CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 210518162001103422

Job options:

ID        	=	 210518162001103422
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -200
DQMAX     	=	 200
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 5
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (1.19.2_4158: ???)
REMARK   3   AUTHORS     : Adams,Afonine,Bunkoczi,Burnley,Chen,Dar,Davis,
REMARK   3               : Draizen,Echols,Gildea,Gros,Grosse-Kunstleve,Headd,
REMARK   3               : Hintze,Hung,Ioerger,Liebschner,McCoy,McKee,Moriarty,
REMARK   3               : Oeffner,Poon,Read,Richardson,Richardson,Sacchettini,
REMARK   3               : Sauter,Sobolev,Storoni,Terwilliger,Williams,Zwart
REMARK   3
REMARK   3  X-RAY DATA.
REMARK   3  
REMARK   3  REFINEMENT TARGET : ML
REMARK   3  
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19    
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.14   
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.97  
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.05 
REMARK   3   NUMBER OF REFLECTIONS             : 197066    
REMARK   3   NUMBER OF REFLECTIONS (NON-ANOMALOUS) : 197066    
REMARK   3  
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2072
REMARK   3   R VALUE            (WORKING SET) : 0.2052
REMARK   3   FREE R VALUE                     : 0.2462
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.98  
REMARK   3   FREE R VALUE TEST SET COUNT      : 9805      
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   70.14 -    6.80    0.99     6364   318  0.1692 0.1819   0.920  0.914
REMARK   3     2    6.80 -    5.40    0.98     6295   335  0.1850 0.2254   0.896  0.856
REMARK   3     3    5.40 -    4.72    0.99     6306   369  0.1725 0.1962   0.910  0.884
REMARK   3     4    4.72 -    4.29    0.98     6371   282  0.1621 0.2034   0.917  0.865
REMARK   3     5    4.29 -    3.98    0.97     6227   359  0.1702 0.2005   0.909  0.870
REMARK   3     6    3.98 -    3.74    0.97     6277   303  0.1824 0.2277   0.902  0.830
REMARK   3     7    3.74 -    3.56    0.98     6299   341  0.1895 0.2394   0.896  0.832
REMARK   3     8    3.56 -    3.40    0.98     6240   327  0.2030 0.2428   0.875  0.816
REMARK   3     9    3.40 -    3.27    0.98     6301   311  0.2296 0.2681   0.857  0.791
REMARK   3    10    3.27 -    3.16    0.98     6298   301  0.2221 0.2618   0.853  0.787
REMARK   3    11    3.16 -    3.06    0.97     6302   334  0.2183 0.2769   0.856  0.763
REMARK   3    12    3.06 -    2.97    0.97     6233   338  0.2245 0.2946   0.863  0.768
REMARK   3    13    2.97 -    2.89    0.97     6190   326  0.2277 0.2859   0.864  0.777
REMARK   3    14    2.89 -    2.82    0.98     6278   340  0.2352 0.2791   0.861  0.781
REMARK   3    15    2.82 -    2.76    0.98     6290   340  0.2439 0.2919   0.836  0.751
REMARK   3    16    2.76 -    2.70    0.97     6188   333  0.2336 0.2707   0.855  0.785
REMARK   3    17    2.70 -    2.65    0.96     6153   351  0.2521 0.3094   0.817  0.707
REMARK   3    18    2.65 -    2.60    0.97     6272   341  0.2349 0.3028   0.831  0.694
REMARK   3    19    2.60 -    2.55    0.97     6298   344  0.2335 0.2839   0.833  0.761
REMARK   3    20    2.55 -    2.51    0.97     6243   293  0.2360 0.2939   0.822  0.719
REMARK   3    21    2.51 -    2.47    0.97     6227   331  0.2396 0.2946   0.809  0.723
REMARK   3    22    2.47 -    2.43    0.97     6264   318  0.2506 0.3070   0.793  0.729
REMARK   3    23    2.43 -    2.39    0.96     6196   285  0.2597 0.3123   0.772  0.676
REMARK   3    24    2.39 -    2.36    0.96     6175   320  0.2610 0.2938   0.769  0.702
REMARK   3    25    2.36 -    2.33    0.96     6205   319  0.2683 0.3067   0.748  0.687
REMARK   3    26    2.33 -    2.30    0.96     6194   315  0.2753 0.3370   0.759  0.622
REMARK   3    27    2.30 -    2.27    0.96     6167   323  0.2889 0.3454   0.709  0.567
REMARK   3    28    2.27 -    2.24    0.95     6066   341  0.3104 0.3498   0.642  0.547
REMARK   3    29    2.24 -    2.21    0.96     6150   328  0.3129 0.3493   0.631  0.565
REMARK   3    30    2.21 -    2.19    0.97     6192   339  0.2868 0.3331   0.682  0.596
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)     : 0.33    
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.15   
REMARK   3  
REMARK   3  STRUCTURE FACTORS CALCULATION ALGORITHM : FFT
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 42.34   
REMARK   3  
REMARK   3  GEOMETRY RESTRAINTS LIBRARY: GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3    BOND      :  0.010   0.242  26183
REMARK   3    ANGLE     :  1.407  45.717  35613
REMARK   3    CHIRALITY :  0.071   0.715   3938
REMARK   3    PLANARITY :  0.013   0.485   4656
REMARK   3    DIHEDRAL  :  7.643  98.437   3477
REMARK   3    MIN NONBONDED DISTANCE : 2.037
REMARK   3  
REMARK   3  MOLPROBITY STATISTICS.
REMARK   3    ALL-ATOM CLASHSCORE : 7.80
REMARK   3    RAMACHANDRAN PLOT:
REMARK   3      OUTLIERS :  0.19 %
REMARK   3      ALLOWED  :  3.38 %
REMARK   3      FAVORED  : 96.43 %
REMARK   3    ROTAMER OUTLIERS :  2.33 %
REMARK   3    CBETA DEVIATIONS :  0.26 %
REMARK   3    PEPTIDE PLANE:
REMARK   3      CIS-PROLINE     : 13.85 %
REMARK   3      CIS-GENERAL     : 0.20 %
REMARK   3      TWISTED PROLINE : 0.00 %
REMARK   3      TWISTED GENERAL : 0.44 %
REMARK   3  
REMARK   3  RAMA-Z (RAMACHANDRAN PLOT Z-SCORE):
REMARK   3  INTERPRETATION: BAD |RAMA-Z| > 3; SUSPICIOUS 2 < |RAMA-Z| < 3; GOOD |RAMA-Z| < 2.
REMARK   3  SCORES FOR WHOLE/HELIX/SHEET/LOOP ARE SCALED INDEPENDENTLY;
REMARK   3  THEREFORE, THE VALUES ARE NOT RELATED IN A SIMPLE MANNER.
REMARK   3    WHOLE: -0.98 (0.14), RESIDUES: 3202
REMARK   3    HELIX: -1.16 (0.15), RESIDUES: 885
REMARK   3    SHEET: -1.15 (0.20), RESIDUES: 508
REMARK   3    LOOP : -0.07 (0.15), RESIDUES: 1809
REMARK   3  
REMARK   3                  min    max   mean    iso aniso
REMARK   3     Overall:   22.61 142.48  55.89   3.60 26317 25558
REMARK   3     Protein:   22.61 142.48  56.12   3.60 25558 25558
REMARK   3     Water:     25.68 103.18  47.98    N/A   741     0
REMARK   3     Other:     40.37  78.56  49.96    N/A    18     0
REMARK   3     Chain  A:  27.60 121.19  59.03    N/A  4249  4249
REMARK   3     Chain  C:  23.38 104.73  47.17    N/A  4265  4265
REMARK   3     Chain  B:  26.84 132.74  56.01    N/A  4249  4249
REMARK   3     Chain  E:  25.29 118.51  56.33    N/A  4246  4246
REMARK   3     Chain  D:  22.61 126.49  55.26    N/A  4311  4311
REMARK   3     Chain  G:  42.23  78.56  59.93    N/A     5     0
REMARK   3     Chain  F:  25.16 142.48  63.01    N/A  4238  4238
REMARK   3     Chain  I:  40.37  54.41  46.43    N/A    12     0
REMARK   3     Chain  H:  42.53  42.53  42.53    N/A     1     0
REMARK   3     Chain  S:  25.68 103.18  47.98    N/A   741     0
REMARK   3     Histogram:
REMARK   3         Values      Number of atoms
REMARK   3      22.61 - 34.59      2567
REMARK   3      34.59 - 46.58      7510
REMARK   3      46.58 - 58.57      6032
REMARK   3      58.57 - 70.56      4585
REMARK   3      70.56 - 82.54      3047
REMARK   3      82.54 - 94.53      1501
REMARK   3      94.53 - 106.52      716
REMARK   3     106.52 - 118.50      258
REMARK   3     118.50 - 130.49       83
REMARK   3     130.49 - 142.48       18
REMARK   3  
REMARK   3  
REMARK   3  TLS DETAILS.
REMARK   3   NUMBER OF TLS GROUPS: 6     
REMARK   3   ORIGIN: CENTER OF MASS
REMARK   3   TLS GROUP : 1     
REMARK   3    SELECTION: (chain A and resseq 3:667)
REMARK   3    ORIGIN FOR THE GROUP (A):   5.5199  -6.4865  43.9849
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.6175 T22:   0.3439                       
REMARK   3      T33:   0.3556 T12:  -0.1411                       
REMARK   3      T13:  -0.0125 T23:  -0.0163                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.9031 L22:   0.8927                       
REMARK   3      L33:   0.7992 L12:  -0.0629                       
REMARK   3      L13:   0.1196 L23:  -0.0323                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0199 S12:   0.1208 S13:  -0.4243         
REMARK   3      S21:  -0.1616 S22:  -0.0113 S23:   0.2040         
REMARK   3      S31:   0.4008 S32:  -0.2778 S33:  -0.0117         
REMARK   3   TLS GROUP : 2     
REMARK   3    SELECTION: (chain B and resseq 3:667)
REMARK   3    ORIGIN FOR THE GROUP (A):  48.8330  10.5304  13.1855
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.5324 T22:   0.3355                       
REMARK   3      T33:   0.3041 T12:   0.0482                       
REMARK   3      T13:   0.0498 T23:  -0.0358                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.6858 L22:   0.9300                       
REMARK   3      L33:   1.0666 L12:  -0.0427                       
REMARK   3      L13:   0.0297 L23:   0.0861                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0212 S12:   0.2828 S13:  -0.2844         
REMARK   3      S21:  -0.1674 S22:  -0.0016 S23:  -0.2162         
REMARK   3      S31:   0.3684 S32:   0.1824 S33:  -0.0290         
REMARK   3   TLS GROUP : 3     
REMARK   3    SELECTION: (chain C and resseq 2:667)
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1564  51.4429  66.1793
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2226 T22:   0.3244                       
REMARK   3      T33:   0.3291 T12:  -0.0118                       
REMARK   3      T13:   0.0115 T23:  -0.0829                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.7224 L22:   0.9845                       
REMARK   3      L33:   0.9144 L12:  -0.6230                       
REMARK   3      L13:  -0.0802 L23:   0.2220                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0141 S12:  -0.3415 S13:   0.2648         
REMARK   3      S21:   0.0654 S22:   0.0223 S23:   0.1214         
REMARK   3      S31:  -0.0641 S32:  -0.1885 S33:  -0.0067         
REMARK   3   TLS GROUP : 4     
REMARK   3    SELECTION: (chain D and resseq 3:667)
REMARK   3    ORIGIN FOR THE GROUP (A):  46.1973  60.2112  50.9824
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.2486 T22:   0.2465                       
REMARK   3      T33:   0.6811 T12:  -0.0153                       
REMARK   3      T13:   0.0157 T23:  -0.0645                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   2.5316 L22:   0.7615                       
REMARK   3      L33:   0.8519 L12:   0.0622                       
REMARK   3      L13:   0.3778 L23:   0.0266                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0262 S12:  -0.0544 S13:   0.9054         
REMARK   3      S21:   0.0250 S22:  -0.0103 S23:  -0.2288         
REMARK   3      S31:  -0.1345 S32:   0.1804 S33:   0.0165         
REMARK   3   TLS GROUP : 5     
REMARK   3    SELECTION: (chain E and resseq 2:667)
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9912   2.8292  73.0531
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.4360 T22:   0.3257                       
REMARK   3      T33:   0.2909 T12:   0.0282                       
REMARK   3      T13:  -0.0001 T23:   0.0726                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.2013 L22:   1.2104                       
REMARK   3      L33:   1.7086 L12:  -0.0951                       
REMARK   3      L13:  -0.0058 L23:  -0.6370                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:  -0.0764 S12:  -0.3025 S13:  -0.1833         
REMARK   3      S21:   0.1746 S22:  -0.0868 S23:  -0.2482         
REMARK   3      S31:   0.2594 S32:   0.3363 S33:   0.1429         
REMARK   3   TLS GROUP : 6     
REMARK   3    SELECTION: (chain F and resseq 2:667)
REMARK   3    ORIGIN FOR THE GROUP (A):  20.5747  40.5417   5.7432
REMARK   3    T TENSOR                                            
REMARK   3      T11:   0.4021 T22:   0.5791                       
REMARK   3      T33:   0.2828 T12:   0.0303                       
REMARK   3      T13:  -0.0269 T23:   0.1478                       
REMARK   3    L TENSOR                                            
REMARK   3      L11:   1.1396 L22:   1.1447                       
REMARK   3      L33:   2.1857 L12:   0.1434                       
REMARK   3      L13:  -0.2390 L23:  -0.5410                       
REMARK   3    S TENSOR                                            
REMARK   3      S11:   0.0007 S12:   0.4432 S13:   0.2455         
REMARK   3      S21:  -0.3051 S22:   0.2103 S23:   0.2399         
REMARK   3      S31:  -0.0856 S32:  -0.6841 S33:  -0.1773         
REMARK   3
LINK        ZN    ZN G   1                 SG  CYS B 603 
LINK        ZN    ZN G   1                 SG  CYS B 628 
LINK        ZN    ZN G   1                 SG  CYS B 606 
LINK        ZN    ZN G   1                 SG  CYS B 631 
LINK        ZN    ZN G   2                 SG  CYS C 603 
LINK        ZN    ZN G   2                 SG  CYS C 606 
LINK        ZN    ZN G   2                 SG  CYS C 628 
LINK        ZN    ZN G   2                 SG  CYS C 631 
LINK        ZN    ZN G   3                 SG  CYS A 603 
LINK        ZN    ZN G   3                 SG  CYS A 606 
LINK        ZN    ZN G   3                 SG  CYS A 631 
LINK        ZN    ZN G   3                 SG  CYS A 628 
LINK        ZN    ZN G   4                 SG  CYS F 606 
LINK        ZN    ZN G   4                 SG  CYS F 603 
LINK        ZN    ZN G   4                 SG  CYS F 631 
LINK        ZN    ZN G   4                 SG  CYS F 628 
LINK        ZN    ZN G   5                 SG  CYS E 603 
LINK        ZN    ZN G   5                 SG  CYS E 606 
LINK        ZN    ZN G   5                 SG  CYS E 628 
LINK        ZN    ZN G   5                 SG  CYS E 631 
LINK        ZN    ZN H   1                 SG  CYS D 603 
LINK        ZN    ZN H   1                 SG  CYS D 606 
LINK        ZN    ZN H   1                 SG  CYS D 631 
LINK        ZN    ZN H   1                 SG  CYS D 628 
CRYST1   98.230  108.300  111.420 117.72 101.32  91.80 P 1
SCALE1      0.010180  0.000320  0.002500        0.00000
SCALE2      0.000000  0.009238  0.005067        0.00000
SCALE3      0.000000  0.000000  0.010440        0.00000
ATOM      1  N   LYS A   3      16.449 -26.211  47.595  1.00 79.97           N
ANISOU    1  N   LYS A   3    12949   5932  11505  -1107     -1     32       N
ATOM      2  CA  LYS A   3      15.158 -26.184  48.268  1.00 78.41           C
ANISOU    2  CA  LYS A   3    12702   5780  11310  -1263    -16    163       C
ATOM      3  C   LYS A   3      14.181 -25.429  47.376  1.00 75.97           C
ANISOU    3  C   LYS A   3    12403   5600  10862  -1359    -36      7       C
ATOM      4  O   LYS A   3      14.258 -24.202  47.250  1.00 64.86           O
ANISOU    4  O   LYS A   3    10980   4410   9254  -1322    -16     -9       O
ATOM      5  CB  LYS A   3      15.288 -25.507  49.619  1.00 83.62           C
ANISOU    5  CB  LYS A   3    13331   6572  11867  -1253     14    408       C
ATOM      6  CG  LYS A   3      14.422 -26.026  50.739  1.00 81.02           C
ANISOU    6  CG  LYS A   3    12935   6222  11627  -1367     13    619       C
ATOM      7  CD  LYS A   3      14.863 -25.202  51.940  1.00 86.20           C
ANISOU    7  CD  LYS A   3    13572   7042  12139  -1315     46    823       C
ATOM      8  CE  LYS A   3      13.911 -25.168  53.120  1.00 86.34           C
ANISOU    8  CE  LYS A   3    13518   7150  12138  -1427     60   1036       C
ATOM      9  NZ  LYS A   3      14.341 -26.063  54.222  1.00 87.64           N
ANISOU    9  NZ  LYS A   3    13646   7222  12433  -1393     72   1249       N
ATOM     10  N   VAL A   4      13.273 -26.162  46.743  1.00 74.23           N
ANISOU   10  N   VAL A   4    12164   5285  10756  -1466    -78   -108       N
ATOM     11  CA  VAL A   4      12.373 -25.592  45.749  1.00 70.23           C
ANISOU   11  CA  VAL A   4    11662   4888  10135  -1553   -110   -281       C
ATOM     12  C   VAL A   4      10.939 -25.865  46.187  1.00 65.37           C
ANISOU   12  C   VAL A   4    10977   4275   9586  -1727   -139   -195       C
ATOM     13  O   VAL A   4      10.650 -26.860  46.855  1.00 67.10           O
ANISOU   13  O   VAL A   4    11152   4350   9993  -1781   -142    -77       O
ATOM     14  CB  VAL A   4      12.677 -26.163  44.338  1.00 69.93           C
ANISOU   14  CB  VAL A   4    11662   4759  10150  -1507   -140   -550       C
ATOM     15  CG1 VAL A   4      11.491 -26.015  43.382  1.00 69.35           C
ANISOU   15  CG1 VAL A   4    11570   4754  10024  -1630   -193   -717       C
ATOM     16  CG2 VAL A   4      13.897 -25.478  43.747  1.00 70.72           C
ANISOU   16  CG2 VAL A   4    11823   4939  10107  -1350   -103   -652       C
ATOM     17  N   TYR A   5      10.035 -24.966  45.820  1.00 70.48           N
ANISOU   17  N   TYR A   5    11599   5096  10083  -1811   -157   -248       N
ATOM     18  CA  TYR A   5       8.643 -25.045  46.238  1.00 68.40           C
ANISOU   18  CA  TYR A   5    11264   4866   9859  -1979   -180   -165       C
ATOM     19  C   TYR A   5       7.745 -25.254  45.027  1.00 70.06           C
ANISOU   19  C   TYR A   5    11463   5071  10086  -2074   -245   -382       C
ATOM     20  O   TYR A   5       7.909 -24.585  44.000  1.00 70.49           O
ANISOU   20  O   TYR A   5    11535   5252   9995  -2017   -262   -556       O
ATOM     21  CB  TYR A   5       8.253 -23.783  47.008  1.00 62.85           C
ANISOU   21  CB  TYR A   5    10481   4426   8974  -1978   -143    -17       C
ATOM     22  CG  TYR A   5       9.288 -23.387  48.036  1.00 59.37           C
ANISOU   22  CG  TYR A   5    10050   4034   8473  -1858    -85    155       C
ATOM     23  CD1 TYR A   5       9.373 -24.067  49.253  1.00 57.43           C
ANISOU   23  CD1 TYR A   5     9799   3678   8343  -1889    -60    368       C
ATOM     24  CD2 TYR A   5      10.157 -22.318  47.813  1.00 57.80           C
ANISOU   24  CD2 TYR A   5     9860   4001   8102  -1718    -58    113       C
ATOM     25  CE1 TYR A   5      10.305 -23.710  50.209  1.00 59.96           C
ANISOU   25  CE1 TYR A   5    10124   4056   8601  -1780    -15    525       C
ATOM     26  CE2 TYR A   5      11.094 -21.951  48.769  1.00 56.66           C
ANISOU   26  CE2 TYR A   5     9717   3905   7906  -1613    -12    264       C
ATOM     27  CZ  TYR A   5      11.160 -22.653  49.970  1.00 60.24           C
ANISOU   27  CZ  TYR A   5    10167   4254   8468  -1643      7    467       C
ATOM     28  OH  TYR A   5      12.083 -22.311  50.933  1.00 60.18           O
ANISOU   28  OH  TYR A   5    10158   4303   8403  -1540     45    616       O
ATOM     29  N   LYS A   6       6.831 -26.220  45.138  1.00 67.74           N
ANISOU   29  N   LYS A   6    11105   4658   9973  -2195   -278   -368       N
ATOM     30  CA  LYS A   6       5.823 -26.457  44.112  1.00 71.35           C
ANISOU   30  CA  LYS A   6    11529   5122  10459  -2303   -347   -556       C
ATOM     31  C   LYS A   6       4.640 -25.505  44.216  1.00 69.68           C
ANISOU   31  C   LYS A   6    11255   5109  10113  -2423   -365   -513       C
ATOM     32  O   LYS A   6       3.864 -25.396  43.261  1.00 73.17           O
ANISOU   32  O   LYS A   6    11670   5610  10520  -2496   -428   -681       O
ATOM     33  CB  LYS A   6       5.308 -27.897  44.193  1.00 63.35           C
ANISOU   33  CB  LYS A   6    10464   3892   9716  -2389   -374   -563       C
ATOM     34  CG  LYS A   6       6.379 -28.959  44.044  1.00 77.14           C
ANISOU   34  CG  LYS A   6    12258   5419  11631  -2280   -361   -618       C
ATOM     35  CD  LYS A   6       7.003 -28.947  42.645  1.00 83.65           C
ANISOU   35  CD  LYS A   6    13149   6242  12392  -2187   -395   -898       C
ATOM     36  CE  LYS A   6       8.205 -29.893  42.550  1.00 84.35           C
ANISOU   36  CE  LYS A   6    13283   6128  12637  -2059   -371   -949       C
ATOM     37  NZ  LYS A   6       9.275 -29.356  41.637  1.00 84.54           N
ANISOU   37  NZ  LYS A   6    13385   6232  12503  -1908   -361  -1123       N
ATOM     38  N   ASP A   7       4.482 -24.824  45.343  1.00 67.87           N
ANISOU   38  N   ASP A   7    10984   4999   9807  -2435   -313   -298       N
ATOM     39  CA  ASP A   7       3.295 -24.009  45.577  1.00 67.58           C
ANISOU   39  CA  ASP A   7    10837   5169   9669  -2530   -319   -238       C
ATOM     40  C   ASP A   7       3.541 -23.122  46.793  1.00 63.74           C
ANISOU   40  C   ASP A   7    10306   4848   9064  -2467   -244    -22       C
ATOM     41  O   ASP A   7       4.580 -23.209  47.453  1.00 62.47           O
ANISOU   41  O   ASP A   7    10197   4634   8905  -2364   -195     84       O
ATOM     42  CB  ASP A   7       2.056 -24.887  45.775  1.00 67.61           C
ANISOU   42  CB  ASP A   7    10778   5057   9852  -2721   -357   -203       C
ATOM     43  CG  ASP A   7       2.169 -25.800  46.991  1.00 70.11           C
ANISOU   43  CG  ASP A   7    11060   5236  10342  -2737   -304     12       C
ATOM     44  OD1 ASP A   7       3.138 -25.657  47.773  1.00 67.77           O
ANISOU   44  OD1 ASP A   7    10809   4931  10008  -2631   -246    149       O
ATOM     45  OD2 ASP A   7       1.292 -26.684  47.162  1.00 73.35           O
ANISOU   45  OD2 ASP A   7    11392   5547  10930  -2855   -321     46       O
ATOM     46  N   LEU A   8       2.536 -22.300  47.101  1.00 63.95           N
ANISOU   46  N   LEU A   8    10229   5074   8994  -2534   -238     39       N
ATOM     47  CA  LEU A   8       2.570 -21.440  48.276  1.00 60.86           C
ANISOU   47  CA  LEU A   8     9780   4855   8491  -2492   -169    230       C
ATOM     48  C   LEU A   8       2.653 -22.252  49.562  1.00 62.64           C
ANISOU   48  C   LEU A   8    10003   4958   8840  -2541   -121    447       C
ATOM     49  O   LEU A   8       3.382 -21.886  50.496  1.00 61.02           O
ANISOU   49  O   LEU A   8     9809   4813   8563  -2450    -63    590       O
ATOM     50  CB  LEU A   8       1.322 -20.556  48.286  1.00 58.02           C
ANISOU   50  CB  LEU A   8     9301   4708   8037  -2571   -178    235       C
ATOM     51  CG  LEU A   8       1.167 -19.649  49.510  1.00 61.60           C
ANISOU   51  CG  LEU A   8     9679   5352   8376  -2542   -106    416       C
ATOM     52  CD1 LEU A   8       2.290 -18.603  49.558  1.00 50.72           C
ANISOU   52  CD1 LEU A   8     8343   4094   6833  -2367    -74    403       C
ATOM     53  CD2 LEU A   8      -0.209 -19.001  49.502  1.00 58.25           C
ANISOU   53  CD2 LEU A   8     9126   5103   7903  -2640   -117    415       C
ATOM     54  N   ARG A   9       1.897 -23.350  49.635  1.00 62.08           N
ANISOU   54  N   ARG A   9     9911   4720   8955  -2689   -146    478       N
ATOM     55  CA  ARG A   9       1.815 -24.108  50.880  1.00 63.06           C
ANISOU   55  CA  ARG A   9    10019   4742   9198  -2754    -99    709       C
ATOM     56  C   ARG A   9       3.168 -24.673  51.282  1.00 63.53           C
ANISOU   56  C   ARG A   9    10161   4662   9314  -2619    -71    777       C
ATOM     57  O   ARG A   9       3.551 -24.595  52.453  1.00 61.76           O
ANISOU   57  O   ARG A   9     9921   4491   9056  -2575    -13    979       O
ATOM     58  CB  ARG A   9       0.780 -25.220  50.742  1.00 62.18           C
ANISOU   58  CB  ARG A   9     9830   4499   9296  -2894   -127    704       C
ATOM     59  CG  ARG A   9      -0.610 -24.673  50.595  1.00 66.37           C
ANISOU   59  CG  ARG A   9    10256   5184   9778  -3033   -146    683       C
ATOM     60  CD  ARG A   9      -1.618 -25.768  50.428  1.00 65.59           C
ANISOU   60  CD  ARG A   9    10073   4955   9892  -3168   -174    670       C
ATOM     61  NE  ARG A   9      -2.882 -25.223  49.958  1.00 70.27           N
ANISOU   61  NE  ARG A   9    10572   5690  10438  -3291   -214    590       N
ATOM     62  CZ  ARG A   9      -4.072 -25.716  50.270  1.00 72.81           C
ANISOU   62  CZ  ARG A   9    10772   6011  10883  -3431   -210    658       C
ATOM     63  NH1 ARG A   9      -4.196 -26.777  51.049  1.00 74.53           N
ANISOU   63  NH1 ARG A   9    10950   6090  11277  -3472   -161    809       N
ATOM     64  NH2 ARG A   9      -5.166 -25.135  49.781  1.00 75.26           N
ANISOU   64  NH2 ARG A   9    10993   6463  11140  -3531   -253    575       N
ATOM     65  N   GLU A  10       3.915 -25.240  50.328  1.00 64.44           N
ANISOU   65  N   GLU A  10    10358   4614   9511  -2546   -113    607       N
ATOM     66  CA  GLU A  10       5.262 -25.698  50.650  1.00 63.63           C
ANISOU   66  CA  GLU A  10    10327   4392   9457  -2405    -88    660       C
ATOM     67  C   GLU A  10       6.117 -24.557  51.185  1.00 61.97           C
ANISOU   67  C   GLU A  10    10159   4347   9041  -2289    -45    737       C
ATOM     68  O   GLU A  10       6.897 -24.752  52.123  1.00 63.91           O
ANISOU   68  O   GLU A  10    10414   4573   9297  -2207     -5    900       O
ATOM     69  CB  GLU A  10       5.913 -26.345  49.429  1.00 62.89           C
ANISOU   69  CB  GLU A  10    10308   4124   9462  -2338   -135    436       C
ATOM     70  CG  GLU A  10       5.266 -27.679  49.049  1.00 63.11           C
ANISOU   70  CG  GLU A  10    10294   3949   9733  -2434   -171    373       C
ATOM     71  CD  GLU A  10       5.857 -28.286  47.795  1.00 68.22           C
ANISOU   71  CD  GLU A  10    11008   4443  10470  -2369   -218    127       C
ATOM     72  OE1 GLU A  10       6.736 -27.649  47.177  1.00 72.38           O
ANISOU   72  OE1 GLU A  10    11611   5031  10857  -2251   -221      5       O
ATOM     73  OE2 GLU A  10       5.422 -29.404  47.416  1.00 87.35           O
ANISOU   73  OE2 GLU A  10    13401   6686  13101  -2437   -246     50       O
ATOM     74  N   PHE A  11       5.968 -23.349  50.625  1.00 61.31           N
ANISOU   74  N   PHE A  11    10053   4473   8770  -2248    -49    620       N
ATOM     75  CA  PHE A  11       6.752 -22.223  51.129  1.00 59.75           C
ANISOU   75  CA  PHE A  11     9849   4467   8386  -2112     -5    678       C
ATOM     76  C   PHE A  11       6.335 -21.843  52.543  1.00 58.42           C
ANISOU   76  C   PHE A  11     9605   4438   8153  -2150     48    904       C
ATOM     77  O   PHE A  11       7.191 -21.559  53.390  1.00 57.98           O
ANISOU   77  O   PHE A  11     9565   4435   8030  -2052     86   1027       O
ATOM     78  CB  PHE A  11       6.635 -21.012  50.204  1.00 55.49           C
ANISOU   78  CB  PHE A  11     9287   4120   7677  -2058    -21    509       C
ATOM     79  CG  PHE A  11       7.525 -19.857  50.606  1.00 52.11           C
ANISOU   79  CG  PHE A  11     8856   3867   7077  -1915     19    548       C
ATOM     80  CD1 PHE A  11       8.859 -20.073  50.886  1.00 52.86           C
ANISOU   80  CD1 PHE A  11     9018   3882   7185  -1791     40    587       C
ATOM     81  CD2 PHE A  11       7.026 -18.570  50.702  1.00 52.44           C
ANISOU   81  CD2 PHE A  11     8824   4144   6959  -1906     33    543       C
ATOM     82  CE1 PHE A  11       9.687 -19.032  51.254  1.00 53.33           C
ANISOU   82  CE1 PHE A  11     9070   4096   7098  -1667     72    619       C
ATOM     83  CE2 PHE A  11       7.846 -17.508  51.057  1.00 52.79           C
ANISOU   83  CE2 PHE A  11     8863   4336   6861  -1780     66    570       C
ATOM     84  CZ  PHE A  11       9.187 -17.739  51.336  1.00 53.55           C
ANISOU   84  CZ  PHE A  11     9026   4352   6968  -1663     84    607       C
ATOM     85  N   LEU A  12       5.026 -21.820  52.811  1.00 58.28           N
ANISOU   85  N   LEU A  12     9502   4492   8151  -2290     50    956       N
ATOM     86  CA  LEU A  12       4.543 -21.444  54.136  1.00 58.95           C
ANISOU   86  CA  LEU A  12     9507   4730   8163  -2330    107   1161       C
ATOM     87  C   LEU A  12       5.013 -22.418  55.215  1.00 60.29           C
ANISOU   87  C   LEU A  12     9707   4762   8438  -2341    138   1374       C
ATOM     88  O   LEU A  12       5.274 -21.994  56.349  1.00 62.64           O
ANISOU   88  O   LEU A  12     9975   5195   8630  -2297    188   1539       O
ATOM     89  CB  LEU A  12       3.018 -21.331  54.137  1.00 57.52           C
ANISOU   89  CB  LEU A  12     9220   4639   7995  -2485    106   1168       C
ATOM     90  CG  LEU A  12       2.356 -20.244  53.285  1.00 56.07           C
ANISOU   90  CG  LEU A  12     8978   4633   7692  -2484     80    999       C
ATOM     91  CD1 LEU A  12       0.873 -20.124  53.614  1.00 53.52           C
ANISOU   91  CD1 LEU A  12     8534   4421   7382  -2630     92   1056       C
ATOM     92  CD2 LEU A  12       3.050 -18.899  53.486  1.00 58.35           C
ANISOU   92  CD2 LEU A  12     9264   5124   7782  -2336    109    978       C
ATOM     93  N   GLU A  13       5.112 -23.726  54.902  1.00 56.67           N
ANISOU   93  N   GLU A  13     9285   4058   8188  -2378    109   1368       N
ATOM     94  CA  GLU A  13       5.636 -24.671  55.900  1.00 62.08           C
ANISOU   94  CA  GLU A  13     9957   4642   8986  -2334    142   1559       C
ATOM     95  C   GLU A  13       7.023 -24.258  56.336  1.00 59.86           C
ANISOU   95  C   GLU A  13     9742   4400   8604  -2173    158   1610       C
ATOM     96  O   GLU A  13       7.336 -24.233  57.526  1.00 63.14           O
ANISOU   96  O   GLU A  13    10123   4900   8965  -2130    201   1804       O
ATOM     97  CB  GLU A  13       5.800 -26.101  55.384  1.00 65.18           C
ANISOU   97  CB  GLU A  13    10375   4761   9630  -2346    113   1509       C
ATOM     98  CG  GLU A  13       5.037 -26.635  54.236  1.00 69.09           C
ANISOU   98  CG  GLU A  13    10865   5126  10260  -2445     61   1324       C
ATOM     99  CD  GLU A  13       5.092 -28.156  54.266  1.00 79.94           C
ANISOU   99  CD  GLU A  13    12234   6245  11894  -2468     63   1360       C
ATOM    100  OE1 GLU A  13       6.034 -28.704  54.903  1.00 84.22           O
ANISOU  100  OE1 GLU A  13    12807   6694  12497  -2370     94   1482       O
ATOM    101  OE2 GLU A  13       4.237 -28.805  53.635  1.00 87.15           O
ANISOU  101  OE2 GLU A  13    13114   7046  12951  -2580     34   1259       O
ATOM    102  N   VAL A  14       7.888 -24.016  55.352  1.00 58.65           N
ANISOU  102  N   VAL A  14     9678   4175   8433  -2079    121   1432       N
ATOM    103  CA  VAL A  14       9.267 -23.636  55.614  1.00 60.64           C
ANISOU  103  CA  VAL A  14     9991   4449   8602  -1921    131   1455       C
ATOM    104  C   VAL A  14       9.324 -22.365  56.458  1.00 61.16           C
ANISOU  104  C   VAL A  14    10019   4775   8443  -1883    170   1547       C
ATOM    105  O   VAL A  14      10.124 -22.266  57.397  1.00 64.01           O
ANISOU  105  O   VAL A  14    10386   5187   8747  -1798    193   1690       O
ATOM    106  CB  VAL A  14      10.018 -23.492  54.278  1.00 62.35           C
ANISOU  106  CB  VAL A  14    10299   4567   8824  -1839     93   1223       C
ATOM    107  CG1 VAL A  14      11.369 -22.833  54.470  1.00 62.16           C
ANISOU  107  CG1 VAL A  14    10306   4626   8686  -1667    110   1222       C
ATOM    108  CG2 VAL A  14      10.164 -24.863  53.619  1.00 63.54           C
ANISOU  108  CG2 VAL A  14    10472   4463   9208  -1844     60   1141       C
ATOM    109  N   LEU A  15       8.472 -21.378  56.149  1.00 60.91           N
ANISOU  109  N   LEU A  15     9921   4935   8286  -1927    178   1454       N
ATOM    110  CA  LEU A  15       8.427 -20.149  56.944  1.00 57.33           C
ANISOU  110  CA  LEU A  15     9403   4749   7633  -1880    218   1516       C
ATOM    111  C   LEU A  15       8.020 -20.446  58.382  1.00 60.96           C
ANISOU  111  C   LEU A  15     9811   5277   8075  -1944    262   1756       C
ATOM    112  O   LEU A  15       8.553 -19.845  59.326  1.00 58.11           O
ANISOU  112  O   LEU A  15     9430   5068   7580  -1866    292   1858       O
ATOM    113  CB  LEU A  15       7.448 -19.157  56.322  1.00 55.37           C
ANISOU  113  CB  LEU A  15     9085   4666   7286  -1929    215   1378       C
ATOM    114  CG  LEU A  15       7.751 -18.537  54.960  1.00 53.12           C
ANISOU  114  CG  LEU A  15     8832   4388   6962  -1862    177   1150       C
ATOM    115  CD1 LEU A  15       6.704 -17.488  54.621  1.00 53.21           C
ANISOU  115  CD1 LEU A  15     8759   4591   6867  -1911    178   1065       C
ATOM    116  CD2 LEU A  15       9.140 -17.930  54.930  1.00 49.62           C
ANISOU  116  CD2 LEU A  15     8439   3984   6432  -1698    182   1113       C
ATOM    117  N   GLU A  16       7.044 -21.348  58.570  1.00 58.99           N
ANISOU  117  N   GLU A  16     9533   4927   7954  -2090    266   1849       N
ATOM    118  CA  GLU A  16       6.637 -21.711  59.925  1.00 61.01           C
ANISOU  118  CA  GLU A  16     9710   5271   8201  -2130    317   2074       C
ATOM    119  C   GLU A  16       7.761 -22.445  60.643  1.00 63.73           C
ANISOU  119  C   GLU A  16    10087   5525   8603  -2020    323   2211       C
ATOM    120  O   GLU A  16       8.096 -22.114  61.785  1.00 66.89           O
ANISOU  120  O   GLU A  16    10453   6080   8881  -1964    361   2360       O
ATOM    121  CB  GLU A  16       5.355 -22.558  59.905  1.00 60.51           C
ANISOU  121  CB  GLU A  16     9572   5135   8284  -2280    329   2121       C
ATOM    122  CG  GLU A  16       4.790 -22.825  61.316  1.00 63.82           C
ANISOU  122  CG  GLU A  16     9896   5683   8671  -2322    399   2348       C
ATOM    123  CD  GLU A  16       3.284 -23.164  61.347  1.00 78.34           C
ANISOU  123  CD  GLU A  16    11636   7543  10585  -2483    426   2379       C
ATOM    124  OE1 GLU A  16       2.853 -24.140  60.686  1.00 79.33           O
ANISOU  124  OE1 GLU A  16    11766   7465  10911  -2562    398   2329       O
ATOM    125  OE2 GLU A  16       2.531 -22.459  62.061  1.00 80.02           O
ANISOU  125  OE2 GLU A  16    11762   7983  10660  -2528    478   2450       O
ATOM    126  N   GLN A  17       8.383 -23.424  59.970  1.00 62.90           N
ANISOU  126  N   GLN A  17    10046   5174   8680  -1981    285   2153       N
ATOM    127  CA  GLN A  17       9.489 -24.163  60.574  1.00 64.40           C
ANISOU  127  CA  GLN A  17    10265   5260   8943  -1872    289   2277       C
ATOM    128  C   GLN A  17      10.616 -23.240  61.010  1.00 60.86           C
ANISOU  128  C   GLN A  17     9849   4956   8319  -1735    286   2292       C
ATOM    129  O   GLN A  17      11.332 -23.544  61.969  1.00 58.04           O
ANISOU  129  O   GLN A  17     9483   4622   7946  -1655    303   2450       O
ATOM    130  CB  GLN A  17      10.056 -25.174  59.584  1.00 68.30           C
ANISOU  130  CB  GLN A  17    10827   5474   9649  -1837    246   2162       C
ATOM    131  CG  GLN A  17       9.058 -26.101  58.963  1.00 71.40           C
ANISOU  131  CG  GLN A  17    11197   5699  10232  -1965    237   2103       C
ATOM    132  CD  GLN A  17       9.730 -27.079  58.034  1.00 75.75           C
ANISOU  132  CD  GLN A  17    11814   5981  10986  -1913    198   1978       C
ATOM    133  OE1 GLN A  17      10.858 -26.838  57.595  1.00 73.72           O
ANISOU  133  OE1 GLN A  17    11622   5685  10702  -1788    171   1888       O
ATOM    134  NE2 GLN A  17       9.018 -28.144  57.657  1.00 70.55           N
ANISOU  134  NE2 GLN A  17    11138   5140  10528  -2011    196   1950       N
ATOM    135  N   GLU A  18      10.817 -22.134  60.295  1.00 60.71           N
ANISOU  135  N   GLU A  18     9870   5027   8170  -1703    267   2125       N
ATOM    136  CA  GLU A  18      11.954 -21.258  60.524  1.00 61.33           C
ANISOU  136  CA  GLU A  18     9987   5215   8102  -1570    261   2107       C
ATOM    137  C   GLU A  18      11.634 -20.099  61.456  1.00 61.49           C
ANISOU  137  C   GLU A  18     9948   5513   7901  -1574    297   2178       C
ATOM    138  O   GLU A  18      12.448 -19.171  61.569  1.00 59.91           O
ANISOU  138  O   GLU A  18     9747   5447   7571  -1458    295   2118       O
ATOM    139  CB  GLU A  18      12.485 -20.731  59.185  1.00 62.45           C
ANISOU  139  CB  GLU A  18    10188   5301   8238  -1501    231   1869       C
ATOM    140  CG  GLU A  18      13.106 -21.812  58.317  1.00 63.27           C
ANISOU  140  CG  GLU A  18    10375   5128   8536  -1470    195   1795       C
ATOM    141  CD  GLU A  18      14.370 -22.383  58.929  1.00 66.73           C
ANISOU  141  CD  GLU A  18    10830   5492   9035  -1344    188   1908       C
ATOM    142  OE1 GLU A  18      15.398 -21.673  58.923  1.00 78.03           O
ANISOU  142  OE1 GLU A  18    12295   6992  10362  -1227    183   1869       O
ATOM    143  OE2 GLU A  18      14.338 -23.533  59.414  1.00 72.07           O
ANISOU  143  OE2 GLU A  18    11480   6039   9866  -1360    189   2038       O
ATOM    144  N   GLY A  19      10.479 -20.127  62.120  1.00 55.69           N
ANISOU  144  N   GLY A  19     9131   4895   7135  -1683    336   2278       N
ATOM    145  CA  GLY A  19      10.064 -19.005  62.938  1.00 51.99           C
ANISOU  145  CA  GLY A  19     8598   4698   6458  -1691    375   2319       C
ATOM    146  C   GLY A  19       9.628 -17.775  62.161  1.00 55.44           C
ANISOU  146  C   GLY A  19     8993   5272   6798  -1676    376   2107       C
ATOM    147  O   GLY A  19       9.538 -16.694  62.742  1.00 49.38           O
ANISOU  147  O   GLY A  19     8167   4732   5862  -1637    403   2095       O
ATOM    148  N   GLN A  20       9.321 -17.914  60.869  1.00 52.64           N
ANISOU  148  N   GLN A  20     8666   4789   6547  -1708    345   1940       N
ATOM    149  CA  GLN A  20       9.005 -16.776  60.015  1.00 53.63           C
ANISOU  149  CA  GLN A  20     8759   5028   6589  -1683    337   1743       C
ATOM    150  C   GLN A  20       7.541 -16.734  59.603  1.00 53.81           C
ANISOU  150  C   GLN A  20     8716   5086   6642  -1816    345   1693       C
ATOM    151  O   GLN A  20       7.206 -16.098  58.599  1.00 47.90           O
ANISOU  151  O   GLN A  20     7955   4368   5878  -1812    323   1522       O
ATOM    152  CB  GLN A  20       9.888 -16.786  58.764  1.00 49.62           C
ANISOU  152  CB  GLN A  20     8328   4381   6143  -1596    292   1572       C
ATOM    153  CG  GLN A  20      11.335 -16.499  59.056  1.00 51.00           C
ANISOU  153  CG  GLN A  20     8548   4565   6266  -1451    285   1585       C
ATOM    154  CD  GLN A  20      11.538 -15.129  59.663  1.00 50.56           C
ANISOU  154  CD  GLN A  20     8434   4749   6029  -1380    307   1571       C
ATOM    155  OE1 GLN A  20      12.366 -14.959  60.547  1.00 54.29           O
ANISOU  155  OE1 GLN A  20     8907   5287   6433  -1302    313   1664       O
ATOM    156  NE2 GLN A  20      10.780 -14.137  59.182  1.00 48.87           N
ANISOU  156  NE2 GLN A  20     8164   4664   5741  -1405    314   1451       N
ATOM    157  N   LEU A  21       6.663 -17.418  60.327  1.00 53.56           N
ANISOU  157  N   LEU A  21     8640   5052   6660  -1936    376   1845       N
ATOM    158  CA  LEU A  21       5.238 -17.265  60.068  1.00 56.59           C
ANISOU  158  CA  LEU A  21     8940   5504   7059  -2062    389   1808       C
ATOM    159  C   LEU A  21       4.491 -17.293  61.392  1.00 55.16           C
ANISOU  159  C   LEU A  21     8674   5475   6811  -2138    453   1996       C
ATOM    160  O   LEU A  21       4.831 -18.076  62.277  1.00 52.94           O
ANISOU  160  O   LEU A  21     8415   5140   6560  -2153    474   2182       O
ATOM    161  CB  LEU A  21       4.718 -18.351  59.121  1.00 58.88           C
ANISOU  161  CB  LEU A  21     9262   5567   7542  -2169    347   1755       C
ATOM    162  CG  LEU A  21       3.267 -18.183  58.664  1.00 55.49           C
ANISOU  162  CG  LEU A  21     8743   5199   7140  -2298    346   1688       C
ATOM    163  CD1 LEU A  21       3.119 -18.599  57.218  1.00 59.65           C
ANISOU  163  CD1 LEU A  21     9317   5558   7790  -2331    279   1507       C
ATOM    164  CD2 LEU A  21       2.358 -19.013  59.542  1.00 58.03           C
ANISOU  164  CD2 LEU A  21     9004   5505   7540  -2441    387   1878       C
ATOM    165  N   ILE A  22       3.503 -16.411  61.525  1.00 56.08           N
ANISOU  165  N   ILE A  22     8689   5787   6832  -2179    485   1950       N
ATOM    166  CA  ILE A  22       2.678 -16.278  62.718  1.00 57.12           C
ANISOU  166  CA  ILE A  22     8723   6100   6879  -2249    555   2101       C
ATOM    167  C   ILE A  22       1.271 -16.728  62.362  1.00 60.69           C
ANISOU  167  C   ILE A  22     9098   6525   7439  -2407    564   2104       C
ATOM    168  O   ILE A  22       0.690 -16.212  61.400  1.00 58.58           O
ANISOU  168  O   ILE A  22     8797   6271   7192  -2425    532   1937       O
ATOM    169  CB  ILE A  22       2.638 -14.822  63.212  1.00 55.48           C
ANISOU  169  CB  ILE A  22     8446   6158   6476  -2162    590   2033       C
ATOM    170  CG1 ILE A  22       3.967 -14.353  63.795  1.00 55.00           C
ANISOU  170  CG1 ILE A  22     8443   6155   6299  -2018    587   2052       C
ATOM    171  CG2 ILE A  22       1.537 -14.640  64.222  1.00 55.47           C
ANISOU  171  CG2 ILE A  22     8327   6353   6397  -2248    666   2147       C
ATOM    172  CD1 ILE A  22       3.937 -12.812  64.100  1.00 50.47           C
ANISOU  172  CD1 ILE A  22     7802   5823   5551  -1929    610   1940       C
ATOM    173  N   ARG A  23       0.701 -17.654  63.141  1.00 61.90           N
ANISOU  173  N   ARG A  23     9215   6648   7658  -2524    607   2298       N
ATOM    174  CA  ARG A  23      -0.679 -18.080  62.918  1.00 63.14           C
ANISOU  174  CA  ARG A  23     9281   6792   7918  -2685    622   2317       C
ATOM    175  C   ARG A  23      -1.621 -17.262  63.788  1.00 66.09           C
ANISOU  175  C   ARG A  23     9520   7444   8148  -2717    700   2370       C
ATOM    176  O   ARG A  23      -1.493 -17.259  65.017  1.00 63.52           O
ANISOU  176  O   ARG A  23     9156   7257   7722  -2680    766   2519       O
ATOM    177  CB  ARG A  23      -0.864 -19.568  63.192  1.00 70.32           C
ANISOU  177  CB  ARG A  23    10188   7516   9014  -2751    627   2453       C
ATOM    178  CG  ARG A  23      -0.281 -20.419  62.100  1.00 69.53           C
ANISOU  178  CG  ARG A  23    10195   7129   9095  -2749    546   2357       C
ATOM    179  CD  ARG A  23      -0.651 -21.867  62.278  1.00 74.51           C
ANISOU  179  CD  ARG A  23    10805   7572   9933  -2823    555   2465       C
ATOM    180  NE  ARG A  23      -0.332 -22.610  61.068  1.00 79.84           N
ANISOU  180  NE  ARG A  23    11563   7982  10790  -2839    475   2330       N
ATOM    181  CZ  ARG A  23      -1.201 -22.886  60.105  1.00 83.22           C
ANISOU  181  CZ  ARG A  23    11961   8318  11342  -2953    430   2207       C
ATOM    182  NH1 ARG A  23      -2.478 -22.557  60.211  1.00 76.93           N
ANISOU  182  NH1 ARG A  23    11047   7657  10526  -3069    457   2214       N
ATOM    183  NH2 ARG A  23      -0.778 -23.514  59.011  1.00 84.51           N
ANISOU  183  NH2 ARG A  23    12209   8252  11651  -2948    356   2064       N
ATOM    184  N   VAL A  24      -2.569 -16.570  63.164  1.00 65.05           N
ANISOU  184  N   VAL A  24     9300   7405   8009  -2754    693   2228       N
ATOM    185  CA  VAL A  24      -3.580 -15.836  63.915  1.00 66.75           C
ANISOU  185  CA  VAL A  24     9374   7876   8111  -2791    770   2266       C
ATOM    186  C   VAL A  24      -4.787 -16.747  64.061  1.00 73.10           C
ANISOU  186  C   VAL A  24    10089   8637   9048  -2974    801   2386       C
ATOM    187  O   VAL A  24      -5.509 -17.033  63.093  1.00 70.95           O
ANISOU  187  O   VAL A  24     9786   8259   8912  -3064    751   2288       O
ATOM    188  CB  VAL A  24      -3.931 -14.488  63.297  1.00 66.30           C
ANISOU  188  CB  VAL A  24     9257   7966   7968  -2717    751   2061       C
ATOM    189  CG1 VAL A  24      -4.978 -13.838  64.171  1.00 66.36           C
ANISOU  189  CG1 VAL A  24     9113   8228   7872  -2755    838   2112       C
ATOM    190  CG2 VAL A  24      -2.683 -13.609  63.286  1.00 63.18           C
ANISOU  190  CG2 VAL A  24     8946   7613   7447  -2541    728   1968       C
ATOM    191  N   LYS A  25      -4.979 -17.196  65.308  1.00 74.75           N
ANISOU  191  N   LYS A  25    10241   8939   9221  -2976    881   2565       N
ATOM    192  CA  LYS A  25      -5.773 -18.383  65.609  1.00 77.20           C
ANISOU  192  CA  LYS A  25    10489   9154   9690  -3083    911   2690       C
ATOM    193  C   LYS A  25      -7.230 -18.036  65.788  1.00 79.68           C
ANISOU  193  C   LYS A  25    10640   9638   9997  -3189    968   2691       C
ATOM    194  O   LYS A  25      -8.098 -18.823  65.416  1.00 75.05           O
ANISOU  194  O   LYS A  25     9995   8939   9580  -3311    959   2709       O
ATOM    195  CB  LYS A  25      -5.259 -19.026  66.886  1.00 76.88           C
ANISOU  195  CB  LYS A  25    10468   9136   9605  -3021    974   2880       C
ATOM    196  CG  LYS A  25      -5.013 -20.495  66.896  1.00 83.10           C
ANISOU  196  CG  LYS A  25    11314   9675  10584  -3059    958   2990       C
ATOM    197  CD  LYS A  25      -4.047 -20.987  65.826  1.00 80.56           C
ANISOU  197  CD  LYS A  25    11129   9085  10394  -3022    858   2892       C
ATOM    198  CE  LYS A  25      -3.976 -22.498  65.909  1.00 83.38           C
ANISOU  198  CE  LYS A  25    11524   9200  10956  -3070    856   3004       C
ATOM    199  NZ  LYS A  25      -5.249 -23.165  65.541  1.00 90.10           N
ANISOU  199  NZ  LYS A  25    12285   9972  11978  -3228    864   3005       N
ATOM    200  N   GLU A  26      -7.494 -16.858  66.345  1.00 80.70           N
ANISOU  200  N   GLU A  26    10690  10034   9936  -3139   1027   2662       N
ATOM    201  CA  GLU A  26      -8.811 -16.313  66.627  1.00 73.69           C
ANISOU  201  CA  GLU A  26     9636   9354   9010  -3212   1093   2652       C
ATOM    202  C   GLU A  26      -9.360 -15.604  65.394  1.00 73.63           C
ANISOU  202  C   GLU A  26     9589   9342   9044  -3271   1029   2472       C
ATOM    203  O   GLU A  26      -8.626 -15.276  64.458  1.00 77.50           O
ANISOU  203  O   GLU A  26    10184   9717   9546  -3198    943   2325       O
ATOM    204  CB  GLU A  26      -8.747 -15.318  67.794  1.00 70.68           C
ANISOU  204  CB  GLU A  26     9192   9264   8399  -3112   1184   2683       C
ATOM    205  CG  GLU A  26      -7.757 -14.142  67.595  1.00 79.42           C
ANISOU  205  CG  GLU A  26    10376  10454   9345  -2984   1153   2556       C
ATOM    206  CD  GLU A  26      -6.285 -14.486  67.892  1.00 84.10           C
ANISOU  206  CD  GLU A  26    11124  10935   9895  -2871   1117   2608       C
ATOM    207  OE1 GLU A  26      -5.515 -13.560  68.229  1.00 84.77           O
ANISOU  207  OE1 GLU A  26    11248  11147   9815  -2753   1123   2549       O
ATOM    208  OE2 GLU A  26      -5.883 -15.663  67.793  1.00 80.87           O
ANISOU  208  OE2 GLU A  26    10793  10313   9621  -2897   1084   2701       O
ATOM    209  N   GLU A  27     -10.666 -15.356  65.413  1.00 66.83           N
ANISOU  209  N   GLU A  27     8569   8613   8210  -3362   1071   2459       N
ATOM    210  CA  GLU A  27     -11.322 -14.676  64.309  1.00 69.13           C
ANISOU  210  CA  GLU A  27     8797   8919   8550  -3381   1007   2270       C
ATOM    211  C   GLU A  27     -11.022 -13.177  64.324  1.00 68.62           C
ANISOU  211  C   GLU A  27     8716   9040   8315  -3210   1013   2115       C
ATOM    212  O   GLU A  27     -11.041 -12.524  65.373  1.00 68.87           O
ANISOU  212  O   GLU A  27     8687   9287   8191  -3147   1104   2166       O
ATOM    213  CB  GLU A  27     -12.824 -14.920  64.378  1.00 70.76           C
ANISOU  213  CB  GLU A  27     8825   9211   8848  -3537   1051   2319       C
ATOM    214  CG  GLU A  27     -13.682 -14.030  63.496  1.00 70.10           C
ANISOU  214  CG  GLU A  27     8633   9214   8786  -3523   1002   2128       C
ATOM    215  CD  GLU A  27     -15.155 -14.064  63.916  1.00 77.22           C
ANISOU  215  CD  GLU A  27     9331  10277   9735  -3653   1077   2197       C
ATOM    216  OE1 GLU A  27     -15.522 -13.342  64.872  1.00 80.65           O
ANISOU  216  OE1 GLU A  27     9658  10955  10030  -3606   1182   2240       O
ATOM    217  OE2 GLU A  27     -15.938 -14.828  63.307  1.00 78.40           O
ANISOU  217  OE2 GLU A  27     9422  10309  10059  -3804   1032   2206       O
ATOM    218  N   VAL A  28     -10.752 -12.624  63.144  1.00 65.95           N
ANISOU  218  N   VAL A  28     8429   8618   8009  -3137    914   1923       N
ATOM    219  CA  VAL A  28     -10.495 -11.199  63.023  1.00 67.79           C
ANISOU  219  CA  VAL A  28     8645   9000   8112  -2981    908   1771       C
ATOM    220  C   VAL A  28     -11.556 -10.593  62.123  1.00 67.81           C
ANISOU  220  C   VAL A  28     8530   9055   8179  -3008    862   1631       C
ATOM    221  O   VAL A  28     -12.215 -11.279  61.339  1.00 66.44           O
ANISOU  221  O   VAL A  28     8327   8765   8151  -3128    805   1616       O
ATOM    222  CB  VAL A  28      -9.081 -10.880  62.482  1.00 61.82           C
ANISOU  222  CB  VAL A  28     8056   8122   7310  -2840    836   1675       C
ATOM    223  CG1 VAL A  28      -8.021 -11.425  63.423  1.00 62.73           C
ANISOU  223  CG1 VAL A  28     8277   8200   7356  -2803    879   1816       C
ATOM    224  CG2 VAL A  28      -8.901 -11.423  61.074  1.00 62.05           C
ANISOU  224  CG2 VAL A  28     8170   7927   7479  -2876    722   1575       C
ATOM    225  N   ASN A  29     -11.746  -9.283  62.281  1.00 64.92           N
ANISOU  225  N   ASN A  29     8087   8872   7707  -2895    887   1529       N
ATOM    226  CA  ASN A  29     -12.566  -8.556  61.330  1.00 66.85           C
ANISOU  226  CA  ASN A  29     8236   9158   8006  -2887    827   1383       C
ATOM    227  C   ASN A  29     -11.759  -8.339  60.052  1.00 63.41           C
ANISOU  227  C   ASN A  29     7930   8560   7601  -2809    707   1247       C
ATOM    228  O   ASN A  29     -10.528  -8.296  60.095  1.00 63.69           O
ANISOU  228  O   ASN A  29     8107   8515   7576  -2716    691   1239       O
ATOM    229  CB  ASN A  29     -13.000  -7.214  61.916  1.00 66.01           C
ANISOU  229  CB  ASN A  29     8005   9286   7789  -2783    891   1319       C
ATOM    230  CG  ASN A  29     -13.994  -7.374  63.060  1.00 72.24           C
ANISOU  230  CG  ASN A  29     8637  10261   8549  -2865   1013   1435       C
ATOM    231  OD1 ASN A  29     -14.878  -8.230  63.016  1.00 73.56           O
ANISOU  231  OD1 ASN A  29     8724  10403   8821  -3018   1026   1521       O
ATOM    232  ND2 ASN A  29     -13.842  -6.557  64.098  1.00 68.90           N
ANISOU  232  ND2 ASN A  29     8168  10028   7982  -2767   1104   1436       N
ATOM    233  N   PRO A  30     -12.418  -8.256  58.891  1.00 63.94           N
ANISOU  233  N   PRO A  30     7951   8579   7763  -2851    619   1143       N
ATOM    234  CA  PRO A  30     -11.643  -8.014  57.653  1.00 58.30           C
ANISOU  234  CA  PRO A  30     7360   7731   7061  -2773    508   1014       C
ATOM    235  C   PRO A  30     -10.929  -6.664  57.647  1.00 56.59           C
ANISOU  235  C   PRO A  30     7173   7600   6727  -2595    508    922       C
ATOM    236  O   PRO A  30      -9.774  -6.592  57.214  1.00 52.77           O
ANISOU  236  O   PRO A  30     6833   7009   6210  -2509    464    878       O
ATOM    237  CB  PRO A  30     -12.686  -8.150  56.532  1.00 55.59           C
ANISOU  237  CB  PRO A  30     6931   7362   6828  -2863    421    931       C
ATOM    238  CG  PRO A  30     -14.025  -8.216  57.201  1.00 61.95           C
ANISOU  238  CG  PRO A  30     7552   8310   7675  -2966    488   1002       C
ATOM    239  CD  PRO A  30     -13.835  -8.576  58.642  1.00 62.31           C
ANISOU  239  CD  PRO A  30     7590   8422   7663  -2987    612   1153       C
ATOM    240  N   GLU A  31     -11.570  -5.603  58.144  1.00 55.93           N
ANISOU  240  N   GLU A  31     6957   7703   6589  -2538    558    893       N
ATOM    241  CA  GLU A  31     -10.964  -4.291  58.329  1.00 58.58           C
ANISOU  241  CA  GLU A  31     7304   8127   6825  -2374    570    814       C
ATOM    242  C   GLU A  31     -11.176  -3.837  59.762  1.00 57.77           C
ANISOU  242  C   GLU A  31     7114   8204   6631  -2340    689    873       C
ATOM    243  O   GLU A  31     -12.252  -4.054  60.325  1.00 63.21           O
ANISOU  243  O   GLU A  31     7666   9007   7342  -2426    752    931       O
ATOM    244  CB  GLU A  31     -11.574  -3.239  57.397  1.00 60.50           C
ANISOU  244  CB  GLU A  31     7461   8426   7100  -2315    503    691       C
ATOM    245  CG  GLU A  31     -11.590  -3.654  55.964  1.00 58.32           C
ANISOU  245  CG  GLU A  31     7244   8011   6903  -2358    386    630       C
ATOM    246  CD  GLU A  31     -12.863  -4.409  55.608  1.00 58.46           C
ANISOU  246  CD  GLU A  31     7152   8034   7027  -2511    359    653       C
ATOM    247  OE1 GLU A  31     -13.883  -4.268  56.326  1.00 61.98           O
ANISOU  247  OE1 GLU A  31     7444   8618   7488  -2561    426    697       O
ATOM    248  OE2 GLU A  31     -12.824  -5.163  54.620  1.00 54.70           O
ANISOU  248  OE2 GLU A  31     6742   7424   6619  -2583    272    624       O
ATOM    249  N   PRO A  32     -10.186  -3.161  60.365  1.00 57.57           N
ANISOU  249  N   PRO A  32     7157   8218   6500  -2214    722    852       N
ATOM    250  CA  PRO A  32      -8.928  -2.847  59.690  1.00 54.44           C
ANISOU  250  CA  PRO A  32     6908   7695   6083  -2113    651    784       C
ATOM    251  C   PRO A  32      -7.851  -3.877  60.019  1.00 52.94           C
ANISOU  251  C   PRO A  32     6866   7378   5870  -2137    658    877       C
ATOM    252  O   PRO A  32      -6.680  -3.677  59.696  1.00 56.73           O
ANISOU  252  O   PRO A  32     7468   7766   6319  -2048    617    837       O
ATOM    253  CB  PRO A  32      -8.587  -1.474  60.262  1.00 56.41           C
ANISOU  253  CB  PRO A  32     7118   8073   6243  -1969    688    706       C
ATOM    254  CG  PRO A  32      -9.074  -1.576  61.719  1.00 57.29           C
ANISOU  254  CG  PRO A  32     7137   8355   6277  -1999    804    787       C
ATOM    255  CD  PRO A  32     -10.269  -2.522  61.697  1.00 50.18           C
ANISOU  255  CD  PRO A  32     6143   7469   5454  -2155    827    873       C
ATOM    256  N   ASP A  33      -8.282  -4.985  60.625  1.00 53.89           N
ANISOU  256  N   ASP A  33     6967   7490   6017  -2260    706   1005       N
ATOM    257  CA  ASP A  33      -7.365  -5.893  61.310  1.00 56.21           C
ANISOU  257  CA  ASP A  33     7375   7706   6277  -2277    737   1123       C
ATOM    258  C   ASP A  33      -6.317  -6.458  60.357  1.00 50.13           C
ANISOU  258  C   ASP A  33     6764   6720   5562  -2256    651   1093       C
ATOM    259  O   ASP A  33      -5.130  -6.518  60.692  1.00 50.85           O
ANISOU  259  O   ASP A  33     6964   6760   5596  -2179    653   1117       O
ATOM    260  CB  ASP A  33      -8.136  -7.048  61.976  1.00 57.73           C
ANISOU  260  CB  ASP A  33     7512   7908   6517  -2428    797   1278       C
ATOM    261  CG  ASP A  33      -9.039  -6.602  63.128  1.00 63.15           C
ANISOU  261  CG  ASP A  33     8046   8825   7125  -2447    903   1333       C
ATOM    262  OD1 ASP A  33      -8.910  -5.460  63.615  1.00 63.53           O
ANISOU  262  OD1 ASP A  33     8047   9026   7066  -2333    939   1258       O
ATOM    263  OD2 ASP A  33      -9.856  -7.437  63.597  1.00 70.23           O
ANISOU  263  OD2 ASP A  33     8868   9750   8067  -2579    957   1457       O
ATOM    264  N   ILE A  34      -6.738  -6.897  59.169  1.00 51.09           N
ANISOU  264  N   ILE A  34     6897   6720   5795  -2324    574   1036       N
ATOM    265  CA  ILE A  34      -5.812  -7.605  58.286  1.00 48.87           C
ANISOU  265  CA  ILE A  34     6763   6233   5571  -2318    501   1008       C
ATOM    266  C   ILE A  34      -4.757  -6.658  57.737  1.00 50.38           C
ANISOU  266  C   ILE A  34     7035   6410   5698  -2169    458    899       C
ATOM    267  O   ILE A  34      -3.591  -7.035  57.567  1.00 51.29           O
ANISOU  267  O   ILE A  34     7278   6403   5807  -2117    436    904       O
ATOM    268  CB  ILE A  34      -6.577  -8.315  57.164  1.00 53.04           C
ANISOU  268  CB  ILE A  34     7277   6649   6227  -2432    429    962       C
ATOM    269  CG1 ILE A  34      -7.498  -9.399  57.760  1.00 49.09           C
ANISOU  269  CG1 ILE A  34     6706   6135   5810  -2591    472   1087       C
ATOM    270  CG2 ILE A  34      -5.593  -8.892  56.168  1.00 51.38           C
ANISOU  270  CG2 ILE A  34     7217   6243   6063  -2406    352    901       C
ATOM    271  CD1 ILE A  34      -8.556  -9.884  56.825  1.00 51.87           C
ANISOU  271  CD1 ILE A  34     6992   6431   6284  -2714    409   1034       C
ATOM    272  N   ALA A  35      -5.144  -5.422  57.432  1.00 45.22           N
ANISOU  272  N   ALA A  35     6302   5873   5006  -2097    446    802       N
ATOM    273  CA  ALA A  35      -4.156  -4.438  57.022  1.00 47.79           C
ANISOU  273  CA  ALA A  35     6691   6193   5273  -1957    415    713       C
ATOM    274  C   ALA A  35      -3.281  -4.027  58.200  1.00 49.66           C
ANISOU  274  C   ALA A  35     6956   6500   5412  -1869    478    759       C
ATOM    275  O   ALA A  35      -2.057  -3.916  58.066  1.00 47.33           O
ANISOU  275  O   ALA A  35     6767   6130   5085  -1784    458    740       O
ATOM    276  CB  ALA A  35      -4.851  -3.222  56.412  1.00 46.97           C
ANISOU  276  CB  ALA A  35     6489   6189   5170  -1907    383    609       C
ATOM    277  N   ALA A  36      -3.897  -3.789  59.364  1.00 47.65           N
ANISOU  277  N   ALA A  36     6602   6399   5103  -1887    556    815       N
ATOM    278  CA  ALA A  36      -3.114  -3.437  60.542  1.00 50.15           C
ANISOU  278  CA  ALA A  36     6941   6802   5314  -1809    614    856       C
ATOM    279  C   ALA A  36      -2.079  -4.511  60.851  1.00 48.36           C
ANISOU  279  C   ALA A  36     6841   6451   5082  -1823    613    956       C
ATOM    280  O   ALA A  36      -0.937  -4.199  61.197  1.00 46.21           O
ANISOU  280  O   ALA A  36     6641   6170   4745  -1728    611    949       O
ATOM    281  CB  ALA A  36      -4.034  -3.217  61.741  1.00 48.22           C
ANISOU  281  CB  ALA A  36     6568   6747   5007  -1844    703    910       C
ATOM    282  N   ALA A  37      -2.444  -5.783  60.688  1.00 47.31           N
ANISOU  282  N   ALA A  37     6734   6213   5029  -1941    608   1047       N
ATOM    283  CA  ALA A  37      -1.472  -6.843  60.923  1.00 53.13           C
ANISOU  283  CA  ALA A  37     7590   6813   5783  -1952    602   1144       C
ATOM    284  C   ALA A  37      -0.335  -6.778  59.923  1.00 49.27           C
ANISOU  284  C   ALA A  37     7221   6173   5325  -1870    530   1057       C
ATOM    285  O   ALA A  37       0.821  -7.028  60.285  1.00 51.03           O
ANISOU  285  O   ALA A  37     7535   6339   5515  -1806    530   1100       O
ATOM    286  CB  ALA A  37      -2.135  -8.212  60.871  1.00 51.90           C
ANISOU  286  CB  ALA A  37     7435   6553   5732  -2098    606   1252       C
ATOM    287  N   GLY A  38      -0.649  -6.475  58.658  1.00 45.73           N
ANISOU  287  N   GLY A  38     6772   5666   4937  -1872    469    941       N
ATOM    288  CA  GLY A  38       0.394  -6.331  57.653  1.00 45.81           C
ANISOU  288  CA  GLY A  38     6887   5554   4966  -1792    408    854       C
ATOM    289  C   GLY A  38       1.296  -5.139  57.917  1.00 49.00           C
ANISOU  289  C   GLY A  38     7301   6037   5278  -1654    415    798       C
ATOM    290  O   GLY A  38       2.523  -5.224  57.788  1.00 45.16           O
ANISOU  290  O   GLY A  38     6910   5469   4779  -1579    397    791       O
ATOM    291  N   ARG A  39       0.696  -3.998  58.272  1.00 45.94           N
ANISOU  291  N   ARG A  39     6810   5806   4837  -1618    439    750       N
ATOM    292  CA  ARG A  39       1.504  -2.848  58.655  1.00 45.71           C
ANISOU  292  CA  ARG A  39     6781   5854   4732  -1494    449    697       C
ATOM    293  C   ARG A  39       2.348  -3.188  59.872  1.00 43.71           C
ANISOU  293  C   ARG A  39     6569   5630   4408  -1462    491    785       C
ATOM    294  O   ARG A  39       3.527  -2.836  59.934  1.00 43.52           O
ANISOU  294  O   ARG A  39     6609   5576   4351  -1370    476    761       O
ATOM    295  CB  ARG A  39       0.614  -1.627  58.923  1.00 45.79           C
ANISOU  295  CB  ARG A  39     6664   6023   4711  -1466    472    631       C
ATOM    296  CG  ARG A  39       1.345  -0.387  59.469  1.00 41.17           C
ANISOU  296  CG  ARG A  39     6063   5524   4057  -1343    485    568       C
ATOM    297  CD  ARG A  39       2.225   0.291  58.415  1.00 41.53           C
ANISOU  297  CD  ARG A  39     6169   5477   4133  -1257    425    482       C
ATOM    298  NE  ARG A  39       3.585  -0.235  58.317  1.00 39.89           N
ANISOU  298  NE  ARG A  39     6081   5160   3917  -1218    407    511       N
ATOM    299  CZ  ARG A  39       4.400   0.030  57.299  1.00 43.85           C
ANISOU  299  CZ  ARG A  39     6648   5561   4450  -1162    359    457       C
ATOM    300  NH1 ARG A  39       4.035   0.838  56.318  1.00 38.70           N
ANISOU  300  NH1 ARG A  39     5961   4908   3834  -1137    323    380       N
ATOM    301  NH2 ARG A  39       5.611  -0.527  57.263  1.00 42.37           N
ANISOU  301  NH2 ARG A  39     6561   5279   4260  -1127    348    487       N
ATOM    302  N   ALA A  40       1.762  -3.907  60.835  1.00 49.78           N
ANISOU  302  N   ALA A  40     7301   6460   5155  -1541    544    896       N
ATOM    303  CA  ALA A  40       2.467  -4.242  62.072  1.00 46.31           C
ANISOU  303  CA  ALA A  40     6891   6072   4633  -1515    585    996       C
ATOM    304  C   ALA A  40       3.634  -5.175  61.798  1.00 44.64           C
ANISOU  304  C   ALA A  40     6807   5692   4463  -1498    549   1054       C
ATOM    305  O   ALA A  40       4.724  -5.000  62.354  1.00 47.64           O
ANISOU  305  O   ALA A  40     7235   6086   4782  -1416    548   1073       O
ATOM    306  CB  ALA A  40       1.497  -4.862  63.079  1.00 49.87           C
ANISOU  306  CB  ALA A  40     7269   6628   5053  -1614    652   1118       C
ATOM    307  N   ALA A  41       3.418  -6.185  60.951  1.00 44.64           N
ANISOU  307  N   ALA A  41     6858   5531   4571  -1574    517   1076       N
ATOM    308  CA  ALA A  41       4.479  -7.149  60.672  1.00 48.39           C
ANISOU  308  CA  ALA A  41     7451   5834   5102  -1558    485   1126       C
ATOM    309  C   ALA A  41       5.657  -6.476  59.993  1.00 49.41           C
ANISOU  309  C   ALA A  41     7643   5910   5220  -1440    443   1022       C
ATOM    310  O   ALA A  41       6.814  -6.745  60.336  1.00 49.52           O
ANISOU  310  O   ALA A  41     7725   5872   5216  -1374    435   1064       O
ATOM    311  CB  ALA A  41       3.956  -8.296  59.808  1.00 46.39           C
ANISOU  311  CB  ALA A  41     7234   5414   4977  -1662    456   1142       C
ATOM    312  N   ALA A  42       5.378  -5.600  59.020  1.00 44.01           N
ANISOU  312  N   ALA A  42     6932   5241   4549  -1412    413    892       N
ATOM    313  CA  ALA A  42       6.447  -4.874  58.347  1.00 47.38           C
ANISOU  313  CA  ALA A  42     7408   5628   4965  -1304    379    799       C
ATOM    314  C   ALA A  42       7.225  -4.015  59.336  1.00 50.68           C
ANISOU  314  C   ALA A  42     7805   6159   5292  -1210    401    804       C
ATOM    315  O   ALA A  42       8.443  -3.850  59.196  1.00 47.81           O
ANISOU  315  O   ALA A  42     7501   5743   4922  -1126    380    783       O
ATOM    316  CB  ALA A  42       5.881  -4.028  57.212  1.00 41.04           C
ANISOU  316  CB  ALA A  42     6566   4841   4186  -1296    347    680       C
ATOM    317  N   ASN A  43       6.536  -3.505  60.372  1.00 49.41           N
ANISOU  317  N   ASN A  43     7557   6158   5059  -1225    444    829       N
ATOM    318  CA  ASN A  43       7.104  -2.641  61.403  1.00 52.43           C
ANISOU  318  CA  ASN A  43     7905   6672   5345  -1144    465    818       C
ATOM    319  C   ASN A  43       7.959  -3.376  62.428  1.00 58.39           C
ANISOU  319  C   ASN A  43     8710   7429   6047  -1127    478    932       C
ATOM    320  O   ASN A  43       8.568  -2.716  63.278  1.00 60.70           O
ANISOU  320  O   ASN A  43     8981   7829   6253  -1057    486    919       O
ATOM    321  CB  ASN A  43       5.990  -1.898  62.148  1.00 50.75           C
ANISOU  321  CB  ASN A  43     7576   6637   5069  -1168    510    795       C
ATOM    322  CG  ASN A  43       5.410  -0.755  61.342  1.00 47.45           C
ANISOU  322  CG  ASN A  43     7095   6248   4687  -1140    492    667       C
ATOM    323  OD1 ASN A  43       5.905  -0.427  60.259  1.00 47.65           O
ANISOU  323  OD1 ASN A  43     7163   6171   4770  -1099    446    598       O
ATOM    324  ND2 ASN A  43       4.359  -0.139  61.860  1.00 46.26           N
ANISOU  324  ND2 ASN A  43     6837   6238   4502  -1160    531    638       N
ATOM    325  N   LEU A  44       7.996  -4.711  62.417  1.00 56.85           N
ANISOU  325  N   LEU A  44     8575   7123   5903  -1191    478   1045       N
ATOM    326  CA  LEU A  44       8.948  -5.385  63.296  1.00 59.08           C
ANISOU  326  CA  LEU A  44     8910   7391   6146  -1160    480   1159       C
ATOM    327  C   LEU A  44      10.397  -5.150  62.866  1.00 62.94           C
ANISOU  327  C   LEU A  44     9468   7794   6654  -1056    435   1107       C
ATOM    328  O   LEU A  44      11.321  -5.586  63.569  1.00 64.83           O
ANISOU  328  O   LEU A  44     9746   8027   6861  -1013    427   1190       O
ATOM    329  CB  LEU A  44       8.633  -6.876  63.358  1.00 54.32           C
ANISOU  329  CB  LEU A  44     8353   6672   5615  -1252    488   1298       C
ATOM    330  CG  LEU A  44       7.261  -7.148  63.982  1.00 53.98           C
ANISOU  330  CG  LEU A  44     8231   6732   5545  -1360    540   1375       C
ATOM    331  CD1 LEU A  44       6.890  -8.613  63.840  1.00 52.78           C
ANISOU  331  CD1 LEU A  44     8122   6434   5498  -1462    542   1502       C
ATOM    332  CD2 LEU A  44       7.241  -6.713  65.451  1.00 59.66           C
ANISOU  332  CD2 LEU A  44     8890   7661   6117  -1335    587   1444       C
ATOM    333  N   GLY A  45      10.612  -4.502  61.723  1.00 57.71           N
ANISOU  333  N   GLY A  45     8816   7066   6044  -1016    405    980       N
ATOM    334  CA  GLY A  45      11.935  -4.032  61.316  1.00 58.81           C
ANISOU  334  CA  GLY A  45     9000   7153   6194   -914    371    917       C
ATOM    335  C   GLY A  45      12.914  -5.088  60.833  1.00 65.83           C
ANISOU  335  C   GLY A  45     9983   7872   7159   -893    345    967       C
ATOM    336  O   GLY A  45      13.479  -4.952  59.739  1.00 62.71           O
ANISOU  336  O   GLY A  45     9627   7375   6823   -852    320    887       O
ATOM    337  N   LYS A  46      13.128  -6.149  61.627  1.00 60.05           N
ANISOU  337  N   LYS A  46     9283   7107   6425   -917    353   1101       N
ATOM    338  CA  LYS A  46      14.020  -7.228  61.227  1.00 61.66           C
ANISOU  338  CA  LYS A  46     9573   7140   6717   -894    329   1153       C
ATOM    339  C   LYS A  46      13.321  -8.559  61.434  1.00 55.12           C
ANISOU  339  C   LYS A  46     8772   6221   5951   -990    343   1273       C
ATOM    340  O   LYS A  46      12.491  -8.699  62.330  1.00 60.36           O
ANISOU  340  O   LYS A  46     9389   6985   6561  -1056    373   1362       O
ATOM    341  CB  LYS A  46      15.328  -7.191  62.011  1.00 60.38           C
ANISOU  341  CB  LYS A  46     9427   7005   6511   -801    312   1209       C
ATOM    342  CG  LYS A  46      16.172  -5.984  61.707  1.00 63.36           C
ANISOU  342  CG  LYS A  46     9781   7438   6855   -707    293   1091       C
ATOM    343  CD  LYS A  46      16.052  -4.944  62.814  1.00 69.00           C
ANISOU  343  CD  LYS A  46    10419   8351   7446   -683    303   1080       C
ATOM    344  CE  LYS A  46      16.512  -3.549  62.346  1.00 63.90           C
ANISOU  344  CE  LYS A  46     9734   7758   6787   -614    288    936       C
ATOM    345  NZ  LYS A  46      15.433  -2.806  61.620  1.00 64.39           N
ANISOU  345  NZ  LYS A  46     9755   7847   6862   -659    304    839       N
ATOM    346  N   ASN A  47      13.666  -9.535  60.592  1.00 52.91           N
ANISOU  346  N   ASN A  47     8566   5749   5790   -998    321   1272       N
ATOM    347  CA  ASN A  47      13.075 -10.875  60.658  1.00 50.10           C
ANISOU  347  CA  ASN A  47     8242   5267   5527  -1092    327   1377       C
ATOM    348  C   ASN A  47      11.560 -10.832  60.552  1.00 47.26           C
ANISOU  348  C   ASN A  47     7827   4962   5168  -1209    351   1368       C
ATOM    349  O   ASN A  47      10.881 -11.669  61.133  1.00 47.52           O
ANISOU  349  O   ASN A  47     7849   4973   5234  -1299    371   1491       O
ATOM    350  CB  ASN A  47      13.448 -11.612  61.955  1.00 55.43           C
ANISOU  350  CB  ASN A  47     8924   5956   6180  -1090    337   1562       C
ATOM    351  CG  ASN A  47      14.908 -11.588  62.241  1.00 57.31           C
ANISOU  351  CG  ASN A  47     9199   6170   6404   -972    311   1584       C
ATOM    352  OD1 ASN A  47      15.681 -12.313  61.615  1.00 62.62           O
ANISOU  352  OD1 ASN A  47     9939   6669   7186   -931    286   1575       O
ATOM    353  ND2 ASN A  47      15.313 -10.757  63.193  1.00 58.88           N
ANISOU  353  ND2 ASN A  47     9353   6547   6473   -914    315   1608       N
ATOM    354  N   GLN A  48      11.003  -9.868  59.830  1.00 45.11           N
ANISOU  354  N   GLN A  48     7512   4762   4865  -1213    348   1232       N
ATOM    355  CA  GLN A  48       9.548  -9.741  59.811  1.00 47.38           C
ANISOU  355  CA  GLN A  48     7731   5123   5148  -1319    370   1226       C
ATOM    356  C   GLN A  48       8.903 -11.006  59.250  1.00 50.45           C
ANISOU  356  C   GLN A  48     8155   5347   5667  -1425    358   1260       C
ATOM    357  O   GLN A  48       9.369 -11.536  58.226  1.00 47.38           O
ANISOU  357  O   GLN A  48     7837   4796   5369  -1410    323   1188       O
ATOM    358  CB  GLN A  48       9.119  -8.532  59.003  1.00 49.17           C
ANISOU  358  CB  GLN A  48     7910   5435   5338  -1296    359   1074       C
ATOM    359  CG  GLN A  48       9.797  -7.280  59.481  1.00 51.84           C
ANISOU  359  CG  GLN A  48     8215   5910   5572  -1192    365   1029       C
ATOM    360  CD  GLN A  48      10.899  -6.847  58.552  1.00 51.20           C
ANISOU  360  CD  GLN A  48     8188   5754   5512  -1096    331    928       C
ATOM    361  OE1 GLN A  48      11.859  -7.590  58.294  1.00 49.53           O
ANISOU  361  OE1 GLN A  48     8052   5413   5354  -1058    314    952       O
ATOM    362  NE2 GLN A  48      10.767  -5.642  58.033  1.00 45.85           N
ANISOU  362  NE2 GLN A  48     7466   5156   4799  -1056    324    819       N
ATOM    363  N   PRO A  49       7.877 -11.544  59.908  1.00 47.66           N
ANISOU  363  N   PRO A  49     7752   5027   5328  -1534    388   1367       N
ATOM    364  CA  PRO A  49       7.255 -12.787  59.458  1.00 47.77           C
ANISOU  364  CA  PRO A  49     7793   4875   5481  -1646    376   1407       C
ATOM    365  C   PRO A  49       6.037 -12.554  58.579  1.00 49.18           C
ANISOU  365  C   PRO A  49     7919   5071   5697  -1734    362   1301       C
ATOM    366  O   PRO A  49       5.441 -11.470  58.543  1.00 48.71           O
ANISOU  366  O   PRO A  49     7783   5172   5553  -1725    374   1231       O
ATOM    367  CB  PRO A  49       6.823 -13.437  60.777  1.00 52.61           C
ANISOU  367  CB  PRO A  49     8370   5536   6082  -1717    421   1604       C
ATOM    368  CG  PRO A  49       6.390 -12.230  61.612  1.00 49.68           C
ANISOU  368  CG  PRO A  49     7905   5419   5551  -1692    464   1604       C
ATOM    369  CD  PRO A  49       7.343 -11.100  61.210  1.00 49.38           C
ANISOU  369  CD  PRO A  49     7889   5438   5435  -1556    439   1468       C
ATOM    370  N   ALA A  50       5.673 -13.620  57.871  1.00 51.15           N
ANISOU  370  N   ALA A  50     8207   5144   6085  -1819    333   1289       N
ATOM    371  CA  ALA A  50       4.336 -13.740  57.316  1.00 49.56           C
ANISOU  371  CA  ALA A  50     7943   4950   5939  -1939    321   1238       C
ATOM    372  C   ALA A  50       3.316 -13.907  58.440  1.00 54.31           C
ANISOU  372  C   ALA A  50     8452   5662   6523  -2040    376   1385       C
ATOM    373  O   ALA A  50       3.624 -14.422  59.524  1.00 49.36           O
ANISOU  373  O   ALA A  50     7833   5036   5885  -2046    414   1546       O
ATOM    374  CB  ALA A  50       4.263 -14.923  56.362  1.00 47.54           C
ANISOU  374  CB  ALA A  50     7753   4469   5842  -2009    273   1188       C
ATOM    375  N   VAL A  51       2.094 -13.442  58.179  1.00 55.89           N
ANISOU  375  N   VAL A  51     8556   5967   6713  -2116    380   1332       N
ATOM    376  CA  VAL A  51       0.988 -13.514  59.129  1.00 58.13           C
ANISOU  376  CA  VAL A  51     8733   6375   6979  -2217    437   1452       C
ATOM    377  C   VAL A  51      -0.176 -14.251  58.464  1.00 57.68           C
ANISOU  377  C   VAL A  51     8631   6227   7058  -2366    411   1430       C
ATOM    378  O   VAL A  51      -0.747 -13.771  57.473  1.00 56.99           O
ANISOU  378  O   VAL A  51     8509   6161   6983  -2380    367   1286       O
ATOM    379  CB  VAL A  51       0.566 -12.113  59.600  1.00 56.45           C
ANISOU  379  CB  VAL A  51     8421   6407   6619  -2161    476   1409       C
ATOM    380  CG1 VAL A  51      -0.644 -12.192  60.521  1.00 55.89           C
ANISOU  380  CG1 VAL A  51     8229   6476   6529  -2267    541   1522       C
ATOM    381  CG2 VAL A  51       1.720 -11.452  60.305  1.00 53.89           C
ANISOU  381  CG2 VAL A  51     8139   6165   6173  -2025    497   1429       C
ATOM    382  N   PHE A  52      -0.537 -15.404  59.022  1.00 58.27           N
ANISOU  382  N   PHE A  52     8702   6204   7235  -2478    434   1578       N
ATOM    383  CA  PHE A  52      -1.606 -16.249  58.495  1.00 56.98           C
ANISOU  383  CA  PHE A  52     8495   5934   7222  -2633    409   1574       C
ATOM    384  C   PHE A  52      -2.827 -16.091  59.391  1.00 60.54           C
ANISOU  384  C   PHE A  52     8806   6553   7643  -2736    477   1690       C
ATOM    385  O   PHE A  52      -2.755 -16.337  60.599  1.00 60.03           O
ANISOU  385  O   PHE A  52     8719   6556   7532  -2750    546   1867       O
ATOM    386  CB  PHE A  52      -1.151 -17.709  58.424  1.00 56.71           C
ANISOU  386  CB  PHE A  52     8551   5643   7352  -2693    385   1656       C
ATOM    387  CG  PHE A  52      -2.169 -18.658  57.839  1.00 64.47           C
ANISOU  387  CG  PHE A  52     9497   6486   8512  -2857    349   1641       C
ATOM    388  CD1 PHE A  52      -1.927 -19.265  56.618  1.00 64.32           C
ANISOU  388  CD1 PHE A  52     9556   6263   8618  -2871    269   1494       C
ATOM    389  CD2 PHE A  52      -3.331 -18.990  58.525  1.00 65.09           C
ANISOU  389  CD2 PHE A  52     9461   6632   8637  -2999    398   1773       C
ATOM    390  CE1 PHE A  52      -2.836 -20.154  56.073  1.00 69.38           C
ANISOU  390  CE1 PHE A  52    10163   6769   9430  -3025    229   1466       C
ATOM    391  CE2 PHE A  52      -4.247 -19.874  57.983  1.00 69.24           C
ANISOU  391  CE2 PHE A  52     9948   7021   9340  -3156    361   1757       C
ATOM    392  CZ  PHE A  52      -3.998 -20.461  56.753  1.00 66.44           C
ANISOU  392  CZ  PHE A  52     9674   6458   9112  -3170    272   1599       C
ATOM    393  N   PHE A  53      -3.941 -15.673  58.807  1.00 59.27           N
ANISOU  393  N   PHE A  53     8547   6472   7502  -2805    458   1593       N
ATOM    394  CA  PHE A  53      -5.197 -15.563  59.533  1.00 60.12           C
ANISOU  394  CA  PHE A  53     8508   6735   7600  -2911    522   1689       C
ATOM    395  C   PHE A  53      -6.005 -16.804  59.215  1.00 64.21           C
ANISOU  395  C   PHE A  53     8999   7091   8309  -3086    498   1743       C
ATOM    396  O   PHE A  53      -6.316 -17.046  58.049  1.00 58.20           O
ANISOU  396  O   PHE A  53     8251   6215   7649  -3132    417   1603       O
ATOM    397  CB  PHE A  53      -5.958 -14.317  59.121  1.00 55.43           C
ANISOU  397  CB  PHE A  53     7808   6331   6923  -2877    515   1554       C
ATOM    398  CG  PHE A  53      -5.216 -13.058  59.376  1.00 60.08           C
ANISOU  398  CG  PHE A  53     8417   7067   7345  -2712    533   1488       C
ATOM    399  CD1 PHE A  53      -4.303 -12.584  58.453  1.00 56.71           C
ANISOU  399  CD1 PHE A  53     8088   6568   6893  -2597    467   1345       C
ATOM    400  CD2 PHE A  53      -5.446 -12.334  60.528  1.00 63.96           C
ANISOU  400  CD2 PHE A  53     8824   7771   7707  -2673    619   1565       C
ATOM    401  CE1 PHE A  53      -3.629 -11.415  58.682  1.00 62.39           C
ANISOU  401  CE1 PHE A  53     8820   7412   7475  -2452    482   1288       C
ATOM    402  CE2 PHE A  53      -4.778 -11.160  60.760  1.00 58.84           C
ANISOU  402  CE2 PHE A  53     8189   7249   6918  -2525    630   1492       C
ATOM    403  CZ  PHE A  53      -3.873 -10.704  59.838  1.00 60.31           C
ANISOU  403  CZ  PHE A  53     8472   7349   7094  -2417    561   1357       C
ATOM    404  N   GLU A  54      -6.319 -17.597  60.246  1.00 66.83           N
ANISOU  404  N   GLU A  54     9293   7412   8688  -3183    565   1948       N
ATOM    405  CA  GLU A  54      -7.131 -18.801  60.064  1.00 69.50           C
ANISOU  405  CA  GLU A  54     9592   7593   9223  -3363    550   2022       C
ATOM    406  C   GLU A  54      -8.619 -18.501  59.971  1.00 71.79           C
ANISOU  406  C   GLU A  54     9716   8022   9540  -3482    568   1999       C
ATOM    407  O   GLU A  54      -9.370 -19.301  59.402  1.00 77.67           O
ANISOU  407  O   GLU A  54    10421   8633  10457  -3627    524   1982       O
ATOM    408  CB  GLU A  54      -6.902 -19.777  61.216  1.00 70.71           C
ANISOU  408  CB  GLU A  54     9750   7690   9427  -3375    619   2240       C
ATOM    409  CG  GLU A  54      -5.551 -20.434  61.213  1.00 74.63           C
ANISOU  409  CG  GLU A  54    10396   7994   9965  -3273    589   2268       C
ATOM    410  CD  GLU A  54      -5.309 -21.238  62.467  1.00 83.27           C
ANISOU  410  CD  GLU A  54    11479   9078  11081  -3246    665   2481       C
ATOM    411  OE1 GLU A  54      -6.217 -21.282  63.328  1.00 86.55           O
ANISOU  411  OE1 GLU A  54    11774   9638  11472  -3308    744   2603       O
ATOM    412  OE2 GLU A  54      -4.214 -21.830  62.591  1.00 87.58           O
ANISOU  412  OE2 GLU A  54    12135   9475  11666  -3159    647   2525       O
ATOM    413  N   LYS A  55      -9.067 -17.387  60.551  1.00 73.39           N
ANISOU  413  N   LYS A  55     9814   8488   9585  -3427    632   1999       N
ATOM    414  CA  LYS A  55     -10.490 -17.090  60.692  1.00 69.71           C
ANISOU  414  CA  LYS A  55     9170   8180   9136  -3534    669   2009       C
ATOM    415  C   LYS A  55     -10.706 -15.609  60.441  1.00 68.28           C
ANISOU  415  C   LYS A  55     8922   8214   8807  -3415    668   1857       C
ATOM    416  O   LYS A  55     -10.202 -14.777  61.201  1.00 67.36           O
ANISOU  416  O   LYS A  55     8812   8257   8526  -3293    729   1881       O
ATOM    417  CB  LYS A  55     -10.995 -17.433  62.092  1.00 69.48           C
ANISOU  417  CB  LYS A  55     9046   8277   9076  -3609    789   2235       C
ATOM    418  CG  LYS A  55     -10.332 -18.628  62.729  1.00 77.30           C
ANISOU  418  CG  LYS A  55    10123   9101  10147  -3585    812   2383       C
ATOM    419  CD  LYS A  55     -11.075 -19.917  62.447  1.00 76.17           C
ANISOU  419  CD  LYS A  55     9936   8771  10232  -3715    791   2427       C
ATOM    420  CE  LYS A  55     -10.781 -20.938  63.531  1.00 81.00           C
ANISOU  420  CE  LYS A  55    10571   9313  10891  -3702    865   2626       C
ATOM    421  NZ  LYS A  55      -9.534 -21.683  63.192  1.00 86.58           N
ANISOU  421  NZ  LYS A  55    11447   9776  11675  -3633    805   2621       N
ATOM    422  N   ILE A  56     -11.481 -15.283  59.411  1.00 67.09           N
ANISOU  422  N   ILE A  56     8702   8069   8719  -3453    597   1706       N
ATOM    423  CA  ILE A  56     -11.896 -13.915  59.118  1.00 66.66           C
ANISOU  423  CA  ILE A  56     8560   8212   8555  -3358    591   1572       C
ATOM    424  C   ILE A  56     -13.419 -13.879  59.151  1.00 71.17           C
ANISOU  424  C   ILE A  56     8942   8904   9197  -3487    613   1587       C
ATOM    425  O   ILE A  56     -14.070 -14.725  58.527  1.00 68.90           O
ANISOU  425  O   ILE A  56     8621   8490   9066  -3628    556   1577       O
ATOM    426  CB  ILE A  56     -11.371 -13.434  57.755  1.00 64.08           C
ANISOU  426  CB  ILE A  56     8323   7798   8226  -3266    476   1373       C
ATOM    427  CG1 ILE A  56      -9.861 -13.651  57.644  1.00 63.63           C
ANISOU  427  CG1 ILE A  56     8452   7597   8127  -3157    452   1361       C
ATOM    428  CG2 ILE A  56     -11.736 -11.978  57.521  1.00 65.25           C
ANISOU  428  CG2 ILE A  56     8383   8145   8264  -3158    472   1255       C
ATOM    429  CD1 ILE A  56      -9.512 -14.845  56.769  1.00 61.69           C
ANISOU  429  CD1 ILE A  56     8316   7094   8030  -3232    370   1325       C
ATOM    430  N   LYS A  57     -13.978 -12.903  59.879  1.00 70.94           N
ANISOU  430  N   LYS A  57     8784   9116   9055  -3436    694   1603       N
ATOM    431  CA  LYS A  57     -15.417 -12.808  60.113  1.00 71.02           C
ANISOU  431  CA  LYS A  57     8595   9271   9118  -3547    737   1636       C
ATOM    432  C   LYS A  57     -16.201 -12.810  58.810  1.00 67.60           C
ANISOU  432  C   LYS A  57     8101   8778   8807  -3613    624   1493       C
ATOM    433  O   LYS A  57     -15.927 -12.015  57.913  1.00 68.67           O
ANISOU  433  O   LYS A  57     8274   8918   8900  -3506    543   1334       O
ATOM    434  CB  LYS A  57     -15.729 -11.534  60.899  1.00 71.55           C
ANISOU  434  CB  LYS A  57     8550   9605   9032  -3437    827   1621       C
ATOM    435  CG  LYS A  57     -17.105 -11.514  61.533  1.00 74.63           C
ANISOU  435  CG  LYS A  57     8730  10174   9453  -3544    913   1699       C
ATOM    436  CD  LYS A  57     -17.174 -10.527  62.689  1.00 78.44           C
ANISOU  436  CD  LYS A  57     9128  10909   9767  -3439   1034   1730       C
ATOM    437  CE  LYS A  57     -17.681  -9.158  62.226  1.00 80.58           C
ANISOU  437  CE  LYS A  57     9293  11328   9993  -3326   1008   1560       C
ATOM    438  NZ  LYS A  57     -17.452  -8.111  63.271  1.00 78.87           N
ANISOU  438  NZ  LYS A  57     9036  11327   9606  -3189   1112   1552       N
ATOM    439  N   GLY A  58     -17.184 -13.709  58.713  1.00 68.34           N
ANISOU  439  N   GLY A  58     8094   8819   9052  -3794    618   1556       N
ATOM    440  CA  GLY A  58     -18.061 -13.788  57.564  1.00 69.39           C
ANISOU  440  CA  GLY A  58     8146   8912   9306  -3877    510   1431       C
ATOM    441  C   GLY A  58     -17.550 -14.615  56.398  1.00 71.20           C
ANISOU  441  C   GLY A  58     8514   8893   9646  -3922    381   1335       C
ATOM    442  O   GLY A  58     -18.275 -14.756  55.405  1.00 66.04           O
ANISOU  442  O   GLY A  58     7797   8204   9092  -4001    282   1224       O
ATOM    443  N   TYR A  59     -16.326 -15.155  56.474  1.00 71.97           N
ANISOU  443  N   TYR A  59     8795   8822   9727  -3872    377   1365       N
ATOM    444  CA  TYR A  59     -15.680 -15.839  55.359  1.00 68.16           C
ANISOU  444  CA  TYR A  59     8460   8109   9330  -3883    260   1252       C
ATOM    445  C   TYR A  59     -15.356 -17.273  55.740  1.00 70.96           C
ANISOU  445  C   TYR A  59     8892   8246   9823  -4003    278   1377       C
ATOM    446  O   TYR A  59     -15.206 -17.602  56.920  1.00 73.26           O
ANISOU  446  O   TYR A  59     9176   8562  10098  -4025    385   1562       O
ATOM    447  CB  TYR A  59     -14.382 -15.127  54.927  1.00 65.68           C
ANISOU  447  CB  TYR A  59     8304   7773   8877  -3691    226   1147       C
ATOM    448  CG  TYR A  59     -14.580 -13.820  54.195  1.00 63.71           C
ANISOU  448  CG  TYR A  59     8008   7678   8523  -3575    173    996       C
ATOM    449  CD1 TYR A  59     -15.166 -13.774  52.930  1.00 63.08           C
ANISOU  449  CD1 TYR A  59     7890   7574   8503  -3618     55    847       C
ATOM    450  CD2 TYR A  59     -14.184 -12.622  54.772  1.00 63.99           C
ANISOU  450  CD2 TYR A  59     8033   7882   8400  -3421    238   1004       C
ATOM    451  CE1 TYR A  59     -15.343 -12.554  52.260  1.00 60.53           C
ANISOU  451  CE1 TYR A  59     7522   7394   8084  -3506      4    725       C
ATOM    452  CE2 TYR A  59     -14.353 -11.416  54.123  1.00 57.19           C
ANISOU  452  CE2 TYR A  59     7126   7147   7457  -3313    190    878       C
ATOM    453  CZ  TYR A  59     -14.925 -11.373  52.873  1.00 59.57           C
ANISOU  453  CZ  TYR A  59     7392   7425   7818  -3353     74    747       C
ATOM    454  OH  TYR A  59     -15.076 -10.133  52.255  1.00 56.38           O
ANISOU  454  OH  TYR A  59     6940   7150   7331  -3238     27    640       O
ATOM    455  N   LYS A  60     -15.272 -18.131  54.721  1.00 75.74           N
ANISOU  455  N   LYS A  60     9571   8640  10569  -4080    171   1275       N
ATOM    456  CA  LYS A  60     -14.968 -19.541  54.951  1.00 70.55           C
ANISOU  456  CA  LYS A  60     8991   7740  10074  -4195    173   1376       C
ATOM    457  C   LYS A  60     -13.471 -19.773  55.119  1.00 71.35           C
ANISOU  457  C   LYS A  60     9286   7705  10119  -4068    184   1398       C
ATOM    458  O   LYS A  60     -13.048 -20.490  56.032  1.00 71.37           O
ANISOU  458  O   LYS A  60     9331   7622  10166  -4074    256   1565       O
ATOM    459  CB  LYS A  60     -15.494 -20.391  53.793  1.00 70.91           C
ANISOU  459  CB  LYS A  60     9030   7609  10303  -4314     52   1235       C
ATOM    460  CG  LYS A  60     -17.008 -20.420  53.660  1.00 81.92           C
ANISOU  460  CG  LYS A  60    10224   9108  11793  -4441     38   1221       C
ATOM    461  CD  LYS A  60     -17.515 -21.788  53.203  1.00 74.67           C
ANISOU  461  CD  LYS A  60     9286   7973  11112  -4553    -17   1182       C
ATOM    462  CE  LYS A  60     -18.977 -22.008  53.576  1.00 82.14           C
ANISOU  462  CE  LYS A  60    10023   9018  12168  -4680     21   1250       C
ATOM    463  NZ  LYS A  60     -19.197 -22.214  55.044  1.00 86.84           N
ANISOU  463  NZ  LYS A  60    10547   9689  12758  -4688    175   1484       N
ATOM    464  N   TYR A  61     -12.660 -19.146  54.273  1.00 74.31           N
ANISOU  464  N   TYR A  61     9769   8074  10392  -3922    118   1231       N
ATOM    465  CA  TYR A  61     -11.263 -19.503  54.096  1.00 71.66           C
ANISOU  465  CA  TYR A  61     9618   7570  10038  -3815    100   1206       C
ATOM    466  C   TYR A  61     -10.368 -18.448  54.736  1.00 67.41           C
ANISOU  466  C   TYR A  61     9130   7186   9297  -3632    168   1246       C
ATOM    467  O   TYR A  61     -10.839 -17.584  55.482  1.00 70.38           O
ANISOU  467  O   TYR A  61     9399   7781   9561  -3601    241   1315       O
ATOM    468  CB  TYR A  61     -10.997 -19.715  52.611  1.00 68.24           C
ANISOU  468  CB  TYR A  61     9271   7002   9657  -3800    -26    985       C
ATOM    469  CG  TYR A  61     -11.883 -20.818  52.075  1.00 70.49           C
ANISOU  469  CG  TYR A  61     9502   7128  10151  -3991    -93    946       C
ATOM    470  CD1 TYR A  61     -11.867 -22.083  52.645  1.00 69.96           C
ANISOU  470  CD1 TYR A  61     9451   6872  10258  -4079    -60   1073       C
ATOM    471  CD2 TYR A  61     -12.759 -20.583  51.031  1.00 71.41           C
ANISOU  471  CD2 TYR A  61     9539   7300  10294  -4053   -188    780       C
ATOM    472  CE1 TYR A  61     -12.684 -23.096  52.171  1.00 71.79           C
ANISOU  472  CE1 TYR A  61     9613   6969  10693  -4197   -111   1016       C
ATOM    473  CE2 TYR A  61     -13.577 -21.582  50.547  1.00 70.35           C
ANISOU  473  CE2 TYR A  61     9349   7025  10355  -4229   -256    734       C
ATOM    474  CZ  TYR A  61     -13.538 -22.838  51.118  1.00 71.70           C
ANISOU  474  CZ  TYR A  61     9527   7012  10705  -4272   -210    842       C
ATOM    475  OH  TYR A  61     -14.361 -23.829  50.625  1.00 70.72           O
ANISOU  475  OH  TYR A  61     9329   6758  10782  -4389   -266    773       O
ATOM    476  N   SER A  62      -9.069 -18.549  54.478  1.00 65.97           N
ANISOU  476  N   SER A  62     9105   6885   9076  -3512    147   1201       N
ATOM    477  CA  SER A  62      -8.059 -17.802  55.217  1.00 65.01           C
ANISOU  477  CA  SER A  62     9044   6864   8791  -3352    213   1264       C
ATOM    478  C   SER A  62      -7.254 -16.864  54.309  1.00 63.17           C
ANISOU  478  C   SER A  62     8892   6670   8438  -3193    157   1088       C
ATOM    479  O   SER A  62      -7.315 -16.939  53.080  1.00 60.55           O
ANISOU  479  O   SER A  62     8594   6264   8148  -3199     67    923       O
ATOM    480  CB  SER A  62      -7.152 -18.776  55.986  1.00 69.50           C
ANISOU  480  CB  SER A  62     9718   7269   9420  -3349    255   1418       C
ATOM    481  OG  SER A  62      -6.995 -20.018  55.329  1.00 73.65           O
ANISOU  481  OG  SER A  62    10320   7532  10130  -3434    191   1380       O
ATOM    482  N   VAL A  63      -6.516 -15.957  54.955  1.00 60.58           N
ANISOU  482  N   VAL A  63     8589   6473   7955  -3052    214   1128       N
ATOM    483  CA  VAL A  63      -5.681 -14.937  54.324  1.00 53.21           C
ANISOU  483  CA  VAL A  63     7722   5599   6896  -2891    181    995       C
ATOM    484  C   VAL A  63      -4.266 -15.062  54.877  1.00 57.06           C
ANISOU  484  C   VAL A  63     8333   6016   7330  -2776    217   1060       C
ATOM    485  O   VAL A  63      -4.089 -15.253  56.084  1.00 58.83           O
ANISOU  485  O   VAL A  63     8544   6280   7528  -2779    291   1221       O
ATOM    486  CB  VAL A  63      -6.218 -13.511  54.611  1.00 58.41           C
ANISOU  486  CB  VAL A  63     8267   6507   7421  -2825    215    971       C
ATOM    487  CG1 VAL A  63      -5.217 -12.400  54.156  1.00 46.14           C
ANISOU  487  CG1 VAL A  63     6783   5011   5737  -2651    194    865       C
ATOM    488  CG2 VAL A  63      -7.595 -13.304  54.016  1.00 56.89           C
ANISOU  488  CG2 VAL A  63     7944   6394   7278  -2924    173    901       C
ATOM    489  N   VAL A  64      -3.255 -14.937  54.011  1.00 54.86           N
ANISOU  489  N   VAL A  64     8168   5647   7029  -2673    164    940       N
ATOM    490  CA  VAL A  64      -1.870 -14.814  54.461  1.00 54.13           C
ANISOU  490  CA  VAL A  64     8178   5519   6868  -2542    194    982       C
ATOM    491  C   VAL A  64      -1.269 -13.555  53.850  1.00 56.36           C
ANISOU  491  C   VAL A  64     8483   5910   7023  -2400    172    855       C
ATOM    492  O   VAL A  64      -1.584 -13.201  52.707  1.00 52.82           O
ANISOU  492  O   VAL A  64     8027   5469   6573  -2398    110    712       O
ATOM    493  CB  VAL A  64      -1.016 -16.062  54.133  1.00 53.57           C
ANISOU  493  CB  VAL A  64     8234   5202   6919  -2550    164    987       C
ATOM    494  CG1 VAL A  64      -0.790 -16.206  52.636  1.00 54.57           C
ANISOU  494  CG1 VAL A  64     8428   5221   7088  -2531     81    794       C
ATOM    495  CG2 VAL A  64       0.327 -15.973  54.859  1.00 50.82           C
ANISOU  495  CG2 VAL A  64     7969   4836   6504  -2423    204   1070       C
ATOM    496  N   THR A  65      -0.424 -12.861  54.626  1.00 52.16           N
ANISOU  496  N   THR A  65     7972   5467   6381  -2283    221    911       N
ATOM    497  CA  THR A  65       0.160 -11.595  54.215  1.00 51.23           C
ANISOU  497  CA  THR A  65     7863   5456   6146  -2150    209    811       C
ATOM    498  C   THR A  65       1.624 -11.532  54.648  1.00 51.05           C
ANISOU  498  C   THR A  65     7935   5389   6072  -2028    232    847       C
ATOM    499  O   THR A  65       2.090 -12.342  55.452  1.00 50.99           O
ANISOU  499  O   THR A  65     7970   5302   6100  -2042    263    967       O
ATOM    500  CB  THR A  65      -0.689 -10.434  54.768  1.00 57.44           C
ANISOU  500  CB  THR A  65     8521   6459   6843  -2142    246    822       C
ATOM    501  OG1 THR A  65      -1.818 -10.226  53.910  1.00 61.24           O
ANISOU  501  OG1 THR A  65     8926   6980   7363  -2214    200    734       O
ATOM    502  CG2 THR A  65       0.072  -9.138  54.872  1.00 52.67           C
ANISOU  502  CG2 THR A  65     7923   5968   6121  -1998    258    772       C
ATOM    503  N   ASN A  66       2.363 -10.581  54.056  1.00 47.60           N
ANISOU  503  N   ASN A  66     7530   4997   5558  -1910    211    746       N
ATOM    504  CA  ASN A  66       3.771 -10.317  54.368  1.00 48.58           C
ANISOU  504  CA  ASN A  66     7731   5101   5628  -1784    227    761       C
ATOM    505  C   ASN A  66       4.609 -11.553  54.110  1.00 47.77           C
ANISOU  505  C   ASN A  66     7737   4796   5616  -1785    210    781       C
ATOM    506  O   ASN A  66       5.615 -11.784  54.784  1.00 47.90           O
ANISOU  506  O   ASN A  66     7805   4774   5620  -1718    234    857       O
ATOM    507  CB  ASN A  66       3.984  -9.790  55.798  1.00 41.99           C
ANISOU  507  CB  ASN A  66     6849   4398   4706  -1741    288    873       C
ATOM    508  CG  ASN A  66       5.260  -8.897  55.923  1.00 47.17           C
ANISOU  508  CG  ASN A  66     7546   5100   5276  -1596    292    838       C
ATOM    509  OD1 ASN A  66       5.450  -7.950  55.162  1.00 44.54           O
ANISOU  509  OD1 ASN A  66     7205   4813   4904  -1530    268    729       O
ATOM    510  ND2 ASN A  66       6.132  -9.222  56.870  1.00 44.83           N
ANISOU  510  ND2 ASN A  66     7289   4789   4957  -1549    320    936       N
ATOM    511  N   VAL A  67       4.182 -12.330  53.107  1.00 43.36           N
ANISOU  511  N   VAL A  67     7208   4111   5154  -1859    163    703       N
ATOM    512  CA  VAL A  67       4.871 -13.560  52.742  1.00 42.66           C
ANISOU  512  CA  VAL A  67     7221   3815   5175  -1866    142    698       C
ATOM    513  C   VAL A  67       6.304 -13.272  52.317  1.00 45.54           C
ANISOU  513  C   VAL A  67     7670   4137   5497  -1726    137    636       C
ATOM    514  O   VAL A  67       7.231 -13.999  52.683  1.00 44.44           O
ANISOU  514  O   VAL A  67     7600   3876   5411  -1683    148    695       O
ATOM    515  CB  VAL A  67       4.083 -14.286  51.634  1.00 45.43           C
ANISOU  515  CB  VAL A  67     7580   4057   5625  -1969     86    591       C
ATOM    516  CG1 VAL A  67       4.931 -15.368  50.975  1.00 47.13           C
ANISOU  516  CG1 VAL A  67     7906   4059   5943  -1947     57    530       C
ATOM    517  CG2 VAL A  67       2.810 -14.859  52.201  1.00 43.24           C
ANISOU  517  CG2 VAL A  67     7224   3781   5424  -2117     95    680       C
ATOM    518  N   HIS A  68       6.509 -12.230  51.517  1.00 44.32           N
ANISOU  518  N   HIS A  68     7507   4078   5255  -1654    119    522       N
ATOM    519  CA  HIS A  68       7.841 -11.855  51.072  1.00 46.17           C
ANISOU  519  CA  HIS A  68     7809   4290   5446  -1524    119    463       C
ATOM    520  C   HIS A  68       8.497 -10.778  51.930  1.00 45.62           C
ANISOU  520  C   HIS A  68     7706   4354   5274  -1426    157    526       C
ATOM    521  O   HIS A  68       9.582 -10.315  51.574  1.00 47.14           O
ANISOU  521  O   HIS A  68     7938   4545   5426  -1319    158    479       O
ATOM    522  CB  HIS A  68       7.789 -11.341  49.642  1.00 44.82           C
ANISOU  522  CB  HIS A  68     7650   4145   5236  -1497     79    308       C
ATOM    523  CG  HIS A  68       7.528 -12.406  48.629  1.00 44.42           C
ANISOU  523  CG  HIS A  68     7654   3951   5273  -1561     36    211       C
ATOM    524  ND1 HIS A  68       6.258 -12.855  48.334  1.00 42.56           N
ANISOU  524  ND1 HIS A  68     7376   3704   5092  -1688      1    184       N
ATOM    525  CD2 HIS A  68       8.368 -13.069  47.800  1.00 45.41           C
ANISOU  525  CD2 HIS A  68     7868   3945   5441  -1514     20    120       C
ATOM    526  CE1 HIS A  68       6.329 -13.761  47.374  1.00 48.84           C
ANISOU  526  CE1 HIS A  68     8235   4362   5960  -1719    -39     76       C
ATOM    527  NE2 HIS A  68       7.599 -13.908  47.033  1.00 49.55           N
ANISOU  527  NE2 HIS A  68     8407   4379   6042  -1612    -26     32       N
ATOM    528  N   GLY A  69       7.869 -10.355  53.030  1.00 45.65           N
ANISOU  528  N   GLY A  69     7633   4477   5234  -1461    188    623       N
ATOM    529  CA  GLY A  69       8.233  -9.109  53.697  1.00 42.52           C
ANISOU  529  CA  GLY A  69     7187   4236   4733  -1378    215    643       C
ATOM    530  C   GLY A  69       9.406  -9.060  54.664  1.00 43.51           C
ANISOU  530  C   GLY A  69     7341   4367   4824  -1290    243    725       C
ATOM    531  O   GLY A  69       9.341  -8.331  55.652  1.00 45.34           O
ANISOU  531  O   GLY A  69     7514   4733   4978  -1266    271    779       O
ATOM    532  N   SER A  70      10.488  -9.788  54.409  1.00 43.81           N
ANISOU  532  N   SER A  70     7464   4270   4914  -1238    233    728       N
ATOM    533  CA  SER A  70      11.728  -9.583  55.160  1.00 40.55           C
ANISOU  533  CA  SER A  70     7072   3871   4463  -1137    249    787       C
ATOM    534  C   SER A  70      12.846 -10.242  54.379  1.00 40.29           C
ANISOU  534  C   SER A  70     7126   3683   4499  -1072    231    738       C
ATOM    535  O   SER A  70      12.603 -11.023  53.449  1.00 45.84           O
ANISOU  535  O   SER A  70     7875   4260   5281  -1114    211    675       O
ATOM    536  CB  SER A  70      11.669 -10.154  56.581  1.00 45.13           C
ANISOU  536  CB  SER A  70     7638   4472   5038  -1167    274    944       C
ATOM    537  OG  SER A  70      11.513 -11.555  56.557  1.00 41.89           O
ANISOU  537  OG  SER A  70     7278   3900   4738  -1233    267   1012       O
ATOM    538  N   TRP A  71      14.076  -9.952  54.787  1.00 38.81           N
ANISOU  538  N   TRP A  71     6955   3507   4283   -968    238    764       N
ATOM    539  CA  TRP A  71      15.212 -10.585  54.131  1.00 42.68           C
ANISOU  539  CA  TRP A  71     7520   3856   4841   -896    227    724       C
ATOM    540  C   TRP A  71      15.278 -12.065  54.439  1.00 41.49           C
ANISOU  540  C   TRP A  71     7423   3539   4801   -934    222    807       C
ATOM    541  O   TRP A  71      15.795 -12.834  53.625  1.00 45.85           O
ANISOU  541  O   TRP A  71     8039   3941   5441   -909    210    745       O
ATOM    542  CB  TRP A  71      16.514  -9.863  54.512  1.00 35.84           C
ANISOU  542  CB  TRP A  71     6645   3051   3923   -776    234    733       C
ATOM    543  CG  TRP A  71      16.553  -8.546  53.774  1.00 40.74           C
ANISOU  543  CG  TRP A  71     7228   3780   4473   -737    235    624       C
ATOM    544  CD1 TRP A  71      16.517  -7.275  54.313  1.00 40.20           C
ANISOU  544  CD1 TRP A  71     7091   3865   4317   -709    242    625       C
ATOM    545  CD2 TRP A  71      16.541  -8.382  52.358  1.00 35.26           C
ANISOU  545  CD2 TRP A  71     6559   3047   3790   -729    227    501       C
ATOM    546  NE1 TRP A  71      16.496  -6.338  53.295  1.00 39.02           N
ANISOU  546  NE1 TRP A  71     6925   3763   4140   -684    238    520       N
ATOM    547  CE2 TRP A  71      16.515  -6.995  52.093  1.00 38.11           C
ANISOU  547  CE2 TRP A  71     6866   3540   4075   -695    230    449       C
ATOM    548  CE3 TRP A  71      16.560  -9.276  51.279  1.00 37.29           C
ANISOU  548  CE3 TRP A  71     6881   3175   4115   -744    217    427       C
ATOM    549  CZ2 TRP A  71      16.518  -6.494  50.805  1.00 39.40           C
ANISOU  549  CZ2 TRP A  71     7037   3713   4222   -678    224    345       C
ATOM    550  CZ3 TRP A  71      16.556  -8.774  50.002  1.00 40.76           C
ANISOU  550  CZ3 TRP A  71     7327   3636   4523   -726    212    310       C
ATOM    551  CH2 TRP A  71      16.547  -7.399  49.773  1.00 37.98           C
ANISOU  551  CH2 TRP A  71     6920   3421   4089   -693    215    279       C
ATOM    552  N   GLN A  72      14.738 -12.476  55.583  1.00 43.77           N
ANISOU  552  N   GLN A  72     7686   3853   5092   -996    233    945       N
ATOM    553  CA  GLN A  72      14.693 -13.892  55.935  1.00 43.74           C
ANISOU  553  CA  GLN A  72     7727   3685   5206  -1044    228   1046       C
ATOM    554  C   GLN A  72      13.736 -14.641  55.022  1.00 44.39           C
ANISOU  554  C   GLN A  72     7834   3646   5387  -1148    212    973       C
ATOM    555  O   GLN A  72      14.079 -15.690  54.472  1.00 46.18           O
ANISOU  555  O   GLN A  72     8125   3685   5737  -1147    195    945       O
ATOM    556  CB  GLN A  72      14.269 -14.057  57.388  1.00 46.28           C
ANISOU  556  CB  GLN A  72     8007   4089   5490  -1092    247   1223       C
ATOM    557  CG  GLN A  72      15.362 -13.947  58.428  1.00 49.71           C
ANISOU  557  CG  GLN A  72     8442   4573   5874   -998    250   1334       C
ATOM    558  CD  GLN A  72      15.949 -12.546  58.570  1.00 52.48           C
ANISOU  558  CD  GLN A  72     8749   5098   6093   -908    254   1265       C
ATOM    559  OE1 GLN A  72      15.319 -11.538  58.231  1.00 47.60           O
ANISOU  559  OE1 GLN A  72     8083   4602   5401   -929    263   1172       O
ATOM    560  NE2 GLN A  72      17.169 -12.485  59.106  1.00 59.58           N
ANISOU  560  NE2 GLN A  72     9660   6007   6973   -806    244   1316       N
ATOM    561  N   ASN A  73      12.526 -14.111  54.853  1.00 45.17           N
ANISOU  561  N   ASN A  73     7875   3851   5436  -1235    214    936       N
ATOM    562  CA  ASN A  73      11.573 -14.730  53.940  1.00 44.60           C
ANISOU  562  CA  ASN A  73     7815   3682   5449  -1337    191    853       C
ATOM    563  C   ASN A  73      12.129 -14.746  52.518  1.00 45.72           C
ANISOU  563  C   ASN A  73     8015   3741   5617  -1281    165    680       C
ATOM    564  O   ASN A  73      12.007 -15.751  51.805  1.00 49.66           O
ANISOU  564  O   ASN A  73     8565   4075   6229  -1323    141    617       O
ATOM    565  CB  ASN A  73      10.233 -13.989  54.002  1.00 40.89           C
ANISOU  565  CB  ASN A  73     7260   3366   4910  -1427    196    839       C
ATOM    566  CG  ASN A  73       9.557 -14.102  55.383  1.00 46.93           C
ANISOU  566  CG  ASN A  73     7963   4215   5653  -1497    230   1007       C
ATOM    567  OD1 ASN A  73      10.189 -14.469  56.369  1.00 45.43           O
ANISOU  567  OD1 ASN A  73     7789   4008   5463  -1461    250   1139       O
ATOM    568  ND2 ASN A  73       8.271 -13.787  55.441  1.00 43.18           N
ANISOU  568  ND2 ASN A  73     7412   3838   5155  -1595    237   1005       N
ATOM    569  N   HIS A  74      12.777 -13.651  52.112  1.00 44.42           N
ANISOU  569  N   HIS A  74     7841   3689   5350  -1183    170    604       N
ATOM    570  CA  HIS A  74      13.383 -13.583  50.793  1.00 43.56           C
ANISOU  570  CA  HIS A  74     7780   3527   5243  -1121    154    451       C
ATOM    571  C   HIS A  74      14.478 -14.634  50.630  1.00 46.29           C
ANISOU  571  C   HIS A  74     8205   3692   5693  -1056    155    446       C
ATOM    572  O   HIS A  74      14.547 -15.304  49.598  1.00 44.83           O
ANISOU  572  O   HIS A  74     8072   3386   5576  -1061    137    328       O
ATOM    573  CB  HIS A  74      13.929 -12.177  50.567  1.00 40.15           C
ANISOU  573  CB  HIS A  74     7314   3255   4687  -1029    168    405       C
ATOM    574  CG  HIS A  74      14.327 -11.882  49.152  1.00 40.32           C
ANISOU  574  CG  HIS A  74     7369   3270   4682   -979    156    254       C
ATOM    575  ND1 HIS A  74      15.452 -12.425  48.570  1.00 39.84           N
ANISOU  575  ND1 HIS A  74     7372   3099   4666   -896    163    194       N
ATOM    576  CD2 HIS A  74      13.811 -11.024  48.238  1.00 39.58           C
ANISOU  576  CD2 HIS A  74     7245   3282   4509   -990    142    159       C
ATOM    577  CE1 HIS A  74      15.590 -11.943  47.345  1.00 39.38           C
ANISOU  577  CE1 HIS A  74     7325   3086   4551   -864    157     66       C
ATOM    578  NE2 HIS A  74      14.602 -11.101  47.117  1.00 40.68           N
ANISOU  578  NE2 HIS A  74     7436   3380   4641   -921    141     47       N
ATOM    579  N   ALA A  75      15.337 -14.802  51.638  1.00 44.55           N
ANISOU  579  N   ALA A  75     7989   3451   5487   -990    173    568       N
ATOM    580  CA  ALA A  75      16.373 -15.825  51.548  1.00 47.92           C
ANISOU  580  CA  ALA A  75     8482   3700   6027   -922    172    574       C
ATOM    581  C   ALA A  75      15.755 -17.219  51.431  1.00 52.09           C
ANISOU  581  C   ALA A  75     9052   4033   6707  -1015    152    586       C
ATOM    582  O   ALA A  75      16.162 -18.024  50.580  1.00 49.91           O
ANISOU  582  O   ALA A  75     8835   3597   6530   -990    140    482       O
ATOM    583  CB  ALA A  75      17.292 -15.742  52.766  1.00 45.49           C
ANISOU  583  CB  ALA A  75     8160   3420   5704   -844    187    723       C
ATOM    584  N   LEU A  76      14.735 -17.497  52.251  1.00 45.70           N
ANISOU  584  N   LEU A  76     8206   3238   5919  -1126    150    706       N
ATOM    585  CA  LEU A  76      14.043 -18.777  52.198  1.00 51.10           C
ANISOU  585  CA  LEU A  76     8918   3739   6758  -1232    131    731       C
ATOM    586  C   LEU A  76      13.354 -18.987  50.862  1.00 53.21           C
ANISOU  586  C   LEU A  76     9206   3951   7062  -1296    101    545       C
ATOM    587  O   LEU A  76      13.271 -20.126  50.378  1.00 48.29           O
ANISOU  587  O   LEU A  76     8633   3128   6589  -1337     78    490       O
ATOM    588  CB  LEU A  76      13.027 -18.867  53.333  1.00 46.81           C
ANISOU  588  CB  LEU A  76     8317   3259   6210  -1344    142    901       C
ATOM    589  CG  LEU A  76      13.625 -18.948  54.727  1.00 51.50           C
ANISOU  589  CG  LEU A  76     8898   3886   6785  -1297    166   1103       C
ATOM    590  CD1 LEU A  76      12.525 -18.819  55.741  1.00 48.92           C
ANISOU  590  CD1 LEU A  76     8502   3672   6413  -1408    186   1249       C
ATOM    591  CD2 LEU A  76      14.386 -20.285  54.929  1.00 53.06           C
ANISOU  591  CD2 LEU A  76     9161   3846   7152  -1264    154   1181       C
ATOM    592  N   MET A  77      12.840 -17.911  50.256  1.00 51.12           N
ANISOU  592  N   MET A  77     8899   3859   6666  -1307     97    446       N
ATOM    593  CA  MET A  77      12.332 -18.038  48.900  1.00 52.19           C
ANISOU  593  CA  MET A  77     9054   3961   6812  -1350     63    260       C
ATOM    594  C   MET A  77      13.411 -18.587  47.976  1.00 52.67           C
ANISOU  594  C   MET A  77     9195   3888   6929  -1253     59    127       C
ATOM    595  O   MET A  77      13.150 -19.482  47.164  1.00 56.35           O
ANISOU  595  O   MET A  77     9705   4209   7497  -1299     29      7       O
ATOM    596  CB  MET A  77      11.818 -16.689  48.412  1.00 51.12           C
ANISOU  596  CB  MET A  77     8862   4043   6517  -1349     61    190       C
ATOM    597  CG  MET A  77      11.475 -16.619  46.939  1.00 51.23           C
ANISOU  597  CG  MET A  77     8896   4064   6504  -1366     24     -3       C
ATOM    598  SD  MET A  77      11.193 -14.920  46.421  1.00 56.12           S
ANISOU  598  SD  MET A  77     9453   4939   6933  -1328     25    -55       S
ATOM    599  CE  MET A  77      12.860 -14.252  46.292  1.00 49.23           C
ANISOU  599  CE  MET A  77     8616   4106   5984  -1156     66    -67       C
ATOM    600  N   LEU A  78      14.641 -18.109  48.119  1.00 50.24           N
ANISOU  600  N   LEU A  78     8902   3622   6564  -1119     89    144       N
ATOM    601  CA  LEU A  78      15.710 -18.570  47.241  1.00 51.94           C
ANISOU  601  CA  LEU A  78     9182   3728   6825  -1018     94     16       C
ATOM    602  C   LEU A  78      16.321 -19.887  47.675  1.00 50.19           C
ANISOU  602  C   LEU A  78     9013   3277   6781   -993     94     71       C
ATOM    603  O   LEU A  78      17.380 -20.237  47.156  1.00 55.37           O
ANISOU  603  O   LEU A  78     9714   3844   7479   -886    107    -12       O
ATOM    604  CB  LEU A  78      16.815 -17.515  47.148  1.00 51.05           C
ANISOU  604  CB  LEU A  78     9055   3753   6589   -884    129      7       C
ATOM    605  CG  LEU A  78      16.435 -16.197  46.470  1.00 43.74           C
ANISOU  605  CG  LEU A  78     8087   3034   5499   -885    130    -70       C
ATOM    606  CD1 LEU A  78      17.510 -15.184  46.728  1.00 40.44           C
ANISOU  606  CD1 LEU A  78     7644   2737   4986   -766    165    -29       C
ATOM    607  CD2 LEU A  78      16.231 -16.377  44.993  1.00 46.38           C
ANISOU  607  CD2 LEU A  78     8457   3352   5813   -894    111   -263       C
ATOM    608  N   GLY A  79      15.715 -20.604  48.616  1.00 51.81           N
ANISOU  608  N   GLY A  79     9207   3386   7091  -1082     83    215       N
ATOM    609  CA  GLY A  79      16.283 -21.853  49.093  1.00 57.93           C
ANISOU  609  CA  GLY A  79    10029   3935   8048  -1058     80    292       C
ATOM    610  C   GLY A  79      17.551 -21.712  49.909  1.00 57.17           C
ANISOU  610  C   GLY A  79     9934   3848   7942   -928    106    417       C
ATOM    611  O   GLY A  79      18.341 -22.660  49.986  1.00 59.40           O
ANISOU  611  O   GLY A  79    10260   3941   8368   -863    104    435       O
ATOM    612  N   LEU A  80      17.754 -20.567  50.548  1.00 51.73           N
ANISOU  612  N   LEU A  80     9192   3367   7096   -888    128    505       N
ATOM    613  CA  LEU A  80      18.987 -20.269  51.267  1.00 53.64           C
ANISOU  613  CA  LEU A  80     9425   3649   7307   -762    147    606       C
ATOM    614  C   LEU A  80      18.725 -20.207  52.766  1.00 54.90           C
ANISOU  614  C   LEU A  80     9542   3874   7442   -800    149    832       C
ATOM    615  O   LEU A  80      17.586 -20.032  53.214  1.00 52.95           O
ANISOU  615  O   LEU A  80     9259   3703   7156   -917    147    899       O
ATOM    616  CB  LEU A  80      19.588 -18.938  50.786  1.00 52.21           C
ANISOU  616  CB  LEU A  80     9214   3662   6962   -673    169    513       C
ATOM    617  CG  LEU A  80      19.855 -18.788  49.285  1.00 49.76           C
ANISOU  617  CG  LEU A  80     8936   3340   6632   -631    175    297       C
ATOM    618  CD1 LEU A  80      20.239 -17.356  48.938  1.00 50.29           C
ANISOU  618  CD1 LEU A  80     8959   3619   6530   -569    197    243       C
ATOM    619  CD2 LEU A  80      20.940 -19.756  48.834  1.00 53.20           C
ANISOU  619  CD2 LEU A  80     9426   3588   7200   -531    181    231       C
ATOM    620  N   ASP A  81      19.793 -20.368  53.544  1.00 58.10           N
ANISOU  620  N   ASP A  81     9949   4258   7870   -700    152    950       N
ATOM    621  CA  ASP A  81      19.696 -20.141  54.981  1.00 53.46           C
ANISOU  621  CA  ASP A  81     9316   3775   7220   -718    154   1160       C
ATOM    622  C   ASP A  81      19.043 -18.786  55.242  1.00 53.52           C
ANISOU  622  C   ASP A  81     9261   4036   7039   -759    170   1149       C
ATOM    623  O   ASP A  81      19.341 -17.794  54.570  1.00 48.14           O
ANISOU  623  O   ASP A  81     8562   3471   6257   -707    179   1017       O
ATOM    624  CB  ASP A  81      21.087 -20.203  55.615  1.00 54.04           C
ANISOU  624  CB  ASP A  81     9390   3839   7305   -581    150   1253       C
ATOM    625  CG  ASP A  81      21.055 -20.117  57.136  1.00 60.59           C
ANISOU  625  CG  ASP A  81    10179   4771   8072   -594    145   1478       C
ATOM    626  OD1 ASP A  81      20.830 -19.009  57.672  1.00 66.16           O
ANISOU  626  OD1 ASP A  81    10829   5699   8610   -603    156   1501       O
ATOM    627  OD2 ASP A  81      21.265 -21.163  57.799  1.00 70.72           O
ANISOU  627  OD2 ASP A  81    11483   5912   9473   -593    129   1632       O
ATOM    628  N   LYS A  82      18.127 -18.754  56.209  1.00 51.36           N
ANISOU  628  N   LYS A  82     8947   3845   6723   -856    175   1289       N
ATOM    629  CA  LYS A  82      17.325 -17.552  56.407  1.00 52.35           C
ANISOU  629  CA  LYS A  82     9008   4193   6688   -907    191   1264       C
ATOM    630  C   LYS A  82      18.177 -16.336  56.779  1.00 49.40           C
ANISOU  630  C   LYS A  82     8596   4001   6171   -800    199   1253       C
ATOM    631  O   LYS A  82      17.763 -15.200  56.538  1.00 43.54           O
ANISOU  631  O   LYS A  82     7810   3421   5313   -811    209   1170       O
ATOM    632  CB  LYS A  82      16.245 -17.816  57.460  1.00 48.62           C
ANISOU  632  CB  LYS A  82     8495   3777   6200  -1023    202   1426       C
ATOM    633  CG  LYS A  82      16.727 -17.762  58.891  1.00 54.84           C
ANISOU  633  CG  LYS A  82     9255   4659   6921   -983    209   1617       C
ATOM    634  CD  LYS A  82      15.542 -17.734  59.871  1.00 62.72           C
ANISOU  634  CD  LYS A  82    10198   5775   7857  -1100    233   1755       C
ATOM    635  CE  LYS A  82      15.996 -17.975  61.315  1.00 72.56           C
ANISOU  635  CE  LYS A  82    11427   7092   9052  -1070    238   1970       C
ATOM    636  NZ  LYS A  82      14.926 -17.658  62.325  1.00 84.90           N
ANISOU  636  NZ  LYS A  82    12921   8833  10504  -1166    272   2089       N
ATOM    637  N   ASN A  83      19.366 -16.537  57.343  1.00 49.64           N
ANISOU  637  N   ASN A  83     8639   4006   6218   -697    190   1332       N
ATOM    638  CA  ASN A  83      20.172 -15.396  57.765  1.00 52.46           C
ANISOU  638  CA  ASN A  83     8950   4534   6447   -604    193   1323       C
ATOM    639  C   ASN A  83      21.153 -14.946  56.702  1.00 49.75           C
ANISOU  639  C   ASN A  83     8624   4164   6114   -503    193   1169       C
ATOM    640  O   ASN A  83      21.966 -14.050  56.965  1.00 49.14           O
ANISOU  640  O   ASN A  83     8509   4207   5955   -420    193   1156       O
ATOM    641  CB  ASN A  83      20.913 -15.710  59.063  1.00 52.89           C
ANISOU  641  CB  ASN A  83     8992   4615   6488   -548    178   1500       C
ATOM    642  CG  ASN A  83      19.968 -15.860  60.249  1.00 56.41           C
ANISOU  642  CG  ASN A  83     9405   5156   6874   -642    186   1661       C
ATOM    643  OD1 ASN A  83      19.093 -15.008  60.471  1.00 57.90           O
ANISOU  643  OD1 ASN A  83     9545   5508   6948   -705    205   1632       O
ATOM    644  ND2 ASN A  83      20.134 -16.942  61.013  1.00 47.34           N
ANISOU  644  ND2 ASN A  83     8279   3906   5802   -651    174   1834       N
ATOM    645  N   THR A  84      21.097 -15.545  55.513  1.00 49.30           N
ANISOU  645  N   THR A  84     8618   3958   6155   -511    195   1051       N
ATOM    646  CA  THR A  84      21.950 -15.107  54.417  1.00 48.52           C
ANISOU  646  CA  THR A  84     8533   3850   6054   -421    205    899       C
ATOM    647  C   THR A  84      21.815 -13.608  54.222  1.00 45.97           C
ANISOU  647  C   THR A  84     8153   3725   5587   -413    217    827       C
ATOM    648  O   THR A  84      20.697 -13.080  54.117  1.00 45.06           O
ANISOU  648  O   THR A  84     8014   3700   5408   -501    219    800       O
ATOM    649  CB  THR A  84      21.579 -15.840  53.128  1.00 43.80           C
ANISOU  649  CB  THR A  84     7992   3102   5549   -455    207    763       C
ATOM    650  OG1 THR A  84      21.654 -17.252  53.355  1.00 52.72           O
ANISOU  650  OG1 THR A  84     9170   4029   6831   -468    193    830       O
ATOM    651  CG2 THR A  84      22.512 -15.442  52.008  1.00 45.49           C
ANISOU  651  CG2 THR A  84     8218   3316   5750   -358    224    614       C
ATOM    652  N   SER A  85      22.962 -12.927  54.201  1.00 43.61           N
ANISOU  652  N   SER A  85     7829   3491   5250   -307    222    803       N
ATOM    653  CA  SER A  85      22.961 -11.473  54.101  1.00 43.83           C
ANISOU  653  CA  SER A  85     7799   3695   5159   -293    231    746       C
ATOM    654  C   SER A  85      22.397 -11.037  52.752  1.00 44.13           C
ANISOU  654  C   SER A  85     7849   3744   5173   -327    246    602       C
ATOM    655  O   SER A  85      22.355 -11.802  51.780  1.00 42.23           O
ANISOU  655  O   SER A  85     7662   3382   5002   -333    250    521       O
ATOM    656  CB  SER A  85      24.366 -10.903  54.204  1.00 43.39           C
ANISOU  656  CB  SER A  85     7713   3684   5088   -176    234    739       C
ATOM    657  OG  SER A  85      24.972 -11.020  52.927  1.00 46.35           O
ANISOU  657  OG  SER A  85     8117   3986   5509   -121    255    620       O
ATOM    658  N   THR A  86      21.981  -9.774  52.700  1.00 39.70           N
ANISOU  658  N   THR A  86     7235   3335   4514   -345    250    567       N
ATOM    659  CA  THR A  86      21.369  -9.261  51.488  1.00 43.39           C
ANISOU  659  CA  THR A  86     7705   3835   4947   -380    257    448       C
ATOM    660  C   THR A  86      22.356  -9.303  50.320  1.00 40.57           C
ANISOU  660  C   THR A  86     7377   3424   4613   -299    276    349       C
ATOM    661  O   THR A  86      22.008  -9.736  49.217  1.00 39.19           O
ANISOU  661  O   THR A  86     7244   3190   4456   -323    280    253       O
ATOM    662  CB  THR A  86      20.845  -7.839  51.759  1.00 44.13           C
ANISOU  662  CB  THR A  86     7729   4097   4943   -401    256    445       C
ATOM    663  OG1 THR A  86      19.892  -7.885  52.838  1.00 38.11           O
ANISOU  663  OG1 THR A  86     6937   3387   4155   -475    246    531       O
ATOM    664  CG2 THR A  86      20.185  -7.245  50.546  1.00 32.71           C
ANISOU  664  CG2 THR A  86     6278   2693   3457   -434    258    342       C
ATOM    665  N   LYS A  87      23.607  -8.914  50.570  1.00 41.54           N
ANISOU  665  N   LYS A  87     7475   3571   4737   -202    289    368       N
ATOM    666  CA  LYS A  87      24.644  -8.950  49.544  1.00 42.47           C
ANISOU  666  CA  LYS A  87     7609   3649   4878   -118    316    284       C
ATOM    667  C   LYS A  87      24.829 -10.358  48.994  1.00 44.23           C
ANISOU  667  C   LYS A  87     7904   3707   5196   -106    321    239       C
ATOM    668  O   LYS A  87      25.001 -10.546  47.785  1.00 44.14           O
ANISOU  668  O   LYS A  87     7923   3662   5185    -84    343    126       O
ATOM    669  CB  LYS A  87      25.965  -8.449  50.121  1.00 46.50           C
ANISOU  669  CB  LYS A  87     8073   4202   5394    -22    324    332       C
ATOM    670  CG  LYS A  87      27.064  -8.191  49.097  1.00 44.77           C
ANISOU  670  CG  LYS A  87     7847   3981   5185     65    361    252       C
ATOM    671  CD  LYS A  87      28.416  -8.110  49.799  1.00 46.82           C
ANISOU  671  CD  LYS A  87     8063   4242   5485    160    362    312       C
ATOM    672  CE  LYS A  87      28.770  -9.474  50.380  1.00 50.54           C
ANISOU  672  CE  LYS A  87     8576   4574   6053    190    346    369       C
ATOM    673  NZ  LYS A  87      30.109  -9.448  51.054  1.00 59.61           N
ANISOU  673  NZ  LYS A  87     9678   5726   7245    288    340    431       N
ATOM    674  N   ASP A  88      24.833 -11.355  49.872  1.00 44.36           N
ANISOU  674  N   ASP A  88     7944   3618   5292   -115    302    327       N
ATOM    675  CA  ASP A  88      24.957 -12.724  49.405  1.00 44.59           C
ANISOU  675  CA  ASP A  88     8041   3470   5433   -106    303    285       C
ATOM    676  C   ASP A  88      23.702 -13.183  48.673  1.00 42.70           C
ANISOU  676  C   ASP A  88     7843   3181   5198   -209    291    206       C
ATOM    677  O   ASP A  88      23.794 -13.988  47.739  1.00 43.06           O
ANISOU  677  O   ASP A  88     7942   3113   5307   -198    298     99       O
ATOM    678  CB  ASP A  88      25.295 -13.636  50.581  1.00 50.63           C
ANISOU  678  CB  ASP A  88     8815   4131   6291    -88    281    420       C
ATOM    679  CG  ASP A  88      26.754 -13.490  51.024  1.00 53.50           C
ANISOU  679  CG  ASP A  88     9146   4503   6679     35    289    468       C
ATOM    680  OD1 ASP A  88      27.572 -12.989  50.219  1.00 53.55           O
ANISOU  680  OD1 ASP A  88     9135   4548   6662    110    319    376       O
ATOM    681  OD2 ASP A  88      27.091 -13.869  52.171  1.00 54.21           O
ANISOU  681  OD2 ASP A  88     9223   4569   6807     56    265    602       O
ATOM    682  N   GLN A  89      22.524 -12.674  49.047  1.00 43.27           N
ANISOU  682  N   GLN A  89     7890   3344   5207   -309    272    245       N
ATOM    683  CA  GLN A  89      21.340 -13.017  48.264  1.00 42.60           C
ANISOU  683  CA  GLN A  89     7834   3229   5123   -407    257    160       C
ATOM    684  C   GLN A  89      21.411 -12.392  46.874  1.00 41.30           C
ANISOU  684  C   GLN A  89     7674   3137   4883   -383    271     15       C
ATOM    685  O   GLN A  89      21.009 -13.012  45.878  1.00 40.31           O
ANISOU  685  O   GLN A  89     7593   2941   4781   -415    264   -100       O
ATOM    686  CB  GLN A  89      20.073 -12.589  48.995  1.00 40.07           C
ANISOU  686  CB  GLN A  89     7473   2998   4755   -514    236    238       C
ATOM    687  CG  GLN A  89      19.855 -13.301  50.336  1.00 39.21           C
ANISOU  687  CG  GLN A  89     7361   2826   4712   -553    225    389       C
ATOM    688  CD  GLN A  89      18.529 -12.932  50.950  1.00 37.79           C
ANISOU  688  CD  GLN A  89     7137   2740   4481   -664    213    452       C
ATOM    689  OE1 GLN A  89      17.486 -12.956  50.275  1.00 41.93           O
ANISOU  689  OE1 GLN A  89     7662   3272   4999   -749    200    380       O
ATOM    690  NE2 GLN A  89      18.555 -12.528  52.212  1.00 37.97           N
ANISOU  690  NE2 GLN A  89     7114   2851   4461   -661    218    581       N
ATOM    691  N   PHE A  90      21.938 -11.172  46.797  1.00 43.48           N
ANISOU  691  N   PHE A  90     7901   3553   5068   -326    291     21       N
ATOM    692  CA  PHE A  90      22.159 -10.505  45.521  1.00 41.07           C
ANISOU  692  CA  PHE A  90     7593   3328   4685   -292    311    -92       C
ATOM    693  C   PHE A  90      23.073 -11.334  44.623  1.00 41.02           C
ANISOU  693  C   PHE A  90     7638   3218   4729   -217    338   -194       C
ATOM    694  O   PHE A  90      22.777 -11.541  43.439  1.00 38.16           O
ANISOU  694  O   PHE A  90     7310   2856   4334   -232    341   -318       O
ATOM    695  CB  PHE A  90      22.747  -9.115  45.785  1.00 39.54           C
ANISOU  695  CB  PHE A  90     7331   3277   4414   -238    330    -42       C
ATOM    696  CG  PHE A  90      23.382  -8.471  44.574  1.00 42.16           C
ANISOU  696  CG  PHE A  90     7657   3681   4682   -177    363   -129       C
ATOM    697  CD1 PHE A  90      22.614  -7.766  43.670  1.00 35.32           C
ANISOU  697  CD1 PHE A  90     6779   2914   3727   -222    355   -185       C
ATOM    698  CD2 PHE A  90      24.750  -8.545  44.364  1.00 39.79           C
ANISOU  698  CD2 PHE A  90     7354   3356   4408    -73    403   -144       C
ATOM    699  CE1 PHE A  90      23.187  -7.170  42.577  1.00 38.66           C
ANISOU  699  CE1 PHE A  90     7194   3412   4084   -169    388   -248       C
ATOM    700  CE2 PHE A  90      25.326  -7.933  43.269  1.00 40.57           C
ANISOU  700  CE2 PHE A  90     7439   3532   4443    -21    441   -212       C
ATOM    701  CZ  PHE A  90      24.544  -7.263  42.372  1.00 38.15           C
ANISOU  701  CZ  PHE A  90     7127   3325   4042    -70    434   -261       C
ATOM    702  N   TYR A  91      24.175 -11.848  45.182  1.00 41.26           N
ANISOU  702  N   TYR A  91     7674   3163   4840   -134    357   -148       N
ATOM    703  CA  TYR A  91      25.116 -12.627  44.380  1.00 41.77           C
ANISOU  703  CA  TYR A  91     7779   3128   4963    -49    388   -247       C
ATOM    704  C   TYR A  91      24.496 -13.936  43.913  1.00 47.66           C
ANISOU  704  C   TYR A  91     8596   3719   5794   -101    368   -335       C
ATOM    705  O   TYR A  91      24.735 -14.366  42.778  1.00 46.42           O
ANISOU  705  O   TYR A  91     8477   3525   5635    -68    388   -479       O
ATOM    706  CB  TYR A  91      26.399 -12.895  45.167  1.00 44.71           C
ANISOU  706  CB  TYR A  91     8131   3440   5415     53    406   -167       C
ATOM    707  CG  TYR A  91      27.350 -11.711  45.185  1.00 50.52           C
ANISOU  707  CG  TYR A  91     8801   4315   6080    129    438   -137       C
ATOM    708  CD1 TYR A  91      27.612 -10.982  44.020  1.00 53.49           C
ANISOU  708  CD1 TYR A  91     9163   4795   6366    157    477   -232       C
ATOM    709  CD2 TYR A  91      27.997 -11.332  46.353  1.00 45.79           C
ANISOU  709  CD2 TYR A  91     8151   3745   5503    170    429    -13       C
ATOM    710  CE1 TYR A  91      28.497  -9.878  44.037  1.00 50.01           C
ANISOU  710  CE1 TYR A  91     8655   4474   5875    220    508   -195       C
ATOM    711  CE2 TYR A  91      28.880 -10.256  46.380  1.00 46.67           C
ANISOU  711  CE2 TYR A  91     8195   3973   5563    233    453      9       C
ATOM    712  CZ  TYR A  91      29.125  -9.542  45.231  1.00 51.16           C
ANISOU  712  CZ  TYR A  91     8748   4631   6059    256    494    -79       C
ATOM    713  OH  TYR A  91      29.994  -8.482  45.279  1.00 53.46           O
ANISOU  713  OH  TYR A  91     8968   5029   6315    312    519    -47       O
ATOM    714  N   GLU A  92      23.681 -14.571  44.767  1.00 46.90           N
ANISOU  714  N   GLU A  92     8515   3534   5773   -184    328   -254       N
ATOM    715  CA  GLU A  92      23.014 -15.808  44.375  1.00 43.35           C
ANISOU  715  CA  GLU A  92     8126   2925   5422   -247    302   -332       C
ATOM    716  C   GLU A  92      21.960 -15.554  43.297  1.00 46.67           C
ANISOU  716  C   GLU A  92     8559   3417   5757   -331    283   -459       C
ATOM    717  O   GLU A  92      21.845 -16.329  42.344  1.00 50.38           O
ANISOU  717  O   GLU A  92     9079   3798   6264   -338    278   -605       O
ATOM    718  CB  GLU A  92      22.401 -16.481  45.614  1.00 47.18           C
ANISOU  718  CB  GLU A  92     8612   3306   6007   -322    268   -189       C
ATOM    719  CG  GLU A  92      21.834 -17.876  45.385  1.00 52.44           C
ANISOU  719  CG  GLU A  92     9338   3772   6816   -386    240   -245       C
ATOM    720  CD  GLU A  92      22.862 -18.842  44.823  1.00 60.94           C
ANISOU  720  CD  GLU A  92    10463   4683   8007   -286    260   -344       C
ATOM    721  OE1 GLU A  92      24.062 -18.718  45.166  1.00 70.39           O
ANISOU  721  OE1 GLU A  92    11644   5880   9222   -169    290   -294       O
ATOM    722  OE2 GLU A  92      22.479 -19.720  44.023  1.00 61.04           O
ANISOU  722  OE2 GLU A  92    10527   4570   8097   -321    245   -481       O
ATOM    723  N   LEU A  93      21.177 -14.479  43.416  1.00 47.06           N
ANISOU  723  N   LEU A  93     8561   3628   5692   -393    269   -412       N
ATOM    724  CA  LEU A  93      20.283 -14.122  42.315  1.00 43.56           C
ANISOU  724  CA  LEU A  93     8121   3274   5154   -458    248   -529       C
ATOM    725  C   LEU A  93      21.070 -13.885  41.035  1.00 46.09           C
ANISOU  725  C   LEU A  93     8461   3652   5399   -372    283   -666       C
ATOM    726  O   LEU A  93      20.693 -14.376  39.964  1.00 48.10           O
ANISOU  726  O   LEU A  93     8757   3886   5634   -399    269   -813       O
ATOM    727  CB  LEU A  93      19.472 -12.867  42.648  1.00 45.95           C
ANISOU  727  CB  LEU A  93     8360   3751   5350   -516    232   -449       C
ATOM    728  CG  LEU A  93      18.026 -13.035  43.099  1.00 47.86           C
ANISOU  728  CG  LEU A  93     8582   3991   5611   -647    185   -406       C
ATOM    729  CD1 LEU A  93      17.410 -11.663  43.190  1.00 47.03           C
ANISOU  729  CD1 LEU A  93     8409   4071   5389   -674    177   -356       C
ATOM    730  CD2 LEU A  93      17.228 -13.894  42.135  1.00 42.92           C
ANISOU  730  CD2 LEU A  93     8001   3291   5016   -723    147   -544       C
ATOM    731  N   ASN A  94      22.174 -13.131  41.126  1.00 44.39           N
ANISOU  731  N   ASN A  94     8213   3516   5136   -271    330   -621       N
ATOM    732  CA  ASN A  94      22.938 -12.832  39.921  1.00 45.84           C
ANISOU  732  CA  ASN A  94     8406   3773   5237   -190    374   -736       C
ATOM    733  C   ASN A  94      23.454 -14.108  39.283  1.00 48.45           C
ANISOU  733  C   ASN A  94     8800   3956   5652   -143    390   -873       C
ATOM    734  O   ASN A  94      23.489 -14.222  38.053  1.00 48.63           O
ANISOU  734  O   ASN A  94     8851   4024   5603   -125    405  -1021       O
ATOM    735  CB  ASN A  94      24.102 -11.889  40.216  1.00 47.33           C
ANISOU  735  CB  ASN A  94     8542   4055   5388    -92    424   -654       C
ATOM    736  CG  ASN A  94      24.975 -11.650  38.986  1.00 49.24           C
ANISOU  736  CG  ASN A  94     8787   4370   5550     -6    480   -763       C
ATOM    737  OD1 ASN A  94      24.536 -11.049  38.009  1.00 47.09           O
ANISOU  737  OD1 ASN A  94     8512   4225   5156    -31    480   -825       O
