.392  1.00 47.68           N
ANISOU 2026  NZ  LYS A 262     8285   4928   4905    822   1045    249       N
ATOM   2027  N   HIS A 263       2.584 -18.415  -6.510  1.00 41.18           N
ANISOU 2027  N   HIS A 263     7415   4228   4005    602    577    265       N
ATOM   2028  CA  HIS A 263       2.378 -18.870  -5.144  1.00 40.10           C
ANISOU 2028  CA  HIS A 263     7198   4145   3894    626    538    273       C
ATOM   2029  C   HIS A 263       0.908 -18.929  -4.782  1.00 40.53           C
ANISOU 2029  C   HIS A 263     7267   4206   3926    539    440    270       C
ATOM   2030  O   HIS A 263       0.580 -19.069  -3.595  1.00 39.28           O
ANISOU 2030  O   HIS A 263     7028   4102   3796    545    397    274       O
ATOM   2031  CB  HIS A 263       3.088 -17.973  -4.149  1.00 39.77           C
ANISOU 2031  CB  HIS A 263     6971   4203   3936    674    532    269       C
ATOM   2032  CG  HIS A 263       4.573 -17.969  -4.296  1.00 40.88           C
ANISOU 2032  CG  HIS A 263     7072   4350   4111    765    624    273       C
ATOM   2033  ND1 HIS A 263       5.224 -17.208  -5.248  1.00 42.00           N
ANISOU 2033  ND1 HIS A 263     7212   4478   4270    769    678    263       N
ATOM   2034  CD2 HIS A 263       5.538 -18.612  -3.598  1.00 35.06           C
ANISOU 2034  CD2 HIS A 263     6291   3632   3398    857    673    285       C
ATOM   2035  CE1 HIS A 263       6.528 -17.384  -5.132  1.00 41.76           C
ANISOU 2035  CE1 HIS A 263     7132   4458   4275    856    758    268       C
ATOM   2036  NE2 HIS A 263       6.744 -18.230  -4.138  1.00 42.63           N
ANISOU 2036  NE2 HIS A 263     7215   4592   4392    913    754    282       N
ATOM   2037  N   GLY A 264       0.020 -18.750  -5.761  1.00 38.09           N
ANISOU 2037  N   GLY A 264     7052   3847   3572    458    402    262       N
ATOM   2038  CA  GLY A 264      -1.394 -18.920  -5.518  1.00 40.02           C
ANISOU 2038  CA  GLY A 264     7320   4091   3795    374    313    260       C
ATOM   2039  C   GLY A 264      -2.100 -17.702  -4.991  1.00 41.77           C
ANISOU 2039  C   GLY A 264     7407   4391   4071    325    231    249       C
ATOM   2040  O   GLY A 264      -3.230 -17.811  -4.511  1.00 41.38           O
ANISOU 2040  O   GLY A 264     7344   4358   4021    265    158    248       O
ATOM   2041  N   ILE A 265      -1.460 -16.555  -5.013  1.00 39.05           N
ANISOU 2041  N   ILE A 265     6960   4098   3779    351    245    241       N
ATOM   2042  CA  ILE A 265      -2.106 -15.336  -4.593  1.00 36.54           C
ANISOU 2042  CA  ILE A 265     6522   3849   3511    306    173    231       C
ATOM   2043  C   ILE A 265      -2.598 -14.613  -5.841  1.00 41.00           C
ANISOU 2043  C   ILE A 265     7152   4377   4051    247    147    222       C
ATOM   2044  O   ILE A 265      -1.808 -14.205  -6.706  1.00 41.76           O
ANISOU 2044  O   ILE A 265     7282   4445   4139    272    204    218       O
ATOM   2045  CB  ILE A 265      -1.169 -14.474  -3.739  1.00 37.26           C
ANISOU 2045  CB  ILE A 265     6458   4023   3676    366    196    227       C
ATOM   2046  CG1 ILE A 265      -0.787 -15.273  -2.480  1.00 37.31           C
ANISOU 2046  CG1 ILE A 265     6413   4062   3700    423    211    237       C
ATOM   2047  CG2 ILE A 265      -1.879 -13.162  -3.369  1.00 35.45           C
ANISOU 2047  CG2 ILE A 265     6116   3859   3494    316    124    215       C
ATOM   2048  CD1 ILE A 265       0.452 -14.794  -1.700  1.00 36.71           C
ANISOU 2048  CD1 ILE A 265     6209   4054   3686    502    252    236       C
ATOM   2049  N   HIS A 266      -3.912 -14.464  -5.931  1.00 38.35           N
ANISOU 2049  N   HIS A 266     6832   4040   3701    169     62    219       N
ATOM   2050  CA  HIS A 266      -4.577 -13.874  -7.077  1.00 39.91           C
ANISOU 2050  CA  HIS A 266     7098   4199   3868    107     20    212       C
ATOM   2051  C   HIS A 266      -5.207 -12.535  -6.689  1.00 38.45           C
ANISOU 2051  C   HIS A 266     6786   4084   3737     72    -50    204       C
ATOM   2052  O   HIS A 266      -5.659 -12.352  -5.551  1.00 34.53           O
ANISOU 2052  O   HIS A 266     6179   3653   3288     67    -92    204       O
ATOM   2053  CB  HIS A 266      -5.654 -14.826  -7.608  1.00 37.50           C
ANISOU 2053  CB  HIS A 266     6923   3829   3498     40    -29    215       C
ATOM   2054  CG  HIS A 266      -6.426 -14.263  -8.756  1.00 50.49           C
ANISOU 2054  CG  HIS A 266     8640   5436   5108    -27    -86    208       C
ATOM   2055  ND1 HIS A 266      -7.503 -13.416  -8.583  1.00 52.07           N
ANISOU 2055  ND1 HIS A 266     8764   5680   5339    -84   -179    203       N
ATOM   2056  CD2 HIS A 266      -6.300 -14.443 -10.095  1.00 56.48           C
ANISOU 2056  CD2 HIS A 266     9545   6114   5802    -44    -66    207       C
ATOM   2057  CE1 HIS A 266      -7.994 -13.083  -9.766  1.00 51.01           C
ANISOU 2057  CE1 HIS A 266     8723   5498   5162   -131   -218    199       C
ATOM   2058  NE2 HIS A 266      -7.288 -13.697 -10.700  1.00 54.02           N
ANISOU 2058  NE2 HIS A 266     9243   5802   5481   -110   -151    201       N
ATOM   2059  N   PHE A 267      -5.196 -11.588  -7.631  1.00 39.45           N
ANISOU 2059  N   PHE A 267     6936   4196   3858     52    -58    197       N
ATOM   2060  CA  PHE A 267      -5.914 -10.322  -7.537  1.00 36.83           C
ANISOU 2060  CA  PHE A 267     6515   3913   3564     13   -128    190       C
ATOM   2061  C   PHE A 267      -6.729 -10.178  -8.814  1.00 38.88           C
ANISOU 2061  C   PHE A 267     6893   4112   3769    -48   -179    188       C
ATOM   2062  O   PHE A 267      -6.273 -10.564  -9.891  1.00 43.02           O
ANISOU 2062  O   PHE A 267     7546   4563   4236    -42   -134    189       O
ATOM   2063  CB  PHE A 267      -4.950  -9.092  -7.405  1.00 32.16           C
ANISOU 2063  CB  PHE A 267     5826   3370   3025     57    -82    182       C
ATOM   2064  CG  PHE A 267      -4.552  -8.752  -5.979  1.00 31.77           C
ANISOU 2064  CG  PHE A 267     5619   3405   3046     97    -75    180       C
ATOM   2065  CD1 PHE A 267      -5.364  -7.960  -5.174  1.00 30.89           C
ANISOU 2065  CD1 PHE A 267     5397   3358   2981     67   -144    177       C
ATOM   2066  CD2 PHE A 267      -3.354  -9.233  -5.445  1.00 32.27           C
ANISOU 2066  CD2 PHE A 267     5650   3483   3127    165      2    182       C
ATOM   2067  CE1 PHE A 267      -5.016  -7.665  -3.868  1.00 26.92           C
ANISOU 2067  CE1 PHE A 267     4762   2929   2537    100   -138    175       C
ATOM   2068  CE2 PHE A 267      -2.983  -8.931  -4.134  1.00 29.30           C
ANISOU 2068  CE2 PHE A 267     5137   3185   2812    200      2    180       C
ATOM   2069  CZ  PHE A 267      -3.828  -8.149  -3.343  1.00 31.18           C
ANISOU 2069  CZ  PHE A 267     5273   3483   3091    166    -68    176       C
ATOM   2070  N   SER A 268      -7.914  -9.595  -8.705  1.00 38.87           N
ANISOU 2070  N   SER A 268     6845   4139   3785   -104   -272    187       N
ATOM   2071  CA  SER A 268      -8.703  -9.215  -9.871  1.00 36.76           C
ANISOU 2071  CA  SER A 268     6669   3825   3475   -159   -333    185       C
ATOM   2072  C   SER A 268      -8.083  -8.006 -10.602  1.00 38.69           C
ANISOU 2072  C   SER A 268     6914   4065   3723   -138   -303    179       C
ATOM   2073  O   SER A 268      -7.371  -7.172 -10.010  1.00 33.09           O
ANISOU 2073  O   SER A 268     6094   3410   3068    -96   -262    175       O
ATOM   2074  CB  SER A 268     -10.121  -8.869  -9.412  1.00 35.90           C
ANISOU 2074  CB  SER A 268     6487   3759   3396   -218   -440    186       C
ATOM   2075  OG  SER A 268     -10.681  -9.965  -8.714  1.00 43.16           O
ANISOU 2075  OG  SER A 268     7404   4681   4314   -240   -461    190       O
ATOM   2076  N   ASN A 269      -8.440  -7.845 -11.880  1.00 32.11           N
ANISOU 2076  N   ASN A 269     6203   3167   2830   -172   -331    178       N
ATOM   2077  CA  ASN A 269      -7.996  -6.622 -12.534  1.00 36.05           C
ANISOU 2077  CA  ASN A 269     6701   3662   3332   -158   -310    173       C
ATOM   2078  C   ASN A 269      -8.762  -5.425 -11.958  1.00 36.64           C
ANISOU 2078  C   ASN A 269     6646   3808   3467   -177   -384    172       C
ATOM   2079  O   ASN A 269      -9.684  -5.584 -11.146  1.00 32.91           O
ANISOU 2079  O   ASN A 269     6093   3382   3028   -205   -453    175       O
ATOM   2080  CB  ASN A 269      -8.117  -6.724 -14.064  1.00 32.13           C
ANISOU 2080  CB  ASN A 269     6381   3075   2753   -185   -316    173       C
ATOM   2081  CG  ASN A 269      -9.553  -6.643 -14.573  1.00 31.95           C
ANISOU 2081  CG  ASN A 269     6406   3035   2700   -254   -438    177       C
ATOM   2082  OD1 ASN A 269     -10.378  -5.891 -14.069  1.00 32.70           O
ANISOU 2082  OD1 ASN A 269     6396   3188   2842   -276   -514    177       O
ATOM   2083  ND2 ASN A 269      -9.833  -7.390 -15.628  1.00 33.28           N
ANISOU 2083  ND2 ASN A 269     6738   3121   2787   -287   -455    178       N
ATOM   2084  N   THR A 270      -8.323  -4.210 -12.335  1.00 32.12           N
ANISOU 2084  N   THR A 270     6051   3243   2909   -160   -361    167       N
ATOM   2085  CA  THR A 270      -8.856  -2.988 -11.716  1.00 34.97           C
ANISOU 2085  CA  THR A 270     6283   3673   3331   -167   -414    165       C
ATOM   2086  C   THR A 270     -10.361  -2.833 -11.936  1.00 33.10           C
ANISOU 2086  C   THR A 270     6055   3438   3085   -223   -533    171       C
ATOM   2087  O   THR A 270     -11.121  -2.713 -10.968  1.00 37.91           O
ANISOU 2087  O   THR A 270     6550   4107   3746   -238   -589    173       O
ATOM   2088  CB  THR A 270      -8.093  -1.768 -12.238  1.00 35.37           C
ANISOU 2088  CB  THR A 270     6333   3717   3388   -141   -363    158       C
ATOM   2089  OG1 THR A 270      -6.799  -1.759 -11.630  1.00 34.01           O
ANISOU 2089  OG1 THR A 270     6095   3574   3254    -90   -263    151       O
ATOM   2090  CG2 THR A 270      -8.833  -0.451 -11.933  1.00 32.03           C
ANISOU 2090  CG2 THR A 270     5817   3344   3008   -157   -429    157       C
ATOM   2091  N   VAL A 271     -10.820  -2.901 -13.187  1.00 31.26           N
ANISOU 2091  N   VAL A 271     5956   3137   2786   -256   -575    174       N
ATOM   2092  CA  VAL A 271     -12.239  -2.680 -13.472  1.00 35.44           C
ANISOU 2092  CA  VAL A 271     6489   3668   3307   -308   -695    180       C
ATOM   2093  C   VAL A 271     -13.099  -3.818 -12.924  1.00 39.69           C
ANISOU 2093  C   VAL A 271     7012   4217   3850   -346   -750    184       C
ATOM   2094  O   VAL A 271     -14.119  -3.570 -12.266  1.00 38.56           O
ANISOU 2094  O   VAL A 271     6769   4126   3755   -373   -826    187       O
ATOM   2095  CB  VAL A 271     -12.476  -2.494 -14.974  1.00 37.58           C
ANISOU 2095  CB  VAL A 271     6918   3861   3501   -332   -729    182       C
ATOM   2096  CG1 VAL A 271     -13.970  -2.455 -15.215  1.00 39.06           C
ANISOU 2096  CG1 VAL A 271     7106   4052   3682   -387   -861    188       C
ATOM   2097  CG2 VAL A 271     -11.800  -1.221 -15.469  1.00 37.86           C
ANISOU 2097  CG2 VAL A 271     6960   3888   3536   -299   -683    178       C
ATOM   2098  N   ASP A 272     -12.717  -5.080 -13.199  1.00 34.94           N
ANISOU 2098  N   ASP A 272     6512   3564   3199   -351   -710    183       N
ATOM   2099  CA  ASP A 272     -13.457  -6.219 -12.635  1.00 37.91           C
ANISOU 2099  CA  ASP A 272     6878   3948   3579   -388   -751    186       C
ATOM   2100  C   ASP A 272     -13.481  -6.143 -11.110  1.00 41.37           C
ANISOU 2100  C   ASP A 272     7152   4469   4098   -367   -737    186       C
ATOM   2101  O   ASP A 272     -14.505  -6.442 -10.478  1.00 41.41           O
ANISOU 2101  O   ASP A 272     7093   4508   4135   -406   -803    189       O
ATOM   2102  CB  ASP A 272     -12.825  -7.559 -13.030  1.00 31.71           C
ANISOU 2102  CB  ASP A 272     6223   3096   2731   -384   -689    185       C
ATOM   2103  CG  ASP A 272     -12.969  -7.894 -14.501  1.00 37.91           C
ANISOU 2103  CG  ASP A 272     7188   3790   3426   -416   -711    185       C
ATOM   2104  OD1 ASP A 272     -13.628  -7.159 -15.277  1.00 42.55           O
ANISOU 2104  OD1 ASP A 272     7810   4363   3994   -446   -785    185       O
ATOM   2105  OD2 ASP A 272     -12.385  -8.925 -14.894  1.00 43.93           O
ANISOU 2105  OD2 ASP A 272     8066   4491   4133   -408   -651    184       O
ATOM   2106  N   GLY A 273     -12.344  -5.760 -10.507  1.00 39.87           N
ANISOU 2106  N   GLY A 273     6896   4311   3942   -307   -649    183       N
ATOM   2107  CA  GLY A 273     -12.243  -5.707  -9.055  1.00 38.64           C
ANISOU 2107  CA  GLY A 273     6595   4230   3856   -282   -630    183       C
ATOM   2108  C   GLY A 273     -13.152  -4.668  -8.437  1.00 41.29           C
ANISOU 2108  C   GLY A 273     6803   4630   4253   -301   -699    184       C
ATOM   2109  O   GLY A 273     -13.702  -4.882  -7.354  1.00 44.35           O
ANISOU 2109  O   GLY A 273     7094   5068   4688   -310   -723    186       O
ATOM   2110  N   PHE A 274     -13.273  -3.506  -9.078  1.00 40.31           N
ANISOU 2110  N   PHE A 274     6679   4505   4131   -301   -725    183       N
ATOM   2111  CA  PHE A 274     -14.262  -2.537  -8.621  1.00 43.06           C
ANISOU 2111  CA  PHE A 274     6921   4908   4533   -320   -798    185       C
ATOM   2112  C   PHE A 274     -15.665  -3.127  -8.717  1.00 45.54           C
ANISOU 2112  C   PHE A 274     7246   5215   4843   -380   -894    192       C
ATOM   2113  O   PHE A 274     -16.420  -3.106  -7.740  1.00 47.08           O
ANISOU 2113  O   PHE A 274     7332   5462   5093   -395   -929    194       O
ATOM   2114  CB  PHE A 274     -14.159  -1.231  -9.415  1.00 41.87           C
ANISOU 2114  CB  PHE A 274     6787   4746   4375   -309   -810    184       C
ATOM   2115  CG  PHE A 274     -15.101  -0.145  -8.935  1.00 40.81           C
ANISOU 2115  CG  PHE A 274     6542   4666   4298   -319   -877    188       C
ATOM   2116  CD1 PHE A 274     -14.710   0.743  -7.947  1.00 41.89           C
ANISOU 2116  CD1 PHE A 274     6556   4864   4495   -285   -840    184       C
ATOM   2117  CD2 PHE A 274     -16.365  -0.027  -9.455  1.00 42.98           C
ANISOU 2117  CD2 PHE A 274     6835   4931   4566   -363   -978    196       C
ATOM   2118  CE1 PHE A 274     -15.552   1.726  -7.503  1.00 43.10           C
ANISOU 2118  CE1 PHE A 274     6614   5063   4700   -291   -894    188       C
ATOM   2119  CE2 PHE A 274     -17.211   0.954  -9.013  1.00 45.21           C
ANISOU 2119  CE2 PHE A 274     7014   5262   4903   -366  -1035    200       C
ATOM   2120  CZ  PHE A 274     -16.804   1.834  -8.034  1.00 45.32           C
ANISOU 2120  CZ  PHE A 274     6912   5333   4976   -330   -990    197       C
ATOM   2121  N   SER A 275     -16.021  -3.699  -9.879  1.00 45.07           N
ANISOU 2121  N   SER A 275     7319   5089   4717   -417   -934    193       N
ATOM   2122  CA  SER A 275     -17.407  -4.126 -10.095  1.00 48.97           C
ANISOU 2122  CA  SER A 275     7822   5577   5209   -480  -1037    198       C
ATOM   2123  C   SER A 275     -17.867  -5.127  -9.057  1.00 55.35           C
ANISOU 2123  C   SER A 275     8569   6412   6048   -504  -1038    198       C
ATOM   2124  O   SER A 275     -18.977  -5.009  -8.543  1.00 62.63           O
ANISOU 2124  O   SER A 275     9405   7374   7018   -539  -1106    202       O
ATOM   2125  CB  SER A 275     -17.598  -4.755 -11.464  1.00 40.49           C
ANISOU 2125  CB  SER A 275     6912   4422   4051   -517  -1074    198       C
ATOM   2126  OG  SER A 275     -17.682  -3.814 -12.505  1.00 46.88           O
ANISOU 2126  OG  SER A 275     7778   5204   4830   -515  -1112    200       O
ATOM   2127  N   LYS A 276     -17.023  -6.088  -8.695  1.00 54.07           N
ANISOU 2127  N   LYS A 276     8448   6232   5864   -482   -960    195       N
ATOM   2128  CA  LYS A 276     -17.412  -7.114  -7.723  1.00 59.20           C
ANISOU 2128  CA  LYS A 276     9057   6900   6536   -503   -955    196       C
ATOM   2129  C   LYS A 276     -17.504  -6.542  -6.320  1.00 61.18           C
ANISOU 2129  C   LYS A 276     9149   7231   6868   -477   -939    197       C
ATOM   2130  O   LYS A 276     -18.354  -6.993  -5.551  1.00 67.43           O
ANISOU 2130  O   LYS A 276     9878   8049   7694   -511   -970    199       O
ATOM   2131  CB  LYS A 276     -16.485  -8.296  -7.863  1.00 55.23           C
ANISOU 2131  CB  LYS A 276     8660   6347   5979   -484   -879    194       C
ATOM   2132  CG  LYS A 276     -16.758  -9.528  -7.070  1.00 62.12           C
ANISOU 2132  CG  LYS A 276     9531   7218   6854   -504   -865    195       C
ATOM   2133  CD  LYS A 276     -18.044 -10.398  -7.371  1.00 66.61           C
ANISOU 2133  CD  LYS A 276    10149   7756   7402   -587   -944    195       C
ATOM   2134  CE  LYS A 276     -18.015 -11.183  -8.815  1.00 68.00           C
ANISOU 2134  CE  LYS A 276    10511   7840   7486   -624   -961    193       C
ATOM   2135  NZ  LYS A 276     -17.096 -12.316  -9.097  1.00 64.67           N
ANISOU 2135  NZ  LYS A 276    10218   7355   6999   -602   -882    192       N
ATOM   2136  N   MET A 277     -16.695  -5.530  -6.010  1.00 54.66           N
ANISOU 2136  N   MET A 277     8259   6440   6070   -422   -892    195       N
ATOM   2137  CA  MET A 277     -16.823  -4.800  -4.741  1.00 53.24           C
ANISOU 2137  CA  MET A 277     7930   6333   5964   -399   -883    195       C
ATOM   2138  C   MET A 277     -18.128  -4.019  -4.668  1.00 59.67           C
ANISOU 2138  C   MET A 277     8665   7181   6824   -436   -968    199       C
ATOM   2139  O   MET A 277     -18.813  -4.013  -3.634  1.00 58.89           O
ANISOU 2139  O   MET A 277     8466   7130   6780   -449   -985    201       O
ATOM   2140  CB  MET A 277     -15.642  -3.822  -4.570  1.00 48.89           C
ANISOU 2140  CB  MET A 277     7340   5807   5428   -337   -817    190       C
ATOM   2141  CG  MET A 277     -15.739  -2.836  -3.386  1.00 50.19           C
ANISOU 2141  CG  MET A 277     7360   6045   5665   -313   -812    189       C
ATOM   2142  SD  MET A 277     -16.637  -1.288  -3.710  1.00 49.18           S
ANISOU 2142  SD  MET A 277     7165   5945   5575   -328   -881    191       S
ATOM   2143  CE  MET A 277     -15.751  -0.528  -5.028  1.00 48.66           C
ANISOU 2143  CE  MET A 277     7191   5834   5462   -303   -856    187       C
ATOM   2144  N   TYR A 278     -18.460  -3.338  -5.760  1.00 58.45           N
ANISOU 2144  N   TYR A 278     8558   7002   6648   -450  -1020    201       N
ATOM   2145  CA  TYR A 278     -19.729  -2.646  -5.899  1.00 62.54           C
ANISOU 2145  CA  TYR A 278     9016   7543   7202   -485  -1110    207       C
ATOM   2146  C   TYR A 278     -20.898  -3.629  -5.858  1.00 74.37           C
ANISOU 2146  C   TYR A 278    10521   9033   8705   -549  -1175    210       C
ATOM   2147  O   TYR A 278     -22.006  -3.255  -5.494  1.00 71.89           O
ANISOU 2147  O   TYR A 278    10117   8754   8443   -577  -1238    214       O
ATOM   2148  CB  TYR A 278     -19.706  -1.828  -7.197  1.00 60.80           C
ANISOU 2148  CB  TYR A 278     8869   7287   6943   -482  -1149    208       C
ATOM   2149  CG  TYR A 278     -20.647  -0.660  -7.306  1.00 55.46           C
ANISOU 2149  CG  TYR A 278     8120   6643   6311   -488  -1223    215       C
ATOM   2150  CD1 TYR A 278     -20.436   0.501  -6.586  1.00 50.57           C
ANISOU 2150  CD1 TYR A 278     7395   6074   5745   -447  -1195    215       C
ATOM   2151  CD2 TYR A 278     -21.716  -0.706  -8.184  1.00 57.01           C
ANISOU 2151  CD2 TYR A 278     8357   6814   6489   -533  -1322    221       C
ATOM   2152  CE1 TYR A 278     -21.292   1.583  -6.720  1.00 52.93           C
ANISOU 2152  CE1 TYR A 278     7632   6398   6080   -448  -1259    223       C
ATOM   2153  CE2 TYR A 278     -22.571   0.363  -8.327  1.00 56.13           C
ANISOU 2153  CE2 TYR A 278     8180   6731   6417   -533  -1392    229       C
ATOM   2154  CZ  TYR A 278     -22.363   1.498  -7.596  1.00 53.63           C
ANISOU 2154  CZ  TYR A 278     7760   6463   6154   -489  -1358    230       C
ATOM   2155  OH  TYR A 278     -23.247   2.529  -7.770  1.00 60.01           O
ANISOU 2155  OH  TYR A 278     8509   7295   6999   -487  -1428    240       O
ATOM   2156  N   LYS A 279     -20.707  -4.862  -6.303  1.00 94.55           N
ANISOU 2156  N   LYS A 279    13184  11536  11204   -575  -1164    207       N
ATOM   2157  CA  LYS A 279     -21.732  -5.921  -6.263  1.00 94.32           C
ANISOU 2157  CA  LYS A 279    13173  11493  11173   -642  -1218    207       C
ATOM   2158  C   LYS A 279     -22.007  -6.438  -4.878  1.00100.70           C
ANISOU 2158  C   LYS A 279    13886  12343  12034   -647  -1185    207       C
ATOM   2159  O   LYS A 279     -23.075  -7.014  -4.615  1.00 97.79           O
ANISOU 2159  O   LYS A 279    13486  11979  11689   -704  -1235    208       O
ATOM   2160  CB  LYS A 279     -21.305  -7.131  -6.924  1.00 94.94           C
ANISOU 2160  CB  LYS A 279    13392  11503  11177   -663  -1196    203       C
ATOM   2161  CG  LYS A 279     -21.526  -7.412  -8.372  1.00 92.99           C
ANISOU 2161  CG  LYS A 279    13283  11191  10860   -700  -1252    202       C
ATOM   2162  CD  LYS A 279     -20.367  -8.183  -8.788  1.00 90.29           C
ANISOU 2162  CD  LYS A 279    13066  10791  10448   -673  -1172    199       C
ATOM   2163  CE  LYS A 279     -20.634  -8.645 -10.384  1.00 87.88           C
ANISOU 2163  CE  LYS A 279    12932  10404  10055   -720  -1231    196       C
ATOM   2164  NZ  LYS A 279     -19.211  -9.176 -10.621  1.00 73.41           N
ANISOU 2164  NZ  LYS A 279    11204   8524   8166   -670  -1123    194       N
ATOM   2165  N   SER A 280     -21.007  -6.361  -4.009  1.00 81.72           N
ANISOU 2165  N   SER A 280    11444   9963   9642   -591  -1099    206       N
ATOM   2166  CA  SER A 280     -21.113  -7.000  -2.660  1.00 83.51           C
ANISOU 2166  CA  SER A 280    11602  10222   9907   -590  -1058    206       C
ATOM   2167  C   SER A 280     -21.932  -6.137  -1.695  1.00 82.09           C
ANISOU 2167  C   SER A 280    11274  10108   9809   -593  -1083    209       C
ATOM   2168  O   SER A 280     -22.846  -6.605  -1.002  1.00 85.50           O
ANISOU 2168  O   SER A 280    11650  10558  10279   -633  -1103    210       O
ATOM   2169  CB  SER A 280     -19.676  -7.220  -2.201  1.00 76.86           C
ANISOU 2169  CB  SER A 280    10785   9378   9042   -525   -962    203       C
ATOM   2170  N   PHE A 281     -21.690  -4.840  -1.777  1.00 81.18           N
ANISOU 2170  N   PHE A 281    11102  10023   9719   -555  -1087    210       N
ATOM   2171  CA  PHE A 281     -22.344  -3.938  -0.859  1.00 77.66           C
ANISOU 2171  CA  PHE A 281    10521   9637   9348   -548  -1101    213       C
ATOM   2172  C   PHE A 281     -23.797  -3.758  -1.239  1.00 76.49           C
ANISOU 2172  C   PHE A 281    10333   9496   9234   -604  -1191    218       C
ATOM   2173  O   PHE A 281     -24.679  -3.973  -0.408  1.00 74.58           O
ANISOU 2173  O   PHE A 281    10008   9283   9045   -632  -1204    220       O
ATOM   2174  CB  PHE A 281     -21.622  -2.602  -0.814  1.00 73.62           C
ANISOU 2174  CB  PHE A 281     9967   9154   8852   -490  -1074    212       C
ATOM   2175  CG  PHE A 281     -21.739  -1.940   0.514  1.00 73.06           C
ANISOU 2175  CG  PHE A 281     9772   9142   8845   -464  -1043    212       C
ATOM   2176  CD1 PHE A 281     -22.859  -1.175   0.824  1.00 69.53           C
ANISOU 2176  CD1 PHE A 281     9230   8731   8459   -482  -1092    218       C
ATOM   2177  CD2 PHE A 281     -20.779  -2.152   1.491  1.00 71.62           C
ANISOU 2177  CD2 PHE A 281     9571   8978   8663   -424   -967    207       C
ATOM   2178  CE1 PHE A 281     -22.999  -0.593   2.068  1.00 69.82           C
ANISOU 2178  CE1 PHE A 281     9159   8817   8552   -459  -1060    218       C
ATOM   2179  CE2 PHE A 281     -20.907  -1.572   2.734  1.00 71.28           C
ANISOU 2179  CE2 PHE A 281     9423   8987   8675   -403   -941    207       C
ATOM   2180  CZ  PHE A 281     -22.022  -0.785   3.025  1.00 72.84           C
ANISOU 2180  CZ  PHE A 281     9531   9216   8930   -421   -984    212       C
ATOM   2181  N   SER A 282     -24.071  -3.420  -2.502  1.00 80.39           N
ANISOU 2181  N   SER A 282    10887   9960   9698   -621  -1255    220       N
ATOM   2182  CA  SER A 282     -25.447  -3.264  -2.981  1.00 78.31           C
ANISOU 2182  CA  SER A 282    10589   9700   9464   -673  -1353    226       C
ATOM   2183  C   SER A 282     -25.490  -3.198  -4.499  1.00 72.38           C
ANISOU 2183  C   SER A 282     9948   8900   8653   -692  -1417    227       C
ATOM   2184  O   SER A 282     -26.012  -2.240  -5.057  1.00 63.19           O
ANISOU 2184  O   SER A 282     8756   7746   7506   -687  -1480    233       O
ATOM   2185  CB  SER A 282     -26.092  -2.007  -2.390  1.00 74.74           C
ANISOU 2185  CB  SER A 282    10003   9306   9089   -652  -1375    232       C
ATOM   2186  OG  SER A 282     -25.217  -0.893  -2.463  1.00 74.24           O
ANISOU 2186  OG  SER A 282     9935   9253   9018   -590  -1337    232       O
TER
ATOM   2187  N   PRO B   0     -47.070 -11.575  28.320  1.00 70.24           N
ANISOU 2187  N   PRO B   0     7836   8822  10031  -1531    434    229       N
ATOM   2188  CA  PRO B   0     -46.302 -10.875  27.288  1.00 69.76           C
ANISOU 2188  CA  PRO B   0     7771   8801   9932  -1471    314    233       C
ATOM   2189  C   PRO B   0     -44.789 -10.941  27.490  1.00 64.53           C
ANISOU 2189  C   PRO B   0     7259   8121   9137  -1394    307    234       C
ATOM   2190  O   PRO B   0     -44.278 -11.909  28.059  1.00 63.32           O
ANISOU 2190  O   PRO B   0     7234   7918   8906  -1404    364    230       O
ATOM   2191  CB  PRO B   0     -46.796  -9.429  27.412  1.00 74.31           C
ANISOU 2191  CB  PRO B   0     8209   9429  10597  -1419    309    243       C
ATOM   2192  CG  PRO B   0     -47.254  -9.301  28.826  1.00 72.78           C
ANISOU 2192  CG  PRO B   0     8004   9211  10436  -1412    447    246       C
ATOM   2193  CD  PRO B   0     -47.773 -10.649  29.225  1.00 73.35           C
ANISOU 2193  CD  PRO B   0     8127   9233  10510  -1503    517    236       C
ATOM   2194  N   MET B   1     -44.096  -9.917  26.991  1.00 64.10           N
ANISOU 2194  N   MET B   1     7186   8108   9062  -1317    235    240       N
ATOM   2195  CA  MET B   1     -42.661  -9.730  27.179  1.00 68.11           C
ANISOU 2195  CA  MET B   1     7812   8610   9459  -1235    225    242       C
ATOM   2196  C   MET B   1     -42.349  -9.017  28.492  1.00 61.26           C
ANISOU 2196  C   MET B   1     6960   7740   8576  -1167    315    247       C
ATOM   2197  O   MET B   1     -43.150  -8.223  28.997  1.00 56.52           O
ANISOU 2197  O   MET B   1     6257   7158   8059  -1162    361    252       O
ATOM   2198  CB  MET B   1     -42.042  -8.976  26.003  1.00 66.81           C
ANISOU 2198  CB  MET B   1     7623   8487   9276  -1189    108    244       C
ATOM   2199  CG  MET B   1     -42.838  -7.815  25.478  1.00 63.19           C
ANISOU 2199  CG  MET B   1     7014   8078   8917  -1182     59    250       C
ATOM   2200  SD  MET B   1     -41.925  -7.200  24.053  1.00 71.84           S
ANISOU 2200  SD  MET B   1     8126   9208   9965  -1133    -75    252       S
ATOM   2201  CE  MET B   1     -40.328  -6.948  24.785  1.00 61.78           C
ANISOU 2201  CE  MET B   1     6978   7921   8575  -1040    -37    252       C
ATOM   2202  N   LYS B   2     -41.179  -9.334  29.052  1.00 60.61           N
ANISOU 2202  N   LYS B   2     7010   7632   8387  -1115    341    246       N
ATOM   2203  CA  LYS B   2     -40.811  -8.781  30.348  1.00 62.80           C
ANISOU 2203  CA  LYS B   2     7324   7901   8638  -1055    426    249       C
ATOM   2204  C   LYS B   2     -40.850  -7.260  30.276  1.00 59.56           C
ANISOU 2204  C   LYS B   2     6815   7540   8276   -997    399    255       C
ATOM   2205  O   LYS B   2     -40.386  -6.647  29.310  1.00 58.66           O
ANISOU 2205  O   LYS B   2     6669   7462   8156   -966    306    256       O
ATOM   2206  CB  LYS B   2     -39.416  -9.269  30.764  1.00 61.59           C
ANISOU 2206  CB  LYS B   2     7322   7721   8358  -1000    430    248       C
ATOM   2207  N   THR B   3     -41.468  -6.664  31.278  1.00 56.66           N
ANISOU 2207  N   THR B   3     6400   7170   7959   -985    485    258       N
ATOM   2208  CA  THR B   3     -41.632  -5.226  31.349  1.00 59.98           C
ANISOU 2208  CA  THR B   3     6728   7631   8432   -933    478    264       C
ATOM   2209  C   THR B   3     -40.558  -4.681  32.296  1.00 60.56           C
ANISOU 2209  C   THR B   3     6894   7696   8421   -854    516    263       C
ATOM   2210  O   THR B   3     -40.378  -5.216  33.396  1.00 61.05           O
ANISOU 2210  O   THR B   3     7045   7718   8435   -852    601    262       O
ATOM   2211  CB  THR B   3     -43.042  -4.901  31.852  1.00 60.03           C
ANISOU 2211  CB  THR B   3     6620   7636   8551   -970    553    269       C
ATOM   2212  OG1 THR B   3     -44.014  -5.630  31.093  1.00 62.41           O
ANISOU 2212  OG1 THR B   3     6848   7939   8924  -1053    524    267       O
ATOM   2213  CG2 THR B   3     -43.345  -3.438  31.635  1.00 61.55           C
ANISOU 2213  CG2 THR B   3     6701   7874   8810   -921    528    276       C
ATOM   2214  N   ILE B   4     -39.826  -3.643  31.880  1.00 58.79           N
ANISOU 2214  N   ILE B   4     6654   7509   8176   -791    453    264       N
ATOM   2215  CA  ILE B   4     -38.777  -3.072  32.725  1.00 52.58           C
ANISOU 2215  CA  ILE B   4     5949   6718   7310   -720    480    262       C
ATOM   2216  C   ILE B   4     -39.079  -1.601  32.998  1.00 54.94           C
ANISOU 2216  C   ILE B   4     6166   7045   7663   -675    497    266       C
ATOM   2217  O   ILE B   4     -39.166  -0.785  32.071  1.00 60.05           O
ANISOU 2217  O   ILE B   4     6732   7732   8353   -660    426    269       O
ATOM   2218  CB  ILE B   4     -37.390  -3.253  32.106  1.00 48.89           C
ANISOU 2218  CB  ILE B   4     5563   6262   6750   -682    398    257       C
ATOM   2219  CG1 ILE B   4     -36.968  -4.725  32.215  1.00 51.15           C
ANISOU 2219  CG1 ILE B   4     5959   6508   6967   -712    408    254       C
ATOM   2220  CG2 ILE B   4     -36.384  -2.391  32.842  1.00 50.24           C
ANISOU 2220  CG2 ILE B   4     5789   6442   6860   -608    411    254       C
ATOM   2221  CD1 ILE B   4     -35.668  -5.061  31.559  1.00 51.03           C
ANISOU 2221  CD1 ILE B   4     6023   6501   6866   -678    332    250       C
ATOM   2222  N   LEU B   5     -39.191  -1.254  34.271  1.00 48.92           N
ANISOU 2222  N   LEU B   5     5435   6261   6892   -652    591    266       N
ATOM   2223  CA  LEU B   5     -39.382   0.127  34.686  1.00 50.69           C
ANISOU 2223  CA  LEU B   5     5603   6504   7153   -605    619    269       C
ATOM   2224  C   LEU B   5     -38.043   0.711  35.136  1.00 50.42           C
ANISOU 2224  C   LEU B   5     5661   6474   7024   -538    602    262       C
ATOM   2225  O   LEU B   5     -37.450   0.227  36.102  1.00 49.42           O
ANISOU 2225  O   LEU B   5     5643   6316   6820   -525    651    258       O
ATOM   2226  CB  LEU B   5     -40.415   0.195  35.807  1.00 50.48           C
ANISOU 2226  CB  LEU B   5     5552   6447   7182   -623    740    273       C
ATOM   2227  CG  LEU B   5     -40.593   1.543  36.465  1.00 48.74           C
ANISOU 2227  CG  LEU B   5     5296   6234   6989   -572    791    276       C
ATOM   2228  CD1 LEU B   5     -41.265   2.430  35.463  1.00 51.56           C
ANISOU 2228  CD1 LEU B   5     5515   6633   7441   -568    734    284       C
ATOM   2229  CD2 LEU B   5     -41.422   1.385  37.704  1.00 46.96           C
ANISOU 2229  CD2 LEU B   5     5082   5967   6795   -589    921    279       C
ATOM   2230  N   VAL B   6     -37.588   1.764  34.457  1.00 52.85           N
ANISOU 2230  N   VAL B   6     5925   6819   7336   -497    534    262       N
ATOM   2231  CA  VAL B   6     -36.302   2.407  34.723  1.00 48.89           C
ANISOU 2231  CA  VAL B   6     5495   6328   6751   -438    505    254       C
ATOM   2232  C   VAL B   6     -36.556   3.771  35.347  1.00 54.25           C
ANISOU 2232  C   VAL B   6     6138   7014   7461   -398    552    255       C
ATOM   2233  O   VAL B   6     -37.249   4.614  34.761  1.00 57.10           O
ANISOU 2233  O   VAL B   6     6397   7399   7900   -395    535    261       O
ATOM   2234  CB  VAL B   6     -35.469   2.573  33.445  1.00 49.72           C
ANISOU 2234  CB  VAL B   6     5591   6468   6831   -423    394    250       C
ATOM   2235  CG1 VAL B   6     -34.165   3.276  33.760  1.00 46.80           C
ANISOU 2235  CG1 VAL B   6     5288   6110   6384   -366    370    241       C
ATOM   2236  CG2 VAL B   6     -35.257   1.233  32.734  1.00 47.80           C
ANISOU 2236  CG2 VAL B   6     5385   6217   6561   -463    347    250       C
ATOM   2237  N   THR B   7     -36.038   3.977  36.546  1.00 52.91           N
ANISOU 2237  N   THR B   7     6053   6820   7229   -368    612    249       N
ATOM   2238  CA  THR B   7     -35.973   5.317  37.097  1.00 52.65           C
ANISOU 2238  CA  THR B   7     6009   6793   7202   -324    644    246       C
ATOM   2239  C   THR B   7     -34.701   5.984  36.581  1.00 56.57           C
ANISOU 2239  C   THR B   7     6536   7320   7639   -283    561    237       C
ATOM   2240  O   THR B   7     -33.778   5.321  36.097  1.00 56.39           O
ANISOU 2240  O   THR B   7     6562   7306   7556   -283    496    231       O
ATOM   2241  CB  THR B   7     -35.972   5.308  38.629  1.00 55.50           C
ANISOU 2241  CB  THR B   7     6455   7112   7519   -311    745    243       C
ATOM   2242  OG1 THR B   7     -34.650   5.014  39.113  1.00 53.37           O
ANISOU 2242  OG1 THR B   7     6302   6836   7139   -285    718    232       O
ATOM   2243  CG2 THR B   7     -36.960   4.294  39.180  1.00 55.44           C
ANISOU 2243  CG2 THR B   7     6450   7067   7546   -358    827    250       C
ATOM   2244  N   GLY B   8     -34.671   7.312  36.660  1.00 57.29           N
ANISOU 2244  N   GLY B   8     6595   7425   7748   -247    566    235       N
ATOM   2245  CA  GLY B   8     -33.553   8.069  36.131  1.00 53.61           C
ANISOU 2245  CA  GLY B   8     6147   6988   7236   -211    492    225       C
ATOM   2246  C   GLY B   8     -33.288   7.793  34.661  1.00 56.97           C
ANISOU 2246  C   GLY B   8     6524   7444   7676   -224    395    227       C
ATOM   2247  O   GLY B   8     -32.143   7.538  34.260  1.00 52.28           O
ANISOU 2247  O   GLY B   8     5983   6864   7018   -212    332    218       O
ATOM   2248  N   GLY B   9     -34.348   7.827  33.847  1.00 53.97           N
ANISOU 2248  N   GLY B   9     6048   7075   7383   -248    381    239       N
ATOM   2249  CA  GLY B   9     -34.199   7.574  32.428  1.00 50.34           C
ANISOU 2249  CA  GLY B   9     5546   6641   6939   -262    288    242       C
ATOM   2250  C   GLY B   9     -33.348   8.611  31.724  1.00 56.66           C
ANISOU 2250  C   GLY B   9     6344   7468   7715   -224    224    235       C
ATOM   2251  O   GLY B   9     -32.812   8.335  30.643  1.00 55.35           O
ANISOU 2251  O   GLY B   9     6178   7320   7532   -230    146    234       O
ATOM   2252  N   SER B  10     -33.195   9.794  32.330  1.00 59.04           N
ANISOU 2252  N   SER B  10     6650   7770   8014   -188    260    231       N
ATOM   2253  CA  SER B  10     -32.489  10.936  31.754  1.00 56.18           C
ANISOU 2253  CA  SER B  10     6282   7428   7634   -153    213    225       C
ATOM   2254  C   SER B  10     -31.033  11.069  32.209  1.00 52.85           C
ANISOU 2254  C   SER B  10     5950   7009   7120   -130    198    207       C
ATOM   2255  O   SER B  10     -30.357  12.027  31.806  1.00 47.58           O
ANISOU 2255  O   SER B  10     5286   6358   6435   -104    164    199       O
ATOM   2256  CB  SER B  10     -33.241  12.203  32.127  1.00 49.40           C
ANISOU 2256  CB  SER B  10     5373   6566   6830   -128    263    230       C
ATOM   2257  OG  SER B  10     -33.447  12.162  33.527  1.00 52.48           O
ANISOU 2257  OG  SER B  10     5806   6929   7204   -124    351    227       O
ATOM   2258  N   GLY B  11     -30.527  10.139  33.042  1.00 52.26           N
ANISOU 2258  N   GLY B  11     5950   6918   6987   -138    223    200       N
ATOM   2259  CA  GLY B  11     -29.137  10.187  33.446  1.00 47.81           C
ANISOU 2259  CA  GLY B  11     5467   6361   6339   -115    201    184       C
ATOM   2260  C   GLY B  11     -28.199   9.549  32.411  1.00 48.11           C
ANISOU 2260  C   GLY B  11     5520   6419   6342   -119    121    180       C
ATOM   2261  O   GLY B  11     -28.609   8.916  31.430  1.00 44.10           O
ANISOU 2261  O   GLY B  11     4975   5916   5866   -143     83    189       O
ATOM   2262  N   PHE B  12     -26.900   9.721  32.661  1.00 45.58           N
ANISOU 2262  N   PHE B  12     5257   6109   5953    -96     95    165       N
ATOM   2263  CA  PHE B  12     -25.880   9.189  31.762  1.00 44.65           C
ANISOU 2263  CA  PHE B  12     5157   6008   5798    -93     26    159       C
ATOM   2264  C   PHE B  12     -26.062   7.689  31.544  1.00 41.57           C
ANISOU 2264  C   PHE B  12     4791   5606   5398   -117     18    169       C
ATOM   2265  O   PHE B  12     -26.090   7.208  30.401  1.00 38.07           O
ANISOU 2265  O   PHE B  12     4323   5170   4970   -133    -30    174       O
ATOM   2266  CB  PHE B  12     -24.505   9.510  32.343  1.00 43.73           C
ANISOU 2266  CB  PHE B  12     5101   5904   5612    -65     12    142       C
ATOM   2267  CG  PHE B  12     -23.401   8.654  31.824  1.00 42.28           C
ANISOU 2267  CG  PHE B  12     4952   5732   5379    -59    -41    137       C
ATOM   2268  CD1 PHE B  12     -22.663   9.048  30.725  1.00 41.52           C
ANISOU 2268  CD1 PHE B  12     4833   5658   5282    -52    -96    130       C
ATOM   2269  CD2 PHE B  12     -23.072   7.478  32.456  1.00 39.94           C
ANISOU 2269  CD2 PHE B  12     4716   5422   5037    -58    -31    139       C
ATOM   2270  CE1 PHE B  12     -21.619   8.255  30.262  1.00 45.49           C
ANISOU 2270  CE1 PHE B  12     5370   6172   5743    -43   -139    126       C
ATOM   2271  CE2 PHE B  12     -22.059   6.688  31.988  1.00 40.59           C
ANISOU 2271  CE2 PHE B  12     4831   5514   5076    -47    -76    135       C
ATOM   2272  CZ  PHE B  12     -21.314   7.067  30.897  1.00 39.82           C
ANISOU 2272  CZ  PHE B  12     4709   5441   4982    -39   -129    129       C
ATOM   2273  N   LEU B  13     -26.192   6.936  32.641  1.00 44.69           N
ANISOU 2273  N   LEU B  13     5238   5977   5763   -121     66    170       N
ATOM   2274  CA  LEU B  13     -26.358   5.489  32.545  1.00 44.29           C
ANISOU 2274  CA  LEU B  13     5221   5909   5698   -144     66    178       C
ATOM   2275  C   LEU B  13     -27.800   5.125  32.237  1.00 42.83           C
ANISOU 2275  C   LEU B  13     4980   5708   5584   -185     94    192       C
ATOM   2276  O   LEU B  13     -28.052   4.257  31.386  1.00 42.65           O
ANISOU 2276  O   LEU B  13     4947   5683   5576   -212     62    199       O
ATOM   2277  CB  LEU B  13     -25.913   4.798  33.841  1.00 33.15           C
ANISOU 2277  CB  LEU B  13     3898   4476   4223   -132    107    175       C
ATOM   2278  CG  LEU B  13     -26.142   3.271  33.829  1.00 41.08           C
ANISOU 2278  CG  LEU B  13     4946   5454   5209   -156    116    184       C
ATOM   2279  CD1 LEU B  13     -25.451   2.606  32.640  1.00 37.14           C
ANISOU 2279  CD1 LEU B  13     4451   4969   4692   -157     48    185       C
ATOM   2280  CD2 LEU B  13     -25.691   2.589  35.138  1.00 42.00           C
ANISOU 2280  CD2 LEU B  13     5158   5545   5256   -138    157    182       C
ATOM   2281  N   GLY B  14     -28.751   5.771  32.917  1.00 39.58           N
ANISOU 2281  N   GLY B  14     4533   5287   5218   -189    153    196       N
ATOM   2282  CA  GLY B  14     -30.153   5.451  32.679  1.00 47.32           C
ANISOU 2282  CA  GLY B  14     5451   6255   6274   -228    183    209       C
ATOM   2283  C   GLY B  14     -30.527   5.561  31.208  1.00 49.74           C
ANISOU 2283  C   GLY B  14     5684   6583   6633   -246    117    216       C
ATOM   2284  O   GLY B  14     -31.113   4.635  30.631  1.00 49.03           O
ANISOU 2284  O   GLY B  14     5575   6484   6569   -285    101    223       O
ATOM   2285  N   ARG B  15     -30.152   6.685  30.573  1.00 50.13           N
ANISOU 2285  N   ARG B  15     5698   6658   6693   -220     75    212       N
ATOM   2286  CA  ARG B  15     -30.435   6.905  29.154  1.00 48.95           C
ANISOU 2286  CA  ARG B  15     5487   6527   6585   -231      8    218       C
ATOM   2287  C   ARG B  15     -29.775   5.844  28.265  1.00 49.34           C
ANISOU 2287  C   ARG B  15     5578   6577   6594   -248    -52    216       C
ATOM   2288  O   ARG B  15     -30.287   5.513  27.190  1.00 49.97           O
ANISOU 2288  O   ARG B  15     5617   6660   6708   -275    -98    223       O
ATOM   2289  CB  ARG B  15     -30.000   8.319  28.758  1.00 47.10           C
ANISOU 2289  CB  ARG B  15     5227   6314   6356   -195    -19    213       C
ATOM   2290  N   ARG B  16     -28.588   5.379  28.641  1.00 48.28           N
ANISOU 2290  N   ARG B  16     5521   6439   6383   -229    -56    206       N
ATOM   2291  CA  ARG B  16     -27.927   4.353  27.852  1.00 45.17           C
ANISOU 2291  CA  ARG B  16     5171   6042   5948   -239   -105    205       C
ATOM   2292  C   ARG B  16     -28.506   2.968  28.107  1.00 50.79           C
ANISOU 2292  C   ARG B  16     5912   6727   6659   -278    -80    212       C
ATOM   2293  O   ARG B  16     -28.490   2.111  27.208  1.00 51.67           O
ANISOU 2293  O   ARG B  16     6036   6831   6764   -303   -120    216       O
ATOM   2294  CB  ARG B  16     -26.430   4.383  28.141  1.00 45.65           C
ANISOU 2294  CB  ARG B  16     5298   6112   5934   -200   -119    193       C
ATOM   2295  CG  ARG B  16     -25.719   5.568  27.481  1.00 43.84           C
ANISOU 2295  CG  ARG B  16     5044   5909   5704   -172   -160    185       C
ATOM   2296  CD  ARG B  16     -24.261   5.656  27.898  1.00 41.38           C
ANISOU 2296  CD  ARG B  16     4789   5608   5324   -135   -169    171       C
ATOM   2297  NE  ARG B  16     -23.539   6.658  27.122  1.00 34.54           N
ANISOU 2297  NE  ARG B  16     3901   4765   4457   -115   -209    162       N
ATOM   2298  CZ  ARG B  16     -23.632   7.968  27.322  1.00 39.65           C
ANISOU 2298  CZ  ARG B  16     4514   5425   5127   -101   -197    157       C
ATOM   2299  NH1 ARG B  16     -24.431   8.460  28.271  1.00 40.58           N
ANISOU 2299  NH1 ARG B  16     4613   5534   5271   -103   -147    159       N
ATOM   2300  NH2 ARG B  16     -22.934   8.796  26.561  1.00 40.70           N
ANISOU 2300  NH2 ARG B  16     4635   5575   5255    -86   -232    148       N
ATOM   2301  N   LEU B  17     -29.030   2.725  29.312  1.00 48.88           N
ANISOU 2301  N   LEU B  17     5686   6466   6422   -285    -10    214       N
ATOM   2302  CA  LEU B  17     -29.688   1.447  29.543  1.00 52.56           C
ANISOU 2302  CA  LEU B  17     6176   6902   6892   -327     20    221       C
ATOM   2303  C   LEU B  17     -30.974   1.359  28.738  1.00 56.67           C
ANISOU 2303  C   LEU B  17     6615   7423   7493   -375      5    230       C
ATOM   2304  O   LEU B  17     -31.257   0.317  28.134  1.00 55.82           O
ANISOU 2304  O   LEU B  17     6520   7301   7386   -415    -17    234       O
ATOM   2305  CB  LEU B  17     -29.983   1.243  31.026  1.00 47.32           C
ANISOU 2305  CB  LEU B  17     5552   6214   6215   -324    103    221       C
ATOM   2306  CG  LEU B  17     -28.770   1.054  31.909  1.00 42.32           C
ANISOU 2306  CG  LEU B  17     5011   5573   5494   -282    116    213       C
ATOM   2307  CD1 LEU B  17     -29.201   1.069  33.354  1.00 42.97           C
ANISOU 2307  CD1 LEU B  17     5128   5630   5569   -279    199    214       C
ATOM   2308  CD2 LEU B  17     -28.151  -0.237  31.554  1.00 42.67           C
ANISOU 2308  CD2 LEU B  17     5125   5602   5486   -289     89    214       C
ATOM   2309  N   VAL B  18     -31.749   2.456  28.712  1.00 64.31           N
ANISOU 2309  N   VAL B  18     7499   8408   8528   -371     15    234       N
ATOM   2310  CA  VAL B  18     -33.013   2.496  27.967  1.00 65.86           C
ANISOU 2310  CA  VAL B  18     7604   8609   8808   -412     -4    243       C
ATOM   2311  C   VAL B  18     -32.800   2.087  26.515  1.00 66.08           C
ANISOU 2311  C   VAL B  18     7629   8647   8831   -431    -90    244       C
ATOM   2312  O   VAL B  18     -33.458   1.168  26.007  1.00 63.13           O
ANISOU 2312  O   VAL B  18     7243   8261   8482   -482   -107    248       O
ATOM   2313  CB  VAL B  18     -33.640   3.902  28.055  1.00 66.23           C
ANISOU 2313  CB  VAL B  18     7567   8678   8921   -388      9    248       C
ATOM   2314  CG1 VAL B  18     -34.799   4.066  27.033  1.00 61.66           C
ANISOU 2314  CG1 VAL B  18     6889   8112   8428   -421    -34    258       C
ATOM   2315  CG2 VAL B  18     -34.090   4.215  29.491  1.00 61.84           C
ANISOU 2315  CG2 VAL B  18     7011   8104   8379   -377    105    248       C
ATOM   2316  N   SER B  19     -31.872   2.769  25.826  1.00 58.67           N
ANISOU 2316  N   SER B  19     6705   7729   7860   -394   -145    239       N
ATOM   2317  CA  SER B  19     -31.641   2.489  24.411  1.00 61.97           C
ANISOU 2317  CA  SER B  19     7124   8153   8269   -409   -225    240       C
ATOM   2318  C   SER B  19     -31.309   1.019  24.191  1.00 58.74           C
ANISOU 2318  C   SER B  19     6788   7719   7812   -441   -234    238       C
ATOM   2319  O   SER B  19     -31.873   0.362  23.311  1.00 56.89           O
ANISOU 2319  O   SER B  19     6540   7476   7599   -485   -275    242       O
ATOM   2320  CB  SER B  19     -30.515   3.388  23.884  1.00 61.84           C
ANISOU 2320  CB  SER B  19     7128   8156   8212   -361   -266    234       C
ATOM   2321  OG  SER B  19     -30.167   3.074  22.539  1.00 64.18           O
ANISOU 2321  OG  SER B  19     7442   8452   8490   -372   -337    234       O
ATOM   2322  N   HIS B  20     -30.434   0.479  25.027  1.00 58.76           N
ANISOU 2322  N   HIS B  20     6869   7707   7749   -419   -196    232       N
ATOM   2323  CA  HIS B  20     -29.950  -0.876  24.840  1.00 59.91           C
ANISOU 2323  CA  HIS B  20     7096   7827   7840   -438   -202    231       C
ATOM   2324  C   HIS B  20     -31.037  -1.909  25.141  1.00 59.87           C
ANISOU 2324  C   HIS B  20     7088   7795   7867   -497   -167    236       C
ATOM   2325  O   HIS B  20     -31.178  -2.909  24.420  1.00 51.47           O
ANISOU 2325  O   HIS B  20     6055   6712   6791   -536   -196    237       O
ATOM   2326  CB  HIS B  20     -28.737  -1.056  25.739  1.00 57.64           C
ANISOU 2326  CB  HIS B  20     6888   7534   7478   -391   -171    225       C
ATOM   2327  CG  HIS B  20     -28.368  -2.479  25.993  1.00 55.46           C
ANISOU 2327  CG  HIS B  20     6700   7226   7147   -404   -152    225       C
ATOM   2328  ND1 HIS B  20     -27.443  -3.153  25.227  1.00 53.37           N
ANISOU 2328  ND1 HIS B  20     6497   6954   6828   -392   -194    223       N
ATOM   2329  CD2 HIS B  20     -28.784  -3.352  26.940  1.00 54.94           C
ANISOU 2329  CD2 HIS B  20     6675   7129   7069   -425    -94    228       C
ATOM   2330  CE1 HIS B  20     -27.312  -4.386  25.682  1.00 53.90           C
ANISOU 2330  CE1 HIS B  20     6640   6987   6851   -404   -163    225       C
ATOM   2331  NE2 HIS B  20     -28.112  -4.533  26.722  1.00 58.68           N
ANISOU 2331  NE2 HIS B  20     7236   7578   7481   -425   -103    228       N
ATOM   2332  N   LEU B  21     -31.840  -1.664  26.183  1.00 61.42           N
ANISOU 2332  N   LEU B  21     7246   7986   8105   -506   -102    239       N
ATOM   2333  CA  LEU B  21     -32.795  -2.655  26.667  1.00 60.90           C
ANISOU 2333  CA  LEU B  21     7183   7890   8065   -561    -53    243       C
ATOM   2334  C   LEU B  21     -34.104  -2.633  25.886  1.00 63.05           C
ANISOU 2334  C   LEU B  21     7363   8170   8424   -618    -81    248       C
ATOM   2335  O   LEU B  21     -34.903  -3.570  26.015  1.00 62.99           O
ANISOU 2335  O   LEU B  21     7355   8138   8442   -675    -54    250       O
ATOM   2336  CB  LEU B  21     -33.073  -2.455  28.162  1.00 55.90           C
ANISOU 2336  CB  LEU B  21     6558   7244   7437   -547     38    243       C
ATOM   2337  CG  LEU B  21     -32.089  -3.058  29.176  1.00 52.34           C
ANISOU 2337  CG  LEU B  21     6219   6769   6899   -514     82    239       C
ATOM   2338  CD1 LEU B  21     -32.740  -3.105  30.551  1.00 48.69           C
ANISOU 2338  CD1 LEU B  21     5764   6283   6452   -522    176    241       C
ATOM   2339  CD2 LEU B  21     -31.613  -4.440  28.767  1.00 48.51           C
ANISOU 2339  CD2 LEU B  21     5819   6255   6356   -535     62    239       C
ATOM   2340  N   SER B  22     -34.351  -1.579  25.105  1.00 62.65           N
ANISOU 2340  N   SER B  22     7233   8152   8420   -603   -135    251       N
ATOM   2341  CA  SER B  22     -35.561  -1.509  24.297  1.00 63.30           C
ANISOU 2341  CA  SER B  22     7223   8245   8584   -652   -174    257       C
ATOM   2342  C   SER B  22     -35.597  -2.559  23.202  1.00 60.93           C
ANISOU 2342  C   SER B  22     6957   7929   8265   -703   -236    255       C
ATOM   2343  O   SER B  22     -36.632  -2.685  22.549  1.00 60.47           O
ANISOU 2343  O   SER B  22     6828   7876   8271   -753   -272    259       O
ATOM   2344  CB  SER B  22     -35.739  -0.132  23.672  1.00 60.11           C
ANISOU 2344  CB  SER B  22     6737   7876   8226   -618   -222    261       C
ATOM   2345  OG  SER B  22     -36.087   0.796  24.669  1.00 63.20           O
ANISOU 2345  OG  SER B  22     7079   8277   8656   -586   -159    264       O
ATOM   2346  N   LYS B  23     -34.502  -3.283  22.952  1.00 59.62           N
ANISOU 2346  N   LYS B  23     6895   7744   8013   -690   -253    249       N
ATOM   2347  CA  LYS B  23     -34.536  -4.227  21.841  1.00 63.08           C
ANISOU 2347  CA  LYS B  23     7371   8165   8431   -736   -313    248       C
ATOM   2348  C   LYS B  23     -35.361  -5.460  22.182  1.00 65.11           C
ANISOU 2348  C   LYS B  23     7643   8389   8705   -807   -275    247       C
ATOM   2349  O   LYS B  23     -36.223  -5.876  21.395  1.00 67.16           O
ANISOU 2349  O   LYS B  23     7863   8646   9008   -869   -318    247       O
ATOM   2350  CB  LYS B  23     -33.106  -4.630  21.465  1.00 59.49           C
ANISOU 2350  CB  LYS B  23     7024   7699   7881   -697   -335    243       C
ATOM   2351  CG  LYS B  23     -32.122  -3.459  21.445  1.00 60.31           C
ANISOU 2351  CG  LYS B  23     7125   7831   7959   -624   -350    241       C
ATOM   2352  CD  LYS B  23     -30.886  -3.766  20.595  1.00 63.16           C
ANISOU 2352  CD  LYS B  23     7568   8185   8246   -597   -396    237       C
ATOM   2353  CE  LYS B  23     -29.848  -4.624  21.362  1.00 61.84           C
ANISOU 2353  CE  LYS B  23     7501   7994   8001   -568   -349    234       C
ATOM   2354  NZ  LYS B  23     -28.625  -5.002  20.558  1.00 53.78           N
ANISOU 2354  NZ  LYS B  23     6559   6964   6910   -539   -386    230       N
ATOM   2355  N   ASN B  24     -35.159  -6.026  23.371  1.00 66.24           N
ANISOU 2355  N   ASN B  24     7842   8508   8818   -801   -193    245       N
ATOM   2356  CA  ASN B  24     -35.897  -7.220  23.754  1.00 67.21           C
ANISOU 2356  CA  ASN B  24     7990   8595   8953   -869   -147    244       C
ATOM   2357  C   ASN B  24     -36.794  -6.993  24.954  1.00 66.97           C
ANISOU 2357  C   ASN B  24     7902   8561   8982   -883    -62    247       C
ATOM   2358  O   ASN B  24     -37.360  -7.965  25.474  1.00 60.78           O
ANISOU 2358  O   ASN B  24     7146   7743   8205   -936     -6    245       O
ATOM   2359  CB  ASN B  24     -34.936  -8.381  24.002  1.00 64.86           C
ANISOU 2359  CB  ASN B  24     7829   8257   8559   -860   -123    241       C
ATOM   2360  CG  ASN B  24     -33.911  -8.496  22.906  1.00 66.78           C
ANISOU 2360  CG  ASN B  24     8131   8502   8740   -833   -197    238       C
ATOM   2361  OD1 ASN B  24     -32.708  -8.403  23.156  1.00 65.31           O
ANISOU 2361  OD1 ASN B  24     8014   8317   8485   -770   -191    238       O
ATOM   2362  ND2 ASN B  24     -34.383  -8.662  21.668  1.00 66.69           N
ANISOU 2362  ND2 ASN B  24     8091   8493   8753   -879   -269    237       N
ATOM   2363  N   TYR B  25     -36.938  -5.753  25.439  1.00 67.20           N
ANISOU 2363  N   TYR B  25     7859   8622   9053   -838    -43    250       N
ATOM   2364  CA  TYR B  25     -37.867  -5.617  26.550  1.00 69.00           C
ANISOU 2364  CA  TYR B  25     8036   8841   9340   -857     45    253       C
ATOM   2365  C   TYR B  25     -38.645  -4.326  26.304  1.00 65.52           C
ANISOU 2365  C   TYR B  25     7464   8441   8990   -843     25    259       C
ATOM   2366  O   TYR B  25     -38.220  -3.468  25.527  1.00 64.84           O
ANISOU 2366  O   TYR B  25     7349   8386   8902   -804    -45    261       O
ATOM   2367  CB  TYR B  25     -37.248  -5.605  27.987  1.00 61.51           C
ANISOU 2367  CB  TYR B  25     7164   7871   8335   -811    135    252       C
ATOM   2368  CG  TYR B  25     -36.150  -6.624  28.297  1.00 63.45           C
ANISOU 2368  CG  TYR B  25     7551   8083   8476   -794    148    248       C
ATOM   2369  CD1 TYR B  25     -34.894  -6.562  27.685  1.00 64.79           C
ANISOU 2369  CD1 TYR B  25     7781   8263   8572   -746     85    246       C
ATOM   2370  CD2 TYR B  25     -36.536  -7.894  28.748  1.00 68.14           C
ANISOU 2370  CD2 TYR B  25     8207   8632   9053   -847    203    247       C
ATOM   2371  CE1 TYR B  25     -33.917  -7.530  27.896  1.00 64.65           C
ANISOU 2371  CE1 TYR B  25     7886   8216   8463   -728     93    244       C
ATOM   2372  CE2 TYR B  25     -35.611  -8.936  28.899  1.00 69.11           C
ANISOU 2372  CE2 TYR B  25     8459   8719   9081   -835    209    245       C
ATOM   2373  CZ  TYR B  25     -34.294  -8.756  28.476  1.00 69.58           C
ANISOU 2373  CZ  TYR B  25     8577   8792   9066   -773    153    244       C
ATOM   2374  OH  TYR B  25     -33.394  -9.810  28.647  1.00 58.55           O
ANISOU 2374  OH  TYR B  25     7306   7360   7579   -757    162    243       O
ATOM   2375  N   THR B  26     -39.802  -4.203  26.950  1.00 61.17           N
ANISOU 2375  N   THR B  26     6833   7888   8521   -876     88    263       N
ATOM   2376  CA  THR B  26     -40.591  -2.973  26.909  1.00 62.07           C
ANISOU 2376  CA  THR B  26     6822   8037   8726   -856     86    270       C
ATOM   2377  C   THR B  26     -40.161  -2.086  28.070  1.00 61.06           C
ANISOU 2377  C   THR B  26     6714   7909   8577   -790    160    272       C
ATOM   2378  O   THR B  26     -40.315  -2.463  29.234  1.00 60.00           O
ANISOU 2378  O   THR B  26     6620   7746   8433   -797    254    270       O
ATOM   2379  CB  THR B  26     -42.103  -3.238  26.951  1.00 60.26           C
ANISOU 2379  CB  THR B  26     6485   7807   8605   -924    115    274       C
ATOM   2380  OG1 THR B  26     -42.414  -4.228  27.941  1.00 64.28           O
ANISOU 2380  OG1 THR B  26     7044   8275   9106   -967    210    270       O
ATOM   2381  CG2 THR B  26     -42.638  -3.676  25.581  1.00 57.31           C
ANISOU 2381  CG2 THR B  26     6058   7448   8270   -981     15    273       C
ATOM   2382  N   VAL B  27     -39.579  -0.929  27.749  1.00 57.06           N
ANISOU 2382  N   VAL B  27     6189   7432   8058   -728    116    273       N
ATOM   2383  CA  VAL B  27     -38.975  -0.039  28.737  1.00 60.03           C
ANISOU 2383  CA  VAL B  27     6599   7810   8401   -663    172    273       C
ATOM   2384  C   VAL B  27     -39.884   1.164  28.955  1.00 58.18           C
ANISOU 2384  C   VAL B  27     6251   7596   8257   -642    200    281       C
ATOM   2385  O   VAL B  27     -40.167   1.925  28.021  1.00 59.92           O
ANISOU 2385  O   VAL B  27     6394   7849   8525   -630    132    287       O
ATOM   2386  CB  VAL B  27     -37.577   0.420  28.299  1.00 57.88           C
ANISOU 2386  CB  VAL B  27     6395   7552   8045   -607    111    267       C
ATOM   2387  CG1 VAL B  27     -36.898   1.182  29.449  1.00 57.51           C
ANISOU 2387  CG1 VAL B  27     6396   7502   7955   -548    172    264       C
ATOM   2388  CG2 VAL B  27     -36.750  -0.774  27.808  1.00 55.39           C
ANISOU 2388  CG2 VAL B  27     6176   7219   7652   -627     69    261       C
ATOM   2389  N   VAL B  28     -40.291   1.371  30.195  1.00 53.74           N
ANISOU 2389  N   VAL B  28     5689   7015   7714   -634    302    282       N
ATOM   2390  CA  VAL B  28     -41.122   2.498  30.569  1.00 52.46           C
ANISOU 2390  CA  VAL B  28     5431   6868   7634   -609    346    291       C
ATOM   2391  C   VAL B  28     -40.241   3.341  31.478  1.00 53.62           C
ANISOU 2391  C   VAL B  28     5649   7008   7717   -543    391    286       C
ATOM   2392  O   VAL B  28     -39.859   2.881  32.560  1.00 54.72           O
ANISOU 2392  O   VAL B  28     5875   7115   7800   -540    464    281       O
ATOM   2393  CB  VAL B  28     -42.396   2.035  31.290  1.00 52.87           C
ANISOU 2393  CB  VAL B  28     5423   6898   7766   -656    437    295       C
ATOM   2394  CG1 VAL B  28     -43.385   3.210  31.518  1.00 57.64           C
ANISOU 2394  CG1 VAL B  28     5910   7521   8472   -630    478    306       C
ATOM   2395  CG2 VAL B  28     -43.009   0.802  30.609  1.00 55.26           C
ANISOU 2395  CG2 VAL B  28     5700   7195   8102   -734    403    294       C
ATOM   2396  N   ALA B  29     -39.864   4.552  31.044  1.00 53.28           N
ANISOU 2396  N   ALA B  29     5576   6993   7676   -491    346    288       N
ATOM   2397  CA  ALA B  29     -38.915   5.374  31.797  1.00 56.20           C
ANISOU 2397  CA  ALA B  29     6018   7358   7979   -433    376    281       C
ATOM   2398  C   ALA B  29     -39.572   6.696  32.179  1.00 58.47           C
ANISOU 2398  C   ALA B  29     6232   7653   8331   -395    423    289       C
ATOM   2399  O   ALA B  29     -39.374   7.717  31.506  1.00 60.35           O
ANISOU 2399  O   ALA B  29     6432   7917   8582   -358    369    291       O
ATOM   2400  CB  ALA B  29     -37.626   5.595  31.002  1.00 52.62           C
ANISOU 2400  CB  ALA B  29     5620   6924   7449   -403    286    273       C
ATOM   2401  N   PRO B  30     -40.321   6.729  33.278  1.00 55.49           N
ANISOU 2401  N   PRO B  30     5843   7251   7991   -401    528    292       N
ATOM   2402  CA  PRO B  30     -40.980   7.978  33.677  1.00 58.22           C
ANISOU 2402  CA  PRO B  30     6122   7600   8400   -362    581    300       C
ATOM   2403  C   PRO B  30     -39.968   9.078  33.979  1.00 62.26           C
ANISOU 2403  C   PRO B  30     6697   8115   8844   -302    575    293       C
ATOM   2404  O   PRO B  30     -38.795   8.836  34.280  1.00 60.69           O
ANISOU 2404  O   PRO B  30     6603   7909   8548   -290    558    280       O
ATOM   2405  CB  PRO B  30     -41.758   7.585  34.941  1.00 55.69           C
ANISOU 2405  CB  PRO B  30     5809   7242   8109   -383    706    303       C
ATOM   2406  CG  PRO B  30     -40.981   6.413  35.483  1.00 55.59           C
ANISOU 2406  CG  PRO B  30     5916   7203   8003   -409    719    292       C
ATOM   2407  CD  PRO B  30     -40.529   5.657  34.258  1.00 54.01           C
ANISOU 2407  CD  PRO B  30     5715   7026   7781   -438    609    289       C
ATOM   2408  N   THR B  31     -40.440  10.311  33.881  1.00 65.67           N
ANISOU 2408  N   THR B  31     7063   8559   9332   -263    587    301       N
ATOM   2409  CA  THR B  31     -39.616  11.445  34.251  1.00 68.78           C
ANISOU 2409  CA  THR B  31     7513   8951   9670   -209    594    293       C
ATOM   2410  C   THR B  31     -39.862  11.810  35.711  1.00 70.09           C
ANISOU 2410  C   THR B  31     7724   9080   9826   -192    714    291       C
ATOM   2411  O   THR B  31     -40.789  11.308  36.352  1.00 68.47           O
ANISOU 2411  O   THR B  31     7491   8853   9672   -217    794    298       O
ATOM   2412  CB  THR B  31     -39.919  12.618  33.328  1.00 67.55           C
ANISOU 2412  CB  THR B  31     7274   8822   9569   -174    542    303       C
ATOM   2413  OG1 THR B  31     -40.086  12.113  31.998  1.00 68.85           O
ANISOU 2413  OG1 THR B  31     7381   9016   9765   -201    443    308       O
ATOM   2414  CG2 THR B  31     -38.774  13.597  33.321  1.00 61.26           C
ANISOU 2414  CG2 THR B  31     6548   8030   8698   -129    514    291       C
ATOM   2415  N   HIS B  32     -39.015  12.706  36.237  1.00 73.51           N
ANISOU 2415  N   HIS B  32     8230   9505  10193   -149    727    281       N
ATOM   2416  CA  HIS B  32     -39.160  13.142  37.627  1.00 73.06           C
ANISOU 2416  CA  HIS B  32     8231   9411  10117   -130    838    277       C
ATOM   2417  C   HIS B  32     -40.484  13.862  37.833  1.00 70.95           C
ANISOU 2417  C   HIS B  32     7869   9134   9954   -114    914    293       C
ATOM   2418  O   HIS B  32     -41.094  13.764  38.903  1.00 69.93           O
ANISOU 2418  O   HIS B  32     7758   8970   9843   -118   1022    296       O
ATOM   2419  CB  HIS B  32     -37.983  14.029  38.043  1.00 66.95           C
ANISOU 2419  CB  HIS B  32     7551   8633   9254    -90    826    262       C
ATOM   2420  N   GLY B  33     -40.913  14.635  36.835  1.00 71.92           N
ANISOU 2420  N   GLY B  33     7896   9286  10144    -93    861    304       N
ATOM   2421  CA  GLY B  33     -42.227  15.243  36.891  1.00 73.41           C
ANISOU 2421  CA  GLY B  33     7979   9471  10442    -76    923    322       C
ATOM   2422  C   GLY B  33     -43.353  14.251  36.685  1.00 75.14           C
ANISOU 2422  C   GLY B  33     8105   9695  10750   -124    941    334       C
ATOM   2423  O   GLY B  33     -44.413  14.378  37.300  1.00 83.16           O
ANISOU 2423  O   GLY B  33     9063  10691  11842   -123   1036    345       O
ATOM   2424  N   GLU B  34     -43.131  13.235  35.847  1.00 77.59           N
ANISOU 2424  N   GLU B  34     8402  10028  11050   -167    854    332       N
ATOM   2425  CA  GLU B  34     -44.178  12.260  35.533  1.00 72.82           C
ANISOU 2425  CA  GLU B  34     7709   9430  10530   -220    859    341       C
ATOM   2426  C   GLU B  34     -44.497  11.344  36.712  1.00 73.87           C
ANISOU 2426  C   GLU B  34     7891   9523  10652   -257    967    337       C
ATOM   2427  O   GLU B  34     -45.637  10.880  36.845  1.00 78.86           O
ANISOU 2427  O   GLU B  34     8438  10149  11374   -291   1021    346       O
ATOM   2428  CB  GLU B  34     -43.767  11.431  34.313  1.00 73.04           C
ANISOU 2428  CB  GLU B  34     7726   9489  10538   -257    736    338       C
ATOM   2429  CG  GLU B  34     -44.135  12.067  32.980  1.00 76.34           C
ANISOU 2429  CG  GLU B  34     8041   9946  11019   -240    639    349       C
ATOM   2430  CD  GLU B  34     -43.196  11.664  31.849  1.00 72.87           C
ANISOU 2430  CD  GLU B  34     7642   9530  10514   -253    514    342       C
ATOM   2431  OE1 GLU B  34     -43.266  12.295  30.776  1.00 74.30           O
ANISOU 2431  OE1 GLU B  34     7766   9739  10724   -231    431    349       O
ATOM   2432  OE2 GLU B  34     -42.384  10.728  32.027  1.00 68.18           O
ANISOU 2432  OE2 GLU B  34     7139   8924   9840   -283    501    328       O
ATOM   2433  N   LEU B  35     -43.516  11.047  37.559  1.00 75.74           N
ANISOU 2433  N   LEU B  35     8264   9732  10781   -254    998    322       N
ATOM   2434  CA  LEU B  35     -43.701  10.110  38.666  1.00 70.63           C
ANISOU 2434  CA  LEU B  35     7686   9043  10109   -289   1095    317       C
ATOM   2435  C   LEU B  35     -42.863  10.663  39.809  1.00 70.40           C
ANISOU 2435  C   LEU B  35     7785   8980   9983   -249   1155    306       C
ATOM   2436  O   LEU B  35     -41.635  10.547  39.802  1.00 67.91           O
ANISOU 2436  O   LEU B  35     7569   8669   9565   -237   1097    293       O
ATOM   2437  CB  LEU B  35     -43.294   8.688  38.289  1.00 64.96           C
ANISOU 2437  CB  LEU B  35     7011   8326   9346   -343   1041    310       C
ATOM   2438  N   ASP B  36     -43.530  11.287  40.773  1.00 62.72           N
ANISOU 2438  N   ASP B  36     6809   7976   9047   -227   1270    311       N
ATOM   2439  CA  ASP B  36     -42.831  11.914  41.882  1.00 66.66           C
ANISOU 2439  CA  ASP B  36     7429   8440   9458   -189   1331    301       C
ATOM   2440  C   ASP B  36     -42.672  10.847  42.961  1.00 72.32           C
ANISOU 2440  C   ASP B  36     8255   9112  10111   -221   1405    294       C
ATOM   2441  O   ASP B  36     -43.657  10.363  43.536  1.00 69.48           O
ANISOU 2441  O   ASP B  36     7869   8722   9809   -249   1505    301       O
ATOM   2442  CB  ASP B  36     -43.567  13.118  42.452  1.00 69.67           C
ANISOU 2442  CB  ASP B  36     7772   8801   9897   -147   1425    310       C
ATOM   2443  CG  ASP B  36     -42.606  14.090  43.100  1.00 74.69           C
ANISOU 2443  CG  ASP B  36     8520   9420  10439   -100   1434    297       C
ATOM   2444  OD1 ASP B  36     -42.126  14.983  42.351  1.00 79.48           O
ANISOU 2444  OD1 ASP B  36     9100  10058  11040    -68   1356    296       O
ATOM   2445  OD2 ASP B  36     -42.152  13.832  44.242  1.00 71.70           O
ANISOU 2445  OD2 ASP B  36     8266   8999   9978   -102   1500    287       O
ATOM   2446  N   LEU B  37     -41.424  10.529  43.255  1.00 81.84           N
ANISOU 2446  N   LEU B  37     9586  10312  11199   -215   1359    279       N
ATOM   2447  CA  LEU B  37     -41.005   9.426  44.095  1.00 78.47           C
ANISOU 2447  CA  LEU B  37     9277   9848  10692   -241   1397    272       C
ATOM   2448  C   LEU B  37     -41.402   9.608  45.548  1.00 76.49           C
ANISOU 2448  C   LEU B  37     9106   9538  10419   -232   1535    271       C
ATOM   2449  O   LEU B  37     -41.567   8.609  46.262  1.00 76.50           O
ANISOU 2449  O   LEU B  37     9177   9500  10390   -263   1598    270       O
ATOM   2450  CB  LEU B  37     -39.508   9.391  43.846  1.00 80.93           C
ANISOU 2450  CB  LEU B  37     9678  10179  10891   -221   1293    258       C
ATOM   2451  CG  LEU B  37     -39.537   8.758  42.459  1.00 79.30           C
ANISOU 2451  CG  LEU B  37     9383  10018  10729   -250   1190    262       C
ATOM   2452  CD1 LEU B  37     -39.094   9.433  41.165  1.00 84.62           C
ANISOU 2452  CD1 LEU B  37     9984  10745  11423   -231   1074    262       C
ATOM   2453  CD2 LEU B  37     -38.122   8.221  42.814  1.00 78.62           C
ANISOU 2453  CD2 LEU B  37     9432   9925  10513   -240   1138    248       C
ATOM   2454  N   THR B  38     -41.648  10.852  45.969  1.00 72.15           N
ANISOU 2454  N   THR B  38     8547   8977   9890   -191   1588    272       N
ATOM   2455  CA  THR B  38     -42.115  11.183  47.313  1.00 67.71           C
ANISOU 2455  CA  THR B  38     8056   8357   9315   -179   1727    273       C
ATOM   2456  C   THR B  38     -43.623  10.990  47.494  1.00 63.97           C
ANISOU 2456  C   THR B  38     7483   7861   8960   -203   1839    288       C
ATOM   2457  O   THR B  38     -44.103  11.030  48.635  1.00 59.91           O
ANISOU 2457  O   THR B  38     7032   7292   8441   -201   1968    289       O
ATOM   2458  CB  THR B  38     -41.721  12.634  47.633  1.00 69.77           C
ANISOU 2458  CB  THR B  38     8349   8614   9546   -124   1736    267       C
ATOM   2459  OG1 THR B  38     -42.641  13.540  47.011  1.00 69.49           O
ANISOU 2459  OG1 THR B  38     8177   8601   9626   -104   1752    281       O
ATOM   2460  CG2 THR B  38     -40.314  12.922  47.101  1.00 67.95           C
ANISOU 2460  CG2 THR B  38     8172   8421   9226   -104   1605    253       C
ATOM   2461  N   ASP B  39     -44.373  10.729  46.415  1.00 62.08           N
ANISOU 2461  N   ASP B  39     7095   7663   8830   -228   1794    299       N
ATOM   2462  CA  ASP B  39     -45.818  10.499  46.502  1.00 63.99           C
ANISOU 2462  CA  ASP B  39     7226   7890   9195   -256   1891    314       C
ATOM   2463  C   ASP B  39     -46.065   8.995  46.446  1.00 63.50           C
ANISOU 2463  C   ASP B  39     7171   7819   9138   -322   1896    313       C
ATOM   2464  O   ASP B  39     -46.098   8.398  45.363  1.00 59.67           O
ANISOU 2464  O   ASP B  39     6607   7376   8689   -355   1798    315       O
ATOM   2465  CB  ASP B  39     -46.559  11.220  45.380  1.00 66.94           C
ANISOU 2465  CB  ASP B  39     7427   8315   9692   -242   1838    327       C
ATOM   2466  N   ARG B  40     -46.294   8.399  47.624  1.00 59.95           N
ANISOU 2466  N   ARG B  40     6818   7308   8652   -342   2015    310       N
ATOM   2467  CA  ARG B  40     -46.443   6.951  47.713  1.00 61.92           C
ANISOU 2467  CA  ARG B  40     7101   7538   8889   -404   2031    308       C
ATOM   2468  C   ARG B  40     -47.621   6.469  46.885  1.00 58.84           C
ANISOU 2468  C   ARG B  40     6546   7175   8637   -455   2030    318       C
ATOM   2469  O   ARG B  40     -47.461   5.608  46.012  1.00 57.65           O
ANISOU 2469  O   ARG B  40     6360   7053   8489   -496   1938    316       O
ATOM   2470  CB  ARG B  40     -46.612   6.522  49.173  1.00 56.63           C
ANISOU 2470  CB  ARG B  40     6562   6792   8164   -414   2175    304       C
ATOM   2471  CG  ARG B  40     -46.875   5.028  49.352  1.00 56.28           C
ANISOU 2471  CG  ARG B  40     6557   6717   8110   -480   2210    303       C
ATOM   2472  CD  ARG B  40     -47.154   4.720  50.818  1.00 64.12           C
ANISOU 2472  CD  ARG B  40     7677   7629   9056   -486   2366    301       C
ATOM   2473  NE  ARG B  40     -46.858   3.339  51.204  1.00 69.01           N
ANISOU 2473  NE  ARG B  40     8410   8210   9602   -531   2383    296       N
ATOM   2474  CZ  ARG B  40     -46.520   2.973  52.440  1.00 70.14           C
ANISOU 2474  CZ  ARG B  40     8722   8285   9645   -525   2472    291       C
ATOM   2475  NH1 ARG B  40     -46.405   3.890  53.402  1.00 70.03           N
ANISOU 2475  NH1 ARG B  40     8785   8235   9587   -477   2548    290       N
ATOM   2476  NH2 ARG B  40     -46.278   1.700  52.717  1.00 66.37           N
ANISOU 2476  NH2 ARG B  40     8343   7772   9103   -565   2483    288       N
ATOM   2477  N   GLU B  41     -48.780   7.114  47.052  1.00 59.56           N
ANISOU 2477  N   GLU B  41     6524   7261   8844   -448   2121    329       N
ATOM   2478  CA  GLU B  41     -49.989   6.650  46.381  1.00 57.06           C
ANISOU 2478  CA  GLU B  41     6046   6968   8667   -499   2131    339       C
ATOM   2479  C   GLU B  41     -49.787   6.586  44.875  1.00 54.46           C
ANISOU 2479  C   GLU B  41     5612   6709   8373   -510   1969    341       C
ATOM   2480  O   GLU B  41     -50.132   5.584  44.243  1.00 51.65           O
ANISOU 2480  O   GLU B  41     5200   6368   8056   -571   1926    340       O
ATOM   2481  CB  GLU B  41     -51.180   7.556  46.722  1.00 51.21           C
ANISOU 2481  CB  GLU B  41     5190   6219   8049   -475   2241    353       C
ATOM   2482  N   LYS B  42     -49.217   7.632  44.273  1.00 55.01           N
ANISOU 2482  N   LYS B  42     5660   6818   8425   -452   1878    343       N
ATOM   2483  CA  LYS B  42     -49.180   7.617  42.817  1.00 56.42           C
ANISOU 2483  CA  LYS B  42     5730   7059   8649   -463   1733    346       C
ATOM   2484  C   LYS B  42     -48.285   6.482  42.305  1.00 55.13           C
ANISOU 2484  C   LYS B  42     5646   6905   8397   -503   1635    335       C
ATOM   2485  O   LYS B  42     -48.663   5.758  41.373  1.00 53.33           O
ANISOU 2485  O   LYS B  42     5336   6705   8221   -554   1565    336       O
ATOM   2486  CB  LYS B  42     -48.715   8.962  42.227  1.00 56.25           C
ANISOU 2486  CB  LYS B  42     5675   7075   8621   -393   1654    350       C
ATOM   2487  CG  LYS B  42     -49.142   9.022  40.744  1.00 55.91           C
ANISOU 2487  CG  LYS B  42     5485   7094   8666   -407   1532    359       C
ATOM   2488  CD  LYS B  42     -48.505  10.051  39.827  1.00 56.55           C
ANISOU 2488  CD  LYS B  42     5544   7218   8727   -352   1417    361       C
ATOM   2489  CE  LYS B  42     -48.894  11.507  39.949  1.00 60.16           C
ANISOU 2489  CE  LYS B  42     5942   7679   9236   -284   1454    372       C
ATOM   2490  NZ  LYS B  42     -48.205  12.155  38.753  1.00 60.84           N
ANISOU 2490  NZ  LYS B  42     6008   7812   9296   -251   1311    373       N
ATOM   2491  N   ILE B  43     -47.109   6.279  42.925  1.00 56.76           N
ANISOU 2491  N   ILE B  43     6014   7084   8467   -484   1631    323       N
ATOM   2492  CA  ILE B  43     -46.161   5.293  42.364  1.00 53.47           C
ANISOU 2492  CA  ILE B  43     5671   6679   7964   -511   1529    313       C
ATOM   2493  C   ILE B  43     -46.572   3.847  42.665  1.00 56.96           C
ANISOU 2493  C   ILE B  43     6147   7087   8407   -582   1580    310       C
ATOM   2494  O   ILE B  43     -46.353   2.957  41.829  1.00 57.68           O
ANISOU 2494  O   ILE B  43     6230   7198   8488   -623   1495    307       O
ATOM   2495  CB  ILE B  43     -44.686   5.555  42.736  1.00 49.23           C
ANISOU 2495  CB  ILE B  43     5283   6136   7288   -464   1483    302       C
ATOM   2496  CG1 ILE B  43     -43.853   4.689  41.808  1.00 54.51           C
ANISOU 2496  CG1 ILE B  43     5982   6830   7898   -487   1360    295       C
ATOM   2497  CG2 ILE B  43     -44.341   5.163  44.168  1.00 50.49           C
ANISOU 2497  CG2 ILE B  43     5592   6234   7359   -460   1588    295       C
ATOM   2498  CD1 ILE B  43     -42.556   5.242  41.428  1.00 53.81           C
ANISOU 2498  CD1 ILE B  43     5955   6769   7721   -439   1262    288       C
ATOM   2499  N   ILE B  44     -47.151   3.565  43.838  1.00 55.94           N
ANISOU 2499  N   ILE B  44     6064   6903   8286   -598   1721    311       N
ATOM   2500  CA  ILE B  44     -47.716   2.229  44.015  1.00 56.59           C
ANISOU 2500  CA  ILE B  44     6158   6955   8390   -672   1774    310       C
ATOM   2501  C   ILE B  44     -48.733   1.916  42.912  1.00 57.96           C
ANISOU 2501  C   ILE B  44     6163   7168   8692   -727   1726    316       C
ATOM   2502  O   ILE B  44     -48.694   0.839  42.306  1.00 58.96           O
ANISOU 2502  O   ILE B  44     6291   7300   8811   -783   1671    311       O
ATOM   2503  CB  ILE B  44     -48.290   2.048  45.440  1.00 54.01           C
ANISOU 2503  CB  ILE B  44     5899   6560   8062   -682   1943    310       C
ATOM   2504  CG1 ILE B  44     -48.997   0.708  45.549  1.00 53.87           C
ANISOU 2504  CG1 ILE B  44     5878   6511   8081   -765   2003    309       C
ATOM   2505  CG2 ILE B  44     -49.184   3.172  45.873  1.00 56.45           C
ANISOU 2505  CG2 ILE B  44     6117   6866   8465   -651   2036    319       C
ATOM   2506  CD1 ILE B  44     -48.143  -0.473  45.282  1.00 62.66           C
ANISOU 2506  CD1 ILE B  44     7101   7613   9093   -795   1933    300       C
ATOM   2507  N   SER B  45     -49.602   2.867  42.579  1.00 53.97           N
ANISOU 2507  N   SER B  45     5511   6694   8302   -708   1737    326       N
ATOM   2508  CA  SER B  45     -50.586   2.620  41.525  1.00 57.74           C
ANISOU 2508  CA  SER B  45     5821   7212   8905   -757   1684    332       C
ATOM   2509  C   SER B  45     -49.914   2.437  40.165  1.00 60.22           C
ANISOU 2509  C   SER B  45     6117   7578   9188   -761   1515    329       C
ATOM   2510  O   SER B  45     -50.234   1.496  39.429  1.00 63.39           O
ANISOU 2510  O   SER B  45     6473   7991   9621   -827   1460    326       O
ATOM   2511  CB  SER B  45     -51.614   3.753  41.491  1.00 55.70           C
ANISOU 2511  CB  SER B  45     5413   6976   8773   -725   1729    346       C
ATOM   2512  OG  SER B  45     -52.266   3.861  42.751  1.00 53.28           O
ANISOU 2512  OG  SER B  45     5127   6619   8498   -724   1894    348       O
ATOM   2513  N   GLU B  46     -48.974   3.321  39.812  1.00 60.03           N
ANISOU 2513  N   GLU B  46     6129   7580   9099   -694   1433    329       N
ATOM   2514  CA  GLU B  46     -48.336   3.222  38.500  1.00 62.53           C
ANISOU 2514  CA  GLU B  46     6428   7943   9388   -695   1278    326       C
ATOM   2515  C   GLU B  46     -47.488   1.954  38.395  1.00 58.93           C
ANISOU 2515  C   GLU B  46     6094   7467   8830   -734   1236    315       C
ATOM   2516  O   GLU B  46     -47.447   1.309  37.339  1.00 58.47           O
ANISOU 2516  O   GLU B  46     6002   7433   8779   -775   1138    313       O
ATOM   2517  CB  GLU B  46     -47.498   4.476  38.225  1.00 60.37           C
ANISOU 2517  CB  GLU B  46     6174   7697   9067   -615   1213    328       C
ATOM   2518  CG  GLU B  46     -48.319   5.772  38.184  1.00 64.10           C
ANISOU 2518  CG  GLU B  46     6524   8190   9640   -571   1243    341       C
ATOM   2519  CD  GLU B  46     -48.699   6.192  36.750  1.00 71.01           C
ANISOU 2519  CD  GLU B  46     7266   9122  10593   -569   1121    350       C
ATOM   2520  OE1 GLU B  46     -47.964   5.792  35.807  1.00 69.73           O
ANISOU 2520  OE1 GLU B  46     7136   8984  10375   -581   1003    344       O
ATOM   2521  OE2 GLU B  46     -49.726   6.910  36.569  1.00 67.12           O
ANISOU 2521  OE2 GLU B  46     6640   8649  10214   -554   1143    363       O
ATOM   2522  N   VAL B  47     -46.816   1.569  39.480  1.00 55.67           N
ANISOU 2522  N   VAL B  47     5828   7008   8318   -722   1308    308       N
ATOM   2523  CA  VAL B  47     -46.057   0.324  39.456  1.00 60.78           C
ANISOU 2523  CA  VAL B  47     6593   7631   8869   -756   1278    298       C
ATOM   2524  C   VAL B  47     -46.979  -0.863  39.186  1.00 65.20           C
ANISOU 2524  C   VAL B  47     7104   8176   9494   -843   1303    298       C
ATOM   2525  O   VAL B  47     -46.644  -1.763  38.399  1.00 64.57           O
ANISOU 2525  O   VAL B  47     7048   8104   9383   -883   1222    293       O
ATOM   2526  CB  VAL B  47     -45.271   0.141  40.770  1.00 59.95           C
ANISOU 2526  CB  VAL B  47     6652   7475   8652   -725   1359    293       C
ATOM   2527  CG1 VAL B  47     -44.760  -1.278  40.885  1.00 58.00           C
ANISOU 2527  CG1 VAL B  47     6520   7194   8322   -767   1353    286       C
ATOM   2528  CG2 VAL B  47     -44.057   1.046  40.783  1.00 48.47           C
ANISOU 2528  CG2 VAL B  47     5265   6042   7111   -649   1295    289       C
ATOM   2529  N   THR B  48     -48.171  -0.865  39.796  1.00 61.64           N
ANISOU 2529  N   THR B  48     6580   7703   9137   -877   1415    303       N
ATOM   2530  CA  THR B  48     -49.088  -1.982  39.601  1.00 62.72           C
ANISOU 2530  CA  THR B  48     6667   7824   9341   -966   1447    300       C
ATOM   2531  C   THR B  48     -49.617  -2.055  38.174  1.00 64.89           C
ANISOU 2531  C   THR B  48     6802   8152   9702  -1005   1332    302       C
ATOM   2532  O   THR B  48     -49.828  -3.158  37.647  1.00 63.33           O
ANISOU 2532  O   THR B  48     6606   7947   9510  -1077   1298    296       O
ATOM   2533  CB  THR B  48     -50.256  -1.854  40.573  1.00 64.18           C
ANISOU 2533  CB  THR B  48     6795   7976   9616   -989   1598    305       C
ATOM   2534  OG1 THR B  48     -49.754  -1.486  41.860  1.00 61.34           O
ANISOU 2534  OG1 THR B  48     6558   7570   9177   -938   1698    304       O
ATOM   2535  CG2 THR B  48     -50.989  -3.178  40.695  1.00 62.60           C
ANISOU 2535  CG2 THR B  48     6592   7740   9453  -1084   1658    299       C
ATOM   2536  N   LYS B  49     -49.784  -0.903  37.520  1.00 69.78           N
ANISOU 2536  N   LYS B  49     7311   8821  10380   -959   1265    311       N
ATOM   2537  CA  LYS B  49     -50.341  -0.870  36.171  1.00 71.90           C
ANISOU 2537  CA  LYS B  49     7445   9142  10734   -991   1152    314       C
ATOM   2538  C   LYS B  49     -49.328  -1.322  35.126  1.00 67.84           C
ANISOU 2538  C   LYS B  49     6998   8647  10131   -993   1014    307       C
ATOM   2539  O   LYS B  49     -49.637  -2.160  34.266  1.00 65.98           O
ANISOU 2539  O   LYS B  49     6727   8421   9921  -1058    947    303       O
ATOM   2540  CB  LYS B  49     -50.879   0.535  35.868  1.00 72.84           C
ANISOU 2540  CB  LYS B  49     7430   9303  10944   -935   1132    327       C
ATOM   2541  CG  LYS B  49     -52.349   0.688  36.249  1.00 67.46           C
ANISOU 2541  CG  LYS B  49     6606   8620  10405   -967   1226    335       C
ATOM   2542  CD  LYS B  49     -52.524   0.537  37.760  1.00 70.35           C
ANISOU 2542  CD  LYS B  49     7048   8929  10754   -966   1394    333       C
ATOM   2543  CE  LYS B  49     -53.937   0.151  38.188  1.00 70.87           C
ANISOU 2543  CE  LYS B  49     7000   8978  10948  -1028   1502    336       C
ATOM   2544  NZ  LYS B  49     -53.913  -0.491  39.535  1.00 63.61           N
ANISOU 2544  NZ  LYS B  49     6198   7991   9980  -1051   1652    329       N
ATOM   2545  N   ILE B  50     -48.116  -0.766  35.177  1.00 65.34           N
ANISOU 2545  N   ILE B  50     6779   8335   9713   -922    972    306       N
ATOM   2546  CA  ILE B  50     -47.066  -1.212  34.262  1.00 63.80           C
ANISOU 2546  CA  ILE B  50     6658   8153   9427   -919    853    300       C
ATOM   2547  C   ILE B  50     -46.719  -2.679  34.523  1.00 56.48           C
ANISOU 2547  C   ILE B  50     5847   7183   8429   -976    878    290       C
ATOM   2548  O   ILE B  50     -46.365  -3.419  33.593  1.00 52.10           O
ANISOU 2548  O   ILE B  50     5318   6637   7841  -1010    788    285       O
ATOM   2549  CB  ILE B  50     -45.841  -0.271  34.374  1.00 58.20           C
ANISOU 2549  CB  ILE B  50     6027   7457   8629   -832    816    299       C
ATOM   2550  CG1 ILE B  50     -46.286   1.191  34.195  1.00 52.59           C
ANISOU 2550  CG1 ILE B  50     5205   6783   7994   -778    806    310       C
ATOM   2551  CG2 ILE B  50     -44.788  -0.630  33.338  1.00 52.17           C
ANISOU 2551  CG2 ILE B  50     5326   6713   7785   -826    693    294       C
ATOM   2552  CD1 ILE B  50     -45.305   2.236  34.691  1.00 53.90           C
ANISOU 2552  CD1 ILE B  50     5444   6951   8086   -696    813    309       C
ATOM   2553  N   ASN B  51     -46.849  -3.116  35.777  1.00 56.61           N
ANISOU 2553  N   ASN B  51     5937   7151   8421   -986   1002    288       N
ATOM   2554  CA  ASN B  51     -46.481  -4.464  36.216  1.00 53.07           C
ANISOU 2554  CA  ASN B  51     5616   6652   7895  -1031   1042    280       C
ATOM   2555  C   ASN B  51     -45.103  -4.827  35.735  1.00 52.04           C
ANISOU 2555  C   ASN B  51     5604   6525   7643   -998    951    275       C
ATOM   2556  O   ASN B  51     -44.953  -5.837  34.937  1.00 49.68           O
ANISOU 2556  O   ASN B  51     5334   6222   7321  -1049    887    269       O
ATOM   2557  CB  ASN B  51     -47.515  -5.500  35.812  1.00 55.66           C
ANISOU 2557  CB  ASN B  51     5882   6968   8298  -1129   1055    276       C
ATOM   2558  CG  ASN B  51     -47.663  -6.572  36.859  1.00 50.89           C
ANISOU 2558  CG  ASN B  51     5382   6298   7655  -1173   1172    271       C
ATOM   2559  OD1 ASN B  51     -47.699  -6.274  38.066  1.00 53.64           O
ANISOU 2559  OD1 ASN B  51     5781   6614   7986  -1143   1284    273       O
ATOM   2560  ND2 ASN B  51     -47.700  -7.822  36.425  1.00 44.64           N
ANISOU 2560  ND2 ASN B  51     4637   5484   6841  -1242   1150    264       N
ATOM   2561  N   PRO B  52     -44.060  -4.129  36.114  1.00 56.48           N
ANISOU 2561  N   PRO B  52     6241   7093   8126   -921    937    275       N
ATOM   2562  CA  PRO B  52     -42.722  -4.441  35.614  1.00 55.79           C
ANISOU 2562  CA  PRO B  52     6256   7012   7929   -887    848    270       C
ATOM   2563  C   PRO B  52     -42.202  -5.728  36.232  1.00 50.11           C
ANISOU 2563  C   PRO B  52     5681   6240   7118   -909    894    265       C
ATOM   2564  O   PRO B  52     -42.438  -6.021  37.407  1.00 46.25           O
ANISOU 2564  O   PRO B  52     5255   5708   6613   -914   1002    265       O
ATOM   2565  CB  PRO B  52     -41.889  -3.216  36.021  1.00 53.23           C
ANISOU 2565  CB  PRO B  52     5956   6709   7560   -801    838    271       C
ATOM   2566  CG  PRO B  52     -42.592  -2.669  37.225  1.00 52.93           C
ANISOU 2566  CG  PRO B  52     5899   6647   7564   -790    958    275       C
ATOM   2567  CD  PRO B  52     -44.055  -2.993  37.062  1.00 52.39           C
ANISOU 2567  CD  PRO B  52     5717   6575   7615   -860   1007    279       C
ATOM   2568  N   GLN B  53     -41.553  -6.535  35.392  1.00 50.76           N
ANISOU 2568  N   GLN B  53     5818   6324   7145   -925    812    261       N
ATOM   2569  CA  GLN B  53     -40.802  -7.688  35.880  1.00 48.60           C
ANISOU 2569  CA  GLN B  53     5695   6002   6768   -928    839    258       C
ATOM   2570  C   GLN B  53     -39.488  -7.269  36.539  1.00 46.34           C
ANISOU 2570  C   GLN B  53     5517   5714   6376   -844    833    258       C
ATOM   2571  O   GLN B  53     -39.044  -7.919  37.493  1.00 46.47           O
ANISOU 2571  O   GLN B  53     5656   5685   6315   -831    894    257       O
ATOM   2572  CB  GLN B  53     -40.561  -8.659  34.738  1.00 45.48           C
ANISOU 2572  CB  GLN B  53     5322   5608   6351   -971    756    254       C
ATOM   2573  CG  GLN B  53     -41.757  -9.548  34.453  1.00 50.20           C
ANISOU 2573  CG  GLN B  53     5870   6183   7022  -1067    788    252       C
ATOM   2574  CD  GLN B  53     -42.908  -8.788  33.813  1.00 54.52           C
ANISOU 2574  CD  GLN B  53     6244   6773   7698  -1102    763    254       C
ATOM   2575  OE1 GLN B  53     -42.773  -8.248  32.711  1.00 56.80           O
ANISOU 2575  OE1 GLN B  53     6462   7107   8012  -1089    659    255       O
ATOM   2576  NE2 GLN B  53     -44.046  -8.730  34.504  1.00 50.82           N
ANISOU 2576  NE2 GLN B  53     5709   6289   7313  -1143    858    255       N
ATOM   2577  N   ILE B  54     -38.844  -6.208  36.045  1.00 40.72           N
ANISOU 2577  N   ILE B  54     4764   5050   5659   -786    758    258       N
ATOM   2578  CA  ILE B  54     -37.562  -5.742  36.570  1.00 46.90           C
ANISOU 2578  CA  ILE B  54     5635   5837   6347   -709    740    256       C
ATOM   2579  C   ILE B  54     -37.596  -4.230  36.761  1.00 46.45           C
ANISOU 2579  C   ILE B  54     5504   5817   6329   -660    738    256       C
ATOM   2580  O   ILE B  54     -38.131  -3.504  35.914  1.00 49.86           O
ANISOU 2580  O   ILE B  54     5818   6288   6840   -669    692    259       O
ATOM   2581  CB  ILE B  54     -36.399  -6.143  35.636  1.00 43.16           C