ATOM    738  ND2 ASN A  94      26.196 -12.186  39.008  1.00 50.12           N
ANISOU  738  ND2 ASN A  94     8906   4404   5734     98    527   -787       N
ATOM    739  N   ARG A  95      23.865 -15.081  40.100  1.00 46.53           N
ANISOU  739  N   ARG A  95     8579   3538   5561   -118    387   -827       N
ATOM    740  CA  ARG A  95      24.374 -16.320  39.530  1.00 46.69           C
ANISOU  740  CA  ARG A  95     8658   3399   5684    -66    402   -961       C
ATOM    741  C   ARG A  95      23.277 -17.057  38.763  1.00 52.19           C
ANISOU  741  C   ARG A  95     9407   4032   6392   -162    356  -1103       C
ATOM    742  O   ARG A  95      23.520 -17.591  37.676  1.00 58.70           O
ANISOU  742  O   ARG A  95    10272   4828   7204   -126    373  -1281       O
ATOM    743  CB  ARG A  95      24.969 -17.196  40.631  1.00 55.77           C
ANISOU  743  CB  ARG A  95     9817   4366   7009    -23    400   -862       C
ATOM    744  CG  ARG A  95      25.613 -18.495  40.133  1.00 54.94           C
ANISOU  744  CG  ARG A  95     9766   4072   7038     47    417   -993       C
ATOM    745  CD  ARG A  95      26.028 -19.363  41.314  1.00 62.45           C
ANISOU  745  CD  ARG A  95    10723   4834   8173     75    402   -866       C
ATOM    746  NE  ARG A  95      24.881 -19.916  42.025  1.00 61.82           N
ANISOU  746  NE  ARG A  95    10662   4650   8175    -51    342   -785       N
ATOM    747  CZ  ARG A  95      24.224 -21.007  41.654  1.00 62.20           C
ANISOU  747  CZ  ARG A  95    10765   4531   8337   -116    309   -885       C
ATOM    748  NH1 ARG A  95      24.608 -21.725  40.611  1.00 66.76           N
ANISOU  748  NH1 ARG A  95    11387   5014   8963    -61    326  -1081       N
ATOM    749  NH2 ARG A  95      23.150 -21.387  42.342  1.00 64.62           N
ANISOU  749  NH2 ARG A  95    11076   4764   8711   -240    258   -792       N
ATOM    750  N   ARG A  96      22.057 -17.072  39.300  1.00 49.44           N
ANISOU  750  N   ARG A  96     9051   3672   6061   -286    299  -1034       N
ATOM    751  CA  ARG A  96      20.969 -17.828  38.696  1.00 53.66           C
ANISOU  751  CA  ARG A  96     9627   4133   6629   -390    247  -1158       C
ATOM    752  C   ARG A  96      20.307 -17.114  37.524  1.00 52.62           C
ANISOU  752  C   ARG A  96     9487   4181   6325   -432    230  -1274       C
ATOM    753  O   ARG A  96      19.696 -17.772  36.677  1.00 52.18           O
ANISOU  753  O   ARG A  96     9471   4081   6275   -487    194  -1432       O
ATOM    754  CB  ARG A  96      19.919 -18.140  39.762  1.00 55.12           C
ANISOU  754  CB  ARG A  96     9797   4238   6908   -511    196  -1029       C
ATOM    755  CG  ARG A  96      20.418 -19.050  40.875  1.00 55.35           C
ANISOU  755  CG  ARG A  96     9842   4071   7118   -485    201   -915       C
ATOM    756  CD  ARG A  96      19.297 -19.317  41.868  1.00 59.78           C
ANISOU  756  CD  ARG A  96    10383   4577   7753   -614    156   -781       C
ATOM    757  NE  ARG A  96      19.780 -19.685  43.195  1.00 63.50           N
ANISOU  757  NE  ARG A  96    10845   4947   8337   -586    167   -600       N
ATOM    758  CZ  ARG A  96      18.996 -20.035  44.206  1.00 59.77           C
ANISOU  758  CZ  ARG A  96    10355   4414   7941   -684    139   -457       C
ATOM    759  NH1 ARG A  96      17.681 -20.057  44.085  1.00 56.11           N
ANISOU  759  NH1 ARG A  96     9877   3976   7468   -818    100   -473       N
ATOM    760  NH2 ARG A  96      19.546 -20.364  45.369  1.00 58.68           N
ANISOU  760  NH2 ARG A  96    10209   4196   7889   -645    150   -290       N
ATOM    761  N   TRP A  97      20.451 -15.795  37.449  1.00 49.77           N
ANISOU  761  N   TRP A  97     9076   4019   5817   -405    253  -1199       N
ATOM    762  CA  TRP A  97      19.596 -14.950  36.614  1.00 52.18           C
ANISOU  762  CA  TRP A  97     9357   4506   5963   -464    223  -1246       C
ATOM    763  C   TRP A  97      19.517 -15.414  35.168  1.00 53.08           C
ANISOU  763  C   TRP A  97     9518   4647   6004   -457    215  -1456       C
ATOM    764  O   TRP A  97      18.444 -15.381  34.560  1.00 54.17           O
ANISOU  764  O   TRP A  97     9656   4849   6076   -548    157  -1530       O
ATOM    765  CB  TRP A  97      20.115 -13.516  36.671  1.00 50.45           C
ANISOU  765  CB  TRP A  97     9079   4471   5617   -402    264  -1140       C
ATOM    766  CG  TRP A  97      19.143 -12.459  36.266  1.00 51.23           C
ANISOU  766  CG  TRP A  97     9135   4748   5582   -469    227  -1112       C
ATOM    767  CD1 TRP A  97      19.070 -11.845  35.060  1.00 50.11           C
ANISOU  767  CD1 TRP A  97     8989   4763   5287   -454    229  -1193       C
ATOM    768  CD2 TRP A  97      18.117 -11.877  37.082  1.00 48.70           C
ANISOU  768  CD2 TRP A  97     8763   4472   5268   -558    183   -990       C
ATOM    769  NE1 TRP A  97      18.063 -10.907  35.067  1.00 51.12           N
ANISOU  769  NE1 TRP A  97     9066   5023   5336   -524    184  -1122       N
ATOM    770  CE2 TRP A  97      17.464 -10.907  36.301  1.00 49.57           C
ANISOU  770  CE2 TRP A  97     8839   4759   5238   -587    157  -1004       C
ATOM    771  CE3 TRP A  97      17.681 -12.091  38.394  1.00 47.85           C
ANISOU  771  CE3 TRP A  97     8634   4278   5270   -612    165   -868       C
ATOM    772  CZ2 TRP A  97      16.395 -10.140  36.789  1.00 47.93           C
ANISOU  772  CZ2 TRP A  97     8571   4634   5007   -665    114   -908       C
ATOM    773  CZ3 TRP A  97      16.618 -11.331  38.880  1.00 45.68           C
ANISOU  773  CZ3 TRP A  97     8300   4097   4960   -692    128   -778       C
ATOM    774  CH2 TRP A  97      15.987 -10.367  38.074  1.00 47.90           C
ANISOU  774  CH2 TRP A  97     8544   4544   5112   -715    103   -802       C
ATOM    775  N   ASP A  98      20.635 -15.820  34.591  1.00 54.43           N
ANISOU  775  N   ASP A  98     9722   4783   6176   -349    272  -1558       N
ATOM    776  CA  ASP A  98      20.683 -16.066  33.156  1.00 58.28           C
ANISOU  776  CA  ASP A  98    10247   5343   6555   -326    277  -1759       C
ATOM    777  C   ASP A  98      20.646 -17.536  32.775  1.00 55.78           C
ANISOU  777  C   ASP A  98     9997   4834   6362   -335    257  -1943       C
ATOM    778  O   ASP A  98      20.754 -17.842  31.590  1.00 63.96           O
ANISOU  778  O   ASP A  98    11068   5923   7311   -309    263  -2133       O
ATOM    779  CB  ASP A  98      21.918 -15.398  32.554  1.00 55.33           C
ANISOU  779  CB  ASP A  98     9856   5101   6065   -198    362  -1771       C
ATOM    780  CG  ASP A  98      21.729 -13.896  32.378  1.00 65.86           C
ANISOU  780  CG  ASP A  98    11130   6661   7232   -206    369  -1651       C
ATOM    781  OD1 ASP A  98      20.573 -13.490  32.125  1.00 64.43           O
ANISOU  781  OD1 ASP A  98    10935   6570   6975   -302    304  -1645       O
ATOM    782  OD2 ASP A  98      22.709 -13.124  32.509  1.00 68.63           O
ANISOU  782  OD2 ASP A  98    11442   7094   7541   -118    435  -1560       O
ATOM    783  N   LYS A  99      20.475 -18.441  33.732  1.00 57.62           N
ANISOU  783  N   LYS A  99    10247   4851   6794   -374    231  -1891       N
ATOM    784  CA  LYS A  99      20.427 -19.868  33.429  1.00 59.93           C
ANISOU  784  CA  LYS A  99    10603   4934   7236   -386    208  -2059       C
ATOM    785  C   LYS A  99      19.366 -20.173  32.375  1.00 60.70           C
ANISOU  785  C   LYS A  99    10726   5079   7259   -483    141  -2245       C
ATOM    786  O   LYS A  99      18.224 -19.712  32.462  1.00 60.36           O
ANISOU  786  O   LYS A  99    10652   5123   7159   -597     79  -2189       O
ATOM    787  CB  LYS A  99      20.163 -20.667  34.710  1.00 56.15           C
ANISOU  787  CB  LYS A  99    10128   4227   6980   -441    178  -1932       C
ATOM    788  CG  LYS A  99      21.362 -20.724  35.664  1.00 66.05           C
ANISOU  788  CG  LYS A  99    11369   5390   8336   -330    239  -1790       C
ATOM    789  CD  LYS A  99      21.054 -21.549  36.927  1.00 67.24           C
ANISOU  789  CD  LYS A  99    11526   5324   8700   -388    205  -1652       C
ATOM    790  CE  LYS A  99      21.129 -23.041  36.639  1.00 68.67           C
ANISOU  790  CE  LYS A  99    11768   5250   9073   -387    185  -1801       C
ATOM    791  NZ  LYS A  99      22.481 -23.595  36.917  1.00 76.56           N
ANISOU  791  NZ  LYS A  99    12783   6114  10194   -244    241  -1794       N
ATOM    792  N   PHE A 100      19.764 -20.947  31.370  1.00 66.76           N
ANISOU  792  N   PHE A 100    11545   5795   8026   -432    153  -2473       N
ATOM    793  CA  PHE A 100      18.936 -21.291  30.224  1.00 64.17           C
ANISOU  793  CA  PHE A 100    11232   5532   7616   -501     91  -2681       C
ATOM    794  C   PHE A 100      19.519 -22.556  29.616  1.00 71.44           C
ANISOU  794  C   PHE A 100    12149   6327   8669   -428     99  -2880       C
ATOM    795  O   PHE A 100      20.744 -22.721  29.616  1.00 71.58           O
ANISOU  795  O   PHE A 100    12171   6307   8721   -295    178  -2895       O
ATOM    796  CB  PHE A 100      18.928 -20.140  29.199  1.00 68.21           C
ANISOU  796  CB  PHE A 100    11732   6337   7848   -475    109  -2720       C
ATOM    797  CG  PHE A 100      18.155 -20.427  27.925  1.00 75.07           C
ANISOU  797  CG  PHE A 100    12587   7328   8610   -527     41  -2925       C
ATOM    798  CD1 PHE A 100      16.777 -20.265  27.876  1.00 73.01           C
ANISOU  798  CD1 PHE A 100    12307   7117   8318   -669    -56  -2916       C
ATOM    799  CD2 PHE A 100      18.818 -20.842  26.769  1.00 71.77           C
ANISOU  799  CD2 PHE A 100    12161   6989   8119   -431     73  -3125       C
ATOM    800  CE1 PHE A 100      16.075 -20.516  26.701  1.00 79.52           C
ANISOU  800  CE1 PHE A 100    13106   8065   9042   -712   -126  -3101       C
ATOM    801  CE2 PHE A 100      18.118 -21.098  25.591  1.00 74.15           C
ANISOU  801  CE2 PHE A 100    12441   7420   8313   -473      5  -3315       C
ATOM    802  CZ  PHE A 100      16.747 -20.939  25.557  1.00 78.07           C
ANISOU  802  CZ  PHE A 100    12919   7962   8781   -613    -98  -3302       C
ATOM    803  N   PRO A 101      18.679 -23.478  29.108  1.00 71.10           N
ANISOU  803  N   PRO A 101    12090   6211   8714   -508     17  -3041       N
ATOM    804  CA  PRO A 101      17.217 -23.429  29.193  1.00 71.60           C
ANISOU  804  CA  PRO A 101    12138   6291   8776   -669    -80  -3022       C
ATOM    805  C   PRO A 101      16.664 -24.191  30.400  1.00 76.30           C
ANISOU  805  C   PRO A 101    12725   6638   9626   -763   -122  -2897       C
ATOM    806  O   PRO A 101      17.220 -25.228  30.808  1.00 76.09           O
ANISOU  806  O   PRO A 101    12700   6394   9816   -716   -107  -2917       O
ATOM    807  CB  PRO A 101      16.779 -24.094  27.884  1.00 74.35           C
ANISOU  807  CB  PRO A 101    12466   6697   9087   -685   -142  -3288       C
ATOM    808  CG  PRO A 101      17.839 -25.153  27.658  1.00 69.95           C
ANISOU  808  CG  PRO A 101    11914   5982   8681   -565    -99  -3428       C
ATOM    809  CD  PRO A 101      19.136 -24.597  28.258  1.00 69.64           C
ANISOU  809  CD  PRO A 101    11896   5946   8620   -438     13  -3279       C
ATOM    810  N   VAL A 102      15.568 -23.685  30.960  1.00 73.50           N
ANISOU  810  N   VAL A 102    12357   6321   9248   -896   -174  -2765       N
ATOM    811  CA  VAL A 102      14.830 -24.410  31.996  1.00 70.87           C
ANISOU  811  CA  VAL A 102    12004   5782   9140  -1008   -221  -2652       C
ATOM    812  C   VAL A 102      13.355 -24.449  31.607  1.00 68.88           C
ANISOU  812  C   VAL A 102    11714   5592   8865  -1163   -319  -2716       C
ATOM    813  O   VAL A 102      12.523 -23.845  32.303  1.00 67.62           O
ANISOU  813  O   VAL A 102    11535   5479   8679  -1267   -344  -2556       O
ATOM    814  CB  VAL A 102      15.023 -23.762  33.378  1.00 67.48           C
ANISOU  814  CB  VAL A 102    11585   5321   8733  -1014   -176  -2381       C
ATOM    815  CG1 VAL A 102      14.605 -24.715  34.481  1.00 68.76           C
ANISOU  815  CG1 VAL A 102    11726   5249   9152  -1093   -203  -2258       C
ATOM    816  CG2 VAL A 102      16.456 -23.339  33.569  1.00 65.51           C
ANISOU  816  CG2 VAL A 102    11368   5092   8431   -856    -82  -2325       C
ATOM    817  N   PRO A 103      12.982 -25.153  30.533  1.00 72.45           N
ANISOU  817  N   PRO A 103    12148   6049   9333  -1182   -379  -2948       N
ATOM    818  CA  PRO A 103      11.581 -25.130  30.072  1.00 73.41           C
ANISOU  818  CA  PRO A 103    12224   6252   9417  -1325   -479  -3019       C
ATOM    819  C   PRO A 103      10.639 -25.638  31.150  1.00 73.31           C
ANISOU  819  C   PRO A 103    12175   6067   9614  -1466   -523  -2876       C
ATOM    820  O   PRO A 103      10.979 -26.567  31.902  1.00 74.93           O
ANISOU  820  O   PRO A 103    12382   6036  10052  -1459   -502  -2818       O
ATOM    821  CB  PRO A 103      11.580 -26.064  28.845  1.00 74.40           C
ANISOU  821  CB  PRO A 103    12338   6357   9576  -1297   -532  -3305       C
ATOM    822  CG  PRO A 103      12.904 -26.738  28.819  1.00 73.36           C
ANISOU  822  CG  PRO A 103    12240   6087   9547  -1154   -461  -3374       C
ATOM    823  CD  PRO A 103      13.854 -25.949  29.651  1.00 68.79           C
ANISOU  823  CD  PRO A 103    11697   5531   8908  -1066   -359  -3165       C
ATOM    824  N   PRO A 104       9.455 -25.046  31.272  1.00 71.25           N
ANISOU  824  N   PRO A 104    11872   5921   9278  -1594   -581  -2806       N
ATOM    825  CA  PRO A 104       8.483 -25.545  32.250  1.00 73.22           C
ANISOU  825  CA  PRO A 104    12073   6022   9724  -1737   -620  -2674       C
ATOM    826  C   PRO A 104       7.936 -26.897  31.821  1.00 77.01           C
ANISOU  826  C   PRO A 104    12515   6330  10416  -1806   -693  -2844       C
ATOM    827  O   PRO A 104       7.919 -27.248  30.643  1.00 79.15           O
ANISOU  827  O   PRO A 104    12783   6654  10637  -1778   -742  -3081       O
ATOM    828  CB  PRO A 104       7.383 -24.478  32.241  1.00 69.27           C
ANISOU  828  CB  PRO A 104    11530   5729   9059  -1844   -667  -2595       C
ATOM    829  CG  PRO A 104       7.458 -23.895  30.865  1.00 69.20           C
ANISOU  829  CG  PRO A 104    11531   5945   8818  -1786   -698  -2777       C
ATOM    830  CD  PRO A 104       8.913 -23.943  30.462  1.00 70.85           C
ANISOU  830  CD  PRO A 104    11806   6145   8968  -1616   -617  -2850       C
ATOM    831  N   ASN A 105       7.484 -27.663  32.803  1.00 80.50           N
ANISOU  831  N   ASN A 105    12921   6566  11098  -1897   -701  -2720       N
ATOM    832  CA  ASN A 105       6.856 -28.949  32.551  1.00 76.23           C
ANISOU  832  CA  ASN A 105    12331   5840  10792  -1982   -771  -2854       C
ATOM    833  C   ASN A 105       5.345 -28.779  32.556  1.00 79.48           C
ANISOU  833  C   ASN A 105    12665   6327  11206  -2154   -853  -2833       C
ATOM    834  O   ASN A 105       4.773 -28.349  33.561  1.00 77.94           O
ANISOU  834  O   ASN A 105    12438   6146  11031  -2241   -835  -2612       O
ATOM    835  CB  ASN A 105       7.306 -29.980  33.578  1.00 78.69           C
ANISOU  835  CB  ASN A 105    12642   5870  11388  -1976   -727  -2730       C
ATOM    836  CG  ASN A 105       7.220 -31.387  33.050  1.00 88.89           C
ANISOU  836  CG  ASN A 105    13904   6947  12922  -1994   -777  -2931       C
ATOM    837  OD1 ASN A 105       7.171 -31.615  31.830  1.00 89.91           O
ANISOU  837  OD1 ASN A 105    14035   7137  12991  -1966   -838  -3191       O
ATOM    838  ND2 ASN A 105       7.179 -32.351  33.960  1.00 95.17           N
ANISOU  838  ND2 ASN A 105    14669   7493  13998  -2044   -751  -2813       N
ATOM    839  N   VAL A 106       4.707 -29.088  31.427  1.00 78.92           N
ANISOU  839  N   VAL A 106    12559   6319  11108  -2199   -945  -3064       N
ATOM    840  CA  VAL A 106       3.253 -28.985  31.316  1.00 76.03           C
ANISOU  840  CA  VAL A 106    12108   6029  10751  -2360  -1033  -3069       C
ATOM    841  C   VAL A 106       2.654 -30.278  31.855  1.00 80.87           C
ANISOU  841  C   VAL A 106    12657   6379  11689  -2473  -1063  -3061       C
ATOM    842  O   VAL A 106       2.809 -31.337  31.249  1.00 85.48           O
ANISOU  842  O   VAL A 106    13236   6812  12431  -2458  -1104  -3262       O
ATOM    843  CB  VAL A 106       2.806 -28.727  29.870  1.00 78.97           C
ANISOU  843  CB  VAL A 106    12463   6597  10945  -2356  -1128  -3314       C
ATOM    844  CG1 VAL A 106       1.260 -28.664  29.750  1.00 82.13           C
ANISOU  844  CG1 VAL A 106    12762   7073  11370  -2524  -1231  -3322       C
ATOM    845  CG2 VAL A 106       3.425 -27.461  29.321  1.00 76.36           C
ANISOU  845  CG2 VAL A 106    12187   6529  10298  -2242  -1088  -3310       C
ATOM    846  N   VAL A 107       1.978 -30.199  32.987  1.00 82.86           N
ANISOU  846  N   VAL A 107    12858   6578  12046  -2586  -1039  -2831       N
ATOM    847  CA  VAL A 107       1.154 -31.304  33.464  1.00 81.83           C
ANISOU  847  CA  VAL A 107    12646   6238  12207  -2725  -1064  -2809       C
ATOM    848  C   VAL A 107      -0.243 -31.088  32.902  1.00 82.31           C
ANISOU  848  C   VAL A 107    12614   6435  12224  -2865  -1166  -2898       C
ATOM    849  O   VAL A 107      -0.673 -29.942  32.720  1.00 82.99           O
ANISOU  849  O   VAL A 107    12690   6764  12077  -2876  -1192  -2848       O
ATOM    850  CB  VAL A 107       1.155 -31.382  35.010  1.00 84.61           C
ANISOU  850  CB  VAL A 107    12983   6470  12696  -2771   -978  -2501       C
ATOM    851  CG1 VAL A 107       2.586 -31.412  35.554  1.00 77.62           C
ANISOU  851  CG1 VAL A 107    12189   5489  11813  -2617   -885  -2400       C
ATOM    852  CG2 VAL A 107       0.369 -30.236  35.637  1.00 79.29           C
ANISOU  852  CG2 VAL A 107    12267   5999  11862  -2849   -977  -2300       C
ATOM    853  N   LYS A 108      -0.939 -32.161  32.545  1.00 82.30           N
ANISOU  853  N   LYS A 108    12542   6289  12440  -2969  -1221  -3047       N
ATOM    854  CA  LYS A 108      -2.313 -31.945  32.123  1.00 89.18           C
ANISOU  854  CA  LYS A 108    13313   7289  13282  -3108  -1320  -3108       C
ATOM    855  C   LYS A 108      -3.220 -32.098  33.355  1.00 87.93           C
ANISOU  855  C   LYS A 108    13068   7053  13290  -3262  -1275  -2864       C
ATOM    856  O   LYS A 108      -2.748 -32.223  34.491  1.00 81.00           O
ANISOU  856  O   LYS A 108    12218   6055  12504  -3246  -1175  -2641       O
ATOM    857  CB  LYS A 108      -2.648 -32.811  30.895  1.00 92.72           C
ANISOU  857  CB  LYS A 108    13732   7720  13777  -3119  -1405  -3389       C
ATOM    858  CG  LYS A 108      -2.319 -32.014  29.575  1.00 94.32           C
ANISOU  858  CG  LYS A 108    13994   8158  13685  -2996  -1512  -3581       C
ATOM    859  CD  LYS A 108      -1.862 -32.842  28.370  1.00 95.90           C
ANISOU  859  CD  LYS A 108    14274   8295  13867  -2885  -1639  -3815       C
ATOM    860  CE  LYS A 108      -2.363 -32.231  27.055  1.00 98.47           C
ANISOU  860  CE  LYS A 108    14654   8857  13903  -2871  -1800  -3967       C
ATOM    861  NZ  LYS A 108      -2.624 -33.233  25.979  1.00 92.71           N
ANISOU  861  NZ  LYS A 108    14275   8022  12928  -3017  -1918  -4044       N
ATOM    862  N   ARG A 109      -4.535 -32.022  33.131  1.00 91.20           N
ANISOU  862  N   ARG A 109    13371   7556  13723  -3405  -1352  -2897       N
ATOM    863  CA  ARG A 109      -5.432 -31.408  34.109  1.00 87.76           C
ANISOU  863  CA  ARG A 109    12855   7211  13277  -3513  -1333  -2646       C
ATOM    864  C   ARG A 109      -5.421 -32.096  35.471  1.00 87.53           C
ANISOU  864  C   ARG A 109    12805   6973  13478  -3581  -1222  -2413       C
ATOM    865  O   ARG A 109      -5.339 -31.409  36.498  1.00 87.77           O
ANISOU  865  O   ARG A 109    12838   7071  13439  -3569  -1161  -2158       O
ATOM    866  CB  ARG A 109      -6.855 -31.336  33.564  1.00 91.78           C
ANISOU  866  CB  ARG A 109    13237   7840  13795  -3656  -1439  -2743       C
ATOM    867  CG  ARG A 109      -7.671 -30.221  34.198  1.00 81.78           C
ANISOU  867  CG  ARG A 109    11898   6781  12395  -3721  -1440  -2531       C
ATOM    868  CD  ARG A 109      -8.990 -30.009  33.476  1.00 79.23           C
ANISOU  868  CD  ARG A 109    11451   6612  12041  -3835  -1559  -2650       C
ATOM    869  NE  ARG A 109      -9.794 -28.996  34.141  1.00 82.29           N
ANISOU  869  NE  ARG A 109    11754   7187  12324  -3901  -1547  -2445       N
ATOM    870  CZ  ARG A 109     -10.428 -29.199  35.290  1.00 83.22           C
ANISOU  870  CZ  ARG A 109    11786   7237  12598  -4011  -1483  -2231       C
ATOM    871  NH1 ARG A 109     -10.433 -30.388  35.873  1.00 82.63           N
ANISOU  871  NH1 ARG A 109    11693   6914  12788  -4081  -1424  -2190       N
ATOM    872  NH2 ARG A 109     -11.072 -28.187  35.865  1.00 81.76           N
ANISOU  872  NH2 ARG A 109    11526   7243  12296  -4054  -1467  -2055       N
ATOM    873  N   GLU A 110      -5.526 -33.438  35.509  1.00 90.53           N
ANISOU  873  N   GLU A 110    13176   7116  14106  -3665  -1172  -2495       N
ATOM    874  CA  GLU A 110      -5.827 -34.092  36.782  1.00 92.40           C
ANISOU  874  CA  GLU A 110    13387   7186  14535  -3771  -1064  -2258       C
ATOM    875  C   GLU A 110      -4.726 -33.875  37.809  1.00 91.73           C
ANISOU  875  C   GLU A 110    13379   7034  14442  -3644   -973  -2028       C
ATOM    876  O   GLU A 110      -5.001 -33.943  39.012  1.00 94.10           O
ANISOU  876  O   GLU A 110    13642   7289  14824  -3703   -901  -1767       O
ATOM    877  CB  GLU A 110      -6.034 -35.625  36.728  1.00 98.75           C
ANISOU  877  CB  GLU A 110    14266   7765  15489  -3900   -996  -2321       C
ATOM    878  CG  GLU A 110      -4.733 -36.453  36.889  1.00101.61           C
ANISOU  878  CG  GLU A 110    14813   7914  15880  -3805   -912  -2311       C
ATOM    879  CD  GLU A 110      -4.944 -37.964  37.098  1.00113.01           C
ANISOU  879  CD  GLU A 110    16388   9088  17464  -3948   -906  -2280       C
ATOM    880  OE1 GLU A 110      -6.035 -38.499  36.796  1.00116.89           O
ANISOU  880  OE1 GLU A 110    16846   9553  18015  -4123   -977  -2342       O
ATOM    881  OE2 GLU A 110      -4.009 -38.612  37.636  1.00117.34           O
ANISOU  881  OE2 GLU A 110    17053   9439  18092  -3876   -846  -2179       O
ATOM    882  N   ALA A 111      -3.495 -33.613  37.371  1.00 91.56           N
ANISOU  882  N   ALA A 111    13460   7015  14312  -3472   -971  -2115       N
ATOM    883  CA  ALA A 111      -2.346 -33.513  38.259  1.00 88.62           C
ANISOU  883  CA  ALA A 111    13170   6567  13936  -3346   -883  -1924       C
ATOM    884  C   ALA A 111      -2.138 -32.114  38.838  1.00 86.58           C
ANISOU  884  C   ALA A 111    12925   6531  13440  -3275   -880  -1729       C
ATOM    885  O   ALA A 111      -1.238 -31.932  39.663  1.00 94.29           O
ANISOU  885  O   ALA A 111    13962   7470  14393  -3179   -803  -1553       O
ATOM    886  CB  ALA A 111      -1.087 -33.962  37.514  1.00 83.35           C
ANISOU  886  CB  ALA A 111    12610   5793  13267  -3200   -864  -2117       C
ATOM    887  N   ALA A 112      -2.951 -31.132  38.449  1.00 87.35           N
ANISOU  887  N   ALA A 112    12972   6862  13355  -3328   -946  -1757       N
ATOM    888  CA  ALA A 112      -2.766 -29.752  38.884  1.00 81.13           C
ANISOU  888  CA  ALA A 112    12210   6298  12316  -3273   -918  -1606       C
ATOM    889  C   ALA A 112      -3.676 -29.448  40.064  1.00 81.01           C
ANISOU  889  C   ALA A 112    12098   6343  12339  -3391   -877  -1352       C
ATOM    890  O   ALA A 112      -4.908 -29.455  39.898  1.00 79.56           O
ANISOU  890  O   ALA A 112    11805   6226  12197  -3526   -930  -1376       O
ATOM    891  CB  ALA A 112      -3.058 -28.796  37.734  1.00 78.35           C
ANISOU  891  CB  ALA A 112    11864   6179  11725  -3252   -999  -1787       C
ATOM    892  N   PRO A 113      -3.136 -29.172  41.257  1.00 78.32           N
ANISOU  892  N   PRO A 113    11784   5992  11981  -3343   -784  -1109       N
ATOM    893  CA  PRO A 113      -4.009 -28.916  42.414  1.00 73.15           C
ANISOU  893  CA  PRO A 113    11029   5406  11358  -3453   -736   -866       C
ATOM    894  C   PRO A 113      -4.892 -27.694  42.255  1.00 75.09           C
ANISOU  894  C   PRO A 113    11206   5916  11409  -3512   -772   -857       C
ATOM    895  O   PRO A 113      -5.918 -27.601  42.935  1.00 75.01           O
ANISOU  895  O   PRO A 113    11080   5970  11449  -3631   -755   -717       O
ATOM    896  CB  PRO A 113      -3.013 -28.743  43.567  1.00 73.86           C
ANISOU  896  CB  PRO A 113    11183   5462  11418  -3352   -635   -642       C
ATOM    897  CG  PRO A 113      -1.778 -29.452  43.107  1.00 72.85           C
ANISOU  897  CG  PRO A 113    11164   5151  11363  -3226   -630   -759       C
ATOM    898  CD  PRO A 113      -1.716 -29.168  41.637  1.00 74.11           C
ANISOU  898  CD  PRO A 113    11365   5380  11412  -3189   -716  -1044       C
ATOM    899  N   CYS A 114      -4.523 -26.742  41.393  1.00 75.92           N
ANISOU  899  N   CYS A 114    11373   6181  11294  -3431   -813   -998       N
ATOM    900  CA  CYS A 114      -5.375 -25.583  41.155  1.00 75.37           C
ANISOU  900  CA  CYS A 114    11232   6360  11047  -3485   -851  -1001       C
ATOM    901  C   CYS A 114      -6.678 -25.962  40.467  1.00 77.22           C
ANISOU  901  C   CYS A 114    11348   6622  11370  -3621   -945  -1128       C
ATOM    902  O   CYS A 114      -7.608 -25.151  40.443  1.00 80.45           O
ANISOU  902  O   CYS A 114    11662   7223  11681  -3693   -976  -1099       O
ATOM    903  CB  CYS A 114      -4.626 -24.521  40.330  1.00 76.58           C
ANISOU  903  CB  CYS A 114    11479   6669  10949  -3360   -871  -1124       C
ATOM    904  SG  CYS A 114      -4.461 -24.785  38.515  1.00 71.43           S
ANISOU  904  SG  CYS A 114    10877   6029  10232  -3310   -982  -1457       S
ATOM    905  N   LYS A 115      -6.769 -27.173  39.930  1.00 76.70           N
ANISOU  905  N   LYS A 115    11279   6368  11496  -3658   -991  -1269       N
ATOM    906  CA  LYS A 115      -7.959 -27.666  39.255  1.00 80.30           C
ANISOU  906  CA  LYS A 115    11623   6826  12061  -3788  -1083  -1407       C
ATOM    907  C   LYS A 115      -8.839 -28.545  40.149  1.00 78.57           C
ANISOU  907  C   LYS A 115    11288   6476  12090  -3931  -1046  -1263       C
ATOM    908  O   LYS A 115      -9.718 -29.242  39.632  1.00 78.26           O
ANISOU  908  O   LYS A 115    11160   6377  12197  -4042  -1111  -1386       O
ATOM    909  CB  LYS A 115      -7.548 -28.440  38.003  1.00 81.18           C
ANISOU  909  CB  LYS A 115    11795   6823  12226  -3743  -1159  -1685       C
ATOM    910  CG  LYS A 115      -6.570 -27.691  37.104  1.00 77.44           C
ANISOU  910  CG  LYS A 115    11441   6469  11512  -3590  -1182  -1828       C
ATOM    911  CD  LYS A 115      -7.299 -26.710  36.198  1.00 76.73           C
ANISOU  911  CD  LYS A 115    11298   6638  11217  -3611  -1273  -1941       C
ATOM    912  CE  LYS A 115      -6.358 -26.084  35.178  1.00 80.19           C
ANISOU  912  CE  LYS A 115    11851   7194  11425  -3463  -1295  -2100       C
ATOM    913  NZ  LYS A 115      -7.072 -25.216  34.202  1.00 78.07           N
ANISOU  913  NZ  LYS A 115    11527   7175  10962  -3480  -1391  -2217       N
ATOM    914  N   GLU A 116      -8.624 -28.535  41.472  1.00 77.98           N
ANISOU  914  N   GLU A 116    11207   6360  12060  -3932   -938  -1006       N
ATOM    915  CA  GLU A 116      -9.400 -29.407  42.356  1.00 81.37           C
ANISOU  915  CA  GLU A 116    11532   6667  12719  -4061   -885   -854       C
ATOM    916  C   GLU A 116     -10.884 -29.040  42.346  1.00 78.96           C
ANISOU  916  C   GLU A 116    11064   6520  12419  -4206   -927   -835       C
ATOM    917  O   GLU A 116     -11.746 -29.916  42.236  1.00 78.77           O
ANISOU  917  O   GLU A 116    10945   6393  12591  -4333   -948   -880       O
ATOM    918  CB  GLU A 116      -8.839 -29.356  43.781  1.00 78.58           C
ANISOU  918  CB  GLU A 116    11205   6280  12373  -4018   -760   -574       C
ATOM    919  CG  GLU A 116      -7.621 -30.251  44.039  1.00 73.37           C
ANISOU  919  CG  GLU A 116    10664   5386  11828  -3920   -704   -553       C
ATOM    920  CD  GLU A 116      -6.801 -29.818  45.271  1.00 83.12           C
ANISOU  920  CD  GLU A 116    11952   6653  12976  -3827   -600   -301       C
ATOM    921  OE1 GLU A 116      -7.358 -29.162  46.180  1.00 86.30           O
ANISOU  921  OE1 GLU A 116    12277   7215  13299  -3873   -547   -106       O
ATOM    922  OE2 GLU A 116      -5.586 -30.117  45.325  1.00 81.89           O
ANISOU  922  OE2 GLU A 116    11912   6376  12828  -3702   -569   -304       O
ATOM    923  N   ASN A 117     -11.207 -27.758  42.438  1.00 80.41           N
ANISOU  923  N   ASN A 117    11208   6951  12392  -4190   -936   -776       N
ATOM    924  CA  ASN A 117     -12.594 -27.317  42.427  1.00 82.31           C
ANISOU  924  CA  ASN A 117    11285   7361  12628  -4314   -975   -756       C
ATOM    925  C   ASN A 117     -12.801 -26.366  41.259  1.00 80.16           C
ANISOU  925  C   ASN A 117    11014   7287  12157  -4278  -1083   -945       C
ATOM    926  O   ASN A 117     -11.893 -25.623  40.878  1.00 83.66           O
ANISOU  926  O   ASN A 117    11574   7807  12407  -4151  -1088   -999       O
ATOM    927  CB  ASN A 117     -12.980 -26.614  43.742  1.00 81.63           C
ANISOU  927  CB  ASN A 117    11116   7417  12481  -4342   -872   -488       C
ATOM    928  CG  ASN A 117     -12.686 -27.459  44.965  1.00 83.03           C
ANISOU  928  CG  ASN A 117    11300   7428  12817  -4360   -755   -277       C
ATOM    929  OD1 ASN A 117     -11.531 -27.581  45.378  1.00 85.41           O
ANISOU  929  OD1 ASN A 117    11729   7636  13089  -4251   -696   -209       O
ATOM    930  ND2 ASN A 117     -13.726 -28.023  45.568  1.00 79.20           N
ANISOU  930  ND2 ASN A 117    10678   6920  12496  -4494   -717   -167       N
ATOM    931  N   VAL A 118     -13.997 -26.390  40.684  1.00 80.99           N
ANISOU  931  N   VAL A 118    10985   7477  12309  -4387  -1170  -1043       N
ATOM    932  CA  VAL A 118     -14.329 -25.533  39.554  1.00 84.44           C
ANISOU  932  CA  VAL A 118    11403   8114  12566  -4359  -1282  -1216       C
ATOM    933  C   VAL A 118     -15.605 -24.774  39.881  1.00 85.62           C
ANISOU  933  C   VAL A 118    11375   8474  12681  -4454  -1295  -1118       C
ATOM    934  O   VAL A 118     -16.636 -25.384  40.183  1.00 85.75           O
ANISOU  934  O   VAL A 118    11254   8450  12879  -4584  -1299  -1078       O
ATOM    935  CB  VAL A 118     -14.485 -26.346  38.254  1.00 85.19           C
ANISOU  935  CB  VAL A 118    11510   8117  12742  -4381  -1402  -1486       C
ATOM    936  CG1 VAL A 118     -15.351 -25.611  37.250  1.00 87.78           C
ANISOU  936  CG1 VAL A 118    11746   8670  12937  -4407  -1526  -1626       C
ATOM    937  CG2 VAL A 118     -13.125 -26.606  37.654  1.00 81.60           C
ANISOU  937  CG2 VAL A 118    11236   7550  12217  -4244  -1403  -1620       C
ATOM    938  N   ILE A 119     -15.549 -23.452  39.818  1.00 82.34           N
ANISOU  938  N   ILE A 119    10957   8286  12044  -4388  -1297  -1082       N
ATOM    939  CA  ILE A 119     -16.757 -22.656  39.956  1.00 85.91           C
ANISOU  939  CA  ILE A 119    11233   8954  12453  -4462  -1324  -1020       C
ATOM    940  C   ILE A 119     -17.068 -22.002  38.623  1.00 90.31           C
ANISOU  940  C   ILE A 119    11773   9682  12860  -4428  -1460  -1215       C
ATOM    941  O   ILE A 119     -16.226 -21.366  37.985  1.00 87.71           O
ANISOU  941  O   ILE A 119    11564   9421  12342  -4309  -1487  -1300       O
ATOM    942  CB  ILE A 119     -16.701 -21.622  41.093  1.00 84.83           C
ANISOU  942  CB  ILE A 119    11059   8965  12209  -4432  -1212   -799       C
ATOM    943  CG1 ILE A 119     -16.289 -22.315  42.382  1.00 82.88           C
ANISOU  943  CG1 ILE A 119    10843   8555  12091  -4450  -1078   -607       C
ATOM    944  CG2 ILE A 119     -18.070 -21.030  41.301  1.00 82.45           C
ANISOU  944  CG2 ILE A 119    10550   8860  11918  -4522  -1232   -737       C
ATOM    945  CD1 ILE A 119     -16.099 -21.425  43.505  1.00 86.30           C
ANISOU  945  CD1 ILE A 119    11256   9116  12418  -4410   -964   -404       C
ATOM    946  N   ASP A 120     -18.303 -22.185  38.224  1.00 85.25           N
ANISOU  946  N   ASP A 120    10974   9112  12307  -4532  -1544  -1276       N
ATOM    947  CA  ASP A 120     -18.707 -22.288  36.844  1.00 89.33           C
ANISOU  947  CA  ASP A 120    11468   9690  12784  -4536  -1694  -1504       C
ATOM    948  C   ASP A 120     -20.075 -21.660  36.644  1.00 94.19           C
ANISOU  948  C   ASP A 120    11884  10518  13387  -4611  -1768  -1493       C
ATOM    949  O   ASP A 120     -20.457 -21.293  35.528  1.00 99.40           O
ANISOU  949  O   ASP A 120    12509  11315  13944  -4588  -1896  -1647       O
ATOM    950  CB  ASP A 120     -18.611 -23.774  36.580  1.00 99.49           C
ANISOU  950  CB  ASP A 120    12794  10725  14284  -4598  -1717  -1624       C
ATOM    951  CG  ASP A 120     -19.484 -24.560  37.533  1.00105.66           C
ANISOU  951  CG  ASP A 120    13439  11392  15313  -4742  -1655  -1491       C
ATOM    952  OD1 ASP A 120     -19.815 -25.719  37.244  1.00120.10           O
ANISOU  952  OD1 ASP A 120    15239  13049  17344  -4827  -1693  -1598       O
ATOM    953  OD2 ASP A 120     -19.869 -23.975  38.584  1.00113.50           O
ANISOU  953  OD2 ASP A 120    14346  12482  16296  -4769  -1563  -1279       O
ATOM    954  N   LYS A 121     -20.810 -21.578  37.745  1.00 94.72           N
ANISOU  954  N   LYS A 121    11815  10611  13563  -4695  -1684  -1305       N
ATOM    955  CA  LYS A 121     -22.130 -20.982  37.843  1.00 94.09           C
ANISOU  955  CA  LYS A 121    11525  10727  13498  -4767  -1721  -1251       C
ATOM    956  C   LYS A 121     -22.137 -20.007  39.007  1.00 88.52           C
ANISOU  956  C   LYS A 121    10764  10152  12717  -4738  -1597  -1029       C
ATOM    957  O   LYS A 121     -21.505 -20.261  40.037  1.00 88.94           O
ANISOU  957  O   LYS A 121    10890  10092  12812  -4728  -1466   -884       O
ATOM    958  CB  LYS A 121     -23.251 -22.011  38.095  1.00 89.40           C
ANISOU  958  CB  LYS A 121    10777  10034  13159  -4923  -1732  -1248       C
ATOM    959  CG  LYS A 121     -23.806 -22.745  36.897  1.00 95.88           C
ANISOU  959  CG  LYS A 121    11557  10806  14066  -4983  -1883  -1475       C
ATOM    960  CD  LYS A 121     -23.629 -24.233  36.991  1.00 96.08           C
ANISOU  960  CD  LYS A 121    11631  10555  14321  -5064  -1862  -1539       C
ATOM    961  CE  LYS A 121     -23.818 -24.865  35.622  1.00101.54           C
ANISOU  961  CE  LYS A 121    12334  11200  15047  -5083  -2018  -1810       C
ATOM    962  NZ  LYS A 121     -23.812 -26.355  35.692  1.00103.06           N
ANISOU  962  NZ  LYS A 121    12541  11122  15494  -5181  -1999  -1890       N
ATOM    963  N   ASP A 122     -22.881 -18.910  38.848  1.00 85.98           N
ANISOU  963  N   ASP A 122    10304  10072  12291  -4722  -1639  -1004       N
ATOM    964  CA  ASP A 122     -23.122 -17.957  39.931  1.00 86.48           C
ANISOU  964  CA  ASP A 122    10271  10285  12303  -4704  -1528   -809       C
ATOM    965  C   ASP A 122     -21.817 -17.595  40.640  1.00 80.49           C
ANISOU  965  C   ASP A 122     9679   9472  11434  -4577  -1401   -706       C
ATOM    966  O   ASP A 122     -21.707 -17.675  41.864  1.00 78.70           O
ANISOU  966  O   ASP A 122     9433   9208  11260  -4585  -1261   -533       O
ATOM    967  CB  ASP A 122     -24.150 -18.506  40.924  1.00 84.24           C
ANISOU  967  CB  ASP A 122     9814   9978  12216  -4830  -1446   -672       C
ATOM    968  CG  ASP A 122     -25.471 -18.851  40.264  1.00 91.61           C
ANISOU  968  CG  ASP A 122    10569  10967  13270  -4930  -1559   -770       C
ATOM    969  OD1 ASP A 122     -26.049 -17.958  39.606  1.00 94.96           O
ANISOU  969  OD1 ASP A 122    10893  11594  13593  -4893  -1654   -831       O
ATOM    970  OD2 ASP A 122     -25.933 -20.008  40.405  1.00 95.74           O
ANISOU  970  OD2 ASP A 122    11048  11332  13995  -5043  -1555   -784       O
ATOM    971  N   ILE A 123     -20.813 -17.226  39.839  1.00 78.23           N
ANISOU  971  N   ILE A 123     9553   9182  10989  -4431  -1444   -816       N
ATOM    972  CA  ILE A 123     -19.483 -16.941  40.363  1.00 76.45           C
ANISOU  972  CA  ILE A 123     9494   8892  10661  -4276  -1330   -743       C
ATOM    973  C   ILE A 123     -19.569 -15.840  41.408  1.00 75.29           C
ANISOU  973  C   ILE A 123     9266   8905  10437  -4173  -1206   -567       C
ATOM    974  O   ILE A 123     -20.156 -14.780  41.162  1.00 78.82           O
ANISOU  974  O   ILE A 123     9598   9556  10794  -4110  -1238   -566       O
ATOM    975  CB  ILE A 123     -18.547 -16.550  39.209  1.00 78.50           C
ANISOU  975  CB  ILE A 123     9906   9169  10750  -4136  -1406   -895       C
ATOM    976  CG1 ILE A 123     -18.130 -17.793  38.417  1.00 78.01           C
ANISOU  976  CG1 ILE A 123     9968   8902  10768  -4219  -1489  -1062       C
ATOM    977  CG2 ILE A 123     -17.348 -15.770  39.723  1.00 66.07           C
ANISOU  977  CG2 ILE A 123     8453   7616   9034  -3946  -1293   -804       C
ATOM    978  CD1 ILE A 123     -17.858 -17.515  36.973  1.00 77.38           C
ANISOU  978  CD1 ILE A 123     9959   8899  10544  -4149  -1619  -1257       C
ATOM    979  N   ASN A 124     -18.988 -16.088  42.583  1.00 71.49           N
ANISOU  979  N   ASN A 124     8839   8333   9990  -4155  -1067   -420       N
ATOM    980  CA  ASN A 124     -18.976 -15.105  43.668  1.00 72.94           C
ANISOU  980  CA  ASN A 124     8958   8661  10097  -4055   -939   -261       C
ATOM    981  C   ASN A 124     -17.583 -15.091  44.293  1.00 68.47           C
ANISOU  981  C   ASN A 124     8565   7995   9456  -3930   -835   -191       C
ATOM    982  O   ASN A 124     -17.212 -16.031  44.995  1.00 69.87           O
ANISOU  982  O   ASN A 124     8804   8010   9732  -3999   -768   -110       O
ATOM    983  CB  ASN A 124     -20.063 -15.429  44.692  1.00 72.83           C
ANISOU  983  CB  ASN A 124     8767   8686  10219  -4196   -867   -123       C
ATOM    984  CG  ASN A 124     -20.125 -14.427  45.844  1.00 75.52           C
ANISOU  984  CG  ASN A 124     9028   9191  10477  -4096   -732     29       C
ATOM    985  OD1 ASN A 124     -19.225 -13.590  46.040  1.00 68.02           O
ANISOU  985  OD1 ASN A 124     8172   8292   9382  -3925   -680     47       O
ATOM    986  ND2 ASN A 124     -21.205 -14.505  46.610  1.00 73.10           N
ANISOU  986  ND2 ASN A 124     8540   8970  10264  -4205   -675    134       N
ATOM    987  N   LEU A 125     -16.814 -14.023  44.032  1.00 68.73           N
ANISOU  987  N   LEU A 125     8671   8124   9318  -3749   -825   -216       N
ATOM    988  CA  LEU A 125     -15.445 -13.953  44.542  1.00 66.46           C
ANISOU  988  CA  LEU A 125     8547   7752   8955  -3624   -737   -162       C
ATOM    989  C   LEU A 125     -15.395 -14.014  46.060  1.00 64.21           C
ANISOU  989  C   LEU A 125     8224   7468   8704  -3635   -594     22       C
ATOM    990  O   LEU A 125     -14.417 -14.508  46.628  1.00 61.77           O
ANISOU  990  O   LEU A 125     8041   7029   8400  -3600   -525     85       O
ATOM    991  CB  LEU A 125     -14.747 -12.681  44.064  1.00 65.95           C
ANISOU  991  CB  LEU A 125     8538   7810   8711  -3435   -746   -208       C
ATOM    992  CG  LEU A 125     -14.340 -12.573  42.600  1.00 65.37           C
ANISOU  992  CG  LEU A 125     8554   7727   8557  -3382   -867   -374       C
ATOM    993  CD1 LEU A 125     -14.244 -11.121  42.199  1.00 65.72           C
ANISOU  993  CD1 LEU A 125     8566   7954   8451  -3232   -883   -385       C
ATOM    994  CD2 LEU A 125     -13.012 -13.254  42.396  1.00 64.83           C
ANISOU  994  CD2 LEU A 125     8680   7480   8473  -3331   -849   -420       C
ATOM    995  N   PHE A 126     -16.434 -13.518  46.730  1.00 66.69           N
ANISOU  995  N   PHE A 126     8363   7935   9039  -3678   -547    109       N
ATOM    996  CA  PHE A 126     -16.423 -13.466  48.187  1.00 63.55           C
ANISOU  996  CA  PHE A 126     7921   7577   8648  -3679   -405    282       C
ATOM    997  C   PHE A 126     -16.535 -14.848  48.817  1.00 66.96           C
ANISOU  997  C   PHE A 126     8367   7841   9232  -3835   -363    378       C
ATOM    998  O   PHE A 126     -16.102 -15.034  49.959  1.00 69.73           O
ANISOU  998  O   PHE A 126     8747   8171   9575  -3820   -248    523       O
ATOM    999  CB  PHE A 126     -17.547 -12.558  48.686  1.00 63.92           C
ANISOU  999  CB  PHE A 126     7768   7845   8676  -3681   -365    336       C
ATOM   1000  CG  PHE A 126     -17.325 -11.103  48.398  1.00 61.21           C
ANISOU 1000  CG  PHE A 126     7410   7662   8186  -3508   -375    283       C
ATOM   1001  CD1 PHE A 126     -17.625 -10.577  47.152  1.00 63.61           C
ANISOU 1001  CD1 PHE A 126     7691   8022   8456  -3472   -499    151       C
ATOM   1002  CD2 PHE A 126     -16.766 -10.267  49.359  1.00 62.10           C
ANISOU 1002  CD2 PHE A 126     7536   7864   8194  -3378   -265    365       C
ATOM   1003  CE1 PHE A 126     -17.400  -9.250  46.879  1.00 63.38           C
ANISOU 1003  CE1 PHE A 126     7650   8127   8306  -3313   -509    116       C
ATOM   1004  CE2 PHE A 126     -16.532  -8.920  49.086  1.00 52.51           C
ANISOU 1004  CE2 PHE A 126     6311   6779   6863  -3219   -277    314       C
ATOM   1005  CZ  PHE A 126     -16.850  -8.420  47.854  1.00 58.85           C
ANISOU 1005  CZ  PHE A 126     7088   7625   7646  -3188   -397    197       C
ATOM   1006  N   GLU A 127     -17.122 -15.818  48.107  1.00 71.30           N
ANISOU 1006  N   GLU A 127     8895   8272   9926  -3986   -455    303       N
ATOM   1007  CA  GLU A 127     -17.182 -17.196  48.610  1.00 74.75           C
ANISOU 1007  CA  GLU A 127     9355   8516  10532  -4139   -425    390       C
ATOM   1008  C   GLU A 127     -15.817 -17.908  48.514  1.00 72.95           C
ANISOU 1008  C   GLU A 127     9336   8071  10310  -4081   -421    374       C
ATOM   1009  O   GLU A 127     -15.671 -18.968  49.112  1.00 75.38           O
ANISOU 1009  O   GLU A 127     9680   8213  10749  -4178   -377    476       O
ATOM   1010  CB  GLU A 127     -18.261 -17.997  47.866  1.00 73.19           C
ANISOU 1010  CB  GLU A 127     9058   8250  10501  -4325   -530    303       C
ATOM   1011  CG  GLU A 127     -19.642 -17.939  48.513  1.00 75.99           C
ANISOU 1011  CG  GLU A 127     9194   8738  10943  -4457   -487    409       C
ATOM   1012  CD  GLU A 127     -20.736 -18.244  47.520  1.00 82.14           C
ANISOU 1012  CD  GLU A 127     9853   9525  11831  -4592   -619    278       C
ATOM   1013  OE1 GLU A 127     -20.463 -18.981  46.542  1.00 86.67           O
ANISOU 1013  OE1 GLU A 127    10523   9934  12475  -4643   -731    134       O
ATOM   1014  OE2 GLU A 127     -21.858 -17.724  47.698  1.00 89.82           O
ANISOU 1014  OE2 GLU A 127    10635  10677  12818  -4643   -613    310       O
ATOM   1015  N   ILE A 128     -14.841 -17.304  47.809  1.00 67.38           N
ANISOU 1015  N   ILE A 128     8760   7374   9469  -3922   -462    259       N
ATOM   1016  CA  ILE A 128     -13.529 -17.870  47.647  1.00 68.61           C
ANISOU 1016  CA  ILE A 128     9104   7344   9619  -3849   -459    229       C
ATOM   1017  C   ILE A 128     -12.572 -17.232  48.643  1.00 66.26           C
ANISOU 1017  C   ILE A 128     8872   7108   9196  -3702   -345    356       C
ATOM   1018  O   ILE A 128     -12.113 -17.863  49.594  1.00 72.84           O
ANISOU 1018  O   ILE A 128     9753   7839  10084  -3723   -265    497       O
ATOM   1019  CB  ILE A 128     -12.947 -17.669  46.230  1.00 69.12           C
ANISOU 1019  CB  ILE A 128     9277   7376   9609  -3764   -570     21       C
ATOM   1020  CG1 ILE A 128     -14.027 -17.583  45.148  1.00 69.09           C
ANISOU 1020  CG1 ILE A 128     9170   7448   9634  -3853   -692   -124       C
ATOM   1021  CG2 ILE A 128     -11.937 -18.719  45.893  1.00 65.66           C
ANISOU 1021  CG2 ILE A 128     9006   6697   9246  -3760   -591    -38       C
ATOM   1022  CD1 ILE A 128     -14.806 -18.811  44.918  1.00 75.96           C
ANISOU 1022  CD1 ILE A 128     9991   8170  10703  -4048   -753   -161       C
ATOM   1023  N   LEU A 129     -12.317 -15.929  48.467  1.00 59.85           N
ANISOU 1023  N   LEU A 129     8051   6474   8216  -3555   -339    315       N
ATOM   1024  CA  LEU A 129     -11.345 -14.983  48.956  1.00 61.35           C
ANISOU 1024  CA  LEU A 129     8307   6751   8251  -3381   -270    359       C
ATOM   1025  C   LEU A 129     -11.960 -14.128  50.046  1.00 59.64           C
ANISOU 1025  C   LEU A 129     7955   6732   7972  -3362   -178    484       C
ATOM   1026  O   LEU A 129     -13.004 -13.490  49.819  1.00 59.94           O
ANISOU 1026  O   LEU A 129     7852   6923   8001  -3392   -204    451       O
ATOM   1027  CB  LEU A 129     -10.891 -14.090  47.802  1.00 60.08           C
ANISOU 1027  CB  LEU A 129     8201   6658   7968  -3254   -347    204       C
ATOM   1028  CG  LEU A 129     -10.403 -14.791  46.529  1.00 58.03           C
ANISOU 1028  CG  LEU A 129     8060   6245   7745  -3266   -449     47       C
ATOM   1029  CD1 LEU A 129     -10.160 -13.706  45.473  1.00 54.98           C
ANISOU 1029  CD1 LEU A 129     7691   5984   7215  -3143   -515    -80       C
ATOM   1030  CD2 LEU A 129      -9.160 -15.639  46.780  1.00 54.00           C
ANISOU 1030  CD2 LEU A 129     7710   5537   7272  -3228   -412     71       C
ATOM   1031  N   PRO A 130     -11.387 -14.122  51.219  1.00 56.02           N
ANISOU 1031  N   PRO A 130     7529   6282   7475  -3316    -73    623       N
ATOM   1032  CA  PRO A 130     -11.784 -13.127  52.217  1.00 58.06           C
ANISOU 1032  CA  PRO A 130     7673   6748   7637  -3261     17    714       C
ATOM   1033  C   PRO A 130     -11.286 -11.741  51.820  1.00 55.78           C
ANISOU 1033  C   PRO A 130     7404   6587   7202  -3090      1    623       C
ATOM   1034  O   PRO A 130     -10.211 -11.309  52.245  1.00 60.03           O
ANISOU 1034  O   PRO A 130     8037   7128   7645  -2964     46    648       O
ATOM   1035  CB  PRO A 130     -11.143 -13.654  53.506  1.00 59.50           C
ANISOU 1035  CB  PRO A 130     7911   6882   7814  -3259    122    880       C
ATOM   1036  CG  PRO A 130     -10.774 -15.118  53.185  1.00 57.10           C
ANISOU 1036  CG  PRO A 130     7712   6330   7655  -3360     82    895       C
ATOM   1037  CD  PRO A 130     -10.460 -15.132  51.749  1.00 54.61           C
ANISOU 1037  CD  PRO A 130     7477   5920   7352  -3328    -33    711       C
ATOM   1038  N   LEU A 131     -12.044 -11.065  50.952  1.00 54.86           N
ANISOU 1038  N   LEU A 131     7199   6570   7075  -3086    -72    516       N
ATOM   1039  CA  LEU A 131     -11.667  -9.748  50.444  1.00 55.39           C
ANISOU 1039  CA  LEU A 131     7275   6748   7022  -2932   -100    432       C
ATOM   1040  C   LEU A 131     -11.900  -8.666  51.503  1.00 56.10           C
ANISOU 1040  C   LEU A 131     7264   7019   7032  -2851     -6    504       C
ATOM   1041  O   LEU A 131     -12.902  -8.695  52.231  1.00 56.69           O
ANISOU 1041  O   LEU A 131     7198   7195   7147  -2930     49    576       O
ATOM   1042  CB  LEU A 131     -12.474  -9.432  49.185  1.00 52.85           C
ANISOU 1042  CB  LEU A 131     6883   6476   6722  -2961   -213    310       C
ATOM   1043  CG  LEU A 131     -12.297 -10.370  47.994  1.00 55.99           C
ANISOU 1043  CG  LEU A 131     7373   6719   7180  -3032   -319    204       C
ATOM   1044  CD1 LEU A 131     -13.528 -10.326  47.099  1.00 54.21           C
ANISOU 1044  CD1 LEU A 131     7024   6565   7008  -3122   -420    121       C
ATOM   1045  CD2 LEU A 131     -11.024 -10.024  47.205  1.00 49.83           C
ANISOU 1045  CD2 LEU A 131     6751   5879   6303  -2897   -358    118       C
ATOM   1046  N   TYR A 132     -10.986  -7.691  51.560  1.00 53.20           N
ANISOU 1046  N   TYR A 132     6962   6696   6554  -2694     12    476       N
ATOM   1047  CA  TYR A 132     -10.967  -6.659  52.595  1.00 47.17           C
ANISOU 1047  CA  TYR A 132     6129   6083   5709  -2599    102    527       C
ATOM   1048  C   TYR A 132     -10.393  -5.365  52.034  1.00 52.50           C
ANISOU 1048  C   TYR A 132     6833   6816   6300  -2442     66    440       C
ATOM   1049  O   TYR A 132      -9.770  -5.353  50.968  1.00 50.44           O
ANISOU 1049  O   TYR A 132     6672   6469   6025  -2399    -12    362       O
ATOM   1050  CB  TYR A 132     -10.120  -7.082  53.794  1.00 51.86           C
ANISOU 1050  CB  TYR A 132     6800   6641   6262  -2579    197    634       C
ATOM   1051  CG  TYR A 132      -8.676  -7.373  53.442  1.00 49.45           C
ANISOU 1051  CG  TYR A 132     6675   6190   5922  -2502    172    611       C
ATOM   1052  CD1 TYR A 132      -8.300  -8.602  52.917  1.00 50.15           C
ANISOU 1052  CD1 TYR A 132     6869   6098   6087  -2580    127    610       C
ATOM   1053  CD2 TYR A 132      -7.689  -6.429  53.657  1.00 49.58           C
ANISOU 1053  CD2 TYR A 132     6751   6248   5837  -2353    194    587       C
ATOM   1054  CE1 TYR A 132      -6.980  -8.871  52.604  1.00 53.30           C
ANISOU 1054  CE1 TYR A 132     7424   6367   6458  -2504    109    585       C
ATOM   1055  CE2 TYR A 132      -6.362  -6.690  53.348  1.00 48.05           C
ANISOU 1055  CE2 TYR A 132     6712   5928   5616  -2282    175    568       C
ATOM   1056  CZ  TYR A 132      -6.010  -7.900  52.815  1.00 50.76           C
ANISOU 1056  CZ  TYR A 132     7155   6101   6031  -2354    134    567       C
ATOM   1057  OH  TYR A 132      -4.687  -8.147  52.491  1.00 52.61           O
ANISOU 1057  OH  TYR A 132     7535   6213   6240  -2276    118    542       O
ATOM   1058  N   ARG A 133     -10.573  -4.269  52.786  1.00 50.55           N
ANISOU 1058  N   ARG A 133     6498   6714   5995  -2355    129    455       N
ATOM   1059  CA  ARG A 133      -9.946  -2.997  52.439  1.00 54.14           C
ANISOU 1059  CA  ARG A 133     6979   7213   6380  -2201    108    388       C
ATOM   1060  C   ARG A 133      -8.519  -2.975  52.981  1.00 51.95           C
ANISOU 1060  C   ARG A 133     6839   6868   6030  -2113    154    413       C
ATOM   1061  O   ARG A 133      -8.293  -3.135  54.186  1.00 53.05           O
ANISOU 1061  O   ARG A 133     6975   7046   6136  -2112    242    488       O
ATOM   1062  CB  ARG A 133     -10.725  -1.787  52.965  1.00 52.59           C
ANISOU 1062  CB  ARG A 133     6627   7187   6168  -2138    148    375       C
ATOM   1063  CG  ARG A 133     -10.566  -0.538  52.051  1.00 46.73           C
ANISOU 1063  CG  ARG A 133     5875   6475   5406  -2016     78    290       C
ATOM   1064  CD  ARG A 133     -11.351   0.684  52.532  1.00 48.17           C
ANISOU 1064  CD  ARG A 133     5899   6809   5594  -1945    113    270       C
ATOM   1065  NE  ARG A 133     -12.807   0.511  52.515  1.00 49.18           N
ANISOU 1065  NE  ARG A 133     5864   7030   5792  -2037    105    278       N
ATOM   1066  CZ  ARG A 133     -13.591   0.624  51.452  1.00 49.41           C
ANISOU 1066  CZ  ARG A 133     5824   7073   5877  -2069     10    237       C
ATOM   1067  NH1 ARG A 133     -13.105   0.867  50.247  1.00 51.71           N
ANISOU 1067  NH1 ARG A 133     6198   7295   6155  -2023    -89    187       N
ATOM   1068  NH2 ARG A 133     -14.903   0.537  51.608  1.00 56.70           N
ANISOU 1068  NH2 ARG A 133     6582   8095   6866  -2146     15    248       N
ATOM   1069  N   ILE A 134      -7.561  -2.778  52.082  1.00 46.04           N
ANISOU 1069  N   ILE A 134     6207   6030   5254  -2039     95    354       N
ATOM   1070  CA  ILE A 134      -6.167  -2.687  52.483  1.00 47.02           C
ANISOU 1070  CA  ILE A 134     6456   6091   5317  -1948    130    370       C
ATOM   1071  C   ILE A 134      -5.855  -1.309  53.075  1.00 45.18           C
ANISOU 1071  C   ILE A 134     6177   5968   5023  -1819    172    352       C
ATOM   1072  O   ILE A 134      -5.290  -1.208  54.161  1.00 49.56           O
ANISOU 1072  O   ILE A 134     6750   6551   5529  -1778    243    397       O
ATOM   1073  CB  ILE A 134      -5.272  -3.035  51.286  1.00 47.29           C
ANISOU 1073  CB  ILE A 134     6624   5993   5350  -1921     56    313       C
ATOM   1074  CG1 ILE A 134      -5.619  -4.443  50.777  1.00 44.02           C
ANISOU 1074  CG1 ILE A 134     6253   5466   5008  -2052     17    316       C
ATOM   1075  CG2 ILE A 134      -3.795  -2.894  51.642  1.00 47.03           C
ANISOU 1075  CG2 ILE A 134     6712   5898   5260  -1821     90    326       C
ATOM   1076  CD1 ILE A 134      -4.903  -4.792  49.503  1.00 40.73           C
ANISOU 1076  CD1 ILE A 134     5954   4935   4587  -2031    -59    238       C
ATOM   1077  N   ASN A 135      -6.222  -0.216  52.418  1.00 47.95           N
ANISOU 1077  N   ASN A 135     6461   6381   5377  -1753    127    288       N
ATOM   1078  CA  ASN A 135      -5.977   1.091  53.027  1.00 47.65           C
ANISOU 1078  CA  ASN A 135     6371   6434   5301  -1635    167    265       C
ATOM   1079  C   ASN A 135      -7.256   1.907  53.085  1.00 48.27           C
ANISOU 1079  C   ASN A 135     6283   6640   5418  -1632    167    239       C
ATOM   1080  O   ASN A 135      -8.162   1.714  52.270  1.00 49.85           O
ANISOU 1080  O   ASN A 135     6422   6851   5669  -1694    107    223       O
ATOM   1081  CB  ASN A 135      -4.876   1.843  52.303  1.00 47.21           C
ANISOU 1081  CB  ASN A 135     6404   6316   5218  -1522    124    218       C
ATOM   1082  CG  ASN A 135      -3.502   1.412  52.757  1.00 44.49           C
ANISOU 1082  CG  ASN A 135     6191   5887   4825  -1486    158    245       C
ATOM   1083  OD1 ASN A 135      -3.149   1.582  53.928  1.00 47.60           O
ANISOU 1083  OD1 ASN A 135     6577   6328   5182  -1454    227    273       O
ATOM   1084  ND2 ASN A 135      -2.719   0.848  51.846  1.00 40.12           N
ANISOU 1084  ND2 ASN A 135     5757   5218   4270  -1489    110    233       N
ATOM   1085  N   GLU A 136      -7.305   2.831  54.060  1.00 56.75           N
ANISOU 1085  N   GLU A 136     7282   7814   6467  -1554    232    227       N
ATOM   1086  CA  GLU A 136      -8.474   3.671  54.381  1.00 55.21           C
ANISOU 1086  CA  GLU A 136     6918   7752   6309  -1535    253    198       C
ATOM   1087  C   GLU A 136      -9.253   4.088  53.157  1.00 54.17           C
ANISOU 1087  C   GLU A 136     6718   7622   6243  -1537    162    161       C
ATOM   1088  O   GLU A 136     -10.458   3.856  53.033  1.00 57.19           O
ANISOU 1088  O   GLU A 136     6982   8071   6675  -1611    150    168       O
ATOM   1089  CB  GLU A 136      -8.078   5.051  54.881  1.00 62.99           C
ANISOU 1089  CB  GLU A 136     7865   8791   7276  -1398    282    142       C
ATOM   1090  CG  GLU A 136      -7.171   5.303  55.995  1.00 74.08           C
ANISOU 1090  CG  GLU A 136     9320  10216   8613  -1335    355    139       C
ATOM   1091  CD  GLU A 136      -7.519   6.641  56.632  1.00 76.88           C
ANISOU 1091  CD  GLU A 136     9556  10675   8979  -1232    393     68       C
ATOM   1092  OE1 GLU A 136      -7.723   7.620  55.858  1.00 72.99           O
ANISOU 1092  OE1 GLU A 136     9016  10164   8551  -1160    336     16       O
ATOM   1093  OE2 GLU A 136      -7.523   6.738  57.872  1.00 85.50           O
ANISOU 1093  OE2 GLU A 136    10608  11862  10016  -1217    478     62       O
ATOM   1094  N   GLN A 137      -8.523   4.792  52.296  1.00 47.84           N
ANISOU 1094  N   GLN A 137     5984   6755   5438  -1448     99    125       N
ATOM   1095  CA  GLN A 137      -9.041   5.558  51.186  1.00 46.81           C
ANISOU 1095  CA  GLN A 137     5792   6637   5356  -1406     13     92       C
ATOM   1096  C   GLN A 137      -9.060   4.764  49.901  1.00 48.55           C
ANISOU 1096  C   GLN A 137     6084   6787   5577  -1479    -78     98       C
ATOM   1097  O   GLN A 137      -9.295   5.353  48.836  1.00 50.26           O
ANISOU 1097  O   GLN A 137     6276   7008   5813  -1441   -161     78       O
ATOM   1098  CB  GLN A 137      -8.204   6.834  51.016  1.00 51.16           C
ANISOU 1098  CB  GLN A 137     6373   7161   5904  -1266      2     60       C
ATOM   1099  CG  GLN A 137      -8.293   7.758  52.226  1.00 52.84           C
ANISOU 1099  CG  GLN A 137     6498   7451   6128  -1186     82     30       C
ATOM   1100  CD  GLN A 137      -9.727   8.191  52.498  1.00 54.22           C
ANISOU 1100  CD  GLN A 137     6491   7743   6366  -1196     94     12       C
ATOM   1101  OE1 GLN A 137     -10.395   8.695  51.606  1.00 54.83           O
ANISOU 1101  OE1 GLN A 137     6495   7834   6504  -1177     20      4       O
ATOM   1102  NE2 GLN A 137     -10.207   7.986  53.727  1.00 53.13           N
ANISOU 1102  NE2 GLN A 137     6277   7698   6212  -1224    186     10       N
ATOM   1103  N   ASP A 138      -8.799   3.453  49.971  1.00 46.99           N
ANISOU 1103  N   ASP A 138     5974   6522   5356  -1580    -67    123       N
ATOM   1104  CA  ASP A 138      -8.903   2.623  48.785  1.00 46.10           C
ANISOU 1104  CA  ASP A 138     5923   6345   5249  -1658   -153    110       C
ATOM   1105  C   ASP A 138     -10.319   2.715  48.221  1.00 49.68           C
ANISOU 1105  C   ASP A 138     6234   6882   5760  -1717   -217     96       C
ATOM   1106  O   ASP A 138     -11.291   2.939  48.950  1.00 49.01           O
ANISOU 1106  O   ASP A 138     6010   6892   5720  -1742   -174    111       O
ATOM   1107  CB  ASP A 138      -8.543   1.176  49.094  1.00 44.96           C
ANISOU 1107  CB  ASP A 138     5874   6110   5097  -1763   -125    138       C
ATOM   1108  CG  ASP A 138      -7.049   0.952  49.242  1.00 47.19           C
ANISOU 1108  CG  ASP A 138     6317   6290   5325  -1705    -94    145       C
ATOM   1109  OD1 ASP A 138      -6.246   1.895  49.072  1.00 41.87           O
ANISOU 1109  OD1 ASP A 138     5682   5613   4615  -1589    -95    127       O
ATOM   1110  OD2 ASP A 138      -6.673  -0.204  49.550  1.00 49.47           O
ANISOU 1110  OD2 ASP A 138     6687   6495   5615  -1778    -69    173       O
ATOM   1111  N   GLY A 139     -10.427   2.577  46.897  1.00 48.24           N
ANISOU 1111  N   GLY A 139     6082   6676   5572  -1736   -321     65       N
ATOM   1112  CA  GLY A 139     -11.732   2.663  46.268  1.00 48.82           C
ANISOU 1112  CA  GLY A 139     6021   6832   5696  -1790   -397     49       C
ATOM   1113  C   GLY A 139     -12.637   1.494  46.584  1.00 48.59           C
ANISOU 1113  C   GLY A 139     5932   6809   5719  -1942   -389     58       C
ATOM   1114  O   GLY A 139     -13.860   1.611  46.490  1.00 53.96           O
ANISOU 1114  O   GLY A 139     6463   7580   6459  -1993   -422     56       O
ATOM   1115  N   GLY A 140     -12.061   0.360  46.936  1.00 51.51           N
ANISOU 1115  N   GLY A 140     6413   7080   6080  -2018   -350     71       N
ATOM   1116  CA  GLY A 140     -12.814  -0.846  47.194  1.00 49.94           C
ANISOU 1116  CA  GLY A 140     6172   6861   5943  -2172   -345     87       C
ATOM   1117  C   GLY A 140     -11.917  -1.889  47.829  1.00 53.84           C
ANISOU 1117  C   GLY A 140     6800   7232   6425  -2218   -278    122       C
ATOM   1118  O   GLY A 140     -10.880  -1.575  48.418  1.00 51.25           O
ANISOU 1118  O   GLY A 140     6560   6870   6042  -2130   -213    146       O
ATOM   1119  N   PHE A 141     -12.334  -3.147  47.727  1.00 53.78           N
ANISOU 1119  N   PHE A 141     6802   7156   6478  -2360   -298    126       N
ATOM   1120  CA  PHE A 141     -11.514  -4.262  48.185  1.00 54.48           C
ANISOU 1120  CA  PHE A 141     7021   7106   6574  -2412   -250    161       C
ATOM   1121  C   PHE A 141     -10.618  -4.712  47.043  1.00 52.65           C
ANISOU 1121  C   PHE A 141     6942   6753   6311  -2393   -328     87       C
ATOM   1122  O   PHE A 141     -11.096  -4.901  45.920  1.00 56.09           O
ANISOU 1122  O   PHE A 141     7363   7188   6761  -2438   -428     12       O
ATOM   1123  CB  PHE A 141     -12.382  -5.429  48.658  1.00 55.16           C
ANISOU 1123  CB  PHE A 141     7040   7159   6758  -2577   -230    209       C
ATOM   1124  CG  PHE A 141     -13.448  -5.040  49.636  1.00 55.22           C
ANISOU 1124  CG  PHE A 141     6874   7306   6799  -2612   -160    276       C
ATOM   1125  CD1 PHE A 141     -13.208  -4.080  50.602  1.00 53.87           C
ANISOU 1125  CD1 PHE A 141     6665   7237   6566  -2505    -69    319       C
ATOM   1126  CD2 PHE A 141     -14.698  -5.648  49.595  1.00 57.10           C
ANISOU 1126  CD2 PHE A 141     6983   7577   7134  -2755   -182    289       C
ATOM   1127  CE1 PHE A 141     -14.195  -3.726  51.518  1.00 56.04           C
ANISOU 1127  CE1 PHE A 141     6776   7652   6866  -2532      3    370       C
ATOM   1128  CE2 PHE A 141     -15.688  -5.294  50.503  1.00 56.27           C
ANISOU 1128  CE2 PHE A 141     6710   7612   7060  -2786   -109    352       C
ATOM   1129  CZ  PHE A 141     -15.430  -4.331  51.470  1.00 56.79           C
ANISOU 1129  CZ  PHE A 141     6740   7784   7053  -2671    -13    390       C
ATOM   1130  N   TYR A 142      -9.337  -4.925  47.332  1.00 51.96           N
ANISOU 1130  N   TYR A 142     6996   6568   6178  -2328   -282    104       N
ATOM   1131  CA  TYR A 142      -8.344  -5.146  46.290  1.00 50.73           C
ANISOU 1131  CA  TYR A 142     6984   6315   5977  -2278   -340     30       C
ATOM   1132  C   TYR A 142      -7.693  -6.512  46.411  1.00 51.65           C
ANISOU 1132  C   TYR A 142     7222   6265   6139  -2347   -324     34       C
ATOM   1133  O   TYR A 142      -7.433  -6.994  47.520  1.00 43.84           O
ANISOU 1133  O   TYR A 142     6249   5228   5181  -2371   -243    120       O
ATOM   1134  CB  TYR A 142      -7.248  -4.087  46.326  1.00 45.66           C
ANISOU 1134  CB  TYR A 142     6407   5698   5244  -2120   -309     33       C
ATOM   1135  CG  TYR A 142      -7.514  -2.917  45.429  1.00 46.39           C
ANISOU 1135  CG  TYR A 142     6445   5895   5286  -2041   -373    -13       C
ATOM   1136  CD1 TYR A 142      -8.259  -1.832  45.879  1.00 46.87           C
ANISOU 1136  CD1 TYR A 142     6370   6086   5354  -1997   -355     18       C
ATOM   1137  CD2 TYR A 142      -7.035  -2.900  44.117  1.00 47.58           C
ANISOU 1137  CD2 TYR A 142     6677   6016   5384  -2007   -452    -87       C
ATOM   1138  CE1 TYR A 142      -8.507  -0.749  45.051  1.00 48.68           C
ANISOU 1138  CE1 TYR A 142     6546   6400   5549  -1920   -419    -12       C
ATOM   1139  CE2 TYR A 142      -7.267  -1.827  43.284  1.00 46.63           C
ANISOU 1139  CE2 TYR A 142     6508   5994   5215  -1933   -513   -111       C
ATOM   1140  CZ  TYR A 142      -8.003  -0.748  43.755  1.00 50.84           C
ANISOU 1140  CZ  TYR A 142     6906   6644   5768  -1890   -499    -68       C
ATOM   1141  OH  TYR A 142      -8.240   0.321  42.919  1.00 50.96           O
ANISOU 1141  OH  TYR A 142     6870   6747   5747  -1814   -563    -81       O
ATOM   1142  N   ILE A 143      -7.425  -7.107  45.247  1.00 50.16           N
ANISOU 1142  N   ILE A 143     7116   5991   5951  -2372   -405    -61       N
ATOM   1143  CA  ILE A 143      -6.474  -8.204  45.104  1.00 47.88           C
ANISOU 1143  CA  ILE A 143     6972   5532   5690  -2389   -398    -86       C
ATOM   1144  C   ILE A 143      -5.142  -7.587  44.676  1.00 52.03           C
ANISOU 1144  C   ILE A 143     7610   6044   6114  -2242   -388   -118       C
ATOM   1145  O   ILE A 143      -5.015  -7.061  43.560  1.00 51.74           O
ANISOU 1145  O   ILE A 143     7593   6059   6009  -2189   -453   -200       O
ATOM   1146  CB  ILE A 143      -6.973  -9.241  44.093  1.00 47.38           C
ANISOU 1146  CB  ILE A 143     6929   5383   5691  -2503   -490   -189       C
ATOM   1147  CG1 ILE A 143      -8.330  -9.787  44.547  1.00 46.05           C
ANISOU 1147  CG1 ILE A 143     6632   5233   5633  -2654   -499   -149       C
ATOM   1148  CG2 ILE A 143      -5.937 -10.335  43.906  1.00 50.39           C
ANISOU 1148  CG2 ILE A 143     7460   5578   6107  -2506   -482   -228       C
ATOM   1149  CD1 ILE A 143      -9.142 -10.404  43.437  1.00 47.56           C
ANISOU 1149  CD1 ILE A 143     6793   5403   5875  -2764   -611   -265       C
ATOM   1150  N   SER A 144      -4.142  -7.651  45.563  1.00 49.32           N
ANISOU 1150  N   SER A 144     7337   5641   5761  -2178   -307    -48       N
ATOM   1151  CA  SER A 144      -2.932  -6.848  45.434  1.00 45.16           C
ANISOU 1151  CA  SER A 144     6886   5129   5144  -2034   -281    -53       C
ATOM   1152  C   SER A 144      -1.676  -7.655  45.139  1.00 50.27           C
ANISOU 1152  C   SER A 144     7679   5627   5792  -1998   -271    -88       C
ATOM   1153  O   SER A 144      -0.591  -7.071  45.033  1.00 46.44           O
ANISOU 1153  O   SER A 144     7259   5147   5240  -1881   -246    -91       O
ATOM   1154  CB  SER A 144      -2.711  -6.030  46.715  1.00 43.93           C
ANISOU 1154  CB  SER A 144     6681   5049   4961  -1967   -197     48       C
ATOM   1155  OG  SER A 144      -2.458  -6.890  47.790  1.00 45.89           O
ANISOU 1155  OG  SER A 144     6959   5216   5262  -2012   -134    129       O
ATOM   1156  N   LYS A 145      -1.780  -8.968  44.999  1.00 46.47           N
ANISOU 1156  N   LYS A 145     7248   5012   5397  -2092   -291   -115       N
ATOM   1157  CA  LYS A 145      -0.590  -9.784  44.815  1.00 48.08           C
ANISOU 1157  CA  LYS A 145     7586   5063   5620  -2053   -276   -146       C
ATOM   1158  C   LYS A 145      -0.824 -10.887  43.807  1.00 49.95           C
ANISOU 1158  C   LYS A 145     7875   5186   5919  -2135   -345   -262       C
ATOM   1159  O   LYS A 145      -0.203 -11.951  43.898  1.00 50.99           O
ANISOU 1159  O   LYS A 145     8094   5154   6124  -2152   -332   -275       O
ATOM   1160  CB  LYS A 145      -0.131 -10.412  46.127  1.00 48.04           C
ANISOU 1160  CB  LYS A 145     7607   4966   5680  -2064   -201    -27       C
ATOM   1161  CG  LYS A 145       1.369 -10.592  46.218  1.00 49.46           C
ANISOU 1161  CG  LYS A 145     7904   5052   5838  -1956   -164    -23       C
ATOM   1162  CD  LYS A 145       1.706 -11.433  47.427  1.00 51.17           C
ANISOU 1162  CD  LYS A 145     8146   5162   6133  -1985   -107     96       C
ATOM   1163  CE  LYS A 145       3.200 -11.520  47.632  1.00 47.94           C
ANISOU 1163  CE  LYS A 145     7837   4676   5702  -1869    -70    113       C
ATOM   1164  NZ  LYS A 145       3.468 -12.370  48.824  1.00 48.58           N
ANISOU 1164  NZ  LYS A 145     7939   4659   5861  -1901    -21    242       N
ATOM   1165  N   ALA A 146      -1.722 -10.667  42.857  1.00 47.07           N
ANISOU 1165  N   ALA A 146     7454   4902   5530  -2187   -423   -350       N
ATOM   1166  CA  ALA A 146      -2.002 -11.676  41.845  1.00 53.72           C
ANISOU 1166  CA  ALA A 146     8339   5649   6422  -2269   -499   -482       C
ATOM   1167  C   ALA A 146      -0.886 -11.722  40.806  1.00 49.67           C
ANISOU 1167  C   ALA A 146     7944   5097   5830  -2172   -517   -596       C
ATOM   1168  O   ALA A 146      -0.198 -10.733  40.566  1.00 52.03           O
ANISOU 1168  O   ALA A 146     8262   5492   6016  -2052   -494   -584       O
ATOM   1169  CB  ALA A 146      -3.343 -11.385  41.159  1.00 52.11           C
ANISOU 1169  CB  ALA A 146     8029   5564   6208  -2355   -584   -541       C
ATOM   1170  N   SER A 147      -0.694 -12.893  40.199  1.00 52.43           N
ANISOU 1170  N   SER A 147     8371   5304   6248  -2224   -554   -708       N
ATOM   1171  CA  SER A 147       0.122 -13.012  38.989  1.00 50.68           C
ANISOU 1171  CA  SER A 147     8245   5067   5943  -2150   -586   -851       C
ATOM   1172  C   SER A 147      -0.821 -13.206  37.807  1.00 51.82           C
ANISOU 1172  C   SER A 147     8355   5275   6060  -2232   -692   -993       C
ATOM   1173  O   SER A 147      -1.524 -14.219  37.727  1.00 51.63           O
ANISOU 1173  O   SER A 147     8318   5148   6152  -2357   -741  -1057       O
ATOM   1174  CB  SER A 147       1.130 -14.156  39.082  1.00 49.54           C
ANISOU 1174  CB  SER A 147     8217   4719   5888  -2130   -552   -897       C
ATOM   1175  OG  SER A 147       2.039 -13.932  40.148  1.00 53.63           O
ANISOU 1175  OG  SER A 147     8763   5193   6420  -2046   -461   -763       O
ATOM   1176  N   VAL A 148      -0.811 -12.239  36.888  1.00 52.94           N
ANISOU 1176  N   VAL A 148     8481   5585   6049  -2163   -731  -1040       N
ATOM   1177  CA  VAL A 148      -1.803 -12.113  35.829  1.00 58.10           C
ANISOU 1177  CA  VAL A 148     9077   6354   6644  -2229   -837  -1146       C
ATOM   1178  C   VAL A 148      -1.174 -12.595  34.527  1.00 56.28           C
ANISOU 1178  C   VAL A 148     8947   6107   6330  -2192   -882  -1323       C
ATOM   1179  O   VAL A 148      -0.110 -12.106  34.128  1.00 59.77           O
ANISOU 1179  O   VAL A 148     9460   6591   6661  -2068   -839  -1331       O
ATOM   1180  CB  VAL A 148      -2.290 -10.655  35.709  1.00 57.06           C
ANISOU 1180  CB  VAL A 148     8850   6433   6398  -2175   -853  -1062       C
ATOM   1181  CG1 VAL A 148      -3.059 -10.436  34.408  1.00 57.63           C
ANISOU 1181  CG1 VAL A 148     8880   6644   6373  -2210   -967  -1175       C
ATOM   1182  CG2 VAL A 148      -3.126 -10.244  36.934  1.00 56.30           C
ANISOU 1182  CG2 VAL A 148     8637   6364   6389  -2226   -818   -914       C
ATOM   1183  N   VAL A 149      -1.827 -13.550  33.869  1.00 59.12           N
ANISOU 1183  N   VAL A 149     9310   6411   6743  -2301   -967  -1468       N
ATOM   1184  CA  VAL A 149      -1.302 -14.229  32.686  1.00 60.79           C
ANISOU 1184  CA  VAL A 149     9617   6586   6894  -2282  -1012  -1664       C
ATOM   1185  C   VAL A 149      -2.027 -13.723  31.445  1.00 61.24           C
ANISOU 1185  C   VAL A 149     9626   6840   6803  -2301  -1119  -1766       C
ATOM   1186  O   VAL A 149      -3.262 -13.777  31.371  1.00 64.50           O
ANISOU 1186  O   VAL A 149     9942   7308   7258  -2413  -1203  -1778       O
ATOM   1187  CB  VAL A 149      -1.448 -15.759  32.802  1.00 60.81           C
ANISOU 1187  CB  VAL A 149     9665   6365   7073  -2391  -1035  -1777       C
ATOM   1188  CG1 VAL A 149      -0.818 -16.460  31.594  1.00 58.02           C
ANISOU 1188  CG1 VAL A 149     9417   5971   6658  -2358  -1074  -1998       C
ATOM   1189  CG2 VAL A 149      -0.817 -16.257  34.085  1.00 58.40           C
ANISOU 1189  CG2 VAL A 149     9398   5871   6920  -2377   -935  -1651       C
ATOM   1190  N   THR A 150      -1.250 -13.281  30.457  1.00 64.55           N
ANISOU 1190  N   THR A 150    10111   7366   7048  -2193  -1119  -1840       N
ATOM   1191  CA  THR A 150      -1.751 -12.863  29.155  1.00 69.00           C
ANISOU 1191  CA  THR A 150    10648   8124   7444  -2195  -1221  -1945       C
ATOM   1192  C   THR A 150      -0.896 -13.490  28.060  1.00 71.35           C
ANISOU 1192  C   THR A 150    11061   8406   7641  -2143  -1229  -2138       C
ATOM   1193  O   THR A 150       0.270 -13.831  28.277  1.00 72.53           O
ANISOU 1193  O   THR A 150    11306   8441   7813  -2062  -1139  -2151       O
ATOM   1194  CB  THR A 150      -1.714 -11.341  28.992  1.00 69.90           C
ANISOU 1194  CB  THR A 150    10705   8447   7405  -2098  -1208  -1803       C
ATOM   1195  OG1 THR A 150      -0.468 -10.844  29.487  1.00 75.01           O
ANISOU 1195  OG1 THR A 150    11416   9057   8029  -1971  -1089  -1701       O
ATOM   1196  CG2 THR A 150      -2.825 -10.710  29.763  1.00 68.48           C
ANISOU 1196  CG2 THR A 150    10394   8324   7302  -2159  -1232  -1660       C
ATOM   1197  N   ALA A 151      -1.482 -13.617  26.869  1.00 71.82           N
ANISOU 1197  N   ALA A 151    11108   8596   7583  -2186  -1340  -2291       N
ATOM   1198  CA  ALA A 151      -0.762 -14.131  25.706  1.00 78.77           C
ANISOU 1198  CA  ALA A 151    12089   9504   8335  -2135  -1356  -2491       C
ATOM   1199  C   ALA A 151      -1.470 -13.757  24.406  1.00 82.83           C
ANISOU 1199  C   ALA A 151    12563  10252   8657  -2158  -1479  -2597       C
ATOM   1200  O   ALA A 151      -2.143 -12.735  24.336  1.00 82.45           O
ANISOU 1200  O   ALA A 151    12422  10378   8527  -2156  -1524  -2470       O
ATOM   1201  CB  ALA A 151      -0.602 -15.647  25.802  1.00 80.05           C
ANISOU 1201  CB  ALA A 151    12322   9430   8662  -2208  -1361  -2668       C
ATOM   1202  N   ASP A 158       1.463 -19.091  20.522  1.00 91.12           N
ANISOU 1202  N   ASP A 158    13917  10934   9771  -1894  -1489  -3704       N
ATOM   1203  CA  ASP A 158       2.896 -19.100  20.825  1.00 95.40           C
ANISOU 1203  CA  ASP A 158    14545  11393  10310  -1775  -1348  -3674       C
ATOM   1204  C   ASP A 158       3.227 -18.774  22.298  1.00 94.22           C
ANISOU 1204  C   ASP A 158    14416  11080  10302  -1806  -1247  -3458       C
ATOM   1205  O   ASP A 158       2.517 -18.013  22.962  1.00 89.78           O
ANISOU 1205  O   ASP A 158    13807  10564   9742  -1885  -1266  -3284       O
ATOM   1206  CB  ASP A 158       3.626 -18.122  19.901  1.00 95.63           C
ANISOU 1206  CB  ASP A 158    14600  11682  10053  -1641  -1305  -3652       C
ATOM   1207  CG  ASP A 158       5.129 -18.135  20.114  1.00 98.38           C
ANISOU 1207  CG  ASP A 158    15029  11961  10392  -1513  -1161  -3633       C
ATOM   1208  OD1 ASP A 158       5.692 -19.242  20.279  1.00 98.29           O
ANISOU 1208  OD1 ASP A 158    15061  11743  10542  -1487  -1127  -3764       O
ATOM   1209  OD2 ASP A 158       5.740 -17.041  20.122  1.00 94.05           O
ANISOU 1209  OD2 ASP A 158    14494  11558   9683  -1438  -1084  -3484       O
ATOM   1210  N   PHE A 159       4.332 -19.349  22.789  1.00 92.67           N
ANISOU 1210  N   PHE A 159    14293  10697  10221  -1734  -1143  -3471       N
ATOM   1211  CA  PHE A 159       4.710 -19.251  24.192  1.00 91.12           C
ANISOU 1211  CA  PHE A 159    14128  10315  10179  -1754  -1054  -3284       C
ATOM   1212  C   PHE A 159       5.663 -18.100  24.495  1.00 91.72           C
ANISOU 1212  C   PHE A 159    14248  10495  10106  -1650   -949  -3117       C
ATOM   1213  O   PHE A 159       5.738 -17.658  25.649  1.00 82.76           O
ANISOU 1213  O   PHE A 159    13126   9271   9049  -1677   -898  -2929       O
ATOM   1214  CB  PHE A 159       5.356 -20.560  24.645  1.00 91.86           C
ANISOU 1214  CB  PHE A 159    14267  10129  10505  -1734  -1008  -3374       C
ATOM   1215  CG  PHE A 159       4.854 -21.048  25.964  1.00 94.67           C
ANISOU 1215  CG  PHE A 159    14607  10255  11109  -1845  -1005  -3245       C
ATOM   1216  CD1 PHE A 159       3.523 -21.389  26.124  1.00 93.81           C
ANISOU 1216  CD1 PHE A 159    14422  10114  11107  -1993  -1105  -3254       C
ATOM   1217  CD2 PHE A 159       5.709 -21.169  27.043  1.00 92.87           C
ANISOU 1217  CD2 PHE A 159    14432   9849  11004  -1800   -903  -3109       C
ATOM   1218  CE1 PHE A 159       3.053 -21.848  27.336  1.00 92.13           C
ANISOU 1218  CE1 PHE A 159    14185   9699  11120  -2097  -1096  -3124       C
ATOM   1219  CE2 PHE A 159       5.245 -21.624  28.258  1.00 89.48           C
ANISOU 1219  CE2 PHE A 159    13983   9221  10793  -1899   -899  -2977       C
ATOM   1220  CZ  PHE A 159       3.913 -21.963  28.405  1.00 92.09           C
ANISOU 1220  CZ  PHE A 159    14237   9526  11228  -2049   -993  -2981       C
ATOM   1221  N   ASN A 160       6.398 -17.613  23.497  1.00 94.03           N
ANISOU 1221  N   ASN A 160    14564  10973  10190  -1532   -915  -3178       N
ATOM   1222  CA  ASN A 160       7.236 -16.439  23.709  1.00 87.51           C
ANISOU 1222  CA  ASN A 160    13768  10263   9218  -1438   -822  -3013       C
ATOM   1223  C   ASN A 160       6.394 -15.192  23.954  1.00 87.01           C
ANISOU 1223  C   ASN A 160    13651  10363   9047  -1500   -869  -2837       C
ATOM   1224  O   ASN A 160       6.855 -14.257  24.615  1.00 87.18           O
ANISOU 1224  O   ASN A 160    13647  10420   9058  -1435   -795  -2631       O
ATOM   1225  CB  ASN A 160       8.161 -16.247  22.509  1.00 92.98           C
ANISOU 1225  CB  ASN A 160    14485  11129   9715  -1303   -777  -3120       C
ATOM   1226  CG  ASN A 160       9.067 -17.448  22.271  1.00 96.45           C
ANISOU 1226  CG  ASN A 160    14973  11411  10263  -1229   -725  -3300       C
ATOM   1227  OD1 ASN A 160       8.888 -18.497  22.889  1.00 97.64           O
ANISOU 1227  OD1 ASN A 160    15134  11323  10641  -1285   -741  -3360       O
ATOM   1228  ND2 ASN A 160      10.024 -17.308  21.356  1.00 96.52           N
ANISOU 1228  ND2 ASN A 160    15004  11555  10116  -1102   -665  -3385       N
ATOM   1229  N   LYS A 161       5.167 -15.163  23.435  1.00 87.25           N
ANISOU 1229  N   LYS A 161    13610  10506   9037  -1592   -988  -2887       N
ATOM   1230  CA  LYS A 161       4.257 -14.040  23.633  1.00 87.07           C
ANISOU 1230  CA  LYS A 161    13508  10640   8937  -1646  -1044  -2722       C
ATOM   1231  C   LYS A 161       3.420 -14.165  24.909  1.00 84.11           C
ANISOU 1231  C   LYS A 161    13063  10115   8779  -1747  -1062  -2588       C
ATOM   1232  O   LYS A 161       2.461 -13.403  25.075  1.00 83.65           O
ANISOU 1232  O   LYS A 161    12911  10174   8696  -1799  -1121  -2471       O
ATOM   1233  CB  LYS A 161       3.306 -13.885  22.432  1.00 91.61           C
ANISOU 1233  CB  LYS A 161    14022  11428   9358  -1686  -1168  -2827       C
ATOM   1234  CG  LYS A 161       3.929 -13.731  21.029  1.00 96.14           C
ANISOU 1234  CG  LYS A 161    14614  12201   9713  -1568  -1163  -2939       C
ATOM   1235  CD  LYS A 161       3.154 -14.607  20.023  1.00101.55           C
ANISOU 1235  CD  LYS A 161    15261  12935  10387  -1611  -1283  -3156       C
ATOM   1236  CE  LYS A 161       3.449 -14.321  18.543  1.00108.78           C
ANISOU 1236  CE  LYS A 161    16179  14097  11055  -1507  -1312  -3253       C
ATOM   1237  NZ  LYS A 161       2.893 -13.038  18.036  1.00115.10           N
ANISOU 1237  NZ  LYS A 161    16917  15159  11657  -1496  -1366  -3106       N
ATOM   1238  N   LEU A 162       3.728 -15.118  25.792  1.00 78.65           N
ANISOU 1238  N   LEU A 162    12411   9173   8299  -1777  -1014  -2603       N
ATOM   1239  CA  LEU A 162       3.005 -15.257  27.052  1.00 75.21           C
ANISOU 1239  CA  LEU A 162    11912   8602   8064  -1869  -1017  -2463       C
ATOM   1240  C   LEU A 162       3.706 -14.434  28.127  1.00 70.66           C
ANISOU 1240  C   LEU A 162    11321   8006   7520  -1781   -907  -2236       C
ATOM   1241  O   LEU A 162       4.926 -14.524  28.281  1.00 68.16           O
ANISOU 1241  O   LEU A 162    11075   7620   7203  -1676   -814  -2227       O
ATOM   1242  CB  LEU A 162       2.912 -16.720  27.483  1.00 72.17           C
ANISOU 1242  CB  LEU A 162    11569   7955   7896  -1956  -1027  -2578       C
ATOM   1243  CG  LEU A 162       2.103 -16.982  28.762  1.00 65.42           C
ANISOU 1243  CG  LEU A 162    10645   6959   7251  -2066  -1031  -2435       C
ATOM   1244  CD1 LEU A 162       1.326 -18.281  28.671  1.00 72.10           C
ANISOU 1244  CD1 LEU A 162    11491   7638   8265  -2209  -1112  -2587       C
ATOM   1245  CD2 LEU A 162       2.980 -16.988  30.021  1.00 64.81           C
ANISOU 1245  CD2 LEU A 162    10597   6732   7297  -2000   -913  -2266       C
ATOM   1246  N   ASN A 163       2.934 -13.647  28.877  1.00 67.69           N
ANISOU 1246  N   ASN A 163    10850   7693   7178  -1823   -919  -2061       N
ATOM   1247  CA  ASN A 163       3.496 -12.742  29.870  1.00 67.81           C
ANISOU 1247  CA  ASN A 163    10840   7714   7209  -1743   -826  -1853       C
ATOM   1248  C   ASN A 163       2.761 -12.857  31.199  1.00 63.41           C
ANISOU 1248  C   ASN A 163    10214   7053   6825  -1829   -818  -1717       C
ATOM   1249  O   ASN A 163       1.573 -13.187  31.256  1.00 64.34           O
ANISOU 1249  O   ASN A 163    10267   7169   7012  -1950   -895  -1741       O
ATOM   1250  CB  ASN A 163       3.469 -11.305  29.363  1.00 71.04           C
ANISOU 1250  CB  ASN A 163    11198   8355   7438  -1669   -832  -1758       C
ATOM   1251  CG  ASN A 163       4.465 -11.084  28.240  1.00 83.37           C
ANISOU 1251  CG  ASN A 163    12832  10019   8825  -1562   -805  -1847       C
ATOM   1252  OD1 ASN A 163       4.084 -10.840  27.092  1.00 89.31           O
ANISOU 1252  OD1 ASN A 163    13575  10934   9423  -1567   -876  -1934       O
ATOM   1253  ND2 ASN A 163       5.752 -11.197  28.560  1.00 81.97           N
ANISOU 1253  ND2 ASN A 163    12722   9752   8669  -1465   -703  -1825       N
ATOM   1254  N   VAL A 164       3.499 -12.620  32.278  1.00 61.19           N
ANISOU 1254  N   VAL A 164     9946   6690   6616  -1767   -722  -1576       N
ATOM   1255  CA  VAL A 164       2.982 -12.704  33.636  1.00 58.51           C
ANISOU 1255  CA  VAL A 164     9546   6259   6425  -1831   -695  -1433       C
ATOM   1256  C   VAL A 164       3.447 -11.471  34.399  1.00 55.32           C
ANISOU 1256  C   VAL A 164     9104   5944   5972  -1738   -623  -1255       C
ATOM   1257  O   VAL A 164       4.648 -11.191  34.462  1.00 53.06           O
ANISOU 1257  O   VAL A 164     8875   5643   5642  -1626   -552  -1227       O
ATOM   1258  CB  VAL A 164       3.444 -13.989  34.351  1.00 53.59           C
ANISOU 1258  CB  VAL A 164     8988   5397   5975  -1864   -654  -1452       C
ATOM   1259  CG1 VAL A 164       2.729 -14.141  35.701  1.00 52.34           C
ANISOU 1259  CG1 VAL A 164     8760   5165   5963  -1951   -635  -1302       C
ATOM   1260  CG2 VAL A 164       3.202 -15.201  33.478  1.00 56.97           C
ANISOU 1260  CG2 VAL A 164     9470   5722   6454  -1936   -721  -1653       C
ATOM   1261  N   GLY A 165       2.500 -10.738  34.974  1.00 55.37           N
ANISOU 1261  N   GLY A 165     9006   6041   5991  -1784   -641  -1143       N
ATOM   1262  CA  GLY A 165       2.821  -9.542  35.725  1.00 55.62           C
ANISOU 1262  CA  GLY A 165     8991   6156   5987  -1703   -580   -987       C
ATOM   1263  C   GLY A 165       1.890  -9.417  36.913  1.00 54.99           C
ANISOU 1263  C   GLY A 165     8818   6065   6011  -1780   -572   -870       C
ATOM   1264  O   GLY A 165       0.918 -10.160  37.044  1.00 51.29           O
ANISOU 1264  O   GLY A 165     8310   5546   5631  -1899   -619   -902       O
ATOM   1265  N   THR A 166       2.223  -8.494  37.804  1.00 59.06           N
ANISOU 1265  N   THR A 166     9295   6627   6517  -1712   -508   -737       N
ATOM   1266  CA  THR A 166       1.384  -8.225  38.964  1.00 57.61           C
ANISOU 1266  CA  THR A 166     9016   6462   6412  -1769   -489   -623       C
ATOM   1267  C   THR A 166       0.696  -6.886  38.747  1.00 58.49           C
ANISOU 1267  C   THR A 166     9026   6750   6448  -1741   -519   -575       C
ATOM   1268  O   THR A 166       1.352  -5.865  38.500  1.00 55.13           O
ANISOU 1268  O   THR A 166     8608   6403   5937  -1634   -496   -541       O
ATOM   1269  CB  THR A 166       2.190  -8.239  40.263  1.00 58.83           C
ANISOU 1269  CB  THR A 166     9196   6536   6622  -1719   -397   -514       C
ATOM   1270  OG1 THR A 166       2.869  -9.497  40.380  1.00 59.81           O
ANISOU 1270  OG1 THR A 166     9415   6490   6822  -1737   -375   -555       O
ATOM   1271  CG2 THR A 166       1.261  -8.068  41.465  1.00 54.69           C
ANISOU 1271  CG2 THR A 166     8571   6040   6168  -1787   -374   -406       C
ATOM   1272  N   TYR A 167      -0.624  -6.905  38.787  1.00 54.99           N
ANISOU 1272  N   TYR A 167     8485   6363   6044  -1837   -573   -573       N
ATOM   1273  CA  TYR A 167      -1.397  -5.702  38.542  1.00 52.77           C
ANISOU 1273  CA  TYR A 167     8098   6245   5708  -1814   -611   -532       C
ATOM   1274  C   TYR A 167      -2.482  -5.666  39.595  1.00 51.63           C
ANISOU 1274  C   TYR A 167     7840   6121   5658  -1893   -597   -456       C
ATOM   1275  O   TYR A 167      -3.098  -6.693  39.899  1.00 51.00           O
ANISOU 1275  O   TYR A 167     7746   5965   5669  -2006   -611   -477       O
ATOM   1276  CB  TYR A 167      -1.982  -5.681  37.120  1.00 53.27           C
ANISOU 1276  CB  TYR A 167     8148   6399   5695  -1843   -716   -632       C
ATOM   1277  CG  TYR A 167      -0.943  -5.999  36.070  1.00 56.82           C
ANISOU 1277  CG  TYR A 167     8717   6821   6051  -1784   -725   -726       C
ATOM   1278  CD1 TYR A 167       0.041  -5.077  35.738  1.00 64.85           C
ANISOU 1278  CD1 TYR A 167     9774   7896   6971  -1658   -687   -687       C
ATOM   1279  CD2 TYR A 167      -0.911  -7.256  35.446  1.00 62.79           C
ANISOU 1279  CD2 TYR A 167     9545   7486   6825  -1853   -766   -857       C
ATOM   1280  CE1 TYR A 167       1.012  -5.375  34.784  1.00 68.26           C
ANISOU 1280  CE1 TYR A 167    10309   8314   7312  -1602   -685   -771       C
ATOM   1281  CE2 TYR A 167       0.061  -7.570  34.487  1.00 60.34           C
ANISOU 1281  CE2 TYR A 167     9343   7157   6426  -1793   -767   -956       C
ATOM   1282  CZ  TYR A 167       1.016  -6.623  34.167  1.00 68.81           C
ANISOU 1282  CZ  TYR A 167    10448   8304   7390  -1667   -723   -909       C
ATOM   1283  OH  TYR A 167       1.977  -6.918  33.232  1.00 78.39           O
ANISOU 1283  OH  TYR A 167    11761   9513   8512  -1605   -715  -1002       O
ATOM   1284  N   ARG A 168      -2.676  -4.495  40.180  1.00 49.35           N
ANISOU 1284  N   ARG A 168     7468   5928   5353  -1831   -565   -368       N
ATOM   1285  CA  ARG A 168      -3.686  -4.360  41.211  1.00 48.91           C
ANISOU 1285  CA  ARG A 168     7295   5912   5376  -1893   -541   -297       C
ATOM   1286  C   ARG A 168      -5.073  -4.615  40.637  1.00 49.04           C
ANISOU 1286  C   ARG A 168     7215   5995   5426  -1999   -628   -343       C
ATOM   1287  O   ARG A 168      -5.417  -4.145  39.546  1.00 47.66           O
ANISOU 1287  O   ARG A 168     7015   5909   5187  -1981   -709   -394       O
ATOM   1288  CB  ARG A 168      -3.613  -2.976  41.830  1.00 46.73           C
ANISOU 1288  CB  ARG A 168     6948   5733   5074  -1794   -495   -216       C
ATOM   1289  CG  ARG A 168      -3.957  -1.835  40.901  1.00 44.55           C
ANISOU 1289  CG  ARG A 168     6613   5580   4734  -1731   -559   -227       C
ATOM   1290  CD  ARG A 168      -3.822  -0.559  41.671  1.00 50.78           C
ANISOU 1290  CD  ARG A 168     7336   6433   5525  -1636   -505   -150       C
ATOM   1291  NE  ARG A 168      -4.503   0.543  41.026  1.00 54.93           N
ANISOU 1291  NE  ARG A 168     7766   7077   6029  -1593   -566   -139       N
ATOM   1292  CZ  ARG A 168      -3.977   1.750  40.885  1.00 57.80           C
ANISOU 1292  CZ  ARG A 168     8121   7482   6358  -1479   -554   -100       C
ATOM   1293  NH1 ARG A 168      -2.742   2.013  41.295  1.00 54.42           N
ANISOU 1293  NH1 ARG A 168     7775   6992   5909  -1401   -487    -77       N
ATOM   1294  NH2 ARG A 168      -4.708   2.718  40.326  1.00 56.53           N
ANISOU 1294  NH2 ARG A 168     7862   7422   6193  -1445   -615    -80       N
ATOM   1295  N   ILE A 169      -5.876  -5.353  41.395  1.00 48.53           N
ANISOU 1295  N   ILE A 169     7089   5892   5460  -2111   -612   -316       N
ATOM   1296  CA  ILE A 169      -7.185  -5.822  40.954  1.00 48.61           C
ANISOU 1296  CA  ILE A 169     7003   5941   5524  -2234   -692   -362       C
ATOM   1297  C   ILE A 169      -8.215  -5.295  41.950  1.00 50.71           C
ANISOU 1297  C   ILE A 169     7117   6299   5852  -2266   -653   -273       C
ATOM   1298  O   ILE A 169      -8.259  -5.755  43.099  1.00 53.03           O
ANISOU 1298  O   ILE A 169     7395   6539   6213  -2312   -574   -203       O
ATOM   1299  CB  ILE A 169      -7.234  -7.356  40.881  1.00 52.26           C
ANISOU 1299  CB  ILE A 169     7528   6258   6072  -2357   -709   -420       C
ATOM   1300  CG1 ILE A 169      -6.126  -7.911  39.982  1.00 49.92           C
ANISOU 1300  CG1 ILE A 169     7386   5863   5719  -2313   -733   -517       C
ATOM   1301  CG2 ILE A 169      -8.589  -7.850  40.437  1.00 52.72           C
ANISOU 1301  CG2 ILE A 169     7481   6353   6197  -2493   -796   -472       C
ATOM   1302  CD1 ILE A 169      -6.054  -7.278  38.669  1.00 52.96           C
ANISOU 1302  CD1 ILE A 169     7784   6350   5988  -2252   -814   -598       C
ATOM   1303  N   GLN A 170      -9.048  -4.350  41.522  1.00 49.69           N
ANISOU 1303  N   GLN A 170     6871   6310   5697  -2242   -708   -274       N
ATOM   1304  CA  GLN A 170     -10.126  -3.848  42.370  1.00 51.75           C
ANISOU 1304  CA  GLN A 170     6972   6669   6021  -2272   -677   -205       C
ATOM   1305  C   GLN A 170     -11.409  -4.649  42.170  1.00 54.89           C
ANISOU 1305  C   GLN A 170     7268   7082   6507  -2425   -739   -236       C
ATOM   1306  O   GLN A 170     -11.929  -4.730  41.055  1.00 54.38           O
ANISOU 1306  O   GLN A 170     7176   7060   6424  -2461   -849   -312       O
ATOM   1307  CB  GLN A 170     -10.416  -2.380  42.091  1.00 49.90           C
ANISOU 1307  CB  GLN A 170     6648   6573   5737  -2163   -702   -183       C
ATOM   1308  CG  GLN A 170     -11.497  -1.813  43.017  1.00 50.29           C
ANISOU 1308  CG  GLN A 170     6528   6726   5856  -2179   -660   -121       C
ATOM   1309  CD  GLN A 170     -11.871  -0.374  42.700  1.00 53.55           C
ANISOU 1309  CD  GLN A 170     6841   7264   6242  -2070   -693   -105       C
ATOM   1310  OE1 GLN A 170     -11.115   0.363  42.036  1.00 52.50           O
ANISOU 1310  OE1 GLN A 170     6777   7135   6035  -1962   -721   -114       O
ATOM   1311  NE2 GLN A 170     -13.035   0.047  43.190  1.00 53.58           N
ANISOU 1311  NE2 GLN A 170     6677   7369   6313  -2096   -687    -76       N
ATOM   1312  N   VAL A 171     -11.957  -5.181  43.258  1.00 56.11           N
ANISOU 1312  N   VAL A 171     7352   7215   6752  -2513   -670   -172       N
ATOM   1313  CA  VAL A 171     -13.205  -5.937  43.177  1.00 56.03           C
ANISOU 1313  CA  VAL A 171     7228   7218   6841  -2667   -719   -189       C
ATOM   1314  C   VAL A 171     -14.360  -4.958  42.967  1.00 55.33           C
ANISOU 1314  C   VAL A 171     6964   7301   6759  -2651   -767   -182       C
ATOM   1315  O   VAL A 171     -14.622  -4.100  43.819  1.00 59.03           O
ANISOU 1315  O   VAL A 171     7340   7860   7229  -2587   -693   -110       O
ATOM   1316  CB  VAL A 171     -13.409  -6.792  44.434  1.00 53.40           C
ANISOU 1316  CB  VAL A 171     6872   6814   6605  -2766   -622   -105       C
ATOM   1317  CG1 VAL A 171     -14.772  -7.468  44.411  1.00 56.15           C
ANISOU 1317  CG1 VAL A 171     7080   7188   7068  -2929   -666   -110       C
ATOM   1318  CG2 VAL A 171     -12.293  -7.827  44.540  1.00 50.27           C
ANISOU 1318  CG2 VAL A 171     6648   6237   6217  -2783   -590   -112       C
ATOM   1319  N   LYS A 172     -15.021  -5.057  41.812  1.00 54.67           N
ANISOU 1319  N   LYS A 172     6834   7264   6674  -2700   -893   -263       N
ATOM   1320  CA  LYS A 172     -16.150  -4.195  41.473  1.00 59.59           C
ANISOU 1320  CA  LYS A 172     7286   8048   7309  -2688   -958   -260       C
ATOM   1321  C   LYS A 172     -17.493  -4.866  41.671  1.00 59.48           C
ANISOU 1321  C   LYS A 172     7117   8068   7414  -2845   -990   -261       C
ATOM   1322  O   LYS A 172     -18.480  -4.185  41.955  1.00 57.56           O
ANISOU 1322  O   LYS A 172     6703   7955   7212  -2839   -991   -221       O
ATOM   1323  CB  LYS A 172     -16.090  -3.730  40.013  1.00 59.16           C
ANISOU 1323  CB  LYS A 172     7259   8055   7164  -2632  -1090   -338       C
ATOM   1324  CG  LYS A 172     -14.760  -3.215  39.556  1.00 59.79           C
ANISOU 1324  CG  LYS A 172     7498   8096   7124  -2496  -1077   -348       C
ATOM   1325  CD  LYS A 172     -14.304  -2.073  40.420  1.00 59.01           C
ANISOU 1325  CD  LYS A 172     7381   8034   7005  -2362   -977   -258       C
ATOM   1326  CE  LYS A 172     -13.495  -1.053  39.605  1.00 60.51           C
ANISOU 1326  CE  LYS A 172     7645   8262   7084  -2216  -1013   -261       C
ATOM   1327  NZ  LYS A 172     -14.365  -0.143  38.826  1.00 60.59           N
ANISOU 1327  NZ  LYS A 172     7529   8414   7079  -2176  -1113   -257       N
ATOM   1328  N   ASP A 173     -17.560  -6.176  41.497  1.00 64.10           N
ANISOU 1328  N   ASP A 173     7754   8538   8064  -2984  -1018   -308       N
ATOM   1329  CA  ASP A 173     -18.800  -6.905  41.700  1.00 65.36           C
ANISOU 1329  CA  ASP A 173     7768   8714   8353  -3149  -1047   -306       C
ATOM   1330  C   ASP A 173     -18.452  -8.310  42.153  1.00 65.36           C
ANISOU 1330  C   ASP A 173     7859   8535   8439  -3276  -1001   -303       C
ATOM   1331  O   ASP A 173     -17.282  -8.692  42.245  1.00 63.06           O
ANISOU 1331  O   ASP A 173     7740   8115   8105  -3228   -956   -309       O
ATOM   1332  CB  ASP A 173     -19.657  -6.939  40.426  1.00 67.83           C
ANISOU 1332  CB  ASP A 173     7998   9106   8669  -3209  -1209   -408       C
ATOM   1333  CG  ASP A 173     -21.142  -7.127  40.713  1.00 72.96           C
ANISOU 1333  CG  ASP A 173     8433   9845   9444  -3337  -1236   -384       C
ATOM   1334  OD1 ASP A 173     -21.507  -7.401  41.876  1.00 75.27           O
ANISOU 1334  OD1 ASP A 173     8648  10123   9828  -3399  -1125   -292       O
ATOM   1335  OD2 ASP A 173     -21.951  -7.019  39.769  1.00 75.23           O
ANISOU 1335  OD2 ASP A 173     8623  10223   9736  -3379  -1369   -455       O
ATOM   1336  N   ARG A 174     -19.499  -9.086  42.405  1.00 67.55           N
ANISOU 1336  N   ARG A 174     8014   8803   8850  -3439  -1017   -292       N
ATOM   1337  CA  ARG A 174     -19.342 -10.481  42.763  1.00 65.07           C
ANISOU 1337  CA  ARG A 174     7765   8311   8647  -3580   -989   -286       C
ATOM   1338  C   ARG A 174     -18.507 -11.220  41.719  1.00 67.18           C
ANISOU 1338  C   ARG A 174     8208   8433   8884  -3587  -1076   -416       C
ATOM   1339  O   ARG A 174     -17.726 -12.113  42.068  1.00 68.16           O
ANISOU 1339  O   ARG A 174     8464   8383   9051  -3618  -1024   -404       O
ATOM   1340  CB  ARG A 174     -20.753 -11.050  42.938  1.00 73.49           C
ANISOU 1340  CB  ARG A 174     8645   9416   9864  -3757  -1021   -270       C
ATOM   1341  CG  ARG A 174     -20.990 -12.511  42.802  1.00 75.74           C
ANISOU 1341  CG  ARG A 174     8954   9531  10293  -3940  -1060   -310       C
ATOM   1342  CD  ARG A 174     -22.427 -12.768  42.355  1.00 77.51           C
ANISOU 1342  CD  ARG A 174     8985   9835  10629  -4090  -1160   -356       C
ATOM   1343  NE  ARG A 174     -23.337 -12.663  43.490  1.00 87.31           N
ANISOU 1343  NE  ARG A 174    10047  11162  11964  -4161  -1058   -217       N
ATOM   1344  CZ  ARG A 174     -24.218 -11.683  43.642  1.00 87.32           C
ANISOU 1344  CZ  ARG A 174     9869  11365  11945  -4118  -1055   -181       C
ATOM   1345  NH1 ARG A 174     -24.406 -10.773  42.697  1.00 82.74           N
ANISOU 1345  NH1 ARG A 174     9254  10914  11269  -4019  -1161   -267       N
ATOM   1346  NH2 ARG A 174     -24.941 -11.625  44.759  1.00 82.94           N
ANISOU 1346  NH2 ARG A 174     9161  10886  11467  -4176   -942    -52       N
ATOM   1347  N   ASP A 175     -18.588 -10.806  40.449  1.00 63.52           N
ANISOU 1347  N   ASP A 175     7755   8045   8334  -3542  -1204   -537       N
ATOM   1348  CA  ASP A 175     -17.886 -11.513  39.386  1.00 65.20           C
ANISOU 1348  CA  ASP A 175     8123   8142   8509  -3552  -1292   -678       C
ATOM   1349  C   ASP A 175     -17.215 -10.554  38.410  1.00 70.57           C
ANISOU 1349  C   ASP A 175     8883   8921   9010  -3392  -1349   -743       C
ATOM   1350  O   ASP A 175     -17.067 -10.876  37.225  1.00 71.87           O
ANISOU 1350  O   ASP A 175     9114   9077   9118  -3404  -1462   -881       O
ATOM   1351  CB  ASP A 175     -18.842 -12.437  38.627  1.00 73.71           C
ANISOU 1351  CB  ASP A 175     9126   9189   9692  -3723  -1421   -795       C
ATOM   1352  CG  ASP A 175     -19.847 -11.668  37.791  1.00 75.62           C
ANISOU 1352  CG  ASP A 175     9221   9631   9881  -3720  -1543   -848       C
ATOM   1353  OD1 ASP A 175     -20.460 -10.717  38.324  1.00 74.30           O
ANISOU 1353  OD1 ASP A 175     8914   9612   9706  -3670  -1502   -744       O
ATOM   1354  OD2 ASP A 175     -20.013 -12.009  36.598  1.00 78.60           O
ANISOU 1354  OD2 ASP A 175     9623  10020  10223  -3761  -1681   -995       O
ATOM   1355  N   ARG A 176     -16.788  -9.384  38.887  1.00 67.75           N
ANISOU 1355  N   ARG A 176     8523   8658   8561  -3243  -1272   -647       N
ATOM   1356  CA  ARG A 176     -16.154  -8.399  38.028  1.00 64.00           C
ANISOU 1356  CA  ARG A 176     8115   8276   7926  -3090  -1317   -684       C
ATOM   1357  C   ARG A 176     -15.089  -7.640  38.807  1.00 62.23           C
ANISOU 1357  C   ARG A 176     7974   8036   7634  -2942  -1190   -585       C
ATOM   1358  O   ARG A 176     -15.283  -7.300  39.980  1.00 60.89           O
ANISOU 1358  O   ARG A 176     7733   7884   7517  -2929  -1087   -472       O
ATOM   1359  CB  ARG A 176     -17.173  -7.407  37.487  1.00 66.97           C
ANISOU 1359  CB  ARG A 176     8332   8849   8265  -3063  -1405   -679       C
ATOM   1360  CG  ARG A 176     -18.075  -7.926  36.397  1.00 71.74           C
ANISOU 1360  CG  ARG A 176     8866   9504   8886  -3176  -1561   -797       C
ATOM   1361  CD  ARG A 176     -18.401  -6.815  35.397  1.00 71.09           C
ANISOU 1361  CD  ARG A 176     8722   9607   8683  -3078  -1667   -813       C
ATOM   1362  NE  ARG A 176     -18.483  -5.486  35.998  1.00 72.86           N
ANISOU 1362  NE  ARG A 176     8862   9938   8882  -2949  -1599   -687       N
ATOM   1363  CZ  ARG A 176     -19.306  -5.131  36.977  1.00 75.54           C
ANISOU 1363  CZ  ARG A 176     9046  10330   9326  -2973  -1537   -595       C
ATOM   1364  NH1 ARG A 176     -20.188  -5.977  37.483  1.00 74.01           N
ANISOU 1364  NH1 ARG A 176     8750  10103   9269  -3127  -1532   -598       N
ATOM   1365  NH2 ARG A 176     -19.238  -3.893  37.462  1.00 72.58           N
ANISOU 1365  NH2 ARG A 176     8615  10042   8921  -2839  -1475   -499       N
ATOM   1366  N   VAL A 177     -13.981  -7.335  38.132  1.00 59.41           N
ANISOU 1366  N   VAL A 177     7761   7659   7155  -2828  -1201   -630       N
ATOM   1367  CA  VAL A 177     -12.857  -6.641  38.747  1.00 59.28           C
ANISOU 1367  CA  VAL A 177     7832   7618   7072  -2687  -1093   -551       C
ATOM   1368  C   VAL A 177     -12.317  -5.589  37.784  1.00 59.78           C
ANISOU 1368  C   VAL A 177     7940   7783   6992  -2548  -1143   -575       C
ATOM   1369  O   VAL A 177     -12.526  -5.655  36.573  1.00 58.66           O
ANISOU 1369  O   VAL A 177     7809   7697   6783  -2561  -1255   -666       O
ATOM   1370  CB  VAL A 177     -11.731  -7.622  39.140  1.00 53.04           C
ANISOU 1370  CB  VAL A 177     7203   6644   6305  -2696  -1020   -565       C
ATOM   1371  CG1 VAL A 177     -12.259  -8.702  40.099  1.00 54.88           C
ANISOU 1371  CG1 VAL A 177     7394   6769   6688  -2838   -971   -523       C
ATOM   1372  CG2 VAL A 177     -11.103  -8.240  37.890  1.00 54.86           C
ANISOU 1372  CG2 VAL A 177     7564   6811   6468  -2696  -1101   -702       C
ATOM   1373  N   GLY A 178     -11.608  -4.606  38.344  1.00 56.11           N
ANISOU 1373  N   GLY A 178     7499   7342   6478  -2416  -1058   -489       N
ATOM   1374  CA  GLY A 178     -10.895  -3.624  37.558  1.00 60.41           C
ANISOU 1374  CA  GLY A 178     8100   7955   6897  -2281  -1084   -490       C
ATOM   1375  C   GLY A 178      -9.428  -3.982  37.444  1.00 55.01           C
ANISOU 1375  C   GLY A 178     7593   7157   6150  -2216  -1028   -517       C
ATOM   1376  O   GLY A 178      -8.901  -4.752  38.236  1.00 59.70           O
ANISOU 1376  O   GLY A 178     8256   7622   6804  -2249   -950   -505       O
ATOM   1377  N   ILE A 179      -8.771  -3.438  36.428  1.00 55.60           N
ANISOU 1377  N   ILE A 179     7738   7283   6104  -2124  -1070   -548       N
ATOM   1378  CA  ILE A 179      -7.359  -3.721  36.194  1.00 57.24           C
ANISOU 1378  CA  ILE A 179     8107   7399   6245  -2055  -1020   -578       C
ATOM   1379  C   ILE A 179      -6.784  -2.565  35.394  1.00 61.38           C
ANISOU 1379  C   ILE A 179     8653   8024   6644  -1926  -1040   -550       C
ATOM   1380  O   ILE A 179      -7.511  -1.855  34.695  1.00 63.59           O
ANISOU 1380  O   ILE A 179     8846   8437   6877  -1912  -1123   -538       O
ATOM   1381  CB  ILE A 179      -7.148  -5.081  35.474  1.00 52.84           C
ANISOU 1381  CB  ILE A 179     7648   6749   5681  -2141  -1068   -711       C
ATOM   1382  CG1 ILE A 179      -5.706  -5.562  35.658  1.00 54.04           C
ANISOU 1382  CG1 ILE A 179     7953   6768   5810  -2080   -985   -730       C
ATOM   1383  CG2 ILE A 179      -7.513  -4.998  33.978  1.00 53.67           C
ANISOU 1383  CG2 ILE A 179     7750   6968   5675  -2148  -1192   -807       C
ATOM   1384  CD1 ILE A 179      -5.431  -6.952  35.105  1.00 56.17           C
ANISOU 1384  CD1 ILE A 179     8323   6920   6100  -2157  -1018   -864       C
ATOM   1385  N   GLN A 180      -5.468  -2.368  35.516  1.00 64.97           N
ANISOU 1385  N   GLN A 180     9218   8416   7050  -1832   -964   -528       N
ATOM   1386  CA  GLN A 180      -4.756  -1.289  34.826  1.00 65.50           C
ANISOU 1386  CA  GLN A 180     9316   8564   7008  -1709   -966   -487       C
ATOM   1387  C   GLN A 180      -4.220  -1.786  33.490  1.00 71.20           C
ANISOU 1387  C   GLN A 180    10139   9307   7607  -1703  -1022   -586       C
ATOM   1388  O   GLN A 180      -3.075  -2.222  33.384  1.00 78.44           O
ANISOU 1388  O   GLN A 180    11175  10142   8486  -1663   -966   -623       O
ATOM   1389  CB  GLN A 180      -3.622  -0.785  35.693  1.00 70.07           C
ANISOU 1389  CB  GLN A 180     9949   9070   7606  -1614   -854   -412       C
ATOM   1390  CG  GLN A 180      -4.062  -0.136  36.963  1.00 61.31           C
ANISOU 1390  CG  GLN A 180     8742   7960   6593  -1601   -797   -321       C
ATOM   1391  CD  GLN A 180      -2.889   0.490  37.646  1.00 65.31           C
ANISOU 1391  CD  GLN A 180     9302   8414   7099  -1498   -702   -257       C
ATOM   1392  OE1 GLN A 180      -1.916  -0.196  37.958  1.00 71.73           O
ANISOU 1392  OE1 GLN A 180    10219   9123   7912  -1491   -642   -280       O
ATOM   1393  NE2 GLN A 180      -2.940   1.798  37.849  1.00 58.25           N
ANISOU 1393  NE2 GLN A 180     8336   7587   6211  -1414   -690   -180       N
ATOM   1394  N   ALA A 181      -5.045  -1.680  32.447  1.00 69.95           N
ANISOU 1394  N   ALA A 181     9927   9271   7381  -1738  -1134   -630       N
ATOM   1395  CA  ALA A 181      -4.690  -2.263  31.153  1.00 73.59           C
ANISOU 1395  CA  ALA A 181    10476   9771   7715  -1747  -1197   -745       C
ATOM   1396  C   ALA A 181      -3.437  -1.628  30.562  1.00 81.68           C
ANISOU 1396  C   ALA A 181    11590  10829   8615  -1624  -1150   -711       C
ATOM   1397  O   ALA A 181      -2.640  -2.309  29.907  1.00 84.19           O
ANISOU 1397  O   ALA A 181    12019  11116   8852  -1615  -1140   -808       O
ATOM   1398  CB  ALA A 181      -5.855  -2.128  30.180  1.00 74.21           C
ANISOU 1398  CB  ALA A 181    10466   9999   7732  -1801  -1333   -785       C
ATOM   1399  N   LEU A 182      -3.260  -0.319  30.754  1.00 81.06           N
ANISOU 1399  N   LEU A 182    11459  10815   8525  -1530  -1122   -578       N
ATOM   1400  CA  LEU A 182      -2.100   0.372  30.209  1.00 80.58           C
ANISOU 1400  CA  LEU A 182    11469  10789   8358  -1418  -1076   -527       C
ATOM   1401  C   LEU A 182      -0.822   0.030  30.960  1.00 81.20           C
ANISOU 1401  C   LEU A 182    11646  10725   8482  -1374   -955   -528       C
ATOM   1402  O   LEU A 182       0.273   0.258  30.436  1.00 84.34           O
ANISOU 1402  O   LEU A 182    12122  11133   8790  -1297   -911   -520       O
ATOM   1403  CB  LEU A 182      -2.339   1.885  30.225  1.00 86.43           C
ANISOU 1403  CB  LEU A 182    12117  11625   9099  -1336  -1086   -380       C
ATOM   1404  CG  LEU A 182      -1.480   2.808  29.356  1.00 83.43           C
ANISOU 1404  CG  LEU A 182    11775  11330   8596  -1231  -1075   -304       C
ATOM   1405  CD1 LEU A 182      -2.359   3.707  28.515  1.00 83.70           C
ANISOU 1405  CD1 LEU A 182    11712  11523   8565  -1212  -1178   -229       C
ATOM   1406  CD2 LEU A 182      -0.587   3.644  30.237  1.00 77.92           C
ANISOU 1406  CD2 LEU A 182    11082  10548   7975  -1145   -969   -197       C
ATOM   1407  N   ALA A 183      -0.938  -0.507  32.174  1.00 80.60           N
ANISOU 1407  N   ALA A 183    11562  10523   8541  -1421   -901   -529       N
ATOM   1408  CA  ALA A 183       0.226  -1.075  32.841  1.00 82.29           C
ANISOU 1408  CA  ALA A 183    11873  10597   8796  -1393   -801   -546       C
ATOM   1409  C   ALA A 183       0.686  -2.377  32.186  1.00 86.50           C
ANISOU 1409  C   ALA A 183    12515  11067   9284  -1434   -811   -687       C
ATOM   1410  O   ALA A 183       1.840  -2.779  32.376  1.00 87.34           O
ANISOU 1410  O   ALA A 183    12714  11080   9391  -1387   -735   -708       O
ATOM   1411  CB  ALA A 183      -0.081  -1.302  34.326  1.00 74.69           C
ANISOU 1411  CB  ALA A 183    10868   9531   7981  -1434   -746   -499       C
ATOM   1412  N   MET A 184      -0.186  -3.027  31.406  1.00 79.55           N
ANISOU 1412  N   MET A 184    11620  10236   8369  -1519   -906   -789       N
ATOM   1413  CA  MET A 184       0.068  -4.350  30.826  1.00 82.83           C
ANISOU 1413  CA  MET A 184    12128  10580   8764  -1573   -927   -947       C
ATOM   1414  C   MET A 184       0.564  -4.160  29.400  1.00 91.73           C
ANISOU 1414  C   MET A 184    13312  11830   9713  -1517   -963  -1015       C
ATOM   1415  O   MET A 184      -0.200  -4.145  28.434  1.00 91.70           O
ANISOU 1415  O   MET A 184    13273  11951   9617  -1556  -1064  -1075       O
ATOM   1416  CB  MET A 184      -1.201  -5.194  30.852  1.00 82.82           C
ANISOU 1416  CB  MET A 184    12071  10557   8839  -1708  -1012  -1028       C
ATOM   1417  CG  MET A 184      -1.683  -5.554  32.242  1.00 79.42           C
ANISOU 1417  CG  MET A 184    11589  10004   8581  -1776   -969   -966       C
ATOM   1418  SD  MET A 184      -2.953  -6.843  32.269  1.00 88.42           S
ANISOU 1418  SD  MET A 184    12684  11077   9833  -1947  -1054  -1077       S
ATOM   1419  CE  MET A 184      -3.042  -7.314  30.549  1.00 78.37           C
ANISOU 1419  CE  MET A 184    11464   9898   8415  -1967  -1165  -1256       C
ATOM   1420  N   HIS A 185       1.869  -3.971  29.273  1.00 94.00           N
ANISOU 1420  N   HIS A 185    13680  12092   9944  -1420   -880   -998       N
ATOM   1421  CA  HIS A 185       2.408  -3.546  27.983  1.00 94.72           C
ANISOU 1421  CA  HIS A 185    13812  12326   9853  -1350   -897  -1026       C
ATOM   1422  C   HIS A 185       2.130  -4.541  26.860  1.00106.33           C
ANISOU 1422  C   HIS A 185    15334  13841  11225  -1407   -973  -1211       C
ATOM   1423  O   HIS A 185       1.338  -4.253  25.960  1.00104.94           O
ANISOU 1423  O   HIS A 185    15112  13821  10941  -1435  -1072  -1235       O
ATOM   1424  CB  HIS A 185       3.907  -3.260  28.103  1.00 95.52           C
ANISOU 1424  CB  HIS A 185    13987  12382   9925  -1242   -783   -981       C
ATOM   1425  CG  HIS A 185       4.221  -2.024  28.896  1.00 99.08           C
ANISOU 1425  CG  HIS A 185    14380  12835  10429  -1172   -724   -802       C
ATOM   1426  ND1 HIS A 185       4.831  -0.920  28.340  1.00100.23           N
ANISOU 1426  ND1 HIS A 185    14516  13092  10474  -1081   -697   -703       N
ATOM   1427  CD2 HIS A 185       3.966  -1.699  30.186  1.00 89.03           C
ANISOU 1427  CD2 HIS A 185    13051  11473   9301  -1184   -690   -708       C
ATOM   1428  CE1 HIS A 185       4.967   0.019  29.259  1.00 93.31           C
ANISOU 1428  CE1 HIS A 185    13584  12180   9691  -1040   -651   -564       C
ATOM   1429  NE2 HIS A 185       4.446  -0.427  30.388  1.00 92.39           N
ANISOU 1429  NE2 HIS A 185    13438  11949   9717  -1099   -646   -570       N
ATOM   1430  N   ASP A 186       2.736  -5.726  26.915  1.00109.38           N
ANISOU 1430  N   ASP A 186    15812  14092  11655  -1425   -934  -1346       N
ATOM   1431  CA  ASP A 186       2.410  -6.727  25.904  1.00110.47           C
ANISOU 1431  CA  ASP A 186    15996  14259  11718  -1485  -1011  -1543       C
ATOM   1432  C   ASP A 186       0.958  -7.145  26.067  1.00108.72           C
ANISOU 1432  C   ASP A 186    15697  14032  11581  -1614  -1120  -1586       C
ATOM   1433  O   ASP A 186       0.651  -7.870  27.016  1.00121.19           O
ANISOU 1433  O   ASP A 186    17268  15444  13336  -1687  -1104  -1598       O
ATOM   1434  CB  ASP A 186       3.333  -7.951  25.990  1.00111.89           C
ANISOU 1434  CB  ASP A 186    16286  14271  11956  -1477   -948  -1686       C
ATOM   1435  CG  ASP A 186       4.602  -7.811  25.148  1.00111.74           C
ANISOU 1435  CG  ASP A 186    16350  14322  11784  -1365   -881  -1733       C
ATOM   1436  OD1 ASP A 186       5.615  -8.448  25.502  1.00113.18           O
ANISOU 1436  OD1 ASP A 186    16609  14362  12033  -1320   -794  -1782       O
ATOM   1437  OD2 ASP A 186       4.588  -7.086  24.129  1.00114.68           O
ANISOU 1437  OD2 ASP A 186    16708  14895  11970  -1321   -914  -1718       O
ATOM   1438  N   ILE A 187       0.103  -6.697  25.129  1.00103.74           N
ANISOU 1438  N   ILE A 187    15006  13588  10823  -1641  -1229  -1605       N
ATOM   1439  CA  ILE A 187      -1.321  -6.988  24.911  1.00 97.23           C
ANISOU 1439  CA  ILE A 187    14095  12817  10030  -1758  -1357  -1663       C
ATOM   1440  C   ILE A 187      -2.018  -5.718  24.446  1.00 94.81           C
ANISOU 1440  C   ILE A 187    13688  12720   9616  -1728  -1427  -1534       C
ATOM   1441  O   ILE A 187      -3.192  -5.758  24.066  1.00 93.72           O
ANISOU 1441  O   ILE A 187    13467  12676   9468  -1808  -1545  -1570       O
ATOM   1442  CB  ILE A 187      -2.101  -7.547  26.126  1.00 97.20           C
ANISOU 1442  CB  ILE A 187    14032  12650  10251  -1864  -1356  -1638       C
ATOM   1443  CG1 ILE A 187      -1.984  -6.637  27.371  1.00 93.83           C
ANISOU 1443  CG1 ILE A 187    13547  12177   9929  -1814  -1268  -1432       C
ATOM   1444  CG2 ILE A 187      -1.865  -9.064  26.324  1.00 89.99           C
ANISOU 1444  CG2 ILE A 187    13200  11541   9452  -1940  -1343  -1805       C
ATOM   1445  CD1 ILE A 187      -3.082  -5.595  27.512  1.00 91.86           C
ANISOU 1445  CD1 ILE A 187    13159  12061   9682  -1829  -1332  -1305       C
ATOM   1446  N   ALA A 188      -1.327  -4.578  24.534  1.00 95.57           N
ANISOU 1446  N   ALA A 188    13782  12880   9651  -1614  -1356  -1376       N
ATOM   1447  CA  ALA A 188      -1.964  -3.294  24.243  1.00 92.48           C
ANISOU 1447  CA  ALA A 188    13288  12659   9192  -1577  -1414  -1227       C
ATOM   1448  C   ALA A 188      -2.545  -3.272  22.830  1.00 90.30           C
ANISOU 1448  C   ALA A 188    12994  12589   8728  -1597  -1542  -1307       C
ATOM   1449  O   ALA A 188      -3.679  -2.826  22.618  1.00 90.83           O
ANISOU 1449  O   ALA A 188    12953  12768   8790  -1639  -1648  -1260       O
ATOM   1450  CB  ALA A 188      -0.962  -2.159  24.437  1.00 90.69           C
ANISOU 1450  CB  ALA A 188    13077  12454   8925  -1450  -1315  -1062       C
ATOM   1451  N   VAL A 189      -1.771  -3.763  21.854  1.00 90.12           N
ANISOU 1451  N   VAL A 189    13074  12624   8545  -1564  -1533  -1431       N
ATOM   1452  CA  VAL A 189      -2.241  -3.886  20.475  1.00 88.32           C
ANISOU 1452  CA  VAL A 189    12843  12599   8117  -1585  -1653  -1534       C
ATOM   1453  C   VAL A 189      -3.379  -4.900  20.377  1.00 89.88           C
ANISOU 1453  C   VAL A 189    13001  12770   8381  -1722  -1772  -1702       C
ATOM   1454  O   VAL A 189      -4.354  -4.700  19.641  1.00 91.33           O
ANISOU 1454  O   VAL A 189    13109  13121   8471  -1766  -1906  -1723       O
ATOM   1455  CB  VAL A 189      -1.067  -4.262  19.556  1.00 86.19           C
ANISOU 1455  CB  VAL A 189    12696  12386   7667  -1517  -1597  -1645       C
ATOM   1456  CG1 VAL A 189      -1.572  -4.732  18.192  1.00 85.41           C
ANISOU 1456  CG1 VAL A 189    12608  12476   7367  -1559  -1723  -1811       C
ATOM   1457  CG2 VAL A 189      -0.074  -3.093  19.432  1.00 86.29           C
ANISOU 1457  CG2 VAL A 189    12725  12476   7585  -1387  -1500  -1459       C
ATOM   1458  N   GLN A 190      -3.265  -6.006  21.109  1.00 91.91           N
ANISOU 1458  N   GLN A 190    13304  12815   8804  -1791  -1729  -1819       N
ATOM   1459  CA  GLN A 190      -4.320  -7.013  21.157  1.00 90.02           C
ANISOU 1459  CA  GLN A 190    13022  12515   8667  -1931  -1832  -1970       C
ATOM   1460  C   GLN A 190      -5.616  -6.402  21.680  1.00 88.99           C
ANISOU 1460  C   GLN A 190    12741  12432   8640  -1992  -1908  -1842       C
ATOM   1461  O   GLN A 190      -6.711  -6.676  21.170  1.00 89.23           O
ANISOU 1461  O   GLN A 190    12694  12555   8652  -2084  -2043  -1925       O
ATOM   1462  CB  GLN A 190      -3.827  -8.141  22.061  1.00 90.59           C
ANISOU 1462  CB  GLN A 190    13167  12323   8929  -1979  -1744  -2061       C
ATOM   1463  CG  GLN A 190      -3.728  -9.522  21.448  1.00 91.97           C
ANISOU 1463  CG  GLN A 190    13425  12424   9097  -2049  -1789  -2318       C
ATOM   1464  CD  GLN A 190      -2.928 -10.472  22.330  1.00 90.47           C
ANISOU 1464  CD  GLN A 190    13322  11968   9084  -2056  -1677  -2370       C
ATOM   1465  OE1 GLN A 190      -2.750 -10.231  23.527  1.00 94.92           O
ANISOU 1465  OE1 GLN A 190    13864  12397   9802  -2044  -1588  -2219       O
ATOM   1466  NE2 GLN A 190      -2.452 -11.564  21.746  1.00 88.22           N
ANISOU 1466  NE2 GLN A 190    13128  11606   8784  -2067  -1681  -2583       N
ATOM   1467  N   LEU A 191      -5.487  -5.531  22.685  1.00 86.55           N
ANISOU 1467  N   LEU A 191    12382  12067   8437  -1937  -1822  -1644       N
ATOM   1468  CA  LEU A 191      -6.634  -4.925  23.348  1.00 85.43           C
ANISOU 1468  CA  LEU A 191    12095  11951   8415  -1982  -1870  -1517       C
ATOM   1469  C   LEU A 191      -7.396  -4.013  22.402  1.00 89.69           C
ANISOU 1469  C   LEU A 191    12540  12728   8809  -1957  -1992  -1454       C
ATOM   1470  O   LEU A 191      -8.619  -4.123  22.261  1.00 88.89           O
ANISOU 1470  O   LEU A 191    12329  12698   8748  -2045  -2110  -1482       O
ATOM   1471  CB  LEU A 191      -6.150  -4.143  24.561  1.00 84.55           C
ANISOU 1471  CB  LEU A 191    11966  11736   8424  -1908  -1741  -1333       C
ATOM   1472  CG  LEU A 191      -7.227  -3.622  25.500  1.00 84.65           C
ANISOU 1472  CG  LEU A 191    11834  11738   8593  -1952  -1758  -1213       C
ATOM   1473  CD1 LEU A 191      -8.312  -4.670  25.693  1.00 80.84           C
ANISOU 1473  CD1 LEU A 191    11290  11199   8227  -2103  -1838  -1332       C
ATOM   1474  CD2 LEU A 191      -6.596  -3.225  26.807  1.00 76.63           C
ANISOU 1474  CD2 LEU A 191    10830  10580   7706  -1895  -1617  -1087       C
ATOM   1475  N   GLU A 192      -6.682  -3.102  21.745  1.00 91.20           N
ANISOU 1475  N   GLU A 192    12769  13047   8834  -1839  -1968  -1360       N
ATOM   1476  CA  GLU A 192      -7.344  -2.115  20.908  1.00 94.44           C
ANISOU 1476  CA  GLU A 192    13089  13683   9113  -1801  -2077  -1262       C
ATOM   1477  C   GLU A 192      -8.004  -2.784  19.705  1.00 93.55           C
ANISOU 1477  C   GLU A 192    12970  13723   8853  -1876  -2228  -1431       C
ATOM   1478  O   GLU A 192      -9.110  -2.402  19.312  1.00 94.72           O
ANISOU 1478  O   GLU A 192    12999  14013   8976  -1912  -2358  -1396       O
ATOM   1479  CB  GLU A 192      -6.328  -1.032  20.522  1.00 98.89           C
ANISOU 1479  CB  GLU A 192    13701  14329   9542  -1659  -2003  -1112       C
ATOM   1480  CG  GLU A 192      -6.591  -0.119  19.308  1.00103.19           C
ANISOU 1480  CG  GLU A 192    14202  15126   9882  -1598  -2103  -1021       C
ATOM   1481  CD  GLU A 192      -6.252   1.357  19.616  1.00105.03           C
ANISOU 1481  CD  GLU A 192    14385  15385  10136  -1481  -2042   -774       C
ATOM   1482  OE1 GLU A 192      -5.330   1.611  20.422  1.00104.32           O
ANISOU 1482  OE1 GLU A 192    14347  15148  10140  -1424  -1903   -705       O
ATOM   1483  OE2 GLU A 192      -6.883   2.263  19.031  1.00105.08           O
ANISOU 1483  OE2 GLU A 192    14299  15557  10068  -1445  -2137   -650       O
ATOM   1484  N   LYS A 193      -7.360  -3.810  19.133  1.00 90.83           N
ANISOU 1484  N   LYS A 193    12747  13348   8417  -1901  -2217  -1624       N
ATOM   1485  CA  LYS A 193      -8.022  -4.623  18.114  1.00 94.29           C
ANISOU 1485  CA  LYS A 193    13173  13888   8766  -1968  -2348  -1815       C
ATOM   1486  C   LYS A 193      -9.264  -5.298  18.682  1.00 94.79           C
ANISOU 1486  C   LYS A 193    13135  13865   9015  -2113  -2436  -1892       C
ATOM   1487  O   LYS A 193     -10.319  -5.330  18.036  1.00 97.03           O
ANISOU 1487  O   LYS A 193    13316  14274   9277  -2147  -2569  -1932       O
ATOM   1488  CB  LYS A 193      -7.068  -5.677  17.545  1.00 98.11           C
ANISOU 1488  CB  LYS A 193    13791  14295   9193  -1932  -2287  -2010       C
ATOM   1489  CG  LYS A 193      -7.259  -5.934  16.042  1.00 99.09           C
ANISOU 1489  CG  LYS A 193    13918  14594   9139  -1878  -2382  -2130       C
ATOM   1490  CD  LYS A 193      -6.707  -7.289  15.576  1.00106.79           C
ANISOU 1490  CD  LYS A 193    14998  15461  10118  -1882  -2359  -2377       C
ATOM   1491  CE  LYS A 193      -7.733  -8.420  15.739  1.00109.53           C
ANISOU 1491  CE  LYS A 193    15292  15696  10629  -2015  -2460  -2553       C
ATOM   1492  NZ  LYS A 193      -7.600  -9.481  14.688  1.00102.44           N
ANISOU 1492  NZ  LYS A 193    14460  14801   9661  -1999  -2516  -2789       N
ATOM   1493  N   ALA A 194      -9.150  -5.863  19.887  1.00 91.72           N
ANISOU 1493  N   ALA A 194    12765  13251   8833  -2183  -2351  -1904       N
ATOM   1494  CA  ALA A 194     -10.307  -6.484  20.524  1.00 90.77           C
ANISOU 1494  CA  ALA A 194    12540  13039   8909  -2322  -2416  -1953       C
ATOM   1495  C   ALA A 194     -11.414  -5.463  20.742  1.00 92.54           C
ANISOU 1495  C   ALA A 194    12596  13390   9175  -2321  -2489  -1786       C
ATOM   1496  O   ALA A 194     -12.578  -5.703  20.391  1.00 93.14           O
ANISOU 1496  O   ALA A 194    12561  13556   9271  -2418  -2628  -1849       O
ATOM   1497  CB  ALA A 194      -9.900  -7.130  21.847  1.00 88.85           C
ANISOU 1497  CB  ALA A 194    12339  12528   8891  -2359  -2283  -1944       C
ATOM   1498  N   GLU A 195     -11.058  -4.301  21.300  1.00 92.18           N
ANISOU 1498  N   GLU A 195    12523  13355   9147  -2210  -2401  -1575       N
ATOM   1499  CA  GLU A 195     -12.040  -3.247  21.540  1.00 90.68           C
ANISOU 1499  CA  GLU A 195    12171  13275   9006  -2191  -2459  -1409       C
ATOM   1500  C   GLU A 195     -12.525  -2.622  20.241  1.00 92.56           C
ANISOU 1500  C   GLU A 195    12355  13769   9043  -2155  -2606  -1391       C
ATOM   1501  O   GLU A 195     -13.700  -2.260  20.127  1.00 97.30           O
ANISOU 1501  O   GLU A 195    12808  14481   9682  -2196  -2721  -1346       O
ATOM   1502  CB  GLU A 195     -11.456  -2.177  22.451  1.00 90.16           C
ANISOU 1502  CB  GLU A 195    12100  13143   9015  -2075  -2325  -1205       C
ATOM   1503  CG  GLU A 195     -11.128  -2.682  23.827  1.00 85.94           C
ANISOU 1503  CG  GLU A 195    11594  12379   8680  -2111  -2190  -1198       C
ATOM   1504  CD  GLU A 195     -10.868  -1.555  24.790  1.00 88.63           C
ANISOU 1504  CD  GLU A 195    11888  12676   9111  -2012  -2084  -1002       C
ATOM   1505  OE1 GLU A 195      -9.782  -0.944  24.707  1.00 87.49           O
ANISOU 1505  OE1 GLU A 195    11831  12525   8887  -1898  -2000   -925       O
ATOM   1506  OE2 GLU A 195     -11.749  -1.278  25.628  1.00 91.45           O
ANISOU 1506  OE2 GLU A 195    12118  13009   9621  -2049  -2084   -930       O
ATOM   1507  N   ALA A 196     -11.636  -2.467  19.257  1.00 92.55           N
ANISOU 1507  N   ALA A 196    12465  13873   8825  -2075  -2603  -1418       N
ATOM   1508  CA  ALA A 196     -12.104  -2.113  17.923  1.00 94.48           C
ANISOU 1508  CA  ALA A 196    12668  14363   8866  -2049  -2747  -1430       C
ATOM   1509  C   ALA A 196     -13.176  -3.085  17.452  1.00 93.67           C
ANISOU 1509  C   ALA A 196    12496  14276   8819  -2146  -2871  -1607       C
ATOM   1510  O   ALA A 196     -14.149  -2.680  16.818  1.00 94.40           O
ANISOU 1510  O   ALA A 196    12471  14527   8871  -2139  -3000  -1570       O
ATOM   1511  CB  ALA A 196     -10.952  -2.081  16.925  1.00 95.70           C
ANISOU 1511  CB  ALA A 196    12959  14586   8816  -1931  -2691  -1462       C
ATOM   1512  N   GLU A 197     -12.997  -4.377  17.718  1.00 94.69           N
ANISOU 1512  N   GLU A 197    12695  14237   9044  -2234  -2837  -1799       N
ATOM   1513  CA  GLU A 197     -13.999  -5.340  17.311  1.00 96.80           C
ANISOU 1513  CA  GLU A 197    12896  14500   9384  -2332  -2955  -1971       C
ATOM   1514  C   GLU A 197     -15.011  -5.665  18.387  1.00 97.73           C
ANISOU 1514  C   GLU A 197    12890  14505   9738  -2471  -2978  -1961       C
ATOM   1515  O   GLU A 197     -15.900  -6.492  18.123  1.00 96.10           O
ANISOU 1515  O   GLU A 197    12616  14281   9619  -2564  -3075  -2099       O
ATOM   1516  CB  GLU A 197     -13.391  -6.685  16.942  1.00 97.04           C
ANISOU 1516  CB  GLU A 197    13054  14399   9417  -2359  -2924  -2203       C
ATOM   1517  CG  GLU A 197     -12.503  -6.771  15.772  1.00103.42           C
ANISOU 1517  CG  GLU A 197    13984  15301  10011  -2245  -2913  -2284       C
ATOM   1518  CD  GLU A 197     -11.877  -8.145  15.681  1.00109.86           C
ANISOU 1518  CD  GLU A 197    14919  15943  10879  -2278  -2866  -2510       C
ATOM   1519  OE1 GLU A 197     -11.723  -8.820  16.732  1.00108.34           O
ANISOU 1519  OE1 GLU A 197    14750  15534  10882  -2363  -2789  -2550       O
ATOM   1520  OE2 GLU A 197     -11.662  -8.621  14.553  1.00109.02           O
ANISOU 1520  OE2 GLU A 197    14876  15911  10635  -2229  -2921  -2655       O
ATOM   1521  N   ASN A 198     -14.841  -5.160  19.606  1.00 93.82           N
ANISOU 1521  N   ASN A 198    12374  13916   9358  -2493  -2885  -1817       N
ATOM   1522  CA  ASN A 198     -15.825  -5.403  20.646  1.00 97.46           C
ANISOU 1522  CA  ASN A 198    12706  14284  10040  -2622  -2900  -1790       C
ATOM   1523  C   ASN A 198     -15.909  -6.903  20.983  1.00 97.67           C
ANISOU 1523  C   ASN A 198    12778  14109  10225  -2746  -2878  -1977       C
ATOM   1524  O   ASN A 198     -16.985  -7.436  21.184  1.00 97.78           O
ANISOU 1524  O   ASN A 198    12672  14094  10385  -2857  -2951  -2032       O
ATOM   1525  CB  ASN A 198     -17.195  -4.792  20.207  1.00 95.60           C
ANISOU 1525  CB  ASN A 198    12280  14235   9810  -2633  -3047  -1725       C
ATOM   1526  CG  ASN A 198     -18.345  -4.953  21.229  1.00100.95           C
ANISOU 1526  CG  ASN A 198    12792  14847  10717  -2760  -3068  -1686       C
ATOM   1527  OD1 ASN A 198     -18.897  -6.039  21.426  1.00 99.26           O
ANISOU 1527  OD1 ASN A 198    12547  14523  10646  -2882  -3092  -1820       O
ATOM   1528  ND2 ASN A 198     -18.744  -3.836  21.826  1.00 99.52           N
ANISOU 1528  ND2 ASN A 198    12493  14713  10606  -2683  -3032  -1487       N
ATOM   1529  N   LYS A 199     -14.820  -7.662  21.036  1.00 94.71           N
ANISOU 1529  N   LYS A 199    12566  13581   9838  -2731  -2782  -2082       N
ATOM   1530  CA  LYS A 199     -14.957  -8.889  21.784  1.00 92.63           C
ANISOU 1530  CA  LYS A 199    12319  13091   9783  -2856  -2740  -2191       C
ATOM   1531  C   LYS A 199     -13.762  -9.162  22.670  1.00 94.86           C
ANISOU 1531  C   LYS A 199    12743  13175  10125  -2832  -2577  -2160       C
ATOM   1532  O   LYS A 199     -12.676  -8.627  22.498  1.00 93.72           O
ANISOU 1532  O   LYS A 199    12706  13051   9854  -2699  -2491  -2102       O
ATOM   1533  CB  LYS A 199     -15.426 -10.084  20.883  1.00100.69           C
ANISOU 1533  CB  LYS A 199    13338  14086  10832  -2913  -2842  -2416       C
ATOM   1534  CG  LYS A 199     -14.701 -10.650  19.696  1.00100.18           C
ANISOU 1534  CG  LYS A 199    13400  14048  10617  -2833  -2868  -2592       C
ATOM   1535  CD  LYS A 199     -15.402 -12.026  19.418  1.00 97.33           C
ANISOU 1535  CD  LYS A 199    13006  13569  10408  -2948  -2956  -2800       C
ATOM   1536  CE  LYS A 199     -15.875 -12.386  17.973  1.00105.71           C
ANISOU 1536  CE  LYS A 199    14053  14770  11342  -2922  -3112  -2970       C
ATOM   1537  NZ  LYS A 199     -14.897 -13.041  17.074  1.00107.97           N
ANISOU 1537  NZ  LYS A 199    14495  15026  11504  -2840  -3100  -3143       N
ATOM   1538  N   PRO A 200     -13.986  -9.979  23.665  1.00 94.28           N
ANISOU 1538  N   PRO A 200    12654  12896  10271  -2934  -2518  -2175       N
ATOM   1539  CA  PRO A 200     -13.128 -10.032  24.885  1.00 84.36           C
ANISOU 1539  CA  PRO A 200    11471  11442   9139  -2885  -2341  -2063       C
ATOM   1540  C   PRO A 200     -11.690 -10.313  24.565  1.00 81.71           C
ANISOU 1540  C   PRO A 200    11318  11027   8700  -2789  -2256  -2131       C
ATOM   1541  O   PRO A 200     -11.305 -10.800  23.475  1.00 81.54           O
ANISOU 1541  O   PRO A 200    11385  11055   8541  -2783  -2320  -2305       O
ATOM   1542  CB  PRO A 200     -13.783 -11.205  25.625  1.00 78.76           C
ANISOU 1542  CB  PRO A 200    10715  10545   8663  -3051  -2344  -2131       C
ATOM   1543  CG  PRO A 200     -15.275 -11.350  24.950  1.00 91.39           C
ANISOU 1543  CG  PRO A 200    12158  12291  10276  -3180  -2526  -2218       C
ATOM   1544  CD  PRO A 200     -15.437 -10.131  24.235  1.00 93.87           C
ANISOU 1544  CD  PRO A 200    12419  12846  10401  -3072  -2589  -2137       C
ATOM   1545  N   LEU A 201     -10.865 -10.004  25.560  1.00 78.67           N
ANISOU 1545  N   LEU A 201    10988  10522   8383  -2709  -2104  -1995       N
ATOM   1546  CA  LEU A 201      -9.403 -10.322  25.634  1.00 76.28           C
ANISOU 1546  CA  LEU A 201    10852  10095   8039  -2617  -1987  -2027       C
ATOM   1547  C   LEU A 201      -9.192 -11.240  26.821  1.00 76.29           C
ANISOU 1547  C   LEU A 201    10884   9845   8258  -2686  -1892  -2015       C
ATOM   1548  O   LEU A 201      -9.286 -10.785  27.973  1.00 72.30           O
ANISOU 1548  O   LEU A 201    10323   9285   7862  -2672  -1805  -1846       O
ATOM   1549  CB  LEU A 201      -8.610  -9.041  25.779  1.00 74.51           C
ANISOU 1549  CB  LEU A 201    10650   9961   7699  -2457  -1899  -1857       C
ATOM   1550  CG  LEU A 201      -7.083  -9.129  25.603  1.00 74.03           C
ANISOU 1550  CG  LEU A 201    10747   9833   7549  -2342  -1793  -1884       C
ATOM   1551  CD1 LEU A 201      -6.397  -9.479  26.898  1.00 74.89           C
ANISOU 1551  CD1 LEU A 201    10905   9727   7821  -2329  -1655  -1805       C
ATOM   1552  CD2 LEU A 201      -6.749 -10.132  24.538  1.00 76.92           C
ANISOU 1552  CD2 LEU A 201    11211  10188   7827  -2375  -1853  -2111       C
ATOM   1553  N   PRO A 202      -8.900 -12.520  26.602  1.00 75.18           N
ANISOU 1553  N   PRO A 202    10832   9547   8187  -2758  -1904  -2188       N
ATOM   1554  CA  PRO A 202      -8.829 -13.476  27.724  1.00 73.84           C
ANISOU 1554  CA  PRO A 202    10680   9130   8244  -2841  -1827  -2168       C
ATOM   1555  C   PRO A 202      -7.601 -13.261  28.594  1.00 71.94           C
ANISOU 1555  C   PRO A 202    10534   8772   8028  -2727  -1671  -2045       C
ATOM   1556  O   PRO A 202      -6.501 -13.012  28.091  1.00 70.05           O
ANISOU 1556  O   PRO A 202    10402   8558   7655  -2606  -1625  -2078       O
ATOM   1557  CB  PRO A 202      -8.767 -14.842  27.024  1.00 73.50           C
ANISOU 1557  CB  PRO A 202    10714   8961   8249  -2931  -1897  -2406       C
ATOM   1558  CG  PRO A 202      -9.293 -14.576  25.631  1.00 73.74           C
ANISOU 1558  CG  PRO A 202    10713   9206   8099  -2938  -2039  -2546       C
ATOM   1559  CD  PRO A 202      -8.818 -13.200  25.304  1.00 75.97           C
ANISOU 1559  CD  PRO A 202    10998   9692   8174  -2786  -2006  -2417       C
ATOM   1560  N   ILE A 203      -7.798 -13.374  29.912  1.00 71.02           N
ANISOU 1560  N   ILE A 203    10370   8532   8081  -2769  -1590  -1903       N
ATOM   1561  CA  ILE A 203      -6.713 -13.328  30.887  1.00 68.90           C
ANISOU 1561  CA  ILE A 203    10183   8133   7864  -2681  -1448  -1787       C
ATOM   1562  C   ILE A 203      -7.011 -14.322  32.004  1.00 68.42           C
ANISOU 1562  C   ILE A 203    10105   7864   8029  -2795  -1402  -1743       C
ATOM   1563  O   ILE A 203      -8.161 -14.699  32.249  1.00 68.59           O
ANISOU 1563  O   ILE A 203    10020   7874   8166  -2930  -1460  -1741       O
ATOM   1564  CB  ILE A 203      -6.483 -11.927  31.507  1.00 67.75           C
ANISOU 1564  CB  ILE A 203     9987   8112   7643  -2566  -1372  -1591       C
ATOM   1565  CG1 ILE A 203      -7.658 -11.509  32.385  1.00 70.05           C
ANISOU 1565  CG1 ILE A 203    10126   8453   8037  -2643  -1377  -1460       C
ATOM   1566  CG2 ILE A 203      -6.255 -10.867  30.447  1.00 70.90           C
ANISOU 1566  CG2 ILE A 203    10389   8717   7832  -2458  -1418  -1605       C
ATOM   1567  CD1 ILE A 203      -7.313 -10.312  33.286  1.00 67.90           C
ANISOU 1567  CD1 ILE A 203     9817   8248   7736  -2532  -1278  -1271       C
ATOM   1568  N   ALA A 204      -5.950 -14.737  32.691  1.00 66.27           N
ANISOU 1568  N   ALA A 204     9933   7429   7819  -2737  -1296  -1696       N
ATOM   1569  CA  ALA A 204      -6.054 -15.564  33.887  1.00 64.06           C
ANISOU 1569  CA  ALA A 204     9645   6954   7741  -2820  -1232  -1610       C
ATOM   1570  C   ALA A 204      -5.377 -14.841  35.042  1.00 60.45           C
ANISOU 1570  C   ALA A 204     9194   6498   7275  -2719  -1106  -1413       C
ATOM   1571  O   ALA A 204      -4.230 -14.406  34.917  1.00 59.81           O
ANISOU 1571  O   ALA A 204     9203   6429   7093  -2583  -1047  -1402       O
ATOM   1572  CB  ALA A 204      -5.419 -16.939  33.676  1.00 62.54           C
ANISOU 1572  CB  ALA A 204     9569   6534   7659  -2857  -1231  -1744       C
ATOM   1573  N   ILE A 205      -6.088 -14.723  36.158  1.00 60.52           N
ANISOU 1573  N   ILE A 205     9104   6503   7390  -2787  -1066  -1264       N
ATOM   1574  CA  ILE A 205      -5.598 -14.070  37.362  1.00 55.57           C
ANISOU 1574  CA  ILE A 205     8467   5887   6761  -2707   -951  -1081       C
ATOM   1575  C   ILE A 205      -5.315 -15.158  38.385  1.00 56.09           C
ANISOU 1575  C   ILE A 205     8574   5742   6995  -2770   -884  -1013       C
ATOM   1576  O   ILE A 205      -6.247 -15.803  38.873  1.00 57.96           O
ANISOU 1576  O   ILE A 205     8735   5917   7371  -2909   -900   -977       O
ATOM   1577  CB  ILE A 205      -6.621 -13.069  37.909  1.00 56.13           C
ANISOU 1577  CB  ILE A 205     8387   6127   6813  -2727   -948   -959       C
ATOM   1578  CG1 ILE A 205      -6.848 -11.931  36.920  1.00 56.92           C
ANISOU 1578  CG1 ILE A 205     8446   6430   6752  -2651  -1015  -1007       C
ATOM   1579  CG2 ILE A 205      -6.147 -12.518  39.267  1.00 55.02           C
ANISOU 1579  CG2 ILE A 205     8236   5986   6684  -2656   -827   -781       C
ATOM   1580  CD1 ILE A 205      -8.148 -11.205  37.128  1.00 54.45           C
ANISOU 1580  CD1 ILE A 205     7969   6272   6448  -2704  -1054   -940       C
ATOM   1581  N   THR A 206      -4.051 -15.355  38.748  1.00 55.46           N
ANISOU 1581  N   THR A 206     8608   5555   6910  -2672   -808   -981       N
ATOM   1582  CA  THR A 206      -3.690 -16.407  39.695  1.00 56.97           C
ANISOU 1582  CA  THR A 206     8846   5540   7260  -2721   -747   -906       C
ATOM   1583  C   THR A 206      -3.307 -15.809  41.043  1.00 51.20           C
ANISOU 1583  C   THR A 206     8091   4846   6518  -2656   -641   -707       C
ATOM   1584  O   THR A 206      -2.570 -14.827  41.116  1.00 53.92           O
ANISOU 1584  O   THR A 206     8459   5294   6733  -2522   -597   -667       O
ATOM   1585  CB  THR A 206      -2.550 -17.283  39.169  1.00 51.84           C
ANISOU 1585  CB  THR A 206     8340   4715   6641  -2666   -744  -1021       C
ATOM   1586  OG1 THR A 206      -1.330 -16.533  39.215  1.00 56.64           O
ANISOU 1586  OG1 THR A 206     9019   5379   7123  -2501   -680   -985       O
ATOM   1587  CG2 THR A 206      -2.849 -17.714  37.726  1.00 54.95           C
ANISOU 1587  CG2 THR A 206     8761   5109   7007  -2708   -851  -1243       C
ATOM   1588  N   ILE A 207      -3.829 -16.415  42.103  1.00 52.27           N
ANISOU 1588  N   ILE A 207     8175   4897   6788  -2757   -602   -585       N
ATOM   1589  CA  ILE A 207      -3.699 -15.929  43.462  1.00 51.70           C
ANISOU 1589  CA  ILE A 207     8060   4876   6708  -2722   -506   -394       C
ATOM   1590  C   ILE A 207      -3.189 -17.063  44.326  1.00 54.00           C
ANISOU 1590  C   ILE A 207     8414   4964   7139  -2761   -452   -302       C
ATOM   1591  O   ILE A 207      -3.798 -18.141  44.375  1.00 58.41           O
ANISOU 1591  O   ILE A 207     8957   5384   7853  -2896   -481   -309       O
ATOM   1592  CB  ILE A 207      -5.038 -15.398  44.005  1.00 55.00           C
ANISOU 1592  CB  ILE A 207     8322   5442   7135  -2811   -504   -308       C
ATOM   1593  CG1 ILE A 207      -5.513 -14.218  43.174  1.00 55.14           C
ANISOU 1593  CG1 ILE A 207     8273   5659   7019  -2760   -559   -386       C
ATOM   1594  CG2 ILE A 207      -4.911 -14.923  45.449  1.00 53.09           C
ANISOU 1594  CG2 ILE A 207     8034   5262   6875  -2775   -400   -120       C
ATOM   1595  CD1 ILE A 207      -6.985 -13.947  43.296  1.00 54.54           C
ANISOU 1595  CD1 ILE A 207     8040   5703   6980  -2870   -593   -359       C
ATOM   1596  N   GLY A 208      -2.038 -16.837  44.956  1.00 51.65           N
ANISOU 1596  N   GLY A 208     8189   4641   6793  -2641   -380   -219       N
ATOM   1597  CA  GLY A 208      -1.488 -17.734  45.946  1.00 57.28           C
ANISOU 1597  CA  GLY A 208     8954   5189   7619  -2656   -321    -94       C
ATOM   1598  C   GLY A 208      -0.560 -18.645  45.184  1.00 55.87           C
ANISOU 1598  C   GLY A 208     8904   4816   7509  -2617   -353   -217       C
ATOM   1599  O   GLY A 208      -0.987 -19.676  44.654  1.00 55.30           O
ANISOU 1599  O   GLY A 208     8848   4593   7571  -2721   -409   -307       O
ATOM   1600  N   ASN A 209       0.721 -18.303  45.174  1.00 51.63           N
ANISOU 1600  N   ASN A 209     8452   4273   6891  -2469   -315   -221       N
ATOM   1601  CA  ASN A 209       1.653 -18.870  44.219  1.00 55.26           C
ANISOU 1601  CA  ASN A 209     9025   4599   7371  -2401   -345   -372       C
ATOM   1602  C   ASN A 209       2.964 -19.200  44.916  1.00 53.88           C
ANISOU 1602  C   ASN A 209     8935   4310   7228  -2295   -281   -281       C
ATOM   1603  O   ASN A 209       3.270 -18.686  45.999  1.00 53.25           O
ANISOU 1603  O   ASN A 209     8829   4304   7102  -2246   -217   -118       O
ATOM   1604  CB  ASN A 209       1.932 -17.899  43.037  1.00 50.53           C
ANISOU 1604  CB  ASN A 209     8442   4156   6602  -2307   -380   -522       C
ATOM   1605  CG  ASN A 209       0.840 -17.921  41.960  1.00 53.13           C
ANISOU 1605  CG  ASN A 209     8721   4547   6919  -2404   -469   -670       C
ATOM   1606  OD1 ASN A 209       0.583 -18.950  41.320  1.00 53.53           O
ANISOU 1606  OD1 ASN A 209     8807   4455   7077  -2484   -526   -795       O
ATOM   1607  ND2 ASN A 209       0.242 -16.764  41.717  1.00 51.54           N
ANISOU 1607  ND2 ASN A 209     8440   4559   6586  -2390   -487   -665       N
ATOM   1608  N   ASN A 210       3.730 -20.068  44.263  1.00 51.38           N
ANISOU 1608  N   ASN A 210     8715   3817   6989  -2257   -301   -398       N
ATOM   1609  CA  ASN A 210       5.147 -20.257  44.524  1.00 53.99           C
ANISOU 1609  CA  ASN A 210     9133   4055   7324  -2123   -253   -368       C
ATOM   1610  C   ASN A 210       5.781 -18.878  44.664  1.00 53.75           C
ANISOU 1610  C   ASN A 210     9087   4232   7105  -1993   -210   -326       C
ATOM   1611  O   ASN A 210       5.613 -18.032  43.774  1.00 55.67           O
ANISOU 1611  O   ASN A 210     9312   4624   7216  -1960   -236   -436       O
ATOM   1612  CB  ASN A 210       5.772 -21.060  43.382  1.00 54.97           C
ANISOU 1612  CB  ASN A 210     9351   4026   7510  -2085   -290   -567       C
ATOM   1613  CG  ASN A 210       7.293 -21.180  43.480  1.00 58.59           C
ANISOU 1613  CG  ASN A 210     9893   4405   7962  -1931   -241   -561       C
ATOM   1614  OD1 ASN A 210       7.996 -20.271  43.920  1.00 57.92           O
ANISOU 1614  OD1 ASN A 210     9802   4449   7758  -1823   -192   -474       O
ATOM   1615  ND2 ASN A 210       7.804 -22.314  43.034  1.00 63.02           N
ANISOU 1615  ND2 ASN A 210    10531   4750   8662  -1920   -258   -665       N
ATOM   1616  N   PRO A 211       6.527 -18.616  45.742  1.00 53.95           N
ANISOU 1616  N   PRO A 211     9117   4269   7113  -1916   -148   -169       N
ATOM   1617  CA  PRO A 211       7.073 -17.259  45.934  1.00 51.60           C
ANISOU 1617  CA  PRO A 211     8794   4165   6647  -1802   -110   -129       C
ATOM   1618  C   PRO A 211       7.947 -16.805  44.784  1.00 53.19           C
ANISOU 1618  C   PRO A 211     9051   4405   6753  -1688   -120   -281       C
ATOM   1619  O   PRO A 211       8.002 -15.602  44.510  1.00 52.85           O
ANISOU 1619  O   PRO A 211     8971   4541   6568  -1629   -112   -295       O
ATOM   1620  CB  PRO A 211       7.880 -17.392  47.229  1.00 52.72           C
ANISOU 1620  CB  PRO A 211     8949   4263   6818  -1742    -52     44       C
ATOM   1621  CG  PRO A 211       8.265 -18.838  47.273  1.00 55.71           C
ANISOU 1621  CG  PRO A 211     9399   4397   7370  -1767    -61     44       C
ATOM   1622  CD  PRO A 211       7.056 -19.565  46.736  1.00 54.93           C
ANISOU 1622  CD  PRO A 211     9278   4219   7372  -1916   -114    -33       C
ATOM   1623  N   LEU A 212       8.602 -17.731  44.068  1.00 55.51           N
ANISOU 1623  N   LEU A 212     9429   4538   7125  -1658   -134   -398       N
ATOM   1624  CA  LEU A 212       9.385 -17.335  42.900  1.00 57.39           C
ANISOU 1624  CA  LEU A 212     9715   4826   7264  -1554   -138   -551       C
ATOM   1625  C   LEU A 212       8.524 -16.979  41.687  1.00 56.47           C
ANISOU 1625  C   LEU A 212     9576   4819   7063  -1610   -197   -702       C
ATOM   1626  O   LEU A 212       8.980 -16.219  40.822  1.00 53.06           O
ANISOU 1626  O   LEU A 212     9155   4508   6496  -1528   -196   -788       O
ATOM   1627  CB  LEU A 212      10.382 -18.435  42.538  1.00 58.65           C
ANISOU 1627  CB  LEU A 212     9967   4786   7531  -1494   -129   -637       C
ATOM   1628  CG  LEU A 212      11.569 -18.463  43.506  1.00 56.95           C
ANISOU 1628  CG  LEU A 212     9776   4513   7349  -1388    -70   -503       C
ATOM   1629  CD1 LEU A 212      12.488 -19.644  43.233  1.00 53.78           C
ANISOU 1629  CD1 LEU A 212     9457   3895   7083  -1330    -63   -577       C
ATOM   1630  CD2 LEU A 212      12.332 -17.157  43.454  1.00 52.57           C
ANISOU 1630  CD2 LEU A 212     9199   4141   6632  -1270    -31   -478       C
ATOM   1631  N   VAL A 213       7.297 -17.502  41.593  1.00 56.70           N
ANISOU 1631  N   VAL A 213     9567   4812   7166  -1749   -251   -730       N
ATOM   1632  CA  VAL A 213       6.392 -17.073  40.525  1.00 50.98           C
ANISOU 1632  CA  VAL A 213     8805   4215   6351  -1807   -315   -857       C
ATOM   1633  C   VAL A 213       5.975 -15.617  40.731  1.00 51.06           C
ANISOU 1633  C   VAL A 213     8731   4453   6215  -1782   -305   -769       C
ATOM   1634  O   VAL A 213       5.971 -14.812  39.793  1.00 50.33           O
ANISOU 1634  O   VAL A 213     8629   4506   5987  -1735   -329   -852       O
ATOM   1635  CB  VAL A 213       5.170 -18.006  40.452  1.00 52.68           C
ANISOU 1635  CB  VAL A 213     8989   4332   6696  -1968   -378   -902       C
ATOM   1636  CG1 VAL A 213       4.086 -17.398  39.570  1.00 50.64           C
ANISOU 1636  CG1 VAL A 213     8664   4239   6337  -2034   -448   -995       C
ATOM   1637  CG2 VAL A 213       5.584 -19.372  39.921  1.00 54.96           C
ANISOU 1637  CG2 VAL A 213     9364   4398   7119  -1985   -402  -1039       C
ATOM   1638  N   THR A 214       5.593 -15.268  41.961  1.00 47.94           N
ANISOU 1638  N   THR A 214     8272   4093   5850  -1812   -270   -601       N
ATOM   1639  CA  THR A 214       5.236 -13.888  42.273  1.00 52.78           C
ANISOU 1639  CA  THR A 214     8803   4908   6343  -1781   -255   -518       C
ATOM   1640  C   THR A 214       6.415 -12.947  42.038  1.00 49.68           C
ANISOU 1640  C   THR A 214     8444   4601   5832  -1632   -214   -517       C
ATOM   1641  O   THR A 214       6.238 -11.829  41.546  1.00 48.36           O
ANISOU 1641  O   THR A 214     8234   4595   5547  -1592   -226   -532       O
ATOM   1642  CB  THR A 214       4.746 -13.822  43.722  1.00 51.97           C
ANISOU 1642  CB  THR A 214     8634   4814   6300  -1833   -214   -346       C
ATOM   1643  OG1 THR A 214       3.673 -14.760  43.882  1.00 48.71           O
ANISOU 1643  OG1 THR A 214     8187   4313   6006  -1978   -249   -345       O
ATOM   1644  CG2 THR A 214       4.270 -12.423  44.089  1.00 48.57           C
ANISOU 1644  CG2 THR A 214     8109   4584   5759  -1806   -199   -274       C
ATOM   1645  N   PHE A 215       7.625 -13.397  42.375  1.00 50.35           N
ANISOU 1645  N   PHE A 215     8601   4575   5956  -1550   -166   -495       N
ATOM   1646  CA  PHE A 215       8.833 -12.609  42.159  1.00 50.02           C
ANISOU 1646  CA  PHE A 215     8589   4597   5818  -1412   -125   -495       C
ATOM   1647  C   PHE A 215       9.069 -12.375  40.671  1.00 48.68           C
ANISOU 1647  C   PHE A 215     8455   4488   5553  -1369   -155   -648       C
ATOM   1648  O   PHE A 215       9.371 -11.257  40.247  1.00 44.63           O
ANISOU 1648  O   PHE A 215     7917   4118   4921  -1298   -144   -644       O
ATOM   1649  CB  PHE A 215      10.011 -13.342  42.802  1.00 47.38           C
ANISOU 1649  CB  PHE A 215     8320   4115   5567  -1345    -76   -448       C
ATOM   1650  CG  PHE A 215      11.281 -12.538  42.890  1.00 49.36           C
ANISOU 1650  CG  PHE A 215     8587   4428   5741  -1208    -26   -415       C
ATOM   1651  CD1 PHE A 215      11.404 -11.503  43.801  1.00 50.82           C
ANISOU 1651  CD1 PHE A 215     8712   4725   5872  -1170      6   -292       C
ATOM   1652  CD2 PHE A 215      12.376 -12.862  42.101  1.00 50.57           C
ANISOU 1652  CD2 PHE A 215     8809   4523   5883  -1118     -8   -512       C
ATOM   1653  CE1 PHE A 215      12.583 -10.783  43.899  1.00 47.44           C
ANISOU 1653  CE1 PHE A 215     8293   4346   5387  -1051     47   -264       C
ATOM   1654  CE2 PHE A 215      13.551 -12.158  42.202  1.00 48.48           C
ANISOU 1654  CE2 PHE A 215     8548   4312   5559   -998     39   -477       C
ATOM   1655  CZ  PHE A 215      13.658 -11.118  43.098  1.00 46.56           C
ANISOU 1655  CZ  PHE A 215     8245   4175   5269   -968     64   -352       C
ATOM   1656  N   MET A 216       8.933 -13.428  39.865  1.00 47.05           N
ANISOU 1656  N   MET A 216     8303   4174   5398  -1414   -193   -783       N
ATOM   1657  CA  MET A 216       9.014 -13.278  38.422  1.00 46.97           C
ANISOU 1657  CA  MET A 216     8324   4239   5285  -1387   -227   -939       C
ATOM   1658  C   MET A 216       7.908 -12.366  37.918  1.00 48.71           C
ANISOU 1658  C   MET A 216     8467   4637   5403  -1441   -282   -943       C
ATOM   1659  O   MET A 216       8.153 -11.475  37.101  1.00 50.46           O
ANISOU 1659  O   MET A 216     8682   5003   5490  -1376   -286   -976       O
ATOM   1660  CB  MET A 216       8.969 -14.661  37.763  1.00 51.64           C
ANISOU 1660  CB  MET A 216     8984   4673   5966  -1436   -263  -1094       C
ATOM   1661  CG  MET A 216       8.985 -14.674  36.241  1.00 48.93           C
ANISOU 1661  CG  MET A 216     8675   4405   5511  -1418   -305  -1279       C
ATOM   1662  SD  MET A 216       7.370 -14.236  35.551  1.00 52.25           S
ANISOU 1662  SD  MET A 216     9019   4979   5855  -1538   -402  -1330       S
ATOM   1663  CE  MET A 216       6.359 -15.667  35.970  1.00 47.34           C
ANISOU 1663  CE  MET A 216     8394   4163   5431  -1696   -458  -1377       C
ATOM   1664  N   ALA A 217       6.693 -12.537  38.439  1.00 48.12           N
ANISOU 1664  N   ALA A 217     8328   4560   5396  -1557   -321   -896       N
ATOM   1665  CA  ALA A 217       5.577 -11.685  38.043  1.00 49.15           C
ANISOU 1665  CA  ALA A 217     8372   4856   5445  -1608   -376   -891       C
ATOM   1666  C   ALA A 217       5.814 -10.227  38.402  1.00 51.30           C
ANISOU 1666  C   ALA A 217     8589   5281   5622  -1525   -339   -776       C
ATOM   1667  O   ALA A 217       5.233  -9.340  37.771  1.00 54.06           O
ANISOU 1667  O   ALA A 217     8883   5781   5876  -1524   -380   -786       O
ATOM   1668  CB  ALA A 217       4.288 -12.169  38.701  1.00 50.09           C
ANISOU 1668  CB  ALA A 217     8422   4936   5673  -1746   -412   -847       C
ATOM   1669  N   SER A 218       6.639  -9.957  39.418  1.00 46.82           N
ANISOU 1669  N   SER A 218     8031   4674   5085  -1457   -267   -666       N
ATOM   1670  CA  SER A 218       6.947  -8.591  39.820  1.00 47.36           C
ANISOU 1670  CA  SER A 218     8047   4869   5079  -1377   -230   -565       C
ATOM   1671  C   SER A 218       8.154  -8.012  39.094  1.00 48.15           C
ANISOU 1671  C   SER A 218     8196   5015   5085  -1256   -199   -597       C
ATOM   1672  O   SER A 218       8.512  -6.861  39.358  1.00 48.99           O
ANISOU 1672  O   SER A 218     8262   5214   5137  -1186   -170   -519       O
ATOM   1673  CB  SER A 218       7.187  -8.512  41.337  1.00 48.65           C
ANISOU 1673  CB  SER A 218     8185   4987   5314  -1367   -173   -432       C
ATOM   1674  OG  SER A 218       6.060  -8.966  42.055  1.00 52.85           O
ANISOU 1674  OG  SER A 218     8660   5495   5924  -1478   -191   -386       O
ATOM   1675  N   THR A 219       8.784  -8.774  38.198  1.00 47.95           N
ANISOU 1675  N   THR A 219     8251   4924   5042  -1231   -203   -713       N
ATOM   1676  CA  THR A 219       9.971  -8.339  37.479  1.00 49.19           C
ANISOU 1676  CA  THR A 219     8454   5124   5111  -1119   -164   -747       C
ATOM   1677  C   THR A 219       9.559  -7.965  36.071  1.00 47.50           C
ANISOU 1677  C   THR A 219     8238   5039   4773  -1124   -216   -840       C
ATOM   1678  O   THR A 219       9.405  -8.852  35.221  1.00 47.55           O
ANISOU 1678  O   THR A 219     8294   5006   4767  -1159   -252   -975       O
ATOM   1679  CB  THR A 219      11.020  -9.450  37.443  1.00 48.48           C
ANISOU 1679  CB  THR A 219     8454   4883   5084  -1076   -125   -815       C
ATOM   1680  OG1 THR A 219      11.255  -9.935  38.759  1.00 49.63           O
ANISOU 1680  OG1 THR A 219     8600   4905   5350  -1086    -91   -722       O
ATOM   1681  CG2 THR A 219      12.311  -8.940  36.861  1.00 47.74           C
ANISOU 1681  CG2 THR A 219     8393   4840   4907   -955    -72   -832       C
ATOM   1682  N   PRO A 220       9.384  -6.682  35.761  1.00 55.38           N
ANISOU 1682  N   PRO A 220     9176   6189   5676  -1087   -224   -776       N
ATOM   1683  CA  PRO A 220       8.839  -6.324  34.443  1.00 51.20           C
ANISOU 1683  CA  PRO A 220     8635   5795   5023  -1101   -284   -848       C
ATOM   1684  C   PRO A 220       9.866  -6.310  33.320  1.00 52.94           C
ANISOU 1684  C   PRO A 220     8919   6065   5131  -1017   -255   -925       C
ATOM   1685  O   PRO A 220       9.456  -6.405  32.157  1.00 53.25           O
ANISOU 1685  O   PRO A 220     8969   6197   5064  -1038   -308  -1019       O
ATOM   1686  CB  PRO A 220       8.242  -4.929  34.661  1.00 46.45           C
ANISOU 1686  CB  PRO A 220     7939   5326   4384  -1091   -302   -728       C
ATOM   1687  CG  PRO A 220       8.768  -4.441  35.983  1.00 50.54           C
ANISOU 1687  CG  PRO A 220     8430   5787   4986  -1049   -237   -607       C
ATOM   1688  CD  PRO A 220       9.527  -5.529  36.668  1.00 53.54           C
ANISOU 1688  CD  PRO A 220     8879   6008   5458  -1044   -187   -633       C
ATOM   1689  N   VAL A 221      11.169  -6.214  33.608  1.00 49.28           N
ANISOU 1689  N   VAL A 221     8493   5552   4679   -925   -174   -891       N
ATOM   1690  CA  VAL A 221      12.195  -6.156  32.567  1.00 48.49           C
ANISOU 1690  CA  VAL A 221     8444   5510   4471   -841   -134   -956       C
ATOM   1691  C   VAL A 221      13.467  -6.781  33.115  1.00 50.64           C
ANISOU 1691  C   VAL A 221     8770   5647   4824   -773    -55   -967       C
ATOM   1692  O   VAL A 221      13.587  -7.029  34.314  1.00 51.67           O
ANISOU 1692  O   VAL A 221     8892   5662   5079   -783    -33   -897       O
ATOM   1693  CB  VAL A 221      12.508  -4.714  32.080  1.00 56.62           C
ANISOU 1693  CB  VAL A 221     9423   6701   5388   -774   -115   -856       C
ATOM   1694  CG1 VAL A 221      11.301  -4.045  31.442  1.00 55.52           C
ANISOU 1694  CG1 VAL A 221     9228   6704   5164   -829   -197   -837       C
ATOM   1695  CG2 VAL A 221      13.052  -3.872  33.248  1.00 53.31           C
ANISOU 1695  CG2 VAL A 221     8958   6246   5053   -728    -61   -708       C
ATOM   1696  N   GLY A 222      14.423  -7.052  32.217  1.00 49.63           N
ANISOU 1696  N   GLY A 222     8695   5542   4619   -701    -12  -1054       N
ATOM   1697  CA  GLY A 222      15.777  -7.415  32.610  1.00 49.70           C
ANISOU 1697  CA  GLY A 222     8741   5454   4689   -614     70  -1052       C
ATOM   1698  C   GLY A 222      16.142  -8.887  32.510  1.00 53.47           C
ANISOU 1698  C   GLY A 222     9294   5779   5244   -613     81  -1192       C
ATOM   1699  O   GLY A 222      17.254  -9.250  32.913  1.00 52.58           O
ANISOU 1699  O   GLY A 222     9207   5571   5199   -538    146  -1186       O
ATOM   1700  N   TYR A 223      15.259  -9.754  32.009  1.00 49.81           N
ANISOU 1700  N   TYR A 223     8862   5278   4785   -693     16  -1320       N
ATOM   1701  CA  TYR A 223      15.631 -11.134  31.730  1.00 55.36           C
ANISOU 1701  CA  TYR A 223     9639   5835   5560   -687     23  -1477       C
ATOM   1702  C   TYR A 223      15.174 -11.525  30.331  1.00 62.61           C
ANISOU 1702  C   TYR A 223    10591   6841   6356   -714    -23  -1657       C
ATOM   1703  O   TYR A 223      14.175 -11.004  29.821  1.00 61.14           O
ANISOU 1703  O   TYR A 223    10370   6789   6072   -779    -90  -1657       O
ATOM   1704  CB  TYR A 223      15.060 -12.124  32.768  1.00 52.97           C
ANISOU 1704  CB  TYR A 223     9348   5336   5443   -768    -11  -1464       C
ATOM   1705  CG  TYR A 223      13.556 -12.120  32.945  1.00 56.87           C
ANISOU 1705  CG  TYR A 223     9802   5850   5956   -897    -97  -1449       C
ATOM   1706  CD1 TYR A 223      12.961 -11.264  33.863  1.00 52.55           C
ANISOU 1706  CD1 TYR A 223     9184   5354   5429   -936   -109  -1283       C
ATOM   1707  CD2 TYR A 223      12.732 -12.997  32.222  1.00 53.43           C
ANISOU 1707  CD2 TYR A 223     9395   5378   5527   -982   -168  -1607       C
ATOM   1708  CE1 TYR A 223      11.589 -11.253  34.051  1.00 55.92           C
ANISOU 1708  CE1 TYR A 223     9564   5804   5879  -1051   -182  -1266       C
ATOM   1709  CE2 TYR A 223      11.357 -12.995  32.404  1.00 51.99           C
ANISOU 1709  CE2 TYR A 223     9166   5216   5372  -1103   -248  -1589       C
ATOM   1710  CZ  TYR A 223      10.790 -12.123  33.326  1.00 57.89           C
ANISOU 1710  CZ  TYR A 223     9837   6019   6138  -1137   -251  -1414       C
ATOM   1711  OH  TYR A 223       9.421 -12.105  33.537  1.00 59.91           O
ANISOU 1711  OH  TYR A 223    10036   6302   6427  -1254   -325  -1392       O
ATOM   1712  N   ASN A 224      15.933 -12.453  29.720  1.00 60.94           N
ANISOU 1712  N   ASN A 224    10446   6558   6151   -659     12  -1817       N
ATOM   1713  CA  ASN A 224      15.719 -12.911  28.351  1.00 62.87           C
ANISOU 1713  CA  ASN A 224    10732   6887   6269   -666    -20  -2016       C
ATOM   1714  C   ASN A 224      14.777 -14.104  28.245  1.00 67.00           C
ANISOU 1714  C   ASN A 224    11290   7279   6890   -770   -103  -2169       C
ATOM   1715  O   ASN A 224      14.157 -14.301  27.190  1.00 68.50           O
ANISOU 1715  O   ASN A 224    11493   7568   6965   -814   -165  -2317       O
ATOM   1716  CB  ASN A 224      17.045 -13.324  27.709  1.00 66.82           C
ANISOU 1716  CB  ASN A 224    11281   7379   6726   -547     66  -2131       C
ATOM   1717  CG  ASN A 224      18.061 -12.232  27.729  1.00 73.19           C
ANISOU 1717  CG  ASN A 224    12052   8311   7445   -444    153  -1995       C
ATOM   1718  OD1 ASN A 224      19.246 -12.475  27.989  1.00 80.73           O
ANISOU 1718  OD1 ASN A 224    13023   9191   8460   -349    236  -1992       O
ATOM   1719  ND2 ASN A 224      17.619 -11.013  27.450  1.00 74.46           N
ANISOU 1719  ND2 ASN A 224    12159   8660   7471   -462    132  -1878       N
ATOM   1720  N   GLN A 225      14.685 -14.923  29.291  1.00 63.15           N
ANISOU 1720  N   GLN A 225    10814   6570   6610   -811   -108  -2137       N
ATOM   1721  CA  GLN A 225      13.912 -16.148  29.213  1.00 64.11           C
ANISOU 1721  CA  GLN A 225    10969   6536   6852   -909   -179  -2282       C
ATOM   1722  C   GLN A 225      12.415 -15.843  29.158  1.00 64.91           C
ANISOU 1722  C   GLN A 225    11019   6721   6924  -1042   -279  -2258       C
ATOM   1723  O   GLN A 225      11.960 -14.742  29.492  1.00 61.00           O
ANISOU 1723  O   GLN A 225    10457   6362   6357  -1060   -289  -2098       O
ATOM   1724  CB  GLN A 225      14.221 -17.051  30.410  1.00 63.63           C
ANISOU 1724  CB  GLN A 225    10931   6218   7030   -918   -153  -2221       C
ATOM   1725  CG  GLN A 225      15.697 -17.343  30.620  1.00 62.64           C
ANISOU 1725  CG  GLN A 225    10845   5999   6958   -784    -58  -2222       C
ATOM   1726  CD  GLN A 225      16.336 -16.422  31.651  1.00 55.76           C
ANISOU 1726  CD  GLN A 225     9927   5163   6095   -721      5  -1993       C
ATOM   1727  OE1 GLN A 225      16.017 -15.242  31.726  1.00 58.90           O
ANISOU 1727  OE1 GLN A 225    10269   5733   6376   -731      1  -1870       O
ATOM   1728  NE2 GLN A 225      17.226 -16.971  32.463  1.00 55.78           N
ANISOU 1728  NE2 GLN A 225     9950   4998   6244   -657     58  -1937       N
ATOM   1729  N   ASN A 226      11.651 -16.843  28.709  1.00 67.67           N
ANISOU 1729  N   ASN A 226    11394   6983   7335  -1135   -356  -2428       N
ATOM   1730  CA  ASN A 226      10.203 -16.817  28.846  1.00 64.98           C
ANISOU 1730  CA  ASN A 226    10999   6668   7023  -1277   -455  -2408       C
ATOM   1731  C   ASN A 226       9.826 -16.861  30.322  1.00 62.99           C
ANISOU 1731  C   ASN A 226    10704   6277   6952  -1337   -444  -2216       C
ATOM   1732  O   ASN A 226      10.617 -17.263  31.181  1.00 64.07           O
ANISOU 1732  O   ASN A 226    10868   6254   7220  -1286   -377  -2140       O
ATOM   1733  CB  ASN A 226       9.552 -17.999  28.126  1.00 69.49           C
ANISOU 1733  CB  ASN A 226    11606   7145   7652  -1367   -538  -2639       C
ATOM   1734  CG  ASN A 226      10.079 -18.197  26.713  1.00 82.50           C
ANISOU 1734  CG  ASN A 226    13308   8902   9136  -1297   -539  -2860       C
ATOM   1735  OD1 ASN A 226       9.521 -17.676  25.745  1.00 95.24           O
ANISOU 1735  OD1 ASN A 226    14885  10730  10571  -1312   -598  -2922       O
ATOM   1736  ND2 ASN A 226      11.148 -18.975  26.589  1.00 79.16           N
ANISOU 1736  ND2 ASN A 226    12926   8356   8793  -1197   -472  -2956       N
ATOM   1737  N   GLU A 227       8.580 -16.479  30.598  1.00 60.39           N
ANISOU 1737  N   GLU A 227    10302   6015   6627  -1448   -513  -2141       N
ATOM   1738  CA  GLU A 227       8.160 -16.160  31.957  1.00 60.40           C
ANISOU 1738  CA  GLU A 227    10244   5962   6745  -1495   -495  -1933       C
ATOM   1739  C   GLU A 227       8.348 -17.341  32.899  1.00 61.02           C
ANISOU 1739  C   GLU A 227    10357   5781   7049  -1534   -472  -1913       C
ATOM   1740  O   GLU A 227       9.037 -17.237  33.922  1.00 59.52           O
ANISOU 1740  O   GLU A 227    10171   5512   6933  -1478   -401  -1766       O
ATOM   1741  CB  GLU A 227       6.703 -15.707  31.928  1.00 58.89           C
ANISOU 1741  CB  GLU A 227     9965   5885   6525  -1614   -579  -1895       C
ATOM   1742  CG  GLU A 227       6.498 -14.501  31.048  1.00 60.06           C
ANISOU 1742  CG  GLU A 227    10073   6287   6460  -1571   -606  -1891       C
ATOM   1743  CD  GLU A 227       7.056 -13.233  31.663  1.00 60.71           C
ANISOU 1743  CD  GLU A 227    10117   6473   6475  -1478   -534  -1698       C
ATOM   1744  OE1 GLU A 227       8.265 -12.961  31.515  1.00 59.80           O
ANISOU 1744  OE1 GLU A 227    10051   6369   6302  -1360   -460  -1688       O
ATOM   1745  OE2 GLU A 227       6.262 -12.502  32.287  1.00 59.90           O
ANISOU 1745  OE2 GLU A 227     9932   6443   6385  -1524   -553  -1563       O
ATOM   1746  N   TYR A 228       7.764 -18.488  32.556  1.00 58.13           N
ANISOU 1746  N   TYR A 228    10015   5276   6796  -1631   -535  -2060       N
ATOM   1747  CA  TYR A 228       7.910 -19.649  33.418  1.00 61.40           C
ANISOU 1747  CA  TYR A 228    10462   5429   7439  -1674   -517  -2034       C
ATOM   1748  C   TYR A 228       9.308 -20.241  33.338  1.00 61.41           C
ANISOU 1748  C   TYR A 228    10548   5293   7490  -1550   -448  -2098       C
ATOM   1749  O   TYR A 228       9.757 -20.868  34.304  1.00 60.17           O
ANISOU 1749  O   TYR A 228    10412   4947   7502  -1539   -406  -2000       O
ATOM   1750  CB  TYR A 228       6.849 -20.690  33.064  1.00 61.64           C
ANISOU 1750  CB  TYR A 228    10486   5339   7594  -1821   -609  -2173       C
ATOM   1751  CG  TYR A 228       5.436 -20.190  33.302  1.00 61.74           C
ANISOU 1751  CG  TYR A 228    10401   5468   7590  -1951   -675  -2091       C
ATOM   1752  CD1 TYR A 228       5.103 -19.517  34.475  1.00 57.81           C
ANISOU 1752  CD1 TYR A 228     9832   5017   7117  -1972   -637  -1859       C
ATOM   1753  CD2 TYR A 228       4.441 -20.388  32.354  1.00 59.89           C
ANISOU 1753  CD2 TYR A 228    10138   5304   7313  -2051   -776  -2252       C
ATOM   1754  CE1 TYR A 228       3.816 -19.051  34.705  1.00 55.73           C
ANISOU 1754  CE1 TYR A 228     9470   4863   6841  -2084   -691  -1786       C
ATOM   1755  CE2 TYR A 228       3.147 -19.939  32.573  1.00 64.24           C
ANISOU 1755  CE2 TYR A 228    10588   5962   7857  -2167   -837  -2175       C
ATOM   1756  CZ  TYR A 228       2.838 -19.270  33.747  1.00 66.72           C
ANISOU 1756  CZ  TYR A 228    10831   6317   8201  -2181   -791  -1942       C
ATOM   1757  OH  TYR A 228       1.547 -18.824  33.946  1.00 65.36           O
ANISOU 1757  OH  TYR A 228    10551   6256   8025  -2292   -848  -1874       O
ATOM   1758  N   GLU A 229      10.009 -20.020  32.222  1.00 60.42           N
ANISOU 1758  N   GLU A 229    10468   5272   7216  -1452   -432  -2250       N
ATOM   1759  CA  GLU A 229      11.411 -20.408  32.122  1.00 63.41           C
ANISOU 1759  CA  GLU A 229    10915   5556   7621  -1316   -355  -2302       C
ATOM   1760  C   GLU A 229      12.249 -19.634  33.132  1.00 63.32           C
ANISOU 1760  C   GLU A 229    10882   5577   7601  -1222   -270  -2081       C
ATOM   1761  O   GLU A 229      13.147 -20.191  33.775  1.00 64.14           O
ANISOU 1761  O   GLU A 229    11020   5516   7833  -1154   -215  -2033       O
ATOM   1762  CB  GLU A 229      11.898 -20.152  30.695  1.00 67.90           C
ANISOU 1762  CB  GLU A 229    11520   6279   7998  -1235   -350  -2496       C
ATOM   1763  CG  GLU A 229      13.011 -21.042  30.186  1.00 74.83           C
ANISOU 1763  CG  GLU A 229    12472   7028   8933  -1131   -301  -2664       C
ATOM   1764  CD  GLU A 229      13.144 -20.984  28.656  1.00 77.93           C
ANISOU 1764  CD  GLU A 229    12857   7602   9150  -1075   -319  -2876       C
ATOM   1765  OE1 GLU A 229      13.395 -19.877  28.108  1.00 76.65           O
ANISOU 1765  OE1 GLU A 229    12698   7666   8761  -1022   -291  -2848       O
ATOM   1766  OE2 GLU A 229      12.982 -22.048  28.004  1.00 79.21           O
ANISOU 1766  OE2 GLU A 229    13007   7683   9404  -1083   -363  -3069       O
ATOM   1767  N   PHE A 230      11.940 -18.353  33.314  1.00 59.01           N
ANISOU 1767  N   PHE A 230    10273   5235   6914  -1220   -265  -1945       N
ATOM   1768  CA  PHE A 230      12.713 -17.548  34.249  1.00 58.77           C
ANISOU 1768  CA  PHE A 230    10216   5246   6869  -1134   -191  -1748       C
ATOM   1769  C   PHE A 230      12.550 -18.063  35.673  1.00 58.87           C
ANISOU 1769  C   PHE A 230    10213   5088   7066  -1184   -181  -1590       C
ATOM   1770  O   PHE A 230      13.514 -18.069  36.451  1.00 53.03           O
ANISOU 1770  O   PHE A 230     9486   4278   6386  -1099   -118  -1483       O
ATOM   1771  CB  PHE A 230      12.304 -16.080  34.143  1.00 56.28           C
ANISOU 1771  CB  PHE A 230     9832   5172   6381  -1131   -196  -1644       C
ATOM   1772  CG  PHE A 230      13.117 -15.162  35.019  1.00 53.39           C
ANISOU 1772  CG  PHE A 230     9435   4860   5992  -1041   -124  -1462       C
ATOM   1773  CD1 PHE A 230      14.497 -15.134  34.915  1.00 52.25           C
ANISOU 1773  CD1 PHE A 230     9327   4694   5830   -912    -51  -1472       C
ATOM   1774  CD2 PHE A 230      12.504 -14.321  35.924  1.00 54.13           C
ANISOU 1774  CD2 PHE A 230     9457   5031   6080  -1085   -130  -1292       C
ATOM   1775  CE1 PHE A 230      15.252 -14.307  35.698  1.00 51.81           C
ANISOU 1775  CE1 PHE A 230     9240   4687   5759   -835      7  -1315       C
ATOM   1776  CE2 PHE A 230      13.267 -13.456  36.727  1.00 51.44           C
ANISOU 1776  CE2 PHE A 230     9087   4742   5716  -1002    -69  -1140       C
ATOM   1777  CZ  PHE A 230      14.639 -13.459  36.614  1.00 51.14           C
ANISOU 1777  CZ  PHE A 230     9087   4676   5667   -881     -4  -1151       C
ATOM   1778  N   VAL A 231      11.347 -18.518  36.033  1.00 58.42           N
ANISOU 1778  N   VAL A 231    10126   4968   7103  -1322   -242  -1570       N
ATOM   1779  CA  VAL A 231      11.184 -19.136  37.344  1.00 60.46           C
ANISOU 1779  CA  VAL A 231    10373   5059   7541  -1375   -230  -1421       C
ATOM   1780  C   VAL A 231      12.122 -20.319  37.468  1.00 60.05           C
ANISOU 1780  C   VAL A 231    10395   4776   7646  -1317   -201  -1477       C
ATOM   1781  O   VAL A 231      12.784 -20.492  38.496  1.00 57.77           O
ANISOU 1781  O   VAL A 231    10112   4391   7448  -1267   -153  -1331       O
ATOM   1782  CB  VAL A 231       9.725 -19.557  37.591  1.00 59.42           C
ANISOU 1782  CB  VAL A 231    10194   4887   7496  -1542   -299  -1407       C
ATOM   1783  CG1 VAL A 231       9.632 -20.319  38.898  1.00 61.06           C
ANISOU 1783  CG1 VAL A 231    10396   4910   7894  -1596   -280  -1252       C
ATOM   1784  CG2 VAL A 231       8.817 -18.346  37.650  1.00 58.84           C
ANISOU 1784  CG2 VAL A 231    10035   5038   7285  -1589   -322  -1325       C
ATOM   1785  N   GLY A 232      12.197 -21.143  36.410  1.00 59.49           N
ANISOU 1785  N   GLY A 232    10380   4616   7607  -1319   -232  -1695       N
ATOM   1786  CA  GLY A 232      13.094 -22.285  36.434  1.00 59.17           C
ANISOU 1786  CA  GLY A 232    10409   4347   7725  -1255   -205  -1770       C
ATOM   1787  C   GLY A 232      14.539 -21.888  36.674  1.00 63.18           C
ANISOU 1787  C   GLY A 232    10937   4879   8188  -1092   -123  -1707       C
ATOM   1788  O   GLY A 232      15.251 -22.534  37.450  1.00 64.98           O
ANISOU 1788  O   GLY A 232    11189   4933   8567  -1041    -89  -1624       O
ATOM   1789  N   ALA A 233      14.992 -20.813  36.019  1.00 59.24           N
ANISOU 1789  N   ALA A 233    10424   4599   7486  -1009    -91  -1738       N
ATOM   1790  CA  ALA A 233      16.346 -20.325  36.264  1.00 59.92           C
ANISOU 1790  CA  ALA A 233    10516   4726   7526   -860    -12  -1668       C
ATOM   1791  C   ALA A 233      16.519 -19.909  37.722  1.00 56.65           C
ANISOU 1791  C   ALA A 233    10058   4299   7168   -854     15  -1420       C
ATOM   1792  O   ALA A 233      17.563 -20.177  38.329  1.00 57.44           O
ANISOU 1792  O   ALA A 233    10173   4303   7349   -760     63  -1346       O
ATOM   1793  CB  ALA A 233      16.672 -19.169  35.316  1.00 55.78           C
ANISOU 1793  CB  ALA A 233     9972   4449   6773   -791     15  -1725       C
ATOM   1794  N   LEU A 234      15.492 -19.266  38.303  1.00 57.37           N
ANISOU 1794  N   LEU A 234    10092   4491   7216   -954    -17  -1295       N
ATOM   1795  CA  LEU A 234      15.518 -18.832  39.699  1.00 55.70           C
ANISOU 1795  CA  LEU A 234     9834   4290   7039   -960      6  -1069       C
ATOM   1796  C   LEU A 234      15.486 -19.993  40.681  1.00 60.72           C
ANISOU 1796  C   LEU A 234    10491   4698   7880  -1002     -1   -979       C
ATOM   1797  O   LEU A 234      15.939 -19.831  41.819  1.00 63.02           O
ANISOU 1797  O   LEU A 234    10762   4974   8210   -966     30   -803       O
ATOM   1798  CB  LEU A 234      14.344 -17.891  39.994  1.00 53.74           C
ANISOU 1798  CB  LEU A 234     9515   4210   6695  -1057    -26   -981       C
ATOM   1799  CG  LEU A 234      14.392 -16.509  39.321  1.00 59.25           C
ANISOU 1799  CG  LEU A 234    10175   5146   7193  -1010    -15  -1003       C
ATOM   1800  CD1 LEU A 234      13.187 -15.636  39.710  1.00 54.37           C
ANISOU 1800  CD1 LEU A 234     9481   4672   6507  -1104    -49   -909       C
ATOM   1801  CD2 LEU A 234      15.695 -15.805  39.650  1.00 52.83           C
ANISOU 1801  CD2 LEU A 234     9357   4392   6324   -874     51   -925       C
ATOM   1802  N   GLN A 235      14.946 -21.146  40.284  1.00 57.12           N
ANISOU 1802  N   GLN A 235    10073   4070   7558  -1081    -44  -1091       N
ATOM   1803  CA  GLN A 235      15.041 -22.375  41.057  1.00 61.92           C
ANISOU 1803  CA  GLN A 235    10711   4431   8384  -1110    -50  -1021       C
ATOM   1804  C   GLN A 235      16.297 -23.162  40.723  1.00 62.90           C
ANISOU 1804  C   GLN A 235    10899   4392   8608   -986    -19  -1113       C
ATOM   1805  O   GLN A 235      16.300 -24.391  40.863  1.00 64.59           O
ANISOU 1805  O   GLN A 235    11153   4369   9020  -1013    -38  -1143       O
ATOM   1806  CB  GLN A 235      13.810 -23.253  40.819  1.00 63.84           C
ANISOU 1806  CB  GLN A 235    10958   4550   8748  -1265   -115  -1093       C
ATOM   1807  CG  GLN A 235      12.495 -22.540  41.080  1.00 62.43           C
ANISOU 1807  CG  GLN A 235    10707   4531   8483  -1393   -148  -1015       C
ATOM   1808  CD  GLN A 235      11.299 -23.454  40.941  1.00 64.50           C
ANISOU 1808  CD  GLN A 235    10962   4661   8885  -1552   -212  -1072       C
ATOM   1809  OE1 GLN A 235      10.369 -23.415  41.745  1.00 68.17           O
ANISOU 1809  OE1 GLN A 235    11370   5140   9393  -1665   -226   -928       O
ATOM   1810  NE2 GLN A 235      11.315 -24.283  39.908  1.00 62.64           N
ANISOU 1810  NE2 GLN A 235    10780   4300   8722  -1564   -250  -1287       N
ATOM   1811  N   ASP A 236      17.331 -22.489  40.218  1.00 60.48           N
ANISOU 1811  N   ASP A 236    10599   4206   8175   -852     29  -1169       N
ATOM   1812  CA  ASP A 236      18.637 -23.093  39.974  1.00 62.93           C
ANISOU 1812  CA  ASP A 236    10954   4389   8566   -714     71  -1242       C
ATOM   1813  C   ASP A 236      18.574 -24.228  38.954  1.00 68.81           C
ANISOU 1813  C   ASP A 236    11761   4962   9421   -724     45  -1475       C
ATOM   1814  O   ASP A 236      19.374 -25.166  39.002  1.00 75.78           O
ANISOU 1814  O   ASP A 236    12652   5677  10463   -639     61  -1511       O
ATOM   1815  CB  ASP A 236      19.255 -23.580  41.286  1.00 65.04           C
ANISOU 1815  CB  ASP A 236    11218   4509   8986   -671     90  -1044       C
ATOM   1816  CG  ASP A 236      20.759 -23.427  41.315  1.00 70.59           C
ANISOU 1816  CG  ASP A 236    11927   5215   9680   -502    148  -1036       C
ATOM   1817  OD1 ASP A 236      21.313 -22.830  40.367  1.00 69.56           O
ANISOU 1817  OD1 ASP A 236    11797   5219   9414   -422    182  -1169       O
ATOM   1818  OD2 ASP A 236      21.385 -23.872  42.305  1.00 72.68           O
ANISOU 1818  OD2 ASP A 236    12188   5357  10069   -450    160   -886       O
ATOM   1819  N   GLY A 237      17.639 -24.158  38.008  1.00 67.00           N
ANISOU 1819  N   GLY A 237    11536   4807   9112   -814     -0  -1634       N
ATOM   1820  CA  GLY A 237      17.540 -25.170  36.974  1.00 66.41           C
ANISOU 1820  CA  GLY A 237    11465   4640   9128   -813    -33  -1863       C
ATOM   1821  C   GLY A 237      16.439 -26.193  37.152  1.00 64.47           C
ANISOU 1821  C   GLY A 237    11185   4241   9068   -949   -106  -1880       C
ATOM   1822  O   GLY A 237      16.356 -27.126  36.346  1.00 68.30           O
ANISOU 1822  O   GLY A 237    11663   4631   9659   -949   -140  -2074       O
ATOM   1823  N   VAL A 238      15.587 -26.059  38.159  1.00 64.22           N
ANISOU 1823  N   VAL A 238    11129   4187   9085  -1067   -131  -1690       N
ATOM   1824  CA  VAL A 238      14.485 -26.990  38.378  1.00 67.47           C
ANISOU 1824  CA  VAL A 238    11499   4461   9677  -1207   -195  -1687       C
ATOM   1825  C   VAL A 238      13.257 -26.435  37.664  1.00 66.52           C
ANISOU 1825  C   VAL A 238    11361   4498   9417  -1331   -251  -1788       C
ATOM   1826  O   VAL A 238      12.797 -25.342  38.021  1.00 63.44           O
ANISOU 1826  O   VAL A 238    10967   4272   8866  -1380   -245  -1673       O
ATOM   1827  CB  VAL A 238      14.198 -27.190  39.868  1.00 67.30           C
ANISOU 1827  CB  VAL A 238    11446   4341   9784  -1270   -187  -1417       C
ATOM   1828  CG1 VAL A 238      12.998 -28.116  40.048  1.00 65.63           C
ANISOU 1828  CG1 VAL A 238    11182   3998   9757  -1423   -248  -1411       C
ATOM   1829  CG2 VAL A 238      15.421 -27.734  40.571  1.00 69.88           C
ANISOU 1829  CG2 VAL A 238    11783   4523  10244  -1143   -140  -1309       C
ATOM   1830  N   PRO A 239      12.690 -27.150  36.692  1.00 65.14           N
ANISOU 1830  N   PRO A 239    11168   4279   9305  -1383   -311  -1998       N
ATOM   1831  CA  PRO A 239      11.503 -26.639  35.996  1.00 67.71           C
ANISOU 1831  CA  PRO A 239    11466   4763   9496  -1500   -374  -2094       C
ATOM   1832  C   PRO A 239      10.347 -26.456  36.966  1.00 71.93           C
ANISOU 1832  C   PRO A 239    11951   5296  10084  -1653   -403  -1903       C
ATOM   1833  O   PRO A 239      10.258 -27.132  37.995  1.00 70.61           O
ANISOU 1833  O   PRO A 239    11759   4961  10110  -1694   -392  -1746       O
ATOM   1834  CB  PRO A 239      11.189 -27.734  34.959  1.00 72.29           C
ANISOU 1834  CB  PRO A 239    12027   5243  10198  -1525   -437  -2344       C
ATOM   1835  CG  PRO A 239      12.433 -28.578  34.861  1.00 63.87           C
ANISOU 1835  CG  PRO A 239    10990   4010   9269  -1387   -393  -2419       C
ATOM   1836  CD  PRO A 239      13.063 -28.502  36.236  1.00 67.34           C
ANISOU 1836  CD  PRO A 239    11439   4351   9795  -1343   -331  -2156       C
ATOM   1837  N   MET A 240       9.477 -25.501  36.657  1.00 71.90           N
ANISOU 1837  N   MET A 240    11926   5490   9902  -1734   -437  -1908       N
ATOM   1838  CA  MET A 240       8.233 -25.377  37.398  1.00 72.28           C
ANISOU 1838  CA  MET A 240    11910   5550  10001  -1891   -473  -1765       C
ATOM   1839  C   MET A 240       7.101 -26.029  36.610  1.00 74.27           C
ANISOU 1839  C   MET A 240    12107   5782  10330  -2012   -563  -1931       C
ATOM   1840  O   MET A 240       7.203 -26.263  35.400  1.00 73.54           O
ANISOU 1840  O   MET A 240    12028   5728  10185  -1975   -602  -2161       O
ATOM   1841  CB  MET A 240       7.900 -23.915  37.697  1.00 68.21           C
ANISOU 1841  CB  MET A 240    11378   5269   9269  -1906   -455  -1642       C
ATOM   1842  CG  MET A 240       7.585 -23.100  36.471  1.00 66.03           C
ANISOU 1842  CG  MET A 240    11087   5219   8782  -1890   -496  -1801       C
ATOM   1843  SD  MET A 240       6.819 -21.543  36.949  1.00 69.31           S
ANISOU 1843  SD  MET A 240    11398   5920   9017  -1916   -490  -1620       S
ATOM   1844  CE  MET A 240       5.292 -22.145  37.687  1.00 62.19           C
ANISOU 1844  CE  MET A 240    10416   4927   8285  -2118   -546  -1530       C
ATOM   1845  N   ASP A 241       6.015 -26.317  37.317  1.00 74.15           N
ANISOU 1845  N   ASP A 241    12022   5714  10437  -2157   -594  -1811       N
ATOM   1846  CA  ASP A 241       4.888 -27.058  36.775  1.00 73.81           C
ANISOU 1846  CA  ASP A 241    11911   5620  10515  -2287   -678  -1940       C
ATOM   1847  C   ASP A 241       3.791 -26.097  36.341  1.00 71.07           C
ANISOU 1847  C   ASP A 241    11512   5500   9991  -2383   -735  -1964       C
ATOM   1848  O   ASP A 241       3.326 -25.282  37.141  1.00 71.60           O
ANISOU 1848  O   ASP A 241    11548   5671   9985  -2438   -712  -1779       O
ATOM   1849  CB  ASP A 241       4.339 -28.038  37.817  1.00 74.01           C
ANISOU 1849  CB  ASP A 241    11876   5442  10804  -2392   -673  -1787       C
ATOM   1850  CG  ASP A 241       5.243 -29.248  38.032  1.00 80.04           C
ANISOU 1850  CG  ASP A 241    12670   5951  11789  -2315   -640  -1806       C
ATOM   1851  OD1 ASP A 241       6.160 -29.479  37.211  1.00 82.25           O
ANISOU 1851  OD1 ASP A 241    13009   6203  12041  -2193   -636  -1984       O
ATOM   1852  OD2 ASP A 241       5.032 -29.968  39.036  1.00 86.41           O
ANISOU 1852  OD2 ASP A 241    13437   6593  12801  -2374   -614  -1637       O
ATOM   1853  N   ILE A 242       3.348 -26.224  35.090  1.00 72.76           N
ANISOU 1853  N   ILE A 242    11709   5792  10145  -2403   -812  -2193       N
ATOM   1854  CA  ILE A 242       2.279 -25.388  34.564  1.00 72.69           C
ANISOU 1854  CA  ILE A 242    11641   6001   9976  -2491   -880  -2232       C
ATOM   1855  C   ILE A 242       1.197 -26.271  33.953  1.00 74.31           C
ANISOU 1855  C   ILE A 242    11767   6147  10321  -2613   -979  -2386       C
ATOM   1856  O   ILE A 242       1.430 -27.425  33.587  1.00 75.58           O
ANISOU 1856  O   ILE A 242    11935   6127  10654  -2603  -1000  -2527       O
ATOM   1857  CB  ILE A 242       2.794 -24.372  33.521  1.00 72.67           C
ANISOU 1857  CB  ILE A 242    11689   6225   9697  -2384   -885  -2352       C
ATOM   1858  CG1 ILE A 242       3.476 -25.101  32.358  1.00 73.53           C
ANISOU 1858  CG1 ILE A 242    11843   6286   9807  -2289   -906  -2601       C
ATOM   1859  CG2 ILE A 242       3.719 -23.332  34.174  1.00 66.22           C
ANISOU 1859  CG2 ILE A 242    10934   5487   8738  -2280   -791  -2185       C
ATOM   1860  CD1 ILE A 242       3.843 -24.185  31.209  1.00 73.63           C
ANISOU 1860  CD1 ILE A 242    11888   6541   9545  -2195   -918  -2728       C
ATOM   1861  N   VAL A 243      -0.002 -25.700  33.826  1.00 73.06           N
ANISOU 1861  N   VAL A 243    11526   6145  10090  -2728  -1043  -2365       N
ATOM   1862  CA  VAL A 243      -1.146 -26.418  33.269  1.00 75.71           C
ANISOU 1862  CA  VAL A 243    11770   6449  10547  -2854  -1144  -2502       C
ATOM   1863  C   VAL A 243      -1.989 -25.442  32.460  1.00 74.77           C
ANISOU 1863  C   VAL A 243    11596   6598  10215  -2895  -1224  -2573       C
ATOM   1864  O   VAL A 243      -2.064 -24.250  32.774  1.00 72.79           O
ANISOU 1864  O   VAL A 243    11343   6527   9789  -2881  -1197  -2438       O
ATOM   1865  CB  VAL A 243      -1.981 -27.090  34.381  1.00 74.27           C
ANISOU 1865  CB  VAL A 243    11503   6106  10611  -2997  -1134  -2337       C
ATOM   1866  CG1 VAL A 243      -2.423 -26.049  35.405  1.00 74.16           C
ANISOU 1866  CG1 VAL A 243    11449   6225  10505  -3047  -1087  -2088       C
ATOM   1867  CG2 VAL A 243      -3.179 -27.833  33.799  1.00 73.98           C
ANISOU 1867  CG2 VAL A 243    11363   6034  10713  -3132  -1238  -2483       C
ATOM   1868  N   LYS A 244      -2.612 -25.962  31.404  1.00 75.86           N
ANISOU 1868  N   LYS A 244    11686   6762  10373  -2940  -1328  -2789       N
ATOM   1869  CA  LYS A 244      -3.498 -25.168  30.565  1.00 79.09           C
ANISOU 1869  CA  LYS A 244    12029   7422  10598  -2982  -1421  -2866       C
ATOM   1870  C   LYS A 244      -4.711 -24.681  31.357  1.00 79.96           C
ANISOU 1870  C   LYS A 244    12026   7603  10752  -3123  -1440  -2687       C
ATOM   1871  O   LYS A 244      -5.236 -25.389  32.220  1.00 82.02           O
ANISOU 1871  O   LYS A 244    12229   7696  11239  -3230  -1424  -2587       O
ATOM   1872  CB  LYS A 244      -3.946 -26.010  29.370  1.00 78.01           C
ANISOU 1872  CB  LYS A 244    11858   7269  10512  -3009  -1536  -3133       C
ATOM   1873  CG  LYS A 244      -4.128 -25.244  28.081  1.00 79.63           C
ANISOU 1873  CG  LYS A 244    12059   7743  10454  -2954  -1618  -3281       C
ATOM   1874  CD  LYS A 244      -5.582 -24.935  27.861  1.00 85.15           C
ANISOU 1874  CD  LYS A 244    12630   8582  11142  -3085  -1727  -3279       C
ATOM   1875  CE  LYS A 244      -6.365 -26.143  27.366  1.00 84.17           C
ANISOU 1875  CE  LYS A 244    12436   8326  11218  -3182  -1838  -3464       C
ATOM   1876  NZ  LYS A 244      -7.836 -25.869  27.380  1.00 85.77           N
ANISOU 1876  NZ  LYS A 244    12498   8644  11448  -3324  -1933  -3424       N
ATOM   1877  N   SER A 245      -5.153 -23.457  31.070  1.00 79.99           N
ANISOU 1877  N   SER A 245    11992   7859  10540  -3120  -1471  -2640       N
ATOM   1878  CA  SER A 245      -6.364 -22.949  31.701  1.00 80.25           C
ANISOU 1878  CA  SER A 245    11902   7984  10605  -3249  -1499  -2492       C
ATOM   1879  C   SER A 245      -7.589 -23.649  31.109  1.00 83.34           C
ANISOU 1879  C   SER A 245    12177   8371  11118  -3374  -1618  -2628       C
ATOM   1880  O   SER A 245      -7.550 -24.185  30.002  1.00 86.83           O
ANISOU 1880  O   SER A 245    12635   8815  11543  -3346  -1698  -2851       O
ATOM   1881  CB  SER A 245      -6.455 -21.425  31.546  1.00 79.77           C
ANISOU 1881  CB  SER A 245    11828   8191  10291  -3201  -1502  -2406       C
ATOM   1882  OG  SER A 245      -7.115 -21.039  30.357  1.00 85.73           O
ANISOU 1882  OG  SER A 245    12524   9146  10904  -3207  -1616  -2550       O
ATOM   1883  N   ASP A 246      -8.685 -23.669  31.876  1.00 82.21           N
ANISOU 1883  N   ASP A 246    11911   8220  11105  -3511  -1629  -2496       N
ATOM   1884  CA  ASP A 246      -9.870 -24.407  31.439  1.00 84.22           C
ANISOU 1884  CA  ASP A 246    12044   8446  11509  -3640  -1735  -2611       C
ATOM   1885  C   ASP A 246     -10.457 -23.830  30.152  1.00 83.09           C
ANISOU 1885  C   ASP A 246    11850   8540  11179  -3626  -1863  -2774       C
ATOM   1886  O   ASP A 246     -10.784 -24.572  29.220  1.00 81.48           O
ANISOU 1886  O   ASP A 246    11624   8305  11030  -3649  -1963  -2983       O
ATOM   1887  CB  ASP A 246     -10.921 -24.432  32.546  1.00 85.48           C
ANISOU 1887  CB  ASP A 246    12072   8576  11829  -3784  -1710  -2418       C
ATOM   1888  CG  ASP A 246     -10.755 -25.622  33.480  1.00 85.48           C
ANISOU 1888  CG  ASP A 246    12078   8294  12105  -3846  -1636  -2338       C
ATOM   1889  OD1 ASP A 246      -9.754 -26.362  33.340  1.00 84.39           O
ANISOU 1889  OD1 ASP A 246    12052   7978  12033  -3769  -1600  -2419       O
ATOM   1890  OD2 ASP A 246     -11.630 -25.823  34.350  1.00 83.28           O
ANISOU 1890  OD2 ASP A 246    11686   7976  11981  -3970  -1611  -2189       O
ATOM   1891  N   LEU A 247     -10.587 -22.508  30.073  1.00 84.51           N
ANISOU 1891  N   LEU A 247    12011   8960  11140  -3583  -1864  -2680       N
ATOM   1892  CA  LEU A 247     -11.335 -21.901  28.980  1.00 83.30           C
ANISOU 1892  CA  LEU A 247    11781   9047  10824  -3583  -1989  -2791       C
ATOM   1893  C   LEU A 247     -10.476 -21.475  27.796  1.00 84.91           C
ANISOU 1893  C   LEU A 247    12090   9387  10786  -3435  -2018  -2937       C
ATOM   1894  O   LEU A 247     -11.012 -21.307  26.695  1.00 81.71           O
ANISOU 1894  O   LEU A 247    11635   9146  10264  -3428  -2136  -3076       O
ATOM   1895  CB  LEU A 247     -12.103 -20.678  29.488  1.00 83.99           C
ANISOU 1895  CB  LEU A 247    11761   9334  10817  -3622  -1989  -2606       C
ATOM   1896  CG  LEU A 247     -12.894 -20.832  30.785  1.00 84.34           C
ANISOU 1896  CG  LEU A 247    11695   9290  11060  -3753  -1937  -2420       C
ATOM   1897  CD1 LEU A 247     -13.737 -19.589  31.029  1.00 78.37           C
ANISOU 1897  CD1 LEU A 247    10815   8767  10193  -3780  -1961  -2282       C
ATOM   1898  CD2 LEU A 247     -13.764 -22.085  30.757  1.00 80.98           C
ANISOU 1898  CD2 LEU A 247    11178   8709  10882  -3886  -1998  -2512       C
ATOM   1899  N   TYR A 248      -9.173 -21.279  27.981  1.00 84.11           N
ANISOU 1899  N   TYR A 248    12126   9232  10600  -3314  -1914  -2903       N
ATOM   1900  CA  TYR A 248      -8.354 -20.591  26.985  1.00 84.85           C
ANISOU 1900  CA  TYR A 248    12307   9499  10434  -3167  -1920  -2988       C
ATOM   1901  C   TYR A 248      -7.086 -21.386  26.696  1.00 86.36           C
ANISOU 1901  C   TYR A 248    12634   9529  10650  -3065  -1858  -3115       C
ATOM   1902  O   TYR A 248      -6.191 -21.465  27.544  1.00 87.41           O
ANISOU 1902  O   TYR A 248    12850   9518  10845  -3018  -1740  -3006       O
ATOM   1903  CB  TYR A 248      -8.031 -19.180  27.461  1.00 80.73           C
ANISOU 1903  CB  TYR A 248    11800   9138   9738  -3105  -1852  -2792       C
ATOM   1904  CG  TYR A 248      -9.281 -18.396  27.783  1.00 84.83           C
ANISOU 1904  CG  TYR A 248    12174   9811  10246  -3200  -1912  -2667       C
ATOM   1905  CD1 TYR A 248     -10.250 -18.179  26.810  1.00 81.23           C
ANISOU 1905  CD1 TYR A 248    11617   9540   9708  -3233  -2046  -2765       C
ATOM   1906  CD2 TYR A 248      -9.492 -17.867  29.053  1.00 80.65           C
ANISOU 1906  CD2 TYR A 248    11603   9251   9790  -3252  -1838  -2453       C
ATOM   1907  CE1 TYR A 248     -11.395 -17.463  27.089  1.00 79.31           C
ANISOU 1907  CE1 TYR A 248    11230   9441   9465  -3312  -2103  -2652       C
ATOM   1908  CE2 TYR A 248     -10.637 -17.143  29.345  1.00 77.38           C
ANISOU 1908  CE2 TYR A 248    11039   8986   9376  -3323  -1886  -2340       C
ATOM   1909  CZ  TYR A 248     -11.587 -16.945  28.358  1.00 85.36           C
ANISOU 1909  CZ  TYR A 248    11950  10172  10309  -3362  -2022  -2443       C
ATOM   1910  OH  TYR A 248     -12.731 -16.225  28.637  1.00 85.98           O
ANISOU 1910  OH  TYR A 248    11875  10400  10394  -3435  -2076  -2335       O
ATOM   1911  N   ASP A 249      -7.005 -21.944  25.483  1.00 84.83           N
ANISOU 1911  N   ASP A 249    12461   9370  10401  -3021  -1942  -3345       N
ATOM   1912  CA  ASP A 249      -5.934 -22.879  25.138  1.00 86.21           C
ANISOU 1912  CA  ASP A 249    12746   9378  10633  -2933  -1901  -3498       C
ATOM   1913  C   ASP A 249      -4.557 -22.234  25.180  1.00 83.01           C
ANISOU 1913  C   ASP A 249    12458   9019  10062  -2780  -1782  -3435       C
ATOM   1914  O   ASP A 249      -3.557 -22.930  25.398  1.00 83.19           O
ANISOU 1914  O   ASP A 249    12569   8859  10179  -2712  -1705  -3481       O
ATOM   1915  CB  ASP A 249      -6.181 -23.478  23.752  1.00 85.31           C
ANISOU 1915  CB  ASP A 249    12628   9326  10461  -2909  -2031  -3759       C
ATOM   1916  CG  ASP A 249      -6.991 -24.760  23.804  1.00 94.57           C
ANISOU 1916  CG  ASP A 249    13739  10294  11897  -3032  -2125  -3879       C
ATOM   1917  OD1 ASP A 249      -8.005 -24.792  24.536  1.00 95.12           O
ANISOU 1917  OD1 ASP A 249    13701  10321  12119  -3171  -2145  -3766       O
ATOM   1918  OD2 ASP A 249      -6.624 -25.729  23.097  1.00 96.23           O
ANISOU 1918  OD2 ASP A 249    14014  10385  12163  -2990  -2185  -4083       O
ATOM   1919  N   HIS A 250      -4.472 -20.928  24.955  1.00 81.26           N
ANISOU 1919  N   HIS A 250    12235   9036   9603  -2721  -1768  -3330       N
ATOM   1920  CA  HIS A 250      -3.181 -20.266  24.855  1.00 77.72           C
ANISOU 1920  CA  HIS A 250    11891   8653   8985  -2572  -1665  -3281       C
ATOM   1921  C   HIS A 250      -2.680 -19.727  26.185  1.00 78.33           C
ANISOU 1921  C   HIS A 250    12005   8639   9118  -2566  -1545  -3050       C
ATOM   1922  O   HIS A 250      -1.551 -19.221  26.246  1.00 76.64           O
ANISOU 1922  O   HIS A 250    11878   8449   8790  -2445  -1452  -2996       O
ATOM   1923  CB  HIS A 250      -3.246 -19.134  23.820  1.00 79.58           C
ANISOU 1923  CB  HIS A 250    12111   9197   8930  -2495  -1712  -3290       C
ATOM   1924  CG  HIS A 250      -4.309 -18.109  24.091  1.00 80.94           C
ANISOU 1924  CG  HIS A 250    12180   9538   9037  -2572  -1769  -3136       C
ATOM   1925  ND1 HIS A 250      -4.017 -16.793  24.388  1.00 80.07           N
ANISOU 1925  ND1 HIS A 250    12076   9577   8769  -2514  -1716  -2955       N
ATOM   1926  CD2 HIS A 250      -5.662 -18.201  24.088  1.00 83.37           C
ANISOU 1926  CD2 HIS A 250    12367   9889   9419  -2698  -1878  -3139       C
ATOM   1927  CE1 HIS A 250      -5.141 -16.122  24.570  1.00 79.34           C
ANISOU 1927  CE1 HIS A 250    11872   9612   8663  -2598  -1790  -2854       C
ATOM   1928  NE2 HIS A 250      -6.154 -16.953  24.393  1.00 83.31           N
ANISOU 1928  NE2 HIS A 250    12294  10057   9302  -2710  -1886  -2961       N
ATOM   1929  N   LEU A 251      -3.474 -19.835  27.247  1.00 78.75           N
ANISOU 1929  N   LEU A 251    11991   8590   9341  -2691  -1547  -2913       N
ATOM   1930  CA  LEU A 251      -3.113 -19.326  28.564  1.00 76.38           C
ANISOU 1930  CA  LEU A 251    11716   8211   9095  -2693  -1444  -2690       C
ATOM   1931  C   LEU A 251      -2.764 -20.488  29.485  1.00 75.93           C
ANISOU 1931  C   LEU A 251    11694   7862   9293  -2731  -1381  -2663       C
ATOM   1932  O   LEU A 251      -3.558 -21.422  29.640  1.00 79.64           O
ANISOU 1932  O   LEU A 251    12098   8205   9956  -2844  -1434  -2713       O
ATOM   1933  CB  LEU A 251      -4.258 -18.507  29.158  1.00 74.39           C
ANISOU 1933  CB  LEU A 251    11344   8081   8841  -2791  -1481  -2527       C
ATOM   1934  CG  LEU A 251      -4.597 -17.212  28.424  1.00 75.73           C
ANISOU 1934  CG  LEU A 251    11452   8542   8779  -2727  -1530  -2494       C
ATOM   1935  CD1 LEU A 251      -5.685 -16.439  29.165  1.00 74.10           C
ANISOU 1935  CD1 LEU A 251    11100   8438   8616  -2789  -1545  -2309       C
ATOM   1936  CD2 LEU A 251      -3.349 -16.360  28.263  1.00 72.41           C
ANISOU 1936  CD2 LEU A 251    11110   8212   8189  -2548  -1437  -2426       C
ATOM   1937  N   TYR A 252      -1.580 -20.428  30.088  1.00 72.86           N
ANISOU 1937  N   TYR A 252    11404   7369   8910  -2634  -1270  -2580       N
ATOM   1938  CA  TYR A 252      -1.103 -21.442  31.015  1.00 71.49           C
ANISOU 1938  CA  TYR A 252    11270   6927   8967  -2647  -1202  -2525       C
ATOM   1939  C   TYR A 252      -0.875 -20.797  32.378  1.00 71.53           C
ANISOU 1939  C   TYR A 252    11266   6912   9001  -2633  -1107  -2267       C
ATOM   1940  O   TYR A 252      -0.465 -19.635  32.463  1.00 67.26           O
ANISOU 1940  O   TYR A 252    10712   6548   8295  -2523  -1057  -2155       O
ATOM   1941  CB  TYR A 252       0.185 -22.113  30.496  1.00 74.82           C
ANISOU 1941  CB  TYR A 252    11795   7236   9397  -2513  -1153  -2663       C
ATOM   1942  CG  TYR A 252      -0.082 -23.074  29.362  1.00 73.60           C
ANISOU 1942  CG  TYR A 252    11623   7050   9293  -2525  -1239  -2914       C
ATOM   1943  CD1 TYR A 252      -0.744 -22.653  28.221  1.00 76.09           C
ANISOU 1943  CD1 TYR A 252    11889   7580   9441  -2540  -1336  -3049       C
ATOM   1944  CD2 TYR A 252       0.301 -24.403  29.440  1.00 77.45           C
ANISOU 1944  CD2 TYR A 252    12135   7294   9998  -2520  -1230  -3015       C
ATOM   1945  CE1 TYR A 252      -1.017 -23.516  27.187  1.00 81.67           C
ANISOU 1945  CE1 TYR A 252    12577   8267  10187  -2549  -1424  -3285       C
ATOM   1946  CE2 TYR A 252       0.033 -25.289  28.397  1.00 76.25           C
ANISOU 1946  CE2 TYR A 252    11963   7108   9900  -2531  -1317  -3260       C
ATOM   1947  CZ  TYR A 252      -0.629 -24.835  27.271  1.00 79.76           C
ANISOU 1947  CZ  TYR A 252    12364   7777  10166  -2545  -1416  -3398       C
ATOM   1948  OH  TYR A 252      -0.916 -25.682  26.215  1.00 82.04           O
ANISOU 1948  OH  TYR A 252    12634   8044  10494  -2551  -1517  -3647       O
ATOM   1949  N   VAL A 253      -1.178 -21.547  33.431  1.00 68.98           N
ANISOU 1949  N   VAL A 253    10920   6394   8896  -2726  -1080  -2159       N
ATOM   1950  CA  VAL A 253      -1.144 -21.049  34.802  1.00 64.29           C
ANISOU 1950  CA  VAL A 253    10278   5801   8350  -2711   -991  -1900       C
ATOM   1951  C   VAL A 253      -0.265 -21.995  35.609  1.00 67.19           C
ANISOU 1951  C   VAL A 253    10726   5913   8891  -2685   -917  -1839       C
ATOM   1952  O   VAL A 253      -0.018 -23.136  35.186  1.00 68.04           O
ANISOU 1952  O   VAL A 253    10890   5832   9131  -2708   -945  -1985       O
ATOM   1953  CB  VAL A 253      -2.565 -20.927  35.404  1.00 65.40           C
ANISOU 1953  CB  VAL A 253    10284   5993   8574  -2862  -1030  -1789       C
ATOM   1954  CG1 VAL A 253      -3.419 -19.963  34.582  1.00 60.67           C
ANISOU 1954  CG1 VAL A 253     9599   5649   7805  -2877  -1110  -1846       C
ATOM   1955  CG2 VAL A 253      -3.210 -22.288  35.528  1.00 62.15           C
ANISOU 1955  CG2 VAL A 253     9861   5359   8395  -3023  -1082  -1857       C
ATOM   1956  N   PRO A 254       0.258 -21.551  36.763  1.00 65.22           N
ANISOU 1956  N   PRO A 254    10471   5662   8648  -2618   -820  -1624       N
ATOM   1957  CA  PRO A 254       1.023 -22.473  37.620  1.00 64.09           C
ANISOU 1957  CA  PRO A 254    10395   5279   8679  -2599   -756  -1540       C
ATOM   1958  C   PRO A 254       0.139 -23.590  38.155  1.00 67.84           C
ANISOU 1958  C   PRO A 254    10829   5559   9390  -2770   -790  -1505       C
ATOM   1959  O   PRO A 254      -1.006 -23.365  38.557  1.00 69.13           O
ANISOU 1959  O   PRO A 254    10884   5800   9580  -2889   -815  -1417       O
ATOM   1960  CB  PRO A 254       1.548 -21.573  38.750  1.00 63.74           C
ANISOU 1960  CB  PRO A 254    10328   5330   8561  -2506   -659  -1309       C
ATOM   1961  CG  PRO A 254       1.156 -20.163  38.381  1.00 61.47           C
ANISOU 1961  CG  PRO A 254     9972   5321   8063  -2463   -671  -1293       C
ATOM   1962  CD  PRO A 254      -0.003 -20.275  37.457  1.00 64.99           C
ANISOU 1962  CD  PRO A 254    10360   5836   8497  -2579   -774  -1437       C
ATOM   1963  N   ALA A 255       0.685 -24.808  38.166  1.00 68.25           N
ANISOU 1963  N   ALA A 255    10924   5383   9625  -2746   -780  -1560       N
ATOM   1964  CA  ALA A 255      -0.154 -25.958  38.486  1.00 71.70           C
ANISOU 1964  CA  ALA A 255    11282   5655  10307  -2872   -812  -1543       C
ATOM   1965  C   ALA A 255      -0.678 -25.882  39.909  1.00 73.98           C
ANISOU 1965  C   ALA A 255    11504   5924  10682  -2959   -757  -1276       C
ATOM   1966  O   ALA A 255      -1.794 -26.341  40.179  1.00 76.97           O
ANISOU 1966  O   ALA A 255    11780   6272  11194  -3098   -788  -1233       O
ATOM   1967  CB  ALA A 255       0.608 -27.269  38.264  1.00 70.71           C
ANISOU 1967  CB  ALA A 255    11205   5284  10376  -2812   -804  -1644       C
ATOM   1968  N   GLY A 256       0.091 -25.287  40.818  1.00 70.59           N
ANISOU 1968  N   GLY A 256    11124   5526  10172  -2877   -673  -1097       N
ATOM   1969  CA  GLY A 256      -0.242 -25.269  42.226  1.00 70.50           C
ANISOU 1969  CA  GLY A 256    11054   5498  10232  -2938   -610   -838       C
ATOM   1970  C   GLY A 256      -0.879 -24.002  42.762  1.00 69.78           C
ANISOU 1970  C   GLY A 256    10886   5651   9975  -2967   -584   -706       C
ATOM   1971  O   GLY A 256      -1.008 -23.876  43.987  1.00 67.59           O
ANISOU 1971  O   GLY A 256    10562   5394   9726  -2988   -517   -486       O
ATOM   1972  N   SER A 257      -1.303 -23.073  41.902  1.00 59.65           N
ANISOU 1972  N   SER A 257     9563   4578   8524  -2945   -631   -827       N
ATOM   1973  CA  SER A 257      -1.907 -21.840  42.395  1.00 60.96           C
ANISOU 1973  CA  SER A 257     9624   4993   8545  -2936   -601   -704       C
ATOM   1974  C   SER A 257      -3.096 -22.135  43.302  1.00 61.65           C
ANISOU 1974  C   SER A 257     9596   5076   8754  -3094   -591   -554       C
ATOM   1975  O   SER A 257      -3.847 -23.091  43.087  1.00 67.04           O
ANISOU 1975  O   SER A 257    10249   5622   9603  -3241   -645   -606       O
ATOM   1976  CB  SER A 257      -2.348 -20.950  41.234  1.00 58.24           C
ANISOU 1976  CB  SER A 257     9244   4850   8036  -2911   -671   -862       C
ATOM   1977  OG  SER A 257      -1.234 -20.470  40.519  1.00 58.11           O
ANISOU 1977  OG  SER A 257     9321   4880   7878  -2755   -662   -964       O
ATOM   1978  N   GLU A 258      -3.246 -21.325  44.351  1.00 59.86           N
ANISOU 1978  N   GLU A 258     9300   4998   8447  -3064   -516   -365       N
ATOM   1979  CA  GLU A 258      -4.403 -21.486  45.225  1.00 63.75           C
ANISOU 1979  CA  GLU A 258     9669   5524   9030  -3207   -495   -218       C
ATOM   1980  C   GLU A 258      -5.699 -21.220  44.471  1.00 64.52           C
ANISOU 1980  C   GLU A 258     9656   5738   9120  -3318   -577   -327       C
ATOM   1981  O   GLU A 258      -6.637 -22.018  44.532  1.00 65.04           O
ANISOU 1981  O   GLU A 258     9655   5713   9346  -3480   -612   -322       O
ATOM   1982  CB  GLU A 258      -4.293 -20.555  46.431  1.00 60.33           C
ANISOU 1982  CB  GLU A 258     9181   5258   8484  -3138   -399    -19       C
ATOM   1983  CG  GLU A 258      -3.131 -20.866  47.331  1.00 63.79           C
ANISOU 1983  CG  GLU A 258     9708   5591   8937  -3047   -321    115       C
ATOM   1984  CD  GLU A 258      -3.329 -22.128  48.133  1.00 66.57           C
ANISOU 1984  CD  GLU A 258    10061   5742   9489  -3165   -295    252       C
ATOM   1985  OE1 GLU A 258      -4.465 -22.347  48.635  1.00 64.91           O
ANISOU 1985  OE1 GLU A 258     9740   5565   9357  -3308   -287    347       O
ATOM   1986  OE2 GLU A 258      -2.339 -22.891  48.248  1.00 67.48           O
ANISOU 1986  OE2 GLU A 258    10286   5667   9687  -3112   -283    268       O
ATOM   1987  N   VAL A 259      -5.771 -20.099  43.752  1.00 60.53           N
ANISOU 1987  N   VAL A 259     9127   5435   8438  -3233   -610   -423       N
ATOM   1988  CA  VAL A 259      -6.980 -19.695  43.050  1.00 58.60           C
ANISOU 1988  CA  VAL A 259     8769   5331   8165  -3320   -691   -515       C
ATOM   1989  C   VAL A 259      -6.614 -19.214  41.658  1.00 60.69           C
ANISOU 1989  C   VAL A 259     9092   5673   8293  -3232   -770   -715       C
ATOM   1990  O   VAL A 259      -5.676 -18.426  41.490  1.00 57.37           O
ANISOU 1990  O   VAL A 259     8739   5334   7723  -3076   -736   -721       O
ATOM   1991  CB  VAL A 259      -7.729 -18.579  43.796  1.00 59.47           C
ANISOU 1991  CB  VAL A 259     8744   5667   8186  -3313   -642   -376       C
ATOM   1992  CG1 VAL A 259      -8.900 -18.116  42.970  1.00 60.25           C
ANISOU 1992  CG1 VAL A 259     8727   5915   8252  -3384   -734   -480       C
ATOM   1993  CG2 VAL A 259      -8.183 -19.050  45.177  1.00 61.13           C
ANISOU 1993  CG2 VAL A 259     8883   5827   8516  -3408   -559   -175       C
ATOM   1994  N   VAL A 260      -7.360 -19.674  40.659  1.00 60.09           N
ANISOU 1994  N   VAL A 260     8985   5580   8265  -3333   -877   -877       N
ATOM   1995  CA  VAL A 260      -7.218 -19.185  39.290  1.00 63.34           C
ANISOU 1995  CA  VAL A 260     9432   6103   8533  -3266   -963  -1066       C
ATOM   1996  C   VAL A 260      -8.538 -18.546  38.888  1.00 65.10           C
ANISOU 1996  C   VAL A 260     9508   6518   8709  -3344  -1039  -1090       C
ATOM   1997  O   VAL A 260      -9.581 -19.210  38.898  1.00 66.72           O
ANISOU 1997  O   VAL A 260     9625   6673   9053  -3504  -1094  -1112       O
ATOM   1998  CB  VAL A 260      -6.842 -20.308  38.312  1.00 66.06           C
ANISOU 1998  CB  VAL A 260     9879   6267   8954  -3304  -1037  -1271       C
ATOM   1999  CG1 VAL A 260      -6.705 -19.748  36.905  1.00 63.38           C
ANISOU 1999  CG1 VAL A 260     9572   6074   8437  -3230  -1121  -1459       C
ATOM   2000  CG2 VAL A 260      -5.562 -20.982  38.753  1.00 65.65           C
ANISOU 2000  CG2 VAL A 260     9962   6013   8968  -3225   -961  -1241       C
ATOM   2001  N   LEU A 261      -8.498 -17.265  38.551  1.00 59.95           N
ANISOU 2001  N   LEU A 261     8823   6081   7875  -3233  -1043  -1079       N
ATOM   2002  CA  LEU A 261      -9.663 -16.547  38.040  1.00 65.23           C
ANISOU 2002  CA  LEU A 261     9356   6946   8483  -3281  -1124  -1108       C
ATOM   2003  C   LEU A 261      -9.504 -16.414  36.533  1.00 65.21           C
ANISOU 2003  C   LEU A 261     9407   7017   8355  -3240  -1233  -1305       C
ATOM   2004  O   LEU A 261      -8.628 -15.682  36.058  1.00 66.41           O
ANISOU 2004  O   LEU A 261     9636   7252   8346  -3093  -1215  -1327       O
ATOM   2005  CB  LEU A 261      -9.807 -15.174  38.692  1.00 61.60           C
ANISOU 2005  CB  LEU A 261     8811   6677   7915  -3186  -1059   -955       C
ATOM   2006  CG  LEU A 261      -9.741 -15.078  40.212  1.00 60.74           C
ANISOU 2006  CG  LEU A 261     8666   6537   7877  -3185   -935   -759       C
ATOM   2007  CD1 LEU A 261      -9.820 -13.639  40.654  1.00 54.13           C
ANISOU 2007  CD1 LEU A 261     7754   5898   6917  -3074   -885   -652       C
ATOM   2008  CD2 LEU A 261     -10.880 -15.867  40.818  1.00 63.72           C
ANISOU 2008  CD2 LEU A 261     8929   6854   8429  -3363   -941   -702       C
ATOM   2009  N   GLU A 262     -10.336 -17.130  35.785  1.00 66.49           N
ANISOU 2009  N   GLU A 262     9524   7151   8588  -3371  -1345  -1446       N
ATOM   2010  CA  GLU A 262     -10.293 -17.110  34.329  1.00 70.46           C
ANISOU 2010  CA  GLU A 262    10070   7734   8969  -3349  -1460  -1647       C
ATOM   2011  C   GLU A 262     -11.383 -16.183  33.813  1.00 69.88           C
ANISOU 2011  C   GLU A 262     9855   7897   8800  -3369  -1549  -1645       C
ATOM   2012  O   GLU A 262     -12.559 -16.347  34.156  1.00 71.53           O
ANISOU 2012  O   GLU A 262     9925   8131   9122  -3498  -1589  -1606       O
ATOM   2013  CB  GLU A 262     -10.468 -18.516  33.745  1.00 66.85           C
ANISOU 2013  CB  GLU A 262     9660   7095   8646  -3477  -1541  -1832       C
ATOM   2014  CG  GLU A 262      -9.466 -19.562  34.257  1.00 70.95           C
ANISOU 2014  CG  GLU A 262    10311   7351   9296  -3468  -1461  -1838       C
ATOM   2015  CD  GLU A 262      -9.538 -20.885  33.483  1.00 80.97           C
ANISOU 2015  CD  GLU A 262    11624   8450  10689  -3547  -1543  -2048       C
ATOM   2016  OE1 GLU A 262      -9.762 -20.848  32.254  1.00 83.63           O
ANISOU 2016  OE1 GLU A 262    11952   8897  10925  -3523  -1643  -2230       O
ATOM   2017  OE2 GLU A 262      -9.367 -21.959  34.098  1.00 83.09           O
ANISOU 2017  OE2 GLU A 262    11912   8493  11167  -3591  -1495  -2019       O
ATOM   2018  N   GLY A 263     -10.995 -15.222  32.999  1.00 64.10           N
ANISOU 2018  N   GLY A 263     9151   7337   7867  -3241  -1579  -1680       N
ATOM   2019  CA  GLY A 263     -11.939 -14.261  32.496  1.00 67.42           C
ANISOU 2019  CA  GLY A 263     9442   7985   8189  -3239  -1663  -1662       C
ATOM   2020  C   GLY A 263     -11.404 -13.520  31.296  1.00 71.21           C
ANISOU 2020  C   GLY A 263     9985   8624   8448  -3115  -1720  -1745       C
ATOM   2021  O   GLY A 263     -10.508 -13.992  30.591  1.00 69.71           O
ANISOU 2021  O   GLY A 263     9930   8373   8185  -3067  -1727  -1875       O
ATOM   2022  N   HIS A 264     -11.975 -12.343  31.066  1.00 71.47           N
ANISOU 2022  N   HIS A 264     9912   8866   8376  -3061  -1759  -1665       N
ATOM   2023  CA  HIS A 264     -11.603 -11.547  29.909  1.00 72.47           C
ANISOU 2023  CA  HIS A 264    10078   9166   8290  -2949  -1821  -1718       C
ATOM   2024  C   HIS A 264     -11.813 -10.075  30.212  1.00 71.64           C
ANISOU 2024  C   HIS A 264     9883   9230   8109  -2843  -1791  -1546       C
ATOM   2025  O   HIS A 264     -12.743  -9.701  30.934  1.00 70.38           O
ANISOU 2025  O   HIS A 264     9583   9112   8047  -2892  -1786  -1440       O
ATOM   2026  CB  HIS A 264     -12.421 -11.928  28.669  1.00 74.51           C
ANISOU 2026  CB  HIS A 264    10291   9532   8488  -3036  -1987  -1889       C
ATOM   2027  CG  HIS A 264     -13.902 -11.750  28.831  1.00 72.20           C
ANISOU 2027  CG  HIS A 264     9814   9337   8284  -3147  -2074  -1849       C
ATOM   2028  ND1 HIS A 264     -14.740 -12.771  29.225  1.00 80.45           N
ANISOU 2028  ND1 HIS A 264    10786  10264   9516  -3317  -2111  -1906       N
ATOM   2029  CD2 HIS A 264     -14.693 -10.664  28.653  1.00 75.11           C
ANISOU 2029  CD2 HIS A 264    10047   9906   8587  -3112  -2131  -1755       C
ATOM   2030  CE1 HIS A 264     -15.986 -12.327  29.264  1.00 77.16           C
ANISOU 2030  CE1 HIS A 264    10196   9981   9140  -3383  -2187  -1854       C
ATOM   2031  NE2 HIS A 264     -15.984 -11.051  28.924  1.00 77.31           N
ANISOU 2031  NE2 HIS A 264    10173  10193   9008  -3257  -2201  -1764       N
ATOM   2032  N   ILE A 265     -10.945  -9.242  29.640  1.00 73.28           N
ANISOU 2032  N   ILE A 265    10165   9532   8145  -2698  -1771  -1522       N
ATOM   2033  CA  ILE A 265     -11.180  -7.808  29.664  1.00 70.72           C
ANISOU 2033  CA  ILE A 265     9754   9377   7738  -2597  -1769  -1379       C
ATOM   2034  C   ILE A 265     -12.414  -7.506  28.827  1.00 76.36           C
ANISOU 2034  C   ILE A 265    10338  10270   8407  -2654  -1920  -1418       C
ATOM   2035  O   ILE A 265     -12.546  -7.972  27.684  1.00 76.10           O
ANISOU 2035  O   ILE A 265    10338  10302   8275  -2693  -2031  -1564       O
ATOM   2036  CB  ILE A 265      -9.948  -7.036  29.165  1.00 72.82           C
ANISOU 2036  CB  ILE A 265    10133   9698   7839  -2437  -1717  -1343       C
ATOM   2037  CG1 ILE A 265      -8.771  -7.195  30.137  1.00 73.84           C
ANISOU 2037  CG1 ILE A 265    10367   9661   8028  -2374  -1566  -1281       C
ATOM   2038  CG2 ILE A 265     -10.279  -5.566  28.981  1.00 69.99           C
ANISOU 2038  CG2 ILE A 265     9678   9518   7396  -2340  -1741  -1208       C
ATOM   2039  CD1 ILE A 265      -7.410  -7.212  29.473  1.00 74.11           C
ANISOU 2039  CD1 ILE A 265    10553   9679   7928  -2269  -1523  -1336       C
ATOM   2040  N   ILE A 266     -13.344  -6.754  29.408  1.00 74.50           N
ANISOU 2040  N   ILE A 266     9948  10116   8243  -2662  -1926  -1295       N
ATOM   2041  CA  ILE A 266     -14.597  -6.435  28.736  1.00 72.54           C
ANISOU 2041  CA  ILE A 266     9552  10035   7973  -2716  -2069  -1315       C
ATOM   2042  C   ILE A 266     -14.321  -5.307  27.750  1.00 73.41           C
ANISOU 2042  C   ILE A 266     9671  10328   7892  -2585  -2127  -1270       C
ATOM   2043  O   ILE A 266     -13.900  -4.215  28.154  1.00 72.73           O
ANISOU 2043  O   ILE A 266     9577  10276   7780  -2461  -2052  -1126       O
ATOM   2044  CB  ILE A 266     -15.690  -6.072  29.752  1.00 74.33           C
ANISOU 2044  CB  ILE A 266     9604  10280   8360  -2769  -2047  -1200       C
ATOM   2045  CG1 ILE A 266     -15.916  -7.248  30.707  1.00 71.80           C
ANISOU 2045  CG1 ILE A 266     9281   9779   8222  -2906  -1984  -1234       C
ATOM   2046  CG2 ILE A 266     -16.990  -5.746  29.033  1.00 73.59           C
ANISOU 2046  CG2 ILE A 266     9348  10363   8250  -2822  -2200  -1221       C
ATOM   2047  CD1 ILE A 266     -17.029  -7.040  31.691  1.00 74.19           C
ANISOU 2047  CD1 ILE A 266     9406  10103   8680  -2975  -1958  -1133       C
ATOM   2048  N   PRO A 267     -14.551  -5.522  26.457  1.00 81.72           N
ANISOU 2048  N   PRO A 267    10737  11504   8809  -2608  -2262  -1387       N
ATOM   2049  CA  PRO A 267     -14.157  -4.515  25.464  1.00 83.68           C
ANISOU 2049  CA  PRO A 267    11012  11927   8858  -2480  -2311  -1336       C
ATOM   2050  C   PRO A 267     -15.000  -3.250  25.568  1.00 83.99           C
ANISOU 2050  C   PRO A 267    10889  12114   8910  -2422  -2357  -1177       C
ATOM   2051  O   PRO A 267     -16.214  -3.304  25.784  1.00 85.40           O
ANISOU 2051  O   PRO A 267    10915  12341   9193  -2506  -2432  -1172       O
ATOM   2052  CB  PRO A 267     -14.383  -5.232  24.128  1.00 84.68           C
ANISOU 2052  CB  PRO A 267    11175  12153   8848  -2546  -2455  -1517       C
ATOM   2053  CG  PRO A 267     -15.460  -6.213  24.425  1.00 87.22           C
ANISOU 2053  CG  PRO A 267    11402  12412   9327  -2714  -2526  -1622       C
ATOM   2054  CD  PRO A 267     -15.234  -6.672  25.840  1.00 78.48           C
ANISOU 2054  CD  PRO A 267    10308  11087   8422  -2755  -2382  -1568       C
ATOM   2055  N   ARG A 268     -14.332  -2.103  25.404  1.00 82.37           N
ANISOU 2055  N   ARG A 268    10715  11976   8606  -2274  -2310  -1047       N
ATOM   2056  CA  ARG A 268     -14.971  -0.785  25.322  1.00 83.90           C
ANISOU 2056  CA  ARG A 268    10773  12314   8793  -2192  -2359   -892       C
ATOM   2057  C   ARG A 268     -15.643  -0.359  26.624  1.00 84.39           C
ANISOU 2057  C   ARG A 268    10701  12307   9055  -2201  -2289   -786       C
ATOM   2058  O   ARG A 268     -16.564   0.464  26.613  1.00 85.83           O
ANISOU 2058  O   ARG A 268    10730  12604   9279  -2175  -2354   -694       O
ATOM   2059  CB  ARG A 268     -15.995  -0.727  24.189  1.00 84.84           C
ANISOU 2059  CB  ARG A 268    10790  12629   8818  -2236  -2544   -938       C
ATOM   2060  CG  ARG A 268     -15.535  -1.372  22.907  1.00 89.66           C
ANISOU 2060  CG  ARG A 268    11517  13319   9231  -2257  -2629  -1081       C
ATOM   2061  CD  ARG A 268     -16.467  -1.004  21.766  1.00 90.72           C
ANISOU 2061  CD  ARG A 268    11544  13682   9243  -2267  -2813  -1087       C
ATOM   2062  NE  ARG A 268     -16.528   0.438  21.544  1.00 93.62           N
ANISOU 2062  NE  ARG A 268    11840  14178   9554  -2133  -2829   -891       N
ATOM   2063  CZ  ARG A 268     -15.536   1.172  21.056  1.00 92.70           C
ANISOU 2063  CZ  ARG A 268    11821  14109   9291  -2006  -2782   -799       C
ATOM   2064  NH1 ARG A 268     -14.380   0.631  20.704  1.00 92.22           N
ANISOU 2064  NH1 ARG A 268    11933  13995   9111  -1989  -2712   -887       N
ATOM   2065  NH2 ARG A 268     -15.712   2.482  20.908  1.00 94.35           N
ANISOU 2065  NH2 ARG A 268    11947  14421   9481  -1894  -2804   -611       N
ATOM   2066  N   VAL A 269     -15.195  -0.887  27.755  1.00 80.25           N
ANISOU 2066  N   VAL A 269    10230  11607   8654  -2234  -2156   -794       N
ATOM   2067  CA  VAL A 269     -15.732  -0.510  29.054  1.00 77.27           C
ANISOU 2067  CA  VAL A 269     9738  11171   8451  -2239  -2072   -698       C
ATOM   2068  C   VAL A 269     -14.621   0.141  29.860  1.00 71.50           C
ANISOU 2068  C   VAL A 269     9093  10342   7732  -2121  -1921   -599       C
ATOM   2069  O   VAL A 269     -13.511  -0.397  29.949  1.00 73.14           O
ANISOU 2069  O   VAL A 269     9456  10437   7896  -2108  -1843   -645       O
ATOM   2070  CB  VAL A 269     -16.328  -1.718  29.797  1.00 73.30           C
ANISOU 2070  CB  VAL A 269     9197  10559   8095  -2394  -2051   -781       C
ATOM   2071  CG1 VAL A 269     -16.778  -1.315  31.181  1.00 62.28           C
ANISOU 2071  CG1 VAL A 269     7690   9113   6859  -2391  -1946   -676       C
ATOM   2072  CG2 VAL A 269     -17.501  -2.247  29.016  1.00 71.73           C
ANISOU 2072  CG2 VAL A 269     8890  10464   7898  -2511  -2208   -874       C
ATOM   2073  N   ARG A 270     -14.920   1.318  30.406  1.00 72.05           N
ANISOU 2073  N   ARG A 270     9057  10457   7862  -2031  -1887   -469       N
ATOM   2074  CA  ARG A 270     -14.049   2.043  31.317  1.00 65.26           C
ANISOU 2074  CA  ARG A 270     8245   9510   7042  -1924  -1749   -374       C
ATOM   2075  C   ARG A 270     -14.897   2.524  32.483  1.00 65.53           C
ANISOU 2075  C   ARG A 270     8125   9539   7233  -1928  -1696   -304       C
ATOM   2076  O   ARG A 270     -15.946   3.142  32.263  1.00 64.63           O
ANISOU 2076  O   ARG A 270     7856   9540   7159  -1919  -1776   -262       O
ATOM   2077  CB  ARG A 270     -13.378   3.231  30.627  1.00 64.09           C
ANISOU 2077  CB  ARG A 270     8134   9431   6786  -1780  -1763   -283       C
ATOM   2078  CG  ARG A 270     -12.499   2.855  29.475  1.00 66.85           C
ANISOU 2078  CG  ARG A 270     8630   9804   6965  -1765  -1804   -342       C
ATOM   2079  CD  ARG A 270     -11.171   2.346  29.948  1.00 67.43           C
ANISOU 2079  CD  ARG A 270     8865   9732   7022  -1746  -1679   -376       C
ATOM   2080  NE  ARG A 270     -10.318   2.025  28.816  1.00 73.34           N
ANISOU 2080  NE  ARG A 270     9747  10515   7604  -1722  -1711   -436       N
ATOM   2081  CZ  ARG A 270     -10.420   0.917  28.095  1.00 79.94           C
ANISOU 2081  CZ  ARG A 270    10643  11363   8368  -1813  -1778   -575       C
ATOM   2082  NH1 ARG A 270     -11.301  -0.028  28.395  1.00 76.79           N
ANISOU 2082  NH1 ARG A 270    10188  10929   8061  -1941  -1821   -667       N
ATOM   2083  NH2 ARG A 270      -9.615   0.748  27.049  1.00 86.61           N
ANISOU 2083  NH2 ARG A 270    11603  12256   9048  -1775  -1801   -628       N
ATOM   2084  N   THR A 271     -14.444   2.236  33.712  1.00 63.23           N
ANISOU 2084  N   THR A 271     7873   9125   7028  -1938  -1562   -293       N
ATOM   2085  CA  THR A 271     -15.159   2.584  34.935  1.00 61.57           C
ANISOU 2085  CA  THR A 271     7528   8910   6957  -1945  -1490   -238       C
ATOM   2086  C   THR A 271     -14.157   3.038  35.988  1.00 62.51           C
ANISOU 2086  C   THR A 271     7720   8930   7100  -1857  -1345   -182       C
ATOM   2087  O   THR A 271     -12.972   2.700  35.926  1.00 64.86           O
ANISOU 2087  O   THR A 271     8176   9137   7330  -1831  -1293   -202       O
ATOM   2088  CB  THR A 271     -15.954   1.405  35.500  1.00 62.91           C
ANISOU 2088  CB  THR A 271     7639   9042   7221  -2101  -1482   -298       C
ATOM   2089  OG1 THR A 271     -15.077   0.279  35.629  1.00 65.37           O
ANISOU 2089  OG1 THR A 271     8110   9221   7506  -2163  -1430   -363       O
ATOM   2090  CG2 THR A 271     -17.122   1.048  34.593  1.00 61.58           C
ANISOU 2090  CG2 THR A 271     7361   8982   7056  -2193  -1629   -352       C
ATOM   2091  N   VAL A 272     -14.660   3.775  36.982  1.00 58.78           N
ANISOU 2091  N   VAL A 272     7126   8480   6727  -1814  -1281   -120       N
ATOM   2092  CA  VAL A 272     -13.803   4.375  38.003  1.00 57.42           C
ANISOU 2092  CA  VAL A 272     7002   8235   6580  -1721  -1153    -71       C
ATOM   2093  C   VAL A 272     -13.082   3.281  38.776  1.00 58.54           C
ANISOU 2093  C   VAL A 272     7264   8257   6723  -1791  -1057   -107       C
ATOM   2094  O   VAL A 272     -13.711   2.395  39.374  1.00 55.17           O
ANISOU 2094  O   VAL A 272     6789   7812   6362  -1905  -1033   -131       O
ATOM   2095  CB  VAL A 272     -14.623   5.258  38.945  1.00 56.57           C
ANISOU 2095  CB  VAL A 272     6729   8185   6582  -1674  -1106    -20       C
ATOM   2096  CG1 VAL A 272     -13.699   5.957  39.970  1.00 49.97           C
ANISOU 2096  CG1 VAL A 272     5943   7280   5763  -1571   -981     17       C
ATOM   2097  CG2 VAL A 272     -15.470   6.260  38.148  1.00 52.53           C
ANISOU 2097  CG2 VAL A 272     6082   7789   6087  -1611  -1213     18       C
ATOM   2098  N   GLU A 273     -11.755   3.340  38.760  1.00 56.39           N
ANISOU 2098  N   GLU A 273     7142   7901   6384  -1724  -1003   -103       N
ATOM   2099  CA  GLU A 273     -10.895   2.414  39.482  1.00 56.39           C
ANISOU 2099  CA  GLU A 273     7264   7780   6382  -1766   -912   -125       C
ATOM   2100  C   GLU A 273      -9.984   3.213  40.406  1.00 51.47           C
ANISOU 2100  C   GLU A 273     6678   7113   5765  -1656   -805    -71       C
ATOM   2101  O   GLU A 273      -9.487   4.284  40.034  1.00 54.12           O
ANISOU 2101  O   GLU A 273     7023   7472   6068  -1542   -815    -37       O
ATOM   2102  CB  GLU A 273     -10.063   1.567  38.496  1.00 56.25           C
ANISOU 2102  CB  GLU A 273     7401   7697   6273  -1794   -955   -189       C
ATOM   2103  CG  GLU A 273      -9.286   0.420  39.109  1.00 52.80           C
ANISOU 2103  CG  GLU A 273     7086   7127   5849  -1852   -879   -219       C
ATOM   2104  CD  GLU A 273      -7.918   0.852  39.579  1.00 56.26           C
ANISOU 2104  CD  GLU A 273     7633   7495   6250  -1745   -789   -183       C
ATOM   2105  OE1 GLU A 273      -7.435   1.890  39.092  1.00 57.90           O
ANISOU 2105  OE1 GLU A 273     7851   7746   6403  -1637   -802   -152       O
ATOM   2106  OE2 GLU A 273      -7.329   0.172  40.447  1.00 57.32           O
ANISOU 2106  OE2 GLU A 273     7835   7531   6413  -1770   -707   -177       O
ATOM   2107  N   GLY A 274      -9.764   2.691  41.604  1.00 52.04           N
ANISOU 2107  N   GLY A 274     6769   7124   5882  -1692   -707    -61       N
ATOM   2108  CA  GLY A 274      -8.972   3.376  42.593  1.00 49.21           C
ANISOU 2108  CA  GLY A 274     6436   6733   5530  -1598   -608    -20       C
ATOM   2109  C   GLY A 274      -9.788   4.344  43.430  1.00 50.26           C
ANISOU 2109  C   GLY A 274     6414   6951   5733  -1553   -571     13       C
ATOM   2110  O   GLY A 274     -11.021   4.370  43.365  1.00 45.14           O
ANISOU 2110  O   GLY A 274     5631   6384   5138  -1605   -611     11       O
ATOM   2111  N   PRO A 275      -9.110   5.144  44.275  1.00 47.99           N
ANISOU 2111  N   PRO A 275     6137   6645   5451  -1457   -491     37       N
ATOM   2112  CA  PRO A 275      -7.651   5.149  44.499  1.00 50.70           C
ANISOU 2112  CA  PRO A 275     6624   6898   5742  -1395   -437     42       C
ATOM   2113  C   PRO A 275      -7.071   3.864  45.078  1.00 46.53           C
ANISOU 2113  C   PRO A 275     6201   6286   5191  -1473   -381     36       C
ATOM   2114  O   PRO A 275      -7.807   2.980  45.557  1.00 48.19           O
ANISOU 2114  O   PRO A 275     6369   6506   5436  -1578   -364     36       O
ATOM   2115  CB  PRO A 275      -7.429   6.294  45.505  1.00 48.23           C
ANISOU 2115  CB  PRO A 275     6251   6608   5466  -1293   -366     61       C
ATOM   2116  CG  PRO A 275      -8.743   6.929  45.760  1.00 49.99           C
ANISOU 2116  CG  PRO A 275     6302   6932   5760  -1291   -380     62       C
ATOM   2117  CD  PRO A 275      -9.826   6.147  45.082  1.00 47.98           C
ANISOU 2117  CD  PRO A 275     5990   6723   5518  -1399   -452     53       C
ATOM   2118  N   PHE A 276      -5.749   3.748  44.992  1.00 45.04           N
ANISOU 2118  N   PHE A 276     6147   6014   4952  -1423   -354     35       N
ATOM   2119  CA  PHE A 276      -5.046   2.644  45.626  1.00 47.88           C
ANISOU 2119  CA  PHE A 276     6609   6285   5297  -1474   -296     39       C
ATOM   2120  C   PHE A 276      -3.619   3.078  45.922  1.00 43.71           C
ANISOU 2120  C   PHE A 276     6181   5698   4730  -1376   -246     50       C
ATOM   2121  O   PHE A 276      -3.072   3.939  45.240  1.00 42.70           O
ANISOU 2121  O   PHE A 276     6075   5573   4578  -1290   -275     47       O
ATOM   2122  CB  PHE A 276      -5.055   1.381  44.746  1.00 43.85           C
ANISOU 2122  CB  PHE A 276     6181   5710   4771  -1568   -351      2       C
ATOM   2123  CG  PHE A 276      -4.589   0.146  45.470  1.00 44.25           C
ANISOU 2123  CG  PHE A 276     6314   5665   4836  -1636   -295     14       C
ATOM   2124  CD1 PHE A 276      -5.349  -0.398  46.503  1.00 45.25           C
ANISOU 2124  CD1 PHE A 276     6369   5808   5016  -1720   -247     51       C
ATOM   2125  CD2 PHE A 276      -3.390  -0.466  45.133  1.00 43.35           C
ANISOU 2125  CD2 PHE A 276     6342   5444   4685  -1615   -287     -5       C
ATOM   2126  CE1 PHE A 276      -4.927  -1.538  47.180  1.00 44.13           C
ANISOU 2126  CE1 PHE A 276     6300   5573   4893  -1783   -197     80       C
ATOM   2127  CE2 PHE A 276      -2.957  -1.600  45.804  1.00 41.85           C
ANISOU 2127  CE2 PHE A 276     6224   5156   4520  -1671   -239     15       C
ATOM   2128  CZ  PHE A 276      -3.724  -2.139  46.830  1.00 42.89           C
ANISOU 2128  CZ  PHE A 276     6288   5300   4707  -1756   -197     62       C
ATOM   2129  N   GLY A 277      -3.017   2.471  46.942  1.00 44.74           N
ANISOU 2129  N   GLY A 277     6366   5775   4857  -1390   -174     72       N
ATOM   2130  CA  GLY A 277      -1.630   2.781  47.252  1.00 42.19           C
ANISOU 2130  CA  GLY A 277     6135   5394   4500  -1303   -131     81       C
ATOM   2131  C   GLY A 277      -0.676   2.320  46.162  1.00 44.25           C
ANISOU 2131  C   GLY A 277     6520   5573   4720  -1288   -168     57       C
ATOM   2132  O   GLY A 277      -0.934   1.353  45.432  1.00 45.35           O
ANISOU 2132  O   GLY A 277     6704   5674   4854  -1362   -211     28       O
ATOM   2133  N   GLU A 278       0.453   3.025  46.063  1.00 40.81           N
ANISOU 2133  N   GLU A 278     6137   5112   4258  -1190   -150     62       N
ATOM   2134  CA  GLU A 278       1.534   2.715  45.128  1.00 44.18           C
ANISOU 2134  CA  GLU A 278     6678   5470   4639  -1157   -168     42       C
ATOM   2135  C   GLU A 278       2.841   2.665  45.910  1.00 44.57           C
ANISOU 2135  C   GLU A 278     6798   5455   4682  -1098   -104     62       C
ATOM   2136  O   GLU A 278       2.951   3.244  46.997  1.00 42.08           O
ANISOU 2136  O   GLU A 278     6436   5167   4386  -1062    -59     87       O
ATOM   2137  CB  GLU A 278       1.607   3.747  43.972  1.00 46.32           C
ANISOU 2137  CB  GLU A 278     6930   5787   4883  -1092   -219     38       C
ATOM   2138  CG  GLU A 278       0.281   3.876  43.250  1.00 48.73           C
ANISOU 2138  CG  GLU A 278     7152   6169   5194  -1142   -290     25       C
ATOM   2139  CD  GLU A 278       0.277   4.847  42.090  1.00 58.31           C
ANISOU 2139  CD  GLU A 278     8343   7436   6375  -1082   -348     37       C
ATOM   2140  OE1 GLU A 278       0.896   5.936  42.182  1.00 60.68           O
ANISOU 2140  OE1 GLU A 278     8629   7739   6686   -991   -327     73       O
ATOM   2141  OE2 GLU A 278      -0.377   4.512  41.073  1.00 60.42           O
ANISOU 2141  OE2 GLU A 278     8602   7745   6608  -1129   -419     13       O
ATOM   2142  N   PHE A 279       3.836   1.973  45.349  1.00 42.57           N
ANISOU 2142  N   PHE A 279     6655   5123   4399  -1087   -103     45       N
ATOM   2143  CA  PHE A 279       5.076   1.746  46.097  1.00 40.26           C
ANISOU 2143  CA  PHE A 279     6429   4764   4104  -1039    -47     65       C
ATOM   2144  C   PHE A 279       5.777   3.024  46.599  1.00 41.41           C
ANISOU 2144  C   PHE A 279     6540   4942   4254   -942    -17     88       C
ATOM   2145  O   PHE A 279       6.436   2.945  47.647  1.00 42.02           O
ANISOU 2145  O   PHE A 279     6631   4996   4338   -916     29    110       O
ATOM   2146  CB  PHE A 279       6.037   0.847  45.277  1.00 40.93           C
ANISOU 2146  CB  PHE A 279     6629   4760   4162  -1032    -52     34       C
ATOM   2147  CG  PHE A 279       6.619   1.500  44.050  1.00 44.67           C
ANISOU 2147  CG  PHE A 279     7129   5253   4591   -969    -76     11       C
ATOM   2148  CD1 PHE A 279       5.952   1.439  42.823  1.00 49.30           C
ANISOU 2148  CD1 PHE A 279     7712   5880   5142  -1002   -135    -27       C
ATOM   2149  CD2 PHE A 279       7.833   2.175  44.110  1.00 45.88           C
ANISOU 2149  CD2 PHE A 279     7307   5390   4733   -879    -43     32       C
ATOM   2150  CE1 PHE A 279       6.472   2.057  41.679  1.00 45.12           C
ANISOU 2150  CE1 PHE A 279     7204   5384   4557   -944   -155    -35       C
ATOM   2151  CE2 PHE A 279       8.367   2.802  42.957  1.00 44.58           C
ANISOU 2151  CE2 PHE A 279     7162   5251   4527   -824    -59     25       C
ATOM   2152  CZ  PHE A 279       7.684   2.740  41.755  1.00 45.55           C
ANISOU 2152  CZ  PHE A 279     7281   5421   4604   -855   -113     -4       C
ATOM   2153  N   PRO A 280       5.662   4.204  45.983  1.00 40.36           N
ANISOU 2153  N   PRO A 280     6356   4860   4121   -889    -43     87       N
ATOM   2154  CA  PRO A 280       6.267   5.390  46.617  1.00 37.19           C
ANISOU 2154  CA  PRO A 280     5912   4474   3745   -807    -15    105       C
ATOM   2155  C   PRO A 280       5.646   5.766  47.961  1.00 40.06           C
ANISOU 2155  C   PRO A 280     6192   4888   4141   -813     15    108       C
ATOM   2156  O   PRO A 280       6.174   6.677  48.621  1.00 39.20           O
ANISOU 2156  O   PRO A 280     6050   4790   4055   -748     40    107       O
ATOM   2157  CB  PRO A 280       6.052   6.490  45.579  1.00 36.08           C
ANISOU 2157  CB  PRO A 280     5727   4371   3612   -763    -57    112       C
ATOM   2158  CG  PRO A 280       5.946   5.778  44.319  1.00 39.84           C
ANISOU 2158  CG  PRO A 280     6262   4838   4037   -800    -97     99       C
ATOM   2159  CD  PRO A 280       5.170   4.536  44.636  1.00 37.44           C
ANISOU 2159  CD  PRO A 280     5972   4526   3729   -893   -102     75       C
ATOM   2160  N   GLY A 281       4.552   5.119  48.370  1.00 37.41           N
ANISOU 2160  N   GLY A 281     5818   4588   3809   -890     15    108       N
ATOM   2161  CA  GLY A 281       3.972   5.314  49.684  1.00 37.94           C
ANISOU 2161  CA  GLY A 281     5810   4716   3891   -903     55    113       C
ATOM   2162  C   GLY A 281       2.778   6.243  49.745  1.00 40.39           C
ANISOU 2162  C   GLY A 281     5995   5111   4239   -898     39     97       C
ATOM   2163  O   GLY A 281       2.429   6.700  50.835  1.00 42.45           O
ANISOU 2163  O   GLY A 281     6185   5433   4513   -882     78     88       O
ATOM   2164  N   SER A 282       2.144   6.516  48.621  1.00 38.29           N
ANISOU 2164  N   SER A 282     5700   4858   3989   -908    -17     92       N
ATOM   2165  CA  SER A 282       1.025   7.428  48.509  1.00 41.10           C
ANISOU 2165  CA  SER A 282     5936   5290   4392   -895    -43     82       C
ATOM   2166  C   SER A 282      -0.081   6.796  47.676  1.00 43.31           C
ANISOU 2166  C   SER A 282     6188   5600   4670   -976    -96     84       C
ATOM   2167  O   SER A 282       0.156   5.887  46.879  1.00 41.04           O
ANISOU 2167  O   SER A 282     5982   5266   4345  -1025   -126     84       O
ATOM   2168  CB  SER A 282       1.455   8.742  47.845  1.00 45.69           C
ANISOU 2168  CB  SER A 282     6495   5860   5007   -802    -74     84       C
ATOM   2169  OG  SER A 282       2.403   9.405  48.652  1.00 49.56           O
ANISOU 2169  OG  SER A 282     6995   6323   5513   -731    -30     72       O
ATOM   2170  N   TYR A 283      -1.294   7.308  47.858  1.00 39.76           N
ANISOU 2170  N   TYR A 283     5614   5229   4265   -987   -109     77       N
ATOM   2171  CA  TYR A 283      -2.417   6.890  47.029  1.00 45.89           C
ANISOU 2171  CA  TYR A 283     6342   6046   5049  -1057   -171     77       C
ATOM   2172  C   TYR A 283      -2.241   7.383  45.604  1.00 45.95           C
ANISOU 2172  C   TYR A 283     6373   6044   5042  -1019   -247     85       C
ATOM   2173  O   TYR A 283      -1.812   8.517  45.375  1.00 47.72           O
ANISOU 2173  O   TYR A 283     6579   6265   5289   -928   -255     99       O
ATOM   2174  CB  TYR A 283      -3.733   7.448  47.572  1.00 48.03           C
ANISOU 2174  CB  TYR A 283     6460   6411   5379  -1065   -166     70       C
ATOM   2175  CG  TYR A 283      -4.191   6.812  48.846  1.00 45.68           C
ANISOU 2175  CG  TYR A 283     6122   6151   5084  -1125    -95     70       C
ATOM   2176  CD1 TYR A 283      -4.872   5.592  48.840  1.00 47.23           C
ANISOU 2176  CD1 TYR A 283     6318   6354   5274  -1243   -100     81       C
ATOM   2177  CD2 TYR A 283      -3.947   7.431  50.067  1.00 42.92           C
ANISOU 2177  CD2 TYR A 283     5731   5833   4742  -1068    -24     58       C
ATOM   2178  CE1 TYR A 283      -5.284   4.996  50.036  1.00 43.97           C
ANISOU 2178  CE1 TYR A 283     5865   5979   4862  -1303    -29     98       C
ATOM   2179  CE2 TYR A 283      -4.357   6.856  51.256  1.00 47.31           C
ANISOU 2179  CE2 TYR A 283     6250   6442   5285  -1122     46     65       C
ATOM   2180  CZ  TYR A 283      -5.035   5.641  51.243  1.00 44.85           C
ANISOU 2180  CZ  TYR A 283     5937   6138   4967  -1240     46     94       C
ATOM   2181  OH  TYR A 283      -5.433   5.090  52.446  1.00 46.98           O
ANISOU 2181  OH  TYR A 283     6165   6465   5222  -1295    122    118       O
ATOM   2182  N   SER A 284      -2.589   6.524  44.647  1.00 45.30           N
ANISOU 2182  N   SER A 284     6329   5960   4922  -1091   -304     76       N
ATOM   2183  CA  SER A 284      -2.811   6.931  43.264  1.00 48.56           C
ANISOU 2183  CA  SER A 284     6735   6404   5310  -1072   -388     84       C
ATOM   2184  C   SER A 284      -4.107   7.738  43.147  1.00 50.06           C
ANISOU 2184  C   SER A 284     6777   6684   5559  -1062   -436     97       C
ATOM   2185  O   SER A 284      -4.848   7.911  44.112  1.00 53.54           O
ANISOU 2185  O   SER A 284     7120   7163   6059  -1075   -399     91       O
ATOM   2186  CB  SER A 284      -2.875   5.702  42.367  1.00 52.73           C
ANISOU 2186  CB  SER A 284     7342   6914   5778  -1158   -436     52       C
ATOM   2187  OG  SER A 284      -4.125   5.046  42.535  1.00 55.49           O
ANISOU 2187  OG  SER A 284     7614   7308   6160  -1255   -464     31       O
ATOM   2188  N   GLY A 285      -4.396   8.240  41.936  1.00 50.87           N
ANISOU 2188  N   GLY A 285     6857   6829   5642  -1037   -519    119       N
ATOM   2189  CA  GLY A 285      -5.679   8.865  41.694  1.00 55.32           C
ANISOU 2189  CA  GLY A 285     7279   7479   6262  -1034   -578    135       C
ATOM   2190  C   GLY A 285      -6.726   7.869  41.200  1.00 57.56           C
ANISOU 2190  C   GLY A 285     7528   7818   6526  -1145   -641    104       C
ATOM   2191  O   GLY A 285      -6.395   6.749  40.790  1.00 55.18           O
ANISOU 2191  O   GLY A 285     7324   7481   6160  -1219   -653     69       O
ATOM   2192  N   ALA A 286      -7.999   8.282  41.261  1.00 51.57           N
ANISOU 2192  N   ALA A 286     6621   7141   5831  -1157   -682    112       N
ATOM   2193  CA  ALA A 286      -9.058   7.530  40.597  1.00 46.93           C
ANISOU 2193  CA  ALA A 286     5981   6619   5232  -1256   -764     87       C
ATOM   2194  C   ALA A 286      -9.032   7.819  39.100  1.00 54.17           C
ANISOU 2194  C   ALA A 286     6922   7581   6079  -1230   -872    107       C
ATOM   2195  O   ALA A 286      -8.940   8.978  38.682  1.00 57.11           O
ANISOU 2195  O   ALA A 286     7253   7981   6464  -1132   -903    164       O
ATOM   2196  CB  ALA A 286     -10.429   7.866  41.185  1.00 46.15           C
ANISOU 2196  CB  ALA A 286     5705   6601   5229  -1276   -769     91       C
ATOM   2197  N   ARG A 287      -9.113   6.763  38.293  1.00 50.71           N
ANISOU 2197  N   ARG A 287     6548   7152   5566  -1319   -931     60       N
ATOM   2198  CA  ARG A 287      -9.158   6.900  36.847  1.00 54.34           C
ANISOU 2198  CA  ARG A 287     7031   7677   5938  -1307  -1039     68       C
ATOM   2199  C   ARG A 287     -10.206   5.952  36.288  1.00 59.23           C
ANISOU 2199  C   ARG A 287     7602   8360   6542  -1426  -1129      7       C
ATOM   2200  O   ARG A 287     -10.589   4.972  36.934  1.00 58.65           O
ANISOU 2200  O   ARG A 287     7521   8248   6514  -1526  -1096    -46       O
ATOM   2201  CB  ARG A 287      -7.801   6.603  36.205  1.00 56.64           C
ANISOU 2201  CB  ARG A 287     7490   7912   6120  -1277  -1020     55       C
ATOM   2202  CG  ARG A 287      -6.679   7.508  36.685  1.00 57.41           C
ANISOU 2202  CG  ARG A 287     7637   7942   6233  -1167   -936    114       C
ATOM   2203  CD  ARG A 287      -6.724   8.864  35.985  1.00 58.98           C
ANISOU 2203  CD  ARG A 287     7777   8203   6430  -1065   -989    202       C
ATOM   2204  NE  ARG A 287      -5.615   9.718  36.390  1.00 65.67           N
ANISOU 2204  NE  ARG A 287     8672   8977   7302   -966   -913    255       N
ATOM   2205  CZ  ARG A 287      -5.578  10.434  37.508  1.00 62.60           C
ANISOU 2205  CZ  ARG A 287     8223   8539   7023   -914   -845    275       C
ATOM   2206  NH1 ARG A 287      -6.598  10.462  38.350  1.00 61.29           N
ANISOU 2206  NH1 ARG A 287     7943   8397   6948   -942   -835    252       N
ATOM   2207  NH2 ARG A 287      -4.483  11.129  37.795  1.00 61.45           N
ANISOU 2207  NH2 ARG A 287     8130   8323   6895   -833   -783    312       N
ATOM   2208  N   LEU A 288     -10.668   6.253  35.072  1.00 60.00           N
ANISOU 2208  N   LEU A 288     7664   8557   6575  -1416  -1245     20       N
ATOM   2209  CA  LEU A 288     -11.527   5.337  34.327  1.00 61.74           C
ANISOU 2209  CA  LEU A 288     7854   8845   6759  -1527  -1348    -51       C
ATOM   2210  C   LEU A 288     -10.628   4.275  33.708  1.00 63.95           C
ANISOU 2210  C   LEU A 288     8301   9069   6930  -1577  -1348   -133       C
ATOM   2211  O   LEU A 288      -9.844   4.562  32.798  1.00 63.52           O
ANISOU 2211  O   LEU A 288     8336   9038   6760  -1514  -1373   -120       O
ATOM   2212  CB  LEU A 288     -12.332   6.078  33.264  1.00 59.14           C
ANISOU 2212  CB  LEU A 288     7422   8655   6392  -1492  -1478     -6       C
ATOM   2213  CG  LEU A 288     -13.447   6.966  33.809  1.00 61.00           C
ANISOU 2213  CG  LEU A 288     7472   8953   6754  -1458  -1495     58       C
ATOM   2214  CD1 LEU A 288     -14.073   7.798  32.697  1.00 60.34           C
ANISOU 2214  CD1 LEU A 288     7298   9000   6628  -1403  -1626    122       C
ATOM   2215  CD2 LEU A 288     -14.511   6.140  34.507  1.00 61.90           C
ANISOU 2215  CD2 LEU A 288     7484   9073   6963  -1578  -1491     -3       C
ATOM   2216  N   GLN A 289     -10.704   3.061  34.232  1.00 61.12           N
ANISOU 2216  N   GLN A 289     7981   8630   6611  -1684  -1313   -212       N
ATOM   2217  CA  GLN A 289      -9.839   1.971  33.817  1.00 62.26           C
ANISOU 2217  CA  GLN A 289     8282   8695   6681  -1731  -1300   -300       C
ATOM   2218  C   GLN A 289     -10.693   0.823  33.309  1.00 63.19           C
ANISOU 2218  C   GLN A 289     8375   8831   6802  -1868  -1390   -405       C
ATOM   2219  O   GLN A 289     -11.922   0.874  33.342  1.00 63.72           O
ANISOU 2219  O   GLN A 289     8304   8975   6934  -1929  -1456   -402       O
ATOM   2220  CB  GLN A 289      -8.938   1.506  34.973  1.00 59.69           C
ANISOU 2220  CB  GLN A 289     8044   8222   6413  -1728  -1166   -297       C
ATOM   2221  CG  GLN A 289      -8.111   2.619  35.572  1.00 60.47           C
ANISOU 2221  CG  GLN A 289     8159   8298   6520  -1601  -1079   -205       C
ATOM   2222  CD  GLN A 289      -6.607   2.376  35.468  1.00 61.93           C
ANISOU 2222  CD  GLN A 289     8504   8392   6635  -1546  -1011   -219       C
ATOM   2223  OE1 GLN A 289      -6.106   1.926  34.435  1.00 60.85           O
ANISOU 2223  OE1 GLN A 289     8460   8265   6397  -1549  -1054   -276       O
ATOM   2224  NE2 GLN A 289      -5.880   2.715  36.532  1.00 60.98           N
ANISOU 2224  NE2 GLN A 289     8410   8194   6567  -1489   -905   -170       N
ATOM   2225  N   CYS A 290     -10.010  -0.215  32.839  1.00 67.36           N
ANISOU 2225  N   CYS A 290     9036   9287   7270  -1915  -1391   -503       N
ATOM   2226  CA  CYS A 290     -10.632  -1.405  32.271  1.00 67.40           C
ANISOU 2226  CA  CYS A 290     9044   9287   7276  -2045  -1477   -626       C
ATOM   2227  C   CYS A 290     -11.288  -2.276  33.347  1.00 62.18           C
ANISOU 2227  C   CYS A 290     8326   8529   6771  -2165  -1434   -642       C
ATOM   2228  O   CYS A 290     -11.016  -2.154  34.542  1.00 61.61           O
ANISOU 2228  O   CYS A 290     8249   8377   6784  -2145  -1323   -570       O
ATOM   2229  CB  CYS A 290      -9.588  -2.226  31.513  1.00 68.69           C
ANISOU 2229  CB  CYS A 290     9375   9386   7338  -2045  -1476   -733       C
ATOM   2230  SG  CYS A 290      -9.154  -1.544  29.913  1.00 83.19           S
ANISOU 2230  SG  CYS A 290    11262  11378   8968  -1953  -1565   -749       S
ATOM   2231  N   GLU A 291     -12.176  -3.163  32.897  1.00 63.84           N
ANISOU 2231  N   GLU A 291     8488   8753   7015  -2294  -1527   -737       N
ATOM   2232  CA  GLU A 291     -12.856  -4.111  33.764  1.00 64.52           C
ANISOU 2232  CA  GLU A 291     8516   8747   7250  -2427  -1499   -756       C
ATOM   2233  C   GLU A 291     -12.760  -5.518  33.186  1.00 66.67           C
ANISOU 2233  C   GLU A 291     8876   8923   7531  -2542  -1554   -901       C
ATOM   2234  O   GLU A 291     -12.725  -5.712  31.968  1.00 68.29           O
ANISOU 2234  O   GLU A 291     9124   9190   7631  -2548  -1657  -1005       O
ATOM   2235  CB  GLU A 291     -14.331  -3.741  33.966  1.00 66.53           C
ANISOU 2235  CB  GLU A 291     8575   9116   7590  -2490  -1561   -716       C
ATOM   2236  CG  GLU A 291     -14.562  -2.693  35.041  1.00 65.07           C
ANISOU 2236  CG  GLU A 291     8287   8970   7467  -2413  -1471   -580       C
ATOM   2237  CD  GLU A 291     -15.996  -2.695  35.569  1.00 69.50           C
ANISOU 2237  CD  GLU A 291     8655   9600   8151  -2504  -1496   -550       C
ATOM   2238  OE1 GLU A 291     -16.808  -3.534  35.102  1.00 64.83           O
ANISOU 2238  OE1 GLU A 291     8008   9020   7604  -2635  -1587   -630       O
ATOM   2239  OE2 GLU A 291     -16.303  -1.854  36.452  1.00 66.86           O
ANISOU 2239  OE2 GLU A 291     8220   9310   7873  -2444  -1424   -452       O
ATOM   2240  N   VAL A 292     -12.742  -6.502  34.079  1.00 63.28           N
ANISOU 2240  N   VAL A 292     8468   8342   7231  -2635  -1485   -908       N
ATOM   2241  CA  VAL A 292     -12.583  -7.900  33.712  1.00 64.42           C
ANISOU 2241  CA  VAL A 292     8701   8356   7421  -2745  -1520  -1040       C
ATOM   2242  C   VAL A 292     -13.765  -8.678  34.260  1.00 67.39           C
ANISOU 2242  C   VAL A 292     8955   8689   7961  -2909  -1546  -1046       C
ATOM   2243  O   VAL A 292     -14.056  -8.616  35.461  1.00 68.67           O
ANISOU 2243  O   VAL A 292     9048   8812   8232  -2935  -1454   -932       O
ATOM   2244  CB  VAL A 292     -11.268  -8.491  34.254  1.00 64.85           C
ANISOU 2244  CB  VAL A 292     8916   8234   7491  -2703  -1408  -1038       C
ATOM   2245  CG1 VAL A 292     -11.230  -9.999  34.029  1.00 65.77           C
ANISOU 2245  CG1 VAL A 292     9105   8190   7696  -2827  -1440  -1167       C
ATOM   2246  CG2 VAL A 292     -10.078  -7.829  33.609  1.00 64.60           C
ANISOU 2246  CG2 VAL A 292     9002   8242   7300  -2552  -1386  -1047       C
ATOM   2247  N   LYS A 293     -14.425  -9.429  33.389  1.00 67.64           N
ANISOU 2247  N   LYS A 293     8961   8729   8010  -3022  -1669  -1179       N
ATOM   2248  CA  LYS A 293     -15.457 -10.367  33.794  1.00 66.84           C
ANISOU 2248  CA  LYS A 293     8759   8560   8078  -3196  -1701  -1206       C
ATOM   2249  C   LYS A 293     -14.834 -11.685  34.247  1.00 67.44           C
ANISOU 2249  C   LYS A 293     8953   8405   8267  -3275  -1641  -1255       C
ATOM   2250  O   LYS A 293     -13.958 -12.236  33.573  1.00 67.00           O
ANISOU 2250  O   LYS A 293     9044   8261   8150  -3246  -1660  -1372       O
ATOM   2251  CB  LYS A 293     -16.407 -10.611  32.617  1.00 74.51           C
ANISOU 2251  CB  LYS A 293     9650   9637   9023  -3286  -1870  -1341       C
ATOM   2252  CG  LYS A 293     -17.383 -11.752  32.806  1.00 71.67           C
ANISOU 2252  CG  LYS A 293     9202   9188   8841  -3481  -1925  -1407       C
ATOM   2253  CD  LYS A 293     -18.781 -11.313  33.200  1.00 73.52           C
ANISOU 2253  CD  LYS A 293     9219   9549   9164  -3557  -1961  -1326       C
ATOM   2254  CE  LYS A 293     -19.814 -12.192  32.506  1.00 77.39           C
ANISOU 2254  CE  LYS A 293     9619  10043   9742  -3729  -2106  -1465       C
ATOM   2255  NZ  LYS A 293     -20.030 -13.506  33.138  1.00 87.17           N
ANISOU 2255  NZ  LYS A 293    10860  11080  11180  -3893  -2070  -1491       N
ATOM   2256  N   ILE A 294     -15.315 -12.213  35.366  1.00 67.01           N
ANISOU 2256  N   ILE A 294     8829   8255   8379  -3375  -1569  -1166       N
ATOM   2257  CA  ILE A 294     -14.916 -13.541  35.833  1.00 72.11           C
ANISOU 2257  CA  ILE A 294     9562   8672   9162  -3472  -1523  -1196       C
ATOM   2258  C   ILE A 294     -15.803 -14.557  35.116  1.00 73.31           C
ANISOU 2258  C   ILE A 294     9660   8775   9418  -3642  -1651  -1343       C
ATOM   2259  O   ILE A 294     -17.016 -14.583  35.341  1.00 78.12           O
ANISOU 2259  O   ILE A 294    10106   9451  10125  -3757  -1694  -1311       O
ATOM   2260  CB  ILE A 294     -15.062 -13.682  37.355  1.00 70.48           C
ANISOU 2260  CB  ILE A 294     9301   8392   9086  -3512  -1391  -1022       C
ATOM   2261  CG1 ILE A 294     -14.405 -12.517  38.095  1.00 69.48           C
ANISOU 2261  CG1 ILE A 294     9192   8353   8855  -3350  -1278   -881       C
ATOM   2262  CG2 ILE A 294     -14.403 -14.966  37.821  1.00 69.36           C
ANISOU 2262  CG2 ILE A 294     9277   8008   9071  -3580  -1335  -1033       C
ATOM   2263  CD1 ILE A 294     -13.109 -12.008  37.484  1.00 63.04           C
ANISOU 2263  CD1 ILE A 294     8530   7541   7880  -3188  -1267   -929       C
ATOM   2264  N   ASP A 295     -15.206 -15.399  34.261  1.00 74.55           N
ANISOU 2264  N   ASP A 295     9948   8816   9561  -3660  -1712  -1512       N
ATOM   2265  CA  ASP A 295     -15.934 -16.451  33.545  1.00 74.49           C
ANISOU 2265  CA  ASP A 295     9906   8739   9658  -3822  -1837  -1679       C
ATOM   2266  C   ASP A 295     -15.859 -17.817  34.219  1.00 74.21           C
ANISOU 2266  C   ASP A 295     9911   8444   9842  -3955  -1791  -1683       C
ATOM   2267  O   ASP A 295     -16.796 -18.613  34.093  1.00 77.34           O
ANISOU 2267  O   ASP A 295    10210   8781  10394  -4103  -1862  -1747       O
ATOM   2268  CB  ASP A 295     -15.413 -16.600  32.108  1.00 77.27           C
ANISOU 2268  CB  ASP A 295    10369   9127   9863  -3770  -1946  -1889       C
ATOM   2269  CG  ASP A 295     -15.525 -15.326  31.312  1.00 79.12           C
ANISOU 2269  CG  ASP A 295    10563   9617   9880  -3651  -2007  -1887       C
ATOM   2270  OD1 ASP A 295     -16.658 -14.814  31.195  1.00 80.23           O
ANISOU 2270  OD1 ASP A 295    10543   9915  10025  -3704  -2082  -1852       O
ATOM   2271  OD2 ASP A 295     -14.489 -14.849  30.790  1.00 80.15           O
ANISOU 2271  OD2 ASP A 295    10820   9793   9842  -3504  -1982  -1915       O
ATOM   2272  N   ARG A 296     -14.766 -18.111  34.917  1.00 76.54           N
ANISOU 2272  N   ARG A 296    10335   8582  10163  -3883  -1671  -1609       N
ATOM   2273  CA  ARG A 296     -14.616 -19.376  35.617  1.00 75.08           C
ANISOU 2273  CA  ARG A 296    10193   8142  10191  -3995  -1620  -1587       C
ATOM   2274  C   ARG A 296     -13.568 -19.219  36.707  1.00 74.86           C
ANISOU 2274  C   ARG A 296    10259   8025  10159  -3886  -1464  -1419       C
ATOM   2275  O   ARG A 296     -12.543 -18.558  36.507  1.00 71.77           O
ANISOU 2275  O   ARG A 296     9972   7688   9607  -3720  -1420  -1417       O
ATOM   2276  CB  ARG A 296     -14.217 -20.501  34.659  1.00 77.39           C
ANISOU 2276  CB  ARG A 296    10581   8277  10547  -3996  -1690  -1800       C
ATOM   2277  CG  ARG A 296     -13.957 -21.833  35.334  1.00 82.24           C
ANISOU 2277  CG  ARG A 296    11233   8617  11398  -4054  -1625  -1771       C
ATOM   2278  CD  ARG A 296     -13.802 -22.946  34.316  1.00 78.94           C
ANISOU 2278  CD  ARG A 296    10865   8060  11070  -4056  -1707  -2001       C
ATOM   2279  NE  ARG A 296     -15.087 -23.538  33.975  1.00 85.03           N
ANISOU 2279  NE  ARG A 296    11484   8832  11992  -4190  -1802  -2081       N
ATOM   2280  CZ  ARG A 296     -15.256 -24.816  33.676  1.00 82.20           C
ANISOU 2280  CZ  ARG A 296    11117   8279  11836  -4255  -1841  -2212       C
ATOM   2281  NH1 ARG A 296     -14.240 -25.660  33.664  1.00 83.00           N
ANISOU 2281  NH1 ARG A 296    11348   8168  12019  -4197  -1796  -2277       N
ATOM   2282  NH2 ARG A 296     -16.477 -25.262  33.394  1.00 89.67           N
ANISOU 2282  NH2 ARG A 296    11912   9240  12917  -4382  -1928  -2279       N
ATOM   2283  N   ILE A 297     -13.840 -19.831  37.854  1.00 77.93           N
ANISOU 2283  N   ILE A 297    10603   8283  10725  -3983  -1384  -1273       N
ATOM   2284  CA  ILE A 297     -12.898 -19.908  38.961  1.00 75.12           C
ANISOU 2284  CA  ILE A 297    10332   7817  10392  -3905  -1245  -1112       C
ATOM   2285  C   ILE A 297     -12.511 -21.367  39.159  1.00 78.87           C
ANISOU 2285  C   ILE A 297    10897   8006  11066  -3999  -1237  -1146       C
ATOM   2286  O   ILE A 297     -13.387 -22.230  39.295  1.00 77.28           O
ANISOU 2286  O   ILE A 297    10595   7714  11052  -4127  -1264  -1147       O
ATOM   2287  CB  ILE A 297     -13.507 -19.338  40.249  1.00 75.10           C
ANISOU 2287  CB  ILE A 297    10199   7918  10416  -3927  -1145   -886       C
ATOM   2288  CG1 ILE A 297     -13.731 -17.835  40.116  1.00 74.88           C
ANISOU 2288  CG1 ILE A 297    10097   8157  10198  -3807  -1141   -850       C
ATOM   2289  CG2 ILE A 297     -12.619 -19.655  41.433  1.00 73.43           C
ANISOU 2289  CG2 ILE A 297    10071   7575  10253  -3877  -1012   -722       C
ATOM   2290  CD1 ILE A 297     -14.551 -17.260  41.243  1.00 72.20           C
ANISOU 2290  CD1 ILE A 297     9603   7942   9889  -3842  -1061   -666       C
ATOM   2291  N   THR A 298     -11.209 -21.643  39.173  1.00 73.29           N
ANISOU 2291  N   THR A 298    10350   7168  10328  -3884  -1185  -1165       N
ATOM   2292  CA  THR A 298     -10.676 -22.943  39.563  1.00 73.38           C
ANISOU 2292  CA  THR A 298    10435   6914  10534  -3906  -1144  -1152       C
ATOM   2293  C   THR A 298      -9.770 -22.715  40.766  1.00 74.48           C
ANISOU 2293  C   THR A 298    10651   6998  10651  -3836  -1015   -949       C
ATOM   2294  O   THR A 298      -9.016 -21.732  40.794  1.00 72.66           O
ANISOU 2294  O   THR A 298    10471   6903  10236  -3674   -966   -917       O
ATOM   2295  CB  THR A 298      -9.927 -23.627  38.401  1.00 76.74           C
ANISOU 2295  CB  THR A 298    10977   7219  10963  -3830  -1208  -1384       C
ATOM   2296  OG1 THR A 298      -8.587 -23.135  38.301  1.00 77.10           O
ANISOU 2296  OG1 THR A 298    11173   7266  10854  -3678  -1158  -1393       O
ATOM   2297  CG2 THR A 298     -10.632 -23.361  37.077  1.00 78.22           C
ANISOU 2297  CG2 THR A 298    11107   7551  11061  -3855  -1339  -1592       C
ATOM   2298  N   HIS A 299      -9.882 -23.577  41.783  1.00 76.99           N
ANISOU 2298  N   HIS A 299    10935   7160  11156  -3895   -943   -796       N
ATOM   2299  CA  HIS A 299      -9.143 -23.353  43.020  1.00 73.98           C
ANISOU 2299  CA  HIS A 299    10606   6751  10751  -3835   -823   -582       C
ATOM   2300  C   HIS A 299      -8.922 -24.654  43.781  1.00 74.44           C
ANISOU 2300  C   HIS A 299    10674   6576  11033  -3865   -765   -474       C
ATOM   2301  O   HIS A 299      -9.705 -25.600  43.670  1.00 75.52           O
ANISOU 2301  O   HIS A 299    10727   6604  11363  -3975   -797   -505       O
ATOM   2302  CB  HIS A 299      -9.864 -22.356  43.938  1.00 72.69           C
ANISOU 2302  CB  HIS A 299    10312   6809  10499  -3851   -757   -400       C
ATOM   2303  CG  HIS A 299     -11.132 -22.886  44.534  1.00 74.24           C
ANISOU 2303  CG  HIS A 299    10360   6990  10859  -4032   -753   -295       C
ATOM   2304  ND1 HIS A 299     -11.155 -23.630  45.694  1.00 75.87           N
ANISOU 2304  ND1 HIS A 299    10535   7083  11209  -4071   -659   -102       N
ATOM   2305  CD2 HIS A 299     -12.422 -22.748  44.153  1.00 73.22           C
ANISOU 2305  CD2 HIS A 299    10081   6973  10766  -4144   -816   -348       C
ATOM   2306  CE1 HIS A 299     -12.401 -23.946  45.988  1.00 74.02           C
ANISOU 2306  CE1 HIS A 299    10142   6885  11096  -4204   -661    -44       C
ATOM   2307  NE2 HIS A 299     -13.190 -23.417  45.073  1.00 74.80           N
ANISOU 2307  NE2 HIS A 299    10165   7120  11136  -4251   -756   -192       N
ATOM   2308  N   ARG A 300      -7.850 -24.673  44.577  1.00 68.70           N
ANISOU 2308  N   ARG A 300    10044   5777  10283  -3767   -677   -340       N
ATOM   2309  CA  ARG A 300      -7.611 -25.754  45.517  1.00 72.77           C
ANISOU 2309  CA  ARG A 300    10559   6101  10990  -3785   -605   -185       C
ATOM   2310  C   ARG A 300      -8.657 -25.730  46.618  1.00 72.93           C
ANISOU 2310  C   ARG A 300    10434   6205  11073  -3900   -542     26       C
ATOM   2311  O   ARG A 300      -9.269 -24.699  46.900  1.00 71.04           O
ANISOU 2311  O   ARG A 300    10114   6183  10696  -3931   -528     88       O
ATOM   2312  CB  ARG A 300      -6.221 -25.637  46.141  1.00 69.88           C
ANISOU 2312  CB  ARG A 300    10320   5675  10556  -3641   -530    -80       C
ATOM   2313  CG  ARG A 300      -5.098 -25.483  45.141  1.00 69.89           C
ANISOU 2313  CG  ARG A 300    10463   5627  10463  -3509   -573   -270       C
ATOM   2314  CD  ARG A 300      -3.756 -25.309  45.833  1.00 72.00           C
ANISOU 2314  CD  ARG A 300    10841   5850  10665  -3368   -495   -152       C
ATOM   2315  NE  ARG A 300      -3.386 -26.480  46.616  1.00 75.34           N
ANISOU 2315  NE  ARG A 300    11271   6068  11288  -3365   -444    -20       N
ATOM   2316  CZ  ARG A 300      -2.142 -26.914  46.764  1.00 74.21           C
ANISOU 2316  CZ  ARG A 300    11232   5786  11178  -3240   -412     -5       C
ATOM   2317  NH1 ARG A 300      -1.126 -26.308  46.172  1.00 66.42           N
ANISOU 2317  NH1 ARG A 300    10354   4839  10043  -3109   -423   -119       N
ATOM   2318  NH2 ARG A 300      -1.915 -27.995  47.507  1.00 73.82           N
ANISOU 2318  NH2 ARG A 300    11173   5554  11322  -3247   -365    128       N
ATOM   2319  N   THR A 301      -8.871 -26.892  47.232  1.00 76.35           N
ANISOU 2319  N   THR A 301    10827   6463  11720  -3964   -499    132       N
ATOM   2320  CA  THR A 301      -9.731 -26.972  48.407  1.00 74.70           C
ANISOU 2320  CA  THR A 301    10488   6323  11571  -4060   -416    356       C
ATOM   2321  C   THR A 301      -9.072 -26.269  49.593  1.00 78.15           C
ANISOU 2321  C   THR A 301    10958   6876  11858  -3970   -313    572       C
ATOM   2322  O   THR A 301      -7.863 -26.381  49.808  1.00 75.74           O
ANISOU 2322  O   THR A 301    10778   6483  11518  -3849   -284    603       O
ATOM   2323  CB  THR A 301     -10.024 -28.432  48.741  1.00 78.78           C
ANISOU 2323  CB  THR A 301    10970   6613  12351  -4144   -386    414       C
ATOM   2324  OG1 THR A 301     -10.636 -29.062  47.607  1.00 80.99           O
ANISOU 2324  OG1 THR A 301    11218   6790  12767  -4229   -483    194       O
ATOM   2325  CG2 THR A 301     -10.938 -28.552  49.961  1.00 79.90           C
ANISOU 2325  CG2 THR A 301    10977   6834  12548  -4244   -290    650       C
ATOM   2326  N   ASN A 302      -9.885 -25.557  50.370  1.00 75.31           N
ANISOU 2326  N   ASN A 302    10479   6722  11414  -4026   -257    714       N
ATOM   2327  CA  ASN A 302      -9.403 -24.622  51.381  1.00 74.88           C
ANISOU 2327  CA  ASN A 302    10438   6838  11175  -3943   -168    882       C
ATOM   2328  C   ASN A 302      -8.369 -23.652  50.800  1.00 72.31           C
ANISOU 2328  C   ASN A 302    10241   6577  10655  -3812   -202    765       C
ATOM   2329  O   ASN A 302      -7.225 -23.605  51.274  1.00 66.25           O
ANISOU 2329  O   ASN A 302     9581   5764   9826  -3695   -155    838       O
ATOM   2330  CB  ASN A 302      -8.825 -25.365  52.577  1.00 72.86           C
ANISOU 2330  CB  ASN A 302    10212   6479  10993  -3903    -70   1097       C
ATOM   2331  CG  ASN A 302      -9.859 -26.146  53.337  1.00 83.94           C
ANISOU 2331  CG  ASN A 302    11483   7860  12551  -4028    -10   1247       C
ATOM   2332  OD1 ASN A 302     -11.059 -25.939  53.168  1.00 90.14           O
ANISOU 2332  OD1 ASN A 302    12135   8751  13362  -4141    -25   1220       O
ATOM   2333  ND2 ASN A 302      -9.401 -27.054  54.195  1.00 84.10           N
ANISOU 2333  ND2 ASN A 302    11535   7745  12673  -4007     63   1410       N
ATOM   2334  N   PRO A 303      -8.735 -22.863  49.781  1.00 70.83           N
ANISOU 2334  N   PRO A 303    10041   6502  10369  -3823   -280    586       N
ATOM   2335  CA  PRO A 303      -7.763 -21.950  49.160  1.00 66.35           C
ANISOU 2335  CA  PRO A 303     9567   6025   9617  -3636   -297    458       C
ATOM   2336  C   PRO A 303      -7.261 -20.916  50.153  1.00 64.38           C
ANISOU 2336  C   PRO A 303     9307   5962   9193  -3505   -200    598       C
ATOM   2337  O   PRO A 303      -7.978 -20.498  51.062  1.00 64.93           O
ANISOU 2337  O   PRO A 303     9260   6182   9227  -3551   -135    740       O
ATOM   2338  CB  PRO A 303      -8.565 -21.284  48.038  1.00 67.00           C
ANISOU 2338  CB  PRO A 303     9576   6247   9632  -3657   -385    273       C
ATOM   2339  CG  PRO A 303      -9.998 -21.411  48.480  1.00 68.64           C
ANISOU 2339  CG  PRO A 303     9618   6533   9930  -3823   -378    359       C
ATOM   2340  CD  PRO A 303     -10.085 -22.707  49.208  1.00 68.82           C
ANISOU 2340  CD  PRO A 303     9649   6344  10155  -3951   -343    498       C
ATOM   2341  N   ILE A 304      -6.006 -20.513  49.980  1.00 65.41           N
ANISOU 2341  N   ILE A 304     9556   6082   9214  -3341   -190    553       N
ATOM   2342  CA  ILE A 304      -5.375 -19.504  50.830  1.00 58.34           C
ANISOU 2342  CA  ILE A 304     8664   5353   8150  -3203   -109    659       C
ATOM   2343  C   ILE A 304      -5.231 -18.229  50.022  1.00 58.84           C
ANISOU 2343  C   ILE A 304     8722   5591   8046  -3085   -144    513       C
ATOM   2344  O   ILE A 304      -4.586 -18.221  48.969  1.00 60.99           O
ANISOU 2344  O   ILE A 304     9085   5796   8293  -3015   -205    356       O
ATOM   2345  CB  ILE A 304      -4.011 -19.968  51.355  1.00 59.36           C
ANISOU 2345  CB  ILE A 304     8922   5345   8287  -3104    -67    740       C
ATOM   2346  CG1 ILE A 304      -4.185 -21.176  52.285  1.00 64.31           C
ANISOU 2346  CG1 ILE A 304     9544   5811   9078  -3218    -27    921       C
ATOM   2347  CG2 ILE A 304      -3.315 -18.818  52.056  1.00 57.16           C
ANISOU 2347  CG2 ILE A 304     8647   5250   7821  -2953     -1    809       C
ATOM   2348  CD1 ILE A 304      -2.982 -22.085  52.358  1.00 63.61           C
ANISOU 2348  CD1 ILE A 304     9593   5496   9080  -3158    -28    951       C
ATOM   2349  N   PHE A 305      -5.816 -17.152  50.524  1.00 58.43           N
ANISOU 2349  N   PHE A 305     8560   5760   7880  -3061   -103    567       N
ATOM   2350  CA  PHE A 305      -5.794 -15.858  49.852  1.00 58.35           C
ANISOU 2350  CA  PHE A 305     8526   5922   7721  -2954   -133    452       C
ATOM   2351  C   PHE A 305      -4.494 -15.133  50.209  1.00 55.76           C
ANISOU 2351  C   PHE A 305     8286   5638   7264  -2782    -85    477       C
ATOM   2352  O   PHE A 305      -4.398 -14.481  51.252  1.00 57.38           O
ANISOU 2352  O   PHE A 305     8446   5967   7389  -2729    -10    591       O
ATOM   2353  CB  PHE A 305      -7.024 -15.053  50.250  1.00 54.30           C
ANISOU 2353  CB  PHE A 305     7850   5615   7168  -3004   -112    496       C
ATOM   2354  CG  PHE A 305      -7.099 -13.699  49.602  1.00 55.12           C
ANISOU 2354  CG  PHE A 305     7915   5892   7135  -2898   -144    392       C
ATOM   2355  CD1 PHE A 305      -6.503 -13.466  48.377  1.00 50.12           C
ANISOU 2355  CD1 PHE A 305     7369   5222   6453  -2821   -219    242       C
ATOM   2356  CD2 PHE A 305      -7.781 -12.662  50.218  1.00 54.47           C
ANISOU 2356  CD2 PHE A 305     7707   6011   6980  -2874    -98    449       C
ATOM   2357  CE1 PHE A 305      -6.574 -12.219  47.785  1.00 52.17           C
ANISOU 2357  CE1 PHE A 305     7591   5638   6594  -2725   -249    167       C
ATOM   2358  CE2 PHE A 305      -7.861 -11.420  49.628  1.00 55.52           C
ANISOU 2358  CE2 PHE A 305     7801   6288   7006  -2775   -131    362       C
ATOM   2359  CZ  PHE A 305      -7.258 -11.202  48.406  1.00 52.10           C
ANISOU 2359  CZ  PHE A 305     7457   5812   6528  -2703   -208    229       C
ATOM   2360  N   GLU A 306      -3.486 -15.255  49.343  1.00 51.96           N
ANISOU 2360  N   GLU A 306     7925   5055   6762  -2695   -127    363       N
ATOM   2361  CA  GLU A 306      -2.205 -14.580  49.534  1.00 50.71           C
ANISOU 2361  CA  GLU A 306     7848   4929   6490  -2533    -91    371       C
ATOM   2362  C   GLU A 306      -2.324 -13.156  49.013  1.00 51.60           C
ANISOU 2362  C   GLU A 306     7911   5229   6464  -2442   -108    292       C
ATOM   2363  O   GLU A 306      -2.440 -12.933  47.806  1.00 50.38           O
ANISOU 2363  O   GLU A 306     7772   5085   6285  -2430   -178    154       O
ATOM   2364  CB  GLU A 306      -1.090 -15.332  48.816  1.00 53.29           C
ANISOU 2364  CB  GLU A 306     8315   5071   6861  -2479   -123    285       C
ATOM   2365  CG  GLU A 306       0.290 -14.695  48.886  1.00 50.44           C
ANISOU 2365  CG  GLU A 306     8037   4733   6394  -2314    -90    281       C
ATOM   2366  CD  GLU A 306       1.227 -15.267  47.814  1.00 55.51           C
ANISOU 2366  CD  GLU A 306     8800   5228   7065  -2258   -134    147       C
ATOM   2367  OE1 GLU A 306       0.729 -15.905  46.870  1.00 57.63           O
ANISOU 2367  OE1 GLU A 306     9081   5414   7403  -2336   -198     29       O
ATOM   2368  OE2 GLU A 306       2.462 -15.093  47.897  1.00 52.79           O
ANISOU 2368  OE2 GLU A 306     8534   4851   6673  -2136   -105    152       O
ATOM   2369  N   ASN A 307      -2.294 -12.193  49.923  1.00 52.76           N
ANISOU 2369  N   ASN A 307     7999   5525   6521  -2377    -46    381       N
ATOM   2370  CA  ASN A 307      -2.537 -10.797  49.608  1.00 49.20           C
ANISOU 2370  CA  ASN A 307     7482   5252   5960  -2298    -56    327       C
ATOM   2371  C   ASN A 307      -1.465  -9.940  50.269  1.00 47.56           C
ANISOU 2371  C   ASN A 307     7312   5107   5652  -2156      1    374       C
ATOM   2372  O   ASN A 307      -0.734 -10.393  51.147  1.00 48.12           O
ANISOU 2372  O   ASN A 307     7437   5117   5732  -2133     53    466       O
ATOM   2373  CB  ASN A 307      -3.948 -10.383  50.052  1.00 50.87           C
ANISOU 2373  CB  ASN A 307     7541   5605   6183  -2381    -44    370       C
ATOM   2374  CG  ASN A 307      -4.579  -9.369  49.125  1.00 47.95           C
ANISOU 2374  CG  ASN A 307     7099   5362   5760  -2352   -103    269       C
ATOM   2375  OD1 ASN A 307      -4.443  -9.441  47.902  1.00 44.53           O
ANISOU 2375  OD1 ASN A 307     6714   4885   5320  -2342   -179    155       O
ATOM   2376  ND2 ASN A 307      -5.269  -8.401  49.715  1.00 51.29           N
ANISOU 2376  ND2 ASN A 307     7401   5947   6138  -2332    -68    311       N
ATOM   2377  N   LEU A 308      -1.352  -8.695  49.823  1.00 47.44           N
ANISOU 2377  N   LEU A 308     7268   5212   5546  -2062    -14    312       N
ATOM   2378  CA  LEU A 308      -0.204  -7.871  50.161  1.00 44.89           C
ANISOU 2378  CA  LEU A 308     6993   4926   5137  -1924     23    325       C
ATOM   2379  C   LEU A 308      -0.694  -6.564  50.755  1.00 44.97           C
ANISOU 2379  C   LEU A 308     6894   5112   5081  -1875     55    349       C
ATOM   2380  O   LEU A 308      -1.664  -5.984  50.267  1.00 51.07           O
ANISOU 2380  O   LEU A 308     7578   5977   5852  -1902     21    304       O
ATOM   2381  CB  LEU A 308       0.677  -7.623  48.911  1.00 46.40           C
ANISOU 2381  CB  LEU A 308     7273   5065   5292  -1841    -27    217       C
ATOM   2382  CG  LEU A 308       1.825  -6.608  48.963  1.00 44.74           C
ANISOU 2382  CG  LEU A 308     7102   4901   4998  -1698     -3    210       C
ATOM   2383  CD1 LEU A 308       3.036  -7.102  48.166  1.00 45.13           C
ANISOU 2383  CD1 LEU A 308     7275   4829   5045  -1638    -21    151       C
ATOM   2384  CD2 LEU A 308       1.349  -5.277  48.417  1.00 45.68           C
ANISOU 2384  CD2 LEU A 308     7144   5157   5058  -1649    -30    161       C
ATOM   2385  N   TYR A 309      -0.047  -6.127  51.823  1.00 42.56           N
ANISOU 2385  N   TYR A 309     6592   4853   4724  -1804    117    417       N
ATOM   2386  CA  TYR A 309      -0.221  -4.786  52.348  1.00 38.42           C
ANISOU 2386  CA  TYR A 309     5983   4482   4133  -1729    147    416       C
ATOM   2387  C   TYR A 309       0.902  -3.896  51.825  1.00 40.82           C
ANISOU 2387  C   TYR A 309     6347   4780   4383  -1600    130    357       C
ATOM   2388  O   TYR A 309       2.072  -4.295  51.817  1.00 41.71           O
ANISOU 2388  O   TYR A 309     6561   4800   4486  -1550    137    366       O
ATOM   2389  CB  TYR A 309      -0.215  -4.777  53.884  1.00 36.15           C
ANISOU 2389  CB  TYR A 309     5655   4267   3814  -1729    225    516       C
ATOM   2390  CG  TYR A 309      -0.217  -3.365  54.405  1.00 40.09           C
ANISOU 2390  CG  TYR A 309     6078   4911   4243  -1636    254    492       C