ANISOU 2581  CB  ILE B  54     5214   5382   5804   -685    637    253       C
ATOM   2582  CG1 ILE B  54     -36.357  -7.660  35.481  1.00 44.67           C
ANISOU 2582  CG1 ILE B  54     5489   5532   5951   -730    645    253       C
ATOM   2583  CG2 ILE B  54     -35.070  -5.661  36.191  1.00 43.81           C
ANISOU 2583  CG2 ILE B  54     5379   5473   5795   -606    618    250       C
ATOM   2584  CD1 ILE B  54     -35.614  -8.110  34.271  1.00 46.50           C
ANISOU 2584  CD1 ILE B  54     5739   5782   6148   -727    546    251       C
ATOM   2585  N   ILE B  55     -37.003  -3.746  37.852  1.00 42.30           N
ANISOU 2585  N   ILE B  55     5052   5278   5744   -608    784    255       N
ATOM   2586  CA  ILE B  55     -36.881  -2.309  38.094  1.00 46.69           C
ANISOU 2586  CA  ILE B  55     5557   5863   6320   -558    783    254       C
ATOM   2587  C   ILE B  55     -35.406  -1.947  38.270  1.00 48.00           C
ANISOU 2587  C   ILE B  55     5808   6043   6387   -493    728    247       C
ATOM   2588  O   ILE B  55     -34.726  -2.496  39.145  1.00 45.89           O
ANISOU 2588  O   ILE B  55     5658   5744   6033   -472    758    245       O
ATOM   2589  CB  ILE B  55     -37.695  -1.856  39.313  1.00 46.36           C
ANISOU 2589  CB  ILE B  55     5511   5791   6312   -559    899    256       C
ATOM   2590  CG1 ILE B  55     -39.192  -1.888  38.981  1.00 41.41           C
ANISOU 2590  CG1 ILE B  55     4763   5165   5807   -617    943    263       C
ATOM   2591  CG2 ILE B  55     -37.209  -0.463  39.763  1.00 45.61           C
ANISOU 2591  CG2 ILE B  55     5412   5717   6201   -496    898    253       C
ATOM   2592  CD1 ILE B  55     -40.087  -1.651  40.187  1.00 43.91           C
ANISOU 2592  CD1 ILE B  55     5079   5444   6162   -627   1072    266       C
ATOM   2593  N   ILE B  56     -34.918  -1.016  37.452  1.00 46.23           N
ANISOU 2593  N   ILE B  56     5524   5866   6176   -462    648    245       N
ATOM   2594  CA  ILE B  56     -33.548  -0.542  37.536  1.00 44.68           C
ANISOU 2594  CA  ILE B  56     5389   5688   5898   -403    594    237       C
ATOM   2595  C   ILE B  56     -33.576   0.877  38.094  1.00 45.29           C
ANISOU 2595  C   ILE B  56     5435   5780   5993   -365    620    234       C
ATOM   2596  O   ILE B  56     -33.988   1.820  37.414  1.00 47.55           O
ANISOU 2596  O   ILE B  56     5623   6098   6346   -362    592    236       O
ATOM   2597  CB  ILE B  56     -32.846  -0.609  36.182  1.00 45.67           C
ANISOU 2597  CB  ILE B  56     5487   5851   6016   -397    487    235       C
ATOM   2598  CG1 ILE B  56     -32.885  -2.054  35.664  1.00 41.14           C
ANISOU 2598  CG1 ILE B  56     4952   5255   5423   -438    468    238       C
ATOM   2599  CG2 ILE B  56     -31.423  -0.100  36.321  1.00 42.71           C
ANISOU 2599  CG2 ILE B  56     5170   5496   5562   -338    437    226       C
ATOM   2600  CD1 ILE B  56     -32.309  -2.217  34.303  1.00 39.97           C
ANISOU 2600  CD1 ILE B  56     4781   5136   5269   -438    371    237       C
ATOM   2601  N   HIS B  57     -33.127   1.021  39.334  1.00 45.12           N
ANISOU 2601  N   HIS B  57     5503   5734   5908   -335    673    229       N
ATOM   2602  CA  HIS B  57     -33.176   2.270  40.083  1.00 45.24           C
ANISOU 2602  CA  HIS B  57     5510   5750   5928   -301    715    225       C
ATOM   2603  C   HIS B  57     -31.840   2.989  39.936  1.00 49.03           C
ANISOU 2603  C   HIS B  57     6024   6262   6344   -251    641    214       C
ATOM   2604  O   HIS B  57     -30.834   2.599  40.541  1.00 46.51           O
ANISOU 2604  O   HIS B  57     5805   5932   5935   -225    627    208       O
ATOM   2605  CB  HIS B  57     -33.505   1.981  41.539  1.00 41.96           C
ANISOU 2605  CB  HIS B  57     5182   5284   5478   -302    818    226       C
ATOM   2606  CG  HIS B  57     -33.814   3.192  42.351  1.00 48.15           C
ANISOU 2606  CG  HIS B  57     5958   6061   6277   -276    879    223       C
ATOM   2607  ND1 HIS B  57     -34.488   4.283  41.839  1.00 50.51           N
ANISOU 2607  ND1 HIS B  57     6146   6385   6661   -274    880    226       N
ATOM   2608  CD2 HIS B  57     -33.596   3.461  43.660  1.00 48.85           C
ANISOU 2608  CD2 HIS B  57     6140   6114   6306   -252    945    219       C
ATOM   2609  CE1 HIS B  57     -34.646   5.183  42.793  1.00 49.43           C
ANISOU 2609  CE1 HIS B  57     6036   6229   6517   -249    947    223       C
ATOM   2610  NE2 HIS B  57     -34.116   4.709  43.908  1.00 47.77           N
ANISOU 2610  NE2 HIS B  57     5950   5981   6218   -237    987    218       N
ATOM   2611  N   THR B  58     -31.832   4.025  39.094  1.00 49.51           N
ANISOU 2611  N   THR B  58     5998   6361   6452   -239    591    213       N
ATOM   2612  CA  THR B  58     -30.686   4.886  38.861  1.00 50.02           C
ANISOU 2612  CA  THR B  58     6076   6457   6471   -198    526    201       C
ATOM   2613  C   THR B  58     -30.958   6.316  39.313  1.00 52.82           C
ANISOU 2613  C   THR B  58     6400   6816   6853   -174    562    197       C
ATOM   2614  O   THR B  58     -30.055   7.155  39.231  1.00 53.07           O
ANISOU 2614  O   THR B  58     6444   6870   6848   -143    518    186       O
ATOM   2615  CB  THR B  58     -30.322   4.928  37.366  1.00 49.50           C
ANISOU 2615  CB  THR B  58     5945   6432   6431   -201    432    202       C
ATOM   2616  OG1 THR B  58     -31.208   5.848  36.694  1.00 47.74           O
ANISOU 2616  OG1 THR B  58     5616   6227   6296   -210    431    207       O
ATOM   2617  CG2 THR B  58     -30.466   3.546  36.741  1.00 44.75           C
ANISOU 2617  CG2 THR B  58     5351   5821   5830   -236    407    209       C
ATOM   2618  N   ALA B  59     -32.183   6.626  39.734  1.00 48.92           N
ANISOU 2618  N   ALA B  59     5861   6301   6425   -190    642    206       N
ATOM   2619  CA  ALA B  59     -32.539   7.986  40.113  1.00 52.21           C
ANISOU 2619  CA  ALA B  59     6245   6718   6874   -167    682    204       C
ATOM   2620  C   ALA B  59     -31.720   8.419  41.322  1.00 56.05           C
ANISOU 2620  C   ALA B  59     6838   7184   7274   -136    711    191       C
ATOM   2621  O   ALA B  59     -31.311   7.589  42.144  1.00 58.38           O
ANISOU 2621  O   ALA B  59     7228   7452   7500   -137    734    188       O
ATOM   2622  CB  ALA B  59     -34.028   8.083  40.436  1.00 53.15           C
ANISOU 2622  CB  ALA B  59     6302   6813   7079   -189    773    217       C
ATOM   2623  N   ALA B  60     -31.509   9.737  41.447  1.00 59.53           N
ANISOU 2623  N   ALA B  60     7266   7635   7717   -108    712    183       N
ATOM   2624  CA  ALA B  60     -30.709  10.269  42.553  1.00 67.23           C
ANISOU 2624  CA  ALA B  60     8341   8593   8609    -80    733    169       C
ATOM   2625  C   ALA B  60     -31.362   9.955  43.895  1.00 71.11           C
ANISOU 2625  C   ALA B  60     8903   9032   9083    -86    839    173       C
ATOM   2626  O   ALA B  60     -32.490  10.377  44.167  1.00 66.65           O
ANISOU 2626  O   ALA B  60     8295   8446   8584    -93    920    182       O
ATOM   2627  CB  ALA B  60     -30.502  11.783  42.396  1.00 55.99           C
ANISOU 2627  CB  ALA B  60     6889   7187   7200    -55    722    160       C
ATOM   2628  N   ILE B  61     -30.645   9.170  44.708  1.00 86.01           N
ANISOU 2628  N   ILE B  61    10901  10899  10882    -82    838    166       N
ATOM   2629  CA  ILE B  61     -31.038   8.773  46.055  1.00 88.60           C
ANISOU 2629  CA  ILE B  61    11323  11172  11169    -85    932    168       C
ATOM   2630  C   ILE B  61     -30.413   9.747  47.048  1.00 91.70           C
ANISOU 2630  C   ILE B  61    11802  11549  11493    -55    949    153       C
ATOM   2631  O   ILE B  61     -29.412   9.423  47.700  1.00 93.88           O
ANISOU 2631  O   ILE B  61    12180  11817  11672    -40    916    142       O
ATOM   2632  CB  ILE B  61     -30.608   7.322  46.356  1.00 76.04           C
ANISOU 2632  CB  ILE B  61     9813   9563   9515    -96    919    171       C
ATOM   2633  N   SER B  62     -30.998  10.948  47.149  1.00 90.38           N
ANISOU 2633  N   SER B  62    11591  11375  11372    -47    998    152       N
ATOM   2634  CA  SER B  62     -30.548  12.056  47.996  1.00 98.06           C
ANISOU 2634  CA  SER B  62    12634  12331  12291    -22   1020    138       C
ATOM   2635  C   SER B  62     -29.277  12.714  47.462  1.00 96.05           C
ANISOU 2635  C   SER B  62    12378  12122  11994     -4    913    121       C
ATOM   2636  O   SER B  62     -28.208  12.097  47.444  1.00 94.87           O
ANISOU 2636  O   SER B  62    12278  11991  11777      0    839    112       O
ATOM   2637  CB  SER B  62     -30.342  11.601  49.448  1.00 94.97           C
ANISOU 2637  CB  SER B  62    12386  11889  11811    -17   1079    132       C
ATOM   2638  N   ASN B  63     -29.382  13.976  47.042  1.00 96.82           N
ANISOU 2638  N   ASN B  63    12419  12236  12132      7    909    116       N
ATOM   2639  CA  ASN B  63     -28.243  14.714  46.518  1.00 95.00           C
ANISOU 2639  CA  ASN B  63    12183  12045  11868     20    818     98       C
ATOM   2640  C   ASN B  63     -28.208  16.123  47.108  1.00 91.05           C
ANISOU 2640  C   ASN B  63    11718  11526  11351     35    858     86       C
ATOM   2641  O   ASN B  63     -29.199  16.643  47.635  1.00 88.29           O
ANISOU 2641  O   ASN B  63    11370  11139  11038     39    953     93       O
ATOM   2642  CB  ASN B  63     -28.258  14.770  44.978  1.00 92.05           C
ANISOU 2642  CB  ASN B  63    11689  11720  11565     14    747    105       C
ATOM   2643  N   THR B  64     -27.030  16.735  47.006  1.00 87.66           N
ANISOU 2643  N   THR B  64    11318  11122  10867     43    784     65       N
ATOM   2644  CA  THR B  64     -26.759  18.020  47.626  1.00 80.32           C
ANISOU 2644  CA  THR B  64    10441  10175   9903     53    809     48       C
ATOM   2645  C   THR B  64     -27.451  19.143  46.869  1.00 75.82           C
ANISOU 2645  C   THR B  64     9784   9611   9414     60    835     54       C
ATOM   2646  O   THR B  64     -28.388  18.898  46.097  1.00 78.75           O
ANISOU 2646  O   THR B  64    10060   9990   9871     58    855     75       O
ATOM   2647  CB  THR B  64     -25.248  18.251  47.709  1.00 75.61           C
ANISOU 2647  CB  THR B  64     9897   9607   9225     54    717     23       C
ATOM   2648  OG1 THR B  64     -24.674  18.228  46.392  1.00 70.19           O
ANISOU 2648  OG1 THR B  64     9123   8974   8574     51    629     22       O
ATOM   2649  CG2 THR B  64     -24.588  17.159  48.567  1.00 69.22           C
ANISOU 2649  CG2 THR B  64     9181   8787   8331     54    693     18       C
ATOM   2650  N   GLY B  65     -27.000  20.373  47.080  1.00 65.58           N
ANISOU 2650  N   GLY B  65     8520   8309   8090     68    834     37       N
ATOM   2651  CA  GLY B  65     -27.718  21.521  46.562  1.00 61.71           C
ANISOU 2651  CA  GLY B  65     7966   7812   7668     80    874     44       C
ATOM   2652  C   GLY B  65     -27.305  21.983  45.179  1.00 58.36           C
ANISOU 2652  C   GLY B  65     7454   7436   7286     81    794     42       C
ATOM   2653  O   GLY B  65     -28.116  22.579  44.461  1.00 52.25           O
ANISOU 2653  O   GLY B  65     6601   6663   6589     92    819     56       O
ATOM   2654  N   LEU B  66     -26.047  21.739  44.797  1.00 57.31           N
ANISOU 2654  N   LEU B  66     7333   7339   7102     70    699     25       N
ATOM   2655  CA  LEU B  66     -25.635  22.021  43.433  1.00 55.36           C
ANISOU 2655  CA  LEU B  66     7004   7136   6894     69    625     24       C
ATOM   2656  C   LEU B  66     -26.495  21.196  42.483  1.00 62.00           C
ANISOU 2656  C   LEU B  66     7749   7994   7814     68    618     50       C
ATOM   2657  O   LEU B  66     -26.951  20.096  42.827  1.00 61.85           O
ANISOU 2657  O   LEU B  66     7735   7966   7800     61    640     63       O
ATOM   2658  CB  LEU B  66     -24.148  21.714  43.242  1.00 52.79           C
ANISOU 2658  CB  LEU B  66     6707   6846   6503     57    531      3       C
ATOM   2659  N   CYS B  67     -26.748  21.767  41.300  1.00 56.31           N
ANISOU 2659  N   CYS B  67     6947   7294   7154     74    590     58       N
ATOM   2660  CA  CYS B  67     -27.651  21.351  40.219  1.00 52.72           C
ANISOU 2660  CA  CYS B  67     6391   6855   6784     75    579     82       C
ATOM   2661  C   CYS B  67     -29.027  22.016  40.334  1.00 51.74           C
ANISOU 2661  C   CYS B  67     6222   6703   6733     93    661    101       C
ATOM   2662  O   CYS B  67     -29.833  21.885  39.411  1.00 53.14           O
ANISOU 2662  O   CYS B  67     6311   6894   6988     97    650    121       O
ATOM   2663  CB  CYS B  67     -27.842  19.820  40.112  1.00 59.89           C
ANISOU 2663  CB  CYS B  67     7282   7774   7699     58    560     95       C
ATOM   2664  SG  CYS B  67     -26.341  18.733  39.927  1.00 52.02           S
ANISOU 2664  SG  CYS B  67     6330   6811   6625     42    466     79       S
ATOM   2665  N   GLU B  68     -29.326  22.715  41.432  1.00 50.10           N
ANISOU 2665  N   GLU B  68     6075   6456   6505    105    741     96       N
ATOM   2666  CA  GLU B  68     -30.504  23.572  41.508  1.00 51.66           C
ANISOU 2666  CA  GLU B  68     6232   6626   6770    128    819    112       C
ATOM   2667  C   GLU B  68     -30.090  24.933  42.050  1.00 47.34           C
ANISOU 2667  C   GLU B  68     5753   6053   6181    144    852     94       C
ATOM   2668  O   GLU B  68     -29.008  25.092  42.619  1.00 45.46           O
ANISOU 2668  O   GLU B  68     5601   5813   5859    132    827     70       O
ATOM   2669  CB  GLU B  68     -31.637  22.938  42.325  1.00 46.95           C
ANISOU 2669  CB  GLU B  68     5631   5998   6211    128    910    129       C
ATOM   2670  CG  GLU B  68     -31.235  22.385  43.648  1.00 51.01           C
ANISOU 2670  CG  GLU B  68     6252   6483   6647    115    951    116       C
ATOM   2671  CD  GLU B  68     -32.354  21.568  44.241  1.00 55.40           C
ANISOU 2671  CD  GLU B  68     6792   7011   7246    109   1033    134       C
ATOM   2672  OE1 GLU B  68     -33.467  21.658  43.695  1.00 55.48           O
ANISOU 2672  OE1 GLU B  68     6706   7023   7351    118   1066    156       O
ATOM   2673  OE2 GLU B  68     -32.138  20.846  45.242  1.00 60.64           O
ANISOU 2673  OE2 GLU B  68     7539   7651   7851     96   1066    128       O
ATOM   2674  N   GLN B  69     -30.951  25.928  41.849  1.00 42.13           N
ANISOU 2674  N   GLN B  69     5055   5374   5581    172    906    107       N
ATOM   2675  CA  GLN B  69     -30.630  27.271  42.317  1.00 47.11           C
ANISOU 2675  CA  GLN B  69     5751   5974   6173    187    943     92       C
ATOM   2676  C   GLN B  69     -31.127  27.567  43.736  1.00 48.60           C
ANISOU 2676  C   GLN B  69     6021   6109   6336    197   1052     90       C
ATOM   2677  O   GLN B  69     -30.619  28.509  44.368  1.00 45.67           O
ANISOU 2677  O   GLN B  69     5736   5710   5907    200   1078     70       O
ATOM   2678  CB  GLN B  69     -31.185  28.333  41.346  1.00 46.52           C
ANISOU 2678  CB  GLN B  69     5607   5902   6166    218    944    106       C
ATOM   2679  N   ASN B  70     -32.084  26.790  44.264  1.00 45.91           N
ANISOU 2679  N   ASN B  70     5659   5750   6034    198   1118    108       N
ATOM   2680  CA  ASN B  70     -32.723  27.091  45.552  1.00 46.02           C
ANISOU 2680  CA  ASN B  70     5743   5707   6035    211   1235    109       C
ATOM   2681  C   ASN B  70     -32.929  25.811  46.377  1.00 51.05           C
ANISOU 2681  C   ASN B  70     6415   6331   6650    189   1268    112       C
ATOM   2682  O   ASN B  70     -34.054  25.325  46.555  1.00 50.19           O
ANISOU 2682  O   ASN B  70     6256   6207   6609    195   1339    134       O
ATOM   2683  CB  ASN B  70     -34.039  27.846  45.296  1.00 40.45           C
ANISOU 2683  CB  ASN B  70     4963   4980   5426    248   1315    134       C
ATOM   2684  CG  ASN B  70     -34.887  28.082  46.580  1.00 45.69           C
ANISOU 2684  CG  ASN B  70     5685   5582   6093    264   1452    140       C
ATOM   2685  OD1 ASN B  70     -34.419  28.650  47.577  1.00 44.16           O
ANISOU 2685  OD1 ASN B  70     5611   5347   5820    264   1497    121       O
ATOM   2686  ND2 ASN B  70     -36.157  27.678  46.524  1.00 42.77           N
ANISOU 2686  ND2 ASN B  70     5230   5204   5816    278   1518    166       N
ATOM   2687  N   PRO B  71     -31.852  25.249  46.919  1.00 52.32           N
ANISOU 2687  N   PRO B  71     6665   6498   6717    164   1220     91       N
ATOM   2688  CA  PRO B  71     -31.978  23.981  47.642  1.00 51.82           C
ANISOU 2688  CA  PRO B  71     6641   6422   6627    145   1244     95       C
ATOM   2689  C   PRO B  71     -32.505  24.176  49.047  1.00 57.03           C
ANISOU 2689  C   PRO B  71     7398   7017   7253    153   1362     94       C
ATOM   2690  O   PRO B  71     -32.329  25.226  49.666  1.00 53.56           O
ANISOU 2690  O   PRO B  71     7034   6543   6772    166   1406     81       O
ATOM   2691  CB  PRO B  71     -30.540  23.451  47.695  1.00 52.67           C
ANISOU 2691  CB  PRO B  71     6814   6558   6640    123   1143     72       C
ATOM   2692  CG  PRO B  71     -29.781  24.281  46.690  1.00 53.44           C
ANISOU 2692  CG  PRO B  71     6870   6695   6741    126   1058     60       C
ATOM   2693  CD  PRO B  71     -30.444  25.610  46.691  1.00 48.77           C
ANISOU 2693  CD  PRO B  71     6266   6075   6191    151   1126     65       C
ATOM   2694  N   GLU B  72     -33.209  23.155  49.536  1.00 58.95           N
ANISOU 2694  N   GLU B  72     7641   7240   7517    143   1421    108       N
ATOM   2695  CA  GLU B  72     -33.520  23.159  50.955  1.00 58.62           C
ANISOU 2695  CA  GLU B  72     7714   7135   7423    145   1527    104       C
ATOM   2696  C   GLU B  72     -32.234  22.943  51.723  1.00 62.58           C
ANISOU 2696  C   GLU B  72     8350   7630   7798    130   1472     78       C
ATOM   2697  O   GLU B  72     -31.967  23.611  52.729  1.00 63.03           O
ANISOU 2697  O   GLU B  72     8523   7642   7783    136   1520     63       O
ATOM   2698  CB  GLU B  72     -34.534  22.079  51.296  1.00 57.59           C
ANISOU 2698  CB  GLU B  72     7556   6983   7343    135   1604    125       C
ATOM   2699  CG  GLU B  72     -34.625  21.845  52.773  1.00 60.17           C
ANISOU 2699  CG  GLU B  72     8021   7244   7596    131   1699    118       C
ATOM   2700  CD  GLU B  72     -35.500  20.657  53.114  1.00 62.97           C
ANISOU 2700  CD  GLU B  72     8359   7577   7990    115   1770    136       C
ATOM   2701  OE1 GLU B  72     -35.901  20.579  54.292  1.00 62.23           O
ANISOU 2701  OE1 GLU B  72     8365   7422   7859    116   1877    136       O
ATOM   2702  OE2 GLU B  72     -35.775  19.815  52.214  1.00 54.01           O
ANISOU 2702  OE2 GLU B  72     7117   6484   6920     99   1721    149       O
ATOM   2703  N   LEU B  73     -31.423  21.997  51.241  1.00 66.70           N
ANISOU 2703  N   LEU B  73     8856   8196   8289    111   1369     73       N
ATOM   2704  CA  LEU B  73     -30.098  21.708  51.764  1.00 70.17           C
ANISOU 2704  CA  LEU B  73     9401   8644   8616     99   1293     50       C
ATOM   2705  C   LEU B  73     -30.061  21.459  53.266  1.00 75.74           C
ANISOU 2705  C   LEU B  73    10255   9290   9234     97   1363     42       C
ATOM   2706  O   LEU B  73     -28.984  21.219  53.817  1.00 74.84           O
ANISOU 2706  O   LEU B  73    10237   9179   9021     90   1301     22       O
ATOM   2707  CB  LEU B  73     -29.173  22.862  51.403  1.00 62.16           C
ANISOU 2707  CB  LEU B  73     8395   7652   7568    103   1225     28       C
ATOM   2708  CG  LEU B  73     -27.727  22.532  51.112  1.00 57.49           C
ANISOU 2708  CG  LEU B  73     7828   7107   6908     88   1099      8       C
ATOM   2709  CD1 LEU B  73     -27.638  21.354  50.184  1.00 61.52           C
ANISOU 2709  CD1 LEU B  73     8251   7666   7459     80   1030     21       C
ATOM   2710  CD2 LEU B  73     -27.211  23.728  50.435  1.00 50.55           C
ANISOU 2710  CD2 LEU B  73     6913   6253   6040     91   1052     -7       C
ATOM   2711  N   SER B  74     -31.211  21.564  53.946  1.00 90.38           N
ANISOU 2711  N   SER B  74    12130  11089  11122    106   1492     56       N
ATOM   2712  CA  SER B  74     -31.288  21.184  55.354  1.00 93.32           C
ANISOU 2712  CA  SER B  74    12645  11398  11413    103   1569     51       C
ATOM   2713  C   SER B  74     -30.565  19.877  55.622  1.00 99.73           C
ANISOU 2713  C   SER B  74    13513  12223  12155     88   1502     48       C
ATOM   2714  O   SER B  74     -30.148  19.638  56.762  1.00 97.37           O
ANISOU 2714  O   SER B  74    13356  11882  11758     86   1523     37       O
ATOM   2715  CB  SER B  74     -32.744  21.063  55.824  1.00 92.89           C
ANISOU 2715  CB  SER B  74    12575  11290  11427    110   1716     73       C
ATOM   2716  OG  SER B  74     -32.809  20.944  57.239  1.00 93.33           O
ANISOU 2716  OG  SER B  74    12786  11277  11399    110   1802     67       O
ATOM   2717  N   GLU B  75     -30.424  19.022  54.593  1.00 99.20           N
ANISOU 2717  N   GLU B  75    13343  12210  12137     78   1425     58       N
ATOM   2718  CA  GLU B  75     -29.704  17.747  54.651  1.00 97.56           C
ANISOU 2718  CA  GLU B  75    13175  12022  11873     67   1352     57       C
ATOM   2719  C   GLU B  75     -30.042  16.981  55.912  1.00114.71           C
ANISOU 2719  C   GLU B  75    15471  14130  13982     64   1436     61       C
ATOM   2720  O   GLU B  75     -29.238  16.221  56.468  1.00109.36           O
ANISOU 2720  O   GLU B  75    14891  13448  13213     63   1386     53       O
ATOM   2721  CB  GLU B  75     -28.199  17.976  54.551  1.00 86.71           C
ANISOU 2721  CB  GLU B  75    11844  10687  10415     69   1227     33       C
ATOM   2722  CG  GLU B  75     -27.496  18.524  55.814  1.00 82.11           C
ANISOU 2722  CG  GLU B  75    11416  10064   9717     74   1233     11       C
ATOM   2723  CD  GLU B  75     -26.148  19.185  55.524  1.00 70.15           C
ANISOU 2723  CD  GLU B  75     9911   8595   8149     73   1115    -15       C
ATOM   2724  OE1 GLU B  75     -25.854  19.542  54.356  1.00 67.07           O
ANISOU 2724  OE1 GLU B  75     9407   8259   7817     71   1047    -16       O
ATOM   2725  OE2 GLU B  75     -25.375  19.334  56.486  1.00 64.12           O
ANISOU 2725  OE2 GLU B  75     9271   7810   7283     73   1090    -34       O
ATOM   2726  N   SER B  76     -31.256  17.161  56.381  1.00158.04           N
ANISOU 2726  N   SER B  76    20960  19567  19520     65   1567     75       N
ATOM   2727  CA  SER B  76     -31.613  16.501  57.625  1.00158.70           C
ANISOU 2727  CA  SER B  76    21172  19583  19543     61   1659     79       C
ATOM   2728  C   SER B  76     -32.162  15.139  57.220  1.00157.54           C
ANISOU 2728  C   SER B  76    20967  19444  19446     44   1671     98       C
ATOM   2729  O   SER B  76     -33.164  15.071  56.507  1.00157.72           O
ANISOU 2729  O   SER B  76    20865  19480  19583     35   1718    115       O
ATOM   2730  CB  SER B  76     -32.509  17.426  58.464  1.00158.68           C
ANISOU 2730  CB  SER B  76    21221  19515  19553     71   1798     80       C
ATOM   2731  OG  SER B  76     -33.738  17.877  57.791  1.00160.55           O
ANISOU 2731  OG  SER B  76    21320  19758  19925     74   1875     99       O
ATOM   2732  N   ILE B  77     -31.352  14.096  57.522  1.00128.93           N
ANISOU 2732  N   ILE B  77    17425  15823  15739     40   1607     94       N
ATOM   2733  CA  ILE B  77     -31.415  12.655  57.211  1.00116.93           C
ANISOU 2733  CA  ILE B  77    15888  14314  14227     24   1584    107       C
ATOM   2734  C   ILE B  77     -31.320  12.419  55.704  1.00114.41           C
ANISOU 2734  C   ILE B  77    15409  14067  13993     15   1492    114       C
ATOM   2735  O   ILE B  77     -30.337  11.855  55.203  1.00108.68           O
ANISOU 2735  O   ILE B  77    14681  13385  13228     17   1379    109       O
ATOM   2736  CB  ILE B  77     -32.670  11.969  57.810  1.00113.24           C
ANISOU 2736  CB  ILE B  77    15444  13784  13797      7   1726    125       C
ATOM   2737  N   ASN B  78     -32.305  12.942  54.976  1.00118.91           N
ANISOU 2737  N   ASN B  78    15849  14652  14679      7   1538    125       N
ATOM   2738  CA  ASN B  78     -32.520  12.680  53.560  1.00113.40           C
ANISOU 2738  CA  ASN B  78    14997  14013  14075     -5   1473    135       C
ATOM   2739  C   ASN B  78     -32.914  11.216  53.432  1.00108.97           C
ANISOU 2739  C   ASN B  78    14430  13444  13531    -30   1488    149       C
ATOM   2740  O   ASN B  78     -32.132  10.320  53.764  1.00105.90           O
ANISOU 2740  O   ASN B  78    14130  13050  13058    -30   1440    145       O
ATOM   2741  CB  ASN B  78     -31.293  13.022  52.709  1.00103.47           C
ANISOU 2741  CB  ASN B  78    13705  12820  12790      6   1332    122       C
ATOM   2742  N   LEU B  79     -34.124  10.966  52.946  1.00119.11           N
ANISOU 2742  N   LEU B  79    15609  14724  14923    -52   1554    166       N
ATOM   2743  CA  LEU B  79     -34.657   9.613  52.906  1.00115.14           C
ANISOU 2743  CA  LEU B  79    15103  14205  14442    -83   1587    179       C
ATOM   2744  C   LEU B  79     -35.882   9.578  52.001  1.00112.64           C
ANISOU 2744  C   LEU B  79    14628  13907  14262   -108   1623    194       C
ATOM   2745  O   LEU B  79     -36.304  10.595  51.443  1.00111.47           O
ANISOU 2745  O   LEU B  79    14379  13784  14189    -97   1623    197       O
ATOM   2746  CB  LEU B  79     -35.007   9.112  54.313  1.00111.29           C
ANISOU 2746  CB  LEU B  79    14753  13641  13893    -88   1702    180       C
ATOM   2747  N   ASN B  80     -36.376   8.353  51.796  1.00 90.07           N
ANISOU 2747  N   ASN B  80    11751  11039  11434   -143   1643    205       N
ATOM   2748  CA  ASN B  80     -37.616   7.952  51.128  1.00 80.42           C
ANISOU 2748  CA  ASN B  80    10399   9824  10334   -179   1690    220       C
ATOM   2749  C   ASN B  80     -37.409   7.779  49.630  1.00 72.17           C
ANISOU 2749  C   ASN B  80     9230   8847   9346   -190   1571    223       C
ATOM   2750  O   ASN B  80     -36.279   7.571  49.178  1.00 72.73           O
ANISOU 2750  O   ASN B  80     9334   8951   9350   -177   1461    214       O
ATOM   2751  CB  ASN B  80     -38.761   8.952  51.342  1.00 81.47           C
ANISOU 2751  CB  ASN B  80    10454   9940  10560   -172   1792    227       C
ATOM   2752  CG  ASN B  80     -39.045   9.250  52.814  1.00 83.66           C
ANISOU 2752  CG  ASN B  80    10853  10146  10788   -159   1922    225       C
ATOM   2753  OD1 ASN B  80     -38.769   8.445  53.714  1.00 83.15           O
ANISOU 2753  OD1 ASN B  80    10919  10035  10640   -169   1964    222       O
ATOM   2754  ND2 ASN B  80     -39.791  10.342  53.028  1.00 88.55           N
ANISOU 2754  ND2 ASN B  80    11420  10752  11471   -141   2001    229       N
ATOM   2755  N   GLY B  81     -38.508   7.845  48.869  1.00 69.84           N
ANISOU 2755  N   GLY B  81     8793   8570   9172   -214   1593    235       N
ATOM   2756  CA  GLY B  81     -38.539   7.770  47.411  1.00 67.98           C
ANISOU 2756  CA  GLY B  81     8429   8395   9004   -228   1490    239       C
ATOM   2757  C   GLY B  81     -38.117   6.415  46.861  1.00 70.73           C
ANISOU 2757  C   GLY B  81     8797   8755   9322   -260   1422    239       C
ATOM   2758  O   GLY B  81     -38.785   5.841  45.991  1.00 67.18           O
ANISOU 2758  O   GLY B  81     8248   8325   8951   -297   1402    248       O
ATOM   2759  N   THR B  82     -36.999   5.896  47.369  1.00 63.23           N
ANISOU 2759  N   THR B  82     7977   7792   8257   -246   1386    230       N
ATOM   2760  CA  THR B  82     -36.598   4.532  47.077  1.00 60.36           C
ANISOU 2760  CA  THR B  82     7656   7426   7851   -272   1341    231       C
ATOM   2761  C   THR B  82     -37.451   3.556  47.873  1.00 59.76           C
ANISOU 2761  C   THR B  82     7630   7292   7784   -310   1453    238       C
ATOM   2762  O   THR B  82     -37.695   2.431  47.425  1.00 57.28           O
ANISOU 2762  O   THR B  82     7303   6974   7486   -350   1441    243       O
ATOM   2763  CB  THR B  82     -35.131   4.357  47.414  1.00 61.30           C
ANISOU 2763  CB  THR B  82     7896   7549   7846   -237   1269    219       C
ATOM   2764  OG1 THR B  82     -35.011   4.316  48.834  1.00 63.16           O
ANISOU 2764  OG1 THR B  82     8263   7730   8005   -222   1351    216       O
ATOM   2765  CG2 THR B  82     -34.342   5.553  46.918  1.00 61.17           C
ANISOU 2765  CG2 THR B  82     7843   7580   7819   -199   1185    210       C
ATOM   2766  N   LYS B  83     -37.859   3.962  49.080  1.00 61.33           N
ANISOU 2766  N   LYS B  83     7895   7441   7965   -299   1564    237       N
ATOM   2767  CA  LYS B  83     -38.759   3.147  49.887  1.00 61.98           C
ANISOU 2767  CA  LYS B  83     8022   7464   8063   -336   1687    244       C
ATOM   2768  C   LYS B  83     -40.078   2.901  49.165  1.00 61.72           C
ANISOU 2768  C   LYS B  83     7843   7443   8166   -385   1727    255       C
ATOM   2769  O   LYS B  83     -40.531   1.755  49.044  1.00 63.79           O
ANISOU 2769  O   LYS B  83     8106   7685   8447   -433   1753    259       O
ATOM   2770  CB  LYS B  83     -39.035   3.828  51.226  1.00 60.79           C
ANISOU 2770  CB  LYS B  83     7957   7260   7881   -312   1802    242       C
ATOM   2771  CG  LYS B  83     -38.023   3.562  52.295  1.00 60.68           C
ANISOU 2771  CG  LYS B  83     8124   7206   7726   -283   1803    234       C
ATOM   2772  CD  LYS B  83     -37.981   4.725  53.267  1.00 66.80           C
ANISOU 2772  CD  LYS B  83     8961   7954   8468   -245   1867    228       C
ATOM   2773  CE  LYS B  83     -39.391   5.131  53.685  1.00 70.36           C
ANISOU 2773  CE  LYS B  83     9351   8367   9016   -265   2009    237       C
ATOM   2774  NZ  LYS B  83     -40.036   4.145  54.621  1.00 66.10           N
ANISOU 2774  NZ  LYS B  83     8900   7756   8458   -297   2133    242       N
ATOM   2775  N   TYR B  84     -40.714   3.972  48.678  1.00 63.45           N
ANISOU 2775  N   TYR B  84     7934   7694   8481   -374   1730    259       N
ATOM   2776  CA  TYR B  84     -42.001   3.803  48.008  1.00 63.72           C
ANISOU 2776  CA  TYR B  84     7819   7742   8650   -418   1765    269       C
ATOM   2777  C   TYR B  84     -41.827   2.954  46.768  1.00 60.58           C
ANISOU 2777  C   TYR B  84     7357   7386   8274   -454   1656    270       C
ATOM   2778  O   TYR B  84     -42.632   2.060  46.498  1.00 59.12           O
ANISOU 2778  O   TYR B  84     7121   7190   8151   -510   1688    275       O
ATOM   2779  CB  TYR B  84     -42.627   5.162  47.685  1.00 57.81           C
ANISOU 2779  CB  TYR B  84     6948   7022   7994   -391   1778    275       C
ATOM   2780  CG  TYR B  84     -42.846   5.983  48.933  1.00 57.45           C
ANISOU 2780  CG  TYR B  84     6972   6929   7927   -357   1894    274       C
ATOM   2781  CD1 TYR B  84     -43.045   5.371  50.160  1.00 55.26           C
ANISOU 2781  CD1 TYR B  84     6813   6584   7598   -372   2010    273       C
ATOM   2782  CD2 TYR B  84     -42.822   7.367  48.894  1.00 61.91           C
ANISOU 2782  CD2 TYR B  84     7495   7513   8515   -309   1890    274       C
ATOM   2783  CE1 TYR B  84     -43.226   6.107  51.309  1.00 56.31           C
ANISOU 2783  CE1 TYR B  84     7021   6670   7705   -341   2118    271       C
ATOM   2784  CE2 TYR B  84     -43.006   8.121  50.052  1.00 62.40           C
ANISOU 2784  CE2 TYR B  84     7631   7527   8551   -278   2000    272       C
ATOM   2785  CZ  TYR B  84     -43.205   7.481  51.251  1.00 57.99           C
ANISOU 2785  CZ  TYR B  84     7190   6901   7941   -295   2113    271       C
ATOM   2786  OH  TYR B  84     -43.386   8.216  52.395  1.00 54.55           O
ANISOU 2786  OH  TYR B  84     6837   6415   7476   -265   2223    269       O
ATOM   2787  N   LEU B  85     -40.740   3.174  46.047  1.00 54.26           N
ANISOU 2787  N   LEU B  85     6569   6629   7419   -425   1531    264       N
ATOM   2788  CA  LEU B  85     -40.414   2.298  44.938  1.00 56.86           C
ANISOU 2788  CA  LEU B  85     6866   6991   7749   -455   1429    264       C
ATOM   2789  C   LEU B  85     -40.270   0.845  45.407  1.00 60.84           C
ANISOU 2789  C   LEU B  85     7475   7450   8190   -492   1462    263       C
ATOM   2790  O   LEU B  85     -40.831  -0.072  44.797  1.00 61.05           O
ANISOU 2790  O   LEU B  85     7452   7477   8267   -545   1454    266       O
ATOM   2791  CB  LEU B  85     -39.127   2.792  44.293  1.00 57.60           C
ANISOU 2791  CB  LEU B  85     6982   7129   7776   -410   1304    257       C
ATOM   2792  CG  LEU B  85     -38.608   2.083  43.059  1.00 57.16           C
ANISOU 2792  CG  LEU B  85     6897   7110   7712   -429   1187    256       C
ATOM   2793  CD1 LEU B  85     -39.699   2.048  42.002  1.00 53.71           C
ANISOU 2793  CD1 LEU B  85     6311   6702   7396   -472   1168    264       C
ATOM   2794  CD2 LEU B  85     -37.362   2.840  42.563  1.00 49.12           C
ANISOU 2794  CD2 LEU B  85     5896   6133   6633   -378   1082    248       C
ATOM   2795  N   ALA B  86     -39.534   0.615  46.503  1.00 58.95           N
ANISOU 2795  N   ALA B  86     7387   7168   7841   -464   1501    258       N
ATOM   2796  CA  ALA B  86     -39.320  -0.754  46.973  1.00 58.66           C
ANISOU 2796  CA  ALA B  86     7465   7087   7737   -492   1531    258       C
ATOM   2797  C   ALA B  86     -40.601  -1.392  47.503  1.00 61.64           C
ANISOU 2797  C   ALA B  86     7827   7414   8179   -548   1658    264       C
ATOM   2798  O   ALA B  86     -40.935  -2.529  47.148  1.00 60.42           O
ANISOU 2798  O   ALA B  86     7673   7245   8040   -600   1662    266       O
ATOM   2799  CB  ALA B  86     -38.237  -0.780  48.049  1.00 59.25           C
ANISOU 2799  CB  ALA B  86     7706   7128   7678   -443   1538    252       C
ATOM   2800  N   GLU B  87     -41.335  -0.681  48.355  1.00 65.59           N
ANISOU 2800  N   GLU B  87     8317   7886   8719   -541   1768    266       N
ATOM   2801  CA  GLU B  87     -42.554  -1.266  48.895  1.00 67.25           C
ANISOU 2801  CA  GLU B  87     8510   8046   8994   -595   1899    271       C
ATOM   2802  C   GLU B  87     -43.562  -1.524  47.790  1.00 65.82           C
ANISOU 2802  C   GLU B  87     8163   7901   8945   -653   1877    276       C
ATOM   2803  O   GLU B  87     -44.281  -2.525  47.841  1.00 72.34           O
ANISOU 2803  O   GLU B  87     8982   8695   9807   -715   1937    278       O
ATOM   2804  CB  GLU B  87     -43.136  -0.376  49.991  1.00 69.11           C
ANISOU 2804  CB  GLU B  87     8762   8245   9250   -572   2024    273       C
ATOM   2805  CG  GLU B  87     -42.310  -0.427  51.287  1.00 71.15           C
ANISOU 2805  CG  GLU B  87     9213   8448   9372   -531   2070    268       C
ATOM   2806  CD  GLU B  87     -42.325   0.885  52.075  1.00 74.58           C
ANISOU 2806  CD  GLU B  87     9669   8871   9798   -481   2127    266       C
ATOM   2807  OE1 GLU B  87     -43.381   1.560  52.109  1.00 77.63           O
ANISOU 2807  OE1 GLU B  87     9949   9256  10290   -491   2207    272       O
ATOM   2808  OE2 GLU B  87     -41.271   1.249  52.648  1.00 69.39           O
ANISOU 2808  OE2 GLU B  87     9132   8205   9028   -432   2090    259       O
ATOM   2809  N   ALA B  88     -43.608  -0.660  46.770  1.00 59.44           N
ANISOU 2809  N   ALA B  88     7223   7158   8205   -635   1788    278       N
ATOM   2810  CA  ALA B  88     -44.443  -0.948  45.609  1.00 59.02           C
ANISOU 2810  CA  ALA B  88     7017   7144   8266   -687   1743    282       C
ATOM   2811  C   ALA B  88     -43.956  -2.202  44.905  1.00 61.16           C
ANISOU 2811  C   ALA B  88     7329   7417   8490   -727   1663    278       C
ATOM   2812  O   ALA B  88     -44.765  -3.041  44.477  1.00 60.32           O
ANISOU 2812  O   ALA B  88     7163   7305   8451   -795   1681    280       O
ATOM   2813  CB  ALA B  88     -44.444   0.222  44.624  1.00 51.21           C
ANISOU 2813  CB  ALA B  88     5895   6220   7341   -653   1650    285       C
ATOM   2814  N   ALA B  89     -42.633  -2.354  44.790  1.00 65.25           N
ANISOU 2814  N   ALA B  89     7952   7945   8894   -686   1577    273       N
ATOM   2815  CA  ALA B  89     -42.075  -3.533  44.136  1.00 63.62           C
ANISOU 2815  CA  ALA B  89     7797   7739   8636   -715   1502    270       C
ATOM   2816  C   ALA B  89     -42.349  -4.812  44.920  1.00 62.90           C
ANISOU 2816  C   ALA B  89     7814   7581   8504   -761   1595    270       C
ATOM   2817  O   ALA B  89     -42.512  -5.877  44.320  1.00 57.63           O
ANISOU 2817  O   ALA B  89     7146   6907   7845   -814   1568    269       O
ATOM   2818  CB  ALA B  89     -40.574  -3.351  43.935  1.00 60.11           C
ANISOU 2818  CB  ALA B  89     7440   7317   8080   -654   1399    265       C
ATOM   2819  N   SER B  90     -42.380  -4.734  46.252  1.00 67.21           N
ANISOU 2819  N   SER B  90     8462   8073   9001   -741   1704    270       N
ATOM   2820  CA  SER B  90     -42.687  -5.922  47.039  1.00 69.80           C
ANISOU 2820  CA  SER B  90     8899   8332   9290   -785   1802    270       C
ATOM   2821  C   SER B  90     -44.088  -6.416  46.726  1.00 71.64           C
ANISOU 2821  C   SER B  90     9021   8554   9645   -868   1871    272       C
ATOM   2822  O   SER B  90     -44.314  -7.629  46.593  1.00 68.10           O
ANISOU 2822  O   SER B  90     8615   8073   9188   -926   1891    271       O
ATOM   2823  CB  SER B  90     -42.558  -5.625  48.535  1.00 70.69           C
ANISOU 2823  CB  SER B  90     9138   8388   9335   -748   1912    271       C
ATOM   2824  OG  SER B  90     -42.503  -6.827  49.290  1.00 72.52           O
ANISOU 2824  OG  SER B  90     9512   8550   9493   -775   1985    271       O
ATOM   2825  N   LYS B  91     -45.022  -5.472  46.532  1.00 62.69           N
ANISOU 2825  N   LYS B  91     7740   7451   8630   -874   1902    275       N
ATOM   2826  CA  LYS B  91     -46.427  -5.808  46.345  1.00 59.38           C
ANISOU 2826  CA  LYS B  91     7202   7022   8339   -950   1978    277       C
ATOM   2827  C   LYS B  91     -46.661  -6.682  45.120  1.00 55.58           C
ANISOU 2827  C   LYS B  91     6647   6569   7902  -1015   1891    275       C
ATOM   2828  O   LYS B  91     -47.597  -7.488  45.119  1.00 49.22           O
ANISOU 2828  O   LYS B  91     5804   5736   7161  -1092   1958    273       O
ATOM   2829  CB  LYS B  91     -47.255  -4.528  46.293  1.00 55.22           C
ANISOU 2829  CB  LYS B  91     6525   6530   7927   -930   2010    283       C
ATOM   2830  CG  LYS B  91     -47.440  -3.973  47.689  1.00 57.94           C
ANISOU 2830  CG  LYS B  91     6945   6822   8246   -895   2146    285       C
ATOM   2831  CD  LYS B  91     -48.310  -2.741  47.746  1.00 62.77           C
ANISOU 2831  CD  LYS B  91     7419   7460   8972   -874   2197    292       C
ATOM   2832  CE  LYS B  91     -49.719  -3.037  47.292  1.00 66.93           C
ANISOU 2832  CE  LYS B  91     7785   7996   9649   -946   2248    295       C
ATOM   2833  NZ  LYS B  91     -50.643  -1.897  47.564  1.00 67.80           N
ANISOU 2833  NZ  LYS B  91     7773   8118   9871   -921   2325    303       N
ATOM   2834  N   ILE B  92     -45.860  -6.519  44.067  1.00 53.42           N
ANISOU 2834  N   ILE B  92     6350   6348   7597   -988   1747    273       N
ATOM   2835  CA  ILE B  92     -46.015  -7.284  42.837  1.00 49.63           C
ANISOU 2835  CA  ILE B  92     5808   5895   7153  -1045   1655    270       C
ATOM   2836  C   ILE B  92     -44.818  -8.190  42.553  1.00 43.83           C
ANISOU 2836  C   ILE B  92     5213   5148   6294  -1033   1578    266       C
ATOM   2837  O   ILE B  92     -44.617  -8.566  41.415  1.00 43.21           O
ANISOU 2837  O   ILE B  92     5093   5102   6224  -1056   1474    264       O
ATOM   2838  CB  ILE B  92     -46.311  -6.363  41.637  1.00 53.66           C
ANISOU 2838  CB  ILE B  92     6151   6480   7756  -1036   1550    273       C
ATOM   2839  CG1 ILE B  92     -45.101  -5.450  41.338  1.00 52.86           C
ANISOU 2839  CG1 ILE B  92     6083   6419   7580   -949   1450    274       C
ATOM   2840  CG2 ILE B  92     -47.647  -5.581  41.895  1.00 51.65           C
ANISOU 2840  CG2 ILE B  92     5748   6237   7640  -1054   1633    279       C
ATOM   2841  CD1 ILE B  92     -45.098  -4.862  39.939  1.00 49.93           C
ANISOU 2841  CD1 ILE B  92     5586   6116   7268   -943   1320    275       C
ATOM   2842  N   ASN B  93     -43.978  -8.473  43.562  1.00 48.09           N
ANISOU 2842  N   ASN B  93     5915   5641   6715   -989   1623    266       N
ATOM   2843  CA  ASN B  93     -42.843  -9.433  43.473  1.00 46.33           C
ANISOU 2843  CA  ASN B  93     5839   5396   6368   -972   1567    264       C
ATOM   2844  C   ASN B  93     -41.862  -9.121  42.336  1.00 42.99           C
ANISOU 2844  C   ASN B  93     5390   5033   5913   -931   1417    263       C
ATOM   2845  O   ASN B  93     -41.444 -10.014  41.606  1.00 37.60           O
ANISOU 2845  O   ASN B  93     4745   4348   5192   -954   1351    261       O
ATOM   2846  CB  ASN B  93     -43.305 -10.901  43.321  1.00 45.55           C
ANISOU 2846  CB  ASN B  93     5789   5250   6268  -1053   1605    261       C
ATOM   2847  CG  ASN B  93     -44.450 -11.287  44.228  1.00 39.24           C
ANISOU 2847  CG  ASN B  93     4992   4396   5524  -1112   1753    261       C
ATOM   2848  OD1 ASN B  93     -44.265 -11.575  45.413  1.00 39.31           O
ANISOU 2848  OD1 ASN B  93     5130   4345   5461  -1094   1850    263       O
ATOM   2849  ND2 ASN B  93     -45.645 -11.346  43.654  1.00 45.44           N
ANISOU 2849  ND2 ASN B  93     5634   5197   6435  -1187   1772    259       N
ATOM   2850  N   SER B  94     -41.424  -7.867  42.230  1.00 45.46           N
ANISOU 2850  N   SER B  94     5650   5393   6231   -867   1366    264       N
ATOM   2851  CA  SER B  94     -40.561  -7.464  41.123  1.00 41.94           C
ANISOU 2851  CA  SER B  94     5167   5003   5764   -831   1230    262       C
ATOM   2852  C   SER B  94     -39.082  -7.660  41.478  1.00 35.64           C
ANISOU 2852  C   SER B  94     4512   4197   4833   -764   1185    261       C
ATOM   2853  O   SER B  94     -38.697  -7.686  42.645  1.00 36.00           O
ANISOU 2853  O   SER B  94     4668   4204   4807   -730   1250    261       O
ATOM   2854  CB  SER B  94     -40.805  -5.992  40.751  1.00 46.68           C
ANISOU 2854  CB  SER B  94     5638   5658   6438   -796   1194    264       C
ATOM   2855  OG  SER B  94     -42.012  -5.799  40.031  1.00 49.43           O
ANISOU 2855  OG  SER B  94     5837   6032   6913   -851   1193    266       O
ATOM   2856  N   LYS B  95     -38.252  -7.813  40.448  1.00 41.75           N
ANISOU 2856  N   LYS B  95     5285   5006   5574   -746   1071    259       N
ATOM   2857  CA  LYS B  95     -36.802  -7.920  40.625  1.00 43.49           C
ANISOU 2857  CA  LYS B  95     5618   5228   5678   -680   1014    258       C
ATOM   2858  C   LYS B  95     -36.180  -6.523  40.535  1.00 39.22           C
ANISOU 2858  C   LYS B  95     5028   4739   5137   -615    959    255       C
ATOM   2859  O   LYS B  95     -36.207  -5.885  39.478  1.00 39.19           O
ANISOU 2859  O   LYS B  95     4919   4785   5187   -614    882    254       O
ATOM   2860  CB  LYS B  95     -36.208  -8.862  39.580  1.00 38.39           C
ANISOU 2860  CB  LYS B  95     5003   4589   4996   -694    929    257       C
ATOM   2861  CG  LYS B  95     -34.751  -9.276  39.823  1.00 38.90           C
ANISOU 2861  CG  LYS B  95     5196   4646   4939   -630    883    257       C
ATOM   2862  CD  LYS B  95     -34.573 -10.009  41.157  1.00 40.35           C
ANISOU 2862  CD  LYS B  95     5522   4766   5042   -617    970    260       C
ATOM   2863  CE  LYS B  95     -33.214 -10.692  41.277  1.00 34.53           C
ANISOU 2863  CE  LYS B  95     4914   4017   4189   -562    920    262       C
ATOM   2864  NZ  LYS B  95     -33.029 -11.178  42.685  1.00 32.35           N
ANISOU 2864  NZ  LYS B  95     4776   3683   3834   -538   1002    266       N
ATOM   2865  N   LEU B  96     -35.661  -6.019  41.642  1.00 34.51           N
ANISOU 2865  N   LEU B  96     4506   4127   4480   -564    999    254       N
ATOM   2866  CA  LEU B  96     -35.124  -4.665  41.648  1.00 40.23           C
ANISOU 2866  CA  LEU B  96     5187   4893   5203   -508    957    250       C
ATOM   2867  C   LEU B  96     -33.600  -4.700  41.554  1.00 40.35           C
ANISOU 2867  C   LEU B  96     5284   4927   5118   -448    873    246       C
ATOM   2868  O   LEU B  96     -32.931  -5.394  42.340  1.00 33.37           O
ANISOU 2868  O   LEU B  96     4527   4008   4143   -424    893    246       O
ATOM   2869  CB  LEU B  96     -35.566  -3.885  42.890  1.00 41.32           C
ANISOU 2869  CB  LEU B  96     5344   5008   5348   -490   1052    250       C
ATOM   2870  CG  LEU B  96     -35.348  -2.363  42.881  1.00 40.47           C
ANISOU 2870  CG  LEU B  96     5172   4941   5265   -445   1025    245       C
ATOM   2871  CD1 LEU B  96     -36.478  -1.624  43.603  1.00 42.67           C
ANISOU 2871  CD1 LEU B  96     5398   5200   5613   -458   1129    248       C
ATOM   2872  CD2 LEU B  96     -34.033  -2.057  43.535  1.00 39.36           C
ANISOU 2872  CD2 LEU B  96     5137   4801   5016   -382    991    239       C
ATOM   2873  N   ILE B  97     -33.073  -3.929  40.600  1.00 39.00           N
ANISOU 2873  N   ILE B  97     5039   4811   4968   -423    782    242       N
ATOM   2874  CA  ILE B  97     -31.650  -3.739  40.357  1.00 34.18           C
ANISOU 2874  CA  ILE B  97     4476   4229   4281   -367    697    236       C
ATOM   2875  C   ILE B  97     -31.331  -2.285  40.671  1.00 41.77           C
ANISOU 2875  C   ILE B  97     5399   5221   5249   -325    686    230       C
ATOM   2876  O   ILE B  97     -31.743  -1.374  39.941  1.00 42.00           O
ANISOU 2876  O   ILE B  97     5320   5286   5350   -332    659    229       O
ATOM   2877  CB  ILE B  97     -31.272  -4.054  38.907  1.00 36.55           C
ANISOU 2877  CB  ILE B  97     4725   4563   4598   -378    603    236       C
ATOM   2878  CG1 ILE B  97     -31.890  -5.377  38.470  1.00 29.46           C
ANISOU 2878  CG1 ILE B  97     3843   3634   3716   -434    621    242       C
ATOM   2879  CG2 ILE B  97     -29.733  -4.006  38.716  1.00 31.85           C
ANISOU 2879  CG2 ILE B  97     4189   3993   3921   -319    525    231       C
ATOM   2880  CD1 ILE B  97     -31.548  -6.510  39.382  1.00 37.78           C
ANISOU 2880  CD1 ILE B  97     5031   4636   4688   -429    670    245       C
ATOM   2881  N   PHE B  98     -30.596  -2.062  41.747  1.00 36.57           N
ANISOU 2881  N   PHE B  98     4834   4548   4513   -281    705    225       N
ATOM   2882  CA  PHE B  98     -30.244  -0.729  42.193  1.00 34.56           C
ANISOU 2882  CA  PHE B  98     4563   4315   4252   -243    700    217       C
ATOM   2883  C   PHE B  98     -28.813  -0.434  41.773  1.00 37.60           C
ANISOU 2883  C   PHE B  98     4968   4740   4578   -196    603    208       C
ATOM   2884  O   PHE B  98     -27.925  -1.287  41.907  1.00 32.34           O
ANISOU 2884  O   PHE B  98     4385   4066   3838   -175    569    208       O
ATOM   2885  CB  PHE B  98     -30.404  -0.639  43.706  1.00 34.23           C
ANISOU 2885  CB  PHE B  98     4614   4228   4162   -229    787    216       C
ATOM   2886  CG  PHE B  98     -29.894   0.644  44.333  1.00 34.85           C
ANISOU 2886  CG  PHE B  98     4705   4322   4214   -187    783    206       C
ATOM   2887  CD1 PHE B  98     -30.339   1.888  43.906  1.00 36.56           C
ANISOU 2887  CD1 PHE B  98     4820   4568   4502   -188    781    203       C
ATOM   2888  CD2 PHE B  98     -29.082   0.590  45.450  1.00 35.22           C
ANISOU 2888  CD2 PHE B  98     4871   4346   4164   -150    791    200       C
ATOM   2889  CE1 PHE B  98     -29.928   3.062  44.542  1.00 36.75           C
ANISOU 2889  CE1 PHE B  98     4864   4600   4499   -154    786    193       C
ATOM   2890  CE2 PHE B  98     -28.653   1.760  46.088  1.00 38.78           C
ANISOU 2890  CE2 PHE B  98     5341   4806   4587   -118    790    189       C
ATOM   2891  CZ  PHE B  98     -29.081   3.005  45.625  1.00 37.63           C
ANISOU 2891  CZ  PHE B  98     5095   4690   4514   -121    790    185       C
ATOM   2892  N   CYS B  99     -28.591   0.779  41.273  1.00 36.36           N
ANISOU 2892  N   CYS B  99     4736   4625   4455   -179    561    201       N
ATOM   2893  CA  CYS B  99     -27.257   1.218  40.865  1.00 31.23           C
ANISOU 2893  CA  CYS B  99     4094   4014   3758   -138    473    191       C
ATOM   2894  C   CYS B  99     -26.606   1.836  42.079  1.00 31.35           C
ANISOU 2894  C   CYS B  99     4184   4021   3707   -100    491    181       C
ATOM   2895  O   CYS B  99     -26.967   2.940  42.486  1.00 33.81           O
ANISOU 2895  O   CYS B  99     4467   4334   4043    -96    524    176       O
ATOM   2896  CB  CYS B  99     -27.348   2.230  39.738  1.00 38.01           C
ANISOU 2896  CB  CYS B  99     4841   4918   4684   -142    423    188       C
ATOM   2897  SG  CYS B  99     -27.966   1.466  38.258  1.00 38.80           S
ANISOU 2897  SG  CYS B  99     4864   5028   4849   -184    386    198       S
ATOM   2898  N   SER B 100     -25.675   1.116  42.684  1.00 28.65           N
ANISOU 2898  N   SER B 100     3942   3666   3277    -72    470    179       N
ATOM   2899  CA  SER B 100     -24.990   1.630  43.849  1.00 30.03           C
ANISOU 2899  CA  SER B 100     4197   3832   3381    -36    477    170       C
ATOM   2900  C   SER B 100     -23.626   2.202  43.429  1.00 27.58           C
ANISOU 2900  C   SER B 100     3873   3571   3037      1    382    156       C
ATOM   2901  O   SER B 100     -23.428   2.577  42.274  1.00 26.39           O
ANISOU 2901  O   SER B 100     3636   3460   2933     -4    329    154       O
ATOM   2902  CB  SER B 100     -24.895   0.534  44.903  1.00 29.24           C
ANISOU 2902  CB  SER B 100     4221   3684   3206    -26    517    176       C
ATOM   2903  OG  SER B 100     -24.573   1.106  46.156  1.00 28.19           O
ANISOU 2903  OG  SER B 100     4166   3531   3012     -0    543    168       O
ATOM   2904  N   SER B 101     -22.709   2.362  44.377  1.00 26.99           N
ANISOU 2904  N   SER B 101     3880   3493   2882     37    363    147       N
ATOM   2905  CA  SER B 101     -21.484   3.103  44.100  1.00 27.42           C
ANISOU 2905  CA  SER B 101     3913   3594   2911     67    281    132       C
ATOM   2906  C   SER B 101     -20.330   2.460  44.840  1.00 26.78           C
ANISOU 2906  C   SER B 101     3928   3511   2736    108    238    128       C
ATOM   2907  O   SER B 101     -20.497   1.968  45.965  1.00 28.80           O
ANISOU 2907  O   SER B 101     4283   3724   2935    117    281    133       O
ATOM   2908  CB  SER B 101     -21.597   4.598  44.541  1.00 26.58           C
ANISOU 2908  CB  SER B 101     3783   3498   2819     66    299    117       C
ATOM   2909  OG  SER B 101     -20.339   5.271  44.429  1.00 26.29           O
ANISOU 2909  OG  SER B 101     3738   3502   2748     93    222    100       O
ATOM   2910  N   ASP B 102     -19.146   2.503  44.217  1.00 26.41           N
ANISOU 2910  N   ASP B 102     3854   3509   2674    134    152    121       N
ATOM   2911  CA  ASP B 102     -17.936   2.108  44.917  1.00 26.62           C
ANISOU 2911  CA  ASP B 102     3957   3542   2616    178    100    115       C
ATOM   2912  C   ASP B 102     -17.470   3.187  45.892  1.00 29.30           C
ANISOU 2912  C   ASP B 102     4331   3888   2914    191     89     97       C
ATOM   2913  O   ASP B 102     -16.629   2.904  46.760  1.00 32.04           O
ANISOU 2913  O   ASP B 102     4758   4231   3184    226     55     93       O
ATOM   2914  CB  ASP B 102     -16.843   1.754  43.900  1.00 26.23           C
ANISOU 2914  CB  ASP B 102     3860   3537   2569    202     17    113       C
ATOM   2915  CG  ASP B 102     -16.623   2.857  42.884  1.00 29.01           C
ANISOU 2915  CG  ASP B 102     4104   3936   2983    187    -19    100       C
ATOM   2916  OD1 ASP B 102     -17.359   3.872  42.975  1.00 27.11           O
ANISOU 2916  OD1 ASP B 102     3828   3691   2783    159     21     94       O
ATOM   2917  OD2 ASP B 102     -15.715   2.736  42.020  1.00 25.39           O
ANISOU 2917  OD2 ASP B 102     3600   3515   2532    204    -82     97       O
ATOM   2918  N   GLN B 103     -18.078   4.379  45.867  1.00 29.24           N
ANISOU 2918  N   GLN B 103     4273   3883   2952    165    124     88       N
ATOM   2919  CA  GLN B 103     -17.737   5.382  46.876  1.00 31.26           C
ANISOU 2919  CA  GLN B 103     4575   4136   3165    173    124     70       C
ATOM   2920  C   GLN B 103     -18.082   4.918  48.302  1.00 32.81           C
ANISOU 2920  C   GLN B 103     4897   4279   3292    183    178     76       C
ATOM   2921  O   GLN B 103     -17.606   5.535  49.273  1.00 27.93           O
ANISOU 2921  O   GLN B 103     4344   3655   2615    196    167     61       O
ATOM   2922  CB  GLN B 103     -18.435   6.697  46.550  1.00 26.75           C
ANISOU 2922  CB  GLN B 103     3933   3572   2658    144    162     62       C
ATOM   2923  CG  GLN B 103     -17.855   7.398  45.340  1.00 30.39           C
ANISOU 2923  CG  GLN B 103     4290   4086   3170    139    100     51       C
ATOM   2924  CD  GLN B 103     -16.499   8.041  45.615  1.00 35.45           C
ANISOU 2924  CD  GLN B 103     4943   4763   3762    160     25     29       C
ATOM   2925  OE1 GLN B 103     -16.196   8.451  46.743  1.00 36.74           O
ANISOU 2925  OE1 GLN B 103     5181   4912   3866    169     28     17       O
ATOM   2926  NE2 GLN B 103     -15.694   8.178  44.566  1.00 34.57           N
ANISOU 2926  NE2 GLN B 103     4757   4699   3678    165    -41     22       N
ATOM   2927  N   ILE B 104     -18.862   3.830  48.448  1.00 27.86           N
ANISOU 2927  N   ILE B 104     4312   3610   2665    175    236     95       N
ATOM   2928  CA  ILE B 104     -19.106   3.267  49.772  1.00 28.52           C
ANISOU 2928  CA  ILE B 104     4524   3638   2675    187    286    101       C
ATOM   2929  C   ILE B 104     -17.800   2.834  50.415  1.00 34.61           C
ANISOU 2929  C   ILE B 104     5380   4420   3352    233    209     95       C
ATOM   2930  O   ILE B 104     -17.666   2.839  51.650  1.00 37.10           O
ANISOU 2930  O   ILE B 104     5806   4700   3591    249    226     92       O
ATOM   2931  CB  ILE B 104     -20.090   2.080  49.674  1.00 33.27           C
ANISOU 2931  CB  ILE B 104     5150   4194   3296    168    357    123       C
ATOM   2932  CG1 ILE B 104     -21.430   2.510  49.040  1.00 28.57           C
ANISOU 2932  CG1 ILE B 104     4463   3591   2801    121    431    129       C
ATOM   2933  CG2 ILE B 104     -20.300   1.402  51.068  1.00 29.47           C
ANISOU 2933  CG2 ILE B 104     4817   3650   2731    181    413    130       C
ATOM   2934  CD1 ILE B 104     -22.481   1.472  49.091  1.00 28.90           C
ANISOU 2934  CD1 ILE B 104     4530   3585   2864     95    509    147       C
ATOM   2935  N   TYR B 105     -16.806   2.500  49.600  1.00 28.41           N
ANISOU 2935  N   TYR B 105     4542   3682   2570    255    122     94       N
ATOM   2936  CA  TYR B 105     -15.514   2.070  50.107  1.00 34.97           C
ANISOU 2936  CA  TYR B 105     5436   4531   3321    303     41     90       C
ATOM   2937  C   TYR B 105     -14.568   3.219  50.440  1.00 36.36           C
ANISOU 2937  C   TYR B 105     5596   4746   3472    314    -26     65       C
ATOM   2938  O   TYR B 105     -13.470   2.952  50.955  1.00 40.43           O
ANISOU 2938  O   TYR B 105     6162   5278   3920    354    -99     60       O
ATOM   2939  CB  TYR B 105     -14.834   1.129  49.080  1.00 33.14           C
ANISOU 2939  CB  TYR B 105     5155   4331   3105    327    -19    100       C
ATOM   2940  CG  TYR B 105     -15.605  -0.150  48.705  1.00 29.28           C
ANISOU 2940  CG  TYR B 105     4690   3803   2632    318     35    123       C
ATOM   2941  CD1 TYR B 105     -15.807  -1.157  49.631  1.00 28.97           C
ANISOU 2941  CD1 TYR B 105     4774   3711   2524    337     71    137       C
ATOM   2942  CD2 TYR B 105     -16.099  -0.353  47.397  1.00 29.40           C
ANISOU 2942  CD2 TYR B 105     4608   3834   2728    289     47    130       C
ATOM   2943  CE1 TYR B 105     -16.490  -2.323  49.285  1.00 35.44           C
ANISOU 2943  CE1 TYR B 105     5617   4491   3356    324    121    157       C
ATOM   2944  CE2 TYR B 105     -16.793  -1.516  47.038  1.00 27.96           C
ANISOU 2944  CE2 TYR B 105     4449   3616   2559    275     93    150       C
ATOM   2945  CZ  TYR B 105     -16.982  -2.503  47.984  1.00 34.60           C
ANISOU 2945  CZ  TYR B 105     5411   4403   3332    291    131    163       C
ATOM   2946  OH  TYR B 105     -17.667  -3.674  47.683  1.00 29.23           O
ANISOU 2946  OH  TYR B 105     4761   3682   2661    274    181    181       O
ATOM   2947  N   ASN B 106     -14.934   4.481  50.170  1.00 35.86           N
ANISOU 2947  N   ASN B 106     5466   4699   3460    281     -5     50       N
ATOM   2948  CA  ASN B 106     -13.879   5.495  50.210  1.00 37.66           C
ANISOU 2948  CA  ASN B 106     5662   4974   3675    289    -81     26       C
ATOM   2949  C   ASN B 106     -13.329   5.767  51.605  1.00 35.45           C
ANISOU 2949  C   ASN B 106     5493   4676   3302    308   -105     13       C
ATOM   2950  O   ASN B 106     -12.338   6.481  51.720  1.00 39.34           O
ANISOU 2950  O   ASN B 106     5966   5208   3772    316   -179     -8       O
ATOM   2951  CB  ASN B 106     -14.341   6.795  49.523  1.00 38.71           C
ANISOU 2951  CB  ASN B 106     5698   5127   3883    250    -56     13       C
ATOM   2952  CG  ASN B 106     -15.519   7.478  50.203  1.00 38.71           C
ANISOU 2952  CG  ASN B 106     5738   5078   3891    221     38     13       C
ATOM   2953  OD1 ASN B 106     -15.731   7.383  51.415  1.00 39.94           O
ANISOU 2953  OD1 ASN B 106     6003   5190   3982    228     74     13       O
ATOM   2954  ND2 ASN B 106     -16.285   8.206  49.404  1.00 33.10           N
ANISOU 2954  ND2 ASN B 106     4938   4374   3262    191     81     13       N
ATOM   2955  N   GLY B 107     -13.900   5.197  52.651  1.00 36.86           N
ANISOU 2955  N   GLY B 107     5788   4796   3421    316    -50     25       N
ATOM   2956  CA  GLY B 107     -13.431   5.494  53.986  1.00 38.25           C
ANISOU 2956  CA  GLY B 107     6079   4949   3504    333    -71     13       C
ATOM   2957  C   GLY B 107     -12.512   4.391  54.459  1.00 39.98           C
ANISOU 2957  C   GLY B 107     6373   5171   3646    383   -141     21       C
ATOM   2958  O   GLY B 107     -11.719   4.560  55.392  1.00 44.64           O
ANISOU 2958  O   GLY B 107     7043   5763   4156    408   -200     10       O
ATOM   2959  N   ASN B 108     -12.593   3.257  53.776  1.00 39.61           N
ANISOU 2959  N   ASN B 108     6301   5125   3623    400   -139     42       N
ATOM   2960  CA  ASN B 108     -11.820   2.085  54.146  1.00 39.31           C
ANISOU 2960  CA  ASN B 108     6336   5084   3516    453   -195     55       C
ATOM   2961  C   ASN B 108     -10.313   2.323  54.073  1.00 39.09           C
ANISOU 2961  C   ASN B 108     6272   5119   3463    489   -318     40       C
ATOM   2962  O   ASN B 108      -9.796   2.921  53.131  1.00 42.73           O
ANISOU 2962  O   ASN B 108     6612   5637   3986    477   -364     27       O
ATOM   2963  CB  ASN B 108     -12.225   0.927  53.248  1.00 38.05           C
ANISOU 2963  CB  ASN B 108     6142   4916   3400    458   -164     79       C
ATOM   2964  CG  ASN B 108     -13.514   0.301  53.688  1.00 41.95           C
ANISOU 2964  CG  ASN B 108     6715   5338   3888    436    -54     97       C
ATOM   2965  OD1 ASN B 108     -14.594   0.638  53.188  1.00 39.95           O
ANISOU 2965  OD1 ASN B 108     6404   5070   3706    390     24    100       O
ATOM   2966  ND2 ASN B 108     -13.421  -0.588  54.668  1.00 39.68           N
ANISOU 2966  ND2 ASN B 108     6562   5003   3513    470    -45    110       N
ATOM   2967  N   ALA B 109      -9.609   1.858  55.099  1.00 42.40           N
ANISOU 2967  N   ALA B 109     6798   5524   3787    533   -372     41       N
ATOM   2968  CA  ALA B 109      -8.163   2.015  55.194  1.00 44.39           C
ANISOU 2968  CA  ALA B 109     7025   5834   4007    571   -494     27       C
ATOM   2969  C   ALA B 109      -7.386   0.817  54.670  1.00 39.15           C
ANISOU 2969  C   ALA B 109     6341   5195   3339    626   -552     46       C
ATOM   2970  O   ALA B 109      -6.158   0.888  54.597  1.00 41.30           O
ANISOU 2970  O   ALA B 109     6573   5522   3599    661   -654     36       O
ATOM   2971  CB  ALA B 109      -7.749   2.287  56.638  1.00 42.70           C
ANISOU 2971  CB  ALA B 109     6937   5597   3690    590   -533     16       C
ATOM   2972  N   GLU B 110      -8.053  -0.288  54.366  1.00 39.06           N
ANISOU 2972  N   GLU B 110     6363   5143   3334    636   -491     72       N
ATOM   2973  CA  GLU B 110      -7.369  -1.455  53.832  1.00 41.16           C
ANISOU 2973  CA  GLU B 110     6617   5427   3597    689   -538     90       C
ATOM   2974  C   GLU B 110      -6.834  -1.158  52.418  1.00 42.57           C
ANISOU 2974  C   GLU B 110     6637   5671   3866    680   -576     83       C
ATOM   2975  O   GLU B 110      -7.223  -0.185  51.769  1.00 41.38           O
ANISOU 2975  O   GLU B 110     6394   5543   3786    629   -550     68       O
ATOM   2976  CB  GLU B 110      -8.321  -2.664  53.829  1.00 40.43           C
ANISOU 2976  CB  GLU B 110     6603   5267   3490    692   -451    118       C
ATOM   2977  CG  GLU B 110      -8.923  -3.054  55.214  1.00 42.75           C
ANISOU 2977  CG  GLU B 110     7065   5487   3693    700   -399    128       C
ATOM   2978  CD  GLU B 110     -10.148  -2.201  55.613  1.00 44.28           C
ANISOU 2978  CD  GLU B 110     7278   5640   3907    636   -302    118       C
ATOM   2979  OE1 GLU B 110     -10.735  -2.413  56.710  1.00 45.14           O
ANISOU 2979  OE1 GLU B 110     7519   5684   3948    634   -245    124       O
ATOM   2980  OE2 GLU B 110     -10.533  -1.313  54.822  1.00 41.16           O
ANISOU 2980  OE2 GLU B 110     6766   5275   3596    587   -279    105       O
ATOM   2981  N   LYS B 111      -5.899  -1.989  51.955  1.00 42.94           N
ANISOU 2981  N   LYS B 111     6658   5748   3909    735   -639     94       N
ATOM   2982  CA  LYS B 111      -5.312  -1.844  50.629  1.00 43.91           C
ANISOU 2982  CA  LYS B 111     6643   5929   4112    733   -674     89       C
ATOM   2983  C   LYS B 111      -5.639  -3.053  49.752  1.00 43.28           C
ANISOU 2983  C   LYS B 111     6560   5827   4059    750   -633    115       C
ATOM   2984  O   LYS B 111      -5.990  -4.133  50.240  1.00 42.35           O
ANISOU 2984  O   LYS B 111     6547   5657   3887    778   -602    137       O
ATOM   2985  CB  LYS B 111      -3.792  -1.616  50.722  1.00 44.89           C
ANISOU 2985  CB  LYS B 111     6718   6118   4221    780   -787     76       C
ATOM   2986  CG  LYS B 111      -3.431  -0.335  51.462  1.00 45.54           C
ANISOU 2986  CG  LYS B 111     6792   6226   4284    755   -832     46       C
ATOM   2987  CD  LYS B 111      -2.042   0.137  51.109  1.00 49.46           C
ANISOU 2987  CD  LYS B 111     7188   6799   4806    777   -933     28       C
ATOM   2988  CE  LYS B 111      -0.979  -0.805  51.646  1.00 48.30           C
ANISOU 2988  CE  LYS B 111     7087   6666   4598    857  -1016     40       C
ATOM   2989  NZ  LYS B 111       0.355  -0.398  51.119  1.00 53.77           N
ANISOU 2989  NZ  LYS B 111     7661   7437   5334    878  -1108     23       N
ATOM   2990  N   GLY B 112      -5.547  -2.850  48.436  1.00 43.69           N
ANISOU 2990  N   GLY B 112     6493   5915   4191    729   -631    111       N
ATOM   2991  CA  GLY B 112      -5.805  -3.902  47.477  1.00 43.48           C
ANISOU 2991  CA  GLY B 112     6455   5871   4195    739   -598    133       C
ATOM   2992  C   GLY B 112      -7.286  -3.963  47.178  1.00 38.27           C
ANISOU 2992  C   GLY B 112     5810   5161   3569    679   -499    140       C
ATOM   2993  O   GLY B 112      -8.077  -3.319  47.857  1.00 37.23           O
ANISOU 2993  O   GLY B 112     5713   5004   3428    639   -455    133       O
ATOM   2994  N   PRO B 113      -7.704  -4.736  46.183  1.00 36.92           N
ANISOU 2994  N   PRO B 113     5617   4974   3436    670   -462    156       N
ATOM   2995  CA  PRO B 113      -9.138  -4.779  45.868  1.00 38.25           C
ANISOU 2995  CA  PRO B 113     5791   5100   3644    608   -372    162       C
ATOM   2996  C   PRO B 113      -9.975  -5.238  47.063  1.00 39.00           C
ANISOU 2996  C   PRO B 113     6011   5130   3678    602   -312    173       C
ATOM   2997  O   PRO B 113      -9.610  -6.169  47.782  1.00 38.04           O
ANISOU 2997  O   PRO B 113     5991   4978   3484    650   -324    187       O
ATOM   2998  CB  PRO B 113      -9.211  -5.742  44.682  1.00 38.05           C
ANISOU 2998  CB  PRO B 113     5738   5066   3653    611   -358    178       C
ATOM   2999  CG  PRO B 113      -7.835  -5.555  43.990  1.00 37.46           C
ANISOU 2999  CG  PRO B 113     5584   5054   3597    654   -440    171       C
ATOM   3000  CD  PRO B 113      -6.876  -5.355  45.133  1.00 40.04           C
ANISOU 3000  CD  PRO B 113     5955   5399   3858    706   -502    164       C
ATOM   3001  N   LEU B 114     -11.080  -4.516  47.296  1.00 37.71           N
ANISOU 3001  N   LEU B 114     5840   4945   3545    543   -247    166       N
ATOM   3002  CA  LEU B 114     -11.999  -4.696  48.417  1.00 35.33           C
ANISOU 3002  CA  LEU B 114     5643   4581   3198    526   -177    172       C
ATOM   3003  C   LEU B 114     -13.216  -5.523  47.991  1.00 36.15           C
ANISOU 3003  C   LEU B 114     5768   4634   3333    485    -90    189       C
ATOM   3004  O   LEU B 114     -13.713  -5.359  46.871  1.00 37.12           O
ANISOU 3004  O   LEU B 114     5797   4773   3534    445    -72    188       O
ATOM   3005  CB  LEU B 114     -12.456  -3.315  48.900  1.00 35.32           C
ANISOU 3005  CB  LEU B 114     5612   4589   3218    486   -155    152       C
ATOM   3006  CG  LEU B 114     -11.668  -2.573  49.996  1.00 42.74           C
ANISOU 3006  CG  LEU B 114     6599   5545   4095    515   -208    136       C
ATOM   3007  CD1 LEU B 114     -10.167  -2.632  49.836  1.00 40.78           C
ANISOU 3007  CD1 LEU B 114     6322   5352   3822    570   -316    130       C
ATOM   3008  CD2 LEU B 114     -12.053  -1.141  49.995  1.00 35.17           C
ANISOU 3008  CD2 LEU B 114     5575   4607   3182    470   -192    115       C
ATOM   3009  N   SER B 115     -13.710  -6.395  48.889  1.00 35.27           N
ANISOU 3009  N   SER B 115     5781   4459   3161    493    -36    204       N
ATOM   3010  CA  SER B 115     -14.889  -7.236  48.645  1.00 38.05           C
ANISOU 3010  CA  SER B 115     6166   4755   3537    451     52    219       C
ATOM   3011  C   SER B 115     -16.173  -6.646  49.270  1.00 41.15           C
ANISOU 3011  C   SER B 115     6573   5109   3952    395    143    214       C
ATOM   3012  O   SER B 115     -16.124  -5.778  50.157  1.00 39.70           O
ANISOU 3012  O   SER B 115     6415   4927   3742    398    145    202       O
ATOM   3013  CB  SER B 115     -14.680  -8.656  49.200  1.00 38.07           C
ANISOU 3013  CB  SER B 115     6300   4704   3459    492     65    239       C
ATOM   3014  OG  SER B 115     -13.913  -9.473  48.336  1.00 37.92           O
ANISOU 3014  OG  SER B 115     6262   4705   3440    529     13    249       O
ATOM   3015  N   GLU B 116     -17.341  -7.173  48.820  1.00 38.45           N
ANISOU 3015  N   GLU B 116     6219   4729   3659    342    222    224       N
ATOM   3016  CA  GLU B 116     -18.659  -6.680  49.266  1.00 37.49           C
ANISOU 3016  CA  GLU B 116     6096   4572   3577    285    317    221       C
ATOM   3017  C   GLU B 116     -18.949  -6.975  50.740  1.00 39.76           C
ANISOU 3017  C   GLU B 116     6526   4797   3784    297    377    226       C
ATOM   3018  O   GLU B 116     -19.850  -6.350  51.327  1.00 38.66           O
ANISOU 3018  O   GLU B 116     6393   4630   3665    261    451    221       O
ATOM   3019  CB  GLU B 116     -19.805  -7.278  48.426  1.00 32.97           C
ANISOU 3019  CB  GLU B 116     5475   3975   3076    226    382    231       C
ATOM   3020  CG  GLU B 116     -19.692  -7.093  46.918  1.00 34.42           C
ANISOU 3020  CG  GLU B 116     5528   4210   3338    206    332    228       C
ATOM   3021  CD  GLU B 116     -18.790  -8.137  46.319  1.00 34.06           C
ANISOU 3021  CD  GLU B 116     5511   4172   3257    245    274    237       C
ATOM   3022  OE1 GLU B 116     -18.614  -8.137  45.094  1.00 35.81           O
ANISOU 3022  OE1 GLU B 116     5645   4431   3532    234    234    236       O
ATOM   3023  OE2 GLU B 116     -18.251  -8.959  47.092  1.00 34.11           O
ANISOU 3023  OE2 GLU B 116     5634   4146   3180    290    270    247       O
ATOM   3024  N   ASP B 117     -18.259  -7.944  51.335  1.00 36.31           N
ANISOU 3024  N   ASP B 117     6208   4331   3257    348    353    237       N
ATOM   3025  CA  ASP B 117     -18.519  -8.316  52.721  1.00 42.16           C
ANISOU 3025  CA  ASP B 117     7100   5006   3914    362    411    244       C
ATOM   3026  C   ASP B 117     -17.806  -7.426  53.738  1.00 45.79           C
ANISOU 3026  C   ASP B 117     7608   5480   4310    401    365    231       C
ATOM   3027  O   ASP B 117     -18.127  -7.506  54.928  1.00 49.44           O
ANISOU 3027  O   ASP B 117     8192   5886   4706    406    419    233       O
ATOM   3028  CB  ASP B 117     -18.149  -9.775  52.963  1.00 43.32           C
ANISOU 3028  CB  ASP B 117     7366   5108   3987    401    409    263       C
ATOM   3029  CG  ASP B 117     -16.746 -10.097  52.516  1.00 44.63           C
ANISOU 3029  CG  ASP B 117     7517   5322   4118    468    295    265       C
ATOM   3030  OD1 ASP B 117     -16.043  -9.172  52.043  1.00 44.23           O
ANISOU 3030  OD1 ASP B 117     7364   5340   4101    481    218    251       O
ATOM   3031  OD2 ASP B 117     -16.347 -11.279  52.635  1.00 56.36           O
ANISOU 3031  OD2 ASP B 117     9096   6775   5544    508    286    282       O
ATOM   3032  N   ILE B 118     -16.816  -6.634  53.315  1.00 47.20           N
ANISOU 3032  N   ILE B 118     7702   5729   4502    428    267    217       N
ATOM   3033  CA  ILE B 118     -16.068  -5.789  54.245  1.00 47.69           C
ANISOU 3033  CA  ILE B 118     7808   5808   4503    461    213    203       C
ATOM   3034  C   ILE B 118     -16.935  -4.698  54.867  1.00 42.18           C
ANISOU 3034  C   ILE B 118     7111   5090   3826    417    284    190       C
ATOM   3035  O   ILE B 118     -17.783  -4.083  54.203  1.00 43.95           O
ANISOU 3035  O   ILE B 118     7230   5326   4141    365    334    185       O
ATOM   3036  CB  ILE B 118     -14.841  -5.211  53.511  1.00 48.44           C
ANISOU 3036  CB  ILE B 118     7798   5987   4621    492     95    190       C
ATOM   3037  CG1 ILE B 118     -13.774  -6.311  53.363  1.00 49.15           C
ANISOU 3037  CG1 ILE B 118     7932   6087   4657    557     21    204       C
ATOM   3038  CG2 ILE B 118     -14.391  -3.856  54.065  1.00 49.67           C
ANISOU 3038  CG2 ILE B 118     7933   6176   4764    493     53    167       C
ATOM   3039  CD1 ILE B 118     -12.611  -6.018  52.427  1.00 52.64           C
ANISOU 3039  CD1 ILE B 118     8261   6606   5133    587    -84    195       C
ATOM   3040  N   ASP B 119     -16.680  -4.425  56.148  1.00 41.65           N
ANISOU 3040  N   ASP B 119     7161   4991   3672    441    285    185       N
ATOM   3041  CA  ASP B 119     -17.369  -3.345  56.850  1.00 43.04           C
ANISOU 3041  CA  ASP B 119     7354   5146   3855    407    348    171       C
ATOM   3042  C   ASP B 119     -16.993  -2.004  56.236  1.00 40.94           C
ANISOU 3042  C   ASP B 119     6956   4949   3651    392    291    150       C
ATOM   3043  O   ASP B 119     -15.823  -1.720  55.962  1.00 39.93           O
ANISOU 3043  O   ASP B 119     6787   4879   3507    425    183    140       O
ATOM   3044  CB  ASP B 119     -17.018  -3.330  58.340  1.00 36.90           C
ANISOU 3044  CB  ASP B 119     6739   4321   2960    440    347    169       C
ATOM   3045  CG  ASP B 119     -17.720  -4.416  59.106  1.00 44.24           C
ANISOU 3045  CG  ASP B 119     7811   5165   3832    441    438    188       C
ATOM   3046  OD1 ASP B 119     -18.698  -4.965  58.566  1.00 51.61           O
ANISOU 3046  OD1 ASP B 119     8708   6072   4829    402    523    200       O
ATOM   3047  OD2 ASP B 119     -17.302  -4.723  60.240  1.00 41.41           O
ANISOU 3047  OD2 ASP B 119     7603   4765   3366    479    426    191       O
ATOM   3048  N   VAL B 120     -17.992  -1.168  56.043  1.00 42.42           N
ANISOU 3048  N   VAL B 120     7079   5129   3910    341    367    144       N
ATOM   3049  CA  VAL B 120     -17.807   0.058  55.295  1.00 41.32           C
ANISOU 3049  CA  VAL B 120     6807   5050   3842    322    327    126       C
ATOM   3050  C   VAL B 120     -18.232   1.235  56.149  1.00 40.94           C
ANISOU 3050  C   VAL B 120     6796   4979   3780    302    377    111       C
ATOM   3051  O   VAL B 120     -19.030   1.100  57.084  1.00 39.99           O
ANISOU 3051  O   VAL B 120     6775   4793   3626    290    469    117       O
ATOM   3052  CB  VAL B 120     -18.594  -0.012  53.970  1.00 39.57           C
ANISOU 3052  CB  VAL B 120     6450   4851   3735    281    363    133       C
ATOM   3053  CG1 VAL B 120     -17.850  -0.912  52.959  1.00 33.78           C
ANISOU 3053  CG1 VAL B 120     5664   4157   3014    305    286    142       C
ATOM   3054  CG2 VAL B 120     -19.964  -0.570  54.215  1.00 31.25           C
ANISOU 3054  CG2 VAL B 120     5432   3733   2708    245    484    148       C
ATOM   3055  N   HIS B 121     -17.644   2.389  55.849  1.00 41.04           N
ANISOU 3055  N   HIS B 121     6734   5045   3815    300    315     91       N
ATOM   3056  CA  HIS B 121     -17.961   3.649  56.508  1.00 38.10           C
ANISOU 3056  CA  HIS B 121     6383   4657   3437    280    353     74       C
ATOM   3057  C   HIS B 121     -17.580   4.786  55.571  1.00 40.78           C
ANISOU 3057  C   HIS B 121     6587   5063   3847    264    299     56       C
ATOM   3058  O   HIS B 121     -16.503   5.376  55.715  1.00 42.71           O
ANISOU 3058  O   HIS B 121     6829   5346   4052    281    210     38       O
ATOM   3059  CB  HIS B 121     -17.246   3.798  57.851  1.00 36.01           C
ANISOU 3059  CB  HIS B 121     6261   4366   3055    310    318     63       C
ATOM   3060  CG  HIS B 121     -15.868   3.226  57.865  1.00 41.74           C
ANISOU 3060  CG  HIS B 121     7011   5132   3718    356    195     61       C
ATOM   3061  ND1 HIS B 121     -15.612   1.899  58.142  1.00 51.80           N
ANISOU 3061  ND1 HIS B 121     8366   6381   4935    391    181     79       N
ATOM   3062  CD2 HIS B 121     -14.668   3.792  57.603  1.00 45.92           C
ANISOU 3062  CD2 HIS B 121     7487   5723   4236    373     82     43       C
ATOM   3063  CE1 HIS B 121     -14.311   1.679  58.067  1.00 45.06           C
ANISOU 3063  CE1 HIS B 121     7507   5574   4038    433     62     74       C
ATOM   3064  NE2 HIS B 121     -13.717   2.809  57.731  1.00 39.66           N
ANISOU 3064  NE2 HIS B 121     6739   4946   3384    421      0     51       N
ATOM   3065  N   PRO B 122     -18.422   5.112  54.596  1.00 39.13           N
ANISOU 3065  N   PRO B 122     6261   4866   3739    231    347     61       N
ATOM   3066  CA  PRO B 122     -18.076   6.167  53.647  1.00 43.36           C
ANISOU 3066  CA  PRO B 122     6673   5462   4341    217    297     46       C
ATOM   3067  C   PRO B 122     -17.909   7.502  54.365  1.00 52.03           C
ANISOU 3067  C   PRO B 122     7804   6555   5411    209    301     24       C
ATOM   3068  O   PRO B 122     -18.362   7.686  55.497  1.00 50.65           O
ANISOU 3068  O   PRO B 122     7737   6326   5183    207    365     23       O
ATOM   3069  CB  PRO B 122     -19.264   6.170  52.678  1.00 40.61           C
ANISOU 3069  CB  PRO B 122     6221   5110   4099    183    368     60       C
ATOM   3070  CG  PRO B 122     -20.364   5.586  53.441  1.00 41.42           C
ANISOU 3070  CG  PRO B 122     6402   5145   4190    171    475     75       C
ATOM   3071  CD  PRO B 122     -19.759   4.564  54.347  1.00 39.87           C
ANISOU 3071  CD  PRO B 122     6336   4920   3893    203    451     81       C
ATOM   3072  N   VAL B 123     -17.174   8.418  53.723  1.00 62.39           N
ANISOU 3072  N   VAL B 123     9033   7923   6751    205    230      6       N
ATOM   3073  CA  VAL B 123     -16.769   9.670  54.366  1.00 65.02           C
ANISOU 3073  CA  VAL B 123     9400   8257   7047    198    215    -19       C
ATOM   3074  C   VAL B 123     -17.456  10.914  53.802  1.00 61.26           C
ANISOU 3074  C   VAL B 123     8840   7787   6650    166    265    -27       C
ATOM   3075  O   VAL B 123     -17.390  11.974  54.442  1.00 62.17           O
ANISOU 3075  O   VAL B 123     8999   7888   6736    156    279    -45       O
ATOM   3076  CB  VAL B 123     -15.233   9.858  54.326  1.00 65.67           C
ANISOU 3076  CB  VAL B 123     9476   8394   7083    217     89    -39       C
ATOM   3077  CG1 VAL B 123     -14.534   8.769  55.147  1.00 60.38           C
ANISOU 3077  CG1 VAL B 123     8911   7711   6320    255     39    -32       C
ATOM   3078  CG2 VAL B 123     -14.705   9.901  52.875  1.00 62.50           C
ANISOU 3078  CG2 VAL B 123     8932   8058   6757    214     26    -40       C
ATOM   3079  N   ASN B 124     -18.110  10.836  52.656  1.00 47.60           N
ANISOU 3079  N   ASN B 124     6997   6075   5013    152    292    -13       N
ATOM   3080  CA  ASN B 124     -18.835  11.977  52.135  1.00 47.39           C
ANISOU 3080  CA  ASN B 124     6894   6050   5061    127    342    -18       C
ATOM   3081  C   ASN B 124     -20.317  11.635  52.021  1.00 46.50           C
ANISOU 3081  C   ASN B 124     6761   5896   5011    113    450      5       C
ATOM   3082  O   ASN B 124     -20.728  10.488  52.180  1.00 46.37           O
ANISOU 3082  O   ASN B 124     6776   5856   4988    117    479     23       O
ATOM   3083  CB  ASN B 124     -18.253  12.433  50.790  1.00 44.09           C
ANISOU 3083  CB  ASN B 124     6352   5696   4706    121    270    -25       C
ATOM   3084  CG  ASN B 124     -18.259  11.348  49.741  1.00 44.46           C
ANISOU 3084  CG  ASN B 124     6326   5769   4797    126    240     -7       C
ATOM   3085  OD1 ASN B 124     -19.045  10.382  49.805  1.00 41.46           O
ANISOU 3085  OD1 ASN B 124     5963   5360   4431    126    292     14       O
ATOM   3086  ND2 ASN B 124     -17.372  11.495  48.749  1.00 45.81           N
ANISOU 3086  ND2 ASN B 124     6418   5996   4993    129    158    -16       N
ATOM   3087  N   VAL B 125     -21.131  12.654  51.749  1.00 45.73           N
ANISOU 3087  N   VAL B 125     6609   5790   4977     96    511      4       N
ATOM   3088  CA  VAL B 125     -22.575  12.464  51.784  1.00 41.74           C
ANISOU 3088  CA  VAL B 125     6084   5243   4533     83    619     24       C
ATOM   3089  C   VAL B 125     -23.042  11.521  50.672  1.00 42.21           C
ANISOU 3089  C   VAL B 125     6048   5325   4665     74    610     44       C
ATOM   3090  O   VAL B 125     -24.011  10.766  50.856  1.00 42.17           O
ANISOU 3090  O   VAL B 125     6052   5284   4686     64    683     62       O
ATOM   3091  CB  VAL B 125     -23.248  13.843  51.725  1.00 46.63           C
ANISOU 3091  CB  VAL B 125     6663   5850   5202     72    679     18       C
ATOM   3092  CG1 VAL B 125     -24.731  13.733  51.942  1.00 52.25           C
ANISOU 3092  CG1 VAL B 125     7362   6516   5974     62    798     37       C
ATOM   3093  CG2 VAL B 125     -22.636  14.764  52.791  1.00 44.37           C
ANISOU 3093  CG2 VAL B 125     6480   5543   4835     78    676     -5       C
ATOM   3094  N   TYR B 126     -22.376  11.530  49.510  1.00 38.38           N
ANISOU 3094  N   TYR B 126     5474   4896   4212     75    524     40       N
ATOM   3095  CA  TYR B 126     -22.790  10.651  48.407  1.00 42.32           C
ANISOU 3095  CA  TYR B 126     5888   5415   4777     65    511     58       C
ATOM   3096  C   TYR B 126     -22.623   9.173  48.764  1.00 38.92           C
ANISOU 3096  C   TYR B 126     5522   4966   4299     72    505     70       C
ATOM   3097  O   TYR B 126     -23.500   8.349  48.486  1.00 30.56           O
ANISOU 3097  O   TYR B 126     4440   3887   3282     57    552     88       O
ATOM   3098  CB  TYR B 126     -21.965  10.939  47.162  1.00 39.83           C
ANISOU 3098  CB  TYR B 126     5483   5160   4492     68    417     50       C
ATOM   3099  CG  TYR B 126     -22.360  10.186  45.908  1.00 38.37           C
ANISOU 3099  CG  TYR B 126     5208   4996   4374     56    398     67       C
ATOM   3100  CD1 TYR B 126     -23.450  10.606  45.128  1.00 33.68           C
ANISOU 3100  CD1 TYR B 126     4522   4403   3871     36    439     78       C
ATOM   3101  CD2 TYR B 126     -21.630   9.046  45.484  1.00 36.19           C
ANISOU 3101  CD2 TYR B 126     4941   4740   4070     66    335     71       C
ATOM   3102  CE1 TYR B 126     -23.779   9.943  43.941  1.00 33.03           C
ANISOU 3102  CE1 TYR B 126     4361   4341   3848     23    413     91       C
ATOM   3103  CE2 TYR B 126     -21.960   8.362  44.295  1.00 26.20           C
ANISOU 3103  CE2 TYR B 126     3599   3492   2862     53    315     85       C
ATOM   3104  CZ  TYR B 126     -23.034   8.816  43.542  1.00 30.77           C
ANISOU 3104  CZ  TYR B 126     4092   4072   3529     29    352     95       C
ATOM   3105  OH  TYR B 126     -23.414   8.180  42.392  1.00 31.87           O
ANISOU 3105  OH  TYR B 126     4161   4226   3723     13    331    107       O
ATOM   3106  N   GLY B 127     -21.463   8.812  49.308  1.00 37.74           N
ANISOU 3106  N   GLY B 127     5450   4826   4063     96    441     60       N
ATOM   3107  CA  GLY B 127     -21.261   7.449  49.744  1.00 34.94           C
ANISOU 3107  CA  GLY B 127     5172   4450   3655    109    437     71       C
ATOM   3108  C   GLY B 127     -22.170   7.116  50.898  1.00 35.13           C
ANISOU 3108  C   GLY B 127     5291   4407   3650    102    538     80       C
ATOM   3109  O   GLY B 127     -22.799   6.046  50.922  1.00 34.44           O
ANISOU 3109  O   GLY B 127     5225   4290   3572     93    584     98       O
ATOM   3110  N   LYS B 128     -22.279   8.040  51.852  1.00 35.36           N
ANISOU 3110  N   LYS B 128     5381   4410   3645    104    578     69       N
ATOM   3111  CA  LYS B 128     -23.143   7.829  53.008  1.00 40.36           C
ANISOU 3111  CA  LYS B 128     6113   4974   4247     98    683     76       C
ATOM   3112  C   LYS B 128     -24.560   7.459  52.591  1.00 38.77           C
ANISOU 3112  C   LYS B 128     5849   4748   4135     69    778     95       C
ATOM   3113  O   LYS B 128     -25.085   6.429  53.015  1.00 39.68           O
ANISOU 3113  O   LYS B 128     6021   4821   4235     62    834    109       O
ATOM   3114  CB  LYS B 128     -23.147   9.075  53.891  1.00 37.53           C
ANISOU 3114  CB  LYS B 128     5810   4593   3855    100    718     60       C
ATOM   3115  CG  LYS B 128     -22.061   9.036  54.968  1.00 41.42           C
ANISOU 3115  CG  LYS B 128     6435   5075   4229    126    665     45       C
ATOM   3116  CD  LYS B 128     -21.926  10.334  55.727  1.00 45.09           C
ANISOU 3116  CD  LYS B 128     6952   5524   4657    125    683     25       C
ATOM   3117  CE  LYS B 128     -20.611  10.353  56.490  1.00 45.25           C
ANISOU 3117  CE  LYS B 128     7072   5554   4568    148    593      8       C
ATOM   3118  NZ  LYS B 128     -20.581   9.375  57.626  1.00 40.35           N
ANISOU 3118  NZ  LYS B 128     6597   4880   3855    166    618     16       N
ATOM   3119  N   HIS B 129     -25.157   8.233  51.688  1.00 37.29           N
ANISOU 3119  N   HIS B 129     5538   4587   4042     51    790     96       N
ATOM   3120  CA  HIS B 129     -26.553   7.995  51.318  1.00 43.60           C
ANISOU 3120  CA  HIS B 129     6269   5365   4933     23    879    113       C
ATOM   3121  C   HIS B 129     -26.687   6.788  50.384  1.00 38.98           C
ANISOU 3121  C   HIS B 129     5626   4798   4386      8    847    127       C
ATOM   3122  O   HIS B 129     -27.712   6.082  50.407  1.00 37.69           O
ANISOU 3122  O   HIS B 129     5452   4602   4266    -17    921    142       O
ATOM   3123  CB  HIS B 129     -27.191   9.276  50.736  1.00 51.66           C
ANISOU 3123  CB  HIS B 129     7184   6405   6041     14    905    110       C
ATOM   3124  CG  HIS B 129     -27.541  10.309  51.784  1.00 65.95           C
ANISOU 3124  CG  HIS B 129     9057   8174   7827     21    982    102       C
ATOM   3125  ND1 HIS B 129     -26.971  11.567  51.821  1.00 64.04           N
ANISOU 3125  ND1 HIS B 129     8814   7952   7569     35    947     85       N
ATOM   3126  CD2 HIS B 129     -28.382  10.254  52.848  1.00 76.35           C
ANISOU 3126  CD2 HIS B 129    10450   9428   9132     16   1096    108       C
ATOM   3127  CE1 HIS B 129     -27.449  12.240  52.855  1.00 71.12           C
ANISOU 3127  CE1 HIS B 129     9782   8799   8441     38   1034     81       C
ATOM   3128  NE2 HIS B 129     -28.308  11.467  53.495  1.00 81.45           N
ANISOU 3128  NE2 HIS B 129    11138  10056   9752     28   1126     95       N
ATOM   3129  N   LYS B 130     -25.692   6.537  49.535  1.00 35.40           N
ANISOU 3129  N   LYS B 130     5135   4395   3920     20    740    123       N
ATOM   3130  CA  LYS B 130     -25.770   5.333  48.722  1.00 36.54           C
ANISOU 3130  CA  LYS B 130     5244   4550   4090      8    712    136       C
ATOM   3131  C   LYS B 130     -25.788   4.078  49.602  1.00 35.05           C
ANISOU 3131  C   LYS B 130     5172   4312   3832     11    751    145       C
ATOM   3132  O   LYS B 130     -26.538   3.131  49.327  1.00 34.89           O
ANISOU 3132  O   LYS B 130     5139   4270   3847    -15    794    159       O
ATOM   3133  CB  LYS B 130     -24.620   5.299  47.724  1.00 34.44           C
ANISOU 3133  CB  LYS B 130     4928   4343   3815     25    595    129       C
ATOM   3134  CG  LYS B 130     -24.824   6.208  46.536  1.00 31.83           C
ANISOU 3134  CG  LYS B 130     4468   4056   3568     13    563    126       C
ATOM   3135  CD  LYS B 130     -25.651   5.558  45.437  1.00 30.76           C
ANISOU 3135  CD  LYS B 130     4244   3928   3514    -18    570    141       C
ATOM   3136  CE  LYS B 130     -25.736   6.515  44.233  1.00 30.63           C
ANISOU 3136  CE  LYS B 130     4108   3957   3572    -24    526    137       C