ATOM   2391  CD1 TYR A 309      -1.408  -2.660  54.544  1.00 41.70           C
ANISOU 2391  CD1 TYR A 309     6152   5244   4449  -1660    263    471       C
ATOM   2392  CD2 TYR A 309       0.984  -2.701  54.690  1.00 36.47           C
ANISOU 2392  CD2 TYR A 309     5674   4455   3728  -1520    268    478       C
ATOM   2393  CE1 TYR A 309      -1.409  -1.348  54.996  1.00 42.74           C
ANISOU 2393  CE1 TYR A 309     6213   5495   4531  -1569    288    436       C
ATOM   2394  CE2 TYR A 309       0.996  -1.393  55.129  1.00 41.32           C
ANISOU 2394  CE2 TYR A 309     6219   5188   4294  -1436    288    442       C
ATOM   2395  CZ  TYR A 309      -0.200  -0.718  55.279  1.00 44.21           C
ANISOU 2395  CZ  TYR A 309     6460   5672   4666  -1459    299    418       C
ATOM   2396  OH  TYR A 309      -0.190   0.587  55.715  1.00 50.12           O
ANISOU 2396  OH  TYR A 309     7138   6526   5380  -1370    319    373       O
ATOM   2397  N   LEU A 310       0.555  -2.685  51.400  1.00 39.41           N
ANISOU 2397  N   LEU A 310     6100   4698   4175  -1544    109    303       N
ATOM   2398  CA  LEU A 310       1.570  -1.688  51.103  1.00 40.17           C
ANISOU 2398  CA  LEU A 310     6234   4805   4226  -1423    104    266       C
ATOM   2399  C   LEU A 310       1.225  -0.383  51.809  1.00 41.25           C
ANISOU 2399  C   LEU A 310     6268   5071   4335  -1362    134    265       C
ATOM   2400  O   LEU A 310       0.053  -0.044  52.032  1.00 45.60           O
ANISOU 2400  O   LEU A 310     6710   5713   4902  -1404    137    264       O
ATOM   2401  CB  LEU A 310       1.761  -1.464  49.585  1.00 42.06           C
ANISOU 2401  CB  LEU A 310     6514   5004   4462  -1397     38    192       C
ATOM   2402  CG  LEU A 310       0.836  -0.554  48.783  1.00 44.97           C
ANISOU 2402  CG  LEU A 310     6795   5461   4831  -1393    -11    147       C
ATOM   2403  CD1 LEU A 310       1.323  -0.453  47.293  1.00 45.34           C
ANISOU 2403  CD1 LEU A 310     6909   5465   4853  -1358    -73     87       C
ATOM   2404  CD2 LEU A 310      -0.598  -1.036  48.839  1.00 39.49           C
ANISOU 2404  CD2 LEU A 310     6015   4811   4180  -1503    -30    153       C
ATOM   2405  N   GLY A 311       2.252   0.330  52.172  1.00 37.77           N
ANISOU 2405  N   GLY A 311     5857   4635   3859  -1264    155    260       N
ATOM   2406  CA  GLY A 311       2.101   1.501  53.009  1.00 39.16           C
ANISOU 2406  CA  GLY A 311     5946   4919   4014  -1201    189    252       C
ATOM   2407  C   GLY A 311       3.343   2.335  52.849  1.00 38.00           C
ANISOU 2407  C   GLY A 311     5847   4745   3848  -1092    184    223       C
ATOM   2408  O   GLY A 311       4.000   2.313  51.810  1.00 34.46           O
ANISOU 2408  O   GLY A 311     5466   4221   3406  -1063    147    200       O
ATOM   2409  N   ILE A 312       3.673   3.083  53.884  1.00 37.44           N
ANISOU 2409  N   ILE A 312     5734   4739   3752  -1033    223    219       N
ATOM   2410  CA  ILE A 312       4.910   3.832  53.879  1.00 33.25           C
ANISOU 2410  CA  ILE A 312     5243   4178   3211   -936    220    194       C
ATOM   2411  C   ILE A 312       6.067   2.842  53.857  1.00 37.15           C
ANISOU 2411  C   ILE A 312     5853   4576   3687   -935    224    232       C
ATOM   2412  O   ILE A 312       6.114   1.905  54.672  1.00 39.26           O
ANISOU 2412  O   ILE A 312     6148   4839   3932   -979    253    287       O
ATOM   2413  CB  ILE A 312       4.958   4.803  55.061  1.00 37.47           C
ANISOU 2413  CB  ILE A 312     5704   4808   3726   -879    257    169       C
ATOM   2414  CG1 ILE A 312       3.915   5.898  54.792  1.00 40.07           C
ANISOU 2414  CG1 ILE A 312     5922   5207   4096   -861    244    118       C
ATOM   2415  CG2 ILE A 312       6.337   5.418  55.180  1.00 39.24           C
ANISOU 2415  CG2 ILE A 312     5973   4993   3945   -790    253    147       C
ATOM   2416  CD1 ILE A 312       3.803   6.929  55.860  1.00 43.60           C
ANISOU 2416  CD1 ILE A 312     6283   5746   4535   -803    278     71       C
ATOM   2417  N   PRO A 313       6.978   2.965  52.900  1.00 37.85           N
ANISOU 2417  N   PRO A 313     6007   4585   3788   -889    195    212       N
ATOM   2418  CA  PRO A 313       8.100   2.030  52.834  1.00 37.70           C
ANISOU 2418  CA  PRO A 313     6091   4472   3760   -880    200    241       C
ATOM   2419  C   PRO A 313       8.902   2.049  54.129  1.00 39.30           C
ANISOU 2419  C   PRO A 313     6300   4700   3933   -839    235    273       C
ATOM   2420  O   PRO A 313       8.952   3.052  54.840  1.00 38.21           O
ANISOU 2420  O   PRO A 313     6098   4640   3778   -791    248    250       O
ATOM   2421  CB  PRO A 313       8.918   2.557  51.644  1.00 35.78           C
ANISOU 2421  CB  PRO A 313     5890   4175   3531   -818    171    203       C
ATOM   2422  CG  PRO A 313       7.865   3.223  50.758  1.00 36.41           C
ANISOU 2422  CG  PRO A 313     5907   4299   3626   -838    138    169       C
ATOM   2423  CD  PRO A 313       6.996   3.926  51.778  1.00 35.69           C
ANISOU 2423  CD  PRO A 313     5714   4306   3539   -843    158    168       C
ATOM   2424  N   TRP A 314       9.517   0.920  54.447  1.00 36.49           N
ANISOU 2424  N   TRP A 314     6018   4276   3570   -857    245    325       N
ATOM   2425  CA  TRP A 314       9.439  -0.305  53.671  1.00 38.03           C
ANISOU 2425  CA  TRP A 314     6286   4367   3796   -913    230    343       C
ATOM   2426  C   TRP A 314       8.211  -1.151  54.031  1.00 38.00           C
ANISOU 2426  C   TRP A 314     6256   4377   3804  -1018    239    385       C
ATOM   2427  O   TRP A 314       7.856  -1.283  55.208  1.00 38.69           O
ANISOU 2427  O   TRP A 314     6303   4533   3864  -1044    273    441       O
ATOM   2428  CB  TRP A 314      10.716  -1.154  53.900  1.00 36.90           C
ANISOU 2428  CB  TRP A 314     6232   4130   3660   -878    238    383       C
ATOM   2429  CG  TRP A 314      11.793  -0.830  52.912  1.00 37.95           C
ANISOU 2429  CG  TRP A 314     6413   4199   3806   -805    221    334       C
ATOM   2430  CD1 TRP A 314      12.186   0.417  52.521  1.00 37.00           C
ANISOU 2430  CD1 TRP A 314     6257   4125   3677   -739    213    287       C
ATOM   2431  CD2 TRP A 314      12.608  -1.761  52.173  1.00 38.65           C
ANISOU 2431  CD2 TRP A 314     6591   4170   3925   -792    213    328       C
ATOM   2432  NE1 TRP A 314      13.186   0.323  51.589  1.00 35.18           N
ANISOU 2432  NE1 TRP A 314     6085   3822   3461   -689    205    261       N
ATOM   2433  CE2 TRP A 314      13.462  -1.000  51.349  1.00 39.99           C
ANISOU 2433  CE2 TRP A 314     6770   4333   4090   -717    206    279       C
ATOM   2434  CE3 TRP A 314      12.690  -3.167  52.126  1.00 40.29           C
ANISOU 2434  CE3 TRP A 314     6867   4271   4170   -834    213    359       C
ATOM   2435  CZ2 TRP A 314      14.396  -1.587  50.482  1.00 36.37           C
ANISOU 2435  CZ2 TRP A 314     6385   3781   3651   -680    205    254       C
ATOM   2436  CZ3 TRP A 314      13.611  -3.751  51.260  1.00 40.75           C
ANISOU 2436  CZ3 TRP A 314     7001   4224   4258   -795    207    325       C
ATOM   2437  CH2 TRP A 314      14.454  -2.957  50.446  1.00 39.53           C
ANISOU 2437  CH2 TRP A 314     6853   4082   4086   -717    205    271       C
ATOM   2438  N   THR A 315       7.589  -1.754  53.022  1.00 37.31           N
ANISOU 2438  N   THR A 315     6191   4230   3756  -1081    210    360       N
ATOM   2439  CA  THR A 315       6.704  -2.885  53.270  1.00 36.33           C
ANISOU 2439  CA  THR A 315     6066   4073   3664  -1187    215    407       C
ATOM   2440  C   THR A 315       7.009  -4.010  52.294  1.00 38.93           C
ANISOU 2440  C   THR A 315     6486   4260   4045  -1222    185    385       C
ATOM   2441  O   THR A 315       7.992  -3.937  51.557  1.00 37.62           O
ANISOU 2441  O   THR A 315     6385   4032   3877  -1155    169    340       O
ATOM   2442  CB  THR A 315       5.243  -2.504  53.142  1.00 31.64           C
ANISOU 2442  CB  THR A 315     5375   3568   3078  -1255    207    388       C
ATOM   2443  OG1 THR A 315       4.941  -2.163  51.781  1.00 39.58           O
ANISOU 2443  OG1 THR A 315     6382   4557   4100  -1254    157    310       O
ATOM   2444  CG2 THR A 315       4.908  -1.355  54.090  1.00 35.44           C
ANISOU 2444  CG2 THR A 315     5761   4192   3514  -1214    240    393       C
ATOM   2445  N   GLU A 316       6.144  -5.028  52.270  1.00 41.65           N
ANISOU 2445  N   GLU A 316     6829   4556   4440  -1327    177    411       N
ATOM   2446  CA  GLU A 316       6.388  -6.220  51.472  1.00 39.36           C
ANISOU 2446  CA  GLU A 316     6625   4117   4213  -1368    149    385       C
ATOM   2447  C   GLU A 316       6.708  -5.893  50.021  1.00 40.20           C
ANISOU 2447  C   GLU A 316     6771   4197   4308  -1327    106    276       C
ATOM   2448  O   GLU A 316       7.561  -6.544  49.419  1.00 42.26           O
ANISOU 2448  O   GLU A 316     7119   4347   4592  -1296     95    240       O
ATOM   2449  CB  GLU A 316       5.189  -7.184  51.534  1.00 40.14           C
ANISOU 2449  CB  GLU A 316     6695   4179   4379  -1501    138    413       C
ATOM   2450  CG  GLU A 316       5.494  -8.488  50.759  1.00 43.91           C
ANISOU 2450  CG  GLU A 316     7265   4483   4938  -1544    107    375       C
ATOM   2451  CD  GLU A 316       4.398  -9.529  50.800  1.00 46.36           C
ANISOU 2451  CD  GLU A 316     7551   4728   5334  -1681     92    400       C
ATOM   2452  OE1 GLU A 316       3.305  -9.250  51.344  1.00 47.22           O
ANISOU 2452  OE1 GLU A 316     7565   4938   5439  -1751    105    447       O
ATOM   2453  OE2 GLU A 316       4.659 -10.658  50.328  1.00 48.68           O
ANISOU 2453  OE2 GLU A 316     7919   4866   5711  -1719     69    374       O
ATOM   2454  N   ILE A 317       6.025  -4.906  49.431  1.00 39.33           N
ANISOU 2454  N   ILE A 317     6594   4190   4160  -1323     81    224       N
ATOM   2455  CA  ILE A 317       6.245  -4.579  48.015  1.00 39.02           C
ANISOU 2455  CA  ILE A 317     6587   4144   4096  -1288     37    132       C
ATOM   2456  C   ILE A 317       7.698  -4.193  47.723  1.00 41.09           C
ANISOU 2456  C   ILE A 317     6914   4375   4325  -1175     55    115       C
ATOM   2457  O   ILE A 317       8.201  -4.428  46.620  1.00 39.23           O
ANISOU 2457  O   ILE A 317     6739   4091   4076  -1149     32     47       O
ATOM   2458  CB  ILE A 317       5.286  -3.459  47.583  1.00 39.04           C
ANISOU 2458  CB  ILE A 317     6495   4273   4064  -1292      8    104       C
ATOM   2459  CG1 ILE A 317       5.337  -3.307  46.056  1.00 44.77           C
ANISOU 2459  CG1 ILE A 317     7254   4997   4759  -1277    -45     19       C
ATOM   2460  CG2 ILE A 317       5.655  -2.158  48.273  1.00 33.96           C
ANISOU 2460  CG2 ILE A 317     5797   3721   3384  -1207     41    139       C
ATOM   2461  CD1 ILE A 317       4.070  -2.749  45.423  1.00 42.89           C
ANISOU 2461  CD1 ILE A 317     6930   4856   4509  -1324    -96    -11       C
ATOM   2462  N   ASP A 318       8.391  -3.590  48.694  1.00 41.46           N
ANISOU 2462  N   ASP A 318     6943   4456   4352  -1108     95    171       N
ATOM   2463  CA  ASP A 318       9.795  -3.228  48.504  1.00 38.67           C
ANISOU 2463  CA  ASP A 318     6640   4075   3977  -1006    112    160       C
ATOM   2464  C   ASP A 318      10.680  -4.462  48.318  1.00 40.04           C
ANISOU 2464  C   ASP A 318     6911   4114   4190   -997    120    155       C
ATOM   2465  O   ASP A 318      11.626  -4.429  47.526  1.00 37.74           O
ANISOU 2465  O   ASP A 318     6672   3784   3886   -932    120    108       O
ATOM   2466  CB  ASP A 318      10.268  -2.355  49.680  1.00 36.00           C
ANISOU 2466  CB  ASP A 318     6255   3806   3618   -946    146    216       C
ATOM   2467  CG  ASP A 318       9.474  -1.049  49.782  1.00 38.83           C
ANISOU 2467  CG  ASP A 318     6516   4287   3950   -940    139    205       C
ATOM   2468  OD1 ASP A 318       9.790  -0.124  48.995  1.00 39.86           O
ANISOU 2468  OD1 ASP A 318     6634   4447   4063   -883    124    167       O
ATOM   2469  OD2 ASP A 318       8.502  -0.968  50.593  1.00 38.27           O
ANISOU 2469  OD2 ASP A 318     6379   4280   3881   -992    148    236       O
ATOM   2470  N   TYR A 319      10.384  -5.565  49.026  1.00 40.21           N
ANISOU 2470  N   TYR A 319     6954   4062   4264  -1061    128    205       N
ATOM   2471  CA  TYR A 319      11.127  -6.812  48.820  1.00 38.30           C
ANISOU 2471  CA  TYR A 319     6800   3673   4079  -1056    130    198       C
ATOM   2472  C   TYR A 319      10.826  -7.448  47.456  1.00 43.50           C
ANISOU 2472  C   TYR A 319     7507   4262   4759  -1094     94     93       C
ATOM   2473  O   TYR A 319      11.682  -8.127  46.888  1.00 42.27           O
ANISOU 2473  O   TYR A 319     7425   4003   4631  -1053     96     45       O
ATOM   2474  CB  TYR A 319      10.817  -7.793  49.953  1.00 38.01           C
ANISOU 2474  CB  TYR A 319     6768   3573   4103  -1119    146    294       C
ATOM   2475  CG  TYR A 319      11.355  -7.307  51.286  1.00 41.15           C
ANISOU 2475  CG  TYR A 319     7133   4036   4466  -1067    181    392       C
ATOM   2476  CD1 TYR A 319      12.691  -7.533  51.650  1.00 36.53           C
ANISOU 2476  CD1 TYR A 319     6597   3393   3890   -981    197    425       C
ATOM   2477  CD2 TYR A 319      10.546  -6.580  52.159  1.00 39.20           C
ANISOU 2477  CD2 TYR A 319     6802   3919   4173  -1099    196    442       C
ATOM   2478  CE1 TYR A 319      13.204  -7.052  52.855  1.00 35.66           C
ANISOU 2478  CE1 TYR A 319     6453   3356   3739   -933    220    506       C
ATOM   2479  CE2 TYR A 319      11.042  -6.113  53.378  1.00 38.34           C
ANISOU 2479  CE2 TYR A 319     6662   3884   4020  -1050    225    517       C
ATOM   2480  CZ  TYR A 319      12.376  -6.358  53.719  1.00 38.54           C
ANISOU 2480  CZ  TYR A 319     6739   3852   4050   -969    234    549       C
ATOM   2481  OH  TYR A 319      12.872  -5.893  54.917  1.00 44.33           O
ANISOU 2481  OH  TYR A 319     7440   4669   4733   -921    254    617       O
ATOM   2482  N   LEU A 320       9.632  -7.241  46.908  1.00 45.05           N
ANISOU 2482  N   LEU A 320     7658   4518   4941  -1169     59     51       N
ATOM   2483  CA  LEU A 320       9.337  -7.723  45.563  1.00 46.17           C
ANISOU 2483  CA  LEU A 320     7839   4618   5084  -1202     16    -60       C
ATOM   2484  C   LEU A 320       9.998  -6.885  44.475  1.00 46.97           C
ANISOU 2484  C   LEU A 320     7957   4786   5104  -1116     11   -131       C
ATOM   2485  O   LEU A 320       9.915  -7.237  43.297  1.00 43.31           O
ANISOU 2485  O   LEU A 320     7533   4305   4620  -1128    -21   -229       O
ATOM   2486  CB  LEU A 320       7.827  -7.741  45.326  1.00 40.84           C
ANISOU 2486  CB  LEU A 320     7101   3998   4418  -1312    -27    -80       C
ATOM   2487  CG  LEU A 320       7.169  -8.868  46.113  1.00 45.24           C
ANISOU 2487  CG  LEU A 320     7655   4462   5072  -1415    -25    -27       C
ATOM   2488  CD1 LEU A 320       5.682  -8.653  46.133  1.00 49.25           C
ANISOU 2488  CD1 LEU A 320     8074   5053   5586  -1517    -57    -22       C
ATOM   2489  CD2 LEU A 320       7.525 -10.240  45.503  1.00 44.78           C
ANISOU 2489  CD2 LEU A 320     7688   4235   5092  -1445    -45    -98       C
ATOM   2490  N   MET A 321      10.615  -5.765  44.817  1.00 42.82           N
ANISOU 2490  N   MET A 321     7398   4342   4529  -1034     40    -84       N
ATOM   2491  CA  MET A 321      11.201  -4.937  43.781  1.00 49.38           C
ANISOU 2491  CA  MET A 321     8237   5238   5288   -959     37   -134       C
ATOM   2492  C   MET A 321      12.685  -4.690  44.004  1.00 46.51           C
ANISOU 2492  C   MET A 321     7908   4845   4920   -855     84   -110       C
ATOM   2493  O   MET A 321      13.311  -4.019  43.185  1.00 47.79           O
ANISOU 2493  O   MET A 321     8075   5057   5027   -789     92   -141       O
ATOM   2494  CB  MET A 321      10.454  -3.597  43.685  1.00 46.88           C
ANISOU 2494  CB  MET A 321     7833   5059   4921   -960     17   -109       C
ATOM   2495  CG  MET A 321       9.028  -3.706  43.117  1.00 49.34           C
ANISOU 2495  CG  MET A 321     8103   5419   5224  -1051    -38   -147       C
ATOM   2496  SD  MET A 321       8.031  -2.227  43.491  1.00 59.69           S
ANISOU 2496  SD  MET A 321     9292   6875   6513  -1053    -55    -91       S
ATOM   2497  CE  MET A 321       8.399  -1.214  42.049  1.00 52.66           C
ANISOU 2497  CE  MET A 321     8402   6067   5539   -983    -81   -127       C
ATOM   2498  N   ALA A 322      13.263  -5.251  45.068  1.00 42.65           N
ANISOU 2498  N   ALA A 322     7438   4279   4487   -839    113    -53       N
ATOM   2499  CA  ALA A 322      14.593  -4.850  45.532  1.00 45.86           C
ANISOU 2499  CA  ALA A 322     7852   4678   4893   -742    153    -13       C
ATOM   2500  C   ALA A 322      15.730  -5.447  44.697  1.00 44.51           C
ANISOU 2500  C   ALA A 322     7754   4431   4729   -677    172    -75       C
ATOM   2501  O   ALA A 322      16.439  -4.733  43.972  1.00 44.15           O
ANISOU 2501  O   ALA A 322     7704   4437   4634   -609    188   -103       O
ATOM   2502  CB  ALA A 322      14.746  -5.252  47.003  1.00 38.32           C
ANISOU 2502  CB  ALA A 322     6888   3683   3987   -750    171     77       C
ATOM   2503  N   LEU A 323      15.899  -6.759  44.758  1.00 40.46           N
ANISOU 2503  N   LEU A 323     7302   3790   4280   -697    172    -97       N
ATOM   2504  CA  LEU A 323      17.052  -7.368  44.104  1.00 40.62           C
ANISOU 2504  CA  LEU A 323     7385   3730   4319   -624    197   -157       C
ATOM   2505  C   LEU A 323      16.794  -7.688  42.637  1.00 44.65           C
ANISOU 2505  C   LEU A 323     7935   4241   4787   -638    181   -281       C
ATOM   2506  O   LEU A 323      17.751  -7.900  41.885  1.00 42.20           O
ANISOU 2506  O   LEU A 323     7665   3906   4462   -567    208   -346       O
ATOM   2507  CB  LEU A 323      17.479  -8.618  44.884  1.00 42.60           C
ANISOU 2507  CB  LEU A 323     7682   3833   4672   -623    205   -122       C
ATOM   2508  CG  LEU A 323      18.080  -8.283  46.263  1.00 41.36           C
ANISOU 2508  CG  LEU A 323     7490   3689   4537   -581    225     -0       C
ATOM   2509  CD1 LEU A 323      18.702  -9.478  46.931  1.00 37.74           C
ANISOU 2509  CD1 LEU A 323     7077   3088   4176   -560    233     45       C
ATOM   2510  CD2 LEU A 323      19.111  -7.156  46.165  1.00 38.81           C
ANISOU 2510  CD2 LEU A 323     7130   3456   4159   -486    253      9       C
ATOM   2511  N   ASN A 324      15.531  -7.712  42.201  1.00 44.71           N
ANISOU 2511  N   ASN A 324     7929   4288   4770   -728    136   -320       N
ATOM   2512  CA  ASN A 324      15.269  -7.886  40.782  1.00 45.77           C
ANISOU 2512  CA  ASN A 324     8094   4452   4843   -740    113   -440       C
ATOM   2513  C   ASN A 324      15.414  -6.586  39.997  1.00 46.09           C
ANISOU 2513  C   ASN A 324     8095   4645   4770   -693    119   -441       C
ATOM   2514  O   ASN A 324      15.510  -6.633  38.764  1.00 47.83           O
ANISOU 2514  O   ASN A 324     8345   4911   4918   -677    112   -533       O
ATOM   2515  CB  ASN A 324      13.886  -8.522  40.561  1.00 44.32           C
ANISOU 2515  CB  ASN A 324     7910   4246   4684   -857     55   -489       C
ATOM   2516  CG  ASN A 324      12.803  -7.881  41.406  1.00 49.54           C
ANISOU 2516  CG  ASN A 324     8494   4978   5351   -926     32   -395       C
ATOM   2517  OD1 ASN A 324      13.075  -7.020  42.257  1.00 48.33           O
ANISOU 2517  OD1 ASN A 324     8293   4882   5189   -888     59   -297       O
ATOM   2518  ND2 ASN A 324      11.562  -8.305  41.183  1.00 46.86           N
ANISOU 2518  ND2 ASN A 324     8138   4638   5030  -1030    -19   -432       N
ATOM   2519  N   THR A 325      15.434  -5.431  40.673  1.00 45.52           N
ANISOU 2519  N   THR A 325     7957   4655   4683   -670    130   -341       N
ATOM   2520  CA  THR A 325      15.864  -4.192  40.029  1.00 43.91           C
ANISOU 2520  CA  THR A 325     7717   4570   4396   -609    146   -323       C
ATOM   2521  C   THR A 325      17.385  -4.094  40.007  1.00 42.93           C
ANISOU 2521  C   THR A 325     7614   4419   4278   -509    205   -313       C
ATOM   2522  O   THR A 325      17.960  -3.582  39.042  1.00 47.46           O
ANISOU 2522  O   THR A 325     8189   5062   4781   -456    228   -338       O
ATOM   2523  CB  THR A 325      15.283  -2.983  40.759  1.00 47.75           C
ANISOU 2523  CB  THR A 325     8120   5141   4883   -623    133   -230       C
ATOM   2524  OG1 THR A 325      13.860  -3.109  40.830  1.00 50.33           O
ANISOU 2524  OG1 THR A 325     8418   5494   5212   -715     81   -237       O
ATOM   2525  CG2 THR A 325      15.650  -1.667  40.048  1.00 42.64           C
ANISOU 2525  CG2 THR A 325     7430   4604   4166   -567    143   -202       C
ATOM   2526  N   SER A 326      18.042  -4.604  41.059  1.00 43.39           N
ANISOU 2526  N   SER A 326     7684   4383   4418   -483    230   -271       N
ATOM   2527  CA  SER A 326      19.489  -4.450  41.213  1.00 40.17           C
ANISOU 2527  CA  SER A 326     7280   3953   4029   -387    282   -249       C
ATOM   2528  C   SER A 326      20.265  -5.347  40.258  1.00 41.11           C
ANISOU 2528  C   SER A 326     7465   4015   4141   -339    312   -345       C
ATOM   2529  O   SER A 326      21.247  -4.905  39.656  1.00 39.09           O
ANISOU 2529  O   SER A 326     7202   3805   3847   -264    355   -356       O
ATOM   2530  CB  SER A 326      19.897  -4.738  42.658  1.00 37.34           C
ANISOU 2530  CB  SER A 326     6910   3521   3756   -374    290   -171       C
ATOM   2531  OG  SER A 326      19.160  -3.914  43.542  1.00 41.13           O
ANISOU 2531  OG  SER A 326     7329   4066   4234   -416    267    -96       O
ATOM   2532  N   VAL A 327      19.849  -6.609  40.114  1.00 40.49           N
ANISOU 2532  N   VAL A 327     7445   3834   4105   -381    291   -418       N
ATOM   2533  CA  VAL A 327      20.642  -7.562  39.342  1.00 39.83           C
ANISOU 2533  CA  VAL A 327     7424   3676   4035   -328    322   -521       C
ATOM   2534  C   VAL A 327      20.792  -7.143  37.882  1.00 42.88           C
ANISOU 2534  C   VAL A 327     7818   4171   4303   -300    339   -607       C
ATOM   2535  O   VAL A 327      21.933  -7.096  37.397  1.00 41.97           O
ANISOU 2535  O   VAL A 327     7709   4069   4166   -212    394   -635       O
ATOM   2536  CB  VAL A 327      20.086  -8.985  39.533  1.00 42.97           C
ANISOU 2536  CB  VAL A 327     7880   3926   4521   -387    290   -583       C
ATOM   2537  CG1 VAL A 327      20.599  -9.948  38.448  1.00 46.94           C
ANISOU 2537  CG1 VAL A 327     8449   4364   5024   -346    310   -730       C
ATOM   2538  CG2 VAL A 327      20.477  -9.494  40.910  1.00 38.81           C
ANISOU 2538  CG2 VAL A 327     7351   3283   4112   -375    297   -486       C
ATOM   2539  N   PRO A 328      19.723  -6.797  37.142  1.00 42.19           N
ANISOU 2539  N   PRO A 328     7724   4175   4130   -366    295   -645       N
ATOM   2540  CA  PRO A 328      19.938  -6.325  35.766  1.00 41.01           C
ANISOU 2540  CA  PRO A 328     7579   4151   3851   -332    312   -709       C
ATOM   2541  C   PRO A 328      20.807  -5.078  35.675  1.00 41.90           C
ANISOU 2541  C   PRO A 328     7637   4369   3915   -260    362   -618       C
ATOM   2542  O   PRO A 328      21.608  -4.969  34.744  1.00 43.86           O
ANISOU 2542  O   PRO A 328     7896   4679   4089   -196    411   -663       O
ATOM   2543  CB  PRO A 328      18.509  -6.050  35.267  1.00 46.20           C
ANISOU 2543  CB  PRO A 328     8223   4892   4439   -424    241   -730       C
ATOM   2544  CG  PRO A 328      17.614  -6.836  36.175  1.00 41.08           C
ANISOU 2544  CG  PRO A 328     7584   4127   3897   -508    193   -727       C
ATOM   2545  CD  PRO A 328      18.290  -6.788  37.491  1.00 42.97           C
ANISOU 2545  CD  PRO A 328     7805   4282   4240   -471    228   -625       C
ATOM   2546  N   LEU A 329      20.678  -4.129  36.611  1.00 41.31           N
ANISOU 2546  N   LEU A 329     7500   4317   3879   -269    353   -494       N
ATOM   2547  CA  LEU A 329      21.557  -2.960  36.582  1.00 43.13           C
ANISOU 2547  CA  LEU A 329     7675   4628   4086   -203    399   -409       C
ATOM   2548  C   LEU A 329      23.002  -3.370  36.786  1.00 43.33           C
ANISOU 2548  C   LEU A 329     7711   4589   4163   -117    465   -418       C
ATOM   2549  O   LEU A 329      23.902  -2.878  36.094  1.00 43.67           O
ANISOU 2549  O   LEU A 329     7734   4702   4156    -53    519   -412       O
ATOM   2550  CB  LEU A 329      21.135  -1.934  37.638  1.00 36.32           C
ANISOU 2550  CB  LEU A 329     6743   3785   3273   -230    372   -293       C
ATOM   2551  CG  LEU A 329      19.936  -1.053  37.274  1.00 40.98           C
ANISOU 2551  CG  LEU A 329     7292   4474   3803   -289    321   -259       C
ATOM   2552  CD1 LEU A 329      19.495  -0.244  38.468  1.00 42.81           C
ANISOU 2552  CD1 LEU A 329     7461   4702   4104   -313    297   -168       C
ATOM   2553  CD2 LEU A 329      20.301  -0.120  36.115  1.00 40.67           C
ANISOU 2553  CD2 LEU A 329     7229   4556   3669   -250    345   -236       C
ATOM   2554  N   TYR A 330      23.241  -4.299  37.718  1.00 43.84           N
ANISOU 2554  N   TYR A 330     7803   4523   4331   -113    461   -426       N
ATOM   2555  CA  TYR A 330      24.592  -4.819  37.894  1.00 45.30           C
ANISOU 2555  CA  TYR A 330     7998   4639   4576    -26    518   -441       C
ATOM   2556  C   TYR A 330      25.118  -5.383  36.582  1.00 44.76           C
ANISOU 2556  C   TYR A 330     7972   4593   4441     22    563   -557       C
ATOM   2557  O   TYR A 330      26.261  -5.114  36.194  1.00 46.77           O
ANISOU 2557  O   TYR A 330     8203   4886   4681    103    627   -555       O
ATOM   2558  CB  TYR A 330      24.611  -5.871  39.010  1.00 40.52           C
ANISOU 2558  CB  TYR A 330     7424   3884   4090    -35    497   -433       C
ATOM   2559  CG  TYR A 330      25.906  -6.650  39.104  1.00 42.63           C
ANISOU 2559  CG  TYR A 330     7709   4061   4429     56    546   -464       C
ATOM   2560  CD1 TYR A 330      27.073  -6.047  39.576  1.00 41.35           C
ANISOU 2560  CD1 TYR A 330     7489   3922   4298    131    586   -391       C
ATOM   2561  CD2 TYR A 330      25.973  -7.993  38.687  1.00 46.42           C
ANISOU 2561  CD2 TYR A 330     8257   4428   4951     69    551   -573       C
ATOM   2562  CE1 TYR A 330      28.265  -6.750  39.632  1.00 43.40           C
ANISOU 2562  CE1 TYR A 330     7757   4106   4628    219    630   -419       C
ATOM   2563  CE2 TYR A 330      27.167  -8.704  38.744  1.00 45.67           C
ANISOU 2563  CE2 TYR A 330     8173   4247   4931    161    597   -604       C
ATOM   2564  CZ  TYR A 330      28.300  -8.073  39.230  1.00 45.73           C
ANISOU 2564  CZ  TYR A 330     8120   4290   4967    237    636   -523       C
ATOM   2565  OH  TYR A 330      29.475  -8.764  39.295  1.00 47.02           O
ANISOU 2565  OH  TYR A 330     8284   4372   5209    331    679   -550       O
ATOM   2566  N   LYS A 331      24.282  -6.128  35.859  1.00 45.19           N
ANISOU 2566  N   LYS A 331     8085   4636   4450    -27    531   -665       N
ATOM   2567  CA  LYS A 331      24.770  -6.793  34.654  1.00 44.71           C
ANISOU 2567  CA  LYS A 331     8070   4592   4325     21    572   -799       C
ATOM   2568  C   LYS A 331      25.121  -5.774  33.575  1.00 47.10           C
ANISOU 2568  C   LYS A 331     8338   5070   4488     55    615   -784       C
ATOM   2569  O   LYS A 331      26.125  -5.924  32.865  1.00 48.23           O
ANISOU 2569  O   LYS A 331     8483   5251   4590    133    686   -838       O
ATOM   2570  CB  LYS A 331      23.732  -7.807  34.149  1.00 43.04           C
ANISOU 2570  CB  LYS A 331     7925   4328   4099    -49    518   -927       C
ATOM   2571  CG  LYS A 331      23.630  -9.097  35.002  1.00 47.90           C
ANISOU 2571  CG  LYS A 331     8587   4746   4866    -67    493   -964       C
ATOM   2572  CD  LYS A 331      22.709 -10.155  34.356  1.00 49.91           C
ANISOU 2572  CD  LYS A 331     8907   4940   5117   -134    443  -1112       C
ATOM   2573  CE  LYS A 331      22.698 -11.481  35.131  1.00 53.16           C
ANISOU 2573  CE  LYS A 331     9365   5139   5696   -149    424  -1145       C
ATOM   2574  NZ  LYS A 331      24.039 -12.081  35.508  1.00 48.49           N
ANISOU 2574  NZ  LYS A 331     8783   4433   5207    -43    484  -1148       N
ATOM   2575  N   GLN A 332      24.313  -4.724  33.446  1.00 45.01           N
ANISOU 2575  N   GLN A 332     8034   4915   4154     -1    576   -705       N
ATOM   2576  CA  GLN A 332      24.593  -3.686  32.457  1.00 46.80           C
ANISOU 2576  CA  GLN A 332     8223   5307   4253     26    612   -664       C
ATOM   2577  C   GLN A 332      25.930  -2.995  32.742  1.00 44.23           C
ANISOU 2577  C   GLN A 332     7838   5000   3968    106    688   -573       C
ATOM   2578  O   GLN A 332      26.783  -2.881  31.855  1.00 43.15           O
ANISOU 2578  O   GLN A 332     7693   4946   3757    168    758   -599       O
ATOM   2579  CB  GLN A 332      23.430  -2.685  32.433  1.00 42.30           C
ANISOU 2579  CB  GLN A 332     7615   4826   3631    -47    547   -579       C
ATOM   2580  CG  GLN A 332      22.202  -3.251  31.723  1.00 41.46           C
ANISOU 2580  CG  GLN A 332     7557   4753   3444   -118    480   -678       C
ATOM   2581  CD  GLN A 332      20.934  -2.429  31.912  1.00 42.28           C
ANISOU 2581  CD  GLN A 332     7620   4917   3527   -195    403   -598       C
ATOM   2582  OE1 GLN A 332      20.885  -1.477  32.689  1.00 49.17           O
ANISOU 2582  OE1 GLN A 332     8432   5790   4461   -199    397   -474       O
ATOM   2583  NE2 GLN A 332      19.917  -2.754  31.134  1.00 49.36           N
ANISOU 2583  NE2 GLN A 332     8544   5874   4336   -252    344   -675       N
ATOM   2584  N   LEU A 333      26.136  -2.550  33.983  1.00 45.59           N
ANISOU 2584  N   LEU A 333     7964   5101   4256    103    674   -471       N
ATOM   2585  CA  LEU A 333      27.403  -1.926  34.362  1.00 45.14           C
ANISOU 2585  CA  LEU A 333     7845   5051   4255    172    736   -391       C
ATOM   2586  C   LEU A 333      28.572  -2.866  34.149  1.00 47.21           C
ANISOU 2586  C   LEU A 333     8130   5257   4550    255    803   -471       C
ATOM   2587  O   LEU A 333      29.641  -2.455  33.682  1.00 48.61           O
ANISOU 2587  O   LEU A 333     8264   5499   4707    320    877   -448       O
ATOM   2588  CB  LEU A 333      27.383  -1.526  35.834  1.00 40.10           C
ANISOU 2588  CB  LEU A 333     7165   4333   3740    154    699   -296       C
ATOM   2589  CG  LEU A 333      27.039  -0.098  36.207  1.00 45.09           C
ANISOU 2589  CG  LEU A 333     7725   5031   4377    121    673   -178       C
ATOM   2590  CD1 LEU A 333      25.755   0.349  35.491  1.00 43.22           C
ANISOU 2590  CD1 LEU A 333     7500   4879   4043     54    625   -178       C
ATOM   2591  CD2 LEU A 333      26.882  -0.051  37.684  1.00 35.81           C
ANISOU 2591  CD2 LEU A 333     6527   3769   3312    100    630   -128       C
ATOM   2592  N   LYS A 334      28.406  -4.117  34.560  1.00 46.94           N
ANISOU 2592  N   LYS A 334     8156   5095   4584    254    780   -558       N
ATOM   2593  CA  LYS A 334      29.516  -5.051  34.580  1.00 50.03           C
ANISOU 2593  CA  LYS A 334     8563   5403   5041    338    836   -627       C
ATOM   2594  C   LYS A 334      30.028  -5.338  33.180  1.00 51.57           C
ANISOU 2594  C   LYS A 334     8779   5687   5130    393    906   -735       C
ATOM   2595  O   LYS A 334      31.199  -5.702  33.017  1.00 52.51           O
ANISOU 2595  O   LYS A 334     8880   5788   5285    481    978   -770       O
ATOM   2596  CB  LYS A 334      29.076  -6.333  35.282  1.00 51.12           C
ANISOU 2596  CB  LYS A 334     8765   5376   5282    316    787   -690       C
ATOM   2597  CG  LYS A 334      30.197  -7.268  35.591  1.00 48.88           C
ANISOU 2597  CG  LYS A 334     8490   4979   5104    406    832   -735       C
ATOM   2598  CD  LYS A 334      31.088  -6.716  36.651  1.00 47.20           C
ANISOU 2598  CD  LYS A 334     8205   4747   4983    449    844   -610       C
ATOM   2599  CE  LYS A 334      31.891  -7.876  37.257  1.00 49.61           C
ANISOU 2599  CE  LYS A 334     8528   4900   5422    521    856   -643       C
ATOM   2600  NZ  LYS A 334      32.898  -7.422  38.263  1.00 52.11           N
ANISOU 2600  NZ  LYS A 334     8770   5203   5828    575    866   -530       N
ATOM   2601  N   GLU A 335      29.170  -5.165  32.165  1.00 52.85           N
ANISOU 2601  N   GLU A 335     8972   5953   5153    344    887   -788       N
ATOM   2602  CA  GLU A 335      29.568  -5.418  30.787  1.00 53.02           C
ANISOU 2602  CA  GLU A 335     9015   6084   5046    391    951   -897       C
ATOM   2603  C   GLU A 335      30.791  -4.590  30.400  1.00 55.24           C
ANISOU 2603  C   GLU A 335     9221   6476   5291    465   1046   -821       C
ATOM   2604  O   GLU A 335      31.777  -5.130  29.889  1.00 53.45           O
ANISOU 2604  O   GLU A 335     8993   6259   5057    548   1126   -903       O
ATOM   2605  CB  GLU A 335      28.400  -5.108  29.851  1.00 51.61           C
ANISOU 2605  CB  GLU A 335     8867   6028   4713    319    903   -932       C
ATOM   2606  CG  GLU A 335      27.447  -6.265  29.582  1.00 59.32           C
ANISOU 2606  CG  GLU A 335     9928   6931   5679    269    840  -1086       C
ATOM   2607  CD  GLU A 335      28.083  -7.653  29.745  1.00 69.67           C
ANISOU 2607  CD  GLU A 335    11288   8090   7094    328    871  -1225       C
ATOM   2608  OE1 GLU A 335      28.736  -8.144  28.791  1.00 70.19           O
ANISOU 2608  OE1 GLU A 335    11375   8208   7087    397    938  -1351       O
ATOM   2609  OE2 GLU A 335      27.914  -8.265  30.833  1.00 75.62           O
ANISOU 2609  OE2 GLU A 335    12059   8671   8002    308    829  -1208       O
ATOM   2610  N   THR A 336      30.768  -3.283  30.680  1.00 54.95           N
ANISOU 2610  N   THR A 336     9115   6515   5248    437   1039   -665       N
ATOM   2611  CA  THR A 336      31.888  -2.407  30.330  1.00 55.15           C
ANISOU 2611  CA  THR A 336     9060   6643   5252    494   1126   -576       C
ATOM   2612  C   THR A 336      32.788  -2.048  31.505  1.00 57.32           C
ANISOU 2612  C   THR A 336     9265   6829   5686    527   1139   -477       C
ATOM   2613  O   THR A 336      33.883  -1.521  31.289  1.00 60.71           O
ANISOU 2613  O   THR A 336     9622   7319   6125    583   1216   -420       O
ATOM   2614  CB  THR A 336      31.376  -1.105  29.688  1.00 58.73           C
ANISOU 2614  CB  THR A 336     9474   7251   5591    445   1118   -462       C
ATOM   2615  OG1 THR A 336      30.366  -0.510  30.518  1.00 55.74           O
ANISOU 2615  OG1 THR A 336     9088   6821   5270    366   1023   -377       O
ATOM   2616  CG2 THR A 336      30.842  -1.349  28.249  1.00 49.58           C
ANISOU 2616  CG2 THR A 336     8365   6234   4239    435   1131   -552       C
ATOM   2617  N   MET A 337      32.368  -2.313  32.735  1.00 57.59           N
ANISOU 2617  N   MET A 337     9312   6728   5840    494   1065   -453       N
ATOM   2618  CA  MET A 337      33.122  -1.913  33.922  1.00 52.62           C
ANISOU 2618  CA  MET A 337     8615   6026   5350    518   1062   -357       C
ATOM   2619  C   MET A 337      33.277  -3.104  34.856  1.00 48.83           C
ANISOU 2619  C   MET A 337     8177   5387   4988    545   1031   -417       C
ATOM   2620  O   MET A 337      32.579  -3.195  35.874  1.00 48.68           O
ANISOU 2620  O   MET A 337     8176   5285   5034    493    955   -380       O
ATOM   2621  CB  MET A 337      32.427  -0.739  34.596  1.00 48.98           C
ANISOU 2621  CB  MET A 337     8113   5587   4912    446    998   -235       C
ATOM   2622  CG  MET A 337      32.098   0.312  33.591  1.00 55.03           C
ANISOU 2622  CG  MET A 337     8850   6495   5562    416   1018   -179       C
ATOM   2623  SD  MET A 337      31.316   1.741  34.286  1.00 56.28           S
ANISOU 2623  SD  MET A 337     8952   6670   5760    341    948    -42       S
ATOM   2624  CE  MET A 337      32.446   2.979  33.641  1.00 45.70           C
ANISOU 2624  CE  MET A 337     7511   5439   4412    379   1031     69       C
ATOM   2625  N   PRO A 338      34.200  -4.026  34.543  1.00 48.34           N
ANISOU 2625  N   PRO A 338     8126   5283   4959    629   1091   -503       N
ATOM   2626  CA  PRO A 338      34.426  -5.191  35.417  1.00 46.53           C
ANISOU 2626  CA  PRO A 338     7932   4891   4856    663   1063   -549       C
ATOM   2627  C   PRO A 338      34.853  -4.830  36.814  1.00 50.13           C
ANISOU 2627  C   PRO A 338     8331   5282   5436    668   1023   -433       C
ATOM   2628  O   PRO A 338      34.839  -5.707  37.692  1.00 48.18           O
ANISOU 2628  O   PRO A 338     8115   4904   5289    680    982   -442       O
ATOM   2629  CB  PRO A 338      35.543  -5.974  34.704  1.00 49.18           C
ANISOU 2629  CB  PRO A 338     8263   5218   5203    769   1151   -650       C
ATOM   2630  CG  PRO A 338      36.152  -5.000  33.710  1.00 56.89           C
ANISOU 2630  CG  PRO A 338     9174   6366   6075    794   1234   -620       C
ATOM   2631  CD  PRO A 338      35.048  -4.045  33.335  1.00 51.09           C
ANISOU 2631  CD  PRO A 338     8452   5735   5225    698   1191   -563       C
ATOM   2632  N   GLU A 339      35.274  -3.584  37.048  1.00 48.37           N
ANISOU 2632  N   GLU A 339     8022   5146   5212    660   1035   -326       N
ATOM   2633  CA  GLU A 339      35.599  -3.163  38.401  1.00 44.70           C
ANISOU 2633  CA  GLU A 339     7501   4631   4852    656    987   -227       C
ATOM   2634  C   GLU A 339      34.371  -3.113  39.305  1.00 42.84           C
ANISOU 2634  C   GLU A 339     7307   4346   4624    570    895   -190       C
ATOM   2635  O   GLU A 339      34.525  -3.058  40.525  1.00 45.59           O
ANISOU 2635  O   GLU A 339     7627   4641   5055    568    848   -126       O
ATOM   2636  CB  GLU A 339      36.293  -1.806  38.371  1.00 45.59           C
ANISOU 2636  CB  GLU A 339     7509   4844   4968    661   1019   -134       C
ATOM   2637  CG  GLU A 339      37.715  -1.862  37.876  1.00 48.04           C
ANISOU 2637  CG  GLU A 339     7753   5190   5310    752   1106   -145       C
ATOM   2638  CD  GLU A 339      37.802  -1.802  36.362  1.00 56.56           C
ANISOU 2638  CD  GLU A 339     8845   6374   6273    769   1190   -201       C
ATOM   2639  OE1 GLU A 339      36.753  -1.623  35.698  1.00 59.46           O
ANISOU 2639  OE1 GLU A 339     9269   6792   6530    708   1173   -225       O
ATOM   2640  OE2 GLU A 339      38.923  -1.936  35.834  1.00 66.32           O
ANISOU 2640  OE2 GLU A 339    10028   7650   7522    846   1274   -222       O
ATOM   2641  N   VAL A 340      33.162  -3.106  38.749  1.00 44.20           N
ANISOU 2641  N   VAL A 340     7539   4546   4709    500    868   -227       N
ATOM   2642  CA  VAL A 340      31.975  -3.021  39.595  1.00 41.40           C
ANISOU 2642  CA  VAL A 340     7212   4155   4363    417    787   -190       C
ATOM   2643  C   VAL A 340      31.804  -4.332  40.353  1.00 44.41           C
ANISOU 2643  C   VAL A 340     7653   4400   4822    422    751   -222       C
ATOM   2644  O   VAL A 340      31.835  -5.426  39.769  1.00 43.39           O
ANISOU 2644  O   VAL A 340     7585   4205   4696    448    772   -315       O
ATOM   2645  CB  VAL A 340      30.734  -2.669  38.761  1.00 43.15           C
ANISOU 2645  CB  VAL A 340     7472   4447   4476    342    766   -219       C
ATOM   2646  CG1 VAL A 340      29.458  -2.642  39.629  1.00 41.78           C
ANISOU 2646  CG1 VAL A 340     7322   4237   4316    257    686   -186       C
ATOM   2647  CG2 VAL A 340      30.908  -1.293  38.100  1.00 44.07           C
ANISOU 2647  CG2 VAL A 340     7523   4693   4528    337    796   -160       C
ATOM   2648  N   VAL A 341      31.624  -4.222  41.662  1.00 41.53           N
ANISOU 2648  N   VAL A 341     7267   3992   4519    398    698   -144       N
ATOM   2649  CA  VAL A 341      31.477  -5.366  42.545  1.00 40.67           C
ANISOU 2649  CA  VAL A 341     7205   3760   4490    399    660   -140       C
ATOM   2650  C   VAL A 341      30.011  -5.699  42.806  1.00 42.35           C
ANISOU 2650  C   VAL A 341     7474   3941   4675    302    604   -145       C
ATOM   2651  O   VAL A 341      29.635  -6.869  42.808  1.00 40.79           O
ANISOU 2651  O   VAL A 341     7343   3639   4518    289    589   -190       O
ATOM   2652  CB  VAL A 341      32.225  -5.081  43.865  1.00 39.62           C
ANISOU 2652  CB  VAL A 341     7009   3613   4431    434    635    -44       C
ATOM   2653  CG1 VAL A 341      31.921  -6.134  44.902  1.00 39.81           C
ANISOU 2653  CG1 VAL A 341     7077   3525   4524    423    587     -9       C
ATOM   2654  CG2 VAL A 341      33.724  -5.020  43.606  1.00 42.84           C
ANISOU 2654  CG2 VAL A 341     7361   4030   4886    535    688    -48       C
ATOM   2655  N   ALA A 342      29.167  -4.693  43.033  1.00 36.37           N
ANISOU 2655  N   ALA A 342     6688   3269   3862    233    573   -100       N
ATOM   2656  CA  ALA A 342      27.788  -4.940  43.420  1.00 34.19           C
ANISOU 2656  CA  ALA A 342     6449   2973   3568    141    521    -93       C
ATOM   2657  C   ALA A 342      26.985  -3.672  43.214  1.00 36.50           C
ANISOU 2657  C   ALA A 342     6699   3382   3787     84    503    -67       C
ATOM   2658  O   ALA A 342      27.513  -2.568  43.383  1.00 35.47           O
ANISOU 2658  O   ALA A 342     6502   3325   3651    111    516    -19       O
ATOM   2659  CB  ALA A 342      27.689  -5.404  44.890  1.00 33.25           C
ANISOU 2659  CB  ALA A 342     6327   2787   3519    127    480    -15       C
ATOM   2660  N   VAL A 343      25.702  -3.839  42.870  1.00 36.66           N
ANISOU 2660  N   VAL A 343     6755   3412   3763      6    471    -99       N
ATOM   2661  CA  VAL A 343      24.767  -2.723  42.679  1.00 33.86           C
ANISOU 2661  CA  VAL A 343     6361   3158   3346    -51    447    -75       C
ATOM   2662  C   VAL A 343      23.550  -2.896  43.599  1.00 37.46           C
ANISOU 2662  C   VAL A 343     6819   3597   3816   -132    396    -42       C
ATOM   2663  O   VAL A 343      22.802  -3.871  43.479  1.00 35.43           O
ANISOU 2663  O   VAL A 343     6615   3280   3568   -183    374    -82       O
ATOM   2664  CB  VAL A 343      24.319  -2.598  41.218  1.00 37.48           C
ANISOU 2664  CB  VAL A 343     6845   3677   3720    -68    457   -143       C
ATOM   2665  CG1 VAL A 343      23.216  -1.575  41.114  1.00 38.66           C
ANISOU 2665  CG1 VAL A 343     6954   3917   3819   -130    420   -109       C
ATOM   2666  CG2 VAL A 343      25.515  -2.184  40.291  1.00 33.70           C
ANISOU 2666  CG2 VAL A 343     6346   3248   3208     10    517   -159       C
ATOM   2667  N   ASN A 344      23.331  -1.928  44.494  1.00 35.26           N
ANISOU 2667  N   ASN A 344     6478   3375   3544   -145    377     25       N
ATOM   2668  CA  ASN A 344      22.157  -1.904  45.360  1.00 36.48           C
ANISOU 2668  CA  ASN A 344     6618   3540   3701   -218    337     58       C
ATOM   2669  C   ASN A 344      21.209  -0.828  44.827  1.00 36.53           C
ANISOU 2669  C   ASN A 344     6583   3642   3656   -260    318     53       C
ATOM   2670  O   ASN A 344      21.392   0.365  45.101  1.00 36.04           O
ANISOU 2670  O   ASN A 344     6456   3644   3593   -239    319     89       O
ATOM   2671  CB  ASN A 344      22.571  -1.652  46.811  1.00 33.86           C
ANISOU 2671  CB  ASN A 344     6245   3210   3408   -199    330    127       C
ATOM   2672  CG  ASN A 344      21.411  -1.305  47.723  1.00 34.67           C
ANISOU 2672  CG  ASN A 344     6314   3360   3498   -266    299    162       C
ATOM   2673  OD1 ASN A 344      20.237  -1.332  47.333  1.00 35.48           O
ANISOU 2673  OD1 ASN A 344     6422   3485   3575   -331    280    140       O
ATOM   2674  ND2 ASN A 344      21.742  -0.949  48.959  1.00 35.01           N
ANISOU 2674  ND2 ASN A 344     6315   3430   3556   -247    292    214       N
ATOM   2675  N   ALA A 345      20.168  -1.244  44.095  1.00 35.35           N
ANISOU 2675  N   ALA A 345     6465   3497   3471   -320    296      8       N
ATOM   2676  CA  ALA A 345      19.167  -0.300  43.580  1.00 36.01           C
ANISOU 2676  CA  ALA A 345     6504   3670   3507   -361    269      9       C
ATOM   2677  C   ALA A 345      17.782  -0.559  44.181  1.00 34.31           C
ANISOU 2677  C   ALA A 345     6275   3461   3300   -444    230     17       C
ATOM   2678  O   ALA A 345      16.771  -0.540  43.486  1.00 41.49           O
ANISOU 2678  O   ALA A 345     7182   4408   4174   -497    200    -14       O
ATOM   2679  CB  ALA A 345      19.118  -0.343  42.051  1.00 35.91           C
ANISOU 2679  CB  ALA A 345     6523   3692   3431   -356    272    -47       C
ATOM   2680  N   MET A 346      17.728  -0.808  45.484  1.00 34.71           N
ANISOU 2680  N   MET A 346     6312   3484   3394   -457    231     61       N
ATOM   2681  CA  MET A 346      16.537  -1.314  46.156  1.00 38.16           C
ANISOU 2681  CA  MET A 346     6740   3916   3844   -538    206     75       C
ATOM   2682  C   MET A 346      15.538  -0.237  46.566  1.00 41.49           C
ANISOU 2682  C   MET A 346     7081   4433   4250   -570    187     99       C
ATOM   2683  O   MET A 346      14.429  -0.592  46.997  1.00 41.66           O
ANISOU 2683  O   MET A 346     7086   4467   4278   -641    168    108       O
ATOM   2684  CB  MET A 346      16.943  -2.097  47.407  1.00 36.70           C
ANISOU 2684  CB  MET A 346     6574   3668   3703   -537    220    125       C
ATOM   2685  CG  MET A 346      17.935  -3.229  47.117  1.00 35.70           C
ANISOU 2685  CG  MET A 346     6522   3432   3611   -499    237    107       C
ATOM   2686  SD  MET A 346      17.964  -4.379  48.468  1.00 38.74           S
ANISOU 2686  SD  MET A 346     6932   3734   4052   -525    238    179       S
ATOM   2687  CE  MET A 346      18.756  -3.344  49.716  1.00 33.28           C
ANISOU 2687  CE  MET A 346     6177   3123   3345   -460    250    248       C
ATOM   2688  N   TYR A 347      15.873   1.055  46.431  1.00 31.38           N
ANISOU 2688  N   TYR A 347     5748   3216   2960   -520    191    110       N
ATOM   2689  CA  TYR A 347      15.126   2.121  47.109  1.00 37.10           C
ANISOU 2689  CA  TYR A 347     6388   4016   3690   -532    178    132       C
ATOM   2690  C   TYR A 347      14.201   2.816  46.119  1.00 35.35           C
ANISOU 2690  C   TYR A 347     6130   3854   3448   -555    148    114       C
ATOM   2691  O   TYR A 347      14.664   3.565  45.260  1.00 39.87           O
ANISOU 2691  O   TYR A 347     6693   4447   4008   -511    148    113       O
ATOM   2692  CB  TYR A 347      16.091   3.096  47.787  1.00 34.84           C
ANISOU 2692  CB  TYR A 347     6060   3750   3429   -463    196    155       C
ATOM   2693  CG  TYR A 347      17.053   2.294  48.620  1.00 35.46           C
ANISOU 2693  CG  TYR A 347     6179   3774   3521   -437    218    175       C
ATOM   2694  CD1 TYR A 347      16.608   1.602  49.744  1.00 36.62           C
ANISOU 2694  CD1 TYR A 347     6329   3917   3668   -476    218    202       C
ATOM   2695  CD2 TYR A 347      18.384   2.138  48.239  1.00 34.91           C
ANISOU 2695  CD2 TYR A 347     6144   3658   3464   -375    238    174       C
ATOM   2696  CE1 TYR A 347      17.467   0.827  50.491  1.00 33.92           C
ANISOU 2696  CE1 TYR A 347     6024   3527   3338   -452    231    234       C
ATOM   2697  CE2 TYR A 347      19.254   1.354  48.990  1.00 32.92           C
ANISOU 2697  CE2 TYR A 347     5925   3354   3231   -348    252    197       C
ATOM   2698  CZ  TYR A 347      18.786   0.695  50.107  1.00 36.23           C
ANISOU 2698  CZ  TYR A 347     6349   3769   3649   -385    245    230       C
ATOM   2699  OH  TYR A 347      19.641  -0.101  50.844  1.00 29.82           O
ANISOU 2699  OH  TYR A 347     5568   2905   2855   -356    254    267       O
ATOM   2700  N   THR A 348      12.897   2.523  46.227  1.00 36.69           N
ANISOU 2700  N   THR A 348     6276   4051   3613   -626    123    106       N
ATOM   2701  CA  THR A 348      11.834   3.157  45.448  1.00 35.84           C
ANISOU 2701  CA  THR A 348     6119   4009   3490   -654     85     95       C
ATOM   2702  C   THR A 348      12.050   2.930  43.952  1.00 41.29           C
ANISOU 2702  C   THR A 348     6860   4695   4134   -648     67     65       C
ATOM   2703  O   THR A 348      12.107   3.872  43.145  1.00 34.26           O
ANISOU 2703  O   THR A 348     5939   3854   3224   -613     53     77       O
ATOM   2704  CB  THR A 348      11.743   4.649  45.782  1.00 39.16           C
ANISOU 2704  CB  THR A 348     6454   4488   3938   -608     84    119       C
ATOM   2705  OG1 THR A 348      12.014   4.817  47.176  1.00 37.79           O
ANISOU 2705  OG1 THR A 348     6251   4313   3795   -592    111    133       O
ATOM   2706  CG2 THR A 348      10.359   5.200  45.459  1.00 37.81           C
ANISOU 2706  CG2 THR A 348     6212   4385   3771   -646     44    117       C
ATOM   2707  N   HIS A 349      12.147   1.632  43.609  1.00 40.72           N
ANISOU 2707  N   HIS A 349     6862   4563   4045   -684     67     26       N
ATOM   2708  CA  HIS A 349      12.395   1.151  42.258  1.00 37.59           C
ANISOU 2708  CA  HIS A 349     6525   4160   3596   -682     54    -24       C
ATOM   2709  C   HIS A 349      13.675   1.752  41.683  1.00 36.42           C
ANISOU 2709  C   HIS A 349     6396   4020   3423   -597     87    -11       C
ATOM   2710  O   HIS A 349      13.760   2.095  40.505  1.00 39.53           O
ANISOU 2710  O   HIS A 349     6798   4464   3758   -578     76    -24       O
ATOM   2711  CB  HIS A 349      11.195   1.417  41.351  1.00 40.47           C
ANISOU 2711  CB  HIS A 349     6857   4601   3920   -731     -2    -45       C
ATOM   2712  CG  HIS A 349      11.035   0.402  40.256  1.00 45.75           C
ANISOU 2712  CG  HIS A 349     7593   5254   4538   -769    -28   -121       C
ATOM   2713  ND1 HIS A 349      10.132   0.556  39.223  1.00 48.86           N
ANISOU 2713  ND1 HIS A 349     7967   5724   4875   -806    -85   -152       N
ATOM   2714  CD2 HIS A 349      11.671  -0.777  40.027  1.00 44.08           C
ANISOU 2714  CD2 HIS A 349     7465   4958   4326   -771     -9   -180       C
ATOM   2715  CE1 HIS A 349      10.214  -0.485  38.409  1.00 49.66           C
ANISOU 2715  CE1 HIS A 349     8138   5795   4935   -834   -100   -235       C
ATOM   2716  NE2 HIS A 349      11.136  -1.311  38.876  1.00 45.93           N
ANISOU 2716  NE2 HIS A 349     7730   5219   4502   -812    -52   -257       N
ATOM   2717  N   GLY A 350      14.695   1.858  42.519  1.00 36.56           N
ANISOU 2717  N   GLY A 350     6417   3992   3483   -546    129     19       N
ATOM   2718  CA  GLY A 350      15.965   2.344  42.025  1.00 39.42           C
ANISOU 2718  CA  GLY A 350     6791   4356   3832   -470    165     32       C
ATOM   2719  C   GLY A 350      16.097   3.847  41.869  1.00 37.74           C
ANISOU 2719  C   GLY A 350     6506   4207   3627   -430    165     85       C
ATOM   2720  O   GLY A 350      16.999   4.298  41.165  1.00 34.76           O
ANISOU 2720  O   GLY A 350     6133   3845   3231   -378    191    102       O
ATOM   2721  N   ILE A 351      15.245   4.644  42.516  1.00 35.17           N
ANISOU 2721  N   ILE A 351     6110   3916   3337   -451    138    114       N
ATOM   2722  CA  ILE A 351      15.530   6.076  42.572  1.00 37.36           C
ANISOU 2722  CA  ILE A 351     6317   4227   3651   -405    141    164       C
ATOM   2723  C   ILE A 351      16.793   6.336  43.408  1.00 35.66           C
ANISOU 2723  C   ILE A 351     6094   3967   3489   -352    181    180       C
ATOM   2724  O   ILE A 351      17.515   7.313  43.169  1.00 32.42           O
ANISOU 2724  O   ILE A 351     5646   3564   3109   -305    196    215       O
ATOM   2725  CB  ILE A 351      14.299   6.849  43.092  1.00 35.27           C
ANISOU 2725  CB  ILE A 351     5974   4005   3423   -434    104    177       C
ATOM   2726  CG1 ILE A 351      13.134   6.693  42.103  1.00 32.77           C
ANISOU 2726  CG1 ILE A 351     5655   3742   3055   -481     59    168       C
ATOM   2727  CG2 ILE A 351      14.622   8.354  43.266  1.00 35.16           C
ANISOU 2727  CG2 ILE A 351     5883   4005   3472   -383    106    222       C
ATOM   2728  CD1 ILE A 351      11.810   7.209  42.633  1.00 32.35           C
ANISOU 2728  CD1 ILE A 351     5524   3730   3038   -515     22    173       C
ATOM   2729  N   GLY A 352      17.065   5.483  44.395  1.00 28.98           N
ANISOU 2729  N   GLY A 352     5279   3075   2658   -361    195    160       N
ATOM   2730  CA  GLY A 352      18.294   5.514  45.170  1.00 30.31           C
ANISOU 2730  CA  GLY A 352     5446   3204   2865   -312    226    171       C
ATOM   2731  C   GLY A 352      19.138   4.301  44.806  1.00 33.82           C
ANISOU 2731  C   GLY A 352     5969   3593   3286   -296    253    150       C
ATOM   2732  O   GLY A 352      18.624   3.181  44.701  1.00 32.17           O
ANISOU 2732  O   GLY A 352     5816   3356   3052   -337    245    121       O
ATOM   2733  N   VAL A 353      20.419   4.540  44.563  1.00 30.07           N
ANISOU 2733  N   VAL A 353     5494   3102   2829   -236    285    163       N
ATOM   2734  CA  VAL A 353      21.310   3.494  44.088  1.00 27.60           C
ANISOU 2734  CA  VAL A 353     5246   2740   2500   -207    317    138       C
ATOM   2735  C   VAL A 353      22.652   3.660  44.764  1.00 33.10           C
ANISOU 2735  C   VAL A 353     5920   3408   3250   -147    344    161       C
ATOM   2736  O   VAL A 353      23.173   4.775  44.847  1.00 34.20           O
ANISOU 2736  O   VAL A 353     5996   3575   3423   -117    350    191       O
ATOM   2737  CB  VAL A 353      21.513   3.517  42.565  1.00 33.51           C
ANISOU 2737  CB  VAL A 353     6022   3519   3193   -192    337    121       C
ATOM   2738  CG1 VAL A 353      22.371   2.277  42.132  1.00 31.54           C
ANISOU 2738  CG1 VAL A 353     5843   3213   2928   -160    373     75       C
ATOM   2739  CG2 VAL A 353      20.182   3.603  41.803  1.00 32.16           C
ANISOU 2739  CG2 VAL A 353     5858   3398   2964   -249    300    104       C
ATOM   2740  N   ILE A 354      23.223   2.552  45.225  1.00 32.41           N
ANISOU 2740  N   ILE A 354     5878   3258   3176   -129    356    148       N
ATOM   2741  CA  ILE A 354      24.551   2.508  45.817  1.00 33.03           C
ANISOU 2741  CA  ILE A 354     5938   3307   3303    -68    377    167       C
ATOM   2742  C   ILE A 354      25.356   1.433  45.089  1.00 34.93           C
ANISOU 2742  C   ILE A 354     6239   3494   3540    -27    413    136       C
ATOM   2743  O   ILE A 354      24.912   0.281  44.987  1.00 35.27           O
ANISOU 2743  O   ILE A 354     6347   3483   3571    -51    407    105       O
ATOM   2744  CB  ILE A 354      24.480   2.212  47.326  1.00 30.73           C
ANISOU 2744  CB  ILE A 354     5635   2999   3042    -77    350    192       C
ATOM   2745  CG1 ILE A 354      23.527   3.191  48.001  1.00 29.44           C
ANISOU 2745  CG1 ILE A 354     5416   2895   2874   -119    318    203       C
ATOM   2746  CG2 ILE A 354      25.863   2.292  47.935  1.00 30.28           C
ANISOU 2746  CG2 ILE A 354     5546   2925   3033    -12    362    214       C
ATOM   2747  CD1 ILE A 354      23.111   2.756  49.337  1.00 31.32           C
ANISOU 2747  CD1 ILE A 354     5653   3135   3110   -144    295    222       C
ATOM   2748  N   ILE A 355      26.536   1.807  44.596  1.00 32.58           N
ANISOU 2748  N   ILE A 355     5912   3206   3260     34    452    142       N
ATOM   2749  CA  ILE A 355      27.371   0.953  43.761  1.00 31.38           C
ANISOU 2749  CA  ILE A 355     5803   3017   3101     83    498    105       C
ATOM   2750  C   ILE A 355      28.708   0.809  44.460  1.00 35.44           C
ANISOU 2750  C   ILE A 355     6283   3497   3684    150    515    130       C
ATOM   2751  O   ILE A 355      29.265   1.801  44.948  1.00 34.20           O
ANISOU 2751  O   ILE A 355     6052   3377   3564    168    512    171       O
ATOM   2752  CB  ILE A 355      27.560   1.544  42.352  1.00 33.58           C
ANISOU 2752  CB  ILE A 355     6072   3361   3326     97    538     91       C
ATOM   2753  CG1 ILE A 355      26.202   1.808  41.687  1.00 33.09           C
ANISOU 2753  CG1 ILE A 355     6032   3347   3193     31    508     76       C
ATOM   2754  CG2 ILE A 355      28.440   0.625  41.490  1.00 32.70           C
ANISOU 2754  CG2 ILE A 355     6002   3223   3199    154    592     38       C
ATOM   2755  CD1 ILE A 355      26.278   2.940  40.583  1.00 31.68           C
ANISOU 2755  CD1 ILE A 355     5812   3260   2966     37    533    107       C
ATOM   2756  N   SER A 356      29.181  -0.424  44.585  1.00 35.60           N
ANISOU 2756  N   SER A 356     6352   3442   3731    185    527    104       N
ATOM   2757  CA  SER A 356      30.523  -0.668  45.084  1.00 35.29           C
ANISOU 2757  CA  SER A 356     6279   3370   3759    259    545    125       C
ATOM   2758  C   SER A 356      31.412  -1.041  43.915  1.00 34.63           C
ANISOU 2758  C   SER A 356     6205   3281   3671    321    610     79       C
ATOM   2759  O   SER A 356      31.044  -1.854  43.067  1.00 34.53           O
ANISOU 2759  O   SER A 356     6261   3239   3622    316    630     15       O
ATOM   2760  CB  SER A 356      30.542  -1.779  46.146  1.00 37.32           C
ANISOU 2760  CB  SER A 356     6573   3544   4063    268    512    144       C
ATOM   2761  OG  SER A 356      30.007  -2.968  45.615  1.00 43.70           O
ANISOU 2761  OG  SER A 356     7464   4277   4862    252    518     93       O
ATOM   2762  N   THR A 357      32.580  -0.445  43.855  1.00 37.72           N
ANISOU 2762  N   THR A 357     6526   3706   4100    377    644    105       N
ATOM   2763  CA  THR A 357      33.422  -0.712  42.706  1.00 37.09           C
ANISOU 2763  CA  THR A 357     6445   3640   4008    436    715     62       C
ATOM   2764  C   THR A 357      34.853  -0.546  43.158  1.00 37.80           C
ANISOU 2764  C   THR A 357     6458   3726   4179    509    739     96       C
ATOM   2765  O   THR A 357      35.134   0.238  44.072  1.00 37.70           O
ANISOU 2765  O   THR A 357     6378   3735   4213    501    703    154       O
ATOM   2766  CB  THR A 357      33.111   0.248  41.532  1.00 34.84           C
ANISOU 2766  CB  THR A 357     6141   3451   3645    408    752     62       C
ATOM   2767  OG1 THR A 357      33.962  -0.043  40.413  1.00 38.30           O
ANISOU 2767  OG1 THR A 357     6576   3919   4057    468    829     21       O
ATOM   2768  CG2 THR A 357      33.360   1.708  41.932  1.00 35.89           C
ANISOU 2768  CG2 THR A 357     6182   3645   3810    389    739    139       C
ATOM   2769  N   LYS A 358      35.748  -1.269  42.498  1.00 36.45           N
ANISOU 2769  N   LYS A 358     6292   3533   4026    582    799     52       N
ATOM   2770  CA  LYS A 358      37.147  -0.896  42.498  1.00 37.28           C
ANISOU 2770  CA  LYS A 358     6305   3665   4193    651    842     80       C
ATOM   2771  C   LYS A 358      37.328   0.342  41.616  1.00 41.30           C
ANISOU 2771  C   LYS A 358     6754   4280   4660    631    891    108       C
ATOM   2772  O   LYS A 358      36.657   0.489  40.588  1.00 42.73           O
ANISOU 2772  O   LYS A 358     6978   4509   4749    598    920     80       O
ATOM   2773  CB  LYS A 358      37.990  -2.049  41.975  1.00 38.94           C
ANISOU 2773  CB  LYS A 358     6537   3825   4435    739    899     18       C
ATOM   2774  CG  LYS A 358      39.497  -1.892  42.199  1.00 45.17           C
ANISOU 2774  CG  LYS A 358     7224   4626   5311    821    936     48       C
ATOM   2775  CD  LYS A 358      40.266  -3.053  41.535  1.00 48.91           C
ANISOU 2775  CD  LYS A 358     7718   5051   5813    915   1002    -28       C
ATOM   2776  CE  LYS A 358      41.752  -2.739  41.411  1.00 59.13           C
ANISOU 2776  CE  LYS A 358     8900   6390   7178    995   1061     -5       C
ATOM   2777  NZ  LYS A 358      42.363  -2.476  42.757  1.00 56.03           N
ANISOU 2777  NZ  LYS A 358     8431   5970   6886   1010    994     73       N
ATOM   2778  N   VAL A 359      38.228   1.237  42.021  1.00 38.69           N
ANISOU 2778  N   VAL A 359     6319   3984   4396    648    897    168       N
ATOM   2779  CA  VAL A 359      38.462   2.508  41.333  1.00 36.47           C
ANISOU 2779  CA  VAL A 359     5966   3791   4100    623    938    216       C
ATOM   2780  C   VAL A 359      39.743   2.360  40.521  1.00 43.33           C
ANISOU 2780  C   VAL A 359     6775   4699   4989    696   1031    209       C
ATOM   2781  O   VAL A 359      40.836   2.252  41.094  1.00 43.89           O
ANISOU 2781  O   VAL A 359     6773   4749   5153    749   1036    225       O
ATOM   2782  CB  VAL A 359      38.556   3.681  42.327  1.00 41.33           C
ANISOU 2782  CB  VAL A 359     6498   4415   4790    583    879    282       C
ATOM   2783  CG1 VAL A 359      38.567   5.036  41.592  1.00 37.61           C
ANISOU 2783  CG1 VAL A 359     5962   4016   4313    543    913    340       C
ATOM   2784  CG2 VAL A 359      37.414   3.645  43.309  1.00 35.38           C
ANISOU 2784  CG2 VAL A 359     5799   3623   4022    527    791    277       C
ATOM   2785  N   ARG A 360      39.608   2.359  39.183  1.00 43.95           N
ANISOU 2785  N   ARG A 360     6880   4845   4975    699   1104    186       N
ATOM   2786  CA  ARG A 360      40.728   2.016  38.297  1.00 46.85           C
ANISOU 2786  CA  ARG A 360     7204   5259   5337    774   1206    162       C
ATOM   2787  C   ARG A 360      41.789   3.101  38.299  1.00 44.72           C
ANISOU 2787  C   ARG A 360     6802   5048   5143    781   1247    247       C
ATOM   2788  O   ARG A 360      42.992   2.812  38.329  1.00 49.53           O
ANISOU 2788  O   ARG A 360     7337   5659   5821    851   1297    243       O
ATOM   2789  CB  ARG A 360      40.229   1.778  36.863  1.00 50.41           C
ANISOU 2789  CB  ARG A 360     7719   5786   5648    770   1272    112       C
ATOM   2790  CG  ARG A 360      41.084   0.800  36.041  1.00 56.14           C
ANISOU 2790  CG  ARG A 360     8449   6532   6347    861   1366     28       C
ATOM   2791  CD  ARG A 360      40.749   0.806  34.531  1.00 59.70           C
ANISOU 2791  CD  ARG A 360     8941   7098   6643    857   1442    -13       C
ATOM   2792  NE  ARG A 360      39.332   0.578  34.265  1.00 61.07           N
ANISOU 2792  NE  ARG A 360     9223   7264   6715    793   1383    -57       N
ATOM   2793  CZ  ARG A 360      38.790   0.503  33.056  1.00 63.75           C
ANISOU 2793  CZ  ARG A 360     9616   7699   6908    779   1421   -103       C
ATOM   2794  NH1 ARG A 360      39.526   0.615  31.963  1.00 62.38           N
ANISOU 2794  NH1 ARG A 360     9403   7643   6657    826   1527   -112       N
ATOM   2795  NH2 ARG A 360      37.473   0.318  32.943  1.00 62.55           N
ANISOU 2795  NH2 ARG A 360     9553   7534   6679    715   1352   -139       N
ATOM   2796  N   TYR A 361      41.357   4.346  38.259  1.00 40.18           N
ANISOU 2796  N   TYR A 361     6187   4514   4564    710   1224    325       N
ATOM   2797  CA  TYR A 361      42.225   5.511  38.321  1.00 42.68           C
ANISOU 2797  CA  TYR A 361     6376   4871   4968    698   1251    415       C
ATOM   2798  C   TYR A 361      41.376   6.654  38.873  1.00 38.63           C
ANISOU 2798  C   TYR A 361     5852   4341   4483    613   1171    475       C
ATOM   2799  O   TYR A 361      40.149   6.566  38.899  1.00 33.77           O
ANISOU 2799  O   TYR A 361     5325   3711   3796    569   1120    453       O
ATOM   2800  CB  TYR A 361      42.800   5.840  36.934  1.00 44.38           C
ANISOU 2800  CB  TYR A 361     6546   5194   5122    717   1367    451       C
ATOM   2801  CG  TYR A 361      41.780   5.777  35.792  1.00 44.71           C
ANISOU 2801  CG  TYR A 361     6679   5303   5004    687   1395    437       C
ATOM   2802  CD1 TYR A 361      40.664   6.623  35.771  1.00 41.47           C
ANISOU 2802  CD1 TYR A 361     6299   4900   4558    608   1336    491       C
ATOM   2803  CD2 TYR A 361      41.922   4.855  34.743  1.00 43.22           C
ANISOU 2803  CD2 TYR A 361     6545   5175   4702    741   1476    362       C
ATOM   2804  CE1 TYR A 361      39.708   6.569  34.729  1.00 42.28           C
ANISOU 2804  CE1 TYR A 361     6481   5073   4512    580   1352    482       C
ATOM   2805  CE2 TYR A 361      40.978   4.806  33.689  1.00 49.12           C
ANISOU 2805  CE2 TYR A 361     7373   5998   5292    711   1494    343       C
ATOM   2806  CZ  TYR A 361      39.879   5.668  33.692  1.00 46.60           C
ANISOU 2806  CZ  TYR A 361     7080   5688   4937    630   1429    409       C
ATOM   2807  OH  TYR A 361      38.949   5.629  32.670  1.00 47.33           O
ANISOU 2807  OH  TYR A 361     7246   5862   4875    602   1437    395       O
ATOM   2808  N   GLY A 362      42.041   7.731  39.296  1.00 39.85           N
ANISOU 2808  N   GLY A 362     5892   4497   4751    591   1162    547       N
ATOM   2809  CA  GLY A 362      41.396   8.922  39.837  1.00 38.49           C
ANISOU 2809  CA  GLY A 362     5691   4302   4633    516   1092    599       C
ATOM   2810  C   GLY A 362      40.144   9.384  39.101  1.00 36.72           C
ANISOU 2810  C   GLY A 362     5533   4108   4311    462   1085    626       C
ATOM   2811  O   GLY A 362      40.165   9.601  37.898  1.00 35.40           O
ANISOU 2811  O   GLY A 362     5365   4013   4071    460   1158    671       O
ATOM   2812  N   GLY A 363      39.027   9.470  39.804  1.00 37.94           N
ANISOU 2812  N   GLY A 363     5746   4216   4454    420    999    599       N
ATOM   2813  CA  GLY A 363      37.787   9.876  39.193  1.00 37.54           C
ANISOU 2813  CA  GLY A 363     5754   4192   4320    371    982    622       C
ATOM   2814  C   GLY A 363      36.915   8.752  38.681  1.00 37.18           C
ANISOU 2814  C   GLY A 363     5829   4163   4134    380    984    552       C
ATOM   2815  O   GLY A 363      35.750   8.996  38.379  1.00 33.74           O
ANISOU 2815  O   GLY A 363     5445   3742   3633    336    949    559       O
ATOM   2816  N   TYR A 364      37.415   7.516  38.623  1.00 35.57           N
ANISOU 2816  N   TYR A 364     5669   3950   3896    435   1017    481       N
ATOM   2817  CA  TYR A 364      36.647   6.441  37.989  1.00 39.12           C
ANISOU 2817  CA  TYR A 364     6231   4414   4220    443   1025    408       C
ATOM   2818  C   TYR A 364      35.280   6.224  38.636  1.00 40.72           C
ANISOU 2818  C   TYR A 364     6508   4568   4396    391    937    373       C
ATOM   2819  O   TYR A 364      34.353   5.763  37.953  1.00 38.92           O
ANISOU 2819  O   TYR A 364     6358   4366   4062    369    932    335       O
ATOM   2820  CB  TYR A 364      37.460   5.157  38.026  1.00 41.47           C
ANISOU 2820  CB  TYR A 364     6556   4682   4520    514   1066    331       C
ATOM   2821  CG  TYR A 364      36.844   3.967  37.337  1.00 50.00           C
ANISOU 2821  CG  TYR A 364     7745   5764   5490    529   1081    239       C
ATOM   2822  CD1 TYR A 364      37.006   3.761  35.960  1.00 52.33           C
ANISOU 2822  CD1 TYR A 364     8060   6147   5676    553   1161    214       C
ATOM   2823  CD2 TYR A 364      36.166   2.990  38.081  1.00 49.41           C
ANISOU 2823  CD2 TYR A 364     7750   5602   5422    521   1018    172       C
ATOM   2824  CE1 TYR A 364      36.462   2.630  35.339  1.00 55.02           C
ANISOU 2824  CE1 TYR A 364     8501   6486   5919    567   1170    109       C
ATOM   2825  CE2 TYR A 364      35.631   1.869  37.474  1.00 51.77           C
ANISOU 2825  CE2 TYR A 364     8145   5887   5638    530   1027     79       C
ATOM   2826  CZ  TYR A 364      35.774   1.691  36.103  1.00 55.73           C
ANISOU 2826  CZ  TYR A 364     8668   6473   6035    554   1100     40       C
ATOM   2827  OH  TYR A 364      35.230   0.562  35.511  1.00 61.42           O
ANISOU 2827  OH  TYR A 364     9483   7176   6677    561   1103    -70       O
ATOM   2828  N   ALA A 365      35.135   6.534  39.940  1.00 34.09           N
ANISOU 2828  N   ALA A 365     5640   3666   3646    370    867    381       N
ATOM   2829  CA  ALA A 365      33.840   6.368  40.601  1.00 35.09           C
ANISOU 2829  CA  ALA A 365     5826   3758   3748    321    790    353       C
ATOM   2830  C   ALA A 365      32.750   7.192  39.926  1.00 33.15           C
ANISOU 2830  C   ALA A 365     5589   3561   3445    265    773    390       C
ATOM   2831  O   ALA A 365      31.614   6.727  39.777  1.00 34.99           O
ANISOU 2831  O   ALA A 365     5894   3795   3605    232    738    353       O
ATOM   2832  CB  ALA A 365      33.923   6.747  42.085  1.00 35.95           C
ANISOU 2832  CB  ALA A 365     5889   3816   3954    309    725    361       C
ATOM   2833  N   LYS A 366      33.060   8.430  39.536  1.00 33.55           N
ANISOU 2833  N   LYS A 366     5563   3648   3537    254    792    468       N
ATOM   2834  CA  LYS A 366      32.055   9.227  38.838  1.00 34.18           C
ANISOU 2834  CA  LYS A 366     5647   3773   3568    208    774    516       C
ATOM   2835  C   LYS A 366      31.754   8.645  37.476  1.00 35.16           C
ANISOU 2835  C   LYS A 366     5834   3971   3554    215    819    503       C
ATOM   2836  O   LYS A 366      30.597   8.693  37.038  1.00 36.37           O
ANISOU 2836  O   LYS A 366     6032   4155   3631    178    783    500       O
ATOM   2837  CB  LYS A 366      32.492  10.698  38.734  1.00 34.89           C
ANISOU 2837  CB  LYS A 366     5635   3871   3750    195    783    614       C
ATOM   2838  CG  LYS A 366      32.279  11.369  40.065  1.00 36.45           C
ANISOU 2838  CG  LYS A 366     5784   4000   4066    172    714    606       C
ATOM   2839  CD  LYS A 366      32.699  12.799  40.167  1.00 40.26           C
ANISOU 2839  CD  LYS A 366     6163   4463   4670    156    711    684       C
ATOM   2840  CE  LYS A 366      32.550  13.248  41.656  1.00 42.28           C
ANISOU 2840  CE  LYS A 366     6377   4650   5036    141    638    638       C
ATOM   2841  NZ  LYS A 366      31.107  13.240  42.079  1.00 47.12           N
ANISOU 2841  NZ  LYS A 366     7040   5256   5609    108    575    600       N
ATOM   2842  N   GLY A 367      32.769   8.061  36.819  1.00 30.35           N
ANISOU 2842  N   GLY A 367     5228   3396   2908    265    895    485       N
ATOM   2843  CA  GLY A 367      32.532   7.331  35.581  1.00 35.86           C
ANISOU 2843  CA  GLY A 367     5993   4168   3463    278    939    443       C
ATOM   2844  C   GLY A 367      31.525   6.206  35.756  1.00 35.92           C
ANISOU 2844  C   GLY A 367     6101   4141   3406    260    889    341       C
ATOM   2845  O   GLY A 367      30.641   6.017  34.917  1.00 37.03           O
ANISOU 2845  O   GLY A 367     6296   4341   3435    233    876    319       O
ATOM   2846  N   VAL A 368      31.618   5.470  36.868  1.00 38.30           N
ANISOU 2846  N   VAL A 368     6424   4347   3779    270    856    284       N
ATOM   2847  CA  VAL A 368      30.677   4.376  37.126  1.00 34.89           C
ANISOU 2847  CA  VAL A 368     6082   3868   3305    246    808    197       C
ATOM   2848  C   VAL A 368      29.272   4.933  37.322  1.00 37.85           C
ANISOU 2848  C   VAL A 368     6469   4255   3660    176    735    222       C
ATOM   2849  O   VAL A 368      28.285   4.393  36.798  1.00 35.94           O
ANISOU 2849  O   VAL A 368     6290   4033   3332    142    708    171       O
ATOM   2850  CB  VAL A 368      31.155   3.554  38.339  1.00 38.95           C
ANISOU 2850  CB  VAL A 368     6608   4280   3912    272    789    158       C
ATOM   2851  CG1 VAL A 368      30.060   2.631  38.865  1.00 34.86           C
ANISOU 2851  CG1 VAL A 368     6167   3699   3378    231    728     97       C
ATOM   2852  CG2 VAL A 368      32.413   2.764  37.959  1.00 41.32           C
ANISOU 2852  CG2 VAL A 368     6910   4568   4222    348    860    115       C
ATOM   2853  N   ALA A 369      29.165   6.043  38.054  1.00 35.38           N
ANISOU 2853  N   ALA A 369     6086   3929   3426    154    702    294       N
ATOM   2854  CA  ALA A 369      27.882   6.708  38.195  1.00 33.67           C
ANISOU 2854  CA  ALA A 369     5864   3729   3200     97    639    322       C
ATOM   2855  C   ALA A 369      27.332   7.166  36.846  1.00 33.46           C
ANISOU 2855  C   ALA A 369     5845   3796   3073     80    649    357       C
ATOM   2856  O   ALA A 369      26.131   7.063  36.614  1.00 33.29           O
ANISOU 2856  O   ALA A 369     5856   3797   2994     36    599    338       O
ATOM   2857  CB  ALA A 369      28.007   7.892  39.146  1.00 35.90           C
ANISOU 2857  CB  ALA A 369     6063   3982   3596     88    610    384       C
ATOM   2858  N   PHE A 370      28.182   7.717  35.959  1.00 31.34           N
ANISOU 2858  N   PHE A 370     5538   3589   2781    111    710    417       N
ATOM   2859  CA  PHE A 370      27.687   8.159  34.653  1.00 33.77           C
ANISOU 2859  CA  PHE A 370     5851   4002   2979     97    719    464       C
ATOM   2860  C   PHE A 370      27.120   6.981  33.853  1.00 37.14           C
ANISOU 2860  C   PHE A 370     6369   4475   3268     91    717    366       C
ATOM   2861  O   PHE A 370      26.144   7.142  33.111  1.00 32.87           O
ANISOU 2861  O   PHE A 370     5850   4005   2633     58    680    375       O
ATOM   2862  CB  PHE A 370      28.784   8.831  33.814  1.00 35.33           C
ANISOU 2862  CB  PHE A 370     5992   4266   3164    133    798    550       C
ATOM   2863  CG  PHE A 370      29.317  10.136  34.371  1.00 37.58           C
ANISOU 2863  CG  PHE A 370     6179   4513   3588    130    800    657       C
ATOM   2864  CD1 PHE A 370      28.538  10.969  35.146  1.00 42.07           C
ANISOU 2864  CD1 PHE A 370     6711   5026   4249     94    728    694       C
ATOM   2865  CD2 PHE A 370      30.633  10.504  34.124  1.00 36.91           C
ANISOU 2865  CD2 PHE A 370     6033   4444   3548    166    875    713       C
ATOM   2866  CE1 PHE A 370      29.066  12.158  35.650  1.00 41.92           C
ANISOU 2866  CE1 PHE A 370     6600   4961   4368     92    729    777       C
ATOM   2867  CE2 PHE A 370      31.168  11.683  34.604  1.00 37.46           C
ANISOU 2867  CE2 PHE A 370     6007   4470   3756    158    875    806       C
ATOM   2868  CZ  PHE A 370      30.391  12.514  35.361  1.00 42.07           C
ANISOU 2868  CZ  PHE A 370     6559   4991   4434    122    800    835       C
ATOM   2869  N   ARG A 371      27.758   5.807  33.939  1.00 32.96           N
ANISOU 2869  N   ARG A 371     5889   3907   2726    125    755    270       N
ATOM   2870  CA  ARG A 371      27.216   4.627  33.263  1.00 37.56           C
ANISOU 2870  CA  ARG A 371     6559   4513   3198    118    747    157       C
ATOM   2871  C   ARG A 371      25.822   4.290  33.777  1.00 34.86           C
ANISOU 2871  C   ARG A 371     6256   4128   2861     54    658    116       C
ATOM   2872  O   ARG A 371      24.908   4.003  33.001  1.00 38.53           O
ANISOU 2872  O   ARG A 371     6762   4654   3222     20    624     74       O
ATOM   2873  CB  ARG A 371      28.145   3.418  33.449  1.00 36.94           C
ANISOU 2873  CB  ARG A 371     6522   4371   3143    170    798     59       C
ATOM   2874  CG  ARG A 371      27.792   2.204  32.540  1.00 38.66           C
ANISOU 2874  CG  ARG A 371     6827   4616   3246    173    804    -72       C
ATOM   2875  CD  ARG A 371      27.970   2.511  31.058  1.00 43.30           C
ANISOU 2875  CD  ARG A 371     7415   5355   3683    192    855    -67       C
ATOM   2876  NE  ARG A 371      27.170   1.625  30.215  1.00 56.52           N
ANISOU 2876  NE  ARG A 371     9167   7074   5233    169    826   -186       N
ATOM   2877  CZ  ARG A 371      25.924   1.868  29.815  1.00 55.43           C
ANISOU 2877  CZ  ARG A 371     9048   6996   5018    107    754   -181       C
ATOM   2878  NH1 ARG A 371      25.271   2.962  30.186  1.00 48.39           N
ANISOU 2878  NH1 ARG A 371     8103   6120   4162     65    703    -62       N
ATOM   2879  NH2 ARG A 371      25.320   0.998  29.008  1.00 57.98           N
ANISOU 2879  NH2 ARG A 371     9439   7363   5227     88    730   -305       N
ATOM   2880  N   LEU A 372      25.644   4.297  35.090  1.00 35.31           N
ANISOU 2880  N   LEU A 372     6296   4086   3033     37    621    125       N
ATOM   2881  CA  LEU A 372      24.339   3.969  35.643  1.00 36.90           C
ANISOU 2881  CA  LEU A 372     6526   4251   3245    -25    545     91       C
ATOM   2882  C   LEU A 372      23.286   4.969  35.186  1.00 38.90           C
ANISOU 2882  C   LEU A 372     6743   4582   3455    -67    496    155       C
ATOM   2883  O   LEU A 372      22.167   4.585  34.788  1.00 35.54           O
ANISOU 2883  O   LEU A 372     6351   4187   2964   -115    445    112       O
ATOM   2884  CB  LEU A 372      24.406   3.926  37.162  1.00 36.15           C
ANISOU 2884  CB  LEU A 372     6408   4056   3272    -32    522    104       C
ATOM   2885  CG  LEU A 372      23.021   3.543  37.693  1.00 34.22           C
ANISOU 2885  CG  LEU A 372     6189   3784   3029    -99    452     72       C
ATOM   2886  CD1 LEU A 372      22.985   2.102  38.148  1.00 34.98           C
ANISOU 2886  CD1 LEU A 372     6354   3795   3144   -109    448    -11       C
ATOM   2887  CD2 LEU A 372      22.589   4.510  38.757  1.00 31.00           C
ANISOU 2887  CD2 LEU A 372     5714   3362   2702   -120    416    138       C
ATOM   2888  N   LEU A 373      23.634   6.267  35.228  1.00 34.79           N
ANISOU 2888  N   LEU A 373     6147   4090   2981    -51    508    261       N
ATOM   2889  CA  LEU A 373      22.739   7.311  34.748  1.00 36.26           C
ANISOU 2889  CA  LEU A 373     6290   4345   3142    -81    464    337       C
ATOM   2890  C   LEU A 373      22.520   7.268  33.241  1.00 37.14           C
ANISOU 2890  C   LEU A 373     6429   4576   3108    -80    473    345       C
ATOM   2891  O   LEU A 373      21.766   8.099  32.719  1.00 35.63           O
ANISOU 2891  O   LEU A 373     6203   4453   2883   -101    433    418       O
ATOM   2892  CB  LEU A 373      23.271   8.684  35.153  1.00 37.05           C
ANISOU 2892  CB  LEU A 373     6303   4430   3345    -60    478    447       C
ATOM   2893  CG  LEU A 373      23.217   8.886  36.665  1.00 34.64           C
ANISOU 2893  CG  LEU A 373     5963   4026   3172    -69    451    435       C
ATOM   2894  CD1 LEU A 373      23.875  10.208  37.054  1.00 40.07           C
ANISOU 2894  CD1 LEU A 373     6564   4690   3973    -47    465    525       C
ATOM   2895  CD2 LEU A 373      21.795   8.814  37.152  1.00 36.06           C
ANISOU 2895  CD2 LEU A 373     6148   4197   3356   -118    379    406       C
ATOM   2896  N   SER A 374      23.150   6.343  32.518  1.00 37.12           N
ANISOU 2896  N   SER A 374     6484   4607   3014    -53    523    272       N
ATOM   2897  CA  SER A 374      22.864   6.191  31.098  1.00 38.28           C
ANISOU 2897  CA  SER A 374     6662   4882   3001    -54    527    258       C
ATOM   2898  C   SER A 374      22.354   4.793  30.746  1.00 39.03           C
ANISOU 2898  C   SER A 374     6844   4976   3011    -76    504    108       C
ATOM   2899  O   SER A 374      22.388   4.419  29.571  1.00 38.36           O
ANISOU 2899  O   SER A 374     6797   4996   2784    -66    522     61       O
ATOM   2900  CB  SER A 374      24.094   6.527  30.253  1.00 37.09           C
ANISOU 2900  CB  SER A 374     6492   4809   2792      1    617    310       C
ATOM   2901  OG  SER A 374      25.211   5.763  30.673  1.00 37.99           O
ANISOU 2901  OG  SER A 374     6626   4852   2955     45    683    241       O
ATOM   2902  N   THR A 375      21.906   4.007  31.729  1.00 39.61           N
ANISOU 2902  N   THR A 375     6948   4936   3168   -107    467     32       N
ATOM   2903  CA  THR A 375      21.211   2.748  31.447  1.00 41.11           C
ANISOU 2903  CA  THR A 375     7212   5110   3300   -143    429   -103       C
ATOM   2904  C   THR A 375      19.713   2.999  31.203  1.00 44.69           C
ANISOU 2904  C   THR A 375     7655   5618   3708   -212    338    -96       C
ATOM   2905  O   THR A 375      19.178   4.056  31.562  1.00 41.39           O
ANISOU 2905  O   THR A 375     7173   5219   3336   -229    302      9       O
ATOM   2906  CB  THR A 375      21.414   1.750  32.597  1.00 41.97           C
ANISOU 2906  CB  THR A 375     7355   5067   3525   -149    431   -174       C
ATOM   2907  OG1 THR A 375      20.842   2.262  33.809  1.00 40.71           O
ANISOU 2907  OG1 THR A 375     7150   4842   3477   -184    388   -107       O
ATOM   2908  CG2 THR A 375      22.900   1.441  32.815  1.00 35.00           C
ANISOU 2908  CG2 THR A 375     6478   4132   2690    -75    515   -184       C
ATOM   2909  N   PRO A 376      19.018   2.061  30.542  1.00 44.93           N
ANISOU 2909  N   PRO A 376     7742   5679   3651   -250    297   -211       N
ATOM   2910  CA  PRO A 376      17.576   2.268  30.287  1.00 44.29           C
ANISOU 2910  CA  PRO A 376     7643   5657   3528   -318    205   -207       C
ATOM   2911  C   PRO A 376      16.740   2.558  31.533  1.00 42.82           C
ANISOU 2911  C   PRO A 376     7412   5385   3475   -365    155   -160       C
ATOM   2912  O   PRO A 376      15.817   3.383  31.478  1.00 47.29           O
ANISOU 2912  O   PRO A 376     7921   6010   4036   -394     97    -88       O
ATOM   2913  CB  PRO A 376      17.155   0.945  29.617  1.00 49.90           C
ANISOU 2913  CB  PRO A 376     8429   6373   4157   -352    175   -369       C
ATOM   2914  CG  PRO A 376      18.380   0.467  28.939  1.00 45.32           C
ANISOU 2914  CG  PRO A 376     7896   5815   3507   -286    256   -432       C
ATOM   2915  CD  PRO A 376      19.548   0.895  29.806  1.00 42.97           C
ANISOU 2915  CD  PRO A 376     7570   5435   3323   -227    333   -348       C
ATOM   2916  N   HIS A 377      17.019   1.900  32.653  1.00 42.02           N
ANISOU 2916  N   HIS A 377     7330   5150   3486   -371    175   -195       N
ATOM   2917  CA  HIS A 377      16.296   2.183  33.893  1.00 42.59           C
ANISOU 2917  CA  HIS A 377     7355   5153   3673   -412    139   -149       C
ATOM   2918  C   HIS A 377      16.948   3.310  34.695  1.00 41.21           C
ANISOU 2918  C   HIS A 377     7117   4956   3584   -365    175    -37       C
ATOM   2919  O   HIS A 377      16.251   4.190  35.223  1.00 39.23           O
ANISOU 2919  O   HIS A 377     6801   4719   3386   -385    139     32       O
ATOM   2920  CB  HIS A 377      16.211   0.916  34.752  1.00 44.81           C
ANISOU 2920  CB  HIS A 377     7686   5310   4031   -446    138   -230       C
ATOM   2921  CG  HIS A 377      15.400   1.079  35.999  1.00 41.61           C
ANISOU 2921  CG  HIS A 377     7235   4850   3725   -494    105   -188       C
ATOM   2922  ND1 HIS A 377      14.032   0.902  36.027  1.00 43.30           N
ANISOU 2922  ND1 HIS A 377     7428   5087   3938   -570     38   -208       N
ATOM   2923  CD2 HIS A 377      15.759   1.419  37.261  1.00 45.11           C
ANISOU 2923  CD2 HIS A 377     7644   5229   4266   -476    130   -128       C
ATOM   2924  CE1 HIS A 377      13.584   1.111  37.254  1.00 44.84           C
ANISOU 2924  CE1 HIS A 377     7578   5234   4224   -596     31   -162       C
ATOM   2925  NE2 HIS A 377      14.610   1.433  38.022  1.00 46.10           N
ANISOU 2925  NE2 HIS A 377     7732   5344   4440   -540     85   -114       N
ATOM   2926  N   GLY A 378      18.281   3.282  34.809  1.00 40.76           N
ANISOU 2926  N   GLY A 378     7075   4864   3550   -304    245    -27       N
ATOM   2927  CA  GLY A 378      18.969   4.261  35.639  1.00 39.33           C
ANISOU 2927  CA  GLY A 378     6833   4650   3461   -264    277     64       C
ATOM   2928  C   GLY A 378      18.820   5.682  35.125  1.00 38.46           C
ANISOU 2928  C   GLY A 378     6653   4623   3336   -250    266    168       C
ATOM   2929  O   GLY A 378      18.722   6.633  35.906  1.00 37.94           O
ANISOU 2929  O   GLY A 378     6522   4531   3362   -245    255    237       O
ATOM   2930  N   MET A 379      18.796   5.847  33.810  1.00 39.20           N
ANISOU 2930  N   MET A 379     6760   4818   3318   -241    268    181       N
ATOM   2931  CA  MET A 379      18.736   7.193  33.251  1.00 38.06           C
ANISOU 2931  CA  MET A 379     6549   4749   3161   -223    261    299       C
ATOM   2932  C   MET A 379      17.498   7.945  33.719  1.00 44.43           C
ANISOU 2932  C   MET A 379     7297   5558   4027   -261    189    347       C
ATOM   2933  O   MET A 379      17.646   9.078  34.219  1.00 42.83           O
ANISOU 2933  O   MET A 379     7024   5328   3920   -240    191    435       O
ATOM   2934  CB  MET A 379      18.853   7.108  31.733  1.00 39.48           C
ANISOU 2934  CB  MET A 379     6760   5055   3187   -210    273    303       C
ATOM   2935  CG  MET A 379      18.920   8.403  31.034  1.00 39.08           C
ANISOU 2935  CG  MET A 379     6647   5088   3113   -189    274    440       C
ATOM   2936  SD  MET A 379      19.459   8.190  29.311  1.00 47.92           S
ANISOU 2936  SD  MET A 379     7807   6366   4035   -160    317    448       S
ATOM   2937  CE  MET A 379      18.634   6.676  28.798  1.00 48.72           C
ANISOU 2937  CE  MET A 379     7998   6506   4009   -203    269    273       C
ATOM   2938  N   PRO A 380      16.272   7.383  33.651  1.00 40.93           N
ANISOU 2938  N   PRO A 380     6870   5136   3545   -315    124    288       N
ATOM   2939  CA  PRO A 380      15.113   8.142  34.146  1.00 39.88           C
ANISOU 2939  CA  PRO A 380     6667   5005   3479   -344     60    334       C
ATOM   2940  C   PRO A 380      14.827   7.978  35.639  1.00 39.99           C
ANISOU 2940  C   PRO A 380     6659   4921   3613   -364     57    301       C
ATOM   2941  O   PRO A 380      14.252   8.885  36.234  1.00 39.45           O
ANISOU 2941  O   PRO A 380     6518   4843   3627   -365     29    352       O
ATOM   2942  CB  PRO A 380      13.964   7.620  33.274  1.00 41.02           C
ANISOU 2942  CB  PRO A 380     6832   5236   3518   -393     -7    289       C
ATOM   2943  CG  PRO A 380      14.369   6.280  32.842  1.00 42.73           C
ANISOU 2943  CG  PRO A 380     7138   5447   3650   -406     16    178       C
ATOM   2944  CD  PRO A 380      15.862   6.179  32.906  1.00 43.16           C
ANISOU 2944  CD  PRO A 380     7225   5459   3716   -349    102    183       C
ATOM   2945  N   TYR A 381      15.246   6.880  36.278  1.00 37.40           N
ANISOU 2945  N   TYR A 381     6389   4523   3299   -376     87    221       N
ATOM   2946  CA  TYR A 381      14.834   6.638  37.664  1.00 37.25           C
ANISOU 2946  CA  TYR A 381     6350   4431   3373   -404     79    196       C
ATOM   2947  C   TYR A 381      15.852   7.123  38.685  1.00 38.03           C
ANISOU 2947  C   TYR A 381     6423   4463   3562   -358    127    227       C
ATOM   2948  O   TYR A 381      15.494   7.820  39.639  1.00 34.82           O
ANISOU 2948  O   TYR A 381     5955   4037   3237   -359    114    252       O
ATOM   2949  CB  TYR A 381      14.575   5.147  37.907  1.00 35.97           C
ANISOU 2949  CB  TYR A 381     6257   4222   3187   -451     75    104       C
ATOM   2950  CG  TYR A 381      13.200   4.637  37.512  1.00 41.73           C
ANISOU 2950  CG  TYR A 381     6988   4993   3875   -521     12     60       C
ATOM   2951  CD1 TYR A 381      12.943   4.204  36.217  1.00 46.99           C
ANISOU 2951  CD1 TYR A 381     7693   5723   4437   -538    -16     18       C
ATOM   2952  CD2 TYR A 381      12.171   4.532  38.451  1.00 45.34           C
ANISOU 2952  CD2 TYR A 381     7403   5430   4393   -573    -19     55       C
ATOM   2953  CE1 TYR A 381      11.689   3.711  35.857  1.00 50.74           C
ANISOU 2953  CE1 TYR A 381     8164   6236   4877   -607    -82    -30       C
ATOM   2954  CE2 TYR A 381      10.920   4.038  38.097  1.00 45.16           C
ANISOU 2954  CE2 TYR A 381     7372   5445   4342   -643    -78     15       C
ATOM   2955  CZ  TYR A 381      10.689   3.634  36.809  1.00 47.59           C
ANISOU 2955  CZ  TYR A 381     7719   5810   4555   -660   -112    -28       C
ATOM   2956  OH  TYR A 381       9.456   3.149  36.458  1.00 59.48           O
ANISOU 2956  OH  TYR A 381     9210   7355   6036   -733   -177    -74       O
ATOM   2957  N   SER A 382      17.117   6.753  38.509  1.00 36.13           N
ANISOU 2957  N   SER A 382     6226   4193   3310   -317    180    218       N
ATOM   2958  CA  SER A 382      18.106   6.890  39.570  1.00 34.29           C
ANISOU 2958  CA  SER A 382     5978   3892   3160   -281    220    228       C
ATOM   2959  C   SER A 382      18.440   8.361  39.780  1.00 38.14           C
ANISOU 2959  C   SER A 382     6384   4388   3719   -246    224    304       C
ATOM   2960  O   SER A 382      18.995   9.015  38.891  1.00 43.23           O
ANISOU 2960  O   SER A 382     7012   5068   4345   -215    244    358       O
ATOM   2961  CB  SER A 382      19.342   6.083  39.202  1.00 36.47           C
ANISOU 2961  CB  SER A 382     6314   4139   3405   -243    274    198       C
ATOM   2962  OG  SER A 382      18.978   4.731  38.992  1.00 38.01           O
ANISOU 2962  OG  SER A 382     6582   4311   3548   -276    265    121       O
ATOM   2963  N   LYS A 383      18.054   8.898  40.929  1.00 36.08           N
ANISOU 2963  N   LYS A 383     6070   4099   3541   -253    204    307       N
ATOM   2964  CA  LYS A 383      18.275  10.301  41.255  1.00 38.09           C
ANISOU 2964  CA  LYS A 383     6242   4346   3884   -224    201    361       C
ATOM   2965  C   LYS A 383      19.472  10.493  42.169  1.00 36.26           C
ANISOU 2965  C   LYS A 383     5992   4060   3725   -187    235    356       C
ATOM   2966  O   LYS A 383      20.252  11.428  41.980  1.00 36.72           O
ANISOU 2966  O   LYS A 383     6004   4105   3842   -153    252    405       O
ATOM   2967  CB  LYS A 383      17.030  10.899  41.933  1.00 38.25           C
ANISOU 2967  CB  LYS A 383     6202   4377   3954   -249    154    355       C
ATOM   2968  CG  LYS A 383      17.109  12.431  42.198  1.00 35.11           C
ANISOU 2968  CG  LYS A 383     5714   3962   3664   -217    143    402       C
ATOM   2969  CD  LYS A 383      15.791  12.920  42.791  1.00 36.78           C
ANISOU 2969  CD  LYS A 383     5865   4189   3919   -238    100    383       C
ATOM   2970  CE  LYS A 383      15.549  12.208  44.115  1.00 37.26           C
ANISOU 2970  CE  LYS A 383     5939   4240   3979   -260    106    310       C
ATOM   2971  NZ  LYS A 383      14.192  12.413  44.599  1.00 34.81           N
ANISOU 2971  NZ  LYS A 383     5578   3963   3686   -287     72    284       N
ATOM   2972  N   ILE A 384      19.613   9.630  43.163  1.00 32.05           N
ANISOU 2972  N   ILE A 384     5490   3495   3190   -196    240    304       N
ATOM   2973  CA  ILE A 384      20.691   9.690  44.135  1.00 34.78           C
ANISOU 2973  CA  ILE A 384     5820   3799   3596   -164    262    294       C
ATOM   2974  C   ILE A 384      21.542   8.453  43.905  1.00 34.66           C
ANISOU 2974  C   ILE A 384     5878   3760   3532   -149    297    274       C
ATOM   2975  O   ILE A 384      21.051   7.326  44.036  1.00 35.94           O
ANISOU 2975  O   ILE A 384     6099   3912   3643   -178    290    237       O
ATOM   2976  CB  ILE A 384      20.141   9.763  45.562  1.00 41.04           C
ANISOU 2976  CB  ILE A 384     6581   4586   4425   -180    237    258       C
ATOM   2977  CG1 ILE A 384      19.254  11.013  45.688  1.00 37.51           C
ANISOU 2977  CG1 ILE A 384     6058   4162   4034   -188    205    268       C
ATOM   2978  CG2 ILE A 384      21.261   9.785  46.575  1.00 36.71           C
ANISOU 2978  CG2 ILE A 384     6016   4008   3924   -147    251    245       C
ATOM   2979  CD1 ILE A 384      18.625  11.115  47.008  1.00 38.32           C
ANISOU 2979  CD1 ILE A 384     6125   4276   4161   -202    186    223       C
ATOM   2980  N   VAL A 385      22.798   8.657  43.501  1.00 34.43           N
ANISOU 2980  N   VAL A 385     5840   3717   3523   -105    335    298       N
ATOM   2981  CA  VAL A 385      23.713   7.570  43.152  1.00 37.04           C
ANISOU 2981  CA  VAL A 385     6231   4026   3818    -78    375    277       C
ATOM   2982  C   VAL A 385      24.971   7.752  43.986  1.00 36.30           C
ANISOU 2982  C   VAL A 385     6100   3897   3796    -35    393    285       C
ATOM   2983  O   VAL A 385      25.694   8.743  43.832  1.00 36.66           O
ANISOU 2983  O   VAL A 385     6083   3948   3899    -10    408    323       O
ATOM   2984  CB  VAL A 385      24.044   7.545  41.648  1.00 38.01           C
ANISOU 2984  CB  VAL A 385     6377   4185   3878    -62    411    296       C
ATOM   2985  CG1 VAL A 385      25.013   6.375  41.324  1.00 31.04           C
ANISOU 2985  CG1 VAL A 385     5554   3277   2964    -26    457    258       C
ATOM   2986  CG2 VAL A 385      22.763   7.434  40.814  1.00 32.63           C
ANISOU 2986  CG2 VAL A 385     5726   3552   3120   -106    380    287       C
ATOM   2987  N   ILE A 386      25.231   6.801  44.866  1.00 34.45           N
ANISOU 2987  N   ILE A 386     5900   3627   3564    -28    389    254       N
ATOM   2988  CA  ILE A 386      26.358   6.841  45.783  1.00 31.88           C
ANISOU 2988  CA  ILE A 386     5539   3275   3299     12    394    259       C
ATOM   2989  C   ILE A 386      27.312   5.743  45.349  1.00 34.83           C
ANISOU 2989  C   ILE A 386     5962   3616   3656     53    434    248       C
ATOM   2990  O   ILE A 386      26.887   4.611  45.113  1.00 34.65           O
ANISOU 2990  O   ILE A 386     6012   3568   3585     40    437    219       O
ATOM   2991  CB  ILE A 386      25.882   6.638  47.235  1.00 31.10           C
ANISOU 2991  CB  ILE A 386     5434   3172   3213     -8    353    242       C
ATOM   2992  CG1 ILE A 386      24.826   7.707  47.612  1.00 38.05           C
ANISOU 2992  CG1 ILE A 386     6262   4087   4106    -45    318    239       C
ATOM   2993  CG2 ILE A 386      27.080   6.555  48.211  1.00 29.45           C
ANISOU 2993  CG2 ILE A 386     5191   2945   3053     36    350    247       C
ATOM   2994  CD1 ILE A 386      24.214   7.539  49.013  1.00 37.58           C
ANISOU 2994  CD1 ILE A 386     6193   4045   4041    -68    284    217       C
ATOM   2995  N   VAL A 387      28.584   6.065  45.217  1.00 34.54           N
ANISOU 2995  N   VAL A 387     5882   3575   3667    102    465    267       N
ATOM   2996  CA  VAL A 387      29.582   5.079  44.825  1.00 32.97           C
ANISOU 2996  CA  VAL A 387     5716   3346   3464    152    508    253       C
ATOM   2997  C   VAL A 387      30.521   4.886  46.000  1.00 36.60           C
ANISOU 2997  C   VAL A 387     6140   3777   3989    190    492    261       C
ATOM   2998  O   VAL A 387      30.976   5.875  46.594  1.00 33.34           O
ANISOU 2998  O   VAL A 387     5649   3383   3635    195    474    282       O
ATOM   2999  CB  VAL A 387      30.354   5.507  43.561  1.00 33.14           C
ANISOU 2999  CB  VAL A 387     5713   3401   3478    183    568    271       C
ATOM   3000  CG1 VAL A 387      31.270   4.383  43.125  1.00 32.43           C
ANISOU 3000  CG1 VAL A 387     5661   3283   3378    239    616    241       C
ATOM   3001  CG2 VAL A 387      29.380   5.849  42.430  1.00 33.61           C
ANISOU 3001  CG2 VAL A 387     5800   3508   3463    145    574    275       C
ATOM   3002  N   VAL A 388      30.786   3.616  46.353  1.00 33.32           N
ANISOU 3002  N   VAL A 388     5779   3315   3568    215    492    243       N
ATOM   3003  CA  VAL A 388      31.632   3.270  47.490  1.00 34.23           C
ANISOU 3003  CA  VAL A 388     5865   3405   3736    254    469    259       C
ATOM   3004  C   VAL A 388      32.706   2.281  47.023  1.00 34.77           C
ANISOU 3004  C   VAL A 388     5955   3428   3829    322    512    249       C
ATOM   3005  O   VAL A 388      32.605   1.694  45.950  1.00 35.48           O
ANISOU 3005  O   VAL A 388     6096   3499   3884    331    555    218       O
ATOM   3006  CB  VAL A 388      30.803   2.694  48.665  1.00 28.01           C
ANISOU 3006  CB  VAL A 388     5114   2601   2926    220    417    265       C
ATOM   3007  CG1 VAL A 388      29.804   3.736  49.149  1.00 29.23           C
ANISOU 3007  CG1 VAL A 388     5235   2810   3062    162    381    265       C
ATOM   3008  CG2 VAL A 388      30.070   1.376  48.243  1.00 31.38           C
ANISOU 3008  CG2 VAL A 388     5639   2973   3312    199    426    245       C
ATOM   3009  N   ASP A 389      33.736   2.098  47.858  1.00 37.78           N
ANISOU 3009  N   ASP A 389     6291   3794   4269    372    497    271       N
ATOM   3010  CA  ASP A 389      34.873   1.214  47.564  1.00 36.69           C
ANISOU 3010  CA  ASP A 389     6155   3612   4173    447    534    266       C
ATOM   3011  C   ASP A 389      34.440  -0.253  47.496  1.00 41.87           C
ANISOU 3011  C   ASP A 389     6906   4189   4811    456    534    244       C
ATOM   3012  O   ASP A 389      33.371  -0.643  47.992  1.00 37.96           O
ANISOU 3012  O   ASP A 389     6467   3674   4282    402    496    249       O
ATOM   3013  CB  ASP A 389      35.973   1.346  48.635  1.00 37.96           C
ANISOU 3013  CB  ASP A 389     6240   3778   4404    496    500    301       C
ATOM   3014  CG  ASP A 389      36.800   2.648  48.490  1.00 44.19           C
ANISOU 3014  CG  ASP A 389     6922   4625   5242    504    513    313       C
ATOM   3015  OD1 ASP A 389      37.191   2.959  47.344  1.00 46.39           O
ANISOU 3015  OD1 ASP A 389     7182   4920   5525    518    577    303       O
ATOM   3016  OD2 ASP A 389      37.066   3.357  49.504  1.00 41.69           O
ANISOU 3016  OD2 ASP A 389     6538   4342   4961    495    460    331       O
ATOM   3017  N   GLU A 390      35.316  -1.077  46.890  1.00 37.70           N
ANISOU 3017  N   GLU A 390     6392   3614   4319    526    581    219       N
ATOM   3018  CA  GLU A 390      34.954  -2.446  46.539  1.00 42.30           C
ANISOU 3018  CA  GLU A 390     7066   4110   4898    537    592    180       C
ATOM   3019  C   GLU A 390      34.762  -3.308  47.771  1.00 39.94           C
ANISOU 3019  C   GLU A 390     6797   3742   4637    537    534    225       C
ATOM   3020  O   GLU A 390      34.007  -4.284  47.715  1.00 42.22           O
ANISOU 3020  O   GLU A 390     7166   3956   4918    510    523    208       O
ATOM   3021  CB  GLU A 390      36.014  -3.072  45.615  1.00 41.14           C
ANISOU 3021  CB  GLU A 390     6915   3929   4788    622    659    132       C
ATOM   3022  CG  GLU A 390      37.264  -3.556  46.362  1.00 49.02           C
ANISOU 3022  CG  GLU A 390     7861   4884   5880    708    650    168       C
ATOM   3023  CD  GLU A 390      38.459  -2.612  46.217  1.00 53.78           C
ANISOU 3023  CD  GLU A 390     8354   5562   6518    754    683    189       C
ATOM   3024  OE1 GLU A 390      38.239  -1.381  46.121  1.00 52.67           O
ANISOU 3024  OE1 GLU A 390     8165   5505   6343    704    681    208       O
ATOM   3025  OE2 GLU A 390      39.612  -3.106  46.204  1.00 65.28           O
ANISOU 3025  OE2 GLU A 390     9767   6990   8046    841    709    187       O
ATOM   3026  N   PHE A 391      35.421  -2.968  48.888  1.00 44.73           N
ANISOU 3026  N   PHE A 391     7338   4375   5282    564    493    287       N
ATOM   3027  CA  PHE A 391      35.275  -3.702  50.150  1.00 44.03           C
ANISOU 3027  CA  PHE A 391     7270   4243   5216    565    434    349       C
ATOM   3028  C   PHE A 391      34.086  -3.229  50.988  1.00 44.93           C
ANISOU 3028  C   PHE A 391     7398   4409   5265    478    385    382       C
ATOM   3029  O   PHE A 391      33.818  -3.817  52.040  1.00 45.74           O
ANISOU 3029  O   PHE A 391     7520   4490   5368    467    339    441       O
ATOM   3030  CB  PHE A 391      36.561  -3.609  50.994  1.00 42.69           C
ANISOU 3030  CB  PHE A 391     7021   4092   5108    639    407    400       C
ATOM   3031  CG  PHE A 391      36.974  -2.203  51.325  1.00 43.00           C
ANISOU 3031  CG  PHE A 391     6965   4238   5136    627    391    406       C
ATOM   3032  CD1 PHE A 391      36.491  -1.573  52.458  1.00 45.63           C
ANISOU 3032  CD1 PHE A 391     7271   4638   5428    579    329    441       C
ATOM   3033  CD2 PHE A 391      37.823  -1.503  50.492  1.00 42.66           C
ANISOU 3033  CD2 PHE A 391     6856   4228   5124    661    440    372       C
ATOM   3034  CE1 PHE A 391      36.847  -0.273  52.746  1.00 45.48           C
ANISOU 3034  CE1 PHE A 391     7164   4705   5411    567    311    431       C
ATOM   3035  CE2 PHE A 391      38.186  -0.200  50.790  1.00 40.78           C
ANISOU 3035  CE2 PHE A 391     6527   4074   4894    644    422    378       C
ATOM   3036  CZ  PHE A 391      37.687   0.408  51.903  1.00 44.44           C
ANISOU 3036  CZ  PHE A 391     6969   4591   5327    597    356    401       C
ATOM   3037  N   VAL A 392      33.356  -2.203  50.554  1.00 41.81           N
ANISOU 3037  N   VAL A 392     6989   4083   4815    418    394    349       N
ATOM   3038  CA  VAL A 392      32.186  -1.723  51.288  1.00 35.96           C
ANISOU 3038  CA  VAL A 392     6254   3394   4016    339    354    368       C
ATOM   3039  C   VAL A 392      30.975  -2.474  50.764  1.00 39.61           C
ANISOU 3039  C   VAL A 392     6801   3803   4444    280    364    346       C
ATOM   3040  O   VAL A 392      30.770  -2.542  49.556  1.00 37.39           O
ANISOU 3040  O   VAL A 392     6552   3502   4152    273    403    290       O
ATOM   3041  CB  VAL A 392      31.999  -0.216  51.112  1.00 37.12           C
ANISOU 3041  CB  VAL A 392     6335   3631   4136    309    354    344       C
ATOM   3042  CG1 VAL A 392      30.619   0.210  51.666  1.00 36.54           C
ANISOU 3042  CG1 VAL A 392     6274   3606   4003    229    322    347       C
ATOM   3043  CG2 VAL A 392      33.173   0.561  51.731  1.00 37.07           C
ANISOU 3043  CG2 VAL A 392     6237   3674   4175    358    335    361       C
ATOM   3044  N   ASP A 393      30.204  -3.088  51.662  1.00 39.14           N
ANISOU 3044  N   ASP A 393     6778   3726   4368    236    328    392       N
ATOM   3045  CA  ASP A 393      28.987  -3.788  51.274  1.00 39.58           C
ANISOU 3045  CA  ASP A 393     6905   3732   4401    167    332    375       C
ATOM   3046  C   ASP A 393      27.958  -2.708  50.969  1.00 36.65           C
ANISOU 3046  C   ASP A 393     6510   3448   3968    100    330    342       C
ATOM   3047  O   ASP A 393      27.489  -2.055  51.908  1.00 37.56           O
ANISOU 3047  O   ASP A 393     6585   3638   4050     68    302    374       O
ATOM   3048  CB  ASP A 393      28.512  -4.735  52.403  1.00 39.50           C
ANISOU 3048  CB  ASP A 393     6928   3681   4400    138    297    453       C
ATOM   3049  CG  ASP A 393      27.161  -5.435  52.090  1.00 43.93           C
ANISOU 3049  CG  ASP A 393     7553   4191   4947     52    298    441       C
ATOM   3050  OD1 ASP A 393      26.565  -5.170  51.020  1.00 38.59           O
ANISOU 3050  OD1 ASP A 393     6895   3519   4247     17    318    368       O
ATOM   3051  OD2 ASP A 393      26.703  -6.272  52.927  1.00 47.61           O
ANISOU 3051  OD2 ASP A 393     8047   4614   5427     18    276    512       O
ATOM   3052  N   PRO A 394      27.595  -2.485  49.694  1.00 32.32           N
ANISOU 3052  N   PRO A 394     5983   2899   3401     83    359    278       N
ATOM   3053  CA  PRO A 394      26.609  -1.441  49.374  1.00 37.97           C
ANISOU 3053  CA  PRO A 394     6670   3694   4064     24    353    256       C
ATOM   3054  C   PRO A 394      25.229  -1.695  49.950  1.00 35.50           C
ANISOU 3054  C   PRO A 394     6377   3393   3719    -57    324    274       C
ATOM   3055  O   PRO A 394      24.417  -0.764  49.965  1.00 34.91           O
ANISOU 3055  O   PRO A 394     6263   3391   3608   -100    313    264       O
ATOM   3056  CB  PRO A 394      26.566  -1.467  47.841  1.00 36.61           C
ANISOU 3056  CB  PRO A 394     6529   3509   3873     28    387    193       C
ATOM   3057  CG  PRO A 394      26.994  -2.881  47.481  1.00 34.58           C
ANISOU 3057  CG  PRO A 394     6341   3148   3652     57    404    168       C
ATOM   3058  CD  PRO A 394      28.030  -3.209  48.483  1.00 36.73           C
ANISOU 3058  CD  PRO A 394     6590   3387   3980    117    397    222       C
ATOM   3059  N   PHE A 395      24.940  -2.913  50.412  1.00 33.52           N
ANISOU 3059  N   PHE A 395     6178   3069   3487    -80    314    303       N
ATOM   3060  CA  PHE A 395      23.669  -3.269  51.024  1.00 34.58           C
ANISOU 3060  CA  PHE A 395     6326   3213   3599   -161    292    333       C
ATOM   3061  C   PHE A 395      23.666  -3.054  52.527  1.00 36.87           C
ANISOU 3061  C   PHE A 395     6575   3560   3872   -165    270    406       C
ATOM   3062  O   PHE A 395      22.638  -3.275  53.166  1.00 37.32           O
ANISOU 3062  O   PHE A 395     6633   3644   3904   -231    258    441       O
ATOM   3063  CB  PHE A 395      23.324  -4.731  50.707  1.00 37.48           C
ANISOU 3063  CB  PHE A 395     6770   3463   4007   -193    293    332       C
ATOM   3064  CG  PHE A 395      23.105  -4.989  49.235  1.00 36.02           C
ANISOU 3064  CG  PHE A 395     6628   3234   3823   -203    309    243       C
ATOM   3065  CD1 PHE A 395      21.880  -4.722  48.656  1.00 34.46           C
ANISOU 3065  CD1 PHE A 395     6432   3077   3585   -278    298    203       C
ATOM   3066  CD2 PHE A 395      24.119  -5.482  48.444  1.00 35.64           C
ANISOU 3066  CD2 PHE A 395     6614   3118   3810   -134    335    196       C
ATOM   3067  CE1 PHE A 395      21.682  -4.922  47.303  1.00 34.62           C
ANISOU 3067  CE1 PHE A 395     6489   3075   3590   -286    306    118       C
ATOM   3068  CE2 PHE A 395      23.927  -5.705  47.071  1.00 33.25           C
ANISOU 3068  CE2 PHE A 395     6350   2794   3491   -141    351    105       C
ATOM   3069  CZ  PHE A 395      22.706  -5.426  46.509  1.00 32.69           C
ANISOU 3069  CZ  PHE A 395     6282   2768   3369   -218    334     67       C
ATOM   3070  N   ASN A 396      24.791  -2.666  53.099  1.00 34.90           N
ANISOU 3070  N   ASN A 396     6289   3338   3635    -96    265    430       N
ATOM   3071  CA  ASN A 396      24.933  -2.452  54.528  1.00 37.85           C
ANISOU 3071  CA  ASN A 396     6621   3779   3980    -89    239    492       C
ATOM   3072  C   ASN A 396      24.965  -0.945  54.733  1.00 35.58           C
ANISOU 3072  C   ASN A 396     6257   3601   3661    -80    232    450       C
ATOM   3073  O   ASN A 396      26.010  -0.316  54.592  1.00 34.69           O
ANISOU 3073  O   ASN A 396     6105   3501   3574    -21    231    429       O
ATOM   3074  CB  ASN A 396      26.196  -3.133  55.046  1.00 42.37           C
ANISOU 3074  CB  ASN A 396     7202   4304   4594    -17    228    545       C
ATOM   3075  CG  ASN A 396      26.398  -2.925  56.527  1.00 43.62           C
ANISOU 3075  CG  ASN A 396     7317   4548   4709     -7    195    612       C
ATOM   3076  OD1 ASN A 396      25.966  -1.919  57.094  1.00 38.97           O
ANISOU 3076  OD1 ASN A 396     6674   4070   4065    -30    184    591       O
ATOM   3077  ND2 ASN A 396      27.060  -3.883  57.171  1.00 46.59           N
ANISOU 3077  ND2 ASN A 396     7715   4877   5111     31    178    691       N
ATOM   3078  N   LEU A 397      23.816  -0.369  55.087  1.00 36.12           N
ANISOU 3078  N   LEU A 397     6298   3744   3683   -140    226    438       N
ATOM   3079  CA  LEU A 397      23.696   1.084  55.042  1.00 38.20           C
ANISOU 3079  CA  LEU A 397     6491   4087   3934   -134    222    383       C
ATOM   3080  C   LEU A 397      24.529   1.765  56.111  1.00 35.41           C
ANISOU 3080  C   LEU A 397     6077   3803   3573    -88    197    387       C
ATOM   3081  O   LEU A 397      24.905   2.922  55.917  1.00 35.30           O
ANISOU 3081  O   LEU A 397     6006   3823   3583    -63    192    337       O
ATOM   3082  CB  LEU A 397      22.223   1.505  55.136  1.00 33.72           C
ANISOU 3082  CB  LEU A 397     5905   3580   3329   -203    223    363       C
ATOM   3083  CG  LEU A 397      21.370   1.112  53.929  1.00 38.35           C
ANISOU 3083  CG  LEU A 397     6535   4112   3925   -251    238    342       C
ATOM   3084  CD1 LEU A 397      19.963   1.642  54.057  1.00 39.19           C
ANISOU 3084  CD1 LEU A 397     6604   4285   4000   -313    234    322       C
ATOM   3085  CD2 LEU A 397      21.993   1.603  52.624  1.00 33.83           C
ANISOU 3085  CD2 LEU A 397     5966   3501   3387   -213    250    298       C
ATOM   3086  N   GLU A 398      24.869   1.070  57.206  1.00 37.81           N
ANISOU 3086  N   GLU A 398     6390   4128   3848    -75    179    447       N
ATOM   3087  CA  GLU A 398      25.762   1.660  58.204  1.00 42.45           C
ANISOU 3087  CA  GLU A 398     6919   4788   4422    -27    147    445       C
ATOM   3088  C   GLU A 398      27.204   1.702  57.694  1.00 37.12           C
ANISOU 3088  C   GLU A 398     6233   4056   3815     43    143    439       C
ATOM   3089  O   GLU A 398      27.969   2.596  58.066  1.00 37.51           O
ANISOU 3089  O   GLU A 398     6217   4156   3881     79    120    404       O
ATOM   3090  CB  GLU A 398      25.651   0.919  59.563  1.00 39.67           C
ANISOU 3090  CB  GLU A 398     6576   4495   4002    -34    124    522       C
ATOM   3091  CG  GLU A 398      26.376  -0.445  59.702  1.00 44.89           C
ANISOU 3091  CG  GLU A 398     7293   5076   4689     -2    117    614       C
ATOM   3092  CD  GLU A 398      25.917  -1.291  60.940  1.00 51.42           C
ANISOU 3092  CD  GLU A 398     8138   5955   5444    -30    102    715       C
ATOM   3093  OE1 GLU A 398      24.986  -0.847  61.642  1.00 52.71           O
ANISOU 3093  OE1 GLU A 398     8273   6225   5530    -78    104    707       O
ATOM   3094  OE2 GLU A 398      26.470  -2.403  61.207  1.00 52.06           O
ANISOU 3094  OE2 GLU A 398     8259   5972   5548     -3     90    806       O
ATOM   3095  N   GLN A 399      27.590   0.760  56.842  1.00 37.50           N
ANISOU 3095  N   GLN A 399     6339   4001   3908     62    167    464       N
ATOM   3096  CA  GLN A 399      28.893   0.859  56.186  1.00 38.81           C
ANISOU 3096  CA  GLN A 399     6487   4118   4142    128    176    449       C
ATOM   3097  C   GLN A 399      28.899   1.913  55.098  1.00 34.77           C
ANISOU 3097  C   GLN A 399     5944   3606   3663    125    202    383       C
ATOM   3098  O   GLN A 399      29.922   2.561  54.860  1.00 32.30           O
ANISOU 3098  O   GLN A 399     5577   3297   3398    170    203    363       O
ATOM   3099  CB  GLN A 399      29.272  -0.460  55.561  1.00 40.17           C
ANISOU 3099  CB  GLN A 399     6728   4180   4354    155    198    483       C
ATOM   3100  CG  GLN A 399      30.717  -0.757  55.604  1.00 40.84           C
ANISOU 3100  CG  GLN A 399     6789   4232   4496    235    193    503       C
ATOM   3101  CD  GLN A 399      30.909  -2.233  55.415  1.00 46.24           C
ANISOU 3101  CD  GLN A 399     7544   4810   5217    260    203    551       C
ATOM   3102  OE1 GLN A 399      30.805  -2.732  54.297  1.00 41.40           O
ANISOU 3102  OE1 GLN A 399     6978   4115   4635    261    243    515       O
ATOM   3103  NE2 GLN A 399      31.095  -2.959  56.522  1.00 51.91           N
ANISOU 3103  NE2 GLN A 399     8269   5529   5926    275    166    631       N
ATOM   3104  N   VAL A 400      27.777   2.078  54.410  1.00 33.97           N
ANISOU 3104  N   VAL A 400     5870   3498   3538     70    223    356       N
ATOM   3105  CA  VAL A 400      27.695   3.148  53.438  1.00 36.16           C
ANISOU 3105  CA  VAL A 400     6114   3786   3840     65    242    309       C
ATOM   3106  C   VAL A 400      27.803   4.505  54.133  1.00 38.09           C
ANISOU 3106  C   VAL A 400     6272   4103   4097     67    215    279       C
ATOM   3107  O   VAL A 400      28.485   5.421  53.636  1.00 36.66           O
ANISOU 3107  O   VAL A 400     6038   3920   3970     92    222    257       O
ATOM   3108  CB  VAL A 400      26.416   3.003  52.599  1.00 35.91           C
ANISOU 3108  CB  VAL A 400     6127   3740   3776      7    261    292       C
ATOM   3109  CG1 VAL A 400      26.251   4.222  51.666  1.00 32.40           C
ANISOU 3109  CG1 VAL A 400     5640   3318   3353      1    274    257       C
ATOM   3110  CG2 VAL A 400      26.529   1.702  51.756  1.00 33.49           C
ANISOU 3110  CG2 VAL A 400     5902   3350   3473     13    287    301       C
ATOM   3111  N   MET A 401      27.186   4.639  55.315  1.00 31.34           N
ANISOU 3111  N   MET A 401     5399   3313   3197     41    184    277       N
ATOM   3112  CA  MET A 401      27.301   5.889  56.060  1.00 33.60           C
ANISOU 3112  CA  MET A 401     5603   3668   3495     47    154    231       C
ATOM   3113  C   MET A 401      28.741   6.151  56.449  1.00 35.10           C
ANISOU 3113  C   MET A 401     5742   3860   3732    102    132    229       C
ATOM   3114  O   MET A 401      29.179   7.308  56.492  1.00 33.10           O
ANISOU 3114  O   MET A 401     5416   3626   3533    113    117    182       O
ATOM   3115  CB  MET A 401      26.445   5.862  57.334  1.00 38.01           C
ANISOU 3115  CB  MET A 401     6152   4312   3980     16    129    224       C
ATOM   3116  CG  MET A 401      24.955   6.143  57.163  1.00 37.71           C
ANISOU 3116  CG  MET A 401     6120   4300   3909    -40    144    201       C
ATOM   3117  SD  MET A 401      24.575   7.699  56.338  1.00 50.65           S
ANISOU 3117  SD  MET A 401     7696   5931   5619    -46    149    133       S
ATOM   3118  CE  MET A 401      25.557   8.902  57.218  1.00 33.05           C
ANISOU 3118  CE  MET A 401     5375   3744   3439     -5    111     72       C
ATOM   3119  N   TRP A 402      29.461   5.092  56.830  1.00 35.03           N
ANISOU 3119  N   TRP A 402     5766   3835   3709    135    124    280       N
ATOM   3120  CA  TRP A 402      30.872   5.234  57.162  1.00 33.98           C
ANISOU 3120  CA  TRP A 402     5581   3705   3625    192    100    284       C
ATOM   3121  C   TRP A 402      31.646   5.803  55.974  1.00 34.22           C
ANISOU 3121  C   TRP A 402     5580   3680   3744    215    133    266       C
ATOM   3122  O   TRP A 402      32.412   6.760  56.120  1.00 34.94           O
ANISOU 3122  O   TRP A 402     5591   3790   3894    233    114    234       O
ATOM   3123  CB  TRP A 402      31.461   3.887  57.611  1.00 33.54           C
ANISOU 3123  CB  TRP A 402     5570   3626   3549    229     89    354       C
ATOM   3124  CG  TRP A 402      32.971   3.995  57.667  1.00 34.88           C
ANISOU 3124  CG  TRP A 402     5682   3786   3785    293     71    360       C
ATOM   3125  CD1 TRP A 402      33.703   4.688  58.578  1.00 34.84           C
ANISOU 3125  CD1 TRP A 402     5596   3852   3791    315     19    335       C
ATOM   3126  CD2 TRP A 402      33.900   3.464  56.732  1.00 36.09           C
ANISOU 3126  CD2 TRP A 402     5845   3861   4007    341    107    382       C
ATOM   3127  NE1 TRP A 402      35.036   4.604  58.285  1.00 36.93           N
ANISOU 3127  NE1 TRP A 402     5816   4085   4132    371     16    349       N
ATOM   3128  CE2 TRP A 402      35.186   3.864  57.148  1.00 38.40           C
ANISOU 3128  CE2 TRP A 402     6055   4182   4354    391     74    378       C
ATOM   3129  CE3 TRP A 402      33.774   2.695  55.566  1.00 38.00           C
ANISOU 3129  CE3 TRP A 402     6152   4017   4267    348    163    396       C
ATOM   3130  CZ2 TRP A 402      36.337   3.511  56.456  1.00 42.71           C
ANISOU 3130  CZ2 TRP A 402     6579   4673   4976    448    102    395       C
ATOM   3131  CZ3 TRP A 402      34.918   2.345  54.883  1.00 43.41           C
ANISOU 3131  CZ3 TRP A 402     6821   4652   5020    408    192    405       C
ATOM   3132  CH2 TRP A 402      36.185   2.757  55.326  1.00 44.24           C
ANISOU 3132  CH2 TRP A 402     6839   4788   5183    458    165    408       C
ATOM   3133  N   ALA A 403      31.420   5.251  54.779  1.00 30.57           N
ANISOU 3133  N   ALA A 403     5176   3152   3287    211    183    285       N
ATOM   3134  CA  ALA A 403      32.091   5.762  53.589  1.00 34.79           C
ANISOU 3134  CA  ALA A 403     5682   3648   3887    232    224    276       C
ATOM   3135  C   ALA A 403      31.683   7.209  53.301  1.00 34.17           C
ANISOU 3135  C   ALA A 403     5545   3594   3844    199    222    240       C
ATOM   3136  O   ALA A 403      32.526   8.037  52.939  1.00 33.58           O
ANISOU 3136  O   ALA A 403     5401   3512   3844    217    230    234       O
ATOM   3137  CB  ALA A 403      31.793   4.866  52.393  1.00 30.01           C
ANISOU 3137  CB  ALA A 403     5156   2984   3261    231    276    292       C
ATOM   3138  N   LEU A 404      30.402   7.538  53.472  1.00 33.19           N
ANISOU 3138  N   LEU A 404     5440   3495   3677    150    211    219       N
ATOM   3139  CA  LEU A 404      29.979   8.927  53.327  1.00 33.24           C
ANISOU 3139  CA  LEU A 404     5384   3517   3728    125    201    183       C
ATOM   3140  C   LEU A 404      30.724   9.830  54.303  1.00 34.72           C
ANISOU 3140  C   LEU A 404     5482   3735   3974    141    157    144       C
ATOM   3141  O   LEU A 404      31.221  10.912  53.930  1.00 33.22           O
ANISOU 3141  O   LEU A 404     5223   3526   3874    144    158    128       O
ATOM   3142  CB  LEU A 404      28.468   9.049  53.550  1.00 33.57           C
ANISOU 3142  CB  LEU A 404     5453   3588   3714     77    191    162       C
ATOM   3143  CG  LEU A 404      27.520   8.368  52.562  1.00 36.18           C
ANISOU 3143  CG  LEU A 404     5858   3894   3993     47    224    188       C
ATOM   3144  CD1 LEU A 404      26.065   8.676  52.956  1.00 42.15           C
ANISOU 3144  CD1 LEU A 404     6616   4691   4710      0    207    162       C
ATOM   3145  CD2 LEU A 404      27.768   8.831  51.153  1.00 28.84           C
ANISOU 3145  CD2 LEU A 404     4925   2930   3104     53    260    207       C
ATOM   3146  N   THR A 405      30.815   9.413  55.570  1.00 33.38           N
ANISOU 3146  N   THR A 405     5311   3617   3756    150    116    128       N
ATOM   3147  CA  THR A 405      31.333  10.347  56.568  1.00 33.34           C
ANISOU 3147  CA  THR A 405     5220   3656   3793    159     65     70       C
ATOM   3148  C   THR A 405      32.843  10.500  56.522  1.00 35.26           C
ANISOU 3148  C   THR A 405     5403   3880   4115    199     53     79       C
ATOM   3149  O   THR A 405      33.350  11.541  56.955  1.00 34.07           O
ANISOU 3149  O   THR A 405     5167   3742   4038    199     17     25       O
ATOM   3150  CB  THR A 405      30.900   9.919  57.953  1.00 34.24           C
ANISOU 3150  CB  THR A 405     5346   3853   3813    155     23     48       C
ATOM   3151  OG1 THR A 405      31.303   8.568  58.168  1.00 33.62           O
ANISOU 3151  OG1 THR A 405     5325   3774   3676    180     26    116       O
ATOM   3152  CG2 THR A 405      29.384  10.056  58.085  1.00 29.88           C
ANISOU 3152  CG2 THR A 405     4824   3330   3199    112     34     25       C
ATOM   3153  N   THR A 406      33.572   9.509  55.990  1.00 32.78           N
ANISOU 3153  N   THR A 406     5126   3531   3797    233     83    140       N
ATOM   3154  CA  THR A 406      35.031   9.584  55.955  1.00 36.10           C
ANISOU 3154  CA  THR A 406     5482   3940   4296    275     75    152       C
ATOM   3155  C   THR A 406      35.626   9.794  54.559  1.00 35.54           C
ANISOU 3155  C   THR A 406     5395   3808   4301    286    138    186       C
ATOM   3156  O   THR A 406      36.766  10.252  54.462  1.00 35.97           O
ANISOU 3156  O   THR A 406     5369   3854   4443    308    135    188       O
ATOM   3157  CB  THR A 406      35.646   8.310  56.568  1.00 29.64           C
ANISOU 3157  CB  THR A 406     4695   3138   3427    320     56    195       C
ATOM   3158  OG1 THR A 406      35.183   7.150  55.849  1.00 36.18           O
ANISOU 3158  OG1 THR A 406     5621   3920   4206    326    106    246       O
ATOM   3159  CG2 THR A 406      35.241   8.169  58.015  1.00 33.54           C
ANISOU 3159  CG2 THR A 406     5190   3711   3841    313     -9    173       C
ATOM   3160  N   ARG A 407      34.897   9.467  53.487  1.00 34.18           N
ANISOU 3160  N   ARG A 407     5292   3601   4093    269    194    214       N
ATOM   3161  CA  ARG A 407      35.404   9.577  52.124  1.00 34.50           C
ANISOU 3161  CA  ARG A 407     5326   3602   4181    281    260    251       C
ATOM   3162  C   ARG A 407      34.833  10.744  51.331  1.00 35.86           C
ANISOU 3162  C   ARG A 407     5471   3761   4395    240    281    252       C
ATOM   3163  O   ARG A 407      35.456  11.141  50.352  1.00 36.92           O
ANISOU 3163  O   ARG A 407     5569   3875   4584    248    329    288       O
ATOM   3164  CB  ARG A 407      35.107   8.292  51.324  1.00 34.23           C
ANISOU 3164  CB  ARG A 407     5391   3544   4073    299    310    281       C
ATOM   3165  CG  ARG A 407      35.679   6.993  51.892  1.00 37.96           C
ANISOU 3165  CG  ARG A 407     5899   4007   4518    346    299    295       C
ATOM   3166  CD  ARG A 407      37.121   7.144  52.176  1.00 41.09           C
ANISOU 3166  CD  ARG A 407     6210   4408   4992    395    290    304       C
ATOM   3167  NE  ARG A 407      37.533   6.439  53.381  1.00 44.77           N
ANISOU 3167  NE  ARG A 407     6674   4893   5443    427    234    310       N
ATOM   3168  CZ  ARG A 407      38.740   5.921  53.565  1.00 49.09           C
ANISOU 3168  CZ  ARG A 407     7181   5435   6038    488    230    333       C
ATOM   3169  NH1 ARG A 407      39.616   5.833  52.575  1.00 50.35           N
ANISOU 3169  NH1 ARG A 407     7309   5566   6256    525    290    347       N
ATOM   3170  NH2 ARG A 407      39.098   5.540  54.787  1.00 48.33           N
ANISOU 3170  NH2 ARG A 407     7064   5371   5929    512    163    342       N
ATOM   3171  N   VAL A 408      33.662  11.284  51.687  1.00 33.55           N
ANISOU 3171  N   VAL A 408     5192   3479   4076    199    251    221       N
ATOM   3172  CA  VAL A 408      33.055  12.351  50.895  1.00 30.72           C
ANISOU 3172  CA  VAL A 408     4808   3100   3762    165    268    232       C
ATOM   3173  C   VAL A 408      33.555  13.723  51.354  1.00 33.72           C
ANISOU 3173  C   VAL A 408     5081   3465   4267    154    234    203       C
ATOM   3174  O   VAL A 408      33.319  14.146  52.494  1.00 32.89           O
ANISOU 3174  O   VAL A 408     4943   3380   4176    145    176    137       O
ATOM   3175  CB  VAL A 408      31.520  12.295  50.940  1.00 33.43           C
ANISOU 3175  CB  VAL A 408     5211   3459   4033    130    256    213       C
ATOM   3176  CG1 VAL A 408      30.930  13.441  50.112  1.00 31.44           C
ANISOU 3176  CG1 VAL A 408     4925   3184   3838    102    267    233       C
ATOM   3177  CG2 VAL A 408      31.009  10.966  50.401  1.00 30.28           C
ANISOU 3177  CG2 VAL A 408     4915   3065   3527    132    288    238       C
ATOM   3178  N   HIS A 409      34.224  14.435  50.446  1.00 35.04           N
ANISOU 3178  N   HIS A 409     5191   3597   4523    152    270    251       N
ATOM   3179  CA  HIS A 409      34.447  15.869  50.583  1.00 34.45           C
ANISOU 3179  CA  HIS A 409     5019   3485   4585    129    244    237       C
ATOM   3180  C   HIS A 409      33.354  16.536  49.788  1.00 31.53           C
ANISOU 3180  C   HIS A 409     4667   3091   4221     99    260    270       C
ATOM   3181  O   HIS A 409      33.406  16.511  48.560  1.00 30.74           O
ANISOU 3181  O   HIS A 409     4586   2984   4112     98    316    350       O
ATOM   3182  CB  HIS A 409      35.827  16.266  50.048  1.00 28.87           C
ANISOU 3182  CB  HIS A 409     4231   2753   3985    139    276    287       C
ATOM   3183  CG  HIS A 409      36.162  17.721  50.201  1.00 34.89           C
ANISOU 3183  CG  HIS A 409     4885   3463   4910    109    248    276       C
ATOM   3184  ND1 HIS A 409      35.323  18.738  49.789  1.00 32.57           N
ANISOU 3184  ND1 HIS A 409     4575   3123   4677     77    243    292       N
ATOM   3185  CD2 HIS A 409      37.274  18.328  50.693  1.00 34.80           C
ANISOU 3185  CD2 HIS A 409     4771   3429   5025    106    220    253       C
ATOM   3186  CE1 HIS A 409      35.902  19.903  50.019  1.00 32.84           C
ANISOU 3186  CE1 HIS A 409     4504   3099   4875     55    216    279       C
ATOM   3187  NE2 HIS A 409      37.084  19.684  50.570  1.00 34.05           N
ANISOU 3187  NE2 HIS A 409     4602   3267   5069     69    201    252       N
ATOM   3188  N   PRO A 410      32.340  17.139  50.426  1.00 31.21           N
ANISOU 3188  N   PRO A 410     4620   3045   4194     79    214    211       N
ATOM   3189  CA  PRO A 410      31.192  17.632  49.657  1.00 29.68           C
ANISOU 3189  CA  PRO A 410     4449   2833   3996     57    226    247       C
ATOM   3190  C   PRO A 410      31.548  18.742  48.676  1.00 37.59           C
ANISOU 3190  C   PRO A 410     5385   3777   5122     43    250    325       C
ATOM   3191  O   PRO A 410      30.794  18.961  47.718  1.00 39.24           O
ANISOU 3191  O   PRO A 410     5620   3980   5308     32    273    390       O
ATOM   3192  CB  PRO A 410      30.221  18.117  50.739  1.00 30.32           C
ANISOU 3192  CB  PRO A 410     4515   2920   4087     46    169    154       C
ATOM   3193  CG  PRO A 410      30.608  17.275  51.961  1.00 34.09           C
ANISOU 3193  CG  PRO A 410     5012   3452   4490     62    140     83       C
ATOM   3194  CD  PRO A 410      32.114  17.251  51.876  1.00 31.94           C
ANISOU 3194  CD  PRO A 410     4691   3162   4283     79    150    108       C
ATOM   3195  N   GLY A 411      32.671  19.443  48.870  1.00 33.47           N
ANISOU 3195  N   GLY A 411     4775   3213   4731     42    244    328       N
ATOM   3196  CA  GLY A 411      33.044  20.465  47.918  1.00 33.30           C
ANISOU 3196  CA  GLY A 411     4687   3133   4833     24    273    419       C
ATOM   3197  C   GLY A 411      33.487  19.921  46.571  1.00 37.10           C
ANISOU 3197  C   GLY A 411     5203   3647   5245     32    351    535       C
ATOM   3198  O   GLY A 411      33.621  20.689  45.606  1.00 38.90           O
ANISOU 3198  O   GLY A 411     5390   3844   5546     16    384    635       O
ATOM   3199  N   LYS A 412      33.764  18.629  46.486  1.00 34.44           N
ANISOU 3199  N   LYS A 412     4937   3374   4775     58    382    525       N
ATOM   3200  CA  LYS A 412      34.197  18.131  45.195  1.00 35.11           C
ANISOU 3200  CA  LYS A 412     5052   3496   4792     70    459    618       C
ATOM   3201  C   LYS A 412      33.619  16.783  44.834  1.00 33.60           C
ANISOU 3201  C   LYS A 412     4975   3366   4425     91    483    601       C
ATOM   3202  O   LYS A 412      33.666  16.430  43.651  1.00 34.32           O
ANISOU 3202  O   LYS A 412     5102   3497   4441     98    543    668       O
ATOM   3203  CB  LYS A 412      35.734  18.055  45.132  1.00 38.83           C
ANISOU 3203  CB  LYS A 412     5455   3968   5331     87    498    644       C
ATOM   3204  CG  LYS A 412      36.369  17.043  46.075  1.00 39.56           C
ANISOU 3204  CG  LYS A 412     5566   4086   5381    121    478    563       C
ATOM   3205  CD  LYS A 412      37.882  16.835  45.784  1.00 43.70           C
ANISOU 3205  CD  LYS A 412     6024   4622   5959    146    529    601       C
ATOM   3206  CE  LYS A 412      38.466  15.764  46.717  1.00 46.35           C
ANISOU 3206  CE  LYS A 412     6378   4982   6250    187    503    528       C
ATOM   3207  NZ  LYS A 412      37.819  14.382  46.642  1.00 51.41           N
ANISOU 3207  NZ  LYS A 412     7143   5660   6732    217    515    499       N
ATOM   3208  N   ASP A 413      33.062  16.023  45.779  1.00 30.98           N
ANISOU 3208  N   ASP A 413     4699   3046   4023     98    440    515       N
ATOM   3209  CA  ASP A 413      32.617  14.653  45.525  1.00 32.93           C
ANISOU 3209  CA  ASP A 413     5052   3338   4123    114    460    494       C
ATOM   3210  C   ASP A 413      31.100  14.548  45.352  1.00 35.58           C
ANISOU 3210  C   ASP A 413     5452   3688   4379     88    435    481       C
ATOM   3211  O   ASP A 413      30.566  13.437  45.241  1.00 34.33           O
ANISOU 3211  O   ASP A 413     5380   3558   4107     91    441    455       O
ATOM   3212  CB  ASP A 413      33.058  13.745  46.675  1.00 38.14           C
ANISOU 3212  CB  ASP A 413     5731   4001   4759    139    432    424       C
ATOM   3213  CG  ASP A 413      34.555  13.493  46.684  1.00 42.38           C
ANISOU 3213  CG  ASP A 413     6218   4536   5347    174    463    439       C
ATOM   3214  OD1 ASP A 413      35.128  13.255  45.586  1.00 42.92           O
ANISOU 3214  OD1 ASP A 413     6290   4620   5396    192    531    493       O
ATOM   3215  OD2 ASP A 413      35.144  13.496  47.796  1.00 43.97           O
ANISOU 3215  OD2 ASP A 413     6377   4729   5601    187    420    394       O
ATOM   3216  N   VAL A 414      30.390  15.664  45.419  1.00 33.35           N
ANISOU 3216  N   VAL A 414     5124   3381   4165     62    402    493       N
ATOM   3217  CA  VAL A 414      28.938  15.691  45.228  1.00 31.02           C