ATOM   3137  NZ  LYS B 130     -26.646   6.100  43.128  1.00 30.96           N
ANISOU 3137  NZ  LYS B 130     4055   4008   3700    -55    531    151       N
ATOM   3138  N   LEU B 131     -25.004   4.055  50.685  1.00 35.21           N
ANISOU 3138  N   LEU B 131     5313   4312   3753     41    738    137       N
ATOM   3139  CA  LEU B 131     -25.039   2.878  51.554  1.00 38.03           C
ANISOU 3139  CA  LEU B 131     5792   4617   4040     47    777    146       C
ATOM   3140  C   LEU B 131     -26.404   2.720  52.231  1.00 39.90           C
ANISOU 3140  C   LEU B 131     6061   4793   4308     16    909    156       C
ATOM   3141  O   LEU B 131     -26.945   1.610  52.286  1.00 37.06           O
ANISOU 3141  O   LEU B 131     5733   4398   3952     -3    957    170       O
ATOM   3142  CB  LEU B 131     -23.919   2.931  52.596  1.00 38.21           C
ANISOU 3142  CB  LEU B 131     5939   4630   3947     88    731    136       C
ATOM   3143  CG  LEU B 131     -23.850   1.899  53.731  1.00 31.15           C
ANISOU 3143  CG  LEU B 131     5199   3677   2961    104    771    144       C
ATOM   3144  CD1 LEU B 131     -23.974   0.479  53.207  1.00 31.14           C
ANISOU 3144  CD1 LEU B 131     5201   3665   2966     97    768    161       C
ATOM   3145  CD2 LEU B 131     -22.553   2.065  54.505  1.00 31.29           C
ANISOU 3145  CD2 LEU B 131     5316   3703   2871    149    691    132       C
ATOM   3146  N   GLU B 132     -26.992   3.816  52.726  1.00 38.08           N
ANISOU 3146  N   GLU B 132     5819   4546   4104      9    973    150       N
ATOM   3147  CA  GLU B 132     -28.257   3.696  53.458  1.00 37.78           C
ANISOU 3147  CA  GLU B 132     5816   4446   4093    -17   1107    159       C
ATOM   3148  C   GLU B 132     -29.396   3.213  52.560  1.00 36.85           C
ANISOU 3148  C   GLU B 132     5584   4332   4086    -59   1154    173       C
ATOM   3149  O   GLU B 132     -30.211   2.384  52.992  1.00 37.30           O
ANISOU 3149  O   GLU B 132     5683   4339   4152    -84   1242    184       O
ATOM   3150  CB  GLU B 132     -28.618   5.013  54.153  1.00 36.85           C
ANISOU 3150  CB  GLU B 132     5711   4309   3981    -11   1167    150       C
ATOM   3151  CG  GLU B 132     -27.975   5.160  55.542  1.00 46.28           C
ANISOU 3151  CG  GLU B 132     7069   5461   5055     17   1179    140       C
ATOM   3152  CD  GLU B 132     -28.153   3.909  56.415  1.00 53.89           C
ANISOU 3152  CD  GLU B 132     8163   6362   5950     16   1236    151       C
ATOM   3153  OE1 GLU B 132     -27.123   3.369  56.921  1.00 50.41           O
ANISOU 3153  OE1 GLU B 132     7831   5916   5405     46   1170    147       O
ATOM   3154  OE2 GLU B 132     -29.323   3.489  56.612  1.00 56.63           O
ANISOU 3154  OE2 GLU B 132     8505   6663   6347    -15   1349    163       O
ATOM   3155  N   ALA B 133     -29.450   3.672  51.305  1.00 34.50           N
ANISOU 3155  N   ALA B 133     5147   4092   3871    -68   1094    173       N
ATOM   3156  CA  ALA B 133     -30.422   3.110  50.365  1.00 41.34           C
ANISOU 3156  CA  ALA B 133     5906   4966   4836   -109   1119    185       C
ATOM   3157  C   ALA B 133     -30.175   1.608  50.129  1.00 44.46           C
ANISOU 3157  C   ALA B 133     6347   5349   5196   -121   1094    194       C
ATOM   3158  O   ALA B 133     -31.118   0.802  50.124  1.00 42.02           O
ANISOU 3158  O   ALA B 133     6030   5006   4928   -159   1165    205       O
ATOM   3159  CB  ALA B 133     -30.387   3.893  49.052  1.00 30.53           C
ANISOU 3159  CB  ALA B 133     4391   3660   3547   -112   1046    183       C
ATOM   3160  N   GLU B 134     -28.907   1.214  49.971  1.00 38.81           N
ANISOU 3160  N   GLU B 134     5684   4657   4404    -89    998    189       N
ATOM   3161  CA  GLU B 134     -28.560  -0.189  49.769  1.00 37.54           C
ANISOU 3161  CA  GLU B 134     5579   4484   4202    -92    971    197       C
ATOM   3162  C   GLU B 134     -29.022  -1.043  50.957  1.00 44.75           C
ANISOU 3162  C   GLU B 134     6621   5323   5059   -101   1067    205       C
ATOM   3163  O   GLU B 134     -29.652  -2.088  50.768  1.00 48.11           O
ANISOU 3163  O   GLU B 134     7054   5719   5507   -135   1112    216       O
ATOM   3164  CB  GLU B 134     -27.036  -0.270  49.524  1.00 37.80           C
ANISOU 3164  CB  GLU B 134     5647   4556   4159    -46    852    190       C
ATOM   3165  CG  GLU B 134     -26.395  -1.596  49.128  1.00 38.04           C
ANISOU 3165  CG  GLU B 134     5724   4585   4143    -36    800    198       C
ATOM   3166  CD  GLU B 134     -24.849  -1.522  48.908  1.00 31.67           C
ANISOU 3166  CD  GLU B 134     4940   3823   3270     16    683    190       C
ATOM   3167  OE1 GLU B 134     -24.368  -1.197  47.801  1.00 29.15           O
ANISOU 3167  OE1 GLU B 134     4526   3559   2991     20    606    185       O
ATOM   3168  OE2 GLU B 134     -24.099  -1.818  49.871  1.00 34.34           O
ANISOU 3168  OE2 GLU B 134     5396   4139   3512     54    669    188       O
ATOM   3169  N   ARG B 135     -28.786  -0.589  52.191  1.00 43.67           N
ANISOU 3169  N   ARG B 135     6590   5151   4850    -74   1106    199       N
ATOM   3170  CA  ARG B 135     -29.180  -1.399  53.346  1.00 43.43           C
ANISOU 3170  CA  ARG B 135     6696   5046   4758    -80   1199    207       C
ATOM   3171  C   ARG B 135     -30.699  -1.473  53.478  1.00 47.27           C
ANISOU 3171  C   ARG B 135     7140   5492   5330   -132   1328    214       C
ATOM   3172  O   ARG B 135     -31.253  -2.535  53.806  1.00 53.49           O
ANISOU 3172  O   ARG B 135     7989   6228   6109   -159   1398    224       O
ATOM   3173  CB  ARG B 135     -28.556  -0.841  54.628  1.00 41.16           C
ANISOU 3173  CB  ARG B 135     6538   4730   4370    -39   1207    198       C
ATOM   3174  N   LYS B 136     -31.389  -0.362  53.192  1.00 43.80           N
ANISOU 3174  N   LYS B 136     6590   5074   4978   -147   1359    210       N
ATOM   3175  CA  LYS B 136     -32.845  -0.346  53.252  1.00 47.43           C
ANISOU 3175  CA  LYS B 136     6988   5502   5532   -194   1478    218       C
ATOM   3176  C   LYS B 136     -33.463  -1.222  52.170  1.00 53.67           C
ANISOU 3176  C   LYS B 136     7680   6309   6404   -241   1469    227       C
ATOM   3177  O   LYS B 136     -34.427  -1.953  52.431  1.00 60.85           O
ANISOU 3177  O   LYS B 136     8600   7172   7349   -284   1564    235       O
ATOM   3178  CB  LYS B 136     -33.355   1.086  53.134  1.00 43.67           C
ANISOU 3178  CB  LYS B 136     6413   5050   5130   -190   1503    213       C
ATOM   3179  CG  LYS B 136     -34.865   1.207  52.995  1.00 48.46           C
ANISOU 3179  CG  LYS B 136     6923   5637   5854   -236   1613    221       C
ATOM   3180  CD  LYS B 136     -35.612   0.384  54.031  1.00 53.05           C
ANISOU 3180  CD  LYS B 136     7605   6140   6413   -262   1744    228       C
ATOM   3181  CE  LYS B 136     -35.233   0.772  55.446  1.00 47.57           C
ANISOU 3181  CE  LYS B 136     7066   5391   5616   -228   1801    223       C
ATOM   3182  NZ  LYS B 136     -35.668   2.150  55.688  1.00 57.64           N
ANISOU 3182  NZ  LYS B 136     8289   6673   6939   -214   1847    218       N
ATOM   3183  N   LEU B 137     -32.914  -1.186  50.958  1.00 52.01           N
ANISOU 3183  N   LEU B 137     7377   6161   6222   -236   1355    225       N
ATOM   3184  CA  LEU B 137     -33.463  -2.031  49.906  1.00 52.73           C
ANISOU 3184  CA  LEU B 137     7383   6268   6385   -282   1340    233       C
ATOM   3185  C   LEU B 137     -33.374  -3.494  50.304  1.00 58.06           C
ANISOU 3185  C   LEU B 137     8172   6891   6996   -298   1370    239       C
ATOM   3186  O   LEU B 137     -34.315  -4.259  50.076  1.00 57.52           O
ANISOU 3186  O   LEU B 137     8074   6796   6984   -351   1432    246       O
ATOM   3187  CB  LEU B 137     -32.736  -1.788  48.584  1.00 48.20           C
ANISOU 3187  CB  LEU B 137     6715   5764   5833   -268   1209    229       C
ATOM   3188  CG  LEU B 137     -33.096  -0.473  47.896  1.00 44.91           C
ANISOU 3188  CG  LEU B 137     6160   5397   5505   -267   1184    225       C
ATOM   3189  CD1 LEU B 137     -32.619  -0.422  46.446  1.00 38.63           C
ANISOU 3189  CD1 LEU B 137     5267   4665   4747   -267   1068    224       C
ATOM   3190  CD2 LEU B 137     -34.578  -0.230  47.992  1.00 46.25           C
ANISOU 3190  CD2 LEU B 137     6249   5546   5777   -310   1287    232       C
ATOM   3191  N   GLN B 138     -32.260  -3.883  50.943  1.00 66.36           N
ANISOU 3191  N   GLN B 138     9359   7927   7929   -252   1330    237       N
ATOM   3192  CA  GLN B 138     -32.095  -5.268  51.363  1.00 65.49           C
ANISOU 3192  CA  GLN B 138     9371   7765   7748   -259   1356    245       C
ATOM   3193  C   GLN B 138     -33.205  -5.701  52.299  1.00 69.80           C
ANISOU 3193  C   GLN B 138     9979   8237   8306   -299   1500    251       C
ATOM   3194  O   GLN B 138     -33.726  -6.815  52.165  1.00 68.56           O
ANISOU 3194  O   GLN B 138     9846   8043   8160   -341   1546    258       O
ATOM   3195  CB  GLN B 138     -30.772  -5.499  52.094  1.00 62.28           C
ANISOU 3195  CB  GLN B 138     9107   7347   7209   -196   1299    243       C
ATOM   3196  CG  GLN B 138     -29.497  -4.983  51.506  1.00 63.66           C
ANISOU 3196  CG  GLN B 138     9249   7588   7352   -146   1166    236       C
ATOM   3197  CD  GLN B 138     -29.243  -5.392  50.075  1.00 67.53           C
ANISOU 3197  CD  GLN B 138     9639   8129   7893   -159   1080    238       C
ATOM   3198  OE1 GLN B 138     -28.518  -4.689  49.358  1.00 68.69           O
ANISOU 3198  OE1 GLN B 138     9710   8336   8053   -133    986    230       O
ATOM   3199  NE2 GLN B 138     -29.797  -6.529  49.648  1.00 66.38           N
ANISOU 3199  NE2 GLN B 138     9497   7955   7770   -201   1112    247       N
ATOM   3200  N   GLU B 139     -33.602  -4.857  53.255  1.00 84.85           N
ANISOU 3200  N   GLU B 139    11914  10116  10209   -289   1578    247       N
ATOM   3201  CA  GLU B 139     -34.622  -5.402  54.134  1.00 91.36           C
ANISOU 3201  CA  GLU B 139    12808  10865  11041   -327   1720    253       C
ATOM   3202  C   GLU B 139     -35.940  -5.607  53.401  1.00 85.78           C
ANISOU 3202  C   GLU B 139    11963  10162  10466   -397   1782    257       C
ATOM   3203  O   GLU B 139     -36.518  -6.705  53.412  1.00 76.46           O
ANISOU 3203  O   GLU B 139    10813   8939   9297   -444   1842    263       O
ATOM   3204  CB  GLU B 139     -35.017  -4.582  55.325  1.00 95.43           C
ANISOU 3204  CB  GLU B 139    13384  11338  11537   -313   1819    250       C
ATOM   3205  CG  GLU B 139     -35.904  -5.722  55.860  1.00 99.45           C
ANISOU 3205  CG  GLU B 139    13967  11772  12049   -363   1942    259       C
ATOM   3206  CD  GLU B 139     -37.375  -5.411  56.026  1.00108.08           C
ANISOU 3206  CD  GLU B 139    14975  12836  13253   -416   2076    261       C
ATOM   3207  OE1 GLU B 139     -37.809  -4.270  55.723  1.00106.51           O
ANISOU 3207  OE1 GLU B 139    14654  12676  13138   -414   2079    257       O
ATOM   3208  OE2 GLU B 139     -38.119  -6.430  56.224  1.00103.94           O
ANISOU 3208  OE2 GLU B 139    14486  12258  12747   -467   2166    267       O
ATOM   3209  N   ILE B 140     -36.438  -4.559  52.754  1.00 75.72           N
ANISOU 3209  N   ILE B 140    10537   8940   9295   -406   1766    254       N
ATOM   3210  CA  ILE B 140     -37.802  -4.707  52.269  1.00 70.37           C
ANISOU 3210  CA  ILE B 140     9735   8258   8743   -471   1840    259       C
ATOM   3211  C   ILE B 140     -37.821  -5.605  51.055  1.00 60.87           C
ANISOU 3211  C   ILE B 140     8460   7086   7581   -511   1767    261       C
ATOM   3212  O   ILE B 140     -38.798  -6.323  50.839  1.00 60.70           O
ANISOU 3212  O   ILE B 140     8396   7040   7627   -574   1832    265       O
ATOM   3213  CB  ILE B 140     -38.508  -3.358  52.030  1.00 64.88           C
ANISOU 3213  CB  ILE B 140     8899   7599   8152   -470   1864    257       C
ATOM   3214  CG1 ILE B 140     -38.760  -2.659  53.360  1.00 66.95           C
ANISOU 3214  CG1 ILE B 140     9246   7811   8381   -445   1973    255       C
ATOM   3215  CG2 ILE B 140     -39.859  -3.587  51.414  1.00 64.82           C
ANISOU 3215  CG2 ILE B 140     8753   7597   8280   -536   1923    262       C
ATOM   3216  CD1 ILE B 140     -39.309  -1.249  53.244  1.00 68.58           C
ANISOU 3216  CD1 ILE B 140     9336   8048   8672   -431   1997    254       C
ATOM   3217  N   LEU B 141     -36.771  -5.593  50.244  1.00 56.91           N
ANISOU 3217  N   LEU B 141     7945   6636   7040   -477   1634    258       N
ATOM   3218  CA  LEU B 141     -36.709  -6.438  49.064  1.00 53.36           C
ANISOU 3218  CA  LEU B 141     7440   6214   6621   -511   1560    260       C
ATOM   3219  C   LEU B 141     -35.496  -7.357  49.174  1.00 52.30           C
ANISOU 3219  C   LEU B 141     7441   6065   6366   -476   1495    261       C
ATOM   3220  O   LEU B 141     -34.462  -7.114  48.536  1.00 49.37           O
ANISOU 3220  O   LEU B 141     7056   5744   5960   -434   1380    258       O
ATOM   3221  CB  LEU B 141     -36.656  -5.594  47.800  1.00 47.89           C
ANISOU 3221  CB  LEU B 141     6590   5599   6007   -507   1461    257       C
ATOM   3222  CG  LEU B 141     -37.975  -4.945  47.418  1.00 54.35           C
ANISOU 3222  CG  LEU B 141     7256   6434   6960   -552   1514    259       C
ATOM   3223  CD1 LEU B 141     -37.878  -4.468  45.995  1.00 53.31           C
ANISOU 3223  CD1 LEU B 141     6986   6373   6896   -555   1402    258       C
ATOM   3224  CD2 LEU B 141     -39.124  -5.912  47.577  1.00 53.51           C
ANISOU 3224  CD2 LEU B 141     7142   6281   6910   -624   1612    263       C
ATOM   3225  N   PRO B 142     -35.605  -8.464  49.910  1.00 50.26           N
ANISOU 3225  N   PRO B 142     7312   5740   6046   -493   1567    266       N
ATOM   3226  CA  PRO B 142     -34.422  -9.322  50.065  1.00 46.48           C
ANISOU 3226  CA  PRO B 142     6967   5245   5448   -450   1505    269       C
ATOM   3227  C   PRO B 142     -33.927  -9.875  48.748  1.00 42.70           C
ANISOU 3227  C   PRO B 142     6431   4809   4982   -457   1398    270       C
ATOM   3228  O   PRO B 142     -32.735 -10.169  48.626  1.00 43.32           O
ANISOU 3228  O   PRO B 142     6580   4903   4978   -404   1314    270       O
ATOM   3229  CB  PRO B 142     -34.893 -10.432  51.020  1.00 46.46           C
ANISOU 3229  CB  PRO B 142     7103   5156   5395   -479   1617    275       C
ATOM   3230  CG  PRO B 142     -36.119  -9.897  51.698  1.00 50.16           C
ANISOU 3230  CG  PRO B 142     7532   5593   5934   -519   1744    274       C
ATOM   3231  CD  PRO B 142     -36.731  -8.877  50.772  1.00 52.15           C
ANISOU 3231  CD  PRO B 142     7592   5911   6312   -542   1711    269       C
ATOM   3232  N   THR B 143     -34.786  -9.996  47.741  1.00 41.40           N
ANISOU 3232  N   THR B 143     6140   4667   4922   -519   1395    269       N
ATOM   3233  CA  THR B 143     -34.334 -10.457  46.423  1.00 42.32           C
ANISOU 3233  CA  THR B 143     6202   4825   5053   -528   1291    269       C
ATOM   3234  C   THR B 143     -33.683  -9.346  45.591  1.00 37.02           C
ANISOU 3234  C   THR B 143     5426   4231   4408   -487   1182    263       C
ATOM   3235  O   THR B 143     -33.180  -9.616  44.491  1.00 34.63           O
ANISOU 3235  O   THR B 143     5083   3965   4110   -485   1091    263       O
ATOM   3236  CB  THR B 143     -35.498 -11.109  45.654  1.00 39.09           C
ANISOU 3236  CB  THR B 143     5710   4406   4737   -615   1326    269       C
ATOM   3237  OG1 THR B 143     -36.533 -10.145  45.395  1.00 35.42           O
ANISOU 3237  OG1 THR B 143     5097   3971   4389   -649   1356    266       O
ATOM   3238  CG2 THR B 143     -36.089 -12.273  46.496  1.00 35.26           C
ANISOU 3238  CG2 THR B 143     5339   3839   4220   -658   1439    274       C
ATOM   3239  N   SER B 144     -33.677  -8.113  46.083  1.00 36.22           N
ANISOU 3239  N   SER B 144     5286   4152   4322   -455   1193    259       N
ATOM   3240  CA  SER B 144     -33.085  -7.033  45.310  1.00 41.37           C
ANISOU 3240  CA  SER B 144     5843   4874   5001   -419   1096    254       C
ATOM   3241  C   SER B 144     -31.568  -7.215  45.198  1.00 38.28           C
ANISOU 3241  C   SER B 144     5529   4504   4511   -355   1001    252       C
ATOM   3242  O   SER B 144     -30.921  -7.889  46.015  1.00 36.56           O
ANISOU 3242  O   SER B 144     5446   4248   4197   -324   1015    255       O
ATOM   3243  CB  SER B 144     -33.432  -5.665  45.915  1.00 39.58           C
ANISOU 3243  CB  SER B 144     5568   4662   4810   -399   1136    249       C
ATOM   3244  OG  SER B 144     -32.725  -5.423  47.120  1.00 39.83           O
ANISOU 3244  OG  SER B 144     5719   4667   4747   -348   1159    247       O
ATOM   3245  N   VAL B 145     -31.021  -6.604  44.147  1.00 36.88           N
ANISOU 3245  N   VAL B 145     5262   4387   4362   -337    903    247       N
ATOM   3246  CA  VAL B 145     -29.626  -6.717  43.741  1.00 35.20           C
ANISOU 3246  CA  VAL B 145     5089   4206   4079   -283    804    245       C
ATOM   3247  C   VAL B 145     -29.001  -5.336  43.759  1.00 36.50           C
ANISOU 3247  C   VAL B 145     5202   4420   4246   -239    753    235       C
ATOM   3248  O   VAL B 145     -29.506  -4.426  43.097  1.00 37.90           O
ANISOU 3248  O   VAL B 145     5262   4633   4504   -257    739    232       O
ATOM   3249  CB  VAL B 145     -29.524  -7.301  42.327  1.00 30.41           C
ANISOU 3249  CB  VAL B 145     4423   3625   3506   -308    735    247       C
ATOM   3250  CG1 VAL B 145     -28.097  -7.344  41.884  1.00 29.33           C
ANISOU 3250  CG1 VAL B 145     4318   3521   3305   -251    639    244       C
ATOM   3251  CG2 VAL B 145     -30.201  -8.682  42.293  1.00 37.05           C
ANISOU 3251  CG2 VAL B 145     5317   4413   4347   -360    789    254       C
ATOM   3252  N   SER B 146     -27.891  -5.183  44.475  1.00 31.44           N
ANISOU 3252  N   SER B 146     4649   3782   3517   -181    722    231       N
ATOM   3253  CA  SER B 146     -27.162  -3.925  44.510  1.00 30.52           C
ANISOU 3253  CA  SER B 146     4493   3711   3393   -139    668    221       C
ATOM   3254  C   SER B 146     -25.854  -4.080  43.757  1.00 32.88           C
ANISOU 3254  C   SER B 146     4789   4051   3652    -99    562    217       C
ATOM   3255  O   SER B 146     -25.076  -4.997  44.041  1.00 35.13           O
ANISOU 3255  O   SER B 146     5168   4319   3861    -69    539    221       O
ATOM   3256  CB  SER B 146     -26.872  -3.483  45.938  1.00 30.73           C
ANISOU 3256  CB  SER B 146     4614   3710   3352   -105    709    216       C
ATOM   3257  OG  SER B 146     -28.050  -3.080  46.584  1.00 33.41           O
ANISOU 3257  OG  SER B 146     4941   4016   3736   -139    808    218       O
ATOM   3258  N   LEU B 147     -25.634  -3.199  42.795  1.00 28.02           N
ANISOU 3258  N   LEU B 147     4069   3488   3088    -98    502    210       N
ATOM   3259  CA  LEU B 147     -24.423  -3.154  41.999  1.00 31.09           C
ANISOU 3259  CA  LEU B 147     4440   3921   3452    -62    406    205       C
ATOM   3260  C   LEU B 147     -23.659  -1.874  42.340  1.00 30.24           C
ANISOU 3260  C   LEU B 147     4312   3851   3327    -25    368    192       C
ATOM   3261  O   LEU B 147     -24.134  -0.767  42.073  1.00 27.82           O
ANISOU 3261  O   LEU B 147     3924   3567   3080    -40    375    185       O
ATOM   3262  CB  LEU B 147     -24.767  -3.199  40.511  1.00 34.16           C
ANISOU 3262  CB  LEU B 147     4728   4338   3913    -95    367    208       C
ATOM   3263  CG  LEU B 147     -25.874  -4.155  40.080  1.00 32.68           C
ANISOU 3263  CG  LEU B 147     4529   4117   3769   -150    412    218       C
ATOM   3264  CD1 LEU B 147     -26.052  -3.983  38.610  1.00 34.77           C
ANISOU 3264  CD1 LEU B 147     4696   4416   4098   -176    357    218       C
ATOM   3265  CD2 LEU B 147     -25.513  -5.574  40.409  1.00 36.31           C
ANISOU 3265  CD2 LEU B 147     5098   4537   4161   -142    423    226       C
ATOM   3266  N   ARG B 148     -22.470  -2.013  42.895  1.00 32.99           N
ANISOU 3266  N   ARG B 148     4733   4207   3596     25    324    187       N
ATOM   3267  CA  ARG B 148     -21.668  -0.836  43.228  1.00 28.83           C
ANISOU 3267  CA  ARG B 148     4190   3715   3049     57    283    172       C
ATOM   3268  C   ARG B 148     -20.907  -0.423  41.984  1.00 30.41           C
ANISOU 3268  C   ARG B 148     4306   3970   3280     67    202    165       C
ATOM   3269  O   ARG B 148     -19.965  -1.099  41.562  1.00 35.70           O
ANISOU 3269  O   ARG B 148     4996   4654   3914     95    146    167       O
ATOM   3270  CB  ARG B 148     -20.748  -1.131  44.396  1.00 27.24           C
ANISOU 3270  CB  ARG B 148     4099   3499   2751    102    268    168       C
ATOM   3271  CG  ARG B 148     -21.549  -1.470  45.647  1.00 27.87           C
ANISOU 3271  CG  ARG B 148     4272   3520   2798     91    355    175       C
ATOM   3272  CD  ARG B 148     -20.671  -1.895  46.791  1.00 28.26           C
ANISOU 3272  CD  ARG B 148     4444   3549   2745    138    338    174       C
ATOM   3273  NE  ARG B 148     -21.397  -1.872  48.052  1.00 28.86           N
ANISOU 3273  NE  ARG B 148     4607   3570   2788    128    422    177       N
ATOM   3274  CZ  ARG B 148     -20.879  -2.310  49.195  1.00 31.00           C
ANISOU 3274  CZ  ARG B 148     5003   3809   2965    163    424    178       C
ATOM   3275  NH1 ARG B 148     -19.643  -2.779  49.194  1.00 30.90           N
ANISOU 3275  NH1 ARG B 148     5032   3819   2891    211    342    178       N
ATOM   3276  NH2 ARG B 148     -21.584  -2.286  50.329  1.00 29.92           N
ANISOU 3276  NH2 ARG B 148     4953   3618   2799    152    508    180       N
ATOM   3277  N   LEU B 149     -21.353   0.653  41.349  1.00 28.25           N
ANISOU 3277  N   LEU B 149     3937   3723   3075     44    200    158       N
ATOM   3278  CA  LEU B 149     -20.799   1.106  40.085  1.00 27.03           C
ANISOU 3278  CA  LEU B 149     3699   3614   2956     47    133    152       C
ATOM   3279  C   LEU B 149     -19.581   1.998  40.315  1.00 26.59           C
ANISOU 3279  C   LEU B 149     3642   3595   2865     83     77    136       C
ATOM   3280  O   LEU B 149     -19.305   2.437  41.434  1.00 26.93           O
ANISOU 3280  O   LEU B 149     3738   3631   2863    101     91    127       O
ATOM   3281  CB  LEU B 149     -21.873   1.831  39.272  1.00 27.32           C
ANISOU 3281  CB  LEU B 149     3640   3659   3082      7    155    154       C
ATOM   3282  CG  LEU B 149     -23.037   0.872  38.966  1.00 30.64           C
ANISOU 3282  CG  LEU B 149     4054   4046   3541    -34    201    170       C
ATOM   3283  CD1 LEU B 149     -24.242   1.563  38.323  1.00 34.21           C
ANISOU 3283  CD1 LEU B 149     4411   4503   4084    -73    228    173       C
ATOM   3284  CD2 LEU B 149     -22.562  -0.226  38.073  1.00 30.51           C
ANISOU 3284  CD2 LEU B 149     4049   4032   3510    -33    156    177       C
ATOM   3285  N   THR B 150     -18.784   2.180  39.263  1.00 26.85           N
ANISOU 3285  N   THR B 150     3621   3668   2914     94     13    130       N
ATOM   3286  CA  THR B 150     -17.635   3.074  39.334  1.00 25.26           C
ANISOU 3286  CA  THR B 150     3403   3506   2689    122    -40    112       C
ATOM   3287  C   THR B 150     -17.895   4.324  38.509  1.00 28.62           C
ANISOU 3287  C   THR B 150     3739   3958   3178    101    -49    103       C
ATOM   3288  O   THR B 150     -18.883   4.423  37.774  1.00 24.12           O
ANISOU 3288  O   THR B 150     3115   3380   2669     69    -24    112       O
ATOM   3289  CB  THR B 150     -16.350   2.425  38.803  1.00 30.15           C
ANISOU 3289  CB  THR B 150     4029   4151   3275    156   -107    111       C
ATOM   3290  OG1 THR B 150     -16.378   2.437  37.354  1.00 25.06           O
ANISOU 3290  OG1 THR B 150     3313   3526   2683    140   -132    113       O
ATOM   3291  CG2 THR B 150     -16.116   1.001  39.376  1.00 28.14           C
ANISOU 3291  CG2 THR B 150     3864   3867   2961    181   -101    124       C
ATOM   3292  N   TRP B 151     -16.954   5.267  38.596  1.00 24.08           N
ANISOU 3292  N   TRP B 151     3146   3415   2588    118    -89     85       N
ATOM   3293  CA  TRP B 151     -16.959   6.365  37.656  1.00 28.18           C
ANISOU 3293  CA  TRP B 151     3585   3961   3160    103   -106     76       C
ATOM   3294  C   TRP B 151     -16.878   5.767  36.255  1.00 30.75           C
ANISOU 3294  C   TRP B 151     3865   4300   3519     96   -137     85       C
ATOM   3295  O   TRP B 151     -16.072   4.858  36.001  1.00 27.18           O
ANISOU 3295  O   TRP B 151     3437   3855   3035    118   -172     88       O
ATOM   3296  CB  TRP B 151     -15.787   7.310  37.944  1.00 32.66           C
ANISOU 3296  CB  TRP B 151     4149   4562   3699    121   -149     54       C
ATOM   3297  CG  TRP B 151     -15.806   8.628  37.201  1.00 34.28           C
ANISOU 3297  CG  TRP B 151     4284   4789   3951    104   -157     42       C
ATOM   3298  CD1 TRP B 151     -16.889   9.255  36.665  1.00 34.39           C
ANISOU 3298  CD1 TRP B 151     4251   4792   4025     79   -122     48       C
ATOM   3299  CD2 TRP B 151     -14.676   9.470  36.921  1.00 33.30           C
ANISOU 3299  CD2 TRP B 151     4132   4701   3820    112   -203     21       C
ATOM   3300  NE1 TRP B 151     -16.506  10.436  36.077  1.00 33.87           N
ANISOU 3300  NE1 TRP B 151     4137   4750   3983     73   -142     34       N
ATOM   3301  CE2 TRP B 151     -15.152  10.588  36.222  1.00 37.47           C
ANISOU 3301  CE2 TRP B 151     4605   5234   4400     91   -190     16       C
ATOM   3302  CE3 TRP B 151     -13.311   9.391  37.217  1.00 34.91           C
ANISOU 3302  CE3 TRP B 151     4352   4932   3979    136   -254      6       C
ATOM   3303  CZ2 TRP B 151     -14.304  11.632  35.803  1.00 41.95           C
ANISOU 3303  CZ2 TRP B 151     5137   5830   4972     89   -221     -4       C
ATOM   3304  CZ3 TRP B 151     -12.474  10.421  36.808  1.00 36.77           C
ANISOU 3304  CZ3 TRP B 151     4545   5200   4225    132   -287    -15       C
ATOM   3305  CH2 TRP B 151     -12.974  11.527  36.103  1.00 37.24           C
ANISOU 3305  CH2 TRP B 151     4556   5261   4335    107   -268    -20       C
ATOM   3306  N   MET B 152     -17.749   6.227  35.368  1.00 27.04           N
ANISOU 3306  N   MET B 152     3334   3828   3112     68   -123     91       N
ATOM   3307  CA  MET B 152     -17.882   5.612  34.060  1.00 31.31           C
ANISOU 3307  CA  MET B 152     3840   4372   3684     56   -147    101       C
ATOM   3308  C   MET B 152     -17.446   6.570  32.983  1.00 35.76           C
ANISOU 3308  C   MET B 152     4342   4965   4280     53   -183     91       C
ATOM   3309  O   MET B 152     -16.934   7.665  33.258  1.00 37.98           O
ANISOU 3309  O   MET B 152     4608   5265   4557     61   -192     75       O
ATOM   3310  CB  MET B 152     -19.305   5.143  33.794  1.00 32.42           C
ANISOU 3310  CB  MET B 152     3965   4484   3870     22   -107    118       C
ATOM   3311  CG  MET B 152     -19.490   3.749  34.314  1.00 30.90           C
ANISOU 3311  CG  MET B 152     3835   4262   3642     23    -87    130       C
ATOM   3312  SD  MET B 152     -21.124   3.438  34.893  1.00 23.84           S
ANISOU 3312  SD  MET B 152     2944   3330   2786    -14    -14    144       S
ATOM   3313  CE  MET B 152     -22.028   3.511  33.381  1.00 30.89           C
ANISOU 3313  CE  MET B 152     3754   4228   3755    -51    -31    153       C
ATOM   3314  N   TYR B 153     -17.563   6.098  31.749  1.00 34.09           N
ANISOU 3314  N   TYR B 153     4103   4755   4095     42   -206    100       N
ATOM   3315  CA  TYR B 153     -17.273   6.938  30.596  1.00 40.24           C
ANISOU 3315  CA  TYR B 153     4829   5555   4906     37   -237     93       C
ATOM   3316  C   TYR B 153     -17.803   6.257  29.348  1.00 37.85           C
ANISOU 3316  C   TYR B 153     4507   5241   4633     17   -252    107       C
ATOM   3317  O   TYR B 153     -17.813   5.020  29.254  1.00 34.80           O
ANISOU 3317  O   TYR B 153     4157   4839   4227     17   -254    117       O
ATOM   3318  CB  TYR B 153     -15.765   7.236  30.441  1.00 38.31           C
ANISOU 3318  CB  TYR B 153     4587   5340   4629     64   -276     76       C
ATOM   3319  CG  TYR B 153     -14.920   6.003  30.156  1.00 35.66           C
ANISOU 3319  CG  TYR B 153     4285   5006   4258     85   -302     81       C
ATOM   3320  CD1 TYR B 153     -14.840   5.477  28.888  1.00 36.12           C
ANISOU 3320  CD1 TYR B 153     4332   5061   4332     79   -322     88       C
ATOM   3321  CD2 TYR B 153     -14.201   5.370  31.169  1.00 34.49           C
ANISOU 3321  CD2 TYR B 153     4186   4860   4059    114   -305     78       C
ATOM   3322  CE1 TYR B 153     -14.080   4.366  28.633  1.00 37.01           C
ANISOU 3322  CE1 TYR B 153     4478   5171   4411    101   -340     93       C
ATOM   3323  CE2 TYR B 153     -13.435   4.249  30.919  1.00 31.88           C
ANISOU 3323  CE2 TYR B 153     3887   4529   3696    139   -327     84       C
ATOM   3324  CZ  TYR B 153     -13.377   3.761  29.641  1.00 33.14           C
ANISOU 3324  CZ  TYR B 153     4033   4685   3875    132   -342     92       C
ATOM   3325  OH  TYR B 153     -12.632   2.661  29.345  1.00 32.02           O
ANISOU 3325  OH  TYR B 153     3925   4540   3703    159   -359     98       O
ATOM   3326  N   ASP B 154     -18.229   7.084  28.399  1.00 37.26           N
ANISOU 3326  N   ASP B 154     4382   5172   4602      1   -263    107       N
ATOM   3327  CA  ASP B 154     -18.420   6.683  27.018  1.00 39.93           C
ANISOU 3327  CA  ASP B 154     4704   5506   4963    -14   -292    116       C
ATOM   3328  C   ASP B 154     -17.223   7.176  26.218  1.00 42.32           C
ANISOU 3328  C   ASP B 154     4999   5829   5251      4   -327    103       C
ATOM   3329  O   ASP B 154     -16.412   7.968  26.703  1.00 45.48           O
ANISOU 3329  O   ASP B 154     5395   6250   5636     21   -327     87       O
ATOM   3330  CB  ASP B 154     -19.724   7.253  26.457  1.00 38.57           C
ANISOU 3330  CB  ASP B 154     4482   5323   4848    -42   -286    126       C
ATOM   3331  CG  ASP B 154     -20.255   6.447  25.295  1.00 40.42           C
ANISOU 3331  CG  ASP B 154     4712   5544   5101    -65   -312    139       C
ATOM   3332  OD1 ASP B 154     -19.535   5.533  24.835  1.00 43.47           O
ANISOU 3332  OD1 ASP B 154     5137   5926   5453    -59   -332    139       O
ATOM   3333  OD2 ASP B 154     -21.388   6.711  24.836  1.00 39.26           O
ANISOU 3333  OD2 ASP B 154     4526   5389   5002    -90   -312    149       O
ATOM   3334  N   HIS B 155     -17.123   6.709  24.977  1.00 41.53           N
ANISOU 3334  N   HIS B 155     4898   5723   5157     -4   -354    109       N
ATOM   3335  CA  HIS B 155     -16.036   7.140  24.104  1.00 47.64           C
ANISOU 3335  CA  HIS B 155     5668   6513   5921     10   -380     98       C
ATOM   3336  C   HIS B 155     -16.129   8.652  23.884  1.00 47.32           C
ANISOU 3336  C   HIS B 155     5586   6484   5908      5   -379     88       C
ATOM   3337  O   HIS B 155     -17.238   9.194  23.799  1.00 46.08           O
ANISOU 3337  O   HIS B 155     5402   6319   5789    -13   -370     96       O
ATOM   3338  CB  HIS B 155     -16.094   6.378  22.770  1.00 47.33           C
ANISOU 3338  CB  HIS B 155     5643   6457   5883     -1   -404    108       C
ATOM   3339  CG  HIS B 155     -14.886   6.550  21.902  1.00 49.98           C
ANISOU 3339  CG  HIS B 155     5985   6803   6202     16   -423     98       C
ATOM   3340  ND1 HIS B 155     -14.526   7.762  21.352  1.00 51.04           N
ANISOU 3340  ND1 HIS B 155     6091   6950   6352     16   -429     87       N
ATOM   3341  CD2 HIS B 155     -13.973   5.652  21.455  1.00 55.28           C
ANISOU 3341  CD2 HIS B 155     6690   7470   6842     34   -432     98       C
ATOM   3342  CE1 HIS B 155     -13.429   7.612  20.628  1.00 51.29           C
ANISOU 3342  CE1 HIS B 155     6136   6987   6366     31   -440     79       C
ATOM   3343  NE2 HIS B 155     -13.070   6.341  20.674  1.00 54.63           N
ANISOU 3343  NE2 HIS B 155     6596   7401   6762     43   -442     86       N
ATOM   3344  N   PRO B 156     -14.994   9.370  23.860  1.00 48.15           N
ANISOU 3344  N   PRO B 156     5686   6611   5999     22   -385     70       N
ATOM   3345  CA  PRO B 156     -15.043  10.830  23.661  1.00 50.02           C
ANISOU 3345  CA  PRO B 156     5891   6856   6260     16   -381     60       C
ATOM   3346  C   PRO B 156     -15.750  11.266  22.372  1.00 54.26           C
ANISOU 3346  C   PRO B 156     6410   7377   6830     -1   -394     69       C
ATOM   3347  O   PRO B 156     -16.286  12.383  22.309  1.00 53.09           O
ANISOU 3347  O   PRO B 156     6237   7227   6708     -7   -386     68       O
ATOM   3348  CB  PRO B 156     -13.561  11.233  23.671  1.00 49.70           C
ANISOU 3348  CB  PRO B 156     5852   6838   6194     32   -389     39       C
ATOM   3349  CG  PRO B 156     -12.871  10.158  24.436  1.00 45.91           C
ANISOU 3349  CG  PRO B 156     5399   6367   5678     52   -393     38       C
ATOM   3350  CD  PRO B 156     -13.622   8.892  24.119  1.00 46.35           C
ANISOU 3350  CD  PRO B 156     5478   6399   5733     47   -395     59       C
ATOM   3351  N   SER B 157     -15.723  10.448  21.321  1.00 52.96           N
ANISOU 3351  N   SER B 157     6261   7200   6660     -6   -417     79       N
ATOM   3352  CA  SER B 157     -16.406  10.753  20.069  1.00 51.94           C
ANISOU 3352  CA  SER B 157     6123   7054   6556    -22   -437     89       C
ATOM   3353  C   SER B 157     -17.823  10.184  20.012  1.00 51.62           C
ANISOU 3353  C   SER B 157     6073   6997   6544    -42   -443    109       C
ATOM   3354  O   SER B 157     -18.376  10.041  18.916  1.00 58.47           O
ANISOU 3354  O   SER B 157     6941   7849   7426    -57   -469    120       O
ATOM   3355  CB  SER B 157     -15.598  10.224  18.879  1.00 52.99           C
ANISOU 3355  CB  SER B 157     6286   7179   6668    -19   -458     88       C
ATOM   3356  OG  SER B 157     -14.273  10.734  18.875  1.00 55.98           O
ANISOU 3356  OG  SER B 157     6667   7574   7027     -2   -450     70       O
ATOM   3357  N   SER B 158     -18.418   9.848  21.151  1.00 55.08           N
ANISOU 3357  N   SER B 158     6502   7435   6989    -45   -419    113       N
ATOM   3358  CA  SER B 158     -19.718   9.182  21.150  1.00 57.38           C
ANISOU 3358  CA  SER B 158     6782   7711   7309    -68   -420    131       C
ATOM   3359  C   SER B 158     -20.832  10.099  20.660  1.00 54.18           C
ANISOU 3359  C   SER B 158     6331   7301   6953    -79   -429    140       C
ATOM   3360  O   SER B 158     -20.834  11.301  20.941  1.00 57.94           O
ANISOU 3360  O   SER B 158     6784   7786   7444    -67   -414    133       O
ATOM   3361  CB  SER B 158     -20.063   8.693  22.545  1.00 49.48           C
ANISOU 3361  CB  SER B 158     5786   6711   6304    -68   -383    132       C
ATOM   3362  OG  SER B 158     -21.418   8.322  22.572  1.00 54.30           O
ANISOU 3362  OG  SER B 158     6372   7306   6953    -93   -377    148       O
ATOM   3363  N   LYS B 159     -21.760   9.530  19.879  1.00 50.12           N
ANISOU 3363  N   LYS B 159     5807   6773   6464   -103   -455    155       N
ATOM   3364  CA  LYS B 159     -22.939  10.290  19.470  1.00 48.98           C
ANISOU 3364  CA  LYS B 159     5614   6625   6372   -113   -468    166       C
ATOM   3365  C   LYS B 159     -23.830  10.618  20.658  1.00 51.29           C
ANISOU 3365  C   LYS B 159     5865   6921   6700   -113   -425    171       C
ATOM   3366  O   LYS B 159     -24.543  11.630  20.628  1.00 59.00           O
ANISOU 3366  O   LYS B 159     6799   7901   7719   -106   -421    176       O
ATOM   3367  CB  LYS B 159     -23.758   9.519  18.430  1.00 44.36           C
ANISOU 3367  CB  LYS B 159     5025   6025   5806   -142   -511    181       C
ATOM   3368  N   ILE B 160     -23.848   9.765  21.677  1.00 51.87           N
ANISOU 3368  N   ILE B 160     5956   6993   6760   -119   -393    170       N
ATOM   3369  CA  ILE B 160     -24.710   9.991  22.838  1.00 51.07           C
ANISOU 3369  CA  ILE B 160     5824   6890   6691   -121   -345    174       C
ATOM   3370  C   ILE B 160     -24.084  11.054  23.738  1.00 50.50           C
ANISOU 3370  C   ILE B 160     5758   6828   6601    -93   -309    161       C
ATOM   3371  O   ILE B 160     -22.918  10.902  24.142  1.00 48.63           O
ANISOU 3371  O   ILE B 160     5564   6598   6314    -78   -305    147       O
ATOM   3372  CB  ILE B 160     -24.944   8.699  23.600  1.00 50.32           C
ANISOU 3372  CB  ILE B 160     5755   6784   6583   -139   -319    178       C
ATOM   3373  CG1 ILE B 160     -25.760   7.706  22.749  1.00 52.22           C
ANISOU 3373  CG1 ILE B 160     5983   7010   6847   -175   -351    191       C
ATOM   3374  CG2 ILE B 160     -25.684   9.033  24.867  1.00 46.83           C
ANISOU 3374  CG2 ILE B 160     5289   6337   6167   -138   -261    180       C
ATOM   3375  CD1 ILE B 160     -24.928   6.785  21.850  1.00 47.93           C
ANISOU 3375  CD1 ILE B 160     5493   6461   6258   -182   -392    189       C
ATOM   3376  N   PRO B 161     -24.822  12.114  24.098  1.00 48.94           N
ANISOU 3376  N   PRO B 161     5520   6631   6445    -84   -283    164       N
ATOM   3377  CA  PRO B 161     -24.224  13.185  24.908  1.00 49.53           C
ANISOU 3377  CA  PRO B 161     5608   6711   6500    -60   -250    150       C
ATOM   3378  C   PRO B 161     -23.888  12.713  26.310  1.00 45.73           C
ANISOU 3378  C   PRO B 161     5163   6227   5984    -56   -206    142       C
ATOM   3379  O   PRO B 161     -24.564  11.873  26.904  1.00 47.86           O
ANISOU 3379  O   PRO B 161     5433   6485   6265    -70   -180    151       O
ATOM   3380  CB  PRO B 161     -25.298  14.279  24.944  1.00 50.37           C
ANISOU 3380  CB  PRO B 161     5663   6813   6663    -52   -228    160       C
ATOM   3381  CG  PRO B 161     -26.575  13.603  24.622  1.00 52.11           C
ANISOU 3381  CG  PRO B 161     5838   7025   6935    -73   -235    179       C
ATOM   3382  CD  PRO B 161     -26.252  12.342  23.835  1.00 54.65           C
ANISOU 3382  CD  PRO B 161     6183   7347   7234    -96   -281    181       C
ATOM   3383  N   GLN B 162     -22.870  13.344  26.863  1.00 39.97           N
ANISOU 3383  N   GLN B 162     4465   5507   5215    -38   -197    124       N
ATOM   3384  CA  GLN B 162     -22.353  13.024  28.173  1.00 40.82           C
ANISOU 3384  CA  GLN B 162     4616   5613   5280    -31   -164    114       C
ATOM   3385  C   GLN B 162     -21.694  14.269  28.736  1.00 40.59           C
ANISOU 3385  C   GLN B 162     4600   5591   5230    -14   -149     96       C
ATOM   3386  O   GLN B 162     -21.306  15.191  28.008  1.00 38.61           O
ANISOU 3386  O   GLN B 162     4335   5349   4987     -9   -169     89       O
ATOM   3387  CB  GLN B 162     -21.383  11.818  28.117  1.00 39.77           C
ANISOU 3387  CB  GLN B 162     4527   5488   5098    -31   -192    109       C
ATOM   3388  CG  GLN B 162     -20.333  11.904  26.985  1.00 39.01           C
ANISOU 3388  CG  GLN B 162     4431   5406   4983    -25   -242    101       C
ATOM   3389  CD  GLN B 162     -19.264  10.768  26.989  1.00 45.38           C
ANISOU 3389  CD  GLN B 162     5281   6221   5741    -18   -266     96       C
ATOM   3390  OE1 GLN B 162     -19.063  10.074  27.993  1.00 44.21           O
ANISOU 3390  OE1 GLN B 162     5168   6068   5560    -11   -248     95       O
ATOM   3391  NE2 GLN B 162     -18.719  10.475  25.807  1.00 43.54           N
ANISOU 3391  NE2 GLN B 162     5047   5993   5504    -18   -304     96       N
ATOM   3392  N   HIS B 163     -21.627  14.306  30.048  1.00 38.93           N
ANISOU 3392  N   HIS B 163     4424   5374   4994     -8   -109     89       N
ATOM   3393  CA  HIS B 163     -20.936  15.390  30.693  1.00 43.39           C
ANISOU 3393  CA  HIS B 163     5011   5944   5531      3    -95     70       C
ATOM   3394  C   HIS B 163     -19.460  15.045  30.793  1.00 44.11           C
ANISOU 3394  C   HIS B 163     5139   6056   5567      9   -132     52       C
ATOM   3395  O   HIS B 163     -19.017  13.962  30.402  1.00 44.37           O
ANISOU 3395  O   HIS B 163     5180   6096   5582      9   -163     56       O
ATOM   3396  CB  HIS B 163     -21.601  15.691  32.028  1.00 52.81           C
ANISOU 3396  CB  HIS B 163     6226   7116   6722      6    -35     70       C
ATOM   3397  CG  HIS B 163     -22.932  16.359  31.874  1.00 56.47           C
ANISOU 3397  CG  HIS B 163     6646   7563   7248      6      4     85       C
ATOM   3398  ND1 HIS B 163     -23.947  16.236  32.797  1.00 63.88           N
ANISOU 3398  ND1 HIS B 163     7587   8479   8206      5     64     96       N
ATOM   3399  CD2 HIS B 163     -23.422  17.138  30.878  1.00 52.70           C
ANISOU 3399  CD2 HIS B 163     6118   7087   6817      8     -9     93       C
ATOM   3400  CE1 HIS B 163     -24.999  16.923  32.387  1.00 57.60           C
ANISOU 3400  CE1 HIS B 163     6740   7674   7472      8     86    109       C
ATOM   3401  NE2 HIS B 163     -24.703  17.483  31.227  1.00 54.90           N
ANISOU 3401  NE2 HIS B 163     6367   7347   7146     11     40    108       N
ATOM   3402  N   LYS B 164     -18.680  15.974  31.333  1.00 43.10           N
ANISOU 3402  N   LYS B 164     5030   5935   5409     15   -129     31       N
ATOM   3403  CA  LYS B 164     -17.230  15.819  31.331  1.00 41.74           C
ANISOU 3403  CA  LYS B 164     4879   5787   5192     21   -168     12       C
ATOM   3404  C   LYS B 164     -16.807  14.660  32.237  1.00 38.32           C
ANISOU 3404  C   LYS B 164     4489   5356   4714     29   -174     12       C
ATOM   3405  O   LYS B 164     -16.971  14.710  33.461  1.00 34.96           O
ANISOU 3405  O   LYS B 164     4103   4919   4263     33   -145      8       O
ATOM   3406  CB  LYS B 164     -16.563  17.126  31.747  1.00 42.71           C
ANISOU 3406  CB  LYS B 164     5013   5917   5298     19   -163    -12       C
ATOM   3407  CG  LYS B 164     -16.542  18.171  30.644  1.00 43.64           C
ANISOU 3407  CG  LYS B 164     5096   6037   5448     13   -171    -16       C
ATOM   3408  CD  LYS B 164     -15.688  19.376  31.012  1.00 48.12           C
ANISOU 3408  CD  LYS B 164     5679   6612   5993      7   -169    -42       C
ATOM   3409  CE  LYS B 164     -16.043  20.541  30.112  1.00 57.77           C
ANISOU 3409  CE  LYS B 164     6876   7823   7250      2   -158    -42       C
ATOM   3410  NZ  LYS B 164     -15.630  20.281  28.698  1.00 53.63           N
ANISOU 3410  NZ  LYS B 164     6324   7311   6742     -1   -195    -38       N
ATOM   3411  N   ASN B 165     -16.337  13.583  31.637  1.00 37.07           N
ANISOU 3411  N   ASN B 165     4330   5208   4547     34   -207     19       N
ATOM   3412  CA  ASN B 165     -15.661  12.540  32.392  1.00 40.62           C
ANISOU 3412  CA  ASN B 165     4823   5663   4947     49   -221     17       C
ATOM   3413  C   ASN B 165     -14.211  12.435  31.915  1.00 39.09           C
ANISOU 3413  C   ASN B 165     4624   5499   4729     61   -270      2       C
ATOM   3414  O   ASN B 165     -13.787  13.146  31.006  1.00 40.64           O
ANISOU 3414  O   ASN B 165     4785   5710   4947     55   -287     -7       O
ATOM   3415  CB  ASN B 165     -16.417  11.226  32.248  1.00 42.62           C
ANISOU 3415  CB  ASN B 165     5088   5898   5209     47   -211     40       C
ATOM   3416  CG  ASN B 165     -16.818  10.979  30.841  1.00 42.67           C
ANISOU 3416  CG  ASN B 165     5054   5903   5256     35   -228     52       C
ATOM   3417  OD1 ASN B 165     -16.089  11.361  29.918  1.00 43.73           O
ANISOU 3417  OD1 ASN B 165     5165   6056   5396     37   -260     43       O
ATOM   3418  ND2 ASN B 165     -17.989  10.366  30.642  1.00 41.44           N
ANISOU 3418  ND2 ASN B 165     4890   5726   5131     20   -207     71       N
ATOM   3419  N   LEU B 166     -13.465  11.503  32.509  1.00 41.28           N
ANISOU 3419  N   LEU B 166     4936   5785   4963     81   -290      1       N
ATOM   3420  CA  LEU B 166     -12.005  11.443  32.365  1.00 43.74           C
ANISOU 3420  CA  LEU B 166     5242   6127   5249     97   -333    -16       C
ATOM   3421  C   LEU B 166     -11.463  11.424  30.936  1.00 42.36           C
ANISOU 3421  C   LEU B 166     5026   5968   5101     96   -358    -16       C
ATOM   3422  O   LEU B 166     -10.527  12.189  30.654  1.00 41.22           O
ANISOU 3422  O   LEU B 166     4857   5847   4959     94   -377    -36       O
ATOM   3423  CB  LEU B 166     -11.434  10.256  33.159  1.00 39.33           C
ANISOU 3423  CB  LEU B 166     4729   5572   4642    125   -351    -11       C
ATOM   3424  CG  LEU B 166      -9.915  10.251  32.985  1.00 33.72           C
ANISOU 3424  CG  LEU B 166     4003   4898   3913    145   -398    -28       C
ATOM   3425  CD1 LEU B 166      -9.297  10.267  34.315  1.00 32.75           C
ANISOU 3425  CD1 LEU B 166     3917   4785   3741    161   -415    -40       C
ATOM   3426  CD2 LEU B 166      -9.475   9.017  32.194  1.00 34.43           C
ANISOU 3426  CD2 LEU B 166     4092   4991   4001    166   -418    -14       C
ATOM   3427  N   PRO B 167     -11.916  10.570  30.026  1.00 34.76           N
ANISOU 3427  N   PRO B 167     4059   4991   4156     95   -358      2       N
ATOM   3428  CA  PRO B 167     -11.340  10.644  28.675  1.00 40.18           C
ANISOU 3428  CA  PRO B 167     4714   5688   4863     94   -379     -0       C
ATOM   3429  C   PRO B 167     -11.466  12.034  28.094  1.00 43.90           C
ANISOU 3429  C   PRO B 167     5151   6164   5367     73   -372    -12       C
ATOM   3430  O   PRO B 167     -10.526  12.545  27.470  1.00 47.25           O
ANISOU 3430  O   PRO B 167     5552   6605   5794     73   -388    -27       O
ATOM   3431  CB  PRO B 167     -12.156   9.613  27.886  1.00 41.90           C
ANISOU 3431  CB  PRO B 167     4942   5883   5096     89   -375     23       C
ATOM   3432  CG  PRO B 167     -12.597   8.615  28.938  1.00 39.86           C
ANISOU 3432  CG  PRO B 167     4726   5609   4810     99   -361     35       C
ATOM   3433  CD  PRO B 167     -12.875   9.454  30.153  1.00 39.49           C
ANISOU 3433  CD  PRO B 167     4686   5564   4754     94   -341     25       C
ATOM   3434  N   ILE B 168     -12.603  12.684  28.336  1.00 44.93           N
ANISOU 3434  N   ILE B 168     5277   6275   5519     56   -344     -6       N
ATOM   3435  CA  ILE B 168     -12.811  14.034  27.834  1.00 42.81           C
ANISOU 3435  CA  ILE B 168     4982   6006   5280     40   -334    -15       C
ATOM   3436  C   ILE B 168     -11.867  15.010  28.516  1.00 41.31           C
ANISOU 3436  C   ILE B 168     4791   5834   5069     39   -336    -41       C
ATOM   3437  O   ILE B 168     -11.400  15.967  27.890  1.00 42.29           O
ANISOU 3437  O   ILE B 168     4895   5966   5207     28   -339    -55       O
ATOM   3438  CB  ILE B 168     -14.287  14.442  28.001  1.00 38.83           C
ANISOU 3438  CB  ILE B 168     4471   5476   4805     28   -302      0       C
ATOM   3439  CG1 ILE B 168     -15.153  13.678  26.996  1.00 40.38           C
ANISOU 3439  CG1 ILE B 168     4656   5657   5031     22   -309     23       C
ATOM   3440  CG2 ILE B 168     -14.431  15.913  27.785  1.00 42.30           C
ANISOU 3440  CG2 ILE B 168     4893   5913   5266     18   -288    -11       C
ATOM   3441  CD1 ILE B 168     -16.583  13.403  27.440  1.00 40.51           C
ANISOU 3441  CD1 ILE B 168     4669   5650   5071     14   -281     42       C
ATOM   3442  N   MET B 169     -11.612  14.820  29.818  1.00 39.82           N
ANISOU 3442  N   MET B 169     4631   5653   4847     47   -334    -49       N
ATOM   3443  CA  MET B 169     -10.737  15.753  30.535  1.00 46.89           C
ANISOU 3443  CA  MET B 169     5530   6567   5721     42   -341    -75       C
ATOM   3444  C   MET B 169      -9.283  15.611  30.092  1.00 40.61           C
ANISOU 3444  C   MET B 169     4714   5803   4915     48   -378    -92       C
ATOM   3445  O   MET B 169      -8.556  16.609  30.016  1.00 39.20           O
ANISOU 3445  O   MET B 169     4518   5638   4738     33   -383   -115       O
ATOM   3446  CB  MET B 169     -10.845  15.596  32.067  1.00 44.05           C
ANISOU 3446  CB  MET B 169     5212   6203   5322     49   -333    -79       C
ATOM   3447  CG  MET B 169     -12.245  15.790  32.693  1.00 43.05           C
ANISOU 3447  CG  MET B 169     5109   6043   5205     44   -287    -65       C
ATOM   3448  SD  MET B 169     -12.246  15.172  34.418  1.00 52.68           S
ANISOU 3448  SD  MET B 169     6393   7255   6370     58   -279    -66       S
ATOM   3449  CE  MET B 169     -13.907  15.524  34.982  1.00 45.29           C
ANISOU 3449  CE  MET B 169     5476   6277   5454     48   -213    -50       C
ATOM   3450  N   LEU B 170      -8.831  14.388  29.807  1.00 41.51           N
ANISOU 3450  N   LEU B 170     4829   5926   5018     70   -400    -81       N
ATOM   3451  CA  LEU B 170      -7.455  14.234  29.329  1.00 42.43           C
ANISOU 3451  CA  LEU B 170     4919   6072   5130     79   -431    -96       C
ATOM   3452  C   LEU B 170      -7.291  14.868  27.958  1.00 44.42           C
ANISOU 3452  C   LEU B 170     5138   6321   5418     62   -423   -100       C
ATOM   3453  O   LEU B 170      -6.243  15.454  27.655  1.00 43.28           O
ANISOU 3453  O   LEU B 170     4967   6199   5279     55   -433   -121       O
ATOM   3454  CB  LEU B 170      -7.039  12.767  29.294  1.00 38.73           C
ANISOU 3454  CB  LEU B 170     4463   5610   4644    110   -452    -81       C
ATOM   3455  CG  LEU B 170      -6.845  12.067  30.638  1.00 35.71           C
ANISOU 3455  CG  LEU B 170     4117   5234   4219    134   -468    -80       C
ATOM   3456  CD1 LEU B 170      -6.801  10.595  30.398  1.00 39.37           C
ANISOU 3456  CD1 LEU B 170     4600   5689   4668    163   -477    -59       C
ATOM   3457  CD2 LEU B 170      -5.620  12.524  31.379  1.00 35.10           C
ANISOU 3457  CD2 LEU B 170     4026   5191   4120    140   -500   -105       C
ATOM   3458  N   LEU B 171      -8.310  14.743  27.110  1.00 42.09           N
ANISOU 3458  N   LEU B 171     4846   5999   5146     56   -405    -80       N
ATOM   3459  CA  LEU B 171      -8.245  15.390  25.809  1.00 44.71           C
ANISOU 3459  CA  LEU B 171     5157   6323   5507     41   -397    -83       C
ATOM   3460  C   LEU B 171      -8.184  16.898  25.968  1.00 48.44           C
ANISOU 3460  C   LEU B 171     5619   6796   5989     17   -381   -103       C
ATOM   3461  O   LEU B 171      -7.419  17.574  25.270  1.00 51.18           O
ANISOU 3461  O   LEU B 171     5948   7151   6347      5   -380   -119       O
ATOM   3462  CB  LEU B 171      -9.441  14.966  24.965  1.00 41.25           C
ANISOU 3462  CB  LEU B 171     4728   5855   5089     38   -388    -57       C
ATOM   3463  CG  LEU B 171      -9.297  13.503  24.498  1.00 44.94           C
ANISOU 3463  CG  LEU B 171     5209   6320   5547     57   -403    -40       C
ATOM   3464  CD1 LEU B 171     -10.277  13.093  23.429  1.00 42.58           C
ANISOU 3464  CD1 LEU B 171     4918   5993   5268     49   -401    -18       C
ATOM   3465  CD2 LEU B 171      -7.895  13.249  24.005  1.00 42.43           C
ANISOU 3465  CD2 LEU B 171     4879   6023   5221     69   -418    -54       C
ATOM   3466  N   GLU B 172      -8.967  17.429  26.909  1.00 44.70           N
ANISOU 3466  N   GLU B 172     5161   6311   5510     11   -364   -103       N
ATOM   3467  CA  GLU B 172      -8.996  18.858  27.172  1.00 44.85           C
ANISOU 3467  CA  GLU B 172     5181   6326   5536    -10   -345   -121       C
ATOM   3468  C   GLU B 172      -7.634  19.369  27.613  1.00 45.49           C
ANISOU 3468  C   GLU B 172     5251   6436   5599    -21   -360   -152       C
ATOM   3469  O   GLU B 172      -7.193  20.439  27.180  1.00 47.95           O
ANISOU 3469  O   GLU B 172     5551   6746   5921    -43   -350   -170       O
ATOM   3470  CB  GLU B 172     -10.015  19.140  28.273  1.00 46.56           C
ANISOU 3470  CB  GLU B 172     5422   6525   5744    -10   -322   -114       C
ATOM   3471  CG  GLU B 172     -11.452  19.358  27.843  1.00 48.86           C
ANISOU 3471  CG  GLU B 172     5714   6786   6066    -10   -295    -91       C
ATOM   3472  CD  GLU B 172     -12.289  19.927  28.991  1.00 50.13           C
ANISOU 3472  CD  GLU B 172     5898   6929   6221    -12   -263    -91       C
ATOM   3473  OE1 GLU B 172     -11.937  19.710  30.180  1.00 52.39           O
ANISOU 3473  OE1 GLU B 172     6208   7224   6474     -9   -264   -101       O
ATOM   3474  OE2 GLU B 172     -13.273  20.632  28.705  1.00 50.43           O
ANISOU 3474  OE2 GLU B 172     5931   6944   6287    -14   -235    -80       O
ATOM   3475  N   ALA B 173      -6.964  18.621  28.494  1.00 51.31           N
ANISOU 3475  N   ALA B 173     5991   7196   6307     -7   -386   -158       N
ATOM   3476  CA  ALA B 173      -5.629  19.005  28.946  1.00 52.10           C
ANISOU 3476  CA  ALA B 173     6075   7328   6393    -17   -410   -187       C
ATOM   3477  C   ALA B 173      -4.673  19.123  27.776  1.00 55.77           C
ANISOU 3477  C   ALA B 173     6501   7807   6881    -24   -416   -197       C
ATOM   3478  O   ALA B 173      -3.800  20.000  27.756  1.00 58.72           O
ANISOU 3478  O   ALA B 173     6854   8197   7259    -47   -417   -224       O
ATOM   3479  CB  ALA B 173      -5.102  17.998  29.966  1.00 50.40           C
ANISOU 3479  CB  ALA B 173     5869   7135   6144      8   -444   -186       C
ATOM   3480  N   LYS B 174      -4.820  18.240  26.790  1.00 49.86           N
ANISOU 3480  N   LYS B 174     5745   7051   6147     -5   -416   -177       N
ATOM   3481  CA  LYS B 174      -3.980  18.324  25.602  1.00 54.90           C
ANISOU 3481  CA  LYS B 174     6354   7697   6807    -10   -413   -184       C
ATOM   3482  C   LYS B 174      -4.372  19.519  24.717  1.00 58.85           C
ANISOU 3482  C   LYS B 174     6859   8173   7330    -39   -381   -190       C
ATOM   3483  O   LYS B 174      -3.499  20.157  24.126  1.00 58.66           O
ANISOU 3483  O   LYS B 174     6814   8157   7320    -57   -373   -210       O
ATOM   3484  CB  LYS B 174      -4.055  16.995  24.821  1.00 48.20           C
ANISOU 3484  CB  LYS B 174     5510   6843   5962     18   -420   -160       C
ATOM   3485  CG  LYS B 174      -3.648  17.041  23.327  1.00 48.65           C
ANISOU 3485  CG  LYS B 174     5553   6888   6041     13   -405   -159       C
ATOM   3486  CD  LYS B 174      -3.413  15.636  22.769  1.00 45.24           C
ANISOU 3486  CD  LYS B 174     5127   6457   5606     44   -415   -140       C
ATOM   3487  CE  LYS B 174      -2.618  15.634  21.461  1.00 51.14           C
ANISOU 3487  CE  LYS B 174     5860   7200   6372     43   -399   -145       C
ATOM   3488  NZ  LYS B 174      -1.610  14.508  21.339  1.00 51.98           N
ANISOU 3488  NZ  LYS B 174     5951   7327   6474     75   -411   -143       N
ATOM   3489  N   GLU B 175      -5.663  19.875  24.650  1.00 65.75           N
ANISOU 3489  N   GLU B 175     7758   9015   8208    -42   -363   -173       N
ATOM   3490  CA  GLU B 175      -6.067  20.845  23.640  1.00 66.43           C
ANISOU 3490  CA  GLU B 175     7851   9074   8315    -59   -337   -173       C
ATOM   3491  C   GLU B 175      -5.711  22.265  24.161  1.00 68.29           C
ANISOU 3491  C   GLU B 175     8089   9311   8548    -89   -319   -201       C
ATOM   3492  O   GLU B 175      -5.322  23.161  23.389  1.00 74.19           O
ANISOU 3492  O   GLU B 175     8834  10047   9308   -110   -300   -214       O
ATOM   3493  CB  GLU B 175      -7.535  20.506  23.253  1.00 61.90           C
ANISOU 3493  CB  GLU B 175     7298   8470   7752    -46   -330   -141       C
ATOM   3494  CG  GLU B 175      -8.952  20.933  23.816  1.00 76.08           C
ANISOU 3494  CG  GLU B 175     9111  10241   9553    -45   -315   -126       C
ATOM   3495  CD  GLU B 175      -9.887  20.822  22.498  1.00 87.70           C
ANISOU 3495  CD  GLU B 175    10589  11685  11049    -39   -313   -101       C
ATOM   3496  OE1 GLU B 175      -9.500  19.900  21.688  1.00 86.31           O
ANISOU 3496  OE1 GLU B 175    10410  11512  10872    -31   -330    -93       O
ATOM   3497  OE2 GLU B 175     -10.844  21.598  22.135  1.00 94.46           O
ANISOU 3497  OE2 GLU B 175    11453  12515  11923    -41   -297    -90       O
ATOM   3498  N   LYS B 176      -5.848  22.492  25.482  1.00 61.03           N
ANISOU 3498  N   LYS B 176     7179   8400   7609    -92   -324   -210       N
ATOM   3499  CA  LYS B 176      -5.571  23.777  26.163  1.00 60.48           C
ANISOU 3499  CA  LYS B 176     7119   8329   7530   -121   -309   -237       C
ATOM   3500  C   LYS B 176      -4.210  23.797  26.880  1.00 58.92           C
ANISOU 3500  C   LYS B 176     6901   8170   7317   -137   -335   -267       C
ATOM   3501  O   LYS B 176      -3.865  24.789  27.520  1.00 54.80           O
ANISOU 3501  O   LYS B 176     6388   7649   6783   -165   -328   -293       O
ATOM   3502  CB  LYS B 176      -6.752  24.123  27.125  1.00 60.56           C
ANISOU 3502  CB  LYS B 176     7164   8317   7529   -116   -292   -226       C
ATOM   3503  CG  LYS B 176      -6.713  25.485  27.934  1.00 61.89           C
ANISOU 3503  CG  LYS B 176     7359   8474   7682   -143   -269   -251       C
ATOM   3504  CD  LYS B 176      -8.037  25.800  28.701  1.00 66.02           C
ANISOU 3504  CD  LYS B 176     7918   8967   8199   -132   -241   -235       C
ATOM   3505  CE  LYS B 176      -8.040  27.149  29.487  1.00 63.92           C
ANISOU 3505  CE  LYS B 176     7688   8683   7916   -158   -213   -258       C
ATOM   3506  NZ  LYS B 176      -7.260  27.046  30.755  1.00 54.95           N
ANISOU 3506  NZ  LYS B 176     6566   7571   6743   -172   -237   -282       N
ATOM   3507  N   ASN B 177      -3.447  22.703  26.824  1.00 63.39           N
ANISOU 3507  N   ASN B 177     7438   8766   7882   -117   -366   -265       N
ATOM   3508  CA  ASN B 177      -2.107  22.648  27.433  1.00 63.58           C
ANISOU 3508  CA  ASN B 177     7431   8830   7896   -128   -397   -292       C
ATOM   3509  C   ASN B 177      -2.117  22.958  28.927  1.00 65.74           C
ANISOU 3509  C   ASN B 177     7728   9114   8137   -136   -415   -307       C
ATOM   3510  O   ASN B 177      -1.131  23.468  29.471  1.00 64.39           O
ANISOU 3510  O   ASN B 177     7539   8968   7957   -161   -436   -337       O
ATOM   3511  CB  ASN B 177      -1.148  23.608  26.721  1.00 64.98           C
ANISOU 3511  CB  ASN B 177     7580   9014   8095   -164   -381   -320       C
ATOM   3512  N   VAL B 178      -3.197  22.602  29.607  1.00 57.69           N
ANISOU 3512  N   VAL B 178     6748   8074   7097   -117   -410   -286       N
ATOM   3513  CA  VAL B 178      -3.296  22.733  31.055  1.00 55.72           C
ANISOU 3513  CA  VAL B 178     6532   7828   6810   -120   -425   -296       C
ATOM   3514  C   VAL B 178      -3.294  21.324  31.643  1.00 57.32           C
ANISOU 3514  C   VAL B 178     6740   8046   6991    -81   -457   -278       C
ATOM   3515  O   VAL B 178      -4.091  20.482  31.219  1.00 56.32           O
ANISOU 3515  O   VAL B 178     6622   7903   6874    -54   -445   -248       O
ATOM   3516  CB  VAL B 178      -4.540  23.533  31.478  1.00 54.76           C
ANISOU 3516  CB  VAL B 178     6458   7666   6681   -129   -383   -289       C
ATOM   3517  CG1 VAL B 178      -5.818  22.946  30.892  1.00 55.37           C
ANISOU 3517  CG1 VAL B 178     6545   7715   6778   -102   -357   -253       C
ATOM   3518  CG2 VAL B 178      -4.620  23.613  32.990  1.00 54.18           C
ANISOU 3518  CG2 VAL B 178     6429   7593   6565   -131   -396   -299       C
ATOM   3519  N   PRO B 179      -2.377  20.999  32.546  1.00 54.11           N
ANISOU 3519  N   PRO B 179     6330   7672   6558    -76   -501   -294       N
ATOM   3520  CA  PRO B 179      -2.282  19.615  33.039  1.00 52.57           C
ANISOU 3520  CA  PRO B 179     6143   7491   6340    -34   -534   -275       C
ATOM   3521  C   PRO B 179      -3.483  19.212  33.882  1.00 52.14           C
ANISOU 3521  C   PRO B 179     6150   7405   6257    -17   -515   -254       C
ATOM   3522  O   PRO B 179      -3.959  19.988  34.714  1.00 54.14           O
ANISOU 3522  O   PRO B 179     6444   7640   6489    -36   -498   -263       O
ATOM   3523  CB  PRO B 179      -0.998  19.623  33.880  1.00 57.01           C
ANISOU 3523  CB  PRO B 179     6689   8095   6879    -37   -588   -302       C
ATOM   3524  CG  PRO B 179      -0.302  20.945  33.559  1.00 59.86           C
ANISOU 3524  CG  PRO B 179     7017   8467   7260    -85   -583   -335       C
ATOM   3525  CD  PRO B 179      -1.381  21.894  33.154  1.00 54.34           C
ANISOU 3525  CD  PRO B 179     6348   7725   6574   -109   -526   -330       C
ATOM   3526  N   PHE B 180      -3.933  17.965  33.702  1.00 50.95           N
ANISOU 3526  N   PHE B 180     6007   7246   6104     18   -515   -225       N
ATOM   3527  CA  PHE B 180      -4.997  17.402  34.530  1.00 49.82           C
ANISOU 3527  CA  PHE B 180     5920   7075   5934     35   -497   -204       C
ATOM   3528  C   PHE B 180      -4.408  16.874  35.833  1.00 51.50           C
ANISOU 3528  C   PHE B 180     6169   7304   6096     54   -537   -211       C
ATOM   3529  O   PHE B 180      -3.493  16.046  35.817  1.00 51.60           O
ANISOU 3529  O   PHE B 180     6162   7346   6098     80   -580   -211       O
ATOM   3530  CB  PHE B 180      -5.730  16.281  33.800  1.00 45.69           C
ANISOU 3530  CB  PHE B 180     5397   6535   5430     60   -480   -172       C
ATOM   3531  CG  PHE B 180      -6.682  15.505  34.687  1.00 53.53           C
ANISOU 3531  CG  PHE B 180     6445   7501   6394     78   -463   -150       C
ATOM   3532  CD1 PHE B 180      -7.985  15.950  34.887  1.00 53.52           C
ANISOU 3532  CD1 PHE B 180     6470   7464   6403     64   -414   -139       C
ATOM   3533  CD2 PHE B 180      -6.272  14.332  35.331  1.00 54.34           C
ANISOU 3533  CD2 PHE B 180     6575   7613   6460    110   -493   -141       C
ATOM   3534  CE1 PHE B 180      -8.863  15.246  35.701  1.00 51.44           C
ANISOU 3534  CE1 PHE B 180     6256   7174   6117     77   -391   -121       C
ATOM   3535  CE2 PHE B 180      -7.146  13.617  36.152  1.00 52.48           C
ANISOU 3535  CE2 PHE B 180     6397   7348   6196    125   -471   -122       C
ATOM   3536  CZ  PHE B 180      -8.445  14.078  36.336  1.00 53.32           C
ANISOU 3536  CZ  PHE B 180     6526   7418   6315    106   -419   -113       C
ATOM   3537  N   VAL B 181      -4.911  17.358  36.959  1.00 50.12           N
ANISOU 3537  N   VAL B 181     6048   7108   5885     43   -524   -218       N
ATOM   3538  CA  VAL B 181      -4.339  17.016  38.256  1.00 52.44           C
ANISOU 3538  CA  VAL B 181     6387   7415   6125     57   -565   -228       C
ATOM   3539  C   VAL B 181      -5.069  15.801  38.803  1.00 49.08           C
ANISOU 3539  C   VAL B 181     6013   6964   5670     92   -553   -199       C
ATOM   3540  O   VAL B 181      -6.303  15.793  38.877  1.00 54.23           O
ANISOU 3540  O   VAL B 181     6698   7578   6329     88   -499   -181       O
ATOM   3541  CB  VAL B 181      -4.421  18.205  39.234  1.00 56.44           C
ANISOU 3541  CB  VAL B 181     6936   7909   6601     25   -557   -252       C
ATOM   3542  CG1 VAL B 181      -4.139  17.752  40.669  1.00 52.76           C
ANISOU 3542  CG1 VAL B 181     6537   7443   6068     43   -592   -257       C
ATOM   3543  CG2 VAL B 181      -3.439  19.300  38.831  1.00 49.60           C
ANISOU 3543  CG2 VAL B 181     6021   7072   5754    -10   -580   -285       C
ATOM   3544  N   THR B 182      -4.307  14.768  39.148  1.00 49.08           N
ANISOU 3544  N   THR B 182     6021   6987   5642    127   -601   -194       N
ATOM   3545  CA  THR B 182      -4.808  13.593  39.857  1.00 47.58           C
ANISOU 3545  CA  THR B 182     5893   6774   5412    162   -596   -170       C
ATOM   3546  C   THR B 182      -3.861  13.326  41.026  1.00 48.71           C
ANISOU 3546  C   THR B 182     6075   6937   5496    183   -656   -183       C
ATOM   3547  O   THR B 182      -3.118  14.205  41.485  1.00 52.85           O
ANISOU 3547  O   THR B 182     6590   7484   6005    162   -692   -212       O
ATOM   3548  CB  THR B 182      -4.944  12.379  38.925  1.00 48.06           C
ANISOU 3548  CB  THR B 182     5930   6834   5499    190   -590   -143       C
ATOM   3549  OG1 THR B 182      -5.231  11.210  39.702  1.00 45.71           O
ANISOU 3549  OG1 THR B 182     5697   6515   5155    225   -592   -123       O
ATOM   3550  CG2 THR B 182      -3.654  12.145  38.121  1.00 47.75           C
ANISOU 3550  CG2 THR B 182     5821   6839   5482    206   -639   -153       C
ATOM   3551  N   THR B 183      -3.841  12.092  41.516  1.00 49.24           N
ANISOU 3551  N   THR B 183     6187   6996   5526    225   -673   -163       N
ATOM   3552  CA  THR B 183      -2.998  11.803  42.671  1.00 52.06           C
ANISOU 3552  CA  THR B 183     6589   7370   5821    250   -734   -174       C
ATOM   3553  C   THR B 183      -2.640  10.325  42.718  1.00 54.18           C
ANISOU 3553  C   THR B 183     6877   7643   6067    305   -763   -150       C
ATOM   3554  O   THR B 183      -3.307   9.486  42.098  1.00 51.55           O
ANISOU 3554  O   THR B 183     6547   7286   5753    320   -723   -124       O
ATOM   3555  CB  THR B 183      -3.686  12.214  43.976  1.00 52.91           C
ANISOU 3555  CB  THR B 183     6791   7440   5874    237   -711   -178       C
ATOM   3556  OG1 THR B 183      -2.893  11.768  45.080  1.00 56.21           O
ANISOU 3556  OG1 THR B 183     7262   7870   6225    267   -775   -184       O
ATOM   3557  CG2 THR B 183      -5.084  11.608  44.075  1.00 51.65           C
ANISOU 3557  CG2 THR B 183     6688   7226   5710    241   -637   -149       C
ATOM   3558  N   VAL B 184      -1.565  10.020  43.470  1.00 51.05           N
ANISOU 3558  N   VAL B 184     6495   7276   5627    336   -835   -160       N
ATOM   3559  CA  VAL B 184      -1.220   8.636  43.807  1.00 51.22           C
ANISOU 3559  CA  VAL B 184     6556   7296   5610    396   -866   -138       C
ATOM   3560  C   VAL B 184      -1.934   8.123  45.050  1.00 50.78           C
ANISOU 3560  C   VAL B 184     6618   7193   5482    412   -849   -124       C
ATOM   3561  O   VAL B 184      -1.859   6.920  45.336  1.00 52.55           O
ANISOU 3561  O   VAL B 184     6891   7403   5671    461   -861   -101       O
ATOM   3562  CB  VAL B 184       0.295   8.447  44.030  1.00 54.65           C
ANISOU 3562  CB  VAL B 184     6949   7784   6031    430   -957   -151       C
ATOM   3563  CG1 VAL B 184       1.054   8.475  42.710  1.00 51.25           C
ANISOU 3563  CG1 VAL B 184     6406   7395   5670    432   -969   -156       C
ATOM   3564  CG2 VAL B 184       0.808   9.526  44.974  1.00 55.07           C
ANISOU 3564  CG2 VAL B 184     7014   7857   6053    401  -1004   -183       C
ATOM   3565  N   ASN B 185      -2.644   8.981  45.782  1.00 51.62           N
ANISOU 3565  N   ASN B 185     6778   7271   5566    374   -815   -135       N
ATOM   3566  CA  ASN B 185      -3.396   8.569  46.964  1.00 52.47           C
ANISOU 3566  CA  ASN B 185     7002   7327   5605    386   -786   -123       C
ATOM   3567  C   ASN B 185      -4.846   8.209  46.637  1.00 52.42           C
ANISOU 3567  C   ASN B 185     7026   7269   5623    370   -691    -99       C
ATOM   3568  O   ASN B 185      -5.715   8.326  47.508  1.00 50.15           O
ANISOU 3568  O   ASN B 185     6823   6934   5297    358   -643    -95       O
ATOM   3569  CB  ASN B 185      -3.358   9.660  48.034  1.00 52.51           C
ANISOU 3569  CB  ASN B 185     7060   7325   5567    355   -798   -148       C
ATOM   3570  CG  ASN B 185      -1.949  10.144  48.326  1.00 57.19           C
ANISOU 3570  CG  ASN B 185     7615   7971   6142    360   -894   -176       C
ATOM   3571  OD1 ASN B 185      -0.968   9.424  48.101  1.00 57.16           O
ANISOU 3571  OD1 ASN B 185     7573   8006   6139    401   -959   -172       O
ATOM   3572  ND2 ASN B 185      -1.840  11.375  48.829  1.00 54.58           N
ANISOU 3572  ND2 ASN B 185     7295   7645   5800    317   -903   -205       N
ATOM   3573  N   GLU B 186      -5.128   7.873  45.378  1.00 56.25           N
ANISOU 3573  N   GLU B 186     7440   7760   6172    366   -663    -86       N
ATOM   3574  CA  GLU B 186      -6.447   7.463  44.909  1.00 51.63           C
ANISOU 3574  CA  GLU B 186     6867   7132   5618    350   -582    -63       C
ATOM   3575  C   GLU B 186      -6.242   6.169  44.122  1.00 54.17           C
ANISOU 3575  C   GLU B 186     7169   7458   5955    385   -591    -40       C
ATOM   3576  O   GLU B 186      -5.424   6.137  43.195  1.00 54.67           O
ANISOU 3576  O   GLU B 186     7156   7562   6055    395   -630    -45       O
ATOM   3577  CB  GLU B 186      -7.049   8.585  44.040  1.00 54.48           C
ANISOU 3577  CB  GLU B 186     7155   7496   6047    301   -540    -73       C
ATOM   3578  CG  GLU B 186      -8.511   8.527  43.546  1.00 56.48           C
ANISOU 3578  CG  GLU B 186     7406   7709   6344    274   -456    -55       C
ATOM   3579  CD  GLU B 186      -8.880   9.695  42.540  1.00 57.14           C
ANISOU 3579  CD  GLU B 186     7406   7805   6498    234   -431    -66       C
ATOM   3580  OE1 GLU B 186     -10.004   9.671  41.995  1.00 55.64           O
ANISOU 3580  OE1 GLU B 186     7200   7590   6352    214   -373    -51       O
ATOM   3581  OE2 GLU B 186      -8.068  10.630  42.280  1.00 55.31           O
ANISOU 3581  OE2 GLU B 186     7125   7609   6279    221   -469    -89       O
ATOM   3582  N   TYR B 187      -6.941   5.096  44.529  1.00 45.69           N
ANISOU 3582  N   TYR B 187     6171   6340   4849    404   -553    -16       N
ATOM   3583  CA  TYR B 187      -6.979   3.795  43.849  1.00 39.40           C
ANISOU 3583  CA  TYR B 187     5376   5534   4062    432   -547      8       C
ATOM   3584  C   TYR B 187      -8.434   3.584  43.434  1.00 39.64           C
ANISOU 3584  C   TYR B 187     5414   5519   4127    396   -464     25       C
ATOM   3585  O   TYR B 187      -9.301   3.304  44.274  1.00 33.61           O
ANISOU 3585  O   TYR B 187     4729   4710   3332    389   -415     34       O
ATOM   3586  CB  TYR B 187      -6.497   2.652  44.744  1.00 42.05           C
ANISOU 3586  CB  TYR B 187     5801   5854   4324    486   -577     22       C
ATOM   3587  CG  TYR B 187      -5.045   2.721  45.174  1.00 44.75           C
ANISOU 3587  CG  TYR B 187     6132   6241   4630    528   -666      9       C
ATOM   3588  CD1 TYR B 187      -4.600   3.730  46.044  1.00 48.47           C
ANISOU 3588  CD1 TYR B 187     6613   6730   5071    517   -704    -16       C
ATOM   3589  CD2 TYR B 187      -4.112   1.788  44.712  1.00 42.16           C
ANISOU 3589  CD2 TYR B 187     5784   5937   4299    580   -714     20       C
ATOM   3590  CE1 TYR B 187      -3.260   3.810  46.447  1.00 49.57           C
ANISOU 3590  CE1 TYR B 187     6738   6915   5182    552   -792    -29       C
ATOM   3591  CE2 TYR B 187      -2.759   1.859  45.114  1.00 44.93           C
ANISOU 3591  CE2 TYR B 187     6116   6334   4623    621   -799      7       C
ATOM   3592  CZ  TYR B 187      -2.348   2.870  45.984  1.00 47.12           C
ANISOU 3592  CZ  TYR B 187     6399   6632   4874    605   -840    -18       C
ATOM   3593  OH  TYR B 187      -1.043   2.966  46.394  1.00 47.62           O
ANISOU 3593  OH  TYR B 187     6438   6742   4913    641   -929    -31       O
ATOM   3594  N   ARG B 188      -8.721   3.781  42.152  1.00 37.15           N
ANISOU 3594  N   ARG B 188     5019   5217   3881    371   -448     27       N
ATOM   3595  CA  ARG B 188     -10.091   3.744  41.672  1.00 37.74           C
ANISOU 3595  CA  ARG B 188     5085   5256   3998    333   -378     40       C
ATOM   3596  C   ARG B 188     -10.109   3.184  40.263  1.00 35.86           C
ANISOU 3596  C   ARG B 188     4789   5028   3810    330   -380     51       C
ATOM   3597  O   ARG B 188      -9.129   3.302  39.528  1.00 41.44           O
ANISOU 3597  O   ARG B 188     5439   5773   4533    345   -428     43       O
ATOM   3598  CB  ARG B 188     -10.736   5.144  41.688  1.00 35.94           C
ANISOU 3598  CB  ARG B 188     4818   5030   3809    289   -346     24       C
ATOM   3599  CG  ARG B 188     -10.656   5.841  40.363  1.00 35.46           C
ANISOU 3599  CG  ARG B 188     4659   4998   3815    266   -356     17       C
ATOM   3600  CD  ARG B 188     -11.169   7.231  40.468  1.00 36.72           C
ANISOU 3600  CD  ARG B 188     4789   5158   4004    230   -329      2       C
ATOM   3601  NE  ARG B 188     -12.614   7.260  40.616  1.00 36.16           N
ANISOU 3601  NE  ARG B 188     4734   5046   3958    203   -258     15       N
ATOM   3602  CZ  ARG B 188     -13.317   8.369  40.788  1.00 31.20           C
ANISOU 3602  CZ  ARG B 188     4089   4407   3357    175   -219      7       C
ATOM   3603  NH1 ARG B 188     -12.706   9.554  40.808  1.00 30.87           N
ANISOU 3603  NH1 ARG B 188     4019   4393   3319    167   -245    -15       N
ATOM   3604  NH2 ARG B 188     -14.630   8.290  40.902  1.00 32.30           N
ANISOU 3604  NH2 ARG B 188     4238   4510   3524    155   -154     22       N
ATOM   3605  N   ALA B 189     -11.244   2.612  39.878  1.00 32.21           N
ANISOU 3605  N   ALA B 189     4338   4529   3373    306   -327     69       N
ATOM   3606  CA  ALA B 189     -11.446   2.122  38.528  1.00 32.17           C
ANISOU 3606  CA  ALA B 189     4283   4525   3414    294   -324     79       C
ATOM   3607  C   ALA B 189     -12.433   3.019  37.793  1.00 29.89           C
ANISOU 3607  C   ALA B 189     3930   4234   3191    246   -290     76       C
ATOM   3608  O   ALA B 189     -13.246   3.701  38.419  1.00 28.86           O
ANISOU 3608  O   ALA B 189     3808   4087   3069    221   -251     73       O
ATOM   3609  CB  ALA B 189     -11.973   0.673  38.528  1.00 32.43           C
ANISOU 3609  CB  ALA B 189     4378   4518   3426    302   -296    102       C
ATOM   3610  N   ILE B 190     -12.299   3.061  36.466  1.00 26.95           N
ANISOU 3610  N   ILE B 190     3497   3880   2865    235   -307     77       N
ATOM   3611  CA  ILE B 190     -13.247   3.692  35.559  1.00 26.40           C
ANISOU 3611  CA  ILE B 190     3368   3805   2857    193   -282     79       C
ATOM   3612  C   ILE B 190     -13.584   2.635  34.525  1.00 33.69           C
ANISOU 3612  C   ILE B 190     4289   4712   3799    186   -279     96       C
ATOM   3613  O   ILE B 190     -12.696   1.906  34.065  1.00 32.16           O
ANISOU 3613  O   ILE B 190     4106   4528   3584    215   -311     99       O
ATOM   3614  CB  ILE B 190     -12.693   4.963  34.876  1.00 23.31           C
ANISOU 3614  CB  ILE B 190     2905   3450   2500    185   -310     61       C
ATOM   3615  CG1 ILE B 190     -11.548   4.620  33.936  1.00 28.51           C
ANISOU 3615  CG1 ILE B 190     3538   4137   3159    208   -355     57       C
ATOM   3616  CG2 ILE B 190     -12.156   5.936  35.900  1.00 30.69           C
ANISOU 3616  CG2 ILE B 190     3849   4403   3408    193   -320     41       C
ATOM   3617  CD1 ILE B 190     -10.856   5.821  33.349  1.00 32.31           C
ANISOU 3617  CD1 ILE B 190     3956   4653   3667    201   -381     37       C
ATOM   3618  N   THR B 191     -14.859   2.547  34.162  1.00 28.17           N
ANISOU 3618  N   THR B 191     3577   3986   3139    148   -241    107       N
ATOM   3619  CA  THR B 191     -15.364   1.450  33.360  1.00 29.01           C
ANISOU 3619  CA  THR B 191     3695   4070   3258    134   -233    123       C
ATOM   3620  C   THR B 191     -16.049   2.002  32.123  1.00 33.81           C
ANISOU 3620  C   THR B 191     4236   4683   3929     98   -235    124       C
ATOM   3621  O   THR B 191     -16.914   2.876  32.226  1.00 30.86           O
ANISOU 3621  O   THR B 191     3824   4307   3594     71   -212    122       O
ATOM   3622  CB  THR B 191     -16.348   0.614  34.167  1.00 31.00           C
ANISOU 3622  CB  THR B 191     4004   4280   3496    119   -184    137       C
ATOM   3623  OG1 THR B 191     -15.768   0.285  35.445  1.00 31.53           O
ANISOU 3623  OG1 THR B 191     4139   4340   3501    153   -180    135       O
ATOM   3624  CG2 THR B 191     -16.708  -0.634  33.418  1.00 28.00           C
ANISOU 3624  CG2 THR B 191     3647   3873   3118    105   -179    152       C
ATOM   3625  N   PHE B 192     -15.696   1.472  30.964  1.00 33.67           N
ANISOU 3625  N   PHE B 192     4208   4667   3918     98   -263    129       N
ATOM   3626  CA  PHE B 192     -16.428   1.829  29.764  1.00 35.13           C
ANISOU 3626  CA  PHE B 192     4342   4851   4157     63   -268    133       C
ATOM   3627  C   PHE B 192     -17.885   1.463  29.986  1.00 37.91           C
ANISOU 3627  C   PHE B 192     4695   5171   4537     24   -229    145       C
ATOM   3628  O   PHE B 192     -18.189   0.413  30.568  1.00 34.59           O
ANISOU 3628  O   PHE B 192     4329   4723   4090     22   -204    155       O
ATOM   3629  CB  PHE B 192     -15.841   1.085  28.549  1.00 36.52           C
ANISOU 3629  CB  PHE B 192     4526   5025   4326     70   -298    137       C
ATOM   3630  CG  PHE B 192     -16.608   1.284  27.253  1.00 36.32           C
ANISOU 3630  CG  PHE B 192     4461   4992   4347     33   -309    142       C
ATOM   3631  CD1 PHE B 192     -17.072   2.536  26.874  1.00 36.80           C
ANISOU 3631  CD1 PHE B 192     4461   5068   4452     14   -313    136       C
ATOM   3632  CD2 PHE B 192     -16.850   0.209  26.407  1.00 35.96           C
ANISOU 3632  CD2 PHE B 192     4444   4922   4297     17   -316    154       C
ATOM   3633  CE1 PHE B 192     -17.768   2.699  25.669  1.00 38.18           C
ANISOU 3633  CE1 PHE B 192     4603   5235   4666    -17   -329    142       C
ATOM   3634  CE2 PHE B 192     -17.551   0.368  25.200  1.00 34.77           C
ANISOU 3634  CE2 PHE B 192     4263   4764   4185    -18   -333    158       C
ATOM   3635  CZ  PHE B 192     -18.007   1.605  24.828  1.00 31.77           C
ANISOU 3635  CZ  PHE B 192     3822   4401   3849    -34   -341    153       C
ATOM   3636  N   VAL B 193     -18.780   2.382  29.625  1.00 34.06           N
ANISOU 3636  N   VAL B 193     4149   4689   4104     -5   -220    145       N
ATOM   3637  CA  VAL B 193     -20.201   2.180  29.884  1.00 31.07           C
ANISOU 3637  CA  VAL B 193     3758   4285   3762    -42   -181    156       C
ATOM   3638  C   VAL B 193     -20.724   1.011  29.062  1.00 37.03           C
ANISOU 3638  C   VAL B 193     4528   5015   4525    -71   -188    168       C
ATOM   3639  O   VAL B 193     -21.684   0.329  29.462  1.00 36.91           O
ANISOU 3639  O   VAL B 193     4529   4973   4523   -100   -152    178       O
ATOM   3640  CB  VAL B 193     -20.950   3.496  29.605  1.00 35.78           C
ANISOU 3640  CB  VAL B 193     4283   4896   4418    -60   -176    153       C
ATOM   3641  CG1 VAL B 193     -20.711   3.939  28.153  1.00 41.91           C
ANISOU 3641  CG1 VAL B 193     5016   5689   5220    -65   -224    151       C
ATOM   3642  CG2 VAL B 193     -22.438   3.396  29.931  1.00 37.03           C
ANISOU 3642  CG2 VAL B 193     4416   5032   4624    -96   -132    164       C
ATOM   3643  N   GLY B 194     -20.067   0.718  27.927  1.00 46.63           N
ANISOU 3643  N   GLY B 194     5746   6239   5732    -65   -231    168       N
ATOM   3644  CA  GLY B 194     -20.474  -0.418  27.108  1.00 41.30           C
ANISOU 3644  CA  GLY B 194     5096   5538   5058    -92   -241    178       C
ATOM   3645  C   GLY B 194     -20.434  -1.749  27.842  1.00 45.17           C
ANISOU 3645  C   GLY B 194     5661   5997   5504    -89   -212    186       C
ATOM   3646  O   GLY B 194     -21.339  -2.571  27.686  1.00 47.73           O
ANISOU 3646  O   GLY B 194     6000   6292   5842   -128   -194    195       O
ATOM   3647  N   GLU B 195     -19.380  -1.997  28.636  1.00 36.49           N
ANISOU 3647  N   GLU B 195     4611   4904   4350    -43   -209    182       N
ATOM   3648  CA  GLU B 195     -19.347  -3.246  29.402  1.00 37.40           C
ANISOU 3648  CA  GLU B 195     4806   4986   4418    -35   -179    190       C
ATOM   3649  C   GLU B 195     -20.388  -3.244  30.515  1.00 38.12           C
ANISOU 3649  C   GLU B 195     4906   5056   4523    -60   -126    194       C
ATOM   3650  O   GLU B 195     -21.078  -4.252  30.718  1.00 35.86           O
ANISOU 3650  O   GLU B 195     4662   4733   4230    -88    -93    203       O
ATOM   3651  CB  GLU B 195     -17.957  -3.521  29.979  1.00 31.78           C
ANISOU 3651  CB  GLU B 195     4145   4285   3644     25   -194    186       C
ATOM   3652  CG  GLU B 195     -16.865  -3.996  28.967  1.00 31.20           C
ANISOU 3652  CG  GLU B 195     4086   4220   3547     54   -235    186       C
ATOM   3653  CD  GLU B 195     -15.481  -4.298  29.649  1.00 36.40           C
ANISOU 3653  CD  GLU B 195     4791   4893   4149    119   -249    183       C
ATOM   3654  OE1 GLU B 195     -15.427  -4.814  30.806  1.00 35.06           O
ANISOU 3654  OE1 GLU B 195     4678   4706   3938    139   -227    188       O
ATOM   3655  OE2 GLU B 195     -14.441  -3.917  29.057  1.00 31.42           O
ANISOU 3655  OE2 GLU B 195     4132   4290   3515    149   -284    176       O
ATOM   3656  N   VAL B 196     -20.584  -2.099  31.178  1.00 36.77           N
ANISOU 3656  N   VAL B 196     4692   4905   4373    -55   -112    186       N
ATOM   3657  CA  VAL B 196     -21.598  -2.001  32.232  1.00 40.18           C
ANISOU 3657  CA  VAL B 196     5131   5316   4821    -78    -53    190       C
ATOM   3658  C   VAL B 196     -22.980  -2.335  31.684  1.00 40.25           C
ANISOU 3658  C   VAL B 196     5102   5303   4888   -136    -30    198       C
ATOM   3659  O   VAL B 196     -23.737  -3.094  32.300  1.00 34.55           O
ANISOU 3659  O   VAL B 196     4416   4547   4165   -162     19    206       O
ATOM   3660  CB  VAL B 196     -21.576  -0.589  32.850  1.00 37.03           C
ANISOU 3660  CB  VAL B 196     4688   4942   4440    -63    -45    179       C
ATOM   3661  CG1 VAL B 196     -22.684  -0.414  33.874  1.00 35.42           C
ANISOU 3661  CG1 VAL B 196     4487   4714   4259    -86     22    183       C
ATOM   3662  CG2 VAL B 196     -20.267  -0.362  33.486  1.00 37.36           C
ANISOU 3662  CG2 VAL B 196     4771   5002   4422    -12    -68    170       C
ATOM   3663  N   VAL B 197     -23.305  -1.802  30.494  1.00 40.53           N
ANISOU 3663  N   VAL B 197     5066   5358   4975   -158    -67    198       N
ATOM   3664  CA  VAL B 197     -24.633  -1.928  29.905  1.00 39.96           C
ANISOU 3664  CA  VAL B 197     4942   5274   4967   -213    -57    205       C
ATOM   3665  C   VAL B 197     -24.831  -3.300  29.281  1.00 44.18           C
ANISOU 3665  C   VAL B 197     5520   5778   5487   -244    -65    212       C
ATOM   3666  O   VAL B 197     -25.925  -3.878  29.351  1.00 40.17           O
ANISOU 3666  O   VAL B 197     5006   5245   5012   -293    -33    219       O
ATOM   3667  CB  VAL B 197     -24.833  -0.810  28.877  1.00 39.50           C
ANISOU 3667  CB  VAL B 197     4798   5247   4962   -219   -100    202       C
ATOM   3668  CG1 VAL B 197     -26.046  -1.087  28.024  1.00 42.04           C
ANISOU 3668  CG1 VAL B 197     5070   5559   5345   -274   -109    210       C
ATOM   3669  CG2 VAL B 197     -24.975   0.523  29.585  1.00 43.87           C
ANISOU 3669  CG2 VAL B 197     5307   5821   5540   -199    -77    196       C
ATOM   3670  N   GLU B 198     -23.794  -3.830  28.631  1.00 39.19           N
ANISOU 3670  N   GLU B 198     4934   5149   4809   -219   -106    211       N
ATOM   3671  CA  GLU B 198     -23.921  -5.134  28.010  1.00 39.75           C
ANISOU 3671  CA  GLU B 198     5057   5188   4860   -247   -113    218       C
ATOM   3672  C   GLU B 198     -23.889  -6.270  29.023  1.00 38.99           C
ANISOU 3672  C   GLU B 198     5048   5052   4714   -243    -63    223       C
ATOM   3673  O   GLU B 198     -24.333  -7.378  28.707  1.00 43.06           O
ANISOU 3673  O   GLU B 198     5606   5533   5221   -280    -52    229       O
ATOM   3674  CB  GLU B 198     -22.848  -5.274  26.935  1.00 41.61           C
ANISOU 3674  CB  GLU B 198     5311   5435   5063   -219   -167    215       C
ATOM   3675  CG  GLU B 198     -23.221  -4.347  25.771  1.00 52.65           C
ANISOU 3675  CG  GLU B 198     6629   6858   6516   -241   -212    212       C
ATOM   3676  CD  GLU B 198     -22.071  -4.019  24.849  1.00 59.09           C
ANISOU 3676  CD  GLU B 198     7450   7695   7307   -204   -260    207       C
ATOM   3677  OE1 GLU B 198     -21.977  -2.847  24.393  1.00 61.96           O
ANISOU 3677  OE1 GLU B 198     7752   8088   7702   -196   -286    201       O
ATOM   3678  OE2 GLU B 198     -21.283  -4.955  24.575  1.00 71.33           O
ANISOU 3678  OE2 GLU B 198     9069   9228   8807   -185   -267    209       O
ATOM   3679  N   ASN B 199     -23.389  -6.030  30.227  1.00 35.93           N
ANISOU 3679  N   ASN B 199     4694   4668   4291   -202    -34    221       N
ATOM   3680  CA  ASN B 199     -23.418  -7.060  31.253  1.00 41.05           C
ANISOU 3680  CA  ASN B 199     5430   5276   4889   -198     16    227       C
ATOM   3681  C   ASN B 199     -24.681  -7.051  32.106  1.00 42.18           C
ANISOU 3681  C   ASN B 199     5563   5396   5069   -241     82    230       C
ATOM   3682  O   ASN B 199     -24.787  -7.918  32.976  1.00 41.42           O
ANISOU 3682  O   ASN B 199     5545   5260   4931   -242    130    236       O
ATOM   3683  CB  ASN B 199     -22.226  -6.892  32.215  1.00 41.11           C
ANISOU 3683  CB  ASN B 199     5493   5295   4833   -129     14    224       C
ATOM   3684  CG  ASN B 199     -20.997  -7.670  31.790  1.00 38.47           C
ANISOU 3684  CG  ASN B 199     5220   4958   4438    -84    -24    227       C
ATOM   3685  OD1 ASN B 199     -21.091  -8.726  31.142  1.00 39.11           O
ANISOU 3685  OD1 ASN B 199     5345   5011   4506   -103    -26    234       O
ATOM   3686  ND2 ASN B 199     -19.824  -7.156  32.178  1.00 32.43           N
ANISOU 3686  ND2 ASN B 199     4461   4223   3637    -24    -52    221       N
ATOM   3687  N   ILE B 200     -25.605  -6.083  31.922  1.00 41.39           N
ANISOU 3687  N   ILE B 200     5368   5315   5042   -273     88    227       N
ATOM   3688  CA  ILE B 200     -26.694  -5.884  32.895  1.00 44.92           C
ANISOU 3688  CA  ILE B 200     5799   5743   5525   -303    158    230       C
ATOM   3689  C   ILE B 200     -27.716  -6.996  32.856  1.00 46.46           C
ANISOU 3689  C   ILE B 200     6017   5896   5740   -364    201    236       C
ATOM   3690  O   ILE B 200     -28.408  -7.241  33.854  1.00 40.72           O
ANISOU 3690  O   ILE B 200     5315   5139   5019   -384    273    239       O
ATOM   3691  CB  ILE B 200     -27.441  -4.546  32.758  1.00 42.30           C
ANISOU 3691  CB  ILE B 200     5360   5443   5270   -317    160    226       C
ATOM   3692  CG1 ILE B 200     -28.056  -4.412  31.373  1.00 44.08           C
ANISOU 3692  CG1 ILE B 200     5504   5685   5560   -358    112    228       C
ATOM   3693  CG2 ILE B 200     -26.595  -3.375  33.230  1.00 44.93           C
ANISOU 3693  CG2 ILE B 200     5682   5808   5581   -261    143    218       C
ATOM   3694  CD1 ILE B 200     -29.276  -3.574  31.365  1.00 48.76           C
ANISOU 3694  CD1 ILE B 200     5998   6289   6237   -391    136    229       C
ATOM   3695  N   GLU B 201     -27.937  -7.590  31.688  1.00 49.76           N
ANISOU 3695  N   GLU B 201     6419   6310   6177   -401    161    238       N
ATOM   3696  CA  GLU B 201     -28.940  -8.640  31.622  1.00 47.47           C
ANISOU 3696  CA  GLU B 201     6147   5979   5909   -467    200    243       C
ATOM   3697  C   GLU B 201     -28.533  -9.816  32.491  1.00 47.59           C
ANISOU 3697  C   GLU B 201     6287   5947   5849   -454    249    247       C
ATOM   3698  O   GLU B 201     -29.384 -10.435  33.128  1.00 47.67           O
ANISOU 3698  O   GLU B 201     6325   5918   5871   -497    316    250       O
ATOM   3699  CB  GLU B 201     -29.141  -9.069  30.173  1.00 49.85           C
ANISOU 3699  CB  GLU B 201     6420   6284   6235   -507    141    242       C
ATOM   3700  CG  GLU B 201     -29.344  -7.902  29.220  1.00 51.75           C
ANISOU 3700  CG  GLU B 201     6553   6573   6538   -509     81    239       C
ATOM   3701  CD  GLU B 201     -28.043  -7.461  28.522  1.00 57.83           C
ANISOU 3701  CD  GLU B 201     7336   7372   7264   -451     15    236       C
ATOM   3702  OE1 GLU B 201     -26.991  -7.302  29.209  1.00 53.23           O
ANISOU 3702  OE1 GLU B 201     6806   6796   6624   -391     23    234       O
ATOM   3703  OE2 GLU B 201     -28.082  -7.290  27.275  1.00 58.37           O
ANISOU 3703  OE2 GLU B 201     7365   7456   7357   -469    -45    235       O
ATOM   3704  N   LYS B 202     -27.233 -10.056  32.636  1.00 40.85           N
ANISOU 3704  N   LYS B 202     5508   5095   4917   -391    221    247       N
ATOM   3705  CA  LYS B 202     -26.817 -11.165  33.473  1.00 41.02           C
ANISOU 3705  CA  LYS B 202     5652   5069   4863   -371    264    253       C
ATOM   3706  C   LYS B 202     -27.193 -10.966  34.938  1.00 37.09           C
ANISOU 3706  C   LYS B 202     5187   4551   4354   -363    338    255       C
ATOM   3707  O   LYS B 202     -27.419 -11.945  35.640  1.00 40.86           O
ANISOU 3707  O   LYS B 202     5755   4977   4791   -376    395    260       O
ATOM   3708  CB  LYS B 202     -25.327 -11.370  33.295  1.00 39.74           C
ANISOU 3708  CB  LYS B 202     5551   4921   4628   -299    213    254       C
ATOM   3709  CG  LYS B 202     -24.969 -11.885  31.889  1.00 39.79           C
ANISOU 3709  CG  LYS B 202     5555   4931   4633   -310    156    255       C
ATOM   3710  CD  LYS B 202     -23.450 -12.088  31.766  1.00 39.30           C
ANISOU 3710  CD  LYS B 202     5550   4881   4502   -233    113    257       C
ATOM   3711  CE  LYS B 202     -23.105 -13.007  30.612  1.00 39.79           C
ANISOU 3711  CE  LYS B 202     5652   4924   4543   -243     80    260       C
ATOM   3712  NZ  LYS B 202     -21.892 -12.567  29.870  1.00 39.60           N
ANISOU 3712  NZ  LYS B 202     5608   4937   4500   -186     18    257       N
ATOM   3713  N   THR B 203     -27.359  -9.730  35.387  1.00 37.39           N
ANISOU 3713  N   THR B 203     5157   4622   4428   -348    344    250       N
ATOM   3714  CA  THR B 203     -27.712  -9.418  36.767  1.00 39.13           C
ANISOU 3714  CA  THR B 203     5409   4823   4638   -338    415    250       C
ATOM   3715  C   THR B 203     -29.160  -9.752  37.119  1.00 38.12           C
ANISOU 3715  C   THR B 203     5259   4657   4566   -409    495    253       C
ATOM   3716  O   THR B 203     -29.498  -9.782  38.312  1.00 35.36           O
ANISOU 3716  O   THR B 203     4961   4276   4198   -407    569    254       O
ATOM   3717  CB  THR B 203     -27.466  -7.926  37.025  1.00 40.52           C
ANISOU 3717  CB  THR B 203     5514   5045   4838   -303    395    243       C
ATOM   3718  OG1 THR B 203     -28.441  -7.162  36.309  1.00 41.59           O
ANISOU 3718  OG1 THR B 203     5529   5206   5069   -348    389    240       O
ATOM   3719  CG2 THR B 203     -26.107  -7.507  36.552  1.00 37.20           C
ANISOU 3719  CG2 THR B 203     5095   4665   4376   -243    314    238       C
ATOM   3720  N   PHE B 204     -30.016  -9.984  36.121  1.00 37.89           N
ANISOU 3720  N   PHE B 204     5158   4633   4607   -472    482    253       N
ATOM   3721  CA  PHE B 204     -31.451 -10.165  36.367  1.00 42.64           C
ANISOU 3721  CA  PHE B 204     5715   5208   5279   -543    553    254       C
ATOM   3722  C   PHE B 204     -31.770 -11.403  37.206  1.00 41.53           C
ANISOU 3722  C   PHE B 204     5684   5002   5094   -570    633    258       C
ATOM   3723  O   PHE B 204     -32.613 -11.345  38.114  1.00 39.31           O
ANISOU 3723  O   PHE B 204     5404   4692   4839   -598    718    259       O
ATOM   3724  CB  PHE B 204     -32.187 -10.296  35.025  1.00 44.92           C
ANISOU 3724  CB  PHE B 204     5909   5514   5642   -605    507    252       C
ATOM   3725  CG  PHE B 204     -32.147  -9.052  34.164  1.00 43.71           C
ANISOU 3725  CG  PHE B 204     5640   5422   5547   -589    437    249       C
ATOM   3726  CD1 PHE B 204     -31.541  -7.881  34.617  1.00 45.31           C
ANISOU 3726  CD1 PHE B 204     5821   5657   5738   -527    425    246       C
ATOM   3727  CD2 PHE B 204     -32.695  -9.069  32.895  1.00 42.36           C
ANISOU 3727  CD2 PHE B 204     5388   5270   5437   -636    382    248       C
ATOM   3728  CE1 PHE B 204     -31.519  -6.739  33.827  1.00 47.91           C
ANISOU 3728  CE1 PHE B 204     6049   6037   6118   -514    366    243       C
ATOM   3729  CE2 PHE B 204     -32.674  -7.938  32.098  1.00 48.52           C
ANISOU 3729  CE2 PHE B 204     6068   6101   6265   -619    319    246       C
ATOM   3730  CZ  PHE B 204     -32.084  -6.772  32.557  1.00 48.18           C
ANISOU 3730  CZ  PHE B 204     6005   6089   6212   -558    313    244       C
ATOM   3731  N   GLU B 205     -31.083 -12.518  36.947  1.00 47.15           N
ANISOU 3731  N   GLU B 205     6494   5685   5734   -560    611    262       N
ATOM   3732  CA  GLU B 205     -31.317 -13.797  37.618  1.00 51.62           C
ANISOU 3732  CA  GLU B 205     7178   6184   6251   -586    682    267       C
ATOM   3733  C   GLU B 205     -30.492 -13.963  38.885  1.00 46.45           C
ANISOU 3733  C   GLU B 205     6646   5502   5503   -519    718    271       C
ATOM   3734  O   GLU B 205     -30.589 -14.997  39.558  1.00 44.68           O
ANISOU 3734  O   GLU B 205     6534   5218   5225   -530    779    277       O
ATOM   3735  CB  GLU B 205     -31.008 -14.952  36.665  1.00 57.09           C
ANISOU 3735  CB  GLU B 205     7923   6856   6912   -608    641    268       C
ATOM   3736  N   LEU B 206     -29.694 -12.971  39.200  1.00 41.69           N
ANISOU 3736  N   LEU B 206     6024   4940   4878   -452    678    269       N
ATOM   3737  CA  LEU B 206     -28.670 -13.091  40.198  1.00 40.15           C
ANISOU 3737  CA  LEU B 206     5940   4729   4586   -379    682    273       C
ATOM   3738  C   LEU B 206     -29.292 -13.069  41.597  1.00 37.57           C
ANISOU 3738  C   LEU B 206     5674   4357   4244   -388    781    275       C
ATOM   3739  O   LEU B 206     -30.257 -12.340  41.841  1.00 38.31           O
ANISOU 3739  O   LEU B 206     5689   4458   4410   -426    829    271       O
ATOM   3740  CB  LEU B 206     -27.703 -11.945  39.939  1.00 39.92           C
ANISOU 3740  CB  LEU B 206     5852   4763   4552   -316    602    267       C
ATOM   3741  CG  LEU B 206     -26.294 -11.844  40.422  1.00 39.58           C
ANISOU 3741  CG  LEU B 206     5882   4734   4422   -232    554    268       C
ATOM   3742  CD1 LEU B 206     -25.537 -13.001  39.764  1.00 36.32           C
ANISOU 3742  CD1 LEU B 206     5538   4306   3957   -212    512    275       C
ATOM   3743  CD2 LEU B 206     -25.789 -10.540  39.826  1.00 42.46           C
ANISOU 3743  CD2 LEU B 206     6140   5168   4827   -204    483    259       C
ATOM   3744  N   PRO B 207     -28.759 -13.836  42.540  1.00 38.93           N
ANISOU 3744  N   PRO B 207     5987   4481   4323   -350    814    282       N
ATOM   3745  CA  PRO B 207     -29.359 -13.870  43.882  1.00 42.13           C
ANISOU 3745  CA  PRO B 207     6464   4836   4707   -360    914    284       C
ATOM   3746  C   PRO B 207     -29.325 -12.513  44.571  1.00 42.74           C
ANISOU 3746  C   PRO B 207     6495   4945   4800   -329    920    278       C
ATOM   3747  O   PRO B 207     -28.435 -11.688  44.338  1.00 42.05           O
ANISOU 3747  O   PRO B 207     6367   4910   4700   -275    842    273       O
ATOM   3748  CB  PRO B 207     -28.498 -14.899  44.629  1.00 41.80           C
ANISOU 3748  CB  PRO B 207     6590   4745   4548   -308    922    293       C
ATOM   3749  CG  PRO B 207     -27.705 -15.655  43.550  1.00 35.24           C
ANISOU 3749  CG  PRO B 207     5770   3928   3691   -290    842    297       C
ATOM   3750  CD  PRO B 207     -27.522 -14.633  42.462  1.00 41.08           C
ANISOU 3750  CD  PRO B 207     6362   4743   4502   -290    761    288       C
ATOM   3751  N   GLY B 208     -30.334 -12.276  45.406  1.00 51.76           N
ANISOU 3751  N   GLY B 208     7641   6053   5975   -366   1018    277       N
ATOM   3752  CA  GLY B 208     -30.397 -11.015  46.132  1.00 51.76           C
ANISOU 3752  CA  GLY B 208     7606   6072   5987   -339   1038    271       C
ATOM   3753  C   GLY B 208     -29.122 -10.762  46.924  1.00 51.38           C
ANISOU 3753  C   GLY B 208     7658   6029   5835   -257    993    271       C
ATOM   3754  O   GLY B 208     -28.554 -11.678  47.528  1.00 51.03           O
ANISOU 3754  O   GLY B 208     7749   5942   5699   -226   1001    278       O
ATOM   3755  N   GLY B 209     -28.664  -9.507  46.916  1.00 42.05           N
ANISOU 3755  N   GLY B 209     6411   4900   4667   -221    943    263       N
ATOM   3756  CA  GLY B 209     -27.454  -9.150  47.627  1.00 42.01           C
ANISOU 3756  CA  GLY B 209     6485   4906   4570   -147    892    260       C
ATOM   3757  C   GLY B 209     -26.719  -8.016  46.939  1.00 39.64           C
ANISOU 3757  C   GLY B 209     6083   4681   4299   -115    797    250       C
ATOM   3758  O   GLY B 209     -27.209  -7.418  45.991  1.00 40.55           O
ANISOU 3758  O   GLY B 209     6070   4836   4503   -148    777    246       O
ATOM   3759  N   VAL B 210     -25.510  -7.758  47.428  1.00 37.55           N
ANISOU 3759  N   VAL B 210     5880   4434   3954    -50    735    246       N
ATOM   3760  CA  VAL B 210     -24.657  -6.672  46.956  1.00 34.88           C
ANISOU 3760  CA  VAL B 210     5463   4162   3628    -15    647    235       C
ATOM   3761  C   VAL B 210     -23.544  -7.236  46.086  1.00 34.56           C
ANISOU 3761  C   VAL B 210     5417   4156   3559     20    552    237       C
ATOM   3762  O   VAL B 210     -22.829  -8.146  46.508  1.00 38.10           O
ANISOU 3762  O   VAL B 210     5971   4580   3928     59    534    244       O
ATOM   3763  CB  VAL B 210     -24.076  -5.910  48.154  1.00 35.24           C
ANISOU 3763  CB  VAL B 210     5577   4205   3607     29    644    227       C
ATOM   3764  CG1 VAL B 210     -23.280  -4.668  47.703  1.00 33.87           C
ANISOU 3764  CG1 VAL B 210     5318   4100   3453     57    561    213       C
ATOM   3765  CG2 VAL B 210     -25.193  -5.564  49.141  1.00 36.89           C
ANISOU 3765  CG2 VAL B 210     5821   4365   3831     -3    755    227       C
ATOM   3766  N   TYR B 211     -23.323  -6.643  44.913  1.00 31.99           N
ANISOU 3766  N   TYR B 211     4973   3886   3295     13    489    231       N
ATOM   3767  CA  TYR B 211     -22.307  -7.143  43.991  1.00 34.23           C
ANISOU 3767  CA  TYR B 211     5245   4202   3560     44    405    232       C
ATOM   3768  C   TYR B 211     -21.423  -6.017  43.477  1.00 32.86           C
ANISOU 3768  C   TYR B 211     4988   4094   3403     75    325    219       C
ATOM   3769  O   TYR B 211     -21.917  -5.057  42.872  1.00 32.42           O
ANISOU 3769  O   TYR B 211     4827   4068   3421     44    322    212       O
ATOM   3770  CB  TYR B 211     -22.936  -7.857  42.797  1.00 31.24           C
ANISOU 3770  CB  TYR B 211     4813   3817   3239     -4    410    239       C
ATOM   3771  CG  TYR B 211     -23.738  -9.066  43.160  1.00 34.58           C
ANISOU 3771  CG  TYR B 211     5315   4176   3646    -39    484    251       C
ATOM   3772  CD1 TYR B 211     -25.003  -8.934  43.720  1.00 36.39           C
ANISOU 3772  CD1 TYR B 211     5540   4370   3916    -90    573    252       C
ATOM   3773  CD2 TYR B 211     -23.249 -10.348  42.921  1.00 38.31           C
ANISOU 3773  CD2 TYR B 211     5868   4621   4066    -22    469    261       C
ATOM   3774  CE1 TYR B 211     -25.758 -10.059  44.053  1.00 39.47           C
ANISOU 3774  CE1 TYR B 211     6003   4698   4294   -128    647    261       C
ATOM   3775  CE2 TYR B 211     -24.005 -11.474  43.229  1.00 37.14           C
ANISOU 3775  CE2 TYR B 211     5798   4410   3903    -59    540    271       C
ATOM   3776  CZ  TYR B 211     -25.250 -11.315  43.796  1.00 36.93           C
ANISOU 3776  CZ  TYR B 211     5764   4349   3917   -114    629    270       C
ATOM   3777  OH  TYR B 211     -25.997 -12.415  44.109  1.00 41.24           O
ANISOU 3777  OH  TYR B 211     6386   4832   4451   -155    704    279       O
ATOM   3778  N   ASN B 212     -20.120  -6.154  43.680  1.00 27.92           N
ANISOU 3778  N   ASN B 212     4407   3488   2712    134    259    217       N
ATOM   3779  CA  ASN B 212     -19.191  -5.294  42.969  1.00 37.21           C
ANISOU 3779  CA  ASN B 212     5501   4728   3909    159    179    205       C
ATOM   3780  C   ASN B 212     -19.406  -5.421  41.458  1.00 39.97           C
ANISOU 3780  C   ASN B 212     5759   5102   4327    129    153    207       C
ATOM   3781  O   ASN B 212     -19.543  -6.530  40.920  1.00 41.52           O
ANISOU 3781  O   ASN B 212     5984   5273   4518    119    160    219       O
ATOM   3782  CB  ASN B 212     -17.753  -5.635  43.376  1.00 37.18           C
ANISOU 3782  CB  ASN B 212     5560   4741   3827    228    113    205       C
ATOM   3783  CG  ASN B 212     -17.380  -5.022  44.729  1.00 39.62           C
ANISOU 3783  CG  ASN B 212     5930   5045   4078    258    114    196       C
ATOM   3784  OD1 ASN B 212     -17.961  -3.991  45.140  1.00 33.97           O
ANISOU 3784  OD1 ASN B 212     5184   4333   3391    231    147    186       O
ATOM   3785  ND2 ASN B 212     -16.426  -5.640  45.428  1.00 36.93           N
ANISOU 3785  ND2 ASN B 212     5680   4696   3655    314     78    201       N
ATOM   3786  N   TYR B 213     -19.524  -4.280  40.776  1.00 40.81           N
ANISOU 3786  N   TYR B 213     5760   5249   4495    111    130    196       N
ATOM   3787  CA  TYR B 213     -19.929  -4.283  39.367  1.00 41.33           C
ANISOU 3787  CA  TYR B 213     5740   5334   4630     75    112    198       C
ATOM   3788  C   TYR B 213     -19.112  -3.269  38.570  1.00 39.12           C
ANISOU 3788  C   TYR B 213     5378   5111   4377     94     45    186       C
ATOM   3789  O   TYR B 213     -19.415  -2.073  38.592  1.00 39.35           O
ANISOU 3789  O   TYR B 213     5344   5161   4445     80     48    176       O
ATOM   3790  CB  TYR B 213     -21.421  -4.004  39.271  1.00 41.77           C
ANISOU 3790  CB  TYR B 213     5747   5368   4754     15    174    201       C
ATOM   3791  CG  TYR B 213     -22.042  -4.389  37.967  1.00 42.91           C
ANISOU 3791  CG  TYR B 213     5829   5515   4959    -28    164    207       C
ATOM   3792  CD1 TYR B 213     -22.909  -5.466  37.897  1.00 43.96           C
ANISOU 3792  CD1 TYR B 213     5997   5606   5102    -68    210    218       C
ATOM   3793  CD2 TYR B 213     -21.827  -3.647  36.819  1.00 43.56           C
ANISOU 3793  CD2 TYR B 213     5821   5640   5090    -33    112    200       C
ATOM   3794  CE1 TYR B 213     -23.491  -5.830  36.722  1.00 47.92           C
ANISOU 3794  CE1 TYR B 213     6444   6107   5655   -112    197    222       C
ATOM   3795  CE2 TYR B 213     -22.430  -4.004  35.613  1.00 47.31           C
ANISOU 3795  CE2 TYR B 213     6245   6115   5616    -74     99    206       C
ATOM   3796  CZ  TYR B 213     -23.268  -5.105  35.579  1.00 49.51           C
ANISOU 3796  CZ  TYR B 213     6559   6351   5902   -114    140    216       C
ATOM   3797  OH  TYR B 213     -23.880  -5.471  34.402  1.00 44.85           O
ANISOU 3797  OH  TYR B 213     5922   5760   5361   -159    124    220       O
ATOM   3798  N   GLY B 214     -18.064  -3.728  37.906  1.00 37.89           N
ANISOU 3798  N   GLY B 214     5225   4975   4196    127    -12    186       N
ATOM   3799  CA  GLY B 214     -17.276  -2.843  37.073  1.00 33.19           C
ANISOU 3799  CA  GLY B 214     4554   4430   3627    141    -70    174       C
ATOM   3800  C   GLY B 214     -15.865  -3.362  36.857  1.00 32.62           C
ANISOU 3800  C   GLY B 214     4510   4378   3507    195   -126    173       C
ATOM   3801  O   GLY B 214     -15.509  -4.461  37.268  1.00 33.22           O
ANISOU 3801  O   GLY B 214     4664   4429   3531    224   -123    184       O
ATOM   3802  N   ALA B 215     -15.056  -2.505  36.248  1.00 32.53           N
ANISOU 3802  N   ALA B 215     4431   4412   3515    210   -175    161       N
ATOM   3803  CA  ALA B 215     -13.673  -2.830  35.969  1.00 29.37           C
ANISOU 3803  CA  ALA B 215     4039   4039   3083    260   -228    158       C
ATOM   3804  C   ALA B 215     -12.869  -2.992  37.265  1.00 33.81           C
ANISOU 3804  C   ALA B 215     4665   4602   3578    309   -244    156       C
ATOM   3805  O   ALA B 215     -13.226  -2.460  38.325  1.00 34.97           O
ANISOU 3805  O   ALA B 215     4837   4741   3708    303   -223    150       O
ATOM   3806  CB  ALA B 215     -13.054  -1.738  35.106  1.00 29.90           C
ANISOU 3806  CB  ALA B 215     4017   4153   3191    259   -269    143       C
ATOM   3807  N   SER B 216     -11.768  -3.738  37.165  1.00 29.91           N
ANISOU 3807  N   SER B 216     4200   4118   3045    361   -283    160       N
ATOM   3808  CA  SER B 216     -10.782  -3.881  38.235  1.00 34.53           C
ANISOU 3808  CA  SER B 216     4837   4715   3569    416   -317    158       C
ATOM   3809  C   SER B 216      -9.611  -2.927  38.007  1.00 35.80           C
ANISOU 3809  C   SER B 216     4925   4933   3743    440   -376    139       C
ATOM   3810  O   SER B 216      -9.425  -2.376  36.910  1.00 34.30           O
ANISOU 3810  O   SER B 216     4656   4771   3604    422   -390    131       O
ATOM   3811  CB  SER B 216     -10.234  -5.320  38.322  1.00 39.86           C
ANISOU 3811  CB  SER B 216     5589   5366   4192    466   -325    175       C
ATOM   3812  OG  SER B 216      -9.491  -5.677  37.151  1.00 36.99           O
ANISOU 3812  OG  SER B 216     5183   5023   3850    486   -355    178       O
ATOM   3813  N   ASN B 217      -8.835  -2.711  39.072  1.00 34.27           N
ANISOU 3813  N   ASN B 217     4763   4757   3502    478   -411    131       N
ATOM   3814  CA  ASN B 217      -7.660  -1.857  38.976  1.00 38.44           C
ANISOU 3814  CA  ASN B 217     5225   5340   4039    500   -470    112       C
ATOM   3815  C   ASN B 217      -6.752  -2.069  40.178  1.00 37.21           C
ANISOU 3815  C   ASN B 217     5125   5196   3819    553   -515    110       C
ATOM   3816  O   ASN B 217      -7.219  -2.042  41.324  1.00 35.56           O
ANISOU 3816  O   ASN B 217     4985   4960   3565    551   -497    111       O
ATOM   3817  CB  ASN B 217      -8.057  -0.380  38.869  1.00 39.11           C
ANISOU 3817  CB  ASN B 217     5244   5447   4169    451   -462     92       C
ATOM   3818  CG  ASN B 217      -6.974   0.470  38.216  1.00 40.36           C
ANISOU 3818  CG  ASN B 217     5314   5660   4360    458   -511     73       C
ATOM   3819  OD1 ASN B 217      -5.904  -0.030  37.838  1.00 39.16           O
ANISOU 3819  OD1 ASN B 217     5145   5533   4202    500   -552     74       O
ATOM   3820  ND2 ASN B 217      -7.248   1.765  38.080  1.00 39.21           N
ANISOU 3820  ND2 ASN B 217     5114   5532   4251    417   -505     55       N
ATOM   3821  N   THR B 218      -5.463  -2.281  39.909  1.00 37.91           N
ANISOU 3821  N   THR B 218     5181   5323   3901    602   -573    107       N
ATOM   3822  CA  THR B 218      -4.460  -2.427  40.958  1.00 44.43           C
ANISOU 3822  CA  THR B 218     6042   6168   4670    656   -630    103       C
ATOM   3823  C   THR B 218      -3.490  -1.261  41.000  1.00 40.93           C
ANISOU 3823  C   THR B 218     5519   5785   4249    655   -687     77       C
ATOM   3824  O   THR B 218      -2.608  -1.243  41.858  1.00 43.04           O
ANISOU 3824  O   THR B 218     5805   6075   4474    695   -744     70       O
ATOM   3825  CB  THR B 218      -3.676  -3.729  40.791  1.00 41.88           C
ANISOU 3825  CB  THR B 218     5754   5841   4317    724   -655    122       C
ATOM   3826  OG1 THR B 218      -3.064  -3.743  39.494  1.00 43.53           O
ANISOU 3826  OG1 THR B 218     5879   6081   4580    730   -667    120       O
ATOM   3827  CG2 THR B 218      -4.608  -4.916  40.948  1.00 35.02           C
ANISOU 3827  CG2 THR B 218     4983   4908   3414    726   -600    148       C
ATOM   3828  N   SER B 219      -3.667  -0.261  40.144  1.00 41.79           N
ANISOU 3828  N   SER B 219     5542   5916   4421    607   -673     61       N
ATOM   3829  CA  SER B 219      -2.781   0.887  40.099  1.00 41.02           C
ANISOU 3829  CA  SER B 219     5365   5871   4348    597   -721     34       C
ATOM   3830  C   SER B 219      -3.511   2.134  40.577  1.00 42.66           C
ANISOU 3830  C   SER B 219     5570   6074   4564    541   -697     16       C
ATOM   3831  O   SER B 219      -4.743   2.227  40.489  1.00 41.14           O
ANISOU 3831  O   SER B 219     5404   5842   4384    502   -637     24       O
ATOM   3832  CB  SER B 219      -2.293   1.135  38.664  1.00 40.35           C
ANISOU 3832  CB  SER B 219     5185   5817   4329    587   -722     28       C
ATOM   3833  OG  SER B 219      -1.747  -0.029  38.088  1.00 43.31           O
ANISOU 3833  OG  SER B 219     5564   6189   4701    637   -731     47       O
ATOM   3834  N   ASN B 220      -2.718   3.121  41.016  1.00 41.48           N
ANISOU 3834  N   ASN B 220     5382   5965   4413    535   -745     -9       N
ATOM   3835  CA  ASN B 220      -3.271   4.364  41.516  1.00 42.98           C
ANISOU 3835  CA  ASN B 220     5574   6151   4608    484   -726    -29       C
ATOM   3836  C   ASN B 220      -3.735   5.203  40.341  1.00 43.24           C
ANISOU 3836  C   ASN B 220     5529   6190   4711    435   -688    -37       C
ATOM   3837  O   ASN B 220      -3.416   4.912  39.188  1.00 41.98           O
ANISOU 3837  O   ASN B 220     5312   6045   4594    441   -688    -32       O
ATOM   3838  CB  ASN B 220      -2.259   5.136  42.382  1.00 49.20           C
ANISOU 3838  CB  ASN B 220     6351   6976   5365    490   -791    -54       C
ATOM   3839  CG  ASN B 220      -0.925   5.458  41.654  1.00 47.99           C
ANISOU 3839  CG  ASN B 220     6099   6883   5252    502   -848    -71       C
ATOM   3840  OD1 ASN B 220      -0.904   6.009  40.545  1.00 45.56           O
ANISOU 3840  OD1 ASN B 220     5715   6591   5006    472   -827    -79       O
ATOM   3841  ND2 ASN B 220       0.182   5.191  42.333  1.00 45.72           N
ANISOU 3841  ND2 ASN B 220     5815   6628   4929    544   -919    -78       N
ATOM   3842  N   SER B 221      -4.509   6.251  40.640  1.00 44.47           N
ANISOU 3842  N   SER B 221     5690   6331   4877    389   -654    -49       N
ATOM   3843  CA  SER B 221      -5.089   7.061  39.573  1.00 43.88           C
ANISOU 3843  CA  SER B 221     5551   6255   4865    344   -614    -54       C
ATOM   3844  C   SER B 221      -4.002   7.657  38.681  1.00 45.26           C
ANISOU 3844  C   SER B 221     5639   6478   5081    340   -653    -73       C
ATOM   3845  O   SER B 221      -4.116   7.645  37.445  1.00 41.95           O
ANISOU 3845  O   SER B 221     5167   6061   4711    329   -634    -67       O
ATOM   3846  CB  SER B 221      -5.942   8.187  40.169  1.00 44.34           C
ANISOU 3846  CB  SER B 221     5632   6293   4924    302   -577    -66       C
ATOM   3847  OG  SER B 221      -7.108   7.727  40.805  1.00 42.10           O
ANISOU 3847  OG  SER B 221     5418   5961   4617    298   -525    -48       O
ATOM   3848  N   TYR B 222      -2.946   8.194  39.294  1.00 37.43           N
ANISOU 3848  N   TYR B 222     4631   5522   4069    347   -706    -95       N
ATOM   3849  CA  TYR B 222      -1.885   8.833  38.522  1.00 45.02           C
ANISOU 3849  CA  TYR B 222     5506   6529   5071    338   -739   -116       C
ATOM   3850  C   TYR B 222      -1.244   7.852  37.535  1.00 44.53           C
ANISOU 3850  C   TYR B 222     5402   6482   5034    375   -752   -102       C
ATOM   3851  O   TYR B 222      -1.136   8.142  36.338  1.00 43.57           O
ANISOU 3851  O   TYR B 222     5221   6370   4963    358   -733   -104       O
ATOM   3852  CB  TYR B 222      -0.844   9.430  39.474  1.00 49.40           C
ANISOU 3852  CB  TYR B 222     6054   7119   5595    341   -800   -142       C
ATOM   3853  CG  TYR B 222       0.384   9.942  38.775  1.00 49.44           C
ANISOU 3853  CG  TYR B 222     5968   7175   5642    335   -839   -164       C
ATOM   3854  CD1 TYR B 222       0.315  11.057  37.953  1.00 47.39           C
ANISOU 3854  CD1 TYR B 222     5653   6923   5432    287   -811   -182       C
ATOM   3855  CD2 TYR B 222       1.606   9.291  38.913  1.00 50.62           C
ANISOU 3855  CD2 TYR B 222     6087   7364   5783    380   -899   -166       C
ATOM   3856  CE1 TYR B 222       1.424  11.525  37.307  1.00 50.74           C
ANISOU 3856  CE1 TYR B 222     5995   7389   5895    278   -839   -202       C
ATOM   3857  CE2 TYR B 222       2.730   9.750  38.264  1.00 54.34           C
ANISOU 3857  CE2 TYR B 222     6468   7881   6298    373   -929   -186       C
ATOM   3858  CZ  TYR B 222       2.634  10.876  37.462  1.00 55.39           C
ANISOU 3858  CZ  TYR B 222     6549   8018   6479    319   -896   -205       C
ATOM   3859  OH  TYR B 222       3.745  11.358  36.807  1.00 59.48           O
ANISOU 3859  OH  TYR B 222     6979   8579   7042    309   -918   -226       O
ATOM   3860  N   GLU B 223      -0.805   6.683  38.019  1.00 41.36           N
ANISOU 3860  N   GLU B 223     5038   6082   4594    428   -782    -86       N
ATOM   3861  CA  GLU B 223      -0.252   5.698  37.101  1.00 43.78           C
ANISOU 3861  CA  GLU B 223     5315   6398   4922    467   -787    -70       C
ATOM   3862  C   GLU B 223      -1.316   5.228  36.108  1.00 44.64           C
ANISOU 3862  C   GLU B 223     5438   6466   5057    451   -727    -49       C
ATOM   3863  O   GLU B 223      -0.999   4.906  34.954  1.00 44.75           O
ANISOU 3863  O   GLU B 223     5409   6487   5108    458   -717    -43       O
ATOM   3864  CB  GLU B 223       0.325   4.501  37.860  1.00 46.73           C
ANISOU 3864  CB  GLU B 223     5736   6774   5245    531   -827    -55       C
ATOM   3865  CG  GLU B 223       1.701   4.694  38.516  1.00 48.61           C
ANISOU 3865  CG  GLU B 223     5939   7062   5467    563   -902    -72       C
ATOM   3866  CD  GLU B 223       2.851   4.784  37.531  1.00 52.40           C
ANISOU 3866  CD  GLU B 223     6323   7587   6001    577   -924    -82       C
ATOM   3867  OE1 GLU B 223       3.716   5.659  37.739  1.00 51.10           O
ANISOU 3867  OE1 GLU B 223     6097   7466   5852    561   -966   -109       O
ATOM   3868  OE2 GLU B 223       2.906   3.983  36.569  1.00 54.00           O
ANISOU 3868  OE2 GLU B 223     6512   7780   6227    602   -899    -64       O
ATOM   3869  N   THR B 224      -2.577   5.129  36.547  1.00 43.29           N
ANISOU 3869  N   THR B 224     5328   6252   4866    429   -686    -36       N
ATOM   3870  CA  THR B 224      -3.629   4.672  35.635  1.00 43.55           C
ANISOU 3870  CA  THR B 224     5372   6249   4927    410   -634    -17       C
ATOM   3871  C   THR B 224      -3.870   5.690  34.533  1.00 42.40           C
ANISOU 3871  C   THR B 224     5161   6111   4839    365   -612    -29       C
ATOM   3872  O   THR B 224      -3.941   5.331  33.355  1.00 40.60           O
ANISOU 3872  O   THR B 224     4908   5876   4642    363   -595    -19       O
ATOM   3873  CB  THR B 224      -4.941   4.388  36.380  1.00 41.70           C
ANISOU 3873  CB  THR B 224     5210   5968   4665    394   -593     -2       C
ATOM   3874  OG1 THR B 224      -4.817   3.193  37.169  1.00 45.54           O
ANISOU 3874  OG1 THR B 224     5769   6437   5098    437   -603     15       O
ATOM   3875  CG2 THR B 224      -6.071   4.183  35.394  1.00 35.87           C
ANISOU 3875  CG2 THR B 224     4466   5197   3965    362   -542     13       C
ATOM   3876  N   TYR B 225      -3.992   6.970  34.907  1.00 43.25           N
ANISOU 3876  N   TYR B 225     5247   6229   4956    330   -610    -50       N
ATOM   3877  CA  TYR B 225      -4.343   8.011  33.948  1.00 44.04           C
ANISOU 3877  CA  TYR B 225     5296   6331   5107    287   -585    -60       C
ATOM   3878  C   TYR B 225      -3.194   8.314  32.982  1.00 42.51           C
ANISOU 3878  C   TYR B 225     5034   6172   4946    291   -608    -74       C
ATOM   3879  O   TYR B 225      -3.423   8.501  31.783  1.00 39.41           O
ANISOU 3879  O   TYR B 225     4610   5772   4592    273   -585    -71       O
ATOM   3880  CB  TYR B 225      -4.814   9.258  34.721  1.00 42.83           C
ANISOU 3880  CB  TYR B 225     5150   6174   4949    252   -573    -77       C
ATOM   3881  CG  TYR B 225      -6.091   9.007  35.546  1.00 41.57           C
ANISOU 3881  CG  TYR B 225     5055   5974   4765    244   -536    -62       C
ATOM   3882  CD1 TYR B 225      -6.986   7.998  35.191  1.00 38.56           C
ANISOU 3882  CD1 TYR B 225     4702   5560   4388    250   -505    -36       C
ATOM   3883  CD2 TYR B 225      -6.385   9.760  36.679  1.00 40.93           C
ANISOU 3883  CD2 TYR B 225     5008   5885   4657    229   -529    -75       C
ATOM   3884  CE1 TYR B 225      -8.138   7.734  35.950  1.00 36.79           C
ANISOU 3884  CE1 TYR B 225     4535   5299   4146    241   -466    -22       C
ATOM   3885  CE2 TYR B 225      -7.542   9.525  37.433  1.00 40.54           C
ANISOU 3885  CE2 TYR B 225     5018   5796   4588    222   -487    -60       C
ATOM   3886  CZ  TYR B 225      -8.415   8.506  37.062  1.00 38.33           C
ANISOU 3886  CZ  TYR B 225     4761   5487   4318    228   -455    -34       C
ATOM   3887  OH  TYR B 225      -9.565   8.249  37.791  1.00 32.62           O
ANISOU 3887  OH  TYR B 225     4092   4724   3580    220   -409    -21       O
ATOM   3888  N   LYS B 226      -1.942   8.268  33.448  1.00 45.88           N
ANISOU 3888  N   LYS B 226     5438   6637   5358    318   -654    -88       N
ATOM   3889  CA  LYS B 226      -0.829   8.439  32.508  1.00 47.21           C
ANISOU 3889  CA  LYS B 226     5539   6838   5562    324   -670   -100       C
ATOM   3890  C   LYS B 226      -0.819   7.325  31.450  1.00 43.65           C
ANISOU 3890  C   LYS B 226     5090   6371   5125    352   -653    -78       C
ATOM   3891  O   LYS B 226      -0.528   7.579  30.268  1.00 41.08           O
ANISOU 3891  O   LYS B 226     4722   6050   4839    340   -636    -81       O
ATOM   3892  CB  LYS B 226       0.511   8.516  33.260  1.00 46.52           C
ANISOU 3892  CB  LYS B 226     5421   6795   5458    350   -725   -119       C
ATOM   3893  CG  LYS B 226       0.931   7.244  33.988  1.00 48.43           C
ANISOU 3893  CG  LYS B 226     5701   7041   5658    409   -759   -102       C
ATOM   3894  CD  LYS B 226       2.455   7.180  34.276  1.00 51.64           C
ANISOU 3894  CD  LYS B 226     6054   7500   6067    442   -817   -118       C
ATOM   3895  CE  LYS B 226       2.993   8.505  34.863  1.00 53.18           C
ANISOU 3895  CE  LYS B 226     6209   7729   6269    404   -847   -152       C
ATOM   3896  NZ  LYS B 226       4.475   8.498  35.080  1.00 47.86           N
ANISOU 3896  NZ  LYS B 226     5471   7109   5606    431   -906   -169       N
ATOM   3897  N   GLU B 227      -1.202   6.101  31.838  1.00 45.89           N
ANISOU 3897  N   GLU B 227     5430   6632   5374    387   -652    -54       N
ATOM   3898  CA  GLU B 227      -1.367   5.029  30.861  1.00 45.98           C
ANISOU 3898  CA  GLU B 227     5457   6619   5394    408   -630    -31       C
ATOM   3899  C   GLU B 227      -2.452   5.358  29.842  1.00 46.54           C
ANISOU 3899  C   GLU B 227     5530   6658   5495    364   -587    -24       C
ATOM   3900  O   GLU B 227      -2.265   5.160  28.635  1.00 48.41           O
ANISOU 3900  O   GLU B 227     5747   6888   5759    363   -572    -20       O
ATOM   3901  CB  GLU B 227      -1.676   3.721  31.572  1.00 47.10           C
ANISOU 3901  CB  GLU B 227     5670   6737   5490    447   -634     -8       C
ATOM   3902  CG  GLU B 227      -0.436   2.970  31.999  1.00 50.82           C
ANISOU 3902  CG  GLU B 227     6137   7235   5937    507   -674     -7       C
ATOM   3903  CD  GLU B 227       0.051   2.015  30.927  1.00 62.59           C
ANISOU 3903  CD  GLU B 227     7621   8718   7443    541   -662      9       C
ATOM   3904  OE1 GLU B 227      -0.810   1.310  30.352  1.00 60.02           O
ANISOU 3904  OE1 GLU B 227     7341   8350   7112    533   -627     28       O
ATOM   3905  OE2 GLU B 227       1.282   1.960  30.669  1.00 65.00           O
ANISOU 3905  OE2 GLU B 227     7876   9059   7764    575   -687      1       O
ATOM   3906  N   ILE B 228      -3.599   5.863  30.305  1.00 45.76           N
ANISOU 3906  N   ILE B 228     5457   6537   5393    329   -567    -23       N
ATOM   3907  CA  ILE B 228      -4.673   6.198  29.380  1.00 42.91           C
ANISOU 3907  CA  ILE B 228     5093   6147   5062    290   -532    -15       C
ATOM   3908  C   ILE B 228      -4.243   7.335  28.470  1.00 42.45           C
ANISOU 3908  C   ILE B 228     4978   6107   5045    264   -529    -33       C
ATOM   3909  O   ILE B 228      -4.520   7.319  27.266  1.00 41.77           O
ANISOU 3909  O   ILE B 228     4882   6005   4985    250   -511    -27       O
ATOM   3910  CB  ILE B 228      -5.967   6.521  30.157  1.00 42.92           C
ANISOU 3910  CB  ILE B 228     5129   6123   5056    263   -509     -9       C
ATOM   3911  CG1 ILE B 228      -6.638   5.210  30.604  1.00 45.18           C
ANISOU 3911  CG1 ILE B 228     5477   6378   5312    281   -497     14       C
ATOM   3912  CG2 ILE B 228      -6.949   7.283  29.311  1.00 35.50           C
ANISOU 3912  CG2 ILE B 228     4167   5165   4155    221   -481     -8       C
ATOM   3913  CD1 ILE B 228      -7.560   5.335  31.811  1.00 38.23           C
ANISOU 3913  CD1 ILE B 228     4638   5478   4409    268   -478     18       C
ATOM   3914  N   ALA B 229      -3.529   8.317  29.019  1.00 42.53           N
ANISOU 3914  N   ALA B 229     4953   6148   5057    256   -547    -57       N
ATOM   3915  CA  ALA B 229      -3.079   9.450  28.217  1.00 45.30           C
ANISOU 3915  CA  ALA B 229     5253   6514   5444    228   -541    -77       C
ATOM   3916  C   ALA B 229      -2.153   9.007  27.088  1.00 48.67           C
ANISOU 3916  C   ALA B 229     5650   6951   5891    246   -541    -77       C
ATOM   3917  O   ALA B 229      -2.336   9.396  25.929  1.00 49.60           O
ANISOU 3917  O   ALA B 229     5754   7055   6037    225   -519    -77       O
ATOM   3918  CB  ALA B 229      -2.390  10.473  29.117  1.00 46.40           C
ANISOU 3918  CB  ALA B 229     5366   6686   5578    216   -562   -104       C
ATOM   3919  N   LYS B 230      -1.169   8.166  27.401  1.00 42.92           N
ANISOU 3919  N   LYS B 230     4916   6245   5147    289   -566    -75       N
ATOM   3920  CA  LYS B 230      -0.265   7.704  26.356  1.00 47.59           C
ANISOU 3920  CA  LYS B 230     5480   6844   5759    310   -560    -74       C
ATOM   3921  C   LYS B 230      -1.026   6.974  25.245  1.00 46.99           C
ANISOU 3921  C   LYS B 230     5441   6726   5687    309   -531    -51       C
ATOM   3922  O   LYS B 230      -0.709   7.151  24.068  1.00 47.74           O
ANISOU 3922  O   LYS B 230     5517   6814   5806    300   -511    -53       O
ATOM   3923  CB  LYS B 230       0.849   6.848  26.961  1.00 49.53           C
ANISOU 3923  CB  LYS B 230     5714   7119   5987    363   -592    -73       C
ATOM   3924  CG  LYS B 230       0.512   5.427  27.280  1.00 48.53           C
ANISOU 3924  CG  LYS B 230     5644   6969   5825    405   -596    -46       C
ATOM   3925  CD  LYS B 230       1.681   4.795  28.014  1.00 54.18           C
ANISOU 3925  CD  LYS B 230     6344   7718   6523    459   -634    -48       C
ATOM   3926  CE  LYS B 230       2.903   4.647  27.120  1.00 51.86           C
ANISOU 3926  CE  LYS B 230     5995   7447   6263    485   -631    -54       C
ATOM   3927  NZ  LYS B 230       3.681   3.465  27.587  1.00 52.81           N
ANISOU 3927  NZ  LYS B 230     6126   7580   6361    553   -656    -40       N
ATOM   3928  N   ILE B 231      -2.071   6.203  25.589  1.00 50.85           N
ANISOU 3928  N   ILE B 231     5985   7185   6151    312   -526    -30       N
ATOM   3929  CA  ILE B 231      -2.872   5.526  24.565  1.00 47.39           C
ANISOU 3929  CA  ILE B 231     5584   6705   5715    304   -502     -9       C
ATOM   3930  C   ILE B 231      -3.487   6.550  23.636  1.00 47.48           C
ANISOU 3930  C   ILE B 231     5579   6703   5758    258   -482    -15       C
ATOM   3931  O   ILE B 231      -3.568   6.356  22.417  1.00 47.40           O
ANISOU 3931  O   ILE B 231     5578   6671   5760    251   -467     -8       O
ATOM   3932  CB  ILE B 231      -3.966   4.664  25.220  1.00 45.10           C
ANISOU 3932  CB  ILE B 231     5352   6387   5397    305   -499     12       C
ATOM   3933  CG1 ILE B 231      -3.336   3.533  26.029  1.00 48.68           C
ANISOU 3933  CG1 ILE B 231     5835   6848   5815    356   -515     21       C
ATOM   3934  CG2 ILE B 231      -4.948   4.124  24.190  1.00 42.68           C
ANISOU 3934  CG2 ILE B 231     5080   6038   5097    284   -477     30       C
ATOM   3935  CD1 ILE B 231      -4.330   2.490  26.502  1.00 47.57           C
ANISOU 3935  CD1 ILE B 231     5761   6671   5644    359   -505     43       C
ATOM   3936  N   MET B 232      -3.871   7.686  24.195  1.00 48.37           N
ANISOU 3936  N   MET B 232     5671   6827   5881    229   -484    -29       N
ATOM   3937  CA  MET B 232      -4.522   8.774  23.489  1.00 47.31           C
ANISOU 3937  CA  MET B 232     5523   6678   5773    189   -467    -35       C
ATOM   3938  C   MET B 232      -3.552   9.773  22.888  1.00 49.59           C
ANISOU 3938  C   MET B 232     5767   6987   6085    178   -462    -57       C
ATOM   3939  O   MET B 232      -3.990  10.837  22.449  1.00 53.07           O
ANISOU 3939  O   MET B 232     6198   7419   6546    145   -449    -65       O
ATOM   3940  CB  MET B 232      -5.479   9.506  24.435  1.00 51.43           C
ANISOU 3940  CB  MET B 232     6049   7198   6294    166   -465    -37       C
ATOM   3941  CG  MET B 232      -6.815   8.852  24.662  1.00 47.48           C
ANISOU 3941  CG  MET B 232     5588   6667   5786    159   -457    -15       C
ATOM   3942  SD  MET B 232      -7.666   9.894  25.856  1.00 54.19           S
ANISOU 3942  SD  MET B 232     6434   7518   6637    136   -447    -23       S
ATOM   3943  CE  MET B 232      -9.354   9.284  25.737  1.00 50.41           C
ANISOU 3943  CE  MET B 232     5986   7000   6167    120   -428      4       C
ATOM   3944  N   ASP B 233      -2.249   9.504  22.929  1.00 56.32           N
ANISOU 3944  N   ASP B 233     6593   7868   6938    203   -471    -68       N
ATOM   3945  CA  ASP B 233      -1.256  10.396  22.351  1.00 55.97           C
ANISOU 3945  CA  ASP B 233     6504   7843   6920    190   -462    -91       C
ATOM   3946  C   ASP B 233      -1.182  11.706  23.132  1.00 56.97           C
ANISOU 3946  C   ASP B 233     6601   7992   7054    161   -468   -115       C
ATOM   3947  O   ASP B 233      -0.630  12.715  22.655  1.00 55.29           O
ANISOU 3947  O   ASP B 233     6356   7787   6864    136   -455   -135       O
ATOM   3948  CB  ASP B 233      -1.516  10.584  20.844  1.00 56.81           C
ANISOU 3948  CB  ASP B 233     6624   7918   7045    173   -433    -85       C
ATOM   3949  CG  ASP B 233      -1.486   9.222  20.068  1.00 59.61           C
ANISOU 3949  CG  ASP B 233     7013   8248   7386    202   -426    -63       C
ATOM   3950  OD1 ASP B 233      -0.526   8.432  20.264  1.00 59.87           O
ANISOU 3950  OD1 ASP B 233     7033   8299   7413    239   -432    -63       O
ATOM   3951  OD2 ASP B 233      -2.414   8.911  19.278  1.00 58.31           O
ANISOU 3951  OD2 ASP B 233     6890   8046   7218    190   -416    -45       O
ATOM   3952  N   VAL B 234      -1.730  11.677  24.341  1.00 55.66           N
ANISOU 3952  N   VAL B 234     6451   7830   6865    162   -486   -112       N
ATOM   3953  CA  VAL B 234      -1.675  12.815  25.254  1.00 53.24           C
ANISOU 3953  CA  VAL B 234     6129   7542   6558    137   -494   -134       C
ATOM   3954  C   VAL B 234      -0.306  12.839  25.920  1.00 57.60           C
ANISOU 3954  C   VAL B 234     6640   8138   7107    152   -523   -155       C
ATOM   3955  O   VAL B 234       0.141  11.798  26.436  1.00 58.40           O
ANISOU 3955  O   VAL B 234     6747   8255   7189    191   -548   -146       O
ATOM   3956  CB  VAL B 234      -2.777  12.714  26.298  1.00 50.74           C
ANISOU 3956  CB  VAL B 234     5852   7210   6217    135   -498   -123       C
ATOM   3957  CG1 VAL B 234      -2.459  13.576  27.492  1.00 50.72           C
ANISOU 3957  CG1 VAL B 234     5840   7230   6200    121   -514   -146       C
ATOM   3958  CG2 VAL B 234      -4.106  13.107  25.703  1.00 49.87           C
ANISOU 3958  CG2 VAL B 234     5765   7064   6121    111   -469   -109       C
ATOM   3959  N   PRO B 235       0.378  13.984  25.915  1.00 53.33           N
ANISOU 3959  N   PRO B 235     6060   7618   6585    122   -522   -183       N
ATOM   3960  CA  PRO B 235       1.705  14.058  26.520  1.00 56.46           C
ANISOU 3960  CA  PRO B 235     6410   8059   6983    131   -554   -206       C
ATOM   3961  C   PRO B 235       1.703  13.544  27.956  1.00 62.30           C
ANISOU 3961  C   PRO B 235     7170   8816   7684    155   -595   -203       C
ATOM   3962  O   PRO B 235       0.717  13.655  28.692  1.00 60.56           O
ANISOU 3962  O   PRO B 235     6996   8575   7438    148   -594   -195       O
ATOM   3963  CB  PRO B 235       2.035  15.553  26.452  1.00 57.49           C
ANISOU 3963  CB  PRO B 235     6511   8199   7134     81   -541   -236       C
ATOM   3964  CG  PRO B 235       1.206  16.088  25.295  1.00 49.69           C
ANISOU 3964  CG  PRO B 235     5546   7171   6165     56   -496   -228       C
ATOM   3965  CD  PRO B 235       0.128  15.099  24.982  1.00 52.48           C
ANISOU 3965  CD  PRO B 235     5946   7492   6504     82   -487   -194       C
ATOM   3966  N   GLU B 236       2.811  12.912  28.327  1.00 75.09           N
ANISOU 3966  N   GLU B 236     8756  10471   9301    189   -631   -209       N
ATOM   3967  CA  GLU B 236       2.933  12.369  29.671  1.00 72.06           C
ANISOU 3967  CA  GLU B 236     8395  10105   8878    218   -676   -206       C
ATOM   3968  C   GLU B 236       2.874  13.487  30.713  1.00 70.59           C
ANISOU 3968  C   GLU B 236     8215   9931   8675    180   -695   -231       C
ATOM   3969  O   GLU B 236       2.177  13.360  31.730  1.00 70.63           O
ANISOU 3969  O   GLU B 236     8274   9922   8641    184   -706   -224       O
ATOM   3970  CB  GLU B 236       4.243  11.568  29.784  1.00 69.77           C
ANISOU 3970  CB  GLU B 236     8061   9855   8594    263   -714   -208       C
ATOM   3971  CG  GLU B 236       4.384  10.316  28.852  1.00 72.01           C
ANISOU 3971  CG  GLU B 236     8347  10126   8888    309   -695   -182       C
ATOM   3972  CD  GLU B 236       4.361  10.625  27.336  1.00 79.49           C
ANISOU 3972  CD  GLU B 236     9273  11054   9877    287   -644   -182       C
ATOM   3973  OE1 GLU B 236       5.041  11.581  26.889  1.00 79.16           O
ANISOU 3973  OE1 GLU B 236     9175  11031   9869    254   -634   -206       O
ATOM   3974  OE2 GLU B 236       3.649   9.908  26.589  1.00 77.01           O
ANISOU 3974  OE2 GLU B 236     8999  10702   9558    300   -614   -157       O
ATOM   3975  N   ASN B 237       3.547  14.616  30.444  1.00 62.44           N
ANISOU 3975  N   ASN B 237     7133   8919   7672    139   -693   -261       N
ATOM   3976  CA  ASN B 237       3.656  15.683  31.434  1.00 58.42           C
ANISOU 3976  CA  ASN B 237     6629   8423   7145    102   -714   -288       C
ATOM   3977  C   ASN B 237       2.305  16.275  31.812  1.00 59.46           C
ANISOU 3977  C   ASN B 237     6826   8513   7255     76   -682   -281       C
ATOM   3978  O   ASN B 237       2.212  16.928  32.859  1.00 61.01           O
ANISOU 3978  O   ASN B 237     7048   8712   7422     54   -700   -298       O
ATOM   3979  CB  ASN B 237       4.626  16.790  30.967  1.00 59.23           C
ANISOU 3979  CB  ASN B 237     6666   8551   7286     58   -711   -322       C
ATOM   3980  CG  ASN B 237       4.102  17.616  29.766  1.00 62.12           C
ANISOU 3980  CG  ASN B 237     7032   8885   7685     20   -650   -324       C
ATOM   3981  OD1 ASN B 237       3.920  17.098  28.660  1.00 58.54           O
ANISOU 3981  OD1 ASN B 237     6574   8415   7255     37   -618   -305       O
ATOM   3982  ND2 ASN B 237       3.889  18.922  29.990  1.00 58.98           N
ANISOU 3982  ND2 ASN B 237     6645   8477   7287    -32   -634   -347       N
ATOM   3983  N   LEU B 238       1.261  16.080  30.992  1.00 60.40           N
ANISOU 3983  N   LEU B 238     6971   8593   7386     77   -636   -258       N
ATOM   3984  CA  LEU B 238      -0.048  16.683  31.255  1.00 56.30           C
ANISOU 3984  CA  LEU B 238     6504   8034   6854     53   -602   -250       C
ATOM   3985  C   LEU B 238      -0.850  15.952  32.326  1.00 54.38           C
ANISOU 3985  C   LEU B 238     6319   7773   6568     79   -611   -231       C
ATOM   3986  O   LEU B 238      -1.940  16.415  32.673  1.00 52.54           O
ANISOU 3986  O   LEU B 238     6129   7509   6326     62   -580   -224       O
ATOM   3987  CB  LEU B 238      -0.881  16.720  29.982  1.00 52.00           C
ANISOU 3987  CB  LEU B 238     5962   7456   6340     46   -555   -231       C
ATOM   3988  CG  LEU B 238      -0.481  17.732  28.925  1.00 53.20           C
ANISOU 3988  CG  LEU B 238     6077   7608   6529     12   -530   -249       C
ATOM   3989  CD1 LEU B 238      -1.138  17.388  27.587  1.00 52.05           C
ANISOU 3989  CD1 LEU B 238     5936   7432   6408     19   -496   -226       C
ATOM   3990  CD2 LEU B 238      -0.897  19.101  29.401  1.00 57.09           C
ANISOU 3990  CD2 LEU B 238     6589   8087   7017    -29   -512   -268       C
ATOM   3991  N   VAL B 239      -0.340  14.847  32.866  1.00 52.59           N
ANISOU 3991  N   VAL B 239     6099   7565   6316    120   -648   -221       N
ATOM   3992  CA  VAL B 239      -0.975  14.142  33.972  1.00 52.54           C
ANISOU 3992  CA  VAL B 239     6156   7542   6264    144   -657   -205       C
ATOM   3993  C   VAL B 239      -0.066  14.329  35.175  1.00 52.75           C
ANISOU 3993  C   VAL B 239     6188   7600   6255    149   -710   -227       C
ATOM   3994  O   VAL B 239       0.975  13.672  35.295  1.00 52.71           O
ANISOU 3994  O   VAL B 239     6154   7629   6244    181   -756   -229       O
ATOM   3995  CB  VAL B 239      -1.215  12.662  33.675  1.00 50.44           C
ANISOU 3995  CB  VAL B 239     5909   7264   5990    189   -656   -174       C
ATOM   3996  CG1 VAL B 239      -2.027  12.054  34.818  1.00 49.01           C
ANISOU 3996  CG1 VAL B 239     5802   7058   5762    207   -654   -158       C
ATOM   3997  CG2 VAL B 239      -1.943  12.492  32.337  1.00 47.70           C
ANISOU 3997  CG2 VAL B 239     5551   6891   5682    181   -612   -156       C
ATOM   3998  N   GLU B 240      -0.474  15.218  36.074  1.00 50.90           N
ANISOU 3998  N   GLU B 240     5992   7354   5995    120   -705   -242       N
ATOM   3999  CA  GLU B 240       0.298  15.577  37.250  1.00 51.15           C
ANISOU 3999  CA  GLU B 240     6037   7411   5989    115   -757   -266       C
ATOM   4000  C   GLU B 240      -0.144  14.778  38.469  1.00 51.32           C
ANISOU 4000  C   GLU B 240     6135   7413   5950    147   -773   -250       C
ATOM   4001  O   GLU B 240      -1.305  14.375  38.584  1.00 48.61           O
ANISOU 4001  O   GLU B 240     5844   7029   5595    155   -729   -226       O
ATOM   4002  CB  GLU B 240       0.182  17.078  37.524  1.00 55.64           C
ANISOU 4002  CB  GLU B 240     6610   7972   6559     60   -741   -294       C
ATOM   4003  CG  GLU B 240       1.093  17.893  36.598  1.00 59.60           C
ANISOU 4003  CG  GLU B 240     7033   8503   7108     27   -745   -319       C
ATOM   4004  CD  GLU B 240       1.281  19.330  37.027  1.00 57.22           C
ANISOU 4004  CD  GLU B 240     6739   8202   6802    -27   -743   -353       C
ATOM   4005  OE1 GLU B 240       0.410  19.865  37.743  1.00 57.02           O
ANISOU 4005  OE1 GLU B 240     6778   8141   6744    -43   -717   -353       O
ATOM   4006  OE2 GLU B 240       2.322  19.916  36.653  1.00 63.04           O
ANISOU 4006  OE2 GLU B 240     7415   8971   7564    -54   -765   -380       O
ATOM   4007  N   ASN B 241       0.826  14.523  39.357  1.00 52.83           N
ANISOU 4007  N   ASN B 241     6331   7636   6105    166   -838   -263       N
ATOM   4008  CA  ASN B 241       0.642  13.807  40.615  1.00 50.98           C
ANISOU 4008  CA  ASN B 241     6175   7389   5807    199   -865   -252       C
ATOM   4009  C   ASN B 241       0.692  14.837  41.727  1.00 51.32           C
ANISOU 4009  C   ASN B 241     6263   7428   5809    164   -884   -279       C
ATOM   4010  O   ASN B 241       1.752  15.419  41.982  1.00 52.87           O
ANISOU 4010  O   ASN B 241     6421   7664   6004    146   -939   -308       O
ATOM   4011  CB  ASN B 241       1.756  12.763  40.780  1.00 51.72           C
ANISOU 4011  CB  ASN B 241     6244   7521   5887    252   -932   -246       C
ATOM   4012  CG  ASN B 241       1.777  12.090  42.170  1.00 55.49           C
ANISOU 4012  CG  ASN B 241     6806   7989   6290    288   -974   -239       C
ATOM   4013  OD1 ASN B 241       0.772  12.045  42.880  1.00 56.30           O
ANISOU 4013  OD1 ASN B 241     6993   8046   6351    283   -939   -228       O
ATOM   4014  ND2 ASN B 241       2.958  11.611  42.572  1.00 52.78           N
ANISOU 4014  ND2 ASN B 241     6438   7688   5929    324  -1051   -245       N
ATOM   4015  N   ASP B 242      -0.446  15.066  42.388  1.00 54.32           N
ANISOU 4015  N   ASP B 242     6723   7760   6156    152   -837   -270       N
ATOM   4016  CA  ASP B 242      -0.527  15.977  43.530  1.00 56.90           C
ANISOU 4016  CA  ASP B 242     7111   8073   6434    121   -846   -293       C
ATOM   4017  C   ASP B 242      -0.537  15.144  44.814  1.00 59.29           C
ANISOU 4017  C   ASP B 242     7502   8362   6663    158   -880   -283       C
ATOM   4018  O   ASP B 242      -1.496  14.410  45.078  1.00 60.05           O
ANISOU 4018  O   ASP B 242     7661   8418   6739    183   -836   -255       O
ATOM   4019  CB  ASP B 242      -1.749  16.889  43.429  1.00 52.99           C
ANISOU 4019  CB  ASP B 242     6649   7531   5952     83   -766   -292       C
ATOM   4020  CG  ASP B 242      -1.739  17.974  44.482  1.00 60.26           C
ANISOU 4020  CG  ASP B 242     7629   8437   6828     46   -771   -320       C
ATOM   4021  OD1 ASP B 242      -0.851  17.915  45.358  1.00 59.17           O
ANISOU 4021  OD1 ASP B 242     7516   8323   6643     51   -840   -338       O
ATOM   4022  OD2 ASP B 242      -2.612  18.877  44.449  1.00 63.55           O
ANISOU 4022  OD2 ASP B 242     8073   8818   7255     14   -708   -323       O
ATOM   4023  N   THR B 243       0.525  15.258  45.613  1.00 59.28           N
ANISOU 4023  N   THR B 243     7509   8394   6622    163   -959   -304       N
ATOM   4024  CA  THR B 243       0.631  14.439  46.814  1.00 59.81           C
ANISOU 4024  CA  THR B 243     7662   8449   6614    203  -1002   -294       C
ATOM   4025  C   THR B 243      -0.212  14.957  47.978  1.00 65.45           C
ANISOU 4025  C   THR B 243     8489   9112   7265    182   -968   -299       C
ATOM   4026  O   THR B 243      -0.506  14.186  48.896  1.00 68.05           O
ANISOU 4026  O   THR B 243     8909   9413   7532    216   -974   -282       O
ATOM   4027  CB  THR B 243       2.105  14.298  47.220  1.00 61.34           C
ANISOU 4027  CB  THR B 243     7818   8699   6788    221  -1107   -314       C
ATOM   4028  OG1 THR B 243       2.838  13.718  46.129  1.00 59.37           O
ANISOU 4028  OG1 THR B 243     7465   8493   6599    247  -1129   -306       O
ATOM   4029  CG2 THR B 243       2.266  13.371  48.434  1.00 67.76           C
ANISOU 4029  CG2 THR B 243     8724   9501   7520    271  -1159   -301       C
ATOM   4030  N   ASN B 244      -0.635  16.220  47.971  1.00 68.38           N
ANISOU 4030  N   ASN B 244     8867   9466   7649    128   -926   -319       N
ATOM   4031  CA  ASN B 244      -1.395  16.688  49.125  1.00 70.39           C
ANISOU 4031  CA  ASN B 244     9236   9669   7841    111   -891   -324       C
ATOM   4032  C   ASN B 244      -2.851  16.241  49.084  1.00 70.56           C
ANISOU 4032  C   ASN B 244     9310   9632   7866    124   -795   -292       C
ATOM   4033  O   ASN B 244      -3.533  16.306  50.115  1.00 72.16           O
ANISOU 4033  O   ASN B 244     9618   9787   8012    123   -761   -289       O
ATOM   4034  CB  ASN B 244      -1.309  18.207  49.241  1.00 71.01           C
ANISOU 4034  CB  ASN B 244     9313   9745   7925     50   -880   -358       C
ATOM   4035  CG  ASN B 244      -2.255  18.920  48.301  1.00 79.64           C
ANISOU 4035  CG  ASN B 244    10366  10812   9081     21   -790   -352       C
ATOM   4036  OD1 ASN B 244      -2.582  18.410  47.226  1.00 73.50           O
ANISOU 4036  OD1 ASN B 244     9522  10042   8363     38   -759   -330       O
ATOM   4037  ND2 ASN B 244      -2.697  20.118  48.695  1.00 84.83           N
ANISOU 4037  ND2 ASN B 244    11069  11438   9725    -23   -749   -372       N
ATOM   4038  N   ARG B 245      -3.337  15.790  47.925  1.00 63.57           N
ANISOU 4038  N   ARG B 245     8356   8749   7047    134   -751   -270       N
ATOM   4039  CA  ARG B 245      -4.706  15.297  47.823  1.00 61.50           C
ANISOU 4039  CA  ARG B 245     8134   8437   6797    145   -665   -240       C
ATOM   4040  C   ARG B 245      -4.819  13.925  48.459  1.00 56.57           C
ANISOU 4040  C   ARG B 245     7577   7795   6123    193   -677   -215       C
ATOM   4041  O   ARG B 245      -4.015  13.030  48.177  1.00 57.54           O
ANISOU 4041  O   ARG B 245     7666   7951   6245    229   -735   -207       O
ATOM   4042  CB  ARG B 245      -5.180  15.277  46.375  1.00 61.14           C
ANISOU 4042  CB  ARG B 245     7996   8399   6835    137   -621   -226       C
ATOM   4043  CG  ARG B 245      -5.375  16.708  45.859  1.00 63.15           C
ANISOU 4043  CG  ARG B 245     8209   8654   7133     89   -589   -247       C
ATOM   4044  CD  ARG B 245      -5.933  16.766  44.467  1.00 60.90           C
ANISOU 4044  CD  ARG B 245     7843   8370   6925     82   -544   -232       C
ATOM   4045  NE  ARG B 245      -7.161  16.000  44.508  1.00 67.49           N
ANISOU 4045  NE  ARG B 245     8714   9163   7765    100   -482   -200       N
ATOM   4046  CZ  ARG B 245      -8.002  15.844  43.500  1.00 73.13           C
ANISOU 4046  CZ  ARG B 245     9382   9866   8539     97   -433   -181       C
ATOM   4047  NH1 ARG B 245      -7.766  16.445  42.331  1.00 72.43           N
ANISOU 4047  NH1 ARG B 245     9212   9800   8507     79   -436   -188       N
ATOM   4048  NH2 ARG B 245      -9.056  15.047  43.662  1.00 68.02           N
ANISOU 4048  NH2 ARG B 245     8770   9183   7893    113   -383   -153       N
ATOM   4049  N   PHE B 246      -5.812  13.776  49.338  1.00 59.41           N
ANISOU 4049  N   PHE B 246     8035   8098   6440    195   -618   -203       N
ATOM   4050  CA  PHE B 246      -5.994  12.559  50.130  1.00 62.38           C
ANISOU 4050  CA  PHE B 246     8499   8447   6757    237   -620   -181       C
ATOM   4051  C   PHE B 246      -4.710  12.229  50.887  1.00 64.89           C
ANISOU 4051  C   PHE B 246     8849   8797   7010    265   -722   -194       C
ATOM   4052  O   PHE B 246      -4.286  11.074  50.968  1.00 58.22           O
ANISOU 4052  O   PHE B 246     8018   7961   6141    311   -762   -177       O
ATOM   4053  CB  PHE B 246      -6.435  11.377  49.259  1.00 56.44           C
ANISOU 4053  CB  PHE B 246     7706   7691   6046    264   -592   -149       C
ATOM   4054  CG  PHE B 246      -7.718  11.609  48.521  1.00 52.02           C
ANISOU 4054  CG  PHE B 246     7113   7101   5551    238   -499   -135       C
ATOM   4055  CD1 PHE B 246      -8.911  11.734  49.213  1.00 48.66           C
ANISOU 4055  CD1 PHE B 246     6763   6618   5107    225   -418   -125       C
ATOM   4056  CD2 PHE B 246      -7.728  11.717  47.133  1.00 50.58           C
ANISOU 4056  CD2 PHE B 246     6823   6947   5447    226   -494   -131       C
ATOM   4057  CE1 PHE B 246     -10.105  11.938  48.534  1.00 50.40           C
ANISOU 4057  CE1 PHE B 246     6944   6813   5391    203   -336   -111       C
ATOM   4058  CE2 PHE B 246      -8.909  11.919  46.448  1.00 50.80           C
ANISOU 4058  CE2 PHE B 246     6820   6950   5534    204   -417   -117       C
ATOM   4059  CZ  PHE B 246     -10.107  12.029  47.143  1.00 49.71           C
ANISOU 4059  CZ  PHE B 246     6749   6757   5382    192   -339   -106       C
ATOM   4060  N   LYS B 247      -4.101  13.270  51.470  1.00 78.96           N
ANISOU 4060  N   LYS B 247    10645  10594   8763    237   -766   -225       N
ATOM   4061  CA  LYS B 247      -2.834  13.102  52.174  1.00 78.09           C
ANISOU 4061  CA  LYS B 247    10556  10520   8595    258   -872   -242       C
ATOM   4062  C   LYS B 247      -3.041  12.406  53.506  1.00 80.43           C
ANISOU 4062  C   LYS B 247    10989  10773   8796    291   -880   -230       C
ATOM   4063  O   LYS B 247      -2.211  11.588  53.920  1.00 82.78           O
ANISOU 4063  O   LYS B 247    11309  11093   9050    335   -959   -225       O
ATOM   4064  CB  LYS B 247      -2.155  14.456  52.388  1.00 75.96           C
ANISOU 4064  CB  LYS B 247    10261  10276   8322    211   -915   -281       C
ATOM   4065  N   ALA B 248      -4.147  12.706  54.183  1.00 70.26           N
ANISOU 4065  N   ALA B 248     9798   9422   7476    272   -798   -225       N
ATOM   4066  CA  ALA B 248      -4.404  12.081  55.475  1.00 75.18           C
ANISOU 4066  CA  ALA B 248    10564   9995   8004    301   -795   -214       C
ATOM   4067  C   ALA B 248      -4.540  10.564  55.341  1.00 72.65           C
ANISOU 4067  C   ALA B 248    10264   9666   7675    356   -792   -180       C
ATOM   4068  O   ALA B 248      -3.859   9.808  56.047  1.00 70.17           O
ANISOU 4068  O   ALA B 248    10013   9355   7292    399   -861   -175       O
ATOM   4069  CB  ALA B 248      -5.654  12.693  56.107  1.00 80.16           C
ANISOU 4069  CB  ALA B 248    11287  10557   8613    269   -690   -213       C
ATOM   4070  N   GLN B 249      -5.404  10.099  54.435  1.00 64.61           N
ANISOU 4070  N   GLN B 249     9195   8633   6723    354   -714   -157       N
ATOM   4071  CA  GLN B 249      -5.551   8.668  54.188  1.00 57.05           C
ANISOU 4071  CA  GLN B 249     8250   7664   5762    401   -705   -125       C
ATOM   4072  C   GLN B 249      -6.006   8.425  52.754  1.00 51.32           C
ANISOU 4072  C   GLN B 249     7410   6955   5134    391   -659   -110       C
ATOM   4073  O   GLN B 249      -6.942   9.072  52.272  1.00 45.39           O
ANISOU 4073  O   GLN B 249     6624   6185   4437    350   -582   -111       O
ATOM   4074  CB  GLN B 249      -6.538   8.003  55.146  1.00 55.35           C
ANISOU 4074  CB  GLN B 249     8172   7374   5485    414   -633   -104       C
ATOM   4075  CG  GLN B 249      -6.601   6.504  54.917  1.00 53.07           C
ANISOU 4075  CG  GLN B 249     7904   7072   5186    462   -629    -73       C
ATOM   4076  CD  GLN B 249      -7.362   5.775  55.999  1.00 58.48           C
ANISOU 4076  CD  GLN B 249     8738   7685   5796    480   -570    -54       C
ATOM   4077  OE1 GLN B 249      -8.583   5.559  55.881  1.00 54.85           O
ANISOU 4077  OE1 GLN B 249     8301   7176   5363    458   -465    -38       O
ATOM   4078  NE2 GLN B 249      -6.649   5.374  57.061  1.00 57.21           N
ANISOU 4078  NE2 GLN B 249     8681   7515   5540    519   -637    -56       N
ATOM   4079  N   ALA B 250      -5.370   7.452  52.105  1.00 49.04           N
ANISOU 4079  N   ALA B 250     7071   6699   4863    430   -706    -96       N
ATOM   4080  CA  ALA B 250      -5.639   7.179  50.705  1.00 48.39           C
ANISOU 4080  CA  ALA B 250     6883   6637   4868    422   -675    -84       C
ATOM   4081  C   ALA B 250      -7.106   6.815  50.513  1.00 45.84           C
ANISOU 4081  C   ALA B 250     6591   6256   4569    403   -568    -61       C
ATOM   4082  O   ALA B 250      -7.696   6.109  51.332  1.00 44.62           O
ANISOU 4082  O   ALA B 250     6541   6052   4361    420   -528    -45       O
ATOM   4083  CB  ALA B 250      -4.733   6.043  50.218  1.00 43.89           C
ANISOU 4083  CB  ALA B 250     6280   6100   4298    475   -738    -69       C
ATOM   4084  N   ARG B 251      -7.711   7.360  49.462  1.00 39.60           N
ANISOU 4084  N   ARG B 251     5711   5474   3860    366   -520    -62       N
ATOM   4085  CA  ARG B 251      -9.038   6.925  49.043  1.00 40.89           C
ANISOU 4085  CA  ARG B 251     5879   5594   4063    349   -428    -40       C
ATOM   4086  C   ARG B 251      -8.844   5.678  48.182  1.00 42.48           C
ANISOU 4086  C   ARG B 251     6046   5807   4288    379   -443    -18       C
ATOM   4087  O   ARG B 251      -8.451   5.769  47.013  1.00 44.25           O
ANISOU 4087  O   ARG B 251     6172   6071   4571    374   -468    -20       O
ATOM   4088  CB  ARG B 251      -9.770   8.032  48.285  1.00 41.31           C
ANISOU 4088  CB  ARG B 251     5854   5652   4192    301   -377    -49       C
ATOM   4089  CG  ARG B 251     -10.912   7.539  47.356  1.00 36.50           C
ANISOU 4089  CG  ARG B 251     5201   5020   3648    284   -306    -26       C
ATOM   4090  CD  ARG B 251     -11.848   8.657  46.939  1.00 40.98           C
ANISOU 4090  CD  ARG B 251     5717   5577   4276    241   -246    -32       C
ATOM   4091  NE  ARG B 251     -12.193   9.548  48.052  1.00 41.22           N
ANISOU 4091  NE  ARG B 251     5815   5578   4269    225   -211    -46       N
ATOM   4092  CZ  ARG B 251     -13.068  10.556  47.977  1.00 45.89           C
ANISOU 4092  CZ  ARG B 251     6385   6151   4901    193   -149    -51       C
ATOM   4093  NH1 ARG B 251     -13.705  10.807  46.834  1.00 45.53           N
ANISOU 4093  NH1 ARG B 251     6249   6114   4936    173   -119    -43       N
ATOM   4094  NH2 ARG B 251     -13.311  11.328  49.045  1.00 43.30           N
ANISOU 4094  NH2 ARG B 251     6129   5793   4531    182   -117    -64       N
ATOM   4095  N   ASN B 252      -9.070   4.496  48.764  1.00 38.46           N
ANISOU 4095  N   ASN B 252     5625   5261   3728    410   -427      3       N
ATOM   4096  CA  ASN B 252      -8.969   3.233  48.033  1.00 39.05           C
ANISOU 4096  CA  ASN B 252     5685   5335   3816    438   -432     25       C
ATOM   4097  C   ASN B 252     -10.380   2.741  47.736  1.00 34.27           C
ANISOU 4097  C   ASN B 252     5096   4680   3244    409   -338     45       C
ATOM   4098  O   ASN B 252     -11.064   2.227  48.632  1.00 31.35           O
ANISOU 4098  O   ASN B 252     4824   4257   2828    411   -287     57       O
ATOM   4099  CB  ASN B 252      -8.184   2.189  48.840  1.00 37.75           C
ANISOU 4099  CB  ASN B 252     5609   5163   3571    496   -483     36       C
ATOM   4100  CG  ASN B 252      -8.253   0.763  48.234  1.00 37.38           C
ANISOU 4100  CG  ASN B 252     5574   5101   3529    526   -472     62       C
ATOM   4101  OD1 ASN B 252      -8.445   0.572  47.018  1.00 36.01           O
ANISOU 4101  OD1 ASN B 252     5319   4941   3421    511   -457     68       O
ATOM   4102  ND2 ASN B 252      -8.061  -0.241  49.089  1.00 36.14           N
ANISOU 4102  ND2 ASN B 252     5524   4911   3296    570   -481     77       N
ATOM   4103  N   ILE B 253     -10.809   2.852  46.477  1.00 33.44           N
ANISOU 4103  N   ILE B 253     4898   4591   3218    381   -316     49       N
ATOM   4104  CA  ILE B 253     -12.103   2.275  46.132  1.00 34.44           C
ANISOU 4104  CA  ILE B 253     5033   4673   3379    354   -236     68       C
ATOM   4105  C   ILE B 253     -11.998   1.199  45.049  1.00 36.75           C
ANISOU 4105  C   ILE B 253     5291   4972   3701    366   -247     85       C
ATOM   4106  O   ILE B 253     -13.023   0.767  44.508  1.00 35.35           O
ANISOU 4106  O   ILE B 253     5101   4767   3565    336   -189     99       O
ATOM   4107  CB  ILE B 253     -13.127   3.365  45.744  1.00 31.06           C
ANISOU 4107  CB  ILE B 253     4542   4240   3018    302   -179     61       C
ATOM   4108  CG1 ILE B 253     -12.777   4.040  44.422  1.00 31.38           C
ANISOU 4108  CG1 ILE B 253     4464   4329   3128    286   -215     51       C
ATOM   4109  CG2 ILE B 253     -13.217   4.424  46.854  1.00 34.94           C
ANISOU 4109  CG2 ILE B 253     5079   4721   3477    292   -164     44       C
ATOM   4110  CD1 ILE B 253     -13.602   5.298  44.173  1.00 29.89           C
ANISOU 4110  CD1 ILE B 253     4220   4139   2996    244   -171     42       C
ATOM   4111  N   SER B 254     -10.793   0.691  44.772  1.00 34.55           N
ANISOU 4111  N   SER B 254     5003   4726   3398    410   -317     85       N
ATOM   4112  CA  SER B 254     -10.669  -0.409  43.822  1.00 33.49           C
ANISOU 4112  CA  SER B 254     4853   4591   3283    425   -323    103       C
ATOM   4113  C   SER B 254     -11.325  -1.631  44.423  1.00 32.05           C
ANISOU 4113  C   SER B 254     4773   4350   3055    435   -274    124       C
ATOM   4114  O   SER B 254     -11.058  -1.986  45.580  1.00 37.50           O
ANISOU 4114  O   SER B 254     5557   5018   3674    467   -281    127       O
ATOM   4115  CB  SER B 254      -9.203  -0.681  43.496  1.00 31.16           C
ANISOU 4115  CB  SER B 254     4530   4341   2970    476   -404     98       C
ATOM   4116  OG  SER B 254      -8.628  -1.460  44.515  1.00 35.10           O
ANISOU 4116  OG  SER B 254     5122   4824   3391    527   -432    106       O
ATOM   4117  N   MET B 255     -12.216  -2.249  43.671  1.00 28.21           N
ANISOU 4117  N   MET B 255     4273   3837   2609    406   -224    138       N
ATOM   4118  CA  MET B 255     -13.009  -3.326  44.254  1.00 36.99           C
ANISOU 4118  CA  MET B 255     5481   4887   3684    402   -165    157       C
ATOM   4119  C   MET B 255     -12.652  -4.687  43.653  1.00 33.31           C
ANISOU 4119  C   MET B 255     5046   4409   3203    431   -178    175       C
ATOM   4120  O   MET B 255     -12.128  -4.807  42.537  1.00 30.82           O
ANISOU 4120  O   MET B 255     4663   4125   2923    439   -215    175       O
ATOM   4121  CB  MET B 255     -14.521  -2.957  44.189  1.00 31.90           C
ANISOU 4121  CB  MET B 255     4818   4211   3093    339    -82    159       C
ATOM   4122  CG  MET B 255     -15.146  -2.778  42.858  1.00 34.15           C
ANISOU 4122  CG  MET B 255     5005   4510   3461    295    -68    160       C
ATOM   4123  SD  MET B 255     -16.781  -1.930  42.916  1.00 32.40           S
ANISOU 4123  SD  MET B 255     4738   4264   3307    228     15    158       S
ATOM   4124  CE  MET B 255     -17.112  -1.966  41.163  1.00 33.05           C
ANISOU 4124  CE  MET B 255     4712   4372   3474    194     -2    161       C
ATOM   4125  N   ASN B 256     -12.929  -5.720  44.425  1.00 37.06           N
ANISOU 4125  N   ASN B 256     5631   4832   3619    448   -143    191       N
ATOM   4126  CA  ASN B 256     -12.713  -7.089  43.981  1.00 38.42           C
ANISOU 4126  CA  ASN B 256     5851   4978   3767    475   -143    209       C
ATOM   4127  C   ASN B 256     -13.976  -7.608  43.316  1.00 36.87           C
ANISOU 4127  C   ASN B 256     5647   4744   3619    415    -73    219       C
ATOM   4128  O   ASN B 256     -15.035  -7.625  43.942  1.00 39.01           O
ANISOU 4128  O   ASN B 256     5960   4972   3890    377     -4    222       O
ATOM   4129  CB  ASN B 256     -12.322  -7.984  45.161  1.00 38.53           C
ANISOU 4129  CB  ASN B 256     5998   4954   3688    527   -143    222       C
ATOM   4130  CG  ASN B 256     -12.191  -9.470  44.763  1.00 41.48           C
ANISOU 4130  CG  ASN B 256     6437   5291   4033    554   -133    243       C
ATOM   4131  OD1 ASN B 256     -13.183 -10.154  44.487  1.00 39.15           O
ANISOU 4131  OD1 ASN B 256     6173   4948   3753    512    -67    253       O
ATOM   4132  ND2 ASN B 256     -10.959  -9.965  44.740  1.00 50.39           N
ANISOU 4132  ND2 ASN B 256     7586   6441   5119    625   -198    249       N
ATOM   4133  N   ILE B 257     -13.868  -8.028  42.056  1.00 37.23           N
ANISOU 4133  N   ILE B 257     5639   4802   3706    406    -88    223       N
ATOM   4134  CA  ILE B 257     -15.047  -8.453  41.314  1.00 39.15           C
ANISOU 4134  CA  ILE B 257     5863   5014   3999    345    -32    231       C
ATOM   4135  C   ILE B 257     -15.113  -9.974  41.183  1.00 39.32           C
ANISOU 4135  C   ILE B 257     5974   4986   3981    357     -8    249       C
ATOM   4136  O   ILE B 257     -15.757 -10.486  40.266  1.00 37.30           O
ANISOU 4136  O   ILE B 257     5697   4711   3764    314     17    255       O
ATOM   4137  CB  ILE B 257     -15.113  -7.800  39.924  1.00 36.35           C
ANISOU 4137  CB  ILE B 257     5388   4701   3723    312    -59    222       C
ATOM   4138  CG1 ILE B 257     -13.861  -8.132  39.117  1.00 30.77           C
ANISOU 4138  CG1 ILE B 257     4660   4026   3004    362   -123    223       C
ATOM   4139  CG2 ILE B 257     -15.365  -6.312  40.032  1.00 37.08           C
ANISOU 4139  CG2 ILE B 257     5397   4830   3861    287    -65    205       C
ATOM   4140  CD1 ILE B 257     -13.956  -7.788  37.636  1.00 34.27           C
ANISOU 4140  CD1 ILE B 257     5009   4497   3515    330   -142    218       C
ATOM   4141  N   GLN B 258     -14.497 -10.715  42.100  1.00 35.32           N
ANISOU 4141  N   GLN B 258     5574   4454   3395    413    -14    259       N
ATOM   4142  CA  GLN B 258     -14.509 -12.165  41.931  1.00 39.70           C
ANISOU 4142  CA  GLN B 258     6218   4958   3909    428      9    277       C
ATOM   4143  C   GLN B 258     -15.905 -12.730  42.192  1.00 40.87           C
ANISOU 4143  C   GLN B 258     6419   5044   4066    363     97    284       C
ATOM   4144  O   GLN B 258     -16.291 -13.753  41.593  1.00 38.39           O
ANISOU 4144  O   GLN B 258     6140   4692   3754    341    126    295       O
ATOM   4145  CB  GLN B 258     -13.445 -12.822  42.810  1.00 38.90           C
ANISOU 4145  CB  GLN B 258     6217   4845   3718    511    -24    288       C
ATOM   4146  CG  GLN B 258     -12.068 -12.796  42.144  1.00 44.13           C
ANISOU 4146  CG  GLN B 258     6831   5559   4379    574   -105    287       C
ATOM   4147  CD  GLN B 258     -12.166 -12.908  40.607  1.00 45.51           C
ANISOU 4147  CD  GLN B 258     6923   5751   4618    543   -110    285       C
ATOM   4148  OE1 GLN B 258     -12.619 -13.932  40.086  1.00 44.68           O
ANISOU 4148  OE1 GLN B 258     6866   5600   4508    524    -73    298       O
ATOM   4149  NE2 GLN B 258     -11.758 -11.844  39.884  1.00 39.39           N
ANISOU 4149  NE2 GLN B 258     6030   5036   3899    534   -155    270       N
ATOM   4150  N   LYS B 259     -16.666 -12.078  43.086  1.00 32.43           N
ANISOU 4150  N   LYS B 259     5356   3962   3004    331    142    278       N
ATOM   4151  CA  LYS B 259     -18.046 -12.483  43.335  1.00 35.56           C
ANISOU 4151  CA  LYS B 259     5787   4304   3422    265    231    283       C
ATOM   4152  C   LYS B 259     -18.842 -12.479  42.043  1.00 38.73           C
ANISOU 4152  C   LYS B 259     6095   4714   3907    198    244    280       C
ATOM   4153  O   LYS B 259     -19.634 -13.397  41.778  1.00 41.92           O
ANISOU 4153  O   LYS B 259     6538   5071   4320    153    296    288       O
ATOM   4154  CB  LYS B 259     -18.705 -11.543  44.341  1.00 37.09           C
ANISOU 4154  CB  LYS B 259     5975   4493   3625    241    275    274       C
ATOM   4155  CG  LYS B 259     -20.101 -11.947  44.755  1.00 35.39           C
ANISOU 4155  CG  LYS B 259     5799   4218   3430    176    375    278       C
ATOM   4156  CD  LYS B 259     -20.514 -11.150  45.955  1.00 35.88           C
ANISOU 4156  CD  LYS B 259     5888   4268   3478    172    419    272       C
ATOM   4157  CE  LYS B 259     -21.645 -11.800  46.681  1.00 39.46           C
ANISOU 4157  CE  LYS B 259     6422   4650   3922    127    523    280       C
ATOM   4158  NZ  LYS B 259     -22.870 -11.748  45.884  1.00 44.54           N
ANISOU 4158  NZ  LYS B 259     6974   5289   4660     47    573    278       N
ATOM   4159  N   ILE B 260     -18.640 -11.452  41.221  1.00 34.40           N
ANISOU 4159  N   ILE B 260     5426   4224   3419    189    195    268       N
ATOM   4160  CA  ILE B 260     -19.412 -11.361  39.998  1.00 39.13           C
ANISOU 4160  CA  ILE B 260     5937   4833   4097    127    201    265       C
ATOM   4161  C   ILE B 260     -18.830 -12.262  38.914  1.00 42.02           C
ANISOU 4161  C   ILE B 260     6315   5198   4454    141    163    272       C
ATOM   4162  O   ILE B 260     -19.574 -12.713  38.030  1.00 40.79           O
ANISOU 4162  O   ILE B 260     6133   5024   4339     86    182    275       O
ATOM   4163  CB  ILE B 260     -19.506  -9.884  39.578  1.00 33.54           C
ANISOU 4163  CB  ILE B 260     5105   4183   3457    110    170    250       C
ATOM   4164  CG1 ILE B 260     -20.823  -9.645  38.884  1.00 39.13           C
ANISOU 4164  CG1 ILE B 260     5736   4885   4247     33    207    248       C
ATOM   4165  CG2 ILE B 260     -18.368  -9.444  38.659  1.00 40.22           C
ANISOU 4165  CG2 ILE B 260     5888   5083   4310    150     89    244       C
ATOM   4166  CD1 ILE B 260     -21.959  -9.699  39.848  1.00 40.46           C
ANISOU 4166  CD1 ILE B 260     5938   5011   4425     -7    290    251       C
ATOM   4167  N   GLU B 261     -17.532 -12.583  38.984  1.00 38.90           N
ANISOU 4167  N   GLU B 261     5962   4818   4001    215    112    276       N
ATOM   4168  CA  GLU B 261     -16.965 -13.524  38.021  1.00 45.93           C
ANISOU 4168  CA  GLU B 261     6877   5700   4877    234     85    285       C
ATOM   4169  C   GLU B 261     -17.488 -14.943  38.246  1.00 42.09           C
ANISOU 4169  C   GLU B 261     6503   5142   4348    217    141    299       C
ATOM   4170  O   GLU B 261     -17.619 -15.712  37.290  1.00 40.66           O
ANISOU 4170  O   GLU B 261     6333   4940   4176    195    143    305       O
ATOM   4171  CB  GLU B 261     -15.433 -13.475  38.059  1.00 40.79           C
ANISOU 4171  CB  GLU B 261     6234   5084   4180    321     20    286       C
ATOM   4172  CG  GLU B 261     -14.845 -12.061  37.784  1.00 37.44           C
ANISOU 4172  CG  GLU B 261     5696   4730   3798    334    -36    269       C
ATOM   4173  CD  GLU B 261     -14.696 -11.743  36.305  1.00 40.89           C
ANISOU 4173  CD  GLU B 261     6044   5200   4293    313    -69    263       C
ATOM   4174  OE1 GLU B 261     -14.415 -10.573  35.976  1.00 40.16           O
ANISOU 4174  OE1 GLU B 261     5857   5159   4243    310   -104    249       O
ATOM   4175  OE2 GLU B 261     -14.831 -12.659  35.453  1.00 47.95           O
ANISOU 4175  OE2 GLU B 261     6965   6065   5187    299    -60    272       O
ATOM   4176  N   LYS B 262     -17.794 -15.308  39.495  1.00 47.48           N
ANISOU 4176  N   LYS B 262     7276   5783   4981    225    190    305       N
ATOM   4177  CA  LYS B 262     -18.304 -16.649  39.746  1.00 47.26           C
ANISOU 4177  CA  LYS B 262     7363   5683   4911    206    249    319       C
ATOM   4178  C   LYS B 262     -19.614 -16.896  39.030  1.00 49.16           C
ANISOU 4178  C   LYS B 262     7566   5898   5216    112    297    316       C
ATOM   4179  O   LYS B 262     -19.913 -18.042  38.677  1.00 53.98           O
ANISOU 4179  O   LYS B 262     8247   6457   5805     88    328    324       O
ATOM   4180  CB  LYS B 262     -18.509 -16.887  41.238  1.00 48.40           C
ANISOU 4180  CB  LYS B 262     7611   5784   4995    225    299    325       C
ATOM   4181  CG  LYS B 262     -17.277 -17.361  41.969  1.00 52.87           C
ANISOU 4181  CG  LYS B 262     8273   6344   5470    321    263    336       C
ATOM   4182  CD  LYS B 262     -17.683 -17.987  43.251  1.00 51.40           C
ANISOU 4182  CD  LYS B 262     8217   6093   5217    326    327    345       C
ATOM   4183  CE  LYS B 262     -17.008 -17.336  44.432  1.00 57.03           C
ANISOU 4183  CE  LYS B 262     8963   6827   5880    388    297    343       C
ATOM   4184  NZ  LYS B 262     -17.556 -17.889  45.711  1.00 54.93           N
ANISOU 4184  NZ  LYS B 262     8831   6491   5550    385    370    352       N
ATOM   4185  N   HIS B 263     -20.415 -15.855  38.826  1.00 43.63           N
ANISOU 4185  N   HIS B 263     6757   5229   4591     57    304    304       N
ATOM   4186  CA  HIS B 263     -21.667 -15.997  38.109  1.00 41.05           C
ANISOU 4186  CA  HIS B 263     6378   4884   4333    -33    341    300       C
ATOM   4187  C   HIS B 263     -21.508 -15.779  36.626  1.00 42.82           C
ANISOU 4187  C   HIS B 263     6516   5146   4608    -52    283    295       C
ATOM   4188  O   HIS B 263     -22.513 -15.670  35.919  1.00 43.56           O
ANISOU 4188  O   HIS B 263     6544   5238   4768   -126    297    290       O
ATOM   4189  CB  HIS B 263     -22.703 -15.052  38.683  1.00 42.26           C
ANISOU 4189  CB  HIS B 263     6464   5048   4545    -82    384    292       C
ATOM   4190  CG  HIS B 263     -22.942 -15.274  40.137  1.00 45.48           C
ANISOU 4190  CG  HIS B 263     6966   5414   4903    -69    449    296       C
ATOM   4191  ND1 HIS B 263     -23.845 -16.206  40.604  1.00 48.13           N
ANISOU 4191  ND1 HIS B 263     7378   5682   5226   -117    530    303       N
ATOM   4192  CD2 HIS B 263     -22.359 -14.729  41.232  1.00 44.61           C
ANISOU 4192  CD2 HIS B 263     6893   5312   4745    -12    446    296       C
ATOM   4193  CE1 HIS B 263     -23.828 -16.204  41.927  1.00 47.81           C
ANISOU 4193  CE1 HIS B 263     7420   5612   5134    -90    577    306       C
ATOM   4194  NE2 HIS B 263     -22.937 -15.314  42.333  1.00 42.03           N
ANISOU 4194  NE2 HIS B 263     6667   4924   4377    -26    525    302       N
ATOM   4195  N   GLY B 264     -20.276 -15.671  36.145  1.00 42.48           N
ANISOU 4195  N   GLY B 264     6467   5137   4537     13    219    296       N
ATOM   4196  CA  GLY B 264     -20.033 -15.514  34.731  1.00 40.50           C
ANISOU 4196  CA  GLY B 264     6148   4916   4326     -0    168    291       C
ATOM   4197  C   GLY B 264     -20.027 -14.089  34.239  1.00 41.68           C
ANISOU 4197  C   GLY B 264     6169   5129   4540     -8    124    278       C
ATOM   4198  O   GLY B 264     -20.006 -13.864  33.025  1.00 36.78           O
ANISOU 4198  O   GLY B 264     5486   4530   3958    -29     86    274       O
ATOM   4199  N   ILE B 265     -20.023 -13.113  35.130  1.00 42.78           N
ANISOU 4199  N   ILE B 265     6273   5295   4687      9    129    272       N
ATOM   4200  CA  ILE B 265     -19.965 -11.723  34.718  1.00 41.23           C
ANISOU 4200  CA  ILE B 265     5961   5157   4547      6     90    260       C
ATOM   4201  C   ILE B 265     -18.512 -11.292  34.804  1.00 38.71           C
ANISOU 4201  C   ILE B 265     5640   4878   4191     83     35    257       C
ATOM   4202  O   ILE B 265     -17.903 -11.317  35.884  1.00 39.95           O
ANISOU 4202  O   ILE B 265     5852   5034   4295    134     38    258       O
ATOM   4203  CB  ILE B 265     -20.883 -10.843  35.581  1.00 37.85           C
ANISOU 4203  CB  ILE B 265     5491   4733   4157    -26    132    254       C
ATOM   4204  CG1 ILE B 265     -22.296 -11.438  35.585  1.00 39.38           C
ANISOU 4204  CG1 ILE B 265     5694   4883   4387   -101    195    259       C
ATOM   4205  CG2 ILE B 265     -20.894  -9.401  35.079  1.00 38.89           C
ANISOU 4205  CG2 ILE B 265     5506   4921   4350    -32     95    242       C
ATOM   4206  CD1 ILE B 265     -23.314 -10.708  36.480  1.00 39.23           C
ANISOU 4206  CD1 ILE B 265     5640   4859   4408   -135    251    255       C
ATOM   4207  N   HIS B 266     -17.942 -10.946  33.662  1.00 33.13           N
ANISOU 4207  N   HIS B 266     4872   4206   3509     93    -17    252       N
ATOM   4208  CA  HIS B 266     -16.544 -10.555  33.592  1.00 39.37           C
ANISOU 4208  CA  HIS B 266     5650   5037   4272    161    -69    247       C
ATOM   4209  C   HIS B 266     -16.420  -9.091  33.195  1.00 37.26           C
ANISOU 4209  C   HIS B 266     5274   4825   4059    154   -103    233       C
ATOM   4210  O   HIS B 266     -17.191  -8.584  32.371  1.00 35.47           O
ANISOU 4210  O   HIS B 266     4980   4607   3892    102   -104    228       O
ATOM   4211  CB  HIS B 266     -15.775 -11.448  32.601  1.00 42.52           C
ANISOU 4211  CB  HIS B 266     6082   5426   4648    189    -96    255       C
ATOM   4212  CG  HIS B 266     -14.492 -10.859  32.094  1.00 39.32           C
ANISOU 4212  CG  HIS B 266     5628   5070   4243    243   -150    248       C
ATOM   4213  ND1 HIS B 266     -13.284 -11.053  32.732  1.00 37.92           N
ANISOU 4213  ND1 HIS B 266     5486   4907   4015    318   -174    250       N
ATOM   4214  CD2 HIS B 266     -14.223 -10.120  30.985  1.00 38.55           C
ANISOU 4214  CD2 HIS B 266     5450   5008   4191    232   -185    238       C
ATOM   4215  CE1 HIS B 266     -12.330 -10.433  32.053  1.00 40.02           C
ANISOU 4215  CE1 HIS B 266     5689   5218   4300    348   -219    242       C
ATOM   4216  NE2 HIS B 266     -12.872  -9.861  30.989  1.00 38.27           N
ANISOU 4216  NE2 HIS B 266     5400   5008   4135    297   -223    234       N
ATOM   4217  N   PHE B 267     -15.443  -8.425  33.789  1.00 34.48           N
ANISOU 4217  N   PHE B 267     4908   4509   3684    206   -134    225       N
ATOM   4218  CA  PHE B 267     -15.051  -7.092  33.385  1.00 37.28           C
ANISOU 4218  CA  PHE B 267     5170   4916   4080    208   -171    210       C
ATOM   4219  C   PHE B 267     -13.555  -7.089  33.137  1.00 33.00           C
ANISOU 4219  C   PHE B 267     4624   4406   3509    271   -220    206       C
ATOM   4220  O   PHE B 267     -12.796  -7.690  33.894  1.00 34.33           O
ANISOU 4220  O   PHE B 267     4855   4568   3622    323   -228    212       O
ATOM   4221  CB  PHE B 267     -15.355  -6.042  34.462  1.00 36.76           C
ANISOU 4221  CB  PHE B 267     5081   4866   4021    203   -157    200       C
ATOM   4222  CG  PHE B 267     -16.782  -5.623  34.525  1.00 36.35           C
ANISOU 4222  CG  PHE B 267     4997   4797   4019    140   -112    200       C
ATOM   4223  CD1 PHE B 267     -17.707  -6.361  35.243  1.00 35.04           C
ANISOU 4223  CD1 PHE B 267     4891   4583   3838    115    -56    210       C
ATOM   4224  CD2 PHE B 267     -17.201  -4.466  33.900  1.00 36.06           C
ANISOU 4224  CD2 PHE B 267     4868   4789   4043    109   -123    191       C
ATOM   4225  CE1 PHE B 267     -19.041  -5.955  35.309  1.00 37.48           C
ANISOU 4225  CE1 PHE B 267     5162   4879   4200     57    -12    210       C
ATOM   4226  CE2 PHE B 267     -18.541  -4.073  33.966  1.00 36.94           C
ANISOU 4226  CE2 PHE B 267     4945   4886   4205     56    -82    192       C
ATOM   4227  CZ  PHE B 267     -19.451  -4.819  34.680  1.00 32.46           C
ANISOU 4227  CZ  PHE B 267     4431   4275   3629     30    -26    202       C
ATOM   4228  N   SER B 268     -13.147  -6.337  32.129  1.00 32.28           N
ANISOU 4228  N   SER B 268     4457   4350   3458    266   -253    197       N
ATOM   4229  CA  SER B 268     -11.754  -6.023  31.893  1.00 35.85           C
ANISOU 4229  CA  SER B 268     4882   4842   3899    319   -298    189       C
ATOM   4230  C   SER B 268     -11.231  -5.089  32.987  1.00 37.74           C
ANISOU 4230  C   SER B 268     5099   5115   4124    344   -316    176       C
ATOM   4231  O   SER B 268     -11.993  -4.361  33.630  1.00 31.20           O
ANISOU 4231  O   SER B 268     4256   4286   3311    312   -295    170       O
ATOM   4232  CB  SER B 268     -11.639  -5.301  30.555  1.00 34.74           C
ANISOU 4232  CB  SER B 268     4664   4727   3810    295   -318    180       C
ATOM   4233  OG  SER B 268     -12.285  -6.064  29.563  1.00 39.77           O
ANISOU 4233  OG  SER B 268     5321   5329   4459    263   -302    191       O
ATOM   4234  N   ASN B 269      -9.910  -5.059  33.155  1.00 34.54           N
ANISOU 4234  N   ASN B 269     4689   4742   3695    400   -356    171       N
ATOM   4235  CA  ASN B 269      -9.319  -4.044  34.021  1.00 37.34           C
ANISOU 4235  CA  ASN B 269     5011   5134   4041    418   -383    155       C
ATOM   4236  C   ASN B 269      -9.393  -2.674  33.324  1.00 33.36           C
ANISOU 4236  C   ASN B 269     4414   4664   3595    382   -394    137       C
ATOM   4237  O   ASN B 269      -9.732  -2.586  32.141  1.00 32.61           O
ANISOU 4237  O   ASN B 269     4283   4567   3541    353   -387    139       O
ATOM   4238  CB  ASN B 269      -7.898  -4.468  34.432  1.00 38.25           C
ANISOU 4238  CB  ASN B 269     5144   5273   4115    489   -427    155       C
ATOM   4239  CG  ASN B 269      -6.917  -4.530  33.273  1.00 40.15           C
ANISOU 4239  CG  ASN B 269     5333   5541   4380    513   -454    152       C
ATOM   4240  OD1 ASN B 269      -7.148  -5.217  32.291  1.00 46.72           O
ANISOU 4240  OD1 ASN B 269     6178   6349   5225    505   -436    163       O
ATOM   4241  ND2 ASN B 269      -5.792  -3.842  33.412  1.00 39.98           N
ANISOU 4241  ND2 ASN B 269     5259   5568   4365    543   -497    137       N
ATOM   4242  N   THR B 270      -9.147  -1.579  34.071  1.00 37.14           N
ANISOU 4242  N   THR B 270     4863   5172   4075    380   -409    121       N
ATOM   4243  CA  THR B 270      -9.445  -0.243  33.513  1.00 35.95           C
ANISOU 4243  CA  THR B 270     4637   5046   3978    339   -409    105       C
ATOM   4244  C   THR B 270      -8.613   0.048  32.274  1.00 33.34           C
ANISOU 4244  C   THR B 270     4244   4743   3678    346   -436     97       C
ATOM   4245  O   THR B 270      -9.139   0.569  31.284  1.00 36.69           O
ANISOU 4245  O   THR B 270     4626   5167   4148    309   -424     95       O
ATOM   4246  CB  THR B 270      -9.307   0.924  34.525  1.00 35.76           C
ANISOU 4246  CB  THR B 270     4596   5045   3947    334   -418     87       C
ATOM   4247  OG1 THR B 270      -7.948   1.339  34.720  1.00 38.96           O
ANISOU 4247  OG1 THR B 270     4973   5493   4339    369   -466     71       O