ANISOU 3217  CA  VAL A 414     4874   3103   3810     38    375    486       C
ATOM   3218  C   VAL A 414      28.686  16.491  43.969  1.00 36.05           C
ANISOU 3218  C   VAL A 414     5488   3741   4469     27    398    580       C
ATOM   3219  O   VAL A 414      29.053  17.672  43.886  1.00 34.23           O
ANISOU 3219  O   VAL A 414     5176   3465   4364     22    393    626       O
ATOM   3220  CB  VAL A 414      28.203  16.290  46.428  1.00 30.46           C
ANISOU 3220  CB  VAL A 414     4766   3009   3798     24    314    415       C
ATOM   3221  CG1 VAL A 414      26.724  16.326  46.136  1.00 37.88           C
ANISOU 3221  CG1 VAL A 414     5740   3969   4681      3    292    415       C
ATOM   3222  CG2 VAL A 414      28.468  15.412  47.708  1.00 30.97           C
ANISOU 3222  CG2 VAL A 414     4858   3092   3819     36    291    331       C
ATOM   3223  N   SER A 415      28.134  15.848  42.959  1.00 34.82           N
ANISOU 3223  N   SER A 415     5401   3637   4194     23    423    614       N
ATOM   3224  CA  SER A 415      27.813  16.555  41.729  1.00 37.00           C
ANISOU 3224  CA  SER A 415     5659   3933   4467     14    441    713       C
ATOM   3225  C   SER A 415      26.306  16.565  41.576  1.00 38.68           C
ANISOU 3225  C   SER A 415     5906   4168   4622     -8    396    703       C
ATOM   3226  O   SER A 415      25.638  15.541  41.761  1.00 41.01           O
ANISOU 3226  O   SER A 415     6273   4497   4813    -16    383    640       O
ATOM   3227  CB  SER A 415      28.491  15.922  40.506  1.00 36.01           C
ANISOU 3227  CB  SER A 415     5573   3868   4241     29    509    770       C
ATOM   3228  OG  SER A 415      29.805  15.505  40.841  1.00 45.47           O
ANISOU 3228  OG  SER A 415     6754   5052   5469     55    549    748       O
ATOM   3229  N   ILE A 416      25.784  17.727  41.255  1.00 39.43           N
ANISOU 3229  N   ILE A 416     5943   4239   4798    -17    371    768       N
ATOM   3230  CA  ILE A 416      24.364  17.980  41.152  1.00 36.31           C
ANISOU 3230  CA  ILE A 416     5555   3859   4381    -33    322    767       C
ATOM   3231  C   ILE A 416      24.158  18.453  39.727  1.00 34.70           C
ANISOU 3231  C   ILE A 416     5346   3697   4141    -34    337    891       C
ATOM   3232  O   ILE A 416      24.740  19.460  39.323  1.00 39.51           O
ANISOU 3232  O   ILE A 416     5890   4270   4851    -29    353    985       O
ATOM   3233  CB  ILE A 416      23.930  19.025  42.190  1.00 38.43           C
ANISOU 3233  CB  ILE A 416     5749   4055   4799    -33    272    727       C
ATOM   3234  CG1 ILE A 416      23.988  18.392  43.593  1.00 45.67           C
ANISOU 3234  CG1 ILE A 416     6682   4961   5708    -33    256    600       C
ATOM   3235  CG2 ILE A 416      22.590  19.604  41.866  1.00 38.23           C
ANISOU 3235  CG2 ILE A 416     5704   4036   4787    -41    228    757       C
ATOM   3236  CD1 ILE A 416      23.708  19.348  44.699  1.00 45.12           C
ANISOU 3236  CD1 ILE A 416     6539   4833   5772    -29    214    538       C
ATOM   3237  N   ILE A 417      23.406  17.684  38.941  1.00 37.22           N
ANISOU 3237  N   ILE A 417     5733   4096   4312    -44    333    895       N
ATOM   3238  CA  ILE A 417      23.247  17.924  37.508  1.00 34.90           C
ANISOU 3238  CA  ILE A 417     5447   3873   3941    -44    349   1008       C
ATOM   3239  C   ILE A 417      21.760  18.102  37.240  1.00 37.60           C
ANISOU 3239  C   ILE A 417     5792   4248   4247    -60    285   1018       C
ATOM   3240  O   ILE A 417      20.970  17.159  37.431  1.00 33.95           O
ANISOU 3240  O   ILE A 417     5388   3825   3688    -76    260    932       O
ATOM   3241  CB  ILE A 417      23.815  16.766  36.665  1.00 34.41           C
ANISOU 3241  CB  ILE A 417     5462   3895   3716    -39    404    994       C
ATOM   3242  CG1 ILE A 417      25.269  16.497  37.054  1.00 36.70           C
ANISOU 3242  CG1 ILE A 417     5743   4151   4050    -18    465    971       C
ATOM   3243  CG2 ILE A 417      23.714  17.072  35.153  1.00 32.06           C
ANISOU 3243  CG2 ILE A 417     5168   3691   3322    -37    423   1114       C
ATOM   3244  CD1 ILE A 417      25.574  15.042  37.312  1.00 40.44           C
ANISOU 3244  CD1 ILE A 417     6297   4647   4422    -10    490    862       C
ATOM   3245  N   GLU A 418      21.395  19.302  36.793  1.00 35.26           N
ANISOU 3245  N   GLU A 418     5428   3932   4036    -55    258   1127       N
ATOM   3246  CA  GLU A 418      20.039  19.774  36.541  1.00 41.41           C
ANISOU 3246  CA  GLU A 418     6183   4729   4821    -60    193   1160       C
ATOM   3247  C   GLU A 418      19.503  19.290  35.202  1.00 37.22           C
ANISOU 3247  C   GLU A 418     5702   4321   4120    -69    185   1223       C
ATOM   3248  O   GLU A 418      20.253  19.024  34.267  1.00 41.50           O
ANISOU 3248  O   GLU A 418     6275   4929   4564    -64    234   1285       O
ATOM   3249  CB  GLU A 418      19.995  21.299  36.508  1.00 40.99           C
ANISOU 3249  CB  GLU A 418     6034   4598   4944    -45    169   1269       C
ATOM   3250  CG  GLU A 418      20.104  22.012  37.842  1.00 49.74           C
ANISOU 3250  CG  GLU A 418     7076   5582   6239    -36    150   1195       C
ATOM   3251  CD  GLU A 418      20.025  23.534  37.638  1.00 56.34           C
ANISOU 3251  CD  GLU A 418     7817   6330   7258    -20    123   1309       C
ATOM   3252  OE1 GLU A 418      19.036  23.960  36.999  1.00 59.40           O
ANISOU 3252  OE1 GLU A 418     8184   6746   7640    -13     78   1387       O
ATOM   3253  OE2 GLU A 418      20.923  24.295  38.093  1.00 56.64           O
ANISOU 3253  OE2 GLU A 418     7798   6270   7452    -14    142   1322       O
ATOM   3254  N   ASN A 419      18.175  19.279  35.086  1.00 35.90           N
ANISOU 3254  N   ASN A 419     5530   4189   3919    -80    119   1213       N
ATOM   3255  CA  ASN A 419      17.514  19.070  33.788  1.00 38.57           C
ANISOU 3255  CA  ASN A 419     5895   4647   4111    -87     92   1287       C
ATOM   3256  C   ASN A 419      17.919  17.749  33.113  1.00 37.18           C
ANISOU 3256  C   ASN A 419     5815   4571   3740   -102    132   1227       C
ATOM   3257  O   ASN A 419      18.129  17.697  31.897  1.00 35.71           O
ANISOU 3257  O   ASN A 419     5651   4485   3430    -97    148   1309       O
ATOM   3258  CB  ASN A 419      17.781  20.268  32.857  1.00 36.49           C
ANISOU 3258  CB  ASN A 419     5573   4395   3897    -66     93   1470       C
ATOM   3259  CG  ASN A 419      16.654  20.490  31.813  1.00 45.77           C
ANISOU 3259  CG  ASN A 419     6738   5673   4980    -68     27   1561       C
ATOM   3260  OD1 ASN A 419      16.908  20.498  30.592  1.00 51.41           O
ANISOU 3260  OD1 ASN A 419     7472   6493   5568    -64     42   1669       O
ATOM   3261  ND2 ASN A 419      15.413  20.661  32.292  1.00 45.64           N
ANISOU 3261  ND2 ASN A 419     6687   5635   5020    -71    -47   1518       N
ATOM   3262  N   CYS A 420      17.983  16.675  33.897  1.00 35.45           N
ANISOU 3262  N   CYS A 420     5651   4326   3491   -118    145   1084       N
ATOM   3263  CA  CYS A 420      18.198  15.296  33.479  1.00 38.01           C
ANISOU 3263  CA  CYS A 420     6067   4718   3658   -133    173    993       C
ATOM   3264  C   CYS A 420      16.869  14.558  33.419  1.00 41.36           C
ANISOU 3264  C   CYS A 420     6524   5191   3999   -169    107    916       C
ATOM   3265  O   CYS A 420      15.840  15.082  33.849  1.00 38.62           O
ANISOU 3265  O   CYS A 420     6125   4823   3725   -180     47    925       O
ATOM   3266  CB  CYS A 420      19.144  14.600  34.462  1.00 37.33           C
ANISOU 3266  CB  CYS A 420     6013   4553   3617   -127    226    895       C
ATOM   3267  SG  CYS A 420      20.838  15.246  34.368  1.00 40.86           S
ANISOU 3267  SG  CYS A 420     6425   4961   4138    -88    308    975       S
ATOM   3268  N   PRO A 421      16.835  13.335  32.862  1.00 38.78           N
ANISOU 3268  N   PRO A 421     6278   4931   3526   -189    116    833       N
ATOM   3269  CA  PRO A 421      15.560  12.618  32.796  1.00 38.47           C
ANISOU 3269  CA  PRO A 421     6264   4934   3419   -232     49    757       C
ATOM   3270  C   PRO A 421      15.132  12.181  34.186  1.00 41.76           C
ANISOU 3270  C   PRO A 421     6676   5256   3933   -256     37    663       C
ATOM   3271  O   PRO A 421      15.967  11.831  35.034  1.00 38.78           O
ANISOU 3271  O   PRO A 421     6319   4801   3614   -245     87    615       O
ATOM   3272  CB  PRO A 421      15.866  11.421  31.890  1.00 38.50           C
ANISOU 3272  CB  PRO A 421     6357   5014   3257   -243     72    682       C
ATOM   3273  CG  PRO A 421      17.082  11.822  31.131  1.00 39.63           C
ANISOU 3273  CG  PRO A 421     6504   5198   3356   -200    141    760       C
ATOM   3274  CD  PRO A 421      17.884  12.578  32.163  1.00 41.58           C
ANISOU 3274  CD  PRO A 421     6699   5331   3769   -173    183    805       C
ATOM   3275  N   GLY A 422      13.817  12.253  34.426  1.00 34.89           N
ANISOU 3275  N   GLY A 422     5771   4403   3082   -289    -31    646       N
ATOM   3276  CA  GLY A 422      13.268  11.823  35.695  1.00 38.44           C
ANISOU 3276  CA  GLY A 422     6211   4785   3610   -318    -43    563       C
ATOM   3277  C   GLY A 422      12.069  10.898  35.527  1.00 41.63           C
ANISOU 3277  C   GLY A 422     6637   5236   3943   -376    -98    489       C
ATOM   3278  O   GLY A 422      11.799  10.372  34.441  1.00 40.47           O
ANISOU 3278  O   GLY A 422     6531   5169   3676   -396   -124    476       O
ATOM   3279  N   MET A 423      11.357  10.661  36.616  1.00 45.69           N
ANISOU 3279  N   MET A 423     7124   5707   4530   -407   -113    437       N
ATOM   3280  CA  MET A 423      10.109   9.927  36.563  1.00 46.20           C
ANISOU 3280  CA  MET A 423     7187   5811   4554   -468   -168    378       C
ATOM   3281  C   MET A 423       9.056  10.692  37.352  1.00 42.78           C
ANISOU 3281  C   MET A 423     6657   5374   4223   -474   -204    398       C
ATOM   3282  O   MET A 423       9.337  11.155  38.467  1.00 43.77           O
ANISOU 3282  O   MET A 423     6747   5436   4448   -451   -170    397       O
ATOM   3283  CB  MET A 423      10.264   8.505  37.095  1.00 44.73           C
ANISOU 3283  CB  MET A 423     7076   5577   4343   -514   -142    279       C
ATOM   3284  CG  MET A 423      11.074   7.581  36.183  1.00 49.50           C
ANISOU 3284  CG  MET A 423     7775   6191   4841   -513   -117    235       C
ATOM   3285  SD  MET A 423      10.127   6.853  34.792  1.00 57.19           S
ANISOU 3285  SD  MET A 423     8782   7268   5681   -566   -188    184       S
ATOM   3286  CE  MET A 423       9.891   8.159  33.586  1.00 42.43           C
ANISOU 3286  CE  MET A 423     6854   5515   3751   -525   -231    295       C
ATOM   3287  N   PRO A 424       7.851  10.867  36.799  1.00 44.79           N
ANISOU 3287  N   PRO A 424     6862   5701   4456   -500   -273    414       N
ATOM   3288  CA  PRO A 424       6.794  11.574  37.544  1.00 44.72           C
ANISOU 3288  CA  PRO A 424     6751   5692   4550   -501   -305    426       C
ATOM   3289  C   PRO A 424       6.493  10.926  38.891  1.00 41.91           C
ANISOU 3289  C   PRO A 424     6389   5288   4246   -540   -274    349       C
ATOM   3290  O   PRO A 424       6.116  11.618  39.851  1.00 40.25           O
ANISOU 3290  O   PRO A 424     6103   5055   4136   -519   -265    352       O
ATOM   3291  CB  PRO A 424       5.576  11.494  36.605  1.00 44.55           C
ANISOU 3291  CB  PRO A 424     6691   5766   4469   -536   -388    440       C
ATOM   3292  CG  PRO A 424       6.077  11.055  35.304  1.00 42.35           C
ANISOU 3292  CG  PRO A 424     6487   5545   4059   -539   -402    452       C
ATOM   3293  CD  PRO A 424       7.400  10.366  35.489  1.00 40.95           C
ANISOU 3293  CD  PRO A 424     6408   5306   3846   -530   -326    409       C
ATOM   3294  N   LEU A 425       6.698   9.611  39.006  1.00 44.92           N
ANISOU 3294  N   LEU A 425     6851   5651   4566   -591   -254    281       N
ATOM   3295  CA  LEU A 425       6.370   8.944  40.255  1.00 42.65           C
ANISOU 3295  CA  LEU A 425     6558   5323   4322   -634   -226    226       C
ATOM   3296  C   LEU A 425       7.245   9.431  41.396  1.00 39.81           C
ANISOU 3296  C   LEU A 425     6191   4900   4033   -585   -164    232       C
ATOM   3297  O   LEU A 425       6.950   9.119  42.550  1.00 37.39           O
ANISOU 3297  O   LEU A 425     5864   4576   3766   -609   -139    199       O
ATOM   3298  CB  LEU A 425       6.458   7.434  40.075  1.00 45.88           C
ANISOU 3298  CB  LEU A 425     7057   5712   4664   -698   -220    163       C
ATOM   3299  CG  LEU A 425       7.769   6.656  39.938  1.00 49.22           C
ANISOU 3299  CG  LEU A 425     7587   6073   5043   -682   -171    137       C
ATOM   3300  CD1 LEU A 425       8.454   6.464  41.278  1.00 46.31           C
ANISOU 3300  CD1 LEU A 425     7231   5632   4733   -667   -111    131       C
ATOM   3301  CD2 LEU A 425       7.461   5.298  39.311  1.00 57.45           C
ANISOU 3301  CD2 LEU A 425     8698   7112   6018   -750   -196     70       C
ATOM   3302  N   ASP A 426       8.298  10.196  41.098  1.00 40.52           N
ANISOU 3302  N   ASP A 426     6294   4964   4139   -521   -141    275       N
ATOM   3303  CA  ASP A 426       9.015  10.952  42.115  1.00 38.79           C
ANISOU 3303  CA  ASP A 426     6043   4692   4003   -470    -99    282       C
ATOM   3304  C   ASP A 426       8.239  12.241  42.352  1.00 37.53           C
ANISOU 3304  C   ASP A 426     5774   4553   3933   -439   -128    310       C
ATOM   3305  O   ASP A 426       8.323  13.164  41.517  1.00 39.47           O
ANISOU 3305  O   ASP A 426     5988   4806   4202   -399   -154    374       O
ATOM   3306  CB  ASP A 426      10.438  11.262  41.652  1.00 35.51           C
ANISOU 3306  CB  ASP A 426     5674   4237   3580   -420    -65    318       C
ATOM   3307  CG  ASP A 426      11.265  12.017  42.705  1.00 42.21           C
ANISOU 3307  CG  ASP A 426     6490   5029   4519   -372    -27    316       C
ATOM   3308  OD1 ASP A 426      10.705  12.514  43.728  1.00 42.75           O
ANISOU 3308  OD1 ASP A 426     6490   5095   4657   -368    -30    288       O
ATOM   3309  OD2 ASP A 426      12.477  12.208  42.442  1.00 45.27           O
ANISOU 3309  OD2 ASP A 426     6910   5381   4911   -336      4    342       O
ATOM   3310  N   PRO A 427       7.497  12.371  43.462  1.00 39.52           N
ANISOU 3310  N   PRO A 427     5962   4812   4240   -450   -123    268       N
ATOM   3311  CA  PRO A 427       6.707  13.603  43.687  1.00 37.06           C
ANISOU 3311  CA  PRO A 427     5539   4517   4025   -413   -150    283       C
ATOM   3312  C   PRO A 427       7.547  14.832  43.966  1.00 36.62           C
ANISOU 3312  C   PRO A 427     5448   4401   4065   -341   -132    305       C
ATOM   3313  O   PRO A 427       6.989  15.940  44.025  1.00 38.97           O
ANISOU 3313  O   PRO A 427     5654   4694   4458   -301   -157    321       O
ATOM   3314  CB  PRO A 427       5.857  13.264  44.919  1.00 38.37           C
ANISOU 3314  CB  PRO A 427     5656   4713   4212   -445   -131    218       C
ATOM   3315  CG  PRO A 427       6.767  12.340  45.725  1.00 38.15           C
ANISOU 3315  CG  PRO A 427     5708   4652   4135   -466    -78    182       C
ATOM   3316  CD  PRO A 427       7.464  11.467  44.635  1.00 35.67           C
ANISOU 3316  CD  PRO A 427     5500   4319   3736   -489    -84    210       C
ATOM   3317  N   SER A 428       8.842  14.679  44.238  1.00 37.65           N
ANISOU 3317  N   SER A 428     5640   4481   4187   -324    -90    299       N
ATOM   3318  CA  SER A 428       9.652  15.866  44.466  1.00 37.18           C
ANISOU 3318  CA  SER A 428     5540   4359   4229   -262    -79    319       C
ATOM   3319  C   SER A 428      10.213  16.459  43.172  1.00 37.76           C
ANISOU 3319  C   SER A 428     5625   4412   4311   -235    -96    413       C
ATOM   3320  O   SER A 428      10.825  17.522  43.236  1.00 36.07           O
ANISOU 3320  O   SER A 428     5368   4139   4198   -188    -91    445       O
ATOM   3321  CB  SER A 428      10.798  15.582  45.449  1.00 36.88           C
ANISOU 3321  CB  SER A 428     5541   4278   4194   -252    -30    270       C
ATOM   3322  OG  SER A 428      11.834  14.810  44.838  1.00 40.69           O
ANISOU 3322  OG  SER A 428     6116   4746   4600   -263     -7    299       O
ATOM   3323  N   THR A 429      10.005  15.828  42.009  1.00 37.96           N
ANISOU 3323  N   THR A 429     5701   4488   4234   -263   -117    459       N
ATOM   3324  CA  THR A 429      10.455  16.430  40.753  1.00 33.92           C
ANISOU 3324  CA  THR A 429     5194   3978   3715   -236   -132    559       C
ATOM   3325  C   THR A 429       9.793  17.785  40.502  1.00 38.47           C
ANISOU 3325  C   THR A 429     5671   4541   4406   -196   -176    626       C
ATOM   3326  O   THR A 429       8.591  17.955  40.707  1.00 38.42           O
ANISOU 3326  O   THR A 429     5602   4566   4429   -203   -216    606       O
ATOM   3327  CB  THR A 429      10.170  15.502  39.578  1.00 34.89           C
ANISOU 3327  CB  THR A 429     5384   4179   3695   -275   -153    582       C
ATOM   3328  OG1 THR A 429       8.778  15.211  39.544  1.00 41.30           O
ANISOU 3328  OG1 THR A 429     6159   5049   4484   -309   -204    556       O
ATOM   3329  CG2 THR A 429      10.970  14.214  39.713  1.00 37.57           C
ANISOU 3329  CG2 THR A 429     5824   4514   3938   -304   -107    521       C
ATOM   3330  N   ASN A 430      10.598  18.757  40.035  1.00 37.27           N
ANISOU 3330  N   ASN A 430     5497   4338   4326   -154   -168    711       N
ATOM   3331  CA  ASN A 430      10.131  20.085  39.632  1.00 39.88           C
ANISOU 3331  CA  ASN A 430     5738   4639   4777   -112   -210    798       C
ATOM   3332  C   ASN A 430      11.073  20.665  38.580  1.00 39.35           C
ANISOU 3332  C   ASN A 430     5685   4552   4713    -89   -199    927       C
ATOM   3333  O   ASN A 430      12.220  20.989  38.898  1.00 37.19           O
ANISOU 3333  O   ASN A 430     5421   4210   4501    -74   -154    931       O
ATOM   3334  CB  ASN A 430      10.036  21.053  40.819  1.00 37.35           C
ANISOU 3334  CB  ASN A 430     5332   4227   4630    -74   -206    741       C
ATOM   3335  CG  ASN A 430       9.165  22.246  40.518  1.00 43.97           C
ANISOU 3335  CG  ASN A 430     6070   5039   5599    -32   -260    807       C
ATOM   3336  OD1 ASN A 430       8.509  22.309  39.467  1.00 44.92           O
ANISOU 3336  OD1 ASN A 430     6178   5218   5671    -33   -307    900       O
ATOM   3337  ND2 ASN A 430       9.168  23.221  41.424  1.00 50.43           N
ANISOU 3337  ND2 ASN A 430     6810   5766   6586      9   -258    759       N
ATOM   3338  N   PRO A 431      10.664  20.763  37.308  1.00 37.70           N
ANISOU 3338  N   PRO A 431     5478   4415   4430    -90   -238   1035       N
ATOM   3339  CA  PRO A 431       9.443  20.276  36.643  1.00 36.27           C
ANISOU 3339  CA  PRO A 431     5296   4338   4146   -114   -298   1044       C
ATOM   3340  C   PRO A 431       9.110  18.817  36.916  1.00 40.23           C
ANISOU 3340  C   PRO A 431     5869   4905   4510   -169   -288    925       C
ATOM   3341  O   PRO A 431      10.028  18.013  36.912  1.00 40.72           O
ANISOU 3341  O   PRO A 431     6015   4968   4489   -189   -237    885       O
ATOM   3342  CB  PRO A 431       9.769  20.426  35.145  1.00 38.88           C
ANISOU 3342  CB  PRO A 431     5655   4742   4377   -108   -313   1182       C
ATOM   3343  CG  PRO A 431      11.022  21.217  35.041  1.00 33.44           C
ANISOU 3343  CG  PRO A 431     4960   3975   3771    -76   -264   1266       C
ATOM   3344  CD  PRO A 431      11.635  21.370  36.373  1.00 38.54           C
ANISOU 3344  CD  PRO A 431     5593   4508   4541    -68   -217   1168       C
ATOM   3345  N   PRO A 432       7.833  18.473  37.107  1.00 39.63           N
ANISOU 3345  N   PRO A 432     5758   4879   4419   -195   -337    875       N
ATOM   3346  CA  PRO A 432       7.484  17.063  37.373  1.00 39.04           C
ANISOU 3346  CA  PRO A 432     5748   4856   4228   -256   -329    768       C
ATOM   3347  C   PRO A 432       7.895  16.196  36.199  1.00 39.99           C
ANISOU 3347  C   PRO A 432     5960   5052   4182   -285   -331    788       C
ATOM   3348  O   PRO A 432       7.668  16.554  35.038  1.00 43.70           O
ANISOU 3348  O   PRO A 432     6420   5591   4594   -274   -375    879       O
ATOM   3349  CB  PRO A 432       5.955  17.081  37.547  1.00 41.06           C
ANISOU 3349  CB  PRO A 432     5927   5162   4510   -275   -391    742       C
ATOM   3350  CG  PRO A 432       5.608  18.531  37.803  1.00 46.92           C
ANISOU 3350  CG  PRO A 432     6561   5853   5413   -213   -415    805       C
ATOM   3351  CD  PRO A 432       6.648  19.339  37.007  1.00 40.34           C
ANISOU 3351  CD  PRO A 432     5744   4982   4599   -169   -403    923       C
ATOM   3352  N   GLY A 433       8.533  15.068  36.499  1.00 41.18           N
ANISOU 3352  N   GLY A 433     6199   5191   4257   -319   -283    703       N
ATOM   3353  CA  GLY A 433       9.090  14.201  35.471  1.00 42.85           C
ANISOU 3353  CA  GLY A 433     6501   5461   4318   -339   -271    700       C
ATOM   3354  C   GLY A 433      10.517  14.518  35.013  1.00 45.39           C
ANISOU 3354  C   GLY A 433     6865   5759   4621   -299   -212    760       C
ATOM   3355  O   GLY A 433      11.060  13.768  34.184  1.00 43.30           O
ANISOU 3355  O   GLY A 433     6676   5547   4228   -310   -192    746       O
ATOM   3356  N   MET A 434      11.124  15.609  35.501  1.00 40.09           N
ANISOU 3356  N   MET A 434     6141   5013   4079   -253   -184    822       N
ATOM   3357  CA  MET A 434      12.531  15.918  35.286  1.00 39.06           C
ANISOU 3357  CA  MET A 434     6037   4845   3959   -220   -121    872       C
ATOM   3358  C   MET A 434      13.287  15.730  36.587  1.00 39.53           C
ANISOU 3358  C   MET A 434     6106   4807   4107   -215    -68    794       C
ATOM   3359  O   MET A 434      12.735  15.878  37.686  1.00 40.31           O
ANISOU 3359  O   MET A 434     6163   4858   4296   -220    -82    735       O
ATOM   3360  CB  MET A 434      12.758  17.361  34.803  1.00 40.61           C
ANISOU 3360  CB  MET A 434     6161   5022   4247   -176   -131   1014       C
ATOM   3361  CG  MET A 434      12.179  17.725  33.439  1.00 38.83           C
ANISOU 3361  CG  MET A 434     5920   4900   3935   -172   -182   1127       C
ATOM   3362  SD  MET A 434      12.657  16.552  32.168  1.00 46.64           S
ANISOU 3362  SD  MET A 434     7013   6016   4690   -195   -158   1111       S
ATOM   3363  CE  MET A 434      14.271  17.194  31.750  1.00 45.75           C
ANISOU 3363  CE  MET A 434     6905   5877   4602   -155    -74   1218       C
ATOM   3364  N   HIS A 435      14.565  15.416  36.465  1.00 39.43           N
ANISOU 3364  N   HIS A 435     6142   4773   4065   -201     -6    795       N
ATOM   3365  CA  HIS A 435      15.389  15.140  37.625  1.00 34.68           C
ANISOU 3365  CA  HIS A 435     5554   4091   3532   -194     40    724       C
ATOM   3366  C   HIS A 435      16.558  16.096  37.673  1.00 37.70           C
ANISOU 3366  C   HIS A 435     5897   4416   4012   -154     80    794       C
ATOM   3367  O   HIS A 435      17.095  16.502  36.634  1.00 42.54           O
ANISOU 3367  O   HIS A 435     6509   5063   4592   -138     99    889       O
ATOM   3368  CB  HIS A 435      15.917  13.724  37.618  1.00 38.46           C
ANISOU 3368  CB  HIS A 435     6125   4585   3904   -214     77    643       C
ATOM   3369  CG  HIS A 435      15.162  12.784  38.503  1.00 37.88           C
ANISOU 3369  CG  HIS A 435     6077   4498   3816   -253     58    542       C
ATOM   3370  ND1 HIS A 435      15.418  11.423  38.536  1.00 39.85           N
ANISOU 3370  ND1 HIS A 435     6410   4749   3983   -277     80    466       N
ATOM   3371  CD2 HIS A 435      14.151  13.002  39.381  1.00 37.77           C
ANISOU 3371  CD2 HIS A 435     6014   4471   3865   -272     22    508       C
ATOM   3372  CE1 HIS A 435      14.612  10.850  39.417  1.00 40.94           C
ANISOU 3372  CE1 HIS A 435     6548   4870   4136   -315     58    401       C
ATOM   3373  NE2 HIS A 435      13.839  11.787  39.950  1.00 42.25           N
ANISOU 3373  NE2 HIS A 435     6634   5035   4385   -312     26    424       N
ATOM   3374  N   THR A 436      16.900  16.499  38.872  1.00 32.88           N
ANISOU 3374  N   THR A 436     5247   3725   3522   -142     91    749       N
ATOM   3375  CA  THR A 436      18.233  16.967  39.171  1.00 37.27           C
ANISOU 3375  CA  THR A 436     5784   4220   4158   -115    137    772       C
ATOM   3376  C   THR A 436      18.950  15.787  39.822  1.00 36.43           C
ANISOU 3376  C   THR A 436     5743   4105   3995   -123    176    680       C
ATOM   3377  O   THR A 436      18.590  15.356  40.919  1.00 38.33           O
ANISOU 3377  O   THR A 436     5988   4323   4252   -135    163    594       O
ATOM   3378  CB  THR A 436      18.198  18.211  40.048  1.00 34.05           C
ANISOU 3378  CB  THR A 436     5285   3728   3924    -96    117    776       C
ATOM   3379  OG1 THR A 436      17.561  19.259  39.314  1.00 41.13           O
ANISOU 3379  OG1 THR A 436     6123   4625   4878    -84     80    875       O
ATOM   3380  CG2 THR A 436      19.630  18.678  40.357  1.00 36.33           C
ANISOU 3380  CG2 THR A 436     5549   3952   4303    -75    160    794       C
ATOM   3381  N   LYS A 437      19.916  15.225  39.112  1.00 33.36           N
ANISOU 3381  N   LYS A 437     5403   3741   3531   -113    224    702       N
ATOM   3382  CA  LYS A 437      20.658  14.097  39.624  1.00 35.81           C
ANISOU 3382  CA  LYS A 437     5774   4038   3795   -112    261    625       C
ATOM   3383  C   LYS A 437      21.656  14.538  40.675  1.00 34.70           C
ANISOU 3383  C   LYS A 437     5589   3827   3770    -89    281    606       C
ATOM   3384  O   LYS A 437      22.207  15.640  40.630  1.00 35.40           O
ANISOU 3384  O   LYS A 437     5610   3879   3961    -71    288    666       O
ATOM   3385  CB  LYS A 437      21.421  13.395  38.504  1.00 36.71           C
ANISOU 3385  CB  LYS A 437     5946   4202   3800   -100    310    647       C
ATOM   3386  CG  LYS A 437      20.583  12.988  37.313  1.00 36.88           C
ANISOU 3386  CG  LYS A 437     6012   4309   3693   -120    290    663       C
ATOM   3387  CD  LYS A 437      19.493  12.047  37.678  1.00 36.67           C
ANISOU 3387  CD  LYS A 437     6031   4292   3610   -158    248    576       C
ATOM   3388  CE  LYS A 437      18.974  11.335  36.416  1.00 40.73           C
ANISOU 3388  CE  LYS A 437     6604   4894   3977   -177    237    566       C
ATOM   3389  NZ  LYS A 437      17.972  10.323  36.811  1.00 39.22           N
ANISOU 3389  NZ  LYS A 437     6457   4700   3745   -221    197    474       N
ATOM   3390  N   MET A 438      21.940  13.631  41.588  1.00 33.53           N
ANISOU 3390  N   MET A 438     5478   3657   3604    -91    289    526       N
ATOM   3391  CA  MET A 438      22.956  13.848  42.598  1.00 35.95           C
ANISOU 3391  CA  MET A 438     5751   3911   3998    -69    304    499       C
ATOM   3392  C   MET A 438      23.860  12.632  42.633  1.00 36.34           C
ANISOU 3392  C   MET A 438     5862   3961   3983    -55    344    464       C
ATOM   3393  O   MET A 438      23.413  11.540  42.982  1.00 36.97           O
ANISOU 3393  O   MET A 438     6004   4049   3994    -70    336    409       O
ATOM   3394  CB  MET A 438      22.339  14.080  43.967  1.00 35.01           C
ANISOU 3394  CB  MET A 438     5599   3768   3937    -80    264    434       C
ATOM   3395  CG  MET A 438      23.370  14.247  45.069  1.00 43.50           C
ANISOU 3395  CG  MET A 438     6639   4802   5086    -58    270    395       C
ATOM   3396  SD  MET A 438      22.538  14.482  46.644  1.00 49.93           S
ANISOU 3396  SD  MET A 438     7417   5615   5937    -70    225    311       S
ATOM   3397  CE  MET A 438      23.895  15.046  47.642  1.00 48.84           C
ANISOU 3397  CE  MET A 438     7221   5437   5900    -41    225    279       C
ATOM   3398  N   ILE A 439      25.125  12.836  42.300  1.00 37.29           N
ANISOU 3398  N   ILE A 439     5962   4070   4138    -24    387    500       N
ATOM   3399  CA  ILE A 439      26.156  11.806  42.350  1.00 37.52           C
ANISOU 3399  CA  ILE A 439     6034   4093   4130      2    428    471       C
ATOM   3400  C   ILE A 439      27.035  12.083  43.556  1.00 36.20           C
ANISOU 3400  C   ILE A 439     5814   3880   4059     21    420    446       C
ATOM   3401  O   ILE A 439      27.550  13.197  43.699  1.00 33.44           O
ANISOU 3401  O   ILE A 439     5386   3508   3811     28    418    481       O
ATOM   3402  CB  ILE A 439      27.009  11.819  41.071  1.00 35.23           C
ANISOU 3402  CB  ILE A 439     5746   3836   3803     26    488    528       C
ATOM   3403  CG1 ILE A 439      26.151  11.500  39.844  1.00 35.21           C
ANISOU 3403  CG1 ILE A 439     5798   3897   3685      7    491    545       C
ATOM   3404  CG2 ILE A 439      28.232  10.901  41.224  1.00 35.26           C
ANISOU 3404  CG2 ILE A 439     5773   3826   3798     64    534    495       C
ATOM   3405  CD1 ILE A 439      26.881  11.773  38.501  1.00 31.02           C
ANISOU 3405  CD1 ILE A 439     5256   3422   3106     29    551    616       C
ATOM   3406  N   ILE A 440      27.224  11.074  44.406  1.00 35.42           N
ANISOU 3406  N   ILE A 440     5757   3767   3934     30    413    389       N
ATOM   3407  CA  ILE A 440      28.097  11.165  45.569  1.00 37.11           C
ANISOU 3407  CA  ILE A 440     5928   3953   4220     52    400    364       C
ATOM   3408  C   ILE A 440      29.212  10.128  45.407  1.00 37.90           C
ANISOU 3408  C   ILE A 440     6062   4044   4295     91    441    359       C
ATOM   3409  O   ILE A 440      28.966   8.923  45.502  1.00 32.34           O
ANISOU 3409  O   ILE A 440     5431   3336   3523     93    443    329       O
ATOM   3410  CB  ILE A 440      27.329  10.941  46.876  1.00 35.12           C
ANISOU 3410  CB  ILE A 440     5684   3701   3960     32    350    310       C
ATOM   3411  CG1 ILE A 440      26.196  11.950  47.000  1.00 36.76           C
ANISOU 3411  CG1 ILE A 440     5852   3918   4195      0    316    306       C
ATOM   3412  CG2 ILE A 440      28.267  11.006  48.088  1.00 30.26           C
ANISOU 3412  CG2 ILE A 440     5024   3072   3401     57    331    283       C
ATOM   3413  CD1 ILE A 440      25.305  11.645  48.181  1.00 32.23           C
ANISOU 3413  CD1 ILE A 440     5289   3362   3594    -22    277    252       C
ATOM   3414  N   ASP A 441      30.440  10.586  45.202  1.00 36.63           N
ANISOU 3414  N   ASP A 441     5841   3875   4200    122    471    389       N
ATOM   3415  CA  ASP A 441      31.594   9.688  45.152  1.00 30.89           C
ANISOU 3415  CA  ASP A 441     5129   3140   3469    168    509    382       C
ATOM   3416  C   ASP A 441      32.145   9.553  46.562  1.00 37.63           C
ANISOU 3416  C   ASP A 441     5949   3973   4378    184    467    351       C
ATOM   3417  O   ASP A 441      32.816  10.463  47.070  1.00 35.29           O
ANISOU 3417  O   ASP A 441     5566   3671   4172    189    450    359       O
ATOM   3418  CB  ASP A 441      32.671  10.216  44.200  1.00 34.32           C
ANISOU 3418  CB  ASP A 441     5507   3589   3946    193    568    434       C
ATOM   3419  CG  ASP A 441      33.985   9.385  44.249  1.00 37.88           C
ANISOU 3419  CG  ASP A 441     5950   4031   4411    249    609    423       C
ATOM   3420  OD1 ASP A 441      34.040   8.327  44.907  1.00 36.15           O
ANISOU 3420  OD1 ASP A 441     5779   3789   4166    271    590    381       O
ATOM   3421  OD2 ASP A 441      34.980   9.794  43.620  1.00 42.62           O
ANISOU 3421  OD2 ASP A 441     6491   4647   5056    272    660    464       O
ATOM   3422  N   ALA A 442      31.896   8.392  47.179  1.00 34.27           N
ANISOU 3422  N   ALA A 442     5587   3536   3898    193    449    320       N
ATOM   3423  CA  ALA A 442      32.364   8.075  48.519  1.00 33.92           C
ANISOU 3423  CA  ALA A 442     5522   3484   3881    212    406    300       C
ATOM   3424  C   ALA A 442      33.470   7.020  48.505  1.00 35.39           C
ANISOU 3424  C   ALA A 442     5724   3648   4074    268    432    306       C
ATOM   3425  O   ALA A 442      33.581   6.209  49.447  1.00 29.45           O
ANISOU 3425  O   ALA A 442     4997   2884   3308    286    400    298       O
ATOM   3426  CB  ALA A 442      31.188   7.628  49.390  1.00 32.11           C
ANISOU 3426  CB  ALA A 442     5344   3264   3593    177    361    275       C
ATOM   3427  N   THR A 443      34.276   7.010  47.448  1.00 33.26           N
ANISOU 3427  N   THR A 443     5438   3376   3824    300    492    324       N
ATOM   3428  CA  THR A 443      35.419   6.112  47.331  1.00 36.88           C
ANISOU 3428  CA  THR A 443     5896   3814   4304    363    525    326       C
ATOM   3429  C   THR A 443      36.682   6.826  47.784  1.00 33.27           C
ANISOU 3429  C   THR A 443     5329   3369   3943    393    518    345       C
ATOM   3430  O   THR A 443      36.716   8.044  47.942  1.00 34.30           O
ANISOU 3430  O   THR A 443     5388   3518   4128    362    500    355       O
ATOM   3431  CB  THR A 443      35.611   5.631  45.895  1.00 35.74           C
ANISOU 3431  CB  THR A 443     5791   3671   4119    386    602    325       C
ATOM   3432  OG1 THR A 443      36.031   6.740  45.075  1.00 37.18           O
ANISOU 3432  OG1 THR A 443     5903   3891   4332    378    643    360       O
ATOM   3433  CG2 THR A 443      34.300   5.068  45.363  1.00 35.63           C
ANISOU 3433  CG2 THR A 443     5876   3651   4011    347    601    299       C
ATOM   3434  N   THR A 444      37.703   6.054  47.990  1.00 33.85           N
ANISOU 3434  N   THR A 444     5388   3427   4047    452    530    346       N
ATOM   3435  CA  THR A 444      39.009   6.544  48.426  1.00 32.67           C
ANISOU 3435  CA  THR A 444     5130   3291   3993    486    522    362       C
ATOM   3436  C   THR A 444      39.781   7.022  47.208  1.00 34.65           C
ANISOU 3436  C   THR A 444     5325   3558   4283    503    602    387       C
ATOM   3437  O   THR A 444      39.878   6.280  46.225  1.00 38.63           O
ANISOU 3437  O   THR A 444     5878   4059   4742    534    670    384       O
ATOM   3438  CB  THR A 444      39.771   5.425  49.149  1.00 36.87           C
ANISOU 3438  CB  THR A 444     5667   3801   4542    550    499    360       C
ATOM   3439  OG1 THR A 444      38.989   4.960  50.255  1.00 42.62           O
ANISOU 3439  OG1 THR A 444     6451   4522   5221    531    429    352       O
ATOM   3440  CG2 THR A 444      41.164   5.876  49.646  1.00 37.80           C
ANISOU 3440  CG2 THR A 444     5662   3939   4760    589    482    375       C
ATOM   3441  N   PRO A 445      40.315   8.247  47.223  1.00 32.50           N
ANISOU 3441  N   PRO A 445     4949   3306   4095    479    600    412       N
ATOM   3442  CA  PRO A 445      41.172   8.700  46.118  1.00 35.64           C
ANISOU 3442  CA  PRO A 445     5279   3725   4537    494    681    452       C
ATOM   3443  C   PRO A 445      42.228   7.674  45.718  1.00 41.40           C
ANISOU 3443  C   PRO A 445     5999   4459   5272    571    740    449       C
ATOM   3444  O   PRO A 445      42.775   6.954  46.557  1.00 43.28           O
ANISOU 3444  O   PRO A 445     6227   4678   5539    617    702    429       O
ATOM   3445  CB  PRO A 445      41.819   9.967  46.680  1.00 39.90           C
ANISOU 3445  CB  PRO A 445     5692   4268   5199    464    644    472       C
ATOM   3446  CG  PRO A 445      40.749  10.549  47.602  1.00 33.42           C
ANISOU 3446  CG  PRO A 445     4898   3431   4368    410    559    440       C
ATOM   3447  CD  PRO A 445      40.111   9.302  48.238  1.00 34.87           C
ANISOU 3447  CD  PRO A 445     5188   3608   4455    434    523    401       C
ATOM   3448  N   VAL A 446      42.453   7.568  44.409  1.00 38.45           N
ANISOU 3448  N   VAL A 446     5632   4114   4862    588    835    468       N
ATOM   3449  CA  VAL A 446      43.607   6.871  43.848  1.00 41.07           C
ANISOU 3449  CA  VAL A 446     5924   4463   5216    662    910    466       C
ATOM   3450  C   VAL A 446      44.247   7.805  42.823  1.00 44.16           C
ANISOU 3450  C   VAL A 446     6225   4911   5643    648    993    525       C
ATOM   3451  O   VAL A 446      43.619   8.786  42.377  1.00 43.28           O
ANISOU 3451  O   VAL A 446     6111   4818   5516    584    997    567       O
ATOM   3452  CB  VAL A 446      43.215   5.490  43.245  1.00 41.46           C
ANISOU 3452  CB  VAL A 446     6090   4497   5166    710    952    414       C
ATOM   3453  CG1 VAL A 446      42.247   4.729  44.181  1.00 38.40           C
ANISOU 3453  CG1 VAL A 446     5803   4049   4736    697    867    374       C
ATOM   3454  CG2 VAL A 446      42.617   5.584  41.884  1.00 35.33           C
ANISOU 3454  CG2 VAL A 446     5369   3765   4288    689   1026    414       C
ATOM   3455  N   PRO A 447      45.525   7.584  42.499  1.00 42.58           N
ANISOU 3455  N   PRO A 447     5937   4738   5502    705   1058    538       N
ATOM   3456  CA  PRO A 447      46.227   8.452  41.530  1.00 41.25           C
ANISOU 3456  CA  PRO A 447     5670   4631   5372    691   1147    606       C
ATOM   3457  C   PRO A 447      45.472   8.608  40.218  1.00 42.34           C
ANISOU 3457  C   PRO A 447     5878   4821   5388    664   1220    631       C
ATOM   3458  O   PRO A 447      44.817   7.673  39.739  1.00 39.40           O
ANISOU 3458  O   PRO A 447     5620   4454   4897    690   1240    575       O
ATOM   3459  CB  PRO A 447      47.567   7.727  41.314  1.00 42.29           C
ANISOU 3459  CB  PRO A 447     5728   4789   5552    777   1217    592       C
ATOM   3460  CG  PRO A 447      47.818   7.032  42.641  1.00 42.21           C
ANISOU 3460  CG  PRO A 447     5720   4716   5600    817   1122    543       C
ATOM   3461  CD  PRO A 447      46.445   6.631  43.164  1.00 42.29           C
ANISOU 3461  CD  PRO A 447     5870   4676   5522    784   1043    501       C
ATOM   3462  N   PRO A 448      45.565   9.795  39.576  1.00 40.39           N
ANISOU 3462  N   PRO A 448     5560   4617   5170    611   1261    718       N
ATOM   3463  CA  PRO A 448      46.367  10.920  40.081  1.00 42.73           C
ANISOU 3463  CA  PRO A 448     5714   4898   5624    574   1241    782       C
ATOM   3464  C   PRO A 448      45.611  11.902  40.990  1.00 41.82           C
ANISOU 3464  C   PRO A 448     5595   4717   5578    499   1132    791       C
ATOM   3465  O   PRO A 448      46.132  13.005  41.232  1.00 43.57           O
ANISOU 3465  O   PRO A 448     5702   4921   5932    455   1117    847       O
ATOM   3466  CB  PRO A 448      46.815  11.634  38.792  1.00 41.66           C
ANISOU 3466  CB  PRO A 448     5509   4840   5482    554   1353    881       C
ATOM   3467  CG  PRO A 448      45.666  11.411  37.848  1.00 43.62           C
ANISOU 3467  CG  PRO A 448     5881   5129   5564    540   1381    883       C
ATOM   3468  CD  PRO A 448      45.059  10.044  38.218  1.00 37.51           C
ANISOU 3468  CD  PRO A 448     5237   4326   4691    590   1341    766       C
ATOM   3469  N   GLU A 449      44.449  11.522  41.507  1.00 40.08           N
ANISOU 3469  N   GLU A 449     5488   4459   5282    486   1058    733       N
ATOM   3470  CA  GLU A 449      43.735  12.417  42.415  1.00 45.47           C
ANISOU 3470  CA  GLU A 449     6163   5086   6028    423    958    728       C
ATOM   3471  C   GLU A 449      44.557  12.608  43.685  1.00 46.52           C
ANISOU 3471  C   GLU A 449     6204   5182   6289    431    887    693       C
ATOM   3472  O   GLU A 449      45.040  11.633  44.253  1.00 43.85           O
ANISOU 3472  O   GLU A 449     5880   4845   5938    487    869    642       O
ATOM   3473  CB  GLU A 449      42.350  11.889  42.762  1.00 40.77           C
ANISOU 3473  CB  GLU A 449     5700   4468   5322    411    899    670       C
ATOM   3474  CG  GLU A 449      41.545  12.905  43.556  1.00 45.33           C
ANISOU 3474  CG  GLU A 449     6265   4999   5959    349    810    665       C
ATOM   3475  CD  GLU A 449      40.231  12.358  44.124  1.00 48.08           C
ANISOU 3475  CD  GLU A 449     6727   5328   6211    337    745    602       C
ATOM   3476  OE1 GLU A 449      39.768  11.282  43.679  1.00 46.72           O
ANISOU 3476  OE1 GLU A 449     6656   5176   5920    365    773    576       O
ATOM   3477  OE2 GLU A 449      39.676  13.002  45.053  1.00 49.43           O
ANISOU 3477  OE2 GLU A 449     6884   5466   6431    300    666    573       O
ATOM   3478  N   PRO A 450      44.804  13.839  44.119  1.00 49.00           N
ANISOU 3478  N   PRO A 450     6419   5466   6734    378    845    720       N
ATOM   3479  CA  PRO A 450      45.588  14.021  45.345  1.00 49.21           C
ANISOU 3479  CA  PRO A 450     6355   5467   6875    383    768    674       C
ATOM   3480  C   PRO A 450      44.807  13.506  46.543  1.00 45.44           C
ANISOU 3480  C   PRO A 450     5960   4969   6338    390    667    589       C
ATOM   3481  O   PRO A 450      43.574  13.481  46.546  1.00 40.74           O
ANISOU 3481  O   PRO A 450     5462   4360   5656    365    644    570       O
ATOM   3482  CB  PRO A 450      45.816  15.540  45.412  1.00 46.95           C
ANISOU 3482  CB  PRO A 450     5955   5143   6742    313    745    716       C
ATOM   3483  CG  PRO A 450      45.487  16.048  44.009  1.00 48.33           C
ANISOU 3483  CG  PRO A 450     6141   5334   6889    284    839    815       C
ATOM   3484  CD  PRO A 450      44.412  15.123  43.516  1.00 42.33           C
ANISOU 3484  CD  PRO A 450     5533   4603   5948    311    861    794       C
ATOM   3485  N   ASN A 451      45.537  13.013  47.531  1.00 51.04           N
ANISOU 3485  N   ASN A 451     6627   5684   7083    428    612    543       N
ATOM   3486  CA  ASN A 451      44.928  12.584  48.789  1.00 47.90           C
ANISOU 3486  CA  ASN A 451     6289   5279   6632    433    513    473       C
ATOM   3487  C   ASN A 451      45.319  13.570  49.880  1.00 45.81           C
ANISOU 3487  C   ASN A 451     5919   5004   6483    396    421    432       C
ATOM   3488  O   ASN A 451      46.520  13.706  50.164  1.00 44.41           O
ANISOU 3488  O   ASN A 451     5630   4839   6406    414    409    435       O
ATOM   3489  CB  ASN A 451      45.385  11.175  49.139  1.00 45.35           C
ANISOU 3489  CB  ASN A 451     6009   4976   6248    509    511    456       C
ATOM   3490  CG  ASN A 451      44.465  10.481  50.136  1.00 47.25           C
ANISOU 3490  CG  ASN A 451     6351   5212   6388    515    435    408       C
ATOM   3491  OD1 ASN A 451      44.011  11.081  51.111  1.00 48.90           O
ANISOU 3491  OD1 ASN A 451     6547   5425   6608    476    353    367       O
ATOM   3492  ND2 ASN A 451      44.183   9.212  49.883  1.00 45.30           N
ANISOU 3492  ND2 ASN A 451     6204   4961   6049    562    466    411       N
ATOM   3493  N   PRO A 452      44.377  14.305  50.479  1.00 45.30           N
ANISOU 3493  N   PRO A 452     5878   4918   6416    345    356    386       N
ATOM   3494  CA  PRO A 452      44.761  15.262  51.534  1.00 46.34           C
ANISOU 3494  CA  PRO A 452     5907   5040   6659    311    265    327       C
ATOM   3495  C   PRO A 452      45.447  14.601  52.721  1.00 49.76           C
ANISOU 3495  C   PRO A 452     6309   5519   7076    354    188    276       C
ATOM   3496  O   PRO A 452      46.294  15.234  53.361  1.00 54.31           O
ANISOU 3496  O   PRO A 452     6769   6102   7765    340    129    241       O
ATOM   3497  CB  PRO A 452      43.418  15.893  51.953  1.00 45.98           C
ANISOU 3497  CB  PRO A 452     5922   4973   6577    264    217    276       C
ATOM   3498  CG  PRO A 452      42.378  14.893  51.540  1.00 42.16           C
ANISOU 3498  CG  PRO A 452     5581   4504   5934    286    257    296       C
ATOM   3499  CD  PRO A 452      42.918  14.283  50.260  1.00 48.50           C
ANISOU 3499  CD  PRO A 452     6399   5311   6719    318    360    377       C
ATOM   3500  N   ARG A 453      45.067  13.370  53.057  1.00 45.40           N
ANISOU 3500  N   ARG A 453     5858   4999   6393    402    181    273       N
ATOM   3501  CA  ARG A 453      45.708  12.600  54.113  1.00 49.70           C
ANISOU 3501  CA  ARG A 453     6382   5590   6910    452    112    248       C
ATOM   3502  C   ARG A 453      45.356  11.138  53.899  1.00 42.73           C
ANISOU 3502  C   ARG A 453     5618   4713   5904    510    149    285       C
ATOM   3503  O   ARG A 453      44.201  10.756  54.082  1.00 43.25           O
ANISOU 3503  O   ARG A 453     5795   4777   5862    496    142    273       O
ATOM   3504  CB  ARG A 453      45.266  13.081  55.506  1.00 44.35           C
ANISOU 3504  CB  ARG A 453     5694   4949   6210    424     -1    166       C
ATOM   3505  CG  ARG A 453      45.962  12.334  56.654  1.00 52.12           C
ANISOU 3505  CG  ARG A 453     6649   5998   7157    475    -83    149       C
ATOM   3506  CD  ARG A 453      45.701  12.970  58.019  1.00 52.17           C
ANISOU 3506  CD  ARG A 453     6619   6059   7144    444   -196     58       C
ATOM   3507  NE  ARG A 453      44.309  12.858  58.441  1.00 48.45           N
ANISOU 3507  NE  ARG A 453     6258   5604   6547    421   -209     27       N
ATOM   3508  CZ  ARG A 453      43.753  11.755  58.932  1.00 48.00           C
ANISOU 3508  CZ  ARG A 453     6299   5586   6351    454   -220     54       C
ATOM   3509  NH1 ARG A 453      44.405  10.608  58.959  1.00 48.86           N
ANISOU 3509  NH1 ARG A 453     6425   5708   6431    516   -215    120       N
ATOM   3510  NH2 ARG A 453      42.503  11.803  59.398  1.00 42.93           N
ANISOU 3510  NH2 ARG A 453     5737   4969   5606    424   -235     19       N
ATOM   3511  N   GLU A 454      46.289  10.300  53.495  1.00 44.49           N
ANISOU 3511  N   GLU A 454     5818   4938   6147    573    192    328       N
ATOM   3512  CA  GLU A 454      45.843   8.928  53.339  1.00 50.87           C
ANISOU 3512  CA  GLU A 454     6745   5735   6849    624    221    352       C
ATOM   3513  C   GLU A 454      46.149   8.112  54.575  1.00 50.33           C
ANISOU 3513  C   GLU A 454     6680   5699   6743    672    135    348       C
ATOM   3514  O   GLU A 454      47.090   8.377  55.332  1.00 50.05           O
ANISOU 3514  O   GLU A 454     6539   5702   6774    691     69    337       O
ATOM   3515  CB  GLU A 454      46.425   8.247  52.116  1.00 52.30           C
ANISOU 3515  CB  GLU A 454     6934   5891   7047    676    325    395       C
ATOM   3516  CG  GLU A 454      47.801   8.622  51.835  1.00 61.78           C
ANISOU 3516  CG  GLU A 454     7997   7107   8369    703    351    414       C
ATOM   3517  CD  GLU A 454      48.264   8.015  50.536  1.00 71.08           C
ANISOU 3517  CD  GLU A 454     9185   8272   9551    752    468    449       C
ATOM   3518  OE1 GLU A 454      47.728   6.948  50.143  1.00 69.07           O
ANISOU 3518  OE1 GLU A 454     9045   7992   9207    790    507    449       O
ATOM   3519  OE2 GLU A 454      49.127   8.639  49.887  1.00 72.86           O
ANISOU 3519  OE2 GLU A 454     9303   8513   9868    748    525    474       O
ATOM   3520  N   THR A 455      45.303   7.131  54.786  1.00 46.14           N
ANISOU 3520  N   THR A 455     6270   5154   6105    687    131    361       N
ATOM   3521  CA  THR A 455      45.335   6.351  55.991  1.00 48.65           C
ANISOU 3521  CA  THR A 455     6612   5505   6368    723     49    373       C
ATOM   3522  C   THR A 455      45.523   4.909  55.576  1.00 49.16           C
ANISOU 3522  C   THR A 455     6747   5521   6412    794     94    424       C
ATOM   3523  O   THR A 455      45.258   4.544  54.431  1.00 49.93           O
ANISOU 3523  O   THR A 455     6903   5564   6505    801    184    430       O
ATOM   3524  CB  THR A 455      44.041   6.543  56.773  1.00 47.82           C
ANISOU 3524  CB  THR A 455     6584   5428   6157    667     -1    345       C
ATOM   3525  OG1 THR A 455      42.944   6.167  55.932  1.00 44.96           O
ANISOU 3525  OG1 THR A 455     6335   5014   5732    640     69    355       O
ATOM   3526  CG2 THR A 455      43.887   8.002  57.220  1.00 47.00           C
ANISOU 3526  CG2 THR A 455     6403   5366   6087    603    -49    279       C
ATOM   3527  N   GLN A 456      46.000   4.098  56.504  1.00 45.97           N
ANISOU 3527  N   GLN A 456     6335   5136   5997    850     28    458       N
ATOM   3528  CA  GLN A 456      45.965   2.658  56.339  1.00 46.61           C
ANISOU 3528  CA  GLN A 456     6498   5158   6055    914     54    509       C
ATOM   3529  C   GLN A 456      44.678   2.191  57.025  1.00 44.20           C
ANISOU 3529  C   GLN A 456     6308   4854   5634    873     15    525       C
ATOM   3530  O   GLN A 456      44.504   2.387  58.229  1.00 46.20           O
ANISOU 3530  O   GLN A 456     6545   5176   5834    856    -71    534       O
ATOM   3531  CB  GLN A 456      47.221   2.019  56.925  1.00 43.35           C
ANISOU 3531  CB  GLN A 456     6006   4758   5708   1003      4    553       C
ATOM   3532  CG  GLN A 456      47.232   0.490  56.874  1.00 49.13           C
ANISOU 3532  CG  GLN A 456     6818   5416   6435   1077     19    611       C
ATOM   3533  CD  GLN A 456      47.058  -0.040  55.461  1.00 52.11           C
ANISOU 3533  CD  GLN A 456     7259   5703   6838   1097    135    590       C
ATOM   3534  OE1 GLN A 456      47.801   0.327  54.549  1.00 53.70           O
ANISOU 3534  OE1 GLN A 456     7390   5901   7111   1121    203    561       O
ATOM   3535  NE2 GLN A 456      46.085  -0.918  55.277  1.00 52.53           N
ANISOU 3535  NE2 GLN A 456     7441   5688   6831   1087    157    602       N
ATOM   3536  N   LEU A 457      43.758   1.622  56.253  1.00 43.57           N
ANISOU 3536  N   LEU A 457     6339   4705   5509    853     81    525       N
ATOM   3537  CA  LEU A 457      42.543   1.053  56.817  1.00 42.30           C
ANISOU 3537  CA  LEU A 457     6285   4536   5250    814     55    548       C
ATOM   3538  C   LEU A 457      42.857  -0.175  57.673  1.00 41.23           C
ANISOU 3538  C   LEU A 457     6176   4382   5108    875      2    626       C
ATOM   3539  O   LEU A 457      43.883  -0.840  57.508  1.00 44.55           O
ANISOU 3539  O   LEU A 457     6560   4762   5606    956      8    657       O
ATOM   3540  CB  LEU A 457      41.561   0.674  55.709  1.00 39.50           C
ANISOU 3540  CB  LEU A 457     6034   4108   4864    780    135    527       C
ATOM   3541  CG  LEU A 457      40.955   1.862  54.959  1.00 45.68           C
ANISOU 3541  CG  LEU A 457     6808   4916   5633    710    177    468       C
ATOM   3542  CD1 LEU A 457      40.072   1.333  53.888  1.00 41.06           C
ANISOU 3542  CD1 LEU A 457     6323   4266   5011    686    247    453       C
ATOM   3543  CD2 LEU A 457      40.169   2.795  55.874  1.00 35.70           C
ANISOU 3543  CD2 LEU A 457     5529   3727   4309    641    117    446       C
ATOM   3544  N   LEU A 458      41.965  -0.467  58.617  1.00 36.64           N
ANISOU 3544  N   LEU A 458     5654   3833   4434    836    -48    663       N
ATOM   3545  CA  LEU A 458      42.151  -1.624  59.489  1.00 42.47           C
ANISOU 3545  CA  LEU A 458     6422   4556   5158    886   -101    756       C
ATOM   3546  C   LEU A 458      41.656  -2.855  58.738  1.00 41.01           C
ANISOU 3546  C   LEU A 458     6344   4240   4998    901    -41    787       C
ATOM   3547  O   LEU A 458      40.537  -3.332  58.923  1.00 47.81           O
ANISOU 3547  O   LEU A 458     7295   5075   5794    849    -36    814       O
ATOM   3548  CB  LEU A 458      41.429  -1.420  60.814  1.00 43.09           C
ANISOU 3548  CB  LEU A 458     6514   4736   5121    837   -175    790       C
ATOM   3549  CG  LEU A 458      41.866  -0.162  61.566  1.00 44.13           C
ANISOU 3549  CG  LEU A 458     6541   4999   5227    819   -239    736       C
ATOM   3550  CD1 LEU A 458      40.894   0.170  62.700  1.00 40.63           C
ANISOU 3550  CD1 LEU A 458     6123   4664   4651    758   -292    740       C
ATOM   3551  CD2 LEU A 458      43.301  -0.284  62.063  1.00 41.24           C
ANISOU 3551  CD2 LEU A 458     6076   4669   4925    899   -301    769       C
ATOM   3552  N   ASP A 459      42.512  -3.366  57.865  1.00 43.81           N
ANISOU 3552  N   ASP A 459     6682   4512   5452    973      8    775       N
ATOM   3553  CA  ASP A 459      42.182  -4.578  57.122  1.00 49.56           C
ANISOU 3553  CA  ASP A 459     7504   5106   6220    998     63    788       C
ATOM   3554  C   ASP A 459      41.828  -5.713  58.078  1.00 47.36           C
ANISOU 3554  C   ASP A 459     7286   4783   5926   1012      8    893       C
ATOM   3555  O   ASP A 459      42.445  -5.840  59.141  1.00 51.23           O
ANISOU 3555  O   ASP A 459     7723   5328   6416   1054    -67    969       O
ATOM   3556  CB  ASP A 459      43.350  -5.001  56.237  1.00 48.76           C
ANISOU 3556  CB  ASP A 459     7358   4936   6233   1093    115    761       C
ATOM   3557  CG  ASP A 459      43.603  -4.023  55.105  1.00 56.76           C
ANISOU 3557  CG  ASP A 459     8324   5981   7259   1075    189    667       C
ATOM   3558  OD1 ASP A 459      42.657  -3.264  54.741  1.00 51.94           O
ANISOU 3558  OD1 ASP A 459     7750   5408   6577    988    213    621       O
ATOM   3559  OD2 ASP A 459      44.746  -4.027  54.582  1.00 60.55           O
ANISOU 3559  OD2 ASP A 459     8729   6453   7825   1149    223    648       O
ATOM   3560  N   PRO A 460      40.852  -6.549  57.729  1.00 49.08           N
ANISOU 3560  N   PRO A 460     7612   4904   6133    975     40    904       N
ATOM   3561  CA  PRO A 460      40.400  -7.600  58.650  1.00 50.13           C
ANISOU 3561  CA  PRO A 460     7804   4990   6253    974     -9   1018       C
ATOM   3562  C   PRO A 460      41.536  -8.576  58.983  1.00 51.56           C
ANISOU 3562  C   PRO A 460     7953   5098   6540   1086    -43   1099       C
ATOM   3563  O   PRO A 460      42.486  -8.724  58.202  1.00 52.41           O
ANISOU 3563  O   PRO A 460     8019   5148   6746   1165     -4   1048       O
ATOM   3564  CB  PRO A 460      39.285  -8.313  57.872  1.00 50.66           C
ANISOU 3564  CB  PRO A 460     7982   4939   6326    918     47    990       C
ATOM   3565  CG  PRO A 460      39.400  -7.851  56.440  1.00 49.77           C
ANISOU 3565  CG  PRO A 460     7870   4798   6243    919    127    860       C
ATOM   3566  CD  PRO A 460      40.071  -6.504  56.481  1.00 49.96           C
ANISOU 3566  CD  PRO A 460     7791   4952   6238    925    120    814       C
ATOM   3567  N   PRO A 461      41.450  -9.234  60.137  1.00 55.49           N
ANISOU 3567  N   PRO A 461     8464   5603   7018   1098   -113   1229       N
ATOM   3568  CA  PRO A 461      42.517 -10.177  60.520  1.00 52.29           C
ANISOU 3568  CA  PRO A 461     8024   5126   6717   1210   -155   1323       C
ATOM   3569  C   PRO A 461      42.382 -11.516  59.801  1.00 56.54           C
ANISOU 3569  C   PRO A 461     8643   5462   7377   1250   -109   1335       C
ATOM   3570  O   PRO A 461      41.288 -11.912  59.407  1.00 57.25           O
ANISOU 3570  O   PRO A 461     8828   5474   7450   1177    -70   1316       O
ATOM   3571  CB  PRO A 461      42.314 -10.334  62.036  1.00 53.99           C
ANISOU 3571  CB  PRO A 461     8230   5438   6846   1194   -248   1467       C
ATOM   3572  CG  PRO A 461      41.380  -9.192  62.438  1.00 50.49           C
ANISOU 3572  CG  PRO A 461     7788   5148   6247   1083   -253   1417       C
ATOM   3573  CD  PRO A 461      40.512  -8.997  61.241  1.00 51.87           C
ANISOU 3573  CD  PRO A 461     8031   5247   6430   1016   -164   1302       C
ATOM   3574  N   ASP A 462      43.520 -12.207  59.615  1.00 58.21           N
ANISOU 3574  N   ASP A 462     8811   5585   7721   1369   -114   1359       N
ATOM   3575  CA  ASP A 462      43.505 -13.620  59.230  1.00 60.39           C
ANISOU 3575  CA  ASP A 462     9156   5659   8131   1424    -93   1396       C
ATOM   3576  C   ASP A 462      42.444 -14.434  59.933  1.00 55.92           C
ANISOU 3576  C   ASP A 462     8682   5025   7539   1358   -127   1517       C
ATOM   3577  O   ASP A 462      42.266 -14.290  61.143  1.00 59.86           O
ANISOU 3577  O   ASP A 462     9163   5629   7952   1331   -200   1644       O
ATOM   3578  CB  ASP A 462      44.828 -14.341  59.491  1.00 65.06           C
ANISOU 3578  CB  ASP A 462     9677   6183   8859   1566   -130   1467       C
ATOM   3579  CG  ASP A 462      45.792 -14.198  58.376  1.00 77.14           C
ANISOU 3579  CG  ASP A 462    11148   7674  10486   1651    -61   1338       C
ATOM   3580  OD1 ASP A 462      46.284 -15.285  57.971  1.00 80.42           O
ANISOU 3580  OD1 ASP A 462    11578   7925  11051   1747    -41   1344       O
ATOM   3581  OD2 ASP A 462      46.005 -13.067  57.885  1.00 73.45           O
ANISOU 3581  OD2 ASP A 462    10625   7328   9955   1622    -24   1234       O
ATOM   3582  N   GLY A 463      41.746 -15.275  59.191  1.00 60.32           N
ANISOU 3582  N   GLY A 463     9334   5416   8169   1330    -75   1477       N
ATOM   3583  CA  GLY A 463      40.741 -16.141  59.754  1.00 58.24           C
ANISOU 3583  CA  GLY A 463     9157   5064   7909   1263   -100   1592       C
ATOM   3584  C   GLY A 463      39.338 -15.590  59.723  1.00 56.74           C
ANISOU 3584  C   GLY A 463     9025   4946   7586   1119    -76   1556       C
ATOM   3585  O   GLY A 463      38.407 -16.335  60.024  1.00 60.60           O
ANISOU 3585  O   GLY A 463     9589   5350   8088   1052    -83   1636       O
ATOM   3586  N   THR A 464      39.153 -14.327  59.329  1.00 56.62           N
ANISOU 3586  N   THR A 464     8978   5079   7459   1070    -46   1438       N
ATOM   3587  CA  THR A 464      37.837 -13.705  59.445  1.00 56.38           C
ANISOU 3587  CA  THR A 464     8988   5137   7296    939    -33   1414       C
ATOM   3588  C   THR A 464      36.778 -14.546  58.750  1.00 61.44           C
ANISOU 3588  C   THR A 464     9729   5623   7992    870     11   1381       C
ATOM   3589  O   THR A 464      35.733 -14.857  59.334  1.00 63.92           O
ANISOU 3589  O   THR A 464    10090   5936   8259    781     -5   1465       O
ATOM   3590  CB  THR A 464      37.857 -12.287  58.866  1.00 57.92           C
ANISOU 3590  CB  THR A 464     9134   5474   7399    908      2   1275       C
ATOM   3591  OG1 THR A 464      38.677 -11.445  59.680  1.00 53.96           O
ANISOU 3591  OG1 THR A 464     8537   5127   6838    950    -49   1310       O
ATOM   3592  CG2 THR A 464      36.443 -11.707  58.809  1.00 53.08           C
ANISOU 3592  CG2 THR A 464     8566   4931   6671    779     23   1236       C
ATOM   3593  N   GLU A 465      37.059 -14.967  57.516  1.00 65.28           N
ANISOU 3593  N   GLU A 465    10244   5978   8581    912     65   1259       N
ATOM   3594  CA  GLU A 465      36.095 -15.758  56.752  1.00 68.19           C
ANISOU 3594  CA  GLU A 465    10706   6197   9008    848    103   1202       C
ATOM   3595  C   GLU A 465      35.826 -17.106  57.416  1.00 64.34           C
ANISOU 3595  C   GLU A 465    10270   5549   8628    846     66   1344       C
ATOM   3596  O   GLU A 465      34.673 -17.543  57.514  1.00 66.86           O
ANISOU 3596  O   GLU A 465    10652   5812   8941    744     67   1378       O
ATOM   3597  CB  GLU A 465      36.601 -15.941  55.322  1.00 70.63           C
ANISOU 3597  CB  GLU A 465    11027   6410   9398    909    167   1034       C
ATOM   3598  CG  GLU A 465      36.521 -14.673  54.465  1.00 67.63           C
ANISOU 3598  CG  GLU A 465    10616   6173   8907    879    215    893       C
ATOM   3599  CD  GLU A 465      35.181 -13.959  54.575  1.00 75.25           C
ANISOU 3599  CD  GLU A 465    11609   7241   9743    745    214    882       C
ATOM   3600  OE1 GLU A 465      34.236 -14.388  53.871  1.00 79.26           O
ANISOU 3600  OE1 GLU A 465    12188   7668  10261    675    240    813       O
ATOM   3601  OE2 GLU A 465      35.076 -12.960  55.337  1.00 67.37           O
ANISOU 3601  OE2 GLU A 465    10558   6403   8635    711    185    933       O
ATOM   3602  N   GLU A 466      36.881 -17.780  57.881  1.00 66.02           N
ANISOU 3602  N   GLU A 466    10452   5684   8949    958     31   1437       N
ATOM   3603  CA  GLU A 466      36.703 -19.056  58.572  1.00 64.60           C
ANISOU 3603  CA  GLU A 466    10315   5347   8884    964    -10   1596       C
ATOM   3604  C   GLU A 466      35.885 -18.886  59.851  1.00 64.46           C
ANISOU 3604  C   GLU A 466    10299   5443   8749    871    -57   1767       C
ATOM   3605  O   GLU A 466      34.985 -19.687  60.136  1.00 62.02           O
ANISOU 3605  O   GLU A 466    10052   5030   8484    794    -63   1857       O
ATOM   3606  CB  GLU A 466      38.073 -19.678  58.892  1.00 67.68           C
ANISOU 3606  CB  GLU A 466    10656   5655   9404   1113    -45   1673       C
ATOM   3607  CG  GLU A 466      38.880 -20.166  57.677  1.00 69.27           C
ANISOU 3607  CG  GLU A 466    10859   5704   9756   1218      5   1520       C
ATOM   3608  CD  GLU A 466      39.725 -19.064  57.011  1.00 75.59           C
ANISOU 3608  CD  GLU A 466    11585   6651  10487   1277     45   1376       C
ATOM   3609  OE1 GLU A 466      39.421 -17.849  57.168  1.00 67.01           O
ANISOU 3609  OE1 GLU A 466    10464   5761   9236   1210     48   1345       O
ATOM   3610  OE2 GLU A 466      40.705 -19.424  56.319  1.00 83.26           O
ANISOU 3610  OE2 GLU A 466    12526   7534  11576   1392     76   1292       O
ATOM   3611  N   TRP A 467      36.172 -17.832  60.626  1.00 65.39           N
ANISOU 3611  N   TRP A 467    10347   5781   8716    873    -88   1807       N
ATOM   3612  CA  TRP A 467      35.490 -17.626  61.902  1.00 63.40           C
ANISOU 3612  CA  TRP A 467    10089   5665   8336    796   -132   1964       C
ATOM   3613  C   TRP A 467      34.030 -17.228  61.713  1.00 61.17           C
ANISOU 3613  C   TRP A 467     9851   5435   7954    652    -93   1913       C
ATOM   3614  O   TRP A 467      33.199 -17.523  62.578  1.00 62.57           O
ANISOU 3614  O   TRP A 467    10050   5649   8075    573   -112   2050       O
ATOM   3615  CB  TRP A 467      36.223 -16.570  62.722  1.00 56.07           C
ANISOU 3615  CB  TRP A 467     9070   4959   7274    841   -177   1992       C
ATOM   3616  CG  TRP A 467      37.280 -17.155  63.556  1.00 53.62           C
ANISOU 3616  CG  TRP A 467     8716   4633   7023    947   -244   2144       C
ATOM   3617  CD1 TRP A 467      38.611 -17.185  63.287  1.00 53.50           C
ANISOU 3617  CD1 TRP A 467     8643   4586   7099   1074   -262   2110       C
ATOM   3618  CD2 TRP A 467      37.100 -17.844  64.803  1.00 58.12           C
ANISOU 3618  CD2 TRP A 467     9294   5219   7570    939   -304   2366       C
ATOM   3619  NE1 TRP A 467      39.284 -17.832  64.303  1.00 57.90           N
ANISOU 3619  NE1 TRP A 467     9168   5139   7693   1150   -337   2296       N
ATOM   3620  CE2 TRP A 467      38.377 -18.250  65.242  1.00 58.09           C
ANISOU 3620  CE2 TRP A 467     9235   5192   7645   1068   -364   2460       C
ATOM   3621  CE3 TRP A 467      35.982 -18.149  65.594  1.00 56.78           C
ANISOU 3621  CE3 TRP A 467     9167   5088   7318    834   -311   2503       C
ATOM   3622  CZ2 TRP A 467      38.572 -18.945  66.444  1.00 60.94           C
ANISOU 3622  CZ2 TRP A 467     9585   5569   7999   1098   -437   2691       C
ATOM   3623  CZ3 TRP A 467      36.176 -18.843  66.789  1.00 57.81           C
ANISOU 3623  CZ3 TRP A 467     9288   5238   7439    860   -376   2734       C
ATOM   3624  CH2 TRP A 467      37.465 -19.231  67.200  1.00 62.21           C
ANISOU 3624  CH2 TRP A 467     9793   5773   8071    992   -440   2828       C
ATOM   3625  N   GLU A 468      33.699 -16.578  60.599  1.00 58.80           N
ANISOU 3625  N   GLU A 468     9563   5146   7632    618    -39   1725       N
ATOM   3626  CA  GLU A 468      32.303 -16.261  60.313  1.00 61.84           C
ANISOU 3626  CA  GLU A 468     9989   5568   7942    486     -5   1670       C
ATOM   3627  C   GLU A 468      31.459 -17.523  60.210  1.00 61.50           C
ANISOU 3627  C   GLU A 468    10020   5337   8009    420      3   1738       C
ATOM   3628  O   GLU A 468      30.368 -17.597  60.786  1.00 60.27           O
ANISOU 3628  O   GLU A 468     9883   5226   7791    313      1   1821       O
ATOM   3629  CB  GLU A 468      32.197 -15.445  59.022  1.00 62.71           C
ANISOU 3629  CB  GLU A 468    10098   5703   8026    475     47   1461       C
ATOM   3630  CG  GLU A 468      32.485 -13.961  59.181  1.00 61.38           C
ANISOU 3630  CG  GLU A 468     9857   5746   7719    483     46   1396       C
ATOM   3631  CD  GLU A 468      32.116 -13.177  57.942  1.00 61.55           C
ANISOU 3631  CD  GLU A 468     9884   5793   7708    448     98   1217       C
ATOM   3632  OE1 GLU A 468      31.096 -13.511  57.301  1.00 69.17           O
ANISOU 3632  OE1 GLU A 468    10907   6686   8688    368    127   1163       O
ATOM   3633  OE2 GLU A 468      32.861 -12.237  57.592  1.00 67.31           O
ANISOU 3633  OE2 GLU A 468    10558   6614   8403    501    108   1135       O
ATOM   3634  N   GLU A 469      31.945 -18.525  59.467  1.00 64.31           N
ANISOU 3634  N   GLU A 469    10418   5479   8539    481     13   1697       N
ATOM   3635  CA  GLU A 469      31.247 -19.809  59.401  1.00 62.38           C
ANISOU 3635  CA  GLU A 469    10243   5030   8430    424     13   1765       C
ATOM   3636  C   GLU A 469      31.210 -20.483  60.767  1.00 61.86           C
ANISOU 3636  C   GLU A 469    10171   4954   8380    417    -36   2010       C
ATOM   3637  O   GLU A 469      30.180 -21.039  61.165  1.00 65.68           O
ANISOU 3637  O   GLU A 469    10691   5386   8879    312    -37   2112       O
ATOM   3638  CB  GLU A 469      31.928 -20.739  58.387  1.00 63.12           C
ANISOU 3638  CB  GLU A 469    10374   4894   8716    510     29   1664       C
ATOM   3639  CG  GLU A 469      31.929 -20.253  56.942  1.00 67.03           C
ANISOU 3639  CG  GLU A 469    10883   5384   9200    516     83   1424       C
ATOM   3640  CD  GLU A 469      33.254 -20.542  56.239  1.00 70.16           C
ANISOU 3640  CD  GLU A 469    11264   5687   9708    662     98   1328       C
ATOM   3641  OE1 GLU A 469      34.040 -21.359  56.772  1.00 80.22           O
ANISOU 3641  OE1 GLU A 469    12527   6844  11107    751     66   1442       O
ATOM   3642  OE2 GLU A 469      33.517 -19.947  55.166  1.00 75.94           O
ANISOU 3642  OE2 GLU A 469    11987   6465  10401    689    144   1147       O
ATOM   3643  N   LYS A 470      32.334 -20.458  61.493  1.00 60.68           N
ANISOU 3643  N   LYS A 470     9972   4855   8228    527    -79   2114       N
ATOM   3644  CA  LYS A 470      32.428 -21.165  62.769  1.00 63.21           C
ANISOU 3644  CA  LYS A 470    10286   5165   8567    536   -132   2360       C
ATOM   3645  C   LYS A 470      31.425 -20.617  63.779  1.00 68.50           C
ANISOU 3645  C   LYS A 470    10940   6032   9054    421   -138   2473       C
ATOM   3646  O   LYS A 470      30.721 -21.378  64.460  1.00 70.07           O
ANISOU 3646  O   LYS A 470    11168   6177   9280    350   -148   2646       O
ATOM   3647  CB  LYS A 470      33.854 -21.058  63.323  1.00 61.24           C
ANISOU 3647  CB  LYS A 470     9973   4971   8324    679   -183   2432       C
ATOM   3648  CG  LYS A 470      34.310 -22.208  64.182  1.00 72.85           C
ANISOU 3648  CG  LYS A 470    11444   6323   9913    735   -240   2658       C
ATOM   3649  CD  LYS A 470      35.706 -21.946  64.740  1.00 79.23           C
ANISOU 3649  CD  LYS A 470    12181   7219  10704    877   -295   2722       C
ATOM   3650  CE  LYS A 470      36.789 -22.650  63.923  1.00 86.29           C
ANISOU 3650  CE  LYS A 470    13062   7915  11809   1004   -299   2638       C
ATOM   3651  NZ  LYS A 470      38.168 -22.123  64.180  1.00 85.87           N
ANISOU 3651  NZ  LYS A 470    12931   7966  11732   1145   -335   2642       N
ATOM   3652  N   LEU A 471      31.357 -19.293  63.901  1.00 62.09           N
ANISOU 3652  N   LEU A 471    10079   5451   8060    404   -129   2379       N
ATOM   3653  CA  LEU A 471      30.373 -18.703  64.794  1.00 68.73           C
ANISOU 3653  CA  LEU A 471    10901   6489   8723    300   -126   2457       C
ATOM   3654  C   LEU A 471      28.959 -19.030  64.323  1.00 70.25           C
ANISOU 3654  C   LEU A 471    11145   6602   8943    164    -78   2424       C
ATOM   3655  O   LEU A 471      28.065 -19.267  65.146  1.00 68.15           O
ANISOU 3655  O   LEU A 471    10883   6398   8613     72    -76   2567       O
ATOM   3656  CB  LEU A 471      30.596 -17.193  64.892  1.00 64.10           C
ANISOU 3656  CB  LEU A 471    10250   6142   7961    314   -125   2333       C
ATOM   3657  CG  LEU A 471      31.933 -16.774  65.511  1.00 58.67           C
ANISOU 3657  CG  LEU A 471     9498   5564   7229    434   -181   2371       C
ATOM   3658  CD1 LEU A 471      32.104 -15.259  65.486  1.00 56.09           C
ANISOU 3658  CD1 LEU A 471     9109   5451   6753    437   -177   2226       C
ATOM   3659  CD2 LEU A 471      32.052 -17.306  66.906  1.00 56.60           C
ANISOU 3659  CD2 LEU A 471     9220   5375   6911    444   -235   2605       C
ATOM   3660  N   LYS A 472      28.750 -19.086  63.002  1.00 66.10           N
ANISOU 3660  N   LYS A 472    10658   5944   8514    150    -40   2242       N
ATOM   3661  CA  LYS A 472      27.400 -19.251  62.472  1.00 69.08           C
ANISOU 3661  CA  LYS A 472    11075   6268   8905     19     -0   2183       C
ATOM   3662  C   LYS A 472      26.755 -20.550  62.937  1.00 75.99           C
ANISOU 3662  C   LYS A 472    11993   6981   9899    -52     -8   2358       C
ATOM   3663  O   LYS A 472      25.636 -20.530  63.462  1.00 81.43           O
ANISOU 3663  O   LYS A 472    12678   7745  10518   -169      9   2441       O
ATOM   3664  CB  LYS A 472      27.374 -19.161  60.946  1.00 66.55           C
ANISOU 3664  CB  LYS A 472    10788   5831   8667     25     34   1958       C
ATOM   3665  CG  LYS A 472      27.061 -17.770  60.447  1.00 66.75           C
ANISOU 3665  CG  LYS A 472    10779   6042   8543     -0     61   1795       C
ATOM   3666  CD  LYS A 472      27.789 -17.450  59.174  1.00 67.53           C
ANISOU 3666  CD  LYS A 472    10885   6083   8691     76     81   1602       C
ATOM   3667  CE  LYS A 472      26.994 -16.467  58.348  1.00 65.37           C
ANISOU 3667  CE  LYS A 472    10604   5913   8322      7    116   1440       C
ATOM   3668  NZ  LYS A 472      27.878 -15.794  57.381  1.00 70.85           N
ANISOU 3668  NZ  LYS A 472    11280   6630   9009     94    134   1282       N
ATOM   3669  N   GLU A 473      27.424 -21.694  62.773  1.00 81.64           N
ANISOU 3669  N   GLU A 473    12734   7482  10804     15    -30   2417       N
ATOM   3670  CA  GLU A 473      26.675 -22.847  63.226  1.00 85.33           C
ANISOU 3670  CA  GLU A 473    13180   7845  11397    -66    -28   2563       C
ATOM   3671  C   GLU A 473      26.895 -23.073  64.737  1.00 83.77           C
ANISOU 3671  C   GLU A 473    12924   7773  11131    -43    -48   2813       C
ATOM   3672  O   GLU A 473      26.012 -23.630  65.398  1.00 88.62           O
ANISOU 3672  O   GLU A 473    13530   8399  11743   -123    -10   2944       O
ATOM   3673  CB  GLU A 473      27.005 -24.141  62.464  1.00 90.06           C
ANISOU 3673  CB  GLU A 473    13798   8163  12259    -28    -31   2522       C
ATOM   3674  CG  GLU A 473      25.892 -25.185  62.813  1.00 94.97           C
ANISOU 3674  CG  GLU A 473    14409   8682  12993   -140      3   2643       C
ATOM   3675  CD  GLU A 473      26.341 -26.459  63.444  1.00102.30           C
ANISOU 3675  CD  GLU A 473    15368   9456  14045    -70     32   2798       C
ATOM   3676  OE1 GLU A 473      27.501 -26.523  63.870  1.00105.86           O
ANISOU 3676  OE1 GLU A 473    15841   9919  14463     55     -4   2845       O
ATOM   3677  OE2 GLU A 473      25.471 -27.306  63.705  1.00103.44           O
ANISOU 3677  OE2 GLU A 473    15566   9506  14229   -161     61   2861       O
ATOM   3678  N   LEU A 474      27.994 -22.561  65.330  1.00 78.57           N
ANISOU 3678  N   LEU A 474    12239   7233  10379     67    -91   2868       N
ATOM   3679  CA  LEU A 474      28.031 -22.457  66.784  1.00 77.72           C
ANISOU 3679  CA  LEU A 474    12101   7312  10118     82    -96   3064       C
ATOM   3680  C   LEU A 474      26.771 -21.766  67.286  1.00 79.84           C
ANISOU 3680  C   LEU A 474    12349   7779  10209    -49    -63   3081       C
ATOM   3681  O   LEU A 474      26.272 -22.091  68.366  1.00 81.31           O
ANISOU 3681  O   LEU A 474    12531   8064  10299    -90    -47   3227       O
ATOM   3682  CB  LEU A 474      29.280 -21.702  67.238  1.00 76.30           C
ANISOU 3682  CB  LEU A 474    11888   7272   9831    200   -159   3079       C
ATOM   3683  CG  LEU A 474      30.539 -22.470  67.650  1.00 73.93           C
ANISOU 3683  CG  LEU A 474    11615   6875   9602    326   -225   3159       C
ATOM   3684  CD1 LEU A 474      31.384 -21.556  68.489  1.00 75.07           C
ANISOU 3684  CD1 LEU A 474    11691   7252   9580    399   -288   3210       C
ATOM   3685  CD2 LEU A 474      30.259 -23.750  68.397  1.00 67.42           C
ANISOU 3685  CD2 LEU A 474    10819   5961   8837    300   -233   3314       C
ATOM   3686  N   LEU A 475      26.239 -20.817  66.509  1.00 79.99           N
ANISOU 3686  N   LEU A 475    12384   7854  10156   -114    -52   2905       N
ATOM   3687  CA  LEU A 475      24.943 -20.213  66.815  1.00 79.64           C
ANISOU 3687  CA  LEU A 475    12322   7970   9967   -241    -11   2897       C
ATOM   3688  C   LEU A 475      23.826 -21.246  66.707  1.00 84.91           C
ANISOU 3688  C   LEU A 475    12992   8507  10764   -347     37   2960       C
ATOM   3689  O   LEU A 475      23.041 -21.432  67.646  1.00 88.14           O
ANISOU 3689  O   LEU A 475    13369   9030  11091   -413     71   3092       O
ATOM   3690  CB  LEU A 475      24.678 -19.038  65.881  1.00 74.47           C
ANISOU 3690  CB  LEU A 475    11686   7383   9227   -263     10   2665       C
ATOM   3691  CG  LEU A 475      25.090 -17.641  66.345  1.00 73.21           C
ANISOU 3691  CG  LEU A 475    11463   7486   8869   -212      1   2587       C
ATOM   3692  CD1 LEU A 475      24.523 -16.566  65.418  1.00 62.51           C
ANISOU 3692  CD1 LEU A 475    10094   6202   7457   -252     39   2361       C
ATOM   3693  CD2 LEU A 475      24.652 -17.419  67.785  1.00 68.72           C
ANISOU 3693  CD2 LEU A 475    10850   7131   8128   -255     -4   2759       C
ATOM   3694  N   LYS A 476      23.756 -21.942  65.565  1.00 84.40           N
ANISOU 3694  N   LYS A 476    12970   8201  10898   -360     42   2852       N
ATOM   3695  CA  LYS A 476      22.672 -22.879  65.285  1.00 86.58           C
ANISOU 3695  CA  LYS A 476    13253   8332  11310   -467     83   2876       C
ATOM   3696  C   LYS A 476      22.558 -23.996  66.315  1.00 87.51           C
ANISOU 3696  C   LYS A 476    13370   8399  11479   -466    109   3084       C
ATOM   3697  O   LYS A 476      21.475 -24.574  66.454  1.00 91.44           O
ANISOU 3697  O   LYS A 476    13870   8853  12021   -576    150   3134       O
ATOM   3698  CB  LYS A 476      22.829 -23.495  63.883  1.00 85.96           C
ANISOU 3698  CB  LYS A 476    13225   7995  11440   -460     73   2709       C
ATOM   3699  CG  LYS A 476      22.207 -22.678  62.747  1.00 81.08           C
ANISOU 3699  CG  LYS A 476    12647   7396  10765   -526     84   2484       C
ATOM   3700  CD  LYS A 476      23.213 -22.395  61.625  1.00 82.76           C
ANISOU 3700  CD  LYS A 476    12914   7508  11022   -421     67   2291       C
ATOM   3701  CE  LYS A 476      22.782 -21.201  60.747  1.00 78.51           C
ANISOU 3701  CE  LYS A 476    12405   7077  10349   -455     92   2088       C
ATOM   3702  NZ  LYS A 476      23.351 -19.867  61.154  1.00 76.03           N
ANISOU 3702  NZ  LYS A 476    12035   7010   9843   -383     92   2052       N
ATOM   3703  N   ASN A 477      23.630 -24.322  67.045  1.00 87.48           N
ANISOU 3703  N   ASN A 477    13383   8400  11453   -353     78   3194       N
ATOM   3704  CA  ASN A 477      23.529 -25.339  68.083  1.00 88.90           C
ANISOU 3704  CA  ASN A 477    13590   8549  11638   -366     74   3378       C
ATOM   3705  C   ASN A 477      23.236 -24.751  69.470  1.00 90.92           C
ANISOU 3705  C   ASN A 477    13799   9088  11658   -392     73   3516       C
ATOM   3706  O   ASN A 477      23.462 -25.427  70.484  1.00 93.26           O
ANISOU 3706  O   ASN A 477    14100   9406  11927   -374     50   3681       O
ATOM   3707  CB  ASN A 477      24.771 -26.260  68.072  1.00 97.73           C
ANISOU 3707  CB  ASN A 477    14757   9485  12890   -247     19   3421       C
ATOM   3708  CG  ASN A 477      26.023 -25.657  68.719  1.00 94.77           C
ANISOU 3708  CG  ASN A 477    14357   9259  12390   -119    -44   3468       C
ATOM   3709  OD1 ASN A 477      25.987 -25.066  69.799  1.00 97.55           O
ANISOU 3709  OD1 ASN A 477    14666   9851  12548   -123    -59   3570       O
ATOM   3710  ND2 ASN A 477      27.162 -25.875  68.065  1.00 89.82           N
ANISOU 3710  ND2 ASN A 477    13755   8487  11885     -4    -85   3391       N
ATOM   3711  N   GLN A 478      22.695 -23.532  69.529  1.00 89.49           N
ANISOU 3711  N   GLN A 478    13567   9125  11309   -437     97   3448       N
ATOM   3712  CA  GLN A 478      22.110 -22.988  70.755  1.00 90.62           C
ANISOU 3712  CA  GLN A 478    13661   9537  11233   -485    115   3550       C
ATOM   3713  C   GLN A 478      20.594 -23.101  70.685  1.00 94.09           C
ANISOU 3713  C   GLN A 478    14078   9995  11676   -631    183   3550       C
ATOM   3714  O   GLN A 478      19.970 -22.506  69.801  1.00 88.62           O
ANISOU 3714  O   GLN A 478    13370   9298  11005   -691    208   3410       O
ATOM   3715  CB  GLN A 478      22.505 -21.521  70.975  1.00 90.10           C
ANISOU 3715  CB  GLN A 478    13549   9720  10964   -438     93   3467       C
ATOM   3716  CG  GLN A 478      23.968 -21.260  71.327  1.00 88.29           C
ANISOU 3716  CG  GLN A 478    13322   9538  10686   -300     20   3487       C
ATOM   3717  CD  GLN A 478      24.699 -22.475  71.885  1.00 90.22           C
ANISOU 3717  CD  GLN A 478    13600   9652  11027   -236    -22   3636       C
ATOM   3718  OE1 GLN A 478      24.260 -23.101  72.854  1.00 94.32           O
ANISOU 3718  OE1 GLN A 478    14113  10223  11500   -280    -12   3786       O
ATOM   3719  NE2 GLN A 478      25.833 -22.808  71.273  1.00 85.83           N
ANISOU 3719  NE2 GLN A 478    13074   8929  10609   -132    -71   3594       N
ATOM   3720  N   MET A 601     -29.788   5.161  51.722  1.00 84.33           N
ANISOU 3720  N   MET A 601     7600  13097  11343  -2286    -71    142       N
ATOM   3721  CA  MET A 601     -28.337   5.040  51.815  1.00 81.44           C
ANISOU 3721  CA  MET A 601     7491  12593  10859  -2243    -50    142       C
ATOM   3722  C   MET A 601     -27.659   5.803  50.676  1.00 77.99           C
ANISOU 3722  C   MET A 601     7171  12062  10398  -2120   -188    102       C
ATOM   3723  O   MET A 601     -28.097   5.733  49.535  1.00 82.37           O
ANISOU 3723  O   MET A 601     7691  12608  10998  -2152   -334     94       O
ATOM   3724  CB  MET A 601     -27.926   3.567  51.794  1.00 78.55           C
ANISOU 3724  CB  MET A 601     7263  12128  10455  -2421    -49    194       C
ATOM   3725  CG  MET A 601     -26.832   3.220  52.786  1.00 84.49           C
ANISOU 3725  CG  MET A 601     8184  12816  11100  -2413     79    226       C
ATOM   3726  SD  MET A 601     -26.958   1.510  53.374  1.00 95.99           S
ANISOU 3726  SD  MET A 601     9676  14233  12562  -2640    150    318       S
ATOM   3727  CE  MET A 601     -27.785   1.725  54.956  1.00 75.74           C
ANISOU 3727  CE  MET A 601     6909  11863  10005  -2645    346    364       C
ATOM   3728  N   LYS A 602     -26.589   6.532  50.986  1.00 77.86           N
ANISOU 3728  N   LYS A 602     7292  11984  10309  -1982   -143     79       N
ATOM   3729  CA  LYS A 602     -25.892   7.353  50.006  1.00 73.11           C
ANISOU 3729  CA  LYS A 602     6796  11296   9685  -1856   -256     52       C
ATOM   3730  C   LYS A 602     -24.448   6.895  49.874  1.00 72.17           C
ANISOU 3730  C   LYS A 602     6936  11032   9454  -1862   -255     61       C
ATOM   3731  O   LYS A 602     -23.864   6.349  50.818  1.00 71.72           O
ANISOU 3731  O   LYS A 602     6968  10947   9334  -1903   -140     78       O
ATOM   3732  CB  LYS A 602     -25.901   8.829  50.392  1.00 71.66           C
ANISOU 3732  CB  LYS A 602     6528  11159   9540  -1667   -216     11       C
ATOM   3733  CG  LYS A 602     -27.165   9.278  51.084  1.00 82.28           C
ANISOU 3733  CG  LYS A 602     7620  12658  10983  -1644   -146     -7       C
ATOM   3734  CD  LYS A 602     -27.010  10.702  51.602  1.00 86.77           C
ANISOU 3734  CD  LYS A 602     8129  13251  11588  -1451    -90    -63       C
ATOM   3735  CE  LYS A 602     -28.053  11.024  52.660  1.00 88.55           C
ANISOU 3735  CE  LYS A 602     8129  13633  11882  -1428     33    -95       C
ATOM   3736  NZ  LYS A 602     -27.479  11.001  54.030  1.00 84.08           N
ANISOU 3736  NZ  LYS A 602     7619  13097  11232  -1406    202   -124       N
ATOM   3737  N   CYS A 603     -23.878   7.135  48.694  1.00 66.34           N
ANISOU 3737  N   CYS A 603     6312  10208   8687  -1817   -383     53       N
ATOM   3738  CA  CYS A 603     -22.491   6.786  48.435  1.00 63.03           C
ANISOU 3738  CA  CYS A 603     6130   9652   8165  -1809   -391     57       C
ATOM   3739  C   CYS A 603     -21.556   7.767  49.138  1.00 60.37           C
ANISOU 3739  C   CYS A 603     5866   9282   7790  -1657   -305     39       C
ATOM   3740  O   CYS A 603     -21.616   8.975  48.899  1.00 60.04           O
ANISOU 3740  O   CYS A 603     5763   9259   7791  -1520   -336     19       O
ATOM   3741  CB  CYS A 603     -22.232   6.769  46.934  1.00 63.73           C
ANISOU 3741  CB  CYS A 603     6304   9681   8231  -1806   -550     53       C
ATOM   3742  SG  CYS A 603     -20.496   6.565  46.514  1.00 53.42           S
ANISOU 3742  SG  CYS A 603     5275   8218   6803  -1766   -560     52       S
ATOM   3743  N   HIS A 604     -20.672   7.242  49.991  1.00 63.19           N
ANISOU 3743  N   HIS A 604     6353   9584   8072  -1683   -203     48       N
ATOM   3744  CA  HIS A 604     -19.809   8.094  50.805  1.00 60.37           C
ANISOU 3744  CA  HIS A 604     6055   9206   7676  -1552   -115     23       C
ATOM   3745  C   HIS A 604     -18.814   8.890  49.972  1.00 60.98           C
ANISOU 3745  C   HIS A 604     6258   9182   7729  -1435   -192     10       C
ATOM   3746  O   HIS A 604     -18.214   9.838  50.493  1.00 59.77           O
ANISOU 3746  O   HIS A 604     6125   9011   7572  -1310   -141    -20       O
ATOM   3747  CB  HIS A 604     -19.054   7.248  51.832  1.00 61.53           C
ANISOU 3747  CB  HIS A 604     6320   9320   7739  -1615     -2     45       C
ATOM   3748  CG  HIS A 604     -19.919   6.252  52.543  1.00 68.87           C
ANISOU 3748  CG  HIS A 604     7154  10331   8684  -1756     69     83       C
ATOM   3749  ND1 HIS A 604     -20.654   6.570  53.666  1.00 71.08           N
ANISOU 3749  ND1 HIS A 604     7277  10744   8985  -1741    183     76       N
ATOM   3750  CD2 HIS A 604     -20.191   4.952  52.272  1.00 67.48           C
ANISOU 3750  CD2 HIS A 604     7007  10122   8512  -1916     44    129       C
ATOM   3751  CE1 HIS A 604     -21.327   5.505  54.066  1.00 72.39           C
ANISOU 3751  CE1 HIS A 604     7382  10961   9164  -1889    228    129       C
ATOM   3752  NE2 HIS A 604     -21.069   4.513  53.234  1.00 69.72           N
ANISOU 3752  NE2 HIS A 604     7153  10515   8823  -1999    143    162       N
ATOM   3753  N   ARG A 605     -18.597   8.510  48.711  1.00 57.92           N
ANISOU 3753  N   ARG A 605     5956   8730   7322  -1475   -312     29       N
ATOM   3754  CA  ARG A 605     -17.641   9.193  47.849  1.00 57.50           C
ANISOU 3754  CA  ARG A 605     6024   8589   7237  -1375   -385     29       C
ATOM   3755  C   ARG A 605     -18.313  10.221  46.947  1.00 57.23           C
ANISOU 3755  C   ARG A 605     5871   8597   7275  -1288   -489     35       C
ATOM   3756  O   ARG A 605     -17.787  11.323  46.756  1.00 57.68           O
ANISOU 3756  O   ARG A 605     5949   8615   7353  -1157   -504     36       O
ATOM   3757  CB  ARG A 605     -16.869   8.177  47.002  1.00 52.77           C
ANISOU 3757  CB  ARG A 605     5602   7896   6553  -1459   -447     46       C
ATOM   3758  CG  ARG A 605     -15.897   8.819  46.028  1.00 54.73           C
ANISOU 3758  CG  ARG A 605     5970   8066   6757  -1364   -520     54       C
ATOM   3759  CD  ARG A 605     -14.739   7.911  45.673  1.00 54.29           C
ANISOU 3759  CD  ARG A 605     6116   7906   6605  -1417   -523     56       C
ATOM   3760  NE  ARG A 605     -15.162   6.874  44.741  1.00 53.21           N
ANISOU 3760  NE  ARG A 605     6003   7771   6444  -1536   -612     51       N
ATOM   3761  CZ  ARG A 605     -14.382   5.919  44.253  1.00 50.07           C
ANISOU 3761  CZ  ARG A 605     5762   7288   5972  -1601   -633     40       C
ATOM   3762  NH1 ARG A 605     -13.088   5.860  44.537  1.00 48.70           N
ANISOU 3762  NH1 ARG A 605     5740   7023   5740  -1555   -575     43       N
ATOM   3763  NH2 ARG A 605     -14.921   4.982  43.478  1.00 53.83           N
ANISOU 3763  NH2 ARG A 605     6239   7774   6441  -1715   -714     19       N
ATOM   3764  N   CYS A 606     -19.464   9.884  46.371  1.00 56.77           N
ANISOU 3764  N   CYS A 606     5686   8618   7265  -1361   -566     45       N
ATOM   3765  CA  CYS A 606     -20.078  10.760  45.386  1.00 59.27           C
ANISOU 3765  CA  CYS A 606     5899   8977   7643  -1286   -683     63       C
ATOM   3766  C   CYS A 606     -21.504  11.170  45.733  1.00 59.28           C
ANISOU 3766  C   CYS A 606     5665   9101   7760  -1277   -681     54       C
ATOM   3767  O   CYS A 606     -22.096  11.964  44.997  1.00 55.37           O
ANISOU 3767  O   CYS A 606     5061   8646   7330  -1204   -778     75       O
ATOM   3768  CB  CYS A 606     -20.052  10.101  43.998  1.00 58.41           C
ANISOU 3768  CB  CYS A 606     5866   8853   7473  -1363   -821     85       C
ATOM   3769  SG  CYS A 606     -21.365   8.893  43.764  1.00 57.29           S
ANISOU 3769  SG  CYS A 606     5603   8803   7362  -1540   -876     72       S
ATOM   3770  N   GLY A 607     -22.066  10.672  46.827  1.00 62.77           N
ANISOU 3770  N   GLY A 607     6016   9605   8227  -1345   -573     31       N
ATOM   3771  CA  GLY A 607     -23.386  11.113  47.239  1.00 64.65           C
ANISOU 3771  CA  GLY A 607     6021   9966   8578  -1327   -555     19       C
ATOM   3772  C   GLY A 607     -24.544  10.565  46.431  1.00 67.34           C
ANISOU 3772  C   GLY A 607     6233  10389   8967  -1429   -665     38       C
ATOM   3773  O   GLY A 607     -25.676  11.023  46.605  1.00 62.20           O
ANISOU 3773  O   GLY A 607     5373   9843   8419  -1403   -669     32       O
ATOM   3774  N   SER A 608     -24.303   9.618  45.537  1.00 65.98           N
ANISOU 3774  N   SER A 608     6171  10172   8726  -1542   -757     54       N
ATOM   3775  CA  SER A 608     -25.404   9.018  44.808  1.00 69.21           C
ANISOU 3775  CA  SER A 608     6456  10660   9178  -1653   -864     61       C
ATOM   3776  C   SER A 608     -26.235   8.149  45.748  1.00 70.99           C
ANISOU 3776  C   SER A 608     6562  10957   9454  -1786   -770     52       C
ATOM   3777  O   SER A 608     -25.729   7.579  46.716  1.00 67.51           O
ANISOU 3777  O   SER A 608     6202  10476   8971  -1836   -643     51       O
ATOM   3778  CB  SER A 608     -24.875   8.195  43.632  1.00 65.04           C
ANISOU 3778  CB  SER A 608     6087  10066   8558  -1740   -985     63       C
ATOM   3779  OG  SER A 608     -25.918   7.501  42.989  1.00 73.66           O
ANISOU 3779  OG  SER A 608     7065  11233   9690  -1864  -1088     55       O
ATOM   3780  N   ASP A 609     -27.532   8.079  45.480  1.00 76.44           N
ANISOU 3780  N   ASP A 609     7049  11758  10237  -1840   -831     55       N
ATOM   3781  CA  ASP A 609     -28.359   7.080  46.132  1.00 80.77           C
ANISOU 3781  CA  ASP A 609     7486  12371  10834  -1998   -766     57       C
ATOM   3782  C   ASP A 609     -28.502   5.824  45.279  1.00 80.22           C
ANISOU 3782  C   ASP A 609     7477  12263  10740  -2171   -875     54       C
ATOM   3783  O   ASP A 609     -29.288   4.944  45.616  1.00 77.93           O
ANISOU 3783  O   ASP A 609     7081  12020  10509  -2319   -849     60       O
ATOM   3784  CB  ASP A 609     -29.723   7.687  46.511  1.00 84.96           C
ANISOU 3784  CB  ASP A 609     7739  13051  11492  -1964   -747     56       C
ATOM   3785  CG  ASP A 609     -30.680   7.814  45.336  1.00 87.65           C
ANISOU 3785  CG  ASP A 609     7939  13463  11900  -1985   -921     59       C
ATOM   3786  OD1 ASP A 609     -31.294   6.795  44.940  1.00 97.91           O
ANISOU 3786  OD1 ASP A 609     9189  14790  13222  -2149   -986     59       O
ATOM   3787  OD2 ASP A 609     -30.812   8.943  44.806  1.00 91.44           O
ANISOU 3787  OD2 ASP A 609     8357  13970  12415  -1837   -997     64       O
ATOM   3788  N   ASN A 610     -27.773   5.743  44.162  1.00 77.46           N
ANISOU 3788  N   ASN A 610     7288  11832  10309  -2156   -996     42       N
ATOM   3789  CA  ASN A 610     -27.644   4.529  43.357  1.00 77.01           C
ANISOU 3789  CA  ASN A 610     7335  11717  10210  -2309  -1091     19       C
ATOM   3790  C   ASN A 610     -26.725   3.530  44.030  1.00 75.92           C
ANISOU 3790  C   ASN A 610     7376  11457  10014  -2395   -984     19       C
ATOM   3791  O   ASN A 610     -25.705   3.138  43.462  1.00 75.75           O
ANISOU 3791  O   ASN A 610     7556  11326   9900  -2398  -1024     -1       O
ATOM   3792  CB  ASN A 610     -27.061   4.822  41.970  1.00 82.73           C
ANISOU 3792  CB  ASN A 610     8184  12403  10847  -2248  -1244      1       C
ATOM   3793  CG  ASN A 610     -28.076   5.265  40.945  1.00 88.61           C
ANISOU 3793  CG  ASN A 610     8768  13263  11637  -2235  -1405     -1       C
ATOM   3794  OD1 ASN A 610     -28.046   6.411  40.487  1.00 92.70           O
ANISOU 3794  OD1 ASN A 610     9250  13823  12150  -2087  -1461     27       O
ATOM   3795  ND2 ASN A 610     -28.908   4.330  40.485  1.00 89.49           N
ANISOU 3795  ND2 ASN A 610     8795  13419  11789  -2393  -1493    -33       N
ATOM   3796  N   VAL A 611     -27.086   3.087  45.216  1.00 74.87           N
ANISOU 3796  N   VAL A 611     7167  11347   9934  -2466   -849     45       N
ATOM   3797  CA  VAL A 611     -26.277   2.131  45.951  1.00 72.45           C
ANISOU 3797  CA  VAL A 611     7016  10931   9581  -2548   -742     63       C
ATOM   3798  C   VAL A 611     -27.089   0.857  46.053  1.00 72.03           C
ANISOU 3798  C   VAL A 611     6882  10881   9607  -2752   -750     72       C
ATOM   3799  O   VAL A 611     -28.296   0.900  46.318  1.00 77.10           O
ANISOU 3799  O   VAL A 611     7308  11640  10346  -2808   -743     87       O
ATOM   3800  CB  VAL A 611     -25.867   2.650  47.344  1.00 73.97           C
ANISOU 3800  CB  VAL A 611     7210  11144   9753  -2460   -567     99       C
ATOM   3801  CG1 VAL A 611     -25.080   1.575  48.096  1.00 69.98           C
ANISOU 3801  CG1 VAL A 611     6857  10533   9200  -2555   -465    131       C
ATOM   3802  CG2 VAL A 611     -25.003   3.899  47.213  1.00 67.83           C
ANISOU 3802  CG2 VAL A 611     6519  10345   8910  -2265   -566     82       C
ATOM   3803  N   ARG A 612     -26.451  -0.263  45.762  1.00 68.47           N
ANISOU 3803  N   ARG A 612     6594  10298   9123  -2861   -775     60       N
ATOM   3804  CA  ARG A 612     -27.105  -1.550  45.867  1.00 72.23           C
ANISOU 3804  CA  ARG A 612     7014  10744   9686  -3062   -781     69       C
ATOM   3805  C   ARG A 612     -26.220  -2.464  46.695  1.00 71.50           C
ANISOU 3805  C   ARG A 612     7081  10520   9564  -3127   -665    114       C
ATOM   3806  O   ARG A 612     -25.031  -2.198  46.889  1.00 70.69           O
ANISOU 3806  O   ARG A 612     7155  10339   9364  -3022   -617    117       O
ATOM   3807  CB  ARG A 612     -27.374  -2.174  44.494  1.00 72.53           C
ANISOU 3807  CB  ARG A 612     7076  10741   9741  -3158   -961     -4       C
ATOM   3808  CG  ARG A 612     -26.116  -2.545  43.754  1.00 74.83           C
ANISOU 3808  CG  ARG A 612     7615  10888   9928  -3129  -1019    -55       C
ATOM   3809  CD  ARG A 612     -26.405  -3.143  42.396  1.00 74.75           C
ANISOU 3809  CD  ARG A 612     7624  10855   9923  -3220  -1196   -142       C
ATOM   3810  NE  ARG A 612     -25.159  -3.488  41.720  1.00 82.86           N
ANISOU 3810  NE  ARG A 612     8888  11751  10843  -3184  -1238   -197       N
ATOM   3811  CZ  ARG A 612     -24.512  -4.634  41.883  1.00 77.81           C
ANISOU 3811  CZ  ARG A 612     8395  10956  10212  -3282  -1204   -215       C
ATOM   3812  NH1 ARG A 612     -24.983  -5.588  42.667  1.00 76.38           N
ANISOU 3812  NH1 ARG A 612     8154  10723  10143  -3432  -1134   -175       N
ATOM   3813  NH2 ARG A 612     -23.367  -4.831  41.237  1.00 77.11           N
ANISOU 3813  NH2 ARG A 612     8514  10763  10023  -3228  -1241   -269       N
ATOM   3814  N   LYS A 613     -26.823  -3.537  47.189  1.00 70.58           N
ANISOU 3814  N   LYS A 613     6893  10383   9541  -3300   -622    155       N
ATOM   3815  CA  LYS A 613     -26.089  -4.571  47.898  1.00 72.40           C
ANISOU 3815  CA  LYS A 613     7266  10478   9765  -3386   -528    209       C
ATOM   3816  C   LYS A 613     -25.331  -5.438  46.902  1.00 73.18           C
ANISOU 3816  C   LYS A 613     7555  10405   9844  -3444   -639    142       C
ATOM   3817  O   LYS A 613     -25.918  -5.941  45.939  1.00 75.65           O
ANISOU 3817  O   LYS A 613     7823  10701  10219  -3546   -771     75       O
ATOM   3818  CB  LYS A 613     -27.048  -5.422  48.730  1.00 68.37           C
ANISOU 3818  CB  LYS A 613     6602  10001   9373  -3558   -447    288       C
ATOM   3819  CG  LYS A 613     -26.406  -6.593  49.455  1.00 71.51           C
ANISOU 3819  CG  LYS A 613     7131  10254   9785  -3665   -357    363       C
ATOM   3820  CD  LYS A 613     -27.361  -7.154  50.502  1.00 74.35           C
ANISOU 3820  CD  LYS A 613     7316  10687  10246  -3805   -242    471       C
ATOM   3821  CE  LYS A 613     -28.031  -8.433  50.022  1.00 78.52           C
ANISOU 3821  CE  LYS A 613     7794  11118  10922  -4022   -321    469       C
ATOM   3822  NZ  LYS A 613     -28.589  -9.225  51.155  1.00 86.84           N
ANISOU 3822  NZ  LYS A 613     8742  12187  12067  -4170   -188    604       N
ATOM   3823  N   MET A 614     -24.024  -5.610  47.130  1.00 72.94           N
ANISOU 3823  N   MET A 614     7734  10251   9728  -3378   -587    153       N
ATOM   3824  CA  MET A 614     -23.219  -6.465  46.265  1.00 72.03           C
ANISOU 3824  CA  MET A 614     7807   9968   9594  -3424   -676     86       C
ATOM   3825  C   MET A 614     -23.270  -7.928  46.707  1.00 72.82           C
ANISOU 3825  C   MET A 614     7943   9929   9796  -3603   -638    129       C
ATOM   3826  O   MET A 614     -23.575  -8.805  45.895  1.00 75.16           O
ANISOU 3826  O   MET A 614     8252  10140  10167  -3729   -746     60       O
ATOM   3827  CB  MET A 614     -21.770  -5.963  46.213  1.00 70.80           C
ANISOU 3827  CB  MET A 614     7854   9741   9306  -3265   -646     73       C
ATOM   3828  CG  MET A 614     -20.760  -7.020  45.753  1.00 72.00           C
ANISOU 3828  CG  MET A 614     8213   9700   9445  -3314   -681     32       C
ATOM   3829  SD  MET A 614     -19.074  -6.406  45.442  1.00 69.03           S
ANISOU 3829  SD  MET A 614     8064   9250   8915  -3127   -669      0       S
ATOM   3830  CE  MET A 614     -19.327  -4.646  45.259  1.00 62.55           C
ANISOU 3830  CE  MET A 614     7140   8612   8015  -2952   -682     -5       C
ATOM   3831  N   VAL A 615     -22.999  -8.208  47.988  1.00 72.60           N
ANISOU 3831  N   VAL A 615     7927   9879   9776  -3619   -489    244       N
ATOM   3832  CA  VAL A 615     -23.055  -9.565  48.535  1.00 74.54           C
ANISOU 3832  CA  VAL A 615     8200   9995  10129  -3787   -440    314       C
ATOM   3833  C   VAL A 615     -23.456  -9.504  50.004  1.00 74.05           C
ANISOU 3833  C   VAL A 615     8024  10025  10084  -3813   -277    459       C
ATOM   3834  O   VAL A 615     -23.356  -8.462  50.657  1.00 72.22           O
ANISOU 3834  O   VAL A 615     7748   9931   9761  -3679   -192    492       O
ATOM   3835  CB  VAL A 615     -21.712 -10.338  48.417  1.00 73.46           C
ANISOU 3835  CB  VAL A 615     8301   9651   9959  -3773   -439    305       C
ATOM   3836  CG1 VAL A 615     -21.384 -10.690  46.965  1.00 71.95           C
ANISOU 3836  CG1 VAL A 615     8219   9353   9767  -3784   -596    157       C
ATOM   3837  CG2 VAL A 615     -20.562  -9.538  49.069  1.00 67.14           C
ANISOU 3837  CG2 VAL A 615     7622   8873   9016  -3593   -343    348       C
ATOM   3838  N   ASP A 616     -23.922 -10.641  50.515  1.00 75.99           N
ANISOU 3838  N   ASP A 616     8222  10198  10453  -3988   -234    543       N
ATOM   3839  CA  ASP A 616     -23.981 -10.925  51.941  1.00 75.58           C
ANISOU 3839  CA  ASP A 616     8125  10185  10409  -4030    -71    702       C
ATOM   3840  C   ASP A 616     -22.727 -11.668  52.371  1.00 75.10           C
ANISOU 3840  C   ASP A 616     8274   9946  10315  -4019    -21    765       C
ATOM   3841  O   ASP A 616     -22.037 -12.288  51.561  1.00 75.77           O
ANISOU 3841  O   ASP A 616     8514   9851  10423  -4035   -113    691       O
ATOM   3842  CB  ASP A 616     -25.190 -11.789  52.295  1.00 76.65           C
ANISOU 3842  CB  ASP A 616     8083  10336  10704  -4236    -46    783       C
ATOM   3843  CG  ASP A 616     -26.493 -11.053  52.171  1.00 82.20           C
ANISOU 3843  CG  ASP A 616     8547  11241  11444  -4248    -61    753       C
ATOM   3844  OD1 ASP A 616     -26.639  -9.987  52.809  1.00 84.67           O
ANISOU 3844  OD1 ASP A 616     8775  11734  11663  -4121     27    778       O
ATOM   3845  OD2 ASP A 616     -27.382 -11.551  51.445  1.00 84.24           O
ANISOU 3845  OD2 ASP A 616     8696  11479  11831  -4384   -164    701       O
ATOM   3846  N   SER A 617     -22.454 -11.629  53.665  1.00 74.22           N
ANISOU 3846  N   SER A 617     8161   9892  10148  -3994    127    902       N
ATOM   3847  CA  SER A 617     -21.382 -12.448  54.207  1.00 72.00           C
ANISOU 3847  CA  SER A 617     8055   9449   9853  -4003    181    991       C
ATOM   3848  C   SER A 617     -21.668 -13.909  53.871  1.00 72.66           C
ANISOU 3848  C   SER A 617     8157   9337  10113  -4200    128   1023       C
ATOM   3849  O   SER A 617     -22.783 -14.383  54.129  1.00 72.86           O
ANISOU 3849  O   SER A 617     8017   9405  10259  -4355    150   1088       O
ATOM   3850  CB  SER A 617     -21.283 -12.244  55.712  1.00 73.65           C
ANISOU 3850  CB  SER A 617     8222   9780   9983  -3972    348   1150       C
ATOM   3851  OG  SER A 617     -22.578 -12.023  56.252  1.00 82.72           O
ANISOU 3851  OG  SER A 617     9145  11109  11177  -4053    416   1210       O
ATOM   3852  N   PRO A 618     -20.737 -14.633  53.247  1.00 72.18           N
ANISOU 3852  N   PRO A 618     8283   9058  10084  -4201     54    969       N
ATOM   3853  CA  PRO A 618     -21.013 -16.041  52.919  1.00 67.50           C
ANISOU 3853  CA  PRO A 618     7707   8261   9677  -4389     -0    987       C
ATOM   3854  C   PRO A 618     -21.148 -16.934  54.141  1.00 76.24           C
ANISOU 3854  C   PRO A 618     8782   9316  10868  -4509    122   1195       C
ATOM   3855  O   PRO A 618     -21.749 -18.014  54.034  1.00 77.72           O
ANISOU 3855  O   PRO A 618     8920   9374  11235  -4662     97   1227       O
ATOM   3856  CB  PRO A 618     -19.814 -16.456  52.060  1.00 69.89           C
ANISOU 3856  CB  PRO A 618     8231   8358   9967  -4322    -91    874       C
ATOM   3857  CG  PRO A 618     -19.129 -15.189  51.669  1.00 70.60           C
ANISOU 3857  CG  PRO A 618     8390   8563   9872  -4116   -111    773       C
ATOM   3858  CD  PRO A 618     -19.449 -14.169  52.706  1.00 70.31           C
ANISOU 3858  CD  PRO A 618     8238   8752   9725  -4033      8    871       C
ATOM   3859  N   VAL A 619     -20.607 -16.539  55.295  1.00 74.77           N
ANISOU 3859  N   VAL A 619     8625   9225  10558  -4415    253   1329       N
ATOM   3860  CA  VAL A 619     -20.828 -17.255  56.548  1.00 76.25           C
ANISOU 3860  CA  VAL A 619     8763   9413  10798  -4506    382   1542       C
ATOM   3861  C   VAL A 619     -21.600 -16.344  57.489  1.00 75.57           C
ANISOU 3861  C   VAL A 619     8496   9609  10608  -4480    502   1625       C
ATOM   3862  O   VAL A 619     -21.159 -15.227  57.787  1.00 74.62           O
ANISOU 3862  O   VAL A 619     8395   9645  10313  -4315    544   1587       O
ATOM   3863  CB  VAL A 619     -19.514 -17.721  57.207  1.00 76.16           C
ANISOU 3863  CB  VAL A 619     8939   9271  10727  -4426    440   1646       C
ATOM   3864  CG1 VAL A 619     -19.823 -18.534  58.465  1.00 78.91           C
ANISOU 3864  CG1 VAL A 619     9234   9616  11134  -4463    567   1849       C
ATOM   3865  CG2 VAL A 619     -18.681 -18.546  56.246  1.00 76.63           C
ANISOU 3865  CG2 VAL A 619     9178   9055  10883  -4432    324   1546       C
ATOM   3866  N   GLY A 620     -22.737 -16.831  57.970  1.00 79.18           N
ANISOU 3866  N   GLY A 620     8789  10119  11176  -4573    560   1708       N
ATOM   3867  CA  GLY A 620     -23.482 -16.106  58.971  1.00 84.20           C
ANISOU 3867  CA  GLY A 620     9254  11016  11722  -4546    690   1796       C
ATOM   3868  C   GLY A 620     -24.120 -14.843  58.419  1.00 85.61           C
ANISOU 3868  C   GLY A 620     9292  11401  11836  -4512    647   1665       C
ATOM   3869  O   GLY A 620     -24.326 -14.678  57.217  1.00 82.04           O
ANISOU 3869  O   GLY A 620     8837  10891  11443  -4531    510   1511       O
ATOM   3870  N   ASP A 621     -24.461 -13.953  59.341  1.00 88.21           N
ANISOU 3870  N   ASP A 621     9501  11977  12039  -4440    770   1721       N
ATOM   3871  CA  ASP A 621     -25.032 -12.651  59.036  1.00 84.38           C
ANISOU 3871  CA  ASP A 621     8885  11694  11480  -4333    754   1594       C
ATOM   3872  C   ASP A 621     -24.135 -11.551  59.587  1.00 84.79           C
ANISOU 3872  C   ASP A 621     9027  11861  11329  -4119    818   1560       C
ATOM   3873  O   ASP A 621     -24.599 -10.583  60.193  1.00 85.37           O
ANISOU 3873  O   ASP A 621     8970  12157  11312  -4031    904   1550       O
ATOM   3874  CB  ASP A 621     -26.451 -12.533  59.585  1.00 83.18           C
ANISOU 3874  CB  ASP A 621     8474  11740  11391  -4429    840   1661       C
ATOM   3875  CG  ASP A 621     -27.474 -13.273  58.735  1.00 95.75           C
ANISOU 3875  CG  ASP A 621     9964  13228  13188  -4567    737   1612       C
ATOM   3876  OD1 ASP A 621     -27.719 -14.481  58.987  1.00 97.34           O
ANISOU 3876  OD1 ASP A 621    10183  13284  13520  -4671    757   1706       O
ATOM   3877  OD2 ASP A 621     -28.034 -12.643  57.808  1.00100.80           O
ANISOU 3877  OD2 ASP A 621    10504  13936  13862  -4568    633   1478       O
ATOM   3878  N   ALA A 622     -22.822 -11.711  59.388  1.00 85.08           N
ANISOU 3878  N   ALA A 622     9286  11740  11300  -4033    776   1537       N
ATOM   3879  CA  ALA A 622     -21.848 -10.792  59.967  1.00 79.26           C
ANISOU 3879  CA  ALA A 622     8649  11089  10378  -3842    835   1516       C
ATOM   3880  C   ALA A 622     -21.851  -9.429  59.286  1.00 78.59           C
ANISOU 3880  C   ALA A 622     8538  11100  10224  -3678    770   1340       C
ATOM   3881  O   ALA A 622     -21.640  -8.412  59.958  1.00 82.13           O
ANISOU 3881  O   ALA A 622     8958  11709  10540  -3539    847   1320       O
ATOM   3882  CB  ALA A 622     -20.449 -11.400  59.900  1.00 79.43           C
ANISOU 3882  CB  ALA A 622     8907  10907  10365  -3803    802   1545       C
ATOM   3883  N   TRP A 623     -22.065  -9.378  57.971  1.00 75.10           N
ANISOU 3883  N   TRP A 623     8105  10562   9867  -3691    626   1211       N
ATOM   3884  CA  TRP A 623     -21.973  -8.115  57.245  1.00 72.48           C
ANISOU 3884  CA  TRP A 623     7765  10301   9472  -3533    554   1058       C
ATOM   3885  C   TRP A 623     -22.561  -8.273  55.854  1.00 69.47           C
ANISOU 3885  C   TRP A 623     7346   9844   9205  -3597    401    948       C
ATOM   3886  O   TRP A 623     -22.921  -9.372  55.424  1.00 68.77           O
ANISOU 3886  O   TRP A 623     7256   9632   9240  -3758    346    973       O
ATOM   3887  CB  TRP A 623     -20.528  -7.612  57.135  1.00 69.85           C
ANISOU 3887  CB  TRP A 623     7636   9889   9015  -3370    534   1004       C
ATOM   3888  CG  TRP A 623     -19.541  -8.689  56.763  1.00 69.40           C
ANISOU 3888  CG  TRP A 623     7778   9604   8988  -3423    481   1032       C
ATOM   3889  CD1 TRP A 623     -18.683  -9.337  57.605  1.00 67.99           C
ANISOU 3889  CD1 TRP A 623     7719   9350   8764  -3431    557   1145       C
ATOM   3890  CD2 TRP A 623     -19.295  -9.226  55.454  1.00 67.40           C
ANISOU 3890  CD2 TRP A 623     7622   9172   8813  -3466    340    939       C
ATOM   3891  NE1 TRP A 623     -17.927 -10.248  56.905  1.00 65.16           N
ANISOU 3891  NE1 TRP A 623     7525   8768   8466  -3475    474   1130       N
ATOM   3892  CE2 TRP A 623     -18.280 -10.198  55.584  1.00 65.02           C
ANISOU 3892  CE2 TRP A 623     7498   8685   8521  -3497    343    997       C
ATOM   3893  CE3 TRP A 623     -19.831  -8.979  54.191  1.00 61.86           C
ANISOU 3893  CE3 TRP A 623     6876   8458   8172  -3479    211    812       C
ATOM   3894  CZ2 TRP A 623     -17.803 -10.927  54.503  1.00 59.70           C
ANISOU 3894  CZ2 TRP A 623     6954   7812   7918  -3539    228    921       C
ATOM   3895  CZ3 TRP A 623     -19.350  -9.701  53.123  1.00 64.60           C
ANISOU 3895  CZ3 TRP A 623     7353   8619   8573  -3524     95    738       C
ATOM   3896  CH2 TRP A 623     -18.344 -10.662  53.284  1.00 63.02           C
ANISOU 3896  CH2 TRP A 623     7328   8234   8384  -3552    107    787       C
ATOM   3897  N   GLU A 624     -22.646  -7.138  55.159  1.00 69.95           N
ANISOU 3897  N   GLU A 624     7374   9982   9223  -3467    330    825       N
ATOM   3898  CA  GLU A 624     -22.995  -7.060  53.747  1.00 70.76           C
ANISOU 3898  CA  GLU A 624     7465  10029   9392  -3483    172    706       C
ATOM   3899  C   GLU A 624     -22.083  -6.039  53.084  1.00 70.22           C
ANISOU 3899  C   GLU A 624     7520   9944   9217  -3298    106    602       C
ATOM   3900  O   GLU A 624     -21.427  -5.231  53.749  1.00 68.64           O
ANISOU 3900  O   GLU A 624     7366   9805   8911  -3158    185    613       O
ATOM   3901  CB  GLU A 624     -24.464  -6.669  53.543  1.00 72.39           C
ANISOU 3901  CB  GLU A 624     7429  10391   9684  -3538    148    683       C
ATOM   3902  CG  GLU A 624     -24.929  -5.599  54.505  1.00 71.11           C
ANISOU 3902  CG  GLU A 624     7119  10437   9464  -3434    267    709       C
ATOM   3903  CD  GLU A 624     -26.402  -5.690  54.812  1.00 78.92           C
ANISOU 3903  CD  GLU A 624     7857  11572  10558  -3543    305    748       C
ATOM   3904  OE1 GLU A 624     -26.780  -5.391  55.969  1.00 84.17           O
ANISOU 3904  OE1 GLU A 624     8407  12385  11188  -3526    449    820       O
ATOM   3905  OE2 GLU A 624     -27.180  -6.046  53.893  1.00 81.61           O
ANISOU 3905  OE2 GLU A 624     8110  11888  11009  -3644    189    702       O
ATOM   3906  N   VAL A 625     -22.032  -6.080  51.760  1.00 70.89           N
ANISOU 3906  N   VAL A 625     7657   9949   9330  -3300    -40    502       N
ATOM   3907  CA  VAL A 625     -21.182  -5.169  51.007  1.00 67.55           C
ANISOU 3907  CA  VAL A 625     7349   9505   8811  -3137   -111    412       C
ATOM   3908  C   VAL A 625     -22.059  -4.370  50.057  1.00 66.44           C
ANISOU 3908  C   VAL A 625     7073   9468   8701  -3101   -219    330       C
ATOM   3909  O   VAL A 625     -22.821  -4.947  49.273  1.00 66.10           O
ANISOU 3909  O   VAL A 625     6962   9408   8744  -3219   -319    293       O
ATOM   3910  CB  VAL A 625     -20.077  -5.916  50.240  1.00 66.60           C
ANISOU 3910  CB  VAL A 625     7446   9192   8667  -3148   -185    370       C
ATOM   3911  CG1 VAL A 625     -19.190  -4.911  49.482  1.00 59.98           C
ANISOU 3911  CG1 VAL A 625     6718   8348   7725  -2976   -248    288       C
ATOM   3912  CG2 VAL A 625     -19.266  -6.774  51.183  1.00 57.48           C
ANISOU 3912  CG2 VAL A 625     6412   7927   7499  -3189    -84    462       C
ATOM   3913  N   TYR A 626     -21.947  -3.048  50.131  1.00 65.08           N
ANISOU 3913  N   TYR A 626     6862   9401   8465  -2938   -204    302       N
ATOM   3914  CA  TYR A 626     -22.688  -2.142  49.270  1.00 64.92           C
ANISOU 3914  CA  TYR A 626     6717   9480   8468  -2876   -305    236       C
ATOM   3915  C   TYR A 626     -21.760  -1.574  48.209  1.00 66.50           C
ANISOU 3915  C   TYR A 626     7067   9612   8589  -2756   -406    167       C
ATOM   3916  O   TYR A 626     -20.552  -1.445  48.425  1.00 64.56           O
ANISOU 3916  O   TYR A 626     6989   9283   8260  -2671   -363    171       O
ATOM   3917  CB  TYR A 626     -23.327  -1.001  50.071  1.00 66.66           C
ANISOU 3917  CB  TYR A 626     6765   9869   8694  -2775   -219    254       C
ATOM   3918  CG  TYR A 626     -24.223  -1.492  51.185  1.00 72.19           C
ANISOU 3918  CG  TYR A 626     7309  10660   9457  -2883   -102    327       C
ATOM   3919  CD1 TYR A 626     -25.424  -2.147  50.902  1.00 69.43           C
ANISOU 3919  CD1 TYR A 626     6803  10356   9221  -3035   -147    339       C
ATOM   3920  CD2 TYR A 626     -23.861  -1.318  52.523  1.00 68.84           C
ANISOU 3920  CD2 TYR A 626     6893  10286   8977  -2838     55    386       C
ATOM   3921  CE1 TYR A 626     -26.238  -2.612  51.922  1.00 71.37           C
ANISOU 3921  CE1 TYR A 626     6900  10689   9527  -3141    -33    416       C
ATOM   3922  CE2 TYR A 626     -24.664  -1.781  53.550  1.00 69.92           C
ANISOU 3922  CE2 TYR A 626     6888  10521   9159  -2939    170    463       C
ATOM   3923  CZ  TYR A 626     -25.852  -2.425  53.245  1.00 75.56           C
ANISOU 3923  CZ  TYR A 626     7445  11275   9990  -3090    129    482       C
ATOM   3924  OH  TYR A 626     -26.655  -2.878  54.267  1.00 77.15           O
ANISOU 3924  OH  TYR A 626     7496  11579  10237  -3194    251    567       O
ATOM   3925  N   VAL A 627     -22.335  -1.243  47.053  1.00 69.59           N
ANISOU 3925  N   VAL A 627     7392  10044   9003  -2751   -542    108       N
ATOM   3926  CA  VAL A 627     -21.579  -0.691  45.933  1.00 66.52           C
ANISOU 3926  CA  VAL A 627     7127   9612   8537  -2644   -647     51       C
ATOM   3927  C   VAL A 627     -22.405   0.389  45.236  1.00 69.58           C
ANISOU 3927  C   VAL A 627     7364  10128   8947  -2564   -739     25       C
ATOM   3928  O   VAL A 627     -23.623   0.251  45.060  1.00 63.19           O
ANISOU 3928  O   VAL A 627     6379   9409   8222  -2645   -789     21       O
ATOM   3929  CB  VAL A 627     -21.163  -1.786  44.926  1.00 66.99           C
ANISOU 3929  CB  VAL A 627     7326   9548   8580  -2745   -749     -3       C
ATOM   3930  CG1 VAL A 627     -22.394  -2.467  44.314  1.00 69.10           C
ANISOU 3930  CG1 VAL A 627     7457   9859   8940  -2896   -851    -37       C
ATOM   3931  CG2 VAL A 627     -20.236  -1.212  43.835  1.00 58.52           C
ANISOU 3931  CG2 VAL A 627     6395   8436   7403  -2626   -838    -55       C
ATOM   3932  N   CYS A 628     -21.727   1.461  44.824  1.00 65.90           N
ANISOU 3932  N   CYS A 628     6963   9665   8411  -2405   -765     14       N
ATOM   3933  CA  CYS A 628     -22.353   2.557  44.103  1.00 67.44           C
ANISOU 3933  CA  CYS A 628     7036   9964   8624  -2309   -858      3       C
ATOM   3934  C   CYS A 628     -22.350   2.224  42.609  1.00 71.39           C
ANISOU 3934  C   CYS A 628     7595  10447   9083  -2348  -1022    -44       C
ATOM   3935  O   CYS A 628     -21.286   1.930  42.047  1.00 69.06           O
ANISOU 3935  O   CYS A 628     7488  10055   8698  -2329  -1050    -68       O
ATOM   3936  CB  CYS A 628     -21.593   3.857  44.399  1.00 64.88           C
ANISOU 3936  CB  CYS A 628     6756   9639   8255  -2123   -805     21       C
ATOM   3937  SG  CYS A 628     -22.089   5.297  43.406  1.00 65.82           S
ANISOU 3937  SG  CYS A 628     6762   9852   8395  -1980   -926     23       S
ATOM   3938  N   GLU A 629     -23.545   2.169  41.999  1.00 78.53           N
ANISOU 3938  N   GLU A 629     8337  11450  10050  -2413  -1129    -61       N
ATOM   3939  CA  GLU A 629     -23.748   2.132  40.546  1.00 82.78           C
ANISOU 3939  CA  GLU A 629     8888  12020  10544  -2426  -1300   -105       C
ATOM   3940  C   GLU A 629     -22.827   3.063  39.800  1.00 82.71           C
ANISOU 3940  C   GLU A 629     8998  11997  10431  -2272  -1348    -95       C
ATOM   3941  O   GLU A 629     -22.256   2.734  38.761  1.00 83.28           O
ANISOU 3941  O   GLU A 629     9201  12033  10410  -2282  -1439   -134       O
ATOM   3942  CB  GLU A 629     -25.200   2.507  40.232  1.00 84.12           C
ANISOU 3942  CB  GLU A 629     8822  12336  10805  -2452  -1390   -100       C
ATOM   3943  CG  GLU A 629     -26.172   1.412  39.823  1.00 91.50           C
ANISOU 3943  CG  GLU A 629     9662  13302  11804  -2635  -1478   -146       C
ATOM   3944  CD  GLU A 629     -26.617   1.450  38.321  1.00100.90           C
ANISOU 3944  CD  GLU A 629    10820  14566  12949  -2651  -1678   -196       C
ATOM   3945  OE1 GLU A 629     -26.780   1.877  37.155  1.00102.38           O
ANISOU 3945  OE1 GLU A 629    10996  14829  13076  -2604  -1825   -214       O
ATOM   3946  OE2 GLU A 629     -25.773   2.358  38.240  1.00100.23           O
ANISOU 3946  OE2 GLU A 629    10834  14463  12787  -2496  -1648   -161       O
ATOM   3947  N   LYS A 630     -22.734   4.271  40.341  1.00 73.35           N
ANISOU 3947  N   LYS A 630     7755  10847   9269  -2128  -1283    -44       N
ATOM   3948  CA  LYS A 630     -22.308   5.448  39.599  1.00 71.87           C
ANISOU 3948  CA  LYS A 630     7596  10684   9028  -1974  -1348    -14       C
ATOM   3949  C   LYS A 630     -20.796   5.645  39.604  1.00 69.39           C
ANISOU 3949  C   LYS A 630     7494  10257   8615  -1890  -1288     -6       C
ATOM   3950  O   LYS A 630     -20.231   5.948  38.549  1.00 69.78           O
ANISOU 3950  O   LYS A 630     7637  10301   8576  -1833  -1375     -2       O
ATOM   3951  CB  LYS A 630     -23.011   6.684  40.164  1.00 70.17           C
ANISOU 3951  CB  LYS A 630     7198  10552   8910  -1859  -1313     33       C
ATOM   3952  CG  LYS A 630     -22.716   7.953  39.437  1.00 69.65           C
ANISOU 3952  CG  LYS A 630     7135  10509   8821  -1702  -1384     78       C
ATOM   3953  CD  LYS A 630     -22.789   9.110  40.404  1.00 73.14           C
ANISOU 3953  CD  LYS A 630     7481  10956   9351  -1569  -1283    110       C
ATOM   3954  CE  LYS A 630     -23.829  10.127  39.980  1.00 69.78           C
ANISOU 3954  CE  LYS A 630     6858  10637   9019  -1483  -1372    148       C
ATOM   3955  NZ  LYS A 630     -23.482  11.396  40.640  1.00 71.46           N
ANISOU 3955  NZ  LYS A 630     7040  10815   9295  -1321  -1291    175       N
ATOM   3956  N   CYS A 631     -20.109   5.439  40.739  1.00 65.10           N
ANISOU 3956  N   CYS A 631     7026   9630   8077  -1884  -1145     -2       N
ATOM   3957  CA  CYS A 631     -18.656   5.607  40.781  1.00 59.13           C
ANISOU 3957  CA  CYS A 631     6463   8768   7234  -1807  -1088      4       C
ATOM   3958  C   CYS A 631     -17.883   4.367  41.213  1.00 55.64           C
ANISOU 3958  C   CYS A 631     6175   8216   6750  -1905  -1018    -27       C
ATOM   3959  O   CYS A 631     -16.652   4.435  41.286  1.00 55.00           O
ANISOU 3959  O   CYS A 631     6252   8046   6600  -1844   -969    -23       O
ATOM   3960  CB  CYS A 631     -18.281   6.781  41.696  1.00 57.01           C
ANISOU 3960  CB  CYS A 631     6164   8492   7004  -1667   -987     43       C
ATOM   3961  SG  CYS A 631     -18.415   6.374  43.445  1.00 61.82           S
ANISOU 3961  SG  CYS A 631     6727   9088   7672  -1714   -819     39       S
ATOM   3962  N   CYS A 632     -18.568   3.251  41.498  1.00 62.21           N
ANISOU 3962  N   CYS A 632     6959   9048   7630  -2053  -1014    -52       N
ATOM   3963  CA  CYS A 632     -18.031   1.933  41.862  1.00 59.12           C
ANISOU 3963  CA  CYS A 632     6693   8547   7224  -2167   -962    -77       C
ATOM   3964  C   CYS A 632     -17.415   1.880  43.254  1.00 58.58           C
ANISOU 3964  C   CYS A 632     6671   8420   7167  -2143   -807    -37       C
ATOM   3965  O   CYS A 632     -16.727   0.901  43.566  1.00 61.19           O
ANISOU 3965  O   CYS A 632     7129   8645   7476  -2209   -759    -43       O
ATOM   3966  CB  CYS A 632     -16.992   1.425  40.857  1.00 58.89           C
ANISOU 3966  CB  CYS A 632     6854   8428   7094  -2166  -1024   -123       C
ATOM   3967  SG  CYS A 632     -17.504   1.541  39.128  1.00 65.88           S
ANISOU 3967  SG  CYS A 632     7713   9396   7924  -2177  -1209   -174       S
ATOM   3968  N   TYR A 633     -17.596   2.905  44.086  1.00 56.88           N
ANISOU 3968  N   TYR A 633     6361   8270   6983  -2044   -731      0       N
ATOM   3969  CA  TYR A 633     -17.110   2.834  45.458  1.00 54.97           C
ANISOU 3969  CA  TYR A 633     6149   7995   6742  -2028   -587     33       C
ATOM   3970  C   TYR A 633     -17.851   1.728  46.196  1.00 60.01           C
ANISOU 3970  C   TYR A 633     6718   8643   7441  -2180   -533     52       C
ATOM   3971  O   TYR A 633     -19.067   1.575  46.054  1.00 64.25           O
ANISOU 3971  O   TYR A 633     7098   9264   8052  -2257   -574     49       O
ATOM   3972  CB  TYR A 633     -17.291   4.184  46.160  1.00 56.62           C
ANISOU 3972  CB  TYR A 633     6250   8286   6978  -1895   -525     50       C
ATOM   3973  CG  TYR A 633     -16.649   4.260  47.527  1.00 54.98           C
ANISOU 3973  CG  TYR A 633     6085   8056   6748  -1856   -383     72       C
ATOM   3974  CD1 TYR A 633     -15.274   4.339  47.677  1.00 54.05           C
ANISOU 3974  CD1 TYR A 633     6137   7842   6557  -1788   -346     73       C
ATOM   3975  CD2 TYR A 633     -17.430   4.208  48.671  1.00 56.59           C
ANISOU 3975  CD2 TYR A 633     6156   8348   7000  -1893   -287     91       C
ATOM   3976  CE1 TYR A 633     -14.697   4.378  48.952  1.00 54.59           C
ANISOU 3976  CE1 TYR A 633     6241   7903   6599  -1757   -223     91       C
ATOM   3977  CE2 TYR A 633     -16.880   4.255  49.928  1.00 56.52           C
ANISOU 3977  CE2 TYR A 633     6182   8339   6956  -1861   -160    110       C
ATOM   3978  CZ  TYR A 633     -15.515   4.339  50.079  1.00 57.62           C
ANISOU 3978  CZ  TYR A 633     6491   8383   7021  -1793   -132    110       C
ATOM   3979  OH  TYR A 633     -14.984   4.397  51.365  1.00 53.16           O
ANISOU 3979  OH  TYR A 633     5953   7830   6413  -1760    -12    127       O
ATOM   3980  N   SER A 634     -17.117   0.919  46.945  1.00 58.42           N
ANISOU 3980  N   SER A 634     6630   8353   7214  -2228   -447     77       N
ATOM   3981  CA  SER A 634     -17.730  -0.182  47.669  1.00 57.56           C
ANISOU 3981  CA  SER A 634     6467   8239   7165  -2376   -390    114       C
ATOM   3982  C   SER A 634     -17.294  -0.142  49.128  1.00 58.58           C
ANISOU 3982  C   SER A 634     6610   8377   7270  -2347   -241    173       C
ATOM   3983  O   SER A 634     -16.202   0.339  49.457  1.00 52.07           O
ANISOU 3983  O   SER A 634     5900   7510   6374  -2238   -195    175       O
ATOM   3984  CB  SER A 634     -17.399  -1.550  46.999  1.00 55.99           C
ANISOU 3984  CB  SER A 634     6393   7908   6974  -2502   -452     91       C
ATOM   3985  OG  SER A 634     -16.009  -1.753  46.799  1.00 55.05           O
ANISOU 3985  OG  SER A 634     6473   7666   6779  -2443   -444     78       O
ATOM   3986  N   TRP A 635     -18.168  -0.628  50.010  1.00 57.76           N
ANISOU 3986  N   TRP A 635     6382   8339   7223  -2445   -167    223       N
ATOM   3987  CA  TRP A 635     -17.843  -0.649  51.434  1.00 57.80           C
ANISOU 3987  CA  TRP A 635     6391   8378   7194  -2428    -24    286       C
ATOM   3988  C   TRP A 635     -18.672  -1.711  52.142  1.00 62.08           C
ANISOU 3988  C   TRP A 635     6841   8946   7801  -2589     39    358       C
ATOM   3989  O   TRP A 635     -19.736  -2.125  51.667  1.00 60.52           O
ANISOU 3989  O   TRP A 635     6525   8780   7690  -2698    -17    352       O
ATOM   3990  CB  TRP A 635     -18.063   0.725  52.076  1.00 57.71           C
ANISOU 3990  CB  TRP A 635     6268   8500   7158  -2289     39    268       C
ATOM   3991  CG  TRP A 635     -19.495   1.143  52.149  1.00 63.00           C
ANISOU 3991  CG  TRP A 635     6717   9314   7907  -2316     39    261       C
ATOM   3992  CD1 TRP A 635     -20.323   1.036  53.227  1.00 62.85           C
ANISOU 3992  CD1 TRP A 635     6549   9415   7916  -2366    147    306       C
ATOM   3993  CD2 TRP A 635     -20.274   1.738  51.103  1.00 60.03           C
ANISOU 3993  CD2 TRP A 635     6233   8984   7590  -2290    -74    210       C
ATOM   3994  NE1 TRP A 635     -21.561   1.529  52.919  1.00 60.29           N
ANISOU 3994  NE1 TRP A 635     6030   9205   7673  -2372    111    279       N
ATOM   3995  CE2 TRP A 635     -21.559   1.965  51.623  1.00 62.81           C
ANISOU 3995  CE2 TRP A 635     6370   9480   8015  -2325    -28    222       C
ATOM   3996  CE3 TRP A 635     -20.007   2.100  49.777  1.00 62.82           C
ANISOU 3996  CE3 TRP A 635     6650   9281   7939  -2239   -209    159       C
ATOM   3997  CZ2 TRP A 635     -22.583   2.531  50.868  1.00 66.78           C
ANISOU 3997  CZ2 TRP A 635     6715  10063   8594  -2310   -118    186       C
ATOM   3998  CZ3 TRP A 635     -21.020   2.668  49.028  1.00 63.68           C
ANISOU 3998  CZ3 TRP A 635     6608   9475   8113  -2225   -300    130       C
ATOM   3999  CH2 TRP A 635     -22.292   2.877  49.577  1.00 64.99           C
ANISOU 3999  CH2 TRP A 635     6557   9776   8360  -2259   -257    143       C
ATOM   4000  N   ARG A 636     -18.165  -2.139  53.293  1.00 59.65           N
ANISOU 4000  N   ARG A 636     6587   8628   7450  -2604    155    432       N
ATOM   4001  CA  ARG A 636     -18.837  -3.120  54.127  1.00 64.12           C
ANISOU 4001  CA  ARG A 636     7074   9222   8067  -2751    235    526       C
ATOM   4002  C   ARG A 636     -19.736  -2.428  55.145  1.00 66.21           C
ANISOU 4002  C   ARG A 636     7149   9681   8327  -2724    342    554       C
ATOM   4003  O   ARG A 636     -19.469  -1.291  55.572  1.00 60.89           O
ANISOU 4003  O   ARG A 636     6453   9098   7585  -2578    387    514       O
ATOM   4004  CB  ARG A 636     -17.817  -4.004  54.842  1.00 62.85           C
ANISOU 4004  CB  ARG A 636     7070   8951   7857  -2784    303    607       C
ATOM   4005  CG  ARG A 636     -18.262  -5.446  54.996  1.00 64.12           C
ANISOU 4005  CG  ARG A 636     7222   9031   8109  -2971    313    694       C
ATOM   4006  CD  ARG A 636     -17.249  -6.237  55.809  1.00 64.05           C
ANISOU 4006  CD  ARG A 636     7360   8923   8054  -2988    387    791       C
ATOM   4007  NE  ARG A 636     -15.915  -6.217  55.209  1.00 58.60           N
ANISOU 4007  NE  ARG A 636     6868   8089   7310  -2896    326    736       N
ATOM   4008  CZ  ARG A 636     -15.530  -7.007  54.217  1.00 57.88           C
ANISOU 4008  CZ  ARG A 636     6890   7826   7277  -2952    228    694       C
ATOM   4009  NH1 ARG A 636     -16.370  -7.855  53.638  1.00 57.31           N
ANISOU 4009  NH1 ARG A 636     6758   7696   7323  -3101    168    688       N
ATOM   4010  NH2 ARG A 636     -14.267  -6.962  53.811  1.00 54.16           N
ANISOU 4010  NH2 ARG A 636     6591   7240   6746  -2859    193    652       N
ATOM   4011  N   SER A 637     -20.812  -3.136  55.531  1.00 62.89           N
ANISOU 4011  N   SER A 637     6588   9323   7986  -2869    384    621       N
ATOM   4012  CA  SER A 637     -21.750  -2.610  56.520  1.00 64.42           C
ANISOU 4012  CA  SER A 637     6586   9712   8179  -2860    497    653       C
ATOM   4013  C   SER A 637     -21.063  -2.335  57.852  1.00 66.69           C
ANISOU 4013  C   SER A 637     6922  10070   8347  -2782    636    705       C
ATOM   4014  O   SER A 637     -21.477  -1.438  58.600  1.00 62.91           O
ANISOU 4014  O   SER A 637     6320   9758   7825  -2696    722    683       O
ATOM   4015  CB  SER A 637     -22.914  -3.589  56.723  1.00 70.80           C
ANISOU 4015  CB  SER A 637     7248  10559   9094  -3049    524    733       C
ATOM   4016  OG  SER A 637     -22.473  -4.916  56.976  1.00 63.08           O
ANISOU 4016  OG  SER A 637     6384   9449   8136  -3182    544    832       O
ATOM   4017  N   THR A 638     -20.011  -3.092  58.159  1.00 64.03           N
ANISOU 4017  N   THR A 638     6763   9610   7955  -2807    656    769       N
ATOM   4018  CA  THR A 638     -19.284  -2.928  59.405  1.00 64.31           C
ANISOU 4018  CA  THR A 638     6857   9710   7869  -2740    776    826       C
ATOM   4019  C   THR A 638     -18.309  -1.760  59.369  1.00 66.80           C
ANISOU 4019  C   THR A 638     7264  10028   8089  -2551    760    728       C
ATOM   4020  O   THR A 638     -17.837  -1.335  60.426  1.00 72.84           O
ANISOU 4020  O   THR A 638     8043  10885   8747  -2472    857    745       O
ATOM   4021  CB  THR A 638     -18.530  -4.214  59.715  1.00 68.24           C
ANISOU 4021  CB  THR A 638     7504  10068   8355  -2838    793    941       C
ATOM   4022  OG1 THR A 638     -17.813  -4.622  58.543  1.00 70.90           O
ANISOU 4022  OG1 THR A 638     7998  10204   8739  -2843    666    889       O
ATOM   4023  CG2 THR A 638     -19.503  -5.316  60.102  1.00 71.14           C
ANISOU 4023  CG2 THR A 638     7762  10457   8810  -3025    844   1062       C
ATOM   4024  N   GLU A 639     -17.981  -1.254  58.187  1.00 68.72           N
ANISOU 4024  N   GLU A 639     7570  10174   8366  -2481    639    631       N
ATOM   4025  CA  GLU A 639     -17.151  -0.067  58.069  1.00 70.55           C
ANISOU 4025  CA  GLU A 639     7870  10407   8530  -2306    619    539       C
ATOM   4026  C   GLU A 639     -17.969   1.192  58.348  1.00 71.73           C
ANISOU 4026  C   GLU A 639     7843  10722   8689  -2208    655    466       C
ATOM   4027  O   GLU A 639     -19.203   1.192  58.306  1.00 73.28           O
ANISOU 4027  O   GLU A 639     7866  11018   8960  -2270    665    469       O
ATOM   4028  CB  GLU A 639     -16.518   0.039  56.677  1.00 67.52           C
ANISOU 4028  CB  GLU A 639     7611   9867   8177  -2267    481    473       C
ATOM   4029  CG  GLU A 639     -15.482  -1.024  56.307  1.00 62.47           C
ANISOU 4029  CG  GLU A 639     7165   9049   7521  -2324    440    516       C
ATOM   4030  CD  GLU A 639     -14.810  -0.687  54.981  1.00 60.27           C
ANISOU 4030  CD  GLU A 639     6999   8649   7251  -2257    317    435       C
ATOM   4031  OE1 GLU A 639     -13.776   0.029  54.991  1.00 58.32           O
ANISOU 4031  OE1 GLU A 639     6851   8371   6936  -2129    316    396       O
ATOM   4032  OE2 GLU A 639     -15.328  -1.105  53.925  1.00 61.30           O
ANISOU 4032  OE2 GLU A 639     7114   8726   7452  -2331    221    408       O
ATOM   4033  N   ASN A 640     -17.250   2.267  58.664  1.00 67.93           N
ANISOU 4033  N   ASN A 640     7403  10265   8141  -2053    675    396       N
ATOM   4034  CA  ASN A 640     -17.813   3.605  58.849  1.00 68.88           C
ANISOU 4034  CA  ASN A 640     7381  10511   8281  -1931    697    304       C
ATOM   4035  C   ASN A 640     -16.950   4.548  58.021  1.00 72.57           C
ANISOU 4035  C   ASN A 640     7948  10873   8751  -1796    604    221       C
ATOM   4036  O   ASN A 640     -16.132   5.303  58.564  1.00 71.54           O
ANISOU 4036  O   ASN A 640     7875  10749   8556  -1678    642    172       O
ATOM   4037  CB  ASN A 640     -17.833   4.002  60.329  1.00 71.96           C
ANISOU 4037  CB  ASN A 640     7703  11058   8581  -1878    839    301       C
ATOM   4038  CG  ASN A 640     -18.854   5.082  60.634  1.00 77.51           C
ANISOU 4038  CG  ASN A 640     8203  11917   9329  -1797    883    219       C
ATOM   4039  OD1 ASN A 640     -20.040   4.800  60.806  1.00 76.28           O
ANISOU 4039  OD1 ASN A 640     7883  11871   9228  -1876    924    250       O
ATOM   4040  ND2 ASN A 640     -18.393   6.330  60.710  1.00 82.58           N
ANISOU 4040  ND2 ASN A 640     8851  12567   9960  -1637    877    113       N
ATOM   4041  N   PRO A 641     -17.090   4.519  56.695  1.00 69.08           N
ANISOU 4041  N   PRO A 641     7530  10336   8383  -1813    480    204       N
ATOM   4042  CA  PRO A 641     -16.071   5.148  55.846  1.00 68.33           C
ANISOU 4042  CA  PRO A 641     7568  10120   8276  -1708    391    154       C
ATOM   4043  C   PRO A 641     -16.240   6.659  55.816  1.00 64.54           C
ANISOU 4043  C   PRO A 641     6994   9696   7832  -1555    383     70       C
ATOM   4044  O   PRO A 641     -17.356   7.179  55.720  1.00 64.98           O
ANISOU 4044  O   PRO A 641     6879   9847   7963  -1541    378     43       O
ATOM   4045  CB  PRO A 641     -16.309   4.517  54.468  1.00 66.08           C
ANISOU 4045  CB  PRO A 641     7322   9739   8048  -1792    267    170       C
ATOM   4046  CG  PRO A 641     -17.715   4.006  54.510  1.00 68.40           C
ANISOU 4046  CG  PRO A 641     7449  10127   8413  -1906    274    198       C
ATOM   4047  CD  PRO A 641     -18.194   3.930  55.918  1.00 64.46           C
ANISOU 4047  CD  PRO A 641     6844   9760   7889  -1928    413    228       C
ATOM   4048  N   VAL A 642     -15.122   7.358  55.957  1.00 61.93           N
ANISOU 4048  N   VAL A 642     6771   9304   7455  -1441    386     30       N
ATOM   4049  CA  VAL A 642     -15.049   8.796  55.745  1.00 57.43           C
ANISOU 4049  CA  VAL A 642     6148   8739   6935  -1292    359    -48       C
ATOM   4050  C   VAL A 642     -14.078   9.028  54.600  1.00 59.29           C
ANISOU 4050  C   VAL A 642     6527   8828   7173  -1246    254    -47       C
ATOM   4051  O   VAL A 642     -12.868   8.792  54.729  1.00 55.71           O
ANISOU 4051  O   VAL A 642     6229   8288   6650  -1230    263    -37       O
ATOM   4052  CB  VAL A 642     -14.624   9.551  57.010  1.00 62.79           C
ANISOU 4052  CB  VAL A 642     6806   9486   7566  -1193    462   -108       C
ATOM   4053  CG1 VAL A 642     -14.406  11.026  56.696  1.00 61.97           C
ANISOU 4053  CG1 VAL A 642     6665   9350   7532  -1039    421   -192       C
ATOM   4054  CG2 VAL A 642     -15.689   9.384  58.107  1.00 61.71           C
ANISOU 4054  CG2 VAL A 642     6508   9520   7420  -1234    571   -113       C
ATOM   4055  N   VAL A 643     -14.613   9.465  53.468  1.00 61.46           N
ANISOU 4055  N   VAL A 643     6745   9082   7524  -1225    153    -51       N
ATOM   4056  CA  VAL A 643     -13.803   9.740  52.289  1.00 60.61           C
ANISOU 4056  CA  VAL A 643     6758   8854   7416  -1180     52    -43       C
ATOM   4057  C   VAL A 643     -13.272  11.162  52.402  1.00 60.59           C
ANISOU 4057  C   VAL A 643     6745   8825   7452  -1025     53    -93       C
ATOM   4058  O   VAL A 643     -14.054  12.116  52.518  1.00 55.53           O
ANISOU 4058  O   VAL A 643     5957   8247   6896   -951     53   -131       O
ATOM   4059  CB  VAL A 643     -14.609   9.544  50.996  1.00 58.77           C
ANISOU 4059  CB  VAL A 643     6471   8622   7235  -1231    -63    -17       C
ATOM   4060  CG1 VAL A 643     -13.710   9.751  49.766  1.00 54.46           C
ANISOU 4060  CG1 VAL A 643     6061   7967   6666  -1189   -162     -2       C
ATOM   4061  CG2 VAL A 643     -15.225   8.142  50.970  1.00 55.30           C
ANISOU 4061  CG2 VAL A 643     6025   8209   6777  -1392    -62     20       C
ATOM   4062  N   MET A 644     -11.941  11.290  52.390  1.00 60.49           N
ANISOU 4062  N   MET A 644     6883   8714   7386   -979     56    -95       N
ATOM   4063  CA  MET A 644     -11.294  12.592  52.401  1.00 58.65           C
ANISOU 4063  CA  MET A 644     6656   8431   7197   -841     48   -138       C
ATOM   4064  C   MET A 644     -11.848  13.447  51.282  1.00 58.06           C
ANISOU 4064  C   MET A 644     6503   8338   7219   -781    -50   -126       C
ATOM   4065  O   MET A 644     -12.193  12.943  50.208  1.00 54.67           O
ANISOU 4065  O   MET A 644     6089   7898   6784   -842   -134    -75       O
ATOM   4066  CB  MET A 644      -9.780  12.458  52.218  1.00 53.34           C
ANISOU 4066  CB  MET A 644     6164   7645   6460   -820     41   -123       C
ATOM   4067  CG  MET A 644      -9.061  11.826  53.388  1.00 60.52           C
ANISOU 4067  CG  MET A 644     7151   8564   7279   -851    134   -136       C
ATOM   4068  SD  MET A 644      -7.320  11.541  53.013  1.00 54.59           S
ANISOU 4068  SD  MET A 644     6605   7678   6460   -835    112   -110       S
ATOM   4069  CE  MET A 644      -6.762  10.691  54.498  1.00 57.18           C
ANISOU 4069  CE  MET A 644     6992   8047   6685   -882    218   -112       C
ATOM   4070  N   GLU A 645     -11.905  14.759  51.541  1.00 61.96           N
ANISOU 4070  N   GLU A 645     6914   8828   7802   -658    -42   -174       N
ATOM   4071  CA  GLU A 645     -12.404  15.709  50.547  1.00 59.52           C
ANISOU 4071  CA  GLU A 645     6521   8494   7598   -583   -135   -152       C
ATOM   4072  C   GLU A 645     -11.740  15.495  49.197  1.00 54.69           C
ANISOU 4072  C   GLU A 645     6034   7796   6950   -602   -233    -77       C
ATOM   4073  O   GLU A 645     -12.408  15.537  48.159  1.00 59.29           O
ANISOU 4073  O   GLU A 645     6564   8398   7564   -615   -324    -29       O
ATOM   4074  CB  GLU A 645     -12.182  17.151  51.024  1.00 62.33           C
ANISOU 4074  CB  GLU A 645     6812   8813   8059   -441   -111   -214       C
ATOM   4075  CG  GLU A 645     -12.746  17.444  52.417  1.00 66.25           C
ANISOU 4075  CG  GLU A 645     7188   9401   8582   -408     -6   -309       C
ATOM   4076  CD  GLU A 645     -14.243  17.175  52.525  1.00 69.08           C
ANISOU 4076  CD  GLU A 645     7379   9887   8982   -450      2   -312       C
ATOM   4077  OE1 GLU A 645     -14.967  17.323  51.511  1.00 67.68           O
ANISOU 4077  OE1 GLU A 645     7132   9713   8872   -452    -90   -259       O
ATOM   4078  OE2 GLU A 645     -14.697  16.794  53.628  1.00 78.39           O
ANISOU 4078  OE2 GLU A 645     8492  11170  10122   -485    100   -363       O
ATOM   4079  N   LYS A 646     -10.434  15.230  49.191  1.00 54.47           N
ANISOU 4079  N   LYS A 646     6166   7683   6848   -605   -215    -67       N
ATOM   4080  CA  LYS A 646      -9.711  15.116  47.931  1.00 54.75           C
ANISOU 4080  CA  LYS A 646     6319   7641   6844   -610   -297     -2       C
ATOM   4081  C   LYS A 646     -10.065  13.846  47.164  1.00 53.33           C
ANISOU 4081  C   LYS A 646     6189   7493   6581   -731   -347     37       C
ATOM   4082  O   LYS A 646      -9.768  13.753  45.967  1.00 54.92           O
ANISOU 4082  O   LYS A 646     6457   7661   6748   -739   -429     87       O
ATOM   4083  CB  LYS A 646      -8.201  15.166  48.187  1.00 52.63           C
ANISOU 4083  CB  LYS A 646     6198   7277   6524   -579   -257     -8       C
ATOM   4084  CG  LYS A 646      -7.673  13.932  48.900  1.00 57.28           C
ANISOU 4084  CG  LYS A 646     6889   7870   7006   -668   -189    -25       C
ATOM   4085  CD  LYS A 646      -6.308  14.142  49.592  1.00 56.76           C
ANISOU 4085  CD  LYS A 646     6928   7731   6908   -620   -129    -51       C
ATOM   4086  CE  LYS A 646      -6.385  15.114  50.785  1.00 61.07           C
ANISOU 4086  CE  LYS A 646     7383   8302   7519   -538    -64   -125       C
ATOM   4087  NZ  LYS A 646      -7.656  15.013  51.604  1.00 59.05           N
ANISOU 4087  NZ  LYS A 646     6988   8162   7288   -562    -17   -168       N
ATOM   4088  N   PHE A 647     -10.669  12.852  47.810  1.00 51.52           N
ANISOU 4088  N   PHE A 647     5931   7328   6317   -829   -300     15       N
ATOM   4089  CA  PHE A 647     -11.009  11.617  47.111  1.00 53.30           C
ANISOU 4089  CA  PHE A 647     6202   7570   6481   -951   -350     42       C
ATOM   4090  C   PHE A 647     -12.495  11.507  46.811  1.00 55.40           C
ANISOU 4090  C   PHE A 647     6313   7935   6803  -1000   -400     46       C
ATOM   4091  O   PHE A 647     -12.939  10.467  46.309  1.00 55.72           O
ANISOU 4091  O   PHE A 647     6368   7996   6805  -1112   -443     57       O
ATOM   4092  CB  PHE A 647     -10.530  10.401  47.901  1.00 54.06           C
ANISOU 4092  CB  PHE A 647     6393   7645   6500  -1044   -273     31       C
ATOM   4093  CG  PHE A 647      -9.036  10.289  47.963  1.00 54.24           C
ANISOU 4093  CG  PHE A 647     6581   7569   6458  -1010   -244     35       C
ATOM   4094  CD1 PHE A 647      -8.262  10.570  46.839  1.00 58.14           C
ANISOU 4094  CD1 PHE A 647     7170   7995   6926   -969   -312     60       C
ATOM   4095  CD2 PHE A 647      -8.399   9.922  49.139  1.00 50.61           C
ANISOU 4095  CD2 PHE A 647     6177   7093   5961  -1019   -149     18       C
ATOM   4096  CE1 PHE A 647      -6.873  10.489  46.891  1.00 58.54           C
ANISOU 4096  CE1 PHE A 647     7362   7959   6923   -936   -282     64       C
ATOM   4097  CE2 PHE A 647      -7.018   9.834  49.197  1.00 50.38           C
ANISOU 4097  CE2 PHE A 647     6290   6976   5878   -985   -127     22       C
ATOM   4098  CZ  PHE A 647      -6.253  10.118  48.079  1.00 53.89           C
ANISOU 4098  CZ  PHE A 647     6822   7348   6306   -944   -192     43       C
ATOM   4099  N   LYS A 648     -13.266  12.560  47.088  1.00 55.68           N
ANISOU 4099  N   LYS A 648     6195   8026   6937   -919   -399     33       N
ATOM   4100  CA  LYS A 648     -14.680  12.597  46.756  1.00 52.43           C
ANISOU 4100  CA  LYS A 648     5618   7711   6592   -949   -454     39       C
ATOM   4101  C   LYS A 648     -14.863  12.890  45.271  1.00 56.25           C
ANISOU 4101  C   LYS A 648     6103   8190   7080   -931   -589     89       C
ATOM   4102  O   LYS A 648     -14.023  13.539  44.633  1.00 52.27           O
ANISOU 4102  O   LYS A 648     5684   7615   6562   -852   -629    120       O
ATOM   4103  CB  LYS A 648     -15.400  13.656  47.599  1.00 58.03           C
ANISOU 4103  CB  LYS A 648     6158   8479   7410   -856   -401      2       C
ATOM   4104  CG  LYS A 648     -15.451  13.329  49.095  1.00 59.30           C
ANISOU 4104  CG  LYS A 648     6290   8686   7555   -881   -266    -51       C
ATOM   4105  CD  LYS A 648     -16.595  14.038  49.819  1.00 58.69           C
ANISOU 4105  CD  LYS A 648     6008   8712   7581   -827   -220    -95       C
ATOM   4106  CE  LYS A 648     -16.576  13.731  51.311  1.00 61.84           C
ANISOU 4106  CE  LYS A 648     6384   9171   7941   -849    -80   -147       C
ATOM   4107  NZ  LYS A 648     -17.694  14.359  52.059  1.00 64.62           N
ANISOU 4107  NZ  LYS A 648     6533   9637   8381   -798    -22   -199       N
ATOM   4108  N   LEU A 649     -15.978  12.405  44.723  1.00 55.08           N
ANISOU 4108  N   LEU A 649     5855   8123   6949  -1008   -661    100       N
ATOM   4109  CA  LEU A 649     -16.308  12.585  43.319  1.00 57.46           C
ANISOU 4109  CA  LEU A 649     6142   8449   7243  -1002   -798    146       C
ATOM   4110  C   LEU A 649     -17.666  13.262  43.178  1.00 57.09           C
ANISOU 4110  C   LEU A 649     5885   8499   7308   -964   -854    158       C
ATOM   4111  O   LEU A 649     -18.505  13.219  44.080  1.00 54.32           O
ANISOU 4111  O   LEU A 649     5399   8212   7028   -984   -790    122       O
ATOM   4112  CB  LEU A 649     -16.315  11.243  42.578  1.00 59.07           C
ANISOU 4112  CB  LEU A 649     6435   8660   7350  -1141   -858    141       C
ATOM   4113  CG  LEU A 649     -14.986  10.482  42.587  1.00 57.54           C
ANISOU 4113  CG  LEU A 649     6447   8366   7048  -1179   -813    129       C
ATOM   4114  CD1 LEU A 649     -15.129   9.164  41.849  1.00 58.58           C
ANISOU 4114  CD1 LEU A 649     6649   8504   7104  -1314   -877    109       C
ATOM   4115  CD2 LEU A 649     -13.854  11.334  41.997  1.00 55.50           C
ANISOU 4115  CD2 LEU A 649     6297   8037   6752  -1067   -833    166       C
ATOM   4116  N   ASP A 650     -17.861  13.912  42.033  1.00 63.29           N
ANISOU 4116  N   ASP A 650     6639   9300   8107   -904   -974    214       N
ATOM   4117  CA  ASP A 650     -19.149  14.464  41.642  1.00 63.58           C
ANISOU 4117  CA  ASP A 650     6481   9433   8242   -873  -1057    239       C
ATOM   4118  C   ASP A 650     -19.347  14.199  40.154  1.00 70.14           C
ANISOU 4118  C   ASP A 650     7338  10308   9002   -910  -1209    293       C
ATOM   4119  O   ASP A 650     -18.496  13.603  39.488  1.00 68.13           O
ANISOU 4119  O   ASP A 650     7249  10011   8625   -958  -1238    301       O
ATOM   4120  CB  ASP A 650     -19.259  15.960  41.998  1.00 65.78           C
ANISOU 4120  CB  ASP A 650     6655   9687   8652   -712  -1037    259       C
ATOM   4121  CG  ASP A 650     -18.238  16.859  41.251  1.00 74.08           C
ANISOU 4121  CG  ASP A 650     7814  10645   9688   -604  -1085    327       C
ATOM   4122  OD1 ASP A 650     -17.768  16.509  40.143  1.00 80.58           O
ANISOU 4122  OD1 ASP A 650     8748  11463  10406   -639  -1170    380       O
ATOM   4123  OD2 ASP A 650     -17.931  17.962  41.771  1.00 72.45           O
ANISOU 4123  OD2 ASP A 650     7574  10372   9582   -482  -1036    327       O
ATOM   4124  N   ASP A 651     -20.482  14.658  39.626  1.00 74.33           N
ANISOU 4124  N   ASP A 651     7699  10932   9610   -884  -1308    327       N
ATOM   4125  CA  ASP A 651     -20.808  14.398  38.229  1.00 75.02           C
ANISOU 4125  CA  ASP A 651     7792  11089   9625   -923  -1462    375       C
ATOM   4126  C   ASP A 651     -19.792  15.009  37.270  1.00 80.26           C
ANISOU 4126  C   ASP A 651     8588  11696  10209   -839  -1520    450       C
ATOM   4127  O   ASP A 651     -19.596  14.475  36.171  1.00 79.03           O
ANISOU 4127  O   ASP A 651     8517  11581   9931   -895  -1618    471       O
ATOM   4128  CB  ASP A 651     -22.217  14.892  37.919  1.00 73.36           C
ANISOU 4128  CB  ASP A 651     7358  10992   9523   -895  -1558    405       C
ATOM   4129  CG  ASP A 651     -23.278  13.988  38.504  1.00 74.06           C
ANISOU 4129  CG  ASP A 651     7322  11163   9656  -1018  -1533    337       C
ATOM   4130  OD1 ASP A 651     -23.054  12.758  38.518  1.00 70.01           O
ANISOU 4130  OD1 ASP A 651     6908  10642   9051  -1156  -1515    285       O
ATOM   4131  OD2 ASP A 651     -24.319  14.510  38.971  1.00 71.77           O
ANISOU 4131  OD2 ASP A 651     6833  10939   9499   -976  -1526    336       O
ATOM   4132  N   ASN A 652     -19.163  16.131  37.621  1.00 93.77           N
ANISOU 4132  N   ASN A 652    10315  13322  11990   -708  -1466    492       N
ATOM   4133  CA  ASN A 652     -18.019  16.537  36.816  1.00 93.65           C
ANISOU 4133  CA  ASN A 652    10451  13243  11889   -650  -1497    562       C
ATOM   4134  C   ASN A 652     -16.859  15.561  36.880  1.00 92.08           C
ANISOU 4134  C   ASN A 652    10456  12980  11550   -731  -1430    513       C
ATOM   4135  O   ASN A 652     -16.530  14.931  35.872  1.00 91.95           O
ANISOU 4135  O   ASN A 652    10541  12997  11397   -790  -1503    527       O
ATOM   4136  CB  ASN A 652     -17.414  17.872  37.221  1.00 93.39           C
ANISOU 4136  CB  ASN A 652    10413  13108  11964   -504  -1443    613       C
ATOM   4137  CG  ASN A 652     -16.778  18.559  36.052  1.00 95.66           C
ANISOU 4137  CG  ASN A 652    10771  13375  12201   -432  -1528    731       C
ATOM   4138  OD1 ASN A 652     -16.425  17.901  35.077  1.00 96.68           O
ANISOU 4138  OD1 ASN A 652    11005  13551  12177   -496  -1594    756       O
ATOM   4139  ND2 ASN A 652     -16.400  19.815  36.222  1.00 98.45           N
ANISOU 4139  ND2 ASN A 652    11094  13640  12670   -303  -1508    795       N
ATOM   4140  N   LYS A 653     -16.218  15.455  38.054  1.00 76.99           N
ANISOU 4140  N   LYS A 653     8605  10980   9670   -728  -1294    453       N
ATOM   4141  CA  LYS A 653     -14.941  14.759  38.148  1.00 77.29           C
ANISOU 4141  CA  LYS A 653     8837  10937   9593   -773  -1227    422       C
ATOM   4142  C   LYS A 653     -15.004  13.419  37.434  1.00 74.71           C
ANISOU 4142  C   LYS A 653     8593  10659   9133   -904  -1283    385       C
ATOM   4143  O   LYS A 653     -14.066  13.041  36.727  1.00 74.70           O
ANISOU 4143  O   LYS A 653     8743  10627   9013   -920  -1299    395       O
ATOM   4144  CB  LYS A 653     -14.557  14.609  39.627  1.00 73.93           C
ANISOU 4144  CB  LYS A 653     8430  10441   9218   -777  -1082    351       C
ATOM   4145  CG  LYS A 653     -14.678  15.934  40.410  1.00 70.83           C
ANISOU 4145  CG  LYS A 653     7931  10011   8971   -649  -1030    362       C
ATOM   4146  CD  LYS A 653     -14.218  15.864  41.875  1.00 73.06           C
ANISOU 4146  CD  LYS A 653     8236  10235   9287   -643   -888    286       C
ATOM   4147  CE  LYS A 653     -12.942  16.681  42.117  1.00 74.34           C
ANISOU 4147  CE  LYS A 653     8497  10283   9464   -547   -836    301       C
ATOM   4148  NZ  LYS A 653     -13.214  18.086  42.575  1.00 77.64           N
ANISOU 4148  NZ  LYS A 653     8793  10670  10037   -417   -821    305       N
ATOM   4149  N   ILE A 654     -16.134  12.725  37.543  1.00 71.90           N
ANISOU 4149  N   ILE A 654     8132  10385   8801   -998  -1319    340       N
ATOM   4150  CA  ILE A 654     -16.327  11.476  36.812  1.00 71.61           C
ANISOU 4150  CA  ILE A 654     8155  10395   8657  -1127  -1387    296       C
ATOM   4151  C   ILE A 654     -16.318  11.732  35.305  1.00 72.10           C
ANISOU 4151  C   ILE A 654     8243  10528   8626  -1102  -1526    351       C
ATOM   4152  O   ILE A 654     -15.624  11.051  34.542  1.00 69.10           O
ANISOU 4152  O   ILE A 654     8004  10138   8111  -1149  -1557    329       O
ATOM   4153  CB  ILE A 654     -17.626  10.800  37.281  1.00 68.01           C
ANISOU 4153  CB  ILE A 654     7556  10012   8274  -1231  -1400    244       C
ATOM   4154  CG1 ILE A 654     -17.465  10.391  38.745  1.00 64.41           C
ANISOU 4154  CG1 ILE A 654     7105   9491   7876  -1267  -1252    195       C
ATOM   4155  CG2 ILE A 654     -18.035   9.608  36.381  1.00 58.76           C
ANISOU 4155  CG2 ILE A 654     6414   8898   7013  -1365  -1501    194       C
ATOM   4156  CD1 ILE A 654     -18.786  10.101  39.441  1.00 65.01           C
ANISOU 4156  CD1 ILE A 654     7001   9644   8056  -1335  -1236    166       C
ATOM   4157  N   ALA A 655     -17.098  12.715  34.849  1.00 70.12           N
ANISOU 4157  N   ALA A 655     7850  10352   8441  -1024  -1612    424       N
ATOM   4158  CA  ALA A 655     -17.157  12.973  33.416  1.00 74.92           C
ANISOU 4158  CA  ALA A 655     8471  11045   8950   -999  -1751    491       C
ATOM   4159  C   ALA A 655     -15.806  13.421  32.857  1.00 73.80           C
ANISOU 4159  C   ALA A 655     8489  10842   8711   -924  -1729    552       C
ATOM   4160  O   ALA A 655     -15.451  13.057  31.731  1.00 73.30           O
ANISOU 4160  O   ALA A 655     8515  10835   8500   -950  -1807    565       O
ATOM   4161  CB  ALA A 655     -18.241  14.004  33.113  1.00 79.29           C
ANISOU 4161  CB  ALA A 655     8833  11685   9607   -919  -1845    573       C
ATOM   4162  N   ASN A 656     -15.028  14.179  33.624  1.00 76.87           N
ANISOU 4162  N   ASN A 656     8913  11118   9174   -835  -1622    584       N
ATOM   4163  CA  ASN A 656     -13.738  14.670  33.153  1.00 75.28           C
ANISOU 4163  CA  ASN A 656     8850  10854   8901   -763  -1595    649       C
ATOM   4164  C   ASN A 656     -12.565  13.774  33.521  1.00 69.70           C
ANISOU 4164  C   ASN A 656     8319  10060   8104   -820  -1494    573       C
ATOM   4165  O   ASN A 656     -11.419  14.197  33.353  1.00 66.56           O
ANISOU 4165  O   ASN A 656     8029   9595   7667   -759  -1447    619       O
ATOM   4166  CB  ASN A 656     -13.454  16.075  33.689  1.00 77.13           C
ANISOU 4166  CB  ASN A 656     9025  11006   9275   -630  -1544    730       C
ATOM   4167  CG  ASN A 656     -14.505  17.085  33.297  1.00 81.03           C
ANISOU 4167  CG  ASN A 656     9347  11567   9874   -553  -1643    820       C
ATOM   4168  OD1 ASN A 656     -15.421  16.798  32.522  1.00 80.37           O
ANISOU 4168  OD1 ASN A 656     9187  11606   9745   -593  -1759    836       O
ATOM   4169  ND2 ASN A 656     -14.376  18.289  33.834  1.00 83.82           N
ANISOU 4169  ND2 ASN A 656     9634  11838  10377   -438  -1600    877       N
ATOM   4170  N   MET A 657     -12.808  12.566  34.015  1.00 67.56           N
ANISOU 4170  N   MET A 657     8076   9785   7810   -933  -1460    464       N
ATOM   4171  CA  MET A 657     -11.723  11.738  34.516  1.00 63.26           C
ANISOU 4171  CA  MET A 657     7686   9143   7206   -979  -1359    396       C
ATOM   4172  C   MET A 657     -10.890  11.178  33.364  1.00 62.17           C
ANISOU 4172  C   MET A 657     7696   9024   6902  -1003  -1401    391       C
ATOM   4173  O   MET A 657     -11.420  10.838  32.303  1.00 59.55           O
ANISOU 4173  O   MET A 657     7349   8797   6481  -1045  -1512    386       O
ATOM   4174  CB  MET A 657     -12.297  10.609  35.366  1.00 64.60           C
ANISOU 4174  CB  MET A 657     7833   9301   7412  -1095  -1315    296       C
ATOM   4175  CG  MET A 657     -11.365  10.025  36.374  1.00 55.06           C
ANISOU 4175  CG  MET A 657     6735   7978   6206  -1119  -1187    244       C
ATOM   4176  SD  MET A 657     -12.286   8.737  37.187  1.00 61.77           S
ANISOU 4176  SD  MET A 657     7531   8837   7104  -1263  -1161    156       S
ATOM   4177  CE  MET A 657     -13.053   9.625  38.540  1.00 60.92           C
ANISOU 4177  CE  MET A 657     7256   8740   7152  -1207  -1086    179       C
ATOM   4178  N   GLY A 658      -9.573  11.103  33.566  1.00 58.06           N
ANISOU 4178  N   GLY A 658     7314   8411   6336   -973  -1313    388       N
ATOM   4179  CA  GLY A 658      -8.708  10.513  32.556  1.00 63.86           C
ANISOU 4179  CA  GLY A 658     8190   9160   6912   -993  -1335    370       C
ATOM   4180  C   GLY A 658      -9.017   9.068  32.201  1.00 64.60           C
ANISOU 4180  C   GLY A 658     8339   9285   6922  -1116  -1374    254       C
ATOM   4181  O   GLY A 658      -9.058   8.215  33.095  1.00 67.97           O
ANISOU 4181  O   GLY A 658     8786   9637   7401  -1188  -1309    175       O
ATOM   4182  N   VAL A 659      -9.214   8.773  30.914  1.00 68.25           N
ANISOU 4182  N   VAL A 659     8825   9852   7254  -1143  -1478    243       N
ATOM   4183  CA  VAL A 659      -9.611   7.436  30.464  1.00 68.02           C
ANISOU 4183  CA  VAL A 659     8836   9859   7151  -1262  -1534    120       C
ATOM   4184  C   VAL A 659      -8.381   6.663  29.998  1.00 77.12           C
ANISOU 4184  C   VAL A 659    10162  10961   8177  -1274  -1488     54       C
ATOM   4185  O   VAL A 659      -7.813   6.961  28.941  1.00 80.27           O
ANISOU 4185  O   VAL A 659    10625  11432   8443  -1224  -1525     87       O
ATOM   4186  CB  VAL A 659     -10.660   7.508  29.356  1.00 70.84           C
ANISOU 4186  CB  VAL A 659     9104  10373   7439  -1291  -1686    126       C
ATOM   4187  CG1 VAL A 659     -11.027   6.102  28.891  1.00 73.05           C
ANISOU 4187  CG1 VAL A 659     9427  10680   7647  -1419  -1746    -18       C
ATOM   4188  CG2 VAL A 659     -11.879   8.251  29.862  1.00 68.20           C
ANISOU 4188  CG2 VAL A 659     8588  10083   7243  -1274  -1727    190       C
ATOM   4189  N   ILE A 660      -7.997   5.646  30.767  1.00 74.52           N
ANISOU 4189  N   ILE A 660     9907  10517   7891  -1340  -1409    -38       N
ATOM   4190  CA  ILE A 660      -6.745   4.921  30.598  1.00 73.60           C
ANISOU 4190  CA  ILE A 660     9951  10321   7693  -1340  -1342   -102       C
ATOM   4191  C   ILE A 660      -7.055   3.467  30.258  1.00 77.97           C
ANISOU 4191  C   ILE A 660    10556  10862   8206  -1460  -1386   -246       C
ATOM   4192  O   ILE A 660      -7.688   2.772  31.055  1.00 75.38           O
ANISOU 4192  O   ILE A 660    10185  10470   7985  -1547  -1372   -297       O
ATOM   4193  CB  ILE A 660      -5.876   4.987  31.864  1.00 72.35           C
ANISOU 4193  CB  ILE A 660     9841  10018   7629  -1304  -1205    -79       C
ATOM   4194  CG1 ILE A 660      -5.366   6.405  32.118  1.00 74.23           C
ANISOU 4194  CG1 ILE A 660    10047  10255   7903  -1183  -1159     48       C
ATOM   4195  CG2 ILE A 660      -4.731   4.005  31.764  1.00 76.87           C
ANISOU 4195  CG2 ILE A 660    10568  10501   8137  -1322  -1143   -161       C
ATOM   4196  CD1 ILE A 660      -4.582   6.532  33.408  1.00 62.70           C
ANISOU 4196  CD1 ILE A 660     8621   8665   6537  -1148  -1035     64       C
ATOM   4197  N   PRO A 661      -6.657   2.957  29.084  1.00 79.89           N
ANISOU 4197  N   PRO A 661    10889  11165   8302  -1471  -1440   -319       N
ATOM   4198  CA  PRO A 661      -6.186   3.670  27.901  1.00 77.77           C
ANISOU 4198  CA  PRO A 661    10652  11017   7879  -1389  -1484   -264       C
ATOM   4199  C   PRO A 661      -7.391   4.139  27.080  1.00 83.06           C
ANISOU 4199  C   PRO A 661    11205  11853   8503  -1405  -1625   -231       C
ATOM   4200  O   PRO A 661      -8.515   3.761  27.416  1.00 81.23           O
ANISOU 4200  O   PRO A 661    10875  11631   8357  -1488  -1684   -273       O
ATOM   4201  CB  PRO A 661      -5.384   2.601  27.172  1.00 83.69           C
ANISOU 4201  CB  PRO A 661    11543  11752   8502  -1420  -1476   -395       C
ATOM   4202  CG  PRO A 661      -6.145   1.364  27.461  1.00 78.93           C
ANISOU 4202  CG  PRO A 661    10928  11093   7968  -1548  -1516   -531       C
ATOM   4203  CD  PRO A 661      -6.573   1.497  28.891  1.00 79.52           C
ANISOU 4203  CD  PRO A 661    10926  11057   8230  -1571  -1451   -475       C
ATOM   4204  N   PRO A 662      -7.174   4.943  26.039  1.00 86.63           N
ANISOU 4204  N   PRO A 662    11658  12436   8823  -1330  -1679   -148       N
ATOM   4205  CA  PRO A 662      -8.314   5.445  25.252  1.00 85.89           C
ANISOU 4205  CA  PRO A 662    11445  12508   8682  -1336  -1820   -100       C
ATOM   4206  C   PRO A 662      -9.085   4.328  24.553  1.00 89.92           C
ANISOU 4206  C   PRO A 662    11952  13100   9115  -1450  -1933   -253       C
ATOM   4207  O   PRO A 662      -8.512   3.326  24.121  1.00 92.25           O
ANISOU 4207  O   PRO A 662    12364  13373   9314  -1497  -1921   -387       O
ATOM   4208  CB  PRO A 662      -7.656   6.393  24.240  1.00 84.07           C
ANISOU 4208  CB  PRO A 662    11249  12391   8303  -1231  -1838     20       C
ATOM   4209  CG  PRO A 662      -6.204   5.993  24.216  1.00 83.68           C
ANISOU 4209  CG  PRO A 662    11355  12259   8181  -1200  -1723    -23       C
ATOM   4210  CD  PRO A 662      -5.899   5.543  25.607  1.00 85.15           C
ANISOU 4210  CD  PRO A 662    11564  12252   8536  -1229  -1609    -71       C
ATOM   4211  N   ILE A 663     -10.398   4.510  24.447  1.00 87.63           N
ANISOU 4211  N   ILE A 663    11519  12900   8874  -1495  -2046   -238       N
ATOM   4212  CA  ILE A 663     -11.246   3.546  23.749  1.00 92.56           C
ANISOU 4212  CA  ILE A 663    12118  13615   9433  -1607  -2172   -379       C
ATOM   4213  C   ILE A 663     -11.204   3.794  22.245  1.00 98.34           C
ANISOU 4213  C   ILE A 663    12874  14546   9944  -1572  -2287   -373       C
ATOM   4214  O   ILE A 663     -11.574   4.882  21.775  1.00 95.82           O
ANISOU 4214  O   ILE A 663    12470  14354   9585  -1497  -2353   -227       O
ATOM   4215  CB  ILE A 663     -12.697   3.569  24.251  1.00 92.83           C
ANISOU 4215  CB  ILE A 663    11981  13675   9616  -1678  -2250   -373       C
ATOM   4216  CG1 ILE A 663     -12.772   3.220  25.733  1.00 85.09           C
ANISOU 4216  CG1 ILE A 663    10976  12514   8838  -1722  -2133   -387       C
ATOM   4217  CG2 ILE A 663     -13.549   2.598  23.452  1.00 92.51           C
ANISOU 4217  CG2 ILE A 663    11909  13734   9505  -1797  -2391   -521       C
ATOM   4218  CD1 ILE A 663     -14.162   3.423  26.304  1.00 83.95           C
ANISOU 4218  CD1 ILE A 663    10648  12403   8845  -1775  -2190   -356       C
ATOM   4219  N   PRO A 664     -10.771   2.807  21.455  1.00101.48           N
ANISOU 4219  N   PRO A 664    13385  14980  10193  -1624  -2315   -528       N
ATOM   4220  CA  PRO A 664     -10.635   3.030  20.019  1.00 96.74           C
ANISOU 4220  CA  PRO A 664    12817  14584   9357  -1586  -2413   -527       C
ATOM   4221  C   PRO A 664     -11.982   3.028  19.340  1.00 94.38           C
ANISOU 4221  C   PRO A 664    12388  14457   9015  -1646  -2593   -549       C
ATOM   4222  O   PRO A 664     -12.965   2.463  19.861  1.00 92.92           O
ANISOU 4222  O   PRO A 664    12112  14223   8970  -1747  -2645   -629       O
ATOM   4223  CB  PRO A 664      -9.777   1.837  19.563  1.00100.36           C
ANISOU 4223  CB  PRO A 664    13433  15002   9696  -1631  -2374   -719       C
ATOM   4224  CG  PRO A 664      -9.254   1.214  20.853  1.00101.04           C
ANISOU 4224  CG  PRO A 664    13577  14842   9971  -1664  -2232   -773       C
ATOM   4225  CD  PRO A 664     -10.303   1.468  21.850  1.00100.49           C
ANISOU 4225  CD  PRO A 664    13367  14706  10109  -1710  -2249   -709       C
ATOM   4226  N   PRO A 665     -12.104   3.663  18.170  1.00 99.95           N
ANISOU 4226  N   PRO A 665    13072  15374   9530  -1589  -2697   -471       N
ATOM   4227  CA  PRO A 665     -13.333   3.549  17.376  1.00 91.24           C
ANISOU 4227  CA  PRO A 665    11854  14458   8354  -1649  -2885   -512       C
ATOM   4228  C   PRO A 665     -13.476   2.162  16.769  1.00 93.97           C
ANISOU 4228  C   PRO A 665    12267  14836   8602  -1763  -2954   -763       C
ATOM   4229  O   PRO A 665     -12.496   1.453  16.529  1.00 95.46           O
ANISOU 4229  O   PRO A 665    12605  14957   8710  -1757  -2869   -886       O
ATOM   4230  CB  PRO A 665     -13.156   4.606  16.279  1.00 93.24           C
ANISOU 4230  CB  PRO A 665    12095  14923   8408  -1540  -2955   -348       C
ATOM   4231  CG  PRO A 665     -12.021   5.493  16.752  1.00 92.99           C
ANISOU 4231  CG  PRO A 665    12133  14784   8414  -1421  -2798   -181       C
ATOM   4232  CD  PRO A 665     -11.140   4.608  17.577  1.00100.11           C
ANISOU 4232  CD  PRO A 665    13159  15474   9405  -1461  -2647   -318       C
ATOM   4233  N   LEU A 666     -14.725   1.804  16.460  1.00 89.89           N
ANISOU 4233  N   LEU A 666    11630  14390   8135  -1830  -3088   -837       N
ATOM   4234  CA  LEU A 666     -15.047   0.467  15.967  1.00 97.19           C
ANISOU 4234  CA  LEU A 666    12593  15287   9047  -1920  -3141  -1079       C
ATOM   4235  C   LEU A 666     -14.677   0.249  14.500  1.00 98.14           C
ANISOU 4235  C   LEU A 666    12800  15543   8945  -1844  -3188  -1159       C
ATOM   4236  O   LEU A 666     -13.902   1.020  13.922  1.00 98.96           O
ANISOU 4236  O   LEU A 666    12967  15736   8897  -1724  -3142  -1035       O
ATOM   4237  CB  LEU A 666     -16.539   0.137  16.124  1.00 94.01           C
ANISOU 4237  CB  LEU A 666    12026  14913   8782  -2022  -3272  -1135       C
ATOM   4238  CG  LEU A 666     -17.275   0.207  17.449  1.00 92.25           C
ANISOU 4238  CG  LEU A 666    11676  14584   8791  -2118  -3259  -1082       C
ATOM   4239  CD1 LEU A 666     -18.701  -0.237  17.220  1.00 92.37           C
ANISOU 4239  CD1 LEU A 666    11538  14658   8899  -2206  -3400  -1164       C
ATOM   4240  CD2 LEU A 666     -16.565  -0.665  18.388  1.00 90.77           C
ANISOU 4240  CD2 LEU A 666    11597  14186   8704  -2200  -3133  -1188       C
ATOM   4241  N   LYS A 667     -15.180  -0.849  13.924  1.00 98.22           N
ANISOU 4241  N   LYS A 667    12818  15556   8944  -1918  -3271  -1371       N
ATOM   4242  CA  LYS A 667     -15.087  -1.156  12.489  1.00 96.87           C
ANISOU 4242  CA  LYS A 667    12710  15526   8572  -1863  -3348  -1472       C
ATOM   4243  C   LYS A 667     -13.673  -1.054  11.928  1.00 99.69           C
ANISOU 4243  C   LYS A 667    13231  15898   8749  -1757  -3234  -1465       C
ATOM   4244  O   LYS A 667     -12.747  -1.675  12.448  1.00100.09           O
ANISOU 4244  O   LYS A 667    13394  15796   8841  -1774  -3111  -1558       O
ATOM   4245  CB  LYS A 667     -16.021  -0.239  11.692  1.00 99.78           C
ANISOU 4245  CB  LYS A 667    12954  16102   8856  -1807  -3489  -1333       C
ATOM   4246  CG  LYS A 667     -17.467  -0.267  12.171  1.00 99.38           C
ANISOU 4246  CG  LYS A 667    12724  16055   8979  -1901  -3607  -1330       C
ATOM   4247  CD  LYS A 667     -18.218  -1.463  11.617  1.00100.87           C
ANISOU 4247  CD  LYS A 667    12898  16245   9184  -2000  -3725  -1565       C
ATOM   4248  CE  LYS A 667     -18.404  -1.372  10.118  1.00 95.46           C
ANISOU 4248  CE  LYS A 667    12237  15753   8280  -1933  -3844  -1597       C
ATOM   4249  NZ  LYS A 667     -19.604  -2.139   9.708  1.00 95.42           N
ANISOU 4249  NZ  LYS A 667    12141  15783   8333  -2031  -4004  -1756       N
TER
ATOM   4250  N   LYS B   3      38.566   3.133  -6.167  1.00 76.70           N
ANISOU 4250  N   LYS B   3    11947  10219   6977      1    309  -2433       N
ATOM   4251  CA  LYS B   3      39.568   3.821  -5.371  1.00 68.92           C
ANISOU 4251  CA  LYS B   3    10910   9196   6081     73    389  -2259       C
ATOM   4252  C   LYS B   3      39.826   3.183  -4.031  1.00 66.34           C
ANISOU 4252  C   LYS B   3    10600   8616   5992     81    389  -2232       C
ATOM   4253  O   LYS B   3      39.235   3.501  -2.999  1.00 67.01           O
ANISOU 4253  O   LYS B   3    10663   8604   6193     19    336  -2100       O
ATOM   4254  CB  LYS B   3      39.204   5.285  -5.271  1.00 70.52           C
ANISOU 4254  CB  LYS B   3    11040   9542   6212     39    370  -2042       C
ATOM   4255  CG  LYS B   3      39.543   5.908  -6.605  1.00 74.31           C
ANISOU 4255  CG  LYS B   3    11502  10272   6460     78    417  -2051       C
ATOM   4256  CD  LYS B   3      39.201   7.353  -6.772  1.00 77.44           C
ANISOU 4256  CD  LYS B   3    11833  10831   6759     52    401  -1847       C
ATOM   4257  CE  LYS B   3      38.955   7.536  -8.247  1.00 74.26           C
ANISOU 4257  CE  LYS B   3    11443  10665   6108     52    395  -1918       C
ATOM   4258  NZ  LYS B   3      37.755   6.769  -8.675  1.00 74.24           N
ANISOU 4258  NZ  LYS B   3    11488  10663   6056    -26    285  -2076       N
ATOM   4259  N   VAL B   4      40.696   2.197  -4.162  1.00 65.21           N
ANISOU 4259  N   VAL B   4    10500   8373   5905    162    448  -2377       N
ATOM   4260  CA  VAL B   4      41.642   1.697  -3.182  1.00 64.51           C
ANISOU 4260  CA  VAL B   4    10414   8096   6000    238    500  -2349       C
ATOM   4261  C   VAL B   4      43.018   1.946  -3.792  1.00 60.63           C
ANISOU 4261  C   VAL B   4     9887   7720   5429    363    615  -2371       C
ATOM   4262  O   VAL B   4      43.133   2.153  -5.000  1.00 64.99           O
ANISOU 4262  O   VAL B   4    10438   8461   5796    383    650  -2456       O
ATOM   4263  CB  VAL B   4      41.362   0.207  -2.880  1.00 66.58           C
ANISOU 4263  CB  VAL B   4    10761   8130   6407    223    461  -2516       C
ATOM   4264  CG1 VAL B   4      41.207  -0.534  -4.132  1.00 61.98           C
ANISOU 4264  CG1 VAL B   4    10233   7611   5706    229    462  -2748       C
ATOM   4265  CG2 VAL B   4      42.508  -0.421  -2.216  1.00 71.41           C
ANISOU 4265  CG2 VAL B   4    11381   8579   7174    331    525  -2526       C
ATOM   4266  N   TYR B   5      44.052   2.018  -2.963  1.00 66.91           N
ANISOU 4266  N   TYR B   5    10645   8425   6353    444    674  -2283       N
ATOM   4267  CA  TYR B   5      45.397   2.303  -3.447  1.00 65.11           C
ANISOU 4267  CA  TYR B   5    10365   8306   6066    560    788  -2289       C
ATOM   4268  C   TYR B   5      46.364   1.210  -3.031  1.00 65.29           C
ANISOU 4268  C   TYR B   5    10411   8154   6242    668    836  -2396       C
ATOM   4269  O   TYR B   5      46.334   0.736  -1.891  1.00 68.43           O
ANISOU 4269  O   TYR B   5    10827   8349   6825    666    796  -2344       O
ATOM   4270  CB  TYR B   5      45.900   3.657  -2.953  1.00 63.99           C
ANISOU 4270  CB  TYR B   5    10130   8264   5920    567    825  -2065       C
ATOM   4271  CG  TYR B   5      44.889   4.743  -3.108  1.00 62.18           C
ANISOU 4271  CG  TYR B   5     9878   8161   5586    463    765  -1934       C
ATOM   4272  CD1 TYR B   5      43.980   5.041  -2.096  1.00 60.32           C
ANISOU 4272  CD1 TYR B   5     9643   7822   5453    376    677  -1816       C
ATOM   4273  CD2 TYR B   5      44.812   5.447  -4.296  1.00 60.39           C
ANISOU 4273  CD2 TYR B   5     9630   8162   5154    454    796  -1932       C
ATOM   4274  CE1 TYR B   5      43.039   6.045  -2.268  1.00 58.65           C
ANISOU 4274  CE1 TYR B   5     9406   7728   5151    290    622  -1702       C
ATOM   4275  CE2 TYR B   5      43.890   6.431  -4.480  1.00 58.51           C
ANISOU 4275  CE2 TYR B   5     9371   8037   4823    369    738  -1809       C
ATOM   4276  CZ  TYR B   5      43.005   6.736  -3.475  1.00 57.37           C
ANISOU 4276  CZ  TYR B   5     9223   7784   4791    290    650  -1698       C
ATOM   4277  OH  TYR B   5      42.087   7.729  -3.693  1.00 55.14           O
ANISOU 4277  OH  TYR B   5     8913   7617   4419    214    593  -1581       O
ATOM   4278  N   LYS B   6      47.212   0.813  -3.972  1.00 67.52           N
ANISOU 4278  N   LYS B   6    10690   8522   6441    765    924  -2543       N
ATOM   4279  CA  LYS B   6      48.277  -0.136  -3.701  1.00 67.40           C
ANISOU 4279  CA  LYS B   6    10682   8366   6561    889    984  -2646       C
ATOM   4280  C   LYS B   6      49.446   0.496  -2.952  1.00 66.73           C
ANISOU 4280  C   LYS B   6    10501   8291   6563    971   1049  -2487       C
ATOM   4281  O   LYS B   6      50.239  -0.235  -2.347  1.00 64.89           O
ANISOU 4281  O   LYS B   6    10263   7902   6488   1067   1074  -2522       O
ATOM   4282  CB  LYS B   6      48.766  -0.724  -5.029  1.00 65.68           C
ANISOU 4282  CB  LYS B   6    10486   8259   6211    968   1062  -2870       C
ATOM   4283  CG  LYS B   6      48.311  -2.149  -5.269  1.00 71.07           C
ANISOU 4283  CG  LYS B   6    11272   8766   6963    972   1018  -3100       C
ATOM   4284  CD  LYS B   6      46.849  -2.159  -5.716  1.00 74.76           C
ANISOU 4284  CD  LYS B   6    11805   9271   7331    830    917  -3151       C
ATOM   4285  CE  LYS B   6      46.388  -3.547  -6.129  1.00 75.66           C
ANISOU 4285  CE  LYS B   6    11982   9243   7523    806    874  -3383       C
ATOM   4286  NZ  LYS B   6      46.000  -4.334  -4.912  1.00 84.08           N
ANISOU 4286  NZ  LYS B   6    13121  10005   8820    783    801  -3359       N
ATOM   4287  N   ASP B   7      49.577   1.826  -2.983  1.00 61.03           N
ANISOU 4287  N   ASP B   7     9698   7742   5747    936   1075  -2314       N
ATOM   4288  CA  ASP B   7      50.794   2.471  -2.495  1.00 56.81           C
ANISOU 4288  CA  ASP B   7     9062   7252   5273   1014   1150  -2188       C
ATOM   4289  C   ASP B   7      50.581   3.976  -2.440  1.00 57.26           C
ANISOU 4289  C   ASP B   7     9047   7468   5240    936   1149  -1987       C
ATOM   4290  O   ASP B   7      49.568   4.507  -2.907  1.00 59.78           O
ANISOU 4290  O   ASP B   7     9396   7880   5437    839   1100  -1953       O
ATOM   4291  CB  ASP B   7      52.016   2.130  -3.364  1.00 58.70           C
ANISOU 4291  CB  ASP B   7     9256   7593   5452   1141   1273  -2316       C
ATOM   4292  CG  ASP B   7      51.808   2.461  -4.845  1.00 65.45           C
ANISOU 4292  CG  ASP B   7    10119   8680   6068   1121   1328  -2405       C
ATOM   4293  OD1 ASP B   7      50.826   3.164  -5.171  1.00 64.09           O
ANISOU 4293  OD1 ASP B   7     9969   8609   5774   1012   1273  -2331       O
ATOM   4294  OD2 ASP B   7      52.636   2.029  -5.693  1.00 64.72           O
ANISOU 4294  OD2 ASP B   7    10008   8678   5903   1219   1428  -2548       O
ATOM   4295  N   LEU B   8      51.578   4.659  -1.888  1.00 54.10           N
ANISOU 4295  N   LEU B   8     8551   7098   4907    984   1203  -1857       N
ATOM   4296  CA  LEU B   8      51.551   6.107  -1.820  1.00 52.87           C
ANISOU 4296  CA  LEU B   8     8320   7081   4688    921   1214  -1668       C
ATOM   4297  C   LEU B   8      51.407   6.728  -3.205  1.00 57.47           C
ANISOU 4297  C   LEU B   8     8893   7893   5050    895   1272  -1684       C
ATOM   4298  O   LEU B   8      50.644   7.683  -3.382  1.00 57.18           O
ANISOU 4298  O   LEU B   8     8853   7947   4926    804   1232  -1566       O
ATOM   4299  CB  LEU B   8      52.826   6.597  -1.135  1.00 51.60           C
ANISOU 4299  CB  LEU B   8     8051   6921   4636    989   1276  -1563       C
ATOM   4300  CG  LEU B   8      52.991   8.113  -1.043  1.00 51.25           C
ANISOU 4300  CG  LEU B   8     7917   7007   4547    929   1299  -1371       C
ATOM   4301  CD1 LEU B   8      51.898   8.715  -0.194  1.00 46.96           C
ANISOU 4301  CD1 LEU B   8     7403   6387   4053    823   1191  -1244       C
ATOM   4302  CD2 LEU B   8      54.364   8.452  -0.497  1.00 53.36           C
ANISOU 4302  CD2 LEU B   8     8071   7283   4921   1002   1368  -1302       C
ATOM   4303  N   ARG B   9      52.119   6.186  -4.202  1.00 59.50           N
ANISOU 4303  N   ARG B   9     9146   8248   5213    978   1366  -1830       N
ATOM   4304  CA  ARG B   9      52.184   6.824  -5.519  1.00 56.93           C
ANISOU 4304  CA  ARG B   9     8799   8165   4667    965   1439  -1832       C
ATOM   4305  C   ARG B   9      50.820   6.868  -6.186  1.00 59.20           C
ANISOU 4305  C   ARG B   9     9171   8515   4807    872   1357  -1867       C
ATOM   4306  O   ARG B   9      50.461   7.868  -6.818  1.00 61.86           O
ANISOU 4306  O   ARG B   9     9486   9025   4993    813   1365  -1758       O
ATOM   4307  CB  ARG B   9      53.193   6.095  -6.411  1.00 63.49           C
ANISOU 4307  CB  ARG B   9     9613   9083   5427   1080   1557  -2005       C
ATOM   4308  CG  ARG B   9      54.553   5.951  -5.752  1.00 66.95           C
ANISOU 4308  CG  ARG B   9     9959   9457   6022   1182   1634  -1984       C
ATOM   4309  CD  ARG B   9      55.705   6.087  -6.718  1.00 63.57           C
ANISOU 4309  CD  ARG B   9     9451   9222   5480   1267   1784  -2038       C
ATOM   4310  NE  ARG B   9      56.874   5.381  -6.202  1.00 70.46           N
ANISOU 4310  NE  ARG B   9    10264   9995   6514   1391   1843  -2113       N
ATOM   4311  CZ  ARG B   9      58.134   5.747  -6.412  1.00 72.64           C
ANISOU 4311  CZ  ARG B   9    10419  10390   6791   1465   1966  -2080       C
ATOM   4312  NH1 ARG B   9      58.439   6.800  -7.160  1.00 74.23           N
ANISOU 4312  NH1 ARG B   9    10550  10815   6839   1425   2053  -1974       N
ATOM   4313  NH2 ARG B   9      59.116   5.046  -5.850  1.00 69.62           N
ANISOU 4313  NH2 ARG B   9     9982   9899   6572   1582   2001  -2149       N
ATOM   4314  N   GLU B  10      50.045   5.792  -6.068  1.00 59.33           N
ANISOU 4314  N   GLU B  10     9281   8393   4868    856   1277  -2018       N
ATOM   4315  CA  GLU B  10      48.683   5.814  -6.590  1.00 59.53           C
ANISOU 4315  CA  GLU B  10     9379   8467   4774    759   1184  -2051       C
ATOM   4316  C   GLU B  10      47.847   6.886  -5.898  1.00 62.09           C
ANISOU 4316  C   GLU B  10     9679   8779   5133    657   1101  -1841       C
ATOM   4317  O   GLU B  10      46.965   7.499  -6.513  1.00 58.94           O
ANISOU 4317  O   GLU B  10     9295   8510   4592    584   1054  -1791       O
ATOM   4318  CB  GLU B  10      48.058   4.431  -6.433  1.00 62.43           C
ANISOU 4318  CB  GLU B  10     9842   8657   5221    754   1111  -2246       C
ATOM   4319  CG  GLU B  10      48.612   3.379  -7.415  1.00 58.70           C
ANISOU 4319  CG  GLU B  10     9410   8225   4669    842   1181  -2490       C
ATOM   4320  CD  GLU B  10      47.604   2.273  -7.739  1.00 66.62           C
ANISOU 4320  CD  GLU B  10    10519   9130   5664    795   1094  -2690       C
ATOM   4321  OE1 GLU B  10      46.712   2.002  -6.888  1.00 69.06           O
ANISOU 4321  OE1 GLU B  10    10869   9265   6106    717    988  -2653       O
ATOM   4322  OE2 GLU B  10      47.720   1.656  -8.828  1.00 68.21           O
ANISOU 4322  OE2 GLU B  10    10740   9418   5757    813   1132  -2870       O
ATOM   4323  N   PHE B  11      48.101   7.125  -4.611  1.00 59.21           N
ANISOU 4323  N   PHE B  11     9276   8262   4957    656   1078  -1720       N
ATOM   4324  CA  PHE B  11      47.356   8.170  -3.931  1.00 57.25           C
ANISOU 4324  CA  PHE B  11     9001   8004   4746    567   1007  -1530       C
ATOM   4325  C   PHE B  11      47.831   9.556  -4.361  1.00 54.97           C
ANISOU 4325  C   PHE B  11     8631   7895   4360    561   1072  -1364       C
ATOM   4326  O   PHE B  11      47.013  10.453  -4.591  1.00 51.66           O
ANISOU 4326  O   PHE B  11     8207   7562   3861    487   1023  -1250       O
ATOM   4327  CB  PHE B  11      47.458   8.009  -2.423  1.00 55.42           C
ANISOU 4327  CB  PHE B  11     8756   7568   4732    565    963  -1458       C
ATOM   4328  CG  PHE B  11      46.560   8.942  -1.673  1.00 50.53           C
ANISOU 4328  CG  PHE B  11     8119   6923   4157    473    883  -1293       C
ATOM   4329  CD1 PHE B  11      45.210   8.997  -1.959  1.00 48.61           C
ANISOU 4329  CD1 PHE B  11     7924   6703   3843    386    795  -1303       C
ATOM   4330  CD2 PHE B  11      47.073   9.789  -0.715  1.00 46.39           C
ANISOU 4330  CD2 PHE B  11     7523   6361   3742    476    895  -1136       C
ATOM   4331  CE1 PHE B  11      44.380   9.855  -1.279  1.00 48.68           C
ANISOU 4331  CE1 PHE B  11     7909   6691   3895    310    726  -1158       C
ATOM   4332  CE2 PHE B  11      46.256  10.656  -0.034  1.00 47.45           C
ANISOU 4332  CE2 PHE B  11     7640   6472   3917    397    826   -997       C
ATOM   4333  CZ  PHE B  11      44.906  10.694  -0.316  1.00 46.14           C
ANISOU 4333  CZ  PHE B  11     7521   6327   3684    317    744  -1007       C
ATOM   4334  N   LEU B  12      49.145   9.749  -4.492  1.00 53.62           N
ANISOU 4334  N   LEU B  12     8393   7781   4201    638   1182  -1345       N
ATOM   4335  CA  LEU B  12      49.654  11.050  -4.906  1.00 51.68           C
ANISOU 4335  CA  LEU B  12     8066   7698   3874    626   1252  -1183       C
ATOM   4336  C   LEU B  12      49.122  11.443  -6.287  1.00 53.95           C
ANISOU 4336  C   LEU B  12     8380   8193   3926    594   1266  -1188       C
ATOM   4337  O   LEU B  12      48.682  12.584  -6.483  1.00 55.42           O
ANISOU 4337  O   LEU B  12     8539   8472   4046    533   1247  -1025       O
ATOM   4338  CB  LEU B  12      51.187  11.055  -4.872  1.00 50.83           C
ANISOU 4338  CB  LEU B  12     7875   7621   3818    715   1374  -1183       C
ATOM   4339  CG  LEU B  12      51.880  10.912  -3.504  1.00 53.45           C
ANISOU 4339  CG  LEU B  12     8156   7779   4373    751   1365  -1140       C
ATOM   4340  CD1 LEU B  12      53.362  11.260  -3.617  1.00 51.52           C
ANISOU 4340  CD1 LEU B  12     7803   7616   4156    822   1487  -1102       C
ATOM   4341  CD2 LEU B  12      51.196  11.710  -2.368  1.00 47.23           C
ANISOU 4341  CD2 LEU B  12     7357   6885   3703    669   1269   -981       C
ATOM   4342  N   GLU B  13      49.123  10.512  -7.254  1.00 57.89           N
ANISOU 4342  N   GLU B  13     8933   8767   4294    635   1294  -1375       N
ATOM   4343  CA  GLU B  13      48.656  10.889  -8.591  1.00 62.50           C
ANISOU 4343  CA  GLU B  13     9541   9570   4635    608   1307  -1381       C
ATOM   4344  C   GLU B  13      47.202  11.361  -8.544  1.00 59.76           C
ANISOU 4344  C   GLU B  13     9237   9224   4247    510   1178  -1303       C
ATOM   4345  O   GLU B  13      46.839  12.363  -9.170  1.00 64.09           O
ANISOU 4345  O   GLU B  13     9765   9929   4659    469   1174  -1167       O
ATOM   4346  CB  GLU B  13      48.777   9.728  -9.595  1.00 65.00           C
ANISOU 4346  CB  GLU B  13     9918   9962   4817    664   1344  -1622       C
ATOM   4347  CG  GLU B  13      48.314   8.404  -9.064  1.00 67.85           C
ANISOU 4347  CG  GLU B  13    10355  10124   5302    673   1268  -1810       C
ATOM   4348  CD  GLU B  13      46.923   8.051  -9.561  1.00 79.66           C
ANISOU 4348  CD  GLU B  13    11933  11645   6691    597   1153  -1899       C
ATOM   4349  OE1 GLU B  13      46.459   6.919  -9.276  1.00 82.37           O
ANISOU 4349  OE1 GLU B  13    12343  11834   7119    593   1090  -2068       O
ATOM   4350  OE2 GLU B  13      46.273   8.894 -10.222  1.00 81.58           O
ANISOU 4350  OE2 GLU B  13    12171  12054   6773    539   1121  -1798       O
ATOM   4351  N   VAL B  14      46.355  10.635  -7.804  1.00 57.74           N
ANISOU 4351  N   VAL B  14     9036   8792   4110    474   1071  -1384       N
ATOM   4352  CA  VAL B  14      44.959  11.027  -7.575  1.00 60.58           C
ANISOU 4352  CA  VAL B  14     9423   9128   4465    382    945  -1313       C
ATOM   4353  C   VAL B  14      44.852  12.418  -6.945  1.00 57.93           C
ANISOU 4353  C   VAL B  14     9021   8791   4199    341    930  -1071       C
ATOM   4354  O   VAL B  14      43.986  13.217  -7.330  1.00 52.66           O
ANISOU 4354  O   VAL B  14     8351   8220   3438    284    871   -965       O
ATOM   4355  CB  VAL B  14      44.265   9.954  -6.716  1.00 55.48           C
ANISOU 4355  CB  VAL B  14     8836   8272   3973    353    853  -1436       C
ATOM   4356  CG1 VAL B  14      43.100  10.537  -5.941  1.00 55.44           C
ANISOU 4356  CG1 VAL B  14     8825   8192   4049    265    741  -1311       C
ATOM   4357  CG2 VAL B  14      43.810   8.833  -7.613  1.00 64.82           C
ANISOU 4357  CG2 VAL B  14    10095   9494   5040    355    825  -1659       C
ATOM   4358  N   LEU B  15      45.698  12.724  -5.953  1.00 51.45           N
ANISOU 4358  N   LEU B  15     8146   7857   3548    368    977   -985       N
ATOM   4359  CA  LEU B  15      45.690  14.067  -5.367  1.00 51.07           C
ANISOU 4359  CA  LEU B  15     8031   7803   3570    331    971   -768       C
ATOM   4360  C   LEU B  15      46.066  15.116  -6.404  1.00 55.04           C
ANISOU 4360  C   LEU B  15     8491   8508   3913    333   1042   -644       C
ATOM   4361  O   LEU B  15      45.465  16.196  -6.454  1.00 53.37           O
ANISOU 4361  O   LEU B  15     8257   8344   3675    283   1000   -484       O
ATOM   4362  CB  LEU B  15      46.648  14.142  -4.181  1.00 50.14           C
ANISOU 4362  CB  LEU B  15     7858   7542   3650    365   1012   -719       C
ATOM   4363  CG  LEU B  15      46.301  13.372  -2.912  1.00 49.35           C
ANISOU 4363  CG  LEU B  15     7789   7233   3731    356    939   -781       C
ATOM   4364  CD1 LEU B  15      47.335  13.690  -1.815  1.00 48.08           C
ANISOU 4364  CD1 LEU B  15     7559   6969   3741    391    983   -702       C
ATOM   4365  CD2 LEU B  15      44.881  13.683  -2.447  1.00 45.15           C
ANISOU 4365  CD2 LEU B  15     7286   6644   3225    274    822   -726       C
ATOM   4366  N   GLU B  16      47.063  14.820  -7.242  1.00 53.33           N
ANISOU 4366  N   GLU B  16     8260   8412   3590    393   1153   -711       N
ATOM   4367  CA  GLU B  16      47.458  15.795  -8.254  1.00 58.74           C
ANISOU 4367  CA  GLU B  16     8905   9299   4114    392   1231   -583       C
ATOM   4368  C   GLU B  16      46.339  16.017  -9.254  1.00 55.28           C
ANISOU 4368  C   GLU B  16     8519   9007   3477    350   1162   -571       C
ATOM   4369  O   GLU B  16      45.966  17.157  -9.550  1.00 59.19           O
ANISOU 4369  O   GLU B  16     8988   9588   3913    309   1145   -389       O
ATOM   4370  CB  GLU B  16      48.721  15.344  -8.976  1.00 60.05           C
ANISOU 4370  CB  GLU B  16     9044   9579   4195    466   1370   -672       C
ATOM   4371  CG  GLU B  16      49.303  16.463  -9.803  1.00 66.48           C
ANISOU 4371  CG  GLU B  16     9797  10581   4880    459   1467   -506       C
ATOM   4372  CD  GLU B  16      50.765  16.248 -10.120  1.00 76.68           C
ANISOU 4372  CD  GLU B  16    11026  11949   6161    528   1619   -548       C
ATOM   4373  OE1 GLU B  16      51.191  15.079 -10.231  1.00 81.67           O
ANISOU 4373  OE1 GLU B  16    11682  12559   6790    594   1654   -749       O
ATOM   4374  OE2 GLU B  16      51.493  17.254 -10.234  1.00 81.47           O
ANISOU 4374  OE2 GLU B  16    11553  12629   6773    515   1705   -380       O
ATOM   4375  N   GLN B  17      45.776  14.928  -9.765  1.00 53.91           N
ANISOU 4375  N   GLN B  17     8418   8859   3207    358   1115   -765       N
ATOM   4376  CA  GLN B  17      44.679  15.017 -10.721  1.00 59.49           C
ANISOU 4376  CA  GLN B  17     9172   9702   3730    314   1035   -776       C
ATOM   4377  C   GLN B  17      43.521  15.850 -10.179  1.00 57.62           C
ANISOU 4377  C   GLN B  17     8929   9416   3550    248    917   -626       C
ATOM   4378  O   GLN B  17      42.840  16.540 -10.947  1.00 56.64           O
ANISOU 4378  O   GLN B  17     8806   9408   3305    211    868   -522       O
ATOM   4379  CB  GLN B  17      44.204  13.609 -11.048  1.00 61.46           C
ANISOU 4379  CB  GLN B  17     9497   9909   3945    317    982  -1023       C
ATOM   4380  CG  GLN B  17      42.824  13.515 -11.632  1.00 62.02           C
ANISOU 4380  CG  GLN B  17     9618  10022   3924    252    853  -1051       C
ATOM   4381  CD  GLN B  17      42.483  12.083 -11.992  1.00 66.36           C
ANISOU 4381  CD  GLN B  17    10241  10521   4453    255    812  -1303       C
ATOM   4382  OE1 GLN B  17      42.184  11.757 -13.139  1.00 71.47           O
ANISOU 4382  OE1 GLN B  17    10927  11262   4965    247    792  -1378       O
ATOM   4383  NE2 GLN B  17      42.510  11.215 -10.983  1.00 72.10           N
ANISOU 4383  NE2 GLN B  17    10989  11086   5319    269    795  -1435       N
ATOM   4384  N   GLU B  18      43.277  15.793  -8.866  1.00 53.89           N
ANISOU 4384  N   GLU B  18     8444   8733   3301    225    863   -606       N
ATOM   4385  CA  GLU B  18      42.149  16.485  -8.262  1.00 55.52           C
ANISOU 4385  CA  GLU B  18     8639   8871   3586    163    751   -486       C
ATOM   4386  C   GLU B  18      42.513  17.875  -7.771  1.00 52.64           C
ANISOU 4386  C   GLU B  18     8204   8483   3313    154    784   -257       C
ATOM   4387  O   GLU B  18      41.699  18.501  -7.088  1.00 51.58           O
ANISOU 4387  O   GLU B  18     8053   8266   3280    112    702   -156       O
ATOM   4388  CB  GLU B  18      41.556  15.659  -7.104  1.00 55.00           C
ANISOU 4388  CB  GLU B  18     8600   8598   3702    135    670   -591       C
ATOM   4389  CG  GLU B  18      40.887  14.359  -7.545  1.00 57.02           C
ANISOU 4389  CG  GLU B  18     8926   8854   3884    122    610   -806       C
ATOM   4390  CD  GLU B  18      39.698  14.582  -8.486  1.00 63.39           C
ANISOU 4390  CD  GLU B  18     9755   9816   4516     77    517   -805       C
ATOM   4391  OE1 GLU B  18      39.004  15.613  -8.356  1.00 65.99           O
ANISOU 4391  OE1 GLU B  18    10047  10177   4851     42    459   -640       O
ATOM   4392  OE2 GLU B  18      39.473  13.737  -9.383  1.00 69.08           O
ANISOU 4392  OE2 GLU B  18    10526  10630   5091     80    501   -972       O
ATOM   4393  N   GLY B  19      43.704  18.372  -8.103  1.00 51.37           N
ANISOU 4393  N   GLY B  19     8001   8393   3125    190    904   -179       N
ATOM   4394  CA  GLY B  19      44.128  19.682  -7.641  1.00 48.35           C
ANISOU 4394  CA  GLY B  19     7549   7977   2843    176    940     31       C
ATOM   4395  C   GLY B  19      44.544  19.741  -6.189  1.00 52.07           C
ANISOU 4395  C   GLY B  19     7982   8245   3558    173    939     46       C
ATOM   4396  O   GLY B  19      44.697  20.836  -5.634  1.00 45.42           O
ANISOU 4396  O   GLY B  19     7085   7346   2825    150    945    207       O
ATOM   4397  N   GLN B  20      44.783  18.587  -5.569  1.00 51.16           N
ANISOU 4397  N   GLN B  20     7893   8017   3529    198    935   -119       N
ATOM   4398  CA  GLN B  20      45.116  18.500  -4.154  1.00 46.72           C
ANISOU 4398  CA  GLN B  20     7301   7266   3185    198    922   -118       C
ATOM   4399  C   GLN B  20      46.593  18.199  -3.913  1.00 48.95           C
ANISOU 4399  C   GLN B  20     7539   7525   3536    254   1031   -155       C
ATOM   4400  O   GLN B  20      46.962  17.730  -2.836  1.00 44.22           O
ANISOU 4400  O   GLN B  20     6928   6779   3095    271   1021   -205       O
ATOM   4401  CB  GLN B  20      44.234  17.448  -3.479  1.00 44.28           C
ANISOU 4401  CB  GLN B  20     7051   6828   2945    181    827   -255       C
ATOM   4402  CG  GLN B  20      42.813  17.913  -3.355  1.00 45.98           C
ANISOU 4402  CG  GLN B  20     7284   7036   3151    121    716   -195       C
ATOM   4403  CD  GLN B  20      42.709  19.178  -2.507  1.00 48.83           C
ANISOU 4403  CD  GLN B  20     7585   7328   3641     92    697    -21       C
ATOM   4404  OE1 GLN B  20      41.959  20.099  -2.842  1.00 47.52           O
ANISOU 4404  OE1 GLN B  20     7405   7221   3428     61    652     96       O
ATOM   4405  NE2 GLN B  20      43.475  19.230  -1.404  1.00 43.63           N
ANISOU 4405  NE2 GLN B  20     6889   6542   3147    107    730     -6       N
ATOM   4406  N   LEU B  21      47.453  18.470  -4.881  1.00 49.61           N
ANISOU 4406  N   LEU B  21     7591   7756   3502    284   1135   -126       N
ATOM   4407  CA  LEU B  21      48.881  18.288  -4.661  1.00 55.28           C
ANISOU 4407  CA  LEU B  21     8247   8463   4291    336   1243   -150       C
ATOM   4408  C   LEU B  21      49.630  19.388  -5.388  1.00 56.03           C
ANISOU 4408  C   LEU B  21     8274   8701   4314    328   1343      2       C
ATOM   4409  O   LEU B  21      49.312  19.695  -6.537  1.00 52.69           O
ANISOU 4409  O   LEU B  21     7874   8440   3707    317   1365     44       O
ATOM   4410  CB  LEU B  21      49.356  16.912  -5.147  1.00 52.90           C
ANISOU 4410  CB  LEU B  21     7985   8191   3922    405   1290   -352       C
ATOM   4411  CG  LEU B  21      50.822  16.600  -4.857  1.00 54.78           C
ANISOU 4411  CG  LEU B  21     8153   8410   4249    472   1396   -393       C
ATOM   4412  CD1 LEU B  21      50.997  15.145  -4.479  1.00 54.37           C
ANISOU 4412  CD1 LEU B  21     8147   8250   4260    535   1380   -590       C
ATOM   4413  CD2 LEU B  21      51.721  16.965  -6.055  1.00 55.33           C
ANISOU 4413  CD2 LEU B  21     8175   8682   4167    501   1529   -362       C
ATOM   4414  N   ILE B  22      50.626  19.957  -4.720  1.00 58.56           N
ANISOU 4414  N   ILE B  22     8509   8965   4776    331   1402     85       N
ATOM   4415  CA  ILE B  22      51.462  21.022  -5.255  1.00 57.69           C
ANISOU 4415  CA  ILE B  22     8320   8966   4635    315   1505    237       C
ATOM   4416  C   ILE B  22      52.854  20.455  -5.487  1.00 57.59           C
ANISOU 4416  C   ILE B  22     8245   9013   4623    378   1629    153       C
ATOM   4417  O   ILE B  22      53.411  19.788  -4.601  1.00 56.10           O
ANISOU 4417  O   ILE B  22     8031   8707   4576    419   1624     56       O
ATOM   4418  CB  ILE B  22      51.517  22.205  -4.271  1.00 61.12           C
ANISOU 4418  CB  ILE B  22     8692   9282   5249    259   1473    397       C
ATOM   4419  CG1 ILE B  22      50.263  23.075  -4.390  1.00 62.86           C
ANISOU 4419  CG1 ILE B  22     8954   9493   5436    200   1383    521       C
ATOM   4420  CG2 ILE B  22      52.785  23.037  -4.495  1.00 61.30           C
ANISOU 4420  CG2 ILE B  22     8610   9372   5309    250   1595    515       C
ATOM   4421  CD1 ILE B  22      50.283  24.277  -3.450  1.00 60.12           C
ANISOU 4421  CD1 ILE B  22     8548   9024   5270    148   1352    669       C
ATOM   4422  N   ARG B  23      53.427  20.718  -6.662  1.00 64.94           N
ANISOU 4422  N   ARG B  23     9148  10130   5396    389   1741    194       N
ATOM   4423  CA  ARG B  23      54.816  20.362  -6.938  1.00 62.48           C
ANISOU 4423  CA  ARG B  23     8756   9896   5085    446   1876    137       C
ATOM   4424  C   ARG B  23      55.711  21.587  -6.767  1.00 64.86           C
ANISOU 4424  C   ARG B  23     8943  10220   5479    400   1957    321       C
ATOM   4425  O   ARG B  23      55.468  22.630  -7.382  1.00 63.75           O
ANISOU 4425  O   ARG B  23     8795  10168   5259    341   1981    489       O
ATOM   4426  CB  ARG B  23      54.993  19.787  -8.337  1.00 64.38           C
ANISOU 4426  CB  ARG B  23     9029  10340   5091    491   1965     47       C
ATOM   4427  CG  ARG B  23      54.911  18.291  -8.387  1.00 70.09           C
ANISOU 4427  CG  ARG B  23     9816  11033   5784    569   1945   -193       C
ATOM   4428  CD  ARG B  23      54.440  17.812  -9.753  1.00 76.18           C
ANISOU 4428  CD  ARG B  23    10661  11987   6296    589   1971   -285       C
ATOM   4429  NE  ARG B  23      54.231  16.369  -9.762  1.00 75.68           N
ANISOU 4429  NE  ARG B  23    10670  11868   6217    656   1937   -526       N
ATOM   4430  CZ  ARG B  23      55.178  15.462  -9.562  1.00 78.27           C
ANISOU 4430  CZ  ARG B  23    10962  12158   6617    741   2006   -676       C
ATOM   4431  NH1 ARG B  23      56.456  15.797  -9.477  1.00 74.13           N
ANISOU 4431  NH1 ARG B  23    10326  11682   6158    775   2126   -623       N
ATOM   4432  NH2 ARG B  23      54.834  14.184  -9.438  1.00 84.78           N
ANISOU 4432  NH2 ARG B  23    11863  12891   7458    794   1953   -885       N
ATOM   4433  N   VAL B  24      56.730  21.461  -5.920  1.00 65.36           N
ANISOU 4433  N   VAL B  24     8918  10200   5717    426   1994    292       N
ATOM   4434  CA  VAL B  24      57.782  22.461  -5.796  1.00 64.02           C
ANISOU 4434  CA  VAL B  24     8623  10062   5640    388   2087    435       C
ATOM   4435  C   VAL B  24      58.951  21.933  -6.616  1.00 64.67           C
ANISOU 4435  C   VAL B  24     8635  10305   5630    451   2237    360       C
ATOM   4436  O   VAL B  24      59.669  21.026  -6.186  1.00 67.56           O
ANISOU 4436  O   VAL B  24     8963  10633   6074    527   2261    216       O
ATOM   4437  CB  VAL B  24      58.178  22.714  -4.340  1.00 60.22           C
ANISOU 4437  CB  VAL B  24     8075   9400   5406    372   2027    450       C
ATOM   4438  CG1 VAL B  24      59.203  23.832  -4.277  1.00 60.99           C
ANISOU 4438  CG1 VAL B  24     8041   9534   5599    318   2118    600       C
ATOM   4439  CG2 VAL B  24      56.954  23.055  -3.498  1.00 61.42           C
ANISOU 4439  CG2 VAL B  24     8303   9395   5637    323   1878    489       C
ATOM   4440  N   LYS B  25      59.121  22.484  -7.818  1.00 67.54           N
ANISOU 4440  N   LYS B  25     8985  10857   5822    425   2340    458       N
ATOM   4441  CA  LYS B  25      60.140  21.988  -8.739  1.00 71.18           C
ANISOU 4441  CA  LYS B  25     9384  11500   6160    485   2494    384       C
ATOM   4442  C   LYS B  25      61.537  22.493  -8.394  1.00 72.25           C
ANISOU 4442  C   LYS B  25     9360  11653   6438    475   2606    454       C
ATOM   4443  O   LYS B  25      62.518  21.781  -8.629  1.00 71.75           O
ANISOU 4443  O   LYS B  25     9225  11672   6363    552   2708    336       O
ATOM   4444  CB  LYS B  25      59.769  22.373 -10.172  1.00 73.26           C
ANISOU 4444  CB  LYS B  25     9697  11945   6194    447   2545    458       C
ATOM   4445  CG  LYS B  25      58.469  21.754 -10.651  1.00 72.01           C
ANISOU 4445  CG  LYS B  25     9686  11782   5891    456   2432    359       C
ATOM   4446  CD  LYS B  25      58.503  21.511 -12.132  1.00 73.72           C
ANISOU 4446  CD  LYS B  25     9943  12148   5918    448   2481    311       C
ATOM   4447  CE  LYS B  25      57.792  20.225 -12.503  1.00 80.78           C
ANISOU 4447  CE  LYS B  25    10949  13045   6699    508   2415     91       C
ATOM   4448  NZ  LYS B  25      58.370  19.629 -13.752  1.00 77.91           N
ANISOU 4448  NZ  LYS B  25    10588  12822   6191    541   2511    -24       N
ATOM   4449  N   GLU B  26      61.644  23.687  -7.816  1.00 73.71           N
ANISOU 4449  N   GLU B  26     9482  11757   6766    385   2585    635       N
ATOM   4450  CA  GLU B  26      62.926  24.287  -7.488  1.00 70.03           C
ANISOU 4450  CA  GLU B  26     8858  11306   6444    356   2684    715       C
ATOM   4451  C   GLU B  26      63.478  23.705  -6.190  1.00 72.10           C
ANISOU 4451  C   GLU B  26     9059  11412   6924    406   2623    594       C
ATOM   4452  O   GLU B  26      62.739  23.217  -5.328  1.00 72.60           O
ANISOU 4452  O   GLU B  26     9205  11316   7065    429   2485    511       O
ATOM   4453  CB  GLU B  26      62.792  25.804  -7.362  1.00 66.18           C
ANISOU 4453  CB  GLU B  26     8331  10777   6036    234   2678    949       C
ATOM   4454  CG  GLU B  26      61.927  26.246  -6.188  1.00 71.42           C
ANISOU 4454  CG  GLU B  26     9049  11220   6866    187   2513    985       C
ATOM   4455  CD  GLU B  26      62.189  27.686  -5.777  1.00 76.88           C
ANISOU 4455  CD  GLU B  26     9660  11838   7711     77   2519   1183       C
ATOM   4456  OE1 GLU B  26      63.145  28.298  -6.311  1.00 80.93           O
ANISOU 4456  OE1 GLU B  26    10064  12460   8226     33   2652   1291       O
ATOM   4457  OE2 GLU B  26      61.453  28.193  -4.902  1.00 77.78           O
ANISOU 4457  OE2 GLU B  26     9818  11783   7952     33   2394   1225       O
ATOM   4458  N   GLU B  27      64.802  23.771  -6.065  1.00 72.06           N
ANISOU 4458  N   GLU B  27     8904  11464   7014    421   2729    591       N
ATOM   4459  CA  GLU B  27      65.496  23.237  -4.902  1.00 69.07           C
ANISOU 4459  CA  GLU B  27     8445  10964   6834    476   2683    485       C
ATOM   4460  C   GLU B  27      65.164  24.056  -3.661  1.00 68.63           C
ANISOU 4460  C   GLU B  27     8379  10723   6975    395   2558    578       C
ATOM   4461  O   GLU B  27      65.042  25.283  -3.715  1.00 67.48           O
ANISOU 4461  O   GLU B  27     8204  10568   6867    288   2566    749       O
ATOM   4462  CB  GLU B  27      67.000  23.244  -5.165  1.00 72.75           C
ANISOU 4462  CB  GLU B  27     8735  11558   7348    503   2833    478       C
ATOM   4463  CG  GLU B  27      67.887  22.965  -3.969  1.00 71.41           C
ANISOU 4463  CG  GLU B  27     8447  11283   7401    543   2792    409       C
ATOM   4464  CD  GLU B  27      69.339  23.320  -4.270  1.00 78.32           C
ANISOU 4464  CD  GLU B  27     9128  12296   8336    536   2944    449       C
ATOM   4465  OE1 GLU B  27      69.700  24.515  -4.153  1.00 83.18           O
ANISOU 4465  OE1 GLU B  27     9651  12917   9039    422   2977    611       O
ATOM   4466  OE2 GLU B  27      70.112  22.417  -4.658  1.00 81.21           O
ANISOU 4466  OE2 GLU B  27     9430  12766   8661    644   3035    319       O
ATOM   4467  N   VAL B  28      64.984  23.367  -2.541  1.00 66.69           N
ANISOU 4467  N   VAL B  28     8161  10326   6852    448   2440    464       N
ATOM   4468  CA  VAL B  28      64.710  24.035  -1.281  1.00 61.16           C
ANISOU 4468  CA  VAL B  28     7448   9457   6333    383   2320    527       C
ATOM   4469  C   VAL B  28      65.775  23.615  -0.281  1.00 63.16           C
ANISOU 4469  C   VAL B  28     7580   9658   6761    436   2306    446       C
ATOM   4470  O   VAL B  28      66.427  22.578  -0.427  1.00 59.58           O
ANISOU 4470  O   VAL B  28     7091   9258   6289    542   2354    317       O
ATOM   4471  CB  VAL B  28      63.303  23.719  -0.746  1.00 62.12           C
ANISOU 4471  CB  VAL B  28     7729   9440   6435    384   2170    488       C
ATOM   4472  CG1 VAL B  28      62.243  24.178  -1.747  1.00 67.35           C
ANISOU 4472  CG1 VAL B  28     8500  10164   6927    333   2175    574       C
ATOM   4473  CG2 VAL B  28      63.169  22.230  -0.440  1.00 54.06           C
ANISOU 4473  CG2 VAL B  28     6774   8373   5394    499   2120    304       C
ATOM   4474  N   ASN B  29      65.973  24.458   0.723  1.00 61.23           N
ANISOU 4474  N   ASN B  29     7266   9311   6687    363   2241    521       N
ATOM   4475  CA  ASN B  29      66.795  24.063   1.850  1.00 60.02           C
ANISOU 4475  CA  ASN B  29     7014   9091   6700    411   2191    443       C
ATOM   4476  C   ASN B  29      66.005  23.080   2.714  1.00 57.55           C
ANISOU 4476  C   ASN B  29     6821   8644   6400    483   2053    328       C
ATOM   4477  O   ASN B  29      64.782  23.175   2.792  1.00 52.59           O
ANISOU 4477  O   ASN B  29     6329   7937   5714    450   1971    348       O
ATOM   4478  CB  ASN B  29      67.175  25.286   2.672  1.00 59.23           C
ANISOU 4478  CB  ASN B  29     6810   8924   6770    304   2154    549       C
ATOM   4479  CG  ASN B  29      68.015  26.272   1.886  1.00 64.40           C
ANISOU 4479  CG  ASN B  29     7336   9698   7436    222   2291    670       C
ATOM   4480  OD1 ASN B  29      68.798  25.884   1.034  1.00 60.76           O
ANISOU 4480  OD1 ASN B  29     6801   9382   6902    268   2420    647       O
ATOM   4481  ND2 ASN B  29      67.836  27.560   2.159  1.00 67.81           N
ANISOU 4481  ND2 ASN B  29     7741  10066   7958     98   2267    802       N
ATOM   4482  N   PRO B  30      66.670  22.098   3.338  1.00 57.28           N
ANISOU 4482  N   PRO B  30     6740   8585   6440    586   2028    211       N
ATOM   4483  CA  PRO B  30      65.919  21.190   4.224  1.00 52.93           C
ANISOU 4483  CA  PRO B  30     6304   7897   5911    647   1895    120       C
ATOM   4484  C   PRO B  30      65.209  21.925   5.354  1.00 53.61           C
ANISOU 4484  C   PRO B  30     6429   7851   6091    563   1765    186       C
ATOM   4485  O   PRO B  30      64.048  21.610   5.658  1.00 56.03           O
ANISOU 4485  O   PRO B  30     6874   8062   6351    560   1674    165       O
ATOM   4486  CB  PRO B  30      66.993  20.218   4.741  1.00 52.81           C
ANISOU 4486  CB  PRO B  30     6195   7884   5986    765   1899     14       C
ATOM   4487  CG  PRO B  30      68.315  20.796   4.335  1.00 55.90           C
ANISOU 4487  CG  PRO B  30     6402   8405   6430    750   2017     56       C
ATOM   4488  CD  PRO B  30      68.097  21.746   3.218  1.00 58.08           C
ANISOU 4488  CD  PRO B  30     6681   8784   6603    654   2121    162       C
ATOM   4489  N   GLU B  31      65.865  22.919   5.961  1.00 48.07           N
ANISOU 4489  N   GLU B  31     5604   7143   5519    492   1758    260       N
ATOM   4490  CA  GLU B  31      65.321  23.768   7.004  1.00 51.41           C
ANISOU 4490  CA  GLU B  31     6043   7452   6038    407   1648    319       C
ATOM   4491  C   GLU B  31      65.560  25.219   6.634  1.00 51.58           C
ANISOU 4491  C   GLU B  31     5985   7510   6104    286   1706    447       C
ATOM   4492  O   GLU B  31      66.657  25.563   6.182  1.00 56.90           O
ANISOU 4492  O   GLU B  31     6521   8280   6817    271   1807    478       O
ATOM   4493  CB  GLU B  31      65.956  23.521   8.383  1.00 54.66           C
ANISOU 4493  CB  GLU B  31     6375   7800   6594    442   1556    266       C
ATOM   4494  CG  GLU B  31      65.926  22.105   8.826  1.00 54.72           C
ANISOU 4494  CG  GLU B  31     6439   7768   6583    565   1502    153       C
ATOM   4495  CD  GLU B  31      67.219  21.368   8.552  1.00 55.33           C
ANISOU 4495  CD  GLU B  31     6396   7933   6692    666   1577     88       C
ATOM   4496  OE1 GLU B  31      68.301  21.998   8.456  1.00 56.77           O
ANISOU 4496  OE1 GLU B  31     6419   8198   6953    636   1642    124       O
ATOM   4497  OE2 GLU B  31      67.132  20.139   8.411  1.00 56.35           O
ANISOU 4497  OE2 GLU B  31     6590   8047   6771    776   1572     -3       O
ATOM   4498  N   PRO B  32      64.568  26.102   6.866  1.00 53.44           N
ANISOU 4498  N   PRO B  32     6296   7661   6346    197   1644    523       N
ATOM   4499  CA  PRO B  32      63.309  25.679   7.471  1.00 49.24           C
ANISOU 4499  CA  PRO B  32     5910   7022   5776    215   1527    481       C
ATOM   4500  C   PRO B  32      62.201  25.431   6.438  1.00 49.13           C
ANISOU 4500  C   PRO B  32     6035   7033   5600    220   1550    500       C
ATOM   4501  O   PRO B  32      61.021  25.428   6.794  1.00 47.52           O
ANISOU 4501  O   PRO B  32     5944   6745   5366    203   1462    499       O
ATOM   4502  CB  PRO B  32      62.976  26.870   8.362  1.00 49.26           C
ANISOU 4502  CB  PRO B  32     5893   6927   5898    118   1450    547       C
ATOM   4503  CG  PRO B  32      63.367  28.034   7.504  1.00 48.91           C
ANISOU 4503  CG  PRO B  32     5775   6940   5870     29   1548    668       C
ATOM   4504  CD  PRO B  32      64.599  27.570   6.704  1.00 51.02           C
ANISOU 4504  CD  PRO B  32     5935   7343   6108     75   1673    652       C
ATOM   4505  N   ASP B  33      62.580  25.229   5.176  1.00 50.33           N
ANISOU 4505  N   ASP B  33     6172   7310   5642    242   1667    515       N
ATOM   4506  CA  ASP B  33      61.623  25.378   4.076  1.00 50.99           C
ANISOU 4506  CA  ASP B  33     6362   7441   5571    219   1699    567       C
ATOM   4507  C   ASP B  33      60.556  24.292   4.106  1.00 44.43           C
ANISOU 4507  C   ASP B  33     5676   6564   4641    281   1624    468       C
ATOM   4508  O   ASP B  33      59.372  24.565   3.886  1.00 44.82           O
ANISOU 4508  O   ASP B  33     5829   6580   4621    243   1572    508       O
ATOM   4509  CB  ASP B  33      62.352  25.357   2.731  1.00 51.40           C
ANISOU 4509  CB  ASP B  33     6360   7655   5515    233   1846    597       C
ATOM   4510  CG  ASP B  33      63.351  26.488   2.591  1.00 57.10           C
ANISOU 4510  CG  ASP B  33     6938   8427   6331    156   1931    712       C
ATOM   4511  OD1 ASP B  33      63.214  27.491   3.321  1.00 57.03           O
ANISOU 4511  OD1 ASP B  33     6898   8323   6450     74   1873    790       O
ATOM   4512  OD2 ASP B  33      64.291  26.358   1.769  1.00 62.98           O
ANISOU 4512  OD2 ASP B  33     7596   9306   7026    177   2058    719       O
ATOM   4513  N   ILE B  34      60.960  23.043   4.331  1.00 46.14           N
ANISOU 4513  N   ILE B  34     5900   6780   4853    378   1620    340       N
ATOM   4514  CA  ILE B  34      59.995  21.956   4.235  1.00 43.54           C
ANISOU 4514  CA  ILE B  34     5706   6408   4430    432   1561    244       C
ATOM   4515  C   ILE B  34      58.956  22.056   5.339  1.00 41.62           C
ANISOU 4515  C   ILE B  34     5540   6024   4250    397   1427    248       C
ATOM   4516  O   ILE B  34      57.765  21.794   5.118  1.00 45.09           O
ANISOU 4516  O   ILE B  34     6096   6431   4605    384   1374    234       O
ATOM   4517  CB  ILE B  34      60.706  20.596   4.251  1.00 48.60           C
ANISOU 4517  CB  ILE B  34     6335   7061   5069    547   1588    108       C
ATOM   4518  CG1 ILE B  34      61.567  20.441   2.994  1.00 46.32           C
ANISOU 4518  CG1 ILE B  34     5984   6928   4688    586   1730     90       C
ATOM   4519  CG2 ILE B  34      59.686  19.466   4.401  1.00 45.19           C
ANISOU 4519  CG2 ILE B  34     6044   6546   4579    593   1509      7       C
ATOM   4520  CD1 ILE B  34      62.532  19.296   3.069  1.00 44.79           C
ANISOU 4520  CD1 ILE B  34     5739   6751   4527    703   1771    -35       C
ATOM   4521  N   ALA B  35      59.379  22.428   6.542  1.00 40.88           N
ANISOU 4521  N   ALA B  35     5378   5853   4300    380   1370    264       N
ATOM   4522  CA  ALA B  35      58.423  22.585   7.641  1.00 39.07           C
ANISOU 4522  CA  ALA B  35     5215   5503   4129    345   1250    268       C
ATOM   4523  C   ALA B  35      57.530  23.797   7.420  1.00 41.97           C
ANISOU 4523  C   ALA B  35     5612   5855   4480    251   1231    373       C
ATOM   4524  O   ALA B  35      56.317  23.726   7.640  1.00 44.53           O
ANISOU 4524  O   ALA B  35     6034   6118   4766    231   1157    370       O
ATOM   4525  CB  ALA B  35      59.165  22.705   8.971  1.00 40.22           C
ANISOU 4525  CB  ALA B  35     5275   5586   4420    353   1195    254       C
ATOM   4526  N   ALA B  36      58.113  24.911   6.966  1.00 41.84           N
ANISOU 4526  N   ALA B  36     5508   5891   4497    194   1298    471       N
ATOM   4527  CA  ALA B  36      57.327  26.104   6.663  1.00 47.17           C
ANISOU 4527  CA  ALA B  36     6209   6548   5166    110   1286    582       C
ATOM   4528  C   ALA B  36      56.277  25.822   5.594  1.00 43.59           C
ANISOU 4528  C   ALA B  36     5866   6145   4553    116   1295    596       C
ATOM   4529  O   ALA B  36      55.153  26.328   5.674  1.00 43.76           O
ANISOU 4529  O   ALA B  36     5952   6115   4559     75   1232    643       O
ATOM   4530  CB  ALA B  36      58.243  27.244   6.227  1.00 44.45           C
ANISOU 4530  CB  ALA B  36     5752   6255   4884     50   1371    689       C
ATOM   4531  N   ALA B  37      56.619  25.015   4.586  1.00 44.60           N
ANISOU 4531  N   ALA B  37     6009   6378   4558    170   1370    549       N
ATOM   4532  CA  ALA B  37      55.614  24.616   3.608  1.00 44.95           C
ANISOU 4532  CA  ALA B  37     6160   6477   4441    180   1366    539       C
ATOM   4533  C   ALA B  37      54.536  23.748   4.247  1.00 44.71           C
ANISOU 4533  C   ALA B  37     6232   6356   4398    205   1260    445       C
ATOM   4534  O   ALA B  37      53.348  23.874   3.910  1.00 42.52           O
ANISOU 4534  O   ALA B  37     6037   6074   4045    178   1209    467       O
ATOM   4535  CB  ALA B  37      56.265  23.891   2.437  1.00 47.00           C
ANISOU 4535  CB  ALA B  37     6413   6873   4572    236   1471    487       C
ATOM   4536  N   GLY B  38      54.925  22.872   5.179  1.00 42.56           N
ANISOU 4536  N   GLY B  38     5954   6013   4204    255   1223    346       N
ATOM   4537  CA  GLY B  38      53.927  22.088   5.894  1.00 38.72           C
ANISOU 4537  CA  GLY B  38     5560   5431   3721    269   1124    271       C
ATOM   4538  C   GLY B  38      52.988  22.964   6.702  1.00 40.54           C
ANISOU 4538  C   GLY B  38     5808   5577   4017    202   1039    339       C
ATOM   4539  O   GLY B  38      51.764  22.825   6.630  1.00 42.10           O
ANISOU 4539  O   GLY B  38     6088   5748   4159    181    979    332       O
ATOM   4540  N   ARG B  39      53.555  23.897   7.471  1.00 40.78           N
ANISOU 4540  N   ARG B  39     5756   5569   4171    168   1034    399       N
ATOM   4541  CA  ARG B  39      52.740  24.832   8.243  1.00 39.18           C
ANISOU 4541  CA  ARG B  39     5560   5286   4040    108    961    457       C
ATOM   4542  C   ARG B  39      51.876  25.668   7.321  1.00 39.31           C
ANISOU 4542  C   ARG B  39     5610   5340   3985     61    969    549       C
ATOM   4543  O   ARG B  39      50.719  25.954   7.630  1.00 37.78           O
ANISOU 4543  O   ARG B  39     5470   5095   3791     33    900    565       O
ATOM   4544  CB  ARG B  39      53.639  25.735   9.091  1.00 40.40           C
ANISOU 4544  CB  ARG B  39     5611   5402   4338     77    963    497       C
ATOM   4545  CG  ARG B  39      52.932  26.815   9.913  1.00 38.79           C
ANISOU 4545  CG  ARG B  39     5402   5112   4222     16    896    548       C
ATOM   4546  CD  ARG B  39      52.185  26.246  11.088  1.00 39.80           C
ANISOU 4546  CD  ARG B  39     5585   5163   4375     30    803    475       C
ATOM   4547  NE  ARG B  39      50.825  25.916  10.700  1.00 40.39           N
ANISOU 4547  NE  ARG B  39     5756   5232   4358     26    765    471       N
ATOM   4548  CZ  ARG B  39      49.922  25.394  11.515  1.00 37.57           C
ANISOU 4548  CZ  ARG B  39     5459   4818   4000     30    691    419       C
ATOM   4549  NH1 ARG B  39      50.217  25.105  12.778  1.00 35.04           N
ANISOU 4549  NH1 ARG B  39     5119   4442   3752     42    646    369       N
ATOM   4550  NH2 ARG B  39      48.691  25.180  11.058  1.00 35.85           N
ANISOU 4550  NH2 ARG B  39     5315   4604   3702     19    662    420       N
ATOM   4551  N   ALA B  40      52.433  26.074   6.181  1.00 43.65           N
ANISOU 4551  N   ALA B  40     6126   5985   4472     55   1057    615       N
ATOM   4552  CA  ALA B  40      51.713  26.950   5.277  1.00 39.55           C
ANISOU 4552  CA  ALA B  40     5633   5509   3886     13   1067    723       C
ATOM   4553  C   ALA B  40      50.571  26.213   4.597  1.00 40.92           C
ANISOU 4553  C   ALA B  40     5908   5725   3914     33   1029    680       C
ATOM   4554  O   ALA B  40      49.467  26.749   4.457  1.00 40.88           O
ANISOU 4554  O   ALA B  40     5945   5702   3885      3    974    736       O
ATOM   4555  CB  ALA B  40      52.686  27.549   4.266  1.00 47.36           C
ANISOU 4555  CB  ALA B  40     6555   6596   4841     -2   1176    814       C
ATOM   4556  N   ALA B  41      50.819  24.984   4.143  1.00 41.73           N
ANISOU 4556  N   ALA B  41     6048   5885   3923     86   1057    576       N
ATOM   4557  CA  ALA B  41      49.735  24.212   3.542  1.00 43.06           C
ANISOU 4557  CA  ALA B  41     6312   6089   3961    100   1014    516       C
ATOM   4558  C   ALA B  41      48.612  23.992   4.546  1.00 43.75           C
ANISOU 4558  C   ALA B  41     6448   6066   4107     83    906    475       C
ATOM   4559  O   ALA B  41      47.429  24.089   4.195  1.00 46.65           O
ANISOU 4559  O   ALA B  41     6870   6447   4408     60    851    492       O
ATOM   4560  CB  ALA B  41      50.254  22.886   2.994  1.00 40.94           C
ANISOU 4560  CB  ALA B  41     6073   5880   3602    162   1060    391       C
ATOM   4561  N   ALA B  42      48.956  23.735   5.812  1.00 38.15           N
ANISOU 4561  N   ALA B  42     5715   5257   3523     91    874    428       N
ATOM   4562  CA  ALA B  42      47.909  23.670   6.837  1.00 43.52           C
ANISOU 4562  CA  ALA B  42     6433   5841   4262     68    780    405       C
ATOM   4563  C   ALA B  42      47.154  25.005   6.967  1.00 47.57           C
ANISOU 4563  C   ALA B  42     6926   6330   4817     16    743    511       C
ATOM   4564  O   ALA B  42      45.926  25.022   7.115  1.00 43.24           O
ANISOU 4564  O   ALA B  42     6423   5758   4249     -4    677    509       O
ATOM   4565  CB  ALA B  42      48.511  23.243   8.173  1.00 38.88           C
ANISOU 4565  CB  ALA B  42     5818   5165   3790     88    756    349       C
ATOM   4566  N   ASN B  43      47.863  26.136   6.880  1.00 41.79           N
ANISOU 4566  N   ASN B  43     6124   5605   4151     -5    788    606       N
ATOM   4567  CA  ASN B  43      47.240  27.430   7.105  1.00 44.83           C
ANISOU 4567  CA  ASN B  43     6485   5943   4603    -49    754    703       C
ATOM   4568  C   ASN B  43      46.328  27.892   5.971  1.00 52.19           C
ANISOU 4568  C   ASN B  43     7455   6942   5432    -62    747    784       C
ATOM   4569  O   ASN B  43      45.588  28.855   6.175  1.00 53.46           O
ANISOU 4569  O   ASN B  43     7608   7057   5649    -88    705    858       O
ATOM   4570  CB  ASN B  43      48.305  28.494   7.352  1.00 49.36           C
ANISOU 4570  CB  ASN B  43     6973   6491   5292    -74    804    778       C
ATOM   4571  CG  ASN B  43      48.954  28.355   8.699  1.00 45.92           C
ANISOU 4571  CG  ASN B  43     6492   5976   4980    -72    782    710       C
ATOM   4572  OD1 ASN B  43      48.536  27.526   9.538  1.00 46.15           O
ANISOU 4572  OD1 ASN B  43     6559   5964   5013    -51    726    619       O
ATOM   4573  ND2 ASN B  43      50.007  29.143   8.922  1.00 41.29           N
ANISOU 4573  ND2 ASN B  43     5821   5373   4494    -95    825    755       N
ATOM   4574  N   LEU B  44      46.334  27.241   4.803  1.00 49.12           N
ANISOU 4574  N   LEU B  44     7106   6662   4895    -40    783    770       N
ATOM   4575  CA  LEU B  44      45.351  27.594   3.777  1.00 52.82           C
ANISOU 4575  CA  LEU B  44     7614   7204   5252    -49    759    840       C
ATOM   4576  C   LEU B  44      43.908  27.333   4.228  1.00 57.12           C
ANISOU 4576  C   LEU B  44     8206   7704   5794    -57    659    796       C
ATOM   4577  O   LEU B  44      42.971  27.779   3.547  1.00 58.09           O
ANISOU 4577  O   LEU B  44     8349   7875   5849    -65    621    862       O
ATOM   4578  CB  LEU B  44      45.654  26.835   2.483  1.00 51.54           C
ANISOU 4578  CB  LEU B  44     7486   7178   4917    -23    814    810       C
ATOM   4579  CG  LEU B  44      47.076  27.060   1.961  1.00 51.83           C
ANISOU 4579  CG  LEU B  44     7470   7279   4946    -14    924    853       C
ATOM   4580  CD1 LEU B  44      47.380  26.239   0.709  1.00 54.49           C
ANISOU 4580  CD1 LEU B  44     7841   7760   5102     19    984    804       C
ATOM   4581  CD2 LEU B  44      47.308  28.537   1.686  1.00 56.48           C
ANISOU 4581  CD2 LEU B  44     8005   7865   5591    -51    956   1023       C
ATOM   4582  N   GLY B  45      43.708  26.620   5.347  1.00 57.86           N
ANISOU 4582  N   GLY B  45     8312   7714   5957    -54    616    692       N
ATOM   4583  CA  GLY B  45      42.414  26.520   6.013  1.00 58.17           C
ANISOU 4583  CA  GLY B  45     8377   7698   6026    -70    529    659       C
ATOM   4584  C   GLY B  45      41.425  25.529   5.424  1.00 58.41           C
ANISOU 4584  C   GLY B  45     8471   7787   5935    -68    484    587       C
ATOM   4585  O   GLY B  45      40.775  24.778   6.171  1.00 55.48           O
ANISOU 4585  O   GLY B  45     8128   7363   5590    -77    433    501       O
ATOM   4586  N   LYS B  46      41.294  25.540   4.086  1.00 54.66           N
ANISOU 4586  N   LYS B  46     8018   7425   5325    -61    501    623       N
ATOM   4587  CA  LYS B  46      40.370  24.686   3.346  1.00 57.66           C
ANISOU 4587  CA  LYS B  46     8454   7880   5575    -63    455    554       C
ATOM   4588  C   LYS B  46      41.040  24.183   2.075  1.00 55.07           C
ANISOU 4588  C   LYS B  46     8153   7672   5100    -39    516    531       C
ATOM   4589  O   LYS B  46      41.857  24.883   1.473  1.00 56.59           O
ANISOU 4589  O   LYS B  46     8314   7921   5265    -28    584    622       O
ATOM   4590  CB  LYS B  46      39.093  25.431   2.942  1.00 56.01           C
ANISOU 4590  CB  LYS B  46     8240   7710   5333    -81    385    633       C
ATOM   4591  CG  LYS B  46      38.363  26.175   4.039  1.00 60.31           C
ANISOU 4591  CG  LYS B  46     8747   8153   6016    -98    331    672       C
ATOM   4592  CD  LYS B  46      37.453  27.282   3.459  1.00 60.91           C
ANISOU 4592  CD  LYS B  46     8799   8273   6073    -99    284    793       C
ATOM   4593  CE  LYS B  46      36.322  26.736   2.576  1.00 59.16           C
ANISOU 4593  CE  LYS B  46     8609   8156   5714   -104    218    761       C
ATOM   4594  NZ  LYS B  46      36.675  26.560   1.125  1.00 64.21           N
ANISOU 4594  NZ  LYS B  46     9279   8936   6183    -89    247    790       N
ATOM   4595  N   ASN B  47      40.649  22.984   1.642  1.00 49.71           N
ANISOU 4595  N   ASN B  47     7530   7035   4323    -35    493    409       N
ATOM   4596  CA  ASN B  47      41.207  22.366   0.427  1.00 52.07           C
ANISOU 4596  CA  ASN B  47     7861   7455   4469     -8    549    357       C
ATOM   4597  C   ASN B  47      42.721  22.267   0.500  1.00 48.41           C
ANISOU 4597  C   ASN B  47     7369   6984   4041     27    650    349       C
ATOM   4598  O   ASN B  47      43.382  22.324  -0.524  1.00 48.65           O
ANISOU 4598  O   ASN B  47     7397   7129   3960     49    720    368       O
ATOM   4599  CB  ASN B  47      40.832  23.128  -0.859  1.00 54.77           C
ANISOU 4599  CB  ASN B  47     8202   7943   4667    -11    548    460       C
ATOM   4600  CG  ASN B  47      39.375  23.542  -0.910  1.00 64.19           C
ANISOU 4600  CG  ASN B  47     9399   9147   5842    -40    445    505       C
ATOM   4601  OD1 ASN B  47      39.008  24.646  -0.503  1.00 66.56           O
ANISOU 4601  OD1 ASN B  47     9659   9403   6229    -52    418    627       O
ATOM   4602  ND2 ASN B  47      38.539  22.670  -1.465  1.00 68.66           N
ANISOU 4602  ND2 ASN B  47    10012   9778   6296    -51    386    401       N
ATOM   4603  N   GLN B  48      43.283  22.155   1.705  1.00 46.56           N
ANISOU 4603  N   GLN B  48     7108   6626   3958     32    659    327       N
ATOM   4604  CA  GLN B  48      44.732  22.210   1.860  1.00 46.48           C
ANISOU 4604  CA  GLN B  48     7052   6609   4000     64    749    334       C
ATOM   4605  C   GLN B  48      45.395  21.059   1.107  1.00 45.88           C
ANISOU 4605  C   GLN B  48     7008   6601   3822    110    808    214       C
ATOM   4606  O   GLN B  48      45.078  19.892   1.372  1.00 46.07           O
ANISOU 4606  O   GLN B  48     7085   6573   3845    123    772     85       O
ATOM   4607  CB  GLN B  48      45.126  22.157   3.331  1.00 43.18           C
ANISOU 4607  CB  GLN B  48     6603   6052   3753     64    732    315       C
ATOM   4608  CG  GLN B  48      44.476  23.221   4.183  1.00 49.13           C
ANISOU 4608  CG  GLN B  48     7324   6730   4612     24    675    407       C
ATOM   4609  CD  GLN B  48      43.362  22.671   5.029  1.00 46.25           C
ANISOU 4609  CD  GLN B  48     7000   6285   4289      3    588    343       C
ATOM   4610  OE1 GLN B  48      42.375  22.155   4.507  1.00 45.71           O
ANISOU 4610  OE1 GLN B  48     6982   6253   4133    -10    542    299       O
ATOM   4611  NE2 GLN B  48      43.512  22.766   6.342  1.00 42.83           N
ANISOU 4611  NE2 GLN B  48     6542   5747   3986     -3    565    335       N
ATOM   4612  N   PRO B  49      46.338  21.336   0.208  1.00 42.63           N
ANISOU 4612  N   PRO B  49     6565   6299   3333    134    901    251       N
ATOM   4613  CA  PRO B  49      46.930  20.283  -0.617  1.00 43.64           C
ANISOU 4613  CA  PRO B  49     6723   6509   3351    184    962    130       C
ATOM   4614  C   PRO B  49      48.134  19.612   0.039  1.00 45.53           C
ANISOU 4614  C   PRO B  49     6927   6679   3693    235   1019     51       C
ATOM   4615  O   PRO B  49      48.702  20.091   1.027  1.00 45.01           O
ANISOU 4615  O   PRO B  49     6803   6527   3773    231   1023    108       O
ATOM   4616  CB  PRO B  49      47.367  21.054  -1.875  1.00 47.24           C
ANISOU 4616  CB  PRO B  49     7149   7129   3670    184   1042    228       C
ATOM   4617  CG  PRO B  49      47.821  22.381  -1.320  1.00 47.81           C
ANISOU 4617  CG  PRO B  49     7144   7158   3864    152   1065    390       C
ATOM   4618  CD  PRO B  49      46.836  22.672  -0.166  1.00 42.09           C
ANISOU 4618  CD  PRO B  49     6433   6291   3268    114    956    411       C
ATOM   4619  N   ALA B  50      48.508  18.468  -0.532  1.00 46.55           N
ANISOU 4619  N   ALA B  50     7094   6849   3746    287   1058    -88       N
ATOM   4620  CA  ALA B  50      49.828  17.908  -0.289  1.00 47.68           C
ANISOU 4620  CA  ALA B  50     7191   6972   3953    352   1136   -153       C
ATOM   4621  C   ALA B  50      50.876  18.764  -1.002  1.00 51.10           C
ANISOU 4621  C   ALA B  50     7542   7535   4339    361   1247    -58       C
ATOM   4622  O   ALA B  50      50.593  19.407  -2.019  1.00 48.10           O
ANISOU 4622  O   ALA B  50     7167   7285   3825    333   1277     17       O
ATOM   4623  CB  ALA B  50      49.892  16.460  -0.782  1.00 42.39           C
ANISOU 4623  CB  ALA B  50     6584   6306   3214    410   1149   -334       C
ATOM   4624  N   VAL B  51      52.089  18.794  -0.452  1.00 48.33           N
ANISOU 4624  N   VAL B  51     7111   7151   4099    397   1308    -53       N
ATOM   4625  CA  VAL B  51      53.191  19.537  -1.060  1.00 50.70           C
ANISOU 4625  CA  VAL B  51     7321   7571   4373    403   1423     32       C
ATOM   4626  C   VAL B  51      54.323  18.556  -1.323  1.00 50.02           C
ANISOU 4626  C   VAL B  51     7200   7524   4280    490   1510    -95       C
ATOM   4627  O   VAL B  51      54.817  17.906  -0.394  1.00 49.78           O
ANISOU 4627  O   VAL B  51     7149   7383   4381    536   1488   -167       O
ATOM   4628  CB  VAL B  51      53.661  20.724  -0.198  1.00 51.44           C
ANISOU 4628  CB  VAL B  51     7324   7603   4619    355   1421    173       C
ATOM   4629  CG1 VAL B  51      54.857  21.387  -0.851  1.00 50.82           C
ANISOU 4629  CG1 VAL B  51     7144   7645   4519    357   1547    252       C
ATOM   4630  CG2 VAL B  51      52.534  21.764  -0.043  1.00 44.79           C
ANISOU 4630  CG2 VAL B  51     6513   6726   3780    276   1343    298       C
ATOM   4631  N   PHE B  52      54.719  18.447  -2.593  1.00 52.31           N
ANISOU 4631  N   PHE B  52     7484   7977   4414    516   1608   -120       N
ATOM   4632  CA  PHE B  52      55.752  17.525  -3.061  1.00 54.36           C
ANISOU 4632  CA  PHE B  52     7712   8302   4640    606   1704   -251       C
ATOM   4633  C   PHE B  52      56.978  18.334  -3.454  1.00 56.35           C
ANISOU 4633  C   PHE B  52     7839   8675   4895    606   1831   -151       C
ATOM   4634  O   PHE B  52      56.900  19.185  -4.348  1.00 59.85           O
ANISOU 4634  O   PHE B  52     8268   9254   5217    557   1889    -39       O
ATOM   4635  CB  PHE B  52      55.237  16.712  -4.251  1.00 52.45           C
ANISOU 4635  CB  PHE B  52     7558   8167   4202    638   1724   -377       C
ATOM   4636  CG  PHE B  52      56.152  15.595  -4.693  1.00 58.61           C
ANISOU 4636  CG  PHE B  52     8322   8994   4952    741   1812   -547       C
ATOM   4637  CD1 PHE B  52      57.155  15.824  -5.627  1.00 57.11           C
ANISOU 4637  CD1 PHE B  52     8056   8981   4663    776   1954   -539       C
ATOM   4638  CD2 PHE B  52      55.970  14.309  -4.218  1.00 56.17           C
ANISOU 4638  CD2 PHE B  52     8076   8553   4711    803   1756   -715       C
ATOM   4639  CE1 PHE B  52      57.982  14.795  -6.054  1.00 61.81           C
ANISOU 4639  CE1 PHE B  52     8632   9623   5231    879   2040   -705       C
ATOM   4640  CE2 PHE B  52      56.790  13.277  -4.640  1.00 58.66           C
ANISOU 4640  CE2 PHE B  52     8379   8901   5009    906   1836   -877       C
ATOM   4641  CZ  PHE B  52      57.798  13.522  -5.562  1.00 61.97           C
ANISOU 4641  CZ  PHE B  52     8717   9501   5329    947   1978   -878       C
ATOM   4642  N   PHE B  53      58.103  18.072  -2.791  1.00 52.98           N
ANISOU 4642  N   PHE B  53     7321   8201   4608    658   1874   -186       N
ATOM   4643  CA  PHE B  53      59.351  18.761  -3.077  1.00 56.28           C
ANISOU 4643  CA  PHE B  53     7605   8728   5051    657   1996   -103       C
ATOM   4644  C   PHE B  53      60.164  17.864  -3.983  1.00 62.58           C
ANISOU 4644  C   PHE B  53     8377   9655   5747    751   2114   -238       C
ATOM   4645  O   PHE B  53      60.519  16.758  -3.579  1.00 61.17           O
ANISOU 4645  O   PHE B  53     8205   9401   5635    841   2101   -387       O
ATOM   4646  CB  PHE B  53      60.139  19.053  -1.810  1.00 54.03           C
ANISOU 4646  CB  PHE B  53     7218   8329   4982    657   1970    -63       C
ATOM   4647  CG  PHE B  53      59.418  19.935  -0.864  1.00 55.14           C
ANISOU 4647  CG  PHE B  53     7376   8345   5229    570   1861     53       C
ATOM   4648  CD1 PHE B  53      58.561  19.398   0.066  1.00 51.36           C
ANISOU 4648  CD1 PHE B  53     6983   7713   4818    575   1733     -5       C
ATOM   4649  CD2 PHE B  53      59.575  21.318  -0.927  1.00 62.69           C
ANISOU 4649  CD2 PHE B  53     8265   9338   6217    481   1890    222       C
ATOM   4650  CE1 PHE B  53      57.886  20.214   0.929  1.00 54.49           C
ANISOU 4650  CE1 PHE B  53     7393   8005   5306    499   1638     94       C
ATOM   4651  CE2 PHE B  53      58.885  22.144  -0.049  1.00 56.87           C
ANISOU 4651  CE2 PHE B  53     7546   8480   5583    406   1789    318       C
ATOM   4652  CZ  PHE B  53      58.047  21.584   0.868  1.00 51.28           C
ANISOU 4652  CZ  PHE B  53     6919   7632   4932    418   1666    248       C
ATOM   4653  N   GLU B  54      60.454  18.341  -5.198  1.00 63.11           N
ANISOU 4653  N   GLU B  54     8414   9912   5652    734   2229   -183       N
ATOM   4654  CA  GLU B  54      61.211  17.530  -6.144  1.00 68.42           C
ANISOU 4654  CA  GLU B  54     9060  10729   6207    824   2353   -317       C
ATOM   4655  C   GLU B  54      62.691  17.490  -5.799  1.00 69.05           C
ANISOU 4655  C   GLU B  54     8987  10834   6415    880   2452   -329       C
ATOM   4656  O   GLU B  54      63.362  16.497  -6.092  1.00 68.86           O
ANISOU 4656  O   GLU B  54     8937  10853   6374    986   2520   -486       O
ATOM   4657  CB  GLU B  54      61.003  18.037  -7.578  1.00 65.52           C
ANISOU 4657  CB  GLU B  54     8714  10577   5603    787   2446   -254       C
ATOM   4658  CG  GLU B  54      59.550  17.941  -8.055  1.00 68.17           C
ANISOU 4658  CG  GLU B  54     9199  10913   5790    746   2347   -265       C
ATOM   4659  CD  GLU B  54      59.403  18.076  -9.561  1.00 72.96           C
ANISOU 4659  CD  GLU B  54     9838  11751   6133    741   2438   -257       C
ATOM   4660  OE1 GLU B  54      60.437  18.214 -10.244  1.00 77.77           O
ANISOU 4660  OE1 GLU B  54    10357  12505   6688    762   2577   -247       O
ATOM   4661  OE2 GLU B  54      58.253  18.061 -10.062  1.00 75.65           O
ANISOU 4661  OE2 GLU B  54    10289  12121   6334    707   2361   -259       O
ATOM   4662  N   LYS B  55      63.224  18.547  -5.188  1.00 69.46           N
ANISOU 4662  N   LYS B  55     8931  10861   6600    812   2462   -172       N
ATOM   4663  CA  LYS B  55      64.649  18.569  -4.873  1.00 66.57           C
ANISOU 4663  CA  LYS B  55     8404  10532   6359    856   2554   -179       C
ATOM   4664  C   LYS B  55      64.934  19.363  -3.612  1.00 67.10           C
ANISOU 4664  C   LYS B  55     8388  10467   6640    793   2481    -64       C
ATOM   4665  O   LYS B  55      64.500  20.509  -3.464  1.00 72.00           O
ANISOU 4665  O   LYS B  55     9010  11065   7281    683   2448     96       O
ATOM   4666  CB  LYS B  55      65.468  19.111  -6.046  1.00 73.59           C
ANISOU 4666  CB  LYS B  55     9195  11646   7121    840   2729   -112       C
ATOM   4667  CG  LYS B  55      65.736  18.038  -7.101  1.00 73.97           C
ANISOU 4667  CG  LYS B  55     9270  11834   7000    948   2830   -284       C
ATOM   4668  CD  LYS B  55      66.544  18.556  -8.253  1.00 81.38           C
ANISOU 4668  CD  LYS B  55    10110  13011   7801    933   3011   -218       C
ATOM   4669  CE  LYS B  55      65.758  19.647  -8.968  1.00 81.71           C
ANISOU 4669  CE  LYS B  55    10214  13140   7693    814   3015    -36       C
ATOM   4670  NZ  LYS B  55      65.239  19.134 -10.275  1.00 86.00           N
ANISOU 4670  NZ  LYS B  55    10868  13791   8018    821   3033   -128       N
ATOM   4671  N   ILE B  56      65.680  18.725  -2.721  1.00 65.26           N
ANISOU 4671  N   ILE B  56     8083  10148   6564    870   2455   -154       N
ATOM   4672  CA  ILE B  56      66.130  19.299  -1.464  1.00 67.38           C
ANISOU 4672  CA  ILE B  56     8259  10304   7039    830   2386    -79       C
ATOM   4673  C   ILE B  56      67.645  19.352  -1.528  1.00 60.82           C
ANISOU 4673  C   ILE B  56     7242   9576   6289    874   2503    -87       C
ATOM   4674  O   ILE B  56      68.278  18.356  -1.894  1.00 61.43           O
ANISOU 4674  O   ILE B  56     7287   9714   6340    991   2571   -222       O
ATOM   4675  CB  ILE B  56      65.650  18.468  -0.254  1.00 60.00           C
ANISOU 4675  CB  ILE B  56     7400   9179   6221    885   2236   -171       C
ATOM   4676  CG1 ILE B  56      64.133  18.255  -0.324  1.00 57.19           C
ANISOU 4676  CG1 ILE B  56     7225   8737   5769    850   2134   -183       C
ATOM   4677  CG2 ILE B  56      66.045  19.139   1.049  1.00 57.28           C
ANISOU 4677  CG2 ILE B  56     6964   8731   6070    836   2158    -90       C
ATOM   4678  CD1 ILE B  56      63.729  16.921  -0.885  1.00 58.60           C
ANISOU 4678  CD1 ILE B  56     7511   8914   5840    946   2136   -348       C
ATOM   4679  N   LYS B  57      68.220  20.512  -1.204  1.00 61.56           N
ANISOU 4679  N   LYS B  57     7213   9691   6486    780   2529     52       N
ATOM   4680  CA  LYS B  57      69.662  20.699  -1.330  1.00 67.90           C
ANISOU 4680  CA  LYS B  57     7823  10609   7367    802   2649     61       C
ATOM   4681  C   LYS B  57      70.424  19.664  -0.517  1.00 64.70           C
ANISOU 4681  C   LYS B  57     7347  10143   7092    929   2610    -78       C
ATOM   4682  O   LYS B  57      70.225  19.549   0.688  1.00 60.25           O
ANISOU 4682  O   LYS B  57     6800   9428   6665    933   2474    -89       O
ATOM   4683  CB  LYS B  57      70.065  22.095  -0.861  1.00 66.54           C
ANISOU 4683  CB  LYS B  57     7535  10424   7322    670   2649    226       C
ATOM   4684  CG  LYS B  57      71.533  22.426  -1.136  1.00 69.54           C
ANISOU 4684  CG  LYS B  57     7705  10944   7774    669   2788    253       C
ATOM   4685  CD  LYS B  57      71.905  23.809  -0.614  1.00 73.06           C
ANISOU 4685  CD  LYS B  57     8038  11358   8364    527   2778    411       C
ATOM   4686  CE  LYS B  57      71.237  24.091   0.740  1.00 73.22           C
ANISOU 4686  CE  LYS B  57     8122  11177   8521    485   2594    422       C
ATOM   4687  NZ  LYS B  57      71.632  25.430   1.301  1.00 75.00           N
ANISOU 4687  NZ  LYS B  57     8234  11361   8902    349   2578    555       N
ATOM   4688  N   GLY B  58      71.334  18.945  -1.178  1.00 66.08           N
ANISOU 4688  N   GLY B  58     7436  10445   7228   1034   2732   -179       N
ATOM   4689  CA  GLY B  58      72.166  17.944  -0.541  1.00 67.44           C
ANISOU 4689  CA  GLY B  58     7525  10577   7522   1170   2711   -310       C
ATOM   4690  C   GLY B  58      71.652  16.518  -0.653  1.00 65.46           C
ANISOU 4690  C   GLY B  58     7410  10251   7209   1304   2668   -479       C
ATOM   4691  O   GLY B  58      72.349  15.593  -0.228  1.00 66.35           O
ANISOU 4691  O   GLY B  58     7462  10330   7419   1434   2659   -592       O
ATOM   4692  N   TYR B  59      70.471  16.317  -1.224  1.00 66.48           N
ANISOU 4692  N   TYR B  59     7718  10354   7186   1277   2639   -498       N
ATOM   4693  CA  TYR B  59      69.793  15.032  -1.237  1.00 65.51           C
ANISOU 4693  CA  TYR B  59     7744  10130   7016   1379   2574   -651       C
ATOM   4694  C   TYR B  59      69.379  14.677  -2.655  1.00 66.08           C
ANISOU 4694  C   TYR B  59     7903  10331   6872   1399   2677   -727       C
ATOM   4695  O   TYR B  59      69.115  15.572  -3.459  1.00 69.40           O
ANISOU 4695  O   TYR B  59     8328  10878   7162   1299   2746   -623       O
ATOM   4696  CB  TYR B  59      68.548  15.053  -0.359  1.00 60.95           C
ANISOU 4696  CB  TYR B  59     7317   9365   6474   1318   2403   -614       C
ATOM   4697  CG  TYR B  59      68.756  15.154   1.126  1.00 59.69           C
ANISOU 4697  CG  TYR B  59     7110   9059   6509   1315   2278   -569       C
ATOM   4698  CD1 TYR B  59      69.352  14.116   1.849  1.00 59.99           C
ANISOU 4698  CD1 TYR B  59     7112   9010   6671   1445   2233   -673       C
ATOM   4699  CD2 TYR B  59      68.315  16.266   1.820  1.00 58.94           C
ANISOU 4699  CD2 TYR B  59     7013   8910   6471   1187   2199   -426       C
ATOM   4700  CE1 TYR B  59      69.505  14.199   3.231  1.00 58.07           C
ANISOU 4700  CE1 TYR B  59     6832   8642   6591   1443   2110   -627       C
ATOM   4701  CE2 TYR B  59      68.461  16.359   3.192  1.00 58.01           C
ANISOU 4701  CE2 TYR B  59     6858   8667   6515   1183   2080   -394       C
ATOM   4702  CZ  TYR B  59      69.055  15.330   3.895  1.00 57.48           C
ANISOU 4702  CZ  TYR B  59     6755   8528   6556   1309   2035   -491       C
ATOM   4703  OH  TYR B  59      69.198  15.454   5.262  1.00 59.29           O
ANISOU 4703  OH  TYR B  59     6948   8649   6932   1303   1913   -451       O
ATOM   4704  N   LYS B  60      69.340  13.383  -2.973  1.00 68.57           N
ANISOU 4704  N   LYS B  60     8287  10618   7149   1527   2686   -909       N
ATOM   4705  CA  LYS B  60      68.846  12.995  -4.289  1.00 63.92           C
ANISOU 4705  CA  LYS B  60     7795  10147   6345   1544   2768  -1000       C
ATOM   4706  C   LYS B  60      67.328  12.890  -4.339  1.00 70.54           C
ANISOU 4706  C   LYS B  60     8830  10885   7087   1475   2651  -1001       C
ATOM   4707  O   LYS B  60      66.722  13.329  -5.323  1.00 67.67           O
ANISOU 4707  O   LYS B  60     8532  10643   6537   1407   2696   -965       O
ATOM   4708  CB  LYS B  60      69.502  11.687  -4.771  1.00 68.54           C
ANISOU 4708  CB  LYS B  60     8362  10763   6918   1711   2848  -1212       C
ATOM   4709  CG  LYS B  60      70.990  11.822  -5.061  1.00 81.67           C
ANISOU 4709  CG  LYS B  60     9822  12582   8629   1780   2999  -1222       C
ATOM   4710  CD  LYS B  60      71.463  11.010  -6.254  1.00 82.08           C
ANISOU 4710  CD  LYS B  60     9860  12785   8542   1897   3146  -1399       C
ATOM   4711  CE  LYS B  60      71.416   9.517  -5.838  1.00 84.17           C
ANISOU 4711  CE  LYS B  60    10199  12878   8904   2052   3077  -1602       C
ATOM   4712  NZ  LYS B  60      71.538   8.807  -7.129  1.00 94.38           N
ANISOU 4712  NZ  LYS B  60    11532  14276  10051   2106   3183  -1767       N
ATOM   4713  N   TYR B  61      66.704  12.302  -3.328  1.00 66.34           N
ANISOU 4713  N   TYR B  61     8389  10144   6673   1493   2504  -1039       N
ATOM   4714  CA  TYR B  61      65.310  11.961  -3.540  1.00 63.04           C
ANISOU 4714  CA  TYR B  61     8153   9647   6152   1448   2410  -1080       C
ATOM   4715  C   TYR B  61      64.456  13.046  -2.911  1.00 63.20           C
ANISOU 4715  C   TYR B  61     8212   9603   6200   1307   2307   -902       C
ATOM   4716  O   TYR B  61      64.965  14.069  -2.439  1.00 65.43           O
ANISOU 4716  O   TYR B  61     8385   9911   6565   1244   2319   -756       O
ATOM   4717  CB  TYR B  61      65.026  10.560  -3.012  1.00 62.90           C
ANISOU 4717  CB  TYR B  61     8229   9450   6222   1550   2326  -1243       C
ATOM   4718  CG  TYR B  61      66.008   9.545  -3.572  1.00 61.92           C
ANISOU 4718  CG  TYR B  61     8046   9381   6098   1702   2434  -1418       C
ATOM   4719  CD1 TYR B  61      66.114   9.320  -4.939  1.00 66.43           C
ANISOU 4719  CD1 TYR B  61     8631  10127   6482   1734   2557  -1524       C
ATOM   4720  CD2 TYR B  61      66.802   8.795  -2.730  1.00 64.83           C
ANISOU 4720  CD2 TYR B  61     8350   9631   6651   1818   2409  -1482       C
ATOM   4721  CE1 TYR B  61      67.012   8.380  -5.450  1.00 67.93           C
ANISOU 4721  CE1 TYR B  61     8766  10369   6675   1880   2661  -1698       C
ATOM   4722  CE2 TYR B  61      67.701   7.876  -3.222  1.00 66.73           C
ANISOU 4722  CE2 TYR B  61     8532   9916   6906   1965   2507  -1644       C
ATOM   4723  CZ  TYR B  61      67.799   7.662  -4.580  1.00 66.94           C
ANISOU 4723  CZ  TYR B  61     8571  10113   6750   1997   2635  -1758       C
ATOM   4724  OH  TYR B  61      68.696   6.730  -5.035  1.00 74.76           O
ANISOU 4724  OH  TYR B  61     9500  11142   7762   2152   2734  -1931       O
ATOM   4725  N   SER B  62      63.153  12.831  -2.922  1.00 61.71           N
ANISOU 4725  N   SER B  62     8174   9330   5943   1256   2207   -919       N
ATOM   4726  CA  SER B  62      62.211  13.899  -2.672  1.00 67.12           C
ANISOU 4726  CA  SER B  62     8905   9994   6604   1124   2130   -762       C
ATOM   4727  C   SER B  62      61.388  13.628  -1.408  1.00 59.95           C
ANISOU 4727  C   SER B  62     8077   8875   5828   1098   1972   -751       C
ATOM   4728  O   SER B  62      61.536  12.601  -0.731  1.00 55.16           O
ANISOU 4728  O   SER B  62     7495   8135   5327   1179   1920   -855       O
ATOM   4729  CB  SER B  62      61.365  14.122  -3.942  1.00 70.09           C
ANISOU 4729  CB  SER B  62     9371  10502   6756   1072   2163   -763       C
ATOM   4730  OG  SER B  62      60.817  12.930  -4.473  1.00 70.19           O
ANISOU 4730  OG  SER B  62     9498  10494   6677   1134   2143   -943       O
ATOM   4731  N   VAL B  63      60.582  14.623  -1.053  1.00 60.34           N
ANISOU 4731  N   VAL B  63     8155   8894   5877    985   1900   -610       N
ATOM   4732  CA  VAL B  63      59.802  14.630   0.175  1.00 53.31           C
ANISOU 4732  CA  VAL B  63     7323   7828   5105    942   1760   -571       C
ATOM   4733  C   VAL B  63      58.375  15.018  -0.196  1.00 52.00           C
ANISOU 4733  C   VAL B  63     7271   7660   4826    851   1693   -526       C
ATOM   4734  O   VAL B  63      58.162  15.863  -1.072  1.00 52.16           O
ANISOU 4734  O   VAL B  63     7283   7811   4725    792   1744   -442       O
ATOM   4735  CB  VAL B  63      60.393  15.619   1.209  1.00 54.51           C
ANISOU 4735  CB  VAL B  63     7364   7941   5407    897   1737   -436       C
ATOM   4736  CG1 VAL B  63      59.485  15.749   2.460  1.00 48.80           C
ANISOU 4736  CG1 VAL B  63     6704   7053   4784    843   1594   -389       C
ATOM   4737  CG2 VAL B  63      61.815  15.231   1.595  1.00 55.80           C
ANISOU 4737  CG2 VAL B  63     7402   8115   5685    988   1795   -481       C
ATOM   4738  N   VAL B  64      57.394  14.381   0.430  1.00 44.56           N
ANISOU 4738  N   VAL B  64     6433   6577   3921    841   1580   -578       N
ATOM   4739  CA  VAL B  64      56.018  14.833   0.294  1.00 45.79           C
ANISOU 4739  CA  VAL B  64     6679   6718   4000    750   1501   -522       C
ATOM   4740  C   VAL B  64      55.429  14.990   1.688  1.00 47.41           C
ANISOU 4740  C   VAL B  64     6906   6761   4347    707   1384   -465       C
ATOM   4741  O   VAL B  64      55.718  14.204   2.601  1.00 48.32           O
ANISOU 4741  O   VAL B  64     7025   6754   4579    759   1342   -524       O
ATOM   4742  CB  VAL B  64      55.167  13.898  -0.590  1.00 43.93           C
ANISOU 4742  CB  VAL B  64     6560   6504   3628    765   1485   -654       C
ATOM   4743  CG1 VAL B  64      54.915  12.581   0.085  1.00 44.35           C
ANISOU 4743  CG1 VAL B  64     6684   6396   3771    818   1417   -786       C
ATOM   4744  CG2 VAL B  64      53.861  14.582  -0.965  1.00 46.51           C
ANISOU 4744  CG2 VAL B  64     6952   6867   3852    668   1421   -577       C
ATOM   4745  N   THR B  65      54.640  16.042   1.865  1.00 45.77           N
ANISOU 4745  N   THR B  65     6706   6557   4127    615   1334   -343       N
ATOM   4746  CA  THR B  65      54.139  16.378   3.182  1.00 45.37           C
ANISOU 4746  CA  THR B  65     6661   6375   4204    570   1235   -280       C
ATOM   4747  C   THR B  65      52.699  16.841   3.055  1.00 44.90           C
ANISOU 4747  C   THR B  65     6677   6303   4079    488   1160   -230       C
ATOM   4748  O   THR B  65      52.232  17.172   1.967  1.00 44.12           O
ANISOU 4748  O   THR B  65     6606   6311   3845    460   1187   -211       O
ATOM   4749  CB  THR B  65      55.013  17.446   3.860  1.00 44.81           C
ANISOU 4749  CB  THR B  65     6473   6308   4244    548   1258   -166       C
ATOM   4750  OG1 THR B  65      54.716  17.475   5.263  1.00 47.15           O
ANISOU 4750  OG1 THR B  65     6773   6471   4668    529   1164   -143       O
ATOM   4751  CG2 THR B  65      54.774  18.842   3.246  1.00 41.39           C
ANISOU 4751  CG2 THR B  65     6004   5968   3753    468   1291    -32       C
ATOM   4752  N   ASN B  66      52.007  16.843   4.197  1.00 43.37           N
ANISOU 4752  N   ASN B  66     6513   5985   3980    453   1065   -208       N
ATOM   4753  CA  ASN B  66      50.595  17.212   4.298  1.00 41.38           C
ANISOU 4753  CA  ASN B  66     6325   5704   3693    380    983   -167       C
ATOM   4754  C   ASN B  66      49.718  16.322   3.438  1.00 43.43           C
ANISOU 4754  C   ASN B  66     6680   5989   3832    381    963   -267       C
ATOM   4755  O   ASN B  66      48.682  16.761   2.934  1.00 40.57           O
ANISOU 4755  O   ASN B  66     6355   5673   3386    326    925   -231       O
ATOM   4756  CB  ASN B  66      50.351  18.682   3.954  1.00 41.73           C
ANISOU 4756  CB  ASN B  66     6324   5823   3710    317    995    -30       C
ATOM   4757  CG  ASN B  66      49.075  19.235   4.626  1.00 44.35           C
ANISOU 4757  CG  ASN B  66     6689   6084   4077    250    899     29       C
ATOM   4758  OD1 ASN B  66      48.897  19.128   5.834  1.00 43.67           O
ANISOU 4758  OD1 ASN B  66     6602   5891   4100    241    841     26       O
ATOM   4759  ND2 ASN B  66      48.171  19.791   3.821  1.00 45.32           N
ANISOU 4759  ND2 ASN B  66     6842   6277   4101    207    882     80       N
ATOM   4760  N   VAL B  67      50.113  15.055   3.314  1.00 43.26           N
ANISOU 4760  N   VAL B  67     6696   5930   3811    446    981   -397       N
ATOM   4761  CA  VAL B  67      49.390  14.123   2.461  1.00 40.20           C
ANISOU 4761  CA  VAL B  67     6397   5562   3314    449    966   -516       C
ATOM   4762  C   VAL B  67      47.961  13.915   2.948  1.00 40.40           C
ANISOU 4762  C   VAL B  67     6494   5504   3354    381    860   -520       C
ATOM   4763  O   VAL B  67      47.033  13.799   2.142  1.00 37.89           O
ANISOU 4763  O   VAL B  67     6228   5244   2924    343    831   -558       O
ATOM   4764  CB  VAL B  67      50.173  12.804   2.368  1.00 40.68           C
ANISOU 4764  CB  VAL B  67     6480   5572   3404    538   1006   -659       C
ATOM   4765  CG1 VAL B  67      49.290  11.682   1.814  1.00 41.12           C
ANISOU 4765  CG1 VAL B  67     6639   5594   3390    532    965   -799       C
ATOM   4766  CG2 VAL B  67      51.388  13.032   1.492  1.00 40.39           C
ANISOU 4766  CG2 VAL B  67     6375   5667   3304    600   1121   -670       C
ATOM   4767  N   HIS B  68      47.751  13.856   4.261  1.00 42.36           N
ANISOU 4767  N   HIS B  68     6739   5622   3732    364    801   -483       N
ATOM   4768  CA  HIS B  68      46.403  13.680   4.798  1.00 44.12           C
ANISOU 4768  CA  HIS B  68     7019   5770   3976    296    709   -480       C
ATOM   4769  C   HIS B  68      45.735  14.985   5.233  1.00 41.67           C
ANISOU 4769  C   HIS B  68     6668   5484   3680    229    669   -348       C
ATOM   4770  O   HIS B  68      44.692  14.930   5.880  1.00 44.75           O
ANISOU 4770  O   HIS B  68     7087   5808   4106    176    596   -335       O
ATOM   4771  CB  HIS B  68      46.427  12.730   5.995  1.00 41.32           C
ANISOU 4771  CB  HIS B  68     6696   5257   3745    313    666   -521       C
ATOM   4772  CG  HIS B  68      46.661  11.299   5.632  1.00 44.50           C
ANISOU 4772  CG  HIS B  68     7163   5598   4147    364    679   -662       C
ATOM   4773  ND1 HIS B  68      47.919  10.793   5.383  1.00 41.75           N
ANISOU 4773  ND1 HIS B  68     6791   5252   3819    456    747   -720       N
ATOM   4774  CD2 HIS B  68      45.800  10.262   5.490  1.00 41.78           C
ANISOU 4774  CD2 HIS B  68     6903   5179   3793    337    632   -759       C
ATOM   4775  CE1 HIS B  68      47.821   9.504   5.110  1.00 44.71           C
ANISOU 4775  CE1 HIS B  68     7237   5550   4201    489    742   -850       C
ATOM   4776  NE2 HIS B  68      46.547   9.157   5.180  1.00 43.42           N
ANISOU 4776  NE2 HIS B  68     7142   5334   4022    414    671   -876       N
ATOM   4777  N   GLY B  69      46.297  16.146   4.901  1.00 40.92           N
ANISOU 4777  N   GLY B  69     6504   5478   3565    229    716   -251       N
ATOM   4778  CA  GLY B  69      45.980  17.377   5.619  1.00 39.62           C
ANISOU 4778  CA  GLY B  69     6289   5299   3467    182    685   -127       C
ATOM   4779  C   GLY B  69      44.790  18.230   5.208  1.00 38.90           C
ANISOU 4779  C   GLY B  69     6205   5260   3315    121    639    -57       C
ATOM   4780  O   GLY B  69      44.885  19.457   5.259  1.00 42.07           O
ANISOU 4780  O   GLY B  69     6552   5693   3740    100    649     54       O
ATOM   4781  N   SER B  70      43.661  17.627   4.837  1.00 38.40           N
ANISOU 4781  N   SER B  70     6205   5201   3185     91    584   -117       N
ATOM   4782  CA  SER B  70      42.450  18.379   4.518  1.00 40.44           C
ANISOU 4782  CA  SER B  70     6465   5507   3394     37    528    -54       C
ATOM   4783  C   SER B  70      41.323  17.375   4.356  1.00 39.52           C
ANISOU 4783  C   SER B  70     6414   5370   3232      5    463   -152       C
ATOM   4784  O   SER B  70      41.564  16.178   4.190  1.00 39.50           O
ANISOU 4784  O   SER B  70     6461   5334   3213     27    473   -268       O
ATOM   4785  CB  SER B  70      42.585  19.214   3.232  1.00 43.31           C
ANISOU 4785  CB  SER B  70     6806   6011   3638     41    567     17       C
ATOM   4786  OG  SER B  70      42.723  18.373   2.088  1.00 37.48           O
ANISOU 4786  OG  SER B  70     6115   5359   2767     65    595    -78       O
ATOM   4787  N   TRP B  71      40.085  17.881   4.354  1.00 37.69           N
ANISOU 4787  N   TRP B  71     6179   5159   2982    -46    396   -108       N
ATOM   4788  CA  TRP B  71      38.953  16.977   4.200  1.00 36.97           C
ANISOU 4788  CA  TRP B  71     6138   5053   2853    -87    330   -200       C
ATOM   4789  C   TRP B  71      38.851  16.493   2.779  1.00 38.91           C
ANISOU 4789  C   TRP B  71     6424   5412   2949    -79    336   -275       C
ATOM   4790  O   TRP B  71      38.365  15.378   2.540  1.00 42.22           O
ANISOU 4790  O   TRP B  71     6897   5807   3337    -99    304   -397       O
ATOM   4791  CB  TRP B  71      37.659  17.645   4.694  1.00 37.33           C
ANISOU 4791  CB  TRP B  71     6157   5092   2936   -142    256   -135       C
ATOM   4792  CG  TRP B  71      37.688  17.754   6.194  1.00 36.26           C
ANISOU 4792  CG  TRP B  71     5998   4836   2942   -153    247   -104       C
ATOM   4793  CD1 TRP B  71      37.739  18.904   6.944  1.00 36.54           C
ANISOU 4793  CD1 TRP B  71     5976   4851   3056   -153    249     -1       C
ATOM   4794  CD2 TRP B  71      37.742  16.666   7.123  1.00 33.73           C
ANISOU 4794  CD2 TRP B  71     5715   4404   2699   -162    239   -177       C
ATOM   4795  NE1 TRP B  71      37.816  18.584   8.281  1.00 35.09           N
ANISOU 4795  NE1 TRP B  71     5791   4562   2980   -162    241    -13       N
ATOM   4796  CE2 TRP B  71      37.816  17.222   8.417  1.00 34.82           C
ANISOU 4796  CE2 TRP B  71     5814   4472   2946   -167    236   -111       C
ATOM   4797  CE3 TRP B  71      37.733  15.278   6.986  1.00 34.51           C
ANISOU 4797  CE3 TRP B  71     5876   4449   2786   -167    234   -291       C
ATOM   4798  CZ2 TRP B  71      37.872  16.433   9.568  1.00 34.60           C
ANISOU 4798  CZ2 TRP B  71     5809   4337   3002   -176    226   -144       C
ATOM   4799  CZ3 TRP B  71      37.802  14.487   8.140  1.00 35.33           C
ANISOU 4799  CZ3 TRP B  71     6005   4428   2991   -176    226   -319       C
ATOM   4800  CH2 TRP B  71      37.866  15.070   9.405  1.00 36.63           C
ANISOU 4800  CH2 TRP B  71     6130   4539   3249   -180    222   -240       C
ATOM   4801  N   GLN B  72      39.373  17.272   1.836  1.00 39.79           N
ANISOU 4801  N   GLN B  72     6510   5644   2966    -51    383   -209       N
ATOM   4802  CA  GLN B  72      39.456  16.807   0.453  1.00 40.29           C
ANISOU 4802  CA  GLN B  72     6611   5832   2867    -34    402   -284       C
ATOM   4803  C   GLN B  72      40.396  15.606   0.344  1.00 43.16           C
ANISOU 4803  C   GLN B  72     7015   6152   3231     12    460   -420       C
ATOM   4804  O   GLN B  72      40.014  14.556  -0.190  1.00 40.12           O
ANISOU 4804  O   GLN B  72     6686   5775   2781      4    436   -558       O
ATOM   4805  CB  GLN B  72      39.908  17.960  -0.450  1.00 41.64           C
ANISOU 4805  CB  GLN B  72     6741   6141   2938    -12    451   -162       C
ATOM   4806  CG  GLN B  72      38.800  18.947  -0.802  1.00 41.63           C
ANISOU 4806  CG  GLN B  72     6716   6215   2886    -50    382    -53       C
ATOM   4807  CD  GLN B  72      38.301  19.760   0.399  1.00 48.28           C
ANISOU 4807  CD  GLN B  72     7513   6949   3883    -77    339     47       C
ATOM   4808  OE1 GLN B  72      39.047  20.044   1.344  1.00 44.86           O
ANISOU 4808  OE1 GLN B  72     7049   6418   3576    -62    380     85       O
ATOM   4809  NE2 GLN B  72      37.017  20.111   0.375  1.00 50.73           N
ANISOU 4809  NE2 GLN B  72     7812   7281   4180   -114    253     80       N
ATOM   4810  N   ASN B  73      41.620  15.728   0.887  1.00 40.84           N
ANISOU 4810  N   ASN B  73     6690   5805   3023     60    533   -389       N
ATOM   4811  CA  ASN B  73      42.560  14.600   0.862  1.00 41.35           C
ANISOU 4811  CA  ASN B  73     6784   5819   3107    116    588   -514       C
ATOM   4812  C   ASN B  73      41.995  13.397   1.612  1.00 44.20           C
ANISOU 4812  C   ASN B  73     7203   6035   3557     96    529   -623       C
ATOM   4813  O   ASN B  73      42.111  12.252   1.158  1.00 45.54           O
ANISOU 4813  O   ASN B  73     7428   6181   3695    118    538   -766       O
ATOM   4814  CB  ASN B  73      43.916  15.004   1.466  1.00 35.89           C
ANISOU 4814  CB  ASN B  73     6034   5092   2511    170    664   -450       C
ATOM   4815  CG  ASN B  73      44.642  16.074   0.627  1.00 43.66           C
ANISOU 4815  CG  ASN B  73     6961   6218   3409    189    740   -350       C
ATOM   4816  OD1 ASN B  73      44.034  16.720  -0.227  1.00 40.46           O
ANISOU 4816  OD1 ASN B  73     6557   5928   2887    159    725   -294       O
ATOM   4817  ND2 ASN B  73      45.945  16.261   0.879  1.00 39.68           N
ANISOU 4817  ND2 ASN B  73     6402   5708   2965    239    820   -323       N
ATOM   4818  N   HIS B  74      41.389  13.639   2.768  1.00 39.92           N
ANISOU 4818  N   HIS B  74     6648   5392   3130     52    473   -558       N
ATOM   4819  CA  HIS B  74      40.771  12.562   3.513  1.00 38.89           C
ANISOU 4819  CA  HIS B  74     6568   5126   3083     21    419   -640       C
ATOM   4820  C   HIS B  74      39.651  11.913   2.708  1.00 41.57           C
ANISOU 4820  C   HIS B  74     6960   5502   3333    -32    361   -742       C
ATOM   4821  O   HIS B  74      39.546  10.682   2.655  1.00 40.91           O
ANISOU 4821  O   HIS B  74     6936   5337   3271    -34    348   -871       O
ATOM   4822  CB  HIS B  74      40.250  13.125   4.835  1.00 36.69           C
ANISOU 4822  CB  HIS B  74     6255   4764   2920    -21    374   -536       C
ATOM   4823  CG  HIS B  74      39.961  12.091   5.862  1.00 38.52           C
ANISOU 4823  CG  HIS B  74     6530   4846   3262    -41    340   -588       C
ATOM   4824  ND1 HIS B  74      38.821  11.313   5.830  1.00 44.41           N
ANISOU 4824  ND1 HIS B  74     7323   5546   4005   -106    278   -660       N
ATOM   4825  CD2 HIS B  74      40.634  11.736   6.984  1.00 40.60           C
ANISOU 4825  CD2 HIS B  74     6792   4995   3641     -9    355   -567       C
ATOM   4826  CE1 HIS B  74      38.814  10.509   6.881  1.00 43.37           C
ANISOU 4826  CE1 HIS B  74     7222   5272   3986   -116    264   -675       C
ATOM   4827  NE2 HIS B  74      39.901  10.748   7.597  1.00 39.29           N
ANISOU 4827  NE2 HIS B  74     6677   4714   3536    -54    308   -618       N
ATOM   4828  N   ALA B  75      38.823  12.722   2.043  1.00 40.29           N
ANISOU 4828  N   ALA B  75     6774   5462   3072    -73    322   -688       N
ATOM   4829  CA  ALA B  75      37.757  12.145   1.239  1.00 41.82           C
ANISOU 4829  CA  ALA B  75     7009   5709   3173   -125    259   -788       C
ATOM   4830  C   ALA B  75      38.326  11.300   0.102  1.00 45.58           C
ANISOU 4830  C   ALA B  75     7535   6244   3539    -83    300   -932       C
ATOM   4831  O   ALA B  75      37.819  10.211  -0.186  1.00 46.68           O
ANISOU 4831  O   ALA B  75     7730   6339   3666   -112    261  -1075       O
ATOM   4832  CB  ALA B  75      36.848  13.242   0.696  1.00 39.83           C
ANISOU 4832  CB  ALA B  75     6713   5590   2828   -163    209   -692       C
ATOM   4833  N   LEU B  76      39.389  11.778  -0.543  1.00 42.89           N
ANISOU 4833  N   LEU B  76     7173   6003   3122    -15    381   -901       N
ATOM   4834  CA  LEU B  76      40.013  10.987  -1.590  1.00 46.63           C
ANISOU 4834  CA  LEU B  76     7689   6540   3488     34    432  -1044       C
ATOM   4835  C   LEU B  76      40.643   9.727  -1.031  1.00 44.72           C
ANISOU 4835  C   LEU B  76     7492   6137   3363     74    460  -1168       C
ATOM   4836  O   LEU B  76      40.671   8.705  -1.713  1.00 44.95           O
ANISOU 4836  O   LEU B  76     7577   6163   3338     89    464  -1333       O
ATOM   4837  CB  LEU B  76      41.048  11.819  -2.337  1.00 42.51           C
ANISOU 4837  CB  LEU B  76     7125   6165   2864     96    523   -970       C
ATOM   4838  CG  LEU B  76      40.395  12.947  -3.115  1.00 45.31           C
ANISOU 4838  CG  LEU B  76     7448   6688   3081     60    493   -857       C
ATOM   4839  CD1 LEU B  76      41.454  13.936  -3.604  1.00 45.42           C
ANISOU 4839  CD1 LEU B  76     7409   6820   3029    111    589   -739       C
ATOM   4840  CD2 LEU B  76      39.570  12.362  -4.275  1.00 45.59           C
ANISOU 4840  CD2 LEU B  76     7534   6838   2950     32    440   -986       C
ATOM   4841  N   MET B  77      41.160   9.781   0.195  1.00 44.86           N
ANISOU 4841  N   MET B  77     7485   6020   3538     94    476  -1093       N
ATOM   4842  CA  MET B  77      41.724   8.582   0.811  1.00 43.80           C
ANISOU 4842  CA  MET B  77     7393   5721   3526    136    494  -1193       C
ATOM   4843  C   MET B  77      40.679   7.469   0.905  1.00 47.07           C
ANISOU 4843  C   MET B  77     7880   6027   3979     72    418  -1314       C
ATOM   4844  O   MET B  77      40.989   6.291   0.689  1.00 48.22           O
ANISOU 4844  O   MET B  77     8082   6083   4155    105    432  -1461       O
ATOM   4845  CB  MET B  77      42.279   8.936   2.190  1.00 45.46           C
ANISOU 4845  CB  MET B  77     7562   5820   3891    157    506  -1071       C
ATOM   4846  CG  MET B  77      42.615   7.739   3.065  1.00 46.20           C
ANISOU 4846  CG  MET B  77     7701   5724   4129    187    500  -1140       C
ATOM   4847  SD  MET B  77      42.988   8.274   4.737  1.00 46.97           S
ANISOU 4847  SD  MET B  77     7748   5717   4381    192    490   -982       S
ATOM   4848  CE  MET B  77      41.330   8.468   5.388  1.00 44.48           C
ANISOU 4848  CE  MET B  77     7450   5359   4092     70    394   -927       C
ATOM   4849  N   LEU B  78      39.426   7.829   1.187  1.00 47.19           N
ANISOU 4849  N   LEU B  78     7888   6048   3995    -21    339  -1259       N
ATOM   4850  CA  LEU B  78      38.319   6.889   1.274  1.00 46.04           C
ANISOU 4850  CA  LEU B  78     7796   5812   3886   -100    263  -1360       C
ATOM   4851  C   LEU B  78      37.700   6.588  -0.075  1.00 53.79           C
ANISOU 4851  C   LEU B  78     8808   6915   4716   -132    230  -1492       C
ATOM   4852  O   LEU B  78      36.687   5.875  -0.126  1.00 52.43           O
ANISOU 4852  O   LEU B  78     8672   6688   4562   -211    159  -1583       O
ATOM   4853  CB  LEU B  78      37.239   7.440   2.203  1.00 46.52           C
ANISOU 4853  CB  LEU B  78     7821   5837   4015   -186    195  -1242       C
ATOM   4854  CG  LEU B  78      37.693   7.711   3.635  1.00 47.55           C
ANISOU 4854  CG  LEU B  78     7925   5851   4291   -167    215  -1118       C
ATOM   4855  CD1 LEU B  78      36.610   8.475   4.354  1.00 44.87           C
ANISOU 4855  CD1 LEU B  78     7539   5525   3984   -245    157  -1003       C
ATOM   4856  CD2 LEU B  78      38.018   6.414   4.361  1.00 53.61           C
ANISOU 4856  CD2 LEU B  78     8753   6428   5191   -154    221  -1191       C
ATOM   4857  N   GLY B  79      38.264   7.137  -1.151  1.00 50.62           N
ANISOU 4857  N   GLY B  79     8388   6684   4161    -78    279  -1499       N
ATOM   4858  CA  GLY B  79      37.741   6.911  -2.484  1.00 52.04           C
ANISOU 4858  CA  GLY B  79     8595   7006   4171   -102    249  -1622       C
ATOM   4859  C   GLY B  79      36.473   7.663  -2.788  1.00 49.90           C
ANISOU 4859  C   GLY B  79     8290   6854   3815   -184    162  -1551       C
ATOM   4860  O   GLY B  79      35.705   7.251  -3.655  1.00 52.16           O
ANISOU 4860  O   GLY B  79     8603   7222   3994   -231    103  -1668       O
ATOM   4861  N   LEU B  80      36.248   8.782  -2.126  1.00 46.79           N
ANISOU 4861  N   LEU B  80     7834   6479   3465   -199    152  -1367       N
ATOM   4862  CA  LEU B  80      35.025   9.540  -2.299  1.00 49.12           C
ANISOU 4862  CA  LEU B  80     8087   6874   3703   -269     67  -1287       C
ATOM   4863  C   LEU B  80      35.317  10.794  -3.111  1.00 51.85           C
ANISOU 4863  C   LEU B  80     8387   7411   3901   -227     95  -1166       C
ATOM   4864  O   LEU B  80      36.473  11.207  -3.266  1.00 51.96           O
ANISOU 4864  O   LEU B  80     8390   7459   3892   -154    185  -1112       O
ATOM   4865  CB  LEU B  80      34.410   9.896  -0.931  1.00 49.60           C
ANISOU 4865  CB  LEU B  80     8109   6810   3927   -319     29  -1171       C
ATOM   4866  CG  LEU B  80      34.146   8.672  -0.037  1.00 49.50           C
ANISOU 4866  CG  LEU B  80     8142   6601   4065   -364      8  -1265       C
ATOM   4867  CD1 LEU B  80      33.765   9.079   1.365  1.00 46.30           C
ANISOU 4867  CD1 LEU B  80     7697   6087   3809   -399     -8  -1138       C
ATOM   4868  CD2 LEU B  80      33.063   7.775  -0.651  1.00 47.69           C
ANISOU 4868  CD2 LEU B  80     7947   6382   3792   -445    -73  -1416       C
ATOM   4869  N   ASP B  81      34.258  11.371  -3.672  1.00 48.15           N
ANISOU 4869  N   ASP B  81     7890   7070   3334   -275     17  -1123       N
ATOM   4870  CA  ASP B  81      34.357  12.721  -4.201  1.00 50.61           C