ATOM   4248  CG2 THR B 270      -9.902   0.554  35.837  1.00 34.52           C
ANISOU 4248  CG2 THR B 270     4511   4858   3747    338   -393     94       C
ATOM   4249  N   VAL B 271      -7.304  -0.254  32.312  1.00 38.66           N
ANISOU 4249  N   VAL B 271     4913   5444   4331    395   -472     93       N
ATOM   4250  CA  VAL B 271      -6.437   0.113  31.192  1.00 42.10           C
ANISOU 4250  CA  VAL B 271     5289   5909   4800    402   -492     84       C
ATOM   4251  C   VAL B 271      -6.766  -0.724  29.959  1.00 41.41           C
ANISOU 4251  C   VAL B 271     5215   5792   4726    394   -473     99       C
ATOM   4252  O   VAL B 271      -6.999  -0.186  28.867  1.00 36.67           O
ANISOU 4252  O   VAL B 271     4573   5194   4166    363   -466     95       O
ATOM   4253  CB  VAL B 271      -4.952  -0.011  31.587  1.00 41.61           C
ANISOU 4253  CB  VAL B 271     5211   5883   4716    457   -534     76       C
ATOM   4254  CG1 VAL B 271      -4.047   0.482  30.441  1.00 41.45           C
ANISOU 4254  CG1 VAL B 271     5121   5893   4735    459   -547     64       C
ATOM   4255  CG2 VAL B 271      -4.681   0.791  32.830  1.00 42.23           C
ANISOU 4255  CG2 VAL B 271     5283   5987   4775    459   -557     60       C
ATOM   4256  N   ASP B 272      -6.822  -2.046  30.115  1.00 41.59           N
ANISOU 4256  N   ASP B 272     5304   5785   4714    422   -463    118       N
ATOM   4257  CA  ASP B 272      -7.159  -2.895  28.969  1.00 44.61           C
ANISOU 4257  CA  ASP B 272     5710   6134   5104    411   -444    132       C
ATOM   4258  C   ASP B 272      -8.584  -2.639  28.473  1.00 44.99           C
ANISOU 4258  C   ASP B 272     5755   6155   5182    348   -417    136       C
ATOM   4259  O   ASP B 272      -8.843  -2.680  27.260  1.00 46.29           O
ANISOU 4259  O   ASP B 272     5907   6308   5374    323   -412    139       O
ATOM   4260  CB  ASP B 272      -6.890  -4.365  29.294  1.00 48.46           C
ANISOU 4260  CB  ASP B 272     6276   6593   5545    455   -438    151       C
ATOM   4261  CG  ASP B 272      -5.380  -4.720  29.164  1.00 54.05           C
ANISOU 4261  CG  ASP B 272     6972   7327   6237    521   -466    150       C
ATOM   4262  OD1 ASP B 272      -4.698  -4.043  28.349  1.00 50.65           O
ANISOU 4262  OD1 ASP B 272     6476   6927   5841    522   -479    137       O
ATOM   4263  OD2 ASP B 272      -4.883  -5.646  29.869  1.00 50.18           O
ANISOU 4263  OD2 ASP B 272     6535   6827   5702    574   -473    161       O
ATOM   4264  N   GLY B 273      -9.533  -2.398  29.390  1.00 44.28           N
ANISOU 4264  N   GLY B 273     5682   6054   5090    321   -399    137       N
ATOM   4265  CA  GLY B 273     -10.892  -2.101  28.955  1.00 37.91           C
ANISOU 4265  CA  GLY B 273     4861   5224   4319    263   -374    141       C
ATOM   4266  C   GLY B 273     -10.948  -0.818  28.151  1.00 40.66           C
ANISOU 4266  C   GLY B 273     5135   5598   4716    235   -386    127       C
ATOM   4267  O   GLY B 273     -11.581  -0.770  27.091  1.00 39.32           O
ANISOU 4267  O   GLY B 273     4949   5414   4577    201   -381    131       O
ATOM   4268  N   PHE B 274     -10.206   0.212  28.599  1.00 35.14           N
ANISOU 4268  N   PHE B 274     4394   4936   4020    251   -404    110       N
ATOM   4269  CA  PHE B 274     -10.103   1.454  27.837  1.00 36.52           C
ANISOU 4269  CA  PHE B 274     4504   5135   4237    229   -414     96       C
ATOM   4270  C   PHE B 274      -9.533   1.213  26.436  1.00 43.31           C
ANISOU 4270  C   PHE B 274     5350   5995   5111    234   -425     97       C
ATOM   4271  O   PHE B 274     -10.024   1.785  25.454  1.00 43.55           O
ANISOU 4271  O   PHE B 274     5352   6021   5176    201   -423     96       O
ATOM   4272  CB  PHE B 274      -9.271   2.493  28.579  1.00 35.45           C
ANISOU 4272  CB  PHE B 274     4334   5038   4098    245   -431     76       C
ATOM   4273  CG  PHE B 274      -9.207   3.821  27.857  1.00 40.59           C
ANISOU 4273  CG  PHE B 274     4924   5709   4790    219   -436     61       C
ATOM   4274  CD1 PHE B 274     -10.195   4.769  28.039  1.00 41.68           C
ANISOU 4274  CD1 PHE B 274     5040   5841   4954    184   -419     58       C
ATOM   4275  CD2 PHE B 274      -8.184   4.102  26.965  1.00 42.82           C
ANISOU 4275  CD2 PHE B 274     5172   6012   5084    232   -453     51       C
ATOM   4276  CE1 PHE B 274     -10.161   5.967  27.364  1.00 40.58           C
ANISOU 4276  CE1 PHE B 274     4853   5716   4850    162   -421     45       C
ATOM   4277  CE2 PHE B 274      -8.156   5.299  26.292  1.00 44.53           C
ANISOU 4277  CE2 PHE B 274     5342   6241   5335    207   -453     38       C
ATOM   4278  CZ  PHE B 274      -9.141   6.223  26.494  1.00 41.59           C
ANISOU 4278  CZ  PHE B 274     4955   5863   4986    173   -439     35       C
ATOM   4279  N   SER B 275      -8.436   0.450  26.330  1.00 42.42           N
ANISOU 4279  N   SER B 275     5257   5889   4971    277   -438     99       N
ATOM   4280  CA  SER B 275      -7.813   0.252  25.018  1.00 43.32           C
ANISOU 4280  CA  SER B 275     5362   6002   5098    285   -442     99       C
ATOM   4281  C   SER B 275      -8.756  -0.453  24.045  1.00 44.26           C
ANISOU 4281  C   SER B 275     5516   6079   5222    254   -428    115       C
ATOM   4282  O   SER B 275      -8.875  -0.037  22.891  1.00 45.28           O
ANISOU 4282  O   SER B 275     5626   6203   5377    231   -430    112       O
ATOM   4283  CB  SER B 275      -6.517  -0.551  25.136  1.00 45.49           C
ANISOU 4283  CB  SER B 275     5654   6288   5344    342   -453    101       C
ATOM   4284  OG  SER B 275      -6.188  -1.150  23.874  1.00 47.30           O
ANISOU 4284  OG  SER B 275     5898   6497   5576    349   -445    108       O
ATOM   4285  N   LYS B 276      -9.497  -1.474  24.502  1.00 42.62           N
ANISOU 4285  N   LYS B 276     5363   5839   4992    248   -415    130       N
ATOM   4286  CA  LYS B 276     -10.328  -2.208  23.545  1.00 46.19           C
ANISOU 4286  CA  LYS B 276     5852   6252   5448    216   -405    143       C
ATOM   4287  C   LYS B 276     -11.482  -1.343  23.046  1.00 49.30           C
ANISOU 4287  C   LYS B 276     6206   6641   5883    161   -406    141       C
ATOM   4288  O   LYS B 276     -11.819  -1.357  21.854  1.00 50.63           O
ANISOU 4288  O   LYS B 276     6376   6793   6068    135   -412    144       O
ATOM   4289  CB  LYS B 276     -10.871  -3.491  24.177  1.00 45.35           C
ANISOU 4289  CB  LYS B 276     5812   6110   5307    218   -387    159       C
ATOM   4290  CG  LYS B 276     -11.877  -4.234  23.268  1.00 50.81           C
ANISOU 4290  CG  LYS B 276     6541   6758   6005    174   -378    171       C
ATOM   4291  CD  LYS B 276     -12.987  -4.930  24.052  1.00 42.04           C
ANISOU 4291  CD  LYS B 276     5470   5618   4885    145   -355    181       C
ATOM   4292  CE  LYS B 276     -12.426  -6.020  24.934  1.00 41.00           C
ANISOU 4292  CE  LYS B 276     5405   5471   4702    189   -340    190       C
ATOM   4293  NZ  LYS B 276     -13.504  -6.644  25.729  1.00 47.35           N
ANISOU 4293  NZ  LYS B 276     6250   6243   5496    158   -312    199       N
ATOM   4294  N   MET B 277     -12.054  -0.541  23.944  1.00 45.68           N
ANISOU 4294  N   MET B 277     5715   6199   5442    146   -400    135       N
ATOM   4295  CA  MET B 277     -13.085   0.423  23.581  1.00 42.97           C
ANISOU 4295  CA  MET B 277     5327   5856   5142    102   -400    133       C
ATOM   4296  C   MET B 277     -12.563   1.487  22.639  1.00 43.13           C
ANISOU 4296  C   MET B 277     5303   5898   5187    101   -417    121       C
ATOM   4297  O   MET B 277     -13.272   1.891  21.719  1.00 47.42           O
ANISOU 4297  O   MET B 277     5829   6430   5759     69   -425    124       O
ATOM   4298  CB  MET B 277     -13.582   1.077  24.866  1.00 43.81           C
ANISOU 4298  CB  MET B 277     5413   5976   5258     97   -385    128       C
ATOM   4299  CG  MET B 277     -14.524   2.235  24.781  1.00 38.87           C
ANISOU 4299  CG  MET B 277     4736   5357   4677     64   -380    124       C
ATOM   4300  SD  MET B 277     -13.651   3.824  24.444  1.00 44.76           S
ANISOU 4300  SD  MET B 277     5426   6140   5441     76   -397    104       S
ATOM   4301  CE  MET B 277     -12.559   3.948  25.832  1.00 40.80           C
ANISOU 4301  CE  MET B 277     4934   5664   4902    115   -395     91       C
ATOM   4302  N   TYR B 278     -11.358   2.003  22.903  1.00 46.44           N
ANISOU 4302  N   TYR B 278     5702   6347   5597    134   -424    107       N
ATOM   4303  CA  TYR B 278     -10.797   3.088  22.102  1.00 47.55           C
ANISOU 4303  CA  TYR B 278     5800   6506   5759    132   -434     94       C
ATOM   4304  C   TYR B 278     -10.378   2.645  20.699  1.00 49.18           C
ANISOU 4304  C   TYR B 278     6027   6695   5963    133   -440     98       C
ATOM   4305  O   TYR B 278     -10.796   3.246  19.708  1.00 51.98           O
ANISOU 4305  O   TYR B 278     6369   7041   6341    107   -446     97       O
ATOM   4306  CB  TYR B 278      -9.606   3.681  22.843  1.00 48.58           C
ANISOU 4306  CB  TYR B 278     5904   6674   5881    163   -438     77       C
ATOM   4307  CG  TYR B 278      -9.061   5.004  22.323  1.00 50.01           C
ANISOU 4307  CG  TYR B 278     6037   6877   6087    155   -443     59       C
ATOM   4308  CD1 TYR B 278      -9.526   6.202  22.829  1.00 51.15           C
ANISOU 4308  CD1 TYR B 278     6148   7035   6253    135   -439     49       C
ATOM   4309  CD2 TYR B 278      -8.051   5.051  21.366  1.00 46.14           C
ANISOU 4309  CD2 TYR B 278     5539   6393   5599    169   -445     52       C
ATOM   4310  CE1 TYR B 278      -9.023   7.400  22.397  1.00 52.22           C
ANISOU 4310  CE1 TYR B 278     6247   7188   6408    126   -440     32       C
ATOM   4311  CE2 TYR B 278      -7.534   6.259  20.937  1.00 46.93           C
ANISOU 4311  CE2 TYR B 278     5598   6511   5721    160   -444     35       C
ATOM   4312  CZ  TYR B 278      -8.028   7.435  21.461  1.00 50.68           C
ANISOU 4312  CZ  TYR B 278     6044   6999   6215    137   -443     25       C
ATOM   4313  OH  TYR B 278      -7.551   8.677  21.070  1.00 56.69           O
ANISOU 4313  OH  TYR B 278     6770   7774   6996    125   -439      7       O
ATOM   4314  N   LYS B 279      -9.557   1.593  20.581  1.00 47.70           N
ANISOU 4314  N   LYS B 279     5877   6500   5746    165   -437    102       N
ATOM   4315  CA  LYS B 279      -9.048   1.275  19.250  1.00 52.81           C
ANISOU 4315  CA  LYS B 279     6545   7130   6390    170   -437    104       C
ATOM   4316  C   LYS B 279      -9.996   0.406  18.430  1.00 61.07           C
ANISOU 4316  C   LYS B 279     7642   8134   7429    141   -438    120       C
ATOM   4317  O   LYS B 279      -9.941   0.451  17.192  1.00 62.50           O
ANISOU 4317  O   LYS B 279     7840   8296   7613    128   -441    121       O
ATOM   4318  CB  LYS B 279      -7.655   0.626  19.350  1.00 53.99           C
ANISOU 4318  CB  LYS B 279     6707   7291   6515    220   -430    102       C
ATOM   4319  CG  LYS B 279      -7.511  -0.479  20.378  1.00 50.04           C
ANISOU 4319  CG  LYS B 279     6244   6788   5983    252   -427    112       C
ATOM   4320  CD  LYS B 279      -6.115  -1.092  20.405  1.00 55.33           C
ANISOU 4320  CD  LYS B 279     6921   7468   6632    308   -423    111       C
ATOM   4321  CE  LYS B 279      -5.063  -0.168  21.019  1.00 53.19           C
ANISOU 4321  CE  LYS B 279     6586   7247   6376    333   -434     92       C
ATOM   4322  NZ  LYS B 279      -3.752  -0.852  21.323  1.00 36.66           N
ANISOU 4322  NZ  LYS B 279     4494   5170   4264    394   -435     93       N
ATOM   4323  N   SER B 280     -10.874  -0.361  19.073  1.00 60.43           N
ANISOU 4323  N   SER B 280     7590   8035   7338    127   -435    132       N
ATOM   4324  CA  SER B 280     -11.885  -1.150  18.359  1.00 61.75           C
ANISOU 4324  CA  SER B 280     7800   8162   7501     90   -439    146       C
ATOM   4325  C   SER B 280     -13.212  -0.387  18.289  1.00 57.50           C
ANISOU 4325  C   SER B 280     7225   7623   7001     42   -451    147       C
ATOM   4326  O   SER B 280     -14.239  -0.828  18.800  1.00 49.00           O
ANISOU 4326  O   SER B 280     6155   6532   5930     15   -448    155       O
ATOM   4327  CB  SER B 280     -12.045  -2.527  19.011  1.00 66.11           C
ANISOU 4327  CB  SER B 280     8409   8689   8019    100   -425    158       C
ATOM   4328  OG  SER B 280     -10.927  -3.393  18.765  1.00 64.03           O
ANISOU 4328  OG  SER B 280     8191   8416   7720    144   -415    160       O
ATOM   4329  N   PHE B 281     -13.170   0.788  17.661  1.00 63.52           N
ANISOU 4329  N   PHE B 281     7945   8400   7789     33   -464    138       N
ATOM   4330  CA  PHE B 281     -14.336   1.669  17.554  1.00 62.17           C
ANISOU 4330  CA  PHE B 281     7732   8232   7657     -4   -477    139       C
ATOM   4331  C   PHE B 281     -14.271   2.568  16.315  1.00 64.11           C
ANISOU 4331  C   PHE B 281     7965   8476   7920    -15   -496    135       C
ATOM   4332  O   PHE B 281     -14.291   2.094  15.179  1.00 69.22           O
ANISOU 4332  O   PHE B 281     8651   9095   8553    -27   -509    140       O
ATOM   4333  CB  PHE B 281     -14.457   2.537  18.800  1.00 62.13           C
ANISOU 4333  CB  PHE B 281     7678   8258   7672      4   -464    132       C
ATOM   4334  CG  PHE B 281     -15.307   3.766  18.610  1.00 64.88           C
ANISOU 4334  CG  PHE B 281     7976   8615   8062    -20   -473    130       C
ATOM   4335  CD1 PHE B 281     -16.690   3.689  18.710  1.00 65.20           C
ANISOU 4335  CD1 PHE B 281     8000   8642   8131    -54   -477    141       C
ATOM   4336  CD2 PHE B 281     -14.722   5.004  18.337  1.00 64.76           C
ANISOU 4336  CD2 PHE B 281     7928   8619   8058     -8   -475    117       C
ATOM   4337  CE1 PHE B 281     -17.482   4.821  18.550  1.00 66.55           C
ANISOU 4337  CE1 PHE B 281     8122   8821   8342    -70   -485    141       C
ATOM   4338  CE2 PHE B 281     -15.500   6.141  18.165  1.00 64.36           C
ANISOU 4338  CE2 PHE B 281     7837   8574   8044    -26   -481    117       C
ATOM   4339  CZ  PHE B 281     -16.891   6.050  18.273  1.00 65.39           C
ANISOU 4339  CZ  PHE B 281     7950   8692   8203    -54   -487    129       C
TER
ATOM   4340  N   PRO C   0     -17.761  43.022  17.482  1.00 58.96           N
ANISOU 4340  N   PRO C   0     7565   7387   7449    124    222    -57       N
ATOM   4341  CA  PRO C   0     -17.208  43.889  18.542  1.00 64.15           C
ANISOU 4341  CA  PRO C   0     8265   8028   8081     91    282    -89       C
ATOM   4342  C   PRO C   0     -15.747  43.532  18.903  1.00 60.49           C
ANISOU 4342  C   PRO C   0     7798   7595   7590     18    282   -133       C
ATOM   4343  O   PRO C   0     -14.874  44.368  18.769  1.00 54.83           O
ANISOU 4343  O   PRO C   0     7138   6852   6842    -21    317   -162       O
ATOM   4344  CB  PRO C   0     -18.170  43.664  19.717  1.00 63.83           C
ANISOU 4344  CB  PRO C   0     8184   8000   8066    121    294    -74       C
ATOM   4345  CG  PRO C   0     -18.862  42.341  19.412  1.00 62.77           C
ANISOU 4345  CG  PRO C   0     7969   7908   7972    148    233    -45       C
ATOM   4346  CD  PRO C   0     -18.968  42.303  17.925  1.00 59.58           C
ANISOU 4346  CD  PRO C   0     7576   7489   7571    169    195    -25       C
ATOM   4347  N   MET C   1     -15.473  42.325  19.379  1.00 61.07           N
ANISOU 4347  N   MET C   1     7806   7723   7675     -1    244   -137       N
ATOM   4348  CA  MET C   1     -14.081  41.910  19.485  1.00 65.50           C
ANISOU 4348  CA  MET C   1     8357   8314   8215    -62    235   -174       C
ATOM   4349  C   MET C   1     -13.632  41.437  18.101  1.00 60.69           C
ANISOU 4349  C   MET C   1     7743   7708   7607    -67    203   -167       C
ATOM   4350  O   MET C   1     -14.376  40.737  17.406  1.00 56.96           O
ANISOU 4350  O   MET C   1     7242   7244   7157    -28    163   -134       O
ATOM   4351  CB  MET C   1     -13.957  40.758  20.464  1.00 62.10           C
ANISOU 4351  CB  MET C   1     7862   7937   7794    -74    204   -179       C
ATOM   4352  CG  MET C   1     -12.545  40.380  20.822  1.00 58.44           C
ANISOU 4352  CG  MET C   1     7385   7509   7310   -134    195   -217       C
ATOM   4353  SD  MET C   1     -12.615  38.908  21.934  1.00 61.02           S
ANISOU 4353  SD  MET C   1     7640   7896   7648   -133    152   -214       S
ATOM   4354  CE  MET C   1     -13.527  39.602  23.351  1.00 64.04           C
ANISOU 4354  CE  MET C   1     8051   8256   8025   -114    195   -211       C
ATOM   4355  N   LYS C   2     -12.432  41.827  17.684  1.00 64.95           N
ANISOU 4355  N   LYS C   2     8314   8241   8123   -115    222   -198       N
ATOM   4356  CA  LYS C   2     -12.028  41.447  16.340  1.00 60.89           C
ANISOU 4356  CA  LYS C   2     7805   7722   7607   -117    201   -192       C
ATOM   4357  C   LYS C   2     -11.937  39.926  16.288  1.00 59.28           C
ANISOU 4357  C   LYS C   2     7531   7571   7423   -114    146   -181       C
ATOM   4358  O   LYS C   2     -11.331  39.299  17.158  1.00 58.89           O
ANISOU 4358  O   LYS C   2     7437   7564   7375   -143    135   -201       O
ATOM   4359  CB  LYS C   2     -10.706  42.125  15.962  1.00 57.27           C
ANISOU 4359  CB  LYS C   2     7390   7247   7125   -174    239   -229       C
ATOM   4360  N   THR C   3     -12.595  39.324  15.309  1.00 56.52           N
ANISOU 4360  N   THR C   3     7172   7216   7085    -77    109   -149       N
ATOM   4361  CA  THR C   3     -12.613  37.873  15.178  1.00 61.12           C
ANISOU 4361  CA  THR C   3     7696   7843   7685    -72     57   -136       C
ATOM   4362  C   THR C   3     -11.638  37.404  14.097  1.00 62.08           C
ANISOU 4362  C   THR C   3     7828   7967   7794    -96     48   -147       C
ATOM   4363  O   THR C   3     -11.597  37.980  12.999  1.00 59.80           O
ANISOU 4363  O   THR C   3     7593   7636   7491    -91     61   -141       O
ATOM   4364  CB  THR C   3     -14.037  37.366  14.923  1.00 60.99           C
ANISOU 4364  CB  THR C   3     7655   7824   7693    -18     18    -94       C
ATOM   4365  OG1 THR C   3     -14.026  35.945  14.746  1.00 62.65           O
ANISOU 4365  OG1 THR C   3     7814   8073   7916    -17    -30    -84       O
ATOM   4366  CG2 THR C   3     -14.659  38.026  13.744  1.00 63.80           C
ANISOU 4366  CG2 THR C   3     8062   8133   8045     15     15    -71       C
ATOM   4367  N   ILE C   4     -10.838  36.376  14.429  1.00 58.31           N
ANISOU 4367  N   ILE C   4     7301   7534   7319   -122     29   -162       N
ATOM   4368  CA  ILE C   4      -9.827  35.807  13.539  1.00 52.63           C
ANISOU 4368  CA  ILE C   4     6583   6821   6592   -145     25   -173       C
ATOM   4369  C   ILE C   4     -10.154  34.338  13.269  1.00 53.33           C
ANISOU 4369  C   ILE C   4     6628   6940   6693   -124    -27   -151       C
ATOM   4370  O   ILE C   4     -10.313  33.546  14.207  1.00 53.94           O
ANISOU 4370  O   ILE C   4     6654   7058   6783   -120    -50   -149       O
ATOM   4371  CB  ILE C   4      -8.414  35.944  14.127  1.00 48.02           C
ANISOU 4371  CB  ILE C   4     5980   6262   6001   -197     53   -215       C
ATOM   4372  CG1 ILE C   4      -8.152  37.386  14.567  1.00 49.88           C
ANISOU 4372  CG1 ILE C   4     6258   6469   6224   -223    103   -239       C
ATOM   4373  CG2 ILE C   4      -7.362  35.455  13.107  1.00 48.03           C
ANISOU 4373  CG2 ILE C   4     5985   6266   5999   -219     59   -226       C
ATOM   4374  CD1 ILE C   4      -6.768  37.606  15.210  1.00 47.99           C
ANISOU 4374  CD1 ILE C   4     5998   6257   5981   -280    128   -283       C
ATOM   4375  N   LEU C   5     -10.244  33.975  11.989  1.00 46.01           N
ANISOU 4375  N   LEU C   5     5730   5991   5759   -111    -44   -134       N
ATOM   4376  CA  LEU C   5     -10.442  32.594  11.565  1.00 44.72           C
ANISOU 4376  CA  LEU C   5     5539   5850   5603    -96    -89   -114       C
ATOM   4377  C   LEU C   5      -9.096  31.984  11.172  1.00 49.88           C
ANISOU 4377  C   LEU C   5     6184   6519   6247   -126    -76   -137       C
ATOM   4378  O   LEU C   5      -8.437  32.468  10.242  1.00 52.15           O
ANISOU 4378  O   LEU C   5     6519   6776   6520   -142    -47   -147       O
ATOM   4379  CB  LEU C   5     -11.416  32.532  10.394  1.00 50.51           C
ANISOU 4379  CB  LEU C   5     6312   6547   6332    -63   -120    -81       C
ATOM   4380  CG  LEU C   5     -11.445  31.263   9.557  1.00 49.69           C
ANISOU 4380  CG  LEU C   5     6204   6450   6224    -56   -161    -65       C
ATOM   4381  CD1 LEU C   5     -11.865  30.095  10.432  1.00 41.52           C
ANISOU 4381  CD1 LEU C   5     5104   5460   5210    -48   -196    -55       C
ATOM   4382  CD2 LEU C   5     -12.385  31.473   8.356  1.00 48.46           C
ANISOU 4382  CD2 LEU C   5     6102   6252   6060    -27   -190    -35       C
ATOM   4383  N   VAL C   6      -8.702  30.917  11.860  1.00 47.32           N
ANISOU 4383  N   VAL C   6     5805   6241   5933   -131    -97   -142       N
ATOM   4384  CA  VAL C   6      -7.400  30.283  11.688  1.00 44.85           C
ANISOU 4384  CA  VAL C   6     5473   5951   5618   -155    -85   -164       C
ATOM   4385  C   VAL C   6      -7.581  28.894  11.065  1.00 42.53           C
ANISOU 4385  C   VAL C   6     5172   5666   5323   -135   -122   -142       C
ATOM   4386  O   VAL C   6      -8.248  28.030  11.646  1.00 42.06           O
ANISOU 4386  O   VAL C   6     5078   5630   5272   -117   -159   -125       O
ATOM   4387  CB  VAL C   6      -6.685  30.204  13.041  1.00 43.72           C
ANISOU 4387  CB  VAL C   6     5276   5854   5484   -176    -78   -190       C
ATOM   4388  CG1 VAL C   6      -5.234  29.724  12.870  1.00 43.13           C
ANISOU 4388  CG1 VAL C   6     5174   5803   5410   -201    -62   -215       C
ATOM   4389  CG2 VAL C   6      -6.821  31.554  13.771  1.00 38.87           C
ANISOU 4389  CG2 VAL C   6     4675   5226   4867   -193    -49   -206       C
ATOM   4390  N   THR C   7      -6.997  28.670   9.890  1.00 38.78           N
ANISOU 4390  N   THR C   7     4732   5167   4836   -141   -108   -143       N
ATOM   4391  CA  THR C   7      -6.946  27.321   9.334  1.00 37.00           C
ANISOU 4391  CA  THR C   7     4504   4950   4606   -127   -136   -127       C
ATOM   4392  C   THR C   7      -5.722  26.560   9.865  1.00 45.00           C
ANISOU 4392  C   THR C   7     5466   6004   5627   -140   -123   -148       C
ATOM   4393  O   THR C   7      -4.716  27.154  10.275  1.00 42.99           O
ANISOU 4393  O   THR C   7     5191   5764   5380   -166    -88   -178       O
ATOM   4394  CB  THR C   7      -6.896  27.338   7.798  1.00 39.08           C
ANISOU 4394  CB  THR C   7     4835   5164   4848   -123   -127   -116       C
ATOM   4395  OG1 THR C   7      -5.580  27.708   7.351  1.00 37.88           O
ANISOU 4395  OG1 THR C   7     4698   5004   4692   -149    -73   -143       O
ATOM   4396  CG2 THR C   7      -7.926  28.290   7.215  1.00 41.74           C
ANISOU 4396  CG2 THR C   7     5227   5458   5174   -110   -135    -99       C
ATOM   4397  N   GLY C   8      -5.800  25.223   9.812  1.00 42.80           N
ANISOU 4397  N   GLY C   8     5171   5743   5348   -123   -154   -134       N
ATOM   4398  CA  GLY C   8      -4.737  24.412  10.372  1.00 40.09           C
ANISOU 4398  CA  GLY C   8     4779   5439   5013   -127   -148   -150       C
ATOM   4399  C   GLY C   8      -4.469  24.677  11.841  1.00 39.74           C
ANISOU 4399  C   GLY C   8     4678   5438   4982   -136   -152   -168       C
ATOM   4400  O   GLY C   8      -3.333  24.988  12.210  1.00 41.89           O
ANISOU 4400  O   GLY C   8     4919   5733   5263   -156   -126   -196       O
ATOM   4401  N   GLY C   9      -5.500  24.591  12.682  1.00 40.60           N
ANISOU 4401  N   GLY C   9     4774   5558   5094   -123   -183   -154       N
ATOM   4402  CA  GLY C   9      -5.342  24.906  14.091  1.00 43.03           C
ANISOU 4402  CA  GLY C   9     5039   5901   5409   -131   -185   -170       C
ATOM   4403  C   GLY C   9      -4.368  24.014  14.838  1.00 47.69           C
ANISOU 4403  C   GLY C   9     5582   6536   6003   -130   -196   -184       C
ATOM   4404  O   GLY C   9      -3.753  24.484  15.809  1.00 45.45           O
ANISOU 4404  O   GLY C   9     5267   6280   5722   -147   -190   -207       O
ATOM   4405  N   SER C  10      -4.130  22.781  14.346  1.00 49.12           N
ANISOU 4405  N   SER C  10     5761   6722   6181   -111   -210   -170       N
ATOM   4406  CA  SER C  10      -3.319  21.762  15.024  1.00 48.55           C
ANISOU 4406  CA  SER C  10     5647   6690   6110    -99   -225   -177       C
ATOM   4407  C   SER C  10      -1.874  21.674  14.530  1.00 50.57           C
ANISOU 4407  C   SER C  10     5881   6958   6374   -108   -198   -198       C
ATOM   4408  O   SER C  10      -1.181  20.711  14.865  1.00 48.82           O
ANISOU 4408  O   SER C  10     5627   6766   6156    -91   -210   -200       O
ATOM   4409  CB  SER C  10      -3.953  20.384  14.883  1.00 44.22           C
ANISOU 4409  CB  SER C  10     5110   6140   5553    -70   -255   -149       C
ATOM   4410  OG  SER C  10      -3.700  19.854  13.594  1.00 53.20           O
ANISOU 4410  OG  SER C  10     6278   7251   6685    -63   -243   -139       O
ATOM   4411  N   GLY C  11      -1.428  22.592  13.675  1.00 49.76           N
ANISOU 4411  N   GLY C  11     5798   6830   6277   -131   -160   -212       N
ATOM   4412  CA  GLY C  11      -0.056  22.567  13.223  1.00 50.43           C
ANISOU 4412  CA  GLY C  11     5859   6927   6377   -143   -127   -233       C
ATOM   4413  C   GLY C  11       0.926  23.244  14.175  1.00 46.30           C
ANISOU 4413  C   GLY C  11     5280   6443   5871   -170   -120   -267       C
ATOM   4414  O   GLY C  11       0.577  23.847  15.190  1.00 46.52           O
ANISOU 4414  O   GLY C  11     5295   6485   5894   -182   -137   -276       O
ATOM   4415  N   PHE C  12       2.201  23.132  13.813  1.00 45.58           N
ANISOU 4415  N   PHE C  12     5154   6367   5798   -179    -92   -287       N
ATOM   4416  CA  PHE C  12       3.255  23.768  14.593  1.00 45.99           C
ANISOU 4416  CA  PHE C  12     5147   6457   5871   -209    -85   -321       C
ATOM   4417  C   PHE C  12       2.958  25.251  14.771  1.00 42.16           C
ANISOU 4417  C   PHE C  12     4685   5951   5382   -251    -65   -339       C
ATOM   4418  O   PHE C  12       2.910  25.750  15.901  1.00 38.34           O
ANISOU 4418  O   PHE C  12     4180   5493   4896   -267    -87   -355       O
ATOM   4419  CB  PHE C  12       4.605  23.550  13.904  1.00 47.30           C
ANISOU 4419  CB  PHE C  12     5276   6633   6064   -216    -47   -338       C
ATOM   4420  CG  PHE C  12       5.763  24.218  14.569  1.00 43.60           C
ANISOU 4420  CG  PHE C  12     4741   6204   5623   -253    -38   -376       C
ATOM   4421  CD1 PHE C  12       6.078  25.545  14.281  1.00 40.48           C
ANISOU 4421  CD1 PHE C  12     4356   5789   5237   -303      4   -402       C
ATOM   4422  CD2 PHE C  12       6.561  23.516  15.455  1.00 39.41           C
ANISOU 4422  CD2 PHE C  12     4138   5729   5108   -237    -73   -385       C
ATOM   4423  CE1 PHE C  12       7.132  26.169  14.893  1.00 37.20           C
ANISOU 4423  CE1 PHE C  12     3878   5408   4847   -343     10   -438       C
ATOM   4424  CE2 PHE C  12       7.638  24.142  16.073  1.00 39.89           C
ANISOU 4424  CE2 PHE C  12     4132   5828   5196   -273    -72   -421       C
ATOM   4425  CZ  PHE C  12       7.931  25.469  15.796  1.00 35.45           C
ANISOU 4425  CZ  PHE C  12     3578   5246   4644   -329    -30   -449       C
ATOM   4426  N   LEU C  13       2.675  25.955  13.666  1.00 38.41           N
ANISOU 4426  N   LEU C  13     4266   5427   4902   -266    -23   -336       N
ATOM   4427  CA  LEU C  13       2.407  27.383  13.768  1.00 37.99           C
ANISOU 4427  CA  LEU C  13     4242   5348   4843   -303      2   -353       C
ATOM   4428  C   LEU C  13       0.976  27.644  14.236  1.00 39.65           C
ANISOU 4428  C   LEU C  13     4494   5541   5031   -286    -27   -331       C
ATOM   4429  O   LEU C  13       0.747  28.519  15.082  1.00 34.60           O
ANISOU 4429  O   LEU C  13     3855   4906   4387   -308    -30   -345       O
ATOM   4430  CB  LEU C  13       2.694  28.079  12.430  1.00 34.51           C
ANISOU 4430  CB  LEU C  13     3850   4858   4402   -325     61   -358       C
ATOM   4431  CG  LEU C  13       2.655  29.620  12.435  1.00 35.07           C
ANISOU 4431  CG  LEU C  13     3956   4900   4470   -368     98   -380       C
ATOM   4432  CD1 LEU C  13       3.275  30.242  13.723  1.00 32.86           C
ANISOU 4432  CD1 LEU C  13     3622   4662   4202   -405     88   -414       C
ATOM   4433  CD2 LEU C  13       3.349  30.183  11.210  1.00 34.01           C
ANISOU 4433  CD2 LEU C  13     3856   4726   4341   -394    163   -393       C
ATOM   4434  N   GLY C  14       0.009  26.887  13.711  1.00 42.23           N
ANISOU 4434  N   GLY C  14     4854   5846   5344   -249    -49   -296       N
ATOM   4435  CA  GLY C  14      -1.374  27.095  14.111  1.00 43.30           C
ANISOU 4435  CA  GLY C  14     5021   5966   5466   -232    -75   -274       C
ATOM   4436  C   GLY C  14      -1.578  27.002  15.613  1.00 47.09           C
ANISOU 4436  C   GLY C  14     5463   6483   5944   -230   -107   -280       C
ATOM   4437  O   GLY C  14      -2.127  27.923  16.231  1.00 44.99           O
ANISOU 4437  O   GLY C  14     5214   6208   5673   -242   -102   -286       O
ATOM   4438  N   ARG C  15      -1.056  25.928  16.236  1.00 50.04           N
ANISOU 4438  N   ARG C  15     5791   6900   6323   -214   -136   -281       N
ATOM   4439  CA  ARG C  15      -1.254  25.740  17.674  1.00 47.75           C
ANISOU 4439  CA  ARG C  15     5472   6643   6026   -210   -169   -285       C
ATOM   4440  C   ARG C  15      -0.760  26.946  18.455  1.00 46.59           C
ANISOU 4440  C   ARG C  15     5316   6506   5879   -249   -154   -318       C
ATOM   4441  O   ARG C  15      -1.431  27.413  19.376  1.00 50.18           O
ANISOU 4441  O   ARG C  15     5784   6959   6322   -251   -164   -318       O
ATOM   4442  CB  ARG C  15      -0.511  24.491  18.172  1.00 49.58           C
ANISOU 4442  CB  ARG C  15     5657   6919   6261   -189   -199   -286       C
ATOM   4443  CG  ARG C  15      -0.946  23.116  17.636  1.00 57.95           C
ANISOU 4443  CG  ARG C  15     6726   7974   7317   -149   -218   -254       C
ATOM   4444  CD  ARG C  15      -0.431  21.952  18.529  1.00 55.40           C
ANISOU 4444  CD  ARG C  15     6363   7694   6991   -124   -254   -253       C
ATOM   4445  NE  ARG C  15       1.016  21.784  18.406  1.00 52.42           N
ANISOU 4445  NE  ARG C  15     5940   7347   6631   -130   -246   -276       N
ATOM   4446  CZ  ARG C  15       1.643  21.136  17.413  1.00 60.99           C
ANISOU 4446  CZ  ARG C  15     7019   8428   7728   -117   -228   -270       C
ATOM   4447  NH1 ARG C  15       0.958  20.553  16.432  1.00 52.75           N
ANISOU 4447  NH1 ARG C  15     6018   7348   6676    -97   -220   -244       N
ATOM   4448  NH2 ARG C  15       2.983  21.069  17.397  1.00 56.08           N
ANISOU 4448  NH2 ARG C  15     6345   7835   7126   -123   -219   -293       N
ATOM   4449  N   ARG C  16       0.386  27.498  18.069  1.00 43.81           N
ANISOU 4449  N   ARG C  16     4944   6160   5542   -282   -126   -347       N
ATOM   4450  CA  ARG C  16       0.946  28.636  18.791  1.00 41.96           C
ANISOU 4450  CA  ARG C  16     4700   5935   5308   -326   -113   -381       C
ATOM   4451  C   ARG C  16       0.268  29.965  18.456  1.00 43.73           C
ANISOU 4451  C   ARG C  16     4983   6111   5522   -348    -75   -384       C
ATOM   4452  O   ARG C  16       0.215  30.850  19.325  1.00 43.71           O
ANISOU 4452  O   ARG C  16     4990   6108   5509   -375    -72   -403       O
ATOM   4453  CB  ARG C  16       2.454  28.707  18.537  1.00 34.68           C
ANISOU 4453  CB  ARG C  16     3728   5040   4409   -357    -97   -412       C
ATOM   4454  CG  ARG C  16       3.240  27.608  19.239  1.00 36.67           C
ANISOU 4454  CG  ARG C  16     3914   5347   4670   -339   -140   -417       C
ATOM   4455  CD  ARG C  16       4.486  27.172  18.485  1.00 34.68           C
ANISOU 4455  CD  ARG C  16     3615   5115   4449   -344   -121   -429       C
ATOM   4456  NE  ARG C  16       5.278  26.158  19.208  1.00 36.30           N
ANISOU 4456  NE  ARG C  16     3753   5374   4664   -322   -164   -433       N
ATOM   4457  CZ  ARG C  16       5.235  24.838  18.963  1.00 39.31           C
ANISOU 4457  CZ  ARG C  16     4123   5767   5046   -272   -184   -408       C
ATOM   4458  NH1 ARG C  16       4.438  24.340  18.010  1.00 41.60           N
ANISOU 4458  NH1 ARG C  16     4461   6018   5326   -244   -167   -377       N
ATOM   4459  NH2 ARG C  16       6.006  24.001  19.655  1.00 37.08           N
ANISOU 4459  NH2 ARG C  16     3783   5534   4773   -251   -223   -413       N
ATOM   4460  N   LEU C  17      -0.270  30.125  17.235  1.00 42.88           N
ANISOU 4460  N   LEU C  17     4919   5959   5413   -336    -49   -364       N
ATOM   4461  CA  LEU C  17      -0.967  31.374  16.904  1.00 44.86           C
ANISOU 4461  CA  LEU C  17     5231   6162   5654   -349    -15   -363       C
ATOM   4462  C   LEU C  17      -2.255  31.507  17.710  1.00 48.40           C
ANISOU 4462  C   LEU C  17     5701   6601   6088   -324    -37   -343       C
ATOM   4463  O   LEU C  17      -2.506  32.554  18.323  1.00 47.61           O
ANISOU 4463  O   LEU C  17     5627   6486   5978   -344    -19   -356       O
ATOM   4464  CB  LEU C  17      -1.264  31.448  15.399  1.00 37.93           C
ANISOU 4464  CB  LEU C  17     4399   5238   4775   -337     12   -344       C
ATOM   4465  CG  LEU C  17      -0.054  31.668  14.472  1.00 38.15           C
ANISOU 4465  CG  LEU C  17     4424   5258   4815   -368     54   -366       C
ATOM   4466  CD1 LEU C  17      -0.435  31.601  12.977  1.00 34.14           C
ANISOU 4466  CD1 LEU C  17     3972   4701   4298   -349     77   -344       C
ATOM   4467  CD2 LEU C  17       0.682  32.958  14.791  1.00 35.55           C
ANISOU 4467  CD2 LEU C  17     4099   4922   4488   -421     94   -404       C
ATOM   4468  N   VAL C  18      -3.050  30.427  17.776  1.00 48.74           N
ANISOU 4468  N   VAL C  18     5734   6653   6130   -282    -72   -311       N
ATOM   4469  CA  VAL C  18      -4.246  30.425  18.624  1.00 51.84           C
ANISOU 4469  CA  VAL C  18     6139   7042   6515   -258    -90   -292       C
ATOM   4470  C   VAL C  18      -3.906  30.830  20.055  1.00 52.04           C
ANISOU 4470  C   VAL C  18     6149   7093   6531   -281    -95   -317       C
ATOM   4471  O   VAL C  18      -4.466  31.795  20.595  1.00 53.10           O
ANISOU 4471  O   VAL C  18     6315   7205   6655   -289    -76   -322       O
ATOM   4472  CB  VAL C  18      -4.937  29.047  18.592  1.00 53.32           C
ANISOU 4472  CB  VAL C  18     6309   7244   6706   -218   -129   -260       C
ATOM   4473  CG1 VAL C  18      -6.014  28.972  19.665  1.00 52.22           C
ANISOU 4473  CG1 VAL C  18     6172   7108   6562   -198   -144   -245       C
ATOM   4474  CG2 VAL C  18      -5.656  28.881  17.261  1.00 46.62           C
ANISOU 4474  CG2 VAL C  18     5491   6359   5862   -196   -126   -232       C
ATOM   4475  N   SER C  19      -2.959  30.122  20.674  1.00 51.01           N
ANISOU 4475  N   SER C  19     5973   7008   6401   -289   -121   -334       N
ATOM   4476  CA  SER C  19      -2.680  30.363  22.085  1.00 54.17           C
ANISOU 4476  CA  SER C  19     6362   7434   6788   -307   -136   -355       C
ATOM   4477  C   SER C  19      -2.334  31.828  22.330  1.00 53.77           C
ANISOU 4477  C   SER C  19     6339   7363   6729   -352   -102   -386       C
ATOM   4478  O   SER C  19      -2.882  32.466  23.234  1.00 54.24           O
ANISOU 4478  O   SER C  19     6427   7410   6771   -358    -96   -391       O
ATOM   4479  CB  SER C  19      -1.554  29.429  22.554  1.00 54.75           C
ANISOU 4479  CB  SER C  19     6379   7559   6864   -310   -172   -370       C
ATOM   4480  OG  SER C  19      -1.961  28.054  22.560  1.00 44.88           O
ANISOU 4480  OG  SER C  19     5112   6325   5615   -266   -204   -341       O
ATOM   4481  N   HIS C  20      -1.446  32.387  21.507  1.00 51.44           N
ANISOU 4481  N   HIS C  20     6039   7061   6446   -385    -75   -407       N
ATOM   4482  CA  HIS C  20      -1.017  33.765  21.714  1.00 51.90           C
ANISOU 4482  CA  HIS C  20     6125   7098   6496   -434    -40   -439       C
ATOM   4483  C   HIS C  20      -2.114  34.747  21.318  1.00 54.63           C
ANISOU 4483  C   HIS C  20     6538   7387   6831   -424     -1   -424       C
ATOM   4484  O   HIS C  20      -2.332  35.754  22.001  1.00 55.97           O
ANISOU 4484  O   HIS C  20     6745   7537   6985   -446     19   -439       O
ATOM   4485  CB  HIS C  20       0.252  34.038  20.918  1.00 50.95           C
ANISOU 4485  CB  HIS C  20     5980   6985   6395   -473    -17   -467       C
ATOM   4486  CG  HIS C  20       0.567  35.488  20.783  1.00 49.60           C
ANISOU 4486  CG  HIS C  20     5849   6780   6218   -524     30   -495       C
ATOM   4487  ND1 HIS C  20       1.498  36.119  21.579  1.00 54.39           N
ANISOU 4487  ND1 HIS C  20     6437   7407   6820   -578     30   -536       N
ATOM   4488  CD2 HIS C  20       0.077  36.436  19.949  1.00 50.11           C
ANISOU 4488  CD2 HIS C  20     5975   6789   6276   -529     79   -489       C
ATOM   4489  CE1 HIS C  20       1.566  37.395  21.244  1.00 52.25           C
ANISOU 4489  CE1 HIS C  20     6217   7094   6543   -618     80   -555       C
ATOM   4490  NE2 HIS C  20       0.712  37.614  20.258  1.00 51.89           N
ANISOU 4490  NE2 HIS C  20     6221   7000   6494   -587    112   -527       N
ATOM   4491  N   LEU C  21      -2.827  34.475  20.223  1.00 52.63           N
ANISOU 4491  N   LEU C  21     6305   7106   6587   -389      7   -392       N
ATOM   4492  CA  LEU C  21      -3.758  35.492  19.766  1.00 55.18           C
ANISOU 4492  CA  LEU C  21     6691   7374   6902   -380     43   -379       C
ATOM   4493  C   LEU C  21      -5.070  35.419  20.520  1.00 54.83           C
ANISOU 4493  C   LEU C  21     6662   7320   6850   -341     31   -353       C
ATOM   4494  O   LEU C  21      -5.777  36.429  20.599  1.00 54.85           O
ANISOU 4494  O   LEU C  21     6713   7282   6843   -337     61   -349       O
ATOM   4495  CB  LEU C  21      -4.015  35.363  18.257  1.00 53.47           C
ANISOU 4495  CB  LEU C  21     6496   7126   6694   -359     57   -356       C
ATOM   4496  CG  LEU C  21      -2.859  35.632  17.274  1.00 50.71           C
ANISOU 4496  CG  LEU C  21     6149   6769   6351   -394     87   -379       C
ATOM   4497  CD1 LEU C  21      -3.287  35.295  15.853  1.00 40.64           C
ANISOU 4497  CD1 LEU C  21     4902   5461   5078   -364     92   -350       C
ATOM   4498  CD2 LEU C  21      -2.373  37.079  17.349  1.00 46.09           C
ANISOU 4498  CD2 LEU C  21     5604   6152   5755   -442    136   -410       C
ATOM   4499  N   SER C  22      -5.375  34.282  21.148  1.00 55.02           N
ANISOU 4499  N   SER C  22     6648   7380   6878   -315    -10   -337       N
ATOM   4500  CA  SER C  22      -6.618  34.218  21.905  1.00 56.56           C
ANISOU 4500  CA  SER C  22     6856   7565   7069   -282    -15   -314       C
ATOM   4501  C   SER C  22      -6.596  35.130  23.120  1.00 55.35           C
ANISOU 4501  C   SER C  22     6731   7405   6896   -305      6   -337       C
ATOM   4502  O   SER C  22      -7.647  35.327  23.730  1.00 55.11           O
ANISOU 4502  O   SER C  22     6723   7356   6862   -280     16   -320       O
ATOM   4503  CB  SER C  22      -6.952  32.781  22.333  1.00 53.62           C
ANISOU 4503  CB  SER C  22     6442   7228   6704   -251    -58   -293       C
ATOM   4504  OG  SER C  22      -7.267  31.949  21.219  1.00 53.35           O
ANISOU 4504  OG  SER C  22     6393   7191   6686   -224    -76   -266       O
ATOM   4505  N   LYS C  23      -5.441  35.724  23.452  1.00 58.08           N
ANISOU 4505  N   LYS C  23     7078   7760   7229   -355     15   -376       N
ATOM   4506  CA  LYS C  23      -5.361  36.519  24.669  1.00 59.25           C
ANISOU 4506  CA  LYS C  23     7257   7903   7354   -382     29   -400       C
ATOM   4507  C   LYS C  23      -6.178  37.789  24.537  1.00 55.11           C
ANISOU 4507  C   LYS C  23     6796   7321   6820   -378     79   -395       C
ATOM   4508  O   LYS C  23      -6.851  38.195  25.488  1.00 59.18           O
ANISOU 4508  O   LYS C  23     7345   7821   7321   -369     94   -393       O
ATOM   4509  CB  LYS C  23      -3.901  36.848  24.997  1.00 54.20           C
ANISOU 4509  CB  LYS C  23     6600   7290   6705   -441     22   -445       C
ATOM   4510  N   ASN C  24      -6.179  38.405  23.362  1.00 55.25           N
ANISOU 4510  N   ASN C  24     6839   7307   6848   -380    108   -391       N
ATOM   4511  CA  ASN C  24      -6.933  39.644  23.189  1.00 56.35           C
ANISOU 4511  CA  ASN C  24     7044   7389   6978   -371    157   -385       C
ATOM   4512  C   ASN C  24      -7.691  39.683  21.850  1.00 52.77           C
ANISOU 4512  C   ASN C  24     6605   6902   6542   -330    167   -351       C
ATOM   4513  O   ASN C  24      -7.877  40.750  21.264  1.00 51.13           O
ANISOU 4513  O   ASN C  24     6452   6647   6327   -333    207   -352       O
ATOM   4514  CB  ASN C  24      -6.027  40.876  23.458  1.00 60.07           C
ANISOU 4514  CB  ASN C  24     7558   7840   7427   -432    194   -427       C
ATOM   4515  CG  ASN C  24      -4.582  40.736  22.902  1.00 63.15           C
ANISOU 4515  CG  ASN C  24     7915   8256   7824   -484    186   -459       C
ATOM   4516  OD1 ASN C  24      -4.227  39.762  22.228  1.00 65.71           O
ANISOU 4516  OD1 ASN C  24     8188   8610   8168   -472    157   -448       O
ATOM   4517  ND2 ASN C  24      -3.727  41.704  23.262  1.00 58.96           N
ANISOU 4517  ND2 ASN C  24     7411   7714   7276   -544    213   -500       N
ATOM   4518  N   TYR C  25      -8.095  38.519  21.345  1.00 53.47           N
ANISOU 4518  N   TYR C  25     6650   7015   6651   -294    128   -322       N
ATOM   4519  CA  TYR C  25      -8.883  38.396  20.129  1.00 50.32           C
ANISOU 4519  CA  TYR C  25     6262   6589   6268   -253    125   -287       C
ATOM   4520  C   TYR C  25      -9.800  37.185  20.277  1.00 52.56           C
ANISOU 4520  C   TYR C  25     6501   6899   6571   -208     83   -253       C
ATOM   4521  O   TYR C  25      -9.559  36.298  21.105  1.00 52.64           O
ANISOU 4521  O   TYR C  25     6469   6949   6581   -213     56   -258       O
ATOM   4522  CB  TYR C  25      -8.013  38.211  18.881  1.00 51.21           C
ANISOU 4522  CB  TYR C  25     6373   6701   6383   -272    123   -295       C
ATOM   4523  CG  TYR C  25      -7.171  39.385  18.398  1.00 53.32           C
ANISOU 4523  CG  TYR C  25     6690   6935   6635   -316    170   -325       C
ATOM   4524  CD1 TYR C  25      -5.896  39.622  18.936  1.00 59.21           C
ANISOU 4524  CD1 TYR C  25     7420   7704   7373   -374    182   -367       C
ATOM   4525  CD2 TYR C  25      -7.597  40.196  17.348  1.00 50.02           C
ANISOU 4525  CD2 TYR C  25     6331   6464   6211   -300    200   -311       C
ATOM   4526  CE1 TYR C  25      -5.081  40.674  18.476  1.00 55.19           C
ANISOU 4526  CE1 TYR C  25     6952   7164   6852   -420    228   -396       C
ATOM   4527  CE2 TYR C  25      -6.799  41.251  16.883  1.00 52.72           C
ANISOU 4527  CE2 TYR C  25     6722   6771   6537   -343    248   -339       C
ATOM   4528  CZ  TYR C  25      -5.535  41.483  17.450  1.00 53.80           C
ANISOU 4528  CZ  TYR C  25     6842   6931   6669   -405    264   -382       C
ATOM   4529  OH  TYR C  25      -4.727  42.517  16.995  1.00 54.99           O
ANISOU 4529  OH  TYR C  25     7040   7048   6807   -453    314   -412       O
ATOM   4530  N   THR C  26     -10.829  37.134  19.432  1.00 45.66           N
ANISOU 4530  N   THR C  26     5637   5999   5712   -165     76   -218       N
ATOM   4531  CA  THR C  26     -11.705  35.963  19.287  1.00 55.38           C
ANISOU 4531  CA  THR C  26     6826   7251   6966   -126     35   -184       C
ATOM   4532  C   THR C  26     -11.198  35.013  18.195  1.00 59.43           C
ANISOU 4532  C   THR C  26     7317   7779   7483   -128      1   -178       C
ATOM   4533  O   THR C  26     -11.211  35.345  17.001  1.00 60.80           O
ANISOU 4533  O   THR C  26     7523   7925   7655   -122      5   -169       O
ATOM   4534  CB  THR C  26     -13.147  36.411  19.020  1.00 56.17           C
ANISOU 4534  CB  THR C  26     6942   7316   7083    -78     41   -150       C
ATOM   4535  OG1 THR C  26     -13.683  37.026  20.204  1.00 51.40           O
ANISOU 4535  OG1 THR C  26     6348   6703   6478    -71     72   -153       O
ATOM   4536  CG2 THR C  26     -14.053  35.307  18.448  1.00 58.39           C
ANISOU 4536  CG2 THR C  26     7184   7611   7391    -42     -5   -114       C
ATOM   4537  N   VAL C  27     -10.746  33.830  18.604  1.00 52.81           N
ANISOU 4537  N   VAL C  27     6433   6984   6647   -136    -30   -182       N
ATOM   4538  CA  VAL C  27     -10.095  32.891  17.700  1.00 52.75           C
ANISOU 4538  CA  VAL C  27     6407   6994   6641   -142    -56   -180       C
ATOM   4539  C   VAL C  27     -11.004  31.701  17.446  1.00 50.47           C
ANISOU 4539  C   VAL C  27     6090   6717   6368   -108    -97   -146       C
ATOM   4540  O   VAL C  27     -11.412  31.012  18.385  1.00 49.98           O
ANISOU 4540  O   VAL C  27     5996   6681   6314    -98   -114   -139       O
ATOM   4541  CB  VAL C  27      -8.743  32.418  18.253  1.00 55.78           C
ANISOU 4541  CB  VAL C  27     6761   7417   7016   -176    -60   -211       C
ATOM   4542  CG1 VAL C  27      -8.081  31.496  17.234  1.00 54.00           C
ANISOU 4542  CG1 VAL C  27     6521   7204   6794   -178    -79   -208       C
ATOM   4543  CG2 VAL C  27      -7.848  33.616  18.629  1.00 52.00           C
ANISOU 4543  CG2 VAL C  27     6305   6929   6523   -217    -21   -248       C
ATOM   4544  N   VAL C  28     -11.315  31.450  16.180  1.00 50.08           N
ANISOU 4544  N   VAL C  28     6058   6648   6324    -92   -114   -126       N
ATOM   4545  CA  VAL C  28     -12.068  30.269  15.773  1.00 48.99           C
ANISOU 4545  CA  VAL C  28     5897   6520   6199    -67   -157    -97       C
ATOM   4546  C   VAL C  28     -11.151  29.460  14.855  1.00 48.98           C
ANISOU 4546  C   VAL C  28     5898   6526   6186    -80   -171   -102       C
ATOM   4547  O   VAL C  28     -10.815  29.911  13.747  1.00 47.99           O
ANISOU 4547  O   VAL C  28     5813   6371   6051    -85   -160   -104       O
ATOM   4548  CB  VAL C  28     -13.396  30.639  15.082  1.00 48.96           C
ANISOU 4548  CB  VAL C  28     5911   6482   6209    -34   -170    -65       C
ATOM   4549  CG1 VAL C  28     -14.110  29.407  14.516  1.00 44.18           C
ANISOU 4549  CG1 VAL C  28     5284   5885   5616    -16   -219    -37       C
ATOM   4550  CG2 VAL C  28     -14.330  31.400  16.060  1.00 49.67           C
ANISOU 4550  CG2 VAL C  28     5993   6565   6315    -17   -150    -58       C
ATOM   4551  N   ALA C  29     -10.712  28.283  15.322  1.00 50.33           N
ANISOU 4551  N   ALA C  29     6033   6733   6358    -84   -191   -106       N
ATOM   4552  CA  ALA C  29      -9.792  27.422  14.572  1.00 48.82           C
ANISOU 4552  CA  ALA C  29     5842   6551   6158    -93   -201   -111       C
ATOM   4553  C   ALA C  29     -10.399  26.029  14.412  1.00 50.43           C
ANISOU 4553  C   ALA C  29     6027   6767   6366    -73   -242    -86       C
ATOM   4554  O   ALA C  29     -10.088  25.104  15.175  1.00 53.76           O
ANISOU 4554  O   ALA C  29     6417   7222   6789    -73   -254    -90       O
ATOM   4555  CB  ALA C  29      -8.419  27.361  15.235  1.00 41.74           C
ANISOU 4555  CB  ALA C  29     4920   5686   5255   -118   -183   -143       C
ATOM   4556  N   PRO C  30     -11.247  25.833  13.418  1.00 51.87           N
ANISOU 4556  N   PRO C  30     6234   6922   6551    -57   -264    -61       N
ATOM   4557  CA  PRO C  30     -11.854  24.512  13.213  1.00 56.14           C
ANISOU 4557  CA  PRO C  30     6762   7471   7096    -44   -304    -38       C
ATOM   4558  C   PRO C  30     -10.814  23.470  12.850  1.00 58.37           C
ANISOU 4558  C   PRO C  30     7046   7767   7364    -52   -307    -46       C
ATOM   4559  O   PRO C  30      -9.643  23.757  12.608  1.00 57.16           O
ANISOU 4559  O   PRO C  30     6901   7616   7200    -66   -280    -68       O
ATOM   4560  CB  PRO C  30     -12.857  24.723  12.068  1.00 55.90           C
ANISOU 4560  CB  PRO C  30     6766   7405   7070    -30   -329    -13       C
ATOM   4561  CG  PRO C  30     -12.681  26.162  11.621  1.00 52.84           C
ANISOU 4561  CG  PRO C  30     6414   6988   6676    -33   -299    -22       C
ATOM   4562  CD  PRO C  30     -11.417  26.700  12.243  1.00 49.71           C
ANISOU 4562  CD  PRO C  30     6009   6607   6270    -55   -256    -55       C
ATOM   4563  N   THR C  31     -11.253  22.224  12.915  1.00 66.58           N
ANISOU 4563  N   THR C  31     8074   8818   8405    -42   -338    -30       N
ATOM   4564  CA  THR C  31     -10.487  21.083  12.451  1.00 70.54           C
ANISOU 4564  CA  THR C  31     8583   9326   8892    -43   -344    -31       C
ATOM   4565  C   THR C  31     -10.825  20.778  10.990  1.00 74.54           C
ANISOU 4565  C   THR C  31     9139   9797   9387    -40   -363    -14       C
ATOM   4566  O   THR C  31     -11.686  21.414  10.376  1.00 75.66           O
ANISOU 4566  O   THR C  31     9304   9910   9531    -37   -377     -0       O
ATOM   4567  CB  THR C  31     -10.765  19.881  13.340  1.00 71.70           C
ANISOU 4567  CB  THR C  31     8700   9500   9042    -35   -365    -22       C
ATOM   4568  OG1 THR C  31     -12.067  19.375  13.035  1.00 71.67           O
ANISOU 4568  OG1 THR C  31     8703   9482   9048    -29   -398      4       O
ATOM   4569  CG2 THR C  31     -10.717  20.307  14.799  1.00 66.29           C
ANISOU 4569  CG2 THR C  31     7977   8843   8366    -36   -351    -35       C
ATOM   4570  N   HIS C  32     -10.119  19.799  10.419  1.00 77.70           N
ANISOU 4570  N   HIS C  32     9557  10194   9770    -40   -363    -15       N
ATOM   4571  CA  HIS C  32     -10.353  19.418   9.028  1.00 85.16           C
ANISOU 4571  CA  HIS C  32    10558  11102  10697    -39   -380     -0       C
ATOM   4572  C   HIS C  32     -11.777  18.901   8.820  1.00 83.60           C
ANISOU 4572  C   HIS C  32    10366  10892  10505    -34   -429     27       C
ATOM   4573  O   HIS C  32     -12.429  19.234   7.819  1.00 80.99           O
ANISOU 4573  O   HIS C  32    10076  10528  10167    -34   -451     41       O
ATOM   4574  CB  HIS C  32      -9.322  18.355   8.612  1.00 86.73           C
ANISOU 4574  CB  HIS C  32    10774  11301  10877    -38   -366     -6       C
ATOM   4575  CG  HIS C  32      -9.351  17.997   7.153  1.00 90.86           C
ANISOU 4575  CG  HIS C  32    11366  11782  11375    -39   -374      5       C
ATOM   4576  ND1 HIS C  32     -10.453  17.434   6.538  1.00 88.02           N
ANISOU 4576  ND1 HIS C  32    11038  11399  11006    -38   -419     29       N
ATOM   4577  CD2 HIS C  32      -8.401  18.101   6.193  1.00 93.13           C
ANISOU 4577  CD2 HIS C  32    11698  12045  11644    -42   -340     -5       C
ATOM   4578  CE1 HIS C  32     -10.186  17.221   5.263  1.00 90.51           C
ANISOU 4578  CE1 HIS C  32    11421  11675  11294    -40   -417     33       C
ATOM   4579  NE2 HIS C  32      -8.947  17.616   5.027  1.00 97.64           N
ANISOU 4579  NE2 HIS C  32    12335  12575  12190    -42   -366     13       N
ATOM   4580  N   GLY C  33     -12.294  18.125   9.778  1.00 80.45           N
ANISOU 4580  N   GLY C  33     9927  10520  10120    -32   -446     35       N
ATOM   4581  CA  GLY C  33     -13.643  17.603   9.652  1.00 78.03           C
ANISOU 4581  CA  GLY C  33     9618  10205   9826    -32   -490     59       C
ATOM   4582  C   GLY C  33     -14.729  18.651   9.778  1.00 78.41           C
ANISOU 4582  C   GLY C  33     9646  10246   9898    -27   -503     69       C
ATOM   4583  O   GLY C  33     -15.754  18.565   9.093  1.00 74.27           O
ANISOU 4583  O   GLY C  33     9135   9703   9381    -27   -543     89       O
ATOM   4584  N   GLU C  34     -14.510  19.669  10.622  1.00 77.85           N
ANISOU 4584  N   GLU C  34     9547  10191   9842    -23   -471     55       N
ATOM   4585  CA  GLU C  34     -15.517  20.706  10.846  1.00 75.54           C
ANISOU 4585  CA  GLU C  34     9236   9892   9574    -14   -476     65       C
ATOM   4586  C   GLU C  34     -15.694  21.616   9.638  1.00 73.10           C
ANISOU 4586  C   GLU C  34     8973   9547   9255     -8   -485     71       C
ATOM   4587  O   GLU C  34     -16.799  22.123   9.401  1.00 71.88           O
ANISOU 4587  O   GLU C  34     8812   9379   9120      4   -511     89       O
ATOM   4588  CB  GLU C  34     -15.141  21.552  12.059  1.00 68.70           C
ANISOU 4588  CB  GLU C  34     8338   9046   8718    -13   -435     47       C
ATOM   4589  CG  GLU C  34     -15.052  20.783  13.347  1.00 69.20           C
ANISOU 4589  CG  GLU C  34     8361   9143   8789    -15   -427     42       C
ATOM   4590  CD  GLU C  34     -14.695  21.686  14.506  1.00 75.53           C
ANISOU 4590  CD  GLU C  34     9141   9961   9595    -15   -389     23       C
ATOM   4591  OE1 GLU C  34     -15.540  22.542  14.855  1.00 79.09           O
ANISOU 4591  OE1 GLU C  34     9580  10405  10068     -7   -381     30       O
ATOM   4592  OE2 GLU C  34     -13.581  21.547  15.065  1.00 68.87           O
ANISOU 4592  OE2 GLU C  34     8294   9139   8737    -23   -369      2       O
ATOM   4593  N   LEU C  35     -14.626  21.839   8.875  1.00 74.49           N
ANISOU 4593  N   LEU C  35     9195   9705   9402    -15   -464     57       N
ATOM   4594  CA  LEU C  35     -14.644  22.819   7.796  1.00 70.17           C
ANISOU 4594  CA  LEU C  35     8701   9120   8841    -10   -462     59       C
ATOM   4595  C   LEU C  35     -13.776  22.314   6.650  1.00 72.01           C
ANISOU 4595  C   LEU C  35     8993   9328   9038    -19   -457     54       C
ATOM   4596  O   LEU C  35     -12.550  22.484   6.664  1.00 68.27           O
ANISOU 4596  O   LEU C  35     8531   8857   8551    -29   -413     32       O
ATOM   4597  CB  LEU C  35     -14.137  24.146   8.328  1.00 63.00           C
ANISOU 4597  CB  LEU C  35     7788   8212   7936    -10   -414     40       C
ATOM   4598  CG  LEU C  35     -14.674  25.391   7.654  1.00 60.35           C
ANISOU 4598  CG  LEU C  35     7491   7840   7598      3   -415     49       C
ATOM   4599  CD1 LEU C  35     -16.176  25.411   7.726  1.00 66.67           C
ANISOU 4599  CD1 LEU C  35     8268   8640   8425     24   -460     77       C
ATOM   4600  CD2 LEU C  35     -14.090  26.591   8.355  1.00 58.51           C
ANISOU 4600  CD2 LEU C  35     7253   7610   7368     -2   -362     27       C
ATOM   4601  N   ASP C  36     -14.415  21.735   5.640  1.00 70.87           N
ANISOU 4601  N   ASP C  36     8889   9159   8880    -17   -503     74       N
ATOM   4602  CA  ASP C  36     -13.686  21.193   4.504  1.00 72.65           C
ANISOU 4602  CA  ASP C  36     9180   9355   9068    -25   -498     71       C
ATOM   4603  C   ASP C  36     -13.530  22.274   3.447  1.00 73.09           C
ANISOU 4603  C   ASP C  36     9305   9367   9101    -20   -486     71       C
ATOM   4604  O   ASP C  36     -14.523  22.750   2.885  1.00 72.49           O
ANISOU 4604  O   ASP C  36     9253   9267   9024     -8   -526     90       O
ATOM   4605  CB  ASP C  36     -14.372  19.963   3.916  1.00 74.70           C
ANISOU 4605  CB  ASP C  36     9460   9604   9317    -28   -553     91       C
ATOM   4606  CG  ASP C  36     -13.451  19.172   2.981  1.00 75.00           C
ANISOU 4606  CG  ASP C  36     9563   9617   9317    -37   -537     85       C
ATOM   4607  OD1 ASP C  36     -12.802  19.788   2.102  1.00 65.25           O
ANISOU 4607  OD1 ASP C  36     8390   8348   8055    -37   -509     77       O
ATOM   4608  OD2 ASP C  36     -13.365  17.930   3.134  1.00 83.35           O
ANISOU 4608  OD2 ASP C  36    10614  10685  10369    -43   -549     88       O
ATOM   4609  N   LEU C  37     -12.275  22.655   3.190  1.00 73.52           N
ANISOU 4609  N   LEU C  37     9388   9410   9137    -30   -428     49       N
ATOM   4610  CA  LEU C  37     -11.949  23.734   2.265  1.00 69.55           C
ANISOU 4610  CA  LEU C  37     8954   8862   8610    -29   -401     44       C
ATOM   4611  C   LEU C  37     -12.205  23.344   0.815  1.00 71.55           C
ANISOU 4611  C   LEU C  37     9296   9066   8824    -26   -432     60       C
ATOM   4612  O   LEU C  37     -12.257  24.226  -0.052  1.00 73.37           O
ANISOU 4612  O   LEU C  37     9595   9254   9031    -20   -424     64       O
ATOM   4613  CB  LEU C  37     -10.496  24.146   2.465  1.00 65.90           C
ANISOU 4613  CB  LEU C  37     8491   8405   8144    -45   -328     14       C
ATOM   4614  CG  LEU C  37     -10.210  25.034   3.677  1.00 64.84           C
ANISOU 4614  CG  LEU C  37     8294   8303   8039    -51   -293     -4       C
ATOM   4615  CD1 LEU C  37     -10.523  24.382   5.026  1.00 60.87           C
ANISOU 4615  CD1 LEU C  37     7706   7854   7568    -49   -314     -4       C
ATOM   4616  CD2 LEU C  37      -8.743  25.465   3.628  1.00 61.23           C
ANISOU 4616  CD2 LEU C  37     7845   7843   7576    -72   -224    -35       C
ATOM   4617  N   THR C  38     -12.316  22.040   0.525  1.00 77.52           N
ANISOU 4617  N   THR C  38    10059   9825   9569    -30   -463     70       N
ATOM   4618  CA  THR C  38     -12.716  21.585  -0.804  1.00 74.65           C
ANISOU 4618  CA  THR C  38     9783   9415   9166    -29   -503     87       C
ATOM   4619  C   THR C  38     -14.226  21.653  -1.022  1.00 72.86           C
ANISOU 4619  C   THR C  38     9553   9182   8947    -17   -583    113       C
ATOM   4620  O   THR C  38     -14.670  21.383  -2.142  1.00 71.10           O
ANISOU 4620  O   THR C  38     9405   8920   8691    -16   -627    129       O
ATOM   4621  CB  THR C  38     -12.239  20.157  -1.073  1.00 64.65           C
ANISOU 4621  CB  THR C  38     8534   8149   7881    -40   -503     86       C
ATOM   4622  OG1 THR C  38     -12.626  19.331   0.025  1.00 62.24           O
ANISOU 4622  OG1 THR C  38     8146   7893   7610    -42   -526     89       O
ATOM   4623  CG2 THR C  38     -10.727  20.126  -1.249  1.00 63.66           C
ANISOU 4623  CG2 THR C  38     8432   8015   7741    -47   -425     63       C
ATOM   4624  N   ASP C  39     -15.019  21.985   0.011  1.00 73.38           N
ANISOU 4624  N   ASP C  39     9537   9287   9058     -8   -604    119       N
ATOM   4625  CA  ASP C  39     -16.479  22.147  -0.099  1.00 77.12           C
ANISOU 4625  CA  ASP C  39     9992   9760   9550      5   -676    144       C
ATOM   4626  C   ASP C  39     -16.784  23.650  -0.177  1.00 76.48           C
ANISOU 4626  C   ASP C  39     9923   9660   9474     27   -665    148       C
ATOM   4627  O   ASP C  39     -16.708  24.379   0.828  1.00 74.68           O
ANISOU 4627  O   ASP C  39     9638   9459   9279     34   -628    138       O
ATOM   4628  CB  ASP C  39     -17.198  21.458   1.068  1.00 81.88           C
ANISOU 4628  CB  ASP C  39    10498  10413  10199      2   -700    150       C
ATOM   4629  CG  ASP C  39     -18.734  21.439   0.915  1.00 79.07           C
ANISOU 4629  CG  ASP C  39    10116  10059   9870     13   -777    177       C
ATOM   4630  OD1 ASP C  39     -19.250  22.053  -0.042  1.00 77.00           O
ANISOU 4630  OD1 ASP C  39     9906   9762   9590     27   -816    191       O
ATOM   4631  OD2 ASP C  39     -19.427  20.802   1.752  1.00 76.24           O
ANISOU 4631  OD2 ASP C  39     9681   9736   9549      7   -800    184       O
ATOM   4632  N   ARG C  40     -17.135  24.104  -1.385  1.00 81.11           N
ANISOU 4632  N   ARG C  40    10591  10199  10027     39   -698    162       N
ATOM   4633  CA  ARG C  40     -17.344  25.529  -1.614  1.00 79.34           C
ANISOU 4633  CA  ARG C  40    10398   9949   9800     63   -685    165       C
ATOM   4634  C   ARG C  40     -18.422  26.106  -0.740  1.00 73.60           C
ANISOU 4634  C   ARG C  40     9590   9251   9123     86   -711    179       C
ATOM   4635  O   ARG C  40     -18.231  27.113  -0.046  1.00 73.66           O
ANISOU 4635  O   ARG C  40     9573   9266   9149     96   -663    169       O
ATOM   4636  CB  ARG C  40     -17.823  25.761  -3.034  1.00 81.13           C
ANISOU 4636  CB  ARG C  40    10723  10121   9983     77   -737    184       C
ATOM   4637  CG  ARG C  40     -18.300  27.260  -3.236  1.00 79.34           C
ANISOU 4637  CG  ARG C  40    10524   9866   9755    110   -736    195       C
ATOM   4638  CD  ARG C  40     -18.481  27.564  -4.743  1.00 81.09           C
ANISOU 4638  CD  ARG C  40    10867  10024   9919    124   -774    210       C
ATOM   4639  NE  ARG C  40     -19.163  28.815  -5.092  1.00 82.41           N
ANISOU 4639  NE  ARG C  40    11069  10161  10082    162   -795    227       N
ATOM   4640  CZ  ARG C  40     -18.971  29.381  -6.278  1.00 87.06           C
ANISOU 4640  CZ  ARG C  40    11777  10687  10614    174   -798    233       C
ATOM   4641  NH1 ARG C  40     -18.079  28.843  -7.070  1.00 90.18           N
ANISOU 4641  NH1 ARG C  40    12255  11050  10960    148   -771    220       N
ATOM   4642  NH2 ARG C  40     -19.537  30.549  -6.613  1.00 89.32           N
ANISOU 4642  NH2 ARG C  40    12103  10941  10892    212   -814    248       N
ATOM   4643  N   GLU C  41     -19.588  25.483  -0.819  1.00 72.59           N
ANISOU 4643  N   GLU C  41     9427   9138   9017     93   -787    201       N
ATOM   4644  CA  GLU C  41     -20.750  25.951  -0.105  1.00 71.01           C
ANISOU 4644  CA  GLU C  41     9149   8963   8869    117   -817    218       C
ATOM   4645  C   GLU C  41     -20.450  25.997   1.390  1.00 66.69           C
ANISOU 4645  C   GLU C  41     8515   8461   8363    109   -759    202       C
ATOM   4646  O   GLU C  41     -20.715  27.004   2.062  1.00 63.05           O
ANISOU 4646  O   GLU C  41     8021   8007   7928    131   -731    202       O
ATOM   4647  CB  GLU C  41     -21.935  25.020  -0.414  1.00 73.89           C
ANISOU 4647  CB  GLU C  41     9480   9340   9254    115   -906    242       C
ATOM   4648  CG  GLU C  41     -22.492  24.967  -1.892  1.00 75.00           C
ANISOU 4648  CG  GLU C  41     9703   9438   9357    125   -984    262       C
ATOM   4649  CD  GLU C  41     -21.862  23.888  -2.828  1.00 77.47           C
ANISOU 4649  CD  GLU C  41    10094   9725   9615     93  -1001    255       C
ATOM   4650  OE1 GLU C  41     -20.790  23.299  -2.523  1.00 78.37           O
ANISOU 4650  OE1 GLU C  41    10217   9847   9713     68   -942    234       O
ATOM   4651  OE2 GLU C  41     -22.537  23.537  -3.829  1.00 75.60           O
ANISOU 4651  OE2 GLU C  41     9905   9463   9356     94  -1079    273       O
ATOM   4652  N   LYS C  42     -19.841  24.925   1.915  1.00 70.24           N
ANISOU 4652  N   LYS C  42     8936   8940   8814     80   -739    187       N
ATOM   4653  CA  LYS C  42     -19.632  24.815   3.354  1.00 72.05           C
ANISOU 4653  CA  LYS C  42     9084   9212   9079     73   -695    173       C
ATOM   4654  C   LYS C  42     -18.726  25.928   3.879  1.00 67.21           C
ANISOU 4654  C   LYS C  42     8482   8596   8459     76   -621    151       C
ATOM   4655  O   LYS C  42     -19.012  26.540   4.917  1.00 64.73           O
ANISOU 4655  O   LYS C  42     8114   8303   8178     86   -594    148       O
ATOM   4656  CB  LYS C  42     -19.058  23.433   3.682  1.00 69.81           C
ANISOU 4656  CB  LYS C  42     8782   8953   8789     44   -689    162       C
ATOM   4657  N   ILE C  43     -17.670  26.257   3.148  1.00 63.16           N
ANISOU 4657  N   ILE C  43     8040   8052   7904     66   -586    136       N
ATOM   4658  CA  ILE C  43     -16.755  27.260   3.674  1.00 62.72           C
ANISOU 4658  CA  ILE C  43     7991   7995   7845     61   -515    112       C
ATOM   4659  C   ILE C  43     -17.404  28.645   3.628  1.00 60.92           C
ANISOU 4659  C   ILE C  43     7780   7743   7625     89   -511    122       C
ATOM   4660  O   ILE C  43     -17.268  29.439   4.570  1.00 57.33           O
ANISOU 4660  O   ILE C  43     7294   7301   7189     92   -466    110       O
ATOM   4661  CB  ILE C  43     -15.400  27.212   2.928  1.00 59.50           C
ANISOU 4661  CB  ILE C  43     7651   7563   7395     39   -472     91       C
ATOM   4662  CG1 ILE C  43     -14.349  28.064   3.640  1.00 54.34           C
ANISOU 4662  CG1 ILE C  43     6987   6917   6743     24   -398     62       C
ATOM   4663  CG2 ILE C  43     -15.519  27.610   1.456  1.00 63.78           C
ANISOU 4663  CG2 ILE C  43     8289   8049   7897     50   -492    103       C
ATOM   4664  CD1 ILE C  43     -13.986  27.554   4.987  1.00 52.59           C
ANISOU 4664  CD1 ILE C  43     6684   6747   6549     10   -378     46       C
ATOM   4665  N   ILE C  44     -18.187  28.927   2.581  1.00 63.73           N
ANISOU 4665  N   ILE C  44     8185   8063   7967    113   -560    146       N
ATOM   4666  CA  ILE C  44     -18.738  30.272   2.404  1.00 63.64           C
ANISOU 4666  CA  ILE C  44     8202   8022   7957    145   -554    157       C
ATOM   4667  C   ILE C  44     -19.690  30.703   3.516  1.00 63.44           C
ANISOU 4667  C   ILE C  44     8096   8024   7982    168   -556    167       C
ATOM   4668  O   ILE C  44     -19.551  31.815   4.047  1.00 65.32           O
ANISOU 4668  O   ILE C  44     8340   8254   8226    180   -507    158       O
ATOM   4669  CB  ILE C  44     -19.407  30.394   1.033  1.00 61.72           C
ANISOU 4669  CB  ILE C  44     8028   7735   7687    169   -616    182       C
ATOM   4670  CG1 ILE C  44     -18.335  30.442  -0.036  1.00 60.26           C
ANISOU 4670  CG1 ILE C  44     7944   7507   7445    150   -587    168       C
ATOM   4671  CG2 ILE C  44     -20.264  31.660   0.987  1.00 54.09           C
ANISOU 4671  CG2 ILE C  44     7074   6745   6733    212   -624    200       C
ATOM   4672  CD1 ILE C  44     -18.891  30.583  -1.404  1.00 64.48           C
ANISOU 4672  CD1 ILE C  44     8563   7994   7943    172   -645    191       C
ATOM   4673  N   SER C  45     -20.722  29.912   3.826  1.00 72.23           N
ANISOU 4673  N   SER C  45     9142   9167   9133    177   -611    187       N
ATOM   4674  CA  SER C  45     -21.668  30.384   4.854  1.00 72.62           C
ANISOU 4674  CA  SER C  45     9119   9240   9234    202   -606    198       C
ATOM   4675  C   SER C  45     -20.995  30.544   6.166  1.00 71.32           C
ANISOU 4675  C   SER C  45     8914   9102   9081    183   -538    173       C
ATOM   4676  O   SER C  45     -21.435  31.289   7.035  1.00 68.47           O
ANISOU 4676  O   SER C  45     8519   8749   8749    202   -507    174       O
ATOM   4677  CB  SER C  45     -22.867  29.396   4.982  1.00 75.54           C
ANISOU 4677  CB  SER C  45     9416   9639   9646    208   -673    222       C
ATOM   4678  OG  SER C  45     -22.460  28.023   5.126  1.00 76.97           O
ANISOU 4678  OG  SER C  45     9575   9847   9822    171   -686    212       O
ATOM   4679  N   GLU C  46     -20.148  29.606   6.387  1.00 65.23           N
ANISOU 4679  N   GLU C  46     8135   8354   8296    148   -526    154       N
ATOM   4680  CA  GLU C  46     -19.586  29.341   7.686  1.00 62.59           C
ANISOU 4680  CA  GLU C  46     7751   8055   7976    127   -479    133       C
ATOM   4681  C   GLU C  46     -18.319  30.131   7.980  1.00 61.97           C
ANISOU 4681  C   GLU C  46     7709   7967   7870    108   -413    102       C
ATOM   4682  O   GLU C  46     -18.022  30.369   9.150  1.00 56.13           O
ANISOU 4682  O   GLU C  46     6934   7251   7143     98   -371     85       O
ATOM   4683  CB  GLU C  46     -19.659  27.833   7.871  1.00 63.56           C
ANISOU 4683  CB  GLU C  46     7832   8211   8108    107   -513    136       C
ATOM   4684  CG  GLU C  46     -19.043  26.767   8.942  1.00 68.21           C
ANISOU 4684  CG  GLU C  46     8372   8841   8702     79   -492    118       C
ATOM   4685  CD  GLU C  46     -19.269  26.923  10.267  1.00 67.83           C
ANISOU 4685  CD  GLU C  46     8272   8819   8681     81   -461    112       C
ATOM   4686  OE1 GLU C  46     -19.699  27.401  11.309  1.00 64.92           O
ANISOU 4686  OE1 GLU C  46     7865   8463   8338     91   -434    111       O
ATOM   4687  OE2 GLU C  46     -20.488  26.734   9.690  1.00 69.38           O
ANISOU 4687  OE2 GLU C  46     8453   9006   8901    100   -513    140       O
ATOM   4688  N   VAL C  47     -17.613  30.617   6.930  1.00 62.03           N
ANISOU 4688  N   VAL C  47     7791   7938   7839    102   -400     94       N
ATOM   4689  CA  VAL C  47     -16.877  31.911   7.016  1.00 59.89           C
ANISOU 4689  CA  VAL C  47     7566   7641   7549     96   -339     73       C
ATOM   4690  C   VAL C  47     -17.810  33.128   7.275  1.00 63.70           C
ANISOU 4690  C   VAL C  47     8054   8101   8048    132   -331     88       C
ATOM   4691  O   VAL C  47     -17.431  34.082   7.976  1.00 59.96           O
ANISOU 4691  O   VAL C  47     7588   7621   7573    126   -276     70       O
ATOM   4692  CB  VAL C  47     -16.093  32.148   5.695  1.00 57.01           C
ANISOU 4692  CB  VAL C  47     7287   7234   7140     85   -329     67       C
ATOM   4693  CG1 VAL C  47     -15.738  33.686   5.417  1.00 51.20           C
ANISOU 4693  CG1 VAL C  47     6619   6453   6382     90   -277     56       C
ATOM   4694  CG2 VAL C  47     -14.962  31.194   5.517  1.00 54.69           C
ANISOU 4694  CG2 VAL C  47     6993   6957   6829     50   -317     47       C
ATOM   4695  N   THR C  48     -18.981  33.190   6.595  1.00 61.38           N
ANISOU 4695  N   THR C  48     7767   7789   7766    169   -384    121       N
ATOM   4696  CA  THR C  48     -19.931  34.318   6.781  1.00 58.39           C
ANISOU 4696  CA  THR C  48     7392   7389   7407    212   -378    139       C
ATOM   4697  C   THR C  48     -20.584  34.318   8.168  1.00 59.69           C
ANISOU 4697  C   THR C  48     7476   7587   7616    222   -361    141       C
ATOM   4698  O   THR C  48     -20.952  35.386   8.692  1.00 56.14           O
ANISOU 4698  O   THR C  48     7032   7122   7179    246   -325    143       O
ATOM   4699  CB  THR C  48     -21.036  34.298   5.710  1.00 58.63           C
ANISOU 4699  CB  THR C  48     7440   7396   7442    252   -448    174       C
ATOM   4700  OG1 THR C  48     -20.443  34.107   4.426  1.00 58.24           O
ANISOU 4700  OG1 THR C  48     7468   7315   7347    239   -467    172       O
ATOM   4701  CG2 THR C  48     -21.872  35.623   5.688  1.00 53.33           C
ANISOU 4701  CG2 THR C  48     6789   6691   6783    302   -438    193       C
ATOM   4702  N   LYS C  49     -20.738  33.132   8.763  1.00 59.53           N
ANISOU 4702  N   LYS C  49     7388   7610   7620    204   -384    141       N
ATOM   4703  CA  LYS C  49     -21.320  33.030  10.095  1.00 59.54           C
ANISOU 4703  CA  LYS C  49     7319   7643   7662    211   -364    143       C
ATOM   4704  C   LYS C  49     -20.349  33.525  11.156  1.00 58.39           C
ANISOU 4704  C   LYS C  49     7180   7504   7500    184   -295    110       C
ATOM   4705  O   LYS C  49     -20.723  34.332  12.020  1.00 55.54           O
ANISOU 4705  O   LYS C  49     6809   7139   7156    201   -255    109       O
ATOM   4706  CB  LYS C  49     -21.727  31.586  10.389  1.00 60.49           C
ANISOU 4706  CB  LYS C  49     7374   7803   7808    197   -405    151       C
ATOM   4707  CG  LYS C  49     -22.416  31.417  11.753  1.00 59.95           C
ANISOU 4707  CG  LYS C  49     7234   7762   7781    204   -382    155       C
ATOM   4708  CD  LYS C  49     -23.139  30.093  11.845  1.00 60.14           C
ANISOU 4708  CD  LYS C  49     7197   7817   7837    198   -430    171       C
ATOM   4709  CE  LYS C  49     -24.037  29.920  10.638  1.00 57.70           C
ANISOU 4709  CE  LYS C  49     6889   7493   7542    220   -498    200       C
ATOM   4710  NZ  LYS C  49     -24.827  28.676  10.710  1.00 56.80           N
ANISOU 4710  NZ  LYS C  49     6714   7407   7462    210   -545    216       N
ATOM   4711  N   ILE C  50     -19.102  33.030  11.122  1.00 63.16           N
ANISOU 4711  N   ILE C  50     7802   8122   8075    144   -281     83       N
ATOM   4712  CA  ILE C  50     -18.066  33.504  12.045  1.00 59.78           C
ANISOU 4712  CA  ILE C  50     7382   7702   7630    114   -223     50       C
ATOM   4713  C   ILE C  50     -17.766  34.976  11.800  1.00 58.11           C
ANISOU 4713  C   ILE C  50     7233   7448   7397    119   -178     39       C
ATOM   4714  O   ILE C  50     -17.415  35.704  12.736  1.00 53.53           O
ANISOU 4714  O   ILE C  50     6658   6868   6813    107   -128     19       O
ATOM   4715  CB  ILE C  50     -16.786  32.652  11.912  1.00 58.95           C
ANISOU 4715  CB  ILE C  50     7279   7619   7500     72   -223     26       C
ATOM   4716  CG1 ILE C  50     -17.075  31.178  12.192  1.00 60.77           C
ANISOU 4716  CG1 ILE C  50     7454   7888   7748     68   -264     36       C
ATOM   4717  CG2 ILE C  50     -15.689  33.156  12.848  1.00 53.00           C
ANISOU 4717  CG2 ILE C  50     6530   6878   6731     40   -169    -10       C
ATOM   4718  CD1 ILE C  50     -16.017  30.235  11.604  1.00 58.67           C
ANISOU 4718  CD1 ILE C  50     7200   7635   7458     40   -277     23       C
ATOM   4719  N   ASN C  51     -17.891  35.416  10.542  1.00 59.63           N
ANISOU 4719  N   ASN C  51     7481   7602   7572    136   -194     53       N
ATOM   4720  CA  ASN C  51     -17.616  36.780  10.093  1.00 61.84           C
ANISOU 4720  CA  ASN C  51     7835   7834   7827    142   -153     45       C
ATOM   4721  C   ASN C  51     -16.254  37.297  10.553  1.00 64.07           C
ANISOU 4721  C   ASN C  51     8146   8116   8083     95    -93      5       C
ATOM   4722  O   ASN C  51     -16.170  38.365  11.200  1.00 59.10           O
ANISOU 4722  O   ASN C  51     7539   7468   7449     93    -44     -9       O
ATOM   4723  CB  ASN C  51     -18.738  37.710  10.537  1.00 63.57           C
ANISOU 4723  CB  ASN C  51     8052   8034   8070    188   -141     66       C
ATOM   4724  CG  ASN C  51     -18.710  39.048   9.824  1.00 60.15           C
ANISOU 4724  CG  ASN C  51     7702   7542   7609    207   -112     68       C
ATOM   4725  OD1 ASN C  51     -18.892  39.116   8.610  1.00 64.51           O
ANISOU 4725  OD1 ASN C  51     8301   8065   8144    226   -144     85       O
ATOM   4726  ND2 ASN C  51     -18.504  40.120  10.579  1.00 60.92           N
ANISOU 4726  ND2 ASN C  51     7826   7621   7700    204    -51     51       N
ATOM   4727  N   PRO C  52     -15.156  36.627  10.183  1.00 59.69           N
ANISOU 4727  N   PRO C  52     7594   7576   7510     56    -93    -15       N
ATOM   4728  CA  PRO C  52     -13.833  37.038  10.671  1.00 57.42           C
ANISOU 4728  CA  PRO C  52     7319   7294   7203      8    -40    -55       C
ATOM   4729  C   PRO C  52     -13.361  38.324  10.019  1.00 57.62           C
ANISOU 4729  C   PRO C  52     7427   7267   7201     -1      8    -68       C
ATOM   4730  O   PRO C  52     -13.565  38.545   8.823  1.00 58.97           O
ANISOU 4730  O   PRO C  52     7653   7398   7354     17     -3    -52       O
ATOM   4731  CB  PRO C  52     -12.931  35.866  10.277  1.00 53.71           C
ANISOU 4731  CB  PRO C  52     6826   6853   6728    -20    -59    -66       C
ATOM   4732  CG  PRO C  52     -13.587  35.311   9.055  1.00 56.21           C
ANISOU 4732  CG  PRO C  52     7166   7151   7041      9   -107    -36       C
ATOM   4733  CD  PRO C  52     -15.067  35.429   9.325  1.00 55.03           C
ANISOU 4733  CD  PRO C  52     6994   7000   6917     54   -142     -3       C
ATOM   4734  N   GLN C  53     -12.752  39.196  10.825  1.00 58.43           N
ANISOU 4734  N   GLN C  53     7541   7365   7296    -31     61    -97       N
ATOM   4735  CA  GLN C  53     -12.049  40.331  10.243  1.00 55.95           C
ANISOU 4735  CA  GLN C  53     7304   7002   6952    -54    114   -117       C
ATOM   4736  C   GLN C  53     -10.729  39.889   9.630  1.00 55.74           C
ANISOU 4736  C   GLN C  53     7285   6982   6911   -100    130   -142       C
ATOM   4737  O   GLN C  53     -10.355  40.373   8.552  1.00 54.73           O
ANISOU 4737  O   GLN C  53     7226   6810   6759   -107    154   -144       O
ATOM   4738  CB  GLN C  53     -11.843  41.420  11.300  1.00 50.81           C
ANISOU 4738  CB  GLN C  53     6667   6340   6297    -74    167   -141       C
ATOM   4739  CG  GLN C  53     -13.133  42.173  11.564  1.00 54.57           C
ANISOU 4739  CG  GLN C  53     7166   6787   6781    -22    168   -114       C
ATOM   4740  CD  GLN C  53     -14.053  41.417  12.493  1.00 58.67           C
ANISOU 4740  CD  GLN C  53     7610   7349   7334      8    130    -94       C
ATOM   4741  OE1 GLN C  53     -13.632  40.969  13.558  1.00 57.32           O
ANISOU 4741  OE1 GLN C  53     7389   7219   7171    -21    134   -114       O
ATOM   4742  NE2 GLN C  53     -15.302  41.200  12.059  1.00 59.30           N
ANISOU 4742  NE2 GLN C  53     7679   7420   7433     65     90    -54       N
ATOM   4743  N   ILE C  54     -10.059  38.915  10.244  1.00 49.56           N
ANISOU 4743  N   ILE C  54     6434   6254   6144   -128    115   -159       N
ATOM   4744  CA  ILE C  54      -8.759  38.479   9.776  1.00 45.73           C
ANISOU 4744  CA  ILE C  54     5944   5780   5651   -171    133   -185       C
ATOM   4745  C   ILE C  54      -8.797  36.963   9.614  1.00 49.38           C
ANISOU 4745  C   ILE C  54     6350   6284   6127   -158     82   -170       C
ATOM   4746  O   ILE C  54      -9.372  36.258  10.452  1.00 51.67           O
ANISOU 4746  O   ILE C  54     6583   6614   6437   -141     44   -158       O
ATOM   4747  CB  ILE C  54      -7.665  38.855  10.789  1.00 45.10           C
ANISOU 4747  CB  ILE C  54     5833   5727   5575   -224    173   -227       C
ATOM   4748  CG1 ILE C  54      -7.702  40.349  11.169  1.00 46.13           C
ANISOU 4748  CG1 ILE C  54     6018   5819   5692   -240    224   -243       C
ATOM   4749  CG2 ILE C  54      -6.332  38.506  10.214  1.00 44.04           C
ANISOU 4749  CG2 ILE C  54     5693   5601   5438   -266    197   -252       C
ATOM   4750  CD1 ILE C  54      -7.559  41.364  10.042  1.00 47.01           C
ANISOU 4750  CD1 ILE C  54     6220   5863   5776   -244    268   -244       C
ATOM   4751  N   ILE C  55      -8.196  36.452   8.542  1.00 45.58           N
ANISOU 4751  N   ILE C  55     5892   5791   5634   -167     83   -170       N
ATOM   4752  CA  ILE C  55      -8.055  35.010   8.338  1.00 43.73           C
ANISOU 4752  CA  ILE C  55     5614   5593   5410   -160     42   -160       C
ATOM   4753  C   ILE C  55      -6.580  34.674   8.203  1.00 42.16           C
ANISOU 4753  C   ILE C  55     5397   5411   5211   -202     77   -191       C
ATOM   4754  O   ILE C  55      -5.888  35.234   7.344  1.00 41.86           O
ANISOU 4754  O   ILE C  55     5412   5336   5157   -223    122   -204       O
ATOM   4755  CB  ILE C  55      -8.852  34.511   7.122  1.00 45.37           C
ANISOU 4755  CB  ILE C  55     5866   5770   5604   -124      3   -125       C
ATOM   4756  CG1 ILE C  55     -10.350  34.495   7.420  1.00 45.83           C
ANISOU 4756  CG1 ILE C  55     5911   5828   5674    -81    -46    -92       C
ATOM   4757  CG2 ILE C  55      -8.337  33.152   6.656  1.00 43.18           C
ANISOU 4757  CG2 ILE C  55     5565   5516   5327   -129    -19   -123       C
ATOM   4758  CD1 ILE C  55     -11.180  34.245   6.195  1.00 44.56           C
ANISOU 4758  CD1 ILE C  55     5801   5632   5499    -47    -87    -60       C
ATOM   4759  N   ILE C  56      -6.094  33.775   9.059  1.00 41.29           N
ANISOU 4759  N   ILE C  56     5212   5356   5119   -212     59   -202       N
ATOM   4760  CA  ILE C  56      -4.705  33.324   9.010  1.00 40.48           C
ANISOU 4760  CA  ILE C  56     5078   5279   5024   -246     86   -230       C
ATOM   4761  C   ILE C  56      -4.722  31.896   8.477  1.00 40.80           C
ANISOU 4761  C   ILE C  56     5100   5335   5066   -224     50   -211       C
ATOM   4762  O   ILE C  56      -5.118  30.965   9.189  1.00 43.20           O
ANISOU 4762  O   ILE C  56     5353   5679   5382   -205      7   -199       O
ATOM   4763  CB  ILE C  56      -4.029  33.382  10.379  1.00 38.66           C
ANISOU 4763  CB  ILE C  56     4780   5098   4812   -274     91   -259       C
ATOM   4764  CG1 ILE C  56      -3.682  34.817  10.752  1.00 35.70           C
ANISOU 4764  CG1 ILE C  56     4431   4702   4432   -310    138   -286       C
ATOM   4765  CG2 ILE C  56      -2.729  32.616  10.326  1.00 39.49           C
ANISOU 4765  CG2 ILE C  56     4838   5238   4931   -297    102   -280       C
ATOM   4766  CD1 ILE C  56      -3.371  35.023  12.221  1.00 23.80           C
ANISOU 4766  CD1 ILE C  56     2869   3237   2936   -332    132   -310       C
ATOM   4767  N   HIS C  57      -4.273  31.717   7.237  1.00 36.06           N
ANISOU 4767  N   HIS C  57     4547   4702   4451   -227     73   -208       N
ATOM   4768  CA  HIS C  57      -4.331  30.435   6.542  1.00 38.02           C
ANISOU 4768  CA  HIS C  57     4798   4953   4694   -205     44   -188       C
ATOM   4769  C   HIS C  57      -3.014  29.664   6.676  1.00 41.88           C
ANISOU 4769  C   HIS C  57     5238   5476   5198   -224     68   -210       C
ATOM   4770  O   HIS C  57      -2.061  29.933   5.938  1.00 41.61           O
ANISOU 4770  O   HIS C  57     5230   5420   5161   -246    119   -227       O
ATOM   4771  CB  HIS C  57      -4.658  30.676   5.079  1.00 35.33           C
ANISOU 4771  CB  HIS C  57     4549   4551   4324   -194     54   -171       C
ATOM   4772  CG  HIS C  57      -4.920  29.425   4.310  1.00 37.87           C
ANISOU 4772  CG  HIS C  57     4888   4867   4634   -171     20   -148       C
ATOM   4773  ND1 HIS C  57      -5.421  28.284   4.899  1.00 36.95           N
ANISOU 4773  ND1 HIS C  57     4719   4790   4529   -151    -33   -132       N
ATOM   4774  CD2 HIS C  57      -4.769  29.141   2.993  1.00 39.48           C
ANISOU 4774  CD2 HIS C  57     5164   5026   4811   -166     32   -138       C
ATOM   4775  CE1 HIS C  57      -5.571  27.349   3.975  1.00 42.08           C
ANISOU 4775  CE1 HIS C  57     5406   5420   5161   -136    -54   -114       C
ATOM   4776  NE2 HIS C  57      -5.179  27.843   2.811  1.00 43.83           N
ANISOU 4776  NE2 HIS C  57     5705   5591   5359   -144    -16   -117       N
ATOM   4777  N   THR C  58      -2.972  28.645   7.566  1.00 44.29           N
ANISOU 4777  N   THR C  58     5475   5834   5520   -212     31   -208       N
ATOM   4778  CA  THR C  58      -1.759  27.838   7.756  1.00 40.64           C
ANISOU 4778  CA  THR C  58     4960   5408   5074   -222     47   -226       C
ATOM   4779  C   THR C  58      -1.934  26.380   7.343  1.00 43.57           C
ANISOU 4779  C   THR C  58     5330   5786   5439   -192     15   -203       C
ATOM   4780  O   THR C  58      -0.970  25.609   7.426  1.00 44.72           O
ANISOU 4780  O   THR C  58     5437   5958   5598   -193     28   -214       O
ATOM   4781  CB  THR C  58      -1.302  27.846   9.217  1.00 37.56           C
ANISOU 4781  CB  THR C  58     4490   5075   4707   -235     34   -247       C
ATOM   4782  OG1 THR C  58      -2.252  27.126  10.018  1.00 38.93           O
ANISOU 4782  OG1 THR C  58     4638   5274   4880   -207    -22   -225       O
ATOM   4783  CG2 THR C  58      -1.279  29.270   9.724  1.00 34.15           C
ANISOU 4783  CG2 THR C  58     4065   4635   4278   -266     60   -268       C
ATOM   4784  N   ALA C  59      -3.141  25.968   6.972  1.00 46.40           N
ANISOU 4784  N   ALA C  59     5726   6122   5780   -166    -28   -172       N
ATOM   4785  CA  ALA C  59      -3.428  24.573   6.653  1.00 47.40           C
ANISOU 4785  CA  ALA C  59     5856   6254   5899   -141    -63   -150       C
ATOM   4786  C   ALA C  59      -2.643  24.119   5.423  1.00 54.43           C
ANISOU 4786  C   ALA C  59     6792   7113   6775   -142    -26   -151       C
ATOM   4787  O   ALA C  59      -2.320  24.915   4.531  1.00 51.84           O
ANISOU 4787  O   ALA C  59     6519   6743   6435   -157     16   -159       O
ATOM   4788  CB  ALA C  59      -4.936  24.367   6.405  1.00 42.92           C
ANISOU 4788  CB  ALA C  59     5324   5665   5318   -119   -116   -118       C
ATOM   4789  N   ALA C  60      -2.363  22.814   5.379  1.00 53.72           N
ANISOU 4789  N   ALA C  60     6687   7040   6685   -124    -40   -142       N
ATOM   4790  CA  ALA C  60      -1.662  22.221   4.252  1.00 62.22           C
ANISOU 4790  CA  ALA C  60     7809   8084   7746   -121     -5   -141       C
ATOM   4791  C   ALA C  60      -2.487  22.304   2.975  1.00 59.43           C
ANISOU 4791  C   ALA C  60     7553   7671   7358   -115    -17   -119       C
ATOM   4792  O   ALA C  60      -3.719  22.246   2.995  1.00 56.81           O
ANISOU 4792  O   ALA C  60     7242   7330   7013   -103    -71    -97       O
ATOM   4793  CB  ALA C  60      -1.329  20.756   4.541  1.00 65.03           C
ANISOU 4793  CB  ALA C  60     8132   8469   8107    -98    -22   -133       C
ATOM   4794  N   ILE C  61      -1.783  22.467   1.855  1.00 60.58           N
ANISOU 4794  N   ILE C  61     7759   7773   7486   -123     36   -126       N
ATOM   4795  CA  ILE C  61      -2.400  22.523   0.533  1.00 67.38           C
ANISOU 4795  CA  ILE C  61     8724   8570   8306   -118     29   -107       C
ATOM   4796  C   ILE C  61      -1.547  21.707  -0.433  1.00 69.09           C
ANISOU 4796  C   ILE C  61     8988   8756   8505   -113     74   -108       C
ATOM   4797  O   ILE C  61      -1.883  21.564  -1.613  1.00 66.71           O
ANISOU 4797  O   ILE C  61     8783   8399   8165   -109     74    -93       O
ATOM   4798  CB  ILE C  61      -2.574  23.974   0.043  1.00 62.41           C
ANISOU 4798  CB  ILE C  61     8147   7901   7665   -134     56   -113       C
ATOM   4799  N   SER C  62      -0.436  21.169   0.066  1.00 71.66           N
ANISOU 4799  N   SER C  62     9248   9119   8859   -113    111   -125       N
ATOM   4800  CA  SER C  62       0.436  20.285  -0.702  1.00 73.20           C
ANISOU 4800  CA  SER C  62     9475   9292   9045   -103    157   -126       C
ATOM   4801  C   SER C  62       0.268  18.885  -0.123  1.00 76.54           C
ANISOU 4801  C   SER C  62     9858   9751   9474    -77    115   -112       C
ATOM   4802  O   SER C  62       0.763  18.585   0.969  1.00 74.07           O
ANISOU 4802  O   SER C  62     9452   9495   9195    -71    110   -123       O
ATOM   4803  CB  SER C  62       1.892  20.747  -0.660  1.00 67.88           C