ANISOU 4870  CA  ASP B  81     8150   7538   3541   -245     30   -962       C
ATOM   4871  C   ASP B  81      35.004  13.639  -3.166  1.00 52.65           C
ANISOU 4871  C   ASP B  81     8361   7709   3935   -212     87   -795       C
ATOM   4872  O   ASP B  81      34.597  13.671  -1.993  1.00 49.00           O
ANISOU 4872  O   ASP B  81     7877   7110   3629   -246     58   -752       O
ATOM   4873  CB  ASP B  81      32.968  13.238  -4.578  1.00 53.66           C
ANISOU 4873  CB  ASP B  81     8501   8030   3859   -304    -80   -915       C
ATOM   4874  CG  ASP B  81      33.016  14.585  -5.277  1.00 57.32           C
ANISOU 4874  CG  ASP B  81     8919   8660   4201   -268    -75   -749       C
ATOM   4875  OD1 ASP B  81      33.187  15.613  -4.587  1.00 60.66           O
ANISOU 4875  OD1 ASP B  81     9293   9038   4719   -251    -52   -583       O
ATOM   4876  OD2 ASP B  81      32.893  14.614  -6.521  1.00 64.88           O
ANISOU 4876  OD2 ASP B  81     9892   9794   4966   -258    -93   -784       O
ATOM   4877  N   LYS B  82      36.013  14.390  -3.613  1.00 45.27           N
ANISOU 4877  N   LYS B  82     7408   6858   2936   -150    169   -703       N
ATOM   4878  CA  LYS B  82      36.837  15.175  -2.698  1.00 48.54           C
ANISOU 4878  CA  LYS B  82     7777   7187   3477   -117    233   -568       C
ATOM   4879  C   LYS B  82      36.010  16.118  -1.832  1.00 48.43           C
ANISOU 4879  C   LYS B  82     7711   7122   3570   -156    173   -431       C
ATOM   4880  O   LYS B  82      36.409  16.427  -0.704  1.00 45.50           O
ANISOU 4880  O   LYS B  82     7312   6629   3347   -149    200   -366       O
ATOM   4881  CB  LYS B  82      37.890  15.946  -3.507  1.00 47.30           C
ANISOU 4881  CB  LYS B  82     7599   7157   3216    -59    323   -481       C
ATOM   4882  CG  LYS B  82      37.293  17.028  -4.388  1.00 46.46           C
ANISOU 4882  CG  LYS B  82     7463   7213   2976    -70    287   -355       C
ATOM   4883  CD  LYS B  82      38.274  17.513  -5.472  1.00 53.12           C
ANISOU 4883  CD  LYS B  82     8301   8211   3670    -20    378   -298       C
ATOM   4884  CE  LYS B  82      39.186  18.632  -4.963  1.00 60.13           C
ANISOU 4884  CE  LYS B  82     9132   9061   4655      5    455   -128       C
ATOM   4885  NZ  LYS B  82      39.401  19.711  -5.989  1.00 70.55           N
ANISOU 4885  NZ  LYS B  82    10426  10547   5835     20    491     23       N
ATOM   4886  N   ASN B  83      34.865  16.582  -2.324  1.00 49.27           N
ANISOU 4886  N   ASN B  83     7797   7322   3600   -193     91   -390       N
ATOM   4887  CA  ASN B  83      34.079  17.551  -1.575  1.00 49.10           C
ANISOU 4887  CA  ASN B  83     7718   7262   3676   -219     39   -260       C
ATOM   4888  C   ASN B  83      33.047  16.894  -0.679  1.00 50.25           C
ANISOU 4888  C   ASN B  83     7862   7300   3930   -280    -33   -332       C
ATOM   4889  O   ASN B  83      32.208  17.599  -0.105  1.00 50.11           O
ANISOU 4889  O   ASN B  83     7793   7263   3983   -305    -85   -246       O
ATOM   4890  CB  ASN B  83      33.407  18.554  -2.518  1.00 51.54           C
ANISOU 4890  CB  ASN B  83     7993   7728   3862   -217    -11   -151       C
ATOM   4891  CG  ASN B  83      34.416  19.446  -3.238  1.00 49.84           C
ANISOU 4891  CG  ASN B  83     7767   7607   3563   -162     67    -33       C
ATOM   4892  OD1 ASN B  83      35.315  20.005  -2.621  1.00 56.81           O
ANISOU 4892  OD1 ASN B  83     8627   8413   4545   -135    139     50       O
ATOM   4893  ND2 ASN B  83      34.279  19.559  -4.533  1.00 51.39           N
ANISOU 4893  ND2 ASN B  83     7979   7974   3574   -150     54    -25       N
ATOM   4894  N   THR B  84      33.105  15.570  -0.532  1.00 47.04           N
ANISOU 4894  N   THR B  84     7509   6819   3544   -303    -33   -485       N
ATOM   4895  CA  THR B  84      32.246  14.886   0.422  1.00 47.21           C
ANISOU 4895  CA  THR B  84     7532   6721   3685   -366    -87   -545       C
ATOM   4896  C   THR B  84      32.370  15.506   1.806  1.00 42.94           C
ANISOU 4896  C   THR B  84     6950   6066   3302   -363    -65   -437       C
ATOM   4897  O   THR B  84      33.472  15.654   2.337  1.00 42.94           O
ANISOU 4897  O   THR B  84     6954   5996   3363   -316      7   -400       O
ATOM   4898  CB  THR B  84      32.586  13.390   0.455  1.00 43.59           C
ANISOU 4898  CB  THR B  84     7144   6170   3248   -380    -70   -711       C
ATOM   4899  OG1 THR B  84      32.325  12.818  -0.838  1.00 43.56           O
ANISOU 4899  OG1 THR B  84     7177   6279   3094   -391   -101   -829       O
ATOM   4900  CG2 THR B  84      31.778  12.652   1.542  1.00 40.67           C
ANISOU 4900  CG2 THR B  84     6778   5659   3016   -451   -115   -756       C
ATOM   4901  N   SER B  85      31.224  15.870   2.381  1.00 41.89           N
ANISOU 4901  N   SER B  85     6769   5920   3229   -412   -130   -393       N
ATOM   4902  CA  SER B  85      31.211  16.525   3.679  1.00 40.91           C
ANISOU 4902  CA  SER B  85     6600   5703   3241   -411   -114   -298       C
ATOM   4903  C   SER B  85      31.779  15.613   4.762  1.00 41.53           C
ANISOU 4903  C   SER B  85     6717   5631   3430   -419    -73   -354       C
ATOM   4904  O   SER B  85      31.836  14.385   4.630  1.00 41.48           O
ANISOU 4904  O   SER B  85     6768   5572   3420   -442    -75   -470       O
ATOM   4905  CB  SER B  85      29.795  16.946   4.063  1.00 48.18           C
ANISOU 4905  CB  SER B  85     7460   6645   4201   -462   -189   -262       C
ATOM   4906  OG  SER B  85      28.996  15.812   4.378  1.00 50.10           O
ANISOU 4906  OG  SER B  85     7722   6834   4478   -535   -231   -368       O
ATOM   4907  N   THR B  86      32.247  16.246   5.835  1.00 34.88           N
ANISOU 4907  N   THR B  86     5845   4719   2690   -394    -36   -269       N
ATOM   4908  CA  THR B  86      32.867  15.501   6.918  1.00 37.84           C
ANISOU 4908  CA  THR B  86     6252   4962   3164   -392      1   -300       C
ATOM   4909  C   THR B  86      31.865  14.529   7.539  1.00 40.31           C
ANISOU 4909  C   THR B  86     6582   5202   3532   -467    -44   -365       C
ATOM   4910  O   THR B  86      32.187  13.365   7.773  1.00 38.05           O
ANISOU 4910  O   THR B  86     6353   4825   3278   -478    -30   -444       O
ATOM   4911  CB  THR B  86      33.432  16.483   7.952  1.00 40.31           C
ANISOU 4911  CB  THR B  86     6519   5234   3564   -358     36   -196       C
ATOM   4912  OG1 THR B  86      34.359  17.371   7.309  1.00 37.58           O
ANISOU 4912  OG1 THR B  86     6153   4951   3172   -298     80   -135       O
ATOM   4913  CG2 THR B  86      34.160  15.748   9.066  1.00 36.50           C
ANISOU 4913  CG2 THR B  86     6068   4630   3172   -347     71   -219       C
ATOM   4914  N   LYS B  87      30.618  14.969   7.737  1.00 40.38           N
ANISOU 4914  N   LYS B  87     6538   5252   3552   -519    -98   -335       N
ATOM   4915  CA  LYS B  87      29.582  14.063   8.228  1.00 41.32           C
ANISOU 4915  CA  LYS B  87     6664   5318   3719   -601   -139   -395       C
ATOM   4916  C   LYS B  87      29.458  12.838   7.329  1.00 42.05           C
ANISOU 4916  C   LYS B  87     6818   5402   3756   -636   -163   -521       C
ATOM   4917  O   LYS B  87      29.345  11.707   7.808  1.00 39.16           O
ANISOU 4917  O   LYS B  87     6497   4929   3451   -682   -162   -588       O
ATOM   4918  CB  LYS B  87      28.241  14.799   8.316  1.00 41.06           C
ANISOU 4918  CB  LYS B  87     6551   5360   3689   -646   -196   -349       C
ATOM   4919  CG  LYS B  87      27.157  14.028   9.067  1.00 45.13           C
ANISOU 4919  CG  LYS B  87     7052   5821   4274   -736   -227   -389       C
ATOM   4920  CD  LYS B  87      25.814  14.728   8.928  1.00 46.61           C
ANISOU 4920  CD  LYS B  87     7150   6106   4453   -775   -286   -358       C
ATOM   4921  CE  LYS B  87      25.404  14.769   7.448  1.00 51.74           C
ANISOU 4921  CE  LYS B  87     7795   6874   4990   -777   -345   -405       C
ATOM   4922  NZ  LYS B  87      23.925  14.726   7.267  1.00 61.26           N
ANISOU 4922  NZ  LYS B  87     8929   8152   6195   -849   -420   -430       N
ATOM   4923  N   ASP B  88      29.481  13.039   6.011  1.00 41.16           N
ANISOU 4923  N   ASP B  88     6710   5401   3526   -615   -183   -557       N
ATOM   4924  CA  ASP B  88      29.320  11.890   5.127  1.00 40.37           C
ANISOU 4924  CA  ASP B  88     6668   5303   3367   -649   -210   -696       C
ATOM   4925  C   ASP B  88      30.560  11.006   5.111  1.00 41.82           C
ANISOU 4925  C   ASP B  88     6931   5391   3569   -601   -148   -765       C
ATOM   4926  O   ASP B  88      30.436   9.788   4.944  1.00 43.25           O
ANISOU 4926  O   ASP B  88     7169   5496   3769   -640   -161   -884       O
ATOM   4927  CB  ASP B  88      28.952  12.349   3.722  1.00 48.21           C
ANISOU 4927  CB  ASP B  88     7643   6460   4214   -640   -254   -718       C
ATOM   4928  CG  ASP B  88      27.487  12.765   3.611  1.00 55.66           C
ANISOU 4928  CG  ASP B  88     8516   7489   5145   -705   -338   -696       C
ATOM   4929  OD1 ASP B  88      26.686  12.395   4.506  1.00 58.61           O
ANISOU 4929  OD1 ASP B  88     8863   7786   5620   -774   -362   -701       O
ATOM   4930  OD2 ASP B  88      27.141  13.484   2.642  1.00 61.56           O
ANISOU 4930  OD2 ASP B  88     9228   8382   5780   -685   -379   -666       O
ATOM   4931  N   GLN B  89      31.757  11.578   5.292  1.00 39.73           N
ANISOU 4931  N   GLN B  89     6667   5122   3307   -517    -81   -697       N
ATOM   4932  CA  GLN B  89      32.949  10.737   5.422  1.00 37.17           C
ANISOU 4932  CA  GLN B  89     6405   4700   3019   -465    -22   -757       C
ATOM   4933  C   GLN B  89      32.889   9.897   6.701  1.00 40.37           C
ANISOU 4933  C   GLN B  89     6838   4939   3561   -497    -19   -761       C
ATOM   4934  O   GLN B  89      33.238   8.704   6.698  1.00 36.19           O
ANISOU 4934  O   GLN B  89     6375   4304   3072   -497     -7   -856       O
ATOM   4935  CB  GLN B  89      34.200  11.608   5.402  1.00 35.49           C
ANISOU 4935  CB  GLN B  89     6169   4527   2787   -374     46   -674       C
ATOM   4936  CG  GLN B  89      34.428  12.370   4.085  1.00 37.19           C
ANISOU 4936  CG  GLN B  89     6365   4904   2861   -337     57   -661       C
ATOM   4937  CD  GLN B  89      35.754  13.100   4.082  1.00 39.15           C
ANISOU 4937  CD  GLN B  89     6592   5179   3106   -256    134   -585       C
ATOM   4938  OE1 GLN B  89      36.796  12.530   4.447  1.00 38.46           O
ANISOU 4938  OE1 GLN B  89     6530   5010   3073   -207    188   -619       O
ATOM   4939  NE2 GLN B  89      35.722  14.379   3.731  1.00 38.51           N
ANISOU 4939  NE2 GLN B  89     6456   5203   2973   -241    138   -475       N
ATOM   4940  N   PHE B  90      32.420  10.511   7.792  1.00 39.10           N
ANISOU 4940  N   PHE B  90     6629   4756   3472   -526    -29   -657       N
ATOM   4941  CA  PHE B  90      32.177   9.807   9.047  1.00 37.67           C
ANISOU 4941  CA  PHE B  90     6467   4440   3407   -568    -30   -642       C
ATOM   4942  C   PHE B  90      31.258   8.603   8.831  1.00 38.51           C
ANISOU 4942  C   PHE B  90     6615   4481   3537   -656    -74   -745       C
ATOM   4943  O   PHE B  90      31.540   7.498   9.305  1.00 38.24           O
ANISOU 4943  O   PHE B  90     6641   4308   3579   -668    -61   -788       O
ATOM   4944  CB  PHE B  90      31.563  10.791  10.061  1.00 36.11           C
ANISOU 4944  CB  PHE B  90     6198   4270   3253   -595    -41   -527       C
ATOM   4945  CG  PHE B  90      30.903  10.126  11.245  1.00 37.64           C
ANISOU 4945  CG  PHE B  90     6399   4361   3540   -665    -52   -510       C
ATOM   4946  CD1 PHE B  90      31.659   9.763  12.346  1.00 36.59           C
ANISOU 4946  CD1 PHE B  90     6295   4123   3483   -634    -15   -465       C
ATOM   4947  CD2 PHE B  90      29.543   9.855  11.249  1.00 35.99           C
ANISOU 4947  CD2 PHE B  90     6164   4169   3341   -761   -100   -534       C
ATOM   4948  CE1 PHE B  90      31.071   9.141  13.455  1.00 35.98           C
ANISOU 4948  CE1 PHE B  90     6229   3959   3484   -699    -21   -435       C
ATOM   4949  CE2 PHE B  90      28.941   9.239  12.350  1.00 36.01           C
ANISOU 4949  CE2 PHE B  90     6171   4083   3430   -832   -102   -510       C
ATOM   4950  CZ  PHE B  90      29.709   8.876  13.449  1.00 37.23           C
ANISOU 4950  CZ  PHE B  90     6362   4132   3651   -801    -60   -456       C
ATOM   4951  N   TYR B  91      30.153   8.799   8.098  1.00 39.87           N
ANISOU 4951  N   TYR B  91     6753   4749   3647   -720   -131   -783       N
ATOM   4952  CA  TYR B  91      29.205   7.707   7.891  1.00 41.07           C
ANISOU 4952  CA  TYR B  91     6934   4845   3827   -817   -179   -884       C
ATOM   4953  C   TYR B  91      29.791   6.600   7.046  1.00 43.51           C
ANISOU 4953  C   TYR B  91     7325   5092   4113   -799   -171  -1024       C
ATOM   4954  O   TYR B  91      29.472   5.430   7.281  1.00 45.19           O
ANISOU 4954  O   TYR B  91     7588   5178   4403   -861   -186  -1101       O
ATOM   4955  CB  TYR B  91      27.925   8.198   7.240  1.00 38.58           C
ANISOU 4955  CB  TYR B  91     6553   4661   3445   -885   -247   -900       C
ATOM   4956  CG  TYR B  91      26.974   8.830   8.232  1.00 42.66           C
ANISOU 4956  CG  TYR B  91     6991   5195   4022   -938   -264   -798       C
ATOM   4957  CD1 TYR B  91      26.761   8.256   9.479  1.00 40.94           C
ANISOU 4957  CD1 TYR B  91     6783   4853   3920   -990   -244   -762       C
ATOM   4958  CD2 TYR B  91      26.303  10.004   7.924  1.00 45.32           C
ANISOU 4958  CD2 TYR B  91     7243   5676   4301   -933   -299   -736       C
ATOM   4959  CE1 TYR B  91      25.881   8.828  10.387  1.00 46.55           C
ANISOU 4959  CE1 TYR B  91     7418   5592   4677  -1038   -252   -676       C
ATOM   4960  CE2 TYR B  91      25.437  10.591   8.825  1.00 45.14           C
ANISOU 4960  CE2 TYR B  91     7143   5672   4338   -974   -310   -653       C
ATOM   4961  CZ  TYR B  91      25.225  10.003  10.046  1.00 51.82           C
ANISOU 4961  CZ  TYR B  91     7996   6403   5288  -1027   -284   -629       C
ATOM   4962  OH  TYR B  91      24.350  10.601  10.933  1.00 59.04           O
ANISOU 4962  OH  TYR B  91     8830   7351   6253  -1065   -289   -553       O
ATOM   4963  N   GLU B  92      30.639   6.952   6.071  1.00 42.70           N
ANISOU 4963  N   GLU B  92     7237   5077   3909   -715   -145  -1059       N
ATOM   4964  CA  GLU B  92      31.293   5.956   5.225  1.00 42.92           C
ANISOU 4964  CA  GLU B  92     7342   5060   3907   -681   -128  -1202       C
ATOM   4965  C   GLU B  92      32.325   5.158   6.008  1.00 44.62           C
ANISOU 4965  C   GLU B  92     7616   5104   4235   -627    -72  -1204       C
ATOM   4966  O   GLU B  92      32.376   3.929   5.893  1.00 44.11           O
ANISOU 4966  O   GLU B  92     7620   4912   4227   -648    -77  -1318       O
ATOM   4967  CB  GLU B  92      31.943   6.641   4.012  1.00 43.46           C
ANISOU 4967  CB  GLU B  92     7399   5287   3826   -603   -105  -1224       C
ATOM   4968  CG  GLU B  92      32.432   5.679   2.939  1.00 51.71           C
ANISOU 4968  CG  GLU B  92     8514   6324   4808   -574    -93  -1395       C
ATOM   4969  CD  GLU B  92      31.333   4.742   2.438  1.00 53.14           C
ANISOU 4969  CD  GLU B  92     8724   6480   4985   -676   -167  -1537       C
ATOM   4970  OE1 GLU B  92      30.159   5.155   2.403  1.00 60.23           O
ANISOU 4970  OE1 GLU B  92     9570   7456   5859   -758   -233  -1506       O
ATOM   4971  OE2 GLU B  92      31.633   3.579   2.103  1.00 56.64           O
ANISOU 4971  OE2 GLU B  92     9240   6821   5460   -674   -159  -1684       O
ATOM   4972  N   LEU B  93      33.146   5.827   6.829  1.00 44.28           N
ANISOU 4972  N   LEU B  93     7547   5049   4230   -558    -23  -1080       N
ATOM   4973  CA  LEU B  93      34.066   5.085   7.691  1.00 43.80           C
ANISOU 4973  CA  LEU B  93     7534   4829   4281   -506     20  -1067       C
ATOM   4974  C   LEU B  93      33.313   4.148   8.619  1.00 44.64           C
ANISOU 4974  C   LEU B  93     7673   4780   4506   -593    -11  -1064       C
ATOM   4975  O   LEU B  93      33.716   2.992   8.801  1.00 47.45           O
ANISOU 4975  O   LEU B  93     8100   4983   4946   -580      1  -1128       O
ATOM   4976  CB  LEU B  93      34.923   6.015   8.537  1.00 40.99           C
ANISOU 4976  CB  LEU B  93     7132   4495   3948   -433     63   -929       C
ATOM   4977  CG  LEU B  93      36.322   6.325   8.035  1.00 48.25           C
ANISOU 4977  CG  LEU B  93     8048   5461   4824   -317    123   -938       C
ATOM   4978  CD1 LEU B  93      36.989   7.277   9.004  1.00 44.78           C
ANISOU 4978  CD1 LEU B  93     7554   5040   4422   -268    153   -798       C
ATOM   4979  CD2 LEU B  93      37.117   5.049   7.897  1.00 43.42           C
ANISOU 4979  CD2 LEU B  93     7509   4719   4270   -262    151  -1041       C
ATOM   4980  N   ASN B  94      32.227   4.631   9.228  1.00 44.23           N
ANISOU 4980  N   ASN B  94     7570   4764   4470   -679    -47   -985       N
ATOM   4981  CA  ASN B  94      31.474   3.789  10.148  1.00 40.85           C
ANISOU 4981  CA  ASN B  94     7166   4202   4153   -771    -68   -967       C
ATOM   4982  C   ASN B  94      30.922   2.574   9.434  1.00 46.29           C
ANISOU 4982  C   ASN B  94     7914   4805   4868   -843   -103  -1114       C
ATOM   4983  O   ASN B  94      30.958   1.463   9.972  1.00 44.51           O
ANISOU 4983  O   ASN B  94     7751   4407   4754   -874    -99  -1135       O
ATOM   4984  CB  ASN B  94      30.353   4.584  10.810  1.00 42.63           C
ANISOU 4984  CB  ASN B  94     7314   4507   4378   -851    -95   -869       C
ATOM   4985  CG  ASN B  94      29.446   3.704  11.644  1.00 45.51           C
ANISOU 4985  CG  ASN B  94     7696   4752   4845   -962   -115   -855       C
ATOM   4986  OD1 ASN B  94      29.877   3.098  12.622  1.00 46.41           O
ANISOU 4986  OD1 ASN B  94     7852   4733   5048   -953    -87   -797       O
ATOM   4987  ND2 ASN B  94      28.190   3.590  11.224  1.00 44.89           N
ANISOU 4987  ND2 ASN B  94     7581   4721   4753  -1070   -164   -907       N
ATOM   4988  N   ARG B  95      30.441   2.761   8.202  1.00 46.60           N
ANISOU 4988  N   ARG B  95     7937   4962   4806   -867   -140  -1217       N
ATOM   4989  CA  ARG B  95      29.909   1.634   7.441  1.00 45.04           C
ANISOU 4989  CA  ARG B  95     7793   4696   4626   -939   -179  -1378       C
ATOM   4990  C   ARG B  95      30.985   0.584   7.159  1.00 47.77           C
ANISOU 4990  C   ARG B  95     8230   4898   5020   -864   -142  -1481       C
ATOM   4991  O   ARG B  95      30.726  -0.625   7.231  1.00 53.20           O
ANISOU 4991  O   ARG B  95     8982   5423   5808   -921   -158  -1570       O
ATOM   4992  CB  ARG B  95      29.290   2.138   6.141  1.00 48.68           C
ANISOU 4992  CB  ARG B  95     8214   5338   4946   -965   -228  -1467       C
ATOM   4993  CG  ARG B  95      28.651   1.037   5.296  1.00 51.81           C
ANISOU 4993  CG  ARG B  95     8656   5684   5347  -1048   -281  -1649       C
ATOM   4994  CD  ARG B  95      28.186   1.619   3.957  1.00 56.20           C
ANISOU 4994  CD  ARG B  95     9171   6446   5737  -1055   -330  -1733       C
ATOM   4995  NE  ARG B  95      29.307   1.951   3.083  1.00 58.71           N
ANISOU 4995  NE  ARG B  95     9517   6853   5938   -932   -285  -1777       N
ATOM   4996  CZ  ARG B  95      29.981   1.053   2.371  1.00 60.59           C
ANISOU 4996  CZ  ARG B  95     9832   7028   6161   -888   -265  -1933       C
ATOM   4997  NH1 ARG B  95      29.689  -0.240   2.427  1.00 56.79           N
ANISOU 4997  NH1 ARG B  95     9414   6379   5786   -954   -287  -2062       N
ATOM   4998  NH2 ARG B  95      30.975   1.462   1.587  1.00 56.07           N
ANISOU 4998  NH2 ARG B  95     9271   6562   5471   -777   -216  -1961       N
ATOM   4999  N   ARG B  96      32.198   1.021   6.849  1.00 46.97           N
ANISOU 4999  N   ARG B  96     8135   4850   4861   -736    -90  -1471       N
ATOM   5000  CA  ARG B  96      33.266   0.092   6.504  1.00 47.97           C
ANISOU 5000  CA  ARG B  96     8338   4859   5029   -649    -50  -1576       C
ATOM   5001  C   ARG B  96      33.912  -0.554   7.724  1.00 48.47           C
ANISOU 5001  C   ARG B  96     8444   4730   5244   -610    -18  -1494       C
ATOM   5002  O   ARG B  96      34.455  -1.660   7.605  1.00 46.13           O
ANISOU 5002  O   ARG B  96     8222   4276   5029   -571     -2  -1589       O
ATOM   5003  CB  ARG B  96      34.329   0.832   5.694  1.00 47.73           C
ANISOU 5003  CB  ARG B  96     8286   4974   4875   -527     -1  -1592       C
ATOM   5004  CG  ARG B  96      33.844   1.297   4.324  1.00 50.44           C
ANISOU 5004  CG  ARG B  96     8605   5504   5056   -550    -30  -1690       C
ATOM   5005  CD  ARG B  96      34.930   2.073   3.643  1.00 50.60           C
ANISOU 5005  CD  ARG B  96     8600   5666   4960   -433     29  -1677       C
ATOM   5006  NE  ARG B  96      34.455   2.834   2.495  1.00 53.14           N
ANISOU 5006  NE  ARG B  96     8883   6197   5110   -452      4  -1710       N
ATOM   5007  CZ  ARG B  96      35.247   3.509   1.671  1.00 49.12           C
ANISOU 5007  CZ  ARG B  96     8353   5839   4473   -367     52  -1708       C
ATOM   5008  NH1 ARG B  96      36.566   3.511   1.818  1.00 42.95           N
ANISOU 5008  NH1 ARG B  96     7578   5026   3716   -258    131  -1689       N
ATOM   5009  NH2 ARG B  96      34.704   4.210   0.686  1.00 47.96           N
ANISOU 5009  NH2 ARG B  96     8171   5882   4169   -392     21  -1719       N
ATOM   5010  N   TRP B  97      33.810   0.101   8.887  1.00 43.00           N
ANISOU 5010  N   TRP B  97     7705   4046   4588   -621    -11  -1322       N
ATOM   5011  CA  TRP B  97      34.689  -0.143  10.031  1.00 47.88           C
ANISOU 5011  CA  TRP B  97     8345   4542   5307   -550     26  -1214       C
ATOM   5012  C   TRP B  97      34.787  -1.618  10.429  1.00 46.61           C
ANISOU 5012  C   TRP B  97     8272   4147   5290   -564     22  -1263       C
ATOM   5013  O   TRP B  97      35.884  -2.121  10.688  1.00 47.64           O
ANISOU 5013  O   TRP B  97     8443   4173   5484   -458     56  -1261       O
ATOM   5014  CB  TRP B  97      34.209   0.704  11.221  1.00 41.18           C
ANISOU 5014  CB  TRP B  97     7433   3743   4468   -595     20  -1040       C
ATOM   5015  CG  TRP B  97      35.231   0.907  12.320  1.00 42.25           C
ANISOU 5015  CG  TRP B  97     7564   3831   4657   -505     56   -914       C
ATOM   5016  CD1 TRP B  97      35.355   0.170  13.464  1.00 45.57           C
ANISOU 5016  CD1 TRP B  97     8027   4097   5191   -511     58   -833       C
ATOM   5017  CD2 TRP B  97      36.241   1.922  12.388  1.00 40.78           C
ANISOU 5017  CD2 TRP B  97     7325   3757   4412   -400     91   -851       C
ATOM   5018  NE1 TRP B  97      36.381   0.652  14.229  1.00 44.58           N
ANISOU 5018  NE1 TRP B  97     7877   3989   5072   -413     86   -729       N
ATOM   5019  CE2 TRP B  97      36.939   1.733  13.600  1.00 41.31           C
ANISOU 5019  CE2 TRP B  97     7401   3735   4559   -346    107   -742       C
ATOM   5020  CE3 TRP B  97      36.612   2.986  11.547  1.00 41.72           C
ANISOU 5020  CE3 TRP B  97     7388   4046   4419   -350    109   -870       C
ATOM   5021  CZ2 TRP B  97      38.002   2.557  13.998  1.00 39.40           C
ANISOU 5021  CZ2 TRP B  97     7110   3567   4293   -248    137   -665       C
ATOM   5022  CZ3 TRP B  97      37.670   3.814  11.942  1.00 42.14           C
ANISOU 5022  CZ3 TRP B  97     7393   4163   4456   -256    146   -786       C
ATOM   5023  CH2 TRP B  97      38.355   3.586  13.163  1.00 40.23           C
ANISOU 5023  CH2 TRP B  97     7157   3829   4300   -207    157   -692       C
ATOM   5024  N   ASP B  98      33.664  -2.323  10.501  1.00 45.99           N
ANISOU 5024  N   ASP B  98     8222   3981   5272   -693    -19  -1303       N
ATOM   5025  CA  ASP B  98      33.655  -3.691  11.027  1.00 52.74           C
ANISOU 5025  CA  ASP B  98     9160   4595   6282   -722    -24  -1322       C
ATOM   5026  C   ASP B  98      33.679  -4.783   9.949  1.00 57.00           C
ANISOU 5026  C   ASP B  98     9773   5026   6858   -728    -38  -1527       C
ATOM   5027  O   ASP B  98      33.543  -5.967  10.289  1.00 52.13           O
ANISOU 5027  O   ASP B  98     9230   4194   6382   -767    -47  -1557       O
ATOM   5028  CB  ASP B  98      32.428  -3.899  11.932  1.00 54.37           C
ANISOU 5028  CB  ASP B  98     9355   4744   6560   -871    -54  -1225       C
ATOM   5029  CG  ASP B  98      32.542  -3.163  13.287  1.00 57.49           C
ANISOU 5029  CG  ASP B  98     9702   5184   6957   -856    -33  -1019       C
ATOM   5030  OD1 ASP B  98      33.674  -2.961  13.786  1.00 56.12           O
ANISOU 5030  OD1 ASP B  98     9537   4997   6791   -734      0   -945       O
ATOM   5031  OD2 ASP B  98      31.490  -2.774  13.848  1.00 59.32           O
ANISOU 5031  OD2 ASP B  98     9884   5474   7181   -966    -51   -938       O
ATOM   5032  N   LYS B  99      33.833  -4.435   8.668  1.00 53.79           N
ANISOU 5032  N   LYS B  99     9351   4758   6329   -691    -39  -1668       N
ATOM   5033  CA  LYS B  99      33.831  -5.459   7.626  1.00 56.78           C
ANISOU 5033  CA  LYS B  99     9798   5045   6730   -697    -53  -1880       C
ATOM   5034  C   LYS B  99      34.899  -6.512   7.901  1.00 57.29           C
ANISOU 5034  C   LYS B  99     9945   4895   6929   -591    -16  -1919       C
ATOM   5035  O   LYS B  99      36.057  -6.184   8.172  1.00 60.44           O
ANISOU 5035  O   LYS B  99    10331   5314   7319   -454     33  -1854       O
ATOM   5036  CB  LYS B  99      34.051  -4.829   6.249  1.00 58.32           C
ANISOU 5036  CB  LYS B  99     9961   5447   6750   -647    -48  -2011       C
ATOM   5037  CG  LYS B  99      32.876  -4.017   5.749  1.00 61.53           C
ANISOU 5037  CG  LYS B  99    10300   6047   7033   -758   -100  -2011       C
ATOM   5038  CD  LYS B  99      33.212  -3.421   4.400  1.00 62.80           C
ANISOU 5038  CD  LYS B  99    10436   6410   7013   -695    -92  -2125       C
ATOM   5039  CE  LYS B  99      33.061  -4.450   3.293  1.00 61.36           C
ANISOU 5039  CE  LYS B  99    10321   6174   6820   -717   -116  -2364       C
ATOM   5040  NZ  LYS B  99      31.725  -4.366   2.668  1.00 65.51           N
ANISOU 5040  NZ  LYS B  99    10816   6800   7274   -855   -195  -2443       N
ATOM   5041  N   PHE B 100      34.489  -7.779   7.849  1.00 61.68           N
ANISOU 5041  N   PHE B 100    10579   5239   7618   -657    -41  -2023       N
ATOM   5042  CA  PHE B 100      35.316  -8.924   8.209  1.00 60.53           C
ANISOU 5042  CA  PHE B 100    10518   4847   7634   -573    -16  -2053       C
ATOM   5043  C   PHE B 100      34.747 -10.138   7.497  1.00 62.17           C
ANISOU 5043  C   PHE B 100    10804   4887   7933   -654    -51  -2256       C
ATOM   5044  O   PHE B 100      33.532 -10.206   7.288  1.00 62.14           O
ANISOU 5044  O   PHE B 100    10787   4906   7919   -810   -102  -2298       O
ATOM   5045  CB  PHE B 100      35.314  -9.154   9.732  1.00 63.69           C
ANISOU 5045  CB  PHE B 100    10931   5099   8169   -592    -14  -1837       C
ATOM   5046  CG  PHE B 100      36.187 -10.300  10.180  1.00 70.68           C
ANISOU 5046  CG  PHE B 100    11902   5726   9225   -496      7  -1840       C
ATOM   5047  CD1 PHE B 100      35.618 -11.525  10.534  1.00 71.39           C
ANISOU 5047  CD1 PHE B 100    12074   5562   9491   -587    -20  -1861       C
ATOM   5048  CD2 PHE B 100      37.572 -10.154  10.274  1.00 71.83           C
ANISOU 5048  CD2 PHE B 100    12044   5882   9368   -314     53  -1814       C
ATOM   5049  CE1 PHE B 100      36.418 -12.596  10.946  1.00 70.83           C
ANISOU 5049  CE1 PHE B 100    12085   5239   9589   -492     -4  -1855       C
ATOM   5050  CE2 PHE B 100      38.378 -11.221  10.689  1.00 72.48           C
ANISOU 5050  CE2 PHE B 100    12199   5724   9616   -215     67  -1813       C
ATOM   5051  CZ  PHE B 100      37.798 -12.441  11.026  1.00 77.12           C
ANISOU 5051  CZ  PHE B 100    12875   6050  10378   -300     38  -1831       C
ATOM   5052  N   PRO B 101      35.589 -11.099   7.078  1.00 68.23           N
ANISOU 5052  N   PRO B 101    11646   5489   8790   -550    -26  -2396       N
ATOM   5053  CA  PRO B 101      37.051 -11.039   7.053  1.00 68.18           C
ANISOU 5053  CA  PRO B 101    11644   5481   8781   -355     34  -2392       C
ATOM   5054  C   PRO B 101      37.589 -10.446   5.759  1.00 64.28           C
ANISOU 5054  C   PRO B 101    11113   5204   8107   -267     65  -2549       C
ATOM   5055  O   PRO B 101      37.018 -10.702   4.694  1.00 65.28           O
ANISOU 5055  O   PRO B 101    11258   5380   8166   -332     39  -2743       O
ATOM   5056  CB  PRO B 101      37.447 -12.510   7.170  1.00 69.49           C
ANISOU 5056  CB  PRO B 101    11895   5354   9155   -308     35  -2481       C
ATOM   5057  CG  PRO B 101      36.358 -13.231   6.438  1.00 64.10           C
ANISOU 5057  CG  PRO B 101    11200   4639   8516   -446    -20  -2642       C
ATOM   5058  CD  PRO B 101      35.095 -12.421   6.637  1.00 65.19           C
ANISOU 5058  CD  PRO B 101    11308   4913   8549   -618    -62  -2559       C
ATOM   5059  N   VAL B 102      38.675  -9.683   5.850  1.00 63.53           N
ANISOU 5059  N   VAL B 102    10964   5241   7935   -126    120  -2467       N
ATOM   5060  CA  VAL B 102      39.388  -9.213   4.661  1.00 63.93           C
ANISOU 5060  CA  VAL B 102    10981   5480   7827    -23    166  -2607       C
ATOM   5061  C   VAL B 102      40.865  -9.549   4.834  1.00 60.90           C
ANISOU 5061  C   VAL B 102    10605   5016   7516    164    232  -2610       C
ATOM   5062  O   VAL B 102      41.690  -8.639   5.000  1.00 59.76           O
ANISOU 5062  O   VAL B 102    10388   5027   7292    259    278  -2502       O
ATOM   5063  CB  VAL B 102      39.198  -7.705   4.430  1.00 62.07           C
ANISOU 5063  CB  VAL B 102    10648   5540   7394    -47    173  -2502       C
ATOM   5064  CG1 VAL B 102      39.574  -7.350   2.988  1.00 59.42           C
ANISOU 5064  CG1 VAL B 102    10293   5404   6881     13    208  -2674       C
ATOM   5065  CG2 VAL B 102      37.770  -7.252   4.769  1.00 60.67           C
ANISOU 5065  CG2 VAL B 102    10446   5420   7187   -222    105  -2413       C
ATOM   5066  N   PRO B 103      41.240 -10.823   4.801  1.00 63.22           N
ANISOU 5066  N   PRO B 103    10981   5070   7969    222    238  -2732       N
ATOM   5067  CA  PRO B 103      42.637 -11.205   5.066  1.00 65.11           C
ANISOU 5067  CA  PRO B 103    11222   5216   8300    408    295  -2725       C
ATOM   5068  C   PRO B 103      43.564 -10.633   4.011  1.00 63.31           C
ANISOU 5068  C   PRO B 103    10937   5202   7915    532    366  -2842       C
ATOM   5069  O   PRO B 103      43.235 -10.661   2.815  1.00 62.24           O
ANISOU 5069  O   PRO B 103    10805   5181   7660    500    371  -3031       O
ATOM   5070  CB  PRO B 103      42.606 -12.740   4.988  1.00 64.64           C
ANISOU 5070  CB  PRO B 103    11215   4897   8448    418    274  -2854       C
ATOM   5071  CG  PRO B 103      41.433 -13.049   4.106  1.00 61.09           C
ANISOU 5071  CG  PRO B 103    10767   4493   7953    269    224  -3013       C
ATOM   5072  CD  PRO B 103      40.415 -11.968   4.381  1.00 61.27           C
ANISOU 5072  CD  PRO B 103    10784   4665   7831    124    188  -2889       C
ATOM   5073  N   PRO B 104      44.742 -10.151   4.404  1.00 62.77           N
ANISOU 5073  N   PRO B 104    10804   5200   7846    673    420  -2736       N
ATOM   5074  CA  PRO B 104      45.682  -9.594   3.424  1.00 65.25           C
ANISOU 5074  CA  PRO B 104    11054   5723   8014    791    498  -2835       C
ATOM   5075  C   PRO B 104      46.217 -10.669   2.488  1.00 65.87           C
ANISOU 5075  C   PRO B 104    11177   5706   8142    890    538  -3086       C
ATOM   5076  O   PRO B 104      46.168 -11.863   2.779  1.00 68.25           O
ANISOU 5076  O   PRO B 104    11513   5778   8640    898    509  -3140       O
ATOM   5077  CB  PRO B 104      46.802  -9.009   4.293  1.00 62.98           C
ANISOU 5077  CB  PRO B 104    10686   5476   7767    910    537  -2649       C
ATOM   5078  CG  PRO B 104      46.735  -9.789   5.564  1.00 65.67           C
ANISOU 5078  CG  PRO B 104    11080   5556   8316    911    488  -2527       C
ATOM   5079  CD  PRO B 104      45.274 -10.096   5.775  1.00 63.39           C
ANISOU 5079  CD  PRO B 104    10861   5172   8054    728    413  -2518       C
ATOM   5080  N   ASN B 105      46.733 -10.218   1.340  1.00 70.06           N
ANISOU 5080  N   ASN B 105    11651   6461   8510    953    603  -3214       N
ATOM   5081  CA  ASN B 105      47.327 -11.084   0.321  1.00 67.73           C
ANISOU 5081  CA  ASN B 105    11324   6165   8244   1038    653  -3439       C
ATOM   5082  C   ASN B 105      48.847 -11.030   0.431  1.00 71.08           C
ANISOU 5082  C   ASN B 105    11687   6613   8709   1229    742  -3421       C
ATOM   5083  O   ASN B 105      49.444  -9.966   0.225  1.00 65.69           O
ANISOU 5083  O   ASN B 105    10945   6143   7871   1287    801  -3353       O
ATOM   5084  CB  ASN B 105      46.899 -10.650  -1.081  1.00 71.80           C
ANISOU 5084  CB  ASN B 105    11807   6933   8541    976    672  -3596       C
ATOM   5085  CG  ASN B 105      45.724 -11.439  -1.605  1.00 78.29           C
ANISOU 5085  CG  ASN B 105    12671   7683   9395    838    600  -3749       C
ATOM   5086  OD1 ASN B 105      45.657 -12.657  -1.442  1.00 84.97           O
ANISOU 5086  OD1 ASN B 105    13550   8300  10436    840    579  -3848       O
ATOM   5087  ND2 ASN B 105      44.783 -10.746  -2.238  1.00 77.39           N
ANISOU 5087  ND2 ASN B 105    12549   7762   9094    718    558  -3767       N
ATOM   5088  N   VAL B 106      49.467 -12.173   0.729  1.00 69.81           N
ANISOU 5088  N   VAL B 106    11532   6235   8758   1325    754  -3482       N
ATOM   5089  CA  VAL B 106      50.919 -12.261   0.882  1.00 69.91           C
ANISOU 5089  CA  VAL B 106    11478   6247   8838   1512    834  -3469       C
ATOM   5090  C   VAL B 106      51.530 -12.532  -0.488  1.00 70.71           C
ANISOU 5090  C   VAL B 106    11524   6490   8851   1576    933  -3692       C
ATOM   5091  O   VAL B 106      51.294 -13.585  -1.086  1.00 71.06           O
ANISOU 5091  O   VAL B 106    11607   6417   8974   1549    948  -3870       O
ATOM   5092  CB  VAL B 106      51.327 -13.347   1.887  1.00 69.32           C
ANISOU 5092  CB  VAL B 106    11431   5872   9033   1589    803  -3410       C
ATOM   5093  CG1 VAL B 106      52.838 -13.412   1.988  1.00 66.43           C
ANISOU 5093  CG1 VAL B 106    10982   5525   8732   1787    883  -3402       C
ATOM   5094  CG2 VAL B 106      50.735 -13.061   3.252  1.00 66.69           C
ANISOU 5094  CG2 VAL B 106    11155   5413   8771   1518    716  -3175       C
ATOM   5095  N   VAL B 107      52.327 -11.591  -0.977  1.00 70.67           N
ANISOU 5095  N   VAL B 107    11437   6733   8683   1653   1015  -3674       N
ATOM   5096  CA  VAL B 107      52.980 -11.721  -2.270  1.00 67.81           C
ANISOU 5096  CA  VAL B 107    11024   6531   8209   1710   1129  -3855       C
ATOM   5097  C   VAL B 107      54.430 -12.136  -2.063  1.00 68.99           C
ANISOU 5097  C   VAL B 107    11105   6622   8486   1897   1214  -3861       C
ATOM   5098  O   VAL B 107      55.019 -11.932  -0.996  1.00 70.04           O
ANISOU 5098  O   VAL B 107    11199   6676   8735   1986   1189  -3703       O
ATOM   5099  CB  VAL B 107      52.875 -10.417  -3.095  1.00 72.75           C
ANISOU 5099  CB  VAL B 107    11596   7489   8556   1661   1173  -3833       C
ATOM   5100  CG1 VAL B 107      51.448  -9.899  -3.104  1.00 68.53           C
ANISOU 5100  CG1 VAL B 107    11122   7008   7908   1486   1074  -3786       C
ATOM   5101  CG2 VAL B 107      53.795  -9.343  -2.506  1.00 73.42           C
ANISOU 5101  CG2 VAL B 107    11591   7706   8598   1761   1212  -3653       C
ATOM   5102  N   LYS B 108      55.004 -12.749  -3.104  1.00 79.93           N
ANISOU 5102  N   LYS B 108    12487   8043   9840   1957   1319  -4040       N
ATOM   5103  CA  LYS B 108      56.411 -13.132  -3.140  1.00 80.06           C
ANISOU 5103  CA  LYS B 108    12432   8040   9949   2137   1416  -4069       C
ATOM   5104  C   LYS B 108      57.283 -11.879  -3.132  1.00 80.97           C
ANISOU 5104  C   LYS B 108    12415   8414   9934   2210   1476  -3956       C
ATOM   5105  O   LYS B 108      56.852 -10.787  -3.508  1.00 74.79           O
ANISOU 5105  O   LYS B 108    11609   7860   8947   2122   1475  -3901       O
ATOM   5106  CB  LYS B 108      56.711 -13.963  -4.396  1.00 77.98           C
ANISOU 5106  CB  LYS B 108    12219   7783   9626   2176   1516  -4281       C
ATOM   5107  CG  LYS B 108      57.912 -14.923  -4.315  1.00 97.71           C
ANISOU 5107  CG  LYS B 108    14693  10133  12299   2357   1591  -4344       C
ATOM   5108  CD  LYS B 108      59.295 -14.303  -4.582  1.00 98.54           C
ANISOU 5108  CD  LYS B 108    14654  10445  12344   2503   1702  -4317       C
ATOM   5109  CE  LYS B 108      60.343 -14.978  -3.692  1.00 96.68           C
ANISOU 5109  CE  LYS B 108    14361  10015  12359   2671   1713  -4262       C
ATOM   5110  NZ  LYS B 108      61.652 -14.268  -3.649  1.00 97.37           N
ANISOU 5110  NZ  LYS B 108    14287  10290  12419   2804   1797  -4193       N
ATOM   5111  N   ARG B 109      58.536 -12.067  -2.726  1.00 84.77           N
ANISOU 5111  N   ARG B 109    12808   8860  10539   2372   1532  -3919       N
ATOM   5112  CA  ARG B 109      59.462 -10.958  -2.546  1.00 80.59           C
ANISOU 5112  CA  ARG B 109    12145   8547   9928   2451   1587  -3796       C
ATOM   5113  C   ARG B 109      59.554 -10.062  -3.790  1.00 81.58           C
ANISOU 5113  C   ARG B 109    12218   8989   9789   2402   1685  -3852       C
ATOM   5114  O   ARG B 109      59.435  -8.840  -3.688  1.00 78.94           O
ANISOU 5114  O   ARG B 109    11831   8850   9311   2351   1680  -3724       O
ATOM   5115  CB  ARG B 109      60.836 -11.505  -2.156  1.00 84.89           C
ANISOU 5115  CB  ARG B 109    12598   9006  10649   2637   1646  -3793       C
ATOM   5116  CG  ARG B 109      61.780 -10.450  -1.649  1.00 80.38           C
ANISOU 5116  CG  ARG B 109    11887   8607  10047   2720   1678  -3639       C
ATOM   5117  CD  ARG B 109      63.123 -11.003  -1.220  1.00 75.36           C
ANISOU 5117  CD  ARG B 109    11149   7889   9595   2903   1726  -3631       C
ATOM   5118  NE  ARG B 109      63.957  -9.907  -0.740  1.00 82.13           N
ANISOU 5118  NE  ARG B 109    11867   8929  10412   2965   1752  -3480       N
ATOM   5119  CZ  ARG B 109      64.535  -9.011  -1.533  1.00 82.71           C
ANISOU 5119  CZ  ARG B 109    11830   9281  10313   2966   1862  -3491       C
ATOM   5120  NH1 ARG B 109      64.425  -9.079  -2.852  1.00 83.47           N
ANISOU 5120  NH1 ARG B 109    11942   9516  10256   2919   1957  -3642       N
ATOM   5121  NH2 ARG B 109      65.227  -8.011  -0.991  1.00 73.44           N
ANISOU 5121  NH2 ARG B 109    10532   8255   9119   3011   1878  -3340       N
ATOM   5122  N   GLU B 110      59.765 -10.639  -4.978  1.00 82.65           N
ANISOU 5122  N   GLU B 110    12377   9178   9847   2418   1777  -4031       N
ATOM   5123  CA  GLU B 110      59.916  -9.781  -6.158  1.00 85.31           C
ANISOU 5123  CA  GLU B 110    12666   9822   9928   2376   1872  -4063       C
ATOM   5124  C   GLU B 110      58.624  -9.275  -6.777  1.00 85.11           C
ANISOU 5124  C   GLU B 110    12725   9913   9700   2203   1819  -4074       C
ATOM   5125  O   GLU B 110      58.686  -8.536  -7.768  1.00 85.01           O
ANISOU 5125  O   GLU B 110    12679  10156   9464   2162   1889  -4082       O
ATOM   5126  CB  GLU B 110      60.783 -10.455  -7.228  1.00 88.07           C
ANISOU 5126  CB  GLU B 110    12998  10222  10242   2478   1999  -4228       C
ATOM   5127  CG  GLU B 110      62.030 -11.105  -6.688  1.00 90.75           C
ANISOU 5127  CG  GLU B 110    13258  10431  10792   2655   2051  -4236       C
ATOM   5128  CD  GLU B 110      62.795 -10.134  -5.759  1.00 92.21           C
ANISOU 5128  CD  GLU B 110    13296  10709  11030   2715   2051  -4046       C
ATOM   5129  OE1 GLU B 110      63.693  -9.400  -6.235  1.00101.97           O
ANISOU 5129  OE1 GLU B 110    14408  12177  12161   2765   2157  -4014       O
ATOM   5130  OE2 GLU B 110      62.521 -10.127  -4.543  1.00 90.26           O
ANISOU 5130  OE2 GLU B 110    13060  10301  10933   2714   1944  -3925       O
ATOM   5131  N   ALA B 111      57.464  -9.611  -6.227  1.00 83.49           N
ANISOU 5131  N   ALA B 111    12624   9536   9564   2098   1696  -4063       N
ATOM   5132  CA  ALA B 111      56.231  -8.917  -6.589  1.00 82.44           C
ANISOU 5132  CA  ALA B 111    12546   9527   9249   1933   1629  -4029       C
ATOM   5133  C   ALA B 111      56.027  -7.640  -5.770  1.00 80.59           C
ANISOU 5133  C   ALA B 111    12251   9401   8968   1892   1575  -3818       C
ATOM   5134  O   ALA B 111      55.085  -6.881  -6.038  1.00 86.94           O
ANISOU 5134  O   ALA B 111    13085  10337   9612   1765   1525  -3762       O
ATOM   5135  CB  ALA B 111      55.029  -9.855  -6.415  1.00 80.39           C
ANISOU 5135  CB  ALA B 111    12422   9042   9081   1828   1523  -4116       C
ATOM   5136  N   ALA B 112      56.900  -7.384  -4.794  1.00 78.11           N
ANISOU 5136  N   ALA B 112    11861   9034   8784   2003   1584  -3693       N
ATOM   5137  CA  ALA B 112      56.765  -6.267  -3.876  1.00 70.76           C
ANISOU 5137  CA  ALA B 112    10899   8159   7826   1982   1533  -3480       C
ATOM   5138  C   ALA B 112      57.695  -5.138  -4.288  1.00 71.26           C
ANISOU 5138  C   ALA B 112    10834   8494   7748   2032   1641  -3394       C
ATOM   5139  O   ALA B 112      58.922  -5.295  -4.191  1.00 69.90           O
ANISOU 5139  O   ALA B 112    10564   8335   7661   2163   1722  -3401       O
ATOM   5140  CB  ALA B 112      57.077  -6.716  -2.449  1.00 74.17           C
ANISOU 5140  CB  ALA B 112    11348   8343   8492   2065   1467  -3376       C
ATOM   5141  N   PRO B 113      57.174  -3.980  -4.707  1.00 71.48           N
ANISOU 5141  N   PRO B 113    10850   8736   7572   1930   1645  -3299       N
ATOM   5142  CA  PRO B 113      58.057  -2.874  -5.118  1.00 68.45           C
ANISOU 5142  CA  PRO B 113    10339   8610   7060   1965   1754  -3203       C
ATOM   5143  C   PRO B 113      58.986  -2.365  -4.025  1.00 69.87           C
ANISOU 5143  C   PRO B 113    10421   8758   7370   2052   1769  -3036       C
ATOM   5144  O   PRO B 113      60.063  -1.845  -4.341  1.00 70.50           O
ANISOU 5144  O   PRO B 113    10375   9004   7406   2127   1878  -3008       O
ATOM   5145  CB  PRO B 113      57.065  -1.789  -5.557  1.00 70.30           C
ANISOU 5145  CB  PRO B 113    10605   9023   7084   1820   1722  -3104       C
ATOM   5146  CG  PRO B 113      55.811  -2.547  -5.909  1.00 70.38           C
ANISOU 5146  CG  PRO B 113    10743   8924   7076   1718   1629  -3229       C
ATOM   5147  CD  PRO B 113      55.751  -3.653  -4.908  1.00 70.79           C
ANISOU 5147  CD  PRO B 113    10861   8672   7365   1775   1555  -3278       C
ATOM   5148  N   CYS B 114      58.615  -2.499  -2.748  1.00 64.30           N
ANISOU 5148  N   CYS B 114     9746   7847   6836   2014   1658  -2905       N
ATOM   5149  CA  CYS B 114      59.513  -2.078  -1.677  1.00 64.65           C
ANISOU 5149  CA  CYS B 114     9681   7859   7026   2071   1656  -2735       C
ATOM   5150  C   CYS B 114      60.797  -2.898  -1.619  1.00 67.85           C
ANISOU 5150  C   CYS B 114    10016   8199   7565   2259   1728  -2843       C
ATOM   5151  O   CYS B 114      61.715  -2.511  -0.891  1.00 67.39           O
ANISOU 5151  O   CYS B 114     9842   8155   7609   2322   1743  -2719       O
ATOM   5152  CB  CYS B 114      58.813  -2.159  -0.324  1.00 59.93           C
ANISOU 5152  CB  CYS B 114     9140   7054   6575   1997   1521  -2586       C
ATOM   5153  SG  CYS B 114      58.590  -3.834   0.323  1.00 64.40           S
ANISOU 5153  SG  CYS B 114     9826   7288   7357   2078   1442  -2706       S
ATOM   5154  N   LYS B 115      60.878  -4.023  -2.332  1.00 65.69           N
ANISOU 5154  N   LYS B 115     9808   7849   7302   2354   1766  -3074       N
ATOM   5155  CA  LYS B 115      62.089  -4.838  -2.381  1.00 70.31           C
ANISOU 5155  CA  LYS B 115    10311   8376   8028   2515   1836  -3175       C
ATOM   5156  C   LYS B 115      62.949  -4.544  -3.606  1.00 73.52           C
ANISOU 5156  C   LYS B 115    10602   9026   8306   2544   1984  -3261       C
ATOM   5157  O   LYS B 115      63.848  -5.333  -3.920  1.00 75.60           O
ANISOU 5157  O   LYS B 115    10809   9248   8668   2656   2054  -3374       O
ATOM   5158  CB  LYS B 115      61.734  -6.328  -2.357  1.00 72.06           C
ANISOU 5158  CB  LYS B 115    10637   8338   8405   2541   1782  -3327       C
ATOM   5159  CG  LYS B 115      60.789  -6.756  -1.242  1.00 72.00           C
ANISOU 5159  CG  LYS B 115    10757   8074   8526   2493   1638  -3250       C
ATOM   5160  CD  LYS B 115      61.527  -6.934   0.052  1.00 73.29           C
ANISOU 5160  CD  LYS B 115    10873   8086   8887   2613   1595  -3122       C
ATOM   5161  CE  LYS B 115      60.592  -7.381   1.153  1.00 73.84           C
ANISOU 5161  CE  LYS B 115    11065   7905   9086   2541   1456  -3020       C
ATOM   5162  NZ  LYS B 115      61.380  -7.705   2.368  1.00 75.59           N
ANISOU 5162  NZ  LYS B 115    11230   7979   9513   2653   1411  -2892       N
ATOM   5163  N   GLU B 116      62.690  -3.442  -4.317  1.00 73.52           N
ANISOU 5163  N   GLU B 116    10572   9274   8090   2445   2036  -3201       N
ATOM   5164  CA  GLU B 116      63.435  -3.171  -5.547  1.00 75.61           C
ANISOU 5164  CA  GLU B 116    10742   9768   8216   2457   2179  -3270       C
ATOM   5165  C   GLU B 116      64.926  -2.980  -5.275  1.00 74.09           C
ANISOU 5165  C   GLU B 116    10380   9648   8123   2588   2274  -3224       C
ATOM   5166  O   GLU B 116      65.770  -3.534  -5.987  1.00 79.19           O
ANISOU 5166  O   GLU B 116    10967  10338   8785   2668   2377  -3344       O
ATOM   5167  CB  GLU B 116      62.849  -1.950  -6.262  1.00 72.03           C
ANISOU 5167  CB  GLU B 116    10289   9560   7521   2319   2206  -3177       C
ATOM   5168  CG  GLU B 116      61.692  -2.266  -7.217  1.00 72.18           C
ANISOU 5168  CG  GLU B 116    10441   9596   7387   2201   2172  -3287       C
ATOM   5169  CD  GLU B 116      60.800  -1.061  -7.504  1.00 79.66           C
ANISOU 5169  CD  GLU B 116    11413  10717   8136   2056   2140  -3152       C
ATOM   5170  OE1 GLU B 116      61.249   0.094  -7.312  1.00 79.05           O
ANISOU 5170  OE1 GLU B 116    11236  10798   8000   2044   2186  -2986       O
ATOM   5171  OE2 GLU B 116      59.637  -1.272  -7.911  1.00 83.54           O
ANISOU 5171  OE2 GLU B 116    12023  11182   8537   1952   2066  -3209       O
ATOM   5172  N   ASN B 117      65.275  -2.213  -4.248  1.00 78.83           N
ANISOU 5172  N   ASN B 117    10902  10259   8792   2614   2242  -3052       N
ATOM   5173  CA  ASN B 117      66.668  -1.982  -3.892  1.00 74.81           C
ANISOU 5173  CA  ASN B 117    10218   9819   8387   2733   2318  -2997       C
ATOM   5174  C   ASN B 117      66.881  -2.420  -2.455  1.00 75.35           C
ANISOU 5174  C   ASN B 117    10286   9664   8678   2831   2214  -2927       C
ATOM   5175  O   ASN B 117      65.985  -2.285  -1.616  1.00 74.24           O
ANISOU 5175  O   ASN B 117    10243   9386   8579   2745   2088  -2817       O
ATOM   5176  CB  ASN B 117      67.054  -0.503  -4.033  1.00 76.21           C
ANISOU 5176  CB  ASN B 117    10271  10252   8433   2669   2392  -2835       C
ATOM   5177  CG  ASN B 117      66.751   0.052  -5.404  1.00 74.81           C
ANISOU 5177  CG  ASN B 117    10104  10297   8023   2557   2483  -2865       C
ATOM   5178  OD1 ASN B 117      67.639   0.162  -6.255  1.00 74.53           O
ANISOU 5178  OD1 ASN B 117     9962  10424   7931   2585   2613  -2908       O
ATOM   5179  ND2 ASN B 117      65.488   0.429  -5.622  1.00 71.11           N
ANISOU 5179  ND2 ASN B 117     9763   9839   7416   2427   2414  -2832       N
ATOM   5180  N   VAL B 118      68.077  -2.916  -2.162  1.00 75.77           N
ANISOU 5180  N   VAL B 118    10218   9681   8891   2972   2257  -2955       N
ATOM   5181  CA  VAL B 118      68.402  -3.436  -0.837  1.00 77.83           C
ANISOU 5181  CA  VAL B 118    10469   9731   9372   3081   2157  -2889       C
ATOM   5182  C   VAL B 118      69.569  -2.642  -0.263  1.00 78.36           C
ANISOU 5182  C   VAL B 118    10339   9931   9504   3142   2197  -2752       C
ATOM   5183  O   VAL B 118      70.596  -2.469  -0.928  1.00 74.26           O
ANISOU 5183  O   VAL B 118     9673   9581   8961   3201   2322  -2802       O
ATOM   5184  CB  VAL B 118      68.729  -4.944  -0.900  1.00 78.42           C
ANISOU 5184  CB  VAL B 118    10583   9594   9620   3194   2146  -3043       C
ATOM   5185  CG1 VAL B 118      69.592  -5.385   0.276  1.00 80.62           C
ANISOU 5185  CG1 VAL B 118    10777   9728  10128   3340   2086  -2966       C
ATOM   5186  CG2 VAL B 118      67.442  -5.748  -0.912  1.00 77.05           C
ANISOU 5186  CG2 VAL B 118    10613   9211   9452   3120   2051  -3121       C
ATOM   5187  N   ILE B 119      69.420  -2.160   0.971  1.00 86.34           N
ANISOU 5187  N   ILE B 119    11333  10858  10613   3075   2079  -2553       N
ATOM   5188  CA  ILE B 119      70.641  -1.748   1.640  1.00 82.56           C
ANISOU 5188  CA  ILE B 119    10665  10452  10252   3155   2094  -2450       C
ATOM   5189  C   ILE B 119      70.924  -2.466   2.959  1.00 80.29           C
ANISOU 5189  C   ILE B 119    10379   9945  10184   3256   1969  -2384       C
ATOM   5190  O   ILE B 119      70.616  -1.954   4.034  1.00 82.57           O
ANISOU 5190  O   ILE B 119    10672  10177  10522   3169   1855  -2207       O
ATOM   5191  CB  ILE B 119      70.726  -0.230   1.841  1.00 78.70           C
ANISOU 5191  CB  ILE B 119    10071  10155   9676   3005   2104  -2263       C
ATOM   5192  CG1 ILE B 119      70.459   0.464   0.526  1.00 75.90           C
ANISOU 5192  CG1 ILE B 119     9718  10016   9104   2911   2228  -2312       C
ATOM   5193  CG2 ILE B 119      72.108   0.159   2.359  1.00 77.85           C
ANISOU 5193  CG2 ILE B 119     9748  10148   9686   3095   2139  -2188       C
ATOM   5194  CD1 ILE B 119      70.722   1.893   0.614  1.00 77.45           C
ANISOU 5194  CD1 ILE B 119     9794  10399   9233   2787   2259  -2142       C
ATOM   5195  N   ASP B 120      71.432  -3.718   2.854  1.00 83.42           N
ANISOU 5195  N   ASP B 120    10785  10204  10707   3442   1986  -2534       N
ATOM   5196  CA  ASP B 120      72.857  -4.004   2.618  1.00 86.40           C
ANISOU 5196  CA  ASP B 120    10981  10670  11176   3621   2082  -2611       C
ATOM   5197  C   ASP B 120      73.913  -3.595   3.673  1.00 86.75           C
ANISOU 5197  C   ASP B 120    10843  10755  11363   3694   2036  -2462       C
ATOM   5198  O   ASP B 120      73.930  -4.095   4.809  1.00 81.55           O
ANISOU 5198  O   ASP B 120    10211   9911  10861   3752   1907  -2375       O
ATOM   5199  CB  ASP B 120      72.983  -3.476   1.165  1.00 90.10           C
ANISOU 5199  CB  ASP B 120    11401  11376  11456   3542   2241  -2709       C
ATOM   5200  CG  ASP B 120      74.348  -3.077   0.706  1.00 95.48           C
ANISOU 5200  CG  ASP B 120    11862  12265  12150   3603   2369  -2717       C
ATOM   5201  OD1 ASP B 120      74.575  -1.826   0.825  1.00 95.22           O
ANISOU 5201  OD1 ASP B 120    11717  12431  12031   3531   2404  -2591       O
ATOM   5202  OD2 ASP B 120      75.059  -3.898   0.070  1.00106.66           O
ANISOU 5202  OD2 ASP B 120    13230  13666  13631   3696   2451  -2850       O
ATOM   5203  N   LYS B 121      74.860  -2.754   3.253  1.00 89.71           N
ANISOU 5203  N   LYS B 121    11024  11374  11687   3698   2147  -2441       N
ATOM   5204  CA  LYS B 121      76.148  -2.531   3.899  1.00 86.86           C
ANISOU 5204  CA  LYS B 121    10449  11091  11464   3806   2147  -2367       C
ATOM   5205  C   LYS B 121      76.333  -1.033   4.061  1.00 84.37           C
ANISOU 5205  C   LYS B 121    10010  10987  11061   3642   2165  -2204       C
ATOM   5206  O   LYS B 121      75.865  -0.252   3.225  1.00 82.40           O
ANISOU 5206  O   LYS B 121     9788  10884  10635   3502   2248  -2204       O
ATOM   5207  CB  LYS B 121      77.318  -3.038   3.023  1.00 88.81           C
ANISOU 5207  CB  LYS B 121    10551  11430  11761   3912   2283  -2501       C
ATOM   5208  CG  LYS B 121      77.576  -4.533   2.954  1.00 91.85           C
ANISOU 5208  CG  LYS B 121    10996  11602  12300   4049   2266  -2626       C
ATOM   5209  CD  LYS B 121      78.337  -4.864   1.654  1.00 88.59           C
ANISOU 5209  CD  LYS B 121    10499  11311  11848   4089   2438  -2779       C
ATOM   5210  CE  LYS B 121      77.791  -6.118   0.971  1.00 94.73           C
ANISOU 5210  CE  LYS B 121    11451  11904  12636   4123   2457  -2949       C
ATOM   5211  NZ  LYS B 121      76.782  -5.849  -0.096  1.00 91.58           N
ANISOU 5211  NZ  LYS B 121    11196  11579  12022   3981   2521  -3034       N
ATOM   5212  N   ASP B 122      77.049  -0.632   5.108  1.00 82.07           N
ANISOU 5212  N   ASP B 122     9575  10713  10894   3664   2087  -2069       N
ATOM   5213  CA  ASP B 122      77.302   0.788   5.362  1.00 82.35           C
ANISOU 5213  CA  ASP B 122     9482  10934  10874   3511   2095  -1917       C
ATOM   5214  C   ASP B 122      76.003   1.591   5.323  1.00 74.95           C
ANISOU 5214  C   ASP B 122     8702   9987   9789   3292   2050  -1824       C
ATOM   5215  O   ASP B 122      75.870   2.563   4.579  1.00 72.95           O
ANISOU 5215  O   ASP B 122     8415   9907   9397   3163   2144  -1797       O
ATOM   5216  CB  ASP B 122      78.311   1.350   4.358  1.00 82.80           C
ANISOU 5216  CB  ASP B 122     9344  11245  10873   3533   2275  -1977       C
ATOM   5217  CG  ASP B 122      79.732   1.286   4.865  1.00 93.85           C
ANISOU 5217  CG  ASP B 122    10506  12721  12433   3673   2284  -1962       C
ATOM   5218  OD1 ASP B 122      79.972   0.589   5.877  1.00 97.95           O
ANISOU 5218  OD1 ASP B 122    11022  13083  13111   3789   2158  -1935       O
ATOM   5219  OD2 ASP B 122      80.610   1.941   4.258  1.00 96.16           O
ANISOU 5219  OD2 ASP B 122    10609  13234  12694   3664   2417  -1972       O
ATOM   5220  N   ILE B 123      75.019   1.158   6.112  1.00 74.66           N
ANISOU 5220  N   ILE B 123     8840   9744   9782   3253   1907  -1772       N
ATOM   5221  CA  ILE B 123      73.699   1.773   6.027  1.00 70.80           C
ANISOU 5221  CA  ILE B 123     8512   9230   9158   3061   1864  -1704       C
ATOM   5222  C   ILE B 123      73.784   3.252   6.372  1.00 68.77           C
ANISOU 5222  C   ILE B 123     8152   9125   8852   2901   1855  -1546       C
ATOM   5223  O   ILE B 123      74.354   3.644   7.397  1.00 69.25           O
ANISOU 5223  O   ILE B 123     8101   9191   9019   2905   1776  -1438       O
ATOM   5224  CB  ILE B 123      72.701   1.042   6.936  1.00 73.55           C
ANISOU 5224  CB  ILE B 123     9046   9335   9566   3051   1711  -1667       C
ATOM   5225  CG1 ILE B 123      72.141  -0.182   6.219  1.00 76.51           C
ANISOU 5225  CG1 ILE B 123     9578   9568   9925   3131   1740  -1833       C
ATOM   5226  CG2 ILE B 123      71.568   1.961   7.359  1.00 64.53           C
ANISOU 5226  CG2 ILE B 123     8005   8185   8328   2847   1632  -1534       C
ATOM   5227  CD1 ILE B 123      71.344  -1.051   7.118  1.00 72.48           C
ANISOU 5227  CD1 ILE B 123     9229   8805   9504   3144   1599  -1801       C
ATOM   5228  N   ASN B 124      73.215   4.089   5.510  1.00 63.56           N
ANISOU 5228  N   ASN B 124     7531   8587   8031   2759   1933  -1533       N
ATOM   5229  CA  ASN B 124      73.189   5.525   5.761  1.00 64.07           C
ANISOU 5229  CA  ASN B 124     7516   8778   8050   2596   1927  -1384       C
ATOM   5230  C   ASN B 124      71.793   6.041   5.435  1.00 63.40           C
ANISOU 5230  C   ASN B 124     7602   8666   7820   2431   1900  -1340       C
ATOM   5231  O   ASN B 124      71.422   6.129   4.261  1.00 64.50           O
ANISOU 5231  O   ASN B 124     7795   8893   7818   2394   2001  -1408       O
ATOM   5232  CB  ASN B 124      74.268   6.232   4.948  1.00 66.27           C
ANISOU 5232  CB  ASN B 124     7600   9284   8295   2599   2080  -1393       C
ATOM   5233  CG  ASN B 124      74.332   7.710   5.230  1.00 65.48           C
ANISOU 5233  CG  ASN B 124     7407   9300   8172   2434   2075  -1238       C
ATOM   5234  OD1 ASN B 124      73.451   8.276   5.891  1.00 62.78           O
ANISOU 5234  OD1 ASN B 124     7161   8879   7813   2307   1968  -1134       O
ATOM   5235  ND2 ASN B 124      75.418   8.337   4.791  1.00 60.76           N
ANISOU 5235  ND2 ASN B 124     6613   8885   7588   2436   2190  -1223       N
ATOM   5236  N   LEU B 125      71.021   6.378   6.473  1.00 61.23           N
ANISOU 5236  N   LEU B 125     7409   8278   7577   2336   1762  -1227       N
ATOM   5237  CA  LEU B 125      69.655   6.850   6.260  1.00 61.29           C
ANISOU 5237  CA  LEU B 125     7574   8251   7462   2185   1725  -1182       C
ATOM   5238  C   LEU B 125      69.621   8.103   5.395  1.00 61.22           C
ANISOU 5238  C   LEU B 125     7508   8428   7327   2058   1824  -1124       C
ATOM   5239  O   LEU B 125      68.709   8.278   4.574  1.00 62.97           O
ANISOU 5239  O   LEU B 125     7843   8676   7408   1978   1858  -1144       O
ATOM   5240  CB  LEU B 125      68.966   7.122   7.601  1.00 63.05           C
ANISOU 5240  CB  LEU B 125     7864   8345   7748   2106   1570  -1062       C
ATOM   5241  CG  LEU B 125      68.542   5.944   8.476  1.00 62.47           C
ANISOU 5241  CG  LEU B 125     7906   8064   7766   2188   1453  -1089       C
ATOM   5242  CD1 LEU B 125      68.142   6.443   9.860  1.00 57.86           C
ANISOU 5242  CD1 LEU B 125     7337   7407   7240   2109   1316   -952       C
ATOM   5243  CD2 LEU B 125      67.406   5.188   7.833  1.00 63.09           C
ANISOU 5243  CD2 LEU B 125     8172   8041   7760   2170   1454  -1179       C
ATOM   5244  N   PHE B 126      70.603   8.986   5.561  1.00 59.81           N
ANISOU 5244  N   PHE B 126     7149   8377   7198   2036   1870  -1047       N
ATOM   5245  CA  PHE B 126      70.602  10.230   4.802  1.00 63.74           C
ANISOU 5245  CA  PHE B 126     7587   9039   7592   1907   1963   -971       C
ATOM   5246  C   PHE B 126      70.727   9.971   3.298  1.00 66.53           C
ANISOU 5246  C   PHE B 126     7948   9523   7805   1943   2116  -1072       C
ATOM   5247  O   PHE B 126      70.282  10.799   2.493  1.00 64.90           O
ANISOU 5247  O   PHE B 126     7767   9427   7466   1831   2182  -1018       O
ATOM   5248  CB  PHE B 126      71.730  11.144   5.295  1.00 62.86           C
ANISOU 5248  CB  PHE B 126     7270   9031   7583   1881   1985   -879       C
ATOM   5249  CG  PHE B 126      71.509  11.686   6.677  1.00 59.41           C
ANISOU 5249  CG  PHE B 126     6826   8498   7250   1810   1840   -770       C
ATOM   5250  CD1 PHE B 126      71.808  10.916   7.787  1.00 60.90           C
ANISOU 5250  CD1 PHE B 126     7005   8569   7566   1911   1730   -790       C
ATOM   5251  CD2 PHE B 126      70.986  12.956   6.875  1.00 61.19           C
ANISOU 5251  CD2 PHE B 126     7058   8750   7444   1647   1812   -648       C
ATOM   5252  CE1 PHE B 126      71.606  11.396   9.053  1.00 56.67           C
ANISOU 5252  CE1 PHE B 126     6463   7959   7109   1848   1598   -696       C
ATOM   5253  CE2 PHE B 126      70.771  13.446   8.163  1.00 59.70           C
ANISOU 5253  CE2 PHE B 126     6863   8474   7345   1585   1679   -563       C
ATOM   5254  CZ  PHE B 126      71.076  12.666   9.249  1.00 59.88           C
ANISOU 5254  CZ  PHE B 126     6876   8396   7479   1684   1573   -589       C
ATOM   5255  N   GLU B 127      71.321   8.838   2.893  1.00 67.28           N
ANISOU 5255  N   GLU B 127     8024   9613   7925   2101   2174  -1218       N
ATOM   5256  CA  GLU B 127      71.481   8.575   1.462  1.00 68.06           C
ANISOU 5256  CA  GLU B 127     8127   9851   7882   2141   2325  -1329       C
ATOM   5257  C   GLU B 127      70.177   8.176   0.773  1.00 68.31           C
ANISOU 5257  C   GLU B 127     8363   9830   7763   2095   2306  -1397       C
ATOM   5258  O   GLU B 127      70.151   8.139  -0.455  1.00 70.19           O
ANISOU 5258  O   GLU B 127     8616  10202   7850   2100   2424  -1473       O
ATOM   5259  CB  GLU B 127      72.541   7.497   1.167  1.00 68.72           C
ANISOU 5259  CB  GLU B 127     8121   9954   8037   2332   2405  -1483       C
ATOM   5260  CG  GLU B 127      74.012   7.935   1.318  1.00 71.62           C
ANISOU 5260  CG  GLU B 127     8248  10459   8505   2386   2488  -1446       C
ATOM   5261  CD  GLU B 127      74.978   6.748   1.374  1.00 80.91           C
ANISOU 5261  CD  GLU B 127     9342  11602   9797   2593   2522  -1591       C
ATOM   5262  OE1 GLU B 127      74.490   5.600   1.436  1.00 77.30           O
ANISOU 5262  OE1 GLU B 127     9022  10988   9361   2691   2467  -1708       O
ATOM   5263  OE2 GLU B 127      76.214   6.958   1.335  1.00 83.98           O
ANISOU 5263  OE2 GLU B 127     9528  12119  10262   2658   2607  -1589       O
ATOM   5264  N   ILE B 128      69.101   7.868   1.514  1.00 65.62           N
ANISOU 5264  N   ILE B 128     8173   9307   7454   2050   2163  -1374       N
ATOM   5265  CA  ILE B 128      67.762   7.747   0.924  1.00 65.98           C
ANISOU 5265  CA  ILE B 128     8399   9316   7354   1969   2132  -1407       C
ATOM   5266  C   ILE B 128      66.745   8.762   1.404  1.00 62.49           C
ANISOU 5266  C   ILE B 128     8023   8843   6876   1804   2040  -1253       C
ATOM   5267  O   ILE B 128      65.967   9.276   0.596  1.00 58.19           O
ANISOU 5267  O   ILE B 128     7552   8380   6178   1709   2068  -1231       O
ATOM   5268  CB  ILE B 128      67.162   6.332   1.017  1.00 69.44           C
ANISOU 5268  CB  ILE B 128     8985   9576   7824   2058   2066  -1555       C
ATOM   5269  CG1 ILE B 128      67.692   5.501  -0.166  1.00 67.00           C
ANISOU 5269  CG1 ILE B 128     8665   9352   7438   2179   2194  -1742       C
ATOM   5270  CG2 ILE B 128      65.622   6.367   0.922  1.00 62.21           C
ANISOU 5270  CG2 ILE B 128     8250   8578   6809   1940   1978  -1541       C
ATOM   5271  CD1 ILE B 128      69.110   4.912  -0.075  1.00 75.41           C
ANISOU 5271  CD1 ILE B 128     9584  10443   8627   2347   2270  -1823       C
ATOM   5272  N   LEU B 129      66.757   9.085   2.694  1.00 61.41           N
ANISOU 5272  N   LEU B 129     7857   8599   6875   1773   1931  -1146       N
ATOM   5273  CA  LEU B 129      65.739   9.989   3.204  1.00 57.69           C
ANISOU 5273  CA  LEU B 129     7455   8086   6378   1625   1840  -1015       C
ATOM   5274  C   LEU B 129      66.283  11.403   3.273  1.00 57.42           C
ANISOU 5274  C   LEU B 129     7286   8179   6352   1533   1883   -873       C
ATOM   5275  O   LEU B 129      67.310  11.640   3.926  1.00 59.89           O
ANISOU 5275  O   LEU B 129     7458   8509   6787   1570   1886   -834       O
ATOM   5276  CB  LEU B 129      65.227   9.554   4.572  1.00 54.50           C
ANISOU 5276  CB  LEU B 129     7122   7489   6098   1627   1690   -982       C
ATOM   5277  CG  LEU B 129      64.605   8.170   4.649  1.00 52.31           C
ANISOU 5277  CG  LEU B 129     6986   7054   5835   1702   1632  -1102       C
ATOM   5278  CD1 LEU B 129      64.150   7.906   6.092  1.00 55.15           C
ANISOU 5278  CD1 LEU B 129     7399   7239   6315   1689   1489  -1034       C
ATOM   5279  CD2 LEU B 129      63.465   8.054   3.653  1.00 51.12           C
ANISOU 5279  CD2 LEU B 129     6972   6923   5527   1635   1649  -1162       C
ATOM   5280  N   PRO B 130      65.645  12.360   2.624  1.00 55.43           N
ANISOU 5280  N   PRO B 130     7067   8015   5978   1413   1914   -794       N
ATOM   5281  CA  PRO B 130      65.988  13.768   2.865  1.00 55.56           C
ANISOU 5281  CA  PRO B 130     6974   8111   6026   1307   1931   -642       C
ATOM   5282  C   PRO B 130      65.498  14.235   4.232  1.00 54.17           C
ANISOU 5282  C   PRO B 130     6818   7799   5963   1239   1791   -549       C
ATOM   5283  O   PRO B 130      64.459  14.889   4.354  1.00 55.07           O
ANISOU 5283  O   PRO B 130     7017   7875   6030   1132   1731   -472       O
ATOM   5284  CB  PRO B 130      65.279  14.505   1.724  1.00 54.77           C
ANISOU 5284  CB  PRO B 130     6932   8123   5755   1210   1995   -589       C
ATOM   5285  CG  PRO B 130      64.887  13.442   0.735  1.00 59.11           C
ANISOU 5285  CG  PRO B 130     7586   8699   6173   1284   2040   -734       C
ATOM   5286  CD  PRO B 130      64.687  12.199   1.524  1.00 54.69           C
ANISOU 5286  CD  PRO B 130     7100   7969   5710   1376   1946   -844       C
ATOM   5287  N   LEU B 131      66.257  13.889   5.268  1.00 55.22           N
ANISOU 5287  N   LEU B 131     6870   7867   6243   1306   1738   -560       N
ATOM   5288  CA  LEU B 131      65.893  14.190   6.645  1.00 57.67           C
ANISOU 5288  CA  LEU B 131     7197   8056   6659   1260   1604   -489       C
ATOM   5289  C   LEU B 131      66.083  15.677   6.936  1.00 53.70           C
ANISOU 5289  C   LEU B 131     6598   7614   6191   1138   1605   -359       C
ATOM   5290  O   LEU B 131      66.956  16.327   6.359  1.00 55.15           O
ANISOU 5290  O   LEU B 131     6652   7924   6377   1119   1706   -325       O
ATOM   5291  CB  LEU B 131      66.741  13.352   7.609  1.00 54.16           C
ANISOU 5291  CB  LEU B 131     6686   7542   6352   1378   1549   -537       C
ATOM   5292  CG  LEU B 131      66.576  11.837   7.537  1.00 54.22           C
ANISOU 5292  CG  LEU B 131     6790   7451   6361   1505   1530   -659       C
ATOM   5293  CD1 LEU B 131      67.742  11.168   8.224  1.00 55.85           C
ANISOU 5293  CD1 LEU B 131     6884   7634   6703   1636   1511   -696       C
ATOM   5294  CD2 LEU B 131      65.257  11.395   8.163  1.00 58.11           C
ANISOU 5294  CD2 LEU B 131     7454   7788   6838   1465   1411   -653       C
ATOM   5295  N   TYR B 132      65.244  16.217   7.818  1.00 53.26           N
ANISOU 5295  N   TYR B 132     6605   7465   6165   1052   1495   -289       N
ATOM   5296  CA  TYR B 132      65.231  17.648   8.095  1.00 51.62           C
ANISOU 5296  CA  TYR B 132     6331   7291   5992    929   1487   -174       C
ATOM   5297  C   TYR B 132      64.676  17.880   9.491  1.00 50.52           C
ANISOU 5297  C   TYR B 132     6230   7032   5933    887   1348   -136       C
ATOM   5298  O   TYR B 132      64.115  16.978  10.122  1.00 46.13           O
ANISOU 5298  O   TYR B 132     5773   6373   5382    938   1263   -184       O
ATOM   5299  CB  TYR B 132      64.406  18.413   7.065  1.00 49.07           C
ANISOU 5299  CB  TYR B 132     6076   7023   5547    833   1543   -114       C
ATOM   5300  CG  TYR B 132      62.964  17.987   7.028  1.00 49.31           C
ANISOU 5300  CG  TYR B 132     6281   6966   5490    813   1471   -136       C
ATOM   5301  CD1 TYR B 132      62.565  16.874   6.306  1.00 50.72           C
ANISOU 5301  CD1 TYR B 132     6559   7142   5572    885   1496   -234       C
ATOM   5302  CD2 TYR B 132      62.004  18.689   7.733  1.00 42.28           C
ANISOU 5302  CD2 TYR B 132     5450   5994   4620    723   1378    -65       C
ATOM   5303  CE1 TYR B 132      61.246  16.484   6.281  1.00 50.97           C
ANISOU 5303  CE1 TYR B 132     6741   7095   5532    858   1428   -257       C
ATOM   5304  CE2 TYR B 132      60.691  18.302   7.721  1.00 45.73           C
ANISOU 5304  CE2 TYR B 132     6033   6358   4983    702   1314    -85       C
ATOM   5305  CZ  TYR B 132      60.313  17.202   6.996  1.00 46.84           C
ANISOU 5305  CZ  TYR B 132     6267   6499   5032    766   1337   -178       C
ATOM   5306  OH  TYR B 132      58.996  16.818   6.987  1.00 47.55           O
ANISOU 5306  OH  TYR B 132     6494   6517   5055    737   1270   -200       O
ATOM   5307  N   ARG B 133      64.846  19.104   9.977  1.00 52.57           N
ANISOU 5307  N   ARG B 133     6410   7305   6257    791   1326    -51       N
ATOM   5308  CA  ARG B 133      64.258  19.510  11.251  1.00 49.83           C
ANISOU 5308  CA  ARG B 133     6099   6861   5973    737   1201    -16       C
ATOM   5309  C   ARG B 133      62.816  19.972  11.051  1.00 47.20           C
ANISOU 5309  C   ARG B 133     5901   6473   5559    651   1168     26       C
ATOM   5310  O   ARG B 133      62.565  20.942  10.331  1.00 48.59           O
ANISOU 5310  O   ARG B 133     6067   6697   5697    568   1224     92       O
ATOM   5311  CB  ARG B 133      65.079  20.615  11.908  1.00 47.43           C
ANISOU 5311  CB  ARG B 133     5648   6589   5783    672   1187     40       C
ATOM   5312  CG  ARG B 133      64.739  20.812  13.359  1.00 45.66           C
ANISOU 5312  CG  ARG B 133     5441   6279   5630    646   1055     47       C
ATOM   5313  CD  ARG B 133      65.762  21.688  14.045  1.00 48.84           C
ANISOU 5313  CD  ARG B 133     5683   6722   6154    603   1035     73       C
ATOM   5314  NE  ARG B 133      66.456  20.890  15.038  1.00 52.40           N
ANISOU 5314  NE  ARG B 133     6079   7162   6669    696    960     22       N
ATOM   5315  CZ  ARG B 133      67.754  20.631  15.040  1.00 49.99           C
ANISOU 5315  CZ  ARG B 133     5628   6931   6434    760    992     -4       C
ATOM   5316  NH1 ARG B 133      68.565  21.157  14.146  1.00 54.05           N
ANISOU 5316  NH1 ARG B 133     6024   7542   6972    733   1104     14       N
ATOM   5317  NH2 ARG B 133      68.253  19.859  15.997  1.00 49.79           N
ANISOU 5317  NH2 ARG B 133     5569   6888   6461    852    907    -43       N
ATOM   5318  N   ILE B 134      61.884  19.309  11.736  1.00 45.83           N
ANISOU 5318  N   ILE B 134     5846   6200   5366    669   1075     -4       N
ATOM   5319  CA  ILE B 134      60.471  19.659  11.641  1.00 42.67           C
ANISOU 5319  CA  ILE B 134     5568   5747   4896    595   1034     28       C
ATOM   5320  C   ILE B 134      60.157  20.934  12.424  1.00 44.91           C
ANISOU 5320  C   ILE B 134     5818   6002   5243    496    978    101       C
ATOM   5321  O   ILE B 134      59.516  21.848  11.902  1.00 47.59           O
ANISOU 5321  O   ILE B 134     6182   6354   5547    416   1000    161       O
ATOM   5322  CB  ILE B 134      59.618  18.478  12.126  1.00 40.20           C
ANISOU 5322  CB  ILE B 134     5385   5340   4550    644    960    -30       C
ATOM   5323  CG1 ILE B 134      59.918  17.229  11.297  1.00 41.62           C
ANISOU 5323  CG1 ILE B 134     5602   5535   4677    741   1017   -114       C
ATOM   5324  CG2 ILE B 134      58.145  18.841  12.071  1.00 43.66           C
ANISOU 5324  CG2 ILE B 134     5936   5731   4923    566    916      1       C
ATOM   5325  CD1 ILE B 134      59.244  15.969  11.843  1.00 40.50           C
ANISOU 5325  CD1 ILE B 134     5577   5283   4529    795    944   -173       C
ATOM   5326  N   ASN B 135      60.552  21.010  13.702  1.00 46.45           N
ANISOU 5326  N   ASN B 135     5961   6156   5530    503    900     95       N
ATOM   5327  CA  ASN B 135      60.281  22.191  14.523  1.00 43.37           C
ANISOU 5327  CA  ASN B 135     5537   5736   5204    413    842    144       C
ATOM   5328  C   ASN B 135      61.561  22.654  15.194  1.00 47.94           C
ANISOU 5328  C   ASN B 135     5967   6353   5896    414    832    143       C
ATOM   5329  O   ASN B 135      62.392  21.841  15.603  1.00 42.90           O
ANISOU 5329  O   ASN B 135     5277   5732   5291    498    816     99       O
ATOM   5330  CB  ASN B 135      59.211  21.940  15.583  1.00 39.68           C
ANISOU 5330  CB  ASN B 135     5170   5183   4725    401    737    131       C
ATOM   5331  CG  ASN B 135      57.808  22.134  15.043  1.00 41.17           C
ANISOU 5331  CG  ASN B 135     5476   5336   4830    351    738    154       C
ATOM   5332  OD1 ASN B 135      57.413  23.257  14.698  1.00 44.62           O
ANISOU 5332  OD1 ASN B 135     5901   5780   5274    273    757    209       O
ATOM   5333  ND2 ASN B 135      57.045  21.048  14.951  1.00 37.80           N
ANISOU 5333  ND2 ASN B 135     5160   4869   4332    393    715    116       N
ATOM   5334  N   GLU B 136      61.689  23.977  15.350  1.00 46.86           N
ANISOU 5334  N   GLU B 136     5759   6221   5824    321    834    192       N
ATOM   5335  CA  GLU B 136      63.002  24.550  15.626  1.00 46.68           C
ANISOU 5335  CA  GLU B 136     5576   6253   5908    304    852    196       C
ATOM   5336  C   GLU B 136      63.624  24.015  16.907  1.00 46.12           C
ANISOU 5336  C   GLU B 136     5449   6175   5898    362    759    142       C
ATOM   5337  O   GLU B 136      64.853  23.898  16.974  1.00 49.64           O
ANISOU 5337  O   GLU B 136     5765   6685   6411    398    780    124       O
ATOM   5338  CB  GLU B 136      62.927  26.075  15.649  1.00 49.35           C
ANISOU 5338  CB  GLU B 136     5859   6575   6318    185    860    254       C
ATOM   5339  CG  GLU B 136      62.492  26.635  16.970  1.00 57.61           C
ANISOU 5339  CG  GLU B 136     6914   7552   7422    139    749    233       C
ATOM   5340  CD  GLU B 136      63.093  27.992  17.271  1.00 62.49           C
ANISOU 5340  CD  GLU B 136     7412   8167   8162     42    748    257       C
ATOM   5341  OE1 GLU B 136      63.326  28.775  16.306  1.00 60.58           O
ANISOU 5341  OE1 GLU B 136     7125   7944   7947    -20    837    323       O
ATOM   5342  OE2 GLU B 136      63.288  28.274  18.482  1.00 61.67           O
ANISOU 5342  OE2 GLU B 136     7265   8041   8125     24    657    211       O
ATOM   5343  N   GLN B 137      62.825  23.637  17.911  1.00 48.47           N
ANISOU 5343  N   GLN B 137     5840   6407   6170    376    659    118       N
ATOM   5344  CA  GLN B 137      63.385  23.134  19.165  1.00 46.11           C
ANISOU 5344  CA  GLN B 137     5495   6111   5915    431    565     78       C
ATOM   5345  C   GLN B 137      63.463  21.610  19.239  1.00 46.85           C
ANISOU 5345  C   GLN B 137     5648   6192   5960    553    548     46       C
ATOM   5346  O   GLN B 137      63.806  21.076  20.302  1.00 47.75           O
ANISOU 5346  O   GLN B 137     5744   6301   6098    609    462     25       O
ATOM   5347  CB  GLN B 137      62.602  23.668  20.365  1.00 46.98           C
ANISOU 5347  CB  GLN B 137     5654   6167   6029    374    462     73       C
ATOM   5348  CG  GLN B 137      62.740  25.173  20.513  1.00 50.70           C
ANISOU 5348  CG  GLN B 137     6044   6641   6578    263    464     88       C
ATOM   5349  CD  GLN B 137      64.179  25.616  20.744  1.00 50.49           C
ANISOU 5349  CD  GLN B 137     5843   6683   6658    254    465     72       C
ATOM   5350  OE1 GLN B 137      64.847  25.127  21.644  1.00 52.14           O
ANISOU 5350  OE1 GLN B 137     5992   6925   6892    310    393     34       O
ATOM   5351  NE2 GLN B 137      64.657  26.551  19.928  1.00 54.08           N
ANISOU 5351  NE2 GLN B 137     6212   7161   7174    183    547    107       N
ATOM   5352  N   ASP B 138      63.169  20.899  18.149  1.00 45.10           N
ANISOU 5352  N   ASP B 138     5499   5966   5673    597    624     41       N
ATOM   5353  CA  ASP B 138      63.286  19.449  18.157  1.00 42.93           C
ANISOU 5353  CA  ASP B 138     5280   5665   5368    715    613      4       C
ATOM   5354  C   ASP B 138      64.711  19.019  18.522  1.00 47.68           C
ANISOU 5354  C   ASP B 138     5744   6322   6049    803    604    -21       C
ATOM   5355  O   ASP B 138      65.678  19.753  18.322  1.00 49.03           O
ANISOU 5355  O   ASP B 138     5773   6571   6287    777    644    -15       O
ATOM   5356  CB  ASP B 138      62.924  18.875  16.793  1.00 41.83           C
ANISOU 5356  CB  ASP B 138     5215   5526   5154    744    710    -14       C
ATOM   5357  CG  ASP B 138      61.442  18.948  16.484  1.00 43.59           C
ANISOU 5357  CG  ASP B 138     5586   5687   5289    682    702      2       C
ATOM   5358  OD1 ASP B 138      60.612  19.371  17.327  1.00 43.50           O
ANISOU 5358  OD1 ASP B 138     5628   5626   5274    621    626     26       O
ATOM   5359  OD2 ASP B 138      61.115  18.635  15.318  1.00 44.98           O
ANISOU 5359  OD2 ASP B 138     5816   5877   5396    691    778    -13       O
ATOM   5360  N   GLY B 139      64.836  17.809  19.076  1.00 46.86           N
ANISOU 5360  N   GLY B 139     5683   6177   5946    910    548    -46       N
ATOM   5361  CA  GLY B 139      66.147  17.279  19.403  1.00 44.24           C
ANISOU 5361  CA  GLY B 139     5226   5894   5689   1013    533    -68       C
ATOM   5362  C   GLY B 139      66.997  16.947  18.193  1.00 47.15           C
ANISOU 5362  C   GLY B 139     5516   6323   6074   1077    650   -102       C
ATOM   5363  O   GLY B 139      68.224  16.983  18.268  1.00 50.36           O
ANISOU 5363  O   GLY B 139     5770   6806   6558   1129    664   -117       O
ATOM   5364  N   GLY B 140      66.371  16.588  17.086  1.00 49.01           N
ANISOU 5364  N   GLY B 140     5851   6535   6235   1078    734   -122       N
ATOM   5365  CA  GLY B 140      67.093  16.159  15.909  1.00 47.18           C
ANISOU 5365  CA  GLY B 140     5561   6365   5999   1147    850   -166       C
ATOM   5366  C   GLY B 140      66.182  16.103  14.698  1.00 49.80           C
ANISOU 5366  C   GLY B 140     6012   6685   6225   1108    935   -179       C
ATOM   5367  O   GLY B 140      65.106  16.704  14.667  1.00 44.01           O
ANISOU 5367  O   GLY B 140     5373   5916   5432   1007    915   -141       O
ATOM   5368  N   PHE B 141      66.636  15.392  13.675  1.00 46.07           N
ANISOU 5368  N   PHE B 141     5528   6251   5726   1191   1030   -238       N
ATOM   5369  CA  PHE B 141      65.802  15.184  12.501  1.00 51.16           C
ANISOU 5369  CA  PHE B 141     6289   6893   6257   1168   1105   -266       C
ATOM   5370  C   PHE B 141      64.897  13.984  12.742  1.00 49.65           C
ANISOU 5370  C   PHE B 141     6259   6576   6031   1224   1042   -314       C
ATOM   5371  O   PHE B 141      65.349  12.945  13.241  1.00 47.37           O
ANISOU 5371  O   PHE B 141     5969   6227   5801   1337   1003   -357       O
ATOM   5372  CB  PHE B 141      66.655  14.977  11.252  1.00 55.07           C
ANISOU 5372  CB  PHE B 141     6702   7496   6724   1227   1241   -318       C
ATOM   5373  CG  PHE B 141      67.700  16.030  11.054  1.00 55.45           C
ANISOU 5373  CG  PHE B 141     6575   7670   6826   1180   1309   -270       C
ATOM   5374  CD1 PHE B 141      67.448  17.357  11.404  1.00 56.69           C
ANISOU 5374  CD1 PHE B 141     6695   7843   7001   1046   1282   -180       C
ATOM   5375  CD2 PHE B 141      68.925  15.703  10.497  1.00 54.82           C
ANISOU 5375  CD2 PHE B 141     6360   7688   6782   1268   1403   -317       C
ATOM   5376  CE1 PHE B 141      68.417  18.345  11.208  1.00 58.19           C
ANISOU 5376  CE1 PHE B 141     6720   8138   7251    992   1347   -134       C
ATOM   5377  CE2 PHE B 141      69.887  16.673  10.302  1.00 61.21           C
ANISOU 5377  CE2 PHE B 141     6998   8614   7644   1215   1470   -270       C
ATOM   5378  CZ  PHE B 141      69.632  18.000  10.658  1.00 60.84           C
ANISOU 5378  CZ  PHE B 141     6920   8576   7622   1072   1441   -176       C
ATOM   5379  N   TYR B 142      63.617  14.124  12.396  1.00 47.69           N
ANISOU 5379  N   TYR B 142     6145   6282   5692   1145   1031   -303       N
ATOM   5380  CA  TYR B 142      62.626  13.154  12.821  1.00 48.22           C
ANISOU 5380  CA  TYR B 142     6363   6221   5737   1168    957   -331       C
ATOM   5381  C   TYR B 142      61.937  12.517  11.632  1.00 49.31           C
ANISOU 5381  C   TYR B 142     6612   6348   5778   1177   1018   -402       C
ATOM   5382  O   TYR B 142      61.602  13.196  10.658  1.00 48.28           O
ANISOU 5382  O   TYR B 142     6486   6298   5560   1109   1086   -393       O
ATOM   5383  CB  TYR B 142      61.570  13.782  13.739  1.00 40.04           C
ANISOU 5383  CB  TYR B 142     5395   5126   4692   1063    862   -259       C
ATOM   5384  CG  TYR B 142      61.891  13.650  15.203  1.00 44.53           C
ANISOU 5384  CG  TYR B 142     5931   5643   5347   1090    760   -221       C
ATOM   5385  CD1 TYR B 142      62.689  14.589  15.842  1.00 44.57           C
ANISOU 5385  CD1 TYR B 142     5803   5717   5416   1062    739   -175       C
ATOM   5386  CD2 TYR B 142      61.402  12.577  15.953  1.00 45.60           C
ANISOU 5386  CD2 TYR B 142     6166   5662   5496   1141    682   -232       C
ATOM   5387  CE1 TYR B 142      62.982  14.483  17.184  1.00 44.05           C
ANISOU 5387  CE1 TYR B 142     5705   5619   5414   1087    639   -145       C
ATOM   5388  CE2 TYR B 142      61.698  12.455  17.293  1.00 46.93           C
ANISOU 5388  CE2 TYR B 142     6306   5797   5729   1168    588   -188       C
ATOM   5389  CZ  TYR B 142      62.490  13.425  17.907  1.00 45.79           C
ANISOU 5389  CZ  TYR B 142     6027   5735   5634   1142    564   -147       C
ATOM   5390  OH  TYR B 142      62.812  13.334  19.243  1.00 43.34           O
ANISOU 5390  OH  TYR B 142     5684   5409   5376   1169    465   -109       O
ATOM   5391  N   ILE B 143      61.740  11.205  11.737  1.00 49.10           N
ANISOU 5391  N   ILE B 143     6672   6217   5767   1263    990   -472       N
ATOM   5392  CA  ILE B 143      60.797  10.470  10.908  1.00 46.55           C
ANISOU 5392  CA  ILE B 143     6484   5842   5360   1258   1010   -546       C
ATOM   5393  C   ILE B 143      59.468  10.464  11.659  1.00 47.33           C
ANISOU 5393  C   ILE B 143     6702   5839   5444   1172    912   -498       C
ATOM   5394  O   ILE B 143      59.325   9.768  12.671  1.00 47.69           O
ANISOU 5394  O   ILE B 143     6791   5771   5558   1207    831   -485       O
ATOM   5395  CB  ILE B 143      61.307   9.050  10.626  1.00 46.85           C
ANISOU 5395  CB  ILE B 143     6551   5810   5440   1394   1033   -655       C
ATOM   5396  CG1 ILE B 143      62.593   9.105   9.817  1.00 45.85           C
ANISOU 5396  CG1 ILE B 143     6298   5803   5321   1479   1142   -709       C
ATOM   5397  CG2 ILE B 143      60.287   8.236   9.859  1.00 47.30           C
ANISOU 5397  CG2 ILE B 143     6753   5798   5420   1382   1041   -743       C
ATOM   5398  CD1 ILE B 143      63.456   7.853   9.946  1.00 49.82           C
ANISOU 5398  CD1 ILE B 143     6779   6236   5916   1637   1150   -795       C
ATOM   5399  N   SER B 144      58.491  11.239  11.173  1.00 45.08           N
ANISOU 5399  N   SER B 144     6465   5596   5069   1061    918   -467       N
ATOM   5400  CA  SER B 144      57.278  11.533  11.944  1.00 46.64           C
ANISOU 5400  CA  SER B 144     6743   5724   5256    968    831   -407       C
ATOM   5401  C   SER B 144      56.016  10.843  11.434  1.00 50.76           C
ANISOU 5401  C   SER B 144     7402   6178   5706    930    812   -461       C
ATOM   5402  O   SER B 144      54.930  11.099  11.972  1.00 46.36           O
ANISOU 5402  O   SER B 144     6908   5573   5133    847    748   -414       O
ATOM   5403  CB  SER B 144      57.023  13.043  11.984  1.00 42.29           C
ANISOU 5403  CB  SER B 144     6134   5259   4674    864    833   -318       C
ATOM   5404  OG  SER B 144      56.735  13.510  10.697  1.00 46.73           O
ANISOU 5404  OG  SER B 144     6705   5911   5139    823    906   -333       O
ATOM   5405  N   LYS B 145      56.110   9.990  10.411  1.00 48.14           N
ANISOU 5405  N   LYS B 145     7114   5844   5331    987    867   -564       N
ATOM   5406  CA  LYS B 145      54.890   9.423   9.848  1.00 48.41           C
ANISOU 5406  CA  LYS B 145     7272   5827   5294    938    848   -624       C
ATOM   5407  C   LYS B 145      55.067   7.960   9.471  1.00 51.00           C
ANISOU 5407  C   LYS B 145     7669   6062   5649   1028    861   -746       C
ATOM   5408  O   LYS B 145      54.360   7.449   8.595  1.00 51.87           O
ANISOU 5408  O   LYS B 145     7861   6161   5684   1006    875   -834       O
ATOM   5409  CB  LYS B 145      54.445  10.216   8.619  1.00 44.22           C
ANISOU 5409  CB  LYS B 145     6739   5426   4634    873    904   -630       C
ATOM   5410  CG  LYS B 145      52.944  10.210   8.357  1.00 47.13           C
ANISOU 5410  CG  LYS B 145     7210   5769   4929    778    854   -636       C
ATOM   5411  CD  LYS B 145      52.618  10.787   6.970  1.00 47.90           C
ANISOU 5411  CD  LYS B 145     7310   6004   4888    737    912   -658       C
ATOM   5412  CE  LYS B 145      51.117  10.897   6.775  1.00 46.54           C
ANISOU 5412  CE  LYS B 145     7222   5816   4645    641    851   -652       C
ATOM   5413  NZ  LYS B 145      50.780  11.312   5.386  1.00 42.99           N
ANISOU 5413  NZ  LYS B 145     6782   5502   4051    612    899   -680       N
ATOM   5414  N   ALA B 146      56.007   7.275  10.092  1.00 47.39           N
ANISOU 5414  N   ALA B 146     7176   5534   5296   1131    855   -759       N
ATOM   5415  CA  ALA B 146      56.238   5.894   9.720  1.00 50.15           C
ANISOU 5415  CA  ALA B 146     7587   5782   5686   1227    872   -879       C
ATOM   5416  C   ALA B 146      55.174   5.005  10.339  1.00 48.88           C
ANISOU 5416  C   ALA B 146     7552   5453   5567   1188    788   -884       C
ATOM   5417  O   ALA B 146      54.608   5.315  11.392  1.00 49.66           O
ANISOU 5417  O   ALA B 146     7669   5503   5698   1123    715   -781       O
ATOM   5418  CB  ALA B 146      57.623   5.437  10.161  1.00 50.68           C
ANISOU 5418  CB  ALA B 146     7568   5826   5861   1362    892   -887       C
ATOM   5419  N   SER B 147      54.883   3.910   9.658  1.00 43.75           N
ANISOU 5419  N   SER B 147     6990   4718   4916   1224    803  -1009       N
ATOM   5420  CA  SER B 147      54.109   2.819  10.233  1.00 51.54           C
ANISOU 5420  CA  SER B 147     8091   5517   5976   1210    734  -1027       C
ATOM   5421  C   SER B 147      55.112   1.765  10.689  1.00 51.44           C
ANISOU 5421  C   SER B 147     8070   5381   6094   1352    733  -1060       C
ATOM   5422  O   SER B 147      55.851   1.212   9.868  1.00 52.64           O
ANISOU 5422  O   SER B 147     8205   5541   6256   1453    799  -1179       O
ATOM   5423  CB  SER B 147      53.110   2.255   9.227  1.00 50.35           C
ANISOU 5423  CB  SER B 147     8042   5334   5753   1151    741  -1150       C
ATOM   5424  OG  SER B 147      52.203   3.268   8.814  1.00 44.67           O
ANISOU 5424  OG  SER B 147     7322   4739   4913   1028    736  -1110       O
ATOM   5425  N   VAL B 148      55.147   1.510  12.003  1.00 51.42           N
ANISOU 5425  N   VAL B 148     8076   5272   6190   1364    660   -951       N
ATOM   5426  CA  VAL B 148      56.161   0.666  12.631  1.00 51.55           C
ANISOU 5426  CA  VAL B 148     8069   5183   6336   1503    646   -943       C
ATOM   5427  C   VAL B 148      55.541  -0.692  12.933  1.00 54.25           C
ANISOU 5427  C   VAL B 148     8541   5305   6767   1516    597   -978       C
ATOM   5428  O   VAL B 148      54.460  -0.774  13.533  1.00 53.26           O
ANISOU 5428  O   VAL B 148     8496   5103   6638   1409    535   -910       O
ATOM   5429  CB  VAL B 148      56.720   1.333  13.901  1.00 53.27           C
ANISOU 5429  CB  VAL B 148     8200   5445   6597   1515    594   -791       C
ATOM   5430  CG1 VAL B 148      57.722   0.425  14.606  1.00 56.15           C
ANISOU 5430  CG1 VAL B 148     8541   5700   7095   1663    565   -771       C
ATOM   5431  CG2 VAL B 148      57.366   2.669  13.563  1.00 53.59           C
ANISOU 5431  CG2 VAL B 148     8108   5690   6564   1498    645   -764       C
ATOM   5432  N   VAL B 149      56.217  -1.760  12.512  1.00 54.77           N
ANISOU 5432  N   VAL B 149     8625   5265   6918   1645    627  -1085       N
ATOM   5433  CA  VAL B 149      55.686  -3.114  12.582  1.00 55.39           C
ANISOU 5433  CA  VAL B 149     8832   5122   7094   1663    593  -1145       C
ATOM   5434  C   VAL B 149      56.419  -3.898  13.668  1.00 60.02           C
ANISOU 5434  C   VAL B 149     9414   5560   7831   1783    541  -1060       C
ATOM   5435  O   VAL B 149      57.653  -3.970  13.674  1.00 58.99           O
ANISOU 5435  O   VAL B 149     9191   5465   7757   1925    570  -1073       O
ATOM   5436  CB  VAL B 149      55.803  -3.831  11.222  1.00 57.48           C
ANISOU 5436  CB  VAL B 149     9136   5357   7348   1720    663  -1351       C
ATOM   5437  CG1 VAL B 149      55.062  -5.162  11.255  1.00 56.99           C
ANISOU 5437  CG1 VAL B 149     9215   5055   7384   1707    623  -1421       C
ATOM   5438  CG2 VAL B 149      55.263  -2.971  10.117  1.00 54.95           C
ANISOU 5438  CG2 VAL B 149     8800   5217   6861   1619    716  -1426       C
ATOM   5439  N   THR B 150      55.651  -4.508  14.569  1.00 62.42           N
ANISOU 5439  N   THR B 150     9816   5699   8203   1727    466   -969       N
ATOM   5440  CA  THR B 150      56.174  -5.386  15.605  1.00 65.54           C
ANISOU 5440  CA  THR B 150    10232   5928   8741   1832    409   -876       C
ATOM   5441  C   THR B 150      55.291  -6.618  15.681  1.00 65.47           C
ANISOU 5441  C   THR B 150    10373   5678   8824   1794    374   -904       C
ATOM   5442  O   THR B 150      54.125  -6.584  15.286  1.00 65.85           O
ANISOU 5442  O   THR B 150    10499   5710   8813   1653    374   -947       O
ATOM   5443  CB  THR B 150      56.193  -4.707  16.976  1.00 67.23           C
ANISOU 5443  CB  THR B 150    10400   6206   8938   1793    339   -676       C
ATOM   5444  OG1 THR B 150      54.877  -4.234  17.270  1.00 69.78           O
ANISOU 5444  OG1 THR B 150    10785   6550   9176   1617    310   -614       O
ATOM   5445  CG2 THR B 150      57.148  -3.544  16.995  1.00 66.48           C
ANISOU 5445  CG2 THR B 150    10152   6330   8777   1835    365   -647       C
ATOM   5446  N   ALA B 151      55.854  -7.700  16.213  1.00 65.82           N
ANISOU 5446  N   ALA B 151    10454   5534   9022   1919    342   -873       N
ATOM   5447  CA  ALA B 151      55.129  -8.957  16.361  1.00 74.01           C
ANISOU 5447  CA  ALA B 151    11633   6313  10175   1894    308   -888       C
ATOM   5448  C   ALA B 151      55.830  -9.872  17.353  1.00 75.55           C
ANISOU 5448  C   ALA B 151    11847   6328  10530   2031    253   -773       C
ATOM   5449  O   ALA B 151      56.310  -9.409  18.382  1.00 78.96           O
ANISOU 5449  O   ALA B 151    12213   6837  10952   2065    206   -609       O
ATOM   5450  CB  ALA B 151      54.983  -9.654  15.012  1.00 76.94           C
ANISOU 5450  CB  ALA B 151    12062   6600  10572   1916    368  -1116       C
ATOM   5451  N   ASP B 157      55.749 -15.762  14.783  1.00 94.51           N
ANISOU 5451  N   ASP B 157    14623   7670  13616   2303    317  -1396       N
ATOM   5452  CA  ASP B 157      54.984 -16.819  15.431  1.00 96.45           C
ANISOU 5452  CA  ASP B 157    14957   7673  14017   2212    258  -1301       C
ATOM   5453  C   ASP B 157      53.530 -16.838  14.962  1.00 97.30           C
ANISOU 5453  C   ASP B 157    15158   7750  14063   1999    256  -1377       C
ATOM   5454  O   ASP B 157      53.040 -17.869  14.503  1.00100.46           O
ANISOU 5454  O   ASP B 157    15605   7976  14588   1944    259  -1488       O
ATOM   5455  CB  ASP B 157      55.055 -16.680  16.964  1.00 94.46           C
ANISOU 5455  CB  ASP B 157    14712   7385  13793   2219    182  -1015       C
ATOM   5456  CG  ASP B 157      54.811 -15.249  17.449  1.00100.54           C
ANISOU 5456  CG  ASP B 157    15471   8371  14358   2158    170   -896       C
ATOM   5457  OD1 ASP B 157      55.611 -14.344  17.105  1.00 93.82           O
ANISOU 5457  OD1 ASP B 157    14512   7736  13399   2242    208   -942       O
ATOM   5458  OD2 ASP B 157      53.824 -15.033  18.188  1.00100.05           O
ANISOU 5458  OD2 ASP B 157    15479   8287  14250   2008    126   -751       O
ATOM   5459  N   ASP B 158      52.859 -15.689  15.050  1.00 93.19           N
ANISOU 5459  N   ASP B 158    14656   7399  13351   1882    253  -1324       N
ATOM   5460  CA  ASP B 158      51.411 -15.622  14.887  1.00 97.43           C
ANISOU 5460  CA  ASP B 158    15276   7914  13830   1668    236  -1342       C
ATOM   5461  C   ASP B 158      51.012 -14.241  14.370  1.00 96.89           C
ANISOU 5461  C   ASP B 158    15169   8114  13531   1579    267  -1384       C
ATOM   5462  O   ASP B 158      51.780 -13.274  14.454  1.00 92.62           O
ANISOU 5462  O   ASP B 158    14513   7794  12883   1650    290  -1333       O
ATOM   5463  CB  ASP B 158      50.709 -15.958  16.217  1.00 96.72           C
ANISOU 5463  CB  ASP B 158    15244   7689  13815   1566    167  -1104       C
ATOM   5464  CG  ASP B 158      49.194 -15.848  16.135  1.00 98.84           C
ANISOU 5464  CG  ASP B 158    15584   7947  14025   1340    150  -1107       C
ATOM   5465  OD1 ASP B 158      48.616 -16.272  15.108  1.00101.92           O
ANISOU 5465  OD1 ASP B 158    15996   8301  14429   1263    172  -1302       O
ATOM   5466  OD2 ASP B 158      48.582 -15.354  17.109  1.00 98.31           O
ANISOU 5466  OD2 ASP B 158    15542   7912  13898   1239    115   -915       O
ATOM   5467  N   PHE B 159      49.788 -14.157  13.834  1.00 95.91           N
ANISOU 5467  N   PHE B 159    15099   8005  13338   1402    264  -1467       N
ATOM   5468  CA  PHE B 159      49.335 -12.944  13.167  1.00 88.06           C
ANISOU 5468  CA  PHE B 159    14033   7289  12136   1300    293  -1522       C
ATOM   5469  C   PHE B 159      48.348 -12.096  13.970  1.00 86.95           C
ANISOU 5469  C   PHE B 159    13876   7265  11897   1130    253  -1342       C
ATOM   5470  O   PHE B 159      48.058 -10.978  13.535  1.00 81.73           O
ANISOU 5470  O   PHE B 159    13145   6842  11068   1060    273  -1360       O
ATOM   5471  CB  PHE B 159      48.713 -13.279  11.822  1.00 83.71           C
ANISOU 5471  CB  PHE B 159    13533   6729  11545   1231    321  -1767       C
ATOM   5472  CG  PHE B 159      49.165 -12.379  10.726  1.00 87.31           C
ANISOU 5472  CG  PHE B 159    13901   7444  11828   1272    382  -1902       C
ATOM   5473  CD1 PHE B 159      50.514 -12.227  10.454  1.00 83.46           C
ANISOU 5473  CD1 PHE B 159    13336   7035  11340   1455    436  -1945       C
ATOM   5474  CD2 PHE B 159      48.246 -11.684   9.963  1.00 88.10           C
ANISOU 5474  CD2 PHE B 159    13991   7716  11767   1130    388  -1979       C
ATOM   5475  CE1 PHE B 159      50.942 -11.402   9.433  1.00 76.73           C
ANISOU 5475  CE1 PHE B 159    12401   6426  10326   1488    501  -2060       C
ATOM   5476  CE2 PHE B 159      48.663 -10.856   8.940  1.00 85.15           C
ANISOU 5476  CE2 PHE B 159    13540   7584  11229   1167    446  -2090       C
ATOM   5477  CZ  PHE B 159      50.016 -10.715   8.676  1.00 81.94           C
ANISOU 5477  CZ  PHE B 159    13060   7252  10821   1344    506  -2128       C
ATOM   5478  N   ASN B 160      47.801 -12.581  15.091  1.00 89.22           N
ANISOU 5478  N   ASN B 160    14225   7394  12280   1062    200  -1173       N
ATOM   5479  CA  ASN B 160      47.255 -11.634  16.055  1.00 89.14           C
ANISOU 5479  CA  ASN B 160    14169   7532  12170    955    171   -975       C
ATOM   5480  C   ASN B 160      48.303 -10.649  16.528  1.00 85.59           C
ANISOU 5480  C   ASN B 160    13606   7276  11638   1067    182   -871       C
ATOM   5481  O   ASN B 160      48.103  -9.428  16.478  1.00 89.20           O
ANISOU 5481  O   ASN B 160    13982   7966  11943   1004    193   -838       O
ATOM   5482  CB  ASN B 160      46.675 -12.319  17.298  1.00 93.78           C
ANISOU 5482  CB  ASN B 160    14832   7931  12870    885    120   -788       C
ATOM   5483  CG  ASN B 160      45.574 -11.484  17.936  1.00 99.64           C
ANISOU 5483  CG  ASN B 160    15550   8811  13497    710     99   -656       C
ATOM   5484  OD1 ASN B 160      45.573 -10.252  17.797  1.00 93.83           O
ANISOU 5484  OD1 ASN B 160    14724   8322  12607    685    114   -647       O
ATOM   5485  ND2 ASN B 160      44.767 -12.103  18.789  1.00100.44           N
ANISOU 5485  ND2 ASN B 160    15724   8759  13679    606     65   -526       N
ATOM   5486  N   LYS B 161      49.431 -11.165  16.985  1.00 86.01           N
ANISOU 5486  N   LYS B 161    13648   7236  11798   1233    176   -820       N
ATOM   5487  CA  LYS B 161      50.361 -10.399  17.797  1.00 88.86           C
ANISOU 5487  CA  LYS B 161    13910   7742  12111   1328    164   -676       C
ATOM   5488  C   LYS B 161      51.228  -9.466  16.955  1.00 84.35           C
ANISOU 5488  C   LYS B 161    13223   7394  11433   1410    218   -785       C
ATOM   5489  O   LYS B 161      52.184  -8.880  17.478  1.00 81.64           O
ANISOU 5489  O   LYS B 161    12785   7168  11066   1508    214   -696       O
ATOM   5490  CB  LYS B 161      51.198 -11.370  18.636  1.00 82.42           C
ANISOU 5490  CB  LYS B 161    13125   6734  11457   1474    127   -571       C
ATOM   5491  CG  LYS B 161      50.330 -12.061  19.704  1.00 87.15           C
ANISOU 5491  CG  LYS B 161    13826   7152  12137   1376     71   -403       C
ATOM   5492  CD  LYS B 161      50.437 -13.589  19.670  1.00 96.02           C
ANISOU 5492  CD  LYS B 161    15060   7961  13463   1446     56   -434       C
ATOM   5493  CE  LYS B 161      49.876 -14.226  20.945  1.00 96.47           C
ANISOU 5493  CE  LYS B 161    15200   7850  13604   1382     -1   -215       C
ATOM   5494  NZ  LYS B 161      49.431 -15.640  20.723  1.00 97.96           N
ANISOU 5494  NZ  LYS B 161    15486   7755  13979   1353     -8   -265       N
ATOM   5495  N   LEU B 162      50.886  -9.302  15.670  1.00 77.67           N
ANISOU 5495  N   LEU B 162    12380   6614  10515   1365    268   -972       N
ATOM   5496  CA  LEU B 162      51.508  -8.318  14.799  1.00 72.26           C
ANISOU 5496  CA  LEU B 162    11591   6161   9705   1410    327  -1067       C
ATOM   5497  C   LEU B 162      50.779  -6.988  14.938  1.00 67.53           C
ANISOU 5497  C   LEU B 162    10938   5775   8947   1267    321   -988       C
ATOM   5498  O   LEU B 162      49.553  -6.925  14.810  1.00 68.68           O
ANISOU 5498  O   LEU B 162    11141   5910   9046   1116    303   -997       O
ATOM   5499  CB  LEU B 162      51.481  -8.774  13.344  1.00 68.75           C
ANISOU 5499  CB  LEU B 162    11178   5699   9246   1432    384  -1302       C
ATOM   5500  CG  LEU B 162      52.312  -7.896  12.406  1.00 65.07           C
ANISOU 5500  CG  LEU B 162    10602   5462   8660   1504    456  -1399       C
ATOM   5501  CD1 LEU B 162      53.113  -8.739  11.424  1.00 66.74           C
ANISOU 5501  CD1 LEU B 162    10823   5599   8935   1647    514  -1595       C
ATOM   5502  CD2 LEU B 162      51.442  -6.900  11.658  1.00 69.03           C
ANISOU 5502  CD2 LEU B 162    11085   6157   8986   1360    476  -1444       C
ATOM   5503  N   ASN B 163      51.530  -5.927  15.191  1.00 63.76           N
ANISOU 5503  N   ASN B 163    10347   5487   8393   1314    336   -916       N
ATOM   5504  CA  ASN B 163      50.936  -4.631  15.464  1.00 63.15           C
ANISOU 5504  CA  ASN B 163    10214   5597   8183   1193    327   -827       C
ATOM   5505  C   ASN B 163      51.610  -3.568  14.614  1.00 56.88           C
ANISOU 5505  C   ASN B 163     9312   5022   7279   1230    388   -894       C
ATOM   5506  O   ASN B 163      52.797  -3.668  14.297  1.00 56.47           O
ANISOU 5506  O   ASN B 163     9197   4999   7260   1367    427   -945       O
ATOM   5507  CB  ASN B 163      51.039  -4.285  16.950  1.00 64.39           C
ANISOU 5507  CB  ASN B 163    10343   5761   8361   1185    270   -628       C
ATOM   5508  CG  ASN B 163      49.914  -4.896  17.752  1.00 76.57           C
ANISOU 5508  CG  ASN B 163    11985   7158   9950   1076    216   -537       C
ATOM   5509  OD1 ASN B 163      48.787  -4.393  17.750  1.00 82.39           O
ANISOU 5509  OD1 ASN B 163    12741   7954  10609    930    207   -518       O
ATOM   5510  ND2 ASN B 163      50.201  -6.012  18.414  1.00 84.01           N
ANISOU 5510  ND2 ASN B 163    12992   7905  11025   1147    183   -478       N
ATOM   5511  N   VAL B 164      50.826  -2.561  14.223  1.00 53.43           N
ANISOU 5511  N   VAL B 164     8852   4736   6714   1107    397   -893       N
ATOM   5512  CA  VAL B 164      51.318  -1.442  13.431  1.00 50.41           C
ANISOU 5512  CA  VAL B 164     8372   4564   6218   1118    454   -934       C
ATOM   5513  C   VAL B 164      50.883  -0.141  14.098  1.00 50.95           C
ANISOU 5513  C   VAL B 164     8380   4772   6206   1020    427   -799       C
ATOM   5514  O   VAL B 164      49.686   0.097  14.313  1.00 47.09           O
ANISOU 5514  O   VAL B 164     7937   4280   5674    892    392   -760       O
ATOM   5515  CB  VAL B 164      50.818  -1.506  11.971  1.00 49.18           C
ANISOU 5515  CB  VAL B 164     8250   4462   5975   1076    501  -1096       C
ATOM   5516  CG1 VAL B 164      51.533  -0.491  11.133  1.00 52.39           C
ANISOU 5516  CG1 VAL B 164     8556   5075   6275   1112    570  -1132       C
ATOM   5517  CG2 VAL B 164      51.031  -2.876  11.378  1.00 49.70           C
ANISOU 5517  CG2 VAL B 164     8393   4365   6126   1154    519  -1244       C
ATOM   5518  N   GLY B 165      51.851   0.714  14.403  1.00 47.37           N
ANISOU 5518  N   GLY B 165     7819   4444   5737   1080    445   -736       N
ATOM   5519  CA  GLY B 165      51.551   1.993  15.001  1.00 48.57           C
ANISOU 5519  CA  GLY B 165     7908   4726   5821    997    423   -623       C
ATOM   5520  C   GLY B 165      52.461   3.037  14.399  1.00 50.33           C
ANISOU 5520  C   GLY B 165     8015   5123   5984   1038    481   -639       C
ATOM   5521  O   GLY B 165      53.444   2.711  13.732  1.00 51.08           O
ANISOU 5521  O   GLY B 165     8071   5236   6102   1142    535   -718       O
ATOM   5522  N   THR B 166      52.098   4.296  14.607  1.00 46.91           N
ANISOU 5522  N   THR B 166     7528   4816   5480    951    474   -565       N
ATOM   5523  CA  THR B 166      52.963   5.418  14.259  1.00 51.16           C
ANISOU 5523  CA  THR B 166     7950   5512   5977    975    522   -549       C
ATOM   5524  C   THR B 166      53.641   5.899  15.531  1.00 48.70           C
ANISOU 5524  C   THR B 166     7562   5219   5722   1004    478   -439       C
ATOM   5525  O   THR B 166      52.974   6.229  16.513  1.00 50.10           O
ANISOU 5525  O   THR B 166     7760   5378   5898    933    419   -352       O
ATOM   5526  CB  THR B 166      52.217   6.587  13.599  1.00 51.23           C
ANISOU 5526  CB  THR B 166     7940   5648   5878    867    544   -539       C
ATOM   5527  OG1 THR B 166      51.511   6.152  12.428  1.00 52.75           O
ANISOU 5527  OG1 THR B 166     8204   5837   6004    834    574   -640       O
ATOM   5528  CG2 THR B 166      53.227   7.658  13.195  1.00 53.99           C
ANISOU 5528  CG2 THR B 166     8168   6145   6200    897    601   -519       C
ATOM   5529  N   TYR B 167      54.959   5.915  15.511  1.00 48.94           N
ANISOU 5529  N   TYR B 167     7502   5293   5800   1109    508   -449       N
ATOM   5530  CA  TYR B 167      55.754   6.389  16.625  1.00 48.41           C
ANISOU 5530  CA  TYR B 167     7347   5263   5786   1145    466   -358       C
ATOM   5531  C   TYR B 167      56.812   7.306  16.046  1.00 45.86           C
ANISOU 5531  C   TYR B 167     6892   5084   5449   1176    529   -375       C
ATOM   5532  O   TYR B 167      57.334   7.057  14.953  1.00 47.17           O
ANISOU 5532  O   TYR B 167     7035   5286   5602   1232    604   -460       O
ATOM   5533  CB  TYR B 167      56.380   5.225  17.396  1.00 50.72           C
ANISOU 5533  CB  TYR B 167     7658   5434   6177   1258    421   -342       C
ATOM   5534  CG  TYR B 167      55.365   4.160  17.744  1.00 56.77           C
ANISOU 5534  CG  TYR B 167     8564   6042   6966   1230    376   -336       C
ATOM   5535  CD1 TYR B 167      54.356   4.408  18.673  1.00 56.43           C
ANISOU 5535  CD1 TYR B 167     8575   5972   6895   1129    315   -247       C
ATOM   5536  CD2 TYR B 167      55.401   2.908  17.121  1.00 58.61           C
ANISOU 5536  CD2 TYR B 167     8872   6149   7250   1300    399   -425       C
ATOM   5537  CE1 TYR B 167      53.418   3.433  18.977  1.00 62.23           C
ANISOU 5537  CE1 TYR B 167     9430   6562   7653   1093    280   -236       C
ATOM   5538  CE2 TYR B 167      54.478   1.921  17.429  1.00 57.06           C
ANISOU 5538  CE2 TYR B 167     8801   5793   7087   1265    359   -418       C
ATOM   5539  CZ  TYR B 167      53.487   2.195  18.352  1.00 63.42           C
ANISOU 5539  CZ  TYR B 167     9653   6579   7863   1158    300   -319       C
ATOM   5540  OH  TYR B 167      52.563   1.229  18.654  1.00 74.63           O
ANISOU 5540  OH  TYR B 167    11191   7845   9318   1113    266   -305       O
ATOM   5541  N   ARG B 168      57.067   8.400  16.746  1.00 47.06           N
ANISOU 5541  N   ARG B 168     6958   5322   5599   1130    502   -296       N
ATOM   5542  CA  ARG B 168      58.053   9.354  16.282  1.00 45.95           C
ANISOU 5542  CA  ARG B 168     6687   5315   5458   1143    559   -299       C
ATOM   5543  C   ARG B 168      59.437   8.737  16.385  1.00 42.70           C
ANISOU 5543  C   ARG B 168     6190   4906   5129   1279    573   -327       C
ATOM   5544  O   ARG B 168      59.739   8.011  17.327  1.00 48.68           O
ANISOU 5544  O   ARG B 168     6958   5584   5954   1349    508   -297       O
ATOM   5545  CB  ARG B 168      57.968  10.651  17.092  1.00 48.98           C
ANISOU 5545  CB  ARG B 168     7002   5773   5835   1058    517   -216       C
ATOM   5546  CG  ARG B 168      58.475  10.546  18.509  1.00 45.64           C
ANISOU 5546  CG  ARG B 168     6537   5328   5477   1097    433   -155       C
ATOM   5547  CD  ARG B 168      58.131  11.804  19.260  1.00 49.89           C
ANISOU 5547  CD  ARG B 168     7033   5929   5995    997    391    -91       C
ATOM   5548  NE  ARG B 168      58.905  11.939  20.484  1.00 50.86           N
ANISOU 5548  NE  ARG B 168     7078   6075   6172   1037    321    -45       N
ATOM   5549  CZ  ARG B 168      58.406  12.407  21.618  1.00 53.23           C
ANISOU 5549  CZ  ARG B 168     7392   6378   6457    978    246      9       C
ATOM   5550  NH1 ARG B 168      57.161  12.853  21.689  1.00 54.09           N
ANISOU 5550  NH1 ARG B 168     7579   6468   6507    876    238     26       N
ATOM   5551  NH2 ARG B 168      59.169  12.419  22.709  1.00 56.35           N
ANISOU 5551  NH2 ARG B 168     7717   6801   6893   1024    178     44       N
ATOM   5552  N   ILE B 169      60.282   9.028  15.409  1.00 42.91           N
ANISOU 5552  N   ILE B 169     6127   5028   5150   1320    661   -380       N
ATOM   5553  CA  ILE B 169      61.559   8.362  15.280  1.00 47.12           C
ANISOU 5553  CA  ILE B 169     6577   5569   5759   1458    693   -426       C
ATOM   5554  C   ILE B 169      62.628   9.428  15.069  1.00 47.42           C
ANISOU 5554  C   ILE B 169     6449   5757   5811   1453    745   -406       C
ATOM   5555  O   ILE B 169      62.691  10.056  14.004  1.00 51.06           O
ANISOU 5555  O   ILE B 169     6874   6315   6211   1409    835   -435       O
ATOM   5556  CB  ILE B 169      61.510   7.328  14.149  1.00 49.09           C
ANISOU 5556  CB  ILE B 169     6894   5769   5990   1530    763   -540       C
ATOM   5557  CG1 ILE B 169      60.634   6.151  14.594  1.00 45.87           C
ANISOU 5557  CG1 ILE B 169     6636   5186   5606   1546    697   -553       C
ATOM   5558  CG2 ILE B 169      62.848   6.853  13.749  1.00 43.02           C
ANISOU 5558  CG2 ILE B 169     6020   5040   5287   1667    823   -602       C
ATOM   5559  CD1 ILE B 169      60.421   5.123  13.521  1.00 53.66           C
ANISOU 5559  CD1 ILE B 169     7706   6106   6577   1602    755   -677       C
ATOM   5560  N   GLN B 170      63.439   9.661  16.100  1.00 46.64           N
ANISOU 5560  N   GLN B 170     6249   5682   5791   1490    685   -352       N
ATOM   5561  CA  GLN B 170      64.545  10.610  16.043  1.00 47.94           C
ANISOU 5561  CA  GLN B 170     6242   5982   5991   1487    723   -333       C
ATOM   5562  C   GLN B 170      65.771   9.950  15.434  1.00 50.35           C
ANISOU 5562  C   GLN B 170     6449   6328   6355   1623    793   -403       C
ATOM   5563  O   GLN B 170      66.223   8.916  15.925  1.00 48.80           O
ANISOU 5563  O   GLN B 170     6256   6057   6229   1745    749   -422       O
ATOM   5564  CB  GLN B 170      64.911  11.124  17.437  1.00 46.71           C
ANISOU 5564  CB  GLN B 170     6012   5841   5894   1469    620   -257       C
ATOM   5565  CG  GLN B 170      65.951  12.253  17.419  1.00 50.30           C
ANISOU 5565  CG  GLN B 170     6287   6433   6390   1437    652   -238       C
ATOM   5566  CD  GLN B 170      66.356  12.737  18.819  1.00 50.60           C
ANISOU 5566  CD  GLN B 170     6246   6493   6485   1421    541   -178       C
ATOM   5567  OE1 GLN B 170      65.647  12.514  19.799  1.00 49.21           O
ANISOU 5567  OE1 GLN B 170     6161   6244   6292   1401    445   -138       O
ATOM   5568  NE2 GLN B 170      67.510  13.392  18.909  1.00 51.35           N
ANISOU 5568  NE2 GLN B 170     6168   6697   6646   1429    556   -176       N
ATOM   5569  N   VAL B 171      66.319  10.567  14.387  1.00 53.44           N
ANISOU 5569  N   VAL B 171     6747   6841   6718   1604    904   -434       N
ATOM   5570  CA  VAL B 171      67.570  10.102  13.791  1.00 54.30           C
ANISOU 5570  CA  VAL B 171     6734   7017   6879   1727    985   -501       C
ATOM   5571  C   VAL B 171      68.726  10.455  14.724  1.00 56.17           C
ANISOU 5571  C   VAL B 171     6804   7315   7224   1770    933   -455       C
ATOM   5572  O   VAL B 171      68.931  11.628  15.067  1.00 54.58           O
ANISOU 5572  O   VAL B 171     6510   7197   7030   1671    920   -393       O
ATOM   5573  CB  VAL B 171      67.767  10.703  12.392  1.00 53.35           C
ANISOU 5573  CB  VAL B 171     6563   7023   6683   1682   1126   -539       C
ATOM   5574  CG1 VAL B 171      69.131  10.347  11.839  1.00 54.66           C
ANISOU 5574  CG1 VAL B 171     6581   7282   6907   1803   1217   -604       C
ATOM   5575  CG2 VAL B 171      66.697  10.186  11.459  1.00 53.58           C
ANISOU 5575  CG2 VAL B 171     6755   6998   6604   1661   1168   -600       C
ATOM   5576  N   LYS B 172      69.461   9.428  15.163  1.00 58.00           N
ANISOU 5576  N   LYS B 172     6997   7498   7543   1920    897   -487       N
ATOM   5577  CA  LYS B 172      70.578   9.555  16.096  1.00 61.94           C
ANISOU 5577  CA  LYS B 172     7337   8049   8147   1986    832   -450       C
ATOM   5578  C   LYS B 172      71.927   9.349  15.434  1.00 64.25           C
ANISOU 5578  C   LYS B 172     7459   8446   8506   2098    925   -513       C
ATOM   5579  O   LYS B 172      72.873  10.074  15.750  1.00 67.42           O
ANISOU 5579  O   LYS B 172     7685   8965   8968   2085    923   -483       O
ATOM   5580  CB  LYS B 172      70.456   8.534  17.239  1.00 58.18           C
ANISOU 5580  CB  LYS B 172     6933   7444   7730   2084    704   -420       C
ATOM   5581  CG  LYS B 172      69.213   8.643  18.096  1.00 56.66           C
ANISOU 5581  CG  LYS B 172     6894   7152   7481   1986    602   -349       C
ATOM   5582  CD  LYS B 172      69.102   9.990  18.779  1.00 56.18           C
ANISOU 5582  CD  LYS B 172     6768   7179   7398   1849    551   -279       C
ATOM   5583  CE  LYS B 172      68.059   9.960  19.897  1.00 54.58           C
ANISOU 5583  CE  LYS B 172     6697   6886   7156   1785    434   -208       C
ATOM   5584  NZ  LYS B 172      68.569   9.335  21.142  1.00 56.56           N
ANISOU 5584  NZ  LYS B 172     6917   7103   7469   1882    316   -160       N
ATOM   5585  N   ASP B 173      72.037   8.375  14.532  1.00 65.12           N
ANISOU 5585  N   ASP B 173     7613   8521   8611   2208   1008   -605       N
ATOM   5586  CA  ASP B 173      73.249   8.161  13.754  1.00 64.19           C
ANISOU 5586  CA  ASP B 173     7336   8510   8543   2317   1118   -680       C
ATOM   5587  C   ASP B 173      72.842   7.759  12.341  1.00 64.45           C
ANISOU 5587  C   ASP B 173     7456   8547   8484   2328   1250   -779       C
ATOM   5588  O   ASP B 173      71.657   7.554  12.055  1.00 61.51           O
ANISOU 5588  O   ASP B 173     7264   8084   8023   2263   1240   -789       O
ATOM   5589  CB  ASP B 173      74.152   7.109  14.404  1.00 65.51           C
ANISOU 5589  CB  ASP B 173     7429   8624   8838   2503   1057   -705       C
ATOM   5590  CG  ASP B 173      75.613   7.366  14.120  1.00 68.92           C
ANISOU 5590  CG  ASP B 173     7626   9211   9350   2583   1129   -736       C
ATOM   5591  OD1 ASP B 173      75.893   8.216  13.241  1.00 69.57           O
ANISOU 5591  OD1 ASP B 173     7619   9434   9382   2499   1249   -752       O
ATOM   5592  OD2 ASP B 173      76.478   6.748  14.780  1.00 72.46           O
ANISOU 5592  OD2 ASP B 173     7973   9644   9913   2725   1066   -737       O
ATOM   5593  N   ARG B 174      73.833   7.633  11.449  1.00 60.75           N
ANISOU 5593  N   ARG B 174     6855   8195   8034   2413   1376   -856       N
ATOM   5594  CA  ARG B 174      73.515   7.297  10.064  1.00 60.57           C
ANISOU 5594  CA  ARG B 174     6903   8202   7908   2426   1509   -959       C
ATOM   5595  C   ARG B 174      72.708   6.001   9.979  1.00 63.30           C
ANISOU 5595  C   ARG B 174     7440   8368   8243   2508   1469  -1040       C
ATOM   5596  O   ARG B 174      71.877   5.859   9.075  1.00 61.84           O
ANISOU 5596  O   ARG B 174     7385   8168   7944   2458   1529  -1100       O
ATOM   5597  CB  ARG B 174      74.807   7.209   9.221  1.00 63.06           C
ANISOU 5597  CB  ARG B 174     7035   8670   8255   2530   1649  -1039       C
ATOM   5598  CG  ARG B 174      75.704   6.022   9.547  1.00 66.74           C
ANISOU 5598  CG  ARG B 174     7430   9075   8854   2739   1629  -1117       C
ATOM   5599  CD  ARG B 174      77.174   6.233   9.151  1.00 67.19           C
ANISOU 5599  CD  ARG B 174     7244   9306   8980   2827   1736  -1155       C
ATOM   5600  NE  ARG B 174      77.355   6.355   7.709  1.00 69.68           N
ANISOU 5600  NE  ARG B 174     7529   9755   9190   2822   1915  -1247       N
ATOM   5601  CZ  ARG B 174      78.144   5.586   6.965  1.00 75.27           C
ANISOU 5601  CZ  ARG B 174     8156  10518   9926   2980   2026  -1376       C
ATOM   5602  NH1 ARG B 174      78.867   4.609   7.496  1.00 73.57           N
ANISOU 5602  NH1 ARG B 174     7874  10225   9853   3165   1978  -1431       N
ATOM   5603  NH2 ARG B 174      78.215   5.806   5.653  1.00 71.20           N
ANISOU 5603  NH2 ARG B 174     7623  10142   9288   2955   2191  -1450       N
ATOM   5604  N   ASP B 175      72.859   5.096  10.959  1.00 65.33           N
ANISOU 5604  N   ASP B 175     7724   8482   8615   2621   1358  -1031       N
ATOM   5605  CA  ASP B 175      72.133   3.829  10.975  1.00 62.86           C
ANISOU 5605  CA  ASP B 175     7591   7978   8317   2698   1313  -1098       C
ATOM   5606  C   ASP B 175      71.427   3.558  12.303  1.00 64.81           C
ANISOU 5606  C   ASP B 175     7948   8065   8612   2667   1152   -994       C
ATOM   5607  O   ASP B 175      71.126   2.395  12.603  1.00 62.09           O
ANISOU 5607  O   ASP B 175     7715   7548   8329   2763   1096  -1028       O
ATOM   5608  CB  ASP B 175      73.084   2.675  10.629  1.00 69.06           C
ANISOU 5608  CB  ASP B 175     8310   8725   9203   2907   1364  -1215       C
ATOM   5609  CG  ASP B 175      74.265   2.590  11.578  1.00 68.04           C
ANISOU 5609  CG  ASP B 175     8011   8621   9219   3023   1300  -1158       C
ATOM   5610  OD1 ASP B 175      74.392   3.478  12.449  1.00 74.22           O
ANISOU 5610  OD1 ASP B 175     8719   9468  10014   2934   1223  -1035       O
ATOM   5611  OD2 ASP B 175      75.073   1.652  11.448  1.00 76.12           O
ANISOU 5611  OD2 ASP B 175     8972   9606  10346   3205   1326  -1240       O
ATOM   5612  N   ARG B 176      71.118   4.601  13.087  1.00 63.29           N
ANISOU 5612  N   ARG B 176     7733   7924   8392   2533   1079   -871       N
ATOM   5613  CA  ARG B 176      70.498   4.437  14.398  1.00 59.03           C
ANISOU 5613  CA  ARG B 176     7284   7260   7885   2499    930   -767       C
ATOM   5614  C   ARG B 176      69.406   5.476  14.607  1.00 59.41           C
ANISOU 5614  C   ARG B 176     7412   7333   7828   2305    898   -689       C
ATOM   5615  O   ARG B 176      69.541   6.625  14.179  1.00 59.10           O
ANISOU 5615  O   ARG B 176     7289   7436   7730   2202    957   -669       O
ATOM   5616  CB  ARG B 176      71.533   4.559  15.510  1.00 64.24           C
ANISOU 5616  CB  ARG B 176     7793   7961   8653   2576    844   -692       C
ATOM   5617  CG  ARG B 176      72.043   3.223  16.007  1.00 70.24           C
ANISOU 5617  CG  ARG B 176     8563   8591   9532   2763    785   -711       C
ATOM   5618  CD  ARG B 176      72.874   3.365  17.277  1.00 68.21           C
ANISOU 5618  CD  ARG B 176     8179   8370   9366   2824    670   -614       C
ATOM   5619  NE  ARG B 176      73.962   4.320  17.114  1.00 74.91           N
ANISOU 5619  NE  ARG B 176     8810   9415  10236   2812    719   -616       N
ATOM   5620  CZ  ARG B 176      73.984   5.527  17.659  1.00 71.77           C
ANISOU 5620  CZ  ARG B 176     8334   9131   9803   2680    677   -539       C
ATOM   5621  NH1 ARG B 176      72.991   5.961  18.416  1.00 67.11           N
ANISOU 5621  NH1 ARG B 176     7862   8488   9148   2553    588   -457       N
ATOM   5622  NH2 ARG B 176      75.034   6.315  17.444  1.00 71.45           N
ANISOU 5622  NH2 ARG B 176     8089   9259   9798   2673    728   -549       N
ATOM   5623  N   VAL B 177      68.325   5.076  15.276  1.00 56.13           N
ANISOU 5623  N   VAL B 177     7156   6777   7393   2256    805   -641       N
ATOM   5624  CA  VAL B 177      67.227   5.986  15.581  1.00 55.92           C
ANISOU 5624  CA  VAL B 177     7209   6762   7275   2083    765   -567       C
ATOM   5625  C   VAL B 177      66.729   5.744  17.003  1.00 55.94           C
ANISOU 5625  C   VAL B 177     7282   6661   7310   2066    627   -468       C
ATOM   5626  O   VAL B 177      66.975   4.700  17.606  1.00 58.26           O
ANISOU 5626  O   VAL B 177     7610   6844   7684   2181    565   -457       O
ATOM   5627  CB  VAL B 177      66.049   5.852  14.585  1.00 52.22           C
ANISOU 5627  CB  VAL B 177     6891   6248   6703   2000    824   -628       C
ATOM   5628  CG1 VAL B 177      66.487   6.162  13.150  1.00 52.38           C
ANISOU 5628  CG1 VAL B 177     6846   6391   6664   2007    964   -720       C
ATOM   5629  CG2 VAL B 177      65.429   4.473  14.677  1.00 58.44           C
ANISOU 5629  CG2 VAL B 177     7831   6851   7523   2068    785   -673       C
ATOM   5630  N   GLY B 178      66.022   6.741  17.537  1.00 53.52           N
ANISOU 5630  N   GLY B 178     6999   6396   6941   1923    581   -391       N
ATOM   5631  CA  GLY B 178      65.326   6.612  18.796  1.00 56.83           C
ANISOU 5631  CA  GLY B 178     7502   6731   7359   1881    462   -301       C
ATOM   5632  C   GLY B 178      63.841   6.367  18.590  1.00 50.23           C
ANISOU 5632  C   GLY B 178     6844   5794   6448   1784    458   -302       C
ATOM   5633  O   GLY B 178      63.295   6.630  17.524  1.00 51.42           O
ANISOU 5633  O   GLY B 178     7038   5967   6531   1719    537   -362       O
ATOM   5634  N   ILE B 179      63.190   5.849  19.630  1.00 51.66           N
ANISOU 5634  N   ILE B 179     7124   5868   6638   1774    363   -231       N
ATOM   5635  CA  ILE B 179      61.793   5.441  19.540  1.00 53.71           C
ANISOU 5635  CA  ILE B 179     7548   6016   6842   1690    352   -229       C
ATOM   5636  C   ILE B 179      61.197   5.362  20.944  1.00 56.31           C
ANISOU 5636  C   ILE B 179     7939   6290   7167   1647    244   -119       C
ATOM   5637  O   ILE B 179      61.900   5.102  21.925  1.00 53.99           O
ANISOU 5637  O   ILE B 179     7593   5995   6927   1726    173    -55       O
ATOM   5638  CB  ILE B 179      61.673   4.092  18.788  1.00 54.84           C
ANISOU 5638  CB  ILE B 179     7786   6022   7027   1778    391   -313       C
ATOM   5639  CG1 ILE B 179      60.257   3.914  18.236  1.00 56.70           C
ANISOU 5639  CG1 ILE B 179     8167   6184   7191   1668    411   -347       C
ATOM   5640  CG2 ILE B 179      62.093   2.922  19.676  1.00 54.99           C
ANISOU 5640  CG2 ILE B 179     7837   5910   7146   1902    317   -266       C
ATOM   5641  CD1 ILE B 179      60.153   2.806  17.186  1.00 55.99           C
ANISOU 5641  CD1 ILE B 179     8158   5990   7128   1735    470   -465       C
ATOM   5642  N   GLN B 180      59.884   5.569  21.032  1.00 60.37           N
ANISOU 5642  N   GLN B 180     8563   6766   7610   1524    232    -96       N
ATOM   5643  CA  GLN B 180      59.174   5.620  22.310  1.00 61.71           C
ANISOU 5643  CA  GLN B 180     8792   6902   7754   1463    144      5       C
ATOM   5644  C   GLN B 180      58.641   4.232  22.627  1.00 66.41           C
ANISOU 5644  C   GLN B 180     9518   7324   8390   1507    109     32       C
ATOM   5645  O   GLN B 180      57.486   3.911  22.350  1.00 70.04           O
ANISOU 5645  O   GLN B 180    10094   7703   8815   1425    122     19       O
ATOM   5646  CB  GLN B 180      58.046   6.645  22.253  1.00 66.58           C
ANISOU 5646  CB  GLN B 180     9442   7577   8278   1307    154     16       C
ATOM   5647  CG  GLN B 180      58.479   8.087  22.056  1.00 56.66           C
ANISOU 5647  CG  GLN B 180     8064   6474   6990   1252    181      5       C
ATOM   5648  CD  GLN B 180      57.662   9.077  22.891  1.00 61.18           C
ANISOU 5648  CD  GLN B 180     8645   7100   7500   1132    135     64       C
ATOM   5649  OE1 GLN B 180      58.174   9.710  23.810  1.00 64.81           O
ANISOU 5649  OE1 GLN B 180     9025   7635   7966   1131     82    108       O
ATOM   5650  NE2 GLN B 180      56.388   9.217  22.560  1.00 61.85           N
ANISOU 5650  NE2 GLN B 180     8823   7151   7526   1033    154     57       N
ATOM   5651  N   ALA B 181      59.487   3.410  23.250  1.00 68.01           N
ANISOU 5651  N   ALA B 181     9700   7468   8673   1635     60     74       N
ATOM   5652  CA  ALA B 181      59.137   2.012  23.505  1.00 71.26           C
ANISOU 5652  CA  ALA B 181    10232   7697   9147   1693     29    103       C
ATOM   5653  C   ALA B 181      57.937   1.868  24.434  1.00 75.71           C
ANISOU 5653  C   ALA B 181    10908   8198   9662   1589    -27    202       C
ATOM   5654  O   ALA B 181      57.182   0.897  24.310  1.00 77.18           O
ANISOU 5654  O   ALA B 181    11218   8230   9877   1573    -25    205       O
ATOM   5655  CB  ALA B 181      60.336   1.269  24.088  1.00 74.81           C
ANISOU 5655  CB  ALA B 181    10625   8107   9695   1858    -21    148       C
ATOM   5656  N   LEU B 182      57.758   2.794  25.385  1.00 76.54           N
ANISOU 5656  N   LEU B 182    10968   8419   9695   1517    -77    281       N
ATOM   5657  CA  LEU B 182      56.612   2.727  26.290  1.00 76.06           C
ANISOU 5657  CA  LEU B 182    11004   8320   9575   1415   -122    374       C
ATOM   5658  C   LEU B 182      55.311   3.117  25.599  1.00 77.61           C
ANISOU 5658  C   LEU B 182    11270   8509   9709   1274    -68    319       C
ATOM   5659  O   LEU B 182      54.236   2.701  26.043  1.00 82.36           O
ANISOU 5659  O   LEU B 182    11974   9035  10286   1195    -86    373       O
ATOM   5660  CB  LEU B 182      56.853   3.618  27.517  1.00 77.28           C
ANISOU 5660  CB  LEU B 182    11085   8614   9666   1389   -190    459       C
ATOM   5661  CG  LEU B 182      55.672   4.156  28.331  1.00 73.75           C
ANISOU 5661  CG  LEU B 182    10693   8208   9122   1254   -215    524       C
ATOM   5662  CD1 LEU B 182      55.063   3.033  29.160  1.00 77.43           C
ANISOU 5662  CD1 LEU B 182    11277   8547   9596   1258   -260    633       C
ATOM   5663  CD2 LEU B 182      56.090   5.310  29.216  1.00 69.47           C
ANISOU 5663  CD2 LEU B 182    10048   7833   8515   1230   -263    555       C
ATOM   5664  N   ALA B 183      55.387   3.894  24.516  1.00 75.77           N
ANISOU 5664  N   ALA B 183    10980   8358   9450   1240     -2    218       N
ATOM   5665  CA  ALA B 183      54.212   4.167  23.693  1.00 76.71           C
ANISOU 5665  CA  ALA B 183    11164   8467   9516   1123     49    158       C
ATOM   5666  C   ALA B 183      53.770   2.940  22.904  1.00 79.49           C
ANISOU 5666  C   ALA B 183    11622   8661   9918   1142     80     97       C
ATOM   5667  O   ALA B 183      52.654   2.927  22.364  1.00 81.82           O
ANISOU 5667  O   ALA B 183    11988   8925  10175   1041    106     58       O
ATOM   5668  CB  ALA B 183      54.508   5.321  22.732  1.00 66.44           C
ANISOU 5668  CB  ALA B 183     9772   7300   8173   1092    109     78       C
ATOM   5669  N   MET B 184      54.637   1.931  22.819  1.00 76.11           N
ANISOU 5669  N   MET B 184    11201   8137   9582   1272     75     82       N
ATOM   5670  CA  MET B 184      54.446   0.749  21.982  1.00 81.86           C
ANISOU 5670  CA  MET B 184    12017   8709  10376   1313    108      1       C
ATOM   5671  C   MET B 184      54.080  -0.451  22.859  1.00 87.58           C
ANISOU 5671  C   MET B 184    12847   9258  11172   1333     52     90       C
ATOM   5672  O   MET B 184      54.882  -1.362  23.063  1.00 90.28           O
ANISOU 5672  O   MET B 184    13195   9496  11611   1461     31    106       O
ATOM   5673  CB  MET B 184      55.731   0.457  21.207  1.00 78.22           C
ANISOU 5673  CB  MET B 184    11485   8257   9979   1455    151    -90       C
ATOM   5674  CG  MET B 184      55.640  -0.626  20.162  1.00 77.49           C
ANISOU 5674  CG  MET B 184    11469   8027   9948   1505    198   -209       C
ATOM   5675  SD  MET B 184      57.041  -0.567  19.013  1.00 92.66           S
ANISOU 5675  SD  MET B 184    13279  10025  11900   1647    276   -342       S
ATOM   5676  CE  MET B 184      57.861   0.944  19.508  1.00 64.39           C
ANISOU 5676  CE  MET B 184     9536   6671   8260   1638    270   -271       C
ATOM   5677  N   HIS B 185      52.861  -0.450  23.406  1.00 87.74           N
ANISOU 5677  N   HIS B 185    12945   9244  11149   1208     27    158       N
ATOM   5678  CA  HIS B 185      52.449  -1.679  24.058  1.00 95.62           C
ANISOU 5678  CA  HIS B 185    14052  10059  12222   1217    -13    237       C
ATOM   5679  C   HIS B 185      52.307  -2.792  23.025  1.00103.18           C
ANISOU 5679  C   HIS B 185    15092  10845  13269   1250     25    123       C
ATOM   5680  O   HIS B 185      52.454  -2.590  21.811  1.00100.41           O
ANISOU 5680  O   HIS B 185    14715  10531  12904   1260     83    -19       O
ATOM   5681  CB  HIS B 185      51.157  -1.552  24.867  1.00 97.10           C
ANISOU 5681  CB  HIS B 185    14306  10239  12350   1073    -40    336       C
ATOM   5682  CG  HIS B 185      51.213  -0.600  26.027  1.00 99.27           C
ANISOU 5682  CG  HIS B 185    14517  10665  12538   1041    -83    449       C
ATOM   5683  ND1 HIS B 185      50.127   0.157  26.416  1.00102.56           N
ANISOU 5683  ND1 HIS B 185    14939  11169  12859    901    -81    484       N
ATOM   5684  CD2 HIS B 185      52.227  -0.250  26.854  1.00 92.72           C
ANISOU 5684  CD2 HIS B 185    13608   9922  11700   1131   -128    522       C
ATOM   5685  CE1 HIS B 185      50.457   0.895  27.463  1.00 96.46           C
ANISOU 5685  CE1 HIS B 185    14104  10524  12024    907   -122    572       C
ATOM   5686  NE2 HIS B 185      51.731   0.678  27.739  1.00 90.42           N
ANISOU 5686  NE2 HIS B 185    13286   9764  11307   1042   -154    595       N
ATOM   5687  N   ASP B 186      51.996  -3.977  23.554  1.00112.00           N
ANISOU 5687  N   ASP B 186    16309  11769  14475   1264     -9    192       N
ATOM   5688  CA  ASP B 186      51.996  -5.275  22.888  1.00113.84           C
ANISOU 5688  CA  ASP B 186    16632  11792  14831   1318      9    110       C
ATOM   5689  C   ASP B 186      53.412  -5.818  22.722  1.00112.87           C
ANISOU 5689  C   ASP B 186    16462  11617  14807   1511      8     77       C
ATOM   5690  O   ASP B 186      53.586  -7.006  22.436  1.00122.69           O
ANISOU 5690  O   ASP B 186    17779  12662  16176   1588      9     35       O
ATOM   5691  CB  ASP B 186      51.311  -5.204  21.524  1.00116.20           C
ANISOU 5691  CB  ASP B 186    16960  12092  15098   1238     69    -62       C
ATOM   5692  CG  ASP B 186      49.804  -5.160  21.618  1.00121.72           C
ANISOU 5692  CG  ASP B 186    17733  12765  15749   1059     64    -40       C
ATOM   5693  OD1 ASP B 186      49.289  -4.308  22.375  1.00132.74           O
ANISOU 5693  OD1 ASP B 186    19097  14286  17054    968     43     64       O
ATOM   5694  OD2 ASP B 186      49.135  -5.959  20.930  1.00124.28           O
ANISOU 5694  OD2 ASP B 186    18144  12949  16128   1008     81   -133       O
ATOM   5695  N   ILE B 187      54.429  -4.993  22.960  1.00101.87           N
ANISOU 5695  N   ILE B 187    14944  10390  13370   1592      2     99       N
ATOM   5696  CA  ILE B 187      55.814  -5.452  22.926  1.00 95.59           C