ANISOU 4803  CB  SER C  62     8758   8631   8404   -120    239   -156       C
ATOM   4804  N   ASN C  63      -0.444  18.041  -0.868  1.00 78.82           N
ANISOU 4804  N   ASN C  63    10222  10002   9724    -63     82    -88       N
ATOM   4805  CA  ASN C  63      -0.716  16.664  -0.492  1.00 81.74           C
ANISOU 4805  CA  ASN C  63    10575  10392  10089    -40     43    -72       C
ATOM   4806  C   ASN C  63       0.461  15.730  -0.756  1.00 89.56           C
ANISOU 4806  C   ASN C  63    11562  11383  11085    -22     98    -79       C
ATOM   4807  O   ASN C  63       0.414  14.572  -0.325  1.00 89.42           O
ANISOU 4807  O   ASN C  63    11523  11385  11067     -0     73    -68       O
ATOM   4808  CB  ASN C  63      -1.959  16.171  -1.242  1.00 72.13           C
ANISOU 4808  CB  ASN C  63     9445   9133   8829    -37    -14    -45       C
ATOM   4809  N   THR C  64       1.497  16.194  -1.457  1.00 95.76           N
ANISOU 4809  N   THR C  64    12369  12141  11875    -30    174    -95       N
ATOM   4810  CA  THR C  64       2.722  15.430  -1.662  1.00 98.34           C
ANISOU 4810  CA  THR C  64    12679  12471  12216    -12    237   -103       C
ATOM   4811  C   THR C  64       3.707  15.744  -0.546  1.00 97.50           C
ANISOU 4811  C   THR C  64    12449  12430  12166    -12    260   -127       C
ATOM   4812  O   THR C  64       3.685  16.835   0.034  1.00101.01           O
ANISOU 4812  O   THR C  64    12844  12902  12635    -36    254   -143       O
ATOM   4813  CB  THR C  64       3.359  15.744  -3.021  1.00 98.56           C
ANISOU 4813  CB  THR C  64    12793  12432  12221    -21    315   -109       C
ATOM   4814  N   GLY C  65       4.561  14.774  -0.230  1.00 85.10           N
ANISOU 4814  N   GLY C  65    10831  10887  10617     16    283   -129       N
ATOM   4815  CA  GLY C  65       5.307  14.854   1.009  1.00 80.97           C
ANISOU 4815  CA  GLY C  65    10186  10435  10145     22    279   -146       C
ATOM   4816  C   GLY C  65       4.386  14.675   2.206  1.00 88.37           C
ANISOU 4816  C   GLY C  65    11078  11418  11082     27    195   -137       C
ATOM   4817  O   GLY C  65       4.703  13.915   3.126  1.00 82.83           O
ANISOU 4817  O   GLY C  65    10310  10763  10399     53    171   -135       O
ATOM   4818  N   LEU C  66       3.252  15.400   2.216  1.00102.36           N
ANISOU 4818  N   LEU C  66    12884  13174  12833      4    151   -130       N
ATOM   4819  CA  LEU C  66       2.117  15.049   3.067  1.00101.58           C
ANISOU 4819  CA  LEU C  66    12771  13100  12724     10     74   -114       C
ATOM   4820  C   LEU C  66       1.495  13.719   2.650  1.00100.94           C
ANISOU 4820  C   LEU C  66    12751  12992  12609     35     45    -87       C
ATOM   4821  O   LEU C  66       0.772  13.109   3.448  1.00 99.99           O
ANISOU 4821  O   LEU C  66    12610  12898  12486     46    -10    -74       O
ATOM   4822  CB  LEU C  66       1.062  16.161   3.032  1.00101.82           C
ANISOU 4822  CB  LEU C  66    12829  13115  12744    -17     43   -111       C
ATOM   4823  N   CYS C  67       1.751  13.275   1.407  1.00 91.82           N
ANISOU 4823  N   CYS C  67    11678  11782  11426     41     84    -80       N
ATOM   4824  CA  CYS C  67       1.528  11.880   1.028  1.00 80.16           C
ANISOU 4824  CA  CYS C  67    10255  10281   9920     66     72    -59       C
ATOM   4825  C   CYS C  67       2.392  10.930   1.854  1.00 75.65           C
ANISOU 4825  C   CYS C  67     9616   9754   9374    100     84    -62       C
ATOM   4826  O   CYS C  67       1.997   9.784   2.091  1.00 70.03           O
ANISOU 4826  O   CYS C  67     8923   9042   8644    122     53    -45       O
ATOM   4827  CB  CYS C  67       1.817  11.682  -0.465  1.00 80.47           C
ANISOU 4827  CB  CYS C  67    10399  10252   9926     65    123    -55       C
ATOM   4828  N   GLU C  68       3.544  11.398   2.345  1.00 72.36           N
ANISOU 4828  N   GLU C  68     9117   9377   9000    105    125    -84       N
ATOM   4829  CA  GLU C  68       4.338  10.593   3.263  1.00 66.61           C
ANISOU 4829  CA  GLU C  68     8313   8698   8299    140    125    -87       C
ATOM   4830  C   GLU C  68       3.721  10.455   4.671  1.00 65.45           C
ANISOU 4830  C   GLU C  68     8103   8603   8160    145     56    -83       C
ATOM   4831  O   GLU C  68       4.293   9.717   5.483  1.00 61.13           O
ANISOU 4831  O   GLU C  68     7502   8096   7629    177     48    -83       O
ATOM   4832  CB  GLU C  68       5.761  11.159   3.351  1.00 63.28           C
ANISOU 4832  CB  GLU C  68     7816   8305   7923    142    185   -112       C
ATOM   4833  N   GLN C  69       2.588  11.107   4.983  1.00 64.07           N
ANISOU 4833  N   GLN C  69     7939   8429   7974    116      7    -79       N
ATOM   4834  CA  GLN C  69       1.939  10.988   6.292  1.00 58.97           C
ANISOU 4834  CA  GLN C  69     7243   7827   7335    119    -52    -75       C
ATOM   4835  C   GLN C  69       0.620  10.214   6.291  1.00 52.41           C
ANISOU 4835  C   GLN C  69     6469   6973   6470    120   -102    -50       C
ATOM   4836  O   GLN C  69      -0.058  10.189   7.327  1.00 49.94           O
ANISOU 4836  O   GLN C  69     6123   6692   6162    118   -148    -45       O
ATOM   4837  CB  GLN C  69       1.705  12.348   6.946  1.00 59.07           C
ANISOU 4837  CB  GLN C  69     7206   7868   7369     87    -67    -92       C
ATOM   4838  CG  GLN C  69       2.941  13.006   7.525  1.00 68.91           C
ANISOU 4838  CG  GLN C  69     8370   9159   8654     84    -38   -120       C
ATOM   4839  CD  GLN C  69       3.417  14.151   6.694  1.00 73.60           C
ANISOU 4839  CD  GLN C  69     8975   9729   9260     53     13   -138       C
ATOM   4840  OE1 GLN C  69       2.623  15.009   6.297  1.00 74.29           O
ANISOU 4840  OE1 GLN C  69     9104   9788   9334     25      6   -136       O
ATOM   4841  NE2 GLN C  69       4.715  14.188   6.420  1.00 74.21           N
ANISOU 4841  NE2 GLN C  69     9016   9816   9364     59     66   -155       N
ATOM   4842  N   ASN C  70       0.219   9.605   5.178  1.00 47.70           N
ANISOU 4842  N   ASN C  70     5959   6324   5841    121    -95    -34       N
ATOM   4843  CA  ASN C  70      -0.960   8.748   5.213  1.00 43.90           C
ANISOU 4843  CA  ASN C  70     5526   5822   5330    120   -143    -11       C
ATOM   4844  C   ASN C  70      -0.683   7.523   4.342  1.00 44.70           C
ANISOU 4844  C   ASN C  70     5702   5882   5401    141   -120      2       C
ATOM   4845  O   ASN C  70       0.068   7.611   3.366  1.00 48.92           O
ANISOU 4845  O   ASN C  70     6274   6385   5930    145    -69     -3       O
ATOM   4846  CB  ASN C  70      -2.251   9.484   4.787  1.00 43.93           C
ANISOU 4846  CB  ASN C  70     5568   5802   5322     85   -181     -3       C
ATOM   4847  CG  ASN C  70      -2.145  10.197   3.435  1.00 46.62           C
ANISOU 4847  CG  ASN C  70     5972   6093   5647     67   -152     -7       C
ATOM   4848  OD1 ASN C  70      -1.334   9.830   2.586  1.00 48.82           O
ANISOU 4848  OD1 ASN C  70     6295   6343   5913     79   -105     -9       O
ATOM   4849  ND2 ASN C  70      -2.982  11.230   3.235  1.00 43.31           N
ANISOU 4849  ND2 ASN C  70     5562   5664   5228     41   -177     -6       N
ATOM   4850  N   PRO C  71      -1.247   6.364   4.678  1.00 38.30           N
ANISOU 4850  N   PRO C  71     4916   5065   4569    153   -151     19       N
ATOM   4851  CA  PRO C  71      -0.916   5.157   3.915  1.00 37.87           C
ANISOU 4851  CA  PRO C  71     4936   4969   4484    175   -125     31       C
ATOM   4852  C   PRO C  71      -1.635   4.996   2.573  1.00 37.43           C
ANISOU 4852  C   PRO C  71     4986   4848   4388    150   -130     43       C
ATOM   4853  O   PRO C  71      -1.220   4.139   1.791  1.00 40.64           O
ANISOU 4853  O   PRO C  71     5463   5213   4766    167    -98     50       O
ATOM   4854  CB  PRO C  71      -1.315   4.025   4.889  1.00 35.47           C
ANISOU 4854  CB  PRO C  71     4621   4685   4172    195   -158     45       C
ATOM   4855  CG  PRO C  71      -1.268   4.641   6.229  1.00 37.46           C
ANISOU 4855  CG  PRO C  71     4776   4998   4459    197   -181     34       C
ATOM   4856  CD  PRO C  71      -1.876   6.002   5.956  1.00 43.59           C
ANISOU 4856  CD  PRO C  71     5539   5774   5248    157   -197     26       C
ATOM   4857  N   GLU C  72      -2.704   5.732   2.286  1.00 36.13           N
ANISOU 4857  N   GLU C  72     4840   4671   4217    114   -172     46       N
ATOM   4858  CA  GLU C  72      -3.445   5.621   1.029  1.00 36.70           C
ANISOU 4858  CA  GLU C  72     5012   4682   4249     89   -189     57       C
ATOM   4859  C   GLU C  72      -3.262   6.856   0.142  1.00 30.01           C
ANISOU 4859  C   GLU C  72     4189   3812   3401     72   -166     47       C
ATOM   4860  O   GLU C  72      -4.229   7.380  -0.405  1.00 25.30           O
ANISOU 4860  O   GLU C  72     3632   3190   2789     44   -207     54       O
ATOM   4861  CB  GLU C  72      -4.922   5.382   1.355  1.00 38.67           C
ANISOU 4861  CB  GLU C  72     5269   4934   4491     63   -262     72       C
ATOM   4862  CG  GLU C  72      -5.863   4.872   0.263  1.00 33.62           C
ANISOU 4862  CG  GLU C  72     4730   4237   3808     37   -298     87       C
ATOM   4863  CD  GLU C  72      -7.329   5.406   0.445  1.00 40.39           C
ANISOU 4863  CD  GLU C  72     5569   5102   4675      3   -370     95       C
ATOM   4864  OE1 GLU C  72      -7.626   6.451   1.154  1.00 36.45           O
ANISOU 4864  OE1 GLU C  72     4992   4643   4212     -2   -386     89       O
ATOM   4865  OE2 GLU C  72      -8.211   4.731  -0.134  1.00 48.77           O
ANISOU 4865  OE2 GLU C  72     6696   6129   5707    -19   -412    108       O
ATOM   4866  N   LEU C  73      -2.023   7.299  -0.050  1.00 34.30           N
ANISOU 4866  N   LEU C  73     4712   4360   3962     88   -101     32       N
ATOM   4867  CA  LEU C  73      -1.745   8.552  -0.758  1.00 39.47           C
ANISOU 4867  CA  LEU C  73     5382   4996   4620     70    -71     19       C
ATOM   4868  C   LEU C  73      -2.062   8.490  -2.259  1.00 34.57           C
ANISOU 4868  C   LEU C  73     4885   4301   3950     56    -63     28       C
ATOM   4869  O   LEU C  73      -1.677   7.546  -2.943  1.00 37.03           O
ANISOU 4869  O   LEU C  73     5267   4572   4230     69    -33     35       O
ATOM   4870  CB  LEU C  73      -0.283   8.919  -0.542  1.00 38.41           C
ANISOU 4870  CB  LEU C  73     5189   4885   4519     89      2     -1       C
ATOM   4871  N   SER C  74      -2.749   9.527  -2.767  1.00 32.46           N
ANISOU 4871  N   SER C  74     4647   4013   3672     30    -89     29       N
ATOM   4872  CA  SER C  74      -3.069   9.654  -4.196  1.00 36.96           C
ANISOU 4872  CA  SER C  74     5339   4513   4193     15    -86     36       C
ATOM   4873  C   SER C  74      -1.841  10.019  -5.048  1.00 38.03           C
ANISOU 4873  C   SER C  74     5519   4611   4320     23      4     23       C
ATOM   4874  O   SER C  74      -1.564   9.365  -6.060  1.00 41.66           O
ANISOU 4874  O   SER C  74     6079   5014   4737     28     36     29       O
ATOM   4875  CB  SER C  74      -4.187  10.700  -4.372  1.00 36.13           C
ANISOU 4875  CB  SER C  74     5244   4401   4083     -9   -145     42       C
ATOM   4876  OG  SER C  74      -4.262  11.200  -5.703  1.00 34.40           O
ANISOU 4876  OG  SER C  74     5132   4116   3820    -21   -132     45       O
ATOM   4877  N   GLU C  75      -1.127  11.092  -4.676  1.00 44.59           N
ANISOU 4877  N   GLU C  75     6283   5471   5189     21     48      4       N
ATOM   4878  CA  GLU C  75       0.096  11.613  -5.304  1.00 48.86           C
ANISOU 4878  CA  GLU C  75     6843   5986   5736     24    140    -13       C
ATOM   4879  C   GLU C  75      -0.093  12.455  -6.576  1.00 54.65           C
ANISOU 4879  C   GLU C  75     7684   6652   6429      4    161    -13       C
ATOM   4880  O   GLU C  75      -0.830  12.074  -7.489  1.00 50.79           O
ANISOU 4880  O   GLU C  75     7304   6109   5886     -3    128      4       O
ATOM   4881  CB  GLU C  75       1.084  10.475  -5.599  1.00 47.48           C
ANISOU 4881  CB  GLU C  75     6689   5795   5555     51    201    -13       C
ATOM   4882  N   SER C  76       0.542  13.642  -6.586  1.00 71.06           N
ANISOU 4882  N   SER C  76     9733   8736   8533     -9    213    -31       N
ATOM   4883  CA  SER C  76       0.765  14.524  -7.738  1.00 71.78           C
ANISOU 4883  CA  SER C  76     9918   8763   8592    -25    264    -37       C
ATOM   4884  C   SER C  76      -0.429  15.354  -8.231  1.00 79.61           C
ANISOU 4884  C   SER C  76    10978   9721   9547    -43    200    -25       C
ATOM   4885  O   SER C  76      -1.576  14.886  -8.201  1.00 84.64           O
ANISOU 4885  O   SER C  76    11640  10358  10161    -42    115     -5       O
ATOM   4886  CB  SER C  76       1.332  13.686  -8.893  1.00 75.29           C
ANISOU 4886  CB  SER C  76    10472   9142   8994    -13    323    -32       C
ATOM   4887  OG  SER C  76       1.646  14.496 -10.009  1.00 74.45           O
ANISOU 4887  OG  SER C  76    10463   8969   8855    -28    382    -38       O
ATOM   4888  N   ILE C  77      -0.118  16.578  -8.729  1.00 75.17           N
ANISOU 4888  N   ILE C  77    10451   9129   8981    -59    247    -37       N
ATOM   4889  CA  ILE C  77      -1.011  17.647  -9.214  1.00 62.07           C
ANISOU 4889  CA  ILE C  77     8855   7436   7292    -73    206    -29       C
ATOM   4890  C   ILE C  77      -1.607  18.445  -8.048  1.00 60.00           C
ANISOU 4890  C   ILE C  77     8487   7237   7075    -79    154    -33       C
ATOM   4891  O   ILE C  77      -1.781  17.911  -6.947  1.00 61.11           O
ANISOU 4891  O   ILE C  77     8526   7441   7253    -71    115    -32       O
ATOM   4892  CB  ILE C  77      -2.114  17.087 -10.126  1.00 64.92           C
ANISOU 4892  CB  ILE C  77     9332   7745   7590    -69    134     -4       C
ATOM   4893  N   ASN C  78      -1.999  19.702  -8.283  1.00 59.90           N
ANISOU 4893  N   ASN C  78     8505   7203   7053    -90    149    -35       N
ATOM   4894  CA  ASN C  78      -2.392  20.606  -7.203  1.00 62.30           C
ANISOU 4894  CA  ASN C  78     8713   7560   7400    -96    119    -41       C
ATOM   4895  C   ASN C  78      -3.822  21.102  -7.377  1.00 64.79           C
ANISOU 4895  C   ASN C  78     9067   7859   7690    -91     32    -20       C
ATOM   4896  O   ASN C  78      -4.247  21.439  -8.486  1.00 63.68           O
ANISOU 4896  O   ASN C  78     9040   7654   7499    -90     22     -8       O
ATOM   4897  CB  ASN C  78      -1.460  21.821  -7.135  1.00 64.99           C
ANISOU 4897  CB  ASN C  78     9036   7895   7762   -115    201    -67       C
ATOM   4898  N   LEU C  79      -4.545  21.186  -6.262  1.00 74.47           N
ANISOU 4898  N   LEU C  79    10198   9142   8953    -87    -27    -15       N
ATOM   4899  CA  LEU C  79      -5.961  21.536  -6.243  1.00 74.02           C
ANISOU 4899  CA  LEU C  79    10155   9083   8886    -78   -114      7       C
ATOM   4900  C   LEU C  79      -6.164  22.880  -5.548  1.00 74.92           C
ANISOU 4900  C   LEU C  79    10217   9218   9030    -81   -107     -2       C
ATOM   4901  O   LEU C  79      -5.243  23.453  -4.956  1.00 75.95           O
ANISOU 4901  O   LEU C  79    10293   9373   9190    -94    -43    -26       O
ATOM   4902  CB  LEU C  79      -6.786  20.429  -5.565  1.00 74.93           C
ANISOU 4902  CB  LEU C  79    10210   9243   9019    -70   -189     23       C
ATOM   4903  CG  LEU C  79      -8.318  20.474  -5.669  1.00 78.98           C
ANISOU 4903  CG  LEU C  79    10736   9751   9522    -61   -286     48       C
ATOM   4904  CD1 LEU C  79      -8.811  19.852  -6.972  1.00 73.40           C
ANISOU 4904  CD1 LEU C  79    10144   8985   8758    -60   -327     67       C
ATOM   4905  CD2 LEU C  79      -9.012  19.849  -4.445  1.00 81.37           C
ANISOU 4905  CD2 LEU C  79    10932  10118   9868    -58   -339     55       C
ATOM   4906  N   ASN C  80      -7.405  23.369  -5.621  1.00 77.49           N
ANISOU 4906  N   ASN C  80    10560   9536   9348    -70   -177     18       N
ATOM   4907  CA  ASN C  80      -7.807  24.710  -5.193  1.00 75.44           C
ANISOU 4907  CA  ASN C  80    10278   9280   9104    -67   -177     16       C
ATOM   4908  C   ASN C  80      -8.607  24.797  -3.890  1.00 71.60           C
ANISOU 4908  C   ASN C  80     9684   8855   8665    -59   -226     21       C
ATOM   4909  O   ASN C  80      -9.755  25.259  -3.885  1.00 68.79           O
ANISOU 4909  O   ASN C  80     9333   8495   8310    -43   -285     40       O
ATOM   4910  CB  ASN C  80      -8.628  25.334  -6.327  1.00 70.64           C
ANISOU 4910  CB  ASN C  80     9781   8610   8451    -53   -215     36       C
ATOM   4911  CG  ASN C  80      -9.800  24.455  -6.763  1.00 66.25           C
ANISOU 4911  CG  ASN C  80     9250   8048   7875    -39   -311     65       C
ATOM   4912  OD1 ASN C  80     -10.243  23.584  -6.022  1.00 69.64           O
ANISOU 4912  OD1 ASN C  80     9601   8525   8334    -38   -355     71       O
ATOM   4913  ND2 ASN C  80     -10.275  24.664  -7.988  1.00 64.53           N
ANISOU 4913  ND2 ASN C  80     9147   7768   7605    -30   -342     81       N
ATOM   4914  N   GLY C  81      -8.053  24.336  -2.777  1.00 68.66           N
ANISOU 4914  N   GLY C  81     9215   8540   8332    -67   -205      5       N
ATOM   4915  CA  GLY C  81      -8.767  24.522  -1.525  1.00 70.69           C
ANISOU 4915  CA  GLY C  81     9379   8850   8631    -61   -242      8       C
ATOM   4916  C   GLY C  81      -8.847  25.986  -1.135  1.00 71.89           C
ANISOU 4916  C   GLY C  81     9521   8997   8796    -62   -216     -1       C
ATOM   4917  O   GLY C  81      -9.867  26.450  -0.616  1.00 68.06           O
ANISOU 4917  O   GLY C  81     9005   8526   8328    -47   -259     13       O
ATOM   4918  N   THR C  82      -7.769  26.732  -1.403  1.00 71.89           N
ANISOU 4918  N   THR C  82     9551   8976   8788    -79   -142    -24       N
ATOM   4919  CA  THR C  82      -7.662  28.155  -1.089  1.00 69.53           C
ANISOU 4919  CA  THR C  82     9255   8666   8496    -86   -104    -37       C
ATOM   4920  C   THR C  82      -8.548  29.022  -1.976  1.00 62.78           C
ANISOU 4920  C   THR C  82     8489   7756   7610    -67   -129    -17       C
ATOM   4921  O   THR C  82      -8.977  30.104  -1.556  1.00 58.92           O
ANISOU 4921  O   THR C  82     7993   7263   7131    -60   -125    -17       O
ATOM   4922  CB  THR C  82      -6.205  28.577  -1.227  1.00 66.17           C
ANISOU 4922  CB  THR C  82     8840   8231   8071   -116    -16    -69       C
ATOM   4923  OG1 THR C  82      -5.812  28.437  -2.600  1.00 61.73           O
ANISOU 4923  OG1 THR C  82     8377   7609   7467   -118     12    -65       O
ATOM   4924  CG2 THR C  82      -5.347  27.682  -0.378  1.00 59.84           C
ANISOU 4924  CG2 THR C  82     7949   7486   7302   -130      1    -87       C
ATOM   4925  N   LYS C  83      -8.781  28.594  -3.215  1.00 68.85           N
ANISOU 4925  N   LYS C  83     9345   8476   8337    -58   -152     -0       N
ATOM   4926  CA  LYS C  83      -9.651  29.354  -4.084  1.00 64.50           C
ANISOU 4926  CA  LYS C  83     8882   7873   7753    -35   -185     22       C
ATOM   4927  C   LYS C  83     -10.972  29.601  -3.389  1.00 69.63           C
ANISOU 4927  C   LYS C  83     9475   8551   8430     -9   -255     43       C
ATOM   4928  O   LYS C  83     -11.489  30.726  -3.405  1.00 69.03           O
ANISOU 4928  O   LYS C  83     9425   8452   8352      8   -256     49       O
ATOM   4929  CB  LYS C  83      -9.863  28.611  -5.399  1.00 64.16           C
ANISOU 4929  CB  LYS C  83     8934   7783   7662    -28   -219     40       C
ATOM   4930  CG  LYS C  83     -10.316  29.467  -6.556  1.00 57.73           C
ANISOU 4930  CG  LYS C  83     8239   6898   6798    -10   -231     55       C
ATOM   4931  CD  LYS C  83     -10.282  28.686  -7.839  1.00 56.13           C
ANISOU 4931  CD  LYS C  83     8138   6647   6544     -9   -252     67       C
ATOM   4932  CE  LYS C  83      -8.862  28.630  -8.383  1.00 59.80           C
ANISOU 4932  CE  LYS C  83     8659   7079   6985    -36   -155     43       C
ATOM   4933  NZ  LYS C  83      -8.827  28.315  -9.851  1.00 59.94           N
ANISOU 4933  NZ  LYS C  83     8814   7024   6936    -32   -160     55       N
ATOM   4934  N   TYR C  84     -11.553  28.575  -2.767  1.00 75.66           N
ANISOU 4934  N   TYR C  84    10162   9362   9222     -4   -310     53       N
ATOM   4935  CA  TYR C  84     -12.829  28.901  -2.170  1.00 73.29           C
ANISOU 4935  CA  TYR C  84     9811   9085   8951     22   -369     74       C
ATOM   4936  C   TYR C  84     -12.679  29.613  -0.855  1.00 72.24           C
ANISOU 4936  C   TYR C  84     9598   8991   8858     17   -331     58       C
ATOM   4937  O   TYR C  84     -13.566  30.380  -0.456  1.00 75.36           O
ANISOU 4937  O   TYR C  84     9975   9388   9272     40   -354     70       O
ATOM   4938  CB  TYR C  84     -13.781  27.767  -2.071  1.00 72.85           C
ANISOU 4938  CB  TYR C  84     9712   9056   8909     31   -448     96       C
ATOM   4939  CG  TYR C  84     -14.062  27.301  -3.429  1.00 73.87           C
ANISOU 4939  CG  TYR C  84     9934   9139   8993     36   -491    113       C
ATOM   4940  CD1 TYR C  84     -15.114  26.612  -3.570  1.00 80.09           C
ANISOU 4940  CD1 TYR C  84    10704   9937   9789     48   -571    136       C
ATOM   4941  CD2 TYR C  84     -13.059  26.965  -4.364  1.00 84.59           C
ANISOU 4941  CD2 TYR C  84    11376  10458  10308     19   -450    101       C
ATOM   4942  CE1 TYR C  84     -15.542  26.126  -4.691  1.00 86.89           C
ANISOU 4942  CE1 TYR C  84    11641  10762  10612     52   -624    153       C
ATOM   4943  CE2 TYR C  84     -13.390  26.358  -5.558  1.00 83.47           C
ANISOU 4943  CE2 TYR C  84    11320  10274  10121     22   -496    118       C
ATOM   4944  CZ  TYR C  84     -14.716  25.910  -5.645  1.00 87.95           C
ANISOU 4944  CZ  TYR C  84    11868  10852  10698     39   -592    145       C
ATOM   4945  OH  TYR C  84     -15.435  25.266  -6.579  1.00 92.91           O
ANISOU 4945  OH  TYR C  84    12554  11453  11294     43   -666    166       O
ATOM   4946  N   LEU C  85     -11.567  29.412  -0.191  1.00 68.87           N
ANISOU 4946  N   LEU C  85     9129   8594   8446    -10   -274     30       N
ATOM   4947  CA  LEU C  85     -11.314  30.237   0.964  1.00 63.91           C
ANISOU 4947  CA  LEU C  85     8442   7993   7846    -19   -234     11       C
ATOM   4948  C   LEU C  85     -11.420  31.723   0.566  1.00 59.35           C
ANISOU 4948  C   LEU C  85     7930   7368   7251    -10   -201     10       C
ATOM   4949  O   LEU C  85     -12.054  32.507   1.280  1.00 52.61           O
ANISOU 4949  O   LEU C  85     7048   6523   6419      5   -205     14       O
ATOM   4950  CB  LEU C  85      -9.960  29.834   1.552  1.00 54.01           C
ANISOU 4950  CB  LEU C  85     7145   6772   6605    -52   -178    -21       C
ATOM   4951  CG  LEU C  85      -9.541  30.307   2.930  1.00 46.99           C
ANISOU 4951  CG  LEU C  85     6179   5926   5748    -68   -144    -44       C
ATOM   4952  CD1 LEU C  85     -10.672  30.056   3.888  1.00 46.72           C
ANISOU 4952  CD1 LEU C  85     6080   5928   5743    -46   -195    -26       C
ATOM   4953  CD2 LEU C  85      -8.334  29.520   3.340  1.00 43.67           C
ANISOU 4953  CD2 LEU C  85     5713   5542   5338    -94   -113    -68       C
ATOM   4954  N   ALA C  86     -10.854  32.111  -0.605  1.00 53.45           N
ANISOU 4954  N   ALA C  86     7280   6566   6464    -17   -168      6       N
ATOM   4955  CA  ALA C  86     -10.738  33.521  -1.005  1.00 53.85           C
ANISOU 4955  CA  ALA C  86     7403   6565   6492    -15   -124      0       C
ATOM   4956  C   ALA C  86     -12.093  34.115  -1.406  1.00 53.26           C
ANISOU 4956  C   ALA C  86     7369   6460   6407     30   -181     33       C
ATOM   4957  O   ALA C  86     -12.381  35.267  -1.033  1.00 52.09           O
ANISOU 4957  O   ALA C  86     7231   6297   6264     42   -158     32       O
ATOM   4958  CB  ALA C  86      -9.647  33.678  -2.075  1.00 55.49           C
ANISOU 4958  CB  ALA C  86     7700   6724   6660    -39    -63    -16       C
ATOM   4959  N   GLU C  87     -12.991  33.330  -2.057  1.00 57.82           N
ANISOU 4959  N   GLU C  87     7961   7033   6975     55   -258     62       N
ATOM   4960  CA  GLU C  87     -14.326  33.876  -2.213  1.00 54.20           C
ANISOU 4960  CA  GLU C  87     7515   6559   6521     99   -318     93       C
ATOM   4961  C   GLU C  87     -14.869  34.188  -0.848  1.00 51.44           C
ANISOU 4961  C   GLU C  87     7066   6257   6221    109   -320     92       C
ATOM   4962  O   GLU C  87     -15.518  35.222  -0.651  1.00 50.44           O
ANISOU 4962  O   GLU C  87     6950   6112   6101    139   -319    103       O
ATOM   4963  CB  GLU C  87     -15.386  32.898  -2.681  1.00 63.84           C
ANISOU 4963  CB  GLU C  87     8723   7791   7744    122   -413    123       C
ATOM   4964  CG  GLU C  87     -15.223  31.933  -3.967  1.00 74.91           C
ANISOU 4964  CG  GLU C  87    10200   9161   9101    114   -451    133       C
ATOM   4965  CD  GLU C  87     -16.713  31.122  -3.958  1.00 78.36           C
ANISOU 4965  CD  GLU C  87    10583   9626   9563    141   -562    166       C
ATOM   4966  OE1 GLU C  87     -17.621  30.279  -4.282  1.00 85.39           O
ANISOU 4966  OE1 GLU C  87    11456  10528  10459    151   -645    188       O
ATOM   4967  OE2 GLU C  87     -16.782  31.730  -5.051  1.00 81.82           O
ANISOU 4967  OE2 GLU C  87    11126  10006   9955    158   -570    176       O
ATOM   4968  N   ALA C  88     -14.677  33.261   0.088  1.00 54.45           N
ANISOU 4968  N   ALA C  88     7354   6696   6637     89   -324     81       N
ATOM   4969  CA  ALA C  88     -15.449  33.433   1.292  1.00 51.66           C
ANISOU 4969  CA  ALA C  88     6914   6384   6330    105   -339     88       C
ATOM   4970  C   ALA C  88     -14.981  34.677   1.968  1.00 45.14           C
ANISOU 4970  C   ALA C  88     6095   5549   5508     98   -270     67       C
ATOM   4971  O   ALA C  88     -15.795  35.477   2.422  1.00 48.56           O
ANISOU 4971  O   ALA C  88     6514   5977   5959    128   -275     80       O
ATOM   4972  CB  ALA C  88     -15.379  32.230   2.242  1.00 53.20           C
ANISOU 4972  CB  ALA C  88     7013   6640   6559     86   -355     81       C
ATOM   4973  N   ALA C  89     -13.675  34.896   1.942  1.00 51.26           N
ANISOU 4973  N   ALA C  89     6897   6316   6265     60   -204     36       N
ATOM   4974  CA  ALA C  89     -13.115  36.102   2.501  1.00 48.70           C
ANISOU 4974  CA  ALA C  89     6587   5977   5939     44   -135     12       C
ATOM   4975  C   ALA C  89     -13.511  37.335   1.711  1.00 51.94           C
ANISOU 4975  C   ALA C  89     7092   6324   6320     71   -121     25       C
ATOM   4976  O   ALA C  89     -13.675  38.409   2.293  1.00 57.07           O
ANISOU 4976  O   ALA C  89     7748   6960   6975     78    -86     19       O
ATOM   4977  CB  ALA C  89     -11.600  35.983   2.524  1.00 49.45           C
ANISOU 4977  CB  ALA C  89     6689   6078   6023     -7    -71    -24       C
ATOM   4978  N   SER C  90     -13.654  37.233   0.394  1.00 48.78           N
ANISOU 4978  N   SER C  90     6773   5879   5884     86   -146     42       N
ATOM   4979  CA  SER C  90     -13.978  38.445  -0.353  1.00 49.46           C
ANISOU 4979  CA  SER C  90     6957   5899   5936    113   -130     54       C
ATOM   4980  C   SER C  90     -15.356  38.985   0.020  1.00 48.70           C
ANISOU 4980  C   SER C  90     6838   5804   5863    167   -176     84       C
ATOM   4981  O   SER C  90     -15.520  40.188   0.250  1.00 51.12           O
ANISOU 4981  O   SER C  90     7182   6079   6164    184   -138     83       O
ATOM   4982  CB  SER C  90     -13.891  38.178  -1.852  1.00 49.73           C
ANISOU 4982  CB  SER C  90     7091   5883   5922    121   -153     68       C
ATOM   4983  OG  SER C  90     -13.801  39.397  -2.562  1.00 51.92           O
ANISOU 4983  OG  SER C  90     7476   6091   6159    134   -114     69       O
ATOM   4984  N   LYS C  91     -16.331  38.098   0.188  1.00 47.75           N
ANISOU 4984  N   LYS C  91     6649   5721   5772    192   -253    109       N
ATOM   4985  CA  LYS C  91     -17.703  38.540   0.408  1.00 48.85           C
ANISOU 4985  CA  LYS C  91     6763   5860   5937    247   -302    140       C
ATOM   4986  C   LYS C  91     -17.824  39.390   1.654  1.00 47.05           C
ANISOU 4986  C   LYS C  91     6490   5647   5741    253   -252    129       C
ATOM   4987  O   LYS C  91     -18.676  40.286   1.710  1.00 46.69           O
ANISOU 4987  O   LYS C  91     6461   5577   5702    299   -258    150       O
ATOM   4988  CB  LYS C  91     -18.635  37.333   0.441  1.00 48.02           C
ANISOU 4988  CB  LYS C  91     6582   5798   5865    263   -388    165       C
ATOM   4989  CG  LYS C  91     -18.399  36.470  -0.790  1.00 49.08           C
ANISOU 4989  CG  LYS C  91     6773   5914   5962    251   -432    172       C
ATOM   4990  CD  LYS C  91     -19.653  35.812  -1.352  1.00 54.31           C
ANISOU 4990  CD  LYS C  91     7414   6583   6637    286   -534    207       C
ATOM   4991  CE  LYS C  91     -19.257  34.785  -2.436  1.00 58.67           C
ANISOU 4991  CE  LYS C  91     8021   7122   7150    263   -571    208       C
ATOM   4992  NZ  LYS C  91     -20.376  33.948  -2.969  1.00 51.34           N
ANISOU 4992  NZ  LYS C  91     7069   6205   6232    284   -674    239       N
ATOM   4993  N   ILE C  92     -16.991  39.146   2.651  1.00 50.94           N
ANISOU 4993  N   ILE C  92     6928   6177   6249    208   -202     98       N
ATOM   4994  CA  ILE C  92     -17.065  39.917   3.875  1.00 54.52           C
ANISOU 4994  CA  ILE C  92     7344   6644   6727    208   -154     85       C
ATOM   4995  C   ILE C  92     -15.854  40.835   4.039  1.00 56.15           C
ANISOU 4995  C   ILE C  92     7607   6822   6905    166    -68     49       C
ATOM   4996  O   ILE C  92     -15.589  41.309   5.145  1.00 53.26           O
ANISOU 4996  O   ILE C  92     7209   6473   6555    148    -22     28       O
ATOM   4997  CB  ILE C  92     -17.281  39.012   5.095  1.00 50.86           C
ANISOU 4997  CB  ILE C  92     6768   6247   6309    195   -170     80       C
ATOM   4998  CG1 ILE C  92     -16.079  38.091   5.319  1.00 56.53           C
ANISOU 4998  CG1 ILE C  92     7458   7000   7021    139   -152     50       C
ATOM   4999  CG2 ILE C  92     -18.532  38.220   4.885  1.00 51.26           C
ANISOU 4999  CG2 ILE C  92     6767   6319   6389    234   -250    116       C
ATOM   5000  CD1 ILE C  92     -16.003  37.536   6.725  1.00 57.72           C
ANISOU 5000  CD1 ILE C  92     7516   7208   7206    119   -144     36       C
ATOM   5001  N   ASN C  93     -15.114  41.087   2.952  1.00 60.00           N
ANISOU 5001  N   ASN C  93     8183   7265   7350    148    -45     40       N
ATOM   5002  CA  ASN C  93     -13.989  42.044   2.939  1.00 61.98           C
ANISOU 5002  CA  ASN C  93     8497   7480   7571    107     39      6       C
ATOM   5003  C   ASN C  93     -12.969  41.677   4.009  1.00 66.70           C
ANISOU 5003  C   ASN C  93     9024   8128   8190     49     80    -32       C
ATOM   5004  O   ASN C  93     -12.527  42.518   4.799  1.00 71.13           O
ANISOU 5004  O   ASN C  93     9588   8685   8753     24    137    -57       O
ATOM   5005  CB  ASN C  93     -14.447  43.489   3.148  1.00 57.87           C
ANISOU 5005  CB  ASN C  93     8036   6913   7041    135     78     11       C
ATOM   5006  CG  ASN C  93     -15.579  43.877   2.246  1.00 58.18           C
ANISOU 5006  CG  ASN C  93     8133   6908   7065    201     31     52       C
ATOM   5007  OD1 ASN C  93     -15.392  44.122   1.049  1.00 56.04           O
ANISOU 5007  OD1 ASN C  93     7955   6585   6752    209     30     60       O
ATOM   5008  ND2 ASN C  93     -16.782  43.924   2.815  1.00 57.86           N
ANISOU 5008  ND2 ASN C  93     8039   6887   7059    252    -11     80       N
ATOM   5009  N   SER C  94     -12.582  40.410   4.021  1.00 56.55           N
ANISOU 5009  N   SER C  94     7680   6888   6919     28     49    -36       N
ATOM   5010  CA  SER C  94     -11.771  39.887   5.102  1.00 54.67           C
ANISOU 5010  CA  SER C  94     7362   6706   6704    -16     71    -67       C
ATOM   5011  C   SER C  94     -10.286  40.015   4.757  1.00 51.31           C
ANISOU 5011  C   SER C  94     6967   6270   6260    -72    131   -103       C
ATOM   5012  O   SER C  94      -9.905  39.947   3.585  1.00 52.98           O
ANISOU 5012  O   SER C  94     7242   6443   6443    -77    140   -100       O
ATOM   5013  CB  SER C  94     -12.204  38.433   5.322  1.00 55.50           C
ANISOU 5013  CB  SER C  94     7388   6864   6836     -3      5    -50       C
ATOM   5014  OG  SER C  94     -11.904  37.961   6.615  1.00 58.44           O
ANISOU 5014  OG  SER C  94     7675   7293   7236    -26      9    -68       O
ATOM   5015  N   LYS C  95      -9.446  40.208   5.783  1.00 47.42           N
ANISOU 5015  N   LYS C  95     6427   5809   5783   -117    172   -137       N
ATOM   5016  CA  LYS C  95      -7.986  40.298   5.605  1.00 47.63           C
ANISOU 5016  CA  LYS C  95     6461   5834   5801   -175    228   -175       C
ATOM   5017  C   LYS C  95      -7.360  38.916   5.788  1.00 40.75           C
ANISOU 5017  C   LYS C  95     5514   5020   4951   -192    202   -183       C
ATOM   5018  O   LYS C  95      -7.339  38.373   6.895  1.00 42.37           O
ANISOU 5018  O   LYS C  95     5637   5281   5182   -199    179   -191       O
ATOM   5019  CB  LYS C  95      -7.366  41.320   6.567  1.00 46.17           C
ANISOU 5019  CB  LYS C  95     6272   5651   5621   -217    285   -210       C
ATOM   5020  CG  LYS C  95      -5.845  41.651   6.378  1.00 38.68           C
ANISOU 5020  CG  LYS C  95     5335   4697   4667   -283    352   -253       C
ATOM   5021  CD  LYS C  95      -5.582  42.759   5.355  1.00 39.78           C
ANISOU 5021  CD  LYS C  95     5583   4761   4773   -295    412   -258       C
ATOM   5022  CE  LYS C  95      -4.090  43.139   5.323  1.00 38.78           C
ANISOU 5022  CE  LYS C  95     5457   4631   4648   -367    483   -303       C
ATOM   5023  NZ  LYS C  95      -3.672  44.039   4.189  1.00 33.27           N
ANISOU 5023  NZ  LYS C  95     4867   3858   3917   -385    549   -311       N
ATOM   5024  N   LEU C  96      -6.860  38.351   4.701  1.00 36.15           N
ANISOU 5024  N   LEU C  96     4963   4420   4353   -197    206   -180       N
ATOM   5025  CA  LEU C  96      -6.313  36.999   4.688  1.00 39.61           C
ANISOU 5025  CA  LEU C  96     5341   4903   4806   -206    182   -183       C
ATOM   5026  C   LEU C  96      -4.789  37.038   4.698  1.00 37.23           C
ANISOU 5026  C   LEU C  96     5022   4613   4512   -260    242   -222       C
ATOM   5027  O   LEU C  96      -4.166  37.676   3.840  1.00 34.11           O
ANISOU 5027  O   LEU C  96     4694   4170   4096   -283    298   -235       O
ATOM   5028  CB  LEU C  96      -6.814  36.234   3.468  1.00 39.27           C
ANISOU 5028  CB  LEU C  96     5344   4833   4742   -174    144   -152       C
ATOM   5029  CG  LEU C  96      -6.489  34.747   3.359  1.00 41.34           C
ANISOU 5029  CG  LEU C  96     5557   5136   5017   -173    111   -148       C
ATOM   5030  CD1 LEU C  96      -7.757  34.025   2.997  1.00 34.12           C
ANISOU 5030  CD1 LEU C  96     4649   4219   4096   -128     37   -109       C
ATOM   5031  CD2 LEU C  96      -5.418  34.489   2.293  1.00 39.95           C
ANISOU 5031  CD2 LEU C  96     5427   4929   4821   -197    158   -161       C
ATOM   5032  N   ILE C  97      -4.197  36.314   5.641  1.00 36.10           N
ANISOU 5032  N   ILE C  97     4788   4531   4397   -279    231   -239       N
ATOM   5033  CA  ILE C  97      -2.754  36.213   5.787  1.00 32.89           C
ANISOU 5033  CA  ILE C  97     4344   4148   4007   -327    279   -276       C
ATOM   5034  C   ILE C  97      -2.336  34.767   5.516  1.00 36.39           C
ANISOU 5034  C   ILE C  97     4740   4625   4461   -316    253   -268       C
ATOM   5035  O   ILE C  97      -2.658  33.857   6.289  1.00 37.92           O
ANISOU 5035  O   ILE C  97     4867   4868   4672   -297    201   -258       O
ATOM   5036  CB  ILE C  97      -2.336  36.680   7.172  1.00 32.31           C
ANISOU 5036  CB  ILE C  97     4205   4116   3954   -359    287   -305       C
ATOM   5037  CG1 ILE C  97      -2.593  38.174   7.230  1.00 34.61           C
ANISOU 5037  CG1 ILE C  97     4559   4361   4229   -375    327   -315       C
ATOM   5038  CG2 ILE C  97      -0.895  36.423   7.416  1.00 35.07           C
ANISOU 5038  CG2 ILE C  97     4498   4501   4328   -405    321   -340       C
ATOM   5039  CD1 ILE C  97      -2.352  38.745   8.528  1.00 35.21           C
ANISOU 5039  CD1 ILE C  97     4591   4468   4318   -405    334   -341       C
ATOM   5040  N   PHE C  98      -1.629  34.548   4.421  1.00 35.52           N
ANISOU 5040  N   PHE C  98     4671   4485   4341   -327    291   -273       N
ATOM   5041  CA  PHE C  98      -1.282  33.205   3.995  1.00 31.56           C
ANISOU 5041  CA  PHE C  98     4142   4004   3845   -312    273   -263       C
ATOM   5042  C   PHE C  98       0.130  32.857   4.413  1.00 36.78           C
ANISOU 5042  C   PHE C  98     4731   4707   4537   -347    311   -296       C
ATOM   5043  O   PHE C  98       1.066  33.636   4.192  1.00 35.76           O
ANISOU 5043  O   PHE C  98     4613   4560   4415   -388    376   -325       O
ATOM   5044  CB  PHE C  98      -1.384  33.095   2.494  1.00 34.61           C
ANISOU 5044  CB  PHE C  98     4623   4329   4198   -298    293   -245       C
ATOM   5045  CG  PHE C  98      -1.030  31.735   1.962  1.00 39.62           C
ANISOU 5045  CG  PHE C  98     5245   4976   4834   -283    280   -235       C
ATOM   5046  CD1 PHE C  98      -1.712  30.608   2.404  1.00 41.39           C
ANISOU 5046  CD1 PHE C  98     5424   5237   5063   -250    211   -212       C
ATOM   5047  CD2 PHE C  98      -0.074  31.586   0.981  1.00 34.26           C
ANISOU 5047  CD2 PHE C  98     4606   4265   4147   -299    341   -246       C
ATOM   5048  CE1 PHE C  98      -1.434  29.376   1.909  1.00 35.69           C
ANISOU 5048  CE1 PHE C  98     4700   4522   4339   -235    201   -202       C
ATOM   5049  CE2 PHE C  98       0.213  30.319   0.466  1.00 39.77           C
ANISOU 5049  CE2 PHE C  98     5299   4969   4842   -281    332   -235       C
ATOM   5050  CZ  PHE C  98      -0.470  29.221   0.941  1.00 38.14           C
ANISOU 5050  CZ  PHE C  98     5051   4801   4640   -249    261   -213       C
ATOM   5051  N   CYS C  99       0.298  31.649   4.936  1.00 33.67           N
ANISOU 5051  N   CYS C  99     4266   4366   4163   -330    272   -290       N
ATOM   5052  CA  CYS C  99       1.614  31.186   5.361  1.00 33.56           C
ANISOU 5052  CA  CYS C  99     4174   4396   4181   -354    299   -318       C
ATOM   5053  C   CYS C  99       2.304  30.511   4.178  1.00 32.86           C
ANISOU 5053  C   CYS C  99     4116   4281   4088   -350    339   -315       C
ATOM   5054  O   CYS C  99       2.033  29.346   3.853  1.00 35.07           O
ANISOU 5054  O   CYS C  99     4397   4567   4360   -315    306   -292       O
ATOM   5055  CB  CYS C  99       1.484  30.249   6.555  1.00 34.28           C
ANISOU 5055  CB  CYS C  99     4178   4554   4292   -335    239   -314       C
ATOM   5056  SG  CYS C  99       0.973  31.157   8.037  1.00 39.20           S
ANISOU 5056  SG  CYS C  99     4765   5207   4922   -351    210   -327       S
ATOM   5057  N   SER C 100       3.226  31.230   3.555  1.00 34.04           N
ANISOU 5057  N   SER C 100     4292   4400   4243   -386    413   -339       N
ATOM   5058  CA  SER C 100       3.985  30.681   2.450  1.00 35.09           C
ANISOU 5058  CA  SER C 100     4455   4505   4374   -386    465   -339       C
ATOM   5059  C   SER C 100       5.332  30.199   2.966  1.00 33.62           C
ANISOU 5059  C   SER C 100     4167   4371   4234   -406    494   -367       C
ATOM   5060  O   SER C 100       5.500  29.962   4.167  1.00 29.84           O
ANISOU 5060  O   SER C 100     3598   3956   3783   -408    453   -378       O
ATOM   5061  CB  SER C 100       4.154  31.687   1.316  1.00 35.76           C
ANISOU 5061  CB  SER C 100     4638   4515   4433   -410    536   -346       C
ATOM   5062  OG  SER C 100       4.786  31.051   0.209  1.00 36.20           O
ANISOU 5062  OG  SER C 100     4734   4539   4482   -404    585   -343       O
ATOM   5063  N   SER C 101       6.278  29.984   2.046  1.00 34.93           N
ANISOU 5063  N   SER C 101     4350   4512   4410   -417    563   -377       N
ATOM   5064  CA  SER C 101       7.536  29.327   2.355  1.00 32.29           C
ANISOU 5064  CA  SER C 101     3922   4226   4123   -426    591   -398       C
ATOM   5065  C   SER C 101       8.658  29.948   1.556  1.00 34.27           C
ANISOU 5065  C   SER C 101     4187   4441   4391   -467    691   -425       C
ATOM   5066  O   SER C 101       8.478  30.320   0.390  1.00 33.56           O
ANISOU 5066  O   SER C 101     4202   4282   4269   -471    741   -417       O
ATOM   5067  CB  SER C 101       7.498  27.837   2.035  1.00 33.01           C
ANISOU 5067  CB  SER C 101     4005   4329   4209   -376    565   -373       C
ATOM   5068  OG  SER C 101       8.796  27.285   2.198  1.00 35.29           O
ANISOU 5068  OG  SER C 101     4207   4655   4544   -382    604   -393       O
ATOM   5069  N   ASP C 102       9.844  29.968   2.171  1.00 36.14           N
ANISOU 5069  N   ASP C 102     4319   4731   4683   -497    718   -457       N
ATOM   5070  CA  ASP C 102      11.057  30.354   1.458  1.00 37.60           C
ANISOU 5070  CA  ASP C 102     4496   4892   4898   -536    818   -484       C
ATOM   5071  C   ASP C 102      11.537  29.265   0.513  1.00 34.98           C
ANISOU 5071  C   ASP C 102     4181   4540   4569   -502    859   -469       C
ATOM   5072  O   ASP C 102      12.346  29.548  -0.382  1.00 38.66           O
ANISOU 5072  O   ASP C 102     4676   4966   5049   -526    952   -484       O
ATOM   5073  CB  ASP C 102      12.173  30.662   2.465  1.00 33.99           C
ANISOU 5073  CB  ASP C 102     3908   4502   4504   -578    827   -523       C
ATOM   5074  CG  ASP C 102      12.534  29.459   3.334  1.00 31.83           C
ANISOU 5074  CG  ASP C 102     3523   4305   4264   -541    766   -517       C
ATOM   5075  OD1 ASP C 102      11.782  28.456   3.343  1.00 33.68           O
ANISOU 5075  OD1 ASP C 102     3781   4545   4471   -484    708   -484       O
ATOM   5076  OD2 ASP C 102      13.567  29.518   4.030  1.00 34.57           O
ANISOU 5076  OD2 ASP C 102     3758   4709   4666   -568    773   -547       O
ATOM   5077  N   GLN C 103      10.971  28.065   0.604  1.00 36.16           N
ANISOU 5077  N   GLN C 103     4331   4707   4701   -445    797   -438       N
ATOM   5078  CA  GLN C 103      11.371  27.023  -0.322  1.00 38.02           C
ANISOU 5078  CA  GLN C 103     4596   4917   4934   -411    837   -422       C
ATOM   5079  C   GLN C 103      11.000  27.378  -1.755  1.00 40.56           C
ANISOU 5079  C   GLN C 103     5061   5146   5205   -414    896   -409       C
ATOM   5080  O   GLN C 103      11.610  26.840  -2.693  1.00 37.82           O
ANISOU 5080  O   GLN C 103     4748   4763   4858   -402    963   -406       O
ATOM   5081  CB  GLN C 103      10.714  25.699   0.079  1.00 34.44           C
ANISOU 5081  CB  GLN C 103     4127   4495   4464   -352    755   -391       C
ATOM   5082  CG  GLN C 103      11.351  25.075   1.279  1.00 39.25           C
ANISOU 5082  CG  GLN C 103     4600   5189   5123   -340    714   -402       C
ATOM   5083  CD  GLN C 103      12.652  24.355   0.948  1.00 41.80           C
ANISOU 5083  CD  GLN C 103     4861   5529   5493   -328    778   -413       C
ATOM   5084  OE1 GLN C 103      12.953  24.073  -0.216  1.00 38.10           O
ANISOU 5084  OE1 GLN C 103     4461   5005   5012   -319    848   -406       O
ATOM   5085  NE2 GLN C 103      13.430  24.052   1.982  1.00 42.63           N
ANISOU 5085  NE2 GLN C 103     4837   5709   5651   -326    753   -430       N
ATOM   5086  N   ILE C 104      10.063  28.313  -1.952  1.00 39.52           N
ANISOU 5086  N   ILE C 104     5014   4971   5029   -429    876   -402       N
ATOM   5087  CA  ILE C 104       9.788  28.769  -3.310  1.00 39.98           C
ANISOU 5087  CA  ILE C 104     5213   4939   5038   -434    934   -391       C
ATOM   5088  C   ILE C 104      11.010  29.429  -3.914  1.00 38.87           C
ANISOU 5088  C   ILE C 104     5075   4768   4926   -480   1051   -423       C
ATOM   5089  O   ILE C 104      11.099  29.539  -5.139  1.00 41.14           O
ANISOU 5089  O   ILE C 104     5472   4980   5179   -481   1118   -416       O
ATOM   5090  CB  ILE C 104       8.515  29.639  -3.361  1.00 39.91           C
ANISOU 5090  CB  ILE C 104     5293   4894   4978   -435    884   -376       C
ATOM   5091  CG1 ILE C 104       8.588  30.870  -2.521  1.00 38.35           C
ANISOU 5091  CG1 ILE C 104     5050   4718   4802   -478    885   -402       C
ATOM   5092  CG2 ILE C 104       7.318  28.875  -2.865  1.00 45.64           C
ANISOU 5092  CG2 ILE C 104     6015   5648   5680   -389    775   -344       C
ATOM   5093  CD1 ILE C 104       7.311  31.612  -2.683  1.00 40.11           C
ANISOU 5093  CD1 ILE C 104     5368   4900   4974   -469    840   -382       C
ATOM   5094  N   TYR C 105      11.969  29.859  -3.087  1.00 35.67           N
ANISOU 5094  N   TYR C 105     4552   4418   4584   -520   1077   -457       N
ATOM   5095  CA  TYR C 105      13.209  30.383  -3.640  1.00 41.41           C
ANISOU 5095  CA  TYR C 105     5266   5120   5347   -566   1192   -489       C
ATOM   5096  C   TYR C 105      14.180  29.274  -4.069  1.00 40.82           C
ANISOU 5096  C   TYR C 105     5142   5058   5309   -541   1245   -488       C
ATOM   5097  O   TYR C 105      15.228  29.579  -4.646  1.00 45.10           O
ANISOU 5097  O   TYR C 105     5675   5575   5884   -574   1349   -512       O
ATOM   5098  CB  TYR C 105      13.924  31.289  -2.617  1.00 41.05           C
ANISOU 5098  CB  TYR C 105     5109   5130   5359   -624   1203   -529       C
ATOM   5099  CG  TYR C 105      13.307  32.652  -2.333  1.00 34.52           C
ANISOU 5099  CG  TYR C 105     4336   4277   4504   -664   1191   -540       C
ATOM   5100  CD1 TYR C 105      13.100  33.578  -3.343  1.00 36.31           C
ANISOU 5100  CD1 TYR C 105     4692   4416   4687   -689   1260   -541       C
ATOM   5101  CD2 TYR C 105      12.929  33.000  -1.044  1.00 31.63           C
ANISOU 5101  CD2 TYR C 105     3896   3971   4151   -675   1112   -549       C
ATOM   5102  CE1 TYR C 105      12.545  34.835  -3.076  1.00 37.68           C
ANISOU 5102  CE1 TYR C 105     4919   4564   4835   -723   1253   -550       C
ATOM   5103  CE2 TYR C 105      12.336  34.259  -0.757  1.00 36.13           C
ANISOU 5103  CE2 TYR C 105     4520   4515   4694   -709   1103   -558       C
ATOM   5104  CZ  TYR C 105      12.156  35.166  -1.779  1.00 39.15           C
ANISOU 5104  CZ  TYR C 105     5028   4810   5036   -732   1174   -558       C
ATOM   5105  OH  TYR C 105      11.611  36.397  -1.519  1.00 33.15           O
ANISOU 5105  OH  TYR C 105     4325   4022   4250   -762   1171   -567       O
ATOM   5106  N   ASN C 106      13.904  28.002  -3.793  1.00 38.34           N
ANISOU 5106  N   ASN C 106     4793   4780   4993   -485   1181   -464       N
ATOM   5107  CA  ASN C 106      14.900  27.018  -4.183  1.00 42.76           C
ANISOU 5107  CA  ASN C 106     5305   5350   5590   -462   1240   -465       C
ATOM   5108  C   ASN C 106      14.923  26.936  -5.704  1.00 44.39           C
ANISOU 5108  C   ASN C 106     5653   5462   5753   -455   1327   -452       C
ATOM   5109  O   ASN C 106      13.972  27.311  -6.385  1.00 46.91           O
ANISOU 5109  O   ASN C 106     6106   5715   6003   -452   1313   -433       O
ATOM   5110  CB  ASN C 106      14.648  25.656  -3.512  1.00 43.81           C
ANISOU 5110  CB  ASN C 106     5372   5542   5731   -402   1155   -442       C
ATOM   5111  CG  ASN C 106      13.417  24.899  -4.049  1.00 44.93           C
ANISOU 5111  CG  ASN C 106     5631   5641   5799   -353   1096   -401       C
ATOM   5112  OD1 ASN C 106      12.966  25.075  -5.175  1.00 42.07           O
ANISOU 5112  OD1 ASN C 106     5403   5198   5382   -352   1132   -386       O
ATOM   5113  ND2 ASN C 106      12.839  24.089  -3.183  1.00 44.95           N
ANISOU 5113  ND2 ASN C 106     5582   5697   5799   -315    999   -383       N
ATOM   5114  N   GLY C 107      16.032  26.517  -6.250  1.00 40.09           N
ANISOU 5114  N   GLY C 107     5079   4907   5248   -455   1421   -464       N
ATOM   5115  CA  GLY C 107      16.151  26.544  -7.684  1.00 46.76           C
ANISOU 5115  CA  GLY C 107     6060   5656   6050   -454   1517   -455       C
ATOM   5116  C   GLY C 107      16.652  27.848  -8.271  1.00 45.50           C
ANISOU 5116  C   GLY C 107     5951   5442   5895   -517   1618   -483       C
ATOM   5117  O   GLY C 107      17.097  27.847  -9.426  1.00 48.00           O
ANISOU 5117  O   GLY C 107     6359   5684   6194   -522   1722   -483       O
ATOM   5118  N   ASN C 108      16.568  28.964  -7.536  1.00 43.71           N
ANISOU 5118  N   ASN C 108     5677   5244   5688   -566   1594   -506       N
ATOM   5119  CA  ASN C 108      17.158  30.223  -8.004  1.00 44.85           C
ANISOU 5119  CA  ASN C 108     5858   5340   5844   -632   1697   -537       C
ATOM   5120  C   ASN C 108      18.678  30.116  -8.046  1.00 43.44           C
ANISOU 5120  C   ASN C 108     5569   5186   5749   -662   1803   -569       C
ATOM   5121  O   ASN C 108      19.296  29.690  -7.067  1.00 45.14           O
ANISOU 5121  O   ASN C 108     5625   5490   6035   -659   1768   -583       O
ATOM   5122  CB  ASN C 108      16.762  31.367  -7.078  1.00 44.84           C
ANISOU 5122  CB  ASN C 108     5819   5370   5847   -677   1643   -556       C
ATOM   5123  CG  ASN C 108      15.397  31.927  -7.389  1.00 45.84           C
ANISOU 5123  CG  ASN C 108     6087   5442   5889   -664   1585   -531       C
ATOM   5124  OD1 ASN C 108      14.399  31.579  -6.732  1.00 42.99           O
ANISOU 5124  OD1 ASN C 108     5715   5117   5502   -628   1470   -508       O
ATOM   5125  ND2 ASN C 108      15.346  32.850  -8.352  1.00 42.93           N
ANISOU 5125  ND2 ASN C 108     5849   4984   5478   -695   1665   -536       N
ATOM   5126  N   ALA C 109      19.302  30.558  -9.136  1.00 48.67           N
ANISOU 5126  N   ALA C 109     6311   5772   6408   -692   1933   -582       N
ATOM   5127  CA  ALA C 109      20.757  30.406  -9.207  1.00 48.38           C
ANISOU 5127  CA  ALA C 109     6163   5760   6458   -719   2039   -611       C
ATOM   5128  C   ALA C 109      21.520  31.614  -8.685  1.00 45.73           C
ANISOU 5128  C   ALA C 109     5741   5451   6185   -801   2089   -656       C
ATOM   5129  O   ALA C 109      22.741  31.521  -8.505  1.00 36.90           O
ANISOU 5129  O   ALA C 109     4496   4371   5152   -828   2160   -685       O
ATOM   5130  CB  ALA C 109      21.212  30.105 -10.642  1.00 43.70           C
ANISOU 5130  CB  ALA C 109     5686   5075   5843   -709   2169   -603       C
ATOM   5131  N   GLU C 110      20.840  32.731  -8.429  1.00 42.38           N
ANISOU 5131  N   GLU C 110     5378   5005   5720   -841   2054   -664       N
ATOM   5132  CA  GLU C 110      21.506  33.921  -7.921  1.00 45.13           C
ANISOU 5132  CA  GLU C 110     5654   5372   6119   -924   2100   -708       C
ATOM   5133  C   GLU C 110      22.010  33.693  -6.493  1.00 50.23           C
ANISOU 5133  C   GLU C 110     6103   6138   6846   -935   2021   -729       C
ATOM   5134  O   GLU C 110      21.589  32.759  -5.792  1.00 46.85           O
ANISOU 5134  O   GLU C 110     5611   5773   6418   -877   1913   -707       O
ATOM   5135  CB  GLU C 110      20.560  35.118  -7.960  1.00 47.15           C
ANISOU 5135  CB  GLU C 110     6034   5575   6306   -955   2074   -707       C
ATOM   5136  CG  GLU C 110      20.052  35.433  -9.353  1.00 48.92           C
ANISOU 5136  CG  GLU C 110     6459   5680   6447   -945   2146   -686       C
ATOM   5137  CD  GLU C 110      18.701  34.805  -9.621  1.00 46.35           C
ANISOU 5137  CD  GLU C 110     6246   5330   6036   -871   2046   -639       C
ATOM   5138  OE1 GLU C 110      17.987  35.281 -10.522  1.00 50.77           O
ANISOU 5138  OE1 GLU C 110     6975   5799   6516   -864   2067   -620       O
ATOM   5139  OE2 GLU C 110      18.348  33.839  -8.923  1.00 46.99           O
ANISOU 5139  OE2 GLU C 110     6244   5481   6130   -820   1944   -620       O
ATOM   5140  N   LYS C 111      22.905  34.584  -6.060  1.00 51.93           N
ANISOU 5140  N   LYS C 111     6226   6379   7126  -1013   2074   -774       N
ATOM   5141  CA  LYS C 111      23.531  34.548  -4.747  1.00 51.55           C
ANISOU 5141  CA  LYS C 111     5992   6439   7156  -1038   2010   -801       C
ATOM   5142  C   LYS C 111      23.096  35.723  -3.877  1.00 54.94           C
ANISOU 5142  C   LYS C 111     6419   6885   7571  -1097   1953   -824       C
ATOM   5143  O   LYS C 111      22.648  36.767  -4.367  1.00 54.75           O
ANISOU 5143  O   LYS C 111     6522   6787   7495  -1137   1998   -829       O
ATOM   5144  CB  LYS C 111      25.057  34.549  -4.883  1.00 57.50           C
ANISOU 5144  CB  LYS C 111     6617   7219   8011  -1084   2116   -838       C
ATOM   5145  CG  LYS C 111      25.638  33.258  -5.462  1.00 56.15           C
ANISOU 5145  CG  LYS C 111     6405   7055   7873  -1020   2161   -819       C
ATOM   5146  CD  LYS C 111      27.147  33.318  -5.424  1.00 59.61           C
ANISOU 5146  CD  LYS C 111     6693   7533   8423  -1067   2255   -857       C
ATOM   5147  CE  LYS C 111      27.665  33.335  -3.991  1.00 54.03           C
ANISOU 5147  CE  LYS C 111     5794   6943   7791  -1091   2161   -884       C
ATOM   5148  NZ  LYS C 111      29.141  33.457  -3.938  1.00 54.13           N
ANISOU 5148  NZ  LYS C 111     5652   6998   7917  -1142   2249   -924       N
ATOM   5149  N   GLY C 112      23.249  35.541  -2.561  1.00 56.07           N
ANISOU 5149  N   GLY C 112     6421   7126   7757  -1100   1853   -837       N
ATOM   5150  CA  GLY C 112      22.931  36.585  -1.614  1.00 54.86           C
ANISOU 5150  CA  GLY C 112     6251   6996   7595  -1156   1796   -861       C
ATOM   5151  C   GLY C 112      21.474  36.558  -1.200  1.00 51.09           C
ANISOU 5151  C   GLY C 112     5865   6510   7035  -1108   1686   -827       C
ATOM   5152  O   GLY C 112      20.686  35.746  -1.691  1.00 49.42           O
ANISOU 5152  O   GLY C 112     5733   6273   6773  -1034   1653   -785       O
ATOM   5153  N   PRO C 113      21.103  37.404  -0.246  1.00 42.09           N
ANISOU 5153  N   PRO C 113     4712   5396   5885  -1148   1625   -845       N
ATOM   5154  CA  PRO C 113      19.700  37.459   0.188  1.00 42.84           C
ANISOU 5154  CA  PRO C 113     4890   5481   5905  -1105   1525   -813       C
ATOM   5155  C   PRO C 113      18.758  37.769  -0.971  1.00 43.52           C
ANISOU 5155  C   PRO C 113     5159   5465   5910  -1078   1567   -783       C
ATOM   5156  O   PRO C 113      18.967  38.725  -1.725  1.00 38.31           O
ANISOU 5156  O   PRO C 113     4588   4733   5234  -1127   1662   -799       O
ATOM   5157  CB  PRO C 113      19.703  38.587   1.230  1.00 42.93           C
ANISOU 5157  CB  PRO C 113     4868   5521   5925  -1173   1492   -848       C
ATOM   5158  CG  PRO C 113      21.123  38.517   1.831  1.00 40.40           C
ANISOU 5158  CG  PRO C 113     4379   5274   5698  -1227   1513   -891       C
ATOM   5159  CD  PRO C 113      22.007  38.138   0.655  1.00 43.63           C
ANISOU 5159  CD  PRO C 113     4786   5647   6144  -1229   1629   -894       C
ATOM   5160  N   LEU C 114      17.686  36.971  -1.097  1.00 38.18           N
ANISOU 5160  N   LEU C 114     4544   4783   5181   -999   1491   -738       N
ATOM   5161  CA  LEU C 114      16.781  37.129  -2.227  1.00 38.83           C
ANISOU 5161  CA  LEU C 114     4795   4771   5186   -966   1519   -705       C
ATOM   5162  C   LEU C 114      15.585  37.992  -1.824  1.00 39.74           C
ANISOU 5162  C   LEU C 114     4996   4861   5242   -965   1458   -694       C
ATOM   5163  O   LEU C 114      15.030  37.838  -0.731  1.00 34.32           O
ANISOU 5163  O   LEU C 114     4251   4234   4556   -947   1358   -688       O
ATOM   5164  CB  LEU C 114      16.287  35.776  -2.754  1.00 40.04           C
ANISOU 5164  CB  LEU C 114     4978   4923   5314   -884   1479   -663       C
ATOM   5165  CG  LEU C 114      17.147  34.901  -3.681  1.00 41.43           C
ANISOU 5165  CG  LEU C 114     5143   5081   5517   -865   1559   -659       C
ATOM   5166  CD1 LEU C 114      17.518  35.539  -5.033  1.00 44.66           C
ANISOU 5166  CD1 LEU C 114     5675   5392   5903   -898   1688   -667       C
ATOM   5167  CD2 LEU C 114      18.391  34.443  -2.957  1.00 39.99           C
ANISOU 5167  CD2 LEU C 114     4787   4983   5426   -886   1570   -689       C
ATOM   5168  N   SER C 115      15.163  38.864  -2.735  1.00 40.32           N
ANISOU 5168  N   SER C 115     5215   4843   5262   -980   1518   -688       N
ATOM   5169  CA  SER C 115      14.054  39.763  -2.488  1.00 40.18           C
ANISOU 5169  CA  SER C 115     5289   4791   5186   -977   1473   -677       C
ATOM   5170  C   SER C 115      12.775  39.198  -3.086  1.00 41.49           C
ANISOU 5170  C   SER C 115     5563   4918   5285   -898   1412   -626       C
ATOM   5171  O   SER C 115      12.800  38.335  -3.970  1.00 39.72           O
ANISOU 5171  O   SER C 115     5377   4668   5046   -859   1430   -604       O
ATOM   5172  CB  SER C 115      14.333  41.150  -3.070  1.00 40.68           C
ANISOU 5172  CB  SER C 115     5452   4775   5230  -1040   1573   -701       C
ATOM   5173  OG  SER C 115      15.193  41.899  -2.228  1.00 47.06           O
ANISOU 5173  OG  SER C 115     6167   5623   6092  -1117   1602   -748       O
ATOM   5174  N   GLU C 116      11.644  39.729  -2.598  1.00 41.39           N
ANISOU 5174  N   GLU C 116     5599   4898   5231   -878   1341   -609       N
ATOM   5175  CA  GLU C 116      10.324  39.270  -3.004  1.00 38.76           C
ANISOU 5175  CA  GLU C 116     5354   4537   4838   -806   1269   -562       C
ATOM   5176  C   GLU C 116      10.009  39.622  -4.452  1.00 42.00           C
ANISOU 5176  C   GLU C 116     5925   4845   5188   -792   1330   -543       C
ATOM   5177  O   GLU C 116       9.076  39.053  -5.019  1.00 47.99           O
ANISOU 5177  O   GLU C 116     6758   5576   5899   -733   1277   -504       O
ATOM   5178  CB  GLU C 116       9.253  39.833  -2.066  1.00 41.59           C
ANISOU 5178  CB  GLU C 116     5713   4914   5174   -791   1186   -552       C
ATOM   5179  CG  GLU C 116       9.459  39.501  -0.579  1.00 36.99           C
ANISOU 5179  CG  GLU C 116     4985   4429   4642   -801   1119   -568       C
ATOM   5180  CD  GLU C 116      10.235  40.608   0.148  1.00 40.29           C
ANISOU 5180  CD  GLU C 116     5355   4861   5093   -878   1166   -614       C
ATOM   5181  OE1 GLU C 116      10.204  40.656   1.398  1.00 40.97           O
ANISOU 5181  OE1 GLU C 116     5352   5012   5205   -890   1108   -628       O
ATOM   5182  OE2 GLU C 116      10.882  41.437  -0.543  1.00 46.46           O
ANISOU 5182  OE2 GLU C 116     6195   5585   5871   -929   1263   -638       O
ATOM   5183  N   ASP C 117      10.717  40.574  -5.050  1.00 41.75           N
ANISOU 5183  N   ASP C 117     5956   4754   5154   -848   1437   -570       N
ATOM   5184  CA  ASP C 117      10.443  40.921  -6.441  1.00 47.59           C
ANISOU 5184  CA  ASP C 117     6860   5391   5832   -834   1498   -552       C
ATOM   5185  C   ASP C 117      11.137  39.986  -7.434  1.00 43.33           C
ANISOU 5185  C   ASP C 117     6337   4830   5298   -823   1558   -547       C
ATOM   5186  O   ASP C 117      10.812  40.021  -8.620  1.00 46.19           O
ANISOU 5186  O   ASP C 117     6840   5110   5602   -799   1593   -526       O
ATOM   5187  CB  ASP C 117      10.781  42.396  -6.716  1.00 47.06           C
ANISOU 5187  CB  ASP C 117     6875   5257   5747   -895   1590   -579       C
ATOM   5188  CG  ASP C 117      12.204  42.765  -6.340  1.00 48.33           C
ANISOU 5188  CG  ASP C 117     6939   5446   5977   -976   1680   -630       C
ATOM   5189  OD1 ASP C 117      12.861  41.939  -5.671  1.00 48.58           O
ANISOU 5189  OD1 ASP C 117     6825   5562   6074   -982   1656   -643       O
ATOM   5190  OD2 ASP C 117      12.656  43.889  -6.707  1.00 50.51           O
ANISOU 5190  OD2 ASP C 117     7285   5661   6244  -1033   1774   -656       O
ATOM   5191  N   ILE C 118      12.086  39.163  -6.988  1.00 46.87           N
ANISOU 5191  N   ILE C 118     6648   5346   5813   -836   1570   -565       N
ATOM   5192  CA  ILE C 118      12.810  38.289  -7.910  1.00 50.29           C
ANISOU 5192  CA  ILE C 118     7095   5757   6256   -824   1637   -562       C
ATOM   5193  C   ILE C 118      11.910  37.228  -8.553  1.00 51.50           C
ANISOU 5193  C   ILE C 118     7322   5889   6356   -749   1570   -516       C
ATOM   5194  O   ILE C 118      10.879  36.804  -7.994  1.00 44.86           O
ANISOU 5194  O   ILE C 118     6463   5086   5495   -703   1456   -489       O
ATOM   5195  CB  ILE C 118      14.000  37.589  -7.230  1.00 49.34           C
ANISOU 5195  CB  ILE C 118     6802   5720   6223   -848   1657   -589       C
ATOM   5196  CG1 ILE C 118      15.140  37.375  -8.241  1.00 46.32           C
ANISOU 5196  CG1 ILE C 118     6442   5293   5864   -872   1787   -605       C
ATOM   5197  CG2 ILE C 118      13.555  36.222  -6.623  1.00 39.70           C
ANISOU 5197  CG2 ILE C 118     5494   4573   5015   -784   1549   -562       C
ATOM   5198  CD1 ILE C 118      15.781  38.651  -8.743  1.00 43.14           C
ANISOU 5198  CD1 ILE C 118     6104   4825   5463   -944   1906   -638       C
ATOM   5199  N   ASP C 119      12.295  36.845  -9.778  1.00 51.53           N
ANISOU 5199  N   ASP C 119     7419   5826   6333   -740   1648   -508       N
ATOM   5200  CA  ASP C 119      11.665  35.736 -10.478  1.00 46.85           C
ANISOU 5200  CA  ASP C 119     6895   5211   5693   -676   1600   -469       C
ATOM   5201  C   ASP C 119      12.002  34.434  -9.786  1.00 42.91           C
ANISOU 5201  C   ASP C 119     6255   4799   5249   -648   1549   -466       C
ATOM   5202  O   ASP C 119      13.167  34.157  -9.498  1.00 47.75           O
ANISOU 5202  O   ASP C 119     6760   5452   5929   -676   1611   -493       O
ATOM   5203  CB  ASP C 119      12.156  35.657 -11.916  1.00 51.46           C
ANISOU 5203  CB  ASP C 119     7611   5702   6240   -679   1708   -466       C
ATOM   5204  CG  ASP C 119      11.621  36.752 -12.763  1.00 61.69           C
ANISOU 5204  CG  ASP C 119     9077   6900   7464   -690   1744   -459       C
ATOM   5205  OD1 ASP C 119      11.046  37.707 -12.195  1.00 63.80           O
ANISOU 5205  OD1 ASP C 119     9347   7173   7720   -704   1701   -463       O
ATOM   5206  OD2 ASP C 119      11.789  36.653 -13.998  1.00 74.20           O
ANISOU 5206  OD2 ASP C 119    10795   8399   8999   -684   1816   -450       O
ATOM   5207  N   VAL C 120      11.001  33.610  -9.579  1.00 45.04           N
ANISOU 5207  N   VAL C 120     6531   5094   5489   -592   1440   -432       N
ATOM   5208  CA  VAL C 120      11.184  32.382  -8.832  1.00 46.84           C
ANISOU 5208  CA  VAL C 120     6632   5405   5762   -562   1381   -427       C
ATOM   5209  C   VAL C 120      10.714  31.228  -9.696  1.00 47.99           C
ANISOU 5209  C   VAL C 120     6861   5514   5859   -508   1356   -392       C
ATOM   5210  O   VAL C 120       9.830  31.359 -10.548  1.00 49.93           O
ANISOU 5210  O   VAL C 120     7248   5690   6033   -486   1333   -366       O
ATOM   5211  CB  VAL C 120      10.451  32.407  -7.480  1.00 42.00           C
ANISOU 5211  CB  VAL C 120     5919   4870   5168   -550   1266   -422       C
ATOM   5212  CG1 VAL C 120      11.109  33.419  -6.564  1.00 41.27           C
ANISOU 5212  CG1 VAL C 120     5732   4820   5130   -607   1296   -460       C
ATOM   5213  CG2 VAL C 120       9.016  32.782  -7.691  1.00 36.05           C
ANISOU 5213  CG2 VAL C 120     5271   4078   4347   -522   1188   -392       C
ATOM   5214  N   HIS C 121      11.317  30.099  -9.457  1.00 46.89           N
ANISOU 5214  N   HIS C 121     6635   5422   5761   -487   1358   -392       N
ATOM   5215  CA  HIS C 121      11.097  28.854 -10.158  1.00 45.96           C
ANISOU 5215  CA  HIS C 121     6574   5278   5609   -440   1344   -364       C
ATOM   5216  C   HIS C 121      11.546  27.676  -9.308  1.00 43.90           C
ANISOU 5216  C   HIS C 121     6174   5102   5405   -413   1307   -365       C
ATOM   5217  O   HIS C 121      12.603  27.073  -9.548  1.00 46.42           O
ANISOU 5217  O   HIS C 121     6447   5427   5763   -410   1382   -376       O
ATOM   5218  CB  HIS C 121      11.761  28.968 -11.532  1.00 47.53           C
ANISOU 5218  CB  HIS C 121     6893   5387   5779   -452   1466   -369       C
ATOM   5219  CG  HIS C 121      13.180  29.455 -11.492  1.00 53.11           C
ANISOU 5219  CG  HIS C 121     7525   6102   6553   -499   1587   -407       C
ATOM   5220  ND1 HIS C 121      13.473  30.803 -11.438  1.00 53.43           N
ANISOU 5220  ND1 HIS C 121     7576   6122   6605   -553   1642   -433       N
ATOM   5221  CD2 HIS C 121      14.369  28.813 -11.393  1.00 51.83           C
ANISOU 5221  CD2 HIS C 121     7265   5973   6455   -501   1658   -424       C
ATOM   5222  CE1 HIS C 121      14.781  30.971 -11.383  1.00 47.54           C
ANISOU 5222  CE1 HIS C 121     6747   5391   5925   -591   1746   -466       C
ATOM   5223  NE2 HIS C 121      15.349  29.780 -11.342  1.00 50.43           N
ANISOU 5223  NE2 HIS C 121     7042   5793   6327   -559   1756   -461       N
ATOM   5224  N   PRO C 122      10.723  27.308  -8.328  1.00 45.46           N
ANISOU 5224  N   PRO C 122     6307   5362   5605   -389   1192   -350       N
ATOM   5225  CA  PRO C 122      11.058  26.215  -7.401  1.00 48.57           C
ANISOU 5225  CA  PRO C 122     6569   5837   6047   -361   1145   -349       C
ATOM   5226  C   PRO C 122      11.188  24.870  -8.107  1.00 48.73           C
ANISOU 5226  C   PRO C 122     6634   5833   6047   -316   1159   -327       C
ATOM   5227  O   PRO C 122      10.600  24.630  -9.163  1.00 47.00           O
ANISOU 5227  O   PRO C 122     6553   5541   5763   -299   1163   -304       O
ATOM   5228  CB  PRO C 122       9.876  26.214  -6.415  1.00 47.65           C
ANISOU 5228  CB  PRO C 122     6418   5769   5918   -344   1020   -332       C
ATOM   5229  CG  PRO C 122       8.789  26.989  -7.109  1.00 47.49           C
ANISOU 5229  CG  PRO C 122     6533   5681   5831   -348    996   -315       C
ATOM   5230  CD  PRO C 122       9.483  28.000  -7.953  1.00 45.19           C
ANISOU 5230  CD  PRO C 122     6311   5326   5533   -388   1104   -337       C
ATOM   5231  N   VAL C 123      11.960  23.977  -7.483  1.00 51.77           N
ANISOU 5231  N   VAL C 123     6902   6280   6487   -297   1163   -333       N
ATOM   5232  CA  VAL C 123      12.382  22.722  -8.111  1.00 55.68           C
ANISOU 5232  CA  VAL C 123     7425   6755   6977   -257   1200   -318       C
ATOM   5233  C   VAL C 123      11.723  21.467  -7.511  1.00 49.55           C
ANISOU 5233  C   VAL C 123     6616   6021   6188   -207   1101   -292       C
ATOM   5234  O   VAL C 123      11.825  20.392  -8.121  1.00 52.59           O
ANISOU 5234  O   VAL C 123     7053   6377   6551   -171   1121   -274       O
ATOM   5235  CB  VAL C 123      13.928  22.582  -8.110  1.00 49.48           C
ANISOU 5235  CB  VAL C 123     6545   5991   6263   -266   1305   -345       C
ATOM   5236  CG1 VAL C 123      14.566  23.521  -9.145  1.00 44.15           C
ANISOU 5236  CG1 VAL C 123     5948   5245   5584   -308   1427   -364       C
ATOM   5237  CG2 VAL C 123      14.510  22.901  -6.743  1.00 49.72           C
ANISOU 5237  CG2 VAL C 123     6404   6118   6370   -284   1274   -370       C
ATOM   5238  N   ASN C 124      11.053  21.563  -6.368  1.00 44.96           N
ANISOU 5238  N   ASN C 124     5960   5504   5618   -205   1002   -289       N
ATOM   5239  CA  ASN C 124      10.308  20.455  -5.769  1.00 47.83           C
ANISOU 5239  CA  ASN C 124     6301   5905   5967   -163    907   -264       C
ATOM   5240  C   ASN C 124       8.821  20.802  -5.638  1.00 50.63           C
ANISOU 5240  C   ASN C 124     6721   6247   6271   -165    812   -244       C
ATOM   5241  O   ASN C 124       8.386  21.920  -5.922  1.00 50.46           O
ANISOU 5241  O   ASN C 124     6752   6192   6227   -196    815   -249       O
ATOM   5242  CB  ASN C 124      10.881  20.063  -4.399  1.00 43.12           C
ANISOU 5242  CB  ASN C 124     5546   5403   5436   -152    871   -277       C
ATOM   5243  CG  ASN C 124      10.763  21.165  -3.370  1.00 46.50           C
ANISOU 5243  CG  ASN C 124     5893   5882   5895   -189    834   -298       C
ATOM   5244  OD1 ASN C 124      10.810  22.339  -3.699  1.00 50.13           O
ANISOU 5244  OD1 ASN C 124     6385   6311   6350   -230    873   -314       O
ATOM   5245  ND2 ASN C 124      10.644  20.786  -2.103  1.00 49.54           N
ANISOU 5245  ND2 ASN C 124     6174   6342   6308   -174    760   -298       N
ATOM   5246  N   VAL C 125       8.028  19.805  -5.237  1.00 51.86           N
ANISOU 5246  N   VAL C 125     6874   6424   6405   -131    729   -220       N
ATOM   5247  CA  VAL C 125       6.574  19.963  -5.205  1.00 50.71           C
ANISOU 5247  CA  VAL C 125     6791   6264   6213   -129    639   -197       C
ATOM   5248  C   VAL C 125       6.130  20.957  -4.124  1.00 48.98           C
ANISOU 5248  C   VAL C 125     6496   6095   6020   -152    588   -209       C
ATOM   5249  O   VAL C 125       5.188  21.729  -4.330  1.00 48.55           O
ANISOU 5249  O   VAL C 125     6502   6012   5933   -165    551   -201       O
ATOM   5250  CB  VAL C 125       5.901  18.584  -5.026  1.00 51.05           C
ANISOU 5250  CB  VAL C 125     6845   6319   6233    -91    569   -170       C
ATOM   5251  CG1 VAL C 125       4.426  18.751  -4.638  1.00 55.91           C
ANISOU 5251  CG1 VAL C 125     7483   6943   6819    -91    467   -151       C
ATOM   5252  CG2 VAL C 125       6.015  17.761  -6.317  1.00 44.07           C
ANISOU 5252  CG2 VAL C 125     6077   5365   5302    -73    611   -155       C
ATOM   5253  N   TYR C 126       6.803  20.979  -2.973  1.00 47.46           N
ANISOU 5253  N   TYR C 126     6174   5974   5883   -157    585   -228       N
ATOM   5254  CA  TYR C 126       6.363  21.857  -1.885  1.00 46.29           C
ANISOU 5254  CA  TYR C 126     5959   5872   5756   -178    534   -239       C
ATOM   5255  C   TYR C 126       6.432  23.317  -2.309  1.00 47.38           C
ANISOU 5255  C   TYR C 126     6141   5973   5889   -219    581   -257       C
ATOM   5256  O   TYR C 126       5.467  24.073  -2.146  1.00 46.83           O
ANISOU 5256  O   TYR C 126     6106   5892   5796   -228    536   -249       O
ATOM   5257  CB  TYR C 126       7.217  21.625  -0.628  1.00 39.98           C
ANISOU 5257  CB  TYR C 126     5021   5154   5016   -177    528   -259       C
ATOM   5258  CG  TYR C 126       6.748  22.393   0.572  1.00 39.02           C
ANISOU 5258  CG  TYR C 126     4834   5081   4912   -196    472   -270       C
ATOM   5259  CD1 TYR C 126       5.783  21.868   1.433  1.00 37.51           C
ANISOU 5259  CD1 TYR C 126     4619   4924   4710   -173    385   -251       C
ATOM   5260  CD2 TYR C 126       7.240  23.663   0.845  1.00 40.81           C
ANISOU 5260  CD2 TYR C 126     5029   5314   5163   -240    509   -298       C
ATOM   5261  CE1 TYR C 126       5.326  22.597   2.545  1.00 32.30           C
ANISOU 5261  CE1 TYR C 126     3906   4303   4062   -190    339   -260       C
ATOM   5262  CE2 TYR C 126       6.775  24.404   1.950  1.00 34.51           C
ANISOU 5262  CE2 TYR C 126     4182   4556   4376   -258    460   -308       C
ATOM   5263  CZ  TYR C 126       5.830  23.866   2.793  1.00 35.51           C
ANISOU 5263  CZ  TYR C 126     4286   4715   4490   -232    376   -288       C
ATOM   5264  OH  TYR C 126       5.388  24.604   3.887  1.00 37.73           O
ANISOU 5264  OH  TYR C 126     4523   5031   4781   -249    334   -298       O
ATOM   5265  N   GLY C 127       7.552  23.716  -2.910  1.00 46.05           N
ANISOU 5265  N   GLY C 127     5976   5780   5739   -242    675   -279       N
ATOM   5266  CA  GLY C 127       7.672  25.086  -3.377  1.00 44.18           C
ANISOU 5266  CA  GLY C 127     5791   5501   5495   -283    729   -296       C
ATOM   5267  C   GLY C 127       6.686  25.418  -4.480  1.00 44.43           C
ANISOU 5267  C   GLY C 127     5968   5453   5459   -277    720   -273       C
ATOM   5268  O   GLY C 127       6.066  26.480  -4.461  1.00 43.76           O
ANISOU 5268  O   GLY C 127     5925   5347   5356   -295    705   -274       O
ATOM   5269  N   LYS C 128       6.529  24.510  -5.452  1.00 46.12           N
ANISOU 5269  N   LYS C 128     6266   5621   5636   -249    728   -251       N
ATOM   5270  CA  LYS C 128       5.613  24.731  -6.571  1.00 47.23           C
ANISOU 5270  CA  LYS C 128     6553   5685   5709   -241    713   -229       C
ATOM   5271  C   LYS C 128       4.217  25.111  -6.097  1.00 44.91           C
ANISOU 5271  C   LYS C 128     6272   5402   5391   -231    614   -209       C
ATOM   5272  O   LYS C 128       3.579  26.009  -6.658  1.00 43.14           O
ANISOU 5272  O   LYS C 128     6136   5128   5130   -240    609   -202       O
ATOM   5273  CB  LYS C 128       5.508  23.466  -7.422  1.00 50.16           C
ANISOU 5273  CB  LYS C 128     6996   6019   6043   -208    711   -206       C
ATOM   5274  CG  LYS C 128       6.617  23.157  -8.391  1.00 49.67           C
ANISOU 5274  CG  LYS C 128     6984   5911   5979   -212    817   -216       C
ATOM   5275  CD  LYS C 128       6.294  21.799  -9.038  1.00 51.18           C
ANISOU 5275  CD  LYS C 128     7244   6073   6130   -176    793   -190       C
ATOM   5276  CE  LYS C 128       7.537  21.121  -9.562  1.00 52.14           C
ANISOU 5276  CE  LYS C 128     7364   6177   6271   -168    891   -201       C
ATOM   5277  NZ  LYS C 128       8.390  22.100 -10.290  1.00 53.76           N
ANISOU 5277  NZ  LYS C 128     7615   6332   6480   -200   1002   -223       N
ATOM   5278  N   HIS C 129       3.699  24.387  -5.103  1.00 46.02           N
ANISOU 5278  N   HIS C 129     6329   5605   5552   -211    535   -199       N
ATOM   5279  CA  HIS C 129       2.318  24.606  -4.688  1.00 50.28           C
ANISOU 5279  CA  HIS C 129     6879   6154   6071   -198    442   -178       C
ATOM   5280  C   HIS C 129       2.183  25.863  -3.850  1.00 44.43           C
ANISOU 5280  C   HIS C 129     6086   5439   5355   -222    438   -194       C
ATOM   5281  O   HIS C 129       1.239  26.635  -4.050  1.00 45.13           O
ANISOU 5281  O   HIS C 129     6232   5498   5416   -221    404   -182       O
ATOM   5282  CB  HIS C 129       1.772  23.385  -3.935  1.00 51.48           C
ANISOU 5282  CB  HIS C 129     6968   6358   6234   -170    365   -160       C
ATOM   5283  CG  HIS C 129       1.754  22.123  -4.754  1.00 58.12           C
ANISOU 5283  CG  HIS C 129     7871   7169   7044   -146    361   -142       C
ATOM   5284  ND1 HIS C 129       0.936  21.051  -4.455  1.00 61.71           N
ANISOU 5284  ND1 HIS C 129     8316   7644   7487   -121    285   -119       N
ATOM   5285  CD2 HIS C 129       2.464  21.756  -5.852  1.00 53.73           C
ANISOU 5285  CD2 HIS C 129     7391   6560   6465   -145    429   -143       C
ATOM   5286  CE1 HIS C 129       1.140  20.083  -5.332  1.00 56.28           C
ANISOU 5286  CE1 HIS C 129     7698   6918   6769   -107    303   -107       C
ATOM   5287  NE2 HIS C 129       2.063  20.484  -6.188  1.00 54.37           N
ANISOU 5287  NE2 HIS C 129     7509   6630   6518   -119    390   -121       N
ATOM   5288  N   LYS C 130       3.140  26.121  -2.954  1.00 46.95           N
ANISOU 5288  N   LYS C 130     6302   5811   5726   -244    474   -223       N
ATOM   5289  CA  LYS C 130       3.100  27.374  -2.199  1.00 44.72           C
ANISOU 5289  CA  LYS C 130     5981   5548   5465   -272    478   -242       C
ATOM   5290  C   LYS C 130       3.156  28.560  -3.162  1.00 43.87           C
ANISOU 5290  C   LYS C 130     5974   5368   5326   -296    538   -249       C
ATOM   5291  O   LYS C 130       2.484  29.582  -2.960  1.00 40.53           O
ANISOU 5291  O   LYS C 130     5579   4931   4891   -304    519   -248       O
ATOM   5292  CB  LYS C 130       4.261  27.435  -1.206  1.00 41.01           C
ANISOU 5292  CB  LYS C 130     5390   5141   5052   -297    513   -274       C
ATOM   5293  CG  LYS C 130       4.143  26.514   0.003  1.00 39.12           C
ANISOU 5293  CG  LYS C 130     5046   4977   4842   -275    447   -270       C
ATOM   5294  CD  LYS C 130       3.293  27.124   1.092  1.00 36.47           C
ANISOU 5294  CD  LYS C 130     4672   4674   4511   -279    386   -269       C
ATOM   5295  CE  LYS C 130       3.101  26.136   2.247  1.00 36.78           C
ANISOU 5295  CE  LYS C 130     4620   4781   4572   -255    321   -261       C
ATOM   5296  NZ  LYS C 130       2.835  26.873   3.549  1.00 36.39           N
ANISOU 5296  NZ  LYS C 130     4508   4776   4544   -271    288   -275       N
ATOM   5297  N   LEU C 131       3.940  28.443  -4.232  1.00 45.12           N
ANISOU 5297  N   LEU C 131     6196   5478   5471   -305    614   -255       N
ATOM   5298  CA  LEU C 131       3.959  29.534  -5.196  1.00 45.79           C
ANISOU 5298  CA  LEU C 131     6390   5488   5521   -326    672   -260       C
ATOM   5299  C   LEU C 131       2.605  29.682  -5.876  1.00 45.39           C
ANISOU 5299  C   LEU C 131     6451   5385   5411   -296    610   -227       C
ATOM   5300  O   LEU C 131       2.074  30.785  -5.976  1.00 45.82           O
ANISOU 5300  O   LEU C 131     6558   5407   5444   -304    608   -226       O
ATOM   5301  CB  LEU C 131       5.053  29.313  -6.226  1.00 42.09           C
ANISOU 5301  CB  LEU C 131     5972   4973   5048   -340    770   -273       C
ATOM   5302  CG  LEU C 131       5.288  30.454  -7.205  1.00 42.01           C
ANISOU 5302  CG  LEU C 131     6075   4883   5005   -368    849   -283       C
ATOM   5303  CD1 LEU C 131       5.828  31.744  -6.498  1.00 33.54           C
ANISOU 5303  CD1 LEU C 131     4947   3828   3968   -415    896   -316       C
ATOM   5304  CD2 LEU C 131       6.235  29.938  -8.263  1.00 33.77           C
ANISOU 5304  CD2 LEU C 131     5086   3792   3952   -373    938   -288       C
ATOM   5305  N   GLU C 132       2.011  28.571  -6.306  1.00 41.42           N
ANISOU 5305  N   GLU C 132     5981   4876   4881   -262    555   -199       N
ATOM   5306  CA  GLU C 132       0.752  28.644  -7.036  1.00 42.57           C
ANISOU 5306  CA  GLU C 132     6232   4972   4971   -235    492   -168       C
ATOM   5307  C   GLU C 132      -0.383  29.122  -6.146  1.00 47.54           C
ANISOU 5307  C   GLU C 132     6816   5638   5611   -222    409   -155       C
ATOM   5308  O   GLU C 132      -1.273  29.863  -6.599  1.00 43.51           O
ANISOU 5308  O   GLU C 132     6383   5083   5064   -210    378   -139       O
ATOM   5309  CB  GLU C 132       0.425  27.290  -7.642  1.00 45.84           C
ANISOU 5309  CB  GLU C 132     6686   5374   5357   -207    451   -144       C
ATOM   5310  CG  GLU C 132       1.135  27.032  -8.954  1.00 50.20           C
ANISOU 5310  CG  GLU C 132     7346   5857   5871   -212    526   -146       C
ATOM   5311  CD  GLU C 132       0.641  27.966 -10.046  1.00 59.96           C
ANISOU 5311  CD  GLU C 132     8725   7010   7048   -213    538   -136       C
ATOM   5312  OE1 GLU C 132      -0.550  27.849 -10.455  1.00 62.26           O
ANISOU 5312  OE1 GLU C 132     9084   7276   7295   -187    454   -107       O
ATOM   5313  OE2 GLU C 132       1.450  28.820 -10.490  1.00 57.82           O
ANISOU 5313  OE2 GLU C 132     8499   6698   6774   -239    630   -156       O
ATOM   5314  N   ALA C 133      -0.383  28.683  -4.882  1.00 43.66           N
ANISOU 5314  N   ALA C 133     6200   5223   5166   -221    372   -162       N
ATOM   5315  CA  ALA C 133      -1.362  29.185  -3.933  1.00 39.24           C
ANISOU 5315  CA  ALA C 133     5590   4698   4622   -211    306   -153       C
ATOM   5316  C   ALA C 133      -1.172  30.674  -3.727  1.00 44.04           C
ANISOU 5316  C   ALA C 133     6212   5287   5233   -235    352   -172       C
ATOM   5317  O   ALA C 133      -2.145  31.444  -3.688  1.00 44.72           O
ANISOU 5317  O   ALA C 133     6336   5353   5303   -221    315   -158       O
ATOM   5318  CB  ALA C 133      -1.243  28.432  -2.616  1.00 41.84           C
ANISOU 5318  CB  ALA C 133     5791   5109   4998   -208    270   -160       C
ATOM   5319  N   GLU C 134       0.083  31.101  -3.613  1.00 39.54           N
ANISOU 5319  N   GLU C 134     5616   4721   4688   -272    436   -205       N
ATOM   5320  CA  GLU C 134       0.380  32.517  -3.447  1.00 41.19           C
ANISOU 5320  CA  GLU C 134     5843   4907   4900   -303    489   -227       C
ATOM   5321  C   GLU C 134      -0.118  33.328  -4.633  1.00 44.35           C
ANISOU 5321  C   GLU C 134     6383   5222   5245   -295    508   -212       C
ATOM   5322  O   GLU C 134      -0.780  34.361  -4.464  1.00 47.03           O
ANISOU 5322  O   GLU C 134     6757   5540   5571   -292    495   -207       O
ATOM   5323  CB  GLU C 134       1.884  32.677  -3.296  1.00 41.20           C
ANISOU 5323  CB  GLU C 134     5794   4924   4936   -348    578   -264       C
ATOM   5324  CG  GLU C 134       2.366  33.817  -2.528  1.00 33.08           C
ANISOU 5324  CG  GLU C 134     4722   3911   3935   -389    618   -295       C
ATOM   5325  CD  GLU C 134       3.894  33.891  -2.583  1.00 37.93           C
ANISOU 5325  CD  GLU C 134     5292   4535   4585   -435    708   -332       C
ATOM   5326  OE1 GLU C 134       4.571  33.519  -1.580  1.00 31.86           O
ANISOU 5326  OE1 GLU C 134     4404   3837   3866   -452    703   -353       O
ATOM   5327  OE2 GLU C 134       4.423  34.310  -3.647  1.00 40.97           O
ANISOU 5327  OE2 GLU C 134     5762   4857   4949   -454    785   -339       O
ATOM   5328  N   ARG C 135       0.149  32.854  -5.850  1.00 42.74           N
ANISOU 5328  N   ARG C 135     6267   4965   5005   -289    538   -203       N
ATOM   5329  CA  ARG C 135      -0.231  33.653  -7.005  1.00 47.40           C
ANISOU 5329  CA  ARG C 135     7001   5471   5540   -282    561   -190       C
ATOM   5330  C   ARG C 135      -1.743  33.767  -7.094  1.00 50.70           C
ANISOU 5330  C   ARG C 135     7461   5875   5926   -239    464   -155       C
ATOM   5331  O   ARG C 135      -2.281  34.846  -7.355  1.00 52.64           O
ANISOU 5331  O   ARG C 135     7778   6077   6144   -232    465   -148       O
ATOM   5332  CB  ARG C 135       0.333  33.040  -8.286  1.00 48.17           C
ANISOU 5332  CB  ARG C 135     7190   5512   5601   -282    610   -186       C
ATOM   5333  CG  ARG C 135       1.842  33.110  -8.416  1.00 48.14           C
ANISOU 5333  CG  ARG C 135     7161   5504   5625   -325    721   -221       C
ATOM   5334  CD  ARG C 135       2.278  32.696  -9.825  1.00 53.80           C
ANISOU 5334  CD  ARG C 135     7998   6148   6296   -322    779   -214       C
ATOM   5335  NE  ARG C 135       1.312  33.110 -10.856  1.00 61.23           N
ANISOU 5335  NE  ARG C 135     9087   7011   7165   -295    745   -186       N
ATOM   5336  CZ  ARG C 135       0.709  32.277 -11.707  1.00 56.29           C
ANISOU 5336  CZ  ARG C 135     8544   6352   6491   -263    694   -158       C
ATOM   5337  NH1 ARG C 135      -0.149  32.742 -12.611  1.00 51.36           N
ANISOU 5337  NH1 ARG C 135     8055   5659   5802   -240    659   -134       N
ATOM   5338  NH2 ARG C 135       0.962  30.977 -11.653  1.00 50.03           N
ANISOU 5338  NH2 ARG C 135     7703   5593   5714   -253    677   -154       N
ATOM   5339  N   LYS C 136      -2.453  32.685  -6.803  1.00 50.84           N
ANISOU 5339  N   LYS C 136     7430   5934   5952   -210    380   -133       N
ATOM   5340  CA  LYS C 136      -3.902  32.758  -6.909  1.00 49.65           C
ANISOU 5340  CA  LYS C 136     7313   5774   5777   -170    287    -99       C
ATOM   5341  C   LYS C 136      -4.480  33.666  -5.832  1.00 48.45           C
ANISOU 5341  C   LYS C 136     7097   5655   5655   -166    263   -102       C
ATOM   5342  O   LYS C 136      -5.510  34.326  -6.036  1.00 51.35           O
ANISOU 5342  O   LYS C 136     7515   5994   6000   -137    218    -80       O
ATOM   5343  CB  LYS C 136      -4.503  31.366  -6.824  1.00 52.28           C
ANISOU 5343  CB  LYS C 136     7604   6144   6115   -146    207    -77       C
ATOM   5344  CG  LYS C 136      -5.990  31.309  -7.080  1.00 56.11           C
ANISOU 5344  CG  LYS C 136     8126   6617   6577   -107    108    -42       C
ATOM   5345  CD  LYS C 136      -6.310  31.723  -8.535  1.00 58.82           C
ANISOU 5345  CD  LYS C 136     8622   6874   6854    -92    107    -24       C
ATOM   5346  CE  LYS C 136      -5.750  30.733  -9.497  1.00 58.28           C
ANISOU 5346  CE  LYS C 136     8619   6774   6752    -99    127    -23       C
ATOM   5347  NZ  LYS C 136      -6.128  30.877 -10.897  1.00 62.10           N
ANISOU 5347  NZ  LYS C 136     9253   7176   7166    -83    113     -4       N
ATOM   5348  N   LEU C 137      -3.887  33.640  -4.642  1.00 51.38           N
ANISOU 5348  N   LEU C 137     7355   6090   6077   -190    286   -126       N
ATOM   5349  CA  LEU C 137      -4.430  34.452  -3.568  1.00 49.66           C
ANISOU 5349  CA  LEU C 137     7080   5903   5886   -188    265   -129       C
ATOM   5350  C   LEU C 137      -4.315  35.911  -3.916  1.00 52.97           C
ANISOU 5350  C   LEU C 137     7580   6265   6282   -200    321   -139       C
ATOM   5351  O   LEU C 137      -5.275  36.671  -3.765  1.00 54.22           O
ANISOU 5351  O   LEU C 137     7766   6407   6430   -174    287   -122       O
ATOM   5352  CB  LEU C 137      -3.722  34.169  -2.249  1.00 45.12           C
ANISOU 5352  CB  LEU C 137     6378   5401   5363   -215    282   -156       C
ATOM   5353  CG  LEU C 137      -4.110  32.833  -1.660  1.00 43.08           C
ANISOU 5353  CG  LEU C 137     6036   5203   5129   -195    214   -142       C
ATOM   5354  CD1 LEU C 137      -3.414  32.606  -0.362  1.00 39.54           C
ANISOU 5354  CD1 LEU C 137     5471   4823   4727   -219    227   -168       C
ATOM   5355  CD2 LEU C 137      -5.618  32.813  -1.492  1.00 44.43           C
ANISOU 5355  CD2 LEU C 137     6211   5376   5294   -154    130   -109       C
ATOM   5356  N   GLN C 138      -3.156  36.308  -4.436  1.00 47.53           N
ANISOU 5356  N   GLN C 138     6934   5542   5584   -238    411   -166       N
ATOM   5357  CA  GLN C 138      -2.970  37.708  -4.797  1.00 51.12           C
ANISOU 5357  CA  GLN C 138     7473   5936   6014   -255    474   -178       C
ATOM   5358  C   GLN C 138      -3.904  38.157  -5.913  1.00 57.15           C
ANISOU 5358  C   GLN C 138     8369   6626   6720   -215    445   -145       C
ATOM   5359  O   GLN C 138      -4.400  39.288  -5.882  1.00 57.22           O
ANISOU 5359  O   GLN C 138     8432   6600   6712   -204    452   -141       O
ATOM   5360  CB  GLN C 138      -1.525  37.982  -5.200  1.00 44.11           C
ANISOU 5360  CB  GLN C 138     6607   5024   5130   -307    580   -213       C
ATOM   5361  CG  GLN C 138      -0.480  37.661  -4.167  1.00 49.88           C
ANISOU 5361  CG  GLN C 138     7210   5824   5917   -350    614   -247       C
ATOM   5362  CD  GLN C 138      -0.710  38.370  -2.815  1.00 47.66           C
ANISOU 5362  CD  GLN C 138     6851   5589   5670   -363    597   -262       C
ATOM   5363  OE1 GLN C 138      -0.627  37.749  -1.744  1.00 44.48           O
ANISOU 5363  OE1 GLN C 138     6333   5260   5309   -366    559   -269       O
ATOM   5364  NE2 GLN C 138      -0.998  39.669  -2.867  1.00 47.71           N
ANISOU 5364  NE2 GLN C 138     6925   5549   5655   -370    627   -266       N
ATOM   5365  N   GLU C 139      -4.130  37.323  -6.933  1.00 68.26           N
ANISOU 5365  N   GLU C 139     9838   8004   8092   -192    414   -124       N
ATOM   5366  CA  GLU C 139      -4.905  37.808  -8.082  1.00 69.50           C
ANISOU 5366  CA  GLU C 139    10134   8085   8189   -157    389    -95       C
ATOM   5367  C   GLU C 139      -6.434  37.803  -7.776  1.00 68.53           C
ANISOU 5367  C   GLU C 139     9992   7980   8065   -104    280    -60       C
ATOM   5368  O   GLU C 139      -7.163  38.698  -8.231  1.00 71.67           O
ANISOU 5368  O   GLU C 139    10476   8327   8429    -74    263    -41       O
ATOM   5369  CB  GLU C 139      -4.257  37.160  -9.365  1.00 72.41           C
ANISOU 5369  CB  GLU C 139    10596   8401   8514   -167    428    -95       C
ATOM   5370  CG  GLU C 139      -4.616  37.202 -10.924  1.00 80.64           C
ANISOU 5370  CG  GLU C 139    11806   9353   9481   -142    419    -70       C
ATOM   5371  CD  GLU C 139      -5.036  35.823 -11.591  1.00 87.89           C
ANISOU 5371  CD  GLU C 139    12745  10274  10375   -118    348    -46       C
ATOM   5372  OE1 GLU C 139      -4.404  34.790 -11.251  1.00 85.20           O
ANISOU 5372  OE1 GLU C 139    12325   9981  10067   -138    362    -59       O
ATOM   5373  OE2 GLU C 139      -5.926  35.757 -12.495  1.00 91.05           O
ANISOU 5373  OE2 GLU C 139    13247  10626  10722    -82    283    -16       O
ATOM   5374  N   ILE C 140      -6.903  36.940  -6.863  1.00 58.39           N
ANISOU 5374  N   ILE C 140     8589   6771   6826    -93    214    -53       N
ATOM   5375  CA  ILE C 140      -8.315  36.995  -6.457  1.00 53.45           C
ANISOU 5375  CA  ILE C 140     7932   6167   6210    -47    121    -22       C
ATOM   5376  C   ILE C 140      -8.549  38.039  -5.370  1.00 52.27           C
ANISOU 5376  C   ILE C 140     7729   6039   6093    -47    139    -32       C
ATOM   5377  O   ILE C 140      -9.533  38.788  -5.412  1.00 56.25           O
ANISOU 5377  O   ILE C 140     8267   6519   6586     -9    103     -9       O
ATOM   5378  CB  ILE C 140      -8.832  35.615  -6.008  1.00 50.63           C
ANISOU 5378  CB  ILE C 140     7481   5874   5884    -35     42     -7       C
ATOM   5379  CG1 ILE C 140      -8.984  34.665  -7.209  1.00 55.90           C
ANISOU 5379  CG1 ILE C 140     8224   6508   6510    -23      3     12       C
ATOM   5380  CG2 ILE C 140     -10.106  35.735  -5.142  1.00 48.96           C
ANISOU 5380  CG2 ILE C 140     7194   5703   5706      1    -34     15       C
ATOM   5381  CD1 ILE C 140      -9.103  33.187  -6.855  1.00 54.47           C
ANISOU 5381  CD1 ILE C 140     7960   6382   6353    -26    -49     17       C
ATOM   5382  N   LEU C 141      -7.673  38.111  -4.371  1.00 53.49           N
ANISOU 5382  N   LEU C 141     7798   6238   6287    -88    194    -64       N
ATOM   5383  CA  LEU C 141      -7.898  38.957  -3.200  1.00 48.41           C
ANISOU 5383  CA  LEU C 141     7095   5623   5676    -91    207    -75       C
ATOM   5384  C   LEU C 141      -6.717  39.919  -3.060  1.00 50.04           C
ANISOU 5384  C   LEU C 141     7329   5805   5880   -142    309   -113       C
ATOM   5385  O   LEU C 141      -5.782  39.669  -2.283  1.00 48.64           O
ANISOU 5385  O   LEU C 141     7071   5675   5737   -185    348   -145       O
ATOM   5386  CB  LEU C 141      -8.074  38.070  -1.966  1.00 46.97           C
ANISOU 5386  CB  LEU C 141     6777   5525   5546    -94    163    -79       C
ATOM   5387  CG  LEU C 141      -8.697  38.480  -0.641  1.00 47.85           C
ANISOU 5387  CG  LEU C 141     6807   5679   5693    -83    142    -79       C
ATOM   5388  CD1 LEU C 141     -10.173  38.634  -0.839  1.00 48.63           C
ANISOU 5388  CD1 LEU C 141     6926   5764   5787    -25     70    -39       C
ATOM   5389  CD2 LEU C 141      -8.451  37.429   0.394  1.00 48.30           C
ANISOU 5389  CD2 LEU C 141     6746   5814   5793    -99    118    -89       C
ATOM   5390  N   PRO C 142      -6.745  41.055  -3.756  1.00 52.32           N
ANISOU 5390  N   PRO C 142     7729   6022   6129   -138    353   -112       N
ATOM   5391  CA  PRO C 142      -5.570  41.953  -3.758  1.00 52.68           C
ANISOU 5391  CA  PRO C 142     7812   6036   6169   -192    457   -150       C
ATOM   5392  C   PRO C 142      -5.170  42.479  -2.397  1.00 45.79           C
ANISOU 5392  C   PRO C 142     6851   5210   5338   -228    488   -180       C
ATOM   5393  O   PRO C 142      -4.034  42.929  -2.238  1.00 42.54           O
ANISOU 5393  O   PRO C 142     6435   4792   4934   -284    568   -217       O
ATOM   5394  CB  PRO C 142      -6.003  43.100  -4.680  1.00 51.22           C
ANISOU 5394  CB  PRO C 142     7769   5762   5931   -168    482   -135       C
ATOM   5395  CG  PRO C 142      -7.128  42.548  -5.487  1.00 54.63           C
ANISOU 5395  CG  PRO C 142     8248   6175   6333   -107    394    -91       C
ATOM   5396  CD  PRO C 142      -7.839  41.576  -4.591  1.00 54.28           C
ANISOU 5396  CD  PRO C 142     8078   6211   6335    -83    309    -76       C
ATOM   5397  N   THR C 143      -6.069  42.486  -1.423  1.00 44.20           N
ANISOU 5397  N   THR C 143     6581   5050   5161   -198    431   -166       N
ATOM   5398  CA  THR C 143      -5.735  42.942  -0.079  1.00 42.13           C
ANISOU 5398  CA  THR C 143     6241   4832   4936   -231    456   -194       C
ATOM   5399  C   THR C 143      -5.028  41.893   0.787  1.00 39.98           C
ANISOU 5399  C   THR C 143     5844   4639   4707   -263    443   -215       C
ATOM   5400  O   THR C 143      -4.642  42.216   1.917  1.00 38.81           O
ANISOU 5400  O   THR C 143     5630   4529   4586   -295    462   -241       O
ATOM   5401  CB  THR C 143      -7.018  43.394   0.622  1.00 45.90           C
ANISOU 5401  CB  THR C 143     6702   5316   5420   -182    405   -169       C
ATOM   5402  OG1 THR C 143      -7.944  42.291   0.666  1.00 43.73           O
ANISOU 5402  OG1 THR C 143     6371   5082   5161   -136    317   -136       O
ATOM   5403  CG2 THR C 143      -7.660  44.579  -0.146  1.00 40.42           C
ANISOU 5403  CG2 THR C 143     6133   4542   4683   -148    424   -149       C
ATOM   5404  N   SER C 144      -4.895  40.646   0.330  1.00 43.33           N
ANISOU 5404  N   SER C 144     6238   5090   5138   -253    407   -204       N
ATOM   5405  CA  SER C 144      -4.280  39.600   1.152  1.00 43.07           C
ANISOU 5405  CA  SER C 144     6089   5131   5144   -276    391   -221       C
ATOM   5406  C   SER C 144      -2.762  39.789   1.292  1.00 40.04           C
ANISOU 5406  C   SER C 144     5679   4757   4777   -340    468   -264       C
ATOM   5407  O   SER C 144      -2.109  40.432   0.467  1.00 40.51           O
ANISOU 5407  O   SER C 144     5815   4763   4815   -367    536   -279       O
ATOM   5408  CB  SER C 144      -4.597  38.208   0.604  1.00 34.68           C
ANISOU 5408  CB  SER C 144     5008   4088   4080   -245    333   -195       C
ATOM   5409  OG  SER C 144      -3.964  38.004  -0.624  1.00 38.66           O
ANISOU 5409  OG  SER C 144     5584   4548   4558   -256    372   -197       O
ATOM   5410  N   VAL C 145      -2.216  39.216   2.373  1.00 33.04           N
ANISOU 5410  N   VAL C 145     4684   3941   3930   -363    455   -285       N
ATOM   5411  CA  VAL C 145      -0.800  39.297   2.730  1.00 34.52           C
ANISOU 5411  CA  VAL C 145     4818   4154   4144   -423    514   -327       C
ATOM   5412  C   VAL C 145      -0.222  37.885   2.730  1.00 35.45           C
ANISOU 5412  C   VAL C 145     4860   4322   4286   -420    491   -327       C
ATOM   5413  O   VAL C 145      -0.741  36.992   3.411  1.00 36.69           O
ANISOU 5413  O   VAL C 145     4950   4531   4459   -391    425   -311       O
ATOM   5414  CB  VAL C 145      -0.592  39.946   4.111  1.00 33.52           C
ANISOU 5414  CB  VAL C 145     4629   4066   4041   -456    519   -354       C
ATOM   5415  CG1 VAL C 145       0.869  39.943   4.472  1.00 31.94           C
ANISOU 5415  CG1 VAL C 145     4366   3899   3872   -517    569   -397       C
ATOM   5416  CG2 VAL C 145      -1.135  41.380   4.129  1.00 32.37           C
ANISOU 5416  CG2 VAL C 145     4565   3866   3870   -459    549   -355       C
ATOM   5417  N   SER C 146       0.847  37.680   1.967  1.00 35.66           N
ANISOU 5417  N   SER C 146     4900   4333   4316   -448    549   -344       N
ATOM   5418  CA  SER C 146       1.520  36.395   1.922  1.00 30.60           C
ANISOU 5418  CA  SER C 146     4190   3736   3700   -445    538   -346       C
ATOM   5419  C   SER C 146       2.877  36.527   2.605  1.00 31.50           C
ANISOU 5419  C   SER C 146     4218   3893   3856   -500    585   -389       C
ATOM   5420  O   SER C 146       3.651  37.437   2.299  1.00 33.58           O
ANISOU 5420  O   SER C 146     4511   4126   4122   -546    658   -417       O
ATOM   5421  CB  SER C 146       1.649  35.908   0.484  1.00 34.05           C
ANISOU 5421  CB  SER C 146     4707   4121   4109   -429    565   -330       C
ATOM   5422  OG  SER C 146       1.852  34.496   0.457  1.00 39.38           O
ANISOU 5422  OG  SER C 146     5327   4836   4800   -406    532   -318       O
ATOM   5423  N   LEU C 147       3.122  35.657   3.572  1.00 31.20           N
ANISOU 5423  N   LEU C 147     4075   3928   3851   -494    539   -393       N
ATOM   5424  CA  LEU C 147       4.332  35.633   4.371  1.00 29.65           C
ANISOU 5424  CA  LEU C 147     3782   3785   3698   -538    563   -431       C
ATOM   5425  C   LEU C 147       5.142  34.395   3.992  1.00 31.55           C
ANISOU 5425  C   LEU C 147     3969   4055   3962   -526    570   -430       C
ATOM   5426  O   LEU C 147       4.629  33.279   4.065  1.00 33.72           O
ANISOU 5426  O   LEU C 147     4225   4354   4234   -480    513   -403       O
ATOM   5427  CB  LEU C 147       3.971  35.631   5.850  1.00 25.61           C
ANISOU 5427  CB  LEU C 147     3196   3332   3202   -536    503   -436       C
ATOM   5428  CG  LEU C 147       3.036  36.783   6.300  1.00 32.69           C
ANISOU 5428  CG  LEU C 147     4146   4200   4074   -539    493   -433       C
ATOM   5429  CD1 LEU C 147       2.612  36.559   7.721  1.00 29.69           C
ANISOU 5429  CD1 LEU C 147     3697   3877   3706   -529    431   -433       C
ATOM   5430  CD2 LEU C 147       3.676  38.170   6.185  1.00 28.82           C
ANISOU 5430  CD2 LEU C 147     3695   3673   3582   -598    566   -467       C
ATOM   5431  N   ARG C 148       6.364  34.593   3.499  1.00 31.15           N
ANISOU 5431  N   ARG C 148     3904   3995   3936   -566    644   -458       N
ATOM   5432  CA  ARG C 148       7.233  33.479   3.085  1.00 31.86           C
ANISOU 5432  CA  ARG C 148     3945   4108   4052   -554    663   -459       C
ATOM   5433  C   ARG C 148       8.059  33.039   4.284  1.00 32.80           C
ANISOU 5433  C   ARG C 148     3931   4309   4220   -570    636   -483       C
ATOM   5434  O   ARG C 148       9.106  33.624   4.578  1.00 30.03           O
ANISOU 5434  O   ARG C 148     3526   3978   3906   -622    682   -520       O
ATOM   5435  CB  ARG C 148       8.119  33.902   1.918  1.00 32.81           C
ANISOU 5435  CB  ARG C 148     4117   4176   4176   -587    762   -475       C
ATOM   5436  CG  ARG C 148       7.323  34.277   0.677  1.00 31.15           C
ANISOU 5436  CG  ARG C 148     4047   3879   3909   -567    786   -450       C
ATOM   5437  CD  ARG C 148       8.169  34.363  -0.565  1.00 31.33           C
ANISOU 5437  CD  ARG C 148     4128   3848   3930   -588    881   -460       C
ATOM   5438  NE  ARG C 148       7.310  34.514  -1.727  1.00 32.96           N
ANISOU 5438  NE  ARG C 148     4473   3975   4076   -559    887   -430       N
ATOM   5439  CZ  ARG C 148       7.743  34.783  -2.953  1.00 35.91           C
ANISOU 5439  CZ  ARG C 148     4939   4279   4428   -572    968   -432       C
ATOM   5440  NH1 ARG C 148       9.048  34.921  -3.200  1.00 31.78           N
ANISOU 5440  NH1 ARG C 148     4378   3755   3942   -616   1058   -464       N
ATOM   5441  NH2 ARG C 148       6.859  34.891  -3.938  1.00 36.73           N
ANISOU 5441  NH2 ARG C 148     5172   4313   4471   -541    959   -403       N
ATOM   5442  N   LEU C 149       7.627  31.963   4.936  1.00 30.23           N
ANISOU 5442  N   LEU C 149     3555   4033   3899   -525    562   -462       N
ATOM   5443  CA  LEU C 149       8.217  31.537   6.190  1.00 26.96           C
ANISOU 5443  CA  LEU C 149     3024   3696   3522   -532    520   -480       C
ATOM   5444  C   LEU C 149       9.405  30.604   5.959  1.00 34.28           C
ANISOU 5444  C   LEU C 149     3877   4657   4490   -526    547   -490       C
ATOM   5445  O   LEU C 149       9.531  29.957   4.909  1.00 34.78           O
ANISOU 5445  O   LEU C 149     3982   4688   4547   -500    582   -473       O
ATOM   5446  CB  LEU C 149       7.165  30.837   7.035  1.00 28.96           C
ANISOU 5446  CB  LEU C 149     3264   3983   3758   -486    431   -452       C
ATOM   5447  CG  LEU C 149       5.870  31.586   7.309  1.00 31.97           C
ANISOU 5447  CG  LEU C 149     3710   4334   4102   -480    399   -437       C
ATOM   5448  CD1 LEU C 149       4.811  30.616   7.809  1.00 30.53           C
ANISOU 5448  CD1 LEU C 149     3522   4174   3902   -427    321   -403       C
ATOM   5449  CD2 LEU C 149       6.091  32.694   8.326  1.00 25.47           C
ANISOU 5449  CD2 LEU C 149     2857   3532   3290   -526    400   -468       C
ATOM   5450  N   THR C 150      10.243  30.487   6.992  1.00 28.88           N
ANISOU 5450  N   THR C 150     3084   4040   3848   -545    526   -516       N
ATOM   5451  CA  THR C 150      11.378  29.576   6.996  1.00 29.79           C
ANISOU 5451  CA  THR C 150     3112   4200   4010   -534    540   -525       C
ATOM   5452  C   THR C 150      11.062  28.353   7.842  1.00 35.45           C
ANISOU 5452  C   THR C 150     3773   4970   4725   -480    458   -503       C
ATOM   5453  O   THR C 150      10.047  28.300   8.560  1.00 30.48           O
ANISOU 5453  O   THR C 150     3165   4350   4065   -460    392   -486       O
ATOM   5454  CB  THR C 150      12.629  30.213   7.609  1.00 36.00           C
ANISOU 5454  CB  THR C 150     3800   5029   4848   -591    566   -570       C
ATOM   5455  OG1 THR C 150      12.473  30.221   9.039  1.00 32.91           O
ANISOU 5455  OG1 THR C 150     3344   4698   4461   -593    487   -578       O
ATOM   5456  CG2 THR C 150      12.919  31.640   7.062  1.00 38.12           C
ANISOU 5456  CG2 THR C 150     4118   5248   5117   -658    643   -598       C
ATOM   5457  N   TRP C 151      11.988  27.388   7.779  1.00 35.14           N
ANISOU 5457  N   TRP C 151     3663   4967   4722   -456    467   -505       N
ATOM   5458  CA  TRP C 151      11.983  26.286   8.727  1.00 35.06           C
ANISOU 5458  CA  TRP C 151     3584   5016   4719   -411    394   -492       C
ATOM   5459  C   TRP C 151      12.096  26.877  10.120  1.00 32.78           C
ANISOU 5459  C   TRP C 151     3231   4782   4444   -441    339   -516       C
ATOM   5460  O   TRP C 151      12.949  27.732  10.380  1.00 32.13           O
ANISOU 5460  O   TRP C 151     3096   4718   4395   -495    367   -552       O
ATOM   5461  CB  TRP C 151      13.144  25.315   8.457  1.00 34.72           C
ANISOU 5461  CB  TRP C 151     3467   5005   4722   -385    421   -495       C
ATOM   5462  CG  TRP C 151      13.080  23.963   9.210  1.00 33.98           C
ANISOU 5462  CG  TRP C 151     3323   4961   4628   -323    351   -473       C
ATOM   5463  CD1 TRP C 151      11.962  23.317   9.640  1.00 37.56           C
ANISOU 5463  CD1 TRP C 151     3821   5413   5039   -282    285   -443       C
ATOM   5464  CD2 TRP C 151      14.184  23.111   9.557  1.00 34.75           C
ANISOU 5464  CD2 TRP C 151     3320   5111   4771   -295    345   -480       C
ATOM   5465  NE1 TRP C 151      12.297  22.138  10.248  1.00 33.42           N
ANISOU 5465  NE1 TRP C 151     3237   4935   4526   -233    241   -431       N
ATOM   5466  CE2 TRP C 151      13.656  21.989  10.215  1.00 37.10           C
ANISOU 5466  CE2 TRP C 151     3614   5436   5046   -238    274   -453       C
ATOM   5467  CE3 TRP C 151      15.571  23.195   9.383  1.00 35.99           C
ANISOU 5467  CE3 TRP C 151     3388   5297   4989   -313    395   -507       C
ATOM   5468  CZ2 TRP C 151      14.468  20.943  10.698  1.00 37.10           C
ANISOU 5468  CZ2 TRP C 151     3531   5489   5078   -193    250   -450       C
ATOM   5469  CZ3 TRP C 151      16.365  22.180   9.872  1.00 36.94           C
ANISOU 5469  CZ3 TRP C 151     3418   5473   5145   -269    368   -504       C
ATOM   5470  CH2 TRP C 151      15.809  21.058  10.516  1.00 35.55           C
ANISOU 5470  CH2 TRP C 151     3247   5320   4941   -207    295   -475       C
ATOM   5471  N   MET C 152      11.221  26.445  11.003  1.00 29.27           N
ANISOU 5471  N   MET C 152     2793   4359   3970   -410    264   -497       N
ATOM   5472  CA  MET C 152      11.127  27.016  12.328  1.00 30.40           C
ANISOU 5472  CA  MET C 152     2896   4542   4112   -436    210   -516       C
ATOM   5473  C   MET C 152      11.461  25.966  13.369  1.00 30.23           C
ANISOU 5473  C   MET C 152     2797   4586   4103   -397    142   -511       C
ATOM   5474  O   MET C 152      11.760  24.807  13.066  1.00 28.54           O
ANISOU 5474  O   MET C 152     2559   4385   3898   -349    138   -492       O
ATOM   5475  CB  MET C 152       9.745  27.606  12.585  1.00 28.37           C
ANISOU 5475  CB  MET C 152     2722   4251   3808   -438    184   -500       C
ATOM   5476  CG  MET C 152       9.371  28.736  11.633  1.00 31.39           C
ANISOU 5476  CG  MET C 152     3186   4568   4174   -474    247   -505       C
ATOM   5477  SD  MET C 152       7.629  29.225  11.801  1.00 34.70           S
ANISOU 5477  SD  MET C 152     3702   4943   4539   -458    214   -477       S
ATOM   5478  CE  MET C 152       6.789  27.776  11.123  1.00 36.82           C
ANISOU 5478  CE  MET C 152     4012   5195   4785   -387    186   -429       C
ATOM   5479  N   TYR C 153      11.402  26.394  14.615  1.00 27.92           N
ANISOU 5479  N   TYR C 153     2472   4332   3806   -417     89   -527       N
ATOM   5480  CA  TYR C 153      11.626  25.488  15.726  1.00 32.07           C
ANISOU 5480  CA  TYR C 153     2935   4916   4334   -381     18   -522       C
ATOM   5481  C   TYR C 153      11.081  26.174  16.960  1.00 31.10           C
ANISOU 5481  C   TYR C 153     2823   4810   4185   -407    -34   -534       C
ATOM   5482  O   TYR C 153      11.000  27.403  17.009  1.00 29.75           O
ANISOU 5482  O   TYR C 153     2676   4617   4010   -462     -9   -558       O
ATOM   5483  CB  TYR C 153      13.108  25.141  15.911  1.00 31.30           C
ANISOU 5483  CB  TYR C 153     2730   4874   4291   -385     18   -546       C
ATOM   5484  CG  TYR C 153      13.962  26.368  16.152  1.00 29.32           C
ANISOU 5484  CG  TYR C 153     2430   4639   4072   -459     42   -591       C
ATOM   5485  CD1 TYR C 153      14.026  26.959  17.402  1.00 31.27           C
ANISOU 5485  CD1 TYR C 153     2649   4922   4312   -493    -14   -615       C
ATOM   5486  CD2 TYR C 153      14.683  26.946  15.121  1.00 29.78           C
ANISOU 5486  CD2 TYR C 153     2478   4672   4166   -498    121   -610       C
ATOM   5487  CE1 TYR C 153      14.791  28.085  17.623  1.00 35.15           C
ANISOU 5487  CE1 TYR C 153     3099   5426   4830   -565      6   -657       C
ATOM   5488  CE2 TYR C 153      15.460  28.073  15.339  1.00 33.37           C
ANISOU 5488  CE2 TYR C 153     2889   5140   4652   -571    146   -653       C
ATOM   5489  CZ  TYR C 153      15.510  28.635  16.601  1.00 34.16           C
ANISOU 5489  CZ  TYR C 153     2958   5278   4743   -606     85   -677       C
ATOM   5490  OH  TYR C 153      16.269  29.750  16.853  1.00 33.32           O
ANISOU 5490  OH  TYR C 153     2811   5183   4665   -683    106   -721       O
ATOM   5491  N   ASP C 154      10.677  25.376  17.930  1.00 31.31           N
ANISOU 5491  N   ASP C 154     2840   4867   4190   -366   -101   -517       N
ATOM   5492  CA  ASP C 154      10.548  25.898  19.280  1.00 32.55           C
ANISOU 5492  CA  ASP C 154     2986   5054   4330   -390   -154   -535       C
ATOM   5493  C   ASP C 154      11.782  25.511  20.095  1.00 32.38           C
ANISOU 5493  C   ASP C 154     2865   5099   4339   -390   -199   -559       C
ATOM   5494  O   ASP C 154      12.656  24.763  19.635  1.00 35.24           O
ANISOU 5494  O   ASP C 154     3167   5486   4737   -364   -189   -557       O
ATOM   5495  CB  ASP C 154       9.253  25.415  19.941  1.00 33.11           C
ANISOU 5495  CB  ASP C 154     3116   5111   4353   -350   -198   -505       C
ATOM   5496  CG  ASP C 154       8.815  26.347  21.032  1.00 35.53           C
ANISOU 5496  CG  ASP C 154     3446   5420   4632   -387   -225   -523       C
ATOM   5497  OD1 ASP C 154       9.634  27.240  21.342  1.00 34.63           O
ANISOU 5497  OD1 ASP C 154     3295   5324   4537   -441   -220   -560       O
ATOM   5498  OD2 ASP C 154       7.693  26.221  21.569  1.00 36.21           O
ANISOU 5498  OD2 ASP C 154     3588   5489   4682   -365   -249   -501       O
ATOM   5499  N   HIS C 155      11.874  26.053  21.302  1.00 38.73           N
ANISOU 5499  N   HIS C 155     3654   5933   5130   -420   -248   -581       N
ATOM   5500  CA  HIS C 155      13.021  25.742  22.161  1.00 46.68           C
ANISOU 5500  CA  HIS C 155     4568   7005   6162   -422   -302   -604       C
ATOM   5501  C   HIS C 155      13.052  24.238  22.452  1.00 43.05           C
ANISOU 5501  C   HIS C 155     4084   6575   5697   -344   -349   -573       C
ATOM   5502  O   HIS C 155      12.014  23.650  22.737  1.00 39.83           O
ANISOU 5502  O   HIS C 155     3740   6147   5247   -303   -370   -542       O
ATOM   5503  CB  HIS C 155      12.947  26.563  23.459  1.00 47.89           C
ANISOU 5503  CB  HIS C 155     4729   7179   6290   -466   -352   -631       C
ATOM   5504  CG  HIS C 155      14.109  26.367  24.375  1.00 48.72           C
ANISOU 5504  CG  HIS C 155     4741   7350   6418   -475   -415   -657       C
ATOM   5505  ND1 HIS C 155      14.246  25.254  25.171  1.00 48.92           N
ANISOU 5505  ND1 HIS C 155     4740   7418   6431   -416   -485   -640       N
ATOM   5506  CD2 HIS C 155      15.191  27.141  24.621  1.00 54.67           C
ANISOU 5506  CD2 HIS C 155     5425   8138   7208   -536   -422   -700       C
ATOM   5507  CE1 HIS C 155      15.365  25.346  25.865  1.00 52.26           C
ANISOU 5507  CE1 HIS C 155     5077   7897   6880   -437   -536   -670       C
ATOM   5508  NE2 HIS C 155      15.958  26.484  25.551  1.00 53.95           N
ANISOU 5508  NE2 HIS C 155     5262   8110   7127   -512   -500   -708       N
ATOM   5509  N   PRO C 156      14.227  23.600  22.425  1.00 42.17           N
ANISOU 5509  N   PRO C 156     3883   6512   5629   -323   -365   -582       N
ATOM   5510  CA  PRO C 156      14.271  22.126  22.542  1.00 40.98           C
ANISOU 5510  CA  PRO C 156     3716   6381   5473   -244   -399   -549       C
ATOM   5511  C   PRO C 156      13.615  21.551  23.787  1.00 43.34           C
ANISOU 5511  C   PRO C 156     4051   6696   5721   -207   -474   -532       C
ATOM   5512  O   PRO C 156      13.025  20.467  23.718  1.00 46.35           O
ANISOU 5512  O   PRO C 156     4471   7064   6078   -145   -484   -497       O
ATOM   5513  CB  PRO C 156      15.780  21.821  22.545  1.00 42.92           C
ANISOU 5513  CB  PRO C 156     3846   6685   5778   -238   -412   -570       C
ATOM   5514  CG  PRO C 156      16.439  23.026  21.949  1.00 41.34           C
ANISOU 5514  CG  PRO C 156     3608   6478   5620   -313   -356   -607       C
ATOM   5515  CD  PRO C 156      15.574  24.195  22.333  1.00 42.66           C
ANISOU 5515  CD  PRO C 156     3850   6611   5747   -371   -353   -621       C
ATOM   5516  N   SER C 157      13.706  22.226  24.928  1.00 46.25           N
ANISOU 5516  N   SER C 157     4412   7089   6071   -243   -525   -557       N
ATOM   5517  CA  SER C 157      13.114  21.743  26.173  1.00 47.00           C
ANISOU 5517  CA  SER C 157     4547   7196   6114   -212   -594   -543       C
ATOM   5518  C   SER C 157      11.709  22.276  26.395  1.00 47.65           C
ANISOU 5518  C   SER C 157     4732   7227   6146   -229   -577   -531       C
ATOM   5519  O   SER C 157      11.251  22.313  27.536  1.00 49.13           O
ANISOU 5519  O   SER C 157     4956   7420   6290   -227   -626   -531       O
ATOM   5520  CB  SER C 157      13.985  22.124  27.370  1.00 47.93           C
ANISOU 5520  CB  SER C 157     4609   7369   6234   -238   -665   -576       C
ATOM   5521  OG  SER C 157      15.350  21.842  27.133  1.00 52.49           O
ANISOU 5521  OG  SER C 157     5078   7996   6867   -232   -679   -593       O
ATOM   5522  N   SER C 158      11.042  22.727  25.337  1.00 49.99           N
ANISOU 5522  N   SER C 158     5073   7472   6447   -247   -509   -522       N
ATOM   5523  CA  SER C 158       9.756  23.398  25.451  1.00 46.71           C
ANISOU 5523  CA  SER C 158     4747   7009   5994   -267   -487   -513       C
ATOM   5524  C   SER C 158       8.629  22.463  25.885  1.00 53.14           C
ANISOU 5524  C   SER C 158     5622   7804   6764   -213   -510   -475       C
ATOM   5525  O   SER C 158       8.506  21.332  25.399  1.00 49.51           O
ANISOU 5525  O   SER C 158     5163   7342   6309   -161   -507   -446       O
ATOM   5526  CB  SER C 158       9.394  24.009  24.103  1.00 44.62           C
ANISOU 5526  CB  SER C 158     4510   6696   5748   -292   -411   -509       C
ATOM   5527  OG  SER C 158       8.254  24.840  24.192  1.00 45.73           O
ANISOU 5527  OG  SER C 158     4727   6791   5857   -316   -389   -505       O
ATOM   5528  N   LYS C 159       7.763  22.979  26.769  1.00 55.95           N
ANISOU 5528  N   LYS C 159     6036   8142   7080   -229   -525   -476       N
ATOM   5529  CA  LYS C 159       6.568  22.245  27.174  1.00 54.21           C
ANISOU 5529  CA  LYS C 159     5879   7897   6821   -186   -536   -441       C
ATOM   5530  C   LYS C 159       5.595  22.054  26.018  1.00 53.83           C
ANISOU 5530  C   LYS C 159     5874   7801   6779   -171   -483   -412       C
ATOM   5531  O   LYS C 159       4.843  21.076  26.007  1.00 57.72           O
ANISOU 5531  O   LYS C 159     6399   8279   7253   -127   -490   -380       O
ATOM   5532  CB  LYS C 159       5.868  22.975  28.322  1.00 59.08           C
ANISOU 5532  CB  LYS C 159     6549   8501   7398   -211   -553   -451       C
ATOM   5533  N   ILE C 160       5.566  22.981  25.067  1.00 49.31           N
ANISOU 5533  N   ILE C 160     5306   7200   6228   -208   -433   -423       N
ATOM   5534  CA  ILE C 160       4.661  22.893  23.914  1.00 42.76           C
ANISOU 5534  CA  ILE C 160     4520   6324   5403   -197   -387   -397       C
ATOM   5535  C   ILE C 160       5.157  21.803  22.968  1.00 47.28           C
ANISOU 5535  C   ILE C 160     5065   6902   5996   -159   -378   -379       C
ATOM   5536  O   ILE C 160       6.346  21.817  22.583  1.00 42.91           O
ANISOU 5536  O   ILE C 160     4454   6375   5474   -169   -370   -399       O
ATOM   5537  CB  ILE C 160       4.587  24.240  23.197  1.00 43.27           C
ANISOU 5537  CB  ILE C 160     4603   6357   5481   -246   -337   -415       C
ATOM   5538  CG1 ILE C 160       4.337  25.374  24.199  1.00 46.71           C
ANISOU 5538  CG1 ILE C 160     5062   6790   5897   -287   -345   -438       C
ATOM   5539  CG2 ILE C 160       3.535  24.213  22.086  1.00 44.01           C
ANISOU 5539  CG2 ILE C 160     4750   6399   5573   -232   -298   -386       C
ATOM   5540  CD1 ILE C 160       5.613  26.102  24.688  1.00 44.61           C
ANISOU 5540  CD1 ILE C 160     4744   6560   5646   -334   -357   -481       C
ATOM   5541  N   PRO C 161       4.309  20.841  22.572  1.00 42.92           N
ANISOU 5541  N   PRO C 161     4551   6327   5431   -118   -377   -344       N
ATOM   5542  CA  PRO C 161       4.795  19.731  21.743  1.00 40.49           C
ANISOU 5542  CA  PRO C 161     4224   6022   5137    -80   -370   -328       C
ATOM   5543  C   PRO C 161       5.241  20.214  20.380  1.00 39.41           C
ANISOU 5543  C   PRO C 161     4082   5863   5030   -102   -317   -336       C
ATOM   5544  O   PRO C 161       4.701  21.172  19.820  1.00 40.00           O
ANISOU 5544  O   PRO C 161     4191   5902   5104   -135   -283   -340       O
ATOM   5545  CB  PRO C 161       3.581  18.804  21.593  1.00 35.32           C
ANISOU 5545  CB  PRO C 161     3625   5337   4457    -44   -376   -291       C
ATOM   5546  CG  PRO C 161       2.485  19.387  22.407  1.00 40.75           C
ANISOU 5546  CG  PRO C 161     4353   6010   5120    -60   -387   -287       C
ATOM   5547  CD  PRO C 161       2.953  20.617  23.098  1.00 42.70           C
ANISOU 5547  CD  PRO C 161     4580   6274   5371   -102   -390   -320       C
ATOM   5548  N   GLN C 162       6.223  19.508  19.837  1.00 37.75           N
ANISOU 5548  N   GLN C 162     3830   5670   4843    -80   -307   -336       N
ATOM   5549  CA  GLN C 162       6.705  19.786  18.498  1.00 40.14           C
ANISOU 5549  CA  GLN C 162     4132   5949   5172    -95   -251   -341       C
ATOM   5550  C   GLN C 162       7.360  18.525  17.987  1.00 41.41           C
ANISOU 5550  C   GLN C 162     4269   6120   5346    -48   -246   -326       C
ATOM   5551  O   GLN C 162       7.905  17.735  18.767  1.00 40.11           O
ANISOU 5551  O   GLN C 162     4062   5996   5183    -14   -285   -325       O
ATOM   5552  CB  GLN C 162       7.707  20.949  18.481  1.00 38.03           C
ANISOU 5552  CB  GLN C 162     3814   5699   4936   -146   -227   -380       C
ATOM   5553  CG  GLN C 162       8.984  20.631  19.166  1.00 31.98           C
ANISOU 5553  CG  GLN C 162     2963   4991   4197   -139   -255   -401       C
ATOM   5554  CD  GLN C 162       9.872  21.871  19.383  1.00 34.11           C
ANISOU 5554  CD  GLN C 162     3181   5282   4496   -199   -240   -442       C
ATOM   5555  OE1 GLN C 162      10.082  22.672  18.484  1.00 30.91           O
ANISOU 5555  OE1 GLN C 162     2786   4849   4110   -237   -184   -456       O
ATOM   5556  NE2 GLN C 162      10.366  22.029  20.591  1.00 31.84           N
ANISOU 5556  NE2 GLN C 162     2846   5042   4210   -209   -292   -462       N
ATOM   5557  N   HIS C 163       7.326  18.356  16.672  1.00 42.74           N
ANISOU 5557  N   HIS C 163     4470   6250   5521    -44   -197   -315       N
ATOM   5558  CA  HIS C 163       8.059  17.259  16.087  1.00 48.42           C
ANISOU 5558  CA  HIS C 163     5169   6974   6255     -2   -181   -304       C
ATOM   5559  C   HIS C 163       9.496  17.720  15.878  1.00 47.23           C
ANISOU 5559  C   HIS C 163     4941   6853   6152    -21   -150   -334       C
ATOM   5560  O   HIS C 163       9.837  18.896  16.066  1.00 42.19           O
ANISOU 5560  O   HIS C 163     4275   6224   5531    -72   -138   -363       O
ATOM   5561  CB  HIS C 163       7.416  16.795  14.787  1.00 55.07           C
ANISOU 5561  CB  HIS C 163     6085   7759   7081     11   -143   -278       C
ATOM   5562  CG  HIS C 163       6.027  16.247  14.934  1.00 62.55           C
ANISOU 5562  CG  HIS C 163     7100   8678   7987     29   -174   -248       C
ATOM   5563  ND1 HIS C 163       5.130  16.214  13.885  1.00 66.79           N
ANISOU 5563  ND1 HIS C 163     7712   9162   8504     25   -151   -229       N
ATOM   5564  CD2 HIS C 163       5.383  15.698  15.992  1.00 63.19           C
ANISOU 5564  CD2 HIS C 163     7186   8778   8045     51   -226   -235       C
ATOM   5565  CE1 HIS C 163       3.989  15.683  14.292  1.00 65.43           C
ANISOU 5565  CE1 HIS C 163     7580   8978   8302     40   -189   -206       C
ATOM   5566  NE2 HIS C 163       4.117  15.357  15.566  1.00 67.22           N
ANISOU 5566  NE2 HIS C 163     7768   9247   8527     56   -230   -209       N
ATOM   5567  N   LYS C 164      10.322  16.805  15.385  1.00 46.33           N
ANISOU 5567  N   LYS C 164     4797   6748   6059     17   -129   -327       N
ATOM   5568  CA  LYS C 164      11.763  17.000  15.284  1.00 45.11           C
ANISOU 5568  CA  LYS C 164     4554   6629   5955     10   -103   -352       C
ATOM   5569  C   LYS C 164      12.170  18.144  14.352  1.00 39.35           C
ANISOU 5569  C   LYS C 164     3825   5874   5254    -45    -35   -376       C
ATOM   5570  O   LYS C 164      11.953  18.097  13.138  1.00 40.96           O
ANISOU 5570  O   LYS C 164     4085   6025   5451    -46     22   -365       O
ATOM   5571  CB  LYS C 164      12.424  15.696  14.819  1.00 48.10           C
ANISOU 5571  CB  LYS C 164     4914   7012   6349     71    -86   -334       C
ATOM   5572  CG  LYS C 164      12.253  14.523  15.752  1.00 54.96           C
ANISOU 5572  CG  LYS C 164     5777   7911   7197    129   -149   -312       C
ATOM   5573  CD  LYS C 164      13.328  13.475  15.464  1.00 65.14           C
ANISOU 5573  CD  LYS C 164     7014   9219   8516    186   -131   -305       C
ATOM   5574  CE  LYS C 164      13.232  12.281  16.414  1.00 68.29           C
ANISOU 5574  CE  LYS C 164     7410   9646   8892    249   -193   -283       C
ATOM   5575  NZ  LYS C 164      13.235  12.719  17.840  1.00 61.81           N
ANISOU 5575  NZ  LYS C 164     6546   8875   8064    234   -266   -298       N
ATOM   5576  N   ASN C 165      12.701  19.206  14.920  1.00 37.71           N
ANISOU 5576  N   ASN C 165     3562   5696   5071    -95    -42   -410       N
ATOM   5577  CA  ASN C 165      13.295  20.298  14.153  1.00 37.54           C
ANISOU 5577  CA  ASN C 165     3527   5656   5081   -151     25   -438       C
ATOM   5578  C   ASN C 165      14.777  20.432  14.525  1.00 36.61           C
ANISOU 5578  C   ASN C 165     3293   5595   5024   -165     29   -469       C
ATOM   5579  O   ASN C 165      15.277  19.725  15.401  1.00 38.54           O
ANISOU 5579  O   ASN C 165     3470   5892   5280   -129    -26   -468       O
ATOM   5580  CB  ASN C 165      12.488  21.582  14.388  1.00 32.47           C
ANISOU 5580  CB  ASN C 165     2935   4989   4413   -208     22   -451       C
ATOM   5581  CG  ASN C 165      12.201  21.827  15.857  1.00 30.82           C
ANISOU 5581  CG  ASN C 165     2700   4822   4188   -216    -54   -460       C
ATOM   5582  OD1 ASN C 165      13.023  21.545  16.723  1.00 36.06           O
ANISOU 5582  OD1 ASN C 165     3283   5543   4875   -208    -95   -475       O
ATOM   5583  ND2 ASN C 165      11.013  22.302  16.146  1.00 32.11           N
ANISOU 5583  ND2 ASN C 165     2934   4957   4309   -229    -73   -450       N
ATOM   5584  N   LEU C 166      15.456  21.411  13.917  1.00 37.40           N
ANISOU 5584  N   LEU C 166     3368   5684   5159   -220     92   -498       N
ATOM   5585  CA  LEU C 166      16.920  21.489  13.956  1.00 38.51           C
ANISOU 5585  CA  LEU C 166     3395   5870   5366   -234    114   -527       C
ATOM   5586  C   LEU C 166      17.535  21.366  15.350  1.00 36.22           C
ANISOU 5586  C   LEU C 166     3008   5656   5097   -230     33   -544       C
ATOM   5587  O   LEU C 166      18.433  20.530  15.523  1.00 33.08           O
ANISOU 5587  O   LEU C 166     2529   5302   4738   -187     19   -542       O
ATOM   5588  CB  LEU C 166      17.411  22.817  13.353  1.00 37.26           C
ANISOU 5588  CB  LEU C 166     3230   5690   5239   -311    185   -561       C
ATOM   5589  CG  LEU C 166      18.937  22.767  13.192  1.00 38.94           C
ANISOU 5589  CG  LEU C 166     3323   5944   5527   -323    222   -588       C
ATOM   5590  CD1 LEU C 166      19.389  22.157  11.846  1.00 38.89           C
ANISOU 5590  CD1 LEU C 166     3332   5900   5545   -292    311   -573       C
ATOM   5591  CD2 LEU C 166      19.680  24.067  13.599  1.00 38.32           C
ANISOU 5591  CD2 LEU C 166     3178   5893   5489   -407    233   -635       C
ATOM   5592  N   PRO C 167      17.145  22.160  16.359  1.00 35.03           N
ANISOU 5592  N   PRO C 167     2862   5524   4924   -272    -21   -562       N
ATOM   5593  CA  PRO C 167      17.787  22.010  17.675  1.00 40.07           C
ANISOU 5593  CA  PRO C 167     3411   6235   5579   -267   -103   -579       C
ATOM   5594  C   PRO C 167      17.654  20.622  18.265  1.00 41.42           C
ANISOU 5594  C   PRO C 167     3573   6434   5731   -185   -165   -548       C
ATOM   5595  O   PRO C 167      18.650  20.068  18.762  1.00 41.20           O
ANISOU 5595  O   PRO C 167     3449   6463   5741   -156   -202   -555       O
ATOM   5596  CB  PRO C 167      17.076  23.069  18.529  1.00 37.85           C
ANISOU 5596  CB  PRO C 167     3175   5948   5259   -322   -142   -596       C
ATOM   5597  CG  PRO C 167      16.615  24.084  17.551  1.00 31.41           C
ANISOU 5597  CG  PRO C 167     2428   5070   4435   -375    -64   -604       C
ATOM   5598  CD  PRO C 167      16.178  23.269  16.367  1.00 32.37           C
ANISOU 5598  CD  PRO C 167     2608   5144   4546   -324    -11   -569       C
ATOM   5599  N   ILE C 168      16.471  20.009  18.148  1.00 37.74           N
ANISOU 5599  N   ILE C 168     3202   5927   5209   -144   -175   -512       N
ATOM   5600  CA  ILE C 168      16.274  18.668  18.688  1.00 38.15           C
ANISOU 5600  CA  ILE C 168     3258   6000   5238    -68   -229   -481       C
ATOM   5601  C   ILE C 168      17.155  17.658  17.955  1.00 42.52           C
ANISOU 5601  C   ILE C 168     3761   6562   5831    -13   -193   -468       C
ATOM   5602  O   ILE C 168      17.746  16.764  18.578  1.00 44.25           O
ANISOU 5602  O   ILE C 168     3922   6826   6064     41   -241   -460       O
ATOM   5603  CB  ILE C 168      14.786  18.293  18.608  1.00 37.95           C
ANISOU 5603  CB  ILE C 168     3348   5923   5148    -45   -237   -447       C
ATOM   5604  CG1 ILE C 168      13.962  19.230  19.509  1.00 34.10           C
ANISOU 5604  CG1 ILE C 168     2901   5433   4623    -91   -278   -459       C
ATOM   5605  CG2 ILE C 168      14.597  16.849  18.959  1.00 39.07           C
ANISOU 5605  CG2 ILE C 168     3502   6076   5266     33   -277   -414       C
ATOM   5606  CD1 ILE C 168      12.501  19.267  19.170  1.00 34.81           C
ANISOU 5606  CD1 ILE C 168     3100   5466   4663    -90   -264   -433       C
ATOM   5607  N   MET C 169      17.288  17.805  16.630  1.00 35.45           N
ANISOU 5607  N   MET C 169     2889   5622   4957    -25   -106   -466       N
ATOM   5608  CA  MET C 169      18.099  16.867  15.865  1.00 39.76           C
ANISOU 5608  CA  MET C 169     3396   6169   5540     27    -61   -453       C
ATOM   5609  C   MET C 169      19.568  16.975  16.234  1.00 43.85           C
ANISOU 5609  C   MET C 169     3779   6753   6130     24    -68   -481       C
ATOM   5610  O   MET C 169      20.282  15.969  16.240  1.00 44.14           O
ANISOU 5610  O   MET C 169     3759   6816   6195     87    -73   -468       O
ATOM   5611  CB  MET C 169      17.948  17.103  14.373  1.00 37.26           C
ANISOU 5611  CB  MET C 169     3141   5788   5228      9     38   -448       C
ATOM   5612  CG  MET C 169      16.695  16.551  13.819  1.00 38.44           C
ANISOU 5612  CG  MET C 169     3413   5877   5317     36     46   -412       C
ATOM   5613  SD  MET C 169      16.555  17.054  12.103  1.00 43.15           S
ANISOU 5613  SD  MET C 169     4085   6397   5915      3    156   -412       S
ATOM   5614  CE  MET C 169      14.850  17.645  12.142  1.00 46.59           C
ANISOU 5614  CE  MET C 169     4642   6781   6277    -28    126   -397       C
ATOM   5615  N   LEU C 170      20.042  18.198  16.504  1.00 42.56           N
ANISOU 5615  N   LEU C 170     3561   6612   5998    -50    -65   -520       N
ATOM   5616  CA  LEU C 170      21.414  18.383  16.932  1.00 38.80           C
ANISOU 5616  CA  LEU C 170     2948   6201   5592    -62    -80   -550       C
ATOM   5617  C   LEU C 170      21.637  17.765  18.305  1.00 45.10           C
ANISOU 5617  C   LEU C 170     3691   7064   6381    -19   -188   -546       C
ATOM   5618  O   LEU C 170      22.721  17.231  18.582  1.00 47.27           O
ANISOU 5618  O   LEU C 170     3859   7393   6709     18   -210   -551       O
ATOM   5619  CB  LEU C 170      21.763  19.867  16.922  1.00 49.32           C
ANISOU 5619  CB  LEU C 170     4249   7538   6954   -159    -54   -593       C
ATOM   5620  CG  LEU C 170      22.162  20.523  15.593  1.00 53.16           C
ANISOU 5620  CG  LEU C 170     4740   7979   7478   -206     60   -609       C
ATOM   5621  CD1 LEU C 170      22.449  22.005  15.805  1.00 45.30           C
ANISOU 5621  CD1 LEU C 170     3718   6991   6505   -304     73   -653       C
ATOM   5622  CD2 LEU C 170      23.386  19.845  14.965  1.00 45.67           C
ANISOU 5622  CD2 LEU C 170     3696   7054   6603   -168    113   -609       C
ATOM   5623  N   LEU C 171      20.643  17.872  19.195  1.00 46.96           N
ANISOU 5623  N   LEU C 171     3997   7295   6552    -23   -256   -537       N
ATOM   5624  CA  LEU C 171      20.741  17.232  20.506  1.00 48.36           C
ANISOU 5624  CA  LEU C 171     4142   7524   6708     22   -358   -530       C
ATOM   5625  C   LEU C 171      20.768  15.711  20.394  1.00 51.90           C
ANISOU 5625  C   LEU C 171     4600   7973   7147    121   -369   -491       C
ATOM   5626  O   LEU C 171      21.519  15.033  21.116  1.00 51.62           O
ANISOU 5626  O   LEU C 171     4489   7992   7132    172   -429   -488       O
ATOM   5627  CB  LEU C 171      19.580  17.682  21.388  1.00 43.89           C
ANISOU 5627  CB  LEU C 171     3664   6941   6072     -4   -414   -527       C
ATOM   5628  CG  LEU C 171      19.814  19.066  22.009  1.00 48.06           C
ANISOU 5628  CG  LEU C 171     4159   7492   6609    -91   -437   -570       C
ATOM   5629  CD1 LEU C 171      18.704  19.473  22.981  1.00 33.43           C
ANISOU 5629  CD1 LEU C 171     2394   5624   4686   -112   -493   -568       C
ATOM   5630  CD2 LEU C 171      21.191  19.095  22.692  1.00 41.49           C
ANISOU 5630  CD2 LEU C 171     3193   6736   5834    -95   -491   -599       C
ATOM   5631  N   GLU C 172      19.930  15.152  19.526  1.00 46.86           N
ANISOU 5631  N   GLU C 172     4059   7273   6474    150   -315   -459       N
ATOM   5632  CA  GLU C 172      19.920  13.703  19.374  1.00 53.69           C
ANISOU 5632  CA  GLU C 172     4944   8131   7325    240   -319   -422       C
ATOM   5633  C   GLU C 172      21.250  13.199  18.834  1.00 53.73           C
ANISOU 5633  C   GLU C 172     4847   8165   7402    280   -281   -425       C
ATOM   5634  O   GLU C 172      21.789  12.202  19.330  1.00 55.83           O
ANISOU 5634  O   GLU C 172     5066   8467   7677    353   -324   -409       O
ATOM   5635  CB  GLU C 172      18.769  13.270  18.474  1.00 50.42           C
ANISOU 5635  CB  GLU C 172     4655   7642   6862    254   -267   -390       C
ATOM   5636  CG  GLU C 172      17.449  13.291  19.210  1.00 57.61           C
ANISOU 5636  CG  GLU C 172     5659   8531   7700    246   -320   -376       C
ATOM   5637  CD  GLU C 172      16.269  12.873  18.352  1.00 59.20           C
ANISOU 5637  CD  GLU C 172     5979   8661   7854    256   -275   -346       C
ATOM   5638  OE1 GLU C 172      15.150  12.836  18.920  1.00 59.60           O
ANISOU 5638  OE1 GLU C 172     6103   8693   7850    251   -315   -332       O
ATOM   5639  OE2 GLU C 172      16.466  12.567  17.141  1.00 54.00           O
ANISOU 5639  OE2 GLU C 172     5339   7966   7214    268   -203   -336       O
ATOM   5640  N   ALA C 173      21.818  13.908  17.856  1.00 53.84           N
ANISOU 5640  N   ALA C 173     4823   8165   7468    233   -199   -447       N
ATOM   5641  CA  ALA C 173      23.104  13.507  17.312  1.00 55.75           C
ANISOU 5641  CA  ALA C 173     4963   8435   7786    266   -152   -453       C
ATOM   5642  C   ALA C 173      24.143  13.391  18.416  1.00 61.90           C
ANISOU 5642  C   ALA C 173     5611   9297   8609    287   -233   -470       C
ATOM   5643  O   ALA C 173      24.921  12.427  18.438  1.00 63.98           O
ANISOU 5643  O   ALA C 173     5810   9591   8908    362   -239   -455       O
ATOM   5644  CB  ALA C 173      23.556  14.503  16.245  1.00 56.49           C
ANISOU 5644  CB  ALA C 173     5032   8502   7928    196    -55   -480       C
ATOM   5645  N   LYS C 174      24.127  14.319  19.385  1.00 56.34           N
ANISOU 5645  N   LYS C 174     4875   8632   7900    227   -302   -499       N
ATOM   5646  CA  LYS C 174      25.064  14.205  20.499  1.00 58.45           C
ANISOU 5646  CA  LYS C 174     5025   8981   8204    246   -391   -516       C
ATOM   5647  C   LYS C 174      24.681  13.049  21.406  1.00 60.42           C
ANISOU 5647  C   LYS C 174     5313   9245   8399    332   -476   -482       C
ATOM   5648  O   LYS C 174      25.555  12.332  21.905  1.00 57.89           O
ANISOU 5648  O   LYS C 174     4905   8978   8113    395   -525   -476       O
ATOM   5649  CB  LYS C 174      25.122  15.506  21.299  1.00 53.82           C
ANISOU 5649  CB  LYS C 174     4405   8426   7618    155   -443   -557       C
ATOM   5650  N   GLU C 175      23.380  12.799  21.540  1.00 62.17           N
ANISOU 5650  N   GLU C 175     5667   9416   8538    339   -486   -457       N
ATOM   5651  CA  GLU C 175      22.898  11.746  22.422  1.00 60.85           C
ANISOU 5651  CA  GLU C 175     5552   9255   8313    414   -561   -426       C
ATOM   5652  C   GLU C 175      23.351  10.371  21.936  1.00 63.53           C
ANISOU 5652  C   GLU C 175     5879   9591   8670    512   -535   -392       C
ATOM   5653  O   GLU C 175      23.708   9.508  22.748  1.00 63.94           O
ANISOU 5653  O   GLU C 175     5903   9679   8712    584   -605   -376       O
ATOM   5654  CB  GLU C 175      21.372  11.851  22.518  1.00 64.14           C
ANISOU 5654  CB  GLU C 175     6112   9613   8646    391   -561   -408       C
ATOM   5655  CG  GLU C 175      20.727  11.121  23.685  1.00 72.83           C
ANISOU 5655  CG  GLU C 175     7274  10720   9678    439   -647   -385       C
ATOM   5656  CD  GLU C 175      20.109   9.779  23.298  1.00 81.73           C
ANISOU 5656  CD  GLU C 175     8487  11802  10764    517   -623   -341       C
ATOM   5657  OE1 GLU C 175      19.526   9.659  22.187  1.00 83.93           O
ANISOU 5657  OE1 GLU C 175     8833  12023  11035    509   -543   -326       O
ATOM   5658  OE2 GLU C 175      20.220   8.836  24.111  1.00 83.19           O
ANISOU 5658  OE2 GLU C 175     8677  12008  10921    587   -686   -320       O
ATOM   5659  N   LYS C 176      23.351  10.153  20.617  1.00 64.91           N
ANISOU 5659  N   LYS C 176     6079   9717   8867    519   -433   -381       N
ATOM   5660  CA  LYS C 176      23.714   8.878  20.007  1.00 64.10           C
ANISOU 5660  CA  LYS C 176     5981   9598   8777    609   -392   -348       C
ATOM   5661  C   LYS C 176      25.140   8.840  19.453  1.00 67.36           C
ANISOU 5661  C   LYS C 176     6262  10048   9284    630   -344   -362       C
ATOM   5662  O   LYS C 176      25.585   7.781  18.975  1.00 61.00           O
ANISOU 5662  O   LYS C 176     5447   9233   8498    710   -308   -337       O
ATOM   5663  CB  LYS C 176      22.723   8.550  18.889  1.00 59.34           C
ANISOU 5663  CB  LYS C 176     5506   8910   8130    607   -309   -324       C
ATOM   5664  N   ASN C 177      25.863   9.965  19.511  1.00 65.08           N
ANISOU 5664  N   ASN C 177     5872   9800   9057    559   -342   -403       N
ATOM   5665  CA  ASN C 177      27.225  10.076  18.975  1.00 61.63           C
ANISOU 5665  CA  ASN C 177     5299   9400   8718    565   -291   -422       C
ATOM   5666  C   ASN C 177      27.252   9.685  17.499  1.00 66.72           C
ANISOU 5666  C   ASN C 177     5988   9982   9381    585   -164   -405       C
ATOM   5667  O   ASN C 177      28.174   9.014  17.023  1.00 68.22           O
ANISOU 5667  O   ASN C 177     6106  10184   9629    646   -117   -395       O
ATOM   5668  CB  ASN C 177      28.220   9.265  19.793  1.00 61.24           C
ANISOU 5668  CB  ASN C 177     5138   9421   8708    648   -365   -414       C
ATOM   5669  CG  ASN C 177      28.858  10.086  20.882  1.00 62.51           C
ANISOU 5669  CG  ASN C 177     5187   9661   8904    600   -458   -450       C
ATOM   5670  OD1 ASN C 177      29.547  11.074  20.610  1.00 60.02           O
ANISOU 5670  OD1 ASN C 177     4778   9372   8656    528   -427   -488       O
ATOM   5671  ND2 ASN C 177      28.617   9.698  22.133  1.00 65.28           N
ANISOU 5671  ND2 ASN C 177     5552  10046   9206    637   -574   -441       N
ATOM   5672  N   VAL C 178      26.191  10.057  16.795  1.00 64.97           N
ANISOU 5672  N   VAL C 178     5893   9689   9105    538   -110   -399       N
ATOM   5673  CA  VAL C 178      26.035   9.878  15.356  1.00 65.42           C
ANISOU 5673  CA  VAL C 178     6017   9675   9165    538      9   -386       C
ATOM   5674  C   VAL C 178      26.035  11.258  14.704  1.00 64.17           C
ANISOU 5674  C   VAL C 178     5855   9494   9031    435     73   -421       C
ATOM   5675  O   VAL C 178      25.217  12.110  15.081  1.00 64.38           O
ANISOU 5675  O   VAL C 178     5937   9510   9013    368     37   -435       O
ATOM   5676  CB  VAL C 178      24.746   9.119  15.031  1.00 61.80           C
ANISOU 5676  CB  VAL C 178     5719   9146   8616    571     16   -349       C
ATOM   5677  CG1 VAL C 178      24.681   8.825  13.538  1.00 59.05           C
ANISOU 5677  CG1 VAL C 178     5440   8725   8270    579    135   -335       C
ATOM   5678  CG2 VAL C 178      24.666   7.875  15.876  1.00 58.40           C
ANISOU 5678  CG2 VAL C 178     5298   8739   8154    662    -59   -318       C
ATOM   5679  N   PRO C 179      26.917  11.525  13.741  1.00 63.73           N
ANISOU 5679  N   PRO C 179     5740   9430   9046    420    171   -436       N
ATOM   5680  CA  PRO C 179      27.001  12.872  13.156  1.00 59.92           C
ANISOU 5680  CA  PRO C 179     5251   8928   8590    320    234   -472       C
ATOM   5681  C   PRO C 179      25.731  13.254  12.400  1.00 65.02           C
ANISOU 5681  C   PRO C 179     6057   9490   9160    278    278   -460       C
ATOM   5682  O   PRO C 179      25.116  12.424  11.725  1.00 63.85           O
ANISOU 5682  O   PRO C 179     6012   9283   8963    327    314   -427       O
ATOM   5683  CB  PRO C 179      28.197  12.757  12.204  1.00 64.29           C
ANISOU 5683  CB  PRO C 179     5719   9479   9229    333    340   -481       C
ATOM   5684  CG  PRO C 179      29.038  11.636  12.813  1.00 65.40           C
ANISOU 5684  CG  PRO C 179     5757   9680   9412    429    292   -464       C
ATOM   5685  CD  PRO C 179      28.004  10.651  13.262  1.00 67.22           C
ANISOU 5685  CD  PRO C 179     6100   9886   9553    494    226   -425       C
ATOM   5686  N   PHE C 180      25.330  14.524  12.546  1.00 63.96           N
ANISOU 5686  N   PHE C 180     5942   9349   9013    188    271   -489       N
ATOM   5687  CA  PHE C 180      24.214  15.119  11.810  1.00 58.01           C
ANISOU 5687  CA  PHE C 180     5326   8520   8197    139    314   -483       C
ATOM   5688  C   PHE C 180      24.714  15.672  10.480  1.00 55.93           C
ANISOU 5688  C   PHE C 180     5072   8208   7973     98    439   -498       C
ATOM   5689  O   PHE C 180      25.483  16.636  10.475  1.00 56.09           O
ANISOU 5689  O   PHE C 180     5009   8253   8052     35    470   -535       O
ATOM   5690  CB  PHE C 180      23.598  16.238  12.654  1.00 56.75           C
ANISOU 5690  CB  PHE C 180     5179   8376   8007     66    248   -507       C
ATOM   5691  CG  PHE C 180      22.512  17.027  11.955  1.00 53.54           C
ANISOU 5691  CG  PHE C 180     4901   7897   7544     10    290   -505       C
ATOM   5692  CD1 PHE C 180      22.813  18.159  11.225  1.00 47.79           C
ANISOU 5692  CD1 PHE C 180     4175   7141   6845    -64    367   -534       C
ATOM   5693  CD2 PHE C 180      21.187  16.638  12.049  1.00 51.81           C
ANISOU 5693  CD2 PHE C 180     4801   7638   7246     33    250   -475       C
ATOM   5694  CE1 PHE C 180      21.837  18.874  10.600  1.00 45.57           C
ANISOU 5694  CE1 PHE C 180     4012   6793   6511   -109    402   -531       C
ATOM   5695  CE2 PHE C 180      20.192  17.370  11.409  1.00 51.39           C
ANISOU 5695  CE2 PHE C 180     4861   7521   7145    -14    284   -473       C
ATOM   5696  CZ  PHE C 180      20.527  18.489  10.692  1.00 48.18           C
ANISOU 5696  CZ  PHE C 180     4456   7087   6765    -83    358   -501       C
ATOM   5697  N   VAL C 181      24.204  15.164   9.356  1.00 51.80           N
ANISOU 5697  N   VAL C 181     4660   7610   7411    126    511   -472       N
ATOM   5698  CA  VAL C 181      24.764  15.553   8.059  1.00 60.11           C
ANISOU 5698  CA  VAL C 181     5726   8612   8500     97    636   -483       C
ATOM   5699  C   VAL C 181      24.044  16.790   7.527  1.00 57.73           C
ANISOU 5699  C   VAL C 181     5516   8256   8161     13    672   -500       C
ATOM   5700  O   VAL C 181      22.827  16.780   7.308  1.00 56.47           O
ANISOU 5700  O   VAL C 181     5485   8046   7924     11    650   -479       O
ATOM   5701  CB  VAL C 181      24.722  14.398   7.042  1.00 58.92           C
ANISOU 5701  CB  VAL C 181     5650   8405   8330    168    705   -449       C
ATOM   5702  CG1 VAL C 181      25.246  14.859   5.678  1.00 55.42           C
ANISOU 5702  CG1 VAL C 181     5236   7903   7917    135    840   -461       C
ATOM   5703  CG2 VAL C 181      25.594  13.253   7.528  1.00 51.21           C
ANISOU 5703  CG2 VAL C 181     4572   7483   7401    252    682   -435       C
ATOM   5704  N   THR C 182      24.826  17.834   7.267  1.00 56.75           N
ANISOU 5704  N   THR C 182     5328   8140   8094    -55    732   -537       N
ATOM   5705  CA  THR C 182      24.362  19.043   6.601  1.00 53.64           C
ANISOU 5705  CA  THR C 182     5017   7689   7675   -134    788   -555       C
ATOM   5706  C   THR C 182      25.291  19.306   5.419  1.00 56.70           C
ANISOU 5706  C   THR C 182     5389   8038   8116   -157    921   -570       C
ATOM   5707  O   THR C 182      25.993  18.417   4.922  1.00 60.85           O
ANISOU 5707  O   THR C 182     5879   8563   8680   -101    976   -557       O
ATOM   5708  CB  THR C 182      24.313  20.237   7.559  1.00 47.34           C
ANISOU 5708  CB  THR C 182     4167   6933   6886   -210    728   -589       C
ATOM   5709  OG1 THR C 182      23.984  21.418   6.822  1.00 48.40           O
ANISOU 5709  OG1 THR C 182     4382   7008   7001   -284    796   -607       O
ATOM   5710  CG2 THR C 182      25.629  20.436   8.218  1.00 51.01           C
ANISOU 5710  CG2 THR C 182     4464   7476   7440   -228    718   -622       C
ATOM   5711  N   THR C 183      25.324  20.550   4.954  1.00 53.85           N
ANISOU 5711  N   THR C 183     5058   7642   7761   -239    981   -598       N
ATOM   5712  CA  THR C 183      26.112  20.847   3.767  1.00 55.11           C
ANISOU 5712  CA  THR C 183     5222   7755   7963   -264   1117   -612       C
ATOM   5713  C   THR C 183      26.474  22.312   3.668  1.00 52.09           C
ANISOU 5713  C   THR C 183     4818   7364   7611   -364   1166   -654       C
ATOM   5714  O   THR C 183      25.795  23.180   4.225  1.00 52.11           O
ANISOU 5714  O   THR C 183     4855   7368   7574   -415   1108   -666       O
ATOM   5715  CB  THR C 183      25.374  20.410   2.504  1.00 56.31           C
ANISOU 5715  CB  THR C 183     5537   7810   8047   -233   1184   -580       C
ATOM   5716  OG1 THR C 183      26.174  20.731   1.363  1.00 56.87           O
ANISOU 5716  OG1 THR C 183     5618   7832   8159   -259   1321   -594       O
ATOM   5717  CG2 THR C 183      23.958  20.975   2.426  1.00 54.03           C
ANISOU 5717  CG2 THR C 183     5392   7470   7666   -260   1137   -567       C
ATOM   5718  N   VAL C 184      27.545  22.567   2.903  1.00 54.42           N
ANISOU 5718  N   VAL C 184     5060   7643   7974   -391   1283   -675       N
ATOM   5719  CA  VAL C 184      27.899  23.924   2.498  1.00 53.69           C
ANISOU 5719  CA  VAL C 184     4973   7522   7906   -487   1360   -714       C
ATOM   5720  C   VAL C 184      27.202  24.326   1.200  1.00 50.07           C
ANISOU 5720  C   VAL C 184     4692   6954   7380   -505   1451   -700       C
ATOM   5721  O   VAL C 184      27.407  25.450   0.724  1.00 42.05           O
ANISOU 5721  O   VAL C 184     3708   5898   6373   -582   1527   -728       O
ATOM   5722  CB  VAL C 184      29.431  24.100   2.380  1.00 51.95           C
ANISOU 5722  CB  VAL C 184     4599   7340   7798   -517   1443   -748       C
ATOM   5723  CG1 VAL C 184      30.003  23.275   1.212  1.00 54.44           C
ANISOU 5723  CG1 VAL C 184     4935   7609   8141   -464   1561   -729       C
ATOM   5724  CG2 VAL C 184      29.840  25.567   2.329  1.00 40.51           C
ANISOU 5724  CG2 VAL C 184     3128   5883   6383   -628   1497   -794       C
ATOM   5725  N   ASN C 185      26.424  23.428   0.578  1.00 48.36           N
ANISOU 5725  N   ASN C 185     4594   6684   7096   -437   1450   -659       N
ATOM   5726  CA  ASN C 185      25.707  23.771  -0.651  1.00 51.16           C
ANISOU 5726  CA  ASN C 185     5125   6934   7379   -451   1525   -644       C
ATOM   5727  C   ASN C 185      24.252  24.224  -0.414  1.00 51.90           C
ANISOU 5727  C   ASN C 185     5344   6998   7379   -462   1440   -627       C
ATOM   5728  O   ASN C 185      23.448  24.235  -1.360  1.00 51.83           O
ANISOU 5728  O   ASN C 185     5489   6906   7298   -452   1473   -605       O
ATOM   5729  CB  ASN C 185      25.752  22.606  -1.641  1.00 52.01           C
ANISOU 5729  CB  ASN C 185     5303   6991   7467   -378   1587   -611       C
ATOM   5730  CG  ASN C 185      27.168  22.082  -1.874  1.00 55.39           C
ANISOU 5730  CG  ASN C 185     5608   7449   7991   -357   1675   -624       C
ATOM   5731  OD1 ASN C 185      28.135  22.830  -1.837  1.00 54.92           O
ANISOU 5731  OD1 ASN C 185     5450   7411   8005   -415   1738   -660       O
ATOM   5732  ND2 ASN C 185      27.288  20.782  -2.102  1.00 63.47           N
ANISOU 5732  ND2 ASN C 185     6632   8472   9013   -273   1678   -593       N
ATOM   5733  N   GLU C 186      23.899  24.614   0.814  1.00 51.34           N
ANISOU 5733  N   GLU C 186     5211   6990   7308   -482   1332   -638       N
ATOM   5734  CA  GLU C 186      22.553  25.076   1.157  1.00 51.26           C
ANISOU 5734  CA  GLU C 186     5303   6958   7217   -492   1251   -624       C
ATOM   5735  C   GLU C 186      22.653  26.390   1.923  1.00 48.18           C
ANISOU 5735  C   GLU C 186     4863   6596   6845   -572   1226   -661       C
ATOM   5736  O   GLU C 186      23.404  26.490   2.902  1.00 47.60           O
ANISOU 5736  O   GLU C 186     4650   6601   6834   -591   1186   -687       O
ATOM   5737  CB  GLU C 186      21.786  24.001   1.972  1.00 52.22           C
ANISOU 5737  CB  GLU C 186     5417   7121   7303   -421   1132   -591       C
ATOM   5738  CG  GLU C 186      20.468  24.444   2.657  1.00 49.35           C
ANISOU 5738  CG  GLU C 186     5121   6757   6872   -430   1032   -580       C
ATOM   5739  CD  GLU C 186      19.807  23.323   3.505  1.00 46.95           C
ANISOU 5739  CD  GLU C 186     4801   6499   6541   -362    922   -549       C
ATOM   5740  OE1 GLU C 186      19.198  22.407   2.910  1.00 47.75           O
ANISOU 5740  OE1 GLU C 186     4986   6560   6597   -307    920   -514       O
ATOM   5741  OE2 GLU C 186      19.884  23.358   4.763  1.00 45.15           O
ANISOU 5741  OE2 GLU C 186     4481   6341   6332   -365    838   -560       O
ATOM   5742  N   TYR C 187      21.915  27.401   1.463  1.00 43.54           N
ANISOU 5742  N   TYR C 187     4394   5944   6204   -617   1250   -665       N
ATOM   5743  CA  TYR C 187      21.850  28.718   2.102  1.00 43.01           C
ANISOU 5743  CA  TYR C 187     4310   5890   6141   -693   1232   -697       C
ATOM   5744  C   TYR C 187      20.432  28.925   2.585  1.00 35.04           C
ANISOU 5744  C   TYR C 187     3392   4867   5054   -678   1139   -675       C
ATOM   5745  O   TYR C 187      19.547  29.208   1.772  1.00 34.27           O
ANISOU 5745  O   TYR C 187     3434   4694   4892   -672   1163   -654       O
ATOM   5746  CB  TYR C 187      22.220  29.836   1.134  1.00 43.35           C
ANISOU 5746  CB  TYR C 187     4420   5863   6189   -762   1350   -722       C
ATOM   5747  CG  TYR C 187      23.668  30.185   1.152  1.00 44.35           C
ANISOU 5747  CG  TYR C 187     4422   6022   6406   -815   1427   -763       C
ATOM   5748  CD1 TYR C 187      24.506  29.755   0.149  1.00 42.10           C
ANISOU 5748  CD1 TYR C 187     4128   5706   6160   -804   1536   -763       C
ATOM   5749  CD2 TYR C 187      24.203  30.934   2.178  1.00 49.97           C
ANISOU 5749  CD2 TYR C 187     5024   6797   7166   -878   1390   -801       C
ATOM   5750  CE1 TYR C 187      25.838  30.076   0.153  1.00 52.87           C
ANISOU 5750  CE1 TYR C 187     5372   7103   7615   -854   1611   -801       C
ATOM   5751  CE2 TYR C 187      25.545  31.263   2.188  1.00 48.49           C
ANISOU 5751  CE2 TYR C 187     4715   6643   7068   -931   1458   -841       C
ATOM   5752  CZ  TYR C 187      26.352  30.833   1.179  1.00 51.42           C
ANISOU 5752  CZ  TYR C 187     5073   6984   7482   -919   1569   -840       C
ATOM   5753  OH  TYR C 187      27.691  31.156   1.194  1.00 61.97           O
ANISOU 5753  OH  TYR C 187     6279   8354   8912   -972   1640   -879       O
ATOM   5754  N   ARG C 188      20.213  28.765   3.887  1.00 37.38           N
ANISOU 5754  N   ARG C 188     3611   5235   5357   -668   1033   -677       N
ATOM   5755  CA  ARG C 188      18.866  28.883   4.436  1.00 41.18           C
ANISOU 5755  CA  ARG C 188     4168   5708   5769   -649    944   -655       C
ATOM   5756  C   ARG C 188      18.933  29.455   5.839  1.00 39.47           C
ANISOU 5756  C   ARG C 188     3868   5557   5570   -686    867   -680       C
ATOM   5757  O   ARG C 188      19.955  29.355   6.514  1.00 44.26           O
ANISOU 5757  O   ARG C 188     4347   6230   6239   -704    854   -707       O
ATOM   5758  CB  ARG C 188      18.143  27.536   4.452  1.00 39.80           C
ANISOU 5758  CB  ARG C 188     4022   5540   5558   -564    881   -611       C
ATOM   5759  CG  ARG C 188      18.287  26.809   5.731  1.00 40.13           C
ANISOU 5759  CG  ARG C 188     3958   5666   5623   -532    786   -609       C
ATOM   5760  CD  ARG C 188      17.817  25.402   5.597  1.00 39.46           C
ANISOU 5760  CD  ARG C 188     3897   5584   5513   -450    746   -569       C
ATOM   5761  NE  ARG C 188      16.379  25.325   5.389  1.00 38.60           N
ANISOU 5761  NE  ARG C 188     3908   5427   5329   -426    705   -537       N
ATOM   5762  CZ  ARG C 188      15.695  24.187   5.433  1.00 36.59           C
ANISOU 5762  CZ  ARG C 188     3687   5173   5041   -361    653   -501       C
ATOM   5763  NH1 ARG C 188      16.334  23.057   5.703  1.00 33.71           N
ANISOU 5763  NH1 ARG C 188     3249   4852   4708   -313    638   -493       N
ATOM   5764  NH2 ARG C 188      14.381  24.187   5.244  1.00 35.24           N
ANISOU 5764  NH2 ARG C 188     3620   4962   4808   -346    615   -474       N
ATOM   5765  N   ALA C 189      17.836  30.078   6.267  1.00 40.13           N
ANISOU 5765  N   ALA C 189     4028   5621   5599   -697    815   -672       N
ATOM   5766  CA  ALA C 189      17.692  30.561   7.635  1.00 38.14           C
ANISOU 5766  CA  ALA C 189     3719   5425   5349   -724    735   -691       C
ATOM   5767  C   ALA C 189      16.625  29.762   8.389  1.00 38.60           C
ANISOU 5767  C   ALA C 189     3798   5507   5362   -661    633   -657       C
ATOM   5768  O   ALA C 189      15.681  29.250   7.787  1.00 33.68           O
ANISOU 5768  O   ALA C 189     3266   4840   4692   -613    628   -620       O
ATOM   5769  CB  ALA C 189      17.353  32.053   7.653  1.00 33.57           C
ANISOU 5769  CB  ALA C 189     3205   4803   4746   -794    764   -715       C
ATOM   5770  N   ILE C 190      16.779  29.685   9.719  1.00 34.08           N
ANISOU 5770  N   ILE C 190     3143   5002   4804   -665    553   -670       N
ATOM   5771  CA  ILE C 190      15.814  29.094  10.642  1.00 32.20           C
ANISOU 5771  CA  ILE C 190     2920   4790   4525   -617    457   -644       C
ATOM   5772  C   ILE C 190      15.441  30.134  11.699  1.00 34.27           C
ANISOU 5772  C   ILE C 190     3186   5067   4768   -666    412   -666       C
ATOM   5773  O   ILE C 190      16.318  30.825  12.235  1.00 41.05           O
ANISOU 5773  O   ILE C 190     3973   5959   5664   -724    417   -706       O
ATOM   5774  CB  ILE C 190      16.399  27.832  11.314  1.00 33.05           C
ANISOU 5774  CB  ILE C 190     2927   4967   4662   -565    399   -635       C
ATOM   5775  CG1 ILE C 190      17.709  28.193  12.003  1.00 34.85           C
ANISOU 5775  CG1 ILE C 190     3030   5258   4954   -611    393   -677       C
ATOM   5776  CG2 ILE C 190      16.575  26.668  10.365  1.00 39.09           C
ANISOU 5776  CG2 ILE C 190     3702   5715   5436   -505    434   -607       C
ATOM   5777  CD1 ILE C 190      18.254  27.124  12.852  1.00 36.54           C
ANISOU 5777  CD1 ILE C 190     3144   5544   5194   -563    323   -672       C
ATOM   5778  N   THR C 191      14.154  30.207  12.049  1.00 33.25           N
ANISOU 5778  N   THR C 191     3136   4914   4583   -642    366   -642       N
ATOM   5779  CA  THR C 191      13.621  31.292  12.867  1.00 31.99           C
ANISOU 5779  CA  THR C 191     3008   4749   4397   -686    340   -659       C
ATOM   5780  C   THR C 191      12.954  30.714  14.098  1.00 28.02           C
ANISOU 5780  C   THR C 191     2490   4289   3868   -647    246   -643       C
ATOM   5781  O   THR C 191      12.021  29.925  13.975  1.00 33.64           O
ANISOU 5781  O   THR C 191     3248   4986   4548   -589    216   -605       O
ATOM   5782  CB  THR C 191      12.558  32.065  12.096  1.00 31.74           C
ANISOU 5782  CB  THR C 191     3100   4640   4319   -692    381   -643       C
ATOM   5783  OG1 THR C 191      13.027  32.363  10.769  1.00 33.07           O
ANISOU 5783  OG1 THR C 191     3303   4759   4502   -712    470   -648       O
ATOM   5784  CG2 THR C 191      12.269  33.349  12.805  1.00 29.46           C
ANISOU 5784  CG2 THR C 191     2840   4341   4012   -747    375   -668       C
ATOM   5785  N   PHE C 192      13.331  31.181  15.266  1.00 28.90           N
ANISOU 5785  N   PHE C 192     2549   4444   3988   -684    202   -671       N
ATOM   5786  CA  PHE C 192      12.603  30.802  16.473  1.00 31.99           C
ANISOU 5786  CA  PHE C 192     2944   4866   4346   -653    119   -657       C
ATOM   5787  C   PHE C 192      11.145  31.210  16.345  1.00 32.84           C
ANISOU 5787  C   PHE C 192     3160   4917   4400   -637    121   -631       C
ATOM   5788  O   PHE C 192      10.857  32.355  15.971  1.00 28.78           O
ANISOU 5788  O   PHE C 192     2706   4355   3872   -679    168   -644       O
ATOM   5789  CB  PHE C 192      13.221  31.498  17.690  1.00 33.20           C
ANISOU 5789  CB  PHE C 192     3042   5064   4510   -707     79   -697       C
ATOM   5790  CG  PHE C 192      12.421  31.336  18.961  1.00 37.35           C
ANISOU 5790  CG  PHE C 192     3590   5608   4993   -685      3   -686       C
ATOM   5791  CD1 PHE C 192      11.928  30.076  19.340  1.00 36.15           C
ANISOU 5791  CD1 PHE C 192     3432   5480   4825   -613    -52   -652       C
ATOM   5792  CD2 PHE C 192      12.186  32.423  19.790  1.00 34.91           C
ANISOU 5792  CD2 PHE C 192     3312   5293   4661   -736    -10   -711       C
ATOM   5793  CE1 PHE C 192      11.224  29.918  20.519  1.00 37.69           C
ANISOU 5793  CE1 PHE C 192     3650   5690   4981   -594   -116   -643       C
ATOM   5794  CE2 PHE C 192      11.452  32.284  20.979  1.00 35.34           C
ANISOU 5794  CE2 PHE C 192     3392   5361   4675   -716    -75   -702       C
ATOM   5795  CZ  PHE C 192      10.965  31.041  21.343  1.00 36.88           C
ANISOU 5795  CZ  PHE C 192     3580   5579   4854   -645   -126   -667       C
ATOM   5796  N   VAL C 193      10.230  30.272  16.657  1.00 35.52           N
ANISOU 5796  N   VAL C 193     3524   5260   4710   -574     72   -594       N
ATOM   5797  CA  VAL C 193       8.788  30.477  16.428  1.00 31.03           C
ANISOU 5797  CA  VAL C 193     3051   4641   4099   -549     72   -564       C
ATOM   5798  C   VAL C 193       8.235  31.580  17.311  1.00 33.77           C
ANISOU 5798  C   VAL C 193     3435   4976   4419   -585     60   -580       C
ATOM   5799  O   VAL C 193       7.210  32.184  16.979  1.00 32.22           O
ANISOU 5799  O   VAL C 193     3319   4730   4195   -582     81   -564       O
ATOM   5800  CB  VAL C 193       7.977  29.170  16.591  1.00 27.90           C
ANISOU 5800  CB  VAL C 193     2664   4254   3682   -479     24   -523       C
ATOM   5801  CG1 VAL C 193       7.870  28.739  18.050  1.00 26.25           C
ANISOU 5801  CG1 VAL C 193     2418   4095   3462   -464    -48   -525       C
ATOM   5802  CG2 VAL C 193       6.593  29.335  15.957  1.00 26.20           C
ANISOU 5802  CG2 VAL C 193     2541   3982   3433   -454     38   -491       C
ATOM   5803  N   GLY C 194       8.886  31.850  18.445  1.00 37.90           N
ANISOU 5803  N   GLY C 194     3904   5546   4951   -618     24   -610       N
ATOM   5804  CA  GLY C 194       8.501  32.993  19.263  1.00 40.29           C
ANISOU 5804  CA  GLY C 194     4247   5834   5228   -661     19   -630       C
ATOM   5805  C   GLY C 194       8.571  34.315  18.507  1.00 39.05           C
ANISOU 5805  C   GLY C 194     4142   5623   5071   -714     91   -650       C
ATOM   5806  O   GLY C 194       7.678  35.155  18.629  1.00 41.39           O
ANISOU 5806  O   GLY C 194     4513   5876   5335   -723    107   -645       O
ATOM   5807  N   GLU C 195       9.613  34.509  17.689  1.00 32.52           N
ANISOU 5807  N   GLU C 195     3279   4796   4281   -749    140   -672       N
ATOM   5808  CA  GLU C 195       9.673  35.756  16.919  1.00 35.48           C
ANISOU 5808  CA  GLU C 195     3712   5114   4653   -800    214   -690       C
ATOM   5809  C   GLU C 195       8.576  35.818  15.860  1.00 34.43           C
ANISOU 5809  C   GLU C 195     3673   4916   4492   -760    250   -653       C
ATOM   5810  O   GLU C 195       7.980  36.879  15.633  1.00 32.06           O
ANISOU 5810  O   GLU C 195     3452   4562   4166   -781    287   -655       O
ATOM   5811  CB  GLU C 195      11.054  35.944  16.288  1.00 35.33           C
ANISOU 5811  CB  GLU C 195     3634   5108   4682   -850    263   -722       C
ATOM   5812  CG  GLU C 195      12.092  36.437  17.322  1.00 39.74           C
ANISOU 5812  CG  GLU C 195     4117   5718   5266   -914    238   -769       C
ATOM   5813  CD  GLU C 195      13.424  36.868  16.706  1.00 35.50           C
ANISOU 5813  CD  GLU C 195     3522   5187   4780   -976    297   -806       C
ATOM   5814  OE1 GLU C 195      13.419  37.357  15.553  1.00 32.06           O
ANISOU 5814  OE1 GLU C 195     3140   4696   4347   -992    375   -805       O
ATOM   5815  OE2 GLU C 195      14.472  36.674  17.377  1.00 33.93           O
ANISOU 5815  OE2 GLU C 195     3223   5050   4618  -1007    263   -836       O
ATOM   5816  N   VAL C 196       8.265  34.681  15.235  1.00 35.23           N
ANISOU 5816  N   VAL C 196     3770   5021   4596   -701    237   -618       N
ATOM   5817  CA  VAL C 196       7.193  34.633  14.240  1.00 33.33           C
ANISOU 5817  CA  VAL C 196     3616   4722   4328   -660    260   -582       C
ATOM   5818  C   VAL C 196       5.857  35.005  14.871  1.00 32.73           C
ANISOU 5818  C   VAL C 196     3597   4624   4214   -636    228   -561       C
ATOM   5819  O   VAL C 196       5.044  35.718  14.268  1.00 30.72           O
ANISOU 5819  O   VAL C 196     3426   4312   3935   -631    259   -547       O
ATOM   5820  CB  VAL C 196       7.158  33.240  13.580  1.00 33.01           C
ANISOU 5820  CB  VAL C 196     3552   4693   4296   -603    243   -550       C
ATOM   5821  CG1 VAL C 196       5.984  33.103  12.594  1.00 30.42           C
ANISOU 5821  CG1 VAL C 196     3313   4307   3937   -560    255   -511       C
ATOM   5822  CG2 VAL C 196       8.495  32.964  12.890  1.00 29.02           C
ANISOU 5822  CG2 VAL C 196     2994   4202   3831   -626    288   -571       C
ATOM   5823  N   VAL C 197       5.594  34.526  16.086  1.00 32.05           N
ANISOU 5823  N   VAL C 197     3474   4583   4123   -619    166   -558       N
ATOM   5824  CA  VAL C 197       4.264  34.758  16.632  1.00 36.80           C
ANISOU 5824  CA  VAL C 197     4129   5162   4690   -590    141   -535       C
ATOM   5825  C   VAL C 197       4.132  36.181  17.162  1.00 38.25           C
ANISOU 5825  C   VAL C 197     4357   5318   4857   -637    167   -560       C
ATOM   5826  O   VAL C 197       3.086  36.815  16.959  1.00 39.89           O
ANISOU 5826  O   VAL C 197     4637   5477   5040   -621    185   -542       O
ATOM   5827  CB  VAL C 197       3.899  33.686  17.681  1.00 43.69           C
ANISOU 5827  CB  VAL C 197     4958   6084   5558   -549     72   -518       C
ATOM   5828  CG1 VAL C 197       4.919  33.622  18.817  1.00 39.06           C
ANISOU 5828  CG1 VAL C 197     4302   5554   4985   -583     40   -552       C
ATOM   5829  CG2 VAL C 197       2.460  33.885  18.180  1.00 39.78           C
ANISOU 5829  CG2 VAL C 197     4519   5563   5033   -517     53   -492       C
ATOM   5830  N   GLU C 198       5.196  36.736  17.783  1.00 38.97           N
ANISOU 5830  N   GLU C 198     4408   5437   4962   -696    174   -603       N
ATOM   5831  CA  GLU C 198       5.104  38.085  18.351  1.00 39.19           C
ANISOU 5831  CA  GLU C 198     4483   5437   4971   -746    199   -629       C
ATOM   5832  C   GLU C 198       5.042  39.173  17.286  1.00 35.64           C
ANISOU 5832  C   GLU C 198     4106   4921   4515   -773    272   -635       C
ATOM   5833  O   GLU C 198       4.559  40.271  17.575  1.00 38.65           O
ANISOU 5833  O   GLU C 198     4553   5263   4871   -795    298   -644       O
ATOM   5834  CB  GLU C 198       6.291  38.430  19.249  1.00 37.58           C
ANISOU 5834  CB  GLU C 198     4220   5277   4782   -809    184   -676       C
ATOM   5835  CG  GLU C 198       6.693  37.450  20.337  1.00 41.52           C
ANISOU 5835  CG  GLU C 198     4640   5845   5289   -794    111   -680       C
ATOM   5836  CD  GLU C 198       5.563  36.968  21.210  1.00 50.80           C
ANISOU 5836  CD  GLU C 198     5843   7026   6434   -742     63   -651       C
ATOM   5837  OE1 GLU C 198       4.494  37.639  21.303  1.00 50.26           O
ANISOU 5837  OE1 GLU C 198     5851   6910   6335   -730     84   -636       O
ATOM   5838  OE2 GLU C 198       5.770  35.894  21.829  1.00 55.04           O
ANISOU 5838  OE2 GLU C 198     6323   7614   6977   -712      6   -642       O
ATOM   5839  N   ASN C 199       5.519  38.913  16.077  1.00 33.45           N
ANISOU 5839  N   ASN C 199     3824   4628   4256   -772    310   -630       N
ATOM   5840  CA  ASN C 199       5.382  39.895  15.016  1.00 34.72           C
ANISOU 5840  CA  ASN C 199     4066   4721   4406   -792    380   -632       C
ATOM   5841  C   ASN C 199       4.110  39.737  14.211  1.00 35.58           C
ANISOU 5841  C   ASN C 199     4249   4781   4489   -729    382   -586       C
ATOM   5842  O   ASN C 199       3.906  40.526  13.286  1.00 34.61           O
ANISOU 5842  O   ASN C 199     4202   4598   4351   -737    436   -583       O
ATOM   5843  CB  ASN C 199       6.577  39.849  14.055  1.00 34.46           C
ANISOU 5843  CB  ASN C 199     4004   4686   4403   -830    431   -653       C
ATOM   5844  CG  ASN C 199       7.776  40.621  14.594  1.00 37.40           C
ANISOU 5844  CG  ASN C 199     4333   5079   4798   -912    457   -705       C
ATOM   5845  OD1 ASN C 199       7.613  41.681  15.210  1.00 40.22           O
ANISOU 5845  OD1 ASN C 199     4731   5414   5135   -952    470   -727       O
ATOM   5846  ND2 ASN C 199       8.983  40.087  14.380  1.00 33.18           N
ANISOU 5846  ND2 ASN C 199     3715   4585   4306   -938    465   -727       N
ATOM   5847  N   ILE C 200       3.271  38.732  14.504  1.00 34.88           N
ANISOU 5847  N   ILE C 200     4141   4717   4396   -668    324   -551       N
ATOM   5848  CA  ILE C 200       2.138  38.442  13.622  1.00 34.22           C
ANISOU 5848  CA  ILE C 200     4116   4592   4293   -609    320   -508       C
ATOM   5849  C   ILE C 200       1.120  39.585  13.635  1.00 36.08           C
ANISOU 5849  C   ILE C 200     4437   4771   4499   -602    342   -497       C
ATOM   5850  O   ILE C 200       0.477  39.868  12.612  1.00 35.73           O
ANISOU 5850  O   ILE C 200     4462   4674   4439   -574    365   -473       O
ATOM   5851  CB  ILE C 200       1.472  37.091  13.980  1.00 32.44           C
ANISOU 5851  CB  ILE C 200     3847   4406   4071   -551    254   -475       C
ATOM   5852  CG1 ILE C 200       0.834  36.485  12.731  1.00 32.79           C
ANISOU 5852  CG1 ILE C 200     3931   4418   4109   -504    253   -437       C
ATOM   5853  CG2 ILE C 200       0.380  37.217  15.050  1.00 36.91           C
ANISOU 5853  CG2 ILE C 200     4423   4979   4621   -524    216   -459       C
ATOM   5854  CD1 ILE C 200       1.893  35.851  11.780  1.00 33.14           C
ANISOU 5854  CD1 ILE C 200     3951   4470   4172   -516    279   -446       C
ATOM   5855  N   GLU C 201       0.937  40.248  14.771  1.00 32.80           N
ANISOU 5855  N   GLU C 201     4024   4364   4075   -622    336   -514       N
ATOM   5856  CA  GLU C 201      -0.061  41.307  14.799  1.00 41.60           C
ANISOU 5856  CA  GLU C 201     5221   5423   5162   -608    360   -502       C
ATOM   5857  C   GLU C 201       0.333  42.458  13.888  1.00 37.90           C
ANISOU 5857  C   GLU C 201     4825   4893   4681   -645    430   -518       C
ATOM   5858  O   GLU C 201      -0.541  43.096  13.284  1.00 35.87           O
ANISOU 5858  O   GLU C 201     4647   4578   4402   -615    452   -495       O
ATOM   5859  CB  GLU C 201      -0.278  41.775  16.235  1.00 39.71           C
ANISOU 5859  CB  GLU C 201     4973   5202   4913   -625    344   -518       C
ATOM   5860  CG  GLU C 201      -1.191  40.829  16.989  1.00 43.18           C
ANISOU 5860  CG  GLU C 201     5376   5676   5354   -570    284   -488       C
ATOM   5861  CD  GLU C 201      -0.865  40.742  18.463  1.00 54.79           C
ANISOU 5861  CD  GLU C 201     6805   7191   6823   -596    255   -512       C
ATOM   5862  OE1 GLU C 201      -0.463  41.770  19.075  1.00 57.62           O
ANISOU 5862  OE1 GLU C 201     7191   7536   7168   -645    283   -545       O
ATOM   5863  OE2 GLU C 201      -0.993  39.622  19.008  1.00 55.98           O
ANISOU 5863  OE2 GLU C 201     6898   7389   6982   -567    203   -499       O
ATOM   5864  N   LYS C 202       1.635  42.688  13.715  1.00 34.51           N
ANISOU 5864  N   LYS C 202     4370   4475   4268   -707    465   -557       N
ATOM   5865  CA  LYS C 202       2.066  43.780  12.848  1.00 35.37           C
ANISOU 5865  CA  LYS C 202     4552   4524   4365   -748    539   -575       C
ATOM   5866  C   LYS C 202       1.707  43.527  11.384  1.00 37.59           C
ANISOU 5866  C   LYS C 202     4886   4759   4636   -708    560   -544       C
ATOM   5867  O   LYS C 202       1.516  44.488  10.628  1.00 40.30           O
ANISOU 5867  O   LYS C 202     5320   5036   4957   -716    613   -542       O
ATOM   5868  CB  LYS C 202       3.563  43.990  12.991  1.00 33.08           C
ANISOU 5868  CB  LYS C 202     4210   4259   4100   -826    572   -623       C
ATOM   5869  CG  LYS C 202       4.010  44.513  14.351  1.00 34.18           C
ANISOU 5869  CG  LYS C 202     4314   4431   4242   -879    559   -660       C
ATOM   5870  CD  LYS C 202       5.435  45.046  14.232  1.00 34.50           C
ANISOU 5870  CD  LYS C 202     4326   4477   4305   -964    607   -710       C
ATOM   5871  CE  LYS C 202       5.969  45.374  15.578  1.00 37.59           C
ANISOU 5871  CE  LYS C 202     4670   4910   4701  -1018    581   -747       C
ATOM   5872  NZ  LYS C 202       5.533  44.251  16.457  1.00 43.03           N
ANISOU 5872  NZ  LYS C 202     5292   5661   5396   -966    498   -726       N
ATOM   5873  N   THR C 203       1.565  42.258  10.975  1.00 35.24           N
ANISOU 5873  N   THR C 203     4543   4493   4353   -664    517   -517       N
ATOM   5874  CA  THR C 203       1.235  41.940   9.584  1.00 38.23           C
ANISOU 5874  CA  THR C 203     4976   4829   4719   -628    532   -488       C
ATOM   5875  C   THR C 203      -0.202  42.279   9.229  1.00 36.32           C
ANISOU 5875  C   THR C 203     4813   4540   4447   -569    513   -448       C
ATOM   5876  O   THR C 203      -0.551  42.320   8.041  1.00 27.36           O
ANISOU 5876  O   THR C 203     3746   3356   3293   -542    529   -426       O
ATOM   5877  CB  THR C 203       1.457  40.445   9.287  1.00 36.58           C
ANISOU 5877  CB  THR C 203     4701   4666   4532   -598    489   -471       C
ATOM   5878  OG1 THR C 203       0.778  39.634  10.265  1.00 38.79           O
ANISOU 5878  OG1 THR C 203     4922   4998   4820   -559    418   -453       O
ATOM   5879  CG2 THR C 203       2.900  40.116   9.294  1.00 34.88           C
ANISOU 5879  CG2 THR C 203     4419   4487   4348   -648    517   -506       C
ATOM   5880  N   PHE C 204      -1.053  42.463  10.232  1.00 35.87           N
ANISOU 5880  N   PHE C 204     4744   4498   4386   -545    477   -438       N
ATOM   5881  CA  PHE C 204      -2.459  42.723   9.956  1.00 37.81           C
ANISOU 5881  CA  PHE C 204     5050   4705   4611   -485    455   -398       C
ATOM   5882  C   PHE C 204      -2.637  44.044   9.213  1.00 37.91           C
ANISOU 5882  C   PHE C 204     5170   4640   4593   -492    514   -399       C
ATOM   5883  O   PHE C 204      -3.541  44.163   8.381  1.00 38.52           O
ANISOU 5883  O   PHE C 204     5311   4673   4652   -441    504   -365       O
ATOM   5884  CB  PHE C 204      -3.277  42.721  11.261  1.00 38.76           C
ANISOU 5884  CB  PHE C 204     5134   4855   4736   -462    415   -390       C
ATOM   5885  CG  PHE C 204      -3.295  41.383  12.009  1.00 37.73           C
ANISOU 5885  CG  PHE C 204     4908   4796   4630   -445    353   -383       C
ATOM   5886  CD1 PHE C 204      -3.137  40.187  11.345  1.00 37.36           C
ANISOU 5886  CD1 PHE C 204     4826   4774   4596   -424    322   -366       C
ATOM   5887  CD2 PHE C 204      -3.524  41.339  13.382  1.00 42.31           C
ANISOU 5887  CD2 PHE C 204     5444   5413   5217   -448    329   -391       C
ATOM   5888  CE1 PHE C 204      -3.169  38.966  12.021  1.00 35.43           C
ANISOU 5888  CE1 PHE C 204     4501   4589   4370   -408    268   -358       C
ATOM   5889  CE2 PHE C 204      -3.573  40.109  14.078  1.00 41.60           C
ANISOU 5889  CE2 PHE C 204     5275   5385   5146   -431    274   -383       C
ATOM   5890  CZ  PHE C 204      -3.394  38.926  13.387  1.00 36.49           C
ANISOU 5890  CZ  PHE C 204     4592   4761   4511   -410    244   -366       C
ATOM   5891  N   GLU C 205      -1.766  45.029   9.471  1.00 37.91           N
ANISOU 5891  N   GLU C 205     5194   4620   4588   -555    574   -439       N
ATOM   5892  CA  GLU C 205      -1.831  46.365   8.874  1.00 40.79           C
ANISOU 5892  CA  GLU C 205     5667   4909   4924   -569    639   -445       C
ATOM   5893  C   GLU C 205      -1.065  46.519   7.558  1.00 37.88           C
ANISOU 5893  C   GLU C 205     5352   4496   4544   -595    693   -454       C
ATOM   5894  O   GLU C 205      -1.080  47.615   6.974  1.00 37.96           O
ANISOU 5894  O   GLU C 205     5462   4437   4525   -608    751   -459       O
ATOM   5895  CB  GLU C 205      -1.297  47.402   9.872  1.00 39.65           C
ANISOU 5895  CB  GLU C 205     5528   4760   4776   -630    680   -486       C
ATOM   5896  CG  GLU C 205      -1.578  47.080  11.326  1.00 39.57           C
ANISOU 5896  CG  GLU C 205     5446   4809   4782   -627    633   -492       C
ATOM   5897  CD  GLU C 205      -3.066  47.171  11.658  1.00 40.76           C
ANISOU 5897  CD  GLU C 205     5624   4943   4919   -555    597   -451       C
ATOM   5898  OE1 GLU C 205      -3.479  46.628  12.712  1.00 40.66           O
ANISOU 5898  OE1 GLU C 205     5549   4979   4921   -537    551   -446       O
ATOM   5899  OE2 GLU C 205      -3.823  47.767  10.853  1.00 39.55           O
ANISOU 5899  OE2 GLU C 205     5554   4729   4744   -514    617   -425       O
ATOM   5900  N   LEU C 206      -0.374  45.481   7.102  1.00 36.59           N
ANISOU 5900  N   LEU C 206     5133   4369   4402   -604    681   -457       N
ATOM   5901  CA  LEU C 206       0.501  45.623   5.952  1.00 33.89           C
ANISOU 5901  CA  LEU C 206     4837   3988   4054   -637    742   -471       C
ATOM   5902  C   LEU C 206      -0.327  45.742   4.682  1.00 36.85           C
ANISOU 5902  C   LEU C 206     5315   4296   4391   -582    744   -432       C
ATOM   5903  O   LEU C 206      -1.355  45.067   4.553  1.00 36.41           O
ANISOU 5903  O   LEU C 206     5254   4251   4330   -517    678   -393       O
ATOM   5904  CB  LEU C 206       1.414  44.424   5.826  1.00 35.48           C
ANISOU 5904  CB  LEU C 206     4948   4245   4289   -654    729   -482       C
ATOM   5905  CG  LEU C 206       2.564  44.313   6.814  1.00 38.32           C
ANISOU 5905  CG  LEU C 206     5207   4665   4687   -718    739   -526       C
ATOM   5906  CD1 LEU C 206       3.200  42.922   6.670  1.00 37.12           C
ANISOU 5906  CD1 LEU C 206     4965   4572   4569   -710    709   -524       C
ATOM   5907  CD2 LEU C 206       3.584  45.437   6.578  1.00 38.28           C
ANISOU 5907  CD2 LEU C 206     5241   4620   4681   -795    827   -568       C
ATOM   5908  N   PRO C 207       0.088  46.577   3.726  1.00 38.21           N
ANISOU 5908  N   PRO C 207     5586   4398   4537   -608    817   -443       N
ATOM   5909  CA  PRO C 207      -0.618  46.614   2.439  1.00 37.76           C
ANISOU 5909  CA  PRO C 207     5632   4275   4439   -556    815   -406       C
ATOM   5910  C   PRO C 207      -0.456  45.270   1.739  1.00 38.09           C
ANISOU 5910  C   PRO C 207     5637   4344   4491   -532    780   -388       C
ATOM   5911  O   PRO C 207       0.493  44.531   1.993  1.00 38.55           O
ANISOU 5911  O   PRO C 207     5610   4453   4584   -568    788   -411       O
ATOM   5912  CB  PRO C 207       0.063  47.761   1.677  1.00 34.22           C
ANISOU 5912  CB  PRO C 207     5290   3750   3964   -602    912   -429       C
ATOM   5913  CG  PRO C 207       0.820  48.545   2.719  1.00 35.79           C
ANISOU 5913  CG  PRO C 207     5448   3968   4184   -673    958   -475       C