ANISOU 5696  CA  ILE B 187    14085   9565  12669   1779     -4     82       C
ATOM   5697  C   ILE B 187      56.562  -5.137  24.204  1.00 90.55           C
ANISOU 5697  C   ILE B 187    13374   9008  12025   1850    -77    240       C
ATOM   5698  O   ILE B 187      57.726  -5.542  24.331  1.00 89.02           O
ANISOU 5698  O   ILE B 187    13118   8791  11915   2011    -96    247       O
ATOM   5699  CB  ILE B 187      56.598  -4.883  21.716  1.00 91.54           C
ANISOU 5699  CB  ILE B 187    13469   9179  12131   1841     69    -80       C
ATOM   5700  CG1 ILE B 187      56.708  -3.357  21.785  1.00 88.87           C
ANISOU 5700  CG1 ILE B 187    13017   9087  11663   1768     82    -63       C
ATOM   5701  CG2 ILE B 187      55.921  -5.258  20.413  1.00 90.70           C
ANISOU 5701  CG2 ILE B 187    13436   9001  12023   1785    137   -245       C
ATOM   5702  CD1 ILE B 187      57.958  -2.802  22.468  1.00 84.07           C
ANISOU 5702  CD1 ILE B 187    12274   8608  11062   1873     47      8       C
ATOM   5703  N   ALA B 188      55.960  -4.386  25.127  1.00 91.33           N
ANISOU 5703  N   ALA B 188    13468   9214  12021   1737   -117    357       N
ATOM   5704  CA  ALA B 188      56.663  -3.997  26.340  1.00 87.34           C
ANISOU 5704  CA  ALA B 188    12886   8810  11488   1797   -189    495       C
ATOM   5705  C   ALA B 188      57.184  -5.230  27.073  1.00 89.30           C
ANISOU 5705  C   ALA B 188    13186   8890  11854   1928   -252    606       C
ATOM   5706  O   ALA B 188      58.333  -5.263  27.534  1.00 88.25           O
ANISOU 5706  O   ALA B 188    12966   8806  11760   2068   -297    654       O
ATOM   5707  CB  ALA B 188      55.736  -3.170  27.226  1.00 80.82           C
ANISOU 5707  CB  ALA B 188    12074   8098  10536   1647   -219    595       C
ATOM   5708  N   VAL B 189      56.348  -6.270  27.161  1.00 88.61           N
ANISOU 5708  N   VAL B 189    13239   8598  11830   1886   -255    649       N
ATOM   5709  CA  VAL B 189      56.723  -7.485  27.878  1.00 82.93           C
ANISOU 5709  CA  VAL B 189    12586   7695  11229   2000   -315    772       C
ATOM   5710  C   VAL B 189      57.802  -8.200  27.089  1.00 91.14           C
ANISOU 5710  C   VAL B 189    13590   8630  12408   2179   -294    664       C
ATOM   5711  O   VAL B 189      58.854  -8.590  27.614  1.00 96.20           O
ANISOU 5711  O   VAL B 189    14177   9252  13122   2340   -347    737       O
ATOM   5712  CB  VAL B 189      55.498  -8.406  28.035  1.00 83.72           C
ANISOU 5712  CB  VAL B 189    12846   7589  11375   1893   -312    832       C
ATOM   5713  CG1 VAL B 189      55.777  -9.574  28.976  1.00 82.60           C
ANISOU 5713  CG1 VAL B 189    12779   7261  11343   1991   -381   1002       C
ATOM   5714  CG2 VAL B 189      54.166  -7.670  28.180  1.00 87.09           C
ANISOU 5714  CG2 VAL B 189    13308   8110  11670   1685   -288    846       C
ATOM   5715  N   GLN B 190      57.548  -8.329  25.788  1.00 93.07           N
ANISOU 5715  N   GLN B 190    13858   8822  12684   2154   -213    481       N
ATOM   5716  CA  GLN B 190      58.494  -8.818  24.805  1.00 91.68           C
ANISOU 5716  CA  GLN B 190    13635   8584  12614   2307   -168    332       C
ATOM   5717  C   GLN B 190      59.810  -8.061  24.908  1.00 90.56           C
ANISOU 5717  C   GLN B 190    13324   8638  12446   2428   -177    324       C
ATOM   5718  O   GLN B 190      60.894  -8.649  24.807  1.00 87.72           O
ANISOU 5718  O   GLN B 190    12911   8220  12201   2607   -187    302       O
ATOM   5719  CB  GLN B 190      57.854  -8.598  23.434  1.00 94.86           C
ANISOU 5719  CB  GLN B 190    14067   8997  12978   2211    -77    136       C
ATOM   5720  CG  GLN B 190      57.661  -9.767  22.507  1.00 92.17           C
ANISOU 5720  CG  GLN B 190    13825   8433  12764   2256    -33     -1       C
ATOM   5721  CD  GLN B 190      56.570  -9.424  21.505  1.00 94.35           C
ANISOU 5721  CD  GLN B 190    14155   8738  12954   2094     30   -140       C
ATOM   5722  OE1 GLN B 190      56.378  -8.252  21.170  1.00 93.06           O
ANISOU 5722  OE1 GLN B 190    13919   8788  12651   2004     63   -178       O
ATOM   5723  NE2 GLN B 190      55.858 -10.432  21.022  1.00 91.12           N
ANISOU 5723  NE2 GLN B 190    13873   8117  12633   2056     45   -215       N
ATOM   5724  N   LEU B 191      59.727  -6.742  25.122  1.00 91.25           N
ANISOU 5724  N   LEU B 191    13323   8957  12391   2330   -175    341       N
ATOM   5725  CA  LEU B 191      60.915  -5.899  25.101  1.00 88.93           C
ANISOU 5725  CA  LEU B 191    12860   8862  12069   2418   -175    315       C
ATOM   5726  C   LEU B 191      61.838  -6.226  26.262  1.00 91.88           C
ANISOU 5726  C   LEU B 191    13175   9237  12499   2554   -271    462       C
ATOM   5727  O   LEU B 191      63.043  -6.433  26.055  1.00 90.11           O
ANISOU 5727  O   LEU B 191    12845   9035  12357   2717   -273    421       O
ATOM   5728  CB  LEU B 191      60.527  -4.421  25.149  1.00 88.43           C
ANISOU 5728  CB  LEU B 191    12725   9024  11849   2269   -158    310       C
ATOM   5729  CG  LEU B 191      61.702  -3.437  25.137  1.00 82.80           C
ANISOU 5729  CG  LEU B 191    11832   8522  11107   2334   -156    283       C
ATOM   5730  CD1 LEU B 191      62.859  -3.907  24.264  1.00 81.11           C
ANISOU 5730  CD1 LEU B 191    11533   8286  10998   2499   -105    167       C
ATOM   5731  CD2 LEU B 191      61.248  -2.089  24.679  1.00 79.85           C
ANISOU 5731  CD2 LEU B 191    11406   8326  10607   2187   -104    222       C
ATOM   5732  N   GLU B 192      61.312  -6.250  27.491  1.00 92.13           N
ANISOU 5732  N   GLU B 192    13265   9260  12480   2494   -352    634       N
ATOM   5733  CA  GLU B 192      62.219  -6.565  28.564  1.00 97.72           C
ANISOU 5733  CA  GLU B 192    13915   9982  13231   2630   -449    775       C
ATOM   5734  C   GLU B 192      62.767  -7.967  28.403  1.00 99.09           C
ANISOU 5734  C   GLU B 192    14139   9932  13579   2804   -464    784       C
ATOM   5735  O   GLU B 192      63.978  -8.173  28.487  1.00101.30           O
ANISOU 5735  O   GLU B 192    14311  10240  13939   2976   -496    784       O
ATOM   5736  CB  GLU B 192      61.546  -6.529  29.953  1.00106.22           C
ANISOU 5736  CB  GLU B 192    15063  11072  14223   2547   -535    971       C
ATOM   5737  CG  GLU B 192      62.390  -7.490  30.781  1.00113.08           C
ANISOU 5737  CG  GLU B 192    15929  11842  15195   2725   -626   1110       C
ATOM   5738  CD  GLU B 192      61.624  -8.330  31.733  1.00117.13           C
ANISOU 5738  CD  GLU B 192    16589  12202  15715   2690   -685   1292       C
ATOM   5739  OE1 GLU B 192      60.476  -8.006  32.088  1.00117.02           O
ANISOU 5739  OE1 GLU B 192    16659  12209  15595   2519   -673   1344       O
ATOM   5740  OE2 GLU B 192      62.138  -9.446  31.981  1.00126.29           O
ANISOU 5740  OE2 GLU B 192    17788  13189  17008   2840   -731   1372       O
ATOM   5741  N   LYS B 193      61.870  -8.954  28.171  1.00 99.81           N
ANISOU 5741  N   LYS B 193    14393   9792  13740   2760   -442    790       N
ATOM   5742  CA  LYS B 193      62.285 -10.349  28.083  1.00102.45           C
ANISOU 5742  CA  LYS B 193    14793   9878  14254   2918   -461    807       C
ATOM   5743  C   LYS B 193      63.542 -10.386  27.233  1.00 99.66           C
ANISOU 5743  C   LYS B 193    14311   9566  13990   3090   -419    658       C
ATOM   5744  O   LYS B 193      64.516 -11.062  27.570  1.00104.88           O
ANISOU 5744  O   LYS B 193    14924  10154  14771   3278   -470    711       O
ATOM   5745  CB  LYS B 193      61.186 -11.276  27.506  1.00108.67           C
ANISOU 5745  CB  LYS B 193    15755  10418  15116   2833   -411    754       C
ATOM   5746  CG  LYS B 193      61.218 -11.486  25.989  1.00108.69           C
ANISOU 5746  CG  LYS B 193    15761  10357  15180   2851   -308    514       C
ATOM   5747  CD  LYS B 193      61.821 -12.837  25.584  1.00111.96           C
ANISOU 5747  CD  LYS B 193    16221  10520  15798   3033   -305    458       C
ATOM   5748  CE  LYS B 193      62.682 -12.655  24.323  1.00108.22           C
ANISOU 5748  CE  LYS B 193    15640  10120  15360   3143   -219    234       C
ATOM   5749  NZ  LYS B 193      63.385 -13.885  23.854  1.00109.21           N
ANISOU 5749  NZ  LYS B 193    15785  10028  15684   3335   -206    150       N
ATOM   5750  N   ALA B 194      63.542  -9.571  26.178  1.00 96.86           N
ANISOU 5750  N   ALA B 194    13886   9351  13565   3025   -328    481       N
ATOM   5751  CA  ALA B 194      64.749  -9.324  25.404  1.00 96.75           C
ANISOU 5751  CA  ALA B 194    13720   9442  13599   3164   -278    344       C
ATOM   5752  C   ALA B 194      65.818  -8.607  26.235  1.00 95.46           C
ANISOU 5752  C   ALA B 194    13389   9483  13399   3245   -349    440       C
ATOM   5753  O   ALA B 194      66.963  -9.066  26.316  1.00 90.72           O
ANISOU 5753  O   ALA B 194    12692   8867  12909   3435   -377    442       O
ATOM   5754  CB  ALA B 194      64.380  -8.517  24.161  1.00 89.70           C
ANISOU 5754  CB  ALA B 194    12798   8670  12612   3048   -165    159       C
ATOM   5755  N   GLU B 195      65.464  -7.478  26.869  1.00 98.15           N
ANISOU 5755  N   GLU B 195    13688  10016  13589   3105   -382    516       N
ATOM   5756  CA  GLU B 195      66.474  -6.690  27.580  1.00 92.20           C
ANISOU 5756  CA  GLU B 195    12765   9473  12795   3165   -446    582       C
ATOM   5757  C   GLU B 195      67.024  -7.428  28.792  1.00 97.16           C
ANISOU 5757  C   GLU B 195    13392  10032  13491   3303   -570    759       C
ATOM   5758  O   GLU B 195      68.222  -7.335  29.088  1.00 95.55           O
ANISOU 5758  O   GLU B 195    13039   9928  13336   3447   -619    777       O
ATOM   5759  CB  GLU B 195      65.918  -5.333  28.010  1.00 90.56           C
ANISOU 5759  CB  GLU B 195    12522   9471  12415   2981   -456    615       C
ATOM   5760  CG  GLU B 195      65.664  -4.381  26.867  1.00 86.31           C
ANISOU 5760  CG  GLU B 195    11937   9051  11806   2866   -345    453       C
ATOM   5761  CD  GLU B 195      65.433  -2.965  27.344  1.00 85.18           C
ANISOU 5761  CD  GLU B 195    11721   9125  11520   2721   -364    485       C
ATOM   5762  OE1 GLU B 195      64.322  -2.673  27.826  1.00 86.50           O
ANISOU 5762  OE1 GLU B 195    11991   9284  11591   2574   -383    550       O
ATOM   5763  OE2 GLU B 195      66.373  -2.146  27.261  1.00 85.89           O
ANISOU 5763  OE2 GLU B 195    11645   9390  11598   2754   -360    443       O
ATOM   5764  N   ALA B 196      66.169  -8.144  29.523  1.00 97.92           N
ANISOU 5764  N   ALA B 196    13648   9969  13589   3259   -624    898       N
ATOM   5765  CA  ALA B 196      66.680  -8.986  30.597  1.00 98.20           C
ANISOU 5765  CA  ALA B 196    13698   9914  13700   3403   -739   1076       C
ATOM   5766  C   ALA B 196      67.649 -10.024  30.040  1.00 97.51           C
ANISOU 5766  C   ALA B 196    13572   9671  13804   3624   -728   1015       C
ATOM   5767  O   ALA B 196      68.698 -10.297  30.633  1.00 96.84           O
ANISOU 5767  O   ALA B 196    13386   9621  13787   3794   -811   1098       O
ATOM   5768  CB  ALA B 196      65.518  -9.644  31.343  1.00100.03           C
ANISOU 5768  CB  ALA B 196    14119   9980  13907   3307   -779   1233       C
ATOM   5769  N   GLU B 197      67.341 -10.574  28.880  1.00 96.97           N
ANISOU 5769  N   GLU B 197    13575   9444  13824   3628   -627    859       N
ATOM   5770  CA  GLU B 197      68.121 -11.645  28.283  1.00 96.70           C
ANISOU 5770  CA  GLU B 197    13527   9233  13980   3833   -605    781       C
ATOM   5771  C   GLU B 197      69.180 -11.103  27.327  1.00 94.57           C
ANISOU 5771  C   GLU B 197    13075   9122  13734   3926   -529    597       C
ATOM   5772  O   GLU B 197      69.885 -11.883  26.677  1.00 96.85           O
ANISOU 5772  O   GLU B 197    13332   9294  14175   4099   -491    496       O
ATOM   5773  CB  GLU B 197      67.115 -12.611  27.631  1.00 97.28           C
ANISOU 5773  CB  GLU B 197    13791   9034  14135   3774   -542    715       C
ATOM   5774  CG  GLU B 197      67.403 -14.115  27.688  1.00104.48           C
ANISOU 5774  CG  GLU B 197    14732   9708  15257   3863   -559    749       C
ATOM   5775  CD  GLU B 197      66.224 -14.930  27.234  1.00112.56           C
ANISOU 5775  CD  GLU B 197    15932  10497  16338   3736   -507    705       C
ATOM   5776  OE1 GLU B 197      65.385 -15.187  28.132  1.00115.33           O
ANISOU 5776  OE1 GLU B 197    16393  10771  16656   3624   -567    881       O
ATOM   5777  OE2 GLU B 197      66.145 -15.283  26.017  1.00111.89           O
ANISOU 5777  OE2 GLU B 197    15867  10323  16324   3743   -409    499       O
ATOM   5778  N   ASN B 198      69.310  -9.773  27.267  1.00 93.81           N
ANISOU 5778  N   ASN B 198    12859   9292  13494   3815   -506    558       N
ATOM   5779  CA  ASN B 198      70.251  -9.074  26.396  1.00 91.76           C
ANISOU 5779  CA  ASN B 198    12417   9215  13233   3868   -427    398       C
ATOM   5780  C   ASN B 198      70.000  -9.394  24.927  1.00 95.92           C
ANISOU 5780  C   ASN B 198    12991   9650  13803   3863   -289    188       C
ATOM   5781  O   ASN B 198      70.939  -9.600  24.150  1.00 96.08           O
ANISOU 5781  O   ASN B 198    12899   9694  13911   4006   -225     57       O
ATOM   5782  CB  ASN B 198      71.700  -9.375  26.764  1.00 95.94           C
ANISOU 5782  CB  ASN B 198    12779   9797  13878   4092   -488    431       C
ATOM   5783  CG  ASN B 198      72.639  -8.341  26.222  1.00 98.20           C
ANISOU 5783  CG  ASN B 198    12852  10336  14124   4102   -430    316       C
ATOM   5784  OD1 ASN B 198      73.146  -7.504  26.960  1.00103.43           O
ANISOU 5784  OD1 ASN B 198    13384  11198  14718   4079   -501    397       O
ATOM   5785  ND2 ASN B 198      72.844  -8.356  24.905  1.00 96.96           N
ANISOU 5785  ND2 ASN B 198    12658  10180  14001   4125   -297    124       N
ATOM   5786  N   LYS B 199      68.723  -9.438  24.532  1.00 94.56           N
ANISOU 5786  N   LYS B 199    12983   9381  13564   3697   -242    152       N
ATOM   5787  CA  LYS B 199      68.472  -9.782  23.136  1.00 88.98           C
ANISOU 5787  CA  LYS B 199    12325   8592  12890   3694   -118    -53       C
ATOM   5788  C   LYS B 199      67.817  -8.672  22.328  1.00 85.98           C
ANISOU 5788  C   LYS B 199    11937   8380  12350   3502    -27   -160       C
ATOM   5789  O   LYS B 199      66.994  -7.903  22.839  1.00 83.35           O
ANISOU 5789  O   LYS B 199    11647   8132  11889   3328    -59    -72       O
ATOM   5790  CB  LYS B 199      67.626 -11.048  22.959  1.00 91.82           C
ANISOU 5790  CB  LYS B 199    12884   8653  13350   3697   -117    -67       C
ATOM   5791  CG  LYS B 199      68.320 -12.309  23.356  1.00 91.23           C
ANISOU 5791  CG  LYS B 199    12826   8370  13467   3912   -175    -15       C
ATOM   5792  CD  LYS B 199      67.356 -13.427  23.109  1.00 96.49           C
ANISOU 5792  CD  LYS B 199    13677   8761  14222   3849   -161    -38       C
ATOM   5793  CE  LYS B 199      67.923 -14.708  23.538  1.00101.31           C
ANISOU 5793  CE  LYS B 199    14272   9188  15032   3967   -210     32       C
ATOM   5794  NZ  LYS B 199      66.773 -15.636  23.655  1.00102.67           N
ANISOU 5794  NZ  LYS B 199    14627   9114  15268   3847   -221     75       N
ATOM   5795  N   PRO B 200      68.173  -8.573  21.046  1.00 82.13           N
ANISOU 5795  N   PRO B 200    11393   7947  11866   3537     89   -352       N
ATOM   5796  CA  PRO B 200      67.522  -7.584  20.188  1.00 77.61           C
ANISOU 5796  CA  PRO B 200    10823   7523  11143   3361    178   -451       C
ATOM   5797  C   PRO B 200      66.039  -7.890  20.071  1.00 75.37           C
ANISOU 5797  C   PRO B 200    10735   7095  10808   3203    176   -450       C
ATOM   5798  O   PRO B 200      65.608  -9.036  20.219  1.00 83.38           O
ANISOU 5798  O   PRO B 200    11882   7872  11924   3247    146   -440       O
ATOM   5799  CB  PRO B 200      68.239  -7.749  18.843  1.00 76.11           C
ANISOU 5799  CB  PRO B 200    10553   7377  10988   3465    300   -655       C
ATOM   5800  CG  PRO B 200      69.531  -8.443  19.154  1.00 78.03           C
ANISOU 5800  CG  PRO B 200    10685   7575  11386   3696    271   -646       C
ATOM   5801  CD  PRO B 200      69.222  -9.325  20.327  1.00 79.83           C
ANISOU 5801  CD  PRO B 200    11023   7598  11711   3744    147   -484       C
ATOM   5802  N   LEU B 201      65.252  -6.849  19.835  1.00 72.76           N
ANISOU 5802  N   LEU B 201    10416   6905  10324   3015    206   -455       N
ATOM   5803  CA  LEU B 201      63.832  -7.014  19.523  1.00 71.38           C
ANISOU 5803  CA  LEU B 201    10406   6628  10088   2855    220   -481       C
ATOM   5804  C   LEU B 201      63.600  -6.510  18.110  1.00 68.95           C
ANISOU 5804  C   LEU B 201    10082   6427   9689   2786    335   -660       C
ATOM   5805  O   LEU B 201      63.671  -5.290  17.875  1.00 67.99           O
ANISOU 5805  O   LEU B 201     9867   6520   9447   2698    370   -660       O
ATOM   5806  CB  LEU B 201      62.944  -6.270  20.519  1.00 65.64           C
ANISOU 5806  CB  LEU B 201     9720   5963   9255   2688    149   -322       C
ATOM   5807  CG  LEU B 201      61.414  -6.399  20.441  1.00 72.20           C
ANISOU 5807  CG  LEU B 201    10712   6697  10026   2512    146   -315       C
ATOM   5808  CD1 LEU B 201      60.808  -5.847  21.689  1.00 81.06           C
ANISOU 5808  CD1 LEU B 201    11855   7868  11075   2400     64   -135       C
ATOM   5809  CD2 LEU B 201      60.767  -5.674  19.271  1.00 70.43           C
ANISOU 5809  CD2 LEU B 201    10493   6585   9683   2384    234   -451       C
ATOM   5810  N   PRO B 202      63.318  -7.385  17.144  1.00 70.45           N
ANISOU 5810  N   PRO B 202    10361   6478   9928   2821    394   -813       N
ATOM   5811  CA  PRO B 202      63.192  -6.931  15.751  1.00 69.48           C
ANISOU 5811  CA  PRO B 202    10216   6476   9706   2772    504   -989       C
ATOM   5812  C   PRO B 202      61.968  -6.049  15.530  1.00 67.59           C
ANISOU 5812  C   PRO B 202    10038   6333   9312   2558    511   -970       C
ATOM   5813  O   PRO B 202      60.891  -6.297  16.079  1.00 68.20           O
ANISOU 5813  O   PRO B 202    10237   6294   9383   2446    450   -894       O
ATOM   5814  CB  PRO B 202      63.077  -8.242  14.965  1.00 72.28           C
ANISOU 5814  CB  PRO B 202    10674   6625  10163   2861    544  -1150       C
ATOM   5815  CG  PRO B 202      63.651  -9.303  15.893  1.00 70.85           C
ANISOU 5815  CG  PRO B 202    10513   6244  10164   3017    468  -1063       C
ATOM   5816  CD  PRO B 202      63.223  -8.850  17.255  1.00 70.90           C
ANISOU 5816  CD  PRO B 202    10534   6263  10140   2924    364   -840       C
ATOM   5817  N   ILE B 203      62.149  -4.998  14.723  1.00 64.96           N
ANISOU 5817  N   ILE B 203     9613   6215   8854   2501    587  -1035       N
ATOM   5818  CA  ILE B 203      61.052  -4.153  14.262  1.00 63.42           C
ANISOU 5818  CA  ILE B 203     9466   6120   8509   2316    608  -1044       C
ATOM   5819  C   ILE B 203      61.324  -3.748  12.821  1.00 62.07           C
ANISOU 5819  C   ILE B 203     9243   6096   8245   2320    722  -1203       C
ATOM   5820  O   ILE B 203      62.456  -3.806  12.334  1.00 61.96           O
ANISOU 5820  O   ILE B 203     9122   6156   8263   2450    787  -1278       O
ATOM   5821  CB  ILE B 203      60.829  -2.873  15.101  1.00 66.27           C
ANISOU 5821  CB  ILE B 203     9763   6632   8785   2199    560   -885       C
ATOM   5822  CG1 ILE B 203      61.906  -1.840  14.809  1.00 62.01           C
ANISOU 5822  CG1 ILE B 203     9052   6308   8200   2239    617   -888       C
ATOM   5823  CG2 ILE B 203      60.760  -3.173  16.593  1.00 67.36           C
ANISOU 5823  CG2 ILE B 203     9928   6665   9000   2210    451   -720       C
ATOM   5824  CD1 ILE B 203      61.671  -0.548  15.562  1.00 61.54           C
ANISOU 5824  CD1 ILE B 203     8931   6389   8062   2119    573   -752       C
ATOM   5825  N   ALA B 204      60.257  -3.350  12.134  1.00 57.33           N
ANISOU 5825  N   ALA B 204     8717   5543   7524   2176    745  -1253       N
ATOM   5826  CA  ALA B 204      60.345  -2.812  10.783  1.00 59.24           C
ANISOU 5826  CA  ALA B 204     8917   5949   7643   2152    847  -1382       C
ATOM   5827  C   ALA B 204      59.692  -1.439  10.770  1.00 55.57           C
ANISOU 5827  C   ALA B 204     8424   5655   7037   1989    844  -1290       C
ATOM   5828  O   ALA B 204      58.586  -1.268  11.292  1.00 58.39           O
ANISOU 5828  O   ALA B 204     8865   5956   7366   1864    777  -1213       O
ATOM   5829  CB  ALA B 204      59.684  -3.746   9.758  1.00 56.54           C
ANISOU 5829  CB  ALA B 204     8697   5501   7285   2147    882  -1558       C
ATOM   5830  N   ILE B 205      60.389  -0.460  10.206  1.00 54.13           N
ANISOU 5830  N   ILE B 205     8117   5675   6775   1994    919  -1295       N
ATOM   5831  CA  ILE B 205      59.909   0.914  10.115  1.00 54.02           C
ANISOU 5831  CA  ILE B 205     8062   5826   6636   1853    925  -1209       C
ATOM   5832  C   ILE B 205      59.606   1.178   8.647  1.00 55.56           C
ANISOU 5832  C   ILE B 205     8273   6141   6695   1811   1016  -1330       C
ATOM   5833  O   ILE B 205      60.514   1.154   7.805  1.00 53.54           O
ANISOU 5833  O   ILE B 205     7939   5986   6416   1900   1110  -1421       O
ATOM   5834  CB  ILE B 205      60.939   1.911  10.664  1.00 55.55           C
ANISOU 5834  CB  ILE B 205     8097   6158   6849   1879    935  -1102       C
ATOM   5835  CG1 ILE B 205      61.151   1.678  12.165  1.00 58.20           C
ANISOU 5835  CG1 ILE B 205     8423   6389   7302   1912    832   -979       C
ATOM   5836  CG2 ILE B 205      60.499   3.343  10.382  1.00 52.83           C
ANISOU 5836  CG2 ILE B 205     7710   5981   6382   1739    957  -1031       C
ATOM   5837  CD1 ILE B 205      62.498   2.183  12.721  1.00 52.03           C
ANISOU 5837  CD1 ILE B 205     7477   5707   6585   1997    836   -914       C
ATOM   5838  N   THR B 206      58.336   1.405   8.318  1.00 54.92           N
ANISOU 5838  N   THR B 206     8290   6058   6519   1679    989  -1333       N
ATOM   5839  CA  THR B 206      57.927   1.576   6.931  1.00 50.89           C
ANISOU 5839  CA  THR B 206     7810   5658   5868   1636   1061  -1448       C
ATOM   5840  C   THR B 206      57.511   3.020   6.706  1.00 51.06           C
ANISOU 5840  C   THR B 206     7782   5855   5765   1511   1073  -1346       C
ATOM   5841  O   THR B 206      56.781   3.594   7.519  1.00 51.44           O
ANISOU 5841  O   THR B 206     7850   5875   5818   1411    998  -1224       O
ATOM   5842  CB  THR B 206      56.782   0.624   6.547  1.00 48.17           C
ANISOU 5842  CB  THR B 206     7617   5179   5508   1588   1021  -1556       C
ATOM   5843  OG1 THR B 206      55.552   1.078   7.122  1.00 50.73           O
ANISOU 5843  OG1 THR B 206     8004   5470   5803   1444    939  -1453       O
ATOM   5844  CG2 THR B 206      57.069  -0.785   7.037  1.00 49.82           C
ANISOU 5844  CG2 THR B 206     7886   5171   5872   1697    988  -1624       C
ATOM   5845  N   ILE B 207      57.968   3.591   5.587  1.00 53.17           N
ANISOU 5845  N   ILE B 207     7984   6299   5918   1520   1171  -1396       N
ATOM   5846  CA  ILE B 207      57.827   5.011   5.273  1.00 55.34           C
ANISOU 5846  CA  ILE B 207     8194   6750   6084   1422   1200  -1292       C
ATOM   5847  C   ILE B 207      57.235   5.151   3.874  1.00 51.05           C
ANISOU 5847  C   ILE B 207     7699   6324   5372   1372   1257  -1382       C
ATOM   5848  O   ILE B 207      57.692   4.487   2.937  1.00 53.73           O
ANISOU 5848  O   ILE B 207     8045   6703   5667   1454   1332  -1524       O
ATOM   5849  CB  ILE B 207      59.193   5.724   5.365  1.00 54.96           C
ANISOU 5849  CB  ILE B 207     7988   6825   6071   1484   1271  -1231       C
ATOM   5850  CG1 ILE B 207      59.797   5.510   6.756  1.00 58.49           C
ANISOU 5850  CG1 ILE B 207     8384   7159   6679   1541   1204  -1152       C
ATOM   5851  CG2 ILE B 207      59.068   7.184   5.058  1.00 54.20           C
ANISOU 5851  CG2 ILE B 207     7825   6890   5878   1379   1302  -1118       C
ATOM   5852  CD1 ILE B 207      61.220   5.956   6.870  1.00 55.96           C
ANISOU 5852  CD1 ILE B 207     7904   6942   6415   1620   1267  -1120       C
ATOM   5853  N   GLY B 208      56.269   6.057   3.706  1.00 49.66           N
ANISOU 5853  N   GLY B 208     7552   6219   5098   1245   1225  -1299       N
ATOM   5854  CA  GLY B 208      55.682   6.206   2.384  1.00 50.16           C
ANISOU 5854  CA  GLY B 208     7662   6406   4992   1199   1269  -1374       C
ATOM   5855  C   GLY B 208      54.680   5.140   1.983  1.00 51.01           C
ANISOU 5855  C   GLY B 208     7902   6413   5067   1181   1220  -1512       C
ATOM   5856  O   GLY B 208      55.027   4.194   1.271  1.00 55.21           O
ANISOU 5856  O   GLY B 208     8466   6930   5580   1263   1269  -1673       O
ATOM   5857  N   ASN B 209      53.455   5.253   2.483  1.00 49.92           N
ANISOU 5857  N   ASN B 209     7837   6196   4935   1076   1123  -1455       N
ATOM   5858  CA  ASN B 209      52.500   4.156   2.506  1.00 52.10           C
ANISOU 5858  CA  ASN B 209     8233   6325   5237   1050   1055  -1564       C
ATOM   5859  C   ASN B 209      51.163   4.546   1.887  1.00 48.69           C
ANISOU 5859  C   ASN B 209     7863   5963   4673    928   1008  -1568       C
ATOM   5860  O   ASN B 209      50.830   5.725   1.764  1.00 46.09           O
ANISOU 5860  O   ASN B 209     7490   5762   4261    856   1006  -1449       O
ATOM   5861  CB  ASN B 209      52.286   3.708   3.958  1.00 46.85           C
ANISOU 5861  CB  ASN B 209     7596   5463   4741   1043    970  -1488       C
ATOM   5862  CG  ASN B 209      53.416   2.845   4.444  1.00 49.78           C
ANISOU 5862  CG  ASN B 209     7942   5724   5250   1176    997  -1534       C
ATOM   5863  OD1 ASN B 209      53.736   1.813   3.827  1.00 52.02           O
ANISOU 5863  OD1 ASN B 209     8267   5950   5547   1257   1033  -1691       O
ATOM   5864  ND2 ASN B 209      54.075   3.284   5.506  1.00 46.04           N
ANISOU 5864  ND2 ASN B 209     7393   5226   4874   1206    981  -1404       N
ATOM   5865  N   ASN B 210      50.410   3.518   1.469  1.00 52.09           N
ANISOU 5865  N   ASN B 210     8395   6307   5092    909    970  -1712       N
ATOM   5866  CA  ASN B 210      48.982   3.600   1.176  1.00 51.03           C
ANISOU 5866  CA  ASN B 210     8329   6182   4878    789    896  -1724       C
ATOM   5867  C   ASN B 210      48.334   4.455   2.267  1.00 48.93           C
ANISOU 5867  C   ASN B 210     8038   5885   4670    700    825  -1539       C
ATOM   5868  O   ASN B 210      48.533   4.187   3.452  1.00 47.84           O
ANISOU 5868  O   ASN B 210     7896   5604   4677    716    792  -1470       O
ATOM   5869  CB  ASN B 210      48.410   2.178   1.129  1.00 49.96           C
ANISOU 5869  CB  ASN B 210     8299   5875   4809    786    848  -1885       C
ATOM   5870  CG  ASN B 210      46.877   2.114   1.095  1.00 56.73           C
ANISOU 5870  CG  ASN B 210     9224   6703   5628    653    755  -1892       C
ATOM   5871  OD1 ASN B 210      46.152   3.059   1.425  1.00 57.67           O
ANISOU 5871  OD1 ASN B 210     9315   6889   5709    563    709  -1757       O
ATOM   5872  ND2 ASN B 210      46.383   0.950   0.731  1.00 60.72           N
ANISOU 5872  ND2 ASN B 210     9815   7096   6158    641    724  -2057       N
ATOM   5873  N   PRO B 211      47.562   5.487   1.917  1.00 49.52           N
ANISOU 5873  N   PRO B 211     8093   6091   4633    610    801  -1456       N
ATOM   5874  CA  PRO B 211      47.060   6.411   2.956  1.00 48.15           C
ANISOU 5874  CA  PRO B 211     7882   5897   4515    538    746  -1282       C
ATOM   5875  C   PRO B 211      46.179   5.743   3.999  1.00 49.24           C
ANISOU 5875  C   PRO B 211     8080   5858   4770    480    659  -1271       C
ATOM   5876  O   PRO B 211      46.026   6.291   5.103  1.00 46.04           O
ANISOU 5876  O   PRO B 211     7643   5407   4443    447    623  -1139       O
ATOM   5877  CB  PRO B 211      46.284   7.462   2.148  1.00 44.53           C
ANISOU 5877  CB  PRO B 211     7406   5608   3906    460    735  -1228       C
ATOM   5878  CG  PRO B 211      45.896   6.741   0.871  1.00 48.53           C
ANISOU 5878  CG  PRO B 211     7974   6176   4288    460    743  -1392       C
ATOM   5879  CD  PRO B 211      47.105   5.874   0.569  1.00 50.80           C
ANISOU 5879  CD  PRO B 211     8265   6429   4610    575    821  -1513       C
ATOM   5880  N   LEU B 212      45.588   4.581   3.686  1.00 47.65           N
ANISOU 5880  N   LEU B 212     7964   5557   4582    462    626  -1408       N
ATOM   5881  CA  LEU B 212      44.818   3.850   4.688  1.00 45.34           C
ANISOU 5881  CA  LEU B 212     7729   5085   4412    406    552  -1394       C
ATOM   5882  C   LEU B 212      45.710   3.019   5.609  1.00 46.52           C
ANISOU 5882  C   LEU B 212     7890   5068   4716    493    566  -1390       C
ATOM   5883  O   LEU B 212      45.322   2.740   6.745  1.00 46.07           O
ANISOU 5883  O   LEU B 212     7855   4881   4768    457    514  -1312       O
ATOM   5884  CB  LEU B 212      43.769   2.981   3.988  1.00 45.34           C
ANISOU 5884  CB  LEU B 212     7811   5041   4374    338    507  -1537       C
ATOM   5885  CG  LEU B 212      42.601   3.790   3.398  1.00 43.10           C
ANISOU 5885  CG  LEU B 212     7515   4899   3962    232    463  -1510       C
ATOM   5886  CD1 LEU B 212      41.770   2.964   2.472  1.00 42.66           C
ANISOU 5886  CD1 LEU B 212     7527   4836   3844    179    426  -1675       C
ATOM   5887  CD2 LEU B 212      41.720   4.379   4.511  1.00 42.54           C
ANISOU 5887  CD2 LEU B 212     7420   4788   3954    143    400  -1361       C
ATOM   5888  N   VAL B 213      46.902   2.623   5.156  1.00 47.30           N
ANISOU 5888  N   VAL B 213     7972   5175   4826    610    634  -1468       N
ATOM   5889  CA  VAL B 213      47.857   1.983   6.057  1.00 44.75           C
ANISOU 5889  CA  VAL B 213     7642   4712   4649    706    645  -1444       C
ATOM   5890  C   VAL B 213      48.305   2.965   7.134  1.00 45.96           C
ANISOU 5890  C   VAL B 213     7713   4904   4845    709    638  -1265       C
ATOM   5891  O   VAL B 213      48.265   2.658   8.333  1.00 47.13           O
ANISOU 5891  O   VAL B 213     7875   4926   5107    708    591  -1182       O
ATOM   5892  CB  VAL B 213      49.052   1.409   5.267  1.00 48.07           C
ANISOU 5892  CB  VAL B 213     8047   5151   5068    838    725  -1573       C
ATOM   5893  CG1 VAL B 213      50.209   1.087   6.199  1.00 44.25           C
ANISOU 5893  CG1 VAL B 213     7519   4570   4722    951    742  -1514       C
ATOM   5894  CG2 VAL B 213      48.636   0.141   4.508  1.00 48.31           C
ANISOU 5894  CG2 VAL B 213     8175   5077   5104    846    720  -1764       C
ATOM   5895  N   THR B 214      48.694   4.179   6.733  1.00 44.40           N
ANISOU 5895  N   THR B 214     7432   4883   4555    707    681  -1202       N
ATOM   5896  CA  THR B 214      49.022   5.186   7.736  1.00 42.96           C
ANISOU 5896  CA  THR B 214     7171   4738   4412    695    667  -1042       C
ATOM   5897  C   THR B 214      47.839   5.450   8.658  1.00 45.89           C
ANISOU 5897  C   THR B 214     7576   5050   4811    587    587   -949       C
ATOM   5898  O   THR B 214      48.009   5.640   9.868  1.00 40.46           O
ANISOU 5898  O   THR B 214     6863   4304   4206    588    553   -845       O
ATOM   5899  CB  THR B 214      49.451   6.482   7.054  1.00 44.13           C
ANISOU 5899  CB  THR B 214     7233   5078   4457    689    724   -991       C
ATOM   5900  OG1 THR B 214      50.534   6.204   6.170  1.00 45.76           O
ANISOU 5900  OG1 THR B 214     7404   5350   4631    787    808  -1081       O
ATOM   5901  CG2 THR B 214      49.868   7.514   8.088  1.00 40.14           C
ANISOU 5901  CG2 THR B 214     6644   4601   4007    678    710   -842       C
ATOM   5902  N   PHE B 215      46.634   5.495   8.087  1.00 46.20           N
ANISOU 5902  N   PHE B 215     7663   5117   4773    494    556   -986       N
ATOM   5903  CA  PHE B 215      45.432   5.798   8.861  1.00 44.59           C
ANISOU 5903  CA  PHE B 215     7480   4876   4586    387    486   -904       C
ATOM   5904  C   PHE B 215      45.174   4.717   9.899  1.00 43.76           C
ANISOU 5904  C   PHE B 215     7437   4586   4602    382    439   -898       C
ATOM   5905  O   PHE B 215      44.838   5.015  11.051  1.00 40.90           O
ANISOU 5905  O   PHE B 215     7062   4184   4293    341    400   -787       O
ATOM   5906  CB  PHE B 215      44.242   5.937   7.911  1.00 42.90           C
ANISOU 5906  CB  PHE B 215     7301   4733   4267    297    462   -963       C
ATOM   5907  CG  PHE B 215      42.993   6.435   8.560  1.00 46.39           C
ANISOU 5907  CG  PHE B 215     7742   5171   4712    189    398   -879       C
ATOM   5908  CD1 PHE B 215      42.883   7.752   8.954  1.00 44.70           C
ANISOU 5908  CD1 PHE B 215     7458   5056   4472    161    395   -758       C
ATOM   5909  CD2 PHE B 215      41.910   5.588   8.749  1.00 45.20           C
ANISOU 5909  CD2 PHE B 215     7659   4920   4596    113    345   -926       C
ATOM   5910  CE1 PHE B 215      41.718   8.215   9.529  1.00 45.01           C
ANISOU 5910  CE1 PHE B 215     7491   5097   4514     68    340   -690       C
ATOM   5911  CE2 PHE B 215      40.750   6.045   9.318  1.00 45.75           C
ANISOU 5911  CE2 PHE B 215     7718   4998   4666     14    292   -853       C
ATOM   5912  CZ  PHE B 215      40.655   7.368   9.711  1.00 46.21           C
ANISOU 5912  CZ  PHE B 215     7703   5160   4693     -4    291   -736       C
ATOM   5913  N   MET B 216      45.324   3.451   9.491  1.00 40.76           N
ANISOU 5913  N   MET B 216     7128   4094   4267    423    446  -1017       N
ATOM   5914  CA  MET B 216      45.263   2.333  10.424  1.00 44.46           C
ANISOU 5914  CA  MET B 216     7658   4370   4865    435    410  -1006       C
ATOM   5915  C   MET B 216      46.398   2.393  11.437  1.00 43.89           C
ANISOU 5915  C   MET B 216     7540   4258   4878    530    420   -912       C
ATOM   5916  O   MET B 216      46.210   2.052  12.611  1.00 45.24           O
ANISOU 5916  O   MET B 216     7734   4322   5133    514    377   -822       O
ATOM   5917  CB  MET B 216      45.292   1.003   9.665  1.00 41.93           C
ANISOU 5917  CB  MET B 216     7418   3930   4581    470    420  -1166       C
ATOM   5918  CG  MET B 216      45.393  -0.236  10.572  1.00 45.91           C
ANISOU 5918  CG  MET B 216     7992   4215   5238    499    389  -1154       C
ATOM   5919  SD  MET B 216      47.069  -0.689  11.082  1.00 48.87           S
ANISOU 5919  SD  MET B 216     8334   4517   5717    673    426  -1131       S
ATOM   5920  CE  MET B 216      47.819  -1.050   9.491  1.00 48.02           C
ANISOU 5920  CE  MET B 216     8223   4470   5551    768    500  -1329       C
ATOM   5921  N   ALA B 217      47.593   2.782  10.998  1.00 44.88           N
ANISOU 5921  N   ALA B 217     7598   4471   4982    629    476   -932       N
ATOM   5922  CA  ALA B 217      48.725   2.826  11.925  1.00 45.27           C
ANISOU 5922  CA  ALA B 217     7593   4493   5115    723    481   -850       C
ATOM   5923  C   ALA B 217      48.536   3.889  12.994  1.00 45.52           C
ANISOU 5923  C   ALA B 217     7566   4589   5139    669    445   -701       C
ATOM   5924  O   ALA B 217      49.150   3.802  14.062  1.00 48.24           O
ANISOU 5924  O   ALA B 217     7884   4887   5559    719    421   -617       O
ATOM   5925  CB  ALA B 217      50.027   3.077  11.173  1.00 46.76           C
ANISOU 5925  CB  ALA B 217     7708   4779   5282    834    553   -907       C
ATOM   5926  N   SER B 218      47.718   4.908  12.721  1.00 43.95           N
ANISOU 5926  N   SER B 218     7345   4504   4852    571    440   -668       N
ATOM   5927  CA  SER B 218      47.416   5.957  13.686  1.00 40.96           C
ANISOU 5927  CA  SER B 218     6915   4185   4465    513    407   -542       C
ATOM   5928  C   SER B 218      46.181   5.653  14.517  1.00 41.71           C
ANISOU 5928  C   SER B 218     7069   4197   4581    418    347   -491       C
ATOM   5929  O   SER B 218      45.763   6.511  15.292  1.00 41.67           O
ANISOU 5929  O   SER B 218     7027   4245   4561    362    321   -399       O
ATOM   5930  CB  SER B 218      47.203   7.318  12.979  1.00 45.18           C
ANISOU 5930  CB  SER B 218     7384   4882   4900    463    434   -525       C
ATOM   5931  OG  SER B 218      48.308   7.694  12.177  1.00 48.93           O
ANISOU 5931  OG  SER B 218     7796   5448   5346    538    498   -561       O
ATOM   5932  N   THR B 219      45.555   4.490  14.344  1.00 39.48           N
ANISOU 5932  N   THR B 219     6876   3791   4333    393    329   -553       N
ATOM   5933  CA  THR B 219      44.392   4.144  15.144  1.00 42.57           C
ANISOU 5933  CA  THR B 219     7320   4103   4752    297    279   -499       C
ATOM   5934  C   THR B 219      44.837   3.186  16.235  1.00 44.96           C
ANISOU 5934  C   THR B 219     7663   4261   5158    347    254   -441       C
ATOM   5935  O   THR B 219      45.037   1.993  15.969  1.00 44.74           O
ANISOU 5935  O   THR B 219     7703   4099   5198    389    256   -506       O
ATOM   5936  CB  THR B 219      43.303   3.502  14.280  1.00 44.86           C
ANISOU 5936  CB  THR B 219     7678   4347   5018    217    269   -597       C
ATOM   5937  OG1 THR B 219      43.001   4.357  13.180  1.00 43.13           O
ANISOU 5937  OG1 THR B 219     7421   4273   4694    186    290   -650       O
ATOM   5938  CG2 THR B 219      42.041   3.272  15.095  1.00 41.99           C
ANISOU 5938  CG2 THR B 219     7351   3922   4680    104    222   -535       C
ATOM   5939  N   PRO B 220      44.983   3.631  17.479  1.00 49.69           N
ANISOU 5939  N   PRO B 220     8228   4877   5774    346    227   -320       N
ATOM   5940  CA  PRO B 220      45.524   2.721  18.500  1.00 47.96           C
ANISOU 5940  CA  PRO B 220     8046   4532   5646    408    201   -254       C
ATOM   5941  C   PRO B 220      44.500   1.766  19.082  1.00 45.71           C
ANISOU 5941  C   PRO B 220     7850   4109   5410    328    168   -217       C
ATOM   5942  O   PRO B 220      44.900   0.718  19.595  1.00 48.92           O
ANISOU 5942  O   PRO B 220     8310   4374   5903    383    152   -186       O
ATOM   5943  CB  PRO B 220      46.095   3.678  19.558  1.00 45.15           C
ANISOU 5943  CB  PRO B 220     7610   4274   5269    434    184   -145       C
ATOM   5944  CG  PRO B 220      45.270   4.927  19.429  1.00 48.32           C
ANISOU 5944  CG  PRO B 220     7964   4810   5584    337    188   -132       C
ATOM   5945  CD  PRO B 220      44.760   4.995  17.993  1.00 48.79           C
ANISOU 5945  CD  PRO B 220     8039   4902   5598    299    220   -243       C
ATOM   5946  N   VAL B 221      43.203   2.050  18.982  1.00 44.24           N
ANISOU 5946  N   VAL B 221     7678   3953   5177    203    159   -218       N
ATOM   5947  CA  VAL B 221      42.166   1.199  19.563  1.00 45.92           C
ANISOU 5947  CA  VAL B 221     7964   4045   5437    111    132   -176       C
ATOM   5948  C   VAL B 221      40.893   1.371  18.751  1.00 46.22           C
ANISOU 5948  C   VAL B 221     8012   4120   5428     -8    134   -251       C
ATOM   5949  O   VAL B 221      40.764   2.293  17.944  1.00 46.88           O
ANISOU 5949  O   VAL B 221     8042   4338   5432    -21    149   -308       O
ATOM   5950  CB  VAL B 221      41.858   1.545  21.041  1.00 49.56           C
ANISOU 5950  CB  VAL B 221     8408   4534   5889     72    107    -27       C
ATOM   5951  CG1 VAL B 221      42.953   1.053  21.965  1.00 55.12           C
ANISOU 5951  CG1 VAL B 221     9123   5170   6651    178     91     59       C
ATOM   5952  CG2 VAL B 221      41.601   3.057  21.177  1.00 47.91           C
ANISOU 5952  CG2 VAL B 221     8109   4512   5584     35    112     -2       C
ATOM   5953  N   GLY B 222      39.937   0.473  18.982  1.00 42.13           N
ANISOU 5953  N   GLY B 222     7561   3484   4963    -98    115   -245       N
ATOM   5954  CA  GLY B 222      38.595   0.642  18.473  1.00 46.11           C
ANISOU 5954  CA  GLY B 222     8064   4028   5429   -227    107   -294       C
ATOM   5955  C   GLY B 222      38.207  -0.251  17.325  1.00 45.27           C
ANISOU 5955  C   GLY B 222     8016   3831   5354   -260    104   -435       C
ATOM   5956  O   GLY B 222      37.107  -0.071  16.792  1.00 47.17           O
ANISOU 5956  O   GLY B 222     8247   4121   5555   -366     91   -488       O
ATOM   5957  N   TYR B 223      39.060  -1.192  16.909  1.00 46.95           N
ANISOU 5957  N   TYR B 223     8285   3916   5636   -172    115   -507       N
ATOM   5958  CA  TYR B 223      38.695  -2.182  15.901  1.00 51.80           C
ANISOU 5958  CA  TYR B 223     8967   4421   6295   -204    110   -653       C
ATOM   5959  C   TYR B 223      39.166  -3.575  16.308  1.00 56.68           C
ANISOU 5959  C   TYR B 223     9672   4810   7053   -157    106   -651       C
ATOM   5960  O   TYR B 223      40.214  -3.741  16.945  1.00 54.74           O
ANISOU 5960  O   TYR B 223     9428   4514   6855    -44    115   -577       O
ATOM   5961  CB  TYR B 223      39.264  -1.827  14.511  1.00 49.72           C
ANISOU 5961  CB  TYR B 223     8679   4257   5953   -134    135   -799       C
ATOM   5962  CG  TYR B 223      40.762  -1.709  14.439  1.00 48.42           C
ANISOU 5962  CG  TYR B 223     8494   4109   5796     23    170   -802       C
ATOM   5963  CD1 TYR B 223      41.389  -0.495  14.691  1.00 45.49           C
ANISOU 5963  CD1 TYR B 223     8036   3898   5349     77    189   -724       C
ATOM   5964  CD2 TYR B 223      41.556  -2.812  14.099  1.00 49.74           C
ANISOU 5964  CD2 TYR B 223     8721   4126   6053    117    185   -890       C
ATOM   5965  CE1 TYR B 223      42.758  -0.366  14.622  1.00 45.03           C
ANISOU 5965  CE1 TYR B 223     7946   3864   5301    214    222   -727       C
ATOM   5966  CE2 TYR B 223      42.942  -2.692  14.018  1.00 51.35           C
ANISOU 5966  CE2 TYR B 223     8891   4355   6265    265    220   -895       C
ATOM   5967  CZ  TYR B 223      43.530  -1.451  14.290  1.00 51.36           C
ANISOU 5967  CZ  TYR B 223     8799   4529   6186    309    238   -811       C
ATOM   5968  OH  TYR B 223      44.891  -1.293  14.231  1.00 55.56           O
ANISOU 5968  OH  TYR B 223     9285   5095   6729    447    272   -813       O
ATOM   5969  N   ASN B 224      38.382  -4.579  15.901  1.00 54.65           N
ANISOU 5969  N   ASN B 224     9485   4412   6868   -243     89   -736       N
ATOM   5970  CA  ASN B 224      38.617  -5.971  16.270  1.00 61.44           C
ANISOU 5970  CA  ASN B 224    10437   5027   7879   -222     81   -734       C
ATOM   5971  C   ASN B 224      39.529  -6.723  15.308  1.00 63.23           C
ANISOU 5971  C   ASN B 224    10711   5154   8160   -105     99   -892       C
ATOM   5972  O   ASN B 224      40.194  -7.681  15.724  1.00 64.55           O
ANISOU 5972  O   ASN B 224    10939   5135   8453    -25     99   -869       O
ATOM   5973  CB  ASN B 224      37.286  -6.720  16.344  1.00 65.00           C
ANISOU 5973  CB  ASN B 224    10940   5357   8398   -385     54   -749       C
ATOM   5974  CG  ASN B 224      36.431  -6.267  17.499  1.00 73.44           C
ANISOU 5974  CG  ASN B 224    11976   6481   9448   -493     43   -576       C
ATOM   5975  OD1 ASN B 224      35.203  -6.259  17.401  1.00 81.05           O
ANISOU 5975  OD1 ASN B 224    12929   7465  10401   -640     27   -591       O
ATOM   5976  ND2 ASN B 224      37.073  -5.878  18.603  1.00 70.96           N
ANISOU 5976  ND2 ASN B 224    11639   6200   9124   -422     51   -416       N
ATOM   5977  N   GLN B 225      39.565  -6.336  14.034  1.00 61.17           N
ANISOU 5977  N   GLN B 225    10424   5012   7808    -92    114  -1053       N
ATOM   5978  CA  GLN B 225      40.362  -7.063  13.057  1.00 58.16           C
ANISOU 5978  CA  GLN B 225    10085   4547   7466     14    137  -1223       C
ATOM   5979  C   GLN B 225      41.852  -6.919  13.363  1.00 57.45           C
ANISOU 5979  C   GLN B 225     9964   4467   7396    191    171  -1174       C
ATOM   5980  O   GLN B 225      42.283  -6.004  14.076  1.00 53.26           O
ANISOU 5980  O   GLN B 225     9364   4062   6809    229    177  -1034       O
ATOM   5981  CB  GLN B 225      40.082  -6.542  11.641  1.00 56.50           C
ANISOU 5981  CB  GLN B 225     9844   4503   7122    -11    150  -1393       C
ATOM   5982  CG  GLN B 225      38.614  -6.511  11.273  1.00 58.59           C
ANISOU 5982  CG  GLN B 225    10116   4800   7346   -183    110  -1443       C
ATOM   5983  CD  GLN B 225      37.975  -5.185  11.603  1.00 57.68           C
ANISOU 5983  CD  GLN B 225     9914   4893   7109   -257     99  -1323       C
ATOM   5984  OE1 GLN B 225      38.312  -4.549  12.617  1.00 57.41           O
ANISOU 5984  OE1 GLN B 225     9836   4906   7071   -226    107  -1157       O
ATOM   5985  NE2 GLN B 225      37.063  -4.737  10.741  1.00 56.73           N
ANISOU 5985  NE2 GLN B 225     9766   4904   6886   -352     77  -1411       N
ATOM   5986  N   ASN B 226      42.637  -7.851  12.813  1.00 60.77           N
ANISOU 5986  N   ASN B 226    10434   4752   7902    301    192  -1299       N
ATOM   5987  CA  ASN B 226      44.085  -7.699  12.729  1.00 60.41           C
ANISOU 5987  CA  ASN B 226    10346   4747   7861    479    232  -1306       C
ATOM   5988  C   ASN B 226      44.441  -6.483  11.873  1.00 56.09           C
ANISOU 5988  C   ASN B 226     9708   4461   7144    507    272  -1363       C
ATOM   5989  O   ASN B 226      43.638  -6.006  11.068  1.00 55.85           O
ANISOU 5989  O   ASN B 226     9666   4551   7002    410    270  -1443       O
ATOM   5990  CB  ASN B 226      44.724  -8.957  12.137  1.00 61.09           C
ANISOU 5990  CB  ASN B 226    10502   4641   8069    585    250  -1462       C
ATOM   5991  CG  ASN B 226      44.602 -10.150  13.055  1.00 67.44           C
ANISOU 5991  CG  ASN B 226    11394   5171   9059    585    214  -1383       C
ATOM   5992  OD1 ASN B 226      44.772 -11.299  12.640  1.00 69.41           O
ANISOU 5992  OD1 ASN B 226    11721   5220   9433    631    216  -1507       O
ATOM   5993  ND2 ASN B 226      44.299  -9.883  14.317  1.00 71.51           N
ANISOU 5993  ND2 ASN B 226    11900   5676   9595    531    181  -1173       N
ATOM   5994  N   GLU B 227      45.683  -6.011  12.032  1.00 54.87           N
ANISOU 5994  N   GLU B 227     9484   4390   6975    644    307  -1318       N
ATOM   5995  CA  GLU B 227      46.082  -4.702  11.515  1.00 52.44           C
ANISOU 5995  CA  GLU B 227     9077   4331   6517    664    346  -1313       C
ATOM   5996  C   GLU B 227      45.861  -4.584  10.004  1.00 55.35           C
ANISOU 5996  C   GLU B 227     9448   4807   6776    647    381  -1499       C
ATOM   5997  O   GLU B 227      45.176  -3.668   9.525  1.00 49.94           O
ANISOU 5997  O   GLU B 227     8726   4290   5958    554    379  -1496       O
ATOM   5998  CB  GLU B 227      47.554  -4.462  11.850  1.00 51.92           C
ANISOU 5998  CB  GLU B 227     8940   4305   6482    822    381  -1262       C
ATOM   5999  CG  GLU B 227      47.929  -4.450  13.322  1.00 55.74           C
ANISOU 5999  CG  GLU B 227     9406   4720   7052    856    343  -1076       C
ATOM   6000  CD  GLU B 227      47.233  -3.381  14.144  1.00 55.75           C
ANISOU 6000  CD  GLU B 227     9365   4841   6977    744    310   -922       C
ATOM   6001  OE1 GLU B 227      45.988  -3.381  14.249  1.00 58.18           O
ANISOU 6001  OE1 GLU B 227     9717   5128   7261    607    279   -905       O
ATOM   6002  OE2 GLU B 227      47.954  -2.529  14.699  1.00 56.50           O
ANISOU 6002  OE2 GLU B 227     9374   5052   7041    796    316   -822       O
ATOM   6003  N   TYR B 228      46.438  -5.501   9.233  1.00 53.90           N
ANISOU 6003  N   TYR B 228     9305   4532   6640    739    414  -1662       N
ATOM   6004  CA  TYR B 228      46.328  -5.395   7.786  1.00 53.05           C
ANISOU 6004  CA  TYR B 228     9198   4545   6413    735    453  -1845       C
ATOM   6005  C   TYR B 228      44.946  -5.777   7.299  1.00 52.79           C
ANISOU 6005  C   TYR B 228     9236   4471   6351    587    405  -1937       C
ATOM   6006  O   TYR B 228      44.512  -5.287   6.250  1.00 50.49           O
ANISOU 6006  O   TYR B 228     8928   4340   5914    537    417  -2035       O
ATOM   6007  CB  TYR B 228      47.386  -6.260   7.125  1.00 55.91           C
ANISOU 6007  CB  TYR B 228     9579   4830   6833    885    507  -2005       C
ATOM   6008  CG  TYR B 228      48.792  -5.823   7.424  1.00 54.72           C
ANISOU 6008  CG  TYR B 228     9340   4754   6698   1033    560  -1935       C
ATOM   6009  CD1 TYR B 228      49.169  -4.496   7.306  1.00 54.60           C
ANISOU 6009  CD1 TYR B 228     9221   4971   6553   1033    595  -1846       C
ATOM   6010  CD2 TYR B 228      49.753  -6.745   7.794  1.00 58.70           C
ANISOU 6010  CD2 TYR B 228     9859   5094   7351   1175    576  -1960       C
ATOM   6011  CE1 TYR B 228      50.468  -4.099   7.558  1.00 55.31           C
ANISOU 6011  CE1 TYR B 228     9221   5133   6662   1162    643  -1789       C
ATOM   6012  CE2 TYR B 228      51.047  -6.357   8.054  1.00 59.50           C
ANISOU 6012  CE2 TYR B 228     9868   5272   7469   1312    621  -1901       C
ATOM   6013  CZ  TYR B 228      51.400  -5.039   7.939  1.00 55.45           C
ANISOU 6013  CZ  TYR B 228     9249   4995   6827   1301    655  -1818       C
ATOM   6014  OH  TYR B 228      52.698  -4.679   8.200  1.00 56.68           O
ANISOU 6014  OH  TYR B 228     9304   5223   7008   1430    699  -1764       O
ATOM   6015  N   GLU B 229      44.243  -6.606   8.073  1.00 55.25           N
ANISOU 6015  N   GLU B 229     9620   4577   6795    514    351  -1894       N
ATOM   6016  CA  GLU B 229      42.845  -6.913   7.796  1.00 54.25           C
ANISOU 6016  CA  GLU B 229     9547   4409   6655    355    298  -1954       C
ATOM   6017  C   GLU B 229      41.985  -5.657   7.913  1.00 51.96           C
ANISOU 6017  C   GLU B 229     9191   4320   6231    238    273  -1842       C
ATOM   6018  O   GLU B 229      41.097  -5.423   7.089  1.00 50.72           O
ANISOU 6018  O   GLU B 229     9035   4263   5972    141    251  -1934       O
ATOM   6019  CB  GLU B 229      42.387  -7.999   8.768  1.00 58.25           C
ANISOU 6019  CB  GLU B 229    10134   4652   7347    304    253  -1896       C
ATOM   6020  CG  GLU B 229      41.215  -8.853   8.356  1.00 64.17           C
ANISOU 6020  CG  GLU B 229    10962   5273   8148    169    208  -2018       C
ATOM   6021  CD  GLU B 229      41.186 -10.171   9.144  1.00 69.91           C
ANISOU 6021  CD  GLU B 229    11778   5696   9087    168    184  -1991       C
ATOM   6022  OE1 GLU B 229      41.423 -10.127  10.383  1.00 72.71           O
ANISOU 6022  OE1 GLU B 229    12126   5978   9523    188    175  -1794       O
ATOM   6023  OE2 GLU B 229      40.924 -11.241   8.533  1.00 68.09           O
ANISOU 6023  OE2 GLU B 229    11627   5302   8944    147    172  -2164       O
ATOM   6024  N   PHE B 230      42.268  -4.813   8.911  1.00 51.80           N
ANISOU 6024  N   PHE B 230     9109   4368   6206    253    275  -1649       N
ATOM   6025  CA  PHE B 230      41.494  -3.590   9.101  1.00 49.23           C
ANISOU 6025  CA  PHE B 230     8717   4220   5766    154    254  -1539       C
ATOM   6026  C   PHE B 230      41.680  -2.636   7.925  1.00 48.82           C
ANISOU 6026  C   PHE B 230     8607   4398   5545    176    287  -1612       C
ATOM   6027  O   PHE B 230      40.727  -1.963   7.513  1.00 47.66           O
ANISOU 6027  O   PHE B 230     8434   4380   5294     74    259  -1608       O
ATOM   6028  CB  PHE B 230      41.899  -2.921  10.414  1.00 47.07           C
ANISOU 6028  CB  PHE B 230     8391   3965   5528    181    253  -1336       C
ATOM   6029  CG  PHE B 230      41.111  -1.689  10.747  1.00 42.22           C
ANISOU 6029  CG  PHE B 230     7711   3512   4818     86    231  -1220       C
ATOM   6030  CD1 PHE B 230      39.725  -1.744  10.896  1.00 41.98           C
ANISOU 6030  CD1 PHE B 230     7699   3467   4783    -59    184  -1207       C
ATOM   6031  CD2 PHE B 230      41.758  -0.473  10.937  1.00 45.49           C
ANISOU 6031  CD2 PHE B 230     8039   4087   5158    140    259  -1125       C
ATOM   6032  CE1 PHE B 230      38.993  -0.603  11.215  1.00 43.57           C
ANISOU 6032  CE1 PHE B 230     7834   3815   4904   -137    165  -1105       C
ATOM   6033  CE2 PHE B 230      41.052   0.673  11.261  1.00 39.52           C
ANISOU 6033  CE2 PHE B 230     7223   3466   4326     60    239  -1024       C
ATOM   6034  CZ  PHE B 230      39.648   0.611  11.399  1.00 41.87           C
ANISOU 6034  CZ  PHE B 230     7541   3751   4618    -76    192  -1014       C
ATOM   6035  N   VAL B 231      42.898  -2.566   7.370  1.00 49.10           N
ANISOU 6035  N   VAL B 231     8617   4489   5549    308    348  -1672       N
ATOM   6036  CA  VAL B 231      43.106  -1.814   6.127  1.00 51.19           C
ANISOU 6036  CA  VAL B 231     8836   4963   5649    330    388  -1754       C
ATOM   6037  C   VAL B 231      42.171  -2.328   5.034  1.00 49.53           C
ANISOU 6037  C   VAL B 231     8682   4769   5369    249    359  -1925       C
ATOM   6038  O   VAL B 231      41.481  -1.546   4.373  1.00 50.09           O
ANISOU 6038  O   VAL B 231     8721   5011   5301    177    342  -1929       O
ATOM   6039  CB  VAL B 231      44.573  -1.906   5.666  1.00 53.81           C
ANISOU 6039  CB  VAL B 231     9139   5332   5976    486    465  -1816       C
ATOM   6040  CG1 VAL B 231      44.745  -1.149   4.341  1.00 51.90           C
ANISOU 6040  CG1 VAL B 231     8852   5316   5551    500    513  -1896       C
ATOM   6041  CG2 VAL B 231      45.511  -1.387   6.723  1.00 49.12           C
ANISOU 6041  CG2 VAL B 231     8480   4734   5451    563    486  -1654       C
ATOM   6042  N   GLY B 232      42.124  -3.657   4.849  1.00 47.42           N
ANISOU 6042  N   GLY B 232     8498   4318   5203    260    348  -2069       N
ATOM   6043  CA  GLY B 232      41.170  -4.245   3.916  1.00 51.77           C
ANISOU 6043  CA  GLY B 232     9105   4859   5704    171    309  -2241       C
ATOM   6044  C   GLY B 232      39.726  -3.859   4.202  1.00 53.59           C
ANISOU 6044  C   GLY B 232     9327   5125   5908      8    235  -2170       C
ATOM   6045  O   GLY B 232      38.940  -3.629   3.278  1.00 51.29           O
ANISOU 6045  O   GLY B 232     9032   4960   5495    -68    204  -2264       O
ATOM   6046  N   ALA B 233      39.350  -3.788   5.485  1.00 48.81           N
ANISOU 6046  N   ALA B 233     8715   4419   5413    -46    205  -2004       N
ATOM   6047  CA  ALA B 233      38.011  -3.306   5.815  1.00 49.17           C
ANISOU 6047  CA  ALA B 233     8735   4517   5430   -194    144  -1924       C
ATOM   6048  C   ALA B 233      37.829  -1.856   5.379  1.00 47.33           C
ANISOU 6048  C   ALA B 233     8416   4539   5030   -204    148  -1849       C
ATOM   6049  O   ALA B 233      36.786  -1.499   4.827  1.00 49.92           O
ANISOU 6049  O   ALA B 233     8724   4975   5267   -303    102  -1883       O
ATOM   6050  CB  ALA B 233      37.746  -3.452   7.315  1.00 50.13           C
ANISOU 6050  CB  ALA B 233     8860   4498   5690   -237    124  -1753       C
ATOM   6051  N   LEU B 234      38.827  -1.001   5.645  1.00 44.49           N
ANISOU 6051  N   LEU B 234     8001   4272   4633   -105    201  -1742       N
ATOM   6052  CA  LEU B 234      38.779   0.396   5.219  1.00 47.26           C
ANISOU 6052  CA  LEU B 234     8271   4848   4836   -105    212  -1664       C
ATOM   6053  C   LEU B 234      38.751   0.567   3.701  1.00 50.47           C
ANISOU 6053  C   LEU B 234     8678   5415   5084    -93    224  -1804       C
ATOM   6054  O   LEU B 234      38.268   1.597   3.216  1.00 48.22           O
ANISOU 6054  O   LEU B 234     8340   5311   4672   -132    209  -1752       O
ATOM   6055  CB  LEU B 234      39.979   1.151   5.770  1.00 43.90           C
ANISOU 6055  CB  LEU B 234     7789   4469   4420      1    271  -1540       C
ATOM   6056  CG  LEU B 234      40.039   1.344   7.278  1.00 44.03           C
ANISOU 6056  CG  LEU B 234     7786   4390   4553     -7    258  -1375       C
ATOM   6057  CD1 LEU B 234      41.357   1.996   7.663  1.00 44.10           C
ANISOU 6057  CD1 LEU B 234     7738   4450   4568    106    314  -1286       C
ATOM   6058  CD2 LEU B 234      38.855   2.165   7.747  1.00 41.98           C
ANISOU 6058  CD2 LEU B 234     7486   4203   4262   -121    208  -1268       C
ATOM   6059  N   GLN B 235      39.264  -0.399   2.942  1.00 47.41           N
ANISOU 6059  N   GLN B 235     8347   4968   4696    -35    251  -1978       N
ATOM   6060  CA  GLN B 235      39.204  -0.361   1.487  1.00 53.30           C
ANISOU 6060  CA  GLN B 235     9102   5868   5282    -26    261  -2129       C
ATOM   6061  C   GLN B 235      37.908  -0.955   0.956  1.00 55.53           C
ANISOU 6061  C   GLN B 235     9428   6132   5539   -147    182  -2256       C
ATOM   6062  O   GLN B 235      37.816  -1.252  -0.242  1.00 59.90           O
ANISOU 6062  O   GLN B 235    10008   6778   5975   -143    180  -2423       O
ATOM   6063  CB  GLN B 235      40.417  -1.083   0.899  1.00 49.86           C
ANISOU 6063  CB  GLN B 235     8700   5392   4851    101    335  -2270       C
ATOM   6064  CG  GLN B 235      41.705  -0.557   1.464  1.00 49.77           C
ANISOU 6064  CG  GLN B 235     8635   5394   4879    218    409  -2149       C
ATOM   6065  CD  GLN B 235      42.918  -1.133   0.788  1.00 54.59           C
ANISOU 6065  CD  GLN B 235     9260   6002   5478    350    489  -2285       C
ATOM   6066  OE1 GLN B 235      43.012  -2.336   0.586  1.00 57.65           O
ANISOU 6066  OE1 GLN B 235     9718   6241   5946    378    487  -2444       O
ATOM   6067  NE2 GLN B 235      43.850  -0.273   0.411  1.00 54.26           N
ANISOU 6067  NE2 GLN B 235     9148   6126   5341    432    562  -2228       N
ATOM   6068  N   ASP B 236      36.916  -1.128   1.836  1.00 51.97           N
ANISOU 6068  N   ASP B 236     8981   5572   5193   -256    119  -2181       N
ATOM   6069  CA  ASP B 236      35.583  -1.610   1.496  1.00 56.03           C
ANISOU 6069  CA  ASP B 236     9518   6068   5701   -389     37  -2276       C
ATOM   6070  C   ASP B 236      35.584  -3.071   1.066  1.00 58.98           C
ANISOU 6070  C   ASP B 236     9982   6274   6156   -398     25  -2486       C
ATOM   6071  O   ASP B 236      34.772  -3.473   0.236  1.00 64.51           O
ANISOU 6071  O   ASP B 236    10703   7013   6793   -479    -30  -2636       O
ATOM   6072  CB  ASP B 236      34.927  -0.738   0.422  1.00 58.23           C
ANISOU 6072  CB  ASP B 236     9749   6594   5783   -431      1  -2302       C
ATOM   6073  CG  ASP B 236      33.417  -0.694   0.556  1.00 62.17           C
ANISOU 6073  CG  ASP B 236    10225   7109   6289   -580    -92  -2290       C
ATOM   6074  OD1 ASP B 236      32.907  -1.109   1.619  1.00 66.40           O
ANISOU 6074  OD1 ASP B 236    10767   7482   6979   -650   -117  -2221       O
ATOM   6075  OD2 ASP B 236      32.735  -0.268  -0.402  1.00 70.06           O
ANISOU 6075  OD2 ASP B 236    11195   8285   7140   -626   -140  -2349       O
ATOM   6076  N   GLY B 237      36.477  -3.877   1.643  1.00 57.69           N
ANISOU 6076  N   GLY B 237     9869   5915   6136   -317     72  -2499       N
ATOM   6077  CA  GLY B 237      36.516  -5.302   1.392  1.00 59.51           C
ANISOU 6077  CA  GLY B 237    10188   5944   6479   -320     63  -2686       C
ATOM   6078  C   GLY B 237      37.649  -5.770   0.509  1.00 57.75           C
ANISOU 6078  C   GLY B 237    10001   5731   6212   -184    128  -2852       C
ATOM   6079  O   GLY B 237      37.718  -6.969   0.211  1.00 63.58           O
ANISOU 6079  O   GLY B 237    10816   6299   7043   -176    123  -3030       O
ATOM   6080  N   VAL B 238      38.537  -4.882   0.084  1.00 55.62           N
ANISOU 6080  N   VAL B 238     9677   5648   5809    -77    193  -2804       N
ATOM   6081  CA  VAL B 238      39.612  -5.229  -0.841  1.00 59.28           C
ANISOU 6081  CA  VAL B 238    10160   6157   6205     54    266  -2964       C
ATOM   6082  C   VAL B 238      40.856  -5.545  -0.019  1.00 56.92           C
ANISOU 6082  C   VAL B 238     9863   5712   6053    186    333  -2890       C
ATOM   6083  O   VAL B 238      41.318  -4.676   0.735  1.00 56.93           O
ANISOU 6083  O   VAL B 238     9799   5769   6061    223    359  -2692       O
ATOM   6084  CB  VAL B 238      39.885  -4.097  -1.837  1.00 59.47           C
ANISOU 6084  CB  VAL B 238    10120   6481   5995     91    305  -2952       C
ATOM   6085  CG1 VAL B 238      40.990  -4.479  -2.790  1.00 57.65           C
ANISOU 6085  CG1 VAL B 238     9905   6309   5689    224    389  -3120       C
ATOM   6086  CG2 VAL B 238      38.637  -3.789  -2.582  1.00 60.50           C
ANISOU 6086  CG2 VAL B 238    10246   6755   5985    -35    228  -3010       C
ATOM   6087  N   PRO B 239      41.410  -6.752  -0.116  1.00 56.61           N
ANISOU 6087  N   PRO B 239     9892   5482   6137    260    357  -3044       N
ATOM   6088  CA  PRO B 239      42.650  -7.049   0.609  1.00 59.57           C
ANISOU 6088  CA  PRO B 239    10259   5728   6646    402    418  -2976       C
ATOM   6089  C   PRO B 239      43.787  -6.152   0.139  1.00 61.33           C
ANISOU 6089  C   PRO B 239    10401   6164   6737    526    506  -2938       C
ATOM   6090  O   PRO B 239      43.822  -5.686  -1.003  1.00 64.76           O
ANISOU 6090  O   PRO B 239    10812   6809   6985    534    537  -3037       O
ATOM   6091  CB  PRO B 239      42.928  -8.526   0.273  1.00 61.22           C
ANISOU 6091  CB  PRO B 239    10559   5716   6987    458    425  -3193       C
ATOM   6092  CG  PRO B 239      41.632  -9.078  -0.236  1.00 58.80           C
ANISOU 6092  CG  PRO B 239    10279   5383   6680    308    343  -3316       C
ATOM   6093  CD  PRO B 239      40.924  -7.906  -0.892  1.00 57.82           C
ANISOU 6093  CD  PRO B 239    10117   5531   6322    221    323  -3286       C
ATOM   6094  N   MET B 240      44.704  -5.887   1.053  1.00 59.67           N
ANISOU 6094  N   MET B 240    10145   5904   6622    617    544  -2785       N
ATOM   6095  CA  MET B 240      45.942  -5.198   0.751  1.00 64.32           C
ANISOU 6095  CA  MET B 240    10653   6654   7131    745    633  -2749       C
ATOM   6096  C   MET B 240      47.055  -6.226   0.605  1.00 65.40           C
ANISOU 6096  C   MET B 240    10816   6654   7381    900    693  -2887       C
ATOM   6097  O   MET B 240      46.960  -7.348   1.108  1.00 65.57           O
ANISOU 6097  O   MET B 240    10909   6426   7576    914    659  -2944       O
ATOM   6098  CB  MET B 240      46.277  -4.187   1.853  1.00 62.01           C
ANISOU 6098  CB  MET B 240    10282   6409   6872    748    632  -2497       C
ATOM   6099  CG  MET B 240      46.741  -4.812   3.150  1.00 58.14           C
ANISOU 6099  CG  MET B 240     9806   5694   6589    804    614  -2398       C
ATOM   6100  SD  MET B 240      47.473  -3.519   4.172  1.00 63.87           S
ANISOU 6100  SD  MET B 240    10419   6536   7313    841    634  -2145       S
ATOM   6101  CE  MET B 240      49.136  -3.441   3.490  1.00 56.70           C
ANISOU 6101  CE  MET B 240     9437   5735   6372   1022    745  -2225       C
ATOM   6102  N   ASP B 241      48.120  -5.827  -0.089  1.00 69.30           N
ANISOU 6102  N   ASP B 241    11244   7311   7776   1017    785  -2937       N
ATOM   6103  CA  ASP B 241      49.251  -6.712  -0.363  1.00 64.13           C
ANISOU 6103  CA  ASP B 241    10595   6562   7208   1178    855  -3082       C
ATOM   6104  C   ASP B 241      50.334  -6.521   0.691  1.00 62.00           C
ANISOU 6104  C   ASP B 241    10254   6229   7072   1289    884  -2919       C
ATOM   6105  O   ASP B 241      50.743  -5.388   0.967  1.00 64.15           O
ANISOU 6105  O   ASP B 241    10433   6669   7273   1290    911  -2755       O
ATOM   6106  CB  ASP B 241      49.829  -6.428  -1.747  1.00 58.48           C
ANISOU 6106  CB  ASP B 241     9841   6074   6305   1248    948  -3239       C
ATOM   6107  CG  ASP B 241      48.919  -6.877  -2.870  1.00 70.85           C
ANISOU 6107  CG  ASP B 241    11458   7699   7764   1155    919  -3433       C
ATOM   6108  OD1 ASP B 241      47.940  -7.609  -2.600  1.00 72.74           O
ANISOU 6108  OD1 ASP B 241    11768   7767   8102   1055    831  -3480       O
ATOM   6109  OD2 ASP B 241      49.175  -6.477  -4.028  1.00 76.17           O
ANISOU 6109  OD2 ASP B 241    12075   8607   8258   1165    983  -3522       O
ATOM   6110  N   ILE B 242      50.802  -7.629   1.264  1.00 59.58           N
ANISOU 6110  N   ILE B 242     9993   5680   6964   1382    875  -2965       N
ATOM   6111  CA  ILE B 242      51.886  -7.626   2.236  1.00 62.85           C
ANISOU 6111  CA  ILE B 242    10343   6021   7517   1504    895  -2831       C
ATOM   6112  C   ILE B 242      52.969  -8.610   1.795  1.00 64.66           C
ANISOU 6112  C   ILE B 242    10574   6152   7841   1684    963  -3006       C
ATOM   6113  O   ILE B 242      52.766  -9.453   0.916  1.00 65.70           O
ANISOU 6113  O   ILE B 242    10762   6228   7973   1694    980  -3221       O
ATOM   6114  CB  ILE B 242      51.400  -7.969   3.663  1.00 63.88           C
ANISOU 6114  CB  ILE B 242    10519   5933   7818   1449    803  -2659       C
ATOM   6115  CG1 ILE B 242      50.823  -9.384   3.699  1.00 65.52           C
ANISOU 6115  CG1 ILE B 242    10853   5866   8175   1434    755  -2790       C
ATOM   6116  CG2 ILE B 242      50.375  -6.913   4.157  1.00 59.92           C
ANISOU 6116  CG2 ILE B 242    10002   5544   7222   1281    744  -2482       C
ATOM   6117  CD1 ILE B 242      50.484  -9.872   5.079  1.00 65.45           C
ANISOU 6117  CD1 ILE B 242    10893   5629   8347   1399    676  -2624       C
ATOM   6118  N   VAL B 243      54.144  -8.471   2.411  1.00 64.62           N
ANISOU 6118  N   VAL B 243    10481   6144   7926   1817   1000  -2908       N
ATOM   6119  CA  VAL B 243      55.314  -9.262   2.060  1.00 61.90           C
ANISOU 6119  CA  VAL B 243    10110   5734   7675   2007   1072  -3051       C
ATOM   6120  C   VAL B 243      56.154  -9.424   3.319  1.00 61.35           C
ANISOU 6120  C   VAL B 243     9986   5536   7786   2113   1046  -2884       C
ATOM   6121  O   VAL B 243      56.186  -8.546   4.186  1.00 62.50           O
ANISOU 6121  O   VAL B 243    10069   5759   7919   2062   1012  -2669       O
ATOM   6122  CB  VAL B 243      56.134  -8.613   0.912  1.00 64.19           C
ANISOU 6122  CB  VAL B 243    10299   6297   7792   2081   1191  -3156       C
ATOM   6123  CG1 VAL B 243      56.709  -7.257   1.333  1.00 59.88           C
ANISOU 6123  CG1 VAL B 243     9620   5967   7166   2070   1220  -2948       C
ATOM   6124  CG2 VAL B 243      57.245  -9.565   0.388  1.00 66.67           C
ANISOU 6124  CG2 VAL B 243    10542   6568   8222   2226   1270  -3311       C
ATOM   6125  N   LYS B 244      56.815 -10.570   3.430  1.00 63.34           N
ANISOU 6125  N   LYS B 244    10253   5595   8216   2252   1057  -2979       N
ATOM   6126  CA  LYS B 244      57.723 -10.807   4.544  1.00 65.10           C
ANISOU 6126  CA  LYS B 244    10429   5695   8609   2386   1034  -2841       C
ATOM   6127  C   LYS B 244      58.912  -9.862   4.461  1.00 67.40           C
ANISOU 6127  C   LYS B 244    10559   6224   8825   2484   1111  -2777       C
ATOM   6128  O   LYS B 244      59.394  -9.539   3.373  1.00 70.54           O
ANISOU 6128  O   LYS B 244    10894   6809   9097   2531   1209  -2915       O
ATOM   6129  CB  LYS B 244      58.191 -12.263   4.533  1.00 65.58           C
ANISOU 6129  CB  LYS B 244    10494   5534   8889   2482   1033  -2946       C
ATOM   6130  CG  LYS B 244      58.494 -12.849   5.895  1.00 67.37           C
ANISOU 6130  CG  LYS B 244    10738   5533   9325   2554    955  -2778       C
ATOM   6131  CD  LYS B 244      59.275 -14.167   5.750  1.00 76.99           C
ANISOU 6131  CD  LYS B 244    11926   6573  10752   2685    983  -2885       C
ATOM   6132  CE  LYS B 244      60.447 -14.072   4.765  1.00 73.12           C
ANISOU 6132  CE  LYS B 244    11312   6256  10215   2817   1106  -3036       C
ATOM   6133  NZ  LYS B 244      61.649 -13.341   5.280  1.00 74.66           N
ANISOU 6133  NZ  LYS B 244    11370   6592  10405   2956   1132  -2914       N
ATOM   6134  N   SER B 245      59.367  -9.395   5.619  1.00 67.84           N
ANISOU 6134  N   SER B 245    10542   6282   8953   2506   1064  -2562       N
ATOM   6135  CA  SER B 245      60.613  -8.649   5.685  1.00 70.62           C
ANISOU 6135  CA  SER B 245    10730   6824   9280   2611   1127  -2498       C
ATOM   6136  C   SER B 245      61.778  -9.566   5.328  1.00 73.83           C
ANISOU 6136  C   SER B 245    11089   7152   9811   2826   1192  -2646       C
ATOM   6137  O   SER B 245      61.688 -10.793   5.442  1.00 76.61           O
ANISOU 6137  O   SER B 245    11521   7267  10320   2887   1160  -2728       O
ATOM   6138  CB  SER B 245      60.822  -8.069   7.086  1.00 73.57           C
ANISOU 6138  CB  SER B 245    11042   7192   9718   2589   1048  -2247       C
ATOM   6139  OG  SER B 245      60.574  -9.052   8.086  1.00 71.68           O
ANISOU 6139  OG  SER B 245    10893   6684   9657   2624    955  -2176       O
ATOM   6140  N   ASP B 246      62.883  -8.958   4.883  1.00 76.28           N
ANISOU 6140  N   ASP B 246    11248   7674  10063   2921   1286  -2668       N
ATOM   6141  CA  ASP B 246      64.057  -9.744   4.500  1.00 77.94           C
ANISOU 6141  CA  ASP B 246    11373   7849  10390   3108   1357  -2798       C
ATOM   6142  C   ASP B 246      64.655 -10.489   5.694  1.00 76.48           C
ANISOU 6142  C   ASP B 246    11169   7455  10436   3230   1278  -2685       C
ATOM   6143  O   ASP B 246      64.981 -11.678   5.594  1.00 76.08           O
ANISOU 6143  O   ASP B 246    11130   7229  10550   3309   1281  -2775       O
ATOM   6144  CB  ASP B 246      65.123  -8.854   3.858  1.00 78.54           C
ANISOU 6144  CB  ASP B 246    11278   8210  10354   3176   1475  -2824       C
ATOM   6145  CG  ASP B 246      64.915  -8.661   2.367  1.00 79.35           C
ANISOU 6145  CG  ASP B 246    11376   8492  10280   3105   1585  -2998       C
ATOM   6146  OD1 ASP B 246      63.840  -9.033   1.851  1.00 83.23           O
ANISOU 6146  OD1 ASP B 246    12000   8914  10708   2990   1559  -3091       O
ATOM   6147  OD2 ASP B 246      65.850  -8.171   1.699  1.00 74.48           O
ANISOU 6147  OD2 ASP B 246    10620   8090   9589   3164   1698  -3043       O
ATOM   6148  N   LEU B 247      64.815  -9.808   6.832  1.00 76.54           N
ANISOU 6148  N   LEU B 247    11134   7487  10462   3229   1208  -2474       N
ATOM   6149  CA  LEU B 247      65.578 -10.373   7.941  1.00 79.63           C
ANISOU 6149  CA  LEU B 247    11479   7727  11048   3373   1139  -2359       C
ATOM   6150  C   LEU B 247      64.737 -11.141   8.952  1.00 78.87           C
ANISOU 6150  C   LEU B 247    11533   7357  11077   3324   1014  -2248       C
ATOM   6151  O   LEU B 247      65.272 -12.038   9.614  1.00 80.04           O
ANISOU 6151  O   LEU B 247    11665   7332  11415   3434    963  -2196       O
ATOM   6152  CB  LEU B 247      66.345  -9.268   8.681  1.00 78.42           C
ANISOU 6152  CB  LEU B 247    11161   7773  10863   3372   1124  -2173       C
ATOM   6153  CG  LEU B 247      67.255  -8.381   7.829  1.00 75.90           C
ANISOU 6153  CG  LEU B 247    10672   7737  10429   3409   1246  -2243       C
ATOM   6154  CD1 LEU B 247      68.102  -7.462   8.696  1.00 68.99           C
ANISOU 6154  CD1 LEU B 247     9630   7013   9568   3425   1216  -2062       C
ATOM   6155  CD2 LEU B 247      68.126  -9.265   6.976  1.00 75.96           C
ANISOU 6155  CD2 LEU B 247    10633   7713  10517   3596   1342  -2449       C
ATOM   6156  N   TYR B 248      63.446 -10.838   9.082  1.00 72.12           N
ANISOU 6156  N   TYR B 248    10794   6478  10130   3127    962  -2189       N
ATOM   6157  CA  TYR B 248      62.644 -11.331  10.200  1.00 71.14           C
ANISOU 6157  CA  TYR B 248    10789   6137  10105   3055    844  -2036       C
ATOM   6158  C   TYR B 248      61.382 -12.008   9.677  1.00 74.65           C
ANISOU 6158  C   TYR B 248    11406   6418  10541   2936    830  -2151       C
ATOM   6159  O   TYR B 248      60.490 -11.342   9.142  1.00 78.18           O
ANISOU 6159  O   TYR B 248    11888   6990  10828   2770    847  -2182       O
ATOM   6160  CB  TYR B 248      62.318 -10.187  11.157  1.00 74.94           C
ANISOU 6160  CB  TYR B 248    11221   6761  10492   2921    781  -1809       C
ATOM   6161  CG  TYR B 248      63.578  -9.494  11.615  1.00 78.08           C
ANISOU 6161  CG  TYR B 248    11441   7329  10897   3030    793  -1713       C
ATOM   6162  CD1 TYR B 248      64.543 -10.188  12.328  1.00 76.26           C
ANISOU 6162  CD1 TYR B 248    11159   6981  10836   3211    753  -1656       C
ATOM   6163  CD2 TYR B 248      63.826  -8.159  11.294  1.00 76.59           C
ANISOU 6163  CD2 TYR B 248    11132   7417  10553   2955    845  -1684       C
ATOM   6164  CE1 TYR B 248      65.711  -9.575  12.740  1.00 76.27           C
ANISOU 6164  CE1 TYR B 248    10987   7143  10847   3310    759  -1576       C
ATOM   6165  CE2 TYR B 248      64.997  -7.529  11.698  1.00 75.08           C
ANISOU 6165  CE2 TYR B 248    10770   7380  10378   3047    856  -1604       C
ATOM   6166  CZ  TYR B 248      65.939  -8.246  12.422  1.00 78.52           C
ANISOU 6166  CZ  TYR B 248    11151   7703  10980   3224    811  -1554       C
ATOM   6167  OH  TYR B 248      67.111  -7.641  12.839  1.00 78.67           O
ANISOU 6167  OH  TYR B 248    10991   7880  11020   3315    815  -1479       O
ATOM   6168  N   ASP B 249      61.308 -13.332   9.864  1.00 78.13           N
ANISOU 6168  N   ASP B 249    11915   6603  11169   2981    794  -2190       N
ATOM   6169  CA  ASP B 249      60.237 -14.142   9.289  1.00 77.18           C
ANISOU 6169  CA  ASP B 249    11918   6330  11077   2856    786  -2316       C
ATOM   6170  C   ASP B 249      58.863 -13.753   9.799  1.00 75.77           C
ANISOU 6170  C   ASP B 249    11864   6107  10817   2669    713  -2204       C
ATOM   6171  O   ASP B 249      57.865 -13.983   9.107  1.00 78.36           O
ANISOU 6171  O   ASP B 249    12277   6405  11093   2534    718  -2324       O
ATOM   6172  CB  ASP B 249      60.476 -15.619   9.591  1.00 79.35           C
ANISOU 6172  CB  ASP B 249    12222   6333  11596   2929    758  -2335       C
ATOM   6173  CG  ASP B 249      61.098 -16.340   8.441  1.00 87.27           C
ANISOU 6173  CG  ASP B 249    13174   7329  12654   3018    858  -2566       C
ATOM   6174  OD1 ASP B 249      60.768 -17.528   8.238  1.00101.26           O
ANISOU 6174  OD1 ASP B 249    15019   8881  14575   3002    858  -2655       O
ATOM   6175  OD2 ASP B 249      61.899 -15.706   7.722  1.00 93.13           O
ANISOU 6175  OD2 ASP B 249    13808   8292  13287   3096    945  -2659       O
ATOM   6176  N   HIS B 250      58.782 -13.217  11.011  1.00 72.50           N
ANISOU 6176  N   HIS B 250    11459   5689  10400   2653    643  -1979       N
ATOM   6177  CA  HIS B 250      57.504 -12.952  11.652  1.00 70.22           C
ANISOU 6177  CA  HIS B 250    11257   5361  10063   2455    571  -1842       C
ATOM   6178  C   HIS B 250      57.010 -11.523  11.428  1.00 72.04           C
ANISOU 6178  C   HIS B 250    11420   5873  10076   2303    590  -1790       C
ATOM   6179  O   HIS B 250      55.900 -11.187  11.859  1.00 69.73           O
ANISOU 6179  O   HIS B 250    11189   5581   9726   2132    539  -1692       O
ATOM   6180  CB  HIS B 250      57.611 -13.283  13.149  1.00 70.33           C
ANISOU 6180  CB  HIS B 250    11290   5228  10203   2483    481  -1606       C
ATOM   6181  CG  HIS B 250      58.622 -12.457  13.884  1.00 75.62           C
ANISOU 6181  CG  HIS B 250    11818   6073  10840   2572    469  -1453       C
ATOM   6182  ND1 HIS B 250      59.975 -12.533  13.630  1.00 74.14           N
ANISOU 6182  ND1 HIS B 250    11518   5944  10708   2766    514  -1513       N
ATOM   6183  CD2 HIS B 250      58.478 -11.553  14.885  1.00 76.76           C
ANISOU 6183  CD2 HIS B 250    11911   6348  10907   2491    416  -1247       C
ATOM   6184  CE1 HIS B 250      60.620 -11.699  14.427  1.00 75.68           C
ANISOU 6184  CE1 HIS B 250    11595   6300  10861   2795    486  -1351       C
ATOM   6185  NE2 HIS B 250      59.734 -11.090  15.198  1.00 77.78           N
ANISOU 6185  NE2 HIS B 250    11897   6610  11043   2631    426  -1191       N
ATOM   6186  N   LEU B 251      57.784 -10.695  10.733  1.00 69.80           N
ANISOU 6186  N   LEU B 251    11015   5827   9679   2360    665  -1858       N
ATOM   6187  CA  LEU B 251      57.416  -9.318  10.428  1.00 66.22           C
ANISOU 6187  CA  LEU B 251    10493   5639   9029   2230    691  -1814       C
ATOM   6188  C   LEU B 251      57.001  -9.190   8.966  1.00 65.27           C
ANISOU 6188  C   LEU B 251    10397   5625   8779   2176    764  -2021       C
ATOM   6189  O   LEU B 251      57.745  -9.590   8.063  1.00 66.43           O
ANISOU 6189  O   LEU B 251    10512   5794   8934   2299    840  -2194       O
ATOM   6190  CB  LEU B 251      58.580  -8.372  10.727  1.00 64.04           C
ANISOU 6190  CB  LEU B 251    10056   5565   8712   2317    722  -1721       C
ATOM   6191  CG  LEU B 251      58.624  -7.743  12.122  1.00 67.53           C
ANISOU 6191  CG  LEU B 251    10451   6039   9170   2278    644  -1483       C
ATOM   6192  CD1 LEU B 251      58.862  -8.787  13.169  1.00 74.84           C
ANISOU 6192  CD1 LEU B 251    11431   6731  10276   2371    570  -1389       C
ATOM   6193  CD2 LEU B 251      59.728  -6.710  12.195  1.00 63.14           C
ANISOU 6193  CD2 LEU B 251     9727   5707   8557   2344    683  -1427       C
ATOM   6194  N   TYR B 252      55.823  -8.619   8.737  1.00 64.85           N
ANISOU 6194  N   TYR B 252    10392   5648   8599   1995    742  -2004       N
ATOM   6195  CA  TYR B 252      55.297  -8.400   7.401  1.00 60.90           C
ANISOU 6195  CA  TYR B 252     9916   5269   7953   1925    797  -2179       C
ATOM   6196  C   TYR B 252      55.069  -6.911   7.198  1.00 60.27           C
ANISOU 6196  C   TYR B 252     9752   5461   7688   1819    818  -2087       C
ATOM   6197  O   TYR B 252      54.541  -6.226   8.082  1.00 63.41           O
ANISOU 6197  O   TYR B 252    10139   5888   8066   1717    759  -1909       O
ATOM   6198  CB  TYR B 252      54.003  -9.186   7.186  1.00 61.58           C
ANISOU 6198  CB  TYR B 252    10145   5186   8066   1804    745  -2265       C
ATOM   6199  CG  TYR B 252      54.251 -10.659   6.945  1.00 62.13           C
ANISOU 6199  CG  TYR B 252    10301   5005   8300   1911    748  -2423       C
ATOM   6200  CD1 TYR B 252      54.453 -11.152   5.670  1.00 64.26           C
ANISOU 6200  CD1 TYR B 252    10593   5294   8529   1970    815  -2669       C
ATOM   6201  CD2 TYR B 252      54.320 -11.548   8.006  1.00 63.83           C
ANISOU 6201  CD2 TYR B 252    10574   4964   8712   1958    686  -2324       C
ATOM   6202  CE1 TYR B 252      54.694 -12.511   5.449  1.00 65.44           C
ANISOU 6202  CE1 TYR B 252    10783   5230   8850   2047    816  -2809       C
ATOM   6203  CE2 TYR B 252      54.560 -12.895   7.805  1.00 68.77           C
ANISOU 6203  CE2 TYR B 252    11272   5349   9507   2055    687  -2459       C
ATOM   6204  CZ  TYR B 252      54.746 -13.378   6.524  1.00 63.91           C
ANISOU 6204  CZ  TYR B 252    10631   4783   8871   2080    751  -2694       C
ATOM   6205  OH  TYR B 252      54.991 -14.723   6.332  1.00 68.11           O
ANISOU 6205  OH  TYR B 252    11174   5110   9593   2137    754  -2809       O
ATOM   6206  N   VAL B 253      55.476  -6.416   6.038  1.00 59.11           N
ANISOU 6206  N   VAL B 253     9545   5508   7405   1848    904  -2208       N
ATOM   6207  CA  VAL B 253      55.379  -4.993   5.720  1.00 63.83           C
ANISOU 6207  CA  VAL B 253    10058   6364   7830   1762    935  -2124       C
ATOM   6208  C   VAL B 253      54.491  -4.849   4.494  1.00 63.99           C
ANISOU 6208  C   VAL B 253    10135   6487   7690   1661    959  -2262       C
ATOM   6209  O   VAL B 253      54.349  -5.796   3.699  1.00 63.51           O
ANISOU 6209  O   VAL B 253    10148   6343   7640   1698    981  -2457       O
ATOM   6210  CB  VAL B 253      56.769  -4.367   5.475  1.00 62.62           C
ANISOU 6210  CB  VAL B 253     9760   6383   7647   1883   1022  -2110       C
ATOM   6211  CG1 VAL B 253      57.588  -4.401   6.753  1.00 57.98           C
ANISOU 6211  CG1 VAL B 253     9107   5715   7208   1970    982  -1959       C
ATOM   6212  CG2 VAL B 253      57.472  -5.107   4.326  1.00 57.55           C
ANISOU 6212  CG2 VAL B 253     9114   5756   6995   2012   1114  -2330       C
ATOM   6213  N   PRO B 254      53.881  -3.677   4.299  1.00 61.02           N
ANISOU 6213  N   PRO B 254     9726   6292   7165   1537    953  -2172       N
ATOM   6214  CA  PRO B 254      53.122  -3.449   3.063  1.00 58.05           C
ANISOU 6214  CA  PRO B 254     9390   6047   6618   1452    977  -2295       C
ATOM   6215  C   PRO B 254      54.030  -3.576   1.851  1.00 61.92           C
ANISOU 6215  C   PRO B 254     9835   6671   7021   1564   1086  -2460       C
ATOM   6216  O   PRO B 254      55.167  -3.096   1.847  1.00 60.22           O
ANISOU 6216  O   PRO B 254     9511   6567   6802   1660   1158  -2416       O
ATOM   6217  CB  PRO B 254      52.592  -2.023   3.225  1.00 57.41           C
ANISOU 6217  CB  PRO B 254     9253   6145   6413   1330    957  -2129       C
ATOM   6218  CG  PRO B 254      52.631  -1.760   4.706  1.00 52.49           C
ANISOU 6218  CG  PRO B 254     8606   5422   5918   1313    893  -1936       C
ATOM   6219  CD  PRO B 254      53.821  -2.522   5.210  1.00 60.63           C
ANISOU 6219  CD  PRO B 254     9605   6332   7099   1468    918  -1955       C
ATOM   6220  N   ALA B 255      53.520  -4.245   0.815  1.00 61.83           N
ANISOU 6220  N   ALA B 255     9904   6652   6937   1549   1099  -2659       N
ATOM   6221  CA  ALA B 255      54.363  -4.545  -0.338  1.00 65.45           C
ANISOU 6221  CA  ALA B 255    10330   7222   7315   1665   1205  -2843       C
ATOM   6222  C   ALA B 255      54.787  -3.276  -1.069  1.00 63.60           C
ANISOU 6222  C   ALA B 255     9993   7284   6888   1650   1287  -2782       C
ATOM   6223  O   ALA B 255      55.866  -3.238  -1.673  1.00 67.53           O
ANISOU 6223  O   ALA B 255    10413   7900   7344   1766   1393  -2856       O
ATOM   6224  CB  ALA B 255      53.640  -5.510  -1.283  1.00 62.64           C
ANISOU 6224  CB  ALA B 255    10088   6800   6911   1640   1193  -3079       C
ATOM   6225  N   GLY B 256      53.972  -2.230  -1.014  1.00 57.20           N
ANISOU 6225  N   GLY B 256     9175   6594   5965   1511   1244  -2643       N
ATOM   6226  CA  GLY B 256      54.214  -1.029  -1.778  1.00 63.93           C
ANISOU 6226  CA  GLY B 256     9945   7716   6629   1481   1315  -2579       C
ATOM   6227  C   GLY B 256      54.905   0.095  -1.041  1.00 63.68           C
ANISOU 6227  C   GLY B 256     9795   7769   6631   1484   1337  -2365       C
ATOM   6228  O   GLY B 256      55.026   1.189  -1.609  1.00 63.50           O
ANISOU 6228  O   GLY B 256     9706   7960   6462   1441   1389  -2286       O
ATOM   6229  N   SER B 257      55.386  -0.140   0.185  1.00 59.64           N
ANISOU 6229  N   SER B 257     9255   7101   6306   1534   1298  -2269       N
ATOM   6230  CA  SER B 257      56.028   0.914   0.967  1.00 58.69           C
ANISOU 6230  CA  SER B 257     9020   7054   6226   1531   1308  -2073       C
ATOM   6231  C   SER B 257      57.193   1.529   0.191  1.00 61.17           C
ANISOU 6231  C   SER B 257     9214   7576   6452   1606   1434  -2085       C
ATOM   6232  O   SER B 257      57.861   0.853  -0.599  1.00 59.18           O
ANISOU 6232  O   SER B 257     8950   7358   6176   1713   1517  -2246       O
ATOM   6233  CB  SER B 257      56.523   0.355   2.302  1.00 57.99           C
ANISOU 6233  CB  SER B 257     8918   6770   6346   1601   1253  -2005       C
ATOM   6234  OG  SER B 257      55.454  -0.146   3.096  1.00 54.33           O
ANISOU 6234  OG  SER B 257     8559   6120   5962   1523   1142  -1969       O
ATOM   6235  N   GLU B 258      57.394   2.837   0.360  1.00 57.26           N
ANISOU 6235  N   GLU B 258     8627   7226   5903   1544   1453  -1919       N
ATOM   6236  CA  GLU B 258      58.512   3.482  -0.324  1.00 56.78           C
ANISOU 6236  CA  GLU B 258     8442   7363   5768   1602   1576  -1909       C
ATOM   6237  C   GLU B 258      59.843   3.009   0.245  1.00 59.17           C
ANISOU 6237  C   GLU B 258     8648   7607   6225   1743   1618  -1927       C
ATOM   6238  O   GLU B 258      60.787   2.725  -0.498  1.00 61.92           O
ANISOU 6238  O   GLU B 258     8930   8053   6542   1848   1727  -2033       O
ATOM   6239  CB  GLU B 258      58.403   5.003  -0.222  1.00 55.02           C
ANISOU 6239  CB  GLU B 258     8144   7288   5471   1495   1581  -1719       C
ATOM   6240  CG  GLU B 258      57.268   5.613  -1.017  1.00 54.90           C
ANISOU 6240  CG  GLU B 258     8198   7381   5280   1373   1562  -1697       C
ATOM   6241  CD  GLU B 258      57.549   5.602  -2.505  1.00 59.93           C
ANISOU 6241  CD  GLU B 258     8826   8211   5733   1404   1673  -1810       C
ATOM   6242  OE1 GLU B 258      58.739   5.720  -2.899  1.00 60.75           O
ANISOU 6242  OE1 GLU B 258     8828   8427   5828   1490   1787  -1831       O
ATOM   6243  OE2 GLU B 258      56.579   5.462  -3.271  1.00 60.48           O
ANISOU 6243  OE2 GLU B 258     8989   8326   5665   1344   1647  -1880       O
ATOM   6244  N   VAL B 259      59.943   2.951   1.568  1.00 57.65           N
ANISOU 6244  N   VAL B 259     8441   7267   6195   1749   1534  -1819       N
ATOM   6245  CA  VAL B 259      61.179   2.624   2.268  1.00 58.40           C
ANISOU 6245  CA  VAL B 259     8434   7310   6445   1876   1553  -1803       C
ATOM   6246  C   VAL B 259      60.830   1.718   3.433  1.00 58.49           C
ANISOU 6246  C   VAL B 259     8524   7079   6621   1905   1439  -1788       C
ATOM   6247  O   VAL B 259      59.868   1.979   4.165  1.00 55.61           O
ANISOU 6247  O   VAL B 259     8229   6630   6270   1798   1340  -1686       O
ATOM   6248  CB  VAL B 259      61.908   3.892   2.772  1.00 58.52           C
ANISOU 6248  CB  VAL B 259     8303   7455   6477   1842   1575  -1633       C
ATOM   6249  CG1 VAL B 259      63.113   3.524   3.599  1.00 54.46           C
ANISOU 6249  CG1 VAL B 259     7682   6882   6130   1968   1575  -1614       C
ATOM   6250  CG2 VAL B 259      62.343   4.755   1.607  1.00 60.93           C
ANISOU 6250  CG2 VAL B 259     8524   7995   6630   1816   1699  -1638       C
ATOM   6251  N   VAL B 260      61.612   0.659   3.611  1.00 57.85           N
ANISOU 6251  N   VAL B 260     8429   6887   6665   2054   1455  -1884       N
ATOM   6252  CA  VAL B 260      61.480  -0.227   4.759  1.00 57.65           C
ANISOU 6252  CA  VAL B 260     8464   6630   6810   2102   1353  -1853       C
ATOM   6253  C   VAL B 260      62.818  -0.236   5.476  1.00 58.91           C
ANISOU 6253  C   VAL B 260     8488   6794   7103   2231   1365  -1793       C
ATOM   6254  O   VAL B 260      63.851  -0.570   4.875  1.00 63.98           O
ANISOU 6254  O   VAL B 260     9044   7501   7764   2360   1458  -1897       O
ATOM   6255  CB  VAL B 260      61.055  -1.646   4.349  1.00 60.78           C
ANISOU 6255  CB  VAL B 260     8990   6848   7255   2166   1341  -2027       C
ATOM   6256  CG1 VAL B 260      60.939  -2.549   5.580  1.00 59.86           C
ANISOU 6256  CG1 VAL B 260     8935   6484   7323   2214   1236  -1971       C
ATOM   6257  CG2 VAL B 260      59.747  -1.604   3.586  1.00 59.08           C
ANISOU 6257  CG2 VAL B 260     8897   6650   6902   2033   1326  -2095       C
ATOM   6258  N   LEU B 261      62.803   0.149   6.743  1.00 55.48           N
ANISOU 6258  N   LEU B 261     8026   6302   6752   2195   1274  -1630       N
ATOM   6259  CA  LEU B 261      63.971   0.072   7.616  1.00 60.18           C
ANISOU 6259  CA  LEU B 261     8500   6880   7484   2312   1256  -1561       C
ATOM   6260  C   LEU B 261      63.784  -1.143   8.509  1.00 60.48           C
ANISOU 6260  C   LEU B 261     8631   6676   7673   2390   1161  -1559       C
ATOM   6261  O   LEU B 261      62.893  -1.156   9.361  1.00 63.67           O
ANISOU 6261  O   LEU B 261     9127   6969   8095   2299   1061  -1458       O
ATOM   6262  CB  LEU B 261      64.125   1.330   8.465  1.00 56.40           C
ANISOU 6262  CB  LEU B 261     7925   6508   6996   2222   1211  -1382       C
ATOM   6263  CG  LEU B 261      63.978   2.659   7.730  1.00 56.48           C
ANISOU 6263  CG  LEU B 261     7875   6727   6859   2101   1282  -1345       C
ATOM   6264  CD1 LEU B 261      64.139   3.800   8.706  1.00 47.43           C
ANISOU 6264  CD1 LEU B 261     6640   5648   5734   2020   1225  -1177       C
ATOM   6265  CD2 LEU B 261      65.027   2.718   6.622  1.00 57.86           C
ANISOU 6265  CD2 LEU B 261     7936   7057   6993   2191   1419  -1450       C
ATOM   6266  N   GLU B 262      64.602  -2.164   8.296  1.00 61.32           N
ANISOU 6266  N   GLU B 262     8715   6700   7885   2558   1196  -1669       N
ATOM   6267  CA  GLU B 262      64.579  -3.379   9.097  1.00 66.63           C
ANISOU 6267  CA  GLU B 262     9466   7132   8717   2655   1113  -1665       C
ATOM   6268  C   GLU B 262      65.672  -3.273  10.151  1.00 65.99           C
ANISOU 6268  C   GLU B 262     9255   7060   8759   2763   1067  -1547       C
ATOM   6269  O   GLU B 262      66.809  -2.908   9.838  1.00 68.12           O
ANISOU 6269  O   GLU B 262     9369   7474   9038   2853   1138  -1574       O
ATOM   6270  CB  GLU B 262      64.775  -4.620   8.218  1.00 65.86           C
ANISOU 6270  CB  GLU B 262     9430   6918   8675   2783   1173  -1867       C
ATOM   6271  CG  GLU B 262      63.796  -4.702   7.041  1.00 69.25           C
ANISOU 6271  CG  GLU B 262     9973   7371   8968   2683   1226  -2010       C
ATOM   6272  CD  GLU B 262      63.740  -6.078   6.377  1.00 73.02           C
ANISOU 6272  CD  GLU B 262    10549   7677   9519   2790   1255  -2211       C
ATOM   6273  OE1 GLU B 262      64.069  -7.079   7.046  1.00 80.93           O
ANISOU 6273  OE1 GLU B 262    11582   8473  10696   2908   1202  -2208       O
ATOM   6274  OE2 GLU B 262      63.360  -6.161   5.189  1.00 67.94           O
ANISOU 6274  OE2 GLU B 262     9953   7103   8758   2757   1328  -2372       O
ATOM   6275  N   GLY B 263      65.315  -3.542  11.394  1.00 60.22           N
ANISOU 6275  N   GLY B 263     8581   6189   8112   2745    948  -1411       N
ATOM   6276  CA  GLY B 263      66.265  -3.384  12.464  1.00 65.55           C
ANISOU 6276  CA  GLY B 263     9137   6884   8886   2834    888  -1287       C
ATOM   6277  C   GLY B 263      65.718  -3.918  13.762  1.00 66.03           C
ANISOU 6277  C   GLY B 263     9296   6763   9030   2820    757  -1151       C
ATOM   6278  O   GLY B 263      64.781  -4.716  13.778  1.00 67.71           O
ANISOU 6278  O   GLY B 263     9667   6794   9265   2782    722  -1175       O
ATOM   6279  N   HIS B 264      66.319  -3.468  14.859  1.00 63.89           N
ANISOU 6279  N   HIS B 264     8925   6547   8801   2846    684  -1007       N
ATOM   6280  CA  HIS B 264      65.971  -4.006  16.162  1.00 66.53           C
ANISOU 6280  CA  HIS B 264     9337   6726   9213   2855    559   -866       C
ATOM   6281  C   HIS B 264      66.177  -2.946  17.229  1.00 64.02           C
ANISOU 6281  C   HIS B 264     8926   6549   8852   2785    487   -706       C
ATOM   6282  O   HIS B 264      67.021  -2.059  17.093  1.00 66.85           O
ANISOU 6282  O   HIS B 264     9125   7094   9181   2797    523   -707       O
ATOM   6283  CB  HIS B 264      66.791  -5.261  16.516  1.00 64.47           C
ANISOU 6283  CB  HIS B 264     9069   6302   9124   3060    525   -877       C
ATOM   6284  CG  HIS B 264      68.276  -5.048  16.563  1.00 67.64           C
ANISOU 6284  CG  HIS B 264     9276   6832   9591   3213    547   -885       C
ATOM   6285  ND1 HIS B 264      69.102  -5.325  15.493  1.00 68.52           N
ANISOU 6285  ND1 HIS B 264     9303   6994   9739   3334    655  -1045       N
ATOM   6286  CD2 HIS B 264      69.089  -4.623  17.562  1.00 71.00           C
ANISOU 6286  CD2 HIS B 264     9572   7348  10056   3266    473   -759       C
ATOM   6287  CE1 HIS B 264      70.355  -5.061  15.822  1.00 64.10           C
ANISOU 6287  CE1 HIS B 264     8562   6550   9242   3454    651  -1012       C
ATOM   6288  NE2 HIS B 264      70.375  -4.638  17.074  1.00 66.50           N
ANISOU 6288  NE2 HIS B 264     8836   6880   9551   3415    536   -841       N
ATOM   6289  N   ILE B 265      65.385  -3.051  18.292  1.00 65.74           N
ANISOU 6289  N   ILE B 265     9241   6673   9063   2708    386   -574       N
ATOM   6290  CA  ILE B 265      65.625  -2.261  19.486  1.00 65.57           C
ANISOU 6290  CA  ILE B 265     9141   6757   9015   2667    299   -423       C
ATOM   6291  C   ILE B 265      66.893  -2.777  20.153  1.00 69.37           C
ANISOU 6291  C   ILE B 265     9513   7226   9619   2851    244   -373       C
ATOM   6292  O   ILE B 265      67.080  -3.993  20.312  1.00 63.95           O
ANISOU 6292  O   ILE B 265     8889   6362   9047   2981    215   -375       O
ATOM   6293  CB  ILE B 265      64.415  -2.326  20.429  1.00 64.95           C
ANISOU 6293  CB  ILE B 265     9203   6584   8892   2543    213   -300       C
ATOM   6294  CG1 ILE B 265      63.148  -1.848  19.707  1.00 64.90           C
ANISOU 6294  CG1 ILE B 265     9296   6590   8772   2369    267   -358       C
ATOM   6295  CG2 ILE B 265      64.681  -1.530  21.718  1.00 67.02           C
ANISOU 6295  CG2 ILE B 265     9385   6962   9119   2507    120   -152       C
ATOM   6296  CD1 ILE B 265      61.961  -1.574  20.635  1.00 67.25           C
ANISOU 6296  CD1 ILE B 265     9697   6853   9004   2223    194   -236       C
ATOM   6297  N   ILE B 266      67.798  -1.864  20.497  1.00 68.15           N
ANISOU 6297  N   ILE B 266     9188   7257   9448   2865    231   -335       N
ATOM   6298  CA  ILE B 266      69.070  -2.271  21.095  1.00 70.25           C
ANISOU 6298  CA  ILE B 266     9325   7539   9828   3042    176   -293       C
ATOM   6299  C   ILE B 266      68.833  -2.471  22.587  1.00 70.01           C
ANISOU 6299  C   ILE B 266     9342   7451   9806   3039     34   -121       C
ATOM   6300  O   ILE B 266      68.379  -1.545  23.274  1.00 67.96           O
ANISOU 6300  O   ILE B 266     9078   7296   9449   2904    -16    -36       O
ATOM   6301  CB  ILE B 266      70.181  -1.249  20.808  1.00 67.59           C
ANISOU 6301  CB  ILE B 266     8774   7429   9478   3058    222   -330       C
ATOM   6302  CG1 ILE B 266      70.163  -0.873  19.326  1.00 66.37           C
ANISOU 6302  CG1 ILE B 266     8594   7351   9273   3015    370   -482       C
ATOM   6303  CG2 ILE B 266      71.536  -1.831  21.183  1.00 65.24           C
ANISOU 6303  CG2 ILE B 266     8336   7141   9313   3262    182   -319       C
ATOM   6304  CD1 ILE B 266      71.353  -0.079  18.876  1.00 66.76           C
ANISOU 6304  CD1 ILE B 266     8430   7603   9332   3054    437   -531       C
ATOM   6305  N   PRO B 267      69.072  -3.672  23.109  1.00 68.56           N
ANISOU 6305  N   PRO B 267     9215   7100   9736   3182    -31    -66       N
ATOM   6306  CA  PRO B 267      68.696  -3.963  24.500  1.00 75.71           C
ANISOU 6306  CA  PRO B 267    10194   7937  10636   3171   -162    109       C
ATOM   6307  C   PRO B 267      69.520  -3.150  25.485  1.00 77.36           C
ANISOU 6307  C   PRO B 267    10244   8334  10815   3189   -250    205       C
ATOM   6308  O   PRO B 267      70.725  -2.954  25.306  1.00 79.07           O
ANISOU 6308  O   PRO B 267    10289   8662  11093   3304   -240    162       O
ATOM   6309  CB  PRO B 267      68.992  -5.462  24.659  1.00 80.00           C
ANISOU 6309  CB  PRO B 267    10809   8258  11329   3350   -199    135       C
ATOM   6310  CG  PRO B 267      69.331  -5.975  23.318  1.00 79.92           C
ANISOU 6310  CG  PRO B 267    10787   8183  11396   3437    -83    -43       C
ATOM   6311  CD  PRO B 267      69.523  -4.856  22.359  1.00 72.79           C
ANISOU 6311  CD  PRO B 267     9774   7481  10401   3348     22   -168       C
ATOM   6312  N   ARG B 268      68.858  -2.706  26.556  1.00 77.77           N
ANISOU 6312  N   ARG B 268    10354   8422  10773   3076   -337    334       N
ATOM   6313  CA  ARG B 268      69.498  -2.075  27.714  1.00 80.85           C
ANISOU 6313  CA  ARG B 268    10623   8970  11127   3090   -446    442       C
ATOM   6314  C   ARG B 268      70.160  -0.743  27.370  1.00 77.56           C
ANISOU 6314  C   ARG B 268    10025   8782  10662   3028   -405    363       C
ATOM   6315  O   ARG B 268      71.056  -0.286  28.082  1.00 76.09           O
ANISOU 6315  O   ARG B 268     9691   8736  10483   3078   -483    411       O
ATOM   6316  CB  ARG B 268      70.518  -3.014  28.375  1.00 76.22           C
ANISOU 6316  CB  ARG B 268     9975   8328  10659   3299   -538    523       C
ATOM   6317  CG  ARG B 268      70.029  -4.437  28.554  1.00 83.73           C
ANISOU 6317  CG  ARG B 268    11094   9026  11693   3386   -566    592       C
ATOM   6318  CD  ARG B 268      71.014  -5.291  29.368  1.00 89.41           C
ANISOU 6318  CD  ARG B 268    11752   9697  12523   3593   -676    702       C
ATOM   6319  NE  ARG B 268      71.175  -4.786  30.726  1.00 93.50           N
ANISOU 6319  NE  ARG B 268    12220  10352  12953   3567   -807    853       N
ATOM   6320  CZ  ARG B 268      70.235  -4.835  31.660  1.00 93.79           C
ANISOU 6320  CZ  ARG B 268    12392  10351  12894   3464   -874    990       C
ATOM   6321  NH1 ARG B 268      69.055  -5.389  31.429  1.00 91.73           N
ANISOU 6321  NH1 ARG B 268    12322   9910  12621   3376   -828   1005       N
ATOM   6322  NH2 ARG B 268      70.480  -4.302  32.854  1.00 93.48           N
ANISOU 6322  NH2 ARG B 268    12289  10466  12764   3446   -990   1109       N
ATOM   6323  N   VAL B 269      69.715  -0.082  26.309  1.00 76.03           N
ANISOU 6323  N   VAL B 269     9840   8631  10417   2912   -289    249       N
ATOM   6324  CA  VAL B 269      70.262   1.207  25.909  1.00 72.32           C
ANISOU 6324  CA  VAL B 269     9209   8363   9905   2837   -240    181       C
ATOM   6325  C   VAL B 269      69.166   2.245  26.058  1.00 72.51           C
ANISOU 6325  C   VAL B 269     9307   8446   9799   2630   -231    198       C
ATOM   6326  O   VAL B 269      68.046   2.043  25.573  1.00 74.87           O
ANISOU 6326  O   VAL B 269     9757   8640  10048   2541   -179    175       O
ATOM   6327  CB  VAL B 269      70.806   1.184  24.470  1.00 68.80           C
ANISOU 6327  CB  VAL B 269     8688   7939   9512   2887   -103     36       C
ATOM   6328  CG1 VAL B 269      71.207   2.578  24.037  1.00 63.78           C
ANISOU 6328  CG1 VAL B 269     7905   7504   8824   2780    -44    -18       C
ATOM   6329  CG2 VAL B 269      71.997   0.239  24.379  1.00 66.90           C
ANISOU 6329  CG2 VAL B 269     8349   7661   9409   3103   -113     12       C
ATOM   6330  N   ARG B 270      69.483   3.336  26.755  1.00 70.93           N
ANISOU 6330  N   ARG B 270     8995   8408   9547   2556   -287    235       N
ATOM   6331  CA  ARG B 270      68.591   4.479  26.908  1.00 64.80           C
ANISOU 6331  CA  ARG B 270     8258   7706   8658   2367   -278    240       C
ATOM   6332  C   ARG B 270      69.380   5.757  26.664  1.00 64.87           C
ANISOU 6332  C   ARG B 270     8084   7898   8665   2310   -248    186       C
ATOM   6333  O   ARG B 270      70.411   5.979  27.309  1.00 64.37           O
ANISOU 6333  O   ARG B 270     7873   7940   8645   2377   -320    210       O
ATOM   6334  CB  ARG B 270      67.968   4.513  28.295  1.00 67.05           C
ANISOU 6334  CB  ARG B 270     8622   7986   8870   2315   -397    358       C
ATOM   6335  CG  ARG B 270      67.084   3.346  28.596  1.00 69.49           C
ANISOU 6335  CG  ARG B 270     9114   8114   9174   2343   -423    428       C
ATOM   6336  CD  ARG B 270      65.800   3.397  27.814  1.00 69.50           C
ANISOU 6336  CD  ARG B 270     9259   8026   9121   2218   -335    380       C
ATOM   6337  NE  ARG B 270      64.893   2.366  28.297  1.00 73.54           N
ANISOU 6337  NE  ARG B 270     9942   8375   9625   2222   -373    461       N
ATOM   6338  CZ  ARG B 270      65.015   1.075  28.020  1.00 76.59           C
ANISOU 6338  CZ  ARG B 270    10401   8599  10103   2340   -367    467       C
ATOM   6339  NH1 ARG B 270      65.983   0.625  27.240  1.00 75.88           N
ANISOU 6339  NH1 ARG B 270    10230   8488  10114   2472   -320    388       N
ATOM   6340  NH2 ARG B 270      64.148   0.216  28.543  1.00 78.85           N
ANISOU 6340  NH2 ARG B 270    10841   8735  10382   2325   -405    554       N
ATOM   6341  N   THR B 271      68.890   6.598  25.747  1.00 63.02           N
ANISOU 6341  N   THR B 271     7858   7703   8383   2185   -148    117       N
ATOM   6342  CA  THR B 271      69.585   7.822  25.374  1.00 61.57           C
ANISOU 6342  CA  THR B 271     7510   7677   8207   2119   -103     67       C
ATOM   6343  C   THR B 271      68.585   8.959  25.234  1.00 59.21           C
ANISOU 6343  C   THR B 271     7270   7412   7816   1934    -71     62       C
ATOM   6344  O   THR B 271      67.383   8.742  25.057  1.00 62.62           O
ANISOU 6344  O   THR B 271     7863   7747   8183   1866    -51     72       O
ATOM   6345  CB  THR B 271      70.368   7.676  24.062  1.00 62.90           C
ANISOU 6345  CB  THR B 271     7585   7875   8441   2188     20    -25       C
ATOM   6346  OG1 THR B 271      69.496   7.164  23.048  1.00 64.11           O
ANISOU 6346  OG1 THR B 271     7883   7919   8557   2168    113    -74       O
ATOM   6347  CG2 THR B 271      71.551   6.734  24.246  1.00 64.11           C
ANISOU 6347  CG2 THR B 271     7635   8023   8700   2378    -13    -28       C
ATOM   6348  N   VAL B 272      69.113  10.184  25.288  1.00 53.84           N
ANISOU 6348  N   VAL B 272     6449   6866   7140   1855    -65     43       N
ATOM   6349  CA  VAL B 272      68.276  11.369  25.228  1.00 53.26           C
ANISOU 6349  CA  VAL B 272     6413   6827   6997   1686    -43     40       C
ATOM   6350  C   VAL B 272      67.559  11.417  23.884  1.00 54.54           C
ANISOU 6350  C   VAL B 272     6662   6937   7124   1629     83     -7       C
ATOM   6351  O   VAL B 272      68.191  11.431  22.818  1.00 52.00           O
ANISOU 6351  O   VAL B 272     6263   6653   6840   1665    182    -62       O
ATOM   6352  CB  VAL B 272      69.119  12.625  25.445  1.00 55.72           C
ANISOU 6352  CB  VAL B 272     6546   7281   7345   1620    -54     22       C
ATOM   6353  CG1 VAL B 272      68.215  13.842  25.518  1.00 49.72           C
ANISOU 6353  CG1 VAL B 272     5831   6539   6521   1451    -44     23       C
ATOM   6354  CG2 VAL B 272      70.028  12.488  26.669  1.00 50.42           C
ANISOU 6354  CG2 VAL B 272     5763   6680   6715   1695   -180     55       C
ATOM   6355  N   GLU B 273      66.231  11.459  23.934  1.00 51.78           N
ANISOU 6355  N   GLU B 273     6468   6511   6695   1541     80     13       N
ATOM   6356  CA  GLU B 273      65.360  11.565  22.772  1.00 43.85           C
ANISOU 6356  CA  GLU B 273     5560   5462   5640   1472    181    -25       C
ATOM   6357  C   GLU B 273      64.460  12.789  22.940  1.00 45.96           C
ANISOU 6357  C   GLU B 273     5858   5762   5844   1316    177     -5       C
ATOM   6358  O   GLU B 273      64.025  13.109  24.052  1.00 42.30           O
ANISOU 6358  O   GLU B 273     5421   5298   5352   1267     88     39       O
ATOM   6359  CB  GLU B 273      64.532  10.295  22.635  1.00 44.05           C
ANISOU 6359  CB  GLU B 273     5749   5347   5640   1524    177    -23       C
ATOM   6360  CG  GLU B 273      63.753  10.163  21.372  1.00 48.37           C
ANISOU 6360  CG  GLU B 273     6391   5848   6140   1479    275    -76       C
ATOM   6361  CD  GLU B 273      62.415  10.879  21.440  1.00 48.72           C
ANISOU 6361  CD  GLU B 273     6533   5878   6101   1334    269    -51       C
ATOM   6362  OE1 GLU B 273      61.900  11.140  22.556  1.00 48.15           O
ANISOU 6362  OE1 GLU B 273     6495   5795   6004   1283    185      7       O
ATOM   6363  OE2 GLU B 273      61.901  11.220  20.358  1.00 48.17           O
ANISOU 6363  OE2 GLU B 273     6498   5818   5985   1274    350    -90       O
ATOM   6364  N   GLY B 274      64.205  13.493  21.847  1.00 46.96           N
ANISOU 6364  N   GLY B 274     5977   5920   5946   1241    272    -37       N
ATOM   6365  CA  GLY B 274      63.401  14.683  21.904  1.00 42.59           C
ANISOU 6365  CA  GLY B 274     5445   5390   5346   1102    274    -19       C
ATOM   6366  C   GLY B 274      64.194  15.876  22.375  1.00 45.16           C
ANISOU 6366  C   GLY B 274     5621   5815   5721   1048    251    -11       C
ATOM   6367  O   GLY B 274      65.423  15.810  22.513  1.00 44.52           O
ANISOU 6367  O   GLY B 274     5407   5799   5710   1115    244    -24       O
ATOM   6368  N   PRO B 275      63.513  17.008  22.629  1.00 44.80           N
ANISOU 6368  N   PRO B 275     5589   5783   5650    927    237      4       N
ATOM   6369  CA  PRO B 275      62.061  17.229  22.551  1.00 45.82           C
ANISOU 6369  CA  PRO B 275     5856   5849   5704    844    239     20       C
ATOM   6370  C   PRO B 275      61.490  17.098  21.160  1.00 45.03           C
ANISOU 6370  C   PRO B 275     5826   5722   5561    824    339      6       C
ATOM   6371  O   PRO B 275      62.248  17.129  20.183  1.00 46.71           O
ANISOU 6371  O   PRO B 275     5967   5982   5799    854    420    -15       O
ATOM   6372  CB  PRO B 275      61.873  18.677  23.029  1.00 48.57           C
ANISOU 6372  CB  PRO B 275     6149   6240   6067    730    213     28       C
ATOM   6373  CG  PRO B 275      63.207  19.202  23.388  1.00 47.76           C
ANISOU 6373  CG  PRO B 275     5883   6219   6046    744    194     15       C
ATOM   6374  CD  PRO B 275      64.260  18.229  22.979  1.00 43.37           C
ANISOU 6374  CD  PRO B 275     5264   5686   5528    863    222      1       C
ATOM   6375  N   PHE B 276      60.169  16.932  21.074  1.00 44.57           N
ANISOU 6375  N   PHE B 276     5902   5598   5434    776    332     16       N
ATOM   6376  CA  PHE B 276      59.482  16.880  19.788  1.00 43.56           C
ANISOU 6376  CA  PHE B 276     5846   5453   5253    746    415      2       C
ATOM   6377  C   PHE B 276      58.046  17.329  19.992  1.00 40.58           C
ANISOU 6377  C   PHE B 276     5570   5033   4817    654    387     24       C
ATOM   6378  O   PHE B 276      57.518  17.264  21.103  1.00 39.32           O
ANISOU 6378  O   PHE B 276     5451   4840   4649    635    310     43       O
ATOM   6379  CB  PHE B 276      59.520  15.470  19.178  1.00 43.89           C
ANISOU 6379  CB  PHE B 276     5959   5443   5275    841    446    -36       C
ATOM   6380  CG  PHE B 276      59.025  15.399  17.756  1.00 41.10           C
ANISOU 6380  CG  PHE B 276     5660   5094   4861    820    534    -66       C
ATOM   6381  CD1 PHE B 276      59.776  15.924  16.716  1.00 41.38           C
ANISOU 6381  CD1 PHE B 276     5609   5214   4900    821    624    -80       C
ATOM   6382  CD2 PHE B 276      57.802  14.807  17.464  1.00 41.39           C
ANISOU 6382  CD2 PHE B 276     5834   5060   4833    795    526    -79       C
ATOM   6383  CE1 PHE B 276      59.321  15.841  15.405  1.00 41.78           C
ANISOU 6383  CE1 PHE B 276     5712   5284   4878    805    703   -106       C
ATOM   6384  CE2 PHE B 276      57.330  14.740  16.157  1.00 41.13           C
ANISOU 6384  CE2 PHE B 276     5850   5043   4735    775    599   -112       C
ATOM   6385  CZ  PHE B 276      58.091  15.248  15.131  1.00 41.55           C
ANISOU 6385  CZ  PHE B 276     5821   5186   4779    783    686   -125       C
ATOM   6386  N   GLY B 277      57.418  17.785  18.910  1.00 39.52           N
ANISOU 6386  N   GLY B 277     5471   4908   4637    599    451     24       N
ATOM   6387  CA  GLY B 277      56.042  18.242  19.007  1.00 38.79           C
ANISOU 6387  CA  GLY B 277     5464   4781   4493    516    428     45       C
ATOM   6388  C   GLY B 277      55.063  17.110  19.264  1.00 41.03           C
ANISOU 6388  C   GLY B 277     5874   4988   4728    534    392     32       C
ATOM   6389  O   GLY B 277      55.280  15.957  18.874  1.00 45.38           O
ANISOU 6389  O   GLY B 277     6468   5502   5271    604    409      1       O
ATOM   6390  N   GLU B 278      53.958  17.455  19.922  1.00 40.86           N
ANISOU 6390  N   GLU B 278     5908   4937   4679    468    344     55       N
ATOM   6391  CA  GLU B 278      52.869  16.516  20.170  1.00 45.09           C
ANISOU 6391  CA  GLU B 278     6560   5402   5169    462    313     51       C
ATOM   6392  C   GLU B 278      51.551  17.143  19.708  1.00 42.65           C
ANISOU 6392  C   GLU B 278     6302   5093   4810    376    323     60       C
ATOM   6393  O   GLU B 278      51.461  18.351  19.453  1.00 39.56           O
ANISOU 6393  O   GLU B 278     5858   4747   4424    324    341     77       O
ATOM   6394  CB  GLU B 278      52.835  16.091  21.662  1.00 47.64           C
ANISOU 6394  CB  GLU B 278     6900   5695   5508    479    235     76       C
ATOM   6395  CG  GLU B 278      54.155  15.392  22.094  1.00 51.14           C
ANISOU 6395  CG  GLU B 278     7290   6138   6002    576    217     74       C
ATOM   6396  CD  GLU B 278      54.158  14.847  23.520  1.00 61.26           C
ANISOU 6396  CD  GLU B 278     8595   7395   7287    603    137    110       C
ATOM   6397  OE1 GLU B 278      54.003  15.643  24.479  1.00 64.82           O
ANISOU 6397  OE1 GLU B 278     9011   7889   7730    558     91    130       O
ATOM   6398  OE2 GLU B 278      54.361  13.623  23.687  1.00 66.04           O
ANISOU 6398  OE2 GLU B 278     9251   7937   7903    674    120    118       O
ATOM   6399  N   PHE B 279      50.530  16.295  19.567  1.00 40.76           N
ANISOU 6399  N   PHE B 279     6162   4798   4527    362    312     48       N
ATOM   6400  CA  PHE B 279      49.269  16.759  18.994  1.00 39.68           C
ANISOU 6400  CA  PHE B 279     6069   4666   4340    288    321     51       C
ATOM   6401  C   PHE B 279      48.534  17.814  19.836  1.00 38.70           C
ANISOU 6401  C   PHE B 279     5924   4561   4221    221    284     84       C
ATOM   6402  O   PHE B 279      47.716  18.545  19.257  1.00 35.41           O
ANISOU 6402  O   PHE B 279     5512   4165   3778    167    298     93       O
ATOM   6403  CB  PHE B 279      48.376  15.542  18.667  1.00 39.14           C
ANISOU 6403  CB  PHE B 279     6105   4534   4232    284    314     22       C
ATOM   6404  CG  PHE B 279      47.821  14.823  19.872  1.00 40.83           C
ANISOU 6404  CG  PHE B 279     6373   4685   4455    274    259     42       C
ATOM   6405  CD1 PHE B 279      46.630  15.235  20.464  1.00 40.03           C
ANISOU 6405  CD1 PHE B 279     6295   4585   4330    201    229     67       C
ATOM   6406  CD2 PHE B 279      48.459  13.698  20.383  1.00 42.89           C
ANISOU 6406  CD2 PHE B 279     6662   4886   4749    340    241     40       C
ATOM   6407  CE1 PHE B 279      46.102  14.573  21.579  1.00 38.99           C
ANISOU 6407  CE1 PHE B 279     6211   4405   4199    186    186     93       C
ATOM   6408  CE2 PHE B 279      47.934  13.026  21.508  1.00 41.48           C
ANISOU 6408  CE2 PHE B 279     6537   4651   4574    328    193     75       C
ATOM   6409  CZ  PHE B 279      46.747  13.480  22.097  1.00 41.74           C
ANISOU 6409  CZ  PHE B 279     6591   4696   4574    246    168    103       C
ATOM   6410  N   PRO B 280      48.737  17.948  21.154  1.00 40.37           N
ANISOU 6410  N   PRO B 280     6111   4767   4459    223    237    101       N
ATOM   6411  CA  PRO B 280      48.165  19.111  21.853  1.00 35.91           C
ANISOU 6411  CA  PRO B 280     5511   4230   3901    165    211    116       C
ATOM   6412  C   PRO B 280      48.781  20.448  21.472  1.00 39.77           C
ANISOU 6412  C   PRO B 280     5912   4763   4435    148    236    121       C
ATOM   6413  O   PRO B 280      48.303  21.479  21.975  1.00 34.60           O
ANISOU 6413  O   PRO B 280     5229   4121   3798    101    217    127       O
ATOM   6414  CB  PRO B 280      48.412  18.794  23.315  1.00 33.91           C
ANISOU 6414  CB  PRO B 280     5255   3974   3657    182    156    125       C
ATOM   6415  CG  PRO B 280      48.468  17.272  23.340  1.00 39.55           C
ANISOU 6415  CG  PRO B 280     6041   4634   4351    230    149    129       C
ATOM   6416  CD  PRO B 280      49.223  16.938  22.113  1.00 36.53           C
ANISOU 6416  CD  PRO B 280     5646   4247   3985    276    198    106       C
ATOM   6417  N   GLY B 281      49.797  20.465  20.598  1.00 38.66           N
ANISOU 6417  N   GLY B 281     5727   4645   4316    183    281    119       N
ATOM   6418  CA  GLY B 281      50.337  21.698  20.045  1.00 37.33           C
ANISOU 6418  CA  GLY B 281     5479   4514   4191    157    316    136       C
ATOM   6419  C   GLY B 281      51.556  22.290  20.736  1.00 39.49           C
ANISOU 6419  C   GLY B 281     5653   4815   4537    169    302    131       C
ATOM   6420  O   GLY B 281      51.921  23.433  20.427  1.00 36.95           O
ANISOU 6420  O   GLY B 281     5261   4512   4265    132    327    147       O
ATOM   6421  N   SER B 282      52.208  21.549  21.625  1.00 37.06           N
ANISOU 6421  N   SER B 282     5334   4508   4241    219    263    114       N
ATOM   6422  CA  SER B 282      53.421  21.983  22.296  1.00 41.34           C
ANISOU 6422  CA  SER B 282     5776   5085   4848    236    240    103       C
ATOM   6423  C   SER B 282      54.494  20.889  22.208  1.00 39.76           C
ANISOU 6423  C   SER B 282     5554   4897   4657    322    245     94       C
ATOM   6424  O   SER B 282      54.230  19.764  21.784  1.00 41.21           O
ANISOU 6424  O   SER B 282     5811   5048   4797    368    260     91       O
ATOM   6425  CB  SER B 282      53.113  22.367  23.762  1.00 41.49           C
ANISOU 6425  CB  SER B 282     5788   5107   4871    211    164     89       C
ATOM   6426  OG  SER B 282      52.576  21.269  24.467  1.00 42.87           O
ANISOU 6426  OG  SER B 282     6043   5259   4988    244    123     93       O
ATOM   6427  N   TYR B 283      55.729  21.245  22.573  1.00 36.09           N
ANISOU 6427  N   TYR B 283     4981   4476   4255    344    234     85       N
ATOM   6428  CA  TYR B 283      56.831  20.287  22.652  1.00 41.18           C
ANISOU 6428  CA  TYR B 283     5586   5139   4922    434    229     75       C
ATOM   6429  C   TYR B 283      56.693  19.359  23.853  1.00 41.80           C
ANISOU 6429  C   TYR B 283     5714   5195   4974    484    149     78       C
ATOM   6430  O   TYR B 283      56.330  19.784  24.948  1.00 42.76           O
ANISOU 6430  O   TYR B 283     5838   5326   5084    448     85     80       O
ATOM   6431  CB  TYR B 283      58.175  21.011  22.785  1.00 44.74           C
ANISOU 6431  CB  TYR B 283     5891   5654   5454    437    232     64       C
ATOM   6432  CG  TYR B 283      58.626  21.739  21.557  1.00 46.64           C
ANISOU 6432  CG  TYR B 283     6067   5925   5729    404    321     73       C
ATOM   6433  CD1 TYR B 283      59.291  21.071  20.525  1.00 45.18           C
ANISOU 6433  CD1 TYR B 283     5862   5763   5542    465    393     68       C
ATOM   6434  CD2 TYR B 283      58.372  23.103  21.414  1.00 44.05           C
ANISOU 6434  CD2 TYR B 283     5700   5602   5437    311    337     87       C
ATOM   6435  CE1 TYR B 283      59.704  21.757  19.386  1.00 45.49           C
ANISOU 6435  CE1 TYR B 283     5839   5844   5601    431    482     84       C
ATOM   6436  CE2 TYR B 283      58.776  23.789  20.286  1.00 47.15           C
ANISOU 6436  CE2 TYR B 283     6035   6021   5859    276    421    111       C
ATOM   6437  CZ  TYR B 283      59.445  23.113  19.271  1.00 46.01           C
ANISOU 6437  CZ  TYR B 283     5869   5914   5700    334    496    113       C
ATOM   6438  OH  TYR B 283      59.854  23.815  18.152  1.00 46.57           O
ANISOU 6438  OH  TYR B 283     5881   6025   5790    296    586    145       O
ATOM   6439  N   SER B 284      57.036  18.092  23.653  1.00 45.90           N
ANISOU 6439  N   SER B 284     6270   5685   5485    569    154     80       N
ATOM   6440  CA  SER B 284      57.290  17.183  24.770  1.00 46.58           C
ANISOU 6440  CA  SER B 284     6377   5755   5565    635     78     97       C
ATOM   6441  C   SER B 284      58.615  17.529  25.458  1.00 46.29           C
ANISOU 6441  C   SER B 284     6210   5791   5587    676     33     91       C
ATOM   6442  O   SER B 284      59.363  18.416  25.042  1.00 49.46           O
ANISOU 6442  O   SER B 284     6502   6248   6042    650     65     69       O
ATOM   6443  CB  SER B 284      57.355  15.748  24.279  1.00 49.71           C
ANISOU 6443  CB  SER B 284     6845   6086   5957    721     99     99       C
ATOM   6444  OG  SER B 284      58.657  15.535  23.748  1.00 49.97           O
ANISOU 6444  OG  SER B 284     6782   6154   6050    799    132     77       O
ATOM   6445  N   GLY B 285      58.924  16.824  26.506  1.00 49.16           N
ANISOU 6445  N   GLY B 285     6579   6156   5942    737    -44    113       N
ATOM   6446  CA  GLY B 285      60.213  17.008  27.131  1.00 54.07           C
ANISOU 6446  CA  GLY B 285     7075   6852   6617    787    -96    107       C
ATOM   6447  C   GLY B 285      61.216  15.993  26.636  1.00 49.45           C
ANISOU 6447  C   GLY B 285     6450   6256   6082    905    -75    107       C
ATOM   6448  O   GLY B 285      60.839  14.996  26.038  1.00 50.92           O
ANISOU 6448  O   GLY B 285     6728   6366   6255    953    -37    115       O
ATOM   6449  N   ALA B 286      62.497  16.255  26.886  1.00 48.49           N
ANISOU 6449  N   ALA B 286     6188   6212   6025    950   -102     93       N
ATOM   6450  CA  ALA B 286      63.516  15.254  26.600  1.00 46.18           C
ANISOU 6450  CA  ALA B 286     5844   5917   5786   1078    -96     94       C
ATOM   6451  C   ALA B 286      63.481  14.159  27.663  1.00 47.05           C
ANISOU 6451  C   ALA B 286     6016   5989   5872   1166   -189    145       C
ATOM   6452  O   ALA B 286      63.277  14.424  28.848  1.00 48.55           O
ANISOU 6452  O   ALA B 286     6211   6216   6020   1138   -279    174       O
ATOM   6453  CB  ALA B 286      64.906  15.886  26.526  1.00 43.45           C
ANISOU 6453  CB  ALA B 286     5313   5673   5522   1098    -94     63       C
ATOM   6454  N   ARG B 287      63.628  12.917  27.215  1.00 45.57           N
ANISOU 6454  N   ARG B 287     5884   5724   5707   1270   -166    157       N
ATOM   6455  CA  ARG B 287      63.651  11.761  28.086  1.00 48.68           C
ANISOU 6455  CA  ARG B 287     6340   6062   6093   1365   -246    217       C
ATOM   6456  C   ARG B 287      64.713  10.804  27.571  1.00 51.21           C
ANISOU 6456  C   ARG B 287     6603   6356   6498   1510   -226    204       C
ATOM   6457  O   ARG B 287      65.125  10.879  26.410  1.00 52.79           O
ANISOU 6457  O   ARG B 287     6753   6562   6744   1527   -132    144       O
ATOM   6458  CB  ARG B 287      62.296  11.059  28.143  1.00 51.42           C
ANISOU 6458  CB  ARG B 287     6868   6292   6377   1331   -239    255       C
ATOM   6459  CG  ARG B 287      61.163  11.926  28.615  1.00 47.90           C
ANISOU 6459  CG  ARG B 287     6483   5869   5849   1196   -252    265       C
ATOM   6460  CD  ARG B 287      61.280  12.177  30.094  1.00 54.71           C
ANISOU 6460  CD  ARG B 287     7319   6802   6666   1191   -359    315       C
ATOM   6461  NE  ARG B 287      60.086  12.829  30.610  1.00 58.65           N
ANISOU 6461  NE  ARG B 287     7892   7312   7080   1073   -369    323       N
ATOM   6462  CZ  ARG B 287      59.908  14.138  30.692  1.00 57.03           C
ANISOU 6462  CZ  ARG B 287     7629   7183   6858    976   -362    276       C
ATOM   6463  NH1 ARG B 287      60.855  14.988  30.330  1.00 58.34           N
ANISOU 6463  NH1 ARG B 287     7659   7423   7085    970   -348    223       N
ATOM   6464  NH2 ARG B 287      58.743  14.603  31.128  1.00 55.14           N
ANISOU 6464  NH2 ARG B 287     7465   6941   6545    882   -365    282       N
ATOM   6465  N   LEU B 288      65.157   9.910  28.453  1.00 48.88           N
ANISOU 6465  N   LEU B 288     6312   6038   6223   1618   -313    263       N
ATOM   6466  CA  LEU B 288      66.023   8.796  28.068  1.00 57.62           C
ANISOU 6466  CA  LEU B 288     7387   7090   7415   1774   -303    260       C
ATOM   6467  C   LEU B 288      65.126   7.705  27.493  1.00 59.73           C
ANISOU 6467  C   LEU B 288     7822   7195   7676   1796   -254    265       C
ATOM   6468  O   LEU B 288      64.301   7.128  28.211  1.00 59.40           O
ANISOU 6468  O   LEU B 288     7908   7071   7590   1782   -308    336       O
ATOM   6469  CB  LEU B 288      66.832   8.286  29.263  1.00 51.99           C
ANISOU 6469  CB  LEU B 288     6613   6414   6728   1884   -425    332       C
ATOM   6470  CG  LEU B 288      67.973   9.186  29.734  1.00 51.81           C
ANISOU 6470  CG  LEU B 288     6398   6554   6734   1890   -478    312       C
ATOM   6471  CD1 LEU B 288      68.613   8.683  31.008  1.00 53.17           C
ANISOU 6471  CD1 LEU B 288     6523   6768   6909   1991   -614    391       C
ATOM   6472  CD2 LEU B 288      69.034   9.310  28.667  1.00 56.09           C
ANISOU 6472  CD2 LEU B 288     6798   7140   7372   1950   -395    234       C
ATOM   6473  N   GLN B 289      65.244   7.459  26.192  1.00 58.77           N
ANISOU 6473  N   GLN B 289     7701   7032   7595   1821   -149    187       N
ATOM   6474  CA  GLN B 289      64.390   6.513  25.488  1.00 61.06           C
ANISOU 6474  CA  GLN B 289     8144   7175   7881   1830    -94    165       C
ATOM   6475  C   GLN B 289      65.241   5.501  24.735  1.00 62.62           C
ANISOU 6475  C   GLN B 289     8311   7309   8174   1981    -48    111       C
ATOM   6476  O   GLN B 289      66.465   5.620  24.649  1.00 61.94           O
ANISOU 6476  O   GLN B 289     8076   7305   8152   2073    -45     87       O
ATOM   6477  CB  GLN B 289      63.425   7.227  24.528  1.00 54.80           C
ANISOU 6477  CB  GLN B 289     7410   6391   7021   1693     -5    107       C
ATOM   6478  CG  GLN B 289      62.664   8.312  25.231  1.00 54.69           C
ANISOU 6478  CG  GLN B 289     7409   6445   6927   1554    -45    150       C
ATOM   6479  CD  GLN B 289      61.174   8.310  24.927  1.00 60.21           C
ANISOU 6479  CD  GLN B 289     8255   7069   7554   1442    -15    149       C
ATOM   6480  OE1 GLN B 289      60.515   7.278  25.026  1.00 64.66           O
ANISOU 6480  OE1 GLN B 289     8943   7509   8118   1464    -29    173       O
ATOM   6481  NE2 GLN B 289      60.628   9.478  24.630  1.00 53.94           N
ANISOU 6481  NE2 GLN B 289     7443   6348   6704   1320     19    128       N
ATOM   6482  N   CYS B 290      64.557   4.496  24.193  1.00 64.24           N
ANISOU 6482  N   CYS B 290     8654   7364   8390   2005    -11     86       N
ATOM   6483  CA  CYS B 290      65.187   3.374  23.521  1.00 63.68           C
ANISOU 6483  CA  CYS B 290     8584   7199   8412   2152     30     28       C
ATOM   6484  C   CYS B 290      65.809   3.815  22.201  1.00 61.37           C
ANISOU 6484  C   CYS B 290     8193   6995   8131   2167    146    -90       C
ATOM   6485  O   CYS B 290      65.476   4.865  21.649  1.00 56.77           O
ANISOU 6485  O   CYS B 290     7582   6512   7476   2047    204   -123       O
ATOM   6486  CB  CYS B 290      64.162   2.268  23.259  1.00 66.32           C
ANISOU 6486  CB  CYS B 290     9102   7344   8753   2148     41     20       C
ATOM   6487  SG  CYS B 290      63.714   1.240  24.693  1.00 83.92           S
ANISOU 6487  SG  CYS B 290    11449   9426  11012   2190    -83    164       S
ATOM   6488  N   GLU B 291      66.717   2.985  21.691  1.00 62.17           N
ANISOU 6488  N   GLU B 291     8242   7058   8324   2320    182   -151       N
ATOM   6489  CA  GLU B 291      67.348   3.196  20.398  1.00 61.81           C
ANISOU 6489  CA  GLU B 291     8106   7089   8289   2355    302   -268       C
ATOM   6490  C   GLU B 291      67.193   1.964  19.511  1.00 65.23           C
ANISOU 6490  C   GLU B 291     8637   7380   8769   2452    365   -364       C
ATOM   6491  O   GLU B 291      67.105   0.829  19.994  1.00 64.64           O
ANISOU 6491  O   GLU B 291     8646   7147   8767   2547    307   -337       O
ATOM   6492  CB  GLU B 291      68.829   3.537  20.550  1.00 62.34           C
ANISOU 6492  CB  GLU B 291     7969   7288   8428   2456    303   -273       C
ATOM   6493  CG  GLU B 291      69.088   5.029  20.625  1.00 65.50           C
ANISOU 6493  CG  GLU B 291     8243   7869   8774   2335    316   -251       C
ATOM   6494  CD  GLU B 291      70.565   5.378  20.520  1.00 70.19           C
ANISOU 6494  CD  GLU B 291     8622   8602   9444   2423    341   -277       C
ATOM   6495  OE1 GLU B 291      71.385   4.463  20.237  1.00 68.34           O
ANISOU 6495  OE1 GLU B 291     8334   8333   9299   2586    363   -325       O
ATOM   6496  OE2 GLU B 291      70.900   6.576  20.715  1.00 67.78           O
ANISOU 6496  OE2 GLU B 291     8199   8439   9116   2328    339   -253       O
ATOM   6497  N   VAL B 292      67.179   2.197  18.199  1.00 63.86           N
ANISOU 6497  N   VAL B 292     8450   7262   8551   2427    484   -478       N
ATOM   6498  CA  VAL B 292      66.970   1.145  17.215  1.00 61.92           C
ANISOU 6498  CA  VAL B 292     8297   6900   8331   2502    554   -595       C
ATOM   6499  C   VAL B 292      68.124   1.159  16.217  1.00 64.43           C
ANISOU 6499  C   VAL B 292     8474   7325   8681   2610    663   -706       C
ATOM   6500  O   VAL B 292      68.406   2.193  15.593  1.00 63.13           O
ANISOU 6500  O   VAL B 292     8209   7330   8447   2538    739   -730       O
ATOM   6501  CB  VAL B 292      65.622   1.315  16.490  1.00 64.86           C
ANISOU 6501  CB  VAL B 292     8815   7235   8594   2357    596   -640       C
ATOM   6502  CG1 VAL B 292      65.631   0.579  15.149  1.00 64.03           C
ANISOU 6502  CG1 VAL B 292     8757   7086   8486   2421    700   -798       C
ATOM   6503  CG2 VAL B 292      64.482   0.839  17.371  1.00 67.09           C
ANISOU 6503  CG2 VAL B 292     9254   7364   8873   2288    499   -556       C
ATOM   6504  N   LYS B 293      68.780   0.005  16.064  1.00 64.41           N
ANISOU 6504  N   LYS B 293     8464   7221   8788   2784    673   -773       N
ATOM   6505  CA  LYS B 293      69.808  -0.198  15.055  1.00 61.42           C
ANISOU 6505  CA  LYS B 293     7967   6924   8446   2905    786   -898       C
ATOM   6506  C   LYS B 293      69.140  -0.559  13.735  1.00 63.32           C
ANISOU 6506  C   LYS B 293     8318   7129   8612   2872    890  -1041       C
ATOM   6507  O   LYS B 293      68.241  -1.404  13.697  1.00 63.24           O
ANISOU 6507  O   LYS B 293     8476   6944   8609   2862    859  -1072       O
ATOM   6508  CB  LYS B 293      70.758  -1.314  15.493  1.00 65.73           C
ANISOU 6508  CB  LYS B 293     8461   7366   9149   3115    746   -913       C
ATOM   6509  CG  LYS B 293      71.935  -1.577  14.548  1.00 72.12           C
ANISOU 6509  CG  LYS B 293     9127   8264  10013   3263    861  -1045       C
ATOM   6510  CD  LYS B 293      72.842  -0.360  14.447  1.00 69.04           C
ANISOU 6510  CD  LYS B 293     8528   8115   9589   3224    911  -1017       C
ATOM   6511  CE  LYS B 293      74.288  -0.764  14.310  1.00 75.76           C
ANISOU 6511  CE  LYS B 293     9195   9030  10559   3414    952  -1074       C
ATOM   6512  NZ  LYS B 293      75.026  -0.499  15.581  1.00 85.48           N
ANISOU 6512  NZ  LYS B 293    10299  10304  11877   3461    833   -944       N
ATOM   6513  N   ILE B 294      69.567   0.077  12.653  1.00 63.64           N
ANISOU 6513  N   ILE B 294     8264   7339   8578   2852   1013  -1125       N
ATOM   6514  CA  ILE B 294      69.022  -0.235  11.336  1.00 67.19           C
ANISOU 6514  CA  ILE B 294     8805   7784   8939   2829   1116  -1269       C
ATOM   6515  C   ILE B 294      69.936  -1.264  10.684  1.00 68.33           C
ANISOU 6515  C   ILE B 294     8899   7892   9174   3022   1193  -1415       C
ATOM   6516  O   ILE B 294      71.083  -0.958  10.351  1.00 69.74           O
ANISOU 6516  O   ILE B 294     8905   8216   9378   3107   1268  -1448       O
ATOM   6517  CB  ILE B 294      68.881   1.020  10.470  1.00 63.91           C
ANISOU 6517  CB  ILE B 294     8331   7577   8376   2693   1211  -1273       C
ATOM   6518  CG1 ILE B 294      67.984   2.034  11.176  1.00 63.85           C
ANISOU 6518  CG1 ILE B 294     8371   7592   8297   2512   1130  -1131       C
ATOM   6519  CG2 ILE B 294      68.316   0.657   9.101  1.00 64.96           C
ANISOU 6519  CG2 ILE B 294     8561   7718   8404   2675   1312  -1423       C
ATOM   6520  CD1 ILE B 294      66.739   1.426  11.804  1.00 63.79           C
ANISOU 6520  CD1 ILE B 294     8550   7394   8295   2453   1026  -1092       C
ATOM   6521  N   ASP B 295      69.427  -2.492  10.514  1.00 70.78           N
ANISOU 6521  N   ASP B 295     9355   8001   9538   3092   1173  -1505       N
ATOM   6522  CA  ASP B 295      70.207  -3.595   9.960  1.00 63.39           C
ANISOU 6522  CA  ASP B 295     8391   6992   8704   3287   1235  -1655       C
ATOM   6523  C   ASP B 29