ATOM   5914  CD  PRO C 207       1.215  47.522   3.758  1.00 38.27           C
ANISOU 5914  CD  PRO C 207     5616   4378   4546   -687    904   -488       C
ATOM   5915  N   GLY C 208      -1.428  44.930   0.904  1.00 40.41           N
ANISOU 5915  N   GLY C 208     5993   4606   4756   -468    736   -346       N
ATOM   5916  CA  GLY C 208      -1.427  43.676   0.170  1.00 42.53           C
ANISOU 5916  CA  GLY C 208     6243   4890   5025   -441    699   -325       C
ATOM   5917  C   GLY C 208      -0.158  43.382  -0.610  1.00 43.00           C
ANISOU 5917  C   GLY C 208     6315   4935   5088   -487    767   -349       C
ATOM   5918  O   GLY C 208       0.511  44.312  -1.077  1.00 43.56           O
ANISOU 5918  O   GLY C 208     6456   4952   5144   -529    850   -373       O
ATOM   5919  N   GLY C 209       0.239  42.110  -0.668  1.00 39.59           N
ANISOU 5919  N   GLY C 209     5810   4551   4681   -482    740   -347       N
ATOM   5920  CA  GLY C 209       1.436  41.723  -1.385  1.00 39.94           C
ANISOU 5920  CA  GLY C 209     5857   4585   4734   -520    805   -368       C
ATOM   5921  C   GLY C 209       2.129  40.557  -0.701  1.00 38.99           C
ANISOU 5921  C   GLY C 209     5605   4546   4663   -533    781   -382       C
ATOM   5922  O   GLY C 209       1.628  39.996   0.269  1.00 35.63           O
ANISOU 5922  O   GLY C 209     5095   4182   4259   -510    709   -373       O
ATOM   5923  N   VAL C 210       3.328  40.255  -1.208  1.00 36.94           N
ANISOU 5923  N   VAL C 210     5330   4284   4421   -571    847   -406       N
ATOM   5924  CA  VAL C 210       4.180  39.163  -0.748  1.00 35.61           C
ANISOU 5924  CA  VAL C 210     5044   4185   4300   -583    839   -420       C
ATOM   5925  C   VAL C 210       5.311  39.736   0.099  1.00 37.88           C
ANISOU 5925  C   VAL C 210     5249   4510   4633   -650    889   -467       C
ATOM   5926  O   VAL C 210       5.932  40.739  -0.284  1.00 37.47           O
ANISOU 5926  O   VAL C 210     5248   4412   4577   -699    971   -493       O
ATOM   5927  CB  VAL C 210       4.748  38.389  -1.941  1.00 34.80           C
ANISOU 5927  CB  VAL C 210     4981   4051   4189   -576    881   -413       C
ATOM   5928  CG1 VAL C 210       5.792  37.439  -1.477  1.00 35.25           C
ANISOU 5928  CG1 VAL C 210     4919   4175   4299   -593    889   -433       C
ATOM   5929  CG2 VAL C 210       3.657  37.663  -2.644  1.00 32.78           C
ANISOU 5929  CG2 VAL C 210     4794   3770   3891   -512    817   -369       C
ATOM   5930  N   TYR C 211       5.573  39.117   1.259  1.00 36.28           N
ANISOU 5930  N   TYR C 211     4921   4390   4473   -654    839   -478       N
ATOM   5931  CA  TYR C 211       6.580  39.623   2.196  1.00 34.89           C
ANISOU 5931  CA  TYR C 211     4657   4257   4340   -716    870   -522       C
ATOM   5932  C   TYR C 211       7.434  38.488   2.768  1.00 34.70           C
ANISOU 5932  C   TYR C 211     4504   4312   4367   -719    845   -535       C
ATOM   5933  O   TYR C 211       6.910  37.586   3.434  1.00 34.88           O
ANISOU 5933  O   TYR C 211     4469   4388   4397   -676    766   -514       O
ATOM   5934  CB  TYR C 211       5.899  40.383   3.340  1.00 33.20           C
ANISOU 5934  CB  TYR C 211     4432   4063   4120   -722    825   -527       C
ATOM   5935  CG  TYR C 211       5.010  41.589   3.000  1.00 35.70           C
ANISOU 5935  CG  TYR C 211     4867   4307   4389   -716    844   -515       C
ATOM   5936  CD1 TYR C 211       3.691  41.438   2.564  1.00 34.84           C
ANISOU 5936  CD1 TYR C 211     4832   4165   4240   -651    795   -472       C
ATOM   5937  CD2 TYR C 211       5.474  42.890   3.211  1.00 38.42           C
ANISOU 5937  CD2 TYR C 211     5246   4620   4732   -776    907   -549       C
ATOM   5938  CE1 TYR C 211       2.879  42.574   2.318  1.00 37.24           C
ANISOU 5938  CE1 TYR C 211     5240   4405   4504   -641    810   -460       C
ATOM   5939  CE2 TYR C 211       4.682  44.016   2.977  1.00 33.38           C
ANISOU 5939  CE2 TYR C 211     4717   3916   4051   -768    926   -538       C
ATOM   5940  CZ  TYR C 211       3.403  43.866   2.536  1.00 37.47           C
ANISOU 5940  CZ  TYR C 211     5305   4402   4530   -698    878   -494       C
ATOM   5941  OH  TYR C 211       2.674  45.018   2.315  1.00 37.91           O
ANISOU 5941  OH  TYR C 211     5466   4392   4546   -688    898   -484       O
ATOM   5942  N   ASN C 212       8.750  38.548   2.582  1.00 28.45           N
ANISOU 5942  N   ASN C 212     3663   3532   3616   -769    913   -568       N
ATOM   5943  CA  ASN C 212       9.618  37.640   3.325  1.00 33.95           C
ANISOU 5943  CA  ASN C 212     4224   4309   4365   -775    887   -585       C
ATOM   5944  C   ASN C 212       9.426  37.832   4.821  1.00 34.77           C
ANISOU 5944  C   ASN C 212     4249   4476   4485   -787    818   -598       C
ATOM   5945  O   ASN C 212       9.625  38.939   5.331  1.00 38.65           O
ANISOU 5945  O   ASN C 212     4746   4961   4979   -839    842   -627       O
ATOM   5946  CB  ASN C 212      11.084  37.897   2.980  1.00 39.25           C
ANISOU 5946  CB  ASN C 212     4848   4983   5083   -835    974   -624       C
ATOM   5947  CG  ASN C 212      11.462  37.434   1.580  1.00 38.99           C
ANISOU 5947  CG  ASN C 212     4873   4899   5044   -820   1044   -611       C
ATOM   5948  OD1 ASN C 212      11.069  36.352   1.117  1.00 30.01           O
ANISOU 5948  OD1 ASN C 212     3749   3761   3891   -761   1012   -579       O
ATOM   5949  ND2 ASN C 212      12.214  38.289   0.883  1.00 38.62           N
ANISOU 5949  ND2 ASN C 212     4868   4801   5004   -875   1144   -638       N
ATOM   5950  N   TYR C 213       9.148  36.739   5.539  1.00 28.09           N
ANISOU 5950  N   TYR C 213     3330   3692   3651   -742    740   -580       N
ATOM   5951  CA  TYR C 213       8.765  36.780   6.955  1.00 30.70           C
ANISOU 5951  CA  TYR C 213     3601   4078   3986   -741    666   -586       C
ATOM   5952  C   TYR C 213       9.542  35.734   7.758  1.00 31.67           C
ANISOU 5952  C   TYR C 213     3598   4283   4153   -734    622   -596       C
ATOM   5953  O   TYR C 213       9.139  34.559   7.827  1.00 32.97           O
ANISOU 5953  O   TYR C 213     3740   4475   4314   -677    569   -567       O
ATOM   5954  CB  TYR C 213       7.261  36.559   7.102  1.00 30.82           C
ANISOU 5954  CB  TYR C 213     3675   4076   3957   -683    602   -545       C
ATOM   5955  CG  TYR C 213       6.662  36.940   8.430  1.00 28.55           C
ANISOU 5955  CG  TYR C 213     3363   3822   3664   -685    545   -549       C
ATOM   5956  CD1 TYR C 213       6.407  38.283   8.762  1.00 33.40           C
ANISOU 5956  CD1 TYR C 213     4027   4403   4259   -723    570   -567       C
ATOM   5957  CD2 TYR C 213       6.304  35.969   9.349  1.00 28.80           C
ANISOU 5957  CD2 TYR C 213     3329   3912   3702   -647    469   -534       C
ATOM   5958  CE1 TYR C 213       5.816  38.635  10.011  1.00 31.79           C
ANISOU 5958  CE1 TYR C 213     3807   4226   4047   -723    520   -570       C
ATOM   5959  CE2 TYR C 213       5.720  36.301  10.581  1.00 27.36           C
ANISOU 5959  CE2 TYR C 213     3130   3756   3510   -647    419   -537       C
ATOM   5960  CZ  TYR C 213       5.470  37.623  10.900  1.00 29.68           C
ANISOU 5960  CZ  TYR C 213     3473   4016   3786   -685    446   -554       C
ATOM   5961  OH  TYR C 213       4.903  37.924  12.113  1.00 28.04           O
ANISOU 5961  OH  TYR C 213     3254   3831   3567   -683    402   -557       O
ATOM   5962  N   GLY C 214      10.638  36.161   8.377  1.00 28.07           N
ANISOU 5962  N   GLY C 214     3063   3866   3737   -791    641   -637       N
ATOM   5963  CA  GLY C 214      11.447  35.263   9.178  1.00 30.33           C
ANISOU 5963  CA  GLY C 214     3226   4231   4066   -785    597   -649       C
ATOM   5964  C   GLY C 214      12.860  35.792   9.377  1.00 30.37           C
ANISOU 5964  C   GLY C 214     3152   4264   4123   -855    643   -697       C
ATOM   5965  O   GLY C 214      13.178  36.930   9.036  1.00 32.05           O
ANISOU 5965  O   GLY C 214     3404   4436   4336   -915    707   -723       O
ATOM   5966  N   ALA C 215      13.695  34.933   9.954  1.00 29.27           N
ANISOU 5966  N   ALA C 215     2898   4196   4029   -846    607   -707       N
ATOM   5967  CA  ALA C 215      15.068  35.287  10.260  1.00 32.95           C
ANISOU 5967  CA  ALA C 215     3266   4702   4552   -908    637   -751       C
ATOM   5968  C   ALA C 215      15.888  35.475   8.980  1.00 36.72           C
ANISOU 5968  C   ALA C 215     3754   5138   5059   -935    741   -763       C
ATOM   5969  O   ALA C 215      15.561  34.929   7.926  1.00 39.61           O
ANISOU 5969  O   ALA C 215     4181   5461   5408   -891    777   -733       O
ATOM   5970  CB  ALA C 215      15.693  34.217  11.164  1.00 30.19           C
ANISOU 5970  CB  ALA C 215     2792   4439   4241   -879    566   -753       C
ATOM   5971  N   SER C 216      16.963  36.269   9.086  1.00 34.51           N
ANISOU 5971  N   SER C 216     3416   4870   4824  -1012    790   -808       N
ATOM   5972  CA  SER C 216      17.969  36.438   8.035  1.00 38.16           C
ANISOU 5972  CA  SER C 216     3864   5306   5330  -1047    893   -827       C
ATOM   5973  C   SER C 216      19.200  35.550   8.297  1.00 38.98           C
ANISOU 5973  C   SER C 216     3820   5483   5508  -1041    884   -842       C
ATOM   5974  O   SER C 216      19.461  35.133   9.434  1.00 36.70           O
ANISOU 5974  O   SER C 216     3434   5269   5241  -1033    801   -850       O
ATOM   5975  CB  SER C 216      18.415  37.914   7.946  1.00 35.80           C
ANISOU 5975  CB  SER C 216     3593   4970   5039  -1142    962   -870       C
ATOM   5976  OG  SER C 216      19.032  38.349   9.158  1.00 33.25           O
ANISOU 5976  OG  SER C 216     3172   4710   4750  -1198    914   -908       O
ATOM   5977  N   ASN C 217      19.987  35.299   7.237  1.00 40.16           N
ANISOU 5977  N   ASN C 217     3955   5608   5695  -1045    975   -846       N
ATOM   5978  CA  ASN C 217      21.198  34.483   7.362  1.00 39.07           C
ANISOU 5978  CA  ASN C 217     3676   5534   5633  -1036    980   -859       C
ATOM   5979  C   ASN C 217      22.115  34.727   6.163  1.00 42.76           C
ANISOU 5979  C   ASN C 217     4144   5960   6144  -1072   1107   -876       C
ATOM   5980  O   ASN C 217      21.642  34.753   5.022  1.00 43.01           O
ANISOU 5980  O   ASN C 217     4291   5913   6136  -1052   1176   -854       O
ATOM   5981  CB  ASN C 217      20.847  32.990   7.481  1.00 43.41           C
ANISOU 5981  CB  ASN C 217     4201   6118   6173   -939    915   -817       C
ATOM   5982  CG  ASN C 217      21.985  32.164   8.103  1.00 43.56           C
ANISOU 5982  CG  ASN C 217     4060   6224   6266   -924    881   -831       C
ATOM   5983  OD1 ASN C 217      22.984  32.733   8.548  1.00 39.42           O
ANISOU 5983  OD1 ASN C 217     3436   5742   5802   -988    893   -873       O
ATOM   5984  ND2 ASN C 217      21.844  30.815   8.108  1.00 36.10           N
ANISOU 5984  ND2 ASN C 217     3091   5306   5320   -838    839   -796       N
ATOM   5985  N   THR C 218      23.412  34.965   6.415  1.00 44.74           N
ANISOU 5985  N   THR C 218     4267   6257   6474  -1128   1141   -917       N
ATOM   5986  CA  THR C 218      24.356  35.194   5.319  1.00 47.70           C
ANISOU 5986  CA  THR C 218     4630   6593   6899  -1165   1269   -935       C
ATOM   5987  C   THR C 218      25.385  34.079   5.136  1.00 45.45           C
ANISOU 5987  C   THR C 218     4219   6360   6689  -1124   1288   -932       C
ATOM   5988  O   THR C 218      26.128  34.117   4.154  1.00 42.20           O
ANISOU 5988  O   THR C 218     3802   5914   6318  -1143   1401   -942       O
ATOM   5989  CB  THR C 218      25.085  36.552   5.478  1.00 45.92           C
ANISOU 5989  CB  THR C 218     4374   6361   6712  -1278   1328   -989       C
ATOM   5990  OG1 THR C 218      26.084  36.486   6.509  1.00 54.20           O
ANISOU 5990  OG1 THR C 218     5254   7503   7835  -1315   1275  -1024       O
ATOM   5991  CG2 THR C 218      24.123  37.673   5.785  1.00 37.36           C
ANISOU 5991  CG2 THR C 218     3409   5231   5557  -1318   1305   -994       C
ATOM   5992  N   SER C 219      25.379  33.041   5.977  1.00 46.29           N
ANISOU 5992  N   SER C 219     4238   6541   6809  -1060   1187   -915       N
ATOM   5993  CA  SER C 219      26.323  31.940   5.868  1.00 45.20           C
ANISOU 5993  CA  SER C 219     3980   6455   6741  -1011   1198   -909       C
ATOM   5994  C   SER C 219      25.585  30.638   5.541  1.00 44.48           C
ANISOU 5994  C   SER C 219     3950   6350   6602   -905   1163   -856       C
ATOM   5995  O   SER C 219      24.366  30.540   5.655  1.00 45.57           O
ANISOU 5995  O   SER C 219     4197   6458   6661   -871   1106   -827       O
ATOM   5996  CB  SER C 219      27.165  31.801   7.153  1.00 45.55           C
ANISOU 5996  CB  SER C 219     3852   6604   6851  -1029   1112   -937       C
ATOM   5997  OG  SER C 219      26.400  31.330   8.250  1.00 46.42           O
ANISOU 5997  OG  SER C 219     3964   6760   6915   -982    980   -917       O
ATOM   5998  N   ASN C 220      26.335  29.644   5.080  1.00 45.61           N
ANISOU 5998  N   ASN C 220     4023   6510   6795   -854   1203   -845       N
ATOM   5999  CA  ASN C 220      25.754  28.393   4.617  1.00 44.40           C
ANISOU 5999  CA  ASN C 220     3933   6336   6601   -758   1189   -797       C
ATOM   6000  C   ASN C 220      25.335  27.517   5.797  1.00 42.11           C
ANISOU 6000  C   ASN C 220     3589   6117   6295   -695   1053   -776       C
ATOM   6001  O   ASN C 220      25.744  27.739   6.941  1.00 39.39           O
ANISOU 6001  O   ASN C 220     3136   5847   5985   -720    977   -799       O
ATOM   6002  CB  ASN C 220      26.752  27.669   3.722  1.00 44.20           C
ANISOU 6002  CB  ASN C 220     3855   6302   6638   -726   1287   -793       C
ATOM   6003  CG  ASN C 220      28.077  27.458   4.412  1.00 44.89           C
ANISOU 6003  CG  ASN C 220     3751   6478   6827   -737   1275   -822       C
ATOM   6004  OD1 ASN C 220      28.198  26.619   5.308  1.00 41.67           O
ANISOU 6004  OD1 ASN C 220     3254   6142   6435   -682   1179   -810       O
ATOM   6005  ND2 ASN C 220      29.082  28.234   4.013  1.00 49.49           N
ANISOU 6005  ND2 ASN C 220     4269   7056   7479   -809   1370   -861       N
ATOM   6006  N   SER C 221      24.549  26.473   5.492  1.00 41.52           N
ANISOU 6006  N   SER C 221     3593   6017   6166   -614   1025   -731       N
ATOM   6007  CA  SER C 221      23.958  25.646   6.546  1.00 42.91           C
ANISOU 6007  CA  SER C 221     3746   6246   6312   -553    901   -707       C
ATOM   6008  C   SER C 221      25.017  25.008   7.426  1.00 43.96           C
ANISOU 6008  C   SER C 221     3714   6470   6518   -528    851   -719       C
ATOM   6009  O   SER C 221      24.906  25.029   8.662  1.00 39.91           O
ANISOU 6009  O   SER C 221     3141   6020   6002   -529    747   -727       O
ATOM   6010  CB  SER C 221      23.075  24.553   5.945  1.00 45.91           C
ANISOU 6010  CB  SER C 221     4233   6581   6631   -472    894   -658       C
ATOM   6011  OG  SER C 221      21.826  25.058   5.532  1.00 46.03           O
ANISOU 6011  OG  SER C 221     4393   6528   6567   -486    890   -642       O
ATOM   6012  N   TYR C 222      26.055  24.437   6.801  1.00 43.33           N
ANISOU 6012  N   TYR C 222     3561   6398   6504   -503    925   -721       N
ATOM   6013  CA  TYR C 222      27.096  23.745   7.552  1.00 46.55           C
ANISOU 6013  CA  TYR C 222     3809   6893   6986   -468    881   -730       C
ATOM   6014  C   TYR C 222      27.750  24.668   8.567  1.00 46.30           C
ANISOU 6014  C   TYR C 222     3659   6929   7004   -541    830   -774       C
ATOM   6015  O   TYR C 222      27.853  24.321   9.750  1.00 48.66           O
ANISOU 6015  O   TYR C 222     3877   7300   7310   -518    721   -776       O
ATOM   6016  CB  TYR C 222      28.144  23.162   6.608  1.00 51.79           C
ANISOU 6016  CB  TYR C 222     4414   7547   7718   -437    987   -728       C
ATOM   6017  CG  TYR C 222      29.366  22.650   7.329  1.00 53.20           C
ANISOU 6017  CG  TYR C 222     4410   7816   7987   -412    952   -743       C
ATOM   6018  CD1 TYR C 222      29.295  21.551   8.185  1.00 55.77           C
ANISOU 6018  CD1 TYR C 222     4686   8199   8306   -330    851   -718       C
ATOM   6019  CD2 TYR C 222      30.593  23.295   7.183  1.00 52.15           C
ANISOU 6019  CD2 TYR C 222     4154   7713   7949   -472   1018   -784       C
ATOM   6020  CE1 TYR C 222      30.435  21.074   8.836  1.00 56.57           C
ANISOU 6020  CE1 TYR C 222     4619   8384   8492   -301    815   -730       C
ATOM   6021  CE2 TYR C 222      31.716  22.847   7.832  1.00 54.72           C
ANISOU 6021  CE2 TYR C 222     4305   8123   8362   -449    983   -798       C
ATOM   6022  CZ  TYR C 222      31.644  21.741   8.660  1.00 57.68           C
ANISOU 6022  CZ  TYR C 222     4632   8555   8728   -361    879   -770       C
ATOM   6023  OH  TYR C 222      32.798  21.330   9.301  1.00 50.37           O
ANISOU 6023  OH  TYR C 222     3530   7716   7892   -336    840   -785       O
ATOM   6024  N   GLU C 223      28.196  25.852   8.130  1.00 42.11           N
ANISOU 6024  N   GLU C 223     3121   6373   6505   -632    908   -812       N
ATOM   6025  CA  GLU C 223      28.752  26.805   9.087  1.00 44.55           C
ANISOU 6025  CA  GLU C 223     3330   6740   6856   -711    860   -857       C
ATOM   6026  C   GLU C 223      27.696  27.210  10.107  1.00 45.84           C
ANISOU 6026  C   GLU C 223     3560   6913   6944   -725    749   -853       C
ATOM   6027  O   GLU C 223      27.990  27.335  11.303  1.00 43.79           O
ANISOU 6027  O   GLU C 223     3211   6726   6703   -741    653   -873       O
ATOM   6028  CB  GLU C 223      29.277  28.058   8.376  1.00 44.25           C
ANISOU 6028  CB  GLU C 223     3298   6661   6855   -811    970   -897       C
ATOM   6029  CG  GLU C 223      30.364  27.821   7.319  1.00 46.99           C
ANISOU 6029  CG  GLU C 223     3581   6991   7281   -811   1097   -905       C
ATOM   6030  CD  GLU C 223      31.760  27.699   7.907  1.00 54.12           C
ANISOU 6030  CD  GLU C 223     4285   7985   8295   -829   1082   -937       C
ATOM   6031  OE1 GLU C 223      32.221  26.548   8.147  1.00 55.41           O
ANISOU 6031  OE1 GLU C 223     4358   8199   8496   -747   1045   -916       O
ATOM   6032  OE2 GLU C 223      32.403  28.757   8.115  1.00 58.63           O
ANISOU 6032  OE2 GLU C 223     4788   8574   8916   -925   1107   -984       O
ATOM   6033  N   THR C 224      26.442  27.355   9.660  1.00 42.65           N
ANISOU 6033  N   THR C 224     3314   6437   6453   -712    758   -826       N
ATOM   6034  CA  THR C 224      25.383  27.813  10.553  1.00 42.82           C
ANISOU 6034  CA  THR C 224     3406   6459   6403   -727    667   -823       C
ATOM   6035  C   THR C 224      25.072  26.795  11.644  1.00 42.83           C
ANISOU 6035  C   THR C 224     3368   6522   6384   -654    545   -798       C
ATOM   6036  O   THR C 224      25.097  27.129  12.829  1.00 43.39           O
ANISOU 6036  O   THR C 224     3389   6645   6452   -680    456   -817       O
ATOM   6037  CB  THR C 224      24.125  28.144   9.747  1.00 40.25           C
ANISOU 6037  CB  THR C 224     3253   6043   5997   -724    708   -797       C
ATOM   6038  OG1 THR C 224      24.470  28.986   8.631  1.00 43.37           O
ANISOU 6038  OG1 THR C 224     3693   6377   6411   -783    829   -816       O
ATOM   6039  CG2 THR C 224      23.144  28.882  10.606  1.00 35.50           C
ANISOU 6039  CG2 THR C 224     2717   5438   5334   -755    634   -801       C
ATOM   6040  N   TYR C 225      24.824  25.539  11.281  1.00 42.83           N
ANISOU 6040  N   TYR C 225     3391   6514   6369   -565    541   -758       N
ATOM   6041  CA  TYR C 225      24.495  24.565  12.319  1.00 42.85           C
ANISOU 6041  CA  TYR C 225     3366   6569   6346   -496    429   -734       C
ATOM   6042  C   TYR C 225      25.708  24.268  13.195  1.00 49.06           C
ANISOU 6042  C   TYR C 225     3989   7446   7206   -490    374   -757       C
ATOM   6043  O   TYR C 225      25.566  24.058  14.408  1.00 48.83           O
ANISOU 6043  O   TYR C 225     3924   7471   7160   -474    266   -757       O
ATOM   6044  CB  TYR C 225      23.969  23.284  11.686  1.00 40.52           C
ANISOU 6044  CB  TYR C 225     3138   6241   6018   -404    443   -686       C
ATOM   6045  CG  TYR C 225      22.838  23.518  10.718  1.00 39.10           C
ANISOU 6045  CG  TYR C 225     3114   5972   5771   -407    497   -663       C
ATOM   6046  CD1 TYR C 225      21.884  24.473  10.974  1.00 39.41           C
ANISOU 6046  CD1 TYR C 225     3239   5980   5756   -456    475   -670       C
ATOM   6047  CD2 TYR C 225      22.740  22.795   9.537  1.00 42.31           C
ANISOU 6047  CD2 TYR C 225     3582   6324   6168   -360    572   -635       C
ATOM   6048  CE1 TYR C 225      20.841  24.703  10.105  1.00 39.10           C
ANISOU 6048  CE1 TYR C 225     3338   5862   5657   -457    517   -648       C
ATOM   6049  CE2 TYR C 225      21.709  23.018   8.648  1.00 43.35           C
ANISOU 6049  CE2 TYR C 225     3859   6376   6238   -364    614   -615       C
ATOM   6050  CZ  TYR C 225      20.752  23.976   8.947  1.00 41.68           C
ANISOU 6050  CZ  TYR C 225     3724   6138   5974   -412    583   -621       C
ATOM   6051  OH  TYR C 225      19.710  24.213   8.080  1.00 40.50           O
ANISOU 6051  OH  TYR C 225     3714   5912   5764   -413    619   -599       O
ATOM   6052  N   LYS C 226      26.914  24.310  12.611  1.00 51.76           N
ANISOU 6052  N   LYS C 226     4231   7805   7631   -507    448   -778       N
ATOM   6053  CA  LYS C 226      28.130  24.122  13.400  1.00 52.89           C
ANISOU 6053  CA  LYS C 226     4207   8036   7853   -508    397   -803       C
ATOM   6054  C   LYS C 226      28.292  25.222  14.455  1.00 52.23           C
ANISOU 6054  C   LYS C 226     4075   7995   7774   -594    328   -845       C
ATOM   6055  O   LYS C 226      28.917  24.991  15.498  1.00 55.43           O
ANISOU 6055  O   LYS C 226     4369   8479   8212   -585    237   -859       O
ATOM   6056  CB  LYS C 226      29.347  24.068  12.464  1.00 51.39           C
ANISOU 6056  CB  LYS C 226     3922   7848   7755   -518    504   -819       C
ATOM   6057  CG  LYS C 226      30.601  23.424  13.034  1.00 54.42           C
ANISOU 6057  CG  LYS C 226     4130   8320   8226   -482    462   -829       C
ATOM   6058  CD  LYS C 226      31.723  23.350  11.979  1.00 59.24           C
ANISOU 6058  CD  LYS C 226     4657   8923   8929   -488    585   -842       C
ATOM   6059  CE  LYS C 226      32.365  24.723  11.745  1.00 54.20           C
ANISOU 6059  CE  LYS C 226     3967   8281   8345   -606    650   -894       C
ATOM   6060  NZ  LYS C 226      33.325  24.733  10.608  1.00 57.82           N
ANISOU 6060  NZ  LYS C 226     4366   8717   8886   -618    787   -905       N
ATOM   6061  N  AGLU C 227      27.734  26.415  14.210  0.61 51.67           N
ANISOU 6061  N  AGLU C 227     4092   7872   7667   -674    367   -865       N
ATOM   6062  CA AGLU C 227      27.773  27.472  15.217  0.61 51.09           C
ANISOU 6062  CA AGLU C 227     3994   7831   7587   -756    303   -903       C
ATOM   6063  C  AGLU C 227      26.693  27.278  16.271  0.61 50.79           C
ANISOU 6063  C  AGLU C 227     4032   7800   7465   -725    193   -883       C
ATOM   6064  O  AGLU C 227      26.928  27.544  17.454  0.61 52.03           O
ANISOU 6064  O  AGLU C 227     4133   8014   7623   -751     99   -905       O
ATOM   6065  CB AGLU C 227      27.632  28.849  14.560  0.61 48.86           C
ANISOU 6065  CB AGLU C 227     3779   7487   7298   -854    393   -933       C
ATOM   6066  CG AGLU C 227      28.013  30.002  15.469  0.61 47.30           C
ANISOU 6066  CG AGLU C 227     3532   7324   7115   -951    347   -982       C
ATOM   6067  CD AGLU C 227      27.859  31.352  14.807  0.61 44.63           C
ANISOU 6067  CD AGLU C 227     3269   6921   6768  -1047    441  -1011       C
ATOM   6068  OE1AGLU C 227      27.554  31.380  13.599  0.61 40.87           O
ANISOU 6068  OE1AGLU C 227     2875   6374   6281  -1036    544   -994       O
ATOM   6069  OE2AGLU C 227      28.067  32.383  15.494  0.61 43.81           O
ANISOU 6069  OE2AGLU C 227     3145   6833   6667  -1132    411  -1051       O
ATOM   6070  N  BGLU C 227      27.740  26.416  14.207  0.39 52.29           N
ANISOU 6070  N  BGLU C 227     4171   7952   7746   -675    368   -865       N
ATOM   6071  CA BGLU C 227      27.776  27.473  15.215  0.39 50.97           C
ANISOU 6071  CA BGLU C 227     3979   7815   7571   -756    303   -903       C
ATOM   6072  C  BGLU C 227      26.699  27.264  16.272  0.39 46.88           C
ANISOU 6072  C  BGLU C 227     3537   7306   6970   -724    193   -883       C
ATOM   6073  O  BGLU C 227      26.945  27.496  17.461  0.39 48.82           O
ANISOU 6073  O  BGLU C 227     3723   7609   7217   -748     98   -904       O
ATOM   6074  CB BGLU C 227      27.630  28.852  14.554  0.39 48.92           C
ANISOU 6074  CB BGLU C 227     3788   7495   7307   -854    394   -933       C
ATOM   6075  CG BGLU C 227      27.303  29.990  15.524  0.39 46.72           C
ANISOU 6075  CG BGLU C 227     3534   7225   6993   -935    333   -966       C
ATOM   6076  CD BGLU C 227      28.490  30.922  15.771  0.39 46.53           C
ANISOU 6076  CD BGLU C 227     3393   7241   7044  -1033    351  -1022       C
ATOM   6077  OE1BGLU C 227      29.644  30.502  15.512  0.39 44.55           O
ANISOU 6077  OE1BGLU C 227     3011   7036   6880  -1027    377  -1035       O
ATOM   6078  OE2BGLU C 227      28.272  32.063  16.252  0.39 44.42           O
ANISOU 6078  OE2BGLU C 227     3165   6962   6752  -1117    336  -1054       O
ATOM   6079  N   ILE C 228      25.510  26.805  15.865  1.00 53.97           N
ANISOU 6079  N   ILE C 228     4565   8145   7795   -670    203   -841       N
ATOM   6080  CA  ILE C 228      24.448  26.541  16.835  1.00 49.06           C
ANISOU 6080  CA  ILE C 228     4016   7528   7097   -636    106   -819       C
ATOM   6081  C   ILE C 228      24.860  25.414  17.761  1.00 49.37           C
ANISOU 6081  C   ILE C 228     3970   7639   7150   -564      9   -805       C
ATOM   6082  O   ILE C 228      24.610  25.458  18.974  1.00 47.60           O
ANISOU 6082  O   ILE C 228     3740   7453   6893   -565    -90   -810       O
ATOM   6083  CB  ILE C 228      23.124  26.183  16.135  1.00 46.58           C
ANISOU 6083  CB  ILE C 228     3848   7139   6710   -590    140   -777       C
ATOM   6084  CG1 ILE C 228      22.671  27.276  15.162  1.00 41.35           C
ANISOU 6084  CG1 ILE C 228     3279   6401   6030   -653    235   -788       C
ATOM   6085  CG2 ILE C 228      22.093  25.830  17.190  1.00 33.31           C
ANISOU 6085  CG2 ILE C 228     2228   5468   4959   -552     42   -754       C
ATOM   6086  CD1 ILE C 228      22.179  28.486  15.822  1.00 40.28           C
ANISOU 6086  CD1 ILE C 228     3191   6254   5859   -725    207   -813       C
ATOM   6087  N   ALA C 229      25.507  24.389  17.195  1.00 46.48           N
ANISOU 6087  N   ALA C 229     3541   7289   6830   -499     40   -785       N
ATOM   6088  CA  ALA C 229      25.944  23.231  17.960  1.00 48.47           C
ANISOU 6088  CA  ALA C 229     3715   7606   7097   -420    -44   -768       C
ATOM   6089  C   ALA C 229      26.867  23.638  19.098  1.00 52.14           C
ANISOU 6089  C   ALA C 229     4055   8151   7605   -459   -129   -805       C
ATOM   6090  O   ALA C 229      26.751  23.116  20.215  1.00 52.68           O
ANISOU 6090  O   ALA C 229     4106   8265   7644   -418   -236   -796       O
ATOM   6091  CB  ALA C 229      26.632  22.236  17.028  1.00 52.26           C
ANISOU 6091  CB  ALA C 229     4141   8085   7631   -353     22   -747       C
ATOM   6092  N   LYS C 230      27.802  24.559  18.827  1.00 51.89           N
ANISOU 6092  N   LYS C 230     3938   8137   7642   -540    -82   -849       N
ATOM   6093  CA  LYS C 230      28.698  25.034  19.875  1.00 50.46           C
ANISOU 6093  CA  LYS C 230     3637   8032   7504   -589   -164   -889       C
ATOM   6094  C   LYS C 230      27.914  25.671  21.011  1.00 45.09           C
ANISOU 6094  C   LYS C 230     3029   7352   6749   -629   -253   -900       C
ATOM   6095  O   LYS C 230      28.247  25.462  22.181  1.00 46.74           O
ANISOU 6095  O   LYS C 230     3179   7625   6956   -618   -363   -910       O
ATOM   6096  CB  LYS C 230      29.722  26.026  19.310  1.00 53.61           C
ANISOU 6096  CB  LYS C 230     3946   8439   7986   -682    -87   -935       C
ATOM   6097  N   ILE C 231      26.849  26.421  20.692  1.00 46.38           N
ANISOU 6097  N   ILE C 231     3328   7446   6849   -671   -208   -897       N
ATOM   6098  CA  ILE C 231      26.051  27.060  21.743  1.00 45.69           C
ANISOU 6098  CA  ILE C 231     3318   7353   6690   -708   -282   -907       C
ATOM   6099  C   ILE C 231      25.458  26.012  22.668  1.00 49.42           C
ANISOU 6099  C   ILE C 231     3823   7849   7105   -621   -382   -871       C
ATOM   6100  O   ILE C 231      25.379  26.213  23.888  1.00 48.42           O
ANISOU 6100  O   ILE C 231     3694   7757   6945   -637   -478   -885       O
ATOM   6101  CB  ILE C 231      24.913  27.911  21.146  1.00 48.23           C
ANISOU 6101  CB  ILE C 231     3784   7589   6953   -750   -210   -901       C
ATOM   6102  CG1 ILE C 231      25.370  28.847  20.035  1.00 48.36           C
ANISOU 6102  CG1 ILE C 231     3793   7566   7016   -824    -96   -929       C
ATOM   6103  CG2 ILE C 231      24.187  28.693  22.227  1.00 46.28           C
ANISOU 6103  CG2 ILE C 231     3610   7335   6639   -795   -277   -916       C
ATOM   6104  CD1 ILE C 231      24.201  29.721  19.511  1.00 38.73           C
ANISOU 6104  CD1 ILE C 231     2723   6260   5731   -861    -33   -922       C
ATOM   6105  N   MET C 232      25.026  24.878  22.104  1.00 47.86           N
ANISOU 6105  N   MET C 232     3663   7628   6892   -531   -358   -826       N
ATOM   6106  CA  MET C 232      24.389  23.823  22.882  1.00 52.75           C
ANISOU 6106  CA  MET C 232     4327   8261   7455   -446   -440   -789       C
ATOM   6107  C   MET C 232      25.381  22.776  23.383  1.00 53.07           C
ANISOU 6107  C   MET C 232     4249   8374   7540   -379   -507   -782       C
ATOM   6108  O   MET C 232      24.958  21.777  23.984  1.00 57.02           O
ANISOU 6108  O   MET C 232     4782   8886   7998   -301   -572   -749       O
ATOM   6109  CB  MET C 232      23.298  23.134  22.052  1.00 52.64           C
ANISOU 6109  CB  MET C 232     4427   8180   7394   -386   -383   -742       C
ATOM   6110  CG  MET C 232      22.242  24.064  21.535  1.00 52.86           C
ANISOU 6110  CG  MET C 232     4574   8136   7375   -439   -322   -743       C
ATOM   6111  SD  MET C 232      20.797  23.139  21.008  1.00 61.55           S
ANISOU 6111  SD  MET C 232     5809   9171   8405   -362   -299   -687       S
ATOM   6112  CE  MET C 232      21.008  23.228  19.230  1.00 49.63           C
ANISOU 6112  CE  MET C 232     4314   7606   6936   -370   -169   -681       C
ATOM   6113  N   ASP C 233      26.676  22.978  23.139  1.00 52.38           N
ANISOU 6113  N   ASP C 233     4028   8334   7540   -406   -491   -811       N
ATOM   6114  CA  ASP C 233      27.741  22.066  23.540  1.00 53.99           C
ANISOU 6114  CA  ASP C 233     4103   8610   7800   -344   -549   -807       C
ATOM   6115  C   ASP C 233      27.693  20.770  22.746  1.00 52.96           C
ANISOU 6115  C   ASP C 233     3982   8460   7679   -242   -501   -762       C
ATOM   6116  O   ASP C 233      28.045  19.702  23.256  1.00 53.18           O
ANISOU 6116  O   ASP C 233     3963   8531   7713   -159   -566   -740       O
ATOM   6117  CB  ASP C 233      27.754  21.795  25.047  1.00 54.06           C
ANISOU 6117  CB  ASP C 233     4097   8674   7769   -321   -688   -810       C
ATOM   6118  CG  ASP C 233      29.111  21.323  25.522  1.00 60.04           C
ANISOU 6118  CG  ASP C 233     4694   9518   8602   -291   -754   -824       C
ATOM   6119  OD1 ASP C 233      29.980  21.174  24.641  1.00 59.27           O
ANISOU 6119  OD1 ASP C 233     4499   9433   8587   -286   -684   -829       O
ATOM   6120  OD2 ASP C 233      29.324  21.132  26.746  1.00 65.28           O
ANISOU 6120  OD2 ASP C 233     5328  10234   9243   -275   -873   -830       O
ATOM   6121  N   VAL C 234      27.110  20.813  21.562  1.00 52.69           N
ANISOU 6121  N   VAL C 234     4030   8355   7633   -244   -394   -745       N
ATOM   6122  CA  VAL C 234      27.155  19.640  20.712  1.00 54.66           C
ANISOU 6122  CA  VAL C 234     4288   8583   7897   -156   -339   -706       C
ATOM   6123  C   VAL C 234      28.498  19.734  20.016  1.00 59.28           C
ANISOU 6123  C   VAL C 234     4738   9199   8585   -169   -275   -728       C
ATOM   6124  O   VAL C 234      28.786  20.748  19.363  1.00 61.38           O
ANISOU 6124  O   VAL C 234     4989   9444   8889   -252   -198   -760       O
ATOM   6125  CB  VAL C 234      25.989  19.607  19.720  1.00 54.60           C
ANISOU 6125  CB  VAL C 234     4427   8488   7833   -152   -256   -678       C
ATOM   6126  CG1 VAL C 234      26.189  18.503  18.698  1.00 51.77           C
ANISOU 6126  CG1 VAL C 234     4071   8102   7496    -73   -185   -644       C
ATOM   6127  CG2 VAL C 234      24.688  19.466  20.472  1.00 50.64           C
ANISOU 6127  CG2 VAL C 234     4045   7961   7237   -135   -322   -656       C
ATOM   6128  N   PRO C 235      29.338  18.713  20.121  1.00 62.02           N
ANISOU 6128  N   PRO C 235     4989   9595   8983    -90   -299   -713       N
ATOM   6129  CA  PRO C 235      30.672  18.806  19.525  1.00 58.78           C
ANISOU 6129  CA  PRO C 235     4435   9220   8679   -102   -239   -736       C
ATOM   6130  C   PRO C 235      30.598  19.104  18.030  1.00 58.58           C
ANISOU 6130  C   PRO C 235     4458   9124   8676   -130    -92   -734       C
ATOM   6131  O   PRO C 235      29.678  18.666  17.337  1.00 60.93           O
ANISOU 6131  O   PRO C 235     4884   9353   8915    -94    -39   -701       O
ATOM   6132  CB  PRO C 235      31.281  17.434  19.826  1.00 58.76           C
ANISOU 6132  CB  PRO C 235     4357   9264   8705     12   -286   -706       C
ATOM   6133  CG  PRO C 235      30.514  16.962  21.097  1.00 53.59           C
ANISOU 6133  CG  PRO C 235     3769   8628   7964     55   -415   -686       C
ATOM   6134  CD  PRO C 235      29.134  17.465  20.891  1.00 57.62           C
ANISOU 6134  CD  PRO C 235     4443   9065   8386     12   -388   -677       C
ATOM   6135  N   GLU C 236      31.551  19.917  17.558  1.00 59.42           N
ANISOU 6135  N   GLU C 236     4464   9247   8865   -201    -27   -773       N
ATOM   6136  CA  GLU C 236      31.630  20.287  16.147  1.00 56.21           C
ANISOU 6136  CA  GLU C 236     4096   8776   8488   -234    118   -777       C
ATOM   6137  C   GLU C 236      31.870  19.064  15.276  1.00 58.12           C
ANISOU 6137  C   GLU C 236     4339   8994   8751   -136    188   -739       C
ATOM   6138  O   GLU C 236      31.501  19.058  14.095  1.00 61.24           O
ANISOU 6138  O   GLU C 236     4825   9314   9130   -138    298   -725       O
ATOM   6139  CB  GLU C 236      32.731  21.326  15.923  1.00 55.79           C
ANISOU 6139  CB  GLU C 236     3919   8751   8526   -327    171   -828       C
ATOM   6140  N   ASN C 237      32.586  18.068  15.804  1.00 53.45           N
ANISOU 6140  N   ASN C 237     3643   8465   8202    -54    129   -724       N
ATOM   6141  CA  ASN C 237      32.889  16.891  15.008  1.00 55.80           C
ANISOU 6141  CA  ASN C 237     3938   8740   8523     43    197   -688       C
ATOM   6142  C   ASN C 237      31.618  16.174  14.576  1.00 60.75           C
ANISOU 6142  C   ASN C 237     4741   9292   9050     98    213   -643       C
ATOM   6143  O   ASN C 237      31.648  15.424  13.596  1.00 64.80           O
ANISOU 6143  O   ASN C 237     5296   9758   9567    155    301   -616       O
ATOM   6144  CB  ASN C 237      33.797  15.942  15.790  1.00 51.46           C
ANISOU 6144  CB  ASN C 237     3252   8273   8027    128    117   -678       C
ATOM   6145  N   LEU C 238      30.510  16.383  15.290  1.00 59.55           N
ANISOU 6145  N   LEU C 238     4691   9127   8809     81    131   -636       N
ATOM   6146  CA  LEU C 238      29.248  15.710  15.017  1.00 61.43           C
ANISOU 6146  CA  LEU C 238     5090   9300   8952    129    132   -594       C
ATOM   6147  C   LEU C 238      28.414  16.370  13.908  1.00 63.74           C
ANISOU 6147  C   LEU C 238     5513   9504   9201     72    229   -594       C
ATOM   6148  O   LEU C 238      27.296  15.913  13.659  1.00 62.92           O
ANISOU 6148  O   LEU C 238     5544   9344   9018    102    227   -562       O
ATOM   6149  CB  LEU C 238      28.435  15.601  16.311  1.00 58.60           C
ANISOU 6149  CB  LEU C 238     4778   8968   8520    140      3   -585       C
ATOM   6150  CG  LEU C 238      28.823  14.503  17.316  1.00 57.28           C
ANISOU 6150  CG  LEU C 238     4546   8862   8356    231    -97   -565       C
ATOM   6151  CD1 LEU C 238      30.111  14.816  18.017  1.00 61.85           C
ANISOU 6151  CD1 LEU C 238     4953   9529   9019    216   -149   -597       C
ATOM   6152  CD2 LEU C 238      27.748  14.293  18.349  1.00 59.34           C
ANISOU 6152  CD2 LEU C 238     4900   9122   8526    246   -199   -548       C
ATOM   6153  N   VAL C 239      28.888  17.457  13.284  1.00 66.32           N
ANISOU 6153  N   VAL C 239     5807   9815   9575    -11    308   -629       N
ATOM   6154  CA  VAL C 239      28.204  18.125  12.175  1.00 64.21           C
ANISOU 6154  CA  VAL C 239     5662   9463   9271    -65    405   -629       C
ATOM   6155  C   VAL C 239      29.146  17.998  10.969  1.00 63.48           C
ANISOU 6155  C   VAL C 239     5524   9346   9249    -59    533   -635       C
ATOM   6156  O   VAL C 239      30.117  18.761  10.849  1.00 58.96           O
ANISOU 6156  O   VAL C 239     4847   8801   8755   -119    578   -672       O
ATOM   6157  CB  VAL C 239      27.897  19.588  12.541  1.00 63.60           C
ANISOU 6157  CB  VAL C 239     5601   9384   9180   -171    388   -667       C
ATOM   6158  CG1 VAL C 239      27.092  20.345  11.477  1.00 58.93           C
ANISOU 6158  CG1 VAL C 239     5145   8703   8541   -225    477   -666       C
ATOM   6159  CG2 VAL C 239      27.358  19.737  13.991  1.00 63.54           C
ANISOU 6159  CG2 VAL C 239     5590   9425   9127   -177    252   -670       C
ATOM   6160  N   GLU C 240      28.887  17.027  10.076  1.00 61.01           N
ANISOU 6160  N   GLU C 240     5290   8979   8912     11    596   -598       N
ATOM   6161  CA  GLU C 240      29.739  16.751   8.904  1.00 63.39           C
ANISOU 6161  CA  GLU C 240     5562   9250   9275     28    723   -598       C
ATOM   6162  C   GLU C 240      29.082  17.462   7.731  1.00 64.47           C
ANISOU 6162  C   GLU C 240     5836   9294   9367    -29    822   -600       C
ATOM   6163  O   GLU C 240      27.847  17.518   7.708  1.00 62.17           O
ANISOU 6163  O   GLU C 240     5679   8956   8986    -33    786   -581       O
ATOM   6164  CB  GLU C 240      29.799  15.234   8.641  1.00 59.85           C
ANISOU 6164  CB  GLU C 240     5133   8792   8817    142    731   -556       C
ATOM   6165  N   ASN C 241      29.797  18.046   6.751  1.00 67.11           N
ANISOU 6165  N   ASN C 241     6149   9594   9755    -75    944   -622       N
ATOM   6166  CA  ASN C 241      28.890  18.503   5.714  1.00 70.95           C
ANISOU 6166  CA  ASN C 241     6802   9985  10172   -110   1015   -613       C
ATOM   6167  C   ASN C 241      29.240  17.591   4.545  1.00 71.69           C
ANISOU 6167  C   ASN C 241     6938  10025  10276    -47   1123   -588       C
ATOM   6168  O   ASN C 241      30.432  17.321   4.279  1.00 74.82           O
ANISOU 6168  O   ASN C 241     7222  10448  10759    -28   1191   -599       O
ATOM   6169  CB  ASN C 241      28.980  19.973   5.235  1.00 70.31           C
ANISOU 6169  CB  ASN C 241     6743   9870  10103   -217   1085   -651       C
ATOM   6170  CG  ASN C 241      29.885  20.263   3.908  1.00 73.66           C
ANISOU 6170  CG  ASN C 241     7161  10242  10586   -244   1248   -666       C
ATOM   6171  OD1 ASN C 241      30.106  19.369   3.058  1.00 80.23           O
ANISOU 6171  OD1 ASN C 241     8028  11034  11421   -181   1323   -641       O
ATOM   6172  ND2 ASN C 241      30.541  21.419   3.907  1.00 72.87           N
ANISOU 6172  ND2 ASN C 241     6991  10155  10543   -333   1295   -709       N
ATOM   6173  N   ASP C 242      28.232  17.235   3.761  1.00 65.26           N
ANISOU 6173  N   ASP C 242     6290   9129   9376    -25   1149   -557       N
ATOM   6174  CA  ASP C 242      28.368  16.420   2.556  1.00 67.42           C
ANISOU 6174  CA  ASP C 242     6642   9335   9640     29   1253   -532       C
ATOM   6175  C   ASP C 242      28.437  17.334   1.330  1.00 69.84           C
ANISOU 6175  C   ASP C 242     7031   9563   9943    -38   1378   -549       C
ATOM   6176  O   ASP C 242      27.527  18.140   1.094  1.00 70.65           O
ANISOU 6176  O   ASP C 242     7245   9618   9981    -94   1368   -553       O
ATOM   6177  CB  ASP C 242      27.191  15.456   2.492  1.00 66.39           C
ANISOU 6177  CB  ASP C 242     6646   9164   9414     91   1195   -489       C
ATOM   6178  CG  ASP C 242      27.057  14.732   1.148  1.00 67.64           C
ANISOU 6178  CG  ASP C 242     6928   9233   9537    133   1298   -462       C
ATOM   6179  OD1 ASP C 242      27.916  14.827   0.239  1.00 64.33           O
ANISOU 6179  OD1 ASP C 242     6493   8781   9167    127   1421   -473       O
ATOM   6180  OD2 ASP C 242      26.007  14.089   0.989  1.00 69.89           O
ANISOU 6180  OD2 ASP C 242     7339   9477   9739    169   1255   -430       O
ATOM   6181  N   THR C 243      29.528  17.232   0.570  1.00 66.90           N
ANISOU 6181  N   THR C 243     6602   9175   9641    -33   1499   -560       N
ATOM   6182  CA  THR C 243      29.666  18.046  -0.635  1.00 63.04           C
ANISOU 6182  CA  THR C 243     6197   8606   9150    -94   1629   -577       C
ATOM   6183  C   THR C 243      28.780  17.552  -1.783  1.00 65.29           C
ANISOU 6183  C   THR C 243     6679   8787   9341    -62   1681   -543       C
ATOM   6184  O   THR C 243      28.459  18.342  -2.681  1.00 66.29           O
ANISOU 6184  O   THR C 243     6919   8839   9431   -117   1756   -551       O
ATOM   6185  CB  THR C 243      31.157  18.093  -1.035  1.00 68.56           C
ANISOU 6185  CB  THR C 243     6765   9324   9960   -100   1745   -600       C
ATOM   6186  OG1 THR C 243      31.908  18.780  -0.016  1.00 64.36           O
ANISOU 6186  OG1 THR C 243     6058   8884   9511   -149   1694   -638       O
ATOM   6187  CG2 THR C 243      31.422  18.673  -2.452  1.00 69.53           C
ANISOU 6187  CG2 THR C 243     6983   9352  10081   -146   1906   -612       C
ATOM   6188  N   ASN C 244      28.329  16.288  -1.752  1.00 66.70           N
ANISOU 6188  N   ASN C 244     6908   8958   9475     23   1637   -505       N
ATOM   6189  CA  ASN C 244      27.549  15.800  -2.874  1.00 72.49           C
ANISOU 6189  CA  ASN C 244     7828   9593  10123     49   1688   -474       C
ATOM   6190  C   ASN C 244      26.117  16.331  -2.815  1.00 70.55           C
ANISOU 6190  C   ASN C 244     7716   9310   9779     12   1608   -465       C
ATOM   6191  O   ASN C 244      25.513  16.517  -3.874  1.00 65.81           O
ANISOU 6191  O   ASN C 244     7272   8621   9113     -4   1664   -454       O
ATOM   6192  CB  ASN C 244      27.584  14.271  -2.937  1.00 66.22           C
ANISOU 6192  CB  ASN C 244     7049   8796   9315    149   1679   -438       C
ATOM   6193  CG  ASN C 244      27.697  13.764  -4.347  1.00 74.52           C
ANISOU 6193  CG  ASN C 244     8228   9751  10337    176   1805   -421       C
ATOM   6194  OD1 ASN C 244      28.641  14.105  -5.063  1.00 71.69           O
ANISOU 6194  OD1 ASN C 244     7838   9366  10036    157   1930   -439       O
ATOM   6195  ND2 ASN C 244      26.713  12.975  -4.778  1.00 79.68           N
ANISOU 6195  ND2 ASN C 244     9033  10346  10898    217   1775   -387       N
ATOM   6196  N   ARG C 245      25.620  16.683  -1.615  1.00 75.85           N
ANISOU 6196  N   ARG C 245     8327  10049  10444     -7   1484   -472       N
ATOM   6197  CA  ARG C 245      24.446  17.526  -1.427  1.00 73.11           C
ANISOU 6197  CA  ARG C 245     8071   9679  10027    -59   1417   -473       C
ATOM   6198  C   ARG C 245      24.461  18.708  -2.354  1.00 68.39           C
ANISOU 6198  C   ARG C 245     7551   9014   9418   -132   1509   -494       C
ATOM   6199  O   ARG C 245      25.368  19.554  -2.280  1.00 69.98           O
ANISOU 6199  O   ARG C 245     7660   9240   9689   -186   1567   -529       O
ATOM   6200  CB  ARG C 245      24.425  18.117  -0.051  1.00 73.28           C
ANISOU 6200  CB  ARG C 245     7978   9787  10079    -91   1313   -494       C
ATOM   6201  CG  ARG C 245      24.520  17.158   0.978  1.00 75.68           C
ANISOU 6201  CG  ARG C 245     8193  10162  10399    -30   1221   -479       C
ATOM   6202  CD  ARG C 245      23.059  16.710   1.185  1.00 80.27           C
ANISOU 6202  CD  ARG C 245     8897  10717  10885     -3   1130   -447       C
ATOM   6203  NE  ARG C 245      22.767  15.730   2.237  1.00 84.50           N
ANISOU 6203  NE  ARG C 245     9386  11311  11411     58   1024   -426       N
ATOM   6204  CZ  ARG C 245      21.898  15.820   3.165  1.00 86.44           C
ANISOU 6204  CZ  ARG C 245     9640  11586  11616     53    917   -420       C
ATOM   6205  NH1 ARG C 245      21.007  16.846   3.310  1.00 83.98           N
ANISOU 6205  NH1 ARG C 245     9390  11257  11263     -7    881   -429       N
ATOM   6206  NH2 ARG C 245      21.835  14.903   4.031  1.00 84.83           N
ANISOU 6206  NH2 ARG C 245     9390  11431  11411    110    839   -403       N
ATOM   6207  N   PHE C 246      23.398  18.819  -3.122  1.00 62.90           N
ANISOU 6207  N   PHE C 246     7023   8240   8635   -138   1512   -474       N
ATOM   6208  CA  PHE C 246      23.145  19.945  -4.006  1.00 62.79           C
ANISOU 6208  CA  PHE C 246     7114   8153   8589   -203   1583   -488       C
ATOM   6209  C   PHE C 246      24.371  20.356  -4.808  1.00 67.18           C
ANISOU 6209  C   PHE C 246     7635   8680   9208   -233   1728   -514       C
ATOM   6210  O   PHE C 246      24.650  21.545  -4.960  1.00 62.22           O
ANISOU 6210  O   PHE C 246     7002   8038   8601   -305   1778   -544       O
ATOM   6211  CB  PHE C 246      22.605  21.164  -3.248  1.00 61.80           C
ANISOU 6211  CB  PHE C 246     6971   8056   8454   -268   1514   -510       C
ATOM   6212  CG  PHE C 246      21.470  20.860  -2.319  1.00 58.04           C
ANISOU 6212  CG  PHE C 246     6509   7617   7927   -243   1374   -489       C
ATOM   6213  CD1 PHE C 246      20.220  20.538  -2.818  1.00 58.46           C
ANISOU 6213  CD1 PHE C 246     6709   7611   7891   -219   1335   -457       C
ATOM   6214  CD2 PHE C 246      21.653  20.891  -0.950  1.00 55.25           C
ANISOU 6214  CD2 PHE C 246     6021   7355   7615   -244   1284   -502       C
ATOM   6215  CE1 PHE C 246      19.176  20.215  -1.964  1.00 56.38           C
ANISOU 6215  CE1 PHE C 246     6455   7382   7587   -196   1212   -437       C
ATOM   6216  CE2 PHE C 246      20.609  20.608  -0.088  1.00 56.60           C
ANISOU 6216  CE2 PHE C 246     6209   7556   7739   -222   1163   -483       C
ATOM   6217  CZ  PHE C 246      19.367  20.255  -0.593  1.00 52.97           C
ANISOU 6217  CZ  PHE C 246     5891   7038   7195   -197   1129   -450       C
ATOM   6218  N   LYS C 247      25.083  19.386  -5.379  1.00 67.54           N
ANISOU 6218  N   LYS C 247     7669   8710   9283   -180   1803   -502       N
ATOM   6219  CA  LYS C 247      26.327  19.722  -6.064  1.00 70.33           C
ANISOU 6219  CA  LYS C 247     7971   9042   9708   -206   1945   -526       C
ATOM   6220  C   LYS C 247      26.055  20.409  -7.395  1.00 78.27           C
ANISOU 6220  C   LYS C 247     9143   9938  10658   -248   2052   -528       C
ATOM   6221  O   LYS C 247      26.791  21.329  -7.790  1.00 74.96           O
ANISOU 6221  O   LYS C 247     8697   9499  10285   -309   2152   -559       O
ATOM   6222  CB  LYS C 247      27.174  18.464  -6.244  1.00 67.64           C
ANISOU 6222  CB  LYS C 247     7565   8717   9417   -131   1997   -511       C
ATOM   6223  N   ALA C 248      24.983  19.997  -8.081  1.00 75.69           N
ANISOU 6223  N   ALA C 248     8989   9538  10231   -219   2028   -496       N
ATOM   6224  CA  ALA C 248      24.655  20.589  -9.373  1.00 77.53           C
ANISOU 6224  CA  ALA C 248     9395   9662  10401   -253   2120   -495       C
ATOM   6225  C   ALA C 248      24.395  22.086  -9.236  1.00 75.43           C
ANISOU 6225  C   ALA C 248     9145   9387  10127   -336   2117   -522       C
ATOM   6226  O   ALA C 248      24.971  22.906  -9.966  1.00 70.49           O
ANISOU 6226  O   ALA C 248     8555   8709   9520   -387   2234   -545       O
ATOM   6227  CB  ALA C 248      23.443  19.872  -9.971  1.00 79.48           C
ANISOU 6227  CB  ALA C 248     9816   9844  10539   -208   2067   -455       C
ATOM   6228  N   GLN C 249      23.549  22.463  -8.287  1.00 72.85           N
ANISOU 6228  N   GLN C 249     8795   9110   9776   -349   1988   -520       N
ATOM   6229  CA  GLN C 249      23.267  23.867  -8.044  1.00 70.89           C
ANISOU 6229  CA  GLN C 249     8559   8858   9520   -424   1976   -545       C
ATOM   6230  C   GLN C 249      22.928  24.054  -6.576  1.00 71.80           C
ANISOU 6230  C   GLN C 249     8553   9069   9659   -431   1844   -553       C
ATOM   6231  O   GLN C 249      22.174  23.262  -5.998  1.00 71.28           O
ANISOU 6231  O   GLN C 249     8486   9037   9559   -380   1734   -526       O
ATOM   6232  CB  GLN C 249      22.106  24.375  -8.895  1.00 67.91           C
ANISOU 6232  CB  GLN C 249     8378   8386   9037   -436   1970   -526       C
ATOM   6233  CG  GLN C 249      21.987  25.880  -8.942  1.00 65.98           C
ANISOU 6233  CG  GLN C 249     8170   8115   8784   -513   1997   -553       C
ATOM   6234  CD  GLN C 249      20.586  26.312  -9.303  1.00 65.99           C
ANISOU 6234  CD  GLN C 249     8332   8056   8683   -512   1932   -530       C
ATOM   6235  OE1 GLN C 249      20.337  26.775 -10.418  1.00 67.50           O
ANISOU 6235  OE1 GLN C 249     8676   8153   8818   -528   2004   -525       O
ATOM   6236  NE2 GLN C 249      19.661  26.187  -8.347  1.00 60.07           N
ANISOU 6236  NE2 GLN C 249     7552   7361   7911   -493   1796   -516       N
ATOM   6237  N   ALA C 250      23.510  25.088  -5.981  1.00 64.03           N
ANISOU 6237  N   ALA C 250     7469   8126   8732   -497   1857   -590       N
ATOM   6238  CA  ALA C 250      23.262  25.373  -4.581  1.00 55.40           C
ANISOU 6238  CA  ALA C 250     6266   7122   7663   -511   1738   -602       C
ATOM   6239  C   ALA C 250      21.779  25.672  -4.369  1.00 54.58           C
ANISOU 6239  C   ALA C 250     6276   6994   7469   -507   1638   -580       C
ATOM   6240  O   ALA C 250      21.119  26.248  -5.239  1.00 54.31           O
ANISOU 6240  O   ALA C 250     6390   6877   7369   -526   1674   -571       O
ATOM   6241  CB  ALA C 250      24.115  26.573  -4.154  1.00 52.22           C
ANISOU 6241  CB  ALA C 250     5763   6751   7328   -594   1783   -649       C
ATOM   6242  N   ARG C 251      21.234  25.246  -3.221  1.00 46.93           N
ANISOU 6242  N   ARG C 251     5240   6095   6495   -478   1512   -569       N
ATOM   6243  CA  ARG C 251      19.952  25.781  -2.743  1.00 47.32           C
ANISOU 6243  CA  ARG C 251     5361   6139   6480   -488   1416   -557       C
ATOM   6244  C   ARG C 251      20.243  27.039  -1.964  1.00 40.01           C
ANISOU 6244  C   ARG C 251     4363   5249   5589   -560   1406   -594       C
ATOM   6245  O   ARG C 251      20.736  26.959  -0.836  1.00 41.99           O
ANISOU 6245  O   ARG C 251     4475   5585   5894   -566   1350   -612       O
ATOM   6246  CB  ARG C 251      19.197  24.859  -1.805  1.00 42.33           C
ANISOU 6246  CB  ARG C 251     4694   5563   5826   -431   1289   -531       C
ATOM   6247  CG  ARG C 251      18.529  23.752  -2.421  1.00 53.60           C
ANISOU 6247  CG  ARG C 251     6215   6952   7200   -367   1271   -491       C
ATOM   6248  CD  ARG C 251      17.940  22.982  -1.264  1.00 56.57           C
ANISOU 6248  CD  ARG C 251     6529   7396   7568   -324   1148   -474       C
ATOM   6249  NE  ARG C 251      16.505  22.951  -1.053  1.00 44.26           N
ANISOU 6249  NE  ARG C 251     5059   5820   5939   -308   1058   -447       N
ATOM   6250  CZ  ARG C 251      15.689  22.237  -1.804  1.00 48.85           C
ANISOU 6250  CZ  ARG C 251     5755   6347   6459   -268   1046   -414       C
ATOM   6251  NH1 ARG C 251      16.147  21.518  -2.812  1.00 52.06           N
ANISOU 6251  NH1 ARG C 251     6212   6708   6861   -240   1119   -403       N
ATOM   6252  NH2 ARG C 251      14.393  22.194  -1.527  1.00 54.99           N
ANISOU 6252  NH2 ARG C 251     6597   7117   7181   -255    959   -391       N
ATOM   6253  N   ASN C 252      19.937  28.184  -2.546  1.00 39.49           N
ANISOU 6253  N   ASN C 252     4395   5120   5490   -612   1457   -606       N
ATOM   6254  CA  ASN C 252      19.963  29.445  -1.813  1.00 42.32           C
ANISOU 6254  CA  ASN C 252     4714   5501   5863   -681   1439   -638       C
ATOM   6255  C   ASN C 252      18.510  29.791  -1.504  1.00 38.66           C
ANISOU 6255  C   ASN C 252     4347   5017   5323   -668   1348   -615       C
ATOM   6256  O   ASN C 252      17.715  30.037  -2.417  1.00 38.34           O
ANISOU 6256  O   ASN C 252     4452   4898   5217   -659   1370   -594       O
ATOM   6257  CB  ASN C 252      20.668  30.545  -2.610  1.00 38.65           C
ANISOU 6257  CB  ASN C 252     4288   4979   5419   -751   1563   -669       C
ATOM   6258  CG  ASN C 252      20.613  31.937  -1.933  1.00 40.83           C
ANISOU 6258  CG  ASN C 252     4547   5266   5701   -827   1550   -703       C
ATOM   6259  OD1 ASN C 252      20.202  32.106  -0.775  1.00 39.85           O
ANISOU 6259  OD1 ASN C 252     4364   5202   5577   -831   1451   -707       O
ATOM   6260  ND2 ASN C 252      21.081  32.932  -2.665  1.00 48.54           N
ANISOU 6260  ND2 ASN C 252     5578   6183   6683   -889   1658   -727       N
ATOM   6261  N   ILE C 253      18.125  29.707  -0.240  1.00 37.58           N
ANISOU 6261  N   ILE C 253     4135   4951   5194   -660   1242   -616       N
ATOM   6262  CA  ILE C 253      16.796  30.213   0.071  1.00 38.66           C
ANISOU 6262  CA  ILE C 253     4357   5066   5264   -656   1169   -598       C
ATOM   6263  C   ILE C 253      16.854  31.302   1.139  1.00 34.78           C
ANISOU 6263  C   ILE C 253     3808   4615   4793   -714   1134   -630       C
ATOM   6264  O   ILE C 253      15.838  31.629   1.731  1.00 40.82           O
ANISOU 6264  O   ILE C 253     4610   5383   5516   -707   1059   -618       O
ATOM   6265  CB  ILE C 253      15.810  29.077   0.433  1.00 35.23           C
ANISOU 6265  CB  ILE C 253     3939   4655   4792   -583   1068   -558       C
ATOM   6266  CG1 ILE C 253      16.227  28.339   1.697  1.00 31.41           C
ANISOU 6266  CG1 ILE C 253     3314   4266   4355   -561    993   -564       C
ATOM   6267  CG2 ILE C 253      15.649  28.114  -0.745  1.00 33.74           C
ANISOU 6267  CG2 ILE C 253     3835   4412   4572   -532   1106   -527       C
ATOM   6268  CD1 ILE C 253      15.380  27.130   2.011  1.00 34.28           C
ANISOU 6268  CD1 ILE C 253     3691   4649   4685   -490    907   -526       C
ATOM   6269  N   SER C 254      18.020  31.916   1.359  1.00 38.02           N
ANISOU 6269  N   SER C 254     4130   5051   5266   -775   1192   -671       N
ATOM   6270  CA  SER C 254      18.112  32.992   2.345  1.00 33.12           C
ANISOU 6270  CA  SER C 254     3461   4463   4661   -837   1163   -704       C
ATOM   6271  C   SER C 254      17.306  34.194   1.883  1.00 34.53           C
ANISOU 6271  C   SER C 254     3774   4566   4782   -871   1193   -704       C
ATOM   6272  O   SER C 254      17.308  34.544   0.704  1.00 35.44           O
ANISOU 6272  O   SER C 254     3990   4604   4873   -881   1278   -699       O
ATOM   6273  CB  SER C 254      19.559  33.429   2.592  1.00 35.40           C
ANISOU 6273  CB  SER C 254     3630   4791   5030   -901   1224   -750       C
ATOM   6274  OG  SER C 254      20.036  34.347   1.627  1.00 41.80           O
ANISOU 6274  OG  SER C 254     4503   5534   5846   -959   1340   -772       O
ATOM   6275  N   MET C 255      16.597  34.835   2.799  1.00 33.91           N
ANISOU 6275  N   MET C 255     3703   4503   4676   -886   1123   -707       N
ATOM   6276  CA  MET C 255      15.697  35.885   2.360  1.00 35.00           C
ANISOU 6276  CA  MET C 255     3976   4568   4755   -905   1144   -701       C
ATOM   6277  C   MET C 255      16.309  37.249   2.645  1.00 41.00           C
ANISOU 6277  C   MET C 255     4724   5317   5537   -992   1198   -745       C
ATOM   6278  O   MET C 255      17.125  37.408   3.558  1.00 40.33           O
ANISOU 6278  O   MET C 255     4522   5298   5506  -1036   1182   -779       O
ATOM   6279  CB  MET C 255      14.337  35.812   3.035  1.00 33.94           C
ANISOU 6279  CB  MET C 255     3885   4443   4569   -861   1042   -672       C
ATOM   6280  CG  MET C 255      13.567  34.463   2.866  1.00 31.72           C
ANISOU 6280  CG  MET C 255     3618   4173   4261   -777    976   -626       C
ATOM   6281  SD  MET C 255      11.885  34.515   3.485  1.00 31.38           S
ANISOU 6281  SD  MET C 255     3640   4126   4157   -732    873   -592       S
ATOM   6282  CE  MET C 255      11.983  34.695   5.255  1.00 35.28           C
ANISOU 6282  CE  MET C 255     4020   4706   4680   -753    793   -614       C
ATOM   6283  N   ASN C 256      15.914  38.237   1.840  1.00 39.92           N
ANISOU 6283  N   ASN C 256     4715   5096   5356  -1018   1263   -746       N
ATOM   6284  CA  ASN C 256      16.144  39.636   2.160  1.00 39.59           C
ANISOU 6284  CA  ASN C 256     4695   5032   5316  -1096   1304   -782       C
ATOM   6285  C   ASN C 256      14.851  40.125   2.805  1.00 39.99           C
ANISOU 6285  C   ASN C 256     4813   5072   5309  -1072   1226   -763       C
ATOM   6286  O   ASN C 256      13.781  40.068   2.180  1.00 37.40           O
ANISOU 6286  O   ASN C 256     4598   4689   4922  -1021   1212   -725       O
ATOM   6287  CB  ASN C 256      16.521  40.433   0.908  1.00 38.71           C
ANISOU 6287  CB  ASN C 256     4687   4830   5190  -1137   1428   -794       C
ATOM   6288  CG  ASN C 256      16.755  41.931   1.184  1.00 42.42           C
ANISOU 6288  CG  ASN C 256     5192   5268   5657  -1221   1478   -832       C
ATOM   6289  OD1 ASN C 256      16.844  42.362   2.341  1.00 44.15           O
ANISOU 6289  OD1 ASN C 256     5340   5538   5895  -1258   1427   -856       O
ATOM   6290  ND2 ASN C 256      16.911  42.720   0.110  1.00 45.45           N
ANISOU 6290  ND2 ASN C 256     5689   5563   6016  -1255   1584   -839       N
ATOM   6291  N   ILE C 257      14.938  40.567   4.058  1.00 44.19           N
ANISOU 6291  N   ILE C 257     5273   5657   5859  -1107   1174   -787       N
ATOM   6292  CA  ILE C 257      13.760  40.958   4.812  1.00 40.12           C
ANISOU 6292  CA  ILE C 257     4807   5140   5296  -1083   1099   -770       C
ATOM   6293  C   ILE C 257      13.654  42.476   4.941  1.00 43.51           C
ANISOU 6293  C   ILE C 257     5312   5518   5702  -1147   1146   -796       C
ATOM   6294  O   ILE C 257      12.916  42.982   5.784  1.00 45.33           O
ANISOU 6294  O   ILE C 257     5565   5755   5904  -1145   1092   -794       O
ATOM   6295  CB  ILE C 257      13.750  40.293   6.195  1.00 34.66           C
ANISOU 6295  CB  ILE C 257     3999   4540   4629  -1066    998   -772       C
ATOM   6296  CG1 ILE C 257      15.056  40.550   6.942  1.00 31.53           C
ANISOU 6296  CG1 ILE C 257     3482   4204   4296  -1138   1010   -822       C
ATOM   6297  CG2 ILE C 257      13.450  38.825   6.078  1.00 33.88           C
ANISOU 6297  CG2 ILE C 257     3861   4478   4534   -987    941   -735       C
ATOM   6298  CD1 ILE C 257      14.959  40.242   8.412  1.00 31.30           C
ANISOU 6298  CD1 ILE C 257     3363   4253   4278  -1133    910   -829       C
ATOM   6299  N   GLN C 258      14.298  43.209   4.047  1.00 36.42           N
ANISOU 6299  N   GLN C 258     4468   4562   4809  -1200   1250   -818       N
ATOM   6300  CA  GLN C 258      14.325  44.664   4.170  1.00 42.99           C
ANISOU 6300  CA  GLN C 258     5370   5343   5621  -1268   1303   -848       C
ATOM   6301  C   GLN C 258      12.958  45.266   3.843  1.00 44.49           C
ANISOU 6301  C   GLN C 258     5706   5462   5736  -1223   1290   -814       C
ATOM   6302  O   GLN C 258      12.626  46.373   4.310  1.00 43.47           O
ANISOU 6302  O   GLN C 258     5633   5302   5580  -1259   1299   -829       O
ATOM   6303  CB  GLN C 258      15.448  45.218   3.290  1.00 38.41           C
ANISOU 6303  CB  GLN C 258     4804   4719   5070  -1338   1423   -881       C
ATOM   6304  CG  GLN C 258      15.820  46.630   3.534  1.00 40.68           C
ANISOU 6304  CG  GLN C 258     5132   4969   5355  -1427   1485   -923       C
ATOM   6305  CD  GLN C 258      15.847  47.017   4.984  1.00 40.34           C
ANISOU 6305  CD  GLN C 258     5015   4987   5326  -1465   1415   -949       C
ATOM   6306  OE1 GLN C 258      15.181  47.976   5.366  1.00 42.09           O
ANISOU 6306  OE1 GLN C 258     5320   5169   5503  -1480   1410   -952       O
ATOM   6307  NE2 GLN C 258      16.632  46.311   5.798  1.00 36.63           N
ANISOU 6307  NE2 GLN C 258     4392   4609   4917  -1481   1365   -970       N
ATOM   6308  N   LYS C 259      12.175  44.571   3.010  1.00 42.84           N
ANISOU 6308  N   LYS C 259     5563   5221   5492  -1146   1271   -768       N
ATOM   6309  CA  LYS C 259      10.859  45.068   2.629  1.00 41.10           C
ANISOU 6309  CA  LYS C 259     5476   4936   5204  -1097   1253   -732       C
ATOM   6310  C   LYS C 259       9.970  45.271   3.844  1.00 46.45           C
ANISOU 6310  C   LYS C 259     6134   5650   5867  -1075   1167   -724       C
ATOM   6311  O   LYS C 259       9.295  46.301   3.960  1.00 49.72           O
ANISOU 6311  O   LYS C 259     6637   6014   6240  -1080   1177   -721       O
ATOM   6312  CB  LYS C 259      10.197  44.119   1.635  1.00 40.36           C
ANISOU 6312  CB  LYS C 259     5437   4817   5082  -1018   1231   -686       C
ATOM   6313  CG  LYS C 259       8.768  44.509   1.304  1.00 40.32           C
ANISOU 6313  CG  LYS C 259     5554   4755   5011   -960   1195   -646       C
ATOM   6314  CD  LYS C 259       8.205  43.635   0.184  1.00 41.86           C
ANISOU 6314  CD  LYS C 259     5812   4917   5175   -892   1179   -603       C
ATOM   6315  CE  LYS C 259       6.801  44.104  -0.207  1.00 39.82           C
ANISOU 6315  CE  LYS C 259     5676   4599   4854   -835   1143   -564       C
ATOM   6316  NZ  LYS C 259       6.223  43.354  -1.381  1.00 33.68           N
ANISOU 6316  NZ  LYS C 259     4976   3782   4040   -774   1127   -523       N
ATOM   6317  N   ILE C 260       9.908  44.295   4.755  1.00 42.64           N
ANISOU 6317  N   ILE C 260     5540   5250   5412  -1046   1082   -717       N
ATOM   6318  CA  ILE C 260       9.005  44.532   5.884  1.00 42.87           C
ANISOU 6318  CA  ILE C 260     5562   5305   5422  -1024   1008   -707       C
ATOM   6319  C   ILE C 260       9.755  45.208   7.017  1.00 45.51           C
ANISOU 6319  C   ILE C 260     5829   5679   5785  -1099   1011   -755       C
ATOM   6320  O   ILE C 260       9.122  45.723   7.956  1.00 44.75           O
ANISOU 6320  O   ILE C 260     5747   5590   5668  -1098    970   -756       O
ATOM   6321  CB  ILE C 260       8.263  43.289   6.426  1.00 46.36           C
ANISOU 6321  CB  ILE C 260     5942   5806   5866   -951    908   -672       C
ATOM   6322  CG1 ILE C 260       9.104  42.299   7.173  1.00 47.51           C
ANISOU 6322  CG1 ILE C 260     5950   6040   6063   -960    866   -689       C
ATOM   6323  CG2 ILE C 260       7.935  42.375   5.279  1.00 48.73           C
ANISOU 6323  CG2 ILE C 260     6279   6082   6153   -892    908   -635       C
ATOM   6324  CD1 ILE C 260       8.184  41.263   7.798  1.00 56.72           C
ANISOU 6324  CD1 ILE C 260     7079   7252   7220   -889    770   -653       C
ATOM   6325  N   GLU C 261      11.088  45.170   6.991  1.00 45.08           N
ANISOU 6325  N   GLU C 261     5697   5653   5779  -1164   1056   -794       N
ATOM   6326  CA  GLU C 261      11.838  45.934   7.976  1.00 46.10           C
ANISOU 6326  CA  GLU C 261     5770   5812   5932  -1245   1063   -842       C
ATOM   6327  C   GLU C 261      11.537  47.417   7.814  1.00 44.53           C
ANISOU 6327  C   GLU C 261     5690   5536   5695  -1290   1126   -858       C
ATOM   6328  O   GLU C 261      11.469  48.155   8.803  1.00 35.58           O
ANISOU 6328  O   GLU C 261     4555   4411   4552  -1330   1108   -882       O
ATOM   6329  CB  GLU C 261      13.337  45.660   7.830  1.00 41.14           C
ANISOU 6329  CB  GLU C 261     5038   5224   5369  -1307   1107   -881       C
ATOM   6330  CG  GLU C 261      14.192  46.331   8.897  1.00 41.93           C
ANISOU 6330  CG  GLU C 261     5063   5366   5501  -1394   1102   -933       C
ATOM   6331  CD  GLU C 261      14.479  45.434  10.092  1.00 43.20           C
ANISOU 6331  CD  GLU C 261     5091   5627   5697  -1380   1005   -939       C
ATOM   6332  OE1 GLU C 261      15.025  45.948  11.109  1.00 42.20           O
ANISOU 6332  OE1 GLU C 261     4909   5538   5588  -1445    981   -978       O
ATOM   6333  OE2 GLU C 261      14.158  44.217  10.009  1.00 44.18           O
ANISOU 6333  OE2 GLU C 261     5172   5787   5826  -1305    950   -904       O
ATOM   6334  N   LYS C 262      11.285  47.846   6.575  1.00 49.30           N
ANISOU 6334  N   LYS C 262     6406   6058   6268  -1278   1198   -842       N
ATOM   6335  CA  LYS C 262      10.873  49.220   6.319  1.00 50.21           C
ANISOU 6335  CA  LYS C 262     6651   6090   6338  -1307   1258   -850       C
ATOM   6336  C   LYS C 262       9.534  49.547   6.981  1.00 49.21           C
ANISOU 6336  C   LYS C 262     6584   5950   6163  -1253   1196   -821       C
ATOM   6337  O   LYS C 262       9.229  50.731   7.189  1.00 54.94           O
ANISOU 6337  O   LYS C 262     7397   6623   6856  -1283   1232   -833       O
ATOM   6338  CB  LYS C 262      10.820  49.485   4.808  1.00 53.26           C
ANISOU 6338  CB  LYS C 262     7149   6390   6695  -1294   1341   -833       C
ATOM   6339  N   HIS C 263       8.687  48.539   7.236  1.00 45.46           N
ANISOU 6339  N   HIS C 263     6074   5516   5684  -1171   1111   -780       N
ATOM   6340  CA  HIS C 263       7.408  48.729   7.923  1.00 44.09           C
ANISOU 6340  CA  HIS C 263     5941   5337   5473  -1116   1049   -752       C
ATOM   6341  C   HIS C 263       7.503  48.565   9.434  1.00 43.75           C
ANISOU 6341  C   HIS C 263     5806   5366   5449  -1136    985   -771       C
ATOM   6342  O   HIS C 263       6.486  48.696  10.122  1.00 43.12           O
ANISOU 6342  O   HIS C 263     5753   5287   5343  -1093    936   -750       O
ATOM   6343  CB  HIS C 263       6.360  47.727   7.408  1.00 44.42           C
ANISOU 6343  CB  HIS C 263     5996   5383   5498  -1018    991   -696       C
ATOM   6344  CG  HIS C 263       5.852  48.006   6.027  1.00 41.88           C
ANISOU 6344  CG  HIS C 263     5792   4980   5139   -981   1036   -667       C
ATOM   6345  ND1 HIS C 263       4.739  48.782   5.787  1.00 41.90           N
ANISOU 6345  ND1 HIS C 263     5908   4919   5095   -939   1039   -640       N
ATOM   6346  CD2 HIS C 263       6.281  47.584   4.815  1.00 42.83           C
ANISOU 6346  CD2 HIS C 263     5939   5072   5262   -975   1078   -659       C
ATOM   6347  CE1 HIS C 263       4.516  48.844   4.485  1.00 41.05           C
ANISOU 6347  CE1 HIS C 263     5891   4748   4959   -911   1076   -617       C
ATOM   6348  NE2 HIS C 263       5.433  48.122   3.872  1.00 41.78           N
ANISOU 6348  NE2 HIS C 263     5937   4859   5078   -933   1102   -628       N
ATOM   6349  N   GLY C 264       8.697  48.341   9.971  1.00 43.04           N
ANISOU 6349  N   GLY C 264     5614   5334   5404  -1201    985   -812       N
ATOM   6350  CA  GLY C 264       8.896  48.172  11.405  1.00 46.40           C
ANISOU 6350  CA  GLY C 264     5954   5829   5847  -1224    920   -834       C
ATOM   6351  C   GLY C 264       8.844  46.745  11.934  1.00 42.10           C
ANISOU 6351  C   GLY C 264     5301   5366   5329  -1172    833   -814       C
ATOM   6352  O   GLY C 264       8.801  46.549  13.160  1.00 36.28           O
ANISOU 6352  O   GLY C 264     4507   4682   4596  -1177    771   -824       O
ATOM   6353  N   ILE C 265       8.851  45.738  11.070  1.00 41.90           N
ANISOU 6353  N   ILE C 265     5250   5350   5318  -1122    828   -786       N
ATOM   6354  CA  ILE C 265       8.900  44.361  11.532  1.00 42.16           C
ANISOU 6354  CA  ILE C 265     5182   5459   5378  -1076    752   -769       C
ATOM   6355  C   ILE C 265      10.345  43.900  11.446  1.00 42.85           C
ANISOU 6355  C   ILE C 265     5165   5595   5520  -1126    770   -802       C
ATOM   6356  O   ILE C 265      10.930  43.818  10.356  1.00 39.92           O
ANISOU 6356  O   ILE C 265     4803   5197   5167  -1138    833   -805       O
ATOM   6357  CB  ILE C 265       7.967  43.439  10.734  1.00 42.03           C
ANISOU 6357  CB  ILE C 265     5199   5426   5344   -989    727   -716       C
ATOM   6358  CG1 ILE C 265       6.562  44.038  10.690  1.00 41.10           C
ANISOU 6358  CG1 ILE C 265     5187   5253   5177   -944    718   -684       C
ATOM   6359  CG2 ILE C 265       7.908  42.067  11.414  1.00 37.76           C
ANISOU 6359  CG2 ILE C 265     4561   4962   4825   -942    644   -699       C
ATOM   6360  CD1 ILE C 265       5.493  43.149  10.054  1.00 37.18           C
ANISOU 6360  CD1 ILE C 265     4720   4745   4662   -857    678   -632       C
ATOM   6361  N   HIS C 266      10.915  43.588  12.597  1.00 35.21           N
ANISOU 6361  N   HIS C 266     4099   4699   4580  -1151    715   -826       N
ATOM   6362  CA  HIS C 266      12.301  43.198  12.688  1.00 36.86           C
ANISOU 6362  CA  HIS C 266     4197   4963   4846  -1199    723   -860       C
ATOM   6363  C   HIS C 266      12.392  41.740  13.096  1.00 38.39           C
ANISOU 6363  C   HIS C 266     4293   5230   5064  -1140    647   -839       C
ATOM   6364  O   HIS C 266      11.614  41.272  13.934  1.00 35.54           O
ANISOU 6364  O   HIS C 266     3928   4896   4679  -1093    572   -817       O
ATOM   6365  CB  HIS C 266      13.042  44.047  13.702  1.00 37.05           C
ANISOU 6365  CB  HIS C 266     4180   5014   4885  -1284    717   -911       C
ATOM   6366  CG  HIS C 266      14.299  43.414  14.199  1.00 39.65           C
ANISOU 6366  CG  HIS C 266     4369   5423   5273  -1317    686   -941       C
ATOM   6367  ND1 HIS C 266      15.483  43.463  13.497  1.00 41.74           N
ANISOU 6367  ND1 HIS C 266     4576   5694   5590  -1367    748   -969       N
ATOM   6368  CD2 HIS C 266      14.563  42.721  15.334  1.00 42.40           C
ANISOU 6368  CD2 HIS C 266     4623   5848   5638  -1306    598   -947       C
ATOM   6369  CE1 HIS C 266      16.423  42.828  14.176  1.00 42.48           C
ANISOU 6369  CE1 HIS C 266     4540   5867   5734  -1383    698   -990       C
ATOM   6370  NE2 HIS C 266      15.892  42.370  15.297  1.00 42.11           N
ANISOU 6370  NE2 HIS C 266     4471   5865   5664  -1346    604   -978       N
ATOM   6371  N   PHE C 267      13.371  41.043  12.517  1.00 36.65           N
ANISOU 6371  N   PHE C 267     3996   5038   4892  -1143    670   -846       N
ATOM   6372  CA  PHE C 267      13.715  39.691  12.897  1.00 34.28           C
ANISOU 6372  CA  PHE C 267     3594   4810   4622  -1096    606   -833       C
ATOM   6373  C   PHE C 267      15.206  39.627  13.198  1.00 36.81           C
ANISOU 6373  C   PHE C 267     3793   5186   5006  -1154    615   -875       C
ATOM   6374  O   PHE C 267      16.010  40.318  12.573  1.00 39.00           O
ANISOU 6374  O   PHE C 267     4067   5438   5311  -1216    693   -906       O
ATOM   6375  CB  PHE C 267      13.366  38.690  11.786  1.00 36.06           C
ANISOU 6375  CB  PHE C 267     3844   5013   4845  -1025    624   -791       C
ATOM   6376  CG  PHE C 267      11.912  38.264  11.762  1.00 33.16           C
ANISOU 6376  CG  PHE C 267     3554   4619   4424   -951    579   -744       C
ATOM   6377  CD1 PHE C 267      11.418  37.380  12.710  1.00 32.89           C
ANISOU 6377  CD1 PHE C 267     3476   4637   4382   -901    491   -724       C
ATOM   6378  CD2 PHE C 267      11.069  38.687  10.753  1.00 28.77           C
ANISOU 6378  CD2 PHE C 267     3113   3988   3831   -930    624   -719       C
ATOM   6379  CE1 PHE C 267      10.096  36.963  12.681  1.00 33.64           C
ANISOU 6379  CE1 PHE C 267     3636   4710   4435   -836    452   -681       C
ATOM   6380  CE2 PHE C 267       9.745  38.275  10.717  1.00 34.06           C
ANISOU 6380  CE2 PHE C 267     3844   4637   4458   -863    579   -675       C
ATOM   6381  CZ  PHE C 267       9.255  37.409  11.672  1.00 32.36           C
ANISOU 6381  CZ  PHE C 267     3581   4476   4240   -818    495   -657       C
ATOM   6382  N   SER C 268      15.573  38.780  14.152  1.00 36.05           N
ANISOU 6382  N   SER C 268     3597   5168   4933  -1132    535   -878       N
ATOM   6383  CA  SER C 268      16.979  38.505  14.386  1.00 40.64           C
ANISOU 6383  CA  SER C 268     4049   5810   5580  -1172    533   -912       C
ATOM   6384  C   SER C 268      17.584  37.718  13.232  1.00 41.93           C
ANISOU 6384  C   SER C 268     4176   5971   5785  -1142    590   -898       C
ATOM   6385  O   SER C 268      16.891  37.065  12.450  1.00 31.54           O
ANISOU 6385  O   SER C 268     2920   4620   4444  -1076    604   -857       O
ATOM   6386  CB  SER C 268      17.178  37.676  15.656  1.00 41.80           C
ANISOU 6386  CB  SER C 268     4103   6040   5738  -1143    428   -912       C
ATOM   6387  OG  SER C 268      17.092  38.434  16.834  1.00 46.28           O
ANISOU 6387  OG  SER C 268     4673   6625   6284  -1192    378   -939       O
ATOM   6388  N   ASN C 269      18.911  37.777  13.142  1.00 44.55           N
ANISOU 6388  N   ASN C 269     4405   6338   6183  -1192    622   -934       N
ATOM   6389  CA  ASN C 269      19.597  36.849  12.262  1.00 41.94           C
ANISOU 6389  CA  ASN C 269     4016   6019   5899  -1156    665   -921       C
ATOM   6390  C   ASN C 269      19.534  35.461  12.893  1.00 40.72           C
ANISOU 6390  C   ASN C 269     3788   5931   5752  -1076    575   -894       C
ATOM   6391  O   ASN C 269      19.255  35.317  14.089  1.00 43.63           O
ANISOU 6391  O   ASN C 269     4128   6346   6103  -1067    483   -895       O
ATOM   6392  CB  ASN C 269      21.045  37.290  12.039  1.00 40.90           C
ANISOU 6392  CB  ASN C 269     3785   5911   5843  -1231    726   -968       C
ATOM   6393  CG  ASN C 269      21.926  37.088  13.275  1.00 43.93           C
ANISOU 6393  CG  ASN C 269     4028   6387   6274  -1258    645   -999       C
ATOM   6394  OD1 ASN C 269      21.971  36.011  13.876  1.00 45.54           O
ANISOU 6394  OD1 ASN C 269     4163   6652   6488  -1195    565   -979       O
ATOM   6395  ND2 ASN C 269      22.635  38.134  13.653  1.00 50.90           N
ANISOU 6395  ND2 ASN C 269     4873   7281   7187  -1354    665  -1048       N
ATOM   6396  N   THR C 270      19.875  34.446  12.103  1.00 33.63           N
ANISOU 6396  N   THR C 270     2859   5037   4882  -1022    605   -871       N
ATOM   6397  CA  THR C 270      19.653  33.060  12.518  1.00 43.20           C
ANISOU 6397  CA  THR C 270     4028   6296   6091   -936    529   -837       C
ATOM   6398  C   THR C 270      20.341  32.722  13.840  1.00 41.79           C
ANISOU 6398  C   THR C 270     3726   6206   5946   -941    440   -858       C
ATOM   6399  O   THR C 270      19.725  32.138  14.742  1.00 35.70           O
ANISOU 6399  O   THR C 270     2959   5467   5141   -894    350   -838       O
ATOM   6400  CB  THR C 270      20.146  32.114  11.417  1.00 43.33           C
ANISOU 6400  CB  THR C 270     4022   6301   6140   -888    590   -817       C
ATOM   6401  OG1 THR C 270      19.261  32.174  10.278  1.00 43.96           O
ANISOU 6401  OG1 THR C 270     4233   6298   6171   -863    649   -787       O
ATOM   6402  CG2 THR C 270      20.291  30.699  11.957  1.00 32.59           C
ANISOU 6402  CG2 THR C 270     2587   5002   4794   -810    515   -792       C
ATOM   6403  N   VAL C 271      21.636  33.031  13.942  1.00 42.29           N
ANISOU 6403  N   VAL C 271     3679   6311   6079   -996    463   -898       N
ATOM   6404  CA  VAL C 271      22.410  32.681  15.127  1.00 42.64           C
ANISOU 6404  CA  VAL C 271     3597   6443   6161  -1001    375   -919       C
ATOM   6405  C   VAL C 271      21.994  33.557  16.306  1.00 46.40           C
ANISOU 6405  C   VAL C 271     4100   6932   6599  -1052    307   -942       C
ATOM   6406  O   VAL C 271      21.724  33.058  17.405  1.00 45.17           O
ANISOU 6406  O   VAL C 271     3921   6823   6419  -1018    208   -933       O
ATOM   6407  CB  VAL C 271      23.923  32.791  14.840  1.00 40.73           C
ANISOU 6407  CB  VAL C 271     3223   6241   6010  -1048    422   -956       C
ATOM   6408  CG1 VAL C 271      24.700  32.748  16.123  1.00 41.03           C
ANISOU 6408  CG1 VAL C 271     3138   6366   6085  -1072    328   -985       C
ATOM   6409  CG2 VAL C 271      24.372  31.693  13.927  1.00 36.59           C
ANISOU 6409  CG2 VAL C 271     2658   5719   5527   -981    471   -929       C
ATOM   6410  N   ASP C 272      21.914  34.877  16.088  1.00 47.31           N
ANISOU 6410  N   ASP C 272     4273   7000   6702  -1135    363   -971       N
ATOM   6411  CA  ASP C 272      21.520  35.769  17.174  1.00 46.01           C
ANISOU 6411  CA  ASP C 272     4144   6841   6498  -1187    307   -995       C
ATOM   6412  C   ASP C 272      20.149  35.384  17.725  1.00 48.13           C
ANISOU 6412  C   ASP C 272     4507   7091   6689  -1122    243   -955       C
ATOM   6413  O   ASP C 272      19.967  35.290  18.946  1.00 49.49           O
ANISOU 6413  O   ASP C 272     4663   7305   6837  -1118    154   -960       O
ATOM   6414  CB  ASP C 272      21.510  37.222  16.692  1.00 46.72           C
ANISOU 6414  CB  ASP C 272     4304   6868   6578  -1277    390  -1026       C
ATOM   6415  CG  ASP C 272      22.890  37.873  16.728  1.00 58.75           C
ANISOU 6415  CG  ASP C 272     5723   8425   8174  -1369    423  -1080       C
ATOM   6416  OD1 ASP C 272      23.807  37.299  17.366  1.00 58.81           O
ANISOU 6416  OD1 ASP C 272     5599   8511   8234  -1367    362  -1096       O
ATOM   6417  OD2 ASP C 272      23.050  38.972  16.130  1.00 50.95           O
ANISOU 6417  OD2 ASP C 272     4786   7384   7191  -1444    509  -1107       O
ATOM   6418  N   GLY C 273      19.189  35.098  16.842  1.00 44.09           N
ANISOU 6418  N   GLY C 273     4093   6519   6139  -1068    287   -915       N
ATOM   6419  CA  GLY C 273      17.859  34.735  17.311  1.00 46.58           C
ANISOU 6419  CA  GLY C 273     4494   6816   6387  -1009    233   -878       C
ATOM   6420  C   GLY C 273      17.828  33.435  18.101  1.00 45.01           C
ANISOU 6420  C   GLY C 273     4235   6678   6187   -936    142   -854       C
ATOM   6421  O   GLY C 273      17.141  33.346  19.122  1.00 42.20           O
ANISOU 6421  O   GLY C 273     3909   6337   5788   -917     70   -845       O
ATOM   6422  N   PHE C 274      18.578  32.413  17.651  1.00 44.74           N
ANISOU 6422  N   PHE C 274     4120   6679   6201   -894    147   -843       N
ATOM   6423  CA  PHE C 274      18.636  31.168  18.415  1.00 45.16           C
ANISOU 6423  CA  PHE C 274     4115   6791   6254   -824     62   -822       C
ATOM   6424  C   PHE C 274      19.170  31.468  19.797  1.00 46.51           C
ANISOU 6424  C   PHE C 274     4217   7023   6430   -861    -21   -854       C
ATOM   6425  O   PHE C 274      18.556  31.158  20.823  1.00 48.66           O
ANISOU 6425  O   PHE C 274     4516   7314   6658   -832    -99   -841       O
ATOM   6426  CB  PHE C 274      19.558  30.117  17.746  1.00 46.06           C
ANISOU 6426  CB  PHE C 274     4139   6935   6425   -779     85   -811       C
ATOM   6427  CG  PHE C 274      19.715  28.837  18.573  1.00 44.84           C
ANISOU 6427  CG  PHE C 274     3922   6843   6273   -706     -4   -790       C
ATOM   6428  CD1 PHE C 274      20.669  28.762  19.584  1.00 41.75           C
ANISOU 6428  CD1 PHE C 274     3421   6525   5916   -723    -73   -818       C
ATOM   6429  CD2 PHE C 274      18.904  27.723  18.350  1.00 41.01           C
ANISOU 6429  CD2 PHE C 274     3490   6340   5752   -622    -21   -743       C
ATOM   6430  CE1 PHE C 274      20.781  27.655  20.390  1.00 39.35           C
ANISOU 6430  CE1 PHE C 274     3070   6274   5608   -656   -158   -799       C
ATOM   6431  CE2 PHE C 274      19.017  26.601  19.154  1.00 39.50           C
ANISOU 6431  CE2 PHE C 274     3251   6200   5556   -557   -100   -725       C
ATOM   6432  CZ  PHE C 274      19.982  26.575  20.179  1.00 44.74           C
ANISOU 6432  CZ  PHE C 274     3810   6937   6254   -572   -169   -752       C
ATOM   6433  N   SER C 275      20.314  32.113  19.820  1.00 43.51           N
ANISOU 6433  N   SER C 275     3755   6673   6106   -931     -2   -897       N
ATOM   6434  CA  SER C 275      21.063  32.270  21.044  1.00 50.67           C
ANISOU 6434  CA  SER C 275     4575   7647   7031   -966    -85   -930       C
ATOM   6435  C   SER C 275      20.283  33.063  22.085  1.00 49.47           C
ANISOU 6435  C   SER C 275     4502   7480   6814  -1002   -135   -942       C
ATOM   6436  O   SER C 275      20.384  32.760  23.279  1.00 49.59           O
ANISOU 6436  O   SER C 275     4485   7544   6811   -991   -229   -947       O
ATOM   6437  CB  SER C 275      22.426  32.899  20.731  1.00 43.74           C
ANISOU 6437  CB  SER C 275     3593   6798   6230  -1043    -44   -977       C
ATOM   6438  OG  SER C 275      23.210  33.073  21.896  1.00 52.23           O
ANISOU 6438  OG  SER C 275     4578   7942   7326  -1082   -129  -1012       O
ATOM   6439  N   LYS C 276      19.508  34.065  21.666  1.00 51.20           N
ANISOU 6439  N   LYS C 276     4828   7630   6996  -1042    -74   -944       N
ATOM   6440  CA  LYS C 276      18.688  34.798  22.621  1.00 50.03           C
ANISOU 6440  CA  LYS C 276     4764   7462   6785  -1069   -113   -952       C
ATOM   6441  C   LYS C 276      17.593  33.891  23.135  1.00 51.80           C
ANISOU 6441  C   LYS C 276     5045   7682   6953   -984   -169   -907       C
ATOM   6442  O   LYS C 276      17.259  33.912  24.318  1.00 53.26           O
ANISOU 6442  O   LYS C 276     5250   7888   7099   -982   -242   -910       O
ATOM   6443  CB  LYS C 276      18.016  36.009  21.966  1.00 47.80           C
ANISOU 6443  CB  LYS C 276     4589   7100   6473  -1118    -29   -958       C
ATOM   6444  CG  LYS C 276      18.864  37.243  21.650  1.00 51.68           C
ANISOU 6444  CG  LYS C 276     5060   7577   7000  -1221     30  -1008       C
ATOM   6445  CD  LYS C 276      17.947  38.328  21.024  1.00 53.12           C
ANISOU 6445  CD  LYS C 276     5374   7671   7138  -1250    110  -1004       C
ATOM   6446  CE  LYS C 276      18.586  38.970  19.789  1.00 44.79           C
ANISOU 6446  CE  LYS C 276     4315   6578   6126  -1303    214  -1024       C
ATOM   6447  NZ  LYS C 276      17.616  39.754  18.982  1.00 40.58           N
ANISOU 6447  NZ  LYS C 276     3914   5955   5548  -1305    292  -1007       N
ATOM   6448  N   MET C 277      17.058  33.055  22.248  1.00 49.25           N
ANISOU 6448  N   MET C 277     4749   7334   6629   -914   -135   -865       N
ATOM   6449  CA  MET C 277      16.032  32.079  22.587  1.00 50.83           C
ANISOU 6449  CA  MET C 277     5000   7530   6784   -831   -180   -820       C
ATOM   6450  C   MET C 277      16.536  31.003  23.538  1.00 50.96           C
ANISOU 6450  C   MET C 277     4939   7616   6808   -785   -271   -814       C
ATOM   6451  O   MET C 277      15.809  30.582  24.442  1.00 49.96           O
ANISOU 6451  O   MET C 277     4854   7496   6633   -747   -331   -795       O
ATOM   6452  CB  MET C 277      15.548  31.450  21.282  1.00 53.18           C
ANISOU 6452  CB  MET C 277     5333   7786   7088   -777   -118   -782       C
ATOM   6453  CG  MET C 277      14.541  30.329  21.360  1.00 48.50           C
ANISOU 6453  CG  MET C 277     4786   7184   6456   -692   -152   -733       C
ATOM   6454  SD  MET C 277      15.330  28.757  21.735  1.00 43.82           S
ANISOU 6454  SD  MET C 277     4093   6661   5894   -623   -215   -718       S
ATOM   6455  CE  MET C 277      16.395  28.572  20.345  1.00 50.45           C
ANISOU 6455  CE  MET C 277     4867   7499   6801   -630   -137   -726       C
ATOM   6456  N   TYR C 278      17.764  30.520  23.327  1.00 53.59           N
ANISOU 6456  N   TYR C 278     5160   8000   7201   -784   -278   -829       N
ATOM   6457  CA  TYR C 278      18.277  29.399  24.111  1.00 52.45           C
ANISOU 6457  CA  TYR C 278     4941   7921   7068   -728   -362   -819       C
ATOM   6458  C   TYR C 278      18.450  29.758  25.577  1.00 57.68           C
ANISOU 6458  C   TYR C 278     5590   8623   7702   -759   -452   -844       C
ATOM   6459  O   TYR C 278      18.017  29.009  26.460  1.00 62.30           O
ANISOU 6459  O   TYR C 278     6196   9228   8246   -705   -523   -823       O
ATOM   6460  CB  TYR C 278      19.616  28.941  23.538  1.00 51.74           C
ANISOU 6460  CB  TYR C 278     4728   7877   7055   -725   -345   -832       C
ATOM   6461  CG  TYR C 278      20.111  27.603  24.028  1.00 54.71           C
ANISOU 6461  CG  TYR C 278     5029   8311   7447   -648   -416   -812       C
ATOM   6462  CD1 TYR C 278      19.297  26.476  24.000  1.00 51.91           C
ANISOU 6462  CD1 TYR C 278     4729   7941   7054   -561   -433   -765       C
ATOM   6463  CD2 TYR C 278      21.413  27.466  24.509  1.00 57.61           C
ANISOU 6463  CD2 TYR C 278     5271   8749   7870   -663   -465   -840       C
ATOM   6464  CE1 TYR C 278      19.767  25.250  24.439  1.00 55.98           C
ANISOU 6464  CE1 TYR C 278     5182   8507   7581   -489   -494   -746       C
ATOM   6465  CE2 TYR C 278      21.898  26.240  24.950  1.00 57.19           C
ANISOU 6465  CE2 TYR C 278     5148   8749   7831   -587   -530   -821       C
ATOM   6466  CZ  TYR C 278      21.074  25.141  24.916  1.00 60.32           C
ANISOU 6466  CZ  TYR C 278     5608   9126   8185   -500   -543   -774       C
ATOM   6467  OH  TYR C 278      21.568  23.934  25.359  1.00 64.00           O
ANISOU 6467  OH  TYR C 278     6012   9641   8663   -424   -605   -754       O
ATOM   6468  N   LYS C 279      19.103  30.890  25.857  1.00 58.46           N
ANISOU 6468  N   LYS C 279     5659   8733   7820   -847   -449   -891       N
ATOM   6469  CA  LYS C 279      19.385  31.276  27.230  1.00 57.23           C
ANISOU 646